data_9DJT
# 
_entry.id   9DJT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DJT         pdb_00009djt 10.2210/pdb9djt/pdb 
WWPDB D_1000288232 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-27 
2 'Structure model' 1 1 2024-12-11 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DJT 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          8TZX 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              james.partridge@novartis.com 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_last          Partridge 
_pdbx_contact_author.name_mi            R 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5652-4351 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Partridge, J.R.' 1 0000-0002-5652-4351 
'Ma, X.'          2 ?                   
'Ornelas, E.'     3 ?                   
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? US ? ? primary J.Med.Chem.                                      JMCMAR 0151 0022-2623 ? ? 67 ? 20682 20694 
;Discovery and Optimization of First-in-Class Molecular Glue Degraders of the WIZ Transcription Factor for Fetal Hemoglobin Induction to Treat Sickle Cell Disease.
;
2024 ? 10.1021/acs.jmedchem.4c02251 39541509 ? ? 
? ? ? ? ? ? ? DK ? ? 1       'Acta Crystallogr., Sect. D: Biol. Crystallogr.' ABCRE6 0766 0907-4449 ? ? 75 ? 861   877   
'Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix' 2019 ? 
10.1107/S2059798319011471    31588918 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kerrigan, J.R.'    1  ?                   
primary 'Thomsen, N.M.'     2  ?                   
primary 'Cernijenko, A.'    3  ?                   
primary 'Kochanek, S.E.'    4  ?                   
primary 'Dewhurst, J.'      5  ?                   
primary 
;O'Brien, G.
;
6  ?                   
primary 'Ware, N.F.'        7  ?                   
primary 'Sanchez, C.C.'     8  ?                   
primary 'Manning, J.R.'     9  ?                   
primary 'Ma, X.'            10 ?                   
primary 'Ornelas, E.'       11 ?                   
primary 'Savage, N.A.'      12 ?                   
primary 'Partridge, J.R.'   13 ?                   
primary 'Patterson, A.W.'   14 ?                   
primary 'Lam, P.'           15 ?                   
primary 'Dales, N.A.'       16 ?                   
primary 'Bonazzi, S.'       17 ?                   
primary 'Borikar, S.'       18 ?                   
primary 'Hinman, A.E.'      19 ?                   
primary 'Ting, P.Y.'        20 ?                   
1       'Liebschner, D.'    21 0000-0003-3921-3209 
1       'Afonine, P.V.'     22 0000-0002-5052-991X 
1       'Baker, M.L.'       23 ?                   
1       'Bunkoczi, G.'      24 ?                   
1       'Chen, V.B.'        25 0000-0003-2492-979X 
1       'Croll, T.I.'       26 ?                   
1       'Hintze, B.'        27 0000-0002-4871-2096 
1       'Hung, L.W.'        28 0000-0001-6690-8458 
1       'Jain, S.'          29 ?                   
1       'McCoy, A.J.'       30 ?                   
1       'Moriarty, N.W.'    31 0000-0001-8857-9464 
1       'Oeffner, R.D.'     32 0000-0003-3107-2202 
1       'Poon, B.K.'        33 0000-0001-9633-6067 
1       'Prisant, M.G.'     34 ?                   
1       'Read, R.J.'        35 0000-0001-8273-0047 
1       'Richardson, J.S.'  36 0000-0002-3311-2944 
1       'Richardson, D.C.'  37 ?                   
1       'Sammito, M.D.'     38 0000-0002-8346-9247 
1       'Sobolev, O.V.'     39 0000-0002-0623-3214 
1       'Stockwell, D.H.'   40 ?                   
1       'Terwilliger, T.C.' 41 0000-0001-6384-0320 
1       'Urzhumtsev, A.G.'  42 ?                   
1       'Videau, L.L.'      43 ?                   
1       'Williams, C.J.'    44 ?                   
1       'Adams, P.D.'       45 0000-0001-9333-8219 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protein cereblon' 42971.574 2  ? ? ? ? 
2 polymer     man 'DNA damage-binding protein 1' 93347.078 2  ? ? ? ? 
3 polymer     man 'Protein Wiz' 3299.722  2  ? ? ? ? 
4 non-polymer syn 'ZINC ION' 65.409    4  ? ? ? ? 
5 non-polymer syn 'SULFATE ION' 96.063    2  ? ? ? ? 
6 non-polymer syn 
'(3S)-3-(5-{[(4R)-6-ethyl-6-azaspiro[2.5]octan-4-yl]oxy}-1-oxo-1,3-dihydro-2H-isoindol-2-yl)piperidine-2,6-dione' 397.467   2  ? ? 
? ? 
7 water       nat water 18.015    42 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
2 
;DDB p127 subunit,DNA damage-binding protein a,DDBa,Damage-specific DNA-binding protein 1,HBV X-associated protein 1,XAP-1,UV-damaged DNA-binding factor,UV-damaged DNA-binding protein 1,UV-DDB 1,XPE-binding factor,XPE-BF,Xeroderma pigmentosum group E-complementing protein,XPCe
;
3 'Widely-interspaced zinc finger-containing protein,Zinc finger protein 803' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;RTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQD
FGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQK
RKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLR
CELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVA
QCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPDKVILCL
;
;RTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQD
FGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQK
RKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLR
CELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVA
QCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPDKVILCL
;
A,D ? 
2 'polypeptide(L)' no no 
;MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFIL
TAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLE
ELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH
NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNG
VVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIGGNGNS
GEIQKLHIRTVPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAPHETSFGE
EVEVHNLLIIDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGKLQTVAEK
EVKGAVYSMVEFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYKPMEGNFEE
IARDFNPNWMSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNLGETSTPT
QGSVLFGTVNGMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESFLDISRPK
MQEVVANLQYDDGSGMKREATADDLIKVVEELTRIH
;
;MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFIL
TAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLE
ELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH
NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNG
VVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIGGNGNS
GEIQKLHIRTVPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAPHETSFGE
EVEVHNLLIIDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGKLQTVAEK
EVKGAVYSMVEFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYKPMEGNFEE
IARDFNPNWMSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNLGETSTPT
QGSVLFGTVNGMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESFLDISRPK
MQEVVANLQYDDGSGMKREATADDLIKVVEELTRIH
;
B,E ? 
3 'polypeptide(L)' no no SQSLTTCEVCGACFETRKGLSSHARSHLRQ SQSLTTCEVCGACFETRKGLSSHARSHLRQ C,F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'ZINC ION'                                                                                                        ZN    
5 'SULFATE ION'                                                                                                     SO4   
6 '(3S)-3-(5-{[(4R)-6-ethyl-6-azaspiro[2.5]octan-4-yl]oxy}-1-oxo-1,3-dihydro-2H-isoindol-2-yl)piperidine-2,6-dione' A1A5H 
7 water                                                                                                             HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ARG n 
1 2   THR n 
1 3   LEU n 
1 4   HIS n 
1 5   ASP n 
1 6   ASP n 
1 7   ASP n 
1 8   SER n 
1 9   CYS n 
1 10  GLN n 
1 11  VAL n 
1 12  ILE n 
1 13  PRO n 
1 14  VAL n 
1 15  LEU n 
1 16  PRO n 
1 17  GLN n 
1 18  VAL n 
1 19  MET n 
1 20  MET n 
1 21  ILE n 
1 22  LEU n 
1 23  ILE n 
1 24  PRO n 
1 25  GLY n 
1 26  GLN n 
1 27  THR n 
1 28  LEU n 
1 29  PRO n 
1 30  LEU n 
1 31  GLN n 
1 32  LEU n 
1 33  PHE n 
1 34  HIS n 
1 35  PRO n 
1 36  GLN n 
1 37  GLU n 
1 38  VAL n 
1 39  SER n 
1 40  MET n 
1 41  VAL n 
1 42  ARG n 
1 43  ASN n 
1 44  LEU n 
1 45  ILE n 
1 46  GLN n 
1 47  LYS n 
1 48  ASP n 
1 49  ARG n 
1 50  THR n 
1 51  PHE n 
1 52  ALA n 
1 53  VAL n 
1 54  LEU n 
1 55  ALA n 
1 56  TYR n 
1 57  SER n 
1 58  ASN n 
1 59  VAL n 
1 60  GLN n 
1 61  GLU n 
1 62  ARG n 
1 63  GLU n 
1 64  ALA n 
1 65  GLN n 
1 66  PHE n 
1 67  GLY n 
1 68  THR n 
1 69  THR n 
1 70  ALA n 
1 71  GLU n 
1 72  ILE n 
1 73  TYR n 
1 74  ALA n 
1 75  TYR n 
1 76  ARG n 
1 77  GLU n 
1 78  GLU n 
1 79  GLN n 
1 80  ASP n 
1 81  PHE n 
1 82  GLY n 
1 83  ILE n 
1 84  GLU n 
1 85  ILE n 
1 86  VAL n 
1 87  LYS n 
1 88  VAL n 
1 89  LYS n 
1 90  ALA n 
1 91  ILE n 
1 92  GLY n 
1 93  ARG n 
1 94  GLN n 
1 95  ARG n 
1 96  PHE n 
1 97  LYS n 
1 98  VAL n 
1 99  LEU n 
1 100 GLU n 
1 101 LEU n 
1 102 ARG n 
1 103 THR n 
1 104 GLN n 
1 105 SER n 
1 106 ASP n 
1 107 GLY n 
1 108 ILE n 
1 109 GLN n 
1 110 GLN n 
1 111 ALA n 
1 112 LYS n 
1 113 VAL n 
1 114 GLN n 
1 115 ILE n 
1 116 LEU n 
1 117 PRO n 
1 118 GLU n 
1 119 CYS n 
1 120 VAL n 
1 121 LEU n 
1 122 PRO n 
1 123 SER n 
1 124 THR n 
1 125 MET n 
1 126 SER n 
1 127 ALA n 
1 128 VAL n 
1 129 GLN n 
1 130 LEU n 
1 131 GLU n 
1 132 SER n 
1 133 LEU n 
1 134 ASN n 
1 135 LYS n 
1 136 CYS n 
1 137 GLN n 
1 138 ILE n 
1 139 PHE n 
1 140 PRO n 
1 141 SER n 
1 142 LYS n 
1 143 PRO n 
1 144 VAL n 
1 145 SER n 
1 146 ARG n 
1 147 GLU n 
1 148 ASP n 
1 149 GLN n 
1 150 CYS n 
1 151 SER n 
1 152 TYR n 
1 153 LYS n 
1 154 TRP n 
1 155 TRP n 
1 156 GLN n 
1 157 LYS n 
1 158 TYR n 
1 159 GLN n 
1 160 LYS n 
1 161 ARG n 
1 162 LYS n 
1 163 PHE n 
1 164 HIS n 
1 165 CYS n 
1 166 ALA n 
1 167 ASN n 
1 168 LEU n 
1 169 THR n 
1 170 SER n 
1 171 TRP n 
1 172 PRO n 
1 173 ARG n 
1 174 TRP n 
1 175 LEU n 
1 176 TYR n 
1 177 SER n 
1 178 LEU n 
1 179 TYR n 
1 180 ASP n 
1 181 ALA n 
1 182 GLU n 
1 183 THR n 
1 184 LEU n 
1 185 MET n 
1 186 ASP n 
1 187 ARG n 
1 188 ILE n 
1 189 LYS n 
1 190 LYS n 
1 191 GLN n 
1 192 LEU n 
1 193 ARG n 
1 194 GLU n 
1 195 TRP n 
1 196 ASP n 
1 197 GLU n 
1 198 ASN n 
1 199 LEU n 
1 200 LYS n 
1 201 ASP n 
1 202 ASP n 
1 203 SER n 
1 204 LEU n 
1 205 PRO n 
1 206 SER n 
1 207 ASN n 
1 208 PRO n 
1 209 ILE n 
1 210 ASP n 
1 211 PHE n 
1 212 SER n 
1 213 TYR n 
1 214 ARG n 
1 215 VAL n 
1 216 ALA n 
1 217 ALA n 
1 218 CYS n 
1 219 LEU n 
1 220 PRO n 
1 221 ILE n 
1 222 ASP n 
1 223 ASP n 
1 224 VAL n 
1 225 LEU n 
1 226 ARG n 
1 227 ILE n 
1 228 GLN n 
1 229 LEU n 
1 230 LEU n 
1 231 LYS n 
1 232 ILE n 
1 233 GLY n 
1 234 SER n 
1 235 ALA n 
1 236 ILE n 
1 237 GLN n 
1 238 ARG n 
1 239 LEU n 
1 240 ARG n 
1 241 CYS n 
1 242 GLU n 
1 243 LEU n 
1 244 ASP n 
1 245 ILE n 
1 246 MET n 
1 247 ASN n 
1 248 LYS n 
1 249 CYS n 
1 250 THR n 
1 251 SER n 
1 252 LEU n 
1 253 CYS n 
1 254 CYS n 
1 255 LYS n 
1 256 GLN n 
1 257 CYS n 
1 258 GLN n 
1 259 GLU n 
1 260 THR n 
1 261 GLU n 
1 262 ILE n 
1 263 THR n 
1 264 THR n 
1 265 LYS n 
1 266 ASN n 
1 267 GLU n 
1 268 ILE n 
1 269 PHE n 
1 270 SER n 
1 271 LEU n 
1 272 SER n 
1 273 LEU n 
1 274 CYS n 
1 275 GLY n 
1 276 PRO n 
1 277 MET n 
1 278 ALA n 
1 279 ALA n 
1 280 TYR n 
1 281 VAL n 
1 282 ASN n 
1 283 PRO n 
1 284 HIS n 
1 285 GLY n 
1 286 TYR n 
1 287 VAL n 
1 288 HIS n 
1 289 GLU n 
1 290 THR n 
1 291 LEU n 
1 292 THR n 
1 293 VAL n 
1 294 TYR n 
1 295 LYS n 
1 296 ALA n 
1 297 CYS n 
1 298 ASN n 
1 299 LEU n 
1 300 ASN n 
1 301 LEU n 
1 302 ILE n 
1 303 GLY n 
1 304 ARG n 
1 305 PRO n 
1 306 SER n 
1 307 THR n 
1 308 GLU n 
1 309 HIS n 
1 310 SER n 
1 311 TRP n 
1 312 PHE n 
1 313 PRO n 
1 314 GLY n 
1 315 TYR n 
1 316 ALA n 
1 317 TRP n 
1 318 THR n 
1 319 VAL n 
1 320 ALA n 
1 321 GLN n 
1 322 CYS n 
1 323 LYS n 
1 324 ILE n 
1 325 CYS n 
1 326 ALA n 
1 327 SER n 
1 328 HIS n 
1 329 ILE n 
1 330 GLY n 
1 331 TRP n 
1 332 LYS n 
1 333 PHE n 
1 334 THR n 
1 335 ALA n 
1 336 THR n 
1 337 LYS n 
1 338 LYS n 
1 339 ASP n 
1 340 MET n 
1 341 SER n 
1 342 PRO n 
1 343 GLN n 
1 344 LYS n 
1 345 PHE n 
1 346 TRP n 
1 347 GLY n 
1 348 LEU n 
1 349 THR n 
1 350 ARG n 
1 351 SER n 
1 352 ALA n 
1 353 LEU n 
1 354 LEU n 
1 355 PRO n 
1 356 THR n 
1 357 ILE n 
1 358 PRO n 
1 359 ASP n 
1 360 THR n 
1 361 GLU n 
1 362 ASP n 
1 363 GLU n 
1 364 ILE n 
1 365 SER n 
1 366 PRO n 
1 367 ASP n 
1 368 LYS n 
1 369 VAL n 
1 370 ILE n 
1 371 LEU n 
1 372 CYS n 
1 373 LEU n 
2 1   MET n 
2 2   SER n 
2 3   TYR n 
2 4   ASN n 
2 5   TYR n 
2 6   VAL n 
2 7   VAL n 
2 8   THR n 
2 9   ALA n 
2 10  GLN n 
2 11  LYS n 
2 12  PRO n 
2 13  THR n 
2 14  ALA n 
2 15  VAL n 
2 16  ASN n 
2 17  GLY n 
2 18  CYS n 
2 19  VAL n 
2 20  THR n 
2 21  GLY n 
2 22  HIS n 
2 23  PHE n 
2 24  THR n 
2 25  SER n 
2 26  ALA n 
2 27  GLU n 
2 28  ASP n 
2 29  LEU n 
2 30  ASN n 
2 31  LEU n 
2 32  LEU n 
2 33  ILE n 
2 34  ALA n 
2 35  LYS n 
2 36  ASN n 
2 37  THR n 
2 38  ARG n 
2 39  LEU n 
2 40  GLU n 
2 41  ILE n 
2 42  TYR n 
2 43  VAL n 
2 44  VAL n 
2 45  THR n 
2 46  ALA n 
2 47  GLU n 
2 48  GLY n 
2 49  LEU n 
2 50  ARG n 
2 51  PRO n 
2 52  VAL n 
2 53  LYS n 
2 54  GLU n 
2 55  VAL n 
2 56  GLY n 
2 57  MET n 
2 58  TYR n 
2 59  GLY n 
2 60  LYS n 
2 61  ILE n 
2 62  ALA n 
2 63  VAL n 
2 64  MET n 
2 65  GLU n 
2 66  LEU n 
2 67  PHE n 
2 68  ARG n 
2 69  PRO n 
2 70  LYS n 
2 71  GLY n 
2 72  GLU n 
2 73  SER n 
2 74  LYS n 
2 75  ASP n 
2 76  LEU n 
2 77  LEU n 
2 78  PHE n 
2 79  ILE n 
2 80  LEU n 
2 81  THR n 
2 82  ALA n 
2 83  LYS n 
2 84  TYR n 
2 85  ASN n 
2 86  ALA n 
2 87  CYS n 
2 88  ILE n 
2 89  LEU n 
2 90  GLU n 
2 91  TYR n 
2 92  LYS n 
2 93  GLN n 
2 94  SER n 
2 95  GLY n 
2 96  GLU n 
2 97  SER n 
2 98  ILE n 
2 99  ASP n 
2 100 ILE n 
2 101 ILE n 
2 102 THR n 
2 103 ARG n 
2 104 ALA n 
2 105 HIS n 
2 106 GLY n 
2 107 ASN n 
2 108 VAL n 
2 109 GLN n 
2 110 ASP n 
2 111 ARG n 
2 112 ILE n 
2 113 GLY n 
2 114 ARG n 
2 115 PRO n 
2 116 SER n 
2 117 GLU n 
2 118 THR n 
2 119 GLY n 
2 120 ILE n 
2 121 ILE n 
2 122 GLY n 
2 123 ILE n 
2 124 ILE n 
2 125 ASP n 
2 126 PRO n 
2 127 GLU n 
2 128 CYS n 
2 129 ARG n 
2 130 MET n 
2 131 ILE n 
2 132 GLY n 
2 133 LEU n 
2 134 ARG n 
2 135 LEU n 
2 136 TYR n 
2 137 ASP n 
2 138 GLY n 
2 139 LEU n 
2 140 PHE n 
2 141 LYS n 
2 142 VAL n 
2 143 ILE n 
2 144 PRO n 
2 145 LEU n 
2 146 ASP n 
2 147 ARG n 
2 148 ASP n 
2 149 ASN n 
2 150 LYS n 
2 151 GLU n 
2 152 LEU n 
2 153 LYS n 
2 154 ALA n 
2 155 PHE n 
2 156 ASN n 
2 157 ILE n 
2 158 ARG n 
2 159 LEU n 
2 160 GLU n 
2 161 GLU n 
2 162 LEU n 
2 163 HIS n 
2 164 VAL n 
2 165 ILE n 
2 166 ASP n 
2 167 VAL n 
2 168 LYS n 
2 169 PHE n 
2 170 LEU n 
2 171 TYR n 
2 172 GLY n 
2 173 CYS n 
2 174 GLN n 
2 175 ALA n 
2 176 PRO n 
2 177 THR n 
2 178 ILE n 
2 179 CYS n 
2 180 PHE n 
2 181 VAL n 
2 182 TYR n 
2 183 GLN n 
2 184 ASP n 
2 185 PRO n 
2 186 GLN n 
2 187 GLY n 
2 188 ARG n 
2 189 HIS n 
2 190 VAL n 
2 191 LYS n 
2 192 THR n 
2 193 TYR n 
2 194 GLU n 
2 195 VAL n 
2 196 SER n 
2 197 LEU n 
2 198 ARG n 
2 199 GLU n 
2 200 LYS n 
2 201 GLU n 
2 202 PHE n 
2 203 ASN n 
2 204 LYS n 
2 205 GLY n 
2 206 PRO n 
2 207 TRP n 
2 208 LYS n 
2 209 GLN n 
2 210 GLU n 
2 211 ASN n 
2 212 VAL n 
2 213 GLU n 
2 214 ALA n 
2 215 GLU n 
2 216 ALA n 
2 217 SER n 
2 218 MET n 
2 219 VAL n 
2 220 ILE n 
2 221 ALA n 
2 222 VAL n 
2 223 PRO n 
2 224 GLU n 
2 225 PRO n 
2 226 PHE n 
2 227 GLY n 
2 228 GLY n 
2 229 ALA n 
2 230 ILE n 
2 231 ILE n 
2 232 ILE n 
2 233 GLY n 
2 234 GLN n 
2 235 GLU n 
2 236 SER n 
2 237 ILE n 
2 238 THR n 
2 239 TYR n 
2 240 HIS n 
2 241 ASN n 
2 242 GLY n 
2 243 ASP n 
2 244 LYS n 
2 245 TYR n 
2 246 LEU n 
2 247 ALA n 
2 248 ILE n 
2 249 ALA n 
2 250 PRO n 
2 251 PRO n 
2 252 ILE n 
2 253 ILE n 
2 254 LYS n 
2 255 GLN n 
2 256 SER n 
2 257 THR n 
2 258 ILE n 
2 259 VAL n 
2 260 CYS n 
2 261 HIS n 
2 262 ASN n 
2 263 ARG n 
2 264 VAL n 
2 265 ASP n 
2 266 PRO n 
2 267 ASN n 
2 268 GLY n 
2 269 SER n 
2 270 ARG n 
2 271 TYR n 
2 272 LEU n 
2 273 LEU n 
2 274 GLY n 
2 275 ASP n 
2 276 MET n 
2 277 GLU n 
2 278 GLY n 
2 279 ARG n 
2 280 LEU n 
2 281 PHE n 
2 282 MET n 
2 283 LEU n 
2 284 LEU n 
2 285 LEU n 
2 286 GLU n 
2 287 LYS n 
2 288 GLU n 
2 289 GLU n 
2 290 GLN n 
2 291 MET n 
2 292 ASP n 
2 293 GLY n 
2 294 THR n 
2 295 VAL n 
2 296 THR n 
2 297 LEU n 
2 298 LYS n 
2 299 ASP n 
2 300 LEU n 
2 301 ARG n 
2 302 VAL n 
2 303 GLU n 
2 304 LEU n 
2 305 LEU n 
2 306 GLY n 
2 307 GLU n 
2 308 THR n 
2 309 SER n 
2 310 ILE n 
2 311 ALA n 
2 312 GLU n 
2 313 CYS n 
2 314 LEU n 
2 315 THR n 
2 316 TYR n 
2 317 LEU n 
2 318 ASP n 
2 319 ASN n 
2 320 GLY n 
2 321 VAL n 
2 322 VAL n 
2 323 PHE n 
2 324 VAL n 
2 325 GLY n 
2 326 SER n 
2 327 ARG n 
2 328 LEU n 
2 329 GLY n 
2 330 ASP n 
2 331 SER n 
2 332 GLN n 
2 333 LEU n 
2 334 VAL n 
2 335 LYS n 
2 336 LEU n 
2 337 ASN n 
2 338 VAL n 
2 339 ASP n 
2 340 SER n 
2 341 ASN n 
2 342 GLU n 
2 343 GLN n 
2 344 GLY n 
2 345 SER n 
2 346 TYR n 
2 347 VAL n 
2 348 VAL n 
2 349 ALA n 
2 350 MET n 
2 351 GLU n 
2 352 THR n 
2 353 PHE n 
2 354 THR n 
2 355 ASN n 
2 356 LEU n 
2 357 GLY n 
2 358 PRO n 
2 359 ILE n 
2 360 VAL n 
2 361 ASP n 
2 362 MET n 
2 363 CYS n 
2 364 VAL n 
2 365 VAL n 
2 366 ASP n 
2 367 LEU n 
2 368 GLU n 
2 369 ARG n 
2 370 GLN n 
2 371 GLY n 
2 372 GLN n 
2 373 GLY n 
2 374 GLN n 
2 375 LEU n 
2 376 VAL n 
2 377 THR n 
2 378 CYS n 
2 379 SER n 
2 380 GLY n 
2 381 ALA n 
2 382 PHE n 
2 383 LYS n 
2 384 GLU n 
2 385 GLY n 
2 386 SER n 
2 387 LEU n 
2 388 ARG n 
2 389 ILE n 
2 390 ILE n 
2 391 ARG n 
2 392 ASN n 
2 393 GLY n 
2 394 ILE n 
2 395 GLY n 
2 396 GLY n 
2 397 ASN n 
2 398 GLY n 
2 399 ASN n 
2 400 SER n 
2 401 GLY n 
2 402 GLU n 
2 403 ILE n 
2 404 GLN n 
2 405 LYS n 
2 406 LEU n 
2 407 HIS n 
2 408 ILE n 
2 409 ARG n 
2 410 THR n 
2 411 VAL n 
2 412 PRO n 
2 413 LEU n 
2 414 TYR n 
2 415 GLU n 
2 416 SER n 
2 417 PRO n 
2 418 ARG n 
2 419 LYS n 
2 420 ILE n 
2 421 CYS n 
2 422 TYR n 
2 423 GLN n 
2 424 GLU n 
2 425 VAL n 
2 426 SER n 
2 427 GLN n 
2 428 CYS n 
2 429 PHE n 
2 430 GLY n 
2 431 VAL n 
2 432 LEU n 
2 433 SER n 
2 434 SER n 
2 435 ARG n 
2 436 ILE n 
2 437 GLU n 
2 438 VAL n 
2 439 GLN n 
2 440 ASP n 
2 441 THR n 
2 442 SER n 
2 443 GLY n 
2 444 GLY n 
2 445 THR n 
2 446 THR n 
2 447 ALA n 
2 448 LEU n 
2 449 ARG n 
2 450 PRO n 
2 451 SER n 
2 452 ALA n 
2 453 SER n 
2 454 THR n 
2 455 GLN n 
2 456 ALA n 
2 457 LEU n 
2 458 SER n 
2 459 SER n 
2 460 SER n 
2 461 VAL n 
2 462 SER n 
2 463 SER n 
2 464 SER n 
2 465 LYS n 
2 466 LEU n 
2 467 PHE n 
2 468 SER n 
2 469 SER n 
2 470 SER n 
2 471 THR n 
2 472 ALA n 
2 473 PRO n 
2 474 HIS n 
2 475 GLU n 
2 476 THR n 
2 477 SER n 
2 478 PHE n 
2 479 GLY n 
2 480 GLU n 
2 481 GLU n 
2 482 VAL n 
2 483 GLU n 
2 484 VAL n 
2 485 HIS n 
2 486 ASN n 
2 487 LEU n 
2 488 LEU n 
2 489 ILE n 
2 490 ILE n 
2 491 ASP n 
2 492 GLN n 
2 493 HIS n 
2 494 THR n 
2 495 PHE n 
2 496 GLU n 
2 497 VAL n 
2 498 LEU n 
2 499 HIS n 
2 500 ALA n 
2 501 HIS n 
2 502 GLN n 
2 503 PHE n 
2 504 LEU n 
2 505 GLN n 
2 506 ASN n 
2 507 GLU n 
2 508 TYR n 
2 509 ALA n 
2 510 LEU n 
2 511 SER n 
2 512 LEU n 
2 513 VAL n 
2 514 SER n 
2 515 CYS n 
2 516 LYS n 
2 517 LEU n 
2 518 GLY n 
2 519 LYS n 
2 520 ASP n 
2 521 PRO n 
2 522 ASN n 
2 523 THR n 
2 524 TYR n 
2 525 PHE n 
2 526 ILE n 
2 527 VAL n 
2 528 GLY n 
2 529 THR n 
2 530 ALA n 
2 531 MET n 
2 532 VAL n 
2 533 TYR n 
2 534 PRO n 
2 535 GLU n 
2 536 GLU n 
2 537 ALA n 
2 538 GLU n 
2 539 PRO n 
2 540 LYS n 
2 541 GLN n 
2 542 GLY n 
2 543 ARG n 
2 544 ILE n 
2 545 VAL n 
2 546 VAL n 
2 547 PHE n 
2 548 GLN n 
2 549 TYR n 
2 550 SER n 
2 551 ASP n 
2 552 GLY n 
2 553 LYS n 
2 554 LEU n 
2 555 GLN n 
2 556 THR n 
2 557 VAL n 
2 558 ALA n 
2 559 GLU n 
2 560 LYS n 
2 561 GLU n 
2 562 VAL n 
2 563 LYS n 
2 564 GLY n 
2 565 ALA n 
2 566 VAL n 
2 567 TYR n 
2 568 SER n 
2 569 MET n 
2 570 VAL n 
2 571 GLU n 
2 572 PHE n 
2 573 ASN n 
2 574 GLY n 
2 575 LYS n 
2 576 LEU n 
2 577 LEU n 
2 578 ALA n 
2 579 SER n 
2 580 ILE n 
2 581 ASN n 
2 582 SER n 
2 583 THR n 
2 584 VAL n 
2 585 ARG n 
2 586 LEU n 
2 587 TYR n 
2 588 GLU n 
2 589 TRP n 
2 590 THR n 
2 591 THR n 
2 592 GLU n 
2 593 LYS n 
2 594 GLU n 
2 595 LEU n 
2 596 ARG n 
2 597 THR n 
2 598 GLU n 
2 599 CYS n 
2 600 ASN n 
2 601 HIS n 
2 602 TYR n 
2 603 ASN n 
2 604 ASN n 
2 605 ILE n 
2 606 MET n 
2 607 ALA n 
2 608 LEU n 
2 609 TYR n 
2 610 LEU n 
2 611 LYS n 
2 612 THR n 
2 613 LYS n 
2 614 GLY n 
2 615 ASP n 
2 616 PHE n 
2 617 ILE n 
2 618 LEU n 
2 619 VAL n 
2 620 GLY n 
2 621 ASP n 
2 622 LEU n 
2 623 MET n 
2 624 ARG n 
2 625 SER n 
2 626 VAL n 
2 627 LEU n 
2 628 LEU n 
2 629 LEU n 
2 630 ALA n 
2 631 TYR n 
2 632 LYS n 
2 633 PRO n 
2 634 MET n 
2 635 GLU n 
2 636 GLY n 
2 637 ASN n 
2 638 PHE n 
2 639 GLU n 
2 640 GLU n 
2 641 ILE n 
2 642 ALA n 
2 643 ARG n 
2 644 ASP n 
2 645 PHE n 
2 646 ASN n 
2 647 PRO n 
2 648 ASN n 
2 649 TRP n 
2 650 MET n 
2 651 SER n 
2 652 ALA n 
2 653 VAL n 
2 654 GLU n 
2 655 ILE n 
2 656 LEU n 
2 657 ASP n 
2 658 ASP n 
2 659 ASP n 
2 660 ASN n 
2 661 PHE n 
2 662 LEU n 
2 663 GLY n 
2 664 ALA n 
2 665 GLU n 
2 666 ASN n 
2 667 ALA n 
2 668 PHE n 
2 669 ASN n 
2 670 LEU n 
2 671 PHE n 
2 672 VAL n 
2 673 CYS n 
2 674 GLN n 
2 675 LYS n 
2 676 ASP n 
2 677 SER n 
2 678 ALA n 
2 679 ALA n 
2 680 THR n 
2 681 THR n 
2 682 ASP n 
2 683 GLU n 
2 684 GLU n 
2 685 ARG n 
2 686 GLN n 
2 687 HIS n 
2 688 LEU n 
2 689 GLN n 
2 690 GLU n 
2 691 VAL n 
2 692 GLY n 
2 693 LEU n 
2 694 PHE n 
2 695 HIS n 
2 696 LEU n 
2 697 GLY n 
2 698 GLU n 
2 699 PHE n 
2 700 VAL n 
2 701 ASN n 
2 702 VAL n 
2 703 PHE n 
2 704 CYS n 
2 705 HIS n 
2 706 GLY n 
2 707 SER n 
2 708 LEU n 
2 709 VAL n 
2 710 MET n 
2 711 GLN n 
2 712 ASN n 
2 713 LEU n 
2 714 GLY n 
2 715 GLU n 
2 716 THR n 
2 717 SER n 
2 718 THR n 
2 719 PRO n 
2 720 THR n 
2 721 GLN n 
2 722 GLY n 
2 723 SER n 
2 724 VAL n 
2 725 LEU n 
2 726 PHE n 
2 727 GLY n 
2 728 THR n 
2 729 VAL n 
2 730 ASN n 
2 731 GLY n 
2 732 MET n 
2 733 ILE n 
2 734 GLY n 
2 735 LEU n 
2 736 VAL n 
2 737 THR n 
2 738 SER n 
2 739 LEU n 
2 740 SER n 
2 741 GLU n 
2 742 SER n 
2 743 TRP n 
2 744 TYR n 
2 745 ASN n 
2 746 LEU n 
2 747 LEU n 
2 748 LEU n 
2 749 ASP n 
2 750 MET n 
2 751 GLN n 
2 752 ASN n 
2 753 ARG n 
2 754 LEU n 
2 755 ASN n 
2 756 LYS n 
2 757 VAL n 
2 758 ILE n 
2 759 LYS n 
2 760 SER n 
2 761 VAL n 
2 762 GLY n 
2 763 LYS n 
2 764 ILE n 
2 765 GLU n 
2 766 HIS n 
2 767 SER n 
2 768 PHE n 
2 769 TRP n 
2 770 ARG n 
2 771 SER n 
2 772 PHE n 
2 773 HIS n 
2 774 THR n 
2 775 GLU n 
2 776 ARG n 
2 777 LYS n 
2 778 THR n 
2 779 GLU n 
2 780 PRO n 
2 781 ALA n 
2 782 THR n 
2 783 GLY n 
2 784 PHE n 
2 785 ILE n 
2 786 ASP n 
2 787 GLY n 
2 788 ASP n 
2 789 LEU n 
2 790 ILE n 
2 791 GLU n 
2 792 SER n 
2 793 PHE n 
2 794 LEU n 
2 795 ASP n 
2 796 ILE n 
2 797 SER n 
2 798 ARG n 
2 799 PRO n 
2 800 LYS n 
2 801 MET n 
2 802 GLN n 
2 803 GLU n 
2 804 VAL n 
2 805 VAL n 
2 806 ALA n 
2 807 ASN n 
2 808 LEU n 
2 809 GLN n 
2 810 TYR n 
2 811 ASP n 
2 812 ASP n 
2 813 GLY n 
2 814 SER n 
2 815 GLY n 
2 816 MET n 
2 817 LYS n 
2 818 ARG n 
2 819 GLU n 
2 820 ALA n 
2 821 THR n 
2 822 ALA n 
2 823 ASP n 
2 824 ASP n 
2 825 LEU n 
2 826 ILE n 
2 827 LYS n 
2 828 VAL n 
2 829 VAL n 
2 830 GLU n 
2 831 GLU n 
2 832 LEU n 
2 833 THR n 
2 834 ARG n 
2 835 ILE n 
2 836 HIS n 
3 1   SER n 
3 2   GLN n 
3 3   SER n 
3 4   LEU n 
3 5   THR n 
3 6   THR n 
3 7   CYS n 
3 8   GLU n 
3 9   VAL n 
3 10  CYS n 
3 11  GLY n 
3 12  ALA n 
3 13  CYS n 
3 14  PHE n 
3 15  GLU n 
3 16  THR n 
3 17  ARG n 
3 18  LYS n 
3 19  GLY n 
3 20  LEU n 
3 21  SER n 
3 22  SER n 
3 23  HIS n 
3 24  ALA n 
3 25  ARG n 
3 26  SER n 
3 27  HIS n 
3 28  LEU n 
3 29  ARG n 
3 30  GLN n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1   373 human ? CRBN          ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'fall armyworm' 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? baculovirus ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1   395 human ? 'DDB1, XAP1'  ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'fall armyworm' 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? baculovirus ? ? ? ? ? ? 
2 2 sample 'Biological sequence' 396 836 human ? 'DDB1, XAP1'  ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'fall armyworm' 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? baculovirus ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1   30  human ? 'WIZ, ZNF803' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ?               
'Escherichia coli'      562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ?           ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A5H non-polymer         . 
'(3S)-3-(5-{[(4R)-6-ethyl-6-azaspiro[2.5]octan-4-yl]oxy}-1-oxo-1,3-dihydro-2H-isoindol-2-yl)piperidine-2,6-dione' ? 
'C22 H27 N3 O4'  397.467 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION' ? 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION' ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ARG 1   70   ?    ?   ?   A . n 
A 1 2   THR 2   71   ?    ?   ?   A . n 
A 1 3   LEU 3   72   ?    ?   ?   A . n 
A 1 4   HIS 4   73   73   HIS HIS A . n 
A 1 5   ASP 5   74   74   ASP ASP A . n 
A 1 6   ASP 6   75   75   ASP ASP A . n 
A 1 7   ASP 7   76   76   ASP ASP A . n 
A 1 8   SER 8   77   77   SER SER A . n 
A 1 9   CYS 9   78   78   CYS CYS A . n 
A 1 10  GLN 10  79   79   GLN GLN A . n 
A 1 11  VAL 11  80   80   VAL VAL A . n 
A 1 12  ILE 12  81   81   ILE ILE A . n 
A 1 13  PRO 13  82   82   PRO PRO A . n 
A 1 14  VAL 14  83   83   VAL VAL A . n 
A 1 15  LEU 15  84   84   LEU LEU A . n 
A 1 16  PRO 16  85   85   PRO PRO A . n 
A 1 17  GLN 17  86   86   GLN GLN A . n 
A 1 18  VAL 18  87   87   VAL VAL A . n 
A 1 19  MET 19  88   88   MET MET A . n 
A 1 20  MET 20  89   89   MET MET A . n 
A 1 21  ILE 21  90   90   ILE ILE A . n 
A 1 22  LEU 22  91   91   LEU LEU A . n 
A 1 23  ILE 23  92   92   ILE ILE A . n 
A 1 24  PRO 24  93   93   PRO PRO A . n 
A 1 25  GLY 25  94   94   GLY GLY A . n 
A 1 26  GLN 26  95   95   GLN GLN A . n 
A 1 27  THR 27  96   96   THR THR A . n 
A 1 28  LEU 28  97   97   LEU LEU A . n 
A 1 29  PRO 29  98   98   PRO PRO A . n 
A 1 30  LEU 30  99   99   LEU LEU A . n 
A 1 31  GLN 31  100  100  GLN GLN A . n 
A 1 32  LEU 32  101  101  LEU LEU A . n 
A 1 33  PHE 33  102  102  PHE PHE A . n 
A 1 34  HIS 34  103  103  HIS HIS A . n 
A 1 35  PRO 35  104  104  PRO PRO A . n 
A 1 36  GLN 36  105  105  GLN GLN A . n 
A 1 37  GLU 37  106  106  GLU GLU A . n 
A 1 38  VAL 38  107  107  VAL VAL A . n 
A 1 39  SER 39  108  108  SER SER A . n 
A 1 40  MET 40  109  109  MET MET A . n 
A 1 41  VAL 41  110  110  VAL VAL A . n 
A 1 42  ARG 42  111  111  ARG ARG A . n 
A 1 43  ASN 43  112  112  ASN ASN A . n 
A 1 44  LEU 44  113  113  LEU LEU A . n 
A 1 45  ILE 45  114  114  ILE ILE A . n 
A 1 46  GLN 46  115  115  GLN GLN A . n 
A 1 47  LYS 47  116  116  LYS LYS A . n 
A 1 48  ASP 48  117  117  ASP ASP A . n 
A 1 49  ARG 49  118  118  ARG ARG A . n 
A 1 50  THR 50  119  119  THR THR A . n 
A 1 51  PHE 51  120  120  PHE PHE A . n 
A 1 52  ALA 52  121  121  ALA ALA A . n 
A 1 53  VAL 53  122  122  VAL VAL A . n 
A 1 54  LEU 54  123  123  LEU LEU A . n 
A 1 55  ALA 55  124  124  ALA ALA A . n 
A 1 56  TYR 56  125  125  TYR TYR A . n 
A 1 57  SER 57  126  ?    ?   ?   A . n 
A 1 58  ASN 58  127  ?    ?   ?   A . n 
A 1 59  VAL 59  128  ?    ?   ?   A . n 
A 1 60  GLN 60  129  ?    ?   ?   A . n 
A 1 61  GLU 61  130  ?    ?   ?   A . n 
A 1 62  ARG 62  131  ?    ?   ?   A . n 
A 1 63  GLU 63  132  ?    ?   ?   A . n 
A 1 64  ALA 64  133  133  ALA ALA A . n 
A 1 65  GLN 65  134  134  GLN GLN A . n 
A 1 66  PHE 66  135  135  PHE PHE A . n 
A 1 67  GLY 67  136  136  GLY GLY A . n 
A 1 68  THR 68  137  137  THR THR A . n 
A 1 69  THR 69  138  138  THR THR A . n 
A 1 70  ALA 70  139  139  ALA ALA A . n 
A 1 71  GLU 71  140  140  GLU GLU A . n 
A 1 72  ILE 72  141  141  ILE ILE A . n 
A 1 73  TYR 73  142  142  TYR TYR A . n 
A 1 74  ALA 74  143  143  ALA ALA A . n 
A 1 75  TYR 75  144  144  TYR TYR A . n 
A 1 76  ARG 76  145  145  ARG ARG A . n 
A 1 77  GLU 77  146  146  GLU GLU A . n 
A 1 78  GLU 78  147  147  GLU GLU A . n 
A 1 79  GLN 79  148  ?    ?   ?   A . n 
A 1 80  ASP 80  149  ?    ?   ?   A . n 
A 1 81  PHE 81  150  ?    ?   ?   A . n 
A 1 82  GLY 82  151  ?    ?   ?   A . n 
A 1 83  ILE 83  152  ?    ?   ?   A . n 
A 1 84  GLU 84  153  ?    ?   ?   A . n 
A 1 85  ILE 85  154  154  ILE ILE A . n 
A 1 86  VAL 86  155  155  VAL VAL A . n 
A 1 87  LYS 87  156  156  LYS LYS A . n 
A 1 88  VAL 88  157  157  VAL VAL A . n 
A 1 89  LYS 89  158  158  LYS LYS A . n 
A 1 90  ALA 90  159  159  ALA ALA A . n 
A 1 91  ILE 91  160  160  ILE ILE A . n 
A 1 92  GLY 92  161  161  GLY GLY A . n 
A 1 93  ARG 93  162  162  ARG ARG A . n 
A 1 94  GLN 94  163  163  GLN GLN A . n 
A 1 95  ARG 95  164  164  ARG ARG A . n 
A 1 96  PHE 96  165  165  PHE PHE A . n 
A 1 97  LYS 97  166  166  LYS LYS A . n 
A 1 98  VAL 98  167  167  VAL VAL A . n 
A 1 99  LEU 99  168  168  LEU LEU A . n 
A 1 100 GLU 100 169  169  GLU GLU A . n 
A 1 101 LEU 101 170  170  LEU LEU A . n 
A 1 102 ARG 102 171  171  ARG ARG A . n 
A 1 103 THR 103 172  172  THR THR A . n 
A 1 104 GLN 104 173  173  GLN GLN A . n 
A 1 105 SER 105 174  174  SER SER A . n 
A 1 106 ASP 106 175  175  ASP ASP A . n 
A 1 107 GLY 107 176  176  GLY GLY A . n 
A 1 108 ILE 108 177  177  ILE ILE A . n 
A 1 109 GLN 109 178  178  GLN GLN A . n 
A 1 110 GLN 110 179  179  GLN GLN A . n 
A 1 111 ALA 111 180  180  ALA ALA A . n 
A 1 112 LYS 112 181  181  LYS LYS A . n 
A 1 113 VAL 113 182  182  VAL VAL A . n 
A 1 114 GLN 114 183  183  GLN GLN A . n 
A 1 115 ILE 115 184  184  ILE ILE A . n 
A 1 116 LEU 116 185  185  LEU LEU A . n 
A 1 117 PRO 117 186  186  PRO PRO A . n 
A 1 118 GLU 118 187  187  GLU GLU A . n 
A 1 119 CYS 119 188  188  CYS CYS A . n 
A 1 120 VAL 120 189  189  VAL VAL A . n 
A 1 121 LEU 121 190  190  LEU LEU A . n 
A 1 122 PRO 122 191  191  PRO PRO A . n 
A 1 123 SER 123 192  192  SER SER A . n 
A 1 124 THR 124 193  193  THR THR A . n 
A 1 125 MET 125 194  194  MET MET A . n 
A 1 126 SER 126 195  195  SER SER A . n 
A 1 127 ALA 127 196  196  ALA ALA A . n 
A 1 128 VAL 128 197  197  VAL VAL A . n 
A 1 129 GLN 129 198  198  GLN GLN A . n 
A 1 130 LEU 130 199  199  LEU LEU A . n 
A 1 131 GLU 131 200  200  GLU GLU A . n 
A 1 132 SER 132 201  201  SER SER A . n 
A 1 133 LEU 133 202  202  LEU LEU A . n 
A 1 134 ASN 134 203  203  ASN ASN A . n 
A 1 135 LYS 135 204  204  LYS LYS A . n 
A 1 136 CYS 136 205  205  CYS CYS A . n 
A 1 137 GLN 137 206  206  GLN GLN A . n 
A 1 138 ILE 138 207  207  ILE ILE A . n 
A 1 139 PHE 139 208  208  PHE PHE A . n 
A 1 140 PRO 140 209  209  PRO PRO A . n 
A 1 141 SER 141 210  210  SER SER A . n 
A 1 142 LYS 142 211  ?    ?   ?   A . n 
A 1 143 PRO 143 212  ?    ?   ?   A . n 
A 1 144 VAL 144 213  ?    ?   ?   A . n 
A 1 145 SER 145 214  ?    ?   ?   A . n 
A 1 146 ARG 146 215  ?    ?   ?   A . n 
A 1 147 GLU 147 216  ?    ?   ?   A . n 
A 1 148 ASP 148 217  ?    ?   ?   A . n 
A 1 149 GLN 149 218  ?    ?   ?   A . n 
A 1 150 CYS 150 219  ?    ?   ?   A . n 
A 1 151 SER 151 220  220  SER SER A . n 
A 1 152 TYR 152 221  221  TYR TYR A . n 
A 1 153 LYS 153 222  222  LYS LYS A . n 
A 1 154 TRP 154 223  223  TRP TRP A . n 
A 1 155 TRP 155 224  224  TRP TRP A . n 
A 1 156 GLN 156 225  225  GLN GLN A . n 
A 1 157 LYS 157 226  226  LYS LYS A . n 
A 1 158 TYR 158 227  227  TYR TYR A . n 
A 1 159 GLN 159 228  228  GLN GLN A . n 
A 1 160 LYS 160 229  229  LYS LYS A . n 
A 1 161 ARG 161 230  230  ARG ARG A . n 
A 1 162 LYS 162 231  231  LYS LYS A . n 
A 1 163 PHE 163 232  232  PHE PHE A . n 
A 1 164 HIS 164 233  233  HIS HIS A . n 
A 1 165 CYS 165 234  234  CYS CYS A . n 
A 1 166 ALA 166 235  235  ALA ALA A . n 
A 1 167 ASN 167 236  236  ASN ASN A . n 
A 1 168 LEU 168 237  237  LEU LEU A . n 
A 1 169 THR 169 238  238  THR THR A . n 
A 1 170 SER 170 239  239  SER SER A . n 
A 1 171 TRP 171 240  240  TRP TRP A . n 
A 1 172 PRO 172 241  241  PRO PRO A . n 
A 1 173 ARG 173 242  242  ARG ARG A . n 
A 1 174 TRP 174 243  243  TRP TRP A . n 
A 1 175 LEU 175 244  244  LEU LEU A . n 
A 1 176 TYR 176 245  245  TYR TYR A . n 
A 1 177 SER 177 246  246  SER SER A . n 
A 1 178 LEU 178 247  247  LEU LEU A . n 
A 1 179 TYR 179 248  248  TYR TYR A . n 
A 1 180 ASP 180 249  249  ASP ASP A . n 
A 1 181 ALA 181 250  250  ALA ALA A . n 
A 1 182 GLU 182 251  251  GLU GLU A . n 
A 1 183 THR 183 252  252  THR THR A . n 
A 1 184 LEU 184 253  253  LEU LEU A . n 
A 1 185 MET 185 254  254  MET MET A . n 
A 1 186 ASP 186 255  255  ASP ASP A . n 
A 1 187 ARG 187 256  256  ARG ARG A . n 
A 1 188 ILE 188 257  257  ILE ILE A . n 
A 1 189 LYS 189 258  258  LYS LYS A . n 
A 1 190 LYS 190 259  259  LYS LYS A . n 
A 1 191 GLN 191 260  260  GLN GLN A . n 
A 1 192 LEU 192 261  261  LEU LEU A . n 
A 1 193 ARG 193 262  262  ARG ARG A . n 
A 1 194 GLU 194 263  263  GLU GLU A . n 
A 1 195 TRP 195 264  264  TRP TRP A . n 
A 1 196 ASP 196 265  265  ASP ASP A . n 
A 1 197 GLU 197 266  266  GLU GLU A . n 
A 1 198 ASN 198 267  267  ASN ASN A . n 
A 1 199 LEU 199 268  268  LEU LEU A . n 
A 1 200 LYS 200 269  269  LYS LYS A . n 
A 1 201 ASP 201 270  270  ASP ASP A . n 
A 1 202 ASP 202 271  271  ASP ASP A . n 
A 1 203 SER 203 272  272  SER SER A . n 
A 1 204 LEU 204 273  273  LEU LEU A . n 
A 1 205 PRO 205 274  274  PRO PRO A . n 
A 1 206 SER 206 275  275  SER SER A . n 
A 1 207 ASN 207 276  276  ASN ASN A . n 
A 1 208 PRO 208 277  277  PRO PRO A . n 
A 1 209 ILE 209 278  278  ILE ILE A . n 
A 1 210 ASP 210 279  279  ASP ASP A . n 
A 1 211 PHE 211 280  280  PHE PHE A . n 
A 1 212 SER 212 281  281  SER SER A . n 
A 1 213 TYR 213 282  282  TYR TYR A . n 
A 1 214 ARG 214 283  283  ARG ARG A . n 
A 1 215 VAL 215 284  284  VAL VAL A . n 
A 1 216 ALA 216 285  285  ALA ALA A . n 
A 1 217 ALA 217 286  286  ALA ALA A . n 
A 1 218 CYS 218 287  287  CYS CYS A . n 
A 1 219 LEU 219 288  288  LEU LEU A . n 
A 1 220 PRO 220 289  289  PRO PRO A . n 
A 1 221 ILE 221 290  290  ILE ILE A . n 
A 1 222 ASP 222 291  291  ASP ASP A . n 
A 1 223 ASP 223 292  292  ASP ASP A . n 
A 1 224 VAL 224 293  293  VAL VAL A . n 
A 1 225 LEU 225 294  294  LEU LEU A . n 
A 1 226 ARG 226 295  295  ARG ARG A . n 
A 1 227 ILE 227 296  296  ILE ILE A . n 
A 1 228 GLN 228 297  297  GLN GLN A . n 
A 1 229 LEU 229 298  298  LEU LEU A . n 
A 1 230 LEU 230 299  299  LEU LEU A . n 
A 1 231 LYS 231 300  300  LYS LYS A . n 
A 1 232 ILE 232 301  301  ILE ILE A . n 
A 1 233 GLY 233 302  302  GLY GLY A . n 
A 1 234 SER 234 303  303  SER SER A . n 
A 1 235 ALA 235 304  304  ALA ALA A . n 
A 1 236 ILE 236 305  305  ILE ILE A . n 
A 1 237 GLN 237 306  306  GLN GLN A . n 
A 1 238 ARG 238 307  307  ARG ARG A . n 
A 1 239 LEU 239 308  308  LEU LEU A . n 
A 1 240 ARG 240 309  309  ARG ARG A . n 
A 1 241 CYS 241 310  310  CYS CYS A . n 
A 1 242 GLU 242 311  311  GLU GLU A . n 
A 1 243 LEU 243 312  312  LEU LEU A . n 
A 1 244 ASP 244 313  313  ASP ASP A . n 
A 1 245 ILE 245 314  314  ILE ILE A . n 
A 1 246 MET 246 315  315  MET MET A . n 
A 1 247 ASN 247 316  316  ASN ASN A . n 
A 1 248 LYS 248 317  317  LYS LYS A . n 
A 1 249 CYS 249 318  318  CYS CYS A . n 
A 1 250 THR 250 319  319  THR THR A . n 
A 1 251 SER 251 320  320  SER SER A . n 
A 1 252 LEU 252 321  321  LEU LEU A . n 
A 1 253 CYS 253 322  322  CYS CYS A . n 
A 1 254 CYS 254 323  323  CYS CYS A . n 
A 1 255 LYS 255 324  324  LYS LYS A . n 
A 1 256 GLN 256 325  325  GLN GLN A . n 
A 1 257 CYS 257 326  326  CYS CYS A . n 
A 1 258 GLN 258 327  327  GLN GLN A . n 
A 1 259 GLU 259 328  328  GLU GLU A . n 
A 1 260 THR 260 329  329  THR THR A . n 
A 1 261 GLU 261 330  330  GLU GLU A . n 
A 1 262 ILE 262 331  331  ILE ILE A . n 
A 1 263 THR 263 332  332  THR THR A . n 
A 1 264 THR 264 333  333  THR THR A . n 
A 1 265 LYS 265 334  334  LYS LYS A . n 
A 1 266 ASN 266 335  335  ASN ASN A . n 
A 1 267 GLU 267 336  336  GLU GLU A . n 
A 1 268 ILE 268 337  337  ILE ILE A . n 
A 1 269 PHE 269 338  338  PHE PHE A . n 
A 1 270 SER 270 339  339  SER SER A . n 
A 1 271 LEU 271 340  340  LEU LEU A . n 
A 1 272 SER 272 341  341  SER SER A . n 
A 1 273 LEU 273 342  342  LEU LEU A . n 
A 1 274 CYS 274 343  343  CYS CYS A . n 
A 1 275 GLY 275 344  344  GLY GLY A . n 
A 1 276 PRO 276 345  345  PRO PRO A . n 
A 1 277 MET 277 346  346  MET MET A . n 
A 1 278 ALA 278 347  347  ALA ALA A . n 
A 1 279 ALA 279 348  348  ALA ALA A . n 
A 1 280 TYR 280 349  349  TYR TYR A . n 
A 1 281 VAL 281 350  350  VAL VAL A . n 
A 1 282 ASN 282 351  351  ASN ASN A . n 
A 1 283 PRO 283 352  352  PRO PRO A . n 
A 1 284 HIS 284 353  353  HIS HIS A . n 
A 1 285 GLY 285 354  354  GLY GLY A . n 
A 1 286 TYR 286 355  355  TYR TYR A . n 
A 1 287 VAL 287 356  356  VAL VAL A . n 
A 1 288 HIS 288 357  357  HIS HIS A . n 
A 1 289 GLU 289 358  358  GLU GLU A . n 
A 1 290 THR 290 359  359  THR THR A . n 
A 1 291 LEU 291 360  360  LEU LEU A . n 
A 1 292 THR 292 361  361  THR THR A . n 
A 1 293 VAL 293 362  362  VAL VAL A . n 
A 1 294 TYR 294 363  363  TYR TYR A . n 
A 1 295 LYS 295 364  364  LYS LYS A . n 
A 1 296 ALA 296 365  365  ALA ALA A . n 
A 1 297 CYS 297 366  366  CYS CYS A . n 
A 1 298 ASN 298 367  367  ASN ASN A . n 
A 1 299 LEU 299 368  368  LEU LEU A . n 
A 1 300 ASN 300 369  369  ASN ASN A . n 
A 1 301 LEU 301 370  370  LEU LEU A . n 
A 1 302 ILE 302 371  371  ILE ILE A . n 
A 1 303 GLY 303 372  372  GLY GLY A . n 
A 1 304 ARG 304 373  373  ARG ARG A . n 
A 1 305 PRO 305 374  374  PRO PRO A . n 
A 1 306 SER 306 375  375  SER SER A . n 
A 1 307 THR 307 376  376  THR THR A . n 
A 1 308 GLU 308 377  377  GLU GLU A . n 
A 1 309 HIS 309 378  378  HIS HIS A . n 
A 1 310 SER 310 379  379  SER SER A . n 
A 1 311 TRP 311 380  380  TRP TRP A . n 
A 1 312 PHE 312 381  381  PHE PHE A . n 
A 1 313 PRO 313 382  382  PRO PRO A . n 
A 1 314 GLY 314 383  383  GLY GLY A . n 
A 1 315 TYR 315 384  384  TYR TYR A . n 
A 1 316 ALA 316 385  385  ALA ALA A . n 
A 1 317 TRP 317 386  386  TRP TRP A . n 
A 1 318 THR 318 387  387  THR THR A . n 
A 1 319 VAL 319 388  388  VAL VAL A . n 
A 1 320 ALA 320 389  389  ALA ALA A . n 
A 1 321 GLN 321 390  390  GLN GLN A . n 
A 1 322 CYS 322 391  391  CYS CYS A . n 
A 1 323 LYS 323 392  392  LYS LYS A . n 
A 1 324 ILE 324 393  393  ILE ILE A . n 
A 1 325 CYS 325 394  394  CYS CYS A . n 
A 1 326 ALA 326 395  395  ALA ALA A . n 
A 1 327 SER 327 396  396  SER SER A . n 
A 1 328 HIS 328 397  397  HIS HIS A . n 
A 1 329 ILE 329 398  398  ILE ILE A . n 
A 1 330 GLY 330 399  399  GLY GLY A . n 
A 1 331 TRP 331 400  400  TRP TRP A . n 
A 1 332 LYS 332 401  401  LYS LYS A . n 
A 1 333 PHE 333 402  402  PHE PHE A . n 
A 1 334 THR 334 403  403  THR THR A . n 
A 1 335 ALA 335 404  404  ALA ALA A . n 
A 1 336 THR 336 405  405  THR THR A . n 
A 1 337 LYS 337 406  406  LYS LYS A . n 
A 1 338 LYS 338 407  407  LYS LYS A . n 
A 1 339 ASP 339 408  408  ASP ASP A . n 
A 1 340 MET 340 409  409  MET MET A . n 
A 1 341 SER 341 410  410  SER SER A . n 
A 1 342 PRO 342 411  411  PRO PRO A . n 
A 1 343 GLN 343 412  412  GLN GLN A . n 
A 1 344 LYS 344 413  413  LYS LYS A . n 
A 1 345 PHE 345 414  414  PHE PHE A . n 
A 1 346 TRP 346 415  415  TRP TRP A . n 
A 1 347 GLY 347 416  416  GLY GLY A . n 
A 1 348 LEU 348 417  417  LEU LEU A . n 
A 1 349 THR 349 418  418  THR THR A . n 
A 1 350 ARG 350 419  419  ARG ARG A . n 
A 1 351 SER 351 420  420  SER SER A . n 
A 1 352 ALA 352 421  421  ALA ALA A . n 
A 1 353 LEU 353 422  422  LEU LEU A . n 
A 1 354 LEU 354 423  423  LEU LEU A . n 
A 1 355 PRO 355 424  424  PRO PRO A . n 
A 1 356 THR 356 425  425  THR THR A . n 
A 1 357 ILE 357 426  426  ILE ILE A . n 
A 1 358 PRO 358 427  427  PRO PRO A . n 
A 1 359 ASP 359 428  ?    ?   ?   A . n 
A 1 360 THR 360 429  ?    ?   ?   A . n 
A 1 361 GLU 361 430  ?    ?   ?   A . n 
A 1 362 ASP 362 431  ?    ?   ?   A . n 
A 1 363 GLU 363 432  ?    ?   ?   A . n 
A 1 364 ILE 364 433  ?    ?   ?   A . n 
A 1 365 SER 365 434  ?    ?   ?   A . n 
A 1 366 PRO 366 435  ?    ?   ?   A . n 
A 1 367 ASP 367 436  ?    ?   ?   A . n 
A 1 368 LYS 368 437  ?    ?   ?   A . n 
A 1 369 VAL 369 438  438  VAL VAL A . n 
A 1 370 ILE 370 439  439  ILE ILE A . n 
A 1 371 LEU 371 440  440  LEU LEU A . n 
A 1 372 CYS 372 441  441  CYS CYS A . n 
A 1 373 LEU 373 442  442  LEU LEU A . n 
B 2 1   MET 1   1    ?    ?   ?   B . n 
B 2 2   SER 2   2    2    SER SER B . n 
B 2 3   TYR 3   3    3    TYR TYR B . n 
B 2 4   ASN 4   4    4    ASN ASN B . n 
B 2 5   TYR 5   5    5    TYR TYR B . n 
B 2 6   VAL 6   6    6    VAL VAL B . n 
B 2 7   VAL 7   7    7    VAL VAL B . n 
B 2 8   THR 8   8    8    THR THR B . n 
B 2 9   ALA 9   9    9    ALA ALA B . n 
B 2 10  GLN 10  10   10   GLN GLN B . n 
B 2 11  LYS 11  11   11   LYS LYS B . n 
B 2 12  PRO 12  12   12   PRO PRO B . n 
B 2 13  THR 13  13   13   THR THR B . n 
B 2 14  ALA 14  14   14   ALA ALA B . n 
B 2 15  VAL 15  15   15   VAL VAL B . n 
B 2 16  ASN 16  16   16   ASN ASN B . n 
B 2 17  GLY 17  17   17   GLY GLY B . n 
B 2 18  CYS 18  18   18   CYS CYS B . n 
B 2 19  VAL 19  19   19   VAL VAL B . n 
B 2 20  THR 20  20   20   THR THR B . n 
B 2 21  GLY 21  21   21   GLY GLY B . n 
B 2 22  HIS 22  22   22   HIS HIS B . n 
B 2 23  PHE 23  23   23   PHE PHE B . n 
B 2 24  THR 24  24   24   THR THR B . n 
B 2 25  SER 25  25   25   SER SER B . n 
B 2 26  ALA 26  26   26   ALA ALA B . n 
B 2 27  GLU 27  27   27   GLU GLU B . n 
B 2 28  ASP 28  28   28   ASP ASP B . n 
B 2 29  LEU 29  29   29   LEU LEU B . n 
B 2 30  ASN 30  30   30   ASN ASN B . n 
B 2 31  LEU 31  31   31   LEU LEU B . n 
B 2 32  LEU 32  32   32   LEU LEU B . n 
B 2 33  ILE 33  33   33   ILE ILE B . n 
B 2 34  ALA 34  34   34   ALA ALA B . n 
B 2 35  LYS 35  35   35   LYS LYS B . n 
B 2 36  ASN 36  36   36   ASN ASN B . n 
B 2 37  THR 37  37   37   THR THR B . n 
B 2 38  ARG 38  38   38   ARG ARG B . n 
B 2 39  LEU 39  39   39   LEU LEU B . n 
B 2 40  GLU 40  40   40   GLU GLU B . n 
B 2 41  ILE 41  41   41   ILE ILE B . n 
B 2 42  TYR 42  42   42   TYR TYR B . n 
B 2 43  VAL 43  43   43   VAL VAL B . n 
B 2 44  VAL 44  44   44   VAL VAL B . n 
B 2 45  THR 45  45   45   THR THR B . n 
B 2 46  ALA 46  46   46   ALA ALA B . n 
B 2 47  GLU 47  47   47   GLU GLU B . n 
B 2 48  GLY 48  48   48   GLY GLY B . n 
B 2 49  LEU 49  49   49   LEU LEU B . n 
B 2 50  ARG 50  50   50   ARG ARG B . n 
B 2 51  PRO 51  51   51   PRO PRO B . n 
B 2 52  VAL 52  52   52   VAL VAL B . n 
B 2 53  LYS 53  53   53   LYS LYS B . n 
B 2 54  GLU 54  54   54   GLU GLU B . n 
B 2 55  VAL 55  55   55   VAL VAL B . n 
B 2 56  GLY 56  56   56   GLY GLY B . n 
B 2 57  MET 57  57   57   MET MET B . n 
B 2 58  TYR 58  58   58   TYR TYR B . n 
B 2 59  GLY 59  59   59   GLY GLY B . n 
B 2 60  LYS 60  60   60   LYS LYS B . n 
B 2 61  ILE 61  61   61   ILE ILE B . n 
B 2 62  ALA 62  62   62   ALA ALA B . n 
B 2 63  VAL 63  63   63   VAL VAL B . n 
B 2 64  MET 64  64   64   MET MET B . n 
B 2 65  GLU 65  65   65   GLU GLU B . n 
B 2 66  LEU 66  66   66   LEU LEU B . n 
B 2 67  PHE 67  67   67   PHE PHE B . n 
B 2 68  ARG 68  68   68   ARG ARG B . n 
B 2 69  PRO 69  69   69   PRO PRO B . n 
B 2 70  LYS 70  70   70   LYS LYS B . n 
B 2 71  GLY 71  71   71   GLY GLY B . n 
B 2 72  GLU 72  72   72   GLU GLU B . n 
B 2 73  SER 73  73   73   SER SER B . n 
B 2 74  LYS 74  74   74   LYS LYS B . n 
B 2 75  ASP 75  75   75   ASP ASP B . n 
B 2 76  LEU 76  76   76   LEU LEU B . n 
B 2 77  LEU 77  77   77   LEU LEU B . n 
B 2 78  PHE 78  78   78   PHE PHE B . n 
B 2 79  ILE 79  79   79   ILE ILE B . n 
B 2 80  LEU 80  80   80   LEU LEU B . n 
B 2 81  THR 81  81   81   THR THR B . n 
B 2 82  ALA 82  82   82   ALA ALA B . n 
B 2 83  LYS 83  83   83   LYS LYS B . n 
B 2 84  TYR 84  84   84   TYR TYR B . n 
B 2 85  ASN 85  85   85   ASN ASN B . n 
B 2 86  ALA 86  86   86   ALA ALA B . n 
B 2 87  CYS 87  87   87   CYS CYS B . n 
B 2 88  ILE 88  88   88   ILE ILE B . n 
B 2 89  LEU 89  89   89   LEU LEU B . n 
B 2 90  GLU 90  90   90   GLU GLU B . n 
B 2 91  TYR 91  91   91   TYR TYR B . n 
B 2 92  LYS 92  92   92   LYS LYS B . n 
B 2 93  GLN 93  93   93   GLN GLN B . n 
B 2 94  SER 94  94   94   SER SER B . n 
B 2 95  GLY 95  95   95   GLY GLY B . n 
B 2 96  GLU 96  96   96   GLU GLU B . n 
B 2 97  SER 97  97   97   SER SER B . n 
B 2 98  ILE 98  98   98   ILE ILE B . n 
B 2 99  ASP 99  99   99   ASP ASP B . n 
B 2 100 ILE 100 100  100  ILE ILE B . n 
B 2 101 ILE 101 101  101  ILE ILE B . n 
B 2 102 THR 102 102  102  THR THR B . n 
B 2 103 ARG 103 103  103  ARG ARG B . n 
B 2 104 ALA 104 104  104  ALA ALA B . n 
B 2 105 HIS 105 105  105  HIS HIS B . n 
B 2 106 GLY 106 106  106  GLY GLY B . n 
B 2 107 ASN 107 107  107  ASN ASN B . n 
B 2 108 VAL 108 108  108  VAL VAL B . n 
B 2 109 GLN 109 109  109  GLN GLN B . n 
B 2 110 ASP 110 110  110  ASP ASP B . n 
B 2 111 ARG 111 111  111  ARG ARG B . n 
B 2 112 ILE 112 112  112  ILE ILE B . n 
B 2 113 GLY 113 113  113  GLY GLY B . n 
B 2 114 ARG 114 114  114  ARG ARG B . n 
B 2 115 PRO 115 115  115  PRO PRO B . n 
B 2 116 SER 116 116  116  SER SER B . n 
B 2 117 GLU 117 117  117  GLU GLU B . n 
B 2 118 THR 118 118  118  THR THR B . n 
B 2 119 GLY 119 119  119  GLY GLY B . n 
B 2 120 ILE 120 120  120  ILE ILE B . n 
B 2 121 ILE 121 121  121  ILE ILE B . n 
B 2 122 GLY 122 122  122  GLY GLY B . n 
B 2 123 ILE 123 123  123  ILE ILE B . n 
B 2 124 ILE 124 124  124  ILE ILE B . n 
B 2 125 ASP 125 125  125  ASP ASP B . n 
B 2 126 PRO 126 126  126  PRO PRO B . n 
B 2 127 GLU 127 127  127  GLU GLU B . n 
B 2 128 CYS 128 128  128  CYS CYS B . n 
B 2 129 ARG 129 129  129  ARG ARG B . n 
B 2 130 MET 130 130  130  MET MET B . n 
B 2 131 ILE 131 131  131  ILE ILE B . n 
B 2 132 GLY 132 132  132  GLY GLY B . n 
B 2 133 LEU 133 133  133  LEU LEU B . n 
B 2 134 ARG 134 134  134  ARG ARG B . n 
B 2 135 LEU 135 135  135  LEU LEU B . n 
B 2 136 TYR 136 136  136  TYR TYR B . n 
B 2 137 ASP 137 137  137  ASP ASP B . n 
B 2 138 GLY 138 138  138  GLY GLY B . n 
B 2 139 LEU 139 139  139  LEU LEU B . n 
B 2 140 PHE 140 140  140  PHE PHE B . n 
B 2 141 LYS 141 141  141  LYS LYS B . n 
B 2 142 VAL 142 142  142  VAL VAL B . n 
B 2 143 ILE 143 143  143  ILE ILE B . n 
B 2 144 PRO 144 144  144  PRO PRO B . n 
B 2 145 LEU 145 145  145  LEU LEU B . n 
B 2 146 ASP 146 146  146  ASP ASP B . n 
B 2 147 ARG 147 147  147  ARG ARG B . n 
B 2 148 ASP 148 148  148  ASP ASP B . n 
B 2 149 ASN 149 149  149  ASN ASN B . n 
B 2 150 LYS 150 150  150  LYS LYS B . n 
B 2 151 GLU 151 151  151  GLU GLU B . n 
B 2 152 LEU 152 152  152  LEU LEU B . n 
B 2 153 LYS 153 153  153  LYS LYS B . n 
B 2 154 ALA 154 154  154  ALA ALA B . n 
B 2 155 PHE 155 155  155  PHE PHE B . n 
B 2 156 ASN 156 156  156  ASN ASN B . n 
B 2 157 ILE 157 157  157  ILE ILE B . n 
B 2 158 ARG 158 158  158  ARG ARG B . n 
B 2 159 LEU 159 159  159  LEU LEU B . n 
B 2 160 GLU 160 160  160  GLU GLU B . n 
B 2 161 GLU 161 161  161  GLU GLU B . n 
B 2 162 LEU 162 162  162  LEU LEU B . n 
B 2 163 HIS 163 163  163  HIS HIS B . n 
B 2 164 VAL 164 164  164  VAL VAL B . n 
B 2 165 ILE 165 165  165  ILE ILE B . n 
B 2 166 ASP 166 166  166  ASP ASP B . n 
B 2 167 VAL 167 167  167  VAL VAL B . n 
B 2 168 LYS 168 168  168  LYS LYS B . n 
B 2 169 PHE 169 169  169  PHE PHE B . n 
B 2 170 LEU 170 170  170  LEU LEU B . n 
B 2 171 TYR 171 171  171  TYR TYR B . n 
B 2 172 GLY 172 172  172  GLY GLY B . n 
B 2 173 CYS 173 173  173  CYS CYS B . n 
B 2 174 GLN 174 174  174  GLN GLN B . n 
B 2 175 ALA 175 175  175  ALA ALA B . n 
B 2 176 PRO 176 176  176  PRO PRO B . n 
B 2 177 THR 177 177  177  THR THR B . n 
B 2 178 ILE 178 178  178  ILE ILE B . n 
B 2 179 CYS 179 179  179  CYS CYS B . n 
B 2 180 PHE 180 180  180  PHE PHE B . n 
B 2 181 VAL 181 181  181  VAL VAL B . n 
B 2 182 TYR 182 182  182  TYR TYR B . n 
B 2 183 GLN 183 183  183  GLN GLN B . n 
B 2 184 ASP 184 184  184  ASP ASP B . n 
B 2 185 PRO 185 185  185  PRO PRO B . n 
B 2 186 GLN 186 186  186  GLN GLN B . n 
B 2 187 GLY 187 187  187  GLY GLY B . n 
B 2 188 ARG 188 188  188  ARG ARG B . n 
B 2 189 HIS 189 189  189  HIS HIS B . n 
B 2 190 VAL 190 190  190  VAL VAL B . n 
B 2 191 LYS 191 191  191  LYS LYS B . n 
B 2 192 THR 192 192  192  THR THR B . n 
B 2 193 TYR 193 193  193  TYR TYR B . n 
B 2 194 GLU 194 194  194  GLU GLU B . n 
B 2 195 VAL 195 195  195  VAL VAL B . n 
B 2 196 SER 196 196  196  SER SER B . n 
B 2 197 LEU 197 197  197  LEU LEU B . n 
B 2 198 ARG 198 198  198  ARG ARG B . n 
B 2 199 GLU 199 199  199  GLU GLU B . n 
B 2 200 LYS 200 200  200  LYS LYS B . n 
B 2 201 GLU 201 201  201  GLU GLU B . n 
B 2 202 PHE 202 202  202  PHE PHE B . n 
B 2 203 ASN 203 203  203  ASN ASN B . n 
B 2 204 LYS 204 204  204  LYS LYS B . n 
B 2 205 GLY 205 205  205  GLY GLY B . n 
B 2 206 PRO 206 206  206  PRO PRO B . n 
B 2 207 TRP 207 207  207  TRP TRP B . n 
B 2 208 LYS 208 208  208  LYS LYS B . n 
B 2 209 GLN 209 209  209  GLN GLN B . n 
B 2 210 GLU 210 210  210  GLU GLU B . n 
B 2 211 ASN 211 211  211  ASN ASN B . n 
B 2 212 VAL 212 212  212  VAL VAL B . n 
B 2 213 GLU 213 213  213  GLU GLU B . n 
B 2 214 ALA 214 214  214  ALA ALA B . n 
B 2 215 GLU 215 215  215  GLU GLU B . n 
B 2 216 ALA 216 216  216  ALA ALA B . n 
B 2 217 SER 217 217  217  SER SER B . n 
B 2 218 MET 218 218  218  MET MET B . n 
B 2 219 VAL 219 219  219  VAL VAL B . n 
B 2 220 ILE 220 220  220  ILE ILE B . n 
B 2 221 ALA 221 221  221  ALA ALA B . n 
B 2 222 VAL 222 222  222  VAL VAL B . n 
B 2 223 PRO 223 223  223  PRO PRO B . n 
B 2 224 GLU 224 224  224  GLU GLU B . n 
B 2 225 PRO 225 225  225  PRO PRO B . n 
B 2 226 PHE 226 226  226  PHE PHE B . n 
B 2 227 GLY 227 227  227  GLY GLY B . n 
B 2 228 GLY 228 228  228  GLY GLY B . n 
B 2 229 ALA 229 229  229  ALA ALA B . n 
B 2 230 ILE 230 230  230  ILE ILE B . n 
B 2 231 ILE 231 231  231  ILE ILE B . n 
B 2 232 ILE 232 232  232  ILE ILE B . n 
B 2 233 GLY 233 233  233  GLY GLY B . n 
B 2 234 GLN 234 234  234  GLN GLN B . n 
B 2 235 GLU 235 235  235  GLU GLU B . n 
B 2 236 SER 236 236  236  SER SER B . n 
B 2 237 ILE 237 237  237  ILE ILE B . n 
B 2 238 THR 238 238  238  THR THR B . n 
B 2 239 TYR 239 239  239  TYR TYR B . n 
B 2 240 HIS 240 240  240  HIS HIS B . n 
B 2 241 ASN 241 241  241  ASN ASN B . n 
B 2 242 GLY 242 242  242  GLY GLY B . n 
B 2 243 ASP 243 243  243  ASP ASP B . n 
B 2 244 LYS 244 244  244  LYS LYS B . n 
B 2 245 TYR 245 245  245  TYR TYR B . n 
B 2 246 LEU 246 246  246  LEU LEU B . n 
B 2 247 ALA 247 247  247  ALA ALA B . n 
B 2 248 ILE 248 248  248  ILE ILE B . n 
B 2 249 ALA 249 249  249  ALA ALA B . n 
B 2 250 PRO 250 250  250  PRO PRO B . n 
B 2 251 PRO 251 251  251  PRO PRO B . n 
B 2 252 ILE 252 252  252  ILE ILE B . n 
B 2 253 ILE 253 253  253  ILE ILE B . n 
B 2 254 LYS 254 254  254  LYS LYS B . n 
B 2 255 GLN 255 255  255  GLN GLN B . n 
B 2 256 SER 256 256  256  SER SER B . n 
B 2 257 THR 257 257  257  THR THR B . n 
B 2 258 ILE 258 258  258  ILE ILE B . n 
B 2 259 VAL 259 259  259  VAL VAL B . n 
B 2 260 CYS 260 260  260  CYS CYS B . n 
B 2 261 HIS 261 261  261  HIS HIS B . n 
B 2 262 ASN 262 262  262  ASN ASN B . n 
B 2 263 ARG 263 263  263  ARG ARG B . n 
B 2 264 VAL 264 264  264  VAL VAL B . n 
B 2 265 ASP 265 265  265  ASP ASP B . n 
B 2 266 PRO 266 266  266  PRO PRO B . n 
B 2 267 ASN 267 267  267  ASN ASN B . n 
B 2 268 GLY 268 268  268  GLY GLY B . n 
B 2 269 SER 269 269  269  SER SER B . n 
B 2 270 ARG 270 270  270  ARG ARG B . n 
B 2 271 TYR 271 271  271  TYR TYR B . n 
B 2 272 LEU 272 272  272  LEU LEU B . n 
B 2 273 LEU 273 273  273  LEU LEU B . n 
B 2 274 GLY 274 274  274  GLY GLY B . n 
B 2 275 ASP 275 275  275  ASP ASP B . n 
B 2 276 MET 276 276  276  MET MET B . n 
B 2 277 GLU 277 277  277  GLU GLU B . n 
B 2 278 GLY 278 278  278  GLY GLY B . n 
B 2 279 ARG 279 279  279  ARG ARG B . n 
B 2 280 LEU 280 280  280  LEU LEU B . n 
B 2 281 PHE 281 281  281  PHE PHE B . n 
B 2 282 MET 282 282  282  MET MET B . n 
B 2 283 LEU 283 283  283  LEU LEU B . n 
B 2 284 LEU 284 284  284  LEU LEU B . n 
B 2 285 LEU 285 285  285  LEU LEU B . n 
B 2 286 GLU 286 286  286  GLU GLU B . n 
B 2 287 LYS 287 287  287  LYS LYS B . n 
B 2 288 GLU 288 288  288  GLU GLU B . n 
B 2 289 GLU 289 289  289  GLU GLU B . n 
B 2 290 GLN 290 290  290  GLN GLN B . n 
B 2 291 MET 291 291  291  MET MET B . n 
B 2 292 ASP 292 292  292  ASP ASP B . n 
B 2 293 GLY 293 293  293  GLY GLY B . n 
B 2 294 THR 294 294  294  THR THR B . n 
B 2 295 VAL 295 295  295  VAL VAL B . n 
B 2 296 THR 296 296  296  THR THR B . n 
B 2 297 LEU 297 297  297  LEU LEU B . n 
B 2 298 LYS 298 298  298  LYS LYS B . n 
B 2 299 ASP 299 299  299  ASP ASP B . n 
B 2 300 LEU 300 300  300  LEU LEU B . n 
B 2 301 ARG 301 301  301  ARG ARG B . n 
B 2 302 VAL 302 302  302  VAL VAL B . n 
B 2 303 GLU 303 303  303  GLU GLU B . n 
B 2 304 LEU 304 304  304  LEU LEU B . n 
B 2 305 LEU 305 305  305  LEU LEU B . n 
B 2 306 GLY 306 306  306  GLY GLY B . n 
B 2 307 GLU 307 307  307  GLU GLU B . n 
B 2 308 THR 308 308  308  THR THR B . n 
B 2 309 SER 309 309  309  SER SER B . n 
B 2 310 ILE 310 310  310  ILE ILE B . n 
B 2 311 ALA 311 311  311  ALA ALA B . n 
B 2 312 GLU 312 312  312  GLU GLU B . n 
B 2 313 CYS 313 313  313  CYS CYS B . n 
B 2 314 LEU 314 314  314  LEU LEU B . n 
B 2 315 THR 315 315  315  THR THR B . n 
B 2 316 TYR 316 316  316  TYR TYR B . n 
B 2 317 LEU 317 317  317  LEU LEU B . n 
B 2 318 ASP 318 318  318  ASP ASP B . n 
B 2 319 ASN 319 319  319  ASN ASN B . n 
B 2 320 GLY 320 320  320  GLY GLY B . n 
B 2 321 VAL 321 321  321  VAL VAL B . n 
B 2 322 VAL 322 322  322  VAL VAL B . n 
B 2 323 PHE 323 323  323  PHE PHE B . n 
B 2 324 VAL 324 324  324  VAL VAL B . n 
B 2 325 GLY 325 325  325  GLY GLY B . n 
B 2 326 SER 326 326  326  SER SER B . n 
B 2 327 ARG 327 327  327  ARG ARG B . n 
B 2 328 LEU 328 328  328  LEU LEU B . n 
B 2 329 GLY 329 329  329  GLY GLY B . n 
B 2 330 ASP 330 330  330  ASP ASP B . n 
B 2 331 SER 331 331  331  SER SER B . n 
B 2 332 GLN 332 332  332  GLN GLN B . n 
B 2 333 LEU 333 333  333  LEU LEU B . n 
B 2 334 VAL 334 334  334  VAL VAL B . n 
B 2 335 LYS 335 335  335  LYS LYS B . n 
B 2 336 LEU 336 336  336  LEU LEU B . n 
B 2 337 ASN 337 337  337  ASN ASN B . n 
B 2 338 VAL 338 338  338  VAL VAL B . n 
B 2 339 ASP 339 339  339  ASP ASP B . n 
B 2 340 SER 340 340  340  SER SER B . n 
B 2 341 ASN 341 341  341  ASN ASN B . n 
B 2 342 GLU 342 342  342  GLU GLU B . n 
B 2 343 GLN 343 343  343  GLN GLN B . n 
B 2 344 GLY 344 344  344  GLY GLY B . n 
B 2 345 SER 345 345  345  SER SER B . n 
B 2 346 TYR 346 346  346  TYR TYR B . n 
B 2 347 VAL 347 347  347  VAL VAL B . n 
B 2 348 VAL 348 348  348  VAL VAL B . n 
B 2 349 ALA 349 349  349  ALA ALA B . n 
B 2 350 MET 350 350  350  MET MET B . n 
B 2 351 GLU 351 351  351  GLU GLU B . n 
B 2 352 THR 352 352  352  THR THR B . n 
B 2 353 PHE 353 353  353  PHE PHE B . n 
B 2 354 THR 354 354  354  THR THR B . n 
B 2 355 ASN 355 355  355  ASN ASN B . n 
B 2 356 LEU 356 356  356  LEU LEU B . n 
B 2 357 GLY 357 357  357  GLY GLY B . n 
B 2 358 PRO 358 358  358  PRO PRO B . n 
B 2 359 ILE 359 359  359  ILE ILE B . n 
B 2 360 VAL 360 360  360  VAL VAL B . n 
B 2 361 ASP 361 361  361  ASP ASP B . n 
B 2 362 MET 362 362  362  MET MET B . n 
B 2 363 CYS 363 363  363  CYS CYS B . n 
B 2 364 VAL 364 364  364  VAL VAL B . n 
B 2 365 VAL 365 365  365  VAL VAL B . n 
B 2 366 ASP 366 366  366  ASP ASP B . n 
B 2 367 LEU 367 367  367  LEU LEU B . n 
B 2 368 GLU 368 368  368  GLU GLU B . n 
B 2 369 ARG 369 369  369  ARG ARG B . n 
B 2 370 GLN 370 370  370  GLN GLN B . n 
B 2 371 GLY 371 371  371  GLY GLY B . n 
B 2 372 GLN 372 372  372  GLN GLN B . n 
B 2 373 GLY 373 373  373  GLY GLY B . n 
B 2 374 GLN 374 374  374  GLN GLN B . n 
B 2 375 LEU 375 375  375  LEU LEU B . n 
B 2 376 VAL 376 376  376  VAL VAL B . n 
B 2 377 THR 377 377  377  THR THR B . n 
B 2 378 CYS 378 378  378  CYS CYS B . n 
B 2 379 SER 379 379  379  SER SER B . n 
B 2 380 GLY 380 380  380  GLY GLY B . n 
B 2 381 ALA 381 381  381  ALA ALA B . n 
B 2 382 PHE 382 382  382  PHE PHE B . n 
B 2 383 LYS 383 383  383  LYS LYS B . n 
B 2 384 GLU 384 384  384  GLU GLU B . n 
B 2 385 GLY 385 385  385  GLY GLY B . n 
B 2 386 SER 386 386  386  SER SER B . n 
B 2 387 LEU 387 387  387  LEU LEU B . n 
B 2 388 ARG 388 388  388  ARG ARG B . n 
B 2 389 ILE 389 389  389  ILE ILE B . n 
B 2 390 ILE 390 390  390  ILE ILE B . n 
B 2 391 ARG 391 391  391  ARG ARG B . n 
B 2 392 ASN 392 392  392  ASN ASN B . n 
B 2 393 GLY 393 697  ?    ?   ?   B . n 
B 2 394 ILE 394 698  ?    ?   ?   B . n 
B 2 395 GLY 395 699  ?    ?   ?   B . n 
B 2 396 GLY 396 700  ?    ?   ?   B . n 
B 2 397 ASN 397 701  ?    ?   ?   B . n 
B 2 398 GLY 398 702  ?    ?   ?   B . n 
B 2 399 ASN 399 703  ?    ?   ?   B . n 
B 2 400 SER 400 704  ?    ?   ?   B . n 
B 2 401 GLY 401 705  ?    ?   ?   B . n 
B 2 402 GLU 402 706  ?    ?   ?   B . n 
B 2 403 ILE 403 707  ?    ?   ?   B . n 
B 2 404 GLN 404 708  ?    ?   ?   B . n 
B 2 405 LYS 405 709  ?    ?   ?   B . n 
B 2 406 LEU 406 710  710  LEU LEU B . n 
B 2 407 HIS 407 711  711  HIS HIS B . n 
B 2 408 ILE 408 712  712  ILE ILE B . n 
B 2 409 ARG 409 713  713  ARG ARG B . n 
B 2 410 THR 410 714  714  THR THR B . n 
B 2 411 VAL 411 715  715  VAL VAL B . n 
B 2 412 PRO 412 716  716  PRO PRO B . n 
B 2 413 LEU 413 717  717  LEU LEU B . n 
B 2 414 TYR 414 718  718  TYR TYR B . n 
B 2 415 GLU 415 719  719  GLU GLU B . n 
B 2 416 SER 416 720  720  SER SER B . n 
B 2 417 PRO 417 721  721  PRO PRO B . n 
B 2 418 ARG 418 722  722  ARG ARG B . n 
B 2 419 LYS 419 723  723  LYS LYS B . n 
B 2 420 ILE 420 724  724  ILE ILE B . n 
B 2 421 CYS 421 725  725  CYS CYS B . n 
B 2 422 TYR 422 726  726  TYR TYR B . n 
B 2 423 GLN 423 727  727  GLN GLN B . n 
B 2 424 GLU 424 728  728  GLU GLU B . n 
B 2 425 VAL 425 729  729  VAL VAL B . n 
B 2 426 SER 426 730  730  SER SER B . n 
B 2 427 GLN 427 731  731  GLN GLN B . n 
B 2 428 CYS 428 732  732  CYS CYS B . n 
B 2 429 PHE 429 733  733  PHE PHE B . n 
B 2 430 GLY 430 734  734  GLY GLY B . n 
B 2 431 VAL 431 735  735  VAL VAL B . n 
B 2 432 LEU 432 736  736  LEU LEU B . n 
B 2 433 SER 433 737  737  SER SER B . n 
B 2 434 SER 434 738  738  SER SER B . n 
B 2 435 ARG 435 739  739  ARG ARG B . n 
B 2 436 ILE 436 740  740  ILE ILE B . n 
B 2 437 GLU 437 741  741  GLU GLU B . n 
B 2 438 VAL 438 742  742  VAL VAL B . n 
B 2 439 GLN 439 743  743  GLN GLN B . n 
B 2 440 ASP 440 744  744  ASP ASP B . n 
B 2 441 THR 441 745  745  THR THR B . n 
B 2 442 SER 442 746  746  SER SER B . n 
B 2 443 GLY 443 747  747  GLY GLY B . n 
B 2 444 GLY 444 748  748  GLY GLY B . n 
B 2 445 THR 445 749  749  THR THR B . n 
B 2 446 THR 446 750  750  THR THR B . n 
B 2 447 ALA 447 751  751  ALA ALA B . n 
B 2 448 LEU 448 752  752  LEU LEU B . n 
B 2 449 ARG 449 753  753  ARG ARG B . n 
B 2 450 PRO 450 754  754  PRO PRO B . n 
B 2 451 SER 451 755  755  SER SER B . n 
B 2 452 ALA 452 756  756  ALA ALA B . n 
B 2 453 SER 453 757  757  SER SER B . n 
B 2 454 THR 454 758  758  THR THR B . n 
B 2 455 GLN 455 759  759  GLN GLN B . n 
B 2 456 ALA 456 760  760  ALA ALA B . n 
B 2 457 LEU 457 761  761  LEU LEU B . n 
B 2 458 SER 458 762  762  SER SER B . n 
B 2 459 SER 459 763  763  SER SER B . n 
B 2 460 SER 460 764  764  SER SER B . n 
B 2 461 VAL 461 765  765  VAL VAL B . n 
B 2 462 SER 462 766  766  SER SER B . n 
B 2 463 SER 463 767  767  SER SER B . n 
B 2 464 SER 464 768  768  SER SER B . n 
B 2 465 LYS 465 769  769  LYS LYS B . n 
B 2 466 LEU 466 770  770  LEU LEU B . n 
B 2 467 PHE 467 771  771  PHE PHE B . n 
B 2 468 SER 468 772  772  SER SER B . n 
B 2 469 SER 469 773  773  SER SER B . n 
B 2 470 SER 470 774  ?    ?   ?   B . n 
B 2 471 THR 471 775  ?    ?   ?   B . n 
B 2 472 ALA 472 776  ?    ?   ?   B . n 
B 2 473 PRO 473 777  ?    ?   ?   B . n 
B 2 474 HIS 474 778  778  HIS ALA B . n 
B 2 475 GLU 475 779  779  GLU ALA B . n 
B 2 476 THR 476 780  780  THR THR B . n 
B 2 477 SER 477 781  781  SER SER B . n 
B 2 478 PHE 478 782  782  PHE PHE B . n 
B 2 479 GLY 479 783  783  GLY GLY B . n 
B 2 480 GLU 480 784  784  GLU GLU B . n 
B 2 481 GLU 481 785  785  GLU GLU B . n 
B 2 482 VAL 482 786  786  VAL VAL B . n 
B 2 483 GLU 483 787  787  GLU GLU B . n 
B 2 484 VAL 484 788  788  VAL VAL B . n 
B 2 485 HIS 485 789  789  HIS HIS B . n 
B 2 486 ASN 486 790  790  ASN ASN B . n 
B 2 487 LEU 487 791  791  LEU LEU B . n 
B 2 488 LEU 488 792  792  LEU LEU B . n 
B 2 489 ILE 489 793  793  ILE ILE B . n 
B 2 490 ILE 490 794  794  ILE ILE B . n 
B 2 491 ASP 491 795  795  ASP ASP B . n 
B 2 492 GLN 492 796  796  GLN GLN B . n 
B 2 493 HIS 493 797  797  HIS HIS B . n 
B 2 494 THR 494 798  798  THR THR B . n 
B 2 495 PHE 495 799  799  PHE PHE B . n 
B 2 496 GLU 496 800  800  GLU GLU B . n 
B 2 497 VAL 497 801  801  VAL VAL B . n 
B 2 498 LEU 498 802  802  LEU LEU B . n 
B 2 499 HIS 499 803  803  HIS HIS B . n 
B 2 500 ALA 500 804  804  ALA ALA B . n 
B 2 501 HIS 501 805  805  HIS HIS B . n 
B 2 502 GLN 502 806  806  GLN GLN B . n 
B 2 503 PHE 503 807  807  PHE PHE B . n 
B 2 504 LEU 504 808  808  LEU LEU B . n 
B 2 505 GLN 505 809  809  GLN GLN B . n 
B 2 506 ASN 506 810  810  ASN ASN B . n 
B 2 507 GLU 507 811  811  GLU GLU B . n 
B 2 508 TYR 508 812  812  TYR TYR B . n 
B 2 509 ALA 509 813  813  ALA ALA B . n 
B 2 510 LEU 510 814  814  LEU LEU B . n 
B 2 511 SER 511 815  815  SER SER B . n 
B 2 512 LEU 512 816  816  LEU LEU B . n 
B 2 513 VAL 513 817  817  VAL VAL B . n 
B 2 514 SER 514 818  818  SER SER B . n 
B 2 515 CYS 515 819  819  CYS CYS B . n 
B 2 516 LYS 516 820  820  LYS LYS B . n 
B 2 517 LEU 517 821  821  LEU LEU B . n 
B 2 518 GLY 518 822  822  GLY GLY B . n 
B 2 519 LYS 519 823  823  LYS LYS B . n 
B 2 520 ASP 520 824  824  ASP ASP B . n 
B 2 521 PRO 521 825  825  PRO PRO B . n 
B 2 522 ASN 522 826  826  ASN ASN B . n 
B 2 523 THR 523 827  827  THR THR B . n 
B 2 524 TYR 524 828  828  TYR TYR B . n 
B 2 525 PHE 525 829  829  PHE PHE B . n 
B 2 526 ILE 526 830  830  ILE ILE B . n 
B 2 527 VAL 527 831  831  VAL VAL B . n 
B 2 528 GLY 528 832  832  GLY GLY B . n 
B 2 529 THR 529 833  833  THR THR B . n 
B 2 530 ALA 530 834  834  ALA ALA B . n 
B 2 531 MET 531 835  835  MET MET B . n 
B 2 532 VAL 532 836  836  VAL VAL B . n 
B 2 533 TYR 533 837  837  TYR TYR B . n 
B 2 534 PRO 534 838  838  PRO PRO B . n 
B 2 535 GLU 535 839  839  GLU GLU B . n 
B 2 536 GLU 536 840  840  GLU GLU B . n 
B 2 537 ALA 537 841  841  ALA ALA B . n 
B 2 538 GLU 538 842  842  GLU GLU B . n 
B 2 539 PRO 539 843  843  PRO PRO B . n 
B 2 540 LYS 540 844  844  LYS LYS B . n 
B 2 541 GLN 541 845  845  GLN GLN B . n 
B 2 542 GLY 542 846  846  GLY GLY B . n 
B 2 543 ARG 543 847  847  ARG ARG B . n 
B 2 544 ILE 544 848  848  ILE ILE B . n 
B 2 545 VAL 545 849  849  VAL VAL B . n 
B 2 546 VAL 546 850  850  VAL VAL B . n 
B 2 547 PHE 547 851  851  PHE PHE B . n 
B 2 548 GLN 548 852  852  GLN GLN B . n 
B 2 549 TYR 549 853  853  TYR TYR B . n 
B 2 550 SER 550 854  854  SER SER B . n 
B 2 551 ASP 551 855  855  ASP ASP B . n 
B 2 552 GLY 552 856  856  GLY GLY B . n 
B 2 553 LYS 553 857  857  LYS LYS B . n 
B 2 554 LEU 554 858  858  LEU LEU B . n 
B 2 555 GLN 555 859  859  GLN GLN B . n 
B 2 556 THR 556 860  860  THR THR B . n 
B 2 557 VAL 557 861  861  VAL VAL B . n 
B 2 558 ALA 558 862  862  ALA ALA B . n 
B 2 559 GLU 559 863  863  GLU GLU B . n 
B 2 560 LYS 560 864  864  LYS LYS B . n 
B 2 561 GLU 561 865  865  GLU GLU B . n 
B 2 562 VAL 562 866  866  VAL VAL B . n 
B 2 563 LYS 563 867  867  LYS LYS B . n 
B 2 564 GLY 564 868  868  GLY GLY B . n 
B 2 565 ALA 565 869  869  ALA ALA B . n 
B 2 566 VAL 566 870  870  VAL VAL B . n 
B 2 567 TYR 567 871  871  TYR TYR B . n 
B 2 568 SER 568 872  872  SER SER B . n 
B 2 569 MET 569 873  873  MET MET B . n 
B 2 570 VAL 570 874  874  VAL VAL B . n 
B 2 571 GLU 571 875  875  GLU GLU B . n 
B 2 572 PHE 572 876  876  PHE PHE B . n 
B 2 573 ASN 573 877  877  ASN ASN B . n 
B 2 574 GLY 574 878  878  GLY GLY B . n 
B 2 575 LYS 575 879  879  LYS LYS B . n 
B 2 576 LEU 576 880  880  LEU LEU B . n 
B 2 577 LEU 577 881  881  LEU LEU B . n 
B 2 578 ALA 578 882  882  ALA ALA B . n 
B 2 579 SER 579 883  883  SER SER B . n 
B 2 580 ILE 580 884  884  ILE ILE B . n 
B 2 581 ASN 581 885  885  ASN ASN B . n 
B 2 582 SER 582 886  886  SER SER B . n 
B 2 583 THR 583 887  887  THR THR B . n 
B 2 584 VAL 584 888  888  VAL VAL B . n 
B 2 585 ARG 585 889  889  ARG ARG B . n 
B 2 586 LEU 586 890  890  LEU LEU B . n 
B 2 587 TYR 587 891  891  TYR TYR B . n 
B 2 588 GLU 588 892  892  GLU GLU B . n 
B 2 589 TRP 589 893  893  TRP TRP B . n 
B 2 590 THR 590 894  894  THR THR B . n 
B 2 591 THR 591 895  895  THR THR B . n 
B 2 592 GLU 592 896  896  GLU GLU B . n 
B 2 593 LYS 593 897  897  LYS LYS B . n 
B 2 594 GLU 594 898  898  GLU GLU B . n 
B 2 595 LEU 595 899  899  LEU LEU B . n 
B 2 596 ARG 596 900  900  ARG ARG B . n 
B 2 597 THR 597 901  901  THR THR B . n 
B 2 598 GLU 598 902  902  GLU GLU B . n 
B 2 599 CYS 599 903  903  CYS CYS B . n 
B 2 600 ASN 600 904  904  ASN ASN B . n 
B 2 601 HIS 601 905  905  HIS HIS B . n 
B 2 602 TYR 602 906  906  TYR TYR B . n 
B 2 603 ASN 603 907  907  ASN ASN B . n 
B 2 604 ASN 604 908  908  ASN ASN B . n 
B 2 605 ILE 605 909  909  ILE ILE B . n 
B 2 606 MET 606 910  910  MET MET B . n 
B 2 607 ALA 607 911  911  ALA ALA B . n 
B 2 608 LEU 608 912  912  LEU LEU B . n 
B 2 609 TYR 609 913  913  TYR TYR B . n 
B 2 610 LEU 610 914  914  LEU LEU B . n 
B 2 611 LYS 611 915  915  LYS LYS B . n 
B 2 612 THR 612 916  916  THR THR B . n 
B 2 613 LYS 613 917  917  LYS LYS B . n 
B 2 614 GLY 614 918  918  GLY GLY B . n 
B 2 615 ASP 615 919  919  ASP ASP B . n 
B 2 616 PHE 616 920  920  PHE PHE B . n 
B 2 617 ILE 617 921  921  ILE ILE B . n 
B 2 618 LEU 618 922  922  LEU LEU B . n 
B 2 619 VAL 619 923  923  VAL VAL B . n 
B 2 620 GLY 620 924  924  GLY GLY B . n 
B 2 621 ASP 621 925  925  ASP ASP B . n 
B 2 622 LEU 622 926  926  LEU LEU B . n 
B 2 623 MET 623 927  927  MET MET B . n 
B 2 624 ARG 624 928  928  ARG ARG B . n 
B 2 625 SER 625 929  929  SER SER B . n 
B 2 626 VAL 626 930  930  VAL VAL B . n 
B 2 627 LEU 627 931  931  LEU LEU B . n 
B 2 628 LEU 628 932  932  LEU LEU B . n 
B 2 629 LEU 629 933  933  LEU LEU B . n 
B 2 630 ALA 630 934  934  ALA ALA B . n 
B 2 631 TYR 631 935  935  TYR TYR B . n 
B 2 632 LYS 632 936  936  LYS LYS B . n 
B 2 633 PRO 633 937  937  PRO PRO B . n 
B 2 634 MET 634 938  938  MET MET B . n 
B 2 635 GLU 635 939  939  GLU GLU B . n 
B 2 636 GLY 636 940  940  GLY GLY B . n 
B 2 637 ASN 637 941  941  ASN ASN B . n 
B 2 638 PHE 638 942  942  PHE PHE B . n 
B 2 639 GLU 639 943  943  GLU GLU B . n 
B 2 640 GLU 640 944  944  GLU GLU B . n 
B 2 641 ILE 641 945  945  ILE ILE B . n 
B 2 642 ALA 642 946  946  ALA ALA B . n 
B 2 643 ARG 643 947  947  ARG ARG B . n 
B 2 644 ASP 644 948  948  ASP ASP B . n 
B 2 645 PHE 645 949  949  PHE PHE B . n 
B 2 646 ASN 646 950  950  ASN ASN B . n 
B 2 647 PRO 647 951  951  PRO PRO B . n 
B 2 648 ASN 648 952  952  ASN ASN B . n 
B 2 649 TRP 649 953  953  TRP TRP B . n 
B 2 650 MET 650 954  954  MET MET B . n 
B 2 651 SER 651 955  955  SER SER B . n 
B 2 652 ALA 652 956  956  ALA ALA B . n 
B 2 653 VAL 653 957  957  VAL VAL B . n 
B 2 654 GLU 654 958  958  GLU GLU B . n 
B 2 655 ILE 655 959  959  ILE ILE B . n 
B 2 656 LEU 656 960  960  LEU LEU B . n 
B 2 657 ASP 657 961  961  ASP ASP B . n 
B 2 658 ASP 658 962  962  ASP ASP B . n 
B 2 659 ASP 659 963  963  ASP ASP B . n 
B 2 660 ASN 660 964  964  ASN ASN B . n 
B 2 661 PHE 661 965  965  PHE PHE B . n 
B 2 662 LEU 662 966  966  LEU LEU B . n 
B 2 663 GLY 663 967  967  GLY GLY B . n 
B 2 664 ALA 664 968  968  ALA ALA B . n 
B 2 665 GLU 665 969  969  GLU GLU B . n 
B 2 666 ASN 666 970  970  ASN ASN B . n 
B 2 667 ALA 667 971  971  ALA ALA B . n 
B 2 668 PHE 668 972  972  PHE PHE B . n 
B 2 669 ASN 669 973  973  ASN ASN B . n 
B 2 670 LEU 670 974  974  LEU LEU B . n 
B 2 671 PHE 671 975  975  PHE PHE B . n 
B 2 672 VAL 672 976  976  VAL VAL B . n 
B 2 673 CYS 673 977  977  CYS CYS B . n 
B 2 674 GLN 674 978  978  GLN GLN B . n 
B 2 675 LYS 675 979  979  LYS LYS B . n 
B 2 676 ASP 676 980  980  ASP ASP B . n 
B 2 677 SER 677 981  981  SER SER B . n 
B 2 678 ALA 678 982  982  ALA ALA B . n 
B 2 679 ALA 679 983  983  ALA ALA B . n 
B 2 680 THR 680 984  984  THR THR B . n 
B 2 681 THR 681 985  985  THR THR B . n 
B 2 682 ASP 682 986  986  ASP ASP B . n 
B 2 683 GLU 683 987  987  GLU GLU B . n 
B 2 684 GLU 684 988  988  GLU GLU B . n 
B 2 685 ARG 685 989  989  ARG ARG B . n 
B 2 686 GLN 686 990  990  GLN GLN B . n 
B 2 687 HIS 687 991  991  HIS HIS B . n 
B 2 688 LEU 688 992  992  LEU LEU B . n 
B 2 689 GLN 689 993  993  GLN GLN B . n 
B 2 690 GLU 690 994  994  GLU GLU B . n 
B 2 691 VAL 691 995  995  VAL VAL B . n 
B 2 692 GLY 692 996  996  GLY GLY B . n 
B 2 693 LEU 693 997  997  LEU LEU B . n 
B 2 694 PHE 694 998  998  PHE PHE B . n 
B 2 695 HIS 695 999  999  HIS HIS B . n 
B 2 696 LEU 696 1000 1000 LEU LEU B . n 
B 2 697 GLY 697 1001 1001 GLY GLY B . n 
B 2 698 GLU 698 1002 1002 GLU GLU B . n 
B 2 699 PHE 699 1003 1003 PHE PHE B . n 
B 2 700 VAL 700 1004 1004 VAL VAL B . n 
B 2 701 ASN 701 1005 1005 ASN ASN B . n 
B 2 702 VAL 702 1006 1006 VAL VAL B . n 
B 2 703 PHE 703 1007 1007 PHE PHE B . n 
B 2 704 CYS 704 1008 1008 CYS CYS B . n 
B 2 705 HIS 705 1009 1009 HIS HIS B . n 
B 2 706 GLY 706 1010 1010 GLY GLY B . n 
B 2 707 SER 707 1011 1011 SER SER B . n 
B 2 708 LEU 708 1012 1012 LEU LEU B . n 
B 2 709 VAL 709 1013 1013 VAL VAL B . n 
B 2 710 MET 710 1014 1014 MET MET B . n 
B 2 711 GLN 711 1015 ?    ?   ?   B . n 
B 2 712 ASN 712 1016 ?    ?   ?   B . n 
B 2 713 LEU 713 1017 ?    ?   ?   B . n 
B 2 714 GLY 714 1018 ?    ?   ?   B . n 
B 2 715 GLU 715 1019 ?    ?   ?   B . n 
B 2 716 THR 716 1020 ?    ?   ?   B . n 
B 2 717 SER 717 1021 ?    ?   ?   B . n 
B 2 718 THR 718 1022 ?    ?   ?   B . n 
B 2 719 PRO 719 1023 1023 PRO PRO B . n 
B 2 720 THR 720 1024 1024 THR THR B . n 
B 2 721 GLN 721 1025 1025 GLN GLN B . n 
B 2 722 GLY 722 1026 1026 GLY GLY B . n 
B 2 723 SER 723 1027 1027 SER SER B . n 
B 2 724 VAL 724 1028 1028 VAL VAL B . n 
B 2 725 LEU 725 1029 1029 LEU LEU B . n 
B 2 726 PHE 726 1030 1030 PHE PHE B . n 
B 2 727 GLY 727 1031 1031 GLY GLY B . n 
B 2 728 THR 728 1032 1032 THR THR B . n 
B 2 729 VAL 729 1033 1033 VAL VAL B . n 
B 2 730 ASN 730 1034 1034 ASN ASN B . n 
B 2 731 GLY 731 1035 1035 GLY GLY B . n 
B 2 732 MET 732 1036 1036 MET MET B . n 
B 2 733 ILE 733 1037 1037 ILE ILE B . n 
B 2 734 GLY 734 1038 1038 GLY GLY B . n 
B 2 735 LEU 735 1039 1039 LEU LEU B . n 
B 2 736 VAL 736 1040 1040 VAL VAL B . n 
B 2 737 THR 737 1041 1041 THR THR B . n 
B 2 738 SER 738 1042 1042 SER SER B . n 
B 2 739 LEU 739 1043 1043 LEU LEU B . n 
B 2 740 SER 740 1044 1044 SER SER B . n 
B 2 741 GLU 741 1045 1045 GLU GLU B . n 
B 2 742 SER 742 1046 1046 SER SER B . n 
B 2 743 TRP 743 1047 1047 TRP TRP B . n 
B 2 744 TYR 744 1048 1048 TYR TYR B . n 
B 2 745 ASN 745 1049 1049 ASN ASN B . n 
B 2 746 LEU 746 1050 1050 LEU LEU B . n 
B 2 747 LEU 747 1051 1051 LEU LEU B . n 
B 2 748 LEU 748 1052 1052 LEU LEU B . n 
B 2 749 ASP 749 1053 1053 ASP ASP B . n 
B 2 750 MET 750 1054 1054 MET MET B . n 
B 2 751 GLN 751 1055 1055 GLN GLN B . n 
B 2 752 ASN 752 1056 1056 ASN ASN B . n 
B 2 753 ARG 753 1057 1057 ARG ARG B . n 
B 2 754 LEU 754 1058 1058 LEU LEU B . n 
B 2 755 ASN 755 1059 1059 ASN ASN B . n 
B 2 756 LYS 756 1060 1060 LYS LYS B . n 
B 2 757 VAL 757 1061 1061 VAL VAL B . n 
B 2 758 ILE 758 1062 1062 ILE ILE B . n 
B 2 759 LYS 759 1063 1063 LYS LYS B . n 
B 2 760 SER 760 1064 1064 SER SER B . n 
B 2 761 VAL 761 1065 1065 VAL VAL B . n 
B 2 762 GLY 762 1066 1066 GLY GLY B . n 
B 2 763 LYS 763 1067 1067 LYS LYS B . n 
B 2 764 ILE 764 1068 1068 ILE ILE B . n 
B 2 765 GLU 765 1069 1069 GLU GLU B . n 
B 2 766 HIS 766 1070 1070 HIS HIS B . n 
B 2 767 SER 767 1071 1071 SER SER B . n 
B 2 768 PHE 768 1072 1072 PHE PHE B . n 
B 2 769 TRP 769 1073 1073 TRP TRP B . n 
B 2 770 ARG 770 1074 1074 ARG ARG B . n 
B 2 771 SER 771 1075 1075 SER SER B . n 
B 2 772 PHE 772 1076 1076 PHE PHE B . n 
B 2 773 HIS 773 1077 1077 HIS HIS B . n 
B 2 774 THR 774 1078 1078 THR THR B . n 
B 2 775 GLU 775 1079 1079 GLU GLU B . n 
B 2 776 ARG 776 1080 1080 ARG ARG B . n 
B 2 777 LYS 777 1081 1081 LYS LYS B . n 
B 2 778 THR 778 1082 1082 THR THR B . n 
B 2 779 GLU 779 1083 1083 GLU GLU B . n 
B 2 780 PRO 780 1084 1084 PRO PRO B . n 
B 2 781 ALA 781 1085 1085 ALA ALA B . n 
B 2 782 THR 782 1086 1086 THR THR B . n 
B 2 783 GLY 783 1087 1087 GLY GLY B . n 
B 2 784 PHE 784 1088 1088 PHE PHE B . n 
B 2 785 ILE 785 1089 1089 ILE ILE B . n 
B 2 786 ASP 786 1090 1090 ASP ASP B . n 
B 2 787 GLY 787 1091 1091 GLY GLY B . n 
B 2 788 ASP 788 1092 1092 ASP ASP B . n 
B 2 789 LEU 789 1093 1093 LEU LEU B . n 
B 2 790 ILE 790 1094 1094 ILE ILE B . n 
B 2 791 GLU 791 1095 1095 GLU GLU B . n 
B 2 792 SER 792 1096 1096 SER SER B . n 
B 2 793 PHE 793 1097 1097 PHE PHE B . n 
B 2 794 LEU 794 1098 1098 LEU LEU B . n 
B 2 795 ASP 795 1099 1099 ASP ASP B . n 
B 2 796 ILE 796 1100 1100 ILE ILE B . n 
B 2 797 SER 797 1101 1101 SER SER B . n 
B 2 798 ARG 798 1102 1102 ARG ARG B . n 
B 2 799 PRO 799 1103 1103 PRO PRO B . n 
B 2 800 LYS 800 1104 1104 LYS LYS B . n 
B 2 801 MET 801 1105 1105 MET MET B . n 
B 2 802 GLN 802 1106 1106 GLN GLN B . n 
B 2 803 GLU 803 1107 1107 GLU GLU B . n 
B 2 804 VAL 804 1108 1108 VAL VAL B . n 
B 2 805 VAL 805 1109 1109 VAL VAL B . n 
B 2 806 ALA 806 1110 1110 ALA ALA B . n 
B 2 807 ASN 807 1111 1111 ASN ASN B . n 
B 2 808 LEU 808 1112 1112 LEU LEU B . n 
B 2 809 GLN 809 1113 1113 GLN GLN B . n 
B 2 810 TYR 810 1114 ?    ?   ?   B . n 
B 2 811 ASP 811 1115 ?    ?   ?   B . n 
B 2 812 ASP 812 1116 ?    ?   ?   B . n 
B 2 813 GLY 813 1117 ?    ?   ?   B . n 
B 2 814 SER 814 1118 ?    ?   ?   B . n 
B 2 815 GLY 815 1119 ?    ?   ?   B . n 
B 2 816 MET 816 1120 ?    ?   ?   B . n 
B 2 817 LYS 817 1121 ?    ?   ?   B . n 
B 2 818 ARG 818 1122 ?    ?   ?   B . n 
B 2 819 GLU 819 1123 1123 GLU GLU B . n 
B 2 820 ALA 820 1124 1124 ALA ALA B . n 
B 2 821 THR 821 1125 1125 THR THR B . n 
B 2 822 ALA 822 1126 1126 ALA ALA B . n 
B 2 823 ASP 823 1127 1127 ASP ASP B . n 
B 2 824 ASP 824 1128 1128 ASP ASP B . n 
B 2 825 LEU 825 1129 1129 LEU LEU B . n 
B 2 826 ILE 826 1130 1130 ILE ILE B . n 
B 2 827 LYS 827 1131 1131 LYS LYS B . n 
B 2 828 VAL 828 1132 1132 VAL VAL B . n 
B 2 829 VAL 829 1133 1133 VAL VAL B . n 
B 2 830 GLU 830 1134 1134 GLU GLU B . n 
B 2 831 GLU 831 1135 1135 GLU GLU B . n 
B 2 832 LEU 832 1136 1136 LEU LEU B . n 
B 2 833 THR 833 1137 1137 THR THR B . n 
B 2 834 ARG 834 1138 1138 ARG ARG B . n 
B 2 835 ILE 835 1139 1139 ILE ILE B . n 
B 2 836 HIS 836 1140 1140 HIS HIS B . n 
C 3 1   SER 1   866  ?    ?   ?   C . n 
C 3 2   GLN 2   867  ?    ?   ?   C . n 
C 3 3   SER 3   868  868  SER SER C . n 
C 3 4   LEU 4   869  869  LEU LEU C . n 
C 3 5   THR 5   870  870  THR THR C . n 
C 3 6   THR 6   871  871  THR THR C . n 
C 3 7   CYS 7   872  872  CYS CYS C . n 
C 3 8   GLU 8   873  873  GLU GLU C . n 
C 3 9   VAL 9   874  874  VAL VAL C . n 
C 3 10  CYS 10  875  875  CYS CYS C . n 
C 3 11  GLY 11  876  876  GLY GLY C . n 
C 3 12  ALA 12  877  877  ALA ALA C . n 
C 3 13  CYS 13  878  878  CYS CYS C . n 
C 3 14  PHE 14  879  879  PHE PHE C . n 
C 3 15  GLU 15  880  880  GLU GLU C . n 
C 3 16  THR 16  881  881  THR THR C . n 
C 3 17  ARG 17  882  882  ARG ARG C . n 
C 3 18  LYS 18  883  883  LYS LYS C . n 
C 3 19  GLY 19  884  884  GLY GLY C . n 
C 3 20  LEU 20  885  885  LEU LEU C . n 
C 3 21  SER 21  886  886  SER SER C . n 
C 3 22  SER 22  887  887  SER SER C . n 
C 3 23  HIS 23  888  888  HIS HIS C . n 
C 3 24  ALA 24  889  889  ALA ALA C . n 
C 3 25  ARG 25  890  890  ARG ARG C . n 
C 3 26  SER 26  891  891  SER SER C . n 
C 3 27  HIS 27  892  892  HIS HIS C . n 
C 3 28  LEU 28  893  893  LEU LEU C . n 
C 3 29  ARG 29  894  ?    ?   ?   C . n 
C 3 30  GLN 30  895  ?    ?   ?   C . n 
D 1 1   ARG 1   70   ?    ?   ?   D . n 
D 1 2   THR 2   71   ?    ?   ?   D . n 
D 1 3   LEU 3   72   ?    ?   ?   D . n 
D 1 4   HIS 4   73   73   HIS HIS D . n 
D 1 5   ASP 5   74   74   ASP ASP D . n 
D 1 6   ASP 6   75   75   ASP ASP D . n 
D 1 7   ASP 7   76   76   ASP ASP D . n 
D 1 8   SER 8   77   77   SER SER D . n 
D 1 9   CYS 9   78   78   CYS CYS D . n 
D 1 10  GLN 10  79   79   GLN GLN D . n 
D 1 11  VAL 11  80   80   VAL VAL D . n 
D 1 12  ILE 12  81   81   ILE ILE D . n 
D 1 13  PRO 13  82   82   PRO PRO D . n 
D 1 14  VAL 14  83   83   VAL VAL D . n 
D 1 15  LEU 15  84   84   LEU LEU D . n 
D 1 16  PRO 16  85   85   PRO PRO D . n 
D 1 17  GLN 17  86   86   GLN GLN D . n 
D 1 18  VAL 18  87   87   VAL VAL D . n 
D 1 19  MET 19  88   88   MET MET D . n 
D 1 20  MET 20  89   89   MET MET D . n 
D 1 21  ILE 21  90   90   ILE ILE D . n 
D 1 22  LEU 22  91   91   LEU LEU D . n 
D 1 23  ILE 23  92   92   ILE ILE D . n 
D 1 24  PRO 24  93   93   PRO PRO D . n 
D 1 25  GLY 25  94   94   GLY GLY D . n 
D 1 26  GLN 26  95   95   GLN GLN D . n 
D 1 27  THR 27  96   96   THR THR D . n 
D 1 28  LEU 28  97   97   LEU LEU D . n 
D 1 29  PRO 29  98   98   PRO PRO D . n 
D 1 30  LEU 30  99   99   LEU LEU D . n 
D 1 31  GLN 31  100  100  GLN GLN D . n 
D 1 32  LEU 32  101  101  LEU LEU D . n 
D 1 33  PHE 33  102  102  PHE PHE D . n 
D 1 34  HIS 34  103  103  HIS HIS D . n 
D 1 35  PRO 35  104  104  PRO PRO D . n 
D 1 36  GLN 36  105  105  GLN GLN D . n 
D 1 37  GLU 37  106  106  GLU GLU D . n 
D 1 38  VAL 38  107  107  VAL VAL D . n 
D 1 39  SER 39  108  108  SER SER D . n 
D 1 40  MET 40  109  109  MET MET D . n 
D 1 41  VAL 41  110  110  VAL VAL D . n 
D 1 42  ARG 42  111  111  ARG ARG D . n 
D 1 43  ASN 43  112  112  ASN ASN D . n 
D 1 44  LEU 44  113  113  LEU LEU D . n 
D 1 45  ILE 45  114  114  ILE ILE D . n 
D 1 46  GLN 46  115  115  GLN GLN D . n 
D 1 47  LYS 47  116  116  LYS LYS D . n 
D 1 48  ASP 48  117  117  ASP ASP D . n 
D 1 49  ARG 49  118  118  ARG ARG D . n 
D 1 50  THR 50  119  119  THR THR D . n 
D 1 51  PHE 51  120  120  PHE PHE D . n 
D 1 52  ALA 52  121  121  ALA ALA D . n 
D 1 53  VAL 53  122  122  VAL VAL D . n 
D 1 54  LEU 54  123  123  LEU LEU D . n 
D 1 55  ALA 55  124  124  ALA ALA D . n 
D 1 56  TYR 56  125  125  TYR TYR D . n 
D 1 57  SER 57  126  ?    ?   ?   D . n 
D 1 58  ASN 58  127  ?    ?   ?   D . n 
D 1 59  VAL 59  128  ?    ?   ?   D . n 
D 1 60  GLN 60  129  ?    ?   ?   D . n 
D 1 61  GLU 61  130  ?    ?   ?   D . n 
D 1 62  ARG 62  131  ?    ?   ?   D . n 
D 1 63  GLU 63  132  ?    ?   ?   D . n 
D 1 64  ALA 64  133  133  ALA ALA D . n 
D 1 65  GLN 65  134  134  GLN GLN D . n 
D 1 66  PHE 66  135  135  PHE PHE D . n 
D 1 67  GLY 67  136  136  GLY GLY D . n 
D 1 68  THR 68  137  137  THR THR D . n 
D 1 69  THR 69  138  138  THR THR D . n 
D 1 70  ALA 70  139  139  ALA ALA D . n 
D 1 71  GLU 71  140  140  GLU GLU D . n 
D 1 72  ILE 72  141  141  ILE ILE D . n 
D 1 73  TYR 73  142  142  TYR TYR D . n 
D 1 74  ALA 74  143  143  ALA ALA D . n 
D 1 75  TYR 75  144  144  TYR TYR D . n 
D 1 76  ARG 76  145  145  ARG ARG D . n 
D 1 77  GLU 77  146  146  GLU GLU D . n 
D 1 78  GLU 78  147  147  GLU GLU D . n 
D 1 79  GLN 79  148  148  GLN GLN D . n 
D 1 80  ASP 80  149  149  ASP ASP D . n 
D 1 81  PHE 81  150  150  PHE PHE D . n 
D 1 82  GLY 82  151  151  GLY GLY D . n 
D 1 83  ILE 83  152  152  ILE ILE D . n 
D 1 84  GLU 84  153  153  GLU GLU D . n 
D 1 85  ILE 85  154  154  ILE ILE D . n 
D 1 86  VAL 86  155  155  VAL VAL D . n 
D 1 87  LYS 87  156  156  LYS LYS D . n 
D 1 88  VAL 88  157  157  VAL VAL D . n 
D 1 89  LYS 89  158  158  LYS LYS D . n 
D 1 90  ALA 90  159  159  ALA ALA D . n 
D 1 91  ILE 91  160  160  ILE ILE D . n 
D 1 92  GLY 92  161  161  GLY GLY D . n 
D 1 93  ARG 93  162  162  ARG ARG D . n 
D 1 94  GLN 94  163  163  GLN GLN D . n 
D 1 95  ARG 95  164  164  ARG ARG D . n 
D 1 96  PHE 96  165  165  PHE PHE D . n 
D 1 97  LYS 97  166  166  LYS LYS D . n 
D 1 98  VAL 98  167  167  VAL VAL D . n 
D 1 99  LEU 99  168  168  LEU LEU D . n 
D 1 100 GLU 100 169  169  GLU GLU D . n 
D 1 101 LEU 101 170  170  LEU LEU D . n 
D 1 102 ARG 102 171  171  ARG ARG D . n 
D 1 103 THR 103 172  172  THR THR D . n 
D 1 104 GLN 104 173  173  GLN GLN D . n 
D 1 105 SER 105 174  174  SER SER D . n 
D 1 106 ASP 106 175  175  ASP ASP D . n 
D 1 107 GLY 107 176  176  GLY GLY D . n 
D 1 108 ILE 108 177  177  ILE ILE D . n 
D 1 109 GLN 109 178  178  GLN GLN D . n 
D 1 110 GLN 110 179  179  GLN GLN D . n 
D 1 111 ALA 111 180  180  ALA ALA D . n 
D 1 112 LYS 112 181  181  LYS LYS D . n 
D 1 113 VAL 113 182  182  VAL VAL D . n 
D 1 114 GLN 114 183  183  GLN GLN D . n 
D 1 115 ILE 115 184  184  ILE ILE D . n 
D 1 116 LEU 116 185  185  LEU LEU D . n 
D 1 117 PRO 117 186  186  PRO PRO D . n 
D 1 118 GLU 118 187  187  GLU GLU D . n 
D 1 119 CYS 119 188  188  CYS CYS D . n 
D 1 120 VAL 120 189  189  VAL VAL D . n 
D 1 121 LEU 121 190  190  LEU LEU D . n 
D 1 122 PRO 122 191  191  PRO PRO D . n 
D 1 123 SER 123 192  192  SER SER D . n 
D 1 124 THR 124 193  193  THR THR D . n 
D 1 125 MET 125 194  194  MET MET D . n 
D 1 126 SER 126 195  195  SER SER D . n 
D 1 127 ALA 127 196  196  ALA ALA D . n 
D 1 128 VAL 128 197  197  VAL VAL D . n 
D 1 129 GLN 129 198  198  GLN GLN D . n 
D 1 130 LEU 130 199  199  LEU LEU D . n 
D 1 131 GLU 131 200  200  GLU GLU D . n 
D 1 132 SER 132 201  201  SER SER D . n 
D 1 133 LEU 133 202  202  LEU LEU D . n 
D 1 134 ASN 134 203  203  ASN ASN D . n 
D 1 135 LYS 135 204  204  LYS LYS D . n 
D 1 136 CYS 136 205  205  CYS CYS D . n 
D 1 137 GLN 137 206  206  GLN GLN D . n 
D 1 138 ILE 138 207  207  ILE ILE D . n 
D 1 139 PHE 139 208  208  PHE PHE D . n 
D 1 140 PRO 140 209  209  PRO PRO D . n 
D 1 141 SER 141 210  210  SER SER D . n 
D 1 142 LYS 142 211  211  LYS LYS D . n 
D 1 143 PRO 143 212  212  PRO PRO D . n 
D 1 144 VAL 144 213  213  VAL VAL D . n 
D 1 145 SER 145 214  ?    ?   ?   D . n 
D 1 146 ARG 146 215  ?    ?   ?   D . n 
D 1 147 GLU 147 216  ?    ?   ?   D . n 
D 1 148 ASP 148 217  ?    ?   ?   D . n 
D 1 149 GLN 149 218  ?    ?   ?   D . n 
D 1 150 CYS 150 219  ?    ?   ?   D . n 
D 1 151 SER 151 220  220  SER SER D . n 
D 1 152 TYR 152 221  221  TYR TYR D . n 
D 1 153 LYS 153 222  222  LYS LYS D . n 
D 1 154 TRP 154 223  223  TRP TRP D . n 
D 1 155 TRP 155 224  224  TRP TRP D . n 
D 1 156 GLN 156 225  225  GLN GLN D . n 
D 1 157 LYS 157 226  226  LYS LYS D . n 
D 1 158 TYR 158 227  227  TYR TYR D . n 
D 1 159 GLN 159 228  228  GLN GLN D . n 
D 1 160 LYS 160 229  229  LYS LYS D . n 
D 1 161 ARG 161 230  230  ARG ARG D . n 
D 1 162 LYS 162 231  231  LYS LYS D . n 
D 1 163 PHE 163 232  232  PHE PHE D . n 
D 1 164 HIS 164 233  233  HIS HIS D . n 
D 1 165 CYS 165 234  234  CYS CYS D . n 
D 1 166 ALA 166 235  235  ALA ALA D . n 
D 1 167 ASN 167 236  236  ASN ASN D . n 
D 1 168 LEU 168 237  237  LEU LEU D . n 
D 1 169 THR 169 238  238  THR THR D . n 
D 1 170 SER 170 239  239  SER SER D . n 
D 1 171 TRP 171 240  240  TRP TRP D . n 
D 1 172 PRO 172 241  241  PRO PRO D . n 
D 1 173 ARG 173 242  242  ARG ARG D . n 
D 1 174 TRP 174 243  243  TRP TRP D . n 
D 1 175 LEU 175 244  244  LEU LEU D . n 
D 1 176 TYR 176 245  245  TYR TYR D . n 
D 1 177 SER 177 246  246  SER SER D . n 
D 1 178 LEU 178 247  247  LEU LEU D . n 
D 1 179 TYR 179 248  248  TYR TYR D . n 
D 1 180 ASP 180 249  249  ASP ASP D . n 
D 1 181 ALA 181 250  250  ALA ALA D . n 
D 1 182 GLU 182 251  251  GLU GLU D . n 
D 1 183 THR 183 252  252  THR THR D . n 
D 1 184 LEU 184 253  253  LEU LEU D . n 
D 1 185 MET 185 254  254  MET MET D . n 
D 1 186 ASP 186 255  255  ASP ASP D . n 
D 1 187 ARG 187 256  256  ARG ARG D . n 
D 1 188 ILE 188 257  257  ILE ILE D . n 
D 1 189 LYS 189 258  258  LYS LYS D . n 
D 1 190 LYS 190 259  259  LYS LYS D . n 
D 1 191 GLN 191 260  260  GLN GLN D . n 
D 1 192 LEU 192 261  261  LEU LEU D . n 
D 1 193 ARG 193 262  262  ARG ARG D . n 
D 1 194 GLU 194 263  263  GLU GLU D . n 
D 1 195 TRP 195 264  264  TRP TRP D . n 
D 1 196 ASP 196 265  265  ASP ASP D . n 
D 1 197 GLU 197 266  266  GLU GLU D . n 
D 1 198 ASN 198 267  267  ASN ASN D . n 
D 1 199 LEU 199 268  268  LEU LEU D . n 
D 1 200 LYS 200 269  269  LYS LYS D . n 
D 1 201 ASP 201 270  270  ASP ASP D . n 
D 1 202 ASP 202 271  271  ASP ASP D . n 
D 1 203 SER 203 272  272  SER SER D . n 
D 1 204 LEU 204 273  273  LEU LEU D . n 
D 1 205 PRO 205 274  274  PRO PRO D . n 
D 1 206 SER 206 275  275  SER SER D . n 
D 1 207 ASN 207 276  276  ASN ASN D . n 
D 1 208 PRO 208 277  277  PRO PRO D . n 
D 1 209 ILE 209 278  278  ILE ILE D . n 
D 1 210 ASP 210 279  279  ASP ASP D . n 
D 1 211 PHE 211 280  280  PHE PHE D . n 
D 1 212 SER 212 281  281  SER SER D . n 
D 1 213 TYR 213 282  282  TYR TYR D . n 
D 1 214 ARG 214 283  283  ARG ARG D . n 
D 1 215 VAL 215 284  284  VAL VAL D . n 
D 1 216 ALA 216 285  285  ALA ALA D . n 
D 1 217 ALA 217 286  286  ALA ALA D . n 
D 1 218 CYS 218 287  287  CYS CYS D . n 
D 1 219 LEU 219 288  288  LEU LEU D . n 
D 1 220 PRO 220 289  289  PRO PRO D . n 
D 1 221 ILE 221 290  290  ILE ILE D . n 
D 1 222 ASP 222 291  291  ASP ASP D . n 
D 1 223 ASP 223 292  292  ASP ASP D . n 
D 1 224 VAL 224 293  293  VAL VAL D . n 
D 1 225 LEU 225 294  294  LEU LEU D . n 
D 1 226 ARG 226 295  295  ARG ARG D . n 
D 1 227 ILE 227 296  296  ILE ILE D . n 
D 1 228 GLN 228 297  297  GLN GLN D . n 
D 1 229 LEU 229 298  298  LEU LEU D . n 
D 1 230 LEU 230 299  299  LEU LEU D . n 
D 1 231 LYS 231 300  300  LYS LYS D . n 
D 1 232 ILE 232 301  301  ILE ILE D . n 
D 1 233 GLY 233 302  302  GLY GLY D . n 
D 1 234 SER 234 303  303  SER SER D . n 
D 1 235 ALA 235 304  304  ALA ALA D . n 
D 1 236 ILE 236 305  305  ILE ILE D . n 
D 1 237 GLN 237 306  306  GLN GLN D . n 
D 1 238 ARG 238 307  307  ARG ARG D . n 
D 1 239 LEU 239 308  308  LEU LEU D . n 
D 1 240 ARG 240 309  309  ARG ARG D . n 
D 1 241 CYS 241 310  310  CYS CYS D . n 
D 1 242 GLU 242 311  311  GLU GLU D . n 
D 1 243 LEU 243 312  312  LEU LEU D . n 
D 1 244 ASP 244 313  313  ASP ASP D . n 
D 1 245 ILE 245 314  314  ILE ILE D . n 
D 1 246 MET 246 315  315  MET MET D . n 
D 1 247 ASN 247 316  316  ASN ASN D . n 
D 1 248 LYS 248 317  317  LYS LYS D . n 
D 1 249 CYS 249 318  318  CYS CYS D . n 
D 1 250 THR 250 319  319  THR THR D . n 
D 1 251 SER 251 320  320  SER SER D . n 
D 1 252 LEU 252 321  321  LEU LEU D . n 
D 1 253 CYS 253 322  322  CYS CYS D . n 
D 1 254 CYS 254 323  323  CYS CYS D . n 
D 1 255 LYS 255 324  324  LYS LYS D . n 
D 1 256 GLN 256 325  325  GLN GLN D . n 
D 1 257 CYS 257 326  326  CYS CYS D . n 
D 1 258 GLN 258 327  327  GLN GLN D . n 
D 1 259 GLU 259 328  328  GLU GLU D . n 
D 1 260 THR 260 329  329  THR THR D . n 
D 1 261 GLU 261 330  330  GLU GLU D . n 
D 1 262 ILE 262 331  331  ILE ILE D . n 
D 1 263 THR 263 332  332  THR THR D . n 
D 1 264 THR 264 333  333  THR THR D . n 
D 1 265 LYS 265 334  334  LYS LYS D . n 
D 1 266 ASN 266 335  335  ASN ASN D . n 
D 1 267 GLU 267 336  336  GLU GLU D . n 
D 1 268 ILE 268 337  337  ILE ILE D . n 
D 1 269 PHE 269 338  338  PHE PHE D . n 
D 1 270 SER 270 339  339  SER SER D . n 
D 1 271 LEU 271 340  340  LEU LEU D . n 
D 1 272 SER 272 341  341  SER SER D . n 
D 1 273 LEU 273 342  342  LEU LEU D . n 
D 1 274 CYS 274 343  343  CYS CYS D . n 
D 1 275 GLY 275 344  344  GLY GLY D . n 
D 1 276 PRO 276 345  345  PRO PRO D . n 
D 1 277 MET 277 346  346  MET MET D . n 
D 1 278 ALA 278 347  347  ALA ALA D . n 
D 1 279 ALA 279 348  348  ALA ALA D . n 
D 1 280 TYR 280 349  349  TYR TYR D . n 
D 1 281 VAL 281 350  350  VAL VAL D . n 
D 1 282 ASN 282 351  351  ASN ASN D . n 
D 1 283 PRO 283 352  352  PRO PRO D . n 
D 1 284 HIS 284 353  353  HIS HIS D . n 
D 1 285 GLY 285 354  354  GLY GLY D . n 
D 1 286 TYR 286 355  355  TYR TYR D . n 
D 1 287 VAL 287 356  356  VAL VAL D . n 
D 1 288 HIS 288 357  357  HIS HIS D . n 
D 1 289 GLU 289 358  358  GLU GLU D . n 
D 1 290 THR 290 359  359  THR THR D . n 
D 1 291 LEU 291 360  360  LEU LEU D . n 
D 1 292 THR 292 361  361  THR THR D . n 
D 1 293 VAL 293 362  362  VAL VAL D . n 
D 1 294 TYR 294 363  363  TYR TYR D . n 
D 1 295 LYS 295 364  364  LYS LYS D . n 
D 1 296 ALA 296 365  365  ALA ALA D . n 
D 1 297 CYS 297 366  366  CYS CYS D . n 
D 1 298 ASN 298 367  367  ASN ASN D . n 
D 1 299 LEU 299 368  368  LEU LEU D . n 
D 1 300 ASN 300 369  369  ASN ASN D . n 
D 1 301 LEU 301 370  370  LEU LEU D . n 
D 1 302 ILE 302 371  371  ILE ILE D . n 
D 1 303 GLY 303 372  372  GLY GLY D . n 
D 1 304 ARG 304 373  373  ARG ARG D . n 
D 1 305 PRO 305 374  374  PRO PRO D . n 
D 1 306 SER 306 375  375  SER SER D . n 
D 1 307 THR 307 376  376  THR THR D . n 
D 1 308 GLU 308 377  377  GLU GLU D . n 
D 1 309 HIS 309 378  378  HIS HIS D . n 
D 1 310 SER 310 379  379  SER SER D . n 
D 1 311 TRP 311 380  380  TRP TRP D . n 
D 1 312 PHE 312 381  381  PHE PHE D . n 
D 1 313 PRO 313 382  382  PRO PRO D . n 
D 1 314 GLY 314 383  383  GLY GLY D . n 
D 1 315 TYR 315 384  384  TYR TYR D . n 
D 1 316 ALA 316 385  385  ALA ALA D . n 
D 1 317 TRP 317 386  386  TRP TRP D . n 
D 1 318 THR 318 387  387  THR THR D . n 
D 1 319 VAL 319 388  388  VAL VAL D . n 
D 1 320 ALA 320 389  389  ALA ALA D . n 
D 1 321 GLN 321 390  390  GLN GLN D . n 
D 1 322 CYS 322 391  391  CYS CYS D . n 
D 1 323 LYS 323 392  392  LYS LYS D . n 
D 1 324 ILE 324 393  393  ILE ILE D . n 
D 1 325 CYS 325 394  394  CYS CYS D . n 
D 1 326 ALA 326 395  395  ALA ALA D . n 
D 1 327 SER 327 396  396  SER SER D . n 
D 1 328 HIS 328 397  397  HIS HIS D . n 
D 1 329 ILE 329 398  398  ILE ILE D . n 
D 1 330 GLY 330 399  399  GLY GLY D . n 
D 1 331 TRP 331 400  400  TRP TRP D . n 
D 1 332 LYS 332 401  401  LYS LYS D . n 
D 1 333 PHE 333 402  402  PHE PHE D . n 
D 1 334 THR 334 403  403  THR THR D . n 
D 1 335 ALA 335 404  404  ALA ALA D . n 
D 1 336 THR 336 405  405  THR THR D . n 
D 1 337 LYS 337 406  406  LYS LYS D . n 
D 1 338 LYS 338 407  407  LYS LYS D . n 
D 1 339 ASP 339 408  408  ASP ASP D . n 
D 1 340 MET 340 409  409  MET MET D . n 
D 1 341 SER 341 410  410  SER SER D . n 
D 1 342 PRO 342 411  411  PRO PRO D . n 
D 1 343 GLN 343 412  412  GLN GLN D . n 
D 1 344 LYS 344 413  413  LYS LYS D . n 
D 1 345 PHE 345 414  414  PHE PHE D . n 
D 1 346 TRP 346 415  415  TRP TRP D . n 
D 1 347 GLY 347 416  416  GLY GLY D . n 
D 1 348 LEU 348 417  417  LEU LEU D . n 
D 1 349 THR 349 418  418  THR THR D . n 
D 1 350 ARG 350 419  419  ARG ARG D . n 
D 1 351 SER 351 420  420  SER SER D . n 
D 1 352 ALA 352 421  421  ALA ALA D . n 
D 1 353 LEU 353 422  422  LEU LEU D . n 
D 1 354 LEU 354 423  423  LEU LEU D . n 
D 1 355 PRO 355 424  424  PRO PRO D . n 
D 1 356 THR 356 425  425  THR THR D . n 
D 1 357 ILE 357 426  426  ILE ILE D . n 
D 1 358 PRO 358 427  427  PRO PRO D . n 
D 1 359 ASP 359 428  ?    ?   ?   D . n 
D 1 360 THR 360 429  ?    ?   ?   D . n 
D 1 361 GLU 361 430  ?    ?   ?   D . n 
D 1 362 ASP 362 431  ?    ?   ?   D . n 
D 1 363 GLU 363 432  ?    ?   ?   D . n 
D 1 364 ILE 364 433  ?    ?   ?   D . n 
D 1 365 SER 365 434  ?    ?   ?   D . n 
D 1 366 PRO 366 435  ?    ?   ?   D . n 
D 1 367 ASP 367 436  ?    ?   ?   D . n 
D 1 368 LYS 368 437  ?    ?   ?   D . n 
D 1 369 VAL 369 438  438  VAL VAL D . n 
D 1 370 ILE 370 439  439  ILE ILE D . n 
D 1 371 LEU 371 440  440  LEU LEU D . n 
D 1 372 CYS 372 441  441  CYS CYS D . n 
D 1 373 LEU 373 442  442  LEU LEU D . n 
E 2 1   MET 1   1    ?    ?   ?   E . n 
E 2 2   SER 2   2    2    SER SER E . n 
E 2 3   TYR 3   3    3    TYR TYR E . n 
E 2 4   ASN 4   4    4    ASN ASN E . n 
E 2 5   TYR 5   5    5    TYR TYR E . n 
E 2 6   VAL 6   6    6    VAL VAL E . n 
E 2 7   VAL 7   7    7    VAL VAL E . n 
E 2 8   THR 8   8    8    THR THR E . n 
E 2 9   ALA 9   9    9    ALA ALA E . n 
E 2 10  GLN 10  10   10   GLN GLN E . n 
E 2 11  LYS 11  11   11   LYS LYS E . n 
E 2 12  PRO 12  12   12   PRO PRO E . n 
E 2 13  THR 13  13   13   THR THR E . n 
E 2 14  ALA 14  14   14   ALA ALA E . n 
E 2 15  VAL 15  15   15   VAL VAL E . n 
E 2 16  ASN 16  16   16   ASN ASN E . n 
E 2 17  GLY 17  17   17   GLY GLY E . n 
E 2 18  CYS 18  18   18   CYS CYS E . n 
E 2 19  VAL 19  19   19   VAL VAL E . n 
E 2 20  THR 20  20   20   THR THR E . n 
E 2 21  GLY 21  21   21   GLY GLY E . n 
E 2 22  HIS 22  22   22   HIS HIS E . n 
E 2 23  PHE 23  23   23   PHE PHE E . n 
E 2 24  THR 24  24   24   THR THR E . n 
E 2 25  SER 25  25   25   SER SER E . n 
E 2 26  ALA 26  26   26   ALA ALA E . n 
E 2 27  GLU 27  27   27   GLU GLU E . n 
E 2 28  ASP 28  28   28   ASP ASP E . n 
E 2 29  LEU 29  29   29   LEU LEU E . n 
E 2 30  ASN 30  30   30   ASN ASN E . n 
E 2 31  LEU 31  31   31   LEU LEU E . n 
E 2 32  LEU 32  32   32   LEU LEU E . n 
E 2 33  ILE 33  33   33   ILE ILE E . n 
E 2 34  ALA 34  34   34   ALA ALA E . n 
E 2 35  LYS 35  35   35   LYS LYS E . n 
E 2 36  ASN 36  36   36   ASN ASN E . n 
E 2 37  THR 37  37   37   THR THR E . n 
E 2 38  ARG 38  38   38   ARG ARG E . n 
E 2 39  LEU 39  39   39   LEU LEU E . n 
E 2 40  GLU 40  40   40   GLU GLU E . n 
E 2 41  ILE 41  41   41   ILE ILE E . n 
E 2 42  TYR 42  42   42   TYR TYR E . n 
E 2 43  VAL 43  43   43   VAL VAL E . n 
E 2 44  VAL 44  44   44   VAL VAL E . n 
E 2 45  THR 45  45   45   THR THR E . n 
E 2 46  ALA 46  46   46   ALA ALA E . n 
E 2 47  GLU 47  47   47   GLU GLU E . n 
E 2 48  GLY 48  48   48   GLY GLY E . n 
E 2 49  LEU 49  49   49   LEU LEU E . n 
E 2 50  ARG 50  50   50   ARG ARG E . n 
E 2 51  PRO 51  51   51   PRO PRO E . n 
E 2 52  VAL 52  52   52   VAL VAL E . n 
E 2 53  LYS 53  53   53   LYS LYS E . n 
E 2 54  GLU 54  54   54   GLU GLU E . n 
E 2 55  VAL 55  55   55   VAL VAL E . n 
E 2 56  GLY 56  56   56   GLY GLY E . n 
E 2 57  MET 57  57   57   MET MET E . n 
E 2 58  TYR 58  58   58   TYR TYR E . n 
E 2 59  GLY 59  59   59   GLY GLY E . n 
E 2 60  LYS 60  60   60   LYS LYS E . n 
E 2 61  ILE 61  61   61   ILE ILE E . n 
E 2 62  ALA 62  62   62   ALA ALA E . n 
E 2 63  VAL 63  63   63   VAL VAL E . n 
E 2 64  MET 64  64   64   MET MET E . n 
E 2 65  GLU 65  65   65   GLU GLU E . n 
E 2 66  LEU 66  66   66   LEU LEU E . n 
E 2 67  PHE 67  67   67   PHE PHE E . n 
E 2 68  ARG 68  68   68   ARG ARG E . n 
E 2 69  PRO 69  69   69   PRO PRO E . n 
E 2 70  LYS 70  70   70   LYS LYS E . n 
E 2 71  GLY 71  71   71   GLY GLY E . n 
E 2 72  GLU 72  72   72   GLU GLU E . n 
E 2 73  SER 73  73   73   SER SER E . n 
E 2 74  LYS 74  74   74   LYS LYS E . n 
E 2 75  ASP 75  75   75   ASP ASP E . n 
E 2 76  LEU 76  76   76   LEU LEU E . n 
E 2 77  LEU 77  77   77   LEU LEU E . n 
E 2 78  PHE 78  78   78   PHE PHE E . n 
E 2 79  ILE 79  79   79   ILE ILE E . n 
E 2 80  LEU 80  80   80   LEU LEU E . n 
E 2 81  THR 81  81   81   THR THR E . n 
E 2 82  ALA 82  82   82   ALA ALA E . n 
E 2 83  LYS 83  83   83   LYS LYS E . n 
E 2 84  TYR 84  84   84   TYR TYR E . n 
E 2 85  ASN 85  85   85   ASN ASN E . n 
E 2 86  ALA 86  86   86   ALA ALA E . n 
E 2 87  CYS 87  87   87   CYS CYS E . n 
E 2 88  ILE 88  88   88   ILE ILE E . n 
E 2 89  LEU 89  89   89   LEU LEU E . n 
E 2 90  GLU 90  90   90   GLU GLU E . n 
E 2 91  TYR 91  91   91   TYR TYR E . n 
E 2 92  LYS 92  92   92   LYS LYS E . n 
E 2 93  GLN 93  93   93   GLN GLN E . n 
E 2 94  SER 94  94   94   SER SER E . n 
E 2 95  GLY 95  95   95   GLY GLY E . n 
E 2 96  GLU 96  96   96   GLU GLU E . n 
E 2 97  SER 97  97   97   SER SER E . n 
E 2 98  ILE 98  98   98   ILE ILE E . n 
E 2 99  ASP 99  99   99   ASP ASP E . n 
E 2 100 ILE 100 100  100  ILE ILE E . n 
E 2 101 ILE 101 101  101  ILE ILE E . n 
E 2 102 THR 102 102  102  THR THR E . n 
E 2 103 ARG 103 103  103  ARG ARG E . n 
E 2 104 ALA 104 104  104  ALA ALA E . n 
E 2 105 HIS 105 105  105  HIS HIS E . n 
E 2 106 GLY 106 106  106  GLY GLY E . n 
E 2 107 ASN 107 107  107  ASN ASN E . n 
E 2 108 VAL 108 108  108  VAL VAL E . n 
E 2 109 GLN 109 109  109  GLN GLN E . n 
E 2 110 ASP 110 110  110  ASP ASP E . n 
E 2 111 ARG 111 111  111  ARG ARG E . n 
E 2 112 ILE 112 112  112  ILE ILE E . n 
E 2 113 GLY 113 113  113  GLY GLY E . n 
E 2 114 ARG 114 114  114  ARG ARG E . n 
E 2 115 PRO 115 115  115  PRO PRO E . n 
E 2 116 SER 116 116  116  SER SER E . n 
E 2 117 GLU 117 117  117  GLU GLU E . n 
E 2 118 THR 118 118  118  THR THR E . n 
E 2 119 GLY 119 119  119  GLY GLY E . n 
E 2 120 ILE 120 120  120  ILE ILE E . n 
E 2 121 ILE 121 121  121  ILE ILE E . n 
E 2 122 GLY 122 122  122  GLY GLY E . n 
E 2 123 ILE 123 123  123  ILE ILE E . n 
E 2 124 ILE 124 124  124  ILE ILE E . n 
E 2 125 ASP 125 125  125  ASP ASP E . n 
E 2 126 PRO 126 126  126  PRO PRO E . n 
E 2 127 GLU 127 127  127  GLU GLU E . n 
E 2 128 CYS 128 128  128  CYS CYS E . n 
E 2 129 ARG 129 129  129  ARG ARG E . n 
E 2 130 MET 130 130  130  MET MET E . n 
E 2 131 ILE 131 131  131  ILE ILE E . n 
E 2 132 GLY 132 132  132  GLY GLY E . n 
E 2 133 LEU 133 133  133  LEU LEU E . n 
E 2 134 ARG 134 134  134  ARG ARG E . n 
E 2 135 LEU 135 135  135  LEU LEU E . n 
E 2 136 TYR 136 136  136  TYR TYR E . n 
E 2 137 ASP 137 137  137  ASP ASP E . n 
E 2 138 GLY 138 138  138  GLY GLY E . n 
E 2 139 LEU 139 139  139  LEU LEU E . n 
E 2 140 PHE 140 140  140  PHE PHE E . n 
E 2 141 LYS 141 141  141  LYS LYS E . n 
E 2 142 VAL 142 142  142  VAL VAL E . n 
E 2 143 ILE 143 143  143  ILE ILE E . n 
E 2 144 PRO 144 144  144  PRO PRO E . n 
E 2 145 LEU 145 145  145  LEU LEU E . n 
E 2 146 ASP 146 146  146  ASP ASP E . n 
E 2 147 ARG 147 147  147  ARG ARG E . n 
E 2 148 ASP 148 148  148  ASP ASP E . n 
E 2 149 ASN 149 149  149  ASN ASN E . n 
E 2 150 LYS 150 150  150  LYS LYS E . n 
E 2 151 GLU 151 151  151  GLU GLU E . n 
E 2 152 LEU 152 152  152  LEU LEU E . n 
E 2 153 LYS 153 153  153  LYS LYS E . n 
E 2 154 ALA 154 154  154  ALA ALA E . n 
E 2 155 PHE 155 155  155  PHE PHE E . n 
E 2 156 ASN 156 156  156  ASN ASN E . n 
E 2 157 ILE 157 157  157  ILE ILE E . n 
E 2 158 ARG 158 158  158  ARG ARG E . n 
E 2 159 LEU 159 159  159  LEU LEU E . n 
E 2 160 GLU 160 160  160  GLU GLU E . n 
E 2 161 GLU 161 161  161  GLU GLU E . n 
E 2 162 LEU 162 162  162  LEU LEU E . n 
E 2 163 HIS 163 163  163  HIS HIS E . n 
E 2 164 VAL 164 164  164  VAL VAL E . n 
E 2 165 ILE 165 165  165  ILE ILE E . n 
E 2 166 ASP 166 166  166  ASP ASP E . n 
E 2 167 VAL 167 167  167  VAL VAL E . n 
E 2 168 LYS 168 168  168  LYS LYS E . n 
E 2 169 PHE 169 169  169  PHE PHE E . n 
E 2 170 LEU 170 170  170  LEU LEU E . n 
E 2 171 TYR 171 171  171  TYR TYR E . n 
E 2 172 GLY 172 172  172  GLY GLY E . n 
E 2 173 CYS 173 173  173  CYS CYS E . n 
E 2 174 GLN 174 174  174  GLN GLN E . n 
E 2 175 ALA 175 175  175  ALA ALA E . n 
E 2 176 PRO 176 176  176  PRO PRO E . n 
E 2 177 THR 177 177  177  THR THR E . n 
E 2 178 ILE 178 178  178  ILE ILE E . n 
E 2 179 CYS 179 179  179  CYS CYS E . n 
E 2 180 PHE 180 180  180  PHE PHE E . n 
E 2 181 VAL 181 181  181  VAL VAL E . n 
E 2 182 TYR 182 182  182  TYR TYR E . n 
E 2 183 GLN 183 183  183  GLN GLN E . n 
E 2 184 ASP 184 184  184  ASP ASP E . n 
E 2 185 PRO 185 185  185  PRO PRO E . n 
E 2 186 GLN 186 186  186  GLN GLN E . n 
E 2 187 GLY 187 187  187  GLY GLY E . n 
E 2 188 ARG 188 188  188  ARG ARG E . n 
E 2 189 HIS 189 189  189  HIS HIS E . n 
E 2 190 VAL 190 190  190  VAL VAL E . n 
E 2 191 LYS 191 191  191  LYS LYS E . n 
E 2 192 THR 192 192  192  THR THR E . n 
E 2 193 TYR 193 193  193  TYR TYR E . n 
E 2 194 GLU 194 194  194  GLU GLU E . n 
E 2 195 VAL 195 195  195  VAL VAL E . n 
E 2 196 SER 196 196  196  SER SER E . n 
E 2 197 LEU 197 197  197  LEU LEU E . n 
E 2 198 ARG 198 198  198  ARG ARG E . n 
E 2 199 GLU 199 199  199  GLU GLU E . n 
E 2 200 LYS 200 200  200  LYS LYS E . n 
E 2 201 GLU 201 201  201  GLU GLU E . n 
E 2 202 PHE 202 202  202  PHE PHE E . n 
E 2 203 ASN 203 203  203  ASN ASN E . n 
E 2 204 LYS 204 204  204  LYS LYS E . n 
E 2 205 GLY 205 205  205  GLY GLY E . n 
E 2 206 PRO 206 206  206  PRO PRO E . n 
E 2 207 TRP 207 207  207  TRP TRP E . n 
E 2 208 LYS 208 208  208  LYS LYS E . n 
E 2 209 GLN 209 209  209  GLN GLN E . n 
E 2 210 GLU 210 210  210  GLU GLU E . n 
E 2 211 ASN 211 211  211  ASN ASN E . n 
E 2 212 VAL 212 212  212  VAL VAL E . n 
E 2 213 GLU 213 213  213  GLU GLU E . n 
E 2 214 ALA 214 214  214  ALA ALA E . n 
E 2 215 GLU 215 215  215  GLU GLU E . n 
E 2 216 ALA 216 216  216  ALA ALA E . n 
E 2 217 SER 217 217  217  SER SER E . n 
E 2 218 MET 218 218  218  MET MET E . n 
E 2 219 VAL 219 219  219  VAL VAL E . n 
E 2 220 ILE 220 220  220  ILE ILE E . n 
E 2 221 ALA 221 221  221  ALA ALA E . n 
E 2 222 VAL 222 222  222  VAL VAL E . n 
E 2 223 PRO 223 223  223  PRO PRO E . n 
E 2 224 GLU 224 224  224  GLU GLU E . n 
E 2 225 PRO 225 225  225  PRO PRO E . n 
E 2 226 PHE 226 226  226  PHE PHE E . n 
E 2 227 GLY 227 227  227  GLY GLY E . n 
E 2 228 GLY 228 228  228  GLY GLY E . n 
E 2 229 ALA 229 229  229  ALA ALA E . n 
E 2 230 ILE 230 230  230  ILE ILE E . n 
E 2 231 ILE 231 231  231  ILE ILE E . n 
E 2 232 ILE 232 232  232  ILE ILE E . n 
E 2 233 GLY 233 233  233  GLY GLY E . n 
E 2 234 GLN 234 234  234  GLN GLN E . n 
E 2 235 GLU 235 235  235  GLU GLU E . n 
E 2 236 SER 236 236  236  SER SER E . n 
E 2 237 ILE 237 237  237  ILE ILE E . n 
E 2 238 THR 238 238  238  THR THR E . n 
E 2 239 TYR 239 239  239  TYR TYR E . n 
E 2 240 HIS 240 240  240  HIS HIS E . n 
E 2 241 ASN 241 241  241  ASN ASN E . n 
E 2 242 GLY 242 242  242  GLY GLY E . n 
E 2 243 ASP 243 243  243  ASP ASP E . n 
E 2 244 LYS 244 244  244  LYS LYS E . n 
E 2 245 TYR 245 245  245  TYR TYR E . n 
E 2 246 LEU 246 246  246  LEU LEU E . n 
E 2 247 ALA 247 247  247  ALA ALA E . n 
E 2 248 ILE 248 248  248  ILE ILE E . n 
E 2 249 ALA 249 249  249  ALA ALA E . n 
E 2 250 PRO 250 250  250  PRO PRO E . n 
E 2 251 PRO 251 251  251  PRO PRO E . n 
E 2 252 ILE 252 252  252  ILE ILE E . n 
E 2 253 ILE 253 253  253  ILE ILE E . n 
E 2 254 LYS 254 254  254  LYS LYS E . n 
E 2 255 GLN 255 255  255  GLN GLN E . n 
E 2 256 SER 256 256  256  SER SER E . n 
E 2 257 THR 257 257  257  THR THR E . n 
E 2 258 ILE 258 258  258  ILE ILE E . n 
E 2 259 VAL 259 259  259  VAL VAL E . n 
E 2 260 CYS 260 260  260  CYS CYS E . n 
E 2 261 HIS 261 261  261  HIS HIS E . n 
E 2 262 ASN 262 262  262  ASN ASN E . n 
E 2 263 ARG 263 263  263  ARG ARG E . n 
E 2 264 VAL 264 264  264  VAL VAL E . n 
E 2 265 ASP 265 265  265  ASP ASP E . n 
E 2 266 PRO 266 266  266  PRO PRO E . n 
E 2 267 ASN 267 267  267  ASN ASN E . n 
E 2 268 GLY 268 268  268  GLY GLY E . n 
E 2 269 SER 269 269  269  SER SER E . n 
E 2 270 ARG 270 270  270  ARG ARG E . n 
E 2 271 TYR 271 271  271  TYR TYR E . n 
E 2 272 LEU 272 272  272  LEU LEU E . n 
E 2 273 LEU 273 273  273  LEU LEU E . n 
E 2 274 GLY 274 274  274  GLY GLY E . n 
E 2 275 ASP 275 275  275  ASP ASP E . n 
E 2 276 MET 276 276  276  MET MET E . n 
E 2 277 GLU 277 277  277  GLU GLU E . n 
E 2 278 GLY 278 278  278  GLY GLY E . n 
E 2 279 ARG 279 279  279  ARG ARG E . n 
E 2 280 LEU 280 280  280  LEU LEU E . n 
E 2 281 PHE 281 281  281  PHE PHE E . n 
E 2 282 MET 282 282  282  MET MET E . n 
E 2 283 LEU 283 283  283  LEU LEU E . n 
E 2 284 LEU 284 284  284  LEU LEU E . n 
E 2 285 LEU 285 285  285  LEU LEU E . n 
E 2 286 GLU 286 286  286  GLU GLU E . n 
E 2 287 LYS 287 287  287  LYS LYS E . n 
E 2 288 GLU 288 288  288  GLU GLU E . n 
E 2 289 GLU 289 289  289  GLU GLU E . n 
E 2 290 GLN 290 290  290  GLN GLN E . n 
E 2 291 MET 291 291  291  MET MET E . n 
E 2 292 ASP 292 292  292  ASP ASP E . n 
E 2 293 GLY 293 293  293  GLY GLY E . n 
E 2 294 THR 294 294  294  THR THR E . n 
E 2 295 VAL 295 295  295  VAL VAL E . n 
E 2 296 THR 296 296  296  THR THR E . n 
E 2 297 LEU 297 297  297  LEU LEU E . n 
E 2 298 LYS 298 298  298  LYS LYS E . n 
E 2 299 ASP 299 299  299  ASP ASP E . n 
E 2 300 LEU 300 300  300  LEU LEU E . n 
E 2 301 ARG 301 301  301  ARG ARG E . n 
E 2 302 VAL 302 302  302  VAL VAL E . n 
E 2 303 GLU 303 303  303  GLU GLU E . n 
E 2 304 LEU 304 304  304  LEU LEU E . n 
E 2 305 LEU 305 305  305  LEU LEU E . n 
E 2 306 GLY 306 306  306  GLY GLY E . n 
E 2 307 GLU 307 307  307  GLU GLU E . n 
E 2 308 THR 308 308  308  THR THR E . n 
E 2 309 SER 309 309  309  SER SER E . n 
E 2 310 ILE 310 310  310  ILE ILE E . n 
E 2 311 ALA 311 311  311  ALA ALA E . n 
E 2 312 GLU 312 312  312  GLU GLU E . n 
E 2 313 CYS 313 313  313  CYS CYS E . n 
E 2 314 LEU 314 314  314  LEU LEU E . n 
E 2 315 THR 315 315  315  THR THR E . n 
E 2 316 TYR 316 316  316  TYR TYR E . n 
E 2 317 LEU 317 317  317  LEU LEU E . n 
E 2 318 ASP 318 318  318  ASP ASP E . n 
E 2 319 ASN 319 319  319  ASN ASN E . n 
E 2 320 GLY 320 320  320  GLY GLY E . n 
E 2 321 VAL 321 321  321  VAL VAL E . n 
E 2 322 VAL 322 322  322  VAL VAL E . n 
E 2 323 PHE 323 323  323  PHE PHE E . n 
E 2 324 VAL 324 324  324  VAL VAL E . n 
E 2 325 GLY 325 325  325  GLY GLY E . n 
E 2 326 SER 326 326  326  SER SER E . n 
E 2 327 ARG 327 327  327  ARG ARG E . n 
E 2 328 LEU 328 328  328  LEU LEU E . n 
E 2 329 GLY 329 329  329  GLY GLY E . n 
E 2 330 ASP 330 330  330  ASP ASP E . n 
E 2 331 SER 331 331  331  SER SER E . n 
E 2 332 GLN 332 332  332  GLN GLN E . n 
E 2 333 LEU 333 333  333  LEU LEU E . n 
E 2 334 VAL 334 334  334  VAL VAL E . n 
E 2 335 LYS 335 335  335  LYS LYS E . n 
E 2 336 LEU 336 336  336  LEU LEU E . n 
E 2 337 ASN 337 337  337  ASN ASN E . n 
E 2 338 VAL 338 338  338  VAL VAL E . n 
E 2 339 ASP 339 339  339  ASP ASP E . n 
E 2 340 SER 340 340  340  SER SER E . n 
E 2 341 ASN 341 341  341  ASN ASN E . n 
E 2 342 GLU 342 342  342  GLU GLU E . n 
E 2 343 GLN 343 343  343  GLN GLN E . n 
E 2 344 GLY 344 344  344  GLY GLY E . n 
E 2 345 SER 345 345  345  SER SER E . n 
E 2 346 TYR 346 346  346  TYR TYR E . n 
E 2 347 VAL 347 347  347  VAL VAL E . n 
E 2 348 VAL 348 348  348  VAL VAL E . n 
E 2 349 ALA 349 349  349  ALA ALA E . n 
E 2 350 MET 350 350  350  MET MET E . n 
E 2 351 GLU 351 351  351  GLU GLU E . n 
E 2 352 THR 352 352  352  THR THR E . n 
E 2 353 PHE 353 353  353  PHE PHE E . n 
E 2 354 THR 354 354  354  THR THR E . n 
E 2 355 ASN 355 355  355  ASN ASN E . n 
E 2 356 LEU 356 356  356  LEU LEU E . n 
E 2 357 GLY 357 357  357  GLY GLY E . n 
E 2 358 PRO 358 358  358  PRO PRO E . n 
E 2 359 ILE 359 359  359  ILE ILE E . n 
E 2 360 VAL 360 360  360  VAL VAL E . n 
E 2 361 ASP 361 361  361  ASP ASP E . n 
E 2 362 MET 362 362  362  MET MET E . n 
E 2 363 CYS 363 363  363  CYS CYS E . n 
E 2 364 VAL 364 364  364  VAL VAL E . n 
E 2 365 VAL 365 365  365  VAL VAL E . n 
E 2 366 ASP 366 366  366  ASP ASP E . n 
E 2 367 LEU 367 367  367  LEU LEU E . n 
E 2 368 GLU 368 368  368  GLU GLU E . n 
E 2 369 ARG 369 369  369  ARG ARG E . n 
E 2 370 GLN 370 370  370  GLN GLN E . n 
E 2 371 GLY 371 371  371  GLY GLY E . n 
E 2 372 GLN 372 372  372  GLN GLN E . n 
E 2 373 GLY 373 373  373  GLY GLY E . n 
E 2 374 GLN 374 374  374  GLN GLN E . n 
E 2 375 LEU 375 375  375  LEU LEU E . n 
E 2 376 VAL 376 376  376  VAL VAL E . n 
E 2 377 THR 377 377  377  THR THR E . n 
E 2 378 CYS 378 378  378  CYS CYS E . n 
E 2 379 SER 379 379  379  SER SER E . n 
E 2 380 GLY 380 380  380  GLY GLY E . n 
E 2 381 ALA 381 381  381  ALA ALA E . n 
E 2 382 PHE 382 382  382  PHE PHE E . n 
E 2 383 LYS 383 383  383  LYS LYS E . n 
E 2 384 GLU 384 384  384  GLU GLU E . n 
E 2 385 GLY 385 385  385  GLY GLY E . n 
E 2 386 SER 386 386  386  SER SER E . n 
E 2 387 LEU 387 387  387  LEU LEU E . n 
E 2 388 ARG 388 388  388  ARG ARG E . n 
E 2 389 ILE 389 389  389  ILE ILE E . n 
E 2 390 ILE 390 390  390  ILE ILE E . n 
E 2 391 ARG 391 391  391  ARG ARG E . n 
E 2 392 ASN 392 392  392  ASN ASN E . n 
E 2 393 GLY 393 697  ?    ?   ?   E . n 
E 2 394 ILE 394 698  ?    ?   ?   E . n 
E 2 395 GLY 395 699  ?    ?   ?   E . n 
E 2 396 GLY 396 700  ?    ?   ?   E . n 
E 2 397 ASN 397 701  ?    ?   ?   E . n 
E 2 398 GLY 398 702  ?    ?   ?   E . n 
E 2 399 ASN 399 703  ?    ?   ?   E . n 
E 2 400 SER 400 704  ?    ?   ?   E . n 
E 2 401 GLY 401 705  ?    ?   ?   E . n 
E 2 402 GLU 402 706  ?    ?   ?   E . n 
E 2 403 ILE 403 707  ?    ?   ?   E . n 
E 2 404 GLN 404 708  ?    ?   ?   E . n 
E 2 405 LYS 405 709  ?    ?   ?   E . n 
E 2 406 LEU 406 710  710  LEU LEU E . n 
E 2 407 HIS 407 711  711  HIS HIS E . n 
E 2 408 ILE 408 712  712  ILE ILE E . n 
E 2 409 ARG 409 713  713  ARG ARG E . n 
E 2 410 THR 410 714  714  THR THR E . n 
E 2 411 VAL 411 715  715  VAL VAL E . n 
E 2 412 PRO 412 716  716  PRO PRO E . n 
E 2 413 LEU 413 717  717  LEU LEU E . n 
E 2 414 TYR 414 718  718  TYR TYR E . n 
E 2 415 GLU 415 719  719  GLU GLU E . n 
E 2 416 SER 416 720  720  SER SER E . n 
E 2 417 PRO 417 721  721  PRO PRO E . n 
E 2 418 ARG 418 722  722  ARG ARG E . n 
E 2 419 LYS 419 723  723  LYS LYS E . n 
E 2 420 ILE 420 724  724  ILE ILE E . n 
E 2 421 CYS 421 725  725  CYS CYS E . n 
E 2 422 TYR 422 726  726  TYR TYR E . n 
E 2 423 GLN 423 727  727  GLN GLN E . n 
E 2 424 GLU 424 728  728  GLU GLU E . n 
E 2 425 VAL 425 729  729  VAL VAL E . n 
E 2 426 SER 426 730  730  SER SER E . n 
E 2 427 GLN 427 731  731  GLN GLN E . n 
E 2 428 CYS 428 732  732  CYS CYS E . n 
E 2 429 PHE 429 733  733  PHE PHE E . n 
E 2 430 GLY 430 734  734  GLY GLY E . n 
E 2 431 VAL 431 735  735  VAL VAL E . n 
E 2 432 LEU 432 736  736  LEU LEU E . n 
E 2 433 SER 433 737  737  SER SER E . n 
E 2 434 SER 434 738  738  SER SER E . n 
E 2 435 ARG 435 739  739  ARG ARG E . n 
E 2 436 ILE 436 740  740  ILE ILE E . n 
E 2 437 GLU 437 741  741  GLU GLU E . n 
E 2 438 VAL 438 742  742  VAL VAL E . n 
E 2 439 GLN 439 743  743  GLN GLN E . n 
E 2 440 ASP 440 744  744  ASP ASP E . n 
E 2 441 THR 441 745  745  THR THR E . n 
E 2 442 SER 442 746  746  SER SER E . n 
E 2 443 GLY 443 747  747  GLY GLY E . n 
E 2 444 GLY 444 748  748  GLY GLY E . n 
E 2 445 THR 445 749  749  THR THR E . n 
E 2 446 THR 446 750  750  THR THR E . n 
E 2 447 ALA 447 751  751  ALA ALA E . n 
E 2 448 LEU 448 752  752  LEU LEU E . n 
E 2 449 ARG 449 753  753  ARG ARG E . n 
E 2 450 PRO 450 754  754  PRO PRO E . n 
E 2 451 SER 451 755  755  SER SER E . n 
E 2 452 ALA 452 756  756  ALA ALA E . n 
E 2 453 SER 453 757  757  SER SER E . n 
E 2 454 THR 454 758  758  THR THR E . n 
E 2 455 GLN 455 759  759  GLN GLN E . n 
E 2 456 ALA 456 760  760  ALA ALA E . n 
E 2 457 LEU 457 761  761  LEU LEU E . n 
E 2 458 SER 458 762  762  SER SER E . n 
E 2 459 SER 459 763  763  SER SER E . n 
E 2 460 SER 460 764  764  SER SER E . n 
E 2 461 VAL 461 765  765  VAL VAL E . n 
E 2 462 SER 462 766  766  SER SER E . n 
E 2 463 SER 463 767  767  SER SER E . n 
E 2 464 SER 464 768  768  SER SER E . n 
E 2 465 LYS 465 769  769  LYS LYS E . n 
E 2 466 LEU 466 770  770  LEU LEU E . n 
E 2 467 PHE 467 771  771  PHE PHE E . n 
E 2 468 SER 468 772  ?    ?   ?   E . n 
E 2 469 SER 469 773  ?    ?   ?   E . n 
E 2 470 SER 470 774  ?    ?   ?   E . n 
E 2 471 THR 471 775  ?    ?   ?   E . n 
E 2 472 ALA 472 776  ?    ?   ?   E . n 
E 2 473 PRO 473 777  ?    ?   ?   E . n 
E 2 474 HIS 474 778  ?    ?   ?   E . n 
E 2 475 GLU 475 779  ?    ?   ?   E . n 
E 2 476 THR 476 780  780  THR THR E . n 
E 2 477 SER 477 781  781  SER SER E . n 
E 2 478 PHE 478 782  782  PHE PHE E . n 
E 2 479 GLY 479 783  783  GLY GLY E . n 
E 2 480 GLU 480 784  784  GLU GLU E . n 
E 2 481 GLU 481 785  785  GLU GLU E . n 
E 2 482 VAL 482 786  786  VAL VAL E . n 
E 2 483 GLU 483 787  787  GLU GLU E . n 
E 2 484 VAL 484 788  788  VAL VAL E . n 
E 2 485 HIS 485 789  789  HIS HIS E . n 
E 2 486 ASN 486 790  790  ASN ASN E . n 
E 2 487 LEU 487 791  791  LEU LEU E . n 
E 2 488 LEU 488 792  792  LEU LEU E . n 
E 2 489 ILE 489 793  793  ILE ILE E . n 
E 2 490 ILE 490 794  794  ILE ILE E . n 
E 2 491 ASP 491 795  795  ASP ASP E . n 
E 2 492 GLN 492 796  796  GLN GLN E . n 
E 2 493 HIS 493 797  797  HIS HIS E . n 
E 2 494 THR 494 798  798  THR THR E . n 
E 2 495 PHE 495 799  799  PHE PHE E . n 
E 2 496 GLU 496 800  800  GLU GLU E . n 
E 2 497 VAL 497 801  801  VAL VAL E . n 
E 2 498 LEU 498 802  802  LEU LEU E . n 
E 2 499 HIS 499 803  803  HIS HIS E . n 
E 2 500 ALA 500 804  804  ALA ALA E . n 
E 2 501 HIS 501 805  805  HIS HIS E . n 
E 2 502 GLN 502 806  806  GLN GLN E . n 
E 2 503 PHE 503 807  807  PHE PHE E . n 
E 2 504 LEU 504 808  808  LEU LEU E . n 
E 2 505 GLN 505 809  809  GLN GLN E . n 
E 2 506 ASN 506 810  810  ASN ASN E . n 
E 2 507 GLU 507 811  811  GLU GLU E . n 
E 2 508 TYR 508 812  812  TYR TYR E . n 
E 2 509 ALA 509 813  813  ALA ALA E . n 
E 2 510 LEU 510 814  814  LEU LEU E . n 
E 2 511 SER 511 815  815  SER SER E . n 
E 2 512 LEU 512 816  816  LEU LEU E . n 
E 2 513 VAL 513 817  817  VAL VAL E . n 
E 2 514 SER 514 818  818  SER SER E . n 
E 2 515 CYS 515 819  819  CYS CYS E . n 
E 2 516 LYS 516 820  820  LYS LYS E . n 
E 2 517 LEU 517 821  821  LEU LEU E . n 
E 2 518 GLY 518 822  822  GLY GLY E . n 
E 2 519 LYS 519 823  823  LYS LYS E . n 
E 2 520 ASP 520 824  824  ASP ASP E . n 
E 2 521 PRO 521 825  825  PRO PRO E . n 
E 2 522 ASN 522 826  826  ASN ASN E . n 
E 2 523 THR 523 827  827  THR THR E . n 
E 2 524 TYR 524 828  828  TYR TYR E . n 
E 2 525 PHE 525 829  829  PHE PHE E . n 
E 2 526 ILE 526 830  830  ILE ILE E . n 
E 2 527 VAL 527 831  831  VAL VAL E . n 
E 2 528 GLY 528 832  832  GLY GLY E . n 
E 2 529 THR 529 833  833  THR THR E . n 
E 2 530 ALA 530 834  834  ALA ALA E . n 
E 2 531 MET 531 835  835  MET MET E . n 
E 2 532 VAL 532 836  836  VAL VAL E . n 
E 2 533 TYR 533 837  837  TYR TYR E . n 
E 2 534 PRO 534 838  838  PRO PRO E . n 
E 2 535 GLU 535 839  839  GLU GLU E . n 
E 2 536 GLU 536 840  840  GLU GLU E . n 
E 2 537 ALA 537 841  841  ALA ALA E . n 
E 2 538 GLU 538 842  842  GLU GLU E . n 
E 2 539 PRO 539 843  843  PRO PRO E . n 
E 2 540 LYS 540 844  844  LYS LYS E . n 
E 2 541 GLN 541 845  845  GLN GLN E . n 
E 2 542 GLY 542 846  846  GLY GLY E . n 
E 2 543 ARG 543 847  847  ARG ARG E . n 
E 2 544 ILE 544 848  848  ILE ILE E . n 
E 2 545 VAL 545 849  849  VAL VAL E . n 
E 2 546 VAL 546 850  850  VAL VAL E . n 
E 2 547 PHE 547 851  851  PHE PHE E . n 
E 2 548 GLN 548 852  852  GLN GLN E . n 
E 2 549 TYR 549 853  853  TYR TYR E . n 
E 2 550 SER 550 854  854  SER SER E . n 
E 2 551 ASP 551 855  855  ASP ASP E . n 
E 2 552 GLY 552 856  856  GLY GLY E . n 
E 2 553 LYS 553 857  857  LYS LYS E . n 
E 2 554 LEU 554 858  858  LEU LEU E . n 
E 2 555 GLN 555 859  859  GLN GLN E . n 
E 2 556 THR 556 860  860  THR THR E . n 
E 2 557 VAL 557 861  861  VAL VAL E . n 
E 2 558 ALA 558 862  862  ALA ALA E . n 
E 2 559 GLU 559 863  863  GLU GLU E . n 
E 2 560 LYS 560 864  864  LYS LYS E . n 
E 2 561 GLU 561 865  865  GLU GLU E . n 
E 2 562 VAL 562 866  866  VAL VAL E . n 
E 2 563 LYS 563 867  867  LYS LYS E . n 
E 2 564 GLY 564 868  868  GLY GLY E . n 
E 2 565 ALA 565 869  869  ALA ALA E . n 
E 2 566 VAL 566 870  870  VAL VAL E . n 
E 2 567 TYR 567 871  871  TYR TYR E . n 
E 2 568 SER 568 872  872  SER SER E . n 
E 2 569 MET 569 873  873  MET MET E . n 
E 2 570 VAL 570 874  874  VAL VAL E . n 
E 2 571 GLU 571 875  875  GLU GLU E . n 
E 2 572 PHE 572 876  876  PHE PHE E . n 
E 2 573 ASN 573 877  877  ASN ASN E . n 
E 2 574 GLY 574 878  878  GLY GLY E . n 
E 2 575 LYS 575 879  879  LYS LYS E . n 
E 2 576 LEU 576 880  880  LEU LEU E . n 
E 2 577 LEU 577 881  881  LEU LEU E . n 
E 2 578 ALA 578 882  882  ALA ALA E . n 
E 2 579 SER 579 883  883  SER SER E . n 
E 2 580 ILE 580 884  884  ILE ILE E . n 
E 2 581 ASN 581 885  885  ASN ASN E . n 
E 2 582 SER 582 886  886  SER SER E . n 
E 2 583 THR 583 887  887  THR THR E . n 
E 2 584 VAL 584 888  888  VAL VAL E . n 
E 2 585 ARG 585 889  889  ARG ARG E . n 
E 2 586 LEU 586 890  890  LEU LEU E . n 
E 2 587 TYR 587 891  891  TYR TYR E . n 
E 2 588 GLU 588 892  892  GLU GLU E . n 
E 2 589 TRP 589 893  893  TRP TRP E . n 
E 2 590 THR 590 894  894  THR THR E . n 
E 2 591 THR 591 895  895  THR THR E . n 
E 2 592 GLU 592 896  896  GLU GLU E . n 
E 2 593 LYS 593 897  897  LYS LYS E . n 
E 2 594 GLU 594 898  898  GLU GLU E . n 
E 2 595 LEU 595 899  899  LEU LEU E . n 
E 2 596 ARG 596 900  900  ARG ARG E . n 
E 2 597 THR 597 901  901  THR THR E . n 
E 2 598 GLU 598 902  902  GLU GLU E . n 
E 2 599 CYS 599 903  903  CYS CYS E . n 
E 2 600 ASN 600 904  904  ASN ASN E . n 
E 2 601 HIS 601 905  905  HIS HIS E . n 
E 2 602 TYR 602 906  906  TYR TYR E . n 
E 2 603 ASN 603 907  907  ASN ASN E . n 
E 2 604 ASN 604 908  908  ASN ASN E . n 
E 2 605 ILE 605 909  909  ILE ILE E . n 
E 2 606 MET 606 910  910  MET MET E . n 
E 2 607 ALA 607 911  911  ALA ALA E . n 
E 2 608 LEU 608 912  912  LEU LEU E . n 
E 2 609 TYR 609 913  913  TYR TYR E . n 
E 2 610 LEU 610 914  914  LEU LEU E . n 
E 2 611 LYS 611 915  915  LYS LYS E . n 
E 2 612 THR 612 916  916  THR THR E . n 
E 2 613 LYS 613 917  917  LYS LYS E . n 
E 2 614 GLY 614 918  918  GLY GLY E . n 
E 2 615 ASP 615 919  919  ASP ASP E . n 
E 2 616 PHE 616 920  920  PHE PHE E . n 
E 2 617 ILE 617 921  921  ILE ILE E . n 
E 2 618 LEU 618 922  922  LEU LEU E . n 
E 2 619 VAL 619 923  923  VAL VAL E . n 
E 2 620 GLY 620 924  924  GLY GLY E . n 
E 2 621 ASP 621 925  925  ASP ASP E . n 
E 2 622 LEU 622 926  926  LEU LEU E . n 
E 2 623 MET 623 927  927  MET MET E . n 
E 2 624 ARG 624 928  928  ARG ARG E . n 
E 2 625 SER 625 929  929  SER SER E . n 
E 2 626 VAL 626 930  930  VAL VAL E . n 
E 2 627 LEU 627 931  931  LEU LEU E . n 
E 2 628 LEU 628 932  932  LEU LEU E . n 
E 2 629 LEU 629 933  933  LEU LEU E . n 
E 2 630 ALA 630 934  934  ALA ALA E . n 
E 2 631 TYR 631 935  935  TYR TYR E . n 
E 2 632 LYS 632 936  936  LYS LYS E . n 
E 2 633 PRO 633 937  937  PRO PRO E . n 
E 2 634 MET 634 938  938  MET MET E . n 
E 2 635 GLU 635 939  939  GLU GLU E . n 
E 2 636 GLY 636 940  940  GLY GLY E . n 
E 2 637 ASN 637 941  941  ASN ASN E . n 
E 2 638 PHE 638 942  942  PHE PHE E . n 
E 2 639 GLU 639 943  943  GLU GLU E . n 
E 2 640 GLU 640 944  944  GLU GLU E . n 
E 2 641 ILE 641 945  945  ILE ILE E . n 
E 2 642 ALA 642 946  946  ALA ALA E . n 
E 2 643 ARG 643 947  947  ARG ARG E . n 
E 2 644 ASP 644 948  948  ASP ASP E . n 
E 2 645 PHE 645 949  949  PHE PHE E . n 
E 2 646 ASN 646 950  950  ASN ASN E . n 
E 2 647 PRO 647 951  951  PRO PRO E . n 
E 2 648 ASN 648 952  952  ASN ASN E . n 
E 2 649 TRP 649 953  953  TRP TRP E . n 
E 2 650 MET 650 954  954  MET MET E . n 
E 2 651 SER 651 955  955  SER SER E . n 
E 2 652 ALA 652 956  956  ALA ALA E . n 
E 2 653 VAL 653 957  957  VAL VAL E . n 
E 2 654 GLU 654 958  958  GLU GLU E . n 
E 2 655 ILE 655 959  959  ILE ILE E . n 
E 2 656 LEU 656 960  960  LEU LEU E . n 
E 2 657 ASP 657 961  961  ASP ASP E . n 
E 2 658 ASP 658 962  962  ASP ASP E . n 
E 2 659 ASP 659 963  963  ASP ASP E . n 
E 2 660 ASN 660 964  964  ASN ASN E . n 
E 2 661 PHE 661 965  965  PHE PHE E . n 
E 2 662 LEU 662 966  966  LEU LEU E . n 
E 2 663 GLY 663 967  967  GLY GLY E . n 
E 2 664 ALA 664 968  968  ALA ALA E . n 
E 2 665 GLU 665 969  969  GLU GLU E . n 
E 2 666 ASN 666 970  970  ASN ASN E . n 
E 2 667 ALA 667 971  971  ALA ALA E . n 
E 2 668 PHE 668 972  972  PHE PHE E . n 
E 2 669 ASN 669 973  973  ASN ASN E . n 
E 2 670 LEU 670 974  974  LEU LEU E . n 
E 2 671 PHE 671 975  975  PHE PHE E . n 
E 2 672 VAL 672 976  976  VAL VAL E . n 
E 2 673 CYS 673 977  977  CYS CYS E . n 
E 2 674 GLN 674 978  978  GLN GLN E . n 
E 2 675 LYS 675 979  979  LYS LYS E . n 
E 2 676 ASP 676 980  980  ASP ASP E . n 
E 2 677 SER 677 981  981  SER SER E . n 
E 2 678 ALA 678 982  ?    ?   ?   E . n 
E 2 679 ALA 679 983  983  ALA ALA E . n 
E 2 680 THR 680 984  984  THR THR E . n 
E 2 681 THR 681 985  985  THR THR E . n 
E 2 682 ASP 682 986  986  ASP ASP E . n 
E 2 683 GLU 683 987  987  GLU GLU E . n 
E 2 684 GLU 684 988  988  GLU GLU E . n 
E 2 685 ARG 685 989  989  ARG ARG E . n 
E 2 686 GLN 686 990  990  GLN GLN E . n 
E 2 687 HIS 687 991  991  HIS HIS E . n 
E 2 688 LEU 688 992  992  LEU LEU E . n 
E 2 689 GLN 689 993  993  GLN GLN E . n 
E 2 690 GLU 690 994  994  GLU GLU E . n 
E 2 691 VAL 691 995  995  VAL VAL E . n 
E 2 692 GLY 692 996  996  GLY GLY E . n 
E 2 693 LEU 693 997  997  LEU LEU E . n 
E 2 694 PHE 694 998  998  PHE PHE E . n 
E 2 695 HIS 695 999  999  HIS HIS E . n 
E 2 696 LEU 696 1000 1000 LEU LEU E . n 
E 2 697 GLY 697 1001 1001 GLY GLY E . n 
E 2 698 GLU 698 1002 1002 GLU GLU E . n 
E 2 699 PHE 699 1003 1003 PHE PHE E . n 
E 2 700 VAL 700 1004 1004 VAL VAL E . n 
E 2 701 ASN 701 1005 1005 ASN ASN E . n 
E 2 702 VAL 702 1006 1006 VAL VAL E . n 
E 2 703 PHE 703 1007 1007 PHE PHE E . n 
E 2 704 CYS 704 1008 1008 CYS CYS E . n 
E 2 705 HIS 705 1009 1009 HIS HIS E . n 
E 2 706 GLY 706 1010 1010 GLY GLY E . n 
E 2 707 SER 707 1011 1011 SER SER E . n 
E 2 708 LEU 708 1012 1012 LEU LEU E . n 
E 2 709 VAL 709 1013 1013 VAL VAL E . n 
E 2 710 MET 710 1014 1014 MET MET E . n 
E 2 711 GLN 711 1015 ?    ?   ?   E . n 
E 2 712 ASN 712 1016 ?    ?   ?   E . n 
E 2 713 LEU 713 1017 ?    ?   ?   E . n 
E 2 714 GLY 714 1018 ?    ?   ?   E . n 
E 2 715 GLU 715 1019 ?    ?   ?   E . n 
E 2 716 THR 716 1020 ?    ?   ?   E . n 
E 2 717 SER 717 1021 ?    ?   ?   E . n 
E 2 718 THR 718 1022 ?    ?   ?   E . n 
E 2 719 PRO 719 1023 1023 PRO PRO E . n 
E 2 720 THR 720 1024 1024 THR THR E . n 
E 2 721 GLN 721 1025 1025 GLN GLN E . n 
E 2 722 GLY 722 1026 1026 GLY GLY E . n 
E 2 723 SER 723 1027 1027 SER SER E . n 
E 2 724 VAL 724 1028 1028 VAL VAL E . n 
E 2 725 LEU 725 1029 1029 LEU LEU E . n 
E 2 726 PHE 726 1030 1030 PHE PHE E . n 
E 2 727 GLY 727 1031 1031 GLY GLY E . n 
E 2 728 THR 728 1032 1032 THR THR E . n 
E 2 729 VAL 729 1033 1033 VAL VAL E . n 
E 2 730 ASN 730 1034 1034 ASN ASN E . n 
E 2 731 GLY 731 1035 1035 GLY GLY E . n 
E 2 732 MET 732 1036 1036 MET MET E . n 
E 2 733 ILE 733 1037 1037 ILE ILE E . n 
E 2 734 GLY 734 1038 1038 GLY GLY E . n 
E 2 735 LEU 735 1039 1039 LEU LEU E . n 
E 2 736 VAL 736 1040 1040 VAL VAL E . n 
E 2 737 THR 737 1041 1041 THR THR E . n 
E 2 738 SER 738 1042 1042 SER SER E . n 
E 2 739 LEU 739 1043 1043 LEU LEU E . n 
E 2 740 SER 740 1044 1044 SER SER E . n 
E 2 741 GLU 741 1045 1045 GLU GLU E . n 
E 2 742 SER 742 1046 1046 SER SER E . n 
E 2 743 TRP 743 1047 1047 TRP TRP E . n 
E 2 744 TYR 744 1048 1048 TYR TYR E . n 
E 2 745 ASN 745 1049 1049 ASN ASN E . n 
E 2 746 LEU 746 1050 1050 LEU LEU E . n 
E 2 747 LEU 747 1051 1051 LEU LEU E . n 
E 2 748 LEU 748 1052 1052 LEU LEU E . n 
E 2 749 ASP 749 1053 1053 ASP ASP E . n 
E 2 750 MET 750 1054 1054 MET MET E . n 
E 2 751 GLN 751 1055 1055 GLN GLN E . n 
E 2 752 ASN 752 1056 1056 ASN ASN E . n 
E 2 753 ARG 753 1057 1057 ARG ARG E . n 
E 2 754 LEU 754 1058 1058 LEU LEU E . n 
E 2 755 ASN 755 1059 1059 ASN ASN E . n 
E 2 756 LYS 756 1060 1060 LYS LYS E . n 
E 2 757 VAL 757 1061 1061 VAL VAL E . n 
E 2 758 ILE 758 1062 1062 ILE ILE E . n 
E 2 759 LYS 759 1063 1063 LYS LYS E . n 
E 2 760 SER 760 1064 1064 SER SER E . n 
E 2 761 VAL 761 1065 1065 VAL VAL E . n 
E 2 762 GLY 762 1066 1066 GLY GLY E . n 
E 2 763 LYS 763 1067 1067 LYS LYS E . n 
E 2 764 ILE 764 1068 1068 ILE ILE E . n 
E 2 765 GLU 765 1069 1069 GLU GLU E . n 
E 2 766 HIS 766 1070 1070 HIS HIS E . n 
E 2 767 SER 767 1071 1071 SER SER E . n 
E 2 768 PHE 768 1072 1072 PHE PHE E . n 
E 2 769 TRP 769 1073 1073 TRP TRP E . n 
E 2 770 ARG 770 1074 1074 ARG ARG E . n 
E 2 771 SER 771 1075 1075 SER SER E . n 
E 2 772 PHE 772 1076 1076 PHE PHE E . n 
E 2 773 HIS 773 1077 1077 HIS HIS E . n 
E 2 774 THR 774 1078 1078 THR THR E . n 
E 2 775 GLU 775 1079 1079 GLU GLU E . n 
E 2 776 ARG 776 1080 1080 ARG ARG E . n 
E 2 777 LYS 777 1081 1081 LYS LYS E . n 
E 2 778 THR 778 1082 1082 THR THR E . n 
E 2 779 GLU 779 1083 1083 GLU GLU E . n 
E 2 780 PRO 780 1084 1084 PRO PRO E . n 
E 2 781 ALA 781 1085 1085 ALA ALA E . n 
E 2 782 THR 782 1086 1086 THR THR E . n 
E 2 783 GLY 783 1087 1087 GLY GLY E . n 
E 2 784 PHE 784 1088 1088 PHE PHE E . n 
E 2 785 ILE 785 1089 1089 ILE ILE E . n 
E 2 786 ASP 786 1090 1090 ASP ASP E . n 
E 2 787 GLY 787 1091 1091 GLY GLY E . n 
E 2 788 ASP 788 1092 1092 ASP ASP E . n 
E 2 789 LEU 789 1093 1093 LEU LEU E . n 
E 2 790 ILE 790 1094 1094 ILE ILE E . n 
E 2 791 GLU 791 1095 1095 GLU GLU E . n 
E 2 792 SER 792 1096 1096 SER SER E . n 
E 2 793 PHE 793 1097 1097 PHE PHE E . n 
E 2 794 LEU 794 1098 1098 LEU LEU E . n 
E 2 795 ASP 795 1099 1099 ASP ASP E . n 
E 2 796 ILE 796 1100 1100 ILE ILE E . n 
E 2 797 SER 797 1101 1101 SER SER E . n 
E 2 798 ARG 798 1102 1102 ARG ARG E . n 
E 2 799 PRO 799 1103 1103 PRO PRO E . n 
E 2 800 LYS 800 1104 1104 LYS LYS E . n 
E 2 801 MET 801 1105 1105 MET MET E . n 
E 2 802 GLN 802 1106 1106 GLN GLN E . n 
E 2 803 GLU 803 1107 1107 GLU GLU E . n 
E 2 804 VAL 804 1108 1108 VAL VAL E . n 
E 2 805 VAL 805 1109 1109 VAL VAL E . n 
E 2 806 ALA 806 1110 1110 ALA ALA E . n 
E 2 807 ASN 807 1111 1111 ASN ASN E . n 
E 2 808 LEU 808 1112 1112 LEU LEU E . n 
E 2 809 GLN 809 1113 ?    ?   ?   E . n 
E 2 810 TYR 810 1114 ?    ?   ?   E . n 
E 2 811 ASP 811 1115 ?    ?   ?   E . n 
E 2 812 ASP 812 1116 ?    ?   ?   E . n 
E 2 813 GLY 813 1117 ?    ?   ?   E . n 
E 2 814 SER 814 1118 ?    ?   ?   E . n 
E 2 815 GLY 815 1119 ?    ?   ?   E . n 
E 2 816 MET 816 1120 ?    ?   ?   E . n 
E 2 817 LYS 817 1121 ?    ?   ?   E . n 
E 2 818 ARG 818 1122 ?    ?   ?   E . n 
E 2 819 GLU 819 1123 1123 GLU GLU E . n 
E 2 820 ALA 820 1124 1124 ALA ALA E . n 
E 2 821 THR 821 1125 1125 THR THR E . n 
E 2 822 ALA 822 1126 1126 ALA ALA E . n 
E 2 823 ASP 823 1127 1127 ASP ASP E . n 
E 2 824 ASP 824 1128 1128 ASP ASP E . n 
E 2 825 LEU 825 1129 1129 LEU LEU E . n 
E 2 826 ILE 826 1130 1130 ILE ILE E . n 
E 2 827 LYS 827 1131 1131 LYS LYS E . n 
E 2 828 VAL 828 1132 1132 VAL VAL E . n 
E 2 829 VAL 829 1133 1133 VAL VAL E . n 
E 2 830 GLU 830 1134 1134 GLU GLU E . n 
E 2 831 GLU 831 1135 1135 GLU GLU E . n 
E 2 832 LEU 832 1136 1136 LEU LEU E . n 
E 2 833 THR 833 1137 1137 THR THR E . n 
E 2 834 ARG 834 1138 1138 ARG ARG E . n 
E 2 835 ILE 835 1139 1139 ILE ILE E . n 
E 2 836 HIS 836 1140 1140 HIS HIS E . n 
F 3 1   SER 1   866  ?    ?   ?   F . n 
F 3 2   GLN 2   867  ?    ?   ?   F . n 
F 3 3   SER 3   868  868  SER SER F . n 
F 3 4   LEU 4   869  869  LEU LEU F . n 
F 3 5   THR 5   870  870  THR THR F . n 
F 3 6   THR 6   871  871  THR THR F . n 
F 3 7   CYS 7   872  872  CYS CYS F . n 
F 3 8   GLU 8   873  873  GLU GLU F . n 
F 3 9   VAL 9   874  874  VAL VAL F . n 
F 3 10  CYS 10  875  875  CYS CYS F . n 
F 3 11  GLY 11  876  876  GLY GLY F . n 
F 3 12  ALA 12  877  877  ALA ALA F . n 
F 3 13  CYS 13  878  878  CYS CYS F . n 
F 3 14  PHE 14  879  879  PHE PHE F . n 
F 3 15  GLU 15  880  880  GLU GLU F . n 
F 3 16  THR 16  881  881  THR THR F . n 
F 3 17  ARG 17  882  882  ARG ARG F . n 
F 3 18  LYS 18  883  883  LYS LYS F . n 
F 3 19  GLY 19  884  884  GLY GLY F . n 
F 3 20  LEU 20  885  885  LEU LEU F . n 
F 3 21  SER 21  886  886  SER SER F . n 
F 3 22  SER 22  887  887  SER SER F . n 
F 3 23  HIS 23  888  888  HIS HIS F . n 
F 3 24  ALA 24  889  889  ALA ALA F . n 
F 3 25  ARG 25  890  890  ARG ARG F . n 
F 3 26  SER 26  891  891  SER SER F . n 
F 3 27  HIS 27  892  892  HIS HIS F . n 
F 3 28  LEU 28  893  893  LEU LEU F . n 
F 3 29  ARG 29  894  894  ARG ARG F . n 
F 3 30  GLN 30  895  ?    ?   ?   F . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A5H 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A5H 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G 4 ZN    1  501  501 ZN    ZN  A . 
H 5 SO4   1  502  502 SO4   SO4 A . 
I 6 A1A5H 1  503  1   A1A5H LI1 A . 
J 4 ZN    1  900  900 ZN    ZN  C . 
K 4 ZN    1  501  501 ZN    ZN  D . 
L 5 SO4   1  502  502 SO4   SO4 D . 
M 6 A1A5H 1  503  1   A1A5H LI1 D . 
N 4 ZN    1  900  900 ZN    ZN  F . 
O 7 HOH   1  601  15  HOH   HOH A . 
O 7 HOH   2  602  13  HOH   HOH A . 
O 7 HOH   3  603  16  HOH   HOH A . 
O 7 HOH   4  604  17  HOH   HOH A . 
O 7 HOH   5  605  35  HOH   HOH A . 
O 7 HOH   6  606  34  HOH   HOH A . 
P 7 HOH   1  1201 11  HOH   HOH B . 
P 7 HOH   2  1202 19  HOH   HOH B . 
P 7 HOH   3  1203 22  HOH   HOH B . 
P 7 HOH   4  1204 2   HOH   HOH B . 
P 7 HOH   5  1205 5   HOH   HOH B . 
P 7 HOH   6  1206 21  HOH   HOH B . 
P 7 HOH   7  1207 40  HOH   HOH B . 
P 7 HOH   8  1208 4   HOH   HOH B . 
P 7 HOH   9  1209 41  HOH   HOH B . 
P 7 HOH   10 1210 18  HOH   HOH B . 
P 7 HOH   11 1211 36  HOH   HOH B . 
P 7 HOH   12 1212 7   HOH   HOH B . 
P 7 HOH   13 1213 3   HOH   HOH B . 
P 7 HOH   14 1214 12  HOH   HOH B . 
P 7 HOH   15 1215 14  HOH   HOH B . 
P 7 HOH   16 1216 20  HOH   HOH B . 
Q 7 HOH   1  1001 8   HOH   HOH C . 
R 7 HOH   1  601  26  HOH   HOH D . 
R 7 HOH   2  602  23  HOH   HOH D . 
R 7 HOH   3  603  25  HOH   HOH D . 
R 7 HOH   4  604  27  HOH   HOH D . 
R 7 HOH   5  605  29  HOH   HOH D . 
R 7 HOH   6  606  28  HOH   HOH D . 
R 7 HOH   7  607  24  HOH   HOH D . 
S 7 HOH   1  1201 37  HOH   HOH E . 
S 7 HOH   2  1202 6   HOH   HOH E . 
S 7 HOH   3  1203 10  HOH   HOH E . 
S 7 HOH   4  1204 39  HOH   HOH E . 
S 7 HOH   5  1205 32  HOH   HOH E . 
S 7 HOH   6  1206 38  HOH   HOH E . 
S 7 HOH   7  1207 1   HOH   HOH E . 
S 7 HOH   8  1208 31  HOH   HOH E . 
S 7 HOH   9  1209 30  HOH   HOH E . 
S 7 HOH   10 1210 9   HOH   HOH E . 
S 7 HOH   11 1211 42  HOH   HOH E . 
T 7 HOH   1  1001 33  HOH   HOH F . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLN 86   ? CG  ? A GLN 17  CG  
2   1 Y 1 A GLN 86   ? CD  ? A GLN 17  CD  
3   1 Y 1 A GLN 86   ? OE1 ? A GLN 17  OE1 
4   1 Y 1 A GLN 86   ? NE2 ? A GLN 17  NE2 
5   1 Y 1 A GLN 100  ? CG  ? A GLN 31  CG  
6   1 Y 1 A GLN 100  ? CD  ? A GLN 31  CD  
7   1 Y 1 A GLN 100  ? OE1 ? A GLN 31  OE1 
8   1 Y 1 A GLN 100  ? NE2 ? A GLN 31  NE2 
9   1 Y 1 A GLN 105  ? CG  ? A GLN 36  CG  
10  1 Y 1 A GLN 105  ? CD  ? A GLN 36  CD  
11  1 Y 1 A GLN 105  ? OE1 ? A GLN 36  OE1 
12  1 Y 1 A GLN 105  ? NE2 ? A GLN 36  NE2 
13  1 Y 1 A ARG 111  ? CG  ? A ARG 42  CG  
14  1 Y 1 A ARG 111  ? CD  ? A ARG 42  CD  
15  1 Y 1 A ARG 111  ? NE  ? A ARG 42  NE  
16  1 Y 1 A ARG 111  ? CZ  ? A ARG 42  CZ  
17  1 Y 1 A ARG 111  ? NH1 ? A ARG 42  NH1 
18  1 Y 1 A ARG 111  ? NH2 ? A ARG 42  NH2 
19  1 Y 1 A LYS 156  ? CG  ? A LYS 87  CG  
20  1 Y 1 A LYS 156  ? CD  ? A LYS 87  CD  
21  1 Y 1 A LYS 156  ? CE  ? A LYS 87  CE  
22  1 Y 1 A LYS 156  ? NZ  ? A LYS 87  NZ  
23  1 Y 1 A LYS 158  ? CG  ? A LYS 89  CG  
24  1 Y 1 A LYS 158  ? CD  ? A LYS 89  CD  
25  1 Y 1 A LYS 158  ? CE  ? A LYS 89  CE  
26  1 Y 1 A LYS 158  ? NZ  ? A LYS 89  NZ  
27  1 Y 1 A ILE 177  ? CG1 ? A ILE 108 CG1 
28  1 Y 1 A ILE 177  ? CG2 ? A ILE 108 CG2 
29  1 Y 1 A ILE 177  ? CD1 ? A ILE 108 CD1 
30  1 Y 1 A GLN 178  ? CG  ? A GLN 109 CG  
31  1 Y 1 A GLN 178  ? CD  ? A GLN 109 CD  
32  1 Y 1 A GLN 178  ? OE1 ? A GLN 109 OE1 
33  1 Y 1 A GLN 178  ? NE2 ? A GLN 109 NE2 
34  1 Y 1 A LYS 181  ? CG  ? A LYS 112 CG  
35  1 Y 1 A LYS 181  ? CD  ? A LYS 112 CD  
36  1 Y 1 A LYS 181  ? CE  ? A LYS 112 CE  
37  1 Y 1 A LYS 181  ? NZ  ? A LYS 112 NZ  
38  1 Y 1 A LYS 204  ? CG  ? A LYS 135 CG  
39  1 Y 1 A LYS 204  ? CD  ? A LYS 135 CD  
40  1 Y 1 A LYS 204  ? CE  ? A LYS 135 CE  
41  1 Y 1 A LYS 204  ? NZ  ? A LYS 135 NZ  
42  1 Y 1 A LYS 222  ? CG  ? A LYS 153 CG  
43  1 Y 1 A LYS 222  ? CD  ? A LYS 153 CD  
44  1 Y 1 A LYS 222  ? CE  ? A LYS 153 CE  
45  1 Y 1 A LYS 222  ? NZ  ? A LYS 153 NZ  
46  1 Y 1 A LYS 226  ? CG  ? A LYS 157 CG  
47  1 Y 1 A LYS 226  ? CD  ? A LYS 157 CD  
48  1 Y 1 A LYS 226  ? CE  ? A LYS 157 CE  
49  1 Y 1 A LYS 226  ? NZ  ? A LYS 157 NZ  
50  1 Y 1 A ARG 230  ? CG  ? A ARG 161 CG  
51  1 Y 1 A ARG 230  ? CD  ? A ARG 161 CD  
52  1 Y 1 A ARG 230  ? NE  ? A ARG 161 NE  
53  1 Y 1 A ARG 230  ? CZ  ? A ARG 161 CZ  
54  1 Y 1 A ARG 230  ? NH1 ? A ARG 161 NH1 
55  1 Y 1 A ARG 230  ? NH2 ? A ARG 161 NH2 
56  1 Y 1 A LEU 268  ? CG  ? A LEU 199 CG  
57  1 Y 1 A LEU 268  ? CD1 ? A LEU 199 CD1 
58  1 Y 1 A LEU 268  ? CD2 ? A LEU 199 CD2 
59  1 Y 1 A LYS 269  ? CG  ? A LYS 200 CG  
60  1 Y 1 A LYS 269  ? CD  ? A LYS 200 CD  
61  1 Y 1 A LYS 269  ? CE  ? A LYS 200 CE  
62  1 Y 1 A LYS 269  ? NZ  ? A LYS 200 NZ  
63  1 Y 1 A GLU 328  ? CG  ? A GLU 259 CG  
64  1 Y 1 A GLU 328  ? CD  ? A GLU 259 CD  
65  1 Y 1 A GLU 328  ? OE1 ? A GLU 259 OE1 
66  1 Y 1 A GLU 328  ? OE2 ? A GLU 259 OE2 
67  1 Y 1 A LYS 364  ? CG  ? A LYS 295 CG  
68  1 Y 1 A LYS 364  ? CD  ? A LYS 295 CD  
69  1 Y 1 A LYS 364  ? CE  ? A LYS 295 CE  
70  1 Y 1 A LYS 364  ? NZ  ? A LYS 295 NZ  
71  1 Y 1 A LYS 407  ? CG  ? A LYS 338 CG  
72  1 Y 1 A LYS 407  ? CD  ? A LYS 338 CD  
73  1 Y 1 A LYS 407  ? CE  ? A LYS 338 CE  
74  1 Y 1 A LYS 407  ? NZ  ? A LYS 338 NZ  
75  1 Y 1 B GLU 27   ? CG  ? B GLU 27  CG  
76  1 Y 1 B GLU 27   ? CD  ? B GLU 27  CD  
77  1 Y 1 B GLU 27   ? OE1 ? B GLU 27  OE1 
78  1 Y 1 B GLU 27   ? OE2 ? B GLU 27  OE2 
79  1 Y 1 B GLU 47   ? CG  ? B GLU 47  CG  
80  1 Y 1 B GLU 47   ? CD  ? B GLU 47  CD  
81  1 Y 1 B GLU 47   ? OE1 ? B GLU 47  OE1 
82  1 Y 1 B GLU 47   ? OE2 ? B GLU 47  OE2 
83  1 Y 1 B LYS 70   ? CG  ? B LYS 70  CG  
84  1 Y 1 B LYS 70   ? CD  ? B LYS 70  CD  
85  1 Y 1 B LYS 70   ? CE  ? B LYS 70  CE  
86  1 Y 1 B LYS 70   ? NZ  ? B LYS 70  NZ  
87  1 Y 1 B LYS 92   ? CG  ? B LYS 92  CG  
88  1 Y 1 B LYS 92   ? CD  ? B LYS 92  CD  
89  1 Y 1 B LYS 92   ? CE  ? B LYS 92  CE  
90  1 Y 1 B LYS 92   ? NZ  ? B LYS 92  NZ  
91  1 Y 1 B GLU 96   ? CG  ? B GLU 96  CG  
92  1 Y 1 B GLU 96   ? CD  ? B GLU 96  CD  
93  1 Y 1 B GLU 96   ? OE1 ? B GLU 96  OE1 
94  1 Y 1 B GLU 96   ? OE2 ? B GLU 96  OE2 
95  1 Y 1 B ARG 111  ? CG  ? B ARG 111 CG  
96  1 Y 1 B ARG 111  ? CD  ? B ARG 111 CD  
97  1 Y 1 B ARG 111  ? NE  ? B ARG 111 NE  
98  1 Y 1 B ARG 111  ? CZ  ? B ARG 111 CZ  
99  1 Y 1 B ARG 111  ? NH1 ? B ARG 111 NH1 
100 1 Y 1 B ARG 111  ? NH2 ? B ARG 111 NH2 
101 1 Y 1 B ARG 114  ? CG  ? B ARG 114 CG  
102 1 Y 1 B ARG 114  ? CD  ? B ARG 114 CD  
103 1 Y 1 B ARG 114  ? NE  ? B ARG 114 NE  
104 1 Y 1 B ARG 114  ? CZ  ? B ARG 114 CZ  
105 1 Y 1 B ARG 114  ? NH1 ? B ARG 114 NH1 
106 1 Y 1 B ARG 114  ? NH2 ? B ARG 114 NH2 
107 1 Y 1 B ARG 147  ? CG  ? B ARG 147 CG  
108 1 Y 1 B ARG 147  ? CD  ? B ARG 147 CD  
109 1 Y 1 B ARG 147  ? NE  ? B ARG 147 NE  
110 1 Y 1 B ARG 147  ? CZ  ? B ARG 147 CZ  
111 1 Y 1 B ARG 147  ? NH1 ? B ARG 147 NH1 
112 1 Y 1 B ARG 147  ? NH2 ? B ARG 147 NH2 
113 1 Y 1 B LYS 150  ? CG  ? B LYS 150 CG  
114 1 Y 1 B LYS 150  ? CD  ? B LYS 150 CD  
115 1 Y 1 B LYS 150  ? CE  ? B LYS 150 CE  
116 1 Y 1 B LYS 150  ? NZ  ? B LYS 150 NZ  
117 1 Y 1 B LYS 153  ? CG  ? B LYS 153 CG  
118 1 Y 1 B LYS 153  ? CD  ? B LYS 153 CD  
119 1 Y 1 B LYS 153  ? CE  ? B LYS 153 CE  
120 1 Y 1 B LYS 153  ? NZ  ? B LYS 153 NZ  
121 1 Y 1 B ARG 198  ? CG  ? B ARG 198 CG  
122 1 Y 1 B ARG 198  ? CD  ? B ARG 198 CD  
123 1 Y 1 B ARG 198  ? NE  ? B ARG 198 NE  
124 1 Y 1 B ARG 198  ? CZ  ? B ARG 198 CZ  
125 1 Y 1 B ARG 198  ? NH1 ? B ARG 198 NH1 
126 1 Y 1 B ARG 198  ? NH2 ? B ARG 198 NH2 
127 1 Y 1 B LYS 204  ? CG  ? B LYS 204 CG  
128 1 Y 1 B LYS 204  ? CD  ? B LYS 204 CD  
129 1 Y 1 B LYS 204  ? CE  ? B LYS 204 CE  
130 1 Y 1 B LYS 204  ? NZ  ? B LYS 204 NZ  
131 1 Y 1 B GLU 210  ? CG  ? B GLU 210 CG  
132 1 Y 1 B GLU 210  ? CD  ? B GLU 210 CD  
133 1 Y 1 B GLU 210  ? OE1 ? B GLU 210 OE1 
134 1 Y 1 B GLU 210  ? OE2 ? B GLU 210 OE2 
135 1 Y 1 B GLN 234  ? CG  ? B GLN 234 CG  
136 1 Y 1 B GLN 234  ? CD  ? B GLN 234 CD  
137 1 Y 1 B GLN 234  ? OE1 ? B GLN 234 OE1 
138 1 Y 1 B GLN 234  ? NE2 ? B GLN 234 NE2 
139 1 Y 1 B LYS 244  ? CG  ? B LYS 244 CG  
140 1 Y 1 B LYS 244  ? CD  ? B LYS 244 CD  
141 1 Y 1 B LYS 244  ? CE  ? B LYS 244 CE  
142 1 Y 1 B LYS 244  ? NZ  ? B LYS 244 NZ  
143 1 Y 1 B LYS 287  ? CG  ? B LYS 287 CG  
144 1 Y 1 B LYS 287  ? CD  ? B LYS 287 CD  
145 1 Y 1 B LYS 287  ? CE  ? B LYS 287 CE  
146 1 Y 1 B LYS 287  ? NZ  ? B LYS 287 NZ  
147 1 Y 1 B GLU 289  ? CG  ? B GLU 289 CG  
148 1 Y 1 B GLU 289  ? CD  ? B GLU 289 CD  
149 1 Y 1 B GLU 289  ? OE1 ? B GLU 289 OE1 
150 1 Y 1 B GLU 289  ? OE2 ? B GLU 289 OE2 
151 1 Y 1 B LYS 335  ? CG  ? B LYS 335 CG  
152 1 Y 1 B LYS 335  ? CD  ? B LYS 335 CD  
153 1 Y 1 B LYS 335  ? CE  ? B LYS 335 CE  
154 1 Y 1 B LYS 335  ? NZ  ? B LYS 335 NZ  
155 1 Y 1 B VAL 338  ? CG1 ? B VAL 338 CG1 
156 1 Y 1 B VAL 338  ? CG2 ? B VAL 338 CG2 
157 1 Y 1 B ASP 339  ? CG  ? B ASP 339 CG  
158 1 Y 1 B ASP 339  ? OD1 ? B ASP 339 OD1 
159 1 Y 1 B ASP 339  ? OD2 ? B ASP 339 OD2 
160 1 Y 1 B GLU 342  ? CG  ? B GLU 342 CG  
161 1 Y 1 B GLU 342  ? CD  ? B GLU 342 CD  
162 1 Y 1 B GLU 342  ? OE1 ? B GLU 342 OE1 
163 1 Y 1 B GLU 342  ? OE2 ? B GLU 342 OE2 
164 1 Y 1 B GLN 343  ? CG  ? B GLN 343 CG  
165 1 Y 1 B GLN 343  ? CD  ? B GLN 343 CD  
166 1 Y 1 B GLN 343  ? OE1 ? B GLN 343 OE1 
167 1 Y 1 B GLN 343  ? NE2 ? B GLN 343 NE2 
168 1 Y 1 B GLN 731  ? CG  ? B GLN 427 CG  
169 1 Y 1 B GLN 731  ? CD  ? B GLN 427 CD  
170 1 Y 1 B GLN 731  ? OE1 ? B GLN 427 OE1 
171 1 Y 1 B GLN 731  ? NE2 ? B GLN 427 NE2 
172 1 Y 1 B LYS 769  ? CG  ? B LYS 465 CG  
173 1 Y 1 B LYS 769  ? CD  ? B LYS 465 CD  
174 1 Y 1 B LYS 769  ? CE  ? B LYS 465 CE  
175 1 Y 1 B LYS 769  ? NZ  ? B LYS 465 NZ  
176 1 Y 1 B HIS 778  ? CG  ? B HIS 474 CG  
177 1 Y 1 B HIS 778  ? ND1 ? B HIS 474 ND1 
178 1 Y 1 B HIS 778  ? CD2 ? B HIS 474 CD2 
179 1 Y 1 B HIS 778  ? CE1 ? B HIS 474 CE1 
180 1 Y 1 B HIS 778  ? NE2 ? B HIS 474 NE2 
181 1 Y 1 B GLU 779  ? CG  ? B GLU 475 CG  
182 1 Y 1 B GLU 779  ? CD  ? B GLU 475 CD  
183 1 Y 1 B GLU 779  ? OE1 ? B GLU 475 OE1 
184 1 Y 1 B GLU 779  ? OE2 ? B GLU 475 OE2 
185 1 Y 1 B LYS 820  ? CG  ? B LYS 516 CG  
186 1 Y 1 B LYS 820  ? CD  ? B LYS 516 CD  
187 1 Y 1 B LYS 820  ? CE  ? B LYS 516 CE  
188 1 Y 1 B LYS 820  ? NZ  ? B LYS 516 NZ  
189 1 Y 1 B LYS 823  ? CG  ? B LYS 519 CG  
190 1 Y 1 B LYS 823  ? CD  ? B LYS 519 CD  
191 1 Y 1 B LYS 823  ? CE  ? B LYS 519 CE  
192 1 Y 1 B LYS 823  ? NZ  ? B LYS 519 NZ  
193 1 Y 1 B GLU 840  ? CG  ? B GLU 536 CG  
194 1 Y 1 B GLU 840  ? CD  ? B GLU 536 CD  
195 1 Y 1 B GLU 840  ? OE1 ? B GLU 536 OE1 
196 1 Y 1 B GLU 840  ? OE2 ? B GLU 536 OE2 
197 1 Y 1 B LYS 844  ? CG  ? B LYS 540 CG  
198 1 Y 1 B LYS 844  ? CD  ? B LYS 540 CD  
199 1 Y 1 B LYS 844  ? CE  ? B LYS 540 CE  
200 1 Y 1 B LYS 844  ? NZ  ? B LYS 540 NZ  
201 1 Y 1 B LYS 857  ? CG  ? B LYS 553 CG  
202 1 Y 1 B LYS 857  ? CD  ? B LYS 553 CD  
203 1 Y 1 B LYS 857  ? CE  ? B LYS 553 CE  
204 1 Y 1 B LYS 857  ? NZ  ? B LYS 553 NZ  
205 1 Y 1 B LYS 864  ? CG  ? B LYS 560 CG  
206 1 Y 1 B LYS 864  ? CD  ? B LYS 560 CD  
207 1 Y 1 B LYS 864  ? CE  ? B LYS 560 CE  
208 1 Y 1 B LYS 864  ? NZ  ? B LYS 560 NZ  
209 1 Y 1 B LYS 867  ? CG  ? B LYS 563 CG  
210 1 Y 1 B LYS 867  ? CD  ? B LYS 563 CD  
211 1 Y 1 B LYS 867  ? CE  ? B LYS 563 CE  
212 1 Y 1 B LYS 867  ? NZ  ? B LYS 563 NZ  
213 1 Y 1 B LYS 879  ? CG  ? B LYS 575 CG  
214 1 Y 1 B LYS 879  ? CD  ? B LYS 575 CD  
215 1 Y 1 B LYS 879  ? CE  ? B LYS 575 CE  
216 1 Y 1 B LYS 879  ? NZ  ? B LYS 575 NZ  
217 1 Y 1 B LYS 897  ? CG  ? B LYS 593 CG  
218 1 Y 1 B LYS 897  ? CD  ? B LYS 593 CD  
219 1 Y 1 B LYS 897  ? CE  ? B LYS 593 CE  
220 1 Y 1 B LYS 897  ? NZ  ? B LYS 593 NZ  
221 1 Y 1 B ARG 900  ? CG  ? B ARG 596 CG  
222 1 Y 1 B ARG 900  ? CD  ? B ARG 596 CD  
223 1 Y 1 B ARG 900  ? NE  ? B ARG 596 NE  
224 1 Y 1 B ARG 900  ? CZ  ? B ARG 596 CZ  
225 1 Y 1 B ARG 900  ? NH1 ? B ARG 596 NH1 
226 1 Y 1 B ARG 900  ? NH2 ? B ARG 596 NH2 
227 1 Y 1 B LYS 917  ? CG  ? B LYS 613 CG  
228 1 Y 1 B LYS 917  ? CD  ? B LYS 613 CD  
229 1 Y 1 B LYS 917  ? CE  ? B LYS 613 CE  
230 1 Y 1 B LYS 917  ? NZ  ? B LYS 613 NZ  
231 1 Y 1 B LYS 936  ? CG  ? B LYS 632 CG  
232 1 Y 1 B LYS 936  ? CD  ? B LYS 632 CD  
233 1 Y 1 B LYS 936  ? CE  ? B LYS 632 CE  
234 1 Y 1 B LYS 936  ? NZ  ? B LYS 632 NZ  
235 1 Y 1 B GLU 943  ? CG  ? B GLU 639 CG  
236 1 Y 1 B GLU 943  ? CD  ? B GLU 639 CD  
237 1 Y 1 B GLU 943  ? OE1 ? B GLU 639 OE1 
238 1 Y 1 B GLU 943  ? OE2 ? B GLU 639 OE2 
239 1 Y 1 B GLU 944  ? CG  ? B GLU 640 CG  
240 1 Y 1 B GLU 944  ? CD  ? B GLU 640 CD  
241 1 Y 1 B GLU 944  ? OE1 ? B GLU 640 OE1 
242 1 Y 1 B GLU 944  ? OE2 ? B GLU 640 OE2 
243 1 Y 1 B ARG 947  ? CG  ? B ARG 643 CG  
244 1 Y 1 B ARG 947  ? CD  ? B ARG 643 CD  
245 1 Y 1 B ARG 947  ? NE  ? B ARG 643 NE  
246 1 Y 1 B ARG 947  ? CZ  ? B ARG 643 CZ  
247 1 Y 1 B ARG 947  ? NH1 ? B ARG 643 NH1 
248 1 Y 1 B ARG 947  ? NH2 ? B ARG 643 NH2 
249 1 Y 1 B ASP 986  ? CG  ? B ASP 682 CG  
250 1 Y 1 B ASP 986  ? OD1 ? B ASP 682 OD1 
251 1 Y 1 B ASP 986  ? OD2 ? B ASP 682 OD2 
252 1 Y 1 B GLU 987  ? CG  ? B GLU 683 CG  
253 1 Y 1 B GLU 987  ? CD  ? B GLU 683 CD  
254 1 Y 1 B GLU 987  ? OE1 ? B GLU 683 OE1 
255 1 Y 1 B GLU 987  ? OE2 ? B GLU 683 OE2 
256 1 Y 1 B GLU 988  ? CG  ? B GLU 684 CG  
257 1 Y 1 B GLU 988  ? CD  ? B GLU 684 CD  
258 1 Y 1 B GLU 988  ? OE1 ? B GLU 684 OE1 
259 1 Y 1 B GLU 988  ? OE2 ? B GLU 684 OE2 
260 1 Y 1 B GLN 990  ? CG  ? B GLN 686 CG  
261 1 Y 1 B GLN 990  ? CD  ? B GLN 686 CD  
262 1 Y 1 B GLN 990  ? OE1 ? B GLN 686 OE1 
263 1 Y 1 B GLN 990  ? NE2 ? B GLN 686 NE2 
264 1 Y 1 B GLU 994  ? CG  ? B GLU 690 CG  
265 1 Y 1 B GLU 994  ? CD  ? B GLU 690 CD  
266 1 Y 1 B GLU 994  ? OE1 ? B GLU 690 OE1 
267 1 Y 1 B GLU 994  ? OE2 ? B GLU 690 OE2 
268 1 Y 1 B GLN 1025 ? CG  ? B GLN 721 CG  
269 1 Y 1 B GLN 1025 ? CD  ? B GLN 721 CD  
270 1 Y 1 B GLN 1025 ? OE1 ? B GLN 721 OE1 
271 1 Y 1 B GLN 1025 ? NE2 ? B GLN 721 NE2 
272 1 Y 1 B LYS 1063 ? CG  ? B LYS 759 CG  
273 1 Y 1 B LYS 1063 ? CD  ? B LYS 759 CD  
274 1 Y 1 B LYS 1063 ? CE  ? B LYS 759 CE  
275 1 Y 1 B LYS 1063 ? NZ  ? B LYS 759 NZ  
276 1 Y 1 B GLU 1079 ? CG  ? B GLU 775 CG  
277 1 Y 1 B GLU 1079 ? CD  ? B GLU 775 CD  
278 1 Y 1 B GLU 1079 ? OE1 ? B GLU 775 OE1 
279 1 Y 1 B GLU 1079 ? OE2 ? B GLU 775 OE2 
280 1 Y 1 B ARG 1080 ? CG  ? B ARG 776 CG  
281 1 Y 1 B ARG 1080 ? CD  ? B ARG 776 CD  
282 1 Y 1 B ARG 1080 ? NE  ? B ARG 776 NE  
283 1 Y 1 B ARG 1080 ? CZ  ? B ARG 776 CZ  
284 1 Y 1 B ARG 1080 ? NH1 ? B ARG 776 NH1 
285 1 Y 1 B ARG 1080 ? NH2 ? B ARG 776 NH2 
286 1 Y 1 B LYS 1081 ? CG  ? B LYS 777 CG  
287 1 Y 1 B LYS 1081 ? CD  ? B LYS 777 CD  
288 1 Y 1 B LYS 1081 ? CE  ? B LYS 777 CE  
289 1 Y 1 B LYS 1081 ? NZ  ? B LYS 777 NZ  
290 1 Y 1 B GLU 1083 ? CG  ? B GLU 779 CG  
291 1 Y 1 B GLU 1083 ? CD  ? B GLU 779 CD  
292 1 Y 1 B GLU 1083 ? OE1 ? B GLU 779 OE1 
293 1 Y 1 B GLU 1083 ? OE2 ? B GLU 779 OE2 
294 1 Y 1 B LYS 1104 ? CG  ? B LYS 800 CG  
295 1 Y 1 B LYS 1104 ? CD  ? B LYS 800 CD  
296 1 Y 1 B LYS 1104 ? CE  ? B LYS 800 CE  
297 1 Y 1 B LYS 1104 ? NZ  ? B LYS 800 NZ  
298 1 Y 1 B GLU 1123 ? CG  ? B GLU 819 CG  
299 1 Y 1 B GLU 1123 ? CD  ? B GLU 819 CD  
300 1 Y 1 B GLU 1123 ? OE1 ? B GLU 819 OE1 
301 1 Y 1 B GLU 1123 ? OE2 ? B GLU 819 OE2 
302 1 Y 1 B LYS 1131 ? CG  ? B LYS 827 CG  
303 1 Y 1 B LYS 1131 ? CD  ? B LYS 827 CD  
304 1 Y 1 B LYS 1131 ? CE  ? B LYS 827 CE  
305 1 Y 1 B LYS 1131 ? NZ  ? B LYS 827 NZ  
306 1 Y 1 B GLU 1134 ? CG  ? B GLU 830 CG  
307 1 Y 1 B GLU 1134 ? CD  ? B GLU 830 CD  
308 1 Y 1 B GLU 1134 ? OE1 ? B GLU 830 OE1 
309 1 Y 1 B GLU 1134 ? OE2 ? B GLU 830 OE2 
310 1 Y 1 B GLU 1135 ? CG  ? B GLU 831 CG  
311 1 Y 1 B GLU 1135 ? CD  ? B GLU 831 CD  
312 1 Y 1 B GLU 1135 ? OE1 ? B GLU 831 OE1 
313 1 Y 1 B GLU 1135 ? OE2 ? B GLU 831 OE2 
314 1 Y 1 B ARG 1138 ? CG  ? B ARG 834 CG  
315 1 Y 1 B ARG 1138 ? CD  ? B ARG 834 CD  
316 1 Y 1 B ARG 1138 ? NE  ? B ARG 834 NE  
317 1 Y 1 B ARG 1138 ? CZ  ? B ARG 834 CZ  
318 1 Y 1 B ARG 1138 ? NH1 ? B ARG 834 NH1 
319 1 Y 1 B ARG 1138 ? NH2 ? B ARG 834 NH2 
320 1 Y 1 C GLU 880  ? CG  ? C GLU 15  CG  
321 1 Y 1 C GLU 880  ? CD  ? C GLU 15  CD  
322 1 Y 1 C GLU 880  ? OE1 ? C GLU 15  OE1 
323 1 Y 1 C GLU 880  ? OE2 ? C GLU 15  OE2 
324 1 Y 1 C ARG 882  ? CG  ? C ARG 17  CG  
325 1 Y 1 C ARG 882  ? CD  ? C ARG 17  CD  
326 1 Y 1 C ARG 882  ? NE  ? C ARG 17  NE  
327 1 Y 1 C ARG 882  ? CZ  ? C ARG 17  CZ  
328 1 Y 1 C ARG 882  ? NH1 ? C ARG 17  NH1 
329 1 Y 1 C ARG 882  ? NH2 ? C ARG 17  NH2 
330 1 Y 1 C ARG 890  ? CG  ? C ARG 25  CG  
331 1 Y 1 C ARG 890  ? CD  ? C ARG 25  CD  
332 1 Y 1 C ARG 890  ? NE  ? C ARG 25  NE  
333 1 Y 1 C ARG 890  ? CZ  ? C ARG 25  CZ  
334 1 Y 1 C ARG 890  ? NH1 ? C ARG 25  NH1 
335 1 Y 1 C ARG 890  ? NH2 ? C ARG 25  NH2 
336 1 Y 1 D LEU 84   ? CG  ? D LEU 15  CG  
337 1 Y 1 D LEU 84   ? CD1 ? D LEU 15  CD1 
338 1 Y 1 D LEU 84   ? CD2 ? D LEU 15  CD2 
339 1 Y 1 D GLN 86   ? CG  ? D GLN 17  CG  
340 1 Y 1 D GLN 86   ? CD  ? D GLN 17  CD  
341 1 Y 1 D GLN 86   ? OE1 ? D GLN 17  OE1 
342 1 Y 1 D GLN 86   ? NE2 ? D GLN 17  NE2 
343 1 Y 1 D MET 88   ? CG  ? D MET 19  CG  
344 1 Y 1 D MET 88   ? SD  ? D MET 19  SD  
345 1 Y 1 D MET 88   ? CE  ? D MET 19  CE  
346 1 Y 1 D GLN 100  ? CG  ? D GLN 31  CG  
347 1 Y 1 D GLN 100  ? CD  ? D GLN 31  CD  
348 1 Y 1 D GLN 100  ? OE1 ? D GLN 31  OE1 
349 1 Y 1 D GLN 100  ? NE2 ? D GLN 31  NE2 
350 1 Y 1 D GLN 105  ? CG  ? D GLN 36  CG  
351 1 Y 1 D GLN 105  ? CD  ? D GLN 36  CD  
352 1 Y 1 D GLN 105  ? OE1 ? D GLN 36  OE1 
353 1 Y 1 D GLN 105  ? NE2 ? D GLN 36  NE2 
354 1 Y 1 D GLU 106  ? CG  ? D GLU 37  CG  
355 1 Y 1 D GLU 106  ? CD  ? D GLU 37  CD  
356 1 Y 1 D GLU 106  ? OE1 ? D GLU 37  OE1 
357 1 Y 1 D GLU 106  ? OE2 ? D GLU 37  OE2 
358 1 Y 1 D ARG 111  ? CG  ? D ARG 42  CG  
359 1 Y 1 D ARG 111  ? CD  ? D ARG 42  CD  
360 1 Y 1 D ARG 111  ? NE  ? D ARG 42  NE  
361 1 Y 1 D ARG 111  ? CZ  ? D ARG 42  CZ  
362 1 Y 1 D ARG 111  ? NH1 ? D ARG 42  NH1 
363 1 Y 1 D ARG 111  ? NH2 ? D ARG 42  NH2 
364 1 Y 1 D GLN 115  ? CG  ? D GLN 46  CG  
365 1 Y 1 D GLN 115  ? CD  ? D GLN 46  CD  
366 1 Y 1 D GLN 115  ? OE1 ? D GLN 46  OE1 
367 1 Y 1 D GLN 115  ? NE2 ? D GLN 46  NE2 
368 1 Y 1 D LYS 116  ? CG  ? D LYS 47  CG  
369 1 Y 1 D LYS 116  ? CD  ? D LYS 47  CD  
370 1 Y 1 D LYS 116  ? CE  ? D LYS 47  CE  
371 1 Y 1 D LYS 116  ? NZ  ? D LYS 47  NZ  
372 1 Y 1 D ARG 118  ? CG  ? D ARG 49  CG  
373 1 Y 1 D ARG 118  ? CD  ? D ARG 49  CD  
374 1 Y 1 D ARG 118  ? NE  ? D ARG 49  NE  
375 1 Y 1 D ARG 118  ? CZ  ? D ARG 49  CZ  
376 1 Y 1 D ARG 118  ? NH1 ? D ARG 49  NH1 
377 1 Y 1 D ARG 118  ? NH2 ? D ARG 49  NH2 
378 1 Y 1 D ARG 145  ? CG  ? D ARG 76  CG  
379 1 Y 1 D ARG 145  ? CD  ? D ARG 76  CD  
380 1 Y 1 D ARG 145  ? NE  ? D ARG 76  NE  
381 1 Y 1 D ARG 145  ? CZ  ? D ARG 76  CZ  
382 1 Y 1 D ARG 145  ? NH1 ? D ARG 76  NH1 
383 1 Y 1 D ARG 145  ? NH2 ? D ARG 76  NH2 
384 1 Y 1 D GLN 148  ? CG  ? D GLN 79  CG  
385 1 Y 1 D GLN 148  ? CD  ? D GLN 79  CD  
386 1 Y 1 D GLN 148  ? OE1 ? D GLN 79  OE1 
387 1 Y 1 D GLN 148  ? NE2 ? D GLN 79  NE2 
388 1 Y 1 D ASP 149  ? CG  ? D ASP 80  CG  
389 1 Y 1 D ASP 149  ? OD1 ? D ASP 80  OD1 
390 1 Y 1 D ASP 149  ? OD2 ? D ASP 80  OD2 
391 1 Y 1 D PHE 150  ? CG  ? D PHE 81  CG  
392 1 Y 1 D PHE 150  ? CD1 ? D PHE 81  CD1 
393 1 Y 1 D PHE 150  ? CD2 ? D PHE 81  CD2 
394 1 Y 1 D PHE 150  ? CE1 ? D PHE 81  CE1 
395 1 Y 1 D PHE 150  ? CE2 ? D PHE 81  CE2 
396 1 Y 1 D PHE 150  ? CZ  ? D PHE 81  CZ  
397 1 Y 1 D ILE 152  ? CG1 ? D ILE 83  CG1 
398 1 Y 1 D ILE 152  ? CG2 ? D ILE 83  CG2 
399 1 Y 1 D ILE 152  ? CD1 ? D ILE 83  CD1 
400 1 Y 1 D LYS 158  ? CG  ? D LYS 89  CG  
401 1 Y 1 D LYS 158  ? CD  ? D LYS 89  CD  
402 1 Y 1 D LYS 158  ? CE  ? D LYS 89  CE  
403 1 Y 1 D LYS 158  ? NZ  ? D LYS 89  NZ  
404 1 Y 1 D LYS 166  ? CG  ? D LYS 97  CG  
405 1 Y 1 D LYS 166  ? CD  ? D LYS 97  CD  
406 1 Y 1 D LYS 166  ? CE  ? D LYS 97  CE  
407 1 Y 1 D LYS 166  ? NZ  ? D LYS 97  NZ  
408 1 Y 1 D GLU 169  ? CG  ? D GLU 100 CG  
409 1 Y 1 D GLU 169  ? CD  ? D GLU 100 CD  
410 1 Y 1 D GLU 169  ? OE1 ? D GLU 100 OE1 
411 1 Y 1 D GLU 169  ? OE2 ? D GLU 100 OE2 
412 1 Y 1 D LEU 170  ? CG  ? D LEU 101 CG  
413 1 Y 1 D LEU 170  ? CD1 ? D LEU 101 CD1 
414 1 Y 1 D LEU 170  ? CD2 ? D LEU 101 CD2 
415 1 Y 1 D ARG 171  ? CG  ? D ARG 102 CG  
416 1 Y 1 D ARG 171  ? CD  ? D ARG 102 CD  
417 1 Y 1 D ARG 171  ? NE  ? D ARG 102 NE  
418 1 Y 1 D ARG 171  ? CZ  ? D ARG 102 CZ  
419 1 Y 1 D ARG 171  ? NH1 ? D ARG 102 NH1 
420 1 Y 1 D ARG 171  ? NH2 ? D ARG 102 NH2 
421 1 Y 1 D GLN 173  ? CG  ? D GLN 104 CG  
422 1 Y 1 D GLN 173  ? CD  ? D GLN 104 CD  
423 1 Y 1 D GLN 173  ? OE1 ? D GLN 104 OE1 
424 1 Y 1 D GLN 173  ? NE2 ? D GLN 104 NE2 
425 1 Y 1 D ASP 175  ? CG  ? D ASP 106 CG  
426 1 Y 1 D ASP 175  ? OD1 ? D ASP 106 OD1 
427 1 Y 1 D ASP 175  ? OD2 ? D ASP 106 OD2 
428 1 Y 1 D LYS 181  ? CG  ? D LYS 112 CG  
429 1 Y 1 D LYS 181  ? CD  ? D LYS 112 CD  
430 1 Y 1 D LYS 181  ? CE  ? D LYS 112 CE  
431 1 Y 1 D LYS 181  ? NZ  ? D LYS 112 NZ  
432 1 Y 1 D LYS 204  ? CG  ? D LYS 135 CG  
433 1 Y 1 D LYS 204  ? CD  ? D LYS 135 CD  
434 1 Y 1 D LYS 204  ? CE  ? D LYS 135 CE  
435 1 Y 1 D LYS 204  ? NZ  ? D LYS 135 NZ  
436 1 Y 1 D TYR 221  ? CG  ? D TYR 152 CG  
437 1 Y 1 D TYR 221  ? CD1 ? D TYR 152 CD1 
438 1 Y 1 D TYR 221  ? CD2 ? D TYR 152 CD2 
439 1 Y 1 D TYR 221  ? CE1 ? D TYR 152 CE1 
440 1 Y 1 D TYR 221  ? CE2 ? D TYR 152 CE2 
441 1 Y 1 D TYR 221  ? CZ  ? D TYR 152 CZ  
442 1 Y 1 D TYR 221  ? OH  ? D TYR 152 OH  
443 1 Y 1 D LYS 222  ? CG  ? D LYS 153 CG  
444 1 Y 1 D LYS 222  ? CD  ? D LYS 153 CD  
445 1 Y 1 D LYS 222  ? CE  ? D LYS 153 CE  
446 1 Y 1 D LYS 222  ? NZ  ? D LYS 153 NZ  
447 1 Y 1 D LYS 226  ? CG  ? D LYS 157 CG  
448 1 Y 1 D LYS 226  ? CD  ? D LYS 157 CD  
449 1 Y 1 D LYS 226  ? CE  ? D LYS 157 CE  
450 1 Y 1 D LYS 226  ? NZ  ? D LYS 157 NZ  
451 1 Y 1 D ARG 230  ? CG  ? D ARG 161 CG  
452 1 Y 1 D ARG 230  ? CD  ? D ARG 161 CD  
453 1 Y 1 D ARG 230  ? NE  ? D ARG 161 NE  
454 1 Y 1 D ARG 230  ? CZ  ? D ARG 161 CZ  
455 1 Y 1 D ARG 230  ? NH1 ? D ARG 161 NH1 
456 1 Y 1 D ARG 230  ? NH2 ? D ARG 161 NH2 
457 1 Y 1 D GLU 251  ? CG  ? D GLU 182 CG  
458 1 Y 1 D GLU 251  ? CD  ? D GLU 182 CD  
459 1 Y 1 D GLU 251  ? OE1 ? D GLU 182 OE1 
460 1 Y 1 D GLU 251  ? OE2 ? D GLU 182 OE2 
461 1 Y 1 D ARG 262  ? CG  ? D ARG 193 CG  
462 1 Y 1 D ARG 262  ? CD  ? D ARG 193 CD  
463 1 Y 1 D ARG 262  ? NE  ? D ARG 193 NE  
464 1 Y 1 D ARG 262  ? CZ  ? D ARG 193 CZ  
465 1 Y 1 D ARG 262  ? NH1 ? D ARG 193 NH1 
466 1 Y 1 D ARG 262  ? NH2 ? D ARG 193 NH2 
467 1 Y 1 D ASN 267  ? CG  ? D ASN 198 CG  
468 1 Y 1 D ASN 267  ? OD1 ? D ASN 198 OD1 
469 1 Y 1 D ASN 267  ? ND2 ? D ASN 198 ND2 
470 1 Y 1 D LEU 268  ? CG  ? D LEU 199 CG  
471 1 Y 1 D LEU 268  ? CD1 ? D LEU 199 CD1 
472 1 Y 1 D LEU 268  ? CD2 ? D LEU 199 CD2 
473 1 Y 1 D LYS 269  ? CG  ? D LYS 200 CG  
474 1 Y 1 D LYS 269  ? CD  ? D LYS 200 CD  
475 1 Y 1 D LYS 269  ? CE  ? D LYS 200 CE  
476 1 Y 1 D LYS 269  ? NZ  ? D LYS 200 NZ  
477 1 Y 1 D ASP 271  ? CG  ? D ASP 202 CG  
478 1 Y 1 D ASP 271  ? OD1 ? D ASP 202 OD1 
479 1 Y 1 D ASP 271  ? OD2 ? D ASP 202 OD2 
480 1 Y 1 D TYR 363  ? CG  ? D TYR 294 CG  
481 1 Y 1 D TYR 363  ? CD1 ? D TYR 294 CD1 
482 1 Y 1 D TYR 363  ? CD2 ? D TYR 294 CD2 
483 1 Y 1 D TYR 363  ? CE1 ? D TYR 294 CE1 
484 1 Y 1 D TYR 363  ? CE2 ? D TYR 294 CE2 
485 1 Y 1 D TYR 363  ? CZ  ? D TYR 294 CZ  
486 1 Y 1 D TYR 363  ? OH  ? D TYR 294 OH  
487 1 Y 1 D LYS 364  ? CG  ? D LYS 295 CG  
488 1 Y 1 D LYS 364  ? CD  ? D LYS 295 CD  
489 1 Y 1 D LYS 364  ? CE  ? D LYS 295 CE  
490 1 Y 1 D LYS 364  ? NZ  ? D LYS 295 NZ  
491 1 Y 1 D ARG 373  ? CG  ? D ARG 304 CG  
492 1 Y 1 D ARG 373  ? CD  ? D ARG 304 CD  
493 1 Y 1 D ARG 373  ? NE  ? D ARG 304 NE  
494 1 Y 1 D ARG 373  ? CZ  ? D ARG 304 CZ  
495 1 Y 1 D ARG 373  ? NH1 ? D ARG 304 NH1 
496 1 Y 1 D ARG 373  ? NH2 ? D ARG 304 NH2 
497 1 Y 1 D GLU 377  ? CG  ? D GLU 308 CG  
498 1 Y 1 D GLU 377  ? CD  ? D GLU 308 CD  
499 1 Y 1 D GLU 377  ? OE1 ? D GLU 308 OE1 
500 1 Y 1 D GLU 377  ? OE2 ? D GLU 308 OE2 
501 1 Y 1 D LYS 406  ? CG  ? D LYS 337 CG  
502 1 Y 1 D LYS 406  ? CD  ? D LYS 337 CD  
503 1 Y 1 D LYS 406  ? CE  ? D LYS 337 CE  
504 1 Y 1 D LYS 406  ? NZ  ? D LYS 337 NZ  
505 1 Y 1 D LYS 407  ? CG  ? D LYS 338 CG  
506 1 Y 1 D LYS 407  ? CD  ? D LYS 338 CD  
507 1 Y 1 D LYS 407  ? CE  ? D LYS 338 CE  
508 1 Y 1 D LYS 407  ? NZ  ? D LYS 338 NZ  
509 1 Y 1 D ASP 408  ? CG  ? D ASP 339 CG  
510 1 Y 1 D ASP 408  ? OD1 ? D ASP 339 OD1 
511 1 Y 1 D ASP 408  ? OD2 ? D ASP 339 OD2 
512 1 Y 1 D LYS 413  ? CG  ? D LYS 344 CG  
513 1 Y 1 D LYS 413  ? CD  ? D LYS 344 CD  
514 1 Y 1 D LYS 413  ? CE  ? D LYS 344 CE  
515 1 Y 1 D LYS 413  ? NZ  ? D LYS 344 NZ  
516 1 Y 1 E LYS 11   ? CG  ? E LYS 11  CG  
517 1 Y 1 E LYS 11   ? CD  ? E LYS 11  CD  
518 1 Y 1 E LYS 11   ? CE  ? E LYS 11  CE  
519 1 Y 1 E LYS 11   ? NZ  ? E LYS 11  NZ  
520 1 Y 1 E GLU 27   ? CG  ? E GLU 27  CG  
521 1 Y 1 E GLU 27   ? CD  ? E GLU 27  CD  
522 1 Y 1 E GLU 27   ? OE1 ? E GLU 27  OE1 
523 1 Y 1 E GLU 27   ? OE2 ? E GLU 27  OE2 
524 1 Y 1 E GLU 47   ? CG  ? E GLU 47  CG  
525 1 Y 1 E GLU 47   ? CD  ? E GLU 47  CD  
526 1 Y 1 E GLU 47   ? OE1 ? E GLU 47  OE1 
527 1 Y 1 E GLU 47   ? OE2 ? E GLU 47  OE2 
528 1 Y 1 E ARG 50   ? CG  ? E ARG 50  CG  
529 1 Y 1 E ARG 50   ? CD  ? E ARG 50  CD  
530 1 Y 1 E ARG 50   ? NE  ? E ARG 50  NE  
531 1 Y 1 E ARG 50   ? CZ  ? E ARG 50  CZ  
532 1 Y 1 E ARG 50   ? NH1 ? E ARG 50  NH1 
533 1 Y 1 E ARG 50   ? NH2 ? E ARG 50  NH2 
534 1 Y 1 E LYS 53   ? CG  ? E LYS 53  CG  
535 1 Y 1 E LYS 53   ? CD  ? E LYS 53  CD  
536 1 Y 1 E LYS 53   ? CE  ? E LYS 53  CE  
537 1 Y 1 E LYS 53   ? NZ  ? E LYS 53  NZ  
538 1 Y 1 E ARG 68   ? CG  ? E ARG 68  CG  
539 1 Y 1 E ARG 68   ? CD  ? E ARG 68  CD  
540 1 Y 1 E ARG 68   ? NE  ? E ARG 68  NE  
541 1 Y 1 E ARG 68   ? CZ  ? E ARG 68  CZ  
542 1 Y 1 E ARG 68   ? NH1 ? E ARG 68  NH1 
543 1 Y 1 E ARG 68   ? NH2 ? E ARG 68  NH2 
544 1 Y 1 E LYS 70   ? CG  ? E LYS 70  CG  
545 1 Y 1 E LYS 70   ? CD  ? E LYS 70  CD  
546 1 Y 1 E LYS 70   ? CE  ? E LYS 70  CE  
547 1 Y 1 E LYS 70   ? NZ  ? E LYS 70  NZ  
548 1 Y 1 E GLU 90   ? CG  ? E GLU 90  CG  
549 1 Y 1 E GLU 90   ? CD  ? E GLU 90  CD  
550 1 Y 1 E GLU 90   ? OE1 ? E GLU 90  OE1 
551 1 Y 1 E GLU 90   ? OE2 ? E GLU 90  OE2 
552 1 Y 1 E LYS 92   ? CG  ? E LYS 92  CG  
553 1 Y 1 E LYS 92   ? CD  ? E LYS 92  CD  
554 1 Y 1 E LYS 92   ? CE  ? E LYS 92  CE  
555 1 Y 1 E LYS 92   ? NZ  ? E LYS 92  NZ  
556 1 Y 1 E GLU 96   ? CG  ? E GLU 96  CG  
557 1 Y 1 E GLU 96   ? CD  ? E GLU 96  CD  
558 1 Y 1 E GLU 96   ? OE1 ? E GLU 96  OE1 
559 1 Y 1 E GLU 96   ? OE2 ? E GLU 96  OE2 
560 1 Y 1 E ASP 99   ? CG  ? E ASP 99  CG  
561 1 Y 1 E ASP 99   ? OD1 ? E ASP 99  OD1 
562 1 Y 1 E ASP 99   ? OD2 ? E ASP 99  OD2 
563 1 Y 1 E ARG 103  ? CG  ? E ARG 103 CG  
564 1 Y 1 E ARG 103  ? CD  ? E ARG 103 CD  
565 1 Y 1 E ARG 103  ? NE  ? E ARG 103 NE  
566 1 Y 1 E ARG 103  ? CZ  ? E ARG 103 CZ  
567 1 Y 1 E ARG 103  ? NH1 ? E ARG 103 NH1 
568 1 Y 1 E ARG 103  ? NH2 ? E ARG 103 NH2 
569 1 Y 1 E ARG 111  ? CG  ? E ARG 111 CG  
570 1 Y 1 E ARG 111  ? CD  ? E ARG 111 CD  
571 1 Y 1 E ARG 111  ? NE  ? E ARG 111 NE  
572 1 Y 1 E ARG 111  ? CZ  ? E ARG 111 CZ  
573 1 Y 1 E ARG 111  ? NH1 ? E ARG 111 NH1 
574 1 Y 1 E ARG 111  ? NH2 ? E ARG 111 NH2 
575 1 Y 1 E ILE 112  ? CG1 ? E ILE 112 CG1 
576 1 Y 1 E ILE 112  ? CG2 ? E ILE 112 CG2 
577 1 Y 1 E ILE 112  ? CD1 ? E ILE 112 CD1 
578 1 Y 1 E ARG 114  ? CG  ? E ARG 114 CG  
579 1 Y 1 E ARG 114  ? CD  ? E ARG 114 CD  
580 1 Y 1 E ARG 114  ? NE  ? E ARG 114 NE  
581 1 Y 1 E ARG 114  ? CZ  ? E ARG 114 CZ  
582 1 Y 1 E ARG 114  ? NH1 ? E ARG 114 NH1 
583 1 Y 1 E ARG 114  ? NH2 ? E ARG 114 NH2 
584 1 Y 1 E GLU 117  ? CG  ? E GLU 117 CG  
585 1 Y 1 E GLU 117  ? CD  ? E GLU 117 CD  
586 1 Y 1 E GLU 117  ? OE1 ? E GLU 117 OE1 
587 1 Y 1 E GLU 117  ? OE2 ? E GLU 117 OE2 
588 1 Y 1 E GLU 127  ? CG  ? E GLU 127 CG  
589 1 Y 1 E GLU 127  ? CD  ? E GLU 127 CD  
590 1 Y 1 E GLU 127  ? OE1 ? E GLU 127 OE1 
591 1 Y 1 E GLU 127  ? OE2 ? E GLU 127 OE2 
592 1 Y 1 E ARG 129  ? CG  ? E ARG 129 CG  
593 1 Y 1 E ARG 129  ? CD  ? E ARG 129 CD  
594 1 Y 1 E ARG 129  ? NE  ? E ARG 129 NE  
595 1 Y 1 E ARG 129  ? CZ  ? E ARG 129 CZ  
596 1 Y 1 E ARG 129  ? NH1 ? E ARG 129 NH1 
597 1 Y 1 E ARG 129  ? NH2 ? E ARG 129 NH2 
598 1 Y 1 E LYS 141  ? CG  ? E LYS 141 CG  
599 1 Y 1 E LYS 141  ? CD  ? E LYS 141 CD  
600 1 Y 1 E LYS 141  ? CE  ? E LYS 141 CE  
601 1 Y 1 E LYS 141  ? NZ  ? E LYS 141 NZ  
602 1 Y 1 E ARG 147  ? CG  ? E ARG 147 CG  
603 1 Y 1 E ARG 147  ? CD  ? E ARG 147 CD  
604 1 Y 1 E ARG 147  ? NE  ? E ARG 147 NE  
605 1 Y 1 E ARG 147  ? CZ  ? E ARG 147 CZ  
606 1 Y 1 E ARG 147  ? NH1 ? E ARG 147 NH1 
607 1 Y 1 E ARG 147  ? NH2 ? E ARG 147 NH2 
608 1 Y 1 E ASP 148  ? CG  ? E ASP 148 CG  
609 1 Y 1 E ASP 148  ? OD1 ? E ASP 148 OD1 
610 1 Y 1 E ASP 148  ? OD2 ? E ASP 148 OD2 
611 1 Y 1 E LYS 150  ? CG  ? E LYS 150 CG  
612 1 Y 1 E LYS 150  ? CD  ? E LYS 150 CD  
613 1 Y 1 E LYS 150  ? CE  ? E LYS 150 CE  
614 1 Y 1 E LYS 150  ? NZ  ? E LYS 150 NZ  
615 1 Y 1 E GLU 151  ? CG  ? E GLU 151 CG  
616 1 Y 1 E GLU 151  ? CD  ? E GLU 151 CD  
617 1 Y 1 E GLU 151  ? OE1 ? E GLU 151 OE1 
618 1 Y 1 E GLU 151  ? OE2 ? E GLU 151 OE2 
619 1 Y 1 E LYS 153  ? CG  ? E LYS 153 CG  
620 1 Y 1 E LYS 153  ? CD  ? E LYS 153 CD  
621 1 Y 1 E LYS 153  ? CE  ? E LYS 153 CE  
622 1 Y 1 E LYS 153  ? NZ  ? E LYS 153 NZ  
623 1 Y 1 E ARG 158  ? CG  ? E ARG 158 CG  
624 1 Y 1 E ARG 158  ? CD  ? E ARG 158 CD  
625 1 Y 1 E ARG 158  ? NE  ? E ARG 158 NE  
626 1 Y 1 E ARG 158  ? CZ  ? E ARG 158 CZ  
627 1 Y 1 E ARG 158  ? NH1 ? E ARG 158 NH1 
628 1 Y 1 E ARG 158  ? NH2 ? E ARG 158 NH2 
629 1 Y 1 E LEU 159  ? CG  ? E LEU 159 CG  
630 1 Y 1 E LEU 159  ? CD1 ? E LEU 159 CD1 
631 1 Y 1 E LEU 159  ? CD2 ? E LEU 159 CD2 
632 1 Y 1 E GLU 160  ? CG  ? E GLU 160 CG  
633 1 Y 1 E GLU 160  ? CD  ? E GLU 160 CD  
634 1 Y 1 E GLU 160  ? OE1 ? E GLU 160 OE1 
635 1 Y 1 E GLU 160  ? OE2 ? E GLU 160 OE2 
636 1 Y 1 E GLU 161  ? CG  ? E GLU 161 CG  
637 1 Y 1 E GLU 161  ? CD  ? E GLU 161 CD  
638 1 Y 1 E GLU 161  ? OE1 ? E GLU 161 OE1 
639 1 Y 1 E GLU 161  ? OE2 ? E GLU 161 OE2 
640 1 Y 1 E LYS 168  ? CG  ? E LYS 168 CG  
641 1 Y 1 E LYS 168  ? CD  ? E LYS 168 CD  
642 1 Y 1 E LYS 168  ? CE  ? E LYS 168 CE  
643 1 Y 1 E LYS 168  ? NZ  ? E LYS 168 NZ  
644 1 Y 1 E ARG 188  ? CG  ? E ARG 188 CG  
645 1 Y 1 E ARG 188  ? CD  ? E ARG 188 CD  
646 1 Y 1 E ARG 188  ? NE  ? E ARG 188 NE  
647 1 Y 1 E ARG 188  ? CZ  ? E ARG 188 CZ  
648 1 Y 1 E ARG 188  ? NH1 ? E ARG 188 NH1 
649 1 Y 1 E ARG 188  ? NH2 ? E ARG 188 NH2 
650 1 Y 1 E LYS 191  ? CG  ? E LYS 191 CG  
651 1 Y 1 E LYS 191  ? CD  ? E LYS 191 CD  
652 1 Y 1 E LYS 191  ? CE  ? E LYS 191 CE  
653 1 Y 1 E LYS 191  ? NZ  ? E LYS 191 NZ  
654 1 Y 1 E ARG 198  ? CG  ? E ARG 198 CG  
655 1 Y 1 E ARG 198  ? CD  ? E ARG 198 CD  
656 1 Y 1 E ARG 198  ? NE  ? E ARG 198 NE  
657 1 Y 1 E ARG 198  ? CZ  ? E ARG 198 CZ  
658 1 Y 1 E ARG 198  ? NH1 ? E ARG 198 NH1 
659 1 Y 1 E ARG 198  ? NH2 ? E ARG 198 NH2 
660 1 Y 1 E LYS 200  ? CG  ? E LYS 200 CG  
661 1 Y 1 E LYS 200  ? CD  ? E LYS 200 CD  
662 1 Y 1 E LYS 200  ? CE  ? E LYS 200 CE  
663 1 Y 1 E LYS 200  ? NZ  ? E LYS 200 NZ  
664 1 Y 1 E LYS 204  ? CG  ? E LYS 204 CG  
665 1 Y 1 E LYS 204  ? CD  ? E LYS 204 CD  
666 1 Y 1 E LYS 204  ? CE  ? E LYS 204 CE  
667 1 Y 1 E LYS 204  ? NZ  ? E LYS 204 NZ  
668 1 Y 1 E GLN 209  ? CG  ? E GLN 209 CG  
669 1 Y 1 E GLN 209  ? CD  ? E GLN 209 CD  
670 1 Y 1 E GLN 209  ? OE1 ? E GLN 209 OE1 
671 1 Y 1 E GLN 209  ? NE2 ? E GLN 209 NE2 
672 1 Y 1 E GLU 210  ? CG  ? E GLU 210 CG  
673 1 Y 1 E GLU 210  ? CD  ? E GLU 210 CD  
674 1 Y 1 E GLU 210  ? OE1 ? E GLU 210 OE1 
675 1 Y 1 E GLU 210  ? OE2 ? E GLU 210 OE2 
676 1 Y 1 E GLU 213  ? CG  ? E GLU 213 CG  
677 1 Y 1 E GLU 213  ? CD  ? E GLU 213 CD  
678 1 Y 1 E GLU 213  ? OE1 ? E GLU 213 OE1 
679 1 Y 1 E GLU 213  ? OE2 ? E GLU 213 OE2 
680 1 Y 1 E PHE 226  ? CG  ? E PHE 226 CG  
681 1 Y 1 E PHE 226  ? CD1 ? E PHE 226 CD1 
682 1 Y 1 E PHE 226  ? CD2 ? E PHE 226 CD2 
683 1 Y 1 E PHE 226  ? CE1 ? E PHE 226 CE1 
684 1 Y 1 E PHE 226  ? CE2 ? E PHE 226 CE2 
685 1 Y 1 E PHE 226  ? CZ  ? E PHE 226 CZ  
686 1 Y 1 E GLU 235  ? CG  ? E GLU 235 CG  
687 1 Y 1 E GLU 235  ? CD  ? E GLU 235 CD  
688 1 Y 1 E GLU 235  ? OE1 ? E GLU 235 OE1 
689 1 Y 1 E GLU 235  ? OE2 ? E GLU 235 OE2 
690 1 Y 1 E ASP 243  ? CG  ? E ASP 243 CG  
691 1 Y 1 E ASP 243  ? OD1 ? E ASP 243 OD1 
692 1 Y 1 E ASP 243  ? OD2 ? E ASP 243 OD2 
693 1 Y 1 E LYS 244  ? CG  ? E LYS 244 CG  
694 1 Y 1 E LYS 244  ? CD  ? E LYS 244 CD  
695 1 Y 1 E LYS 244  ? CE  ? E LYS 244 CE  
696 1 Y 1 E LYS 244  ? NZ  ? E LYS 244 NZ  
697 1 Y 1 E LYS 254  ? CG  ? E LYS 254 CG  
698 1 Y 1 E LYS 254  ? CD  ? E LYS 254 CD  
699 1 Y 1 E LYS 254  ? CE  ? E LYS 254 CE  
700 1 Y 1 E LYS 254  ? NZ  ? E LYS 254 NZ  
701 1 Y 1 E ARG 270  ? CG  ? E ARG 270 CG  
702 1 Y 1 E ARG 270  ? CD  ? E ARG 270 CD  
703 1 Y 1 E ARG 270  ? NE  ? E ARG 270 NE  
704 1 Y 1 E ARG 270  ? CZ  ? E ARG 270 CZ  
705 1 Y 1 E ARG 270  ? NH1 ? E ARG 270 NH1 
706 1 Y 1 E ARG 270  ? NH2 ? E ARG 270 NH2 
707 1 Y 1 E GLU 286  ? CG  ? E GLU 286 CG  
708 1 Y 1 E GLU 286  ? CD  ? E GLU 286 CD  
709 1 Y 1 E GLU 286  ? OE1 ? E GLU 286 OE1 
710 1 Y 1 E GLU 286  ? OE2 ? E GLU 286 OE2 
711 1 Y 1 E LYS 287  ? CG  ? E LYS 287 CG  
712 1 Y 1 E LYS 287  ? CD  ? E LYS 287 CD  
713 1 Y 1 E LYS 287  ? CE  ? E LYS 287 CE  
714 1 Y 1 E LYS 287  ? NZ  ? E LYS 287 NZ  
715 1 Y 1 E GLU 288  ? CG  ? E GLU 288 CG  
716 1 Y 1 E GLU 288  ? CD  ? E GLU 288 CD  
717 1 Y 1 E GLU 288  ? OE1 ? E GLU 288 OE1 
718 1 Y 1 E GLU 288  ? OE2 ? E GLU 288 OE2 
719 1 Y 1 E GLU 289  ? CG  ? E GLU 289 CG  
720 1 Y 1 E GLU 289  ? CD  ? E GLU 289 CD  
721 1 Y 1 E GLU 289  ? OE1 ? E GLU 289 OE1 
722 1 Y 1 E GLU 289  ? OE2 ? E GLU 289 OE2 
723 1 Y 1 E LYS 298  ? CG  ? E LYS 298 CG  
724 1 Y 1 E LYS 298  ? CD  ? E LYS 298 CD  
725 1 Y 1 E LYS 298  ? CE  ? E LYS 298 CE  
726 1 Y 1 E LYS 298  ? NZ  ? E LYS 298 NZ  
727 1 Y 1 E ARG 301  ? CG  ? E ARG 301 CG  
728 1 Y 1 E ARG 301  ? CD  ? E ARG 301 CD  
729 1 Y 1 E ARG 301  ? NE  ? E ARG 301 NE  
730 1 Y 1 E ARG 301  ? CZ  ? E ARG 301 CZ  
731 1 Y 1 E ARG 301  ? NH1 ? E ARG 301 NH1 
732 1 Y 1 E ARG 301  ? NH2 ? E ARG 301 NH2 
733 1 Y 1 E LYS 335  ? CG  ? E LYS 335 CG  
734 1 Y 1 E LYS 335  ? CD  ? E LYS 335 CD  
735 1 Y 1 E LYS 335  ? CE  ? E LYS 335 CE  
736 1 Y 1 E LYS 335  ? NZ  ? E LYS 335 NZ  
737 1 Y 1 E ASP 339  ? CG  ? E ASP 339 CG  
738 1 Y 1 E ASP 339  ? OD1 ? E ASP 339 OD1 
739 1 Y 1 E ASP 339  ? OD2 ? E ASP 339 OD2 
740 1 Y 1 E ASN 341  ? CG  ? E ASN 341 CG  
741 1 Y 1 E ASN 341  ? OD1 ? E ASN 341 OD1 
742 1 Y 1 E ASN 341  ? ND2 ? E ASN 341 ND2 
743 1 Y 1 E GLU 342  ? CG  ? E GLU 342 CG  
744 1 Y 1 E GLU 342  ? CD  ? E GLU 342 CD  
745 1 Y 1 E GLU 342  ? OE1 ? E GLU 342 OE1 
746 1 Y 1 E GLU 342  ? OE2 ? E GLU 342 OE2 
747 1 Y 1 E GLN 343  ? CG  ? E GLN 343 CG  
748 1 Y 1 E GLN 343  ? CD  ? E GLN 343 CD  
749 1 Y 1 E GLN 343  ? OE1 ? E GLN 343 OE1 
750 1 Y 1 E GLN 343  ? NE2 ? E GLN 343 NE2 
751 1 Y 1 E ARG 369  ? CG  ? E ARG 369 CG  
752 1 Y 1 E ARG 369  ? CD  ? E ARG 369 CD  
753 1 Y 1 E ARG 369  ? NE  ? E ARG 369 NE  
754 1 Y 1 E ARG 369  ? CZ  ? E ARG 369 CZ  
755 1 Y 1 E ARG 369  ? NH1 ? E ARG 369 NH1 
756 1 Y 1 E ARG 369  ? NH2 ? E ARG 369 NH2 
757 1 Y 1 E ARG 391  ? CG  ? E ARG 391 CG  
758 1 Y 1 E ARG 391  ? CD  ? E ARG 391 CD  
759 1 Y 1 E ARG 391  ? NE  ? E ARG 391 NE  
760 1 Y 1 E ARG 391  ? CZ  ? E ARG 391 CZ  
761 1 Y 1 E ARG 391  ? NH1 ? E ARG 391 NH1 
762 1 Y 1 E ARG 391  ? NH2 ? E ARG 391 NH2 
763 1 Y 1 E LYS 769  ? CG  ? E LYS 465 CG  
764 1 Y 1 E LYS 769  ? CD  ? E LYS 465 CD  
765 1 Y 1 E LYS 769  ? CE  ? E LYS 465 CE  
766 1 Y 1 E LYS 769  ? NZ  ? E LYS 465 NZ  
767 1 Y 1 E LEU 770  ? CG  ? E LEU 466 CG  
768 1 Y 1 E LEU 770  ? CD1 ? E LEU 466 CD1 
769 1 Y 1 E LEU 770  ? CD2 ? E LEU 466 CD2 
770 1 Y 1 E PHE 782  ? CG  ? E PHE 478 CG  
771 1 Y 1 E PHE 782  ? CD1 ? E PHE 478 CD1 
772 1 Y 1 E PHE 782  ? CD2 ? E PHE 478 CD2 
773 1 Y 1 E PHE 782  ? CE1 ? E PHE 478 CE1 
774 1 Y 1 E PHE 782  ? CE2 ? E PHE 478 CE2 
775 1 Y 1 E PHE 782  ? CZ  ? E PHE 478 CZ  
776 1 Y 1 E GLU 784  ? CG  ? E GLU 480 CG  
777 1 Y 1 E GLU 784  ? CD  ? E GLU 480 CD  
778 1 Y 1 E GLU 784  ? OE1 ? E GLU 480 OE1 
779 1 Y 1 E GLU 784  ? OE2 ? E GLU 480 OE2 
780 1 Y 1 E GLN 809  ? CG  ? E GLN 505 CG  
781 1 Y 1 E GLN 809  ? CD  ? E GLN 505 CD  
782 1 Y 1 E GLN 809  ? OE1 ? E GLN 505 OE1 
783 1 Y 1 E GLN 809  ? NE2 ? E GLN 505 NE2 
784 1 Y 1 E LYS 820  ? CG  ? E LYS 516 CG  
785 1 Y 1 E LYS 820  ? CD  ? E LYS 516 CD  
786 1 Y 1 E LYS 820  ? CE  ? E LYS 516 CE  
787 1 Y 1 E LYS 820  ? NZ  ? E LYS 516 NZ  
788 1 Y 1 E LYS 823  ? CG  ? E LYS 519 CG  
789 1 Y 1 E LYS 823  ? CD  ? E LYS 519 CD  
790 1 Y 1 E LYS 823  ? CE  ? E LYS 519 CE  
791 1 Y 1 E LYS 823  ? NZ  ? E LYS 519 NZ  
792 1 Y 1 E GLU 839  ? CG  ? E GLU 535 CG  
793 1 Y 1 E GLU 839  ? CD  ? E GLU 535 CD  
794 1 Y 1 E GLU 839  ? OE1 ? E GLU 535 OE1 
795 1 Y 1 E GLU 839  ? OE2 ? E GLU 535 OE2 
796 1 Y 1 E GLU 840  ? CG  ? E GLU 536 CG  
797 1 Y 1 E GLU 840  ? CD  ? E GLU 536 CD  
798 1 Y 1 E GLU 840  ? OE1 ? E GLU 536 OE1 
799 1 Y 1 E GLU 840  ? OE2 ? E GLU 536 OE2 
800 1 Y 1 E LYS 857  ? CG  ? E LYS 553 CG  
801 1 Y 1 E LYS 857  ? CD  ? E LYS 553 CD  
802 1 Y 1 E LYS 857  ? CE  ? E LYS 553 CE  
803 1 Y 1 E LYS 857  ? NZ  ? E LYS 553 NZ  
804 1 Y 1 E GLN 859  ? CG  ? E GLN 555 CG  
805 1 Y 1 E GLN 859  ? CD  ? E GLN 555 CD  
806 1 Y 1 E GLN 859  ? OE1 ? E GLN 555 OE1 
807 1 Y 1 E GLN 859  ? NE2 ? E GLN 555 NE2 
808 1 Y 1 E LYS 867  ? CG  ? E LYS 563 CG  
809 1 Y 1 E LYS 867  ? CD  ? E LYS 563 CD  
810 1 Y 1 E LYS 867  ? CE  ? E LYS 563 CE  
811 1 Y 1 E LYS 867  ? NZ  ? E LYS 563 NZ  
812 1 Y 1 E GLU 896  ? CG  ? E GLU 592 CG  
813 1 Y 1 E GLU 896  ? CD  ? E GLU 592 CD  
814 1 Y 1 E GLU 896  ? OE1 ? E GLU 592 OE1 
815 1 Y 1 E GLU 896  ? OE2 ? E GLU 592 OE2 
816 1 Y 1 E LYS 897  ? CG  ? E LYS 593 CG  
817 1 Y 1 E LYS 897  ? CD  ? E LYS 593 CD  
818 1 Y 1 E LYS 897  ? CE  ? E LYS 593 CE  
819 1 Y 1 E LYS 897  ? NZ  ? E LYS 593 NZ  
820 1 Y 1 E ARG 900  ? CG  ? E ARG 596 CG  
821 1 Y 1 E ARG 900  ? CD  ? E ARG 596 CD  
822 1 Y 1 E ARG 900  ? NE  ? E ARG 596 NE  
823 1 Y 1 E ARG 900  ? CZ  ? E ARG 596 CZ  
824 1 Y 1 E ARG 900  ? NH1 ? E ARG 596 NH1 
825 1 Y 1 E ARG 900  ? NH2 ? E ARG 596 NH2 
826 1 Y 1 E GLU 902  ? CG  ? E GLU 598 CG  
827 1 Y 1 E GLU 902  ? CD  ? E GLU 598 CD  
828 1 Y 1 E GLU 902  ? OE1 ? E GLU 598 OE1 
829 1 Y 1 E GLU 902  ? OE2 ? E GLU 598 OE2 
830 1 Y 1 E LYS 936  ? CG  ? E LYS 632 CG  
831 1 Y 1 E LYS 936  ? CD  ? E LYS 632 CD  
832 1 Y 1 E LYS 936  ? CE  ? E LYS 632 CE  
833 1 Y 1 E LYS 936  ? NZ  ? E LYS 632 NZ  
834 1 Y 1 E MET 938  ? CG  ? E MET 634 CG  
835 1 Y 1 E MET 938  ? SD  ? E MET 634 SD  
836 1 Y 1 E MET 938  ? CE  ? E MET 634 CE  
837 1 Y 1 E GLU 939  ? CG  ? E GLU 635 CG  
838 1 Y 1 E GLU 939  ? CD  ? E GLU 635 CD  
839 1 Y 1 E GLU 939  ? OE1 ? E GLU 635 OE1 
840 1 Y 1 E GLU 939  ? OE2 ? E GLU 635 OE2 
841 1 Y 1 E LYS 979  ? CG  ? E LYS 675 CG  
842 1 Y 1 E LYS 979  ? CD  ? E LYS 675 CD  
843 1 Y 1 E LYS 979  ? CE  ? E LYS 675 CE  
844 1 Y 1 E LYS 979  ? NZ  ? E LYS 675 NZ  
845 1 Y 1 E GLU 987  ? CG  ? E GLU 683 CG  
846 1 Y 1 E GLU 987  ? CD  ? E GLU 683 CD  
847 1 Y 1 E GLU 987  ? OE1 ? E GLU 683 OE1 
848 1 Y 1 E GLU 987  ? OE2 ? E GLU 683 OE2 
849 1 Y 1 E GLU 988  ? CG  ? E GLU 684 CG  
850 1 Y 1 E GLU 988  ? CD  ? E GLU 684 CD  
851 1 Y 1 E GLU 988  ? OE1 ? E GLU 684 OE1 
852 1 Y 1 E GLU 988  ? OE2 ? E GLU 684 OE2 
853 1 Y 1 E GLN 990  ? CG  ? E GLN 686 CG  
854 1 Y 1 E GLN 990  ? CD  ? E GLN 686 CD  
855 1 Y 1 E GLN 990  ? OE1 ? E GLN 686 OE1 
856 1 Y 1 E GLN 990  ? NE2 ? E GLN 686 NE2 
857 1 Y 1 E ARG 1057 ? CG  ? E ARG 753 CG  
858 1 Y 1 E ARG 1057 ? CD  ? E ARG 753 CD  
859 1 Y 1 E ARG 1057 ? NE  ? E ARG 753 NE  
860 1 Y 1 E ARG 1057 ? CZ  ? E ARG 753 CZ  
861 1 Y 1 E ARG 1057 ? NH1 ? E ARG 753 NH1 
862 1 Y 1 E ARG 1057 ? NH2 ? E ARG 753 NH2 
863 1 Y 1 E LYS 1060 ? CG  ? E LYS 756 CG  
864 1 Y 1 E LYS 1060 ? CD  ? E LYS 756 CD  
865 1 Y 1 E LYS 1060 ? CE  ? E LYS 756 CE  
866 1 Y 1 E LYS 1060 ? NZ  ? E LYS 756 NZ  
867 1 Y 1 E LYS 1063 ? CG  ? E LYS 759 CG  
868 1 Y 1 E LYS 1063 ? CD  ? E LYS 759 CD  
869 1 Y 1 E LYS 1063 ? CE  ? E LYS 759 CE  
870 1 Y 1 E LYS 1063 ? NZ  ? E LYS 759 NZ  
871 1 Y 1 E LYS 1067 ? CG  ? E LYS 763 CG  
872 1 Y 1 E LYS 1067 ? CD  ? E LYS 763 CD  
873 1 Y 1 E LYS 1067 ? CE  ? E LYS 763 CE  
874 1 Y 1 E LYS 1067 ? NZ  ? E LYS 763 NZ  
875 1 Y 1 E ARG 1080 ? CG  ? E ARG 776 CG  
876 1 Y 1 E ARG 1080 ? CD  ? E ARG 776 CD  
877 1 Y 1 E ARG 1080 ? NE  ? E ARG 776 NE  
878 1 Y 1 E ARG 1080 ? CZ  ? E ARG 776 CZ  
879 1 Y 1 E ARG 1080 ? NH1 ? E ARG 776 NH1 
880 1 Y 1 E ARG 1080 ? NH2 ? E ARG 776 NH2 
881 1 Y 1 E LYS 1081 ? CG  ? E LYS 777 CG  
882 1 Y 1 E LYS 1081 ? CD  ? E LYS 777 CD  
883 1 Y 1 E LYS 1081 ? CE  ? E LYS 777 CE  
884 1 Y 1 E LYS 1081 ? NZ  ? E LYS 777 NZ  
885 1 Y 1 E LYS 1104 ? CG  ? E LYS 800 CG  
886 1 Y 1 E LYS 1104 ? CD  ? E LYS 800 CD  
887 1 Y 1 E LYS 1104 ? CE  ? E LYS 800 CE  
888 1 Y 1 E LYS 1104 ? NZ  ? E LYS 800 NZ  
889 1 Y 1 E GLU 1123 ? CG  ? E GLU 819 CG  
890 1 Y 1 E GLU 1123 ? CD  ? E GLU 819 CD  
891 1 Y 1 E GLU 1123 ? OE1 ? E GLU 819 OE1 
892 1 Y 1 E GLU 1123 ? OE2 ? E GLU 819 OE2 
893 1 Y 1 F ARG 890  ? CG  ? F ARG 25  CG  
894 1 Y 1 F ARG 890  ? CD  ? F ARG 25  CD  
895 1 Y 1 F ARG 890  ? NE  ? F ARG 25  NE  
896 1 Y 1 F ARG 890  ? CZ  ? F ARG 25  CZ  
897 1 Y 1 F ARG 890  ? NH1 ? F ARG 25  NH1 
898 1 Y 1 F ARG 890  ? NH2 ? F ARG 25  NH2 
899 1 Y 1 F ARG 894  ? CG  ? F ARG 29  CG  
900 1 Y 1 F ARG 894  ? CD  ? F ARG 29  CD  
901 1 Y 1 F ARG 894  ? NE  ? F ARG 29  NE  
902 1 Y 1 F ARG 894  ? CZ  ? F ARG 29  CZ  
903 1 Y 1 F ARG 894  ? NH1 ? F ARG 29  NH1 
904 1 Y 1 F ARG 894  ? NH2 ? F ARG 29  NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.21_5207 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .         4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DJT 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     109.711 
_cell.length_a_esd                 ? 
_cell.length_b                     145.600 
_cell.length_b_esd                 ? 
_cell.length_c                     192.099 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9DJT 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DJT 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.75 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.23 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M Sodium Sulfate, 0.1 M Bis-Tris Propane pH 7.5, 20% w/v PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-04-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 17-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          97.55 
_reflns.entry_id                                       9DJT 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.95 
_reflns.d_resolution_low                               29.96 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     64947 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.227 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.95 
_reflns_shell.d_res_low                                     3.02 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4489 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               14 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.303 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DJT 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.95 
_refine.ls_d_res_low                             29.96 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     64731 
_refine.ls_number_reflns_R_free                  3177 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.00 
_refine.ls_percent_reflns_R_free                 4.91 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2079 
_refine.ls_R_factor_R_free                       0.2600 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2051 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.59 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.48 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.95 
_refine_hist.d_res_low                        29.96 
_refine_hist.number_atoms_solvent             42 
_refine_hist.number_atoms_total               17688 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        17574 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         72 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  ? 18029 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.074  ? 24570 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 20.441 ? 6330  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.052  ? 2897  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 3163  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.95 2.99  . . 106 2626 98.00  . . . . 0.3891 . . . . . . . . . . . 0.4079 
'X-RAY DIFFRACTION' 2.99 3.04  . . 146 2622 98.00  . . . . 0.3469 . . . . . . . . . . . 0.3456 
'X-RAY DIFFRACTION' 3.04 3.09  . . 133 2613 99.00  . . . . 0.3235 . . . . . . . . . . . 0.3463 
'X-RAY DIFFRACTION' 3.09 3.14  . . 121 2662 99.00  . . . . 0.3206 . . . . . . . . . . . 0.3784 
'X-RAY DIFFRACTION' 3.14 3.20  . . 143 2613 99.00  . . . . 0.3146 . . . . . . . . . . . 0.3565 
'X-RAY DIFFRACTION' 3.20 3.26  . . 126 2663 99.00  . . . . 0.3028 . . . . . . . . . . . 0.3834 
'X-RAY DIFFRACTION' 3.26 3.33  . . 121 2655 99.00  . . . . 0.2985 . . . . . . . . . . . 0.3442 
'X-RAY DIFFRACTION' 3.33 3.40  . . 139 2649 99.00  . . . . 0.2896 . . . . . . . . . . . 0.3761 
'X-RAY DIFFRACTION' 3.40 3.48  . . 154 2625 99.00  . . . . 0.2670 . . . . . . . . . . . 0.3551 
'X-RAY DIFFRACTION' 3.48 3.57  . . 139 2640 99.00  . . . . 0.2430 . . . . . . . . . . . 0.3159 
'X-RAY DIFFRACTION' 3.57 3.66  . . 160 2655 99.00  . . . . 0.2220 . . . . . . . . . . . 0.2956 
'X-RAY DIFFRACTION' 3.66 3.77  . . 121 2652 99.00  . . . . 0.2167 . . . . . . . . . . . 0.3023 
'X-RAY DIFFRACTION' 3.77 3.89  . . 119 2708 99.00  . . . . 0.2175 . . . . . . . . . . . 0.2903 
'X-RAY DIFFRACTION' 3.89 4.03  . . 139 2646 99.00  . . . . 0.1942 . . . . . . . . . . . 0.2502 
'X-RAY DIFFRACTION' 4.03 4.19  . . 143 2664 99.00  . . . . 0.1894 . . . . . . . . . . . 0.2645 
'X-RAY DIFFRACTION' 4.19 4.38  . . 162 2678 99.00  . . . . 0.1693 . . . . . . . . . . . 0.2521 
'X-RAY DIFFRACTION' 4.38 4.61  . . 146 2677 99.00  . . . . 0.1668 . . . . . . . . . . . 0.2037 
'X-RAY DIFFRACTION' 4.61 4.90  . . 138 2700 100.00 . . . . 0.1570 . . . . . . . . . . . 0.2183 
'X-RAY DIFFRACTION' 4.90 5.28  . . 138 2707 99.00  . . . . 0.1723 . . . . . . . . . . . 0.2372 
'X-RAY DIFFRACTION' 5.28 5.80  . . 150 2720 100.00 . . . . 0.1868 . . . . . . . . . . . 0.2699 
'X-RAY DIFFRACTION' 5.80 6.64  . . 135 2740 100.00 . . . . 0.1997 . . . . . . . . . . . 0.2503 
'X-RAY DIFFRACTION' 6.64 8.33  . . 153 2770 100.00 . . . . 0.1999 . . . . . . . . . . . 0.2548 
'X-RAY DIFFRACTION' 8.33 29.96 . . 145 2869 99.00  . . . . 0.1769 . . . . . . . . . . . 0.1934 
# 
_struct.entry_id                     9DJT 
_struct.title                        'Ternary complex structure of Cereblon-DDB1 bound to WIZ(ZF7) and the molecular glue WIZ-5' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9DJT 
_struct_keywords.text            'Cereblon, Ligase, Molecular Glue' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 6 ? 
J N N 4 ? 
K N N 4 ? 
L N N 5 ? 
M N N 6 ? 
N N N 4 ? 
O N N 7 ? 
P N N 7 ? 
Q N N 7 ? 
R N N 7 ? 
S N N 7 ? 
T N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP CRBN_HUMAN Q96SW2 ? 1 
;RTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQD
FGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQK
RKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLR
CELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVA
QCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPDKVILCL
;
70  
2 UNP DDB1_HUMAN Q16531 ? 2 
;MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFIL
TAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLE
ELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH
NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNG
VVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIG
;
1   
3 UNP DDB1_HUMAN Q16531 ? 2 
;EIQKLHIRTVPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAPHETSFGEE
VEVHNLLIIDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGKLQTVAEKE
VKGAVYSMVEFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYKPMEGNFEEI
ARDFNPNWMSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNLGETSTPTQ
GSVLFGTVNGMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESFLDISRPKM
QEVVANLQYDDGSGMKREATADDLIKVVEELTRIH
;
706 
4 UNP WIZ_HUMAN  O95785 ? 3 QSLTTCEVCGACFETRKGLSSHARSHLRQ 867 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9DJT A 1   ? 373 ? Q96SW2 70  ? 442  ? 70  442  
2 2 9DJT B 1   ? 395 ? Q16531 1   ? 395  ? 1   699  
3 3 9DJT B 402 ? 836 ? Q16531 706 ? 1140 ? 706 1140 
4 4 9DJT C 2   ? 30  ? O95785 867 ? 895  ? 867 895  
5 1 9DJT D 1   ? 373 ? Q96SW2 70  ? 442  ? 70  442  
6 2 9DJT E 1   ? 395 ? Q16531 1   ? 395  ? 1   699  
7 3 9DJT E 402 ? 836 ? Q16531 706 ? 1140 ? 706 1140 
8 4 9DJT F 2   ? 30  ? O95785 867 ? 895  ? 867 895  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
2 9DJT GLY B 396 ? UNP Q16531 ? ? linker           700 1  
2 9DJT ASN B 397 ? UNP Q16531 ? ? linker           701 2  
2 9DJT GLY B 398 ? UNP Q16531 ? ? linker           702 3  
2 9DJT ASN B 399 ? UNP Q16531 ? ? linker           703 4  
2 9DJT SER B 400 ? UNP Q16531 ? ? linker           704 5  
2 9DJT GLY B 401 ? UNP Q16531 ? ? linker           705 6  
4 9DJT SER C 1   ? UNP O95785 ? ? 'expression tag' 866 7  
6 9DJT GLY E 396 ? UNP Q16531 ? ? linker           700 8  
6 9DJT ASN E 397 ? UNP Q16531 ? ? linker           701 9  
6 9DJT GLY E 398 ? UNP Q16531 ? ? linker           702 10 
6 9DJT ASN E 399 ? UNP Q16531 ? ? linker           703 11 
6 9DJT SER E 400 ? UNP Q16531 ? ? linker           704 12 
6 9DJT GLY E 401 ? UNP Q16531 ? ? linker           705 13 
8 9DJT SER F 1   ? UNP O95785 ? ? 'expression tag' 866 14 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA trimeric 3 
2 author_and_software_defined_assembly PISA trimeric 3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5830  ? 
1 MORE         -60   ? 
1 'SSA (A^2)'  48430 ? 
2 'ABSA (A^2)' 5940  ? 
2 MORE         -61   ? 
2 'SSA (A^2)'  48150 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,G,H,I,J,O,P,Q 
2 1 D,E,F,K,L,M,N,R,S,T 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 34  ? LYS A 47  ? HIS A 103  LYS A 116  1 ? 14 
HELX_P HELX_P2  AA2 LEU A 130 ? GLN A 137 ? LEU A 199  GLN A 206  5 ? 8  
HELX_P HELX_P3  AA3 TYR A 152 ? PHE A 163 ? TYR A 221  PHE A 232  1 ? 12 
HELX_P HELX_P4  AA4 HIS A 164 ? THR A 169 ? HIS A 233  THR A 238  5 ? 6  
HELX_P HELX_P5  AA5 PRO A 172 ? LEU A 178 ? PRO A 241  LEU A 247  1 ? 7  
HELX_P HELX_P6  AA6 ASP A 180 ? TRP A 195 ? ASP A 249  TRP A 264  1 ? 16 
HELX_P HELX_P7  AA7 ASN A 207 ? LEU A 219 ? ASN A 276  LEU A 288  1 ? 13 
HELX_P HELX_P8  AA8 ASP A 222 ? LYS A 231 ? ASP A 291  LYS A 300  1 ? 10 
HELX_P HELX_P9  AA9 SER A 234 ? CYS A 249 ? SER A 303  CYS A 318  1 ? 16 
HELX_P HELX_P10 AB1 ASN A 266 ? ILE A 268 ? ASN A 335  ILE A 337  5 ? 3  
HELX_P HELX_P11 AB2 PRO B 250 ? SER B 256 ? PRO B 250  SER B 256  5 ? 7  
HELX_P HELX_P12 AB3 ALA B 381 ? GLU B 384 ? ALA B 381  GLU B 384  5 ? 4  
HELX_P HELX_P13 AB4 GLU B 424 ? SER B 426 ? GLU B 728  SER B 730  5 ? 3  
HELX_P HELX_P14 AB5 THR B 681 ? GLN B 686 ? THR B 985  GLN B 990  1 ? 6  
HELX_P HELX_P15 AB6 SER B 740 ? ILE B 758 ? SER B 1044 ILE B 1062 1 ? 19 
HELX_P HELX_P16 AB7 GLU B 765 ? SER B 771 ? GLU B 1069 SER B 1075 1 ? 7  
HELX_P HELX_P17 AB8 GLY B 787 ? SER B 792 ? GLY B 1091 SER B 1096 1 ? 6  
HELX_P HELX_P18 AB9 PHE B 793 ? ILE B 796 ? PHE B 1097 ILE B 1100 5 ? 4  
HELX_P HELX_P19 AC1 SER B 797 ? ALA B 806 ? SER B 1101 ALA B 1110 1 ? 10 
HELX_P HELX_P20 AC2 THR B 821 ? ARG B 834 ? THR B 1125 ARG B 1138 1 ? 14 
HELX_P HELX_P21 AC3 LYS C 18  ? LEU C 28  ? LYS C 883  LEU C 893  1 ? 11 
HELX_P HELX_P22 AC4 HIS D 34  ? GLN D 46  ? HIS D 103  GLN D 115  1 ? 13 
HELX_P HELX_P23 AC5 SER D 123 ? ALA D 127 ? SER D 192  ALA D 196  5 ? 5  
HELX_P HELX_P24 AC6 LEU D 130 ? ILE D 138 ? LEU D 199  ILE D 207  5 ? 9  
HELX_P HELX_P25 AC7 TYR D 152 ? PHE D 163 ? TYR D 221  PHE D 232  1 ? 12 
HELX_P HELX_P26 AC8 HIS D 164 ? THR D 169 ? HIS D 233  THR D 238  5 ? 6  
HELX_P HELX_P27 AC9 PRO D 172 ? TYR D 179 ? PRO D 241  TYR D 248  1 ? 8  
HELX_P HELX_P28 AD1 ASP D 180 ? TRP D 195 ? ASP D 249  TRP D 264  1 ? 16 
HELX_P HELX_P29 AD2 ASN D 207 ? LEU D 219 ? ASN D 276  LEU D 288  1 ? 13 
HELX_P HELX_P30 AD3 ASP D 222 ? ILE D 232 ? ASP D 291  ILE D 301  1 ? 11 
HELX_P HELX_P31 AD4 SER D 234 ? CYS D 249 ? SER D 303  CYS D 318  1 ? 16 
HELX_P HELX_P32 AD5 ASN D 266 ? ILE D 268 ? ASN D 335  ILE D 337  5 ? 3  
HELX_P HELX_P33 AD6 PRO E 251 ? SER E 256 ? PRO E 251  SER E 256  5 ? 6  
HELX_P HELX_P34 AD7 ALA E 381 ? GLU E 384 ? ALA E 381  GLU E 384  5 ? 4  
HELX_P HELX_P35 AD8 GLU E 424 ? SER E 426 ? GLU E 728  SER E 730  5 ? 3  
HELX_P HELX_P36 AD9 THR E 681 ? GLN E 686 ? THR E 985  GLN E 990  1 ? 6  
HELX_P HELX_P37 AE1 SER E 740 ? ILE E 758 ? SER E 1044 ILE E 1062 1 ? 19 
HELX_P HELX_P38 AE2 SER E 760 ? ILE E 764 ? SER E 1064 ILE E 1068 5 ? 5  
HELX_P HELX_P39 AE3 GLU E 765 ? SER E 771 ? GLU E 1069 SER E 1075 1 ? 7  
HELX_P HELX_P40 AE4 GLY E 787 ? PHE E 793 ? GLY E 1091 PHE E 1097 1 ? 7  
HELX_P HELX_P41 AE5 LEU E 794 ? ILE E 796 ? LEU E 1098 ILE E 1100 5 ? 3  
HELX_P HELX_P42 AE6 SER E 797 ? ALA E 806 ? SER E 1101 ALA E 1110 1 ? 10 
HELX_P HELX_P43 AE7 ALA E 822 ? THR E 833 ? ALA E 1126 THR E 1137 1 ? 12 
HELX_P HELX_P44 AE8 ARG E 834 ? HIS E 836 ? ARG E 1138 HIS E 1140 5 ? 3  
HELX_P HELX_P45 AE9 THR F 16  ? ARG F 29  ? THR F 881  ARG F 894  1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? B CYS 18  SG  ? ? ? 1_555 B CYS 313 SG ? ? B CYS 18  B CYS 313 1_555 ? ? ? ? ? ? ? 2.135 ? ? 
disulf2  disulf ? ? E CYS 18  SG  ? ? ? 1_555 E CYS 313 SG ? ? E CYS 18  E CYS 313 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
metalc1  metalc ? ? A CYS 254 SG  ? ? ? 1_555 G ZN  .   ZN ? ? A CYS 323 A ZN  501 1_555 ? ? ? ? ? ? ? 2.273 ? ? 
metalc2  metalc ? ? A CYS 257 SG  ? ? ? 1_555 G ZN  .   ZN ? ? A CYS 326 A ZN  501 1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc3  metalc ? ? A CYS 322 SG  ? ? ? 1_555 G ZN  .   ZN ? ? A CYS 391 A ZN  501 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
metalc4  metalc ? ? A CYS 325 SG  ? ? ? 1_555 G ZN  .   ZN ? ? A CYS 394 A ZN  501 1_555 ? ? ? ? ? ? ? 2.317 ? ? 
metalc5  metalc ? ? C CYS 7   SG  ? ? ? 1_555 J ZN  .   ZN ? ? C CYS 872 C ZN  900 1_555 ? ? ? ? ? ? ? 2.276 ? ? 
metalc6  metalc ? ? C CYS 10  SG  ? ? ? 1_555 J ZN  .   ZN ? ? C CYS 875 C ZN  900 1_555 ? ? ? ? ? ? ? 2.288 ? ? 
metalc7  metalc ? ? C HIS 23  NE2 ? ? ? 1_555 J ZN  .   ZN ? ? C HIS 888 C ZN  900 1_555 ? ? ? ? ? ? ? 2.009 ? ? 
metalc8  metalc ? ? C HIS 27  NE2 ? ? ? 1_555 J ZN  .   ZN ? ? C HIS 892 C ZN  900 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc9  metalc ? ? D CYS 254 SG  ? ? ? 1_555 K ZN  .   ZN ? ? D CYS 323 D ZN  501 1_555 ? ? ? ? ? ? ? 2.320 ? ? 
metalc10 metalc ? ? D CYS 257 SG  ? ? ? 1_555 K ZN  .   ZN ? ? D CYS 326 D ZN  501 1_555 ? ? ? ? ? ? ? 2.262 ? ? 
metalc11 metalc ? ? D CYS 322 SG  ? ? ? 1_555 K ZN  .   ZN ? ? D CYS 391 D ZN  501 1_555 ? ? ? ? ? ? ? 2.292 ? ? 
metalc12 metalc ? ? D CYS 325 SG  ? ? ? 1_555 K ZN  .   ZN ? ? D CYS 394 D ZN  501 1_555 ? ? ? ? ? ? ? 2.260 ? ? 
metalc13 metalc ? ? F CYS 7   SG  ? ? ? 1_555 N ZN  .   ZN ? ? F CYS 872 F ZN  900 1_555 ? ? ? ? ? ? ? 2.269 ? ? 
metalc14 metalc ? ? F CYS 10  SG  ? ? ? 1_555 N ZN  .   ZN ? ? F CYS 875 F ZN  900 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
metalc15 metalc ? ? F HIS 23  NE2 ? ? ? 1_555 N ZN  .   ZN ? ? F HIS 888 F ZN  900 1_555 ? ? ? ? ? ? ? 1.904 ? ? 
metalc16 metalc ? ? F HIS 27  NE2 ? ? ? 1_555 N ZN  .   ZN ? ? F HIS 892 F ZN  900 1_555 ? ? ? ? ? ? ? 1.945 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A CYS 254 ? A CYS 323 ? 1_555 ZN ? G ZN . ? A ZN 501 ? 1_555 SG  ? A CYS 257 ? A CYS 326 ? 1_555 99.2  ? 
2  SG  ? A CYS 254 ? A CYS 323 ? 1_555 ZN ? G ZN . ? A ZN 501 ? 1_555 SG  ? A CYS 322 ? A CYS 391 ? 1_555 116.6 ? 
3  SG  ? A CYS 257 ? A CYS 326 ? 1_555 ZN ? G ZN . ? A ZN 501 ? 1_555 SG  ? A CYS 322 ? A CYS 391 ? 1_555 106.6 ? 
4  SG  ? A CYS 254 ? A CYS 323 ? 1_555 ZN ? G ZN . ? A ZN 501 ? 1_555 SG  ? A CYS 325 ? A CYS 394 ? 1_555 98.7  ? 
5  SG  ? A CYS 257 ? A CYS 326 ? 1_555 ZN ? G ZN . ? A ZN 501 ? 1_555 SG  ? A CYS 325 ? A CYS 394 ? 1_555 117.8 ? 
6  SG  ? A CYS 322 ? A CYS 391 ? 1_555 ZN ? G ZN . ? A ZN 501 ? 1_555 SG  ? A CYS 325 ? A CYS 394 ? 1_555 116.7 ? 
7  SG  ? C CYS 7   ? C CYS 872 ? 1_555 ZN ? J ZN . ? C ZN 900 ? 1_555 SG  ? C CYS 10  ? C CYS 875 ? 1_555 113.9 ? 
8  SG  ? C CYS 7   ? C CYS 872 ? 1_555 ZN ? J ZN . ? C ZN 900 ? 1_555 NE2 ? C HIS 23  ? C HIS 888 ? 1_555 104.4 ? 
9  SG  ? C CYS 10  ? C CYS 875 ? 1_555 ZN ? J ZN . ? C ZN 900 ? 1_555 NE2 ? C HIS 23  ? C HIS 888 ? 1_555 90.2  ? 
10 SG  ? C CYS 7   ? C CYS 872 ? 1_555 ZN ? J ZN . ? C ZN 900 ? 1_555 NE2 ? C HIS 27  ? C HIS 892 ? 1_555 103.9 ? 
11 SG  ? C CYS 10  ? C CYS 875 ? 1_555 ZN ? J ZN . ? C ZN 900 ? 1_555 NE2 ? C HIS 27  ? C HIS 892 ? 1_555 133.1 ? 
12 NE2 ? C HIS 23  ? C HIS 888 ? 1_555 ZN ? J ZN . ? C ZN 900 ? 1_555 NE2 ? C HIS 27  ? C HIS 892 ? 1_555 106.6 ? 
13 SG  ? D CYS 254 ? D CYS 323 ? 1_555 ZN ? K ZN . ? D ZN 501 ? 1_555 SG  ? D CYS 257 ? D CYS 326 ? 1_555 101.7 ? 
14 SG  ? D CYS 254 ? D CYS 323 ? 1_555 ZN ? K ZN . ? D ZN 501 ? 1_555 SG  ? D CYS 322 ? D CYS 391 ? 1_555 116.9 ? 
15 SG  ? D CYS 257 ? D CYS 326 ? 1_555 ZN ? K ZN . ? D ZN 501 ? 1_555 SG  ? D CYS 322 ? D CYS 391 ? 1_555 108.6 ? 
16 SG  ? D CYS 254 ? D CYS 323 ? 1_555 ZN ? K ZN . ? D ZN 501 ? 1_555 SG  ? D CYS 325 ? D CYS 394 ? 1_555 100.3 ? 
17 SG  ? D CYS 257 ? D CYS 326 ? 1_555 ZN ? K ZN . ? D ZN 501 ? 1_555 SG  ? D CYS 325 ? D CYS 394 ? 1_555 116.1 ? 
18 SG  ? D CYS 322 ? D CYS 391 ? 1_555 ZN ? K ZN . ? D ZN 501 ? 1_555 SG  ? D CYS 325 ? D CYS 394 ? 1_555 112.8 ? 
19 SG  ? F CYS 7   ? F CYS 872 ? 1_555 ZN ? N ZN . ? F ZN 900 ? 1_555 SG  ? F CYS 10  ? F CYS 875 ? 1_555 117.0 ? 
20 SG  ? F CYS 7   ? F CYS 872 ? 1_555 ZN ? N ZN . ? F ZN 900 ? 1_555 NE2 ? F HIS 23  ? F HIS 888 ? 1_555 113.5 ? 
21 SG  ? F CYS 10  ? F CYS 875 ? 1_555 ZN ? N ZN . ? F ZN 900 ? 1_555 NE2 ? F HIS 23  ? F HIS 888 ? 1_555 100.8 ? 
22 SG  ? F CYS 7   ? F CYS 872 ? 1_555 ZN ? N ZN . ? F ZN 900 ? 1_555 NE2 ? F HIS 27  ? F HIS 892 ? 1_555 112.6 ? 
23 SG  ? F CYS 10  ? F CYS 875 ? 1_555 ZN ? N ZN . ? F ZN 900 ? 1_555 NE2 ? F HIS 27  ? F HIS 892 ? 1_555 107.2 ? 
24 NE2 ? F HIS 23  ? F HIS 888 ? 1_555 ZN ? N ZN . ? F ZN 900 ? 1_555 NE2 ? F HIS 27  ? F HIS 892 ? 1_555 104.5 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS B 18 ? CYS B 313 ? CYS B 18 ? 1_555 CYS B 313 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS E 18 ? CYS E 313 ? CYS E 18 ? 1_555 CYS E 313 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 341 A . ? SER 410 A PRO 342 A ? PRO 411 A 1 2.37   
2 GLY 357 B . ? GLY 357 B PRO 358 B ? PRO 358 B 1 -12.11 
3 ASN 666 B . ? ASN 970 B ALA 667 B ? ALA 971 B 1 -7.53  
4 SER 341 D . ? SER 410 D PRO 342 D ? PRO 411 D 1 -2.39  
5 GLY 357 E . ? GLY 357 E PRO 358 E ? PRO 358 E 1 -7.15  
6 ASN 666 E . ? ASN 970 E ALA 667 E ? ALA 971 E 1 -7.38  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
AA4 ? 6 ? 
AA5 ? 5 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
AB4 ? 4 ? 
AB5 ? 4 ? 
AB6 ? 3 ? 
AB7 ? 5 ? 
AB8 ? 4 ? 
AB9 ? 4 ? 
AC1 ? 4 ? 
AC2 ? 4 ? 
AC3 ? 4 ? 
AC4 ? 2 ? 
AC5 ? 7 ? 
AC6 ? 3 ? 
AC7 ? 6 ? 
AC8 ? 5 ? 
AC9 ? 4 ? 
AD1 ? 4 ? 
AD2 ? 3 ? 
AD3 ? 4 ? 
AD4 ? 4 ? 
AD5 ? 4 ? 
AD6 ? 4 ? 
AD7 ? 4 ? 
AD8 ? 3 ? 
AD9 ? 5 ? 
AE1 ? 4 ? 
AE2 ? 4 ? 
AE3 ? 4 ? 
AE4 ? 4 ? 
AE5 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB7 4 5 ? parallel      
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC5 3 4 ? anti-parallel 
AC5 4 5 ? parallel      
AC5 5 6 ? anti-parallel 
AC5 6 7 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC7 2 3 ? anti-parallel 
AC7 3 4 ? anti-parallel 
AC7 4 5 ? anti-parallel 
AC7 5 6 ? anti-parallel 
AC8 1 2 ? anti-parallel 
AC8 2 3 ? anti-parallel 
AC8 3 4 ? anti-parallel 
AC8 4 5 ? parallel      
AC9 1 2 ? anti-parallel 
AC9 2 3 ? anti-parallel 
AC9 3 4 ? anti-parallel 
AD1 1 2 ? anti-parallel 
AD1 2 3 ? anti-parallel 
AD1 3 4 ? anti-parallel 
AD2 1 2 ? anti-parallel 
AD2 2 3 ? anti-parallel 
AD3 1 2 ? anti-parallel 
AD3 2 3 ? anti-parallel 
AD3 3 4 ? anti-parallel 
AD4 1 2 ? anti-parallel 
AD4 2 3 ? anti-parallel 
AD4 3 4 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD5 2 3 ? anti-parallel 
AD5 3 4 ? anti-parallel 
AD6 1 2 ? anti-parallel 
AD6 2 3 ? anti-parallel 
AD6 3 4 ? anti-parallel 
AD7 1 2 ? anti-parallel 
AD7 2 3 ? anti-parallel 
AD7 3 4 ? anti-parallel 
AD8 1 2 ? anti-parallel 
AD8 2 3 ? anti-parallel 
AD9 1 2 ? anti-parallel 
AD9 2 3 ? anti-parallel 
AD9 3 4 ? anti-parallel 
AD9 4 5 ? parallel      
AE1 1 2 ? anti-parallel 
AE1 2 3 ? anti-parallel 
AE1 3 4 ? anti-parallel 
AE2 1 2 ? anti-parallel 
AE2 2 3 ? anti-parallel 
AE2 3 4 ? anti-parallel 
AE3 1 2 ? anti-parallel 
AE3 2 3 ? anti-parallel 
AE3 3 4 ? anti-parallel 
AE4 1 2 ? anti-parallel 
AE4 2 3 ? anti-parallel 
AE4 3 4 ? anti-parallel 
AE5 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 27  ? LEU A 32  ? THR A 96   LEU A 101  
AA1 2 VAL A 86  ? VAL A 98  ? VAL A 155  VAL A 167  
AA1 3 PHE A 66  ? ARG A 76  ? PHE A 135  ARG A 145  
AA1 4 THR A 50  ? LEU A 54  ? THR A 119  LEU A 123  
AA1 5 CYS A 9   ? VAL A 14  ? CYS A 78   VAL A 83   
AA1 6 GLN A 109 ? ILE A 115 ? GLN A 178  ILE A 184  
AA1 7 ARG A 102 ? THR A 103 ? ARG A 171  THR A 172  
AA2 1 THR A 27  ? LEU A 32  ? THR A 96   LEU A 101  
AA2 2 VAL A 86  ? VAL A 98  ? VAL A 155  VAL A 167  
AA2 3 GLN A 109 ? ILE A 115 ? GLN A 178  ILE A 184  
AA2 4 ARG A 102 ? THR A 103 ? ARG A 171  THR A 172  
AA3 1 GLU A 261 ? THR A 264 ? GLU A 330  THR A 333  
AA3 2 SER A 251 ? CYS A 254 ? SER A 320  CYS A 323  
AA3 3 LEU A 353 ? THR A 356 ? LEU A 422  THR A 425  
AA4 1 MET A 277 ? VAL A 281 ? MET A 346  VAL A 350  
AA4 2 VAL A 287 ? VAL A 293 ? VAL A 356  VAL A 362  
AA4 3 LYS A 344 ? THR A 349 ? LYS A 413  THR A 418  
AA4 4 HIS A 328 ? ALA A 335 ? HIS A 397  ALA A 404  
AA4 5 TYR A 315 ? CYS A 322 ? TYR A 384  CYS A 391  
AA4 6 LEU A 299 ? SER A 306 ? LEU A 368  SER A 375  
AA5 1 VAL B 700 ? HIS B 705 ? VAL B 1004 HIS B 1009 
AA5 2 GLN B 721 ? THR B 728 ? GLN B 1025 THR B 1032 
AA5 3 ILE B 733 ? SER B 738 ? ILE B 1037 SER B 1042 
AA5 4 ASN B 4   ? GLN B 10  ? ASN B 4    GLN B 10   
AA5 5 PHE B 784 ? ASP B 786 ? PHE B 1088 ASP B 1090 
AA6 1 GLY B 17  ? GLY B 21  ? GLY B 17   GLY B 21   
AA6 2 ASN B 30  ? LYS B 35  ? ASN B 30   LYS B 35   
AA6 3 ARG B 38  ? VAL B 44  ? ARG B 38   VAL B 44   
AA6 4 LEU B 49  ? GLY B 56  ? LEU B 49   GLY B 56   
AA7 1 ILE B 61  ? PHE B 67  ? ILE B 61   PHE B 67   
AA7 2 LEU B 76  ? THR B 81  ? LEU B 76   THR B 81   
AA7 3 ASN B 85  ? SER B 94  ? ASN B 85   SER B 94   
AA7 4 SER B 97  ? ASN B 107 ? SER B 97   ASN B 107  
AA8 1 ILE B 121 ? ILE B 124 ? ILE B 121  ILE B 124  
AA8 2 MET B 130 ? ARG B 134 ? MET B 130  ARG B 134  
AA8 3 LEU B 139 ? PRO B 144 ? LEU B 139  PRO B 144  
AA8 4 PHE B 155 ? ARG B 158 ? PHE B 155  ARG B 158  
AA9 1 VAL B 164 ? PHE B 169 ? VAL B 164  PHE B 169  
AA9 2 THR B 177 ? ASP B 184 ? THR B 177  ASP B 184  
AA9 3 GLY B 187 ? SER B 196 ? GLY B 187  SER B 196  
AA9 4 GLU B 201 ? ASN B 203 ? GLU B 201  ASN B 203  
AB1 1 VAL B 164 ? PHE B 169 ? VAL B 164  PHE B 169  
AB1 2 THR B 177 ? ASP B 184 ? THR B 177  ASP B 184  
AB1 3 GLY B 187 ? SER B 196 ? GLY B 187  SER B 196  
AB1 4 LYS B 208 ? GLN B 209 ? LYS B 208  GLN B 209  
AB2 1 MET B 218 ? ALA B 221 ? MET B 218  ALA B 221  
AB2 2 ALA B 229 ? ILE B 232 ? ALA B 229  ILE B 232  
AB2 3 ILE B 237 ? ASN B 241 ? ILE B 237  ASN B 241  
AB2 4 LYS B 244 ? ILE B 248 ? LYS B 244  ILE B 248  
AB3 1 ILE B 258 ? ARG B 263 ? ILE B 258  ARG B 263  
AB3 2 ARG B 270 ? ASP B 275 ? ARG B 270  ASP B 275  
AB3 3 ARG B 279 ? GLU B 289 ? ARG B 279  GLU B 289  
AB3 4 VAL B 295 ? GLU B 307 ? VAL B 295  GLU B 307  
AB4 1 ALA B 311 ? ASP B 318 ? ALA B 311  ASP B 318  
AB4 2 VAL B 321 ? SER B 326 ? VAL B 321  SER B 326  
AB4 3 SER B 331 ? LEU B 336 ? SER B 331  LEU B 336  
AB4 4 VAL B 347 ? PHE B 353 ? VAL B 347  PHE B 353  
AB5 1 ILE B 359 ? VAL B 365 ? ILE B 359  VAL B 365  
AB5 2 GLN B 374 ? SER B 379 ? GLN B 374  SER B 379  
AB5 3 SER B 386 ? ARG B 391 ? SER B 386  ARG B 391  
AB5 4 HIS B 407 ? PRO B 412 ? HIS B 711  PRO B 716  
AB6 1 SER B 416 ? GLN B 423 ? SER B 720  GLN B 727  
AB6 2 CYS B 428 ? GLN B 439 ? CYS B 732  GLN B 743  
AB6 3 THR B 445 ? ALA B 447 ? THR B 749  ALA B 751  
AB7 1 SER B 416 ? GLN B 423 ? SER B 720  GLN B 727  
AB7 2 CYS B 428 ? GLN B 439 ? CYS B 732  GLN B 743  
AB7 3 GLU B 481 ? ASP B 491 ? GLU B 785  ASP B 795  
AB7 4 VAL B 497 ? GLN B 502 ? VAL B 801  GLN B 806  
AB7 5 SER B 458 ? VAL B 461 ? SER B 762  VAL B 765  
AB8 1 GLU B 507 ? LYS B 516 ? GLU B 811  LYS B 820  
AB8 2 THR B 523 ? MET B 531 ? THR B 827  MET B 835  
AB8 3 GLY B 542 ? TYR B 549 ? GLY B 846  TYR B 853  
AB8 4 LEU B 554 ? VAL B 562 ? LEU B 858  VAL B 866  
AB9 1 VAL B 566 ? GLU B 571 ? VAL B 870  GLU B 875  
AB9 2 LEU B 576 ? ILE B 580 ? LEU B 880  ILE B 884  
AB9 3 THR B 583 ? TRP B 589 ? THR B 887  TRP B 893  
AB9 4 LEU B 595 ? TYR B 602 ? LEU B 899  TYR B 906  
AC1 1 TYR B 609 ? LYS B 613 ? TYR B 913  LYS B 917  
AC1 2 PHE B 616 ? GLY B 620 ? PHE B 920  GLY B 924  
AC1 3 SER B 625 ? LYS B 632 ? SER B 929  LYS B 936  
AC1 4 ASN B 637 ? PHE B 638 ? ASN B 941  PHE B 942  
AC2 1 TYR B 609 ? LYS B 613 ? TYR B 913  LYS B 917  
AC2 2 PHE B 616 ? GLY B 620 ? PHE B 920  GLY B 924  
AC2 3 SER B 625 ? LYS B 632 ? SER B 929  LYS B 936  
AC2 4 ALA B 642 ? PHE B 645 ? ALA B 946  PHE B 949  
AC3 1 MET B 650 ? ILE B 655 ? MET B 954  ILE B 959  
AC3 2 ASN B 660 ? GLU B 665 ? ASN B 964  GLU B 969  
AC3 3 ASN B 669 ? LYS B 675 ? ASN B 973  LYS B 979  
AC3 4 LEU B 688 ? HIS B 695 ? LEU B 992  HIS B 999  
AC4 1 PHE B 772 ? HIS B 773 ? PHE B 1076 HIS B 1077 
AC4 2 THR B 778 ? GLU B 779 ? THR B 1082 GLU B 1083 
AC5 1 THR D 27  ? LEU D 32  ? THR D 96   LEU D 101  
AC5 2 VAL D 86  ? GLU D 100 ? VAL D 155  GLU D 169  
AC5 3 GLN D 109 ? ILE D 115 ? GLN D 178  ILE D 184  
AC5 4 CYS D 9   ? VAL D 14  ? CYS D 78   VAL D 83   
AC5 5 THR D 50  ? ALA D 55  ? THR D 119  ALA D 124  
AC5 6 PHE D 66  ? GLU D 77  ? PHE D 135  GLU D 146  
AC5 7 VAL D 86  ? GLU D 100 ? VAL D 155  GLU D 169  
AC6 1 GLU D 261 ? THR D 264 ? GLU D 330  THR D 333  
AC6 2 SER D 251 ? CYS D 254 ? SER D 320  CYS D 323  
AC6 3 LEU D 353 ? THR D 356 ? LEU D 422  THR D 425  
AC7 1 MET D 277 ? VAL D 281 ? MET D 346  VAL D 350  
AC7 2 VAL D 287 ? VAL D 293 ? VAL D 356  VAL D 362  
AC7 3 LYS D 344 ? THR D 349 ? LYS D 413  THR D 418  
AC7 4 HIS D 328 ? ALA D 335 ? HIS D 397  ALA D 404  
AC7 5 TYR D 315 ? CYS D 322 ? TYR D 384  CYS D 391  
AC7 6 LEU D 299 ? LEU D 301 ? LEU D 368  LEU D 370  
AC8 1 VAL E 700 ? HIS E 705 ? VAL E 1004 HIS E 1009 
AC8 2 GLN E 721 ? THR E 728 ? GLN E 1025 THR E 1032 
AC8 3 ILE E 733 ? LEU E 739 ? ILE E 1037 LEU E 1043 
AC8 4 TYR E 3   ? GLN E 10  ? TYR E 3    GLN E 10   
AC8 5 PHE E 784 ? ASP E 786 ? PHE E 1088 ASP E 1090 
AC9 1 GLY E 17  ? GLY E 21  ? GLY E 17   GLY E 21   
AC9 2 ASN E 30  ? LYS E 35  ? ASN E 30   LYS E 35   
AC9 3 ARG E 38  ? VAL E 44  ? ARG E 38   VAL E 44   
AC9 4 LEU E 49  ? GLY E 56  ? LEU E 49   GLY E 56   
AD1 1 ILE E 61  ? PHE E 67  ? ILE E 61   PHE E 67   
AD1 2 LEU E 76  ? THR E 81  ? LEU E 76   THR E 81   
AD1 3 ASN E 85  ? SER E 94  ? ASN E 85   SER E 94   
AD1 4 SER E 97  ? ASN E 107 ? SER E 97   ASN E 107  
AD2 1 ILE E 121 ? ILE E 124 ? ILE E 121  ILE E 124  
AD2 2 MET E 130 ? ARG E 134 ? MET E 130  ARG E 134  
AD2 3 LYS E 141 ? PRO E 144 ? LYS E 141  PRO E 144  
AD3 1 VAL E 164 ? PHE E 169 ? VAL E 164  PHE E 169  
AD3 2 THR E 177 ? ASP E 184 ? THR E 177  ASP E 184  
AD3 3 GLY E 187 ? SER E 196 ? GLY E 187  SER E 196  
AD3 4 GLU E 201 ? GLN E 209 ? GLU E 201  GLN E 209  
AD4 1 MET E 218 ? ALA E 221 ? MET E 218  ALA E 221  
AD4 2 ALA E 229 ? ILE E 232 ? ALA E 229  ILE E 232  
AD4 3 ILE E 237 ? ASN E 241 ? ILE E 237  ASN E 241  
AD4 4 LYS E 244 ? ILE E 248 ? LYS E 244  ILE E 248  
AD5 1 ILE E 258 ? ARG E 263 ? ILE E 258  ARG E 263  
AD5 2 ARG E 270 ? ASP E 275 ? ARG E 270  ASP E 275  
AD5 3 ARG E 279 ? GLU E 289 ? ARG E 279  GLU E 289  
AD5 4 VAL E 295 ? GLU E 307 ? VAL E 295  GLU E 307  
AD6 1 CYS E 313 ? ASP E 318 ? CYS E 313  ASP E 318  
AD6 2 VAL E 321 ? GLY E 325 ? VAL E 321  GLY E 325  
AD6 3 GLN E 332 ? LEU E 336 ? GLN E 332  LEU E 336  
AD6 4 VAL E 347 ? ALA E 349 ? VAL E 347  ALA E 349  
AD7 1 ILE E 359 ? VAL E 365 ? ILE E 359  VAL E 365  
AD7 2 GLN E 374 ? SER E 379 ? GLN E 374  SER E 379  
AD7 3 SER E 386 ? ARG E 391 ? SER E 386  ARG E 391  
AD7 4 HIS E 407 ? PRO E 412 ? HIS E 711  PRO E 716  
AD8 1 SER E 416 ? GLN E 423 ? SER E 720  GLN E 727  
AD8 2 CYS E 428 ? GLN E 439 ? CYS E 732  GLN E 743  
AD8 3 THR E 445 ? ALA E 447 ? THR E 749  ALA E 751  
AD9 1 SER E 416 ? GLN E 423 ? SER E 720  GLN E 727  
AD9 2 CYS E 428 ? GLN E 439 ? CYS E 732  GLN E 743  
AD9 3 GLU E 481 ? ASP E 491 ? GLU E 785  ASP E 795  
AD9 4 VAL E 497 ? GLN E 502 ? VAL E 801  GLN E 806  
AD9 5 SER E 458 ? VAL E 461 ? SER E 762  VAL E 765  
AE1 1 GLU E 507 ? CYS E 515 ? GLU E 811  CYS E 819  
AE1 2 TYR E 524 ? MET E 531 ? TYR E 828  MET E 835  
AE1 3 GLY E 542 ? TYR E 549 ? GLY E 846  TYR E 853  
AE1 4 LEU E 554 ? VAL E 562 ? LEU E 858  VAL E 866  
AE2 1 VAL E 566 ? PHE E 572 ? VAL E 870  PHE E 876  
AE2 2 LYS E 575 ? ILE E 580 ? LYS E 879  ILE E 884  
AE2 3 THR E 583 ? TRP E 589 ? THR E 887  TRP E 893  
AE2 4 LEU E 595 ? TYR E 602 ? LEU E 899  TYR E 906  
AE3 1 TYR E 609 ? LYS E 613 ? TYR E 913  LYS E 917  
AE3 2 PHE E 616 ? GLY E 620 ? PHE E 920  GLY E 924  
AE3 3 SER E 625 ? LYS E 632 ? SER E 929  LYS E 936  
AE3 4 ASN E 637 ? PHE E 645 ? ASN E 941  PHE E 949  
AE4 1 MET E 650 ? ILE E 655 ? MET E 954  ILE E 959  
AE4 2 ASN E 660 ? GLU E 665 ? ASN E 964  GLU E 969  
AE4 3 ASN E 669 ? LYS E 675 ? ASN E 973  LYS E 979  
AE4 4 LEU E 688 ? HIS E 695 ? LEU E 992  HIS E 999  
AE5 1 PHE E 772 ? THR E 774 ? PHE E 1076 THR E 1078 
AE5 2 LYS E 777 ? GLU E 779 ? LYS E 1081 GLU E 1083 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 32  ? N LEU A 101  O VAL A 86  ? O VAL A 155  
AA1 2 3 O GLN A 94  ? O GLN A 163  N THR A 69  ? N THR A 138  
AA1 3 4 O THR A 68  ? O THR A 137  N VAL A 53  ? N VAL A 122  
AA1 4 5 O ALA A 52  ? O ALA A 121  N PRO A 13  ? N PRO A 82   
AA1 5 6 N GLN A 10  ? N GLN A 79   O VAL A 113 ? O VAL A 182  
AA1 6 7 O GLN A 110 ? O GLN A 179  N ARG A 102 ? N ARG A 171  
AA2 1 2 N LEU A 32  ? N LEU A 101  O VAL A 86  ? O VAL A 155  
AA2 2 3 N LYS A 97  ? N LYS A 166  O GLN A 114 ? O GLN A 183  
AA2 3 4 O GLN A 110 ? O GLN A 179  N ARG A 102 ? N ARG A 171  
AA3 1 2 O ILE A 262 ? O ILE A 331  N LEU A 252 ? N LEU A 321  
AA3 2 3 N CYS A 253 ? N CYS A 322  O LEU A 354 ? O LEU A 423  
AA4 1 2 N ALA A 278 ? N ALA A 347  O THR A 290 ? O THR A 359  
AA4 2 3 N LEU A 291 ? N LEU A 360  O LEU A 348 ? O LEU A 417  
AA4 3 4 O PHE A 345 ? O PHE A 414  N PHE A 333 ? N PHE A 402  
AA4 4 5 O GLY A 330 ? O GLY A 399  N ALA A 320 ? N ALA A 389  
AA4 5 6 O VAL A 319 ? O VAL A 388  N ILE A 302 ? N ILE A 371  
AA5 1 2 N CYS B 704 ? N CYS B 1008 O LEU B 725 ? O LEU B 1029 
AA5 2 3 N PHE B 726 ? N PHE B 1030 O GLY B 734 ? O GLY B 1038 
AA5 3 4 O THR B 737 ? O THR B 1041 N TYR B 5   ? N TYR B 5    
AA5 4 5 N VAL B 6   ? N VAL B 6    O ILE B 785 ? O ILE B 1089 
AA6 1 2 N VAL B 19  ? N VAL B 19   O LEU B 32  ? O LEU B 32   
AA6 2 3 N LYS B 35  ? N LYS B 35   O ARG B 38  ? O ARG B 38   
AA6 3 4 N VAL B 43  ? N VAL B 43   O ARG B 50  ? O ARG B 50   
AA7 1 2 N PHE B 67  ? N PHE B 67   O LEU B 76  ? O LEU B 76   
AA7 2 3 N THR B 81  ? N THR B 81   O ASN B 85  ? O ASN B 85   
AA7 3 4 N LYS B 92  ? N LYS B 92   O ASP B 99  ? O ASP B 99   
AA8 1 2 N ILE B 123 ? N ILE B 123  O GLY B 132 ? O GLY B 132  
AA8 2 3 N ILE B 131 ? N ILE B 131  O ILE B 143 ? O ILE B 143  
AA8 3 4 N PHE B 140 ? N PHE B 140  O ILE B 157 ? O ILE B 157  
AA9 1 2 N ILE B 165 ? N ILE B 165  O VAL B 181 ? O VAL B 181  
AA9 2 3 N TYR B 182 ? N TYR B 182  O HIS B 189 ? O HIS B 189  
AA9 3 4 N GLU B 194 ? N GLU B 194  O ASN B 203 ? O ASN B 203  
AB1 1 2 N ILE B 165 ? N ILE B 165  O VAL B 181 ? O VAL B 181  
AB1 2 3 N TYR B 182 ? N TYR B 182  O HIS B 189 ? O HIS B 189  
AB1 3 4 N VAL B 190 ? N VAL B 190  O GLN B 209 ? O GLN B 209  
AB2 1 2 N ILE B 220 ? N ILE B 220  O ILE B 230 ? O ILE B 230  
AB2 2 3 N ILE B 231 ? N ILE B 231  O THR B 238 ? O THR B 238  
AB2 3 4 N ASN B 241 ? N ASN B 241  O LYS B 244 ? O LYS B 244  
AB3 1 2 N VAL B 259 ? N VAL B 259  O GLY B 274 ? O GLY B 274  
AB3 2 3 N LEU B 273 ? N LEU B 273  O PHE B 281 ? O PHE B 281  
AB3 3 4 N MET B 282 ? N MET B 282  O GLU B 303 ? O GLU B 303  
AB4 1 2 N GLU B 312 ? N GLU B 312  O GLY B 325 ? O GLY B 325  
AB4 2 3 N VAL B 322 ? N VAL B 322  O VAL B 334 ? O VAL B 334  
AB4 3 4 N SER B 331 ? N SER B 331  O PHE B 353 ? O PHE B 353  
AB5 1 2 N ASP B 361 ? N ASP B 361  O CYS B 378 ? O CYS B 378  
AB5 2 3 N SER B 379 ? N SER B 379  O SER B 386 ? O SER B 386  
AB5 3 4 N LEU B 387 ? N LEU B 387  O VAL B 411 ? O VAL B 715  
AB6 1 2 N ARG B 418 ? N ARG B 722  O LEU B 432 ? O LEU B 736  
AB6 2 3 N VAL B 438 ? N VAL B 742  O THR B 446 ? O THR B 750  
AB7 1 2 N ARG B 418 ? N ARG B 722  O LEU B 432 ? O LEU B 736  
AB7 2 3 N GLU B 437 ? N GLU B 741  O VAL B 482 ? O VAL B 786  
AB7 3 4 N LEU B 487 ? N LEU B 791  O HIS B 501 ? O HIS B 805  
AB7 4 5 O GLN B 502 ? O GLN B 806  N SER B 460 ? N SER B 764  
AB8 1 2 N VAL B 513 ? N VAL B 817  O ILE B 526 ? O ILE B 830  
AB8 2 3 N PHE B 525 ? N PHE B 829  O PHE B 547 ? O PHE B 851  
AB8 3 4 N VAL B 546 ? N VAL B 850  O VAL B 557 ? O VAL B 861  
AB9 1 2 N VAL B 570 ? N VAL B 874  O LEU B 577 ? O LEU B 881  
AB9 2 3 N ALA B 578 ? N ALA B 882  O ARG B 585 ? O ARG B 889  
AB9 3 4 N VAL B 584 ? N VAL B 888  O HIS B 601 ? O HIS B 905  
AC1 1 2 N LYS B 611 ? N LYS B 915  O LEU B 618 ? O LEU B 922  
AC1 2 3 N ILE B 617 ? N ILE B 921  O LEU B 629 ? O LEU B 933  
AC1 3 4 N LYS B 632 ? N LYS B 936  O ASN B 637 ? O ASN B 941  
AC2 1 2 N LYS B 611 ? N LYS B 915  O LEU B 618 ? O LEU B 922  
AC2 2 3 N ILE B 617 ? N ILE B 921  O LEU B 629 ? O LEU B 933  
AC2 3 4 N LEU B 628 ? N LEU B 932  O ALA B 642 ? O ALA B 946  
AC3 1 2 N GLU B 654 ? N GLU B 958  O LEU B 662 ? O LEU B 966  
AC3 2 3 N GLU B 665 ? N GLU B 969  O ASN B 669 ? O ASN B 973  
AC3 3 4 N LEU B 670 ? N LEU B 974  O PHE B 694 ? O PHE B 998  
AC4 1 2 N PHE B 772 ? N PHE B 1076 O GLU B 779 ? O GLU B 1083 
AC5 1 2 N LEU D 30  ? N LEU D 99   O VAL D 88  ? O VAL D 157  
AC5 2 3 N LEU D 99  ? N LEU D 168  O LYS D 112 ? O LYS D 181  
AC5 3 4 O GLN D 109 ? O GLN D 178  N VAL D 14  ? N VAL D 83   
AC5 4 5 N PRO D 13  ? N PRO D 82   O ALA D 52  ? O ALA D 121  
AC5 5 6 N VAL D 53  ? N VAL D 122  O THR D 68  ? O THR D 137  
AC5 6 7 N THR D 69  ? N THR D 138  O GLN D 94  ? O GLN D 163  
AC6 1 2 O THR D 263 ? O THR D 332  N LEU D 252 ? N LEU D 321  
AC6 2 3 N SER D 251 ? N SER D 320  O THR D 356 ? O THR D 425  
AC7 1 2 N TYR D 280 ? N TYR D 349  O HIS D 288 ? O HIS D 357  
AC7 2 3 N VAL D 293 ? N VAL D 362  O TRP D 346 ? O TRP D 415  
AC7 3 4 O PHE D 345 ? O PHE D 414  N PHE D 333 ? N PHE D 402  
AC7 4 5 O THR D 334 ? O THR D 403  N ALA D 316 ? N ALA D 385  
AC7 5 6 O GLN D 321 ? O GLN D 390  N ASN D 300 ? N ASN D 369  
AC8 1 2 N CYS E 704 ? N CYS E 1008 O LEU E 725 ? O LEU E 1029 
AC8 2 3 N VAL E 724 ? N VAL E 1028 O VAL E 736 ? O VAL E 1040 
AC8 3 4 O ILE E 733 ? O ILE E 1037 N GLN E 10  ? N GLN E 10   
AC8 4 5 N VAL E 6   ? N VAL E 6    O ILE E 785 ? O ILE E 1089 
AC9 1 2 N GLY E 21  ? N GLY E 21   O ASN E 30  ? O ASN E 30   
AC9 2 3 N ILE E 33  ? N ILE E 33   O GLU E 40  ? O GLU E 40   
AC9 3 4 N ILE E 41  ? N ILE E 41   O LYS E 53  ? O LYS E 53   
AD1 1 2 N PHE E 67  ? N PHE E 67   O LEU E 76  ? O LEU E 76   
AD1 2 3 N LEU E 77  ? N LEU E 77   O LEU E 89  ? O LEU E 89   
AD1 3 4 N ALA E 86  ? N ALA E 86   O GLY E 106 ? O GLY E 106  
AD2 1 2 N ILE E 123 ? N ILE E 123  O GLY E 132 ? O GLY E 132  
AD2 2 3 N ILE E 131 ? N ILE E 131  O ILE E 143 ? O ILE E 143  
AD3 1 2 N ILE E 165 ? N ILE E 165  O VAL E 181 ? O VAL E 181  
AD3 2 3 N PHE E 180 ? N PHE E 180  O LYS E 191 ? O LYS E 191  
AD3 3 4 N GLU E 194 ? N GLU E 194  O ASN E 203 ? O ASN E 203  
AD4 1 2 N ILE E 220 ? N ILE E 220  O ILE E 230 ? O ILE E 230  
AD4 2 3 N ILE E 231 ? N ILE E 231  O THR E 238 ? O THR E 238  
AD4 3 4 N TYR E 239 ? N TYR E 239  O LEU E 246 ? O LEU E 246  
AD5 1 2 N ASN E 262 ? N ASN E 262  O LEU E 272 ? O LEU E 272  
AD5 2 3 N TYR E 271 ? N TYR E 271  O LEU E 283 ? O LEU E 283  
AD5 3 4 N MET E 282 ? N MET E 282  O GLU E 303 ? O GLU E 303  
AD6 1 2 N LEU E 317 ? N LEU E 317  O VAL E 321 ? O VAL E 321  
AD6 2 3 N VAL E 324 ? N VAL E 324  O GLN E 332 ? O GLN E 332  
AD6 3 4 N LYS E 335 ? N LYS E 335  O VAL E 348 ? O VAL E 348  
AD7 1 2 N ASP E 361 ? N ASP E 361  O CYS E 378 ? O CYS E 378  
AD7 2 3 N SER E 379 ? N SER E 379  O SER E 386 ? O SER E 386  
AD7 3 4 N LEU E 387 ? N LEU E 387  O VAL E 411 ? O VAL E 715  
AD8 1 2 N CYS E 421 ? N CYS E 725  O GLY E 430 ? O GLY E 734  
AD8 2 3 N VAL E 438 ? N VAL E 742  O THR E 446 ? O THR E 750  
AD9 1 2 N CYS E 421 ? N CYS E 725  O GLY E 430 ? O GLY E 734  
AD9 2 3 N VAL E 431 ? N VAL E 735  O LEU E 488 ? O LEU E 792  
AD9 3 4 N ILE E 489 ? N ILE E 793  O LEU E 498 ? O LEU E 802  
AD9 4 5 O GLN E 502 ? O GLN E 806  N SER E 460 ? N SER E 764  
AE1 1 2 N TYR E 508 ? N TYR E 812  O ALA E 530 ? O ALA E 834  
AE1 2 3 N VAL E 527 ? N VAL E 831  O VAL E 545 ? O VAL E 849  
AE1 3 4 N VAL E 546 ? N VAL E 850  O VAL E 557 ? O VAL E 861  
AE2 1 2 N VAL E 570 ? N VAL E 874  O LEU E 577 ? O LEU E 881  
AE2 2 3 N ILE E 580 ? N ILE E 884  O THR E 583 ? O THR E 887  
AE2 3 4 N LEU E 586 ? N LEU E 890  O GLU E 598 ? O GLU E 902  
AE3 1 2 N LYS E 611 ? N LYS E 915  O LEU E 618 ? O LEU E 922  
AE3 2 3 N ILE E 617 ? N ILE E 921  O LEU E 629 ? O LEU E 933  
AE3 3 4 N LYS E 632 ? N LYS E 936  O ASN E 637 ? O ASN E 941  
AE4 1 2 N GLU E 654 ? N GLU E 958  O LEU E 662 ? O LEU E 966  
AE4 2 3 N GLY E 663 ? N GLY E 967  O PHE E 671 ? O PHE E 975  
AE4 3 4 N LEU E 670 ? N LEU E 974  O PHE E 694 ? O PHE E 998  
AE5 1 2 N THR E 774 ? N THR E 1078 O LYS E 777 ? O LYS E 1081 
# 
_pdbx_entry_details.entry_id                   9DJT 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_1              186 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_2              186 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             C 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_3              186 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                97.76 
_pdbx_validate_rmsd_angle.angle_target_value         111.70 
_pdbx_validate_rmsd_angle.angle_deviation            -13.94 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.10 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PRO A 85   ? ? -60.69  -79.83  
2  1 LYS A 116  ? ? -108.35 -81.03  
3  1 ALA A 143  ? ? -172.18 122.94  
4  1 ARG A 162  ? ? -124.68 -55.04  
5  1 ASP A 265  ? ? -162.72 83.75   
6  1 ASN A 267  ? ? -168.81 -115.71 
7  1 LYS A 269  ? ? -161.49 3.93    
8  1 ASP A 270  ? ? -99.89  -125.56 
9  1 GLN A 327  ? ? 64.40   -2.31   
10 1 THR A 329  ? ? -169.70 105.81  
11 1 CYS A 343  ? ? -10.03  -69.68  
12 1 PRO A 352  ? ? -56.31  -5.23   
13 1 ASN B 36   ? ? 52.90   -127.23 
14 1 VAL B 52   ? ? -131.78 -51.29  
15 1 LYS B 53   ? ? -172.28 138.34  
16 1 LYS B 83   ? ? -91.32  31.54   
17 1 LYS B 92   ? ? -160.50 114.65  
18 1 ASP B 148  ? ? -69.28  92.72   
19 1 ASN B 211  ? ? -170.23 108.38  
20 1 SER B 217  ? ? -143.16 -34.04  
21 1 ASP B 275  ? ? -104.75 -166.32 
22 1 LEU B 317  ? ? -108.90 -70.97  
23 1 ASP B 318  ? ? 177.89  162.92  
24 1 ASN B 341  ? ? -111.19 -168.73 
25 1 GLN B 372  ? ? -95.73  -77.55  
26 1 PHE B 382  ? ? 59.87   -134.05 
27 1 SER B 755  ? ? 179.89  -179.14 
28 1 GLN B 759  ? ? -115.88 65.88   
29 1 THR B 780  ? ? -97.09  -111.44 
30 1 LEU B 814  ? ? -123.66 -52.26  
31 1 SER B 854  ? ? -138.16 -63.83  
32 1 ASP B 855  ? ? -106.14 62.38   
33 1 LYS B 867  ? ? -110.93 51.54   
34 1 PHE B 876  ? ? -118.03 63.16   
35 1 ASN B 877  ? ? 58.61   70.67   
36 1 ASN B 885  ? ? 48.22   -117.13 
37 1 ASN B 952  ? ? 171.09  158.00  
38 1 ALA B 956  ? ? 176.90  153.88  
39 1 VAL B 957  ? ? -170.33 143.77  
40 1 ALA B 983  ? ? -68.30  99.74   
41 1 THR B 984  ? ? -108.61 -85.88  
42 1 GLN B 990  ? ? -95.10  42.90   
43 1 ASP D 76   ? ? -104.57 40.26   
44 1 MET D 88   ? ? -155.49 44.68   
45 1 LYS D 116  ? ? -138.00 -123.34 
46 1 PHE D 120  ? ? -117.53 -169.68 
47 1 GLU D 147  ? ? -161.76 83.26   
48 1 GLN D 148  ? ? -59.31  108.49  
49 1 PHE D 150  ? ? 53.47   -128.48 
50 1 ARG D 162  ? ? -125.80 -76.64  
51 1 LEU D 168  ? ? -103.81 -60.91  
52 1 LEU D 170  ? ? -154.03 57.83   
53 1 CYS D 234  ? ? -68.78  0.55    
54 1 ASP D 265  ? ? -175.00 140.27  
55 1 ASN D 267  ? ? -111.33 -155.24 
56 1 ASP D 271  ? ? 51.11   -83.90  
57 1 SER D 272  ? ? 2.69    -79.82  
58 1 CYS D 318  ? ? -100.73 65.19   
59 1 GLN D 327  ? ? 48.42   17.24   
60 1 THR D 329  ? ? -160.48 93.06   
61 1 ASN D 335  ? ? -67.98  2.89    
62 1 PRO D 352  ? ? -77.66  21.74   
63 1 ALA D 395  ? ? 47.12   18.17   
64 1 LYS D 406  ? ? -121.71 -165.74 
65 1 ASN E 36   ? ? 54.18   -130.60 
66 1 VAL E 52   ? ? -107.31 -61.76  
67 1 SER E 94   ? ? -115.69 73.02   
68 1 LEU E 145  ? ? -101.99 77.55   
69 1 LYS E 168  ? ? -177.09 136.21  
70 1 LYS E 200  ? ? 34.81   46.50   
71 1 PRO E 225  ? ? -39.46  -74.20  
72 1 ASN E 241  ? ? -160.24 88.86   
73 1 TYR E 245  ? ? -163.10 105.03  
74 1 ASP E 292  ? ? -89.62  31.20   
75 1 LEU E 317  ? ? -102.92 -71.85  
76 1 PHE E 382  ? ? 57.51   -130.81 
77 1 GLN E 759  ? ? -110.78 51.60   
78 1 HIS E 797  ? ? -91.44  -65.61  
79 1 SER E 854  ? ? -153.25 -15.14  
80 1 ALA E 862  ? ? -173.30 149.81  
81 1 LYS E 867  ? ? -93.10  39.51   
82 1 ASN E 885  ? ? 50.91   -125.68 
83 1 ASP E 961  ? ? -136.46 -158.40 
84 1 PHE E 998  ? ? -172.88 127.25  
85 1 SER E 1027 ? ? -171.16 124.86  
86 1 ARG E 1080 ? ? -143.45 43.54   
87 1 ASP E 1099 ? ? -98.97  47.29   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         27.7128 
_pdbx_refine_tls.origin_y         10.8362 
_pdbx_refine_tls.origin_z         -20.4147 
_pdbx_refine_tls.T[1][1]          0.6905 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0644 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0835 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.8674 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0033 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.7978 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.1479 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.2787 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0030 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.7531 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0346 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.2907 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0344 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0227 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0326 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0547 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0538 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0596 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0249 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0085 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0181 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A ARG 70   ? A ARG 1   
2   1 Y 1 A THR 71   ? A THR 2   
3   1 Y 1 A LEU 72   ? A LEU 3   
4   1 Y 1 A SER 126  ? A SER 57  
5   1 Y 1 A ASN 127  ? A ASN 58  
6   1 Y 1 A VAL 128  ? A VAL 59  
7   1 Y 1 A GLN 129  ? A GLN 60  
8   1 Y 1 A GLU 130  ? A GLU 61  
9   1 Y 1 A ARG 131  ? A ARG 62  
10  1 Y 1 A GLU 132  ? A GLU 63  
11  1 Y 1 A GLN 148  ? A GLN 79  
12  1 Y 1 A ASP 149  ? A ASP 80  
13  1 Y 1 A PHE 150  ? A PHE 81  
14  1 Y 1 A GLY 151  ? A GLY 82  
15  1 Y 1 A ILE 152  ? A ILE 83  
16  1 Y 1 A GLU 153  ? A GLU 84  
17  1 Y 1 A LYS 211  ? A LYS 142 
18  1 Y 1 A PRO 212  ? A PRO 143 
19  1 Y 1 A VAL 213  ? A VAL 144 
20  1 Y 1 A SER 214  ? A SER 145 
21  1 Y 1 A ARG 215  ? A ARG 146 
22  1 Y 1 A GLU 216  ? A GLU 147 
23  1 Y 1 A ASP 217  ? A ASP 148 
24  1 Y 1 A GLN 218  ? A GLN 149 
25  1 Y 1 A CYS 219  ? A CYS 150 
26  1 Y 1 A ASP 428  ? A ASP 359 
27  1 Y 1 A THR 429  ? A THR 360 
28  1 Y 1 A GLU 430  ? A GLU 361 
29  1 Y 1 A ASP 431  ? A ASP 362 
30  1 Y 1 A GLU 432  ? A GLU 363 
31  1 Y 1 A ILE 433  ? A ILE 364 
32  1 Y 1 A SER 434  ? A SER 365 
33  1 Y 1 A PRO 435  ? A PRO 366 
34  1 Y 1 A ASP 436  ? A ASP 367 
35  1 Y 1 A LYS 437  ? A LYS 368 
36  1 Y 1 B MET 1    ? B MET 1   
37  1 Y 1 B GLY 697  ? B GLY 393 
38  1 Y 1 B ILE 698  ? B ILE 394 
39  1 Y 1 B GLY 699  ? B GLY 395 
40  1 Y 1 B GLY 700  ? B GLY 396 
41  1 Y 1 B ASN 701  ? B ASN 397 
42  1 Y 1 B GLY 702  ? B GLY 398 
43  1 Y 1 B ASN 703  ? B ASN 399 
44  1 Y 1 B SER 704  ? B SER 400 
45  1 Y 1 B GLY 705  ? B GLY 401 
46  1 Y 1 B GLU 706  ? B GLU 402 
47  1 Y 1 B ILE 707  ? B ILE 403 
48  1 Y 1 B GLN 708  ? B GLN 404 
49  1 Y 1 B LYS 709  ? B LYS 405 
50  1 Y 1 B SER 774  ? B SER 470 
51  1 Y 1 B THR 775  ? B THR 471 
52  1 Y 1 B ALA 776  ? B ALA 472 
53  1 Y 1 B PRO 777  ? B PRO 473 
54  1 Y 1 B GLN 1015 ? B GLN 711 
55  1 Y 1 B ASN 1016 ? B ASN 712 
56  1 Y 1 B LEU 1017 ? B LEU 713 
57  1 Y 1 B GLY 1018 ? B GLY 714 
58  1 Y 1 B GLU 1019 ? B GLU 715 
59  1 Y 1 B THR 1020 ? B THR 716 
60  1 Y 1 B SER 1021 ? B SER 717 
61  1 Y 1 B THR 1022 ? B THR 718 
62  1 Y 1 B TYR 1114 ? B TYR 810 
63  1 Y 1 B ASP 1115 ? B ASP 811 
64  1 Y 1 B ASP 1116 ? B ASP 812 
65  1 Y 1 B GLY 1117 ? B GLY 813 
66  1 Y 1 B SER 1118 ? B SER 814 
67  1 Y 1 B GLY 1119 ? B GLY 815 
68  1 Y 1 B MET 1120 ? B MET 816 
69  1 Y 1 B LYS 1121 ? B LYS 817 
70  1 Y 1 B ARG 1122 ? B ARG 818 
71  1 Y 1 C SER 866  ? C SER 1   
72  1 Y 1 C GLN 867  ? C GLN 2   
73  1 Y 1 C ARG 894  ? C ARG 29  
74  1 Y 1 C GLN 895  ? C GLN 30  
75  1 Y 1 D ARG 70   ? D ARG 1   
76  1 Y 1 D THR 71   ? D THR 2   
77  1 Y 1 D LEU 72   ? D LEU 3   
78  1 Y 1 D SER 126  ? D SER 57  
79  1 Y 1 D ASN 127  ? D ASN 58  
80  1 Y 1 D VAL 128  ? D VAL 59  
81  1 Y 1 D GLN 129  ? D GLN 60  
82  1 Y 1 D GLU 130  ? D GLU 61  
83  1 Y 1 D ARG 131  ? D ARG 62  
84  1 Y 1 D GLU 132  ? D GLU 63  
85  1 Y 1 D SER 214  ? D SER 145 
86  1 Y 1 D ARG 215  ? D ARG 146 
87  1 Y 1 D GLU 216  ? D GLU 147 
88  1 Y 1 D ASP 217  ? D ASP 148 
89  1 Y 1 D GLN 218  ? D GLN 149 
90  1 Y 1 D CYS 219  ? D CYS 150 
91  1 Y 1 D ASP 428  ? D ASP 359 
92  1 Y 1 D THR 429  ? D THR 360 
93  1 Y 1 D GLU 430  ? D GLU 361 
94  1 Y 1 D ASP 431  ? D ASP 362 
95  1 Y 1 D GLU 432  ? D GLU 363 
96  1 Y 1 D ILE 433  ? D ILE 364 
97  1 Y 1 D SER 434  ? D SER 365 
98  1 Y 1 D PRO 435  ? D PRO 366 
99  1 Y 1 D ASP 436  ? D ASP 367 
100 1 Y 1 D LYS 437  ? D LYS 368 
101 1 Y 1 E MET 1    ? E MET 1   
102 1 Y 1 E GLY 697  ? E GLY 393 
103 1 Y 1 E ILE 698  ? E ILE 394 
104 1 Y 1 E GLY 699  ? E GLY 395 
105 1 Y 1 E GLY 700  ? E GLY 396 
106 1 Y 1 E ASN 701  ? E ASN 397 
107 1 Y 1 E GLY 702  ? E GLY 398 
108 1 Y 1 E ASN 703  ? E ASN 399 
109 1 Y 1 E SER 704  ? E SER 400 
110 1 Y 1 E GLY 705  ? E GLY 401 
111 1 Y 1 E GLU 706  ? E GLU 402 
112 1 Y 1 E ILE 707  ? E ILE 403 
113 1 Y 1 E GLN 708  ? E GLN 404 
114 1 Y 1 E LYS 709  ? E LYS 405 
115 1 Y 1 E SER 772  ? E SER 468 
116 1 Y 1 E SER 773  ? E SER 469 
117 1 Y 1 E SER 774  ? E SER 470 
118 1 Y 1 E THR 775  ? E THR 471 
119 1 Y 1 E ALA 776  ? E ALA 472 
120 1 Y 1 E PRO 777  ? E PRO 473 
121 1 Y 1 E HIS 778  ? E HIS 474 
122 1 Y 1 E GLU 779  ? E GLU 475 
123 1 Y 1 E ALA 982  ? E ALA 678 
124 1 Y 1 E GLN 1015 ? E GLN 711 
125 1 Y 1 E ASN 1016 ? E ASN 712 
126 1 Y 1 E LEU 1017 ? E LEU 713 
127 1 Y 1 E GLY 1018 ? E GLY 714 
128 1 Y 1 E GLU 1019 ? E GLU 715 
129 1 Y 1 E THR 1020 ? E THR 716 
130 1 Y 1 E SER 1021 ? E SER 717 
131 1 Y 1 E THR 1022 ? E THR 718 
132 1 Y 1 E GLN 1113 ? E GLN 809 
133 1 Y 1 E TYR 1114 ? E TYR 810 
134 1 Y 1 E ASP 1115 ? E ASP 811 
135 1 Y 1 E ASP 1116 ? E ASP 812 
136 1 Y 1 E GLY 1117 ? E GLY 813 
137 1 Y 1 E SER 1118 ? E SER 814 
138 1 Y 1 E GLY 1119 ? E GLY 815 
139 1 Y 1 E MET 1120 ? E MET 816 
140 1 Y 1 E LYS 1121 ? E LYS 817 
141 1 Y 1 E ARG 1122 ? E ARG 818 
142 1 Y 1 F SER 866  ? F SER 1   
143 1 Y 1 F GLN 867  ? F GLN 2   
144 1 Y 1 F GLN 895  ? F GLN 30  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1A5H C1   C  Y N 1   
A1A5H C2   C  Y N 2   
A1A5H C3   C  Y N 3   
A1A5H C11  C  N R 4   
A1A5H C13  C  N N 5   
A1A5H C14  C  N N 6   
A1A5H C15  C  N N 7   
A1A5H C17  C  N N 8   
A1A5H C18  C  N N 9   
A1A5H C19  C  N N 10  
A1A5H C20  C  N N 11  
A1A5H C21  C  N N 12  
A1A5H C22  C  N S 13  
A1A5H C23  C  N N 14  
A1A5H C24  C  N N 15  
A1A5H C25  C  N N 16  
A1A5H C27  C  N N 17  
A1A5H C4   C  Y N 18  
A1A5H C5   C  Y N 19  
A1A5H C6   C  Y N 20  
A1A5H C7   C  N N 21  
A1A5H C9   C  N N 22  
A1A5H N16  N  N N 23  
A1A5H N26  N  N N 24  
A1A5H N8   N  N N 25  
A1A5H O10  O  N N 26  
A1A5H O12  O  N N 27  
A1A5H O28  O  N N 28  
A1A5H O29  O  N N 29  
A1A5H H30  H  N N 30  
A1A5H H31  H  N N 31  
A1A5H H35  H  N N 32  
A1A5H H36  H  N N 33  
A1A5H H37  H  N N 34  
A1A5H H39  H  N N 35  
A1A5H H38  H  N N 36  
A1A5H H40  H  N N 37  
A1A5H H41  H  N N 38  
A1A5H H43  H  N N 39  
A1A5H H42  H  N N 40  
A1A5H H45  H  N N 41  
A1A5H H44  H  N N 42  
A1A5H H47  H  N N 43  
A1A5H H46  H  N N 44  
A1A5H H50  H  N N 45  
A1A5H H48  H  N N 46  
A1A5H H49  H  N N 47  
A1A5H H51  H  N N 48  
A1A5H H53  H  N N 49  
A1A5H H52  H  N N 50  
A1A5H H55  H  N N 51  
A1A5H H54  H  N N 52  
A1A5H H32  H  N N 53  
A1A5H H33  H  N N 54  
A1A5H H34  H  N N 55  
A1A5H H56  H  N N 56  
ALA   N    N  N N 57  
ALA   CA   C  N S 58  
ALA   C    C  N N 59  
ALA   O    O  N N 60  
ALA   CB   C  N N 61  
ALA   OXT  O  N N 62  
ALA   H    H  N N 63  
ALA   H2   H  N N 64  
ALA   HA   H  N N 65  
ALA   HB1  H  N N 66  
ALA   HB2  H  N N 67  
ALA   HB3  H  N N 68  
ALA   HXT  H  N N 69  
ARG   N    N  N N 70  
ARG   CA   C  N S 71  
ARG   C    C  N N 72  
ARG   O    O  N N 73  
ARG   CB   C  N N 74  
ARG   CG   C  N N 75  
ARG   CD   C  N N 76  
ARG   NE   N  N N 77  
ARG   CZ   C  N N 78  
ARG   NH1  N  N N 79  
ARG   NH2  N  N N 80  
ARG   OXT  O  N N 81  
ARG   H    H  N N 82  
ARG   H2   H  N N 83  
ARG   HA   H  N N 84  
ARG   HB2  H  N N 85  
ARG   HB3  H  N N 86  
ARG   HG2  H  N N 87  
ARG   HG3  H  N N 88  
ARG   HD2  H  N N 89  
ARG   HD3  H  N N 90  
ARG   HE   H  N N 91  
ARG   HH11 H  N N 92  
ARG   HH12 H  N N 93  
ARG   HH21 H  N N 94  
ARG   HH22 H  N N 95  
ARG   HXT  H  N N 96  
ASN   N    N  N N 97  
ASN   CA   C  N S 98  
ASN   C    C  N N 99  
ASN   O    O  N N 100 
ASN   CB   C  N N 101 
ASN   CG   C  N N 102 
ASN   OD1  O  N N 103 
ASN   ND2  N  N N 104 
ASN   OXT  O  N N 105 
ASN   H    H  N N 106 
ASN   H2   H  N N 107 
ASN   HA   H  N N 108 
ASN   HB2  H  N N 109 
ASN   HB3  H  N N 110 
ASN   HD21 H  N N 111 
ASN   HD22 H  N N 112 
ASN   HXT  H  N N 113 
ASP   N    N  N N 114 
ASP   CA   C  N S 115 
ASP   C    C  N N 116 
ASP   O    O  N N 117 
ASP   CB   C  N N 118 
ASP   CG   C  N N 119 
ASP   OD1  O  N N 120 
ASP   OD2  O  N N 121 
ASP   OXT  O  N N 122 
ASP   H    H  N N 123 
ASP   H2   H  N N 124 
ASP   HA   H  N N 125 
ASP   HB2  H  N N 126 
ASP   HB3  H  N N 127 
ASP   HD2  H  N N 128 
ASP   HXT  H  N N 129 
CYS   N    N  N N 130 
CYS   CA   C  N R 131 
CYS   C    C  N N 132 
CYS   O    O  N N 133 
CYS   CB   C  N N 134 
CYS   SG   S  N N 135 
CYS   OXT  O  N N 136 
CYS   H    H  N N 137 
CYS   H2   H  N N 138 
CYS   HA   H  N N 139 
CYS   HB2  H  N N 140 
CYS   HB3  H  N N 141 
CYS   HG   H  N N 142 
CYS   HXT  H  N N 143 
GLN   N    N  N N 144 
GLN   CA   C  N S 145 
GLN   C    C  N N 146 
GLN   O    O  N N 147 
GLN   CB   C  N N 148 
GLN   CG   C  N N 149 
GLN   CD   C  N N 150 
GLN   OE1  O  N N 151 
GLN   NE2  N  N N 152 
GLN   OXT  O  N N 153 
GLN   H    H  N N 154 
GLN   H2   H  N N 155 
GLN   HA   H  N N 156 
GLN   HB2  H  N N 157 
GLN   HB3  H  N N 158 
GLN   HG2  H  N N 159 
GLN   HG3  H  N N 160 
GLN   HE21 H  N N 161 
GLN   HE22 H  N N 162 
GLN   HXT  H  N N 163 
GLU   N    N  N N 164 
GLU   CA   C  N S 165 
GLU   C    C  N N 166 
GLU   O    O  N N 167 
GLU   CB   C  N N 168 
GLU   CG   C  N N 169 
GLU   CD   C  N N 170 
GLU   OE1  O  N N 171 
GLU   OE2  O  N N 172 
GLU   OXT  O  N N 173 
GLU   H    H  N N 174 
GLU   H2   H  N N 175 
GLU   HA   H  N N 176 
GLU   HB2  H  N N 177 
GLU   HB3  H  N N 178 
GLU   HG2  H  N N 179 
GLU   HG3  H  N N 180 
GLU   HE2  H  N N 181 
GLU   HXT  H  N N 182 
GLY   N    N  N N 183 
GLY   CA   C  N N 184 
GLY   C    C  N N 185 
GLY   O    O  N N 186 
GLY   OXT  O  N N 187 
GLY   H    H  N N 188 
GLY   H2   H  N N 189 
GLY   HA2  H  N N 190 
GLY   HA3  H  N N 191 
GLY   HXT  H  N N 192 
HIS   N    N  N N 193 
HIS   CA   C  N S 194 
HIS   C    C  N N 195 
HIS   O    O  N N 196 
HIS   CB   C  N N 197 
HIS   CG   C  Y N 198 
HIS   ND1  N  Y N 199 
HIS   CD2  C  Y N 200 
HIS   CE1  C  Y N 201 
HIS   NE2  N  Y N 202 
HIS   OXT  O  N N 203 
HIS   H    H  N N 204 
HIS   H2   H  N N 205 
HIS   HA   H  N N 206 
HIS   HB2  H  N N 207 
HIS   HB3  H  N N 208 
HIS   HD1  H  N N 209 
HIS   HD2  H  N N 210 
HIS   HE1  H  N N 211 
HIS   HE2  H  N N 212 
HIS   HXT  H  N N 213 
HOH   O    O  N N 214 
HOH   H1   H  N N 215 
HOH   H2   H  N N 216 
ILE   N    N  N N 217 
ILE   CA   C  N S 218 
ILE   C    C  N N 219 
ILE   O    O  N N 220 
ILE   CB   C  N S 221 
ILE   CG1  C  N N 222 
ILE   CG2  C  N N 223 
ILE   CD1  C  N N 224 
ILE   OXT  O  N N 225 
ILE   H    H  N N 226 
ILE   H2   H  N N 227 
ILE   HA   H  N N 228 
ILE   HB   H  N N 229 
ILE   HG12 H  N N 230 
ILE   HG13 H  N N 231 
ILE   HG21 H  N N 232 
ILE   HG22 H  N N 233 
ILE   HG23 H  N N 234 
ILE   HD11 H  N N 235 
ILE   HD12 H  N N 236 
ILE   HD13 H  N N 237 
ILE   HXT  H  N N 238 
LEU   N    N  N N 239 
LEU   CA   C  N S 240 
LEU   C    C  N N 241 
LEU   O    O  N N 242 
LEU   CB   C  N N 243 
LEU   CG   C  N N 244 
LEU   CD1  C  N N 245 
LEU   CD2  C  N N 246 
LEU   OXT  O  N N 247 
LEU   H    H  N N 248 
LEU   H2   H  N N 249 
LEU   HA   H  N N 250 
LEU   HB2  H  N N 251 
LEU   HB3  H  N N 252 
LEU   HG   H  N N 253 
LEU   HD11 H  N N 254 
LEU   HD12 H  N N 255 
LEU   HD13 H  N N 256 
LEU   HD21 H  N N 257 
LEU   HD22 H  N N 258 
LEU   HD23 H  N N 259 
LEU   HXT  H  N N 260 
LYS   N    N  N N 261 
LYS   CA   C  N S 262 
LYS   C    C  N N 263 
LYS   O    O  N N 264 
LYS   CB   C  N N 265 
LYS   CG   C  N N 266 
LYS   CD   C  N N 267 
LYS   CE   C  N N 268 
LYS   NZ   N  N N 269 
LYS   OXT  O  N N 270 
LYS   H    H  N N 271 
LYS   H2   H  N N 272 
LYS   HA   H  N N 273 
LYS   HB2  H  N N 274 
LYS   HB3  H  N N 275 
LYS   HG2  H  N N 276 
LYS   HG3  H  N N 277 
LYS   HD2  H  N N 278 
LYS   HD3  H  N N 279 
LYS   HE2  H  N N 280 
LYS   HE3  H  N N 281 
LYS   HZ1  H  N N 282 
LYS   HZ2  H  N N 283 
LYS   HZ3  H  N N 284 
LYS   HXT  H  N N 285 
MET   N    N  N N 286 
MET   CA   C  N S 287 
MET   C    C  N N 288 
MET   O    O  N N 289 
MET   CB   C  N N 290 
MET   CG   C  N N 291 
MET   SD   S  N N 292 
MET   CE   C  N N 293 
MET   OXT  O  N N 294 
MET   H    H  N N 295 
MET   H2   H  N N 296 
MET   HA   H  N N 297 
MET   HB2  H  N N 298 
MET   HB3  H  N N 299 
MET   HG2  H  N N 300 
MET   HG3  H  N N 301 
MET   HE1  H  N N 302 
MET   HE2  H  N N 303 
MET   HE3  H  N N 304 
MET   HXT  H  N N 305 
PHE   N    N  N N 306 
PHE   CA   C  N S 307 
PHE   C    C  N N 308 
PHE   O    O  N N 309 
PHE   CB   C  N N 310 
PHE   CG   C  Y N 311 
PHE   CD1  C  Y N 312 
PHE   CD2  C  Y N 313 
PHE   CE1  C  Y N 314 
PHE   CE2  C  Y N 315 
PHE   CZ   C  Y N 316 
PHE   OXT  O  N N 317 
PHE   H    H  N N 318 
PHE   H2   H  N N 319 
PHE   HA   H  N N 320 
PHE   HB2  H  N N 321 
PHE   HB3  H  N N 322 
PHE   HD1  H  N N 323 
PHE   HD2  H  N N 324 
PHE   HE1  H  N N 325 
PHE   HE2  H  N N 326 
PHE   HZ   H  N N 327 
PHE   HXT  H  N N 328 
PRO   N    N  N N 329 
PRO   CA   C  N S 330 
PRO   C    C  N N 331 
PRO   O    O  N N 332 
PRO   CB   C  N N 333 
PRO   CG   C  N N 334 
PRO   CD   C  N N 335 
PRO   OXT  O  N N 336 
PRO   H    H  N N 337 
PRO   HA   H  N N 338 
PRO   HB2  H  N N 339 
PRO   HB3  H  N N 340 
PRO   HG2  H  N N 341 
PRO   HG3  H  N N 342 
PRO   HD2  H  N N 343 
PRO   HD3  H  N N 344 
PRO   HXT  H  N N 345 
SER   N    N  N N 346 
SER   CA   C  N S 347 
SER   C    C  N N 348 
SER   O    O  N N 349 
SER   CB   C  N N 350 
SER   OG   O  N N 351 
SER   OXT  O  N N 352 
SER   H    H  N N 353 
SER   H2   H  N N 354 
SER   HA   H  N N 355 
SER   HB2  H  N N 356 
SER   HB3  H  N N 357 
SER   HG   H  N N 358 
SER   HXT  H  N N 359 
SO4   S    S  N N 360 
SO4   O1   O  N N 361 
SO4   O2   O  N N 362 
SO4   O3   O  N N 363 
SO4   O4   O  N N 364 
THR   N    N  N N 365 
THR   CA   C  N S 366 
THR   C    C  N N 367 
THR   O    O  N N 368 
THR   CB   C  N R 369 
THR   OG1  O  N N 370 
THR   CG2  C  N N 371 
THR   OXT  O  N N 372 
THR   H    H  N N 373 
THR   H2   H  N N 374 
THR   HA   H  N N 375 
THR   HB   H  N N 376 
THR   HG1  H  N N 377 
THR   HG21 H  N N 378 
THR   HG22 H  N N 379 
THR   HG23 H  N N 380 
THR   HXT  H  N N 381 
TRP   N    N  N N 382 
TRP   CA   C  N S 383 
TRP   C    C  N N 384 
TRP   O    O  N N 385 
TRP   CB   C  N N 386 
TRP   CG   C  Y N 387 
TRP   CD1  C  Y N 388 
TRP   CD2  C  Y N 389 
TRP   NE1  N  Y N 390 
TRP   CE2  C  Y N 391 
TRP   CE3  C  Y N 392 
TRP   CZ2  C  Y N 393 
TRP   CZ3  C  Y N 394 
TRP   CH2  C  Y N 395 
TRP   OXT  O  N N 396 
TRP   H    H  N N 397 
TRP   H2   H  N N 398 
TRP   HA   H  N N 399 
TRP   HB2  H  N N 400 
TRP   HB3  H  N N 401 
TRP   HD1  H  N N 402 
TRP   HE1  H  N N 403 
TRP   HE3  H  N N 404 
TRP   HZ2  H  N N 405 
TRP   HZ3  H  N N 406 
TRP   HH2  H  N N 407 
TRP   HXT  H  N N 408 
TYR   N    N  N N 409 
TYR   CA   C  N S 410 
TYR   C    C  N N 411 
TYR   O    O  N N 412 
TYR   CB   C  N N 413 
TYR   CG   C  Y N 414 
TYR   CD1  C  Y N 415 
TYR   CD2  C  Y N 416 
TYR   CE1  C  Y N 417 
TYR   CE2  C  Y N 418 
TYR   CZ   C  Y N 419 
TYR   OH   O  N N 420 
TYR   OXT  O  N N 421 
TYR   H    H  N N 422 
TYR   H2   H  N N 423 
TYR   HA   H  N N 424 
TYR   HB2  H  N N 425 
TYR   HB3  H  N N 426 
TYR   HD1  H  N N 427 
TYR   HD2  H  N N 428 
TYR   HE1  H  N N 429 
TYR   HE2  H  N N 430 
TYR   HH   H  N N 431 
TYR   HXT  H  N N 432 
VAL   N    N  N N 433 
VAL   CA   C  N S 434 
VAL   C    C  N N 435 
VAL   O    O  N N 436 
VAL   CB   C  N N 437 
VAL   CG1  C  N N 438 
VAL   CG2  C  N N 439 
VAL   OXT  O  N N 440 
VAL   H    H  N N 441 
VAL   H2   H  N N 442 
VAL   HA   H  N N 443 
VAL   HB   H  N N 444 
VAL   HG11 H  N N 445 
VAL   HG12 H  N N 446 
VAL   HG13 H  N N 447 
VAL   HG21 H  N N 448 
VAL   HG22 H  N N 449 
VAL   HG23 H  N N 450 
VAL   HXT  H  N N 451 
ZN    ZN   ZN N N 452 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1A5H C1  C2   doub Y N 1   
A1A5H C1  C6   sing Y N 2   
A1A5H C2  C3   sing Y N 3   
A1A5H C2  O12  sing N N 4   
A1A5H C3  C4   doub Y N 5   
A1A5H C4  C5   sing Y N 6   
A1A5H C4  C7   sing N N 7   
A1A5H C5  C6   doub Y N 8   
A1A5H C5  C9   sing N N 9   
A1A5H C7  N8   sing N N 10  
A1A5H N8  C9   sing N N 11  
A1A5H N8  C22  sing N N 12  
A1A5H C9  O10  doub N N 13  
A1A5H C11 O12  sing N N 14  
A1A5H C11 C13  sing N N 15  
A1A5H C11 C17  sing N N 16  
A1A5H C13 C14  sing N N 17  
A1A5H C13 C18  sing N N 18  
A1A5H C13 C19  sing N N 19  
A1A5H C14 C15  sing N N 20  
A1A5H C15 N16  sing N N 21  
A1A5H N16 C17  sing N N 22  
A1A5H N16 C20  sing N N 23  
A1A5H C18 C19  sing N N 24  
A1A5H C20 C21  sing N N 25  
A1A5H C22 C23  sing N N 26  
A1A5H C22 C27  sing N N 27  
A1A5H C23 C24  sing N N 28  
A1A5H C24 C25  sing N N 29  
A1A5H C25 N26  sing N N 30  
A1A5H C25 O29  doub N N 31  
A1A5H N26 C27  sing N N 32  
A1A5H C27 O28  doub N N 33  
A1A5H C1  H30  sing N N 34  
A1A5H C3  H31  sing N N 35  
A1A5H C11 H35  sing N N 36  
A1A5H C14 H36  sing N N 37  
A1A5H C14 H37  sing N N 38  
A1A5H C15 H39  sing N N 39  
A1A5H C15 H38  sing N N 40  
A1A5H C17 H40  sing N N 41  
A1A5H C17 H41  sing N N 42  
A1A5H C18 H43  sing N N 43  
A1A5H C18 H42  sing N N 44  
A1A5H C19 H45  sing N N 45  
A1A5H C19 H44  sing N N 46  
A1A5H C20 H47  sing N N 47  
A1A5H C20 H46  sing N N 48  
A1A5H C21 H50  sing N N 49  
A1A5H C21 H48  sing N N 50  
A1A5H C21 H49  sing N N 51  
A1A5H C22 H51  sing N N 52  
A1A5H C23 H53  sing N N 53  
A1A5H C23 H52  sing N N 54  
A1A5H C24 H55  sing N N 55  
A1A5H C24 H54  sing N N 56  
A1A5H C6  H32  sing N N 57  
A1A5H C7  H33  sing N N 58  
A1A5H C7  H34  sing N N 59  
A1A5H N26 H56  sing N N 60  
ALA   N   CA   sing N N 61  
ALA   N   H    sing N N 62  
ALA   N   H2   sing N N 63  
ALA   CA  C    sing N N 64  
ALA   CA  CB   sing N N 65  
ALA   CA  HA   sing N N 66  
ALA   C   O    doub N N 67  
ALA   C   OXT  sing N N 68  
ALA   CB  HB1  sing N N 69  
ALA   CB  HB2  sing N N 70  
ALA   CB  HB3  sing N N 71  
ALA   OXT HXT  sing N N 72  
ARG   N   CA   sing N N 73  
ARG   N   H    sing N N 74  
ARG   N   H2   sing N N 75  
ARG   CA  C    sing N N 76  
ARG   CA  CB   sing N N 77  
ARG   CA  HA   sing N N 78  
ARG   C   O    doub N N 79  
ARG   C   OXT  sing N N 80  
ARG   CB  CG   sing N N 81  
ARG   CB  HB2  sing N N 82  
ARG   CB  HB3  sing N N 83  
ARG   CG  CD   sing N N 84  
ARG   CG  HG2  sing N N 85  
ARG   CG  HG3  sing N N 86  
ARG   CD  NE   sing N N 87  
ARG   CD  HD2  sing N N 88  
ARG   CD  HD3  sing N N 89  
ARG   NE  CZ   sing N N 90  
ARG   NE  HE   sing N N 91  
ARG   CZ  NH1  sing N N 92  
ARG   CZ  NH2  doub N N 93  
ARG   NH1 HH11 sing N N 94  
ARG   NH1 HH12 sing N N 95  
ARG   NH2 HH21 sing N N 96  
ARG   NH2 HH22 sing N N 97  
ARG   OXT HXT  sing N N 98  
ASN   N   CA   sing N N 99  
ASN   N   H    sing N N 100 
ASN   N   H2   sing N N 101 
ASN   CA  C    sing N N 102 
ASN   CA  CB   sing N N 103 
ASN   CA  HA   sing N N 104 
ASN   C   O    doub N N 105 
ASN   C   OXT  sing N N 106 
ASN   CB  CG   sing N N 107 
ASN   CB  HB2  sing N N 108 
ASN   CB  HB3  sing N N 109 
ASN   CG  OD1  doub N N 110 
ASN   CG  ND2  sing N N 111 
ASN   ND2 HD21 sing N N 112 
ASN   ND2 HD22 sing N N 113 
ASN   OXT HXT  sing N N 114 
ASP   N   CA   sing N N 115 
ASP   N   H    sing N N 116 
ASP   N   H2   sing N N 117 
ASP   CA  C    sing N N 118 
ASP   CA  CB   sing N N 119 
ASP   CA  HA   sing N N 120 
ASP   C   O    doub N N 121 
ASP   C   OXT  sing N N 122 
ASP   CB  CG   sing N N 123 
ASP   CB  HB2  sing N N 124 
ASP   CB  HB3  sing N N 125 
ASP   CG  OD1  doub N N 126 
ASP   CG  OD2  sing N N 127 
ASP   OD2 HD2  sing N N 128 
ASP   OXT HXT  sing N N 129 
CYS   N   CA   sing N N 130 
CYS   N   H    sing N N 131 
CYS   N   H2   sing N N 132 
CYS   CA  C    sing N N 133 
CYS   CA  CB   sing N N 134 
CYS   CA  HA   sing N N 135 
CYS   C   O    doub N N 136 
CYS   C   OXT  sing N N 137 
CYS   CB  SG   sing N N 138 
CYS   CB  HB2  sing N N 139 
CYS   CB  HB3  sing N N 140 
CYS   SG  HG   sing N N 141 
CYS   OXT HXT  sing N N 142 
GLN   N   CA   sing N N 143 
GLN   N   H    sing N N 144 
GLN   N   H2   sing N N 145 
GLN   CA  C    sing N N 146 
GLN   CA  CB   sing N N 147 
GLN   CA  HA   sing N N 148 
GLN   C   O    doub N N 149 
GLN   C   OXT  sing N N 150 
GLN   CB  CG   sing N N 151 
GLN   CB  HB2  sing N N 152 
GLN   CB  HB3  sing N N 153 
GLN   CG  CD   sing N N 154 
GLN   CG  HG2  sing N N 155 
GLN   CG  HG3  sing N N 156 
GLN   CD  OE1  doub N N 157 
GLN   CD  NE2  sing N N 158 
GLN   NE2 HE21 sing N N 159 
GLN   NE2 HE22 sing N N 160 
GLN   OXT HXT  sing N N 161 
GLU   N   CA   sing N N 162 
GLU   N   H    sing N N 163 
GLU   N   H2   sing N N 164 
GLU   CA  C    sing N N 165 
GLU   CA  CB   sing N N 166 
GLU   CA  HA   sing N N 167 
GLU   C   O    doub N N 168 
GLU   C   OXT  sing N N 169 
GLU   CB  CG   sing N N 170 
GLU   CB  HB2  sing N N 171 
GLU   CB  HB3  sing N N 172 
GLU   CG  CD   sing N N 173 
GLU   CG  HG2  sing N N 174 
GLU   CG  HG3  sing N N 175 
GLU   CD  OE1  doub N N 176 
GLU   CD  OE2  sing N N 177 
GLU   OE2 HE2  sing N N 178 
GLU   OXT HXT  sing N N 179 
GLY   N   CA   sing N N 180 
GLY   N   H    sing N N 181 
GLY   N   H2   sing N N 182 
GLY   CA  C    sing N N 183 
GLY   CA  HA2  sing N N 184 
GLY   CA  HA3  sing N N 185 
GLY   C   O    doub N N 186 
GLY   C   OXT  sing N N 187 
GLY   OXT HXT  sing N N 188 
HIS   N   CA   sing N N 189 
HIS   N   H    sing N N 190 
HIS   N   H2   sing N N 191 
HIS   CA  C    sing N N 192 
HIS   CA  CB   sing N N 193 
HIS   CA  HA   sing N N 194 
HIS   C   O    doub N N 195 
HIS   C   OXT  sing N N 196 
HIS   CB  CG   sing N N 197 
HIS   CB  HB2  sing N N 198 
HIS   CB  HB3  sing N N 199 
HIS   CG  ND1  sing Y N 200 
HIS   CG  CD2  doub Y N 201 
HIS   ND1 CE1  doub Y N 202 
HIS   ND1 HD1  sing N N 203 
HIS   CD2 NE2  sing Y N 204 
HIS   CD2 HD2  sing N N 205 
HIS   CE1 NE2  sing Y N 206 
HIS   CE1 HE1  sing N N 207 
HIS   NE2 HE2  sing N N 208 
HIS   OXT HXT  sing N N 209 
HOH   O   H1   sing N N 210 
HOH   O   H2   sing N N 211 
ILE   N   CA   sing N N 212 
ILE   N   H    sing N N 213 
ILE   N   H2   sing N N 214 
ILE   CA  C    sing N N 215 
ILE   CA  CB   sing N N 216 
ILE   CA  HA   sing N N 217 
ILE   C   O    doub N N 218 
ILE   C   OXT  sing N N 219 
ILE   CB  CG1  sing N N 220 
ILE   CB  CG2  sing N N 221 
ILE   CB  HB   sing N N 222 
ILE   CG1 CD1  sing N N 223 
ILE   CG1 HG12 sing N N 224 
ILE   CG1 HG13 sing N N 225 
ILE   CG2 HG21 sing N N 226 
ILE   CG2 HG22 sing N N 227 
ILE   CG2 HG23 sing N N 228 
ILE   CD1 HD11 sing N N 229 
ILE   CD1 HD12 sing N N 230 
ILE   CD1 HD13 sing N N 231 
ILE   OXT HXT  sing N N 232 
LEU   N   CA   sing N N 233 
LEU   N   H    sing N N 234 
LEU   N   H2   sing N N 235 
LEU   CA  C    sing N N 236 
LEU   CA  CB   sing N N 237 
LEU   CA  HA   sing N N 238 
LEU   C   O    doub N N 239 
LEU   C   OXT  sing N N 240 
LEU   CB  CG   sing N N 241 
LEU   CB  HB2  sing N N 242 
LEU   CB  HB3  sing N N 243 
LEU   CG  CD1  sing N N 244 
LEU   CG  CD2  sing N N 245 
LEU   CG  HG   sing N N 246 
LEU   CD1 HD11 sing N N 247 
LEU   CD1 HD12 sing N N 248 
LEU   CD1 HD13 sing N N 249 
LEU   CD2 HD21 sing N N 250 
LEU   CD2 HD22 sing N N 251 
LEU   CD2 HD23 sing N N 252 
LEU   OXT HXT  sing N N 253 
LYS   N   CA   sing N N 254 
LYS   N   H    sing N N 255 
LYS   N   H2   sing N N 256 
LYS   CA  C    sing N N 257 
LYS   CA  CB   sing N N 258 
LYS   CA  HA   sing N N 259 
LYS   C   O    doub N N 260 
LYS   C   OXT  sing N N 261 
LYS   CB  CG   sing N N 262 
LYS   CB  HB2  sing N N 263 
LYS   CB  HB3  sing N N 264 
LYS   CG  CD   sing N N 265 
LYS   CG  HG2  sing N N 266 
LYS   CG  HG3  sing N N 267 
LYS   CD  CE   sing N N 268 
LYS   CD  HD2  sing N N 269 
LYS   CD  HD3  sing N N 270 
LYS   CE  NZ   sing N N 271 
LYS   CE  HE2  sing N N 272 
LYS   CE  HE3  sing N N 273 
LYS   NZ  HZ1  sing N N 274 
LYS   NZ  HZ2  sing N N 275 
LYS   NZ  HZ3  sing N N 276 
LYS   OXT HXT  sing N N 277 
MET   N   CA   sing N N 278 
MET   N   H    sing N N 279 
MET   N   H2   sing N N 280 
MET   CA  C    sing N N 281 
MET   CA  CB   sing N N 282 
MET   CA  HA   sing N N 283 
MET   C   O    doub N N 284 
MET   C   OXT  sing N N 285 
MET   CB  CG   sing N N 286 
MET   CB  HB2  sing N N 287 
MET   CB  HB3  sing N N 288 
MET   CG  SD   sing N N 289 
MET   CG  HG2  sing N N 290 
MET   CG  HG3  sing N N 291 
MET   SD  CE   sing N N 292 
MET   CE  HE1  sing N N 293 
MET   CE  HE2  sing N N 294 
MET   CE  HE3  sing N N 295 
MET   OXT HXT  sing N N 296 
PHE   N   CA   sing N N 297 
PHE   N   H    sing N N 298 
PHE   N   H2   sing N N 299 
PHE   CA  C    sing N N 300 
PHE   CA  CB   sing N N 301 
PHE   CA  HA   sing N N 302 
PHE   C   O    doub N N 303 
PHE   C   OXT  sing N N 304 
PHE   CB  CG   sing N N 305 
PHE   CB  HB2  sing N N 306 
PHE   CB  HB3  sing N N 307 
PHE   CG  CD1  doub Y N 308 
PHE   CG  CD2  sing Y N 309 
PHE   CD1 CE1  sing Y N 310 
PHE   CD1 HD1  sing N N 311 
PHE   CD2 CE2  doub Y N 312 
PHE   CD2 HD2  sing N N 313 
PHE   CE1 CZ   doub Y N 314 
PHE   CE1 HE1  sing N N 315 
PHE   CE2 CZ   sing Y N 316 
PHE   CE2 HE2  sing N N 317 
PHE   CZ  HZ   sing N N 318 
PHE   OXT HXT  sing N N 319 
PRO   N   CA   sing N N 320 
PRO   N   CD   sing N N 321 
PRO   N   H    sing N N 322 
PRO   CA  C    sing N N 323 
PRO   CA  CB   sing N N 324 
PRO   CA  HA   sing N N 325 
PRO   C   O    doub N N 326 
PRO   C   OXT  sing N N 327 
PRO   CB  CG   sing N N 328 
PRO   CB  HB2  sing N N 329 
PRO   CB  HB3  sing N N 330 
PRO   CG  CD   sing N N 331 
PRO   CG  HG2  sing N N 332 
PRO   CG  HG3  sing N N 333 
PRO   CD  HD2  sing N N 334 
PRO   CD  HD3  sing N N 335 
PRO   OXT HXT  sing N N 336 
SER   N   CA   sing N N 337 
SER   N   H    sing N N 338 
SER   N   H2   sing N N 339 
SER   CA  C    sing N N 340 
SER   CA  CB   sing N N 341 
SER   CA  HA   sing N N 342 
SER   C   O    doub N N 343 
SER   C   OXT  sing N N 344 
SER   CB  OG   sing N N 345 
SER   CB  HB2  sing N N 346 
SER   CB  HB3  sing N N 347 
SER   OG  HG   sing N N 348 
SER   OXT HXT  sing N N 349 
SO4   S   O1   doub N N 350 
SO4   S   O2   doub N N 351 
SO4   S   O3   sing N N 352 
SO4   S   O4   sing N N 353 
THR   N   CA   sing N N 354 
THR   N   H    sing N N 355 
THR   N   H2   sing N N 356 
THR   CA  C    sing N N 357 
THR   CA  CB   sing N N 358 
THR   CA  HA   sing N N 359 
THR   C   O    doub N N 360 
THR   C   OXT  sing N N 361 
THR   CB  OG1  sing N N 362 
THR   CB  CG2  sing N N 363 
THR   CB  HB   sing N N 364 
THR   OG1 HG1  sing N N 365 
THR   CG2 HG21 sing N N 366 
THR   CG2 HG22 sing N N 367 
THR   CG2 HG23 sing N N 368 
THR   OXT HXT  sing N N 369 
TRP   N   CA   sing N N 370 
TRP   N   H    sing N N 371 
TRP   N   H2   sing N N 372 
TRP   CA  C    sing N N 373 
TRP   CA  CB   sing N N 374 
TRP   CA  HA   sing N N 375 
TRP   C   O    doub N N 376 
TRP   C   OXT  sing N N 377 
TRP   CB  CG   sing N N 378 
TRP   CB  HB2  sing N N 379 
TRP   CB  HB3  sing N N 380 
TRP   CG  CD1  doub Y N 381 
TRP   CG  CD2  sing Y N 382 
TRP   CD1 NE1  sing Y N 383 
TRP   CD1 HD1  sing N N 384 
TRP   CD2 CE2  doub Y N 385 
TRP   CD2 CE3  sing Y N 386 
TRP   NE1 CE2  sing Y N 387 
TRP   NE1 HE1  sing N N 388 
TRP   CE2 CZ2  sing Y N 389 
TRP   CE3 CZ3  doub Y N 390 
TRP   CE3 HE3  sing N N 391 
TRP   CZ2 CH2  doub Y N 392 
TRP   CZ2 HZ2  sing N N 393 
TRP   CZ3 CH2  sing Y N 394 
TRP   CZ3 HZ3  sing N N 395 
TRP   CH2 HH2  sing N N 396 
TRP   OXT HXT  sing N N 397 
TYR   N   CA   sing N N 398 
TYR   N   H    sing N N 399 
TYR   N   H2   sing N N 400 
TYR   CA  C    sing N N 401 
TYR   CA  CB   sing N N 402 
TYR   CA  HA   sing N N 403 
TYR   C   O    doub N N 404 
TYR   C   OXT  sing N N 405 
TYR   CB  CG   sing N N 406 
TYR   CB  HB2  sing N N 407 
TYR   CB  HB3  sing N N 408 
TYR   CG  CD1  doub Y N 409 
TYR   CG  CD2  sing Y N 410 
TYR   CD1 CE1  sing Y N 411 
TYR   CD1 HD1  sing N N 412 
TYR   CD2 CE2  doub Y N 413 
TYR   CD2 HD2  sing N N 414 
TYR   CE1 CZ   doub Y N 415 
TYR   CE1 HE1  sing N N 416 
TYR   CE2 CZ   sing Y N 417 
TYR   CE2 HE2  sing N N 418 
TYR   CZ  OH   sing N N 419 
TYR   OH  HH   sing N N 420 
TYR   OXT HXT  sing N N 421 
VAL   N   CA   sing N N 422 
VAL   N   H    sing N N 423 
VAL   N   H2   sing N N 424 
VAL   CA  C    sing N N 425 
VAL   CA  CB   sing N N 426 
VAL   CA  HA   sing N N 427 
VAL   C   O    doub N N 428 
VAL   C   OXT  sing N N 429 
VAL   CB  CG1  sing N N 430 
VAL   CB  CG2  sing N N 431 
VAL   CB  HB   sing N N 432 
VAL   CG1 HG11 sing N N 433 
VAL   CG1 HG12 sing N N 434 
VAL   CG1 HG13 sing N N 435 
VAL   CG2 HG21 sing N N 436 
VAL   CG2 HG22 sing N N 437 
VAL   CG2 HG23 sing N N 438 
VAL   OXT HXT  sing N N 439 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8tzx 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9DJT 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.009115 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006868 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.005206 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C    ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H    ? ? 0.99627  ?       ? ? 14.84254 ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N    ? ? 6.96715  ?       ? ? 11.43723 ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O    ? ? 7.96527  ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S    ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN   ? ? ?        ?       ? ? ?        ?        ? ? ?   ? ? 
ZN2+ ? ? 27.87530 ?       ? ? 3.31736  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . HIS   A 1 4   ? 41.620  28.366  -29.604 1.00 166.57 ? 73   HIS   A N   1 
ATOM   2     C  CA  . HIS   A 1 4   ? 42.745  29.296  -29.694 1.00 169.93 ? 73   HIS   A CA  1 
ATOM   3     C  C   . HIS   A 1 4   ? 42.639  30.406  -28.652 1.00 174.76 ? 73   HIS   A C   1 
ATOM   4     O  O   . HIS   A 1 4   ? 42.159  30.181  -27.537 1.00 178.23 ? 73   HIS   A O   1 
ATOM   5     C  CB  . HIS   A 1 4   ? 42.831  29.922  -31.087 1.00 168.37 ? 73   HIS   A CB  1 
ATOM   6     C  CG  . HIS   A 1 4   ? 43.061  28.933  -32.187 1.00 172.13 ? 73   HIS   A CG  1 
ATOM   7     N  ND1 . HIS   A 1 4   ? 42.026  28.274  -32.819 1.00 176.52 ? 73   HIS   A ND1 1 
ATOM   8     C  CD2 . HIS   A 1 4   ? 44.202  28.497  -32.773 1.00 170.12 ? 73   HIS   A CD2 1 
ATOM   9     C  CE1 . HIS   A 1 4   ? 42.521  27.470  -33.744 1.00 173.33 ? 73   HIS   A CE1 1 
ATOM   10    N  NE2 . HIS   A 1 4   ? 43.838  27.586  -33.735 1.00 174.73 ? 73   HIS   A NE2 1 
ATOM   11    N  N   . ASP   A 1 5   ? 43.095  31.607  -29.028 1.00 175.21 ? 74   ASP   A N   1 
ATOM   12    C  CA  . ASP   A 1 5   ? 43.031  32.800  -28.186 1.00 173.64 ? 74   ASP   A CA  1 
ATOM   13    C  C   . ASP   A 1 5   ? 42.279  33.896  -28.931 1.00 173.05 ? 74   ASP   A C   1 
ATOM   14    O  O   . ASP   A 1 5   ? 42.579  34.172  -30.098 1.00 169.56 ? 74   ASP   A O   1 
ATOM   15    C  CB  . ASP   A 1 5   ? 44.430  33.298  -27.794 1.00 173.57 ? 74   ASP   A CB  1 
ATOM   16    C  CG  . ASP   A 1 5   ? 45.278  32.222  -27.132 1.00 175.67 ? 74   ASP   A CG  1 
ATOM   17    O  OD1 . ASP   A 1 5   ? 44.706  31.203  -26.685 1.00 177.81 ? 74   ASP   A OD1 1 
ATOM   18    O  OD2 . ASP   A 1 5   ? 46.517  32.392  -27.072 1.00 176.24 ? 74   ASP   A OD2 1 
ATOM   19    N  N   . ASP   A 1 6   ? 41.330  34.543  -28.243 1.00 173.27 ? 75   ASP   A N   1 
ATOM   20    C  CA  . ASP   A 1 6   ? 40.344  35.417  -28.879 1.00 172.33 ? 75   ASP   A CA  1 
ATOM   21    C  C   . ASP   A 1 6   ? 40.954  36.396  -29.888 1.00 168.29 ? 75   ASP   A C   1 
ATOM   22    O  O   . ASP   A 1 6   ? 40.313  36.720  -30.896 1.00 163.74 ? 75   ASP   A O   1 
ATOM   23    C  CB  . ASP   A 1 6   ? 39.546  36.179  -27.807 1.00 173.59 ? 75   ASP   A CB  1 
ATOM   24    C  CG  . ASP   A 1 6   ? 38.244  36.781  -28.349 1.00 167.29 ? 75   ASP   A CG  1 
ATOM   25    O  OD1 . ASP   A 1 6   ? 37.530  36.084  -29.109 1.00 163.95 ? 75   ASP   A OD1 1 
ATOM   26    O  OD2 . ASP   A 1 6   ? 37.936  37.948  -28.012 1.00 165.51 ? 75   ASP   A OD2 1 
ATOM   27    N  N   . ASP   A 1 7   ? 42.184  36.859  -29.651 1.00 152.82 ? 76   ASP   A N   1 
ATOM   28    C  CA  . ASP   A 1 7   ? 42.864  37.819  -30.527 1.00 140.13 ? 76   ASP   A CA  1 
ATOM   29    C  C   . ASP   A 1 7   ? 44.309  37.376  -30.782 1.00 135.63 ? 76   ASP   A C   1 
ATOM   30    O  O   . ASP   A 1 7   ? 45.262  38.156  -30.706 1.00 134.01 ? 76   ASP   A O   1 
ATOM   31    C  CB  . ASP   A 1 7   ? 42.794  39.233  -29.936 1.00 143.12 ? 76   ASP   A CB  1 
ATOM   32    C  CG  . ASP   A 1 7   ? 41.619  40.063  -30.494 1.00 139.88 ? 76   ASP   A CG  1 
ATOM   33    O  OD1 . ASP   A 1 7   ? 41.355  39.981  -31.713 1.00 136.21 ? 76   ASP   A OD1 1 
ATOM   34    O  OD2 . ASP   A 1 7   ? 40.970  40.808  -29.722 1.00 132.72 ? 76   ASP   A OD2 1 
ATOM   35    N  N   . SER   A 1 8   ? 44.476  36.096  -31.099 1.00 137.14 ? 77   SER   A N   1 
ATOM   36    C  CA  . SER   A 1 8   ? 45.772  35.515  -31.404 1.00 132.97 ? 77   SER   A CA  1 
ATOM   37    C  C   . SER   A 1 8   ? 46.168  35.844  -32.846 1.00 126.14 ? 77   SER   A C   1 
ATOM   38    O  O   . SER   A 1 8   ? 45.326  36.185  -33.681 1.00 121.16 ? 77   SER   A O   1 
ATOM   39    C  CB  . SER   A 1 8   ? 45.714  33.996  -31.174 1.00 138.36 ? 77   SER   A CB  1 
ATOM   40    O  OG  . SER   A 1 8   ? 46.935  33.341  -31.471 1.00 135.28 ? 77   SER   A OG  1 
ATOM   41    N  N   . CYS   A 1 9   ? 47.472  35.769  -33.131 1.00 127.46 ? 78   CYS   A N   1 
ATOM   42    C  CA  . CYS   A 1 9   ? 47.975  35.785  -34.508 1.00 125.05 ? 78   CYS   A CA  1 
ATOM   43    C  C   . CYS   A 1 9   ? 48.513  34.390  -34.810 1.00 127.25 ? 78   CYS   A C   1 
ATOM   44    O  O   . CYS   A 1 9   ? 49.660  34.080  -34.475 1.00 130.83 ? 78   CYS   A O   1 
ATOM   45    C  CB  . CYS   A 1 9   ? 49.075  36.824  -34.723 1.00 125.40 ? 78   CYS   A CB  1 
ATOM   46    S  SG  . CYS   A 1 9   ? 48.818  38.470  -34.026 1.00 143.43 ? 78   CYS   A SG  1 
ATOM   47    N  N   . GLN   A 1 10  ? 47.703  33.552  -35.454 1.00 117.13 ? 79   GLN   A N   1 
ATOM   48    C  CA  . GLN   A 1 10  ? 48.090  32.178  -35.732 1.00 116.53 ? 79   GLN   A CA  1 
ATOM   49    C  C   . GLN   A 1 10  ? 48.257  31.951  -37.229 1.00 110.57 ? 79   GLN   A C   1 
ATOM   50    O  O   . GLN   A 1 10  ? 47.725  32.692  -38.060 1.00 105.46 ? 79   GLN   A O   1 
ATOM   51    C  CB  . GLN   A 1 10  ? 47.053  31.196  -35.181 1.00 121.01 ? 79   GLN   A CB  1 
ATOM   52    C  CG  . GLN   A 1 10  ? 46.957  31.155  -33.666 1.00 129.61 ? 79   GLN   A CG  1 
ATOM   53    C  CD  . GLN   A 1 10  ? 48.010  30.251  -33.050 1.00 135.94 ? 79   GLN   A CD  1 
ATOM   54    O  OE1 . GLN   A 1 10  ? 48.874  29.712  -33.753 1.00 134.37 ? 79   GLN   A OE1 1 
ATOM   55    N  NE2 . GLN   A 1 10  ? 47.941  30.073  -31.732 1.00 137.06 ? 79   GLN   A NE2 1 
ATOM   56    N  N   . VAL   A 1 11  ? 48.981  30.891  -37.575 1.00 112.43 ? 80   VAL   A N   1 
ATOM   57    C  CA  . VAL   A 1 11  ? 49.129  30.478  -38.969 1.00 113.85 ? 80   VAL   A CA  1 
ATOM   58    C  C   . VAL   A 1 11  ? 48.362  29.174  -39.188 1.00 110.97 ? 80   VAL   A C   1 
ATOM   59    O  O   . VAL   A 1 11  ? 48.362  28.287  -38.329 1.00 110.59 ? 80   VAL   A O   1 
ATOM   60    C  CB  . VAL   A 1 11  ? 50.613  30.350  -39.382 1.00 112.92 ? 80   VAL   A CB  1 
ATOM   61    C  CG1 . VAL   A 1 11  ? 51.400  29.510  -38.374 1.00 113.11 ? 80   VAL   A CG1 1 
ATOM   62    C  CG2 . VAL   A 1 11  ? 50.720  29.797  -40.811 1.00 115.05 ? 80   VAL   A CG2 1 
ATOM   63    N  N   . ILE   A 1 12  ? 47.700  29.072  -40.338 1.00 109.55 ? 81   ILE   A N   1 
ATOM   64    C  CA  . ILE   A 1 12  ? 46.736  28.016  -40.616 1.00 104.04 ? 81   ILE   A CA  1 
ATOM   65    C  C   . ILE   A 1 12  ? 46.702  27.761  -42.116 1.00 113.31 ? 81   ILE   A C   1 
ATOM   66    O  O   . ILE   A 1 12  ? 46.631  28.716  -42.907 1.00 113.74 ? 81   ILE   A O   1 
ATOM   67    C  CB  . ILE   A 1 12  ? 45.340  28.397  -40.120 1.00 99.98  ? 81   ILE   A CB  1 
ATOM   68    C  CG1 . ILE   A 1 12  ? 45.350  28.577  -38.608 1.00 100.48 ? 81   ILE   A CG1 1 
ATOM   69    C  CG2 . ILE   A 1 12  ? 44.314  27.361  -40.561 1.00 105.45 ? 81   ILE   A CG2 1 
ATOM   70    C  CD1 . ILE   A 1 12  ? 44.183  29.333  -38.125 1.00 97.44  ? 81   ILE   A CD1 1 
ATOM   71    N  N   . PRO   A 1 13  ? 46.727  26.506  -42.556 1.00 113.04 ? 82   PRO   A N   1 
ATOM   72    C  CA  . PRO   A 1 13  ? 46.675  26.238  -43.997 1.00 113.71 ? 82   PRO   A CA  1 
ATOM   73    C  C   . PRO   A 1 13  ? 45.282  26.439  -44.579 1.00 110.95 ? 82   PRO   A C   1 
ATOM   74    O  O   . PRO   A 1 13  ? 44.261  26.343  -43.900 1.00 108.58 ? 82   PRO   A O   1 
ATOM   75    C  CB  . PRO   A 1 13  ? 47.118  24.778  -44.097 1.00 114.73 ? 82   PRO   A CB  1 
ATOM   76    C  CG  . PRO   A 1 13  ? 46.769  24.199  -42.763 1.00 113.47 ? 82   PRO   A CG  1 
ATOM   77    C  CD  . PRO   A 1 13  ? 46.952  25.283  -41.762 1.00 107.39 ? 82   PRO   A CD  1 
ATOM   78    N  N   . VAL   A 1 14  ? 45.264  26.725  -45.869 1.00 117.71 ? 83   VAL   A N   1 
ATOM   79    C  CA  . VAL   A 1 14  ? 44.056  27.100  -46.586 1.00 122.65 ? 83   VAL   A CA  1 
ATOM   80    C  C   . VAL   A 1 14  ? 43.700  25.988  -47.558 1.00 129.69 ? 83   VAL   A C   1 
ATOM   81    O  O   . VAL   A 1 14  ? 44.447  25.730  -48.512 1.00 137.68 ? 83   VAL   A O   1 
ATOM   82    C  CB  . VAL   A 1 14  ? 44.238  28.412  -47.354 1.00 117.08 ? 83   VAL   A CB  1 
ATOM   83    C  CG1 . VAL   A 1 14  ? 42.948  28.782  -48.067 1.00 118.72 ? 83   VAL   A CG1 1 
ATOM   84    C  CG2 . VAL   A 1 14  ? 44.676  29.502  -46.423 1.00 115.76 ? 83   VAL   A CG2 1 
ATOM   85    N  N   . LEU   A 1 15  ? 42.551  25.365  -47.360 1.00 124.91 ? 84   LEU   A N   1 
ATOM   86    C  CA  . LEU   A 1 15  ? 42.065  24.488  -48.410 1.00 138.16 ? 84   LEU   A CA  1 
ATOM   87    C  C   . LEU   A 1 15  ? 42.014  25.274  -49.717 1.00 148.03 ? 84   LEU   A C   1 
ATOM   88    O  O   . LEU   A 1 15  ? 41.332  26.308  -49.782 1.00 147.87 ? 84   LEU   A O   1 
ATOM   89    C  CB  . LEU   A 1 15  ? 40.695  23.925  -48.068 1.00 133.29 ? 84   LEU   A CB  1 
ATOM   90    C  CG  . LEU   A 1 15  ? 40.896  22.482  -47.635 1.00 124.32 ? 84   LEU   A CG  1 
ATOM   91    C  CD1 . LEU   A 1 15  ? 41.548  21.618  -48.730 1.00 135.34 ? 84   LEU   A CD1 1 
ATOM   92    C  CD2 . LEU   A 1 15  ? 41.755  22.480  -46.383 1.00 124.45 ? 84   LEU   A CD2 1 
ATOM   93    N  N   . PRO   A 1 16  ? 42.741  24.849  -50.751 1.00 171.05 ? 85   PRO   A N   1 
ATOM   94    C  CA  . PRO   A 1 16  ? 42.965  25.722  -51.919 1.00 173.28 ? 85   PRO   A CA  1 
ATOM   95    C  C   . PRO   A 1 16  ? 41.682  26.124  -52.621 1.00 173.05 ? 85   PRO   A C   1 
ATOM   96    O  O   . PRO   A 1 16  ? 41.179  27.235  -52.426 1.00 173.22 ? 85   PRO   A O   1 
ATOM   97    C  CB  . PRO   A 1 16  ? 43.852  24.868  -52.839 1.00 175.60 ? 85   PRO   A CB  1 
ATOM   98    C  CG  . PRO   A 1 16  ? 43.641  23.468  -52.392 1.00 174.88 ? 85   PRO   A CG  1 
ATOM   99    C  CD  . PRO   A 1 16  ? 43.428  23.556  -50.901 1.00 171.54 ? 85   PRO   A CD  1 
ATOM   100   N  N   . GLN   A 1 17  ? 41.148  25.228  -53.447 1.00 156.48 ? 86   GLN   A N   1 
ATOM   101   C  CA  . GLN   A 1 17  ? 40.038  25.612  -54.291 1.00 149.95 ? 86   GLN   A CA  1 
ATOM   102   C  C   . GLN   A 1 17  ? 38.781  25.932  -53.486 1.00 150.12 ? 86   GLN   A C   1 
ATOM   103   O  O   . GLN   A 1 17  ? 37.886  26.601  -54.010 1.00 148.19 ? 86   GLN   A O   1 
ATOM   104   C  CB  . GLN   A 1 17  ? 39.754  24.517  -55.319 1.00 144.48 ? 86   GLN   A CB  1 
ATOM   105   N  N   . VAL   A 1 18  ? 38.692  25.494  -52.228 1.00 149.27 ? 87   VAL   A N   1 
ATOM   106   C  CA  . VAL   A 1 18  ? 37.492  25.773  -51.451 1.00 145.20 ? 87   VAL   A CA  1 
ATOM   107   C  C   . VAL   A 1 18  ? 37.277  27.281  -51.354 1.00 149.42 ? 87   VAL   A C   1 
ATOM   108   O  O   . VAL   A 1 18  ? 38.224  28.065  -51.190 1.00 148.23 ? 87   VAL   A O   1 
ATOM   109   C  CB  . VAL   A 1 18  ? 37.578  25.134  -50.057 1.00 137.58 ? 87   VAL   A CB  1 
ATOM   110   C  CG1 . VAL   A 1 18  ? 38.048  23.718  -50.186 1.00 137.73 ? 87   VAL   A CG1 1 
ATOM   111   C  CG2 . VAL   A 1 18  ? 38.502  25.925  -49.177 1.00 140.13 ? 87   VAL   A CG2 1 
ATOM   112   N  N   . MET   A 1 19  ? 36.014  27.692  -51.463 1.00 146.65 ? 88   MET   A N   1 
ATOM   113   C  CA  . MET   A 1 19  ? 35.627  29.103  -51.477 1.00 142.36 ? 88   MET   A CA  1 
ATOM   114   C  C   . MET   A 1 19  ? 34.251  29.179  -50.844 1.00 141.79 ? 88   MET   A C   1 
ATOM   115   O  O   . MET   A 1 19  ? 33.337  28.474  -51.289 1.00 145.90 ? 88   MET   A O   1 
ATOM   116   C  CB  . MET   A 1 19  ? 35.603  29.663  -52.905 1.00 145.67 ? 88   MET   A CB  1 
ATOM   117   C  CG  . MET   A 1 19  ? 34.491  29.035  -53.773 1.00 152.21 ? 88   MET   A CG  1 
ATOM   118   S  SD  . MET   A 1 19  ? 34.210  29.601  -55.468 1.00 165.41 ? 88   MET   A SD  1 
ATOM   119   C  CE  . MET   A 1 19  ? 32.415  29.763  -55.503 1.00 153.44 ? 88   MET   A CE  1 
ATOM   120   N  N   . MET   A 1 20  ? 34.089  30.008  -49.821 1.00 134.47 ? 89   MET   A N   1 
ATOM   121   C  CA  . MET   A 1 20  ? 32.819  29.904  -49.119 1.00 128.14 ? 89   MET   A CA  1 
ATOM   122   C  C   . MET   A 1 20  ? 32.811  30.937  -48.005 1.00 124.34 ? 89   MET   A C   1 
ATOM   123   O  O   . MET   A 1 20  ? 33.855  31.465  -47.626 1.00 124.09 ? 89   MET   A O   1 
ATOM   124   C  CB  . MET   A 1 20  ? 32.615  28.486  -48.553 1.00 127.15 ? 89   MET   A CB  1 
ATOM   125   C  CG  . MET   A 1 20  ? 31.374  28.285  -47.704 1.00 127.68 ? 89   MET   A CG  1 
ATOM   126   S  SD  . MET   A 1 20  ? 31.371  26.700  -46.817 1.00 139.77 ? 89   MET   A SD  1 
ATOM   127   C  CE  . MET   A 1 20  ? 29.695  26.657  -46.136 1.00 127.04 ? 89   MET   A CE  1 
ATOM   128   N  N   . ILE   A 1 21  ? 31.609  31.240  -47.511 1.00 115.79 ? 90   ILE   A N   1 
ATOM   129   C  CA  . ILE   A 1 21  ? 31.414  31.886  -46.219 1.00 107.11 ? 90   ILE   A CA  1 
ATOM   130   C  C   . ILE   A 1 21  ? 30.958  30.788  -45.266 1.00 106.57 ? 90   ILE   A C   1 
ATOM   131   O  O   . ILE   A 1 21  ? 29.896  30.184  -45.472 1.00 106.47 ? 90   ILE   A O   1 
ATOM   132   C  CB  . ILE   A 1 21  ? 30.400  33.040  -46.269 1.00 104.81 ? 90   ILE   A CB  1 
ATOM   133   C  CG1 . ILE   A 1 21  ? 31.034  34.277  -46.868 1.00 104.24 ? 90   ILE   A CG1 1 
ATOM   134   C  CG2 . ILE   A 1 21  ? 29.987  33.444  -44.864 1.00 98.34  ? 90   ILE   A CG2 1 
ATOM   135   C  CD1 . ILE   A 1 21  ? 31.809  34.010  -48.084 1.00 113.45 ? 90   ILE   A CD1 1 
ATOM   136   N  N   . LEU   A 1 22  ? 31.764  30.515  -44.247 1.00 103.30 ? 91   LEU   A N   1 
ATOM   137   C  CA  . LEU   A 1 22  ? 31.511  29.435  -43.301 1.00 93.79  ? 91   LEU   A CA  1 
ATOM   138   C  C   . LEU   A 1 22  ? 31.119  30.047  -41.957 1.00 93.58  ? 91   LEU   A C   1 
ATOM   139   O  O   . LEU   A 1 22  ? 31.926  30.735  -41.318 1.00 89.64  ? 91   LEU   A O   1 
ATOM   140   C  CB  . LEU   A 1 22  ? 32.749  28.564  -43.150 1.00 94.04  ? 91   LEU   A CB  1 
ATOM   141   C  CG  . LEU   A 1 22  ? 32.687  27.445  -42.112 1.00 89.47  ? 91   LEU   A CG  1 
ATOM   142   C  CD1 . LEU   A 1 22  ? 31.657  26.402  -42.499 1.00 92.26  ? 91   LEU   A CD1 1 
ATOM   143   C  CD2 . LEU   A 1 22  ? 34.062  26.821  -41.920 1.00 87.99  ? 91   LEU   A CD2 1 
ATOM   144   N  N   . ILE   A 1 23  ? 29.881  29.827  -41.527 1.00 93.64  ? 92   ILE   A N   1 
ATOM   145   C  CA  . ILE   A 1 23  ? 29.444  30.380  -40.242 1.00 91.71  ? 92   ILE   A CA  1 
ATOM   146   C  C   . ILE   A 1 23  ? 29.850  29.414  -39.139 1.00 92.00  ? 92   ILE   A C   1 
ATOM   147   O  O   . ILE   A 1 23  ? 29.580  28.224  -39.262 1.00 89.91  ? 92   ILE   A O   1 
ATOM   148   C  CB  . ILE   A 1 23  ? 27.931  30.674  -40.188 1.00 85.08  ? 92   ILE   A CB  1 
ATOM   149   C  CG1 . ILE   A 1 23  ? 27.471  31.474  -41.384 1.00 84.73  ? 92   ILE   A CG1 1 
ATOM   150   C  CG2 . ILE   A 1 23  ? 27.629  31.422  -38.932 1.00 78.01  ? 92   ILE   A CG2 1 
ATOM   151   C  CD1 . ILE   A 1 23  ? 27.244  30.668  -42.605 1.00 91.20  ? 92   ILE   A CD1 1 
ATOM   152   N  N   . PRO   A 1 24  ? 30.486  29.870  -38.072 1.00 90.86  ? 93   PRO   A N   1 
ATOM   153   C  CA  . PRO   A 1 24  ? 30.828  28.960  -36.964 1.00 89.03  ? 93   PRO   A CA  1 
ATOM   154   C  C   . PRO   A 1 24  ? 29.697  27.998  -36.594 1.00 86.81  ? 93   PRO   A C   1 
ATOM   155   O  O   . PRO   A 1 24  ? 28.583  28.424  -36.286 1.00 90.03  ? 93   PRO   A O   1 
ATOM   156   C  CB  . PRO   A 1 24  ? 31.159  29.940  -35.812 1.00 85.48  ? 93   PRO   A CB  1 
ATOM   157   C  CG  . PRO   A 1 24  ? 31.726  31.129  -36.511 1.00 80.40  ? 93   PRO   A CG  1 
ATOM   158   C  CD  . PRO   A 1 24  ? 30.972  31.258  -37.826 1.00 84.34  ? 93   PRO   A CD  1 
ATOM   159   N  N   . GLY   A 1 25  ? 29.952  26.694  -36.624 1.00 85.85  ? 94   GLY   A N   1 
ATOM   160   C  CA  . GLY   A 1 25  ? 28.923  25.729  -36.318 1.00 87.00  ? 94   GLY   A CA  1 
ATOM   161   C  C   . GLY   A 1 25  ? 28.234  25.158  -37.526 1.00 91.67  ? 94   GLY   A C   1 
ATOM   162   O  O   . GLY   A 1 25  ? 27.246  24.445  -37.379 1.00 94.45  ? 94   GLY   A O   1 
ATOM   163   N  N   . GLN   A 1 26  ? 28.730  25.480  -38.715 1.00 92.74  ? 95   GLN   A N   1 
ATOM   164   C  CA  . GLN   A 1 26  ? 28.342  24.872  -39.975 1.00 91.22  ? 95   GLN   A CA  1 
ATOM   165   C  C   . GLN   A 1 26  ? 29.344  23.766  -40.309 1.00 93.06  ? 95   GLN   A C   1 
ATOM   166   O  O   . GLN   A 1 26  ? 30.522  23.843  -39.931 1.00 93.06  ? 95   GLN   A O   1 
ATOM   167   C  CB  . GLN   A 1 26  ? 28.317  25.927  -41.092 1.00 93.47  ? 95   GLN   A CB  1 
ATOM   168   C  CG  . GLN   A 1 26  ? 26.964  26.621  -41.413 1.00 94.09  ? 95   GLN   A CG  1 
ATOM   169   C  CD  . GLN   A 1 26  ? 26.994  27.349  -42.783 1.00 98.98  ? 95   GLN   A CD  1 
ATOM   170   O  OE1 . GLN   A 1 26  ? 28.044  27.840  -43.214 1.00 99.23  ? 95   GLN   A OE1 1 
ATOM   171   N  NE2 . GLN   A 1 26  ? 25.848  27.394  -43.471 1.00 98.09  ? 95   GLN   A NE2 1 
ATOM   172   N  N   . THR   A 1 27  ? 28.884  22.737  -41.014 1.00 90.58  ? 96   THR   A N   1 
ATOM   173   C  CA  . THR   A 1 27  ? 29.749  21.623  -41.383 1.00 92.72  ? 96   THR   A CA  1 
ATOM   174   C  C   . THR   A 1 27  ? 29.944  21.680  -42.902 1.00 94.89  ? 96   THR   A C   1 
ATOM   175   O  O   . THR   A 1 27  ? 28.995  21.928  -43.655 1.00 95.93  ? 96   THR   A O   1 
ATOM   176   C  CB  . THR   A 1 27  ? 29.171  20.264  -40.893 1.00 88.33  ? 96   THR   A CB  1 
ATOM   177   O  OG1 . THR   A 1 27  ? 28.246  19.712  -41.833 1.00 96.30  ? 96   THR   A OG1 1 
ATOM   178   C  CG2 . THR   A 1 27  ? 28.419  20.425  -39.577 1.00 86.90  ? 96   THR   A CG2 1 
ATOM   179   N  N   . LEU   A 1 28  ? 31.192  21.556  -43.351 1.00 89.61  ? 97   LEU   A N   1 
ATOM   180   C  CA  . LEU   A 1 28  ? 31.469  21.529  -44.783 1.00 95.35  ? 97   LEU   A CA  1 
ATOM   181   C  C   . LEU   A 1 28  ? 32.023  20.166  -45.170 1.00 105.91 ? 97   LEU   A C   1 
ATOM   182   O  O   . LEU   A 1 28  ? 33.049  19.731  -44.610 1.00 103.00 ? 97   LEU   A O   1 
ATOM   183   C  CB  . LEU   A 1 28  ? 32.433  22.646  -45.213 1.00 101.06 ? 97   LEU   A CB  1 
ATOM   184   C  CG  . LEU   A 1 28  ? 33.935  22.492  -44.992 1.00 100.52 ? 97   LEU   A CG  1 
ATOM   185   C  CD1 . LEU   A 1 28  ? 34.762  23.348  -45.970 1.00 94.35  ? 97   LEU   A CD1 1 
ATOM   186   C  CD2 . LEU   A 1 28  ? 34.274  22.829  -43.545 1.00 100.77 ? 97   LEU   A CD2 1 
ATOM   187   N  N   . PRO   A 1 29  ? 31.368  19.463  -46.099 1.00 107.63 ? 98   PRO   A N   1 
ATOM   188   C  CA  . PRO   A 1 29  ? 31.865  18.156  -46.554 1.00 100.63 ? 98   PRO   A CA  1 
ATOM   189   C  C   . PRO   A 1 29  ? 32.874  18.343  -47.673 1.00 101.89 ? 98   PRO   A C   1 
ATOM   190   O  O   . PRO   A 1 29  ? 32.591  19.016  -48.666 1.00 109.02 ? 98   PRO   A O   1 
ATOM   191   C  CB  . PRO   A 1 29  ? 30.604  17.448  -47.059 1.00 108.47 ? 98   PRO   A CB  1 
ATOM   192   C  CG  . PRO   A 1 29  ? 29.422  18.390  -46.691 1.00 111.05 ? 98   PRO   A CG  1 
ATOM   193   C  CD  . PRO   A 1 29  ? 30.018  19.755  -46.610 1.00 105.86 ? 98   PRO   A CD  1 
ATOM   194   N  N   . LEU   A 1 30  ? 34.059  17.748  -47.512 1.00 104.00 ? 99   LEU   A N   1 
ATOM   195   C  CA  . LEU   A 1 30  ? 35.142  17.914  -48.471 1.00 110.59 ? 99   LEU   A CA  1 
ATOM   196   C  C   . LEU   A 1 30  ? 35.696  16.569  -48.924 1.00 113.91 ? 99   LEU   A C   1 
ATOM   197   O  O   . LEU   A 1 30  ? 35.845  15.645  -48.121 1.00 114.68 ? 99   LEU   A O   1 
ATOM   198   C  CB  . LEU   A 1 30  ? 36.276  18.769  -47.886 1.00 111.87 ? 99   LEU   A CB  1 
ATOM   199   C  CG  . LEU   A 1 30  ? 35.924  20.263  -47.784 1.00 113.16 ? 99   LEU   A CG  1 
ATOM   200   C  CD1 . LEU   A 1 30  ? 37.111  21.143  -47.354 1.00 115.27 ? 99   LEU   A CD1 1 
ATOM   201   C  CD2 . LEU   A 1 30  ? 35.325  20.762  -49.093 1.00 110.64 ? 99   LEU   A CD2 1 
ATOM   202   N  N   . GLN   A 1 31  ? 35.995  16.477  -50.228 1.00 118.71 ? 100  GLN   A N   1 
ATOM   203   C  CA  . GLN   A 1 31  ? 36.628  15.317  -50.854 1.00 115.87 ? 100  GLN   A CA  1 
ATOM   204   C  C   . GLN   A 1 31  ? 37.917  15.808  -51.510 1.00 116.56 ? 100  GLN   A C   1 
ATOM   205   O  O   . GLN   A 1 31  ? 37.871  16.594  -52.467 1.00 120.48 ? 100  GLN   A O   1 
ATOM   206   C  CB  . GLN   A 1 31  ? 35.696  14.655  -51.870 1.00 109.09 ? 100  GLN   A CB  1 
ATOM   207   N  N   . LEU   A 1 32  ? 39.056  15.356  -50.984 1.00 118.10 ? 101  LEU   A N   1 
ATOM   208   C  CA  . LEU   A 1 32  ? 40.380  15.822  -51.388 1.00 122.89 ? 101  LEU   A CA  1 
ATOM   209   C  C   . LEU   A 1 32  ? 41.036  14.776  -52.280 1.00 131.65 ? 101  LEU   A C   1 
ATOM   210   O  O   . LEU   A 1 32  ? 41.444  13.714  -51.797 1.00 130.67 ? 101  LEU   A O   1 
ATOM   211   C  CB  . LEU   A 1 32  ? 41.260  16.090  -50.173 1.00 124.98 ? 101  LEU   A CB  1 
ATOM   212   C  CG  . LEU   A 1 32  ? 41.113  17.388  -49.373 1.00 128.55 ? 101  LEU   A CG  1 
ATOM   213   C  CD1 . LEU   A 1 32  ? 41.919  18.540  -49.973 1.00 132.19 ? 101  LEU   A CD1 1 
ATOM   214   C  CD2 . LEU   A 1 32  ? 39.658  17.775  -49.262 1.00 125.73 ? 101  LEU   A CD2 1 
ATOM   215   N  N   . PHE   A 1 33  ? 41.169  15.081  -53.573 1.00 134.93 ? 102  PHE   A N   1 
ATOM   216   C  CA  . PHE   A 1 33  ? 41.842  14.151  -54.467 1.00 140.21 ? 102  PHE   A CA  1 
ATOM   217   C  C   . PHE   A 1 33  ? 43.154  14.676  -55.026 1.00 143.75 ? 102  PHE   A C   1 
ATOM   218   O  O   . PHE   A 1 33  ? 44.056  13.866  -55.260 1.00 145.82 ? 102  PHE   A O   1 
ATOM   219   C  CB  . PHE   A 1 33  ? 40.916  13.692  -55.615 1.00 137.83 ? 102  PHE   A CB  1 
ATOM   220   C  CG  . PHE   A 1 33  ? 40.667  14.713  -56.710 1.00 140.00 ? 102  PHE   A CG  1 
ATOM   221   C  CD1 . PHE   A 1 33  ? 41.682  15.138  -57.551 1.00 147.11 ? 102  PHE   A CD1 1 
ATOM   222   C  CD2 . PHE   A 1 33  ? 39.372  15.173  -56.952 1.00 143.42 ? 102  PHE   A CD2 1 
ATOM   223   C  CE1 . PHE   A 1 33  ? 41.438  16.040  -58.579 1.00 149.10 ? 102  PHE   A CE1 1 
ATOM   224   C  CE2 . PHE   A 1 33  ? 39.114  16.098  -57.977 1.00 149.16 ? 102  PHE   A CE2 1 
ATOM   225   C  CZ  . PHE   A 1 33  ? 40.150  16.520  -58.800 1.00 147.67 ? 102  PHE   A CZ  1 
ATOM   226   N  N   . HIS   A 1 34  ? 43.333  15.989  -55.251 1.00 146.32 ? 103  HIS   A N   1 
ATOM   227   C  CA  . HIS   A 1 34  ? 44.597  16.397  -55.836 1.00 150.60 ? 103  HIS   A CA  1 
ATOM   228   C  C   . HIS   A 1 34  ? 45.695  16.051  -54.829 1.00 151.78 ? 103  HIS   A C   1 
ATOM   229   O  O   . HIS   A 1 34  ? 45.525  16.286  -53.626 1.00 151.11 ? 103  HIS   A O   1 
ATOM   230   C  CB  . HIS   A 1 34  ? 44.673  17.894  -56.210 1.00 152.18 ? 103  HIS   A CB  1 
ATOM   231   C  CG  . HIS   A 1 34  ? 43.581  18.407  -57.119 1.00 148.94 ? 103  HIS   A CG  1 
ATOM   232   N  ND1 . HIS   A 1 34  ? 42.438  19.012  -56.636 1.00 151.97 ? 103  HIS   A ND1 1 
ATOM   233   C  CD2 . HIS   A 1 34  ? 43.501  18.489  -58.473 1.00 147.36 ? 103  HIS   A CD2 1 
ATOM   234   C  CE1 . HIS   A 1 34  ? 41.696  19.425  -57.647 1.00 149.23 ? 103  HIS   A CE1 1 
ATOM   235   N  NE2 . HIS   A 1 34  ? 42.308  19.106  -58.773 1.00 151.20 ? 103  HIS   A NE2 1 
ATOM   236   N  N   . PRO   A 1 35  ? 46.821  15.481  -55.270 1.00 157.92 ? 104  PRO   A N   1 
ATOM   237   C  CA  . PRO   A 1 35  ? 47.801  14.942  -54.293 1.00 158.10 ? 104  PRO   A CA  1 
ATOM   238   C  C   . PRO   A 1 35  ? 48.311  15.983  -53.322 1.00 156.16 ? 104  PRO   A C   1 
ATOM   239   O  O   . PRO   A 1 35  ? 48.409  15.709  -52.117 1.00 154.50 ? 104  PRO   A O   1 
ATOM   240   C  CB  . PRO   A 1 35  ? 48.922  14.387  -55.190 1.00 159.83 ? 104  PRO   A CB  1 
ATOM   241   C  CG  . PRO   A 1 35  ? 48.237  14.119  -56.501 1.00 161.11 ? 104  PRO   A CG  1 
ATOM   242   C  CD  . PRO   A 1 35  ? 47.197  15.183  -56.664 1.00 158.55 ? 104  PRO   A CD  1 
ATOM   243   N  N   . GLN   A 1 36  ? 48.619  17.186  -53.815 1.00 159.05 ? 105  GLN   A N   1 
ATOM   244   C  CA  . GLN   A 1 36  ? 49.049  18.260  -52.932 1.00 158.42 ? 105  GLN   A CA  1 
ATOM   245   C  C   . GLN   A 1 36  ? 48.084  18.411  -51.764 1.00 157.93 ? 105  GLN   A C   1 
ATOM   246   O  O   . GLN   A 1 36  ? 48.497  18.455  -50.600 1.00 157.12 ? 105  GLN   A O   1 
ATOM   247   C  CB  . GLN   A 1 36  ? 49.168  19.570  -53.712 1.00 160.11 ? 105  GLN   A CB  1 
ATOM   248   N  N   . GLU   A 1 37  ? 46.788  18.447  -52.058 1.00 149.80 ? 106  GLU   A N   1 
ATOM   249   C  CA  . GLU   A 1 37  ? 45.806  18.626  -51.003 1.00 146.66 ? 106  GLU   A CA  1 
ATOM   250   C  C   . GLU   A 1 37  ? 45.850  17.478  -49.991 1.00 143.41 ? 106  GLU   A C   1 
ATOM   251   O  O   . GLU   A 1 37  ? 45.970  17.715  -48.787 1.00 143.18 ? 106  GLU   A O   1 
ATOM   252   C  CB  . GLU   A 1 37  ? 44.416  18.758  -51.605 1.00 146.24 ? 106  GLU   A CB  1 
ATOM   253   C  CG  . GLU   A 1 37  ? 44.131  19.991  -52.394 1.00 150.32 ? 106  GLU   A CG  1 
ATOM   254   C  CD  . GLU   A 1 37  ? 43.089  19.705  -53.432 1.00 153.08 ? 106  GLU   A CD  1 
ATOM   255   O  OE1 . GLU   A 1 37  ? 42.935  18.464  -53.688 1.00 151.58 ? 106  GLU   A OE1 1 
ATOM   256   O  OE2 . GLU   A 1 37  ? 42.462  20.648  -53.976 1.00 154.46 ? 106  GLU   A OE2 1 
ATOM   257   N  N   . VAL   A 1 38  ? 45.775  16.220  -50.454 1.00 142.98 ? 107  VAL   A N   1 
ATOM   258   C  CA  . VAL   A 1 38  ? 45.679  15.101  -49.510 1.00 140.02 ? 107  VAL   A CA  1 
ATOM   259   C  C   . VAL   A 1 38  ? 46.860  15.110  -48.551 1.00 138.18 ? 107  VAL   A C   1 
ATOM   260   O  O   . VAL   A 1 38  ? 46.734  14.718  -47.381 1.00 133.81 ? 107  VAL   A O   1 
ATOM   261   C  CB  . VAL   A 1 38  ? 45.578  13.756  -50.250 1.00 138.75 ? 107  VAL   A CB  1 
ATOM   262   C  CG1 . VAL   A 1 38  ? 44.627  13.871  -51.424 1.00 138.09 ? 107  VAL   A CG1 1 
ATOM   263   C  CG2 . VAL   A 1 38  ? 46.950  13.316  -50.688 1.00 143.31 ? 107  VAL   A CG2 1 
ATOM   264   N  N   . SER   A 1 39  ? 48.027  15.551  -49.027 1.00 140.42 ? 108  SER   A N   1 
ATOM   265   C  CA  . SER   A 1 39  ? 49.170  15.699  -48.136 1.00 140.43 ? 108  SER   A CA  1 
ATOM   266   C  C   . SER   A 1 39  ? 48.795  16.543  -46.925 1.00 137.19 ? 108  SER   A C   1 
ATOM   267   O  O   . SER   A 1 39  ? 48.852  16.075  -45.785 1.00 135.72 ? 108  SER   A O   1 
ATOM   268   C  CB  . SER   A 1 39  ? 50.343  16.322  -48.890 1.00 141.45 ? 108  SER   A CB  1 
ATOM   269   O  OG  . SER   A 1 39  ? 50.287  15.971  -50.259 1.00 147.69 ? 108  SER   A OG  1 
ATOM   270   N  N   . MET   A 1 40  ? 48.362  17.785  -47.172 1.00 143.46 ? 109  MET   A N   1 
ATOM   271   C  CA  . MET   A 1 40  ? 48.001  18.709  -46.097 1.00 142.72 ? 109  MET   A CA  1 
ATOM   272   C  C   . MET   A 1 40  ? 47.054  18.058  -45.093 1.00 138.39 ? 109  MET   A C   1 
ATOM   273   O  O   . MET   A 1 40  ? 47.301  18.074  -43.877 1.00 134.73 ? 109  MET   A O   1 
ATOM   274   C  CB  . MET   A 1 40  ? 47.347  19.971  -46.676 1.00 141.42 ? 109  MET   A CB  1 
ATOM   275   C  CG  . MET   A 1 40  ? 46.745  20.894  -45.601 1.00 140.28 ? 109  MET   A CG  1 
ATOM   276   S  SD  . MET   A 1 40  ? 45.485  22.080  -46.138 1.00 150.22 ? 109  MET   A SD  1 
ATOM   277   C  CE  . MET   A 1 40  ? 44.607  21.147  -47.391 1.00 144.90 ? 109  MET   A CE  1 
ATOM   278   N  N   . VAL   A 1 41  ? 45.939  17.522  -45.596 1.00 134.74 ? 110  VAL   A N   1 
ATOM   279   C  CA  . VAL   A 1 41  ? 44.932  16.894  -44.756 1.00 126.51 ? 110  VAL   A CA  1 
ATOM   280   C  C   . VAL   A 1 41  ? 45.611  15.939  -43.799 1.00 127.87 ? 110  VAL   A C   1 
ATOM   281   O  O   . VAL   A 1 41  ? 45.311  15.920  -42.598 1.00 125.19 ? 110  VAL   A O   1 
ATOM   282   C  CB  . VAL   A 1 41  ? 43.913  16.154  -45.617 1.00 123.63 ? 110  VAL   A CB  1 
ATOM   283   C  CG1 . VAL   A 1 41  ? 42.675  15.908  -44.818 1.00 120.29 ? 110  VAL   A CG1 1 
ATOM   284   C  CG2 . VAL   A 1 41  ? 43.608  16.941  -46.856 1.00 125.67 ? 110  VAL   A CG2 1 
ATOM   285   N  N   . ARG   A 1 42  ? 46.531  15.134  -44.335 1.00 125.87 ? 111  ARG   A N   1 
ATOM   286   C  CA  . ARG   A 1 42  ? 47.327  14.204  -43.553 1.00 122.95 ? 111  ARG   A CA  1 
ATOM   287   C  C   . ARG   A 1 42  ? 48.019  14.910  -42.391 1.00 124.78 ? 111  ARG   A C   1 
ATOM   288   O  O   . ARG   A 1 42  ? 47.776  14.581  -41.220 1.00 125.39 ? 111  ARG   A O   1 
ATOM   289   C  CB  . ARG   A 1 42  ? 48.354  13.525  -44.450 1.00 121.64 ? 111  ARG   A CB  1 
ATOM   290   N  N   . ASN   A 1 43  ? 48.892  15.872  -42.711 1.00 125.15 ? 112  ASN   A N   1 
ATOM   291   C  CA  . ASN   A 1 43  ? 49.564  16.672  -41.688 1.00 124.88 ? 112  ASN   A CA  1 
ATOM   292   C  C   . ASN   A 1 43  ? 48.564  17.261  -40.705 1.00 119.14 ? 112  ASN   A C   1 
ATOM   293   O  O   . ASN   A 1 43  ? 48.709  17.118  -39.485 1.00 118.95 ? 112  ASN   A O   1 
ATOM   294   C  CB  . ASN   A 1 43  ? 50.365  17.800  -42.343 1.00 130.60 ? 112  ASN   A CB  1 
ATOM   295   C  CG  . ASN   A 1 43  ? 51.254  17.315  -43.481 1.00 137.62 ? 112  ASN   A CG  1 
ATOM   296   O  OD1 . ASN   A 1 43  ? 50.769  16.756  -44.475 1.00 138.07 ? 112  ASN   A OD1 1 
ATOM   297   N  ND2 . ASN   A 1 43  ? 52.557  17.534  -43.348 1.00 139.26 ? 112  ASN   A ND2 1 
ATOM   298   N  N   . LEU   A 1 44  ? 47.559  17.964  -41.230 1.00 118.80 ? 113  LEU   A N   1 
ATOM   299   C  CA  . LEU   A 1 44  ? 46.551  18.592  -40.385 1.00 119.39 ? 113  LEU   A CA  1 
ATOM   300   C  C   . LEU   A 1 44  ? 46.004  17.617  -39.367 1.00 119.95 ? 113  LEU   A C   1 
ATOM   301   O  O   . LEU   A 1 44  ? 45.965  17.893  -38.161 1.00 118.12 ? 113  LEU   A O   1 
ATOM   302   C  CB  . LEU   A 1 44  ? 45.408  19.104  -41.242 1.00 119.83 ? 113  LEU   A CB  1 
ATOM   303   C  CG  . LEU   A 1 44  ? 45.718  20.379  -41.986 1.00 119.68 ? 113  LEU   A CG  1 
ATOM   304   C  CD1 . LEU   A 1 44  ? 44.413  21.027  -42.394 1.00 115.98 ? 113  LEU   A CD1 1 
ATOM   305   C  CD2 . LEU   A 1 44  ? 46.551  21.292  -41.096 1.00 123.14 ? 113  LEU   A CD2 1 
ATOM   306   N  N   . ILE   A 1 45  ? 45.545  16.468  -39.856 1.00 122.29 ? 114  ILE   A N   1 
ATOM   307   C  CA  . ILE   A 1 45  ? 44.827  15.521  -39.023 1.00 119.81 ? 114  ILE   A CA  1 
ATOM   308   C  C   . ILE   A 1 45  ? 45.745  14.924  -37.969 1.00 117.61 ? 114  ILE   A C   1 
ATOM   309   O  O   . ILE   A 1 45  ? 45.293  14.516  -36.889 1.00 110.10 ? 114  ILE   A O   1 
ATOM   310   C  CB  . ILE   A 1 45  ? 44.214  14.452  -39.927 1.00 115.75 ? 114  ILE   A CB  1 
ATOM   311   C  CG1 . ILE   A 1 45  ? 43.011  13.847  -39.219 1.00 117.57 ? 114  ILE   A CG1 1 
ATOM   312   C  CG2 . ILE   A 1 45  ? 45.279  13.463  -40.321 1.00 114.24 ? 114  ILE   A CG2 1 
ATOM   313   C  CD1 . ILE   A 1 45  ? 42.061  14.918  -38.695 1.00 112.61 ? 114  ILE   A CD1 1 
ATOM   314   N  N   . GLN   A 1 46  ? 47.039  14.843  -38.274 1.00 116.73 ? 115  GLN   A N   1 
ATOM   315   C  CA  . GLN   A 1 46  ? 48.035  14.458  -37.289 1.00 115.51 ? 115  GLN   A CA  1 
ATOM   316   C  C   . GLN   A 1 46  ? 48.326  15.559  -36.273 1.00 116.60 ? 115  GLN   A C   1 
ATOM   317   O  O   . GLN   A 1 46  ? 48.834  15.268  -35.183 1.00 111.86 ? 115  GLN   A O   1 
ATOM   318   C  CB  . GLN   A 1 46  ? 49.343  14.097  -37.994 1.00 118.71 ? 115  GLN   A CB  1 
ATOM   319   C  CG  . GLN   A 1 46  ? 49.259  12.878  -38.891 1.00 123.72 ? 115  GLN   A CG  1 
ATOM   320   C  CD  . GLN   A 1 46  ? 50.209  11.779  -38.447 1.00 132.12 ? 115  GLN   A CD  1 
ATOM   321   O  OE1 . GLN   A 1 46  ? 49.939  11.053  -37.480 1.00 124.89 ? 115  GLN   A OE1 1 
ATOM   322   N  NE2 . GLN   A 1 46  ? 51.340  11.661  -39.146 1.00 134.42 ? 115  GLN   A NE2 1 
ATOM   323   N  N   . LYS   A 1 47  ? 48.030  16.816  -36.612 1.00 120.50 ? 116  LYS   A N   1 
ATOM   324   C  CA  . LYS   A 1 47  ? 48.360  17.958  -35.768 1.00 118.51 ? 116  LYS   A CA  1 
ATOM   325   C  C   . LYS   A 1 47  ? 47.321  18.767  -34.992 1.00 118.63 ? 116  LYS   A C   1 
ATOM   326   O  O   . LYS   A 1 47  ? 47.118  18.532  -33.792 1.00 120.00 ? 116  LYS   A O   1 
ATOM   327   C  CB  . LYS   A 1 47  ? 49.183  18.998  -36.533 1.00 115.03 ? 116  LYS   A CB  1 
ATOM   328   C  CG  . LYS   A 1 47  ? 50.222  18.353  -37.434 1.00 113.61 ? 116  LYS   A CG  1 
ATOM   329   C  CD  . LYS   A 1 47  ? 51.504  19.166  -37.476 1.00 114.86 ? 116  LYS   A CD  1 
ATOM   330   C  CE  . LYS   A 1 47  ? 52.564  18.479  -38.331 1.00 119.71 ? 116  LYS   A CE  1 
ATOM   331   N  NZ  . LYS   A 1 47  ? 53.412  17.484  -37.612 1.00 119.53 ? 116  LYS   A NZ  1 
ATOM   332   N  N   . ASP   A 1 48  ? 46.638  19.704  -35.670 1.00 125.48 ? 117  ASP   A N   1 
ATOM   333   C  CA  . ASP   A 1 48  ? 45.660  20.597  -35.039 1.00 124.10 ? 117  ASP   A CA  1 
ATOM   334   C  C   . ASP   A 1 48  ? 44.331  20.246  -35.701 1.00 121.25 ? 117  ASP   A C   1 
ATOM   335   O  O   . ASP   A 1 48  ? 43.280  20.533  -35.109 1.00 118.98 ? 117  ASP   A O   1 
ATOM   336   C  CB  . ASP   A 1 48  ? 45.863  22.117  -35.198 1.00 124.82 ? 117  ASP   A CB  1 
ATOM   337   C  CG  . ASP   A 1 48  ? 45.816  22.581  -36.674 1.00 128.43 ? 117  ASP   A CG  1 
ATOM   338   O  OD1 . ASP   A 1 48  ? 44.699  22.751  -37.232 1.00 130.28 ? 117  ASP   A OD1 1 
ATOM   339   O  OD2 . ASP   A 1 48  ? 46.909  22.769  -37.275 1.00 127.29 ? 117  ASP   A OD2 1 
ATOM   340   N  N   . ARG   A 1 49  ? 44.349  19.686  -36.912 1.00 118.08 ? 118  ARG   A N   1 
ATOM   341   C  CA  . ARG   A 1 49  ? 43.140  19.295  -37.642 1.00 114.53 ? 118  ARG   A CA  1 
ATOM   342   C  C   . ARG   A 1 49  ? 42.266  20.485  -38.013 1.00 110.06 ? 118  ARG   A C   1 
ATOM   343   O  O   . ARG   A 1 49  ? 41.070  20.325  -38.269 1.00 105.12 ? 118  ARG   A O   1 
ATOM   344   C  CB  . ARG   A 1 49  ? 42.306  18.275  -36.855 1.00 113.60 ? 118  ARG   A CB  1 
ATOM   345   C  CG  . ARG   A 1 49  ? 43.068  17.522  -35.796 1.00 113.03 ? 118  ARG   A CG  1 
ATOM   346   C  CD  . ARG   A 1 49  ? 42.251  16.380  -35.249 1.00 111.01 ? 118  ARG   A CD  1 
ATOM   347   N  NE  . ARG   A 1 49  ? 41.030  16.816  -34.587 1.00 103.06 ? 118  ARG   A NE  1 
ATOM   348   C  CZ  . ARG   A 1 49  ? 40.960  17.151  -33.306 1.00 107.16 ? 118  ARG   A CZ  1 
ATOM   349   N  NH1 . ARG   A 1 49  ? 42.051  17.238  -32.551 1.00 111.41 ? 118  ARG   A NH1 1 
ATOM   350   N  NH2 . ARG   A 1 49  ? 39.766  17.400  -32.766 1.00 104.33 ? 118  ARG   A NH2 1 
ATOM   351   N  N   . THR   A 1 50  ? 42.845  21.683  -38.027 1.00 114.88 ? 119  THR   A N   1 
ATOM   352   C  CA  . THR   A 1 50  ? 42.117  22.903  -38.351 1.00 105.05 ? 119  THR   A CA  1 
ATOM   353   C  C   . THR   A 1 50  ? 42.772  23.557  -39.551 1.00 107.65 ? 119  THR   A C   1 
ATOM   354   O  O   . THR   A 1 50  ? 43.973  23.831  -39.525 1.00 111.83 ? 119  THR   A O   1 
ATOM   355   C  CB  . THR   A 1 50  ? 42.099  23.898  -37.194 1.00 102.20 ? 119  THR   A CB  1 
ATOM   356   O  OG1 . THR   A 1 50  ? 41.578  23.296  -36.007 1.00 106.31 ? 119  THR   A OG1 1 
ATOM   357   C  CG2 . THR   A 1 50  ? 41.198  25.040  -37.555 1.00 98.75  ? 119  THR   A CG2 1 
ATOM   358   N  N   . PHE   A 1 51  ? 41.984  23.827  -40.584 1.00 104.91 ? 120  PHE   A N   1 
ATOM   359   C  CA  . PHE   A 1 51  ? 42.420  24.615  -41.729 1.00 101.62 ? 120  PHE   A CA  1 
ATOM   360   C  C   . PHE   A 1 51  ? 41.621  25.917  -41.798 1.00 97.20  ? 120  PHE   A C   1 
ATOM   361   O  O   . PHE   A 1 51  ? 40.760  26.204  -40.953 1.00 94.65  ? 120  PHE   A O   1 
ATOM   362   C  CB  . PHE   A 1 51  ? 42.305  23.806  -43.034 1.00 105.21 ? 120  PHE   A CB  1 
ATOM   363   C  CG  . PHE   A 1 51  ? 40.914  23.326  -43.336 1.00 101.72 ? 120  PHE   A CG  1 
ATOM   364   C  CD1 . PHE   A 1 51  ? 40.404  22.194  -42.709 1.00 95.34  ? 120  PHE   A CD1 1 
ATOM   365   C  CD2 . PHE   A 1 51  ? 40.116  24.010  -44.243 1.00 98.44  ? 120  PHE   A CD2 1 
ATOM   366   C  CE1 . PHE   A 1 51  ? 39.124  21.756  -42.986 1.00 91.50  ? 120  PHE   A CE1 1 
ATOM   367   C  CE2 . PHE   A 1 51  ? 38.839  23.573  -44.526 1.00 101.97 ? 120  PHE   A CE2 1 
ATOM   368   C  CZ  . PHE   A 1 51  ? 38.338  22.436  -43.894 1.00 95.22  ? 120  PHE   A CZ  1 
ATOM   369   N  N   . ALA   A 1 52  ? 41.911  26.713  -42.825 1.00 100.91 ? 121  ALA   A N   1 
ATOM   370   C  CA  . ALA   A 1 52  ? 41.378  28.065  -42.968 1.00 97.72  ? 121  ALA   A CA  1 
ATOM   371   C  C   . ALA   A 1 52  ? 40.471  28.134  -44.187 1.00 95.84  ? 121  ALA   A C   1 
ATOM   372   O  O   . ALA   A 1 52  ? 40.893  27.794  -45.297 1.00 102.98 ? 121  ALA   A O   1 
ATOM   373   C  CB  . ALA   A 1 52  ? 42.517  29.080  -43.085 1.00 97.85  ? 121  ALA   A CB  1 
ATOM   374   N  N   . VAL   A 1 53  ? 39.229  28.559  -43.974 1.00 93.53  ? 122  VAL   A N   1 
ATOM   375   C  CA  . VAL   A 1 53  ? 38.278  28.810  -45.053 1.00 99.10  ? 122  VAL   A CA  1 
ATOM   376   C  C   . VAL   A 1 53  ? 38.172  30.325  -45.252 1.00 105.24 ? 122  VAL   A C   1 
ATOM   377   O  O   . VAL   A 1 53  ? 37.690  31.056  -44.374 1.00 103.90 ? 122  VAL   A O   1 
ATOM   378   C  CB  . VAL   A 1 53  ? 36.912  28.178  -44.748 1.00 95.52  ? 122  VAL   A CB  1 
ATOM   379   C  CG1 . VAL   A 1 53  ? 35.877  28.648  -45.763 1.00 102.24 ? 122  VAL   A CG1 1 
ATOM   380   C  CG2 . VAL   A 1 53  ? 37.043  26.675  -44.771 1.00 94.56  ? 122  VAL   A CG2 1 
ATOM   381   N  N   . LEU   A 1 54  ? 38.612  30.788  -46.409 1.00 109.19 ? 123  LEU   A N   1 
ATOM   382   C  CA  . LEU   A 1 54  ? 38.678  32.211  -46.718 1.00 116.23 ? 123  LEU   A CA  1 
ATOM   383   C  C   . LEU   A 1 54  ? 37.356  32.711  -47.301 1.00 124.50 ? 123  LEU   A C   1 
ATOM   384   O  O   . LEU   A 1 54  ? 36.571  31.952  -47.883 1.00 127.75 ? 123  LEU   A O   1 
ATOM   385   C  CB  . LEU   A 1 54  ? 39.830  32.471  -47.692 1.00 115.98 ? 123  LEU   A CB  1 
ATOM   386   C  CG  . LEU   A 1 54  ? 41.214  32.368  -47.038 1.00 106.71 ? 123  LEU   A CG  1 
ATOM   387   C  CD1 . LEU   A 1 54  ? 42.401  32.545  -47.995 1.00 96.77  ? 123  LEU   A CD1 1 
ATOM   388   C  CD2 . LEU   A 1 54  ? 41.260  33.395  -45.929 1.00 105.63 ? 123  LEU   A CD2 1 
ATOM   389   N  N   . ALA   A 1 55  ? 37.128  34.020  -47.151 1.00 130.48 ? 124  ALA   A N   1 
ATOM   390   C  CA  . ALA   A 1 55  ? 35.910  34.692  -47.600 1.00 134.12 ? 124  ALA   A CA  1 
ATOM   391   C  C   . ALA   A 1 55  ? 35.986  35.274  -49.020 1.00 137.13 ? 124  ALA   A C   1 
ATOM   392   O  O   . ALA   A 1 55  ? 34.938  35.457  -49.652 1.00 135.87 ? 124  ALA   A O   1 
ATOM   393   C  CB  . ALA   A 1 55  ? 35.536  35.812  -46.611 1.00 128.60 ? 124  ALA   A CB  1 
ATOM   394   N  N   . TYR   A 1 56  ? 37.168  35.590  -49.534 1.00 139.57 ? 125  TYR   A N   1 
ATOM   395   C  CA  . TYR   A 1 56  ? 37.302  36.005  -50.936 1.00 138.09 ? 125  TYR   A CA  1 
ATOM   396   C  C   . TYR   A 1 56  ? 36.453  37.214  -51.338 1.00 141.39 ? 125  TYR   A C   1 
ATOM   397   O  O   . TYR   A 1 56  ? 36.970  38.209  -51.870 1.00 144.67 ? 125  TYR   A O   1 
ATOM   398   C  CB  . TYR   A 1 56  ? 36.951  34.832  -51.847 1.00 140.08 ? 125  TYR   A CB  1 
ATOM   399   C  CG  . TYR   A 1 56  ? 37.917  33.669  -51.737 1.00 144.28 ? 125  TYR   A CG  1 
ATOM   400   C  CD1 . TYR   A 1 56  ? 39.267  33.882  -51.464 1.00 144.50 ? 125  TYR   A CD1 1 
ATOM   401   C  CD2 . TYR   A 1 56  ? 37.482  32.357  -51.894 1.00 146.94 ? 125  TYR   A CD2 1 
ATOM   402   C  CE1 . TYR   A 1 56  ? 40.161  32.815  -51.356 1.00 145.50 ? 125  TYR   A CE1 1 
ATOM   403   C  CE2 . TYR   A 1 56  ? 38.363  31.287  -51.787 1.00 148.49 ? 125  TYR   A CE2 1 
ATOM   404   C  CZ  . TYR   A 1 56  ? 39.701  31.520  -51.519 1.00 148.88 ? 125  TYR   A CZ  1 
ATOM   405   O  OH  . TYR   A 1 56  ? 40.568  30.447  -51.417 1.00 151.25 ? 125  TYR   A OH  1 
ATOM   406   N  N   . ALA   A 1 64  ? 38.965  38.929  -50.662 1.00 140.09 ? 133  ALA   A N   1 
ATOM   407   C  CA  . ALA   A 1 64  ? 38.644  39.174  -49.248 1.00 142.02 ? 133  ALA   A CA  1 
ATOM   408   C  C   . ALA   A 1 64  ? 39.712  38.682  -48.252 1.00 137.61 ? 133  ALA   A C   1 
ATOM   409   O  O   . ALA   A 1 64  ? 40.408  37.688  -48.482 1.00 136.27 ? 133  ALA   A O   1 
ATOM   410   C  CB  . ALA   A 1 64  ? 37.296  38.544  -48.891 1.00 142.83 ? 133  ALA   A CB  1 
ATOM   411   N  N   . GLN   A 1 65  ? 39.792  39.385  -47.124 1.00 127.45 ? 134  GLN   A N   1 
ATOM   412   C  CA  . GLN   A 1 65  ? 40.797  39.139  -46.104 1.00 118.97 ? 134  GLN   A CA  1 
ATOM   413   C  C   . GLN   A 1 65  ? 40.198  38.569  -44.824 1.00 118.03 ? 134  GLN   A C   1 
ATOM   414   O  O   . GLN   A 1 65  ? 40.791  38.726  -43.753 1.00 113.67 ? 134  GLN   A O   1 
ATOM   415   C  CB  . GLN   A 1 65  ? 41.557  40.431  -45.794 1.00 118.47 ? 134  GLN   A CB  1 
ATOM   416   C  CG  . GLN   A 1 65  ? 40.695  41.690  -45.775 1.00 124.58 ? 134  GLN   A CG  1 
ATOM   417   C  CD  . GLN   A 1 65  ? 40.897  42.582  -47.007 1.00 123.37 ? 134  GLN   A CD  1 
ATOM   418   O  OE1 . GLN   A 1 65  ? 41.110  42.095  -48.119 1.00 122.15 ? 134  GLN   A OE1 1 
ATOM   419   N  NE2 . GLN   A 1 65  ? 40.834  43.897  -46.802 1.00 119.60 ? 134  GLN   A NE2 1 
ATOM   420   N  N   . PHE   A 1 66  ? 39.027  37.921  -44.907 1.00 123.37 ? 135  PHE   A N   1 
ATOM   421   C  CA  . PHE   A 1 66  ? 38.370  37.323  -43.740 1.00 120.16 ? 135  PHE   A CA  1 
ATOM   422   C  C   . PHE   A 1 66  ? 38.034  35.856  -44.012 1.00 119.22 ? 135  PHE   A C   1 
ATOM   423   O  O   . PHE   A 1 66  ? 38.174  35.356  -45.132 1.00 122.41 ? 135  PHE   A O   1 
ATOM   424   C  CB  . PHE   A 1 66  ? 37.098  38.096  -43.348 1.00 121.27 ? 135  PHE   A CB  1 
ATOM   425   C  CG  . PHE   A 1 66  ? 37.366  39.440  -42.706 1.00 119.65 ? 135  PHE   A CG  1 
ATOM   426   C  CD1 . PHE   A 1 66  ? 38.559  40.105  -42.919 1.00 119.32 ? 135  PHE   A CD1 1 
ATOM   427   C  CD2 . PHE   A 1 66  ? 36.409  40.033  -41.888 1.00 118.09 ? 135  PHE   A CD2 1 
ATOM   428   C  CE1 . PHE   A 1 66  ? 38.809  41.308  -42.330 1.00 121.92 ? 135  PHE   A CE1 1 
ATOM   429   C  CE2 . PHE   A 1 66  ? 36.640  41.251  -41.303 1.00 116.58 ? 135  PHE   A CE2 1 
ATOM   430   C  CZ  . PHE   A 1 66  ? 37.843  41.886  -41.512 1.00 122.07 ? 135  PHE   A CZ  1 
ATOM   431   N  N   . GLY   A 1 67  ? 37.585  35.157  -42.976 1.00 113.29 ? 136  GLY   A N   1 
ATOM   432   C  CA  . GLY   A 1 67  ? 37.285  33.746  -43.121 1.00 108.97 ? 136  GLY   A CA  1 
ATOM   433   C  C   . GLY   A 1 67  ? 36.998  33.100  -41.779 1.00 97.87  ? 136  GLY   A C   1 
ATOM   434   O  O   . GLY   A 1 67  ? 36.895  33.771  -40.751 1.00 92.39  ? 136  GLY   A O   1 
ATOM   435   N  N   . THR   A 1 68  ? 36.858  31.776  -41.813 1.00 97.41  ? 137  THR   A N   1 
ATOM   436   C  CA  . THR   A 1 68  ? 36.635  31.004  -40.601 1.00 92.91  ? 137  THR   A CA  1 
ATOM   437   C  C   . THR   A 1 68  ? 37.541  29.783  -40.563 1.00 90.96  ? 137  THR   A C   1 
ATOM   438   O  O   . THR   A 1 68  ? 37.870  29.189  -41.594 1.00 87.28  ? 137  THR   A O   1 
ATOM   439   C  CB  . THR   A 1 68  ? 35.194  30.559  -40.480 1.00 87.07  ? 137  THR   A CB  1 
ATOM   440   O  OG1 . THR   A 1 68  ? 34.341  31.692  -40.638 1.00 91.62  ? 137  THR   A OG1 1 
ATOM   441   C  CG2 . THR   A 1 68  ? 34.961  29.961  -39.119 1.00 87.63  ? 137  THR   A CG2 1 
ATOM   442   N  N   . THR   A 1 69  ? 37.958  29.433  -39.352 1.00 89.45  ? 138  THR   A N   1 
ATOM   443   C  CA  . THR   A 1 69  ? 38.687  28.198  -39.122 1.00 87.72  ? 138  THR   A CA  1 
ATOM   444   C  C   . THR   A 1 69  ? 37.714  27.031  -39.174 1.00 88.95  ? 138  THR   A C   1 
ATOM   445   O  O   . THR   A 1 69  ? 36.578  27.139  -38.701 1.00 88.97  ? 138  THR   A O   1 
ATOM   446   C  CB  . THR   A 1 69  ? 39.362  28.254  -37.763 1.00 88.10  ? 138  THR   A CB  1 
ATOM   447   O  OG1 . THR   A 1 69  ? 38.375  27.996  -36.763 1.00 87.38  ? 138  THR   A OG1 1 
ATOM   448   C  CG2 . THR   A 1 69  ? 39.870  29.646  -37.557 1.00 90.21  ? 138  THR   A CG2 1 
ATOM   449   N  N   . ALA   A 1 70  ? 38.154  25.909  -39.752 1.00 88.55  ? 139  ALA   A N   1 
ATOM   450   C  CA  . ALA   A 1 70  ? 37.333  24.700  -39.791 1.00 89.85  ? 139  ALA   A CA  1 
ATOM   451   C  C   . ALA   A 1 70  ? 38.101  23.516  -39.214 1.00 93.16  ? 139  ALA   A C   1 
ATOM   452   O  O   . ALA   A 1 70  ? 39.169  23.152  -39.724 1.00 95.27  ? 139  ALA   A O   1 
ATOM   453   C  CB  . ALA   A 1 70  ? 36.863  24.405  -41.213 1.00 89.77  ? 139  ALA   A CB  1 
ATOM   454   N  N   . GLU   A 1 71  ? 37.536  22.904  -38.170 1.00 93.96  ? 140  GLU   A N   1 
ATOM   455   C  CA  . GLU   A 1 71  ? 38.133  21.778  -37.456 1.00 95.15  ? 140  GLU   A CA  1 
ATOM   456   C  C   . GLU   A 1 71  ? 37.537  20.458  -37.934 1.00 90.04  ? 140  GLU   A C   1 
ATOM   457   O  O   . GLU   A 1 71  ? 36.320  20.344  -38.091 1.00 89.97  ? 140  GLU   A O   1 
ATOM   458   C  CB  . GLU   A 1 71  ? 37.901  21.930  -35.959 1.00 91.12  ? 140  GLU   A CB  1 
ATOM   459   C  CG  . GLU   A 1 71  ? 38.407  20.796  -35.153 1.00 93.08  ? 140  GLU   A CG  1 
ATOM   460   C  CD  . GLU   A 1 71  ? 37.450  20.460  -34.047 1.00 97.21  ? 140  GLU   A CD  1 
ATOM   461   O  OE1 . GLU   A 1 71  ? 36.894  21.411  -33.447 1.00 87.13  ? 140  GLU   A OE1 1 
ATOM   462   O  OE2 . GLU   A 1 71  ? 37.232  19.245  -33.797 1.00 107.70 ? 140  GLU   A OE2 1 
ATOM   463   N  N   . ILE   A 1 72  ? 38.394  19.462  -38.161 1.00 93.79  ? 141  ILE   A N   1 
ATOM   464   C  CA  . ILE   A 1 72  ? 37.965  18.197  -38.761 1.00 99.49  ? 141  ILE   A CA  1 
ATOM   465   C  C   . ILE   A 1 72  ? 37.474  17.241  -37.680 1.00 96.63  ? 141  ILE   A C   1 
ATOM   466   O  O   . ILE   A 1 72  ? 38.136  17.045  -36.652 1.00 95.20  ? 141  ILE   A O   1 
ATOM   467   C  CB  . ILE   A 1 72  ? 39.097  17.557  -39.582 1.00 101.09 ? 141  ILE   A CB  1 
ATOM   468   C  CG1 . ILE   A 1 72  ? 39.863  18.630  -40.370 1.00 101.44 ? 141  ILE   A CG1 1 
ATOM   469   C  CG2 . ILE   A 1 72  ? 38.498  16.503  -40.518 1.00 101.41 ? 141  ILE   A CG2 1 
ATOM   470   C  CD1 . ILE   A 1 72  ? 41.324  18.286  -40.662 1.00 108.88 ? 141  ILE   A CD1 1 
ATOM   471   N  N   . TYR   A 1 73  ? 36.300  16.652  -37.902 1.00 91.04  ? 142  TYR   A N   1 
ATOM   472   C  CA  . TYR   A 1 73  ? 35.735  15.709  -36.945 1.00 96.03  ? 142  TYR   A CA  1 
ATOM   473   C  C   . TYR   A 1 73  ? 35.389  14.379  -37.599 1.00 102.37 ? 142  TYR   A C   1 
ATOM   474   O  O   . TYR   A 1 73  ? 34.605  13.600  -37.044 1.00 102.86 ? 142  TYR   A O   1 
ATOM   475   C  CB  . TYR   A 1 73  ? 34.509  16.308  -36.254 1.00 96.71  ? 142  TYR   A CB  1 
ATOM   476   C  CG  . TYR   A 1 73  ? 33.375  16.688  -37.187 1.00 98.05  ? 142  TYR   A CG  1 
ATOM   477   C  CD1 . TYR   A 1 73  ? 32.447  15.736  -37.643 1.00 97.02  ? 142  TYR   A CD1 1 
ATOM   478   C  CD2 . TYR   A 1 73  ? 33.206  18.000  -37.576 1.00 92.08  ? 142  TYR   A CD2 1 
ATOM   479   C  CE1 . TYR   A 1 73  ? 31.401  16.105  -38.481 1.00 96.17  ? 142  TYR   A CE1 1 
ATOM   480   C  CE2 . TYR   A 1 73  ? 32.178  18.369  -38.405 1.00 93.27  ? 142  TYR   A CE2 1 
ATOM   481   C  CZ  . TYR   A 1 73  ? 31.279  17.426  -38.857 1.00 96.34  ? 142  TYR   A CZ  1 
ATOM   482   O  OH  . TYR   A 1 73  ? 30.266  17.839  -39.692 1.00 99.20  ? 142  TYR   A OH  1 
ATOM   483   N  N   . ALA   A 1 74  ? 35.966  14.101  -38.767 1.00 104.09 ? 143  ALA   A N   1 
ATOM   484   C  CA  . ALA   A 1 74  ? 35.616  12.926  -39.555 1.00 96.96  ? 143  ALA   A CA  1 
ATOM   485   C  C   . ALA   A 1 74  ? 36.633  12.879  -40.697 1.00 107.59 ? 143  ALA   A C   1 
ATOM   486   O  O   . ALA   A 1 74  ? 36.750  13.831  -41.484 1.00 107.64 ? 143  ALA   A O   1 
ATOM   487   C  CB  . ALA   A 1 74  ? 34.151  13.006  -39.979 1.00 97.73  ? 143  ALA   A CB  1 
ATOM   488   N  N   . TYR   A 1 75  ? 37.352  11.752  -40.795 1.00 110.68 ? 144  TYR   A N   1 
ATOM   489   C  CA  . TYR   A 1 75  ? 38.505  11.572  -41.679 1.00 109.32 ? 144  TYR   A CA  1 
ATOM   490   C  C   . TYR   A 1 75  ? 38.482  10.123  -42.158 1.00 117.37 ? 144  TYR   A C   1 
ATOM   491   O  O   . TYR   A 1 75  ? 38.750  9.204   -41.372 1.00 118.96 ? 144  TYR   A O   1 
ATOM   492   C  CB  . TYR   A 1 75  ? 39.841  11.911  -41.009 1.00 109.62 ? 144  TYR   A CB  1 
ATOM   493   C  CG  . TYR   A 1 75  ? 41.087  11.859  -41.870 1.00 116.46 ? 144  TYR   A CG  1 
ATOM   494   C  CD1 . TYR   A 1 75  ? 41.524  10.657  -42.445 1.00 117.50 ? 144  TYR   A CD1 1 
ATOM   495   C  CD2 . TYR   A 1 75  ? 41.881  12.997  -42.044 1.00 118.67 ? 144  TYR   A CD2 1 
ATOM   496   C  CE1 . TYR   A 1 75  ? 42.684  10.601  -43.222 1.00 120.59 ? 144  TYR   A CE1 1 
ATOM   497   C  CE2 . TYR   A 1 75  ? 43.052  12.952  -42.821 1.00 120.96 ? 144  TYR   A CE2 1 
ATOM   498   C  CZ  . TYR   A 1 75  ? 43.446  11.754  -43.402 1.00 121.01 ? 144  TYR   A CZ  1 
ATOM   499   O  OH  . TYR   A 1 75  ? 44.604  11.740  -44.155 1.00 121.59 ? 144  TYR   A OH  1 
ATOM   500   N  N   . ARG   A 1 76  ? 38.171  9.924   -43.446 1.00 126.33 ? 145  ARG   A N   1 
ATOM   501   C  CA  . ARG   A 1 76  ? 38.083  8.602   -44.068 1.00 127.65 ? 145  ARG   A CA  1 
ATOM   502   C  C   . ARG   A 1 76  ? 38.899  8.600   -45.355 1.00 130.99 ? 145  ARG   A C   1 
ATOM   503   O  O   . ARG   A 1 76  ? 38.597  9.364   -46.284 1.00 130.44 ? 145  ARG   A O   1 
ATOM   504   C  CB  . ARG   A 1 76  ? 36.626  8.213   -44.373 1.00 127.27 ? 145  ARG   A CB  1 
ATOM   505   C  CG  . ARG   A 1 76  ? 36.478  6.824   -44.984 1.00 127.87 ? 145  ARG   A CG  1 
ATOM   506   C  CD  . ARG   A 1 76  ? 35.035  6.466   -45.313 1.00 133.64 ? 145  ARG   A CD  1 
ATOM   507   N  NE  . ARG   A 1 76  ? 34.085  6.933   -44.305 1.00 135.13 ? 145  ARG   A NE  1 
ATOM   508   C  CZ  . ARG   A 1 76  ? 33.116  7.811   -44.542 1.00 129.93 ? 145  ARG   A CZ  1 
ATOM   509   N  NH1 . ARG   A 1 76  ? 32.936  8.333   -45.744 1.00 130.94 ? 145  ARG   A NH1 1 
ATOM   510   N  NH2 . ARG   A 1 76  ? 32.299  8.164   -43.552 1.00 124.69 ? 145  ARG   A NH2 1 
ATOM   511   N  N   . GLU   A 1 77  ? 39.918  7.737   -45.416 1.00 128.78 ? 146  GLU   A N   1 
ATOM   512   C  CA  . GLU   A 1 77  ? 40.756  7.572   -46.600 1.00 128.44 ? 146  GLU   A CA  1 
ATOM   513   C  C   . GLU   A 1 77  ? 40.245  6.382   -47.425 1.00 131.23 ? 146  GLU   A C   1 
ATOM   514   O  O   . GLU   A 1 77  ? 40.195  5.251   -46.930 1.00 129.76 ? 146  GLU   A O   1 
ATOM   515   C  CB  . GLU   A 1 77  ? 42.226  7.403   -46.190 1.00 126.62 ? 146  GLU   A CB  1 
ATOM   516   C  CG  . GLU   A 1 77  ? 43.040  8.731   -46.214 1.00 125.31 ? 146  GLU   A CG  1 
ATOM   517   C  CD  . GLU   A 1 77  ? 44.483  8.638   -45.664 1.00 125.86 ? 146  GLU   A CD  1 
ATOM   518   O  OE1 . GLU   A 1 77  ? 44.822  9.365   -44.704 1.00 126.09 ? 146  GLU   A OE1 1 
ATOM   519   O  OE2 . GLU   A 1 77  ? 45.285  7.833   -46.198 1.00 127.86 ? 146  GLU   A OE2 1 
ATOM   520   N  N   . GLU   A 1 78  ? 39.846  6.645   -48.673 1.00 130.40 ? 147  GLU   A N   1 
ATOM   521   C  CA  . GLU   A 1 78  ? 39.269  5.616   -49.544 1.00 130.04 ? 147  GLU   A CA  1 
ATOM   522   C  C   . GLU   A 1 78  ? 40.251  5.079   -50.586 1.00 135.79 ? 147  GLU   A C   1 
ATOM   523   O  O   . GLU   A 1 78  ? 41.133  5.791   -51.060 1.00 135.73 ? 147  GLU   A O   1 
ATOM   524   C  CB  . GLU   A 1 78  ? 38.032  6.155   -50.260 1.00 130.68 ? 147  GLU   A CB  1 
ATOM   525   C  CG  . GLU   A 1 78  ? 36.727  5.845   -49.556 1.00 137.33 ? 147  GLU   A CG  1 
ATOM   526   C  CD  . GLU   A 1 78  ? 35.595  5.576   -50.537 1.00 148.74 ? 147  GLU   A CD  1 
ATOM   527   O  OE1 . GLU   A 1 78  ? 35.776  4.728   -51.446 1.00 144.02 ? 147  GLU   A OE1 1 
ATOM   528   O  OE2 . GLU   A 1 78  ? 34.530  6.223   -50.404 1.00 154.88 ? 147  GLU   A OE2 1 
ATOM   529   N  N   . ILE   A 1 85  ? 42.076  8.860   -52.429 1.00 139.40 ? 154  ILE   A N   1 
ATOM   530   C  CA  . ILE   A 1 85  ? 41.484  10.138  -52.033 1.00 140.98 ? 154  ILE   A CA  1 
ATOM   531   C  C   . ILE   A 1 85  ? 41.125  10.160  -50.547 1.00 138.58 ? 154  ILE   A C   1 
ATOM   532   O  O   . ILE   A 1 85  ? 40.794  9.129   -49.972 1.00 137.17 ? 154  ILE   A O   1 
ATOM   533   C  CB  . ILE   A 1 85  ? 40.234  10.457  -52.877 1.00 141.16 ? 154  ILE   A CB  1 
ATOM   534   C  CG1 . ILE   A 1 85  ? 38.959  10.325  -52.027 1.00 141.06 ? 154  ILE   A CG1 1 
ATOM   535   C  CG2 . ILE   A 1 85  ? 40.170  9.534   -54.082 1.00 145.02 ? 154  ILE   A CG2 1 
ATOM   536   C  CD1 . ILE   A 1 85  ? 38.127  11.621  -51.903 1.00 138.97 ? 154  ILE   A CD1 1 
ATOM   537   N  N   . VAL   A 1 86  ? 41.172  11.351  -49.946 1.00 134.75 ? 155  VAL   A N   1 
ATOM   538   C  CA  . VAL   A 1 86  ? 40.823  11.572  -48.544 1.00 126.02 ? 155  VAL   A CA  1 
ATOM   539   C  C   . VAL   A 1 86  ? 39.479  12.291  -48.487 1.00 123.27 ? 155  VAL   A C   1 
ATOM   540   O  O   . VAL   A 1 86  ? 39.283  13.303  -49.171 1.00 124.45 ? 155  VAL   A O   1 
ATOM   541   C  CB  . VAL   A 1 86  ? 41.918  12.381  -47.824 1.00 120.48 ? 155  VAL   A CB  1 
ATOM   542   C  CG1 . VAL   A 1 86  ? 41.513  12.684  -46.401 1.00 118.73 ? 155  VAL   A CG1 1 
ATOM   543   C  CG2 . VAL   A 1 86  ? 43.233  11.625  -47.851 1.00 120.60 ? 155  VAL   A CG2 1 
ATOM   544   N  N   . LYS   A 1 87  ? 38.548  11.764  -47.692 1.00 119.82 ? 156  LYS   A N   1 
ATOM   545   C  CA  . LYS   A 1 87  ? 37.228  12.363  -47.518 1.00 118.29 ? 156  LYS   A CA  1 
ATOM   546   C  C   . LYS   A 1 87  ? 37.105  12.871  -46.084 1.00 114.00 ? 156  LYS   A C   1 
ATOM   547   O  O   . LYS   A 1 87  ? 37.409  12.136  -45.141 1.00 114.10 ? 156  LYS   A O   1 
ATOM   548   C  CB  . LYS   A 1 87  ? 36.120  11.349  -47.840 1.00 118.11 ? 156  LYS   A CB  1 
ATOM   549   N  N   . VAL   A 1 88  ? 36.668  14.127  -45.912 1.00 112.86 ? 157  VAL   A N   1 
ATOM   550   C  CA  . VAL   A 1 88  ? 36.687  14.797  -44.608 1.00 111.37 ? 157  VAL   A CA  1 
ATOM   551   C  C   . VAL   A 1 88  ? 35.366  15.518  -44.355 1.00 105.16 ? 157  VAL   A C   1 
ATOM   552   O  O   . VAL   A 1 88  ? 34.567  15.755  -45.260 1.00 104.21 ? 157  VAL   A O   1 
ATOM   553   C  CB  . VAL   A 1 88  ? 37.847  15.813  -44.473 1.00 107.60 ? 157  VAL   A CB  1 
ATOM   554   C  CG1 . VAL   A 1 88  ? 39.198  15.173  -44.770 1.00 107.38 ? 157  VAL   A CG1 1 
ATOM   555   C  CG2 . VAL   A 1 88  ? 37.585  17.000  -45.389 1.00 108.56 ? 157  VAL   A CG2 1 
ATOM   556   N  N   . LYS   A 1 89  ? 35.167  15.901  -43.100 1.00 101.33 ? 158  LYS   A N   1 
ATOM   557   C  CA  . LYS   A 1 89  ? 34.015  16.709  -42.723 1.00 100.94 ? 158  LYS   A CA  1 
ATOM   558   C  C   . LYS   A 1 89  ? 34.447  17.616  -41.577 1.00 102.05 ? 158  LYS   A C   1 
ATOM   559   O  O   . LYS   A 1 89  ? 34.881  17.114  -40.528 1.00 95.88  ? 158  LYS   A O   1 
ATOM   560   C  CB  . LYS   A 1 89  ? 32.818  15.820  -42.337 1.00 92.36  ? 158  LYS   A CB  1 
ATOM   561   N  N   . ALA   A 1 90  ? 34.371  18.947  -41.788 1.00 99.69  ? 159  ALA   A N   1 
ATOM   562   C  CA  . ALA   A 1 90  ? 34.815  19.914  -40.789 1.00 91.20  ? 159  ALA   A CA  1 
ATOM   563   C  C   . ALA   A 1 90  ? 33.661  20.785  -40.293 1.00 90.16  ? 159  ALA   A C   1 
ATOM   564   O  O   . ALA   A 1 90  ? 32.657  20.985  -40.986 1.00 91.72  ? 159  ALA   A O   1 
ATOM   565   C  CB  . ALA   A 1 90  ? 35.958  20.785  -41.323 1.00 86.85  ? 159  ALA   A CB  1 
ATOM   566   N  N   . ILE   A 1 91  ? 33.807  21.262  -39.055 1.00 89.47  ? 160  ILE   A N   1 
ATOM   567   C  CA  . ILE   A 1 91  ? 32.902  22.216  -38.420 1.00 87.17  ? 160  ILE   A CA  1 
ATOM   568   C  C   . ILE   A 1 91  ? 33.613  23.573  -38.364 1.00 92.10  ? 160  ILE   A C   1 
ATOM   569   O  O   . ILE   A 1 91  ? 34.835  23.642  -38.161 1.00 89.41  ? 160  ILE   A O   1 
ATOM   570   C  CB  . ILE   A 1 91  ? 32.501  21.730  -37.010 1.00 75.29  ? 160  ILE   A CB  1 
ATOM   571   C  CG1 . ILE   A 1 91  ? 31.382  22.575  -36.408 1.00 81.45  ? 160  ILE   A CG1 1 
ATOM   572   C  CG2 . ILE   A 1 91  ? 33.700  21.778  -36.078 1.00 80.79  ? 160  ILE   A CG2 1 
ATOM   573   C  CD1 . ILE   A 1 91  ? 30.288  22.915  -37.364 1.00 88.89  ? 160  ILE   A CD1 1 
ATOM   574   N  N   . GLY   A 1 92  ? 32.858  24.655  -38.551 1.00 86.38  ? 161  GLY   A N   1 
ATOM   575   C  CA  . GLY   A 1 92  ? 33.444  25.987  -38.448 1.00 87.19  ? 161  GLY   A CA  1 
ATOM   576   C  C   . GLY   A 1 92  ? 33.491  26.424  -36.997 1.00 84.19  ? 161  GLY   A C   1 
ATOM   577   O  O   . GLY   A 1 92  ? 32.560  26.191  -36.231 1.00 86.65  ? 161  GLY   A O   1 
ATOM   578   N  N   . ARG   A 1 93  ? 34.602  27.051  -36.612 1.00 82.19  ? 162  ARG   A N   1 
ATOM   579   C  CA  . ARG   A 1 93  ? 34.834  27.342  -35.200 1.00 86.75  ? 162  ARG   A CA  1 
ATOM   580   C  C   . ARG   A 1 93  ? 35.097  28.814  -34.904 1.00 90.22  ? 162  ARG   A C   1 
ATOM   581   O  O   . ARG   A 1 93  ? 34.422  29.391  -34.048 1.00 89.21  ? 162  ARG   A O   1 
ATOM   582   C  CB  . ARG   A 1 93  ? 35.990  26.475  -34.699 1.00 87.58  ? 162  ARG   A CB  1 
ATOM   583   C  CG  . ARG   A 1 93  ? 35.753  25.000  -34.941 1.00 92.18  ? 162  ARG   A CG  1 
ATOM   584   C  CD  . ARG   A 1 93  ? 34.655  24.402  -34.033 1.00 89.06  ? 162  ARG   A CD  1 
ATOM   585   N  NE  . ARG   A 1 93  ? 35.116  23.146  -33.451 1.00 85.61  ? 162  ARG   A NE  1 
ATOM   586   C  CZ  . ARG   A 1 93  ? 34.366  22.303  -32.757 1.00 86.57  ? 162  ARG   A CZ  1 
ATOM   587   N  NH1 . ARG   A 1 93  ? 33.056  22.462  -32.653 1.00 89.17  ? 162  ARG   A NH1 1 
ATOM   588   N  NH2 . ARG   A 1 93  ? 34.950  21.279  -32.141 1.00 89.43  ? 162  ARG   A NH2 1 
ATOM   589   N  N   . GLN   A 1 94  ? 36.074  29.435  -35.548 1.00 93.00  ? 163  GLN   A N   1 
ATOM   590   C  CA  . GLN   A 1 94  ? 36.433  30.802  -35.223 1.00 90.97  ? 163  GLN   A CA  1 
ATOM   591   C  C   . GLN   A 1 94  ? 36.592  31.620  -36.489 1.00 94.55  ? 163  GLN   A C   1 
ATOM   592   O  O   . GLN   A 1 94  ? 37.059  31.122  -37.520 1.00 90.87  ? 163  GLN   A O   1 
ATOM   593   C  CB  . GLN   A 1 94  ? 37.718  30.863  -34.432 1.00 92.87  ? 163  GLN   A CB  1 
ATOM   594   C  CG  . GLN   A 1 94  ? 37.551  30.510  -32.990 1.00 99.11  ? 163  GLN   A CG  1 
ATOM   595   C  CD  . GLN   A 1 94  ? 38.866  30.136  -32.381 1.00 117.30 ? 163  GLN   A CD  1 
ATOM   596   O  OE1 . GLN   A 1 94  ? 39.541  29.227  -32.864 1.00 124.31 ? 163  GLN   A OE1 1 
ATOM   597   N  NE2 . GLN   A 1 94  ? 39.261  30.849  -31.331 1.00 124.85 ? 163  GLN   A NE2 1 
ATOM   598   N  N   . ARG   A 1 95  ? 36.212  32.891  -36.389 1.00 93.15  ? 164  ARG   A N   1 
ATOM   599   C  CA  . ARG   A 1 95  ? 36.382  33.819  -37.489 1.00 92.06  ? 164  ARG   A CA  1 
ATOM   600   C  C   . ARG   A 1 95  ? 37.705  34.554  -37.332 1.00 96.56  ? 164  ARG   A C   1 
ATOM   601   O  O   . ARG   A 1 95  ? 38.168  34.775  -36.214 1.00 99.43  ? 164  ARG   A O   1 
ATOM   602   C  CB  . ARG   A 1 95  ? 35.230  34.806  -37.520 1.00 91.98  ? 164  ARG   A CB  1 
ATOM   603   C  CG  . ARG   A 1 95  ? 33.898  34.170  -37.299 1.00 88.82  ? 164  ARG   A CG  1 
ATOM   604   C  CD  . ARG   A 1 95  ? 33.086  35.060  -36.406 1.00 87.94  ? 164  ARG   A CD  1 
ATOM   605   N  NE  . ARG   A 1 95  ? 33.908  35.531  -35.302 1.00 94.16  ? 164  ARG   A NE  1 
ATOM   606   C  CZ  . ARG   A 1 95  ? 33.654  36.619  -34.588 1.00 96.46  ? 164  ARG   A CZ  1 
ATOM   607   N  NH1 . ARG   A 1 95  ? 32.592  37.368  -34.823 1.00 93.04  ? 164  ARG   A NH1 1 
ATOM   608   N  NH2 . ARG   A 1 95  ? 34.494  36.971  -33.622 1.00 101.98 ? 164  ARG   A NH2 1 
ATOM   609   N  N   . PHE   A 1 96  ? 38.320  34.921  -38.462 1.00 97.87  ? 165  PHE   A N   1 
ATOM   610   C  CA  . PHE   A 1 96  ? 39.645  35.539  -38.444 1.00 97.40  ? 165  PHE   A CA  1 
ATOM   611   C  C   . PHE   A 1 96  ? 39.759  36.599  -39.540 1.00 100.14 ? 165  PHE   A C   1 
ATOM   612   O  O   . PHE   A 1 96  ? 38.921  36.689  -40.443 1.00 102.07 ? 165  PHE   A O   1 
ATOM   613   C  CB  . PHE   A 1 96  ? 40.766  34.485  -38.587 1.00 96.59  ? 165  PHE   A CB  1 
ATOM   614   C  CG  . PHE   A 1 96  ? 40.665  33.610  -39.839 1.00 97.34  ? 165  PHE   A CG  1 
ATOM   615   C  CD1 . PHE   A 1 96  ? 40.585  34.177  -41.110 1.00 97.59  ? 165  PHE   A CD1 1 
ATOM   616   C  CD2 . PHE   A 1 96  ? 40.672  32.212  -39.736 1.00 92.60  ? 165  PHE   A CD2 1 
ATOM   617   C  CE1 . PHE   A 1 96  ? 40.490  33.373  -42.248 1.00 101.17 ? 165  PHE   A CE1 1 
ATOM   618   C  CE2 . PHE   A 1 96  ? 40.584  31.405  -40.872 1.00 92.80  ? 165  PHE   A CE2 1 
ATOM   619   C  CZ  . PHE   A 1 96  ? 40.489  31.989  -42.131 1.00 95.57  ? 165  PHE   A CZ  1 
ATOM   620   N  N   . LYS   A 1 97  ? 40.830  37.397  -39.451 1.00 99.95  ? 166  LYS   A N   1 
ATOM   621   C  CA  . LYS   A 1 97  ? 41.209  38.377  -40.464 1.00 102.06 ? 166  LYS   A CA  1 
ATOM   622   C  C   . LYS   A 1 97  ? 42.579  38.023  -41.031 1.00 96.84  ? 166  LYS   A C   1 
ATOM   623   O  O   . LYS   A 1 97  ? 43.535  37.846  -40.272 1.00 96.90  ? 166  LYS   A O   1 
ATOM   624   C  CB  . LYS   A 1 97  ? 41.247  39.797  -39.886 1.00 106.10 ? 166  LYS   A CB  1 
ATOM   625   C  CG  . LYS   A 1 97  ? 41.691  40.838  -40.914 1.00 105.40 ? 166  LYS   A CG  1 
ATOM   626   C  CD  . LYS   A 1 97  ? 41.670  42.226  -40.344 1.00 107.25 ? 166  LYS   A CD  1 
ATOM   627   C  CE  . LYS   A 1 97  ? 41.632  43.230  -41.459 1.00 111.14 ? 166  LYS   A CE  1 
ATOM   628   N  NZ  . LYS   A 1 97  ? 42.742  44.190  -41.296 1.00 110.20 ? 166  LYS   A NZ  1 
ATOM   629   N  N   . VAL   A 1 98  ? 42.695  37.940  -42.357 1.00 96.73  ? 167  VAL   A N   1 
ATOM   630   C  CA  . VAL   A 1 98  ? 43.967  37.522  -42.938 1.00 96.57  ? 167  VAL   A CA  1 
ATOM   631   C  C   . VAL   A 1 98  ? 45.009  38.614  -42.737 1.00 101.46 ? 167  VAL   A C   1 
ATOM   632   O  O   . VAL   A 1 98  ? 44.748  39.802  -42.975 1.00 107.14 ? 167  VAL   A O   1 
ATOM   633   C  CB  . VAL   A 1 98  ? 43.819  37.170  -44.426 1.00 101.85 ? 167  VAL   A CB  1 
ATOM   634   C  CG1 . VAL   A 1 98  ? 45.203  37.117  -45.094 1.00 102.26 ? 167  VAL   A CG1 1 
ATOM   635   C  CG2 . VAL   A 1 98  ? 43.093  35.831  -44.602 1.00 105.14 ? 167  VAL   A CG2 1 
ATOM   636   N  N   . LEU   A 1 99  ? 46.204  38.212  -42.303 1.00 101.14 ? 168  LEU   A N   1 
ATOM   637   C  CA  . LEU   A 1 99  ? 47.355  39.103  -42.175 1.00 101.15 ? 168  LEU   A CA  1 
ATOM   638   C  C   . LEU   A 1 99  ? 48.356  38.954  -43.322 1.00 104.02 ? 168  LEU   A C   1 
ATOM   639   O  O   . LEU   A 1 99  ? 48.805  39.963  -43.875 1.00 108.81 ? 168  LEU   A O   1 
ATOM   640   C  CB  . LEU   A 1 99  ? 48.042  38.865  -40.827 1.00 95.93  ? 168  LEU   A CB  1 
ATOM   641   C  CG  . LEU   A 1 99  ? 47.122  39.101  -39.637 1.00 90.14  ? 168  LEU   A CG  1 
ATOM   642   C  CD1 . LEU   A 1 99  ? 47.943  39.652  -38.516 1.00 92.10  ? 168  LEU   A CD1 1 
ATOM   643   C  CD2 . LEU   A 1 99  ? 46.003  40.049  -40.000 1.00 90.76  ? 168  LEU   A CD2 1 
ATOM   644   N  N   . GLU   A 1 100 ? 48.723  37.723  -43.689 1.00 105.42 ? 169  GLU   A N   1 
ATOM   645   C  CA  . GLU   A 1 100 ? 49.587  37.455  -44.840 1.00 109.75 ? 169  GLU   A CA  1 
ATOM   646   C  C   . GLU   A 1 100 ? 49.053  36.237  -45.602 1.00 116.93 ? 169  GLU   A C   1 
ATOM   647   O  O   . GLU   A 1 100 ? 48.048  35.634  -45.216 1.00 113.25 ? 169  GLU   A O   1 
ATOM   648   C  CB  . GLU   A 1 100 ? 51.040  37.238  -44.405 1.00 107.99 ? 169  GLU   A CB  1 
ATOM   649   C  CG  . GLU   A 1 100 ? 51.658  38.385  -43.693 1.00 107.25 ? 169  GLU   A CG  1 
ATOM   650   C  CD  . GLU   A 1 100 ? 53.082  38.089  -43.334 1.00 118.96 ? 169  GLU   A CD  1 
ATOM   651   O  OE1 . GLU   A 1 100 ? 53.571  37.030  -43.774 1.00 120.24 ? 169  GLU   A OE1 1 
ATOM   652   O  OE2 . GLU   A 1 100 ? 53.712  38.898  -42.616 1.00 126.57 ? 169  GLU   A OE2 1 
ATOM   653   N  N   . LEU   A 1 101 ? 49.739  35.868  -46.697 1.00 123.79 ? 170  LEU   A N   1 
ATOM   654   C  CA  . LEU   A 1 101 ? 49.321  34.741  -47.541 1.00 122.71 ? 170  LEU   A CA  1 
ATOM   655   C  C   . LEU   A 1 101 ? 50.547  34.179  -48.265 1.00 135.59 ? 170  LEU   A C   1 
ATOM   656   O  O   . LEU   A 1 101 ? 50.965  34.730  -49.288 1.00 135.93 ? 170  LEU   A O   1 
ATOM   657   C  CB  . LEU   A 1 101 ? 48.248  35.168  -48.537 1.00 111.10 ? 170  LEU   A CB  1 
ATOM   658   C  CG  . LEU   A 1 101 ? 46.774  34.946  -48.183 1.00 112.90 ? 170  LEU   A CG  1 
ATOM   659   C  CD1 . LEU   A 1 101 ? 45.859  35.621  -49.200 1.00 100.09 ? 170  LEU   A CD1 1 
ATOM   660   C  CD2 . LEU   A 1 101 ? 46.465  33.456  -48.102 1.00 118.82 ? 170  LEU   A CD2 1 
ATOM   661   N  N   . ARG   A 1 102 ? 51.109  33.084  -47.740 1.00 148.87 ? 171  ARG   A N   1 
ATOM   662   C  CA  . ARG   A 1 102 ? 52.175  32.340  -48.417 1.00 153.01 ? 171  ARG   A CA  1 
ATOM   663   C  C   . ARG   A 1 102 ? 51.554  31.401  -49.443 1.00 157.84 ? 171  ARG   A C   1 
ATOM   664   O  O   . ARG   A 1 102 ? 50.945  30.392  -49.076 1.00 159.05 ? 171  ARG   A O   1 
ATOM   665   C  CB  . ARG   A 1 102 ? 52.995  31.506  -47.434 1.00 151.94 ? 171  ARG   A CB  1 
ATOM   666   C  CG  . ARG   A 1 102 ? 54.261  32.125  -46.895 1.00 149.60 ? 171  ARG   A CG  1 
ATOM   667   C  CD  . ARG   A 1 102 ? 54.297  31.870  -45.401 1.00 148.04 ? 171  ARG   A CD  1 
ATOM   668   N  NE  . ARG   A 1 102 ? 52.983  32.152  -44.838 1.00 150.30 ? 171  ARG   A NE  1 
ATOM   669   C  CZ  . ARG   A 1 102 ? 52.554  33.361  -44.499 1.00 147.43 ? 171  ARG   A CZ  1 
ATOM   670   N  NH1 . ARG   A 1 102 ? 53.351  34.418  -44.534 1.00 145.49 ? 171  ARG   A NH1 1 
ATOM   671   N  NH2 . ARG   A 1 102 ? 51.289  33.518  -44.128 1.00 145.35 ? 171  ARG   A NH2 1 
ATOM   672   N  N   . THR   A 1 103 ? 51.708  31.726  -50.726 1.00 161.03 ? 172  THR   A N   1 
ATOM   673   C  CA  . THR   A 1 103 ? 51.233  30.795  -51.771 1.00 163.88 ? 172  THR   A CA  1 
ATOM   674   C  C   . THR   A 1 103 ? 52.405  29.911  -52.132 1.00 163.62 ? 172  THR   A C   1 
ATOM   675   O  O   . THR   A 1 103 ? 53.050  30.174  -53.165 1.00 165.99 ? 172  THR   A O   1 
ATOM   676   C  CB  . THR   A 1 103 ? 50.678  31.563  -52.968 1.00 162.39 ? 172  THR   A CB  1 
ATOM   677   O  OG1 . THR   A 1 103 ? 49.995  32.687  -52.423 1.00 154.36 ? 172  THR   A OG1 1 
ATOM   678   C  CG2 . THR   A 1 103 ? 49.704  30.734  -53.785 1.00 162.41 ? 172  THR   A CG2 1 
ATOM   679   N  N   . GLN   A 1 104 ? 52.682  28.896  -51.312 1.00 165.51 ? 173  GLN   A N   1 
ATOM   680   C  CA  . GLN   A 1 104 ? 53.880  28.042  -51.525 1.00 168.70 ? 173  GLN   A CA  1 
ATOM   681   C  C   . GLN   A 1 104 ? 53.812  27.288  -52.862 1.00 172.52 ? 173  GLN   A C   1 
ATOM   682   O  O   . GLN   A 1 104 ? 52.696  27.124  -53.403 1.00 172.14 ? 173  GLN   A O   1 
ATOM   683   C  CB  . GLN   A 1 104 ? 54.011  27.071  -50.352 1.00 169.14 ? 173  GLN   A CB  1 
ATOM   684   C  CG  . GLN   A 1 104 ? 54.337  27.751  -49.027 1.00 169.24 ? 173  GLN   A CG  1 
ATOM   685   C  CD  . GLN   A 1 104 ? 54.394  26.791  -47.861 1.00 168.52 ? 173  GLN   A CD  1 
ATOM   686   O  OE1 . GLN   A 1 104 ? 53.776  25.721  -47.876 1.00 167.79 ? 173  GLN   A OE1 1 
ATOM   687   N  NE2 . GLN   A 1 104 ? 55.134  27.169  -46.830 1.00 164.26 ? 173  GLN   A NE2 1 
ATOM   688   N  N   . SER   A 1 105 ? 54.964  26.816  -53.348 1.00 169.31 ? 174  SER   A N   1 
ATOM   689   C  CA  . SER   A 1 105 ? 55.034  26.091  -54.645 1.00 164.51 ? 174  SER   A CA  1 
ATOM   690   C  C   . SER   A 1 105 ? 54.003  24.962  -54.688 1.00 164.67 ? 174  SER   A C   1 
ATOM   691   O  O   . SER   A 1 105 ? 53.216  24.922  -55.655 1.00 162.26 ? 174  SER   A O   1 
ATOM   692   C  CB  . SER   A 1 105 ? 56.412  25.541  -54.861 1.00 156.77 ? 174  SER   A CB  1 
ATOM   693   O  OG  . SER   A 1 105 ? 56.772  24.672  -53.796 1.00 156.12 ? 174  SER   A OG  1 
ATOM   694   N  N   . ASP   A 1 106 ? 54.014  24.084  -53.684 1.00 164.09 ? 175  ASP   A N   1 
ATOM   695   C  CA  . ASP   A 1 106 ? 53.077  22.928  -53.630 1.00 162.83 ? 175  ASP   A CA  1 
ATOM   696   C  C   . ASP   A 1 106 ? 51.726  23.281  -54.260 1.00 164.05 ? 175  ASP   A C   1 
ATOM   697   O  O   . ASP   A 1 106 ? 51.160  22.413  -54.955 1.00 162.33 ? 175  ASP   A O   1 
ATOM   698   C  CB  . ASP   A 1 106 ? 52.897  22.462  -52.196 1.00 163.45 ? 175  ASP   A CB  1 
ATOM   699   C  CG  . ASP   A 1 106 ? 52.863  23.573  -51.157 1.00 166.10 ? 175  ASP   A CG  1 
ATOM   700   O  OD1 . ASP   A 1 106 ? 52.104  24.543  -51.362 1.00 168.11 ? 175  ASP   A OD1 1 
ATOM   701   O  OD2 . ASP   A 1 106 ? 53.599  23.461  -50.156 1.00 167.62 ? 175  ASP   A OD2 1 
ATOM   702   N  N   . GLY   A 1 107 ? 51.218  24.489  -54.013 1.00 166.20 ? 176  GLY   A N   1 
ATOM   703   C  CA  . GLY   A 1 107 ? 49.887  24.875  -54.514 1.00 165.22 ? 176  GLY   A CA  1 
ATOM   704   C  C   . GLY   A 1 107 ? 48.990  25.186  -53.336 1.00 166.20 ? 176  GLY   A C   1 
ATOM   705   O  O   . GLY   A 1 107 ? 47.893  25.741  -53.549 1.00 165.96 ? 176  GLY   A O   1 
ATOM   706   N  N   . ILE   A 1 108 ? 49.447  24.840  -52.131 1.00 157.63 ? 177  ILE   A N   1 
ATOM   707   C  CA  . ILE   A 1 108 ? 48.667  25.144  -50.900 1.00 148.39 ? 177  ILE   A CA  1 
ATOM   708   C  C   . ILE   A 1 108 ? 49.016  26.571  -50.460 1.00 148.96 ? 177  ILE   A C   1 
ATOM   709   O  O   . ILE   A 1 108 ? 50.067  27.087  -50.893 1.00 153.24 ? 177  ILE   A O   1 
ATOM   710   C  CB  . ILE   A 1 108 ? 48.978  24.119  -49.796 1.00 138.25 ? 177  ILE   A CB  1 
ATOM   711   N  N   . GLN   A 1 109 ? 48.169  27.171  -49.627 1.00 142.21 ? 178  GLN   A N   1 
ATOM   712   C  CA  . GLN   A 1 109 ? 48.409  28.535  -49.166 1.00 142.88 ? 178  GLN   A CA  1 
ATOM   713   C  C   . GLN   A 1 109 ? 48.373  28.604  -47.640 1.00 142.99 ? 178  GLN   A C   1 
ATOM   714   O  O   . GLN   A 1 109 ? 47.349  28.282  -47.027 1.00 134.94 ? 178  GLN   A O   1 
ATOM   715   C  CB  . GLN   A 1 109 ? 47.371  29.488  -49.759 1.00 138.19 ? 178  GLN   A CB  1 
ATOM   716   N  N   . GLN   A 1 110 ? 49.480  29.048  -47.034 1.00 159.42 ? 179  GLN   A N   1 
ATOM   717   C  CA  . GLN   A 1 110 ? 49.545  29.326  -45.599 1.00 157.21 ? 179  GLN   A CA  1 
ATOM   718   C  C   . GLN   A 1 110 ? 49.067  30.749  -45.304 1.00 157.04 ? 179  GLN   A C   1 
ATOM   719   O  O   . GLN   A 1 110 ? 49.110  31.624  -46.171 1.00 159.86 ? 179  GLN   A O   1 
ATOM   720   C  CB  . GLN   A 1 110 ? 50.974  29.144  -45.089 1.00 158.14 ? 179  GLN   A CB  1 
ATOM   721   C  CG  . GLN   A 1 110 ? 51.574  27.801  -45.443 1.00 161.81 ? 179  GLN   A CG  1 
ATOM   722   C  CD  . GLN   A 1 110 ? 50.792  26.655  -44.836 1.00 161.87 ? 179  GLN   A CD  1 
ATOM   723   O  OE1 . GLN   A 1 110 ? 50.158  26.812  -43.789 1.00 155.12 ? 179  GLN   A OE1 1 
ATOM   724   N  NE2 . GLN   A 1 110 ? 50.827  25.495  -45.491 1.00 161.99 ? 179  GLN   A NE2 1 
ATOM   725   N  N   . ALA   A 1 111 ? 48.621  30.989  -44.066 1.00 135.56 ? 180  ALA   A N   1 
ATOM   726   C  CA  . ALA   A 1 111 ? 47.971  32.269  -43.784 1.00 122.30 ? 180  ALA   A CA  1 
ATOM   727   C  C   . ALA   A 1 111 ? 48.221  32.765  -42.362 1.00 113.05 ? 180  ALA   A C   1 
ATOM   728   O  O   . ALA   A 1 111 ? 47.919  32.064  -41.392 1.00 103.82 ? 180  ALA   A O   1 
ATOM   729   C  CB  . ALA   A 1 111 ? 46.464  32.167  -44.032 1.00 113.40 ? 180  ALA   A CB  1 
ATOM   730   N  N   . LYS   A 1 112 ? 48.753  33.991  -42.249 1.00 110.57 ? 181  LYS   A N   1 
ATOM   731   C  CA  . LYS   A 1 112 ? 48.821  34.695  -40.967 1.00 105.62 ? 181  LYS   A CA  1 
ATOM   732   C  C   . LYS   A 1 112 ? 47.435  35.232  -40.647 1.00 101.52 ? 181  LYS   A C   1 
ATOM   733   O  O   . LYS   A 1 112 ? 46.846  35.966  -41.444 1.00 101.17 ? 181  LYS   A O   1 
ATOM   734   C  CB  . LYS   A 1 112 ? 49.834  35.840  -40.986 1.00 98.48  ? 181  LYS   A CB  1 
ATOM   735   N  N   . VAL   A 1 113 ? 46.907  34.865  -39.493 1.00 100.72 ? 182  VAL   A N   1 
ATOM   736   C  CA  . VAL   A 1 113 ? 45.502  35.078  -39.206 1.00 97.54  ? 182  VAL   A CA  1 
ATOM   737   C  C   . VAL   A 1 113 ? 45.375  35.809  -37.879 1.00 100.04 ? 182  VAL   A C   1 
ATOM   738   O  O   . VAL   A 1 113 ? 46.132  35.547  -36.939 1.00 108.90 ? 182  VAL   A O   1 
ATOM   739   C  CB  . VAL   A 1 113 ? 44.745  33.732  -39.198 1.00 98.60  ? 182  VAL   A CB  1 
ATOM   740   C  CG1 . VAL   A 1 113 ? 43.558  33.801  -38.292 1.00 101.65 ? 182  VAL   A CG1 1 
ATOM   741   C  CG2 . VAL   A 1 113 ? 44.303  33.368  -40.600 1.00 95.86  ? 182  VAL   A CG2 1 
ATOM   742   N  N   . GLN   A 1 114 ? 44.437  36.740  -37.812 1.00 97.40  ? 183  GLN   A N   1 
ATOM   743   C  CA  . GLN   A 1 114 ? 44.084  37.429  -36.579 1.00 101.71 ? 183  GLN   A CA  1 
ATOM   744   C  C   . GLN   A 1 114 ? 42.683  36.964  -36.194 1.00 104.05 ? 183  GLN   A C   1 
ATOM   745   O  O   . GLN   A 1 114 ? 41.727  37.189  -36.943 1.00 103.11 ? 183  GLN   A O   1 
ATOM   746   C  CB  . GLN   A 1 114 ? 44.164  38.945  -36.783 1.00 105.80 ? 183  GLN   A CB  1 
ATOM   747   C  CG  . GLN   A 1 114 ? 43.716  39.828  -35.607 1.00 113.38 ? 183  GLN   A CG  1 
ATOM   748   C  CD  . GLN   A 1 114 ? 44.759  39.949  -34.507 1.00 115.39 ? 183  GLN   A CD  1 
ATOM   749   O  OE1 . GLN   A 1 114 ? 45.963  40.016  -34.771 1.00 117.28 ? 183  GLN   A OE1 1 
ATOM   750   N  NE2 . GLN   A 1 114 ? 44.297  39.978  -33.263 1.00 117.33 ? 183  GLN   A NE2 1 
ATOM   751   N  N   . ILE   A 1 115 ? 42.560  36.292  -35.048 1.00 113.07 ? 184  ILE   A N   1 
ATOM   752   C  CA  . ILE   A 1 115 ? 41.261  35.764  -34.634 1.00 116.72 ? 184  ILE   A CA  1 
ATOM   753   C  C   . ILE   A 1 115 ? 40.355  36.921  -34.235 1.00 116.35 ? 184  ILE   A C   1 
ATOM   754   O  O   . ILE   A 1 115 ? 40.636  37.648  -33.276 1.00 123.26 ? 184  ILE   A O   1 
ATOM   755   C  CB  . ILE   A 1 115 ? 41.408  34.752  -33.492 1.00 118.45 ? 184  ILE   A CB  1 
ATOM   756   C  CG1 . ILE   A 1 115 ? 42.349  33.641  -33.920 1.00 114.34 ? 184  ILE   A CG1 1 
ATOM   757   C  CG2 . ILE   A 1 115 ? 40.060  34.147  -33.134 1.00 116.66 ? 184  ILE   A CG2 1 
ATOM   758   C  CD1 . ILE   A 1 115 ? 42.466  32.548  -32.910 1.00 136.86 ? 184  ILE   A CD1 1 
ATOM   759   N  N   . LEU   A 1 116 ? 39.264  37.098  -34.974 1.00 112.29 ? 185  LEU   A N   1 
ATOM   760   C  CA  . LEU   A 1 116 ? 38.304  38.135  -34.658 1.00 110.56 ? 185  LEU   A CA  1 
ATOM   761   C  C   . LEU   A 1 116 ? 37.758  37.926  -33.245 1.00 117.42 ? 185  LEU   A C   1 
ATOM   762   O  O   . LEU   A 1 116 ? 37.926  36.856  -32.655 1.00 116.63 ? 185  LEU   A O   1 
ATOM   763   C  CB  . LEU   A 1 116 ? 37.176  38.136  -35.688 1.00 106.03 ? 185  LEU   A CB  1 
ATOM   764   C  CG  . LEU   A 1 116 ? 37.448  38.885  -37.001 1.00 103.66 ? 185  LEU   A CG  1 
ATOM   765   C  CD1 . LEU   A 1 116 ? 38.909  38.774  -37.461 1.00 101.39 ? 185  LEU   A CD1 1 
ATOM   766   C  CD2 . LEU   A 1 116 ? 36.516  38.381  -38.089 1.00 101.35 ? 185  LEU   A CD2 1 
ATOM   767   N  N   . PRO   A 1 117 ? 37.137  38.955  -32.670 1.00 123.53 ? 186  PRO   A N   1 
ATOM   768   C  CA  . PRO   A 1 117 ? 36.712  38.877  -31.263 1.00 123.72 ? 186  PRO   A CA  1 
ATOM   769   C  C   . PRO   A 1 117 ? 35.279  38.538  -30.880 1.00 120.43 ? 186  PRO   A C   1 
ATOM   770   O  O   . PRO   A 1 117 ? 34.313  39.169  -31.320 1.00 117.58 ? 186  PRO   A O   1 
ATOM   771   C  CB  . PRO   A 1 117 ? 36.705  40.345  -30.813 1.00 121.93 ? 186  PRO   A CB  1 
ATOM   772   C  CG  . PRO   A 1 117 ? 36.580  41.144  -32.066 1.00 119.94 ? 186  PRO   A CG  1 
ATOM   773   C  CD  . PRO   A 1 117 ? 37.239  40.345  -33.155 1.00 120.55 ? 186  PRO   A CD  1 
ATOM   774   N  N   . GLU   A 1 118 ? 35.163  37.505  -30.028 1.00 119.35 ? 187  GLU   A N   1 
ATOM   775   C  CA  . GLU   A 1 118 ? 33.899  37.124  -29.391 1.00 112.30 ? 187  GLU   A CA  1 
ATOM   776   C  C   . GLU   A 1 118 ? 33.705  37.644  -27.966 1.00 108.00 ? 187  GLU   A C   1 
ATOM   777   O  O   . GLU   A 1 118 ? 33.736  36.877  -27.000 1.00 110.93 ? 187  GLU   A O   1 
ATOM   778   C  CB  . GLU   A 1 118 ? 33.826  35.590  -29.449 1.00 105.69 ? 187  GLU   A CB  1 
ATOM   779   C  CG  . GLU   A 1 118 ? 32.385  35.046  -29.476 1.00 104.68 ? 187  GLU   A CG  1 
ATOM   780   C  CD  . GLU   A 1 118 ? 31.710  35.155  -30.866 1.00 104.30 ? 187  GLU   A CD  1 
ATOM   781   O  OE1 . GLU   A 1 118 ? 32.268  34.614  -31.854 1.00 104.15 ? 187  GLU   A OE1 1 
ATOM   782   O  OE2 . GLU   A 1 118 ? 30.615  35.772  -30.970 1.00 100.45 ? 187  GLU   A OE2 1 
ATOM   783   N  N   . CYS   A 1 119 ? 33.499  38.957  -27.848 1.00 102.91 ? 188  CYS   A N   1 
ATOM   784   C  CA  . CYS   A 1 119 ? 33.326  39.583  -26.541 1.00 98.80  ? 188  CYS   A CA  1 
ATOM   785   C  C   . CYS   A 1 119 ? 32.099  39.020  -25.865 1.00 90.25  ? 188  CYS   A C   1 
ATOM   786   O  O   . CYS   A 1 119 ? 30.994  39.058  -26.419 1.00 85.56  ? 188  CYS   A O   1 
ATOM   787   C  CB  . CYS   A 1 119 ? 33.185  41.100  -26.662 1.00 96.37  ? 188  CYS   A CB  1 
ATOM   788   S  SG  . CYS   A 1 119 ? 34.261  41.824  -27.891 1.00 100.87 ? 188  CYS   A SG  1 
ATOM   789   N  N   . VAL   A 1 120 ? 32.303  38.499  -24.664 1.00 89.25  ? 189  VAL   A N   1 
ATOM   790   C  CA  . VAL   A 1 120 ? 31.233  37.981  -23.832 1.00 88.07  ? 189  VAL   A CA  1 
ATOM   791   C  C   . VAL   A 1 120 ? 31.078  38.940  -22.664 1.00 83.68  ? 189  VAL   A C   1 
ATOM   792   O  O   . VAL   A 1 120 ? 32.075  39.301  -22.028 1.00 88.13  ? 189  VAL   A O   1 
ATOM   793   C  CB  . VAL   A 1 120 ? 31.538  36.546  -23.374 1.00 79.78  ? 189  VAL   A CB  1 
ATOM   794   C  CG1 . VAL   A 1 120 ? 32.969  36.462  -22.840 1.00 90.45  ? 189  VAL   A CG1 1 
ATOM   795   C  CG2 . VAL   A 1 120 ? 30.520  36.105  -22.358 1.00 72.07  ? 189  VAL   A CG2 1 
ATOM   796   N  N   . LEU   A 1 121 ? 29.843  39.384  -22.404 1.00 80.86  ? 190  LEU   A N   1 
ATOM   797   C  CA  . LEU   A 1 121 ? 29.640  40.446  -21.428 1.00 79.38  ? 190  LEU   A CA  1 
ATOM   798   C  C   . LEU   A 1 121 ? 28.742  39.988  -20.295 1.00 80.19  ? 190  LEU   A C   1 
ATOM   799   O  O   . LEU   A 1 121 ? 27.856  39.152  -20.500 1.00 86.92  ? 190  LEU   A O   1 
ATOM   800   C  CB  . LEU   A 1 121 ? 29.013  41.688  -22.061 1.00 84.57  ? 190  LEU   A CB  1 
ATOM   801   C  CG  . LEU   A 1 121 ? 29.837  42.368  -23.139 1.00 84.51  ? 190  LEU   A CG  1 
ATOM   802   C  CD1 . LEU   A 1 121 ? 29.172  43.682  -23.420 1.00 86.37  ? 190  LEU   A CD1 1 
ATOM   803   C  CD2 . LEU   A 1 121 ? 31.270  42.565  -22.665 1.00 85.13  ? 190  LEU   A CD2 1 
ATOM   804   N  N   . PRO   A 1 122 ? 28.915  40.557  -19.098 1.00 81.98  ? 191  PRO   A N   1 
ATOM   805   C  CA  . PRO   A 1 122 ? 28.028  40.223  -17.979 1.00 81.21  ? 191  PRO   A CA  1 
ATOM   806   C  C   . PRO   A 1 122 ? 26.645  40.814  -18.155 1.00 86.49  ? 191  PRO   A C   1 
ATOM   807   O  O   . PRO   A 1 122 ? 26.390  41.534  -19.123 1.00 89.04  ? 191  PRO   A O   1 
ATOM   808   C  CB  . PRO   A 1 122 ? 28.743  40.832  -16.768 1.00 83.26  ? 191  PRO   A CB  1 
ATOM   809   C  CG  . PRO   A 1 122 ? 29.524  41.962  -17.328 1.00 85.99  ? 191  PRO   A CG  1 
ATOM   810   C  CD  . PRO   A 1 122 ? 29.953  41.527  -18.711 1.00 87.86  ? 191  PRO   A CD  1 
ATOM   811   N  N   . SER   A 1 123 ? 25.742  40.523  -17.224 1.00 91.98  ? 192  SER   A N   1 
ATOM   812   C  CA  . SER   A 1 123 ? 24.423  41.142  -17.240 1.00 88.71  ? 192  SER   A CA  1 
ATOM   813   C  C   . SER   A 1 123 ? 24.559  42.657  -17.168 1.00 89.40  ? 192  SER   A C   1 
ATOM   814   O  O   . SER   A 1 123 ? 25.505  43.188  -16.573 1.00 89.95  ? 192  SER   A O   1 
ATOM   815   C  CB  . SER   A 1 123 ? 23.590  40.621  -16.066 1.00 88.90  ? 192  SER   A CB  1 
ATOM   816   O  OG  . SER   A 1 123 ? 22.338  41.274  -15.970 1.00 87.14  ? 192  SER   A OG  1 
ATOM   817   N  N   . THR   A 1 124 ? 23.602  43.357  -17.787 1.00 89.86  ? 193  THR   A N   1 
ATOM   818   C  CA  . THR   A 1 124 ? 23.591  44.818  -17.699 1.00 91.79  ? 193  THR   A CA  1 
ATOM   819   C  C   . THR   A 1 124 ? 23.517  45.294  -16.239 1.00 89.59  ? 193  THR   A C   1 
ATOM   820   O  O   . THR   A 1 124 ? 24.253  46.206  -15.839 1.00 88.02  ? 193  THR   A O   1 
ATOM   821   C  CB  . THR   A 1 124 ? 22.445  45.395  -18.555 1.00 89.75  ? 193  THR   A CB  1 
ATOM   822   O  OG1 . THR   A 1 124 ? 21.203  44.739  -18.240 1.00 94.24  ? 193  THR   A OG1 1 
ATOM   823   C  CG2 . THR   A 1 124 ? 22.749  45.200  -20.039 1.00 85.80  ? 193  THR   A CG2 1 
ATOM   824   N  N   . MET   A 1 125 ? 22.687  44.657  -15.414 1.00 88.02  ? 194  MET   A N   1 
ATOM   825   C  CA  . MET   A 1 125 ? 22.532  45.093  -14.032 1.00 90.32  ? 194  MET   A CA  1 
ATOM   826   C  C   . MET   A 1 125 ? 23.575  44.480  -13.073 1.00 94.01  ? 194  MET   A C   1 
ATOM   827   O  O   . MET   A 1 125 ? 23.464  44.681  -11.858 1.00 97.53  ? 194  MET   A O   1 
ATOM   828   C  CB  . MET   A 1 125 ? 21.109  44.780  -13.528 1.00 86.90  ? 194  MET   A CB  1 
ATOM   829   C  CG  . MET   A 1 125 ? 19.930  45.493  -14.250 1.00 85.63  ? 194  MET   A CG  1 
ATOM   830   S  SD  . MET   A 1 125 ? 19.970  47.319  -14.387 1.00 94.37  ? 194  MET   A SD  1 
ATOM   831   C  CE  . MET   A 1 125 ? 21.288  47.573  -15.611 1.00 88.41  ? 194  MET   A CE  1 
ATOM   832   N  N   . SER   A 1 126 ? 24.585  43.757  -13.582 1.00 95.42  ? 195  SER   A N   1 
ATOM   833   C  CA  . SER   A 1 126 ? 25.575  43.119  -12.706 1.00 97.19  ? 195  SER   A CA  1 
ATOM   834   C  C   . SER   A 1 126 ? 26.268  44.140  -11.810 1.00 98.54  ? 195  SER   A C   1 
ATOM   835   O  O   . SER   A 1 126 ? 26.361  43.950  -10.591 1.00 101.47 ? 195  SER   A O   1 
ATOM   836   C  CB  . SER   A 1 126 ? 26.611  42.347  -13.535 1.00 96.23  ? 195  SER   A CB  1 
ATOM   837   O  OG  . SER   A 1 126 ? 27.567  43.225  -14.128 1.00 95.98  ? 195  SER   A OG  1 
ATOM   838   N  N   . ALA   A 1 127 ? 26.751  45.240  -12.397 1.00 97.79  ? 196  ALA   A N   1 
ATOM   839   C  CA  . ALA   A 1 127 ? 27.445  46.269  -11.624 1.00 98.72  ? 196  ALA   A CA  1 
ATOM   840   C  C   . ALA   A 1 127 ? 26.512  47.120  -10.776 1.00 99.57  ? 196  ALA   A C   1 
ATOM   841   O  O   . ALA   A 1 127 ? 26.927  47.667  -9.748  1.00 101.66 ? 196  ALA   A O   1 
ATOM   842   C  CB  . ALA   A 1 127 ? 28.263  47.144  -12.576 1.00 96.30  ? 196  ALA   A CB  1 
ATOM   843   N  N   . VAL   A 1 128 ? 25.260  47.264  -11.153 1.00 98.79  ? 197  VAL   A N   1 
ATOM   844   C  CA  . VAL   A 1 128 ? 24.377  48.202  -10.474 1.00 99.94  ? 197  VAL   A CA  1 
ATOM   845   C  C   . VAL   A 1 128 ? 23.467  47.444  -9.506  1.00 100.31 ? 197  VAL   A C   1 
ATOM   846   O  O   . VAL   A 1 128 ? 22.503  47.990  -8.960  1.00 97.26  ? 197  VAL   A O   1 
ATOM   847   C  CB  . VAL   A 1 128 ? 23.652  49.040  -11.558 1.00 98.95  ? 197  VAL   A CB  1 
ATOM   848   C  CG1 . VAL   A 1 128 ? 22.266  49.546  -11.106 1.00 99.09  ? 197  VAL   A CG1 1 
ATOM   849   C  CG2 . VAL   A 1 128 ? 24.571  50.172  -12.022 1.00 95.62  ? 197  VAL   A CG2 1 
ATOM   850   N  N   . GLN   A 1 129 ? 23.807  46.203  -9.259  1.00 104.73 ? 198  GLN   A N   1 
ATOM   851   C  CA  . GLN   A 1 129 ? 22.949  45.373  -8.435  1.00 106.15 ? 198  GLN   A CA  1 
ATOM   852   C  C   . GLN   A 1 129 ? 23.047  45.796  -6.976  1.00 107.65 ? 198  GLN   A C   1 
ATOM   853   O  O   . GLN   A 1 129 ? 24.149  45.946  -6.441  1.00 109.60 ? 198  GLN   A O   1 
ATOM   854   C  CB  . GLN   A 1 129 ? 23.302  43.895  -8.590  1.00 109.43 ? 198  GLN   A CB  1 
ATOM   855   C  CG  . GLN   A 1 129 ? 22.991  43.360  -9.987  1.00 111.59 ? 198  GLN   A CG  1 
ATOM   856   C  CD  . GLN   A 1 129 ? 23.406  41.892  -10.190 1.00 114.96 ? 198  GLN   A CD  1 
ATOM   857   O  OE1 . GLN   A 1 129 ? 24.309  41.369  -9.517  1.00 112.60 ? 198  GLN   A OE1 1 
ATOM   858   N  NE2 . GLN   A 1 129 ? 22.737  41.225  -11.120 1.00 122.23 ? 198  GLN   A NE2 1 
ATOM   859   N  N   . LEU   A 1 130 ? 21.897  46.022  -6.347  1.00 101.14 ? 199  LEU   A N   1 
ATOM   860   C  CA  . LEU   A 1 130 ? 21.869  46.308  -4.921  1.00 97.36  ? 199  LEU   A CA  1 
ATOM   861   C  C   . LEU   A 1 130 ? 22.065  45.011  -4.149  1.00 103.28 ? 199  LEU   A C   1 
ATOM   862   O  O   . LEU   A 1 130 ? 21.306  44.053  -4.341  1.00 107.38 ? 199  LEU   A O   1 
ATOM   863   C  CB  . LEU   A 1 130 ? 20.543  46.956  -4.538  1.00 94.76  ? 199  LEU   A CB  1 
ATOM   864   C  CG  . LEU   A 1 130 ? 20.430  48.464  -4.311  1.00 94.24  ? 199  LEU   A CG  1 
ATOM   865   C  CD1 . LEU   A 1 130 ? 19.275  48.715  -3.367  1.00 97.13  ? 199  LEU   A CD1 1 
ATOM   866   C  CD2 . LEU   A 1 130 ? 21.710  49.055  -3.741  1.00 93.19  ? 199  LEU   A CD2 1 
ATOM   867   N  N   . GLU   A 1 131 ? 23.076  44.976  -3.272  1.00 100.77 ? 200  GLU   A N   1 
ATOM   868   C  CA  . GLU   A 1 131 ? 23.416  43.760  -2.531  1.00 100.58 ? 200  GLU   A CA  1 
ATOM   869   C  C   . GLU   A 1 131 ? 22.175  43.083  -1.964  1.00 98.86  ? 200  GLU   A C   1 
ATOM   870   O  O   . GLU   A 1 131 ? 21.906  41.912  -2.248  1.00 103.93 ? 200  GLU   A O   1 
ATOM   871   C  CB  . GLU   A 1 131 ? 24.411  44.082  -1.406  1.00 103.68 ? 200  GLU   A CB  1 
ATOM   872   C  CG  . GLU   A 1 131 ? 25.879  44.153  -1.856  1.00 106.57 ? 200  GLU   A CG  1 
ATOM   873   C  CD  . GLU   A 1 131 ? 26.139  45.280  -2.863  1.00 112.03 ? 200  GLU   A CD  1 
ATOM   874   O  OE1 . GLU   A 1 131 ? 25.471  46.350  -2.761  1.00 105.82 ? 200  GLU   A OE1 1 
ATOM   875   O  OE2 . GLU   A 1 131 ? 27.011  45.092  -3.752  1.00 113.85 ? 200  GLU   A OE2 1 
ATOM   876   N  N   . SER   A 1 132 ? 21.412  43.821  -1.153  1.00 96.37  ? 201  SER   A N   1 
ATOM   877   C  CA  . SER   A 1 132 ? 20.129  43.349  -0.632  1.00 95.93  ? 201  SER   A CA  1 
ATOM   878   C  C   . SER   A 1 132 ? 19.289  42.645  -1.686  1.00 98.44  ? 201  SER   A C   1 
ATOM   879   O  O   . SER   A 1 132 ? 18.606  41.664  -1.384  1.00 105.51 ? 201  SER   A O   1 
ATOM   880   C  CB  . SER   A 1 132 ? 19.338  44.523  -0.059  1.00 96.09  ? 201  SER   A CB  1 
ATOM   881   O  OG  . SER   A 1 132 ? 19.004  45.463  -1.072  1.00 96.26  ? 201  SER   A OG  1 
ATOM   882   N  N   . LEU   A 1 133 ? 19.291  43.144  -2.919  1.00 102.06 ? 202  LEU   A N   1 
ATOM   883   C  CA  . LEU   A 1 133 ? 18.461  42.533  -3.948  1.00 104.01 ? 202  LEU   A CA  1 
ATOM   884   C  C   . LEU   A 1 133 ? 19.074  41.267  -4.542  1.00 110.68 ? 202  LEU   A C   1 
ATOM   885   O  O   . LEU   A 1 133 ? 18.376  40.540  -5.257  1.00 112.77 ? 202  LEU   A O   1 
ATOM   886   C  CB  . LEU   A 1 133 ? 18.169  43.548  -5.059  1.00 101.68 ? 202  LEU   A CB  1 
ATOM   887   C  CG  . LEU   A 1 133 ? 17.161  44.627  -4.661  1.00 98.53  ? 202  LEU   A CG  1 
ATOM   888   C  CD1 . LEU   A 1 133 ? 16.046  44.044  -3.783  1.00 90.10  ? 202  LEU   A CD1 1 
ATOM   889   C  CD2 . LEU   A 1 133 ? 17.863  45.757  -3.953  1.00 104.39 ? 202  LEU   A CD2 1 
ATOM   890   N  N   . ASN   A 1 134 ? 20.342  40.970  -4.241  1.00 113.81 ? 203  ASN   A N   1 
ATOM   891   C  CA  . ASN   A 1 134 ? 21.057  39.905  -4.944  1.00 114.31 ? 203  ASN   A CA  1 
ATOM   892   C  C   . ASN   A 1 134 ? 20.439  38.533  -4.701  1.00 113.89 ? 203  ASN   A C   1 
ATOM   893   O  O   . ASN   A 1 134 ? 20.608  37.625  -5.526  1.00 114.30 ? 203  ASN   A O   1 
ATOM   894   C  CB  . ASN   A 1 134 ? 22.531  39.888  -4.523  1.00 113.27 ? 203  ASN   A CB  1 
ATOM   895   C  CG  . ASN   A 1 134 ? 23.424  40.670  -5.476  1.00 115.10 ? 203  ASN   A CG  1 
ATOM   896   O  OD1 . ASN   A 1 134 ? 24.653  40.645  -5.364  1.00 118.67 ? 203  ASN   A OD1 1 
ATOM   897   N  ND2 . ASN   A 1 134 ? 22.802  41.377  -6.419  1.00 115.41 ? 203  ASN   A ND2 1 
ATOM   898   N  N   . LYS   A 1 135 ? 19.759  38.351  -3.568  1.00 110.65 ? 204  LYS   A N   1 
ATOM   899   C  CA  . LYS   A 1 135 ? 19.165  37.066  -3.224  1.00 107.50 ? 204  LYS   A CA  1 
ATOM   900   C  C   . LYS   A 1 135 ? 17.778  36.871  -3.845  1.00 106.44 ? 204  LYS   A C   1 
ATOM   901   O  O   . LYS   A 1 135 ? 17.124  35.868  -3.550  1.00 99.51  ? 204  LYS   A O   1 
ATOM   902   C  CB  . LYS   A 1 135 ? 19.108  36.913  -1.691  1.00 103.09 ? 204  LYS   A CB  1 
ATOM   903   N  N   . CYS   A 1 136 ? 17.324  37.783  -4.715  1.00 115.08 ? 205  CYS   A N   1 
ATOM   904   C  CA  . CYS   A 1 136 ? 16.098  37.613  -5.498  1.00 118.18 ? 205  CYS   A CA  1 
ATOM   905   C  C   . CYS   A 1 136 ? 16.375  37.426  -6.986  1.00 122.29 ? 205  CYS   A C   1 
ATOM   906   O  O   . CYS   A 1 136 ? 15.434  37.263  -7.774  1.00 120.00 ? 205  CYS   A O   1 
ATOM   907   C  CB  . CYS   A 1 136 ? 15.164  38.821  -5.313  1.00 115.74 ? 205  CYS   A CB  1 
ATOM   908   S  SG  . CYS   A 1 136 ? 14.932  39.403  -3.601  1.00 105.55 ? 205  CYS   A SG  1 
ATOM   909   N  N   . GLN   A 1 137 ? 17.642  37.458  -7.392  1.00 140.36 ? 206  GLN   A N   1 
ATOM   910   C  CA  . GLN   A 1 137 ? 17.956  37.429  -8.812  1.00 143.33 ? 206  GLN   A CA  1 
ATOM   911   C  C   . GLN   A 1 137 ? 17.690  36.066  -9.418  1.00 145.48 ? 206  GLN   A C   1 
ATOM   912   O  O   . GLN   A 1 137 ? 17.369  35.974  -10.606 1.00 147.35 ? 206  GLN   A O   1 
ATOM   913   C  CB  . GLN   A 1 137 ? 19.408  37.841  -9.037  1.00 142.57 ? 206  GLN   A CB  1 
ATOM   914   C  CG  . GLN   A 1 137 ? 19.545  39.325  -8.971  1.00 142.48 ? 206  GLN   A CG  1 
ATOM   915   C  CD  . GLN   A 1 137 ? 18.206  40.000  -9.258  1.00 147.91 ? 206  GLN   A CD  1 
ATOM   916   O  OE1 . GLN   A 1 137 ? 17.667  40.731  -8.410  1.00 145.82 ? 206  GLN   A OE1 1 
ATOM   917   N  NE2 . GLN   A 1 137 ? 17.655  39.749  -10.454 1.00 141.54 ? 206  GLN   A NE2 1 
ATOM   918   N  N   . ILE   A 1 138 ? 17.825  35.002  -8.635  1.00 125.88 ? 207  ILE   A N   1 
ATOM   919   C  CA  . ILE   A 1 138 ? 17.449  33.696  -9.144  1.00 122.35 ? 207  ILE   A CA  1 
ATOM   920   C  C   . ILE   A 1 138 ? 15.938  33.692  -9.329  1.00 122.38 ? 207  ILE   A C   1 
ATOM   921   O  O   . ILE   A 1 138 ? 15.180  33.969  -8.392  1.00 120.34 ? 207  ILE   A O   1 
ATOM   922   C  CB  . ILE   A 1 138 ? 17.925  32.582  -8.204  1.00 116.40 ? 207  ILE   A CB  1 
ATOM   923   C  CG1 . ILE   A 1 138 ? 18.121  31.275  -8.986  1.00 111.75 ? 207  ILE   A CG1 1 
ATOM   924   C  CG2 . ILE   A 1 138 ? 16.973  32.411  -7.021  1.00 107.50 ? 207  ILE   A CG2 1 
ATOM   925   C  CD1 . ILE   A 1 138 ? 19.376  31.248  -9.863  1.00 104.48 ? 207  ILE   A CD1 1 
ATOM   926   N  N   . PHE   A 1 139 ? 15.498  33.463  -10.555 1.00 126.19 ? 208  PHE   A N   1 
ATOM   927   C  CA  . PHE   A 1 139 ? 14.056  33.430  -10.659 1.00 125.27 ? 208  PHE   A CA  1 
ATOM   928   C  C   . PHE   A 1 139 ? 13.558  31.995  -10.615 1.00 124.95 ? 208  PHE   A C   1 
ATOM   929   O  O   . PHE   A 1 139 ? 14.312  31.053  -10.895 1.00 123.97 ? 208  PHE   A O   1 
ATOM   930   C  CB  . PHE   A 1 139 ? 13.585  34.100  -11.952 1.00 123.45 ? 208  PHE   A CB  1 
ATOM   931   C  CG  . PHE   A 1 139 ? 13.624  35.599  -11.894 1.00 126.25 ? 208  PHE   A CG  1 
ATOM   932   C  CD1 . PHE   A 1 139 ? 13.224  36.278  -10.730 1.00 126.42 ? 208  PHE   A CD1 1 
ATOM   933   C  CD2 . PHE   A 1 139 ? 14.079  36.336  -12.977 1.00 123.06 ? 208  PHE   A CD2 1 
ATOM   934   C  CE1 . PHE   A 1 139 ? 13.259  37.666  -10.657 1.00 122.61 ? 208  PHE   A CE1 1 
ATOM   935   C  CE2 . PHE   A 1 139 ? 14.129  37.723  -12.919 1.00 118.37 ? 208  PHE   A CE2 1 
ATOM   936   C  CZ  . PHE   A 1 139 ? 13.718  38.392  -11.755 1.00 120.97 ? 208  PHE   A CZ  1 
ATOM   937   N  N   . PRO   A 1 140 ? 12.305  31.797  -10.227 1.00 116.56 ? 209  PRO   A N   1 
ATOM   938   C  CA  . PRO   A 1 140 ? 11.726  30.459  -10.341 1.00 119.08 ? 209  PRO   A CA  1 
ATOM   939   C  C   . PRO   A 1 140 ? 11.637  30.098  -11.813 1.00 130.12 ? 209  PRO   A C   1 
ATOM   940   O  O   . PRO   A 1 140 ? 11.366  30.951  -12.668 1.00 130.27 ? 209  PRO   A O   1 
ATOM   941   C  CB  . PRO   A 1 140 ? 10.346  30.604  -9.690  1.00 114.37 ? 209  PRO   A CB  1 
ATOM   942   C  CG  . PRO   A 1 140 ? 10.360  31.942  -8.988  1.00 106.15 ? 209  PRO   A CG  1 
ATOM   943   C  CD  . PRO   A 1 140 ? 11.339  32.784  -9.723  1.00 111.19 ? 209  PRO   A CD  1 
ATOM   944   N  N   . SER   A 1 141 ? 11.899  28.833  -12.105 1.00 137.82 ? 210  SER   A N   1 
ATOM   945   C  CA  . SER   A 1 141 ? 12.094  28.388  -13.482 1.00 143.20 ? 210  SER   A CA  1 
ATOM   946   C  C   . SER   A 1 141 ? 11.105  28.994  -14.497 1.00 142.89 ? 210  SER   A C   1 
ATOM   947   O  O   . SER   A 1 141 ? 9.891   28.787  -14.430 1.00 141.94 ? 210  SER   A O   1 
ATOM   948   C  CB  . SER   A 1 141 ? 12.024  26.861  -13.529 1.00 146.07 ? 210  SER   A CB  1 
ATOM   949   O  OG  . SER   A 1 141 ? 12.361  26.400  -14.820 1.00 151.76 ? 210  SER   A OG  1 
ATOM   950   N  N   . SER   A 1 151 ? 4.743   33.690  -22.597 1.00 118.69 ? 220  SER   A N   1 
ATOM   951   C  CA  . SER   A 1 151 ? 3.549   34.329  -22.036 1.00 127.12 ? 220  SER   A CA  1 
ATOM   952   C  C   . SER   A 1 151 ? 3.829   35.797  -21.643 1.00 129.57 ? 220  SER   A C   1 
ATOM   953   O  O   . SER   A 1 151 ? 4.672   36.070  -20.781 1.00 121.59 ? 220  SER   A O   1 
ATOM   954   C  CB  . SER   A 1 151 ? 3.037   33.532  -20.823 1.00 124.98 ? 220  SER   A CB  1 
ATOM   955   O  OG  . SER   A 1 151 ? 1.661   33.772  -20.573 1.00 125.01 ? 220  SER   A OG  1 
ATOM   956   N  N   . TYR   A 1 152 ? 3.111   36.726  -22.292 1.00 142.62 ? 221  TYR   A N   1 
ATOM   957   C  CA  . TYR   A 1 152 ? 3.220   38.173  -22.102 1.00 139.93 ? 221  TYR   A CA  1 
ATOM   958   C  C   . TYR   A 1 152 ? 3.478   38.572  -20.651 1.00 138.74 ? 221  TYR   A C   1 
ATOM   959   O  O   . TYR   A 1 152 ? 4.420   39.324  -20.365 1.00 137.23 ? 221  TYR   A O   1 
ATOM   960   C  CB  . TYR   A 1 152 ? 1.930   38.819  -22.604 1.00 142.86 ? 221  TYR   A CB  1 
ATOM   961   C  CG  . TYR   A 1 152 ? 1.889   40.329  -22.699 1.00 146.07 ? 221  TYR   A CG  1 
ATOM   962   C  CD1 . TYR   A 1 152 ? 3.046   41.100  -22.681 1.00 146.14 ? 221  TYR   A CD1 1 
ATOM   963   C  CD2 . TYR   A 1 152 ? 0.667   40.979  -22.833 1.00 149.02 ? 221  TYR   A CD2 1 
ATOM   964   C  CE1 . TYR   A 1 152 ? 2.981   42.478  -22.788 1.00 146.60 ? 221  TYR   A CE1 1 
ATOM   965   C  CE2 . TYR   A 1 152 ? 0.591   42.345  -22.936 1.00 151.82 ? 221  TYR   A CE2 1 
ATOM   966   C  CZ  . TYR   A 1 152 ? 1.749   43.092  -22.912 1.00 149.24 ? 221  TYR   A CZ  1 
ATOM   967   O  OH  . TYR   A 1 152 ? 1.676   44.460  -23.010 1.00 148.85 ? 221  TYR   A OH  1 
ATOM   968   N  N   . LYS   A 1 153 ? 2.637   38.079  -19.730 1.00 123.95 ? 222  LYS   A N   1 
ATOM   969   C  CA  . LYS   A 1 153 ? 2.754   38.477  -18.329 1.00 110.55 ? 222  LYS   A CA  1 
ATOM   970   C  C   . LYS   A 1 153 ? 4.106   38.084  -17.761 1.00 105.19 ? 222  LYS   A C   1 
ATOM   971   O  O   . LYS   A 1 153 ? 4.719   38.852  -17.010 1.00 103.64 ? 222  LYS   A O   1 
ATOM   972   C  CB  . LYS   A 1 153 ? 1.634   37.852  -17.501 1.00 100.27 ? 222  LYS   A CB  1 
ATOM   973   N  N   . TRP   A 1 154 ? 4.595   36.894  -18.113 1.00 105.36 ? 223  TRP   A N   1 
ATOM   974   C  CA  . TRP   A 1 154 ? 5.844   36.429  -17.527 1.00 96.01  ? 223  TRP   A CA  1 
ATOM   975   C  C   . TRP   A 1 154 ? 6.995   37.344  -17.893 1.00 96.20  ? 223  TRP   A C   1 
ATOM   976   O  O   . TRP   A 1 154 ? 7.841   37.663  -17.048 1.00 94.86  ? 223  TRP   A O   1 
ATOM   977   C  CB  . TRP   A 1 154 ? 6.160   35.018  -17.975 1.00 93.34  ? 223  TRP   A CB  1 
ATOM   978   C  CG  . TRP   A 1 154 ? 7.205   34.413  -17.114 1.00 87.59  ? 223  TRP   A CG  1 
ATOM   979   C  CD1 . TRP   A 1 154 ? 6.998   33.715  -15.975 1.00 90.18  ? 223  TRP   A CD1 1 
ATOM   980   C  CD2 . TRP   A 1 154 ? 8.621   34.451  -17.310 1.00 80.11  ? 223  TRP   A CD2 1 
ATOM   981   N  NE1 . TRP   A 1 154 ? 8.192   33.302  -15.443 1.00 90.24  ? 223  TRP   A NE1 1 
ATOM   982   C  CE2 . TRP   A 1 154 ? 9.206   33.738  -16.245 1.00 76.96  ? 223  TRP   A CE2 1 
ATOM   983   C  CE3 . TRP   A 1 154 ? 9.449   35.016  -18.279 1.00 83.88  ? 223  TRP   A CE3 1 
ATOM   984   C  CZ2 . TRP   A 1 154 ? 10.574  33.570  -16.115 1.00 84.93  ? 223  TRP   A CZ2 1 
ATOM   985   C  CZ3 . TRP   A 1 154 ? 10.818  34.850  -18.153 1.00 85.95  ? 223  TRP   A CZ3 1 
ATOM   986   C  CH2 . TRP   A 1 154 ? 11.369  34.130  -17.072 1.00 86.56  ? 223  TRP   A CH2 1 
ATOM   987   N  N   . TRP   A 1 155 ? 7.053   37.770  -19.156 1.00 99.07  ? 224  TRP   A N   1 
ATOM   988   C  CA  . TRP   A 1 155 ? 8.149   38.632  -19.565 1.00 93.82  ? 224  TRP   A CA  1 
ATOM   989   C  C   . TRP   A 1 155 ? 7.956   40.065  -19.093 1.00 87.46  ? 224  TRP   A C   1 
ATOM   990   O  O   . TRP   A 1 155 ? 8.940   40.795  -18.949 1.00 83.01  ? 224  TRP   A O   1 
ATOM   991   C  CB  . TRP   A 1 155 ? 8.323   38.560  -21.082 1.00 88.72  ? 224  TRP   A CB  1 
ATOM   992   C  CG  . TRP   A 1 155 ? 8.977   37.269  -21.535 1.00 88.24  ? 224  TRP   A CG  1 
ATOM   993   C  CD1 . TRP   A 1 155 ? 8.349   36.136  -21.966 1.00 89.53  ? 224  TRP   A CD1 1 
ATOM   994   C  CD2 . TRP   A 1 155 ? 10.382  36.987  -21.590 1.00 85.71  ? 224  TRP   A CD2 1 
ATOM   995   N  NE1 . TRP   A 1 155 ? 9.276   35.171  -22.300 1.00 82.30  ? 224  TRP   A NE1 1 
ATOM   996   C  CE2 . TRP   A 1 155 ? 10.528  35.670  -22.080 1.00 79.59  ? 224  TRP   A CE2 1 
ATOM   997   C  CE3 . TRP   A 1 155 ? 11.534  37.729  -21.287 1.00 82.14  ? 224  TRP   A CE3 1 
ATOM   998   C  CZ2 . TRP   A 1 155 ? 11.766  35.082  -22.267 1.00 81.92  ? 224  TRP   A CZ2 1 
ATOM   999   C  CZ3 . TRP   A 1 155 ? 12.770  37.142  -21.475 1.00 79.43  ? 224  TRP   A CZ3 1 
ATOM   1000  C  CH2 . TRP   A 1 155 ? 12.876  35.830  -21.961 1.00 85.19  ? 224  TRP   A CH2 1 
ATOM   1001  N  N   . GLN   A 1 156 ? 6.718   40.480  -18.828 1.00 88.97  ? 225  GLN   A N   1 
ATOM   1002  C  CA  . GLN   A 1 156 ? 6.533   41.756  -18.156 1.00 91.75  ? 225  GLN   A CA  1 
ATOM   1003  C  C   . GLN   A 1 156 ? 7.153   41.722  -16.764 1.00 92.96  ? 225  GLN   A C   1 
ATOM   1004  O  O   . GLN   A 1 156 ? 7.900   42.636  -16.386 1.00 88.32  ? 225  GLN   A O   1 
ATOM   1005  C  CB  . GLN   A 1 156 ? 5.052   42.118  -18.095 1.00 95.94  ? 225  GLN   A CB  1 
ATOM   1006  C  CG  . GLN   A 1 156 ? 4.645   43.127  -19.134 1.00 104.77 ? 225  GLN   A CG  1 
ATOM   1007  C  CD  . GLN   A 1 156 ? 3.147   43.226  -19.280 1.00 117.57 ? 225  GLN   A CD  1 
ATOM   1008  O  OE1 . GLN   A 1 156 ? 2.525   42.424  -19.976 1.00 125.93 ? 225  GLN   A OE1 1 
ATOM   1009  N  NE2 . GLN   A 1 156 ? 2.554   44.215  -18.629 1.00 116.34 ? 225  GLN   A NE2 1 
ATOM   1010  N  N   . LYS   A 1 157 ? 6.878   40.660  -15.995 1.00 91.14  ? 226  LYS   A N   1 
ATOM   1011  C  CA  . LYS   A 1 157 ? 7.500   40.529  -14.684 1.00 82.07  ? 226  LYS   A CA  1 
ATOM   1012  C  C   . LYS   A 1 157 ? 9.011   40.346  -14.813 1.00 82.00  ? 226  LYS   A C   1 
ATOM   1013  O  O   . LYS   A 1 157 ? 9.773   40.987  -14.092 1.00 82.82  ? 226  LYS   A O   1 
ATOM   1014  C  CB  . LYS   A 1 157 ? 6.855   39.381  -13.907 1.00 79.78  ? 226  LYS   A CB  1 
ATOM   1015  N  N   . TYR   A 1 158 ? 9.468   39.501  -15.743 1.00 86.56  ? 227  TYR   A N   1 
ATOM   1016  C  CA  . TYR   A 1 158 ? 10.912  39.313  -15.948 1.00 85.31  ? 227  TYR   A CA  1 
ATOM   1017  C  C   . TYR   A 1 158 ? 11.651  40.645  -15.993 1.00 82.58  ? 227  TYR   A C   1 
ATOM   1018  O  O   . TYR   A 1 158 ? 12.690  40.808  -15.341 1.00 80.53  ? 227  TYR   A O   1 
ATOM   1019  C  CB  . TYR   A 1 158 ? 11.186  38.521  -17.247 1.00 80.25  ? 227  TYR   A CB  1 
ATOM   1020  C  CG  . TYR   A 1 158 ? 12.662  38.416  -17.648 1.00 77.24  ? 227  TYR   A CG  1 
ATOM   1021  C  CD1 . TYR   A 1 158 ? 13.484  37.404  -17.143 1.00 82.07  ? 227  TYR   A CD1 1 
ATOM   1022  C  CD2 . TYR   A 1 158 ? 13.225  39.313  -18.548 1.00 78.79  ? 227  TYR   A CD2 1 
ATOM   1023  C  CE1 . TYR   A 1 158 ? 14.838  37.304  -17.521 1.00 83.12  ? 227  TYR   A CE1 1 
ATOM   1024  C  CE2 . TYR   A 1 158 ? 14.574  39.222  -18.933 1.00 79.48  ? 227  TYR   A CE2 1 
ATOM   1025  C  CZ  . TYR   A 1 158 ? 15.374  38.219  -18.418 1.00 82.75  ? 227  TYR   A CZ  1 
ATOM   1026  O  OH  . TYR   A 1 158 ? 16.705  38.145  -18.798 1.00 85.72  ? 227  TYR   A OH  1 
ATOM   1027  N  N   . GLN   A 1 159 ? 11.134  41.607  -16.771 1.00 79.32  ? 228  GLN   A N   1 
ATOM   1028  C  CA  . GLN   A 1 159 ? 11.826  42.880  -16.954 1.00 78.39  ? 228  GLN   A CA  1 
ATOM   1029  C  C   . GLN   A 1 159 ? 11.688  43.757  -15.709 1.00 83.02  ? 228  GLN   A C   1 
ATOM   1030  O  O   . GLN   A 1 159 ? 12.667  44.369  -15.258 1.00 82.54  ? 228  GLN   A O   1 
ATOM   1031  C  CB  . GLN   A 1 159 ? 11.301  43.573  -18.225 1.00 75.41  ? 228  GLN   A CB  1 
ATOM   1032  C  CG  . GLN   A 1 159 ? 11.578  45.076  -18.364 1.00 73.96  ? 228  GLN   A CG  1 
ATOM   1033  C  CD  . GLN   A 1 159 ? 10.643  45.769  -19.367 1.00 74.04  ? 228  GLN   A CD  1 
ATOM   1034  O  OE1 . GLN   A 1 159 ? 9.605   46.324  -18.991 1.00 82.28  ? 228  GLN   A OE1 1 
ATOM   1035  N  NE2 . GLN   A 1 159 ? 11.015  45.748  -20.645 1.00 72.97  ? 228  GLN   A NE2 1 
ATOM   1036  N  N   . LYS   A 1 160 ? 10.496  43.781  -15.109 1.00 81.38  ? 229  LYS   A N   1 
ATOM   1037  C  CA  . LYS   A 1 160 ? 10.291  44.520  -13.871 1.00 77.38  ? 229  LYS   A CA  1 
ATOM   1038  C  C   . LYS   A 1 160 ? 11.193  44.037  -12.739 1.00 79.53  ? 229  LYS   A C   1 
ATOM   1039  O  O   . LYS   A 1 160 ? 11.435  44.797  -11.796 1.00 89.00  ? 229  LYS   A O   1 
ATOM   1040  C  CB  . LYS   A 1 160 ? 8.825   44.413  -13.456 1.00 80.88  ? 229  LYS   A CB  1 
ATOM   1041  C  CG  . LYS   A 1 160 ? 8.433   45.284  -12.311 1.00 89.04  ? 229  LYS   A CG  1 
ATOM   1042  C  CD  . LYS   A 1 160 ? 7.505   46.399  -12.772 1.00 96.59  ? 229  LYS   A CD  1 
ATOM   1043  C  CE  . LYS   A 1 160 ? 7.058   47.203  -11.571 1.00 99.71  ? 229  LYS   A CE  1 
ATOM   1044  N  NZ  . LYS   A 1 160 ? 8.250   47.818  -10.902 1.00 100.09 ? 229  LYS   A NZ  1 
ATOM   1045  N  N   . ARG   A 1 161 ? 11.696  42.805  -12.800 1.00 79.99  ? 230  ARG   A N   1 
ATOM   1046  C  CA  . ARG   A 1 161 ? 12.486  42.240  -11.714 1.00 80.19  ? 230  ARG   A CA  1 
ATOM   1047  C  C   . ARG   A 1 161 ? 13.972  42.176  -12.020 1.00 84.84  ? 230  ARG   A C   1 
ATOM   1048  O  O   . ARG   A 1 161 ? 14.786  42.375  -11.115 1.00 89.54  ? 230  ARG   A O   1 
ATOM   1049  C  CB  . ARG   A 1 161 ? 11.992  40.836  -11.356 1.00 79.90  ? 230  ARG   A CB  1 
ATOM   1050  N  N   . LYS   A 1 162 ? 14.356  41.897  -13.267 1.00 85.56  ? 231  LYS   A N   1 
ATOM   1051  C  CA  . LYS   A 1 162 ? 15.775  41.792  -13.599 1.00 85.51  ? 231  LYS   A CA  1 
ATOM   1052  C  C   . LYS   A 1 162 ? 16.431  43.156  -13.726 1.00 79.54  ? 231  LYS   A C   1 
ATOM   1053  O  O   . LYS   A 1 162 ? 17.651  43.259  -13.593 1.00 79.10  ? 231  LYS   A O   1 
ATOM   1054  C  CB  . LYS   A 1 162 ? 15.986  40.994  -14.912 1.00 80.31  ? 231  LYS   A CB  1 
ATOM   1055  C  CG  . LYS   A 1 162 ? 17.477  40.924  -15.317 1.00 75.61  ? 231  LYS   A CG  1 
ATOM   1056  C  CD  . LYS   A 1 162 ? 17.801  40.065  -16.537 1.00 76.95  ? 231  LYS   A CD  1 
ATOM   1057  C  CE  . LYS   A 1 162 ? 19.342  39.950  -16.707 1.00 84.21  ? 231  LYS   A CE  1 
ATOM   1058  N  NZ  . LYS   A 1 162 ? 19.847  38.574  -17.097 1.00 93.22  ? 231  LYS   A NZ  1 
ATOM   1059  N  N   . PHE   A 1 163 ? 15.650  44.195  -13.990 1.00 80.15  ? 232  PHE   A N   1 
ATOM   1060  C  CA  . PHE   A 1 163 ? 16.193  45.521  -14.231 1.00 82.74  ? 232  PHE   A CA  1 
ATOM   1061  C  C   . PHE   A 1 163 ? 15.657  46.519  -13.225 1.00 85.09  ? 232  PHE   A C   1 
ATOM   1062  O  O   . PHE   A 1 163 ? 15.634  47.723  -13.503 1.00 85.75  ? 232  PHE   A O   1 
ATOM   1063  C  CB  . PHE   A 1 163 ? 15.873  45.970  -15.652 1.00 79.49  ? 232  PHE   A CB  1 
ATOM   1064  C  CG  . PHE   A 1 163 ? 16.265  44.975  -16.690 1.00 77.81  ? 232  PHE   A CG  1 
ATOM   1065  C  CD1 . PHE   A 1 163 ? 17.608  44.703  -16.931 1.00 76.28  ? 232  PHE   A CD1 1 
ATOM   1066  C  CD2 . PHE   A 1 163 ? 15.296  44.307  -17.429 1.00 75.68  ? 232  PHE   A CD2 1 
ATOM   1067  C  CE1 . PHE   A 1 163 ? 17.979  43.788  -17.890 1.00 77.96  ? 232  PHE   A CE1 1 
ATOM   1068  C  CE2 . PHE   A 1 163 ? 15.655  43.388  -18.393 1.00 75.35  ? 232  PHE   A CE2 1 
ATOM   1069  C  CZ  . PHE   A 1 163 ? 17.000  43.125  -18.627 1.00 78.29  ? 232  PHE   A CZ  1 
ATOM   1070  N  N   . HIS   A 1 164 ? 15.191  46.030  -12.072 1.00 85.34  ? 233  HIS   A N   1 
ATOM   1071  C  CA  . HIS   A 1 164 ? 14.679  46.930  -11.046 1.00 86.36  ? 233  HIS   A CA  1 
ATOM   1072  C  C   . HIS   A 1 164 ? 15.708  48.004  -10.707 1.00 85.27  ? 233  HIS   A C   1 
ATOM   1073  O  O   . HIS   A 1 164 ? 15.370  49.187  -10.554 1.00 80.18  ? 233  HIS   A O   1 
ATOM   1074  C  CB  . HIS   A 1 164 ? 14.282  46.127  -9.806  1.00 81.20  ? 233  HIS   A CB  1 
ATOM   1075  C  CG  . HIS   A 1 164 ? 13.888  46.968  -8.635  1.00 79.23  ? 233  HIS   A CG  1 
ATOM   1076  N  ND1 . HIS   A 1 164 ? 14.637  47.021  -7.480  1.00 81.10  ? 233  HIS   A ND1 1 
ATOM   1077  C  CD2 . HIS   A 1 164 ? 12.818  47.771  -8.428  1.00 81.30  ? 233  HIS   A CD2 1 
ATOM   1078  C  CE1 . HIS   A 1 164 ? 14.049  47.827  -6.613  1.00 87.07  ? 233  HIS   A CE1 1 
ATOM   1079  N  NE2 . HIS   A 1 164 ? 12.944  48.298  -7.164  1.00 82.09  ? 233  HIS   A NE2 1 
ATOM   1080  N  N   . CYS   A 1 165 ? 16.986  47.629  -10.670 1.00 83.97  ? 234  CYS   A N   1 
ATOM   1081  C  CA  . CYS   A 1 165 ? 18.016  48.601  -10.324 1.00 81.35  ? 234  CYS   A CA  1 
ATOM   1082  C  C   . CYS   A 1 165 ? 18.302  49.586  -11.448 1.00 75.96  ? 234  CYS   A C   1 
ATOM   1083  O  O   . CYS   A 1 165 ? 19.302  50.305  -11.393 1.00 77.93  ? 234  CYS   A O   1 
ATOM   1084  C  CB  . CYS   A 1 165 ? 19.284  47.878  -9.869  1.00 90.03  ? 234  CYS   A CB  1 
ATOM   1085  S  SG  . CYS   A 1 165 ? 19.282  47.411  -8.123  1.00 88.97  ? 234  CYS   A SG  1 
ATOM   1086  N  N   . ALA   A 1 166 ? 17.468  49.630  -12.483 1.00 78.30  ? 235  ALA   A N   1 
ATOM   1087  C  CA  . ALA   A 1 166 ? 17.620  50.673  -13.503 1.00 78.19  ? 235  ALA   A CA  1 
ATOM   1088  C  C   . ALA   A 1 166 ? 17.362  52.078  -12.949 1.00 80.24  ? 235  ALA   A C   1 
ATOM   1089  O  O   . ALA   A 1 166 ? 17.895  53.077  -13.466 1.00 75.37  ? 235  ALA   A O   1 
ATOM   1090  C  CB  . ALA   A 1 166 ? 16.710  50.356  -14.688 1.00 75.66  ? 235  ALA   A CB  1 
ATOM   1091  N  N   . ASN   A 1 167 ? 16.565  52.156  -11.885 1.00 78.44  ? 236  ASN   A N   1 
ATOM   1092  C  CA  . ASN   A 1 167 ? 16.312  53.414  -11.222 1.00 77.08  ? 236  ASN   A CA  1 
ATOM   1093  C  C   . ASN   A 1 167 ? 17.573  54.037  -10.676 1.00 75.03  ? 236  ASN   A C   1 
ATOM   1094  O  O   . ASN   A 1 167 ? 17.608  55.254  -10.470 1.00 78.89  ? 236  ASN   A O   1 
ATOM   1095  C  CB  . ASN   A 1 167 ? 15.292  53.198  -10.124 1.00 78.15  ? 236  ASN   A CB  1 
ATOM   1096  C  CG  . ASN   A 1 167 ? 13.894  53.111  -10.679 1.00 90.69  ? 236  ASN   A CG  1 
ATOM   1097  O  OD1 . ASN   A 1 167 ? 13.304  54.130  -11.118 1.00 88.80  ? 236  ASN   A OD1 1 
ATOM   1098  N  ND2 . ASN   A 1 167 ? 13.356  51.883  -10.714 1.00 94.60  ? 236  ASN   A ND2 1 
ATOM   1099  N  N   . LEU   A 1 168 ? 18.610  53.250  -10.448 1.00 71.33  ? 237  LEU   A N   1 
ATOM   1100  C  CA  . LEU   A 1 168 ? 19.858  53.855  -10.016 1.00 76.17  ? 237  LEU   A CA  1 
ATOM   1101  C  C   . LEU   A 1 168 ? 20.674  54.425  -11.167 1.00 75.28  ? 237  LEU   A C   1 
ATOM   1102  O  O   . LEU   A 1 168 ? 21.730  55.017  -10.923 1.00 76.16  ? 237  LEU   A O   1 
ATOM   1103  C  CB  . LEU   A 1 168 ? 20.706  52.834  -9.258  1.00 75.75  ? 237  LEU   A CB  1 
ATOM   1104  C  CG  . LEU   A 1 168 ? 19.979  51.968  -8.249  1.00 71.50  ? 237  LEU   A CG  1 
ATOM   1105  C  CD1 . LEU   A 1 168 ? 20.934  50.925  -7.727  1.00 78.35  ? 237  LEU   A CD1 1 
ATOM   1106  C  CD2 . LEU   A 1 168 ? 19.473  52.821  -7.128  1.00 67.32  ? 237  LEU   A CD2 1 
ATOM   1107  N  N   . THR   A 1 169 ? 20.259  54.222  -12.402 1.00 72.14  ? 238  THR   A N   1 
ATOM   1108  C  CA  . THR   A 1 169 ? 21.031  54.732  -13.518 1.00 79.36  ? 238  THR   A CA  1 
ATOM   1109  C  C   . THR   A 1 169 ? 20.231  55.792  -14.236 1.00 78.69  ? 238  THR   A C   1 
ATOM   1110  O  O   . THR   A 1 169 ? 19.131  56.167  -13.820 1.00 76.72  ? 238  THR   A O   1 
ATOM   1111  C  CB  . THR   A 1 169 ? 21.407  53.627  -14.500 1.00 80.76  ? 238  THR   A CB  1 
ATOM   1112  O  OG1 . THR   A 1 169 ? 20.203  53.040  -15.019 1.00 80.52  ? 238  THR   A OG1 1 
ATOM   1113  C  CG2 . THR   A 1 169 ? 22.279  52.596  -13.826 1.00 71.21  ? 238  THR   A CG2 1 
ATOM   1114  N  N   . SER   A 1 170 ? 20.782  56.241  -15.353 1.00 75.16  ? 239  SER   A N   1 
ATOM   1115  C  CA  . SER   A 1 170 ? 20.164  57.310  -16.112 1.00 78.20  ? 239  SER   A CA  1 
ATOM   1116  C  C   . SER   A 1 170 ? 19.319  56.798  -17.279 1.00 79.37  ? 239  SER   A C   1 
ATOM   1117  O  O   . SER   A 1 170 ? 18.965  57.589  -18.164 1.00 83.67  ? 239  SER   A O   1 
ATOM   1118  C  CB  . SER   A 1 170 ? 21.247  58.287  -16.595 1.00 84.43  ? 239  SER   A CB  1 
ATOM   1119  O  OG  . SER   A 1 170 ? 22.100  57.692  -17.569 1.00 83.34  ? 239  SER   A OG  1 
ATOM   1120  N  N   . TRP   A 1 171 ? 18.982  55.510  -17.292 1.00 82.11  ? 240  TRP   A N   1 
ATOM   1121  C  CA  . TRP   A 1 171 ? 18.210  54.865  -18.343 1.00 75.64  ? 240  TRP   A CA  1 
ATOM   1122  C  C   . TRP   A 1 171 ? 17.058  54.056  -17.773 1.00 79.43  ? 240  TRP   A C   1 
ATOM   1123  O  O   . TRP   A 1 171 ? 17.085  53.643  -16.607 1.00 75.77  ? 240  TRP   A O   1 
ATOM   1124  C  CB  . TRP   A 1 171 ? 19.091  53.934  -19.177 1.00 77.68  ? 240  TRP   A CB  1 
ATOM   1125  C  CG  . TRP   A 1 171 ? 20.154  54.654  -19.898 1.00 77.67  ? 240  TRP   A CG  1 
ATOM   1126  C  CD1 . TRP   A 1 171 ? 21.497  54.464  -19.802 1.00 76.47  ? 240  TRP   A CD1 1 
ATOM   1127  C  CD2 . TRP   A 1 171 ? 19.965  55.694  -20.842 1.00 82.14  ? 240  TRP   A CD2 1 
ATOM   1128  N  NE1 . TRP   A 1 171 ? 22.162  55.326  -20.634 1.00 77.87  ? 240  TRP   A NE1 1 
ATOM   1129  C  CE2 . TRP   A 1 171 ? 21.236  56.094  -21.285 1.00 82.77  ? 240  TRP   A CE2 1 
ATOM   1130  C  CE3 . TRP   A 1 171 ? 18.838  56.322  -21.370 1.00 84.83  ? 240  TRP   A CE3 1 
ATOM   1131  C  CZ2 . TRP   A 1 171 ? 21.409  57.092  -22.220 1.00 90.36  ? 240  TRP   A CZ2 1 
ATOM   1132  C  CZ3 . TRP   A 1 171 ? 19.009  57.309  -22.288 1.00 86.66  ? 240  TRP   A CZ3 1 
ATOM   1133  C  CH2 . TRP   A 1 171 ? 20.282  57.691  -22.708 1.00 93.61  ? 240  TRP   A CH2 1 
ATOM   1134  N  N   . PRO   A 1 172 ? 16.024  53.801  -18.594 1.00 82.08  ? 241  PRO   A N   1 
ATOM   1135  C  CA  . PRO   A 1 172 ? 14.825  53.085  -18.128 1.00 80.46  ? 241  PRO   A CA  1 
ATOM   1136  C  C   . PRO   A 1 172 ? 14.917  51.593  -18.397 1.00 78.46  ? 241  PRO   A C   1 
ATOM   1137  O  O   . PRO   A 1 172 ? 15.743  51.165  -19.211 1.00 80.37  ? 241  PRO   A O   1 
ATOM   1138  C  CB  . PRO   A 1 172 ? 13.720  53.712  -18.978 1.00 82.83  ? 241  PRO   A CB  1 
ATOM   1139  C  CG  . PRO   A 1 172 ? 14.414  53.931  -20.293 1.00 79.33  ? 241  PRO   A CG  1 
ATOM   1140  C  CD  . PRO   A 1 172 ? 15.853  54.314  -19.963 1.00 77.47  ? 241  PRO   A CD  1 
ATOM   1141  N  N   . ARG   A 1 173 ? 14.041  50.814  -17.747 1.00 77.69  ? 242  ARG   A N   1 
ATOM   1142  C  CA  . ARG   A 1 173 ? 14.108  49.352  -17.825 1.00 76.80  ? 242  ARG   A CA  1 
ATOM   1143  C  C   . ARG   A 1 173 ? 14.028  48.854  -19.271 1.00 79.07  ? 242  ARG   A C   1 
ATOM   1144  O  O   . ARG   A 1 173 ? 14.855  48.047  -19.718 1.00 76.26  ? 242  ARG   A O   1 
ATOM   1145  C  CB  . ARG   A 1 173 ? 12.979  48.735  -16.990 1.00 76.03  ? 242  ARG   A CB  1 
ATOM   1146  C  CG  . ARG   A 1 173 ? 13.225  48.735  -15.502 1.00 82.09  ? 242  ARG   A CG  1 
ATOM   1147  C  CD  . ARG   A 1 173 ? 12.151  47.921  -14.728 1.00 87.64  ? 242  ARG   A CD  1 
ATOM   1148  N  NE  . ARG   A 1 173 ? 11.000  48.722  -14.318 1.00 88.51  ? 242  ARG   A NE  1 
ATOM   1149  C  CZ  . ARG   A 1 173 ? 9.825   48.735  -14.937 1.00 96.44  ? 242  ARG   A CZ  1 
ATOM   1150  N  NH1 . ARG   A 1 173 ? 9.577   47.940  -15.983 1.00 86.61  ? 242  ARG   A NH1 1 
ATOM   1151  N  NH2 . ARG   A 1 173 ? 8.873   49.561  -14.497 1.00 96.19  ? 242  ARG   A NH2 1 
ATOM   1152  N  N   . TRP   A 1 174 ? 13.014  49.311  -20.012 1.00 77.66  ? 243  TRP   A N   1 
ATOM   1153  C  CA  . TRP   A 1 174 ? 12.824  48.861  -21.386 1.00 72.11  ? 243  TRP   A CA  1 
ATOM   1154  C  C   . TRP   A 1 174 ? 14.064  49.081  -22.253 1.00 80.00  ? 243  TRP   A C   1 
ATOM   1155  O  O   . TRP   A 1 174 ? 14.280  48.329  -23.214 1.00 81.01  ? 243  TRP   A O   1 
ATOM   1156  C  CB  . TRP   A 1 174 ? 11.613  49.559  -22.001 1.00 80.07  ? 243  TRP   A CB  1 
ATOM   1157  C  CG  . TRP   A 1 174 ? 11.653  51.088  -21.958 1.00 86.19  ? 243  TRP   A CG  1 
ATOM   1158  C  CD1 . TRP   A 1 174 ? 11.240  51.911  -20.926 1.00 86.49  ? 243  TRP   A CD1 1 
ATOM   1159  C  CD2 . TRP   A 1 174 ? 12.090  51.955  -22.995 1.00 85.89  ? 243  TRP   A CD2 1 
ATOM   1160  N  NE1 . TRP   A 1 174 ? 11.398  53.234  -21.269 1.00 79.21  ? 243  TRP   A NE1 1 
ATOM   1161  C  CE2 . TRP   A 1 174 ? 11.926  53.291  -22.531 1.00 83.54  ? 243  TRP   A CE2 1 
ATOM   1162  C  CE3 . TRP   A 1 174 ? 12.602  51.740  -24.278 1.00 84.96  ? 243  TRP   A CE3 1 
ATOM   1163  C  CZ2 . TRP   A 1 174 ? 12.261  54.398  -23.310 1.00 80.12  ? 243  TRP   A CZ2 1 
ATOM   1164  C  CZ3 . TRP   A 1 174 ? 12.942  52.852  -25.051 1.00 88.30  ? 243  TRP   A CZ3 1 
ATOM   1165  C  CH2 . TRP   A 1 174 ? 12.766  54.159  -24.562 1.00 79.82  ? 243  TRP   A CH2 1 
ATOM   1166  N  N   . LEU   A 1 175 ? 14.886  50.097  -21.962 1.00 80.96  ? 244  LEU   A N   1 
ATOM   1167  C  CA  . LEU   A 1 175 ? 16.123  50.232  -22.731 1.00 82.73  ? 244  LEU   A CA  1 
ATOM   1168  C  C   . LEU   A 1 175 ? 17.033  49.037  -22.479 1.00 79.44  ? 244  LEU   A C   1 
ATOM   1169  O  O   . LEU   A 1 175 ? 17.535  48.407  -23.418 1.00 79.34  ? 244  LEU   A O   1 
ATOM   1170  C  CB  . LEU   A 1 175 ? 16.870  51.531  -22.411 1.00 77.35  ? 244  LEU   A CB  1 
ATOM   1171  C  CG  . LEU   A 1 175 ? 18.161  51.521  -23.253 1.00 75.67  ? 244  LEU   A CG  1 
ATOM   1172  C  CD1 . LEU   A 1 175 ? 17.886  51.199  -24.707 1.00 81.73  ? 244  LEU   A CD1 1 
ATOM   1173  C  CD2 . LEU   A 1 175 ? 18.912  52.810  -23.164 1.00 79.14  ? 244  LEU   A CD2 1 
ATOM   1174  N  N   . TYR   A 1 176 ? 17.234  48.697  -21.208 1.00 76.73  ? 245  TYR   A N   1 
ATOM   1175  C  CA  . TYR   A 1 176 ? 18.107  47.581  -20.882 1.00 79.49  ? 245  TYR   A CA  1 
ATOM   1176  C  C   . TYR   A 1 176 ? 17.613  46.271  -21.499 1.00 83.13  ? 245  TYR   A C   1 
ATOM   1177  O  O   . TYR   A 1 176 ? 18.431  45.407  -21.855 1.00 84.86  ? 245  TYR   A O   1 
ATOM   1178  C  CB  . TYR   A 1 176 ? 18.243  47.467  -19.365 1.00 77.85  ? 245  TYR   A CB  1 
ATOM   1179  C  CG  . TYR   A 1 176 ? 19.064  48.579  -18.757 1.00 73.40  ? 245  TYR   A CG  1 
ATOM   1180  C  CD1 . TYR   A 1 176 ? 20.432  48.656  -18.986 1.00 74.19  ? 245  TYR   A CD1 1 
ATOM   1181  C  CD2 . TYR   A 1 176 ? 18.481  49.545  -17.950 1.00 74.76  ? 245  TYR   A CD2 1 
ATOM   1182  C  CE1 . TYR   A 1 176 ? 21.196  49.659  -18.437 1.00 73.27  ? 245  TYR   A CE1 1 
ATOM   1183  C  CE2 . TYR   A 1 176 ? 19.243  50.563  -17.389 1.00 76.74  ? 245  TYR   A CE2 1 
ATOM   1184  C  CZ  . TYR   A 1 176 ? 20.603  50.617  -17.637 1.00 77.38  ? 245  TYR   A CZ  1 
ATOM   1185  O  OH  . TYR   A 1 176 ? 21.366  51.637  -17.088 1.00 80.00  ? 245  TYR   A OH  1 
ATOM   1186  N  N   . SER   A 1 177 ? 16.294  46.100  -21.656 1.00 78.88  ? 246  SER   A N   1 
ATOM   1187  C  CA  . SER   A 1 177 ? 15.805  44.885  -22.311 1.00 78.50  ? 246  SER   A CA  1 
ATOM   1188  C  C   . SER   A 1 177 ? 16.292  44.790  -23.747 1.00 79.42  ? 246  SER   A C   1 
ATOM   1189  O  O   . SER   A 1 177 ? 16.470  43.686  -24.258 1.00 82.69  ? 246  SER   A O   1 
ATOM   1190  C  CB  . SER   A 1 177 ? 14.275  44.815  -22.289 1.00 76.77  ? 246  SER   A CB  1 
ATOM   1191  O  OG  . SER   A 1 177 ? 13.764  45.230  -21.029 1.00 75.00  ? 246  SER   A OG  1 
ATOM   1192  N  N   . LEU   A 1 178 ? 16.494  45.923  -24.421 1.00 80.41  ? 247  LEU   A N   1 
ATOM   1193  C  CA  . LEU   A 1 178 ? 16.938  45.856  -25.807 1.00 79.77  ? 247  LEU   A CA  1 
ATOM   1194  C  C   . LEU   A 1 178 ? 18.390  45.421  -25.943 1.00 82.06  ? 247  LEU   A C   1 
ATOM   1195  O  O   . LEU   A 1 178 ? 18.861  45.246  -27.076 1.00 83.93  ? 247  LEU   A O   1 
ATOM   1196  C  CB  . LEU   A 1 178 ? 16.742  47.205  -26.496 1.00 80.91  ? 247  LEU   A CB  1 
ATOM   1197  C  CG  . LEU   A 1 178 ? 15.339  47.794  -26.528 1.00 85.86  ? 247  LEU   A CG  1 
ATOM   1198  C  CD1 . LEU   A 1 178 ? 15.378  49.092  -27.348 1.00 86.73  ? 247  LEU   A CD1 1 
ATOM   1199  C  CD2 . LEU   A 1 178 ? 14.311  46.785  -27.063 1.00 82.31  ? 247  LEU   A CD2 1 
ATOM   1200  N  N   . TYR   A 1 179 ? 19.111  45.251  -24.828 1.00 78.84  ? 248  TYR   A N   1 
ATOM   1201  C  CA  . TYR   A 1 179 ? 20.490  44.766  -24.829 1.00 80.37  ? 248  TYR   A CA  1 
ATOM   1202  C  C   . TYR   A 1 179 ? 20.636  43.528  -23.958 1.00 82.50  ? 248  TYR   A C   1 
ATOM   1203  O  O   . TYR   A 1 179 ? 21.765  43.139  -23.609 1.00 84.66  ? 248  TYR   A O   1 
ATOM   1204  C  CB  . TYR   A 1 179 ? 21.474  45.842  -24.356 1.00 81.84  ? 248  TYR   A CB  1 
ATOM   1205  C  CG  . TYR   A 1 179 ? 21.641  47.011  -25.299 1.00 82.03  ? 248  TYR   A CG  1 
ATOM   1206  C  CD1 . TYR   A 1 179 ? 20.837  48.130  -25.194 1.00 79.75  ? 248  TYR   A CD1 1 
ATOM   1207  C  CD2 . TYR   A 1 179 ? 22.613  46.999  -26.291 1.00 87.57  ? 248  TYR   A CD2 1 
ATOM   1208  C  CE1 . TYR   A 1 179 ? 20.989  49.196  -26.055 1.00 86.97  ? 248  TYR   A CE1 1 
ATOM   1209  C  CE2 . TYR   A 1 179 ? 22.771  48.075  -27.165 1.00 86.21  ? 248  TYR   A CE2 1 
ATOM   1210  C  CZ  . TYR   A 1 179 ? 21.955  49.171  -27.043 1.00 88.76  ? 248  TYR   A CZ  1 
ATOM   1211  O  OH  . TYR   A 1 179 ? 22.098  50.252  -27.908 1.00 96.15  ? 248  TYR   A OH  1 
ATOM   1212  N  N   . ASP   A 1 180 ? 19.520  42.920  -23.565 1.00 80.28  ? 249  ASP   A N   1 
ATOM   1213  C  CA  . ASP   A 1 180 ? 19.541  41.784  -22.654 1.00 85.55  ? 249  ASP   A CA  1 
ATOM   1214  C  C   . ASP   A 1 180 ? 19.444  40.500  -23.461 1.00 82.99  ? 249  ASP   A C   1 
ATOM   1215  O  O   . ASP   A 1 180 ? 18.373  40.163  -23.973 1.00 82.57  ? 249  ASP   A O   1 
ATOM   1216  C  CB  . ASP   A 1 180 ? 18.409  41.852  -21.640 1.00 84.09  ? 249  ASP   A CB  1 
ATOM   1217  C  CG  . ASP   A 1 180 ? 18.459  40.698  -20.680 1.00 84.13  ? 249  ASP   A CG  1 
ATOM   1218  O  OD1 . ASP   A 1 180 ? 19.470  40.610  -19.949 1.00 87.06  ? 249  ASP   A OD1 1 
ATOM   1219  O  OD2 . ASP   A 1 180 ? 17.527  39.871  -20.687 1.00 81.56  ? 249  ASP   A OD2 1 
ATOM   1220  N  N   . ALA   A 1 181 ? 20.556  39.767  -23.534 1.00 83.38  ? 250  ALA   A N   1 
ATOM   1221  C  CA  . ALA   A 1 181 ? 20.631  38.596  -24.397 1.00 82.02  ? 250  ALA   A CA  1 
ATOM   1222  C  C   . ALA   A 1 181 ? 19.379  37.720  -24.310 1.00 84.41  ? 250  ALA   A C   1 
ATOM   1223  O  O   . ALA   A 1 181 ? 18.774  37.386  -25.335 1.00 82.52  ? 250  ALA   A O   1 
ATOM   1224  C  CB  . ALA   A 1 181 ? 21.887  37.796  -24.056 1.00 81.14  ? 250  ALA   A CB  1 
ATOM   1225  N  N   . GLU   A 1 182 ? 18.962  37.349  -23.098 1.00 93.52  ? 251  GLU   A N   1 
ATOM   1226  C  CA  . GLU   A 1 182 ? 17.852  36.404  -22.985 1.00 94.84  ? 251  GLU   A CA  1 
ATOM   1227  C  C   . GLU   A 1 182 ? 16.559  36.978  -23.569 1.00 91.99  ? 251  GLU   A C   1 
ATOM   1228  O  O   . GLU   A 1 182 ? 15.766  36.231  -24.156 1.00 90.33  ? 251  GLU   A O   1 
ATOM   1229  C  CB  . GLU   A 1 182 ? 17.658  35.966  -21.525 1.00 98.44  ? 251  GLU   A CB  1 
ATOM   1230  C  CG  . GLU   A 1 182 ? 18.916  35.376  -20.842 1.00 105.01 ? 251  GLU   A CG  1 
ATOM   1231  C  CD  . GLU   A 1 182 ? 18.817  33.866  -20.577 1.00 119.71 ? 251  GLU   A CD  1 
ATOM   1232  O  OE1 . GLU   A 1 182 ? 17.679  33.338  -20.608 1.00 123.03 ? 251  GLU   A OE1 1 
ATOM   1233  O  OE2 . GLU   A 1 182 ? 19.869  33.207  -20.343 1.00 116.28 ? 251  GLU   A OE2 1 
ATOM   1234  N  N   . THR   A 1 183 ? 16.328  38.291  -23.439 1.00 83.65  ? 252  THR   A N   1 
ATOM   1235  C  CA  . THR   A 1 183 ? 15.154  38.878  -24.079 1.00 79.69  ? 252  THR   A CA  1 
ATOM   1236  C  C   . THR   A 1 183 ? 15.298  38.855  -25.593 1.00 81.41  ? 252  THR   A C   1 
ATOM   1237  O  O   . THR   A 1 183 ? 14.383  38.436  -26.316 1.00 76.87  ? 252  THR   A O   1 
ATOM   1238  C  CB  . THR   A 1 183 ? 14.938  40.312  -23.613 1.00 75.95  ? 252  THR   A CB  1 
ATOM   1239  O  OG1 . THR   A 1 183 ? 15.202  40.435  -22.215 1.00 85.75  ? 252  THR   A OG1 1 
ATOM   1240  C  CG2 . THR   A 1 183 ? 13.510  40.696  -23.850 1.00 82.91  ? 252  THR   A CG2 1 
ATOM   1241  N  N   . LEU   A 1 184 ? 16.434  39.343  -26.092 1.00 80.73  ? 253  LEU   A N   1 
ATOM   1242  C  CA  . LEU   A 1 184 ? 16.680  39.322  -27.524 1.00 76.79  ? 253  LEU   A CA  1 
ATOM   1243  C  C   . LEU   A 1 184 ? 16.375  37.956  -28.093 1.00 79.39  ? 253  LEU   A C   1 
ATOM   1244  O  O   . LEU   A 1 184 ? 15.730  37.840  -29.141 1.00 80.64  ? 253  LEU   A O   1 
ATOM   1245  C  CB  . LEU   A 1 184 ? 18.129  39.701  -27.816 1.00 78.88  ? 253  LEU   A CB  1 
ATOM   1246  C  CG  . LEU   A 1 184 ? 18.419  41.186  -27.613 1.00 79.93  ? 253  LEU   A CG  1 
ATOM   1247  C  CD1 . LEU   A 1 184 ? 19.805  41.568  -28.131 1.00 79.28  ? 253  LEU   A CD1 1 
ATOM   1248  C  CD2 . LEU   A 1 184 ? 17.330  42.031  -28.266 1.00 80.98  ? 253  LEU   A CD2 1 
ATOM   1249  N  N   . MET   A 1 185 ? 16.810  36.902  -27.398 1.00 81.91  ? 254  MET   A N   1 
ATOM   1250  C  CA  . MET   A 1 185 ? 16.676  35.563  -27.960 1.00 78.42  ? 254  MET   A CA  1 
ATOM   1251  C  C   . MET   A 1 185 ? 15.221  35.137  -28.029 1.00 77.58  ? 254  MET   A C   1 
ATOM   1252  O  O   . MET   A 1 185 ? 14.801  34.539  -29.024 1.00 81.61  ? 254  MET   A O   1 
ATOM   1253  C  CB  . MET   A 1 185 ? 17.515  34.567  -27.171 1.00 77.01  ? 254  MET   A CB  1 
ATOM   1254  C  CG  . MET   A 1 185 ? 19.019  34.764  -27.425 1.00 77.94  ? 254  MET   A CG  1 
ATOM   1255  S  SD  . MET   A 1 185 ? 20.037  33.516  -26.576 1.00 87.07  ? 254  MET   A SD  1 
ATOM   1256  C  CE  . MET   A 1 185 ? 18.809  32.216  -26.339 1.00 89.23  ? 254  MET   A CE  1 
ATOM   1257  N  N   . ASP   A 1 186 ? 14.427  35.435  -26.997 1.00 79.50  ? 255  ASP   A N   1 
ATOM   1258  C  CA  . ASP   A 1 186 ? 13.021  35.053  -27.086 1.00 80.25  ? 255  ASP   A CA  1 
ATOM   1259  C  C   . ASP   A 1 186 ? 12.345  35.824  -28.209 1.00 84.20  ? 255  ASP   A C   1 
ATOM   1260  O  O   . ASP   A 1 186 ? 11.621  35.229  -29.021 1.00 83.73  ? 255  ASP   A O   1 
ATOM   1261  C  CB  . ASP   A 1 186 ? 12.288  35.260  -25.756 1.00 79.81  ? 255  ASP   A CB  1 
ATOM   1262  C  CG  . ASP   A 1 186 ? 10.957  34.490  -25.689 1.00 87.64  ? 255  ASP   A CG  1 
ATOM   1263  O  OD1 . ASP   A 1 186 ? 10.968  33.231  -25.712 1.00 96.10  ? 255  ASP   A OD1 1 
ATOM   1264  O  OD2 . ASP   A 1 186 ? 9.892   35.140  -25.607 1.00 85.25  ? 255  ASP   A OD2 1 
ATOM   1265  N  N   . ARG   A 1 187 ? 12.614  37.142  -28.299 1.00 85.76  ? 256  ARG   A N   1 
ATOM   1266  C  CA  . ARG   A 1 187 ? 12.150  37.945  -29.436 1.00 82.54  ? 256  ARG   A CA  1 
ATOM   1267  C  C   . ARG   A 1 187 ? 12.407  37.227  -30.762 1.00 79.34  ? 256  ARG   A C   1 
ATOM   1268  O  O   . ARG   A 1 187 ? 11.512  37.115  -31.608 1.00 81.36  ? 256  ARG   A O   1 
ATOM   1269  C  CB  . ARG   A 1 187 ? 12.812  39.327  -29.413 1.00 78.73  ? 256  ARG   A CB  1 
ATOM   1270  C  CG  . ARG   A 1 187 ? 12.051  40.364  -28.595 1.00 77.61  ? 256  ARG   A CG  1 
ATOM   1271  C  CD  . ARG   A 1 187 ? 12.882  41.627  -28.359 1.00 83.67  ? 256  ARG   A CD  1 
ATOM   1272  N  NE  . ARG   A 1 187 ? 12.713  42.640  -29.405 1.00 87.36  ? 256  ARG   A NE  1 
ATOM   1273  C  CZ  . ARG   A 1 187 ? 13.659  43.495  -29.775 1.00 85.26  ? 256  ARG   A CZ  1 
ATOM   1274  N  NH1 . ARG   A 1 187 ? 14.866  43.468  -29.236 1.00 87.27  ? 256  ARG   A NH1 1 
ATOM   1275  N  NH2 . ARG   A 1 187 ? 13.396  44.385  -30.720 1.00 85.75  ? 256  ARG   A NH2 1 
ATOM   1276  N  N   . ILE   A 1 188 ? 13.616  36.698  -30.941 1.00 76.28  ? 257  ILE   A N   1 
ATOM   1277  C  CA  . ILE   A 1 188 ? 13.958  35.999  -32.176 1.00 77.24  ? 257  ILE   A CA  1 
ATOM   1278  C  C   . ILE   A 1 188 ? 13.163  34.704  -32.318 1.00 80.72  ? 257  ILE   A C   1 
ATOM   1279  O  O   . ILE   A 1 188 ? 12.594  34.429  -33.383 1.00 81.53  ? 257  ILE   A O   1 
ATOM   1280  C  CB  . ILE   A 1 188 ? 15.467  35.743  -32.228 1.00 78.58  ? 257  ILE   A CB  1 
ATOM   1281  C  CG1 . ILE   A 1 188 ? 16.207  37.076  -32.199 1.00 76.34  ? 257  ILE   A CG1 1 
ATOM   1282  C  CG2 . ILE   A 1 188 ? 15.832  34.869  -33.427 1.00 74.23  ? 257  ILE   A CG2 1 
ATOM   1283  C  CD1 . ILE   A 1 188 ? 17.652  36.913  -32.578 1.00 77.43  ? 257  ILE   A CD1 1 
ATOM   1284  N  N   . LYS   A 1 189 ? 13.146  33.871  -31.263 1.00 82.94  ? 258  LYS   A N   1 
ATOM   1285  C  CA  . LYS   A 1 189 ? 12.345  32.641  -31.258 1.00 79.84  ? 258  LYS   A CA  1 
ATOM   1286  C  C   . LYS   A 1 189 ? 10.909  32.908  -31.689 1.00 83.49  ? 258  LYS   A C   1 
ATOM   1287  O  O   . LYS   A 1 189 ? 10.348  32.179  -32.515 1.00 83.29  ? 258  LYS   A O   1 
ATOM   1288  C  CB  . LYS   A 1 189 ? 12.322  31.999  -29.865 1.00 81.03  ? 258  LYS   A CB  1 
ATOM   1289  C  CG  . LYS   A 1 189 ? 13.623  31.401  -29.346 1.00 81.86  ? 258  LYS   A CG  1 
ATOM   1290  C  CD  . LYS   A 1 189 ? 13.310  30.277  -28.361 1.00 94.88  ? 258  LYS   A CD  1 
ATOM   1291  C  CE  . LYS   A 1 189 ? 13.561  30.646  -26.902 1.00 98.41  ? 258  LYS   A CE  1 
ATOM   1292  N  NZ  . LYS   A 1 189 ? 13.567  29.386  -26.079 1.00 113.20 ? 258  LYS   A NZ  1 
ATOM   1293  N  N   . LYS   A 1 190 ? 10.282  33.935  -31.105 1.00 81.24  ? 259  LYS   A N   1 
ATOM   1294  C  CA  . LYS   A 1 190 ? 8.868   34.155  -31.370 1.00 81.38  ? 259  LYS   A CA  1 
ATOM   1295  C  C   . LYS   A 1 190 ? 8.630   34.382  -32.853 1.00 86.50  ? 259  LYS   A C   1 
ATOM   1296  O  O   . LYS   A 1 190 ? 7.698   33.811  -33.432 1.00 92.11  ? 259  LYS   A O   1 
ATOM   1297  C  CB  . LYS   A 1 190 ? 8.334   35.320  -30.536 1.00 84.81  ? 259  LYS   A CB  1 
ATOM   1298  C  CG  . LYS   A 1 190 ? 8.310   35.064  -29.027 1.00 84.10  ? 259  LYS   A CG  1 
ATOM   1299  C  CD  . LYS   A 1 190 ? 7.515   33.833  -28.647 1.00 94.54  ? 259  LYS   A CD  1 
ATOM   1300  C  CE  . LYS   A 1 190 ? 8.209   33.085  -27.498 1.00 99.53  ? 259  LYS   A CE  1 
ATOM   1301  N  NZ  . LYS   A 1 190 ? 7.347   31.994  -26.955 1.00 115.06 ? 259  LYS   A NZ  1 
ATOM   1302  N  N   . GLN   A 1 191 ? 9.496   35.171  -33.497 1.00 85.15  ? 260  GLN   A N   1 
ATOM   1303  C  CA  . GLN   A 1 191 ? 9.382   35.362  -34.938 1.00 86.86  ? 260  GLN   A CA  1 
ATOM   1304  C  C   . GLN   A 1 191 ? 9.628   34.050  -35.668 1.00 88.11  ? 260  GLN   A C   1 
ATOM   1305  O  O   . GLN   A 1 191 ? 8.780   33.577  -36.423 1.00 90.65  ? 260  GLN   A O   1 
ATOM   1306  C  CB  . GLN   A 1 191 ? 10.342  36.458  -35.397 1.00 86.32  ? 260  GLN   A CB  1 
ATOM   1307  C  CG  . GLN   A 1 191 ? 9.933   37.783  -34.799 1.00 92.62  ? 260  GLN   A CG  1 
ATOM   1308  C  CD  . GLN   A 1 191 ? 10.698  38.969  -35.325 1.00 91.34  ? 260  GLN   A CD  1 
ATOM   1309  O  OE1 . GLN   A 1 191 ? 11.068  39.041  -36.503 1.00 90.82  ? 260  GLN   A OE1 1 
ATOM   1310  N  NE2 . GLN   A 1 191 ? 10.934  39.925  -34.442 1.00 95.34  ? 260  GLN   A NE2 1 
ATOM   1311  N  N   . LEU   A 1 192 ? 10.768  33.416  -35.407 1.00 83.26  ? 261  LEU   A N   1 
ATOM   1312  C  CA  . LEU   A 1 192 ? 11.050  32.129  -36.018 1.00 82.11  ? 261  LEU   A CA  1 
ATOM   1313  C  C   . LEU   A 1 192 ? 9.914   31.121  -35.826 1.00 90.64  ? 261  LEU   A C   1 
ATOM   1314  O  O   . LEU   A 1 192 ? 9.853   30.127  -36.560 1.00 93.90  ? 261  LEU   A O   1 
ATOM   1315  C  CB  . LEU   A 1 192 ? 12.355  31.584  -35.452 1.00 80.92  ? 261  LEU   A CB  1 
ATOM   1316  C  CG  . LEU   A 1 192 ? 13.646  32.153  -36.027 1.00 76.25  ? 261  LEU   A CG  1 
ATOM   1317  C  CD1 . LEU   A 1 192 ? 14.806  31.685  -35.168 1.00 80.18  ? 261  LEU   A CD1 1 
ATOM   1318  C  CD2 . LEU   A 1 192 ? 13.822  31.690  -37.455 1.00 79.19  ? 261  LEU   A CD2 1 
ATOM   1319  N  N   . ARG   A 1 193 ? 9.008   31.344  -34.867 1.00 88.84  ? 262  ARG   A N   1 
ATOM   1320  C  CA  . ARG   A 1 193 ? 7.913   30.400  -34.694 1.00 89.61  ? 262  ARG   A CA  1 
ATOM   1321  C  C   . ARG   A 1 193 ? 6.769   30.671  -35.655 1.00 96.01  ? 262  ARG   A C   1 
ATOM   1322  O  O   . ARG   A 1 193 ? 6.060   29.737  -36.036 1.00 103.63 ? 262  ARG   A O   1 
ATOM   1323  C  CB  . ARG   A 1 193 ? 7.404   30.420  -33.255 1.00 96.53  ? 262  ARG   A CB  1 
ATOM   1324  C  CG  . ARG   A 1 193 ? 6.987   29.023  -32.783 1.00 106.12 ? 262  ARG   A CG  1 
ATOM   1325  C  CD  . ARG   A 1 193 ? 5.974   29.052  -31.652 1.00 110.36 ? 262  ARG   A CD  1 
ATOM   1326  N  NE  . ARG   A 1 193 ? 6.473   29.758  -30.475 1.00 116.07 ? 262  ARG   A NE  1 
ATOM   1327  C  CZ  . ARG   A 1 193 ? 7.401   29.286  -29.645 1.00 121.01 ? 262  ARG   A CZ  1 
ATOM   1328  N  NH1 . ARG   A 1 193 ? 8.024   28.137  -29.873 1.00 118.75 ? 262  ARG   A NH1 1 
ATOM   1329  N  NH2 . ARG   A 1 193 ? 7.704   29.977  -28.550 1.00 119.42 ? 262  ARG   A NH2 1 
ATOM   1330  N  N   . GLU   A 1 194 ? 6.564   31.935  -36.047 1.00 103.76 ? 263  GLU   A N   1 
ATOM   1331  C  CA  . GLU   A 1 194 ? 5.657   32.251  -37.142 1.00 105.39 ? 263  GLU   A CA  1 
ATOM   1332  C  C   . GLU   A 1 194 ? 6.096   31.606  -38.465 1.00 104.41 ? 263  GLU   A C   1 
ATOM   1333  O  O   . GLU   A 1 194 ? 5.323   31.607  -39.426 1.00 103.14 ? 263  GLU   A O   1 
ATOM   1334  C  CB  . GLU   A 1 194 ? 5.537   33.776  -37.264 1.00 105.40 ? 263  GLU   A CB  1 
ATOM   1335  C  CG  . GLU   A 1 194 ? 6.808   34.462  -37.749 1.00 107.12 ? 263  GLU   A CG  1 
ATOM   1336  C  CD  . GLU   A 1 194 ? 6.733   35.988  -37.684 1.00 115.19 ? 263  GLU   A CD  1 
ATOM   1337  O  OE1 . GLU   A 1 194 ? 7.598   36.689  -38.313 1.00 112.67 ? 263  GLU   A OE1 1 
ATOM   1338  O  OE2 . GLU   A 1 194 ? 5.792   36.476  -37.010 1.00 120.49 ? 263  GLU   A OE2 1 
ATOM   1339  N  N   . TRP   A 1 195 ? 7.312   31.055  -38.538 1.00 97.71  ? 264  TRP   A N   1 
ATOM   1340  C  CA  . TRP   A 1 195 ? 7.822   30.336  -39.702 1.00 93.74  ? 264  TRP   A CA  1 
ATOM   1341  C  C   . TRP   A 1 195 ? 7.828   28.834  -39.525 1.00 99.29  ? 264  TRP   A C   1 
ATOM   1342  O  O   . TRP   A 1 195 ? 8.094   28.122  -40.497 1.00 99.02  ? 264  TRP   A O   1 
ATOM   1343  C  CB  . TRP   A 1 195 ? 9.260   30.774  -40.014 1.00 89.11  ? 264  TRP   A CB  1 
ATOM   1344  C  CG  . TRP   A 1 195 ? 9.398   32.169  -40.416 1.00 84.40  ? 264  TRP   A CG  1 
ATOM   1345  C  CD1 . TRP   A 1 195 ? 8.391   33.048  -40.660 1.00 89.01  ? 264  TRP   A CD1 1 
ATOM   1346  C  CD2 . TRP   A 1 195 ? 10.620  32.888  -40.612 1.00 81.90  ? 264  TRP   A CD2 1 
ATOM   1347  N  NE1 . TRP   A 1 195 ? 8.905   34.280  -41.003 1.00 88.83  ? 264  TRP   A NE1 1 
ATOM   1348  C  CE2 . TRP   A 1 195 ? 10.274  34.207  -40.979 1.00 86.42  ? 264  TRP   A CE2 1 
ATOM   1349  C  CE3 . TRP   A 1 195 ? 11.971  32.550  -40.514 1.00 81.59  ? 264  TRP   A CE3 1 
ATOM   1350  C  CZ2 . TRP   A 1 195 ? 11.234  35.189  -41.253 1.00 86.77  ? 264  TRP   A CZ2 1 
ATOM   1351  C  CZ3 . TRP   A 1 195 ? 12.930  33.540  -40.785 1.00 84.42  ? 264  TRP   A CZ3 1 
ATOM   1352  C  CH2 . TRP   A 1 195 ? 12.554  34.837  -41.151 1.00 81.67  ? 264  TRP   A CH2 1 
ATOM   1353  N  N   . ASP   A 1 196 ? 7.640   28.367  -38.293 1.00 103.40 ? 265  ASP   A N   1 
ATOM   1354  C  CA  . ASP   A 1 196 ? 7.700   26.907  -38.024 1.00 104.01 ? 265  ASP   A CA  1 
ATOM   1355  C  C   . ASP   A 1 196 ? 7.046   26.611  -36.684 1.00 109.60 ? 265  ASP   A C   1 
ATOM   1356  O  O   . ASP   A 1 196 ? 7.777   26.538  -35.682 1.00 113.58 ? 265  ASP   A O   1 
ATOM   1357  C  CB  . ASP   A 1 196 ? 9.121   26.372  -37.996 1.00 103.46 ? 265  ASP   A CB  1 
ATOM   1358  C  CG  . ASP   A 1 196 ? 9.250   24.860  -38.112 1.00 108.69 ? 265  ASP   A CG  1 
ATOM   1359  O  OD1 . ASP   A 1 196 ? 8.208   24.193  -38.271 1.00 112.36 ? 265  ASP   A OD1 1 
ATOM   1360  O  OD2 . ASP   A 1 196 ? 10.391  24.362  -38.046 1.00 107.75 ? 265  ASP   A OD2 1 
ATOM   1361  N  N   . GLU   A 1 197 ? 5.723   26.475  -36.662 1.00 118.80 ? 266  GLU   A N   1 
ATOM   1362  C  CA  . GLU   A 1 197 ? 5.071   26.054  -35.399 1.00 122.40 ? 266  GLU   A CA  1 
ATOM   1363  C  C   . GLU   A 1 197 ? 5.783   24.710  -35.243 1.00 126.35 ? 266  GLU   A C   1 
ATOM   1364  O  O   . GLU   A 1 197 ? 5.578   23.830  -36.101 1.00 125.80 ? 266  GLU   A O   1 
ATOM   1365  C  CB  . GLU   A 1 197 ? 3.555   26.041  -35.569 1.00 123.01 ? 266  GLU   A CB  1 
ATOM   1366  C  CG  . GLU   A 1 197 ? 3.051   27.099  -36.546 1.00 127.19 ? 266  GLU   A CG  1 
ATOM   1367  C  CD  . GLU   A 1 197 ? 3.076   28.517  -36.008 1.00 126.59 ? 266  GLU   A CD  1 
ATOM   1368  O  OE1 . GLU   A 1 197 ? 3.004   28.690  -34.775 1.00 134.21 ? 266  GLU   A OE1 1 
ATOM   1369  O  OE2 . GLU   A 1 197 ? 3.169   29.452  -36.829 1.00 118.99 ? 266  GLU   A OE2 1 
ATOM   1370  N  N   . ASN   A 1 198 ? 6.602   24.568  -34.201 1.00 127.97 ? 267  ASN   A N   1 
ATOM   1371  C  CA  . ASN   A 1 198 ? 7.422   23.337  -34.098 1.00 130.04 ? 267  ASN   A CA  1 
ATOM   1372  C  C   . ASN   A 1 198 ? 8.075   23.232  -32.723 1.00 136.93 ? 267  ASN   A C   1 
ATOM   1373  O  O   . ASN   A 1 198 ? 7.336   23.148  -31.722 1.00 142.79 ? 267  ASN   A O   1 
ATOM   1374  C  CB  . ASN   A 1 198 ? 8.527   23.152  -35.123 1.00 128.73 ? 267  ASN   A CB  1 
ATOM   1375  C  CG  . ASN   A 1 198 ? 8.355   21.887  -35.922 1.00 130.67 ? 267  ASN   A CG  1 
ATOM   1376  O  OD1 . ASN   A 1 198 ? 7.247   21.589  -36.381 1.00 132.43 ? 267  ASN   A OD1 1 
ATOM   1377  N  ND2 . ASN   A 1 198 ? 9.436   21.141  -36.097 1.00 128.69 ? 267  ASN   A ND2 1 
ATOM   1378  N  N   . LEU   A 1 199 ? 9.407   23.281  -32.661 1.00 130.61 ? 268  LEU   A N   1 
ATOM   1379  C  CA  . LEU   A 1 199 ? 10.085  23.060  -31.357 1.00 125.56 ? 268  LEU   A CA  1 
ATOM   1380  C  C   . LEU   A 1 199 ? 10.408  24.397  -30.685 1.00 124.57 ? 268  LEU   A C   1 
ATOM   1381  O  O   . LEU   A 1 199 ? 10.109  25.447  -31.287 1.00 132.98 ? 268  LEU   A O   1 
ATOM   1382  C  CB  . LEU   A 1 199 ? 11.342  22.220  -31.560 1.00 124.29 ? 268  LEU   A CB  1 
ATOM   1383  N  N   . LYS   A 1 200 ? 10.997  24.344  -29.489 1.00 121.56 ? 269  LYS   A N   1 
ATOM   1384  C  CA  . LYS   A 1 200 ? 11.321  25.576  -28.726 1.00 127.72 ? 269  LYS   A CA  1 
ATOM   1385  C  C   . LYS   A 1 200 ? 12.367  25.220  -27.671 1.00 126.82 ? 269  LYS   A C   1 
ATOM   1386  O  O   . LYS   A 1 200 ? 12.727  26.100  -26.862 1.00 118.56 ? 269  LYS   A O   1 
ATOM   1387  C  CB  . LYS   A 1 200 ? 10.086  26.118  -28.004 1.00 125.89 ? 269  LYS   A CB  1 
ATOM   1388  N  N   . ASP   A 1 201 ? 12.826  23.972  -27.688 1.00 134.61 ? 270  ASP   A N   1 
ATOM   1389  C  CA  . ASP   A 1 201 ? 13.789  23.505  -26.662 1.00 140.12 ? 270  ASP   A CA  1 
ATOM   1390  C  C   . ASP   A 1 201 ? 15.191  23.534  -27.253 1.00 139.97 ? 270  ASP   A C   1 
ATOM   1391  O  O   . ASP   A 1 201 ? 15.586  24.578  -27.806 1.00 130.69 ? 270  ASP   A O   1 
ATOM   1392  C  CB  . ASP   A 1 201 ? 13.456  22.095  -26.208 1.00 144.07 ? 270  ASP   A CB  1 
ATOM   1393  C  CG  . ASP   A 1 201 ? 13.125  21.111  -27.322 1.00 149.88 ? 270  ASP   A CG  1 
ATOM   1394  O  OD1 . ASP   A 1 201 ? 13.320  21.470  -28.503 1.00 151.97 ? 270  ASP   A OD1 1 
ATOM   1395  O  OD2 . ASP   A 1 201 ? 12.686  19.989  -26.997 1.00 152.26 ? 270  ASP   A OD2 1 
ATOM   1396  N  N   . ASP   A 1 202 ? 15.882  22.398  -27.194 1.00 174.13 ? 271  ASP   A N   1 
ATOM   1397  C  CA  . ASP   A 1 202 ? 17.239  22.302  -27.788 1.00 174.69 ? 271  ASP   A CA  1 
ATOM   1398  C  C   . ASP   A 1 202 ? 17.138  22.694  -29.259 1.00 173.13 ? 271  ASP   A C   1 
ATOM   1399  O  O   . ASP   A 1 202 ? 18.197  22.936  -29.873 1.00 173.10 ? 271  ASP   A O   1 
ATOM   1400  C  CB  . ASP   A 1 202 ? 17.836  20.923  -27.566 1.00 184.35 ? 271  ASP   A CB  1 
ATOM   1401  C  CG  . ASP   A 1 202 ? 18.237  20.621  -26.130 1.00 189.53 ? 271  ASP   A CG  1 
ATOM   1402  O  OD1 . ASP   A 1 202 ? 18.321  21.577  -25.332 1.00 189.27 ? 271  ASP   A OD1 1 
ATOM   1403  O  OD2 . ASP   A 1 202 ? 18.468  19.433  -25.823 1.00 195.41 ? 271  ASP   A OD2 1 
ATOM   1404  N  N   . SER   A 1 203 ? 15.925  22.696  -29.812 1.00 140.40 ? 272  SER   A N   1 
ATOM   1405  C  CA  . SER   A 1 203 ? 15.747  23.191  -31.193 1.00 130.78 ? 272  SER   A CA  1 
ATOM   1406  C  C   . SER   A 1 203 ? 16.774  24.291  -31.457 1.00 122.04 ? 272  SER   A C   1 
ATOM   1407  O  O   . SER   A 1 203 ? 17.380  24.299  -32.548 1.00 116.15 ? 272  SER   A O   1 
ATOM   1408  C  CB  . SER   A 1 203 ? 14.386  23.766  -31.344 1.00 128.55 ? 272  SER   A CB  1 
ATOM   1409  O  OG  . SER   A 1 203 ? 14.220  24.287  -32.654 1.00 126.49 ? 272  SER   A OG  1 
ATOM   1410  N  N   . LEU   A 1 204 ? 16.958  25.175  -30.474 1.00 116.32 ? 273  LEU   A N   1 
ATOM   1411  C  CA  . LEU   A 1 204 ? 17.916  26.285  -30.660 1.00 104.64 ? 273  LEU   A CA  1 
ATOM   1412  C  C   . LEU   A 1 204 ? 18.827  26.243  -29.428 1.00 96.40  ? 273  LEU   A C   1 
ATOM   1413  O  O   . LEU   A 1 204 ? 18.362  25.815  -28.358 1.00 101.20 ? 273  LEU   A O   1 
ATOM   1414  C  CB  . LEU   A 1 204 ? 17.179  27.613  -30.793 1.00 103.45 ? 273  LEU   A CB  1 
ATOM   1415  C  CG  . LEU   A 1 204 ? 16.616  27.928  -32.180 1.00 94.66  ? 273  LEU   A CG  1 
ATOM   1416  C  CD1 . LEU   A 1 204 ? 15.353  28.756  -32.042 1.00 87.22  ? 273  LEU   A CD1 1 
ATOM   1417  C  CD2 . LEU   A 1 204 ? 17.656  28.668  -32.999 1.00 90.87  ? 273  LEU   A CD2 1 
ATOM   1418  N  N   . PRO   A 1 205 ? 20.103  26.660  -29.541 1.00 89.49  ? 274  PRO   A N   1 
ATOM   1419  C  CA  . PRO   A 1 205 ? 21.017  26.629  -28.411 1.00 88.92  ? 274  PRO   A CA  1 
ATOM   1420  C  C   . PRO   A 1 205 ? 20.641  27.590  -27.294 1.00 95.35  ? 274  PRO   A C   1 
ATOM   1421  O  O   . PRO   A 1 205 ? 19.773  28.455  -27.498 1.00 95.14  ? 274  PRO   A O   1 
ATOM   1422  C  CB  . PRO   A 1 205 ? 22.338  27.016  -29.072 1.00 83.91  ? 274  PRO   A CB  1 
ATOM   1423  C  CG  . PRO   A 1 205 ? 22.134  26.717  -30.535 1.00 87.48  ? 274  PRO   A CG  1 
ATOM   1424  C  CD  . PRO   A 1 205 ? 20.705  27.149  -30.762 1.00 92.14  ? 274  PRO   A CD  1 
ATOM   1425  N  N   . SER   A 1 206 ? 21.285  27.451  -26.131 1.00 95.20  ? 275  SER   A N   1 
ATOM   1426  C  CA  . SER   A 1 206 ? 20.986  28.309  -24.998 1.00 90.88  ? 275  SER   A CA  1 
ATOM   1427  C  C   . SER   A 1 206 ? 22.042  29.360  -24.814 1.00 93.95  ? 275  SER   A C   1 
ATOM   1428  O  O   . SER   A 1 206 ? 21.789  30.397  -24.191 1.00 97.08  ? 275  SER   A O   1 
ATOM   1429  C  CB  . SER   A 1 206 ? 20.898  27.484  -23.719 1.00 88.12  ? 275  SER   A CB  1 
ATOM   1430  O  OG  . SER   A 1 206 ? 19.719  26.718  -23.748 1.00 94.58  ? 275  SER   A OG  1 
ATOM   1431  N  N   . ASN   A 1 207 ? 23.236  29.104  -25.341 1.00 92.95  ? 276  ASN   A N   1 
ATOM   1432  C  CA  . ASN   A 1 207 ? 24.336  30.095  -25.225 1.00 94.08  ? 276  ASN   A CA  1 
ATOM   1433  C  C   . ASN   A 1 207 ? 24.111  31.191  -26.260 1.00 95.47  ? 276  ASN   A C   1 
ATOM   1434  O  O   . ASN   A 1 207 ? 24.111  30.881  -27.463 1.00 96.92  ? 276  ASN   A O   1 
ATOM   1435  C  CB  . ASN   A 1 207 ? 25.702  29.452  -25.403 1.00 97.11  ? 276  ASN   A CB  1 
ATOM   1436  C  CG  . ASN   A 1 207 ? 26.831  30.454  -25.433 1.00 98.49  ? 276  ASN   A CG  1 
ATOM   1437  O  OD1 . ASN   A 1 207 ? 26.750  31.517  -24.808 1.00 101.89 ? 276  ASN   A OD1 1 
ATOM   1438  N  ND2 . ASN   A 1 207 ? 27.904  30.124  -26.136 1.00 101.68 ? 276  ASN   A ND2 1 
ATOM   1439  N  N   . PRO   A 1 208 ? 23.933  32.457  -25.844 1.00 94.49  ? 277  PRO   A N   1 
ATOM   1440  C  CA  . PRO   A 1 208 ? 23.782  33.539  -26.796 1.00 87.94  ? 277  PRO   A CA  1 
ATOM   1441  C  C   . PRO   A 1 208 ? 24.705  33.365  -27.980 1.00 86.89  ? 277  PRO   A C   1 
ATOM   1442  O  O   . PRO   A 1 208 ? 24.241  33.465  -29.124 1.00 87.03  ? 277  PRO   A O   1 
ATOM   1443  C  CB  . PRO   A 1 208 ? 24.192  34.700  -25.909 1.00 87.08  ? 277  PRO   A CB  1 
ATOM   1444  C  CG  . PRO   A 1 208 ? 23.571  34.361  -24.583 1.00 88.70  ? 277  PRO   A CG  1 
ATOM   1445  C  CD  . PRO   A 1 208 ? 23.848  32.877  -24.458 1.00 96.20  ? 277  PRO   A CD  1 
ATOM   1446  N  N   . ILE   A 1 209 ? 25.983  33.103  -27.721 1.00 86.83  ? 278  ILE   A N   1 
ATOM   1447  C  CA  . ILE   A 1 209 ? 26.976  33.003  -28.830 1.00 91.92  ? 278  ILE   A CA  1 
ATOM   1448  C  C   . ILE   A 1 209 ? 26.505  31.945  -29.832 1.00 91.84  ? 278  ILE   A C   1 
ATOM   1449  O  O   . ILE   A 1 209 ? 26.398  32.264  -31.030 1.00 84.75  ? 278  ILE   A O   1 
ATOM   1450  C  CB  . ILE   A 1 209 ? 28.369  32.674  -28.270 1.00 92.65  ? 278  ILE   A CB  1 
ATOM   1451  C  CG1 . ILE   A 1 209 ? 28.740  33.609  -27.125 1.00 97.96  ? 278  ILE   A CG1 1 
ATOM   1452  C  CG2 . ILE   A 1 209 ? 29.419  32.689  -29.378 1.00 87.86  ? 278  ILE   A CG2 1 
ATOM   1453  C  CD1 . ILE   A 1 209 ? 29.998  33.204  -26.381 1.00 92.81  ? 278  ILE   A CD1 1 
ATOM   1454  N  N   . ASP   A 1 210 ? 26.243  30.735  -29.349 1.00 92.15  ? 279  ASP   A N   1 
ATOM   1455  C  CA  . ASP   A 1 210 ? 25.801  29.638  -30.246 1.00 88.37  ? 279  ASP   A CA  1 
ATOM   1456  C  C   . ASP   A 1 210 ? 24.512  30.068  -30.950 1.00 86.18  ? 279  ASP   A C   1 
ATOM   1457  O  O   . ASP   A 1 210 ? 24.475  30.041  -32.191 1.00 89.24  ? 279  ASP   A O   1 
ATOM   1458  C  CB  . ASP   A 1 210 ? 25.674  28.339  -29.473 1.00 88.14  ? 279  ASP   A CB  1 
ATOM   1459  C  CG  . ASP   A 1 210 ? 26.898  27.945  -28.662 1.00 96.36  ? 279  ASP   A CG  1 
ATOM   1460  O  OD1 . ASP   A 1 210 ? 27.953  28.581  -28.852 1.00 99.19  ? 279  ASP   A OD1 1 
ATOM   1461  O  OD2 . ASP   A 1 210 ? 26.782  27.007  -27.848 1.00 98.14  ? 279  ASP   A OD2 1 
ATOM   1462  N  N   . PHE   A 1 211 ? 23.499  30.458  -30.180 1.00 78.31  ? 280  PHE   A N   1 
ATOM   1463  C  CA  . PHE   A 1 211 ? 22.233  30.874  -30.780 1.00 81.63  ? 280  PHE   A CA  1 
ATOM   1464  C  C   . PHE   A 1 211 ? 22.430  31.961  -31.832 1.00 86.64  ? 280  PHE   A C   1 
ATOM   1465  O  O   . PHE   A 1 211 ? 21.857  31.894  -32.927 1.00 84.79  ? 280  PHE   A O   1 
ATOM   1466  C  CB  . PHE   A 1 211 ? 21.323  31.364  -29.668 1.00 82.69  ? 280  PHE   A CB  1 
ATOM   1467  C  CG  . PHE   A 1 211 ? 19.922  31.704  -30.086 1.00 79.02  ? 280  PHE   A CG  1 
ATOM   1468  C  CD1 . PHE   A 1 211 ? 19.647  32.885  -30.751 1.00 77.49  ? 280  PHE   A CD1 1 
ATOM   1469  C  CD2 . PHE   A 1 211 ? 18.860  30.895  -29.697 1.00 80.65  ? 280  PHE   A CD2 1 
ATOM   1470  C  CE1 . PHE   A 1 211 ? 18.345  33.221  -31.074 1.00 80.31  ? 280  PHE   A CE1 1 
ATOM   1471  C  CE2 . PHE   A 1 211 ? 17.552  31.232  -30.018 1.00 82.69  ? 280  PHE   A CE2 1 
ATOM   1472  C  CZ  . PHE   A 1 211 ? 17.293  32.394  -30.707 1.00 79.49  ? 280  PHE   A CZ  1 
ATOM   1473  N  N   . SER   A 1 212 ? 23.195  32.998  -31.503 1.00 79.95  ? 281  SER   A N   1 
ATOM   1474  C  CA  . SER   A 1 212 ? 23.499  33.999  -32.509 1.00 80.38  ? 281  SER   A CA  1 
ATOM   1475  C  C   . SER   A 1 212 ? 23.979  33.346  -33.806 1.00 83.98  ? 281  SER   A C   1 
ATOM   1476  O  O   . SER   A 1 212 ? 23.511  33.695  -34.895 1.00 83.83  ? 281  SER   A O   1 
ATOM   1477  C  CB  . SER   A 1 212 ? 24.532  34.989  -31.968 1.00 86.47  ? 281  SER   A CB  1 
ATOM   1478  O  OG  . SER   A 1 212 ? 24.023  35.748  -30.874 1.00 88.78  ? 281  SER   A OG  1 
ATOM   1479  N  N   . TYR   A 1 213 ? 24.883  32.366  -33.714 1.00 85.60  ? 282  TYR   A N   1 
ATOM   1480  C  CA  . TYR   A 1 213 ? 25.469  31.825  -34.941 1.00 82.72  ? 282  TYR   A CA  1 
ATOM   1481  C  C   . TYR   A 1 213 ? 24.490  30.940  -35.702 1.00 83.18  ? 282  TYR   A C   1 
ATOM   1482  O  O   . TYR   A 1 213 ? 24.545  30.881  -36.934 1.00 83.02  ? 282  TYR   A O   1 
ATOM   1483  C  CB  . TYR   A 1 213 ? 26.763  31.068  -34.638 1.00 81.50  ? 282  TYR   A CB  1 
ATOM   1484  C  CG  . TYR   A 1 213 ? 27.955  31.997  -34.500 1.00 87.15  ? 282  TYR   A CG  1 
ATOM   1485  C  CD1 . TYR   A 1 213 ? 28.291  32.887  -35.513 1.00 84.94  ? 282  TYR   A CD1 1 
ATOM   1486  C  CD2 . TYR   A 1 213 ? 28.725  32.010  -33.342 1.00 92.28  ? 282  TYR   A CD2 1 
ATOM   1487  C  CE1 . TYR   A 1 213 ? 29.370  33.749  -35.385 1.00 85.85  ? 282  TYR   A CE1 1 
ATOM   1488  C  CE2 . TYR   A 1 213 ? 29.809  32.873  -33.203 1.00 85.44  ? 282  TYR   A CE2 1 
ATOM   1489  C  CZ  . TYR   A 1 213 ? 30.123  33.736  -34.224 1.00 85.80  ? 282  TYR   A CZ  1 
ATOM   1490  O  OH  . TYR   A 1 213 ? 31.195  34.591  -34.083 1.00 89.60  ? 282  TYR   A OH  1 
ATOM   1491  N  N   . ARG   A 1 214 ? 23.592  30.249  -35.000 1.00 83.31  ? 283  ARG   A N   1 
ATOM   1492  C  CA  . ARG   A 1 214 ? 22.581  29.450  -35.691 1.00 85.97  ? 283  ARG   A CA  1 
ATOM   1493  C  C   . ARG   A 1 214 ? 21.669  30.341  -36.525 1.00 80.80  ? 283  ARG   A C   1 
ATOM   1494  O  O   . ARG   A 1 214 ? 21.477  30.108  -37.721 1.00 83.26  ? 283  ARG   A O   1 
ATOM   1495  C  CB  . ARG   A 1 214 ? 21.767  28.624  -34.679 1.00 89.42  ? 283  ARG   A CB  1 
ATOM   1496  C  CG  . ARG   A 1 214 ? 20.601  27.790  -35.264 1.00 93.32  ? 283  ARG   A CG  1 
ATOM   1497  C  CD  . ARG   A 1 214 ? 21.084  26.525  -35.957 1.00 94.46  ? 283  ARG   A CD  1 
ATOM   1498  N  NE  . ARG   A 1 214 ? 21.813  25.701  -35.006 1.00 102.03 ? 283  ARG   A NE  1 
ATOM   1499  C  CZ  . ARG   A 1 214 ? 21.228  24.932  -34.096 1.00 103.73 ? 283  ARG   A CZ  1 
ATOM   1500  N  NH1 . ARG   A 1 214 ? 19.908  24.824  -34.028 1.00 104.98 ? 283  ARG   A NH1 1 
ATOM   1501  N  NH2 . ARG   A 1 214 ? 21.984  24.270  -33.221 1.00 96.55  ? 283  ARG   A NH2 1 
ATOM   1502  N  N   . VAL   A 1 215 ? 21.110  31.377  -35.899 1.00 83.96  ? 284  VAL   A N   1 
ATOM   1503  C  CA  . VAL   A 1 215 ? 20.208  32.303  -36.579 1.00 80.69  ? 284  VAL   A CA  1 
ATOM   1504  C  C   . VAL   A 1 215 ? 20.807  32.766  -37.902 1.00 84.92  ? 284  VAL   A C   1 
ATOM   1505  O  O   . VAL   A 1 215 ? 20.144  32.754  -38.948 1.00 84.52  ? 284  VAL   A O   1 
ATOM   1506  C  CB  . VAL   A 1 215 ? 19.896  33.491  -35.655 1.00 77.66  ? 284  VAL   A CB  1 
ATOM   1507  C  CG1 . VAL   A 1 215 ? 19.143  34.570  -36.394 1.00 82.38  ? 284  VAL   A CG1 1 
ATOM   1508  C  CG2 . VAL   A 1 215 ? 19.090  33.009  -34.476 1.00 78.05  ? 284  VAL   A CG2 1 
ATOM   1509  N  N   . ALA   A 1 216 ? 22.083  33.168  -37.873 1.00 83.14  ? 285  ALA   A N   1 
ATOM   1510  C  CA  . ALA   A 1 216 ? 22.749  33.678  -39.071 1.00 80.93  ? 285  ALA   A CA  1 
ATOM   1511  C  C   . ALA   A 1 216 ? 22.755  32.656  -40.204 1.00 88.52  ? 285  ALA   A C   1 
ATOM   1512  O  O   . ALA   A 1 216 ? 22.570  33.015  -41.382 1.00 86.71  ? 285  ALA   A O   1 
ATOM   1513  C  CB  . ALA   A 1 216 ? 24.181  34.081  -38.732 1.00 77.06  ? 285  ALA   A CB  1 
ATOM   1514  N  N   . ALA   A 1 217 ? 22.989  31.378  -39.873 1.00 89.80  ? 286  ALA   A N   1 
ATOM   1515  C  CA  . ALA   A 1 217 ? 23.057  30.352  -40.903 1.00 85.27  ? 286  ALA   A CA  1 
ATOM   1516  C  C   . ALA   A 1 217 ? 21.691  29.862  -41.327 1.00 86.58  ? 286  ALA   A C   1 
ATOM   1517  O  O   . ALA   A 1 217 ? 21.599  29.106  -42.302 1.00 94.31  ? 286  ALA   A O   1 
ATOM   1518  C  CB  . ALA   A 1 217 ? 23.899  29.170  -40.443 1.00 78.60  ? 286  ALA   A CB  1 
ATOM   1519  N  N   . CYS   A 1 218 ? 20.632  30.285  -40.648 1.00 85.88  ? 287  CYS   A N   1 
ATOM   1520  C  CA  . CYS   A 1 218 ? 19.310  29.805  -40.990 1.00 90.55  ? 287  CYS   A CA  1 
ATOM   1521  C  C   . CYS   A 1 218 ? 18.337  30.906  -41.410 1.00 89.88  ? 287  CYS   A C   1 
ATOM   1522  O  O   . CYS   A 1 218 ? 17.220  30.589  -41.842 1.00 91.51  ? 287  CYS   A O   1 
ATOM   1523  C  CB  . CYS   A 1 218 ? 18.732  29.006  -39.820 1.00 96.17  ? 287  CYS   A CB  1 
ATOM   1524  S  SG  . CYS   A 1 218 ? 17.828  30.085  -38.716 1.00 108.12 ? 287  CYS   A SG  1 
ATOM   1525  N  N   . LEU   A 1 219 ? 18.712  32.178  -41.287 1.00 91.43  ? 288  LEU   A N   1 
ATOM   1526  C  CA  . LEU   A 1 219 ? 17.933  33.245  -41.902 1.00 82.87  ? 288  LEU   A CA  1 
ATOM   1527  C  C   . LEU   A 1 219 ? 18.083  33.189  -43.417 1.00 85.55  ? 288  LEU   A C   1 
ATOM   1528  O  O   . LEU   A 1 219 ? 19.152  32.814  -43.920 1.00 90.01  ? 288  LEU   A O   1 
ATOM   1529  C  CB  . LEU   A 1 219 ? 18.405  34.601  -41.416 1.00 80.02  ? 288  LEU   A CB  1 
ATOM   1530  C  CG  . LEU   A 1 219 ? 18.036  34.917  -39.988 1.00 78.21  ? 288  LEU   A CG  1 
ATOM   1531  C  CD1 . LEU   A 1 219 ? 18.663  36.236  -39.551 1.00 76.49  ? 288  LEU   A CD1 1 
ATOM   1532  C  CD2 . LEU   A 1 219 ? 16.516  34.950  -39.898 1.00 78.80  ? 288  LEU   A CD2 1 
ATOM   1533  N  N   . PRO   A 1 220 ? 17.027  33.560  -44.169 1.00 84.04  ? 289  PRO   A N   1 
ATOM   1534  C  CA  . PRO   A 1 220 ? 17.138  33.749  -45.641 1.00 77.53  ? 289  PRO   A CA  1 
ATOM   1535  C  C   . PRO   A 1 220 ? 17.857  35.054  -45.972 1.00 84.95  ? 289  PRO   A C   1 
ATOM   1536  O  O   . PRO   A 1 220 ? 17.278  36.071  -46.378 1.00 91.49  ? 289  PRO   A O   1 
ATOM   1537  C  CB  . PRO   A 1 220 ? 15.676  33.764  -46.095 1.00 78.24  ? 289  PRO   A CB  1 
ATOM   1538  C  CG  . PRO   A 1 220 ? 14.909  34.306  -44.882 1.00 86.24  ? 289  PRO   A CG  1 
ATOM   1539  C  CD  . PRO   A 1 220 ? 15.673  33.831  -43.650 1.00 83.48  ? 289  PRO   A CD  1 
ATOM   1540  N  N   . ILE   A 1 221 ? 19.168  35.063  -45.780 1.00 83.13  ? 290  ILE   A N   1 
ATOM   1541  C  CA  . ILE   A 1 221 ? 19.962  36.238  -46.074 1.00 83.30  ? 290  ILE   A CA  1 
ATOM   1542  C  C   . ILE   A 1 221 ? 21.004  35.847  -47.103 1.00 84.30  ? 290  ILE   A C   1 
ATOM   1543  O  O   . ILE   A 1 221 ? 21.296  34.673  -47.306 1.00 84.89  ? 290  ILE   A O   1 
ATOM   1544  C  CB  . ILE   A 1 221 ? 20.602  36.836  -44.805 1.00 86.25  ? 290  ILE   A CB  1 
ATOM   1545  C  CG1 . ILE   A 1 221 ? 21.537  35.824  -44.124 1.00 85.13  ? 290  ILE   A CG1 1 
ATOM   1546  C  CG2 . ILE   A 1 221 ? 19.513  37.236  -43.861 1.00 83.14  ? 290  ILE   A CG2 1 
ATOM   1547  C  CD1 . ILE   A 1 221 ? 22.013  36.237  -42.741 1.00 81.72  ? 290  ILE   A CD1 1 
ATOM   1548  N  N   . ASP   A 1 222 ? 21.543  36.852  -47.776 1.00 89.33  ? 291  ASP   A N   1 
ATOM   1549  C  CA  . ASP   A 1 222 ? 22.571  36.636  -48.775 1.00 89.02  ? 291  ASP   A CA  1 
ATOM   1550  C  C   . ASP   A 1 222 ? 23.944  36.658  -48.112 1.00 89.26  ? 291  ASP   A C   1 
ATOM   1551  O  O   . ASP   A 1 222 ? 24.079  36.962  -46.927 1.00 92.10  ? 291  ASP   A O   1 
ATOM   1552  C  CB  . ASP   A 1 222 ? 22.482  37.709  -49.846 1.00 95.52  ? 291  ASP   A CB  1 
ATOM   1553  C  CG  . ASP   A 1 222 ? 22.722  39.089  -49.287 1.00 91.88  ? 291  ASP   A CG  1 
ATOM   1554  O  OD1 . ASP   A 1 222 ? 23.024  39.229  -48.074 1.00 89.81  ? 291  ASP   A OD1 1 
ATOM   1555  O  OD2 . ASP   A 1 222 ? 22.599  40.039  -50.075 1.00 95.75  ? 291  ASP   A OD2 1 
ATOM   1556  N  N   . ASP   A 1 223 ? 24.990  36.373  -48.887 1.00 102.57 ? 292  ASP   A N   1 
ATOM   1557  C  CA  . ASP   A 1 223 ? 26.300  36.214  -48.263 1.00 104.90 ? 292  ASP   A CA  1 
ATOM   1558  C  C   . ASP   A 1 223 ? 26.816  37.527  -47.664 1.00 104.14 ? 292  ASP   A C   1 
ATOM   1559  O  O   . ASP   A 1 223 ? 27.549  37.505  -46.668 1.00 105.73 ? 292  ASP   A O   1 
ATOM   1560  C  CB  . ASP   A 1 223 ? 27.301  35.618  -49.263 1.00 109.50 ? 292  ASP   A CB  1 
ATOM   1561  C  CG  . ASP   A 1 223 ? 27.217  34.078  -49.355 1.00 111.91 ? 292  ASP   A CG  1 
ATOM   1562  O  OD1 . ASP   A 1 223 ? 26.363  33.459  -48.665 1.00 110.37 ? 292  ASP   A OD1 1 
ATOM   1563  O  OD2 . ASP   A 1 223 ? 28.013  33.484  -50.124 1.00 114.26 ? 292  ASP   A OD2 1 
ATOM   1564  N  N   . VAL   A 1 224 ? 26.423  38.680  -48.202 1.00 96.45  ? 293  VAL   A N   1 
ATOM   1565  C  CA  . VAL   A 1 224 ? 26.921  39.932  -47.635 1.00 93.13  ? 293  VAL   A CA  1 
ATOM   1566  C  C   . VAL   A 1 224 ? 26.368  40.139  -46.226 1.00 91.58  ? 293  VAL   A C   1 
ATOM   1567  O  O   . VAL   A 1 224 ? 27.130  40.367  -45.279 1.00 93.02  ? 293  VAL   A O   1 
ATOM   1568  C  CB  . VAL   A 1 224 ? 26.613  41.113  -48.572 1.00 88.27  ? 293  VAL   A CB  1 
ATOM   1569  C  CG1 . VAL   A 1 224 ? 27.177  40.822  -49.974 1.00 88.54  ? 293  VAL   A CG1 1 
ATOM   1570  C  CG2 . VAL   A 1 224 ? 25.129  41.369  -48.632 1.00 91.22  ? 293  VAL   A CG2 1 
ATOM   1571  N  N   . LEU   A 1 225 ? 25.043  40.032  -46.055 1.00 91.40  ? 294  LEU   A N   1 
ATOM   1572  C  CA  . LEU   A 1 225 ? 24.468  40.068  -44.711 1.00 87.22  ? 294  LEU   A CA  1 
ATOM   1573  C  C   . LEU   A 1 225 ? 25.160  39.074  -43.796 1.00 87.32  ? 294  LEU   A C   1 
ATOM   1574  O  O   . LEU   A 1 225 ? 25.495  39.394  -42.655 1.00 85.68  ? 294  LEU   A O   1 
ATOM   1575  C  CB  . LEU   A 1 225 ? 22.978  39.767  -44.748 1.00 85.16  ? 294  LEU   A CB  1 
ATOM   1576  C  CG  . LEU   A 1 225 ? 22.108  40.991  -44.901 1.00 87.95  ? 294  LEU   A CG  1 
ATOM   1577  C  CD1 . LEU   A 1 225 ? 20.677  40.636  -44.509 1.00 86.50  ? 294  LEU   A CD1 1 
ATOM   1578  C  CD2 . LEU   A 1 225 ? 22.664  42.136  -44.072 1.00 88.04  ? 294  LEU   A CD2 1 
ATOM   1579  N  N   . ARG   A 1 226 ? 25.345  37.841  -44.264 1.00 87.46  ? 295  ARG   A N   1 
ATOM   1580  C  CA  . ARG   A 1 226 ? 26.077  36.868  -43.469 1.00 84.85  ? 295  ARG   A CA  1 
ATOM   1581  C  C   . ARG   A 1 226 ? 27.417  37.442  -43.015 1.00 88.77  ? 295  ARG   A C   1 
ATOM   1582  O  O   . ARG   A 1 226 ? 27.754  37.413  -41.824 1.00 87.33  ? 295  ARG   A O   1 
ATOM   1583  C  CB  . ARG   A 1 226 ? 26.272  35.580  -44.267 1.00 86.41  ? 295  ARG   A CB  1 
ATOM   1584  C  CG  . ARG   A 1 226 ? 24.996  34.803  -44.481 1.00 86.22  ? 295  ARG   A CG  1 
ATOM   1585  C  CD  . ARG   A 1 226 ? 25.339  33.376  -44.838 1.00 88.53  ? 295  ARG   A CD  1 
ATOM   1586  N  NE  . ARG   A 1 226 ? 24.269  32.442  -44.509 1.00 93.50  ? 295  ARG   A NE  1 
ATOM   1587  C  CZ  . ARG   A 1 226 ? 24.190  31.214  -45.004 1.00 93.60  ? 295  ARG   A CZ  1 
ATOM   1588  N  NH1 . ARG   A 1 226 ? 25.106  30.753  -45.841 1.00 86.50  ? 295  ARG   A NH1 1 
ATOM   1589  N  NH2 . ARG   A 1 226 ? 23.165  30.435  -44.656 1.00 90.75  ? 295  ARG   A NH2 1 
ATOM   1590  N  N   . ILE   A 1 227 ? 28.184  38.008  -43.950 1.00 89.75  ? 296  ILE   A N   1 
ATOM   1591  C  CA  . ILE   A 1 227 ? 29.524  38.488  -43.612 1.00 86.70  ? 296  ILE   A CA  1 
ATOM   1592  C  C   . ILE   A 1 227 ? 29.451  39.587  -42.553 1.00 86.22  ? 296  ILE   A C   1 
ATOM   1593  O  O   . ILE   A 1 227 ? 30.317  39.689  -41.669 1.00 84.87  ? 296  ILE   A O   1 
ATOM   1594  C  CB  . ILE   A 1 227 ? 30.263  38.953  -44.883 1.00 83.57  ? 296  ILE   A CB  1 
ATOM   1595  C  CG1 . ILE   A 1 227 ? 30.462  37.787  -45.836 1.00 85.24  ? 296  ILE   A CG1 1 
ATOM   1596  C  CG2 . ILE   A 1 227 ? 31.607  39.549  -44.529 1.00 84.47  ? 296  ILE   A CG2 1 
ATOM   1597  C  CD1 . ILE   A 1 227 ? 31.682  37.937  -46.712 1.00 87.05  ? 296  ILE   A CD1 1 
ATOM   1598  N  N   . GLN   A 1 228 ? 28.417  40.422  -42.614 1.00 87.17  ? 297  GLN   A N   1 
ATOM   1599  C  CA  . GLN   A 1 228 ? 28.250  41.434  -41.581 1.00 88.13  ? 297  GLN   A CA  1 
ATOM   1600  C  C   . GLN   A 1 228 ? 28.130  40.791  -40.200 1.00 86.40  ? 297  GLN   A C   1 
ATOM   1601  O  O   . GLN   A 1 228 ? 28.865  41.145  -39.271 1.00 87.65  ? 297  GLN   A O   1 
ATOM   1602  C  CB  . GLN   A 1 228 ? 27.032  42.306  -41.894 1.00 91.13  ? 297  GLN   A CB  1 
ATOM   1603  C  CG  . GLN   A 1 228 ? 27.024  42.878  -43.309 1.00 96.53  ? 297  GLN   A CG  1 
ATOM   1604  C  CD  . GLN   A 1 228 ? 26.181  44.150  -43.429 1.00 107.92 ? 297  GLN   A CD  1 
ATOM   1605  O  OE1 . GLN   A 1 228 ? 25.535  44.399  -44.454 1.00 114.45 ? 297  GLN   A OE1 1 
ATOM   1606  N  NE2 . GLN   A 1 228 ? 26.184  44.961  -42.367 1.00 114.54 ? 297  GLN   A NE2 1 
ATOM   1607  N  N   . LEU   A 1 229 ? 27.200  39.845  -40.045 1.00 85.54  ? 298  LEU   A N   1 
ATOM   1608  C  CA  . LEU   A 1 229 ? 27.020  39.196  -38.750 1.00 83.19  ? 298  LEU   A CA  1 
ATOM   1609  C  C   . LEU   A 1 229 ? 28.321  38.551  -38.283 1.00 84.85  ? 298  LEU   A C   1 
ATOM   1610  O  O   . LEU   A 1 229 ? 28.668  38.614  -37.096 1.00 84.61  ? 298  LEU   A O   1 
ATOM   1611  C  CB  . LEU   A 1 229 ? 25.885  38.164  -38.832 1.00 79.68  ? 298  LEU   A CB  1 
ATOM   1612  C  CG  . LEU   A 1 229 ? 24.507  38.656  -39.309 1.00 79.17  ? 298  LEU   A CG  1 
ATOM   1613  C  CD1 . LEU   A 1 229 ? 23.448  37.561  -39.605 1.00 71.88  ? 298  LEU   A CD1 1 
ATOM   1614  C  CD2 . LEU   A 1 229 ? 23.985  39.641  -38.275 1.00 89.56  ? 298  LEU   A CD2 1 
ATOM   1615  N  N   . LEU   A 1 230 ? 29.078  37.949  -39.205 1.00 84.67  ? 299  LEU   A N   1 
ATOM   1616  C  CA  . LEU   A 1 230 ? 30.345  37.346  -38.800 1.00 84.85  ? 299  LEU   A CA  1 
ATOM   1617  C  C   . LEU   A 1 230 ? 31.377  38.390  -38.379 1.00 83.99  ? 299  LEU   A C   1 
ATOM   1618  O  O   . LEU   A 1 230 ? 32.315  38.056  -37.651 1.00 85.70  ? 299  LEU   A O   1 
ATOM   1619  C  CB  . LEU   A 1 230 ? 30.907  36.455  -39.921 1.00 84.18  ? 299  LEU   A CB  1 
ATOM   1620  C  CG  . LEU   A 1 230 ? 30.061  35.210  -40.259 1.00 87.92  ? 299  LEU   A CG  1 
ATOM   1621  C  CD1 . LEU   A 1 230 ? 30.503  34.538  -41.557 1.00 85.42  ? 299  LEU   A CD1 1 
ATOM   1622  C  CD2 . LEU   A 1 230 ? 30.026  34.185  -39.108 1.00 84.59  ? 299  LEU   A CD2 1 
ATOM   1623  N  N   . LYS   A 1 231 ? 31.230  39.640  -38.808 1.00 84.67  ? 300  LYS   A N   1 
ATOM   1624  C  CA  . LYS   A 1 231 ? 32.176  40.679  -38.433 1.00 82.51  ? 300  LYS   A CA  1 
ATOM   1625  C  C   . LYS   A 1 231 ? 31.754  41.425  -37.165 1.00 85.51  ? 300  LYS   A C   1 
ATOM   1626  O  O   . LYS   A 1 231 ? 32.456  42.344  -36.729 1.00 88.27  ? 300  LYS   A O   1 
ATOM   1627  C  CB  . LYS   A 1 231 ? 32.367  41.657  -39.592 1.00 85.29  ? 300  LYS   A CB  1 
ATOM   1628  C  CG  . LYS   A 1 231 ? 32.772  41.003  -40.931 1.00 84.08  ? 300  LYS   A CG  1 
ATOM   1629  C  CD  . LYS   A 1 231 ? 33.761  41.910  -41.666 1.00 91.71  ? 300  LYS   A CD  1 
ATOM   1630  C  CE  . LYS   A 1 231 ? 33.784  41.704  -43.171 1.00 96.38  ? 300  LYS   A CE  1 
ATOM   1631  N  NZ  . LYS   A 1 231 ? 33.035  42.784  -43.895 1.00 93.84  ? 300  LYS   A NZ  1 
ATOM   1632  N  N   . ILE   A 1 232 ? 30.650  41.037  -36.555 1.00 83.65  ? 301  ILE   A N   1 
ATOM   1633  C  CA  . ILE   A 1 232 ? 30.155  41.675  -35.346 1.00 81.02  ? 301  ILE   A CA  1 
ATOM   1634  C  C   . ILE   A 1 232 ? 30.841  41.055  -34.135 1.00 87.09  ? 301  ILE   A C   1 
ATOM   1635  O  O   . ILE   A 1 232 ? 30.990  39.824  -34.039 1.00 85.30  ? 301  ILE   A O   1 
ATOM   1636  C  CB  . ILE   A 1 232 ? 28.625  41.540  -35.278 1.00 85.89  ? 301  ILE   A CB  1 
ATOM   1637  C  CG1 . ILE   A 1 232 ? 27.997  42.320  -36.434 1.00 86.08  ? 301  ILE   A CG1 1 
ATOM   1638  C  CG2 . ILE   A 1 232 ? 28.083  41.945  -33.902 1.00 85.31  ? 301  ILE   A CG2 1 
ATOM   1639  C  CD1 . ILE   A 1 232 ? 26.478  42.247  -36.464 1.00 84.40  ? 301  ILE   A CD1 1 
ATOM   1640  N  N   . GLY   A 1 233 ? 31.249  41.908  -33.193 1.00 88.20  ? 302  GLY   A N   1 
ATOM   1641  C  CA  . GLY   A 1 233 ? 32.155  41.463  -32.153 1.00 88.20  ? 302  GLY   A CA  1 
ATOM   1642  C  C   . GLY   A 1 233 ? 31.511  40.796  -30.957 1.00 90.29  ? 302  GLY   A C   1 
ATOM   1643  O  O   . GLY   A 1 233 ? 32.196  40.105  -30.209 1.00 98.77  ? 302  GLY   A O   1 
ATOM   1644  N  N   . SER   A 1 234 ? 30.213  40.990  -30.737 1.00 88.88  ? 303  SER   A N   1 
ATOM   1645  C  CA  . SER   A 1 234 ? 29.564  40.475  -29.537 1.00 88.93  ? 303  SER   A CA  1 
ATOM   1646  C  C   . SER   A 1 234 ? 28.303  39.692  -29.888 1.00 86.26  ? 303  SER   A C   1 
ATOM   1647  O  O   . SER   A 1 234 ? 27.593  40.039  -30.834 1.00 86.85  ? 303  SER   A O   1 
ATOM   1648  C  CB  . SER   A 1 234 ? 29.214  41.623  -28.592 1.00 87.63  ? 303  SER   A CB  1 
ATOM   1649  O  OG  . SER   A 1 234 ? 28.320  42.525  -29.231 1.00 87.12  ? 303  SER   A OG  1 
ATOM   1650  N  N   . ALA   A 1 235 ? 28.007  38.646  -29.114 1.00 82.24  ? 304  ALA   A N   1 
ATOM   1651  C  CA  . ALA   A 1 235 ? 26.770  37.927  -29.370 1.00 81.78  ? 304  ALA   A CA  1 
ATOM   1652  C  C   . ALA   A 1 235 ? 25.554  38.823  -29.179 1.00 80.69  ? 304  ALA   A C   1 
ATOM   1653  O  O   . ALA   A 1 235 ? 24.549  38.648  -29.870 1.00 84.37  ? 304  ALA   A O   1 
ATOM   1654  C  CB  . ALA   A 1 235 ? 26.678  36.682  -28.487 1.00 84.90  ? 304  ALA   A CB  1 
ATOM   1655  N  N   . ILE   A 1 236 ? 25.620  39.779  -28.252 1.00 82.15  ? 305  ILE   A N   1 
ATOM   1656  C  CA  . ILE   A 1 236 ? 24.488  40.675  -28.025 1.00 80.71  ? 305  ILE   A CA  1 
ATOM   1657  C  C   . ILE   A 1 236 ? 24.282  41.580  -29.226 1.00 78.05  ? 305  ILE   A C   1 
ATOM   1658  O  O   . ILE   A 1 236 ? 23.163  41.736  -29.725 1.00 76.12  ? 305  ILE   A O   1 
ATOM   1659  C  CB  . ILE   A 1 236 ? 24.710  41.501  -26.750 1.00 83.78  ? 305  ILE   A CB  1 
ATOM   1660  C  CG1 . ILE   A 1 236 ? 24.203  40.756  -25.518 1.00 80.67  ? 305  ILE   A CG1 1 
ATOM   1661  C  CG2 . ILE   A 1 236 ? 24.048  42.862  -26.869 1.00 82.17  ? 305  ILE   A CG2 1 
ATOM   1662  C  CD1 . ILE   A 1 236 ? 24.774  41.336  -24.249 1.00 86.22  ? 305  ILE   A CD1 1 
ATOM   1663  N  N   . GLN   A 1 237 ? 25.358  42.221  -29.687 1.00 79.13  ? 306  GLN   A N   1 
ATOM   1664  C  CA  . GLN   A 1 237 ? 25.261  43.061  -30.876 1.00 82.29  ? 306  GLN   A CA  1 
ATOM   1665  C  C   . GLN   A 1 237 ? 24.785  42.263  -32.082 1.00 85.05  ? 306  GLN   A C   1 
ATOM   1666  O  O   . GLN   A 1 237 ? 24.123  42.817  -32.969 1.00 88.56  ? 306  GLN   A O   1 
ATOM   1667  C  CB  . GLN   A 1 237 ? 26.612  43.713  -31.192 1.00 82.35  ? 306  GLN   A CB  1 
ATOM   1668  C  CG  . GLN   A 1 237 ? 27.042  44.821  -30.251 1.00 82.13  ? 306  GLN   A CG  1 
ATOM   1669  C  CD  . GLN   A 1 237 ? 28.444  45.341  -30.557 1.00 86.56  ? 306  GLN   A CD  1 
ATOM   1670  O  OE1 . GLN   A 1 237 ? 29.324  44.600  -31.043 1.00 84.28  ? 306  GLN   A OE1 1 
ATOM   1671  N  NE2 . GLN   A 1 237 ? 28.661  46.627  -30.266 1.00 88.05  ? 306  GLN   A NE2 1 
ATOM   1672  N  N   . ARG   A 1 238 ? 25.132  40.971  -32.147 1.00 82.61  ? 307  ARG   A N   1 
ATOM   1673  C  CA  . ARG   A 1 238 ? 24.770  40.158  -33.304 1.00 81.19  ? 307  ARG   A CA  1 
ATOM   1674  C  C   . ARG   A 1 238 ? 23.300  39.746  -33.263 1.00 81.05  ? 307  ARG   A C   1 
ATOM   1675  O  O   . ARG   A 1 238 ? 22.639  39.686  -34.307 1.00 83.96  ? 307  ARG   A O   1 
ATOM   1676  C  CB  . ARG   A 1 238 ? 25.678  38.930  -33.392 1.00 84.62  ? 307  ARG   A CB  1 
ATOM   1677  C  CG  . ARG   A 1 238 ? 25.954  38.460  -34.832 1.00 83.40  ? 307  ARG   A CG  1 
ATOM   1678  C  CD  . ARG   A 1 238 ? 26.822  37.184  -34.909 1.00 82.61  ? 307  ARG   A CD  1 
ATOM   1679  N  NE  . ARG   A 1 238 ? 28.197  37.409  -34.483 1.00 80.65  ? 307  ARG   A NE  1 
ATOM   1680  C  CZ  . ARG   A 1 238 ? 28.662  37.130  -33.270 1.00 86.87  ? 307  ARG   A CZ  1 
ATOM   1681  N  NH1 . ARG   A 1 238 ? 27.914  36.500  -32.373 1.00 85.74  ? 307  ARG   A NH1 1 
ATOM   1682  N  NH2 . ARG   A 1 238 ? 29.903  37.508  -32.942 1.00 88.32  ? 307  ARG   A NH2 1 
ATOM   1683  N  N   . LEU   A 1 239 ? 22.765  39.465  -32.074 1.00 80.19  ? 308  LEU   A N   1 
ATOM   1684  C  CA  . LEU   A 1 239 ? 21.328  39.219  -31.944 1.00 80.70  ? 308  LEU   A CA  1 
ATOM   1685  C  C   . LEU   A 1 239 ? 20.513  40.463  -32.300 1.00 82.30  ? 308  LEU   A C   1 
ATOM   1686  O  O   . LEU   A 1 239 ? 19.514  40.379  -33.028 1.00 77.49  ? 308  LEU   A O   1 
ATOM   1687  C  CB  . LEU   A 1 239 ? 21.006  38.746  -30.528 1.00 78.80  ? 308  LEU   A CB  1 
ATOM   1688  C  CG  . LEU   A 1 239 ? 21.801  37.508  -30.160 1.00 75.25  ? 308  LEU   A CG  1 
ATOM   1689  C  CD1 . LEU   A 1 239 ? 21.928  37.335  -28.655 1.00 74.39  ? 308  LEU   A CD1 1 
ATOM   1690  C  CD2 . LEU   A 1 239 ? 21.093  36.329  -30.785 1.00 79.80  ? 308  LEU   A CD2 1 
ATOM   1691  N  N   . ARG   A 1 240 ? 20.919  41.632  -31.782 1.00 84.27  ? 309  ARG   A N   1 
ATOM   1692  C  CA  . ARG   A 1 240 ? 20.255  42.881  -32.158 1.00 83.76  ? 309  ARG   A CA  1 
ATOM   1693  C  C   . ARG   A 1 240 ? 20.233  43.035  -33.671 1.00 81.92  ? 309  ARG   A C   1 
ATOM   1694  O  O   . ARG   A 1 240 ? 19.197  43.357  -34.265 1.00 82.26  ? 309  ARG   A O   1 
ATOM   1695  C  CB  . ARG   A 1 240 ? 20.947  44.079  -31.497 1.00 85.97  ? 309  ARG   A CB  1 
ATOM   1696  C  CG  . ARG   A 1 240 ? 20.434  44.384  -30.091 1.00 86.03  ? 309  ARG   A CG  1 
ATOM   1697  C  CD  . ARG   A 1 240 ? 21.261  45.440  -29.363 1.00 80.18  ? 309  ARG   A CD  1 
ATOM   1698  N  NE  . ARG   A 1 240 ? 21.142  46.746  -29.995 1.00 82.45  ? 309  ARG   A NE  1 
ATOM   1699  C  CZ  . ARG   A 1 240 ? 20.079  47.536  -29.899 1.00 88.03  ? 309  ARG   A CZ  1 
ATOM   1700  N  NH1 . ARG   A 1 240 ? 19.033  47.208  -29.159 1.00 91.50  ? 309  ARG   A NH1 1 
ATOM   1701  N  NH2 . ARG   A 1 240 ? 20.054  48.674  -30.583 1.00 94.00  ? 309  ARG   A NH2 1 
ATOM   1702  N  N   . CYS   A 1 241 ? 21.364  42.765  -34.313 1.00 78.08  ? 310  CYS   A N   1 
ATOM   1703  C  CA  . CYS   A 1 241 ? 21.423  42.837  -35.763 1.00 85.80  ? 310  CYS   A CA  1 
ATOM   1704  C  C   . CYS   A 1 241 ? 20.424  41.885  -36.397 1.00 84.12  ? 310  CYS   A C   1 
ATOM   1705  O  O   . CYS   A 1 241 ? 19.541  42.305  -37.155 1.00 82.58  ? 310  CYS   A O   1 
ATOM   1706  C  CB  . CYS   A 1 241 ? 22.836  42.523  -36.251 1.00 91.48  ? 310  CYS   A CB  1 
ATOM   1707  S  SG  . CYS   A 1 241 ? 23.187  43.282  -37.855 1.00 100.72 ? 310  CYS   A SG  1 
ATOM   1708  N  N   . GLU   A 1 242 ? 20.564  40.587  -36.117 1.00 84.80  ? 311  GLU   A N   1 
ATOM   1709  C  CA  . GLU   A 1 242 ? 19.678  39.598  -36.736 1.00 82.91  ? 311  GLU   A CA  1 
ATOM   1710  C  C   . GLU   A 1 242 ? 18.221  39.976  -36.550 1.00 81.54  ? 311  GLU   A C   1 
ATOM   1711  O  O   . GLU   A 1 242 ? 17.394  39.784  -37.451 1.00 80.17  ? 311  GLU   A O   1 
ATOM   1712  C  CB  . GLU   A 1 242 ? 19.947  38.217  -36.159 1.00 78.45  ? 311  GLU   A CB  1 
ATOM   1713  C  CG  . GLU   A 1 242 ? 21.330  37.739  -36.480 1.00 79.90  ? 311  GLU   A CG  1 
ATOM   1714  C  CD  . GLU   A 1 242 ? 21.689  36.522  -35.686 1.00 82.52  ? 311  GLU   A CD  1 
ATOM   1715  O  OE1 . GLU   A 1 242 ? 21.047  36.297  -34.635 1.00 83.52  ? 311  GLU   A OE1 1 
ATOM   1716  O  OE2 . GLU   A 1 242 ? 22.604  35.787  -36.115 1.00 83.99  ? 311  GLU   A OE2 1 
ATOM   1717  N  N   . LEU   A 1 243 ? 17.890  40.529  -35.388 1.00 82.55  ? 312  LEU   A N   1 
ATOM   1718  C  CA  . LEU   A 1 243 ? 16.543  41.043  -35.205 1.00 81.95  ? 312  LEU   A CA  1 
ATOM   1719  C  C   . LEU   A 1 243 ? 16.253  42.152  -36.200 1.00 80.59  ? 312  LEU   A C   1 
ATOM   1720  O  O   . LEU   A 1 243 ? 15.190  42.164  -36.830 1.00 80.83  ? 312  LEU   A O   1 
ATOM   1721  C  CB  . LEU   A 1 243 ? 16.352  41.524  -33.770 1.00 82.80  ? 312  LEU   A CB  1 
ATOM   1722  C  CG  . LEU   A 1 243 ? 15.561  40.554  -32.894 1.00 80.07  ? 312  LEU   A CG  1 
ATOM   1723  C  CD1 . LEU   A 1 243 ? 15.744  40.897  -31.444 1.00 78.49  ? 312  LEU   A CD1 1 
ATOM   1724  C  CD2 . LEU   A 1 243 ? 14.086  40.587  -33.266 1.00 83.53  ? 312  LEU   A CD2 1 
ATOM   1725  N  N   . ASP   A 1 244 ? 17.198  43.079  -36.374 1.00 80.70  ? 313  ASP   A N   1 
ATOM   1726  C  CA  . ASP   A 1 244 ? 16.988  44.170  -37.319 1.00 84.59  ? 313  ASP   A CA  1 
ATOM   1727  C  C   . ASP   A 1 244 ? 16.790  43.644  -38.738 1.00 83.63  ? 313  ASP   A C   1 
ATOM   1728  O  O   . ASP   A 1 244 ? 15.938  44.145  -39.484 1.00 82.76  ? 313  ASP   A O   1 
ATOM   1729  C  CB  . ASP   A 1 244 ? 18.166  45.142  -37.263 1.00 88.59  ? 313  ASP   A CB  1 
ATOM   1730  C  CG  . ASP   A 1 244 ? 17.717  46.577  -37.159 1.00 91.57  ? 313  ASP   A CG  1 
ATOM   1731  O  OD1 . ASP   A 1 244 ? 16.523  46.781  -36.820 1.00 91.23  ? 313  ASP   A OD1 1 
ATOM   1732  O  OD2 . ASP   A 1 244 ? 18.549  47.484  -37.421 1.00 92.76  ? 313  ASP   A OD2 1 
ATOM   1733  N  N   . ILE   A 1 245 ? 17.578  42.641  -39.130 1.00 83.19  ? 314  ILE   A N   1 
ATOM   1734  C  CA  . ILE   A 1 245 ? 17.367  41.983  -40.417 1.00 83.33  ? 314  ILE   A CA  1 
ATOM   1735  C  C   . ILE   A 1 245 ? 15.955  41.422  -40.514 1.00 82.13  ? 314  ILE   A C   1 
ATOM   1736  O  O   . ILE   A 1 245 ? 15.277  41.578  -41.532 1.00 81.74  ? 314  ILE   A O   1 
ATOM   1737  C  CB  . ILE   A 1 245 ? 18.399  40.870  -40.631 1.00 80.40  ? 314  ILE   A CB  1 
ATOM   1738  C  CG1 . ILE   A 1 245 ? 19.814  41.432  -40.570 1.00 87.12  ? 314  ILE   A CG1 1 
ATOM   1739  C  CG2 . ILE   A 1 245 ? 18.131  40.221  -41.936 1.00 76.51  ? 314  ILE   A CG2 1 
ATOM   1740  C  CD1 . ILE   A 1 245 ? 20.856  40.443  -41.087 1.00 82.78  ? 314  ILE   A CD1 1 
ATOM   1741  N  N   . MET   A 1 246 ? 15.511  40.718  -39.475 1.00 82.75  ? 315  MET   A N   1 
ATOM   1742  C  CA  . MET   A 1 246 ? 14.216  40.048  -39.521 1.00 82.37  ? 315  MET   A CA  1 
ATOM   1743  C  C   . MET   A 1 246 ? 13.043  41.010  -39.461 1.00 84.25  ? 315  MET   A C   1 
ATOM   1744  O  O   . MET   A 1 246 ? 11.905  40.589  -39.725 1.00 82.57  ? 315  MET   A O   1 
ATOM   1745  C  CB  . MET   A 1 246 ? 14.093  39.054  -38.378 1.00 82.10  ? 315  MET   A CB  1 
ATOM   1746  C  CG  . MET   A 1 246 ? 15.168  37.975  -38.342 1.00 80.75  ? 315  MET   A CG  1 
ATOM   1747  S  SD  . MET   A 1 246 ? 14.914  37.092  -36.792 1.00 81.86  ? 315  MET   A SD  1 
ATOM   1748  C  CE  . MET   A 1 246 ? 13.150  36.813  -36.924 1.00 77.85  ? 315  MET   A CE  1 
ATOM   1749  N  N   . ASN   A 1 247 ? 13.301  42.280  -39.124 1.00 85.01  ? 316  ASN   A N   1 
ATOM   1750  C  CA  . ASN   A 1 247 ? 12.270  43.299  -38.998 1.00 82.27  ? 316  ASN   A CA  1 
ATOM   1751  C  C   . ASN   A 1 247 ? 12.277  44.311  -40.133 1.00 83.52  ? 316  ASN   A C   1 
ATOM   1752  O  O   . ASN   A 1 247 ? 11.234  44.913  -40.419 1.00 81.70  ? 316  ASN   A O   1 
ATOM   1753  C  CB  . ASN   A 1 247 ? 12.418  44.029  -37.653 1.00 76.64  ? 316  ASN   A CB  1 
ATOM   1754  C  CG  . ASN   A 1 247 ? 11.904  43.195  -36.484 1.00 86.79  ? 316  ASN   A CG  1 
ATOM   1755  O  OD1 . ASN   A 1 247 ? 10.802  42.639  -36.543 1.00 86.39  ? 316  ASN   A OD1 1 
ATOM   1756  N  ND2 . ASN   A 1 247 ? 12.702  43.098  -35.419 1.00 87.41  ? 316  ASN   A ND2 1 
ATOM   1757  N  N   . LYS   A 1 248 ? 13.404  44.483  -40.811 1.00 83.48  ? 317  LYS   A N   1 
ATOM   1758  C  CA  . LYS   A 1 248 ? 13.517  45.483  -41.860 1.00 80.63  ? 317  LYS   A CA  1 
ATOM   1759  C  C   . LYS   A 1 248 ? 13.616  44.893  -43.263 1.00 82.49  ? 317  LYS   A C   1 
ATOM   1760  O  O   . LYS   A 1 248 ? 13.120  45.502  -44.208 1.00 85.26  ? 317  LYS   A O   1 
ATOM   1761  C  CB  . LYS   A 1 248 ? 14.730  46.383  -41.592 1.00 82.71  ? 317  LYS   A CB  1 
ATOM   1762  C  CG  . LYS   A 1 248 ? 14.586  47.209  -40.326 1.00 78.44  ? 317  LYS   A CG  1 
ATOM   1763  C  CD  . LYS   A 1 248 ? 15.344  48.521  -40.433 1.00 81.57  ? 317  LYS   A CD  1 
ATOM   1764  C  CE  . LYS   A 1 248 ? 16.381  48.692  -39.321 1.00 86.56  ? 317  LYS   A CE  1 
ATOM   1765  N  NZ  . LYS   A 1 248 ? 15.760  48.801  -37.969 1.00 88.33  ? 317  LYS   A NZ  1 
ATOM   1766  N  N   . CYS   A 1 249 ? 14.230  43.719  -43.423 1.00 82.99  ? 318  CYS   A N   1 
ATOM   1767  C  CA  . CYS   A 1 249 ? 14.403  43.083  -44.733 1.00 83.72  ? 318  CYS   A CA  1 
ATOM   1768  C  C   . CYS   A 1 249 ? 13.343  42.013  -44.938 1.00 83.91  ? 318  CYS   A C   1 
ATOM   1769  O  O   . CYS   A 1 249 ? 13.597  40.799  -45.029 1.00 88.03  ? 318  CYS   A O   1 
ATOM   1770  C  CB  . CYS   A 1 249 ? 15.795  42.504  -44.856 1.00 85.09  ? 318  CYS   A CB  1 
ATOM   1771  S  SG  . CYS   A 1 249 ? 16.965  43.797  -44.503 1.00 84.43  ? 318  CYS   A SG  1 
ATOM   1772  N  N   . THR   A 1 250 ? 12.136  42.534  -45.012 1.00 84.45  ? 319  THR   A N   1 
ATOM   1773  C  CA  . THR   A 1 250 ? 10.906  41.784  -45.117 1.00 88.19  ? 319  THR   A CA  1 
ATOM   1774  C  C   . THR   A 1 250 ? 10.568  41.380  -46.555 1.00 92.26  ? 319  THR   A C   1 
ATOM   1775  O  O   . THR   A 1 250 ? 9.516   40.768  -46.786 1.00 92.04  ? 319  THR   A O   1 
ATOM   1776  C  CB  . THR   A 1 250 ? 9.797   42.650  -44.547 1.00 84.57  ? 319  THR   A CB  1 
ATOM   1777  O  OG1 . THR   A 1 250 ? 9.475   43.648  -45.518 1.00 88.08  ? 319  THR   A OG1 1 
ATOM   1778  C  CG2 . THR   A 1 250 ? 10.292  43.362  -43.319 1.00 84.26  ? 319  THR   A CG2 1 
ATOM   1779  N  N   . SER   A 1 251 ? 11.407  41.729  -47.528 1.00 93.81  ? 320  SER   A N   1 
ATOM   1780  C  CA  . SER   A 1 251 ? 11.149  41.429  -48.931 1.00 92.64  ? 320  SER   A CA  1 
ATOM   1781  C  C   . SER   A 1 251 ? 12.369  40.756  -49.530 1.00 91.18  ? 320  SER   A C   1 
ATOM   1782  O  O   . SER   A 1 251 ? 13.503  41.151  -49.250 1.00 92.52  ? 320  SER   A O   1 
ATOM   1783  C  CB  . SER   A 1 251 ? 10.816  42.686  -49.722 1.00 92.83  ? 320  SER   A CB  1 
ATOM   1784  O  OG  . SER   A 1 251 ? 9.794   43.419  -49.066 1.00 95.79  ? 320  SER   A OG  1 
ATOM   1785  N  N   . LEU   A 1 252 ? 12.136  39.742  -50.353 1.00 86.41  ? 321  LEU   A N   1 
ATOM   1786  C  CA  . LEU   A 1 252 ? 13.219  38.969  -50.933 1.00 86.16  ? 321  LEU   A CA  1 
ATOM   1787  C  C   . LEU   A 1 252 ? 13.208  39.148  -52.445 1.00 85.51  ? 321  LEU   A C   1 
ATOM   1788  O  O   . LEU   A 1 252 ? 12.207  38.838  -53.103 1.00 84.73  ? 321  LEU   A O   1 
ATOM   1789  C  CB  . LEU   A 1 252 ? 13.093  37.493  -50.534 1.00 82.62  ? 321  LEU   A CB  1 
ATOM   1790  C  CG  . LEU   A 1 252 ? 13.797  37.113  -49.239 1.00 77.09  ? 321  LEU   A CG  1 
ATOM   1791  C  CD1 . LEU   A 1 252 ? 13.309  37.969  -48.077 1.00 89.72  ? 321  LEU   A CD1 1 
ATOM   1792  C  CD2 . LEU   A 1 252 ? 13.546  35.671  -48.950 1.00 78.96  ? 321  LEU   A CD2 1 
ATOM   1793  N  N   . CYS   A 1 253 ? 14.319  39.638  -52.995 1.00 80.78  ? 322  CYS   A N   1 
ATOM   1794  C  CA  . CYS   A 1 253 ? 14.415  39.916  -54.418 1.00 81.76  ? 322  CYS   A CA  1 
ATOM   1795  C  C   . CYS   A 1 253 ? 15.430  39.018  -55.109 1.00 82.82  ? 322  CYS   A C   1 
ATOM   1796  O  O   . CYS   A 1 253 ? 16.250  38.362  -54.468 1.00 82.42  ? 322  CYS   A O   1 
ATOM   1797  C  CB  . CYS   A 1 253 ? 14.776  41.377  -54.645 1.00 83.67  ? 322  CYS   A CB  1 
ATOM   1798  S  SG  . CYS   A 1 253 ? 13.615  42.423  -53.796 1.00 90.65  ? 322  CYS   A SG  1 
ATOM   1799  N  N   . CYS   A 1 254 ? 15.339  38.996  -56.440 1.00 82.87  ? 323  CYS   A N   1 
ATOM   1800  C  CA  . CYS   A 1 254 ? 16.363  38.396  -57.279 1.00 84.30  ? 323  CYS   A CA  1 
ATOM   1801  C  C   . CYS   A 1 254 ? 17.707  39.073  -57.052 1.00 85.79  ? 323  CYS   A C   1 
ATOM   1802  O  O   . CYS   A 1 254 ? 17.890  40.238  -57.404 1.00 92.60  ? 323  CYS   A O   1 
ATOM   1803  C  CB  . CYS   A 1 254 ? 15.947  38.514  -58.742 1.00 85.12  ? 323  CYS   A CB  1 
ATOM   1804  S  SG  . CYS   A 1 254 ? 17.230  38.115  -59.956 1.00 82.72  ? 323  CYS   A SG  1 
ATOM   1805  N  N   . LYS   A 1 255 ? 18.648  38.341  -56.453 1.00 85.74  ? 324  LYS   A N   1 
ATOM   1806  C  CA  . LYS   A 1 255 ? 19.982  38.880  -56.226 1.00 86.04  ? 324  LYS   A CA  1 
ATOM   1807  C  C   . LYS   A 1 255 ? 20.627  39.370  -57.521 1.00 91.23  ? 324  LYS   A C   1 
ATOM   1808  O  O   . LYS   A 1 255 ? 21.434  40.302  -57.496 1.00 95.45  ? 324  LYS   A O   1 
ATOM   1809  C  CB  . LYS   A 1 255 ? 20.860  37.814  -55.572 1.00 85.95  ? 324  LYS   A CB  1 
ATOM   1810  C  CG  . LYS   A 1 255 ? 22.003  38.378  -54.782 1.00 86.45  ? 324  LYS   A CG  1 
ATOM   1811  C  CD  . LYS   A 1 255 ? 23.303  37.655  -55.063 1.00 93.42  ? 324  LYS   A CD  1 
ATOM   1812  C  CE  . LYS   A 1 255 ? 24.431  38.407  -54.379 1.00 98.88  ? 324  LYS   A CE  1 
ATOM   1813  N  NZ  . LYS   A 1 255 ? 24.416  39.871  -54.741 1.00 107.45 ? 324  LYS   A NZ  1 
ATOM   1814  N  N   . GLN   A 1 256 ? 20.280  38.769  -58.658 1.00 99.70  ? 325  GLN   A N   1 
ATOM   1815  C  CA  . GLN   A 1 256 ? 20.986  39.001  -59.916 1.00 100.12 ? 325  GLN   A CA  1 
ATOM   1816  C  C   . GLN   A 1 256 ? 20.596  40.293  -60.613 1.00 99.77  ? 325  GLN   A C   1 
ATOM   1817  O  O   . GLN   A 1 256 ? 21.473  41.037  -61.061 1.00 103.11 ? 325  GLN   A O   1 
ATOM   1818  C  CB  . GLN   A 1 256 ? 20.771  37.816  -60.862 1.00 102.17 ? 325  GLN   A CB  1 
ATOM   1819  C  CG  . GLN   A 1 256 ? 21.725  36.701  -60.528 1.00 105.31 ? 325  GLN   A CG  1 
ATOM   1820  C  CD  . GLN   A 1 256 ? 23.050  37.286  -60.142 1.00 108.72 ? 325  GLN   A CD  1 
ATOM   1821  O  OE1 . GLN   A 1 256 ? 23.611  38.098  -60.890 1.00 115.14 ? 325  GLN   A OE1 1 
ATOM   1822  N  NE2 . GLN   A 1 256 ? 23.551  36.918  -58.958 1.00 106.71 ? 325  GLN   A NE2 1 
ATOM   1823  N  N   . CYS   A 1 257 ? 19.305  40.570  -60.756 1.00 93.80  ? 326  CYS   A N   1 
ATOM   1824  C  CA  . CYS   A 1 257 ? 18.883  41.800  -61.406 1.00 95.08  ? 326  CYS   A CA  1 
ATOM   1825  C  C   . CYS   A 1 257 ? 18.323  42.814  -60.432 1.00 94.39  ? 326  CYS   A C   1 
ATOM   1826  O  O   . CYS   A 1 257 ? 18.053  43.947  -60.834 1.00 102.15 ? 326  CYS   A O   1 
ATOM   1827  C  CB  . CYS   A 1 257 ? 17.826  41.512  -62.472 1.00 96.68  ? 326  CYS   A CB  1 
ATOM   1828  S  SG  . CYS   A 1 257 ? 16.306  41.003  -61.677 1.00 93.78  ? 326  CYS   A SG  1 
ATOM   1829  N  N   . GLN   A 1 258 ? 18.095  42.428  -59.182 1.00 94.84  ? 327  GLN   A N   1 
ATOM   1830  C  CA  . GLN   A 1 258 ? 17.796  43.374  -58.112 1.00 97.93  ? 327  GLN   A CA  1 
ATOM   1831  C  C   . GLN   A 1 258 ? 16.486  44.121  -58.319 1.00 100.25 ? 327  GLN   A C   1 
ATOM   1832  O  O   . GLN   A 1 258 ? 16.093  44.941  -57.483 1.00 100.95 ? 327  GLN   A O   1 
ATOM   1833  C  CB  . GLN   A 1 258 ? 18.923  44.391  -57.983 1.00 95.60  ? 327  GLN   A CB  1 
ATOM   1834  C  CG  . GLN   A 1 258 ? 19.945  44.100  -56.936 1.00 97.28  ? 327  GLN   A CG  1 
ATOM   1835  C  CD  . GLN   A 1 258 ? 20.732  45.349  -56.625 1.00 104.49 ? 327  GLN   A CD  1 
ATOM   1836  O  OE1 . GLN   A 1 258 ? 20.208  46.462  -56.756 1.00 100.26 ? 327  GLN   A OE1 1 
ATOM   1837  N  NE2 . GLN   A 1 258 ? 22.000  45.185  -56.236 1.00 103.25 ? 327  GLN   A NE2 1 
ATOM   1838  N  N   . GLU   A 1 259 ? 15.806  43.880  -59.427 1.00 106.23 ? 328  GLU   A N   1 
ATOM   1839  C  CA  . GLU   A 1 259 ? 14.605  44.625  -59.752 1.00 109.43 ? 328  GLU   A CA  1 
ATOM   1840  C  C   . GLU   A 1 259 ? 13.463  43.625  -59.933 1.00 105.92 ? 328  GLU   A C   1 
ATOM   1841  O  O   . GLU   A 1 259 ? 12.830  43.543  -60.985 1.00 107.72 ? 328  GLU   A O   1 
ATOM   1842  C  CB  . GLU   A 1 259 ? 14.829  45.513  -60.991 1.00 111.79 ? 328  GLU   A CB  1 
ATOM   1843  N  N   . THR   A 1 260 ? 13.225  42.827  -58.893 1.00 95.43  ? 329  THR   A N   1 
ATOM   1844  C  CA  . THR   A 1 260 ? 12.186  41.804  -58.931 1.00 96.90  ? 329  THR   A CA  1 
ATOM   1845  C  C   . THR   A 1 260 ? 11.956  41.216  -57.552 1.00 90.65  ? 329  THR   A C   1 
ATOM   1846  O  O   . THR   A 1 260 ? 12.763  40.434  -57.039 1.00 87.20  ? 329  THR   A O   1 
ATOM   1847  C  CB  . THR   A 1 260 ? 12.522  40.668  -59.904 1.00 95.02  ? 329  THR   A CB  1 
ATOM   1848  O  OG1 . THR   A 1 260 ? 12.906  41.216  -61.167 1.00 96.73  ? 329  THR   A OG1 1 
ATOM   1849  C  CG2 . THR   A 1 260 ? 11.302  39.711  -60.074 1.00 89.84  ? 329  THR   A CG2 1 
ATOM   1850  N  N   . GLU   A 1 261 ? 10.849  41.598  -56.949 1.00 91.18  ? 330  GLU   A N   1 
ATOM   1851  C  CA  . GLU   A 1 261 ? 10.502  41.110  -55.634 1.00 89.95  ? 330  GLU   A CA  1 
ATOM   1852  C  C   . GLU   A 1 261 ? 9.861   39.754  -55.824 1.00 89.52  ? 330  GLU   A C   1 
ATOM   1853  O  O   . GLU   A 1 261 ? 8.915   39.615  -56.611 1.00 93.09  ? 330  GLU   A O   1 
ATOM   1854  C  CB  . GLU   A 1 261 ? 9.569   42.096  -54.939 1.00 96.61  ? 330  GLU   A CB  1 
ATOM   1855  C  CG  . GLU   A 1 261 ? 9.225   41.751  -53.529 1.00 94.43  ? 330  GLU   A CG  1 
ATOM   1856  C  CD  . GLU   A 1 261 ? 8.524   42.886  -52.845 1.00 100.09 ? 330  GLU   A CD  1 
ATOM   1857  O  OE1 . GLU   A 1 261 ? 7.744   43.606  -53.515 1.00 105.48 ? 330  GLU   A OE1 1 
ATOM   1858  O  OE2 . GLU   A 1 261 ? 8.771   43.072  -51.641 1.00 104.79 ? 330  GLU   A OE2 1 
ATOM   1859  N  N   . ILE   A 1 262 ? 10.415  38.753  -55.152 1.00 88.78  ? 331  ILE   A N   1 
ATOM   1860  C  CA  . ILE   A 1 262 ? 9.957   37.383  -55.312 1.00 88.80  ? 331  ILE   A CA  1 
ATOM   1861  C  C   . ILE   A 1 262 ? 8.870   37.054  -54.304 1.00 91.11  ? 331  ILE   A C   1 
ATOM   1862  O  O   . ILE   A 1 262 ? 7.803   36.550  -54.671 1.00 90.66  ? 331  ILE   A O   1 
ATOM   1863  C  CB  . ILE   A 1 262 ? 11.149  36.406  -55.185 1.00 89.74  ? 331  ILE   A CB  1 
ATOM   1864  C  CG1 . ILE   A 1 262 ? 12.247  36.727  -56.205 1.00 84.25  ? 331  ILE   A CG1 1 
ATOM   1865  C  CG2 . ILE   A 1 262 ? 10.673  34.971  -55.353 1.00 88.51  ? 331  ILE   A CG2 1 
ATOM   1866  C  CD1 . ILE   A 1 262 ? 11.730  36.905  -57.597 1.00 81.62  ? 331  ILE   A CD1 1 
ATOM   1867  N  N   . THR   A 1 263 ? 9.127   37.353  -53.032 1.00 90.30  ? 332  THR   A N   1 
ATOM   1868  C  CA  . THR   A 1 263 ? 8.260   36.901  -51.955 1.00 90.99  ? 332  THR   A CA  1 
ATOM   1869  C  C   . THR   A 1 263 ? 8.504   37.762  -50.722 1.00 95.68  ? 332  THR   A C   1 
ATOM   1870  O  O   . THR   A 1 263 ? 9.509   38.478  -50.614 1.00 91.82  ? 332  THR   A O   1 
ATOM   1871  C  CB  . THR   A 1 263 ? 8.494   35.425  -51.646 1.00 86.03  ? 332  THR   A CB  1 
ATOM   1872  O  OG1 . THR   A 1 263 ? 7.361   34.897  -50.944 1.00 88.14  ? 332  THR   A OG1 1 
ATOM   1873  C  CG2 . THR   A 1 263 ? 9.749   35.276  -50.804 1.00 84.64  ? 332  THR   A CG2 1 
ATOM   1874  N  N   . THR   A 1 264 ? 7.561   37.678  -49.785 1.00 99.66  ? 333  THR   A N   1 
ATOM   1875  C  CA  . THR   A 1 264 ? 7.525   38.556  -48.626 1.00 96.14  ? 333  THR   A CA  1 
ATOM   1876  C  C   . THR   A 1 264 ? 7.566   37.722  -47.355 1.00 95.15  ? 333  THR   A C   1 
ATOM   1877  O  O   . THR   A 1 264 ? 7.110   36.576  -47.340 1.00 96.02  ? 333  THR   A O   1 
ATOM   1878  C  CB  . THR   A 1 264 ? 6.275   39.413  -48.630 1.00 96.89  ? 333  THR   A CB  1 
ATOM   1879  O  OG1 . THR   A 1 264 ? 5.131   38.554  -48.626 1.00 103.32 ? 333  THR   A OG1 1 
ATOM   1880  C  CG2 . THR   A 1 264 ? 6.226   40.251  -49.888 1.00 97.47  ? 333  THR   A CG2 1 
ATOM   1881  N  N   . LYS   A 1 265 ? 8.103   38.319  -46.286 1.00 89.55  ? 334  LYS   A N   1 
ATOM   1882  C  CA  . LYS   A 1 265 ? 8.332   37.584  -45.049 1.00 89.36  ? 334  LYS   A CA  1 
ATOM   1883  C  C   . LYS   A 1 265 ? 7.114   36.760  -44.657 1.00 91.78  ? 334  LYS   A C   1 
ATOM   1884  O  O   . LYS   A 1 265 ? 7.247   35.591  -44.278 1.00 92.86  ? 334  LYS   A O   1 
ATOM   1885  C  CB  . LYS   A 1 265 ? 8.715   38.565  -43.935 1.00 94.44  ? 334  LYS   A CB  1 
ATOM   1886  C  CG  . LYS   A 1 265 ? 8.850   37.961  -42.541 1.00 95.22  ? 334  LYS   A CG  1 
ATOM   1887  C  CD  . LYS   A 1 265 ? 9.316   38.999  -41.526 1.00 95.82  ? 334  LYS   A CD  1 
ATOM   1888  C  CE  . LYS   A 1 265 ? 9.239   38.450  -40.103 1.00 97.64  ? 334  LYS   A CE  1 
ATOM   1889  N  NZ  . LYS   A 1 265 ? 9.515   39.553  -39.155 1.00 93.86  ? 334  LYS   A NZ  1 
ATOM   1890  N  N   . ASN   A 1 266 ? 5.913   37.335  -44.782 1.00 90.05  ? 335  ASN   A N   1 
ATOM   1891  C  CA  . ASN   A 1 266 ? 4.717   36.683  -44.257 1.00 90.74  ? 335  ASN   A CA  1 
ATOM   1892  C  C   . ASN   A 1 266 ? 4.482   35.321  -44.880 1.00 94.00  ? 335  ASN   A C   1 
ATOM   1893  O  O   . ASN   A 1 266 ? 3.914   34.432  -44.233 1.00 99.55  ? 335  ASN   A O   1 
ATOM   1894  C  CB  . ASN   A 1 266 ? 3.509   37.565  -44.489 1.00 94.33  ? 335  ASN   A CB  1 
ATOM   1895  C  CG  . ASN   A 1 266 ? 3.785   38.975  -44.138 1.00 108.36 ? 335  ASN   A CG  1 
ATOM   1896  O  OD1 . ASN   A 1 266 ? 4.365   39.249  -43.080 1.00 113.13 ? 335  ASN   A OD1 1 
ATOM   1897  N  ND2 . ASN   A 1 266 ? 3.401   39.897  -45.023 1.00 111.32 ? 335  ASN   A ND2 1 
ATOM   1898  N  N   . GLU   A 1 267 ? 4.902   35.137  -46.114 1.00 90.66  ? 336  GLU   A N   1 
ATOM   1899  C  CA  . GLU   A 1 267 ? 4.629   33.906  -46.826 1.00 92.00  ? 336  GLU   A CA  1 
ATOM   1900  C  C   . GLU   A 1 267 ? 5.574   32.773  -46.450 1.00 90.11  ? 336  GLU   A C   1 
ATOM   1901  O  O   . GLU   A 1 267 ? 5.517   31.714  -47.085 1.00 93.47  ? 336  GLU   A O   1 
ATOM   1902  C  CB  . GLU   A 1 267 ? 4.682   34.157  -48.340 1.00 91.28  ? 336  GLU   A CB  1 
ATOM   1903  C  CG  . GLU   A 1 267 ? 3.910   35.403  -48.797 1.00 95.24  ? 336  GLU   A CG  1 
ATOM   1904  C  CD  . GLU   A 1 267 ? 2.439   35.138  -49.134 1.00 98.59  ? 336  GLU   A CD  1 
ATOM   1905  O  OE1 . GLU   A 1 267 ? 2.048   33.947  -49.208 1.00 100.67 ? 336  GLU   A OE1 1 
ATOM   1906  O  OE2 . GLU   A 1 267 ? 1.674   36.122  -49.334 1.00 93.11  ? 336  GLU   A OE2 1 
ATOM   1907  N  N   . ILE   A 1 268 ? 6.433   32.934  -45.448 1.00 85.95  ? 337  ILE   A N   1 
ATOM   1908  C  CA  . ILE   A 1 268 ? 7.339   31.846  -45.091 1.00 87.19  ? 337  ILE   A CA  1 
ATOM   1909  C  C   . ILE   A 1 268 ? 6.615   30.864  -44.180 1.00 91.46  ? 337  ILE   A C   1 
ATOM   1910  O  O   . ILE   A 1 268 ? 5.914   31.261  -43.240 1.00 92.71  ? 337  ILE   A O   1 
ATOM   1911  C  CB  . ILE   A 1 268 ? 8.614   32.387  -44.422 1.00 85.95  ? 337  ILE   A CB  1 
ATOM   1912  C  CG1 . ILE   A 1 268 ? 9.579   32.949  -45.470 1.00 82.66  ? 337  ILE   A CG1 1 
ATOM   1913  C  CG2 . ILE   A 1 268 ? 9.269   31.290  -43.575 1.00 87.19  ? 337  ILE   A CG2 1 
ATOM   1914  C  CD1 . ILE   A 1 268 ? 10.822  33.559  -44.899 1.00 76.02  ? 337  ILE   A CD1 1 
ATOM   1915  N  N   . PHE   A 1 269 ? 6.784   29.573  -44.458 1.00 91.01  ? 338  PHE   A N   1 
ATOM   1916  C  CA  . PHE   A 1 269 ? 6.250   28.517  -43.606 1.00 91.84  ? 338  PHE   A CA  1 
ATOM   1917  C  C   . PHE   A 1 269 ? 7.210   27.329  -43.666 1.00 91.74  ? 338  PHE   A C   1 
ATOM   1918  O  O   . PHE   A 1 269 ? 8.222   27.363  -44.370 1.00 89.67  ? 338  PHE   A O   1 
ATOM   1919  C  CB  . PHE   A 1 269 ? 4.833   28.136  -44.039 1.00 95.63  ? 338  PHE   A CB  1 
ATOM   1920  C  CG  . PHE   A 1 269 ? 4.796   27.245  -45.238 1.00 99.17  ? 338  PHE   A CG  1 
ATOM   1921  C  CD1 . PHE   A 1 269 ? 5.103   27.747  -46.500 1.00 98.89  ? 338  PHE   A CD1 1 
ATOM   1922  C  CD2 . PHE   A 1 269 ? 4.474   25.899  -45.112 1.00 100.63 ? 338  PHE   A CD2 1 
ATOM   1923  C  CE1 . PHE   A 1 269 ? 5.083   26.917  -47.624 1.00 96.23  ? 338  PHE   A CE1 1 
ATOM   1924  C  CE2 . PHE   A 1 269 ? 4.452   25.063  -46.231 1.00 99.88  ? 338  PHE   A CE2 1 
ATOM   1925  C  CZ  . PHE   A 1 269 ? 4.752   25.573  -47.483 1.00 96.98  ? 338  PHE   A CZ  1 
ATOM   1926  N  N   . SER   A 1 270 ? 6.907   26.274  -42.906 1.00 97.97  ? 339  SER   A N   1 
ATOM   1927  C  CA  . SER   A 1 270 ? 7.717   25.054  -42.905 1.00 98.64  ? 339  SER   A CA  1 
ATOM   1928  C  C   . SER   A 1 270 ? 6.843   23.895  -43.335 1.00 101.01 ? 339  SER   A C   1 
ATOM   1929  O  O   . SER   A 1 270 ? 5.779   23.673  -42.749 1.00 102.40 ? 339  SER   A O   1 
ATOM   1930  C  CB  . SER   A 1 270 ? 8.327   24.768  -41.532 1.00 96.93  ? 339  SER   A CB  1 
ATOM   1931  O  OG  . SER   A 1 270 ? 9.320   25.731  -41.205 1.00 99.23  ? 339  SER   A OG  1 
ATOM   1932  N  N   . LEU   A 1 271 ? 7.254   23.188  -44.387 1.00 103.47 ? 340  LEU   A N   1 
ATOM   1933  C  CA  . LEU   A 1 271 ? 6.408   22.096  -44.932 1.00 107.14 ? 340  LEU   A CA  1 
ATOM   1934  C  C   . LEU   A 1 271 ? 6.358   20.963  -43.906 1.00 110.14 ? 340  LEU   A C   1 
ATOM   1935  O  O   . LEU   A 1 271 ? 5.246   20.511  -43.571 1.00 112.61 ? 340  LEU   A O   1 
ATOM   1936  C  CB  . LEU   A 1 271 ? 6.966   21.612  -46.267 1.00 102.51 ? 340  LEU   A CB  1 
ATOM   1937  C  CG  . LEU   A 1 271 ? 6.239   20.434  -46.922 1.00 98.78  ? 340  LEU   A CG  1 
ATOM   1938  C  CD1 . LEU   A 1 271 ? 4.811   20.814  -47.268 1.00 111.78 ? 340  LEU   A CD1 1 
ATOM   1939  C  CD2 . LEU   A 1 271 ? 6.965   19.924  -48.153 1.00 99.82  ? 340  LEU   A CD2 1 
ATOM   1940  N  N   . SER   A 1 272 ? 7.525   20.530  -43.435 1.00 106.96 ? 341  SER   A N   1 
ATOM   1941  C  CA  . SER   A 1 272 ? 7.563   19.476  -42.395 1.00 114.91 ? 341  SER   A CA  1 
ATOM   1942  C  C   . SER   A 1 272 ? 8.358   19.985  -41.193 1.00 117.09 ? 341  SER   A C   1 
ATOM   1943  O  O   . SER   A 1 272 ? 8.801   21.148  -41.226 1.00 116.28 ? 341  SER   A O   1 
ATOM   1944  C  CB  . SER   A 1 272 ? 8.172   18.219  -42.931 1.00 124.38 ? 341  SER   A CB  1 
ATOM   1945  O  OG  . SER   A 1 272 ? 9.508   18.065  -42.469 1.00 129.16 ? 341  SER   A OG  1 
ATOM   1946  N  N   . LEU   A 1 273 ? 8.540   19.134  -40.188 1.00 117.86 ? 342  LEU   A N   1 
ATOM   1947  C  CA  . LEU   A 1 273 ? 9.370   19.512  -39.021 1.00 121.97 ? 342  LEU   A CA  1 
ATOM   1948  C  C   . LEU   A 1 273 ? 10.652  20.170  -39.526 1.00 122.50 ? 342  LEU   A C   1 
ATOM   1949  O  O   . LEU   A 1 273 ? 10.951  21.289  -39.065 1.00 120.18 ? 342  LEU   A O   1 
ATOM   1950  C  CB  . LEU   A 1 273 ? 9.668   18.216  -38.277 1.00 126.46 ? 342  LEU   A CB  1 
ATOM   1951  C  CG  . LEU   A 1 273 ? 8.452   17.513  -37.666 1.00 126.60 ? 342  LEU   A CG  1 
ATOM   1952  C  CD1 . LEU   A 1 273 ? 8.830   16.167  -37.077 1.00 115.92 ? 342  LEU   A CD1 1 
ATOM   1953  C  CD2 . LEU   A 1 273 ? 7.774   18.387  -36.627 1.00 128.28 ? 342  LEU   A CD2 1 
ATOM   1954  N  N   . CYS   A 1 274 ? 11.366  19.497  -40.430 1.00 121.94 ? 343  CYS   A N   1 
ATOM   1955  C  CA  . CYS   A 1 274 ? 12.630  20.022  -41.010 1.00 119.87 ? 343  CYS   A CA  1 
ATOM   1956  C  C   . CYS   A 1 274 ? 12.865  21.492  -40.639 1.00 115.96 ? 343  CYS   A C   1 
ATOM   1957  O  O   . CYS   A 1 274 ? 13.810  21.762  -39.871 1.00 110.42 ? 343  CYS   A O   1 
ATOM   1958  C  CB  . CYS   A 1 274 ? 12.591  19.900  -42.527 1.00 119.23 ? 343  CYS   A CB  1 
ATOM   1959  S  SG  . CYS   A 1 274 ? 11.124  20.649  -43.285 1.00 126.23 ? 343  CYS   A SG  1 
ATOM   1960  N  N   . GLY   A 1 275 ? 12.059  22.401  -41.187 1.00 108.79 ? 344  GLY   A N   1 
ATOM   1961  C  CA  . GLY   A 1 275 ? 12.259  23.839  -40.944 1.00 105.16 ? 344  GLY   A CA  1 
ATOM   1962  C  C   . GLY   A 1 275 ? 11.844  24.636  -42.161 1.00 103.65 ? 344  GLY   A C   1 
ATOM   1963  O  O   . GLY   A 1 275 ? 11.371  24.018  -43.135 1.00 103.94 ? 344  GLY   A O   1 
ATOM   1964  N  N   . PRO   A 1 276 ? 11.964  25.979  -42.158 1.00 96.29  ? 345  PRO   A N   1 
ATOM   1965  C  CA  . PRO   A 1 276 ? 11.497  26.807  -43.275 1.00 90.68  ? 345  PRO   A CA  1 
ATOM   1966  C  C   . PRO   A 1 276 ? 12.523  26.971  -44.393 1.00 93.16  ? 345  PRO   A C   1 
ATOM   1967  O  O   . PRO   A 1 276 ? 12.141  27.245  -45.536 1.00 92.01  ? 345  PRO   A O   1 
ATOM   1968  C  CB  . PRO   A 1 276 ? 11.206  28.143  -42.599 1.00 86.89  ? 345  PRO   A CB  1 
ATOM   1969  C  CG  . PRO   A 1 276 ? 12.281  28.227  -41.585 1.00 92.27  ? 345  PRO   A CG  1 
ATOM   1970  C  CD  . PRO   A 1 276 ? 12.496  26.814  -41.070 1.00 96.94  ? 345  PRO   A CD  1 
ATOM   1971  N  N   . MET   A 1 277 ? 13.831  26.810  -44.098 1.00 91.38  ? 346  MET   A N   1 
ATOM   1972  C  CA  . MET   A 1 277 ? 14.858  26.783  -45.147 1.00 84.98  ? 346  MET   A CA  1 
ATOM   1973  C  C   . MET   A 1 277 ? 15.888  25.703  -44.767 1.00 87.12  ? 346  MET   A C   1 
ATOM   1974  O  O   . MET   A 1 277 ? 17.005  25.956  -44.316 1.00 83.50  ? 346  MET   A O   1 
ATOM   1975  C  CB  . MET   A 1 277 ? 15.488  28.160  -45.364 1.00 81.67  ? 346  MET   A CB  1 
ATOM   1976  C  CG  . MET   A 1 277 ? 16.955  28.121  -45.822 1.00 89.32  ? 346  MET   A CG  1 
ATOM   1977  S  SD  . MET   A 1 277 ? 17.834  29.696  -46.112 1.00 91.07  ? 346  MET   A SD  1 
ATOM   1978  C  CE  . MET   A 1 277 ? 17.039  30.728  -44.870 1.00 89.40  ? 346  MET   A CE  1 
ATOM   1979  N  N   . ALA   A 1 278 ? 15.506  24.442  -44.943 1.00 90.97  ? 347  ALA   A N   1 
ATOM   1980  C  CA  . ALA   A 1 278 ? 16.483  23.383  -44.741 1.00 93.77  ? 347  ALA   A CA  1 
ATOM   1981  C  C   . ALA   A 1 278 ? 17.404  23.289  -45.954 1.00 90.68  ? 347  ALA   A C   1 
ATOM   1982  O  O   . ALA   A 1 278 ? 17.188  23.942  -46.991 1.00 87.94  ? 347  ALA   A O   1 
ATOM   1983  C  CB  . ALA   A 1 278 ? 15.792  22.046  -44.473 1.00 91.20  ? 347  ALA   A CB  1 
ATOM   1984  N  N   . ALA   A 1 279 ? 18.436  22.446  -45.829 1.00 88.08  ? 348  ALA   A N   1 
ATOM   1985  C  CA  . ALA   A 1 279 ? 19.333  22.112  -46.932 1.00 84.77  ? 348  ALA   A CA  1 
ATOM   1986  C  C   . ALA   A 1 279 ? 18.933  20.774  -47.550 1.00 86.14  ? 348  ALA   A C   1 
ATOM   1987  O  O   . ALA   A 1 279 ? 18.881  19.761  -46.853 1.00 95.78  ? 348  ALA   A O   1 
ATOM   1988  C  CB  . ALA   A 1 279 ? 20.778  22.055  -46.447 1.00 80.66  ? 348  ALA   A CB  1 
ATOM   1989  N  N   . TYR   A 1 280 ? 18.672  20.763  -48.855 1.00 84.95  ? 349  TYR   A N   1 
ATOM   1990  C  CA  . TYR   A 1 280 ? 18.291  19.554  -49.571 1.00 88.70  ? 349  TYR   A CA  1 
ATOM   1991  C  C   . TYR   A 1 280 ? 19.353  19.248  -50.617 1.00 90.60  ? 349  TYR   A C   1 
ATOM   1992  O  O   . TYR   A 1 280 ? 20.075  20.148  -51.061 1.00 90.36  ? 349  TYR   A O   1 
ATOM   1993  C  CB  . TYR   A 1 280 ? 16.912  19.703  -50.241 1.00 90.70  ? 349  TYR   A CB  1 
ATOM   1994  C  CG  . TYR   A 1 280 ? 15.764  20.054  -49.294 1.00 92.42  ? 349  TYR   A CG  1 
ATOM   1995  C  CD1 . TYR   A 1 280 ? 15.076  19.068  -48.599 1.00 93.20  ? 349  TYR   A CD1 1 
ATOM   1996  C  CD2 . TYR   A 1 280 ? 15.355  21.372  -49.121 1.00 91.98  ? 349  TYR   A CD2 1 
ATOM   1997  C  CE1 . TYR   A 1 280 ? 14.027  19.383  -47.751 1.00 93.42  ? 349  TYR   A CE1 1 
ATOM   1998  C  CE2 . TYR   A 1 280 ? 14.305  21.696  -48.264 1.00 94.58  ? 349  TYR   A CE2 1 
ATOM   1999  C  CZ  . TYR   A 1 280 ? 13.646  20.699  -47.584 1.00 94.85  ? 349  TYR   A CZ  1 
ATOM   2000  O  OH  . TYR   A 1 280 ? 12.616  21.038  -46.735 1.00 95.26  ? 349  TYR   A OH  1 
ATOM   2001  N  N   . VAL   A 1 281 ? 19.460  17.974  -51.007 1.00 94.31  ? 350  VAL   A N   1 
ATOM   2002  C  CA  . VAL   A 1 281 ? 20.485  17.540  -51.954 1.00 95.50  ? 350  VAL   A CA  1 
ATOM   2003  C  C   . VAL   A 1 281 ? 19.832  17.033  -53.228 1.00 97.54  ? 350  VAL   A C   1 
ATOM   2004  O  O   . VAL   A 1 281 ? 18.818  16.328  -53.184 1.00 95.27  ? 350  VAL   A O   1 
ATOM   2005  C  CB  . VAL   A 1 281 ? 21.411  16.454  -51.381 1.00 93.40  ? 350  VAL   A CB  1 
ATOM   2006  C  CG1 . VAL   A 1 281 ? 22.648  16.308  -52.286 1.00 95.00  ? 350  VAL   A CG1 1 
ATOM   2007  C  CG2 . VAL   A 1 281 ? 21.796  16.790  -49.954 1.00 96.35  ? 350  VAL   A CG2 1 
ATOM   2008  N  N   . ASN   A 1 282 ? 20.430  17.381  -54.362 1.00 102.39 ? 351  ASN   A N   1 
ATOM   2009  C  CA  . ASN   A 1 282 ? 19.974  16.904  -55.658 1.00 100.42 ? 351  ASN   A CA  1 
ATOM   2010  C  C   . ASN   A 1 282 ? 20.786  15.687  -56.060 1.00 101.93 ? 351  ASN   A C   1 
ATOM   2011  O  O   . ASN   A 1 282 ? 21.834  15.383  -55.472 1.00 98.99  ? 351  ASN   A O   1 
ATOM   2012  C  CB  . ASN   A 1 282 ? 20.065  18.027  -56.703 1.00 96.16  ? 351  ASN   A CB  1 
ATOM   2013  C  CG  . ASN   A 1 282 ? 21.467  18.202  -57.305 1.00 97.34  ? 351  ASN   A CG  1 
ATOM   2014  O  OD1 . ASN   A 1 282 ? 22.464  17.669  -56.804 1.00 103.47 ? 351  ASN   A OD1 1 
ATOM   2015  N  ND2 . ASN   A 1 282 ? 21.542  18.973  -58.386 1.00 94.37  ? 351  ASN   A ND2 1 
ATOM   2016  N  N   . PRO   A 1 283 ? 20.318  14.959  -57.075 1.00 104.55 ? 352  PRO   A N   1 
ATOM   2017  C  CA  . PRO   A 1 283 ? 20.992  13.717  -57.464 1.00 102.70 ? 352  PRO   A CA  1 
ATOM   2018  C  C   . PRO   A 1 283 ? 22.470  13.901  -57.802 1.00 103.66 ? 352  PRO   A C   1 
ATOM   2019  O  O   . PRO   A 1 283 ? 23.156  12.906  -58.054 1.00 104.29 ? 352  PRO   A O   1 
ATOM   2020  C  CB  . PRO   A 1 283 ? 20.197  13.253  -58.694 1.00 101.77 ? 352  PRO   A CB  1 
ATOM   2021  C  CG  . PRO   A 1 283 ? 18.927  14.030  -58.673 1.00 99.73  ? 352  PRO   A CG  1 
ATOM   2022  C  CD  . PRO   A 1 283 ? 19.222  15.317  -57.992 1.00 102.87 ? 352  PRO   A CD  1 
ATOM   2023  N  N   . HIS   A 1 284 ? 22.989  15.133  -57.825 1.00 102.76 ? 353  HIS   A N   1 
ATOM   2024  C  CA  . HIS   A 1 284 ? 24.381  15.358  -58.207 1.00 104.79 ? 353  HIS   A CA  1 
ATOM   2025  C  C   . HIS   A 1 284 ? 25.188  16.017  -57.097 1.00 103.64 ? 353  HIS   A C   1 
ATOM   2026  O  O   . HIS   A 1 284 ? 26.185  16.695  -57.377 1.00 105.62 ? 353  HIS   A O   1 
ATOM   2027  C  CB  . HIS   A 1 284 ? 24.460  16.184  -59.494 1.00 104.46 ? 353  HIS   A CB  1 
ATOM   2028  C  CG  . HIS   A 1 284 ? 23.959  15.459  -60.704 1.00 107.57 ? 353  HIS   A CG  1 
ATOM   2029  N  ND1 . HIS   A 1 284 ? 24.589  14.349  -61.225 1.00 108.87 ? 353  HIS   A ND1 1 
ATOM   2030  C  CD2 . HIS   A 1 284 ? 22.879  15.681  -61.487 1.00 107.37 ? 353  HIS   A CD2 1 
ATOM   2031  C  CE1 . HIS   A 1 284 ? 23.916  13.921  -62.277 1.00 110.37 ? 353  HIS   A CE1 1 
ATOM   2032  N  NE2 . HIS   A 1 284 ? 22.876  14.713  -62.459 1.00 105.61 ? 353  HIS   A NE2 1 
ATOM   2033  N  N   . GLY   A 1 285 ? 24.785  15.818  -55.839 1.00 106.58 ? 354  GLY   A N   1 
ATOM   2034  C  CA  . GLY   A 1 285 ? 25.492  16.369  -54.703 1.00 110.27 ? 354  GLY   A CA  1 
ATOM   2035  C  C   . GLY   A 1 285 ? 25.400  17.869  -54.529 1.00 109.36 ? 354  GLY   A C   1 
ATOM   2036  O  O   . GLY   A 1 285 ? 25.825  18.381  -53.482 1.00 111.24 ? 354  GLY   A O   1 
ATOM   2037  N  N   . TYR   A 1 286 ? 24.881  18.595  -55.512 1.00 100.07 ? 355  TYR   A N   1 
ATOM   2038  C  CA  . TYR   A 1 286 ? 24.570  19.997  -55.300 1.00 95.05  ? 355  TYR   A CA  1 
ATOM   2039  C  C   . TYR   A 1 286 ? 23.589  20.141  -54.140 1.00 96.68  ? 355  TYR   A C   1 
ATOM   2040  O  O   . TYR   A 1 286 ? 22.603  19.398  -54.039 1.00 95.33  ? 355  TYR   A O   1 
ATOM   2041  C  CB  . TYR   A 1 286 ? 24.009  20.599  -56.591 1.00 93.80  ? 355  TYR   A CB  1 
ATOM   2042  C  CG  . TYR   A 1 286 ? 25.069  20.751  -57.653 1.00 93.94  ? 355  TYR   A CG  1 
ATOM   2043  C  CD1 . TYR   A 1 286 ? 26.165  21.591  -57.445 1.00 94.92  ? 355  TYR   A CD1 1 
ATOM   2044  C  CD2 . TYR   A 1 286 ? 24.996  20.056  -58.850 1.00 92.56  ? 355  TYR   A CD2 1 
ATOM   2045  C  CE1 . TYR   A 1 286 ? 27.155  21.739  -58.400 1.00 88.85  ? 355  TYR   A CE1 1 
ATOM   2046  C  CE2 . TYR   A 1 286 ? 25.988  20.202  -59.821 1.00 94.89  ? 355  TYR   A CE2 1 
ATOM   2047  C  CZ  . TYR   A 1 286 ? 27.062  21.050  -59.581 1.00 89.53  ? 355  TYR   A CZ  1 
ATOM   2048  O  OH  . TYR   A 1 286 ? 28.057  21.213  -60.508 1.00 87.87  ? 355  TYR   A OH  1 
ATOM   2049  N  N   . VAL   A 1 287 ? 23.876  21.090  -53.247 1.00 94.32  ? 356  VAL   A N   1 
ATOM   2050  C  CA  . VAL   A 1 287 ? 23.056  21.327  -52.062 1.00 91.74  ? 356  VAL   A CA  1 
ATOM   2051  C  C   . VAL   A 1 287 ? 22.309  22.638  -52.246 1.00 87.53  ? 356  VAL   A C   1 
ATOM   2052  O  O   . VAL   A 1 287 ? 22.769  23.540  -52.953 1.00 94.58  ? 356  VAL   A O   1 
ATOM   2053  C  CB  . VAL   A 1 287 ? 23.899  21.340  -50.763 1.00 92.38  ? 356  VAL   A CB  1 
ATOM   2054  C  CG1 . VAL   A 1 287 ? 23.005  21.298  -49.537 1.00 81.85  ? 356  VAL   A CG1 1 
ATOM   2055  C  CG2 . VAL   A 1 287 ? 24.899  20.167  -50.753 1.00 93.57  ? 356  VAL   A CG2 1 
ATOM   2056  N  N   . HIS   A 1 288 ? 21.138  22.732  -51.611 1.00 85.45  ? 357  HIS   A N   1 
ATOM   2057  C  CA  . HIS   A 1 288 ? 20.214  23.850  -51.815 1.00 83.80  ? 357  HIS   A CA  1 
ATOM   2058  C  C   . HIS   A 1 288 ? 19.505  24.189  -50.505 1.00 81.28  ? 357  HIS   A C   1 
ATOM   2059  O  O   . HIS   A 1 288 ? 18.502  23.558  -50.160 1.00 82.02  ? 357  HIS   A O   1 
ATOM   2060  C  CB  . HIS   A 1 288 ? 19.181  23.524  -52.893 1.00 82.26  ? 357  HIS   A CB  1 
ATOM   2061  C  CG  . HIS   A 1 288 ? 19.695  23.614  -54.296 1.00 86.92  ? 357  HIS   A CG  1 
ATOM   2062  N  ND1 . HIS   A 1 288 ? 19.738  24.797  -54.998 1.00 86.92  ? 357  HIS   A ND1 1 
ATOM   2063  C  CD2 . HIS   A 1 288 ? 20.140  22.655  -55.144 1.00 92.62  ? 357  HIS   A CD2 1 
ATOM   2064  C  CE1 . HIS   A 1 288 ? 20.209  24.567  -56.211 1.00 91.23  ? 357  HIS   A CE1 1 
ATOM   2065  N  NE2 . HIS   A 1 288 ? 20.462  23.275  -56.325 1.00 89.45  ? 357  HIS   A NE2 1 
ATOM   2066  N  N   . GLU   A 1 289 ? 19.982  25.208  -49.799 1.00 80.37  ? 358  GLU   A N   1 
ATOM   2067  C  CA  . GLU   A 1 289 ? 19.154  25.823  -48.763 1.00 80.94  ? 358  GLU   A CA  1 
ATOM   2068  C  C   . GLU   A 1 289 ? 17.885  26.375  -49.416 1.00 80.56  ? 358  GLU   A C   1 
ATOM   2069  O  O   . GLU   A 1 289 ? 17.946  27.367  -50.154 1.00 79.83  ? 358  GLU   A O   1 
ATOM   2070  C  CB  . GLU   A 1 289 ? 19.947  26.920  -48.050 1.00 80.64  ? 358  GLU   A CB  1 
ATOM   2071  C  CG  . GLU   A 1 289 ? 21.440  26.628  -47.977 1.00 84.47  ? 358  GLU   A CG  1 
ATOM   2072  C  CD  . GLU   A 1 289 ? 22.224  27.496  -46.978 1.00 93.82  ? 358  GLU   A CD  1 
ATOM   2073  O  OE1 . GLU   A 1 289 ? 21.780  27.679  -45.814 1.00 93.67  ? 358  GLU   A OE1 1 
ATOM   2074  O  OE2 . GLU   A 1 289 ? 23.317  27.978  -47.363 1.00 95.21  ? 358  GLU   A OE2 1 
ATOM   2075  N  N   . THR   A 1 290 ? 16.729  25.736  -49.165 1.00 80.11  ? 359  THR   A N   1 
ATOM   2076  C  CA  . THR   A 1 290 ? 15.499  26.021  -49.917 1.00 80.99  ? 359  THR   A CA  1 
ATOM   2077  C  C   . THR   A 1 290 ? 14.371  26.536  -49.028 1.00 81.95  ? 359  THR   A C   1 
ATOM   2078  O  O   . THR   A 1 290 ? 13.617  25.749  -48.445 1.00 82.05  ? 359  THR   A O   1 
ATOM   2079  C  CB  . THR   A 1 290 ? 15.016  24.793  -50.680 1.00 80.39  ? 359  THR   A CB  1 
ATOM   2080  O  OG1 . THR   A 1 290 ? 16.101  24.231  -51.436 1.00 80.71  ? 359  THR   A OG1 1 
ATOM   2081  C  CG2 . THR   A 1 290 ? 13.862  25.173  -51.623 1.00 78.70  ? 359  THR   A CG2 1 
ATOM   2082  N  N   . LEU   A 1 291 ? 14.215  27.860  -49.001 1.00 78.77  ? 360  LEU   A N   1 
ATOM   2083  C  CA  . LEU   A 1 291 ? 13.134  28.495  -48.264 1.00 78.89  ? 360  LEU   A CA  1 
ATOM   2084  C  C   . LEU   A 1 291 ? 11.794  28.197  -48.912 1.00 78.00  ? 360  LEU   A C   1 
ATOM   2085  O  O   . LEU   A 1 291 ? 11.571  28.540  -50.071 1.00 80.38  ? 360  LEU   A O   1 
ATOM   2086  C  CB  . LEU   A 1 291 ? 13.372  29.993  -48.214 1.00 79.33  ? 360  LEU   A CB  1 
ATOM   2087  C  CG  . LEU   A 1 291 ? 12.308  30.892  -47.610 1.00 76.80  ? 360  LEU   A CG  1 
ATOM   2088  C  CD1 . LEU   A 1 291 ? 12.390  30.795  -46.109 1.00 80.05  ? 360  LEU   A CD1 1 
ATOM   2089  C  CD2 . LEU   A 1 291 ? 12.516  32.329  -48.081 1.00 78.05  ? 360  LEU   A CD2 1 
ATOM   2090  N  N   . THR   A 1 292 ? 10.901  27.573  -48.166 1.00 79.63  ? 361  THR   A N   1 
ATOM   2091  C  CA  . THR   A 1 292 ? 9.564   27.280  -48.642 1.00 78.39  ? 361  THR   A CA  1 
ATOM   2092  C  C   . THR   A 1 292 ? 8.670   28.473  -48.330 1.00 82.04  ? 361  THR   A C   1 
ATOM   2093  O  O   . THR   A 1 292 ? 8.692   29.004  -47.217 1.00 83.63  ? 361  THR   A O   1 
ATOM   2094  C  CB  . THR   A 1 292 ? 9.049   25.989  -47.988 1.00 87.12  ? 361  THR   A CB  1 
ATOM   2095  O  OG1 . THR   A 1 292 ? 8.962   26.147  -46.568 1.00 91.28  ? 361  THR   A OG1 1 
ATOM   2096  C  CG2 . THR   A 1 292 ? 10.015  24.830  -48.256 1.00 87.24  ? 361  THR   A CG2 1 
ATOM   2097  N  N   . VAL   A 1 293 ? 7.927   28.938  -49.326 1.00 87.21  ? 362  VAL   A N   1 
ATOM   2098  C  CA  . VAL   A 1 293 ? 7.032   30.074  -49.136 1.00 88.88  ? 362  VAL   A CA  1 
ATOM   2099  C  C   . VAL   A 1 293 ? 5.686   29.727  -49.749 1.00 92.39  ? 362  VAL   A C   1 
ATOM   2100  O  O   . VAL   A 1 293 ? 5.588   28.893  -50.655 1.00 93.68  ? 362  VAL   A O   1 
ATOM   2101  C  CB  . VAL   A 1 293 ? 7.576   31.377  -49.759 1.00 82.38  ? 362  VAL   A CB  1 
ATOM   2102  C  CG1 . VAL   A 1 293 ? 8.858   31.800  -49.077 1.00 79.05  ? 362  VAL   A CG1 1 
ATOM   2103  C  CG2 . VAL   A 1 293 ? 7.832   31.161  -51.206 1.00 87.03  ? 362  VAL   A CG2 1 
ATOM   2104  N  N   . TYR   A 1 294 ? 4.634   30.376  -49.250 1.00 96.79  ? 363  TYR   A N   1 
ATOM   2105  C  CA  . TYR   A 1 294 ? 3.296   30.083  -49.753 1.00 96.47  ? 363  TYR   A CA  1 
ATOM   2106  C  C   . TYR   A 1 294 ? 3.096   30.629  -51.157 1.00 94.46  ? 363  TYR   A C   1 
ATOM   2107  O  O   . TYR   A 1 294 ? 2.602   29.914  -52.034 1.00 99.08  ? 363  TYR   A O   1 
ATOM   2108  C  CB  . TYR   A 1 294 ? 2.233   30.634  -48.803 1.00 97.38  ? 363  TYR   A CB  1 
ATOM   2109  C  CG  . TYR   A 1 294 ? 1.950   29.690  -47.664 1.00 100.94 ? 363  TYR   A CG  1 
ATOM   2110  C  CD1 . TYR   A 1 294 ? 2.169   28.320  -47.808 1.00 100.54 ? 363  TYR   A CD1 1 
ATOM   2111  C  CD2 . TYR   A 1 294 ? 1.483   30.159  -46.446 1.00 101.01 ? 363  TYR   A CD2 1 
ATOM   2112  C  CE1 . TYR   A 1 294 ? 1.928   27.440  -46.776 1.00 101.24 ? 363  TYR   A CE1 1 
ATOM   2113  C  CE2 . TYR   A 1 294 ? 1.237   29.282  -45.400 1.00 104.76 ? 363  TYR   A CE2 1 
ATOM   2114  C  CZ  . TYR   A 1 294 ? 1.466   27.926  -45.573 1.00 104.83 ? 363  TYR   A CZ  1 
ATOM   2115  O  OH  . TYR   A 1 294 ? 1.228   27.049  -44.539 1.00 106.11 ? 363  TYR   A OH  1 
ATOM   2116  N  N   . LYS   A 1 295 ? 3.449   31.891  -51.384 1.00 92.00  ? 364  LYS   A N   1 
ATOM   2117  C  CA  . LYS   A 1 295 ? 3.290   32.537  -52.679 1.00 90.75  ? 364  LYS   A CA  1 
ATOM   2118  C  C   . LYS   A 1 295 ? 4.587   33.240  -53.073 1.00 95.35  ? 364  LYS   A C   1 
ATOM   2119  O  O   . LYS   A 1 295 ? 5.258   33.841  -52.227 1.00 97.81  ? 364  LYS   A O   1 
ATOM   2120  C  CB  . LYS   A 1 295 ? 2.119   33.552  -52.652 1.00 81.40  ? 364  LYS   A CB  1 
ATOM   2121  N  N   . ALA   A 1 296 ? 4.950   33.146  -54.356 1.00 94.50  ? 365  ALA   A N   1 
ATOM   2122  C  CA  . ALA   A 1 296 ? 6.025   33.936  -54.948 1.00 91.38  ? 365  ALA   A CA  1 
ATOM   2123  C  C   . ALA   A 1 296 ? 5.504   34.627  -56.204 1.00 97.10  ? 365  ALA   A C   1 
ATOM   2124  O  O   . ALA   A 1 296 ? 4.514   34.201  -56.796 1.00 97.74  ? 365  ALA   A O   1 
ATOM   2125  C  CB  . ALA   A 1 296 ? 7.238   33.074  -55.298 1.00 87.81  ? 365  ALA   A CB  1 
ATOM   2126  N  N   . CYS   A 1 297 ? 6.184   35.687  -56.637 1.00 96.69  ? 366  CYS   A N   1 
ATOM   2127  C  CA  . CYS   A 1 297 ? 5.702   36.453  -57.781 1.00 98.31  ? 366  CYS   A CA  1 
ATOM   2128  C  C   . CYS   A 1 297 ? 6.808   36.690  -58.805 1.00 98.21  ? 366  CYS   A C   1 
ATOM   2129  O  O   . CYS   A 1 297 ? 7.989   36.436  -58.555 1.00 97.31  ? 366  CYS   A O   1 
ATOM   2130  C  CB  . CYS   A 1 297 ? 5.089   37.782  -57.318 1.00 99.68  ? 366  CYS   A CB  1 
ATOM   2131  S  SG  . CYS   A 1 297 ? 3.543   37.475  -56.440 1.00 111.07 ? 366  CYS   A SG  1 
ATOM   2132  N  N   . ASN   A 1 298 ? 6.396   37.157  -59.987 1.00 93.27  ? 367  ASN   A N   1 
ATOM   2133  C  CA  . ASN   A 1 298 ? 7.330   37.521  -61.049 1.00 87.66  ? 367  ASN   A CA  1 
ATOM   2134  C  C   . ASN   A 1 298 ? 8.299   36.388  -61.377 1.00 85.46  ? 367  ASN   A C   1 
ATOM   2135  O  O   . ASN   A 1 298 ? 9.481   36.615  -61.626 1.00 82.72  ? 367  ASN   A O   1 
ATOM   2136  C  CB  . ASN   A 1 298 ? 8.098   38.787  -60.670 1.00 89.97  ? 367  ASN   A CB  1 
ATOM   2137  C  CG  . ASN   A 1 298 ? 7.191   39.973  -60.486 1.00 93.40  ? 367  ASN   A CG  1 
ATOM   2138  O  OD1 . ASN   A 1 298 ? 6.482   40.375  -61.413 1.00 91.05  ? 367  ASN   A OD1 1 
ATOM   2139  N  ND2 . ASN   A 1 298 ? 7.180   40.529  -59.269 1.00 96.85  ? 367  ASN   A ND2 1 
ATOM   2140  N  N   . LEU   A 1 299 ? 7.807   35.157  -61.387 1.00 89.02  ? 368  LEU   A N   1 
ATOM   2141  C  CA  . LEU   A 1 299 ? 8.634   34.007  -61.733 1.00 89.25  ? 368  LEU   A CA  1 
ATOM   2142  C  C   . LEU   A 1 299 ? 8.042   33.279  -62.928 1.00 94.33  ? 368  LEU   A C   1 
ATOM   2143  O  O   . LEU   A 1 299 ? 6.825   33.114  -63.020 1.00 100.56 ? 368  LEU   A O   1 
ATOM   2144  C  CB  . LEU   A 1 299 ? 8.767   33.044  -60.570 1.00 85.59  ? 368  LEU   A CB  1 
ATOM   2145  C  CG  . LEU   A 1 299 ? 9.705   33.535  -59.487 1.00 82.67  ? 368  LEU   A CG  1 
ATOM   2146  C  CD1 . LEU   A 1 299 ? 9.712   32.480  -58.428 1.00 81.45  ? 368  LEU   A CD1 1 
ATOM   2147  C  CD2 . LEU   A 1 299 ? 11.106  33.767  -60.057 1.00 85.06  ? 368  LEU   A CD2 1 
ATOM   2148  N  N   . ASN   A 1 300 ? 8.901   32.840  -63.843 1.00 98.24  ? 369  ASN   A N   1 
ATOM   2149  C  CA  . ASN   A 1 300 ? 8.484   32.065  -65.003 1.00 99.08  ? 369  ASN   A CA  1 
ATOM   2150  C  C   . ASN   A 1 300 ? 8.872   30.604  -64.808 1.00 101.77 ? 369  ASN   A C   1 
ATOM   2151  O  O   . ASN   A 1 300 ? 9.956   30.298  -64.292 1.00 101.33 ? 369  ASN   A O   1 
ATOM   2152  C  CB  . ASN   A 1 300 ? 9.123   32.609  -66.279 1.00 101.01 ? 369  ASN   A CB  1 
ATOM   2153  C  CG  . ASN   A 1 300 ? 8.183   33.464  -67.069 1.00 109.65 ? 369  ASN   A CG  1 
ATOM   2154  O  OD1 . ASN   A 1 300 ? 7.051   33.056  -67.357 1.00 122.07 ? 369  ASN   A OD1 1 
ATOM   2155  N  ND2 . ASN   A 1 300 ? 8.633   34.671  -67.424 1.00 105.83 ? 369  ASN   A ND2 1 
ATOM   2156  N  N   . LEU   A 1 301 ? 7.998   29.697  -65.223 1.00 92.49  ? 370  LEU   A N   1 
ATOM   2157  C  CA  . LEU   A 1 301 ? 8.227   28.282  -64.975 1.00 90.52  ? 370  LEU   A CA  1 
ATOM   2158  C  C   . LEU   A 1 301 ? 8.811   27.609  -66.212 1.00 92.21  ? 370  LEU   A C   1 
ATOM   2159  O  O   . LEU   A 1 301 ? 8.369   27.858  -67.336 1.00 98.71  ? 370  LEU   A O   1 
ATOM   2160  C  CB  . LEU   A 1 301 ? 6.934   27.588  -64.523 1.00 90.86  ? 370  LEU   A CB  1 
ATOM   2161  C  CG  . LEU   A 1 301 ? 6.552   27.664  -63.039 1.00 88.42  ? 370  LEU   A CG  1 
ATOM   2162  C  CD1 . LEU   A 1 301 ? 5.659   28.842  -62.701 1.00 92.82  ? 370  LEU   A CD1 1 
ATOM   2163  C  CD2 . LEU   A 1 301 ? 5.870   26.377  -62.639 1.00 97.71  ? 370  LEU   A CD2 1 
ATOM   2164  N  N   . ILE   A 1 302 ? 9.811   26.758  -65.992 1.00 91.45  ? 371  ILE   A N   1 
ATOM   2165  C  CA  . ILE   A 1 302 ? 10.640  26.176  -67.046 1.00 89.43  ? 371  ILE   A CA  1 
ATOM   2166  C  C   . ILE   A 1 302 ? 10.354  24.677  -67.083 1.00 99.96  ? 371  ILE   A C   1 
ATOM   2167  O  O   . ILE   A 1 302 ? 10.763  23.917  -66.184 1.00 100.21 ? 371  ILE   A O   1 
ATOM   2168  C  CB  . ILE   A 1 302 ? 12.138  26.449  -66.811 1.00 84.70  ? 371  ILE   A CB  1 
ATOM   2169  C  CG1 . ILE   A 1 302 ? 12.493  27.896  -67.152 1.00 90.31  ? 371  ILE   A CG1 1 
ATOM   2170  C  CG2 . ILE   A 1 302 ? 13.008  25.500  -67.584 1.00 82.86  ? 371  ILE   A CG2 1 
ATOM   2171  C  CD1 . ILE   A 1 302 ? 11.659  28.505  -68.227 1.00 95.26  ? 371  ILE   A CD1 1 
ATOM   2172  N  N   . GLY   A 1 303 ? 9.650   24.255  -68.115 1.00 97.77  ? 372  GLY   A N   1 
ATOM   2173  C  CA  . GLY   A 1 303 ? 9.451   22.842  -68.366 1.00 93.35  ? 372  GLY   A CA  1 
ATOM   2174  C  C   . GLY   A 1 303 ? 8.115   22.353  -67.843 1.00 98.16  ? 372  GLY   A C   1 
ATOM   2175  O  O   . GLY   A 1 303 ? 7.197   23.094  -67.522 1.00 97.31  ? 372  GLY   A O   1 
ATOM   2176  N  N   . ARG   A 1 304 ? 8.038   21.037  -67.790 1.00 103.09 ? 373  ARG   A N   1 
ATOM   2177  C  CA  . ARG   A 1 304 ? 6.865   20.391  -67.260 1.00 104.09 ? 373  ARG   A CA  1 
ATOM   2178  C  C   . ARG   A 1 304 ? 7.172   19.821  -65.877 1.00 101.26 ? 373  ARG   A C   1 
ATOM   2179  O  O   . ARG   A 1 304 ? 8.300   19.373  -65.627 1.00 102.15 ? 373  ARG   A O   1 
ATOM   2180  C  CB  . ARG   A 1 304 ? 6.410   19.276  -68.204 1.00 103.96 ? 373  ARG   A CB  1 
ATOM   2181  C  CG  . ARG   A 1 304 ? 5.888   19.759  -69.565 1.00 107.54 ? 373  ARG   A CG  1 
ATOM   2182  C  CD  . ARG   A 1 304 ? 5.399   18.592  -70.452 1.00 116.03 ? 373  ARG   A CD  1 
ATOM   2183  N  NE  . ARG   A 1 304 ? 4.969   19.045  -71.769 1.00 122.98 ? 373  ARG   A NE  1 
ATOM   2184  C  CZ  . ARG   A 1 304 ? 4.615   18.229  -72.754 1.00 131.18 ? 373  ARG   A CZ  1 
ATOM   2185  N  NH1 . ARG   A 1 304 ? 4.571   16.916  -72.581 1.00 134.87 ? 373  ARG   A NH1 1 
ATOM   2186  N  NH2 . ARG   A 1 304 ? 4.325   18.737  -73.952 1.00 133.54 ? 373  ARG   A NH2 1 
ATOM   2187  N  N   . PRO   A 1 305 ? 6.216   19.842  -64.949 1.00 97.15  ? 374  PRO   A N   1 
ATOM   2188  C  CA  . PRO   A 1 305 ? 6.496   19.336  -63.604 1.00 97.22  ? 374  PRO   A CA  1 
ATOM   2189  C  C   . PRO   A 1 305 ? 7.042   17.918  -63.670 1.00 100.63 ? 374  PRO   A C   1 
ATOM   2190  O  O   . PRO   A 1 305 ? 6.747   17.160  -64.597 1.00 100.64 ? 374  PRO   A O   1 
ATOM   2191  C  CB  . PRO   A 1 305 ? 5.127   19.379  -62.914 1.00 96.00  ? 374  PRO   A CB  1 
ATOM   2192  C  CG  . PRO   A 1 305 ? 4.322   20.359  -63.699 1.00 98.96  ? 374  PRO   A CG  1 
ATOM   2193  C  CD  . PRO   A 1 305 ? 4.801   20.221  -65.111 1.00 101.20 ? 374  PRO   A CD  1 
ATOM   2194  N  N   . SER   A 1 306 ? 7.849   17.567  -62.675 1.00 97.95  ? 375  SER   A N   1 
ATOM   2195  C  CA  . SER   A 1 306 ? 8.360   16.214  -62.526 1.00 97.56  ? 375  SER   A CA  1 
ATOM   2196  C  C   . SER   A 1 306 ? 8.208   15.782  -61.070 1.00 103.25 ? 375  SER   A C   1 
ATOM   2197  O  O   . SER   A 1 306 ? 7.775   16.554  -60.203 1.00 101.19 ? 375  SER   A O   1 
ATOM   2198  C  CB  . SER   A 1 306 ? 9.822   16.119  -62.984 1.00 98.81  ? 375  SER   A CB  1 
ATOM   2199  O  OG  . SER   A 1 306 ? 10.370  14.839  -62.718 1.00 99.40  ? 375  SER   A OG  1 
ATOM   2200  N  N   . THR   A 1 307 ? 8.581   14.532  -60.797 1.00 104.26 ? 376  THR   A N   1 
ATOM   2201  C  CA  . THR   A 1 307 ? 8.581   14.029  -59.431 1.00 99.75  ? 376  THR   A CA  1 
ATOM   2202  C  C   . THR   A 1 307 ? 9.904   13.421  -58.992 1.00 101.45 ? 376  THR   A C   1 
ATOM   2203  O  O   . THR   A 1 307 ? 10.069  13.186  -57.793 1.00 103.97 ? 376  THR   A O   1 
ATOM   2204  C  CB  . THR   A 1 307 ? 7.470   12.990  -59.243 1.00 96.99  ? 376  THR   A CB  1 
ATOM   2205  O  OG1 . THR   A 1 307 ? 7.791   11.818  -59.996 1.00 101.94 ? 376  THR   A OG1 1 
ATOM   2206  C  CG2 . THR   A 1 307 ? 6.153   13.543  -59.743 1.00 93.80  ? 376  THR   A CG2 1 
ATOM   2207  N  N   . GLU   A 1 308 ? 10.854  13.185  -59.907 1.00 104.83 ? 377  GLU   A N   1 
ATOM   2208  C  CA  . GLU   A 1 308 ? 12.144  12.592  -59.553 1.00 106.14 ? 377  GLU   A CA  1 
ATOM   2209  C  C   . GLU   A 1 308 ? 12.828  13.364  -58.437 1.00 104.47 ? 377  GLU   A C   1 
ATOM   2210  O  O   . GLU   A 1 308 ? 13.103  14.560  -58.567 1.00 106.59 ? 377  GLU   A O   1 
ATOM   2211  C  CB  . GLU   A 1 308 ? 13.065  12.564  -60.768 1.00 108.61 ? 377  GLU   A CB  1 
ATOM   2212  C  CG  . GLU   A 1 308 ? 12.350  12.392  -62.070 1.00 118.99 ? 377  GLU   A CG  1 
ATOM   2213  C  CD  . GLU   A 1 308 ? 13.296  12.437  -63.271 1.00 125.85 ? 377  GLU   A CD  1 
ATOM   2214  O  OE1 . GLU   A 1 308 ? 13.602  13.565  -63.747 1.00 122.12 ? 377  GLU   A OE1 1 
ATOM   2215  O  OE2 . GLU   A 1 308 ? 13.736  11.342  -63.715 1.00 120.34 ? 377  GLU   A OE2 1 
ATOM   2216  N  N   . HIS   A 1 309 ? 13.130  12.678  -57.347 1.00 104.68 ? 378  HIS   A N   1 
ATOM   2217  C  CA  . HIS   A 1 309 ? 13.874  13.244  -56.234 1.00 107.36 ? 378  HIS   A CA  1 
ATOM   2218  C  C   . HIS   A 1 309 ? 13.135  14.435  -55.644 1.00 107.72 ? 378  HIS   A C   1 
ATOM   2219  O  O   . HIS   A 1 309 ? 13.777  15.307  -55.039 1.00 110.38 ? 378  HIS   A O   1 
ATOM   2220  C  CB  . HIS   A 1 309 ? 15.226  13.811  -56.679 1.00 109.52 ? 378  HIS   A CB  1 
ATOM   2221  C  CG  . HIS   A 1 309 ? 16.347  13.503  -55.734 1.00 115.49 ? 378  HIS   A CG  1 
ATOM   2222  N  ND1 . HIS   A 1 309 ? 17.672  13.735  -56.042 1.00 115.43 ? 378  HIS   A ND1 1 
ATOM   2223  C  CD2 . HIS   A 1 309 ? 16.340  12.973  -54.486 1.00 116.82 ? 378  HIS   A CD2 1 
ATOM   2224  C  CE1 . HIS   A 1 309 ? 18.432  13.360  -55.028 1.00 115.67 ? 378  HIS   A CE1 1 
ATOM   2225  N  NE2 . HIS   A 1 309 ? 17.649  12.895  -54.071 1.00 118.58 ? 378  HIS   A NE2 1 
ATOM   2226  N  N   . SER   A 1 310 ? 11.813  14.503  -55.791 1.00 98.97  ? 379  SER   A N   1 
ATOM   2227  C  CA  . SER   A 1 310 ? 11.039  15.600  -55.227 1.00 98.83  ? 379  SER   A CA  1 
ATOM   2228  C  C   . SER   A 1 310 ? 11.368  15.548  -53.743 1.00 102.72 ? 379  SER   A C   1 
ATOM   2229  O  O   . SER   A 1 310 ? 11.063  14.567  -53.055 1.00 103.91 ? 379  SER   A O   1 
ATOM   2230  C  CB  . SER   A 1 310 ? 9.556   15.375  -55.500 1.00 102.51 ? 379  SER   A CB  1 
ATOM   2231  O  OG  . SER   A 1 310 ? 8.836   16.552  -55.169 1.00 100.49 ? 379  SER   A OG  1 
ATOM   2232  N  N   . TRP   A 1 311 ? 11.987  16.616  -53.243 1.00 100.47 ? 380  TRP   A N   1 
ATOM   2233  C  CA  . TRP   A 1 311 ? 12.414  16.650  -51.854 1.00 95.49  ? 380  TRP   A CA  1 
ATOM   2234  C  C   . TRP   A 1 311 ? 11.197  16.600  -50.938 1.00 97.75  ? 380  TRP   A C   1 
ATOM   2235  O  O   . TRP   A 1 311 ? 11.296  16.132  -49.800 1.00 101.49 ? 380  TRP   A O   1 
ATOM   2236  C  CB  . TRP   A 1 311 ? 13.195  17.920  -51.615 1.00 95.40  ? 380  TRP   A CB  1 
ATOM   2237  C  CG  . TRP   A 1 311 ? 14.527  17.942  -52.261 1.00 92.75  ? 380  TRP   A CG  1 
ATOM   2238  C  CD1 . TRP   A 1 311 ? 15.399  16.913  -52.367 1.00 98.05  ? 380  TRP   A CD1 1 
ATOM   2239  C  CD2 . TRP   A 1 311 ? 15.159  19.069  -52.873 1.00 97.15  ? 380  TRP   A CD2 1 
ATOM   2240  N  NE1 . TRP   A 1 311 ? 16.546  17.322  -53.005 1.00 96.45  ? 380  TRP   A NE1 1 
ATOM   2241  C  CE2 . TRP   A 1 311 ? 16.420  18.645  -53.327 1.00 95.58  ? 380  TRP   A CE2 1 
ATOM   2242  C  CE3 . TRP   A 1 311 ? 14.779  20.405  -53.079 1.00 96.04  ? 380  TRP   A CE3 1 
ATOM   2243  C  CZ2 . TRP   A 1 311 ? 17.304  19.503  -53.980 1.00 97.58  ? 380  TRP   A CZ2 1 
ATOM   2244  C  CZ3 . TRP   A 1 311 ? 15.665  21.259  -53.721 1.00 87.37  ? 380  TRP   A CZ3 1 
ATOM   2245  C  CH2 . TRP   A 1 311 ? 16.909  20.805  -54.165 1.00 91.55  ? 380  TRP   A CH2 1 
ATOM   2246  N  N   . PHE   A 1 312 ? 10.059  17.081  -51.407 1.00 95.48  ? 381  PHE   A N   1 
ATOM   2247  C  CA  . PHE   A 1 312 ? 8.827   17.098  -50.636 1.00 100.94 ? 381  PHE   A CA  1 
ATOM   2248  C  C   . PHE   A 1 312 ? 7.876   16.058  -51.200 1.00 101.02 ? 381  PHE   A C   1 
ATOM   2249  O  O   . PHE   A 1 312 ? 7.056   16.360  -52.083 1.00 100.18 ? 381  PHE   A O   1 
ATOM   2250  C  CB  . PHE   A 1 312 ? 8.202   18.488  -50.661 1.00 101.18 ? 381  PHE   A CB  1 
ATOM   2251  C  CG  . PHE   A 1 312 ? 9.172   19.558  -50.363 1.00 100.39 ? 381  PHE   A CG  1 
ATOM   2252  C  CD1 . PHE   A 1 312 ? 9.389   19.970  -49.058 1.00 101.52 ? 381  PHE   A CD1 1 
ATOM   2253  C  CD2 . PHE   A 1 312 ? 9.920   20.123  -51.376 1.00 99.21  ? 381  PHE   A CD2 1 
ATOM   2254  C  CE1 . PHE   A 1 312 ? 10.316  20.960  -48.773 1.00 101.33 ? 381  PHE   A CE1 1 
ATOM   2255  C  CE2 . PHE   A 1 312 ? 10.851  21.113  -51.098 1.00 100.01 ? 381  PHE   A CE2 1 
ATOM   2256  C  CZ  . PHE   A 1 312 ? 11.046  21.535  -49.789 1.00 98.00  ? 381  PHE   A CZ  1 
ATOM   2257  N  N   . PRO   A 1 313 ? 7.980   14.819  -50.732 1.00 103.12 ? 382  PRO   A N   1 
ATOM   2258  C  CA  . PRO   A 1 313 ? 7.202   13.736  -51.337 1.00 102.45 ? 382  PRO   A CA  1 
ATOM   2259  C  C   . PRO   A 1 313 ? 5.721   14.060  -51.284 1.00 105.68 ? 382  PRO   A C   1 
ATOM   2260  O  O   . PRO   A 1 313 ? 5.188   14.455  -50.247 1.00 108.02 ? 382  PRO   A O   1 
ATOM   2261  C  CB  . PRO   A 1 313 ? 7.568   12.526  -50.479 1.00 99.65  ? 382  PRO   A CB  1 
ATOM   2262  C  CG  . PRO   A 1 313 ? 8.976   12.822  -50.047 1.00 103.25 ? 382  PRO   A CG  1 
ATOM   2263  C  CD  . PRO   A 1 313 ? 8.938   14.307  -49.737 1.00 107.46 ? 382  PRO   A CD  1 
ATOM   2264  N  N   . GLY   A 1 314 ? 5.068   13.946  -52.441 1.00 100.63 ? 383  GLY   A N   1 
ATOM   2265  C  CA  . GLY   A 1 314 ? 3.673   14.288  -52.599 1.00 102.87 ? 383  GLY   A CA  1 
ATOM   2266  C  C   . GLY   A 1 314 ? 3.441   15.417  -53.577 1.00 109.84 ? 383  GLY   A C   1 
ATOM   2267  O  O   . GLY   A 1 314 ? 2.362   15.479  -54.207 1.00 109.46 ? 383  GLY   A O   1 
ATOM   2268  N  N   . TYR   A 1 315 ? 4.407   16.319  -53.717 1.00 108.09 ? 384  TYR   A N   1 
ATOM   2269  C  CA  . TYR   A 1 315 ? 4.326   17.392  -54.697 1.00 103.39 ? 384  TYR   A CA  1 
ATOM   2270  C  C   . TYR   A 1 315 ? 5.343   17.142  -55.803 1.00 101.08 ? 384  TYR   A C   1 
ATOM   2271  O  O   . TYR   A 1 315 ? 6.371   16.489  -55.588 1.00 97.24  ? 384  TYR   A O   1 
ATOM   2272  C  CB  . TYR   A 1 315 ? 4.596   18.753  -54.047 1.00 102.97 ? 384  TYR   A CB  1 
ATOM   2273  C  CG  . TYR   A 1 315 ? 3.751   19.065  -52.828 1.00 101.67 ? 384  TYR   A CG  1 
ATOM   2274  C  CD1 . TYR   A 1 315 ? 4.073   18.552  -51.575 1.00 103.87 ? 384  TYR   A CD1 1 
ATOM   2275  C  CD2 . TYR   A 1 315 ? 2.653   19.908  -52.925 1.00 103.45 ? 384  TYR   A CD2 1 
ATOM   2276  C  CE1 . TYR   A 1 315 ? 3.305   18.860  -50.454 1.00 104.15 ? 384  TYR   A CE1 1 
ATOM   2277  C  CE2 . TYR   A 1 315 ? 1.885   20.217  -51.820 1.00 106.19 ? 384  TYR   A CE2 1 
ATOM   2278  C  CZ  . TYR   A 1 315 ? 2.212   19.692  -50.586 1.00 104.69 ? 384  TYR   A CZ  1 
ATOM   2279  O  OH  . TYR   A 1 315 ? 1.447   20.007  -49.484 1.00 107.41 ? 384  TYR   A OH  1 
ATOM   2280  N  N   . ALA   A 1 316 ? 5.042   17.662  -56.992 1.00 100.10 ? 385  ALA   A N   1 
ATOM   2281  C  CA  . ALA   A 1 316 ? 5.967   17.635  -58.112 1.00 97.19  ? 385  ALA   A CA  1 
ATOM   2282  C  C   . ALA   A 1 316 ? 6.616   19.000  -58.262 1.00 97.03  ? 385  ALA   A C   1 
ATOM   2283  O  O   . ALA   A 1 316 ? 6.081   20.009  -57.796 1.00 98.43  ? 385  ALA   A O   1 
ATOM   2284  C  CB  . ALA   A 1 316 ? 5.247   17.248  -59.397 1.00 94.93  ? 385  ALA   A CB  1 
ATOM   2285  N  N   . TRP   A 1 317 ? 7.777   19.026  -58.920 1.00 96.66  ? 386  TRP   A N   1 
ATOM   2286  C  CA  . TRP   A 1 317 ? 8.567   20.246  -59.034 1.00 95.36  ? 386  TRP   A CA  1 
ATOM   2287  C  C   . TRP   A 1 317 ? 8.640   20.753  -60.468 1.00 92.57  ? 386  TRP   A C   1 
ATOM   2288  O  O   . TRP   A 1 317 ? 8.686   19.973  -61.418 1.00 92.96  ? 386  TRP   A O   1 
ATOM   2289  C  CB  . TRP   A 1 317 ? 9.982   20.048  -58.503 1.00 91.76  ? 386  TRP   A CB  1 
ATOM   2290  C  CG  . TRP   A 1 317 ? 10.698  18.918  -59.118 1.00 92.88  ? 386  TRP   A CG  1 
ATOM   2291  C  CD1 . TRP   A 1 317 ? 10.720  17.632  -58.672 1.00 96.26  ? 386  TRP   A CD1 1 
ATOM   2292  C  CD2 . TRP   A 1 317 ? 11.534  18.958  -60.278 1.00 94.45  ? 386  TRP   A CD2 1 
ATOM   2293  N  NE1 . TRP   A 1 317 ? 11.513  16.863  -59.487 1.00 97.90  ? 386  TRP   A NE1 1 
ATOM   2294  C  CE2 . TRP   A 1 317 ? 12.025  17.656  -60.482 1.00 97.34  ? 386  TRP   A CE2 1 
ATOM   2295  C  CE3 . TRP   A 1 317 ? 11.916  19.967  -61.165 1.00 95.93  ? 386  TRP   A CE3 1 
ATOM   2296  C  CZ2 . TRP   A 1 317 ? 12.863  17.333  -61.546 1.00 100.96 ? 386  TRP   A CZ2 1 
ATOM   2297  C  CZ3 . TRP   A 1 317 ? 12.763  19.644  -62.216 1.00 94.46  ? 386  TRP   A CZ3 1 
ATOM   2298  C  CH2 . TRP   A 1 317 ? 13.226  18.343  -62.393 1.00 99.62  ? 386  TRP   A CH2 1 
ATOM   2299  N  N   . THR   A 1 318 ? 8.668   22.071  -60.602 1.00 92.11  ? 387  THR   A N   1 
ATOM   2300  C  CA  . THR   A 1 318 ? 8.796   22.760  -61.873 1.00 90.11  ? 387  THR   A CA  1 
ATOM   2301  C  C   . THR   A 1 318 ? 9.796   23.880  -61.657 1.00 91.08  ? 387  THR   A C   1 
ATOM   2302  O  O   . THR   A 1 318 ? 9.639   24.679  -60.731 1.00 87.57  ? 387  THR   A O   1 
ATOM   2303  C  CB  . THR   A 1 318 ? 7.449   23.323  -62.335 1.00 90.83  ? 387  THR   A CB  1 
ATOM   2304  O  OG1 . THR   A 1 318 ? 6.406   22.406  -61.972 1.00 94.54  ? 387  THR   A OG1 1 
ATOM   2305  C  CG2 . THR   A 1 318 ? 7.438   23.539  -63.827 1.00 91.92  ? 387  THR   A CG2 1 
ATOM   2306  N  N   . VAL   A 1 319 ? 10.834  23.929  -62.493 1.00 95.11  ? 388  VAL   A N   1 
ATOM   2307  C  CA  . VAL   A 1 319 ? 11.913  24.893  -62.282 1.00 90.61  ? 388  VAL   A CA  1 
ATOM   2308  C  C   . VAL   A 1 319 ? 11.392  26.309  -62.459 1.00 87.56  ? 388  VAL   A C   1 
ATOM   2309  O  O   . VAL   A 1 319 ? 10.587  26.590  -63.352 1.00 90.21  ? 388  VAL   A O   1 
ATOM   2310  C  CB  . VAL   A 1 319 ? 13.075  24.618  -63.249 1.00 86.66  ? 388  VAL   A CB  1 
ATOM   2311  C  CG1 . VAL   A 1 319 ? 14.289  25.429  -62.867 1.00 85.86  ? 388  VAL   A CG1 1 
ATOM   2312  C  CG2 . VAL   A 1 319 ? 13.385  23.148  -63.239 1.00 90.64  ? 388  VAL   A CG2 1 
ATOM   2313  N  N   . ALA   A 1 320 ? 11.862  27.220  -61.618 1.00 88.22  ? 389  ALA   A N   1 
ATOM   2314  C  CA  . ALA   A 1 320 ? 11.376  28.593  -61.641 1.00 87.63  ? 389  ALA   A CA  1 
ATOM   2315  C  C   . ALA   A 1 320 ? 12.544  29.563  -61.755 1.00 86.29  ? 389  ALA   A C   1 
ATOM   2316  O  O   . ALA   A 1 320 ? 13.625  29.319  -61.213 1.00 83.61  ? 389  ALA   A O   1 
ATOM   2317  C  CB  . ALA   A 1 320 ? 10.525  28.885  -60.392 1.00 83.14  ? 389  ALA   A CB  1 
ATOM   2318  N  N   . GLN   A 1 321 ? 12.315  30.671  -62.465 1.00 89.11  ? 390  GLN   A N   1 
ATOM   2319  C  CA  . GLN   A 1 321 ? 13.373  31.645  -62.709 1.00 88.10  ? 390  GLN   A CA  1 
ATOM   2320  C  C   . GLN   A 1 321 ? 12.794  33.045  -62.855 1.00 86.74  ? 390  GLN   A C   1 
ATOM   2321  O  O   . GLN   A 1 321 ? 11.616  33.227  -63.179 1.00 85.52  ? 390  GLN   A O   1 
ATOM   2322  C  CB  . GLN   A 1 321 ? 14.193  31.277  -63.953 1.00 91.10  ? 390  GLN   A CB  1 
ATOM   2323  C  CG  . GLN   A 1 321 ? 13.341  31.024  -65.192 1.00 92.98  ? 390  GLN   A CG  1 
ATOM   2324  C  CD  . GLN   A 1 321 ? 14.168  30.851  -66.451 1.00 96.74  ? 390  GLN   A CD  1 
ATOM   2325  O  OE1 . GLN   A 1 321 ? 15.068  29.996  -66.511 1.00 94.10  ? 390  GLN   A OE1 1 
ATOM   2326  N  NE2 . GLN   A 1 321 ? 13.874  31.673  -67.468 1.00 95.77  ? 390  GLN   A NE2 1 
ATOM   2327  N  N   . CYS   A 1 322 ? 13.661  34.031  -62.620 1.00 86.57  ? 391  CYS   A N   1 
ATOM   2328  C  CA  . CYS   A 1 322 ? 13.295  35.441  -62.725 1.00 90.89  ? 391  CYS   A CA  1 
ATOM   2329  C  C   . CYS   A 1 322 ? 12.743  35.781  -64.106 1.00 91.55  ? 391  CYS   A C   1 
ATOM   2330  O  O   . CYS   A 1 322 ? 13.322  35.406  -65.127 1.00 95.73  ? 391  CYS   A O   1 
ATOM   2331  C  CB  . CYS   A 1 322 ? 14.522  36.301  -62.430 1.00 90.90  ? 391  CYS   A CB  1 
ATOM   2332  S  SG  . CYS   A 1 322 ? 14.188  38.047  -62.414 1.00 85.37  ? 391  CYS   A SG  1 
ATOM   2333  N  N   . LYS   A 1 323 ? 11.621  36.498  -64.142 1.00 86.93  ? 392  LYS   A N   1 
ATOM   2334  C  CA  . LYS   A 1 323 ? 11.017  36.847  -65.418 1.00 85.26  ? 392  LYS   A CA  1 
ATOM   2335  C  C   . LYS   A 1 323 ? 11.759  37.969  -66.119 1.00 90.98  ? 392  LYS   A C   1 
ATOM   2336  O  O   . LYS   A 1 323 ? 11.390  38.339  -67.248 1.00 93.48  ? 392  LYS   A O   1 
ATOM   2337  C  CB  . LYS   A 1 323 ? 9.551   37.237  -65.227 1.00 87.09  ? 392  LYS   A CB  1 
ATOM   2338  C  CG  . LYS   A 1 323 ? 9.327   38.543  -64.475 1.00 84.38  ? 392  LYS   A CG  1 
ATOM   2339  C  CD  . LYS   A 1 323 ? 7.844   38.830  -64.420 1.00 84.74  ? 392  LYS   A CD  1 
ATOM   2340  C  CE  . LYS   A 1 323 ? 7.547   40.238  -63.975 1.00 84.59  ? 392  LYS   A CE  1 
ATOM   2341  N  NZ  . LYS   A 1 323 ? 6.080   40.442  -64.044 1.00 82.95  ? 392  LYS   A NZ  1 
ATOM   2342  N  N   . ILE   A 1 324 ? 12.798  38.508  -65.485 1.00 88.14  ? 393  ILE   A N   1 
ATOM   2343  C  CA  . ILE   A 1 324 ? 13.516  39.665  -66.001 1.00 93.43  ? 393  ILE   A CA  1 
ATOM   2344  C  C   . ILE   A 1 324 ? 14.927  39.300  -66.446 1.00 94.68  ? 393  ILE   A C   1 
ATOM   2345  O  O   . ILE   A 1 324 ? 15.397  39.800  -67.473 1.00 93.72  ? 393  ILE   A O   1 
ATOM   2346  C  CB  . ILE   A 1 324 ? 13.552  40.814  -64.964 1.00 89.83  ? 393  ILE   A CB  1 
ATOM   2347  C  CG1 . ILE   A 1 324 ? 12.143  41.241  -64.554 1.00 86.01  ? 393  ILE   A CG1 1 
ATOM   2348  C  CG2 . ILE   A 1 324 ? 14.299  42.003  -65.514 1.00 83.35  ? 393  ILE   A CG2 1 
ATOM   2349  C  CD1 . ILE   A 1 324 ? 11.553  42.267  -65.458 1.00 83.81  ? 393  ILE   A CD1 1 
ATOM   2350  N  N   . CYS   A 1 325 ? 15.636  38.455  -65.671 1.00 91.21  ? 394  CYS   A N   1 
ATOM   2351  C  CA  . CYS   A 1 325 ? 17.000  38.071  -66.011 1.00 89.34  ? 394  CYS   A CA  1 
ATOM   2352  C  C   . CYS   A 1 325 ? 17.161  36.571  -66.162 1.00 90.52  ? 394  CYS   A C   1 
ATOM   2353  O  O   . CYS   A 1 325 ? 18.272  36.103  -66.433 1.00 95.63  ? 394  CYS   A O   1 
ATOM   2354  C  CB  . CYS   A 1 325 ? 17.999  38.612  -64.975 1.00 92.45  ? 394  CYS   A CB  1 
ATOM   2355  S  SG  . CYS   A 1 325 ? 18.025  37.848  -63.337 1.00 92.99  ? 394  CYS   A SG  1 
ATOM   2356  N  N   . ALA   A 1 326 ? 16.077  35.813  -66.036 1.00 97.73  ? 395  ALA   A N   1 
ATOM   2357  C  CA  . ALA   A 1 326 ? 16.090  34.355  -66.201 1.00 99.04  ? 395  ALA   A CA  1 
ATOM   2358  C  C   . ALA   A 1 326 ? 17.197  33.712  -65.373 1.00 98.43  ? 395  ALA   A C   1 
ATOM   2359  O  O   . ALA   A 1 326 ? 17.816  32.734  -65.796 1.00 99.76  ? 395  ALA   A O   1 
ATOM   2360  C  CB  . ALA   A 1 326 ? 16.218  33.946  -67.673 1.00 94.89  ? 395  ALA   A CB  1 
ATOM   2361  N  N   . SER   A 1 327 ? 17.466  34.271  -64.196 1.00 92.34  ? 396  SER   A N   1 
ATOM   2362  C  CA  . SER   A 1 327 ? 18.360  33.607  -63.265 1.00 93.39  ? 396  SER   A CA  1 
ATOM   2363  C  C   . SER   A 1 327 ? 17.549  32.605  -62.459 1.00 92.01  ? 396  SER   A C   1 
ATOM   2364  O  O   . SER   A 1 327 ? 16.347  32.792  -62.241 1.00 89.74  ? 396  SER   A O   1 
ATOM   2365  C  CB  . SER   A 1 327 ? 19.059  34.618  -62.357 1.00 91.57  ? 396  SER   A CB  1 
ATOM   2366  O  OG  . SER   A 1 327 ? 20.278  35.045  -62.938 1.00 95.03  ? 396  SER   A OG  1 
ATOM   2367  N  N   . HIS   A 1 328 ? 18.196  31.513  -62.054 1.00 84.91  ? 397  HIS   A N   1 
ATOM   2368  C  CA  . HIS   A 1 328 ? 17.462  30.469  -61.357 1.00 78.48  ? 397  HIS   A CA  1 
ATOM   2369  C  C   . HIS   A 1 328 ? 17.079  30.952  -59.968 1.00 78.42  ? 397  HIS   A C   1 
ATOM   2370  O  O   . HIS   A 1 328 ? 17.912  31.493  -59.236 1.00 80.70  ? 397  HIS   A O   1 
ATOM   2371  C  CB  . HIS   A 1 328 ? 18.290  29.186  -61.274 1.00 89.64  ? 397  HIS   A CB  1 
ATOM   2372  C  CG  . HIS   A 1 328 ? 17.601  28.070  -60.544 1.00 79.87  ? 397  HIS   A CG  1 
ATOM   2373  N  ND1 . HIS   A 1 328 ? 18.039  27.591  -59.332 1.00 76.80  ? 397  HIS   A ND1 1 
ATOM   2374  C  CD2 . HIS   A 1 328 ? 16.491  27.359  -60.848 1.00 77.85  ? 397  HIS   A CD2 1 
ATOM   2375  C  CE1 . HIS   A 1 328 ? 17.228  26.635  -58.920 1.00 76.48  ? 397  HIS   A CE1 1 
ATOM   2376  N  NE2 . HIS   A 1 328 ? 16.280  26.474  -59.822 1.00 77.11  ? 397  HIS   A NE2 1 
ATOM   2377  N  N   . ILE   A 1 329 ? 15.805  30.786  -59.613 1.00 77.45  ? 398  ILE   A N   1 
ATOM   2378  C  CA  . ILE   A 1 329 ? 15.336  31.136  -58.284 1.00 78.68  ? 398  ILE   A CA  1 
ATOM   2379  C  C   . ILE   A 1 329 ? 14.983  29.902  -57.460 1.00 82.13  ? 398  ILE   A C   1 
ATOM   2380  O  O   . ILE   A 1 329 ? 15.201  29.900  -56.242 1.00 82.67  ? 398  ILE   A O   1 
ATOM   2381  C  CB  . ILE   A 1 329 ? 14.144  32.120  -58.343 1.00 79.63  ? 398  ILE   A CB  1 
ATOM   2382  C  CG1 . ILE   A 1 329 ? 14.529  33.406  -59.109 1.00 83.35  ? 398  ILE   A CG1 1 
ATOM   2383  C  CG2 . ILE   A 1 329 ? 13.646  32.441  -56.935 1.00 76.13  ? 398  ILE   A CG2 1 
ATOM   2384  C  CD1 . ILE   A 1 329 ? 15.609  34.303  -58.431 1.00 81.18  ? 398  ILE   A CD1 1 
ATOM   2385  N  N   . GLY   A 1 330 ? 14.464  28.854  -58.082 1.00 81.20  ? 399  GLY   A N   1 
ATOM   2386  C  CA  . GLY   A 1 330 ? 14.109  27.639  -57.379 1.00 79.05  ? 399  GLY   A CA  1 
ATOM   2387  C  C   . GLY   A 1 330 ? 13.105  26.794  -58.141 1.00 81.57  ? 399  GLY   A C   1 
ATOM   2388  O  O   . GLY   A 1 330 ? 13.237  26.619  -59.357 1.00 82.66  ? 399  GLY   A O   1 
ATOM   2389  N  N   . TRP   A 1 331 ? 12.083  26.274  -57.462 1.00 79.24  ? 400  TRP   A N   1 
ATOM   2390  C  CA  . TRP   A 1 331 ? 11.117  25.404  -58.116 1.00 84.97  ? 400  TRP   A CA  1 
ATOM   2391  C  C   . TRP   A 1 331 ? 9.714   25.757  -57.656 1.00 85.30  ? 400  TRP   A C   1 
ATOM   2392  O  O   . TRP   A 1 331 ? 9.526   26.402  -56.626 1.00 84.68  ? 400  TRP   A O   1 
ATOM   2393  C  CB  . TRP   A 1 331 ? 11.425  23.934  -57.818 1.00 87.88  ? 400  TRP   A CB  1 
ATOM   2394  C  CG  . TRP   A 1 331 ? 12.853  23.567  -58.109 1.00 84.69  ? 400  TRP   A CG  1 
ATOM   2395  C  CD1 . TRP   A 1 331 ? 13.345  22.978  -59.254 1.00 86.50  ? 400  TRP   A CD1 1 
ATOM   2396  C  CD2 . TRP   A 1 331 ? 13.975  23.778  -57.257 1.00 75.53  ? 400  TRP   A CD2 1 
ATOM   2397  N  NE1 . TRP   A 1 331 ? 14.703  22.806  -59.147 1.00 83.64  ? 400  TRP   A NE1 1 
ATOM   2398  C  CE2 . TRP   A 1 331 ? 15.111  23.287  -57.930 1.00 82.32  ? 400  TRP   A CE2 1 
ATOM   2399  C  CE3 . TRP   A 1 331 ? 14.132  24.323  -55.987 1.00 79.06  ? 400  TRP   A CE3 1 
ATOM   2400  C  CZ2 . TRP   A 1 331 ? 16.389  23.331  -57.370 1.00 88.03  ? 400  TRP   A CZ2 1 
ATOM   2401  C  CZ3 . TRP   A 1 331 ? 15.409  24.356  -55.425 1.00 83.30  ? 400  TRP   A CZ3 1 
ATOM   2402  C  CH2 . TRP   A 1 331 ? 16.517  23.871  -56.118 1.00 81.13  ? 400  TRP   A CH2 1 
ATOM   2403  N  N   . LYS   A 1 332 ? 8.724   25.297  -58.407 1.00 88.10  ? 401  LYS   A N   1 
ATOM   2404  C  CA  . LYS   A 1 332 ? 7.336   25.398  -57.981 1.00 89.66  ? 401  LYS   A CA  1 
ATOM   2405  C  C   . LYS   A 1 332 ? 6.794   23.998  -57.727 1.00 91.67  ? 401  LYS   A C   1 
ATOM   2406  O  O   . LYS   A 1 332 ? 6.751   23.162  -58.637 1.00 90.87  ? 401  LYS   A O   1 
ATOM   2407  C  CB  . LYS   A 1 332 ? 6.492   26.130  -59.017 1.00 89.33  ? 401  LYS   A CB  1 
ATOM   2408  C  CG  . LYS   A 1 332 ? 5.050   26.251  -58.631 1.00 89.81  ? 401  LYS   A CG  1 
ATOM   2409  C  CD  . LYS   A 1 332 ? 4.275   26.865  -59.769 1.00 89.81  ? 401  LYS   A CD  1 
ATOM   2410  C  CE  . LYS   A 1 332 ? 3.120   27.683  -59.262 1.00 97.31  ? 401  LYS   A CE  1 
ATOM   2411  N  NZ  . LYS   A 1 332 ? 2.732   28.723  -60.254 1.00 107.98 ? 401  LYS   A NZ  1 
ATOM   2412  N  N   . PHE   A 1 333 ? 6.383   23.747  -56.494 1.00 93.49  ? 402  PHE   A N   1 
ATOM   2413  C  CA  . PHE   A 1 333 ? 5.870   22.448  -56.106 1.00 91.93  ? 402  PHE   A CA  1 
ATOM   2414  C  C   . PHE   A 1 333 ? 4.351   22.450  -56.164 1.00 97.20  ? 402  PHE   A C   1 
ATOM   2415  O  O   . PHE   A 1 333 ? 3.691   23.358  -55.644 1.00 97.97  ? 402  PHE   A O   1 
ATOM   2416  C  CB  . PHE   A 1 333 ? 6.374   22.077  -54.723 1.00 89.26  ? 402  PHE   A CB  1 
ATOM   2417  C  CG  . PHE   A 1 333 ? 7.858   21.901  -54.671 1.00 91.88  ? 402  PHE   A CG  1 
ATOM   2418  C  CD1 . PHE   A 1 333 ? 8.690   22.988  -54.432 1.00 86.49  ? 402  PHE   A CD1 1 
ATOM   2419  C  CD2 . PHE   A 1 333 ? 8.431   20.654  -54.893 1.00 92.72  ? 402  PHE   A CD2 1 
ATOM   2420  C  CE1 . PHE   A 1 333 ? 10.056  22.835  -54.392 1.00 83.69  ? 402  PHE   A CE1 1 
ATOM   2421  C  CE2 . PHE   A 1 333 ? 9.796   20.487  -54.851 1.00 91.78  ? 402  PHE   A CE2 1 
ATOM   2422  C  CZ  . PHE   A 1 333 ? 10.614  21.581  -54.601 1.00 92.53  ? 402  PHE   A CZ  1 
ATOM   2423  N  N   . THR   A 1 334 ? 3.808   21.430  -56.811 1.00 100.29 ? 403  THR   A N   1 
ATOM   2424  C  CA  . THR   A 1 334 ? 2.395   21.312  -57.111 1.00 97.21  ? 403  THR   A CA  1 
ATOM   2425  C  C   . THR   A 1 334 ? 1.939   19.939  -56.638 1.00 101.97 ? 403  THR   A C   1 
ATOM   2426  O  O   . THR   A 1 334 ? 2.656   18.947  -56.817 1.00 103.67 ? 403  THR   A O   1 
ATOM   2427  C  CB  . THR   A 1 334 ? 2.181   21.489  -58.608 1.00 96.91  ? 403  THR   A CB  1 
ATOM   2428  O  OG1 . THR   A 1 334 ? 2.930   20.487  -59.311 1.00 104.37 ? 403  THR   A OG1 1 
ATOM   2429  C  CG2 . THR   A 1 334 ? 2.709   22.860  -59.051 1.00 89.72  ? 403  THR   A CG2 1 
ATOM   2430  N  N   . ALA   A 1 335 ? 0.765   19.872  -56.014 1.00 103.81 ? 404  ALA   A N   1 
ATOM   2431  C  CA  . ALA   A 1 335 ? 0.356   18.633  -55.354 1.00 110.12 ? 404  ALA   A CA  1 
ATOM   2432  C  C   . ALA   A 1 335 ? -0.043  17.572  -56.374 1.00 108.38 ? 404  ALA   A C   1 
ATOM   2433  O  O   . ALA   A 1 335 ? -0.800  17.849  -57.306 1.00 107.24 ? 404  ALA   A O   1 
ATOM   2434  C  CB  . ALA   A 1 335 ? -0.807  18.887  -54.395 1.00 112.09 ? 404  ALA   A CB  1 
ATOM   2435  N  N   . THR   A 1 336 ? 0.441   16.346  -56.194 1.00 111.89 ? 405  THR   A N   1 
ATOM   2436  C  CA  . THR   A 1 336 ? -0.057  15.281  -57.061 1.00 115.58 ? 405  THR   A CA  1 
ATOM   2437  C  C   . THR   A 1 336 ? -1.488  14.911  -56.694 1.00 122.82 ? 405  THR   A C   1 
ATOM   2438  O  O   . THR   A 1 336 ? -2.343  14.770  -57.574 1.00 124.29 ? 405  THR   A O   1 
ATOM   2439  C  CB  . THR   A 1 336 ? 0.838   14.040  -57.007 1.00 110.16 ? 405  THR   A CB  1 
ATOM   2440  O  OG1 . THR   A 1 336 ? 0.975   13.587  -55.659 1.00 115.76 ? 405  THR   A OG1 1 
ATOM   2441  C  CG2 . THR   A 1 336 ? 2.205   14.340  -57.577 1.00 105.33 ? 405  THR   A CG2 1 
ATOM   2442  N  N   . LYS   A 1 337 ? -1.778  14.777  -55.400 1.00 124.81 ? 406  LYS   A N   1 
ATOM   2443  C  CA  . LYS   A 1 337 ? -3.096  14.299  -55.005 1.00 129.15 ? 406  LYS   A CA  1 
ATOM   2444  C  C   . LYS   A 1 337 ? -4.026  15.500  -54.915 1.00 134.62 ? 406  LYS   A C   1 
ATOM   2445  O  O   . LYS   A 1 337 ? -3.669  16.604  -55.342 1.00 132.43 ? 406  LYS   A O   1 
ATOM   2446  C  CB  . LYS   A 1 337 ? -3.048  13.609  -53.639 1.00 130.26 ? 406  LYS   A CB  1 
ATOM   2447  C  CG  . LYS   A 1 337 ? -2.257  12.295  -53.620 1.00 121.16 ? 406  LYS   A CG  1 
ATOM   2448  C  CD  . LYS   A 1 337 ? -2.218  11.659  -52.232 1.00 126.28 ? 406  LYS   A CD  1 
ATOM   2449  C  CE  . LYS   A 1 337 ? -1.454  10.336  -52.199 1.00 135.26 ? 406  LYS   A CE  1 
ATOM   2450  N  NZ  . LYS   A 1 337 ? -1.407  9.738   -50.817 1.00 132.59 ? 406  LYS   A NZ  1 
ATOM   2451  N  N   . LYS   A 1 338 ? -5.240  15.285  -54.423 1.00 152.84 ? 407  LYS   A N   1 
ATOM   2452  C  CA  . LYS   A 1 338 ? -6.106  16.392  -54.073 1.00 152.48 ? 407  LYS   A CA  1 
ATOM   2453  C  C   . LYS   A 1 338 ? -6.343  16.541  -52.595 1.00 154.17 ? 407  LYS   A C   1 
ATOM   2454  O  O   . LYS   A 1 338 ? -6.803  17.610  -52.148 1.00 154.26 ? 407  LYS   A O   1 
ATOM   2455  C  CB  . LYS   A 1 338 ? -7.452  16.209  -54.782 1.00 147.53 ? 407  LYS   A CB  1 
ATOM   2456  N  N   . ASP   A 1 339 ? -6.044  15.500  -51.821 1.00 152.82 ? 408  ASP   A N   1 
ATOM   2457  C  CA  . ASP   A 1 339 ? -6.003  15.650  -50.380 1.00 155.10 ? 408  ASP   A CA  1 
ATOM   2458  C  C   . ASP   A 1 339 ? -5.089  16.802  -49.983 1.00 153.50 ? 408  ASP   A C   1 
ATOM   2459  O  O   . ASP   A 1 339 ? -5.531  17.785  -49.376 1.00 153.78 ? 408  ASP   A O   1 
ATOM   2460  C  CB  . ASP   A 1 339 ? -5.533  14.326  -49.779 1.00 155.63 ? 408  ASP   A CB  1 
ATOM   2461  C  CG  . ASP   A 1 339 ? -4.861  14.479  -48.439 1.00 162.93 ? 408  ASP   A CG  1 
ATOM   2462  O  OD1 . ASP   A 1 339 ? -5.257  15.401  -47.654 1.00 165.71 ? 408  ASP   A OD1 1 
ATOM   2463  O  OD2 . ASP   A 1 339 ? -3.966  13.672  -48.167 1.00 165.15 ? 408  ASP   A OD2 1 
ATOM   2464  N  N   . MET   A 1 340 ? -3.818  16.713  -50.367 1.00 143.95 ? 409  MET   A N   1 
ATOM   2465  C  CA  . MET   A 1 340 ? -2.769  17.488  -49.719 1.00 135.81 ? 409  MET   A CA  1 
ATOM   2466  C  C   . MET   A 1 340 ? -3.119  18.974  -49.616 1.00 129.41 ? 409  MET   A C   1 
ATOM   2467  O  O   . MET   A 1 340 ? -3.747  19.551  -50.515 1.00 124.06 ? 409  MET   A O   1 
ATOM   2468  C  CB  . MET   A 1 340 ? -1.454  17.324  -50.474 1.00 127.98 ? 409  MET   A CB  1 
ATOM   2469  C  CG  . MET   A 1 340 ? -1.313  16.030  -51.223 1.00 129.14 ? 409  MET   A CG  1 
ATOM   2470  S  SD  . MET   A 1 340 ? 0.350   15.982  -51.905 1.00 119.63 ? 409  MET   A SD  1 
ATOM   2471  C  CE  . MET   A 1 340 ? 1.238   15.036  -50.649 1.00 105.30 ? 409  MET   A CE  1 
ATOM   2472  N  N   . SER   A 1 341 ? -2.709  19.584  -48.492 1.00 121.11 ? 410  SER   A N   1 
ATOM   2473  C  CA  . SER   A 1 341 ? -2.643  21.029  -48.340 1.00 115.27 ? 410  SER   A CA  1 
ATOM   2474  C  C   . SER   A 1 341 ? -1.258  21.403  -47.827 1.00 110.56 ? 410  SER   A C   1 
ATOM   2475  O  O   . SER   A 1 341 ? -0.731  20.750  -46.911 1.00 108.69 ? 410  SER   A O   1 
ATOM   2476  C  CB  . SER   A 1 341 ? -3.681  21.588  -47.376 1.00 117.04 ? 410  SER   A CB  1 
ATOM   2477  O  OG  . SER   A 1 341 ? -3.516  23.000  -47.253 1.00 113.53 ? 410  SER   A OG  1 
ATOM   2478  N  N   . PRO   A 1 342 ? -0.637  22.441  -48.385 1.00 109.90 ? 411  PRO   A N   1 
ATOM   2479  C  CA  . PRO   A 1 342 ? -1.153  23.327  -49.433 1.00 110.63 ? 411  PRO   A CA  1 
ATOM   2480  C  C   . PRO   A 1 342 ? -1.123  22.643  -50.807 1.00 110.05 ? 411  PRO   A C   1 
ATOM   2481  O  O   . PRO   A 1 342 ? -0.380  21.680  -50.998 1.00 106.40 ? 411  PRO   A O   1 
ATOM   2482  C  CB  . PRO   A 1 342 ? -0.199  24.519  -49.350 1.00 105.03 ? 411  PRO   A CB  1 
ATOM   2483  C  CG  . PRO   A 1 342 ? 1.126   23.854  -49.022 1.00 104.29 ? 411  PRO   A CG  1 
ATOM   2484  C  CD  . PRO   A 1 342 ? 0.787   22.698  -48.107 1.00 105.40 ? 411  PRO   A CD  1 
ATOM   2485  N  N   . GLN   A 1 343 ? -1.911  23.108  -51.783 1.00 109.89 ? 412  GLN   A N   1 
ATOM   2486  C  CA  . GLN   A 1 343 ? -1.890  22.501  -53.117 1.00 109.42 ? 412  GLN   A CA  1 
ATOM   2487  C  C   . GLN   A 1 343 ? -0.639  22.910  -53.898 1.00 105.73 ? 412  GLN   A C   1 
ATOM   2488  O  O   . GLN   A 1 343 ? 0.047   22.058  -54.475 1.00 105.41 ? 412  GLN   A O   1 
ATOM   2489  C  CB  . GLN   A 1 343 ? -3.164  22.873  -53.895 1.00 110.25 ? 412  GLN   A CB  1 
ATOM   2490  C  CG  . GLN   A 1 343 ? -4.433  22.112  -53.476 1.00 113.32 ? 412  GLN   A CG  1 
ATOM   2491  C  CD  . GLN   A 1 343 ? -4.439  20.645  -53.912 1.00 114.95 ? 412  GLN   A CD  1 
ATOM   2492  O  OE1 . GLN   A 1 343 ? -4.915  20.309  -54.998 1.00 115.70 ? 412  GLN   A OE1 1 
ATOM   2493  N  NE2 . GLN   A 1 343 ? -3.911  19.769  -53.062 1.00 117.46 ? 412  GLN   A NE2 1 
ATOM   2494  N  N   . LYS   A 1 344 ? -0.340  24.206  -53.937 1.00 100.76 ? 413  LYS   A N   1 
ATOM   2495  C  CA  . LYS   A 1 344 ? 0.903   24.713  -54.488 1.00 92.59  ? 413  LYS   A CA  1 
ATOM   2496  C  C   . LYS   A 1 344 ? 1.740   25.389  -53.413 1.00 97.51  ? 413  LYS   A C   1 
ATOM   2497  O  O   . LYS   A 1 344 ? 1.212   25.943  -52.438 1.00 96.10  ? 413  LYS   A O   1 
ATOM   2498  C  CB  . LYS   A 1 344 ? 0.647   25.711  -55.595 1.00 96.46  ? 413  LYS   A CB  1 
ATOM   2499  C  CG  . LYS   A 1 344 ? 0.862   25.151  -56.997 1.00 108.06 ? 413  LYS   A CG  1 
ATOM   2500  C  CD  . LYS   A 1 344 ? 0.919   26.275  -58.074 1.00 109.29 ? 413  LYS   A CD  1 
ATOM   2501  C  CE  . LYS   A 1 344 ? 0.378   25.813  -59.457 1.00 111.27 ? 413  LYS   A CE  1 
ATOM   2502  N  NZ  . LYS   A 1 344 ? 0.839   26.694  -60.589 1.00 111.85 ? 413  LYS   A NZ  1 
ATOM   2503  N  N   . PHE   A 1 345 ? 3.055   25.319  -53.596 1.00 98.14  ? 414  PHE   A N   1 
ATOM   2504  C  CA  . PHE   A 1 345 ? 3.997   26.177  -52.881 1.00 99.67  ? 414  PHE   A CA  1 
ATOM   2505  C  C   . PHE   A 1 345 ? 5.267   26.301  -53.718 1.00 95.65  ? 414  PHE   A C   1 
ATOM   2506  O  O   . PHE   A 1 345 ? 5.419   25.666  -54.764 1.00 95.05  ? 414  PHE   A O   1 
ATOM   2507  C  CB  . PHE   A 1 345 ? 4.296   25.674  -51.452 1.00 94.16  ? 414  PHE   A CB  1 
ATOM   2508  C  CG  . PHE   A 1 345 ? 5.051   24.367  -51.371 1.00 87.81  ? 414  PHE   A CG  1 
ATOM   2509  C  CD1 . PHE   A 1 345 ? 6.435   24.340  -51.345 1.00 88.19  ? 414  PHE   A CD1 1 
ATOM   2510  C  CD2 . PHE   A 1 345 ? 4.365   23.168  -51.248 1.00 90.53  ? 414  PHE   A CD2 1 
ATOM   2511  C  CE1 . PHE   A 1 345 ? 7.123   23.115  -51.232 1.00 93.20  ? 414  PHE   A CE1 1 
ATOM   2512  C  CE2 . PHE   A 1 345 ? 5.038   21.960  -51.140 1.00 93.53  ? 414  PHE   A CE2 1 
ATOM   2513  C  CZ  . PHE   A 1 345 ? 6.418   21.929  -51.132 1.00 93.58  ? 414  PHE   A CZ  1 
ATOM   2514  N  N   . TRP   A 1 346 ? 6.178   27.141  -53.255 1.00 93.31  ? 415  TRP   A N   1 
ATOM   2515  C  CA  . TRP   A 1 346 ? 7.417   27.410  -53.960 1.00 88.13  ? 415  TRP   A CA  1 
ATOM   2516  C  C   . TRP   A 1 346 ? 8.619   27.170  -53.057 1.00 87.90  ? 415  TRP   A C   1 
ATOM   2517  O  O   . TRP   A 1 346 ? 8.609   27.532  -51.877 1.00 90.21  ? 415  TRP   A O   1 
ATOM   2518  C  CB  . TRP   A 1 346 ? 7.474   28.844  -54.445 1.00 89.62  ? 415  TRP   A CB  1 
ATOM   2519  C  CG  . TRP   A 1 346 ? 6.296   29.360  -55.235 1.00 94.77  ? 415  TRP   A CG  1 
ATOM   2520  C  CD1 . TRP   A 1 346 ? 5.118   29.838  -54.734 1.00 99.53  ? 415  TRP   A CD1 1 
ATOM   2521  C  CD2 . TRP   A 1 346 ? 6.218   29.527  -56.664 1.00 93.63  ? 415  TRP   A CD2 1 
ATOM   2522  N  NE1 . TRP   A 1 346 ? 4.302   30.272  -55.763 1.00 97.43  ? 415  TRP   A NE1 1 
ATOM   2523  C  CE2 . TRP   A 1 346 ? 4.955   30.092  -56.953 1.00 96.41  ? 415  TRP   A CE2 1 
ATOM   2524  C  CE3 . TRP   A 1 346 ? 7.090   29.249  -57.723 1.00 92.27  ? 415  TRP   A CE3 1 
ATOM   2525  C  CZ2 . TRP   A 1 346 ? 4.543   30.386  -58.257 1.00 97.98  ? 415  TRP   A CZ2 1 
ATOM   2526  C  CZ3 . TRP   A 1 346 ? 6.678   29.534  -59.018 1.00 93.28  ? 415  TRP   A CZ3 1 
ATOM   2527  C  CH2 . TRP   A 1 346 ? 5.415   30.099  -59.275 1.00 96.87  ? 415  TRP   A CH2 1 
ATOM   2528  N  N   . GLY   A 1 347 ? 9.677   26.610  -53.630 1.00 83.52  ? 416  GLY   A N   1 
ATOM   2529  C  CA  . GLY   A 1 347 ? 10.952  26.509  -52.944 1.00 79.19  ? 416  GLY   A CA  1 
ATOM   2530  C  C   . GLY   A 1 347 ? 11.988  27.418  -53.572 1.00 79.99  ? 416  GLY   A C   1 
ATOM   2531  O  O   . GLY   A 1 347 ? 12.249  27.307  -54.772 1.00 83.14  ? 416  GLY   A O   1 
ATOM   2532  N  N   . LEU   A 1 348 ? 12.569  28.335  -52.795 1.00 82.65  ? 417  LEU   A N   1 
ATOM   2533  C  CA  . LEU   A 1 348 ? 13.543  29.299  -53.295 1.00 78.36  ? 417  LEU   A CA  1 
ATOM   2534  C  C   . LEU   A 1 348 ? 14.874  29.066  -52.600 1.00 79.41  ? 417  LEU   A C   1 
ATOM   2535  O  O   . LEU   A 1 348 ? 14.914  28.887  -51.377 1.00 80.04  ? 417  LEU   A O   1 
ATOM   2536  C  CB  . LEU   A 1 348 ? 13.047  30.722  -53.072 1.00 77.52  ? 417  LEU   A CB  1 
ATOM   2537  C  CG  . LEU   A 1 348 ? 11.538  30.875  -53.282 1.00 76.03  ? 417  LEU   A CG  1 
ATOM   2538  C  CD1 . LEU   A 1 348 ? 11.004  32.079  -52.516 1.00 73.83  ? 417  LEU   A CD1 1 
ATOM   2539  C  CD2 . LEU   A 1 348 ? 11.206  30.945  -54.779 1.00 74.97  ? 417  LEU   A CD2 1 
ATOM   2540  N  N   . THR   A 1 349 ? 15.955  29.052  -53.384 1.00 81.75  ? 418  THR   A N   1 
ATOM   2541  C  CA  . THR   A 1 349 ? 17.279  28.670  -52.889 1.00 85.09  ? 418  THR   A CA  1 
ATOM   2542  C  C   . THR   A 1 349 ? 18.074  29.909  -52.454 1.00 83.22  ? 418  THR   A C   1 
ATOM   2543  O  O   . THR   A 1 349 ? 18.276  30.850  -53.232 1.00 77.05  ? 418  THR   A O   1 
ATOM   2544  C  CB  . THR   A 1 349 ? 18.039  27.836  -53.942 1.00 79.36  ? 418  THR   A CB  1 
ATOM   2545  O  OG1 . THR   A 1 349 ? 19.419  27.673  -53.558 1.00 79.76  ? 418  THR   A OG1 1 
ATOM   2546  C  CG2 . THR   A 1 349 ? 17.942  28.457  -55.341 1.00 74.44  ? 418  THR   A CG2 1 
ATOM   2547  N  N   . ARG   A 1 350 ? 18.523  29.890  -51.200 1.00 81.35  ? 419  ARG   A N   1 
ATOM   2548  C  CA  . ARG   A 1 350 ? 19.134  31.051  -50.566 1.00 82.13  ? 419  ARG   A CA  1 
ATOM   2549  C  C   . ARG   A 1 350 ? 20.070  31.834  -51.486 1.00 81.21  ? 419  ARG   A C   1 
ATOM   2550  O  O   . ARG   A 1 350 ? 20.114  33.071  -51.436 1.00 82.73  ? 419  ARG   A O   1 
ATOM   2551  C  CB  . ARG   A 1 350 ? 19.884  30.598  -49.323 1.00 79.13  ? 419  ARG   A CB  1 
ATOM   2552  C  CG  . ARG   A 1 350 ? 20.308  31.699  -48.446 1.00 81.58  ? 419  ARG   A CG  1 
ATOM   2553  C  CD  . ARG   A 1 350 ? 21.298  31.173  -47.476 1.00 88.27  ? 419  ARG   A CD  1 
ATOM   2554  N  NE  . ARG   A 1 350 ? 22.373  30.506  -48.188 1.00 87.27  ? 419  ARG   A NE  1 
ATOM   2555  C  CZ  . ARG   A 1 350 ? 23.385  31.141  -48.754 1.00 90.79  ? 419  ARG   A CZ  1 
ATOM   2556  N  NH1 . ARG   A 1 350 ? 23.484  32.462  -48.711 1.00 88.98  ? 419  ARG   A NH1 1 
ATOM   2557  N  NH2 . ARG   A 1 350 ? 24.324  30.432  -49.375 1.00 98.18  ? 419  ARG   A NH2 1 
ATOM   2558  N  N   . SER   A 1 351 ? 20.821  31.136  -52.330 1.00 79.42  ? 420  SER   A N   1 
ATOM   2559  C  CA  . SER   A 1 351 ? 21.857  31.797  -53.118 1.00 81.83  ? 420  SER   A CA  1 
ATOM   2560  C  C   . SER   A 1 351 ? 21.291  32.727  -54.188 1.00 83.91  ? 420  SER   A C   1 
ATOM   2561  O  O   . SER   A 1 351 ? 22.002  33.629  -54.655 1.00 82.70  ? 420  SER   A O   1 
ATOM   2562  C  CB  . SER   A 1 351 ? 22.756  30.743  -53.757 1.00 80.33  ? 420  SER   A CB  1 
ATOM   2563  O  OG  . SER   A 1 351 ? 22.012  29.947  -54.683 1.00 84.89  ? 420  SER   A OG  1 
ATOM   2564  N  N   . ALA   A 1 352 ? 20.028  32.548  -54.579 1.00 82.12  ? 421  ALA   A N   1 
ATOM   2565  C  CA  . ALA   A 1 352 ? 19.435  33.421  -55.586 1.00 79.89  ? 421  ALA   A CA  1 
ATOM   2566  C  C   . ALA   A 1 352 ? 18.835  34.695  -55.006 1.00 81.84  ? 421  ALA   A C   1 
ATOM   2567  O  O   . ALA   A 1 352 ? 18.560  35.630  -55.772 1.00 83.70  ? 421  ALA   A O   1 
ATOM   2568  C  CB  . ALA   A 1 352 ? 18.357  32.674  -56.385 1.00 77.73  ? 421  ALA   A CB  1 
ATOM   2569  N  N   . LEU   A 1 353 ? 18.651  34.767  -53.688 1.00 79.52  ? 422  LEU   A N   1 
ATOM   2570  C  CA  . LEU   A 1 353 ? 17.816  35.792  -53.076 1.00 82.10  ? 422  LEU   A CA  1 
ATOM   2571  C  C   . LEU   A 1 353 ? 18.641  36.940  -52.484 1.00 82.53  ? 422  LEU   A C   1 
ATOM   2572  O  O   . LEU   A 1 353 ? 19.822  36.788  -52.154 1.00 85.74  ? 422  LEU   A O   1 
ATOM   2573  C  CB  . LEU   A 1 353 ? 16.921  35.156  -52.002 1.00 81.58  ? 422  LEU   A CB  1 
ATOM   2574  C  CG  . LEU   A 1 353 ? 15.934  34.126  -52.563 1.00 78.08  ? 422  LEU   A CG  1 
ATOM   2575  C  CD1 . LEU   A 1 353 ? 15.246  33.246  -51.490 1.00 73.33  ? 422  LEU   A CD1 1 
ATOM   2576  C  CD2 . LEU   A 1 353 ? 14.916  34.869  -53.383 1.00 74.65  ? 422  LEU   A CD2 1 
ATOM   2577  N  N   . LEU   A 1 354 ? 17.991  38.110  -52.369 1.00 81.65  ? 423  LEU   A N   1 
ATOM   2578  C  CA  . LEU   A 1 354 ? 18.566  39.317  -51.776 1.00 83.98  ? 423  LEU   A CA  1 
ATOM   2579  C  C   . LEU   A 1 354 ? 17.556  40.022  -50.880 1.00 83.51  ? 423  LEU   A C   1 
ATOM   2580  O  O   . LEU   A 1 354 ? 16.545  40.526  -51.382 1.00 82.33  ? 423  LEU   A O   1 
ATOM   2581  C  CB  . LEU   A 1 354 ? 19.018  40.284  -52.861 1.00 84.31  ? 423  LEU   A CB  1 
ATOM   2582  C  CG  . LEU   A 1 354 ? 19.716  41.541  -52.372 1.00 81.11  ? 423  LEU   A CG  1 
ATOM   2583  C  CD1 . LEU   A 1 354 ? 21.223  41.365  -52.433 1.00 85.08  ? 423  LEU   A CD1 1 
ATOM   2584  C  CD2 . LEU   A 1 354 ? 19.273  42.678  -53.251 1.00 89.34  ? 423  LEU   A CD2 1 
ATOM   2585  N  N   . PRO   A 1 355 ? 17.790  40.069  -49.561 1.00 86.85  ? 424  PRO   A N   1 
ATOM   2586  C  CA  . PRO   A 1 355 ? 16.880  40.796  -48.656 1.00 85.09  ? 424  PRO   A CA  1 
ATOM   2587  C  C   . PRO   A 1 355 ? 16.881  42.303  -48.903 1.00 86.13  ? 424  PRO   A C   1 
ATOM   2588  O  O   . PRO   A 1 355 ? 17.905  42.909  -49.229 1.00 87.75  ? 424  PRO   A O   1 
ATOM   2589  C  CB  . PRO   A 1 355 ? 17.435  40.469  -47.261 1.00 84.17  ? 424  PRO   A CB  1 
ATOM   2590  C  CG  . PRO   A 1 355 ? 18.278  39.228  -47.451 1.00 85.35  ? 424  PRO   A CG  1 
ATOM   2591  C  CD  . PRO   A 1 355 ? 18.861  39.363  -48.825 1.00 85.04  ? 424  PRO   A CD  1 
ATOM   2592  N  N   . THR   A 1 356 ? 15.711  42.918  -48.736 1.00 84.10  ? 425  THR   A N   1 
ATOM   2593  C  CA  . THR   A 1 356 ? 15.548  44.315  -49.127 1.00 88.75  ? 425  THR   A CA  1 
ATOM   2594  C  C   . THR   A 1 356 ? 14.513  44.984  -48.223 1.00 89.17  ? 425  THR   A C   1 
ATOM   2595  O  O   . THR   A 1 356 ? 13.668  44.318  -47.619 1.00 88.00  ? 425  THR   A O   1 
ATOM   2596  C  CB  . THR   A 1 356 ? 15.173  44.448  -50.629 1.00 89.80  ? 425  THR   A CB  1 
ATOM   2597  O  OG1 . THR   A 1 356 ? 13.844  43.960  -50.883 1.00 87.67  ? 425  THR   A OG1 1 
ATOM   2598  C  CG2 . THR   A 1 356 ? 16.163  43.680  -51.500 1.00 83.60  ? 425  THR   A CG2 1 
ATOM   2599  N  N   . ILE   A 1 357 ? 14.598  46.313  -48.130 1.00 84.31  ? 426  ILE   A N   1 
ATOM   2600  C  CA  . ILE   A 1 357 ? 13.817  47.081  -47.165 1.00 84.14  ? 426  ILE   A CA  1 
ATOM   2601  C  C   . ILE   A 1 357 ? 12.760  47.885  -47.910 1.00 89.71  ? 426  ILE   A C   1 
ATOM   2602  O  O   . ILE   A 1 357 ? 13.072  48.957  -48.452 1.00 101.44 ? 426  ILE   A O   1 
ATOM   2603  C  CB  . ILE   A 1 357 ? 14.714  48.007  -46.326 1.00 84.28  ? 426  ILE   A CB  1 
ATOM   2604  C  CG1 . ILE   A 1 357 ? 15.754  47.217  -45.549 1.00 80.22  ? 426  ILE   A CG1 1 
ATOM   2605  C  CG2 . ILE   A 1 357 ? 13.898  48.779  -45.346 1.00 88.75  ? 426  ILE   A CG2 1 
ATOM   2606  C  CD1 . ILE   A 1 357 ? 16.691  48.108  -44.787 1.00 85.63  ? 426  ILE   A CD1 1 
ATOM   2607  N  N   . PRO   A 1 358 ? 11.500  47.430  -47.954 1.00 85.25  ? 427  PRO   A N   1 
ATOM   2608  C  CA  . PRO   A 1 358 ? 10.412  48.063  -48.715 1.00 88.93  ? 427  PRO   A CA  1 
ATOM   2609  C  C   . PRO   A 1 358 ? 9.895   49.401  -48.154 1.00 96.04  ? 427  PRO   A C   1 
ATOM   2610  O  O   . PRO   A 1 358 ? 9.099   50.098  -48.813 1.00 97.06  ? 427  PRO   A O   1 
ATOM   2611  C  CB  . PRO   A 1 358 ? 9.308   47.008  -48.662 1.00 81.57  ? 427  PRO   A CB  1 
ATOM   2612  C  CG  . PRO   A 1 358 ? 9.551   46.288  -47.426 1.00 89.23  ? 427  PRO   A CG  1 
ATOM   2613  C  CD  . PRO   A 1 358 ? 11.048  46.200  -47.294 1.00 90.20  ? 427  PRO   A CD  1 
ATOM   2614  N  N   . VAL   A 1 369 ? 17.888  53.912  -44.260 1.00 125.15 ? 438  VAL   A N   1 
ATOM   2615  C  CA  . VAL   A 1 369 ? 17.616  52.779  -43.375 1.00 119.17 ? 438  VAL   A CA  1 
ATOM   2616  C  C   . VAL   A 1 369 ? 18.798  51.800  -43.355 1.00 117.26 ? 438  VAL   A C   1 
ATOM   2617  O  O   . VAL   A 1 369 ? 19.126  51.196  -44.375 1.00 121.02 ? 438  VAL   A O   1 
ATOM   2618  C  CB  . VAL   A 1 369 ? 16.321  52.048  -43.791 1.00 118.07 ? 438  VAL   A CB  1 
ATOM   2619  C  CG1 . VAL   A 1 369 ? 15.098  52.872  -43.432 1.00 116.78 ? 438  VAL   A CG1 1 
ATOM   2620  C  CG2 . VAL   A 1 369 ? 16.343  51.735  -45.296 1.00 121.83 ? 438  VAL   A CG2 1 
ATOM   2621  N  N   . ILE   A 1 370 ? 19.433  51.636  -42.195 1.00 112.95 ? 439  ILE   A N   1 
ATOM   2622  C  CA  . ILE   A 1 370 ? 20.577  50.744  -42.049 1.00 110.48 ? 439  ILE   A CA  1 
ATOM   2623  C  C   . ILE   A 1 370 ? 20.268  49.652  -41.024 1.00 104.48 ? 439  ILE   A C   1 
ATOM   2624  O  O   . ILE   A 1 370 ? 19.309  49.733  -40.254 1.00 100.77 ? 439  ILE   A O   1 
ATOM   2625  C  CB  . ILE   A 1 370 ? 21.847  51.492  -41.629 1.00 104.01 ? 439  ILE   A CB  1 
ATOM   2626  C  CG1 . ILE   A 1 370 ? 21.923  52.827  -42.332 1.00 100.78 ? 439  ILE   A CG1 1 
ATOM   2627  C  CG2 . ILE   A 1 370 ? 23.059  50.644  -41.945 1.00 107.88 ? 439  ILE   A CG2 1 
ATOM   2628  C  CD1 . ILE   A 1 370 ? 23.090  53.631  -41.889 1.00 100.63 ? 439  ILE   A CD1 1 
ATOM   2629  N  N   . LEU   A 1 371 ? 21.128  48.639  -41.003 1.00 99.46  ? 440  LEU   A N   1 
ATOM   2630  C  CA  . LEU   A 1 371 ? 21.083  47.628  -39.962 1.00 99.67  ? 440  LEU   A CA  1 
ATOM   2631  C  C   . LEU   A 1 371 ? 21.959  48.051  -38.783 1.00 100.75 ? 440  LEU   A C   1 
ATOM   2632  O  O   . LEU   A 1 371 ? 23.087  48.519  -38.971 1.00 99.28  ? 440  LEU   A O   1 
ATOM   2633  C  CB  . LEU   A 1 371 ? 21.526  46.275  -40.519 1.00 98.69  ? 440  LEU   A CB  1 
ATOM   2634  C  CG  . LEU   A 1 371 ? 20.611  45.660  -41.590 1.00 94.52  ? 440  LEU   A CG  1 
ATOM   2635  C  CD1 . LEU   A 1 371 ? 19.159  45.672  -41.125 1.00 92.14  ? 440  LEU   A CD1 1 
ATOM   2636  C  CD2 . LEU   A 1 371 ? 20.750  46.368  -42.937 1.00 103.64 ? 440  LEU   A CD2 1 
ATOM   2637  N  N   . CYS   A 1 372 ? 21.435  47.868  -37.567 1.00 99.07  ? 441  CYS   A N   1 
ATOM   2638  C  CA  . CYS   A 1 372 ? 21.993  48.416  -36.337 1.00 96.77  ? 441  CYS   A CA  1 
ATOM   2639  C  C   . CYS   A 1 372 ? 22.613  47.339  -35.443 1.00 95.68  ? 441  CYS   A C   1 
ATOM   2640  O  O   . CYS   A 1 372 ? 22.257  46.158  -35.508 1.00 95.32  ? 441  CYS   A O   1 
ATOM   2641  C  CB  . CYS   A 1 372 ? 20.900  49.155  -35.567 1.00 99.02  ? 441  CYS   A CB  1 
ATOM   2642  S  SG  . CYS   A 1 372 ? 21.435  50.712  -34.848 1.00 106.12 ? 441  CYS   A SG  1 
ATOM   2643  N  N   . LEU   A 1 373 ? 23.540  47.770  -34.585 1.00 96.06  ? 442  LEU   A N   1 
ATOM   2644  C  CA  . LEU   A 1 373 ? 24.206  46.888  -33.605 1.00 98.52  ? 442  LEU   A CA  1 
ATOM   2645  C  C   . LEU   A 1 373 ? 23.784  47.209  -32.152 1.00 97.67  ? 442  LEU   A C   1 
ATOM   2646  O  O   . LEU   A 1 373 ? 24.624  47.361  -31.234 1.00 94.67  ? 442  LEU   A O   1 
ATOM   2647  C  CB  . LEU   A 1 373 ? 25.734  46.991  -33.711 1.00 92.89  ? 442  LEU   A CB  1 
ATOM   2648  C  CG  . LEU   A 1 373 ? 26.378  47.210  -35.072 1.00 94.05  ? 442  LEU   A CG  1 
ATOM   2649  C  CD1 . LEU   A 1 373 ? 27.884  47.335  -34.883 1.00 95.89  ? 442  LEU   A CD1 1 
ATOM   2650  C  CD2 . LEU   A 1 373 ? 26.023  46.102  -36.065 1.00 98.82  ? 442  LEU   A CD2 1 
ATOM   2651  O  OXT . LEU   A 1 373 ? 22.584  47.325  -31.865 1.00 95.01  ? 442  LEU   A OXT 1 
ATOM   2652  N  N   . SER   B 2 2   ? 45.750  61.578  -24.106 1.00 109.34 ? 2    SER   B N   1 
ATOM   2653  C  CA  . SER   B 2 2   ? 46.287  62.505  -23.125 1.00 111.93 ? 2    SER   B CA  1 
ATOM   2654  C  C   . SER   B 2 2   ? 46.666  61.804  -21.828 1.00 111.06 ? 2    SER   B C   1 
ATOM   2655  O  O   . SER   B 2 2   ? 46.860  60.595  -21.766 1.00 111.15 ? 2    SER   B O   1 
ATOM   2656  C  CB  . SER   B 2 2   ? 45.279  63.637  -22.833 1.00 109.75 ? 2    SER   B CB  1 
ATOM   2657  O  OG  . SER   B 2 2   ? 44.087  63.160  -22.231 1.00 104.78 ? 2    SER   B OG  1 
ATOM   2658  N  N   . TYR   B 2 3   ? 46.772  62.602  -20.783 1.00 110.22 ? 3    TYR   B N   1 
ATOM   2659  C  CA  . TYR   B 2 3   ? 47.094  62.120  -19.458 1.00 110.37 ? 3    TYR   B CA  1 
ATOM   2660  C  C   . TYR   B 2 3   ? 46.169  62.842  -18.496 1.00 111.87 ? 3    TYR   B C   1 
ATOM   2661  O  O   . TYR   B 2 3   ? 45.991  64.060  -18.607 1.00 111.60 ? 3    TYR   B O   1 
ATOM   2662  C  CB  . TYR   B 2 3   ? 48.550  62.407  -19.125 1.00 117.59 ? 3    TYR   B CB  1 
ATOM   2663  C  CG  . TYR   B 2 3   ? 49.529  62.120  -20.242 1.00 122.54 ? 3    TYR   B CG  1 
ATOM   2664  C  CD1 . TYR   B 2 3   ? 50.025  60.836  -20.433 1.00 123.69 ? 3    TYR   B CD1 1 
ATOM   2665  C  CD2 . TYR   B 2 3   ? 49.988  63.139  -21.076 1.00 121.22 ? 3    TYR   B CD2 1 
ATOM   2666  C  CE1 . TYR   B 2 3   ? 50.942  60.570  -21.432 1.00 126.56 ? 3    TYR   B CE1 1 
ATOM   2667  C  CE2 . TYR   B 2 3   ? 50.907  62.883  -22.076 1.00 121.92 ? 3    TYR   B CE2 1 
ATOM   2668  C  CZ  . TYR   B 2 3   ? 51.381  61.596  -22.249 1.00 123.94 ? 3    TYR   B CZ  1 
ATOM   2669  O  OH  . TYR   B 2 3   ? 52.297  61.319  -23.240 1.00 122.75 ? 3    TYR   B OH  1 
ATOM   2670  N  N   . ASN   B 2 4   ? 45.557  62.106  -17.577 1.00 106.67 ? 4    ASN   B N   1 
ATOM   2671  C  CA  . ASN   B 2 4   ? 44.500  62.687  -16.766 1.00 105.29 ? 4    ASN   B CA  1 
ATOM   2672  C  C   . ASN   B 2 4   ? 44.702  62.421  -15.280 1.00 102.90 ? 4    ASN   B C   1 
ATOM   2673  O  O   . ASN   B 2 4   ? 45.439  61.520  -14.871 1.00 103.45 ? 4    ASN   B O   1 
ATOM   2674  C  CB  . ASN   B 2 4   ? 43.145  62.195  -17.246 1.00 102.88 ? 4    ASN   B CB  1 
ATOM   2675  C  CG  . ASN   B 2 4   ? 42.761  62.823  -18.565 1.00 109.72 ? 4    ASN   B CG  1 
ATOM   2676  O  OD1 . ASN   B 2 4   ? 41.882  63.693  -18.612 1.00 111.37 ? 4    ASN   B OD1 1 
ATOM   2677  N  ND2 . ASN   B 2 4   ? 43.426  62.423  -19.631 1.00 113.71 ? 4    ASN   B ND2 1 
ATOM   2678  N  N   . TYR   B 2 5   ? 44.080  63.282  -14.477 1.00 101.10 ? 5    TYR   B N   1 
ATOM   2679  C  CA  . TYR   B 2 5   ? 44.182  63.243  -13.026 1.00 97.63  ? 5    TYR   B CA  1 
ATOM   2680  C  C   . TYR   B 2 5   ? 42.769  63.192  -12.449 1.00 101.54 ? 5    TYR   B C   1 
ATOM   2681  O  O   . TYR   B 2 5   ? 41.913  64.002  -12.820 1.00 99.75  ? 5    TYR   B O   1 
ATOM   2682  C  CB  . TYR   B 2 5   ? 44.977  64.455  -12.545 1.00 94.75  ? 5    TYR   B CB  1 
ATOM   2683  C  CG  . TYR   B 2 5   ? 45.123  64.733  -11.047 1.00 94.55  ? 5    TYR   B CG  1 
ATOM   2684  C  CD1 . TYR   B 2 5   ? 44.232  65.583  -10.392 1.00 94.40  ? 5    TYR   B CD1 1 
ATOM   2685  C  CD2 . TYR   B 2 5   ? 46.209  64.251  -10.310 1.00 96.16  ? 5    TYR   B CD2 1 
ATOM   2686  C  CE1 . TYR   B 2 5   ? 44.370  65.907  -9.025  1.00 94.79  ? 5    TYR   B CE1 1 
ATOM   2687  C  CE2 . TYR   B 2 5   ? 46.362  64.571  -8.915  1.00 98.49  ? 5    TYR   B CE2 1 
ATOM   2688  C  CZ  . TYR   B 2 5   ? 45.429  65.409  -8.283  1.00 100.59 ? 5    TYR   B CZ  1 
ATOM   2689  O  OH  . TYR   B 2 5   ? 45.512  65.771  -6.935  1.00 95.82  ? 5    TYR   B OH  1 
ATOM   2690  N  N   . VAL   B 2 6   ? 42.518  62.196  -11.588 1.00 100.80 ? 6    VAL   B N   1 
ATOM   2691  C  CA  . VAL   B 2 6   ? 41.228  61.959  -10.945 1.00 90.57  ? 6    VAL   B CA  1 
ATOM   2692  C  C   . VAL   B 2 6   ? 41.383  62.254  -9.462  1.00 88.99  ? 6    VAL   B C   1 
ATOM   2693  O  O   . VAL   B 2 6   ? 42.392  61.880  -8.852  1.00 89.56  ? 6    VAL   B O   1 
ATOM   2694  C  CB  . VAL   B 2 6   ? 40.771  60.503  -11.152 1.00 88.49  ? 6    VAL   B CB  1 
ATOM   2695  C  CG1 . VAL   B 2 6   ? 39.400  60.293  -10.590 1.00 89.90  ? 6    VAL   B CG1 1 
ATOM   2696  C  CG2 . VAL   B 2 6   ? 40.815  60.130  -12.605 1.00 91.16  ? 6    VAL   B CG2 1 
ATOM   2697  N  N   . VAL   B 2 7   ? 40.394  62.917  -8.871  1.00 87.48  ? 7    VAL   B N   1 
ATOM   2698  C  CA  . VAL   B 2 7   ? 40.429  63.156  -7.430  1.00 92.80  ? 7    VAL   B CA  1 
ATOM   2699  C  C   . VAL   B 2 7   ? 39.014  63.082  -6.896  1.00 91.08  ? 7    VAL   B C   1 
ATOM   2700  O  O   . VAL   B 2 7   ? 38.056  63.489  -7.564  1.00 88.51  ? 7    VAL   B O   1 
ATOM   2701  C  CB  . VAL   B 2 7   ? 41.069  64.516  -7.043  1.00 96.20  ? 7    VAL   B CB  1 
ATOM   2702  C  CG1 . VAL   B 2 7   ? 40.266  65.659  -7.616  1.00 91.37  ? 7    VAL   B CG1 1 
ATOM   2703  C  CG2 . VAL   B 2 7   ? 41.175  64.648  -5.511  1.00 93.92  ? 7    VAL   B CG2 1 
ATOM   2704  N  N   . THR   B 2 8   ? 38.890  62.573  -5.673  1.00 88.84  ? 8    THR   B N   1 
ATOM   2705  C  CA  . THR   B 2 8   ? 37.588  62.525  -5.036  1.00 88.19  ? 8    THR   B CA  1 
ATOM   2706  C  C   . THR   B 2 8   ? 37.255  63.882  -4.451  1.00 92.73  ? 8    THR   B C   1 
ATOM   2707  O  O   . THR   B 2 8   ? 38.036  64.458  -3.680  1.00 92.79  ? 8    THR   B O   1 
ATOM   2708  C  CB  . THR   B 2 8   ? 37.519  61.465  -3.958  1.00 83.87  ? 8    THR   B CB  1 
ATOM   2709  O  OG1 . THR   B 2 8   ? 37.345  60.189  -4.596  1.00 91.96  ? 8    THR   B OG1 1 
ATOM   2710  C  CG2 . THR   B 2 8   ? 36.328  61.762  -3.051  1.00 81.50  ? 8    THR   B CG2 1 
ATOM   2711  N  N   . ALA   B 2 9   ? 36.095  64.389  -4.838  1.00 90.55  ? 9    ALA   B N   1 
ATOM   2712  C  CA  . ALA   B 2 9   ? 35.547  65.611  -4.295  1.00 81.91  ? 9    ALA   B CA  1 
ATOM   2713  C  C   . ALA   B 2 9   ? 34.511  65.331  -3.236  1.00 83.29  ? 9    ALA   B C   1 
ATOM   2714  O  O   . ALA   B 2 9   ? 34.269  66.173  -2.374  1.00 87.35  ? 9    ALA   B O   1 
ATOM   2715  C  CB  . ALA   B 2 9   ? 34.914  66.427  -5.412  1.00 87.05  ? 9    ALA   B CB  1 
ATOM   2716  N  N   . GLN   B 2 10  ? 33.897  64.158  -3.285  1.00 82.78  ? 10   GLN   B N   1 
ATOM   2717  C  CA  . GLN   B 2 10  ? 32.937  63.762  -2.269  1.00 83.27  ? 10   GLN   B CA  1 
ATOM   2718  C  C   . GLN   B 2 10  ? 33.018  62.256  -2.114  1.00 86.87  ? 10   GLN   B C   1 
ATOM   2719  O  O   . GLN   B 2 10  ? 32.768  61.531  -3.084  1.00 89.88  ? 10   GLN   B O   1 
ATOM   2720  C  CB  . GLN   B 2 10  ? 31.516  64.198  -2.641  1.00 81.17  ? 10   GLN   B CB  1 
ATOM   2721  C  CG  . GLN   B 2 10  ? 30.426  63.572  -1.774  1.00 79.89  ? 10   GLN   B CG  1 
ATOM   2722  C  CD  . GLN   B 2 10  ? 30.661  63.774  -0.277  1.00 84.42  ? 10   GLN   B CD  1 
ATOM   2723  O  OE1 . GLN   B 2 10  ? 30.521  64.883  0.247   1.00 86.58  ? 10   GLN   B OE1 1 
ATOM   2724  N  NE2 . GLN   B 2 10  ? 31.015  62.699  0.417   1.00 85.67  ? 10   GLN   B NE2 1 
ATOM   2725  N  N   . LYS   B 2 11  ? 33.377  61.790  -0.908  1.00 84.67  ? 11   LYS   B N   1 
ATOM   2726  C  CA  . LYS   B 2 11  ? 33.392  60.361  -0.633  1.00 81.96  ? 11   LYS   B CA  1 
ATOM   2727  C  C   . LYS   B 2 11  ? 32.016  59.749  -0.910  1.00 83.89  ? 11   LYS   B C   1 
ATOM   2728  O  O   . LYS   B 2 11  ? 30.997  60.444  -0.901  1.00 81.50  ? 11   LYS   B O   1 
ATOM   2729  C  CB  . LYS   B 2 11  ? 33.803  60.097  0.823   1.00 87.52  ? 11   LYS   B CB  1 
ATOM   2730  C  CG  . LYS   B 2 11  ? 35.298  59.805  1.044   1.00 90.82  ? 11   LYS   B CG  1 
ATOM   2731  C  CD  . LYS   B 2 11  ? 35.671  59.621  2.523   1.00 90.77  ? 11   LYS   B CD  1 
ATOM   2732  C  CE  . LYS   B 2 11  ? 36.192  60.911  3.127   1.00 95.30  ? 11   LYS   B CE  1 
ATOM   2733  N  NZ  . LYS   B 2 11  ? 36.325  60.847  4.610   1.00 99.03  ? 11   LYS   B NZ  1 
ATOM   2734  N  N   . PRO   B 2 12  ? 31.959  58.442  -1.167  1.00 86.52  ? 12   PRO   B N   1 
ATOM   2735  C  CA  . PRO   B 2 12  ? 30.653  57.781  -1.291  1.00 83.35  ? 12   PRO   B CA  1 
ATOM   2736  C  C   . PRO   B 2 12  ? 29.834  57.978  -0.025  1.00 79.87  ? 12   PRO   B C   1 
ATOM   2737  O  O   . PRO   B 2 12  ? 30.369  57.963  1.083   1.00 80.66  ? 12   PRO   B O   1 
ATOM   2738  C  CB  . PRO   B 2 12  ? 31.025  56.307  -1.515  1.00 82.06  ? 12   PRO   B CB  1 
ATOM   2739  C  CG  . PRO   B 2 12  ? 32.468  56.192  -1.099  1.00 80.19  ? 12   PRO   B CG  1 
ATOM   2740  C  CD  . PRO   B 2 12  ? 33.063  57.511  -1.456  1.00 85.95  ? 12   PRO   B CD  1 
ATOM   2741  N  N   . THR   B 2 13  ? 28.525  58.177  -0.198  1.00 76.47  ? 13   THR   B N   1 
ATOM   2742  C  CA  . THR   B 2 13  ? 27.643  58.405  0.939   1.00 78.94  ? 13   THR   B CA  1 
ATOM   2743  C  C   . THR   B 2 13  ? 26.638  57.293  1.171   1.00 79.65  ? 13   THR   B C   1 
ATOM   2744  O  O   . THR   B 2 13  ? 26.060  57.222  2.258   1.00 82.49  ? 13   THR   B O   1 
ATOM   2745  C  CB  . THR   B 2 13  ? 26.855  59.713  0.777   1.00 85.02  ? 13   THR   B CB  1 
ATOM   2746  O  OG1 . THR   B 2 13  ? 25.915  59.573  -0.302  1.00 85.83  ? 13   THR   B OG1 1 
ATOM   2747  C  CG2 . THR   B 2 13  ? 27.793  60.877  0.494   1.00 80.80  ? 13   THR   B CG2 1 
ATOM   2748  N  N   . ALA   B 2 14  ? 26.399  56.446  0.184   1.00 85.05  ? 14   ALA   B N   1 
ATOM   2749  C  CA  . ALA   B 2 14  ? 25.459  55.357  0.369   1.00 79.95  ? 14   ALA   B CA  1 
ATOM   2750  C  C   . ALA   B 2 14  ? 26.062  54.336  1.306   1.00 80.73  ? 14   ALA   B C   1 
ATOM   2751  O  O   . ALA   B 2 14  ? 27.255  54.034  1.228   1.00 80.65  ? 14   ALA   B O   1 
ATOM   2752  C  CB  . ALA   B 2 14  ? 25.122  54.710  -0.968  1.00 83.48  ? 14   ALA   B CB  1 
ATOM   2753  N  N   . VAL   B 2 15  ? 25.245  53.821  2.207   1.00 83.54  ? 15   VAL   B N   1 
ATOM   2754  C  CA  . VAL   B 2 15  ? 25.685  52.776  3.125   1.00 84.76  ? 15   VAL   B CA  1 
ATOM   2755  C  C   . VAL   B 2 15  ? 25.373  51.421  2.500   1.00 86.12  ? 15   VAL   B C   1 
ATOM   2756  O  O   . VAL   B 2 15  ? 24.265  51.197  2.007   1.00 87.78  ? 15   VAL   B O   1 
ATOM   2757  C  CB  . VAL   B 2 15  ? 25.004  52.934  4.492   1.00 87.65  ? 15   VAL   B CB  1 
ATOM   2758  C  CG1 . VAL   B 2 15  ? 25.477  51.847  5.420   1.00 87.71  ? 15   VAL   B CG1 1 
ATOM   2759  C  CG2 . VAL   B 2 15  ? 25.268  54.341  5.077   1.00 82.52  ? 15   VAL   B CG2 1 
ATOM   2760  N  N   . ASN   B 2 16  ? 26.347  50.522  2.469   1.00 95.35  ? 16   ASN   B N   1 
ATOM   2761  C  CA  . ASN   B 2 16  ? 26.076  49.225  1.866   1.00 94.82  ? 16   ASN   B CA  1 
ATOM   2762  C  C   . ASN   B 2 16  ? 26.135  48.069  2.858   1.00 95.07  ? 16   ASN   B C   1 
ATOM   2763  O  O   . ASN   B 2 16  ? 25.932  46.918  2.458   1.00 102.81 ? 16   ASN   B O   1 
ATOM   2764  C  CB  . ASN   B 2 16  ? 27.033  48.955  0.698   1.00 98.50  ? 16   ASN   B CB  1 
ATOM   2765  C  CG  . ASN   B 2 16  ? 28.450  48.826  1.147   1.00 98.07  ? 16   ASN   B CG  1 
ATOM   2766  O  OD1 . ASN   B 2 16  ? 28.724  48.231  2.179   1.00 99.24  ? 16   ASN   B OD1 1 
ATOM   2767  N  ND2 . ASN   B 2 16  ? 29.369  49.395  0.386   1.00 99.38  ? 16   ASN   B ND2 1 
ATOM   2768  N  N   . GLY   B 2 17  ? 26.397  48.335  4.130   1.00 86.97  ? 17   GLY   B N   1 
ATOM   2769  C  CA  . GLY   B 2 17  ? 26.476  47.285  5.117   1.00 86.07  ? 17   GLY   B CA  1 
ATOM   2770  C  C   . GLY   B 2 17  ? 26.884  47.820  6.476   1.00 90.60  ? 17   GLY   B C   1 
ATOM   2771  O  O   . GLY   B 2 17  ? 27.687  48.759  6.577   1.00 86.39  ? 17   GLY   B O   1 
ATOM   2772  N  N   . CYS   B 2 18  ? 26.357  47.199  7.532   1.00 89.52  ? 18   CYS   B N   1 
ATOM   2773  C  CA  . CYS   B 2 18  ? 26.429  47.758  8.873   1.00 80.31  ? 18   CYS   B CA  1 
ATOM   2774  C  C   . CYS   B 2 18  ? 26.396  46.624  9.875   1.00 89.05  ? 18   CYS   B C   1 
ATOM   2775  O  O   . CYS   B 2 18  ? 25.405  45.893  9.939   1.00 91.05  ? 18   CYS   B O   1 
ATOM   2776  C  CB  . CYS   B 2 18  ? 25.269  48.708  9.115   1.00 78.97  ? 18   CYS   B CB  1 
ATOM   2777  S  SG  . CYS   B 2 18  ? 23.599  48.078  8.742   1.00 94.12  ? 18   CYS   B SG  1 
ATOM   2778  N  N   . VAL   B 2 19  ? 27.463  46.482  10.658  1.00 90.21  ? 19   VAL   B N   1 
ATOM   2779  C  CA  . VAL   B 2 19  ? 27.528  45.440  11.665  1.00 85.67  ? 19   VAL   B CA  1 
ATOM   2780  C  C   . VAL   B 2 19  ? 27.765  46.067  13.024  1.00 88.18  ? 19   VAL   B C   1 
ATOM   2781  O  O   . VAL   B 2 19  ? 28.423  47.106  13.157  1.00 82.86  ? 19   VAL   B O   1 
ATOM   2782  C  CB  . VAL   B 2 19  ? 28.620  44.404  11.356  1.00 89.22  ? 19   VAL   B CB  1 
ATOM   2783  C  CG1 . VAL   B 2 19  ? 28.296  43.696  10.053  1.00 92.14  ? 19   VAL   B CG1 1 
ATOM   2784  C  CG2 . VAL   B 2 19  ? 29.998  45.066  11.323  1.00 86.51  ? 19   VAL   B CG2 1 
ATOM   2785  N  N   . THR   B 2 20  ? 27.224  45.398  14.042  1.00 95.49  ? 20   THR   B N   1 
ATOM   2786  C  CA  . THR   B 2 20  ? 27.243  45.854  15.429  1.00 93.42  ? 20   THR   B CA  1 
ATOM   2787  C  C   . THR   B 2 20  ? 27.970  44.805  16.265  1.00 93.23  ? 20   THR   B C   1 
ATOM   2788  O  O   . THR   B 2 20  ? 27.530  43.653  16.341  1.00 92.30  ? 20   THR   B O   1 
ATOM   2789  C  CB  . THR   B 2 20  ? 25.818  46.100  15.959  1.00 88.63  ? 20   THR   B CB  1 
ATOM   2790  O  OG1 . THR   B 2 20  ? 25.857  46.167  17.375  1.00 93.79  ? 20   THR   B OG1 1 
ATOM   2791  C  CG2 . THR   B 2 20  ? 24.840  44.977  15.563  1.00 95.23  ? 20   THR   B CG2 1 
ATOM   2792  N  N   . GLY   B 2 21  ? 29.072  45.200  16.885  1.00 96.67  ? 21   GLY   B N   1 
ATOM   2793  C  CA  . GLY   B 2 21  ? 29.921  44.265  17.594  1.00 97.98  ? 21   GLY   B CA  1 
ATOM   2794  C  C   . GLY   B 2 21  ? 30.856  44.946  18.590  1.00 100.39 ? 21   GLY   B C   1 
ATOM   2795  O  O   . GLY   B 2 21  ? 30.569  46.031  19.105  1.00 97.67  ? 21   GLY   B O   1 
ATOM   2796  N  N   . HIS   B 2 22  ? 32.010  44.288  18.861  1.00 101.37 ? 22   HIS   B N   1 
ATOM   2797  C  CA  . HIS   B 2 22  ? 32.957  44.728  19.899  1.00 100.20 ? 22   HIS   B CA  1 
ATOM   2798  C  C   . HIS   B 2 22  ? 34.375  44.821  19.331  1.00 99.40  ? 22   HIS   B C   1 
ATOM   2799  O  O   . HIS   B 2 22  ? 35.259  44.026  19.685  1.00 98.38  ? 22   HIS   B O   1 
ATOM   2800  C  CB  . HIS   B 2 22  ? 32.913  43.791  21.098  1.00 99.09  ? 22   HIS   B CB  1 
ATOM   2801  C  CG  . HIS   B 2 22  ? 31.548  43.657  21.684  1.00 101.67 ? 22   HIS   B CG  1 
ATOM   2802  N  ND1 . HIS   B 2 22  ? 30.979  44.645  22.459  1.00 105.27 ? 22   HIS   B ND1 1 
ATOM   2803  C  CD2 . HIS   B 2 22  ? 30.623  42.673  21.586  1.00 98.04  ? 22   HIS   B CD2 1 
ATOM   2804  C  CE1 . HIS   B 2 22  ? 29.768  44.268  22.828  1.00 103.26 ? 22   HIS   B CE1 1 
ATOM   2805  N  NE2 . HIS   B 2 22  ? 29.528  43.074  22.314  1.00 97.08  ? 22   HIS   B NE2 1 
ATOM   2806  N  N   . PHE   B 2 23  ? 34.588  45.822  18.478  1.00 98.02  ? 23   PHE   B N   1 
ATOM   2807  C  CA  . PHE   B 2 23  ? 35.813  45.961  17.699  1.00 98.55  ? 23   PHE   B CA  1 
ATOM   2808  C  C   . PHE   B 2 23  ? 36.856  46.843  18.378  1.00 98.23  ? 23   PHE   B C   1 
ATOM   2809  O  O   . PHE   B 2 23  ? 38.057  46.570  18.254  1.00 100.66 ? 23   PHE   B O   1 
ATOM   2810  C  CB  . PHE   B 2 23  ? 35.467  46.520  16.314  1.00 96.77  ? 23   PHE   B CB  1 
ATOM   2811  C  CG  . PHE   B 2 23  ? 36.592  46.445  15.342  1.00 96.08  ? 23   PHE   B CG  1 
ATOM   2812  C  CD1 . PHE   B 2 23  ? 37.243  45.247  15.130  1.00 95.02  ? 23   PHE   B CD1 1 
ATOM   2813  C  CD2 . PHE   B 2 23  ? 37.009  47.574  14.653  1.00 93.64  ? 23   PHE   B CD2 1 
ATOM   2814  C  CE1 . PHE   B 2 23  ? 38.289  45.167  14.241  1.00 95.76  ? 23   PHE   B CE1 1 
ATOM   2815  C  CE2 . PHE   B 2 23  ? 38.053  47.502  13.766  1.00 95.51  ? 23   PHE   B CE2 1 
ATOM   2816  C  CZ  . PHE   B 2 23  ? 38.697  46.295  13.557  1.00 96.08  ? 23   PHE   B CZ  1 
ATOM   2817  N  N   . THR   B 2 24  ? 36.424  47.903  19.083  1.00 103.75 ? 24   THR   B N   1 
ATOM   2818  C  CA  . THR   B 2 24  ? 37.324  48.859  19.730  1.00 108.27 ? 24   THR   B CA  1 
ATOM   2819  C  C   . THR   B 2 24  ? 37.762  48.399  21.125  1.00 105.73 ? 24   THR   B C   1 
ATOM   2820  O  O   . THR   B 2 24  ? 38.855  48.756  21.580  1.00 103.13 ? 24   THR   B O   1 
ATOM   2821  C  CB  . THR   B 2 24  ? 36.676  50.257  19.815  1.00 103.10 ? 24   THR   B CB  1 
ATOM   2822  O  OG1 . THR   B 2 24  ? 35.630  50.283  20.795  1.00 104.95 ? 24   THR   B OG1 1 
ATOM   2823  C  CG2 . THR   B 2 24  ? 36.098  50.682  18.468  1.00 97.79  ? 24   THR   B CG2 1 
ATOM   2824  N  N   . SER   B 2 25  ? 36.961  47.583  21.798  1.00 103.95 ? 25   SER   B N   1 
ATOM   2825  C  CA  . SER   B 2 25  ? 37.323  47.018  23.089  1.00 103.64 ? 25   SER   B CA  1 
ATOM   2826  C  C   . SER   B 2 25  ? 36.221  46.043  23.443  1.00 104.35 ? 25   SER   B C   1 
ATOM   2827  O  O   . SER   B 2 25  ? 35.139  46.081  22.850  1.00 107.70 ? 25   SER   B O   1 
ATOM   2828  C  CB  . SER   B 2 25  ? 37.443  48.084  24.185  1.00 105.06 ? 25   SER   B CB  1 
ATOM   2829  O  OG  . SER   B 2 25  ? 36.262  48.114  24.970  1.00 110.32 ? 25   SER   B OG  1 
ATOM   2830  N  N   . ALA   B 2 26  ? 36.495  45.163  24.396  1.00 100.20 ? 26   ALA   B N   1 
ATOM   2831  C  CA  . ALA   B 2 26  ? 35.473  44.184  24.704  1.00 101.74 ? 26   ALA   B CA  1 
ATOM   2832  C  C   . ALA   B 2 26  ? 34.259  44.819  25.375  1.00 107.91 ? 26   ALA   B C   1 
ATOM   2833  O  O   . ALA   B 2 26  ? 33.167  44.249  25.300  1.00 109.50 ? 26   ALA   B O   1 
ATOM   2834  C  CB  . ALA   B 2 26  ? 36.060  43.068  25.559  1.00 107.33 ? 26   ALA   B CB  1 
ATOM   2835  N  N   . GLU   B 2 27  ? 34.416  46.005  25.978  1.00 118.90 ? 27   GLU   B N   1 
ATOM   2836  C  CA  . GLU   B 2 27  ? 33.378  46.660  26.772  1.00 122.17 ? 27   GLU   B CA  1 
ATOM   2837  C  C   . GLU   B 2 27  ? 32.578  47.705  25.989  1.00 125.20 ? 27   GLU   B C   1 
ATOM   2838  O  O   . GLU   B 2 27  ? 31.636  48.280  26.553  1.00 130.67 ? 27   GLU   B O   1 
ATOM   2839  C  CB  . GLU   B 2 27  ? 33.989  47.327  28.019  1.00 121.00 ? 27   GLU   B CB  1 
ATOM   2840  N  N   . ASP   B 2 28  ? 32.924  47.966  24.727  1.00 118.18 ? 28   ASP   B N   1 
ATOM   2841  C  CA  . ASP   B 2 28  ? 32.252  48.957  23.886  1.00 113.23 ? 28   ASP   B CA  1 
ATOM   2842  C  C   . ASP   B 2 28  ? 31.307  48.279  22.892  1.00 110.35 ? 28   ASP   B C   1 
ATOM   2843  O  O   . ASP   B 2 28  ? 31.618  47.215  22.338  1.00 108.43 ? 28   ASP   B O   1 
ATOM   2844  C  CB  . ASP   B 2 28  ? 33.259  49.816  23.112  1.00 105.86 ? 28   ASP   B CB  1 
ATOM   2845  C  CG  . ASP   B 2 28  ? 34.369  50.343  23.981  1.00 111.14 ? 28   ASP   B CG  1 
ATOM   2846  O  OD1 . ASP   B 2 28  ? 34.263  50.206  25.214  1.00 118.87 ? 28   ASP   B OD1 1 
ATOM   2847  O  OD2 . ASP   B 2 28  ? 35.357  50.879  23.434  1.00 111.28 ? 28   ASP   B OD2 1 
ATOM   2848  N  N   . LEU   B 2 29  ? 30.151  48.901  22.681  1.00 107.69 ? 29   LEU   B N   1 
ATOM   2849  C  CA  . LEU   B 2 29  ? 29.259  48.552  21.586  1.00 104.38 ? 29   LEU   B CA  1 
ATOM   2850  C  C   . LEU   B 2 29  ? 29.635  49.427  20.396  1.00 104.22 ? 29   LEU   B C   1 
ATOM   2851  O  O   . LEU   B 2 29  ? 29.435  50.645  20.429  1.00 106.67 ? 29   LEU   B O   1 
ATOM   2852  C  CB  . LEU   B 2 29  ? 27.797  48.761  21.976  1.00 100.13 ? 29   LEU   B CB  1 
ATOM   2853  C  CG  . LEU   B 2 29  ? 26.835  48.068  20.998  1.00 103.09 ? 29   LEU   B CG  1 
ATOM   2854  C  CD1 . LEU   B 2 29  ? 27.398  46.734  20.494  1.00 99.68  ? 29   LEU   B CD1 1 
ATOM   2855  C  CD2 . LEU   B 2 29  ? 25.444  47.877  21.593  1.00 101.15 ? 29   LEU   B CD2 1 
ATOM   2856  N  N   . ASN   B 2 30  ? 30.194  48.819  19.352  1.00 101.61 ? 30   ASN   B N   1 
ATOM   2857  C  CA  . ASN   B 2 30  ? 30.546  49.555  18.152  1.00 99.60  ? 30   ASN   B CA  1 
ATOM   2858  C  C   . ASN   B 2 30  ? 29.530  49.294  17.053  1.00 99.33  ? 30   ASN   B C   1 
ATOM   2859  O  O   . ASN   B 2 30  ? 28.860  48.251  17.016  1.00 97.00  ? 30   ASN   B O   1 
ATOM   2860  C  CB  . ASN   B 2 30  ? 31.924  49.179  17.625  1.00 97.01  ? 30   ASN   B CB  1 
ATOM   2861  C  CG  . ASN   B 2 30  ? 32.917  48.995  18.712  1.00 101.33 ? 30   ASN   B CG  1 
ATOM   2862  O  OD1 . ASN   B 2 30  ? 33.283  47.862  19.029  1.00 108.51 ? 30   ASN   B OD1 1 
ATOM   2863  N  ND2 . ASN   B 2 30  ? 33.369  50.096  19.303  1.00 102.61 ? 30   ASN   B ND2 1 
ATOM   2864  N  N   . LEU   B 2 31  ? 29.441  50.275  16.157  1.00 97.09  ? 31   LEU   B N   1 
ATOM   2865  C  CA  . LEU   B 2 31  ? 28.726  50.171  14.891  1.00 91.47  ? 31   LEU   B CA  1 
ATOM   2866  C  C   . LEU   B 2 31  ? 29.758  50.382  13.798  1.00 91.75  ? 31   LEU   B C   1 
ATOM   2867  O  O   . LEU   B 2 31  ? 30.292  51.486  13.665  1.00 92.38  ? 31   LEU   B O   1 
ATOM   2868  C  CB  . LEU   B 2 31  ? 27.626  51.211  14.806  1.00 88.80  ? 31   LEU   B CB  1 
ATOM   2869  C  CG  . LEU   B 2 31  ? 26.785  51.102  13.552  1.00 91.54  ? 31   LEU   B CG  1 
ATOM   2870  C  CD1 . LEU   B 2 31  ? 26.094  49.758  13.548  1.00 88.55  ? 31   LEU   B CD1 1 
ATOM   2871  C  CD2 . LEU   B 2 31  ? 25.786  52.249  13.516  1.00 96.38  ? 31   LEU   B CD2 1 
ATOM   2872  N  N   . LEU   B 2 32  ? 30.079  49.332  13.045  1.00 91.50  ? 32   LEU   B N   1 
ATOM   2873  C  CA  . LEU   B 2 32  ? 30.871  49.518  11.843  1.00 86.05  ? 32   LEU   B CA  1 
ATOM   2874  C  C   . LEU   B 2 32  ? 29.914  49.731  10.685  1.00 85.80  ? 32   LEU   B C   1 
ATOM   2875  O  O   . LEU   B 2 32  ? 28.896  49.039  10.584  1.00 86.40  ? 32   LEU   B O   1 
ATOM   2876  C  CB  . LEU   B 2 32  ? 31.791  48.330  11.586  1.00 86.62  ? 32   LEU   B CB  1 
ATOM   2877  C  CG  . LEU   B 2 32  ? 32.993  48.318  12.528  1.00 90.05  ? 32   LEU   B CG  1 
ATOM   2878  C  CD1 . LEU   B 2 32  ? 32.526  47.975  13.928  1.00 88.79  ? 32   LEU   B CD1 1 
ATOM   2879  C  CD2 . LEU   B 2 32  ? 34.071  47.347  12.052  1.00 87.80  ? 32   LEU   B CD2 1 
ATOM   2880  N  N   . ILE   B 2 33  ? 30.222  50.716  9.844   1.00 82.98  ? 33   ILE   B N   1 
ATOM   2881  C  CA  . ILE   B 2 33  ? 29.417  51.056  8.682   1.00 76.87  ? 33   ILE   B CA  1 
ATOM   2882  C  C   . ILE   B 2 33  ? 30.305  51.033  7.448   1.00 82.47  ? 33   ILE   B C   1 
ATOM   2883  O  O   . ILE   B 2 33  ? 31.458  51.483  7.488   1.00 81.52  ? 33   ILE   B O   1 
ATOM   2884  C  CB  . ILE   B 2 33  ? 28.750  52.435  8.825   1.00 83.49  ? 33   ILE   B CB  1 
ATOM   2885  C  CG1 . ILE   B 2 33  ? 27.380  52.311  9.479   1.00 85.10  ? 33   ILE   B CG1 1 
ATOM   2886  C  CG2 . ILE   B 2 33  ? 28.638  53.117  7.463   1.00 84.63  ? 33   ILE   B CG2 1 
ATOM   2887  C  CD1 . ILE   B 2 33  ? 26.766  53.663  9.810   1.00 88.70  ? 33   ILE   B CD1 1 
ATOM   2888  N  N   . ALA   B 2 34  ? 29.750  50.539  6.341   1.00 85.94  ? 34   ALA   B N   1 
ATOM   2889  C  CA  . ALA   B 2 34  ? 30.472  50.373  5.086   1.00 85.35  ? 34   ALA   B CA  1 
ATOM   2890  C  C   . ALA   B 2 34  ? 29.871  51.260  4.000   1.00 85.84  ? 34   ALA   B C   1 
ATOM   2891  O  O   . ALA   B 2 34  ? 28.675  51.171  3.700   1.00 89.24  ? 34   ALA   B O   1 
ATOM   2892  C  CB  . ALA   B 2 34  ? 30.447  48.902  4.657   1.00 76.82  ? 34   ALA   B CB  1 
ATOM   2893  N  N   . LYS   B 2 35  ? 30.705  52.095  3.393   1.00 82.91  ? 35   LYS   B N   1 
ATOM   2894  C  CA  . LYS   B 2 35  ? 30.303  52.898  2.224   1.00 85.21  ? 35   LYS   B CA  1 
ATOM   2895  C  C   . LYS   B 2 35  ? 31.295  52.654  1.104   1.00 87.46  ? 35   LYS   B C   1 
ATOM   2896  O  O   . LYS   B 2 35  ? 32.265  53.407  0.933   1.00 84.48  ? 35   LYS   B O   1 
ATOM   2897  C  CB  . LYS   B 2 35  ? 30.217  54.382  2.631   1.00 84.01  ? 35   LYS   B CB  1 
ATOM   2898  C  CG  . LYS   B 2 35  ? 29.249  54.634  3.790   1.00 85.26  ? 35   LYS   B CG  1 
ATOM   2899  C  CD  . LYS   B 2 35  ? 29.239  56.092  4.227   1.00 79.69  ? 35   LYS   B CD  1 
ATOM   2900  C  CE  . LYS   B 2 35  ? 28.734  56.215  5.659   1.00 86.75  ? 35   LYS   B CE  1 
ATOM   2901  N  NZ  . LYS   B 2 35  ? 28.324  57.576  6.141   1.00 79.19  ? 35   LYS   B NZ  1 
ATOM   2902  N  N   . ASN   B 2 36  ? 31.056  51.564  0.359   1.00 82.96  ? 36   ASN   B N   1 
ATOM   2903  C  CA  . ASN   B 2 36  ? 31.850  51.185  -0.826  1.00 84.10  ? 36   ASN   B CA  1 
ATOM   2904  C  C   . ASN   B 2 36  ? 33.213  51.239  -0.125  1.00 82.06  ? 36   ASN   B C   1 
ATOM   2905  O  O   . ASN   B 2 36  ? 33.426  50.619  0.915   1.00 80.40  ? 36   ASN   B O   1 
ATOM   2906  C  CB  . ASN   B 2 36  ? 31.734  52.237  -1.929  1.00 87.97  ? 36   ASN   B CB  1 
ATOM   2907  C  CG  . ASN   B 2 36  ? 31.947  51.644  -3.330  1.00 86.95  ? 36   ASN   B CG  1 
ATOM   2908  O  OD1 . ASN   B 2 36  ? 31.764  50.439  -3.543  1.00 93.30  ? 36   ASN   B OD1 1 
ATOM   2909  N  ND2 . ASN   B 2 36  ? 32.309  52.495  -4.292  1.00 80.79  ? 36   ASN   B ND2 1 
ATOM   2910  N  N   . THR   B 2 37  ? 34.139  51.984  -0.708  1.00 84.71  ? 37   THR   B N   1 
ATOM   2911  C  CA  . THR   B 2 37  ? 35.509  52.031  -0.234  1.00 81.65  ? 37   THR   B CA  1 
ATOM   2912  C  C   . THR   B 2 37  ? 35.822  52.370  1.200   1.00 85.15  ? 37   THR   B C   1 
ATOM   2913  O  O   . THR   B 2 37  ? 36.951  52.132  1.642   1.00 90.54  ? 37   THR   B O   1 
ATOM   2914  C  CB  . THR   B 2 37  ? 36.264  52.812  -1.302  1.00 87.92  ? 37   THR   B CB  1 
ATOM   2915  O  OG1 . THR   B 2 37  ? 35.853  54.189  -1.262  1.00 87.87  ? 37   THR   B OG1 1 
ATOM   2916  C  CG2 . THR   B 2 37  ? 35.969  52.240  -2.662  1.00 90.71  ? 37   THR   B CG2 1 
ATOM   2917  N  N   . ARG   B 2 38  ? 34.887  52.964  1.928   1.00 86.28  ? 38   ARG   B N   1 
ATOM   2918  C  CA  . ARG   B 2 38  ? 35.194  53.464  3.260   1.00 88.82  ? 38   ARG   B CA  1 
ATOM   2919  C  C   . ARG   B 2 38  ? 34.578  52.712  4.435   1.00 89.54  ? 38   ARG   B C   1 
ATOM   2920  O  O   . ARG   B 2 38  ? 33.407  52.315  4.390   1.00 86.62  ? 38   ARG   B O   1 
ATOM   2921  C  CB  . ARG   B 2 38  ? 34.676  54.910  3.182   1.00 88.56  ? 38   ARG   B CB  1 
ATOM   2922  C  CG  . ARG   B 2 38  ? 35.197  55.724  1.983   1.00 89.66  ? 38   ARG   B CG  1 
ATOM   2923  C  CD  . ARG   B 2 38  ? 36.704  55.980  2.025   1.00 90.85  ? 38   ARG   B CD  1 
ATOM   2924  N  NE  . ARG   B 2 38  ? 37.145  56.771  3.170   1.00 93.30  ? 38   ARG   B NE  1 
ATOM   2925  C  CZ  . ARG   B 2 38  ? 38.400  57.167  3.344   1.00 97.56  ? 38   ARG   B CZ  1 
ATOM   2926  N  NH1 . ARG   B 2 38  ? 39.332  56.911  2.437   1.00 98.19  ? 38   ARG   B NH1 1 
ATOM   2927  N  NH2 . ARG   B 2 38  ? 38.733  57.823  4.457   1.00 98.88  ? 38   ARG   B NH2 1 
ATOM   2928  N  N   . LEU   B 2 39  ? 35.378  52.492  5.471   1.00 92.19  ? 39   LEU   B N   1 
ATOM   2929  C  CA  . LEU   B 2 39  ? 34.915  51.884  6.706   1.00 89.25  ? 39   LEU   B CA  1 
ATOM   2930  C  C   . LEU   B 2 39  ? 34.771  52.972  7.761   1.00 92.86  ? 39   LEU   B C   1 
ATOM   2931  O  O   . LEU   B 2 39  ? 35.612  53.878  7.863   1.00 93.13  ? 39   LEU   B O   1 
ATOM   2932  C  CB  . LEU   B 2 39  ? 35.884  50.795  7.178   1.00 93.11  ? 39   LEU   B CB  1 
ATOM   2933  C  CG  . LEU   B 2 39  ? 35.587  49.998  8.458   1.00 97.00  ? 39   LEU   B CG  1 
ATOM   2934  C  CD1 . LEU   B 2 39  ? 34.297  49.193  8.319   1.00 93.74  ? 39   LEU   B CD1 1 
ATOM   2935  C  CD2 . LEU   B 2 39  ? 36.745  49.059  8.838   1.00 91.99  ? 39   LEU   B CD2 1 
ATOM   2936  N  N   . GLU   B 2 40  ? 33.691  52.898  8.527   1.00 87.64  ? 40   GLU   B N   1 
ATOM   2937  C  CA  . GLU   B 2 40  ? 33.430  53.865  9.582   1.00 89.33  ? 40   GLU   B CA  1 
ATOM   2938  C  C   . GLU   B 2 40  ? 33.191  53.118  10.885  1.00 90.12  ? 40   GLU   B C   1 
ATOM   2939  O  O   . GLU   B 2 40  ? 32.490  52.099  10.904  1.00 91.31  ? 40   GLU   B O   1 
ATOM   2940  C  CB  . GLU   B 2 40  ? 32.233  54.757  9.237   1.00 88.45  ? 40   GLU   B CB  1 
ATOM   2941  C  CG  . GLU   B 2 40  ? 32.575  55.950  8.347   1.00 88.20  ? 40   GLU   B CG  1 
ATOM   2942  C  CD  . GLU   B 2 40  ? 31.317  56.644  7.828   1.00 95.85  ? 40   GLU   B CD  1 
ATOM   2943  O  OE1 . GLU   B 2 40  ? 30.224  56.400  8.412   1.00 93.98  ? 40   GLU   B OE1 1 
ATOM   2944  O  OE2 . GLU   B 2 40  ? 31.411  57.423  6.838   1.00 96.14  ? 40   GLU   B OE2 1 
ATOM   2945  N  N   . ILE   B 2 41  ? 33.785  53.614  11.967  1.00 92.61  ? 41   ILE   B N   1 
ATOM   2946  C  CA  . ILE   B 2 41  ? 33.746  52.943  13.259  1.00 92.31  ? 41   ILE   B CA  1 
ATOM   2947  C  C   . ILE   B 2 41  ? 33.269  53.941  14.302  1.00 90.72  ? 41   ILE   B C   1 
ATOM   2948  O  O   . ILE   B 2 41  ? 33.963  54.926  14.578  1.00 92.67  ? 41   ILE   B O   1 
ATOM   2949  C  CB  . ILE   B 2 41  ? 35.119  52.370  13.638  1.00 88.40  ? 41   ILE   B CB  1 
ATOM   2950  C  CG1 . ILE   B 2 41  ? 35.578  51.321  12.625  1.00 92.85  ? 41   ILE   B CG1 1 
ATOM   2951  C  CG2 . ILE   B 2 41  ? 35.056  51.745  14.988  1.00 90.98  ? 41   ILE   B CG2 1 
ATOM   2952  C  CD1 . ILE   B 2 41  ? 37.090  51.313  12.386  1.00 93.51  ? 41   ILE   B CD1 1 
ATOM   2953  N  N   . TYR   B 2 42  ? 32.096  53.681  14.885  1.00 88.71  ? 42   TYR   B N   1 
ATOM   2954  C  CA  . TYR   B 2 42  ? 31.523  54.484  15.958  1.00 95.16  ? 42   TYR   B CA  1 
ATOM   2955  C  C   . TYR   B 2 42  ? 31.545  53.726  17.282  1.00 99.59  ? 42   TYR   B C   1 
ATOM   2956  O  O   . TYR   B 2 42  ? 31.799  52.517  17.344  1.00 97.40  ? 42   TYR   B O   1 
ATOM   2957  C  CB  . TYR   B 2 42  ? 30.079  54.895  15.632  1.00 92.37  ? 42   TYR   B CB  1 
ATOM   2958  C  CG  . TYR   B 2 42  ? 30.000  55.787  14.441  1.00 94.68  ? 42   TYR   B CG  1 
ATOM   2959  C  CD1 . TYR   B 2 42  ? 29.918  55.256  13.159  1.00 95.49  ? 42   TYR   B CD1 1 
ATOM   2960  C  CD2 . TYR   B 2 42  ? 30.061  57.160  14.582  1.00 94.34  ? 42   TYR   B CD2 1 
ATOM   2961  C  CE1 . TYR   B 2 42  ? 29.873  56.084  12.043  1.00 94.39  ? 42   TYR   B CE1 1 
ATOM   2962  C  CE2 . TYR   B 2 42  ? 30.020  57.984  13.484  1.00 94.60  ? 42   TYR   B CE2 1 
ATOM   2963  C  CZ  . TYR   B 2 42  ? 29.924  57.444  12.219  1.00 91.00  ? 42   TYR   B CZ  1 
ATOM   2964  O  OH  . TYR   B 2 42  ? 29.884  58.271  11.130  1.00 91.00  ? 42   TYR   B OH  1 
ATOM   2965  N  N   . VAL   B 2 43  ? 31.264  54.459  18.358  1.00 102.27 ? 43   VAL   B N   1 
ATOM   2966  C  CA  . VAL   B 2 43  ? 30.902  53.847  19.630  1.00 102.75 ? 43   VAL   B CA  1 
ATOM   2967  C  C   . VAL   B 2 43  ? 29.474  54.251  19.960  1.00 103.31 ? 43   VAL   B C   1 
ATOM   2968  O  O   . VAL   B 2 43  ? 29.083  55.412  19.791  1.00 105.04 ? 43   VAL   B O   1 
ATOM   2969  C  CB  . VAL   B 2 43  ? 31.856  54.224  20.781  1.00 96.62  ? 43   VAL   B CB  1 
ATOM   2970  C  CG1 . VAL   B 2 43  ? 31.389  53.556  22.051  1.00 94.59  ? 43   VAL   B CG1 1 
ATOM   2971  C  CG2 . VAL   B 2 43  ? 33.269  53.786  20.442  1.00 100.47 ? 43   VAL   B CG2 1 
ATOM   2972  N  N   . VAL   B 2 44  ? 28.693  53.281  20.415  1.00 102.70 ? 44   VAL   B N   1 
ATOM   2973  C  CA  . VAL   B 2 44  ? 27.284  53.490  20.702  1.00 106.76 ? 44   VAL   B CA  1 
ATOM   2974  C  C   . VAL   B 2 44  ? 27.166  53.978  22.139  1.00 112.09 ? 44   VAL   B C   1 
ATOM   2975  O  O   . VAL   B 2 44  ? 27.210  53.187  23.082  1.00 112.56 ? 44   VAL   B O   1 
ATOM   2976  C  CB  . VAL   B 2 44  ? 26.473  52.217  20.491  1.00 107.29 ? 44   VAL   B CB  1 
ATOM   2977  C  CG1 . VAL   B 2 44  ? 25.163  52.345  21.229  1.00 111.71 ? 44   VAL   B CG1 1 
ATOM   2978  C  CG2 . VAL   B 2 44  ? 26.251  51.998  19.024  1.00 106.02 ? 44   VAL   B CG2 1 
ATOM   2979  N  N   . THR   B 2 45  ? 26.994  55.280  22.308  1.00 118.90 ? 45   THR   B N   1 
ATOM   2980  C  CA  . THR   B 2 45  ? 26.712  55.843  23.619  1.00 121.21 ? 45   THR   B CA  1 
ATOM   2981  C  C   . THR   B 2 45  ? 25.206  55.840  23.872  1.00 127.72 ? 45   THR   B C   1 
ATOM   2982  O  O   . THR   B 2 45  ? 24.397  55.689  22.949  1.00 129.32 ? 45   THR   B O   1 
ATOM   2983  C  CB  . THR   B 2 45  ? 27.268  57.265  23.722  1.00 121.39 ? 45   THR   B CB  1 
ATOM   2984  O  OG1 . THR   B 2 45  ? 26.400  58.177  23.030  1.00 123.71 ? 45   THR   B OG1 1 
ATOM   2985  C  CG2 . THR   B 2 45  ? 28.648  57.318  23.102  1.00 106.71 ? 45   THR   B CG2 1 
ATOM   2986  N  N   . ALA   B 2 46  ? 24.831  55.993  25.146  1.00 129.57 ? 46   ALA   B N   1 
ATOM   2987  C  CA  . ALA   B 2 46  ? 23.418  56.149  25.465  1.00 128.65 ? 46   ALA   B CA  1 
ATOM   2988  C  C   . ALA   B 2 46  ? 22.858  57.487  24.979  1.00 126.98 ? 46   ALA   B C   1 
ATOM   2989  O  O   . ALA   B 2 46  ? 21.636  57.662  24.993  1.00 121.73 ? 46   ALA   B O   1 
ATOM   2990  C  CB  . ALA   B 2 46  ? 23.197  55.997  26.976  1.00 123.63 ? 46   ALA   B CB  1 
ATOM   2991  N  N   . GLU   B 2 47  ? 23.711  58.426  24.555  1.00 132.58 ? 47   GLU   B N   1 
ATOM   2992  C  CA  . GLU   B 2 47  ? 23.237  59.659  23.939  1.00 137.17 ? 47   GLU   B CA  1 
ATOM   2993  C  C   . GLU   B 2 47  ? 23.129  59.534  22.423  1.00 139.55 ? 47   GLU   B C   1 
ATOM   2994  O  O   . GLU   B 2 47  ? 22.217  60.122  21.825  1.00 142.00 ? 47   GLU   B O   1 
ATOM   2995  C  CB  . GLU   B 2 47  ? 24.154  60.834  24.305  1.00 136.26 ? 47   GLU   B CB  1 
ATOM   2996  N  N   . GLY   B 2 48  ? 24.030  58.782  21.786  1.00 157.01 ? 48   GLY   B N   1 
ATOM   2997  C  CA  . GLY   B 2 48  ? 23.969  58.572  20.343  1.00 156.14 ? 48   GLY   B CA  1 
ATOM   2998  C  C   . GLY   B 2 48  ? 25.119  57.788  19.717  1.00 153.31 ? 48   GLY   B C   1 
ATOM   2999  O  O   . GLY   B 2 48  ? 25.369  56.643  20.099  1.00 152.22 ? 48   GLY   B O   1 
ATOM   3000  N  N   . LEU   B 2 49  ? 25.812  58.382  18.748  1.00 124.46 ? 49   LEU   B N   1 
ATOM   3001  C  CA  . LEU   B 2 49  ? 26.952  57.764  18.089  1.00 112.64 ? 49   LEU   B CA  1 
ATOM   3002  C  C   . LEU   B 2 49  ? 28.196  58.617  18.279  1.00 107.75 ? 49   LEU   B C   1 
ATOM   3003  O  O   . LEU   B 2 49  ? 28.218  59.781  17.870  1.00 109.26 ? 49   LEU   B O   1 
ATOM   3004  C  CB  . LEU   B 2 49  ? 26.686  57.586  16.599  1.00 109.36 ? 49   LEU   B CB  1 
ATOM   3005  C  CG  . LEU   B 2 49  ? 26.365  56.192  16.102  1.00 102.29 ? 49   LEU   B CG  1 
ATOM   3006  C  CD1 . LEU   B 2 49  ? 24.934  55.880  16.459  1.00 110.33 ? 49   LEU   B CD1 1 
ATOM   3007  C  CD2 . LEU   B 2 49  ? 26.575  56.185  14.614  1.00 94.10  ? 49   LEU   B CD2 1 
ATOM   3008  N  N   . ARG   B 2 50  ? 29.245  58.028  18.870  1.00 102.77 ? 50   ARG   B N   1 
ATOM   3009  C  CA  . ARG   B 2 50  ? 30.534  58.706  18.987  1.00 100.20 ? 50   ARG   B CA  1 
ATOM   3010  C  C   . ARG   B 2 50  ? 31.461  58.232  17.879  1.00 98.94  ? 50   ARG   B C   1 
ATOM   3011  O  O   . ARG   B 2 50  ? 31.760  57.023  17.792  1.00 96.18  ? 50   ARG   B O   1 
ATOM   3012  C  CB  . ARG   B 2 50  ? 31.169  58.448  20.351  1.00 98.93  ? 50   ARG   B CB  1 
ATOM   3013  C  CG  . ARG   B 2 50  ? 32.442  59.253  20.604  1.00 95.28  ? 50   ARG   B CG  1 
ATOM   3014  C  CD  . ARG   B 2 50  ? 33.462  58.470  21.444  1.00 95.93  ? 50   ARG   B CD  1 
ATOM   3015  N  NE  . ARG   B 2 50  ? 32.860  57.861  22.627  1.00 99.50  ? 50   ARG   B NE  1 
ATOM   3016  C  CZ  . ARG   B 2 50  ? 33.261  56.719  23.184  1.00 107.74 ? 50   ARG   B CZ  1 
ATOM   3017  N  NH1 . ARG   B 2 50  ? 34.268  56.012  22.685  1.00 102.27 ? 50   ARG   B NH1 1 
ATOM   3018  N  NH2 . ARG   B 2 50  ? 32.633  56.271  24.272  1.00 109.51 ? 50   ARG   B NH2 1 
ATOM   3019  N  N   . PRO   B 2 51  ? 31.913  59.135  17.010  1.00 95.68  ? 51   PRO   B N   1 
ATOM   3020  C  CA  . PRO   B 2 51  ? 32.861  58.752  15.966  1.00 92.37  ? 51   PRO   B CA  1 
ATOM   3021  C  C   . PRO   B 2 51  ? 34.171  58.317  16.572  1.00 94.64  ? 51   PRO   B C   1 
ATOM   3022  O  O   . PRO   B 2 51  ? 34.575  58.797  17.629  1.00 102.00 ? 51   PRO   B O   1 
ATOM   3023  C  CB  . PRO   B 2 51  ? 33.050  60.039  15.165  1.00 91.38  ? 51   PRO   B CB  1 
ATOM   3024  C  CG  . PRO   B 2 51  ? 31.888  60.878  15.514  1.00 94.93  ? 51   PRO   B CG  1 
ATOM   3025  C  CD  . PRO   B 2 51  ? 31.573  60.554  16.936  1.00 94.95  ? 51   PRO   B CD  1 
ATOM   3026  N  N   . VAL   B 2 52  ? 34.844  57.412  15.882  1.00 92.35  ? 52   VAL   B N   1 
ATOM   3027  C  CA  . VAL   B 2 52  ? 36.097  56.881  16.397  1.00 97.60  ? 52   VAL   B CA  1 
ATOM   3028  C  C   . VAL   B 2 52  ? 37.183  56.904  15.329  1.00 99.91  ? 52   VAL   B C   1 
ATOM   3029  O  O   . VAL   B 2 52  ? 38.292  57.395  15.581  1.00 102.70 ? 52   VAL   B O   1 
ATOM   3030  C  CB  . VAL   B 2 52  ? 35.916  55.460  16.954  1.00 95.80  ? 52   VAL   B CB  1 
ATOM   3031  C  CG1 . VAL   B 2 52  ? 37.222  54.988  17.531  1.00 91.24  ? 52   VAL   B CG1 1 
ATOM   3032  C  CG2 . VAL   B 2 52  ? 34.796  55.427  17.994  1.00 95.76  ? 52   VAL   B CG2 1 
ATOM   3033  N  N   . LYS   B 2 53  ? 36.886  56.357  14.147  1.00 97.85  ? 53   LYS   B N   1 
ATOM   3034  C  CA  . LYS   B 2 53  ? 37.863  56.293  13.067  1.00 96.08  ? 53   LYS   B CA  1 
ATOM   3035  C  C   . LYS   B 2 53  ? 37.194  55.797  11.791  1.00 100.23 ? 53   LYS   B C   1 
ATOM   3036  O  O   . LYS   B 2 53  ? 36.400  54.844  11.824  1.00 95.02  ? 53   LYS   B O   1 
ATOM   3037  C  CB  . LYS   B 2 53  ? 39.045  55.387  13.414  1.00 96.10  ? 53   LYS   B CB  1 
ATOM   3038  C  CG  . LYS   B 2 53  ? 40.103  55.344  12.321  1.00 96.69  ? 53   LYS   B CG  1 
ATOM   3039  C  CD  . LYS   B 2 53  ? 41.302  54.522  12.752  1.00 103.99 ? 53   LYS   B CD  1 
ATOM   3040  C  CE  . LYS   B 2 53  ? 42.536  54.900  11.953  1.00 106.63 ? 53   LYS   B CE  1 
ATOM   3041  N  NZ  . LYS   B 2 53  ? 42.549  56.380  11.712  1.00 107.36 ? 53   LYS   B NZ  1 
ATOM   3042  N  N   . GLU   B 2 54  ? 37.553  56.431  10.666  1.00 102.37 ? 54   GLU   B N   1 
ATOM   3043  C  CA  . GLU   B 2 54  ? 36.947  56.182  9.358   1.00 100.25 ? 54   GLU   B CA  1 
ATOM   3044  C  C   . GLU   B 2 54  ? 38.074  55.937  8.367   1.00 100.78 ? 54   GLU   B C   1 
ATOM   3045  O  O   . GLU   B 2 54  ? 38.825  56.855  8.026   1.00 103.13 ? 54   GLU   B O   1 
ATOM   3046  C  CB  . GLU   B 2 54  ? 36.072  57.362  8.921   1.00 100.73 ? 54   GLU   B CB  1 
ATOM   3047  C  CG  . GLU   B 2 54  ? 35.412  57.211  7.549   1.00 101.89 ? 54   GLU   B CG  1 
ATOM   3048  C  CD  . GLU   B 2 54  ? 36.281  57.707  6.379   1.00 102.50 ? 54   GLU   B CD  1 
ATOM   3049  O  OE1 . GLU   B 2 54  ? 37.373  58.288  6.619   1.00 101.83 ? 54   GLU   B OE1 1 
ATOM   3050  O  OE2 . GLU   B 2 54  ? 35.852  57.518  5.211   1.00 98.34  ? 54   GLU   B OE2 1 
ATOM   3051  N  N   . VAL   B 2 55  ? 38.189  54.709  7.903   1.00 104.53 ? 55   VAL   B N   1 
ATOM   3052  C  CA  . VAL   B 2 55  ? 39.378  54.274  7.194   1.00 110.03 ? 55   VAL   B CA  1 
ATOM   3053  C  C   . VAL   B 2 55  ? 39.041  54.070  5.720   1.00 110.01 ? 55   VAL   B C   1 
ATOM   3054  O  O   . VAL   B 2 55  ? 37.875  53.897  5.335   1.00 108.30 ? 55   VAL   B O   1 
ATOM   3055  C  CB  . VAL   B 2 55  ? 39.951  52.985  7.830   1.00 112.08 ? 55   VAL   B CB  1 
ATOM   3056  C  CG1 . VAL   B 2 55  ? 38.844  51.952  8.029   1.00 110.32 ? 55   VAL   B CG1 1 
ATOM   3057  C  CG2 . VAL   B 2 55  ? 41.066  52.406  6.992   1.00 111.59 ? 55   VAL   B CG2 1 
ATOM   3058  N  N   . GLY   B 2 56  ? 40.088  54.090  4.885   1.00 103.34 ? 56   GLY   B N   1 
ATOM   3059  C  CA  . GLY   B 2 56  ? 39.956  53.775  3.469   1.00 96.59  ? 56   GLY   B CA  1 
ATOM   3060  C  C   . GLY   B 2 56  ? 40.632  52.494  3.011   1.00 95.56  ? 56   GLY   B C   1 
ATOM   3061  O  O   . GLY   B 2 56  ? 41.815  52.250  3.280   1.00 94.31  ? 56   GLY   B O   1 
ATOM   3062  N  N   . MET   B 2 57  ? 39.879  51.676  2.288   1.00 94.46  ? 57   MET   B N   1 
ATOM   3063  C  CA  . MET   B 2 57  ? 40.377  50.432  1.724   1.00 87.37  ? 57   MET   B CA  1 
ATOM   3064  C  C   . MET   B 2 57  ? 40.568  50.577  0.218   1.00 86.99  ? 57   MET   B C   1 
ATOM   3065  O  O   . MET   B 2 57  ? 39.802  51.253  -0.472  1.00 88.93  ? 57   MET   B O   1 
ATOM   3066  C  CB  . MET   B 2 57  ? 39.417  49.278  2.004   1.00 83.85  ? 57   MET   B CB  1 
ATOM   3067  C  CG  . MET   B 2 57  ? 39.370  48.820  3.448   1.00 86.47  ? 57   MET   B CG  1 
ATOM   3068  S  SD  . MET   B 2 57  ? 39.130  47.031  3.439   1.00 99.23  ? 57   MET   B SD  1 
ATOM   3069  C  CE  . MET   B 2 57  ? 38.247  46.726  4.966   1.00 92.92  ? 57   MET   B CE  1 
ATOM   3070  N  N   . TYR   B 2 58  ? 41.597  49.929  -0.289  1.00 90.35  ? 58   TYR   B N   1 
ATOM   3071  C  CA  . TYR   B 2 58  ? 41.792  49.830  -1.731  1.00 84.23  ? 58   TYR   B CA  1 
ATOM   3072  C  C   . TYR   B 2 58  ? 40.912  48.763  -2.336  1.00 81.93  ? 58   TYR   B C   1 
ATOM   3073  O  O   . TYR   B 2 58  ? 41.418  47.895  -3.038  1.00 81.82  ? 58   TYR   B O   1 
ATOM   3074  C  CB  . TYR   B 2 58  ? 43.241  49.517  -2.047  1.00 85.81  ? 58   TYR   B CB  1 
ATOM   3075  C  CG  . TYR   B 2 58  ? 44.164  50.668  -1.815  1.00 90.76  ? 58   TYR   B CG  1 
ATOM   3076  C  CD1 . TYR   B 2 58  ? 43.684  51.896  -1.395  1.00 89.93  ? 58   TYR   B CD1 1 
ATOM   3077  C  CD2 . TYR   B 2 58  ? 45.527  50.526  -2.028  1.00 93.21  ? 58   TYR   B CD2 1 
ATOM   3078  C  CE1 . TYR   B 2 58  ? 44.543  52.966  -1.183  1.00 93.56  ? 58   TYR   B CE1 1 
ATOM   3079  C  CE2 . TYR   B 2 58  ? 46.389  51.583  -1.829  1.00 98.64  ? 58   TYR   B CE2 1 
ATOM   3080  C  CZ  . TYR   B 2 58  ? 45.904  52.800  -1.408  1.00 95.31  ? 58   TYR   B CZ  1 
ATOM   3081  O  OH  . TYR   B 2 58  ? 46.781  53.851  -1.212  1.00 95.76  ? 58   TYR   B OH  1 
ATOM   3082  N  N   . GLY   B 2 59  ? 39.617  48.786  -2.054  1.00 81.52  ? 59   GLY   B N   1 
ATOM   3083  C  CA  . GLY   B 2 59  ? 38.723  47.770  -2.574  1.00 78.69  ? 59   GLY   B CA  1 
ATOM   3084  C  C   . GLY   B 2 59  ? 37.288  48.172  -2.333  1.00 82.62  ? 59   GLY   B C   1 
ATOM   3085  O  O   . GLY   B 2 59  ? 37.008  49.207  -1.732  1.00 87.11  ? 59   GLY   B O   1 
ATOM   3086  N  N   . LYS   B 2 60  ? 36.368  47.348  -2.822  1.00 82.02  ? 60   LYS   B N   1 
ATOM   3087  C  CA  . LYS   B 2 60  ? 34.945  47.574  -2.610  1.00 80.10  ? 60   LYS   B CA  1 
ATOM   3088  C  C   . LYS   B 2 60  ? 34.461  46.557  -1.595  1.00 77.97  ? 60   LYS   B C   1 
ATOM   3089  O  O   . LYS   B 2 60  ? 34.564  45.348  -1.838  1.00 79.22  ? 60   LYS   B O   1 
ATOM   3090  C  CB  . LYS   B 2 60  ? 34.164  47.483  -3.917  1.00 83.98  ? 60   LYS   B CB  1 
ATOM   3091  C  CG  . LYS   B 2 60  ? 34.083  48.826  -4.640  1.00 83.26  ? 60   LYS   B CG  1 
ATOM   3092  C  CD  . LYS   B 2 60  ? 33.859  48.650  -6.132  1.00 81.91  ? 60   LYS   B CD  1 
ATOM   3093  C  CE  . LYS   B 2 60  ? 32.497  48.058  -6.413  1.00 79.40  ? 60   LYS   B CE  1 
ATOM   3094  N  NZ  . LYS   B 2 60  ? 31.416  48.965  -5.941  1.00 82.98  ? 60   LYS   B NZ  1 
ATOM   3095  N  N   . ILE   B 2 61  ? 33.974  47.044  -0.455  1.00 79.10  ? 61   ILE   B N   1 
ATOM   3096  C  CA  . ILE   B 2 61  ? 33.692  46.162  0.668   1.00 77.66  ? 61   ILE   B CA  1 
ATOM   3097  C  C   . ILE   B 2 61  ? 32.475  45.324  0.334   1.00 78.18  ? 61   ILE   B C   1 
ATOM   3098  O  O   . ILE   B 2 61  ? 31.367  45.850  0.214   1.00 81.43  ? 61   ILE   B O   1 
ATOM   3099  C  CB  . ILE   B 2 61  ? 33.460  46.936  1.963   1.00 76.42  ? 61   ILE   B CB  1 
ATOM   3100  C  CG1 . ILE   B 2 61  ? 34.791  47.476  2.482   1.00 80.88  ? 61   ILE   B CG1 1 
ATOM   3101  C  CG2 . ILE   B 2 61  ? 32.773  46.006  2.945   1.00 78.12  ? 61   ILE   B CG2 1 
ATOM   3102  C  CD1 . ILE   B 2 61  ? 34.735  48.001  3.917   1.00 85.53  ? 61   ILE   B CD1 1 
ATOM   3103  N  N   . ALA   B 2 62  ? 32.662  44.012  0.245   1.00 78.77  ? 62   ALA   B N   1 
ATOM   3104  C  CA  . ALA   B 2 62  ? 31.583  43.103  -0.107  1.00 74.65  ? 62   ALA   B CA  1 
ATOM   3105  C  C   . ALA   B 2 62  ? 31.197  42.176  1.032   1.00 74.92  ? 62   ALA   B C   1 
ATOM   3106  O  O   . ALA   B 2 62  ? 30.039  41.785  1.141   1.00 74.19  ? 62   ALA   B O   1 
ATOM   3107  C  CB  . ALA   B 2 62  ? 31.973  42.268  -1.332  1.00 74.19  ? 62   ALA   B CB  1 
ATOM   3108  N  N   . VAL   B 2 63  ? 32.135  41.810  1.885   1.00 72.89  ? 63   VAL   B N   1 
ATOM   3109  C  CA  . VAL   B 2 63  ? 31.818  41.054  3.083   1.00 77.80  ? 63   VAL   B CA  1 
ATOM   3110  C  C   . VAL   B 2 63  ? 32.457  41.782  4.262   1.00 80.70  ? 63   VAL   B C   1 
ATOM   3111  O  O   . VAL   B 2 63  ? 33.642  42.134  4.220   1.00 80.20  ? 63   VAL   B O   1 
ATOM   3112  C  CB  . VAL   B 2 63  ? 32.291  39.587  2.967   1.00 83.69  ? 63   VAL   B CB  1 
ATOM   3113  C  CG1 . VAL   B 2 63  ? 31.575  38.689  3.970   1.00 83.00  ? 63   VAL   B CG1 1 
ATOM   3114  C  CG2 . VAL   B 2 63  ? 32.046  39.072  1.566   1.00 79.51  ? 63   VAL   B CG2 1 
ATOM   3115  N  N   . MET   B 2 64  ? 31.658  42.067  5.280   1.00 83.63  ? 64   MET   B N   1 
ATOM   3116  C  CA  . MET   B 2 64  ? 32.132  42.801  6.449   1.00 84.30  ? 64   MET   B CA  1 
ATOM   3117  C  C   . MET   B 2 64  ? 31.455  42.185  7.663   1.00 87.14  ? 64   MET   B C   1 
ATOM   3118  O  O   . MET   B 2 64  ? 30.248  42.367  7.869   1.00 84.73  ? 64   MET   B O   1 
ATOM   3119  C  CB  . MET   B 2 64  ? 31.822  44.289  6.337   1.00 80.31  ? 64   MET   B CB  1 
ATOM   3120  C  CG  . MET   B 2 64  ? 32.301  45.086  7.522   1.00 84.68  ? 64   MET   B CG  1 
ATOM   3121  S  SD  . MET   B 2 64  ? 31.555  46.739  7.574   1.00 89.66  ? 64   MET   B SD  1 
ATOM   3122  C  CE  . MET   B 2 64  ? 29.935  46.392  8.300   1.00 78.43  ? 64   MET   B CE  1 
ATOM   3123  N  N   . GLU   B 2 65  ? 32.222  41.437  8.445   1.00 87.33  ? 65   GLU   B N   1 
ATOM   3124  C  CA  . GLU   B 2 65  ? 31.653  40.696  9.556   1.00 88.55  ? 65   GLU   B CA  1 
ATOM   3125  C  C   . GLU   B 2 65  ? 32.654  40.658  10.700  1.00 88.80  ? 65   GLU   B C   1 
ATOM   3126  O  O   . GLU   B 2 65  ? 33.855  40.473  10.476  1.00 87.72  ? 65   GLU   B O   1 
ATOM   3127  C  CB  . GLU   B 2 65  ? 31.259  39.279  9.118   1.00 86.22  ? 65   GLU   B CB  1 
ATOM   3128  C  CG  . GLU   B 2 65  ? 29.925  39.217  8.354   1.00 88.75  ? 65   GLU   B CG  1 
ATOM   3129  C  CD  . GLU   B 2 65  ? 28.722  39.388  9.286   1.00 97.55  ? 65   GLU   B CD  1 
ATOM   3130  O  OE1 . GLU   B 2 65  ? 28.934  39.296  10.523  1.00 99.22  ? 65   GLU   B OE1 1 
ATOM   3131  O  OE2 . GLU   B 2 65  ? 27.574  39.607  8.793   1.00 96.16  ? 65   GLU   B OE2 1 
ATOM   3132  N  N   . LEU   B 2 66  ? 32.155  40.867  11.921  1.00 88.96  ? 66   LEU   B N   1 
ATOM   3133  C  CA  . LEU   B 2 66  ? 32.972  40.761  13.121  1.00 89.66  ? 66   LEU   B CA  1 
ATOM   3134  C  C   . LEU   B 2 66  ? 32.779  39.393  13.758  1.00 89.37  ? 66   LEU   B C   1 
ATOM   3135  O  O   . LEU   B 2 66  ? 31.720  38.771  13.636  1.00 90.80  ? 66   LEU   B O   1 
ATOM   3136  C  CB  . LEU   B 2 66  ? 32.630  41.849  14.132  1.00 89.74  ? 66   LEU   B CB  1 
ATOM   3137  C  CG  . LEU   B 2 66  ? 32.717  43.316  13.721  1.00 83.58  ? 66   LEU   B CG  1 
ATOM   3138  C  CD1 . LEU   B 2 66  ? 31.761  44.108  14.605  1.00 78.59  ? 66   LEU   B CD1 1 
ATOM   3139  C  CD2 . LEU   B 2 66  ? 34.150  43.848  13.814  1.00 85.39  ? 66   LEU   B CD2 1 
ATOM   3140  N  N   . PHE   B 2 67  ? 33.819  38.938  14.451  1.00 88.02  ? 67   PHE   B N   1 
ATOM   3141  C  CA  . PHE   B 2 67  ? 33.879  37.594  15.014  1.00 89.40  ? 67   PHE   B CA  1 
ATOM   3142  C  C   . PHE   B 2 67  ? 35.021  37.556  16.024  1.00 90.42  ? 67   PHE   B C   1 
ATOM   3143  O  O   . PHE   B 2 67  ? 35.936  38.388  15.983  1.00 92.62  ? 67   PHE   B O   1 
ATOM   3144  C  CB  . PHE   B 2 67  ? 34.076  36.538  13.925  1.00 87.11  ? 67   PHE   B CB  1 
ATOM   3145  C  CG  . PHE   B 2 67  ? 35.391  36.647  13.229  1.00 86.16  ? 67   PHE   B CG  1 
ATOM   3146  C  CD1 . PHE   B 2 67  ? 35.685  37.757  12.455  1.00 87.19  ? 67   PHE   B CD1 1 
ATOM   3147  C  CD2 . PHE   B 2 67  ? 36.341  35.653  13.350  1.00 87.92  ? 67   PHE   B CD2 1 
ATOM   3148  C  CE1 . PHE   B 2 67  ? 36.904  37.875  11.805  1.00 87.56  ? 67   PHE   B CE1 1 
ATOM   3149  C  CE2 . PHE   B 2 67  ? 37.568  35.758  12.697  1.00 85.68  ? 67   PHE   B CE2 1 
ATOM   3150  C  CZ  . PHE   B 2 67  ? 37.849  36.866  11.926  1.00 86.91  ? 67   PHE   B CZ  1 
ATOM   3151  N  N   . ARG   B 2 68  ? 34.952  36.585  16.940  1.00 91.52  ? 68   ARG   B N   1 
ATOM   3152  C  CA  . ARG   B 2 68  ? 35.828  36.520  18.112  1.00 93.25  ? 68   ARG   B CA  1 
ATOM   3153  C  C   . ARG   B 2 68  ? 36.351  35.097  18.274  1.00 95.08  ? 68   ARG   B C   1 
ATOM   3154  O  O   . ARG   B 2 68  ? 35.736  34.278  18.960  1.00 95.49  ? 68   ARG   B O   1 
ATOM   3155  C  CB  . ARG   B 2 68  ? 35.079  36.970  19.366  1.00 93.60  ? 68   ARG   B CB  1 
ATOM   3156  C  CG  . ARG   B 2 68  ? 35.877  36.843  20.633  1.00 96.67  ? 68   ARG   B CG  1 
ATOM   3157  C  CD  . ARG   B 2 68  ? 36.730  38.066  20.865  1.00 98.69  ? 68   ARG   B CD  1 
ATOM   3158  N  NE  . ARG   B 2 68  ? 35.945  39.282  21.059  1.00 101.31 ? 68   ARG   B NE  1 
ATOM   3159  C  CZ  . ARG   B 2 68  ? 35.306  39.600  22.178  1.00 100.33 ? 68   ARG   B CZ  1 
ATOM   3160  N  NH1 . ARG   B 2 68  ? 35.201  38.743  23.181  1.00 93.91  ? 68   ARG   B NH1 1 
ATOM   3161  N  NH2 . ARG   B 2 68  ? 34.769  40.816  22.296  1.00 100.08 ? 68   ARG   B NH2 1 
ATOM   3162  N  N   . PRO   B 2 69  ? 37.490  34.771  17.672  1.00 96.30  ? 69   PRO   B N   1 
ATOM   3163  C  CA  . PRO   B 2 69  ? 37.978  33.402  17.681  1.00 97.49  ? 69   PRO   B CA  1 
ATOM   3164  C  C   . PRO   B 2 69  ? 38.541  33.064  19.044  1.00 102.87 ? 69   PRO   B C   1 
ATOM   3165  O  O   . PRO   B 2 69  ? 38.619  33.928  19.924  1.00 99.62  ? 69   PRO   B O   1 
ATOM   3166  C  CB  . PRO   B 2 69  ? 39.065  33.405  16.593  1.00 95.84  ? 69   PRO   B CB  1 
ATOM   3167  C  CG  . PRO   B 2 69  ? 38.928  34.718  15.904  1.00 96.93  ? 69   PRO   B CG  1 
ATOM   3168  C  CD  . PRO   B 2 69  ? 38.390  35.649  16.930  1.00 99.56  ? 69   PRO   B CD  1 
ATOM   3169  N  N   . LYS   B 2 70  ? 38.910  31.794  19.224  1.00 105.67 ? 70   LYS   B N   1 
ATOM   3170  C  CA  . LYS   B 2 70  ? 39.486  31.332  20.484  1.00 103.66 ? 70   LYS   B CA  1 
ATOM   3171  C  C   . LYS   B 2 70  ? 40.792  32.065  20.740  1.00 108.47 ? 70   LYS   B C   1 
ATOM   3172  O  O   . LYS   B 2 70  ? 41.649  32.145  19.858  1.00 106.29 ? 70   LYS   B O   1 
ATOM   3173  C  CB  . LYS   B 2 70  ? 39.721  29.822  20.449  1.00 96.26  ? 70   LYS   B CB  1 
ATOM   3174  N  N   . GLY   B 2 71  ? 40.921  32.653  21.933  1.00 122.68 ? 71   GLY   B N   1 
ATOM   3175  C  CA  . GLY   B 2 71  ? 42.135  33.337  22.328  1.00 123.06 ? 71   GLY   B CA  1 
ATOM   3176  C  C   . GLY   B 2 71  ? 42.269  34.754  21.814  1.00 125.41 ? 71   GLY   B C   1 
ATOM   3177  O  O   . GLY   B 2 71  ? 43.358  35.162  21.386  1.00 129.68 ? 71   GLY   B O   1 
ATOM   3178  N  N   . GLU   B 2 72  ? 41.177  35.527  21.859  1.00 117.24 ? 72   GLU   B N   1 
ATOM   3179  C  CA  . GLU   B 2 72  ? 41.146  36.908  21.402  1.00 108.63 ? 72   GLU   B CA  1 
ATOM   3180  C  C   . GLU   B 2 72  ? 40.434  37.787  22.422  1.00 103.51 ? 72   GLU   B C   1 
ATOM   3181  O  O   . GLU   B 2 72  ? 39.349  37.438  22.900  1.00 104.48 ? 72   GLU   B O   1 
ATOM   3182  C  CB  . GLU   B 2 72  ? 40.434  37.014  20.057  1.00 106.96 ? 72   GLU   B CB  1 
ATOM   3183  C  CG  . GLU   B 2 72  ? 41.226  36.451  18.888  1.00 108.12 ? 72   GLU   B CG  1 
ATOM   3184  C  CD  . GLU   B 2 72  ? 42.517  37.220  18.634  1.00 112.18 ? 72   GLU   B CD  1 
ATOM   3185  O  OE1 . GLU   B 2 72  ? 43.324  36.762  17.792  1.00 113.78 ? 72   GLU   B OE1 1 
ATOM   3186  O  OE2 . GLU   B 2 72  ? 42.724  38.280  19.274  1.00 114.43 ? 72   GLU   B OE2 1 
ATOM   3187  N  N   . SER   B 2 73  ? 41.028  38.941  22.733  1.00 101.11 ? 73   SER   B N   1 
ATOM   3188  C  CA  . SER   B 2 73  ? 40.410  39.858  23.686  1.00 98.10  ? 73   SER   B CA  1 
ATOM   3189  C  C   . SER   B 2 73  ? 39.164  40.542  23.102  1.00 104.70 ? 73   SER   B C   1 
ATOM   3190  O  O   . SER   B 2 73  ? 38.082  40.467  23.694  1.00 107.54 ? 73   SER   B O   1 
ATOM   3191  C  CB  . SER   B 2 73  ? 41.438  40.888  24.167  1.00 99.71  ? 73   SER   B CB  1 
ATOM   3192  O  OG  . SER   B 2 73  ? 42.324  41.309  23.132  1.00 103.28 ? 73   SER   B OG  1 
ATOM   3193  N  N   . LYS   B 2 74  ? 39.282  41.221  21.958  1.00 105.10 ? 74   LYS   B N   1 
ATOM   3194  C  CA  . LYS   B 2 74  ? 38.136  41.864  21.315  1.00 100.95 ? 74   LYS   B CA  1 
ATOM   3195  C  C   . LYS   B 2 74  ? 37.880  41.234  19.945  1.00 102.38 ? 74   LYS   B C   1 
ATOM   3196  O  O   . LYS   B 2 74  ? 38.707  40.469  19.428  1.00 95.60  ? 74   LYS   B O   1 
ATOM   3197  C  CB  . LYS   B 2 74  ? 38.355  43.375  21.178  1.00 94.96  ? 74   LYS   B CB  1 
ATOM   3198  C  CG  . LYS   B 2 74  ? 39.798  43.768  20.984  1.00 93.92  ? 74   LYS   B CG  1 
ATOM   3199  C  CD  . LYS   B 2 74  ? 39.881  45.262  20.783  1.00 96.73  ? 74   LYS   B CD  1 
ATOM   3200  C  CE  . LYS   B 2 74  ? 41.299  45.758  20.904  1.00 98.62  ? 74   LYS   B CE  1 
ATOM   3201  N  NZ  . LYS   B 2 74  ? 42.234  44.918  20.110  1.00 99.76  ? 74   LYS   B NZ  1 
ATOM   3202  N  N   . ASP   B 2 75  ? 36.711  41.557  19.367  1.00 99.05  ? 75   ASP   B N   1 
ATOM   3203  C  CA  . ASP   B 2 75  ? 36.316  41.018  18.068  1.00 90.15  ? 75   ASP   B CA  1 
ATOM   3204  C  C   . ASP   B 2 75  ? 37.330  41.394  17.001  1.00 90.86  ? 75   ASP   B C   1 
ATOM   3205  O  O   . ASP   B 2 75  ? 38.058  42.391  17.113  1.00 94.17  ? 75   ASP   B O   1 
ATOM   3206  C  CB  . ASP   B 2 75  ? 34.952  41.551  17.620  1.00 89.08  ? 75   ASP   B CB  1 
ATOM   3207  C  CG  . ASP   B 2 75  ? 33.820  41.124  18.527  1.00 96.54  ? 75   ASP   B CG  1 
ATOM   3208  O  OD1 . ASP   B 2 75  ? 34.114  40.596  19.620  1.00 99.13  ? 75   ASP   B OD1 1 
ATOM   3209  O  OD2 . ASP   B 2 75  ? 32.633  41.310  18.154  1.00 97.47  ? 75   ASP   B OD2 1 
ATOM   3210  N  N   . LEU   B 2 76  ? 37.332  40.620  15.925  1.00 85.70  ? 76   LEU   B N   1 
ATOM   3211  C  CA  . LEU   B 2 76  ? 38.119  40.950  14.753  1.00 86.57  ? 76   LEU   B CA  1 
ATOM   3212  C  C   . LEU   B 2 76  ? 37.183  41.164  13.566  1.00 86.53  ? 76   LEU   B C   1 
ATOM   3213  O  O   . LEU   B 2 76  ? 36.001  40.810  13.606  1.00 86.50  ? 76   LEU   B O   1 
ATOM   3214  C  CB  . LEU   B 2 76  ? 39.159  39.860  14.486  1.00 90.82  ? 76   LEU   B CB  1 
ATOM   3215  C  CG  . LEU   B 2 76  ? 40.179  39.733  15.627  1.00 92.86  ? 76   LEU   B CG  1 
ATOM   3216  C  CD1 . LEU   B 2 76  ? 40.842  38.370  15.648  1.00 87.49  ? 76   LEU   B CD1 1 
ATOM   3217  C  CD2 . LEU   B 2 76  ? 41.228  40.815  15.489  1.00 93.39  ? 76   LEU   B CD2 1 
ATOM   3218  N  N   . LEU   B 2 77  ? 37.701  41.795  12.518  1.00 87.27  ? 77   LEU   B N   1 
ATOM   3219  C  CA  . LEU   B 2 77  ? 36.888  42.205  11.375  1.00 89.32  ? 77   LEU   B CA  1 
ATOM   3220  C  C   . LEU   B 2 77  ? 37.364  41.476  10.122  1.00 87.98  ? 77   LEU   B C   1 
ATOM   3221  O  O   . LEU   B 2 77  ? 38.550  41.542  9.771   1.00 81.92  ? 77   LEU   B O   1 
ATOM   3222  C  CB  . LEU   B 2 77  ? 36.960  43.723  11.171  1.00 88.91  ? 77   LEU   B CB  1 
ATOM   3223  C  CG  . LEU   B 2 77  ? 35.996  44.315  10.150  1.00 85.90  ? 77   LEU   B CG  1 
ATOM   3224  C  CD1 . LEU   B 2 77  ? 34.588  43.959  10.550  1.00 86.93  ? 77   LEU   B CD1 1 
ATOM   3225  C  CD2 . LEU   B 2 77  ? 36.172  45.811  10.098  1.00 83.78  ? 77   LEU   B CD2 1 
ATOM   3226  N  N   . PHE   B 2 78  ? 36.443  40.776  9.458   1.00 87.73  ? 78   PHE   B N   1 
ATOM   3227  C  CA  . PHE   B 2 78  ? 36.718  40.130  8.178   1.00 88.94  ? 78   PHE   B CA  1 
ATOM   3228  C  C   . PHE   B 2 78  ? 36.105  40.999  7.093   1.00 85.04  ? 78   PHE   B C   1 
ATOM   3229  O  O   . PHE   B 2 78  ? 34.898  41.264  7.112   1.00 84.37  ? 78   PHE   B O   1 
ATOM   3230  C  CB  . PHE   B 2 78  ? 36.159  38.703  8.119   1.00 82.93  ? 78   PHE   B CB  1 
ATOM   3231  C  CG  . PHE   B 2 78  ? 36.330  38.014  6.778   1.00 79.18  ? 78   PHE   B CG  1 
ATOM   3232  C  CD1 . PHE   B 2 78  ? 37.572  37.542  6.364   1.00 80.73  ? 78   PHE   B CD1 1 
ATOM   3233  C  CD2 . PHE   B 2 78  ? 35.227  37.798  5.951   1.00 82.63  ? 78   PHE   B CD2 1 
ATOM   3234  C  CE1 . PHE   B 2 78  ? 37.725  36.877  5.130   1.00 80.89  ? 78   PHE   B CE1 1 
ATOM   3235  C  CE2 . PHE   B 2 78  ? 35.354  37.141  4.717   1.00 82.06  ? 78   PHE   B CE2 1 
ATOM   3236  C  CZ  . PHE   B 2 78  ? 36.611  36.672  4.307   1.00 82.49  ? 78   PHE   B CZ  1 
ATOM   3237  N  N   . ILE   B 2 79  ? 36.942  41.489  6.190   1.00 84.46  ? 79   ILE   B N   1 
ATOM   3238  C  CA  . ILE   B 2 79  ? 36.467  42.202  5.020   1.00 85.24  ? 79   ILE   B CA  1 
ATOM   3239  C  C   . ILE   B 2 79  ? 36.876  41.365  3.826   1.00 81.48  ? 79   ILE   B C   1 
ATOM   3240  O  O   . ILE   B 2 79  ? 37.914  40.696  3.849   1.00 79.15  ? 79   ILE   B O   1 
ATOM   3241  C  CB  . ILE   B 2 79  ? 37.005  43.654  4.937   1.00 87.73  ? 79   ILE   B CB  1 
ATOM   3242  C  CG1 . ILE   B 2 79  ? 36.039  44.633  5.623   1.00 78.94  ? 79   ILE   B CG1 1 
ATOM   3243  C  CG2 . ILE   B 2 79  ? 37.221  44.096  3.498   1.00 84.23  ? 79   ILE   B CG2 1 
ATOM   3244  C  CD1 . ILE   B 2 79  ? 35.894  44.410  7.091   1.00 82.99  ? 79   ILE   B CD1 1 
ATOM   3245  N  N   . LEU   B 2 80  ? 36.008  41.325  2.832   1.00 80.62  ? 80   LEU   B N   1 
ATOM   3246  C  CA  . LEU   B 2 80  ? 36.298  40.692  1.564   1.00 76.00  ? 80   LEU   B CA  1 
ATOM   3247  C  C   . LEU   B 2 80  ? 35.855  41.689  0.518   1.00 78.79  ? 80   LEU   B C   1 
ATOM   3248  O  O   . LEU   B 2 80  ? 34.728  42.191  0.587   1.00 77.92  ? 80   LEU   B O   1 
ATOM   3249  C  CB  . LEU   B 2 80  ? 35.558  39.357  1.430   1.00 79.65  ? 80   LEU   B CB  1 
ATOM   3250  C  CG  . LEU   B 2 80  ? 35.569  38.659  0.072   1.00 80.11  ? 80   LEU   B CG  1 
ATOM   3251  C  CD1 . LEU   B 2 80  ? 36.953  38.704  -0.547  1.00 81.10  ? 80   LEU   B CD1 1 
ATOM   3252  C  CD2 . LEU   B 2 80  ? 35.119  37.214  0.224   1.00 83.49  ? 80   LEU   B CD2 1 
ATOM   3253  N  N   . THR   B 2 81  ? 36.753  42.034  -0.398  1.00 80.22  ? 81   THR   B N   1 
ATOM   3254  C  CA  . THR   B 2 81  ? 36.446  43.030  -1.418  1.00 80.14  ? 81   THR   B CA  1 
ATOM   3255  C  C   . THR   B 2 81  ? 35.984  42.377  -2.711  1.00 80.20  ? 81   THR   B C   1 
ATOM   3256  O  O   . THR   B 2 81  ? 36.241  41.200  -2.973  1.00 78.54  ? 81   THR   B O   1 
ATOM   3257  C  CB  . THR   B 2 81  ? 37.651  43.907  -1.743  1.00 79.15  ? 81   THR   B CB  1 
ATOM   3258  O  OG1 . THR   B 2 81  ? 38.505  43.206  -2.666  1.00 79.82  ? 81   THR   B OG1 1 
ATOM   3259  C  CG2 . THR   B 2 81  ? 38.410  44.265  -0.474  1.00 75.63  ? 81   THR   B CG2 1 
ATOM   3260  N  N   . ALA   B 2 82  ? 35.359  43.192  -3.563  1.00 82.52  ? 82   ALA   B N   1 
ATOM   3261  C  CA  . ALA   B 2 82  ? 34.866  42.684  -4.841  1.00 79.02  ? 82   ALA   B CA  1 
ATOM   3262  C  C   . ALA   B 2 82  ? 35.971  42.084  -5.697  1.00 82.01  ? 82   ALA   B C   1 
ATOM   3263  O  O   . ALA   B 2 82  ? 35.711  41.188  -6.506  1.00 82.80  ? 82   ALA   B O   1 
ATOM   3264  C  CB  . ALA   B 2 82  ? 34.152  43.798  -5.603  1.00 81.45  ? 82   ALA   B CB  1 
ATOM   3265  N  N   . LYS   B 2 83  ? 37.212  42.559  -5.578  1.00 83.01  ? 83   LYS   B N   1 
ATOM   3266  C  CA  . LYS   B 2 83  ? 38.273  41.961  -6.385  1.00 81.23  ? 83   LYS   B CA  1 
ATOM   3267  C  C   . LYS   B 2 83  ? 38.892  40.846  -5.580  1.00 86.07  ? 83   LYS   B C   1 
ATOM   3268  O  O   . LYS   B 2 83  ? 40.108  40.585  -5.667  1.00 87.89  ? 83   LYS   B O   1 
ATOM   3269  C  CB  . LYS   B 2 83  ? 39.302  42.989  -6.836  1.00 80.95  ? 83   LYS   B CB  1 
ATOM   3270  C  CG  . LYS   B 2 83  ? 38.891  43.822  -8.027  1.00 84.60  ? 83   LYS   B CG  1 
ATOM   3271  C  CD  . LYS   B 2 83  ? 40.115  44.401  -8.671  1.00 90.59  ? 83   LYS   B CD  1 
ATOM   3272  C  CE  . LYS   B 2 83  ? 39.813  45.655  -9.457  1.00 89.86  ? 83   LYS   B CE  1 
ATOM   3273  N  NZ  . LYS   B 2 83  ? 41.125  46.221  -9.884  1.00 89.85  ? 83   LYS   B NZ  1 
ATOM   3274  N  N   . TYR   B 2 84  ? 38.082  40.203  -4.743  1.00 83.38  ? 84   TYR   B N   1 
ATOM   3275  C  CA  . TYR   B 2 84  ? 38.426  38.973  -4.032  1.00 83.14  ? 84   TYR   B CA  1 
ATOM   3276  C  C   . TYR   B 2 84  ? 39.550  39.159  -3.010  1.00 86.00  ? 84   TYR   B C   1 
ATOM   3277  O  O   . TYR   B 2 84  ? 40.139  38.166  -2.550  1.00 88.11  ? 84   TYR   B O   1 
ATOM   3278  C  CB  . TYR   B 2 84  ? 38.750  37.847  -5.026  1.00 83.84  ? 84   TYR   B CB  1 
ATOM   3279  C  CG  . TYR   B 2 84  ? 37.501  37.549  -5.834  1.00 87.30  ? 84   TYR   B CG  1 
ATOM   3280  C  CD1 . TYR   B 2 84  ? 36.446  36.813  -5.271  1.00 86.27  ? 84   TYR   B CD1 1 
ATOM   3281  C  CD2 . TYR   B 2 84  ? 37.333  38.059  -7.129  1.00 87.53  ? 84   TYR   B CD2 1 
ATOM   3282  C  CE1 . TYR   B 2 84  ? 35.268  36.564  -5.997  1.00 86.19  ? 84   TYR   B CE1 1 
ATOM   3283  C  CE2 . TYR   B 2 84  ? 36.156  37.811  -7.862  1.00 89.26  ? 84   TYR   B CE2 1 
ATOM   3284  C  CZ  . TYR   B 2 84  ? 35.126  37.063  -7.290  1.00 89.02  ? 84   TYR   B CZ  1 
ATOM   3285  O  OH  . TYR   B 2 84  ? 33.960  36.823  -8.016  1.00 85.39  ? 84   TYR   B OH  1 
ATOM   3286  N  N   . ASN   B 2 85  ? 39.823  40.393  -2.589  1.00 86.20  ? 85   ASN   B N   1 
ATOM   3287  C  CA  . ASN   B 2 85  ? 40.773  40.617  -1.507  1.00 82.11  ? 85   ASN   B CA  1 
ATOM   3288  C  C   . ASN   B 2 85  ? 40.118  40.333  -0.151  1.00 77.10  ? 85   ASN   B C   1 
ATOM   3289  O  O   . ASN   B 2 85  ? 39.015  40.815  0.147   1.00 69.75  ? 85   ASN   B O   1 
ATOM   3290  C  CB  . ASN   B 2 85  ? 41.321  42.049  -1.578  1.00 84.46  ? 85   ASN   B CB  1 
ATOM   3291  C  CG  . ASN   B 2 85  ? 41.742  42.446  -2.986  1.00 85.38  ? 85   ASN   B CG  1 
ATOM   3292  O  OD1 . ASN   B 2 85  ? 41.154  43.353  -3.600  1.00 82.13  ? 85   ASN   B OD1 1 
ATOM   3293  N  ND2 . ASN   B 2 85  ? 42.770  41.771  -3.503  1.00 87.10  ? 85   ASN   B ND2 1 
ATOM   3294  N  N   . ALA   B 2 86  ? 40.792  39.519  0.656   1.00 79.11  ? 86   ALA   B N   1 
ATOM   3295  C  CA  . ALA   B 2 86  ? 40.296  39.095  1.957   1.00 82.19  ? 86   ALA   B CA  1 
ATOM   3296  C  C   . ALA   B 2 86  ? 41.320  39.460  3.009   1.00 84.60  ? 86   ALA   B C   1 
ATOM   3297  O  O   . ALA   B 2 86  ? 42.510  39.183  2.846   1.00 88.08  ? 86   ALA   B O   1 
ATOM   3298  C  CB  . ALA   B 2 86  ? 40.017  37.591  2.018   1.00 86.52  ? 86   ALA   B CB  1 
ATOM   3299  N  N   . CYS   B 2 87  ? 40.844  40.079  4.088   1.00 86.96  ? 87   CYS   B N   1 
ATOM   3300  C  CA  . CYS   B 2 87  ? 41.692  40.519  5.179   1.00 87.59  ? 87   CYS   B CA  1 
ATOM   3301  C  C   . CYS   B 2 87  ? 40.971  40.259  6.488   1.00 89.29  ? 87   CYS   B C   1 
ATOM   3302  O  O   . CYS   B 2 87  ? 39.738  40.139  6.535   1.00 87.91  ? 87   CYS   B O   1 
ATOM   3303  C  CB  . CYS   B 2 87  ? 42.035  42.008  5.074   1.00 90.00  ? 87   CYS   B CB  1 
ATOM   3304  S  SG  . CYS   B 2 87  ? 40.621  43.142  5.318   1.00 97.51  ? 87   CYS   B SG  1 
ATOM   3305  N  N   . ILE   B 2 88  ? 41.754  40.195  7.556   1.00 91.98  ? 88   ILE   B N   1 
ATOM   3306  C  CA  . ILE   B 2 88  ? 41.230  40.207  8.910   1.00 91.76  ? 88   ILE   B CA  1 
ATOM   3307  C  C   . ILE   B 2 88  ? 41.895  41.365  9.639   1.00 93.45  ? 88   ILE   B C   1 
ATOM   3308  O  O   . ILE   B 2 88  ? 43.126  41.462  9.655   1.00 97.81  ? 88   ILE   B O   1 
ATOM   3309  C  CB  . ILE   B 2 88  ? 41.480  38.869  9.625   1.00 90.09  ? 88   ILE   B CB  1 
ATOM   3310  C  CG1 . ILE   B 2 88  ? 40.562  37.774  9.064   1.00 90.17  ? 88   ILE   B CG1 1 
ATOM   3311  C  CG2 . ILE   B 2 88  ? 41.260  39.048  11.088  1.00 92.35  ? 88   ILE   B CG2 1 
ATOM   3312  C  CD1 . ILE   B 2 88  ? 40.382  36.580  9.984   1.00 88.85  ? 88   ILE   B CD1 1 
ATOM   3313  N  N   . LEU   B 2 89  ? 41.094  42.274  10.186  1.00 94.20  ? 89   LEU   B N   1 
ATOM   3314  C  CA  . LEU   B 2 89  ? 41.628  43.500  10.766  1.00 96.43  ? 89   LEU   B CA  1 
ATOM   3315  C  C   . LEU   B 2 89  ? 41.427  43.504  12.277  1.00 93.27  ? 89   LEU   B C   1 
ATOM   3316  O  O   . LEU   B 2 89  ? 40.491  42.888  12.804  1.00 92.19  ? 89   LEU   B O   1 
ATOM   3317  C  CB  . LEU   B 2 89  ? 40.972  44.759  10.133  1.00 92.85  ? 89   LEU   B CB  1 
ATOM   3318  C  CG  . LEU   B 2 89  ? 40.870  44.731  8.602   1.00 91.92  ? 89   LEU   B CG  1 
ATOM   3319  C  CD1 . LEU   B 2 89  ? 40.672  46.095  8.030   1.00 89.72  ? 89   LEU   B CD1 1 
ATOM   3320  C  CD2 . LEU   B 2 89  ? 42.122  44.114  8.004   1.00 99.00  ? 89   LEU   B CD2 1 
ATOM   3321  N  N   . GLU   B 2 90  ? 42.333  44.185  12.967  1.00 95.61  ? 90   GLU   B N   1 
ATOM   3322  C  CA  . GLU   B 2 90  ? 42.223  44.408  14.400  1.00 100.94 ? 90   GLU   B CA  1 
ATOM   3323  C  C   . GLU   B 2 90  ? 42.414  45.887  14.707  1.00 104.45 ? 90   GLU   B C   1 
ATOM   3324  O  O   . GLU   B 2 90  ? 43.100  46.610  13.978  1.00 102.17 ? 90   GLU   B O   1 
ATOM   3325  C  CB  . GLU   B 2 90  ? 43.250  43.601  15.192  1.00 99.40  ? 90   GLU   B CB  1 
ATOM   3326  C  CG  . GLU   B 2 90  ? 43.160  43.866  16.681  1.00 102.33 ? 90   GLU   B CG  1 
ATOM   3327  C  CD  . GLU   B 2 90  ? 44.212  43.127  17.479  1.00 106.32 ? 90   GLU   B CD  1 
ATOM   3328  O  OE1 . GLU   B 2 90  ? 45.167  42.598  16.864  1.00 106.66 ? 90   GLU   B OE1 1 
ATOM   3329  O  OE2 . GLU   B 2 90  ? 44.077  43.066  18.724  1.00 107.17 ? 90   GLU   B OE2 1 
ATOM   3330  N  N   . TYR   B 2 91  ? 41.823  46.318  15.815  1.00 102.75 ? 91   TYR   B N   1 
ATOM   3331  C  CA  . TYR   B 2 91  ? 41.917  47.694  16.275  1.00 105.51 ? 91   TYR   B CA  1 
ATOM   3332  C  C   . TYR   B 2 91  ? 43.097  47.836  17.235  1.00 106.47 ? 91   TYR   B C   1 
ATOM   3333  O  O   . TYR   B 2 91  ? 43.421  46.905  17.977  1.00 105.48 ? 91   TYR   B O   1 
ATOM   3334  C  CB  . TYR   B 2 91  ? 40.589  48.068  16.938  1.00 107.44 ? 91   TYR   B CB  1 
ATOM   3335  C  CG  . TYR   B 2 91  ? 40.373  49.518  17.266  1.00 112.25 ? 91   TYR   B CG  1 
ATOM   3336  C  CD1 . TYR   B 2 91  ? 40.459  50.510  16.296  1.00 112.72 ? 91   TYR   B CD1 1 
ATOM   3337  C  CD2 . TYR   B 2 91  ? 40.019  49.885  18.546  1.00 111.02 ? 91   TYR   B CD2 1 
ATOM   3338  C  CE1 . TYR   B 2 91  ? 40.246  51.841  16.626  1.00 109.10 ? 91   TYR   B CE1 1 
ATOM   3339  C  CE2 . TYR   B 2 91  ? 39.795  51.187  18.882  1.00 110.37 ? 91   TYR   B CE2 1 
ATOM   3340  C  CZ  . TYR   B 2 91  ? 39.915  52.169  17.931  1.00 110.02 ? 91   TYR   B CZ  1 
ATOM   3341  O  OH  . TYR   B 2 91  ? 39.703  53.482  18.312  1.00 114.95 ? 91   TYR   B OH  1 
ATOM   3342  N  N   . LYS   B 2 92  ? 43.749  49.003  17.214  1.00 113.79 ? 92   LYS   B N   1 
ATOM   3343  C  CA  . LYS   B 2 92  ? 44.912  49.216  18.087  1.00 121.90 ? 92   LYS   B CA  1 
ATOM   3344  C  C   . LYS   B 2 92  ? 45.196  50.712  18.263  1.00 127.58 ? 92   LYS   B C   1 
ATOM   3345  O  O   . LYS   B 2 92  ? 45.598  51.389  17.307  1.00 125.23 ? 92   LYS   B O   1 
ATOM   3346  C  CB  . LYS   B 2 92  ? 46.131  48.476  17.526  1.00 115.10 ? 92   LYS   B CB  1 
ATOM   3347  N  N   . GLN   B 2 93  ? 45.039  51.213  19.497  1.00 132.53 ? 93   GLN   B N   1 
ATOM   3348  C  CA  . GLN   B 2 93  ? 45.151  52.642  19.824  1.00 132.50 ? 93   GLN   B CA  1 
ATOM   3349  C  C   . GLN   B 2 93  ? 46.267  52.890  20.842  1.00 134.78 ? 93   GLN   B C   1 
ATOM   3350  O  O   . GLN   B 2 93  ? 46.074  52.670  22.041  1.00 133.58 ? 93   GLN   B O   1 
ATOM   3351  C  CB  . GLN   B 2 93  ? 43.828  53.169  20.368  1.00 131.47 ? 93   GLN   B CB  1 
ATOM   3352  C  CG  . GLN   B 2 93  ? 43.941  54.488  21.113  1.00 135.36 ? 93   GLN   B CG  1 
ATOM   3353  C  CD  . GLN   B 2 93  ? 42.606  54.970  21.652  1.00 135.45 ? 93   GLN   B CD  1 
ATOM   3354  O  OE1 . GLN   B 2 93  ? 41.542  54.434  21.294  1.00 132.24 ? 93   GLN   B OE1 1 
ATOM   3355  N  NE2 . GLN   B 2 93  ? 42.650  55.986  22.519  1.00 130.08 ? 93   GLN   B NE2 1 
ATOM   3356  N  N   . SER   B 2 94  ? 47.419  53.389  20.390  1.00 140.43 ? 94   SER   B N   1 
ATOM   3357  C  CA  . SER   B 2 94  ? 48.486  53.729  21.326  1.00 141.84 ? 94   SER   B CA  1 
ATOM   3358  C  C   . SER   B 2 94  ? 48.034  55.006  22.043  1.00 144.15 ? 94   SER   B C   1 
ATOM   3359  O  O   . SER   B 2 94  ? 48.394  56.106  21.629  1.00 148.98 ? 94   SER   B O   1 
ATOM   3360  C  CB  . SER   B 2 94  ? 49.800  53.962  20.580  1.00 142.30 ? 94   SER   B CB  1 
ATOM   3361  O  OG  . SER   B 2 94  ? 50.888  54.164  21.472  1.00 143.22 ? 94   SER   B OG  1 
ATOM   3362  N  N   . GLY   B 2 95  ? 47.251  54.869  23.122  1.00 140.83 ? 95   GLY   B N   1 
ATOM   3363  C  CA  . GLY   B 2 95  ? 46.650  56.047  23.728  1.00 136.70 ? 95   GLY   B CA  1 
ATOM   3364  C  C   . GLY   B 2 95  ? 46.027  57.050  22.779  1.00 140.46 ? 95   GLY   B C   1 
ATOM   3365  O  O   . GLY   B 2 95  ? 44.799  57.158  22.695  1.00 139.62 ? 95   GLY   B O   1 
ATOM   3366  N  N   . GLU   B 2 96  ? 46.873  57.780  22.047  1.00 141.74 ? 96   GLU   B N   1 
ATOM   3367  C  CA  . GLU   B 2 96  ? 46.426  58.745  21.048  1.00 142.07 ? 96   GLU   B CA  1 
ATOM   3368  C  C   . GLU   B 2 96  ? 46.442  58.200  19.624  1.00 144.22 ? 96   GLU   B C   1 
ATOM   3369  O  O   . GLU   B 2 96  ? 45.619  58.617  18.802  1.00 139.35 ? 96   GLU   B O   1 
ATOM   3370  C  CB  . GLU   B 2 96  ? 47.293  60.010  21.109  1.00 134.37 ? 96   GLU   B CB  1 
ATOM   3371  N  N   . SER   B 2 97  ? 47.345  57.260  19.327  1.00 150.93 ? 97   SER   B N   1 
ATOM   3372  C  CA  . SER   B 2 97  ? 47.548  56.753  17.973  1.00 151.34 ? 97   SER   B CA  1 
ATOM   3373  C  C   . SER   B 2 97  ? 46.616  55.572  17.701  1.00 146.41 ? 97   SER   B C   1 
ATOM   3374  O  O   . SER   B 2 97  ? 46.677  54.557  18.410  1.00 143.79 ? 97   SER   B O   1 
ATOM   3375  C  CB  . SER   B 2 97  ? 49.008  56.340  17.792  1.00 150.25 ? 97   SER   B CB  1 
ATOM   3376  O  OG  . SER   B 2 97  ? 49.159  55.499  16.667  1.00 149.48 ? 97   SER   B OG  1 
ATOM   3377  N  N   . ILE   B 2 98  ? 45.779  55.684  16.663  1.00 134.84 ? 98   ILE   B N   1 
ATOM   3378  C  CA  . ILE   B 2 98  ? 44.792  54.650  16.323  1.00 131.02 ? 98   ILE   B CA  1 
ATOM   3379  C  C   . ILE   B 2 98  ? 45.064  54.081  14.934  1.00 125.55 ? 98   ILE   B C   1 
ATOM   3380  O  O   . ILE   B 2 98  ? 44.916  54.781  13.923  1.00 117.12 ? 98   ILE   B O   1 
ATOM   3381  C  CB  . ILE   B 2 98  ? 43.357  55.182  16.393  1.00 126.15 ? 98   ILE   B CB  1 
ATOM   3382  C  CG1 . ILE   B 2 98  ? 42.910  55.274  17.842  1.00 129.66 ? 98   ILE   B CG1 1 
ATOM   3383  C  CG2 . ILE   B 2 98  ? 42.415  54.271  15.625  1.00 117.73 ? 98   ILE   B CG2 1 
ATOM   3384  C  CD1 . ILE   B 2 98  ? 41.424  55.595  17.965  1.00 123.76 ? 98   ILE   B CD1 1 
ATOM   3385  N  N   . ASP   B 2 99  ? 45.411  52.788  14.883  1.00 126.30 ? 99   ASP   B N   1 
ATOM   3386  C  CA  . ASP   B 2 99  ? 45.724  52.083  13.645  1.00 124.46 ? 99   ASP   B CA  1 
ATOM   3387  C  C   . ASP   B 2 99  ? 44.877  50.812  13.524  1.00 120.47 ? 99   ASP   B C   1 
ATOM   3388  O  O   . ASP   B 2 99  ? 44.521  50.186  14.531  1.00 116.69 ? 99   ASP   B O   1 
ATOM   3389  C  CB  . ASP   B 2 99  ? 47.240  51.734  13.569  1.00 127.40 ? 99   ASP   B CB  1 
ATOM   3390  C  CG  . ASP   B 2 99  ? 48.162  52.939  13.862  1.00 134.07 ? 99   ASP   B CG  1 
ATOM   3391  O  OD1 . ASP   B 2 99  ? 47.654  54.047  14.166  1.00 136.96 ? 99   ASP   B OD1 1 
ATOM   3392  O  OD2 . ASP   B 2 99  ? 49.404  52.773  13.793  1.00 138.36 ? 99   ASP   B OD2 1 
ATOM   3393  N  N   . ILE   B 2 100 ? 44.537  50.451  12.282  1.00 116.82 ? 100  ILE   B N   1 
ATOM   3394  C  CA  . ILE   B 2 100 ? 43.800  49.230  11.971  1.00 108.85 ? 100  ILE   B CA  1 
ATOM   3395  C  C   . ILE   B 2 100 ? 44.785  48.283  11.312  1.00 109.04 ? 100  ILE   B C   1 
ATOM   3396  O  O   . ILE   B 2 100 ? 45.109  48.437  10.127  1.00 109.29 ? 100  ILE   B O   1 
ATOM   3397  C  CB  . ILE   B 2 100 ? 42.595  49.492  11.057  1.00 101.73 ? 100  ILE   B CB  1 
ATOM   3398  C  CG1 . ILE   B 2 100 ? 41.707  50.607  11.612  1.00 105.79 ? 100  ILE   B CG1 1 
ATOM   3399  C  CG2 . ILE   B 2 100 ? 41.770  48.218  10.890  1.00 99.35  ? 100  ILE   B CG2 1 
ATOM   3400  C  CD1 . ILE   B 2 100 ? 40.832  50.176  12.783  1.00 102.40 ? 100  ILE   B CD1 1 
ATOM   3401  N  N   . ILE   B 2 101 ? 45.251  47.306  12.066  1.00 108.72 ? 101  ILE   B N   1 
ATOM   3402  C  CA  . ILE   B 2 101 ? 46.292  46.398  11.599  1.00 108.33 ? 101  ILE   B CA  1 
ATOM   3403  C  C   . ILE   B 2 101 ? 45.662  45.197  10.907  1.00 105.68 ? 101  ILE   B C   1 
ATOM   3404  O  O   . ILE   B 2 101 ? 44.669  44.629  11.379  1.00 106.47 ? 101  ILE   B O   1 
ATOM   3405  C  CB  . ILE   B 2 101 ? 47.168  45.966  12.779  1.00 110.50 ? 101  ILE   B CB  1 
ATOM   3406  C  CG1 . ILE   B 2 101 ? 46.312  45.204  13.780  1.00 113.76 ? 101  ILE   B CG1 1 
ATOM   3407  C  CG2 . ILE   B 2 101 ? 47.735  47.200  13.464  1.00 114.27 ? 101  ILE   B CG2 1 
ATOM   3408  C  CD1 . ILE   B 2 101 ? 46.903  43.885  14.193  1.00 118.95 ? 101  ILE   B CD1 1 
ATOM   3409  N  N   . THR   B 2 102 ? 46.238  44.801  9.783   1.00 103.35 ? 102  THR   B N   1 
ATOM   3410  C  CA  . THR   B 2 102 ? 45.763  43.634  9.051   1.00 102.46 ? 102  THR   B CA  1 
ATOM   3411  C  C   . THR   B 2 102 ? 46.489  42.399  9.594   1.00 104.97 ? 102  THR   B C   1 
ATOM   3412  O  O   . THR   B 2 102 ? 47.692  42.208  9.364   1.00 100.32 ? 102  THR   B O   1 
ATOM   3413  C  CB  . THR   B 2 102 ? 45.973  43.816  7.547   1.00 101.30 ? 102  THR   B CB  1 
ATOM   3414  O  OG1 . THR   B 2 102 ? 45.320  42.767  6.821   1.00 105.36 ? 102  THR   B OG1 1 
ATOM   3415  C  CG2 . THR   B 2 102 ? 47.463  43.805  7.224   1.00 101.67 ? 102  THR   B CG2 1 
ATOM   3416  N  N   . ARG   B 2 103 ? 45.750  41.568  10.332  1.00 104.88 ? 103  ARG   B N   1 
ATOM   3417  C  CA  . ARG   B 2 103 ? 46.287  40.348  10.917  1.00 98.58  ? 103  ARG   B CA  1 
ATOM   3418  C  C   . ARG   B 2 103 ? 46.398  39.217  9.900   1.00 96.81  ? 103  ARG   B C   1 
ATOM   3419  O  O   . ARG   B 2 103 ? 47.309  38.392  10.002  1.00 100.27 ? 103  ARG   B O   1 
ATOM   3420  C  CB  . ARG   B 2 103 ? 45.406  39.929  12.088  1.00 98.04  ? 103  ARG   B CB  1 
ATOM   3421  C  CG  . ARG   B 2 103 ? 45.306  40.988  13.192  1.00 101.91 ? 103  ARG   B CG  1 
ATOM   3422  C  CD  . ARG   B 2 103 ? 46.224  40.611  14.350  1.00 110.55 ? 103  ARG   B CD  1 
ATOM   3423  N  NE  . ARG   B 2 103 ? 45.989  39.231  14.779  1.00 105.72 ? 103  ARG   B NE  1 
ATOM   3424  C  CZ  . ARG   B 2 103 ? 45.188  38.901  15.780  1.00 103.55 ? 103  ARG   B CZ  1 
ATOM   3425  N  NH1 . ARG   B 2 103 ? 44.610  39.824  16.538  1.00 105.02 ? 103  ARG   B NH1 1 
ATOM   3426  N  NH2 . ARG   B 2 103 ? 44.948  37.621  16.018  1.00 101.84 ? 103  ARG   B NH2 1 
ATOM   3427  N  N   . ALA   B 2 104 ? 45.492  39.151  8.926   1.00 95.85  ? 104  ALA   B N   1 
ATOM   3428  C  CA  . ALA   B 2 104 ? 45.604  38.187  7.839   1.00 96.61  ? 104  ALA   B CA  1 
ATOM   3429  C  C   . ALA   B 2 104 ? 45.123  38.842  6.556   1.00 100.86 ? 104  ALA   B C   1 
ATOM   3430  O  O   . ALA   B 2 104 ? 44.362  39.821  6.581   1.00 98.62  ? 104  ALA   B O   1 
ATOM   3431  C  CB  . ALA   B 2 104 ? 44.790  36.914  8.096   1.00 93.61  ? 104  ALA   B CB  1 
ATOM   3432  N  N   . HIS   B 2 105 ? 45.568  38.285  5.429   1.00 97.82  ? 105  HIS   B N   1 
ATOM   3433  C  CA  . HIS   B 2 105 ? 45.139  38.779  4.129   1.00 95.96  ? 105  HIS   B CA  1 
ATOM   3434  C  C   . HIS   B 2 105 ? 45.490  37.750  3.061   1.00 96.34  ? 105  HIS   B C   1 
ATOM   3435  O  O   . HIS   B 2 105 ? 46.219  36.792  3.311   1.00 101.37 ? 105  HIS   B O   1 
ATOM   3436  C  CB  . HIS   B 2 105 ? 45.765  40.141  3.816   1.00 99.32  ? 105  HIS   B CB  1 
ATOM   3437  C  CG  . HIS   B 2 105 ? 47.257  40.106  3.710   1.00 101.90 ? 105  HIS   B CG  1 
ATOM   3438  N  ND1 . HIS   B 2 105 ? 47.930  40.460  2.559   1.00 100.65 ? 105  HIS   B ND1 1 
ATOM   3439  C  CD2 . HIS   B 2 105 ? 48.205  39.750  4.610   1.00 105.89 ? 105  HIS   B CD2 1 
ATOM   3440  C  CE1 . HIS   B 2 105 ? 49.230  40.331  2.757   1.00 103.83 ? 105  HIS   B CE1 1 
ATOM   3441  N  NE2 . HIS   B 2 105 ? 49.424  39.902  3.993   1.00 110.87 ? 105  HIS   B NE2 1 
ATOM   3442  N  N   . GLY   B 2 106 ? 44.938  37.955  1.877   1.00 94.79  ? 106  GLY   B N   1 
ATOM   3443  C  CA  . GLY   B 2 106 ? 45.156  37.140  0.699   1.00 85.96  ? 106  GLY   B CA  1 
ATOM   3444  C  C   . GLY   B 2 106 ? 43.994  37.308  -0.265  1.00 84.88  ? 106  GLY   B C   1 
ATOM   3445  O  O   . GLY   B 2 106 ? 42.896  37.727  0.095   1.00 88.00  ? 106  GLY   B O   1 
ATOM   3446  N  N   . ASN   B 2 107 ? 44.234  36.978  -1.529  1.00 83.14  ? 107  ASN   B N   1 
ATOM   3447  C  CA  . ASN   B 2 107 ? 43.195  37.023  -2.553  1.00 80.02  ? 107  ASN   B CA  1 
ATOM   3448  C  C   . ASN   B 2 107 ? 42.585  35.635  -2.720  1.00 83.22  ? 107  ASN   B C   1 
ATOM   3449  O  O   . ASN   B 2 107 ? 43.281  34.696  -3.114  1.00 84.48  ? 107  ASN   B O   1 
ATOM   3450  C  CB  . ASN   B 2 107 ? 43.771  37.518  -3.871  1.00 81.05  ? 107  ASN   B CB  1 
ATOM   3451  C  CG  . ASN   B 2 107 ? 42.706  37.844  -4.879  1.00 91.44  ? 107  ASN   B CG  1 
ATOM   3452  O  OD1 . ASN   B 2 107 ? 41.932  38.794  -4.688  1.00 94.66  ? 107  ASN   B OD1 1 
ATOM   3453  N  ND2 . ASN   B 2 107 ? 42.659  37.076  -5.972  1.00 91.96  ? 107  ASN   B ND2 1 
ATOM   3454  N  N   . VAL   B 2 108 ? 41.290  35.510  -2.423  1.00 83.29  ? 108  VAL   B N   1 
ATOM   3455  C  CA  . VAL   B 2 108 ? 40.631  34.206  -2.353  1.00 84.31  ? 108  VAL   B CA  1 
ATOM   3456  C  C   . VAL   B 2 108 ? 40.137  33.747  -3.717  1.00 90.95  ? 108  VAL   B C   1 
ATOM   3457  O  O   . VAL   B 2 108 ? 39.408  32.744  -3.819  1.00 90.51  ? 108  VAL   B O   1 
ATOM   3458  C  CB  . VAL   B 2 108 ? 39.456  34.233  -1.366  1.00 85.58  ? 108  VAL   B CB  1 
ATOM   3459  C  CG1 . VAL   B 2 108 ? 39.975  34.330  0.071   1.00 84.85  ? 108  VAL   B CG1 1 
ATOM   3460  C  CG2 . VAL   B 2 108 ? 38.497  35.387  -1.726  1.00 88.46  ? 108  VAL   B CG2 1 
ATOM   3461  N  N   . GLN   B 2 109 ? 40.530  34.464  -4.772  1.00 90.96  ? 109  GLN   B N   1 
ATOM   3462  C  CA  . GLN   B 2 109 ? 40.015  34.167  -6.104  1.00 90.74  ? 109  GLN   B CA  1 
ATOM   3463  C  C   . GLN   B 2 109 ? 40.405  32.754  -6.552  1.00 91.22  ? 109  GLN   B C   1 
ATOM   3464  O  O   . GLN   B 2 109 ? 41.417  32.202  -6.120  1.00 93.31  ? 109  GLN   B O   1 
ATOM   3465  C  CB  . GLN   B 2 109 ? 40.535  35.198  -7.095  1.00 89.21  ? 109  GLN   B CB  1 
ATOM   3466  C  CG  . GLN   B 2 109 ? 40.159  34.888  -8.509  1.00 92.23  ? 109  GLN   B CG  1 
ATOM   3467  C  CD  . GLN   B 2 109 ? 40.311  36.082  -9.406  1.00 96.66  ? 109  GLN   B CD  1 
ATOM   3468  O  OE1 . GLN   B 2 109 ? 41.224  36.904  -9.219  1.00 99.42  ? 109  GLN   B OE1 1 
ATOM   3469  N  NE2 . GLN   B 2 109 ? 39.408  36.208  -10.381 1.00 93.18  ? 109  GLN   B NE2 1 
ATOM   3470  N  N   . ASP   B 2 110 ? 39.581  32.154  -7.418  1.00 92.78  ? 110  ASP   B N   1 
ATOM   3471  C  CA  . ASP   B 2 110 ? 39.880  30.860  -8.025  1.00 94.73  ? 110  ASP   B CA  1 
ATOM   3472  C  C   . ASP   B 2 110 ? 40.047  31.049  -9.530  1.00 99.10  ? 110  ASP   B C   1 
ATOM   3473  O  O   . ASP   B 2 110 ? 39.192  31.666  -10.178 1.00 95.77  ? 110  ASP   B O   1 
ATOM   3474  C  CB  . ASP   B 2 110 ? 38.788  29.817  -7.733  1.00 96.12  ? 110  ASP   B CB  1 
ATOM   3475  C  CG  . ASP   B 2 110 ? 38.710  29.420  -6.258  1.00 92.11  ? 110  ASP   B CG  1 
ATOM   3476  O  OD1 . ASP   B 2 110 ? 39.763  29.418  -5.569  1.00 88.85  ? 110  ASP   B OD1 1 
ATOM   3477  O  OD2 . ASP   B 2 110 ? 37.583  29.100  -5.800  1.00 90.27  ? 110  ASP   B OD2 1 
ATOM   3478  N  N   . ARG   B 2 111 ? 41.157  30.514  -10.069 1.00 108.65 ? 111  ARG   B N   1 
ATOM   3479  C  CA  . ARG   B 2 111 ? 41.532  30.697  -11.470 1.00 108.99 ? 111  ARG   B CA  1 
ATOM   3480  C  C   . ARG   B 2 111 ? 40.350  30.448  -12.388 1.00 110.02 ? 111  ARG   B C   1 
ATOM   3481  O  O   . ARG   B 2 111 ? 40.093  31.229  -13.311 1.00 113.30 ? 111  ARG   B O   1 
ATOM   3482  C  CB  . ARG   B 2 111 ? 42.693  29.761  -11.828 1.00 110.79 ? 111  ARG   B CB  1 
ATOM   3483  N  N   . ILE   B 2 112 ? 39.628  29.362  -12.142 1.00 100.50 ? 112  ILE   B N   1 
ATOM   3484  C  CA  . ILE   B 2 112 ? 38.402  29.060  -12.858 1.00 101.94 ? 112  ILE   B CA  1 
ATOM   3485  C  C   . ILE   B 2 112 ? 37.243  29.116  -11.860 1.00 100.68 ? 112  ILE   B C   1 
ATOM   3486  O  O   . ILE   B 2 112 ? 37.439  28.943  -10.650 1.00 100.86 ? 112  ILE   B O   1 
ATOM   3487  C  CB  . ILE   B 2 112 ? 38.468  27.675  -13.535 1.00 115.01 ? 112  ILE   B CB  1 
ATOM   3488  C  CG1 . ILE   B 2 112 ? 37.108  27.284  -14.132 1.00 116.69 ? 112  ILE   B CG1 1 
ATOM   3489  C  CG2 . ILE   B 2 112 ? 38.944  26.614  -12.529 1.00 106.06 ? 112  ILE   B CG2 1 
ATOM   3490  C  CD1 . ILE   B 2 112 ? 36.495  28.307  -15.108 1.00 108.64 ? 112  ILE   B CD1 1 
ATOM   3491  N  N   . GLY   B 2 113 ? 36.041  29.354  -12.368 1.00 99.85  ? 113  GLY   B N   1 
ATOM   3492  C  CA  . GLY   B 2 113 ? 34.834  29.280  -11.568 1.00 94.95  ? 113  GLY   B CA  1 
ATOM   3493  C  C   . GLY   B 2 113 ? 33.798  30.269  -12.040 1.00 97.71  ? 113  GLY   B C   1 
ATOM   3494  O  O   . GLY   B 2 113 ? 34.165  31.412  -12.335 1.00 101.71 ? 113  GLY   B O   1 
ATOM   3495  N  N   . ARG   B 2 114 ? 32.529  29.863  -12.174 1.00 89.39  ? 114  ARG   B N   1 
ATOM   3496  C  CA  . ARG   B 2 114 ? 31.482  30.823  -12.546 1.00 93.56  ? 114  ARG   B CA  1 
ATOM   3497  C  C   . ARG   B 2 114 ? 31.102  31.632  -11.310 1.00 95.87  ? 114  ARG   B C   1 
ATOM   3498  O  O   . ARG   B 2 114 ? 30.760  31.040  -10.281 1.00 98.78  ? 114  ARG   B O   1 
ATOM   3499  C  CB  . ARG   B 2 114 ? 30.267  30.127  -13.124 1.00 92.20  ? 114  ARG   B CB  1 
ATOM   3500  N  N   . PRO   B 2 115 ? 31.170  32.959  -11.345 1.00 93.40  ? 115  PRO   B N   1 
ATOM   3501  C  CA  . PRO   B 2 115 ? 30.625  33.737  -10.227 1.00 92.65  ? 115  PRO   B CA  1 
ATOM   3502  C  C   . PRO   B 2 115 ? 29.156  33.396  -10.010 1.00 93.88  ? 115  PRO   B C   1 
ATOM   3503  O  O   . PRO   B 2 115 ? 28.376  33.283  -10.959 1.00 93.35  ? 115  PRO   B O   1 
ATOM   3504  C  CB  . PRO   B 2 115 ? 30.817  35.187  -10.682 1.00 91.71  ? 115  PRO   B CB  1 
ATOM   3505  C  CG  . PRO   B 2 115 ? 32.054  35.115  -11.524 1.00 92.46  ? 115  PRO   B CG  1 
ATOM   3506  C  CD  . PRO   B 2 115 ? 31.998  33.785  -12.238 1.00 93.95  ? 115  PRO   B CD  1 
ATOM   3507  N  N   . SER   B 2 116 ? 28.785  33.191  -8.750  1.00 91.37  ? 116  SER   B N   1 
ATOM   3508  C  CA  . SER   B 2 116 ? 27.398  32.900  -8.448  1.00 89.93  ? 116  SER   B CA  1 
ATOM   3509  C  C   . SER   B 2 116 ? 26.523  34.110  -8.736  1.00 92.46  ? 116  SER   B C   1 
ATOM   3510  O  O   . SER   B 2 116 ? 26.951  35.264  -8.607  1.00 90.68  ? 116  SER   B O   1 
ATOM   3511  C  CB  . SER   B 2 116 ? 27.249  32.484  -6.992  1.00 86.02  ? 116  SER   B CB  1 
ATOM   3512  O  OG  . SER   B 2 116 ? 27.769  31.179  -6.829  1.00 91.35  ? 116  SER   B OG  1 
ATOM   3513  N  N   . GLU   B 2 117 ? 25.274  33.824  -9.119  1.00 91.76  ? 117  GLU   B N   1 
ATOM   3514  C  CA  . GLU   B 2 117 ? 24.318  34.876  -9.448  1.00 84.37  ? 117  GLU   B CA  1 
ATOM   3515  C  C   . GLU   B 2 117 ? 23.980  35.726  -8.234  1.00 88.53  ? 117  GLU   B C   1 
ATOM   3516  O  O   . GLU   B 2 117 ? 23.972  36.960  -8.313  1.00 100.33 ? 117  GLU   B O   1 
ATOM   3517  C  CB  . GLU   B 2 117 ? 23.043  34.268  -10.018 1.00 90.00  ? 117  GLU   B CB  1 
ATOM   3518  C  CG  . GLU   B 2 117 ? 23.246  33.415  -11.257 1.00 101.98 ? 117  GLU   B CG  1 
ATOM   3519  C  CD  . GLU   B 2 117 ? 21.938  33.168  -12.008 1.00 113.62 ? 117  GLU   B CD  1 
ATOM   3520  O  OE1 . GLU   B 2 117 ? 21.796  32.083  -12.624 1.00 118.93 ? 117  GLU   B OE1 1 
ATOM   3521  O  OE2 . GLU   B 2 117 ? 21.049  34.056  -11.984 1.00 116.71 ? 117  GLU   B OE2 1 
ATOM   3522  N  N   . THR   B 2 118 ? 23.658  35.089  -7.107  1.00 89.66  ? 118  THR   B N   1 
ATOM   3523  C  CA  . THR   B 2 118 ? 23.375  35.855  -5.899  1.00 90.93  ? 118  THR   B CA  1 
ATOM   3524  C  C   . THR   B 2 118 ? 24.630  36.459  -5.277  1.00 90.33  ? 118  THR   B C   1 
ATOM   3525  O  O   . THR   B 2 118 ? 24.526  37.079  -4.216  1.00 93.11  ? 118  THR   B O   1 
ATOM   3526  C  CB  . THR   B 2 118 ? 22.671  34.994  -4.849  1.00 87.62  ? 118  THR   B CB  1 
ATOM   3527  O  OG1 . THR   B 2 118 ? 23.577  33.979  -4.410  1.00 85.24  ? 118  THR   B OG1 1 
ATOM   3528  C  CG2 . THR   B 2 118 ? 21.401  34.358  -5.408  1.00 87.40  ? 118  THR   B CG2 1 
ATOM   3529  N  N   . GLY   B 2 119 ? 25.801  36.286  -5.883  1.00 86.41  ? 119  GLY   B N   1 
ATOM   3530  C  CA  . GLY   B 2 119 ? 26.962  37.081  -5.514  1.00 87.46  ? 119  GLY   B CA  1 
ATOM   3531  C  C   . GLY   B 2 119 ? 27.749  36.545  -4.333  1.00 77.72  ? 119  GLY   B C   1 
ATOM   3532  O  O   . GLY   B 2 119 ? 27.523  35.445  -3.835  1.00 80.19  ? 119  GLY   B O   1 
ATOM   3533  N  N   . ILE   B 2 120 ? 28.706  37.349  -3.878  1.00 77.95  ? 120  ILE   B N   1 
ATOM   3534  C  CA  . ILE   B 2 120 ? 29.654  36.883  -2.870  1.00 76.68  ? 120  ILE   B CA  1 
ATOM   3535  C  C   . ILE   B 2 120 ? 28.932  36.767  -1.538  1.00 76.79  ? 120  ILE   B C   1 
ATOM   3536  O  O   . ILE   B 2 120 ? 28.331  37.733  -1.071  1.00 79.23  ? 120  ILE   B O   1 
ATOM   3537  C  CB  . ILE   B 2 120 ? 30.862  37.818  -2.757  1.00 73.26  ? 120  ILE   B CB  1 
ATOM   3538  C  CG1 . ILE   B 2 120 ? 31.665  37.823  -4.059  1.00 78.21  ? 120  ILE   B CG1 1 
ATOM   3539  C  CG2 . ILE   B 2 120 ? 31.736  37.361  -1.610  1.00 80.12  ? 120  ILE   B CG2 1 
ATOM   3540  C  CD1 . ILE   B 2 120 ? 32.732  38.969  -4.212  1.00 73.04  ? 120  ILE   B CD1 1 
ATOM   3541  N  N   . ILE   B 2 121 ? 28.970  35.578  -0.936  1.00 75.05  ? 121  ILE   B N   1 
ATOM   3542  C  CA  . ILE   B 2 121 ? 28.469  35.347  0.413   1.00 69.34  ? 121  ILE   B CA  1 
ATOM   3543  C  C   . ILE   B 2 121 ? 29.652  34.997  1.303   1.00 78.30  ? 121  ILE   B C   1 
ATOM   3544  O  O   . ILE   B 2 121 ? 30.523  34.208  0.912   1.00 78.28  ? 121  ILE   B O   1 
ATOM   3545  C  CB  . ILE   B 2 121 ? 27.419  34.224  0.461   1.00 68.30  ? 121  ILE   B CB  1 
ATOM   3546  C  CG1 . ILE   B 2 121 ? 26.211  34.568  -0.406  1.00 71.29  ? 121  ILE   B CG1 1 
ATOM   3547  C  CG2 . ILE   B 2 121 ? 27.007  33.953  1.906   1.00 70.69  ? 121  ILE   B CG2 1 
ATOM   3548  C  CD1 . ILE   B 2 121 ? 24.897  33.936  0.048   1.00 72.12  ? 121  ILE   B CD1 1 
ATOM   3549  N  N   . GLY   B 2 122 ? 29.687  35.575  2.499   1.00 76.86  ? 122  GLY   B N   1 
ATOM   3550  C  CA  . GLY   B 2 122 ? 30.790  35.290  3.386   1.00 77.40  ? 122  GLY   B CA  1 
ATOM   3551  C  C   . GLY   B 2 122 ? 30.257  35.116  4.780   1.00 79.04  ? 122  GLY   B C   1 
ATOM   3552  O  O   . GLY   B 2 122 ? 29.723  36.080  5.342   1.00 81.77  ? 122  GLY   B O   1 
ATOM   3553  N  N   . ILE   B 2 123 ? 30.364  33.897  5.328   1.00 79.54  ? 123  ILE   B N   1 
ATOM   3554  C  CA  . ILE   B 2 123 ? 29.855  33.572  6.655   1.00 78.74  ? 123  ILE   B CA  1 
ATOM   3555  C  C   . ILE   B 2 123 ? 30.995  33.144  7.574   1.00 80.19  ? 123  ILE   B C   1 
ATOM   3556  O  O   . ILE   B 2 123 ? 32.077  32.741  7.141   1.00 80.38  ? 123  ILE   B O   1 
ATOM   3557  C  CB  . ILE   B 2 123 ? 28.767  32.482  6.613   1.00 77.65  ? 123  ILE   B CB  1 
ATOM   3558  C  CG1 . ILE   B 2 123 ? 29.188  31.324  5.709   1.00 85.10  ? 123  ILE   B CG1 1 
ATOM   3559  C  CG2 . ILE   B 2 123 ? 27.487  33.027  6.086   1.00 76.54  ? 123  ILE   B CG2 1 
ATOM   3560  C  CD1 . ILE   B 2 123 ? 28.027  30.358  5.421   1.00 80.76  ? 123  ILE   B CD1 1 
ATOM   3561  N  N   . ILE   B 2 124 ? 30.730  33.222  8.869   1.00 79.81  ? 124  ILE   B N   1 
ATOM   3562  C  CA  . ILE   B 2 124 ? 31.665  32.756  9.876   1.00 81.30  ? 124  ILE   B CA  1 
ATOM   3563  C  C   . ILE   B 2 124 ? 30.925  31.835  10.833  1.00 90.76  ? 124  ILE   B C   1 
ATOM   3564  O  O   . ILE   B 2 124 ? 29.853  32.186  11.338  1.00 89.46  ? 124  ILE   B O   1 
ATOM   3565  C  CB  . ILE   B 2 124 ? 32.325  33.921  10.620  1.00 82.17  ? 124  ILE   B CB  1 
ATOM   3566  C  CG1 . ILE   B 2 124 ? 33.543  34.389  9.831   1.00 86.57  ? 124  ILE   B CG1 1 
ATOM   3567  C  CG2 . ILE   B 2 124 ? 32.743  33.486  12.016  1.00 89.62  ? 124  ILE   B CG2 1 
ATOM   3568  C  CD1 . ILE   B 2 124 ? 33.832  35.853  9.937   1.00 81.53  ? 124  ILE   B CD1 1 
ATOM   3569  N  N   . ASP   B 2 125 ? 31.493  30.646  11.048  1.00 94.07  ? 125  ASP   B N   1 
ATOM   3570  C  CA  . ASP   B 2 125 ? 30.946  29.648  11.959  1.00 94.36  ? 125  ASP   B CA  1 
ATOM   3571  C  C   . ASP   B 2 125 ? 30.721  30.240  13.357  1.00 95.42  ? 125  ASP   B C   1 
ATOM   3572  O  O   . ASP   B 2 125 ? 31.546  31.031  13.847  1.00 92.63  ? 125  ASP   B O   1 
ATOM   3573  C  CB  . ASP   B 2 125 ? 31.904  28.449  12.024  1.00 95.93  ? 125  ASP   B CB  1 
ATOM   3574  C  CG  . ASP   B 2 125 ? 31.602  27.509  13.178  1.00 100.55 ? 125  ASP   B CG  1 
ATOM   3575  O  OD1 . ASP   B 2 125 ? 32.067  27.803  14.300  1.00 103.37 ? 125  ASP   B OD1 1 
ATOM   3576  O  OD2 . ASP   B 2 125 ? 30.904  26.483  12.971  1.00 103.05 ? 125  ASP   B OD2 1 
ATOM   3577  N  N   . PRO   B 2 126 ? 29.630  29.865  14.033  1.00 92.09  ? 126  PRO   B N   1 
ATOM   3578  C  CA  . PRO   B 2 126 ? 29.321  30.454  15.347  1.00 94.52  ? 126  PRO   B CA  1 
ATOM   3579  C  C   . PRO   B 2 126 ? 30.414  30.261  16.364  1.00 103.53 ? 126  PRO   B C   1 
ATOM   3580  O  O   . PRO   B 2 126 ? 30.602  31.109  17.252  1.00 103.92 ? 126  PRO   B O   1 
ATOM   3581  C  CB  . PRO   B 2 126 ? 28.046  29.715  15.766  1.00 92.06  ? 126  PRO   B CB  1 
ATOM   3582  C  CG  . PRO   B 2 126 ? 27.410  29.329  14.492  1.00 97.65  ? 126  PRO   B CG  1 
ATOM   3583  C  CD  . PRO   B 2 126 ? 28.546  29.005  13.548  1.00 97.75  ? 126  PRO   B CD  1 
ATOM   3584  N  N   . GLU   B 2 127 ? 31.121  29.140  16.284  1.00 107.13 ? 127  GLU   B N   1 
ATOM   3585  C  CA  . GLU   B 2 127 ? 32.274  28.882  17.141  1.00 110.01 ? 127  GLU   B CA  1 
ATOM   3586  C  C   . GLU   B 2 127 ? 33.588  29.368  16.555  1.00 109.87 ? 127  GLU   B C   1 
ATOM   3587  O  O   . GLU   B 2 127 ? 34.663  28.915  16.956  1.00 110.75 ? 127  GLU   B O   1 
ATOM   3588  C  CB  . GLU   B 2 127 ? 32.290  27.417  17.555  1.00 111.73 ? 127  GLU   B CB  1 
ATOM   3589  C  CG  . GLU   B 2 127 ? 30.901  26.868  17.833  1.00 113.84 ? 127  GLU   B CG  1 
ATOM   3590  C  CD  . GLU   B 2 127 ? 30.918  25.486  18.481  1.00 132.80 ? 127  GLU   B CD  1 
ATOM   3591  O  OE1 . GLU   B 2 127 ? 32.001  24.843  18.505  1.00 135.80 ? 127  GLU   B OE1 1 
ATOM   3592  O  OE2 . GLU   B 2 127 ? 29.848  25.039  18.963  1.00 137.68 ? 127  GLU   B OE2 1 
ATOM   3593  N  N   . CYS   B 2 128 ? 33.509  30.289  15.589  1.00 106.46 ? 128  CYS   B N   1 
ATOM   3594  C  CA  . CYS   B 2 128 ? 34.645  30.847  14.860  1.00 104.52 ? 128  CYS   B CA  1 
ATOM   3595  C  C   . CYS   B 2 128 ? 35.625  29.767  14.423  1.00 104.60 ? 128  CYS   B C   1 
ATOM   3596  O  O   . CYS   B 2 128 ? 36.838  29.988  14.457  1.00 107.76 ? 128  CYS   B O   1 
ATOM   3597  C  CB  . CYS   B 2 128 ? 35.400  31.923  15.648  1.00 99.32  ? 128  CYS   B CB  1 
ATOM   3598  S  SG  . CYS   B 2 128 ? 34.394  33.395  15.944  1.00 106.31 ? 128  CYS   B SG  1 
ATOM   3599  N  N   . ARG   B 2 129 ? 35.125  28.604  14.003  1.00 110.24 ? 129  ARG   B N   1 
ATOM   3600  C  CA  . ARG   B 2 129 ? 36.043  27.554  13.571  1.00 113.21 ? 129  ARG   B CA  1 
ATOM   3601  C  C   . ARG   B 2 129 ? 36.536  27.808  12.151  1.00 113.86 ? 129  ARG   B C   1 
ATOM   3602  O  O   . ARG   B 2 129 ? 37.679  27.469  11.816  1.00 114.45 ? 129  ARG   B O   1 
ATOM   3603  C  CB  . ARG   B 2 129 ? 35.369  26.179  13.667  1.00 113.71 ? 129  ARG   B CB  1 
ATOM   3604  C  CG  . ARG   B 2 129 ? 35.097  25.747  15.107  1.00 116.82 ? 129  ARG   B CG  1 
ATOM   3605  C  CD  . ARG   B 2 129 ? 36.180  24.821  15.663  1.00 123.48 ? 129  ARG   B CD  1 
ATOM   3606  N  NE  . ARG   B 2 129 ? 36.029  23.472  15.126  1.00 130.12 ? 129  ARG   B NE  1 
ATOM   3607  C  CZ  . ARG   B 2 129 ? 36.913  22.863  14.344  1.00 129.58 ? 129  ARG   B CZ  1 
ATOM   3608  N  NH1 . ARG   B 2 129 ? 38.096  23.401  14.078  1.00 128.26 ? 129  ARG   B NH1 1 
ATOM   3609  N  NH2 . ARG   B 2 129 ? 36.597  21.690  13.805  1.00 124.80 ? 129  ARG   B NH2 1 
ATOM   3610  N  N   . MET   B 2 130 ? 35.712  28.434  11.321  1.00 106.65 ? 130  MET   B N   1 
ATOM   3611  C  CA  . MET   B 2 130 ? 36.065  28.608  9.928   1.00 100.08 ? 130  MET   B CA  1 
ATOM   3612  C  C   . MET   B 2 130 ? 35.325  29.822  9.389   1.00 96.27  ? 130  MET   B C   1 
ATOM   3613  O  O   . MET   B 2 130 ? 34.320  30.268  9.948   1.00 93.01  ? 130  MET   B O   1 
ATOM   3614  C  CB  . MET   B 2 130 ? 35.707  27.361  9.129   1.00 93.33  ? 130  MET   B CB  1 
ATOM   3615  C  CG  . MET   B 2 130 ? 34.234  27.072  9.231   1.00 90.94  ? 130  MET   B CG  1 
ATOM   3616  S  SD  . MET   B 2 130 ? 33.828  25.419  8.689   1.00 104.27 ? 130  MET   B SD  1 
ATOM   3617  C  CE  . MET   B 2 130 ? 34.609  25.403  7.078   1.00 96.76  ? 130  MET   B CE  1 
ATOM   3618  N  N   . ILE   B 2 131 ? 35.845  30.349  8.294   1.00 93.46  ? 131  ILE   B N   1 
ATOM   3619  C  CA  . ILE   B 2 131 ? 35.143  31.316  7.476   1.00 86.05  ? 131  ILE   B CA  1 
ATOM   3620  C  C   . ILE   B 2 131 ? 34.658  30.587  6.230   1.00 87.98  ? 131  ILE   B C   1 
ATOM   3621  O  O   . ILE   B 2 131 ? 35.432  29.870  5.581   1.00 86.15  ? 131  ILE   B O   1 
ATOM   3622  C  CB  . ILE   B 2 131 ? 36.060  32.496  7.119   1.00 88.56  ? 131  ILE   B CB  1 
ATOM   3623  C  CG1 . ILE   B 2 131 ? 36.608  33.129  8.389   1.00 88.90  ? 131  ILE   B CG1 1 
ATOM   3624  C  CG2 . ILE   B 2 131 ? 35.322  33.538  6.323   1.00 84.86  ? 131  ILE   B CG2 1 
ATOM   3625  C  CD1 . ILE   B 2 131 ? 37.546  34.250  8.128   1.00 87.20  ? 131  ILE   B CD1 1 
ATOM   3626  N  N   . GLY   B 2 132 ? 33.376  30.736  5.913   1.00 86.04  ? 132  GLY   B N   1 
ATOM   3627  C  CA  . GLY   B 2 132 ? 32.807  30.184  4.692   1.00 79.03  ? 132  GLY   B CA  1 
ATOM   3628  C  C   . GLY   B 2 132 ? 32.652  31.247  3.616   1.00 79.47  ? 132  GLY   B C   1 
ATOM   3629  O  O   . GLY   B 2 132 ? 32.193  32.360  3.883   1.00 79.14  ? 132  GLY   B O   1 
ATOM   3630  N  N   . LEU   B 2 133 ? 33.056  30.899  2.394   1.00 81.23  ? 133  LEU   B N   1 
ATOM   3631  C  CA  . LEU   B 2 133 ? 32.931  31.794  1.251   1.00 76.91  ? 133  LEU   B CA  1 
ATOM   3632  C  C   . LEU   B 2 133 ? 32.226  31.051  0.130   1.00 78.94  ? 133  LEU   B C   1 
ATOM   3633  O  O   . LEU   B 2 133 ? 32.609  29.931  -0.210  1.00 84.82  ? 133  LEU   B O   1 
ATOM   3634  C  CB  . LEU   B 2 133 ? 34.297  32.306  0.795   1.00 72.49  ? 133  LEU   B CB  1 
ATOM   3635  C  CG  . LEU   B 2 133 ? 34.935  33.280  1.787   1.00 74.97  ? 133  LEU   B CG  1 
ATOM   3636  C  CD1 . LEU   B 2 133 ? 36.208  33.864  1.213   1.00 73.74  ? 133  LEU   B CD1 1 
ATOM   3637  C  CD2 . LEU   B 2 133 ? 33.947  34.379  2.144   1.00 75.71  ? 133  LEU   B CD2 1 
ATOM   3638  N  N   . ARG   B 2 134 ? 31.170  31.643  -0.406  1.00 77.35  ? 134  ARG   B N   1 
ATOM   3639  C  CA  . ARG   B 2 134 ? 30.459  31.092  -1.557  1.00 81.53  ? 134  ARG   B CA  1 
ATOM   3640  C  C   . ARG   B 2 134 ? 30.650  32.098  -2.687  1.00 86.10  ? 134  ARG   B C   1 
ATOM   3641  O  O   . ARG   B 2 134 ? 29.846  33.022  -2.872  1.00 80.65  ? 134  ARG   B O   1 
ATOM   3642  C  CB  . ARG   B 2 134 ? 28.985  30.844  -1.277  1.00 74.09  ? 134  ARG   B CB  1 
ATOM   3643  C  CG  . ARG   B 2 134 ? 28.308  29.974  -2.327  1.00 76.58  ? 134  ARG   B CG  1 
ATOM   3644  C  CD  . ARG   B 2 134 ? 28.234  30.641  -3.682  1.00 80.10  ? 134  ARG   B CD  1 
ATOM   3645  N  NE  . ARG   B 2 134 ? 27.499  31.901  -3.607  1.00 86.74  ? 134  ARG   B NE  1 
ATOM   3646  C  CZ  . ARG   B 2 134 ? 26.218  32.051  -3.924  1.00 84.62  ? 134  ARG   B CZ  1 
ATOM   3647  N  NH1 . ARG   B 2 134 ? 25.498  31.040  -4.389  1.00 84.18  ? 134  ARG   B NH1 1 
ATOM   3648  N  NH2 . ARG   B 2 134 ? 25.646  33.246  -3.770  1.00 77.53  ? 134  ARG   B NH2 1 
ATOM   3649  N  N   . LEU   B 2 135 ? 31.725  31.912  -3.441  1.00 87.97  ? 135  LEU   B N   1 
ATOM   3650  C  CA  . LEU   B 2 135 ? 32.066  32.810  -4.529  1.00 84.47  ? 135  LEU   B CA  1 
ATOM   3651  C  C   . LEU   B 2 135 ? 31.631  32.263  -5.871  1.00 84.98  ? 135  LEU   B C   1 
ATOM   3652  O  O   . LEU   B 2 135 ? 31.112  32.996  -6.715  1.00 84.64  ? 135  LEU   B O   1 
ATOM   3653  C  CB  . LEU   B 2 135 ? 33.573  33.055  -4.535  1.00 84.98  ? 135  LEU   B CB  1 
ATOM   3654  C  CG  . LEU   B 2 135 ? 34.173  33.353  -3.159  1.00 85.48  ? 135  LEU   B CG  1 
ATOM   3655  C  CD1 . LEU   B 2 135 ? 35.702  33.159  -3.183  1.00 85.90  ? 135  LEU   B CD1 1 
ATOM   3656  C  CD2 . LEU   B 2 135 ? 33.810  34.790  -2.736  1.00 86.65  ? 135  LEU   B CD2 1 
ATOM   3657  N  N   . TYR   B 2 136 ? 31.787  30.975  -6.079  1.00 88.77  ? 136  TYR   B N   1 
ATOM   3658  C  CA  . TYR   B 2 136 ? 31.537  30.419  -7.390  1.00 89.79  ? 136  TYR   B CA  1 
ATOM   3659  C  C   . TYR   B 2 136 ? 30.501  29.304  -7.300  1.00 88.39  ? 136  TYR   B C   1 
ATOM   3660  O  O   . TYR   B 2 136 ? 30.458  28.558  -6.316  1.00 89.73  ? 136  TYR   B O   1 
ATOM   3661  C  CB  . TYR   B 2 136 ? 32.844  29.929  -7.980  1.00 90.63  ? 136  TYR   B CB  1 
ATOM   3662  C  CG  . TYR   B 2 136 ? 33.949  30.965  -7.997  1.00 92.28  ? 136  TYR   B CG  1 
ATOM   3663  C  CD1 . TYR   B 2 136 ? 33.836  32.109  -8.776  1.00 91.39  ? 136  TYR   B CD1 1 
ATOM   3664  C  CD2 . TYR   B 2 136 ? 35.125  30.783  -7.255  1.00 91.59  ? 136  TYR   B CD2 1 
ATOM   3665  C  CE1 . TYR   B 2 136 ? 34.861  33.045  -8.817  1.00 90.42  ? 136  TYR   B CE1 1 
ATOM   3666  C  CE2 . TYR   B 2 136 ? 36.147  31.717  -7.291  1.00 87.93  ? 136  TYR   B CE2 1 
ATOM   3667  C  CZ  . TYR   B 2 136 ? 36.009  32.839  -8.077  1.00 89.17  ? 136  TYR   B CZ  1 
ATOM   3668  O  OH  . TYR   B 2 136 ? 37.013  33.781  -8.134  1.00 94.99  ? 136  TYR   B OH  1 
ATOM   3669  N  N   . ASP   B 2 137 ? 29.634  29.234  -8.310  1.00 88.18  ? 137  ASP   B N   1 
ATOM   3670  C  CA  . ASP   B 2 137 ? 28.687  28.136  -8.416  1.00 90.55  ? 137  ASP   B CA  1 
ATOM   3671  C  C   . ASP   B 2 137 ? 29.437  26.816  -8.339  1.00 88.28  ? 137  ASP   B C   1 
ATOM   3672  O  O   . ASP   B 2 137 ? 30.435  26.622  -9.036  1.00 84.79  ? 137  ASP   B O   1 
ATOM   3673  C  CB  . ASP   B 2 137 ? 27.898  28.224  -9.730  1.00 89.19  ? 137  ASP   B CB  1 
ATOM   3674  C  CG  . ASP   B 2 137 ? 26.805  29.303  -9.706  1.00 97.74  ? 137  ASP   B CG  1 
ATOM   3675  O  OD1 . ASP   B 2 137 ? 26.447  29.809  -8.611  1.00 97.85  ? 137  ASP   B OD1 1 
ATOM   3676  O  OD2 . ASP   B 2 137 ? 26.288  29.637  -10.797 1.00 102.86 ? 137  ASP   B OD2 1 
ATOM   3677  N  N   . GLY   B 2 138 ? 28.975  25.926  -7.455  1.00 91.84  ? 138  GLY   B N   1 
ATOM   3678  C  CA  . GLY   B 2 138 ? 29.518  24.584  -7.343  1.00 91.15  ? 138  GLY   B CA  1 
ATOM   3679  C  C   . GLY   B 2 138 ? 30.649  24.389  -6.348  1.00 90.74  ? 138  GLY   B C   1 
ATOM   3680  O  O   . GLY   B 2 138 ? 31.052  23.242  -6.107  1.00 94.37  ? 138  GLY   B O   1 
ATOM   3681  N  N   . LEU   B 2 139 ? 31.182  25.454  -5.764  1.00 92.80  ? 139  LEU   B N   1 
ATOM   3682  C  CA  . LEU   B 2 139 ? 32.298  25.344  -4.835  1.00 91.24  ? 139  LEU   B CA  1 
ATOM   3683  C  C   . LEU   B 2 139 ? 31.973  26.075  -3.535  1.00 91.44  ? 139  LEU   B C   1 
ATOM   3684  O  O   . LEU   B 2 139 ? 30.974  26.802  -3.437  1.00 90.42  ? 139  LEU   B O   1 
ATOM   3685  C  CB  . LEU   B 2 139 ? 33.580  25.897  -5.463  1.00 90.71  ? 139  LEU   B CB  1 
ATOM   3686  C  CG  . LEU   B 2 139 ? 34.249  24.970  -6.458  1.00 87.97  ? 139  LEU   B CG  1 
ATOM   3687  C  CD1 . LEU   B 2 139 ? 35.345  25.736  -7.175  1.00 85.22  ? 139  LEU   B CD1 1 
ATOM   3688  C  CD2 . LEU   B 2 139 ? 34.793  23.742  -5.716  1.00 89.96  ? 139  LEU   B CD2 1 
ATOM   3689  N  N   . PHE   B 2 140 ? 32.835  25.868  -2.529  1.00 83.78  ? 140  PHE   B N   1 
ATOM   3690  C  CA  . PHE   B 2 140 ? 32.679  26.498  -1.220  1.00 77.47  ? 140  PHE   B CA  1 
ATOM   3691  C  C   . PHE   B 2 140 ? 34.060  26.593  -0.595  1.00 85.42  ? 140  PHE   B C   1 
ATOM   3692  O  O   . PHE   B 2 140 ? 34.624  25.562  -0.209  1.00 89.80  ? 140  PHE   B O   1 
ATOM   3693  C  CB  . PHE   B 2 140 ? 31.736  25.690  -0.336  1.00 84.63  ? 140  PHE   B CB  1 
ATOM   3694  C  CG  . PHE   B 2 140 ? 31.381  26.361  0.968   1.00 89.17  ? 140  PHE   B CG  1 
ATOM   3695  C  CD1 . PHE   B 2 140 ? 30.547  27.478  0.984   1.00 85.73  ? 140  PHE   B CD1 1 
ATOM   3696  C  CD2 . PHE   B 2 140 ? 31.856  25.863  2.184   1.00 88.46  ? 140  PHE   B CD2 1 
ATOM   3697  C  CE1 . PHE   B 2 140 ? 30.202  28.096  2.188   1.00 80.45  ? 140  PHE   B CE1 1 
ATOM   3698  C  CE2 . PHE   B 2 140 ? 31.513  26.483  3.381   1.00 84.54  ? 140  PHE   B CE2 1 
ATOM   3699  C  CZ  . PHE   B 2 140 ? 30.683  27.603  3.377   1.00 79.92  ? 140  PHE   B CZ  1 
ATOM   3700  N  N   . LYS   B 2 141 ? 34.609  27.809  -0.496  1.00 86.84  ? 141  LYS   B N   1 
ATOM   3701  C  CA  . LYS   B 2 141 ? 35.934  27.975  0.092   1.00 83.84  ? 141  LYS   B CA  1 
ATOM   3702  C  C   . LYS   B 2 141 ? 35.835  27.966  1.609   1.00 83.20  ? 141  LYS   B C   1 
ATOM   3703  O  O   . LYS   B 2 141 ? 34.825  28.380  2.191   1.00 79.77  ? 141  LYS   B O   1 
ATOM   3704  C  CB  . LYS   B 2 141 ? 36.622  29.255  -0.384  1.00 78.07  ? 141  LYS   B CB  1 
ATOM   3705  C  CG  . LYS   B 2 141 ? 37.604  29.038  -1.537  1.00 80.84  ? 141  LYS   B CG  1 
ATOM   3706  C  CD  . LYS   B 2 141 ? 38.617  30.161  -1.568  1.00 84.71  ? 141  LYS   B CD  1 
ATOM   3707  C  CE  . LYS   B 2 141 ? 39.527  30.070  -2.783  1.00 86.97  ? 141  LYS   B CE  1 
ATOM   3708  N  NZ  . LYS   B 2 141 ? 40.985  30.165  -2.397  1.00 86.07  ? 141  LYS   B NZ  1 
ATOM   3709  N  N   . VAL   B 2 142 ? 36.888  27.464  2.243   1.00 85.01  ? 142  VAL   B N   1 
ATOM   3710  C  CA  . VAL   B 2 142 ? 36.910  27.231  3.673   1.00 86.30  ? 142  VAL   B CA  1 
ATOM   3711  C  C   . VAL   B 2 142 ? 38.249  27.754  4.170   1.00 90.97  ? 142  VAL   B C   1 
ATOM   3712  O  O   . VAL   B 2 142 ? 39.299  27.157  3.906   1.00 90.93  ? 142  VAL   B O   1 
ATOM   3713  C  CB  . VAL   B 2 142 ? 36.718  25.757  4.027   1.00 85.06  ? 142  VAL   B CB  1 
ATOM   3714  C  CG1 . VAL   B 2 142 ? 37.194  25.498  5.448   1.00 90.58  ? 142  VAL   B CG1 1 
ATOM   3715  C  CG2 . VAL   B 2 142 ? 35.260  25.383  3.861   1.00 83.31  ? 142  VAL   B CG2 1 
ATOM   3716  N  N   . ILE   B 2 143 ? 38.217  28.887  4.863   1.00 90.75  ? 143  ILE   B N   1 
ATOM   3717  C  CA  . ILE   B 2 143 ? 39.391  29.447  5.512   1.00 90.01  ? 143  ILE   B CA  1 
ATOM   3718  C  C   . ILE   B 2 143 ? 39.398  28.931  6.937   1.00 94.07  ? 143  ILE   B C   1 
ATOM   3719  O  O   . ILE   B 2 143 ? 38.626  29.424  7.772   1.00 96.10  ? 143  ILE   B O   1 
ATOM   3720  C  CB  . ILE   B 2 143 ? 39.360  30.973  5.516   1.00 93.83  ? 143  ILE   B CB  1 
ATOM   3721  C  CG1 . ILE   B 2 143 ? 39.419  31.535  4.102   1.00 92.76  ? 143  ILE   B CG1 1 
ATOM   3722  C  CG2 . ILE   B 2 143 ? 40.498  31.510  6.351   1.00 94.49  ? 143  ILE   B CG2 1 
ATOM   3723  C  CD1 . ILE   B 2 143 ? 39.410  33.024  4.121   1.00 93.47  ? 143  ILE   B CD1 1 
ATOM   3724  N  N   . PRO   B 2 144 ? 40.220  27.912  7.292   1.00 96.84  ? 144  PRO   B N   1 
ATOM   3725  C  CA  . PRO   B 2 144 ? 40.280  27.464  8.668   1.00 98.30  ? 144  PRO   B CA  1 
ATOM   3726  C  C   . PRO   B 2 144 ? 40.717  28.602  9.554   1.00 100.30 ? 144  PRO   B C   1 
ATOM   3727  O  O   . PRO   B 2 144 ? 41.724  29.263  9.250   1.00 98.53  ? 144  PRO   B O   1 
ATOM   3728  C  CB  . PRO   B 2 144 ? 41.318  26.353  8.606   1.00 103.70 ? 144  PRO   B CB  1 
ATOM   3729  C  CG  . PRO   B 2 144 ? 41.172  25.805  7.216   1.00 103.51 ? 144  PRO   B CG  1 
ATOM   3730  C  CD  . PRO   B 2 144 ? 41.109  27.096  6.441   1.00 98.00  ? 144  PRO   B CD  1 
ATOM   3731  N  N   . LEU   B 2 145 ? 40.026  28.774  10.680  1.00 104.08 ? 145  LEU   B N   1 
ATOM   3732  C  CA  . LEU   B 2 145 ? 40.420  29.809  11.665  1.00 105.93 ? 145  LEU   B CA  1 
ATOM   3733  C  C   . LEU   B 2 145 ? 41.062  29.108  12.864  1.00 109.99 ? 145  LEU   B C   1 
ATOM   3734  O  O   . LEU   B 2 145 ? 41.585  29.813  13.747  1.00 114.70 ? 145  LEU   B O   1 
ATOM   3735  C  CB  . LEU   B 2 145 ? 39.169  30.563  12.097  1.00 106.58 ? 145  LEU   B CB  1 
ATOM   3736  C  CG  . LEU   B 2 145 ? 38.551  31.501  11.061  1.00 101.49 ? 145  LEU   B CG  1 
ATOM   3737  C  CD1 . LEU   B 2 145 ? 37.341  32.160  11.696  1.00 100.73 ? 145  LEU   B CD1 1 
ATOM   3738  C  CD2 . LEU   B 2 145 ? 39.589  32.533  10.671  1.00 93.66  ? 145  LEU   B CD2 1 
ATOM   3739  N  N   . ASP   B 2 146 ? 40.987  27.777  12.904  1.00 114.01 ? 146  ASP   B N   1 
ATOM   3740  C  CA  . ASP   B 2 146 ? 41.498  27.003  14.070  1.00 112.14 ? 146  ASP   B CA  1 
ATOM   3741  C  C   . ASP   B 2 146 ? 42.883  27.499  14.484  1.00 112.91 ? 146  ASP   B C   1 
ATOM   3742  O  O   . ASP   B 2 146 ? 43.248  27.295  15.656  1.00 113.75 ? 146  ASP   B O   1 
ATOM   3743  C  CB  . ASP   B 2 146 ? 41.530  25.516  13.769  1.00 113.09 ? 146  ASP   B CB  1 
ATOM   3744  C  CG  . ASP   B 2 146 ? 41.949  24.638  14.940  1.00 120.33 ? 146  ASP   B CG  1 
ATOM   3745  O  OD1 . ASP   B 2 146 ? 42.207  25.194  16.028  1.00 116.56 ? 146  ASP   B OD1 1 
ATOM   3746  O  OD2 . ASP   B 2 146 ? 42.032  23.406  14.747  1.00 124.68 ? 146  ASP   B OD2 1 
ATOM   3747  N  N   . ARG   B 2 147 ? 43.629  28.098  13.558  1.00 115.20 ? 147  ARG   B N   1 
ATOM   3748  C  CA  . ARG   B 2 147 ? 45.009  28.537  13.882  1.00 115.54 ? 147  ARG   B CA  1 
ATOM   3749  C  C   . ARG   B 2 147 ? 45.307  29.858  13.164  1.00 114.58 ? 147  ARG   B C   1 
ATOM   3750  O  O   . ARG   B 2 147 ? 44.413  30.365  12.461  1.00 113.94 ? 147  ARG   B O   1 
ATOM   3751  C  CB  . ARG   B 2 147 ? 46.006  27.445  13.494  1.00 115.95 ? 147  ARG   B CB  1 
ATOM   3752  N  N   . ASP   B 2 148 ? 46.515  30.389  13.341  1.00 126.76 ? 148  ASP   B N   1 
ATOM   3753  C  CA  . ASP   B 2 148 ? 46.847  31.708  12.744  1.00 121.88 ? 148  ASP   B CA  1 
ATOM   3754  C  C   . ASP   B 2 148 ? 46.907  31.489  11.231  1.00 121.75 ? 148  ASP   B C   1 
ATOM   3755  O  O   . ASP   B 2 148 ? 47.992  31.141  10.733  1.00 124.50 ? 148  ASP   B O   1 
ATOM   3756  C  CB  . ASP   B 2 148 ? 48.123  32.265  13.344  1.00 124.11 ? 148  ASP   B CB  1 
ATOM   3757  C  CG  . ASP   B 2 148 ? 47.992  32.728  14.786  1.00 128.91 ? 148  ASP   B CG  1 
ATOM   3758  O  OD1 . ASP   B 2 148 ? 46.842  32.885  15.243  1.00 132.49 ? 148  ASP   B OD1 1 
ATOM   3759  O  OD2 . ASP   B 2 148 ? 49.039  32.936  15.433  1.00 135.21 ? 148  ASP   B OD2 1 
ATOM   3760  N  N   . ASN   B 2 149 ? 45.793  31.707  10.529  1.00 106.74 ? 149  ASN   B N   1 
ATOM   3761  C  CA  . ASN   B 2 149 ? 45.801  31.577  9.047   1.00 101.44 ? 149  ASN   B CA  1 
ATOM   3762  C  C   . ASN   B 2 149 ? 46.216  32.951  8.522   1.00 101.89 ? 149  ASN   B C   1 
ATOM   3763  O  O   . ASN   B 2 149 ? 45.466  33.528  7.721   1.00 99.69  ? 149  ASN   B O   1 
ATOM   3764  C  CB  . ASN   B 2 149 ? 44.464  31.119  8.489   1.00 94.50  ? 149  ASN   B CB  1 
ATOM   3765  C  CG  . ASN   B 2 149 ? 44.646  30.239  7.282   1.00 92.10  ? 149  ASN   B CG  1 
ATOM   3766  O  OD1 . ASN   B 2 149 ? 45.712  30.268  6.659   1.00 91.20  ? 149  ASN   B OD1 1 
ATOM   3767  N  ND2 . ASN   B 2 149 ? 43.631  29.461  6.942   1.00 95.12  ? 149  ASN   B ND2 1 
ATOM   3768  N  N   . LYS   B 2 150 ? 47.374  33.441  8.952   1.00 99.38  ? 150  LYS   B N   1 
ATOM   3769  C  CA  . LYS   B 2 150 ? 47.845  34.812  8.556   1.00 95.92  ? 150  LYS   B CA  1 
ATOM   3770  C  C   . LYS   B 2 150 ? 47.645  34.896  7.053   1.00 99.87  ? 150  LYS   B C   1 
ATOM   3771  O  O   . LYS   B 2 150 ? 47.208  35.951  6.571   1.00 107.32 ? 150  LYS   B O   1 
ATOM   3772  C  CB  . LYS   B 2 150 ? 49.267  34.986  9.030   1.00 95.03  ? 150  LYS   B CB  1 
ATOM   3773  N  N   . GLU   B 2 151 ? 47.970  33.858  6.277   1.00 94.95  ? 151  GLU   B N   1 
ATOM   3774  C  CA  . GLU   B 2 151 ? 47.802  33.946  4.827   1.00 96.69  ? 151  GLU   B CA  1 
ATOM   3775  C  C   . GLU   B 2 151 ? 46.450  33.509  4.282   1.00 97.55  ? 151  GLU   B C   1 
ATOM   3776  O  O   . GLU   B 2 151 ? 46.279  33.452  3.054   1.00 96.40  ? 151  GLU   B O   1 
ATOM   3777  C  CB  . GLU   B 2 151 ? 48.899  33.133  4.138   1.00 101.45 ? 151  GLU   B CB  1 
ATOM   3778  C  CG  . GLU   B 2 151 ? 50.272  33.528  4.562   1.00 108.46 ? 151  GLU   B CG  1 
ATOM   3779  C  CD  . GLU   B 2 151 ? 51.330  33.399  3.465   1.00 126.56 ? 151  GLU   B CD  1 
ATOM   3780  O  OE1 . GLU   B 2 151 ? 51.195  32.547  2.541   1.00 131.52 ? 151  GLU   B OE1 1 
ATOM   3781  O  OE2 . GLU   B 2 151 ? 52.325  34.160  3.555   1.00 130.60 ? 151  GLU   B OE2 1 
ATOM   3782  N  N   . LEU   B 2 152 ? 45.498  33.187  5.165   1.00 95.60  ? 152  LEU   B N   1 
ATOM   3783  C  CA  . LEU   B 2 152 ? 44.152  32.786  4.762   1.00 92.47  ? 152  LEU   B CA  1 
ATOM   3784  C  C   . LEU   B 2 152 ? 44.192  31.580  3.817   1.00 91.32  ? 152  LEU   B C   1 
ATOM   3785  O  O   . LEU   B 2 152 ? 43.432  31.487  2.847   1.00 89.16  ? 152  LEU   B O   1 
ATOM   3786  C  CB  . LEU   B 2 152 ? 43.394  33.968  4.145   1.00 93.51  ? 152  LEU   B CB  1 
ATOM   3787  C  CG  . LEU   B 2 152 ? 43.208  35.234  4.998   1.00 97.54  ? 152  LEU   B CG  1 
ATOM   3788  C  CD1 . LEU   B 2 152 ? 42.586  36.335  4.157   1.00 93.78  ? 152  LEU   B CD1 1 
ATOM   3789  C  CD2 . LEU   B 2 152 ? 42.356  34.966  6.229   1.00 95.40  ? 152  LEU   B CD2 1 
ATOM   3790  N  N   . LYS   B 2 153 ? 45.096  30.647  4.103   1.00 90.23  ? 153  LYS   B N   1 
ATOM   3791  C  CA  . LYS   B 2 153 ? 45.069  29.351  3.446   1.00 89.51  ? 153  LYS   B CA  1 
ATOM   3792  C  C   . LYS   B 2 153 ? 43.648  28.780  3.471   1.00 87.64  ? 153  LYS   B C   1 
ATOM   3793  O  O   . LYS   B 2 153 ? 43.011  28.727  4.525   1.00 91.00  ? 153  LYS   B O   1 
ATOM   3794  C  CB  . LYS   B 2 153 ? 46.068  28.423  4.151   1.00 80.25  ? 153  LYS   B CB  1 
ATOM   3795  N  N   . ALA   B 2 154 ? 43.125  28.393  2.303   1.00 84.52  ? 154  ALA   B N   1 
ATOM   3796  C  CA  . ALA   B 2 154 ? 41.741  27.911  2.208   1.00 89.49  ? 154  ALA   B CA  1 
ATOM   3797  C  C   . ALA   B 2 154 ? 41.658  26.588  1.450   1.00 90.65  ? 154  ALA   B C   1 
ATOM   3798  O  O   . ALA   B 2 154 ? 42.611  26.148  0.796   1.00 89.69  ? 154  ALA   B O   1 
ATOM   3799  C  CB  . ALA   B 2 154 ? 40.814  28.928  1.517   1.00 86.90  ? 154  ALA   B CB  1 
ATOM   3800  N  N   . PHE   B 2 155 ? 40.488  25.954  1.526   1.00 87.31  ? 155  PHE   B N   1 
ATOM   3801  C  CA  . PHE   B 2 155 ? 40.244  24.776  0.716   1.00 85.83  ? 155  PHE   B CA  1 
ATOM   3802  C  C   . PHE   B 2 155 ? 38.822  24.823  0.186   1.00 87.83  ? 155  PHE   B C   1 
ATOM   3803  O  O   . PHE   B 2 155 ? 37.929  25.403  0.817   1.00 87.55  ? 155  PHE   B O   1 
ATOM   3804  C  CB  . PHE   B 2 155 ? 40.544  23.462  1.476   1.00 86.06  ? 155  PHE   B CB  1 
ATOM   3805  C  CG  . PHE   B 2 155 ? 39.645  23.162  2.647   1.00 83.09  ? 155  PHE   B CG  1 
ATOM   3806  C  CD1 . PHE   B 2 155 ? 38.415  22.569  2.463   1.00 84.17  ? 155  PHE   B CD1 1 
ATOM   3807  C  CD2 . PHE   B 2 155 ? 40.084  23.373  3.939   1.00 91.77  ? 155  PHE   B CD2 1 
ATOM   3808  C  CE1 . PHE   B 2 155 ? 37.608  22.250  3.538   1.00 86.07  ? 155  PHE   B CE1 1 
ATOM   3809  C  CE2 . PHE   B 2 155 ? 39.286  23.053  5.025   1.00 94.55  ? 155  PHE   B CE2 1 
ATOM   3810  C  CZ  . PHE   B 2 155 ? 38.049  22.492  4.823   1.00 95.06  ? 155  PHE   B CZ  1 
ATOM   3811  N  N   . ASN   B 2 156 ? 38.630  24.216  -1.003  1.00 82.43  ? 156  ASN   B N   1 
ATOM   3812  C  CA  . ASN   B 2 156 ? 37.405  24.347  -1.787  1.00 80.72  ? 156  ASN   B CA  1 
ATOM   3813  C  C   . ASN   B 2 156 ? 36.614  23.051  -1.791  1.00 81.05  ? 156  ASN   B C   1 
ATOM   3814  O  O   . ASN   B 2 156 ? 36.855  22.197  -2.635  1.00 93.38  ? 156  ASN   B O   1 
ATOM   3815  C  CB  . ASN   B 2 156 ? 37.737  24.727  -3.221  1.00 86.33  ? 156  ASN   B CB  1 
ATOM   3816  C  CG  . ASN   B 2 156 ? 37.372  26.150  -3.548  1.00 89.29  ? 156  ASN   B CG  1 
ATOM   3817  O  OD1 . ASN   B 2 156 ? 36.411  26.705  -3.003  1.00 89.26  ? 156  ASN   B OD1 1 
ATOM   3818  N  ND2 . ASN   B 2 156 ? 38.139  26.758  -4.449  1.00 93.09  ? 156  ASN   B ND2 1 
ATOM   3819  N  N   . ILE   B 2 157 ? 35.625  22.927  -0.916  1.00 85.80  ? 157  ILE   B N   1 
ATOM   3820  C  CA  . ILE   B 2 157 ? 34.746  21.761  -0.929  1.00 85.68  ? 157  ILE   B CA  1 
ATOM   3821  C  C   . ILE   B 2 157 ? 33.798  21.859  -2.118  1.00 91.85  ? 157  ILE   B C   1 
ATOM   3822  O  O   . ILE   B 2 157 ? 33.144  22.891  -2.324  1.00 91.23  ? 157  ILE   B O   1 
ATOM   3823  C  CB  . ILE   B 2 157 ? 33.965  21.653  0.387   1.00 89.30  ? 157  ILE   B CB  1 
ATOM   3824  C  CG1 . ILE   B 2 157 ? 34.927  21.673  1.569   1.00 89.98  ? 157  ILE   B CG1 1 
ATOM   3825  C  CG2 . ILE   B 2 157 ? 33.131  20.379  0.425   1.00 91.56  ? 157  ILE   B CG2 1 
ATOM   3826  C  CD1 . ILE   B 2 157 ? 34.222  21.613  2.909   1.00 90.75  ? 157  ILE   B CD1 1 
ATOM   3827  N  N   . ARG   B 2 158 ? 33.734  20.789  -2.912  1.00 92.03  ? 158  ARG   B N   1 
ATOM   3828  C  CA  . ARG   B 2 158 ? 32.768  20.694  -3.993  1.00 90.26  ? 158  ARG   B CA  1 
ATOM   3829  C  C   . ARG   B 2 158 ? 31.357  20.671  -3.425  1.00 92.95  ? 158  ARG   B C   1 
ATOM   3830  O  O   . ARG   B 2 158 ? 31.122  20.210  -2.305  1.00 93.26  ? 158  ARG   B O   1 
ATOM   3831  C  CB  . ARG   B 2 158 ? 33.029  19.437  -4.814  1.00 101.32 ? 158  ARG   B CB  1 
ATOM   3832  C  CG  . ARG   B 2 158 ? 32.113  19.197  -6.023  1.00 110.53 ? 158  ARG   B CG  1 
ATOM   3833  C  CD  . ARG   B 2 158 ? 32.747  18.150  -6.977  1.00 115.00 ? 158  ARG   B CD  1 
ATOM   3834  N  NE  . ARG   B 2 158 ? 34.211  18.200  -6.910  1.00 123.21 ? 158  ARG   B NE  1 
ATOM   3835  C  CZ  . ARG   B 2 158 ? 34.943  19.303  -7.060  1.00 117.01 ? 158  ARG   B CZ  1 
ATOM   3836  N  NH1 . ARG   B 2 158 ? 34.383  20.472  -7.342  1.00 116.23 ? 158  ARG   B NH1 1 
ATOM   3837  N  NH2 . ARG   B 2 158 ? 36.263  19.240  -6.891  1.00 108.00 ? 158  ARG   B NH2 1 
ATOM   3838  N  N   . LEU   B 2 159 ? 30.411  21.183  -4.209  1.00 97.20  ? 159  LEU   B N   1 
ATOM   3839  C  CA  . LEU   B 2 159 ? 29.007  21.277  -3.801  1.00 97.83  ? 159  LEU   B CA  1 
ATOM   3840  C  C   . LEU   B 2 159 ? 28.148  21.017  -5.032  1.00 100.97 ? 159  LEU   B C   1 
ATOM   3841  O  O   . LEU   B 2 159 ? 28.326  21.681  -6.060  1.00 100.21 ? 159  LEU   B O   1 
ATOM   3842  C  CB  . LEU   B 2 159 ? 28.711  22.662  -3.197  1.00 96.32  ? 159  LEU   B CB  1 
ATOM   3843  C  CG  . LEU   B 2 159 ? 27.277  22.989  -2.770  1.00 96.93  ? 159  LEU   B CG  1 
ATOM   3844  C  CD1 . LEU   B 2 159 ? 26.873  22.112  -1.614  1.00 98.40  ? 159  LEU   B CD1 1 
ATOM   3845  C  CD2 . LEU   B 2 159 ? 27.131  24.436  -2.386  1.00 90.77  ? 159  LEU   B CD2 1 
ATOM   3846  N  N   . GLU   B 2 160 ? 27.218  20.061  -4.943  1.00 107.86 ? 160  GLU   B N   1 
ATOM   3847  C  CA  . GLU   B 2 160 ? 26.513  19.630  -6.151  1.00 107.96 ? 160  GLU   B CA  1 
ATOM   3848  C  C   . GLU   B 2 160 ? 25.387  20.569  -6.542  1.00 103.80 ? 160  GLU   B C   1 
ATOM   3849  O  O   . GLU   B 2 160 ? 25.072  20.697  -7.734  1.00 102.83 ? 160  GLU   B O   1 
ATOM   3850  C  CB  . GLU   B 2 160 ? 25.965  18.228  -5.953  1.00 109.88 ? 160  GLU   B CB  1 
ATOM   3851  C  CG  . GLU   B 2 160 ? 27.060  17.247  -5.695  1.00 116.46 ? 160  GLU   B CG  1 
ATOM   3852  C  CD  . GLU   B 2 160 ? 26.552  15.845  -5.710  1.00 134.02 ? 160  GLU   B CD  1 
ATOM   3853  O  OE1 . GLU   B 2 160 ? 25.526  15.575  -5.033  1.00 134.46 ? 160  GLU   B OE1 1 
ATOM   3854  O  OE2 . GLU   B 2 160 ? 27.170  15.021  -6.422  1.00 146.60 ? 160  GLU   B OE2 1 
ATOM   3855  N  N   . GLU   B 2 161 ? 24.763  21.203  -5.555  1.00 98.26  ? 161  GLU   B N   1 
ATOM   3856  C  CA  . GLU   B 2 161 ? 23.736  22.205  -5.789  1.00 96.09  ? 161  GLU   B CA  1 
ATOM   3857  C  C   . GLU   B 2 161 ? 24.395  23.459  -6.358  1.00 95.69  ? 161  GLU   B C   1 
ATOM   3858  O  O   . GLU   B 2 161 ? 25.199  24.102  -5.680  1.00 96.05  ? 161  GLU   B O   1 
ATOM   3859  C  CB  . GLU   B 2 161 ? 23.003  22.477  -4.482  1.00 93.75  ? 161  GLU   B CB  1 
ATOM   3860  C  CG  . GLU   B 2 161 ? 22.124  21.309  -3.982  1.00 95.18  ? 161  GLU   B CG  1 
ATOM   3861  C  CD  . GLU   B 2 161 ? 22.906  20.100  -3.449  1.00 102.45 ? 161  GLU   B CD  1 
ATOM   3862  O  OE1 . GLU   B 2 161 ? 24.102  20.232  -3.095  1.00 101.71 ? 161  GLU   B OE1 1 
ATOM   3863  O  OE2 . GLU   B 2 161 ? 22.304  18.997  -3.385  1.00 106.15 ? 161  GLU   B OE2 1 
ATOM   3864  N  N   . LEU   B 2 162 ? 24.089  23.792  -7.611  1.00 95.45  ? 162  LEU   B N   1 
ATOM   3865  C  CA  . LEU   B 2 162 ? 24.818  24.823  -8.337  1.00 96.04  ? 162  LEU   B CA  1 
ATOM   3866  C  C   . LEU   B 2 162 ? 24.084  26.158  -8.396  1.00 98.14  ? 162  LEU   B C   1 
ATOM   3867  O  O   . LEU   B 2 162 ? 24.609  27.112  -8.981  1.00 100.30 ? 162  LEU   B O   1 
ATOM   3868  C  CB  . LEU   B 2 162 ? 25.122  24.340  -9.763  1.00 92.00  ? 162  LEU   B CB  1 
ATOM   3869  C  CG  . LEU   B 2 162 ? 25.587  22.897  -9.914  1.00 87.74  ? 162  LEU   B CG  1 
ATOM   3870  C  CD1 . LEU   B 2 162 ? 25.629  22.558  -11.352 1.00 79.39  ? 162  LEU   B CD1 1 
ATOM   3871  C  CD2 . LEU   B 2 162 ? 26.955  22.700  -9.326  1.00 90.24  ? 162  LEU   B CD2 1 
ATOM   3872  N  N   . HIS   B 2 163 ? 22.878  26.250  -7.839  1.00 95.32  ? 163  HIS   B N   1 
ATOM   3873  C  CA  . HIS   B 2 163 ? 22.186  27.534  -7.691  1.00 93.60  ? 163  HIS   B CA  1 
ATOM   3874  C  C   . HIS   B 2 163 ? 21.711  27.610  -6.243  1.00 93.38  ? 163  HIS   B C   1 
ATOM   3875  O  O   . HIS   B 2 163 ? 20.547  27.342  -5.943  1.00 94.39  ? 163  HIS   B O   1 
ATOM   3876  C  CB  . HIS   B 2 163 ? 21.017  27.696  -8.673  1.00 93.68  ? 163  HIS   B CB  1 
ATOM   3877  C  CG  . HIS   B 2 163 ? 21.419  27.627  -10.114 1.00 103.07 ? 163  HIS   B CG  1 
ATOM   3878  N  ND1 . HIS   B 2 163 ? 22.172  28.611  -10.726 1.00 105.65 ? 163  HIS   B ND1 1 
ATOM   3879  C  CD2 . HIS   B 2 163 ? 21.192  26.685  -11.063 1.00 109.13 ? 163  HIS   B CD2 1 
ATOM   3880  C  CE1 . HIS   B 2 163 ? 22.379  28.285  -11.990 1.00 104.86 ? 163  HIS   B CE1 1 
ATOM   3881  N  NE2 . HIS   B 2 163 ? 21.798  27.121  -12.220 1.00 110.63 ? 163  HIS   B NE2 1 
ATOM   3882  N  N   . VAL   B 2 164 ? 22.619  27.976  -5.343  1.00 85.20  ? 164  VAL   B N   1 
ATOM   3883  C  CA  . VAL   B 2 164 ? 22.253  28.241  -3.962  1.00 84.54  ? 164  VAL   B CA  1 
ATOM   3884  C  C   . VAL   B 2 164 ? 21.891  29.716  -3.820  1.00 84.05  ? 164  VAL   B C   1 
ATOM   3885  O  O   . VAL   B 2 164 ? 22.663  30.594  -4.224  1.00 78.37  ? 164  VAL   B O   1 
ATOM   3886  C  CB  . VAL   B 2 164 ? 23.403  27.858  -3.019  1.00 88.37  ? 164  VAL   B CB  1 
ATOM   3887  C  CG1 . VAL   B 2 164 ? 24.011  26.565  -3.468  1.00 87.54  ? 164  VAL   B CG1 1 
ATOM   3888  C  CG2 . VAL   B 2 164 ? 24.464  28.927  -3.025  1.00 88.59  ? 164  VAL   B CG2 1 
ATOM   3889  N  N   . ILE   B 2 165 ? 20.718  29.993  -3.246  1.00 85.23  ? 165  ILE   B N   1 
ATOM   3890  C  CA  . ILE   B 2 165 ? 20.255  31.376  -3.084  1.00 80.92  ? 165  ILE   B CA  1 
ATOM   3891  C  C   . ILE   B 2 165 ? 20.962  32.070  -1.919  1.00 80.71  ? 165  ILE   B C   1 
ATOM   3892  O  O   . ILE   B 2 165 ? 21.648  33.073  -2.114  1.00 86.41  ? 165  ILE   B O   1 
ATOM   3893  C  CB  . ILE   B 2 165 ? 18.719  31.396  -2.913  1.00 79.65  ? 165  ILE   B CB  1 
ATOM   3894  C  CG1 . ILE   B 2 165 ? 18.082  30.291  -3.769  1.00 81.71  ? 165  ILE   B CG1 1 
ATOM   3895  C  CG2 . ILE   B 2 165 ? 18.187  32.782  -3.196  1.00 83.87  ? 165  ILE   B CG2 1 
ATOM   3896  C  CD1 . ILE   B 2 165 ? 18.486  30.321  -5.210  1.00 82.16  ? 165  ILE   B CD1 1 
ATOM   3897  N  N   . ASP   B 2 166 ? 20.800  31.548  -0.700  1.00 78.89  ? 166  ASP   B N   1 
ATOM   3898  C  CA  . ASP   B 2 166 ? 21.338  32.095  0.542   1.00 72.29  ? 166  ASP   B CA  1 
ATOM   3899  C  C   . ASP   B 2 166 ? 21.808  30.951  1.436   1.00 82.04  ? 166  ASP   B C   1 
ATOM   3900  O  O   . ASP   B 2 166 ? 21.228  29.859  1.414   1.00 82.43  ? 166  ASP   B O   1 
ATOM   3901  C  CB  . ASP   B 2 166 ? 20.267  32.900  1.273   1.00 74.34  ? 166  ASP   B CB  1 
ATOM   3902  C  CG  . ASP   B 2 166 ? 20.800  33.670  2.475   1.00 80.66  ? 166  ASP   B CG  1 
ATOM   3903  O  OD1 . ASP   B 2 166 ? 22.033  33.798  2.678   1.00 79.37  ? 166  ASP   B OD1 1 
ATOM   3904  O  OD2 . ASP   B 2 166 ? 19.937  34.170  3.231   1.00 82.83  ? 166  ASP   B OD2 1 
ATOM   3905  N  N   . VAL   B 2 167 ? 22.841  31.208  2.248   1.00 81.64  ? 167  VAL   B N   1 
ATOM   3906  C  CA  . VAL   B 2 167 ? 23.471  30.161  3.058   1.00 79.83  ? 167  VAL   B CA  1 
ATOM   3907  C  C   . VAL   B 2 167 ? 24.017  30.757  4.345   1.00 79.41  ? 167  VAL   B C   1 
ATOM   3908  O  O   . VAL   B 2 167 ? 24.772  31.728  4.312   1.00 84.04  ? 167  VAL   B O   1 
ATOM   3909  C  CB  . VAL   B 2 167 ? 24.625  29.470  2.308   1.00 79.63  ? 167  VAL   B CB  1 
ATOM   3910  C  CG1 . VAL   B 2 167 ? 25.616  30.506  1.851   1.00 73.81  ? 167  VAL   B CG1 1 
ATOM   3911  C  CG2 . VAL   B 2 167 ? 25.321  28.515  3.225   1.00 74.47  ? 167  VAL   B CG2 1 
ATOM   3912  N  N   . LYS   B 2 168 ? 23.709  30.130  5.477   1.00 81.81  ? 168  LYS   B N   1 
ATOM   3913  C  CA  . LYS   B 2 168 ? 24.244  30.566  6.759   1.00 82.40  ? 168  LYS   B CA  1 
ATOM   3914  C  C   . LYS   B 2 168 ? 24.684  29.356  7.576   1.00 84.21  ? 168  LYS   B C   1 
ATOM   3915  O  O   . LYS   B 2 168 ? 24.142  28.259  7.417   1.00 81.93  ? 168  LYS   B O   1 
ATOM   3916  C  CB  . LYS   B 2 168 ? 23.202  31.399  7.532   1.00 78.26  ? 168  LYS   B CB  1 
ATOM   3917  C  CG  . LYS   B 2 168 ? 22.707  32.631  6.777   1.00 81.04  ? 168  LYS   B CG  1 
ATOM   3918  C  CD  . LYS   B 2 168 ? 22.675  33.853  7.667   1.00 83.32  ? 168  LYS   B CD  1 
ATOM   3919  C  CE  . LYS   B 2 168 ? 22.824  35.140  6.867   1.00 86.77  ? 168  LYS   B CE  1 
ATOM   3920  N  NZ  . LYS   B 2 168 ? 21.656  35.381  5.959   1.00 88.45  ? 168  LYS   B NZ  1 
ATOM   3921  N  N   . PHE   B 2 169 ? 25.692  29.550  8.435   1.00 83.33  ? 169  PHE   B N   1 
ATOM   3922  C  CA  . PHE   B 2 169 ? 26.005  28.518  9.418   1.00 84.33  ? 169  PHE   B CA  1 
ATOM   3923  C  C   . PHE   B 2 169 ? 24.866  28.430  10.427  1.00 86.94  ? 169  PHE   B C   1 
ATOM   3924  O  O   . PHE   B 2 169 ? 24.209  29.432  10.733  1.00 90.57  ? 169  PHE   B O   1 
ATOM   3925  C  CB  . PHE   B 2 169 ? 27.325  28.807  10.140  1.00 85.27  ? 169  PHE   B CB  1 
ATOM   3926  C  CG  . PHE   B 2 169 ? 28.554  28.462  9.337   1.00 87.98  ? 169  PHE   B CG  1 
ATOM   3927  C  CD1 . PHE   B 2 169 ? 29.053  27.164  9.321   1.00 93.40  ? 169  PHE   B CD1 1 
ATOM   3928  C  CD2 . PHE   B 2 169 ? 29.221  29.428  8.609   1.00 86.93  ? 169  PHE   B CD2 1 
ATOM   3929  C  CE1 . PHE   B 2 169 ? 30.192  26.837  8.584   1.00 90.24  ? 169  PHE   B CE1 1 
ATOM   3930  C  CE2 . PHE   B 2 169 ? 30.350  29.111  7.877   1.00 86.00  ? 169  PHE   B CE2 1 
ATOM   3931  C  CZ  . PHE   B 2 169 ? 30.836  27.813  7.866   1.00 88.15  ? 169  PHE   B CZ  1 
ATOM   3932  N  N   . LEU   B 2 170 ? 24.616  27.227  10.937  1.00 86.26  ? 170  LEU   B N   1 
ATOM   3933  C  CA  . LEU   B 2 170 ? 23.539  27.018  11.898  1.00 87.17  ? 170  LEU   B CA  1 
ATOM   3934  C  C   . LEU   B 2 170 ? 24.076  27.068  13.318  1.00 92.57  ? 170  LEU   B C   1 
ATOM   3935  O  O   . LEU   B 2 170 ? 25.258  26.815  13.569  1.00 92.24  ? 170  LEU   B O   1 
ATOM   3936  C  CB  . LEU   B 2 170 ? 22.845  25.676  11.676  1.00 88.43  ? 170  LEU   B CB  1 
ATOM   3937  C  CG  . LEU   B 2 170 ? 21.939  25.484  10.466  1.00 87.55  ? 170  LEU   B CG  1 
ATOM   3938  C  CD1 . LEU   B 2 170 ? 21.246  24.157  10.621  1.00 90.00  ? 170  LEU   B CD1 1 
ATOM   3939  C  CD2 . LEU   B 2 170 ? 20.915  26.594  10.365  1.00 87.65  ? 170  LEU   B CD2 1 
ATOM   3940  N  N   . TYR   B 2 171 ? 23.189  27.382  14.254  1.00 94.17  ? 171  TYR   B N   1 
ATOM   3941  C  CA  . TYR   B 2 171 ? 23.608  27.418  15.644  1.00 94.77  ? 171  TYR   B CA  1 
ATOM   3942  C  C   . TYR   B 2 171 ? 23.378  26.059  16.305  1.00 98.53  ? 171  TYR   B C   1 
ATOM   3943  O  O   . TYR   B 2 171 ? 22.660  25.194  15.790  1.00 98.56  ? 171  TYR   B O   1 
ATOM   3944  C  CB  . TYR   B 2 171 ? 22.855  28.517  16.403  1.00 95.51  ? 171  TYR   B CB  1 
ATOM   3945  C  CG  . TYR   B 2 171 ? 23.375  29.928  16.186  1.00 89.65  ? 171  TYR   B CG  1 
ATOM   3946  C  CD1 . TYR   B 2 171 ? 24.591  30.326  16.706  1.00 89.40  ? 171  TYR   B CD1 1 
ATOM   3947  C  CD2 . TYR   B 2 171 ? 22.633  30.868  15.487  1.00 92.55  ? 171  TYR   B CD2 1 
ATOM   3948  C  CE1 . TYR   B 2 171 ? 25.071  31.614  16.531  1.00 87.21  ? 171  TYR   B CE1 1 
ATOM   3949  C  CE2 . TYR   B 2 171 ? 23.101  32.174  15.298  1.00 92.94  ? 171  TYR   B CE2 1 
ATOM   3950  C  CZ  . TYR   B 2 171 ? 24.327  32.543  15.824  1.00 92.21  ? 171  TYR   B CZ  1 
ATOM   3951  O  OH  . TYR   B 2 171 ? 24.808  33.829  15.648  1.00 83.43  ? 171  TYR   B OH  1 
ATOM   3952  N  N   . GLY   B 2 172 ? 24.008  25.881  17.464  1.00 101.39 ? 172  GLY   B N   1 
ATOM   3953  C  CA  . GLY   B 2 172 ? 23.640  24.818  18.377  1.00 109.07 ? 172  GLY   B CA  1 
ATOM   3954  C  C   . GLY   B 2 172 ? 23.789  23.413  17.838  1.00 113.07 ? 172  GLY   B C   1 
ATOM   3955  O  O   . GLY   B 2 172 ? 22.945  22.546  18.082  1.00 115.31 ? 172  GLY   B O   1 
ATOM   3956  N  N   . CYS   B 2 173 ? 24.861  23.160  17.110  1.00 111.53 ? 173  CYS   B N   1 
ATOM   3957  C  CA  . CYS   B 2 173 ? 25.036  21.868  16.476  1.00 113.91 ? 173  CYS   B CA  1 
ATOM   3958  C  C   . CYS   B 2 173 ? 26.476  21.422  16.677  1.00 119.52 ? 173  CYS   B C   1 
ATOM   3959  O  O   . CYS   B 2 173 ? 27.378  22.246  16.853  1.00 120.08 ? 173  CYS   B O   1 
ATOM   3960  C  CB  . CYS   B 2 173 ? 24.655  21.932  14.987  1.00 110.82 ? 173  CYS   B CB  1 
ATOM   3961  S  SG  . CYS   B 2 173 ? 25.939  22.625  13.918  1.00 118.01 ? 173  CYS   B SG  1 
ATOM   3962  N  N   . GLN   B 2 174 ? 26.678  20.102  16.672  1.00 123.93 ? 174  GLN   B N   1 
ATOM   3963  C  CA  . GLN   B 2 174 ? 27.927  19.539  17.178  1.00 120.71 ? 174  GLN   B CA  1 
ATOM   3964  C  C   . GLN   B 2 174 ? 29.113  19.970  16.328  1.00 116.42 ? 174  GLN   B C   1 
ATOM   3965  O  O   . GLN   B 2 174 ? 30.054  20.603  16.828  1.00 112.29 ? 174  GLN   B O   1 
ATOM   3966  C  CB  . GLN   B 2 174 ? 27.818  18.021  17.224  1.00 127.65 ? 174  GLN   B CB  1 
ATOM   3967  C  CG  . GLN   B 2 174 ? 26.411  17.534  17.521  1.00 139.22 ? 174  GLN   B CG  1 
ATOM   3968  C  CD  . GLN   B 2 174 ? 26.370  16.388  18.525  1.00 147.48 ? 174  GLN   B CD  1 
ATOM   3969  O  OE1 . GLN   B 2 174 ? 27.334  16.148  19.258  1.00 142.99 ? 174  GLN   B OE1 1 
ATOM   3970  N  NE2 . GLN   B 2 174 ? 25.244  15.675  18.562  1.00 149.77 ? 174  GLN   B NE2 1 
ATOM   3971  N  N   . ALA   B 2 175 ? 29.087  19.612  15.017  1.00 111.68 ? 175  ALA   B N   1 
ATOM   3972  C  CA  . ALA   B 2 175 ? 30.069  19.922  13.992  1.00 105.60 ? 175  ALA   B CA  1 
ATOM   3973  C  C   . ALA   B 2 175 ? 29.577  21.061  13.111  1.00 100.98 ? 175  ALA   B C   1 
ATOM   3974  O  O   . ALA   B 2 175 ? 28.370  21.206  12.901  1.00 100.00 ? 175  ALA   B O   1 
ATOM   3975  C  CB  . ALA   B 2 175 ? 30.347  18.704  13.114  1.00 103.26 ? 175  ALA   B CB  1 
ATOM   3976  N  N   . PRO   B 2 176 ? 30.489  21.877  12.584  1.00 93.60  ? 176  PRO   B N   1 
ATOM   3977  C  CA  . PRO   B 2 176 ? 30.076  23.032  11.783  1.00 96.39  ? 176  PRO   B CA  1 
ATOM   3978  C  C   . PRO   B 2 176 ? 29.081  22.633  10.706  1.00 96.21  ? 176  PRO   B C   1 
ATOM   3979  O  O   . PRO   B 2 176 ? 29.290  21.675  9.954   1.00 96.06  ? 176  PRO   B O   1 
ATOM   3980  C  CB  . PRO   B 2 176 ? 31.396  23.532  11.195  1.00 94.20  ? 176  PRO   B CB  1 
ATOM   3981  C  CG  . PRO   B 2 176 ? 32.390  23.158  12.229  1.00 99.61  ? 176  PRO   B CG  1 
ATOM   3982  C  CD  . PRO   B 2 176 ? 31.949  21.812  12.737  1.00 95.59  ? 176  PRO   B CD  1 
ATOM   3983  N  N   . THR   B 2 177 ? 27.982  23.375  10.643  1.00 91.74  ? 177  THR   B N   1 
ATOM   3984  C  CA  . THR   B 2 177 ? 26.873  23.043  9.767   1.00 92.26  ? 177  THR   B CA  1 
ATOM   3985  C  C   . THR   B 2 177 ? 26.387  24.274  9.022   1.00 91.18  ? 177  THR   B C   1 
ATOM   3986  O  O   . THR   B 2 177 ? 26.070  25.296  9.637   1.00 90.96  ? 177  THR   B O   1 
ATOM   3987  C  CB  . THR   B 2 177 ? 25.703  22.457  10.551  1.00 90.19  ? 177  THR   B CB  1 
ATOM   3988  O  OG1 . THR   B 2 177 ? 26.066  21.164  11.036  1.00 95.59  ? 177  THR   B OG1 1 
ATOM   3989  C  CG2 . THR   B 2 177 ? 24.466  22.358  9.647   1.00 88.04  ? 177  THR   B CG2 1 
ATOM   3990  N  N   . ILE   B 2 178 ? 26.279  24.153  7.718   1.00 89.55  ? 178  ILE   B N   1 
ATOM   3991  C  CA  . ILE   B 2 178 ? 25.696  25.197  6.899   1.00 85.09  ? 178  ILE   B CA  1 
ATOM   3992  C  C   . ILE   B 2 178 ? 24.282  24.792  6.526   1.00 87.43  ? 178  ILE   B C   1 
ATOM   3993  O  O   . ILE   B 2 178 ? 23.969  23.610  6.348   1.00 88.63  ? 178  ILE   B O   1 
ATOM   3994  C  CB  . ILE   B 2 178 ? 26.532  25.486  5.636   1.00 82.72  ? 178  ILE   B CB  1 
ATOM   3995  C  CG1 . ILE   B 2 178 ? 26.815  24.199  4.854   1.00 83.12  ? 178  ILE   B CG1 1 
ATOM   3996  C  CG2 . ILE   B 2 178 ? 27.791  26.247  6.013   1.00 84.93  ? 178  ILE   B CG2 1 
ATOM   3997  C  CD1 . ILE   B 2 178 ? 27.196  24.457  3.419   1.00 79.14  ? 178  ILE   B CD1 1 
ATOM   3998  N  N   . CYS   B 2 179 ? 23.427  25.799  6.396   1.00 86.99  ? 179  CYS   B N   1 
ATOM   3999  C  CA  . CYS   B 2 179 ? 22.044  25.629  5.989   1.00 83.81  ? 179  CYS   B CA  1 
ATOM   4000  C  C   . CYS   B 2 179 ? 21.812  26.513  4.778   1.00 84.22  ? 179  CYS   B C   1 
ATOM   4001  O  O   . CYS   B 2 179 ? 22.110  27.711  4.833   1.00 81.64  ? 179  CYS   B O   1 
ATOM   4002  C  CB  . CYS   B 2 179 ? 21.106  25.999  7.129   1.00 79.00  ? 179  CYS   B CB  1 
ATOM   4003  S  SG  . CYS   B 2 179 ? 19.427  25.784  6.694   1.00 84.88  ? 179  CYS   B SG  1 
ATOM   4004  N  N   . PHE   B 2 180 ? 21.313  25.928  3.679   1.00 88.09  ? 180  PHE   B N   1 
ATOM   4005  C  CA  . PHE   B 2 180 ? 21.237  26.676  2.428   1.00 84.02  ? 180  PHE   B CA  1 
ATOM   4006  C  C   . PHE   B 2 180 ? 19.946  26.388  1.665   1.00 85.03  ? 180  PHE   B C   1 
ATOM   4007  O  O   . PHE   B 2 180 ? 19.356  25.312  1.772   1.00 84.91  ? 180  PHE   B O   1 
ATOM   4008  C  CB  . PHE   B 2 180 ? 22.495  26.435  1.548   1.00 81.58  ? 180  PHE   B CB  1 
ATOM   4009  C  CG  . PHE   B 2 180 ? 22.699  25.008  1.089   1.00 82.42  ? 180  PHE   B CG  1 
ATOM   4010  C  CD1 . PHE   B 2 180 ? 23.225  24.049  1.937   1.00 85.84  ? 180  PHE   B CD1 1 
ATOM   4011  C  CD2 . PHE   B 2 180 ? 22.427  24.648  -0.233  1.00 88.42  ? 180  PHE   B CD2 1 
ATOM   4012  C  CE1 . PHE   B 2 180 ? 23.425  22.724  1.480   1.00 95.52  ? 180  PHE   B CE1 1 
ATOM   4013  C  CE2 . PHE   B 2 180 ? 22.631  23.350  -0.698  1.00 90.82  ? 180  PHE   B CE2 1 
ATOM   4014  C  CZ  . PHE   B 2 180 ? 23.129  22.380  0.161   1.00 95.51  ? 180  PHE   B CZ  1 
ATOM   4015  N  N   . VAL   B 2 181 ? 19.495  27.409  0.929   1.00 89.63  ? 181  VAL   B N   1 
ATOM   4016  C  CA  . VAL   B 2 181 ? 18.341  27.344  0.036   1.00 85.34  ? 181  VAL   B CA  1 
ATOM   4017  C  C   . VAL   B 2 181 ? 18.871  27.332  -1.389  1.00 85.09  ? 181  VAL   B C   1 
ATOM   4018  O  O   . VAL   B 2 181 ? 19.584  28.262  -1.795  1.00 80.65  ? 181  VAL   B O   1 
ATOM   4019  C  CB  . VAL   B 2 181 ? 17.399  28.539  0.245   1.00 81.51  ? 181  VAL   B CB  1 
ATOM   4020  C  CG1 . VAL   B 2 181 ? 16.467  28.686  -0.954  1.00 81.14  ? 181  VAL   B CG1 1 
ATOM   4021  C  CG2 . VAL   B 2 181 ? 16.613  28.386  1.521   1.00 78.26  ? 181  VAL   B CG2 1 
ATOM   4022  N  N   . TYR   B 2 182 ? 18.520  26.285  -2.145  1.00 88.88  ? 182  TYR   B N   1 
ATOM   4023  C  CA  . TYR   B 2 182 ? 18.979  26.106  -3.522  1.00 86.50  ? 182  TYR   B CA  1 
ATOM   4024  C  C   . TYR   B 2 182 ? 17.796  25.846  -4.448  1.00 86.18  ? 182  TYR   B C   1 
ATOM   4025  O  O   . TYR   B 2 182 ? 16.711  25.444  -4.008  1.00 88.71  ? 182  TYR   B O   1 
ATOM   4026  C  CB  . TYR   B 2 182 ? 19.993  24.952  -3.635  1.00 86.66  ? 182  TYR   B CB  1 
ATOM   4027  C  CG  . TYR   B 2 182 ? 19.441  23.611  -3.241  1.00 89.90  ? 182  TYR   B CG  1 
ATOM   4028  C  CD1 . TYR   B 2 182 ? 19.304  23.267  -1.907  1.00 92.99  ? 182  TYR   B CD1 1 
ATOM   4029  C  CD2 . TYR   B 2 182 ? 19.041  22.680  -4.203  1.00 93.28  ? 182  TYR   B CD2 1 
ATOM   4030  C  CE1 . TYR   B 2 182 ? 18.784  22.025  -1.530  1.00 96.33  ? 182  TYR   B CE1 1 
ATOM   4031  C  CE2 . TYR   B 2 182 ? 18.521  21.433  -3.832  1.00 92.87  ? 182  TYR   B CE2 1 
ATOM   4032  C  CZ  . TYR   B 2 182 ? 18.397  21.118  -2.500  1.00 94.02  ? 182  TYR   B CZ  1 
ATOM   4033  O  OH  . TYR   B 2 182 ? 17.886  19.901  -2.121  1.00 101.54 ? 182  TYR   B OH  1 
ATOM   4034  N  N   . GLN   B 2 183 ? 18.019  26.072  -5.749  1.00 90.98  ? 183  GLN   B N   1 
ATOM   4035  C  CA  . GLN   B 2 183 ? 17.014  25.818  -6.779  1.00 94.09  ? 183  GLN   B CA  1 
ATOM   4036  C  C   . GLN   B 2 183 ? 17.559  24.848  -7.819  1.00 93.21  ? 183  GLN   B C   1 
ATOM   4037  O  O   . GLN   B 2 183 ? 18.725  24.936  -8.218  1.00 92.83  ? 183  GLN   B O   1 
ATOM   4038  C  CB  . GLN   B 2 183 ? 16.550  27.102  -7.462  1.00 88.78  ? 183  GLN   B CB  1 
ATOM   4039  C  CG  . GLN   B 2 183 ? 15.534  26.828  -8.537  1.00 92.83  ? 183  GLN   B CG  1 
ATOM   4040  C  CD  . GLN   B 2 183 ? 14.581  27.985  -8.757  1.00 103.61 ? 183  GLN   B CD  1 
ATOM   4041  O  OE1 . GLN   B 2 183 ? 13.627  28.169  -7.996  1.00 104.65 ? 183  GLN   B OE1 1 
ATOM   4042  N  NE2 . GLN   B 2 183 ? 14.823  28.767  -9.810  1.00 107.71 ? 183  GLN   B NE2 1 
ATOM   4043  N  N   . ASP   B 2 184 ? 16.726  23.904  -8.218  1.00 96.59  ? 184  ASP   B N   1 
ATOM   4044  C  CA  . ASP   B 2 184 ? 17.021  22.966  -9.291  1.00 98.61  ? 184  ASP   B CA  1 
ATOM   4045  C  C   . ASP   B 2 184 ? 15.746  22.854  -10.109 1.00 102.16 ? 184  ASP   B C   1 
ATOM   4046  O  O   . ASP   B 2 184 ? 14.759  23.546  -9.812  1.00 102.36 ? 184  ASP   B O   1 
ATOM   4047  C  CB  . ASP   B 2 184 ? 17.436  21.594  -8.749  1.00 99.18  ? 184  ASP   B CB  1 
ATOM   4048  C  CG  . ASP   B 2 184 ? 16.367  20.951  -7.884  1.00 102.96 ? 184  ASP   B CG  1 
ATOM   4049  O  OD1 . ASP   B 2 184 ? 15.233  21.496  -7.827  1.00 99.69  ? 184  ASP   B OD1 1 
ATOM   4050  O  OD2 . ASP   B 2 184 ? 16.674  19.906  -7.253  1.00 104.67 ? 184  ASP   B OD2 1 
ATOM   4051  N  N   . PRO   B 2 185 ? 15.722  22.014  -11.142 1.00 102.88 ? 185  PRO   B N   1 
ATOM   4052  C  CA  . PRO   B 2 185 ? 14.491  21.880  -11.937 1.00 103.43 ? 185  PRO   B CA  1 
ATOM   4053  C  C   . PRO   B 2 185 ? 13.219  21.765  -11.110 1.00 110.50 ? 185  PRO   B C   1 
ATOM   4054  O  O   . PRO   B 2 185 ? 12.257  22.509  -11.356 1.00 112.59 ? 185  PRO   B O   1 
ATOM   4055  C  CB  . PRO   B 2 185 ? 14.758  20.625  -12.768 1.00 97.41  ? 185  PRO   B CB  1 
ATOM   4056  C  CG  . PRO   B 2 185 ? 16.233  20.606  -12.911 1.00 97.48  ? 185  PRO   B CG  1 
ATOM   4057  C  CD  . PRO   B 2 185 ? 16.789  21.122  -11.621 1.00 101.63 ? 185  PRO   B CD  1 
ATOM   4058  N  N   . GLN   B 2 186 ? 13.197  20.883  -10.107 1.00 112.92 ? 186  GLN   B N   1 
ATOM   4059  C  CA  . GLN   B 2 186 ? 11.948  20.590  -9.413  1.00 113.39 ? 186  GLN   B CA  1 
ATOM   4060  C  C   . GLN   B 2 186 ? 11.577  21.618  -8.342  1.00 116.13 ? 186  GLN   B C   1 
ATOM   4061  O  O   . GLN   B 2 186 ? 10.498  21.500  -7.752  1.00 120.49 ? 186  GLN   B O   1 
ATOM   4062  C  CB  . GLN   B 2 186 ? 12.020  19.192  -8.806  1.00 113.34 ? 186  GLN   B CB  1 
ATOM   4063  C  CG  . GLN   B 2 186 ? 12.571  18.149  -9.779  1.00 118.99 ? 186  GLN   B CG  1 
ATOM   4064  C  CD  . GLN   B 2 186 ? 13.933  17.587  -9.351  1.00 119.43 ? 186  GLN   B CD  1 
ATOM   4065  O  OE1 . GLN   B 2 186 ? 14.100  17.134  -8.214  1.00 123.24 ? 186  GLN   B OE1 1 
ATOM   4066  N  NE2 . GLN   B 2 186 ? 14.910  17.622  -10.261 1.00 114.13 ? 186  GLN   B NE2 1 
ATOM   4067  N  N   . GLY   B 2 187 ? 12.404  22.618  -8.078  1.00 107.25 ? 187  GLY   B N   1 
ATOM   4068  C  CA  . GLY   B 2 187 ? 11.935  23.704  -7.238  1.00 99.25  ? 187  GLY   B CA  1 
ATOM   4069  C  C   . GLY   B 2 187 ? 13.076  24.318  -6.447  1.00 97.73  ? 187  GLY   B C   1 
ATOM   4070  O  O   . GLY   B 2 187 ? 14.231  24.285  -6.871  1.00 97.69  ? 187  GLY   B O   1 
ATOM   4071  N  N   . ARG   B 2 188 ? 12.699  24.885  -5.303  1.00 97.97  ? 188  ARG   B N   1 
ATOM   4072  C  CA  . ARG   B 2 188 ? 13.616  25.448  -4.325  1.00 91.17  ? 188  ARG   B CA  1 
ATOM   4073  C  C   . ARG   B 2 188 ? 13.528  24.634  -3.038  1.00 91.55  ? 188  ARG   B C   1 
ATOM   4074  O  O   . ARG   B 2 188 ? 12.438  24.251  -2.591  1.00 94.01  ? 188  ARG   B O   1 
ATOM   4075  C  CB  . ARG   B 2 188 ? 13.289  26.928  -4.065  1.00 92.35  ? 188  ARG   B CB  1 
ATOM   4076  C  CG  . ARG   B 2 188 ? 13.525  27.820  -5.274  1.00 91.85  ? 188  ARG   B CG  1 
ATOM   4077  C  CD  . ARG   B 2 188 ? 13.265  29.288  -4.970  1.00 94.34  ? 188  ARG   B CD  1 
ATOM   4078  N  NE  . ARG   B 2 188 ? 13.468  30.144  -6.136  1.00 94.96  ? 188  ARG   B NE  1 
ATOM   4079  C  CZ  . ARG   B 2 188 ? 14.649  30.600  -6.524  1.00 96.05  ? 188  ARG   B CZ  1 
ATOM   4080  N  NH1 . ARG   B 2 188 ? 15.758  30.294  -5.870  1.00 93.82  ? 188  ARG   B NH1 1 
ATOM   4081  N  NH2 . ARG   B 2 188 ? 14.717  31.382  -7.590  1.00 106.22 ? 188  ARG   B NH2 1 
ATOM   4082  N  N   . HIS   B 2 189 ? 14.678  24.355  -2.450  1.00 90.08  ? 189  HIS   B N   1 
ATOM   4083  C  CA  . HIS   B 2 189 ? 14.739  23.390  -1.368  1.00 95.81  ? 189  HIS   B CA  1 
ATOM   4084  C  C   . HIS   B 2 189 ? 15.768  23.863  -0.361  1.00 92.53  ? 189  HIS   B C   1 
ATOM   4085  O  O   . HIS   B 2 189 ? 16.665  24.646  -0.687  1.00 89.54  ? 189  HIS   B O   1 
ATOM   4086  C  CB  . HIS   B 2 189 ? 15.105  21.987  -1.882  1.00 97.70  ? 189  HIS   B CB  1 
ATOM   4087  C  CG  . HIS   B 2 189 ? 14.531  21.669  -3.230  1.00 97.00  ? 189  HIS   B CG  1 
ATOM   4088  N  ND1 . HIS   B 2 189 ? 13.231  21.242  -3.407  1.00 100.90 ? 189  HIS   B ND1 1 
ATOM   4089  C  CD2 . HIS   B 2 189 ? 15.076  21.737  -4.468  1.00 96.14  ? 189  HIS   B CD2 1 
ATOM   4090  C  CE1 . HIS   B 2 189 ? 13.003  21.046  -4.694  1.00 100.75 ? 189  HIS   B CE1 1 
ATOM   4091  N  NE2 . HIS   B 2 189 ? 14.106  21.340  -5.361  1.00 100.59 ? 189  HIS   B NE2 1 
ATOM   4092  N  N   . VAL   B 2 190 ? 15.621  23.400  0.878   1.00 91.44  ? 190  VAL   B N   1 
ATOM   4093  C  CA  . VAL   B 2 190 ? 16.539  23.753  1.953   1.00 89.42  ? 190  VAL   B CA  1 
ATOM   4094  C  C   . VAL   B 2 190 ? 17.268  22.494  2.375   1.00 90.22  ? 190  VAL   B C   1 
ATOM   4095  O  O   . VAL   B 2 190 ? 16.643  21.463  2.626   1.00 98.08  ? 190  VAL   B O   1 
ATOM   4096  C  CB  . VAL   B 2 190 ? 15.824  24.405  3.148   1.00 89.63  ? 190  VAL   B CB  1 
ATOM   4097  C  CG1 . VAL   B 2 190 ? 16.795  24.589  4.282   1.00 89.67  ? 190  VAL   B CG1 1 
ATOM   4098  C  CG2 . VAL   B 2 190 ? 15.251  25.767  2.762   1.00 91.89  ? 190  VAL   B CG2 1 
ATOM   4099  N  N   . LYS   B 2 191 ? 18.588  22.575  2.446   1.00 89.03  ? 191  LYS   B N   1 
ATOM   4100  C  CA  . LYS   B 2 191 ? 19.400  21.447  2.842   1.00 89.34  ? 191  LYS   B CA  1 
ATOM   4101  C  C   . LYS   B 2 191 ? 20.458  21.924  3.827   1.00 90.50  ? 191  LYS   B C   1 
ATOM   4102  O  O   . LYS   B 2 191 ? 20.801  23.108  3.876   1.00 84.96  ? 191  LYS   B O   1 
ATOM   4103  C  CB  . LYS   B 2 191 ? 20.039  20.792  1.621   1.00 90.17  ? 191  LYS   B CB  1 
ATOM   4104  C  CG  . LYS   B 2 191 ? 20.848  19.592  1.993   1.00 95.96  ? 191  LYS   B CG  1 
ATOM   4105  C  CD  . LYS   B 2 191 ? 20.964  18.653  0.824   1.00 98.80  ? 191  LYS   B CD  1 
ATOM   4106  C  CE  . LYS   B 2 191 ? 21.920  19.205  -0.203  1.00 101.19 ? 191  LYS   B CE  1 
ATOM   4107  N  NZ  . LYS   B 2 191 ? 22.429  18.093  -1.050  1.00 105.05 ? 191  LYS   B NZ  1 
ATOM   4108  N  N   . THR   B 2 192 ? 20.967  20.990  4.628   1.00 94.93  ? 192  THR   B N   1 
ATOM   4109  C  CA  . THR   B 2 192 ? 22.144  21.243  5.446   1.00 91.94  ? 192  THR   B CA  1 
ATOM   4110  C  C   . THR   B 2 192 ? 23.270  20.311  5.023   1.00 87.58  ? 192  THR   B C   1 
ATOM   4111  O  O   . THR   B 2 192 ? 23.043  19.313  4.334   1.00 93.59  ? 192  THR   B O   1 
ATOM   4112  C  CB  . THR   B 2 192 ? 21.873  21.043  6.929   1.00 89.89  ? 192  THR   B CB  1 
ATOM   4113  O  OG1 . THR   B 2 192 ? 21.527  19.673  7.146   1.00 85.09  ? 192  THR   B OG1 1 
ATOM   4114  C  CG2 . THR   B 2 192 ? 20.747  21.982  7.406   1.00 88.32  ? 192  THR   B CG2 1 
ATOM   4115  N  N   . TYR   B 2 193 ? 24.489  20.671  5.432   1.00 81.92  ? 193  TYR   B N   1 
ATOM   4116  C  CA  . TYR   B 2 193 ? 25.668  19.816  5.355   1.00 88.87  ? 193  TYR   B CA  1 
ATOM   4117  C  C   . TYR   B 2 193 ? 26.542  20.104  6.561   1.00 92.76  ? 193  TYR   B C   1 
ATOM   4118  O  O   . TYR   B 2 193 ? 26.519  21.210  7.108   1.00 93.44  ? 193  TYR   B O   1 
ATOM   4119  C  CB  . TYR   B 2 193 ? 26.547  20.052  4.120   1.00 94.07  ? 193  TYR   B CB  1 
ATOM   4120  C  CG  . TYR   B 2 193 ? 26.063  19.480  2.806   1.00 95.37  ? 193  TYR   B CG  1 
ATOM   4121  C  CD1 . TYR   B 2 193 ? 25.507  18.214  2.722   1.00 90.68  ? 193  TYR   B CD1 1 
ATOM   4122  C  CD2 . TYR   B 2 193 ? 26.173  20.224  1.647   1.00 94.41  ? 193  TYR   B CD2 1 
ATOM   4123  C  CE1 . TYR   B 2 193 ? 25.068  17.715  1.498   1.00 93.35  ? 193  TYR   B CE1 1 
ATOM   4124  C  CE2 . TYR   B 2 193 ? 25.742  19.741  0.445   1.00 97.62  ? 193  TYR   B CE2 1 
ATOM   4125  C  CZ  . TYR   B 2 193 ? 25.192  18.492  0.363   1.00 96.72  ? 193  TYR   B CZ  1 
ATOM   4126  O  OH  . TYR   B 2 193 ? 24.789  18.057  -0.884  1.00 98.67  ? 193  TYR   B OH  1 
ATOM   4127  N  N   . GLU   B 2 194 ? 27.347  19.125  6.946   1.00 89.89  ? 194  GLU   B N   1 
ATOM   4128  C  CA  . GLU   B 2 194 ? 28.367  19.373  7.949   1.00 91.25  ? 194  GLU   B CA  1 
ATOM   4129  C  C   . GLU   B 2 194 ? 29.717  19.497  7.267   1.00 93.65  ? 194  GLU   B C   1 
ATOM   4130  O  O   . GLU   B 2 194 ? 29.986  18.844  6.254   1.00 94.52  ? 194  GLU   B O   1 
ATOM   4131  C  CB  . GLU   B 2 194 ? 28.420  18.269  9.002   1.00 96.57  ? 194  GLU   B CB  1 
ATOM   4132  C  CG  . GLU   B 2 194 ? 27.227  18.259  9.935   1.00 99.60  ? 194  GLU   B CG  1 
ATOM   4133  C  CD  . GLU   B 2 194 ? 27.455  17.421  11.188  1.00 105.62 ? 194  GLU   B CD  1 
ATOM   4134  O  OE1 . GLU   B 2 194 ? 28.433  16.637  11.244  1.00 101.04 ? 194  GLU   B OE1 1 
ATOM   4135  O  OE2 . GLU   B 2 194 ? 26.642  17.564  12.126  1.00 114.68 ? 194  GLU   B OE2 1 
ATOM   4136  N  N   . VAL   B 2 195 ? 30.558  20.349  7.829   1.00 91.68  ? 195  VAL   B N   1 
ATOM   4137  C  CA  . VAL   B 2 195 ? 31.828  20.696  7.221   1.00 93.86  ? 195  VAL   B CA  1 
ATOM   4138  C  C   . VAL   B 2 195 ? 32.906  19.939  7.984   1.00 98.97  ? 195  VAL   B C   1 
ATOM   4139  O  O   . VAL   B 2 195 ? 33.152  20.207  9.174   1.00 98.68  ? 195  VAL   B O   1 
ATOM   4140  C  CB  . VAL   B 2 195 ? 32.061  22.215  7.246   1.00 95.80  ? 195  VAL   B CB  1 
ATOM   4141  C  CG1 . VAL   B 2 195 ? 33.304  22.597  6.445   1.00 93.77  ? 195  VAL   B CG1 1 
ATOM   4142  C  CG2 . VAL   B 2 195 ? 30.829  22.944  6.699   1.00 93.03  ? 195  VAL   B CG2 1 
ATOM   4143  N  N   . SER   B 2 196 ? 33.542  18.980  7.314   1.00 97.07  ? 196  SER   B N   1 
ATOM   4144  C  CA  . SER   B 2 196 ? 34.640  18.235  7.917   1.00 103.53 ? 196  SER   B CA  1 
ATOM   4145  C  C   . SER   B 2 196 ? 35.945  18.844  7.442   1.00 103.91 ? 196  SER   B C   1 
ATOM   4146  O  O   . SER   B 2 196 ? 36.334  18.690  6.276   1.00 102.30 ? 196  SER   B O   1 
ATOM   4147  C  CB  . SER   B 2 196 ? 34.589  16.754  7.575   1.00 107.82 ? 196  SER   B CB  1 
ATOM   4148  O  OG  . SER   B 2 196 ? 35.370  16.047  8.534   1.00 114.64 ? 196  SER   B OG  1 
ATOM   4149  N  N   . LEU   B 2 197 ? 36.617  19.553  8.347   1.00 100.96 ? 197  LEU   B N   1 
ATOM   4150  C  CA  . LEU   B 2 197 ? 37.944  20.048  8.017   1.00 107.25 ? 197  LEU   B CA  1 
ATOM   4151  C  C   . LEU   B 2 197 ? 38.941  18.896  7.996   1.00 114.74 ? 197  LEU   B C   1 
ATOM   4152  O  O   . LEU   B 2 197 ? 39.781  18.804  7.087   1.00 114.76 ? 197  LEU   B O   1 
ATOM   4153  C  CB  . LEU   B 2 197 ? 38.353  21.135  9.011   1.00 107.27 ? 197  LEU   B CB  1 
ATOM   4154  C  CG  . LEU   B 2 197 ? 37.242  22.151  9.283   1.00 108.48 ? 197  LEU   B CG  1 
ATOM   4155  C  CD1 . LEU   B 2 197 ? 36.446  21.734  10.513  1.00 114.68 ? 197  LEU   B CD1 1 
ATOM   4156  C  CD2 . LEU   B 2 197 ? 37.793  23.554  9.452   1.00 104.53 ? 197  LEU   B CD2 1 
ATOM   4157  N  N   . ARG   B 2 198 ? 38.853  18.002  8.991   1.00 117.72 ? 198  ARG   B N   1 
ATOM   4158  C  CA  . ARG   B 2 198 ? 39.604  16.757  8.970   1.00 111.36 ? 198  ARG   B CA  1 
ATOM   4159  C  C   . ARG   B 2 198 ? 39.597  16.185  7.564   1.00 109.76 ? 198  ARG   B C   1 
ATOM   4160  O  O   . ARG   B 2 198 ? 40.645  16.055  6.927   1.00 112.76 ? 198  ARG   B O   1 
ATOM   4161  C  CB  . ARG   B 2 198 ? 39.002  15.767  9.974   1.00 108.51 ? 198  ARG   B CB  1 
ATOM   4162  N  N   . GLU   B 2 199 ? 38.400  15.934  7.037   1.00 111.85 ? 199  GLU   B N   1 
ATOM   4163  C  CA  . GLU   B 2 199 ? 38.224  15.318  5.728   1.00 110.98 ? 199  GLU   B CA  1 
ATOM   4164  C  C   . GLU   B 2 199 ? 38.136  16.321  4.573   1.00 110.91 ? 199  GLU   B C   1 
ATOM   4165  O  O   . GLU   B 2 199 ? 38.154  15.891  3.414   1.00 113.09 ? 199  GLU   B O   1 
ATOM   4166  C  CB  . GLU   B 2 199 ? 36.965  14.431  5.738   1.00 115.02 ? 199  GLU   B CB  1 
ATOM   4167  C  CG  . GLU   B 2 199 ? 36.801  13.538  6.997   1.00 122.07 ? 199  GLU   B CG  1 
ATOM   4168  C  CD  . GLU   B 2 199 ? 35.686  12.469  6.878   1.00 127.07 ? 199  GLU   B CD  1 
ATOM   4169  O  OE1 . GLU   B 2 199 ? 34.972  12.410  5.840   1.00 121.24 ? 199  GLU   B OE1 1 
ATOM   4170  O  OE2 . GLU   B 2 199 ? 35.533  11.680  7.842   1.00 129.91 ? 199  GLU   B OE2 1 
ATOM   4171  N  N   . LYS   B 2 200 ? 38.045  17.634  4.841   1.00 107.83 ? 200  LYS   B N   1 
ATOM   4172  C  CA  . LYS   B 2 200 ? 38.061  18.650  3.778   1.00 97.61  ? 200  LYS   B CA  1 
ATOM   4173  C  C   . LYS   B 2 200 ? 36.986  18.381  2.730   1.00 100.43 ? 200  LYS   B C   1 
ATOM   4174  O  O   . LYS   B 2 200 ? 37.202  18.564  1.525   1.00 94.38  ? 200  LYS   B O   1 
ATOM   4175  C  CB  . LYS   B 2 200 ? 39.437  18.747  3.114   1.00 95.29  ? 200  LYS   B CB  1 
ATOM   4176  C  CG  . LYS   B 2 200 ? 40.467  19.516  3.942   1.00 106.30 ? 200  LYS   B CG  1 
ATOM   4177  C  CD  . LYS   B 2 200 ? 41.917  19.166  3.584   1.00 112.32 ? 200  LYS   B CD  1 
ATOM   4178  C  CE  . LYS   B 2 200 ? 42.361  19.840  2.289   1.00 109.11 ? 200  LYS   B CE  1 
ATOM   4179  N  NZ  . LYS   B 2 200 ? 43.853  19.896  2.191   1.00 112.99 ? 200  LYS   B NZ  1 
ATOM   4180  N  N   . GLU   B 2 201 ? 35.827  17.920  3.197   1.00 101.29 ? 201  GLU   B N   1 
ATOM   4181  C  CA  . GLU   B 2 201 ? 34.640  17.805  2.361   1.00 101.51 ? 201  GLU   B CA  1 
ATOM   4182  C  C   . GLU   B 2 201 ? 33.432  17.781  3.281   1.00 102.77 ? 201  GLU   B C   1 
ATOM   4183  O  O   . GLU   B 2 201 ? 33.566  17.827  4.508   1.00 103.31 ? 201  GLU   B O   1 
ATOM   4184  C  CB  . GLU   B 2 201 ? 34.690  16.568  1.455   1.00 108.91 ? 201  GLU   B CB  1 
ATOM   4185  C  CG  . GLU   B 2 201 ? 33.875  15.337  1.941   1.00 115.89 ? 201  GLU   B CG  1 
ATOM   4186  C  CD  . GLU   B 2 201 ? 34.716  14.320  2.719   1.00 119.80 ? 201  GLU   B CD  1 
ATOM   4187  O  OE1 . GLU   B 2 201 ? 35.866  14.683  3.060   1.00 117.12 ? 201  GLU   B OE1 1 
ATOM   4188  O  OE2 . GLU   B 2 201 ? 34.231  13.178  2.982   1.00 120.01 ? 201  GLU   B OE2 1 
ATOM   4189  N  N   . PHE   B 2 202 ? 32.245  17.719  2.670   1.00 98.12  ? 202  PHE   B N   1 
ATOM   4190  C  CA  . PHE   B 2 202 ? 30.966  17.724  3.373   1.00 96.28  ? 202  PHE   B CA  1 
ATOM   4191  C  C   . PHE   B 2 202 ? 30.573  16.310  3.790   1.00 101.12 ? 202  PHE   B C   1 
ATOM   4192  O  O   . PHE   B 2 202 ? 30.896  15.329  3.111   1.00 106.88 ? 202  PHE   B O   1 
ATOM   4193  C  CB  . PHE   B 2 202 ? 29.852  18.295  2.490   1.00 95.16  ? 202  PHE   B CB  1 
ATOM   4194  C  CG  . PHE   B 2 202 ? 29.917  19.784  2.272   1.00 95.88  ? 202  PHE   B CG  1 
ATOM   4195  C  CD1 . PHE   B 2 202 ? 30.177  20.650  3.316   1.00 95.54  ? 202  PHE   B CD1 1 
ATOM   4196  C  CD2 . PHE   B 2 202 ? 29.684  20.314  1.012   1.00 94.79  ? 202  PHE   B CD2 1 
ATOM   4197  C  CE1 . PHE   B 2 202 ? 30.217  22.016  3.107   1.00 93.83  ? 202  PHE   B CE1 1 
ATOM   4198  C  CE2 . PHE   B 2 202 ? 29.727  21.678  0.793   1.00 92.80  ? 202  PHE   B CE2 1 
ATOM   4199  C  CZ  . PHE   B 2 202 ? 29.990  22.534  1.843   1.00 92.35  ? 202  PHE   B CZ  1 
ATOM   4200  N  N   . ASN   B 2 203 ? 29.858  16.220  4.911   1.00 98.54  ? 203  ASN   B N   1 
ATOM   4201  C  CA  . ASN   B 2 203 ? 29.187  15.012  5.371   1.00 94.34  ? 203  ASN   B CA  1 
ATOM   4202  C  C   . ASN   B 2 203 ? 27.702  15.316  5.493   1.00 90.25  ? 203  ASN   B C   1 
ATOM   4203  O  O   . ASN   B 2 203 ? 27.291  16.475  5.423   1.00 99.98  ? 203  ASN   B O   1 
ATOM   4204  C  CB  . ASN   B 2 203 ? 29.751  14.534  6.716   1.00 99.82  ? 203  ASN   B CB  1 
ATOM   4205  C  CG  . ASN   B 2 203 ? 31.129  13.877  6.584   1.00 111.59 ? 203  ASN   B CG  1 
ATOM   4206  O  OD1 . ASN   B 2 203 ? 31.405  13.141  5.622   1.00 116.01 ? 203  ASN   B OD1 1 
ATOM   4207  N  ND2 . ASN   B 2 203 ? 32.004  14.144  7.556   1.00 112.24 ? 203  ASN   B ND2 1 
ATOM   4208  N  N   . LYS   B 2 204 ? 26.881  14.283  5.682   1.00 89.48  ? 204  LYS   B N   1 
ATOM   4209  C  CA  . LYS   B 2 204 ? 25.436  14.498  5.722   1.00 95.48  ? 204  LYS   B CA  1 
ATOM   4210  C  C   . LYS   B 2 204 ? 25.072  15.565  6.758   1.00 93.32  ? 204  LYS   B C   1 
ATOM   4211  O  O   . LYS   B 2 204 ? 25.822  15.820  7.700   1.00 94.88  ? 204  LYS   B O   1 
ATOM   4212  C  CB  . LYS   B 2 204 ? 24.698  13.199  6.053   1.00 93.10  ? 204  LYS   B CB  1 
ATOM   4213  N  N   . GLY   B 2 205 ? 23.903  16.184  6.592   1.00 85.37  ? 205  GLY   B N   1 
ATOM   4214  C  CA  . GLY   B 2 205 ? 23.468  17.212  7.510   1.00 89.92  ? 205  GLY   B CA  1 
ATOM   4215  C  C   . GLY   B 2 205 ? 22.361  16.762  8.450   1.00 94.77  ? 205  GLY   B C   1 
ATOM   4216  O  O   . GLY   B 2 205 ? 21.731  15.729  8.243   1.00 100.55 ? 205  GLY   B O   1 
ATOM   4217  N  N   . PRO   B 2 206 ? 22.094  17.546  9.508   1.00 94.37  ? 206  PRO   B N   1 
ATOM   4218  C  CA  . PRO   B 2 206 ? 21.021  17.163  10.453  1.00 92.25  ? 206  PRO   B CA  1 
ATOM   4219  C  C   . PRO   B 2 206 ? 19.623  17.061  9.849   1.00 94.16  ? 206  PRO   B C   1 
ATOM   4220  O  O   . PRO   B 2 206 ? 18.877  16.163  10.255  1.00 95.15  ? 206  PRO   B O   1 
ATOM   4221  C  CB  . PRO   B 2 206 ? 21.091  18.263  11.519  1.00 92.94  ? 206  PRO   B CB  1 
ATOM   4222  C  CG  . PRO   B 2 206 ? 21.939  19.339  10.954  1.00 91.00  ? 206  PRO   B CG  1 
ATOM   4223  C  CD  . PRO   B 2 206 ? 22.897  18.660  10.036  1.00 91.76  ? 206  PRO   B CD  1 
ATOM   4224  N  N   . TRP   B 2 207 ? 19.231  17.937  8.917   1.00 95.02  ? 207  TRP   B N   1 
ATOM   4225  C  CA  . TRP   B 2 207 ? 17.857  17.922  8.424   1.00 98.48  ? 207  TRP   B CA  1 
ATOM   4226  C  C   . TRP   B 2 207 ? 17.753  18.530  7.023   1.00 104.89 ? 207  TRP   B C   1 
ATOM   4227  O  O   . TRP   B 2 207 ? 18.659  19.231  6.550   1.00 104.93 ? 207  TRP   B O   1 
ATOM   4228  C  CB  . TRP   B 2 207 ? 16.937  18.661  9.388   1.00 102.20 ? 207  TRP   B CB  1 
ATOM   4229  C  CG  . TRP   B 2 207 ? 17.421  20.024  9.827   1.00 102.98 ? 207  TRP   B CG  1 
ATOM   4230  C  CD1 . TRP   B 2 207 ? 18.156  20.326  10.946  1.00 102.18 ? 207  TRP   B CD1 1 
ATOM   4231  C  CD2 . TRP   B 2 207 ? 17.156  21.271  9.177   1.00 101.56 ? 207  TRP   B CD2 1 
ATOM   4232  N  NE1 . TRP   B 2 207 ? 18.374  21.685  11.021  1.00 97.71  ? 207  TRP   B NE1 1 
ATOM   4233  C  CE2 . TRP   B 2 207 ? 17.767  22.284  9.945   1.00 101.56 ? 207  TRP   B CE2 1 
ATOM   4234  C  CE3 . TRP   B 2 207 ? 16.465  21.629  8.015   1.00 99.40  ? 207  TRP   B CE3 1 
ATOM   4235  C  CZ2 . TRP   B 2 207 ? 17.705  23.629  9.581   1.00 100.94 ? 207  TRP   B CZ2 1 
ATOM   4236  C  CZ3 . TRP   B 2 207 ? 16.405  22.961  7.659   1.00 96.78  ? 207  TRP   B CZ3 1 
ATOM   4237  C  CH2 . TRP   B 2 207 ? 17.018  23.944  8.435   1.00 98.02  ? 207  TRP   B CH2 1 
ATOM   4238  N  N   . LYS   B 2 208 ? 16.615  18.272  6.362   1.00 108.95 ? 208  LYS   B N   1 
ATOM   4239  C  CA  . LYS   B 2 208 ? 16.363  18.743  4.998   1.00 103.97 ? 208  LYS   B CA  1 
ATOM   4240  C  C   . LYS   B 2 208 ? 14.863  18.902  4.800   1.00 106.53 ? 208  LYS   B C   1 
ATOM   4241  O  O   . LYS   B 2 208 ? 14.074  18.238  5.471   1.00 116.15 ? 208  LYS   B O   1 
ATOM   4242  C  CB  . LYS   B 2 208 ? 16.922  17.780  3.963   1.00 101.38 ? 208  LYS   B CB  1 
ATOM   4243  C  CG  . LYS   B 2 208 ? 15.937  16.695  3.601   1.00 115.47 ? 208  LYS   B CG  1 
ATOM   4244  C  CD  . LYS   B 2 208 ? 16.594  15.537  2.852   1.00 123.04 ? 208  LYS   B CD  1 
ATOM   4245  C  CE  . LYS   B 2 208 ? 17.560  16.034  1.814   1.00 114.37 ? 208  LYS   B CE  1 
ATOM   4246  N  NZ  . LYS   B 2 208 ? 17.566  15.211  0.588   1.00 111.13 ? 208  LYS   B NZ  1 
ATOM   4247  N  N   . GLN   B 2 209 ? 14.473  19.775  3.867   1.00 104.44 ? 209  GLN   B N   1 
ATOM   4248  C  CA  . GLN   B 2 209 ? 13.078  19.950  3.459   1.00 108.74 ? 209  GLN   B CA  1 
ATOM   4249  C  C   . GLN   B 2 209 ? 13.066  20.196  1.959   1.00 107.81 ? 209  GLN   B C   1 
ATOM   4250  O  O   . GLN   B 2 209 ? 13.656  21.174  1.484   1.00 107.92 ? 209  GLN   B O   1 
ATOM   4251  C  CB  . GLN   B 2 209 ? 12.387  21.117  4.188   1.00 110.20 ? 209  GLN   B CB  1 
ATOM   4252  C  CG  . GLN   B 2 209 ? 10.904  20.868  4.571   1.00 110.96 ? 209  GLN   B CG  1 
ATOM   4253  C  CD  . GLN   B 2 209 ? 9.982   20.605  3.372   1.00 122.33 ? 209  GLN   B CD  1 
ATOM   4254  O  OE1 . GLN   B 2 209 ? 10.401  20.664  2.204   1.00 120.65 ? 209  GLN   B OE1 1 
ATOM   4255  N  NE2 . GLN   B 2 209 ? 8.716   20.312  3.663   1.00 125.82 ? 209  GLN   B NE2 1 
ATOM   4256  N  N   . GLU   B 2 210 ? 12.367  19.330  1.227   1.00 109.47 ? 210  GLU   B N   1 
ATOM   4257  C  CA  . GLU   B 2 210 ? 12.520  19.224  -0.215  1.00 110.81 ? 210  GLU   B CA  1 
ATOM   4258  C  C   . GLU   B 2 210 ? 11.443  19.974  -0.998  1.00 110.38 ? 210  GLU   B C   1 
ATOM   4259  O  O   . GLU   B 2 210 ? 11.240  19.670  -2.174  1.00 118.33 ? 210  GLU   B O   1 
ATOM   4260  C  CB  . GLU   B 2 210 ? 12.548  17.752  -0.640  1.00 114.87 ? 210  GLU   B CB  1 
ATOM   4261  N  N   . ASN   B 2 211 ? 10.757  20.946  -0.402  1.00 107.66 ? 211  ASN   B N   1 
ATOM   4262  C  CA  . ASN   B 2 211 ? 9.979   21.830  -1.268  1.00 110.02 ? 211  ASN   B CA  1 
ATOM   4263  C  C   . ASN   B 2 211 ? 9.523   22.958  -0.358  1.00 114.16 ? 211  ASN   B C   1 
ATOM   4264  O  O   . ASN   B 2 211 ? 8.626   22.763  0.469   1.00 122.44 ? 211  ASN   B O   1 
ATOM   4265  C  CB  . ASN   B 2 211 ? 8.828   21.071  -1.935  1.00 107.83 ? 211  ASN   B CB  1 
ATOM   4266  C  CG  . ASN   B 2 211 ? 9.046   20.888  -3.430  1.00 112.07 ? 211  ASN   B CG  1 
ATOM   4267  O  OD1 . ASN   B 2 211 ? 8.920   21.834  -4.220  1.00 114.27 ? 211  ASN   B OD1 1 
ATOM   4268  N  ND2 . ASN   B 2 211 ? 9.385   19.669  -3.822  1.00 110.91 ? 211  ASN   B ND2 1 
ATOM   4269  N  N   . VAL   B 2 212 ? 10.098  24.145  -0.532  1.00 106.42 ? 212  VAL   B N   1 
ATOM   4270  C  CA  . VAL   B 2 212 ? 9.853   25.266  0.365   1.00 102.36 ? 212  VAL   B CA  1 
ATOM   4271  C  C   . VAL   B 2 212 ? 9.290   26.322  -0.606  1.00 96.31  ? 212  VAL   B C   1 
ATOM   4272  O  O   . VAL   B 2 212 ? 9.156   26.070  -1.802  1.00 100.57 ? 212  VAL   B O   1 
ATOM   4273  C  CB  . VAL   B 2 212 ? 11.020  25.716  1.252   1.00 103.22 ? 212  VAL   B CB  1 
ATOM   4274  C  CG1 . VAL   B 2 212 ? 12.059  26.471  0.428   1.00 94.87  ? 212  VAL   B CG1 1 
ATOM   4275  C  CG2 . VAL   B 2 212 ? 10.503  26.531  2.433   1.00 106.22 ? 212  VAL   B CG2 1 
ATOM   4276  N  N   . GLU   B 2 213 ? 8.930   27.499  -0.071  1.00 95.80  ? 213  GLU   B N   1 
ATOM   4277  C  CA  . GLU   B 2 213 ? 8.332   28.591  -0.844  1.00 94.65  ? 213  GLU   B CA  1 
ATOM   4278  C  C   . GLU   B 2 213 ? 9.031   28.998  -2.161  1.00 92.67  ? 213  GLU   B C   1 
ATOM   4279  O  O   . GLU   B 2 213 ? 10.221  29.308  -2.152  1.00 95.64  ? 213  GLU   B O   1 
ATOM   4280  C  CB  . GLU   B 2 213 ? 8.464   29.917  -0.057  1.00 98.16  ? 213  GLU   B CB  1 
ATOM   4281  C  CG  . GLU   B 2 213 ? 7.409   31.027  -0.345  1.00 96.23  ? 213  GLU   B CG  1 
ATOM   4282  C  CD  . GLU   B 2 213 ? 7.874   32.119  -1.311  1.00 98.13  ? 213  GLU   B CD  1 
ATOM   4283  O  OE1 . GLU   B 2 213 ? 7.513   32.074  -2.509  1.00 100.94 ? 213  GLU   B OE1 1 
ATOM   4284  O  OE2 . GLU   B 2 213 ? 8.605   33.027  -0.865  1.00 99.17  ? 213  GLU   B OE2 1 
ATOM   4285  N  N   . ALA   B 2 214 ? 8.305   29.022  -3.280  1.00 90.94  ? 214  ALA   B N   1 
ATOM   4286  C  CA  . ALA   B 2 214 ? 8.999   29.232  -4.548  1.00 96.52  ? 214  ALA   B CA  1 
ATOM   4287  C  C   . ALA   B 2 214 ? 10.019  30.355  -4.682  1.00 94.58  ? 214  ALA   B C   1 
ATOM   4288  O  O   . ALA   B 2 214 ? 10.945  30.261  -5.497  1.00 95.72  ? 214  ALA   B O   1 
ATOM   4289  C  CB  . ALA   B 2 214 ? 7.956   29.328  -5.659  1.00 96.40  ? 214  ALA   B CB  1 
ATOM   4290  N  N   . GLU   B 2 215 ? 9.857   31.421  -3.919  1.00 98.86  ? 215  GLU   B N   1 
ATOM   4291  C  CA  . GLU   B 2 215 ? 10.763  32.558  -3.927  1.00 99.89  ? 215  GLU   B CA  1 
ATOM   4292  C  C   . GLU   B 2 215 ? 11.388  32.751  -2.559  1.00 100.31 ? 215  GLU   B C   1 
ATOM   4293  O  O   . GLU   B 2 215 ? 11.532  33.875  -2.077  1.00 101.18 ? 215  GLU   B O   1 
ATOM   4294  C  CB  . GLU   B 2 215 ? 10.048  33.835  -4.352  1.00 101.87 ? 215  GLU   B CB  1 
ATOM   4295  C  CG  . GLU   B 2 215 ? 10.229  34.192  -5.792  1.00 103.88 ? 215  GLU   B CG  1 
ATOM   4296  C  CD  . GLU   B 2 215 ? 9.039   34.957  -6.300  1.00 118.16 ? 215  GLU   B CD  1 
ATOM   4297  O  OE1 . GLU   B 2 215 ? 8.661   35.973  -5.655  1.00 124.39 ? 215  GLU   B OE1 1 
ATOM   4298  O  OE2 . GLU   B 2 215 ? 8.463   34.521  -7.326  1.00 123.91 ? 215  GLU   B OE2 1 
ATOM   4299  N  N   . ALA   B 2 216 ? 11.741  31.657  -1.900  1.00 94.92  ? 216  ALA   B N   1 
ATOM   4300  C  CA  . ALA   B 2 216 ? 12.465  31.762  -0.648  1.00 89.04  ? 216  ALA   B CA  1 
ATOM   4301  C  C   . ALA   B 2 216 ? 13.857  32.320  -0.925  1.00 86.81  ? 216  ALA   B C   1 
ATOM   4302  O  O   . ALA   B 2 216 ? 14.499  31.959  -1.914  1.00 85.73  ? 216  ALA   B O   1 
ATOM   4303  C  CB  . ALA   B 2 216 ? 12.536  30.398  0.026   1.00 87.34  ? 216  ALA   B CB  1 
ATOM   4304  N  N   . SER   B 2 217 ? 14.320  33.223  -0.060  1.00 84.83  ? 217  SER   B N   1 
ATOM   4305  C  CA  . SER   B 2 217 ? 15.520  33.982  -0.401  1.00 80.76  ? 217  SER   B CA  1 
ATOM   4306  C  C   . SER   B 2 217 ? 16.393  34.227  0.820   1.00 82.18  ? 217  SER   B C   1 
ATOM   4307  O  O   . SER   B 2 217 ? 17.621  34.247  0.702   1.00 85.87  ? 217  SER   B O   1 
ATOM   4308  C  CB  . SER   B 2 217 ? 15.127  35.204  -1.220  1.00 89.56  ? 217  SER   B CB  1 
ATOM   4309  O  OG  . SER   B 2 217 ? 14.002  35.839  -0.642  1.00 89.06  ? 217  SER   B OG  1 
ATOM   4310  N  N   . MET   B 2 218 ? 15.786  34.407  1.994   1.00 83.71  ? 218  MET   B N   1 
ATOM   4311  C  CA  . MET   B 2 218 ? 16.508  34.680  3.235   1.00 80.97  ? 218  MET   B CA  1 
ATOM   4312  C  C   . MET   B 2 218 ? 16.616  33.496  4.191   1.00 81.89  ? 218  MET   B C   1 
ATOM   4313  O  O   . MET   B 2 218 ? 15.594  32.952  4.616   1.00 86.01  ? 218  MET   B O   1 
ATOM   4314  C  CB  . MET   B 2 218 ? 15.731  35.827  3.886   1.00 79.28  ? 218  MET   B CB  1 
ATOM   4315  C  CG  . MET   B 2 218 ? 16.404  36.472  5.069   1.00 86.48  ? 218  MET   B CG  1 
ATOM   4316  S  SD  . MET   B 2 218 ? 16.036  38.253  5.104   1.00 96.94  ? 218  MET   B SD  1 
ATOM   4317  C  CE  . MET   B 2 218 ? 17.568  38.932  4.417   1.00 91.53  ? 218  MET   B CE  1 
ATOM   4318  N  N   . VAL   B 2 219 ? 17.833  33.077  4.530   1.00 79.09  ? 219  VAL   B N   1 
ATOM   4319  C  CA  . VAL   B 2 219 ? 18.018  32.078  5.579   1.00 78.54  ? 219  VAL   B CA  1 
ATOM   4320  C  C   . VAL   B 2 219 ? 18.550  32.794  6.804   1.00 81.02  ? 219  VAL   B C   1 
ATOM   4321  O  O   . VAL   B 2 219 ? 19.615  33.418  6.758   1.00 82.22  ? 219  VAL   B O   1 
ATOM   4322  C  CB  . VAL   B 2 219 ? 18.948  30.925  5.156   1.00 81.38  ? 219  VAL   B CB  1 
ATOM   4323  C  CG1 . VAL   B 2 219 ? 18.630  30.460  3.749   1.00 84.60  ? 219  VAL   B CG1 1 
ATOM   4324  C  CG2 . VAL   B 2 219 ? 20.415  31.296  5.289   1.00 85.00  ? 219  VAL   B CG2 1 
ATOM   4325  N  N   . ILE   B 2 220 ? 17.793  32.719  7.889   1.00 83.45  ? 220  ILE   B N   1 
ATOM   4326  C  CA  . ILE   B 2 220 ? 18.167  33.281  9.179   1.00 85.23  ? 220  ILE   B CA  1 
ATOM   4327  C  C   . ILE   B 2 220 ? 18.408  32.115  10.122  1.00 85.53  ? 220  ILE   B C   1 
ATOM   4328  O  O   . ILE   B 2 220 ? 17.515  31.280  10.312  1.00 86.29  ? 220  ILE   B O   1 
ATOM   4329  C  CB  . ILE   B 2 220 ? 17.064  34.194  9.733   1.00 84.83  ? 220  ILE   B CB  1 
ATOM   4330  C  CG1 . ILE   B 2 220 ? 17.128  35.574  9.120   1.00 81.25  ? 220  ILE   B CG1 1 
ATOM   4331  C  CG2 . ILE   B 2 220 ? 17.120  34.247  11.243  1.00 87.26  ? 220  ILE   B CG2 1 
ATOM   4332  C  CD1 . ILE   B 2 220 ? 15.797  36.205  9.124   1.00 82.46  ? 220  ILE   B CD1 1 
ATOM   4333  N  N   . ALA   B 2 221 ? 19.593  32.068  10.735  1.00 88.08  ? 221  ALA   B N   1 
ATOM   4334  C  CA  . ALA   B 2 221 ? 19.957  30.988  11.656  1.00 86.23  ? 221  ALA   B CA  1 
ATOM   4335  C  C   . ALA   B 2 221 ? 19.553  31.372  13.071  1.00 86.03  ? 221  ALA   B C   1 
ATOM   4336  O  O   . ALA   B 2 221 ? 20.162  32.259  13.673  1.00 91.06  ? 221  ALA   B O   1 
ATOM   4337  C  CB  . ALA   B 2 221 ? 21.454  30.689  11.590  1.00 86.20  ? 221  ALA   B CB  1 
ATOM   4338  N  N   . VAL   B 2 222 ? 18.550  30.696  13.615  1.00 88.10  ? 222  VAL   B N   1 
ATOM   4339  C  CA  . VAL   B 2 222 ? 18.119  31.051  14.972  1.00 92.53  ? 222  VAL   B CA  1 
ATOM   4340  C  C   . VAL   B 2 222 ? 19.203  30.645  15.962  1.00 93.25  ? 222  VAL   B C   1 
ATOM   4341  O  O   . VAL   B 2 222 ? 19.797  29.563  15.814  1.00 100.08 ? 222  VAL   B O   1 
ATOM   4342  C  CB  . VAL   B 2 222 ? 16.787  30.388  15.308  1.00 92.11  ? 222  VAL   B CB  1 
ATOM   4343  C  CG1 . VAL   B 2 222 ? 16.155  31.099  16.493  1.00 95.82  ? 222  VAL   B CG1 1 
ATOM   4344  C  CG2 . VAL   B 2 222 ? 15.863  30.424  14.107  1.00 88.81  ? 222  VAL   B CG2 1 
ATOM   4345  N  N   . PRO   B 2 223 ? 19.507  31.467  16.959  1.00 93.68  ? 223  PRO   B N   1 
ATOM   4346  C  CA  . PRO   B 2 223 ? 20.590  31.139  17.892  1.00 97.43  ? 223  PRO   B CA  1 
ATOM   4347  C  C   . PRO   B 2 223 ? 20.282  29.993  18.833  1.00 105.81 ? 223  PRO   B C   1 
ATOM   4348  O  O   . PRO   B 2 223 ? 19.217  29.368  18.787  1.00 103.78 ? 223  PRO   B O   1 
ATOM   4349  C  CB  . PRO   B 2 223 ? 20.783  32.438  18.681  1.00 97.16  ? 223  PRO   B CB  1 
ATOM   4350  C  CG  . PRO   B 2 223 ? 20.248  33.485  17.816  1.00 102.40 ? 223  PRO   B CG  1 
ATOM   4351  C  CD  . PRO   B 2 223 ? 19.084  32.864  17.088  1.00 100.50 ? 223  PRO   B CD  1 
ATOM   4352  N  N   . GLU   B 2 224 ? 21.225  29.783  19.744  1.00 112.82 ? 224  GLU   B N   1 
ATOM   4353  C  CA  . GLU   B 2 224 ? 21.267  28.572  20.555  1.00 117.63 ? 224  GLU   B CA  1 
ATOM   4354  C  C   . GLU   B 2 224 ? 19.971  28.230  21.282  1.00 120.48 ? 224  GLU   B C   1 
ATOM   4355  O  O   . GLU   B 2 224 ? 19.646  27.032  21.358  1.00 124.95 ? 224  GLU   B O   1 
ATOM   4356  C  CB  . GLU   B 2 224 ? 22.423  28.693  21.551  1.00 122.61 ? 224  GLU   B CB  1 
ATOM   4357  C  CG  . GLU   B 2 224 ? 23.799  28.690  20.894  1.00 124.97 ? 224  GLU   B CG  1 
ATOM   4358  C  CD  . GLU   B 2 224 ? 24.934  28.884  21.895  1.00 130.87 ? 224  GLU   B CD  1 
ATOM   4359  O  OE1 . GLU   B 2 224 ? 24.649  29.210  23.068  1.00 129.35 ? 224  GLU   B OE1 1 
ATOM   4360  O  OE2 . GLU   B 2 224 ? 26.115  28.718  21.505  1.00 135.66 ? 224  GLU   B OE2 1 
ATOM   4361  N  N   . PRO   B 2 225 ? 19.203  29.180  21.841  1.00 110.38 ? 225  PRO   B N   1 
ATOM   4362  C  CA  . PRO   B 2 225 ? 18.004  28.797  22.609  1.00 106.91 ? 225  PRO   B CA  1 
ATOM   4363  C  C   . PRO   B 2 225 ? 17.060  27.890  21.836  1.00 111.82 ? 225  PRO   B C   1 
ATOM   4364  O  O   . PRO   B 2 225 ? 16.770  26.770  22.272  1.00 113.15 ? 225  PRO   B O   1 
ATOM   4365  C  CB  . PRO   B 2 225 ? 17.343  30.138  22.919  1.00 106.88 ? 225  PRO   B CB  1 
ATOM   4366  C  CG  . PRO   B 2 225 ? 17.891  31.064  21.903  1.00 114.16 ? 225  PRO   B CG  1 
ATOM   4367  C  CD  . PRO   B 2 225 ? 19.307  30.632  21.693  1.00 110.40 ? 225  PRO   B CD  1 
ATOM   4368  N  N   . PHE   B 2 226 ? 16.567  28.350  20.685  1.00 107.91 ? 226  PHE   B N   1 
ATOM   4369  C  CA  . PHE   B 2 226 ? 15.781  27.463  19.829  1.00 105.41 ? 226  PHE   B CA  1 
ATOM   4370  C  C   . PHE   B 2 226 ? 16.695  26.592  18.968  1.00 109.66 ? 226  PHE   B C   1 
ATOM   4371  O  O   . PHE   B 2 226 ? 16.653  25.358  19.049  1.00 114.98 ? 226  PHE   B O   1 
ATOM   4372  C  CB  . PHE   B 2 226 ? 14.839  28.252  18.913  1.00 103.57 ? 226  PHE   B CB  1 
ATOM   4373  C  CG  . PHE   B 2 226 ? 13.972  29.247  19.630  1.00 110.39 ? 226  PHE   B CG  1 
ATOM   4374  C  CD1 . PHE   B 2 226 ? 14.474  30.488  19.989  1.00 109.78 ? 226  PHE   B CD1 1 
ATOM   4375  C  CD2 . PHE   B 2 226 ? 12.640  28.952  19.901  1.00 113.45 ? 226  PHE   B CD2 1 
ATOM   4376  C  CE1 . PHE   B 2 226 ? 13.684  31.404  20.630  1.00 112.13 ? 226  PHE   B CE1 1 
ATOM   4377  C  CE2 . PHE   B 2 226 ? 11.840  29.862  20.542  1.00 114.77 ? 226  PHE   B CE2 1 
ATOM   4378  C  CZ  . PHE   B 2 226 ? 12.358  31.091  20.906  1.00 117.03 ? 226  PHE   B CZ  1 
ATOM   4379  N  N   . GLY   B 2 227 ? 17.520  27.220  18.125  1.00 106.63 ? 227  GLY   B N   1 
ATOM   4380  C  CA  . GLY   B 2 227 ? 18.309  26.502  17.139  1.00 102.18 ? 227  GLY   B CA  1 
ATOM   4381  C  C   . GLY   B 2 227 ? 17.456  26.306  15.909  1.00 99.87  ? 227  GLY   B C   1 
ATOM   4382  O  O   . GLY   B 2 227 ? 16.251  26.248  16.049  1.00 99.36  ? 227  GLY   B O   1 
ATOM   4383  N  N   . GLY   B 2 228 ? 18.050  26.250  14.707  1.00 103.31 ? 228  GLY   B N   1 
ATOM   4384  C  CA  . GLY   B 2 228 ? 17.272  26.104  13.488  1.00 103.02 ? 228  GLY   B CA  1 
ATOM   4385  C  C   . GLY   B 2 228 ? 17.529  27.236  12.508  1.00 102.12 ? 228  GLY   B C   1 
ATOM   4386  O  O   . GLY   B 2 228 ? 18.579  27.890  12.550  1.00 102.10 ? 228  GLY   B O   1 
ATOM   4387  N  N   . ALA   B 2 229 ? 16.541  27.475  11.635  1.00 95.30  ? 229  ALA   B N   1 
ATOM   4388  C  CA  . ALA   B 2 229 ? 16.652  28.499  10.601  1.00 86.63  ? 229  ALA   B CA  1 
ATOM   4389  C  C   . ALA   B 2 229 ? 15.259  28.985  10.225  1.00 90.87  ? 229  ALA   B C   1 
ATOM   4390  O  O   . ALA   B 2 229 ? 14.318  28.190  10.166  1.00 93.07  ? 229  ALA   B O   1 
ATOM   4391  C  CB  . ALA   B 2 229 ? 17.363  27.976  9.352   1.00 87.05  ? 229  ALA   B CB  1 
ATOM   4392  N  N   . ILE   B 2 230 ? 15.136  30.292  10.000  1.00 88.67  ? 230  ILE   B N   1 
ATOM   4393  C  CA  . ILE   B 2 230 ? 13.921  30.922  9.498   1.00 86.12  ? 230  ILE   B CA  1 
ATOM   4394  C  C   . ILE   B 2 230 ? 14.111  31.199  8.014   1.00 91.80  ? 230  ILE   B C   1 
ATOM   4395  O  O   . ILE   B 2 230 ? 14.965  32.010  7.635   1.00 88.27  ? 230  ILE   B O   1 
ATOM   4396  C  CB  . ILE   B 2 230 ? 13.615  32.224  10.241  1.00 84.04  ? 230  ILE   B CB  1 
ATOM   4397  C  CG1 . ILE   B 2 230 ? 13.096  31.917  11.636  1.00 88.04  ? 230  ILE   B CG1 1 
ATOM   4398  C  CG2 . ILE   B 2 230 ? 12.636  33.069  9.445   1.00 85.97  ? 230  ILE   B CG2 1 
ATOM   4399  C  CD1 . ILE   B 2 230 ? 13.129  33.103  12.570  1.00 87.59  ? 230  ILE   B CD1 1 
ATOM   4400  N  N   . ILE   B 2 231 ? 13.308  30.538  7.173   1.00 94.30  ? 231  ILE   B N   1 
ATOM   4401  C  CA  . ILE   B 2 231 ? 13.293  30.775  5.726   1.00 87.47  ? 231  ILE   B CA  1 
ATOM   4402  C  C   . ILE   B 2 231 ? 12.249  31.843  5.414   1.00 88.60  ? 231  ILE   B C   1 
ATOM   4403  O  O   . ILE   B 2 231 ? 11.050  31.624  5.621   1.00 90.70  ? 231  ILE   B O   1 
ATOM   4404  C  CB  . ILE   B 2 231 ? 12.982  29.491  4.950   1.00 89.11  ? 231  ILE   B CB  1 
ATOM   4405  C  CG1 . ILE   B 2 231 ? 13.905  28.374  5.383   1.00 91.64  ? 231  ILE   B CG1 1 
ATOM   4406  C  CG2 . ILE   B 2 231 ? 13.202  29.711  3.495   1.00 84.76  ? 231  ILE   B CG2 1 
ATOM   4407  C  CD1 . ILE   B 2 231 ? 15.320  28.841  5.442   1.00 87.65  ? 231  ILE   B CD1 1 
ATOM   4408  N  N   . ILE   B 2 232 ? 12.690  32.985  4.880   1.00 88.51  ? 232  ILE   B N   1 
ATOM   4409  C  CA  . ILE   B 2 232 ? 11.771  34.050  4.478   1.00 91.17  ? 232  ILE   B CA  1 
ATOM   4410  C  C   . ILE   B 2 232 ? 11.604  34.044  2.961   1.00 90.62  ? 232  ILE   B C   1 
ATOM   4411  O  O   . ILE   B 2 232 ? 12.569  33.825  2.210   1.00 87.58  ? 232  ILE   B O   1 
ATOM   4412  C  CB  . ILE   B 2 232 ? 12.229  35.435  4.975   1.00 84.31  ? 232  ILE   B CB  1 
ATOM   4413  C  CG1 . ILE   B 2 232 ? 12.550  35.382  6.463   1.00 85.17  ? 232  ILE   B CG1 1 
ATOM   4414  C  CG2 . ILE   B 2 232 ? 11.120  36.448  4.732   1.00 86.24  ? 232  ILE   B CG2 1 
ATOM   4415  C  CD1 . ILE   B 2 232 ? 12.408  36.731  7.137   1.00 85.97  ? 232  ILE   B CD1 1 
ATOM   4416  N  N   . GLY   B 2 233 ? 10.369  34.265  2.510   1.00 92.08  ? 233  GLY   B N   1 
ATOM   4417  C  CA  . GLY   B 2 233 ? 10.034  34.299  1.101   1.00 93.83  ? 233  GLY   B CA  1 
ATOM   4418  C  C   . GLY   B 2 233 ? 9.067   35.424  0.774   1.00 98.35  ? 233  GLY   B C   1 
ATOM   4419  O  O   . GLY   B 2 233 ? 8.823   36.299  1.618   1.00 99.66  ? 233  GLY   B O   1 
ATOM   4420  N  N   . GLN   B 2 234 ? 8.505   35.411  -0.442  1.00 99.48  ? 234  GLN   B N   1 
ATOM   4421  C  CA  . GLN   B 2 234 ? 7.620   36.492  -0.869  1.00 100.40 ? 234  GLN   B CA  1 
ATOM   4422  C  C   . GLN   B 2 234 ? 6.394   36.591  0.031   1.00 103.65 ? 234  GLN   B C   1 
ATOM   4423  O  O   . GLN   B 2 234 ? 5.988   37.689  0.437   1.00 109.68 ? 234  GLN   B O   1 
ATOM   4424  C  CB  . GLN   B 2 234 ? 7.204   36.290  -2.326  1.00 93.59  ? 234  GLN   B CB  1 
ATOM   4425  N  N   . GLU   B 2 235 ? 5.794   35.450  0.365   1.00 105.86 ? 235  GLU   B N   1 
ATOM   4426  C  CA  . GLU   B 2 235 ? 4.530   35.444  1.074   1.00 108.66 ? 235  GLU   B CA  1 
ATOM   4427  C  C   . GLU   B 2 235 ? 4.552   34.678  2.383   1.00 105.58 ? 235  GLU   B C   1 
ATOM   4428  O  O   . GLU   B 2 235 ? 3.603   34.807  3.163   1.00 106.45 ? 235  GLU   B O   1 
ATOM   4429  C  CB  . GLU   B 2 235 ? 3.429   34.848  0.187   1.00 113.67 ? 235  GLU   B CB  1 
ATOM   4430  C  CG  . GLU   B 2 235 ? 3.754   33.462  -0.308  1.00 116.57 ? 235  GLU   B CG  1 
ATOM   4431  C  CD  . GLU   B 2 235 ? 2.518   32.686  -0.696  1.00 127.11 ? 235  GLU   B CD  1 
ATOM   4432  O  OE1 . GLU   B 2 235 ? 1.539   32.688  0.096   1.00 129.27 ? 235  GLU   B OE1 1 
ATOM   4433  O  OE2 . GLU   B 2 235 ? 2.528   32.079  -1.794  1.00 131.31 ? 235  GLU   B OE2 1 
ATOM   4434  N  N   . SER   B 2 236 ? 5.591   33.901  2.654   1.00 99.36  ? 236  SER   B N   1 
ATOM   4435  C  CA  . SER   B 2 236 ? 5.616   33.048  3.828   1.00 97.21  ? 236  SER   B CA  1 
ATOM   4436  C  C   . SER   B 2 236 ? 6.899   33.260  4.613   1.00 94.08  ? 236  SER   B C   1 
ATOM   4437  O  O   . SER   B 2 236 ? 7.959   33.513  4.040   1.00 93.03  ? 236  SER   B O   1 
ATOM   4438  C  CB  . SER   B 2 236 ? 5.517   31.599  3.424   1.00 98.54  ? 236  SER   B CB  1 
ATOM   4439  O  OG  . SER   B 2 236 ? 6.630   31.284  2.617   1.00 101.35 ? 236  SER   B OG  1 
ATOM   4440  N  N   . ILE   B 2 237 ? 6.799   33.127  5.932   1.00 93.51  ? 237  ILE   B N   1 
ATOM   4441  C  CA  . ILE   B 2 237 ? 7.953   33.154  6.832   1.00 94.14  ? 237  ILE   B CA  1 
ATOM   4442  C  C   . ILE   B 2 237 ? 7.973   31.806  7.549   1.00 95.52  ? 237  ILE   B C   1 
ATOM   4443  O  O   . ILE   B 2 237 ? 7.215   31.586  8.499   1.00 98.30  ? 237  ILE   B O   1 
ATOM   4444  C  CB  . ILE   B 2 237 ? 7.889   34.317  7.829   1.00 89.90  ? 237  ILE   B CB  1 
ATOM   4445  C  CG1 . ILE   B 2 237 ? 7.930   35.646  7.108   1.00 88.74  ? 237  ILE   B CG1 1 
ATOM   4446  C  CG2 . ILE   B 2 237 ? 9.043   34.269  8.806   1.00 89.61  ? 237  ILE   B CG2 1 
ATOM   4447  C  CD1 . ILE   B 2 237 ? 8.053   36.766  8.047   1.00 89.77  ? 237  ILE   B CD1 1 
ATOM   4448  N  N   . THR   B 2 238 ? 8.819   30.888  7.105   1.00 95.10  ? 238  THR   B N   1 
ATOM   4449  C  CA  . THR   B 2 238 ? 8.803   29.541  7.651   1.00 96.03  ? 238  THR   B CA  1 
ATOM   4450  C  C   . THR   B 2 238 ? 10.025  29.283  8.538   1.00 97.59  ? 238  THR   B C   1 
ATOM   4451  O  O   . THR   B 2 238 ? 11.086  29.902  8.389   1.00 94.55  ? 238  THR   B O   1 
ATOM   4452  C  CB  . THR   B 2 238 ? 8.693   28.493  6.530   1.00 98.16  ? 238  THR   B CB  1 
ATOM   4453  O  OG1 . THR   B 2 238 ? 9.017   27.195  7.044   1.00 100.91 ? 238  THR   B OG1 1 
ATOM   4454  C  CG2 . THR   B 2 238 ? 9.593   28.836  5.321   1.00 104.50 ? 238  THR   B CG2 1 
ATOM   4455  N  N   . TYR   B 2 239 ? 9.837   28.389  9.512   1.00 104.68 ? 239  TYR   B N   1 
ATOM   4456  C  CA  . TYR   B 2 239 ? 10.878  27.960  10.440  1.00 99.78  ? 239  TYR   B CA  1 
ATOM   4457  C  C   . TYR   B 2 239 ? 11.058  26.452  10.322  1.00 101.74 ? 239  TYR   B C   1 
ATOM   4458  O  O   . TYR   B 2 239 ? 10.072  25.707  10.254  1.00 103.08 ? 239  TYR   B O   1 
ATOM   4459  C  CB  . TYR   B 2 239 ? 10.537  28.328  11.880  1.00 95.91  ? 239  TYR   B CB  1 
ATOM   4460  C  CG  . TYR   B 2 239 ? 11.487  27.737  12.893  1.00 99.27  ? 239  TYR   B CG  1 
ATOM   4461  C  CD1 . TYR   B 2 239 ? 11.316  26.440  13.360  1.00 102.87 ? 239  TYR   B CD1 1 
ATOM   4462  C  CD2 . TYR   B 2 239 ? 12.550  28.474  13.389  1.00 95.07  ? 239  TYR   B CD2 1 
ATOM   4463  C  CE1 . TYR   B 2 239 ? 12.176  25.901  14.280  1.00 98.06  ? 239  TYR   B CE1 1 
ATOM   4464  C  CE2 . TYR   B 2 239 ? 13.409  27.945  14.303  1.00 95.37  ? 239  TYR   B CE2 1 
ATOM   4465  C  CZ  . TYR   B 2 239 ? 13.215  26.659  14.744  1.00 98.00  ? 239  TYR   B CZ  1 
ATOM   4466  O  OH  . TYR   B 2 239 ? 14.071  26.121  15.663  1.00 104.29 ? 239  TYR   B OH  1 
ATOM   4467  N  N   . HIS   B 2 240 ? 12.317  26.013  10.285  1.00 101.88 ? 240  HIS   B N   1 
ATOM   4468  C  CA  . HIS   B 2 240 ? 12.687  24.615  10.110  1.00 103.19 ? 240  HIS   B CA  1 
ATOM   4469  C  C   . HIS   B 2 240 ? 13.718  24.242  11.165  1.00 105.06 ? 240  HIS   B C   1 
ATOM   4470  O  O   . HIS   B 2 240 ? 14.700  24.968  11.357  1.00 103.19 ? 240  HIS   B O   1 
ATOM   4471  C  CB  . HIS   B 2 240 ? 13.273  24.348  8.714   1.00 100.61 ? 240  HIS   B CB  1 
ATOM   4472  C  CG  . HIS   B 2 240 ? 12.333  24.635  7.590   1.00 98.72  ? 240  HIS   B CG  1 
ATOM   4473  N  ND1 . HIS   B 2 240 ? 11.534  23.666  7.016   1.00 97.42  ? 240  HIS   B ND1 1 
ATOM   4474  C  CD2 . HIS   B 2 240 ? 12.069  25.787  6.928   1.00 101.84 ? 240  HIS   B CD2 1 
ATOM   4475  C  CE1 . HIS   B 2 240 ? 10.815  24.209  6.049   1.00 105.42 ? 240  HIS   B CE1 1 
ATOM   4476  N  NE2 . HIS   B 2 240 ? 11.121  25.496  5.975   1.00 107.12 ? 240  HIS   B NE2 1 
ATOM   4477  N  N   . ASN   B 2 241 ? 13.504  23.122  11.852  1.00 109.40 ? 241  ASN   B N   1 
ATOM   4478  C  CA  . ASN   B 2 241 ? 14.552  22.576  12.709  1.00 107.91 ? 241  ASN   B CA  1 
ATOM   4479  C  C   . ASN   B 2 241 ? 14.232  21.103  12.880  1.00 114.90 ? 241  ASN   B C   1 
ATOM   4480  O  O   . ASN   B 2 241 ? 13.156  20.774  13.385  1.00 124.14 ? 241  ASN   B O   1 
ATOM   4481  C  CB  . ASN   B 2 241 ? 14.612  23.290  14.049  1.00 99.76  ? 241  ASN   B CB  1 
ATOM   4482  C  CG  . ASN   B 2 241 ? 15.841  22.899  14.848  1.00 103.64 ? 241  ASN   B CG  1 
ATOM   4483  O  OD1 . ASN   B 2 241 ? 16.726  22.203  14.346  1.00 108.05 ? 241  ASN   B OD1 1 
ATOM   4484  N  ND2 . ASN   B 2 241 ? 15.913  23.360  16.094  1.00 103.74 ? 241  ASN   B ND2 1 
ATOM   4485  N  N   . GLY   B 2 242 ? 15.135  20.232  12.441  1.00 111.47 ? 242  GLY   B N   1 
ATOM   4486  C  CA  . GLY   B 2 242 ? 14.874  18.814  12.529  1.00 122.52 ? 242  GLY   B CA  1 
ATOM   4487  C  C   . GLY   B 2 242 ? 13.435  18.463  12.205  1.00 135.41 ? 242  GLY   B C   1 
ATOM   4488  O  O   . GLY   B 2 242 ? 13.058  18.398  11.031  1.00 135.75 ? 242  GLY   B O   1 
ATOM   4489  N  N   . ASP   B 2 243 ? 12.612  18.262  13.228  1.00 153.77 ? 243  ASP   B N   1 
ATOM   4490  C  CA  . ASP   B 2 243 ? 11.224  17.874  13.023  1.00 159.32 ? 243  ASP   B CA  1 
ATOM   4491  C  C   . ASP   B 2 243 ? 10.238  19.020  13.232  1.00 158.70 ? 243  ASP   B C   1 
ATOM   4492  O  O   . ASP   B 2 243 ? 9.080   18.899  12.815  1.00 159.53 ? 243  ASP   B O   1 
ATOM   4493  C  CB  . ASP   B 2 243 ? 10.862  16.715  13.959  1.00 164.41 ? 243  ASP   B CB  1 
ATOM   4494  C  CG  . ASP   B 2 243 ? 11.310  16.973  15.381  1.00 168.27 ? 243  ASP   B CG  1 
ATOM   4495  O  OD1 . ASP   B 2 243 ? 11.711  18.125  15.668  1.00 164.90 ? 243  ASP   B OD1 1 
ATOM   4496  O  OD2 . ASP   B 2 243 ? 11.263  16.021  16.203  1.00 174.85 ? 243  ASP   B OD2 1 
ATOM   4497  N  N   . LYS   B 2 244 ? 10.653  20.120  13.857  1.00 138.27 ? 244  LYS   B N   1 
ATOM   4498  C  CA  . LYS   B 2 244 ? 9.771   21.271  13.973  1.00 130.43 ? 244  LYS   B CA  1 
ATOM   4499  C  C   . LYS   B 2 244 ? 9.628   21.959  12.619  1.00 125.29 ? 244  LYS   B C   1 
ATOM   4500  O  O   . LYS   B 2 244 ? 10.609  22.154  11.891  1.00 119.87 ? 244  LYS   B O   1 
ATOM   4501  C  CB  . LYS   B 2 244 ? 10.293  22.264  15.015  1.00 121.63 ? 244  LYS   B CB  1 
ATOM   4502  N  N   . TYR   B 2 245 ? 8.384   22.319  12.274  1.00 119.12 ? 245  TYR   B N   1 
ATOM   4503  C  CA  . TYR   B 2 245 ? 8.084   23.047  11.037  1.00 114.01 ? 245  TYR   B CA  1 
ATOM   4504  C  C   . TYR   B 2 245 ? 6.902   23.956  11.367  1.00 110.29 ? 245  TYR   B C   1 
ATOM   4505  O  O   . TYR   B 2 245 ? 5.763   23.493  11.432  1.00 113.88 ? 245  TYR   B O   1 
ATOM   4506  C  CB  . TYR   B 2 245 ? 7.780   22.092  9.882   1.00 114.67 ? 245  TYR   B CB  1 
ATOM   4507  C  CG  . TYR   B 2 245 ? 7.096   22.722  8.672   1.00 115.32 ? 245  TYR   B CG  1 
ATOM   4508  C  CD1 . TYR   B 2 245 ? 7.242   24.076  8.394   1.00 114.30 ? 245  TYR   B CD1 1 
ATOM   4509  C  CD2 . TYR   B 2 245 ? 6.310   21.959  7.806   1.00 115.69 ? 245  TYR   B CD2 1 
ATOM   4510  C  CE1 . TYR   B 2 245 ? 6.621   24.662  7.301   1.00 115.94 ? 245  TYR   B CE1 1 
ATOM   4511  C  CE2 . TYR   B 2 245 ? 5.678   22.542  6.698   1.00 122.82 ? 245  TYR   B CE2 1 
ATOM   4512  C  CZ  . TYR   B 2 245 ? 5.841   23.904  6.451   1.00 120.95 ? 245  TYR   B CZ  1 
ATOM   4513  O  OH  . TYR   B 2 245 ? 5.245   24.543  5.375   1.00 117.00 ? 245  TYR   B OH  1 
ATOM   4514  N  N   . LEU   B 2 246 ? 7.183   25.229  11.621  1.00 109.98 ? 246  LEU   B N   1 
ATOM   4515  C  CA  . LEU   B 2 246 ? 6.145   26.214  11.876  1.00 104.86 ? 246  LEU   B CA  1 
ATOM   4516  C  C   . LEU   B 2 246 ? 6.181   27.232  10.746  1.00 103.24 ? 246  LEU   B C   1 
ATOM   4517  O  O   . LEU   B 2 246 ? 7.216   27.868  10.526  1.00 104.20 ? 246  LEU   B O   1 
ATOM   4518  C  CB  . LEU   B 2 246 ? 6.346   26.876  13.236  1.00 99.83  ? 246  LEU   B CB  1 
ATOM   4519  C  CG  . LEU   B 2 246 ? 5.253   27.864  13.615  1.00 110.63 ? 246  LEU   B CG  1 
ATOM   4520  C  CD1 . LEU   B 2 246 ? 3.865   27.423  13.123  1.00 107.60 ? 246  LEU   B CD1 1 
ATOM   4521  C  CD2 . LEU   B 2 246 ? 5.271   28.047  15.119  1.00 114.79 ? 246  LEU   B CD2 1 
ATOM   4522  N  N   . ALA   B 2 247 ? 5.061   27.373  10.023  1.00 100.79 ? 247  ALA   B N   1 
ATOM   4523  C  CA  . ALA   B 2 247 ? 4.960   28.251  8.861   1.00 98.17  ? 247  ALA   B CA  1 
ATOM   4524  C  C   . ALA   B 2 247 ? 3.768   29.201  8.994   1.00 98.60  ? 247  ALA   B C   1 
ATOM   4525  O  O   . ALA   B 2 247 ? 2.659   28.765  9.315   1.00 100.80 ? 247  ALA   B O   1 
ATOM   4526  C  CB  . ALA   B 2 247 ? 4.841   27.438  7.571   1.00 95.21  ? 247  ALA   B CB  1 
ATOM   4527  N  N   . ILE   B 2 248 ? 3.999   30.494  8.726   1.00 98.82  ? 248  ILE   B N   1 
ATOM   4528  C  CA  . ILE   B 2 248 ? 2.967   31.518  8.724   1.00 93.99  ? 248  ILE   B CA  1 
ATOM   4529  C  C   . ILE   B 2 248 ? 2.994   32.263  7.388   1.00 97.59  ? 248  ILE   B C   1 
ATOM   4530  O  O   . ILE   B 2 248 ? 4.001   32.280  6.677   1.00 93.52  ? 248  ILE   B O   1 
ATOM   4531  C  CB  . ILE   B 2 248 ? 3.141   32.510  9.884   1.00 93.21  ? 248  ILE   B CB  1 
ATOM   4532  C  CG1 . ILE   B 2 248 ? 4.350   33.417  9.633   1.00 94.20  ? 248  ILE   B CG1 1 
ATOM   4533  C  CG2 . ILE   B 2 248 ? 3.323   31.761  11.183  1.00 100.15 ? 248  ILE   B CG2 1 
ATOM   4534  C  CD1 . ILE   B 2 248 ? 4.407   34.596  10.557  1.00 99.35  ? 248  ILE   B CD1 1 
ATOM   4535  N  N   . ALA   B 2 249 ? 1.851   32.884  7.050   1.00 100.69 ? 249  ALA   B N   1 
ATOM   4536  C  CA  . ALA   B 2 249 ? 1.717   33.805  5.914   1.00 99.23  ? 249  ALA   B CA  1 
ATOM   4537  C  C   . ALA   B 2 249 ? 1.093   35.108  6.392   1.00 102.99 ? 249  ALA   B C   1 
ATOM   4538  O  O   . ALA   B 2 249 ? -0.114  35.324  6.272   1.00 105.99 ? 249  ALA   B O   1 
ATOM   4539  C  CB  . ALA   B 2 249 ? 0.901   33.190  4.770   1.00 91.15  ? 249  ALA   B CB  1 
ATOM   4540  N  N   . PRO   B 2 250 ? 1.902   36.002  6.933   1.00 104.07 ? 250  PRO   B N   1 
ATOM   4541  C  CA  . PRO   B 2 250 ? 1.400   37.298  7.408   1.00 105.19 ? 250  PRO   B CA  1 
ATOM   4542  C  C   . PRO   B 2 250 ? 0.867   38.111  6.247   1.00 106.38 ? 250  PRO   B C   1 
ATOM   4543  O  O   . PRO   B 2 250 ? 1.584   38.373  5.268   1.00 107.50 ? 250  PRO   B O   1 
ATOM   4544  C  CB  . PRO   B 2 250 ? 2.647   37.954  8.035   1.00 108.11 ? 250  PRO   B CB  1 
ATOM   4545  C  CG  . PRO   B 2 250 ? 3.845   37.216  7.445   1.00 105.53 ? 250  PRO   B CG  1 
ATOM   4546  C  CD  . PRO   B 2 250 ? 3.360   35.846  7.109   1.00 103.91 ? 250  PRO   B CD  1 
ATOM   4547  N  N   . PRO   B 2 251 ? -0.380  38.545  6.335   1.00 106.96 ? 251  PRO   B N   1 
ATOM   4548  C  CA  . PRO   B 2 251 ? -0.915  39.454  5.311   1.00 109.28 ? 251  PRO   B CA  1 
ATOM   4549  C  C   . PRO   B 2 251 ? -0.101  40.723  5.179   1.00 105.92 ? 251  PRO   B C   1 
ATOM   4550  O  O   . PRO   B 2 251 ? 0.099   41.254  4.079   1.00 105.97 ? 251  PRO   B O   1 
ATOM   4551  C  CB  . PRO   B 2 251 ? -2.335  39.766  5.829   1.00 110.37 ? 251  PRO   B CB  1 
ATOM   4552  C  CG  . PRO   B 2 251 ? -2.640  38.670  6.810   1.00 110.34 ? 251  PRO   B CG  1 
ATOM   4553  C  CD  . PRO   B 2 251 ? -1.331  38.290  7.425   1.00 108.78 ? 251  PRO   B CD  1 
ATOM   4554  N  N   . ILE   B 2 252 ? 0.410   41.212  6.300   1.00 104.10 ? 252  ILE   B N   1 
ATOM   4555  C  CA  . ILE   B 2 252 ? 1.067   42.504  6.300   1.00 101.99 ? 252  ILE   B CA  1 
ATOM   4556  C  C   . ILE   B 2 252 ? 2.305   42.479  5.423   1.00 104.59 ? 252  ILE   B C   1 
ATOM   4557  O  O   . ILE   B 2 252 ? 2.652   43.493  4.805   1.00 109.68 ? 252  ILE   B O   1 
ATOM   4558  C  CB  . ILE   B 2 252 ? 1.376   42.908  7.745   1.00 103.06 ? 252  ILE   B CB  1 
ATOM   4559  C  CG1 . ILE   B 2 252 ? 0.103   42.755  8.600   1.00 111.20 ? 252  ILE   B CG1 1 
ATOM   4560  C  CG2 . ILE   B 2 252 ? 1.856   44.339  7.783   1.00 96.30  ? 252  ILE   B CG2 1 
ATOM   4561  C  CD1 . ILE   B 2 252 ? -0.397  41.301  8.870   1.00 104.92 ? 252  ILE   B CD1 1 
ATOM   4562  N  N   . ILE   B 2 253 ? 2.973   41.325  5.316   1.00 102.77 ? 253  ILE   B N   1 
ATOM   4563  C  CA  . ILE   B 2 253 ? 4.223   41.288  4.559   1.00 104.83 ? 253  ILE   B CA  1 
ATOM   4564  C  C   . ILE   B 2 253 ? 4.018   41.151  3.056   1.00 114.20 ? 253  ILE   B C   1 
ATOM   4565  O  O   . ILE   B 2 253 ? 4.983   41.275  2.292   1.00 116.10 ? 253  ILE   B O   1 
ATOM   4566  C  CB  . ILE   B 2 253 ? 5.172   40.144  4.971   1.00 98.64  ? 253  ILE   B CB  1 
ATOM   4567  C  CG1 . ILE   B 2 253 ? 4.828   38.840  4.243   1.00 103.20 ? 253  ILE   B CG1 1 
ATOM   4568  C  CG2 . ILE   B 2 253 ? 5.189   39.988  6.459   1.00 101.64 ? 253  ILE   B CG2 1 
ATOM   4569  C  CD1 . ILE   B 2 253 ? 5.978   37.868  4.224   1.00 95.70  ? 253  ILE   B CD1 1 
ATOM   4570  N  N   . LYS   B 2 254 ? 2.801   40.888  2.596   1.00 110.82 ? 254  LYS   B N   1 
ATOM   4571  C  CA  . LYS   B 2 254 ? 2.610   40.629  1.181   1.00 110.62 ? 254  LYS   B CA  1 
ATOM   4572  C  C   . LYS   B 2 254 ? 2.395   41.904  0.378   1.00 116.28 ? 254  LYS   B C   1 
ATOM   4573  O  O   . LYS   B 2 254 ? 1.874   41.839  -0.737  1.00 119.03 ? 254  LYS   B O   1 
ATOM   4574  C  CB  . LYS   B 2 254 ? 1.450   39.660  0.985   1.00 113.16 ? 254  LYS   B CB  1 
ATOM   4575  C  CG  . LYS   B 2 254 ? 0.160   40.094  1.615   1.00 111.59 ? 254  LYS   B CG  1 
ATOM   4576  C  CD  . LYS   B 2 254 ? -0.888  39.026  1.408   1.00 116.69 ? 254  LYS   B CD  1 
ATOM   4577  C  CE  . LYS   B 2 254 ? -2.292  39.599  1.471   1.00 122.42 ? 254  LYS   B CE  1 
ATOM   4578  N  NZ  . LYS   B 2 254 ? -3.321  38.511  1.456   1.00 128.97 ? 254  LYS   B NZ  1 
ATOM   4579  N  N   . GLN   B 2 255 ? 2.805   43.055  0.903   1.00 129.68 ? 255  GLN   B N   1 
ATOM   4580  C  CA  . GLN   B 2 255 ? 2.763   44.312  0.160   1.00 133.90 ? 255  GLN   B CA  1 
ATOM   4581  C  C   . GLN   B 2 255 ? 4.086   44.661  -0.514  1.00 132.40 ? 255  GLN   B C   1 
ATOM   4582  O  O   . GLN   B 2 255 ? 4.091   45.368  -1.529  1.00 130.01 ? 255  GLN   B O   1 
ATOM   4583  C  CB  . GLN   B 2 255 ? 2.364   45.464  1.092   1.00 133.06 ? 255  GLN   B CB  1 
ATOM   4584  C  CG  . GLN   B 2 255 ? 0.868   45.647  1.251   1.00 135.57 ? 255  GLN   B CG  1 
ATOM   4585  C  CD  . GLN   B 2 255 ? 0.299   46.622  0.241   1.00 136.87 ? 255  GLN   B CD  1 
ATOM   4586  O  OE1 . GLN   B 2 255 ? 1.038   47.241  -0.523  1.00 134.92 ? 255  GLN   B OE1 1 
ATOM   4587  N  NE2 . GLN   B 2 255 ? -1.022  46.768  0.236   1.00 138.33 ? 255  GLN   B NE2 1 
ATOM   4588  N  N   . SER   B 2 256 ? 5.202   44.198  0.043   1.00 120.92 ? 256  SER   B N   1 
ATOM   4589  C  CA  . SER   B 2 256 ? 6.533   44.450  -0.492  1.00 113.78 ? 256  SER   B CA  1 
ATOM   4590  C  C   . SER   B 2 256 ? 7.442   43.343  0.024   1.00 104.78 ? 256  SER   B C   1 
ATOM   4591  O  O   . SER   B 2 256 ? 7.100   42.631  0.972   1.00 98.68  ? 256  SER   B O   1 
ATOM   4592  C  CB  . SER   B 2 256 ? 7.064   45.843  -0.091  1.00 106.22 ? 256  SER   B CB  1 
ATOM   4593  O  OG  . SER   B 2 256 ? 8.358   46.090  -0.638  1.00 98.53  ? 256  SER   B OG  1 
ATOM   4594  N  N   . THR   B 2 257 ? 8.608   43.218  -0.604  1.00 98.49  ? 257  THR   B N   1 
ATOM   4595  C  CA  . THR   B 2 257 ? 9.492   42.088  -0.382  1.00 92.95  ? 257  THR   B CA  1 
ATOM   4596  C  C   . THR   B 2 257 ? 10.498  42.367  0.727   1.00 92.16  ? 257  THR   B C   1 
ATOM   4597  O  O   . THR   B 2 257 ? 11.067  43.459  0.803   1.00 97.25  ? 257  THR   B O   1 
ATOM   4598  C  CB  . THR   B 2 257 ? 10.220  41.755  -1.679  1.00 94.14  ? 257  THR   B CB  1 
ATOM   4599  O  OG1 . THR   B 2 257 ? 9.246   41.547  -2.710  1.00 98.72  ? 257  THR   B OG1 1 
ATOM   4600  C  CG2 . THR   B 2 257 ? 11.068  40.498  -1.499  1.00 98.05  ? 257  THR   B CG2 1 
ATOM   4601  N  N   . ILE   B 2 258 ? 10.722  41.363  1.581   1.00 92.91  ? 258  ILE   B N   1 
ATOM   4602  C  CA  . ILE   B 2 258 ? 11.660  41.478  2.697   1.00 90.04  ? 258  ILE   B CA  1 
ATOM   4603  C  C   . ILE   B 2 258 ? 13.075  41.275  2.170   1.00 89.12  ? 258  ILE   B C   1 
ATOM   4604  O  O   . ILE   B 2 258 ? 13.352  40.313  1.446   1.00 91.92  ? 258  ILE   B O   1 
ATOM   4605  C  CB  . ILE   B 2 258 ? 11.321  40.465  3.811   1.00 89.92  ? 258  ILE   B CB  1 
ATOM   4606  C  CG1 . ILE   B 2 258 ? 9.859   40.585  4.263   1.00 91.33  ? 258  ILE   B CG1 1 
ATOM   4607  C  CG2 . ILE   B 2 258 ? 12.172  40.691  5.036   1.00 86.85  ? 258  ILE   B CG2 1 
ATOM   4608  C  CD1 . ILE   B 2 258 ? 9.553   41.832  5.090   1.00 82.67  ? 258  ILE   B CD1 1 
ATOM   4609  N  N   . VAL   B 2 259 ? 13.972  42.190  2.531   1.00 90.29  ? 259  VAL   B N   1 
ATOM   4610  C  CA  . VAL   B 2 259 ? 15.359  42.155  2.078   1.00 90.21  ? 259  VAL   B CA  1 
ATOM   4611  C  C   . VAL   B 2 259 ? 16.357  42.367  3.204   1.00 91.66  ? 259  VAL   B C   1 
ATOM   4612  O  O   . VAL   B 2 259 ? 17.556  42.118  3.004   1.00 95.06  ? 259  VAL   B O   1 
ATOM   4613  C  CB  . VAL   B 2 259 ? 15.582  43.205  0.963   1.00 90.97  ? 259  VAL   B CB  1 
ATOM   4614  C  CG1 . VAL   B 2 259 ? 15.108  42.664  -0.372  1.00 93.83  ? 259  VAL   B CG1 1 
ATOM   4615  C  CG2 . VAL   B 2 259 ? 14.826  44.482  1.298   1.00 86.34  ? 259  VAL   B CG2 1 
ATOM   4616  N  N   . CYS   B 2 260 ? 15.933  42.839  4.377   1.00 90.63  ? 260  CYS   B N   1 
ATOM   4617  C  CA  . CYS   B 2 260 ? 16.793  43.067  5.528   1.00 90.68  ? 260  CYS   B CA  1 
ATOM   4618  C  C   . CYS   B 2 260 ? 16.370  42.190  6.693   1.00 91.28  ? 260  CYS   B C   1 
ATOM   4619  O  O   . CYS   B 2 260 ? 15.184  41.893  6.878   1.00 91.52  ? 260  CYS   B O   1 
ATOM   4620  C  CB  . CYS   B 2 260 ? 16.720  44.510  6.048   1.00 91.37  ? 260  CYS   B CB  1 
ATOM   4621  S  SG  . CYS   B 2 260 ? 17.201  45.809  4.980   1.00 97.35  ? 260  CYS   B SG  1 
ATOM   4622  N  N   . HIS   B 2 261 ? 17.335  41.878  7.544   1.00 85.33  ? 261  HIS   B N   1 
ATOM   4623  C  CA  . HIS   B 2 261 ? 16.992  41.368  8.853   1.00 83.45  ? 261  HIS   B CA  1 
ATOM   4624  C  C   . HIS   B 2 261 ? 18.162  41.677  9.772   1.00 83.53  ? 261  HIS   B C   1 
ATOM   4625  O  O   . HIS   B 2 261 ? 19.314  41.655  9.337   1.00 87.86  ? 261  HIS   B O   1 
ATOM   4626  C  CB  . HIS   B 2 261 ? 16.714  39.863  8.795   1.00 84.80  ? 261  HIS   B CB  1 
ATOM   4627  C  CG  . HIS   B 2 261 ? 17.957  39.056  8.663   1.00 82.54  ? 261  HIS   B CG  1 
ATOM   4628  N  ND1 . HIS   B 2 261 ? 18.477  38.700  7.439   1.00 88.46  ? 261  HIS   B ND1 1 
ATOM   4629  C  CD2 . HIS   B 2 261 ? 18.826  38.598  9.593   1.00 79.40  ? 261  HIS   B CD2 1 
ATOM   4630  C  CE1 . HIS   B 2 261 ? 19.599  38.026  7.618   1.00 91.43  ? 261  HIS   B CE1 1 
ATOM   4631  N  NE2 . HIS   B 2 261 ? 19.836  37.956  8.917   1.00 88.27  ? 261  HIS   B NE2 1 
ATOM   4632  N  N   . ASN   B 2 262 ? 17.857  42.002  11.022  1.00 80.64  ? 262  ASN   B N   1 
ATOM   4633  C  CA  . ASN   B 2 262 ? 18.858  42.085  12.073  1.00 83.80  ? 262  ASN   B CA  1 
ATOM   4634  C  C   . ASN   B 2 262 ? 18.326  41.339  13.280  1.00 88.06  ? 262  ASN   B C   1 
ATOM   4635  O  O   . ASN   B 2 262 ? 17.115  41.324  13.526  1.00 87.73  ? 262  ASN   B O   1 
ATOM   4636  C  CB  . ASN   B 2 262 ? 19.201  43.533  12.468  1.00 84.78  ? 262  ASN   B CB  1 
ATOM   4637  C  CG  . ASN   B 2 262 ? 20.421  43.620  13.396  1.00 93.02  ? 262  ASN   B CG  1 
ATOM   4638  O  OD1 . ASN   B 2 262 ? 20.307  43.957  14.588  1.00 93.57  ? 262  ASN   B OD1 1 
ATOM   4639  N  ND2 . ASN   B 2 262 ? 21.598  43.309  12.848  1.00 95.47  ? 262  ASN   B ND2 1 
ATOM   4640  N  N   . ARG   B 2 263 ? 19.224  40.693  14.019  1.00 90.36  ? 263  ARG   B N   1 
ATOM   4641  C  CA  . ARG   B 2 263 ? 18.832  40.016  15.249  1.00 92.40  ? 263  ARG   B CA  1 
ATOM   4642  C  C   . ARG   B 2 263 ? 18.884  41.022  16.400  1.00 99.56  ? 263  ARG   B C   1 
ATOM   4643  O  O   . ARG   B 2 263 ? 19.915  41.676  16.625  1.00 99.77  ? 263  ARG   B O   1 
ATOM   4644  C  CB  . ARG   B 2 263 ? 19.720  38.803  15.529  1.00 91.57  ? 263  ARG   B CB  1 
ATOM   4645  C  CG  . ARG   B 2 263 ? 19.030  37.747  16.404  1.00 97.42  ? 263  ARG   B CG  1 
ATOM   4646  C  CD  . ARG   B 2 263 ? 19.979  37.018  17.369  1.00 95.40  ? 263  ARG   B CD  1 
ATOM   4647  N  NE  . ARG   B 2 263 ? 20.972  36.227  16.652  1.00 93.92  ? 263  ARG   B NE  1 
ATOM   4648  C  CZ  . ARG   B 2 263 ? 22.277  36.464  16.670  1.00 91.07  ? 263  ARG   B CZ  1 
ATOM   4649  N  NH1 . ARG   B 2 263 ? 22.790  37.441  17.402  1.00 91.34  ? 263  ARG   B NH1 1 
ATOM   4650  N  NH2 . ARG   B 2 263 ? 23.088  35.704  15.933  1.00 88.63  ? 263  ARG   B NH2 1 
ATOM   4651  N  N   . VAL   B 2 264 ? 17.771  41.163  17.114  1.00 97.66  ? 264  VAL   B N   1 
ATOM   4652  C  CA  . VAL   B 2 264 ? 17.717  42.105  18.219  1.00 97.42  ? 264  VAL   B CA  1 
ATOM   4653  C  C   . VAL   B 2 264 ? 18.242  41.629  19.560  1.00 105.65 ? 264  VAL   B C   1 
ATOM   4654  O  O   . VAL   B 2 264 ? 19.127  42.261  20.140  1.00 108.88 ? 264  VAL   B O   1 
ATOM   4655  C  CB  . VAL   B 2 264 ? 16.273  42.536  18.496  1.00 101.92 ? 264  VAL   B CB  1 
ATOM   4656  C  CG1 . VAL   B 2 264 ? 16.129  42.987  19.934  1.00 107.29 ? 264  VAL   B CG1 1 
ATOM   4657  C  CG2 . VAL   B 2 264 ? 15.870  43.647  17.505  1.00 100.51 ? 264  VAL   B CG2 1 
ATOM   4658  N  N   . ASP   B 2 265 ? 17.715  40.496  20.052  1.00 113.32 ? 265  ASP   B N   1 
ATOM   4659  C  CA  . ASP   B 2 265 ? 18.105  39.974  21.356  1.00 117.65 ? 265  ASP   B CA  1 
ATOM   4660  C  C   . ASP   B 2 265 ? 19.103  38.859  21.030  1.00 118.50 ? 265  ASP   B C   1 
ATOM   4661  O  O   . ASP   B 2 265 ? 18.895  38.089  20.085  1.00 115.57 ? 265  ASP   B O   1 
ATOM   4662  C  CB  . ASP   B 2 265 ? 16.935  39.413  22.184  1.00 119.61 ? 265  ASP   B CB  1 
ATOM   4663  C  CG  . ASP   B 2 265 ? 15.930  38.611  21.341  1.00 120.93 ? 265  ASP   B CG  1 
ATOM   4664  O  OD1 . ASP   B 2 265 ? 16.388  37.770  20.523  1.00 119.15 ? 265  ASP   B OD1 1 
ATOM   4665  O  OD2 . ASP   B 2 265 ? 14.692  38.817  21.512  1.00 122.36 ? 265  ASP   B OD2 1 
ATOM   4666  N  N   . PRO   B 2 266 ? 20.205  38.765  21.781  1.00 117.79 ? 266  PRO   B N   1 
ATOM   4667  C  CA  . PRO   B 2 266 ? 21.181  37.695  21.511  1.00 114.35 ? 266  PRO   B CA  1 
ATOM   4668  C  C   . PRO   B 2 266 ? 20.582  36.296  21.520  1.00 113.76 ? 266  PRO   B C   1 
ATOM   4669  O  O   . PRO   B 2 266 ? 21.129  35.397  20.864  1.00 112.10 ? 266  PRO   B O   1 
ATOM   4670  C  CB  . PRO   B 2 266 ? 22.211  37.884  22.629  1.00 115.80 ? 266  PRO   B CB  1 
ATOM   4671  C  CG  . PRO   B 2 266 ? 22.170  39.384  22.903  1.00 113.73 ? 266  PRO   B CG  1 
ATOM   4672  C  CD  . PRO   B 2 266 ? 20.725  39.774  22.727  1.00 114.90 ? 266  PRO   B CD  1 
ATOM   4673  N  N   . ASN   B 2 267 ? 19.475  36.069  22.234  1.00 116.96 ? 267  ASN   B N   1 
ATOM   4674  C  CA  . ASN   B 2 267 ? 18.841  34.752  22.191  1.00 112.46 ? 267  ASN   B CA  1 
ATOM   4675  C  C   . ASN   B 2 267 ? 18.055  34.522  20.902  1.00 108.54 ? 267  ASN   B C   1 
ATOM   4676  O  O   . ASN   B 2 267 ? 17.688  33.384  20.613  1.00 105.08 ? 267  ASN   B O   1 
ATOM   4677  C  CB  . ASN   B 2 267 ? 17.911  34.568  23.393  1.00 113.88 ? 267  ASN   B CB  1 
ATOM   4678  C  CG  . ASN   B 2 267 ? 16.683  35.469  23.320  1.00 117.18 ? 267  ASN   B CG  1 
ATOM   4679  O  OD1 . ASN   B 2 267 ? 15.830  35.307  22.439  1.00 116.49 ? 267  ASN   B OD1 1 
ATOM   4680  N  ND2 . ASN   B 2 267 ? 16.584  36.422  24.247  1.00 116.10 ? 267  ASN   B ND2 1 
ATOM   4681  N  N   . GLY   B 2 268 ? 17.757  35.572  20.140  1.00 110.27 ? 268  GLY   B N   1 
ATOM   4682  C  CA  . GLY   B 2 268 ? 17.155  35.397  18.828  1.00 106.34 ? 268  GLY   B CA  1 
ATOM   4683  C  C   . GLY   B 2 268 ? 15.668  35.098  18.769  1.00 104.55 ? 268  GLY   B C   1 
ATOM   4684  O  O   . GLY   B 2 268 ? 15.237  34.255  17.976  1.00 102.92 ? 268  GLY   B O   1 
ATOM   4685  N  N   . SER   B 2 269 ? 14.865  35.789  19.585  1.00 106.41 ? 269  SER   B N   1 
ATOM   4686  C  CA  . SER   B 2 269 ? 13.412  35.690  19.540  1.00 103.80 ? 269  SER   B CA  1 
ATOM   4687  C  C   . SER   B 2 269 ? 12.758  36.982  19.071  1.00 105.42 ? 269  SER   B C   1 
ATOM   4688  O  O   . SER   B 2 269 ? 11.527  37.058  19.036  1.00 102.93 ? 269  SER   B O   1 
ATOM   4689  C  CB  . SER   B 2 269 ? 12.877  35.294  20.912  1.00 107.33 ? 269  SER   B CB  1 
ATOM   4690  O  OG  . SER   B 2 269 ? 13.377  36.187  21.891  1.00 113.00 ? 269  SER   B OG  1 
ATOM   4691  N  N   . ARG   B 2 270 ? 13.560  37.998  18.724  1.00 108.45 ? 270  ARG   B N   1 
ATOM   4692  C  CA  . ARG   B 2 270 ? 13.097  39.203  18.031  1.00 101.61 ? 270  ARG   B CA  1 
ATOM   4693  C  C   . ARG   B 2 270 ? 14.072  39.563  16.914  1.00 95.21  ? 270  ARG   B C   1 
ATOM   4694  O  O   . ARG   B 2 270 ? 15.260  39.795  17.165  1.00 92.61  ? 270  ARG   B O   1 
ATOM   4695  C  CB  . ARG   B 2 270 ? 12.928  40.372  19.002  1.00 105.00 ? 270  ARG   B CB  1 
ATOM   4696  C  CG  . ARG   B 2 270 ? 11.777  40.146  19.942  1.00 111.62 ? 270  ARG   B CG  1 
ATOM   4697  C  CD  . ARG   B 2 270 ? 11.434  41.404  20.656  1.00 115.76 ? 270  ARG   B CD  1 
ATOM   4698  N  NE  . ARG   B 2 270 ? 12.541  41.851  21.487  1.00 123.48 ? 270  ARG   B NE  1 
ATOM   4699  C  CZ  . ARG   B 2 270 ? 12.731  41.419  22.726  1.00 136.62 ? 270  ARG   B CZ  1 
ATOM   4700  N  NH1 . ARG   B 2 270 ? 11.907  40.546  23.283  1.00 145.57 ? 270  ARG   B NH1 1 
ATOM   4701  N  NH2 . ARG   B 2 270 ? 13.762  41.884  23.429  1.00 133.32 ? 270  ARG   B NH2 1 
ATOM   4702  N  N   . TYR   B 2 271 ? 13.560  39.587  15.680  1.00 90.60  ? 271  TYR   B N   1 
ATOM   4703  C  CA  . TYR   B 2 271 ? 14.300  39.932  14.470  1.00 89.02  ? 271  TYR   B CA  1 
ATOM   4704  C  C   . TYR   B 2 271 ? 13.639  41.146  13.820  1.00 91.84  ? 271  TYR   B C   1 
ATOM   4705  O  O   . TYR   B 2 271 ? 12.416  41.163  13.651  1.00 93.27  ? 271  TYR   B O   1 
ATOM   4706  C  CB  . TYR   B 2 271 ? 14.309  38.745  13.480  1.00 89.62  ? 271  TYR   B CB  1 
ATOM   4707  C  CG  . TYR   B 2 271 ? 15.247  37.606  13.847  1.00 92.10  ? 271  TYR   B CG  1 
ATOM   4708  C  CD1 . TYR   B 2 271 ? 16.572  37.611  13.423  1.00 90.92  ? 271  TYR   B CD1 1 
ATOM   4709  C  CD2 . TYR   B 2 271 ? 14.820  36.537  14.638  1.00 90.09  ? 271  TYR   B CD2 1 
ATOM   4710  C  CE1 . TYR   B 2 271 ? 17.451  36.583  13.779  1.00 94.63  ? 271  TYR   B CE1 1 
ATOM   4711  C  CE2 . TYR   B 2 271 ? 15.687  35.506  14.989  1.00 90.66  ? 271  TYR   B CE2 1 
ATOM   4712  C  CZ  . TYR   B 2 271 ? 17.003  35.527  14.557  1.00 95.32  ? 271  TYR   B CZ  1 
ATOM   4713  O  OH  . TYR   B 2 271 ? 17.872  34.494  14.894  1.00 94.74  ? 271  TYR   B OH  1 
ATOM   4714  N  N   . LEU   B 2 272 ? 14.423  42.165  13.462  1.00 91.43  ? 272  LEU   B N   1 
ATOM   4715  C  CA  . LEU   B 2 272 ? 13.891  43.258  12.652  1.00 83.20  ? 272  LEU   B CA  1 
ATOM   4716  C  C   . LEU   B 2 272 ? 13.876  42.850  11.193  1.00 85.18  ? 272  LEU   B C   1 
ATOM   4717  O  O   . LEU   B 2 272 ? 14.803  42.195  10.715  1.00 87.68  ? 272  LEU   B O   1 
ATOM   4718  C  CB  . LEU   B 2 272 ? 14.728  44.515  12.789  1.00 81.34  ? 272  LEU   B CB  1 
ATOM   4719  C  CG  . LEU   B 2 272 ? 14.708  45.208  14.124  1.00 85.94  ? 272  LEU   B CG  1 
ATOM   4720  C  CD1 . LEU   B 2 272 ? 15.624  46.394  13.994  1.00 81.24  ? 272  LEU   B CD1 1 
ATOM   4721  C  CD2 . LEU   B 2 272 ? 13.286  45.622  14.416  1.00 89.39  ? 272  LEU   B CD2 1 
ATOM   4722  N  N   . LEU   B 2 273 ? 12.842  43.259  10.472  1.00 86.59  ? 273  LEU   B N   1 
ATOM   4723  C  CA  . LEU   B 2 273 ? 12.748  42.944  9.053   1.00 87.26  ? 273  LEU   B CA  1 
ATOM   4724  C  C   . LEU   B 2 273 ? 12.399  44.197  8.266   1.00 85.82  ? 273  LEU   B C   1 
ATOM   4725  O  O   . LEU   B 2 273 ? 11.554  44.988  8.690   1.00 85.91  ? 273  LEU   B O   1 
ATOM   4726  C  CB  . LEU   B 2 273 ? 11.698  41.850  8.793   1.00 86.91  ? 273  LEU   B CB  1 
ATOM   4727  C  CG  . LEU   B 2 273 ? 11.993  40.441  9.315   1.00 84.73  ? 273  LEU   B CG  1 
ATOM   4728  C  CD1 . LEU   B 2 273 ? 10.962  39.401  8.826   1.00 80.95  ? 273  LEU   B CD1 1 
ATOM   4729  C  CD2 . LEU   B 2 273 ? 13.416  40.051  8.920   1.00 85.52  ? 273  LEU   B CD2 1 
ATOM   4730  N  N   . GLY   B 2 274 ? 13.039  44.369  7.120   1.00 87.36  ? 274  GLY   B N   1 
ATOM   4731  C  CA  . GLY   B 2 274 ? 12.753  45.502  6.252   1.00 90.88  ? 274  GLY   B CA  1 
ATOM   4732  C  C   . GLY   B 2 274 ? 12.493  45.088  4.818   1.00 88.48  ? 274  GLY   B C   1 
ATOM   4733  O  O   . GLY   B 2 274 ? 13.124  44.168  4.303   1.00 86.28  ? 274  GLY   B O   1 
ATOM   4734  N  N   . ASP   B 2 275 ? 11.557  45.790  4.170   1.00 89.42  ? 275  ASP   B N   1 
ATOM   4735  C  CA  . ASP   B 2 275 ? 11.237  45.528  2.774   1.00 90.15  ? 275  ASP   B CA  1 
ATOM   4736  C  C   . ASP   B 2 275 ? 11.824  46.608  1.867   1.00 91.66  ? 275  ASP   B C   1 
ATOM   4737  O  O   . ASP   B 2 275 ? 12.674  47.415  2.266   1.00 91.71  ? 275  ASP   B O   1 
ATOM   4738  C  CB  . ASP   B 2 275 ? 9.722   45.408  2.567   1.00 92.90  ? 275  ASP   B CB  1 
ATOM   4739  C  CG  . ASP   B 2 275 ? 8.975   46.715  2.820   1.00 94.80  ? 275  ASP   B CG  1 
ATOM   4740  O  OD1 . ASP   B 2 275 ? 9.631   47.727  3.186   1.00 92.75  ? 275  ASP   B OD1 1 
ATOM   4741  O  OD2 . ASP   B 2 275 ? 7.725   46.710  2.662   1.00 96.21  ? 275  ASP   B OD2 1 
ATOM   4742  N  N   . MET   B 2 276 ? 11.368  46.633  0.623   1.00 92.29  ? 276  MET   B N   1 
ATOM   4743  C  CA  . MET   B 2 276 ? 11.911  47.569  -0.340  1.00 90.86  ? 276  MET   B CA  1 
ATOM   4744  C  C   . MET   B 2 276 ? 11.115  48.842  -0.413  1.00 89.08  ? 276  MET   B C   1 
ATOM   4745  O  O   . MET   B 2 276 ? 11.396  49.675  -1.271  1.00 92.41  ? 276  MET   B O   1 
ATOM   4746  C  CB  . MET   B 2 276 ? 11.971  46.929  -1.716  1.00 95.64  ? 276  MET   B CB  1 
ATOM   4747  C  CG  . MET   B 2 276 ? 12.489  45.508  -1.704  1.00 94.55  ? 276  MET   B CG  1 
ATOM   4748  S  SD  . MET   B 2 276 ? 12.433  44.845  -3.381  1.00 92.58  ? 276  MET   B SD  1 
ATOM   4749  C  CE  . MET   B 2 276 ? 10.668  44.983  -3.735  1.00 90.37  ? 276  MET   B CE  1 
ATOM   4750  N  N   . GLU   B 2 277 ? 10.122  49.012  0.453   1.00 91.02  ? 277  GLU   B N   1 
ATOM   4751  C  CA  . GLU   B 2 277 ? 9.348   50.245  0.489   1.00 92.98  ? 277  GLU   B CA  1 
ATOM   4752  C  C   . GLU   B 2 277 ? 9.440   50.926  1.854   1.00 95.03  ? 277  GLU   B C   1 
ATOM   4753  O  O   . GLU   B 2 277 ? 8.554   51.712  2.221   1.00 99.88  ? 277  GLU   B O   1 
ATOM   4754  C  CB  . GLU   B 2 277 ? 7.891   49.968  0.110   1.00 96.48  ? 277  GLU   B CB  1 
ATOM   4755  C  CG  . GLU   B 2 277 ? 7.699   49.256  -1.234  1.00 98.40  ? 277  GLU   B CG  1 
ATOM   4756  C  CD  . GLU   B 2 277 ? 6.241   48.868  -1.503  1.00 110.04 ? 277  GLU   B CD  1 
ATOM   4757  O  OE1 . GLU   B 2 277 ? 5.369   49.263  -0.695  1.00 114.36 ? 277  GLU   B OE1 1 
ATOM   4758  O  OE2 . GLU   B 2 277 ? 5.965   48.169  -2.512  1.00 114.97 ? 277  GLU   B OE2 1 
ATOM   4759  N  N   . GLY   B 2 278 ? 10.487  50.632  2.625   1.00 91.21  ? 278  GLY   B N   1 
ATOM   4760  C  CA  . GLY   B 2 278 ? 10.702  51.302  3.886   1.00 87.85  ? 278  GLY   B CA  1 
ATOM   4761  C  C   . GLY   B 2 278 ? 9.830   50.839  5.028   1.00 90.66  ? 278  GLY   B C   1 
ATOM   4762  O  O   . GLY   B 2 278 ? 9.896   51.434  6.112   1.00 91.19  ? 278  GLY   B O   1 
ATOM   4763  N  N   . ARG   B 2 279 ? 9.018   49.804  4.837   1.00 91.45  ? 279  ARG   B N   1 
ATOM   4764  C  CA  . ARG   B 2 279 ? 8.340   49.203  5.975   1.00 90.92  ? 279  ARG   B CA  1 
ATOM   4765  C  C   . ARG   B 2 279 ? 9.346   48.500  6.881   1.00 91.07  ? 279  ARG   B C   1 
ATOM   4766  O  O   . ARG   B 2 279 ? 10.282  47.841  6.414   1.00 88.26  ? 279  ARG   B O   1 
ATOM   4767  C  CB  . ARG   B 2 279 ? 7.243   48.243  5.505   1.00 85.21  ? 279  ARG   B CB  1 
ATOM   4768  C  CG  . ARG   B 2 279 ? 6.121   49.007  4.816   1.00 91.50  ? 279  ARG   B CG  1 
ATOM   4769  C  CD  . ARG   B 2 279 ? 4.971   48.168  4.357   1.00 88.33  ? 279  ARG   B CD  1 
ATOM   4770  N  NE  . ARG   B 2 279 ? 3.994   48.982  3.654   1.00 99.91  ? 279  ARG   B NE  1 
ATOM   4771  C  CZ  . ARG   B 2 279 ? 2.928   48.501  3.035   1.00 104.20 ? 279  ARG   B CZ  1 
ATOM   4772  N  NH1 . ARG   B 2 279 ? 2.655   47.207  3.033   1.00 107.83 ? 279  ARG   B NH1 1 
ATOM   4773  N  NH2 . ARG   B 2 279 ? 2.129   49.334  2.381   1.00 108.94 ? 279  ARG   B NH2 1 
ATOM   4774  N  N   . LEU   B 2 280 ? 9.179   48.704  8.187   1.00 91.08  ? 280  LEU   B N   1 
ATOM   4775  C  CA  . LEU   B 2 280 ? 10.023  48.116  9.220   1.00 88.95  ? 280  LEU   B CA  1 
ATOM   4776  C  C   . LEU   B 2 280 ? 9.182   47.138  10.030  1.00 90.37  ? 280  LEU   B C   1 
ATOM   4777  O  O   . LEU   B 2 280 ? 8.202   47.536  10.670  1.00 92.01  ? 280  LEU   B O   1 
ATOM   4778  C  CB  . LEU   B 2 280 ? 10.614  49.192  10.134  1.00 88.62  ? 280  LEU   B CB  1 
ATOM   4779  C  CG  . LEU   B 2 280 ? 11.457  48.648  11.285  1.00 89.69  ? 280  LEU   B CG  1 
ATOM   4780  C  CD1 . LEU   B 2 280 ? 12.458  47.617  10.775  1.00 81.64  ? 280  LEU   B CD1 1 
ATOM   4781  C  CD2 . LEU   B 2 280 ? 12.154  49.791  11.996  1.00 83.46  ? 280  LEU   B CD2 1 
ATOM   4782  N  N   . PHE   B 2 281 ? 9.556   45.869  9.999   1.00 90.54  ? 281  PHE   B N   1 
ATOM   4783  C  CA  . PHE   B 2 281 ? 8.802   44.830  10.672  1.00 91.51  ? 281  PHE   B CA  1 
ATOM   4784  C  C   . PHE   B 2 281 ? 9.593   44.264  11.842  1.00 96.69  ? 281  PHE   B C   1 
ATOM   4785  O  O   . PHE   B 2 281 ? 10.830  44.295  11.868  1.00 94.86  ? 281  PHE   B O   1 
ATOM   4786  C  CB  . PHE   B 2 281 ? 8.450   43.697  9.716   1.00 86.23  ? 281  PHE   B CB  1 
ATOM   4787  C  CG  . PHE   B 2 281 ? 7.460   44.076  8.666   1.00 90.77  ? 281  PHE   B CG  1 
ATOM   4788  C  CD1 . PHE   B 2 281 ? 6.099   43.980  8.918   1.00 94.42  ? 281  PHE   B CD1 1 
ATOM   4789  C  CD2 . PHE   B 2 281 ? 7.878   44.508  7.417   1.00 85.19  ? 281  PHE   B CD2 1 
ATOM   4790  C  CE1 . PHE   B 2 281 ? 5.168   44.308  7.941   1.00 94.55  ? 281  PHE   B CE1 1 
ATOM   4791  C  CE2 . PHE   B 2 281 ? 6.953   44.835  6.443   1.00 89.59  ? 281  PHE   B CE2 1 
ATOM   4792  C  CZ  . PHE   B 2 281 ? 5.593   44.734  6.707   1.00 91.93  ? 281  PHE   B CZ  1 
ATOM   4793  N  N   . MET   B 2 282 ? 8.842   43.748  12.819  1.00 102.84 ? 282  MET   B N   1 
ATOM   4794  C  CA  . MET   B 2 282 ? 9.376   42.948  13.916  1.00 100.43 ? 282  MET   B CA  1 
ATOM   4795  C  C   . MET   B 2 282 ? 8.753   41.556  13.879  1.00 100.06 ? 282  MET   B C   1 
ATOM   4796  O  O   . MET   B 2 282 ? 7.524   41.425  13.870  1.00 103.35 ? 282  MET   B O   1 
ATOM   4797  C  CB  . MET   B 2 282 ? 9.101   43.597  15.268  1.00 99.84  ? 282  MET   B CB  1 
ATOM   4798  C  CG  . MET   B 2 282 ? 9.412   42.644  16.368  1.00 98.08  ? 282  MET   B CG  1 
ATOM   4799  S  SD  . MET   B 2 282 ? 10.930  43.106  17.129  1.00 105.69 ? 282  MET   B SD  1 
ATOM   4800  C  CE  . MET   B 2 282 ? 10.245  44.276  18.310  1.00 118.66 ? 282  MET   B CE  1 
ATOM   4801  N  N   . LEU   B 2 283 ? 9.599   40.524  13.853  1.00 96.51  ? 283  LEU   B N   1 
ATOM   4802  C  CA  . LEU   B 2 283 ? 9.183   39.124  13.922  1.00 95.94  ? 283  LEU   B CA  1 
ATOM   4803  C  C   . LEU   B 2 283 ? 9.543   38.586  15.305  1.00 99.71  ? 283  LEU   B C   1 
ATOM   4804  O  O   . LEU   B 2 283 ? 10.715  38.628  15.704  1.00 101.34 ? 283  LEU   B O   1 
ATOM   4805  C  CB  . LEU   B 2 283 ? 9.858   38.310  12.815  1.00 89.94  ? 283  LEU   B CB  1 
ATOM   4806  C  CG  . LEU   B 2 283 ? 10.077  36.794  12.900  1.00 89.08  ? 283  LEU   B CG  1 
ATOM   4807  C  CD1 . LEU   B 2 283 ? 8.776   36.016  12.753  1.00 95.27  ? 283  LEU   B CD1 1 
ATOM   4808  C  CD2 . LEU   B 2 283 ? 11.094  36.338  11.851  1.00 87.50  ? 283  LEU   B CD2 1 
ATOM   4809  N  N   . LEU   B 2 284 ? 8.542   38.104  16.046  1.00 100.70 ? 284  LEU   B N   1 
ATOM   4810  C  CA  . LEU   B 2 284 ? 8.732   37.655  17.423  1.00 102.09 ? 284  LEU   B CA  1 
ATOM   4811  C  C   . LEU   B 2 284 ? 8.593   36.141  17.482  1.00 102.19 ? 284  LEU   B C   1 
ATOM   4812  O  O   . LEU   B 2 284 ? 7.558   35.597  17.081  1.00 107.02 ? 284  LEU   B O   1 
ATOM   4813  C  CB  . LEU   B 2 284 ? 7.732   38.317  18.369  1.00 100.42 ? 284  LEU   B CB  1 
ATOM   4814  C  CG  . LEU   B 2 284 ? 7.855   39.828  18.464  1.00 101.72 ? 284  LEU   B CG  1 
ATOM   4815  C  CD1 . LEU   B 2 284 ? 7.121   40.412  17.297  1.00 105.33 ? 284  LEU   B CD1 1 
ATOM   4816  C  CD2 . LEU   B 2 284 ? 7.246   40.335  19.732  1.00 113.75 ? 284  LEU   B CD2 1 
ATOM   4817  N  N   . LEU   B 2 285 ? 9.636   35.469  17.964  1.00 100.43 ? 285  LEU   B N   1 
ATOM   4818  C  CA  . LEU   B 2 285 ? 9.587   34.021  18.139  1.00 106.40 ? 285  LEU   B CA  1 
ATOM   4819  C  C   . LEU   B 2 285 ? 8.930   33.728  19.480  1.00 117.10 ? 285  LEU   B C   1 
ATOM   4820  O  O   . LEU   B 2 285 ? 9.555   33.871  20.535  1.00 119.38 ? 285  LEU   B O   1 
ATOM   4821  C  CB  . LEU   B 2 285 ? 10.980  33.406  18.053  1.00 107.79 ? 285  LEU   B CB  1 
ATOM   4822  C  CG  . LEU   B 2 285 ? 11.674  33.372  16.686  1.00 105.56 ? 285  LEU   B CG  1 
ATOM   4823  C  CD1 . LEU   B 2 285 ? 12.570  32.166  16.544  1.00 97.55  ? 285  LEU   B CD1 1 
ATOM   4824  C  CD2 . LEU   B 2 285 ? 10.675  33.365  15.578  1.00 99.72  ? 285  LEU   B CD2 1 
ATOM   4825  N  N   . GLU   B 2 286 ? 7.656   33.328  19.441  1.00 129.53 ? 286  GLU   B N   1 
ATOM   4826  C  CA  . GLU   B 2 286 ? 6.916   33.007  20.658  1.00 132.07 ? 286  GLU   B CA  1 
ATOM   4827  C  C   . GLU   B 2 286 ? 7.432   31.686  21.225  1.00 133.14 ? 286  GLU   B C   1 
ATOM   4828  O  O   . GLU   B 2 286 ? 7.308   30.634  20.587  1.00 132.82 ? 286  GLU   B O   1 
ATOM   4829  C  CB  . GLU   B 2 286 ? 5.411   32.940  20.369  1.00 134.35 ? 286  GLU   B CB  1 
ATOM   4830  C  CG  . GLU   B 2 286 ? 4.619   34.254  20.645  1.00 139.45 ? 286  GLU   B CG  1 
ATOM   4831  C  CD  . GLU   B 2 286 ? 3.583   34.633  19.548  1.00 142.65 ? 286  GLU   B CD  1 
ATOM   4832  O  OE1 . GLU   B 2 286 ? 3.559   35.817  19.135  1.00 137.16 ? 286  GLU   B OE1 1 
ATOM   4833  O  OE2 . GLU   B 2 286 ? 2.783   33.772  19.108  1.00 144.30 ? 286  GLU   B OE2 1 
ATOM   4834  N  N   . LYS   B 2 287 ? 8.030   31.746  22.412  1.00 132.66 ? 287  LYS   B N   1 
ATOM   4835  C  CA  . LYS   B 2 287 ? 8.733   30.613  22.997  1.00 136.18 ? 287  LYS   B CA  1 
ATOM   4836  C  C   . LYS   B 2 287 ? 7.857   29.905  24.020  1.00 143.41 ? 287  LYS   B C   1 
ATOM   4837  O  O   . LYS   B 2 287 ? 6.920   30.483  24.579  1.00 146.74 ? 287  LYS   B O   1 
ATOM   4838  C  CB  . LYS   B 2 287 ? 10.045  31.064  23.657  1.00 132.55 ? 287  LYS   B CB  1 
ATOM   4839  N  N   . GLU   B 2 288 ? 8.184   28.636  24.259  1.00 149.93 ? 288  GLU   B N   1 
ATOM   4840  C  CA  . GLU   B 2 288 ? 7.430   27.757  25.150  1.00 152.53 ? 288  GLU   B CA  1 
ATOM   4841  C  C   . GLU   B 2 288 ? 8.407   27.192  26.175  1.00 154.34 ? 288  GLU   B C   1 
ATOM   4842  O  O   . GLU   B 2 288 ? 9.200   26.306  25.840  1.00 154.56 ? 288  GLU   B O   1 
ATOM   4843  C  CB  . GLU   B 2 288 ? 6.760   26.626  24.361  1.00 154.74 ? 288  GLU   B CB  1 
ATOM   4844  C  CG  . GLU   B 2 288 ? 5.890   25.687  25.187  1.00 159.67 ? 288  GLU   B CG  1 
ATOM   4845  C  CD  . GLU   B 2 288 ? 4.442   26.152  25.307  1.00 163.36 ? 288  GLU   B CD  1 
ATOM   4846  O  OE1 . GLU   B 2 288 ? 3.588   25.626  24.554  1.00 163.21 ? 288  GLU   B OE1 1 
ATOM   4847  O  OE2 . GLU   B 2 288 ? 4.164   27.052  26.136  1.00 164.43 ? 288  GLU   B OE2 1 
ATOM   4848  N  N   . GLU   B 2 289 ? 8.339   27.686  27.421  1.00 151.98 ? 289  GLU   B N   1 
ATOM   4849  C  CA  . GLU   B 2 289 ? 9.237   27.281  28.515  1.00 149.31 ? 289  GLU   B CA  1 
ATOM   4850  C  C   . GLU   B 2 289 ? 8.712   26.015  29.204  1.00 149.65 ? 289  GLU   B C   1 
ATOM   4851  O  O   . GLU   B 2 289 ? 7.922   26.079  30.150  1.00 149.73 ? 289  GLU   B O   1 
ATOM   4852  C  CB  . GLU   B 2 289 ? 9.397   28.422  29.517  1.00 145.87 ? 289  GLU   B CB  1 
ATOM   4853  N  N   . GLN   B 2 290 ? 9.192   24.856  28.753  1.00 142.93 ? 290  GLN   B N   1 
ATOM   4854  C  CA  . GLN   B 2 290 ? 8.716   23.568  29.236  1.00 146.37 ? 290  GLN   B CA  1 
ATOM   4855  C  C   . GLN   B 2 290 ? 9.435   23.176  30.524  1.00 146.37 ? 290  GLN   B C   1 
ATOM   4856  O  O   . GLN   B 2 290 ? 10.551  23.627  30.809  1.00 147.45 ? 290  GLN   B O   1 
ATOM   4857  C  CB  . GLN   B 2 290 ? 8.938   22.472  28.191  1.00 149.45 ? 290  GLN   B CB  1 
ATOM   4858  C  CG  . GLN   B 2 290 ? 8.241   22.700  26.869  1.00 150.23 ? 290  GLN   B CG  1 
ATOM   4859  C  CD  . GLN   B 2 290 ? 6.766   22.990  27.029  1.00 150.98 ? 290  GLN   B CD  1 
ATOM   4860  O  OE1 . GLN   B 2 290 ? 6.377   23.926  27.725  1.00 151.67 ? 290  GLN   B OE1 1 
ATOM   4861  N  NE2 . GLN   B 2 290 ? 5.934   22.184  26.387  1.00 152.83 ? 290  GLN   B NE2 1 
ATOM   4862  N  N   . MET   B 2 291 ? 8.794   22.286  31.291  1.00 143.62 ? 291  MET   B N   1 
ATOM   4863  C  CA  . MET   B 2 291 ? 9.288   21.985  32.633  1.00 137.13 ? 291  MET   B CA  1 
ATOM   4864  C  C   . MET   B 2 291 ? 10.582  21.175  32.598  1.00 139.60 ? 291  MET   B C   1 
ATOM   4865  O  O   . MET   B 2 291 ? 11.437  21.343  33.484  1.00 133.86 ? 291  MET   B O   1 
ATOM   4866  C  CB  . MET   B 2 291 ? 8.225   21.240  33.437  1.00 133.17 ? 291  MET   B CB  1 
ATOM   4867  C  CG  . MET   B 2 291 ? 7.373   22.146  34.319  1.00 134.32 ? 291  MET   B CG  1 
ATOM   4868  S  SD  . MET   B 2 291 ? 8.300   23.568  34.914  1.00 141.27 ? 291  MET   B SD  1 
ATOM   4869  C  CE  . MET   B 2 291 ? 9.817   22.760  35.429  1.00 125.13 ? 291  MET   B CE  1 
ATOM   4870  N  N   . ASP   B 2 292 ? 10.757  20.319  31.574  1.00 142.57 ? 292  ASP   B N   1 
ATOM   4871  C  CA  . ASP   B 2 292 ? 11.916  19.436  31.401  1.00 138.27 ? 292  ASP   B CA  1 
ATOM   4872  C  C   . ASP   B 2 292 ? 13.202  20.242  31.346  1.00 139.67 ? 292  ASP   B C   1 
ATOM   4873  O  O   . ASP   B 2 292 ? 14.309  19.691  31.426  1.00 134.10 ? 292  ASP   B O   1 
ATOM   4874  C  CB  . ASP   B 2 292 ? 11.759  18.623  30.113  1.00 137.90 ? 292  ASP   B CB  1 
ATOM   4875  C  CG  . ASP   B 2 292 ? 11.476  19.502  28.908  1.00 146.71 ? 292  ASP   B CG  1 
ATOM   4876  O  OD1 . ASP   B 2 292 ? 12.065  20.593  28.817  1.00 149.14 ? 292  ASP   B OD1 1 
ATOM   4877  O  OD2 . ASP   B 2 292 ? 10.662  19.107  28.043  1.00 152.48 ? 292  ASP   B OD2 1 
ATOM   4878  N  N   . GLY   B 2 293 ? 13.035  21.556  31.193  1.00 146.03 ? 293  GLY   B N   1 
ATOM   4879  C  CA  . GLY   B 2 293 ? 14.107  22.496  30.988  1.00 144.53 ? 293  GLY   B CA  1 
ATOM   4880  C  C   . GLY   B 2 293 ? 14.255  22.968  29.556  1.00 147.12 ? 293  GLY   B C   1 
ATOM   4881  O  O   . GLY   B 2 293 ? 14.886  24.008  29.329  1.00 146.32 ? 293  GLY   B O   1 
ATOM   4882  N  N   . THR   B 2 294 ? 13.704  22.230  28.588  1.00 150.55 ? 294  THR   B N   1 
ATOM   4883  C  CA  . THR   B 2 294 ? 13.799  22.573  27.174  1.00 149.08 ? 294  THR   B CA  1 
ATOM   4884  C  C   . THR   B 2 294 ? 12.759  23.627  26.813  1.00 150.08 ? 294  THR   B C   1 
ATOM   4885  O  O   . THR   B 2 294 ? 11.865  23.956  27.600  1.00 151.32 ? 294  THR   B O   1 
ATOM   4886  C  CB  . THR   B 2 294 ? 13.602  21.350  26.270  1.00 145.86 ? 294  THR   B CB  1 
ATOM   4887  O  OG1 . THR   B 2 294 ? 12.198  21.109  26.096  1.00 146.75 ? 294  THR   B OG1 1 
ATOM   4888  C  CG2 . THR   B 2 294 ? 14.268  20.115  26.857  1.00 146.31 ? 294  THR   B CG2 1 
ATOM   4889  N  N   . VAL   B 2 295 ? 12.886  24.156  25.599  1.00 144.27 ? 295  VAL   B N   1 
ATOM   4890  C  CA  . VAL   B 2 295 ? 11.976  25.171  25.086  1.00 142.60 ? 295  VAL   B CA  1 
ATOM   4891  C  C   . VAL   B 2 295 ? 11.623  24.793  23.656  1.00 139.20 ? 295  VAL   B C   1 
ATOM   4892  O  O   . VAL   B 2 295 ? 12.462  24.269  22.915  1.00 139.12 ? 295  VAL   B O   1 
ATOM   4893  C  CB  . VAL   B 2 295 ? 12.587  26.591  25.166  1.00 140.18 ? 295  VAL   B CB  1 
ATOM   4894  C  CG1 . VAL   B 2 295 ? 11.508  27.662  25.017  1.00 144.45 ? 295  VAL   B CG1 1 
ATOM   4895  C  CG2 . VAL   B 2 295 ? 13.330  26.788  26.483  1.00 133.42 ? 295  VAL   B CG2 1 
ATOM   4896  N  N   . THR   B 2 296 ? 10.372  25.030  23.284  1.00 136.05 ? 296  THR   B N   1 
ATOM   4897  C  CA  . THR   B 2 296 ? 9.889   24.795  21.934  1.00 135.75 ? 296  THR   B CA  1 
ATOM   4898  C  C   . THR   B 2 296 ? 9.396   26.116  21.355  1.00 130.71 ? 296  THR   B C   1 
ATOM   4899  O  O   . THR   B 2 296 ? 9.130   27.070  22.091  1.00 133.93 ? 296  THR   B O   1 
ATOM   4900  C  CB  . THR   B 2 296 ? 8.773   23.746  21.933  1.00 137.81 ? 296  THR   B CB  1 
ATOM   4901  O  OG1 . THR   B 2 296 ? 7.982   23.911  23.122  1.00 140.91 ? 296  THR   B OG1 1 
ATOM   4902  C  CG2 . THR   B 2 296 ? 9.358   22.332  21.888  1.00 128.67 ? 296  THR   B CG2 1 
ATOM   4903  N  N   . LEU   B 2 297 ? 9.293   26.178  20.026  1.00 125.19 ? 297  LEU   B N   1 
ATOM   4904  C  CA  . LEU   B 2 297 ? 8.829   27.382  19.337  1.00 121.04 ? 297  LEU   B CA  1 
ATOM   4905  C  C   . LEU   B 2 297 ? 7.313   27.312  19.187  1.00 118.88 ? 297  LEU   B C   1 
ATOM   4906  O  O   . LEU   B 2 297 ? 6.797   26.575  18.344  1.00 116.52 ? 297  LEU   B O   1 
ATOM   4907  C  CB  . LEU   B 2 297 ? 9.505   27.532  17.977  1.00 116.32 ? 297  LEU   B CB  1 
ATOM   4908  C  CG  . LEU   B 2 297 ? 8.779   28.486  17.027  1.00 118.07 ? 297  LEU   B CG  1 
ATOM   4909  C  CD1 . LEU   B 2 297 ? 8.891   29.894  17.577  1.00 118.62 ? 297  LEU   B CD1 1 
ATOM   4910  C  CD2 . LEU   B 2 297 ? 9.291   28.405  15.579  1.00 108.47 ? 297  LEU   B CD2 1 
ATOM   4911  N  N   . LYS   B 2 298 ? 6.598   28.088  19.996  1.00 119.61 ? 298  LYS   B N   1 
ATOM   4912  C  CA  . LYS   B 2 298 ? 5.142   28.026  19.985  1.00 122.05 ? 298  LYS   B CA  1 
ATOM   4913  C  C   . LYS   B 2 298 ? 4.576   28.584  18.681  1.00 126.20 ? 298  LYS   B C   1 
ATOM   4914  O  O   . LYS   B 2 298 ? 3.885   27.875  17.940  1.00 123.73 ? 298  LYS   B O   1 
ATOM   4915  C  CB  . LYS   B 2 298 ? 4.589   28.768  21.209  1.00 132.68 ? 298  LYS   B CB  1 
ATOM   4916  C  CG  . LYS   B 2 298 ? 3.219   29.424  21.023  1.00 135.86 ? 298  LYS   B CG  1 
ATOM   4917  C  CD  . LYS   B 2 298 ? 2.102   28.681  21.752  1.00 140.99 ? 298  LYS   B CD  1 
ATOM   4918  C  CE  . LYS   B 2 298 ? 0.760   29.372  21.498  1.00 136.96 ? 298  LYS   B CE  1 
ATOM   4919  N  NZ  . LYS   B 2 298 ? -0.379  28.489  21.878  1.00 140.43 ? 298  LYS   B NZ  1 
ATOM   4920  N  N   . ASP   B 2 299 ? 4.877   29.850  18.372  1.00 127.11 ? 299  ASP   B N   1 
ATOM   4921  C  CA  . ASP   B 2 299 ? 4.294   30.548  17.229  1.00 124.41 ? 299  ASP   B CA  1 
ATOM   4922  C  C   . ASP   B 2 299 ? 5.278   31.571  16.676  1.00 122.09 ? 299  ASP   B C   1 
ATOM   4923  O  O   . ASP   B 2 299 ? 6.190   32.026  17.369  1.00 121.73 ? 299  ASP   B O   1 
ATOM   4924  C  CB  . ASP   B 2 299 ? 2.993   31.263  17.618  1.00 130.03 ? 299  ASP   B CB  1 
ATOM   4925  C  CG  . ASP   B 2 299 ? 1.765   30.666  16.955  1.00 134.84 ? 299  ASP   B CG  1 
ATOM   4926  O  OD1 . ASP   B 2 299 ? 1.869   30.193  15.795  1.00 132.28 ? 299  ASP   B OD1 1 
ATOM   4927  O  OD2 . ASP   B 2 299 ? 0.692   30.675  17.602  1.00 139.93 ? 299  ASP   B OD2 1 
ATOM   4928  N  N   . LEU   B 2 300 ? 5.056   31.953  15.421  1.00 117.93 ? 300  LEU   B N   1 
ATOM   4929  C  CA  . LEU   B 2 300 ? 5.726   33.090  14.803  1.00 112.11 ? 300  LEU   B CA  1 
ATOM   4930  C  C   . LEU   B 2 300 ? 4.719   34.202  14.566  1.00 112.74 ? 300  LEU   B C   1 
ATOM   4931  O  O   . LEU   B 2 300 ? 3.706   33.985  13.887  1.00 109.62 ? 300  LEU   B O   1 
ATOM   4932  C  CB  . LEU   B 2 300 ? 6.339   32.712  13.462  1.00 107.05 ? 300  LEU   B CB  1 
ATOM   4933  C  CG  . LEU   B 2 300 ? 7.336   31.587  13.461  1.00 104.22 ? 300  LEU   B CG  1 
ATOM   4934  C  CD1 . LEU   B 2 300 ? 7.373   31.036  12.058  1.00 99.44  ? 300  LEU   B CD1 1 
ATOM   4935  C  CD2 . LEU   B 2 300 ? 8.641   32.201  13.843  1.00 98.45  ? 300  LEU   B CD2 1 
ATOM   4936  N  N   . ARG   B 2 301 ? 5.015   35.394  15.083  1.00 113.29 ? 301  ARG   B N   1 
ATOM   4937  C  CA  . ARG   B 2 301 ? 4.190   36.572  14.841  1.00 114.10 ? 301  ARG   B CA  1 
ATOM   4938  C  C   . ARG   B 2 301 ? 4.990   37.669  14.144  1.00 107.64 ? 301  ARG   B C   1 
ATOM   4939  O  O   . ARG   B 2 301 ? 6.217   37.749  14.270  1.00 104.98 ? 301  ARG   B O   1 
ATOM   4940  C  CB  . ARG   B 2 301 ? 3.587   37.106  16.143  1.00 117.96 ? 301  ARG   B CB  1 
ATOM   4941  C  CG  . ARG   B 2 301 ? 2.394   36.298  16.627  1.00 123.44 ? 301  ARG   B CG  1 
ATOM   4942  C  CD  . ARG   B 2 301 ? 1.477   37.149  17.481  1.00 131.78 ? 301  ARG   B CD  1 
ATOM   4943  N  NE  . ARG   B 2 301 ? 2.236   37.954  18.434  1.00 139.29 ? 301  ARG   B NE  1 
ATOM   4944  C  CZ  . ARG   B 2 301 ? 2.285   39.284  18.442  1.00 138.97 ? 301  ARG   B CZ  1 
ATOM   4945  N  NH1 . ARG   B 2 301 ? 1.591   40.012  17.578  1.00 131.78 ? 301  ARG   B NH1 1 
ATOM   4946  N  NH2 . ARG   B 2 301 ? 3.040   39.900  19.352  1.00 133.56 ? 301  ARG   B NH2 1 
ATOM   4947  N  N   . VAL   B 2 302 ? 4.275   38.512  13.399  1.00 109.49 ? 302  VAL   B N   1 
ATOM   4948  C  CA  . VAL   B 2 302 ? 4.870   39.618  12.660  1.00 105.82 ? 302  VAL   B CA  1 
ATOM   4949  C  C   . VAL   B 2 302 ? 4.106   40.902  12.971  1.00 109.23 ? 302  VAL   B C   1 
ATOM   4950  O  O   . VAL   B 2 302 ? 2.872   40.931  12.902  1.00 110.13 ? 302  VAL   B O   1 
ATOM   4951  C  CB  . VAL   B 2 302 ? 4.867   39.345  11.153  1.00 102.00 ? 302  VAL   B CB  1 
ATOM   4952  C  CG1 . VAL   B 2 302 ? 5.113   40.634  10.426  1.00 107.49 ? 302  VAL   B CG1 1 
ATOM   4953  C  CG2 . VAL   B 2 302 ? 5.916   38.307  10.800  1.00 96.98  ? 302  VAL   B CG2 1 
ATOM   4954  N  N   . GLU   B 2 303 ? 4.833   41.962  13.306  1.00 117.80 ? 303  GLU   B N   1 
ATOM   4955  C  CA  . GLU   B 2 303 ? 4.224   43.230  13.684  1.00 120.06 ? 303  GLU   B CA  1 
ATOM   4956  C  C   . GLU   B 2 303 ? 4.818   44.358  12.846  1.00 115.77 ? 303  GLU   B C   1 
ATOM   4957  O  O   . GLU   B 2 303 ? 6.034   44.414  12.635  1.00 114.98 ? 303  GLU   B O   1 
ATOM   4958  C  CB  . GLU   B 2 303 ? 4.436   43.518  15.181  1.00 122.25 ? 303  GLU   B CB  1 
ATOM   4959  C  CG  . GLU   B 2 303 ? 3.224   44.093  15.924  1.00 128.83 ? 303  GLU   B CG  1 
ATOM   4960  C  CD  . GLU   B 2 303 ? 2.190   43.029  16.270  1.00 136.83 ? 303  GLU   B CD  1 
ATOM   4961  O  OE1 . GLU   B 2 303 ? 0.991   43.391  16.426  1.00 142.33 ? 303  GLU   B OE1 1 
ATOM   4962  O  OE2 . GLU   B 2 303 ? 2.578   41.840  16.380  1.00 137.44 ? 303  GLU   B OE2 1 
ATOM   4963  N  N   . LEU   B 2 304 ? 3.962   45.252  12.360  1.00 101.92 ? 304  LEU   B N   1 
ATOM   4964  C  CA  . LEU   B 2 304 ? 4.421   46.396  11.588  1.00 97.62  ? 304  LEU   B CA  1 
ATOM   4965  C  C   . LEU   B 2 304 ? 4.772   47.523  12.547  1.00 97.79  ? 304  LEU   B C   1 
ATOM   4966  O  O   . LEU   B 2 304 ? 3.925   47.966  13.324  1.00 103.48 ? 304  LEU   B O   1 
ATOM   4967  C  CB  . LEU   B 2 304 ? 3.359   46.850  10.593  1.00 96.46  ? 304  LEU   B CB  1 
ATOM   4968  C  CG  . LEU   B 2 304 ? 3.765   48.010  9.675   1.00 88.57  ? 304  LEU   B CG  1 
ATOM   4969  C  CD1 . LEU   B 2 304 ? 5.262   48.028  9.392   1.00 94.10  ? 304  LEU   B CD1 1 
ATOM   4970  C  CD2 . LEU   B 2 304 ? 3.003   47.918  8.379   1.00 79.97  ? 304  LEU   B CD2 1 
ATOM   4971  N  N   . LEU   B 2 305 ? 6.017   47.984  12.493  1.00 92.75  ? 305  LEU   B N   1 
ATOM   4972  C  CA  . LEU   B 2 305 ? 6.501   48.995  13.425  1.00 97.41  ? 305  LEU   B CA  1 
ATOM   4973  C  C   . LEU   B 2 305 ? 6.438   50.409  12.863  1.00 102.26 ? 305  LEU   B C   1 
ATOM   4974  O  O   . LEU   B 2 305 ? 6.128   51.353  13.602  1.00 108.16 ? 305  LEU   B O   1 
ATOM   4975  C  CB  . LEU   B 2 305 ? 7.940   48.682  13.851  1.00 95.85  ? 305  LEU   B CB  1 
ATOM   4976  C  CG  . LEU   B 2 305 ? 8.242   47.520  14.803  1.00 101.67 ? 305  LEU   B CG  1 
ATOM   4977  C  CD1 . LEU   B 2 305 ? 7.635   46.206  14.315  1.00 103.01 ? 305  LEU   B CD1 1 
ATOM   4978  C  CD2 . LEU   B 2 305 ? 9.754   47.375  15.001  1.00 100.36 ? 305  LEU   B CD2 1 
ATOM   4979  N  N   . GLY   B 2 306 ? 6.727   50.600  11.581  1.00 94.84  ? 306  GLY   B N   1 
ATOM   4980  C  CA  . GLY   B 2 306 ? 6.752   51.950  11.052  1.00 95.54  ? 306  GLY   B CA  1 
ATOM   4981  C  C   . GLY   B 2 306 ? 7.378   51.977  9.671   1.00 98.30  ? 306  GLY   B C   1 
ATOM   4982  O  O   . GLY   B 2 306 ? 7.459   50.955  8.990   1.00 95.25  ? 306  GLY   B O   1 
ATOM   4983  N  N   . GLU   B 2 307 ? 7.806   53.167  9.264   1.00 97.09  ? 307  GLU   B N   1 
ATOM   4984  C  CA  . GLU   B 2 307 ? 8.405   53.347  7.952   1.00 95.15  ? 307  GLU   B CA  1 
ATOM   4985  C  C   . GLU   B 2 307 ? 9.632   54.236  8.063   1.00 96.21  ? 307  GLU   B C   1 
ATOM   4986  O  O   . GLU   B 2 307 ? 9.618   55.257  8.761   1.00 95.12  ? 307  GLU   B O   1 
ATOM   4987  C  CB  . GLU   B 2 307 ? 7.425   53.949  6.949   1.00 96.92  ? 307  GLU   B CB  1 
ATOM   4988  C  CG  . GLU   B 2 307 ? 8.119   54.852  5.943   1.00 99.72  ? 307  GLU   B CG  1 
ATOM   4989  C  CD  . GLU   B 2 307 ? 7.239   55.221  4.768   1.00 102.10 ? 307  GLU   B CD  1 
ATOM   4990  O  OE1 . GLU   B 2 307 ? 7.217   56.421  4.401   1.00 102.36 ? 307  GLU   B OE1 1 
ATOM   4991  O  OE2 . GLU   B 2 307 ? 6.581   54.306  4.214   1.00 101.27 ? 307  GLU   B OE2 1 
ATOM   4992  N  N   . THR   B 2 308 ? 10.679  53.850  7.334   1.00 95.32  ? 308  THR   B N   1 
ATOM   4993  C  CA  . THR   B 2 308 ? 11.986  54.495  7.386   1.00 93.70  ? 308  THR   B CA  1 
ATOM   4994  C  C   . THR   B 2 308 ? 12.526  54.665  5.967   1.00 90.15  ? 308  THR   B C   1 
ATOM   4995  O  O   . THR   B 2 308 ? 11.824  54.353  4.995   1.00 89.56  ? 308  THR   B O   1 
ATOM   4996  C  CB  . THR   B 2 308 ? 12.963  53.661  8.214   1.00 90.63  ? 308  THR   B CB  1 
ATOM   4997  O  OG1 . THR   B 2 308 ? 13.504  52.629  7.378   1.00 85.40  ? 308  THR   B OG1 1 
ATOM   4998  C  CG2 . THR   B 2 308 ? 12.248  53.018  9.446   1.00 88.55  ? 308  THR   B CG2 1 
ATOM   4999  N  N   . SER   B 2 309 ? 13.765  55.143  5.832   1.00 86.44  ? 309  SER   B N   1 
ATOM   5000  C  CA  . SER   B 2 309 ? 14.399  55.162  4.520   1.00 85.91  ? 309  SER   B CA  1 
ATOM   5001  C  C   . SER   B 2 309 ? 14.453  53.752  3.966   1.00 80.92  ? 309  SER   B C   1 
ATOM   5002  O  O   . SER   B 2 309 ? 14.587  52.784  4.706   1.00 86.27  ? 309  SER   B O   1 
ATOM   5003  C  CB  . SER   B 2 309 ? 15.818  55.727  4.592   1.00 83.27  ? 309  SER   B CB  1 
ATOM   5004  O  OG  . SER   B 2 309 ? 15.815  57.106  4.864   1.00 85.93  ? 309  SER   B OG  1 
ATOM   5005  N  N   . ILE   B 2 310 ? 14.351  53.633  2.654   1.00 78.03  ? 310  ILE   B N   1 
ATOM   5006  C  CA  . ILE   B 2 310 ? 14.441  52.314  2.038   1.00 83.43  ? 310  ILE   B CA  1 
ATOM   5007  C  C   . ILE   B 2 310 ? 15.743  51.675  2.497   1.00 80.57  ? 310  ILE   B C   1 
ATOM   5008  O  O   . ILE   B 2 310 ? 16.832  52.178  2.194   1.00 81.44  ? 310  ILE   B O   1 
ATOM   5009  C  CB  . ILE   B 2 310 ? 14.348  52.414  0.509   1.00 83.41  ? 310  ILE   B CB  1 
ATOM   5010  C  CG1 . ILE   B 2 310 ? 13.035  53.082  0.093   1.00 82.04  ? 310  ILE   B CG1 1 
ATOM   5011  C  CG2 . ILE   B 2 310 ? 14.389  51.058  -0.137  1.00 73.67  ? 310  ILE   B CG2 1 
ATOM   5012  C  CD1 . ILE   B 2 310 ? 12.935  53.294  -1.416  1.00 73.81  ? 310  ILE   B CD1 1 
ATOM   5013  N  N   . ALA   B 2 311 ? 15.634  50.575  3.251   1.00 80.99  ? 311  ALA   B N   1 
ATOM   5014  C  CA  . ALA   B 2 311 ? 16.758  50.023  4.009   1.00 79.60  ? 311  ALA   B CA  1 
ATOM   5015  C  C   . ALA   B 2 311 ? 17.582  49.059  3.175   1.00 81.47  ? 311  ALA   B C   1 
ATOM   5016  O  O   . ALA   B 2 311 ? 17.036  48.156  2.538   1.00 85.93  ? 311  ALA   B O   1 
ATOM   5017  C  CB  . ALA   B 2 311 ? 16.268  49.297  5.259   1.00 79.32  ? 311  ALA   B CB  1 
ATOM   5018  N  N   . GLU   B 2 312 ? 18.888  49.263  3.162   1.00 79.88  ? 312  GLU   B N   1 
ATOM   5019  C  CA  . GLU   B 2 312 ? 19.776  48.274  2.576   1.00 80.47  ? 312  GLU   B CA  1 
ATOM   5020  C  C   . GLU   B 2 312 ? 20.270  47.305  3.633   1.00 87.74  ? 312  GLU   B C   1 
ATOM   5021  O  O   . GLU   B 2 312 ? 20.436  46.114  3.345   1.00 89.88  ? 312  GLU   B O   1 
ATOM   5022  C  CB  . GLU   B 2 312 ? 20.953  48.974  1.876   1.00 79.99  ? 312  GLU   B CB  1 
ATOM   5023  C  CG  . GLU   B 2 312 ? 22.053  48.078  1.344   1.00 86.85  ? 312  GLU   B CG  1 
ATOM   5024  C  CD  . GLU   B 2 312 ? 21.667  47.300  0.090   1.00 95.39  ? 312  GLU   B CD  1 
ATOM   5025  O  OE1 . GLU   B 2 312 ? 20.458  47.240  -0.245  1.00 91.34  ? 312  GLU   B OE1 1 
ATOM   5026  O  OE2 . GLU   B 2 312 ? 22.591  46.746  -0.559  1.00 97.99  ? 312  GLU   B OE2 1 
ATOM   5027  N  N   . CYS   B 2 313 ? 20.474  47.802  4.858   1.00 83.12  ? 313  CYS   B N   1 
ATOM   5028  C  CA  . CYS   B 2 313 ? 20.885  46.993  5.992   1.00 80.23  ? 313  CYS   B CA  1 
ATOM   5029  C  C   . CYS   B 2 313 ? 20.325  47.612  7.269   1.00 87.15  ? 313  CYS   B C   1 
ATOM   5030  O  O   . CYS   B 2 313 ? 20.060  48.816  7.331   1.00 87.30  ? 313  CYS   B O   1 
ATOM   5031  C  CB  . CYS   B 2 313 ? 22.407  46.868  6.049   1.00 82.09  ? 313  CYS   B CB  1 
ATOM   5032  S  SG  . CYS   B 2 313 ? 23.266  48.332  6.648   1.00 94.84  ? 313  CYS   B SG  1 
ATOM   5033  N  N   . LEU   B 2 314 ? 20.122  46.764  8.284   1.00 91.05  ? 314  LEU   B N   1 
ATOM   5034  C  CA  . LEU   B 2 314 ? 19.517  47.145  9.558   1.00 87.44  ? 314  LEU   B CA  1 
ATOM   5035  C  C   . LEU   B 2 314 ? 20.358  46.586  10.683  1.00 91.73  ? 314  LEU   B C   1 
ATOM   5036  O  O   . LEU   B 2 314 ? 20.769  45.419  10.636  1.00 95.21  ? 314  LEU   B O   1 
ATOM   5037  C  CB  . LEU   B 2 314 ? 18.103  46.578  9.715   1.00 87.78  ? 314  LEU   B CB  1 
ATOM   5038  C  CG  . LEU   B 2 314 ? 16.843  47.311  9.301   1.00 89.20  ? 314  LEU   B CG  1 
ATOM   5039  C  CD1 . LEU   B 2 314 ? 17.100  48.060  8.022   1.00 91.11  ? 314  LEU   B CD1 1 
ATOM   5040  C  CD2 . LEU   B 2 314 ? 15.775  46.250  9.082   1.00 86.83  ? 314  LEU   B CD2 1 
ATOM   5041  N  N   . THR   B 2 315 ? 20.571  47.391  11.713  1.00 88.75  ? 315  THR   B N   1 
ATOM   5042  C  CA  . THR   B 2 315 ? 21.105  46.847  12.949  1.00 90.12  ? 315  THR   B CA  1 
ATOM   5043  C  C   . THR   B 2 315 ? 20.420  47.562  14.100  1.00 92.30  ? 315  THR   B C   1 
ATOM   5044  O  O   . THR   B 2 315 ? 20.260  48.788  14.074  1.00 91.92  ? 315  THR   B O   1 
ATOM   5045  C  CB  . THR   B 2 315 ? 22.636  46.982  13.042  1.00 91.09  ? 315  THR   B CB  1 
ATOM   5046  O  OG1 . THR   B 2 315 ? 22.978  48.267  13.561  1.00 94.78  ? 315  THR   B OG1 1 
ATOM   5047  C  CG2 . THR   B 2 315 ? 23.287  46.841  11.664  1.00 92.95  ? 315  THR   B CG2 1 
ATOM   5048  N  N   . TYR   B 2 316 ? 19.963  46.784  15.075  1.00 94.97  ? 316  TYR   B N   1 
ATOM   5049  C  CA  . TYR   B 2 316 ? 19.612  47.350  16.366  1.00 93.34  ? 316  TYR   B CA  1 
ATOM   5050  C  C   . TYR   B 2 316 ? 20.895  47.737  17.090  1.00 89.85  ? 316  TYR   B C   1 
ATOM   5051  O  O   . TYR   B 2 316 ? 21.932  47.095  16.917  1.00 95.37  ? 316  TYR   B O   1 
ATOM   5052  C  CB  . TYR   B 2 316 ? 18.800  46.336  17.173  1.00 95.46  ? 316  TYR   B CB  1 
ATOM   5053  C  CG  . TYR   B 2 316 ? 18.369  46.803  18.546  1.00 101.40 ? 316  TYR   B CG  1 
ATOM   5054  C  CD1 . TYR   B 2 316 ? 18.167  48.153  18.826  1.00 103.35 ? 316  TYR   B CD1 1 
ATOM   5055  C  CD2 . TYR   B 2 316 ? 18.158  45.890  19.570  1.00 105.31 ? 316  TYR   B CD2 1 
ATOM   5056  C  CE1 . TYR   B 2 316 ? 17.769  48.572  20.101  1.00 105.62 ? 316  TYR   B CE1 1 
ATOM   5057  C  CE2 . TYR   B 2 316 ? 17.763  46.299  20.838  1.00 108.21 ? 316  TYR   B CE2 1 
ATOM   5058  C  CZ  . TYR   B 2 316 ? 17.570  47.636  21.097  1.00 106.46 ? 316  TYR   B CZ  1 
ATOM   5059  O  OH  . TYR   B 2 316 ? 17.182  48.025  22.356  1.00 108.62 ? 316  TYR   B OH  1 
ATOM   5060  N  N   . LEU   B 2 317 ? 20.829  48.815  17.873  1.00 96.12  ? 317  LEU   B N   1 
ATOM   5061  C  CA  . LEU   B 2 317 ? 21.950  49.272  18.693  1.00 101.97 ? 317  LEU   B CA  1 
ATOM   5062  C  C   . LEU   B 2 317 ? 21.674  49.024  20.173  1.00 103.12 ? 317  LEU   B C   1 
ATOM   5063  O  O   . LEU   B 2 317 ? 22.296  48.163  20.786  1.00 102.27 ? 317  LEU   B O   1 
ATOM   5064  C  CB  . LEU   B 2 317 ? 22.229  50.752  18.431  1.00 97.37  ? 317  LEU   B CB  1 
ATOM   5065  C  CG  . LEU   B 2 317 ? 22.277  51.222  16.978  1.00 96.29  ? 317  LEU   B CG  1 
ATOM   5066  C  CD1 . LEU   B 2 317 ? 22.511  52.708  16.950  1.00 98.85  ? 317  LEU   B CD1 1 
ATOM   5067  C  CD2 . LEU   B 2 317 ? 23.383  50.527  16.238  1.00 94.09  ? 317  LEU   B CD2 1 
ATOM   5068  N  N   . ASP   B 2 318 ? 20.753  49.773  20.773  1.00 104.95 ? 318  ASP   B N   1 
ATOM   5069  C  CA  . ASP   B 2 318 ? 20.428  49.639  22.189  1.00 105.04 ? 318  ASP   B CA  1 
ATOM   5070  C  C   . ASP   B 2 318 ? 19.379  50.694  22.500  1.00 108.15 ? 318  ASP   B C   1 
ATOM   5071  O  O   . ASP   B 2 318 ? 19.194  51.649  21.739  1.00 110.56 ? 318  ASP   B O   1 
ATOM   5072  C  CB  . ASP   B 2 318 ? 21.658  49.821  23.067  1.00 106.99 ? 318  ASP   B CB  1 
ATOM   5073  C  CG  . ASP   B 2 318 ? 21.436  49.348  24.492  1.00 114.97 ? 318  ASP   B CG  1 
ATOM   5074  O  OD1 . ASP   B 2 318 ? 20.828  48.262  24.652  1.00 119.55 ? 318  ASP   B OD1 1 
ATOM   5075  O  OD2 . ASP   B 2 318 ? 21.897  50.028  25.449  1.00 116.51 ? 318  ASP   B OD2 1 
ATOM   5076  N  N   . ASN   B 2 319 ? 18.694  50.524  23.625  1.00 107.92 ? 319  ASN   B N   1 
ATOM   5077  C  CA  . ASN   B 2 319 ? 17.744  51.538  24.092  1.00 108.69 ? 319  ASN   B CA  1 
ATOM   5078  C  C   . ASN   B 2 319 ? 16.753  51.917  22.997  1.00 105.41 ? 319  ASN   B C   1 
ATOM   5079  O  O   . ASN   B 2 319 ? 16.328  53.073  22.902  1.00 110.31 ? 319  ASN   B O   1 
ATOM   5080  C  CB  . ASN   B 2 319 ? 18.472  52.788  24.599  1.00 107.39 ? 319  ASN   B CB  1 
ATOM   5081  C  CG  . ASN   B 2 319 ? 19.772  52.460  25.306  1.00 113.77 ? 319  ASN   B CG  1 
ATOM   5082  O  OD1 . ASN   B 2 319 ? 20.844  52.474  24.695  1.00 117.88 ? 319  ASN   B OD1 1 
ATOM   5083  N  ND2 . ASN   B 2 319 ? 19.684  52.144  26.595  1.00 115.66 ? 319  ASN   B ND2 1 
ATOM   5084  N  N   . GLY   B 2 320 ? 16.420  50.952  22.141  1.00 106.62 ? 320  GLY   B N   1 
ATOM   5085  C  CA  . GLY   B 2 320 ? 15.445  51.162  21.084  1.00 111.66 ? 320  GLY   B CA  1 
ATOM   5086  C  C   . GLY   B 2 320 ? 15.905  51.964  19.887  1.00 103.51 ? 320  GLY   B C   1 
ATOM   5087  O  O   . GLY   B 2 320 ? 15.067  52.396  19.084  1.00 98.88  ? 320  GLY   B O   1 
ATOM   5088  N  N   . VAL   B 2 321 ? 17.202  52.184  19.734  1.00 100.58 ? 321  VAL   B N   1 
ATOM   5089  C  CA  . VAL   B 2 321 ? 17.718  52.887  18.572  1.00 97.58  ? 321  VAL   B CA  1 
ATOM   5090  C  C   . VAL   B 2 321 ? 18.096  51.872  17.505  1.00 96.89  ? 321  VAL   B C   1 
ATOM   5091  O  O   . VAL   B 2 321 ? 18.855  50.931  17.764  1.00 97.62  ? 321  VAL   B O   1 
ATOM   5092  C  CB  . VAL   B 2 321 ? 18.916  53.771  18.930  1.00 99.12  ? 321  VAL   B CB  1 
ATOM   5093  C  CG1 . VAL   B 2 321 ? 19.649  54.135  17.666  1.00 93.62  ? 321  VAL   B CG1 1 
ATOM   5094  C  CG2 . VAL   B 2 321 ? 18.430  55.021  19.609  1.00 104.00 ? 321  VAL   B CG2 1 
ATOM   5095  N  N   . VAL   B 2 322 ? 17.564  52.069  16.305  1.00 95.18  ? 322  VAL   B N   1 
ATOM   5096  C  CA  . VAL   B 2 322 ? 17.901  51.273  15.136  1.00 93.37  ? 322  VAL   B CA  1 
ATOM   5097  C  C   . VAL   B 2 322 ? 18.649  52.154  14.155  1.00 92.66  ? 322  VAL   B C   1 
ATOM   5098  O  O   . VAL   B 2 322 ? 18.174  53.247  13.816  1.00 87.97  ? 322  VAL   B O   1 
ATOM   5099  C  CB  . VAL   B 2 322 ? 16.647  50.706  14.455  1.00 93.54  ? 322  VAL   B CB  1 
ATOM   5100  C  CG1 . VAL   B 2 322 ? 17.049  49.877  13.245  1.00 87.42  ? 322  VAL   B CG1 1 
ATOM   5101  C  CG2 . VAL   B 2 322 ? 15.861  49.883  15.432  1.00 94.97  ? 322  VAL   B CG2 1 
ATOM   5102  N  N   . PHE   B 2 323 ? 19.804  51.673  13.684  1.00 92.33  ? 323  PHE   B N   1 
ATOM   5103  C  CA  . PHE   B 2 323 ? 20.450  52.283  12.530  1.00 87.05  ? 323  PHE   B CA  1 
ATOM   5104  C  C   . PHE   B 2 323 ? 19.816  51.757  11.254  1.00 86.99  ? 323  PHE   B C   1 
ATOM   5105  O  O   . PHE   B 2 323 ? 19.512  50.567  11.133  1.00 89.21  ? 323  PHE   B O   1 
ATOM   5106  C  CB  . PHE   B 2 323 ? 21.950  52.013  12.490  1.00 83.16  ? 323  PHE   B CB  1 
ATOM   5107  C  CG  . PHE   B 2 323 ? 22.619  52.611  11.286  1.00 86.64  ? 323  PHE   B CG  1 
ATOM   5108  C  CD1 . PHE   B 2 323 ? 22.777  53.991  11.175  1.00 90.89  ? 323  PHE   B CD1 1 
ATOM   5109  C  CD2 . PHE   B 2 323 ? 23.087  51.812  10.265  1.00 86.45  ? 323  PHE   B CD2 1 
ATOM   5110  C  CE1 . PHE   B 2 323 ? 23.400  54.567  10.070  1.00 84.69  ? 323  PHE   B CE1 1 
ATOM   5111  C  CE2 . PHE   B 2 323 ? 23.710  52.376  9.153   1.00 90.88  ? 323  PHE   B CE2 1 
ATOM   5112  C  CZ  . PHE   B 2 323 ? 23.862  53.764  9.056   1.00 88.52  ? 323  PHE   B CZ  1 
ATOM   5113  N  N   . VAL   B 2 324 ? 19.603  52.650  10.308  1.00 86.57  ? 324  VAL   B N   1 
ATOM   5114  C  CA  . VAL   B 2 324 ? 19.111  52.270  9.007   1.00 84.15  ? 324  VAL   B CA  1 
ATOM   5115  C  C   . VAL   B 2 324 ? 20.168  52.691  8.002   1.00 86.86  ? 324  VAL   B C   1 
ATOM   5116  O  O   . VAL   B 2 324 ? 20.429  53.894  7.839   1.00 89.04  ? 324  VAL   B O   1 
ATOM   5117  C  CB  . VAL   B 2 324 ? 17.754  52.914  8.706   1.00 83.94  ? 324  VAL   B CB  1 
ATOM   5118  C  CG1 . VAL   B 2 324 ? 17.411  52.723  7.235   1.00 83.69  ? 324  VAL   B CG1 1 
ATOM   5119  C  CG2 . VAL   B 2 324 ? 16.708  52.285  9.587   1.00 81.97  ? 324  VAL   B CG2 1 
ATOM   5120  N  N   . GLY   B 2 325 ? 20.792  51.711  7.351   1.00 81.21  ? 325  GLY   B N   1 
ATOM   5121  C  CA  . GLY   B 2 325 ? 21.660  51.982  6.226   1.00 78.15  ? 325  GLY   B CA  1 
ATOM   5122  C  C   . GLY   B 2 325 ? 20.821  52.054  4.971   1.00 80.49  ? 325  GLY   B C   1 
ATOM   5123  O  O   . GLY   B 2 325 ? 19.993  51.179  4.722   1.00 80.69  ? 325  GLY   B O   1 
ATOM   5124  N  N   . SER   B 2 326 ? 21.008  53.117  4.196   1.00 82.99  ? 326  SER   B N   1 
ATOM   5125  C  CA  . SER   B 2 326 ? 20.204  53.324  2.998   1.00 81.04  ? 326  SER   B CA  1 
ATOM   5126  C  C   . SER   B 2 326 ? 21.117  53.637  1.831   1.00 83.28  ? 326  SER   B C   1 
ATOM   5127  O  O   . SER   B 2 326 ? 22.187  54.240  2.010   1.00 83.15  ? 326  SER   B O   1 
ATOM   5128  C  CB  . SER   B 2 326 ? 19.180  54.450  3.184   1.00 77.72  ? 326  SER   B CB  1 
ATOM   5129  O  OG  . SER   B 2 326 ? 18.022  54.226  2.410   1.00 79.56  ? 326  SER   B OG  1 
ATOM   5130  N  N   . ARG   B 2 327 ? 20.694  53.198  0.643   1.00 79.04  ? 327  ARG   B N   1 
ATOM   5131  C  CA  . ARG   B 2 327 ? 21.358  53.567  -0.602  1.00 79.10  ? 327  ARG   B CA  1 
ATOM   5132  C  C   . ARG   B 2 327 ? 20.484  54.398  -1.522  1.00 79.51  ? 327  ARG   B C   1 
ATOM   5133  O  O   . ARG   B 2 327 ? 21.007  55.172  -2.334  1.00 79.19  ? 327  ARG   B O   1 
ATOM   5134  C  CB  . ARG   B 2 327 ? 21.842  52.315  -1.349  1.00 82.75  ? 327  ARG   B CB  1 
ATOM   5135  C  CG  . ARG   B 2 327 ? 22.818  51.445  -0.557  1.00 84.83  ? 327  ARG   B CG  1 
ATOM   5136  C  CD  . ARG   B 2 327 ? 23.519  50.434  -1.445  1.00 86.75  ? 327  ARG   B CD  1 
ATOM   5137  N  NE  . ARG   B 2 327 ? 24.123  51.086  -2.597  1.00 89.03  ? 327  ARG   B NE  1 
ATOM   5138  C  CZ  . ARG   B 2 327 ? 24.643  50.445  -3.635  1.00 97.26  ? 327  ARG   B CZ  1 
ATOM   5139  N  NH1 . ARG   B 2 327 ? 24.682  49.121  -3.682  1.00 98.26  ? 327  ARG   B NH1 1 
ATOM   5140  N  NH2 . ARG   B 2 327 ? 25.132  51.152  -4.655  1.00 93.08  ? 327  ARG   B NH2 1 
ATOM   5141  N  N   . LEU   B 2 328 ? 19.164  54.262  -1.417  1.00 77.77  ? 328  LEU   B N   1 
ATOM   5142  C  CA  . LEU   B 2 328 ? 18.311  55.104  -2.239  1.00 75.01  ? 328  LEU   B CA  1 
ATOM   5143  C  C   . LEU   B 2 328 ? 18.067  56.458  -1.593  1.00 79.89  ? 328  LEU   B C   1 
ATOM   5144  O  O   . LEU   B 2 328 ? 17.762  57.420  -2.300  1.00 79.80  ? 328  LEU   B O   1 
ATOM   5145  C  CB  . LEU   B 2 328 ? 16.981  54.420  -2.514  1.00 72.04  ? 328  LEU   B CB  1 
ATOM   5146  C  CG  . LEU   B 2 328 ? 17.151  53.046  -3.141  1.00 78.64  ? 328  LEU   B CG  1 
ATOM   5147  C  CD1 . LEU   B 2 328 ? 15.796  52.479  -3.625  1.00 69.97  ? 328  LEU   B CD1 1 
ATOM   5148  C  CD2 . LEU   B 2 328 ? 18.207  53.125  -4.256  1.00 74.54  ? 328  LEU   B CD2 1 
ATOM   5149  N  N   . GLY   B 2 329 ? 18.195  56.552  -0.272  1.00 76.74  ? 329  GLY   B N   1 
ATOM   5150  C  CA  . GLY   B 2 329 ? 17.935  57.783  0.436   1.00 77.46  ? 329  GLY   B CA  1 
ATOM   5151  C  C   . GLY   B 2 329 ? 18.892  57.988  1.595   1.00 85.30  ? 329  GLY   B C   1 
ATOM   5152  O  O   . GLY   B 2 329 ? 19.985  57.398  1.631   1.00 84.27  ? 329  GLY   B O   1 
ATOM   5153  N  N   . ASP   B 2 330 ? 18.504  58.832  2.554   1.00 82.39  ? 330  ASP   B N   1 
ATOM   5154  C  CA  . ASP   B 2 330 ? 19.383  59.100  3.681   1.00 81.62  ? 330  ASP   B CA  1 
ATOM   5155  C  C   . ASP   B 2 330 ? 19.339  57.934  4.663   1.00 82.25  ? 330  ASP   B C   1 
ATOM   5156  O  O   . ASP   B 2 330 ? 18.297  57.301  4.853   1.00 81.12  ? 330  ASP   B O   1 
ATOM   5157  C  CB  . ASP   B 2 330 ? 18.984  60.407  4.375   1.00 85.22  ? 330  ASP   B CB  1 
ATOM   5158  C  CG  . ASP   B 2 330 ? 19.568  61.654  3.694   1.00 84.40  ? 330  ASP   B CG  1 
ATOM   5159  O  OD1 . ASP   B 2 330 ? 19.973  61.582  2.518   1.00 85.98  ? 330  ASP   B OD1 1 
ATOM   5160  O  OD2 . ASP   B 2 330 ? 19.626  62.718  4.344   1.00 88.69  ? 330  ASP   B OD2 1 
ATOM   5161  N  N   . SER   B 2 331 ? 20.496  57.632  5.257   1.00 81.00  ? 331  SER   B N   1 
ATOM   5162  C  CA  . SER   B 2 331 ? 20.560  56.784  6.434   1.00 80.74  ? 331  SER   B CA  1 
ATOM   5163  C  C   . SER   B 2 331 ? 20.123  57.576  7.659   1.00 86.30  ? 331  SER   B C   1 
ATOM   5164  O  O   . SER   B 2 331 ? 20.157  58.807  7.675   1.00 86.51  ? 331  SER   B O   1 
ATOM   5165  C  CB  . SER   B 2 331 ? 21.966  56.230  6.644   1.00 85.39  ? 331  SER   B CB  1 
ATOM   5166  O  OG  . SER   B 2 331 ? 22.215  55.096  5.815   1.00 91.00  ? 331  SER   B OG  1 
ATOM   5167  N  N   . GLN   B 2 332 ? 19.711  56.857  8.698   1.00 89.00  ? 332  GLN   B N   1 
ATOM   5168  C  CA  . GLN   B 2 332 ? 19.052  57.511  9.818   1.00 84.85  ? 332  GLN   B CA  1 
ATOM   5169  C  C   . GLN   B 2 332 ? 19.173  56.633  11.057  1.00 89.28  ? 332  GLN   B C   1 
ATOM   5170  O  O   . GLN   B 2 332 ? 19.361  55.417  10.965  1.00 89.27  ? 332  GLN   B O   1 
ATOM   5171  C  CB  . GLN   B 2 332 ? 17.579  57.790  9.486   1.00 84.36  ? 332  GLN   B CB  1 
ATOM   5172  C  CG  . GLN   B 2 332 ? 16.812  56.540  9.022   1.00 88.63  ? 332  GLN   B CG  1 
ATOM   5173  C  CD  . GLN   B 2 332 ? 15.373  56.822  8.553   1.00 90.48  ? 332  GLN   B CD  1 
ATOM   5174  O  OE1 . GLN   B 2 332 ? 14.695  55.922  8.031   1.00 87.17  ? 332  GLN   B OE1 1 
ATOM   5175  N  NE2 . GLN   B 2 332 ? 14.901  58.063  8.746   1.00 89.73  ? 332  GLN   B NE2 1 
ATOM   5176  N  N   . LEU   B 2 333 ? 19.104  57.281  12.220  1.00 92.94  ? 333  LEU   B N   1 
ATOM   5177  C  CA  . LEU   B 2 333 ? 18.802  56.636  13.498  1.00 88.32  ? 333  LEU   B CA  1 
ATOM   5178  C  C   . LEU   B 2 333 ? 17.319  56.830  13.763  1.00 88.99  ? 333  LEU   B C   1 
ATOM   5179  O  O   . LEU   B 2 333 ? 16.804  57.938  13.602  1.00 93.75  ? 333  LEU   B O   1 
ATOM   5180  C  CB  . LEU   B 2 333 ? 19.613  57.245  14.643  1.00 83.91  ? 333  LEU   B CB  1 
ATOM   5181  C  CG  . LEU   B 2 333 ? 21.090  56.857  14.744  1.00 92.85  ? 333  LEU   B CG  1 
ATOM   5182  C  CD1 . LEU   B 2 333 ? 21.908  57.809  15.628  1.00 89.60  ? 333  LEU   B CD1 1 
ATOM   5183  C  CD2 . LEU   B 2 333 ? 21.163  55.442  15.280  1.00 95.34  ? 333  LEU   B CD2 1 
ATOM   5184  N  N   . VAL   B 2 334 ? 16.626  55.764  14.136  1.00 90.85  ? 334  VAL   B N   1 
ATOM   5185  C  CA  . VAL   B 2 334 ? 15.207  55.845  14.455  1.00 91.33  ? 334  VAL   B CA  1 
ATOM   5186  C  C   . VAL   B 2 334 ? 15.021  55.247  15.835  1.00 94.57  ? 334  VAL   B C   1 
ATOM   5187  O  O   . VAL   B 2 334 ? 15.663  54.245  16.164  1.00 98.04  ? 334  VAL   B O   1 
ATOM   5188  C  CB  . VAL   B 2 334 ? 14.338  55.099  13.426  1.00 92.14  ? 334  VAL   B CB  1 
ATOM   5189  C  CG1 . VAL   B 2 334 ? 14.692  55.532  12.010  1.00 90.99  ? 334  VAL   B CG1 1 
ATOM   5190  C  CG2 . VAL   B 2 334 ? 14.545  53.619  13.591  1.00 90.88  ? 334  VAL   B CG2 1 
ATOM   5191  N  N   . LYS   B 2 335 ? 14.167  55.864  16.651  1.00 96.84  ? 335  LYS   B N   1 
ATOM   5192  C  CA  . LYS   B 2 335 ? 13.850  55.348  17.977  1.00 99.25  ? 335  LYS   B CA  1 
ATOM   5193  C  C   . LYS   B 2 335 ? 12.550  54.562  17.897  1.00 101.82 ? 335  LYS   B C   1 
ATOM   5194  O  O   . LYS   B 2 335 ? 11.576  55.027  17.297  1.00 100.11 ? 335  LYS   B O   1 
ATOM   5195  C  CB  . LYS   B 2 335 ? 13.734  56.464  19.019  1.00 90.41  ? 335  LYS   B CB  1 
ATOM   5196  N  N   . LEU   B 2 336 ? 12.550  53.359  18.465  1.00 103.32 ? 336  LEU   B N   1 
ATOM   5197  C  CA  . LEU   B 2 336 ? 11.359  52.523  18.509  1.00 107.54 ? 336  LEU   B CA  1 
ATOM   5198  C  C   . LEU   B 2 336 ? 10.709  52.708  19.874  1.00 116.32 ? 336  LEU   B C   1 
ATOM   5199  O  O   . LEU   B 2 336 ? 11.304  52.366  20.900  1.00 123.29 ? 336  LEU   B O   1 
ATOM   5200  C  CB  . LEU   B 2 336 ? 11.698  51.056  18.264  1.00 106.38 ? 336  LEU   B CB  1 
ATOM   5201  C  CG  . LEU   B 2 336 ? 12.393  50.696  16.962  1.00 104.60 ? 336  LEU   B CG  1 
ATOM   5202  C  CD1 . LEU   B 2 336 ? 13.271  49.534  17.217  1.00 103.39 ? 336  LEU   B CD1 1 
ATOM   5203  C  CD2 . LEU   B 2 336 ? 11.405  50.317  15.890  1.00 104.26 ? 336  LEU   B CD2 1 
ATOM   5204  N  N   . ASN   B 2 337 ? 9.495   53.243  19.885  1.00 118.01 ? 337  ASN   B N   1 
ATOM   5205  C  CA  . ASN   B 2 337 ? 8.822   53.544  21.138  1.00 120.08 ? 337  ASN   B CA  1 
ATOM   5206  C  C   . ASN   B 2 337 ? 8.050   52.327  21.652  1.00 125.73 ? 337  ASN   B C   1 
ATOM   5207  O  O   . ASN   B 2 337 ? 7.858   51.329  20.947  1.00 125.43 ? 337  ASN   B O   1 
ATOM   5208  C  CB  . ASN   B 2 337 ? 7.898   54.758  20.966  1.00 121.18 ? 337  ASN   B CB  1 
ATOM   5209  C  CG  . ASN   B 2 337 ? 8.665   56.078  20.830  1.00 115.78 ? 337  ASN   B CG  1 
ATOM   5210  O  OD1 . ASN   B 2 337 ? 8.578   56.765  19.804  1.00 104.36 ? 337  ASN   B OD1 1 
ATOM   5211  N  ND2 . ASN   B 2 337 ? 9.421   56.435  21.876  1.00 112.64 ? 337  ASN   B ND2 1 
ATOM   5212  N  N   . VAL   B 2 338 ? 7.629   52.421  22.917  1.00 131.59 ? 338  VAL   B N   1 
ATOM   5213  C  CA  . VAL   B 2 338 ? 6.920   51.323  23.569  1.00 129.93 ? 338  VAL   B CA  1 
ATOM   5214  C  C   . VAL   B 2 338 ? 5.487   51.246  23.061  1.00 132.47 ? 338  VAL   B C   1 
ATOM   5215  O  O   . VAL   B 2 338 ? 4.979   50.165  22.730  1.00 132.67 ? 338  VAL   B O   1 
ATOM   5216  C  CB  . VAL   B 2 338 ? 6.972   51.497  25.097  1.00 123.70 ? 338  VAL   B CB  1 
ATOM   5217  N  N   . ASP   B 2 339 ? 4.821   52.396  22.978  1.00 136.10 ? 339  ASP   B N   1 
ATOM   5218  C  CA  . ASP   B 2 339 ? 3.507   52.517  22.361  1.00 136.78 ? 339  ASP   B CA  1 
ATOM   5219  C  C   . ASP   B 2 339 ? 3.648   52.952  20.902  1.00 135.40 ? 339  ASP   B C   1 
ATOM   5220  O  O   . ASP   B 2 339 ? 4.736   53.301  20.430  1.00 134.74 ? 339  ASP   B O   1 
ATOM   5221  C  CB  . ASP   B 2 339 ? 2.636   53.516  23.137  1.00 139.40 ? 339  ASP   B CB  1 
ATOM   5222  N  N   . SER   B 2 340 ? 2.530   52.915  20.190  1.00 136.93 ? 340  SER   B N   1 
ATOM   5223  C  CA  . SER   B 2 340 ? 2.476   53.395  18.811  1.00 138.28 ? 340  SER   B CA  1 
ATOM   5224  C  C   . SER   B 2 340 ? 2.140   54.891  18.803  1.00 145.91 ? 340  SER   B C   1 
ATOM   5225  O  O   . SER   B 2 340 ? 2.075   55.545  19.854  1.00 141.58 ? 340  SER   B O   1 
ATOM   5226  C  CB  . SER   B 2 340 ? 1.493   52.548  18.002  1.00 136.29 ? 340  SER   B CB  1 
ATOM   5227  O  OG  . SER   B 2 340 ? 0.147   52.957  18.205  1.00 143.85 ? 340  SER   B OG  1 
ATOM   5228  N  N   . ASN   B 2 341 ? 1.945   55.478  17.611  1.00 151.54 ? 341  ASN   B N   1 
ATOM   5229  C  CA  . ASN   B 2 341 ? 1.615   56.894  17.464  1.00 154.06 ? 341  ASN   B CA  1 
ATOM   5230  C  C   . ASN   B 2 341 ? 0.179   57.025  16.963  1.00 159.95 ? 341  ASN   B C   1 
ATOM   5231  O  O   . ASN   B 2 341 ? -0.586  56.053  16.963  1.00 156.77 ? 341  ASN   B O   1 
ATOM   5232  C  CB  . ASN   B 2 341 ? 2.643   57.621  16.564  1.00 154.58 ? 341  ASN   B CB  1 
ATOM   5233  C  CG  . ASN   B 2 341 ? 2.307   57.573  15.064  1.00 158.20 ? 341  ASN   B CG  1 
ATOM   5234  O  OD1 . ASN   B 2 341 ? 1.440   56.823  14.613  1.00 162.80 ? 341  ASN   B OD1 1 
ATOM   5235  N  ND2 . ASN   B 2 341 ? 3.028   58.379  14.283  1.00 157.28 ? 341  ASN   B ND2 1 
ATOM   5236  N  N   . GLU   B 2 342 ? -0.189  58.251  16.557  1.00 168.72 ? 342  GLU   B N   1 
ATOM   5237  C  CA  . GLU   B 2 342 ? -1.532  58.523  16.047  1.00 171.49 ? 342  GLU   B CA  1 
ATOM   5238  C  C   . GLU   B 2 342 ? -1.917  57.547  14.935  1.00 175.32 ? 342  GLU   B C   1 
ATOM   5239  O  O   . GLU   B 2 342 ? -2.939  56.855  15.023  1.00 178.23 ? 342  GLU   B O   1 
ATOM   5240  C  CB  . GLU   B 2 342 ? -1.615  59.973  15.559  1.00 168.73 ? 342  GLU   B CB  1 
ATOM   5241  N  N   . GLN   B 2 343 ? -1.105  57.487  13.871  1.00 175.62 ? 343  GLN   B N   1 
ATOM   5242  C  CA  . GLN   B 2 343 ? -1.293  56.470  12.835  1.00 171.33 ? 343  GLN   B CA  1 
ATOM   5243  C  C   . GLN   B 2 343 ? -1.021  55.066  13.384  1.00 169.77 ? 343  GLN   B C   1 
ATOM   5244  O  O   . GLN   B 2 343 ? -1.919  54.217  13.421  1.00 173.17 ? 343  GLN   B O   1 
ATOM   5245  C  CB  . GLN   B 2 343 ? -0.399  56.773  11.630  1.00 168.42 ? 343  GLN   B CB  1 
ATOM   5246  N  N   . GLY   B 2 344 ? 0.217   54.799  13.818  1.00 157.93 ? 344  GLY   B N   1 
ATOM   5247  C  CA  . GLY   B 2 344 ? 0.548   53.536  14.456  1.00 149.76 ? 344  GLY   B CA  1 
ATOM   5248  C  C   . GLY   B 2 344 ? 2.019   53.174  14.396  1.00 138.49 ? 344  GLY   B C   1 
ATOM   5249  O  O   . GLY   B 2 344 ? 2.408   52.026  14.651  1.00 132.43 ? 344  GLY   B O   1 
ATOM   5250  N  N   . SER   B 2 345 ? 2.855   54.147  14.071  1.00 133.75 ? 345  SER   B N   1 
ATOM   5251  C  CA  . SER   B 2 345 ? 4.280   53.918  13.900  1.00 121.90 ? 345  SER   B CA  1 
ATOM   5252  C  C   . SER   B 2 345 ? 4.975   54.013  15.253  1.00 120.92 ? 345  SER   B C   1 
ATOM   5253  O  O   . SER   B 2 345 ? 5.090   55.100  15.833  1.00 121.30 ? 345  SER   B O   1 
ATOM   5254  C  CB  . SER   B 2 345 ? 4.873   54.930  12.924  1.00 122.11 ? 345  SER   B CB  1 
ATOM   5255  O  OG  . SER   B 2 345 ? 6.276   54.758  12.802  1.00 114.83 ? 345  SER   B OG  1 
ATOM   5256  N  N   . TYR   B 2 346 ? 5.448   52.871  15.747  1.00 113.14 ? 346  TYR   B N   1 
ATOM   5257  C  CA  . TYR   B 2 346 ? 6.373   52.862  16.863  1.00 112.79 ? 346  TYR   B CA  1 
ATOM   5258  C  C   . TYR   B 2 346 ? 7.627   53.638  16.520  1.00 106.09 ? 346  TYR   B C   1 
ATOM   5259  O  O   . TYR   B 2 346 ? 8.446   53.896  17.401  1.00 105.83 ? 346  TYR   B O   1 
ATOM   5260  C  CB  . TYR   B 2 346 ? 6.634   51.432  17.344  1.00 115.30 ? 346  TYR   B CB  1 
ATOM   5261  C  CG  . TYR   B 2 346 ? 5.422   50.589  17.731  1.00 121.67 ? 346  TYR   B CG  1 
ATOM   5262  C  CD1 . TYR   B 2 346 ? 4.465   50.221  16.793  1.00 123.66 ? 346  TYR   B CD1 1 
ATOM   5263  C  CD2 . TYR   B 2 346 ? 5.271   50.112  19.025  1.00 128.74 ? 346  TYR   B CD2 1 
ATOM   5264  C  CE1 . TYR   B 2 346 ? 3.369   49.428  17.144  1.00 124.65 ? 346  TYR   B CE1 1 
ATOM   5265  C  CE2 . TYR   B 2 346 ? 4.174   49.316  19.388  1.00 131.63 ? 346  TYR   B CE2 1 
ATOM   5266  C  CZ  . TYR   B 2 346 ? 3.223   48.975  18.436  1.00 129.28 ? 346  TYR   B CZ  1 
ATOM   5267  O  OH  . TYR   B 2 346 ? 2.121   48.190  18.738  1.00 127.62 ? 346  TYR   B OH  1 
ATOM   5268  N  N   . VAL   B 2 347 ? 7.831   53.969  15.272  1.00 104.05 ? 347  VAL   B N   1 
ATOM   5269  C  CA  . VAL   B 2 347 ? 9.075   54.563  14.827  1.00 103.53 ? 347  VAL   B CA  1 
ATOM   5270  C  C   . VAL   B 2 347 ? 9.054   56.078  14.910  1.00 103.04 ? 347  VAL   B C   1 
ATOM   5271  O  O   . VAL   B 2 347 ? 8.011   56.708  14.698  1.00 106.13 ? 347  VAL   B O   1 
ATOM   5272  C  CB  . VAL   B 2 347 ? 9.314   54.070  13.388  1.00 102.12 ? 347  VAL   B CB  1 
ATOM   5273  C  CG1 . VAL   B 2 347 ? 10.644  54.612  12.835  1.00 100.91 ? 347  VAL   B CG1 1 
ATOM   5274  C  CG2 . VAL   B 2 347 ? 9.248   52.542  13.338  1.00 96.80  ? 347  VAL   B CG2 1 
ATOM   5275  N  N   . VAL   B 2 348 ? 10.188  56.670  15.265  1.00 97.05  ? 348  VAL   B N   1 
ATOM   5276  C  CA  . VAL   B 2 348 ? 10.332  58.116  15.191  1.00 97.37  ? 348  VAL   B CA  1 
ATOM   5277  C  C   . VAL   B 2 348 ? 11.767  58.402  14.781  1.00 98.55  ? 348  VAL   B C   1 
ATOM   5278  O  O   . VAL   B 2 348 ? 12.711  57.869  15.380  1.00 95.05  ? 348  VAL   B O   1 
ATOM   5279  C  CB  . VAL   B 2 348 ? 9.988   58.826  16.504  1.00 90.22  ? 348  VAL   B CB  1 
ATOM   5280  C  CG1 . VAL   B 2 348 ? 11.202  58.930  17.386  1.00 92.51  ? 348  VAL   B CG1 1 
ATOM   5281  C  CG2 . VAL   B 2 348 ? 9.472   60.185  16.195  1.00 97.32  ? 348  VAL   B CG2 1 
ATOM   5282  N  N   . ALA   B 2 349 ? 11.939  59.185  13.723  1.00 94.08  ? 349  ALA   B N   1 
ATOM   5283  C  CA  . ALA   B 2 349 ? 13.288  59.444  13.247  1.00 92.79  ? 349  ALA   B CA  1 
ATOM   5284  C  C   . ALA   B 2 349 ? 14.013  60.326  14.264  1.00 91.98  ? 349  ALA   B C   1 
ATOM   5285  O  O   . ALA   B 2 349 ? 13.547  61.418  14.594  1.00 92.68  ? 349  ALA   B O   1 
ATOM   5286  C  CB  . ALA   B 2 349 ? 13.236  60.085  11.865  1.00 88.52  ? 349  ALA   B CB  1 
ATOM   5287  N  N   . MET   B 2 350 ? 15.130  59.850  14.803  1.00 89.58  ? 350  MET   B N   1 
ATOM   5288  C  CA  . MET   B 2 350 ? 15.837  60.625  15.806  1.00 89.09  ? 350  MET   B CA  1 
ATOM   5289  C  C   . MET   B 2 350 ? 17.155  61.201  15.303  1.00 90.85  ? 350  MET   B C   1 
ATOM   5290  O  O   . MET   B 2 350 ? 17.808  61.940  16.045  1.00 98.68  ? 350  MET   B O   1 
ATOM   5291  C  CB  . MET   B 2 350 ? 16.068  59.785  17.065  1.00 86.72  ? 350  MET   B CB  1 
ATOM   5292  C  CG  . MET   B 2 350 ? 17.307  58.947  17.030  1.00 95.15  ? 350  MET   B CG  1 
ATOM   5293  S  SD  . MET   B 2 350 ? 17.549  58.045  18.586  1.00 102.86 ? 350  MET   B SD  1 
ATOM   5294  C  CE  . MET   B 2 350 ? 19.063  58.807  19.219  1.00 97.57  ? 350  MET   B CE  1 
ATOM   5295  N  N   . GLU   B 2 351 ? 17.557  60.892  14.070  1.00 91.06  ? 351  GLU   B N   1 
ATOM   5296  C  CA  . GLU   B 2 351 ? 18.696  61.503  13.382  1.00 88.29  ? 351  GLU   B CA  1 
ATOM   5297  C  C   . GLU   B 2 351 ? 18.566  61.167  11.907  1.00 87.27  ? 351  GLU   B C   1 
ATOM   5298  O  O   . GLU   B 2 351 ? 17.751  60.331  11.514  1.00 87.91  ? 351  GLU   B O   1 
ATOM   5299  C  CB  . GLU   B 2 351 ? 20.048  61.011  13.894  1.00 87.41  ? 351  GLU   B CB  1 
ATOM   5300  C  CG  . GLU   B 2 351 ? 20.826  62.048  14.692  1.00 96.70  ? 351  GLU   B CG  1 
ATOM   5301  C  CD  . GLU   B 2 351 ? 22.342  61.815  14.656  1.00 103.15 ? 351  GLU   B CD  1 
ATOM   5302  O  OE1 . GLU   B 2 351 ? 22.891  61.074  15.522  1.00 102.26 ? 351  GLU   B OE1 1 
ATOM   5303  O  OE2 . GLU   B 2 351 ? 22.987  62.391  13.750  1.00 105.86 ? 351  GLU   B OE2 1 
ATOM   5304  N  N   . THR   B 2 352 ? 19.405  61.803  11.097  1.00 88.00  ? 352  THR   B N   1 
ATOM   5305  C  CA  . THR   B 2 352 ? 19.542  61.428  9.696   1.00 87.40  ? 352  THR   B CA  1 
ATOM   5306  C  C   . THR   B 2 352 ? 20.969  61.688  9.246   1.00 87.13  ? 352  THR   B C   1 
ATOM   5307  O  O   . THR   B 2 352 ? 21.683  62.499  9.844   1.00 93.54  ? 352  THR   B O   1 
ATOM   5308  C  CB  . THR   B 2 352 ? 18.597  62.206  8.793   1.00 81.65  ? 352  THR   B CB  1 
ATOM   5309  O  OG1 . THR   B 2 352 ? 18.931  63.587  8.913   1.00 89.87  ? 352  THR   B OG1 1 
ATOM   5310  C  CG2 . THR   B 2 352 ? 17.146  61.976  9.197   1.00 79.46  ? 352  THR   B CG2 1 
ATOM   5311  N  N   . PHE   B 2 353 ? 21.362  61.023  8.158   1.00 86.09  ? 353  PHE   B N   1 
ATOM   5312  C  CA  . PHE   B 2 353 ? 22.700  61.150  7.586   1.00 87.06  ? 353  PHE   B CA  1 
ATOM   5313  C  C   . PHE   B 2 353 ? 22.614  61.336  6.079   1.00 88.91  ? 353  PHE   B C   1 
ATOM   5314  O  O   . PHE   B 2 353 ? 21.915  60.583  5.389   1.00 89.06  ? 353  PHE   B O   1 
ATOM   5315  C  CB  . PHE   B 2 353 ? 23.555  59.933  7.916   1.00 87.06  ? 353  PHE   B CB  1 
ATOM   5316  C  CG  . PHE   B 2 353 ? 23.678  59.683  9.374   1.00 86.21  ? 353  PHE   B CG  1 
ATOM   5317  C  CD1 . PHE   B 2 353 ? 24.675  60.284  10.098  1.00 85.65  ? 353  PHE   B CD1 1 
ATOM   5318  C  CD2 . PHE   B 2 353 ? 22.775  58.872  10.025  1.00 84.23  ? 353  PHE   B CD2 1 
ATOM   5319  C  CE1 . PHE   B 2 353 ? 24.784  60.059  11.446  1.00 90.11  ? 353  PHE   B CE1 1 
ATOM   5320  C  CE2 . PHE   B 2 353 ? 22.882  58.651  11.360  1.00 86.03  ? 353  PHE   B CE2 1 
ATOM   5321  C  CZ  . PHE   B 2 353 ? 23.888  59.242  12.078  1.00 86.12  ? 353  PHE   B CZ  1 
ATOM   5322  N  N   . THR   B 2 354 ? 23.330  62.331  5.570   1.00 86.54  ? 354  THR   B N   1 
ATOM   5323  C  CA  . THR   B 2 354 ? 23.171  62.689  4.174   1.00 85.15  ? 354  THR   B CA  1 
ATOM   5324  C  C   . THR   B 2 354 ? 23.684  61.593  3.259   1.00 83.35  ? 354  THR   B C   1 
ATOM   5325  O  O   . THR   B 2 354 ? 24.759  61.023  3.473   1.00 82.34  ? 354  THR   B O   1 
ATOM   5326  C  CB  . THR   B 2 354 ? 23.884  63.993  3.895   1.00 85.93  ? 354  THR   B CB  1 
ATOM   5327  O  OG1 . THR   B 2 354 ? 23.285  64.989  4.719   1.00 99.39  ? 354  THR   B OG1 1 
ATOM   5328  C  CG2 . THR   B 2 354 ? 23.703  64.391  2.445   1.00 82.83  ? 354  THR   B CG2 1 
ATOM   5329  N  N   . ASN   B 2 355 ? 22.887  61.286  2.244   1.00 79.94  ? 355  ASN   B N   1 
ATOM   5330  C  CA  . ASN   B 2 355 ? 23.284  60.385  1.172   1.00 79.74  ? 355  ASN   B CA  1 
ATOM   5331  C  C   . ASN   B 2 355 ? 22.896  61.043  -0.143  1.00 81.45  ? 355  ASN   B C   1 
ATOM   5332  O  O   . ASN   B 2 355 ? 21.709  61.273  -0.383  1.00 83.48  ? 355  ASN   B O   1 
ATOM   5333  C  CB  . ASN   B 2 355 ? 22.615  59.015  1.324   1.00 81.42  ? 355  ASN   B CB  1 
ATOM   5334  C  CG  . ASN   B 2 355 ? 22.832  58.130  0.115   1.00 83.90  ? 355  ASN   B CG  1 
ATOM   5335  O  OD1 . ASN   B 2 355 ? 23.802  58.299  -0.626  1.00 81.73  ? 355  ASN   B OD1 1 
ATOM   5336  N  ND2 . ASN   B 2 355 ? 21.913  57.184  -0.105  1.00 82.71  ? 355  ASN   B ND2 1 
ATOM   5337  N  N   . LEU   B 2 356 ? 23.879  61.374  -0.981  1.00 80.90  ? 356  LEU   B N   1 
ATOM   5338  C  CA  . LEU   B 2 356 ? 23.585  61.950  -2.289  1.00 79.10  ? 356  LEU   B CA  1 
ATOM   5339  C  C   . LEU   B 2 356 ? 23.360  60.900  -3.360  1.00 82.00  ? 356  LEU   B C   1 
ATOM   5340  O  O   . LEU   B 2 356 ? 23.089  61.265  -4.509  1.00 84.76  ? 356  LEU   B O   1 
ATOM   5341  C  CB  . LEU   B 2 356 ? 24.707  62.861  -2.747  1.00 79.77  ? 356  LEU   B CB  1 
ATOM   5342  C  CG  . LEU   B 2 356 ? 25.428  63.542  -1.621  1.00 75.66  ? 356  LEU   B CG  1 
ATOM   5343  C  CD1 . LEU   B 2 356 ? 26.539  64.286  -2.264  1.00 80.68  ? 356  LEU   B CD1 1 
ATOM   5344  C  CD2 . LEU   B 2 356 ? 24.458  64.473  -0.989  1.00 80.79  ? 356  LEU   B CD2 1 
ATOM   5345  N  N   . GLY   B 2 357 ? 23.492  59.617  -3.029  1.00 81.72  ? 357  GLY   B N   1 
ATOM   5346  C  CA  . GLY   B 2 357 ? 23.258  58.564  -3.986  1.00 77.89  ? 357  GLY   B CA  1 
ATOM   5347  C  C   . GLY   B 2 357 ? 21.823  58.065  -4.044  1.00 79.82  ? 357  GLY   B C   1 
ATOM   5348  O  O   . GLY   B 2 357 ? 21.043  58.192  -3.086  1.00 80.31  ? 357  GLY   B O   1 
ATOM   5349  N  N   . PRO   B 2 358 ? 21.439  57.503  -5.209  1.00 80.25  ? 358  PRO   B N   1 
ATOM   5350  C  CA  . PRO   B 2 358 ? 22.198  57.568  -6.471  1.00 80.45  ? 358  PRO   B CA  1 
ATOM   5351  C  C   . PRO   B 2 358 ? 22.132  58.977  -7.069  1.00 80.35  ? 358  PRO   B C   1 
ATOM   5352  O  O   . PRO   B 2 358 ? 21.118  59.665  -6.941  1.00 76.03  ? 358  PRO   B O   1 
ATOM   5353  C  CB  . PRO   B 2 358 ? 21.514  56.506  -7.362  1.00 77.23  ? 358  PRO   B CB  1 
ATOM   5354  C  CG  . PRO   B 2 358 ? 20.164  56.266  -6.748  1.00 75.15  ? 358  PRO   B CG  1 
ATOM   5355  C  CD  . PRO   B 2 358 ? 20.394  56.464  -5.260  1.00 76.82  ? 358  PRO   B CD  1 
ATOM   5356  N  N   . ILE   B 2 359 ? 23.227  59.423  -7.684  1.00 82.41  ? 359  ILE   B N   1 
ATOM   5357  C  CA  . ILE   B 2 359 ? 23.270  60.673  -8.431  1.00 82.39  ? 359  ILE   B CA  1 
ATOM   5358  C  C   . ILE   B 2 359 ? 22.953  60.321  -9.880  1.00 84.37  ? 359  ILE   B C   1 
ATOM   5359  O  O   . ILE   B 2 359 ? 23.826  59.845  -10.620 1.00 85.02  ? 359  ILE   B O   1 
ATOM   5360  C  CB  . ILE   B 2 359 ? 24.632  61.357  -8.315  1.00 83.95  ? 359  ILE   B CB  1 
ATOM   5361  C  CG1 . ILE   B 2 359 ? 24.893  61.845  -6.885  1.00 83.80  ? 359  ILE   B CG1 1 
ATOM   5362  C  CG2 . ILE   B 2 359 ? 24.709  62.534  -9.290  1.00 85.98  ? 359  ILE   B CG2 1 
ATOM   5363  C  CD1 . ILE   B 2 359 ? 24.305  63.248  -6.596  1.00 86.20  ? 359  ILE   B CD1 1 
ATOM   5364  N  N   . VAL   B 2 360 ? 21.705  60.549  -10.289 1.00 80.96  ? 360  VAL   B N   1 
ATOM   5365  C  CA  . VAL   B 2 360 ? 21.285  60.174  -11.638 1.00 80.22  ? 360  VAL   B CA  1 
ATOM   5366  C  C   . VAL   B 2 360 ? 21.615  61.264  -12.653 1.00 82.28  ? 360  VAL   B C   1 
ATOM   5367  O  O   . VAL   B 2 360 ? 22.111  60.959  -13.739 1.00 87.69  ? 360  VAL   B O   1 
ATOM   5368  C  CB  . VAL   B 2 360 ? 19.788  59.802  -11.655 1.00 76.23  ? 360  VAL   B CB  1 
ATOM   5369  C  CG1 . VAL   B 2 360 ? 19.564  58.545  -10.808 1.00 78.06  ? 360  VAL   B CG1 1 
ATOM   5370  C  CG2 . VAL   B 2 360 ? 18.934  60.950  -11.179 1.00 72.98  ? 360  VAL   B CG2 1 
ATOM   5371  N  N   . ASP   B 2 361 ? 21.363  62.533  -12.315 1.00 82.74  ? 361  ASP   B N   1 
ATOM   5372  C  CA  . ASP   B 2 361 ? 21.734  63.684  -13.134 1.00 80.57  ? 361  ASP   B CA  1 
ATOM   5373  C  C   . ASP   B 2 361 ? 22.224  64.806  -12.222 1.00 84.05  ? 361  ASP   B C   1 
ATOM   5374  O  O   . ASP   B 2 361 ? 21.877  64.862  -11.037 1.00 79.23  ? 361  ASP   B O   1 
ATOM   5375  C  CB  . ASP   B 2 361 ? 20.552  64.176  -13.992 1.00 80.76  ? 361  ASP   B CB  1 
ATOM   5376  C  CG  . ASP   B 2 361 ? 20.995  65.117  -15.129 1.00 87.02  ? 361  ASP   B CG  1 
ATOM   5377  O  OD1 . ASP   B 2 361 ? 22.227  65.175  -15.399 1.00 82.92  ? 361  ASP   B OD1 1 
ATOM   5378  O  OD2 . ASP   B 2 361 ? 20.113  65.780  -15.760 1.00 82.93  ? 361  ASP   B OD2 1 
ATOM   5379  N  N   . MET   B 2 362 ? 23.032  65.709  -12.790 1.00 84.80  ? 362  MET   B N   1 
ATOM   5380  C  CA  . MET   B 2 362 ? 23.488  66.890  -12.064 1.00 84.60  ? 362  MET   B CA  1 
ATOM   5381  C  C   . MET   B 2 362 ? 23.738  68.032  -13.057 1.00 83.78  ? 362  MET   B C   1 
ATOM   5382  O  O   . MET   B 2 362 ? 23.724  67.843  -14.274 1.00 81.49  ? 362  MET   B O   1 
ATOM   5383  C  CB  . MET   B 2 362 ? 24.737  66.560  -11.207 1.00 83.23  ? 362  MET   B CB  1 
ATOM   5384  C  CG  . MET   B 2 362 ? 26.090  66.673  -11.943 1.00 87.61  ? 362  MET   B CG  1 
ATOM   5385  S  SD  . MET   B 2 362 ? 27.495  65.689  -11.285 1.00 87.77  ? 362  MET   B SD  1 
ATOM   5386  C  CE  . MET   B 2 362 ? 27.106  65.626  -9.539  1.00 86.48  ? 362  MET   B CE  1 
ATOM   5387  N  N   . CYS   B 2 363 ? 23.919  69.237  -12.521 1.00 87.19  ? 363  CYS   B N   1 
ATOM   5388  C  CA  . CYS   B 2 363 ? 24.295  70.401  -13.312 1.00 86.67  ? 363  CYS   B CA  1 
ATOM   5389  C  C   . CYS   B 2 363 ? 25.005  71.365  -12.391 1.00 86.02  ? 363  CYS   B C   1 
ATOM   5390  O  O   . CYS   B 2 363 ? 24.760  71.371  -11.180 1.00 86.77  ? 363  CYS   B O   1 
ATOM   5391  C  CB  . CYS   B 2 363 ? 23.100  71.112  -13.915 1.00 83.00  ? 363  CYS   B CB  1 
ATOM   5392  S  SG  . CYS   B 2 363 ? 22.158  71.824  -12.573 1.00 90.45  ? 363  CYS   B SG  1 
ATOM   5393  N  N   . VAL   B 2 364 ? 25.882  72.180  -12.964 1.00 87.84  ? 364  VAL   B N   1 
ATOM   5394  C  CA  . VAL   B 2 364 ? 26.656  73.151  -12.197 1.00 91.43  ? 364  VAL   B CA  1 
ATOM   5395  C  C   . VAL   B 2 364 ? 26.121  74.544  -12.502 1.00 91.29  ? 364  VAL   B C   1 
ATOM   5396  O  O   . VAL   B 2 364 ? 25.777  74.849  -13.649 1.00 91.43  ? 364  VAL   B O   1 
ATOM   5397  C  CB  . VAL   B 2 364 ? 28.158  73.034  -12.509 1.00 91.97  ? 364  VAL   B CB  1 
ATOM   5398  C  CG1 . VAL   B 2 364 ? 28.353  72.718  -14.004 1.00 95.09  ? 364  VAL   B CG1 1 
ATOM   5399  C  CG2 . VAL   B 2 364 ? 28.903  74.302  -12.060 1.00 91.87  ? 364  VAL   B CG2 1 
ATOM   5400  N  N   . VAL   B 2 365 ? 26.022  75.380  -11.474 1.00 94.10  ? 365  VAL   B N   1 
ATOM   5401  C  CA  . VAL   B 2 365 ? 25.265  76.621  -11.581 1.00 95.42  ? 365  VAL   B CA  1 
ATOM   5402  C  C   . VAL   B 2 365 ? 25.754  77.594  -10.518 1.00 102.09 ? 365  VAL   B C   1 
ATOM   5403  O  O   . VAL   B 2 365 ? 25.946  77.227  -9.358  1.00 102.32 ? 365  VAL   B O   1 
ATOM   5404  C  CB  . VAL   B 2 365 ? 23.746  76.363  -11.447 1.00 97.33  ? 365  VAL   B CB  1 
ATOM   5405  C  CG1 . VAL   B 2 365 ? 22.988  77.689  -11.411 1.00 101.47 ? 365  VAL   B CG1 1 
ATOM   5406  C  CG2 . VAL   B 2 365 ? 23.227  75.476  -12.596 1.00 90.18  ? 365  VAL   B CG2 1 
ATOM   5407  N  N   . ASP   B 2 366 ? 25.926  78.851  -10.923 1.00 105.44 ? 366  ASP   B N   1 
ATOM   5408  C  CA  . ASP   B 2 366 ? 26.338  79.932  -10.027 1.00 110.95 ? 366  ASP   B CA  1 
ATOM   5409  C  C   . ASP   B 2 366 ? 25.089  80.699  -9.599  1.00 112.40 ? 366  ASP   B C   1 
ATOM   5410  O  O   . ASP   B 2 366 ? 24.704  81.689  -10.216 1.00 113.92 ? 366  ASP   B O   1 
ATOM   5411  C  CB  . ASP   B 2 366 ? 27.347  80.841  -10.718 1.00 118.05 ? 366  ASP   B CB  1 
ATOM   5412  C  CG  . ASP   B 2 366 ? 27.940  81.889  -9.780  1.00 129.02 ? 366  ASP   B CG  1 
ATOM   5413  O  OD1 . ASP   B 2 366 ? 27.317  82.184  -8.734  1.00 132.59 ? 366  ASP   B OD1 1 
ATOM   5414  O  OD2 . ASP   B 2 366 ? 29.030  82.427  -10.104 1.00 132.66 ? 366  ASP   B OD2 1 
ATOM   5415  N  N   . LEU   B 2 367 ? 24.462  80.235  -8.511  1.00 113.98 ? 367  LEU   B N   1 
ATOM   5416  C  CA  . LEU   B 2 367 ? 23.233  80.847  -8.004  1.00 114.84 ? 367  LEU   B CA  1 
ATOM   5417  C  C   . LEU   B 2 367 ? 23.468  82.204  -7.362  1.00 121.45 ? 367  LEU   B C   1 
ATOM   5418  O  O   . LEU   B 2 367 ? 22.543  83.022  -7.295  1.00 126.08 ? 367  LEU   B O   1 
ATOM   5419  C  CB  . LEU   B 2 367 ? 22.569  79.940  -6.966  1.00 117.84 ? 367  LEU   B CB  1 
ATOM   5420  C  CG  . LEU   B 2 367 ? 21.458  78.960  -7.348  1.00 114.93 ? 367  LEU   B CG  1 
ATOM   5421  C  CD1 . LEU   B 2 367 ? 21.799  78.314  -8.702  1.00 107.66 ? 367  LEU   B CD1 1 
ATOM   5422  C  CD2 . LEU   B 2 367 ? 21.316  77.906  -6.260  1.00 108.26 ? 367  LEU   B CD2 1 
ATOM   5423  N  N   . GLU   B 2 368 ? 24.655  82.448  -6.826  1.00 123.54 ? 368  GLU   B N   1 
ATOM   5424  C  CA  . GLU   B 2 368 ? 24.904  83.698  -6.130  1.00 125.32 ? 368  GLU   B CA  1 
ATOM   5425  C  C   . GLU   B 2 368 ? 25.668  84.696  -6.983  1.00 127.37 ? 368  GLU   B C   1 
ATOM   5426  O  O   . GLU   B 2 368 ? 26.017  85.770  -6.492  1.00 129.15 ? 368  GLU   B O   1 
ATOM   5427  C  CB  . GLU   B 2 368 ? 25.635  83.419  -4.817  1.00 127.74 ? 368  GLU   B CB  1 
ATOM   5428  C  CG  . GLU   B 2 368 ? 24.768  82.620  -3.842  1.00 123.11 ? 368  GLU   B CG  1 
ATOM   5429  C  CD  . GLU   B 2 368 ? 25.567  81.913  -2.757  1.00 129.62 ? 368  GLU   B CD  1 
ATOM   5430  O  OE1 . GLU   B 2 368 ? 26.616  82.457  -2.331  1.00 133.18 ? 368  GLU   B OE1 1 
ATOM   5431  O  OE2 . GLU   B 2 368 ? 25.149  80.803  -2.345  1.00 127.86 ? 368  GLU   B OE2 1 
ATOM   5432  N  N   . ARG   B 2 369 ? 25.904  84.381  -8.254  1.00 129.07 ? 369  ARG   B N   1 
ATOM   5433  C  CA  . ARG   B 2 369 ? 26.618  85.281  -9.146  1.00 130.74 ? 369  ARG   B CA  1 
ATOM   5434  C  C   . ARG   B 2 369 ? 27.944  85.707  -8.521  1.00 139.07 ? 369  ARG   B C   1 
ATOM   5435  O  O   . ARG   B 2 369 ? 28.337  86.876  -8.569  1.00 135.56 ? 369  ARG   B O   1 
ATOM   5436  C  CB  . ARG   B 2 369 ? 25.746  86.485  -9.499  1.00 128.90 ? 369  ARG   B CB  1 
ATOM   5437  C  CG  . ARG   B 2 369 ? 25.001  86.349  -10.827 1.00 132.06 ? 369  ARG   B CG  1 
ATOM   5438  C  CD  . ARG   B 2 369 ? 25.617  87.253  -11.918 1.00 139.61 ? 369  ARG   B CD  1 
ATOM   5439  N  NE  . ARG   B 2 369 ? 24.967  87.128  -13.223 1.00 141.59 ? 369  ARG   B NE  1 
ATOM   5440  C  CZ  . ARG   B 2 369 ? 25.568  87.334  -14.392 1.00 143.97 ? 369  ARG   B CZ  1 
ATOM   5441  N  NH1 . ARG   B 2 369 ? 26.859  87.628  -14.468 1.00 144.51 ? 369  ARG   B NH1 1 
ATOM   5442  N  NH2 . ARG   B 2 369 ? 24.858  87.239  -15.515 1.00 139.33 ? 369  ARG   B NH2 1 
ATOM   5443  N  N   . GLN   B 2 370 ? 28.629  84.739  -7.910  1.00 152.62 ? 370  GLN   B N   1 
ATOM   5444  C  CA  . GLN   B 2 370 ? 29.877  84.975  -7.190  1.00 154.64 ? 370  GLN   B CA  1 
ATOM   5445  C  C   . GLN   B 2 370 ? 31.102  84.437  -7.902  1.00 154.44 ? 370  GLN   B C   1 
ATOM   5446  O  O   . GLN   B 2 370 ? 32.222  84.689  -7.444  1.00 156.56 ? 370  GLN   B O   1 
ATOM   5447  C  CB  . GLN   B 2 370 ? 29.829  84.324  -5.802  1.00 156.03 ? 370  GLN   B CB  1 
ATOM   5448  C  CG  . GLN   B 2 370 ? 28.627  84.698  -4.965  1.00 157.46 ? 370  GLN   B CG  1 
ATOM   5449  C  CD  . GLN   B 2 370 ? 28.555  86.187  -4.633  1.00 157.22 ? 370  GLN   B CD  1 
ATOM   5450  O  OE1 . GLN   B 2 370 ? 29.554  86.909  -4.696  1.00 156.81 ? 370  GLN   B OE1 1 
ATOM   5451  N  NE2 . GLN   B 2 370 ? 27.359  86.648  -4.273  1.00 151.77 ? 370  GLN   B NE2 1 
ATOM   5452  N  N   . GLY   B 2 371 ? 30.925  83.689  -8.985  1.00 143.18 ? 371  GLY   B N   1 
ATOM   5453  C  CA  . GLY   B 2 371 ? 32.054  83.079  -9.641  1.00 135.85 ? 371  GLY   B CA  1 
ATOM   5454  C  C   . GLY   B 2 371 ? 32.530  81.823  -8.963  1.00 134.78 ? 371  GLY   B C   1 
ATOM   5455  O  O   . GLY   B 2 371 ? 33.660  81.380  -9.209  1.00 127.97 ? 371  GLY   B O   1 
ATOM   5456  N  N   . GLN   B 2 372 ? 31.709  81.236  -8.102  1.00 132.27 ? 372  GLN   B N   1 
ATOM   5457  C  CA  . GLN   B 2 372 ? 32.067  79.989  -7.447  1.00 128.91 ? 372  GLN   B CA  1 
ATOM   5458  C  C   . GLN   B 2 372 ? 31.466  78.830  -8.224  1.00 127.64 ? 372  GLN   B C   1 
ATOM   5459  O  O   . GLN   B 2 372 ? 32.164  78.148  -8.985  1.00 127.71 ? 372  GLN   B O   1 
ATOM   5460  C  CB  . GLN   B 2 372 ? 31.580  79.979  -5.996  1.00 129.81 ? 372  GLN   B CB  1 
ATOM   5461  C  CG  . GLN   B 2 372 ? 32.376  79.067  -5.067  1.00 131.18 ? 372  GLN   B CG  1 
ATOM   5462  C  CD  . GLN   B 2 372 ? 33.874  79.344  -5.117  1.00 132.76 ? 372  GLN   B CD  1 
ATOM   5463  O  OE1 . GLN   B 2 372 ? 34.497  79.265  -6.176  1.00 132.41 ? 372  GLN   B OE1 1 
ATOM   5464  N  NE2 . GLN   B 2 372 ? 34.453  79.689  -3.973  1.00 134.35 ? 372  GLN   B NE2 1 
ATOM   5465  N  N   . GLY   B 2 373 ? 30.166  78.610  -8.044  1.00 121.77 ? 373  GLY   B N   1 
ATOM   5466  C  CA  . GLY   B 2 373 ? 29.515  77.471  -8.667  1.00 117.19 ? 373  GLY   B CA  1 
ATOM   5467  C  C   . GLY   B 2 373 ? 29.098  76.361  -7.714  1.00 108.41 ? 373  GLY   B C   1 
ATOM   5468  O  O   . GLY   B 2 373 ? 29.946  75.651  -7.160  1.00 103.47 ? 373  GLY   B O   1 
ATOM   5469  N  N   . GLN   B 2 374 ? 27.782  76.223  -7.520  1.00 104.56 ? 374  GLN   B N   1 
ATOM   5470  C  CA  . GLN   B 2 374 ? 27.125  75.154  -6.778  1.00 98.62  ? 374  GLN   B CA  1 
ATOM   5471  C  C   . GLN   B 2 374 ? 26.721  74.017  -7.721  1.00 97.61  ? 374  GLN   B C   1 
ATOM   5472  O  O   . GLN   B 2 374 ? 26.579  74.200  -8.931  1.00 98.37  ? 374  GLN   B O   1 
ATOM   5473  C  CB  . GLN   B 2 374 ? 25.888  75.691  -6.045  1.00 96.53  ? 374  GLN   B CB  1 
ATOM   5474  C  CG  . GLN   B 2 374 ? 26.202  76.380  -4.716  1.00 104.05 ? 374  GLN   B CG  1 
ATOM   5475  C  CD  . GLN   B 2 374 ? 25.067  77.280  -4.193  1.00 113.54 ? 374  GLN   B CD  1 
ATOM   5476  O  OE1 . GLN   B 2 374 ? 24.655  78.236  -4.855  1.00 114.83 ? 374  GLN   B OE1 1 
ATOM   5477  N  NE2 . GLN   B 2 374 ? 24.574  76.978  -2.994  1.00 115.92 ? 374  GLN   B NE2 1 
ATOM   5478  N  N   . LEU   B 2 375 ? 26.518  72.831  -7.151  1.00 96.09  ? 375  LEU   B N   1 
ATOM   5479  C  CA  . LEU   B 2 375 ? 26.126  71.659  -7.923  1.00 88.75  ? 375  LEU   B CA  1 
ATOM   5480  C  C   . LEU   B 2 375 ? 24.749  71.204  -7.458  1.00 86.88  ? 375  LEU   B C   1 
ATOM   5481  O  O   . LEU   B 2 375 ? 24.529  71.027  -6.254  1.00 89.60  ? 375  LEU   B O   1 
ATOM   5482  C  CB  . LEU   B 2 375 ? 27.174  70.548  -7.770  1.00 90.06  ? 375  LEU   B CB  1 
ATOM   5483  C  CG  . LEU   B 2 375 ? 27.227  69.344  -8.732  1.00 89.36  ? 375  LEU   B CG  1 
ATOM   5484  C  CD1 . LEU   B 2 375 ? 27.158  69.753  -10.212 1.00 89.57  ? 375  LEU   B CD1 1 
ATOM   5485  C  CD2 . LEU   B 2 375 ? 28.466  68.449  -8.467  1.00 84.31  ? 375  LEU   B CD2 1 
ATOM   5486  N  N   . VAL   B 2 376 ? 23.812  71.065  -8.398  1.00 83.29  ? 376  VAL   B N   1 
ATOM   5487  C  CA  . VAL   B 2 376 ? 22.459  70.595  -8.101  1.00 84.53  ? 376  VAL   B CA  1 
ATOM   5488  C  C   . VAL   B 2 376 ? 22.284  69.210  -8.702  1.00 86.64  ? 376  VAL   B C   1 
ATOM   5489  O  O   . VAL   B 2 376 ? 22.479  69.029  -9.910  1.00 86.51  ? 376  VAL   B O   1 
ATOM   5490  C  CB  . VAL   B 2 376 ? 21.376  71.543  -8.640  1.00 84.52  ? 376  VAL   B CB  1 
ATOM   5491  C  CG1 . VAL   B 2 376 ? 20.018  71.088  -8.140  1.00 80.87  ? 376  VAL   B CG1 1 
ATOM   5492  C  CG2 . VAL   B 2 376 ? 21.651  72.998  -8.236  1.00 83.55  ? 376  VAL   B CG2 1 
ATOM   5493  N  N   . THR   B 2 377 ? 21.878  68.240  -7.872  1.00 84.47  ? 377  THR   B N   1 
ATOM   5494  C  CA  . THR   B 2 377 ? 21.824  66.831  -8.260  1.00 82.91  ? 377  THR   B CA  1 
ATOM   5495  C  C   . THR   B 2 377 ? 20.399  66.296  -8.234  1.00 82.37  ? 377  THR   B C   1 
ATOM   5496  O  O   . THR   B 2 377 ? 19.634  66.595  -7.308  1.00 81.74  ? 377  THR   B O   1 
ATOM   5497  C  CB  . THR   B 2 377 ? 22.683  65.940  -7.325  1.00 82.34  ? 377  THR   B CB  1 
ATOM   5498  O  OG1 . THR   B 2 377 ? 22.025  65.772  -6.063  1.00 74.69  ? 377  THR   B OG1 1 
ATOM   5499  C  CG2 . THR   B 2 377 ? 24.075  66.540  -7.117  1.00 80.41  ? 377  THR   B CG2 1 
ATOM   5500  N  N   . CYS   B 2 378 ? 20.046  65.487  -9.243  1.00 83.89  ? 378  CYS   B N   1 
ATOM   5501  C  CA  . CYS   B 2 378 ? 18.923  64.559  -9.101  1.00 79.21  ? 378  CYS   B CA  1 
ATOM   5502  C  C   . CYS   B 2 378 ? 19.393  63.414  -8.231  1.00 78.68  ? 378  CYS   B C   1 
ATOM   5503  O  O   . CYS   B 2 378 ? 20.276  62.661  -8.644  1.00 79.07  ? 378  CYS   B O   1 
ATOM   5504  C  CB  . CYS   B 2 378 ? 18.478  64.026  -10.452 1.00 76.39  ? 378  CYS   B CB  1 
ATOM   5505  S  SG  . CYS   B 2 378 ? 17.721  65.267  -11.456 1.00 83.81  ? 378  CYS   B SG  1 
ATOM   5506  N  N   . SER   B 2 379 ? 18.839  63.276  -7.027  1.00 77.28  ? 379  SER   B N   1 
ATOM   5507  C  CA  . SER   B 2 379 ? 19.375  62.308  -6.086  1.00 73.69  ? 379  SER   B CA  1 
ATOM   5508  C  C   . SER   B 2 379 ? 18.311  61.338  -5.596  1.00 76.79  ? 379  SER   B C   1 
ATOM   5509  O  O   . SER   B 2 379 ? 17.157  61.723  -5.362  1.00 75.06  ? 379  SER   B O   1 
ATOM   5510  C  CB  . SER   B 2 379 ? 20.032  63.009  -4.918  1.00 75.07  ? 379  SER   B CB  1 
ATOM   5511  O  OG  . SER   B 2 379 ? 21.160  63.732  -5.375  1.00 76.61  ? 379  SER   B OG  1 
ATOM   5512  N  N   . GLY   B 2 380 ? 18.728  60.060  -5.444  1.00 76.36  ? 380  GLY   B N   1 
ATOM   5513  C  CA  . GLY   B 2 380 ? 17.884  59.017  -4.879  1.00 73.97  ? 380  GLY   B CA  1 
ATOM   5514  C  C   . GLY   B 2 380 ? 16.761  58.569  -5.801  1.00 72.09  ? 380  GLY   B C   1 
ATOM   5515  O  O   . GLY   B 2 380 ? 16.690  58.940  -6.984  1.00 79.79  ? 380  GLY   B O   1 
ATOM   5516  N  N   . ALA   B 2 381 ? 15.851  57.769  -5.236  1.00 71.30  ? 381  ALA   B N   1 
ATOM   5517  C  CA  . ALA   B 2 381 ? 14.729  57.234  -6.001  1.00 70.09  ? 381  ALA   B CA  1 
ATOM   5518  C  C   . ALA   B 2 381 ? 13.518  57.065  -5.099  1.00 68.21  ? 381  ALA   B C   1 
ATOM   5519  O  O   . ALA   B 2 381 ? 13.641  56.921  -3.882  1.00 68.26  ? 381  ALA   B O   1 
ATOM   5520  C  CB  . ALA   B 2 381 ? 15.094  55.895  -6.673  1.00 68.55  ? 381  ALA   B CB  1 
ATOM   5521  N  N   . PHE   B 2 382 ? 12.347  57.057  -5.721  1.00 68.75  ? 382  PHE   B N   1 
ATOM   5522  C  CA  . PHE   B 2 382 ? 11.066  56.744  -5.051  1.00 75.54  ? 382  PHE   B CA  1 
ATOM   5523  C  C   . PHE   B 2 382 ? 10.867  57.768  -3.936  1.00 76.92  ? 382  PHE   B C   1 
ATOM   5524  O  O   . PHE   B 2 382 ? 11.050  58.975  -4.169  1.00 73.39  ? 382  PHE   B O   1 
ATOM   5525  C  CB  . PHE   B 2 382 ? 11.013  55.270  -4.578  1.00 70.84  ? 382  PHE   B CB  1 
ATOM   5526  C  CG  . PHE   B 2 382 ? 11.482  54.278  -5.623  1.00 71.57  ? 382  PHE   B CG  1 
ATOM   5527  C  CD1 . PHE   B 2 382 ? 10.783  54.110  -6.816  1.00 74.91  ? 382  PHE   B CD1 1 
ATOM   5528  C  CD2 . PHE   B 2 382 ? 12.630  53.541  -5.428  1.00 67.92  ? 382  PHE   B CD2 1 
ATOM   5529  C  CE1 . PHE   B 2 382 ? 11.228  53.219  -7.785  1.00 76.14  ? 382  PHE   B CE1 1 
ATOM   5530  C  CE2 . PHE   B 2 382 ? 13.074  52.642  -6.397  1.00 72.89  ? 382  PHE   B CE2 1 
ATOM   5531  C  CZ  . PHE   B 2 382 ? 12.382  52.478  -7.569  1.00 73.17  ? 382  PHE   B CZ  1 
ATOM   5532  N  N   . LYS   B 2 383 ? 10.482  57.324  -2.738  1.00 76.29  ? 383  LYS   B N   1 
ATOM   5533  C  CA  . LYS   B 2 383 ? 10.163  58.290  -1.706  1.00 77.42  ? 383  LYS   B CA  1 
ATOM   5534  C  C   . LYS   B 2 383 ? 11.405  59.049  -1.260  1.00 79.44  ? 383  LYS   B C   1 
ATOM   5535  O  O   . LYS   B 2 383 ? 11.293  60.166  -0.748  1.00 85.29  ? 383  LYS   B O   1 
ATOM   5536  C  CB  . LYS   B 2 383 ? 9.476   57.586  -0.525  1.00 79.96  ? 383  LYS   B CB  1 
ATOM   5537  C  CG  . LYS   B 2 383 ? 10.359  56.637  0.267   1.00 79.40  ? 383  LYS   B CG  1 
ATOM   5538  C  CD  . LYS   B 2 383 ? 9.489   55.572  0.900   1.00 81.86  ? 383  LYS   B CD  1 
ATOM   5539  C  CE  . LYS   B 2 383 ? 9.241   55.830  2.357   1.00 82.88  ? 383  LYS   B CE  1 
ATOM   5540  N  NZ  . LYS   B 2 383 ? 10.467  55.571  3.148   1.00 86.17  ? 383  LYS   B NZ  1 
ATOM   5541  N  N   . GLU   B 2 384 ? 12.591  58.498  -1.484  1.00 75.88  ? 384  GLU   B N   1 
ATOM   5542  C  CA  . GLU   B 2 384 ? 13.785  59.218  -1.085  1.00 76.18  ? 384  GLU   B CA  1 
ATOM   5543  C  C   . GLU   B 2 384 ? 14.255  60.232  -2.125  1.00 79.23  ? 384  GLU   B C   1 
ATOM   5544  O  O   . GLU   B 2 384 ? 15.176  61.004  -1.826  1.00 83.92  ? 384  GLU   B O   1 
ATOM   5545  C  CB  . GLU   B 2 384 ? 14.932  58.246  -0.779  1.00 77.99  ? 384  GLU   B CB  1 
ATOM   5546  C  CG  . GLU   B 2 384 ? 14.611  57.065  0.136   1.00 80.19  ? 384  GLU   B CG  1 
ATOM   5547  C  CD  . GLU   B 2 384 ? 14.000  57.454  1.468   1.00 87.86  ? 384  GLU   B CD  1 
ATOM   5548  O  OE1 . GLU   B 2 384 ? 14.313  58.558  2.019   1.00 87.17  ? 384  GLU   B OE1 1 
ATOM   5549  O  OE2 . GLU   B 2 384 ? 13.202  56.616  1.960   1.00 90.49  ? 384  GLU   B OE2 1 
ATOM   5550  N  N   . GLY   B 2 385 ? 13.665  60.258  -3.323  1.00 75.42  ? 385  GLY   B N   1 
ATOM   5551  C  CA  . GLY   B 2 385 ? 14.109  61.194  -4.354  1.00 75.99  ? 385  GLY   B CA  1 
ATOM   5552  C  C   . GLY   B 2 385 ? 14.205  62.644  -3.886  1.00 81.17  ? 385  GLY   B C   1 
ATOM   5553  O  O   . GLY   B 2 385 ? 13.403  63.093  -3.046  1.00 80.50  ? 385  GLY   B O   1 
ATOM   5554  N  N   . SER   B 2 386 ? 15.176  63.395  -4.413  1.00 76.97  ? 386  SER   B N   1 
ATOM   5555  C  CA  . SER   B 2 386 ? 15.426  64.746  -3.930  1.00 74.47  ? 386  SER   B CA  1 
ATOM   5556  C  C   . SER   B 2 386 ? 16.294  65.505  -4.922  1.00 77.20  ? 386  SER   B C   1 
ATOM   5557  O  O   . SER   B 2 386 ? 16.910  64.930  -5.825  1.00 78.28  ? 386  SER   B O   1 
ATOM   5558  C  CB  . SER   B 2 386 ? 16.117  64.720  -2.564  1.00 77.58  ? 386  SER   B CB  1 
ATOM   5559  O  OG  . SER   B 2 386 ? 17.468  64.259  -2.696  1.00 78.69  ? 386  SER   B OG  1 
ATOM   5560  N  N   . LEU   B 2 387 ? 16.358  66.816  -4.713  1.00 76.44  ? 387  LEU   B N   1 
ATOM   5561  C  CA  . LEU   B 2 387 ? 17.443  67.640  -5.223  1.00 75.62  ? 387  LEU   B CA  1 
ATOM   5562  C  C   . LEU   B 2 387 ? 18.428  67.859  -4.092  1.00 73.59  ? 387  LEU   B C   1 
ATOM   5563  O  O   . LEU   B 2 387 ? 18.019  68.168  -2.977  1.00 79.64  ? 387  LEU   B O   1 
ATOM   5564  C  CB  . LEU   B 2 387 ? 16.911  68.971  -5.755  1.00 72.22  ? 387  LEU   B CB  1 
ATOM   5565  C  CG  . LEU   B 2 387 ? 15.946  68.643  -6.885  1.00 73.28  ? 387  LEU   B CG  1 
ATOM   5566  C  CD1 . LEU   B 2 387 ? 15.335  69.855  -7.472  1.00 73.44  ? 387  LEU   B CD1 1 
ATOM   5567  C  CD2 . LEU   B 2 387 ? 16.694  67.874  -7.944  1.00 74.67  ? 387  LEU   B CD2 1 
ATOM   5568  N  N   . ARG   B 2 388 ? 19.713  67.670  -4.351  1.00 75.51  ? 388  ARG   B N   1 
ATOM   5569  C  CA  . ARG   B 2 388 ? 20.731  68.126  -3.411  1.00 82.40  ? 388  ARG   B CA  1 
ATOM   5570  C  C   . ARG   B 2 388 ? 21.463  69.332  -4.000  1.00 85.24  ? 388  ARG   B C   1 
ATOM   5571  O  O   . ARG   B 2 388 ? 21.764  69.354  -5.200  1.00 84.07  ? 388  ARG   B O   1 
ATOM   5572  C  CB  . ARG   B 2 388 ? 21.714  66.997  -3.067  1.00 79.94  ? 388  ARG   B CB  1 
ATOM   5573  C  CG  . ARG   B 2 388 ? 21.045  65.716  -2.583  1.00 78.34  ? 388  ARG   B CG  1 
ATOM   5574  C  CD  . ARG   B 2 388 ? 20.415  65.919  -1.222  1.00 79.58  ? 388  ARG   B CD  1 
ATOM   5575  N  NE  . ARG   B 2 388 ? 19.502  64.846  -0.844  1.00 74.41  ? 388  ARG   B NE  1 
ATOM   5576  C  CZ  . ARG   B 2 388 ? 19.774  63.917  0.064   1.00 80.97  ? 388  ARG   B CZ  1 
ATOM   5577  N  NH1 . ARG   B 2 388 ? 20.928  63.895  0.708   1.00 82.97  ? 388  ARG   B NH1 1 
ATOM   5578  N  NH2 . ARG   B 2 388 ? 18.862  62.986  0.340   1.00 86.23  ? 388  ARG   B NH2 1 
ATOM   5579  N  N   . ILE   B 2 389 ? 21.718  70.355  -3.177  1.00 84.80  ? 389  ILE   B N   1 
ATOM   5580  C  CA  . ILE   B 2 389 ? 22.505  71.517  -3.607  1.00 89.40  ? 389  ILE   B CA  1 
ATOM   5581  C  C   . ILE   B 2 389 ? 23.819  71.541  -2.825  1.00 88.96  ? 389  ILE   B C   1 
ATOM   5582  O  O   . ILE   B 2 389 ? 23.819  71.699  -1.597  1.00 88.60  ? 389  ILE   B O   1 
ATOM   5583  C  CB  . ILE   B 2 389 ? 21.745  72.849  -3.456  1.00 86.49  ? 389  ILE   B CB  1 
ATOM   5584  C  CG1 . ILE   B 2 389 ? 20.422  72.835  -4.225  1.00 82.77  ? 389  ILE   B CG1 1 
ATOM   5585  C  CG2 . ILE   B 2 389 ? 22.582  73.982  -4.013  1.00 86.39  ? 389  ILE   B CG2 1 
ATOM   5586  C  CD1 . ILE   B 2 389 ? 19.333  72.024  -3.582  1.00 81.42  ? 389  ILE   B CD1 1 
ATOM   5587  N  N   . ILE   B 2 390 ? 24.934  71.400  -3.541  1.00 86.03  ? 390  ILE   B N   1 
ATOM   5588  C  CA  . ILE   B 2 390 ? 26.254  71.205  -2.942  1.00 90.12  ? 390  ILE   B CA  1 
ATOM   5589  C  C   . ILE   B 2 390 ? 27.133  72.400  -3.292  1.00 98.08  ? 390  ILE   B C   1 
ATOM   5590  O  O   . ILE   B 2 390 ? 27.443  72.616  -4.473  1.00 95.72  ? 390  ILE   B O   1 
ATOM   5591  C  CB  . ILE   B 2 390 ? 26.901  69.897  -3.431  1.00 92.70  ? 390  ILE   B CB  1 
ATOM   5592  C  CG1 . ILE   B 2 390 ? 26.064  68.696  -2.986  1.00 93.58  ? 390  ILE   B CG1 1 
ATOM   5593  C  CG2 . ILE   B 2 390 ? 28.342  69.754  -2.945  1.00 88.54  ? 390  ILE   B CG2 1 
ATOM   5594  C  CD1 . ILE   B 2 390 ? 25.488  67.948  -4.129  1.00 88.40  ? 390  ILE   B CD1 1 
ATOM   5595  N  N   . ARG   B 2 391 ? 27.542  73.168  -2.257  1.00 103.11 ? 391  ARG   B N   1 
ATOM   5596  C  CA  . ARG   B 2 391 ? 28.477  74.292  -2.352  1.00 101.34 ? 391  ARG   B CA  1 
ATOM   5597  C  C   . ARG   B 2 391 ? 29.673  74.061  -1.432  1.00 105.34 ? 391  ARG   B C   1 
ATOM   5598  O  O   . ARG   B 2 391 ? 29.554  73.415  -0.389  1.00 108.63 ? 391  ARG   B O   1 
ATOM   5599  C  CB  . ARG   B 2 391 ? 27.809  75.638  -1.987  1.00 101.21 ? 391  ARG   B CB  1 
ATOM   5600  C  CG  . ARG   B 2 391 ? 27.058  75.684  -0.645  1.00 108.50 ? 391  ARG   B CG  1 
ATOM   5601  C  CD  . ARG   B 2 391 ? 27.298  77.015  0.099   1.00 112.49 ? 391  ARG   B CD  1 
ATOM   5602  N  NE  . ARG   B 2 391 ? 28.731  77.261  0.251   1.00 121.02 ? 391  ARG   B NE  1 
ATOM   5603  C  CZ  . ARG   B 2 391 ? 29.284  78.404  0.651   1.00 129.19 ? 391  ARG   B CZ  1 
ATOM   5604  N  NH1 . ARG   B 2 391 ? 28.550  79.464  0.963   1.00 133.46 ? 391  ARG   B NH1 1 
ATOM   5605  N  NH2 . ARG   B 2 391 ? 30.611  78.488  0.740   1.00 131.00 ? 391  ARG   B NH2 1 
ATOM   5606  N  N   . ASN   B 2 392 ? 30.830  74.598  -1.817  1.00 111.18 ? 392  ASN   B N   1 
ATOM   5607  C  CA  . ASN   B 2 392 ? 32.024  74.555  -0.956  1.00 114.19 ? 392  ASN   B CA  1 
ATOM   5608  C  C   . ASN   B 2 392 ? 31.848  75.465  0.270   1.00 115.38 ? 392  ASN   B C   1 
ATOM   5609  O  O   . ASN   B 2 392 ? 32.340  76.597  0.317   1.00 114.56 ? 392  ASN   B O   1 
ATOM   5610  C  CB  . ASN   B 2 392 ? 33.292  74.949  -1.743  1.00 113.35 ? 392  ASN   B CB  1 
ATOM   5611  C  CG  . ASN   B 2 392 ? 34.045  73.736  -2.313  1.00 111.70 ? 392  ASN   B CG  1 
ATOM   5612  O  OD1 . ASN   B 2 392 ? 34.361  72.784  -1.592  1.00 112.96 ? 392  ASN   B OD1 1 
ATOM   5613  N  ND2 . ASN   B 2 392 ? 34.333  73.774  -3.613  1.00 111.58 ? 392  ASN   B ND2 1 
ATOM   5614  N  N   . LEU   B 2 406 ? 32.002  70.184  2.333   1.00 107.33 ? 710  LEU   B N   1 
ATOM   5615  C  CA  . LEU   B 2 406 ? 31.134  71.128  1.619   1.00 109.27 ? 710  LEU   B CA  1 
ATOM   5616  C  C   . LEU   B 2 406 ? 29.720  71.139  2.233   1.00 108.39 ? 710  LEU   B C   1 
ATOM   5617  O  O   . LEU   B 2 406 ? 29.296  70.123  2.792   1.00 103.41 ? 710  LEU   B O   1 
ATOM   5618  C  CB  . LEU   B 2 406 ? 31.064  70.765  0.121   1.00 107.50 ? 710  LEU   B CB  1 
ATOM   5619  C  CG  . LEU   B 2 406 ? 32.138  71.266  -0.868  1.00 101.46 ? 710  LEU   B CG  1 
ATOM   5620  C  CD1 . LEU   B 2 406 ? 33.471  70.654  -0.561  1.00 93.57  ? 710  LEU   B CD1 1 
ATOM   5621  C  CD2 . LEU   B 2 406 ? 31.802  70.983  -2.324  1.00 103.72 ? 710  LEU   B CD2 1 
ATOM   5622  N  N   . HIS   B 2 407 ? 28.995  72.265  2.120   1.00 109.60 ? 711  HIS   B N   1 
ATOM   5623  C  CA  . HIS   B 2 407 ? 27.631  72.388  2.646   1.00 106.88 ? 711  HIS   B CA  1 
ATOM   5624  C  C   . HIS   B 2 407 ? 26.597  71.844  1.649   1.00 105.96 ? 711  HIS   B C   1 
ATOM   5625  O  O   . HIS   B 2 407 ? 26.745  72.009  0.432   1.00 103.63 ? 711  HIS   B O   1 
ATOM   5626  C  CB  . HIS   B 2 407 ? 27.345  73.854  2.998   1.00 108.98 ? 711  HIS   B CB  1 
ATOM   5627  C  CG  . HIS   B 2 407 ? 28.270  74.429  4.035   1.00 119.25 ? 711  HIS   B CG  1 
ATOM   5628  N  ND1 . HIS   B 2 407 ? 28.251  74.031  5.357   1.00 119.91 ? 711  HIS   B ND1 1 
ATOM   5629  C  CD2 . HIS   B 2 407 ? 29.247  75.369  3.939   1.00 125.83 ? 711  HIS   B CD2 1 
ATOM   5630  C  CE1 . HIS   B 2 407 ? 29.174  74.701  6.031   1.00 117.39 ? 711  HIS   B CE1 1 
ATOM   5631  N  NE2 . HIS   B 2 407 ? 29.789  75.522  5.195   1.00 124.42 ? 711  HIS   B NE2 1 
ATOM   5632  N  N   . ILE   B 2 408 ? 25.557  71.177  2.173   1.00 105.10 ? 712  ILE   B N   1 
ATOM   5633  C  CA  . ILE   B 2 408 ? 24.550  70.479  1.360   1.00 98.56  ? 712  ILE   B CA  1 
ATOM   5634  C  C   . ILE   B 2 408 ? 23.154  70.853  1.828   1.00 95.72  ? 712  ILE   B C   1 
ATOM   5635  O  O   . ILE   B 2 408 ? 22.844  70.739  3.018   1.00 94.03  ? 712  ILE   B O   1 
ATOM   5636  C  CB  . ILE   B 2 408 ? 24.702  68.953  1.426   1.00 99.18  ? 712  ILE   B CB  1 
ATOM   5637  C  CG1 . ILE   B 2 408 ? 25.947  68.488  0.685   1.00 95.46  ? 712  ILE   B CG1 1 
ATOM   5638  C  CG2 . ILE   B 2 408 ? 23.466  68.274  0.846   1.00 97.46  ? 712  ILE   B CG2 1 
ATOM   5639  C  CD1 . ILE   B 2 408 ? 26.611  67.326  1.372   1.00 95.33  ? 712  ILE   B CD1 1 
ATOM   5640  N  N   . ARG   B 2 409 ? 22.313  71.266  0.885   1.00 94.32  ? 713  ARG   B N   1 
ATOM   5641  C  CA  . ARG   B 2 409 ? 20.905  71.543  1.116   1.00 88.24  ? 713  ARG   B CA  1 
ATOM   5642  C  C   . ARG   B 2 409 ? 20.113  70.507  0.342   1.00 88.17  ? 713  ARG   B C   1 
ATOM   5643  O  O   . ARG   B 2 409 ? 20.289  70.380  -0.877  1.00 85.89  ? 713  ARG   B O   1 
ATOM   5644  C  CB  . ARG   B 2 409 ? 20.544  72.951  0.651   1.00 87.64  ? 713  ARG   B CB  1 
ATOM   5645  C  CG  . ARG   B 2 409 ? 19.395  73.555  1.400   1.00 100.60 ? 713  ARG   B CG  1 
ATOM   5646  C  CD  . ARG   B 2 409 ? 18.318  74.109  0.480   1.00 101.16 ? 713  ARG   B CD  1 
ATOM   5647  N  NE  . ARG   B 2 409 ? 17.213  74.663  1.256   1.00 109.89 ? 713  ARG   B NE  1 
ATOM   5648  C  CZ  . ARG   B 2 409 ? 16.202  75.348  0.741   1.00 108.64 ? 713  ARG   B CZ  1 
ATOM   5649  N  NH1 . ARG   B 2 409 ? 16.122  75.587  -0.555  1.00 100.88 ? 713  ARG   B NH1 1 
ATOM   5650  N  NH2 . ARG   B 2 409 ? 15.248  75.807  1.549   1.00 113.25 ? 713  ARG   B NH2 1 
ATOM   5651  N  N   . THR   B 2 410 ? 19.268  69.749  1.041   1.00 88.83  ? 714  THR   B N   1 
ATOM   5652  C  CA  . THR   B 2 410 ? 18.482  68.689  0.404   1.00 87.73  ? 714  THR   B CA  1 
ATOM   5653  C  C   . THR   B 2 410 ? 17.046  69.156  0.194   1.00 81.51  ? 714  THR   B C   1 
ATOM   5654  O  O   . THR   B 2 410 ? 16.375  69.561  1.141   1.00 84.80  ? 714  THR   B O   1 
ATOM   5655  C  CB  . THR   B 2 410 ? 18.444  67.387  1.220   1.00 86.78  ? 714  THR   B CB  1 
ATOM   5656  O  OG1 . THR   B 2 410 ? 17.631  67.604  2.374   1.00 97.14  ? 714  THR   B OG1 1 
ATOM   5657  C  CG2 . THR   B 2 410 ? 19.847  66.893  1.656   1.00 81.07  ? 714  THR   B CG2 1 
ATOM   5658  N  N   . VAL   B 2 411 ? 16.571  69.061  -1.036  1.00 82.57  ? 715  VAL   B N   1 
ATOM   5659  C  CA  . VAL   B 2 411 ? 15.168  69.314  -1.339  1.00 82.79  ? 715  VAL   B CA  1 
ATOM   5660  C  C   . VAL   B 2 411 ? 14.440  67.979  -1.480  1.00 84.80  ? 715  VAL   B C   1 
ATOM   5661  O  O   . VAL   B 2 411 ? 14.544  67.324  -2.537  1.00 85.06  ? 715  VAL   B O   1 
ATOM   5662  C  CB  . VAL   B 2 411 ? 15.015  70.143  -2.620  1.00 81.06  ? 715  VAL   B CB  1 
ATOM   5663  C  CG1 . VAL   B 2 411 ? 13.568  70.551  -2.795  1.00 83.21  ? 715  VAL   B CG1 1 
ATOM   5664  C  CG2 . VAL   B 2 411 ? 15.967  71.349  -2.613  1.00 82.62  ? 715  VAL   B CG2 1 
ATOM   5665  N  N   . PRO   B 2 412 ? 13.673  67.547  -0.478  1.00 80.83  ? 716  PRO   B N   1 
ATOM   5666  C  CA  . PRO   B 2 412 ? 12.954  66.278  -0.603  1.00 75.58  ? 716  PRO   B CA  1 
ATOM   5667  C  C   . PRO   B 2 412 ? 11.886  66.388  -1.678  1.00 79.36  ? 716  PRO   B C   1 
ATOM   5668  O  O   . PRO   B 2 412 ? 11.127  67.351  -1.720  1.00 88.76  ? 716  PRO   B O   1 
ATOM   5669  C  CB  . PRO   B 2 412 ? 12.344  66.078  0.786   1.00 75.98  ? 716  PRO   B CB  1 
ATOM   5670  C  CG  . PRO   B 2 412 ? 12.098  67.419  1.256   1.00 91.71  ? 716  PRO   B CG  1 
ATOM   5671  C  CD  . PRO   B 2 412 ? 13.197  68.327  0.671   1.00 89.78  ? 716  PRO   B CD  1 
ATOM   5672  N  N   . LEU   B 2 413 ? 11.836  65.394  -2.560  1.00 84.05  ? 717  LEU   B N   1 
ATOM   5673  C  CA  . LEU   B 2 413 ? 10.868  65.382  -3.643  1.00 79.06  ? 717  LEU   B CA  1 
ATOM   5674  C  C   . LEU   B 2 413 ? 9.797   64.304  -3.516  1.00 77.80  ? 717  LEU   B C   1 
ATOM   5675  O  O   . LEU   B 2 413 ? 8.712   64.485  -4.079  1.00 76.86  ? 717  LEU   B O   1 
ATOM   5676  C  CB  . LEU   B 2 413 ? 11.597  65.221  -4.979  1.00 78.25  ? 717  LEU   B CB  1 
ATOM   5677  C  CG  . LEU   B 2 413 ? 12.487  66.409  -5.303  1.00 75.38  ? 717  LEU   B CG  1 
ATOM   5678  C  CD1 . LEU   B 2 413 ? 13.223  66.160  -6.611  1.00 76.48  ? 717  LEU   B CD1 1 
ATOM   5679  C  CD2 . LEU   B 2 413 ? 11.613  67.626  -5.402  1.00 75.92  ? 717  LEU   B CD2 1 
ATOM   5680  N  N   . TYR   B 2 414 ? 10.052  63.212  -2.776  1.00 77.72  ? 718  TYR   B N   1 
ATOM   5681  C  CA  . TYR   B 2 414 ? 9.094   62.102  -2.620  1.00 78.42  ? 718  TYR   B CA  1 
ATOM   5682  C  C   . TYR   B 2 414 ? 8.675   61.498  -3.961  1.00 78.54  ? 718  TYR   B C   1 
ATOM   5683  O  O   . TYR   B 2 414 ? 7.587   60.912  -4.052  1.00 75.92  ? 718  TYR   B O   1 
ATOM   5684  C  CB  . TYR   B 2 414 ? 7.836   62.526  -1.846  1.00 78.72  ? 718  TYR   B CB  1 
ATOM   5685  C  CG  . TYR   B 2 414 ? 8.145   63.251  -0.558  1.00 84.23  ? 718  TYR   B CG  1 
ATOM   5686  C  CD1 . TYR   B 2 414 ? 8.705   64.523  -0.582  1.00 86.77  ? 718  TYR   B CD1 1 
ATOM   5687  C  CD2 . TYR   B 2 414 ? 7.881   62.677  0.681   1.00 87.01  ? 718  TYR   B CD2 1 
ATOM   5688  C  CE1 . TYR   B 2 414 ? 9.019   65.203  0.578   1.00 87.55  ? 718  TYR   B CE1 1 
ATOM   5689  C  CE2 . TYR   B 2 414 ? 8.182   63.354  1.853   1.00 86.36  ? 718  TYR   B CE2 1 
ATOM   5690  C  CZ  . TYR   B 2 414 ? 8.755   64.617  1.796   1.00 91.13  ? 718  TYR   B CZ  1 
ATOM   5691  O  OH  . TYR   B 2 414 ? 9.069   65.313  2.946   1.00 96.78  ? 718  TYR   B OH  1 
ATOM   5692  N  N   . GLU   B 2 415 ? 9.503   61.688  -5.002  1.00 75.57  ? 719  GLU   B N   1 
ATOM   5693  C  CA  . GLU   B 2 415 ? 9.428   60.985  -6.283  1.00 73.89  ? 719  GLU   B CA  1 
ATOM   5694  C  C   . GLU   B 2 415 ? 10.809  61.078  -6.920  1.00 73.69  ? 719  GLU   B C   1 
ATOM   5695  O  O   . GLU   B 2 415 ? 11.685  61.788  -6.427  1.00 73.38  ? 719  GLU   B O   1 
ATOM   5696  C  CB  . GLU   B 2 415 ? 8.330   61.528  -7.222  1.00 73.44  ? 719  GLU   B CB  1 
ATOM   5697  C  CG  . GLU   B 2 415 ? 8.054   63.027  -7.177  1.00 75.90  ? 719  GLU   B CG  1 
ATOM   5698  C  CD  . GLU   B 2 415 ? 6.747   63.426  -7.907  1.00 85.28  ? 719  GLU   B CD  1 
ATOM   5699  O  OE1 . GLU   B 2 415 ? 6.819   63.779  -9.121  1.00 84.83  ? 719  GLU   B OE1 1 
ATOM   5700  O  OE2 . GLU   B 2 415 ? 5.650   63.401  -7.267  1.00 85.35  ? 719  GLU   B OE2 1 
ATOM   5701  N  N   . SER   B 2 416 ? 11.000  60.347  -8.021  1.00 74.42  ? 720  SER   B N   1 
ATOM   5702  C  CA  . SER   B 2 416 ? 12.340  60.162  -8.569  1.00 75.76  ? 720  SER   B CA  1 
ATOM   5703  C  C   . SER   B 2 416 ? 12.680  61.302  -9.520  1.00 77.28  ? 720  SER   B C   1 
ATOM   5704  O  O   . SER   B 2 416 ? 12.017  61.450  -10.560 1.00 76.49  ? 720  SER   B O   1 
ATOM   5705  C  CB  . SER   B 2 416 ? 12.459  58.831  -9.290  1.00 75.22  ? 720  SER   B CB  1 
ATOM   5706  O  OG  . SER   B 2 416 ? 11.669  57.830  -8.671  1.00 79.06  ? 720  SER   B OG  1 
ATOM   5707  N  N   . PRO   B 2 417 ? 13.676  62.126  -9.214  1.00 76.95  ? 721  PRO   B N   1 
ATOM   5708  C  CA  . PRO   B 2 417 ? 14.170  63.068  -10.222 1.00 76.83  ? 721  PRO   B CA  1 
ATOM   5709  C  C   . PRO   B 2 417 ? 15.014  62.310  -11.220 1.00 71.93  ? 721  PRO   B C   1 
ATOM   5710  O  O   . PRO   B 2 417 ? 15.822  61.462  -10.847 1.00 77.70  ? 721  PRO   B O   1 
ATOM   5711  C  CB  . PRO   B 2 417 ? 15.023  64.069  -9.415  1.00 79.55  ? 721  PRO   B CB  1 
ATOM   5712  C  CG  . PRO   B 2 417 ? 15.101  63.511  -7.999  1.00 80.11  ? 721  PRO   B CG  1 
ATOM   5713  C  CD  . PRO   B 2 417 ? 14.542  62.096  -8.027  1.00 78.15  ? 721  PRO   B CD  1 
ATOM   5714  N  N   . ARG   B 2 418 ? 14.839  62.622  -12.497 1.00 76.74  ? 722  ARG   B N   1 
ATOM   5715  C  CA  . ARG   B 2 418 ? 15.617  61.944  -13.529 1.00 78.30  ? 722  ARG   B CA  1 
ATOM   5716  C  C   . ARG   B 2 418 ? 16.528  62.886  -14.313 1.00 80.69  ? 722  ARG   B C   1 
ATOM   5717  O  O   . ARG   B 2 418 ? 17.715  62.584  -14.485 1.00 85.13  ? 722  ARG   B O   1 
ATOM   5718  C  CB  . ARG   B 2 418 ? 14.676  61.155  -14.454 1.00 76.79  ? 722  ARG   B CB  1 
ATOM   5719  C  CG  . ARG   B 2 418 ? 13.839  60.074  -13.724 1.00 71.08  ? 722  ARG   B CG  1 
ATOM   5720  C  CD  . ARG   B 2 418 ? 14.665  58.879  -13.249 1.00 76.46  ? 722  ARG   B CD  1 
ATOM   5721  N  NE  . ARG   B 2 418 ? 15.211  58.048  -14.326 1.00 85.66  ? 722  ARG   B NE  1 
ATOM   5722  C  CZ  . ARG   B 2 418 ? 16.317  57.306  -14.221 1.00 82.94  ? 722  ARG   B CZ  1 
ATOM   5723  N  NH1 . ARG   B 2 418 ? 17.007  57.233  -13.080 1.00 75.84  ? 722  ARG   B NH1 1 
ATOM   5724  N  NH2 . ARG   B 2 418 ? 16.751  56.629  -15.287 1.00 81.41  ? 722  ARG   B NH2 1 
ATOM   5725  N  N   . LYS   B 2 419 ? 16.054  64.046  -14.756 1.00 80.92  ? 723  LYS   B N   1 
ATOM   5726  C  CA  . LYS   B 2 419 ? 16.955  64.965  -15.437 1.00 81.08  ? 723  LYS   B CA  1 
ATOM   5727  C  C   . LYS   B 2 419 ? 16.747  66.381  -14.909 1.00 79.70  ? 723  LYS   B C   1 
ATOM   5728  O  O   . LYS   B 2 419 ? 15.649  66.741  -14.478 1.00 78.35  ? 723  LYS   B O   1 
ATOM   5729  C  CB  . LYS   B 2 419 ? 16.748  64.876  -16.951 1.00 82.46  ? 723  LYS   B CB  1 
ATOM   5730  C  CG  . LYS   B 2 419 ? 16.846  63.448  -17.506 1.00 83.31  ? 723  LYS   B CG  1 
ATOM   5731  C  CD  . LYS   B 2 419 ? 18.296  62.965  -17.635 1.00 84.44  ? 723  LYS   B CD  1 
ATOM   5732  C  CE  . LYS   B 2 419 ? 18.348  61.447  -17.682 1.00 86.00  ? 723  LYS   B CE  1 
ATOM   5733  N  NZ  . LYS   B 2 419 ? 19.518  60.967  -18.465 1.00 90.43  ? 723  LYS   B NZ  1 
ATOM   5734  N  N   . ILE   B 2 420 ? 17.817  67.183  -14.913 1.00 81.60  ? 724  ILE   B N   1 
ATOM   5735  C  CA  . ILE   B 2 420 ? 17.750  68.541  -14.376 1.00 82.63  ? 724  ILE   B CA  1 
ATOM   5736  C  C   . ILE   B 2 420 ? 18.525  69.513  -15.262 1.00 81.45  ? 724  ILE   B C   1 
ATOM   5737  O  O   . ILE   B 2 420 ? 19.577  69.193  -15.826 1.00 84.37  ? 724  ILE   B O   1 
ATOM   5738  C  CB  . ILE   B 2 420 ? 18.271  68.620  -12.924 1.00 80.10  ? 724  ILE   B CB  1 
ATOM   5739  C  CG1 . ILE   B 2 420 ? 18.239  70.076  -12.457 1.00 83.08  ? 724  ILE   B CG1 1 
ATOM   5740  C  CG2 . ILE   B 2 420 ? 19.687  68.085  -12.842 1.00 77.12  ? 724  ILE   B CG2 1 
ATOM   5741  C  CD1 . ILE   B 2 420 ? 18.298  70.243  -10.966 1.00 81.30  ? 724  ILE   B CD1 1 
ATOM   5742  N  N   . CYS   B 2 421 ? 18.010  70.728  -15.360 1.00 83.38  ? 725  CYS   B N   1 
ATOM   5743  C  CA  . CYS   B 2 421 ? 18.669  71.751  -16.152 1.00 86.07  ? 725  CYS   B CA  1 
ATOM   5744  C  C   . CYS   B 2 421 ? 18.298  73.102  -15.570 1.00 81.67  ? 725  CYS   B C   1 
ATOM   5745  O  O   . CYS   B 2 421 ? 17.215  73.280  -15.006 1.00 80.09  ? 725  CYS   B O   1 
ATOM   5746  C  CB  . CYS   B 2 421 ? 18.259  71.673  -17.624 1.00 85.02  ? 725  CYS   B CB  1 
ATOM   5747  S  SG  . CYS   B 2 421 ? 16.645  72.430  -17.894 1.00 95.35  ? 725  CYS   B SG  1 
ATOM   5748  N  N   . TYR   B 2 422 ? 19.204  74.061  -15.726 1.00 82.63  ? 726  TYR   B N   1 
ATOM   5749  C  CA  . TYR   B 2 422 ? 19.014  75.394  -15.165 1.00 89.86  ? 726  TYR   B CA  1 
ATOM   5750  C  C   . TYR   B 2 422 ? 18.610  76.366  -16.272 1.00 92.51  ? 726  TYR   B C   1 
ATOM   5751  O  O   . TYR   B 2 422 ? 19.279  76.447  -17.300 1.00 94.59  ? 726  TYR   B O   1 
ATOM   5752  C  CB  . TYR   B 2 422 ? 20.288  75.839  -14.442 1.00 87.84  ? 726  TYR   B CB  1 
ATOM   5753  C  CG  . TYR   B 2 422 ? 20.195  77.211  -13.858 1.00 94.17  ? 726  TYR   B CG  1 
ATOM   5754  C  CD1 . TYR   B 2 422 ? 19.351  77.473  -12.789 1.00 95.39  ? 726  TYR   B CD1 1 
ATOM   5755  C  CD2 . TYR   B 2 422 ? 20.942  78.255  -14.376 1.00 97.63  ? 726  TYR   B CD2 1 
ATOM   5756  C  CE1 . TYR   B 2 422 ? 19.260  78.746  -12.251 1.00 97.27  ? 726  TYR   B CE1 1 
ATOM   5757  C  CE2 . TYR   B 2 422 ? 20.857  79.523  -13.847 1.00 100.44 ? 726  TYR   B CE2 1 
ATOM   5758  C  CZ  . TYR   B 2 422 ? 20.014  79.767  -12.788 1.00 100.15 ? 726  TYR   B CZ  1 
ATOM   5759  O  OH  . TYR   B 2 422 ? 19.928  81.038  -12.273 1.00 100.21 ? 726  TYR   B OH  1 
ATOM   5760  N  N   . GLN   B 2 423 ? 17.497  77.071  -16.086 1.00 95.92  ? 727  GLN   B N   1 
ATOM   5761  C  CA  . GLN   B 2 423 ? 17.089  78.135  -17.010 1.00 101.18 ? 727  GLN   B CA  1 
ATOM   5762  C  C   . GLN   B 2 423 ? 17.304  79.459  -16.279 1.00 102.02 ? 727  GLN   B C   1 
ATOM   5763  O  O   . GLN   B 2 423 ? 16.472  79.905  -15.485 1.00 93.92  ? 727  GLN   B O   1 
ATOM   5764  C  CB  . GLN   B 2 423 ? 15.652  77.943  -17.478 1.00 98.27  ? 727  GLN   B CB  1 
ATOM   5765  C  CG  . GLN   B 2 423 ? 15.097  79.039  -18.373 1.00 96.93  ? 727  GLN   B CG  1 
ATOM   5766  C  CD  . GLN   B 2 423 ? 14.028  78.498  -19.295 1.00 91.81  ? 727  GLN   B CD  1 
ATOM   5767  O  OE1 . GLN   B 2 423 ? 14.330  77.743  -20.215 1.00 91.50  ? 727  GLN   B OE1 1 
ATOM   5768  N  NE2 . GLN   B 2 423 ? 12.771  78.851  -19.037 1.00 90.71  ? 727  GLN   B NE2 1 
ATOM   5769  N  N   . GLU   B 2 424 ? 18.460  80.064  -16.543 1.00 107.00 ? 728  GLU   B N   1 
ATOM   5770  C  CA  . GLU   B 2 424 ? 18.861  81.234  -15.780 1.00 108.08 ? 728  GLU   B CA  1 
ATOM   5771  C  C   . GLU   B 2 424 ? 17.943  82.419  -16.056 1.00 109.92 ? 728  GLU   B C   1 
ATOM   5772  O  O   . GLU   B 2 424 ? 17.693  83.251  -15.175 1.00 111.71 ? 728  GLU   B O   1 
ATOM   5773  C  CB  . GLU   B 2 424 ? 20.307  81.592  -16.109 1.00 113.75 ? 728  GLU   B CB  1 
ATOM   5774  C  CG  . GLU   B 2 424 ? 20.884  82.649  -15.198 1.00 119.07 ? 728  GLU   B CG  1 
ATOM   5775  C  CD  . GLU   B 2 424 ? 22.215  83.160  -15.692 1.00 123.91 ? 728  GLU   B CD  1 
ATOM   5776  O  OE1 . GLU   B 2 424 ? 22.353  83.362  -16.915 1.00 129.57 ? 728  GLU   B OE1 1 
ATOM   5777  O  OE2 . GLU   B 2 424 ? 23.126  83.357  -14.861 1.00 132.73 ? 728  GLU   B OE2 1 
ATOM   5778  N  N   . VAL   B 2 425 ? 17.419  82.503  -17.272 1.00 105.50 ? 729  VAL   B N   1 
ATOM   5779  C  CA  . VAL   B 2 425 ? 16.592  83.644  -17.640 1.00 99.08  ? 729  VAL   B CA  1 
ATOM   5780  C  C   . VAL   B 2 425 ? 15.416  83.792  -16.679 1.00 98.11  ? 729  VAL   B C   1 
ATOM   5781  O  O   . VAL   B 2 425 ? 15.083  84.898  -16.248 1.00 103.23 ? 729  VAL   B O   1 
ATOM   5782  C  CB  . VAL   B 2 425 ? 16.141  83.488  -19.098 1.00 106.34 ? 729  VAL   B CB  1 
ATOM   5783  C  CG1 . VAL   B 2 425 ? 15.754  84.838  -19.698 1.00 102.82 ? 729  VAL   B CG1 1 
ATOM   5784  C  CG2 . VAL   B 2 425 ? 17.272  82.813  -19.904 1.00 104.55 ? 729  VAL   B CG2 1 
ATOM   5785  N  N   . SER   B 2 426 ? 14.779  82.679  -16.315 1.00 101.40 ? 730  SER   B N   1 
ATOM   5786  C  CA  . SER   B 2 426 ? 13.606  82.683  -15.444 1.00 97.66  ? 730  SER   B CA  1 
ATOM   5787  C  C   . SER   B 2 426 ? 13.928  82.261  -14.016 1.00 100.67 ? 730  SER   B C   1 
ATOM   5788  O  O   . SER   B 2 426 ? 13.008  82.068  -13.212 1.00 101.19 ? 730  SER   B O   1 
ATOM   5789  C  CB  . SER   B 2 426 ? 12.506  81.782  -16.022 1.00 98.91  ? 730  SER   B CB  1 
ATOM   5790  O  OG  . SER   B 2 426 ? 13.042  80.595  -16.599 1.00 100.01 ? 730  SER   B OG  1 
ATOM   5791  N  N   . GLN   B 2 427 ? 15.214  82.120  -13.681 1.00 103.33 ? 731  GLN   B N   1 
ATOM   5792  C  CA  . GLN   B 2 427 ? 15.658  81.887  -12.307 1.00 98.63  ? 731  GLN   B CA  1 
ATOM   5793  C  C   . GLN   B 2 427 ? 15.017  80.632  -11.720 1.00 101.33 ? 731  GLN   B C   1 
ATOM   5794  O  O   . GLN   B 2 427 ? 14.564  80.623  -10.571 1.00 97.00  ? 731  GLN   B O   1 
ATOM   5795  C  CB  . GLN   B 2 427 ? 15.379  83.104  -11.419 1.00 97.80  ? 731  GLN   B CB  1 
ATOM   5796  N  N   . CYS   B 2 428 ? 14.991  79.555  -12.511 1.00 103.63 ? 732  CYS   B N   1 
ATOM   5797  C  CA  . CYS   B 2 428 ? 14.379  78.313  -12.045 1.00 101.40 ? 732  CYS   B CA  1 
ATOM   5798  C  C   . CYS   B 2 428 ? 15.072  77.099  -12.659 1.00 100.22 ? 732  CYS   B C   1 
ATOM   5799  O  O   . CYS   B 2 428 ? 15.850  77.209  -13.613 1.00 98.46  ? 732  CYS   B O   1 
ATOM   5800  C  CB  . CYS   B 2 428 ? 12.896  78.275  -12.390 1.00 100.24 ? 732  CYS   B CB  1 
ATOM   5801  S  SG  . CYS   B 2 428 ? 12.733  78.138  -14.155 1.00 109.04 ? 732  CYS   B SG  1 
ATOM   5802  N  N   . PHE   B 2 429 ? 14.761  75.926  -12.107 1.00 99.35  ? 733  PHE   B N   1 
ATOM   5803  C  CA  . PHE   B 2 429 ? 15.248  74.658  -12.631 1.00 93.05  ? 733  PHE   B CA  1 
ATOM   5804  C  C   . PHE   B 2 429 ? 14.128  73.865  -13.277 1.00 87.35  ? 733  PHE   B C   1 
ATOM   5805  O  O   . PHE   B 2 429 ? 13.009  73.792  -12.742 1.00 82.03  ? 733  PHE   B O   1 
ATOM   5806  C  CB  . PHE   B 2 429 ? 15.842  73.785  -11.545 1.00 84.17  ? 733  PHE   B CB  1 
ATOM   5807  C  CG  . PHE   B 2 429 ? 17.075  74.330  -10.932 1.00 84.46  ? 733  PHE   B CG  1 
ATOM   5808  C  CD1 . PHE   B 2 429 ? 18.307  74.028  -11.474 1.00 83.36  ? 733  PHE   B CD1 1 
ATOM   5809  C  CD2 . PHE   B 2 429 ? 17.010  75.108  -9.780  1.00 86.39  ? 733  PHE   B CD2 1 
ATOM   5810  C  CE1 . PHE   B 2 429 ? 19.457  74.506  -10.888 1.00 85.85  ? 733  PHE   B CE1 1 
ATOM   5811  C  CE2 . PHE   B 2 429 ? 18.158  75.584  -9.187  1.00 85.97  ? 733  PHE   B CE2 1 
ATOM   5812  C  CZ  . PHE   B 2 429 ? 19.377  75.288  -9.736  1.00 85.91  ? 733  PHE   B CZ  1 
ATOM   5813  N  N   . GLY   B 2 430 ? 14.457  73.242  -14.409 1.00 84.96  ? 734  GLY   B N   1 
ATOM   5814  C  CA  . GLY   B 2 430 ? 13.604  72.213  -14.994 1.00 85.71  ? 734  GLY   B CA  1 
ATOM   5815  C  C   . GLY   B 2 430 ? 14.007  70.799  -14.571 1.00 82.20  ? 734  GLY   B C   1 
ATOM   5816  O  O   . GLY   B 2 430 ? 15.153  70.374  -14.747 1.00 83.35  ? 734  GLY   B O   1 
ATOM   5817  N  N   . VAL   B 2 431 ? 13.070  70.051  -14.014 1.00 79.79  ? 735  VAL   B N   1 
ATOM   5818  C  CA  . VAL   B 2 431 ? 13.357  68.675  -13.621 1.00 80.54  ? 735  VAL   B CA  1 
ATOM   5819  C  C   . VAL   B 2 431 ? 12.320  67.745  -14.236 1.00 78.05  ? 735  VAL   B C   1 
ATOM   5820  O  O   . VAL   B 2 431 ? 11.113  68.027  -14.206 1.00 79.86  ? 735  VAL   B O   1 
ATOM   5821  C  CB  . VAL   B 2 431 ? 13.422  68.520  -12.092 1.00 80.54  ? 735  VAL   B CB  1 
ATOM   5822  C  CG1 . VAL   B 2 431 ? 13.441  67.042  -11.726 1.00 83.54  ? 735  VAL   B CG1 1 
ATOM   5823  C  CG2 . VAL   B 2 431 ? 14.677  69.204  -11.555 1.00 78.55  ? 735  VAL   B CG2 1 
ATOM   5824  N  N   . LEU   B 2 432 ? 12.799  66.661  -14.834 1.00 78.57  ? 736  LEU   B N   1 
ATOM   5825  C  CA  . LEU   B 2 432 ? 11.934  65.577  -15.280 1.00 78.14  ? 736  LEU   B CA  1 
ATOM   5826  C  C   . LEU   B 2 432 ? 11.883  64.549  -14.161 1.00 78.41  ? 736  LEU   B C   1 
ATOM   5827  O  O   . LEU   B 2 432 ? 12.929  64.117  -13.674 1.00 78.71  ? 736  LEU   B O   1 
ATOM   5828  C  CB  . LEU   B 2 432 ? 12.453  64.948  -16.574 1.00 74.46  ? 736  LEU   B CB  1 
ATOM   5829  C  CG  . LEU   B 2 432 ? 12.560  65.743  -17.883 1.00 80.86  ? 736  LEU   B CG  1 
ATOM   5830  C  CD1 . LEU   B 2 432 ? 13.241  64.879  -18.943 1.00 79.16  ? 736  LEU   B CD1 1 
ATOM   5831  C  CD2 . LEU   B 2 432 ? 11.196  66.234  -18.386 1.00 80.01  ? 736  LEU   B CD2 1 
ATOM   5832  N  N   . SER   B 2 433 ? 10.672  64.187  -13.736 1.00 77.89  ? 737  SER   B N   1 
ATOM   5833  C  CA  . SER   B 2 433 ? 10.468  63.344  -12.563 1.00 79.41  ? 737  SER   B CA  1 
ATOM   5834  C  C   . SER   B 2 433 ? 9.408   62.284  -12.845 1.00 80.64  ? 737  SER   B C   1 
ATOM   5835  O  O   . SER   B 2 433 ? 8.455   62.520  -13.595 1.00 79.87  ? 737  SER   B O   1 
ATOM   5836  C  CB  . SER   B 2 433 ? 10.023  64.175  -11.350 1.00 75.85  ? 737  SER   B CB  1 
ATOM   5837  O  OG  . SER   B 2 433 ? 8.603   64.315  -11.366 1.00 78.11  ? 737  SER   B OG  1 
ATOM   5838  N  N   . SER   B 2 434 ? 9.553   61.122  -12.199 1.00 78.97  ? 738  SER   B N   1 
ATOM   5839  C  CA  . SER   B 2 434 ? 8.546   60.071  -12.292 1.00 82.21  ? 738  SER   B CA  1 
ATOM   5840  C  C   . SER   B 2 434 ? 7.950   59.805  -10.914 1.00 79.95  ? 738  SER   B C   1 
ATOM   5841  O  O   . SER   B 2 434 ? 8.621   59.973  -9.883  1.00 77.25  ? 738  SER   B O   1 
ATOM   5842  C  CB  . SER   B 2 434 ? 9.115   58.765  -12.939 1.00 77.63  ? 738  SER   B CB  1 
ATOM   5843  O  OG  . SER   B 2 434 ? 9.777   57.902  -12.018 1.00 85.36  ? 738  SER   B OG  1 
ATOM   5844  N  N   . ARG   B 2 435 ? 6.662   59.451  -10.922 1.00 75.85  ? 739  ARG   B N   1 
ATOM   5845  C  CA  . ARG   B 2 435 ? 5.898   59.083  -9.743  1.00 76.77  ? 739  ARG   B CA  1 
ATOM   5846  C  C   . ARG   B 2 435 ? 5.287   57.718  -10.001 1.00 87.72  ? 739  ARG   B C   1 
ATOM   5847  O  O   . ARG   B 2 435 ? 4.719   57.487  -11.077 1.00 86.02  ? 739  ARG   B O   1 
ATOM   5848  C  CB  . ARG   B 2 435 ? 4.806   60.098  -9.470  1.00 75.03  ? 739  ARG   B CB  1 
ATOM   5849  C  CG  . ARG   B 2 435 ? 3.819   59.761  -8.369  1.00 80.67  ? 739  ARG   B CG  1 
ATOM   5850  C  CD  . ARG   B 2 435 ? 2.681   60.800  -8.362  1.00 86.10  ? 739  ARG   B CD  1 
ATOM   5851  N  NE  . ARG   B 2 435 ? 2.215   61.105  -9.714  1.00 87.77  ? 739  ARG   B NE  1 
ATOM   5852  C  CZ  . ARG   B 2 435 ? 1.511   62.184  -10.034 1.00 91.65  ? 739  ARG   B CZ  1 
ATOM   5853  N  NH1 . ARG   B 2 435 ? 1.202   63.095  -9.126  1.00 94.69  ? 739  ARG   B NH1 1 
ATOM   5854  N  NH2 . ARG   B 2 435 ? 1.113   62.356  -11.297 1.00 84.41  ? 739  ARG   B NH2 1 
ATOM   5855  N  N   . ILE   B 2 436 ? 5.402   56.811  -9.022  1.00 82.65  ? 740  ILE   B N   1 
ATOM   5856  C  CA  . ILE   B 2 436 ? 4.689   55.544  -9.093  1.00 76.88  ? 740  ILE   B CA  1 
ATOM   5857  C  C   . ILE   B 2 436 ? 3.260   55.753  -8.636  1.00 81.67  ? 740  ILE   B C   1 
ATOM   5858  O  O   . ILE   B 2 436 ? 3.022   56.269  -7.538  1.00 84.52  ? 740  ILE   B O   1 
ATOM   5859  C  CB  . ILE   B 2 436 ? 5.358   54.474  -8.223  1.00 82.66  ? 740  ILE   B CB  1 
ATOM   5860  C  CG1 . ILE   B 2 436 ? 6.803   54.245  -8.630  1.00 82.07  ? 740  ILE   B CG1 1 
ATOM   5861  C  CG2 . ILE   B 2 436 ? 4.551   53.189  -8.311  1.00 80.20  ? 740  ILE   B CG2 1 
ATOM   5862  C  CD1 . ILE   B 2 436 ? 6.939   53.473  -9.858  1.00 81.42  ? 740  ILE   B CD1 1 
ATOM   5863  N  N   . GLU   B 2 437 ? 2.305   55.340  -9.465  1.00 89.97  ? 741  GLU   B N   1 
ATOM   5864  C  CA  . GLU   B 2 437 ? 0.929   55.174  -9.024  1.00 94.73  ? 741  GLU   B CA  1 
ATOM   5865  C  C   . GLU   B 2 437 ? 0.475   53.739  -9.327  1.00 94.80  ? 741  GLU   B C   1 
ATOM   5866  O  O   . GLU   B 2 437 ? 1.150   52.992  -10.039 1.00 92.66  ? 741  GLU   B O   1 
ATOM   5867  C  CB  . GLU   B 2 437 ? 0.021   56.248  -9.658  1.00 95.92  ? 741  GLU   B CB  1 
ATOM   5868  C  CG  . GLU   B 2 437 ? 0.324   57.695  -9.125  1.00 98.97  ? 741  GLU   B CG  1 
ATOM   5869  C  CD  . GLU   B 2 437 ? -0.604  58.805  -9.690  1.00 102.61 ? 741  GLU   B CD  1 
ATOM   5870  O  OE1 . GLU   B 2 437 ? -1.338  58.526  -10.669 1.00 105.16 ? 741  GLU   B OE1 1 
ATOM   5871  O  OE2 . GLU   B 2 437 ? -0.597  59.951  -9.146  1.00 100.06 ? 741  GLU   B OE2 1 
ATOM   5872  N  N   . VAL   B 2 438 ? -0.666  53.335  -8.746  1.00 99.79  ? 742  VAL   B N   1 
ATOM   5873  C  CA  . VAL   B 2 438 ? -1.143  51.952  -8.764  1.00 94.88  ? 742  VAL   B CA  1 
ATOM   5874  C  C   . VAL   B 2 438 ? -2.611  51.916  -9.173  1.00 97.66  ? 742  VAL   B C   1 
ATOM   5875  O  O   . VAL   B 2 438 ? -3.422  52.645  -8.602  1.00 103.16 ? 742  VAL   B O   1 
ATOM   5876  C  CB  . VAL   B 2 438 ? -1.002  51.331  -7.377  1.00 90.04  ? 742  VAL   B CB  1 
ATOM   5877  C  CG1 . VAL   B 2 438 ? -1.646  52.252  -6.404  1.00 91.53  ? 742  VAL   B CG1 1 
ATOM   5878  C  CG2 . VAL   B 2 438 ? -1.725  50.033  -7.351  1.00 104.52 ? 742  VAL   B CG2 1 
ATOM   5879  N  N   . GLN   B 2 439 ? -2.972  51.020  -10.097 1.00 101.01 ? 743  GLN   B N   1 
ATOM   5880  C  CA  . GLN   B 2 439 ? -4.338  50.971  -10.632 1.00 105.34 ? 743  GLN   B CA  1 
ATOM   5881  C  C   . GLN   B 2 439 ? -5.369  50.817  -9.521  1.00 111.01 ? 743  GLN   B C   1 
ATOM   5882  O  O   . GLN   B 2 439 ? -5.288  49.888  -8.714  1.00 111.39 ? 743  GLN   B O   1 
ATOM   5883  C  CB  . GLN   B 2 439 ? -4.471  49.801  -11.599 1.00 105.76 ? 743  GLN   B CB  1 
ATOM   5884  C  CG  . GLN   B 2 439 ? -3.381  49.712  -12.638 1.00 110.32 ? 743  GLN   B CG  1 
ATOM   5885  C  CD  . GLN   B 2 439 ? -3.723  50.459  -13.912 1.00 111.91 ? 743  GLN   B CD  1 
ATOM   5886  O  OE1 . GLN   B 2 439 ? -4.638  51.300  -13.948 1.00 111.12 ? 743  GLN   B OE1 1 
ATOM   5887  N  NE2 . GLN   B 2 439 ? -2.992  50.146  -14.978 1.00 102.62 ? 743  GLN   B NE2 1 
ATOM   5888  N  N   . ASP   B 2 440 ? -6.375  51.695  -9.511  1.00 121.91 ? 744  ASP   B N   1 
ATOM   5889  C  CA  . ASP   B 2 440 ? -7.331  51.781  -8.407  1.00 125.03 ? 744  ASP   B CA  1 
ATOM   5890  C  C   . ASP   B 2 440 ? -8.645  51.089  -8.746  1.00 127.60 ? 744  ASP   B C   1 
ATOM   5891  O  O   . ASP   B 2 440 ? -9.039  50.983  -9.915  1.00 122.60 ? 744  ASP   B O   1 
ATOM   5892  C  CB  . ASP   B 2 440 ? -7.639  53.252  -8.059  1.00 127.01 ? 744  ASP   B CB  1 
ATOM   5893  C  CG  . ASP   B 2 440 ? -8.414  53.431  -6.728  1.00 133.01 ? 744  ASP   B CG  1 
ATOM   5894  O  OD1 . ASP   B 2 440 ? -8.823  52.414  -6.099  1.00 133.63 ? 744  ASP   B OD1 1 
ATOM   5895  O  OD2 . ASP   B 2 440 ? -8.609  54.594  -6.312  1.00 134.42 ? 744  ASP   B OD2 1 
ATOM   5896  N  N   . THR   B 2 441 ? -9.347  50.674  -7.680  1.00 137.27 ? 745  THR   B N   1 
ATOM   5897  C  CA  . THR   B 2 441 ? -10.663 50.042  -7.750  1.00 136.80 ? 745  THR   B CA  1 
ATOM   5898  C  C   . THR   B 2 441 ? -11.752 50.996  -8.224  1.00 133.53 ? 745  THR   B C   1 
ATOM   5899  O  O   . THR   B 2 441 ? -12.870 50.552  -8.499  1.00 130.64 ? 745  THR   B O   1 
ATOM   5900  C  CB  . THR   B 2 441 ? -11.053 49.475  -6.381  1.00 131.86 ? 745  THR   B CB  1 
ATOM   5901  O  OG1 . THR   B 2 441 ? -11.419 50.566  -5.517  1.00 133.58 ? 745  THR   B OG1 1 
ATOM   5902  C  CG2 . THR   B 2 441 ? -9.892  48.681  -5.762  1.00 124.81 ? 745  THR   B CG2 1 
ATOM   5903  N  N   . SER   B 2 442 ? -11.472 52.285  -8.308  1.00 132.69 ? 746  SER   B N   1 
ATOM   5904  C  CA  . SER   B 2 442 ? -12.406 53.176  -8.973  1.00 132.26 ? 746  SER   B CA  1 
ATOM   5905  C  C   . SER   B 2 442 ? -12.275 53.122  -10.493 1.00 133.06 ? 746  SER   B C   1 
ATOM   5906  O  O   . SER   B 2 442 ? -13.112 53.706  -11.191 1.00 136.22 ? 746  SER   B O   1 
ATOM   5907  C  CB  . SER   B 2 442 ? -12.215 54.610  -8.449  1.00 134.61 ? 746  SER   B CB  1 
ATOM   5908  O  OG  . SER   B 2 442 ? -10.849 54.925  -8.226  1.00 136.76 ? 746  SER   B OG  1 
ATOM   5909  N  N   . GLY   B 2 443 ? -11.288 52.407  -11.026 1.00 127.37 ? 747  GLY   B N   1 
ATOM   5910  C  CA  . GLY   B 2 443 ? -11.104 52.357  -12.457 1.00 128.46 ? 747  GLY   B CA  1 
ATOM   5911  C  C   . GLY   B 2 443 ? -10.084 53.335  -13.003 1.00 133.11 ? 747  GLY   B C   1 
ATOM   5912  O  O   . GLY   B 2 443 ? -10.137 53.666  -14.197 1.00 130.87 ? 747  GLY   B O   1 
ATOM   5913  N  N   . GLY   B 2 444 ? -9.165  53.815  -12.164 1.00 133.59 ? 748  GLY   B N   1 
ATOM   5914  C  CA  . GLY   B 2 444 ? -8.066  54.655  -12.600 1.00 130.06 ? 748  GLY   B CA  1 
ATOM   5915  C  C   . GLY   B 2 444 ? -6.745  54.271  -11.954 1.00 129.32 ? 748  GLY   B C   1 
ATOM   5916  O  O   . GLY   B 2 444 ? -6.374  53.088  -11.904 1.00 126.78 ? 748  GLY   B O   1 
ATOM   5917  N  N   . THR   B 2 445 ? -6.011  55.272  -11.465 1.00 117.78 ? 749  THR   B N   1 
ATOM   5918  C  CA  . THR   B 2 445 ? -4.797  55.038  -10.695 1.00 107.08 ? 749  THR   B CA  1 
ATOM   5919  C  C   . THR   B 2 445 ? -4.729  56.025  -9.545  1.00 103.89 ? 749  THR   B C   1 
ATOM   5920  O  O   . THR   B 2 445 ? -5.118  57.192  -9.671  1.00 111.32 ? 749  THR   B O   1 
ATOM   5921  C  CB  . THR   B 2 445 ? -3.519  55.144  -11.546 1.00 104.73 ? 749  THR   B CB  1 
ATOM   5922  O  OG1 . THR   B 2 445 ? -3.396  56.461  -12.096 1.00 109.02 ? 749  THR   B OG1 1 
ATOM   5923  C  CG2 . THR   B 2 445 ? -3.549  54.112  -12.659 1.00 104.84 ? 749  THR   B CG2 1 
ATOM   5924  N  N   . THR   B 2 446 ? -4.224  55.534  -8.432  1.00 104.89 ? 750  THR   B N   1 
ATOM   5925  C  CA  . THR   B 2 446 ? -4.059  56.275  -7.197  1.00 98.88  ? 750  THR   B CA  1 
ATOM   5926  C  C   . THR   B 2 446 ? -2.578  56.532  -6.972  1.00 93.31  ? 750  THR   B C   1 
ATOM   5927  O  O   . THR   B 2 446 ? -1.736  55.673  -7.247  1.00 95.18  ? 750  THR   B O   1 
ATOM   5928  C  CB  . THR   B 2 446 ? -4.636  55.461  -6.034  1.00 100.78 ? 750  THR   B CB  1 
ATOM   5929  O  OG1 . THR   B 2 446 ? -6.059  55.636  -5.972  1.00 113.44 ? 750  THR   B OG1 1 
ATOM   5930  C  CG2 . THR   B 2 446 ? -4.002  55.837  -4.719  1.00 94.81  ? 750  THR   B CG2 1 
ATOM   5931  N  N   . ALA   B 2 447 ? -2.255  57.714  -6.477  1.00 94.54  ? 751  ALA   B N   1 
ATOM   5932  C  CA  . ALA   B 2 447 ? -0.870  57.937  -6.089  1.00 97.08  ? 751  ALA   B CA  1 
ATOM   5933  C  C   . ALA   B 2 447 ? -0.599  57.290  -4.726  1.00 93.16  ? 751  ALA   B C   1 
ATOM   5934  O  O   . ALA   B 2 447 ? -1.509  57.068  -3.921  1.00 87.01  ? 751  ALA   B O   1 
ATOM   5935  C  CB  . ALA   B 2 447 ? -0.558  59.439  -6.068  1.00 95.52  ? 751  ALA   B CB  1 
ATOM   5936  N  N   . LEU   B 2 448 ? 0.660   56.956  -4.473  1.00 87.06  ? 752  LEU   B N   1 
ATOM   5937  C  CA  . LEU   B 2 448 ? 0.941   56.307  -3.202  1.00 88.42  ? 752  LEU   B CA  1 
ATOM   5938  C  C   . LEU   B 2 448 ? 1.138   57.290  -2.067  1.00 89.41  ? 752  LEU   B C   1 
ATOM   5939  O  O   . LEU   B 2 448 ? 1.069   56.891  -0.901  1.00 94.07  ? 752  LEU   B O   1 
ATOM   5940  C  CB  . LEU   B 2 448 ? 2.172   55.415  -3.317  1.00 89.10  ? 752  LEU   B CB  1 
ATOM   5941  C  CG  . LEU   B 2 448 ? 1.836   54.213  -4.176  1.00 86.12  ? 752  LEU   B CG  1 
ATOM   5942  C  CD1 . LEU   B 2 448 ? 3.079   53.365  -4.360  1.00 80.86  ? 752  LEU   B CD1 1 
ATOM   5943  C  CD2 . LEU   B 2 448 ? 0.688   53.451  -3.517  1.00 81.58  ? 752  LEU   B CD2 1 
ATOM   5944  N  N   . ARG   B 2 449 ? 1.371   58.554  -2.380  1.00 91.26  ? 753  ARG   B N   1 
ATOM   5945  C  CA  . ARG   B 2 449 ? 1.590   59.579  -1.374  1.00 85.29  ? 753  ARG   B CA  1 
ATOM   5946  C  C   . ARG   B 2 449 ? 1.698   60.922  -2.085  1.00 88.98  ? 753  ARG   B C   1 
ATOM   5947  O  O   . ARG   B 2 449 ? 2.009   60.973  -3.289  1.00 85.96  ? 753  ARG   B O   1 
ATOM   5948  C  CB  . ARG   B 2 449 ? 2.864   59.296  -0.563  1.00 82.57  ? 753  ARG   B CB  1 
ATOM   5949  C  CG  . ARG   B 2 449 ? 4.140   59.684  -1.275  1.00 83.44  ? 753  ARG   B CG  1 
ATOM   5950  C  CD  . ARG   B 2 449 ? 5.347   58.954  -0.730  1.00 89.06  ? 753  ARG   B CD  1 
ATOM   5951  N  NE  . ARG   B 2 449 ? 5.592   57.729  -1.480  1.00 88.87  ? 753  ARG   B NE  1 
ATOM   5952  C  CZ  . ARG   B 2 449 ? 5.790   56.539  -0.938  1.00 86.24  ? 753  ARG   B CZ  1 
ATOM   5953  N  NH1 . ARG   B 2 449 ? 5.834   56.374  0.383   1.00 78.60  ? 753  ARG   B NH1 1 
ATOM   5954  N  NH2 . ARG   B 2 449 ? 5.961   55.492  -1.741  1.00 94.31  ? 753  ARG   B NH2 1 
ATOM   5955  N  N   . PRO   B 2 450 ? 1.453   62.012  -1.368  1.00 89.91  ? 754  PRO   B N   1 
ATOM   5956  C  CA  . PRO   B 2 450 ? 1.673   63.344  -1.948  1.00 87.37  ? 754  PRO   B CA  1 
ATOM   5957  C  C   . PRO   B 2 450 ? 3.129   63.499  -2.353  1.00 83.46  ? 754  PRO   B C   1 
ATOM   5958  O  O   . PRO   B 2 450 ? 4.010   62.807  -1.838  1.00 85.22  ? 754  PRO   B O   1 
ATOM   5959  C  CB  . PRO   B 2 450 ? 1.322   64.287  -0.797  1.00 91.29  ? 754  PRO   B CB  1 
ATOM   5960  C  CG  . PRO   B 2 450 ? 1.641   63.458  0.448   1.00 91.27  ? 754  PRO   B CG  1 
ATOM   5961  C  CD  . PRO   B 2 450 ? 1.285   62.044  0.095   1.00 86.11  ? 754  PRO   B CD  1 
ATOM   5962  N  N   . SER   B 2 451 ? 3.393   64.423  -3.267  1.00 82.12  ? 755  SER   B N   1 
ATOM   5963  C  CA  . SER   B 2 451 ? 4.772   64.593  -3.715  1.00 84.21  ? 755  SER   B CA  1 
ATOM   5964  C  C   . SER   B 2 451 ? 4.831   65.697  -4.757  1.00 86.32  ? 755  SER   B C   1 
ATOM   5965  O  O   . SER   B 2 451 ? 3.802   66.264  -5.100  1.00 91.29  ? 755  SER   B O   1 
ATOM   5966  C  CB  . SER   B 2 451 ? 5.309   63.295  -4.283  1.00 83.69  ? 755  SER   B CB  1 
ATOM   5967  O  OG  . SER   B 2 451 ? 4.415   62.823  -5.284  1.00 91.17  ? 755  SER   B OG  1 
ATOM   5968  N  N   . ALA   B 2 452 ? 6.024   65.979  -5.295  1.00 81.55  ? 756  ALA   B N   1 
ATOM   5969  C  CA  . ALA   B 2 452 ? 6.220   67.132  -6.152  1.00 83.27  ? 756  ALA   B CA  1 
ATOM   5970  C  C   . ALA   B 2 452 ? 5.133   67.442  -7.196  1.00 88.06  ? 756  ALA   B C   1 
ATOM   5971  O  O   . ALA   B 2 452 ? 4.579   68.545  -7.199  1.00 95.84  ? 756  ALA   B O   1 
ATOM   5972  C  CB  . ALA   B 2 452 ? 7.501   67.074  -6.946  1.00 78.95  ? 756  ALA   B CB  1 
ATOM   5973  N  N   . SER   B 2 453 ? 4.852   66.493  -8.098  1.00 85.51  ? 757  SER   B N   1 
ATOM   5974  C  CA  . SER   B 2 453 ? 3.793   66.652  -9.078  1.00 87.75  ? 757  SER   B CA  1 
ATOM   5975  C  C   . SER   B 2 453 ? 2.455   66.835  -8.316  1.00 90.26  ? 757  SER   B C   1 
ATOM   5976  O  O   . SER   B 2 453 ? 1.693   67.776  -8.566  1.00 93.16  ? 757  SER   B O   1 
ATOM   5977  C  CB  . SER   B 2 453 ? 3.723   65.444  -10.004 1.00 91.73  ? 757  SER   B CB  1 
ATOM   5978  O  OG  . SER   B 2 453 ? 3.374   64.234  -9.314  1.00 87.84  ? 757  SER   B OG  1 
ATOM   5979  N  N   . THR   B 2 454 ? 2.175   65.925  -7.376  1.00 93.63  ? 758  THR   B N   1 
ATOM   5980  C  CA  . THR   B 2 454 ? 0.950   65.988  -6.576  1.00 94.06  ? 758  THR   B CA  1 
ATOM   5981  C  C   . THR   B 2 454 ? 0.715   67.364  -5.988  1.00 93.07  ? 758  THR   B C   1 
ATOM   5982  O  O   . THR   B 2 454 ? -0.381  67.922  -6.074  1.00 94.23  ? 758  THR   B O   1 
ATOM   5983  C  CB  . THR   B 2 454 ? 1.012   64.985  -5.431  1.00 91.34  ? 758  THR   B CB  1 
ATOM   5984  O  OG1 . THR   B 2 454 ? 1.371   63.707  -5.945  1.00 96.42  ? 758  THR   B OG1 1 
ATOM   5985  C  CG2 . THR   B 2 454 ? -0.331  64.902  -4.732  1.00 91.50  ? 758  THR   B CG2 1 
ATOM   5986  N  N   . GLN   B 2 455 ? 1.710   67.900  -5.324  1.00 95.71  ? 759  GLN   B N   1 
ATOM   5987  C  CA  . GLN   B 2 455 ? 1.477   69.137  -4.617  1.00 98.08  ? 759  GLN   B CA  1 
ATOM   5988  C  C   . GLN   B 2 455 ? 2.327   70.263  -5.209  1.00 99.04  ? 759  GLN   B C   1 
ATOM   5989  O  O   . GLN   B 2 455 ? 3.224   70.757  -4.554  1.00 104.54 ? 759  GLN   B O   1 
ATOM   5990  C  CB  . GLN   B 2 455 ? 1.778   68.923  -3.118  1.00 97.57  ? 759  GLN   B CB  1 
ATOM   5991  C  CG  . GLN   B 2 455 ? 3.229   68.501  -2.859  1.00 99.42  ? 759  GLN   B CG  1 
ATOM   5992  C  CD  . GLN   B 2 455 ? 3.402   67.757  -1.548  1.00 103.39 ? 759  GLN   B CD  1 
ATOM   5993  O  OE1 . GLN   B 2 455 ? 2.450   67.646  -0.765  1.00 103.96 ? 759  GLN   B OE1 1 
ATOM   5994  N  NE2 . GLN   B 2 455 ? 4.619   67.235  -1.300  1.00 101.58 ? 759  GLN   B NE2 1 
ATOM   5995  N  N   . ALA   B 2 456 ? 2.068   70.659  -6.452  1.00 95.55  ? 760  ALA   B N   1 
ATOM   5996  C  CA  . ALA   B 2 456 ? 2.707   71.844  -7.004  1.00 94.36  ? 760  ALA   B CA  1 
ATOM   5997  C  C   . ALA   B 2 456 ? 1.672   72.944  -7.144  1.00 98.23  ? 760  ALA   B C   1 
ATOM   5998  O  O   . ALA   B 2 456 ? 0.523   72.672  -7.511  1.00 102.93 ? 760  ALA   B O   1 
ATOM   5999  C  CB  . ALA   B 2 456 ? 3.352   71.591  -8.371  1.00 92.57  ? 760  ALA   B CB  1 
ATOM   6000  N  N   . LEU   B 2 457 ? 2.080   74.186  -6.865  1.00 97.15  ? 761  LEU   B N   1 
ATOM   6001  C  CA  . LEU   B 2 457 ? 1.148   75.308  -6.919  1.00 93.10  ? 761  LEU   B CA  1 
ATOM   6002  C  C   . LEU   B 2 457 ? 0.269   75.222  -8.158  1.00 96.40  ? 761  LEU   B C   1 
ATOM   6003  O  O   . LEU   B 2 457 ? -0.954  75.109  -8.055  1.00 103.82 ? 761  LEU   B O   1 
ATOM   6004  C  CB  . LEU   B 2 457 ? 1.923   76.622  -6.882  1.00 96.52  ? 761  LEU   B CB  1 
ATOM   6005  C  CG  . LEU   B 2 457 ? 2.884   76.595  -5.690  1.00 106.62 ? 761  LEU   B CG  1 
ATOM   6006  C  CD1 . LEU   B 2 457 ? 3.882   77.758  -5.700  1.00 102.67 ? 761  LEU   B CD1 1 
ATOM   6007  C  CD2 . LEU   B 2 457 ? 2.114   76.520  -4.357  1.00 99.30  ? 761  LEU   B CD2 1 
ATOM   6008  N  N   . SER   B 2 458 ? 0.877   75.238  -9.337  1.00 94.67  ? 762  SER   B N   1 
ATOM   6009  C  CA  . SER   B 2 458 ? 0.142   75.075  -10.577 1.00 95.81  ? 762  SER   B CA  1 
ATOM   6010  C  C   . SER   B 2 458 ? 0.555   73.774  -11.261 1.00 96.45  ? 762  SER   B C   1 
ATOM   6011  O  O   . SER   B 2 458 ? 1.691   73.309  -11.128 1.00 94.02  ? 762  SER   B O   1 
ATOM   6012  C  CB  . SER   B 2 458 ? 0.364   76.270  -11.512 1.00 98.04  ? 762  SER   B CB  1 
ATOM   6013  O  OG  . SER   B 2 458 ? 1.637   76.220  -12.147 1.00 103.53 ? 762  SER   B OG  1 
ATOM   6014  N  N   . SER   B 2 459 ? -0.382  73.191  -11.998 1.00 93.61  ? 763  SER   B N   1 
ATOM   6015  C  CA  . SER   B 2 459 ? -0.176  71.949  -12.715 1.00 92.05  ? 763  SER   B CA  1 
ATOM   6016  C  C   . SER   B 2 459 ? -0.745  72.096  -14.111 1.00 90.88  ? 763  SER   B C   1 
ATOM   6017  O  O   . SER   B 2 459 ? -1.558  72.974  -14.365 1.00 98.41  ? 763  SER   B O   1 
ATOM   6018  C  CB  . SER   B 2 459 ? -0.878  70.806  -12.006 1.00 97.17  ? 763  SER   B CB  1 
ATOM   6019  O  OG  . SER   B 2 459 ? -2.209  71.207  -11.754 1.00 98.70  ? 763  SER   B OG  1 
ATOM   6020  N  N   . SER   B 2 460 ? -0.331  71.214  -15.015 1.00 95.57  ? 764  SER   B N   1 
ATOM   6021  C  CA  . SER   B 2 460 ? -0.898  71.146  -16.359 1.00 91.22  ? 764  SER   B CA  1 
ATOM   6022  C  C   . SER   B 2 460 ? -0.766  69.720  -16.868 1.00 93.79  ? 764  SER   B C   1 
ATOM   6023  O  O   . SER   B 2 460 ? 0.079   68.948  -16.392 1.00 94.00  ? 764  SER   B O   1 
ATOM   6024  C  CB  . SER   B 2 460 ? -0.203  72.107  -17.329 1.00 93.15  ? 764  SER   B CB  1 
ATOM   6025  O  OG  . SER   B 2 460 ? 1.117   71.671  -17.602 1.00 91.66  ? 764  SER   B OG  1 
ATOM   6026  N  N   . VAL   B 2 461 ? -1.607  69.376  -17.847 1.00 95.97  ? 765  VAL   B N   1 
ATOM   6027  C  CA  . VAL   B 2 461 ? -1.647  68.029  -18.415 1.00 97.23  ? 765  VAL   B CA  1 
ATOM   6028  C  C   . VAL   B 2 461 ? -1.641  68.125  -19.940 1.00 100.62 ? 765  VAL   B C   1 
ATOM   6029  O  O   . VAL   B 2 461 ? -2.477  68.826  -20.526 1.00 106.88 ? 765  VAL   B O   1 
ATOM   6030  C  CB  . VAL   B 2 461 ? -2.871  67.232  -17.931 1.00 97.25  ? 765  VAL   B CB  1 
ATOM   6031  C  CG1 . VAL   B 2 461 ? -2.859  65.843  -18.539 1.00 98.61  ? 765  VAL   B CG1 1 
ATOM   6032  C  CG2 . VAL   B 2 461 ? -2.896  67.163  -16.397 1.00 95.38  ? 765  VAL   B CG2 1 
ATOM   6033  N  N   . SER   B 2 462 ? -0.701  67.418  -20.578 1.00 101.78 ? 766  SER   B N   1 
ATOM   6034  C  CA  . SER   B 2 462 ? -0.535  67.528  -22.020 1.00 104.48 ? 766  SER   B CA  1 
ATOM   6035  C  C   . SER   B 2 462 ? -1.826  67.152  -22.731 1.00 108.24 ? 766  SER   B C   1 
ATOM   6036  O  O   . SER   B 2 462 ? -2.626  66.350  -22.244 1.00 103.58 ? 766  SER   B O   1 
ATOM   6037  C  CB  . SER   B 2 462 ? 0.617   66.647  -22.502 1.00 99.65  ? 766  SER   B CB  1 
ATOM   6038  O  OG  . SER   B 2 462 ? 1.859   67.099  -21.978 1.00 96.69  ? 766  SER   B OG  1 
ATOM   6039  N  N   . SER   B 2 463 ? -2.028  67.761  -23.883 1.00 124.18 ? 767  SER   B N   1 
ATOM   6040  C  CA  . SER   B 2 463 ? -3.261  67.622  -24.645 1.00 130.89 ? 767  SER   B CA  1 
ATOM   6041  C  C   . SER   B 2 463 ? -2.851  67.539  -26.109 1.00 134.88 ? 767  SER   B C   1 
ATOM   6042  O  O   . SER   B 2 463 ? -2.867  68.537  -26.838 1.00 141.52 ? 767  SER   B O   1 
ATOM   6043  C  CB  . SER   B 2 463 ? -4.211  68.789  -24.380 1.00 137.36 ? 767  SER   B CB  1 
ATOM   6044  O  OG  . SER   B 2 463 ? -5.101  68.993  -25.466 1.00 144.26 ? 767  SER   B OG  1 
ATOM   6045  N  N   . SER   B 2 464 ? -2.473  66.339  -26.541 1.00 125.96 ? 768  SER   B N   1 
ATOM   6046  C  CA  . SER   B 2 464 ? -1.831  66.181  -27.839 1.00 130.40 ? 768  SER   B CA  1 
ATOM   6047  C  C   . SER   B 2 464 ? -2.731  65.543  -28.883 1.00 137.38 ? 768  SER   B C   1 
ATOM   6048  O  O   . SER   B 2 464 ? -2.812  66.036  -30.015 1.00 138.28 ? 768  SER   B O   1 
ATOM   6049  C  CB  . SER   B 2 464 ? -0.543  65.362  -27.705 1.00 123.70 ? 768  SER   B CB  1 
ATOM   6050  O  OG  . SER   B 2 464 ? -0.826  64.039  -27.272 1.00 119.07 ? 768  SER   B OG  1 
ATOM   6051  N  N   . LYS   B 2 465 ? -3.403  64.449  -28.548 1.00 137.86 ? 769  LYS   B N   1 
ATOM   6052  C  CA  . LYS   B 2 465 ? -4.200  63.698  -29.511 1.00 139.93 ? 769  LYS   B CA  1 
ATOM   6053  C  C   . LYS   B 2 465 ? -3.357  63.152  -30.659 1.00 141.91 ? 769  LYS   B C   1 
ATOM   6054  O  O   . LYS   B 2 465 ? -3.913  62.699  -31.667 1.00 142.91 ? 769  LYS   B O   1 
ATOM   6055  C  CB  . LYS   B 2 465 ? -5.353  64.552  -30.066 1.00 134.86 ? 769  LYS   B CB  1 
ATOM   6056  N  N   . LEU   B 2 466 ? -2.021  63.192  -30.545 1.00 138.28 ? 770  LEU   B N   1 
ATOM   6057  C  CA  . LEU   B 2 466 ? -1.173  62.658  -31.605 1.00 135.78 ? 770  LEU   B CA  1 
ATOM   6058  C  C   . LEU   B 2 466 ? -1.239  61.146  -31.671 1.00 136.47 ? 770  LEU   B C   1 
ATOM   6059  O  O   . LEU   B 2 466 ? -0.877  60.557  -32.697 1.00 133.60 ? 770  LEU   B O   1 
ATOM   6060  C  CB  . LEU   B 2 466 ? 0.275   63.108  -31.410 1.00 130.72 ? 770  LEU   B CB  1 
ATOM   6061  C  CG  . LEU   B 2 466 ? 0.536   64.486  -32.018 1.00 133.15 ? 770  LEU   B CG  1 
ATOM   6062  C  CD1 . LEU   B 2 466 ? 0.085   64.488  -33.472 1.00 136.51 ? 770  LEU   B CD1 1 
ATOM   6063  C  CD2 . LEU   B 2 466 ? -0.192  65.595  -31.249 1.00 134.74 ? 770  LEU   B CD2 1 
ATOM   6064  N  N   . PHE   B 2 467 ? -1.690  60.512  -30.599 1.00 141.51 ? 771  PHE   B N   1 
ATOM   6065  C  CA  . PHE   B 2 467 ? -1.753  59.067  -30.516 1.00 143.13 ? 771  PHE   B CA  1 
ATOM   6066  C  C   . PHE   B 2 467 ? -3.113  58.673  -29.953 1.00 149.92 ? 771  PHE   B C   1 
ATOM   6067  O  O   . PHE   B 2 467 ? -3.871  59.513  -29.462 1.00 150.41 ? 771  PHE   B O   1 
ATOM   6068  C  CB  . PHE   B 2 467 ? -0.588  58.543  -29.671 1.00 131.40 ? 771  PHE   B CB  1 
ATOM   6069  C  CG  . PHE   B 2 467 ? 0.734   59.196  -30.017 1.00 126.81 ? 771  PHE   B CG  1 
ATOM   6070  C  CD1 . PHE   B 2 467 ? 1.366   58.932  -31.231 1.00 125.09 ? 771  PHE   B CD1 1 
ATOM   6071  C  CD2 . PHE   B 2 467 ? 1.330   60.092  -29.151 1.00 122.04 ? 771  PHE   B CD2 1 
ATOM   6072  C  CE1 . PHE   B 2 467 ? 2.578   59.538  -31.560 1.00 115.65 ? 771  PHE   B CE1 1 
ATOM   6073  C  CE2 . PHE   B 2 467 ? 2.545   60.697  -29.475 1.00 116.32 ? 771  PHE   B CE2 1 
ATOM   6074  C  CZ  . PHE   B 2 467 ? 3.168   60.414  -30.679 1.00 109.97 ? 771  PHE   B CZ  1 
ATOM   6075  N  N   . SER   B 2 468 ? -3.441  57.388  -30.062 1.00 168.62 ? 772  SER   B N   1 
ATOM   6076  C  CA  . SER   B 2 468 ? -4.739  56.883  -29.621 1.00 169.29 ? 772  SER   B CA  1 
ATOM   6077  C  C   . SER   B 2 468 ? -4.665  55.973  -28.411 1.00 170.74 ? 772  SER   B C   1 
ATOM   6078  O  O   . SER   B 2 468 ? -5.574  55.996  -27.577 1.00 175.85 ? 772  SER   B O   1 
ATOM   6079  C  CB  . SER   B 2 468 ? -5.430  56.118  -30.748 1.00 169.24 ? 772  SER   B CB  1 
ATOM   6080  O  OG  . SER   B 2 468 ? -4.682  54.976  -31.086 1.00 170.86 ? 772  SER   B OG  1 
ATOM   6081  N  N   . SER   B 2 469 ? -3.633  55.142  -28.313 1.00 155.61 ? 773  SER   B N   1 
ATOM   6082  C  CA  . SER   B 2 469 ? -3.475  54.261  -27.167 1.00 145.51 ? 773  SER   B CA  1 
ATOM   6083  C  C   . SER   B 2 469 ? -2.578  54.934  -26.137 1.00 143.70 ? 773  SER   B C   1 
ATOM   6084  O  O   . SER   B 2 469 ? -2.038  56.013  -26.383 1.00 141.70 ? 773  SER   B O   1 
ATOM   6085  C  CB  . SER   B 2 469 ? -2.889  52.912  -27.593 1.00 141.73 ? 773  SER   B CB  1 
ATOM   6086  O  OG  . SER   B 2 469 ? -3.704  52.275  -28.561 1.00 147.94 ? 773  SER   B OG  1 
ATOM   6087  N  N   . HIS   B 2 474 ? -8.767  47.025  -21.110 1.00 103.78 ? 778  HIS   B N   1 
ATOM   6088  C  CA  . HIS   B 2 474 ? -8.921  47.513  -19.720 1.00 111.39 ? 778  HIS   B CA  1 
ATOM   6089  C  C   . HIS   B 2 474 ? -8.610  46.380  -18.745 1.00 119.96 ? 778  HIS   B C   1 
ATOM   6090  O  O   . HIS   B 2 474 ? -8.719  46.586  -17.521 1.00 119.19 ? 778  HIS   B O   1 
ATOM   6091  C  CB  . HIS   B 2 474 ? -10.317 48.042  -19.511 1.00 101.26 ? 778  HIS   B CB  1 
ATOM   6092  N  N   . GLU   B 2 475 ? -8.239  45.215  -19.275 1.00 121.73 ? 779  GLU   B N   1 
ATOM   6093  C  CA  . GLU   B 2 475 ? -7.874  44.074  -18.407 1.00 119.58 ? 779  GLU   B CA  1 
ATOM   6094  C  C   . GLU   B 2 475 ? -6.405  44.198  -18.009 1.00 123.51 ? 779  GLU   B C   1 
ATOM   6095  O  O   . GLU   B 2 475 ? -5.560  43.510  -18.617 1.00 120.01 ? 779  GLU   B O   1 
ATOM   6096  C  CB  . GLU   B 2 475 ? -8.147  42.777  -19.123 1.00 116.15 ? 779  GLU   B CB  1 
ATOM   6097  N  N   . THR   B 2 476 ? -6.109  45.061  -17.034 1.00 126.15 ? 780  THR   B N   1 
ATOM   6098  C  CA  . THR   B 2 476 ? -4.728  45.210  -16.534 1.00 124.97 ? 780  THR   B CA  1 
ATOM   6099  C  C   . THR   B 2 476 ? -4.606  44.365  -15.297 1.00 125.01 ? 780  THR   B C   1 
ATOM   6100  O  O   . THR   B 2 476 ? -4.669  43.127  -15.429 1.00 131.51 ? 780  THR   B O   1 
ATOM   6101  C  CB  . THR   B 2 476 ? -4.457  46.680  -16.236 1.00 123.10 ? 780  THR   B CB  1 
ATOM   6102  O  OG1 . THR   B 2 476 ? -5.491  47.071  -15.339 1.00 124.71 ? 780  THR   B OG1 1 
ATOM   6103  C  CG2 . THR   B 2 476 ? -4.512  47.544  -17.482 1.00 117.45 ? 780  THR   B CG2 1 
ATOM   6104  N  N   . SER   B 2 477 ? -4.459  44.998  -14.134 1.00 120.81 ? 781  SER   B N   1 
ATOM   6105  C  CA  . SER   B 2 477 ? -4.428  44.243  -12.857 1.00 117.26 ? 781  SER   B CA  1 
ATOM   6106  C  C   . SER   B 2 477 ? -4.653  45.311  -11.787 1.00 110.37 ? 781  SER   B C   1 
ATOM   6107  O  O   . SER   B 2 477 ? -4.020  46.374  -11.872 1.00 116.83 ? 781  SER   B O   1 
ATOM   6108  C  CB  . SER   B 2 477 ? -3.188  43.411  -12.733 1.00 121.53 ? 781  SER   B CB  1 
ATOM   6109  O  OG  . SER   B 2 477 ? -3.156  42.733  -11.485 1.00 132.06 ? 781  SER   B OG  1 
ATOM   6110  N  N   . PHE   B 2 478 ? -5.528  45.038  -10.827 1.00 107.34 ? 782  PHE   B N   1 
ATOM   6111  C  CA  . PHE   B 2 478 ? -5.684  46.005  -9.715  1.00 109.07 ? 782  PHE   B CA  1 
ATOM   6112  C  C   . PHE   B 2 478 ? -4.434  45.721  -8.905  1.00 109.65 ? 782  PHE   B C   1 
ATOM   6113  O  O   . PHE   B 2 478 ? -4.241  44.574  -8.463  1.00 108.89 ? 782  PHE   B O   1 
ATOM   6114  C  CB  . PHE   B 2 478 ? -6.988  45.741  -8.959  1.00 100.96 ? 782  PHE   B CB  1 
ATOM   6115  C  CG  . PHE   B 2 478 ? -8.235  46.172  -9.713  1.00 102.43 ? 782  PHE   B CG  1 
ATOM   6116  C  CD1 . PHE   B 2 478 ? -8.590  47.512  -9.793  1.00 105.96 ? 782  PHE   B CD1 1 
ATOM   6117  C  CD2 . PHE   B 2 478 ? -9.044  45.237  -10.346 1.00 108.74 ? 782  PHE   B CD2 1 
ATOM   6118  C  CE1 . PHE   B 2 478 ? -9.724  47.901  -10.485 1.00 110.63 ? 782  PHE   B CE1 1 
ATOM   6119  C  CE2 . PHE   B 2 478 ? -10.177 45.633  -11.036 1.00 110.75 ? 782  PHE   B CE2 1 
ATOM   6120  C  CZ  . PHE   B 2 478 ? -10.515 46.963  -11.102 1.00 109.24 ? 782  PHE   B CZ  1 
ATOM   6121  N  N   . GLY   B 2 479 ? -3.583  46.731  -8.747  1.00 117.67 ? 783  GLY   B N   1 
ATOM   6122  C  CA  . GLY   B 2 479 ? -2.320  46.542  -8.015  1.00 120.34 ? 783  GLY   B CA  1 
ATOM   6123  C  C   . GLY   B 2 479 ? -1.143  46.842  -8.914  1.00 120.03 ? 783  GLY   B C   1 
ATOM   6124  O  O   . GLY   B 2 479 ? -0.119  47.338  -8.409  1.00 121.05 ? 783  GLY   B O   1 
ATOM   6125  N  N   . GLU   B 2 480 ? -1.280  46.548  -10.206 1.00 115.22 ? 784  GLU   B N   1 
ATOM   6126  C  CA  . GLU   B 2 480 ? -0.200  46.877  -11.163 1.00 113.58 ? 784  GLU   B CA  1 
ATOM   6127  C  C   . GLU   B 2 480 ? 0.185   48.338  -10.934 1.00 110.44 ? 784  GLU   B C   1 
ATOM   6128  O  O   . GLU   B 2 480 ? -0.724  49.179  -10.815 1.00 109.73 ? 784  GLU   B O   1 
ATOM   6129  C  CB  . GLU   B 2 480 ? -0.670  46.692  -12.602 1.00 119.15 ? 784  GLU   B CB  1 
ATOM   6130  C  CG  . GLU   B 2 480 ? -0.128  45.427  -13.258 1.00 126.57 ? 784  GLU   B CG  1 
ATOM   6131  C  CD  . GLU   B 2 480 ? -0.735  45.158  -14.623 1.00 129.49 ? 784  GLU   B CD  1 
ATOM   6132  O  OE1 . GLU   B 2 480 ? -0.710  43.991  -15.065 1.00 129.27 ? 784  GLU   B OE1 1 
ATOM   6133  O  OE2 . GLU   B 2 480 ? -1.233  46.120  -15.243 1.00 129.35 ? 784  GLU   B OE2 1 
ATOM   6134  N  N   . GLU   B 2 481 ? 1.481   48.623  -10.883 1.00 96.90  ? 785  GLU   B N   1 
ATOM   6135  C  CA  . GLU   B 2 481 ? 1.875   50.009  -10.725 1.00 90.88  ? 785  GLU   B CA  1 
ATOM   6136  C  C   . GLU   B 2 481 ? 2.144   50.673  -12.070 1.00 86.16  ? 785  GLU   B C   1 
ATOM   6137  O  O   . GLU   B 2 481 ? 2.521   50.026  -13.043 1.00 83.26  ? 785  GLU   B O   1 
ATOM   6138  C  CB  . GLU   B 2 481 ? 3.096   50.156  -9.810  1.00 93.34  ? 785  GLU   B CB  1 
ATOM   6139  C  CG  . GLU   B 2 481 ? 4.049   49.001  -9.737  1.00 96.13  ? 785  GLU   B CG  1 
ATOM   6140  C  CD  . GLU   B 2 481 ? 5.194   49.254  -8.744  1.00 96.55  ? 785  GLU   B CD  1 
ATOM   6141  O  OE1 . GLU   B 2 481 ? 6.349   49.419  -9.196  1.00 102.58 ? 785  GLU   B OE1 1 
ATOM   6142  O  OE2 . GLU   B 2 481 ? 4.944   49.299  -7.515  1.00 90.55  ? 785  GLU   B OE2 1 
ATOM   6143  N  N   . VAL   B 2 482 ? 1.947   51.989  -12.101 1.00 87.78  ? 786  VAL   B N   1 
ATOM   6144  C  CA  . VAL   B 2 482 ? 2.222   52.806  -13.269 1.00 79.18  ? 786  VAL   B CA  1 
ATOM   6145  C  C   . VAL   B 2 482 ? 3.063   54.010  -12.881 1.00 79.17  ? 786  VAL   B C   1 
ATOM   6146  O  O   . VAL   B 2 482 ? 2.929   54.555  -11.782 1.00 84.06  ? 786  VAL   B O   1 
ATOM   6147  C  CB  . VAL   B 2 482 ? 0.922   53.268  -13.921 1.00 77.93  ? 786  VAL   B CB  1 
ATOM   6148  C  CG1 . VAL   B 2 482 ? 1.203   53.662  -15.340 1.00 82.01  ? 786  VAL   B CG1 1 
ATOM   6149  C  CG2 . VAL   B 2 482 ? -0.127  52.165  -13.819 1.00 89.15  ? 786  VAL   B CG2 1 
ATOM   6150  N  N   . GLU   B 2 483 ? 3.924   54.432  -13.804 1.00 75.13  ? 787  GLU   B N   1 
ATOM   6151  C  CA  . GLU   B 2 483 ? 4.728   55.641  -13.663 1.00 74.40  ? 787  GLU   B CA  1 
ATOM   6152  C  C   . GLU   B 2 483 ? 4.024   56.828  -14.319 1.00 82.78  ? 787  GLU   B C   1 
ATOM   6153  O  O   . GLU   B 2 483 ? 3.536   56.710  -15.450 1.00 84.70  ? 787  GLU   B O   1 
ATOM   6154  C  CB  . GLU   B 2 483 ? 6.090   55.449  -14.317 1.00 71.71  ? 787  GLU   B CB  1 
ATOM   6155  C  CG  . GLU   B 2 483 ? 7.016   54.561  -13.575 1.00 75.45  ? 787  GLU   B CG  1 
ATOM   6156  C  CD  . GLU   B 2 483 ? 8.318   54.342  -14.322 1.00 85.06  ? 787  GLU   B CD  1 
ATOM   6157  O  OE1 . GLU   B 2 483 ? 8.718   55.218  -15.126 1.00 79.08  ? 787  GLU   B OE1 1 
ATOM   6158  O  OE2 . GLU   B 2 483 ? 8.945   53.278  -14.103 1.00 103.88 ? 787  GLU   B OE2 1 
ATOM   6159  N  N   . VAL   B 2 484 ? 4.007   57.979  -13.638 1.00 81.14  ? 788  VAL   B N   1 
ATOM   6160  C  CA  . VAL   B 2 484 ? 3.459   59.219  -14.194 1.00 76.84  ? 788  VAL   B CA  1 
ATOM   6161  C  C   . VAL   B 2 484 ? 4.602   60.232  -14.340 1.00 80.20  ? 788  VAL   B C   1 
ATOM   6162  O  O   . VAL   B 2 484 ? 5.098   60.776  -13.346 1.00 85.58  ? 788  VAL   B O   1 
ATOM   6163  C  CB  . VAL   B 2 484 ? 2.315   59.779  -13.336 1.00 81.19  ? 788  VAL   B CB  1 
ATOM   6164  C  CG1 . VAL   B 2 484 ? 1.528   60.800  -14.109 1.00 83.62  ? 788  VAL   B CG1 1 
ATOM   6165  C  CG2 . VAL   B 2 484 ? 1.389   58.680  -12.863 1.00 81.16  ? 788  VAL   B CG2 1 
ATOM   6166  N  N   . HIS   B 2 485 ? 5.000   60.511  -15.578 1.00 81.74  ? 789  HIS   B N   1 
ATOM   6167  C  CA  . HIS   B 2 485 ? 6.117   61.412  -15.874 1.00 84.83  ? 789  HIS   B CA  1 
ATOM   6168  C  C   . HIS   B 2 485 ? 5.683   62.888  -15.891 1.00 83.75  ? 789  HIS   B C   1 
ATOM   6169  O  O   . HIS   B 2 485 ? 4.694   63.236  -16.539 1.00 82.29  ? 789  HIS   B O   1 
ATOM   6170  C  CB  . HIS   B 2 485 ? 6.738   60.991  -17.213 1.00 79.39  ? 789  HIS   B CB  1 
ATOM   6171  C  CG  . HIS   B 2 485 ? 7.627   59.801  -17.089 1.00 80.50  ? 789  HIS   B CG  1 
ATOM   6172  N  ND1 . HIS   B 2 485 ? 8.857   59.717  -17.704 1.00 85.07  ? 789  HIS   B ND1 1 
ATOM   6173  C  CD2 . HIS   B 2 485 ? 7.494   58.671  -16.357 1.00 80.71  ? 789  HIS   B CD2 1 
ATOM   6174  C  CE1 . HIS   B 2 485 ? 9.434   58.572  -17.373 1.00 81.12  ? 789  HIS   B CE1 1 
ATOM   6175  N  NE2 . HIS   B 2 485 ? 8.629   57.921  -16.554 1.00 79.41  ? 789  HIS   B NE2 1 
ATOM   6176  N  N   . ASN   B 2 486 ? 6.420   63.755  -15.170 1.00 83.45  ? 790  ASN   B N   1 
ATOM   6177  C  CA  . ASN   B 2 486 ? 6.118   65.186  -15.092 1.00 79.49  ? 790  ASN   B CA  1 
ATOM   6178  C  C   . ASN   B 2 486 ? 7.335   66.051  -15.395 1.00 81.62  ? 790  ASN   B C   1 
ATOM   6179  O  O   . ASN   B 2 486 ? 8.477   65.673  -15.116 1.00 77.24  ? 790  ASN   B O   1 
ATOM   6180  C  CB  . ASN   B 2 486 ? 5.625   65.603  -13.714 1.00 81.39  ? 790  ASN   B CB  1 
ATOM   6181  C  CG  . ASN   B 2 486 ? 4.257   65.102  -13.411 1.00 87.29  ? 790  ASN   B CG  1 
ATOM   6182  O  OD1 . ASN   B 2 486 ? 3.270   65.824  -13.609 1.00 84.83  ? 790  ASN   B OD1 1 
ATOM   6183  N  ND2 . ASN   B 2 486 ? 4.172   63.858  -12.913 1.00 87.39  ? 790  ASN   B ND2 1 
ATOM   6184  N  N   . LEU   B 2 487 ? 7.072   67.246  -15.922 1.00 84.88  ? 791  LEU   B N   1 
ATOM   6185  C  CA  . LEU   B 2 487 ? 8.057   68.316  -15.937 1.00 78.56  ? 791  LEU   B CA  1 
ATOM   6186  C  C   . LEU   B 2 487 ? 7.798   69.181  -14.727 1.00 80.44  ? 791  LEU   B C   1 
ATOM   6187  O  O   . LEU   B 2 487 ? 6.696   69.720  -14.579 1.00 82.89  ? 791  LEU   B O   1 
ATOM   6188  C  CB  . LEU   B 2 487 ? 7.970   69.153  -17.204 1.00 79.72  ? 791  LEU   B CB  1 
ATOM   6189  C  CG  . LEU   B 2 487 ? 8.971   70.289  -17.238 1.00 80.87  ? 791  LEU   B CG  1 
ATOM   6190  C  CD1 . LEU   B 2 487 ? 10.275  69.862  -16.567 1.00 75.16  ? 791  LEU   B CD1 1 
ATOM   6191  C  CD2 . LEU   B 2 487 ? 9.188   70.698  -18.685 1.00 77.57  ? 791  LEU   B CD2 1 
ATOM   6192  N  N   . LEU   B 2 488 ? 8.779   69.260  -13.838 1.00 81.73  ? 792  LEU   B N   1 
ATOM   6193  C  CA  . LEU   B 2 488 ? 8.712   70.151  -12.689 1.00 85.07  ? 792  LEU   B CA  1 
ATOM   6194  C  C   . LEU   B 2 488 ? 9.476   71.435  -12.970 1.00 85.43  ? 792  LEU   B C   1 
ATOM   6195  O  O   . LEU   B 2 488 ? 10.533  71.416  -13.610 1.00 85.03  ? 792  LEU   B O   1 
ATOM   6196  C  CB  . LEU   B 2 488 ? 9.300   69.506  -11.447 1.00 79.09  ? 792  LEU   B CB  1 
ATOM   6197  C  CG  . LEU   B 2 488 ? 8.624   68.213  -11.121 1.00 74.93  ? 792  LEU   B CG  1 
ATOM   6198  C  CD1 . LEU   B 2 488 ? 9.593   67.465  -10.268 1.00 71.41  ? 792  LEU   B CD1 1 
ATOM   6199  C  CD2 . LEU   B 2 488 ? 7.345   68.524  -10.386 1.00 79.89  ? 792  LEU   B CD2 1 
ATOM   6200  N  N   . ILE   B 2 489 ? 8.938   72.539  -12.471 1.00 86.96  ? 793  ILE   B N   1 
ATOM   6201  C  CA  . ILE   B 2 489 ? 9.557   73.852  -12.559 1.00 86.35  ? 793  ILE   B CA  1 
ATOM   6202  C  C   . ILE   B 2 489 ? 9.756   74.313  -11.122 1.00 88.01  ? 793  ILE   B C   1 
ATOM   6203  O  O   . ILE   B 2 489 ? 8.794   74.701  -10.444 1.00 88.60  ? 793  ILE   B O   1 
ATOM   6204  C  CB  . ILE   B 2 489 ? 8.704   74.833  -13.374 1.00 86.39  ? 793  ILE   B CB  1 
ATOM   6205  C  CG1 . ILE   B 2 489 ? 8.681   74.382  -14.821 1.00 88.15  ? 793  ILE   B CG1 1 
ATOM   6206  C  CG2 . ILE   B 2 489 ? 9.267   76.211  -13.294 1.00 88.24  ? 793  ILE   B CG2 1 
ATOM   6207  C  CD1 . ILE   B 2 489 ? 10.059  74.076  -15.331 1.00 83.60  ? 793  ILE   B CD1 1 
ATOM   6208  N  N   . ILE   B 2 490 ? 10.993  74.246  -10.630 1.00 87.06  ? 794  ILE   B N   1 
ATOM   6209  C  CA  . ILE   B 2 490 ? 11.290  74.525  -9.226  1.00 87.40  ? 794  ILE   B CA  1 
ATOM   6210  C  C   . ILE   B 2 490 ? 12.010  75.857  -9.118  1.00 93.22  ? 794  ILE   B C   1 
ATOM   6211  O  O   . ILE   B 2 490 ? 12.969  76.114  -9.862  1.00 92.31  ? 794  ILE   B O   1 
ATOM   6212  C  CB  . ILE   B 2 490 ? 12.157  73.425  -8.600  1.00 86.01  ? 794  ILE   B CB  1 
ATOM   6213  C  CG1 . ILE   B 2 490 ? 11.568  72.049  -8.908  1.00 85.86  ? 794  ILE   B CG1 1 
ATOM   6214  C  CG2 . ILE   B 2 490 ? 12.323  73.682  -7.104  1.00 90.19  ? 794  ILE   B CG2 1 
ATOM   6215  C  CD1 . ILE   B 2 490 ? 12.630  71.050  -9.260  1.00 85.24  ? 794  ILE   B CD1 1 
ATOM   6216  N  N   . ASP   B 2 491 ? 11.581  76.682  -8.162  1.00 92.59  ? 795  ASP   B N   1 
ATOM   6217  C  CA  . ASP   B 2 491 ? 12.187  77.991  -7.988  1.00 90.90  ? 795  ASP   B CA  1 
ATOM   6218  C  C   . ASP   B 2 491 ? 13.602  77.863  -7.450  1.00 91.04  ? 795  ASP   B C   1 
ATOM   6219  O  O   . ASP   B 2 491 ? 13.872  77.061  -6.551  1.00 90.06  ? 795  ASP   B O   1 
ATOM   6220  C  CB  . ASP   B 2 491 ? 11.371  78.855  -7.041  1.00 94.25  ? 795  ASP   B CB  1 
ATOM   6221  C  CG  . ASP   B 2 491 ? 12.085  80.164  -6.714  1.00 98.25  ? 795  ASP   B CG  1 
ATOM   6222  O  OD1 . ASP   B 2 491 ? 12.270  80.980  -7.659  1.00 98.77  ? 795  ASP   B OD1 1 
ATOM   6223  O  OD2 . ASP   B 2 491 ? 12.480  80.370  -5.533  1.00 93.79  ? 795  ASP   B OD2 1 
ATOM   6224  N  N   . GLN   B 2 492 ? 14.504  78.687  -7.985  1.00 94.51  ? 796  GLN   B N   1 
ATOM   6225  C  CA  . GLN   B 2 492 ? 15.906  78.566  -7.615  1.00 95.92  ? 796  GLN   B CA  1 
ATOM   6226  C  C   . GLN   B 2 492 ? 16.219  79.128  -6.239  1.00 91.32  ? 796  GLN   B C   1 
ATOM   6227  O  O   . GLN   B 2 492 ? 17.308  78.863  -5.720  1.00 90.36  ? 796  GLN   B O   1 
ATOM   6228  C  CB  . GLN   B 2 492 ? 16.781  79.245  -8.656  1.00 95.10  ? 796  GLN   B CB  1 
ATOM   6229  C  CG  . GLN   B 2 492 ? 16.742  80.720  -8.592  1.00 91.40  ? 796  GLN   B CG  1 
ATOM   6230  C  CD  . GLN   B 2 492 ? 17.846  81.322  -9.414  1.00 97.52  ? 796  GLN   B CD  1 
ATOM   6231  O  OE1 . GLN   B 2 492 ? 18.216  80.796  -10.462 1.00 99.27  ? 796  GLN   B OE1 1 
ATOM   6232  N  NE2 . GLN   B 2 492 ? 18.401  82.421  -8.934  1.00 104.42 ? 796  GLN   B NE2 1 
ATOM   6233  N  N   . HIS   B 2 493 ? 15.301  79.872  -5.630  1.00 90.03  ? 797  HIS   B N   1 
ATOM   6234  C  CA  . HIS   B 2 493 ? 15.538  80.424  -4.307  1.00 95.71  ? 797  HIS   B CA  1 
ATOM   6235  C  C   . HIS   B 2 493 ? 14.769  79.679  -3.225  1.00 95.00  ? 797  HIS   B C   1 
ATOM   6236  O  O   . HIS   B 2 493 ? 15.378  79.235  -2.255  1.00 96.47  ? 797  HIS   B O   1 
ATOM   6237  C  CB  . HIS   B 2 493 ? 15.198  81.924  -4.287  1.00 95.95  ? 797  HIS   B CB  1 
ATOM   6238  C  CG  . HIS   B 2 493 ? 15.862  82.713  -5.371  1.00 96.05  ? 797  HIS   B CG  1 
ATOM   6239  N  ND1 . HIS   B 2 493 ? 15.177  83.182  -6.472  1.00 97.66  ? 797  HIS   B ND1 1 
ATOM   6240  C  CD2 . HIS   B 2 493 ? 17.140  83.137  -5.512  1.00 94.90  ? 797  HIS   B CD2 1 
ATOM   6241  C  CE1 . HIS   B 2 493 ? 16.007  83.850  -7.252  1.00 98.72  ? 797  HIS   B CE1 1 
ATOM   6242  N  NE2 . HIS   B 2 493 ? 17.203  83.841  -6.690  1.00 100.61 ? 797  HIS   B NE2 1 
ATOM   6243  N  N   . THR   B 2 494 ? 13.444  79.545  -3.355  1.00 93.30  ? 798  THR   B N   1 
ATOM   6244  C  CA  . THR   B 2 494 ? 12.655  78.796  -2.379  1.00 93.10  ? 798  THR   B CA  1 
ATOM   6245  C  C   . THR   B 2 494 ? 12.725  77.303  -2.601  1.00 97.32  ? 798  THR   B C   1 
ATOM   6246  O  O   . THR   B 2 494 ? 12.359  76.533  -1.703  1.00 102.13 ? 798  THR   B O   1 
ATOM   6247  C  CB  . THR   B 2 494 ? 11.171  79.183  -2.407  1.00 94.76  ? 798  THR   B CB  1 
ATOM   6248  O  OG1 . THR   B 2 494 ? 10.737  79.398  -3.758  1.00 92.65  ? 798  THR   B OG1 1 
ATOM   6249  C  CG2 . THR   B 2 494 ? 10.920  80.411  -1.559  1.00 100.10 ? 798  THR   B CG2 1 
ATOM   6250  N  N   . PHE   B 2 495 ? 13.184  76.885  -3.773  1.00 96.63  ? 799  PHE   B N   1 
ATOM   6251  C  CA  . PHE   B 2 495 ? 13.166  75.484  -4.136  1.00 94.01  ? 799  PHE   B CA  1 
ATOM   6252  C  C   . PHE   B 2 495 ? 11.770  74.928  -3.939  1.00 96.78  ? 799  PHE   B C   1 
ATOM   6253  O  O   . PHE   B 2 495 ? 11.572  73.836  -3.405  1.00 99.34  ? 799  PHE   B O   1 
ATOM   6254  C  CB  . PHE   B 2 495 ? 14.207  74.705  -3.350  1.00 85.95  ? 799  PHE   B CB  1 
ATOM   6255  C  CG  . PHE   B 2 495 ? 15.547  74.810  -3.945  1.00 86.39  ? 799  PHE   B CG  1 
ATOM   6256  C  CD1 . PHE   B 2 495 ? 15.790  74.253  -5.193  1.00 93.10  ? 799  PHE   B CD1 1 
ATOM   6257  C  CD2 . PHE   B 2 495 ? 16.550  75.506  -3.313  1.00 85.74  ? 799  PHE   B CD2 1 
ATOM   6258  C  CE1 . PHE   B 2 495 ? 17.040  74.356  -5.793  1.00 94.22  ? 799  PHE   B CE1 1 
ATOM   6259  C  CE2 . PHE   B 2 495 ? 17.799  75.611  -3.884  1.00 90.71  ? 799  PHE   B CE2 1 
ATOM   6260  C  CZ  . PHE   B 2 495 ? 18.048  75.036  -5.134  1.00 94.77  ? 799  PHE   B CZ  1 
ATOM   6261  N  N   . GLU   B 2 496 ? 10.788  75.711  -4.358  1.00 99.89  ? 800  GLU   B N   1 
ATOM   6262  C  CA  . GLU   B 2 496 ? 9.406   75.283  -4.307  1.00 100.56 ? 800  GLU   B CA  1 
ATOM   6263  C  C   . GLU   B 2 496 ? 8.971   74.792  -5.685  1.00 100.82 ? 800  GLU   B C   1 
ATOM   6264  O  O   . GLU   B 2 496 ? 9.546   75.172  -6.716  1.00 101.41 ? 800  GLU   B O   1 
ATOM   6265  C  CB  . GLU   B 2 496 ? 8.521   76.424  -3.814  1.00 104.29 ? 800  GLU   B CB  1 
ATOM   6266  C  CG  . GLU   B 2 496 ? 7.088   76.026  -3.566  1.00 113.07 ? 800  GLU   B CG  1 
ATOM   6267  C  CD  . GLU   B 2 496 ? 6.254   77.169  -3.001  1.00 119.39 ? 800  GLU   B CD  1 
ATOM   6268  O  OE1 . GLU   B 2 496 ? 5.171   76.869  -2.451  1.00 124.27 ? 800  GLU   B OE1 1 
ATOM   6269  O  OE2 . GLU   B 2 496 ? 6.671   78.354  -3.106  1.00 116.93 ? 800  GLU   B OE2 1 
ATOM   6270  N  N   . VAL   B 2 497 ? 7.972   73.912  -5.700  1.00 94.96  ? 801  VAL   B N   1 
ATOM   6271  C  CA  . VAL   B 2 497 ? 7.503   73.340  -6.954  1.00 94.79  ? 801  VAL   B CA  1 
ATOM   6272  C  C   . VAL   B 2 497 ? 6.433   74.278  -7.501  1.00 94.32  ? 801  VAL   B C   1 
ATOM   6273  O  O   . VAL   B 2 497 ? 5.295   74.309  -7.012  1.00 90.74  ? 801  VAL   B O   1 
ATOM   6274  C  CB  . VAL   B 2 497 ? 6.998   71.909  -6.785  1.00 95.18  ? 801  VAL   B CB  1 
ATOM   6275  C  CG1 . VAL   B 2 497 ? 6.963   71.236  -8.129  1.00 95.54  ? 801  VAL   B CG1 1 
ATOM   6276  C  CG2 . VAL   B 2 497 ? 7.927   71.134  -5.891  1.00 94.74  ? 801  VAL   B CG2 1 
ATOM   6277  N  N   . LEU   B 2 498 ? 6.821   75.054  -8.521  1.00 94.25  ? 802  LEU   B N   1 
ATOM   6278  C  CA  . LEU   B 2 498 ? 5.981   76.118  -9.060  1.00 90.33  ? 802  LEU   B CA  1 
ATOM   6279  C  C   . LEU   B 2 498 ? 4.962   75.569  -10.040 1.00 94.29  ? 802  LEU   B C   1 
ATOM   6280  O  O   . LEU   B 2 498 ? 3.754   75.772  -9.876  1.00 96.64  ? 802  LEU   B O   1 
ATOM   6281  C  CB  . LEU   B 2 498 ? 6.846   77.175  -9.745  1.00 89.62  ? 802  LEU   B CB  1 
ATOM   6282  C  CG  . LEU   B 2 498 ? 7.949   77.839  -8.919  1.00 89.89  ? 802  LEU   B CG  1 
ATOM   6283  C  CD1 . LEU   B 2 498 ? 8.450   79.056  -9.651  1.00 90.86  ? 802  LEU   B CD1 1 
ATOM   6284  C  CD2 . LEU   B 2 498 ? 7.507   78.175  -7.489  1.00 86.21  ? 802  LEU   B CD2 1 
ATOM   6285  N  N   . HIS   B 2 499 ? 5.437   74.883  -11.077 1.00 93.29  ? 803  HIS   B N   1 
ATOM   6286  C  CA  . HIS   B 2 499 ? 4.570   74.241  -12.047 1.00 94.25  ? 803  HIS   B CA  1 
ATOM   6287  C  C   . HIS   B 2 499 ? 4.918   72.766  -12.140 1.00 94.24  ? 803  HIS   B C   1 
ATOM   6288  O  O   . HIS   B 2 499 ? 6.075   72.366  -11.963 1.00 91.98  ? 803  HIS   B O   1 
ATOM   6289  C  CB  . HIS   B 2 499 ? 4.684   74.883  -13.436 1.00 98.17  ? 803  HIS   B CB  1 
ATOM   6290  C  CG  . HIS   B 2 499 ? 3.612   74.447  -14.393 1.00 100.30 ? 803  HIS   B CG  1 
ATOM   6291  N  ND1 . HIS   B 2 499 ? 2.265   74.512  -14.089 1.00 99.90  ? 803  HIS   B ND1 1 
ATOM   6292  C  CD2 . HIS   B 2 499 ? 3.690   73.937  -15.647 1.00 98.98  ? 803  HIS   B CD2 1 
ATOM   6293  C  CE1 . HIS   B 2 499 ? 1.564   74.058  -15.114 1.00 99.44  ? 803  HIS   B CE1 1 
ATOM   6294  N  NE2 . HIS   B 2 499 ? 2.404   73.706  -16.074 1.00 96.95  ? 803  HIS   B NE2 1 
ATOM   6295  N  N   . ALA   B 2 500 ? 3.900   71.958  -12.431 1.00 94.09  ? 804  ALA   B N   1 
ATOM   6296  C  CA  . ALA   B 2 500 ? 4.091   70.530  -12.662 1.00 91.73  ? 804  ALA   B CA  1 
ATOM   6297  C  C   . ALA   B 2 500 ? 3.275   70.158  -13.882 1.00 88.38  ? 804  ALA   B C   1 
ATOM   6298  O  O   . ALA   B 2 500 ? 2.047   70.072  -13.808 1.00 87.74  ? 804  ALA   B O   1 
ATOM   6299  C  CB  . ALA   B 2 500 ? 3.680   69.682  -11.455 1.00 92.36  ? 804  ALA   B CB  1 
ATOM   6300  N  N   . HIS   B 2 501 ? 3.961   69.920  -14.985 1.00 87.28  ? 805  HIS   B N   1 
ATOM   6301  C  CA  . HIS   B 2 501 ? 3.319   69.518  -16.224 1.00 87.27  ? 805  HIS   B CA  1 
ATOM   6302  C  C   . HIS   B 2 501 ? 3.334   67.999  -16.335 1.00 89.29  ? 805  HIS   B C   1 
ATOM   6303  O  O   . HIS   B 2 501 ? 4.404   67.379  -16.294 1.00 88.40  ? 805  HIS   B O   1 
ATOM   6304  C  CB  . HIS   B 2 501 ? 4.036   70.155  -17.405 1.00 87.10  ? 805  HIS   B CB  1 
ATOM   6305  C  CG  . HIS   B 2 501 ? 3.483   69.746  -18.727 1.00 88.91  ? 805  HIS   B CG  1 
ATOM   6306  N  ND1 . HIS   B 2 501 ? 2.128   69.661  -18.971 1.00 87.73  ? 805  HIS   B ND1 1 
ATOM   6307  C  CD2 . HIS   B 2 501 ? 4.103   69.387  -19.876 1.00 86.95  ? 805  HIS   B CD2 1 
ATOM   6308  C  CE1 . HIS   B 2 501 ? 1.939   69.263  -20.217 1.00 89.49  ? 805  HIS   B CE1 1 
ATOM   6309  N  NE2 . HIS   B 2 501 ? 3.120   69.093  -20.788 1.00 90.00  ? 805  HIS   B NE2 1 
ATOM   6310  N  N   . GLN   B 2 502 ? 2.157   67.397  -16.475 1.00 88.01  ? 806  GLN   B N   1 
ATOM   6311  C  CA  . GLN   B 2 502 ? 2.071   65.953  -16.622 1.00 85.94  ? 806  GLN   B CA  1 
ATOM   6312  C  C   . GLN   B 2 502 ? 2.036   65.584  -18.095 1.00 84.30  ? 806  GLN   B C   1 
ATOM   6313  O  O   . GLN   B 2 502 ? 1.189   66.078  -18.841 1.00 89.07  ? 806  GLN   B O   1 
ATOM   6314  C  CB  . GLN   B 2 502 ? 0.836   65.413  -15.912 1.00 91.59  ? 806  GLN   B CB  1 
ATOM   6315  C  CG  . GLN   B 2 502 ? 0.541   63.950  -16.192 1.00 84.34  ? 806  GLN   B CG  1 
ATOM   6316  C  CD  . GLN   B 2 502 ? -0.655  63.468  -15.410 1.00 83.11  ? 806  GLN   B CD  1 
ATOM   6317  O  OE1 . GLN   B 2 502 ? -0.686  63.567  -14.187 1.00 84.86  ? 806  GLN   B OE1 1 
ATOM   6318  N  NE2 . GLN   B 2 502 ? -1.660  62.964  -16.113 1.00 90.51  ? 806  GLN   B NE2 1 
ATOM   6319  N  N   . PHE   B 2 503 ? 2.952   64.714  -18.511 1.00 84.43  ? 807  PHE   B N   1 
ATOM   6320  C  CA  . PHE   B 2 503 ? 3.037   64.325  -19.911 1.00 86.43  ? 807  PHE   B CA  1 
ATOM   6321  C  C   . PHE   B 2 503 ? 1.911   63.359  -20.291 1.00 90.91  ? 807  PHE   B C   1 
ATOM   6322  O  O   . PHE   B 2 503 ? 1.063   62.972  -19.473 1.00 92.91  ? 807  PHE   B O   1 
ATOM   6323  C  CB  . PHE   B 2 503 ? 4.397   63.706  -20.208 1.00 80.52  ? 807  PHE   B CB  1 
ATOM   6324  C  CG  . PHE   B 2 503 ? 5.507   64.706  -20.301 1.00 84.29  ? 807  PHE   B CG  1 
ATOM   6325  C  CD1 . PHE   B 2 503 ? 5.724   65.413  -21.478 1.00 82.82  ? 807  PHE   B CD1 1 
ATOM   6326  C  CD2 . PHE   B 2 503 ? 6.348   64.935  -19.219 1.00 82.62  ? 807  PHE   B CD2 1 
ATOM   6327  C  CE1 . PHE   B 2 503 ? 6.757   66.346  -21.575 1.00 82.78  ? 807  PHE   B CE1 1 
ATOM   6328  C  CE2 . PHE   B 2 503 ? 7.389   65.869  -19.304 1.00 85.55  ? 807  PHE   B CE2 1 
ATOM   6329  C  CZ  . PHE   B 2 503 ? 7.593   66.577  -20.485 1.00 85.47  ? 807  PHE   B CZ  1 
ATOM   6330  N  N   . LEU   B 2 504 ? 1.915   62.967  -21.563 1.00 89.87  ? 808  LEU   B N   1 
ATOM   6331  C  CA  . LEU   B 2 504 ? 0.897   62.073  -22.101 1.00 94.79  ? 808  LEU   B CA  1 
ATOM   6332  C  C   . LEU   B 2 504 ? 0.906   60.714  -21.406 1.00 89.98  ? 808  LEU   B C   1 
ATOM   6333  O  O   . LEU   B 2 504 ? 1.933   60.243  -20.920 1.00 93.01  ? 808  LEU   B O   1 
ATOM   6334  C  CB  . LEU   B 2 504 ? 1.124   61.875  -23.602 1.00 98.47  ? 808  LEU   B CB  1 
ATOM   6335  C  CG  . LEU   B 2 504 ? 0.268   62.730  -24.548 1.00 100.76 ? 808  LEU   B CG  1 
ATOM   6336  C  CD1 . LEU   B 2 504 ? 0.266   64.208  -24.170 1.00 102.71 ? 808  LEU   B CD1 1 
ATOM   6337  C  CD2 . LEU   B 2 504 ? 0.744   62.554  -25.971 1.00 99.21  ? 808  LEU   B CD2 1 
ATOM   6338  N  N   . GLN   B 2 505 ? -0.253  60.068  -21.385 1.00 90.07  ? 809  GLN   B N   1 
ATOM   6339  C  CA  . GLN   B 2 505 ? -0.342  58.731  -20.821 1.00 93.34  ? 809  GLN   B CA  1 
ATOM   6340  C  C   . GLN   B 2 505 ? 0.383   57.730  -21.708 1.00 94.68  ? 809  GLN   B C   1 
ATOM   6341  O  O   . GLN   B 2 505 ? 0.159   57.681  -22.924 1.00 97.12  ? 809  GLN   B O   1 
ATOM   6342  C  CB  . GLN   B 2 505 ? -1.798  58.316  -20.652 1.00 100.17 ? 809  GLN   B CB  1 
ATOM   6343  C  CG  . GLN   B 2 505 ? -1.967  56.805  -20.633 1.00 105.62 ? 809  GLN   B CG  1 
ATOM   6344  C  CD  . GLN   B 2 505 ? -3.215  56.365  -19.892 1.00 109.37 ? 809  GLN   B CD  1 
ATOM   6345  O  OE1 . GLN   B 2 505 ? -3.707  57.071  -19.008 1.00 113.81 ? 809  GLN   B OE1 1 
ATOM   6346  N  NE2 . GLN   B 2 505 ? -3.737  55.196  -20.251 1.00 111.57 ? 809  GLN   B NE2 1 
ATOM   6347  N  N   . ASN   B 2 506 ? 1.241   56.916  -21.096 1.00 89.96  ? 810  ASN   B N   1 
ATOM   6348  C  CA  . ASN   B 2 506 ? 2.095   55.998  -21.835 1.00 91.60  ? 810  ASN   B CA  1 
ATOM   6349  C  C   . ASN   B 2 506 ? 3.260   56.709  -22.513 1.00 90.50  ? 810  ASN   B C   1 
ATOM   6350  O  O   . ASN   B 2 506 ? 3.814   56.188  -23.492 1.00 89.45  ? 810  ASN   B O   1 
ATOM   6351  C  CB  . ASN   B 2 506 ? 1.282   55.213  -22.876 1.00 98.09  ? 810  ASN   B CB  1 
ATOM   6352  C  CG  . ASN   B 2 506 ? 0.764   53.894  -22.343 1.00 97.20  ? 810  ASN   B CG  1 
ATOM   6353  O  OD1 . ASN   B 2 506 ? -0.094  53.853  -21.453 1.00 95.62  ? 810  ASN   B OD1 1 
ATOM   6354  N  ND2 . ASN   B 2 506 ? 1.285   52.802  -22.888 1.00 98.77  ? 810  ASN   B ND2 1 
ATOM   6355  N  N   . GLU   B 2 507 ? 3.643   57.889  -22.015 1.00 91.84  ? 811  GLU   B N   1 
ATOM   6356  C  CA  . GLU   B 2 507 ? 4.757   58.657  -22.557 1.00 84.94  ? 811  GLU   B CA  1 
ATOM   6357  C  C   . GLU   B 2 507 ? 5.872   58.799  -21.521 1.00 84.24  ? 811  GLU   B C   1 
ATOM   6358  O  O   . GLU   B 2 507 ? 5.624   59.206  -20.376 1.00 80.18  ? 811  GLU   B O   1 
ATOM   6359  C  CB  . GLU   B 2 507 ? 4.278   60.019  -23.035 1.00 84.27  ? 811  GLU   B CB  1 
ATOM   6360  C  CG  . GLU   B 2 507 ? 5.301   60.735  -23.861 1.00 88.61  ? 811  GLU   B CG  1 
ATOM   6361  C  CD  . GLU   B 2 507 ? 4.932   62.187  -24.124 1.00 91.74  ? 811  GLU   B CD  1 
ATOM   6362  O  OE1 . GLU   B 2 507 ? 4.270   62.828  -23.270 1.00 91.74  ? 811  GLU   B OE1 1 
ATOM   6363  O  OE2 . GLU   B 2 507 ? 5.313   62.683  -25.200 1.00 91.20  ? 811  GLU   B OE2 1 
ATOM   6364  N  N   . TYR   B 2 508 ? 7.098   58.443  -21.936 1.00 86.14  ? 812  TYR   B N   1 
ATOM   6365  C  CA  . TYR   B 2 508 ? 8.270   58.313  -21.074 1.00 85.97  ? 812  TYR   B CA  1 
ATOM   6366  C  C   . TYR   B 2 508 ? 9.276   59.393  -21.463 1.00 84.98  ? 812  TYR   B C   1 
ATOM   6367  O  O   . TYR   B 2 508 ? 9.892   59.322  -22.534 1.00 84.28  ? 812  TYR   B O   1 
ATOM   6368  C  CB  . TYR   B 2 508 ? 8.888   56.919  -21.202 1.00 88.54  ? 812  TYR   B CB  1 
ATOM   6369  C  CG  . TYR   B 2 508 ? 9.891   56.598  -20.111 1.00 89.35  ? 812  TYR   B CG  1 
ATOM   6370  C  CD1 . TYR   B 2 508 ? 11.165  57.158  -20.137 1.00 89.67  ? 812  TYR   B CD1 1 
ATOM   6371  C  CD2 . TYR   B 2 508 ? 9.567   55.744  -19.045 1.00 89.63  ? 812  TYR   B CD2 1 
ATOM   6372  C  CE1 . TYR   B 2 508 ? 12.097  56.892  -19.129 1.00 91.75  ? 812  TYR   B CE1 1 
ATOM   6373  C  CE2 . TYR   B 2 508 ? 10.501  55.470  -18.027 1.00 91.09  ? 812  TYR   B CE2 1 
ATOM   6374  C  CZ  . TYR   B 2 508 ? 11.765  56.056  -18.082 1.00 91.18  ? 812  TYR   B CZ  1 
ATOM   6375  O  OH  . TYR   B 2 508 ? 12.711  55.821  -17.105 1.00 96.25  ? 812  TYR   B OH  1 
ATOM   6376  N  N   . ALA   B 2 509 ? 9.447   60.386  -20.597 1.00 81.07  ? 813  ALA   B N   1 
ATOM   6377  C  CA  . ALA   B 2 509 ? 10.312  61.505  -20.916 1.00 78.26  ? 813  ALA   B CA  1 
ATOM   6378  C  C   . ALA   B 2 509 ? 11.763  61.108  -20.736 1.00 77.59  ? 813  ALA   B C   1 
ATOM   6379  O  O   . ALA   B 2 509 ? 12.112  60.428  -19.776 1.00 85.78  ? 813  ALA   B O   1 
ATOM   6380  C  CB  . ALA   B 2 509 ? 9.977   62.699  -20.032 1.00 79.94  ? 813  ALA   B CB  1 
ATOM   6381  N  N   . LEU   B 2 510 ? 12.610  61.528  -21.665 1.00 76.06  ? 814  LEU   B N   1 
ATOM   6382  C  CA  . LEU   B 2 510 ? 14.000  61.102  -21.652 1.00 75.83  ? 814  LEU   B CA  1 
ATOM   6383  C  C   . LEU   B 2 510 ? 14.972  62.268  -21.619 1.00 82.48  ? 814  LEU   B C   1 
ATOM   6384  O  O   . LEU   B 2 510 ? 15.843  62.309  -20.742 1.00 87.13  ? 814  LEU   B O   1 
ATOM   6385  C  CB  . LEU   B 2 510 ? 14.283  60.199  -22.868 1.00 79.34  ? 814  LEU   B CB  1 
ATOM   6386  C  CG  . LEU   B 2 510 ? 13.425  58.922  -23.005 1.00 84.97  ? 814  LEU   B CG  1 
ATOM   6387  C  CD1 . LEU   B 2 510 ? 13.558  58.258  -24.386 1.00 80.63  ? 814  LEU   B CD1 1 
ATOM   6388  C  CD2 . LEU   B 2 510 ? 13.747  57.894  -21.906 1.00 81.14  ? 814  LEU   B CD2 1 
ATOM   6389  N  N   . SER   B 2 511 ? 14.843  63.229  -22.529 1.00 81.07  ? 815  SER   B N   1 
ATOM   6390  C  CA  . SER   B 2 511 ? 15.770  64.343  -22.604 1.00 79.47  ? 815  SER   B CA  1 
ATOM   6391  C  C   . SER   B 2 511 ? 15.173  65.621  -22.033 1.00 85.73  ? 815  SER   B C   1 
ATOM   6392  O  O   . SER   B 2 511 ? 13.977  65.896  -22.184 1.00 84.75  ? 815  SER   B O   1 
ATOM   6393  C  CB  . SER   B 2 511 ? 16.178  64.619  -24.038 1.00 89.37  ? 815  SER   B CB  1 
ATOM   6394  O  OG  . SER   B 2 511 ? 16.013  63.484  -24.846 1.00 83.58  ? 815  SER   B OG  1 
ATOM   6395  N  N   . LEU   B 2 512 ? 16.043  66.446  -21.450 1.00 83.78  ? 816  LEU   B N   1 
ATOM   6396  C  CA  . LEU   B 2 512 ? 15.645  67.791  -21.058 1.00 85.69  ? 816  LEU   B CA  1 
ATOM   6397  C  C   . LEU   B 2 512 ? 16.726  68.797  -21.431 1.00 85.37  ? 816  LEU   B C   1 
ATOM   6398  O  O   . LEU   B 2 512 ? 17.918  68.506  -21.324 1.00 89.25  ? 816  LEU   B O   1 
ATOM   6399  C  CB  . LEU   B 2 512 ? 15.343  67.832  -19.565 1.00 82.11  ? 816  LEU   B CB  1 
ATOM   6400  C  CG  . LEU   B 2 512 ? 14.749  69.133  -19.063 1.00 82.96  ? 816  LEU   B CG  1 
ATOM   6401  C  CD1 . LEU   B 2 512 ? 13.378  69.304  -19.670 1.00 82.53  ? 816  LEU   B CD1 1 
ATOM   6402  C  CD2 . LEU   B 2 512 ? 14.676  69.130  -17.548 1.00 82.49  ? 816  LEU   B CD2 1 
ATOM   6403  N  N   . VAL   B 2 513 ? 16.307  69.974  -21.896 1.00 89.92  ? 817  VAL   B N   1 
ATOM   6404  C  CA  . VAL   B 2 513 ? 17.236  71.029  -22.311 1.00 91.71  ? 817  VAL   B CA  1 
ATOM   6405  C  C   . VAL   B 2 513 ? 16.594  72.381  -22.055 1.00 87.04  ? 817  VAL   B C   1 
ATOM   6406  O  O   . VAL   B 2 513 ? 15.383  72.549  -22.227 1.00 86.85  ? 817  VAL   B O   1 
ATOM   6407  C  CB  . VAL   B 2 513 ? 17.640  70.919  -23.799 1.00 89.60  ? 817  VAL   B CB  1 
ATOM   6408  C  CG1 . VAL   B 2 513 ? 18.565  72.066  -24.164 1.00 90.32  ? 817  VAL   B CG1 1 
ATOM   6409  C  CG2 . VAL   B 2 513 ? 18.317  69.579  -24.089 1.00 92.04  ? 817  VAL   B CG2 1 
ATOM   6410  N  N   . SER   B 2 514 ? 17.417  73.344  -21.629 1.00 91.16  ? 818  SER   B N   1 
ATOM   6411  C  CA  . SER   B 2 514 ? 17.025  74.748  -21.504 1.00 93.49  ? 818  SER   B CA  1 
ATOM   6412  C  C   . SER   B 2 514 ? 17.949  75.534  -22.420 1.00 92.47  ? 818  SER   B C   1 
ATOM   6413  O  O   . SER   B 2 514 ? 19.125  75.703  -22.097 1.00 99.17  ? 818  SER   B O   1 
ATOM   6414  C  CB  . SER   B 2 514 ? 17.114  75.242  -20.056 1.00 93.62  ? 818  SER   B CB  1 
ATOM   6415  O  OG  . SER   B 2 514 ? 16.849  76.647  -19.956 1.00 99.16  ? 818  SER   B OG  1 
ATOM   6416  N  N   . CYS   B 2 515 ? 17.441  76.000  -23.561 1.00 95.46  ? 819  CYS   B N   1 
ATOM   6417  C  CA  . CYS   B 2 515 ? 18.261  76.805  -24.463 1.00 103.30 ? 819  CYS   B CA  1 
ATOM   6418  C  C   . CYS   B 2 515 ? 17.388  77.829  -25.182 1.00 104.64 ? 819  CYS   B C   1 
ATOM   6419  O  O   . CYS   B 2 515 ? 16.186  77.621  -25.355 1.00 103.14 ? 819  CYS   B O   1 
ATOM   6420  C  CB  . CYS   B 2 515 ? 19.002  75.927  -25.475 1.00 99.11  ? 819  CYS   B CB  1 
ATOM   6421  S  SG  . CYS   B 2 515 ? 17.876  75.122  -26.612 1.00 103.54 ? 819  CYS   B SG  1 
ATOM   6422  N  N   . LYS   B 2 516 ? 17.996  78.952  -25.573 1.00 109.52 ? 820  LYS   B N   1 
ATOM   6423  C  CA  . LYS   B 2 516 ? 17.416  79.814  -26.604 1.00 111.36 ? 820  LYS   B CA  1 
ATOM   6424  C  C   . LYS   B 2 516 ? 17.791  79.230  -27.961 1.00 103.79 ? 820  LYS   B C   1 
ATOM   6425  O  O   . LYS   B 2 516 ? 18.897  78.702  -28.136 1.00 101.89 ? 820  LYS   B O   1 
ATOM   6426  C  CB  . LYS   B 2 516 ? 17.900  81.269  -26.471 1.00 99.34  ? 820  LYS   B CB  1 
ATOM   6427  N  N   . LEU   B 2 517 ? 16.859  79.277  -28.896 1.00 101.19 ? 821  LEU   B N   1 
ATOM   6428  C  CA  . LEU   B 2 517 ? 17.080  78.708  -30.211 1.00 105.94 ? 821  LEU   B CA  1 
ATOM   6429  C  C   . LEU   B 2 517 ? 16.802  79.772  -31.264 1.00 109.82 ? 821  LEU   B C   1 
ATOM   6430  O  O   . LEU   B 2 517 ? 15.961  80.658  -31.065 1.00 112.21 ? 821  LEU   B O   1 
ATOM   6431  C  CB  . LEU   B 2 517 ? 16.201  77.483  -30.463 1.00 101.17 ? 821  LEU   B CB  1 
ATOM   6432  C  CG  . LEU   B 2 517 ? 16.864  76.179  -30.057 1.00 101.86 ? 821  LEU   B CG  1 
ATOM   6433  C  CD1 . LEU   B 2 517 ? 16.200  75.008  -30.739 1.00 104.52 ? 821  LEU   B CD1 1 
ATOM   6434  C  CD2 . LEU   B 2 517 ? 18.326  76.239  -30.421 1.00 105.48 ? 821  LEU   B CD2 1 
ATOM   6435  N  N   . GLY   B 2 518 ? 17.524  79.688  -32.386 1.00 108.00 ? 822  GLY   B N   1 
ATOM   6436  C  CA  . GLY   B 2 518 ? 17.386  80.599  -33.519 1.00 108.98 ? 822  GLY   B CA  1 
ATOM   6437  C  C   . GLY   B 2 518 ? 17.449  82.077  -33.103 1.00 115.80 ? 822  GLY   B C   1 
ATOM   6438  O  O   . GLY   B 2 518 ? 17.909  82.465  -32.024 1.00 115.31 ? 822  GLY   B O   1 
ATOM   6439  N  N   . LYS   B 2 519 ? 16.973  82.924  -34.016 1.00 119.07 ? 823  LYS   B N   1 
ATOM   6440  C  CA  . LYS   B 2 519 ? 16.913  84.333  -33.662 1.00 118.54 ? 823  LYS   B CA  1 
ATOM   6441  C  C   . LYS   B 2 519 ? 15.823  84.625  -32.626 1.00 121.13 ? 823  LYS   B C   1 
ATOM   6442  O  O   . LYS   B 2 519 ? 15.639  85.794  -32.264 1.00 124.16 ? 823  LYS   B O   1 
ATOM   6443  C  CB  . LYS   B 2 519 ? 16.699  85.188  -34.927 1.00 115.27 ? 823  LYS   B CB  1 
ATOM   6444  N  N   . ASP   B 2 520 ? 15.132  83.605  -32.119 1.00 114.16 ? 824  ASP   B N   1 
ATOM   6445  C  CA  . ASP   B 2 520 ? 14.151  83.801  -31.058 1.00 110.86 ? 824  ASP   B CA  1 
ATOM   6446  C  C   . ASP   B 2 520 ? 14.849  84.278  -29.782 1.00 111.42 ? 824  ASP   B C   1 
ATOM   6447  O  O   . ASP   B 2 520 ? 15.929  83.773  -29.453 1.00 109.77 ? 824  ASP   B O   1 
ATOM   6448  C  CB  . ASP   B 2 520 ? 13.407  82.489  -30.810 1.00 110.86 ? 824  ASP   B CB  1 
ATOM   6449  C  CG  . ASP   B 2 520 ? 12.038  82.698  -30.217 1.00 112.88 ? 824  ASP   B CG  1 
ATOM   6450  O  OD1 . ASP   B 2 520 ? 11.950  83.371  -29.162 1.00 111.30 ? 824  ASP   B OD1 1 
ATOM   6451  O  OD2 . ASP   B 2 520 ? 11.054  82.199  -30.817 1.00 114.55 ? 824  ASP   B OD2 1 
ATOM   6452  N  N   . PRO   B 2 521 ? 14.274  85.293  -29.043 1.00 113.53 ? 825  PRO   B N   1 
ATOM   6453  C  CA  . PRO   B 2 521 ? 14.896  85.749  -27.783 1.00 113.06 ? 825  PRO   B CA  1 
ATOM   6454  C  C   . PRO   B 2 521 ? 14.419  85.010  -26.535 1.00 114.25 ? 825  PRO   B C   1 
ATOM   6455  O  O   . PRO   B 2 521 ? 15.090  85.051  -25.490 1.00 113.49 ? 825  PRO   B O   1 
ATOM   6456  C  CB  . PRO   B 2 521 ? 14.503  87.225  -27.728 1.00 103.43 ? 825  PRO   B CB  1 
ATOM   6457  C  CG  . PRO   B 2 521 ? 13.149  87.235  -28.352 1.00 104.38 ? 825  PRO   B CG  1 
ATOM   6458  C  CD  . PRO   B 2 521 ? 13.203  86.214  -29.468 1.00 109.41 ? 825  PRO   B CD  1 
ATOM   6459  N  N   . ASN   B 2 522 ? 13.266  84.340  -26.613 1.00 114.10 ? 826  ASN   B N   1 
ATOM   6460  C  CA  . ASN   B 2 522 ? 12.838  83.503  -25.498 1.00 112.16 ? 826  ASN   B CA  1 
ATOM   6461  C  C   . ASN   B 2 522 ? 13.861  82.409  -25.251 1.00 112.42 ? 826  ASN   B C   1 
ATOM   6462  O  O   . ASN   B 2 522 ? 14.429  81.836  -26.189 1.00 110.81 ? 826  ASN   B O   1 
ATOM   6463  C  CB  . ASN   B 2 522 ? 11.477  82.868  -25.780 1.00 107.36 ? 826  ASN   B CB  1 
ATOM   6464  C  CG  . ASN   B 2 522 ? 10.419  83.884  -26.098 1.00 112.72 ? 826  ASN   B CG  1 
ATOM   6465  O  OD1 . ASN   B 2 522 ? 9.974   84.637  -25.220 1.00 117.65 ? 826  ASN   B OD1 1 
ATOM   6466  N  ND2 . ASN   B 2 522 ? 9.992   83.916  -27.358 1.00 113.69 ? 826  ASN   B ND2 1 
ATOM   6467  N  N   . THR   B 2 523 ? 14.087  82.104  -23.989 1.00 111.47 ? 827  THR   B N   1 
ATOM   6468  C  CA  . THR   B 2 523 ? 14.778  80.868  -23.649 1.00 113.78 ? 827  THR   B CA  1 
ATOM   6469  C  C   . THR   B 2 523 ? 13.728  79.812  -23.295 1.00 109.69 ? 827  THR   B C   1 
ATOM   6470  O  O   . THR   B 2 523 ? 12.766  80.096  -22.579 1.00 110.98 ? 827  THR   B O   1 
ATOM   6471  C  CB  . THR   B 2 523 ? 15.764  81.116  -22.510 1.00 111.78 ? 827  THR   B CB  1 
ATOM   6472  O  OG1 . THR   B 2 523 ? 15.069  81.690  -21.399 1.00 112.39 ? 827  THR   B OG1 1 
ATOM   6473  C  CG2 . THR   B 2 523 ? 16.854  82.101  -22.968 1.00 111.75 ? 827  THR   B CG2 1 
ATOM   6474  N  N   . TYR   B 2 524 ? 13.883  78.603  -23.836 1.00 104.86 ? 828  TYR   B N   1 
ATOM   6475  C  CA  . TYR   B 2 524 ? 12.825  77.595  -23.789 1.00 102.59 ? 828  TYR   B CA  1 
ATOM   6476  C  C   . TYR   B 2 524 ? 13.247  76.357  -23.000 1.00 102.79 ? 828  TYR   B C   1 
ATOM   6477  O  O   . TYR   B 2 524 ? 14.432  76.119  -22.753 1.00 103.58 ? 828  TYR   B O   1 
ATOM   6478  C  CB  . TYR   B 2 524 ? 12.422  77.177  -25.205 1.00 103.34 ? 828  TYR   B CB  1 
ATOM   6479  C  CG  . TYR   B 2 524 ? 11.756  78.250  -26.029 1.00 106.86 ? 828  TYR   B CG  1 
ATOM   6480  C  CD1 . TYR   B 2 524 ? 10.733  79.023  -25.499 1.00 108.43 ? 828  TYR   B CD1 1 
ATOM   6481  C  CD2 . TYR   B 2 524 ? 12.143  78.489  -27.349 1.00 110.38 ? 828  TYR   B CD2 1 
ATOM   6482  C  CE1 . TYR   B 2 524 ? 10.110  80.008  -26.253 1.00 111.00 ? 828  TYR   B CE1 1 
ATOM   6483  C  CE2 . TYR   B 2 524 ? 11.525  79.478  -28.115 1.00 110.02 ? 828  TYR   B CE2 1 
ATOM   6484  C  CZ  . TYR   B 2 524 ? 10.511  80.229  -27.556 1.00 111.92 ? 828  TYR   B CZ  1 
ATOM   6485  O  OH  . TYR   B 2 524 ? 9.884   81.207  -28.285 1.00 116.57 ? 828  TYR   B OH  1 
ATOM   6486  N  N   . PHE   B 2 525 ? 12.234  75.547  -22.608 1.00 97.79  ? 829  PHE   B N   1 
ATOM   6487  C  CA  . PHE   B 2 525 ? 12.427  74.186  -22.076 1.00 92.20  ? 829  PHE   B CA  1 
ATOM   6488  C  C   . PHE   B 2 525 ? 12.113  73.191  -23.192 1.00 89.62  ? 829  PHE   B C   1 
ATOM   6489  O  O   . PHE   B 2 525 ? 10.971  73.121  -23.658 1.00 90.12  ? 829  PHE   B O   1 
ATOM   6490  C  CB  . PHE   B 2 525 ? 11.528  73.910  -20.862 1.00 84.16  ? 829  PHE   B CB  1 
ATOM   6491  C  CG  . PHE   B 2 525 ? 12.022  74.503  -19.558 1.00 86.86  ? 829  PHE   B CG  1 
ATOM   6492  C  CD1 . PHE   B 2 525 ? 13.326  74.293  -19.123 1.00 87.04  ? 829  PHE   B CD1 1 
ATOM   6493  C  CD2 . PHE   B 2 525 ? 11.157  75.255  -18.747 1.00 87.51  ? 829  PHE   B CD2 1 
ATOM   6494  C  CE1 . PHE   B 2 525 ? 13.765  74.833  -17.909 1.00 91.07  ? 829  PHE   B CE1 1 
ATOM   6495  C  CE2 . PHE   B 2 525 ? 11.587  75.798  -17.522 1.00 87.09  ? 829  PHE   B CE2 1 
ATOM   6496  C  CZ  . PHE   B 2 525 ? 12.890  75.594  -17.107 1.00 90.79  ? 829  PHE   B CZ  1 
ATOM   6497  N  N   . ILE   B 2 526 ? 13.113  72.429  -23.633 1.00 88.97  ? 830  ILE   B N   1 
ATOM   6498  C  CA  . ILE   B 2 526 ? 12.892  71.392  -24.641 1.00 90.25  ? 830  ILE   B CA  1 
ATOM   6499  C  C   . ILE   B 2 526 ? 12.914  70.037  -23.951 1.00 85.33  ? 830  ILE   B C   1 
ATOM   6500  O  O   . ILE   B 2 526 ? 13.830  69.737  -23.178 1.00 85.44  ? 830  ILE   B O   1 
ATOM   6501  C  CB  . ILE   B 2 526 ? 13.916  71.468  -25.789 1.00 87.18  ? 830  ILE   B CB  1 
ATOM   6502  C  CG1 . ILE   B 2 526 ? 13.918  72.867  -26.418 1.00 91.01  ? 830  ILE   B CG1 1 
ATOM   6503  C  CG2 . ILE   B 2 526 ? 13.528  70.531  -26.903 1.00 84.28  ? 830  ILE   B CG2 1 
ATOM   6504  C  CD1 . ILE   B 2 526 ? 14.830  72.969  -27.637 1.00 77.58  ? 830  ILE   B CD1 1 
ATOM   6505  N  N   . VAL   B 2 527 ? 11.884  69.236  -24.202 1.00 83.83  ? 831  VAL   B N   1 
ATOM   6506  C  CA  . VAL   B 2 527 ? 11.728  67.929  -23.587 1.00 85.89  ? 831  VAL   B CA  1 
ATOM   6507  C  C   . VAL   B 2 527 ? 11.600  66.888  -24.686 1.00 86.97  ? 831  VAL   B C   1 
ATOM   6508  O  O   . VAL   B 2 527 ? 10.693  66.961  -25.528 1.00 85.96  ? 831  VAL   B O   1 
ATOM   6509  C  CB  . VAL   B 2 527 ? 10.510  67.875  -22.664 1.00 83.12  ? 831  VAL   B CB  1 
ATOM   6510  C  CG1 . VAL   B 2 527 ? 10.150  66.443  -22.431 1.00 78.31  ? 831  VAL   B CG1 1 
ATOM   6511  C  CG2 . VAL   B 2 527 ? 10.835  68.554  -21.375 1.00 88.36  ? 831  VAL   B CG2 1 
ATOM   6512  N  N   . GLY   B 2 528 ? 12.502  65.910  -24.674 1.00 86.57  ? 832  GLY   B N   1 
ATOM   6513  C  CA  . GLY   B 2 528 ? 12.434  64.809  -25.622 1.00 90.51  ? 832  GLY   B CA  1 
ATOM   6514  C  C   . GLY   B 2 528 ? 11.853  63.563  -24.978 1.00 83.92  ? 832  GLY   B C   1 
ATOM   6515  O  O   . GLY   B 2 528 ? 12.280  63.154  -23.896 1.00 82.80  ? 832  GLY   B O   1 
ATOM   6516  N  N   . THR   B 2 529 ? 10.887  62.955  -25.653 1.00 80.26  ? 833  THR   B N   1 
ATOM   6517  C  CA  . THR   B 2 529 ? 10.165  61.845  -25.058 1.00 84.30  ? 833  THR   B CA  1 
ATOM   6518  C  C   . THR   B 2 529 ? 10.132  60.634  -26.004 1.00 86.14  ? 833  THR   B C   1 
ATOM   6519  O  O   . THR   B 2 529 ? 10.691  60.644  -27.112 1.00 79.82  ? 833  THR   B O   1 
ATOM   6520  C  CB  . THR   B 2 529 ? 8.761   62.307  -24.667 1.00 83.72  ? 833  THR   B CB  1 
ATOM   6521  O  OG1 . THR   B 2 529 ? 8.025   62.611  -25.855 1.00 83.59  ? 833  THR   B OG1 1 
ATOM   6522  C  CG2 . THR   B 2 529 ? 8.873   63.565  -23.851 1.00 83.35  ? 833  THR   B CG2 1 
ATOM   6523  N  N   . ALA   B 2 530 ? 9.484   59.564  -25.525 1.00 86.44  ? 834  ALA   B N   1 
ATOM   6524  C  CA  . ALA   B 2 530 ? 9.272   58.336  -26.288 1.00 86.16  ? 834  ALA   B CA  1 
ATOM   6525  C  C   . ALA   B 2 530 ? 8.006   57.627  -25.820 1.00 83.98  ? 834  ALA   B C   1 
ATOM   6526  O  O   . ALA   B 2 530 ? 7.765   57.496  -24.620 1.00 86.46  ? 834  ALA   B O   1 
ATOM   6527  C  CB  . ALA   B 2 530 ? 10.459  57.379  -26.161 1.00 83.77  ? 834  ALA   B CB  1 
ATOM   6528  N  N   . MET   B 2 531 ? 7.219   57.138  -26.766 1.00 85.52  ? 835  MET   B N   1 
ATOM   6529  C  CA  . MET   B 2 531 ? 6.009   56.394  -26.446 1.00 90.20  ? 835  MET   B CA  1 
ATOM   6530  C  C   . MET   B 2 531 ? 6.360   54.920  -26.222 1.00 90.40  ? 835  MET   B C   1 
ATOM   6531  O  O   . MET   B 2 531 ? 6.934   54.275  -27.109 1.00 87.76  ? 835  MET   B O   1 
ATOM   6532  C  CB  . MET   B 2 531 ? 4.999   56.580  -27.577 1.00 96.73  ? 835  MET   B CB  1 
ATOM   6533  C  CG  . MET   B 2 531 ? 4.579   58.033  -27.756 1.00 96.34  ? 835  MET   B CG  1 
ATOM   6534  S  SD  . MET   B 2 531 ? 3.767   58.629  -26.255 1.00 91.71  ? 835  MET   B SD  1 
ATOM   6535  C  CE  . MET   B 2 531 ? 2.219   57.723  -26.311 1.00 94.99  ? 835  MET   B CE  1 
ATOM   6536  N  N   . VAL   B 2 532 ? 6.031   54.391  -25.036 1.00 89.29  ? 836  VAL   B N   1 
ATOM   6537  C  CA  . VAL   B 2 532 ? 6.382   53.021  -24.660 1.00 88.93  ? 836  VAL   B CA  1 
ATOM   6538  C  C   . VAL   B 2 532 ? 5.117   52.230  -24.366 1.00 89.94  ? 836  VAL   B C   1 
ATOM   6539  O  O   . VAL   B 2 532 ? 4.219   52.708  -23.664 1.00 92.42  ? 836  VAL   B O   1 
ATOM   6540  C  CB  . VAL   B 2 532 ? 7.321   52.971  -23.442 1.00 92.36  ? 836  VAL   B CB  1 
ATOM   6541  C  CG1 . VAL   B 2 532 ? 8.425   54.037  -23.559 1.00 89.69  ? 836  VAL   B CG1 1 
ATOM   6542  C  CG2 . VAL   B 2 532 ? 6.537   53.105  -22.139 1.00 92.78  ? 836  VAL   B CG2 1 
ATOM   6543  N  N   . TYR   B 2 533 ? 5.049   51.023  -24.899 1.00 92.24  ? 837  TYR   B N   1 
ATOM   6544  C  CA  . TYR   B 2 533 ? 3.961   50.129  -24.551 1.00 96.28  ? 837  TYR   B CA  1 
ATOM   6545  C  C   . TYR   B 2 533 ? 4.558   48.774  -24.215 1.00 96.58  ? 837  TYR   B C   1 
ATOM   6546  O  O   . TYR   B 2 533 ? 5.569   48.386  -24.806 1.00 97.15  ? 837  TYR   B O   1 
ATOM   6547  C  CB  . TYR   B 2 533 ? 2.957   49.984  -25.697 1.00 94.96  ? 837  TYR   B CB  1 
ATOM   6548  C  CG  . TYR   B 2 533 ? 2.441   51.290  -26.250 1.00 96.25  ? 837  TYR   B CG  1 
ATOM   6549  C  CD1 . TYR   B 2 533 ? 1.374   51.943  -25.651 1.00 100.81 ? 837  TYR   B CD1 1 
ATOM   6550  C  CD2 . TYR   B 2 533 ? 3.007   51.862  -27.394 1.00 100.34 ? 837  TYR   B CD2 1 
ATOM   6551  C  CE1 . TYR   B 2 533 ? 0.878   53.145  -26.161 1.00 106.66 ? 837  TYR   B CE1 1 
ATOM   6552  C  CE2 . TYR   B 2 533 ? 2.526   53.061  -27.916 1.00 99.74  ? 837  TYR   B CE2 1 
ATOM   6553  C  CZ  . TYR   B 2 533 ? 1.458   53.700  -27.295 1.00 107.63 ? 837  TYR   B CZ  1 
ATOM   6554  O  OH  . TYR   B 2 533 ? 0.981   54.890  -27.811 1.00 103.99 ? 837  TYR   B OH  1 
ATOM   6555  N  N   . PRO   B 2 534 ? 3.978   48.043  -23.258 1.00 97.11  ? 838  PRO   B N   1 
ATOM   6556  C  CA  . PRO   B 2 534 ? 4.616   46.790  -22.814 1.00 102.28 ? 838  PRO   B CA  1 
ATOM   6557  C  C   . PRO   B 2 534 ? 4.769   45.770  -23.926 1.00 102.13 ? 838  PRO   B C   1 
ATOM   6558  O  O   . PRO   B 2 534 ? 5.644   44.893  -23.844 1.00 97.81  ? 838  PRO   B O   1 
ATOM   6559  C  CB  . PRO   B 2 534 ? 3.671   46.281  -21.714 1.00 105.04 ? 838  PRO   B CB  1 
ATOM   6560  C  CG  . PRO   B 2 534 ? 2.881   47.462  -21.305 1.00 101.83 ? 838  PRO   B CG  1 
ATOM   6561  C  CD  . PRO   B 2 534 ? 2.729   48.310  -22.531 1.00 96.66  ? 838  PRO   B CD  1 
ATOM   6562  N  N   . GLU   B 2 535 ? 3.949   45.872  -24.971 1.00 99.66  ? 839  GLU   B N   1 
ATOM   6563  C  CA  . GLU   B 2 535 ? 3.995   44.925  -26.073 1.00 93.77  ? 839  GLU   B CA  1 
ATOM   6564  C  C   . GLU   B 2 535 ? 5.159   45.219  -27.008 1.00 92.47  ? 839  GLU   B C   1 
ATOM   6565  O  O   . GLU   B 2 535 ? 5.915   44.307  -27.370 1.00 95.04  ? 839  GLU   B O   1 
ATOM   6566  C  CB  . GLU   B 2 535 ? 2.681   44.954  -26.853 1.00 97.95  ? 839  GLU   B CB  1 
ATOM   6567  C  CG  . GLU   B 2 535 ? 1.430   45.130  -26.012 1.00 105.18 ? 839  GLU   B CG  1 
ATOM   6568  C  CD  . GLU   B 2 535 ? 1.233   46.571  -25.559 1.00 105.53 ? 839  GLU   B CD  1 
ATOM   6569  O  OE1 . GLU   B 2 535 ? 2.194   47.153  -25.002 1.00 102.47 ? 839  GLU   B OE1 1 
ATOM   6570  O  OE2 . GLU   B 2 535 ? 0.126   47.122  -25.763 1.00 108.01 ? 839  GLU   B OE2 1 
ATOM   6571  N  N   . GLU   B 2 536 ? 5.320   46.487  -27.408 1.00 93.11  ? 840  GLU   B N   1 
ATOM   6572  C  CA  . GLU   B 2 536 ? 6.286   46.854  -28.441 1.00 89.80  ? 840  GLU   B CA  1 
ATOM   6573  C  C   . GLU   B 2 536 ? 7.653   47.050  -27.798 1.00 81.78  ? 840  GLU   B C   1 
ATOM   6574  O  O   . GLU   B 2 536 ? 7.813   47.868  -26.888 1.00 87.22  ? 840  GLU   B O   1 
ATOM   6575  C  CB  . GLU   B 2 536 ? 5.822   48.104  -29.206 1.00 82.56  ? 840  GLU   B CB  1 
ATOM   6576  N  N   . ALA   B 2 537 ? 8.633   46.279  -28.259 1.00 80.18  ? 841  ALA   B N   1 
ATOM   6577  C  CA  . ALA   B 2 537 ? 9.932   46.256  -27.604 1.00 80.37  ? 841  ALA   B CA  1 
ATOM   6578  C  C   . ALA   B 2 537 ? 10.692  47.516  -27.915 1.00 86.25  ? 841  ALA   B C   1 
ATOM   6579  O  O   . ALA   B 2 537 ? 11.152  48.229  -27.014 1.00 90.81  ? 841  ALA   B O   1 
ATOM   6580  C  CB  . ALA   B 2 537 ? 10.741  45.044  -28.068 1.00 85.99  ? 841  ALA   B CB  1 
ATOM   6581  N  N   . GLU   B 2 538 ? 10.838  47.785  -29.176 1.00 90.00  ? 842  GLU   B N   1 
ATOM   6582  C  CA  . GLU   B 2 538 ? 11.546  48.940  -29.658 1.00 87.27  ? 842  GLU   B CA  1 
ATOM   6583  C  C   . GLU   B 2 538 ? 10.589  50.123  -29.731 1.00 85.67  ? 842  GLU   B C   1 
ATOM   6584  O  O   . GLU   B 2 538 ? 9.428   49.960  -30.120 1.00 83.60  ? 842  GLU   B O   1 
ATOM   6585  C  CB  . GLU   B 2 538 ? 12.140  48.649  -31.019 1.00 88.30  ? 842  GLU   B CB  1 
ATOM   6586  C  CG  . GLU   B 2 538 ? 13.153  49.671  -31.463 1.00 99.60  ? 842  GLU   B CG  1 
ATOM   6587  C  CD  . GLU   B 2 538 ? 14.587  49.255  -31.142 1.00 109.32 ? 842  GLU   B CD  1 
ATOM   6588  O  OE1 . GLU   B 2 538 ? 14.843  48.012  -31.139 1.00 107.74 ? 842  GLU   B OE1 1 
ATOM   6589  O  OE2 . GLU   B 2 538 ? 15.443  50.161  -30.902 1.00 110.87 ? 842  GLU   B OE2 1 
ATOM   6590  N  N   . PRO   B 2 539 ? 11.042  51.310  -29.321 1.00 92.88  ? 843  PRO   B N   1 
ATOM   6591  C  CA  . PRO   B 2 539 ? 10.170  52.493  -29.321 1.00 87.01  ? 843  PRO   B CA  1 
ATOM   6592  C  C   . PRO   B 2 539 ? 10.045  53.036  -30.738 1.00 83.74  ? 843  PRO   B C   1 
ATOM   6593  O  O   . PRO   B 2 539 ? 11.048  53.392  -31.364 1.00 82.93  ? 843  PRO   B O   1 
ATOM   6594  C  CB  . PRO   B 2 539 ? 10.909  53.470  -28.403 1.00 79.14  ? 843  PRO   B CB  1 
ATOM   6595  C  CG  . PRO   B 2 539 ? 12.361  53.109  -28.618 1.00 83.71  ? 843  PRO   B CG  1 
ATOM   6596  C  CD  . PRO   B 2 539 ? 12.416  51.628  -28.893 1.00 87.12  ? 843  PRO   B CD  1 
ATOM   6597  N  N   . LYS   B 2 540 ? 8.809   53.099  -31.246 1.00 84.01  ? 844  LYS   B N   1 
ATOM   6598  C  CA  . LYS   B 2 540 ? 8.553   53.472  -32.636 1.00 88.46  ? 844  LYS   B CA  1 
ATOM   6599  C  C   . LYS   B 2 540 ? 8.018   54.904  -32.814 1.00 89.19  ? 844  LYS   B C   1 
ATOM   6600  O  O   . LYS   B 2 540 ? 7.754   55.308  -33.950 1.00 86.14  ? 844  LYS   B O   1 
ATOM   6601  C  CB  . LYS   B 2 540 ? 7.586   52.457  -33.272 1.00 75.96  ? 844  LYS   B CB  1 
ATOM   6602  N  N   . GLN   B 2 541 ? 7.884   55.692  -31.744 1.00 87.25  ? 845  GLN   B N   1 
ATOM   6603  C  CA  . GLN   B 2 541 ? 7.261   57.007  -31.837 1.00 87.12  ? 845  GLN   B CA  1 
ATOM   6604  C  C   . GLN   B 2 541 ? 7.568   57.839  -30.600 1.00 88.86  ? 845  GLN   B C   1 
ATOM   6605  O  O   . GLN   B 2 541 ? 7.573   57.319  -29.488 1.00 89.98  ? 845  GLN   B O   1 
ATOM   6606  C  CB  . GLN   B 2 541 ? 5.740   56.884  -32.009 1.00 94.30  ? 845  GLN   B CB  1 
ATOM   6607  C  CG  . GLN   B 2 541 ? 5.078   55.754  -31.225 1.00 97.05  ? 845  GLN   B CG  1 
ATOM   6608  C  CD  . GLN   B 2 541 ? 3.654   55.476  -31.705 1.00 105.86 ? 845  GLN   B CD  1 
ATOM   6609  O  OE1 . GLN   B 2 541 ? 2.681   56.087  -31.237 1.00 107.42 ? 845  GLN   B OE1 1 
ATOM   6610  N  NE2 . GLN   B 2 541 ? 3.529   54.542  -32.645 1.00 112.94 ? 845  GLN   B NE2 1 
ATOM   6611  N  N   . GLY   B 2 542 ? 7.764   59.141  -30.804 1.00 94.47  ? 846  GLY   B N   1 
ATOM   6612  C  CA  . GLY   B 2 542 ? 8.105   60.061  -29.733 1.00 87.68  ? 846  GLY   B CA  1 
ATOM   6613  C  C   . GLY   B 2 542 ? 7.750   61.502  -30.059 1.00 87.47  ? 846  GLY   B C   1 
ATOM   6614  O  O   . GLY   B 2 542 ? 6.923   61.776  -30.928 1.00 88.21  ? 846  GLY   B O   1 
ATOM   6615  N  N   . ARG   B 2 543 ? 8.372   62.431  -29.354 1.00 87.00  ? 847  ARG   B N   1 
ATOM   6616  C  CA  . ARG   B 2 543 ? 7.929   63.814  -29.408 1.00 82.78  ? 847  ARG   B CA  1 
ATOM   6617  C  C   . ARG   B 2 543 ? 9.063   64.667  -28.893 1.00 86.67  ? 847  ARG   B C   1 
ATOM   6618  O  O   . ARG   B 2 543 ? 9.637   64.363  -27.845 1.00 85.49  ? 847  ARG   B O   1 
ATOM   6619  C  CB  . ARG   B 2 543 ? 6.681   64.045  -28.559 1.00 82.30  ? 847  ARG   B CB  1 
ATOM   6620  C  CG  . ARG   B 2 543 ? 5.400   63.497  -29.141 1.00 92.66  ? 847  ARG   B CG  1 
ATOM   6621  C  CD  . ARG   B 2 543 ? 4.218   64.324  -28.640 1.00 101.59 ? 847  ARG   B CD  1 
ATOM   6622  N  NE  . ARG   B 2 543 ? 3.997   64.158  -27.208 1.00 100.06 ? 847  ARG   B NE  1 
ATOM   6623  C  CZ  . ARG   B 2 543 ? 3.711   65.148  -26.371 1.00 101.59 ? 847  ARG   B CZ  1 
ATOM   6624  N  NH1 . ARG   B 2 543 ? 3.672   66.407  -26.778 1.00 98.52  ? 847  ARG   B NH1 1 
ATOM   6625  N  NH2 . ARG   B 2 543 ? 3.459   64.867  -25.091 1.00 99.84  ? 847  ARG   B NH2 1 
ATOM   6626  N  N   . ILE   B 2 544 ? 9.392   65.712  -29.637 1.00 90.77  ? 848  ILE   B N   1 
ATOM   6627  C  CA  . ILE   B 2 544 ? 10.110  66.851  -29.093 1.00 84.09  ? 848  ILE   B CA  1 
ATOM   6628  C  C   . ILE   B 2 544 ? 9.064   67.909  -28.811 1.00 82.72  ? 848  ILE   B C   1 
ATOM   6629  O  O   . ILE   B 2 544 ? 8.288   68.265  -29.702 1.00 86.62  ? 848  ILE   B O   1 
ATOM   6630  C  CB  . ILE   B 2 544 ? 11.196  67.350  -30.050 1.00 83.83  ? 848  ILE   B CB  1 
ATOM   6631  C  CG1 . ILE   B 2 544 ? 11.988  66.141  -30.570 1.00 87.06  ? 848  ILE   B CG1 1 
ATOM   6632  C  CG2 . ILE   B 2 544 ? 12.072  68.395  -29.373 1.00 86.48  ? 848  ILE   B CG2 1 
ATOM   6633  C  CD1 . ILE   B 2 544 ? 13.274  66.484  -31.269 1.00 87.16  ? 848  ILE   B CD1 1 
ATOM   6634  N  N   . VAL   B 2 545 ? 8.989   68.349  -27.566 1.00 84.94  ? 849  VAL   B N   1 
ATOM   6635  C  CA  . VAL   B 2 545 ? 8.092   69.424  -27.169 1.00 85.77  ? 849  VAL   B CA  1 
ATOM   6636  C  C   . VAL   B 2 545 ? 8.931   70.653  -26.867 1.00 91.43  ? 849  VAL   B C   1 
ATOM   6637  O  O   . VAL   B 2 545 ? 10.085  70.548  -26.433 1.00 89.57  ? 849  VAL   B O   1 
ATOM   6638  C  CB  . VAL   B 2 545 ? 7.229   69.019  -25.961 1.00 88.74  ? 849  VAL   B CB  1 
ATOM   6639  C  CG1 . VAL   B 2 545 ? 6.548   70.227  -25.357 1.00 90.66  ? 849  VAL   B CG1 1 
ATOM   6640  C  CG2 . VAL   B 2 545 ? 6.200   68.036  -26.392 1.00 93.43  ? 849  VAL   B CG2 1 
ATOM   6641  N  N   . VAL   B 2 546 ? 8.352   71.830  -27.112 1.00 96.52  ? 850  VAL   B N   1 
ATOM   6642  C  CA  . VAL   B 2 546 ? 8.990   73.105  -26.796 1.00 92.33  ? 850  VAL   B CA  1 
ATOM   6643  C  C   . VAL   B 2 546 ? 8.098   73.856  -25.830 1.00 94.40  ? 850  VAL   B C   1 
ATOM   6644  O  O   . VAL   B 2 546 ? 7.004   74.302  -26.204 1.00 89.31  ? 850  VAL   B O   1 
ATOM   6645  C  CB  . VAL   B 2 546 ? 9.265   73.956  -28.036 1.00 90.80  ? 850  VAL   B CB  1 
ATOM   6646  C  CG1 . VAL   B 2 546 ? 10.297  74.993  -27.685 1.00 92.46  ? 850  VAL   B CG1 1 
ATOM   6647  C  CG2 . VAL   B 2 546 ? 9.734   73.094  -29.172 1.00 95.93  ? 850  VAL   B CG2 1 
ATOM   6648  N  N   . PHE   B 2 547 ? 8.581   74.020  -24.597 1.00 96.74  ? 851  PHE   B N   1 
ATOM   6649  C  CA  . PHE   B 2 547 ? 7.910   74.799  -23.565 1.00 93.71  ? 851  PHE   B CA  1 
ATOM   6650  C  C   . PHE   B 2 547 ? 8.560   76.169  -23.387 1.00 95.61  ? 851  PHE   B C   1 
ATOM   6651  O  O   . PHE   B 2 547 ? 9.683   76.436  -23.834 1.00 91.85  ? 851  PHE   B O   1 
ATOM   6652  C  CB  . PHE   B 2 547 ? 7.915   74.075  -22.215 1.00 89.45  ? 851  PHE   B CB  1 
ATOM   6653  C  CG  . PHE   B 2 547 ? 7.183   72.766  -22.211 1.00 96.30  ? 851  PHE   B CG  1 
ATOM   6654  C  CD1 . PHE   B 2 547 ? 5.797   72.725  -22.212 1.00 96.45  ? 851  PHE   B CD1 1 
ATOM   6655  C  CD2 . PHE   B 2 547 ? 7.886   71.571  -22.154 1.00 93.24  ? 851  PHE   B CD2 1 
ATOM   6656  C  CE1 . PHE   B 2 547 ? 5.136   71.515  -22.180 1.00 92.59  ? 851  PHE   B CE1 1 
ATOM   6657  C  CE2 . PHE   B 2 547 ? 7.231   70.374  -22.120 1.00 90.01  ? 851  PHE   B CE2 1 
ATOM   6658  C  CZ  . PHE   B 2 547 ? 5.863   70.342  -22.138 1.00 90.98  ? 851  PHE   B CZ  1 
ATOM   6659  N  N   . GLN   B 2 548 ? 7.833   77.012  -22.650 1.00 100.47 ? 852  GLN   B N   1 
ATOM   6660  C  CA  . GLN   B 2 548 ? 8.336   78.358  -22.298 1.00 95.97  ? 852  GLN   B CA  1 
ATOM   6661  C  C   . GLN   B 2 548 ? 7.652   78.720  -20.975 1.00 95.06  ? 852  GLN   B C   1 
ATOM   6662  O  O   . GLN   B 2 548 ? 6.408   78.682  -20.928 1.00 93.98  ? 852  GLN   B O   1 
ATOM   6663  C  CB  . GLN   B 2 548 ? 7.956   79.399  -23.343 1.00 100.32 ? 852  GLN   B CB  1 
ATOM   6664  C  CG  . GLN   B 2 548 ? 8.533   80.782  -23.068 1.00 102.60 ? 852  GLN   B CG  1 
ATOM   6665  C  CD  . GLN   B 2 548 ? 7.680   81.895  -23.630 1.00 95.12  ? 852  GLN   B CD  1 
ATOM   6666  O  OE1 . GLN   B 2 548 ? 7.847   82.320  -24.777 1.00 99.42  ? 852  GLN   B OE1 1 
ATOM   6667  N  NE2 . GLN   B 2 548 ? 6.743   82.370  -22.823 1.00 96.25  ? 852  GLN   B NE2 1 
ATOM   6668  N  N   . TYR   B 2 549 ? 8.434   79.010  -19.938 1.00 94.48  ? 853  TYR   B N   1 
ATOM   6669  C  CA  . TYR   B 2 549 ? 7.850   79.401  -18.629 1.00 104.08 ? 853  TYR   B CA  1 
ATOM   6670  C  C   . TYR   B 2 549 ? 7.803   80.906  -18.478 1.00 119.13 ? 853  TYR   B C   1 
ATOM   6671  O  O   . TYR   B 2 549 ? 8.859   81.560  -18.586 1.00 120.82 ? 853  TYR   B O   1 
ATOM   6672  C  CB  . TYR   B 2 549 ? 8.678   78.875  -17.456 1.00 102.82 ? 853  TYR   B CB  1 
ATOM   6673  C  CG  . TYR   B 2 549 ? 7.955   78.905  -16.119 1.00 103.56 ? 853  TYR   B CG  1 
ATOM   6674  C  CD1 . TYR   B 2 549 ? 6.825   78.130  -15.900 1.00 108.13 ? 853  TYR   B CD1 1 
ATOM   6675  C  CD2 . TYR   B 2 549 ? 8.403   79.710  -15.081 1.00 103.92 ? 853  TYR   B CD2 1 
ATOM   6676  C  CE1 . TYR   B 2 549 ? 6.164   78.152  -14.685 1.00 110.76 ? 853  TYR   B CE1 1 
ATOM   6677  C  CE2 . TYR   B 2 549 ? 7.749   79.743  -13.862 1.00 103.82 ? 853  TYR   B CE2 1 
ATOM   6678  C  CZ  . TYR   B 2 549 ? 6.627   78.960  -13.665 1.00 108.39 ? 853  TYR   B CZ  1 
ATOM   6679  O  OH  . TYR   B 2 549 ? 5.980   78.987  -12.466 1.00 110.51 ? 853  TYR   B OH  1 
ATOM   6680  N  N   . SER   B 2 550 ? 6.611   81.447  -18.228 1.00 139.02 ? 854  SER   B N   1 
ATOM   6681  C  CA  . SER   B 2 550 ? 6.489   82.917  -18.138 1.00 141.42 ? 854  SER   B CA  1 
ATOM   6682  C  C   . SER   B 2 550 ? 5.621   83.589  -17.044 1.00 143.79 ? 854  SER   B C   1 
ATOM   6683  O  O   . SER   B 2 550 ? 6.202   84.303  -16.202 1.00 143.17 ? 854  SER   B O   1 
ATOM   6684  C  CB  . SER   B 2 550 ? 5.854   83.394  -19.419 1.00 146.35 ? 854  SER   B CB  1 
ATOM   6685  O  OG  . SER   B 2 550 ? 4.687   82.645  -19.729 1.00 147.67 ? 854  SER   B OG  1 
ATOM   6686  N  N   . ASP   B 2 551 ? 4.308   83.363  -17.061 1.00 142.19 ? 855  ASP   B N   1 
ATOM   6687  C  CA  . ASP   B 2 551 ? 3.434   84.048  -16.102 1.00 140.52 ? 855  ASP   B CA  1 
ATOM   6688  C  C   . ASP   B 2 551 ? 3.096   82.908  -15.131 1.00 135.37 ? 855  ASP   B C   1 
ATOM   6689  O  O   . ASP   B 2 551 ? 1.917   82.528  -15.023 1.00 131.61 ? 855  ASP   B O   1 
ATOM   6690  C  CB  . ASP   B 2 551 ? 2.158   84.695  -16.669 1.00 142.89 ? 855  ASP   B CB  1 
ATOM   6691  C  CG  . ASP   B 2 551 ? 2.387   86.026  -17.366 1.00 145.37 ? 855  ASP   B CG  1 
ATOM   6692  O  OD1 . ASP   B 2 551 ? 3.493   86.584  -17.209 1.00 145.37 ? 855  ASP   B OD1 1 
ATOM   6693  O  OD2 . ASP   B 2 551 ? 1.458   86.490  -18.060 1.00 148.52 ? 855  ASP   B OD2 1 
ATOM   6694  N  N   . GLY   B 2 552 ? 4.118   82.373  -14.467 1.00 138.84 ? 856  GLY   B N   1 
ATOM   6695  C  CA  . GLY   B 2 552 ? 3.890   81.326  -13.456 1.00 138.68 ? 856  GLY   B CA  1 
ATOM   6696  C  C   . GLY   B 2 552 ? 3.342   80.058  -14.070 1.00 138.44 ? 856  GLY   B C   1 
ATOM   6697  O  O   . GLY   B 2 552 ? 3.055   79.115  -13.307 1.00 134.93 ? 856  GLY   B O   1 
ATOM   6698  N  N   . LYS   B 2 553 ? 3.219   80.016  -15.394 1.00 129.12 ? 857  LYS   B N   1 
ATOM   6699  C  CA  . LYS   B 2 553 ? 2.598   78.832  -16.031 1.00 123.58 ? 857  LYS   B CA  1 
ATOM   6700  C  C   . LYS   B 2 553 ? 3.465   78.357  -17.197 1.00 120.28 ? 857  LYS   B C   1 
ATOM   6701  O  O   . LYS   B 2 553 ? 4.109   79.203  -17.853 1.00 118.70 ? 857  LYS   B O   1 
ATOM   6702  C  CB  . LYS   B 2 553 ? 1.184   79.183  -16.502 1.00 128.41 ? 857  LYS   B CB  1 
ATOM   6703  N  N   . LEU   B 2 554 ? 3.498   77.045  -17.419 1.00 113.98 ? 858  LEU   B N   1 
ATOM   6704  C  CA  . LEU   B 2 554 ? 4.233   76.510  -18.550 1.00 112.34 ? 858  LEU   B CA  1 
ATOM   6705  C  C   . LEU   B 2 554 ? 3.287   76.367  -19.731 1.00 117.69 ? 858  LEU   B C   1 
ATOM   6706  O  O   . LEU   B 2 554 ? 2.240   75.715  -19.623 1.00 118.82 ? 858  LEU   B O   1 
ATOM   6707  C  CB  . LEU   B 2 554 ? 4.828   75.150  -18.196 1.00 104.42 ? 858  LEU   B CB  1 
ATOM   6708  C  CG  . LEU   B 2 554 ? 5.919   74.609  -19.100 1.00 96.78  ? 858  LEU   B CG  1 
ATOM   6709  C  CD1 . LEU   B 2 554 ? 7.282   75.121  -18.653 1.00 93.79  ? 858  LEU   B CD1 1 
ATOM   6710  C  CD2 . LEU   B 2 554 ? 5.838   73.106  -19.048 1.00 99.21  ? 858  LEU   B CD2 1 
ATOM   6711  N  N   . GLN   B 2 555 ? 3.646   76.957  -20.860 1.00 113.09 ? 859  GLN   B N   1 
ATOM   6712  C  CA  . GLN   B 2 555 ? 2.817   76.783  -22.036 1.00 116.13 ? 859  GLN   B CA  1 
ATOM   6713  C  C   . GLN   B 2 555 ? 3.599   76.071  -23.134 1.00 112.90 ? 859  GLN   B C   1 
ATOM   6714  O  O   . GLN   B 2 555 ? 4.829   76.138  -23.178 1.00 112.96 ? 859  GLN   B O   1 
ATOM   6715  C  CB  . GLN   B 2 555 ? 2.278   78.136  -22.488 1.00 121.07 ? 859  GLN   B CB  1 
ATOM   6716  C  CG  . GLN   B 2 555 ? 1.228   78.054  -23.588 1.00 131.00 ? 859  GLN   B CG  1 
ATOM   6717  C  CD  . GLN   B 2 555 ? 0.254   76.875  -23.451 1.00 132.48 ? 859  GLN   B CD  1 
ATOM   6718  O  OE1 . GLN   B 2 555 ? 0.364   76.033  -22.548 1.00 130.69 ? 859  GLN   B OE1 1 
ATOM   6719  N  NE2 . GLN   B 2 555 ? -0.710  76.821  -24.359 1.00 134.80 ? 859  GLN   B NE2 1 
ATOM   6720  N  N   . THR   B 2 556 ? 2.879   75.365  -24.009 1.00 100.53 ? 860  THR   B N   1 
ATOM   6721  C  CA  . THR   B 2 556 ? 3.498   74.548  -25.054 1.00 103.90 ? 860  THR   B CA  1 
ATOM   6722  C  C   . THR   B 2 556 ? 3.604   75.359  -26.339 1.00 101.90 ? 860  THR   B C   1 
ATOM   6723  O  O   . THR   B 2 556 ? 2.592   75.846  -26.857 1.00 105.33 ? 860  THR   B O   1 
ATOM   6724  C  CB  . THR   B 2 556 ? 2.696   73.272  -25.339 1.00 103.55 ? 860  THR   B CB  1 
ATOM   6725  O  OG1 . THR   B 2 556 ? 2.382   72.570  -24.125 1.00 104.14 ? 860  THR   B OG1 1 
ATOM   6726  C  CG2 . THR   B 2 556 ? 3.493   72.356  -26.272 1.00 96.22  ? 860  THR   B CG2 1 
ATOM   6727  N  N   . VAL   B 2 557 ? 4.815   75.463  -26.883 1.00 98.66  ? 861  VAL   B N   1 
ATOM   6728  C  CA  . VAL   B 2 557 ? 5.051   76.269  -28.078 1.00 93.88  ? 861  VAL   B CA  1 
ATOM   6729  C  C   . VAL   B 2 557 ? 4.909   75.417  -29.344 1.00 96.41  ? 861  VAL   B C   1 
ATOM   6730  O  O   . VAL   B 2 557 ? 4.071   75.703  -30.205 1.00 96.13  ? 861  VAL   B O   1 
ATOM   6731  C  CB  . VAL   B 2 557 ? 6.430   76.945  -27.988 1.00 93.03  ? 861  VAL   B CB  1 
ATOM   6732  C  CG1 . VAL   B 2 557 ? 6.722   77.733  -29.240 1.00 95.18  ? 861  VAL   B CG1 1 
ATOM   6733  C  CG2 . VAL   B 2 557 ? 6.531   77.815  -26.726 1.00 90.33  ? 861  VAL   B CG2 1 
ATOM   6734  N  N   . ALA   B 2 558 ? 5.710   74.361  -29.475 1.00 96.16  ? 862  ALA   B N   1 
ATOM   6735  C  CA  . ALA   B 2 558 ? 5.558   73.440  -30.597 1.00 94.30  ? 862  ALA   B CA  1 
ATOM   6736  C  C   . ALA   B 2 558 ? 5.914   72.025  -30.170 1.00 95.59  ? 862  ALA   B C   1 
ATOM   6737  O  O   . ALA   B 2 558 ? 6.793   71.810  -29.331 1.00 92.22  ? 862  ALA   B O   1 
ATOM   6738  C  CB  . ALA   B 2 558 ? 6.434   73.846  -31.784 1.00 99.39  ? 862  ALA   B CB  1 
ATOM   6739  N  N   . GLU   B 2 559 ? 5.241   71.056  -30.777 1.00 96.53  ? 863  GLU   B N   1 
ATOM   6740  C  CA  . GLU   B 2 559 ? 5.581   69.652  -30.608 1.00 93.16  ? 863  GLU   B CA  1 
ATOM   6741  C  C   . GLU   B 2 559 ? 5.895   69.071  -31.984 1.00 92.15  ? 863  GLU   B C   1 
ATOM   6742  O  O   . GLU   B 2 559 ? 5.082   69.201  -32.902 1.00 93.72  ? 863  GLU   B O   1 
ATOM   6743  C  CB  . GLU   B 2 559 ? 4.434   68.895  -29.913 1.00 92.85  ? 863  GLU   B CB  1 
ATOM   6744  C  CG  . GLU   B 2 559 ? 3.019   69.197  -30.458 1.00 102.70 ? 863  GLU   B CG  1 
ATOM   6745  C  CD  . GLU   B 2 559 ? 1.943   68.135  -30.115 1.00 112.87 ? 863  GLU   B CD  1 
ATOM   6746  O  OE1 . GLU   B 2 559 ? 2.205   66.927  -30.309 1.00 115.66 ? 863  GLU   B OE1 1 
ATOM   6747  O  OE2 . GLU   B 2 559 ? 0.829   68.506  -29.659 1.00 116.36 ? 863  GLU   B OE2 1 
ATOM   6748  N  N   . LYS   B 2 560 ? 7.097   68.482  -32.154 1.00 90.25  ? 864  LYS   B N   1 
ATOM   6749  C  CA  . LYS   B 2 560 ? 7.443   67.709  -33.362 1.00 91.45  ? 864  LYS   B CA  1 
ATOM   6750  C  C   . LYS   B 2 560 ? 7.330   66.224  -33.017 1.00 91.28  ? 864  LYS   B C   1 
ATOM   6751  O  O   . LYS   B 2 560 ? 8.169   65.679  -32.293 1.00 90.73  ? 864  LYS   B O   1 
ATOM   6752  C  CB  . LYS   B 2 560 ? 8.840   68.046  -33.905 1.00 82.87  ? 864  LYS   B CB  1 
ATOM   6753  N  N   . GLU   B 2 561 ? 6.295   65.568  -33.545 1.00 92.44  ? 865  GLU   B N   1 
ATOM   6754  C  CA  . GLU   B 2 561 ? 6.064   64.136  -33.322 1.00 93.28  ? 865  GLU   B CA  1 
ATOM   6755  C  C   . GLU   B 2 561 ? 7.037   63.308  -34.166 1.00 89.99  ? 865  GLU   B C   1 
ATOM   6756  O  O   . GLU   B 2 561 ? 6.868   63.169  -35.379 1.00 89.33  ? 865  GLU   B O   1 
ATOM   6757  C  CB  . GLU   B 2 561 ? 4.611   63.787  -33.637 1.00 94.30  ? 865  GLU   B CB  1 
ATOM   6758  C  CG  . GLU   B 2 561 ? 4.327   62.305  -33.587 1.00 104.90 ? 865  GLU   B CG  1 
ATOM   6759  C  CD  . GLU   B 2 561 ? 3.467   61.830  -34.746 1.00 117.39 ? 865  GLU   B CD  1 
ATOM   6760  O  OE1 . GLU   B 2 561 ? 3.895   61.970  -35.924 1.00 114.15 ? 865  GLU   B OE1 1 
ATOM   6761  O  OE2 . GLU   B 2 561 ? 2.356   61.317  -34.464 1.00 122.93 ? 865  GLU   B OE2 1 
ATOM   6762  N  N   . VAL   B 2 562 ? 8.047   62.725  -33.510 1.00 91.96  ? 866  VAL   B N   1 
ATOM   6763  C  CA  . VAL   B 2 562 ? 9.105   61.942  -34.154 1.00 92.00  ? 866  VAL   B CA  1 
ATOM   6764  C  C   . VAL   B 2 562 ? 8.743   60.454  -34.245 1.00 90.28  ? 866  VAL   B C   1 
ATOM   6765  O  O   . VAL   B 2 562 ? 7.743   60.000  -33.675 1.00 87.88  ? 866  VAL   B O   1 
ATOM   6766  C  CB  . VAL   B 2 562 ? 10.438  62.137  -33.408 1.00 89.57  ? 866  VAL   B CB  1 
ATOM   6767  C  CG1 . VAL   B 2 562 ? 11.023  63.499  -33.744 1.00 90.29  ? 866  VAL   B CG1 1 
ATOM   6768  C  CG2 . VAL   B 2 562 ? 10.225  61.983  -31.887 1.00 85.73  ? 866  VAL   B CG2 1 
ATOM   6769  N  N   . LYS   B 2 563 ? 9.541   59.682  -34.978 1.00 85.17  ? 867  LYS   B N   1 
ATOM   6770  C  CA  . LYS   B 2 563 ? 9.193   58.283  -35.199 1.00 88.16  ? 867  LYS   B CA  1 
ATOM   6771  C  C   . LYS   B 2 563 ? 10.176  57.389  -34.455 1.00 90.99  ? 867  LYS   B C   1 
ATOM   6772  O  O   . LYS   B 2 563 ? 10.754  56.453  -35.023 1.00 87.77  ? 867  LYS   B O   1 
ATOM   6773  C  CB  . LYS   B 2 563 ? 9.160   57.956  -36.699 1.00 89.78  ? 867  LYS   B CB  1 
ATOM   6774  N  N   . GLY   B 2 564 ? 10.347  57.678  -33.171 1.00 89.72  ? 868  GLY   B N   1 
ATOM   6775  C  CA  . GLY   B 2 564 ? 11.343  57.010  -32.362 1.00 86.74  ? 868  GLY   B CA  1 
ATOM   6776  C  C   . GLY   B 2 564 ? 11.440  57.660  -30.995 1.00 87.16  ? 868  GLY   B C   1 
ATOM   6777  O  O   . GLY   B 2 564 ? 10.608  58.483  -30.615 1.00 86.90  ? 868  GLY   B O   1 
ATOM   6778  N  N   . ALA   B 2 565 ? 12.474  57.259  -30.264 1.00 90.30  ? 869  ALA   B N   1 
ATOM   6779  C  CA  . ALA   B 2 565 ? 12.724  57.741  -28.913 1.00 85.95  ? 869  ALA   B CA  1 
ATOM   6780  C  C   . ALA   B 2 565 ? 13.823  58.785  -28.956 1.00 83.92  ? 869  ALA   B C   1 
ATOM   6781  O  O   . ALA   B 2 565 ? 14.933  58.502  -29.424 1.00 80.53  ? 869  ALA   B O   1 
ATOM   6782  C  CB  . ALA   B 2 565 ? 13.130  56.597  -27.986 1.00 82.07  ? 869  ALA   B CB  1 
ATOM   6783  N  N   . VAL   B 2 566 ? 13.513  59.984  -28.466 1.00 81.57  ? 870  VAL   B N   1 
ATOM   6784  C  CA  . VAL   B 2 566 ? 14.511  61.046  -28.343 1.00 84.43  ? 870  VAL   B CA  1 
ATOM   6785  C  C   . VAL   B 2 566 ? 15.339  60.725  -27.102 1.00 84.66  ? 870  VAL   B C   1 
ATOM   6786  O  O   . VAL   B 2 566 ? 14.917  61.002  -25.984 1.00 84.21  ? 870  VAL   B O   1 
ATOM   6787  C  CB  . VAL   B 2 566 ? 13.873  62.435  -28.255 1.00 85.21  ? 870  VAL   B CB  1 
ATOM   6788  C  CG1 . VAL   B 2 566 ? 14.936  63.505  -28.394 1.00 88.71  ? 870  VAL   B CG1 1 
ATOM   6789  C  CG2 . VAL   B 2 566 ? 12.781  62.603  -29.303 1.00 83.79  ? 870  VAL   B CG2 1 
ATOM   6790  N  N   . TYR   B 2 567 ? 16.520  60.130  -27.291 1.00 87.06  ? 871  TYR   B N   1 
ATOM   6791  C  CA  . TYR   B 2 567 ? 17.358  59.736  -26.161 1.00 88.28  ? 871  TYR   B CA  1 
ATOM   6792  C  C   . TYR   B 2 567 ? 18.223  60.879  -25.661 1.00 92.49  ? 871  TYR   B C   1 
ATOM   6793  O  O   . TYR   B 2 567 ? 18.629  60.870  -24.489 1.00 90.78  ? 871  TYR   B O   1 
ATOM   6794  C  CB  . TYR   B 2 567 ? 18.274  58.549  -26.527 1.00 93.53  ? 871  TYR   B CB  1 
ATOM   6795  C  CG  . TYR   B 2 567 ? 17.587  57.205  -26.806 1.00 88.54  ? 871  TYR   B CG  1 
ATOM   6796  C  CD1 . TYR   B 2 567 ? 16.634  56.691  -25.934 1.00 82.49  ? 871  TYR   B CD1 1 
ATOM   6797  C  CD2 . TYR   B 2 567 ? 17.898  56.461  -27.949 1.00 88.37  ? 871  TYR   B CD2 1 
ATOM   6798  C  CE1 . TYR   B 2 567 ? 16.005  55.470  -26.196 1.00 91.94  ? 871  TYR   B CE1 1 
ATOM   6799  C  CE2 . TYR   B 2 567 ? 17.282  55.251  -28.212 1.00 90.06  ? 871  TYR   B CE2 1 
ATOM   6800  C  CZ  . TYR   B 2 567 ? 16.335  54.746  -27.335 1.00 93.87  ? 871  TYR   B CZ  1 
ATOM   6801  O  OH  . TYR   B 2 567 ? 15.720  53.525  -27.614 1.00 90.80  ? 871  TYR   B OH  1 
ATOM   6802  N  N   . SER   B 2 568 ? 18.521  61.855  -26.517 1.00 102.66 ? 872  SER   B N   1 
ATOM   6803  C  CA  . SER   B 2 568 ? 19.330  62.992  -26.107 1.00 103.68 ? 872  SER   B CA  1 
ATOM   6804  C  C   . SER   B 2 568 ? 19.013  64.194  -26.975 1.00 104.24 ? 872  SER   B C   1 
ATOM   6805  O  O   . SER   B 2 568 ? 18.819  64.067  -28.185 1.00 103.70 ? 872  SER   B O   1 
ATOM   6806  C  CB  . SER   B 2 568 ? 20.826  62.676  -26.191 1.00 105.29 ? 872  SER   B CB  1 
ATOM   6807  O  OG  . SER   B 2 568 ? 21.242  61.909  -25.073 1.00 107.92 ? 872  SER   B OG  1 
ATOM   6808  N  N   . MET   B 2 569 ? 18.973  65.356  -26.337 1.00 94.30  ? 873  MET   B N   1 
ATOM   6809  C  CA  . MET   B 2 569 ? 18.879  66.642  -27.001 1.00 92.29  ? 873  MET   B CA  1 
ATOM   6810  C  C   . MET   B 2 569 ? 20.034  67.512  -26.527 1.00 92.11  ? 873  MET   B C   1 
ATOM   6811  O  O   . MET   B 2 569 ? 20.350  67.538  -25.334 1.00 93.06  ? 873  MET   B O   1 
ATOM   6812  C  CB  . MET   B 2 569 ? 17.545  67.316  -26.697 1.00 85.91  ? 873  MET   B CB  1 
ATOM   6813  C  CG  . MET   B 2 569 ? 16.323  66.626  -27.274 1.00 86.26  ? 873  MET   B CG  1 
ATOM   6814  S  SD  . MET   B 2 569 ? 14.946  67.683  -26.832 1.00 94.71  ? 873  MET   B SD  1 
ATOM   6815  C  CE  . MET   B 2 569 ? 14.780  67.261  -25.091 1.00 91.37  ? 873  MET   B CE  1 
ATOM   6816  N  N   . VAL   B 2 570 ? 20.676  68.214  -27.457 1.00 92.99  ? 874  VAL   B N   1 
ATOM   6817  C  CA  . VAL   B 2 570 ? 21.655  69.230  -27.097 1.00 93.03  ? 874  VAL   B CA  1 
ATOM   6818  C  C   . VAL   B 2 570 ? 21.468  70.420  -28.015 1.00 97.70  ? 874  VAL   B C   1 
ATOM   6819  O  O   . VAL   B 2 570 ? 21.285  70.252  -29.227 1.00 95.39  ? 874  VAL   B O   1 
ATOM   6820  C  CB  . VAL   B 2 570 ? 23.101  68.717  -27.184 1.00 88.74  ? 874  VAL   B CB  1 
ATOM   6821  C  CG1 . VAL   B 2 570 ? 23.248  67.461  -26.370 1.00 89.75  ? 874  VAL   B CG1 1 
ATOM   6822  C  CG2 . VAL   B 2 570 ? 23.484  68.493  -28.636 1.00 92.53  ? 874  VAL   B CG2 1 
ATOM   6823  N  N   . GLU   B 2 571 ? 21.474  71.616  -27.426 1.00 98.22  ? 875  GLU   B N   1 
ATOM   6824  C  CA  . GLU   B 2 571 ? 21.656  72.839  -28.190 1.00 97.26  ? 875  GLU   B CA  1 
ATOM   6825  C  C   . GLU   B 2 571 ? 22.958  72.742  -28.967 1.00 97.77  ? 875  GLU   B C   1 
ATOM   6826  O  O   . GLU   B 2 571 ? 24.014  72.466  -28.394 1.00 95.94  ? 875  GLU   B O   1 
ATOM   6827  C  CB  . GLU   B 2 571 ? 21.674  74.045  -27.251 1.00 96.75  ? 875  GLU   B CB  1 
ATOM   6828  C  CG  . GLU   B 2 571 ? 21.803  75.384  -27.944 1.00 109.05 ? 875  GLU   B CG  1 
ATOM   6829  C  CD  . GLU   B 2 571 ? 23.199  75.657  -28.508 1.00 114.69 ? 875  GLU   B CD  1 
ATOM   6830  O  OE1 . GLU   B 2 571 ? 24.172  75.018  -28.038 1.00 109.73 ? 875  GLU   B OE1 1 
ATOM   6831  O  OE2 . GLU   B 2 571 ? 23.314  76.515  -29.425 1.00 113.37 ? 875  GLU   B OE2 1 
ATOM   6832  N  N   . PHE   B 2 572 ? 22.878  72.947  -30.275 1.00 102.16 ? 876  PHE   B N   1 
ATOM   6833  C  CA  . PHE   B 2 572 ? 24.034  72.876  -31.167 1.00 105.37 ? 876  PHE   B CA  1 
ATOM   6834  C  C   . PHE   B 2 572 ? 24.482  74.097  -31.955 1.00 111.64 ? 876  PHE   B C   1 
ATOM   6835  O  O   . PHE   B 2 572 ? 24.466  74.081  -33.193 1.00 112.03 ? 876  PHE   B O   1 
ATOM   6836  C  CB  . PHE   B 2 572 ? 23.917  71.725  -32.169 1.00 103.37 ? 876  PHE   B CB  1 
ATOM   6837  C  CG  . PHE   B 2 572 ? 25.122  71.558  -33.062 1.00 103.85 ? 876  PHE   B CG  1 
ATOM   6838  C  CD1 . PHE   B 2 572 ? 26.377  71.343  -32.520 1.00 105.34 ? 876  PHE   B CD1 1 
ATOM   6839  C  CD2 . PHE   B 2 572 ? 24.992  71.585  -34.446 1.00 104.52 ? 876  PHE   B CD2 1 
ATOM   6840  C  CE1 . PHE   B 2 572 ? 27.484  71.176  -33.338 1.00 110.36 ? 876  PHE   B CE1 1 
ATOM   6841  C  CE2 . PHE   B 2 572 ? 26.096  71.419  -35.266 1.00 105.93 ? 876  PHE   B CE2 1 
ATOM   6842  C  CZ  . PHE   B 2 572 ? 27.342  71.219  -34.708 1.00 112.05 ? 876  PHE   B CZ  1 
ATOM   6843  N  N   . ASN   B 2 573 ? 24.890  75.135  -31.211 1.00 111.28 ? 877  ASN   B N   1 
ATOM   6844  C  CA  . ASN   B 2 573 ? 25.161  76.483  -31.708 1.00 112.33 ? 877  ASN   B CA  1 
ATOM   6845  C  C   . ASN   B 2 573 ? 23.868  76.984  -32.353 1.00 108.32 ? 877  ASN   B C   1 
ATOM   6846  O  O   . ASN   B 2 573 ? 23.765  77.092  -33.579 1.00 109.94 ? 877  ASN   B O   1 
ATOM   6847  C  CB  . ASN   B 2 573 ? 26.403  76.729  -32.591 1.00 111.24 ? 877  ASN   B CB  1 
ATOM   6848  C  CG  . ASN   B 2 573 ? 27.719  76.638  -31.819 1.00 111.91 ? 877  ASN   B CG  1 
ATOM   6849  O  OD1 . ASN   B 2 573 ? 27.745  76.811  -30.600 1.00 114.54 ? 877  ASN   B OD1 1 
ATOM   6850  N  ND2 . ASN   B 2 573 ? 28.816  76.347  -32.530 1.00 112.29 ? 877  ASN   B ND2 1 
ATOM   6851  N  N   . GLY   B 2 574 ? 22.864  77.266  -31.517 1.00 106.86 ? 878  GLY   B N   1 
ATOM   6852  C  CA  . GLY   B 2 574 ? 21.635  77.889  -31.952 1.00 109.02 ? 878  GLY   B CA  1 
ATOM   6853  C  C   . GLY   B 2 574 ? 20.606  76.980  -32.583 1.00 109.19 ? 878  GLY   B C   1 
ATOM   6854  O  O   . GLY   B 2 574 ? 19.433  77.364  -32.669 1.00 107.81 ? 878  GLY   B O   1 
ATOM   6855  N  N   . LYS   B 2 575 ? 21.010  75.802  -33.035 1.00 110.81 ? 879  LYS   B N   1 
ATOM   6856  C  CA  . LYS   B 2 575 ? 20.092  74.775  -33.490 1.00 109.21 ? 879  LYS   B CA  1 
ATOM   6857  C  C   . LYS   B 2 575 ? 19.821  73.792  -32.345 1.00 105.34 ? 879  LYS   B C   1 
ATOM   6858  O  O   . LYS   B 2 575 ? 20.199  74.019  -31.192 1.00 106.44 ? 879  LYS   B O   1 
ATOM   6859  C  CB  . LYS   B 2 575 ? 20.667  74.098  -34.738 1.00 110.92 ? 879  LYS   B CB  1 
ATOM   6860  N  N   . LEU   B 2 576 ? 19.138  72.695  -32.656 1.00 103.19 ? 880  LEU   B N   1 
ATOM   6861  C  CA  . LEU   B 2 576 ? 18.792  71.675  -31.668 1.00 101.45 ? 880  LEU   B CA  1 
ATOM   6862  C  C   . LEU   B 2 576 ? 19.177  70.313  -32.228 1.00 97.02  ? 880  LEU   B C   1 
ATOM   6863  O  O   . LEU   B 2 576 ? 18.499  69.791  -33.118 1.00 91.51  ? 880  LEU   B O   1 
ATOM   6864  C  CB  . LEU   B 2 576 ? 17.301  71.716  -31.320 1.00 97.86  ? 880  LEU   B CB  1 
ATOM   6865  C  CG  . LEU   B 2 576 ? 16.920  70.657  -30.289 1.00 91.81  ? 880  LEU   B CG  1 
ATOM   6866  C  CD1 . LEU   B 2 576 ? 17.327  71.140  -28.907 1.00 88.61  ? 880  LEU   B CD1 1 
ATOM   6867  C  CD2 . LEU   B 2 576 ? 15.435  70.246  -30.352 1.00 88.79  ? 880  LEU   B CD2 1 
ATOM   6868  N  N   . LEU   B 2 577 ? 20.257  69.740  -31.706 1.00 94.26  ? 881  LEU   B N   1 
ATOM   6869  C  CA  . LEU   B 2 577 ? 20.737  68.442  -32.161 1.00 94.91  ? 881  LEU   B CA  1 
ATOM   6870  C  C   . LEU   B 2 577 ? 20.029  67.336  -31.374 1.00 95.26  ? 881  LEU   B C   1 
ATOM   6871  O  O   . LEU   B 2 577 ? 20.250  67.200  -30.170 1.00 93.76  ? 881  LEU   B O   1 
ATOM   6872  C  CB  . LEU   B 2 577 ? 22.252  68.361  -31.984 1.00 93.06  ? 881  LEU   B CB  1 
ATOM   6873  C  CG  . LEU   B 2 577 ? 22.833  67.061  -32.541 1.00 93.99  ? 881  LEU   B CG  1 
ATOM   6874  C  CD1 . LEU   B 2 577 ? 22.756  67.073  -34.079 1.00 95.60  ? 881  LEU   B CD1 1 
ATOM   6875  C  CD2 . LEU   B 2 577 ? 24.262  66.785  -32.043 1.00 88.44  ? 881  LEU   B CD2 1 
ATOM   6876  N  N   . ALA   B 2 578 ? 19.173  66.550  -32.034 1.00 94.02  ? 882  ALA   B N   1 
ATOM   6877  C  CA  . ALA   B 2 578 ? 18.454  65.469  -31.367 1.00 93.42  ? 882  ALA   B CA  1 
ATOM   6878  C  C   . ALA   B 2 578 ? 18.864  64.112  -31.928 1.00 93.93  ? 882  ALA   B C   1 
ATOM   6879  O  O   . ALA   B 2 578 ? 19.236  63.983  -33.096 1.00 93.64  ? 882  ALA   B O   1 
ATOM   6880  C  CB  . ALA   B 2 578 ? 16.928  65.631  -31.488 1.00 88.55  ? 882  ALA   B CB  1 
ATOM   6881  N  N   . SER   B 2 579 ? 18.815  63.100  -31.078 1.00 94.67  ? 883  SER   B N   1 
ATOM   6882  C  CA  . SER   B 2 579 ? 18.998  61.716  -31.495 1.00 93.79  ? 883  SER   B CA  1 
ATOM   6883  C  C   . SER   B 2 579 ? 17.631  61.060  -31.485 1.00 92.74  ? 883  SER   B C   1 
ATOM   6884  O  O   . SER   B 2 579 ? 16.907  61.158  -30.486 1.00 92.76  ? 883  SER   B O   1 
ATOM   6885  C  CB  . SER   B 2 579 ? 19.948  60.977  -30.559 1.00 94.97  ? 883  SER   B CB  1 
ATOM   6886  O  OG  . SER   B 2 579 ? 19.547  61.223  -29.223 1.00 96.78  ? 883  SER   B OG  1 
ATOM   6887  N  N   . ILE   B 2 580 ? 17.261  60.437  -32.600 1.00 91.13  ? 884  ILE   B N   1 
ATOM   6888  C  CA  . ILE   B 2 580 ? 16.063  59.613  -32.674 1.00 87.72  ? 884  ILE   B CA  1 
ATOM   6889  C  C   . ILE   B 2 580 ? 16.514  58.203  -32.993 1.00 88.50  ? 884  ILE   B C   1 
ATOM   6890  O  O   . ILE   B 2 580 ? 16.953  57.935  -34.117 1.00 86.77  ? 884  ILE   B O   1 
ATOM   6891  C  CB  . ILE   B 2 580 ? 15.073  60.096  -33.729 1.00 85.04  ? 884  ILE   B CB  1 
ATOM   6892  C  CG1 . ILE   B 2 580 ? 14.706  61.545  -33.474 1.00 89.01  ? 884  ILE   B CG1 1 
ATOM   6893  C  CG2 . ILE   B 2 580 ? 13.851  59.222  -33.651 1.00 89.69  ? 884  ILE   B CG2 1 
ATOM   6894  C  CD1 . ILE   B 2 580 ? 14.426  61.792  -32.003 1.00 93.53  ? 884  ILE   B CD1 1 
ATOM   6895  N  N   . ASN   B 2 581 ? 16.397  57.300  -32.021 1.00 89.17  ? 885  ASN   B N   1 
ATOM   6896  C  CA  . ASN   B 2 581 ? 16.871  55.938  -32.223 1.00 85.91  ? 885  ASN   B CA  1 
ATOM   6897  C  C   . ASN   B 2 581 ? 18.286  55.984  -32.807 1.00 89.87  ? 885  ASN   B C   1 
ATOM   6898  O  O   . ASN   B 2 581 ? 19.199  56.516  -32.162 1.00 90.58  ? 885  ASN   B O   1 
ATOM   6899  C  CB  . ASN   B 2 581 ? 15.879  55.177  -33.102 1.00 83.04  ? 885  ASN   B CB  1 
ATOM   6900  C  CG  . ASN   B 2 581 ? 14.542  54.896  -32.379 1.00 86.33  ? 885  ASN   B CG  1 
ATOM   6901  O  OD1 . ASN   B 2 581 ? 14.304  55.357  -31.268 1.00 85.20  ? 885  ASN   B OD1 1 
ATOM   6902  N  ND2 . ASN   B 2 581 ? 13.678  54.129  -33.023 1.00 94.35  ? 885  ASN   B ND2 1 
ATOM   6903  N  N   . SER   B 2 582 ? 18.492  55.473  -34.024 1.00 89.63  ? 886  SER   B N   1 
ATOM   6904  C  CA  . SER   B 2 582 ? 19.827  55.392  -34.608 1.00 88.17  ? 886  SER   B CA  1 
ATOM   6905  C  C   . SER   B 2 582 ? 20.181  56.596  -35.485 1.00 91.64  ? 886  SER   B C   1 
ATOM   6906  O  O   . SER   B 2 582 ? 21.162  56.537  -36.234 1.00 92.39  ? 886  SER   B O   1 
ATOM   6907  C  CB  . SER   B 2 582 ? 19.954  54.105  -35.414 1.00 88.77  ? 886  SER   B CB  1 
ATOM   6908  O  OG  . SER   B 2 582 ? 18.786  53.919  -36.187 1.00 84.74  ? 886  SER   B OG  1 
ATOM   6909  N  N   . THR   B 2 583 ? 19.412  57.684  -35.412 1.00 93.13  ? 887  THR   B N   1 
ATOM   6910  C  CA  . THR   B 2 583 ? 19.605  58.847  -36.274 1.00 93.68  ? 887  THR   B CA  1 
ATOM   6911  C  C   . THR   B 2 583 ? 19.977  60.064  -35.443 1.00 91.32  ? 887  THR   B C   1 
ATOM   6912  O  O   . THR   B 2 583 ? 19.307  60.376  -34.457 1.00 88.78  ? 887  THR   B O   1 
ATOM   6913  C  CB  . THR   B 2 583 ? 18.352  59.176  -37.094 1.00 91.98  ? 887  THR   B CB  1 
ATOM   6914  O  OG1 . THR   B 2 583 ? 17.714  57.975  -37.538 1.00 97.89  ? 887  THR   B OG1 1 
ATOM   6915  C  CG2 . THR   B 2 583 ? 18.752  59.970  -38.306 1.00 97.84  ? 887  THR   B CG2 1 
ATOM   6916  N  N   . VAL   B 2 584 ? 21.037  60.747  -35.848 1.00 91.04  ? 888  VAL   B N   1 
ATOM   6917  C  CA  . VAL   B 2 584 ? 21.427  62.031  -35.284 1.00 96.38  ? 888  VAL   B CA  1 
ATOM   6918  C  C   . VAL   B 2 584 ? 20.836  63.100  -36.191 1.00 94.95  ? 888  VAL   B C   1 
ATOM   6919  O  O   . VAL   B 2 584 ? 21.284  63.273  -37.324 1.00 102.33 ? 888  VAL   B O   1 
ATOM   6920  C  CB  . VAL   B 2 584 ? 22.953  62.149  -35.176 1.00 99.09  ? 888  VAL   B CB  1 
ATOM   6921  C  CG1 . VAL   B 2 584 ? 23.361  63.462  -34.538 1.00 94.23  ? 888  VAL   B CG1 1 
ATOM   6922  C  CG2 . VAL   B 2 584 ? 23.505  60.963  -34.405 1.00 94.95  ? 888  VAL   B CG2 1 
ATOM   6923  N  N   . ARG   B 2 585 ? 19.821  63.809  -35.707 1.00 95.16  ? 889  ARG   B N   1 
ATOM   6924  C  CA  . ARG   B 2 585 ? 19.039  64.750  -36.504 1.00 99.58  ? 889  ARG   B CA  1 
ATOM   6925  C  C   . ARG   B 2 585 ? 19.317  66.185  -36.066 1.00 98.90  ? 889  ARG   B C   1 
ATOM   6926  O  O   . ARG   B 2 585 ? 19.288  66.483  -34.868 1.00 97.76  ? 889  ARG   B O   1 
ATOM   6927  C  CB  . ARG   B 2 585 ? 17.550  64.435  -36.361 1.00 97.26  ? 889  ARG   B CB  1 
ATOM   6928  C  CG  . ARG   B 2 585 ? 16.633  65.628  -36.498 1.00 95.12  ? 889  ARG   B CG  1 
ATOM   6929  C  CD  . ARG   B 2 585 ? 15.237  65.115  -36.718 1.00 91.00  ? 889  ARG   B CD  1 
ATOM   6930  N  NE  . ARG   B 2 585 ? 15.251  64.116  -37.774 1.00 89.34  ? 889  ARG   B NE  1 
ATOM   6931  C  CZ  . ARG   B 2 585 ? 14.231  63.326  -38.060 1.00 96.24  ? 889  ARG   B CZ  1 
ATOM   6932  N  NH1 . ARG   B 2 585 ? 13.081  63.429  -37.414 1.00 97.09  ? 889  ARG   B NH1 1 
ATOM   6933  N  NH2 . ARG   B 2 585 ? 14.374  62.400  -39.007 1.00 100.58 ? 889  ARG   B NH2 1 
ATOM   6934  N  N   . LEU   B 2 586 ? 19.588  67.074  -37.023 1.00 96.49  ? 890  LEU   B N   1 
ATOM   6935  C  CA  . LEU   B 2 586 ? 19.842  68.475  -36.696 1.00 98.86  ? 890  LEU   B CA  1 
ATOM   6936  C  C   . LEU   B 2 586 ? 18.636  69.344  -37.050 1.00 98.78  ? 890  LEU   B C   1 
ATOM   6937  O  O   . LEU   B 2 586 ? 18.065  69.220  -38.137 1.00 100.29 ? 890  LEU   B O   1 
ATOM   6938  C  CB  . LEU   B 2 586 ? 21.090  68.985  -37.405 1.00 98.81  ? 890  LEU   B CB  1 
ATOM   6939  C  CG  . LEU   B 2 586 ? 21.499  70.402  -37.030 1.00 99.83  ? 890  LEU   B CG  1 
ATOM   6940  C  CD1 . LEU   B 2 586 ? 21.140  70.707  -35.566 1.00 96.19  ? 890  LEU   B CD1 1 
ATOM   6941  C  CD2 . LEU   B 2 586 ? 22.994  70.578  -37.299 1.00 100.97 ? 890  LEU   B CD2 1 
ATOM   6942  N  N   . TYR   B 2 587 ? 18.251  70.222  -36.117 1.00 94.85  ? 891  TYR   B N   1 
ATOM   6943  C  CA  . TYR   B 2 587 ? 17.006  70.975  -36.199 1.00 96.11  ? 891  TYR   B CA  1 
ATOM   6944  C  C   . TYR   B 2 587 ? 17.287  72.467  -36.111 1.00 101.04 ? 891  TYR   B C   1 
ATOM   6945  O  O   . TYR   B 2 587 ? 18.221  72.879  -35.414 1.00 100.55 ? 891  TYR   B O   1 
ATOM   6946  C  CB  . TYR   B 2 587 ? 16.074  70.615  -35.065 1.00 99.07  ? 891  TYR   B CB  1 
ATOM   6947  C  CG  . TYR   B 2 587 ? 15.125  69.450  -35.265 1.00 98.62  ? 891  TYR   B CG  1 
ATOM   6948  C  CD1 . TYR   B 2 587 ? 14.167  69.452  -36.271 1.00 99.19  ? 891  TYR   B CD1 1 
ATOM   6949  C  CD2 . TYR   B 2 587 ? 15.152  68.372  -34.398 1.00 97.76  ? 891  TYR   B CD2 1 
ATOM   6950  C  CE1 . TYR   B 2 587 ? 13.272  68.386  -36.416 1.00 99.03  ? 891  TYR   B CE1 1 
ATOM   6951  C  CE2 . TYR   B 2 587 ? 14.267  67.314  -34.527 1.00 100.28 ? 891  TYR   B CE2 1 
ATOM   6952  C  CZ  . TYR   B 2 587 ? 13.328  67.316  -35.529 1.00 99.21  ? 891  TYR   B CZ  1 
ATOM   6953  O  OH  . TYR   B 2 587 ? 12.481  66.224  -35.591 1.00 92.37  ? 891  TYR   B OH  1 
ATOM   6954  N  N   . GLU   B 2 588 ? 16.464  73.283  -36.810 1.00 105.07 ? 892  GLU   B N   1 
ATOM   6955  C  CA  . GLU   B 2 588 ? 16.530  74.749  -36.732 1.00 102.67 ? 892  GLU   B CA  1 
ATOM   6956  C  C   . GLU   B 2 588 ? 15.186  75.343  -36.319 1.00 99.85  ? 892  GLU   B C   1 
ATOM   6957  O  O   . GLU   B 2 588 ? 14.125  74.812  -36.664 1.00 103.11 ? 892  GLU   B O   1 
ATOM   6958  C  CB  . GLU   B 2 588 ? 16.964  75.380  -38.051 1.00 97.55  ? 892  GLU   B CB  1 
ATOM   6959  C  CG  . GLU   B 2 588 ? 18.474  75.494  -38.230 1.00 109.27 ? 892  GLU   B CG  1 
ATOM   6960  C  CD  . GLU   B 2 588 ? 18.877  75.851  -39.665 1.00 118.73 ? 892  GLU   B CD  1 
ATOM   6961  O  OE1 . GLU   B 2 588 ? 19.787  76.697  -39.856 1.00 120.11 ? 892  GLU   B OE1 1 
ATOM   6962  O  OE2 . GLU   B 2 588 ? 18.271  75.278  -40.603 1.00 118.71 ? 892  GLU   B OE2 1 
ATOM   6963  N  N   . TRP   B 2 589 ? 15.241  76.449  -35.579 1.00 99.51  ? 893  TRP   B N   1 
ATOM   6964  C  CA  . TRP   B 2 589 ? 14.047  77.146  -35.109 1.00 107.57 ? 893  TRP   B CA  1 
ATOM   6965  C  C   . TRP   B 2 589 ? 13.618  78.151  -36.178 1.00 115.70 ? 893  TRP   B C   1 
ATOM   6966  O  O   . TRP   B 2 589 ? 14.398  79.039  -36.541 1.00 114.02 ? 893  TRP   B O   1 
ATOM   6967  C  CB  . TRP   B 2 589 ? 14.352  77.837  -33.781 1.00 102.96 ? 893  TRP   B CB  1 
ATOM   6968  C  CG  . TRP   B 2 589 ? 13.183  78.192  -32.919 1.00 103.80 ? 893  TRP   B CG  1 
ATOM   6969  C  CD1 . TRP   B 2 589 ? 13.040  79.328  -32.181 1.00 106.26 ? 893  TRP   B CD1 1 
ATOM   6970  C  CD2 . TRP   B 2 589 ? 12.015  77.406  -32.671 1.00 106.39 ? 893  TRP   B CD2 1 
ATOM   6971  N  NE1 . TRP   B 2 589 ? 11.852  79.309  -31.496 1.00 107.62 ? 893  TRP   B NE1 1 
ATOM   6972  C  CE2 . TRP   B 2 589 ? 11.202  78.138  -31.778 1.00 108.37 ? 893  TRP   B CE2 1 
ATOM   6973  C  CE3 . TRP   B 2 589 ? 11.572  76.161  -33.119 1.00 112.21 ? 893  TRP   B CE3 1 
ATOM   6974  C  CZ2 . TRP   B 2 589 ? 9.973   77.664  -31.326 1.00 107.98 ? 893  TRP   B CZ2 1 
ATOM   6975  C  CZ3 . TRP   B 2 589 ? 10.348  75.689  -32.668 1.00 115.01 ? 893  TRP   B CZ3 1 
ATOM   6976  C  CH2 . TRP   B 2 589 ? 9.563   76.439  -31.781 1.00 112.20 ? 893  TRP   B CH2 1 
ATOM   6977  N  N   . THR   B 2 590 ? 12.398  78.002  -36.704 1.00 117.25 ? 894  THR   B N   1 
ATOM   6978  C  CA  . THR   B 2 590 ? 11.951  78.865  -37.794 1.00 121.69 ? 894  THR   B CA  1 
ATOM   6979  C  C   . THR   B 2 590 ? 11.311  80.146  -37.257 1.00 123.18 ? 894  THR   B C   1 
ATOM   6980  O  O   . THR   B 2 590 ? 10.973  80.260  -36.077 1.00 119.20 ? 894  THR   B O   1 
ATOM   6981  C  CB  . THR   B 2 590 ? 10.947  78.148  -38.715 1.00 124.42 ? 894  THR   B CB  1 
ATOM   6982  O  OG1 . THR   B 2 590 ? 9.886   77.562  -37.941 1.00 124.75 ? 894  THR   B OG1 1 
ATOM   6983  C  CG2 . THR   B 2 590 ? 11.626  77.076  -39.557 1.00 115.57 ? 894  THR   B CG2 1 
ATOM   6984  N  N   . THR   B 2 591 ? 11.138  81.118  -38.156 1.00 125.29 ? 895  THR   B N   1 
ATOM   6985  C  CA  . THR   B 2 591 ? 10.454  82.349  -37.779 1.00 130.70 ? 895  THR   B CA  1 
ATOM   6986  C  C   . THR   B 2 591 ? 9.070   82.068  -37.224 1.00 131.42 ? 895  THR   B C   1 
ATOM   6987  O  O   . THR   B 2 591 ? 8.581   82.805  -36.359 1.00 127.02 ? 895  THR   B O   1 
ATOM   6988  C  CB  . THR   B 2 591 ? 10.346  83.271  -38.983 1.00 132.12 ? 895  THR   B CB  1 
ATOM   6989  O  OG1 . THR   B 2 591 ? 9.460   82.683  -39.946 1.00 136.13 ? 895  THR   B OG1 1 
ATOM   6990  C  CG2 . THR   B 2 591 ? 11.721  83.453  -39.611 1.00 128.19 ? 895  THR   B CG2 1 
ATOM   6991  N  N   . GLU   B 2 592 ? 8.425   80.999  -37.705 1.00 138.09 ? 896  GLU   B N   1 
ATOM   6992  C  CA  . GLU   B 2 592 ? 7.079   80.632  -37.287 1.00 138.54 ? 896  GLU   B CA  1 
ATOM   6993  C  C   . GLU   B 2 592 ? 7.072   79.719  -36.073 1.00 133.97 ? 896  GLU   B C   1 
ATOM   6994  O  O   . GLU   B 2 592 ? 6.057   79.054  -35.817 1.00 134.80 ? 896  GLU   B O   1 
ATOM   6995  C  CB  . GLU   B 2 592 ? 6.325   80.001  -38.460 1.00 139.54 ? 896  GLU   B CB  1 
ATOM   6996  C  CG  . GLU   B 2 592 ? 5.826   81.034  -39.474 1.00 139.45 ? 896  GLU   B CG  1 
ATOM   6997  C  CD  . GLU   B 2 592 ? 5.136   82.222  -38.801 1.00 142.74 ? 896  GLU   B CD  1 
ATOM   6998  O  OE1 . GLU   B 2 592 ? 5.841   83.179  -38.403 1.00 145.68 ? 896  GLU   B OE1 1 
ATOM   6999  O  OE2 . GLU   B 2 592 ? 3.892   82.191  -38.656 1.00 142.46 ? 896  GLU   B OE2 1 
ATOM   7000  N  N   . LYS   B 2 593 ? 8.171   79.679  -35.327 1.00 124.46 ? 897  LYS   B N   1 
ATOM   7001  C  CA  . LYS   B 2 593 ? 8.216   79.008  -34.042 1.00 119.57 ? 897  LYS   B CA  1 
ATOM   7002  C  C   . LYS   B 2 593 ? 7.882   77.516  -34.201 1.00 128.16 ? 897  LYS   B C   1 
ATOM   7003  O  O   . LYS   B 2 593 ? 6.987   76.953  -33.553 1.00 122.66 ? 897  LYS   B O   1 
ATOM   7004  C  CB  . LYS   B 2 593 ? 7.279   79.706  -33.051 1.00 106.88 ? 897  LYS   B CB  1 
ATOM   7005  N  N   . GLU   B 2 594 ? 8.616   76.877  -35.106 1.00 126.54 ? 898  GLU   B N   1 
ATOM   7006  C  CA  . GLU   B 2 594 ? 8.468   75.447  -35.312 1.00 126.31 ? 898  GLU   B CA  1 
ATOM   7007  C  C   . GLU   B 2 594 ? 9.825   74.876  -35.701 1.00 126.77 ? 898  GLU   B C   1 
ATOM   7008  O  O   . GLU   B 2 594 ? 10.772  75.616  -35.990 1.00 125.57 ? 898  GLU   B O   1 
ATOM   7009  C  CB  . GLU   B 2 594 ? 7.405   75.150  -36.367 1.00 128.81 ? 898  GLU   B CB  1 
ATOM   7010  C  CG  . GLU   B 2 594 ? 7.750   75.692  -37.741 1.00 133.84 ? 898  GLU   B CG  1 
ATOM   7011  C  CD  . GLU   B 2 594 ? 7.072   74.919  -38.869 1.00 146.52 ? 898  GLU   B CD  1 
ATOM   7012  O  OE1 . GLU   B 2 594 ? 6.029   74.275  -38.614 1.00 149.64 ? 898  GLU   B OE1 1 
ATOM   7013  O  OE2 . GLU   B 2 594 ? 7.589   74.943  -40.013 1.00 151.79 ? 898  GLU   B OE2 1 
ATOM   7014  N  N   . LEU   B 2 595 ? 9.925   73.549  -35.700 1.00 120.10 ? 899  LEU   B N   1 
ATOM   7015  C  CA  . LEU   B 2 595 ? 11.198  72.878  -35.924 1.00 114.01 ? 899  LEU   B CA  1 
ATOM   7016  C  C   . LEU   B 2 595 ? 11.289  72.343  -37.350 1.00 111.83 ? 899  LEU   B C   1 
ATOM   7017  O  O   . LEU   B 2 595 ? 10.429  71.569  -37.791 1.00 114.98 ? 899  LEU   B O   1 
ATOM   7018  C  CB  . LEU   B 2 595 ? 11.395  71.746  -34.905 1.00 110.13 ? 899  LEU   B CB  1 
ATOM   7019  C  CG  . LEU   B 2 595 ? 12.192  72.085  -33.644 1.00 109.01 ? 899  LEU   B CG  1 
ATOM   7020  C  CD1 . LEU   B 2 595 ? 11.981  71.030  -32.583 1.00 104.80 ? 899  LEU   B CD1 1 
ATOM   7021  C  CD2 . LEU   B 2 595 ? 13.688  72.144  -34.000 1.00 108.43 ? 899  LEU   B CD2 1 
ATOM   7022  N  N   . ARG   B 2 596 ? 12.345  72.744  -38.061 1.00 107.31 ? 900  ARG   B N   1 
ATOM   7023  C  CA  . ARG   B 2 596 ? 12.612  72.286  -39.422 1.00 108.25 ? 900  ARG   B CA  1 
ATOM   7024  C  C   . ARG   B 2 596 ? 13.853  71.405  -39.404 1.00 98.13  ? 900  ARG   B C   1 
ATOM   7025  O  O   . ARG   B 2 596 ? 14.770  71.642  -38.617 1.00 99.88  ? 900  ARG   B O   1 
ATOM   7026  C  CB  . ARG   B 2 596 ? 12.800  73.481  -40.405 1.00 102.57 ? 900  ARG   B CB  1 
ATOM   7027  N  N   . THR   B 2 597 ? 13.891  70.398  -40.279 1.00 96.37  ? 901  THR   B N   1 
ATOM   7028  C  CA  . THR   B 2 597 ? 14.980  69.416  -40.296 1.00 101.33 ? 901  THR   B CA  1 
ATOM   7029  C  C   . THR   B 2 597 ? 16.063  69.853  -41.277 1.00 98.61  ? 901  THR   B C   1 
ATOM   7030  O  O   . THR   B 2 597 ? 15.868  69.772  -42.493 1.00 101.63 ? 901  THR   B O   1 
ATOM   7031  C  CB  . THR   B 2 597 ? 14.453  68.036  -40.693 1.00 99.72  ? 901  THR   B CB  1 
ATOM   7032  O  OG1 . THR   B 2 597 ? 13.282  67.717  -39.920 1.00 100.94 ? 901  THR   B OG1 1 
ATOM   7033  C  CG2 . THR   B 2 597 ? 15.551  66.948  -40.517 1.00 97.18  ? 901  THR   B CG2 1 
ATOM   7034  N  N   . GLU   B 2 598 ? 17.222  70.273  -40.764 1.00 98.76  ? 902  GLU   B N   1 
ATOM   7035  C  CA  . GLU   B 2 598 ? 18.339  70.594  -41.654 1.00 103.11 ? 902  GLU   B CA  1 
ATOM   7036  C  C   . GLU   B 2 598 ? 18.892  69.333  -42.296 1.00 106.94 ? 902  GLU   B C   1 
ATOM   7037  O  O   . GLU   B 2 598 ? 18.728  69.099  -43.499 1.00 110.45 ? 902  GLU   B O   1 
ATOM   7038  C  CB  . GLU   B 2 598 ? 19.463  71.328  -40.906 1.00 108.05 ? 902  GLU   B CB  1 
ATOM   7039  C  CG  . GLU   B 2 598 ? 20.739  71.504  -41.759 1.00 111.02 ? 902  GLU   B CG  1 
ATOM   7040  C  CD  . GLU   B 2 598 ? 21.711  72.603  -41.278 1.00 109.93 ? 902  GLU   B CD  1 
ATOM   7041  O  OE1 . GLU   B 2 598 ? 22.886  72.593  -41.716 1.00 104.76 ? 902  GLU   B OE1 1 
ATOM   7042  O  OE2 . GLU   B 2 598 ? 21.306  73.480  -40.481 1.00 112.37 ? 902  GLU   B OE2 1 
ATOM   7043  N  N   . CYS   B 2 599 ? 19.541  68.499  -41.491 1.00 106.04 ? 903  CYS   B N   1 
ATOM   7044  C  CA  . CYS   B 2 599 ? 20.174  67.293  -41.991 1.00 106.92 ? 903  CYS   B CA  1 
ATOM   7045  C  C   . CYS   B 2 599 ? 19.934  66.144  -41.026 1.00 108.38 ? 903  CYS   B C   1 
ATOM   7046  O  O   . CYS   B 2 599 ? 19.635  66.340  -39.844 1.00 105.39 ? 903  CYS   B O   1 
ATOM   7047  C  CB  . CYS   B 2 599 ? 21.668  67.508  -42.178 1.00 111.05 ? 903  CYS   B CB  1 
ATOM   7048  S  SG  . CYS   B 2 599 ? 22.292  68.497  -40.833 1.00 107.77 ? 903  CYS   B SG  1 
ATOM   7049  N  N   . ASN   B 2 600 ? 20.071  64.934  -41.561 1.00 113.99 ? 904  ASN   B N   1 
ATOM   7050  C  CA  . ASN   B 2 600 ? 20.035  63.703  -40.791 1.00 109.61 ? 904  ASN   B CA  1 
ATOM   7051  C  C   . ASN   B 2 600 ? 21.354  62.963  -40.941 1.00 108.93 ? 904  ASN   B C   1 
ATOM   7052  O  O   . ASN   B 2 600 ? 22.049  63.089  -41.957 1.00 112.07 ? 904  ASN   B O   1 
ATOM   7053  C  CB  . ASN   B 2 600 ? 18.897  62.793  -41.240 1.00 108.57 ? 904  ASN   B CB  1 
ATOM   7054  C  CG  . ASN   B 2 600 ? 17.582  63.157  -40.600 1.00 108.15 ? 904  ASN   B CG  1 
ATOM   7055  O  OD1 . ASN   B 2 600 ? 17.506  63.367  -39.386 1.00 107.27 ? 904  ASN   B OD1 1 
ATOM   7056  N  ND2 . ASN   B 2 600 ? 16.531  63.243  -41.411 1.00 109.82 ? 904  ASN   B ND2 1 
ATOM   7057  N  N   . HIS   B 2 601 ? 21.691  62.182  -39.922 1.00 104.91 ? 905  HIS   B N   1 
ATOM   7058  C  CA  . HIS   B 2 601 ? 22.816  61.256  -40.004 1.00 101.55 ? 905  HIS   B CA  1 
ATOM   7059  C  C   . HIS   B 2 601 ? 22.407  59.929  -39.400 1.00 96.91  ? 905  HIS   B C   1 
ATOM   7060  O  O   . HIS   B 2 601 ? 22.078  59.862  -38.213 1.00 97.86  ? 905  HIS   B O   1 
ATOM   7061  C  CB  . HIS   B 2 601 ? 24.045  61.781  -39.288 1.00 99.08  ? 905  HIS   B CB  1 
ATOM   7062  C  CG  . HIS   B 2 601 ? 25.264  60.973  -39.571 1.00 100.13 ? 905  HIS   B CG  1 
ATOM   7063  N  ND1 . HIS   B 2 601 ? 25.394  59.665  -39.167 1.00 100.57 ? 905  HIS   B ND1 1 
ATOM   7064  C  CD2 . HIS   B 2 601 ? 26.391  61.266  -40.258 1.00 104.25 ? 905  HIS   B CD2 1 
ATOM   7065  C  CE1 . HIS   B 2 601 ? 26.562  59.194  -39.566 1.00 101.15 ? 905  HIS   B CE1 1 
ATOM   7066  N  NE2 . HIS   B 2 601 ? 27.188  60.146  -40.231 1.00 99.53  ? 905  HIS   B NE2 1 
ATOM   7067  N  N   . TYR   B 2 602 ? 22.454  58.879  -40.209 1.00 100.78 ? 906  TYR   B N   1 
ATOM   7068  C  CA  . TYR   B 2 602 ? 21.951  57.565  -39.834 1.00 99.16  ? 906  TYR   B CA  1 
ATOM   7069  C  C   . TYR   B 2 602 ? 23.129  56.669  -39.481 1.00 97.70  ? 906  TYR   B C   1 
ATOM   7070  O  O   . TYR   B 2 602 ? 23.997  56.427  -40.325 1.00 99.81  ? 906  TYR   B O   1 
ATOM   7071  C  CB  . TYR   B 2 602 ? 21.145  56.976  -40.987 1.00 95.81  ? 906  TYR   B CB  1 
ATOM   7072  C  CG  . TYR   B 2 602 ? 20.022  57.872  -41.454 1.00 99.84  ? 906  TYR   B CG  1 
ATOM   7073  C  CD1 . TYR   B 2 602 ? 18.766  57.777  -40.870 1.00 101.69 ? 906  TYR   B CD1 1 
ATOM   7074  C  CD2 . TYR   B 2 602 ? 20.210  58.820  -42.474 1.00 100.47 ? 906  TYR   B CD2 1 
ATOM   7075  C  CE1 . TYR   B 2 602 ? 17.712  58.586  -41.283 1.00 104.05 ? 906  TYR   B CE1 1 
ATOM   7076  C  CE2 . TYR   B 2 602 ? 19.147  59.642  -42.903 1.00 96.22  ? 906  TYR   B CE2 1 
ATOM   7077  C  CZ  . TYR   B 2 602 ? 17.901  59.508  -42.287 1.00 97.64  ? 906  TYR   B CZ  1 
ATOM   7078  O  OH  . TYR   B 2 602 ? 16.807  60.260  -42.625 1.00 90.24  ? 906  TYR   B OH  1 
ATOM   7079  N  N   . ASN   B 2 603 ? 23.171  56.187  -38.248 1.00 96.24  ? 907  ASN   B N   1 
ATOM   7080  C  CA  . ASN   B 2 603 ? 24.274  55.342  -37.815 1.00 98.21  ? 907  ASN   B CA  1 
ATOM   7081  C  C   . ASN   B 2 603 ? 23.812  53.912  -37.587 1.00 102.49 ? 907  ASN   B C   1 
ATOM   7082  O  O   . ASN   B 2 603 ? 22.613  53.603  -37.560 1.00 99.96  ? 907  ASN   B O   1 
ATOM   7083  C  CB  . ASN   B 2 603 ? 24.914  55.865  -36.530 1.00 102.43 ? 907  ASN   B CB  1 
ATOM   7084  C  CG  . ASN   B 2 603 ? 24.895  57.384  -36.436 1.00 102.35 ? 907  ASN   B CG  1 
ATOM   7085  O  OD1 . ASN   B 2 603 ? 23.842  57.998  -36.179 1.00 98.11  ? 907  ASN   B OD1 1 
ATOM   7086  N  ND2 . ASN   B 2 603 ? 26.071  58.000  -36.601 1.00 95.13  ? 907  ASN   B ND2 1 
ATOM   7087  N  N   . ASN   B 2 604 ? 24.804  53.047  -37.395 1.00 110.49 ? 908  ASN   B N   1 
ATOM   7088  C  CA  . ASN   B 2 604 ? 24.606  51.632  -37.132 1.00 108.20 ? 908  ASN   B CA  1 
ATOM   7089  C  C   . ASN   B 2 604 ? 24.601  51.306  -35.638 1.00 108.91 ? 908  ASN   B C   1 
ATOM   7090  O  O   . ASN   B 2 604 ? 24.758  50.141  -35.277 1.00 112.22 ? 908  ASN   B O   1 
ATOM   7091  C  CB  . ASN   B 2 604 ? 25.693  50.826  -37.830 1.00 109.95 ? 908  ASN   B CB  1 
ATOM   7092  C  CG  . ASN   B 2 604 ? 27.070  51.404  -37.590 1.00 117.55 ? 908  ASN   B CG  1 
ATOM   7093  O  OD1 . ASN   B 2 604 ? 27.238  52.632  -37.475 1.00 123.30 ? 908  ASN   B OD1 1 
ATOM   7094  N  ND2 . ASN   B 2 604 ? 28.070  50.530  -37.506 1.00 116.09 ? 908  ASN   B ND2 1 
ATOM   7095  N  N   . ILE   B 2 605 ? 24.465  52.306  -34.767 1.00 98.66  ? 909  ILE   B N   1 
ATOM   7096  C  CA  . ILE   B 2 605 ? 24.229  52.103  -33.344 1.00 96.12  ? 909  ILE   B CA  1 
ATOM   7097  C  C   . ILE   B 2 605 ? 23.034  52.973  -32.945 1.00 94.11  ? 909  ILE   B C   1 
ATOM   7098  O  O   . ILE   B 2 605 ? 22.430  53.648  -33.775 1.00 94.16  ? 909  ILE   B O   1 
ATOM   7099  C  CB  . ILE   B 2 605 ? 25.489  52.391  -32.485 1.00 95.37  ? 909  ILE   B CB  1 
ATOM   7100  C  CG1 . ILE   B 2 605 ? 25.907  53.861  -32.518 1.00 91.71  ? 909  ILE   B CG1 1 
ATOM   7101  C  CG2 . ILE   B 2 605 ? 26.667  51.611  -32.986 1.00 94.98  ? 909  ILE   B CG2 1 
ATOM   7102  C  CD1 . ILE   B 2 605 ? 25.249  54.751  -31.455 1.00 87.38  ? 909  ILE   B CD1 1 
ATOM   7103  N  N   . MET   B 2 606 ? 22.634  52.881  -31.685 1.00 88.98  ? 910  MET   B N   1 
ATOM   7104  C  CA  . MET   B 2 606 ? 21.590  53.748  -31.163 1.00 86.21  ? 910  MET   B CA  1 
ATOM   7105  C  C   . MET   B 2 606 ? 22.247  54.948  -30.496 1.00 88.97  ? 910  MET   B C   1 
ATOM   7106  O  O   . MET   B 2 606 ? 23.162  54.790  -29.684 1.00 88.01  ? 910  MET   B O   1 
ATOM   7107  C  CB  . MET   B 2 606 ? 20.697  52.993  -30.177 1.00 85.58  ? 910  MET   B CB  1 
ATOM   7108  C  CG  . MET   B 2 606 ? 19.384  52.513  -30.786 1.00 95.33  ? 910  MET   B CG  1 
ATOM   7109  S  SD  . MET   B 2 606 ? 18.407  51.558  -29.587 1.00 124.82 ? 910  MET   B SD  1 
ATOM   7110  C  CE  . MET   B 2 606 ? 19.155  52.152  -28.053 1.00 94.41  ? 910  MET   B CE  1 
ATOM   7111  N  N   . ALA   B 2 607 ? 21.792  56.151  -30.836 1.00 88.34  ? 911  ALA   B N   1 
ATOM   7112  C  CA  . ALA   B 2 607 ? 22.460  57.348  -30.329 1.00 89.02  ? 911  ALA   B CA  1 
ATOM   7113  C  C   . ALA   B 2 607 ? 21.943  57.660  -28.926 1.00 93.13  ? 911  ALA   B C   1 
ATOM   7114  O  O   . ALA   B 2 607 ? 21.190  58.608  -28.696 1.00 94.88  ? 911  ALA   B O   1 
ATOM   7115  C  CB  . ALA   B 2 607 ? 22.270  58.526  -31.270 1.00 87.76  ? 911  ALA   B CB  1 
ATOM   7116  N  N   . LEU   B 2 608 ? 22.372  56.830  -27.969 1.00 94.89  ? 912  LEU   B N   1 
ATOM   7117  C  CA  . LEU   B 2 608 ? 21.976  57.041  -26.577 1.00 94.57  ? 912  LEU   B CA  1 
ATOM   7118  C  C   . LEU   B 2 608 ? 22.662  58.272  -25.990 1.00 98.45  ? 912  LEU   B C   1 
ATOM   7119  O  O   . LEU   B 2 608 ? 22.041  59.026  -25.229 1.00 99.69  ? 912  LEU   B O   1 
ATOM   7120  C  CB  . LEU   B 2 608 ? 22.285  55.799  -25.727 1.00 91.58  ? 912  LEU   B CB  1 
ATOM   7121  C  CG  . LEU   B 2 608 ? 21.321  54.596  -25.715 1.00 91.55  ? 912  LEU   B CG  1 
ATOM   7122  C  CD1 . LEU   B 2 608 ? 19.868  55.043  -25.785 1.00 93.40  ? 912  LEU   B CD1 1 
ATOM   7123  C  CD2 . LEU   B 2 608 ? 21.613  53.543  -26.806 1.00 94.53  ? 912  LEU   B CD2 1 
ATOM   7124  N  N   . TYR   B 2 609 ? 23.937  58.498  -26.330 1.00 95.26  ? 913  TYR   B N   1 
ATOM   7125  C  CA  . TYR   B 2 609 ? 24.749  59.565  -25.741 1.00 94.86  ? 913  TYR   B CA  1 
ATOM   7126  C  C   . TYR   B 2 609 ? 25.147  60.552  -26.830 1.00 94.64  ? 913  TYR   B C   1 
ATOM   7127  O  O   . TYR   B 2 609 ? 25.581  60.142  -27.915 1.00 94.76  ? 913  TYR   B O   1 
ATOM   7128  C  CB  . TYR   B 2 609 ? 26.010  59.014  -25.038 1.00 92.59  ? 913  TYR   B CB  1 
ATOM   7129  C  CG  . TYR   B 2 609 ? 25.741  57.974  -23.961 1.00 85.88  ? 913  TYR   B CG  1 
ATOM   7130  C  CD1 . TYR   B 2 609 ? 25.118  58.316  -22.773 1.00 85.66  ? 913  TYR   B CD1 1 
ATOM   7131  C  CD2 . TYR   B 2 609 ? 26.111  56.654  -24.144 1.00 88.47  ? 913  TYR   B CD2 1 
ATOM   7132  C  CE1 . TYR   B 2 609 ? 24.866  57.370  -21.790 1.00 87.55  ? 913  TYR   B CE1 1 
ATOM   7133  C  CE2 . TYR   B 2 609 ? 25.861  55.697  -23.167 1.00 92.58  ? 913  TYR   B CE2 1 
ATOM   7134  C  CZ  . TYR   B 2 609 ? 25.238  56.063  -21.981 1.00 89.18  ? 913  TYR   B CZ  1 
ATOM   7135  O  OH  . TYR   B 2 609 ? 24.983  55.127  -20.991 1.00 79.16  ? 913  TYR   B OH  1 
ATOM   7136  N  N   . LEU   B 2 610 ? 25.028  61.848  -26.533 1.00 92.47  ? 914  LEU   B N   1 
ATOM   7137  C  CA  . LEU   B 2 610 ? 25.295  62.895  -27.512 1.00 89.31  ? 914  LEU   B CA  1 
ATOM   7138  C  C   . LEU   B 2 610 ? 26.070  64.007  -26.841 1.00 91.89  ? 914  LEU   B C   1 
ATOM   7139  O  O   . LEU   B 2 610 ? 25.567  64.613  -25.894 1.00 99.40  ? 914  LEU   B O   1 
ATOM   7140  C  CB  . LEU   B 2 610 ? 23.988  63.436  -28.080 1.00 91.30  ? 914  LEU   B CB  1 
ATOM   7141  C  CG  . LEU   B 2 610 ? 24.056  63.887  -29.529 1.00 96.31  ? 914  LEU   B CG  1 
ATOM   7142  C  CD1 . LEU   B 2 610 ? 24.734  62.805  -30.354 1.00 92.52  ? 914  LEU   B CD1 1 
ATOM   7143  C  CD2 . LEU   B 2 610 ? 22.655  64.170  -30.053 1.00 97.65  ? 914  LEU   B CD2 1 
ATOM   7144  N  N   . LYS   B 2 611 ? 27.277  64.292  -27.325 1.00 95.11  ? 915  LYS   B N   1 
ATOM   7145  C  CA  . LYS   B 2 611 ? 28.030  65.450  -26.841 1.00 98.78  ? 915  LYS   B CA  1 
ATOM   7146  C  C   . LYS   B 2 611 ? 28.566  66.279  -28.005 1.00 99.11  ? 915  LYS   B C   1 
ATOM   7147  O  O   . LYS   B 2 611 ? 28.759  65.778  -29.119 1.00 100.26 ? 915  LYS   B O   1 
ATOM   7148  C  CB  . LYS   B 2 611 ? 29.182  65.033  -25.925 1.00 92.26  ? 915  LYS   B CB  1 
ATOM   7149  C  CG  . LYS   B 2 611 ? 28.726  64.293  -24.670 1.00 91.09  ? 915  LYS   B CG  1 
ATOM   7150  C  CD  . LYS   B 2 611 ? 27.870  65.148  -23.740 1.00 90.54  ? 915  LYS   B CD  1 
ATOM   7151  C  CE  . LYS   B 2 611 ? 27.512  64.373  -22.473 1.00 87.11  ? 915  LYS   B CE  1 
ATOM   7152  N  NZ  . LYS   B 2 611 ? 26.650  65.134  -21.513 1.00 91.36  ? 915  LYS   B NZ  1 
ATOM   7153  N  N   . THR   B 2 612 ? 28.786  67.570  -27.741 1.00 98.32  ? 916  THR   B N   1 
ATOM   7154  C  CA  . THR   B 2 612 ? 29.328  68.483  -28.748 1.00 102.69 ? 916  THR   B CA  1 
ATOM   7155  C  C   . THR   B 2 612 ? 30.314  69.446  -28.095 1.00 92.75  ? 916  THR   B C   1 
ATOM   7156  O  O   . THR   B 2 612 ? 30.012  70.023  -27.046 1.00 93.35  ? 916  THR   B O   1 
ATOM   7157  C  CB  . THR   B 2 612 ? 28.206  69.266  -29.478 1.00 97.63  ? 916  THR   B CB  1 
ATOM   7158  O  OG1 . THR   B 2 612 ? 27.894  70.468  -28.777 1.00 95.62  ? 916  THR   B OG1 1 
ATOM   7159  C  CG2 . THR   B 2 612 ? 26.932  68.444  -29.560 1.00 100.55 ? 916  THR   B CG2 1 
ATOM   7160  N  N   . LYS   B 2 613 ? 31.506  69.569  -28.686 1.00 92.97  ? 917  LYS   B N   1 
ATOM   7161  C  CA  . LYS   B 2 613 ? 32.386  70.720  -28.493 1.00 98.57  ? 917  LYS   B CA  1 
ATOM   7162  C  C   . LYS   B 2 613 ? 32.488  71.415  -29.844 1.00 110.73 ? 917  LYS   B C   1 
ATOM   7163  O  O   . LYS   B 2 613 ? 32.960  70.813  -30.817 1.00 115.78 ? 917  LYS   B O   1 
ATOM   7164  C  CB  . LYS   B 2 613 ? 33.777  70.334  -27.981 1.00 78.28  ? 917  LYS   B CB  1 
ATOM   7165  N  N   . GLY   B 2 614 ? 32.024  72.662  -29.918 1.00 100.94 ? 918  GLY   B N   1 
ATOM   7166  C  CA  . GLY   B 2 614 ? 32.051  73.362  -31.187 1.00 109.62 ? 918  GLY   B CA  1 
ATOM   7167  C  C   . GLY   B 2 614 ? 31.237  72.717  -32.287 1.00 117.74 ? 918  GLY   B C   1 
ATOM   7168  O  O   . GLY   B 2 614 ? 30.009  72.658  -32.200 1.00 118.57 ? 918  GLY   B O   1 
ATOM   7169  N  N   . ASP   B 2 615 ? 31.901  72.250  -33.340 1.00 132.53 ? 919  ASP   B N   1 
ATOM   7170  C  CA  . ASP   B 2 615 ? 31.211  71.589  -34.432 1.00 133.66 ? 919  ASP   B CA  1 
ATOM   7171  C  C   . ASP   B 2 615 ? 31.463  70.080  -34.448 1.00 133.71 ? 919  ASP   B C   1 
ATOM   7172  O  O   . ASP   B 2 615 ? 31.065  69.398  -35.405 1.00 133.54 ? 919  ASP   B O   1 
ATOM   7173  C  CB  . ASP   B 2 615 ? 31.599  72.228  -35.774 1.00 137.17 ? 919  ASP   B CB  1 
ATOM   7174  C  CG  . ASP   B 2 615 ? 30.766  73.486  -36.115 1.00 140.77 ? 919  ASP   B CG  1 
ATOM   7175  O  OD1 . ASP   B 2 615 ? 30.906  74.534  -35.438 1.00 142.63 ? 919  ASP   B OD1 1 
ATOM   7176  O  OD2 . ASP   B 2 615 ? 29.982  73.431  -37.096 1.00 143.47 ? 919  ASP   B OD2 1 
ATOM   7177  N  N   . PHE   B 2 616 ? 32.100  69.543  -33.410 1.00 125.48 ? 920  PHE   B N   1 
ATOM   7178  C  CA  . PHE   B 2 616 ? 32.280  68.106  -33.252 1.00 125.83 ? 920  PHE   B CA  1 
ATOM   7179  C  C   . PHE   B 2 616 ? 31.059  67.494  -32.563 1.00 122.49 ? 920  PHE   B C   1 
ATOM   7180  O  O   . PHE   B 2 616 ? 30.399  68.138  -31.740 1.00 121.48 ? 920  PHE   B O   1 
ATOM   7181  C  CB  . PHE   B 2 616 ? 33.541  67.805  -32.437 1.00 125.96 ? 920  PHE   B CB  1 
ATOM   7182  C  CG  . PHE   B 2 616 ? 34.828  67.938  -33.213 1.00 130.61 ? 920  PHE   B CG  1 
ATOM   7183  C  CD1 . PHE   B 2 616 ? 34.876  67.672  -34.580 1.00 131.08 ? 920  PHE   B CD1 1 
ATOM   7184  C  CD2 . PHE   B 2 616 ? 36.000  68.322  -32.566 1.00 130.10 ? 920  PHE   B CD2 1 
ATOM   7185  C  CE1 . PHE   B 2 616 ? 36.072  67.790  -35.291 1.00 131.32 ? 920  PHE   B CE1 1 
ATOM   7186  C  CE2 . PHE   B 2 616 ? 37.195  68.444  -33.266 1.00 129.83 ? 920  PHE   B CE2 1 
ATOM   7187  C  CZ  . PHE   B 2 616 ? 37.230  68.178  -34.632 1.00 131.20 ? 920  PHE   B CZ  1 
ATOM   7188  N  N   . ILE   B 2 617 ? 30.764  66.240  -32.905 1.00 109.65 ? 921  ILE   B N   1 
ATOM   7189  C  CA  . ILE   B 2 617 ? 29.623  65.520  -32.352 1.00 104.76 ? 921  ILE   B CA  1 
ATOM   7190  C  C   . ILE   B 2 617 ? 30.086  64.142  -31.887 1.00 104.51 ? 921  ILE   B C   1 
ATOM   7191  O  O   . ILE   B 2 617 ? 30.721  63.403  -32.648 1.00 102.76 ? 921  ILE   B O   1 
ATOM   7192  C  CB  . ILE   B 2 617 ? 28.486  65.400  -33.382 1.00 102.92 ? 921  ILE   B CB  1 
ATOM   7193  C  CG1 . ILE   B 2 617 ? 27.935  66.795  -33.695 1.00 106.25 ? 921  ILE   B CG1 1 
ATOM   7194  C  CG2 . ILE   B 2 617 ? 27.412  64.429  -32.888 1.00 98.92  ? 921  ILE   B CG2 1 
ATOM   7195  C  CD1 . ILE   B 2 617 ? 26.491  66.823  -34.152 1.00 101.70 ? 921  ILE   B CD1 1 
ATOM   7196  N  N   . LEU   B 2 618 ? 29.784  63.803  -30.638 1.00 100.00 ? 922  LEU   B N   1 
ATOM   7197  C  CA  . LEU   B 2 618 ? 30.137  62.510  -30.067 1.00 97.92  ? 922  LEU   B CA  1 
ATOM   7198  C  C   . LEU   B 2 618 ? 28.872  61.689  -29.869 1.00 96.26  ? 922  LEU   B C   1 
ATOM   7199  O  O   . LEU   B 2 618 ? 27.914  62.165  -29.250 1.00 96.95  ? 922  LEU   B O   1 
ATOM   7200  C  CB  . LEU   B 2 618 ? 30.876  62.681  -28.738 1.00 96.69  ? 922  LEU   B CB  1 
ATOM   7201  C  CG  . LEU   B 2 618 ? 31.569  61.432  -28.196 1.00 92.88  ? 922  LEU   B CG  1 
ATOM   7202  C  CD1 . LEU   B 2 618 ? 32.163  60.633  -29.358 1.00 92.97  ? 922  LEU   B CD1 1 
ATOM   7203  C  CD2 . LEU   B 2 618 ? 32.639  61.828  -27.189 1.00 88.75  ? 922  LEU   B CD2 1 
ATOM   7204  N  N   . VAL   B 2 619 ? 28.878  60.460  -30.387 1.00 91.00  ? 923  VAL   B N   1 
ATOM   7205  C  CA  . VAL   B 2 619 ? 27.740  59.551  -30.313 1.00 90.63  ? 923  VAL   B CA  1 
ATOM   7206  C  C   . VAL   B 2 619 ? 28.211  58.224  -29.717 1.00 93.38  ? 923  VAL   B C   1 
ATOM   7207  O  O   . VAL   B 2 619 ? 29.271  57.708  -30.085 1.00 94.95  ? 923  VAL   B O   1 
ATOM   7208  C  CB  . VAL   B 2 619 ? 27.105  59.346  -31.707 1.00 90.38  ? 923  VAL   B CB  1 
ATOM   7209  C  CG1 . VAL   B 2 619 ? 26.100  58.232  -31.688 1.00 87.91  ? 923  VAL   B CG1 1 
ATOM   7210  C  CG2 . VAL   B 2 619 ? 26.450  60.621  -32.194 1.00 93.55  ? 923  VAL   B CG2 1 
ATOM   7211  N  N   . GLY   B 2 620 ? 27.433  57.677  -28.784 1.00 91.96  ? 924  GLY   B N   1 
ATOM   7212  C  CA  . GLY   B 2 620 ? 27.752  56.385  -28.199 1.00 87.22  ? 924  GLY   B CA  1 
ATOM   7213  C  C   . GLY   B 2 620 ? 26.502  55.630  -27.796 1.00 90.33  ? 924  GLY   B C   1 
ATOM   7214  O  O   . GLY   B 2 620 ? 25.426  56.214  -27.629 1.00 91.57  ? 924  GLY   B O   1 
ATOM   7215  N  N   . ASP   B 2 621 ? 26.646  54.315  -27.658 1.00 91.43  ? 925  ASP   B N   1 
ATOM   7216  C  CA  . ASP   B 2 621 ? 25.534  53.513  -27.161 1.00 88.87  ? 925  ASP   B CA  1 
ATOM   7217  C  C   . ASP   B 2 621 ? 25.958  52.796  -25.892 1.00 86.79  ? 925  ASP   B C   1 
ATOM   7218  O  O   . ASP   B 2 621 ? 27.056  53.002  -25.365 1.00 84.66  ? 925  ASP   B O   1 
ATOM   7219  C  CB  . ASP   B 2 621 ? 25.031  52.519  -28.210 1.00 83.53  ? 925  ASP   B CB  1 
ATOM   7220  C  CG  . ASP   B 2 621 ? 26.096  51.567  -28.654 1.00 87.53  ? 925  ASP   B CG  1 
ATOM   7221  O  OD1 . ASP   B 2 621 ? 27.270  51.794  -28.274 1.00 86.50  ? 925  ASP   B OD1 1 
ATOM   7222  O  OD2 . ASP   B 2 621 ? 25.764  50.597  -29.383 1.00 92.19  ? 925  ASP   B OD2 1 
ATOM   7223  N  N   . LEU   B 2 622 ? 25.069  51.930  -25.418 1.00 85.40  ? 926  LEU   B N   1 
ATOM   7224  C  CA  . LEU   B 2 622 ? 25.290  51.220  -24.173 1.00 80.49  ? 926  LEU   B CA  1 
ATOM   7225  C  C   . LEU   B 2 622 ? 26.501  50.306  -24.218 1.00 83.77  ? 926  LEU   B C   1 
ATOM   7226  O  O   . LEU   B 2 622 ? 26.885  49.781  -23.169 1.00 85.64  ? 926  LEU   B O   1 
ATOM   7227  C  CB  . LEU   B 2 622 ? 24.049  50.407  -23.841 1.00 83.23  ? 926  LEU   B CB  1 
ATOM   7228  C  CG  . LEU   B 2 622 ? 23.707  50.210  -22.371 1.00 77.66  ? 926  LEU   B CG  1 
ATOM   7229  C  CD1 . LEU   B 2 622 ? 23.381  51.528  -21.733 1.00 77.75  ? 926  LEU   B CD1 1 
ATOM   7230  C  CD2 . LEU   B 2 622 ? 22.526  49.291  -22.286 1.00 80.12  ? 926  LEU   B CD2 1 
ATOM   7231  N  N   . MET   B 2 623 ? 27.105  50.091  -25.389 1.00 87.46  ? 927  MET   B N   1 
ATOM   7232  C  CA  . MET   B 2 623 ? 28.106  49.043  -25.566 1.00 84.20  ? 927  MET   B CA  1 
ATOM   7233  C  C   . MET   B 2 623 ? 29.478  49.605  -25.960 1.00 86.42  ? 927  MET   B C   1 
ATOM   7234  O  O   . MET   B 2 623 ? 30.255  48.958  -26.680 1.00 86.96  ? 927  MET   B O   1 
ATOM   7235  C  CB  . MET   B 2 623 ? 27.605  48.003  -26.567 1.00 83.27  ? 927  MET   B CB  1 
ATOM   7236  C  CG  . MET   B 2 623 ? 26.539  47.055  -25.975 1.00 89.87  ? 927  MET   B CG  1 
ATOM   7237  S  SD  . MET   B 2 623 ? 26.287  45.444  -26.816 1.00 85.39  ? 927  MET   B SD  1 
ATOM   7238  C  CE  . MET   B 2 623 ? 27.691  44.486  -26.232 1.00 80.17  ? 927  MET   B CE  1 
ATOM   7239  N  N   . ARG   B 2 624 ? 29.810  50.788  -25.421 1.00 83.37  ? 928  ARG   B N   1 
ATOM   7240  C  CA  . ARG   B 2 624 ? 31.101  51.449  -25.651 1.00 84.77  ? 928  ARG   B CA  1 
ATOM   7241  C  C   . ARG   B 2 624 ? 31.417  51.561  -27.141 1.00 87.60  ? 928  ARG   B C   1 
ATOM   7242  O  O   . ARG   B 2 624 ? 32.590  51.577  -27.548 1.00 86.54  ? 928  ARG   B O   1 
ATOM   7243  C  CB  . ARG   B 2 624 ? 32.242  50.744  -24.913 1.00 84.22  ? 928  ARG   B CB  1 
ATOM   7244  C  CG  . ARG   B 2 624 ? 33.509  51.589  -24.824 1.00 88.71  ? 928  ARG   B CG  1 
ATOM   7245  C  CD  . ARG   B 2 624 ? 34.648  50.831  -24.148 1.00 95.09  ? 928  ARG   B CD  1 
ATOM   7246  N  NE  . ARG   B 2 624 ? 35.979  51.395  -24.374 1.00 95.84  ? 928  ARG   B NE  1 
ATOM   7247  C  CZ  . ARG   B 2 624 ? 36.449  51.782  -25.555 1.00 103.49 ? 928  ARG   B CZ  1 
ATOM   7248  N  NH1 . ARG   B 2 624 ? 35.666  51.855  -26.626 1.00 100.73 ? 928  ARG   B NH1 1 
ATOM   7249  N  NH2 . ARG   B 2 624 ? 37.741  52.098  -25.666 1.00 111.05 ? 928  ARG   B NH2 1 
ATOM   7250  N  N   . SER   B 2 625 ? 30.365  51.617  -27.962 1.00 86.59  ? 929  SER   B N   1 
ATOM   7251  C  CA  . SER   B 2 625 ? 30.505  52.031  -29.352 1.00 89.21  ? 929  SER   B CA  1 
ATOM   7252  C  C   . SER   B 2 625 ? 30.645  53.544  -29.365 1.00 90.06  ? 929  SER   B C   1 
ATOM   7253  O  O   . SER   B 2 625 ? 29.811  54.253  -28.789 1.00 90.09  ? 929  SER   B O   1 
ATOM   7254  C  CB  . SER   B 2 625 ? 29.308  51.600  -30.202 1.00 91.37  ? 929  SER   B CB  1 
ATOM   7255  O  OG  . SER   B 2 625 ? 29.115  50.190  -30.192 1.00 93.46  ? 929  SER   B OG  1 
ATOM   7256  N  N   . VAL   B 2 626 ? 31.704  54.040  -29.993 1.00 94.66  ? 930  VAL   B N   1 
ATOM   7257  C  CA  . VAL   B 2 626 ? 31.942  55.472  -30.084 1.00 90.99  ? 930  VAL   B CA  1 
ATOM   7258  C  C   . VAL   B 2 626 ? 31.979  55.860  -31.549 1.00 93.74  ? 930  VAL   B C   1 
ATOM   7259  O  O   . VAL   B 2 626 ? 32.501  55.116  -32.383 1.00 100.93 ? 930  VAL   B O   1 
ATOM   7260  C  CB  . VAL   B 2 626 ? 33.243  55.899  -29.385 1.00 87.82  ? 930  VAL   B CB  1 
ATOM   7261  C  CG1 . VAL   B 2 626 ? 33.157  57.350  -29.063 1.00 88.74  ? 930  VAL   B CG1 1 
ATOM   7262  C  CG2 . VAL   B 2 626 ? 33.513  55.041  -28.139 1.00 90.06  ? 930  VAL   B CG2 1 
ATOM   7263  N  N   . LEU   B 2 627 ? 31.441  57.037  -31.849 1.00 93.84  ? 931  LEU   B N   1 
ATOM   7264  C  CA  . LEU   B 2 627 ? 31.305  57.528  -33.219 1.00 93.57  ? 931  LEU   B CA  1 
ATOM   7265  C  C   . LEU   B 2 627 ? 31.409  59.050  -33.189 1.00 101.60 ? 931  LEU   B C   1 
ATOM   7266  O  O   . LEU   B 2 627 ? 30.550  59.731  -32.611 1.00 97.93  ? 931  LEU   B O   1 
ATOM   7267  C  CB  . LEU   B 2 627 ? 29.981  57.053  -33.815 1.00 83.86  ? 931  LEU   B CB  1 
ATOM   7268  C  CG  . LEU   B 2 627 ? 29.408  57.657  -35.087 1.00 86.86  ? 931  LEU   B CG  1 
ATOM   7269  C  CD1 . LEU   B 2 627 ? 28.880  56.572  -36.006 1.00 95.93  ? 931  LEU   B CD1 1 
ATOM   7270  C  CD2 . LEU   B 2 627 ? 28.292  58.637  -34.750 1.00 97.45  ? 931  LEU   B CD2 1 
ATOM   7271  N  N   . LEU   B 2 628 ? 32.470  59.580  -33.791 1.00 102.39 ? 932  LEU   B N   1 
ATOM   7272  C  CA  . LEU   B 2 628 ? 32.740  61.008  -33.807 1.00 98.21  ? 932  LEU   B CA  1 
ATOM   7273  C  C   . LEU   B 2 628 ? 32.260  61.575  -35.138 1.00 102.26 ? 932  LEU   B C   1 
ATOM   7274  O  O   . LEU   B 2 628 ? 32.771  61.196  -36.196 1.00 100.78 ? 932  LEU   B O   1 
ATOM   7275  C  CB  . LEU   B 2 628 ? 34.233  61.280  -33.596 1.00 101.10 ? 932  LEU   B CB  1 
ATOM   7276  C  CG  . LEU   B 2 628 ? 34.607  62.728  -33.258 1.00 108.88 ? 932  LEU   B CG  1 
ATOM   7277  C  CD1 . LEU   B 2 628 ? 33.953  63.158  -31.949 1.00 106.06 ? 932  LEU   B CD1 1 
ATOM   7278  C  CD2 . LEU   B 2 628 ? 36.128  62.941  -33.198 1.00 111.22 ? 932  LEU   B CD2 1 
ATOM   7279  N  N   . LEU   B 2 629 ? 31.253  62.455  -35.083 1.00 104.99 ? 933  LEU   B N   1 
ATOM   7280  C  CA  . LEU   B 2 629 ? 30.739  63.172  -36.244 1.00 104.50 ? 933  LEU   B CA  1 
ATOM   7281  C  C   . LEU   B 2 629 ? 31.280  64.594  -36.259 1.00 105.83 ? 933  LEU   B C   1 
ATOM   7282  O  O   . LEU   B 2 629 ? 31.956  65.045  -35.329 1.00 108.77 ? 933  LEU   B O   1 
ATOM   7283  C  CB  . LEU   B 2 629 ? 29.206  63.198  -36.251 1.00 102.89 ? 933  LEU   B CB  1 
ATOM   7284  C  CG  . LEU   B 2 629 ? 28.537  61.814  -36.273 1.00 98.25  ? 933  LEU   B CG  1 
ATOM   7285  C  CD1 . LEU   B 2 629 ? 27.011  61.922  -36.344 1.00 96.68  ? 933  LEU   B CD1 1 
ATOM   7286  C  CD2 . LEU   B 2 629 ? 29.090  61.002  -37.431 1.00 93.29  ? 933  LEU   B CD2 1 
ATOM   7287  N  N   . ALA   B 2 630 ? 30.966  65.309  -37.336 1.00 111.46 ? 934  ALA   B N   1 
ATOM   7288  C  CA  . ALA   B 2 630 ? 31.281  66.726  -37.438 1.00 111.10 ? 934  ALA   B CA  1 
ATOM   7289  C  C   . ALA   B 2 630 ? 30.313  67.351  -38.427 1.00 109.74 ? 934  ALA   B C   1 
ATOM   7290  O  O   . ALA   B 2 630 ? 30.004  66.748  -39.456 1.00 110.53 ? 934  ALA   B O   1 
ATOM   7291  C  CB  . ALA   B 2 630 ? 32.732  66.953  -37.872 1.00 104.70 ? 934  ALA   B CB  1 
ATOM   7292  N  N   . TYR   B 2 631 ? 29.820  68.545  -38.101 1.00 111.82 ? 935  TYR   B N   1 
ATOM   7293  C  CA  . TYR   B 2 631 ? 28.852  69.249  -38.950 1.00 116.72 ? 935  TYR   B CA  1 
ATOM   7294  C  C   . TYR   B 2 631 ? 29.606  70.187  -39.890 1.00 116.40 ? 935  TYR   B C   1 
ATOM   7295  O  O   . TYR   B 2 631 ? 30.018  71.277  -39.492 1.00 122.52 ? 935  TYR   B O   1 
ATOM   7296  C  CB  . TYR   B 2 631 ? 27.837  70.003  -38.090 1.00 116.20 ? 935  TYR   B CB  1 
ATOM   7297  C  CG  . TYR   B 2 631 ? 27.008  71.031  -38.837 1.00 115.50 ? 935  TYR   B CG  1 
ATOM   7298  C  CD1 . TYR   B 2 631 ? 26.019  70.639  -39.734 1.00 115.01 ? 935  TYR   B CD1 1 
ATOM   7299  C  CD2 . TYR   B 2 631 ? 27.208  72.401  -38.635 1.00 117.76 ? 935  TYR   B CD2 1 
ATOM   7300  C  CE1 . TYR   B 2 631 ? 25.263  71.590  -40.427 1.00 121.75 ? 935  TYR   B CE1 1 
ATOM   7301  C  CE2 . TYR   B 2 631 ? 26.458  73.356  -39.323 1.00 112.64 ? 935  TYR   B CE2 1 
ATOM   7302  C  CZ  . TYR   B 2 631 ? 25.492  72.946  -40.213 1.00 113.77 ? 935  TYR   B CZ  1 
ATOM   7303  O  OH  . TYR   B 2 631 ? 24.752  73.884  -40.884 1.00 113.24 ? 935  TYR   B OH  1 
ATOM   7304  N  N   . LYS   B 2 632 ? 29.785  69.776  -41.141 1.00 115.76 ? 936  LYS   B N   1 
ATOM   7305  C  CA  . LYS   B 2 632 ? 30.449  70.635  -42.121 1.00 119.74 ? 936  LYS   B CA  1 
ATOM   7306  C  C   . LYS   B 2 632 ? 29.588  71.870  -42.389 1.00 123.15 ? 936  LYS   B C   1 
ATOM   7307  O  O   . LYS   B 2 632 ? 28.560  71.750  -43.072 1.00 123.41 ? 936  LYS   B O   1 
ATOM   7308  C  CB  . LYS   B 2 632 ? 30.709  69.855  -43.411 1.00 120.83 ? 936  LYS   B CB  1 
ATOM   7309  N  N   . PRO   B 2 633 ? 29.969  73.066  -41.898 1.00 124.19 ? 937  PRO   B N   1 
ATOM   7310  C  CA  . PRO   B 2 633 ? 29.024  74.211  -41.911 1.00 122.75 ? 937  PRO   B CA  1 
ATOM   7311  C  C   . PRO   B 2 633 ? 28.566  74.636  -43.293 1.00 124.16 ? 937  PRO   B C   1 
ATOM   7312  O  O   . PRO   B 2 633 ? 27.361  74.817  -43.512 1.00 125.04 ? 937  PRO   B O   1 
ATOM   7313  C  CB  . PRO   B 2 633 ? 29.820  75.329  -41.225 1.00 114.99 ? 937  PRO   B CB  1 
ATOM   7314  C  CG  . PRO   B 2 633 ? 30.842  74.609  -40.414 1.00 122.80 ? 937  PRO   B CG  1 
ATOM   7315  C  CD  . PRO   B 2 633 ? 31.236  73.418  -41.237 1.00 121.22 ? 937  PRO   B CD  1 
ATOM   7316  N  N   . MET   B 2 634 ? 29.501  74.832  -44.226 1.00 122.26 ? 938  MET   B N   1 
ATOM   7317  C  CA  . MET   B 2 634 ? 29.125  75.231  -45.580 1.00 127.34 ? 938  MET   B CA  1 
ATOM   7318  C  C   . MET   B 2 634 ? 28.204  74.202  -46.227 1.00 128.88 ? 938  MET   B C   1 
ATOM   7319  O  O   . MET   B 2 634 ? 27.241  74.559  -46.917 1.00 130.05 ? 938  MET   B O   1 
ATOM   7320  C  CB  . MET   B 2 634 ? 30.381  75.434  -46.423 1.00 128.41 ? 938  MET   B CB  1 
ATOM   7321  C  CG  . MET   B 2 634 ? 31.609  75.740  -45.589 1.00 131.48 ? 938  MET   B CG  1 
ATOM   7322  S  SD  . MET   B 2 634 ? 33.034  76.232  -46.568 1.00 143.31 ? 938  MET   B SD  1 
ATOM   7323  C  CE  . MET   B 2 634 ? 34.269  76.509  -45.288 1.00 126.65 ? 938  MET   B CE  1 
ATOM   7324  N  N   . GLU   B 2 635 ? 28.482  72.918  -46.019 1.00 127.05 ? 939  GLU   B N   1 
ATOM   7325  C  CA  . GLU   B 2 635 ? 27.627  71.894  -46.596 1.00 125.03 ? 939  GLU   B CA  1 
ATOM   7326  C  C   . GLU   B 2 635 ? 26.296  71.782  -45.855 1.00 124.91 ? 939  GLU   B C   1 
ATOM   7327  O  O   . GLU   B 2 635 ? 25.241  71.609  -46.471 1.00 124.88 ? 939  GLU   B O   1 
ATOM   7328  C  CB  . GLU   B 2 635 ? 28.349  70.557  -46.600 1.00 122.69 ? 939  GLU   B CB  1 
ATOM   7329  C  CG  . GLU   B 2 635 ? 27.365  69.415  -46.753 1.00 130.20 ? 939  GLU   B CG  1 
ATOM   7330  C  CD  . GLU   B 2 635 ? 26.452  69.546  -47.989 1.00 133.45 ? 939  GLU   B CD  1 
ATOM   7331  O  OE1 . GLU   B 2 635 ? 25.775  68.538  -48.353 1.00 139.16 ? 939  GLU   B OE1 1 
ATOM   7332  O  OE2 . GLU   B 2 635 ? 26.432  70.671  -48.575 1.00 132.96 ? 939  GLU   B OE2 1 
ATOM   7333  N  N   . GLY   B 2 636 ? 26.314  71.872  -44.536 1.00 122.34 ? 940  GLY   B N   1 
ATOM   7334  C  CA  . GLY   B 2 636 ? 25.092  71.606  -43.804 1.00 122.74 ? 940  GLY   B CA  1 
ATOM   7335  C  C   . GLY   B 2 636 ? 24.733  70.137  -43.718 1.00 124.99 ? 940  GLY   B C   1 
ATOM   7336  O  O   . GLY   B 2 636 ? 23.541  69.801  -43.732 1.00 123.71 ? 940  GLY   B O   1 
ATOM   7337  N  N   . ASN   B 2 637 ? 25.734  69.247  -43.649 1.00 127.63 ? 941  ASN   B N   1 
ATOM   7338  C  CA  . ASN   B 2 637 ? 25.573  67.833  -43.317 1.00 125.02 ? 941  ASN   B CA  1 
ATOM   7339  C  C   . ASN   B 2 637 ? 26.636  67.435  -42.292 1.00 124.47 ? 941  ASN   B C   1 
ATOM   7340  O  O   . ASN   B 2 637 ? 27.553  68.205  -41.990 1.00 124.32 ? 941  ASN   B O   1 
ATOM   7341  C  CB  . ASN   B 2 637 ? 25.685  66.935  -44.558 1.00 124.22 ? 941  ASN   B CB  1 
ATOM   7342  C  CG  . ASN   B 2 637 ? 24.627  67.239  -45.605 1.00 128.95 ? 941  ASN   B CG  1 
ATOM   7343  O  OD1 . ASN   B 2 637 ? 23.631  67.915  -45.334 1.00 128.28 ? 941  ASN   B OD1 1 
ATOM   7344  N  ND2 . ASN   B 2 637 ? 24.834  66.727  -46.812 1.00 133.36 ? 941  ASN   B ND2 1 
ATOM   7345  N  N   . PHE   B 2 638 ? 26.514  66.216  -41.756 1.00 115.77 ? 942  PHE   B N   1 
ATOM   7346  C  CA  . PHE   B 2 638 ? 27.516  65.636  -40.869 1.00 110.48 ? 942  PHE   B CA  1 
ATOM   7347  C  C   . PHE   B 2 638 ? 28.441  64.707  -41.657 1.00 111.05 ? 942  PHE   B C   1 
ATOM   7348  O  O   . PHE   B 2 638 ? 28.044  64.073  -42.637 1.00 111.75 ? 942  PHE   B O   1 
ATOM   7349  C  CB  . PHE   B 2 638 ? 26.881  64.838  -39.716 1.00 106.89 ? 942  PHE   B CB  1 
ATOM   7350  C  CG  . PHE   B 2 638 ? 25.716  65.521  -39.029 1.00 105.76 ? 942  PHE   B CG  1 
ATOM   7351  C  CD1 . PHE   B 2 638 ? 24.423  65.340  -39.500 1.00 105.11 ? 942  PHE   B CD1 1 
ATOM   7352  C  CD2 . PHE   B 2 638 ? 25.905  66.293  -37.896 1.00 101.44 ? 942  PHE   B CD2 1 
ATOM   7353  C  CE1 . PHE   B 2 638 ? 23.346  65.923  -38.882 1.00 98.84  ? 942  PHE   B CE1 1 
ATOM   7354  C  CE2 . PHE   B 2 638 ? 24.822  66.887  -37.265 1.00 102.04 ? 942  PHE   B CE2 1 
ATOM   7355  C  CZ  . PHE   B 2 638 ? 23.541  66.696  -37.759 1.00 103.01 ? 942  PHE   B CZ  1 
ATOM   7356  N  N   . GLU   B 2 639 ? 29.690  64.624  -41.204 1.00 110.10 ? 943  GLU   B N   1 
ATOM   7357  C  CA  . GLU   B 2 639 ? 30.683  63.749  -41.812 1.00 105.04 ? 943  GLU   B CA  1 
ATOM   7358  C  C   . GLU   B 2 639 ? 31.375  62.941  -40.726 1.00 105.11 ? 943  GLU   B C   1 
ATOM   7359  O  O   . GLU   B 2 639 ? 31.876  63.511  -39.753 1.00 108.42 ? 943  GLU   B O   1 
ATOM   7360  C  CB  . GLU   B 2 639 ? 31.712  64.550  -42.615 1.00 103.35 ? 943  GLU   B CB  1 
ATOM   7361  N  N   . GLU   B 2 640 ? 31.407  61.620  -40.907 1.00 103.86 ? 944  GLU   B N   1 
ATOM   7362  C  CA  . GLU   B 2 640 ? 32.013  60.711  -39.940 1.00 103.71 ? 944  GLU   B CA  1 
ATOM   7363  C  C   . GLU   B 2 640 ? 33.502  60.977  -39.834 1.00 102.14 ? 944  GLU   B C   1 
ATOM   7364  O  O   . GLU   B 2 640 ? 34.224  60.871  -40.827 1.00 107.78 ? 944  GLU   B O   1 
ATOM   7365  C  CB  . GLU   B 2 640 ? 31.776  59.259  -40.360 1.00 102.49 ? 944  GLU   B CB  1 
ATOM   7366  N  N   . ILE   B 2 641 ? 33.967  61.321  -38.642 1.00 104.38 ? 945  ILE   B N   1 
ATOM   7367  C  CA  . ILE   B 2 641 ? 35.398  61.528  -38.449 1.00 107.98 ? 945  ILE   B CA  1 
ATOM   7368  C  C   . ILE   B 2 641 ? 36.092  60.240  -38.024 1.00 112.15 ? 945  ILE   B C   1 
ATOM   7369  O  O   . ILE   B 2 641 ? 37.152  59.899  -38.556 1.00 113.30 ? 945  ILE   B O   1 
ATOM   7370  C  CB  . ILE   B 2 641 ? 35.648  62.668  -37.437 1.00 109.34 ? 945  ILE   B CB  1 
ATOM   7371  C  CG1 . ILE   B 2 641 ? 35.056  63.992  -37.936 1.00 105.77 ? 945  ILE   B CG1 1 
ATOM   7372  C  CG2 . ILE   B 2 641 ? 37.138  62.794  -37.135 1.00 108.79 ? 945  ILE   B CG2 1 
ATOM   7373  C  CD1 . ILE   B 2 641 ? 35.685  65.240  -37.306 1.00 116.74 ? 945  ILE   B CD1 1 
ATOM   7374  N  N   . ALA   B 2 642 ? 35.514  59.508  -37.070 1.00 117.57 ? 946  ALA   B N   1 
ATOM   7375  C  CA  . ALA   B 2 642 ? 36.136  58.295  -36.546 1.00 119.00 ? 946  ALA   B CA  1 
ATOM   7376  C  C   . ALA   B 2 642 ? 35.118  57.504  -35.730 1.00 116.85 ? 946  ALA   B C   1 
ATOM   7377  O  O   . ALA   B 2 642 ? 34.047  58.002  -35.374 1.00 114.01 ? 946  ALA   B O   1 
ATOM   7378  C  CB  . ALA   B 2 642 ? 37.372  58.624  -35.700 1.00 124.75 ? 946  ALA   B CB  1 
ATOM   7379  N  N   . ARG   B 2 643 ? 35.482  56.257  -35.433 1.00 119.14 ? 947  ARG   B N   1 
ATOM   7380  C  CA  . ARG   B 2 643 ? 34.638  55.327  -34.691 1.00 111.76 ? 947  ARG   B CA  1 
ATOM   7381  C  C   . ARG   B 2 643 ? 35.545  54.333  -33.979 1.00 111.99 ? 947  ARG   B C   1 
ATOM   7382  O  O   . ARG   B 2 643 ? 36.714  54.164  -34.333 1.00 115.58 ? 947  ARG   B O   1 
ATOM   7383  C  CB  . ARG   B 2 643 ? 33.640  54.593  -35.605 1.00 93.08  ? 947  ARG   B CB  1 
ATOM   7384  N  N   . ASP   B 2 644 ? 34.997  53.695  -32.952 1.00 108.02 ? 948  ASP   B N   1 
ATOM   7385  C  CA  . ASP   B 2 644 ? 35.665  52.580  -32.300 1.00 107.32 ? 948  ASP   B CA  1 
ATOM   7386  C  C   . ASP   B 2 644 ? 34.575  51.674  -31.766 1.00 104.63 ? 948  ASP   B C   1 
ATOM   7387  O  O   . ASP   B 2 644 ? 33.514  52.152  -31.357 1.00 103.12 ? 948  ASP   B O   1 
ATOM   7388  C  CB  . ASP   B 2 644 ? 36.609  53.035  -31.172 1.00 111.10 ? 948  ASP   B CB  1 
ATOM   7389  C  CG  . ASP   B 2 644 ? 37.433  51.881  -30.579 1.00 114.93 ? 948  ASP   B CG  1 
ATOM   7390  O  OD1 . ASP   B 2 644 ? 38.071  51.134  -31.355 1.00 114.79 ? 948  ASP   B OD1 1 
ATOM   7391  O  OD2 . ASP   B 2 644 ? 37.461  51.731  -29.333 1.00 118.71 ? 948  ASP   B OD2 1 
ATOM   7392  N  N   . PHE   B 2 645 ? 34.822  50.369  -31.836 1.00 100.74 ? 949  PHE   B N   1 
ATOM   7393  C  CA  . PHE   B 2 645 ? 33.959  49.353  -31.237 1.00 101.21 ? 949  PHE   B CA  1 
ATOM   7394  C  C   . PHE   B 2 645 ? 34.853  48.498  -30.344 1.00 100.40 ? 949  PHE   B C   1 
ATOM   7395  O  O   . PHE   B 2 645 ? 35.669  47.710  -30.837 1.00 101.41 ? 949  PHE   B O   1 
ATOM   7396  C  CB  . PHE   B 2 645 ? 33.259  48.488  -32.290 1.00 103.20 ? 949  PHE   B CB  1 
ATOM   7397  C  CG  . PHE   B 2 645 ? 32.374  49.256  -33.256 1.00 106.06 ? 949  PHE   B CG  1 
ATOM   7398  C  CD1 . PHE   B 2 645 ? 31.387  50.116  -32.796 1.00 105.43 ? 949  PHE   B CD1 1 
ATOM   7399  C  CD2 . PHE   B 2 645 ? 32.524  49.092  -34.634 1.00 100.40 ? 949  PHE   B CD2 1 
ATOM   7400  C  CE1 . PHE   B 2 645 ? 30.576  50.806  -33.691 1.00 105.73 ? 949  PHE   B CE1 1 
ATOM   7401  C  CE2 . PHE   B 2 645 ? 31.720  49.770  -35.526 1.00 100.32 ? 949  PHE   B CE2 1 
ATOM   7402  C  CZ  . PHE   B 2 645 ? 30.741  50.628  -35.054 1.00 109.41 ? 949  PHE   B CZ  1 
ATOM   7403  N  N   . ASN   B 2 646 ? 34.715  48.665  -29.034 1.00 98.81  ? 950  ASN   B N   1 
ATOM   7404  C  CA  . ASN   B 2 646 ? 35.366  47.804  -28.054 1.00 91.91  ? 950  ASN   B CA  1 
ATOM   7405  C  C   . ASN   B 2 646 ? 34.263  47.380  -27.087 1.00 88.68  ? 950  ASN   B C   1 
ATOM   7406  O  O   . ASN   B 2 646 ? 34.109  47.961  -25.999 1.00 91.05  ? 950  ASN   B O   1 
ATOM   7407  C  CB  . ASN   B 2 646 ? 36.530  48.525  -27.376 1.00 95.14  ? 950  ASN   B CB  1 
ATOM   7408  C  CG  . ASN   B 2 646 ? 37.054  47.764  -26.190 1.00 103.76 ? 950  ASN   B CG  1 
ATOM   7409  O  OD1 . ASN   B 2 646 ? 36.798  48.132  -25.031 1.00 104.40 ? 950  ASN   B OD1 1 
ATOM   7410  N  ND2 . ASN   B 2 646 ? 37.772  46.676  -26.459 1.00 110.09 ? 950  ASN   B ND2 1 
ATOM   7411  N  N   . PRO   B 2 647 ? 33.490  46.358  -27.446 1.00 85.38  ? 951  PRO   B N   1 
ATOM   7412  C  CA  . PRO   B 2 647 ? 32.202  46.121  -26.786 1.00 84.75  ? 951  PRO   B CA  1 
ATOM   7413  C  C   . PRO   B 2 647 ? 32.348  45.871  -25.294 1.00 85.96  ? 951  PRO   B C   1 
ATOM   7414  O  O   . PRO   B 2 647 ? 33.243  45.151  -24.852 1.00 88.19  ? 951  PRO   B O   1 
ATOM   7415  C  CB  . PRO   B 2 647 ? 31.662  44.884  -27.514 1.00 87.69  ? 951  PRO   B CB  1 
ATOM   7416  C  CG  . PRO   B 2 647 ? 32.433  44.799  -28.771 1.00 87.12  ? 951  PRO   B CG  1 
ATOM   7417  C  CD  . PRO   B 2 647 ? 33.796  45.316  -28.431 1.00 89.47  ? 951  PRO   B CD  1 
ATOM   7418  N  N   . ASN   B 2 648 ? 31.427  46.460  -24.534 1.00 85.27  ? 952  ASN   B N   1 
ATOM   7419  C  CA  . ASN   B 2 648 ? 31.397  46.552  -23.084 1.00 83.70  ? 952  ASN   B CA  1 
ATOM   7420  C  C   . ASN   B 2 648 ? 30.259  47.515  -22.731 1.00 86.15  ? 952  ASN   B C   1 
ATOM   7421  O  O   . ASN   B 2 648 ? 29.846  48.337  -23.562 1.00 86.08  ? 952  ASN   B O   1 
ATOM   7422  C  CB  . ASN   B 2 648 ? 32.726  47.050  -22.491 1.00 81.93  ? 952  ASN   B CB  1 
ATOM   7423  C  CG  . ASN   B 2 648 ? 32.832  46.814  -20.988 1.00 84.48  ? 952  ASN   B CG  1 
ATOM   7424  O  OD1 . ASN   B 2 648 ? 32.058  46.057  -20.400 1.00 86.11  ? 952  ASN   B OD1 1 
ATOM   7425  N  ND2 . ASN   B 2 648 ? 33.814  47.453  -20.362 1.00 84.62  ? 952  ASN   B ND2 1 
ATOM   7426  N  N   . TRP   B 2 649 ? 29.753  47.414  -21.509 1.00 80.41  ? 953  TRP   B N   1 
ATOM   7427  C  CA  . TRP   B 2 649 ? 28.705  48.320  -21.054 1.00 74.54  ? 953  TRP   B CA  1 
ATOM   7428  C  C   . TRP   B 2 649 ? 29.312  49.672  -20.704 1.00 84.18  ? 953  TRP   B C   1 
ATOM   7429  O  O   . TRP   B 2 649 ? 30.259  49.747  -19.918 1.00 85.47  ? 953  TRP   B O   1 
ATOM   7430  C  CB  . TRP   B 2 649 ? 27.957  47.763  -19.844 1.00 75.63  ? 953  TRP   B CB  1 
ATOM   7431  C  CG  . TRP   B 2 649 ? 27.412  46.375  -19.993 1.00 82.60  ? 953  TRP   B CG  1 
ATOM   7432  C  CD1 . TRP   B 2 649 ? 27.684  45.314  -19.181 1.00 86.91  ? 953  TRP   B CD1 1 
ATOM   7433  C  CD2 . TRP   B 2 649 ? 26.478  45.888  -20.979 1.00 92.45  ? 953  TRP   B CD2 1 
ATOM   7434  N  NE1 . TRP   B 2 649 ? 26.999  44.192  -19.598 1.00 87.66  ? 953  TRP   B NE1 1 
ATOM   7435  C  CE2 . TRP   B 2 649 ? 26.254  44.513  -20.700 1.00 88.74  ? 953  TRP   B CE2 1 
ATOM   7436  C  CE3 . TRP   B 2 649 ? 25.825  46.469  -22.081 1.00 87.62  ? 953  TRP   B CE3 1 
ATOM   7437  C  CZ2 . TRP   B 2 649 ? 25.407  43.716  -21.476 1.00 89.00  ? 953  TRP   B CZ2 1 
ATOM   7438  C  CZ3 . TRP   B 2 649 ? 24.977  45.670  -22.851 1.00 83.48  ? 953  TRP   B CZ3 1 
ATOM   7439  C  CH2 . TRP   B 2 649 ? 24.776  44.312  -22.541 1.00 89.15  ? 953  TRP   B CH2 1 
ATOM   7440  N  N   . MET   B 2 650 ? 28.740  50.735  -21.277 1.00 85.35  ? 954  MET   B N   1 
ATOM   7441  C  CA  . MET   B 2 650 ? 29.125  52.125  -21.065 1.00 81.62  ? 954  MET   B CA  1 
ATOM   7442  C  C   . MET   B 2 650 ? 27.940  52.888  -20.483 1.00 78.78  ? 954  MET   B C   1 
ATOM   7443  O  O   . MET   B 2 650 ? 26.814  52.734  -20.957 1.00 81.44  ? 954  MET   B O   1 
ATOM   7444  C  CB  . MET   B 2 650 ? 29.554  52.730  -22.392 1.00 82.61  ? 954  MET   B CB  1 
ATOM   7445  C  CG  . MET   B 2 650 ? 30.053  54.148  -22.322 1.00 86.68  ? 954  MET   B CG  1 
ATOM   7446  S  SD  . MET   B 2 650 ? 30.888  54.643  -23.867 1.00 84.29  ? 954  MET   B SD  1 
ATOM   7447  C  CE  . MET   B 2 650 ? 29.467  55.094  -24.887 1.00 86.78  ? 954  MET   B CE  1 
ATOM   7448  N  N   . SER   B 2 651 ? 28.182  53.703  -19.463 1.00 74.73  ? 955  SER   B N   1 
ATOM   7449  C  CA  . SER   B 2 651 ? 27.096  54.347  -18.743 1.00 81.37  ? 955  SER   B CA  1 
ATOM   7450  C  C   . SER   B 2 651 ? 27.073  55.864  -18.887 1.00 90.64  ? 955  SER   B C   1 
ATOM   7451  O  O   . SER   B 2 651 ? 26.107  56.505  -18.445 1.00 88.58  ? 955  SER   B O   1 
ATOM   7452  C  CB  . SER   B 2 651 ? 27.174  54.000  -17.247 1.00 81.11  ? 955  SER   B CB  1 
ATOM   7453  O  OG  . SER   B 2 651 ? 28.380  54.485  -16.661 1.00 83.81  ? 955  SER   B OG  1 
ATOM   7454  N  N   . ALA   B 2 652 ? 28.093  56.452  -19.498 1.00 88.25  ? 956  ALA   B N   1 
ATOM   7455  C  CA  . ALA   B 2 652 ? 28.327  57.877  -19.385 1.00 83.65  ? 956  ALA   B CA  1 
ATOM   7456  C  C   . ALA   B 2 652 ? 29.606  58.163  -20.142 1.00 88.73  ? 956  ALA   B C   1 
ATOM   7457  O  O   . ALA   B 2 652 ? 30.480  57.298  -20.262 1.00 86.50  ? 956  ALA   B O   1 
ATOM   7458  C  CB  . ALA   B 2 652 ? 28.445  58.326  -17.928 1.00 79.50  ? 956  ALA   B CB  1 
ATOM   7459  N  N   . VAL   B 2 653 ? 29.724  59.394  -20.622 1.00 91.27  ? 957  VAL   B N   1 
ATOM   7460  C  CA  . VAL   B 2 653 ? 30.742  59.716  -21.615 1.00 89.24  ? 957  VAL   B CA  1 
ATOM   7461  C  C   . VAL   B 2 653 ? 30.790  61.223  -21.788 1.00 95.10  ? 957  VAL   B C   1 
ATOM   7462  O  O   . VAL   B 2 653 ? 29.761  61.883  -21.727 1.00 98.10  ? 957  VAL   B O   1 
ATOM   7463  C  CB  . VAL   B 2 653 ? 30.414  58.989  -22.929 1.00 89.32  ? 957  VAL   B CB  1 
ATOM   7464  C  CG1 . VAL   B 2 653 ? 29.317  59.733  -23.648 1.00 87.56  ? 957  VAL   B CG1 1 
ATOM   7465  C  CG2 . VAL   B 2 653 ? 31.643  58.793  -23.782 1.00 87.16  ? 957  VAL   B CG2 1 
ATOM   7466  N  N   . GLU   B 2 654 ? 31.987  61.776  -22.001 1.00 99.98  ? 958  GLU   B N   1 
ATOM   7467  C  CA  . GLU   B 2 654 ? 32.136  63.225  -22.006 1.00 102.88 ? 958  GLU   B CA  1 
ATOM   7468  C  C   . GLU   B 2 654 ? 33.329  63.619  -22.870 1.00 104.75 ? 958  GLU   B C   1 
ATOM   7469  O  O   . GLU   B 2 654 ? 34.287  62.849  -23.017 1.00 104.60 ? 958  GLU   B O   1 
ATOM   7470  C  CB  . GLU   B 2 654 ? 32.314  63.740  -20.576 1.00 102.52 ? 958  GLU   B CB  1 
ATOM   7471  C  CG  . GLU   B 2 654 ? 32.459  65.234  -20.494 1.00 102.39 ? 958  GLU   B CG  1 
ATOM   7472  C  CD  . GLU   B 2 654 ? 31.272  65.928  -21.105 1.00 103.72 ? 958  GLU   B CD  1 
ATOM   7473  O  OE1 . GLU   B 2 654 ? 30.117  65.572  -20.752 1.00 103.20 ? 958  GLU   B OE1 1 
ATOM   7474  O  OE2 . GLU   B 2 654 ? 31.497  66.817  -21.952 1.00 106.33 ? 958  GLU   B OE2 1 
ATOM   7475  N  N   . ILE   B 2 655 ? 33.274  64.831  -23.435 1.00 97.00  ? 959  ILE   B N   1 
ATOM   7476  C  CA  . ILE   B 2 655 ? 34.364  65.335  -24.273 1.00 102.56 ? 959  ILE   B CA  1 
ATOM   7477  C  C   . ILE   B 2 655 ? 35.359  66.092  -23.396 1.00 102.77 ? 959  ILE   B C   1 
ATOM   7478  O  O   . ILE   B 2 655 ? 35.026  67.111  -22.776 1.00 98.18  ? 959  ILE   B O   1 
ATOM   7479  C  CB  . ILE   B 2 655 ? 33.845  66.214  -25.424 1.00 99.66  ? 959  ILE   B CB  1 
ATOM   7480  C  CG1 . ILE   B 2 655 ? 32.806  65.449  -26.250 1.00 98.05  ? 959  ILE   B CG1 1 
ATOM   7481  C  CG2 . ILE   B 2 655 ? 35.000  66.648  -26.331 1.00 99.35  ? 959  ILE   B CG2 1 
ATOM   7482  C  CD1 . ILE   B 2 655 ? 32.702  65.882  -27.690 1.00 92.13  ? 959  ILE   B CD1 1 
ATOM   7483  N  N   . LEU   B 2 656 ? 36.581  65.569  -23.322 1.00 101.47 ? 960  LEU   B N   1 
ATOM   7484  C  CA  . LEU   B 2 656 ? 37.661  66.240  -22.619 1.00 100.94 ? 960  LEU   B CA  1 
ATOM   7485  C  C   . LEU   B 2 656 ? 38.164  67.413  -23.446 1.00 105.91 ? 960  LEU   B C   1 
ATOM   7486  O  O   . LEU   B 2 656 ? 38.039  68.568  -23.032 1.00 107.00 ? 960  LEU   B O   1 
ATOM   7487  C  CB  . LEU   B 2 656 ? 38.784  65.252  -22.328 1.00 101.50 ? 960  LEU   B CB  1 
ATOM   7488  C  CG  . LEU   B 2 656 ? 38.341  64.349  -21.194 1.00 100.78 ? 960  LEU   B CG  1 
ATOM   7489  C  CD1 . LEU   B 2 656 ? 39.538  63.721  -20.475 1.00 102.01 ? 960  LEU   B CD1 1 
ATOM   7490  C  CD2 . LEU   B 2 656 ? 37.479  65.186  -20.250 1.00 94.84  ? 960  LEU   B CD2 1 
ATOM   7491  N  N   . ASP   B 2 657 ? 38.739  67.117  -24.615 1.00 108.55 ? 961  ASP   B N   1 
ATOM   7492  C  CA  . ASP   B 2 657 ? 39.083  68.141  -25.594 1.00 109.49 ? 961  ASP   B CA  1 
ATOM   7493  C  C   . ASP   B 2 657 ? 38.674  67.679  -26.989 1.00 109.54 ? 961  ASP   B C   1 
ATOM   7494  O  O   . ASP   B 2 657 ? 37.982  66.665  -27.130 1.00 112.33 ? 961  ASP   B O   1 
ATOM   7495  C  CB  . ASP   B 2 657 ? 40.580  68.491  -25.523 1.00 115.30 ? 961  ASP   B CB  1 
ATOM   7496  C  CG  . ASP   B 2 657 ? 41.495  67.299  -25.771 1.00 112.73 ? 961  ASP   B CG  1 
ATOM   7497  O  OD1 . ASP   B 2 657 ? 41.068  66.335  -26.445 1.00 111.23 ? 961  ASP   B OD1 1 
ATOM   7498  O  OD2 . ASP   B 2 657 ? 42.656  67.342  -25.288 1.00 113.94 ? 961  ASP   B OD2 1 
ATOM   7499  N  N   . ASP   B 2 658 ? 39.068  68.408  -28.022 1.00 111.34 ? 962  ASP   B N   1 
ATOM   7500  C  CA  . ASP   B 2 658 ? 38.638  68.021  -29.359 1.00 116.28 ? 962  ASP   B CA  1 
ATOM   7501  C  C   . ASP   B 2 658 ? 39.226  66.698  -29.836 1.00 117.52 ? 962  ASP   B C   1 
ATOM   7502  O  O   . ASP   B 2 658 ? 38.859  66.254  -30.935 1.00 121.93 ? 962  ASP   B O   1 
ATOM   7503  C  CB  . ASP   B 2 658 ? 38.994  69.124  -30.342 1.00 120.99 ? 962  ASP   B CB  1 
ATOM   7504  C  CG  . ASP   B 2 658 ? 38.489  70.457  -29.905 1.00 124.89 ? 962  ASP   B CG  1 
ATOM   7505  O  OD1 . ASP   B 2 658 ? 39.129  71.076  -29.023 1.00 122.78 ? 962  ASP   B OD1 1 
ATOM   7506  O  OD2 . ASP   B 2 658 ? 37.430  70.867  -30.423 1.00 127.60 ? 962  ASP   B OD2 1 
ATOM   7507  N  N   . ASP   B 2 659 ? 40.108  66.059  -29.075 1.00 112.53 ? 963  ASP   B N   1 
ATOM   7508  C  CA  . ASP   B 2 659 ? 40.772  64.853  -29.566 1.00 113.27 ? 963  ASP   B CA  1 
ATOM   7509  C  C   . ASP   B 2 659 ? 40.601  63.716  -28.582 1.00 110.91 ? 963  ASP   B C   1 
ATOM   7510  O  O   . ASP   B 2 659 ? 40.530  62.552  -28.984 1.00 112.69 ? 963  ASP   B O   1 
ATOM   7511  C  CB  . ASP   B 2 659 ? 42.266  65.110  -29.810 1.00 119.48 ? 963  ASP   B CB  1 
ATOM   7512  C  CG  . ASP   B 2 659 ? 42.526  66.360  -30.642 1.00 125.62 ? 963  ASP   B CG  1 
ATOM   7513  O  OD1 . ASP   B 2 659 ? 42.119  67.448  -30.182 1.00 125.89 ? 963  ASP   B OD1 1 
ATOM   7514  O  OD2 . ASP   B 2 659 ? 43.122  66.271  -31.749 1.00 128.32 ? 963  ASP   B OD2 1 
ATOM   7515  N  N   . ASN   B 2 660 ? 40.559  64.031  -27.291 1.00 113.61 ? 964  ASN   B N   1 
ATOM   7516  C  CA  . ASN   B 2 660 ? 40.389  63.034  -26.247 1.00 108.20 ? 964  ASN   B CA  1 
ATOM   7517  C  C   . ASN   B 2 660 ? 38.940  62.961  -25.791 1.00 106.25 ? 964  ASN   B C   1 
ATOM   7518  O  O   . ASN   B 2 660 ? 38.209  63.951  -25.812 1.00 105.35 ? 964  ASN   B O   1 
ATOM   7519  C  CB  . ASN   B 2 660 ? 41.287  63.325  -25.048 1.00 104.73 ? 964  ASN   B CB  1 
ATOM   7520  C  CG  . ASN   B 2 660 ? 42.749  63.329  -25.420 1.00 107.55 ? 964  ASN   B CG  1 
ATOM   7521  O  OD1 . ASN   B 2 660 ? 43.404  62.291  -25.421 1.00 109.30 ? 964  ASN   B OD1 1 
ATOM   7522  N  ND2 . ASN   B 2 660 ? 43.270  64.504  -25.753 1.00 110.49 ? 964  ASN   B ND2 1 
ATOM   7523  N  N   . PHE   B 2 661 ? 38.528  61.769  -25.383 1.00 108.62 ? 965  PHE   B N   1 
ATOM   7524  C  CA  . PHE   B 2 661 ? 37.164  61.523  -24.943 1.00 105.96 ? 965  PHE   B CA  1 
ATOM   7525  C  C   . PHE   B 2 661 ? 37.189  60.656  -23.688 1.00 103.27 ? 965  PHE   B C   1 
ATOM   7526  O  O   . PHE   B 2 661 ? 38.000  59.729  -23.578 1.00 102.02 ? 965  PHE   B O   1 
ATOM   7527  C  CB  . PHE   B 2 661 ? 36.343  60.863  -26.072 1.00 105.68 ? 965  PHE   B CB  1 
ATOM   7528  C  CG  . PHE   B 2 661 ? 36.546  61.508  -27.418 1.00 108.06 ? 965  PHE   B CG  1 
ATOM   7529  C  CD1 . PHE   B 2 661 ? 36.201  62.837  -27.625 1.00 108.70 ? 965  PHE   B CD1 1 
ATOM   7530  C  CD2 . PHE   B 2 661 ? 37.093  60.795  -28.469 1.00 107.09 ? 965  PHE   B CD2 1 
ATOM   7531  C  CE1 . PHE   B 2 661 ? 36.394  63.436  -28.858 1.00 109.25 ? 965  PHE   B CE1 1 
ATOM   7532  C  CE2 . PHE   B 2 661 ? 37.282  61.395  -29.707 1.00 109.79 ? 965  PHE   B CE2 1 
ATOM   7533  C  CZ  . PHE   B 2 661 ? 36.932  62.713  -29.898 1.00 109.82 ? 965  PHE   B CZ  1 
ATOM   7534  N  N   . LEU   B 2 662 ? 36.320  60.983  -22.731 1.00 100.49 ? 966  LEU   B N   1 
ATOM   7535  C  CA  . LEU   B 2 662 ? 36.284  60.312  -21.441 1.00 94.78  ? 966  LEU   B CA  1 
ATOM   7536  C  C   . LEU   B 2 662 ? 34.992  59.525  -21.296 1.00 93.51  ? 966  LEU   B C   1 
ATOM   7537  O  O   . LEU   B 2 662 ? 33.942  59.933  -21.801 1.00 90.90  ? 966  LEU   B O   1 
ATOM   7538  C  CB  . LEU   B 2 662 ? 36.395  61.302  -20.281 1.00 90.96  ? 966  LEU   B CB  1 
ATOM   7539  C  CG  . LEU   B 2 662 ? 36.280  60.634  -18.909 1.00 89.19  ? 966  LEU   B CG  1 
ATOM   7540  C  CD1 . LEU   B 2 662 ? 37.516  59.771  -18.632 1.00 86.89  ? 966  LEU   B CD1 1 
ATOM   7541  C  CD2 . LEU   B 2 662 ? 36.049  61.672  -17.814 1.00 90.27  ? 966  LEU   B CD2 1 
ATOM   7542  N  N   . GLY   B 2 663 ? 35.074  58.406  -20.571 1.00 93.53  ? 967  GLY   B N   1 
ATOM   7543  C  CA  . GLY   B 2 663 ? 33.921  57.537  -20.425 1.00 90.10  ? 967  GLY   B CA  1 
ATOM   7544  C  C   . GLY   B 2 663 ? 33.993  56.645  -19.209 1.00 84.36  ? 967  GLY   B C   1 
ATOM   7545  O  O   . GLY   B 2 663 ? 35.070  56.380  -18.665 1.00 84.58  ? 967  GLY   B O   1 
ATOM   7546  N  N   . ALA   B 2 664 ? 32.815  56.178  -18.793 1.00 83.19  ? 968  ALA   B N   1 
ATOM   7547  C  CA  . ALA   B 2 664 ? 32.654  55.205  -17.719 1.00 84.36  ? 968  ALA   B CA  1 
ATOM   7548  C  C   . ALA   B 2 664 ? 32.113  53.896  -18.279 1.00 87.93  ? 968  ALA   B C   1 
ATOM   7549  O  O   . ALA   B 2 664 ? 31.068  53.890  -18.946 1.00 88.18  ? 968  ALA   B O   1 
ATOM   7550  C  CB  . ALA   B 2 664 ? 31.703  55.731  -16.643 1.00 82.68  ? 968  ALA   B CB  1 
ATOM   7551  N  N   . GLU   B 2 665 ? 32.807  52.789  -17.995 1.00 86.49  ? 969  GLU   B N   1 
ATOM   7552  C  CA  . GLU   B 2 665 ? 32.361  51.472  -18.440 1.00 89.61  ? 969  GLU   B CA  1 
ATOM   7553  C  C   . GLU   B 2 665 ? 32.486  50.459  -17.308 1.00 87.06  ? 969  GLU   B C   1 
ATOM   7554  O  O   . GLU   B 2 665 ? 33.108  50.717  -16.268 1.00 85.27  ? 969  GLU   B O   1 
ATOM   7555  C  CB  . GLU   B 2 665 ? 33.134  50.983  -19.687 1.00 89.32  ? 969  GLU   B CB  1 
ATOM   7556  C  CG  . GLU   B 2 665 ? 34.646  50.762  -19.529 1.00 91.04  ? 969  GLU   B CG  1 
ATOM   7557  C  CD  . GLU   B 2 665 ? 35.337  50.394  -20.864 1.00 95.46  ? 969  GLU   B CD  1 
ATOM   7558  O  OE1 . GLU   B 2 665 ? 34.647  49.975  -21.834 1.00 101.34 ? 969  GLU   B OE1 1 
ATOM   7559  O  OE2 . GLU   B 2 665 ? 36.580  50.524  -20.959 1.00 97.69  ? 969  GLU   B OE2 1 
ATOM   7560  N  N   . ASN   B 2 666 ? 31.877  49.292  -17.544 1.00 87.70  ? 970  ASN   B N   1 
ATOM   7561  C  CA  . ASN   B 2 666 ? 31.926  48.173  -16.608 1.00 88.01  ? 970  ASN   B CA  1 
ATOM   7562  C  C   . ASN   B 2 666 ? 33.359  47.659  -16.491 1.00 88.18  ? 970  ASN   B C   1 
ATOM   7563  O  O   . ASN   B 2 666 ? 34.114  47.671  -17.468 1.00 87.64  ? 970  ASN   B O   1 
ATOM   7564  C  CB  . ASN   B 2 666 ? 30.967  47.062  -17.080 1.00 79.47  ? 970  ASN   B CB  1 
ATOM   7565  C  CG  . ASN   B 2 666 ? 31.115  45.761  -16.296 1.00 86.78  ? 970  ASN   B CG  1 
ATOM   7566  O  OD1 . ASN   B 2 666 ? 30.464  45.565  -15.263 1.00 86.31  ? 970  ASN   B OD1 1 
ATOM   7567  N  ND2 . ASN   B 2 666 ? 31.942  44.845  -16.813 1.00 90.53  ? 970  ASN   B ND2 1 
ATOM   7568  N  N   . ALA   B 2 667 ? 33.755  47.253  -15.278 1.00 89.30  ? 971  ALA   B N   1 
ATOM   7569  C  CA  . ALA   B 2 667 ? 32.943  47.436  -14.085 1.00 83.91  ? 971  ALA   B CA  1 
ATOM   7570  C  C   . ALA   B 2 667 ? 33.587  48.502  -13.197 1.00 90.40  ? 971  ALA   B C   1 
ATOM   7571  O  O   . ALA   B 2 667 ? 34.676  48.299  -12.630 1.00 88.25  ? 971  ALA   B O   1 
ATOM   7572  C  CB  . ALA   B 2 667 ? 32.782  46.164  -13.357 1.00 72.31  ? 971  ALA   B CB  1 
ATOM   7573  N  N   . PHE   B 2 668 ? 32.905  49.649  -13.095 1.00 88.09  ? 972  PHE   B N   1 
ATOM   7574  C  CA  . PHE   B 2 668 ? 33.381  50.779  -12.304 1.00 81.37  ? 972  PHE   B CA  1 
ATOM   7575  C  C   . PHE   B 2 668 ? 34.750  51.230  -12.801 1.00 84.01  ? 972  PHE   B C   1 
ATOM   7576  O  O   . PHE   B 2 668 ? 35.636  51.598  -12.029 1.00 87.25  ? 972  PHE   B O   1 
ATOM   7577  C  CB  . PHE   B 2 668 ? 33.408  50.441  -10.810 1.00 79.96  ? 972  PHE   B CB  1 
ATOM   7578  C  CG  . PHE   B 2 668 ? 32.217  49.625  -10.347 1.00 83.09  ? 972  PHE   B CG  1 
ATOM   7579  C  CD1 . PHE   B 2 668 ? 31.005  50.231  -10.049 1.00 81.96  ? 972  PHE   B CD1 1 
ATOM   7580  C  CD2 . PHE   B 2 668 ? 32.304  48.244  -10.227 1.00 84.05  ? 972  PHE   B CD2 1 
ATOM   7581  C  CE1 . PHE   B 2 668 ? 29.903  49.473  -9.631  1.00 81.20  ? 972  PHE   B CE1 1 
ATOM   7582  C  CE2 . PHE   B 2 668 ? 31.209  47.490  -9.815  1.00 82.08  ? 972  PHE   B CE2 1 
ATOM   7583  C  CZ  . PHE   B 2 668 ? 30.013  48.108  -9.513  1.00 82.64  ? 972  PHE   B CZ  1 
ATOM   7584  N  N   . ASN   B 2 669 ? 34.927  51.214  -14.114 1.00 83.77  ? 973  ASN   B N   1 
ATOM   7585  C  CA  . ASN   B 2 669 ? 36.161  51.688  -14.719 1.00 86.13  ? 973  ASN   B CA  1 
ATOM   7586  C  C   . ASN   B 2 669 ? 35.892  52.962  -15.507 1.00 86.47  ? 973  ASN   B C   1 
ATOM   7587  O  O   . ASN   B 2 669 ? 34.794  53.174  -16.029 1.00 88.04  ? 973  ASN   B O   1 
ATOM   7588  C  CB  . ASN   B 2 669 ? 36.769  50.643  -15.645 1.00 87.63  ? 973  ASN   B CB  1 
ATOM   7589  C  CG  . ASN   B 2 669 ? 36.904  49.308  -14.987 1.00 89.14  ? 973  ASN   B CG  1 
ATOM   7590  O  OD1 . ASN   B 2 669 ? 37.278  49.217  -13.817 1.00 90.51  ? 973  ASN   B OD1 1 
ATOM   7591  N  ND2 . ASN   B 2 669 ? 36.592  48.248  -15.733 1.00 90.74  ? 973  ASN   B ND2 1 
ATOM   7592  N  N   . LEU   B 2 670 ? 36.910  53.803  -15.585 1.00 86.20  ? 974  LEU   B N   1 
ATOM   7593  C  CA  . LEU   B 2 670 ? 36.965  54.924  -16.502 1.00 83.39  ? 974  LEU   B CA  1 
ATOM   7594  C  C   . LEU   B 2 670 ? 37.918  54.596  -17.639 1.00 87.46  ? 974  LEU   B C   1 
ATOM   7595  O  O   . LEU   B 2 670 ? 38.749  53.688  -17.546 1.00 92.47  ? 974  LEU   B O   1 
ATOM   7596  C  CB  . LEU   B 2 670 ? 37.437  56.176  -15.782 1.00 84.65  ? 974  LEU   B CB  1 
ATOM   7597  C  CG  . LEU   B 2 670 ? 36.459  56.714  -14.770 1.00 82.78  ? 974  LEU   B CG  1 
ATOM   7598  C  CD1 . LEU   B 2 670 ? 37.207  57.758  -14.001 1.00 84.32  ? 974  LEU   B CD1 1 
ATOM   7599  C  CD2 . LEU   B 2 670 ? 35.335  57.342  -15.535 1.00 86.59  ? 974  LEU   B CD2 1 
ATOM   7600  N  N   . PHE   B 2 671 ? 37.808  55.360  -18.715 1.00 88.65  ? 975  PHE   B N   1 
ATOM   7601  C  CA  . PHE   B 2 671 ? 38.659  55.132  -19.873 1.00 91.63  ? 975  PHE   B CA  1 
ATOM   7602  C  C   . PHE   B 2 671 ? 38.642  56.368  -20.757 1.00 92.97  ? 975  PHE   B C   1 
ATOM   7603  O  O   . PHE   B 2 671 ? 37.635  57.077  -20.846 1.00 88.64  ? 975  PHE   B O   1 
ATOM   7604  C  CB  . PHE   B 2 671 ? 38.191  53.927  -20.691 1.00 92.93  ? 975  PHE   B CB  1 
ATOM   7605  C  CG  . PHE   B 2 671 ? 36.990  54.225  -21.552 1.00 89.47  ? 975  PHE   B CG  1 
ATOM   7606  C  CD1 . PHE   B 2 671 ? 37.140  54.753  -22.814 1.00 88.37  ? 975  PHE   B CD1 1 
ATOM   7607  C  CD2 . PHE   B 2 671 ? 35.711  54.013  -21.073 1.00 91.63  ? 975  PHE   B CD2 1 
ATOM   7608  C  CE1 . PHE   B 2 671 ? 36.041  55.046  -23.581 1.00 94.53  ? 975  PHE   B CE1 1 
ATOM   7609  C  CE2 . PHE   B 2 671 ? 34.606  54.303  -21.840 1.00 90.05  ? 975  PHE   B CE2 1 
ATOM   7610  C  CZ  . PHE   B 2 671 ? 34.769  54.818  -23.093 1.00 92.45  ? 975  PHE   B CZ  1 
ATOM   7611  N  N   . VAL   B 2 672 ? 39.755  56.580  -21.453 1.00 94.91  ? 976  VAL   B N   1 
ATOM   7612  C  CA  . VAL   B 2 672 ? 39.903  57.695  -22.377 1.00 97.81  ? 976  VAL   B CA  1 
ATOM   7613  C  C   . VAL   B 2 672 ? 40.505  57.177  -23.680 1.00 102.54 ? 976  VAL   B C   1 
ATOM   7614  O  O   . VAL   B 2 672 ? 41.516  56.464  -23.663 1.00 99.13  ? 976  VAL   B O   1 
ATOM   7615  C  CB  . VAL   B 2 672 ? 40.778  58.805  -21.766 1.00 96.09  ? 976  VAL   B CB  1 
ATOM   7616  C  CG1 . VAL   B 2 672 ? 40.928  59.955  -22.749 1.00 97.21  ? 976  VAL   B CG1 1 
ATOM   7617  C  CG2 . VAL   B 2 672 ? 40.188  59.257  -20.421 1.00 92.05  ? 976  VAL   B CG2 1 
ATOM   7618  N  N   . CYS   B 2 673 ? 39.864  57.512  -24.804 1.00 106.90 ? 977  CYS   B N   1 
ATOM   7619  C  CA  . CYS   B 2 673 ? 40.424  57.321  -26.136 1.00 109.85 ? 977  CYS   B CA  1 
ATOM   7620  C  C   . CYS   B 2 673 ? 40.471  58.660  -26.866 1.00 110.68 ? 977  CYS   B C   1 
ATOM   7621  O  O   . CYS   B 2 673 ? 39.708  59.589  -26.566 1.00 107.17 ? 977  CYS   B O   1 
ATOM   7622  C  CB  . CYS   B 2 673 ? 39.625  56.302  -26.954 1.00 113.74 ? 977  CYS   B CB  1 
ATOM   7623  S  SG  . CYS   B 2 673 ? 37.865  56.666  -27.098 1.00 123.12 ? 977  CYS   B SG  1 
ATOM   7624  N  N   . GLN   B 2 674 ? 41.400  58.756  -27.812 1.00 114.94 ? 978  GLN   B N   1 
ATOM   7625  C  CA  . GLN   B 2 674 ? 41.636  59.998  -28.522 1.00 118.02 ? 978  GLN   B CA  1 
ATOM   7626  C  C   . GLN   B 2 674 ? 41.604  59.735  -30.015 1.00 121.62 ? 978  GLN   B C   1 
ATOM   7627  O  O   . GLN   B 2 674 ? 41.938  58.638  -30.476 1.00 118.80 ? 978  GLN   B O   1 
ATOM   7628  C  CB  . GLN   B 2 674 ? 42.980  60.624  -28.150 1.00 112.42 ? 978  GLN   B CB  1 
ATOM   7629  C  CG  . GLN   B 2 674 ? 44.127  60.070  -28.959 1.00 115.68 ? 978  GLN   B CG  1 
ATOM   7630  C  CD  . GLN   B 2 674 ? 45.452  60.541  -28.438 1.00 115.28 ? 978  GLN   B CD  1 
ATOM   7631  O  OE1 . GLN   B 2 674 ? 45.532  61.086  -27.336 1.00 108.59 ? 978  GLN   B OE1 1 
ATOM   7632  N  NE2 . GLN   B 2 674 ? 46.509  60.341  -29.225 1.00 121.85 ? 978  GLN   B NE2 1 
ATOM   7633  N  N   . LYS   B 2 675 ? 41.181  60.757  -30.759 1.00 124.31 ? 979  LYS   B N   1 
ATOM   7634  C  CA  . LYS   B 2 675 ? 41.344  60.735  -32.199 1.00 131.79 ? 979  LYS   B CA  1 
ATOM   7635  C  C   . LYS   B 2 675 ? 42.808  60.453  -32.493 1.00 142.79 ? 979  LYS   B C   1 
ATOM   7636  O  O   . LYS   B 2 675 ? 43.696  60.856  -31.732 1.00 142.16 ? 979  LYS   B O   1 
ATOM   7637  C  CB  . LYS   B 2 675 ? 40.897  62.070  -32.810 1.00 127.62 ? 979  LYS   B CB  1 
ATOM   7638  C  CG  . LYS   B 2 675 ? 40.951  62.156  -34.344 1.00 136.32 ? 979  LYS   B CG  1 
ATOM   7639  C  CD  . LYS   B 2 675 ? 40.444  63.500  -34.877 1.00 146.73 ? 979  LYS   B CD  1 
ATOM   7640  C  CE  . LYS   B 2 675 ? 40.503  63.636  -36.402 1.00 144.32 ? 979  LYS   B CE  1 
ATOM   7641  N  NZ  . LYS   B 2 675 ? 39.988  64.979  -36.827 1.00 156.97 ? 979  LYS   B NZ  1 
ATOM   7642  N  N   . ASP   B 2 676 ? 43.055  59.701  -33.563 1.00 162.01 ? 980  ASP   B N   1 
ATOM   7643  C  CA  . ASP   B 2 676 ? 44.426  59.461  -34.000 1.00 165.68 ? 980  ASP   B CA  1 
ATOM   7644  C  C   . ASP   B 2 676 ? 44.827  60.880  -34.390 1.00 168.03 ? 980  ASP   B C   1 
ATOM   7645  O  O   . ASP   B 2 676 ? 44.355  61.412  -35.398 1.00 169.78 ? 980  ASP   B O   1 
ATOM   7646  C  CB  . ASP   B 2 676 ? 44.466  58.399  -35.105 1.00 169.04 ? 980  ASP   B CB  1 
ATOM   7647  C  CG  . ASP   B 2 676 ? 45.698  57.511  -35.013 1.00 172.89 ? 980  ASP   B CG  1 
ATOM   7648  O  OD1 . ASP   B 2 676 ? 46.781  58.029  -34.646 1.00 173.81 ? 980  ASP   B OD1 1 
ATOM   7649  O  OD2 . ASP   B 2 676 ? 45.565  56.302  -35.310 1.00 172.27 ? 980  ASP   B OD2 1 
ATOM   7650  N  N   . SER   B 2 677 ? 45.695  61.505  -33.572 1.00 165.84 ? 981  SER   B N   1 
ATOM   7651  C  CA  . SER   B 2 677 ? 46.186  62.851  -33.826 1.00 168.49 ? 981  SER   B CA  1 
ATOM   7652  C  C   . SER   B 2 677 ? 47.137  62.677  -34.999 1.00 175.71 ? 981  SER   B C   1 
ATOM   7653  O  O   . SER   B 2 677 ? 47.295  63.575  -35.834 1.00 176.04 ? 981  SER   B O   1 
ATOM   7654  C  CB  . SER   B 2 677 ? 46.924  63.378  -32.595 1.00 165.36 ? 981  SER   B CB  1 
ATOM   7655  O  OG  . SER   B 2 677 ? 46.103  63.379  -31.437 1.00 153.47 ? 981  SER   B OG  1 
ATOM   7656  N  N   . ALA   B 2 678 ? 47.768  61.500  -35.072 1.00 186.98 ? 982  ALA   B N   1 
ATOM   7657  C  CA  . ALA   B 2 678 ? 48.644  61.119  -36.174 1.00 191.08 ? 982  ALA   B CA  1 
ATOM   7658  C  C   . ALA   B 2 678 ? 47.783  60.829  -37.403 1.00 192.90 ? 982  ALA   B C   1 
ATOM   7659  O  O   . ALA   B 2 678 ? 47.429  59.684  -37.689 1.00 189.51 ? 982  ALA   B O   1 
ATOM   7660  C  CB  . ALA   B 2 678 ? 49.505  59.923  -35.774 1.00 184.11 ? 982  ALA   B CB  1 
ATOM   7661  N  N   . ALA   B 2 679 ? 47.436  61.885  -38.116 1.00 184.57 ? 983  ALA   B N   1 
ATOM   7662  C  CA  . ALA   B 2 679 ? 46.631  61.784  -39.328 1.00 176.01 ? 983  ALA   B CA  1 
ATOM   7663  C  C   . ALA   B 2 679 ? 47.631  61.079  -40.250 1.00 177.34 ? 983  ALA   B C   1 
ATOM   7664  O  O   . ALA   B 2 679 ? 48.532  61.725  -40.799 1.00 179.05 ? 983  ALA   B O   1 
ATOM   7665  C  CB  . ALA   B 2 679 ? 46.203  63.188  -39.798 1.00 171.40 ? 983  ALA   B CB  1 
ATOM   7666  N  N   . THR   B 2 680 ? 47.492  59.753  -40.414 1.00 175.30 ? 984  THR   B N   1 
ATOM   7667  C  CA  . THR   B 2 680 ? 48.416  58.942  -41.212 1.00 171.90 ? 984  THR   B CA  1 
ATOM   7668  C  C   . THR   B 2 680 ? 47.603  58.579  -42.449 1.00 167.20 ? 984  THR   B C   1 
ATOM   7669  O  O   . THR   B 2 680 ? 47.691  59.252  -43.481 1.00 164.48 ? 984  THR   B O   1 
ATOM   7670  C  CB  . THR   B 2 680 ? 48.939  57.648  -40.566 1.00 168.96 ? 984  THR   B CB  1 
ATOM   7671  O  OG1 . THR   B 2 680 ? 47.845  56.764  -40.276 1.00 165.44 ? 984  THR   B OG1 1 
ATOM   7672  C  CG2 . THR   B 2 680 ? 49.713  57.952  -39.291 1.00 170.47 ? 984  THR   B CG2 1 
ATOM   7673  N  N   . THR   B 2 681 ? 46.828  57.506  -42.367 1.00 163.75 ? 985  THR   B N   1 
ATOM   7674  C  CA  . THR   B 2 681 ? 46.012  57.062  -43.484 1.00 163.57 ? 985  THR   B CA  1 
ATOM   7675  C  C   . THR   B 2 681 ? 44.551  57.018  -43.068 1.00 161.90 ? 985  THR   B C   1 
ATOM   7676  O  O   . THR   B 2 681 ? 44.216  57.122  -41.885 1.00 160.88 ? 985  THR   B O   1 
ATOM   7677  C  CB  . THR   B 2 681 ? 46.450  55.682  -43.974 1.00 167.51 ? 985  THR   B CB  1 
ATOM   7678  O  OG1 . THR   B 2 681 ? 45.998  54.694  -43.040 1.00 167.28 ? 985  THR   B OG1 1 
ATOM   7679  C  CG2 . THR   B 2 681 ? 47.966  55.616  -44.085 1.00 167.84 ? 985  THR   B CG2 1 
ATOM   7680  N  N   . ASP   B 2 682 ? 43.683  56.831  -44.067 1.00 159.50 ? 986  ASP   B N   1 
ATOM   7681  C  CA  . ASP   B 2 682 ? 42.243  56.838  -43.827 1.00 156.68 ? 986  ASP   B CA  1 
ATOM   7682  C  C   . ASP   B 2 682 ? 41.867  55.911  -42.683 1.00 156.32 ? 986  ASP   B C   1 
ATOM   7683  O  O   . ASP   B 2 682 ? 41.174  56.315  -41.741 1.00 155.11 ? 986  ASP   B O   1 
ATOM   7684  C  CB  . ASP   B 2 682 ? 41.494  56.429  -45.093 1.00 155.24 ? 986  ASP   B CB  1 
ATOM   7685  N  N   . GLU   B 2 683 ? 42.294  54.650  -42.766 1.00 159.07 ? 987  GLU   B N   1 
ATOM   7686  C  CA  . GLU   B 2 683 ? 41.945  53.690  -41.730 1.00 155.43 ? 987  GLU   B CA  1 
ATOM   7687  C  C   . GLU   B 2 683 ? 42.398  54.180  -40.361 1.00 157.02 ? 987  GLU   B C   1 
ATOM   7688  O  O   . GLU   B 2 683 ? 41.677  54.026  -39.366 1.00 155.46 ? 987  GLU   B O   1 
ATOM   7689  C  CB  . GLU   B 2 683 ? 42.551  52.327  -42.056 1.00 149.88 ? 987  GLU   B CB  1 
ATOM   7690  N  N   . GLU   B 2 684 ? 43.578  54.798  -40.293 1.00 165.19 ? 988  GLU   B N   1 
ATOM   7691  C  CA  . GLU   B 2 684 ? 44.086  55.269  -39.009 1.00 164.39 ? 988  GLU   B CA  1 
ATOM   7692  C  C   . GLU   B 2 684 ? 43.318  56.495  -38.529 1.00 161.99 ? 988  GLU   B C   1 
ATOM   7693  O  O   . GLU   B 2 684 ? 42.830  56.529  -37.392 1.00 160.33 ? 988  GLU   B O   1 
ATOM   7694  C  CB  . GLU   B 2 684 ? 45.580  55.574  -39.117 1.00 164.68 ? 988  GLU   B CB  1 
ATOM   7695  N  N   . ARG   B 2 685 ? 43.195  57.513  -39.388 1.00 157.15 ? 989  ARG   B N   1 
ATOM   7696  C  CA  . ARG   B 2 685 ? 42.565  58.767  -38.986 1.00 148.59 ? 989  ARG   B CA  1 
ATOM   7697  C  C   . ARG   B 2 685 ? 41.115  58.565  -38.555 1.00 142.63 ? 989  ARG   B C   1 
ATOM   7698  O  O   . ARG   B 2 685 ? 40.610  59.313  -37.705 1.00 131.70 ? 989  ARG   B O   1 
ATOM   7699  C  CB  . ARG   B 2 685 ? 42.654  59.774  -40.133 1.00 150.72 ? 989  ARG   B CB  1 
ATOM   7700  C  CG  . ARG   B 2 685 ? 44.057  59.980  -40.700 1.00 158.25 ? 989  ARG   B CG  1 
ATOM   7701  C  CD  . ARG   B 2 685 ? 44.051  61.017  -41.815 1.00 155.87 ? 989  ARG   B CD  1 
ATOM   7702  N  NE  . ARG   B 2 685 ? 43.271  60.588  -42.972 1.00 157.59 ? 989  ARG   B NE  1 
ATOM   7703  C  CZ  . ARG   B 2 685 ? 43.788  60.275  -44.153 1.00 157.73 ? 989  ARG   B CZ  1 
ATOM   7704  N  NH1 . ARG   B 2 685 ? 45.089  60.354  -44.380 1.00 162.02 ? 989  ARG   B NH1 1 
ATOM   7705  N  NH2 . ARG   B 2 685 ? 42.979  59.876  -45.132 1.00 154.35 ? 989  ARG   B NH2 1 
ATOM   7706  N  N   . GLN   B 2 686 ? 40.435  57.564  -39.126 1.00 144.43 ? 990  GLN   B N   1 
ATOM   7707  C  CA  . GLN   B 2 686 ? 39.044  57.225  -38.810 1.00 135.51 ? 990  GLN   B CA  1 
ATOM   7708  C  C   . GLN   B 2 686 ? 38.936  56.119  -37.758 1.00 135.70 ? 990  GLN   B C   1 
ATOM   7709  O  O   . GLN   B 2 686 ? 38.114  55.210  -37.880 1.00 134.70 ? 990  GLN   B O   1 
ATOM   7710  C  CB  . GLN   B 2 686 ? 38.304  56.840  -40.090 1.00 122.81 ? 990  GLN   B CB  1 
ATOM   7711  N  N   . HIS   B 2 687 ? 39.755  56.187  -36.706 1.00 136.40 ? 991  HIS   B N   1 
ATOM   7712  C  CA  . HIS   B 2 687 ? 39.740  55.240  -35.599 1.00 132.34 ? 991  HIS   B CA  1 
ATOM   7713  C  C   . HIS   B 2 687 ? 40.279  55.943  -34.352 1.00 133.96 ? 991  HIS   B C   1 
ATOM   7714  O  O   . HIS   B 2 687 ? 41.182  56.781  -34.453 1.00 137.10 ? 991  HIS   B O   1 
ATOM   7715  C  CB  . HIS   B 2 687 ? 40.575  53.989  -35.925 1.00 131.35 ? 991  HIS   B CB  1 
ATOM   7716  C  CG  . HIS   B 2 687 ? 40.974  53.211  -34.713 1.00 132.50 ? 991  HIS   B CG  1 
ATOM   7717  N  ND1 . HIS   B 2 687 ? 41.972  53.628  -33.857 1.00 134.69 ? 991  HIS   B ND1 1 
ATOM   7718  C  CD2 . HIS   B 2 687 ? 40.494  52.056  -34.194 1.00 133.36 ? 991  HIS   B CD2 1 
ATOM   7719  C  CE1 . HIS   B 2 687 ? 42.095  52.758  -32.868 1.00 132.56 ? 991  HIS   B CE1 1 
ATOM   7720  N  NE2 . HIS   B 2 687 ? 41.209  51.795  -33.049 1.00 133.73 ? 991  HIS   B NE2 1 
ATOM   7721  N  N   . LEU   B 2 688 ? 39.722  55.612  -33.182 1.00 128.81 ? 992  LEU   B N   1 
ATOM   7722  C  CA  . LEU   B 2 688 ? 40.135  56.202  -31.908 1.00 125.06 ? 992  LEU   B CA  1 
ATOM   7723  C  C   . LEU   B 2 688 ? 40.941  55.200  -31.086 1.00 124.40 ? 992  LEU   B C   1 
ATOM   7724  O  O   . LEU   B 2 688 ? 40.452  54.106  -30.796 1.00 129.34 ? 992  LEU   B O   1 
ATOM   7725  C  CB  . LEU   B 2 688 ? 38.920  56.646  -31.099 1.00 118.43 ? 992  LEU   B CB  1 
ATOM   7726  C  CG  . LEU   B 2 688 ? 37.900  57.561  -31.755 1.00 116.56 ? 992  LEU   B CG  1 
ATOM   7727  C  CD1 . LEU   B 2 688 ? 36.646  57.541  -30.919 1.00 106.40 ? 992  LEU   B CD1 1 
ATOM   7728  C  CD2 . LEU   B 2 688 ? 38.452  58.979  -31.865 1.00 121.19 ? 992  LEU   B CD2 1 
ATOM   7729  N  N   . GLN   B 2 689 ? 42.154  55.582  -30.680 1.00 122.70 ? 993  GLN   B N   1 
ATOM   7730  C  CA  . GLN   B 2 689 ? 43.004  54.709  -29.873 1.00 120.78 ? 993  GLN   B CA  1 
ATOM   7731  C  C   . GLN   B 2 689 ? 42.698  54.852  -28.385 1.00 117.05 ? 993  GLN   B C   1 
ATOM   7732  O  O   . GLN   B 2 689 ? 42.386  55.951  -27.904 1.00 111.93 ? 993  GLN   B O   1 
ATOM   7733  C  CB  . GLN   B 2 689 ? 44.490  55.019  -30.101 1.00 123.35 ? 993  GLN   B CB  1 
ATOM   7734  C  CG  . GLN   B 2 689 ? 44.880  55.263  -31.533 1.00 135.29 ? 993  GLN   B CG  1 
ATOM   7735  C  CD  . GLN   B 2 689 ? 45.019  53.981  -32.310 1.00 136.80 ? 993  GLN   B CD  1 
ATOM   7736  O  OE1 . GLN   B 2 689 ? 45.020  52.890  -31.735 1.00 128.81 ? 993  GLN   B OE1 1 
ATOM   7737  N  NE2 . GLN   B 2 689 ? 45.134  54.101  -33.629 1.00 140.47 ? 993  GLN   B NE2 1 
ATOM   7738  N  N   . GLU   B 2 690 ? 42.825  53.733  -27.655 1.00 113.00 ? 994  GLU   B N   1 
ATOM   7739  C  CA  . GLU   B 2 690 ? 42.620  53.693  -26.202 1.00 107.52 ? 994  GLU   B CA  1 
ATOM   7740  C  C   . GLU   B 2 690 ? 43.872  54.219  -25.490 1.00 106.22 ? 994  GLU   B C   1 
ATOM   7741  O  O   . GLU   B 2 690 ? 44.916  53.562  -25.498 1.00 108.31 ? 994  GLU   B O   1 
ATOM   7742  C  CB  . GLU   B 2 690 ? 42.293  52.267  -25.757 1.00 99.07  ? 994  GLU   B CB  1 
ATOM   7743  N  N   . VAL   B 2 691 ? 43.781  55.395  -24.858 1.00 101.18 ? 995  VAL   B N   1 
ATOM   7744  C  CA  . VAL   B 2 691 ? 44.959  56.040  -24.286 1.00 100.35 ? 995  VAL   B CA  1 
ATOM   7745  C  C   . VAL   B 2 691 ? 44.832  56.242  -22.772 1.00 101.72 ? 995  VAL   B C   1 
ATOM   7746  O  O   . VAL   B 2 691 ? 45.522  57.095  -22.201 1.00 104.37 ? 995  VAL   B O   1 
ATOM   7747  C  CB  . VAL   B 2 691 ? 45.270  57.374  -24.998 1.00 103.36 ? 995  VAL   B CB  1 
ATOM   7748  C  CG1 . VAL   B 2 691 ? 45.141  57.228  -26.509 1.00 108.84 ? 995  VAL   B CG1 1 
ATOM   7749  C  CG2 . VAL   B 2 691 ? 44.386  58.504  -24.479 1.00 104.09 ? 995  VAL   B CG2 1 
ATOM   7750  N  N   . GLY   B 2 692 ? 43.983  55.455  -22.103 1.00 97.13  ? 996  GLY   B N   1 
ATOM   7751  C  CA  . GLY   B 2 692 ? 43.805  55.581  -20.663 1.00 96.44  ? 996  GLY   B CA  1 
ATOM   7752  C  C   . GLY   B 2 692 ? 42.817  54.605  -20.050 1.00 96.28  ? 996  GLY   B C   1 
ATOM   7753  O  O   . GLY   B 2 692 ? 41.675  54.478  -20.518 1.00 92.94  ? 996  GLY   B O   1 
ATOM   7754  N  N   . LEU   B 2 693 ? 43.243  53.922  -18.984 1.00 97.83  ? 997  LEU   B N   1 
ATOM   7755  C  CA  . LEU   B 2 693 ? 42.447  52.884  -18.337 1.00 93.81  ? 997  LEU   B CA  1 
ATOM   7756  C  C   . LEU   B 2 693 ? 42.612  52.991  -16.836 1.00 89.07  ? 997  LEU   B C   1 
ATOM   7757  O  O   . LEU   B 2 693 ? 43.744  53.006  -16.350 1.00 92.36  ? 997  LEU   B O   1 
ATOM   7758  C  CB  . LEU   B 2 693 ? 42.878  51.496  -18.790 1.00 92.28  ? 997  LEU   B CB  1 
ATOM   7759  C  CG  . LEU   B 2 693 ? 42.393  51.211  -20.194 1.00 92.35  ? 997  LEU   B CG  1 
ATOM   7760  C  CD1 . LEU   B 2 693 ? 42.374  49.727  -20.362 1.00 97.00  ? 997  LEU   B CD1 1 
ATOM   7761  C  CD2 . LEU   B 2 693 ? 41.005  51.784  -20.357 1.00 91.05  ? 997  LEU   B CD2 1 
ATOM   7762  N  N   . PHE   B 2 694 ? 41.495  53.041  -16.105 1.00 86.82  ? 998  PHE   B N   1 
ATOM   7763  C  CA  . PHE   B 2 694 ? 41.570  53.265  -14.662 1.00 90.89  ? 998  PHE   B CA  1 
ATOM   7764  C  C   . PHE   B 2 694 ? 40.351  52.685  -13.969 1.00 87.90  ? 998  PHE   B C   1 
ATOM   7765  O  O   . PHE   B 2 694 ? 39.216  52.979  -14.355 1.00 85.73  ? 998  PHE   B O   1 
ATOM   7766  C  CB  . PHE   B 2 694 ? 41.694  54.757  -14.353 1.00 91.42  ? 998  PHE   B CB  1 
ATOM   7767  C  CG  . PHE   B 2 694 ? 41.898  55.078  -12.904 1.00 89.81  ? 998  PHE   B CG  1 
ATOM   7768  C  CD1 . PHE   B 2 694 ? 43.163  54.998  -12.328 1.00 89.91  ? 998  PHE   B CD1 1 
ATOM   7769  C  CD2 . PHE   B 2 694 ? 40.829  55.516  -12.125 1.00 88.47  ? 998  PHE   B CD2 1 
ATOM   7770  C  CE1 . PHE   B 2 694 ? 43.345  55.322  -10.984 1.00 90.88  ? 998  PHE   B CE1 1 
ATOM   7771  C  CE2 . PHE   B 2 694 ? 41.001  55.845  -10.797 1.00 83.93  ? 998  PHE   B CE2 1 
ATOM   7772  C  CZ  . PHE   B 2 694 ? 42.257  55.753  -10.224 1.00 87.11  ? 998  PHE   B CZ  1 
ATOM   7773  N  N   . HIS   B 2 695 ? 40.589  51.872  -12.945 1.00 86.54  ? 999  HIS   B N   1 
ATOM   7774  C  CA  . HIS   B 2 695 ? 39.501  51.312  -12.164 1.00 85.49  ? 999  HIS   B CA  1 
ATOM   7775  C  C   . HIS   B 2 695 ? 39.126  52.338  -11.112 1.00 87.80  ? 999  HIS   B C   1 
ATOM   7776  O  O   . HIS   B 2 695 ? 39.908  52.609  -10.195 1.00 89.93  ? 999  HIS   B O   1 
ATOM   7777  C  CB  . HIS   B 2 695 ? 39.887  49.994  -11.515 1.00 87.01  ? 999  HIS   B CB  1 
ATOM   7778  C  CG  . HIS   B 2 695 ? 38.769  49.379  -10.739 1.00 85.66  ? 999  HIS   B CG  1 
ATOM   7779  N  ND1 . HIS   B 2 695 ? 37.905  48.454  -11.287 1.00 87.35  ? 999  HIS   B ND1 1 
ATOM   7780  C  CD2 . HIS   B 2 695 ? 38.347  49.584  -9.470  1.00 84.55  ? 999  HIS   B CD2 1 
ATOM   7781  C  CE1 . HIS   B 2 695 ? 37.009  48.101  -10.384 1.00 86.28  ? 999  HIS   B CE1 1 
ATOM   7782  N  NE2 . HIS   B 2 695 ? 37.260  48.766  -9.270  1.00 88.08  ? 999  HIS   B NE2 1 
ATOM   7783  N  N   . LEU   B 2 696 ? 37.943  52.929  -11.250 1.00 87.16  ? 1000 LEU   B N   1 
ATOM   7784  C  CA  . LEU   B 2 696 ? 37.549  53.966  -10.302 1.00 86.00  ? 1000 LEU   B CA  1 
ATOM   7785  C  C   . LEU   B 2 696 ? 37.011  53.358  -9.013  1.00 78.54  ? 1000 LEU   B C   1 
ATOM   7786  O  O   . LEU   B 2 696 ? 37.544  53.596  -7.928  1.00 82.38  ? 1000 LEU   B O   1 
ATOM   7787  C  CB  . LEU   B 2 696 ? 36.508  54.879  -10.943 1.00 83.77  ? 1000 LEU   B CB  1 
ATOM   7788  C  CG  . LEU   B 2 696 ? 36.003  55.985  -10.052 1.00 76.43  ? 1000 LEU   B CG  1 
ATOM   7789  C  CD1 . LEU   B 2 696 ? 37.042  57.056  -10.022 1.00 72.71  ? 1000 LEU   B CD1 1 
ATOM   7790  C  CD2 . LEU   B 2 696 ? 34.715  56.467  -10.648 1.00 75.97  ? 1000 LEU   B CD2 1 
ATOM   7791  N  N   . GLY   B 2 697 ? 35.967  52.561  -9.114  1.00 76.00  ? 1001 GLY   B N   1 
ATOM   7792  C  CA  . GLY   B 2 697 ? 35.297  52.031  -7.954  1.00 78.41  ? 1001 GLY   B CA  1 
ATOM   7793  C  C   . GLY   B 2 697 ? 33.872  52.488  -7.821  1.00 81.57  ? 1001 GLY   B C   1 
ATOM   7794  O  O   . GLY   B 2 697 ? 33.141  51.966  -6.963  1.00 85.18  ? 1001 GLY   B O   1 
ATOM   7795  N  N   . GLU   B 2 698 ? 33.441  53.438  -8.637  1.00 82.36  ? 1002 GLU   B N   1 
ATOM   7796  C  CA  . GLU   B 2 698 ? 32.082  53.959  -8.611  1.00 80.01  ? 1002 GLU   B CA  1 
ATOM   7797  C  C   . GLU   B 2 698 ? 31.453  53.739  -9.970  1.00 77.67  ? 1002 GLU   B C   1 
ATOM   7798  O  O   . GLU   B 2 698 ? 32.131  53.395  -10.941 1.00 77.06  ? 1002 GLU   B O   1 
ATOM   7799  C  CB  . GLU   B 2 698 ? 32.081  55.450  -8.267  1.00 82.58  ? 1002 GLU   B CB  1 
ATOM   7800  C  CG  . GLU   B 2 698 ? 32.874  55.771  -7.038  1.00 76.23  ? 1002 GLU   B CG  1 
ATOM   7801  C  CD  . GLU   B 2 698 ? 32.167  55.249  -5.825  1.00 83.03  ? 1002 GLU   B CD  1 
ATOM   7802  O  OE1 . GLU   B 2 698 ? 32.781  55.247  -4.730  1.00 85.64  ? 1002 GLU   B OE1 1 
ATOM   7803  O  OE2 . GLU   B 2 698 ? 30.983  54.823  -6.003  1.00 82.50  ? 1002 GLU   B OE2 1 
ATOM   7804  N  N   . PHE   B 2 699 ? 30.166  53.969  -10.052 1.00 78.92  ? 1003 PHE   B N   1 
ATOM   7805  C  CA  . PHE   B 2 699 ? 29.436  53.738  -11.295 1.00 79.49  ? 1003 PHE   B CA  1 
ATOM   7806  C  C   . PHE   B 2 699 ? 28.949  55.108  -11.760 1.00 82.63  ? 1003 PHE   B C   1 
ATOM   7807  O  O   . PHE   B 2 699 ? 27.979  55.643  -11.207 1.00 81.44  ? 1003 PHE   B O   1 
ATOM   7808  C  CB  . PHE   B 2 699 ? 28.307  52.741  -11.054 1.00 76.01  ? 1003 PHE   B CB  1 
ATOM   7809  C  CG  . PHE   B 2 699 ? 27.572  52.332  -12.271 1.00 74.46  ? 1003 PHE   B CG  1 
ATOM   7810  C  CD1 . PHE   B 2 699 ? 26.574  53.132  -12.794 1.00 77.92  ? 1003 PHE   B CD1 1 
ATOM   7811  C  CD2 . PHE   B 2 699 ? 27.825  51.112  -12.865 1.00 81.50  ? 1003 PHE   B CD2 1 
ATOM   7812  C  CE1 . PHE   B 2 699 ? 25.859  52.739  -13.911 1.00 77.08  ? 1003 PHE   B CE1 1 
ATOM   7813  C  CE2 . PHE   B 2 699 ? 27.118  50.711  -13.984 1.00 81.39  ? 1003 PHE   B CE2 1 
ATOM   7814  C  CZ  . PHE   B 2 699 ? 26.133  51.530  -14.509 1.00 75.55  ? 1003 PHE   B CZ  1 
ATOM   7815  N  N   . VAL   B 2 700 ? 29.641  55.686  -12.752 1.00 83.27  ? 1004 VAL   B N   1 
ATOM   7816  C  CA  . VAL   B 2 700 ? 29.382  57.064  -13.162 1.00 77.99  ? 1004 VAL   B CA  1 
ATOM   7817  C  C   . VAL   B 2 700 ? 28.079  57.133  -13.947 1.00 78.97  ? 1004 VAL   B C   1 
ATOM   7818  O  O   . VAL   B 2 700 ? 27.835  56.328  -14.852 1.00 79.57  ? 1004 VAL   B O   1 
ATOM   7819  C  CB  . VAL   B 2 700 ? 30.553  57.628  -13.982 1.00 75.92  ? 1004 VAL   B CB  1 
ATOM   7820  C  CG1 . VAL   B 2 700 ? 30.171  58.990  -14.588 1.00 79.49  ? 1004 VAL   B CG1 1 
ATOM   7821  C  CG2 . VAL   B 2 700 ? 31.803  57.756  -13.125 1.00 71.93  ? 1004 VAL   B CG2 1 
ATOM   7822  N  N   . ASN   B 2 701 ? 27.247  58.115  -13.607 1.00 77.25  ? 1005 ASN   B N   1 
ATOM   7823  C  CA  . ASN   B 2 701 ? 25.926  58.294  -14.188 1.00 76.56  ? 1005 ASN   B CA  1 
ATOM   7824  C  C   . ASN   B 2 701 ? 25.801  59.538  -15.058 1.00 83.10  ? 1005 ASN   B C   1 
ATOM   7825  O  O   . ASN   B 2 701 ? 24.968  59.556  -15.978 1.00 84.44  ? 1005 ASN   B O   1 
ATOM   7826  C  CB  . ASN   B 2 701 ? 24.876  58.382  -13.077 1.00 76.67  ? 1005 ASN   B CB  1 
ATOM   7827  C  CG  . ASN   B 2 701 ? 24.143  57.088  -12.856 1.00 80.35  ? 1005 ASN   B CG  1 
ATOM   7828  O  OD1 . ASN   B 2 701 ? 24.060  56.231  -13.751 1.00 84.54  ? 1005 ASN   B OD1 1 
ATOM   7829  N  ND2 . ASN   B 2 701 ? 23.572  56.942  -11.656 1.00 79.07  ? 1005 ASN   B ND2 1 
ATOM   7830  N  N   . VAL   B 2 702 ? 26.599  60.569  -14.779 1.00 80.40  ? 1006 VAL   B N   1 
ATOM   7831  C  CA  . VAL   B 2 702 ? 26.541  61.848  -15.471 1.00 78.78  ? 1006 VAL   B CA  1 
ATOM   7832  C  C   . VAL   B 2 702 ? 27.900  62.500  -15.358 1.00 86.35  ? 1006 VAL   B C   1 
ATOM   7833  O  O   . VAL   B 2 702 ? 28.536  62.443  -14.300 1.00 84.06  ? 1006 VAL   B O   1 
ATOM   7834  C  CB  . VAL   B 2 702 ? 25.476  62.769  -14.871 1.00 80.64  ? 1006 VAL   B CB  1 
ATOM   7835  C  CG1 . VAL   B 2 702 ? 25.556  62.668  -13.388 1.00 82.91  ? 1006 VAL   B CG1 1 
ATOM   7836  C  CG2 . VAL   B 2 702 ? 25.736  64.189  -15.291 1.00 80.93  ? 1006 VAL   B CG2 1 
ATOM   7837  N  N   . PHE   B 2 703 ? 28.345  63.107  -16.459 1.00 87.66  ? 1007 PHE   B N   1 
ATOM   7838  C  CA  . PHE   B 2 703 ? 29.583  63.876  -16.529 1.00 85.65  ? 1007 PHE   B CA  1 
ATOM   7839  C  C   . PHE   B 2 703 ? 29.194  65.330  -16.756 1.00 89.52  ? 1007 PHE   B C   1 
ATOM   7840  O  O   . PHE   B 2 703 ? 28.405  65.637  -17.655 1.00 96.63  ? 1007 PHE   B O   1 
ATOM   7841  C  CB  . PHE   B 2 703 ? 30.504  63.393  -17.663 1.00 87.69  ? 1007 PHE   B CB  1 
ATOM   7842  C  CG  . PHE   B 2 703 ? 31.360  62.198  -17.314 1.00 86.81  ? 1007 PHE   B CG  1 
ATOM   7843  C  CD1 . PHE   B 2 703 ? 32.352  62.296  -16.351 1.00 84.87  ? 1007 PHE   B CD1 1 
ATOM   7844  C  CD2 . PHE   B 2 703 ? 31.202  60.981  -17.985 1.00 87.76  ? 1007 PHE   B CD2 1 
ATOM   7845  C  CE1 . PHE   B 2 703 ? 33.158  61.197  -16.048 1.00 83.72  ? 1007 PHE   B CE1 1 
ATOM   7846  C  CE2 . PHE   B 2 703 ? 31.999  59.883  -17.680 1.00 83.89  ? 1007 PHE   B CE2 1 
ATOM   7847  C  CZ  . PHE   B 2 703 ? 32.977  59.991  -16.711 1.00 81.87  ? 1007 PHE   B CZ  1 
ATOM   7848  N  N   . CYS   B 2 704 ? 29.733  66.226  -15.954 1.00 89.24  ? 1008 CYS   B N   1 
ATOM   7849  C  CA  . CYS   B 2 704 ? 29.304  67.611  -16.006 1.00 88.50  ? 1008 CYS   B CA  1 
ATOM   7850  C  C   . CYS   B 2 704 ? 30.534  68.499  -16.023 1.00 90.87  ? 1008 CYS   B C   1 
ATOM   7851  O  O   . CYS   B 2 704 ? 31.305  68.507  -15.056 1.00 87.66  ? 1008 CYS   B O   1 
ATOM   7852  C  CB  . CYS   B 2 704 ? 28.407  67.928  -14.817 1.00 86.56  ? 1008 CYS   B CB  1 
ATOM   7853  S  SG  . CYS   B 2 704 ? 27.370  69.341  -15.065 1.00 110.97 ? 1008 CYS   B SG  1 
ATOM   7854  N  N   . HIS   B 2 705 ? 30.720  69.229  -17.123 1.00 94.03  ? 1009 HIS   B N   1 
ATOM   7855  C  CA  . HIS   B 2 705 ? 31.827  70.177  -17.238 1.00 95.61  ? 1009 HIS   B CA  1 
ATOM   7856  C  C   . HIS   B 2 705 ? 31.644  71.352  -16.273 1.00 93.95  ? 1009 HIS   B C   1 
ATOM   7857  O  O   . HIS   B 2 705 ? 30.672  72.111  -16.376 1.00 89.77  ? 1009 HIS   B O   1 
ATOM   7858  C  CB  . HIS   B 2 705 ? 31.925  70.675  -18.671 1.00 93.26  ? 1009 HIS   B CB  1 
ATOM   7859  C  CG  . HIS   B 2 705 ? 32.900  69.916  -19.499 1.00 93.92  ? 1009 HIS   B CG  1 
ATOM   7860  N  ND1 . HIS   B 2 705 ? 34.256  69.948  -19.254 1.00 94.44  ? 1009 HIS   B ND1 1 
ATOM   7861  C  CD2 . HIS   B 2 705 ? 32.723  69.108  -20.570 1.00 93.91  ? 1009 HIS   B CD2 1 
ATOM   7862  C  CE1 . HIS   B 2 705 ? 34.875  69.188  -20.142 1.00 100.54 ? 1009 HIS   B CE1 1 
ATOM   7863  N  NE2 . HIS   B 2 705 ? 33.968  68.665  -20.951 1.00 98.54  ? 1009 HIS   B NE2 1 
ATOM   7864  N  N   . GLY   B 2 706 ? 32.571  71.508  -15.335 1.00 92.40  ? 1010 GLY   B N   1 
ATOM   7865  C  CA  . GLY   B 2 706 ? 32.395  72.528  -14.322 1.00 94.18  ? 1010 GLY   B CA  1 
ATOM   7866  C  C   . GLY   B 2 706 ? 33.380  72.378  -13.185 1.00 91.59  ? 1010 GLY   B C   1 
ATOM   7867  O  O   . GLY   B 2 706 ? 34.186  71.445  -13.138 1.00 89.12  ? 1010 GLY   B O   1 
ATOM   7868  N  N   . SER   B 2 707 ? 33.298  73.335  -12.264 1.00 89.84  ? 1011 SER   B N   1 
ATOM   7869  C  CA  . SER   B 2 707 ? 34.167  73.351  -11.100 1.00 94.33  ? 1011 SER   B CA  1 
ATOM   7870  C  C   . SER   B 2 707 ? 33.459  74.093  -9.972  1.00 102.95 ? 1011 SER   B C   1 
ATOM   7871  O  O   . SER   B 2 707 ? 32.657  75.004  -10.214 1.00 108.47 ? 1011 SER   B O   1 
ATOM   7872  C  CB  . SER   B 2 707 ? 35.516  74.005  -11.422 1.00 93.43  ? 1011 SER   B CB  1 
ATOM   7873  O  OG  . SER   B 2 707 ? 36.402  73.905  -10.323 1.00 97.64  ? 1011 SER   B OG  1 
ATOM   7874  N  N   . LEU   B 2 708 ? 33.762  73.699  -8.736  1.00 102.73 ? 1012 LEU   B N   1 
ATOM   7875  C  CA  . LEU   B 2 708 ? 33.117  74.267  -7.559  1.00 105.96 ? 1012 LEU   B CA  1 
ATOM   7876  C  C   . LEU   B 2 708 ? 34.062  75.179  -6.780  1.00 109.06 ? 1012 LEU   B C   1 
ATOM   7877  O  O   . LEU   B 2 708 ? 33.888  75.387  -5.581  1.00 108.60 ? 1012 LEU   B O   1 
ATOM   7878  C  CB  . LEU   B 2 708 ? 32.591  73.158  -6.656  1.00 106.40 ? 1012 LEU   B CB  1 
ATOM   7879  C  CG  . LEU   B 2 708 ? 31.315  72.438  -7.106  1.00 102.20 ? 1012 LEU   B CG  1 
ATOM   7880  C  CD1 . LEU   B 2 708 ? 31.291  72.235  -8.613  1.00 97.22  ? 1012 LEU   B CD1 1 
ATOM   7881  C  CD2 . LEU   B 2 708 ? 31.171  71.110  -6.366  1.00 92.90  ? 1012 LEU   B CD2 1 
ATOM   7882  N  N   . VAL   B 2 709 ? 35.069  75.723  -7.457  1.00 110.37 ? 1013 VAL   B N   1 
ATOM   7883  C  CA  . VAL   B 2 709 ? 36.051  76.613  -6.860  1.00 113.53 ? 1013 VAL   B CA  1 
ATOM   7884  C  C   . VAL   B 2 709 ? 36.295  77.793  -7.797  1.00 121.56 ? 1013 VAL   B C   1 
ATOM   7885  O  O   . VAL   B 2 709 ? 35.688  77.888  -8.876  1.00 120.80 ? 1013 VAL   B O   1 
ATOM   7886  C  CB  . VAL   B 2 709 ? 37.383  75.896  -6.554  1.00 106.13 ? 1013 VAL   B CB  1 
ATOM   7887  C  CG1 . VAL   B 2 709 ? 37.210  74.886  -5.434  1.00 100.33 ? 1013 VAL   B CG1 1 
ATOM   7888  C  CG2 . VAL   B 2 709 ? 37.924  75.254  -7.828  1.00 103.23 ? 1013 VAL   B CG2 1 
ATOM   7889  N  N   . MET   B 2 710 ? 37.221  78.673  -7.401  1.00 117.80 ? 1014 MET   B N   1 
ATOM   7890  C  CA  . MET   B 2 710 ? 37.429  79.950  -8.080  1.00 120.08 ? 1014 MET   B CA  1 
ATOM   7891  C  C   . MET   B 2 710 ? 36.168  80.814  -7.967  1.00 124.23 ? 1014 MET   B C   1 
ATOM   7892  O  O   . MET   B 2 710 ? 36.143  81.805  -7.234  1.00 125.75 ? 1014 MET   B O   1 
ATOM   7893  C  CB  . MET   B 2 710 ? 37.823  79.738  -9.558  1.00 120.81 ? 1014 MET   B CB  1 
ATOM   7894  C  CG  . MET   B 2 710 ? 37.503  80.860  -10.541 1.00 123.46 ? 1014 MET   B CG  1 
ATOM   7895  S  SD  . MET   B 2 710 ? 38.147  82.482  -10.031 1.00 150.83 ? 1014 MET   B SD  1 
ATOM   7896  C  CE  . MET   B 2 710 ? 38.040  83.495  -11.518 1.00 139.77 ? 1014 MET   B CE  1 
ATOM   7897  N  N   . PRO   B 2 719 ? 48.824  74.314  -14.003 1.00 132.79 ? 1023 PRO   B N   1 
ATOM   7898  C  CA  . PRO   B 2 719 ? 49.452  73.016  -13.717 1.00 131.84 ? 1023 PRO   B CA  1 
ATOM   7899  C  C   . PRO   B 2 719 ? 48.557  71.854  -14.132 1.00 134.29 ? 1023 PRO   B C   1 
ATOM   7900  O  O   . PRO   B 2 719 ? 49.040  70.805  -14.582 1.00 130.88 ? 1023 PRO   B O   1 
ATOM   7901  C  CB  . PRO   B 2 719 ? 49.645  73.050  -12.201 1.00 132.34 ? 1023 PRO   B CB  1 
ATOM   7902  C  CG  . PRO   B 2 719 ? 48.513  73.899  -11.719 1.00 133.44 ? 1023 PRO   B CG  1 
ATOM   7903  C  CD  . PRO   B 2 719 ? 48.308  74.961  -12.783 1.00 136.88 ? 1023 PRO   B CD  1 
ATOM   7904  N  N   . THR   B 2 720 ? 47.249  72.051  -13.966 1.00 133.55 ? 1024 THR   B N   1 
ATOM   7905  C  CA  . THR   B 2 720 ? 46.229  71.162  -14.507 1.00 130.76 ? 1024 THR   B CA  1 
ATOM   7906  C  C   . THR   B 2 720 ? 45.331  71.950  -15.449 1.00 131.47 ? 1024 THR   B C   1 
ATOM   7907  O  O   . THR   B 2 720 ? 45.078  73.139  -15.234 1.00 133.22 ? 1024 THR   B O   1 
ATOM   7908  C  CB  . THR   B 2 720 ? 45.373  70.534  -13.402 1.00 128.51 ? 1024 THR   B CB  1 
ATOM   7909  O  OG1 . THR   B 2 720 ? 44.503  71.534  -12.840 1.00 128.86 ? 1024 THR   B OG1 1 
ATOM   7910  C  CG2 . THR   B 2 720 ? 46.266  69.967  -12.321 1.00 127.46 ? 1024 THR   B CG2 1 
ATOM   7911  N  N   . GLN   B 2 721 ? 44.847  71.274  -16.488 1.00 121.32 ? 1025 GLN   B N   1 
ATOM   7912  C  CA  . GLN   B 2 721 ? 43.946  71.868  -17.466 1.00 116.63 ? 1025 GLN   B CA  1 
ATOM   7913  C  C   . GLN   B 2 721 ? 42.656  71.060  -17.496 1.00 118.18 ? 1025 GLN   B C   1 
ATOM   7914  O  O   . GLN   B 2 721 ? 42.685  69.842  -17.710 1.00 118.70 ? 1025 GLN   B O   1 
ATOM   7915  C  CB  . GLN   B 2 721 ? 44.588  71.905  -18.852 1.00 115.88 ? 1025 GLN   B CB  1 
ATOM   7916  N  N   . GLY   B 2 722 ? 41.532  71.724  -17.278 1.00 115.99 ? 1026 GLY   B N   1 
ATOM   7917  C  CA  . GLY   B 2 722 ? 40.247  71.067  -17.395 1.00 106.48 ? 1026 GLY   B CA  1 
ATOM   7918  C  C   . GLY   B 2 722 ? 39.539  70.944  -16.055 1.00 99.08  ? 1026 GLY   B C   1 
ATOM   7919  O  O   . GLY   B 2 722 ? 40.135  71.040  -14.985 1.00 103.37 ? 1026 GLY   B O   1 
ATOM   7920  N  N   . SER   B 2 723 ? 38.231  70.737  -16.129 1.00 96.02  ? 1027 SER   B N   1 
ATOM   7921  C  CA  . SER   B 2 723 ? 37.493  70.397  -14.921 1.00 93.62  ? 1027 SER   B CA  1 
ATOM   7922  C  C   . SER   B 2 723 ? 36.215  69.697  -15.352 1.00 99.64  ? 1027 SER   B C   1 
ATOM   7923  O  O   . SER   B 2 723 ? 35.324  70.351  -15.914 1.00 96.49  ? 1027 SER   B O   1 
ATOM   7924  C  CB  . SER   B 2 723 ? 37.202  71.632  -14.096 1.00 89.81  ? 1027 SER   B CB  1 
ATOM   7925  O  OG  . SER   B 2 723 ? 36.796  71.291  -12.788 1.00 88.12  ? 1027 SER   B OG  1 
ATOM   7926  N  N   . VAL   B 2 724 ? 36.148  68.379  -15.109 1.00 94.90  ? 1028 VAL   B N   1 
ATOM   7927  C  CA  . VAL   B 2 724 ? 34.956  67.568  -15.349 1.00 93.25  ? 1028 VAL   B CA  1 
ATOM   7928  C  C   . VAL   B 2 724 ? 34.553  66.920  -14.036 1.00 93.35  ? 1028 VAL   B C   1 
ATOM   7929  O  O   . VAL   B 2 724 ? 35.333  66.161  -13.441 1.00 96.12  ? 1028 VAL   B O   1 
ATOM   7930  C  CB  . VAL   B 2 724 ? 35.167  66.483  -16.414 1.00 88.73  ? 1028 VAL   B CB  1 
ATOM   7931  C  CG1 . VAL   B 2 724 ? 33.823  65.844  -16.729 1.00 90.33  ? 1028 VAL   B CG1 1 
ATOM   7932  C  CG2 . VAL   B 2 724 ? 35.800  67.045  -17.651 1.00 86.81  ? 1028 VAL   B CG2 1 
ATOM   7933  N  N   . LEU   B 2 725 ? 33.336  67.199  -13.601 1.00 90.23  ? 1029 LEU   B N   1 
ATOM   7934  C  CA  . LEU   B 2 725 ? 32.811  66.629  -12.375 1.00 90.84  ? 1029 LEU   B CA  1 
ATOM   7935  C  C   . LEU   B 2 725 ? 31.888  65.477  -12.723 1.00 88.20  ? 1029 LEU   B C   1 
ATOM   7936  O  O   . LEU   B 2 725 ? 31.245  65.477  -13.775 1.00 91.19  ? 1029 LEU   B O   1 
ATOM   7937  C  CB  . LEU   B 2 725 ? 32.062  67.688  -11.568 1.00 87.88  ? 1029 LEU   B CB  1 
ATOM   7938  C  CG  . LEU   B 2 725 ? 32.854  68.958  -11.284 1.00 88.14  ? 1029 LEU   B CG  1 
ATOM   7939  C  CD1 . LEU   B 2 725 ? 32.171  69.718  -10.176 1.00 94.01  ? 1029 LEU   B CD1 1 
ATOM   7940  C  CD2 . LEU   B 2 725 ? 34.294  68.643  -10.917 1.00 90.29  ? 1029 LEU   B CD2 1 
ATOM   7941  N  N   . PHE   B 2 726 ? 31.842  64.481  -11.850 1.00 86.70  ? 1030 PHE   B N   1 
ATOM   7942  C  CA  . PHE   B 2 726 ? 30.977  63.348  -12.107 1.00 86.11  ? 1030 PHE   B CA  1 
ATOM   7943  C  C   . PHE   B 2 726 ? 30.290  62.931  -10.823 1.00 85.74  ? 1030 PHE   B C   1 
ATOM   7944  O  O   . PHE   B 2 726 ? 30.883  62.997  -9.743  1.00 86.26  ? 1030 PHE   B O   1 
ATOM   7945  C  CB  . PHE   B 2 726 ? 31.738  62.163  -12.761 1.00 81.40  ? 1030 PHE   B CB  1 
ATOM   7946  C  CG  . PHE   B 2 726 ? 32.877  61.577  -11.938 1.00 81.69  ? 1030 PHE   B CG  1 
ATOM   7947  C  CD1 . PHE   B 2 726 ? 32.647  60.567  -11.010 1.00 81.30  ? 1030 PHE   B CD1 1 
ATOM   7948  C  CD2 . PHE   B 2 726 ? 34.196  61.974  -12.151 1.00 86.46  ? 1030 PHE   B CD2 1 
ATOM   7949  C  CE1 . PHE   B 2 726 ? 33.707  59.998  -10.284 1.00 81.74  ? 1030 PHE   B CE1 1 
ATOM   7950  C  CE2 . PHE   B 2 726 ? 35.264  61.403  -11.414 1.00 83.47  ? 1030 PHE   B CE2 1 
ATOM   7951  C  CZ  . PHE   B 2 726 ? 35.008  60.422  -10.491 1.00 80.96  ? 1030 PHE   B CZ  1 
ATOM   7952  N  N   . GLY   B 2 727 ? 29.021  62.539  -10.950 1.00 84.21  ? 1031 GLY   B N   1 
ATOM   7953  C  CA  . GLY   B 2 727 ? 28.313  61.851  -9.893  1.00 80.59  ? 1031 GLY   B CA  1 
ATOM   7954  C  C   . GLY   B 2 727 ? 28.176  60.358  -10.172 1.00 81.36  ? 1031 GLY   B C   1 
ATOM   7955  O  O   . GLY   B 2 727 ? 28.222  59.883  -11.310 1.00 79.10  ? 1031 GLY   B O   1 
ATOM   7956  N  N   . THR   B 2 728 ? 27.972  59.606  -9.105  1.00 83.80  ? 1032 THR   B N   1 
ATOM   7957  C  CA  . THR   B 2 728 ? 27.945  58.162  -9.162  1.00 73.18  ? 1032 THR   B CA  1 
ATOM   7958  C  C   . THR   B 2 728 ? 26.739  57.652  -8.406  1.00 77.50  ? 1032 THR   B C   1 
ATOM   7959  O  O   . THR   B 2 728 ? 25.952  58.416  -7.844  1.00 78.40  ? 1032 THR   B O   1 
ATOM   7960  C  CB  . THR   B 2 728 ? 29.220  57.574  -8.574  1.00 78.54  ? 1032 THR   B CB  1 
ATOM   7961  O  OG1 . THR   B 2 728 ? 29.412  58.099  -7.253  1.00 74.42  ? 1032 THR   B OG1 1 
ATOM   7962  C  CG2 . THR   B 2 728 ? 30.410  57.923  -9.455  1.00 77.65  ? 1032 THR   B CG2 1 
ATOM   7963  N  N   . VAL   B 2 729 ? 26.605  56.330  -8.385  1.00 81.66  ? 1033 VAL   B N   1 
ATOM   7964  C  CA  . VAL   B 2 729 ? 25.426  55.754  -7.765  1.00 80.21  ? 1033 VAL   B CA  1 
ATOM   7965  C  C   . VAL   B 2 729 ? 25.550  55.819  -6.254  1.00 79.58  ? 1033 VAL   B C   1 
ATOM   7966  O  O   . VAL   B 2 729 ? 24.546  55.961  -5.545  1.00 77.84  ? 1033 VAL   B O   1 
ATOM   7967  C  CB  . VAL   B 2 729 ? 25.223  54.322  -8.280  1.00 72.96  ? 1033 VAL   B CB  1 
ATOM   7968  C  CG1 . VAL   B 2 729 ? 24.963  54.358  -9.771  1.00 70.44  ? 1033 VAL   B CG1 1 
ATOM   7969  C  CG2 . VAL   B 2 729 ? 26.453  53.505  -7.968  1.00 82.47  ? 1033 VAL   B CG2 1 
ATOM   7970  N  N   . ASN   B 2 730 ? 26.776  55.748  -5.738  1.00 77.70  ? 1034 ASN   B N   1 
ATOM   7971  C  CA  . ASN   B 2 730 ? 27.026  55.768  -4.307  1.00 77.72  ? 1034 ASN   B CA  1 
ATOM   7972  C  C   . ASN   B 2 730 ? 27.130  57.173  -3.748  1.00 81.05  ? 1034 ASN   B C   1 
ATOM   7973  O  O   . ASN   B 2 730 ? 27.622  57.350  -2.623  1.00 78.24  ? 1034 ASN   B O   1 
ATOM   7974  C  CB  . ASN   B 2 730 ? 28.307  54.989  -4.002  1.00 80.77  ? 1034 ASN   B CB  1 
ATOM   7975  C  CG  . ASN   B 2 730 ? 28.178  53.525  -4.311  1.00 83.81  ? 1034 ASN   B CG  1 
ATOM   7976  O  OD1 . ASN   B 2 730 ? 27.586  52.782  -3.540  1.00 89.86  ? 1034 ASN   B OD1 1 
ATOM   7977  N  ND2 . ASN   B 2 730 ? 28.738  53.092  -5.438  1.00 90.66  ? 1034 ASN   B ND2 1 
ATOM   7978  N  N   . GLY   B 2 731 ? 26.677  58.177  -4.502  1.00 83.46  ? 1035 GLY   B N   1 
ATOM   7979  C  CA  . GLY   B 2 731 ? 26.753  59.543  -4.024  1.00 79.26  ? 1035 GLY   B CA  1 
ATOM   7980  C  C   . GLY   B 2 731 ? 28.157  60.068  -3.910  1.00 77.89  ? 1035 GLY   B C   1 
ATOM   7981  O  O   . GLY   B 2 731 ? 28.387  61.041  -3.194  1.00 81.75  ? 1035 GLY   B O   1 
ATOM   7982  N  N   . MET   B 2 732 ? 29.111  59.439  -4.586  1.00 79.96  ? 1036 MET   B N   1 
ATOM   7983  C  CA  . MET   B 2 732 ? 30.466  59.949  -4.648  1.00 80.21  ? 1036 MET   B CA  1 
ATOM   7984  C  C   . MET   B 2 732 ? 30.583  60.943  -5.784  1.00 80.43  ? 1036 MET   B C   1 
ATOM   7985  O  O   . MET   B 2 732 ? 30.050  60.719  -6.872  1.00 86.57  ? 1036 MET   B O   1 
ATOM   7986  C  CB  . MET   B 2 732 ? 31.461  58.815  -4.852  1.00 80.48  ? 1036 MET   B CB  1 
ATOM   7987  C  CG  . MET   B 2 732 ? 32.867  59.300  -5.081  1.00 79.10  ? 1036 MET   B CG  1 
ATOM   7988  S  SD  . MET   B 2 732 ? 33.355  59.332  -6.805  1.00 88.24  ? 1036 MET   B SD  1 
ATOM   7989  C  CE  . MET   B 2 732 ? 35.123  59.117  -6.653  1.00 79.75  ? 1036 MET   B CE  1 
ATOM   7990  N  N   . ILE   B 2 733 ? 31.235  62.058  -5.529  1.00 80.24  ? 1037 ILE   B N   1 
ATOM   7991  C  CA  . ILE   B 2 733 ? 31.416  63.066  -6.566  1.00 85.41  ? 1037 ILE   B CA  1 
ATOM   7992  C  C   . ILE   B 2 733 ? 32.890  63.139  -6.923  1.00 87.91  ? 1037 ILE   B C   1 
ATOM   7993  O  O   . ILE   B 2 733 ? 33.762  63.129  -6.039  1.00 87.90  ? 1037 ILE   B O   1 
ATOM   7994  C  CB  . ILE   B 2 733 ? 30.889  64.453  -6.166  1.00 83.36  ? 1037 ILE   B CB  1 
ATOM   7995  C  CG1 . ILE   B 2 733 ? 29.363  64.465  -6.200  1.00 81.48  ? 1037 ILE   B CG1 1 
ATOM   7996  C  CG2 . ILE   B 2 733 ? 31.437  65.480  -7.104  1.00 79.37  ? 1037 ILE   B CG2 1 
ATOM   7997  C  CD1 . ILE   B 2 733 ? 28.748  65.020  -4.936  1.00 81.23  ? 1037 ILE   B CD1 1 
ATOM   7998  N  N   . GLY   B 2 734 ? 33.164  63.242  -8.225  1.00 88.69  ? 1038 GLY   B N   1 
ATOM   7999  C  CA  . GLY   B 2 734 ? 34.519  63.180  -8.715  1.00 90.52  ? 1038 GLY   B CA  1 
ATOM   8000  C  C   . GLY   B 2 734 ? 34.864  64.336  -9.634  1.00 90.75  ? 1038 GLY   B C   1 
ATOM   8001  O  O   . GLY   B 2 734 ? 34.007  64.920  -10.304 1.00 88.71  ? 1038 GLY   B O   1 
ATOM   8002  N  N   . LEU   B 2 735 ? 36.155  64.633  -9.671  1.00 94.58  ? 1039 LEU   B N   1 
ATOM   8003  C  CA  . LEU   B 2 735 ? 36.724  65.577  -10.613 1.00 94.82  ? 1039 LEU   B CA  1 
ATOM   8004  C  C   . LEU   B 2 735 ? 37.773  64.885  -11.472 1.00 97.79  ? 1039 LEU   B C   1 
ATOM   8005  O  O   . LEU   B 2 735 ? 38.588  64.102  -10.965 1.00 99.95  ? 1039 LEU   B O   1 
ATOM   8006  C  CB  . LEU   B 2 735 ? 37.335  66.751  -9.877  1.00 96.40  ? 1039 LEU   B CB  1 
ATOM   8007  C  CG  . LEU   B 2 735 ? 37.667  67.940  -10.760 1.00 102.02 ? 1039 LEU   B CG  1 
ATOM   8008  C  CD1 . LEU   B 2 735 ? 37.502  69.234  -9.985  1.00 108.09 ? 1039 LEU   B CD1 1 
ATOM   8009  C  CD2 . LEU   B 2 735 ? 39.089  67.827  -11.274 1.00 104.51 ? 1039 LEU   B CD2 1 
ATOM   8010  N  N   . VAL   B 2 736 ? 37.742  65.164  -12.774 1.00 94.86  ? 1040 VAL   B N   1 
ATOM   8011  C  CA  . VAL   B 2 736 ? 38.804  64.763  -13.688 1.00 96.17  ? 1040 VAL   B CA  1 
ATOM   8012  C  C   . VAL   B 2 736 ? 39.392  66.021  -14.309 1.00 103.05 ? 1040 VAL   B C   1 
ATOM   8013  O  O   . VAL   B 2 736 ? 38.655  66.953  -14.658 1.00 101.01 ? 1040 VAL   B O   1 
ATOM   8014  C  CB  . VAL   B 2 736 ? 38.302  63.799  -14.775 1.00 94.87  ? 1040 VAL   B CB  1 
ATOM   8015  C  CG1 . VAL   B 2 736 ? 39.334  63.649  -15.849 1.00 98.28  ? 1040 VAL   B CG1 1 
ATOM   8016  C  CG2 . VAL   B 2 736 ? 38.065  62.459  -14.162 1.00 98.66  ? 1040 VAL   B CG2 1 
ATOM   8017  N  N   . THR   B 2 737 ? 40.724  66.052  -14.429 1.00 106.64 ? 1041 THR   B N   1 
ATOM   8018  C  CA  . THR   B 2 737 ? 41.458  67.166  -15.027 1.00 108.73 ? 1041 THR   B CA  1 
ATOM   8019  C  C   . THR   B 2 737 ? 42.634  66.628  -15.843 1.00 111.46 ? 1041 THR   B C   1 
ATOM   8020  O  O   . THR   B 2 737 ? 43.284  65.650  -15.445 1.00 111.31 ? 1041 THR   B O   1 
ATOM   8021  C  CB  . THR   B 2 737 ? 41.951  68.162  -13.957 1.00 109.74 ? 1041 THR   B CB  1 
ATOM   8022  O  OG1 . THR   B 2 737 ? 42.411  69.355  -14.600 1.00 115.54 ? 1041 THR   B OG1 1 
ATOM   8023  C  CG2 . THR   B 2 737 ? 43.097  67.595  -13.155 1.00 107.37 ? 1041 THR   B CG2 1 
ATOM   8024  N  N   . SER   B 2 738 ? 42.897  67.265  -16.986 1.00 113.59 ? 1042 SER   B N   1 
ATOM   8025  C  CA  . SER   B 2 738 ? 43.909  66.779  -17.918 1.00 113.56 ? 1042 SER   B CA  1 
ATOM   8026  C  C   . SER   B 2 738 ? 45.290  67.314  -17.559 1.00 114.31 ? 1042 SER   B C   1 
ATOM   8027  O  O   . SER   B 2 738 ? 45.446  68.460  -17.128 1.00 114.14 ? 1042 SER   B O   1 
ATOM   8028  C  CB  . SER   B 2 738 ? 43.542  67.174  -19.345 1.00 115.84 ? 1042 SER   B CB  1 
ATOM   8029  O  OG  . SER   B 2 738 ? 42.265  66.650  -19.680 1.00 116.14 ? 1042 SER   B OG  1 
ATOM   8030  N  N   . LEU   B 2 739 ? 46.294  66.468  -17.741 1.00 116.63 ? 1043 LEU   B N   1 
ATOM   8031  C  CA  . LEU   B 2 739 ? 47.640  66.726  -17.259 1.00 120.24 ? 1043 LEU   B CA  1 
ATOM   8032  C  C   . LEU   B 2 739 ? 48.603  66.946  -18.409 1.00 122.22 ? 1043 LEU   B C   1 
ATOM   8033  O  O   . LEU   B 2 739 ? 48.272  66.748  -19.580 1.00 123.05 ? 1043 LEU   B O   1 
ATOM   8034  C  CB  . LEU   B 2 739 ? 48.135  65.565  -16.400 1.00 118.42 ? 1043 LEU   B CB  1 
ATOM   8035  C  CG  . LEU   B 2 739 ? 47.679  65.684  -14.961 1.00 114.23 ? 1043 LEU   B CG  1 
ATOM   8036  C  CD1 . LEU   B 2 739 ? 48.514  64.747  -14.105 1.00 116.58 ? 1043 LEU   B CD1 1 
ATOM   8037  C  CD2 . LEU   B 2 739 ? 47.822  67.133  -14.519 1.00 117.49 ? 1043 LEU   B CD2 1 
ATOM   8038  N  N   . SER   B 2 740 ? 49.829  67.315  -18.039 1.00 128.02 ? 1044 SER   B N   1 
ATOM   8039  C  CA  . SER   B 2 740 ? 50.891  67.654  -18.978 1.00 131.68 ? 1044 SER   B CA  1 
ATOM   8040  C  C   . SER   B 2 740 ? 51.962  66.577  -18.948 1.00 134.03 ? 1044 SER   B C   1 
ATOM   8041  O  O   . SER   B 2 740 ? 52.438  66.209  -17.868 1.00 136.51 ? 1044 SER   B O   1 
ATOM   8042  C  CB  . SER   B 2 740 ? 51.508  69.004  -18.631 1.00 127.82 ? 1044 SER   B CB  1 
ATOM   8043  O  OG  . SER   B 2 740 ? 50.495  69.891  -18.202 1.00 128.93 ? 1044 SER   B OG  1 
ATOM   8044  N  N   . GLU   B 2 741 ? 52.352  66.098  -20.135 1.00 136.35 ? 1045 GLU   B N   1 
ATOM   8045  C  CA  . GLU   B 2 741 ? 53.234  64.939  -20.243 1.00 134.01 ? 1045 GLU   B CA  1 
ATOM   8046  C  C   . GLU   B 2 741 ? 54.320  64.965  -19.182 1.00 133.83 ? 1045 GLU   B C   1 
ATOM   8047  O  O   . GLU   B 2 741 ? 54.595  63.955  -18.532 1.00 129.26 ? 1045 GLU   B O   1 
ATOM   8048  C  CB  . GLU   B 2 741 ? 53.850  64.871  -21.643 1.00 134.83 ? 1045 GLU   B CB  1 
ATOM   8049  C  CG  . GLU   B 2 741 ? 54.911  63.786  -21.761 1.00 136.51 ? 1045 GLU   B CG  1 
ATOM   8050  C  CD  . GLU   B 2 741 ? 55.125  63.288  -23.185 1.00 138.45 ? 1045 GLU   B CD  1 
ATOM   8051  O  OE1 . GLU   B 2 741 ? 55.028  64.096  -24.137 1.00 138.34 ? 1045 GLU   B OE1 1 
ATOM   8052  O  OE2 . GLU   B 2 741 ? 55.396  62.073  -23.344 1.00 141.42 ? 1045 GLU   B OE2 1 
ATOM   8053  N  N   . SER   B 2 742 ? 54.939  66.124  -18.976 1.00 151.88 ? 1046 SER   B N   1 
ATOM   8054  C  CA  . SER   B 2 742 ? 55.884  66.241  -17.876 1.00 154.09 ? 1046 SER   B CA  1 
ATOM   8055  C  C   . SER   B 2 742 ? 55.203  65.927  -16.549 1.00 152.25 ? 1046 SER   B C   1 
ATOM   8056  O  O   . SER   B 2 742 ? 55.651  65.053  -15.796 1.00 150.17 ? 1046 SER   B O   1 
ATOM   8057  C  CB  . SER   B 2 742 ? 56.499  67.638  -17.856 1.00 159.50 ? 1046 SER   B CB  1 
ATOM   8058  O  OG  . SER   B 2 742 ? 57.304  67.814  -16.701 1.00 166.13 ? 1046 SER   B OG  1 
ATOM   8059  N  N   . TRP   B 2 743 ? 54.106  66.631  -16.248 1.00 138.24 ? 1047 TRP   B N   1 
ATOM   8060  C  CA  . TRP   B 2 743 ? 53.445  66.456  -14.959 1.00 133.96 ? 1047 TRP   B CA  1 
ATOM   8061  C  C   . TRP   B 2 743 ? 53.106  64.987  -14.712 1.00 130.66 ? 1047 TRP   B C   1 
ATOM   8062  O  O   . TRP   B 2 743 ? 53.488  64.412  -13.683 1.00 124.05 ? 1047 TRP   B O   1 
ATOM   8063  C  CB  . TRP   B 2 743 ? 52.190  67.326  -14.893 1.00 130.89 ? 1047 TRP   B CB  1 
ATOM   8064  C  CG  . TRP   B 2 743 ? 52.434  68.810  -14.645 1.00 136.41 ? 1047 TRP   B CG  1 
ATOM   8065  C  CD1 . TRP   B 2 743 ? 52.315  69.831  -15.553 1.00 137.72 ? 1047 TRP   B CD1 1 
ATOM   8066  C  CD2 . TRP   B 2 743 ? 52.806  69.429  -13.401 1.00 133.65 ? 1047 TRP   B CD2 1 
ATOM   8067  N  NE1 . TRP   B 2 743 ? 52.599  71.038  -14.953 1.00 136.79 ? 1047 TRP   B NE1 1 
ATOM   8068  C  CE2 . TRP   B 2 743 ? 52.902  70.818  -13.634 1.00 135.06 ? 1047 TRP   B CE2 1 
ATOM   8069  C  CE3 . TRP   B 2 743 ? 53.072  68.942  -12.118 1.00 127.58 ? 1047 TRP   B CE3 1 
ATOM   8070  C  CZ2 . TRP   B 2 743 ? 53.250  71.719  -12.630 1.00 135.18 ? 1047 TRP   B CZ2 1 
ATOM   8071  C  CZ3 . TRP   B 2 743 ? 53.418  69.836  -11.128 1.00 123.77 ? 1047 TRP   B CZ3 1 
ATOM   8072  C  CH2 . TRP   B 2 743 ? 53.503  71.206  -11.387 1.00 130.08 ? 1047 TRP   B CH2 1 
ATOM   8073  N  N   . TYR   B 2 744 ? 52.423  64.355  -15.677 1.00 130.47 ? 1048 TYR   B N   1 
ATOM   8074  C  CA  . TYR   B 2 744 ? 51.994  62.966  -15.525 1.00 122.90 ? 1048 TYR   B CA  1 
ATOM   8075  C  C   . TYR   B 2 744 ? 53.155  62.064  -15.122 1.00 123.49 ? 1048 TYR   B C   1 
ATOM   8076  O  O   . TYR   B 2 744 ? 53.020  61.235  -14.212 1.00 122.79 ? 1048 TYR   B O   1 
ATOM   8077  C  CB  . TYR   B 2 744 ? 51.345  62.470  -16.821 1.00 117.73 ? 1048 TYR   B CB  1 
ATOM   8078  C  CG  . TYR   B 2 744 ? 51.018  60.981  -16.826 1.00 119.57 ? 1048 TYR   B CG  1 
ATOM   8079  C  CD1 . TYR   B 2 744 ? 49.931  60.483  -16.121 1.00 114.45 ? 1048 TYR   B CD1 1 
ATOM   8080  C  CD2 . TYR   B 2 744 ? 51.800  60.077  -17.547 1.00 116.16 ? 1048 TYR   B CD2 1 
ATOM   8081  C  CE1 . TYR   B 2 744 ? 49.634  59.122  -16.135 1.00 111.55 ? 1048 TYR   B CE1 1 
ATOM   8082  C  CE2 . TYR   B 2 744 ? 51.513  58.730  -17.565 1.00 110.64 ? 1048 TYR   B CE2 1 
ATOM   8083  C  CZ  . TYR   B 2 744 ? 50.429  58.252  -16.860 1.00 111.64 ? 1048 TYR   B CZ  1 
ATOM   8084  O  OH  . TYR   B 2 744 ? 50.135  56.897  -16.883 1.00 114.59 ? 1048 TYR   B OH  1 
ATOM   8085  N  N   . ASN   B 2 745 ? 54.310  62.211  -15.788 1.00 127.27 ? 1049 ASN   B N   1 
ATOM   8086  C  CA  . ASN   B 2 745 ? 55.463  61.368  -15.469 1.00 124.95 ? 1049 ASN   B CA  1 
ATOM   8087  C  C   . ASN   B 2 745 ? 55.903  61.579  -14.030 1.00 122.82 ? 1049 ASN   B C   1 
ATOM   8088  O  O   . ASN   B 2 745 ? 56.110  60.616  -13.280 1.00 123.81 ? 1049 ASN   B O   1 
ATOM   8089  C  CB  . ASN   B 2 745 ? 56.632  61.662  -16.410 1.00 124.05 ? 1049 ASN   B CB  1 
ATOM   8090  C  CG  . ASN   B 2 745 ? 56.284  61.464  -17.864 1.00 125.75 ? 1049 ASN   B CG  1 
ATOM   8091  O  OD1 . ASN   B 2 745 ? 56.538  62.338  -18.696 1.00 125.93 ? 1049 ASN   B OD1 1 
ATOM   8092  N  ND2 . ASN   B 2 745 ? 55.703  60.310  -18.186 1.00 122.51 ? 1049 ASN   B ND2 1 
ATOM   8093  N  N   . LEU   B 2 746 ? 56.051  62.844  -13.632 1.00 122.74 ? 1050 LEU   B N   1 
ATOM   8094  C  CA  . LEU   B 2 746 ? 56.502  63.171  -12.284 1.00 122.18 ? 1050 LEU   B CA  1 
ATOM   8095  C  C   . LEU   B 2 746 ? 55.574  62.565  -11.237 1.00 121.28 ? 1050 LEU   B C   1 
ATOM   8096  O  O   . LEU   B 2 746 ? 56.026  61.891  -10.299 1.00 116.92 ? 1050 LEU   B O   1 
ATOM   8097  C  CB  . LEU   B 2 746 ? 56.587  64.691  -12.138 1.00 121.51 ? 1050 LEU   B CB  1 
ATOM   8098  C  CG  . LEU   B 2 746 ? 57.051  65.241  -10.796 1.00 118.58 ? 1050 LEU   B CG  1 
ATOM   8099  C  CD1 . LEU   B 2 746 ? 55.853  65.459  -9.878  1.00 114.87 ? 1050 LEU   B CD1 1 
ATOM   8100  C  CD2 . LEU   B 2 746 ? 58.073  64.278  -10.181 1.00 112.38 ? 1050 LEU   B CD2 1 
ATOM   8101  N  N   . LEU   B 2 747 ? 54.263  62.792  -11.395 1.00 118.74 ? 1051 LEU   B N   1 
ATOM   8102  C  CA  . LEU   B 2 747 ? 53.272  62.206  -10.497 1.00 115.17 ? 1051 LEU   B CA  1 
ATOM   8103  C  C   . LEU   B 2 747 ? 53.358  60.685  -10.492 1.00 120.06 ? 1051 LEU   B C   1 
ATOM   8104  O  O   . LEU   B 2 747 ? 53.282  60.051  -9.429  1.00 121.90 ? 1051 LEU   B O   1 
ATOM   8105  C  CB  . LEU   B 2 747 ? 51.868  62.653  -10.900 1.00 112.95 ? 1051 LEU   B CB  1 
ATOM   8106  C  CG  . LEU   B 2 747 ? 51.499  64.059  -10.468 1.00 108.58 ? 1051 LEU   B CG  1 
ATOM   8107  C  CD1 . LEU   B 2 747 ? 51.570  64.162  -8.949  1.00 103.45 ? 1051 LEU   B CD1 1 
ATOM   8108  C  CD2 . LEU   B 2 747 ? 52.433  65.055  -11.149 1.00 119.04 ? 1051 LEU   B CD2 1 
ATOM   8109  N  N   . LEU   B 2 748 ? 53.470  60.076  -11.677 1.00 118.46 ? 1052 LEU   B N   1 
ATOM   8110  C  CA  . LEU   B 2 748 ? 53.609  58.629  -11.749 1.00 118.66 ? 1052 LEU   B CA  1 
ATOM   8111  C  C   . LEU   B 2 748 ? 54.615  58.142  -10.718 1.00 121.37 ? 1052 LEU   B C   1 
ATOM   8112  O  O   . LEU   B 2 748 ? 54.329  57.238  -9.921  1.00 119.65 ? 1052 LEU   B O   1 
ATOM   8113  C  CB  . LEU   B 2 748 ? 54.024  58.213  -13.157 1.00 114.58 ? 1052 LEU   B CB  1 
ATOM   8114  C  CG  . LEU   B 2 748 ? 52.790  57.963  -14.000 1.00 113.39 ? 1052 LEU   B CG  1 
ATOM   8115  C  CD1 . LEU   B 2 748 ? 53.168  57.151  -15.197 1.00 117.51 ? 1052 LEU   B CD1 1 
ATOM   8116  C  CD2 . LEU   B 2 748 ? 51.793  57.231  -13.145 1.00 111.27 ? 1052 LEU   B CD2 1 
ATOM   8117  N  N   . ASP   B 2 749 ? 55.792  58.776  -10.698 1.00 120.40 ? 1053 ASP   B N   1 
ATOM   8118  C  CA  . ASP   B 2 749 ? 56.833  58.404  -9.743  1.00 125.27 ? 1053 ASP   B CA  1 
ATOM   8119  C  C   . ASP   B 2 749 ? 56.356  58.605  -8.309  1.00 123.90 ? 1053 ASP   B C   1 
ATOM   8120  O  O   . ASP   B 2 749 ? 56.510  57.715  -7.461  1.00 124.37 ? 1053 ASP   B O   1 
ATOM   8121  C  CB  . ASP   B 2 749 ? 58.113  59.206  -10.010 1.00 127.55 ? 1053 ASP   B CB  1 
ATOM   8122  C  CG  . ASP   B 2 749 ? 59.388  58.385  -9.768  1.00 133.14 ? 1053 ASP   B CG  1 
ATOM   8123  O  OD1 . ASP   B 2 749 ? 59.459  57.231  -10.269 1.00 134.79 ? 1053 ASP   B OD1 1 
ATOM   8124  O  OD2 . ASP   B 2 749 ? 60.301  58.877  -9.057  1.00 135.41 ? 1053 ASP   B OD2 1 
ATOM   8125  N  N   . MET   B 2 750 ? 55.779  59.773  -8.016  1.00 119.80 ? 1054 MET   B N   1 
ATOM   8126  C  CA  . MET   B 2 750 ? 55.197  60.010  -6.699  1.00 118.76 ? 1054 MET   B CA  1 
ATOM   8127  C  C   . MET   B 2 750 ? 54.329  58.834  -6.263  1.00 118.18 ? 1054 MET   B C   1 
ATOM   8128  O  O   . MET   B 2 750 ? 54.530  58.253  -5.186  1.00 114.14 ? 1054 MET   B O   1 
ATOM   8129  C  CB  . MET   B 2 750 ? 54.377  61.298  -6.723  1.00 117.93 ? 1054 MET   B CB  1 
ATOM   8130  C  CG  . MET   B 2 750 ? 55.228  62.542  -6.686  1.00 121.10 ? 1054 MET   B CG  1 
ATOM   8131  S  SD  . MET   B 2 750 ? 56.184  62.561  -5.156  1.00 140.40 ? 1054 MET   B SD  1 
ATOM   8132  C  CE  . MET   B 2 750 ? 54.873  62.651  -3.931  1.00 127.41 ? 1054 MET   B CE  1 
ATOM   8133  N  N   . GLN   B 2 751 ? 53.349  58.479  -7.101  1.00 116.38 ? 1055 GLN   B N   1 
ATOM   8134  C  CA  . GLN   B 2 751 ? 52.431  57.386  -6.804  1.00 114.01 ? 1055 GLN   B CA  1 
ATOM   8135  C  C   . GLN   B 2 751 ? 53.176  56.163  -6.269  1.00 112.39 ? 1055 GLN   B C   1 
ATOM   8136  O  O   . GLN   B 2 751 ? 52.894  55.671  -5.170  1.00 111.88 ? 1055 GLN   B O   1 
ATOM   8137  C  CB  . GLN   B 2 751 ? 51.616  57.051  -8.065  1.00 110.40 ? 1055 GLN   B CB  1 
ATOM   8138  C  CG  . GLN   B 2 751 ? 50.104  57.240  -7.880  1.00 105.15 ? 1055 GLN   B CG  1 
ATOM   8139  C  CD  . GLN   B 2 751 ? 49.300  57.154  -9.179  1.00 105.25 ? 1055 GLN   B CD  1 
ATOM   8140  O  OE1 . GLN   B 2 751 ? 48.914  58.177  -9.751  1.00 102.39 ? 1055 GLN   B OE1 1 
ATOM   8141  N  NE2 . GLN   B 2 751 ? 49.020  55.925  -9.633  1.00 104.89 ? 1055 GLN   B NE2 1 
ATOM   8142  N  N   . ASN   B 2 752 ? 54.153  55.675  -7.029  1.00 112.10 ? 1056 ASN   B N   1 
ATOM   8143  C  CA  . ASN   B 2 752 ? 54.905  54.515  -6.572  1.00 113.40 ? 1056 ASN   B CA  1 
ATOM   8144  C  C   . ASN   B 2 752 ? 55.746  54.860  -5.355  1.00 117.89 ? 1056 ASN   B C   1 
ATOM   8145  O  O   . ASN   B 2 752 ? 55.749  54.121  -4.362  1.00 114.19 ? 1056 ASN   B O   1 
ATOM   8146  C  CB  . ASN   B 2 752 ? 55.776  53.986  -7.706  1.00 114.06 ? 1056 ASN   B CB  1 
ATOM   8147  C  CG  . ASN   B 2 752 ? 54.983  53.753  -8.975  1.00 120.46 ? 1056 ASN   B CG  1 
ATOM   8148  O  OD1 . ASN   B 2 752 ? 55.148  54.478  -9.960  1.00 120.97 ? 1056 ASN   B OD1 1 
ATOM   8149  N  ND2 . ASN   B 2 752 ? 54.101  52.743  -8.955  1.00 113.73 ? 1056 ASN   B ND2 1 
ATOM   8150  N  N   . ARG   B 2 753 ? 56.466  55.982  -5.416  1.00 120.84 ? 1057 ARG   B N   1 
ATOM   8151  C  CA  . ARG   B 2 753 ? 57.188  56.462  -4.247  1.00 119.42 ? 1057 ARG   B CA  1 
ATOM   8152  C  C   . ARG   B 2 753 ? 56.311  56.368  -3.012  1.00 119.43 ? 1057 ARG   B C   1 
ATOM   8153  O  O   . ARG   B 2 753 ? 56.701  55.768  -2.003  1.00 118.18 ? 1057 ARG   B O   1 
ATOM   8154  C  CB  . ARG   B 2 753 ? 57.651  57.903  -4.462  1.00 125.01 ? 1057 ARG   B CB  1 
ATOM   8155  C  CG  . ARG   B 2 753 ? 58.717  58.108  -5.517  1.00 124.71 ? 1057 ARG   B CG  1 
ATOM   8156  C  CD  . ARG   B 2 753 ? 60.105  57.945  -4.939  1.00 127.43 ? 1057 ARG   B CD  1 
ATOM   8157  N  NE  . ARG   B 2 753 ? 61.121  58.416  -5.868  1.00 131.64 ? 1057 ARG   B NE  1 
ATOM   8158  C  CZ  . ARG   B 2 753 ? 61.927  59.442  -5.638  1.00 144.03 ? 1057 ARG   B CZ  1 
ATOM   8159  N  NH1 . ARG   B 2 753 ? 61.873  60.127  -4.508  1.00 145.96 ? 1057 ARG   B NH1 1 
ATOM   8160  N  NH2 . ARG   B 2 753 ? 62.819  59.784  -6.563  1.00 152.03 ? 1057 ARG   B NH2 1 
ATOM   8161  N  N   . LEU   B 2 754 ? 55.106  56.943  -3.085  1.00 117.95 ? 1058 LEU   B N   1 
ATOM   8162  C  CA  . LEU   B 2 754 ? 54.193  56.867  -1.952  1.00 117.32 ? 1058 LEU   B CA  1 
ATOM   8163  C  C   . LEU   B 2 754 ? 53.827  55.425  -1.644  1.00 115.44 ? 1058 LEU   B C   1 
ATOM   8164  O  O   . LEU   B 2 754 ? 53.955  54.979  -0.500  1.00 116.20 ? 1058 LEU   B O   1 
ATOM   8165  C  CB  . LEU   B 2 754 ? 52.933  57.687  -2.205  1.00 112.74 ? 1058 LEU   B CB  1 
ATOM   8166  C  CG  . LEU   B 2 754 ? 53.146  59.011  -2.895  1.00 110.88 ? 1058 LEU   B CG  1 
ATOM   8167  C  CD1 . LEU   B 2 754 ? 51.885  59.815  -2.752  1.00 111.07 ? 1058 LEU   B CD1 1 
ATOM   8168  C  CD2 . LEU   B 2 754 ? 54.322  59.721  -2.294  1.00 117.65 ? 1058 LEU   B CD2 1 
ATOM   8169  N  N   . ASN   B 2 755 ? 53.387  54.671  -2.656  1.00 111.66 ? 1059 ASN   B N   1 
ATOM   8170  C  CA  . ASN   B 2 755 ? 52.849  53.338  -2.386  1.00 115.90 ? 1059 ASN   B CA  1 
ATOM   8171  C  C   . ASN   B 2 755 ? 53.741  52.501  -1.467  1.00 116.94 ? 1059 ASN   B C   1 
ATOM   8172  O  O   . ASN   B 2 755 ? 53.242  51.575  -0.813  1.00 110.43 ? 1059 ASN   B O   1 
ATOM   8173  C  CB  . ASN   B 2 755 ? 52.578  52.610  -3.700  1.00 110.56 ? 1059 ASN   B CB  1 
ATOM   8174  C  CG  . ASN   B 2 755 ? 51.276  53.052  -4.324  1.00 109.06 ? 1059 ASN   B CG  1 
ATOM   8175  O  OD1 . ASN   B 2 755 ? 50.240  53.077  -3.655  1.00 104.93 ? 1059 ASN   B OD1 1 
ATOM   8176  N  ND2 . ASN   B 2 755 ? 51.326  53.457  -5.589  1.00 110.70 ? 1059 ASN   B ND2 1 
ATOM   8177  N  N   . LYS   B 2 756 ? 55.035  52.851  -1.373  1.00 119.61 ? 1060 LYS   B N   1 
ATOM   8178  C  CA  . LYS   B 2 756 ? 55.963  52.228  -0.428  1.00 116.09 ? 1060 LYS   B CA  1 
ATOM   8179  C  C   . LYS   B 2 756 ? 55.686  52.632  1.011   1.00 114.63 ? 1060 LYS   B C   1 
ATOM   8180  O  O   . LYS   B 2 756 ? 55.819  51.804  1.915   1.00 119.42 ? 1060 LYS   B O   1 
ATOM   8181  C  CB  . LYS   B 2 756 ? 57.409  52.575  -0.803  1.00 114.29 ? 1060 LYS   B CB  1 
ATOM   8182  C  CG  . LYS   B 2 756 ? 57.928  51.838  -2.038  1.00 124.71 ? 1060 LYS   B CG  1 
ATOM   8183  C  CD  . LYS   B 2 756 ? 58.534  52.776  -3.082  1.00 126.87 ? 1060 LYS   B CD  1 
ATOM   8184  C  CE  . LYS   B 2 756 ? 59.219  51.970  -4.190  1.00 125.56 ? 1060 LYS   B CE  1 
ATOM   8185  N  NZ  . LYS   B 2 756 ? 60.536  52.571  -4.574  1.00 133.70 ? 1060 LYS   B NZ  1 
ATOM   8186  N  N   . VAL   B 2 757 ? 55.295  53.879  1.264   1.00 112.96 ? 1061 VAL   B N   1 
ATOM   8187  C  CA  . VAL   B 2 757 ? 55.159  54.347  2.642   1.00 110.52 ? 1061 VAL   B CA  1 
ATOM   8188  C  C   . VAL   B 2 757 ? 53.716  54.253  3.129   1.00 110.88 ? 1061 VAL   B C   1 
ATOM   8189  O  O   . VAL   B 2 757 ? 53.487  53.922  4.289   1.00 115.47 ? 1061 VAL   B O   1 
ATOM   8190  C  CB  . VAL   B 2 757 ? 55.728  55.785  2.821   1.00 114.93 ? 1061 VAL   B CB  1 
ATOM   8191  C  CG1 . VAL   B 2 757 ? 57.049  55.938  2.099   1.00 116.90 ? 1061 VAL   B CG1 1 
ATOM   8192  C  CG2 . VAL   B 2 757 ? 54.724  56.861  2.376   1.00 115.58 ? 1061 VAL   B CG2 1 
ATOM   8193  N  N   . ILE   B 2 758 ? 52.736  54.544  2.267   1.00 108.28 ? 1062 ILE   B N   1 
ATOM   8194  C  CA  . ILE   B 2 758 ? 51.339  54.542  2.708   1.00 108.84 ? 1062 ILE   B CA  1 
ATOM   8195  C  C   . ILE   B 2 758 ? 50.860  53.107  2.873   1.00 106.41 ? 1062 ILE   B C   1 
ATOM   8196  O  O   . ILE   B 2 758 ? 50.998  52.275  1.966   1.00 109.01 ? 1062 ILE   B O   1 
ATOM   8197  C  CB  . ILE   B 2 758 ? 50.429  55.329  1.748   1.00 107.89 ? 1062 ILE   B CB  1 
ATOM   8198  C  CG1 . ILE   B 2 758 ? 50.892  56.761  1.663   1.00 110.21 ? 1062 ILE   B CG1 1 
ATOM   8199  C  CG2 . ILE   B 2 758 ? 49.064  55.466  2.287   1.00 106.43 ? 1062 ILE   B CG2 1 
ATOM   8200  C  CD1 . ILE   B 2 758 ? 51.953  56.901  0.554   1.00 113.54 ? 1062 ILE   B CD1 1 
ATOM   8201  N  N   . LYS   B 2 759 ? 50.277  52.824  4.032   1.00 102.08 ? 1063 LYS   B N   1 
ATOM   8202  C  CA  . LYS   B 2 759 ? 49.987  51.467  4.463   1.00 102.53 ? 1063 LYS   B CA  1 
ATOM   8203  C  C   . LYS   B 2 759 ? 48.556  51.114  4.068   1.00 108.42 ? 1063 LYS   B C   1 
ATOM   8204  O  O   . LYS   B 2 759 ? 47.634  51.902  4.310   1.00 109.66 ? 1063 LYS   B O   1 
ATOM   8205  C  CB  . LYS   B 2 759 ? 50.200  51.339  5.976   1.00 95.46  ? 1063 LYS   B CB  1 
ATOM   8206  N  N   . SER   B 2 760 ? 48.381  49.956  3.418   1.00 103.01 ? 1064 SER   B N   1 
ATOM   8207  C  CA  . SER   B 2 760 ? 47.063  49.510  2.986   1.00 98.26  ? 1064 SER   B CA  1 
ATOM   8208  C  C   . SER   B 2 760 ? 46.329  48.860  4.149   1.00 98.70  ? 1064 SER   B C   1 
ATOM   8209  O  O   . SER   B 2 760 ? 46.944  48.340  5.081   1.00 109.32 ? 1064 SER   B O   1 
ATOM   8210  C  CB  . SER   B 2 760 ? 47.172  48.511  1.836   1.00 97.59  ? 1064 SER   B CB  1 
ATOM   8211  O  OG  . SER   B 2 760 ? 45.968  47.763  1.700   1.00 101.32 ? 1064 SER   B OG  1 
ATOM   8212  N  N   . VAL   B 2 761 ? 44.999  48.873  4.086   1.00 95.71  ? 1065 VAL   B N   1 
ATOM   8213  C  CA  . VAL   B 2 761 ? 44.225  48.387  5.225   1.00 99.20  ? 1065 VAL   B CA  1 
ATOM   8214  C  C   . VAL   B 2 761 ? 44.029  46.880  5.159   1.00 101.53 ? 1065 VAL   B C   1 
ATOM   8215  O  O   . VAL   B 2 761 ? 44.018  46.190  6.186   1.00 105.36 ? 1065 VAL   B O   1 
ATOM   8216  C  CB  . VAL   B 2 761 ? 42.889  49.136  5.293   1.00 100.29 ? 1065 VAL   B CB  1 
ATOM   8217  C  CG1 . VAL   B 2 761 ? 42.023  48.574  6.409   1.00 96.39  ? 1065 VAL   B CG1 1 
ATOM   8218  C  CG2 . VAL   B 2 761 ? 43.180  50.607  5.489   1.00 94.95  ? 1065 VAL   B CG2 1 
ATOM   8219  N  N   . GLY   B 2 762 ? 43.856  46.340  3.969   1.00 99.24  ? 1066 GLY   B N   1 
ATOM   8220  C  CA  . GLY   B 2 762 ? 43.840  44.899  3.852   1.00 98.10  ? 1066 GLY   B CA  1 
ATOM   8221  C  C   . GLY   B 2 762 ? 45.183  44.413  3.358   1.00 95.73  ? 1066 GLY   B C   1 
ATOM   8222  O  O   . GLY   B 2 762 ? 45.314  43.273  2.907   1.00 97.00  ? 1066 GLY   B O   1 
ATOM   8223  N  N   . LYS   B 2 763 ? 46.192  45.274  3.455   1.00 91.71  ? 1067 LYS   B N   1 
ATOM   8224  C  CA  . LYS   B 2 763 ? 47.432  45.072  2.728   1.00 93.94  ? 1067 LYS   B CA  1 
ATOM   8225  C  C   . LYS   B 2 763 ? 47.117  44.796  1.262   1.00 94.60  ? 1067 LYS   B C   1 
ATOM   8226  O  O   . LYS   B 2 763 ? 47.395  43.721  0.717   1.00 95.22  ? 1067 LYS   B O   1 
ATOM   8227  C  CB  . LYS   B 2 763 ? 48.262  43.946  3.333   1.00 97.97  ? 1067 LYS   B CB  1 
ATOM   8228  C  CG  . LYS   B 2 763 ? 48.740  44.203  4.766   1.00 105.19 ? 1067 LYS   B CG  1 
ATOM   8229  C  CD  . LYS   B 2 763 ? 50.173  43.699  4.971   1.00 109.30 ? 1067 LYS   B CD  1 
ATOM   8230  C  CE  . LYS   B 2 763 ? 50.338  42.911  6.265   1.00 109.42 ? 1067 LYS   B CE  1 
ATOM   8231  N  NZ  . LYS   B 2 763 ? 51.591  42.083  6.252   1.00 112.34 ? 1067 LYS   B NZ  1 
ATOM   8232  N  N   . ILE   B 2 764 ? 46.482  45.782  0.633   1.00 94.27  ? 1068 ILE   B N   1 
ATOM   8233  C  CA  . ILE   B 2 764 ? 46.074  45.707  -0.757  1.00 88.18  ? 1068 ILE   B CA  1 
ATOM   8234  C  C   . ILE   B 2 764 ? 46.973  46.629  -1.570  1.00 92.02  ? 1068 ILE   B C   1 
ATOM   8235  O  O   . ILE   B 2 764 ? 47.251  47.766  -1.164  1.00 95.17  ? 1068 ILE   B O   1 
ATOM   8236  C  CB  . ILE   B 2 764 ? 44.584  46.071  -0.897  1.00 88.88  ? 1068 ILE   B CB  1 
ATOM   8237  C  CG1 . ILE   B 2 764 ? 43.758  45.185  0.030   1.00 89.40  ? 1068 ILE   B CG1 1 
ATOM   8238  C  CG2 . ILE   B 2 764 ? 44.124  45.902  -2.323  1.00 87.26  ? 1068 ILE   B CG2 1 
ATOM   8239  C  CD1 . ILE   B 2 764 ? 42.293  45.081  -0.365  1.00 86.27  ? 1068 ILE   B CD1 1 
ATOM   8240  N  N   . GLU   B 2 765 ? 47.457  46.130  -2.706  1.00 90.56  ? 1069 GLU   B N   1 
ATOM   8241  C  CA  . GLU   B 2 765 ? 48.340  46.916  -3.565  1.00 91.74  ? 1069 GLU   B CA  1 
ATOM   8242  C  C   . GLU   B 2 765 ? 47.549  47.968  -4.330  1.00 92.25  ? 1069 GLU   B C   1 
ATOM   8243  O  O   . GLU   B 2 765 ? 46.639  47.637  -5.101  1.00 87.63  ? 1069 GLU   B O   1 
ATOM   8244  C  CB  . GLU   B 2 765 ? 49.071  46.018  -4.559  1.00 92.25  ? 1069 GLU   B CB  1 
ATOM   8245  C  CG  . GLU   B 2 765 ? 50.072  45.068  -3.959  1.00 102.12 ? 1069 GLU   B CG  1 
ATOM   8246  C  CD  . GLU   B 2 765 ? 51.231  45.790  -3.309  1.00 109.31 ? 1069 GLU   B CD  1 
ATOM   8247  O  OE1 . GLU   B 2 765 ? 51.410  47.005  -3.589  1.00 113.28 ? 1069 GLU   B OE1 1 
ATOM   8248  O  OE2 . GLU   B 2 765 ? 51.958  45.141  -2.519  1.00 112.48 ? 1069 GLU   B OE2 1 
ATOM   8249  N  N   . HIS   B 2 766 ? 47.924  49.229  -4.150  1.00 92.06  ? 1070 HIS   B N   1 
ATOM   8250  C  CA  . HIS   B 2 766 ? 47.307  50.298  -4.917  1.00 94.50  ? 1070 HIS   B CA  1 
ATOM   8251  C  C   . HIS   B 2 766 ? 47.176  49.922  -6.392  1.00 96.07  ? 1070 HIS   B C   1 
ATOM   8252  O  O   . HIS   B 2 766 ? 46.136  50.191  -7.004  1.00 96.63  ? 1070 HIS   B O   1 
ATOM   8253  C  CB  . HIS   B 2 766 ? 48.105  51.594  -4.755  1.00 97.88  ? 1070 HIS   B CB  1 
ATOM   8254  C  CG  . HIS   B 2 766 ? 47.644  52.704  -5.650  1.00 97.71  ? 1070 HIS   B CG  1 
ATOM   8255  N  ND1 . HIS   B 2 766 ? 48.228  52.967  -6.873  1.00 101.23 ? 1070 HIS   B ND1 1 
ATOM   8256  C  CD2 . HIS   B 2 766 ? 46.644  53.607  -5.508  1.00 92.04  ? 1070 HIS   B CD2 1 
ATOM   8257  C  CE1 . HIS   B 2 766 ? 47.608  53.988  -7.442  1.00 101.85 ? 1070 HIS   B CE1 1 
ATOM   8258  N  NE2 . HIS   B 2 766 ? 46.646  54.395  -6.633  1.00 94.57  ? 1070 HIS   B NE2 1 
ATOM   8259  N  N   . SER   B 2 767 ? 48.201  49.287  -6.980  1.00 97.88  ? 1071 SER   B N   1 
ATOM   8260  C  CA  . SER   B 2 767 ? 48.163  49.011  -8.416  1.00 98.17  ? 1071 SER   B CA  1 
ATOM   8261  C  C   . SER   B 2 767 ? 47.152  47.911  -8.762  1.00 97.34  ? 1071 SER   B C   1 
ATOM   8262  O  O   . SER   B 2 767 ? 46.457  47.995  -9.786  1.00 97.29  ? 1071 SER   B O   1 
ATOM   8263  C  CB  . SER   B 2 767 ? 49.559  48.652  -8.921  1.00 100.76 ? 1071 SER   B CB  1 
ATOM   8264  O  OG  . SER   B 2 767 ? 50.481  49.678  -8.591  1.00 114.89 ? 1071 SER   B OG  1 
ATOM   8265  N  N   . PHE   B 2 768 ? 47.058  46.864  -7.937  1.00 92.17  ? 1072 PHE   B N   1 
ATOM   8266  C  CA  . PHE   B 2 768 ? 45.980  45.899  -8.112  1.00 84.53  ? 1072 PHE   B CA  1 
ATOM   8267  C  C   . PHE   B 2 768 ? 44.632  46.608  -8.128  1.00 87.17  ? 1072 PHE   B C   1 
ATOM   8268  O  O   . PHE   B 2 768 ? 43.829  46.455  -9.059  1.00 86.21  ? 1072 PHE   B O   1 
ATOM   8269  C  CB  . PHE   B 2 768 ? 46.018  44.856  -6.993  1.00 84.14  ? 1072 PHE   B CB  1 
ATOM   8270  C  CG  . PHE   B 2 768 ? 44.952  43.796  -7.109  1.00 86.48  ? 1072 PHE   B CG  1 
ATOM   8271  C  CD1 . PHE   B 2 768 ? 45.135  42.692  -7.918  1.00 76.74  ? 1072 PHE   B CD1 1 
ATOM   8272  C  CD2 . PHE   B 2 768 ? 43.761  43.907  -6.403  1.00 91.51  ? 1072 PHE   B CD2 1 
ATOM   8273  C  CE1 . PHE   B 2 768 ? 44.146  41.728  -8.019  1.00 81.15  ? 1072 PHE   B CE1 1 
ATOM   8274  C  CE2 . PHE   B 2 768 ? 42.767  42.924  -6.513  1.00 88.14  ? 1072 PHE   B CE2 1 
ATOM   8275  C  CZ  . PHE   B 2 768 ? 42.966  41.844  -7.315  1.00 80.23  ? 1072 PHE   B CZ  1 
ATOM   8276  N  N   . TRP   B 2 769 ? 44.394  47.426  -7.107  1.00 90.37  ? 1073 TRP   B N   1 
ATOM   8277  C  CA  . TRP   B 2 769 ? 43.085  48.033  -6.901  1.00 88.80  ? 1073 TRP   B CA  1 
ATOM   8278  C  C   . TRP   B 2 769 ? 42.691  48.936  -8.059  1.00 86.40  ? 1073 TRP   B C   1 
ATOM   8279  O  O   . TRP   B 2 769 ? 41.518  48.974  -8.447  1.00 85.41  ? 1073 TRP   B O   1 
ATOM   8280  C  CB  . TRP   B 2 769 ? 43.091  48.804  -5.580  1.00 85.78  ? 1073 TRP   B CB  1 
ATOM   8281  C  CG  . TRP   B 2 769 ? 42.088  49.913  -5.452  1.00 84.12  ? 1073 TRP   B CG  1 
ATOM   8282  C  CD1 . TRP   B 2 769 ? 42.367  51.235  -5.249  1.00 84.09  ? 1073 TRP   B CD1 1 
ATOM   8283  C  CD2 . TRP   B 2 769 ? 40.655  49.814  -5.510  1.00 82.86  ? 1073 TRP   B CD2 1 
ATOM   8284  N  NE1 . TRP   B 2 769 ? 41.206  51.964  -5.183  1.00 83.16  ? 1073 TRP   B NE1 1 
ATOM   8285  C  CE2 . TRP   B 2 769 ? 40.141  51.113  -5.334  1.00 84.46  ? 1073 TRP   B CE2 1 
ATOM   8286  C  CE3 . TRP   B 2 769 ? 39.759  48.760  -5.701  1.00 84.97  ? 1073 TRP   B CE3 1 
ATOM   8287  C  CZ2 . TRP   B 2 769 ? 38.770  51.379  -5.332  1.00 85.04  ? 1073 TRP   B CZ2 1 
ATOM   8288  C  CZ3 . TRP   B 2 769 ? 38.389  49.036  -5.698  1.00 83.32  ? 1073 TRP   B CZ3 1 
ATOM   8289  C  CH2 . TRP   B 2 769 ? 37.915  50.324  -5.516  1.00 81.59  ? 1073 TRP   B CH2 1 
ATOM   8290  N  N   . ARG   B 2 770 ? 43.648  49.686  -8.611  1.00 85.07  ? 1074 ARG   B N   1 
ATOM   8291  C  CA  . ARG   B 2 770 ? 43.334  50.629  -9.676  1.00 90.23  ? 1074 ARG   B CA  1 
ATOM   8292  C  C   . ARG   B 2 770 ? 43.328  49.976  -11.047 1.00 91.20  ? 1074 ARG   B C   1 
ATOM   8293  O  O   . ARG   B 2 770 ? 42.735  50.531  -11.986 1.00 90.24  ? 1074 ARG   B O   1 
ATOM   8294  C  CB  . ARG   B 2 770 ? 44.320  51.802  -9.665  1.00 92.79  ? 1074 ARG   B CB  1 
ATOM   8295  C  CG  . ARG   B 2 770 ? 44.056  52.813  -8.580  1.00 87.44  ? 1074 ARG   B CG  1 
ATOM   8296  C  CD  . ARG   B 2 770 ? 42.581  53.088  -8.468  1.00 81.00  ? 1074 ARG   B CD  1 
ATOM   8297  N  NE  . ARG   B 2 770 ? 42.343  54.154  -7.508  1.00 85.50  ? 1074 ARG   B NE  1 
ATOM   8298  C  CZ  . ARG   B 2 770 ? 41.145  54.582  -7.144  1.00 88.27  ? 1074 ARG   B CZ  1 
ATOM   8299  N  NH1 . ARG   B 2 770 ? 40.042  54.030  -7.619  1.00 92.07  ? 1074 ARG   B NH1 1 
ATOM   8300  N  NH2 . ARG   B 2 770 ? 41.052  55.595  -6.288  1.00 86.06  ? 1074 ARG   B NH2 1 
ATOM   8301  N  N   . SER   B 2 771 ? 43.967  48.818  -11.167 1.00 97.26  ? 1075 SER   B N   1 
ATOM   8302  C  CA  . SER   B 2 771 ? 43.984  48.058  -12.409 1.00 100.56 ? 1075 SER   B CA  1 
ATOM   8303  C  C   . SER   B 2 771 ? 42.575  47.935  -12.994 1.00 100.22 ? 1075 SER   B C   1 
ATOM   8304  O  O   . SER   B 2 771 ? 41.609  47.659  -12.277 1.00 100.80 ? 1075 SER   B O   1 
ATOM   8305  C  CB  . SER   B 2 771 ? 44.597  46.673  -12.131 1.00 102.19 ? 1075 SER   B CB  1 
ATOM   8306  O  OG  . SER   B 2 771 ? 44.863  45.927  -13.312 1.00 108.92 ? 1075 SER   B OG  1 
ATOM   8307  N  N   . PHE   B 2 772 ? 42.465  48.153  -14.301 1.00 98.39  ? 1076 PHE   B N   1 
ATOM   8308  C  CA  . PHE   B 2 772 ? 41.175  48.089  -14.973 1.00 96.56  ? 1076 PHE   B CA  1 
ATOM   8309  C  C   . PHE   B 2 772 ? 40.595  46.687  -14.851 1.00 98.24  ? 1076 PHE   B C   1 
ATOM   8310  O  O   . PHE   B 2 772 ? 41.289  45.702  -15.116 1.00 98.03  ? 1076 PHE   B O   1 
ATOM   8311  C  CB  . PHE   B 2 772 ? 41.365  48.464  -16.437 1.00 96.48  ? 1076 PHE   B CB  1 
ATOM   8312  C  CG  . PHE   B 2 772 ? 40.143  48.327  -17.270 1.00 96.05  ? 1076 PHE   B CG  1 
ATOM   8313  C  CD1 . PHE   B 2 772 ? 39.711  47.086  -17.701 1.00 96.47  ? 1076 PHE   B CD1 1 
ATOM   8314  C  CD2 . PHE   B 2 772 ? 39.442  49.456  -17.662 1.00 97.21  ? 1076 PHE   B CD2 1 
ATOM   8315  C  CE1 . PHE   B 2 772 ? 38.587  46.975  -18.492 1.00 97.48  ? 1076 PHE   B CE1 1 
ATOM   8316  C  CE2 . PHE   B 2 772 ? 38.323  49.351  -18.459 1.00 95.03  ? 1076 PHE   B CE2 1 
ATOM   8317  C  CZ  . PHE   B 2 772 ? 37.896  48.110  -18.875 1.00 95.54  ? 1076 PHE   B CZ  1 
ATOM   8318  N  N   . HIS   B 2 773 ? 39.311  46.598  -14.472 1.00 95.74  ? 1077 HIS   B N   1 
ATOM   8319  C  CA  . HIS   B 2 773 ? 38.709  45.330  -14.063 1.00 98.88  ? 1077 HIS   B CA  1 
ATOM   8320  C  C   . HIS   B 2 773 ? 37.342  45.116  -14.701 1.00 95.71  ? 1077 HIS   B C   1 
ATOM   8321  O  O   . HIS   B 2 773 ? 36.353  45.709  -14.260 1.00 89.61  ? 1077 HIS   B O   1 
ATOM   8322  C  CB  . HIS   B 2 773 ? 38.587  45.249  -12.535 1.00 99.85  ? 1077 HIS   B CB  1 
ATOM   8323  C  CG  . HIS   B 2 773 ? 38.194  43.892  -12.046 1.00 100.89 ? 1077 HIS   B CG  1 
ATOM   8324  N  ND1 . HIS   B 2 773 ? 38.895  42.753  -12.391 1.00 102.59 ? 1077 HIS   B ND1 1 
ATOM   8325  C  CD2 . HIS   B 2 773 ? 37.161  43.484  -11.270 1.00 99.65  ? 1077 HIS   B CD2 1 
ATOM   8326  C  CE1 . HIS   B 2 773 ? 38.317  41.701  -11.841 1.00 105.53 ? 1077 HIS   B CE1 1 
ATOM   8327  N  NE2 . HIS   B 2 773 ? 37.263  42.116  -11.156 1.00 105.53 ? 1077 HIS   B NE2 1 
ATOM   8328  N  N   . THR   B 2 774 ? 37.289  44.231  -15.704 1.00 103.50 ? 1078 THR   B N   1 
ATOM   8329  C  CA  . THR   B 2 774 ? 36.056  43.664  -16.240 1.00 104.07 ? 1078 THR   B CA  1 
ATOM   8330  C  C   . THR   B 2 774 ? 35.715  42.354  -15.536 1.00 112.46 ? 1078 THR   B C   1 
ATOM   8331  O  O   . THR   B 2 774 ? 36.452  41.847  -14.681 1.00 106.27 ? 1078 THR   B O   1 
ATOM   8332  C  CB  . THR   B 2 774 ? 36.142  43.383  -17.738 1.00 107.48 ? 1078 THR   B CB  1 
ATOM   8333  O  OG1 . THR   B 2 774 ? 36.652  42.052  -17.946 1.00 112.84 ? 1078 THR   B OG1 1 
ATOM   8334  C  CG2 . THR   B 2 774 ? 37.040  44.381  -18.427 1.00 106.26 ? 1078 THR   B CG2 1 
ATOM   8335  N  N   . GLU   B 2 775 ? 34.556  41.809  -15.926 1.00 124.37 ? 1079 GLU   B N   1 
ATOM   8336  C  CA  . GLU   B 2 775 ? 34.122  40.524  -15.407 1.00 124.88 ? 1079 GLU   B CA  1 
ATOM   8337  C  C   . GLU   B 2 775 ? 35.130  39.435  -15.741 1.00 124.77 ? 1079 GLU   B C   1 
ATOM   8338  O  O   . GLU   B 2 775 ? 35.339  38.519  -14.934 1.00 123.58 ? 1079 GLU   B O   1 
ATOM   8339  C  CB  . GLU   B 2 775 ? 32.735  40.177  -15.953 1.00 123.86 ? 1079 GLU   B CB  1 
ATOM   8340  N  N   . ARG   B 2 776 ? 35.793  39.529  -16.898 1.00 118.80 ? 1080 ARG   B N   1 
ATOM   8341  C  CA  . ARG   B 2 776 ? 36.687  38.469  -17.338 1.00 114.06 ? 1080 ARG   B CA  1 
ATOM   8342  C  C   . ARG   B 2 776 ? 38.074  38.970  -17.739 1.00 112.58 ? 1080 ARG   B C   1 
ATOM   8343  O  O   . ARG   B 2 776 ? 38.836  38.196  -18.332 1.00 109.49 ? 1080 ARG   B O   1 
ATOM   8344  C  CB  . ARG   B 2 776 ? 36.059  37.688  -18.494 1.00 115.02 ? 1080 ARG   B CB  1 
ATOM   8345  N  N   . LYS   B 2 777 ? 38.427  40.228  -17.439 1.00 111.80 ? 1081 LYS   B N   1 
ATOM   8346  C  CA  . LYS   B 2 777 ? 39.716  40.802  -17.821 1.00 108.67 ? 1081 LYS   B CA  1 
ATOM   8347  C  C   . LYS   B 2 777 ? 40.240  41.701  -16.707 1.00 107.76 ? 1081 LYS   B C   1 
ATOM   8348  O  O   . LYS   B 2 777 ? 39.463  42.227  -15.901 1.00 106.85 ? 1081 LYS   B O   1 
ATOM   8349  C  CB  . LYS   B 2 777 ? 39.622  41.616  -19.122 1.00 102.02 ? 1081 LYS   B CB  1 
ATOM   8350  N  N   . THR   B 2 778 ? 41.569  41.874  -16.665 1.00 102.75 ? 1082 THR   B N   1 
ATOM   8351  C  CA  . THR   B 2 778 ? 42.210  42.772  -15.697 1.00 103.79 ? 1082 THR   B CA  1 
ATOM   8352  C  C   . THR   B 2 778 ? 43.553  43.202  -16.266 1.00 108.82 ? 1082 THR   B C   1 
ATOM   8353  O  O   . THR   B 2 778 ? 44.470  42.380  -16.348 1.00 107.71 ? 1082 THR   B O   1 
ATOM   8354  C  CB  . THR   B 2 778 ? 42.395  42.114  -14.338 1.00 104.14 ? 1082 THR   B CB  1 
ATOM   8355  O  OG1 . THR   B 2 778 ? 41.149  41.545  -13.910 1.00 112.63 ? 1082 THR   B OG1 1 
ATOM   8356  C  CG2 . THR   B 2 778 ? 42.841  43.158  -13.295 1.00 104.88 ? 1082 THR   B CG2 1 
ATOM   8357  N  N   . GLU   B 2 779 ? 43.662  44.487  -16.641 1.00 112.45 ? 1083 GLU   B N   1 
ATOM   8358  C  CA  . GLU   B 2 779 ? 44.803  45.157  -17.253 1.00 113.02 ? 1083 GLU   B CA  1 
ATOM   8359  C  C   . GLU   B 2 779 ? 45.215  46.378  -16.424 1.00 112.02 ? 1083 GLU   B C   1 
ATOM   8360  O  O   . GLU   B 2 779 ? 44.368  47.014  -15.787 1.00 111.20 ? 1083 GLU   B O   1 
ATOM   8361  C  CB  . GLU   B 2 779 ? 44.485  45.606  -18.689 1.00 113.16 ? 1083 GLU   B CB  1 
ATOM   8362  N  N   . PRO   B 2 780 ? 46.503  46.730  -16.407 1.00 108.65 ? 1084 PRO   B N   1 
ATOM   8363  C  CA  . PRO   B 2 780 ? 46.967  47.760  -15.468 1.00 106.76 ? 1084 PRO   B CA  1 
ATOM   8364  C  C   . PRO   B 2 780 ? 46.608  49.159  -15.942 1.00 105.19 ? 1084 PRO   B C   1 
ATOM   8365  O  O   . PRO   B 2 780 ? 46.675  49.478  -17.131 1.00 99.56  ? 1084 PRO   B O   1 
ATOM   8366  C  CB  . PRO   B 2 780 ? 48.494  47.558  -15.429 1.00 104.44 ? 1084 PRO   B CB  1 
ATOM   8367  C  CG  . PRO   B 2 780 ? 48.745  46.245  -16.104 1.00 106.17 ? 1084 PRO   B CG  1 
ATOM   8368  C  CD  . PRO   B 2 780 ? 47.629  46.088  -17.102 1.00 110.83 ? 1084 PRO   B CD  1 
ATOM   8369  N  N   . ALA   B 2 781 ? 46.225  49.994  -14.981 1.00 105.36 ? 1085 ALA   B N   1 
ATOM   8370  C  CA  . ALA   B 2 781 ? 45.804  51.348  -15.274 1.00 96.44  ? 1085 ALA   B CA  1 
ATOM   8371  C  C   . ALA   B 2 781 ? 46.867  52.143  -16.019 1.00 99.24  ? 1085 ALA   B C   1 
ATOM   8372  O  O   . ALA   B 2 781 ? 48.067  51.890  -15.889 1.00 100.02 ? 1085 ALA   B O   1 
ATOM   8373  C  CB  . ALA   B 2 781 ? 45.556  52.117  -13.978 1.00 92.72  ? 1085 ALA   B CB  1 
ATOM   8374  N  N   . THR   B 2 782 ? 46.409  53.122  -16.809 1.00 99.35  ? 1086 THR   B N   1 
ATOM   8375  C  CA  . THR   B 2 782 ? 47.310  53.910  -17.638 1.00 99.05  ? 1086 THR   B CA  1 
ATOM   8376  C  C   . THR   B 2 782 ? 46.767  55.318  -17.850 1.00 102.41 ? 1086 THR   B C   1 
ATOM   8377  O  O   . THR   B 2 782 ? 45.550  55.511  -17.960 1.00 99.93  ? 1086 THR   B O   1 
ATOM   8378  C  CB  . THR   B 2 782 ? 47.431  53.203  -18.986 1.00 96.17  ? 1086 THR   B CB  1 
ATOM   8379  O  OG1 . THR   B 2 782 ? 48.553  53.734  -19.694 1.00 109.95 ? 1086 THR   B OG1 1 
ATOM   8380  C  CG2 . THR   B 2 782 ? 46.177  53.416  -19.816 1.00 89.10  ? 1086 THR   B CG2 1 
ATOM   8381  N  N   . GLY   B 2 783 ? 47.680  56.294  -17.929 1.00 101.46 ? 1087 GLY   B N   1 
ATOM   8382  C  CA  . GLY   B 2 783 ? 47.294  57.664  -18.245 1.00 103.77 ? 1087 GLY   B CA  1 
ATOM   8383  C  C   . GLY   B 2 783 ? 46.379  58.321  -17.236 1.00 100.33 ? 1087 GLY   B C   1 
ATOM   8384  O  O   . GLY   B 2 783 ? 45.699  59.293  -17.571 1.00 104.44 ? 1087 GLY   B O   1 
ATOM   8385  N  N   . PHE   B 2 784 ? 46.341  57.809  -16.006 1.00 98.29  ? 1088 PHE   B N   1 
ATOM   8386  C  CA  . PHE   B 2 784 ? 45.576  58.380  -14.912 1.00 95.21  ? 1088 PHE   B CA  1 
ATOM   8387  C  C   . PHE   B 2 784 ? 46.466  58.473  -13.680 1.00 99.23  ? 1088 PHE   B C   1 
ATOM   8388  O  O   . PHE   B 2 784 ? 47.269  57.572  -13.406 1.00 105.42 ? 1088 PHE   B O   1 
ATOM   8389  C  CB  . PHE   B 2 784 ? 44.335  57.532  -14.577 1.00 95.59  ? 1088 PHE   B CB  1 
ATOM   8390  C  CG  . PHE   B 2 784 ? 43.127  57.812  -15.442 1.00 96.36  ? 1088 PHE   B CG  1 
ATOM   8391  C  CD1 . PHE   B 2 784 ? 42.215  58.798  -15.099 1.00 95.74  ? 1088 PHE   B CD1 1 
ATOM   8392  C  CD2 . PHE   B 2 784 ? 42.876  57.053  -16.579 1.00 98.59  ? 1088 PHE   B CD2 1 
ATOM   8393  C  CE1 . PHE   B 2 784 ? 41.087  59.041  -15.890 1.00 96.56  ? 1088 PHE   B CE1 1 
ATOM   8394  C  CE2 . PHE   B 2 784 ? 41.746  57.293  -17.373 1.00 95.63  ? 1088 PHE   B CE2 1 
ATOM   8395  C  CZ  . PHE   B 2 784 ? 40.854  58.288  -17.026 1.00 91.61  ? 1088 PHE   B CZ  1 
ATOM   8396  N  N   . ILE   B 2 785 ? 46.317  59.559  -12.934 1.00 96.79  ? 1089 ILE   B N   1 
ATOM   8397  C  CA  . ILE   B 2 785 ? 46.995  59.737  -11.658 1.00 99.40  ? 1089 ILE   B CA  1 
ATOM   8398  C  C   . ILE   B 2 785 ? 45.940  59.666  -10.570 1.00 97.58  ? 1089 ILE   B C   1 
ATOM   8399  O  O   . ILE   B 2 785 ? 44.898  60.326  -10.674 1.00 94.01  ? 1089 ILE   B O   1 
ATOM   8400  C  CB  . ILE   B 2 785 ? 47.737  61.083  -11.582 1.00 100.60 ? 1089 ILE   B CB  1 
ATOM   8401  C  CG1 . ILE   B 2 785 ? 48.582  61.324  -12.838 1.00 107.20 ? 1089 ILE   B CG1 1 
ATOM   8402  C  CG2 . ILE   B 2 785 ? 48.595  61.124  -10.337 1.00 97.12  ? 1089 ILE   B CG2 1 
ATOM   8403  C  CD1 . ILE   B 2 785 ? 49.736  60.369  -12.982 1.00 110.44 ? 1089 ILE   B CD1 1 
ATOM   8404  N  N   . ASP   B 2 786 ? 46.204  58.881  -9.526  1.00 96.08  ? 1090 ASP   B N   1 
ATOM   8405  C  CA  . ASP   B 2 786 ? 45.252  58.790  -8.422  1.00 95.72  ? 1090 ASP   B CA  1 
ATOM   8406  C  C   . ASP   B 2 786 ? 45.521  59.942  -7.461  1.00 97.42  ? 1090 ASP   B C   1 
ATOM   8407  O  O   . ASP   B 2 786 ? 46.299  59.834  -6.509  1.00 97.03  ? 1090 ASP   B O   1 
ATOM   8408  C  CB  . ASP   B 2 786 ? 45.332  57.439  -7.729  1.00 96.13  ? 1090 ASP   B CB  1 
ATOM   8409  C  CG  . ASP   B 2 786 ? 44.153  57.202  -6.784  1.00 97.28  ? 1090 ASP   B CG  1 
ATOM   8410  O  OD1 . ASP   B 2 786 ? 43.566  58.193  -6.273  1.00 100.14 ? 1090 ASP   B OD1 1 
ATOM   8411  O  OD2 . ASP   B 2 786 ? 43.809  56.024  -6.556  1.00 93.09  ? 1090 ASP   B OD2 1 
ATOM   8412  N  N   . GLY   B 2 787 ? 44.853  61.068  -7.726  1.00 97.23  ? 1091 GLY   B N   1 
ATOM   8413  C  CA  . GLY   B 2 787 ? 45.021  62.240  -6.889  1.00 97.06  ? 1091 GLY   B CA  1 
ATOM   8414  C  C   . GLY   B 2 787 ? 44.704  61.980  -5.432  1.00 99.48  ? 1091 GLY   B C   1 
ATOM   8415  O  O   . GLY   B 2 787 ? 45.281  62.617  -4.548  1.00 98.50  ? 1091 GLY   B O   1 
ATOM   8416  N  N   . ASP   B 2 788 ? 43.782  61.052  -5.158  1.00 98.14  ? 1092 ASP   B N   1 
ATOM   8417  C  CA  . ASP   B 2 788 ? 43.494  60.701  -3.775  1.00 94.16  ? 1092 ASP   B CA  1 
ATOM   8418  C  C   . ASP   B 2 788 ? 44.761  60.242  -3.064  1.00 101.80 ? 1092 ASP   B C   1 
ATOM   8419  O  O   . ASP   B 2 788 ? 45.029  60.654  -1.929  1.00 106.09 ? 1092 ASP   B O   1 
ATOM   8420  C  CB  . ASP   B 2 788 ? 42.416  59.616  -3.714  1.00 97.61  ? 1092 ASP   B CB  1 
ATOM   8421  C  CG  . ASP   B 2 788 ? 40.989  60.169  -3.825  1.00 97.52  ? 1092 ASP   B CG  1 
ATOM   8422  O  OD1 . ASP   B 2 788 ? 40.815  61.389  -4.065  1.00 96.97  ? 1092 ASP   B OD1 1 
ATOM   8423  O  OD2 . ASP   B 2 788 ? 40.029  59.370  -3.661  1.00 95.71  ? 1092 ASP   B OD2 1 
ATOM   8424  N  N   . LEU   B 2 789 ? 45.573  59.407  -3.723  1.00 101.48 ? 1093 LEU   B N   1 
ATOM   8425  C  CA  . LEU   B 2 789 ? 46.831  58.993  -3.108  1.00 104.72 ? 1093 LEU   B CA  1 
ATOM   8426  C  C   . LEU   B 2 789 ? 47.838  60.127  -3.114  1.00 102.54 ? 1093 LEU   B C   1 
ATOM   8427  O  O   . LEU   B 2 789 ? 48.478  60.405  -2.097  1.00 105.50 ? 1093 LEU   B O   1 
ATOM   8428  C  CB  . LEU   B 2 789 ? 47.428  57.784  -3.815  1.00 103.78 ? 1093 LEU   B CB  1 
ATOM   8429  C  CG  . LEU   B 2 789 ? 48.373  57.115  -2.813  1.00 104.65 ? 1093 LEU   B CG  1 
ATOM   8430  C  CD1 . LEU   B 2 789 ? 47.551  56.584  -1.613  1.00 105.79 ? 1093 LEU   B CD1 1 
ATOM   8431  C  CD2 . LEU   B 2 789 ? 49.198  56.022  -3.475  1.00 103.80 ? 1093 LEU   B CD2 1 
ATOM   8432  N  N   . ILE   B 2 790 ? 48.007  60.772  -4.266  1.00 101.73 ? 1094 ILE   B N   1 
ATOM   8433  C  CA  . ILE   B 2 790 ? 48.894  61.926  -4.358  1.00 104.70 ? 1094 ILE   B CA  1 
ATOM   8434  C  C   . ILE   B 2 790 ? 48.660  62.880  -3.186  1.00 109.87 ? 1094 ILE   B C   1 
ATOM   8435  O  O   . ILE   B 2 790 ? 49.600  63.268  -2.479  1.00 111.34 ? 1094 ILE   B O   1 
ATOM   8436  C  CB  . ILE   B 2 790 ? 48.703  62.632  -5.711  1.00 103.06 ? 1094 ILE   B CB  1 
ATOM   8437  C  CG1 . ILE   B 2 790 ? 49.170  61.736  -6.860  1.00 101.94 ? 1094 ILE   B CG1 1 
ATOM   8438  C  CG2 . ILE   B 2 790 ? 49.462  63.938  -5.728  1.00 104.34 ? 1094 ILE   B CG2 1 
ATOM   8439  C  CD1 . ILE   B 2 790 ? 50.678  61.544  -6.905  1.00 104.82 ? 1094 ILE   B CD1 1 
ATOM   8440  N  N   . GLU   B 2 791 ? 47.398  63.275  -2.959  1.00 109.71 ? 1095 GLU   B N   1 
ATOM   8441  C  CA  . GLU   B 2 791 ? 47.122  64.253  -1.904  1.00 107.24 ? 1095 GLU   B CA  1 
ATOM   8442  C  C   . GLU   B 2 791 ? 47.415  63.690  -0.522  1.00 108.47 ? 1095 GLU   B C   1 
ATOM   8443  O  O   . GLU   B 2 791 ? 47.520  64.458  0.436   1.00 108.82 ? 1095 GLU   B O   1 
ATOM   8444  C  CB  . GLU   B 2 791 ? 45.660  64.760  -1.968  1.00 107.36 ? 1095 GLU   B CB  1 
ATOM   8445  C  CG  . GLU   B 2 791 ? 45.335  65.621  -3.225  1.00 111.77 ? 1095 GLU   B CG  1 
ATOM   8446  C  CD  . GLU   B 2 791 ? 43.951  66.333  -3.243  1.00 109.55 ? 1095 GLU   B CD  1 
ATOM   8447  O  OE1 . GLU   B 2 791 ? 43.251  66.396  -2.193  1.00 105.85 ? 1095 GLU   B OE1 1 
ATOM   8448  O  OE2 . GLU   B 2 791 ? 43.590  66.852  -4.340  1.00 101.89 ? 1095 GLU   B OE2 1 
ATOM   8449  N  N   . SER   B 2 792 ? 47.545  62.371  -0.389  1.00 108.98 ? 1096 SER   B N   1 
ATOM   8450  C  CA  . SER   B 2 792 ? 47.857  61.834  0.927   1.00 110.46 ? 1096 SER   B CA  1 
ATOM   8451  C  C   . SER   B 2 792 ? 49.265  62.189  1.364   1.00 112.34 ? 1096 SER   B C   1 
ATOM   8452  O  O   . SER   B 2 792 ? 49.596  62.006  2.539   1.00 114.08 ? 1096 SER   B O   1 
ATOM   8453  C  CB  . SER   B 2 792 ? 47.660  60.309  0.952   1.00 112.14 ? 1096 SER   B CB  1 
ATOM   8454  O  OG  . SER   B 2 792 ? 48.664  59.616  0.228   1.00 110.05 ? 1096 SER   B OG  1 
ATOM   8455  N  N   . PHE   B 2 793 ? 50.092  62.703  0.453   1.00 115.56 ? 1097 PHE   B N   1 
ATOM   8456  C  CA  . PHE   B 2 793 ? 51.445  63.093  0.821   1.00 116.34 ? 1097 PHE   B CA  1 
ATOM   8457  C  C   . PHE   B 2 793 ? 51.440  64.169  1.903   1.00 119.96 ? 1097 PHE   B C   1 
ATOM   8458  O  O   . PHE   B 2 793 ? 52.280  64.144  2.807   1.00 125.13 ? 1097 PHE   B O   1 
ATOM   8459  C  CB  . PHE   B 2 793 ? 52.195  63.551  -0.428  1.00 116.80 ? 1097 PHE   B CB  1 
ATOM   8460  C  CG  . PHE   B 2 793 ? 53.527  64.187  -0.147  1.00 126.33 ? 1097 PHE   B CG  1 
ATOM   8461  C  CD1 . PHE   B 2 793 ? 54.460  63.571  0.699   1.00 130.76 ? 1097 PHE   B CD1 1 
ATOM   8462  C  CD2 . PHE   B 2 793 ? 53.854  65.408  -0.725  1.00 130.91 ? 1097 PHE   B CD2 1 
ATOM   8463  C  CE1 . PHE   B 2 793 ? 55.696  64.172  0.979   1.00 133.25 ? 1097 PHE   B CE1 1 
ATOM   8464  C  CE2 . PHE   B 2 793 ? 55.095  66.014  -0.472  1.00 131.34 ? 1097 PHE   B CE2 1 
ATOM   8465  C  CZ  . PHE   B 2 793 ? 56.018  65.394  0.380   1.00 132.49 ? 1097 PHE   B CZ  1 
ATOM   8466  N  N   . LEU   B 2 794 ? 50.501  65.118  1.846   1.00 116.06 ? 1098 LEU   B N   1 
ATOM   8467  C  CA  . LEU   B 2 794 ? 50.508  66.166  2.858   1.00 113.13 ? 1098 LEU   B CA  1 
ATOM   8468  C  C   . LEU   B 2 794 ? 50.098  65.652  4.227   1.00 118.11 ? 1098 LEU   B C   1 
ATOM   8469  O  O   . LEU   B 2 794 ? 50.335  66.343  5.219   1.00 122.82 ? 1098 LEU   B O   1 
ATOM   8470  C  CB  . LEU   B 2 794 ? 49.589  67.326  2.481   1.00 108.45 ? 1098 LEU   B CB  1 
ATOM   8471  C  CG  . LEU   B 2 794 ? 49.568  67.818  1.041   1.00 110.09 ? 1098 LEU   B CG  1 
ATOM   8472  C  CD1 . LEU   B 2 794 ? 48.581  66.968  0.291   1.00 118.46 ? 1098 LEU   B CD1 1 
ATOM   8473  C  CD2 . LEU   B 2 794 ? 49.191  69.292  0.920   1.00 114.21 ? 1098 LEU   B CD2 1 
ATOM   8474  N  N   . ASP   B 2 795 ? 49.511  64.460  4.322   1.00 120.41 ? 1099 ASP   B N   1 
ATOM   8475  C  CA  . ASP   B 2 795 ? 49.072  63.933  5.608   1.00 122.41 ? 1099 ASP   B CA  1 
ATOM   8476  C  C   . ASP   B 2 795 ? 50.047  62.924  6.217   1.00 125.34 ? 1099 ASP   B C   1 
ATOM   8477  O  O   . ASP   B 2 795 ? 49.739  62.351  7.264   1.00 129.36 ? 1099 ASP   B O   1 
ATOM   8478  C  CB  . ASP   B 2 795 ? 47.681  63.301  5.482   1.00 125.35 ? 1099 ASP   B CB  1 
ATOM   8479  C  CG  . ASP   B 2 795 ? 46.584  64.325  5.184   1.00 133.01 ? 1099 ASP   B CG  1 
ATOM   8480  O  OD1 . ASP   B 2 795 ? 46.401  64.704  3.998   1.00 129.60 ? 1099 ASP   B OD1 1 
ATOM   8481  O  OD2 . ASP   B 2 795 ? 45.899  64.746  6.146   1.00 141.42 ? 1099 ASP   B OD2 1 
ATOM   8482  N  N   . ILE   B 2 796 ? 51.209  62.699  5.611   1.00 125.75 ? 1100 ILE   B N   1 
ATOM   8483  C  CA  . ILE   B 2 796 ? 52.184  61.766  6.153   1.00 125.38 ? 1100 ILE   B CA  1 
ATOM   8484  C  C   . ILE   B 2 796 ? 53.250  62.518  6.937   1.00 130.62 ? 1100 ILE   B C   1 
ATOM   8485  O  O   . ILE   B 2 796 ? 53.296  63.746  6.958   1.00 123.17 ? 1100 ILE   B O   1 
ATOM   8486  C  CB  . ILE   B 2 796 ? 52.842  60.893  5.063   1.00 117.63 ? 1100 ILE   B CB  1 
ATOM   8487  C  CG1 . ILE   B 2 796 ? 53.462  61.762  3.978   1.00 126.36 ? 1100 ILE   B CG1 1 
ATOM   8488  C  CG2 . ILE   B 2 796 ? 51.856  59.921  4.495   1.00 119.69 ? 1100 ILE   B CG2 1 
ATOM   8489  C  CD1 . ILE   B 2 796 ? 54.583  61.082  3.251   1.00 128.70 ? 1100 ILE   B CD1 1 
ATOM   8490  N  N   . SER   B 2 797 ? 54.147  61.758  7.563   1.00 141.20 ? 1101 SER   B N   1 
ATOM   8491  C  CA  . SER   B 2 797 ? 55.128  62.322  8.481   1.00 145.05 ? 1101 SER   B CA  1 
ATOM   8492  C  C   . SER   B 2 797 ? 56.273  62.988  7.715   1.00 144.24 ? 1101 SER   B C   1 
ATOM   8493  O  O   . SER   B 2 797 ? 56.708  62.503  6.664   1.00 143.88 ? 1101 SER   B O   1 
ATOM   8494  C  CB  . SER   B 2 797 ? 55.664  61.222  9.411   1.00 145.46 ? 1101 SER   B CB  1 
ATOM   8495  O  OG  . SER   B 2 797 ? 54.648  60.702  10.271  1.00 142.33 ? 1101 SER   B OG  1 
ATOM   8496  N  N   . ARG   B 2 798 ? 56.745  64.124  8.234   1.00 140.89 ? 1102 ARG   B N   1 
ATOM   8497  C  CA  . ARG   B 2 798 ? 57.858  64.807  7.583   1.00 140.94 ? 1102 ARG   B CA  1 
ATOM   8498  C  C   . ARG   B 2 798 ? 59.114  63.938  7.498   1.00 145.78 ? 1102 ARG   B C   1 
ATOM   8499  O  O   . ARG   B 2 798 ? 59.884  64.129  6.543   1.00 147.61 ? 1102 ARG   B O   1 
ATOM   8500  C  CB  . ARG   B 2 798 ? 58.156  66.137  8.287   1.00 137.85 ? 1102 ARG   B CB  1 
ATOM   8501  C  CG  . ARG   B 2 798 ? 59.334  66.932  7.697   1.00 139.58 ? 1102 ARG   B CG  1 
ATOM   8502  C  CD  . ARG   B 2 798 ? 59.079  67.403  6.271   1.00 140.65 ? 1102 ARG   B CD  1 
ATOM   8503  N  NE  . ARG   B 2 798 ? 60.303  67.852  5.613   1.00 146.44 ? 1102 ARG   B NE  1 
ATOM   8504  C  CZ  . ARG   B 2 798 ? 60.596  69.119  5.347   1.00 148.64 ? 1102 ARG   B CZ  1 
ATOM   8505  N  NH1 . ARG   B 2 798 ? 59.765  70.101  5.663   1.00 145.45 ? 1102 ARG   B NH1 1 
ATOM   8506  N  NH2 . ARG   B 2 798 ? 61.747  69.405  4.739   1.00 147.19 ? 1102 ARG   B NH2 1 
ATOM   8507  N  N   . PRO   B 2 799 ? 59.385  63.002  8.421   1.00 145.91 ? 1103 PRO   B N   1 
ATOM   8508  C  CA  . PRO   B 2 799 ? 60.396  61.963  8.122   1.00 147.91 ? 1103 PRO   B CA  1 
ATOM   8509  C  C   . PRO   B 2 799 ? 60.047  61.146  6.882   1.00 148.31 ? 1103 PRO   B C   1 
ATOM   8510  O  O   . PRO   B 2 799 ? 60.876  61.024  5.974   1.00 150.35 ? 1103 PRO   B O   1 
ATOM   8511  C  CB  . PRO   B 2 799 ? 60.404  61.106  9.390   1.00 144.94 ? 1103 PRO   B CB  1 
ATOM   8512  C  CG  . PRO   B 2 799 ? 59.054  61.342  10.015  1.00 147.46 ? 1103 PRO   B CG  1 
ATOM   8513  C  CD  . PRO   B 2 799 ? 58.763  62.796  9.739   1.00 144.83 ? 1103 PRO   B CD  1 
ATOM   8514  N  N   . LYS   B 2 800 ? 58.826  60.595  6.828   1.00 148.22 ? 1104 LYS   B N   1 
ATOM   8515  C  CA  . LYS   B 2 800 ? 58.421  59.785  5.681   1.00 146.04 ? 1104 LYS   B CA  1 
ATOM   8516  C  C   . LYS   B 2 800 ? 58.341  60.616  4.404   1.00 148.26 ? 1104 LYS   B C   1 
ATOM   8517  O  O   . LYS   B 2 800 ? 58.696  60.132  3.327   1.00 151.54 ? 1104 LYS   B O   1 
ATOM   8518  C  CB  . LYS   B 2 800 ? 57.084  59.103  5.974   1.00 134.54 ? 1104 LYS   B CB  1 
ATOM   8519  N  N   . MET   B 2 801 ? 57.864  61.862  4.503   1.00 141.55 ? 1105 MET   B N   1 
ATOM   8520  C  CA  . MET   B 2 801 ? 57.836  62.747  3.341   1.00 142.79 ? 1105 MET   B CA  1 
ATOM   8521  C  C   . MET   B 2 801 ? 59.180  62.754  2.627   1.00 146.58 ? 1105 MET   B C   1 
ATOM   8522  O  O   . MET   B 2 801 ? 59.255  62.579  1.405   1.00 145.34 ? 1105 MET   B O   1 
ATOM   8523  C  CB  . MET   B 2 801 ? 57.454  64.166  3.773   1.00 140.58 ? 1105 MET   B CB  1 
ATOM   8524  C  CG  . MET   B 2 801 ? 56.101  64.272  4.495   1.00 134.96 ? 1105 MET   B CG  1 
ATOM   8525  S  SD  . MET   B 2 801 ? 55.628  65.985  4.843   1.00 139.62 ? 1105 MET   B SD  1 
ATOM   8526  C  CE  . MET   B 2 801 ? 55.528  66.727  3.238   1.00 128.62 ? 1105 MET   B CE  1 
ATOM   8527  N  N   . GLN   B 2 802 ? 60.258  62.961  3.383   1.00 152.80 ? 1106 GLN   B N   1 
ATOM   8528  C  CA  . GLN   B 2 802 ? 61.581  63.009  2.773   1.00 155.62 ? 1106 GLN   B CA  1 
ATOM   8529  C  C   . GLN   B 2 802 ? 61.929  61.682  2.104   1.00 157.14 ? 1106 GLN   B C   1 
ATOM   8530  O  O   . GLN   B 2 802 ? 62.595  61.664  1.062   1.00 158.61 ? 1106 GLN   B O   1 
ATOM   8531  C  CB  . GLN   B 2 802 ? 62.629  63.388  3.821   1.00 157.30 ? 1106 GLN   B CB  1 
ATOM   8532  C  CG  . GLN   B 2 802 ? 62.592  64.855  4.248   1.00 158.87 ? 1106 GLN   B CG  1 
ATOM   8533  C  CD  . GLN   B 2 802 ? 62.995  65.051  5.701   1.00 159.92 ? 1106 GLN   B CD  1 
ATOM   8534  O  OE1 . GLN   B 2 802 ? 63.146  64.075  6.447   1.00 160.53 ? 1106 GLN   B OE1 1 
ATOM   8535  N  NE2 . GLN   B 2 802 ? 63.166  66.312  6.113   1.00 154.84 ? 1106 GLN   B NE2 1 
ATOM   8536  N  N   . GLU   B 2 803 ? 61.483  60.561  2.679   1.00 165.62 ? 1107 GLU   B N   1 
ATOM   8537  C  CA  . GLU   B 2 803 ? 61.832  59.260  2.107   1.00 165.45 ? 1107 GLU   B CA  1 
ATOM   8538  C  C   . GLU   B 2 803 ? 61.227  59.083  0.721   1.00 162.21 ? 1107 GLU   B C   1 
ATOM   8539  O  O   . GLU   B 2 803 ? 61.861  58.506  -0.170  1.00 162.49 ? 1107 GLU   B O   1 
ATOM   8540  C  CB  . GLU   B 2 803 ? 61.390  58.110  3.019   1.00 163.98 ? 1107 GLU   B CB  1 
ATOM   8541  C  CG  . GLU   B 2 803 ? 61.547  58.348  4.523   1.00 168.42 ? 1107 GLU   B CG  1 
ATOM   8542  C  CD  . GLU   B 2 803 ? 62.915  58.885  4.976   1.00 173.38 ? 1107 GLU   B CD  1 
ATOM   8543  O  OE1 . GLU   B 2 803 ? 63.202  58.820  6.184   1.00 173.93 ? 1107 GLU   B OE1 1 
ATOM   8544  O  OE2 . GLU   B 2 803 ? 63.702  59.382  4.115   1.00 174.27 ? 1107 GLU   B OE2 1 
ATOM   8545  N  N   . VAL   B 2 804 ? 60.006  59.580  0.515   1.00 149.45 ? 1108 VAL   B N   1 
ATOM   8546  C  CA  . VAL   B 2 804 ? 59.372  59.455  -0.794  1.00 142.86 ? 1108 VAL   B CA  1 
ATOM   8547  C  C   . VAL   B 2 804 ? 59.914  60.460  -1.801  1.00 141.29 ? 1108 VAL   B C   1 
ATOM   8548  O  O   . VAL   B 2 804 ? 59.689  60.296  -3.005  1.00 139.16 ? 1108 VAL   B O   1 
ATOM   8549  C  CB  . VAL   B 2 804 ? 57.849  59.611  -0.670  1.00 135.72 ? 1108 VAL   B CB  1 
ATOM   8550  C  CG1 . VAL   B 2 804 ? 57.374  59.035  0.642   1.00 135.33 ? 1108 VAL   B CG1 1 
ATOM   8551  C  CG2 . VAL   B 2 804 ? 57.454  61.077  -0.779  1.00 140.83 ? 1108 VAL   B CG2 1 
ATOM   8552  N  N   . VAL   B 2 805 ? 60.606  61.505  -1.349  1.00 143.35 ? 1109 VAL   B N   1 
ATOM   8553  C  CA  . VAL   B 2 805 ? 61.196  62.470  -2.269  1.00 145.63 ? 1109 VAL   B CA  1 
ATOM   8554  C  C   . VAL   B 2 805 ? 62.658  62.168  -2.535  1.00 150.68 ? 1109 VAL   B C   1 
ATOM   8555  O  O   . VAL   B 2 805 ? 63.268  62.815  -3.404  1.00 153.99 ? 1109 VAL   B O   1 
ATOM   8556  C  CB  . VAL   B 2 805 ? 61.028  63.907  -1.733  1.00 145.76 ? 1109 VAL   B CB  1 
ATOM   8557  C  CG1 . VAL   B 2 805 ? 59.570  64.292  -1.728  1.00 139.84 ? 1109 VAL   B CG1 1 
ATOM   8558  C  CG2 . VAL   B 2 805 ? 61.575  64.003  -0.333  1.00 150.91 ? 1109 VAL   B CG2 1 
ATOM   8559  N  N   . ALA   B 2 806 ? 63.219  61.170  -1.854  1.00 148.12 ? 1110 ALA   B N   1 
ATOM   8560  C  CA  . ALA   B 2 806 ? 64.648  60.873  -1.894  1.00 153.38 ? 1110 ALA   B CA  1 
ATOM   8561  C  C   . ALA   B 2 806 ? 65.127  60.597  -3.319  1.00 158.28 ? 1110 ALA   B C   1 
ATOM   8562  O  O   . ALA   B 2 806 ? 64.620  59.696  -3.993  1.00 155.74 ? 1110 ALA   B O   1 
ATOM   8563  C  CB  . ALA   B 2 806 ? 64.935  59.668  -0.998  1.00 151.17 ? 1110 ALA   B CB  1 
ATOM   8564  N  N   . ASN   B 2 807 ? 66.129  61.362  -3.763  1.00 162.74 ? 1111 ASN   B N   1 
ATOM   8565  C  CA  . ASN   B 2 807 ? 66.770  61.133  -5.054  1.00 163.70 ? 1111 ASN   B CA  1 
ATOM   8566  C  C   . ASN   B 2 807 ? 66.068  61.347  -6.391  1.00 162.82 ? 1111 ASN   B C   1 
ATOM   8567  O  O   . ASN   B 2 807 ? 66.059  60.456  -7.249  1.00 161.46 ? 1111 ASN   B O   1 
ATOM   8568  C  CB  . ASN   B 2 807 ? 67.379  59.726  -5.118  1.00 162.36 ? 1111 ASN   B CB  1 
ATOM   8569  C  CG  . ASN   B 2 807 ? 68.732  59.641  -4.420  1.00 162.17 ? 1111 ASN   B CG  1 
ATOM   8570  O  OD1 . ASN   B 2 807 ? 69.781  59.729  -5.057  1.00 166.38 ? 1111 ASN   B OD1 1 
ATOM   8571  N  ND2 . ASN   B 2 807 ? 68.711  59.468  -3.105  1.00 158.89 ? 1111 ASN   B ND2 1 
ATOM   8572  N  N   . LEU   B 2 808 ? 65.492  62.534  -6.579  1.00 163.76 ? 1112 LEU   B N   1 
ATOM   8573  C  CA  . LEU   B 2 808 ? 64.896  62.929  -7.847  1.00 163.66 ? 1112 LEU   B CA  1 
ATOM   8574  C  C   . LEU   B 2 808 ? 64.863  64.442  -8.007  1.00 170.09 ? 1112 LEU   B C   1 
ATOM   8575  O  O   . LEU   B 2 808 ? 64.529  65.154  -7.052  1.00 171.74 ? 1112 LEU   B O   1 
ATOM   8576  C  CB  . LEU   B 2 808 ? 63.479  62.367  -7.734  1.00 160.85 ? 1112 LEU   B CB  1 
ATOM   8577  C  CG  . LEU   B 2 808 ? 62.737  62.171  -9.055  1.00 166.26 ? 1112 LEU   B CG  1 
ATOM   8578  C  CD1 . LEU   B 2 808 ? 62.426  63.501  -9.744  1.00 166.28 ? 1112 LEU   B CD1 1 
ATOM   8579  C  CD2 . LEU   B 2 808 ? 63.573  61.293  -9.956  1.00 162.86 ? 1112 LEU   B CD2 1 
ATOM   8580  N  N   . GLN   B 2 809 ? 65.202  64.946  -9.197  1.00 172.93 ? 1113 GLN   B N   1 
ATOM   8581  C  CA  . GLN   B 2 809 ? 65.244  66.396  -9.447  1.00 173.56 ? 1113 GLN   B CA  1 
ATOM   8582  C  C   . GLN   B 2 809 ? 64.144  66.890  -10.384 1.00 170.41 ? 1113 GLN   B C   1 
ATOM   8583  O  O   . GLN   B 2 809 ? 63.032  66.369  -10.393 1.00 168.21 ? 1113 GLN   B O   1 
ATOM   8584  C  CB  . GLN   B 2 809 ? 66.594  66.809  -10.028 1.00 170.38 ? 1113 GLN   B CB  1 
ATOM   8585  C  CG  . GLN   B 2 809 ? 66.994  68.202  -9.577  1.00 167.17 ? 1113 GLN   B CG  1 
ATOM   8586  C  CD  . GLN   B 2 809 ? 67.412  68.213  -8.088  1.00 167.50 ? 1113 GLN   B CD  1 
ATOM   8587  O  OE1 . GLN   B 2 809 ? 68.298  67.442  -7.667  1.00 166.20 ? 1113 GLN   B OE1 1 
ATOM   8588  N  NE2 . GLN   B 2 809 ? 66.693  68.978  -7.282  1.00 166.53 ? 1113 GLN   B NE2 1 
ATOM   8589  N  N   . GLU   B 2 819 ? 68.719  65.532  -5.503  1.00 167.82 ? 1123 GLU   B N   1 
ATOM   8590  C  CA  . GLU   B 2 819 ? 67.319  65.210  -5.375  1.00 168.14 ? 1123 GLU   B CA  1 
ATOM   8591  C  C   . GLU   B 2 819 ? 66.526  66.503  -4.956  1.00 170.13 ? 1123 GLU   B C   1 
ATOM   8592  O  O   . GLU   B 2 819 ? 67.147  67.540  -4.597  1.00 166.28 ? 1123 GLU   B O   1 
ATOM   8593  C  CB  . GLU   B 2 819 ? 67.129  64.135  -4.317  1.00 161.92 ? 1123 GLU   B CB  1 
ATOM   8594  N  N   . ALA   B 2 820 ? 65.183  66.452  -4.997  1.00 168.20 ? 1124 ALA   B N   1 
ATOM   8595  C  CA  . ALA   B 2 820 ? 64.355  67.583  -4.614  1.00 165.99 ? 1124 ALA   B CA  1 
ATOM   8596  C  C   . ALA   B 2 820 ? 63.827  67.359  -3.203  1.00 162.52 ? 1124 ALA   B C   1 
ATOM   8597  O  O   . ALA   B 2 820 ? 63.560  66.219  -2.807  1.00 157.56 ? 1124 ALA   B O   1 
ATOM   8598  C  CB  . ALA   B 2 820 ? 63.232  67.789  -5.617  1.00 163.80 ? 1124 ALA   B CB  1 
ATOM   8599  N  N   . THR   B 2 821 ? 63.740  68.442  -2.427  1.00 163.01 ? 1125 THR   B N   1 
ATOM   8600  C  CA  . THR   B 2 821 ? 63.377  68.323  -1.028  1.00 159.24 ? 1125 THR   B CA  1 
ATOM   8601  C  C   . THR   B 2 821 ? 61.888  68.045  -0.903  1.00 154.92 ? 1125 THR   B C   1 
ATOM   8602  O  O   . THR   B 2 821 ? 61.150  67.989  -1.890  1.00 153.33 ? 1125 THR   B O   1 
ATOM   8603  C  CB  . THR   B 2 821 ? 63.721  69.601  -0.270  1.00 156.09 ? 1125 THR   B CB  1 
ATOM   8604  O  OG1 . THR   B 2 821 ? 65.018  70.065  -0.663  1.00 160.02 ? 1125 THR   B OG1 1 
ATOM   8605  C  CG2 . THR   B 2 821 ? 63.707  69.346  1.254   1.00 149.64 ? 1125 THR   B CG2 1 
ATOM   8606  N  N   . ALA   B 2 822 ? 61.440  67.878  0.334   1.00 154.31 ? 1126 ALA   B N   1 
ATOM   8607  C  CA  . ALA   B 2 822 ? 60.009  67.863  0.575   1.00 149.77 ? 1126 ALA   B CA  1 
ATOM   8608  C  C   . ALA   B 2 822 ? 59.410  69.229  0.267   1.00 147.37 ? 1126 ALA   B C   1 
ATOM   8609  O  O   . ALA   B 2 822 ? 58.512  69.360  -0.571  1.00 145.42 ? 1126 ALA   B O   1 
ATOM   8610  C  CB  . ALA   B 2 822 ? 59.730  67.442  2.019   1.00 146.67 ? 1126 ALA   B CB  1 
ATOM   8611  N  N   . ASP   B 2 823 ? 59.943  70.269  0.908   1.00 150.35 ? 1127 ASP   B N   1 
ATOM   8612  C  CA  . ASP   B 2 823 ? 59.269  71.564  0.966   1.00 151.60 ? 1127 ASP   B CA  1 
ATOM   8613  C  C   . ASP   B 2 823 ? 58.849  72.088  -0.399  1.00 152.73 ? 1127 ASP   B C   1 
ATOM   8614  O  O   . ASP   B 2 823 ? 57.903  72.875  -0.494  1.00 151.61 ? 1127 ASP   B O   1 
ATOM   8615  C  CB  . ASP   B 2 823 ? 60.173  72.583  1.651   1.00 151.58 ? 1127 ASP   B CB  1 
ATOM   8616  C  CG  . ASP   B 2 823 ? 60.585  72.141  3.032   1.00 152.94 ? 1127 ASP   B CG  1 
ATOM   8617  O  OD1 . ASP   B 2 823 ? 59.752  72.269  3.954   1.00 153.41 ? 1127 ASP   B OD1 1 
ATOM   8618  O  OD2 . ASP   B 2 823 ? 61.725  71.641  3.186   1.00 153.81 ? 1127 ASP   B OD2 1 
ATOM   8619  N  N   . ASP   B 2 824 ? 59.544  71.698  -1.464  1.00 162.82 ? 1128 ASP   B N   1 
ATOM   8620  C  CA  . ASP   B 2 824 ? 59.114  72.149  -2.782  1.00 164.07 ? 1128 ASP   B CA  1 
ATOM   8621  C  C   . ASP   B 2 824 ? 57.999  71.275  -3.340  1.00 161.07 ? 1128 ASP   B C   1 
ATOM   8622  O  O   . ASP   B 2 824 ? 57.213  71.743  -4.171  1.00 161.42 ? 1128 ASP   B O   1 
ATOM   8623  C  CB  . ASP   B 2 824 ? 60.306  72.194  -3.738  1.00 168.73 ? 1128 ASP   B CB  1 
ATOM   8624  C  CG  . ASP   B 2 824 ? 61.259  71.030  -3.535  1.00 169.56 ? 1128 ASP   B CG  1 
ATOM   8625  O  OD1 . ASP   B 2 824 ? 61.214  70.419  -2.445  1.00 172.59 ? 1128 ASP   B OD1 1 
ATOM   8626  O  OD2 . ASP   B 2 824 ? 62.042  70.729  -4.469  1.00 167.90 ? 1128 ASP   B OD2 1 
ATOM   8627  N  N   . LEU   B 2 825 ? 57.919  70.017  -2.905  1.00 145.32 ? 1129 LEU   B N   1 
ATOM   8628  C  CA  . LEU   B 2 825 ? 56.818  69.143  -3.294  1.00 137.16 ? 1129 LEU   B CA  1 
ATOM   8629  C  C   . LEU   B 2 825 ? 55.569  69.412  -2.482  1.00 132.64 ? 1129 LEU   B C   1 
ATOM   8630  O  O   . LEU   B 2 825 ? 54.454  69.204  -2.976  1.00 129.53 ? 1129 LEU   B O   1 
ATOM   8631  C  CB  . LEU   B 2 825 ? 57.211  67.677  -3.122  1.00 134.65 ? 1129 LEU   B CB  1 
ATOM   8632  C  CG  . LEU   B 2 825 ? 57.807  67.033  -4.366  1.00 131.35 ? 1129 LEU   B CG  1 
ATOM   8633  C  CD1 . LEU   B 2 825 ? 58.317  65.631  -4.083  1.00 126.06 ? 1129 LEU   B CD1 1 
ATOM   8634  C  CD2 . LEU   B 2 825 ? 56.738  67.019  -5.435  1.00 129.72 ? 1129 LEU   B CD2 1 
ATOM   8635  N  N   . ILE   B 2 826 ? 55.735  69.850  -1.232  1.00 134.46 ? 1130 ILE   B N   1 
ATOM   8636  C  CA  . ILE   B 2 826 ? 54.579  70.235  -0.436  1.00 125.21 ? 1130 ILE   B CA  1 
ATOM   8637  C  C   . ILE   B 2 826 ? 53.833  71.366  -1.122  1.00 124.51 ? 1130 ILE   B C   1 
ATOM   8638  O  O   . ILE   B 2 826 ? 52.602  71.457  -1.036  1.00 123.54 ? 1130 ILE   B O   1 
ATOM   8639  C  CB  . ILE   B 2 826 ? 54.990  70.609  0.996   1.00 118.93 ? 1130 ILE   B CB  1 
ATOM   8640  C  CG1 . ILE   B 2 826 ? 55.263  69.365  1.815   1.00 123.92 ? 1130 ILE   B CG1 1 
ATOM   8641  C  CG2 . ILE   B 2 826 ? 53.882  71.312  1.663   1.00 112.46 ? 1130 ILE   B CG2 1 
ATOM   8642  C  CD1 . ILE   B 2 826 ? 56.677  68.836  1.608   1.00 130.39 ? 1130 ILE   B CD1 1 
ATOM   8643  N  N   . LYS   B 2 827 ? 54.558  72.244  -1.816  1.00 125.42 ? 1131 LYS   B N   1 
ATOM   8644  C  CA  . LYS   B 2 827 ? 53.895  73.294  -2.583  1.00 125.67 ? 1131 LYS   B CA  1 
ATOM   8645  C  C   . LYS   B 2 827 ? 53.079  72.696  -3.727  1.00 125.03 ? 1131 LYS   B C   1 
ATOM   8646  O  O   . LYS   B 2 827 ? 51.874  72.954  -3.856  1.00 122.25 ? 1131 LYS   B O   1 
ATOM   8647  C  CB  . LYS   B 2 827 ? 54.933  74.288  -3.112  1.00 121.16 ? 1131 LYS   B CB  1 
ATOM   8648  N  N   . VAL   B 2 828 ? 53.712  71.847  -4.539  1.00 120.82 ? 1132 VAL   B N   1 
ATOM   8649  C  CA  . VAL   B 2 828 ? 53.070  71.351  -5.751  1.00 122.73 ? 1132 VAL   B CA  1 
ATOM   8650  C  C   . VAL   B 2 828 ? 51.729  70.701  -5.425  1.00 122.38 ? 1132 VAL   B C   1 
ATOM   8651  O  O   . VAL   B 2 828 ? 50.718  70.956  -6.093  1.00 122.38 ? 1132 VAL   B O   1 
ATOM   8652  C  CB  . VAL   B 2 828 ? 54.014  70.384  -6.492  1.00 124.30 ? 1132 VAL   B CB  1 
ATOM   8653  C  CG1 . VAL   B 2 828 ? 55.437  70.943  -6.511  1.00 131.93 ? 1132 VAL   B CG1 1 
ATOM   8654  C  CG2 . VAL   B 2 828 ? 54.000  69.012  -5.861  1.00 124.13 ? 1132 VAL   B CG2 1 
ATOM   8655  N  N   . VAL   B 2 829 ? 51.688  69.865  -4.387  1.00 121.12 ? 1133 VAL   B N   1 
ATOM   8656  C  CA  . VAL   B 2 829 ? 50.432  69.213  -4.034  1.00 118.18 ? 1133 VAL   B CA  1 
ATOM   8657  C  C   . VAL   B 2 829 ? 49.388  70.245  -3.641  1.00 121.82 ? 1133 VAL   B C   1 
ATOM   8658  O  O   . VAL   B 2 829 ? 48.214  70.135  -4.022  1.00 120.57 ? 1133 VAL   B O   1 
ATOM   8659  C  CB  . VAL   B 2 829 ? 50.642  68.202  -2.901  1.00 119.93 ? 1133 VAL   B CB  1 
ATOM   8660  C  CG1 . VAL   B 2 829 ? 49.433  68.241  -2.022  1.00 116.99 ? 1133 VAL   B CG1 1 
ATOM   8661  C  CG2 . VAL   B 2 829 ? 50.844  66.802  -3.459  1.00 116.17 ? 1133 VAL   B CG2 1 
ATOM   8662  N  N   . GLU   B 2 830 ? 49.791  71.248  -2.848  1.00 122.52 ? 1134 GLU   B N   1 
ATOM   8663  C  CA  . GLU   B 2 830 ? 48.853  72.275  -2.408  1.00 119.36 ? 1134 GLU   B CA  1 
ATOM   8664  C  C   . GLU   B 2 830 ? 48.087  72.861  -3.591  1.00 117.57 ? 1134 GLU   B C   1 
ATOM   8665  O  O   . GLU   B 2 830 ? 46.857  72.967  -3.548  1.00 118.98 ? 1134 GLU   B O   1 
ATOM   8666  C  CB  . GLU   B 2 830 ? 49.597  73.362  -1.619  1.00 123.29 ? 1134 GLU   B CB  1 
ATOM   8667  N  N   . GLU   B 2 831 ? 48.788  73.204  -4.678  1.00 114.89 ? 1135 GLU   B N   1 
ATOM   8668  C  CA  . GLU   B 2 831 ? 48.096  73.658  -5.880  1.00 116.10 ? 1135 GLU   B CA  1 
ATOM   8669  C  C   . GLU   B 2 831 ? 46.970  72.703  -6.259  1.00 117.14 ? 1135 GLU   B C   1 
ATOM   8670  O  O   . GLU   B 2 831 ? 45.872  73.138  -6.632  1.00 117.62 ? 1135 GLU   B O   1 
ATOM   8671  C  CB  . GLU   B 2 831 ? 49.087  73.800  -7.037  1.00 114.73 ? 1135 GLU   B CB  1 
ATOM   8672  N  N   . LEU   B 2 832 ? 47.220  71.391  -6.145  1.00 117.38 ? 1136 LEU   B N   1 
ATOM   8673  C  CA  . LEU   B 2 832 ? 46.246  70.390  -6.579  1.00 112.26 ? 1136 LEU   B CA  1 
ATOM   8674  C  C   . LEU   B 2 832 ? 45.039  70.334  -5.653  1.00 111.69 ? 1136 LEU   B C   1 
ATOM   8675  O  O   . LEU   B 2 832 ? 43.899  70.207  -6.121  1.00 112.45 ? 1136 LEU   B O   1 
ATOM   8676  C  CB  . LEU   B 2 832 ? 46.902  69.020  -6.654  1.00 109.26 ? 1136 LEU   B CB  1 
ATOM   8677  C  CG  . LEU   B 2 832 ? 48.219  68.987  -7.410  1.00 109.41 ? 1136 LEU   B CG  1 
ATOM   8678  C  CD1 . LEU   B 2 832 ? 48.660  67.548  -7.547  1.00 105.62 ? 1136 LEU   B CD1 1 
ATOM   8679  C  CD2 . LEU   B 2 832 ? 48.062  69.648  -8.770  1.00 108.49 ? 1136 LEU   B CD2 1 
ATOM   8680  N  N   . THR   B 2 833 ? 45.269  70.395  -4.336  1.00 110.39 ? 1137 THR   B N   1 
ATOM   8681  C  CA  . THR   B 2 833 ? 44.155  70.418  -3.396  1.00 110.23 ? 1137 THR   B CA  1 
ATOM   8682  C  C   . THR   B 2 833 ? 43.185  71.546  -3.730  1.00 111.25 ? 1137 THR   B C   1 
ATOM   8683  O  O   . THR   B 2 833 ? 41.976  71.416  -3.492  1.00 110.90 ? 1137 THR   B O   1 
ATOM   8684  C  CB  . THR   B 2 833 ? 44.681  70.533  -1.955  1.00 112.86 ? 1137 THR   B CB  1 
ATOM   8685  O  OG1 . THR   B 2 833 ? 45.086  71.879  -1.670  1.00 115.02 ? 1137 THR   B OG1 1 
ATOM   8686  C  CG2 . THR   B 2 833 ? 45.877  69.607  -1.748  1.00 113.01 ? 1137 THR   B CG2 1 
ATOM   8687  N  N   . ARG   B 2 834 ? 43.688  72.620  -4.346  1.00 111.20 ? 1138 ARG   B N   1 
ATOM   8688  C  CA  . ARG   B 2 834 ? 42.872  73.782  -4.667  1.00 112.38 ? 1138 ARG   B CA  1 
ATOM   8689  C  C   . ARG   B 2 834 ? 41.841  73.508  -5.758  1.00 110.93 ? 1138 ARG   B C   1 
ATOM   8690  O  O   . ARG   B 2 834 ? 40.818  74.203  -5.802  1.00 113.62 ? 1138 ARG   B O   1 
ATOM   8691  C  CB  . ARG   B 2 834 ? 43.779  74.946  -5.078  1.00 111.68 ? 1138 ARG   B CB  1 
ATOM   8692  N  N   . ILE   B 2 835 ? 42.073  72.524  -6.633  1.00 109.25 ? 1139 ILE   B N   1 
ATOM   8693  C  CA  . ILE   B 2 835 ? 41.115  72.246  -7.706  1.00 110.43 ? 1139 ILE   B CA  1 
ATOM   8694  C  C   . ILE   B 2 835 ? 39.739  71.849  -7.157  1.00 109.87 ? 1139 ILE   B C   1 
ATOM   8695  O  O   . ILE   B 2 835 ? 38.721  71.997  -7.851  1.00 103.76 ? 1139 ILE   B O   1 
ATOM   8696  C  CB  . ILE   B 2 835 ? 41.686  71.154  -8.647  1.00 108.49 ? 1139 ILE   B CB  1 
ATOM   8697  C  CG1 . ILE   B 2 835 ? 40.884  71.055  -9.960  1.00 114.47 ? 1139 ILE   B CG1 1 
ATOM   8698  C  CG2 . ILE   B 2 835 ? 41.670  69.813  -7.942  1.00 99.56  ? 1139 ILE   B CG2 1 
ATOM   8699  C  CD1 . ILE   B 2 835 ? 40.444  72.401  -10.597 1.00 107.76 ? 1139 ILE   B CD1 1 
ATOM   8700  N  N   . HIS   B 2 836 ? 39.683  71.341  -5.926  1.00 107.51 ? 1140 HIS   B N   1 
ATOM   8701  C  CA  . HIS   B 2 836 ? 38.415  71.004  -5.285  1.00 107.06 ? 1140 HIS   B CA  1 
ATOM   8702  C  C   . HIS   B 2 836 ? 38.400  71.553  -3.859  1.00 106.12 ? 1140 HIS   B C   1 
ATOM   8703  O  O   . HIS   B 2 836 ? 37.338  71.850  -3.311  1.00 108.24 ? 1140 HIS   B O   1 
ATOM   8704  C  CB  . HIS   B 2 836 ? 38.186  69.480  -5.284  1.00 107.81 ? 1140 HIS   B CB  1 
ATOM   8705  C  CG  . HIS   B 2 836 ? 39.195  68.721  -4.475  1.00 102.72 ? 1140 HIS   B CG  1 
ATOM   8706  N  ND1 . HIS   B 2 836 ? 38.889  68.113  -3.276  1.00 100.30 ? 1140 HIS   B ND1 1 
ATOM   8707  C  CD2 . HIS   B 2 836 ? 40.517  68.503  -4.678  1.00 102.15 ? 1140 HIS   B CD2 1 
ATOM   8708  C  CE1 . HIS   B 2 836 ? 39.975  67.542  -2.781  1.00 100.13 ? 1140 HIS   B CE1 1 
ATOM   8709  N  NE2 . HIS   B 2 836 ? 40.977  67.766  -3.612  1.00 101.67 ? 1140 HIS   B NE2 1 
ATOM   8710  N  N   . SER   C 3 3   ? 18.979  13.705  -71.273 1.00 109.24 ? 868  SER   C N   1 
ATOM   8711  C  CA  . SER   C 3 3   ? 20.173  13.477  -70.446 1.00 112.27 ? 868  SER   C CA  1 
ATOM   8712  C  C   . SER   C 3 3   ? 21.238  14.551  -70.603 1.00 111.45 ? 868  SER   C C   1 
ATOM   8713  O  O   . SER   C 3 3   ? 21.604  15.214  -69.640 1.00 108.81 ? 868  SER   C O   1 
ATOM   8714  C  CB  . SER   C 3 3   ? 20.808  12.116  -70.758 1.00 111.08 ? 868  SER   C CB  1 
ATOM   8715  O  OG  . SER   C 3 3   ? 22.214  12.214  -70.571 1.00 98.85  ? 868  SER   C OG  1 
ATOM   8716  N  N   . LEU   C 3 4   ? 21.768  14.685  -71.820 1.00 113.86 ? 869  LEU   C N   1 
ATOM   8717  C  CA  . LEU   C 3 4   ? 22.676  15.760  -72.185 1.00 108.72 ? 869  LEU   C CA  1 
ATOM   8718  C  C   . LEU   C 3 4   ? 22.022  17.097  -71.949 1.00 107.71 ? 869  LEU   C C   1 
ATOM   8719  O  O   . LEU   C 3 4   ? 22.734  18.070  -71.715 1.00 107.65 ? 869  LEU   C O   1 
ATOM   8720  C  CB  . LEU   C 3 4   ? 23.334  15.456  -73.528 1.00 112.66 ? 869  LEU   C CB  1 
ATOM   8721  C  CG  . LEU   C 3 4   ? 24.623  14.667  -73.620 1.00 110.72 ? 869  LEU   C CG  1 
ATOM   8722  C  CD1 . LEU   C 3 4   ? 25.081  14.700  -75.084 1.00 93.20  ? 869  LEU   C CD1 1 
ATOM   8723  C  CD2 . LEU   C 3 4   ? 25.670  15.268  -72.658 1.00 107.26 ? 869  LEU   C CD2 1 
ATOM   8724  N  N   . THR   C 3 5   ? 20.686  17.160  -72.016 1.00 110.38 ? 870  THR   C N   1 
ATOM   8725  C  CA  . THR   C 3 5   ? 19.928  18.395  -71.844 1.00 107.81 ? 870  THR   C CA  1 
ATOM   8726  C  C   . THR   C 3 5   ? 19.239  18.676  -70.511 1.00 107.60 ? 870  THR   C C   1 
ATOM   8727  O  O   . THR   C 3 5   ? 18.306  19.485  -70.456 1.00 109.23 ? 870  THR   C O   1 
ATOM   8728  C  CB  . THR   C 3 5   ? 18.887  18.321  -72.969 1.00 107.59 ? 870  THR   C CB  1 
ATOM   8729  O  OG1 . THR   C 3 5   ? 17.762  17.556  -72.515 1.00 112.38 ? 870  THR   C OG1 1 
ATOM   8730  C  CG2 . THR   C 3 5   ? 19.481  17.637  -74.170 1.00 107.90 ? 870  THR   C CG2 1 
ATOM   8731  N  N   . THR   C 3 6   ? 19.654  18.012  -69.445 1.00 103.35 ? 871  THR   C N   1 
ATOM   8732  C  CA  . THR   C 3 6   ? 19.178  18.321  -68.114 1.00 102.38 ? 871  THR   C CA  1 
ATOM   8733  C  C   . THR   C 3 6   ? 20.277  19.056  -67.363 1.00 101.69 ? 871  THR   C C   1 
ATOM   8734  O  O   . THR   C 3 6   ? 21.462  18.780  -67.545 1.00 100.51 ? 871  THR   C O   1 
ATOM   8735  C  CB  . THR   C 3 6   ? 18.761  17.066  -67.353 1.00 104.84 ? 871  THR   C CB  1 
ATOM   8736  O  OG1 . THR   C 3 6   ? 19.926  16.414  -66.817 1.00 110.29 ? 871  THR   C OG1 1 
ATOM   8737  C  CG2 . THR   C 3 6   ? 18.029  16.130  -68.284 1.00 102.10 ? 871  THR   C CG2 1 
ATOM   8738  N  N   . CYS   C 3 7   ? 19.879  20.021  -66.551 1.00 100.98 ? 872  CYS   C N   1 
ATOM   8739  C  CA  . CYS   C 3 7   ? 20.840  20.769  -65.765 1.00 98.80  ? 872  CYS   C CA  1 
ATOM   8740  C  C   . CYS   C 3 7   ? 21.229  19.957  -64.541 1.00 98.74  ? 872  CYS   C C   1 
ATOM   8741  O  O   . CYS   C 3 7   ? 20.367  19.454  -63.811 1.00 97.77  ? 872  CYS   C O   1 
ATOM   8742  C  CB  . CYS   C 3 7   ? 20.267  22.122  -65.347 1.00 94.83  ? 872  CYS   C CB  1 
ATOM   8743  S  SG  . CYS   C 3 7   ? 21.365  23.071  -64.235 1.00 96.83  ? 872  CYS   C SG  1 
ATOM   8744  N  N   . GLU   C 3 8   ? 22.533  19.846  -64.310 1.00 104.12 ? 873  GLU   C N   1 
ATOM   8745  C  CA  . GLU   C 3 8   ? 23.014  19.151  -63.127 1.00 106.65 ? 873  GLU   C CA  1 
ATOM   8746  C  C   . GLU   C 3 8   ? 22.597  19.825  -61.824 1.00 107.91 ? 873  GLU   C C   1 
ATOM   8747  O  O   . GLU   C 3 8   ? 22.601  19.162  -60.779 1.00 109.45 ? 873  GLU   C O   1 
ATOM   8748  C  CB  . GLU   C 3 8   ? 24.539  19.050  -63.168 1.00 110.91 ? 873  GLU   C CB  1 
ATOM   8749  C  CG  . GLU   C 3 8   ? 25.073  18.230  -64.313 1.00 117.75 ? 873  GLU   C CG  1 
ATOM   8750  C  CD  . GLU   C 3 8   ? 25.665  16.908  -63.849 1.00 125.24 ? 873  GLU   C CD  1 
ATOM   8751  O  OE1 . GLU   C 3 8   ? 26.060  16.823  -62.659 1.00 126.39 ? 873  GLU   C OE1 1 
ATOM   8752  O  OE2 . GLU   C 3 8   ? 25.733  15.959  -64.672 1.00 125.80 ? 873  GLU   C OE2 1 
ATOM   8753  N  N   . VAL   C 3 9   ? 22.256  21.113  -61.846 1.00 100.22 ? 874  VAL   C N   1 
ATOM   8754  C  CA  . VAL   C 3 9   ? 22.139  21.909  -60.627 1.00 92.96  ? 874  VAL   C CA  1 
ATOM   8755  C  C   . VAL   C 3 9   ? 20.694  22.064  -60.183 1.00 92.15  ? 874  VAL   C C   1 
ATOM   8756  O  O   . VAL   C 3 9   ? 20.373  21.894  -59.008 1.00 94.74  ? 874  VAL   C O   1 
ATOM   8757  C  CB  . VAL   C 3 9   ? 22.817  23.278  -60.828 1.00 89.45  ? 874  VAL   C CB  1 
ATOM   8758  C  CG1 . VAL   C 3 9   ? 22.685  24.118  -59.573 1.00 92.31  ? 874  VAL   C CG1 1 
ATOM   8759  C  CG2 . VAL   C 3 9   ? 24.262  23.063  -61.172 1.00 89.02  ? 874  VAL   C CG2 1 
ATOM   8760  N  N   . CYS   C 3 10  ? 19.807  22.395  -61.105 1.00 91.58  ? 875  CYS   C N   1 
ATOM   8761  C  CA  . CYS   C 3 10  ? 18.405  22.587  -60.781 1.00 88.59  ? 875  CYS   C CA  1 
ATOM   8762  C  C   . CYS   C 3 10  ? 17.522  21.498  -61.348 1.00 91.28  ? 875  CYS   C C   1 
ATOM   8763  O  O   . CYS   C 3 10  ? 16.349  21.413  -60.962 1.00 91.72  ? 875  CYS   C O   1 
ATOM   8764  C  CB  . CYS   C 3 10  ? 17.913  23.943  -61.314 1.00 88.18  ? 875  CYS   C CB  1 
ATOM   8765  S  SG  . CYS   C 3 10  ? 17.838  24.087  -63.151 1.00 88.66  ? 875  CYS   C SG  1 
ATOM   8766  N  N   . GLY   C 3 11  ? 18.040  20.701  -62.283 1.00 91.18  ? 876  GLY   C N   1 
ATOM   8767  C  CA  . GLY   C 3 11  ? 17.283  19.606  -62.852 1.00 93.28  ? 876  GLY   C CA  1 
ATOM   8768  C  C   . GLY   C 3 11  ? 16.397  19.981  -64.015 1.00 95.21  ? 876  GLY   C C   1 
ATOM   8769  O  O   . GLY   C 3 11  ? 15.403  19.293  -64.275 1.00 95.46  ? 876  GLY   C O   1 
ATOM   8770  N  N   . ALA   C 3 12  ? 16.723  21.048  -64.736 1.00 96.33  ? 877  ALA   C N   1 
ATOM   8771  C  CA  . ALA   C 3 12  ? 15.897  21.469  -65.857 1.00 92.19  ? 877  ALA   C CA  1 
ATOM   8772  C  C   . ALA   C 3 12  ? 16.183  20.594  -67.076 1.00 96.56  ? 877  ALA   C C   1 
ATOM   8773  O  O   . ALA   C 3 12  ? 17.251  19.991  -67.193 1.00 99.70  ? 877  ALA   C O   1 
ATOM   8774  C  CB  . ALA   C 3 12  ? 16.151  22.946  -66.161 1.00 92.91  ? 877  ALA   C CB  1 
ATOM   8775  N  N   . CYS   C 3 13  ? 15.219  20.506  -67.985 1.00 95.50  ? 878  CYS   C N   1 
ATOM   8776  C  CA  . CYS   C 3 13  ? 15.402  19.692  -69.183 1.00 101.89 ? 878  CYS   C CA  1 
ATOM   8777  C  C   . CYS   C 3 13  ? 14.996  20.469  -70.430 1.00 102.52 ? 878  CYS   C C   1 
ATOM   8778  O  O   . CYS   C 3 13  ? 13.810  20.750  -70.617 1.00 100.09 ? 878  CYS   C O   1 
ATOM   8779  C  CB  . CYS   C 3 13  ? 14.616  18.392  -69.096 1.00 98.19  ? 878  CYS   C CB  1 
ATOM   8780  S  SG  . CYS   C 3 13  ? 15.560  17.051  -69.827 1.00 107.54 ? 878  CYS   C SG  1 
ATOM   8781  N  N   . PHE   C 3 14  ? 15.971  20.746  -71.314 1.00 101.86 ? 879  PHE   C N   1 
ATOM   8782  C  CA  . PHE   C 3 14  ? 15.778  21.430  -72.587 1.00 103.11 ? 879  PHE   C CA  1 
ATOM   8783  C  C   . PHE   C 3 14  ? 15.709  20.470  -73.756 1.00 102.62 ? 879  PHE   C C   1 
ATOM   8784  O  O   . PHE   C 3 14  ? 16.231  19.359  -73.705 1.00 102.86 ? 879  PHE   C O   1 
ATOM   8785  C  CB  . PHE   C 3 14  ? 16.900  22.418  -72.842 1.00 99.85  ? 879  PHE   C CB  1 
ATOM   8786  C  CG  . PHE   C 3 14  ? 17.044  23.394  -71.776 1.00 103.39 ? 879  PHE   C CG  1 
ATOM   8787  C  CD1 . PHE   C 3 14  ? 15.941  24.049  -71.274 1.00 104.55 ? 879  PHE   C CD1 1 
ATOM   8788  C  CD2 . PHE   C 3 14  ? 18.308  23.673  -71.258 1.00 104.74 ? 879  PHE   C CD2 1 
ATOM   8789  C  CE1 . PHE   C 3 14  ? 16.067  24.970  -70.266 1.00 100.20 ? 879  PHE   C CE1 1 
ATOM   8790  C  CE2 . PHE   C 3 14  ? 18.452  24.591  -70.245 1.00 102.15 ? 879  PHE   C CE2 1 
ATOM   8791  C  CZ  . PHE   C 3 14  ? 17.330  25.242  -69.743 1.00 98.79  ? 879  PHE   C CZ  1 
ATOM   8792  N  N   . GLU   C 3 15  ? 15.087  20.938  -74.838 1.00 99.94  ? 880  GLU   C N   1 
ATOM   8793  C  CA  . GLU   C 3 15  ? 15.075  20.121  -76.038 1.00 105.66 ? 880  GLU   C CA  1 
ATOM   8794  C  C   . GLU   C 3 15  ? 16.456  20.058  -76.675 1.00 108.74 ? 880  GLU   C C   1 
ATOM   8795  O  O   . GLU   C 3 15  ? 16.734  19.134  -77.448 1.00 110.57 ? 880  GLU   C O   1 
ATOM   8796  C  CB  . GLU   C 3 15  ? 14.018  20.646  -77.023 1.00 99.39  ? 880  GLU   C CB  1 
ATOM   8797  N  N   . THR   C 3 16  ? 17.350  20.967  -76.295 1.00 106.22 ? 881  THR   C N   1 
ATOM   8798  C  CA  . THR   C 3 16  ? 18.565  21.208  -77.050 1.00 105.40 ? 881  THR   C CA  1 
ATOM   8799  C  C   . THR   C 3 16  ? 19.762  21.392  -76.131 1.00 102.33 ? 881  THR   C C   1 
ATOM   8800  O  O   . THR   C 3 16  ? 19.649  21.993  -75.059 1.00 99.08  ? 881  THR   C O   1 
ATOM   8801  C  CB  . THR   C 3 16  ? 18.395  22.445  -77.908 1.00 107.16 ? 881  THR   C CB  1 
ATOM   8802  O  OG1 . THR   C 3 16  ? 19.665  22.792  -78.475 1.00 112.01 ? 881  THR   C OG1 1 
ATOM   8803  C  CG2 . THR   C 3 16  ? 17.830  23.605  -77.041 1.00 101.67 ? 881  THR   C CG2 1 
ATOM   8804  N  N   . ARG   C 3 17  ? 20.920  20.899  -76.577 1.00 105.41 ? 882  ARG   C N   1 
ATOM   8805  C  CA  . ARG   C 3 17  ? 22.147  21.042  -75.802 1.00 106.09 ? 882  ARG   C CA  1 
ATOM   8806  C  C   . ARG   C 3 17  ? 22.768  22.434  -75.922 1.00 99.96  ? 882  ARG   C C   1 
ATOM   8807  O  O   . ARG   C 3 17  ? 23.791  22.686  -75.283 1.00 99.56  ? 882  ARG   C O   1 
ATOM   8808  C  CB  . ARG   C 3 17  ? 23.177  19.947  -76.177 1.00 106.15 ? 882  ARG   C CB  1 
ATOM   8809  N  N   . LYS   C 3 18  ? 22.192  23.348  -76.704 1.00 99.40  ? 883  LYS   C N   1 
ATOM   8810  C  CA  . LYS   C 3 18  ? 22.575  24.748  -76.553 1.00 101.09 ? 883  LYS   C CA  1 
ATOM   8811  C  C   . LYS   C 3 18  ? 21.750  25.444  -75.485 1.00 98.63  ? 883  LYS   C C   1 
ATOM   8812  O  O   . LYS   C 3 18  ? 22.291  26.187  -74.661 1.00 98.67  ? 883  LYS   C O   1 
ATOM   8813  C  CB  . LYS   C 3 18  ? 22.383  25.525  -77.853 1.00 99.93  ? 883  LYS   C CB  1 
ATOM   8814  C  CG  . LYS   C 3 18  ? 22.543  27.026  -77.670 1.00 96.51  ? 883  LYS   C CG  1 
ATOM   8815  C  CD  . LYS   C 3 18  ? 23.891  27.520  -78.220 1.00 96.85  ? 883  LYS   C CD  1 
ATOM   8816  C  CE  . LYS   C 3 18  ? 24.181  28.980  -77.876 1.00 95.08  ? 883  LYS   C CE  1 
ATOM   8817  N  NZ  . LYS   C 3 18  ? 23.389  29.951  -78.668 1.00 98.43  ? 883  LYS   C NZ  1 
ATOM   8818  N  N   . GLY   C 3 19  ? 20.440  25.206  -75.501 1.00 96.80  ? 884  GLY   C N   1 
ATOM   8819  C  CA  . GLY   C 3 19  ? 19.564  25.644  -74.439 1.00 97.38  ? 884  GLY   C CA  1 
ATOM   8820  C  C   . GLY   C 3 19  ? 20.178  25.396  -73.076 1.00 99.32  ? 884  GLY   C C   1 
ATOM   8821  O  O   . GLY   C 3 19  ? 20.025  26.206  -72.151 1.00 102.68 ? 884  GLY   C O   1 
ATOM   8822  N  N   . LEU   C 3 20  ? 20.941  24.307  -72.963 1.00 97.57  ? 885  LEU   C N   1 
ATOM   8823  C  CA  . LEU   C 3 20  ? 21.481  23.941  -71.660 1.00 101.26 ? 885  LEU   C CA  1 
ATOM   8824  C  C   . LEU   C 3 20  ? 22.652  24.839  -71.285 1.00 99.78  ? 885  LEU   C C   1 
ATOM   8825  O  O   . LEU   C 3 20  ? 22.863  25.113  -70.096 1.00 98.98  ? 885  LEU   C O   1 
ATOM   8826  C  CB  . LEU   C 3 20  ? 21.919  22.476  -71.646 1.00 101.34 ? 885  LEU   C CB  1 
ATOM   8827  C  CG  . LEU   C 3 20  ? 21.212  21.625  -70.597 1.00 99.24  ? 885  LEU   C CG  1 
ATOM   8828  C  CD1 . LEU   C 3 20  ? 21.851  20.263  -70.463 1.00 109.61 ? 885  LEU   C CD1 1 
ATOM   8829  C  CD2 . LEU   C 3 20  ? 21.160  22.307  -69.259 1.00 95.90  ? 885  LEU   C CD2 1 
ATOM   8830  N  N   . SER   C 3 21  ? 23.444  25.277  -72.265 1.00 93.60  ? 886  SER   C N   1 
ATOM   8831  C  CA  . SER   C 3 21  ? 24.565  26.145  -71.930 1.00 96.06  ? 886  SER   C CA  1 
ATOM   8832  C  C   . SER   C 3 21  ? 24.078  27.547  -71.566 1.00 101.06 ? 886  SER   C C   1 
ATOM   8833  O  O   . SER   C 3 21  ? 24.522  28.129  -70.565 1.00 99.76  ? 886  SER   C O   1 
ATOM   8834  C  CB  . SER   C 3 21  ? 25.559  26.182  -73.085 1.00 95.65  ? 886  SER   C CB  1 
ATOM   8835  O  OG  . SER   C 3 21  ? 25.012  26.927  -74.162 1.00 102.88 ? 886  SER   C OG  1 
ATOM   8836  N  N   . SER   C 3 22  ? 23.153  28.102  -72.353 1.00 96.11  ? 887  SER   C N   1 
ATOM   8837  C  CA  . SER   C 3 22  ? 22.610  29.409  -72.008 1.00 98.03  ? 887  SER   C CA  1 
ATOM   8838  C  C   . SER   C 3 22  ? 21.939  29.386  -70.650 1.00 101.40 ? 887  SER   C C   1 
ATOM   8839  O  O   . SER   C 3 22  ? 21.792  30.438  -70.015 1.00 109.48 ? 887  SER   C O   1 
ATOM   8840  C  CB  . SER   C 3 22  ? 21.622  29.880  -73.072 1.00 97.42  ? 887  SER   C CB  1 
ATOM   8841  O  OG  . SER   C 3 22  ? 20.545  28.973  -73.156 1.00 97.00  ? 887  SER   C OG  1 
ATOM   8842  N  N   . HIS   C 3 23  ? 21.516  28.208  -70.197 1.00 97.76  ? 888  HIS   C N   1 
ATOM   8843  C  CA  . HIS   C 3 23  ? 21.058  28.077  -68.820 1.00 100.68 ? 888  HIS   C CA  1 
ATOM   8844  C  C   . HIS   C 3 23  ? 22.237  28.071  -67.854 1.00 105.58 ? 888  HIS   C C   1 
ATOM   8845  O  O   . HIS   C 3 23  ? 22.169  28.683  -66.783 1.00 110.43 ? 888  HIS   C O   1 
ATOM   8846  C  CB  . HIS   C 3 23  ? 20.213  26.812  -68.672 1.00 98.22  ? 888  HIS   C CB  1 
ATOM   8847  C  CG  . HIS   C 3 23  ? 19.812  26.499  -67.263 1.00 98.07  ? 888  HIS   C CG  1 
ATOM   8848  N  ND1 . HIS   C 3 23  ? 19.191  27.411  -66.438 1.00 105.20 ? 888  HIS   C ND1 1 
ATOM   8849  C  CD2 . HIS   C 3 23  ? 19.921  25.358  -66.542 1.00 98.11  ? 888  HIS   C CD2 1 
ATOM   8850  C  CE1 . HIS   C 3 23  ? 18.950  26.851  -65.263 1.00 102.63 ? 888  HIS   C CE1 1 
ATOM   8851  N  NE2 . HIS   C 3 23  ? 19.380  25.603  -65.302 1.00 96.68  ? 888  HIS   C NE2 1 
ATOM   8852  N  N   . ALA   C 3 24  ? 23.342  27.411  -68.222 1.00 103.74 ? 889  ALA   C N   1 
ATOM   8853  C  CA  . ALA   C 3 24  ? 24.474  27.293  -67.302 1.00 101.25 ? 889  ALA   C CA  1 
ATOM   8854  C  C   . ALA   C 3 24  ? 25.026  28.664  -66.910 1.00 108.35 ? 889  ALA   C C   1 
ATOM   8855  O  O   . ALA   C 3 24  ? 25.494  28.850  -65.780 1.00 115.49 ? 889  ALA   C O   1 
ATOM   8856  C  CB  . ALA   C 3 24  ? 25.570  26.422  -67.913 1.00 98.98  ? 889  ALA   C CB  1 
ATOM   8857  N  N   . ARG   C 3 25  ? 24.995  29.636  -67.822 1.00 106.94 ? 890  ARG   C N   1 
ATOM   8858  C  CA  . ARG   C 3 25  ? 25.319  30.998  -67.423 1.00 106.02 ? 890  ARG   C CA  1 
ATOM   8859  C  C   . ARG   C 3 25  ? 24.541  31.391  -66.172 1.00 110.89 ? 890  ARG   C C   1 
ATOM   8860  O  O   . ARG   C 3 25  ? 25.127  31.682  -65.123 1.00 114.73 ? 890  ARG   C O   1 
ATOM   8861  C  CB  . ARG   C 3 25  ? 25.024  31.974  -68.570 1.00 113.26 ? 890  ARG   C CB  1 
ATOM   8862  N  N   . SER   C 3 26  ? 23.212  31.359  -66.252 1.00 114.85 ? 891  SER   C N   1 
ATOM   8863  C  CA  . SER   C 3 26  ? 22.360  31.874  -65.183 1.00 116.76 ? 891  SER   C CA  1 
ATOM   8864  C  C   . SER   C 3 26  ? 22.643  31.325  -63.774 1.00 118.42 ? 891  SER   C C   1 
ATOM   8865  O  O   . SER   C 3 26  ? 22.215  31.915  -62.770 1.00 117.55 ? 891  SER   C O   1 
ATOM   8866  C  CB  . SER   C 3 26  ? 20.900  31.826  -65.643 1.00 114.91 ? 891  SER   C CB  1 
ATOM   8867  O  OG  . SER   C 3 26  ? 20.283  30.602  -65.267 1.00 118.20 ? 891  SER   C OG  1 
ATOM   8868  N  N   . HIS   C 3 27  ? 23.356  30.200  -63.674 1.00 110.20 ? 892  HIS   C N   1 
ATOM   8869  C  CA  . HIS   C 3 27  ? 23.953  29.787  -62.410 1.00 106.99 ? 892  HIS   C CA  1 
ATOM   8870  C  C   . HIS   C 3 27  ? 25.239  30.450  -61.948 1.00 111.95 ? 892  HIS   C C   1 
ATOM   8871  O  O   . HIS   C 3 27  ? 25.401  30.681  -60.743 1.00 120.37 ? 892  HIS   C O   1 
ATOM   8872  C  CB  . HIS   C 3 27  ? 24.168  28.267  -62.419 1.00 107.43 ? 892  HIS   C CB  1 
ATOM   8873  C  CG  . HIS   C 3 27  ? 22.905  27.459  -62.364 1.00 101.93 ? 892  HIS   C CG  1 
ATOM   8874  N  ND1 . HIS   C 3 27  ? 22.023  27.513  -61.306 1.00 99.01  ? 892  HIS   C ND1 1 
ATOM   8875  C  CD2 . HIS   C 3 27  ? 22.398  26.547  -63.227 1.00 97.85  ? 892  HIS   C CD2 1 
ATOM   8876  C  CE1 . HIS   C 3 27  ? 21.019  26.683  -61.529 1.00 92.62  ? 892  HIS   C CE1 1 
ATOM   8877  N  NE2 . HIS   C 3 27  ? 21.222  26.085  -62.689 1.00 91.61  ? 892  HIS   C NE2 1 
ATOM   8878  N  N   . LEU   C 3 28  ? 26.139  30.780  -62.875 1.00 106.81 ? 893  LEU   C N   1 
ATOM   8879  C  CA  . LEU   C 3 28  ? 27.387  31.475  -62.537 1.00 114.92 ? 893  LEU   C CA  1 
ATOM   8880  C  C   . LEU   C 3 28  ? 27.228  33.023  -62.426 1.00 117.46 ? 893  LEU   C C   1 
ATOM   8881  O  O   . LEU   C 3 28  ? 26.810  33.724  -63.372 1.00 106.48 ? 893  LEU   C O   1 
ATOM   8882  C  CB  . LEU   C 3 28  ? 28.482  31.123  -63.563 1.00 116.29 ? 893  LEU   C CB  1 
ATOM   8883  C  CG  . LEU   C 3 28  ? 29.243  29.786  -63.410 1.00 118.28 ? 893  LEU   C CG  1 
ATOM   8884  C  CD1 . LEU   C 3 28  ? 28.483  28.603  -64.022 1.00 112.58 ? 893  LEU   C CD1 1 
ATOM   8885  C  CD2 . LEU   C 3 28  ? 30.684  29.845  -63.954 1.00 110.57 ? 893  LEU   C CD2 1 
ATOM   8886  N  N   . HIS   D 1 4   ? 14.771  -43.424 -12.732 1.00 126.83 ? 73   HIS   D N   1 
ATOM   8887  C  CA  . HIS   D 1 4   ? 13.808  -42.334 -12.880 1.00 135.22 ? 73   HIS   D CA  1 
ATOM   8888  C  C   . HIS   D 1 4   ? 14.356  -41.244 -13.781 1.00 147.81 ? 73   HIS   D C   1 
ATOM   8889  O  O   . HIS   D 1 4   ? 15.386  -41.428 -14.432 1.00 151.14 ? 73   HIS   D O   1 
ATOM   8890  C  CB  . HIS   D 1 4   ? 13.445  -41.736 -11.525 1.00 129.60 ? 73   HIS   D CB  1 
ATOM   8891  C  CG  . HIS   D 1 4   ? 13.079  -42.754 -10.499 1.00 121.26 ? 73   HIS   D CG  1 
ATOM   8892  N  ND1 . HIS   D 1 4   ? 13.453  -42.643 -9.178  1.00 118.41 ? 73   HIS   D ND1 1 
ATOM   8893  C  CD2 . HIS   D 1 4   ? 12.374  -43.905 -10.596 1.00 126.36 ? 73   HIS   D CD2 1 
ATOM   8894  C  CE1 . HIS   D 1 4   ? 12.992  -43.680 -8.503  1.00 125.43 ? 73   HIS   D CE1 1 
ATOM   8895  N  NE2 . HIS   D 1 4   ? 12.331  -44.460 -9.340  1.00 131.56 ? 73   HIS   D NE2 1 
ATOM   8896  N  N   . ASP   D 1 5   ? 13.665  -40.103 -13.809 1.00 156.04 ? 74   ASP   D N   1 
ATOM   8897  C  CA  . ASP   D 1 5   ? 14.059  -38.961 -14.621 1.00 161.63 ? 74   ASP   D CA  1 
ATOM   8898  C  C   . ASP   D 1 5   ? 14.733  -37.913 -13.736 1.00 162.67 ? 74   ASP   D C   1 
ATOM   8899  O  O   . ASP   D 1 5   ? 14.772  -38.040 -12.511 1.00 161.33 ? 74   ASP   D O   1 
ATOM   8900  C  CB  . ASP   D 1 5   ? 12.850  -38.395 -15.369 1.00 162.74 ? 74   ASP   D CB  1 
ATOM   8901  C  CG  . ASP   D 1 5   ? 12.605  -39.103 -16.693 1.00 166.41 ? 74   ASP   D CG  1 
ATOM   8902  O  OD1 . ASP   D 1 5   ? 13.576  -39.217 -17.479 1.00 162.53 ? 74   ASP   D OD1 1 
ATOM   8903  O  OD2 . ASP   D 1 5   ? 11.461  -39.556 -16.941 1.00 163.80 ? 74   ASP   D OD2 1 
ATOM   8904  N  N   . ASP   D 1 6   ? 15.269  -36.861 -14.364 1.00 184.39 ? 75   ASP   D N   1 
ATOM   8905  C  CA  . ASP   D 1 6   ? 16.144  -35.936 -13.647 1.00 185.34 ? 75   ASP   D CA  1 
ATOM   8906  C  C   . ASP   D 1 6   ? 15.385  -35.180 -12.549 1.00 185.20 ? 75   ASP   D C   1 
ATOM   8907  O  O   . ASP   D 1 6   ? 15.795  -35.195 -11.380 1.00 183.76 ? 75   ASP   D O   1 
ATOM   8908  C  CB  . ASP   D 1 6   ? 16.797  -34.956 -14.618 1.00 186.03 ? 75   ASP   D CB  1 
ATOM   8909  C  CG  . ASP   D 1 6   ? 17.974  -34.242 -13.996 1.00 183.30 ? 75   ASP   D CG  1 
ATOM   8910  O  OD1 . ASP   D 1 6   ? 18.748  -34.911 -13.272 1.00 184.18 ? 75   ASP   D OD1 1 
ATOM   8911  O  OD2 . ASP   D 1 6   ? 18.122  -33.025 -14.221 1.00 183.09 ? 75   ASP   D OD2 1 
ATOM   8912  N  N   . ASP   D 1 7   ? 14.283  -34.503 -12.900 1.00 163.05 ? 76   ASP   D N   1 
ATOM   8913  C  CA  . ASP   D 1 7   ? 13.424  -33.801 -11.938 1.00 150.16 ? 76   ASP   D CA  1 
ATOM   8914  C  C   . ASP   D 1 7   ? 12.141  -34.565 -11.680 1.00 145.32 ? 76   ASP   D C   1 
ATOM   8915  O  O   . ASP   D 1 7   ? 11.084  -33.948 -11.601 1.00 146.79 ? 76   ASP   D O   1 
ATOM   8916  C  CB  . ASP   D 1 7   ? 13.086  -32.395 -12.460 1.00 153.15 ? 76   ASP   D CB  1 
ATOM   8917  C  CG  . ASP   D 1 7   ? 12.442  -31.438 -11.414 1.00 150.59 ? 76   ASP   D CG  1 
ATOM   8918  O  OD1 . ASP   D 1 7   ? 11.622  -31.897 -10.534 1.00 146.62 ? 76   ASP   D OD1 1 
ATOM   8919  O  OD2 . ASP   D 1 7   ? 12.711  -30.232 -11.548 1.00 148.20 ? 76   ASP   D OD2 1 
ATOM   8920  N  N   . SER   D 1 8   ? 12.196  -35.882 -11.572 1.00 148.00 ? 77   SER   D N   1 
ATOM   8921  C  CA  . SER   D 1 8   ? 10.975  -36.656 -11.432 1.00 144.01 ? 77   SER   D CA  1 
ATOM   8922  C  C   . SER   D 1 8   ? 10.447  -36.578 -10.005 1.00 139.48 ? 77   SER   D C   1 
ATOM   8923  O  O   . SER   D 1 8   ? 11.203  -36.403 -9.041  1.00 129.53 ? 77   SER   D O   1 
ATOM   8924  C  CB  . SER   D 1 8   ? 11.210  -38.116 -11.825 1.00 142.16 ? 77   SER   D CB  1 
ATOM   8925  O  OG  . SER   D 1 8   ? 10.003  -38.830 -11.742 1.00 138.90 ? 77   SER   D OG  1 
ATOM   8926  N  N   . CYS   D 1 9   ? 9.127   -36.683 -9.887  1.00 150.80 ? 78   CYS   D N   1 
ATOM   8927  C  CA  . CYS   D 1 9   ? 8.463   -36.843 -8.603  1.00 148.42 ? 78   CYS   D CA  1 
ATOM   8928  C  C   . CYS   D 1 9   ? 8.079   -38.309 -8.465  1.00 145.45 ? 78   CYS   D C   1 
ATOM   8929  O  O   . CYS   D 1 9   ? 7.286   -38.819 -9.263  1.00 147.39 ? 78   CYS   D O   1 
ATOM   8930  C  CB  . CYS   D 1 9   ? 7.227   -35.950 -8.493  1.00 148.78 ? 78   CYS   D CB  1 
ATOM   8931  S  SG  . CYS   D 1 9   ? 7.401   -34.294 -9.206  1.00 158.61 ? 78   CYS   D SG  1 
ATOM   8932  N  N   . GLN   D 1 10  ? 8.625   -38.976 -7.452  1.00 125.99 ? 79   GLN   D N   1 
ATOM   8933  C  CA  . GLN   D 1 10  ? 8.451   -40.411 -7.281  1.00 126.09 ? 79   GLN   D CA  1 
ATOM   8934  C  C   . GLN   D 1 10  ? 8.000   -40.714 -5.858  1.00 121.43 ? 79   GLN   D C   1 
ATOM   8935  O  O   . GLN   D 1 10  ? 8.268   -39.944 -4.932  1.00 118.41 ? 79   GLN   D O   1 
ATOM   8936  C  CB  . GLN   D 1 10  ? 9.757   -41.164 -7.594  1.00 126.53 ? 79   GLN   D CB  1 
ATOM   8937  C  CG  . GLN   D 1 10  ? 10.445  -40.718 -8.884  1.00 126.75 ? 79   GLN   D CG  1 
ATOM   8938  C  CD  . GLN   D 1 10  ? 9.650   -41.067 -10.128 1.00 131.82 ? 79   GLN   D CD  1 
ATOM   8939  O  OE1 . GLN   D 1 10  ? 8.762   -40.320 -10.538 1.00 138.29 ? 79   GLN   D OE1 1 
ATOM   8940  N  NE2 . GLN   D 1 10  ? 9.969   -42.201 -10.741 1.00 127.41 ? 79   GLN   D NE2 1 
ATOM   8941  N  N   . VAL   D 1 11  ? 7.309   -41.842 -5.691  1.00 118.62 ? 80   VAL   D N   1 
ATOM   8942  C  CA  . VAL   D 1 11  ? 6.883   -42.315 -4.380  1.00 115.38 ? 80   VAL   D CA  1 
ATOM   8943  C  C   . VAL   D 1 11  ? 7.655   -43.592 -4.103  1.00 115.73 ? 80   VAL   D C   1 
ATOM   8944  O  O   . VAL   D 1 11  ? 7.316   -44.659 -4.624  1.00 123.08 ? 80   VAL   D O   1 
ATOM   8945  C  CB  . VAL   D 1 11  ? 5.370   -42.552 -4.318  1.00 118.23 ? 80   VAL   D CB  1 
ATOM   8946  C  CG1 . VAL   D 1 11  ? 4.954   -42.977 -2.909  1.00 119.85 ? 80   VAL   D CG1 1 
ATOM   8947  C  CG2 . VAL   D 1 11  ? 4.620   -41.300 -4.773  1.00 113.35 ? 80   VAL   D CG2 1 
ATOM   8948  N  N   . ILE   D 1 12  ? 8.702   -43.493 -3.294  1.00 115.80 ? 81   ILE   D N   1 
ATOM   8949  C  CA  . ILE   D 1 12  ? 9.651   -44.577 -3.090  1.00 118.18 ? 81   ILE   D CA  1 
ATOM   8950  C  C   . ILE   D 1 12  ? 9.571   -45.006 -1.630  1.00 118.24 ? 81   ILE   D C   1 
ATOM   8951  O  O   . ILE   D 1 12  ? 9.539   -44.149 -0.745  1.00 120.37 ? 81   ILE   D O   1 
ATOM   8952  C  CB  . ILE   D 1 12  ? 11.090  -44.168 -3.462  1.00 121.13 ? 81   ILE   D CB  1 
ATOM   8953  C  CG1 . ILE   D 1 12  ? 11.171  -43.687 -4.927  1.00 121.53 ? 81   ILE   D CG1 1 
ATOM   8954  C  CG2 . ILE   D 1 12  ? 12.070  -45.325 -3.212  1.00 117.58 ? 81   ILE   D CG2 1 
ATOM   8955  C  CD1 . ILE   D 1 12  ? 10.989  -44.794 -6.002  1.00 124.19 ? 81   ILE   D CD1 1 
ATOM   8956  N  N   . PRO   D 1 13  ? 9.520   -46.301 -1.332  1.00 117.21 ? 82   PRO   D N   1 
ATOM   8957  C  CA  . PRO   D 1 13  ? 9.479   -46.732 0.069   1.00 118.25 ? 82   PRO   D CA  1 
ATOM   8958  C  C   . PRO   D 1 13  ? 10.804  -46.479 0.762   1.00 112.12 ? 82   PRO   D C   1 
ATOM   8959  O  O   . PRO   D 1 13  ? 11.874  -46.577 0.162   1.00 109.91 ? 82   PRO   D O   1 
ATOM   8960  C  CB  . PRO   D 1 13  ? 9.198   -48.233 -0.031  1.00 118.96 ? 82   PRO   D CB  1 
ATOM   8961  C  CG  . PRO   D 1 13  ? 9.796   -48.619 -1.339  1.00 114.65 ? 82   PRO   D CG  1 
ATOM   8962  C  CD  . PRO   D 1 13  ? 9.560   -47.443 -2.258  1.00 118.44 ? 82   PRO   D CD  1 
ATOM   8963  N  N   . VAL   D 1 14  ? 10.729  -46.182 2.044   1.00 117.80 ? 83   VAL   D N   1 
ATOM   8964  C  CA  . VAL   D 1 14  ? 11.900  -45.810 2.824   1.00 115.43 ? 83   VAL   D CA  1 
ATOM   8965  C  C   . VAL   D 1 14  ? 12.387  -47.009 3.610   1.00 114.65 ? 83   VAL   D C   1 
ATOM   8966  O  O   . VAL   D 1 14  ? 11.589  -47.708 4.240   1.00 118.46 ? 83   VAL   D O   1 
ATOM   8967  C  CB  . VAL   D 1 14  ? 11.584  -44.653 3.785   1.00 116.29 ? 83   VAL   D CB  1 
ATOM   8968  C  CG1 . VAL   D 1 14  ? 12.875  -44.012 4.252   1.00 108.72 ? 83   VAL   D CG1 1 
ATOM   8969  C  CG2 . VAL   D 1 14  ? 10.650  -43.660 3.119   1.00 122.02 ? 83   VAL   D CG2 1 
ATOM   8970  N  N   . LEU   D 1 15  ? 13.695  -47.220 3.623   1.00 113.17 ? 84   LEU   D N   1 
ATOM   8971  C  CA  . LEU   D 1 15  ? 14.247  -48.219 4.526   1.00 120.33 ? 84   LEU   D CA  1 
ATOM   8972  C  C   . LEU   D 1 15  ? 13.991  -47.768 5.962   1.00 125.76 ? 84   LEU   D C   1 
ATOM   8973  O  O   . LEU   D 1 15  ? 14.293  -46.620 6.306   1.00 126.69 ? 84   LEU   D O   1 
ATOM   8974  C  CB  . LEU   D 1 15  ? 15.742  -48.429 4.278   1.00 115.80 ? 84   LEU   D CB  1 
ATOM   8975  N  N   . PRO   D 1 16  ? 13.430  -48.632 6.822   1.00 134.79 ? 85   PRO   D N   1 
ATOM   8976  C  CA  . PRO   D 1 16  ? 12.892  -48.183 8.123   1.00 138.14 ? 85   PRO   D CA  1 
ATOM   8977  C  C   . PRO   D 1 16  ? 13.819  -47.340 8.991   1.00 138.38 ? 85   PRO   D C   1 
ATOM   8978  O  O   . PRO   D 1 16  ? 13.553  -46.152 9.195   1.00 139.13 ? 85   PRO   D O   1 
ATOM   8979  C  CB  . PRO   D 1 16  ? 12.551  -49.505 8.819   1.00 137.32 ? 85   PRO   D CB  1 
ATOM   8980  C  CG  . PRO   D 1 16  ? 12.182  -50.403 7.683   1.00 138.40 ? 85   PRO   D CG  1 
ATOM   8981  C  CD  . PRO   D 1 16  ? 13.106  -50.043 6.551   1.00 133.63 ? 85   PRO   D CD  1 
ATOM   8982  N  N   . GLN   D 1 17  ? 14.885  -47.926 9.528   1.00 136.13 ? 86   GLN   D N   1 
ATOM   8983  C  CA  . GLN   D 1 17  ? 15.759  -47.207 10.451  1.00 132.81 ? 86   GLN   D CA  1 
ATOM   8984  C  C   . GLN   D 1 17  ? 17.009  -46.710 9.721   1.00 142.28 ? 86   GLN   D C   1 
ATOM   8985  O  O   . GLN   D 1 17  ? 18.138  -47.115 10.003  1.00 140.73 ? 86   GLN   D O   1 
ATOM   8986  C  CB  . GLN   D 1 17  ? 16.112  -48.098 11.636  1.00 130.11 ? 86   GLN   D CB  1 
ATOM   8987  N  N   . VAL   D 1 18  ? 16.785  -45.792 8.771   1.00 149.10 ? 87   VAL   D N   1 
ATOM   8988  C  CA  . VAL   D 1 18  ? 17.869  -45.159 8.027   1.00 148.57 ? 87   VAL   D CA  1 
ATOM   8989  C  C   . VAL   D 1 18  ? 18.384  -43.958 8.805   1.00 148.62 ? 87   VAL   D C   1 
ATOM   8990  O  O   . VAL   D 1 18  ? 17.606  -43.189 9.379   1.00 151.47 ? 87   VAL   D O   1 
ATOM   8991  C  CB  . VAL   D 1 18  ? 17.400  -44.727 6.623   1.00 148.51 ? 87   VAL   D CB  1 
ATOM   8992  C  CG1 . VAL   D 1 18  ? 16.853  -45.905 5.838   1.00 149.39 ? 87   VAL   D CG1 1 
ATOM   8993  C  CG2 . VAL   D 1 18  ? 16.375  -43.601 6.715   1.00 148.15 ? 87   VAL   D CG2 1 
ATOM   8994  N  N   . MET   D 1 19  ? 19.705  -43.779 8.807   1.00 139.61 ? 88   MET   D N   1 
ATOM   8995  C  CA  . MET   D 1 19  ? 20.301  -42.616 9.453   1.00 138.78 ? 88   MET   D CA  1 
ATOM   8996  C  C   . MET   D 1 19  ? 21.661  -42.294 8.849   1.00 133.83 ? 88   MET   D C   1 
ATOM   8997  O  O   . MET   D 1 19  ? 22.613  -42.012 9.584   1.00 136.07 ? 88   MET   D O   1 
ATOM   8998  C  CB  . MET   D 1 19  ? 20.434  -42.851 10.961  1.00 142.42 ? 88   MET   D CB  1 
ATOM   8999  N  N   . MET   D 1 20  ? 21.766  -42.317 7.522   1.00 125.37 ? 89   MET   D N   1 
ATOM   9000  C  CA  . MET   D 1 20  ? 23.058  -42.235 6.867   1.00 120.10 ? 89   MET   D CA  1 
ATOM   9001  C  C   . MET   D 1 20  ? 23.038  -41.193 5.762   1.00 116.00 ? 89   MET   D C   1 
ATOM   9002  O  O   . MET   D 1 20  ? 21.988  -40.828 5.227   1.00 117.20 ? 89   MET   D O   1 
ATOM   9003  C  CB  . MET   D 1 20  ? 23.479  -43.605 6.298   1.00 121.09 ? 89   MET   D CB  1 
ATOM   9004  C  CG  . MET   D 1 20  ? 24.314  -43.550 5.012   1.00 121.17 ? 89   MET   D CG  1 
ATOM   9005  S  SD  . MET   D 1 20  ? 24.861  -45.193 4.459   1.00 134.74 ? 89   MET   D SD  1 
ATOM   9006  C  CE  . MET   D 1 20  ? 26.616  -45.202 4.874   1.00 125.73 ? 89   MET   D CE  1 
ATOM   9007  N  N   . ILE   D 1 21  ? 24.228  -40.696 5.446   1.00 109.13 ? 90   ILE   D N   1 
ATOM   9008  C  CA  . ILE   D 1 21  ? 24.472  -39.968 4.211   1.00 104.01 ? 90   ILE   D CA  1 
ATOM   9009  C  C   . ILE   D 1 21  ? 24.973  -41.007 3.211   1.00 99.68  ? 90   ILE   D C   1 
ATOM   9010  O  O   . ILE   D 1 21  ? 26.098  -41.488 3.298   1.00 99.56  ? 90   ILE   D O   1 
ATOM   9011  C  CB  . ILE   D 1 21  ? 25.478  -38.830 4.405   1.00 101.87 ? 90   ILE   D CB  1 
ATOM   9012  C  CG1 . ILE   D 1 21  ? 24.809  -37.592 5.008   1.00 94.86  ? 90   ILE   D CG1 1 
ATOM   9013  C  CG2 . ILE   D 1 21  ? 26.167  -38.488 3.085   1.00 96.77  ? 90   ILE   D CG2 1 
ATOM   9014  C  CD1 . ILE   D 1 21  ? 24.132  -37.820 6.326   1.00 101.01 ? 90   ILE   D CD1 1 
ATOM   9015  N  N   . LEU   D 1 22  ? 24.137  -41.388 2.281   1.00 97.39  ? 91   LEU   D N   1 
ATOM   9016  C  CA  . LEU   D 1 22  ? 24.516  -42.392 1.309   1.00 97.19  ? 91   LEU   D CA  1 
ATOM   9017  C  C   . LEU   D 1 22  ? 24.902  -41.707 -0.001  1.00 93.70  ? 91   LEU   D C   1 
ATOM   9018  O  O   . LEU   D 1 22  ? 24.075  -41.034 -0.623  1.00 94.71  ? 91   LEU   D O   1 
ATOM   9019  C  CB  . LEU   D 1 22  ? 23.366  -43.370 1.120   1.00 94.78  ? 91   LEU   D CB  1 
ATOM   9020  C  CG  . LEU   D 1 22  ? 23.626  -44.203 -0.105  1.00 91.98  ? 91   LEU   D CG  1 
ATOM   9021  C  CD1 . LEU   D 1 22  ? 24.855  -45.049 0.167   1.00 91.03  ? 91   LEU   D CD1 1 
ATOM   9022  C  CD2 . LEU   D 1 22  ? 22.389  -45.009 -0.419  1.00 90.24  ? 91   LEU   D CD2 1 
ATOM   9023  N  N   . ILE   D 1 23  ? 26.155  -41.847 -0.409  1.00 89.77  ? 92   ILE   D N   1 
ATOM   9024  C  CA  . ILE   D 1 23  ? 26.555  -41.215 -1.661  1.00 93.53  ? 92   ILE   D CA  1 
ATOM   9025  C  C   . ILE   D 1 23  ? 26.299  -42.191 -2.811  1.00 95.89  ? 92   ILE   D C   1 
ATOM   9026  O  O   . ILE   D 1 23  ? 26.453  -43.413 -2.636  1.00 87.95  ? 92   ILE   D O   1 
ATOM   9027  C  CB  . ILE   D 1 23  ? 28.022  -40.761 -1.614  1.00 90.54  ? 92   ILE   D CB  1 
ATOM   9028  C  CG1 . ILE   D 1 23  ? 28.310  -40.050 -0.302  1.00 88.85  ? 92   ILE   D CG1 1 
ATOM   9029  C  CG2 . ILE   D 1 23  ? 28.353  -39.831 -2.793  1.00 87.10  ? 92   ILE   D CG2 1 
ATOM   9030  C  CD1 . ILE   D 1 23  ? 29.747  -39.540 -0.215  1.00 86.69  ? 92   ILE   D CD1 1 
ATOM   9031  N  N   . PRO   D 1 24  ? 25.906  -41.706 -3.994  1.00 94.83  ? 93   PRO   D N   1 
ATOM   9032  C  CA  . PRO   D 1 24  ? 25.656  -42.622 -5.109  1.00 87.35  ? 93   PRO   D CA  1 
ATOM   9033  C  C   . PRO   D 1 24  ? 26.911  -43.410 -5.432  1.00 90.64  ? 93   PRO   D C   1 
ATOM   9034  O  O   . PRO   D 1 24  ? 28.005  -42.846 -5.518  1.00 91.48  ? 93   PRO   D O   1 
ATOM   9035  C  CB  . PRO   D 1 24  ? 25.254  -41.687 -6.257  1.00 81.56  ? 93   PRO   D CB  1 
ATOM   9036  C  CG  . PRO   D 1 24  ? 24.919  -40.412 -5.620  1.00 85.61  ? 93   PRO   D CG  1 
ATOM   9037  C  CD  . PRO   D 1 24  ? 25.773  -40.300 -4.413  1.00 89.15  ? 93   PRO   D CD  1 
ATOM   9038  N  N   . GLY   D 1 25  ? 26.736  -44.726 -5.620  1.00 92.17  ? 94   GLY   D N   1 
ATOM   9039  C  CA  . GLY   D 1 25  ? 27.818  -45.647 -5.939  1.00 89.62  ? 94   GLY   D CA  1 
ATOM   9040  C  C   . GLY   D 1 25  ? 28.396  -46.350 -4.722  1.00 89.88  ? 94   GLY   D C   1 
ATOM   9041  O  O   . GLY   D 1 25  ? 28.803  -47.509 -4.811  1.00 88.96  ? 94   GLY   D O   1 
ATOM   9042  N  N   . GLN   D 1 26  ? 28.481  -45.637 -3.594  1.00 91.60  ? 95   GLN   D N   1 
ATOM   9043  C  CA  . GLN   D 1 26  ? 28.758  -46.270 -2.316  1.00 88.29  ? 95   GLN   D CA  1 
ATOM   9044  C  C   . GLN   D 1 26  ? 27.809  -47.434 -2.105  1.00 90.49  ? 95   GLN   D C   1 
ATOM   9045  O  O   . GLN   D 1 26  ? 26.637  -47.348 -2.479  1.00 88.53  ? 95   GLN   D O   1 
ATOM   9046  C  CB  . GLN   D 1 26  ? 28.511  -45.303 -1.153  1.00 93.66  ? 95   GLN   D CB  1 
ATOM   9047  C  CG  . GLN   D 1 26  ? 29.736  -44.555 -0.604  1.00 96.40  ? 95   GLN   D CG  1 
ATOM   9048  C  CD  . GLN   D 1 26  ? 29.428  -43.793 0.703   1.00 96.32  ? 95   GLN   D CD  1 
ATOM   9049  O  OE1 . GLN   D 1 26  ? 28.258  -43.534 1.023   1.00 96.31  ? 95   GLN   D OE1 1 
ATOM   9050  N  NE2 . GLN   D 1 26  ? 30.476  -43.445 1.461   1.00 91.03  ? 95   GLN   D NE2 1 
ATOM   9051  N  N   . THR   D 1 27  ? 28.286  -48.514 -1.496  1.00 94.79  ? 96   THR   D N   1 
ATOM   9052  C  CA  . THR   D 1 27  ? 27.452  -49.685 -1.288  1.00 95.32  ? 96   THR   D CA  1 
ATOM   9053  C  C   . THR   D 1 27  ? 26.977  -49.854 0.143   1.00 92.25  ? 96   THR   D C   1 
ATOM   9054  O  O   . THR   D 1 27  ? 27.782  -49.855 1.089   1.00 92.44  ? 96   THR   D O   1 
ATOM   9055  C  CB  . THR   D 1 27  ? 28.236  -50.904 -1.760  1.00 99.90  ? 96   THR   D CB  1 
ATOM   9056  O  OG1 . THR   D 1 27  ? 28.880  -50.559 -2.991  1.00 102.60 ? 96   THR   D OG1 1 
ATOM   9057  C  CG2 . THR   D 1 27  ? 27.283  -52.087 -1.980  1.00 96.49  ? 96   THR   D CG2 1 
ATOM   9058  N  N   . LEU   D 1 28  ? 25.675  -49.972 0.279   1.00 91.97  ? 97   LEU   D N   1 
ATOM   9059  C  CA  . LEU   D 1 28  ? 25.033  -50.074 1.570   1.00 93.33  ? 97   LEU   D CA  1 
ATOM   9060  C  C   . LEU   D 1 28  ? 24.796  -51.536 1.879   1.00 97.31  ? 97   LEU   D C   1 
ATOM   9061  O  O   . LEU   D 1 28  ? 23.933  -52.153 1.261   1.00 95.88  ? 97   LEU   D O   1 
ATOM   9062  C  CB  . LEU   D 1 28  ? 23.723  -49.296 1.565   1.00 92.83  ? 97   LEU   D CB  1 
ATOM   9063  C  CG  . LEU   D 1 28  ? 22.822  -49.479 2.777   1.00 96.53  ? 97   LEU   D CG  1 
ATOM   9064  C  CD1 . LEU   D 1 28  ? 23.535  -48.909 3.984   1.00 100.19 ? 97   LEU   D CD1 1 
ATOM   9065  C  CD2 . LEU   D 1 28  ? 21.495  -48.791 2.532   1.00 97.23  ? 97   LEU   D CD2 1 
ATOM   9066  N  N   . PRO   D 1 29  ? 25.591  -52.148 2.753   1.00 99.52  ? 98   PRO   D N   1 
ATOM   9067  C  CA  . PRO   D 1 29  ? 25.309  -53.531 3.159   1.00 90.61  ? 98   PRO   D CA  1 
ATOM   9068  C  C   . PRO   D 1 29  ? 24.297  -53.576 4.291   1.00 94.93  ? 98   PRO   D C   1 
ATOM   9069  O  O   . PRO   D 1 29  ? 24.358  -52.775 5.224   1.00 98.38  ? 98   PRO   D O   1 
ATOM   9070  C  CB  . PRO   D 1 29  ? 26.677  -54.057 3.612   1.00 91.44  ? 98   PRO   D CB  1 
ATOM   9071  C  CG  . PRO   D 1 29  ? 27.684  -52.999 3.193   1.00 96.24  ? 98   PRO   D CG  1 
ATOM   9072  C  CD  . PRO   D 1 29  ? 26.919  -51.719 3.212   1.00 100.30 ? 98   PRO   D CD  1 
ATOM   9073  N  N   . LEU   D 1 30  ? 23.377  -54.532 4.215   1.00 100.51 ? 99   LEU   D N   1 
ATOM   9074  C  CA  . LEU   D 1 30  ? 22.352  -54.735 5.235   1.00 104.42 ? 99   LEU   D CA  1 
ATOM   9075  C  C   . LEU   D 1 30  ? 22.276  -56.208 5.651   1.00 108.58 ? 99   LEU   D C   1 
ATOM   9076  O  O   . LEU   D 1 30  ? 22.462  -57.107 4.825   1.00 105.13 ? 99   LEU   D O   1 
ATOM   9077  C  CB  . LEU   D 1 30  ? 20.970  -54.261 4.731   1.00 100.59 ? 99   LEU   D CB  1 
ATOM   9078  C  CG  . LEU   D 1 30  ? 20.844  -52.861 4.122   1.00 96.61  ? 99   LEU   D CG  1 
ATOM   9079  C  CD1 . LEU   D 1 30  ? 19.389  -52.484 3.929   1.00 99.94  ? 99   LEU   D CD1 1 
ATOM   9080  C  CD2 . LEU   D 1 30  ? 21.520  -51.819 4.974   1.00 99.56  ? 99   LEU   D CD2 1 
ATOM   9081  N  N   . GLN   D 1 31  ? 22.043  -56.448 6.955   1.00 115.86 ? 100  GLN   D N   1 
ATOM   9082  C  CA  . GLN   D 1 31  ? 21.636  -57.754 7.495   1.00 117.01 ? 100  GLN   D CA  1 
ATOM   9083  C  C   . GLN   D 1 31  ? 20.229  -57.556 8.045   1.00 118.56 ? 100  GLN   D C   1 
ATOM   9084  O  O   . GLN   D 1 31  ? 20.050  -57.119 9.185   1.00 122.00 ? 100  GLN   D O   1 
ATOM   9085  C  CB  . GLN   D 1 31  ? 22.592  -58.266 8.570   1.00 111.88 ? 100  GLN   D CB  1 
ATOM   9086  N  N   . LEU   D 1 32  ? 19.234  -57.827 7.217   1.00 120.07 ? 101  LEU   D N   1 
ATOM   9087  C  CA  . LEU   D 1 32  ? 17.857  -57.681 7.634   1.00 121.17 ? 101  LEU   D CA  1 
ATOM   9088  C  C   . LEU   D 1 32  ? 17.492  -58.833 8.550   1.00 129.69 ? 101  LEU   D C   1 
ATOM   9089  O  O   . LEU   D 1 32  ? 17.974  -59.953 8.380   1.00 138.33 ? 101  LEU   D O   1 
ATOM   9090  C  CB  . LEU   D 1 32  ? 16.923  -57.645 6.421   1.00 125.24 ? 101  LEU   D CB  1 
ATOM   9091  C  CG  . LEU   D 1 32  ? 16.742  -56.307 5.698   1.00 122.70 ? 101  LEU   D CG  1 
ATOM   9092  C  CD1 . LEU   D 1 32  ? 18.105  -55.693 5.433   1.00 118.71 ? 101  LEU   D CD1 1 
ATOM   9093  C  CD2 . LEU   D 1 32  ? 15.967  -56.472 4.391   1.00 122.84 ? 101  LEU   D CD2 1 
ATOM   9094  N  N   . PHE   D 1 33  ? 16.654  -58.550 9.533   1.00 136.02 ? 102  PHE   D N   1 
ATOM   9095  C  CA  . PHE   D 1 33  ? 16.175  -59.585 10.441  1.00 139.12 ? 102  PHE   D CA  1 
ATOM   9096  C  C   . PHE   D 1 33  ? 14.670  -59.559 10.651  1.00 144.25 ? 102  PHE   D C   1 
ATOM   9097  O  O   . PHE   D 1 33  ? 14.103  -60.591 11.021  1.00 149.26 ? 102  PHE   D O   1 
ATOM   9098  C  CB  . PHE   D 1 33  ? 16.857  -59.445 11.805  1.00 139.15 ? 102  PHE   D CB  1 
ATOM   9099  C  CG  . PHE   D 1 33  ? 16.110  -58.542 12.753  1.00 146.12 ? 102  PHE   D CG  1 
ATOM   9100  C  CD1 . PHE   D 1 33  ? 15.048  -59.031 13.508  1.00 150.05 ? 102  PHE   D CD1 1 
ATOM   9101  C  CD2 . PHE   D 1 33  ? 16.452  -57.197 12.867  1.00 145.29 ? 102  PHE   D CD2 1 
ATOM   9102  C  CE1 . PHE   D 1 33  ? 14.358  -58.193 14.391  1.00 153.26 ? 102  PHE   D CE1 1 
ATOM   9103  C  CE2 . PHE   D 1 33  ? 15.753  -56.342 13.742  1.00 143.17 ? 102  PHE   D CE2 1 
ATOM   9104  C  CZ  . PHE   D 1 33  ? 14.718  -56.831 14.503  1.00 147.08 ? 102  PHE   D CZ  1 
ATOM   9105  N  N   . HIS   D 1 34  ? 14.008  -58.427 10.451  1.00 146.03 ? 103  HIS   D N   1 
ATOM   9106  C  CA  . HIS   D 1 34  ? 12.617  -58.243 10.869  1.00 151.24 ? 103  HIS   D CA  1 
ATOM   9107  C  C   . HIS   D 1 34  ? 11.682  -58.504 9.691   1.00 154.83 ? 103  HIS   D C   1 
ATOM   9108  O  O   . HIS   D 1 34  ? 11.989  -58.065 8.576   1.00 150.29 ? 103  HIS   D O   1 
ATOM   9109  C  CB  . HIS   D 1 34  ? 12.424  -56.815 11.390  1.00 151.36 ? 103  HIS   D CB  1 
ATOM   9110  C  CG  . HIS   D 1 34  ? 11.010  -56.478 11.774  1.00 156.73 ? 103  HIS   D CG  1 
ATOM   9111  N  ND1 . HIS   D 1 34  ? 9.903   -56.911 11.070  1.00 157.68 ? 103  HIS   D ND1 1 
ATOM   9112  C  CD2 . HIS   D 1 34  ? 10.530  -55.719 12.788  1.00 157.95 ? 103  HIS   D CD2 1 
ATOM   9113  C  CE1 . HIS   D 1 34  ? 8.806   -56.444 11.639  1.00 157.29 ? 103  HIS   D CE1 1 
ATOM   9114  N  NE2 . HIS   D 1 34  ? 9.159   -55.718 12.685  1.00 159.77 ? 103  HIS   D NE2 1 
ATOM   9115  N  N   . PRO   D 1 35  ? 10.545  -59.210 9.925   1.00 173.08 ? 104  PRO   D N   1 
ATOM   9116  C  CA  . PRO   D 1 35  ? 9.647   -59.560 8.814   1.00 173.90 ? 104  PRO   D CA  1 
ATOM   9117  C  C   . PRO   D 1 35  ? 9.015   -58.397 8.062   1.00 172.84 ? 104  PRO   D C   1 
ATOM   9118  O  O   . PRO   D 1 35  ? 9.071   -58.370 6.818   1.00 172.65 ? 104  PRO   D O   1 
ATOM   9119  C  CB  . PRO   D 1 35  ? 8.575   -60.401 9.484   1.00 174.84 ? 104  PRO   D CB  1 
ATOM   9120  C  CG  . PRO   D 1 35  ? 9.295   -61.021 10.652  1.00 177.72 ? 104  PRO   D CG  1 
ATOM   9121  C  CD  . PRO   D 1 35  ? 10.263  -59.927 11.126  1.00 174.34 ? 104  PRO   D CD  1 
ATOM   9122  N  N   . GLN   D 1 36  ? 8.400   -57.433 8.754   1.00 157.45 ? 105  GLN   D N   1 
ATOM   9123  C  CA  . GLN   D 1 36  ? 7.760   -56.291 8.091   1.00 150.89 ? 105  GLN   D CA  1 
ATOM   9124  C  C   . GLN   D 1 36  ? 8.704   -55.709 7.052   1.00 149.48 ? 105  GLN   D C   1 
ATOM   9125  O  O   . GLN   D 1 36  ? 8.280   -55.298 5.964   1.00 146.45 ? 105  GLN   D O   1 
ATOM   9126  C  CB  . GLN   D 1 36  ? 7.360   -55.224 9.112   1.00 146.04 ? 105  GLN   D CB  1 
ATOM   9127  N  N   . GLU   D 1 37  ? 9.996   -55.680 7.390   1.00 149.51 ? 106  GLU   D N   1 
ATOM   9128  C  CA  . GLU   D 1 37  ? 11.011  -55.183 6.465   1.00 143.21 ? 106  GLU   D CA  1 
ATOM   9129  C  C   . GLU   D 1 37  ? 11.212  -56.149 5.302   1.00 139.88 ? 106  GLU   D C   1 
ATOM   9130  O  O   . GLU   D 1 37  ? 10.966  -55.800 4.141   1.00 136.96 ? 106  GLU   D O   1 
ATOM   9131  C  CB  . GLU   D 1 37  ? 12.325  -54.947 7.218   1.00 139.20 ? 106  GLU   D CB  1 
ATOM   9132  N  N   . VAL   D 1 38  ? 11.656  -57.377 5.602   1.00 140.95 ? 107  VAL   D N   1 
ATOM   9133  C  CA  . VAL   D 1 38  ? 11.891  -58.382 4.566   1.00 137.69 ? 107  VAL   D CA  1 
ATOM   9134  C  C   . VAL   D 1 38  ? 10.679  -58.540 3.657   1.00 135.60 ? 107  VAL   D C   1 
ATOM   9135  O  O   . VAL   D 1 38  ? 10.821  -58.854 2.469   1.00 133.24 ? 107  VAL   D O   1 
ATOM   9136  C  CB  . VAL   D 1 38  ? 12.288  -59.728 5.204   1.00 132.92 ? 107  VAL   D CB  1 
ATOM   9137  C  CG1 . VAL   D 1 38  ? 11.352  -60.073 6.345   1.00 145.13 ? 107  VAL   D CG1 1 
ATOM   9138  C  CG2 . VAL   D 1 38  ? 12.264  -60.824 4.156   1.00 127.49 ? 107  VAL   D CG2 1 
ATOM   9139  N  N   . SER   D 1 39  ? 9.473   -58.333 4.188   1.00 137.59 ? 108  SER   D N   1 
ATOM   9140  C  CA  . SER   D 1 39  ? 8.288   -58.358 3.337   1.00 135.43 ? 108  SER   D CA  1 
ATOM   9141  C  C   . SER   D 1 39  ? 8.394   -57.298 2.253   1.00 135.04 ? 108  SER   D C   1 
ATOM   9142  O  O   . SER   D 1 39  ? 8.130   -57.562 1.075   1.00 133.12 ? 108  SER   D O   1 
ATOM   9143  C  CB  . SER   D 1 39  ? 7.027   -58.139 4.173   1.00 141.98 ? 108  SER   D CB  1 
ATOM   9144  O  OG  . SER   D 1 39  ? 7.142   -58.719 5.460   1.00 141.32 ? 108  SER   D OG  1 
ATOM   9145  N  N   . MET   D 1 40  ? 8.789   -56.083 2.642   1.00 143.16 ? 109  MET   D N   1 
ATOM   9146  C  CA  . MET   D 1 40  ? 8.976   -55.011 1.670   1.00 143.84 ? 109  MET   D CA  1 
ATOM   9147  C  C   . MET   D 1 40  ? 10.099  -55.348 0.693   1.00 141.82 ? 109  MET   D C   1 
ATOM   9148  O  O   . MET   D 1 40  ? 9.971   -55.125 -0.520  1.00 139.48 ? 109  MET   D O   1 
ATOM   9149  C  CB  . MET   D 1 40  ? 9.268   -53.696 2.399   1.00 145.14 ? 109  MET   D CB  1 
ATOM   9150  C  CG  . MET   D 1 40  ? 9.298   -52.476 1.480   1.00 148.91 ? 109  MET   D CG  1 
ATOM   9151  S  SD  . MET   D 1 40  ? 10.230  -51.056 2.110   1.00 155.78 ? 109  MET   D SD  1 
ATOM   9152  C  CE  . MET   D 1 40  ? 11.892  -51.720 2.212   1.00 142.64 ? 109  MET   D CE  1 
ATOM   9153  N  N   . VAL   D 1 41  ? 11.202  -55.904 1.207   1.00 137.43 ? 110  VAL   D N   1 
ATOM   9154  C  CA  . VAL   D 1 41  ? 12.363  -56.232 0.378   1.00 130.21 ? 110  VAL   D CA  1 
ATOM   9155  C  C   . VAL   D 1 41  ? 11.974  -57.224 -0.713  1.00 129.77 ? 110  VAL   D C   1 
ATOM   9156  O  O   . VAL   D 1 41  ? 12.157  -56.964 -1.911  1.00 125.83 ? 110  VAL   D O   1 
ATOM   9157  C  CB  . VAL   D 1 41  ? 13.501  -56.781 1.256   1.00 128.46 ? 110  VAL   D CB  1 
ATOM   9158  C  CG1 . VAL   D 1 41  ? 14.807  -56.826 0.482   1.00 123.62 ? 110  VAL   D CG1 1 
ATOM   9159  C  CG2 . VAL   D 1 41  ? 13.638  -55.946 2.526   1.00 127.02 ? 110  VAL   D CG2 1 
ATOM   9160  N  N   . ARG   D 1 42  ? 11.451  -58.388 -0.304  1.00 132.80 ? 111  ARG   D N   1 
ATOM   9161  C  CA  . ARG   D 1 42  ? 10.962  -59.376 -1.260  1.00 128.71 ? 111  ARG   D CA  1 
ATOM   9162  C  C   . ARG   D 1 42  ? 10.087  -58.697 -2.303  1.00 126.51 ? 111  ARG   D C   1 
ATOM   9163  O  O   . ARG   D 1 42  ? 10.424  -58.660 -3.493  1.00 126.12 ? 111  ARG   D O   1 
ATOM   9164  C  CB  . ARG   D 1 42  ? 10.203  -60.493 -0.528  1.00 117.31 ? 111  ARG   D CB  1 
ATOM   9165  N  N   . ASN   D 1 43  ? 8.989   -58.090 -1.853  1.00 126.55 ? 112  ASN   D N   1 
ATOM   9166  C  CA  . ASN   D 1 43  ? 8.117   -57.357 -2.763  1.00 126.36 ? 112  ASN   D CA  1 
ATOM   9167  C  C   . ASN   D 1 43  ? 8.908   -56.461 -3.712  1.00 127.91 ? 112  ASN   D C   1 
ATOM   9168  O  O   . ASN   D 1 43  ? 8.534   -56.313 -4.886  1.00 129.03 ? 112  ASN   D O   1 
ATOM   9169  C  CB  . ASN   D 1 43  ? 7.115   -56.532 -1.955  1.00 126.27 ? 112  ASN   D CB  1 
ATOM   9170  C  CG  . ASN   D 1 43  ? 6.076   -55.847 -2.831  1.00 128.34 ? 112  ASN   D CG  1 
ATOM   9171  O  OD1 . ASN   D 1 43  ? 6.299   -55.611 -4.023  1.00 129.19 ? 112  ASN   D OD1 1 
ATOM   9172  N  ND2 . ASN   D 1 43  ? 4.933   -55.516 -2.238  1.00 129.35 ? 112  ASN   D ND2 1 
ATOM   9173  N  N   . LEU   D 1 44  ? 10.010  -55.870 -3.230  1.00 128.26 ? 113  LEU   D N   1 
ATOM   9174  C  CA  . LEU   D 1 44  ? 10.750  -54.870 -4.000  1.00 126.18 ? 113  LEU   D CA  1 
ATOM   9175  C  C   . LEU   D 1 44  ? 11.558  -55.496 -5.132  1.00 128.34 ? 113  LEU   D C   1 
ATOM   9176  O  O   . LEU   D 1 44  ? 11.555  -54.980 -6.259  1.00 128.19 ? 113  LEU   D O   1 
ATOM   9177  C  CB  . LEU   D 1 44  ? 11.667  -54.065 -3.075  1.00 123.51 ? 113  LEU   D CB  1 
ATOM   9178  C  CG  . LEU   D 1 44  ? 11.318  -52.593 -2.823  1.00 117.24 ? 113  LEU   D CG  1 
ATOM   9179  C  CD1 . LEU   D 1 44  ? 12.393  -51.879 -2.001  1.00 112.79 ? 113  LEU   D CD1 1 
ATOM   9180  C  CD2 . LEU   D 1 44  ? 11.063  -51.856 -4.133  1.00 117.15 ? 113  LEU   D CD2 1 
ATOM   9181  N  N   . ILE   D 1 45  ? 12.311  -56.552 -4.821  1.00 124.46 ? 114  ILE   D N   1 
ATOM   9182  C  CA  . ILE   D 1 45  ? 13.204  -57.142 -5.864  1.00 121.19 ? 114  ILE   D CA  1 
ATOM   9183  C  C   . ILE   D 1 45  ? 12.340  -57.505 -7.077  1.00 121.37 ? 114  ILE   D C   1 
ATOM   9184  O  O   . ILE   D 1 45  ? 12.892  -57.634 -8.185  1.00 120.76 ? 114  ILE   D O   1 
ATOM   9185  C  CB  . ILE   D 1 45  ? 13.982  -58.356 -5.331  1.00 114.33 ? 114  ILE   D CB  1 
ATOM   9186  C  CG1 . ILE   D 1 45  ? 14.970  -57.960 -4.246  1.00 114.77 ? 114  ILE   D CG1 1 
ATOM   9187  C  CG2 . ILE   D 1 45  ? 14.683  -59.095 -6.471  1.00 116.33 ? 114  ILE   D CG2 1 
ATOM   9188  C  CD1 . ILE   D 1 45  ? 15.570  -59.139 -3.505  1.00 109.53 ? 114  ILE   D CD1 1 
ATOM   9189  N  N   . GLN   D 1 46  ? 11.032  -57.631 -6.867  1.00 125.76 ? 115  GLN   D N   1 
ATOM   9190  C  CA  . GLN   D 1 46  ? 10.113  -57.996 -7.972  1.00 124.32 ? 115  GLN   D CA  1 
ATOM   9191  C  C   . GLN   D 1 46  ? 9.652   -56.724 -8.691  1.00 132.92 ? 115  GLN   D C   1 
ATOM   9192  O  O   . GLN   D 1 46  ? 8.716   -56.819 -9.509  1.00 130.81 ? 115  GLN   D O   1 
ATOM   9193  C  CB  . GLN   D 1 46  ? 8.905   -58.737 -7.407  1.00 125.34 ? 115  GLN   D CB  1 
ATOM   9194  N  N   . LYS   D 1 47  ? 10.285  -55.587 -8.396  1.00 138.39 ? 116  LYS   D N   1 
ATOM   9195  C  CA  . LYS   D 1 47  ? 9.860   -54.299 -9.000  1.00 138.93 ? 116  LYS   D CA  1 
ATOM   9196  C  C   . LYS   D 1 47  ? 11.074  -53.463 -9.422  1.00 139.25 ? 116  LYS   D C   1 
ATOM   9197  O  O   . LYS   D 1 47  ? 11.896  -53.972 -10.208 1.00 141.52 ? 116  LYS   D O   1 
ATOM   9198  C  CB  . LYS   D 1 47  ? 8.978   -53.546 -8.001  1.00 138.24 ? 116  LYS   D CB  1 
ATOM   9199  N  N   . ASP   D 1 48  ? 11.180  -52.235 -8.912  1.00 141.97 ? 117  ASP   D N   1 
ATOM   9200  C  CA  . ASP   D 1 48  ? 12.294  -51.328 -9.288  1.00 139.26 ? 117  ASP   D CA  1 
ATOM   9201  C  C   . ASP   D 1 48  ? 13.502  -51.659 -8.418  1.00 143.07 ? 117  ASP   D C   1 
ATOM   9202  O  O   . ASP   D 1 48  ? 14.563  -51.042 -8.633  1.00 142.97 ? 117  ASP   D O   1 
ATOM   9203  C  CB  . ASP   D 1 48  ? 11.920  -49.877 -9.068  1.00 136.87 ? 117  ASP   D CB  1 
ATOM   9204  C  CG  . ASP   D 1 48  ? 11.165  -49.606 -7.775  1.00 144.30 ? 117  ASP   D CG  1 
ATOM   9205  O  OD1 . ASP   D 1 48  ? 11.780  -49.739 -6.698  1.00 148.98 ? 117  ASP   D OD1 1 
ATOM   9206  O  OD2 . ASP   D 1 48  ? 9.965   -49.275 -7.856  1.00 150.74 ? 117  ASP   D OD2 1 
ATOM   9207  N  N   . ARG   D 1 49  ? 13.330  -52.564 -7.454  1.00 135.25 ? 118  ARG   D N   1 
ATOM   9208  C  CA  . ARG   D 1 49  ? 14.436  -52.940 -6.538  1.00 122.83 ? 118  ARG   D CA  1 
ATOM   9209  C  C   . ARG   D 1 49  ? 15.089  -51.662 -6.000  1.00 119.03 ? 118  ARG   D C   1 
ATOM   9210  O  O   . ARG   D 1 49  ? 16.324  -51.610 -5.975  1.00 115.78 ? 118  ARG   D O   1 
ATOM   9211  C  CB  . ARG   D 1 49  ? 15.462  -53.819 -7.261  1.00 116.82 ? 118  ARG   D CB  1 
ATOM   9212  N  N   . THR   D 1 50  ? 14.285  -50.686 -5.580  1.00 119.81 ? 119  THR   D N   1 
ATOM   9213  C  CA  . THR   D 1 50  ? 14.820  -49.419 -5.070  1.00 111.56 ? 119  THR   D CA  1 
ATOM   9214  C  C   . THR   D 1 50  ? 14.055  -48.952 -3.834  1.00 112.25 ? 119  THR   D C   1 
ATOM   9215  O  O   . THR   D 1 50  ? 12.822  -48.870 -3.854  1.00 115.74 ? 119  THR   D O   1 
ATOM   9216  C  CB  . THR   D 1 50  ? 14.762  -48.304 -6.138  1.00 110.92 ? 119  THR   D CB  1 
ATOM   9217  O  OG1 . THR   D 1 50  ? 15.405  -48.735 -7.342  1.00 113.72 ? 119  THR   D OG1 1 
ATOM   9218  C  CG2 . THR   D 1 50  ? 15.460  -47.045 -5.640  1.00 100.66 ? 119  THR   D CG2 1 
ATOM   9219  N  N   . PHE   D 1 51  ? 14.783  -48.612 -2.773  1.00 105.17 ? 120  PHE   D N   1 
ATOM   9220  C  CA  . PHE   D 1 51  ? 14.210  -47.909 -1.629  1.00 102.74 ? 120  PHE   D CA  1 
ATOM   9221  C  C   . PHE   D 1 51  ? 14.888  -46.547 -1.488  1.00 101.67 ? 120  PHE   D C   1 
ATOM   9222  O  O   . PHE   D 1 51  ? 15.646  -46.111 -2.370  1.00 99.55  ? 120  PHE   D O   1 
ATOM   9223  C  CB  . PHE   D 1 51  ? 14.353  -48.740 -0.359  1.00 101.29 ? 120  PHE   D CB  1 
ATOM   9224  C  CG  . PHE   D 1 51  ? 15.745  -49.185 -0.107  1.00 97.97  ? 120  PHE   D CG  1 
ATOM   9225  C  CD1 . PHE   D 1 51  ? 16.683  -48.307 0.396   1.00 100.54 ? 120  PHE   D CD1 1 
ATOM   9226  C  CD2 . PHE   D 1 51  ? 16.133  -50.472 -0.405  1.00 95.80  ? 120  PHE   D CD2 1 
ATOM   9227  C  CE1 . PHE   D 1 51  ? 17.980  -48.722 0.615   1.00 100.87 ? 120  PHE   D CE1 1 
ATOM   9228  C  CE2 . PHE   D 1 51  ? 17.425  -50.890 -0.185  1.00 91.20  ? 120  PHE   D CE2 1 
ATOM   9229  C  CZ  . PHE   D 1 51  ? 18.345  -50.022 0.328   1.00 92.16  ? 120  PHE   D CZ  1 
ATOM   9230  N  N   . ALA   D 1 52  ? 14.623  -45.876 -0.362  1.00 106.51 ? 121  ALA   D N   1 
ATOM   9231  C  CA  . ALA   D 1 52  ? 15.171  -44.553 -0.079  1.00 102.28 ? 121  ALA   D CA  1 
ATOM   9232  C  C   . ALA   D 1 52  ? 15.981  -44.588 1.212   1.00 104.56 ? 121  ALA   D C   1 
ATOM   9233  O  O   . ALA   D 1 52  ? 15.543  -45.160 2.220   1.00 106.13 ? 121  ALA   D O   1 
ATOM   9234  C  CB  . ALA   D 1 52  ? 14.056  -43.510 0.013   1.00 93.24  ? 121  ALA   D CB  1 
ATOM   9235  N  N   . VAL   D 1 53  ? 17.173  -43.998 1.168   1.00 100.63 ? 122  VAL   D N   1 
ATOM   9236  C  CA  . VAL   D 1 53  ? 18.003  -43.815 2.350   1.00 108.10 ? 122  VAL   D CA  1 
ATOM   9237  C  C   . VAL   D 1 53  ? 17.940  -42.351 2.739   1.00 110.72 ? 122  VAL   D C   1 
ATOM   9238  O  O   . VAL   D 1 53  ? 18.140  -41.459 1.902   1.00 101.79 ? 122  VAL   D O   1 
ATOM   9239  C  CB  . VAL   D 1 53  ? 19.457  -44.253 2.123   1.00 107.84 ? 122  VAL   D CB  1 
ATOM   9240  C  CG1 . VAL   D 1 53  ? 20.202  -44.261 3.469   1.00 108.71 ? 122  VAL   D CG1 1 
ATOM   9241  C  CG2 . VAL   D 1 53  ? 19.491  -45.605 1.466   1.00 99.28  ? 122  VAL   D CG2 1 
ATOM   9242  N  N   . LEU   D 1 54  ? 17.681  -42.106 4.010   1.00 118.28 ? 123  LEU   D N   1 
ATOM   9243  C  CA  . LEU   D 1 54  ? 17.400  -40.768 4.491   1.00 115.03 ? 123  LEU   D CA  1 
ATOM   9244  C  C   . LEU   D 1 54  ? 18.539  -40.282 5.374   1.00 119.29 ? 123  LEU   D C   1 
ATOM   9245  O  O   . LEU   D 1 54  ? 19.042  -41.027 6.226   1.00 119.15 ? 123  LEU   D O   1 
ATOM   9246  C  CB  . LEU   D 1 54  ? 16.074  -40.758 5.246   1.00 112.91 ? 123  LEU   D CB  1 
ATOM   9247  C  CG  . LEU   D 1 54  ? 14.865  -40.805 4.316   1.00 109.28 ? 123  LEU   D CG  1 
ATOM   9248  C  CD1 . LEU   D 1 54  ? 13.578  -40.818 5.112   1.00 107.21 ? 123  LEU   D CD1 1 
ATOM   9249  C  CD2 . LEU   D 1 54  ? 14.900  -39.617 3.369   1.00 106.60 ? 123  LEU   D CD2 1 
ATOM   9250  N  N   . ALA   D 1 55  ? 18.962  -39.043 5.132   1.00 119.32 ? 124  ALA   D N   1 
ATOM   9251  C  CA  . ALA   D 1 55  ? 19.860  -38.320 6.016   1.00 124.20 ? 124  ALA   D CA  1 
ATOM   9252  C  C   . ALA   D 1 55  ? 19.031  -37.406 6.907   1.00 132.33 ? 124  ALA   D C   1 
ATOM   9253  O  O   . ALA   D 1 55  ? 17.986  -36.899 6.490   1.00 136.61 ? 124  ALA   D O   1 
ATOM   9254  C  CB  . ALA   D 1 55  ? 20.874  -37.505 5.204   1.00 111.37 ? 124  ALA   D CB  1 
ATOM   9255  N  N   . TYR   D 1 56  ? 19.491  -37.198 8.136   1.00 132.28 ? 125  TYR   D N   1 
ATOM   9256  C  CA  . TYR   D 1 56  ? 18.815  -36.217 8.990   1.00 144.41 ? 125  TYR   D CA  1 
ATOM   9257  C  C   . TYR   D 1 56  ? 19.743  -35.103 9.461   1.00 145.80 ? 125  TYR   D C   1 
ATOM   9258  O  O   . TYR   D 1 56  ? 19.278  -34.061 9.919   1.00 150.24 ? 125  TYR   D O   1 
ATOM   9259  C  CB  . TYR   D 1 56  ? 18.178  -36.904 10.195  1.00 147.67 ? 125  TYR   D CB  1 
ATOM   9260  C  CG  . TYR   D 1 56  ? 17.539  -35.954 11.182  1.00 150.35 ? 125  TYR   D CG  1 
ATOM   9261  C  CD1 . TYR   D 1 56  ? 16.299  -35.377 10.911  1.00 149.77 ? 125  TYR   D CD1 1 
ATOM   9262  C  CD2 . TYR   D 1 56  ? 18.172  -35.628 12.377  1.00 150.75 ? 125  TYR   D CD2 1 
ATOM   9263  C  CE1 . TYR   D 1 56  ? 15.705  -34.501 11.800  1.00 145.97 ? 125  TYR   D CE1 1 
ATOM   9264  C  CE2 . TYR   D 1 56  ? 17.586  -34.750 13.280  1.00 152.31 ? 125  TYR   D CE2 1 
ATOM   9265  C  CZ  . TYR   D 1 56  ? 16.352  -34.190 12.980  1.00 150.33 ? 125  TYR   D CZ  1 
ATOM   9266  O  OH  . TYR   D 1 56  ? 15.750  -33.319 13.854  1.00 150.53 ? 125  TYR   D OH  1 
ATOM   9267  N  N   . ALA   D 1 64  ? 16.228  -34.205 9.043   1.00 156.39 ? 133  ALA   D N   1 
ATOM   9268  C  CA  . ALA   D 1 64  ? 16.351  -33.426 7.811   1.00 159.01 ? 133  ALA   D CA  1 
ATOM   9269  C  C   . ALA   D 1 64  ? 15.583  -34.067 6.627   1.00 158.35 ? 133  ALA   D C   1 
ATOM   9270  O  O   . ALA   D 1 64  ? 14.916  -35.103 6.790   1.00 156.90 ? 133  ALA   D O   1 
ATOM   9271  C  CB  . ALA   D 1 64  ? 17.827  -33.236 7.455   1.00 158.87 ? 133  ALA   D CB  1 
ATOM   9272  N  N   . GLN   D 1 65  ? 15.699  -33.460 5.439   1.00 143.61 ? 134  GLN   D N   1 
ATOM   9273  C  CA  . GLN   D 1 65  ? 14.797  -33.729 4.325   1.00 125.29 ? 134  GLN   D CA  1 
ATOM   9274  C  C   . GLN   D 1 65  ? 15.546  -33.925 3.008   1.00 119.47 ? 134  GLN   D C   1 
ATOM   9275  O  O   . GLN   D 1 65  ? 15.158  -33.380 1.972   1.00 117.09 ? 134  GLN   D O   1 
ATOM   9276  C  CB  . GLN   D 1 65  ? 13.776  -32.603 4.177   1.00 123.50 ? 134  GLN   D CB  1 
ATOM   9277  C  CG  . GLN   D 1 65  ? 14.372  -31.204 3.932   1.00 127.52 ? 134  GLN   D CG  1 
ATOM   9278  C  CD  . GLN   D 1 65  ? 14.619  -30.419 5.215   1.00 131.74 ? 134  GLN   D CD  1 
ATOM   9279  O  OE1 . GLN   D 1 65  ? 15.448  -30.806 6.041   1.00 135.76 ? 134  GLN   D OE1 1 
ATOM   9280  N  NE2 . GLN   D 1 65  ? 13.897  -29.311 5.387   1.00 126.69 ? 134  GLN   D NE2 1 
ATOM   9281  N  N   . PHE   D 1 66  ? 16.614  -34.723 3.006   1.00 118.54 ? 135  PHE   D N   1 
ATOM   9282  C  CA  . PHE   D 1 66  ? 17.211  -35.182 1.750   1.00 111.16 ? 135  PHE   D CA  1 
ATOM   9283  C  C   . PHE   D 1 66  ? 17.632  -36.635 1.907   1.00 109.74 ? 135  PHE   D C   1 
ATOM   9284  O  O   . PHE   D 1 66  ? 17.468  -37.241 2.969   1.00 114.97 ? 135  PHE   D O   1 
ATOM   9285  C  CB  . PHE   D 1 66  ? 18.418  -34.340 1.328   1.00 107.06 ? 135  PHE   D CB  1 
ATOM   9286  C  CG  . PHE   D 1 66  ? 18.108  -32.886 1.117   1.00 115.27 ? 135  PHE   D CG  1 
ATOM   9287  C  CD1 . PHE   D 1 66  ? 17.625  -32.431 -0.105  1.00 113.62 ? 135  PHE   D CD1 1 
ATOM   9288  C  CD2 . PHE   D 1 66  ? 18.326  -31.963 2.128   1.00 115.19 ? 135  PHE   D CD2 1 
ATOM   9289  C  CE1 . PHE   D 1 66  ? 17.356  -31.087 -0.304  1.00 105.99 ? 135  PHE   D CE1 1 
ATOM   9290  C  CE2 . PHE   D 1 66  ? 18.061  -30.635 1.933   1.00 109.97 ? 135  PHE   D CE2 1 
ATOM   9291  C  CZ  . PHE   D 1 66  ? 17.574  -30.197 0.716   1.00 108.02 ? 135  PHE   D CZ  1 
ATOM   9292  N  N   . GLY   D 1 67  ? 18.190  -37.200 0.844   1.00 106.99 ? 136  GLY   D N   1 
ATOM   9293  C  CA  . GLY   D 1 67  ? 18.606  -38.586 0.889   1.00 106.62 ? 136  GLY   D CA  1 
ATOM   9294  C  C   . GLY   D 1 67  ? 18.949  -39.096 -0.495  1.00 98.31  ? 136  GLY   D C   1 
ATOM   9295  O  O   . GLY   D 1 67  ? 18.962  -38.342 -1.467  1.00 91.22  ? 136  GLY   D O   1 
ATOM   9296  N  N   . THR   D 1 68  ? 19.229  -40.402 -0.556  1.00 95.40  ? 137  THR   D N   1 
ATOM   9297  C  CA  . THR   D 1 68  ? 19.595  -41.069 -1.796  1.00 91.67  ? 137  THR   D CA  1 
ATOM   9298  C  C   . THR   D 1 68  ? 18.820  -42.364 -1.930  1.00 94.78  ? 137  THR   D C   1 
ATOM   9299  O  O   . THR   D 1 68  ? 18.560  -43.043 -0.932  1.00 97.66  ? 137  THR   D O   1 
ATOM   9300  C  CB  . THR   D 1 68  ? 21.087  -41.388 -1.868  1.00 89.34  ? 137  THR   D CB  1 
ATOM   9301  O  OG1 . THR   D 1 68  ? 21.841  -40.228 -1.506  1.00 94.85  ? 137  THR   D OG1 1 
ATOM   9302  C  CG2 . THR   D 1 68  ? 21.457  -41.816 -3.278  1.00 89.03  ? 137  THR   D CG2 1 
ATOM   9303  N  N   . THR   D 1 69  ? 18.449  -42.701 -3.166  1.00 96.44  ? 138  THR   D N   1 
ATOM   9304  C  CA  . THR   D 1 69  ? 17.860  -44.007 -3.429  1.00 90.86  ? 138  THR   D CA  1 
ATOM   9305  C  C   . THR   D 1 69  ? 18.952  -45.053 -3.472  1.00 88.01  ? 138  THR   D C   1 
ATOM   9306  O  O   . THR   D 1 69  ? 20.090  -44.765 -3.842  1.00 83.67  ? 138  THR   D O   1 
ATOM   9307  C  CB  . THR   D 1 69  ? 17.104  -44.049 -4.750  1.00 91.12  ? 138  THR   D CB  1 
ATOM   9308  O  OG1 . THR   D 1 69  ? 17.986  -43.699 -5.825  1.00 89.73  ? 138  THR   D OG1 1 
ATOM   9309  C  CG2 . THR   D 1 69  ? 15.886  -43.136 -4.709  1.00 93.18  ? 138  THR   D CG2 1 
ATOM   9310  N  N   . ALA   D 1 70  ? 18.593  -46.280 -3.090  1.00 92.81  ? 139  ALA   D N   1 
ATOM   9311  C  CA  . ALA   D 1 70  ? 19.508  -47.416 -3.163  1.00 92.21  ? 139  ALA   D CA  1 
ATOM   9312  C  C   . ALA   D 1 70  ? 18.844  -48.600 -3.845  1.00 93.08  ? 139  ALA   D C   1 
ATOM   9313  O  O   . ALA   D 1 70  ? 17.748  -49.013 -3.450  1.00 95.67  ? 139  ALA   D O   1 
ATOM   9314  C  CB  . ALA   D 1 70  ? 19.991  -47.838 -1.780  1.00 90.91  ? 139  ALA   D CB  1 
ATOM   9315  N  N   . GLU   D 1 71  ? 19.543  -49.169 -4.830  1.00 92.21  ? 140  GLU   D N   1 
ATOM   9316  C  CA  . GLU   D 1 71  ? 19.070  -50.320 -5.605  1.00 96.78  ? 140  GLU   D CA  1 
ATOM   9317  C  C   . GLU   D 1 71  ? 19.604  -51.623 -5.024  1.00 92.53  ? 140  GLU   D C   1 
ATOM   9318  O  O   . GLU   D 1 71  ? 20.823  -51.793 -4.881  1.00 93.91  ? 140  GLU   D O   1 
ATOM   9319  C  CB  . GLU   D 1 71  ? 19.485  -50.214 -7.079  1.00 94.67  ? 140  GLU   D CB  1 
ATOM   9320  C  CG  . GLU   D 1 71  ? 18.874  -51.249 -8.019  1.00 93.69  ? 140  GLU   D CG  1 
ATOM   9321  C  CD  . GLU   D 1 71  ? 19.406  -51.085 -9.430  1.00 93.41  ? 140  GLU   D CD  1 
ATOM   9322  O  OE1 . GLU   D 1 71  ? 20.153  -50.108 -9.647  1.00 78.06  ? 140  GLU   D OE1 1 
ATOM   9323  O  OE2 . GLU   D 1 71  ? 19.099  -51.928 -10.313 1.00 103.09 ? 140  GLU   D OE2 1 
ATOM   9324  N  N   . ILE   D 1 72  ? 18.695  -52.542 -4.693  1.00 96.42  ? 141  ILE   D N   1 
ATOM   9325  C  CA  . ILE   D 1 72  ? 19.143  -53.869 -4.300  1.00 94.37  ? 141  ILE   D CA  1 
ATOM   9326  C  C   . ILE   D 1 72  ? 19.803  -54.532 -5.499  1.00 94.22  ? 141  ILE   D C   1 
ATOM   9327  O  O   . ILE   D 1 72  ? 19.259  -54.531 -6.613  1.00 98.63  ? 141  ILE   D O   1 
ATOM   9328  C  CB  . ILE   D 1 72  ? 17.986  -54.720 -3.756  1.00 93.18  ? 141  ILE   D CB  1 
ATOM   9329  C  CG1 . ILE   D 1 72  ? 17.197  -53.975 -2.693  1.00 90.80  ? 141  ILE   D CG1 1 
ATOM   9330  C  CG2 . ILE   D 1 72  ? 18.532  -55.948 -3.130  1.00 96.04  ? 141  ILE   D CG2 1 
ATOM   9331  C  CD1 . ILE   D 1 72  ? 15.957  -53.282 -3.263  1.00 99.23  ? 141  ILE   D CD1 1 
ATOM   9332  N  N   . TYR   D 1 73  ? 20.993  -55.078 -5.284  1.00 89.41  ? 142  TYR   D N   1 
ATOM   9333  C  CA  . TYR   D 1 73  ? 21.676  -55.821 -6.329  1.00 94.13  ? 142  TYR   D CA  1 
ATOM   9334  C  C   . TYR   D 1 73  ? 22.233  -57.145 -5.835  1.00 91.51  ? 142  TYR   D C   1 
ATOM   9335  O  O   . TYR   D 1 73  ? 22.823  -57.882 -6.630  1.00 96.87  ? 142  TYR   D O   1 
ATOM   9336  C  CB  . TYR   D 1 73  ? 22.803  -54.976 -6.951  1.00 95.06  ? 142  TYR   D CB  1 
ATOM   9337  C  CG  . TYR   D 1 73  ? 24.036  -54.859 -6.093  1.00 97.89  ? 142  TYR   D CG  1 
ATOM   9338  C  CD1 . TYR   D 1 73  ? 24.124  -53.869 -5.123  1.00 95.09  ? 142  TYR   D CD1 1 
ATOM   9339  C  CD2 . TYR   D 1 73  ? 25.109  -55.741 -6.241  1.00 102.49 ? 142  TYR   D CD2 1 
ATOM   9340  C  CE1 . TYR   D 1 73  ? 25.235  -53.752 -4.324  1.00 98.32  ? 142  TYR   D CE1 1 
ATOM   9341  C  CE2 . TYR   D 1 73  ? 26.237  -55.632 -5.427  1.00 106.59 ? 142  TYR   D CE2 1 
ATOM   9342  C  CZ  . TYR   D 1 73  ? 26.280  -54.622 -4.467  1.00 97.57  ? 142  TYR   D CZ  1 
ATOM   9343  O  OH  . TYR   D 1 73  ? 27.351  -54.444 -3.626  1.00 101.52 ? 142  TYR   D OH  1 
ATOM   9344  N  N   . ALA   D 1 74  ? 22.075  -57.453 -4.549  1.00 91.42  ? 143  ALA   D N   1 
ATOM   9345  C  CA  . ALA   D 1 74  ? 22.414  -58.749 -3.988  1.00 97.17  ? 143  ALA   D CA  1 
ATOM   9346  C  C   . ALA   D 1 74  ? 21.403  -59.092 -2.900  1.00 100.46 ? 143  ALA   D C   1 
ATOM   9347  O  O   . ALA   D 1 74  ? 20.965  -58.221 -2.149  1.00 96.81  ? 143  ALA   D O   1 
ATOM   9348  C  CB  . ALA   D 1 74  ? 23.844  -58.776 -3.427  1.00 93.40  ? 143  ALA   D CB  1 
ATOM   9349  N  N   . TYR   D 1 75  ? 21.035  -60.367 -2.817  1.00 104.70 ? 144  TYR   D N   1 
ATOM   9350  C  CA  . TYR   D 1 75  ? 20.044  -60.818 -1.855  1.00 97.10  ? 144  TYR   D CA  1 
ATOM   9351  C  C   . TYR   D 1 75  ? 20.349  -62.274 -1.526  1.00 97.23  ? 144  TYR   D C   1 
ATOM   9352  O  O   . TYR   D 1 75  ? 20.653  -63.054 -2.428  1.00 101.19 ? 144  TYR   D O   1 
ATOM   9353  C  CB  . TYR   D 1 75  ? 18.638  -60.640 -2.429  1.00 97.82  ? 144  TYR   D CB  1 
ATOM   9354  C  CG  . TYR   D 1 75  ? 17.529  -61.154 -1.552  1.00 104.10 ? 144  TYR   D CG  1 
ATOM   9355  C  CD1 . TYR   D 1 75  ? 17.175  -62.503 -1.555  1.00 103.53 ? 144  TYR   D CD1 1 
ATOM   9356  C  CD2 . TYR   D 1 75  ? 16.819  -60.288 -0.728  1.00 109.86 ? 144  TYR   D CD2 1 
ATOM   9357  C  CE1 . TYR   D 1 75  ? 16.142  -62.977 -0.744  1.00 104.99 ? 144  TYR   D CE1 1 
ATOM   9358  C  CE2 . TYR   D 1 75  ? 15.789  -60.745 0.084   1.00 114.12 ? 144  TYR   D CE2 1 
ATOM   9359  C  CZ  . TYR   D 1 75  ? 15.453  -62.086 0.076   1.00 109.19 ? 144  TYR   D CZ  1 
ATOM   9360  O  OH  . TYR   D 1 75  ? 14.427  -62.512 0.889   1.00 114.70 ? 144  TYR   D OH  1 
ATOM   9361  N  N   . ARG   D 1 76  ? 20.316  -62.627 -0.235  1.00 106.84 ? 145  ARG   D N   1 
ATOM   9362  C  CA  . ARG   D 1 76  ? 20.513  -64.018 0.194   1.00 107.19 ? 145  ARG   D CA  1 
ATOM   9363  C  C   . ARG   D 1 76  ? 19.799  -64.255 1.510   1.00 112.13 ? 145  ARG   D C   1 
ATOM   9364  O  O   . ARG   D 1 76  ? 20.046  -63.542 2.490   1.00 111.62 ? 145  ARG   D O   1 
ATOM   9365  C  CB  . ARG   D 1 76  ? 21.999  -64.391 0.343   1.00 102.33 ? 145  ARG   D CB  1 
ATOM   9366  N  N   . GLU   D 1 77  ? 18.942  -65.269 1.531   1.00 114.56 ? 146  GLU   D N   1 
ATOM   9367  C  CA  . GLU   D 1 77  ? 18.356  -65.750 2.774   1.00 119.05 ? 146  GLU   D CA  1 
ATOM   9368  C  C   . GLU   D 1 77  ? 19.295  -66.754 3.437   1.00 125.79 ? 146  GLU   D C   1 
ATOM   9369  O  O   . GLU   D 1 77  ? 19.963  -67.535 2.753   1.00 122.13 ? 146  GLU   D O   1 
ATOM   9370  C  CB  . GLU   D 1 77  ? 16.995  -66.397 2.500   1.00 118.03 ? 146  GLU   D CB  1 
ATOM   9371  C  CG  . GLU   D 1 77  ? 16.200  -65.718 1.405   1.00 112.47 ? 146  GLU   D CG  1 
ATOM   9372  C  CD  . GLU   D 1 77  ? 14.708  -65.715 1.697   1.00 115.80 ? 146  GLU   D CD  1 
ATOM   9373  O  OE1 . GLU   D 1 77  ? 14.320  -66.218 2.775   1.00 128.25 ? 146  GLU   D OE1 1 
ATOM   9374  O  OE2 . GLU   D 1 77  ? 13.927  -65.209 0.856   1.00 110.44 ? 146  GLU   D OE2 1 
ATOM   9375  N  N   . GLU   D 1 78  ? 19.350  -66.733 4.773   1.00 134.16 ? 147  GLU   D N   1 
ATOM   9376  C  CA  . GLU   D 1 78  ? 20.266  -67.633 5.474   1.00 143.88 ? 147  GLU   D CA  1 
ATOM   9377  C  C   . GLU   D 1 78  ? 19.881  -67.792 6.949   1.00 154.42 ? 147  GLU   D C   1 
ATOM   9378  O  O   . GLU   D 1 78  ? 20.451  -67.139 7.830   1.00 157.07 ? 147  GLU   D O   1 
ATOM   9379  C  CB  . GLU   D 1 78  ? 21.704  -67.114 5.330   1.00 137.91 ? 147  GLU   D CB  1 
ATOM   9380  C  CG  . GLU   D 1 78  ? 22.735  -67.750 6.257   1.00 144.36 ? 147  GLU   D CG  1 
ATOM   9381  C  CD  . GLU   D 1 78  ? 23.720  -66.728 6.812   1.00 148.47 ? 147  GLU   D CD  1 
ATOM   9382  O  OE1 . GLU   D 1 78  ? 24.008  -66.782 8.036   1.00 149.36 ? 147  GLU   D OE1 1 
ATOM   9383  O  OE2 . GLU   D 1 78  ? 24.194  -65.865 6.030   1.00 144.94 ? 147  GLU   D OE2 1 
ATOM   9384  N  N   . GLN   D 1 79  ? 18.929  -68.690 7.232   1.00 171.70 ? 148  GLN   D N   1 
ATOM   9385  C  CA  . GLN   D 1 79  ? 18.405  -68.873 8.583   1.00 176.97 ? 148  GLN   D CA  1 
ATOM   9386  C  C   . GLN   D 1 79  ? 19.549  -69.266 9.526   1.00 183.12 ? 148  GLN   D C   1 
ATOM   9387  O  O   . GLN   D 1 79  ? 20.034  -70.402 9.471   1.00 181.51 ? 148  GLN   D O   1 
ATOM   9388  C  CB  . GLN   D 1 79  ? 17.273  -69.912 8.558   1.00 173.08 ? 148  GLN   D CB  1 
ATOM   9389  N  N   . ASP   D 1 80  ? 19.959  -68.346 10.419  1.00 178.38 ? 149  ASP   D N   1 
ATOM   9390  C  CA  . ASP   D 1 80  ? 21.074  -68.576 11.341  1.00 178.70 ? 149  ASP   D CA  1 
ATOM   9391  C  C   . ASP   D 1 80  ? 20.530  -69.162 12.643  1.00 180.65 ? 149  ASP   D C   1 
ATOM   9392  O  O   . ASP   D 1 80  ? 19.692  -68.547 13.311  1.00 178.69 ? 149  ASP   D O   1 
ATOM   9393  C  CB  . ASP   D 1 80  ? 21.852  -67.289 11.643  1.00 176.25 ? 149  ASP   D CB  1 
ATOM   9394  N  N   . PHE   D 1 81  ? 21.048  -70.335 13.022  1.00 188.48 ? 150  PHE   D N   1 
ATOM   9395  C  CA  . PHE   D 1 81  ? 20.542  -71.114 14.154  1.00 189.55 ? 150  PHE   D CA  1 
ATOM   9396  C  C   . PHE   D 1 81  ? 19.072  -71.192 13.756  1.00 189.06 ? 150  PHE   D C   1 
ATOM   9397  O  O   . PHE   D 1 81  ? 18.739  -71.586 12.630  1.00 187.65 ? 150  PHE   D O   1 
ATOM   9398  C  CB  . PHE   D 1 81  ? 20.768  -70.379 15.481  1.00 185.55 ? 150  PHE   D CB  1 
ATOM   9399  N  N   . GLY   D 1 82  ? 18.187  -70.827 14.679  1.00 184.93 ? 151  GLY   D N   1 
ATOM   9400  C  CA  . GLY   D 1 82  ? 16.779  -70.697 14.377  1.00 180.98 ? 151  GLY   D CA  1 
ATOM   9401  C  C   . GLY   D 1 82  ? 16.231  -69.379 13.868  1.00 176.13 ? 151  GLY   D C   1 
ATOM   9402  O  O   . GLY   D 1 82  ? 15.031  -69.257 13.589  1.00 173.66 ? 151  GLY   D O   1 
ATOM   9403  N  N   . ILE   D 1 83  ? 17.095  -68.382 13.743  1.00 175.08 ? 152  ILE   D N   1 
ATOM   9404  C  CA  . ILE   D 1 83  ? 16.685  -67.047 13.329  1.00 168.95 ? 152  ILE   D CA  1 
ATOM   9405  C  C   . ILE   D 1 83  ? 16.894  -66.920 11.824  1.00 172.35 ? 152  ILE   D C   1 
ATOM   9406  O  O   . ILE   D 1 83  ? 18.010  -67.095 11.327  1.00 173.40 ? 152  ILE   D O   1 
ATOM   9407  C  CB  . ILE   D 1 83  ? 17.455  -65.964 14.093  1.00 158.10 ? 152  ILE   D CB  1 
ATOM   9408  N  N   . GLU   D 1 84  ? 15.807  -66.639 11.093  1.00 172.62 ? 153  GLU   D N   1 
ATOM   9409  C  CA  . GLU   D 1 84  ? 15.881  -66.386 9.653   1.00 171.79 ? 153  GLU   D CA  1 
ATOM   9410  C  C   . GLU   D 1 84  ? 16.508  -65.015 9.384   1.00 170.40 ? 153  GLU   D C   1 
ATOM   9411  O  O   . GLU   D 1 84  ? 15.992  -63.986 9.834   1.00 170.30 ? 153  GLU   D O   1 
ATOM   9412  C  CB  . GLU   D 1 84  ? 14.491  -66.448 9.032   1.00 173.87 ? 153  GLU   D CB  1 
ATOM   9413  C  CG  . GLU   D 1 84  ? 14.417  -65.707 7.695   1.00 174.72 ? 153  GLU   D CG  1 
ATOM   9414  C  CD  . GLU   D 1 84  ? 13.017  -65.252 7.317   1.00 177.22 ? 153  GLU   D CD  1 
ATOM   9415  O  OE1 . GLU   D 1 84  ? 12.572  -64.187 7.807   1.00 173.19 ? 153  GLU   D OE1 1 
ATOM   9416  O  OE2 . GLU   D 1 84  ? 12.371  -65.955 6.509   1.00 181.38 ? 153  GLU   D OE2 1 
ATOM   9417  N  N   . ILE   D 1 85  ? 17.597  -64.992 8.616   1.00 159.77 ? 154  ILE   D N   1 
ATOM   9418  C  CA  . ILE   D 1 85  ? 18.320  -63.766 8.301   1.00 146.24 ? 154  ILE   D CA  1 
ATOM   9419  C  C   . ILE   D 1 85  ? 18.264  -63.538 6.799   1.00 137.99 ? 154  ILE   D C   1 
ATOM   9420  O  O   . ILE   D 1 85  ? 18.267  -64.491 6.008   1.00 137.38 ? 154  ILE   D O   1 
ATOM   9421  C  CB  . ILE   D 1 85  ? 19.790  -63.814 8.773   1.00 147.90 ? 154  ILE   D CB  1 
ATOM   9422  C  CG1 . ILE   D 1 85  ? 19.933  -64.672 10.035  1.00 159.75 ? 154  ILE   D CG1 1 
ATOM   9423  C  CG2 . ILE   D 1 85  ? 20.337  -62.406 9.002   1.00 141.47 ? 154  ILE   D CG2 1 
ATOM   9424  C  CD1 . ILE   D 1 85  ? 19.061  -64.215 11.180  1.00 165.95 ? 154  ILE   D CD1 1 
ATOM   9425  N  N   . VAL   D 1 86  ? 18.209  -62.271 6.410   1.00 127.69 ? 155  VAL   D N   1 
ATOM   9426  C  CA  . VAL   D 1 86  ? 18.356  -61.862 5.023   1.00 122.45 ? 155  VAL   D CA  1 
ATOM   9427  C  C   . VAL   D 1 86  ? 19.573  -60.963 4.942   1.00 122.09 ? 155  VAL   D C   1 
ATOM   9428  O  O   . VAL   D 1 86  ? 19.763  -60.084 5.788   1.00 120.59 ? 155  VAL   D O   1 
ATOM   9429  C  CB  . VAL   D 1 86  ? 17.106  -61.138 4.495   1.00 121.93 ? 155  VAL   D CB  1 
ATOM   9430  C  CG1 . VAL   D 1 86  ? 17.444  -60.366 3.218   1.00 121.26 ? 155  VAL   D CG1 1 
ATOM   9431  C  CG2 . VAL   D 1 86  ? 16.001  -62.120 4.234   1.00 118.21 ? 155  VAL   D CG2 1 
ATOM   9432  N  N   . LYS   D 1 87  ? 20.400  -61.187 3.942   1.00 114.85 ? 156  LYS   D N   1 
ATOM   9433  C  CA  . LYS   D 1 87  ? 21.556  -60.342 3.709   1.00 109.65 ? 156  LYS   D CA  1 
ATOM   9434  C  C   . LYS   D 1 87  ? 21.383  -59.716 2.332   1.00 103.66 ? 156  LYS   D C   1 
ATOM   9435  O  O   . LYS   D 1 87  ? 21.503  -60.398 1.312   1.00 102.76 ? 156  LYS   D O   1 
ATOM   9436  C  CB  . LYS   D 1 87  ? 22.856  -61.140 3.838   1.00 113.28 ? 156  LYS   D CB  1 
ATOM   9437  C  CG  . LYS   D 1 87  ? 23.507  -61.085 5.243   1.00 120.83 ? 156  LYS   D CG  1 
ATOM   9438  C  CD  . LYS   D 1 87  ? 24.625  -62.146 5.392   1.00 128.05 ? 156  LYS   D CD  1 
ATOM   9439  C  CE  . LYS   D 1 87  ? 25.473  -61.953 6.652   1.00 124.53 ? 156  LYS   D CE  1 
ATOM   9440  N  NZ  . LYS   D 1 87  ? 26.611  -61.011 6.426   1.00 126.66 ? 156  LYS   D NZ  1 
ATOM   9441  N  N   . VAL   D 1 88  ? 21.082  -58.423 2.310   1.00 107.60 ? 157  VAL   D N   1 
ATOM   9442  C  CA  . VAL   D 1 88  ? 20.929  -57.650 1.080   1.00 102.88 ? 157  VAL   D CA  1 
ATOM   9443  C  C   . VAL   D 1 88  ? 22.108  -56.687 0.943   1.00 96.94  ? 157  VAL   D C   1 
ATOM   9444  O  O   . VAL   D 1 88  ? 22.745  -56.307 1.928   1.00 96.16  ? 157  VAL   D O   1 
ATOM   9445  C  CB  . VAL   D 1 88  ? 19.587  -56.885 1.082   1.00 99.09  ? 157  VAL   D CB  1 
ATOM   9446  C  CG1 . VAL   D 1 88  ? 19.639  -55.825 2.135   1.00 105.27 ? 157  VAL   D CG1 1 
ATOM   9447  C  CG2 . VAL   D 1 88  ? 19.346  -56.212 -0.235  1.00 94.18  ? 157  VAL   D CG2 1 
ATOM   9448  N  N   . LYS   D 1 89  ? 22.419  -56.319 -0.293  1.00 97.37  ? 158  LYS   D N   1 
ATOM   9449  C  CA  . LYS   D 1 89  ? 23.355  -55.240 -0.591  1.00 93.26  ? 158  LYS   D CA  1 
ATOM   9450  C  C   . LYS   D 1 89  ? 22.695  -54.339 -1.626  1.00 89.83  ? 158  LYS   D C   1 
ATOM   9451  O  O   . LYS   D 1 89  ? 21.936  -54.814 -2.471  1.00 92.01  ? 158  LYS   D O   1 
ATOM   9452  C  CB  . LYS   D 1 89  ? 24.720  -55.765 -1.098  1.00 86.53  ? 158  LYS   D CB  1 
ATOM   9453  N  N   . ALA   D 1 90  ? 22.921  -53.033 -1.520  1.00 91.46  ? 159  ALA   D N   1 
ATOM   9454  C  CA  . ALA   D 1 90  ? 22.329  -52.083 -2.448  1.00 86.71  ? 159  ALA   D CA  1 
ATOM   9455  C  C   . ALA   D 1 90  ? 23.353  -51.007 -2.728  1.00 89.13  ? 159  ALA   D C   1 
ATOM   9456  O  O   . ALA   D 1 90  ? 24.334  -50.849 -1.999  1.00 94.28  ? 159  ALA   D O   1 
ATOM   9457  C  CB  . ALA   D 1 90  ? 21.028  -51.473 -1.917  1.00 84.42  ? 159  ALA   D CB  1 
ATOM   9458  N  N   . ILE   D 1 91  ? 23.121  -50.268 -3.798  1.00 83.50  ? 160  ILE   D N   1 
ATOM   9459  C  CA  . ILE   D 1 91  ? 24.069  -49.265 -4.231  1.00 84.73  ? 160  ILE   D CA  1 
ATOM   9460  C  C   . ILE   D 1 91  ? 23.335  -47.940 -4.379  1.00 92.78  ? 160  ILE   D C   1 
ATOM   9461  O  O   . ILE   D 1 91  ? 22.137  -47.902 -4.687  1.00 88.46  ? 160  ILE   D O   1 
ATOM   9462  C  CB  . ILE   D 1 91  ? 24.748  -49.700 -5.533  1.00 82.12  ? 160  ILE   D CB  1 
ATOM   9463  C  CG1 . ILE   D 1 91  ? 25.899  -48.777 -5.873  1.00 86.52  ? 160  ILE   D CG1 1 
ATOM   9464  C  CG2 . ILE   D 1 91  ? 23.752  -49.733 -6.665  1.00 80.55  ? 160  ILE   D CG2 1 
ATOM   9465  C  CD1 . ILE   D 1 91  ? 26.405  -49.041 -7.235  1.00 79.46  ? 160  ILE   D CD1 1 
ATOM   9466  N  N   . GLY   D 1 92  ? 24.063  -46.848 -4.131  1.00 96.92  ? 161  GLY   D N   1 
ATOM   9467  C  CA  . GLY   D 1 92  ? 23.473  -45.521 -4.235  1.00 96.46  ? 161  GLY   D CA  1 
ATOM   9468  C  C   . GLY   D 1 92  ? 23.209  -45.149 -5.685  1.00 97.18  ? 161  GLY   D C   1 
ATOM   9469  O  O   . GLY   D 1 92  ? 24.011  -45.424 -6.577  1.00 97.47  ? 161  GLY   D O   1 
ATOM   9470  N  N   . ARG   D 1 93  ? 22.063  -44.519 -5.923  1.00 89.86  ? 162  ARG   D N   1 
ATOM   9471  C  CA  . ARG   D 1 93  ? 21.626  -44.302 -7.294  1.00 87.89  ? 162  ARG   D CA  1 
ATOM   9472  C  C   . ARG   D 1 93  ? 21.338  -42.833 -7.547  1.00 89.12  ? 162  ARG   D C   1 
ATOM   9473  O  O   . ARG   D 1 93  ? 22.156  -42.143 -8.157  1.00 91.62  ? 162  ARG   D O   1 
ATOM   9474  C  CB  . ARG   D 1 93  ? 20.395  -45.152 -7.603  1.00 93.09  ? 162  ARG   D CB  1 
ATOM   9475  C  CG  . ARG   D 1 93  ? 20.716  -46.598 -7.937  1.00 84.09  ? 162  ARG   D CG  1 
ATOM   9476  C  CD  . ARG   D 1 93  ? 21.677  -46.666 -9.102  1.00 83.08  ? 162  ARG   D CD  1 
ATOM   9477  N  NE  . ARG   D 1 93  ? 21.660  -47.998 -9.695  1.00 94.99  ? 162  ARG   D NE  1 
ATOM   9478  C  CZ  . ARG   D 1 93  ? 22.731  -48.742 -9.947  1.00 89.32  ? 162  ARG   D CZ  1 
ATOM   9479  N  NH1 . ARG   D 1 93  ? 23.956  -48.294 -9.720  1.00 85.34  ? 162  ARG   D NH1 1 
ATOM   9480  N  NH2 . ARG   D 1 93  ? 22.565  -49.967 -10.434 1.00 87.11  ? 162  ARG   D NH2 1 
ATOM   9481  N  N   . GLN   D 1 94  ? 20.199  -42.333 -7.071  1.00 92.45  ? 163  GLN   D N   1 
ATOM   9482  C  CA  . GLN   D 1 94  ? 19.829  -40.941 -7.277  1.00 88.99  ? 163  GLN   D CA  1 
ATOM   9483  C  C   . GLN   D 1 94  ? 19.657  -40.216 -5.946  1.00 93.60  ? 163  GLN   D C   1 
ATOM   9484  O  O   . GLN   D 1 94  ? 19.212  -40.807 -4.952  1.00 88.50  ? 163  GLN   D O   1 
ATOM   9485  C  CB  . GLN   D 1 94  ? 18.555  -40.840 -8.111  1.00 91.11  ? 163  GLN   D CB  1 
ATOM   9486  C  CG  . GLN   D 1 94  ? 18.689  -41.412 -9.517  1.00 94.38  ? 163  GLN   D CG  1 
ATOM   9487  C  CD  . GLN   D 1 94  ? 17.344  -41.743 -10.142 1.00 108.38 ? 163  GLN   D CD  1 
ATOM   9488  O  OE1 . GLN   D 1 94  ? 16.951  -41.147 -11.155 1.00 110.76 ? 163  GLN   D OE1 1 
ATOM   9489  N  NE2 . GLN   D 1 94  ? 16.632  -42.713 -9.546  1.00 106.90 ? 163  GLN   D NE2 1 
ATOM   9490  N  N   . ARG   D 1 95  ? 20.039  -38.929 -5.944  1.00 95.96  ? 164  ARG   D N   1 
ATOM   9491  C  CA  . ARG   D 1 95  ? 19.832  -38.024 -4.825  1.00 89.80  ? 164  ARG   D CA  1 
ATOM   9492  C  C   . ARG   D 1 95  ? 18.472  -37.357 -4.951  1.00 89.30  ? 164  ARG   D C   1 
ATOM   9493  O  O   . ARG   D 1 95  ? 17.939  -37.199 -6.046  1.00 91.29  ? 164  ARG   D O   1 
ATOM   9494  C  CB  . ARG   D 1 95  ? 20.927  -36.961 -4.772  1.00 88.22  ? 164  ARG   D CB  1 
ATOM   9495  C  CG  . ARG   D 1 95  ? 22.340  -37.506 -4.699  1.00 88.38  ? 164  ARG   D CG  1 
ATOM   9496  C  CD  . ARG   D 1 95  ? 23.251  -36.548 -5.390  1.00 83.35  ? 164  ARG   D CD  1 
ATOM   9497  N  NE  . ARG   D 1 95  ? 22.497  -35.924 -6.464  1.00 89.72  ? 164  ARG   D NE  1 
ATOM   9498  C  CZ  . ARG   D 1 95  ? 22.883  -34.848 -7.130  1.00 89.76  ? 164  ARG   D CZ  1 
ATOM   9499  N  NH1 . ARG   D 1 95  ? 24.057  -34.280 -6.897  1.00 91.92  ? 164  ARG   D NH1 1 
ATOM   9500  N  NH2 . ARG   D 1 95  ? 22.069  -34.328 -8.045  1.00 95.34  ? 164  ARG   D NH2 1 
ATOM   9501  N  N   . PHE   D 1 96  ? 17.905  -36.967 -3.816  1.00 95.29  ? 165  PHE   D N   1 
ATOM   9502  C  CA  . PHE   D 1 96  ? 16.544  -36.452 -3.836  1.00 100.74 ? 165  PHE   D CA  1 
ATOM   9503  C  C   . PHE   D 1 96  ? 16.302  -35.533 -2.636  1.00 105.38 ? 165  PHE   D C   1 
ATOM   9504  O  O   . PHE   D 1 96  ? 17.019  -35.579 -1.628  1.00 106.34 ? 165  PHE   D O   1 
ATOM   9505  C  CB  . PHE   D 1 96  ? 15.522  -37.608 -3.872  1.00 102.28 ? 165  PHE   D CB  1 
ATOM   9506  C  CG  . PHE   D 1 96  ? 15.572  -38.526 -2.666  1.00 95.99  ? 165  PHE   D CG  1 
ATOM   9507  C  CD1 . PHE   D 1 96  ? 15.060  -38.118 -1.447  1.00 98.03  ? 165  PHE   D CD1 1 
ATOM   9508  C  CD2 . PHE   D 1 96  ? 16.102  -39.796 -2.764  1.00 93.90  ? 165  PHE   D CD2 1 
ATOM   9509  C  CE1 . PHE   D 1 96  ? 15.097  -38.944 -0.341  1.00 97.21  ? 165  PHE   D CE1 1 
ATOM   9510  C  CE2 . PHE   D 1 96  ? 16.143  -40.631 -1.654  1.00 99.38  ? 165  PHE   D CE2 1 
ATOM   9511  C  CZ  . PHE   D 1 96  ? 15.637  -40.200 -0.438  1.00 96.45  ? 165  PHE   D CZ  1 
ATOM   9512  N  N   . LYS   D 1 97  ? 15.280  -34.687 -2.767  1.00 103.18 ? 166  LYS   D N   1 
ATOM   9513  C  CA  . LYS   D 1 97  ? 14.706  -33.951 -1.648  1.00 104.96 ? 166  LYS   D CA  1 
ATOM   9514  C  C   . LYS   D 1 97  ? 13.329  -34.530 -1.356  1.00 104.84 ? 166  LYS   D C   1 
ATOM   9515  O  O   . LYS   D 1 97  ? 12.601  -34.886 -2.286  1.00 107.77 ? 166  LYS   D O   1 
ATOM   9516  C  CB  . LYS   D 1 97  ? 14.595  -32.452 -1.963  1.00 107.47 ? 166  LYS   D CB  1 
ATOM   9517  N  N   . VAL   D 1 98  ? 12.964  -34.638 -0.069  1.00 108.70 ? 167  VAL   D N   1 
ATOM   9518  C  CA  . VAL   D 1 98  ? 11.673  -35.227 0.294   1.00 109.40 ? 167  VAL   D CA  1 
ATOM   9519  C  C   . VAL   D 1 98  ? 10.593  -34.147 0.346   1.00 109.37 ? 167  VAL   D C   1 
ATOM   9520  O  O   . VAL   D 1 98  ? 10.805  -33.035 0.846   1.00 101.06 ? 167  VAL   D O   1 
ATOM   9521  C  CB  . VAL   D 1 98  ? 11.751  -35.984 1.629   1.00 101.82 ? 167  VAL   D CB  1 
ATOM   9522  C  CG1 . VAL   D 1 98  ? 13.000  -36.803 1.678   1.00 106.51 ? 167  VAL   D CG1 1 
ATOM   9523  C  CG2 . VAL   D 1 98  ? 11.713  -35.006 2.779   1.00 111.06 ? 167  VAL   D CG2 1 
ATOM   9524  N  N   . LEU   D 1 99  ? 9.416   -34.496 -0.170  1.00 108.71 ? 168  LEU   D N   1 
ATOM   9525  C  CA  . LEU   D 1 99  ? 8.262   -33.611 -0.219  1.00 107.13 ? 168  LEU   D CA  1 
ATOM   9526  C  C   . LEU   D 1 99  ? 7.233   -33.973 0.845   1.00 108.43 ? 168  LEU   D C   1 
ATOM   9527  O  O   . LEU   D 1 99  ? 6.918   -33.136 1.697   1.00 114.36 ? 168  LEU   D O   1 
ATOM   9528  C  CB  . LEU   D 1 99  ? 7.630   -33.651 -1.622  1.00 103.97 ? 168  LEU   D CB  1 
ATOM   9529  C  CG  . LEU   D 1 99  ? 8.339   -32.986 -2.808  1.00 98.70  ? 168  LEU   D CG  1 
ATOM   9530  C  CD1 . LEU   D 1 99  ? 8.832   -31.618 -2.419  1.00 114.10 ? 168  LEU   D CD1 1 
ATOM   9531  C  CD2 . LEU   D 1 99  ? 9.473   -33.807 -3.372  1.00 106.10 ? 168  LEU   D CD2 1 
ATOM   9532  N  N   . GLU   D 1 100 ? 6.686   -35.193 0.793   1.00 103.60 ? 169  GLU   D N   1 
ATOM   9533  C  CA  . GLU   D 1 100 ? 5.817   -35.765 1.814   1.00 112.42 ? 169  GLU   D CA  1 
ATOM   9534  C  C   . GLU   D 1 100 ? 6.450   -37.057 2.322   1.00 116.91 ? 169  GLU   D C   1 
ATOM   9535  O  O   . GLU   D 1 100 ? 7.392   -37.586 1.733   1.00 115.95 ? 169  GLU   D O   1 
ATOM   9536  C  CB  . GLU   D 1 100 ? 4.400   -36.023 1.272   1.00 110.21 ? 169  GLU   D CB  1 
ATOM   9537  N  N   . LEU   D 1 101 ? 5.943   -37.559 3.444   1.00 122.33 ? 170  LEU   D N   1 
ATOM   9538  C  CA  . LEU   D 1 101 ? 6.495   -38.763 4.058   1.00 126.92 ? 170  LEU   D CA  1 
ATOM   9539  C  C   . LEU   D 1 101 ? 5.413   -39.464 4.886   1.00 141.28 ? 170  LEU   D C   1 
ATOM   9540  O  O   . LEU   D 1 101 ? 5.541   -39.689 6.089   1.00 145.64 ? 170  LEU   D O   1 
ATOM   9541  C  CB  . LEU   D 1 101 ? 7.720   -38.420 4.904   1.00 110.52 ? 170  LEU   D CB  1 
ATOM   9542  N  N   . ARG   D 1 102 ? 4.307   -39.823 4.245   1.00 156.76 ? 171  ARG   D N   1 
ATOM   9543  C  CA  . ARG   D 1 102 ? 3.239   -40.542 4.940   1.00 159.82 ? 171  ARG   D CA  1 
ATOM   9544  C  C   . ARG   D 1 102 ? 3.748   -41.893 5.453   1.00 162.39 ? 171  ARG   D C   1 
ATOM   9545  O  O   . ARG   D 1 102 ? 4.311   -42.681 4.685   1.00 162.61 ? 171  ARG   D O   1 
ATOM   9546  C  CB  . ARG   D 1 102 ? 2.047   -40.740 3.990   1.00 157.33 ? 171  ARG   D CB  1 
ATOM   9547  N  N   . THR   D 1 103 ? 3.561   -42.160 6.748   1.00 154.51 ? 172  THR   D N   1 
ATOM   9548  C  CA  . THR   D 1 103 ? 3.862   -43.482 7.299   1.00 155.22 ? 172  THR   D CA  1 
ATOM   9549  C  C   . THR   D 1 103 ? 2.690   -44.439 7.095   1.00 155.59 ? 172  THR   D C   1 
ATOM   9550  O  O   . THR   D 1 103 ? 1.527   -44.034 7.051   1.00 154.59 ? 172  THR   D O   1 
ATOM   9551  C  CB  . THR   D 1 103 ? 4.200   -43.406 8.796   1.00 152.94 ? 172  THR   D CB  1 
ATOM   9552  O  OG1 . THR   D 1 103 ? 5.549   -42.948 8.958   1.00 151.17 ? 172  THR   D OG1 1 
ATOM   9553  C  CG2 . THR   D 1 103 ? 4.036   -44.774 9.490   1.00 148.12 ? 172  THR   D CG2 1 
ATOM   9554  N  N   . GLN   D 1 104 ? 3.010   -45.717 6.946   1.00 161.57 ? 173  GLN   D N   1 
ATOM   9555  C  CA  . GLN   D 1 104 ? 1.981   -46.742 6.876   1.00 170.97 ? 173  GLN   D CA  1 
ATOM   9556  C  C   . GLN   D 1 104 ? 1.694   -47.284 8.272   1.00 180.37 ? 173  GLN   D C   1 
ATOM   9557  O  O   . GLN   D 1 104 ? 2.529   -47.209 9.178   1.00 179.62 ? 173  GLN   D O   1 
ATOM   9558  C  CB  . GLN   D 1 104 ? 2.406   -47.880 5.943   1.00 171.63 ? 173  GLN   D CB  1 
ATOM   9559  N  N   . SER   D 1 105 ? 0.481   -47.813 8.447   1.00 191.59 ? 174  SER   D N   1 
ATOM   9560  C  CA  . SER   D 1 105 ? 0.177   -48.537 9.677   1.00 192.44 ? 174  SER   D CA  1 
ATOM   9561  C  C   . SER   D 1 105 ? 1.116   -49.725 9.846   1.00 196.80 ? 174  SER   D C   1 
ATOM   9562  O  O   . SER   D 1 105 ? 1.518   -50.056 10.969  1.00 199.48 ? 174  SER   D O   1 
ATOM   9563  C  CB  . SER   D 1 105 ? -1.279  -48.994 9.671   1.00 190.01 ? 174  SER   D CB  1 
ATOM   9564  O  OG  . SER   D 1 105 ? -1.542  -49.786 8.526   1.00 195.37 ? 174  SER   D OG  1 
ATOM   9565  N  N   . ASP   D 1 106 ? 1.478   -50.375 8.732   1.00 202.73 ? 175  ASP   D N   1 
ATOM   9566  C  CA  . ASP   D 1 106 ? 2.469   -51.448 8.768   1.00 200.02 ? 175  ASP   D CA  1 
ATOM   9567  C  C   . ASP   D 1 106 ? 3.797   -50.949 9.337   1.00 200.24 ? 175  ASP   D C   1 
ATOM   9568  O  O   . ASP   D 1 106 ? 4.417   -51.614 10.177  1.00 199.67 ? 175  ASP   D O   1 
ATOM   9569  C  CB  . ASP   D 1 106 ? 2.658   -52.027 7.362   1.00 193.30 ? 175  ASP   D CB  1 
ATOM   9570  N  N   . GLY   D 1 107 ? 4.239   -49.770 8.899   1.00 190.00 ? 176  GLY   D N   1 
ATOM   9571  C  CA  . GLY   D 1 107 ? 5.473   -49.171 9.369   1.00 180.12 ? 176  GLY   D CA  1 
ATOM   9572  C  C   . GLY   D 1 107 ? 6.307   -48.605 8.238   1.00 177.07 ? 176  GLY   D C   1 
ATOM   9573  O  O   . GLY   D 1 107 ? 6.786   -47.467 8.307   1.00 171.25 ? 176  GLY   D O   1 
ATOM   9574  N  N   . ILE   D 1 108 ? 6.479   -49.399 7.182   1.00 187.95 ? 177  ILE   D N   1 
ATOM   9575  C  CA  . ILE   D 1 108 ? 7.295   -49.024 6.031   1.00 185.69 ? 177  ILE   D CA  1 
ATOM   9576  C  C   . ILE   D 1 108 ? 6.796   -47.642 5.622   1.00 183.30 ? 177  ILE   D C   1 
ATOM   9577  O  O   . ILE   D 1 108 ? 5.611   -47.459 5.313   1.00 185.90 ? 177  ILE   D O   1 
ATOM   9578  C  CB  . ILE   D 1 108 ? 7.223   -50.103 4.934   1.00 186.97 ? 177  ILE   D CB  1 
ATOM   9579  C  CG1 . ILE   D 1 108 ? 7.898   -51.402 5.394   1.00 183.71 ? 177  ILE   D CG1 1 
ATOM   9580  C  CG2 . ILE   D 1 108 ? 7.828   -49.577 3.642   1.00 179.70 ? 177  ILE   D CG2 1 
ATOM   9581  C  CD1 . ILE   D 1 108 ? 6.922   -52.503 5.763   1.00 181.38 ? 177  ILE   D CD1 1 
ATOM   9582  N  N   . GLN   D 1 109 ? 7.697   -46.663 5.596   1.00 159.63 ? 178  GLN   D N   1 
ATOM   9583  C  CA  . GLN   D 1 109 ? 7.303   -45.302 5.267   1.00 148.06 ? 178  GLN   D CA  1 
ATOM   9584  C  C   . GLN   D 1 109 ? 7.417   -45.188 3.753   1.00 140.82 ? 178  GLN   D C   1 
ATOM   9585  O  O   . GLN   D 1 109 ? 8.301   -45.785 3.130   1.00 138.29 ? 178  GLN   D O   1 
ATOM   9586  C  CB  . GLN   D 1 109 ? 8.198   -44.260 5.938   1.00 140.83 ? 178  GLN   D CB  1 
ATOM   9587  C  CG  . GLN   D 1 109 ? 7.444   -43.123 6.635   1.00 140.47 ? 178  GLN   D CG  1 
ATOM   9588  C  CD  . GLN   D 1 109 ? 8.284   -42.434 7.699   1.00 132.57 ? 178  GLN   D CD  1 
ATOM   9589  O  OE1 . GLN   D 1 109 ? 9.492   -42.653 7.785   1.00 126.56 ? 178  GLN   D OE1 1 
ATOM   9590  N  NE2 . GLN   D 1 109 ? 7.645   -41.608 8.522   1.00 131.40 ? 178  GLN   D NE2 1 
ATOM   9591  N  N   . GLN   D 1 110 ? 6.506   -44.423 3.163   1.00 140.70 ? 179  GLN   D N   1 
ATOM   9592  C  CA  . GLN   D 1 110 ? 6.620   -43.992 1.778   1.00 139.52 ? 179  GLN   D CA  1 
ATOM   9593  C  C   . GLN   D 1 110 ? 6.980   -42.508 1.723   1.00 134.93 ? 179  GLN   D C   1 
ATOM   9594  O  O   . GLN   D 1 110 ? 6.687   -41.745 2.649   1.00 135.04 ? 179  GLN   D O   1 
ATOM   9595  C  CB  . GLN   D 1 110 ? 5.323   -44.256 1.009   1.00 140.13 ? 179  GLN   D CB  1 
ATOM   9596  C  CG  . GLN   D 1 110 ? 5.105   -45.721 0.670   1.00 140.43 ? 179  GLN   D CG  1 
ATOM   9597  C  CD  . GLN   D 1 110 ? 4.397   -45.906 -0.666  1.00 149.74 ? 179  GLN   D CD  1 
ATOM   9598  O  OE1 . GLN   D 1 110 ? 3.174   -45.769 -0.756  1.00 154.06 ? 179  GLN   D OE1 1 
ATOM   9599  N  NE2 . GLN   D 1 110 ? 5.166   -46.209 -1.716  1.00 142.60 ? 179  GLN   D NE2 1 
ATOM   9600  N  N   . ALA   D 1 111 ? 7.617   -42.098 0.626   1.00 124.85 ? 180  ALA   D N   1 
ATOM   9601  C  CA  . ALA   D 1 111 ? 8.134   -40.738 0.522   1.00 121.99 ? 180  ALA   D CA  1 
ATOM   9602  C  C   . ALA   D 1 111 ? 7.877   -40.147 -0.859  1.00 115.84 ? 180  ALA   D C   1 
ATOM   9603  O  O   . ALA   D 1 111 ? 8.242   -40.741 -1.878  1.00 113.30 ? 180  ALA   D O   1 
ATOM   9604  C  CB  . ALA   D 1 111 ? 9.632   -40.708 0.831   1.00 118.99 ? 180  ALA   D CB  1 
ATOM   9605  N  N   . LYS   D 1 112 ? 7.236   -38.980 -0.884  1.00 113.89 ? 181  LYS   D N   1 
ATOM   9606  C  CA  . LYS   D 1 112 ? 7.188   -38.171 -2.096  1.00 112.07 ? 181  LYS   D CA  1 
ATOM   9607  C  C   . LYS   D 1 112 ? 8.540   -37.486 -2.242  1.00 111.40 ? 181  LYS   D C   1 
ATOM   9608  O  O   . LYS   D 1 112 ? 8.926   -36.649 -1.419  1.00 106.92 ? 181  LYS   D O   1 
ATOM   9609  C  CB  . LYS   D 1 112 ? 6.043   -37.160 -2.052  1.00 106.63 ? 181  LYS   D CB  1 
ATOM   9610  N  N   . VAL   D 1 113 ? 9.269   -37.878 -3.274  1.00 112.64 ? 182  VAL   D N   1 
ATOM   9611  C  CA  . VAL   D 1 113 ? 10.674  -37.552 -3.433  1.00 106.93 ? 182  VAL   D CA  1 
ATOM   9612  C  C   . VAL   D 1 113 ? 10.832  -36.755 -4.715  1.00 109.94 ? 182  VAL   D C   1 
ATOM   9613  O  O   . VAL   D 1 113 ? 10.224  -37.081 -5.739  1.00 115.04 ? 182  VAL   D O   1 
ATOM   9614  C  CB  . VAL   D 1 113 ? 11.523  -38.841 -3.458  1.00 109.38 ? 182  VAL   D CB  1 
ATOM   9615  C  CG1 . VAL   D 1 113 ? 12.794  -38.650 -4.252  1.00 106.22 ? 182  VAL   D CG1 1 
ATOM   9616  C  CG2 . VAL   D 1 113 ? 11.832  -39.277 -2.037  1.00 109.86 ? 182  VAL   D CG2 1 
ATOM   9617  N  N   . GLN   D 1 114 ? 11.616  -35.690 -4.642  1.00 111.97 ? 183  GLN   D N   1 
ATOM   9618  C  CA  . GLN   D 1 114 ? 11.982  -34.871 -5.793  1.00 112.02 ? 183  GLN   D CA  1 
ATOM   9619  C  C   . GLN   D 1 114 ? 13.440  -35.201 -6.094  1.00 107.94 ? 183  GLN   D C   1 
ATOM   9620  O  O   . GLN   D 1 114 ? 14.334  -34.800 -5.343  1.00 106.61 ? 183  GLN   D O   1 
ATOM   9621  C  CB  . GLN   D 1 114 ? 11.777  -33.388 -5.487  1.00 110.02 ? 183  GLN   D CB  1 
ATOM   9622  C  CG  . GLN   D 1 114 ? 12.062  -32.435 -6.656  1.00 120.39 ? 183  GLN   D CG  1 
ATOM   9623  C  CD  . GLN   D 1 114 ? 10.807  -32.077 -7.450  1.00 128.31 ? 183  GLN   D CD  1 
ATOM   9624  O  OE1 . GLN   D 1 114 ? 10.562  -32.617 -8.534  1.00 128.45 ? 183  GLN   D OE1 1 
ATOM   9625  N  NE2 . GLN   D 1 114 ? 10.005  -31.161 -6.907  1.00 130.46 ? 183  GLN   D NE2 1 
ATOM   9626  N  N   . ILE   D 1 115 ? 13.676  -35.961 -7.171  1.00 111.60 ? 184  ILE   D N   1 
ATOM   9627  C  CA  . ILE   D 1 115 ? 15.043  -36.326 -7.534  1.00 111.43 ? 184  ILE   D CA  1 
ATOM   9628  C  C   . ILE   D 1 115 ? 15.818  -35.060 -7.856  1.00 109.97 ? 184  ILE   D C   1 
ATOM   9629  O  O   . ILE   D 1 115 ? 15.421  -34.281 -8.725  1.00 120.25 ? 184  ILE   D O   1 
ATOM   9630  C  CB  . ILE   D 1 115 ? 15.053  -37.301 -8.716  1.00 116.75 ? 184  ILE   D CB  1 
ATOM   9631  C  CG1 . ILE   D 1 115 ? 14.306  -38.579 -8.365  1.00 110.49 ? 184  ILE   D CG1 1 
ATOM   9632  C  CG2 . ILE   D 1 115 ? 16.495  -37.645 -9.099  1.00 114.51 ? 184  ILE   D CG2 1 
ATOM   9633  C  CD1 . ILE   D 1 115 ? 15.158  -39.568 -7.622  1.00 100.08 ? 184  ILE   D CD1 1 
ATOM   9634  N  N   . LEU   D 1 116 ? 16.917  -34.834 -7.148  1.00 106.04 ? 185  LEU   D N   1 
ATOM   9635  C  CA  . LEU   D 1 116 ? 17.687  -33.630 -7.385  1.00 105.73 ? 185  LEU   D CA  1 
ATOM   9636  C  C   . LEU   D 1 116 ? 18.295  -33.683 -8.778  1.00 111.59 ? 185  LEU   D C   1 
ATOM   9637  O  O   . LEU   D 1 116 ? 18.393  -34.750 -9.383  1.00 117.29 ? 185  LEU   D O   1 
ATOM   9638  C  CB  . LEU   D 1 116 ? 18.797  -33.465 -6.352  1.00 101.57 ? 185  LEU   D CB  1 
ATOM   9639  C  CG  . LEU   D 1 116 ? 18.353  -33.343 -4.898  1.00 98.65  ? 185  LEU   D CG  1 
ATOM   9640  C  CD1 . LEU   D 1 116 ? 19.459  -32.683 -4.103  1.00 99.40  ? 185  LEU   D CD1 1 
ATOM   9641  C  CD2 . LEU   D 1 116 ? 17.051  -32.557 -4.795  1.00 101.02 ? 185  LEU   D CD2 1 
ATOM   9642  N  N   . PRO   D 1 117 ? 18.708  -32.539 -9.307  1.00 113.01 ? 186  PRO   D N   1 
ATOM   9643  C  CA  . PRO   D 1 117 ? 19.188  -32.495 -10.691 1.00 117.58 ? 186  PRO   D CA  1 
ATOM   9644  C  C   . PRO   D 1 117 ? 20.574  -33.100 -10.849 1.00 114.41 ? 186  PRO   D C   1 
ATOM   9645  O  O   . PRO   D 1 117 ? 21.414  -33.026 -9.948  1.00 111.13 ? 186  PRO   D O   1 
ATOM   9646  C  CB  . PRO   D 1 117 ? 19.197  -30.995 -11.011 1.00 116.45 ? 186  PRO   D CB  1 
ATOM   9647  C  CG  . PRO   D 1 117 ? 19.371  -30.325 -9.671  1.00 110.36 ? 186  PRO   D CG  1 
ATOM   9648  C  CD  . PRO   D 1 117 ? 18.667  -31.208 -8.671  1.00 109.14 ? 186  PRO   D CD  1 
ATOM   9649  N  N   . GLU   D 1 118 ? 20.799  -33.716 -12.024 1.00 118.68 ? 187  GLU   D N   1 
ATOM   9650  C  CA  . GLU   D 1 118 ? 22.145  -34.072 -12.503 1.00 112.79 ? 187  GLU   D CA  1 
ATOM   9651  C  C   . GLU   D 1 118 ? 22.297  -33.518 -13.921 1.00 107.69 ? 187  GLU   D C   1 
ATOM   9652  O  O   . GLU   D 1 118 ? 22.177  -34.246 -14.914 1.00 107.71 ? 187  GLU   D O   1 
ATOM   9653  C  CB  . GLU   D 1 118 ? 22.419  -35.582 -12.443 1.00 107.32 ? 187  GLU   D CB  1 
ATOM   9654  C  CG  . GLU   D 1 118 ? 23.418  -35.970 -11.323 1.00 105.53 ? 187  GLU   D CG  1 
ATOM   9655  C  CD  . GLU   D 1 118 ? 24.889  -35.627 -11.640 1.00 103.90 ? 187  GLU   D CD  1 
ATOM   9656  O  OE1 . GLU   D 1 118 ? 25.584  -35.031 -10.780 1.00 101.15 ? 187  GLU   D OE1 1 
ATOM   9657  O  OE2 . GLU   D 1 118 ? 25.354  -35.972 -12.755 1.00 106.76 ? 187  GLU   D OE2 1 
ATOM   9658  N  N   . CYS   D 1 119 ? 22.602  -32.225 -13.992 1.00 100.17 ? 188  CYS   D N   1 
ATOM   9659  C  CA  . CYS   D 1 119 ? 22.752  -31.520 -15.255 1.00 99.95  ? 188  CYS   D CA  1 
ATOM   9660  C  C   . CYS   D 1 119 ? 24.011  -31.996 -15.963 1.00 99.33  ? 188  CYS   D C   1 
ATOM   9661  O  O   . CYS   D 1 119 ? 25.105  -31.956 -15.387 1.00 97.21  ? 188  CYS   D O   1 
ATOM   9662  C  CB  . CYS   D 1 119 ? 22.822  -30.013 -15.015 1.00 92.90  ? 188  CYS   D CB  1 
ATOM   9663  S  SG  . CYS   D 1 119 ? 21.481  -29.361 -13.995 1.00 105.37 ? 188  CYS   D SG  1 
ATOM   9664  N  N   . VAL   D 1 120 ? 23.857  -32.463 -17.205 1.00 98.51  ? 189  VAL   D N   1 
ATOM   9665  C  CA  . VAL   D 1 120 ? 24.972  -32.866 -18.055 1.00 87.20  ? 189  VAL   D CA  1 
ATOM   9666  C  C   . VAL   D 1 120 ? 25.107  -31.798 -19.117 1.00 83.90  ? 189  VAL   D C   1 
ATOM   9667  O  O   . VAL   D 1 120 ? 24.112  -31.417 -19.732 1.00 89.19  ? 189  VAL   D O   1 
ATOM   9668  C  CB  . VAL   D 1 120 ? 24.735  -34.256 -18.673 1.00 86.06  ? 189  VAL   D CB  1 
ATOM   9669  C  CG1 . VAL   D 1 120 ? 26.051  -34.873 -19.081 1.00 86.14  ? 189  VAL   D CG1 1 
ATOM   9670  C  CG2 . VAL   D 1 120 ? 24.007  -35.185 -17.688 1.00 91.18  ? 189  VAL   D CG2 1 
ATOM   9671  N  N   . LEU   D 1 121 ? 26.322  -31.281 -19.302 1.00 83.91  ? 190  LEU   D N   1 
ATOM   9672  C  CA  . LEU   D 1 121 ? 26.540  -30.155 -20.206 1.00 82.75  ? 190  LEU   D CA  1 
ATOM   9673  C  C   . LEU   D 1 121 ? 27.497  -30.512 -21.334 1.00 86.04  ? 190  LEU   D C   1 
ATOM   9674  O  O   . LEU   D 1 121 ? 28.534  -31.153 -21.100 1.00 87.18  ? 190  LEU   D O   1 
ATOM   9675  C  CB  . LEU   D 1 121 ? 27.131  -28.941 -19.468 1.00 82.26  ? 190  LEU   D CB  1 
ATOM   9676  C  CG  . LEU   D 1 121 ? 26.260  -28.244 -18.457 1.00 80.38  ? 190  LEU   D CG  1 
ATOM   9677  C  CD1 . LEU   D 1 121 ? 27.069  -27.115 -17.898 1.00 86.06  ? 190  LEU   D CD1 1 
ATOM   9678  C  CD2 . LEU   D 1 121 ? 25.042  -27.726 -19.159 1.00 83.69  ? 190  LEU   D CD2 1 
ATOM   9679  N  N   . PRO   D 1 122 ? 27.211  -30.062 -22.546 1.00 83.59  ? 191  PRO   D N   1 
ATOM   9680  C  CA  . PRO   D 1 122 ? 28.118  -30.330 -23.665 1.00 85.93  ? 191  PRO   D CA  1 
ATOM   9681  C  C   . PRO   D 1 122 ? 29.462  -29.665 -23.443 1.00 85.75  ? 191  PRO   D C   1 
ATOM   9682  O  O   . PRO   D 1 122 ? 29.646  -28.855 -22.537 1.00 89.97  ? 191  PRO   D O   1 
ATOM   9683  C  CB  . PRO   D 1 122 ? 27.391  -29.723 -24.869 1.00 96.54  ? 191  PRO   D CB  1 
ATOM   9684  C  CG  . PRO   D 1 122 ? 26.528  -28.621 -24.263 1.00 98.38  ? 191  PRO   D CG  1 
ATOM   9685  C  CD  . PRO   D 1 122 ? 26.112  -29.147 -22.906 1.00 89.77  ? 191  PRO   D CD  1 
ATOM   9686  N  N   . SER   D 1 123 ? 30.413  -29.989 -24.313 1.00 87.46  ? 192  SER   D N   1 
ATOM   9687  C  CA  . SER   D 1 123 ? 31.661  -29.237 -24.308 1.00 88.17  ? 192  SER   D CA  1 
ATOM   9688  C  C   . SER   D 1 123 ? 31.370  -27.763 -24.530 1.00 91.28  ? 192  SER   D C   1 
ATOM   9689  O  O   . SER   D 1 123 ? 30.540  -27.395 -25.367 1.00 94.08  ? 192  SER   D O   1 
ATOM   9690  C  CB  . SER   D 1 123 ? 32.604  -29.734 -25.388 1.00 93.36  ? 192  SER   D CB  1 
ATOM   9691  O  OG  . SER   D 1 123 ? 33.571  -28.740 -25.676 1.00 91.10  ? 192  SER   D OG  1 
ATOM   9692  N  N   . THR   D 1 124 ? 32.062  -26.908 -23.785 1.00 93.38  ? 193  THR   D N   1 
ATOM   9693  C  CA  . THR   D 1 124 ? 31.839  -25.481 -23.967 1.00 94.63  ? 193  THR   D CA  1 
ATOM   9694  C  C   . THR   D 1 124 ? 32.014  -25.064 -25.415 1.00 95.59  ? 193  THR   D C   1 
ATOM   9695  O  O   . THR   D 1 124 ? 31.320  -24.152 -25.885 1.00 96.46  ? 193  THR   D O   1 
ATOM   9696  C  CB  . THR   D 1 124 ? 32.773  -24.663 -23.073 1.00 94.52  ? 193  THR   D CB  1 
ATOM   9697  O  OG1 . THR   D 1 124 ? 34.089  -25.243 -23.075 1.00 99.22  ? 193  THR   D OG1 1 
ATOM   9698  C  CG2 . THR   D 1 124 ? 32.209  -24.606 -21.653 1.00 92.35  ? 193  THR   D CG2 1 
ATOM   9699  N  N   . MET   D 1 125 ? 32.918  -25.721 -26.146 1.00 94.90  ? 194  MET   D N   1 
ATOM   9700  C  CA  . MET   D 1 125 ? 33.155  -25.330 -27.530 1.00 95.38  ? 194  MET   D CA  1 
ATOM   9701  C  C   . MET   D 1 125 ? 32.066  -25.816 -28.480 1.00 95.22  ? 194  MET   D C   1 
ATOM   9702  O  O   . MET   D 1 125 ? 31.985  -25.316 -29.608 1.00 95.66  ? 194  MET   D O   1 
ATOM   9703  C  CB  . MET   D 1 125 ? 34.520  -25.836 -27.995 1.00 92.34  ? 194  MET   D CB  1 
ATOM   9704  C  CG  . MET   D 1 125 ? 35.710  -25.278 -27.200 1.00 95.81  ? 194  MET   D CG  1 
ATOM   9705  S  SD  . MET   D 1 125 ? 36.084  -23.497 -27.389 1.00 90.84  ? 194  MET   D SD  1 
ATOM   9706  C  CE  . MET   D 1 125 ? 34.797  -22.798 -26.338 1.00 85.67  ? 194  MET   D CE  1 
ATOM   9707  N  N   . SER   D 1 126 ? 31.222  -26.754 -28.040 1.00 95.16  ? 195  SER   D N   1 
ATOM   9708  C  CA  . SER   D 1 126 ? 30.162  -27.274 -28.899 1.00 95.93  ? 195  SER   D CA  1 
ATOM   9709  C  C   . SER   D 1 126 ? 29.444  -26.144 -29.632 1.00 97.03  ? 195  SER   D C   1 
ATOM   9710  O  O   . SER   D 1 126 ? 29.269  -26.195 -30.855 1.00 102.29 ? 195  SER   D O   1 
ATOM   9711  C  CB  . SER   D 1 126 ? 29.169  -28.108 -28.073 1.00 97.76  ? 195  SER   D CB  1 
ATOM   9712  O  OG  . SER   D 1 126 ? 28.431  -27.298 -27.164 1.00 98.54  ? 195  SER   D OG  1 
ATOM   9713  N  N   . ALA   D 1 127 ? 29.074  -25.086 -28.906 1.00 95.86  ? 196  ALA   D N   1 
ATOM   9714  C  CA  . ALA   D 1 127 ? 28.245  -24.035 -29.489 1.00 97.23  ? 196  ALA   D CA  1 
ATOM   9715  C  C   . ALA   D 1 127 ? 29.027  -23.148 -30.460 1.00 99.32  ? 196  ALA   D C   1 
ATOM   9716  O  O   . ALA   D 1 127 ? 28.476  -22.682 -31.467 1.00 97.54  ? 196  ALA   D O   1 
ATOM   9717  C  CB  . ALA   D 1 127 ? 27.615  -23.192 -28.380 1.00 91.81  ? 196  ALA   D CB  1 
ATOM   9718  N  N   . VAL   D 1 128 ? 30.293  -22.875 -30.184 1.00 101.38 ? 197  VAL   D N   1 
ATOM   9719  C  CA  . VAL   D 1 128 ? 31.067  -22.003 -31.057 1.00 102.43 ? 197  VAL   D CA  1 
ATOM   9720  C  C   . VAL   D 1 128 ? 32.053  -22.804 -31.914 1.00 106.55 ? 197  VAL   D C   1 
ATOM   9721  O  O   . VAL   D 1 128 ? 33.043  -22.257 -32.408 1.00 104.31 ? 197  VAL   D O   1 
ATOM   9722  C  CB  . VAL   D 1 128 ? 31.772  -20.885 -30.263 1.00 100.32 ? 197  VAL   D CB  1 
ATOM   9723  C  CG1 . VAL   D 1 128 ? 30.822  -20.318 -29.227 1.00 98.87  ? 197  VAL   D CG1 1 
ATOM   9724  C  CG2 . VAL   D 1 128 ? 33.061  -21.367 -29.610 1.00 100.87 ? 197  VAL   D CG2 1 
ATOM   9725  N  N   . GLN   D 1 129 ? 31.797  -24.094 -32.107 1.00 105.88 ? 198  GLN   D N   1 
ATOM   9726  C  CA  . GLN   D 1 129 ? 32.673  -24.868 -32.968 1.00 104.77 ? 198  GLN   D CA  1 
ATOM   9727  C  C   . GLN   D 1 129 ? 32.485  -24.431 -34.411 1.00 107.71 ? 198  GLN   D C   1 
ATOM   9728  O  O   . GLN   D 1 129 ? 31.361  -24.201 -34.871 1.00 109.17 ? 198  GLN   D O   1 
ATOM   9729  C  CB  . GLN   D 1 129 ? 32.410  -26.370 -32.825 1.00 105.79 ? 198  GLN   D CB  1 
ATOM   9730  C  CG  . GLN   D 1 129 ? 33.563  -27.119 -32.151 1.00 107.67 ? 198  GLN   D CG  1 
ATOM   9731  C  CD  . GLN   D 1 129 ? 34.920  -26.777 -32.744 1.00 106.10 ? 198  GLN   D CD  1 
ATOM   9732  O  OE1 . GLN   D 1 129 ? 35.086  -26.740 -33.959 1.00 106.06 ? 198  GLN   D OE1 1 
ATOM   9733  N  NE2 . GLN   D 1 129 ? 35.899  -26.508 -31.879 1.00 105.17 ? 198  GLN   D NE2 1 
ATOM   9734  N  N   . LEU   D 1 130 ? 33.603  -24.292 -35.117 1.00 107.83 ? 199  LEU   D N   1 
ATOM   9735  C  CA  . LEU   D 1 130 ? 33.598  -24.028 -36.550 1.00 107.57 ? 199  LEU   D CA  1 
ATOM   9736  C  C   . LEU   D 1 130 ? 33.442  -25.340 -37.315 1.00 109.92 ? 199  LEU   D C   1 
ATOM   9737  O  O   . LEU   D 1 130 ? 34.276  -26.245 -37.197 1.00 106.77 ? 199  LEU   D O   1 
ATOM   9738  C  CB  . LEU   D 1 130 ? 34.880  -23.315 -36.974 1.00 102.13 ? 199  LEU   D CB  1 
ATOM   9739  C  CG  . LEU   D 1 130 ? 34.980  -21.817 -36.716 1.00 96.69  ? 199  LEU   D CG  1 
ATOM   9740  C  CD1 . LEU   D 1 130 ? 35.993  -21.218 -37.669 1.00 93.87  ? 199  LEU   D CD1 1 
ATOM   9741  C  CD2 . LEU   D 1 130 ? 33.618  -21.176 -36.907 1.00 95.74  ? 199  LEU   D CD2 1 
ATOM   9742  N  N   . GLU   D 1 131 ? 32.379  -25.426 -38.109 1.00 114.11 ? 200  GLU   D N   1 
ATOM   9743  C  CA  . GLU   D 1 131 ? 32.090  -26.616 -38.895 1.00 114.88 ? 200  GLU   D CA  1 
ATOM   9744  C  C   . GLU   D 1 131 ? 33.335  -27.208 -39.548 1.00 114.91 ? 200  GLU   D C   1 
ATOM   9745  O  O   . GLU   D 1 131 ? 33.564  -28.421 -39.468 1.00 119.58 ? 200  GLU   D O   1 
ATOM   9746  C  CB  . GLU   D 1 131 ? 31.037  -26.269 -39.951 1.00 118.41 ? 200  GLU   D CB  1 
ATOM   9747  C  CG  . GLU   D 1 131 ? 30.596  -27.471 -40.798 1.00 120.77 ? 200  GLU   D CG  1 
ATOM   9748  C  CD  . GLU   D 1 131 ? 29.510  -27.136 -41.820 1.00 121.33 ? 200  GLU   D CD  1 
ATOM   9749  O  OE1 . GLU   D 1 131 ? 29.115  -25.945 -41.904 1.00 121.93 ? 200  GLU   D OE1 1 
ATOM   9750  O  OE2 . GLU   D 1 131 ? 29.049  -28.063 -42.535 1.00 117.98 ? 200  GLU   D OE2 1 
ATOM   9751  N  N   . SER   D 1 132 ? 34.155  -26.374 -40.200 1.00 104.27 ? 201  SER   D N   1 
ATOM   9752  C  CA  . SER   D 1 132 ? 35.341  -26.898 -40.877 1.00 104.57 ? 201  SER   D CA  1 
ATOM   9753  C  C   . SER   D 1 132 ? 36.276  -27.593 -39.905 1.00 108.61 ? 201  SER   D C   1 
ATOM   9754  O  O   . SER   D 1 132 ? 36.952  -28.563 -40.270 1.00 109.59 ? 201  SER   D O   1 
ATOM   9755  C  CB  . SER   D 1 132 ? 36.094  -25.785 -41.595 1.00 98.14  ? 201  SER   D CB  1 
ATOM   9756  O  OG  . SER   D 1 132 ? 36.894  -25.065 -40.685 1.00 98.68  ? 201  SER   D OG  1 
ATOM   9757  N  N   . LEU   D 1 133 ? 36.320  -27.115 -38.660 1.00 110.21 ? 202  LEU   D N   1 
ATOM   9758  C  CA  . LEU   D 1 133 ? 37.189  -27.665 -37.632 1.00 108.62 ? 202  LEU   D CA  1 
ATOM   9759  C  C   . LEU   D 1 133 ? 36.600  -28.889 -36.948 1.00 108.42 ? 202  LEU   D C   1 
ATOM   9760  O  O   . LEU   D 1 133 ? 37.320  -29.566 -36.208 1.00 111.30 ? 202  LEU   D O   1 
ATOM   9761  C  CB  . LEU   D 1 133 ? 37.491  -26.588 -36.592 1.00 106.42 ? 202  LEU   D CB  1 
ATOM   9762  C  CG  . LEU   D 1 133 ? 38.748  -25.772 -36.872 1.00 103.05 ? 202  LEU   D CG  1 
ATOM   9763  C  CD1 . LEU   D 1 133 ? 38.840  -25.407 -38.343 1.00 99.40  ? 202  LEU   D CD1 1 
ATOM   9764  C  CD2 . LEU   D 1 133 ? 38.724  -24.537 -35.999 1.00 103.86 ? 202  LEU   D CD2 1 
ATOM   9765  N  N   . ASN   D 1 134 ? 35.314  -29.179 -37.163 1.00 110.00 ? 203  ASN   D N   1 
ATOM   9766  C  CA  . ASN   D 1 134 ? 34.686  -30.284 -36.451 1.00 110.45 ? 203  ASN   D CA  1 
ATOM   9767  C  C   . ASN   D 1 134 ? 35.426  -31.593 -36.694 1.00 112.63 ? 203  ASN   D C   1 
ATOM   9768  O  O   . ASN   D 1 134 ? 35.493  -32.435 -35.792 1.00 114.16 ? 203  ASN   D O   1 
ATOM   9769  C  CB  . ASN   D 1 134 ? 33.207  -30.393 -36.849 1.00 110.28 ? 203  ASN   D CB  1 
ATOM   9770  C  CG  . ASN   D 1 134 ? 32.328  -29.358 -36.141 1.00 110.25 ? 203  ASN   D CG  1 
ATOM   9771  O  OD1 . ASN   D 1 134 ? 32.446  -28.159 -36.386 1.00 117.84 ? 203  ASN   D OD1 1 
ATOM   9772  N  ND2 . ASN   D 1 134 ? 31.448  -29.821 -35.261 1.00 107.23 ? 203  ASN   D ND2 1 
ATOM   9773  N  N   . LYS   D 1 135 ? 36.017  -31.763 -37.886 1.00 113.99 ? 204  LYS   D N   1 
ATOM   9774  C  CA  . LYS   D 1 135 ? 36.729  -32.999 -38.219 1.00 112.36 ? 204  LYS   D CA  1 
ATOM   9775  C  C   . LYS   D 1 135 ? 37.925  -33.251 -37.296 1.00 115.82 ? 204  LYS   D C   1 
ATOM   9776  O  O   . LYS   D 1 135 ? 38.224  -34.403 -36.964 1.00 120.19 ? 204  LYS   D O   1 
ATOM   9777  C  CB  . LYS   D 1 135 ? 37.188  -32.958 -39.678 1.00 106.32 ? 204  LYS   D CB  1 
ATOM   9778  N  N   . CYS   D 1 136 ? 38.615  -32.199 -36.870 1.00 118.32 ? 205  CYS   D N   1 
ATOM   9779  C  CA  . CYS   D 1 136 ? 39.821  -32.305 -36.056 1.00 122.08 ? 205  CYS   D CA  1 
ATOM   9780  C  C   . CYS   D 1 136 ? 39.535  -32.464 -34.562 1.00 126.82 ? 205  CYS   D C   1 
ATOM   9781  O  O   . CYS   D 1 136 ? 40.462  -32.350 -33.748 1.00 127.94 ? 205  CYS   D O   1 
ATOM   9782  C  CB  . CYS   D 1 136 ? 40.702  -31.071 -36.278 1.00 124.75 ? 205  CYS   D CB  1 
ATOM   9783  S  SG  . CYS   D 1 136 ? 40.955  -30.638 -38.024 1.00 122.38 ? 205  CYS   D SG  1 
ATOM   9784  N  N   . GLN   D 1 137 ? 38.286  -32.720 -34.183 1.00 126.06 ? 206  GLN   D N   1 
ATOM   9785  C  CA  . GLN   D 1 137 ? 37.909  -32.799 -32.786 1.00 127.18 ? 206  GLN   D CA  1 
ATOM   9786  C  C   . GLN   D 1 137 ? 38.079  -34.199 -32.200 1.00 135.51 ? 206  GLN   D C   1 
ATOM   9787  O  O   . GLN   D 1 137 ? 37.839  -34.394 -31.005 1.00 138.25 ? 206  GLN   D O   1 
ATOM   9788  C  CB  . GLN   D 1 137 ? 36.464  -32.324 -32.607 1.00 122.97 ? 206  GLN   D CB  1 
ATOM   9789  C  CG  . GLN   D 1 137 ? 36.301  -30.841 -32.817 1.00 122.40 ? 206  GLN   D CG  1 
ATOM   9790  C  CD  . GLN   D 1 137 ? 37.383  -30.051 -32.109 1.00 126.10 ? 206  GLN   D CD  1 
ATOM   9791  O  OE1 . GLN   D 1 137 ? 38.275  -29.486 -32.754 1.00 126.18 ? 206  GLN   D OE1 1 
ATOM   9792  N  NE2 . GLN   D 1 137 ? 37.321  -30.014 -30.772 1.00 120.44 ? 206  GLN   D NE2 1 
ATOM   9793  N  N   . ILE   D 1 138 ? 38.484  -35.178 -32.991 1.00 133.11 ? 207  ILE   D N   1 
ATOM   9794  C  CA  . ILE   D 1 138 ? 38.842  -36.481 -32.459 1.00 136.49 ? 207  ILE   D CA  1 
ATOM   9795  C  C   . ILE   D 1 138 ? 40.357  -36.500 -32.345 1.00 138.97 ? 207  ILE   D C   1 
ATOM   9796  O  O   . ILE   D 1 138 ? 41.063  -36.444 -33.356 1.00 136.88 ? 207  ILE   D O   1 
ATOM   9797  C  CB  . ILE   D 1 138 ? 38.330  -37.626 -33.338 1.00 136.12 ? 207  ILE   D CB  1 
ATOM   9798  C  CG1 . ILE   D 1 138 ? 36.796  -37.638 -33.373 1.00 139.10 ? 207  ILE   D CG1 1 
ATOM   9799  C  CG2 . ILE   D 1 138 ? 38.854  -38.949 -32.796 1.00 132.85 ? 207  ILE   D CG2 1 
ATOM   9800  C  CD1 . ILE   D 1 138 ? 36.149  -38.485 -32.284 1.00 133.34 ? 207  ILE   D CD1 1 
ATOM   9801  N  N   . PHE   D 1 139 ? 40.869  -36.557 -31.107 1.00 148.65 ? 208  PHE   D N   1 
ATOM   9802  C  CA  . PHE   D 1 139 ? 42.313  -36.482 -30.901 1.00 151.66 ? 208  PHE   D CA  1 
ATOM   9803  C  C   . PHE   D 1 139 ? 42.910  -37.875 -30.757 1.00 151.67 ? 208  PHE   D C   1 
ATOM   9804  O  O   . PHE   D 1 139 ? 42.285  -38.759 -30.163 1.00 153.20 ? 208  PHE   D O   1 
ATOM   9805  C  CB  . PHE   D 1 139 ? 42.646  -35.664 -29.652 1.00 151.74 ? 208  PHE   D CB  1 
ATOM   9806  C  CG  . PHE   D 1 139 ? 41.834  -34.409 -29.503 1.00 151.44 ? 208  PHE   D CG  1 
ATOM   9807  C  CD1 . PHE   D 1 139 ? 41.862  -33.412 -30.483 1.00 150.56 ? 208  PHE   D CD1 1 
ATOM   9808  C  CD2 . PHE   D 1 139 ? 41.054  -34.222 -28.380 1.00 149.52 ? 208  PHE   D CD2 1 
ATOM   9809  C  CE1 . PHE   D 1 139 ? 41.114  -32.256 -30.338 1.00 146.34 ? 208  PHE   D CE1 1 
ATOM   9810  C  CE2 . PHE   D 1 139 ? 40.306  -33.071 -28.220 1.00 149.64 ? 208  PHE   D CE2 1 
ATOM   9811  C  CZ  . PHE   D 1 139 ? 40.332  -32.084 -29.203 1.00 147.84 ? 208  PHE   D CZ  1 
ATOM   9812  N  N   . PRO   D 1 140 ? 44.107  -38.117 -31.284 1.00 139.08 ? 209  PRO   D N   1 
ATOM   9813  C  CA  . PRO   D 1 140 ? 44.714  -39.443 -31.125 1.00 138.82 ? 209  PRO   D CA  1 
ATOM   9814  C  C   . PRO   D 1 140 ? 44.866  -39.777 -29.646 1.00 144.45 ? 209  PRO   D C   1 
ATOM   9815  O  O   . PRO   D 1 140 ? 45.036  -38.890 -28.803 1.00 143.53 ? 209  PRO   D O   1 
ATOM   9816  C  CB  . PRO   D 1 140 ? 46.069  -39.304 -31.831 1.00 134.10 ? 209  PRO   D CB  1 
ATOM   9817  C  CG  . PRO   D 1 140 ? 45.878  -38.165 -32.804 1.00 125.31 ? 209  PRO   D CG  1 
ATOM   9818  C  CD  . PRO   D 1 140 ? 44.890  -37.235 -32.168 1.00 130.65 ? 209  PRO   D CD  1 
ATOM   9819  N  N   . SER   D 1 141 ? 44.775  -41.072 -29.330 1.00 147.75 ? 210  SER   D N   1 
ATOM   9820  C  CA  . SER   D 1 141 ? 44.790  -41.515 -27.936 1.00 150.42 ? 210  SER   D CA  1 
ATOM   9821  C  C   . SER   D 1 141 ? 46.023  -40.989 -27.212 1.00 149.72 ? 210  SER   D C   1 
ATOM   9822  O  O   . SER   D 1 141 ? 47.098  -40.831 -27.804 1.00 149.19 ? 210  SER   D O   1 
ATOM   9823  C  CB  . SER   D 1 141 ? 44.769  -43.044 -27.843 1.00 147.95 ? 210  SER   D CB  1 
ATOM   9824  O  OG  . SER   D 1 141 ? 43.750  -43.621 -28.636 1.00 146.40 ? 210  SER   D OG  1 
ATOM   9825  N  N   . LYS   D 1 142 ? 45.861  -40.744 -25.906 1.00 141.83 ? 211  LYS   D N   1 
ATOM   9826  C  CA  . LYS   D 1 142 ? 46.953  -40.253 -25.073 1.00 139.05 ? 211  LYS   D CA  1 
ATOM   9827  C  C   . LYS   D 1 142 ? 47.915  -41.377 -24.677 1.00 153.06 ? 211  LYS   D C   1 
ATOM   9828  O  O   . LYS   D 1 142 ? 47.551  -42.249 -23.880 1.00 155.20 ? 211  LYS   D O   1 
ATOM   9829  C  CB  . LYS   D 1 142 ? 46.422  -39.574 -23.809 1.00 129.02 ? 211  LYS   D CB  1 
ATOM   9830  C  CG  . LYS   D 1 142 ? 44.960  -39.860 -23.483 1.00 128.00 ? 211  LYS   D CG  1 
ATOM   9831  C  CD  . LYS   D 1 142 ? 44.499  -39.098 -22.216 1.00 126.26 ? 211  LYS   D CD  1 
ATOM   9832  C  CE  . LYS   D 1 142 ? 42.967  -39.084 -22.076 1.00 125.03 ? 211  LYS   D CE  1 
ATOM   9833  N  NZ  . LYS   D 1 142 ? 42.460  -38.110 -21.054 1.00 121.71 ? 211  LYS   D NZ  1 
ATOM   9834  N  N   . PRO   D 1 143 ? 49.143  -41.391 -25.199 1.00 158.03 ? 212  PRO   D N   1 
ATOM   9835  C  CA  . PRO   D 1 143 ? 50.132  -42.374 -24.736 1.00 156.88 ? 212  PRO   D CA  1 
ATOM   9836  C  C   . PRO   D 1 143 ? 50.513  -42.079 -23.291 1.00 157.17 ? 212  PRO   D C   1 
ATOM   9837  O  O   . PRO   D 1 143 ? 50.854  -40.945 -22.933 1.00 160.03 ? 212  PRO   D O   1 
ATOM   9838  C  CB  . PRO   D 1 143 ? 51.315  -42.154 -25.690 1.00 157.17 ? 212  PRO   D CB  1 
ATOM   9839  C  CG  . PRO   D 1 143 ? 50.733  -41.506 -26.907 1.00 157.71 ? 212  PRO   D CG  1 
ATOM   9840  C  CD  . PRO   D 1 143 ? 49.624  -40.634 -26.377 1.00 154.82 ? 212  PRO   D CD  1 
ATOM   9841  N  N   . VAL   D 1 144 ? 50.468  -43.113 -22.455 1.00 154.55 ? 213  VAL   D N   1 
ATOM   9842  C  CA  . VAL   D 1 144 ? 50.726  -42.938 -21.028 1.00 151.57 ? 213  VAL   D CA  1 
ATOM   9843  C  C   . VAL   D 1 144 ? 52.194  -42.623 -20.743 1.00 147.20 ? 213  VAL   D C   1 
ATOM   9844  O  O   . VAL   D 1 144 ? 52.504  -41.927 -19.778 1.00 143.80 ? 213  VAL   D O   1 
ATOM   9845  C  CB  . VAL   D 1 144 ? 50.302  -44.167 -20.227 1.00 147.10 ? 213  VAL   D CB  1 
ATOM   9846  C  CG1 . VAL   D 1 144 ? 48.793  -44.293 -20.256 1.00 142.89 ? 213  VAL   D CG1 1 
ATOM   9847  C  CG2 . VAL   D 1 144 ? 50.970  -45.413 -20.805 1.00 151.27 ? 213  VAL   D CG2 1 
ATOM   9848  N  N   . SER   D 1 151 ? 52.031  -36.607 -19.617 1.00 122.92 ? 220  SER   D N   1 
ATOM   9849  C  CA  . SER   D 1 151 ? 53.055  -35.647 -20.037 1.00 135.18 ? 220  SER   D CA  1 
ATOM   9850  C  C   . SER   D 1 151 ? 52.397  -34.285 -20.374 1.00 134.96 ? 220  SER   D C   1 
ATOM   9851  O  O   . SER   D 1 151 ? 51.397  -34.248 -21.092 1.00 128.92 ? 220  SER   D O   1 
ATOM   9852  C  CB  . SER   D 1 151 ? 53.847  -36.210 -21.236 1.00 131.24 ? 220  SER   D CB  1 
ATOM   9853  O  OG  . SER   D 1 151 ? 54.758  -35.267 -21.783 1.00 128.35 ? 220  SER   D OG  1 
ATOM   9854  N  N   . TYR   D 1 152 ? 52.946  -33.179 -19.837 1.00 141.29 ? 221  TYR   D N   1 
ATOM   9855  C  CA  . TYR   D 1 152 ? 52.350  -31.857 -20.058 1.00 140.66 ? 221  TYR   D CA  1 
ATOM   9856  C  C   . TYR   D 1 152 ? 52.133  -31.564 -21.539 1.00 138.80 ? 221  TYR   D C   1 
ATOM   9857  O  O   . TYR   D 1 152 ? 51.152  -30.905 -21.911 1.00 135.46 ? 221  TYR   D O   1 
ATOM   9858  C  CB  . TYR   D 1 152 ? 53.213  -30.755 -19.427 1.00 142.18 ? 221  TYR   D CB  1 
ATOM   9859  N  N   . LYS   D 1 153 ? 53.045  -32.031 -22.398 1.00 130.27 ? 222  LYS   D N   1 
ATOM   9860  C  CA  . LYS   D 1 153 ? 52.960  -31.729 -23.827 1.00 119.86 ? 222  LYS   D CA  1 
ATOM   9861  C  C   . LYS   D 1 153 ? 51.621  -32.149 -24.407 1.00 118.92 ? 222  LYS   D C   1 
ATOM   9862  O  O   . LYS   D 1 153 ? 51.054  -31.445 -25.250 1.00 118.32 ? 222  LYS   D O   1 
ATOM   9863  C  CB  . LYS   D 1 153 ? 54.097  -32.412 -24.584 1.00 118.91 ? 222  LYS   D CB  1 
ATOM   9864  N  N   . TRP   D 1 154 ? 51.098  -33.299 -23.968 1.00 120.21 ? 223  TRP   D N   1 
ATOM   9865  C  CA  . TRP   D 1 154 ? 49.765  -33.706 -24.399 1.00 114.20 ? 223  TRP   D CA  1 
ATOM   9866  C  C   . TRP   D 1 154 ? 48.706  -32.720 -23.903 1.00 114.93 ? 223  TRP   D C   1 
ATOM   9867  O  O   . TRP   D 1 154 ? 48.015  -32.077 -24.704 1.00 113.10 ? 223  TRP   D O   1 
ATOM   9868  C  CB  . TRP   D 1 154 ? 49.446  -35.126 -23.931 1.00 106.04 ? 223  TRP   D CB  1 
ATOM   9869  C  CG  . TRP   D 1 154 ? 48.258  -35.698 -24.631 1.00 104.21 ? 223  TRP   D CG  1 
ATOM   9870  C  CD1 . TRP   D 1 154 ? 48.243  -36.310 -25.852 1.00 109.92 ? 223  TRP   D CD1 1 
ATOM   9871  C  CD2 . TRP   D 1 154 ? 46.905  -35.706 -24.163 1.00 105.98 ? 223  TRP   D CD2 1 
ATOM   9872  N  NE1 . TRP   D 1 154 ? 46.960  -36.704 -26.174 1.00 114.62 ? 223  TRP   D NE1 1 
ATOM   9873  C  CE2 . TRP   D 1 154 ? 46.121  -36.346 -25.152 1.00 109.58 ? 223  TRP   D CE2 1 
ATOM   9874  C  CE3 . TRP   D 1 154 ? 46.280  -35.244 -23.002 1.00 103.42 ? 223  TRP   D CE3 1 
ATOM   9875  C  CZ2 . TRP   D 1 154 ? 44.746  -36.532 -25.011 1.00 106.68 ? 223  TRP   D CZ2 1 
ATOM   9876  C  CZ3 . TRP   D 1 154 ? 44.913  -35.428 -22.865 1.00 106.90 ? 223  TRP   D CZ3 1 
ATOM   9877  C  CH2 . TRP   D 1 154 ? 44.162  -36.066 -23.865 1.00 105.45 ? 223  TRP   D CH2 1 
ATOM   9878  N  N   . TRP   D 1 155 ? 48.580  -32.560 -22.578 1.00 112.78 ? 224  TRP   D N   1 
ATOM   9879  C  CA  . TRP   D 1 155 ? 47.500  -31.732 -22.044 1.00 108.32 ? 224  TRP   D CA  1 
ATOM   9880  C  C   . TRP   D 1 155 ? 47.628  -30.264 -22.451 1.00 109.59 ? 224  TRP   D C   1 
ATOM   9881  O  O   . TRP   D 1 155 ? 46.671  -29.494 -22.271 1.00 109.81 ? 224  TRP   D O   1 
ATOM   9882  C  CB  . TRP   D 1 155 ? 47.432  -31.852 -20.521 1.00 104.61 ? 224  TRP   D CB  1 
ATOM   9883  C  CG  . TRP   D 1 155 ? 46.857  -33.154 -20.056 1.00 99.17  ? 224  TRP   D CG  1 
ATOM   9884  C  CD1 . TRP   D 1 155 ? 47.555  -34.256 -19.673 1.00 97.66  ? 224  TRP   D CD1 1 
ATOM   9885  C  CD2 . TRP   D 1 155 ? 45.464  -33.493 -19.921 1.00 96.57  ? 224  TRP   D CD2 1 
ATOM   9886  N  NE1 . TRP   D 1 155 ? 46.691  -35.256 -19.299 1.00 98.86  ? 224  TRP   D NE1 1 
ATOM   9887  C  CE2 . TRP   D 1 155 ? 45.402  -34.816 -19.446 1.00 98.28  ? 224  TRP   D CE2 1 
ATOM   9888  C  CE3 . TRP   D 1 155 ? 44.268  -32.805 -20.149 1.00 96.36  ? 224  TRP   D CE3 1 
ATOM   9889  C  CZ2 . TRP   D 1 155 ? 44.185  -35.473 -19.196 1.00 97.87  ? 224  TRP   D CZ2 1 
ATOM   9890  C  CZ3 . TRP   D 1 155 ? 43.055  -33.462 -19.901 1.00 94.74  ? 224  TRP   D CZ3 1 
ATOM   9891  C  CH2 . TRP   D 1 155 ? 43.029  -34.777 -19.429 1.00 94.18  ? 224  TRP   D CH2 1 
ATOM   9892  N  N   . GLN   D 1 156 ? 48.779  -29.856 -22.986 1.00 112.57 ? 225  GLN   D N   1 
ATOM   9893  C  CA  . GLN   D 1 156 ? 48.881  -28.527 -23.578 1.00 110.77 ? 225  GLN   D CA  1 
ATOM   9894  C  C   . GLN   D 1 156 ? 48.398  -28.541 -25.027 1.00 106.99 ? 225  GLN   D C   1 
ATOM   9895  O  O   . GLN   D 1 156 ? 47.603  -27.685 -25.438 1.00 104.20 ? 225  GLN   D O   1 
ATOM   9896  C  CB  . GLN   D 1 156 ? 50.315  -28.015 -23.467 1.00 113.97 ? 225  GLN   D CB  1 
ATOM   9897  C  CG  . GLN   D 1 156 ? 50.790  -27.854 -22.023 1.00 121.30 ? 225  GLN   D CG  1 
ATOM   9898  C  CD  . GLN   D 1 156 ? 50.053  -26.738 -21.272 1.00 123.04 ? 225  GLN   D CD  1 
ATOM   9899  O  OE1 . GLN   D 1 156 ? 50.435  -25.562 -21.350 1.00 119.57 ? 225  GLN   D OE1 1 
ATOM   9900  N  NE2 . GLN   D 1 156 ? 48.995  -27.106 -20.545 1.00 117.26 ? 225  GLN   D NE2 1 
ATOM   9901  N  N   . LYS   D 1 157 ? 48.845  -29.523 -25.815 1.00 107.22 ? 226  LYS   D N   1 
ATOM   9902  C  CA  . LYS   D 1 157 ? 48.273  -29.685 -27.145 1.00 103.91 ? 226  LYS   D CA  1 
ATOM   9903  C  C   . LYS   D 1 157 ? 46.779  -29.966 -27.040 1.00 99.51  ? 226  LYS   D C   1 
ATOM   9904  O  O   . LYS   D 1 157 ? 46.002  -29.585 -27.920 1.00 96.40  ? 226  LYS   D O   1 
ATOM   9905  C  CB  . LYS   D 1 157 ? 48.997  -30.801 -27.900 1.00 105.13 ? 226  LYS   D CB  1 
ATOM   9906  N  N   . TYR   D 1 158 ? 46.354  -30.617 -25.959 1.00 101.44 ? 227  TYR   D N   1 
ATOM   9907  C  CA  . TYR   D 1 158 ? 44.931  -30.871 -25.768 1.00 101.18 ? 227  TYR   D CA  1 
ATOM   9908  C  C   . TYR   D 1 158 ? 44.175  -29.559 -25.658 1.00 95.21  ? 227  TYR   D C   1 
ATOM   9909  O  O   . TYR   D 1 158 ? 43.185  -29.338 -26.357 1.00 94.49  ? 227  TYR   D O   1 
ATOM   9910  C  CB  . TYR   D 1 158 ? 44.722  -31.749 -24.529 1.00 98.97  ? 227  TYR   D CB  1 
ATOM   9911  C  CG  . TYR   D 1 158 ? 43.303  -31.812 -24.013 1.00 94.52  ? 227  TYR   D CG  1 
ATOM   9912  C  CD1 . TYR   D 1 158 ? 42.825  -30.853 -23.129 1.00 91.69  ? 227  TYR   D CD1 1 
ATOM   9913  C  CD2 . TYR   D 1 158 ? 42.439  -32.833 -24.402 1.00 93.78  ? 227  TYR   D CD2 1 
ATOM   9914  C  CE1 . TYR   D 1 158 ? 41.524  -30.904 -22.644 1.00 88.62  ? 227  TYR   D CE1 1 
ATOM   9915  C  CE2 . TYR   D 1 158 ? 41.137  -32.892 -23.920 1.00 93.92  ? 227  TYR   D CE2 1 
ATOM   9916  C  CZ  . TYR   D 1 158 ? 40.685  -31.923 -23.041 1.00 89.08  ? 227  TYR   D CZ  1 
ATOM   9917  O  OH  . TYR   D 1 158 ? 39.391  -31.972 -22.568 1.00 88.96  ? 227  TYR   D OH  1 
ATOM   9918  N  N   . GLN   D 1 159 ? 44.669  -28.654 -24.818 1.00 94.15  ? 228  GLN   D N   1 
ATOM   9919  C  CA  . GLN   D 1 159 ? 44.003  -27.374 -24.636 1.00 92.43  ? 228  GLN   D CA  1 
ATOM   9920  C  C   . GLN   D 1 159 ? 44.016  -26.545 -25.917 1.00 92.42  ? 228  GLN   D C   1 
ATOM   9921  O  O   . GLN   D 1 159 ? 43.035  -25.861 -26.221 1.00 91.87  ? 228  GLN   D O   1 
ATOM   9922  C  CB  . GLN   D 1 159 ? 44.669  -26.634 -23.486 1.00 94.05  ? 228  GLN   D CB  1 
ATOM   9923  C  CG  . GLN   D 1 159 ? 44.145  -25.246 -23.205 1.00 89.56  ? 228  GLN   D CG  1 
ATOM   9924  C  CD  . GLN   D 1 159 ? 44.973  -24.577 -22.142 1.00 88.21  ? 228  GLN   D CD  1 
ATOM   9925  O  OE1 . GLN   D 1 159 ? 44.601  -24.546 -20.964 1.00 82.58  ? 228  GLN   D OE1 1 
ATOM   9926  N  NE2 . GLN   D 1 159 ? 46.129  -24.064 -22.544 1.00 93.23  ? 228  GLN   D NE2 1 
ATOM   9927  N  N   . LYS   D 1 160 ? 45.113  -26.597 -26.688 1.00 93.14  ? 229  LYS   D N   1 
ATOM   9928  C  CA  . LYS   D 1 160 ? 45.180  -25.808 -27.920 1.00 94.50  ? 229  LYS   D CA  1 
ATOM   9929  C  C   . LYS   D 1 160 ? 44.148  -26.271 -28.946 1.00 92.28  ? 229  LYS   D C   1 
ATOM   9930  O  O   . LYS   D 1 160 ? 43.544  -25.447 -29.641 1.00 98.36  ? 229  LYS   D O   1 
ATOM   9931  C  CB  . LYS   D 1 160 ? 46.586  -25.862 -28.521 1.00 97.19  ? 229  LYS   D CB  1 
ATOM   9932  C  CG  . LYS   D 1 160 ? 47.481  -24.657 -28.192 1.00 108.70 ? 229  LYS   D CG  1 
ATOM   9933  C  CD  . LYS   D 1 160 ? 47.349  -23.487 -29.203 1.00 115.54 ? 229  LYS   D CD  1 
ATOM   9934  C  CE  . LYS   D 1 160 ? 48.384  -22.365 -28.920 1.00 122.77 ? 229  LYS   D CE  1 
ATOM   9935  N  NZ  . LYS   D 1 160 ? 47.924  -20.945 -29.157 1.00 114.36 ? 229  LYS   D NZ  1 
ATOM   9936  N  N   . ARG   D 1 161 ? 43.939  -27.581 -29.081 1.00 92.20  ? 230  ARG   D N   1 
ATOM   9937  C  CA  . ARG   D 1 161 ? 42.970  -28.054 -30.065 1.00 92.10  ? 230  ARG   D CA  1 
ATOM   9938  C  C   . ARG   D 1 161 ? 41.534  -27.902 -29.556 1.00 95.03  ? 230  ARG   D C   1 
ATOM   9939  O  O   . ARG   D 1 161 ? 40.676  -27.373 -30.270 1.00 103.51 ? 230  ARG   D O   1 
ATOM   9940  C  CB  . ARG   D 1 161 ? 43.270  -29.509 -30.460 1.00 91.07  ? 230  ARG   D CB  1 
ATOM   9941  N  N   . LYS   D 1 162 ? 41.254  -28.331 -28.315 1.00 97.26  ? 231  LYS   D N   1 
ATOM   9942  C  CA  . LYS   D 1 162 ? 39.866  -28.446 -27.848 1.00 93.66  ? 231  LYS   D CA  1 
ATOM   9943  C  C   . LYS   D 1 162 ? 39.200  -27.087 -27.668 1.00 88.51  ? 231  LYS   D C   1 
ATOM   9944  O  O   . LYS   D 1 162 ? 37.982  -26.973 -27.826 1.00 87.21  ? 231  LYS   D O   1 
ATOM   9945  C  CB  . LYS   D 1 162 ? 39.793  -29.236 -26.529 1.00 87.97  ? 231  LYS   D CB  1 
ATOM   9946  C  CG  . LYS   D 1 162 ? 38.366  -29.668 -26.145 1.00 89.68  ? 231  LYS   D CG  1 
ATOM   9947  C  CD  . LYS   D 1 162 ? 38.324  -30.572 -24.898 1.00 94.07  ? 231  LYS   D CD  1 
ATOM   9948  C  CE  . LYS   D 1 162 ? 37.062  -31.473 -24.809 1.00 98.60  ? 231  LYS   D CE  1 
ATOM   9949  N  NZ  . LYS   D 1 162 ? 37.295  -32.940 -25.111 1.00 99.10  ? 231  LYS   D NZ  1 
ATOM   9950  N  N   . PHE   D 1 163 ? 39.974  -26.058 -27.325 1.00 90.09  ? 232  PHE   D N   1 
ATOM   9951  C  CA  . PHE   D 1 163 ? 39.454  -24.734 -27.009 1.00 88.13  ? 232  PHE   D CA  1 
ATOM   9952  C  C   . PHE   D 1 163 ? 39.934  -23.682 -28.008 1.00 90.36  ? 232  PHE   D C   1 
ATOM   9953  O  O   . PHE   D 1 163 ? 39.993  -22.487 -27.692 1.00 88.09  ? 232  PHE   D O   1 
ATOM   9954  C  CB  . PHE   D 1 163 ? 39.850  -24.356 -25.587 1.00 83.99  ? 232  PHE   D CB  1 
ATOM   9955  C  CG  . PHE   D 1 163 ? 39.418  -25.347 -24.548 1.00 83.69  ? 232  PHE   D CG  1 
ATOM   9956  C  CD1 . PHE   D 1 163 ? 38.076  -25.568 -24.288 1.00 83.31  ? 232  PHE   D CD1 1 
ATOM   9957  C  CD2 . PHE   D 1 163 ? 40.360  -26.045 -23.808 1.00 85.45  ? 232  PHE   D CD2 1 
ATOM   9958  C  CE1 . PHE   D 1 163 ? 37.686  -26.474 -23.313 1.00 81.62  ? 232  PHE   D CE1 1 
ATOM   9959  C  CE2 . PHE   D 1 163 ? 39.967  -26.944 -22.827 1.00 81.24  ? 232  PHE   D CE2 1 
ATOM   9960  C  CZ  . PHE   D 1 163 ? 38.626  -27.151 -22.589 1.00 80.26  ? 232  PHE   D CZ  1 
ATOM   9961  N  N   . HIS   D 1 164 ? 40.271  -24.117 -29.221 1.00 92.22  ? 233  HIS   D N   1 
ATOM   9962  C  CA  . HIS   D 1 164 ? 40.760  -23.210 -30.250 1.00 89.15  ? 233  HIS   D CA  1 
ATOM   9963  C  C   . HIS   D 1 164 ? 39.730  -22.132 -30.588 1.00 86.56  ? 233  HIS   D C   1 
ATOM   9964  O  O   . HIS   D 1 164 ? 40.061  -20.945 -30.677 1.00 85.44  ? 233  HIS   D O   1 
ATOM   9965  C  CB  . HIS   D 1 164 ? 41.123  -24.038 -31.469 1.00 83.48  ? 233  HIS   D CB  1 
ATOM   9966  C  CG  . HIS   D 1 164 ? 41.270  -23.243 -32.716 1.00 88.50  ? 233  HIS   D CG  1 
ATOM   9967  N  ND1 . HIS   D 1 164 ? 42.434  -22.585 -33.047 1.00 84.92  ? 233  HIS   D ND1 1 
ATOM   9968  C  CD2 . HIS   D 1 164 ? 40.403  -23.014 -33.731 1.00 89.68  ? 233  HIS   D CD2 1 
ATOM   9969  C  CE1 . HIS   D 1 164 ? 42.278  -21.985 -34.215 1.00 89.55  ? 233  HIS   D CE1 1 
ATOM   9970  N  NE2 . HIS   D 1 164 ? 41.054  -22.226 -34.650 1.00 88.82  ? 233  HIS   D NE2 1 
ATOM   9971  N  N   . CYS   D 1 165 ? 38.472  -22.534 -30.782 1.00 87.15  ? 234  CYS   D N   1 
ATOM   9972  C  CA  . CYS   D 1 165 ? 37.361  -21.622 -31.037 1.00 82.81  ? 234  CYS   D CA  1 
ATOM   9973  C  C   . CYS   D 1 165 ? 36.991  -20.770 -29.845 1.00 80.71  ? 234  CYS   D C   1 
ATOM   9974  O  O   . CYS   D 1 165 ? 36.023  -20.012 -29.930 1.00 78.73  ? 234  CYS   D O   1 
ATOM   9975  C  CB  . CYS   D 1 165 ? 36.129  -22.407 -31.468 1.00 88.50  ? 234  CYS   D CB  1 
ATOM   9976  S  SG  . CYS   D 1 165 ? 36.327  -23.124 -33.077 1.00 90.48  ? 234  CYS   D SG  1 
ATOM   9977  N  N   . ALA   D 1 166 ? 37.676  -20.901 -28.720 1.00 80.38  ? 235  ALA   D N   1 
ATOM   9978  C  CA  . ALA   D 1 166 ? 37.494  -19.887 -27.704 1.00 77.75  ? 235  ALA   D CA  1 
ATOM   9979  C  C   . ALA   D 1 166 ? 37.950  -18.536 -28.228 1.00 82.07  ? 235  ALA   D C   1 
ATOM   9980  O  O   . ALA   D 1 166 ? 37.678  -17.493 -27.610 1.00 78.86  ? 235  ALA   D O   1 
ATOM   9981  C  CB  . ALA   D 1 166 ? 38.254  -20.291 -26.448 1.00 81.51  ? 235  ALA   D CB  1 
ATOM   9982  N  N   . ASN   D 1 167 ? 38.634  -18.546 -29.376 1.00 84.01  ? 236  ASN   D N   1 
ATOM   9983  C  CA  . ASN   D 1 167 ? 39.058  -17.323 -30.040 1.00 80.58  ? 236  ASN   D CA  1 
ATOM   9984  C  C   . ASN   D 1 167 ? 37.888  -16.523 -30.588 1.00 78.96  ? 236  ASN   D C   1 
ATOM   9985  O  O   . ASN   D 1 167 ? 38.004  -15.305 -30.770 1.00 84.94  ? 236  ASN   D O   1 
ATOM   9986  C  CB  . ASN   D 1 167 ? 40.055  -17.674 -31.137 1.00 81.79  ? 236  ASN   D CB  1 
ATOM   9987  C  CG  . ASN   D 1 167 ? 41.474  -17.579 -30.640 1.00 90.29  ? 236  ASN   D CG  1 
ATOM   9988  O  OD1 . ASN   D 1 167 ? 42.059  -16.484 -30.637 1.00 92.63  ? 236  ASN   D OD1 1 
ATOM   9989  N  ND2 . ASN   D 1 167 ? 42.034  -18.714 -30.170 1.00 90.52  ? 236  ASN   D ND2 1 
ATOM   9990  N  N   . LEU   D 1 168 ? 36.765  -17.176 -30.843 1.00 75.65  ? 237  LEU   D N   1 
ATOM   9991  C  CA  . LEU   D 1 168 ? 35.556  -16.466 -31.222 1.00 77.34  ? 237  LEU   D CA  1 
ATOM   9992  C  C   . LEU   D 1 168 ? 34.785  -15.896 -30.033 1.00 74.56  ? 237  LEU   D C   1 
ATOM   9993  O  O   . LEU   D 1 168 ? 33.730  -15.284 -30.243 1.00 76.14  ? 237  LEU   D O   1 
ATOM   9994  C  CB  . LEU   D 1 168 ? 34.654  -17.402 -32.017 1.00 80.19  ? 237  LEU   D CB  1 
ATOM   9995  C  CG  . LEU   D 1 168 ? 35.376  -18.228 -33.069 1.00 77.03  ? 237  LEU   D CG  1 
ATOM   9996  C  CD1 . LEU   D 1 168 ? 34.668  -19.545 -33.160 1.00 85.00  ? 237  LEU   D CD1 1 
ATOM   9997  C  CD2 . LEU   D 1 168 ? 35.332  -17.494 -34.401 1.00 78.80  ? 237  LEU   D CD2 1 
ATOM   9998  N  N   . THR   D 1 169 ? 35.262  -16.085 -28.804 1.00 71.73  ? 238  THR   D N   1 
ATOM   9999  C  CA  . THR   D 1 169 ? 34.507  -15.687 -27.617 1.00 77.44  ? 238  THR   D CA  1 
ATOM   10000 C  C   . THR   D 1 169 ? 35.301  -14.663 -26.811 1.00 76.75  ? 238  THR   D C   1 
ATOM   10001 O  O   . THR   D 1 169 ? 36.457  -14.352 -27.114 1.00 75.97  ? 238  THR   D O   1 
ATOM   10002 C  CB  . THR   D 1 169 ? 34.163  -16.893 -26.729 1.00 77.96  ? 238  THR   D CB  1 
ATOM   10003 O  OG1 . THR   D 1 169 ? 35.314  -17.243 -25.951 1.00 74.18  ? 238  THR   D OG1 1 
ATOM   10004 C  CG2 . THR   D 1 169 ? 33.729  -18.093 -27.573 1.00 75.03  ? 238  THR   D CG2 1 
ATOM   10005 N  N   . SER   D 1 170 ? 34.678  -14.168 -25.742 1.00 73.26  ? 239  SER   D N   1 
ATOM   10006 C  CA  . SER   D 1 170 ? 35.264  -13.115 -24.924 1.00 74.61  ? 239  SER   D CA  1 
ATOM   10007 C  C   . SER   D 1 170 ? 36.209  -13.624 -23.850 1.00 73.10  ? 239  SER   D C   1 
ATOM   10008 O  O   . SER   D 1 170 ? 36.731  -12.814 -23.076 1.00 79.30  ? 239  SER   D O   1 
ATOM   10009 C  CB  . SER   D 1 170 ? 34.162  -12.277 -24.280 1.00 78.44  ? 239  SER   D CB  1 
ATOM   10010 O  OG  . SER   D 1 170 ? 33.133  -13.129 -23.825 1.00 83.42  ? 239  SER   D OG  1 
ATOM   10011 N  N   . TRP   D 1 171 ? 36.464  -14.923 -23.788 1.00 75.70  ? 240  TRP   D N   1 
ATOM   10012 C  CA  . TRP   D 1 171 ? 37.347  -15.518 -22.798 1.00 73.15  ? 240  TRP   D CA  1 
ATOM   10013 C  C   . TRP   D 1 171 ? 38.401  -16.399 -23.456 1.00 74.19  ? 240  TRP   D C   1 
ATOM   10014 O  O   . TRP   D 1 171 ? 38.229  -16.840 -24.595 1.00 74.36  ? 240  TRP   D O   1 
ATOM   10015 C  CB  . TRP   D 1 171 ? 36.527  -16.352 -21.815 1.00 73.41  ? 240  TRP   D CB  1 
ATOM   10016 C  CG  . TRP   D 1 171 ? 35.400  -15.638 -21.186 1.00 73.33  ? 240  TRP   D CG  1 
ATOM   10017 C  CD1 . TRP   D 1 171 ? 34.068  -15.821 -21.421 1.00 71.37  ? 240  TRP   D CD1 1 
ATOM   10018 C  CD2 . TRP   D 1 171 ? 35.497  -14.650 -20.155 1.00 83.30  ? 240  TRP   D CD2 1 
ATOM   10019 N  NE1 . TRP   D 1 171 ? 33.321  -14.996 -20.601 1.00 77.03  ? 240  TRP   D NE1 1 
ATOM   10020 C  CE2 . TRP   D 1 171 ? 34.179  -14.266 -19.815 1.00 83.97  ? 240  TRP   D CE2 1 
ATOM   10021 C  CE3 . TRP   D 1 171 ? 36.573  -14.040 -19.491 1.00 79.12  ? 240  TRP   D CE3 1 
ATOM   10022 C  CZ2 . TRP   D 1 171 ? 33.916  -13.300 -18.837 1.00 86.09  ? 240  TRP   D CZ2 1 
ATOM   10023 C  CZ3 . TRP   D 1 171 ? 36.308  -13.084 -18.532 1.00 81.61  ? 240  TRP   D CZ3 1 
ATOM   10024 C  CH2 . TRP   D 1 171 ? 34.995  -12.723 -18.211 1.00 85.30  ? 240  TRP   D CH2 1 
ATOM   10025 N  N   . PRO   D 1 172 ? 39.509  -16.706 -22.740 1.00 74.64  ? 241  PRO   D N   1 
ATOM   10026 C  CA  . PRO   D 1 172 ? 40.611  -17.478 -23.344 1.00 79.59  ? 241  PRO   D CA  1 
ATOM   10027 C  C   . PRO   D 1 172 ? 40.589  -18.987 -23.063 1.00 77.86  ? 241  PRO   D C   1 
ATOM   10028 O  O   . PRO   D 1 172 ? 39.806  -19.489 -22.257 1.00 75.34  ? 241  PRO   D O   1 
ATOM   10029 C  CB  . PRO   D 1 172 ? 41.846  -16.834 -22.700 1.00 78.85  ? 241  PRO   D CB  1 
ATOM   10030 C  CG  . PRO   D 1 172 ? 41.356  -16.519 -21.291 1.00 77.07  ? 241  PRO   D CG  1 
ATOM   10031 C  CD  . PRO   D 1 172 ? 39.847  -16.266 -21.375 1.00 74.18  ? 241  PRO   D CD  1 
ATOM   10032 N  N   . ARG   D 1 173 ? 41.502  -19.704 -23.720 1.00 76.19  ? 242  ARG   D N   1 
ATOM   10033 C  CA  . ARG   D 1 173 ? 41.594  -21.157 -23.568 1.00 78.41  ? 242  ARG   D CA  1 
ATOM   10034 C  C   . ARG   D 1 173 ? 41.654  -21.582 -22.101 1.00 80.04  ? 242  ARG   D C   1 
ATOM   10035 O  O   . ARG   D 1 173 ? 40.898  -22.454 -21.651 1.00 79.86  ? 242  ARG   D O   1 
ATOM   10036 C  CB  . ARG   D 1 173 ? 42.826  -21.674 -24.314 1.00 80.74  ? 242  ARG   D CB  1 
ATOM   10037 C  CG  . ARG   D 1 173 ? 42.573  -21.973 -25.762 1.00 85.84  ? 242  ARG   D CG  1 
ATOM   10038 C  CD  . ARG   D 1 173 ? 43.804  -22.589 -26.429 1.00 96.65  ? 242  ARG   D CD  1 
ATOM   10039 N  NE  . ARG   D 1 173 ? 43.998  -22.019 -27.758 1.00 107.36 ? 242  ARG   D NE  1 
ATOM   10040 C  CZ  . ARG   D 1 173 ? 44.891  -21.081 -28.055 1.00 115.37 ? 242  ARG   D CZ  1 
ATOM   10041 N  NH1 . ARG   D 1 173 ? 45.816  -20.696 -27.178 1.00 112.42 ? 242  ARG   D NH1 1 
ATOM   10042 N  NH2 . ARG   D 1 173 ? 44.854  -20.509 -29.262 1.00 114.12 ? 242  ARG   D NH2 1 
ATOM   10043 N  N   . TRP   D 1 174 ? 42.579  -20.995 -21.345 1.00 78.65  ? 243  TRP   D N   1 
ATOM   10044 C  CA  . TRP   D 1 174 ? 42.819  -21.476 -19.990 1.00 74.40  ? 243  TRP   D CA  1 
ATOM   10045 C  C   . TRP   D 1 174 ? 41.602  -21.311 -19.092 1.00 75.19  ? 243  TRP   D C   1 
ATOM   10046 O  O   . TRP   D 1 174 ? 41.458  -22.045 -18.105 1.00 77.92  ? 243  TRP   D O   1 
ATOM   10047 C  CB  . TRP   D 1 174 ? 44.030  -20.772 -19.384 1.00 80.58  ? 243  TRP   D CB  1 
ATOM   10048 C  CG  . TRP   D 1 174 ? 44.048  -19.238 -19.384 1.00 82.01  ? 243  TRP   D CG  1 
ATOM   10049 C  CD1 . TRP   D 1 174 ? 44.671  -18.426 -20.298 1.00 81.63  ? 243  TRP   D CD1 1 
ATOM   10050 C  CD2 . TRP   D 1 174 ? 43.501  -18.363 -18.388 1.00 76.83  ? 243  TRP   D CD2 1 
ATOM   10051 N  NE1 . TRP   D 1 174 ? 44.522  -17.104 -19.950 1.00 82.02  ? 243  TRP   D NE1 1 
ATOM   10052 C  CE2 . TRP   D 1 174 ? 43.809  -17.038 -18.780 1.00 81.32  ? 243  TRP   D CE2 1 
ATOM   10053 C  CE3 . TRP   D 1 174 ? 42.769  -18.567 -17.213 1.00 77.17  ? 243  TRP   D CE3 1 
ATOM   10054 C  CZ2 . TRP   D 1 174 ? 43.418  -15.930 -18.030 1.00 81.65  ? 243  TRP   D CZ2 1 
ATOM   10055 C  CZ3 . TRP   D 1 174 ? 42.374  -17.467 -16.470 1.00 77.85  ? 243  TRP   D CZ3 1 
ATOM   10056 C  CH2 . TRP   D 1 174 ? 42.705  -16.166 -16.879 1.00 84.21  ? 243  TRP   D CH2 1 
ATOM   10057 N  N   . LEU   D 1 175 ? 40.733  -20.343 -19.390 1.00 78.18  ? 244  LEU   D N   1 
ATOM   10058 C  CA  . LEU   D 1 175 ? 39.465  -20.253 -18.670 1.00 78.29  ? 244  LEU   D CA  1 
ATOM   10059 C  C   . LEU   D 1 175 ? 38.624  -21.492 -18.929 1.00 78.56  ? 244  LEU   D C   1 
ATOM   10060 O  O   . LEU   D 1 175 ? 38.295  -22.243 -18.005 1.00 80.63  ? 244  LEU   D O   1 
ATOM   10061 C  CB  . LEU   D 1 175 ? 38.686  -18.994 -19.071 1.00 76.97  ? 244  LEU   D CB  1 
ATOM   10062 C  CG  . LEU   D 1 175 ? 37.747  -18.554 -17.942 1.00 78.59  ? 244  LEU   D CG  1 
ATOM   10063 C  CD1 . LEU   D 1 175 ? 36.375  -19.173 -18.031 1.00 81.95  ? 244  LEU   D CD1 1 
ATOM   10064 C  CD2 . LEU   D 1 175 ? 38.382  -18.941 -16.635 1.00 77.84  ? 244  LEU   D CD2 1 
ATOM   10065 N  N   . TYR   D 1 176 ? 38.293  -21.743 -20.194 1.00 79.45  ? 245  TYR   D N   1 
ATOM   10066 C  CA  . TYR   D 1 176 ? 37.444  -22.884 -20.489 1.00 81.14  ? 245  TYR   D CA  1 
ATOM   10067 C  C   . TYR   D 1 176 ? 38.043  -24.171 -19.944 1.00 78.44  ? 245  TYR   D C   1 
ATOM   10068 O  O   . TYR   D 1 176 ? 37.301  -25.109 -19.644 1.00 81.31  ? 245  TYR   D O   1 
ATOM   10069 C  CB  . TYR   D 1 176 ? 37.192  -22.979 -21.996 1.00 80.72  ? 245  TYR   D CB  1 
ATOM   10070 C  CG  . TYR   D 1 176 ? 36.363  -21.820 -22.515 1.00 79.52  ? 245  TYR   D CG  1 
ATOM   10071 C  CD1 . TYR   D 1 176 ? 34.978  -21.819 -22.402 1.00 78.23  ? 245  TYR   D CD1 1 
ATOM   10072 C  CD2 . TYR   D 1 176 ? 36.972  -20.716 -23.102 1.00 76.82  ? 245  TYR   D CD2 1 
ATOM   10073 C  CE1 . TYR   D 1 176 ? 34.230  -20.755 -22.878 1.00 78.36  ? 245  TYR   D CE1 1 
ATOM   10074 C  CE2 . TYR   D 1 176 ? 36.236  -19.657 -23.574 1.00 72.43  ? 245  TYR   D CE2 1 
ATOM   10075 C  CZ  . TYR   D 1 176 ? 34.862  -19.671 -23.467 1.00 74.47  ? 245  TYR   D CZ  1 
ATOM   10076 O  OH  . TYR   D 1 176 ? 34.121  -18.598 -23.955 1.00 72.07  ? 245  TYR   D OH  1 
ATOM   10077 N  N   . SER   D 1 177 ? 39.367  -24.237 -19.788 1.00 75.32  ? 246  SER   D N   1 
ATOM   10078 C  CA  . SER   D 1 177 ? 39.960  -25.418 -19.159 1.00 78.92  ? 246  SER   D CA  1 
ATOM   10079 C  C   . SER   D 1 177 ? 39.443  -25.597 -17.736 1.00 79.95  ? 246  SER   D C   1 
ATOM   10080 O  O   . SER   D 1 177 ? 39.031  -26.695 -17.336 1.00 79.95  ? 246  SER   D O   1 
ATOM   10081 C  CB  . SER   D 1 177 ? 41.487  -25.316 -19.149 1.00 78.07  ? 246  SER   D CB  1 
ATOM   10082 O  OG  . SER   D 1 177 ? 42.013  -25.424 -20.460 1.00 81.20  ? 246  SER   D OG  1 
ATOM   10083 N  N   . LEU   D 1 178 ? 39.448  -24.524 -16.957 1.00 77.54  ? 247  LEU   D N   1 
ATOM   10084 C  CA  . LEU   D 1 178 ? 38.978  -24.630 -15.593 1.00 80.24  ? 247  LEU   D CA  1 
ATOM   10085 C  C   . LEU   D 1 178 ? 37.575  -25.246 -15.498 1.00 78.27  ? 247  LEU   D C   1 
ATOM   10086 O  O   . LEU   D 1 178 ? 37.201  -25.723 -14.425 1.00 79.61  ? 247  LEU   D O   1 
ATOM   10087 C  CB  . LEU   D 1 178 ? 39.064  -23.240 -14.942 1.00 80.93  ? 247  LEU   D CB  1 
ATOM   10088 C  CG  . LEU   D 1 178 ? 40.451  -22.581 -15.013 1.00 77.13  ? 247  LEU   D CG  1 
ATOM   10089 C  CD1 . LEU   D 1 178 ? 40.408  -21.239 -14.341 1.00 72.30  ? 247  LEU   D CD1 1 
ATOM   10090 C  CD2 . LEU   D 1 178 ? 41.500  -23.450 -14.362 1.00 81.54  ? 247  LEU   D CD2 1 
ATOM   10091 N  N   . TYR   D 1 179 ? 36.803  -25.293 -16.585 1.00 75.82  ? 248  TYR   D N   1 
ATOM   10092 C  CA  . TYR   D 1 179 ? 35.462  -25.862 -16.521 1.00 76.55  ? 248  TYR   D CA  1 
ATOM   10093 C  C   . TYR   D 1 179 ? 35.307  -27.100 -17.387 1.00 81.93  ? 248  TYR   D C   1 
ATOM   10094 O  O   . TYR   D 1 179 ? 34.168  -27.489 -17.670 1.00 84.33  ? 248  TYR   D O   1 
ATOM   10095 C  CB  . TYR   D 1 179 ? 34.402  -24.837 -16.910 1.00 78.25  ? 248  TYR   D CB  1 
ATOM   10096 C  CG  . TYR   D 1 179 ? 34.217  -23.697 -15.921 1.00 80.09  ? 248  TYR   D CG  1 
ATOM   10097 C  CD1 . TYR   D 1 179 ? 35.082  -22.620 -15.904 1.00 80.68  ? 248  TYR   D CD1 1 
ATOM   10098 C  CD2 . TYR   D 1 179 ? 33.158  -23.692 -15.021 1.00 80.65  ? 248  TYR   D CD2 1 
ATOM   10099 C  CE1 . TYR   D 1 179 ? 34.903  -21.553 -14.997 1.00 87.64  ? 248  TYR   D CE1 1 
ATOM   10100 C  CE2 . TYR   D 1 179 ? 32.971  -22.644 -14.123 1.00 79.45  ? 248  TYR   D CE2 1 
ATOM   10101 C  CZ  . TYR   D 1 179 ? 33.841  -21.576 -14.107 1.00 83.82  ? 248  TYR   D CZ  1 
ATOM   10102 O  OH  . TYR   D 1 179 ? 33.639  -20.546 -13.199 1.00 87.74  ? 248  TYR   D OH  1 
ATOM   10103 N  N   . ASP   D 1 180 ? 36.415  -27.728 -17.797 1.00 83.72  ? 249  ASP   D N   1 
ATOM   10104 C  CA  . ASP   D 1 180 ? 36.383  -28.840 -18.744 1.00 84.24  ? 249  ASP   D CA  1 
ATOM   10105 C  C   . ASP   D 1 180 ? 36.519  -30.179 -18.027 1.00 83.87  ? 249  ASP   D C   1 
ATOM   10106 O  O   . ASP   D 1 180 ? 37.600  -30.498 -17.517 1.00 85.58  ? 249  ASP   D O   1 
ATOM   10107 C  CB  . ASP   D 1 180 ? 37.490  -28.684 -19.773 1.00 83.76  ? 249  ASP   D CB  1 
ATOM   10108 C  CG  . ASP   D 1 180 ? 37.636  -29.912 -20.616 1.00 86.01  ? 249  ASP   D CG  1 
ATOM   10109 O  OD1 . ASP   D 1 180 ? 36.580  -30.447 -21.057 1.00 88.97  ? 249  ASP   D OD1 1 
ATOM   10110 O  OD2 . ASP   D 1 180 ? 38.794  -30.351 -20.825 1.00 87.56  ? 249  ASP   D OD2 1 
ATOM   10111 N  N   . ALA   D 1 181 ? 35.443  -30.975 -18.046 1.00 78.55  ? 250  ALA   D N   1 
ATOM   10112 C  CA  . ALA   D 1 181 ? 35.360  -32.272 -17.354 1.00 81.31  ? 250  ALA   D CA  1 
ATOM   10113 C  C   . ALA   D 1 181 ? 36.632  -33.168 -17.418 1.00 85.10  ? 250  ALA   D C   1 
ATOM   10114 O  O   . ALA   D 1 181 ? 37.107  -33.631 -16.375 1.00 82.28  ? 250  ALA   D O   1 
ATOM   10115 C  CB  . ALA   D 1 181 ? 34.287  -33.128 -17.950 1.00 86.27  ? 250  ALA   D CB  1 
ATOM   10116 N  N   . GLU   D 1 182 ? 37.134  -33.423 -18.632 1.00 87.18  ? 251  GLU   D N   1 
ATOM   10117 C  CA  . GLU   D 1 182 ? 38.204  -34.352 -18.817 1.00 87.61  ? 251  GLU   D CA  1 
ATOM   10118 C  C   . GLU   D 1 182 ? 39.486  -33.750 -18.134 1.00 85.00  ? 251  GLU   D C   1 
ATOM   10119 O  O   . GLU   D 1 182 ? 40.256  -34.484 -17.494 1.00 78.25  ? 251  GLU   D O   1 
ATOM   10120 C  CB  . GLU   D 1 182 ? 38.478  -34.561 -20.332 1.00 82.64  ? 251  GLU   D CB  1 
ATOM   10121 N  N   . THR   D 1 183 ? 39.655  -32.412 -18.212 1.00 86.98  ? 252  THR   D N   1 
ATOM   10122 C  CA  . THR   D 1 183 ? 40.755  -31.697 -17.546 1.00 84.19  ? 252  THR   D CA  1 
ATOM   10123 C  C   . THR   D 1 183 ? 40.609  -31.712 -16.023 1.00 81.74  ? 252  THR   D C   1 
ATOM   10124 O  O   . THR   D 1 183 ? 41.598  -31.900 -15.301 1.00 78.78  ? 252  THR   D O   1 
ATOM   10125 C  CB  . THR   D 1 183 ? 40.833  -30.246 -18.053 1.00 78.05  ? 252  THR   D CB  1 
ATOM   10126 O  OG1 . THR   D 1 183 ? 41.094  -30.234 -19.451 1.00 85.89  ? 252  THR   D OG1 1 
ATOM   10127 C  CG2 . THR   D 1 183 ? 41.940  -29.457 -17.356 1.00 81.37  ? 252  THR   D CG2 1 
ATOM   10128 N  N   . LEU   D 1 184 ? 39.398  -31.504 -15.505 1.00 81.14  ? 253  LEU   D N   1 
ATOM   10129 C  CA  . LEU   D 1 184 ? 39.249  -31.515 -14.056 1.00 80.69  ? 253  LEU   D CA  1 
ATOM   10130 C  C   . LEU   D 1 184 ? 39.540  -32.895 -13.493 1.00 81.00  ? 253  LEU   D C   1 
ATOM   10131 O  O   . LEU   D 1 184 ? 40.264  -33.017 -12.496 1.00 80.46  ? 253  LEU   D O   1 
ATOM   10132 C  CB  . LEU   D 1 184 ? 37.851  -31.040 -13.652 1.00 83.34  ? 253  LEU   D CB  1 
ATOM   10133 C  CG  . LEU   D 1 184 ? 37.569  -29.580 -14.030 1.00 77.67  ? 253  LEU   D CG  1 
ATOM   10134 C  CD1 . LEU   D 1 184 ? 36.174  -29.143 -13.557 1.00 77.31  ? 253  LEU   D CD1 1 
ATOM   10135 C  CD2 . LEU   D 1 184 ? 38.695  -28.644 -13.534 1.00 81.23  ? 253  LEU   D CD2 1 
ATOM   10136 N  N   . MET   D 1 185 ? 39.010  -33.953 -14.133 1.00 84.53  ? 254  MET   D N   1 
ATOM   10137 C  CA  . MET   D 1 185 ? 39.273  -35.314 -13.660 1.00 79.62  ? 254  MET   D CA  1 
ATOM   10138 C  C   . MET   D 1 185 ? 40.766  -35.594 -13.603 1.00 80.57  ? 254  MET   D C   1 
ATOM   10139 O  O   . MET   D 1 185 ? 41.248  -36.198 -12.640 1.00 81.25  ? 254  MET   D O   1 
ATOM   10140 C  CB  . MET   D 1 185 ? 38.575  -36.342 -14.550 1.00 77.79  ? 254  MET   D CB  1 
ATOM   10141 C  CG  . MET   D 1 185 ? 37.221  -35.924 -14.990 1.00 82.65  ? 254  MET   D CG  1 
ATOM   10142 S  SD  . MET   D 1 185 ? 36.113  -37.320 -15.160 1.00 86.81  ? 254  MET   D SD  1 
ATOM   10143 C  CE  . MET   D 1 185 ? 36.626  -37.954 -16.733 1.00 92.39  ? 254  MET   D CE  1 
ATOM   10144 N  N   . ASP   D 1 186 ? 41.521  -35.162 -14.622 1.00 79.45  ? 255  ASP   D N   1 
ATOM   10145 C  CA  . ASP   D 1 186 ? 42.957  -35.441 -14.612 1.00 83.93  ? 255  ASP   D CA  1 
ATOM   10146 C  C   . ASP   D 1 186 ? 43.646  -34.733 -13.445 1.00 86.15  ? 255  ASP   D C   1 
ATOM   10147 O  O   . ASP   D 1 186 ? 44.447  -35.349 -12.726 1.00 88.15  ? 255  ASP   D O   1 
ATOM   10148 C  CB  . ASP   D 1 186 ? 43.619  -35.062 -15.944 1.00 86.00  ? 255  ASP   D CB  1 
ATOM   10149 C  CG  . ASP   D 1 186 ? 45.035  -35.658 -16.090 1.00 92.70  ? 255  ASP   D CG  1 
ATOM   10150 O  OD1 . ASP   D 1 186 ? 45.141  -36.871 -16.415 1.00 93.96  ? 255  ASP   D OD1 1 
ATOM   10151 O  OD2 . ASP   D 1 186 ? 46.035  -34.916 -15.890 1.00 94.46  ? 255  ASP   D OD2 1 
ATOM   10152 N  N   . ARG   D 1 187 ? 43.336  -33.448 -13.228 1.00 83.25  ? 256  ARG   D N   1 
ATOM   10153 C  CA  . ARG   D 1 187 ? 43.895  -32.727 -12.082 1.00 86.68  ? 256  ARG   D CA  1 
ATOM   10154 C  C   . ARG   D 1 187 ? 43.584  -33.435 -10.752 1.00 84.31  ? 256  ARG   D C   1 
ATOM   10155 O  O   . ARG   D 1 187 ? 44.436  -33.497 -9.853  1.00 82.04  ? 256  ARG   D O   1 
ATOM   10156 C  CB  . ARG   D 1 187 ? 43.387  -31.280 -12.077 1.00 85.19  ? 256  ARG   D CB  1 
ATOM   10157 C  CG  . ARG   D 1 187 ? 43.821  -30.458 -13.270 1.00 82.70  ? 256  ARG   D CG  1 
ATOM   10158 C  CD  . ARG   D 1 187 ? 43.861  -28.981 -12.912 1.00 84.35  ? 256  ARG   D CD  1 
ATOM   10159 N  NE  . ARG   D 1 187 ? 42.558  -28.479 -12.494 1.00 85.97  ? 256  ARG   D NE  1 
ATOM   10160 C  CZ  . ARG   D 1 187 ? 42.370  -27.346 -11.825 1.00 93.56  ? 256  ARG   D CZ  1 
ATOM   10161 N  NH1 . ARG   D 1 187 ? 43.381  -26.584 -11.459 1.00 95.90  ? 256  ARG   D NH1 1 
ATOM   10162 N  NH2 . ARG   D 1 187 ? 41.133  -26.964 -11.510 1.00 94.66  ? 256  ARG   D NH2 1 
ATOM   10163 N  N   . ILE   D 1 188 ? 42.375  -33.978 -10.605 1.00 77.93  ? 257  ILE   D N   1 
ATOM   10164 C  CA  . ILE   D 1 188 ? 42.014  -34.646 -9.360  1.00 80.85  ? 257  ILE   D CA  1 
ATOM   10165 C  C   . ILE   D 1 188 ? 42.753  -35.969 -9.212  1.00 84.46  ? 257  ILE   D C   1 
ATOM   10166 O  O   . ILE   D 1 188 ? 43.162  -36.349 -8.107  1.00 85.01  ? 257  ILE   D O   1 
ATOM   10167 C  CB  . ILE   D 1 188 ? 40.498  -34.835 -9.300  1.00 79.78  ? 257  ILE   D CB  1 
ATOM   10168 C  CG1 . ILE   D 1 188 ? 39.862  -33.475 -9.137  1.00 68.43  ? 257  ILE   D CG1 1 
ATOM   10169 C  CG2 . ILE   D 1 188 ? 40.139  -35.814 -8.192  1.00 79.31  ? 257  ILE   D CG2 1 
ATOM   10170 C  CD1 . ILE   D 1 188 ? 38.443  -33.562 -8.768  1.00 73.81  ? 257  ILE   D CD1 1 
ATOM   10171 N  N   . LYS   D 1 189 ? 42.917  -36.699 -10.313 1.00 81.61  ? 258  LYS   D N   1 
ATOM   10172 C  CA  . LYS   D 1 189 ? 43.743  -37.896 -10.292 1.00 79.71  ? 258  LYS   D CA  1 
ATOM   10173 C  C   . LYS   D 1 189 ? 45.161  -37.575 -9.872  1.00 79.68  ? 258  LYS   D C   1 
ATOM   10174 O  O   . LYS   D 1 189 ? 45.724  -38.233 -8.999  1.00 82.97  ? 258  LYS   D O   1 
ATOM   10175 C  CB  . LYS   D 1 189 ? 43.748  -38.548 -11.666 1.00 85.49  ? 258  LYS   D CB  1 
ATOM   10176 C  CG  . LYS   D 1 189 ? 42.680  -39.574 -11.832 1.00 85.07  ? 258  LYS   D CG  1 
ATOM   10177 C  CD  . LYS   D 1 189 ? 42.457  -39.851 -13.311 1.00 92.33  ? 258  LYS   D CD  1 
ATOM   10178 C  CE  . LYS   D 1 189 ? 43.775  -39.863 -14.094 1.00 94.25  ? 258  LYS   D CE  1 
ATOM   10179 N  NZ  . LYS   D 1 189 ? 43.920  -41.109 -14.901 1.00 100.84 ? 258  LYS   D NZ  1 
ATOM   10180 N  N   . LYS   D 1 190 ? 45.772  -36.584 -10.511 1.00 83.82  ? 259  LYS   D N   1 
ATOM   10181 C  CA  . LYS   D 1 190 ? 47.156  -36.255 -10.194 1.00 86.41  ? 259  LYS   D CA  1 
ATOM   10182 C  C   . LYS   D 1 190 ? 47.361  -36.123 -8.690  1.00 87.39  ? 259  LYS   D C   1 
ATOM   10183 O  O   . LYS   D 1 190 ? 48.238  -36.781 -8.116  1.00 88.66  ? 259  LYS   D O   1 
ATOM   10184 C  CB  . LYS   D 1 190 ? 47.575  -34.968 -10.916 1.00 88.87  ? 259  LYS   D CB  1 
ATOM   10185 C  CG  . LYS   D 1 190 ? 47.931  -35.192 -12.389 1.00 92.46  ? 259  LYS   D CG  1 
ATOM   10186 C  CD  . LYS   D 1 190 ? 48.932  -34.146 -12.867 1.00 107.86 ? 259  LYS   D CD  1 
ATOM   10187 C  CE  . LYS   D 1 190 ? 49.299  -34.351 -14.336 1.00 122.52 ? 259  LYS   D CE  1 
ATOM   10188 N  NZ  . LYS   D 1 190 ? 50.299  -33.332 -14.798 1.00 128.72 ? 259  LYS   D NZ  1 
ATOM   10189 N  N   . GLN   D 1 191 ? 46.543  -35.282 -8.033  1.00 84.91  ? 260  GLN   D N   1 
ATOM   10190 C  CA  . GLN   D 1 191 ? 46.653  -35.088 -6.588  1.00 82.70  ? 260  GLN   D CA  1 
ATOM   10191 C  C   . GLN   D 1 191 ? 46.422  -36.394 -5.839  1.00 87.24  ? 260  GLN   D C   1 
ATOM   10192 O  O   . GLN   D 1 191 ? 47.145  -36.708 -4.885  1.00 90.78  ? 260  GLN   D O   1 
ATOM   10193 C  CB  . GLN   D 1 191 ? 45.667  -34.016 -6.107  1.00 85.81  ? 260  GLN   D CB  1 
ATOM   10194 C  CG  . GLN   D 1 191 ? 45.933  -32.617 -6.669  1.00 91.24  ? 260  GLN   D CG  1 
ATOM   10195 C  CD  . GLN   D 1 191 ? 45.462  -31.491 -5.749  1.00 92.40  ? 260  GLN   D CD  1 
ATOM   10196 O  OE1 . GLN   D 1 191 ? 45.796  -31.462 -4.559  1.00 93.30  ? 260  GLN   D OE1 1 
ATOM   10197 N  NE2 . GLN   D 1 191 ? 44.697  -30.548 -6.305  1.00 92.63  ? 260  GLN   D NE2 1 
ATOM   10198 N  N   . LEU   D 1 192 ? 45.425  -37.175 -6.259  1.00 85.40  ? 261  LEU   D N   1 
ATOM   10199 C  CA  . LEU   D 1 192 ? 45.198  -38.464 -5.612  1.00 86.04  ? 261  LEU   D CA  1 
ATOM   10200 C  C   . LEU   D 1 192 ? 46.412  -39.385 -5.725  1.00 87.61  ? 261  LEU   D C   1 
ATOM   10201 O  O   . LEU   D 1 192 ? 46.645  -40.206 -4.831  1.00 89.72  ? 261  LEU   D O   1 
ATOM   10202 C  CB  . LEU   D 1 192 ? 43.972  -39.153 -6.204  1.00 80.06  ? 261  LEU   D CB  1 
ATOM   10203 C  CG  . LEU   D 1 192 ? 42.647  -38.422 -6.052  1.00 83.34  ? 261  LEU   D CG  1 
ATOM   10204 C  CD1 . LEU   D 1 192 ? 41.580  -39.187 -6.838  1.00 82.39  ? 261  LEU   D CD1 1 
ATOM   10205 C  CD2 . LEU   D 1 192 ? 42.260  -38.264 -4.581  1.00 73.93  ? 261  LEU   D CD2 1 
ATOM   10206 N  N   . ARG   D 1 193 ? 47.177  -39.289 -6.821  1.00 88.25  ? 262  ARG   D N   1 
ATOM   10207 C  CA  . ARG   D 1 193 ? 48.392  -40.084 -6.947  1.00 90.33  ? 262  ARG   D CA  1 
ATOM   10208 C  C   . ARG   D 1 193 ? 49.435  -39.663 -5.926  1.00 92.06  ? 262  ARG   D C   1 
ATOM   10209 O  O   . ARG   D 1 193 ? 50.310  -40.464 -5.570  1.00 95.20  ? 262  ARG   D O   1 
ATOM   10210 C  CB  . ARG   D 1 193 ? 48.952  -39.997 -8.368  1.00 82.21  ? 262  ARG   D CB  1 
ATOM   10211 N  N   . GLU   D 1 194 ? 49.348  -38.424 -5.438  1.00 88.58  ? 263  GLU   D N   1 
ATOM   10212 C  CA  . GLU   D 1 194 ? 50.207  -37.996 -4.343  1.00 93.86  ? 263  GLU   D CA  1 
ATOM   10213 C  C   . GLU   D 1 194 ? 49.980  -38.846 -3.094  1.00 93.14  ? 263  GLU   D C   1 
ATOM   10214 O  O   . GLU   D 1 194 ? 50.931  -39.161 -2.363  1.00 87.32  ? 263  GLU   D O   1 
ATOM   10215 C  CB  . GLU   D 1 194 ? 49.955  -36.515 -4.067  1.00 92.75  ? 263  GLU   D CB  1 
ATOM   10216 C  CG  . GLU   D 1 194 ? 50.713  -35.601 -4.968  1.00 93.81  ? 263  GLU   D CG  1 
ATOM   10217 C  CD  . GLU   D 1 194 ? 52.087  -35.295 -4.416  1.00 113.05 ? 263  GLU   D CD  1 
ATOM   10218 O  OE1 . GLU   D 1 194 ? 52.162  -34.532 -3.422  1.00 118.55 ? 263  GLU   D OE1 1 
ATOM   10219 O  OE2 . GLU   D 1 194 ? 53.088  -35.827 -4.961  1.00 116.39 ? 263  GLU   D OE2 1 
ATOM   10220 N  N   . TRP   D 1 195 ? 48.723  -39.205 -2.831  1.00 93.58  ? 264  TRP   D N   1 
ATOM   10221 C  CA  . TRP   D 1 195 ? 48.296  -40.022 -1.700  1.00 92.21  ? 264  TRP   D CA  1 
ATOM   10222 C  C   . TRP   D 1 195 ? 48.407  -41.513 -1.956  1.00 97.48  ? 264  TRP   D C   1 
ATOM   10223 O  O   . TRP   D 1 195 ? 48.059  -42.311 -1.078  1.00 100.29 ? 264  TRP   D O   1 
ATOM   10224 C  CB  . TRP   D 1 195 ? 46.839  -39.719 -1.348  1.00 91.16  ? 264  TRP   D CB  1 
ATOM   10225 C  CG  . TRP   D 1 195 ? 46.624  -38.314 -0.982  1.00 89.43  ? 264  TRP   D CG  1 
ATOM   10226 C  CD1 . TRP   D 1 195 ? 47.583  -37.388 -0.690  1.00 87.39  ? 264  TRP   D CD1 1 
ATOM   10227 C  CD2 . TRP   D 1 195 ? 45.368  -37.647 -0.860  1.00 83.04  ? 264  TRP   D CD2 1 
ATOM   10228 N  NE1 . TRP   D 1 195 ? 46.999  -36.185 -0.392  1.00 89.02  ? 264  TRP   D NE1 1 
ATOM   10229 C  CE2 . TRP   D 1 195 ? 45.639  -36.320 -0.489  1.00 86.14  ? 264  TRP   D CE2 1 
ATOM   10230 C  CE3 . TRP   D 1 195 ? 44.040  -38.046 -1.025  1.00 80.68  ? 264  TRP   D CE3 1 
ATOM   10231 C  CZ2 . TRP   D 1 195 ? 44.632  -35.387 -0.278  1.00 92.00  ? 264  TRP   D CZ2 1 
ATOM   10232 C  CZ3 . TRP   D 1 195 ? 43.039  -37.116 -0.819  1.00 81.79  ? 264  TRP   D CZ3 1 
ATOM   10233 C  CH2 . TRP   D 1 195 ? 43.340  -35.803 -0.452  1.00 87.31  ? 264  TRP   D CH2 1 
ATOM   10234 N  N   . ASP   D 1 196 ? 48.839  -41.919 -3.139  1.00 98.03  ? 265  ASP   D N   1 
ATOM   10235 C  CA  . ASP   D 1 196 ? 48.767  -43.338 -3.433  1.00 102.71 ? 265  ASP   D CA  1 
ATOM   10236 C  C   . ASP   D 1 196 ? 49.430  -43.557 -4.781  1.00 111.49 ? 265  ASP   D C   1 
ATOM   10237 O  O   . ASP   D 1 196 ? 49.256  -42.754 -5.703  1.00 108.92 ? 265  ASP   D O   1 
ATOM   10238 C  CB  . ASP   D 1 196 ? 47.319  -43.810 -3.307  1.00 103.12 ? 265  ASP   D CB  1 
ATOM   10239 C  CG  . ASP   D 1 196 ? 47.149  -45.249 -3.675  1.00 101.83 ? 265  ASP   D CG  1 
ATOM   10240 O  OD1 . ASP   D 1 196 ? 48.181  -45.913 -3.827  1.00 106.40 ? 265  ASP   D OD1 1 
ATOM   10241 O  OD2 . ASP   D 1 196 ? 45.994  -45.711 -3.819  1.00 103.15 ? 265  ASP   D OD2 1 
ATOM   10242 N  N   . GLU   D 1 197 ? 50.185  -44.646 -4.899  1.00 117.41 ? 266  GLU   D N   1 
ATOM   10243 C  CA  . GLU   D 1 197 ? 50.717  -45.088 -6.183  1.00 120.12 ? 266  GLU   D CA  1 
ATOM   10244 C  C   . GLU   D 1 197 ? 49.723  -46.154 -6.645  1.00 118.93 ? 266  GLU   D C   1 
ATOM   10245 O  O   . GLU   D 1 197 ? 49.875  -47.358 -6.419  1.00 112.35 ? 266  GLU   D O   1 
ATOM   10246 C  CB  . GLU   D 1 197 ? 52.143  -45.592 -6.058  1.00 124.67 ? 266  GLU   D CB  1 
ATOM   10247 C  CG  . GLU   D 1 197 ? 53.131  -44.436 -5.792  1.00 127.74 ? 266  GLU   D CG  1 
ATOM   10248 C  CD  . GLU   D 1 197 ? 53.486  -43.657 -7.057  1.00 135.63 ? 266  GLU   D CD  1 
ATOM   10249 O  OE1 . GLU   D 1 197 ? 54.590  -43.062 -7.110  1.00 145.32 ? 266  GLU   D OE1 1 
ATOM   10250 O  OE2 . GLU   D 1 197 ? 52.664  -43.653 -8.001  1.00 131.66 ? 266  GLU   D OE2 1 
ATOM   10251 N  N   . ASN   D 1 198 ? 48.637  -45.670 -7.249  1.00 123.48 ? 267  ASN   D N   1 
ATOM   10252 C  CA  . ASN   D 1 198 ? 47.555  -46.592 -7.678  1.00 122.80 ? 267  ASN   D CA  1 
ATOM   10253 C  C   . ASN   D 1 198 ? 47.494  -46.661 -9.199  1.00 125.84 ? 267  ASN   D C   1 
ATOM   10254 O  O   . ASN   D 1 198 ? 48.516  -46.373 -9.852  1.00 129.32 ? 267  ASN   D O   1 
ATOM   10255 C  CB  . ASN   D 1 198 ? 46.193  -46.126 -7.185  1.00 120.71 ? 267  ASN   D CB  1 
ATOM   10256 N  N   . LEU   D 1 199 ? 46.324  -47.005 -9.733  1.00 119.65 ? 268  LEU   D N   1 
ATOM   10257 C  CA  . LEU   D 1 199 ? 46.208  -47.188 -11.197 1.00 117.65 ? 268  LEU   D CA  1 
ATOM   10258 C  C   . LEU   D 1 199 ? 45.215  -46.176 -11.767 1.00 120.37 ? 268  LEU   D C   1 
ATOM   10259 O  O   . LEU   D 1 199 ? 44.435  -45.611 -10.982 1.00 118.34 ? 268  LEU   D O   1 
ATOM   10260 C  CB  . LEU   D 1 199 ? 45.745  -48.621 -11.436 1.00 112.81 ? 268  LEU   D CB  1 
ATOM   10261 N  N   . LYS   D 1 200 ? 45.271  -45.943 -13.077 1.00 120.82 ? 269  LYS   D N   1 
ATOM   10262 C  CA  . LYS   D 1 200 ? 44.287  -45.048 -13.729 1.00 112.79 ? 269  LYS   D CA  1 
ATOM   10263 C  C   . LYS   D 1 200 ? 43.203  -45.944 -14.326 1.00 115.64 ? 269  LYS   D C   1 
ATOM   10264 O  O   . LYS   D 1 200 ? 42.028  -45.532 -14.355 1.00 116.11 ? 269  LYS   D O   1 
ATOM   10265 C  CB  . LYS   D 1 200 ? 44.989  -44.231 -14.813 1.00 104.57 ? 269  LYS   D CB  1 
ATOM   10266 N  N   . ASP   D 1 201 ? 43.598  -47.141 -14.754 1.00 116.23 ? 270  ASP   D N   1 
ATOM   10267 C  CA  . ASP   D 1 201 ? 42.623  -48.101 -15.332 1.00 122.49 ? 270  ASP   D CA  1 
ATOM   10268 C  C   . ASP   D 1 201 ? 41.659  -48.536 -14.232 1.00 124.98 ? 270  ASP   D C   1 
ATOM   10269 O  O   . ASP   D 1 201 ? 42.100  -48.589 -13.072 1.00 118.13 ? 270  ASP   D O   1 
ATOM   10270 C  CB  . ASP   D 1 201 ? 43.327  -49.291 -15.962 1.00 123.60 ? 270  ASP   D CB  1 
ATOM   10271 C  CG  . ASP   D 1 201 ? 44.079  -49.008 -17.254 1.00 129.79 ? 270  ASP   D CG  1 
ATOM   10272 O  OD1 . ASP   D 1 201 ? 43.839  -47.936 -17.847 1.00 131.54 ? 270  ASP   D OD1 1 
ATOM   10273 O  OD2 . ASP   D 1 201 ? 44.897  -49.861 -17.654 1.00 135.21 ? 270  ASP   D OD2 1 
ATOM   10274 N  N   . ASP   D 1 202 ? 40.410  -48.839 -14.592 1.00 145.01 ? 271  ASP   D N   1 
ATOM   10275 C  CA  . ASP   D 1 202 ? 39.410  -49.330 -13.605 1.00 146.20 ? 271  ASP   D CA  1 
ATOM   10276 C  C   . ASP   D 1 202 ? 39.382  -48.377 -12.412 1.00 145.03 ? 271  ASP   D C   1 
ATOM   10277 O  O   . ASP   D 1 202 ? 38.495  -47.510 -12.393 1.00 143.84 ? 271  ASP   D O   1 
ATOM   10278 C  CB  . ASP   D 1 202 ? 39.695  -50.768 -13.198 1.00 148.48 ? 271  ASP   D CB  1 
ATOM   10279 N  N   . SER   D 1 203 ? 40.292  -48.557 -11.456 1.00 119.84 ? 272  SER   D N   1 
ATOM   10280 C  CA  . SER   D 1 203 ? 40.400  -47.663 -10.278 1.00 109.40 ? 272  SER   D CA  1 
ATOM   10281 C  C   . SER   D 1 203 ? 39.311  -46.590 -10.291 1.00 109.46 ? 272  SER   D C   1 
ATOM   10282 O  O   . SER   D 1 203 ? 38.311  -46.756 -9.566  1.00 109.28 ? 272  SER   D O   1 
ATOM   10283 C  CB  . SER   D 1 203 ? 41.744  -47.020 -10.258 1.00 109.35 ? 272  SER   D CB  1 
ATOM   10284 O  OG  . SER   D 1 203 ? 42.749  -48.004 -10.065 1.00 114.28 ? 272  SER   D OG  1 
ATOM   10285 N  N   . LEU   D 1 204 ? 39.505  -45.533 -11.076 1.00 106.49 ? 273  LEU   D N   1 
ATOM   10286 C  CA  . LEU   D 1 204 ? 38.545  -44.405 -11.034 1.00 94.78  ? 273  LEU   D CA  1 
ATOM   10287 C  C   . LEU   D 1 204 ? 37.629  -44.415 -12.263 1.00 91.45  ? 273  LEU   D C   1 
ATOM   10288 O  O   . LEU   D 1 204 ? 38.109  -44.730 -13.366 1.00 90.19  ? 273  LEU   D O   1 
ATOM   10289 C  CB  . LEU   D 1 204 ? 39.384  -43.139 -10.925 1.00 96.75  ? 273  LEU   D CB  1 
ATOM   10290 C  CG  . LEU   D 1 204 ? 39.993  -42.881 -9.545  1.00 89.91  ? 273  LEU   D CG  1 
ATOM   10291 C  CD1 . LEU   D 1 204 ? 41.387  -42.303 -9.676  1.00 85.31  ? 273  LEU   D CD1 1 
ATOM   10292 C  CD2 . LEU   D 1 204 ? 39.097  -41.967 -8.732  1.00 95.44  ? 273  LEU   D CD2 1 
ATOM   10293 N  N   . PRO   D 1 205 ? 36.336  -44.061 -12.109 1.00 87.95  ? 274  PRO   D N   1 
ATOM   10294 C  CA  . PRO   D 1 205 ? 35.392  -44.088 -13.217 1.00 88.41  ? 274  PRO   D CA  1 
ATOM   10295 C  C   . PRO   D 1 205 ? 35.760  -43.175 -14.376 1.00 90.47  ? 274  PRO   D C   1 
ATOM   10296 O  O   . PRO   D 1 205 ? 36.623  -42.295 -14.221 1.00 93.22  ? 274  PRO   D O   1 
ATOM   10297 C  CB  . PRO   D 1 205 ? 34.099  -43.632 -12.531 1.00 83.16  ? 274  PRO   D CB  1 
ATOM   10298 C  CG  . PRO   D 1 205 ? 34.296  -43.981 -11.081 1.00 85.25  ? 274  PRO   D CG  1 
ATOM   10299 C  CD  . PRO   D 1 205 ? 35.748  -43.629 -10.857 1.00 91.86  ? 274  PRO   D CD  1 
ATOM   10300 N  N   . SER   D 1 206 ? 35.100  -43.363 -15.522 1.00 96.12  ? 275  SER   D N   1 
ATOM   10301 C  CA  . SER   D 1 206 ? 35.425  -42.559 -16.689 1.00 96.93  ? 275  SER   D CA  1 
ATOM   10302 C  C   . SER   D 1 206 ? 34.395  -41.470 -16.927 1.00 91.77  ? 275  SER   D C   1 
ATOM   10303 O  O   . SER   D 1 206 ? 34.757  -40.336 -17.237 1.00 93.03  ? 275  SER   D O   1 
ATOM   10304 C  CB  . SER   D 1 206 ? 35.556  -43.444 -17.939 1.00 96.84  ? 275  SER   D CB  1 
ATOM   10305 O  OG  . SER   D 1 206 ? 34.280  -43.830 -18.415 1.00 104.14 ? 275  SER   D OG  1 
ATOM   10306 N  N   . ASN   D 1 207 ? 33.118  -41.799 -16.773 1.00 89.04  ? 276  ASN   D N   1 
ATOM   10307 C  CA  . ASN   D 1 207 ? 32.071  -40.796 -16.855 1.00 86.78  ? 276  ASN   D CA  1 
ATOM   10308 C  C   . ASN   D 1 207 ? 32.280  -39.787 -15.741 1.00 90.96  ? 276  ASN   D C   1 
ATOM   10309 O  O   . ASN   D 1 207 ? 32.488  -40.192 -14.590 1.00 92.21  ? 276  ASN   D O   1 
ATOM   10310 C  CB  . ASN   D 1 207 ? 30.695  -41.435 -16.722 1.00 92.25  ? 276  ASN   D CB  1 
ATOM   10311 C  CG  . ASN   D 1 207 ? 29.596  -40.409 -16.596 1.00 92.21  ? 276  ASN   D CG  1 
ATOM   10312 O  OD1 . ASN   D 1 207 ? 29.641  -39.537 -15.728 1.00 94.54  ? 276  ASN   D OD1 1 
ATOM   10313 N  ND2 . ASN   D 1 207 ? 28.604  -40.493 -17.481 1.00 100.56 ? 276  ASN   D ND2 1 
ATOM   10314 N  N   . PRO   D 1 208 ? 32.240  -38.478 -16.030 1.00 90.33  ? 277  PRO   D N   1 
ATOM   10315 C  CA  . PRO   D 1 208 ? 32.539  -37.500 -14.980 1.00 90.13  ? 277  PRO   D CA  1 
ATOM   10316 C  C   . PRO   D 1 208 ? 31.468  -37.433 -13.915 1.00 89.14  ? 277  PRO   D C   1 
ATOM   10317 O  O   . PRO   D 1 208 ? 31.783  -37.040 -12.783 1.00 87.29  ? 277  PRO   D O   1 
ATOM   10318 C  CB  . PRO   D 1 208 ? 32.662  -36.175 -15.750 1.00 88.81  ? 277  PRO   D CB  1 
ATOM   10319 C  CG  . PRO   D 1 208 ? 32.704  -36.560 -17.165 1.00 88.64  ? 277  PRO   D CG  1 
ATOM   10320 C  CD  . PRO   D 1 208 ? 31.884  -37.794 -17.271 1.00 89.20  ? 277  PRO   D CD  1 
ATOM   10321 N  N   . ILE   D 1 209 ? 30.221  -37.804 -14.232 1.00 87.54  ? 278  ILE   D N   1 
ATOM   10322 C  CA  . ILE   D 1 209 ? 29.227  -37.966 -13.176 1.00 86.80  ? 278  ILE   D CA  1 
ATOM   10323 C  C   . ILE   D 1 209 ? 29.754  -38.937 -12.123 1.00 90.07  ? 278  ILE   D C   1 
ATOM   10324 O  O   . ILE   D 1 209 ? 29.954  -38.574 -10.957 1.00 93.39  ? 278  ILE   D O   1 
ATOM   10325 C  CB  . ILE   D 1 209 ? 27.866  -38.418 -13.738 1.00 84.12  ? 278  ILE   D CB  1 
ATOM   10326 C  CG1 . ILE   D 1 209 ? 27.265  -37.349 -14.654 1.00 93.90  ? 278  ILE   D CG1 1 
ATOM   10327 C  CG2 . ILE   D 1 209 ? 26.897  -38.610 -12.610 1.00 85.06  ? 278  ILE   D CG2 1 
ATOM   10328 C  CD1 . ILE   D 1 209 ? 27.787  -37.394 -16.121 1.00 95.94  ? 278  ILE   D CD1 1 
ATOM   10329 N  N   . ASP   D 1 210 ? 30.050  -40.169 -12.529 1.00 89.26  ? 279  ASP   D N   1 
ATOM   10330 C  CA  . ASP   D 1 210 ? 30.436  -41.182 -11.545 1.00 88.54  ? 279  ASP   D CA  1 
ATOM   10331 C  C   . ASP   D 1 210 ? 31.757  -40.853 -10.861 1.00 87.57  ? 279  ASP   D C   1 
ATOM   10332 O  O   . ASP   D 1 210 ? 31.951  -41.181 -9.682  1.00 87.86  ? 279  ASP   D O   1 
ATOM   10333 C  CB  . ASP   D 1 210 ? 30.510  -42.546 -12.215 1.00 87.62  ? 279  ASP   D CB  1 
ATOM   10334 C  CG  . ASP   D 1 210 ? 29.216  -42.909 -12.904 1.00 93.23  ? 279  ASP   D CG  1 
ATOM   10335 O  OD1 . ASP   D 1 210 ? 28.137  -42.640 -12.315 1.00 94.32  ? 279  ASP   D OD1 1 
ATOM   10336 O  OD2 . ASP   D 1 210 ? 29.275  -43.447 -14.036 1.00 99.52  ? 279  ASP   D OD2 1 
ATOM   10337 N  N   . PHE   D 1 211 ? 32.676  -40.213 -11.585 1.00 88.08  ? 280  PHE   D N   1 
ATOM   10338 C  CA  . PHE   D 1 211 ? 33.946  -39.823 -10.987 1.00 85.71  ? 280  PHE   D CA  1 
ATOM   10339 C  C   . PHE   D 1 211 ? 33.728  -38.771 -9.908  1.00 87.14  ? 280  PHE   D C   1 
ATOM   10340 O  O   . PHE   D 1 211 ? 34.345  -38.838 -8.840  1.00 88.05  ? 280  PHE   D O   1 
ATOM   10341 C  CB  . PHE   D 1 211 ? 34.904  -39.328 -12.075 1.00 84.75  ? 280  PHE   D CB  1 
ATOM   10342 C  CG  . PHE   D 1 211 ? 36.272  -38.932 -11.577 1.00 85.77  ? 280  PHE   D CG  1 
ATOM   10343 C  CD1 . PHE   D 1 211 ? 36.461  -37.713 -10.910 1.00 84.78  ? 280  PHE   D CD1 1 
ATOM   10344 C  CD2 . PHE   D 1 211 ? 37.382  -39.744 -11.823 1.00 82.24  ? 280  PHE   D CD2 1 
ATOM   10345 C  CE1 . PHE   D 1 211 ? 37.728  -37.323 -10.461 1.00 81.89  ? 280  PHE   D CE1 1 
ATOM   10346 C  CE2 . PHE   D 1 211 ? 38.655  -39.361 -11.382 1.00 84.43  ? 280  PHE   D CE2 1 
ATOM   10347 C  CZ  . PHE   D 1 211 ? 38.823  -38.144 -10.695 1.00 83.51  ? 280  PHE   D CZ  1 
ATOM   10348 N  N   . SER   D 1 212 ? 32.842  -37.801 -10.149 1.00 83.72  ? 281  SER   D N   1 
ATOM   10349 C  CA  . SER   D 1 212 ? 32.573  -36.812 -9.110  1.00 84.18  ? 281  SER   D CA  1 
ATOM   10350 C  C   . SER   D 1 212 ? 32.106  -37.485 -7.825  1.00 85.72  ? 281  SER   D C   1 
ATOM   10351 O  O   . SER   D 1 212 ? 32.560  -37.133 -6.727  1.00 82.98  ? 281  SER   D O   1 
ATOM   10352 C  CB  . SER   D 1 212 ? 31.532  -35.800 -9.573  1.00 84.37  ? 281  SER   D CB  1 
ATOM   10353 O  OG  . SER   D 1 212 ? 30.266  -36.416 -9.682  1.00 86.59  ? 281  SER   D OG  1 
ATOM   10354 N  N   . TYR   D 1 213 ? 31.190  -38.456 -7.933  1.00 86.08  ? 282  TYR   D N   1 
ATOM   10355 C  CA  . TYR   D 1 213 ? 30.655  -39.069 -6.719  1.00 84.54  ? 282  TYR   D CA  1 
ATOM   10356 C  C   . TYR   D 1 213 ? 31.647  -40.015 -6.076  1.00 82.07  ? 282  TYR   D C   1 
ATOM   10357 O  O   . TYR   D 1 213 ? 31.602  -40.209 -4.852  1.00 80.33  ? 282  TYR   D O   1 
ATOM   10358 C  CB  . TYR   D 1 213 ? 29.345  -39.806 -7.002  1.00 85.25  ? 282  TYR   D CB  1 
ATOM   10359 C  CG  . TYR   D 1 213 ? 28.188  -38.891 -7.375  1.00 84.17  ? 282  TYR   D CG  1 
ATOM   10360 C  CD1 . TYR   D 1 213 ? 27.687  -37.971 -6.472  1.00 83.88  ? 282  TYR   D CD1 1 
ATOM   10361 C  CD2 . TYR   D 1 213 ? 27.589  -38.968 -8.625  1.00 86.76  ? 282  TYR   D CD2 1 
ATOM   10362 C  CE1 . TYR   D 1 213 ? 26.632  -37.144 -6.803  1.00 85.35  ? 282  TYR   D CE1 1 
ATOM   10363 C  CE2 . TYR   D 1 213 ? 26.534  -38.152 -8.967  1.00 87.19  ? 282  TYR   D CE2 1 
ATOM   10364 C  CZ  . TYR   D 1 213 ? 26.055  -37.240 -8.054  1.00 88.22  ? 282  TYR   D CZ  1 
ATOM   10365 O  OH  . TYR   D 1 213 ? 24.998  -36.429 -8.403  1.00 95.27  ? 282  TYR   D OH  1 
ATOM   10366 N  N   . ARG   D 1 214 ? 32.551  -40.594 -6.870  1.00 83.18  ? 283  ARG   D N   1 
ATOM   10367 C  CA  . ARG   D 1 214 ? 33.586  -41.436 -6.289  1.00 86.60  ? 283  ARG   D CA  1 
ATOM   10368 C  C   . ARG   D 1 214 ? 34.524  -40.604 -5.419  1.00 86.59  ? 283  ARG   D C   1 
ATOM   10369 O  O   . ARG   D 1 214 ? 34.880  -41.011 -4.306  1.00 86.03  ? 283  ARG   D O   1 
ATOM   10370 C  CB  . ARG   D 1 214 ? 34.349  -42.156 -7.401  1.00 87.01  ? 283  ARG   D CB  1 
ATOM   10371 C  CG  . ARG   D 1 214 ? 35.559  -42.903 -6.885  1.00 89.86  ? 283  ARG   D CG  1 
ATOM   10372 C  CD  . ARG   D 1 214 ? 35.117  -44.131 -6.138  1.00 94.49  ? 283  ARG   D CD  1 
ATOM   10373 N  NE  . ARG   D 1 214 ? 34.665  -45.132 -7.094  1.00 96.26  ? 283  ARG   D NE  1 
ATOM   10374 C  CZ  . ARG   D 1 214 ? 35.493  -45.867 -7.826  1.00 100.01 ? 283  ARG   D CZ  1 
ATOM   10375 N  NH1 . ARG   D 1 214 ? 36.810  -45.748 -7.701  1.00 99.83  ? 283  ARG   D NH1 1 
ATOM   10376 N  NH2 . ARG   D 1 214 ? 34.992  -46.730 -8.711  1.00 96.07  ? 283  ARG   D NH2 1 
ATOM   10377 N  N   . VAL   D 1 215 ? 34.901  -39.414 -5.904  1.00 87.17  ? 284  VAL   D N   1 
ATOM   10378 C  CA  . VAL   D 1 215 ? 35.788  -38.519 -5.166  1.00 80.09  ? 284  VAL   D CA  1 
ATOM   10379 C  C   . VAL   D 1 215 ? 35.109  -38.007 -3.904  1.00 79.17  ? 284  VAL   D C   1 
ATOM   10380 O  O   . VAL   D 1 215 ? 35.750  -37.852 -2.861  1.00 81.77  ? 284  VAL   D O   1 
ATOM   10381 C  CB  . VAL   D 1 215 ? 36.246  -37.378 -6.093  1.00 81.16  ? 284  VAL   D CB  1 
ATOM   10382 C  CG1 . VAL   D 1 215 ? 37.300  -36.468 -5.428  1.00 78.35  ? 284  VAL   D CG1 1 
ATOM   10383 C  CG2 . VAL   D 1 215 ? 36.753  -37.970 -7.418  1.00 84.63  ? 284  VAL   D CG2 1 
ATOM   10384 N  N   . ALA   D 1 216 ? 33.811  -37.725 -3.967  1.00 76.26  ? 285  ALA   D N   1 
ATOM   10385 C  CA  . ALA   D 1 216 ? 33.111  -37.381 -2.734  1.00 78.64  ? 285  ALA   D CA  1 
ATOM   10386 C  C   . ALA   D 1 216 ? 33.306  -38.463 -1.684  1.00 86.46  ? 285  ALA   D C   1 
ATOM   10387 O  O   . ALA   D 1 216 ? 33.512  -38.165 -0.495  1.00 87.80  ? 285  ALA   D O   1 
ATOM   10388 C  CB  . ALA   D 1 216 ? 31.619  -37.165 -2.992  1.00 80.95  ? 285  ALA   D CB  1 
ATOM   10389 N  N   . ALA   D 1 217 ? 33.285  -39.733 -2.119  1.00 90.10  ? 286  ALA   D N   1 
ATOM   10390 C  CA  . ALA   D 1 217 ? 33.354  -40.884 -1.226  1.00 82.40  ? 286  ALA   D CA  1 
ATOM   10391 C  C   . ALA   D 1 217 ? 34.763  -41.203 -0.732  1.00 79.55  ? 286  ALA   D C   1 
ATOM   10392 O  O   . ALA   D 1 217 ? 34.901  -41.872 0.292   1.00 89.81  ? 286  ALA   D O   1 
ATOM   10393 C  CB  . ALA   D 1 217 ? 32.764  -42.105 -1.923  1.00 82.93  ? 286  ALA   D CB  1 
ATOM   10394 N  N   . CYS   D 1 218 ? 35.806  -40.745 -1.409  1.00 81.96  ? 287  CYS   D N   1 
ATOM   10395 C  CA  . CYS   D 1 218 ? 37.166  -41.067 -1.008  1.00 82.91  ? 287  CYS   D CA  1 
ATOM   10396 C  C   . CYS   D 1 218 ? 37.870  -39.951 -0.243  1.00 86.13  ? 287  CYS   D C   1 
ATOM   10397 O  O   . CYS   D 1 218 ? 38.834  -40.230 0.472   1.00 91.83  ? 287  CYS   D O   1 
ATOM   10398 C  CB  . CYS   D 1 218 ? 37.979  -41.461 -2.240  1.00 89.15  ? 287  CYS   D CB  1 
ATOM   10399 S  SG  . CYS   D 1 218 ? 37.296  -42.984 -3.052  1.00 127.44 ? 287  CYS   D SG  1 
ATOM   10400 N  N   . LEU   D 1 219 ? 37.407  -38.729 -0.336  1.00 84.33  ? 288  LEU   D N   1 
ATOM   10401 C  CA  . LEU   D 1 219 ? 38.026  -37.608 0.360   1.00 81.46  ? 288  LEU   D CA  1 
ATOM   10402 C  C   . LEU   D 1 219 ? 37.819  -37.718 1.870   1.00 84.53  ? 288  LEU   D C   1 
ATOM   10403 O  O   . LEU   D 1 219 ? 36.730  -38.087 2.328   1.00 86.17  ? 288  LEU   D O   1 
ATOM   10404 C  CB  . LEU   D 1 219 ? 37.448  -36.283 -0.141  1.00 80.59  ? 288  LEU   D CB  1 
ATOM   10405 C  CG  . LEU   D 1 219 ? 38.237  -35.700 -1.314  1.00 81.08  ? 288  LEU   D CG  1 
ATOM   10406 C  CD1 . LEU   D 1 219 ? 38.750  -36.838 -2.151  1.00 79.24  ? 288  LEU   D CD1 1 
ATOM   10407 C  CD2 . LEU   D 1 219 ? 37.492  -34.664 -2.185  1.00 81.13  ? 288  LEU   D CD2 1 
ATOM   10408 N  N   . PRO   D 1 220 ? 38.843  -37.371 2.659   1.00 81.24  ? 289  PRO   D N   1 
ATOM   10409 C  CA  . PRO   D 1 220 ? 38.685  -37.313 4.120   1.00 80.66  ? 289  PRO   D CA  1 
ATOM   10410 C  C   . PRO   D 1 220 ? 37.923  -36.068 4.558   1.00 84.85  ? 289  PRO   D C   1 
ATOM   10411 O  O   . PRO   D 1 220 ? 38.470  -35.206 5.261   1.00 78.03  ? 289  PRO   D O   1 
ATOM   10412 C  CB  . PRO   D 1 220 ? 40.135  -37.302 4.622   1.00 79.13  ? 289  PRO   D CB  1 
ATOM   10413 C  CG  . PRO   D 1 220 ? 40.873  -36.575 3.524   1.00 82.11  ? 289  PRO   D CG  1 
ATOM   10414 C  CD  . PRO   D 1 220 ? 40.173  -36.921 2.218   1.00 80.62  ? 289  PRO   D CD  1 
ATOM   10415 N  N   . ILE   D 1 221 ? 36.661  -35.958 4.125   1.00 84.78  ? 290  ILE   D N   1 
ATOM   10416 C  CA  . ILE   D 1 221 ? 35.805  -34.822 4.453   1.00 81.57  ? 290  ILE   D CA  1 
ATOM   10417 C  C   . ILE   D 1 221 ? 34.775  -35.261 5.477   1.00 82.09  ? 290  ILE   D C   1 
ATOM   10418 O  O   . ILE   D 1 221 ? 34.470  -36.451 5.620   1.00 78.54  ? 290  ILE   D O   1 
ATOM   10419 C  CB  . ILE   D 1 221 ? 35.086  -34.225 3.224   1.00 82.63  ? 290  ILE   D CB  1 
ATOM   10420 C  CG1 . ILE   D 1 221 ? 34.269  -35.305 2.536   1.00 88.59  ? 290  ILE   D CG1 1 
ATOM   10421 C  CG2 . ILE   D 1 221 ? 36.064  -33.680 2.219   1.00 81.13  ? 290  ILE   D CG2 1 
ATOM   10422 C  CD1 . ILE   D 1 221 ? 33.931  -34.942 1.125   1.00 89.27  ? 290  ILE   D CD1 1 
ATOM   10423 N  N   . ASP   D 1 222 ? 34.239  -34.275 6.191   1.00 85.47  ? 291  ASP   D N   1 
ATOM   10424 C  CA  . ASP   D 1 222 ? 33.214  -34.485 7.193   1.00 87.95  ? 291  ASP   D CA  1 
ATOM   10425 C  C   . ASP   D 1 222 ? 31.855  -34.532 6.502   1.00 88.10  ? 291  ASP   D C   1 
ATOM   10426 O  O   . ASP   D 1 222 ? 31.738  -34.284 5.297   1.00 88.89  ? 291  ASP   D O   1 
ATOM   10427 C  CB  . ASP   D 1 222 ? 33.262  -33.374 8.230   1.00 86.73  ? 291  ASP   D CB  1 
ATOM   10428 C  CG  . ASP   D 1 222 ? 32.757  -32.056 7.666   1.00 93.31  ? 291  ASP   D CG  1 
ATOM   10429 O  OD1 . ASP   D 1 222 ? 33.135  -31.687 6.519   1.00 91.93  ? 291  ASP   D OD1 1 
ATOM   10430 O  OD2 . ASP   D 1 222 ? 31.955  -31.393 8.356   1.00 96.66  ? 291  ASP   D OD2 1 
ATOM   10431 N  N   . ASP   D 1 223 ? 30.799  -34.820 7.266   1.00 87.90  ? 292  ASP   D N   1 
ATOM   10432 C  CA  . ASP   D 1 223 ? 29.524  -35.097 6.615   1.00 87.83  ? 292  ASP   D CA  1 
ATOM   10433 C  C   . ASP   D 1 223 ? 28.972  -33.858 5.911   1.00 84.90  ? 292  ASP   D C   1 
ATOM   10434 O  O   . ASP   D 1 223 ? 28.438  -33.958 4.797   1.00 81.80  ? 292  ASP   D O   1 
ATOM   10435 C  CB  . ASP   D 1 223 ? 28.531  -35.681 7.625   1.00 92.61  ? 292  ASP   D CB  1 
ATOM   10436 C  CG  . ASP   D 1 223 ? 28.702  -37.206 7.806   1.00 97.52  ? 292  ASP   D CG  1 
ATOM   10437 O  OD1 . ASP   D 1 223 ? 29.137  -37.863 6.828   1.00 95.95  ? 292  ASP   D OD1 1 
ATOM   10438 O  OD2 . ASP   D 1 223 ? 28.408  -37.757 8.903   1.00 95.86  ? 292  ASP   D OD2 1 
ATOM   10439 N  N   . VAL   D 1 224 ? 29.136  -32.674 6.504   1.00 89.00  ? 293  VAL   D N   1 
ATOM   10440 C  CA  . VAL   D 1 224 ? 28.574  -31.470 5.878   1.00 90.81  ? 293  VAL   D CA  1 
ATOM   10441 C  C   . VAL   D 1 224 ? 29.170  -31.246 4.493   1.00 85.59  ? 293  VAL   D C   1 
ATOM   10442 O  O   . VAL   D 1 224 ? 28.465  -30.847 3.558   1.00 82.55  ? 293  VAL   D O   1 
ATOM   10443 C  CB  . VAL   D 1 224 ? 28.764  -30.231 6.769   1.00 79.97  ? 293  VAL   D CB  1 
ATOM   10444 C  CG1 . VAL   D 1 224 ? 28.266  -30.525 8.150   1.00 73.28  ? 293  VAL   D CG1 1 
ATOM   10445 C  CG2 . VAL   D 1 224 ? 30.221  -29.794 6.772   1.00 83.52  ? 293  VAL   D CG2 1 
ATOM   10446 N  N   . LEU   D 1 225 ? 30.472  -31.484 4.336   1.00 85.10  ? 294  LEU   D N   1 
ATOM   10447 C  CA  . LEU   D 1 225 ? 31.067  -31.347 3.009   1.00 87.81  ? 294  LEU   D CA  1 
ATOM   10448 C  C   . LEU   D 1 225 ? 30.577  -32.440 2.058   1.00 86.71  ? 294  LEU   D C   1 
ATOM   10449 O  O   . LEU   D 1 225 ? 30.432  -32.194 0.850   1.00 80.08  ? 294  LEU   D O   1 
ATOM   10450 C  CB  . LEU   D 1 225 ? 32.591  -31.354 3.127   1.00 86.83  ? 294  LEU   D CB  1 
ATOM   10451 C  CG  . LEU   D 1 225 ? 33.249  -30.028 2.753   1.00 81.29  ? 294  LEU   D CG  1 
ATOM   10452 C  CD1 . LEU   D 1 225 ? 32.509  -28.845 3.389   1.00 78.99  ? 294  LEU   D CD1 1 
ATOM   10453 C  CD2 . LEU   D 1 225 ? 34.724  -30.044 3.147   1.00 83.26  ? 294  LEU   D CD2 1 
ATOM   10454 N  N   . ARG   D 1 226 ? 30.310  -33.641 2.599   1.00 82.60  ? 295  ARG   D N   1 
ATOM   10455 C  CA  . ARG   D 1 226 ? 29.687  -34.706 1.820   1.00 81.78  ? 295  ARG   D CA  1 
ATOM   10456 C  C   . ARG   D 1 226 ? 28.304  -34.292 1.320   1.00 83.57  ? 295  ARG   D C   1 
ATOM   10457 O  O   . ARG   D 1 226 ? 27.979  -34.446 0.134   1.00 82.03  ? 295  ARG   D O   1 
ATOM   10458 C  CB  . ARG   D 1 226 ? 29.605  -35.994 2.644   1.00 81.70  ? 295  ARG   D CB  1 
ATOM   10459 C  CG  . ARG   D 1 226 ? 30.791  -36.858 2.416   1.00 81.09  ? 295  ARG   D CG  1 
ATOM   10460 C  CD  . ARG   D 1 226 ? 30.769  -38.138 3.230   1.00 86.03  ? 295  ARG   D CD  1 
ATOM   10461 N  NE  . ARG   D 1 226 ? 31.999  -38.866 2.942   1.00 89.93  ? 295  ARG   D NE  1 
ATOM   10462 C  CZ  . ARG   D 1 226 ? 32.151  -40.178 3.052   1.00 88.10  ? 295  ARG   D CZ  1 
ATOM   10463 N  NH1 . ARG   D 1 226 ? 31.173  -40.956 3.496   1.00 87.18  ? 295  ARG   D NH1 1 
ATOM   10464 N  NH2 . ARG   D 1 226 ? 33.308  -40.725 2.691   1.00 89.34  ? 295  ARG   D NH2 1 
ATOM   10465 N  N   . ILE   D 1 227 ? 27.463  -33.782 2.210   1.00 83.01  ? 296  ILE   D N   1 
ATOM   10466 C  CA  . ILE   D 1 227 ? 26.141  -33.350 1.774   1.00 86.31  ? 296  ILE   D CA  1 
ATOM   10467 C  C   . ILE   D 1 227 ? 26.251  -32.249 0.735   1.00 83.96  ? 296  ILE   D C   1 
ATOM   10468 O  O   . ILE   D 1 227 ? 25.544  -32.257 -0.279  1.00 87.45  ? 296  ILE   D O   1 
ATOM   10469 C  CB  . ILE   D 1 227 ? 25.297  -32.901 2.972   1.00 84.11  ? 296  ILE   D CB  1 
ATOM   10470 C  CG1 . ILE   D 1 227 ? 24.929  -34.147 3.766   1.00 82.81  ? 296  ILE   D CG1 1 
ATOM   10471 C  CG2 . ILE   D 1 227 ? 24.123  -32.074 2.458   1.00 79.79  ? 296  ILE   D CG2 1 
ATOM   10472 C  CD1 . ILE   D 1 227 ? 24.930  -33.932 5.250   1.00 88.38  ? 296  ILE   D CD1 1 
ATOM   10473 N  N   . GLN   D 1 228 ? 27.120  -31.273 0.970   1.00 79.95  ? 297  GLN   D N   1 
ATOM   10474 C  CA  . GLN   D 1 228 ? 27.254  -30.204 -0.006  1.00 83.31  ? 297  GLN   D CA  1 
ATOM   10475 C  C   . GLN   D 1 228 ? 27.512  -30.773 -1.396  1.00 82.77  ? 297  GLN   D C   1 
ATOM   10476 O  O   . GLN   D 1 228 ? 26.776  -30.484 -2.346  1.00 82.20  ? 297  GLN   D O   1 
ATOM   10477 C  CB  . GLN   D 1 228 ? 28.359  -29.236 0.415   1.00 86.10  ? 297  GLN   D CB  1 
ATOM   10478 C  CG  . GLN   D 1 228 ? 27.901  -28.208 1.443   1.00 91.98  ? 297  GLN   D CG  1 
ATOM   10479 C  CD  . GLN   D 1 228 ? 28.936  -27.119 1.702   1.00 96.92  ? 297  GLN   D CD  1 
ATOM   10480 O  OE1 . GLN   D 1 228 ? 29.385  -26.927 2.840   1.00 91.21  ? 297  GLN   D OE1 1 
ATOM   10481 N  NE2 . GLN   D 1 228 ? 29.305  -26.383 0.642   1.00 99.50  ? 297  GLN   D NE2 1 
ATOM   10482 N  N   . LEU   D 1 229 ? 28.550  -31.600 -1.538  1.00 82.45  ? 298  LEU   D N   1 
ATOM   10483 C  CA  . LEU   D 1 229 ? 28.816  -32.191 -2.845  1.00 81.70  ? 298  LEU   D CA  1 
ATOM   10484 C  C   . LEU   D 1 229 ? 27.577  -32.888 -3.394  1.00 85.48  ? 298  LEU   D C   1 
ATOM   10485 O  O   . LEU   D 1 229 ? 27.336  -32.876 -4.613  1.00 87.12  ? 298  LEU   D O   1 
ATOM   10486 C  CB  . LEU   D 1 229 ? 29.983  -33.164 -2.753  1.00 77.30  ? 298  LEU   D CB  1 
ATOM   10487 C  CG  . LEU   D 1 229 ? 31.313  -32.495 -2.461  1.00 74.76  ? 298  LEU   D CG  1 
ATOM   10488 C  CD1 . LEU   D 1 229 ? 32.378  -33.548 -2.277  1.00 79.48  ? 298  LEU   D CD1 1 
ATOM   10489 C  CD2 . LEU   D 1 229 ? 31.657  -31.613 -3.615  1.00 77.86  ? 298  LEU   D CD2 1 
ATOM   10490 N  N   . LEU   D 1 230 ? 26.760  -33.467 -2.509  1.00 81.00  ? 299  LEU   D N   1 
ATOM   10491 C  CA  . LEU   D 1 230 ? 25.547  -34.134 -2.957  1.00 78.83  ? 299  LEU   D CA  1 
ATOM   10492 C  C   . LEU   D 1 230 ? 24.492  -33.145 -3.438  1.00 81.50  ? 299  LEU   D C   1 
ATOM   10493 O  O   . LEU   D 1 230 ? 23.685  -33.475 -4.307  1.00 87.19  ? 299  LEU   D O   1 
ATOM   10494 C  CB  . LEU   D 1 230 ? 25.012  -35.031 -1.845  1.00 79.97  ? 299  LEU   D CB  1 
ATOM   10495 C  CG  . LEU   D 1 230 ? 25.481  -36.481 -2.005  1.00 88.83  ? 299  LEU   D CG  1 
ATOM   10496 C  CD1 . LEU   D 1 230 ? 26.943  -36.537 -2.406  1.00 85.81  ? 299  LEU   D CD1 1 
ATOM   10497 C  CD2 . LEU   D 1 230 ? 25.260  -37.325 -0.748  1.00 93.33  ? 299  LEU   D CD2 1 
ATOM   10498 N  N   . LYS   D 1 231 ? 24.480  -31.930 -2.930  1.00 83.90  ? 300  LYS   D N   1 
ATOM   10499 C  CA  . LYS   D 1 231 ? 23.451  -31.010 -3.389  1.00 82.25  ? 300  LYS   D CA  1 
ATOM   10500 C  C   . LYS   D 1 231 ? 23.869  -30.228 -4.620  1.00 79.53  ? 300  LYS   D C   1 
ATOM   10501 O  O   . LYS   D 1 231 ? 23.009  -29.646 -5.285  1.00 76.55  ? 300  LYS   D O   1 
ATOM   10502 C  CB  . LYS   D 1 231 ? 23.065  -30.051 -2.269  1.00 79.75  ? 300  LYS   D CB  1 
ATOM   10503 C  CG  . LYS   D 1 231 ? 23.422  -30.603 -0.931  1.00 83.58  ? 300  LYS   D CG  1 
ATOM   10504 C  CD  . LYS   D 1 231 ? 22.696  -29.896 0.168   1.00 90.37  ? 300  LYS   D CD  1 
ATOM   10505 C  CE  . LYS   D 1 231 ? 21.190  -30.044 0.023   1.00 97.64  ? 300  LYS   D CE  1 
ATOM   10506 N  NZ  . LYS   D 1 231 ? 20.507  -29.257 1.088   1.00 107.89 ? 300  LYS   D NZ  1 
ATOM   10507 N  N   . ILE   D 1 232 ? 25.164  -30.199 -4.937  1.00 79.24  ? 301  ILE   D N   1 
ATOM   10508 C  CA  . ILE   D 1 232 ? 25.594  -29.558 -6.164  1.00 78.41  ? 301  ILE   D CA  1 
ATOM   10509 C  C   . ILE   D 1 232 ? 24.870  -30.198 -7.349  1.00 87.16  ? 301  ILE   D C   1 
ATOM   10510 O  O   . ILE   D 1 232 ? 24.558  -31.398 -7.349  1.00 87.37  ? 301  ILE   D O   1 
ATOM   10511 C  CB  . ILE   D 1 232 ? 27.122  -29.635 -6.313  1.00 82.08  ? 301  ILE   D CB  1 
ATOM   10512 C  CG1 . ILE   D 1 232 ? 27.812  -28.672 -5.349  1.00 81.35  ? 301  ILE   D CG1 1 
ATOM   10513 C  CG2 . ILE   D 1 232 ? 27.532  -29.367 -7.742  1.00 84.75  ? 301  ILE   D CG2 1 
ATOM   10514 C  CD1 . ILE   D 1 232 ? 29.280  -28.333 -5.707  1.00 84.55  ? 301  ILE   D CD1 1 
ATOM   10515 N  N   . GLY   D 1 233 ? 24.602  -29.380 -8.373  1.00 88.31  ? 302  GLY   D N   1 
ATOM   10516 C  CA  . GLY   D 1 233 ? 23.736  -29.723 -9.484  1.00 90.31  ? 302  GLY   D CA  1 
ATOM   10517 C  C   . GLY   D 1 233 ? 24.396  -30.255 -10.742 1.00 91.45  ? 302  GLY   D C   1 
ATOM   10518 O  O   . GLY   D 1 233 ? 23.688  -30.637 -11.677 1.00 94.40  ? 302  GLY   D O   1 
ATOM   10519 N  N   . SER   D 1 234 ? 25.729  -30.303 -10.803 1.00 88.17  ? 303  SER   D N   1 
ATOM   10520 C  CA  . SER   D 1 234 ? 26.404  -30.799 -11.991 1.00 84.56  ? 303  SER   D CA  1 
ATOM   10521 C  C   . SER   D 1 234 ? 27.759  -31.388 -11.640 1.00 84.66  ? 303  SER   D C   1 
ATOM   10522 O  O   . SER   D 1 234 ? 28.501  -30.838 -10.821 1.00 82.83  ? 303  SER   D O   1 
ATOM   10523 C  CB  . SER   D 1 234 ? 26.602  -29.682 -13.000 1.00 83.56  ? 303  SER   D CB  1 
ATOM   10524 O  OG  . SER   D 1 234 ? 27.530  -28.753 -12.468 1.00 86.23  ? 303  SER   D OG  1 
ATOM   10525 N  N   . ALA   D 1 235 ? 28.089  -32.491 -12.303 1.00 82.72  ? 304  ALA   D N   1 
ATOM   10526 C  CA  . ALA   D 1 235 ? 29.390  -33.097 -12.078 1.00 80.74  ? 304  ALA   D CA  1 
ATOM   10527 C  C   . ALA   D 1 235 ? 30.527  -32.110 -12.326 1.00 80.49  ? 304  ALA   D C   1 
ATOM   10528 O  O   . ALA   D 1 235 ? 31.579  -32.214 -11.688 1.00 84.46  ? 304  ALA   D O   1 
ATOM   10529 C  CB  . ALA   D 1 235 ? 29.543  -34.353 -12.943 1.00 87.82  ? 304  ALA   D CB  1 
ATOM   10530 N  N   . ILE   D 1 236 ? 30.349  -31.136 -13.223 1.00 81.81  ? 305  ILE   D N   1 
ATOM   10531 C  CA  . ILE   D 1 236 ? 31.412  -30.149 -13.423 1.00 79.28  ? 305  ILE   D CA  1 
ATOM   10532 C  C   . ILE   D 1 236 ? 31.598  -29.322 -12.157 1.00 80.67  ? 305  ILE   D C   1 
ATOM   10533 O  O   . ILE   D 1 236 ? 32.714  -29.178 -11.642 1.00 81.42  ? 305  ILE   D O   1 
ATOM   10534 C  CB  . ILE   D 1 236 ? 31.132  -29.241 -14.635 1.00 80.21  ? 305  ILE   D CB  1 
ATOM   10535 C  CG1 . ILE   D 1 236 ? 31.357  -29.966 -15.963 1.00 79.21  ? 305  ILE   D CG1 1 
ATOM   10536 C  CG2 . ILE   D 1 236 ? 32.102  -28.080 -14.600 1.00 82.90  ? 305  ILE   D CG2 1 
ATOM   10537 C  CD1 . ILE   D 1 236 ? 32.772  -29.805 -16.558 1.00 77.01  ? 305  ILE   D CD1 1 
ATOM   10538 N  N   . GLN   D 1 237 ? 30.513  -28.745 -11.648 1.00 80.09  ? 306  GLN   D N   1 
ATOM   10539 C  CA  . GLN   D 1 237 ? 30.634  -27.944 -10.435 1.00 81.50  ? 306  GLN   D CA  1 
ATOM   10540 C  C   . GLN   D 1 237 ? 31.093  -28.796 -9.261  1.00 84.78  ? 306  GLN   D C   1 
ATOM   10541 O  O   . GLN   D 1 237 ? 31.804  -28.298 -8.375  1.00 87.78  ? 306  GLN   D O   1 
ATOM   10542 C  CB  . GLN   D 1 237 ? 29.301  -27.247 -10.129 1.00 81.27  ? 306  GLN   D CB  1 
ATOM   10543 C  CG  . GLN   D 1 237 ? 28.961  -26.146 -11.136 1.00 83.34  ? 306  GLN   D CG  1 
ATOM   10544 C  CD  . GLN   D 1 237 ? 27.514  -25.711 -11.104 1.00 82.69  ? 306  GLN   D CD  1 
ATOM   10545 O  OE1 . GLN   D 1 237 ? 26.595  -26.523 -10.978 1.00 79.94  ? 306  GLN   D OE1 1 
ATOM   10546 N  NE2 . GLN   D 1 237 ? 27.303  -24.405 -11.237 1.00 89.92  ? 306  GLN   D NE2 1 
ATOM   10547 N  N   . ARG   D 1 238 ? 30.719  -30.084 -9.249  1.00 79.71  ? 307  ARG   D N   1 
ATOM   10548 C  CA  . ARG   D 1 238 ? 31.089  -30.950 -8.134  1.00 81.54  ? 307  ARG   D CA  1 
ATOM   10549 C  C   . ARG   D 1 238 ? 32.591  -31.235 -8.140  1.00 81.43  ? 307  ARG   D C   1 
ATOM   10550 O  O   . ARG   D 1 238 ? 33.257  -31.158 -7.094  1.00 79.34  ? 307  ARG   D O   1 
ATOM   10551 C  CB  . ARG   D 1 238 ? 30.272  -32.245 -8.194  1.00 83.89  ? 307  ARG   D CB  1 
ATOM   10552 C  CG  . ARG   D 1 238 ? 30.263  -33.058 -6.903  1.00 84.91  ? 307  ARG   D CG  1 
ATOM   10553 C  CD  . ARG   D 1 238 ? 29.289  -34.224 -6.990  1.00 83.36  ? 307  ARG   D CD  1 
ATOM   10554 N  NE  . ARG   D 1 238 ? 27.968  -33.769 -7.407  1.00 81.54  ? 307  ARG   D NE  1 
ATOM   10555 C  CZ  . ARG   D 1 238 ? 27.416  -34.069 -8.574  1.00 85.11  ? 307  ARG   D CZ  1 
ATOM   10556 N  NH1 . ARG   D 1 238 ? 27.979  -34.940 -9.398  1.00 87.97  ? 307  ARG   D NH1 1 
ATOM   10557 N  NH2 . ARG   D 1 238 ? 26.279  -33.472 -8.933  1.00 87.18  ? 307  ARG   D NH2 1 
ATOM   10558 N  N   . LEU   D 1 239 ? 33.137  -31.553 -9.319  1.00 80.47  ? 308  LEU   D N   1 
ATOM   10559 C  CA  . LEU   D 1 239 ? 34.581  -31.717 -9.481  1.00 77.47  ? 308  LEU   D CA  1 
ATOM   10560 C  C   . LEU   D 1 239 ? 35.329  -30.468 -9.049  1.00 80.00  ? 308  LEU   D C   1 
ATOM   10561 O  O   . LEU   D 1 239 ? 36.287  -30.540 -8.271  1.00 79.13  ? 308  LEU   D O   1 
ATOM   10562 C  CB  . LEU   D 1 239 ? 34.925  -32.046 -10.938 1.00 77.47  ? 308  LEU   D CB  1 
ATOM   10563 C  CG  . LEU   D 1 239 ? 34.446  -33.361 -11.542 1.00 77.97  ? 308  LEU   D CG  1 
ATOM   10564 C  CD1 . LEU   D 1 239 ? 35.283  -33.746 -12.760 1.00 82.52  ? 308  LEU   D CD1 1 
ATOM   10565 C  CD2 . LEU   D 1 239 ? 34.473  -34.462 -10.501 1.00 86.13  ? 308  LEU   D CD2 1 
ATOM   10566 N  N   . ARG   D 1 240 ? 34.926  -29.308 -9.575  1.00 85.22  ? 309  ARG   D N   1 
ATOM   10567 C  CA  . ARG   D 1 240 ? 35.585  -28.060 -9.205  1.00 80.87  ? 309  ARG   D CA  1 
ATOM   10568 C  C   . ARG   D 1 240 ? 35.558  -27.856 -7.700  1.00 82.20  ? 309  ARG   D C   1 
ATOM   10569 O  O   . ARG   D 1 240 ? 36.577  -27.515 -7.085  1.00 81.92  ? 309  ARG   D O   1 
ATOM   10570 C  CB  . ARG   D 1 240 ? 34.924  -26.892 -9.926  1.00 81.08  ? 309  ARG   D CB  1 
ATOM   10571 C  CG  . ARG   D 1 240 ? 35.501  -26.667 -11.300 1.00 77.45  ? 309  ARG   D CG  1 
ATOM   10572 C  CD  . ARG   D 1 240 ? 34.607  -25.741 -12.087 1.00 80.10  ? 309  ARG   D CD  1 
ATOM   10573 N  NE  . ARG   D 1 240 ? 34.386  -24.508 -11.353 1.00 77.06  ? 309  ARG   D NE  1 
ATOM   10574 C  CZ  . ARG   D 1 240 ? 35.178  -23.455 -11.453 1.00 86.15  ? 309  ARG   D CZ  1 
ATOM   10575 N  NH1 . ARG   D 1 240 ? 36.187  -23.433 -12.312 1.00 82.67  ? 309  ARG   D NH1 1 
ATOM   10576 N  NH2 . ARG   D 1 240 ? 34.959  -22.398 -10.667 1.00 96.21  ? 309  ARG   D NH2 1 
ATOM   10577 N  N   . CYS   D 1 241 ? 34.401  -28.081 -7.087  1.00 83.16  ? 310  CYS   D N   1 
ATOM   10578 C  CA  . CYS   D 1 241 ? 34.312  -27.990 -5.638  1.00 82.94  ? 310  CYS   D CA  1 
ATOM   10579 C  C   . CYS   D 1 241 ? 35.261  -28.977 -4.962  1.00 79.56  ? 310  CYS   D C   1 
ATOM   10580 O  O   . CYS   D 1 241 ? 36.025  -28.610 -4.063  1.00 79.61  ? 310  CYS   D O   1 
ATOM   10581 C  CB  . CYS   D 1 241 ? 32.878  -28.249 -5.193  1.00 81.13  ? 310  CYS   D CB  1 
ATOM   10582 S  SG  . CYS   D 1 241 ? 32.739  -27.780 -3.499  1.00 90.43  ? 310  CYS   D SG  1 
ATOM   10583 N  N   . GLU   D 1 242 ? 35.180  -30.253 -5.343  1.00 76.85  ? 311  GLU   D N   1 
ATOM   10584 C  CA  . GLU   D 1 242 ? 36.126  -31.230 -4.827  1.00 77.95  ? 311  GLU   D CA  1 
ATOM   10585 C  C   . GLU   D 1 242 ? 37.549  -30.733 -4.988  1.00 77.55  ? 311  GLU   D C   1 
ATOM   10586 O  O   . GLU   D 1 242 ? 38.317  -30.650 -4.022  1.00 77.13  ? 311  GLU   D O   1 
ATOM   10587 C  CB  . GLU   D 1 242 ? 35.942  -32.563 -5.541  1.00 79.08  ? 311  GLU   D CB  1 
ATOM   10588 C  CG  . GLU   D 1 242 ? 34.851  -33.372 -4.929  1.00 78.50  ? 311  GLU   D CG  1 
ATOM   10589 C  CD  . GLU   D 1 242 ? 34.213  -34.277 -5.931  1.00 82.88  ? 311  GLU   D CD  1 
ATOM   10590 O  OE1 . GLU   D 1 242 ? 34.860  -34.575 -6.968  1.00 81.17  ? 311  GLU   D OE1 1 
ATOM   10591 O  OE2 . GLU   D 1 242 ? 33.058  -34.687 -5.687  1.00 85.00  ? 311  GLU   D OE2 1 
ATOM   10592 N  N   . LEU   D 1 243 ? 37.918  -30.393 -6.213  1.00 80.09  ? 312  LEU   D N   1 
ATOM   10593 C  CA  . LEU   D 1 243 ? 39.241  -29.845 -6.439  1.00 77.93  ? 312  LEU   D CA  1 
ATOM   10594 C  C   . LEU   D 1 243 ? 39.540  -28.716 -5.454  1.00 82.65  ? 312  LEU   D C   1 
ATOM   10595 O  O   . LEU   D 1 243 ? 40.672  -28.591 -4.976  1.00 87.12  ? 312  LEU   D O   1 
ATOM   10596 C  CB  . LEU   D 1 243 ? 39.351  -29.390 -7.895  1.00 75.67  ? 312  LEU   D CB  1 
ATOM   10597 C  CG  . LEU   D 1 243 ? 40.757  -29.473 -8.477  1.00 79.10  ? 312  LEU   D CG  1 
ATOM   10598 C  CD1 . LEU   D 1 243 ? 41.555  -30.565 -7.766  1.00 80.80  ? 312  LEU   D CD1 1 
ATOM   10599 C  CD2 . LEU   D 1 243 ? 40.674  -29.670 -10.001 1.00 76.54  ? 312  LEU   D CD2 1 
ATOM   10600 N  N   . ASP   D 1 244 ? 38.526  -27.911 -5.095  1.00 84.15  ? 313  ASP   D N   1 
ATOM   10601 C  CA  . ASP   D 1 244 ? 38.765  -26.783 -4.186  1.00 83.31  ? 313  ASP   D CA  1 
ATOM   10602 C  C   . ASP   D 1 244 ? 39.001  -27.255 -2.758  1.00 81.78  ? 313  ASP   D C   1 
ATOM   10603 O  O   . ASP   D 1 244 ? 39.799  -26.667 -2.022  1.00 80.25  ? 313  ASP   D O   1 
ATOM   10604 C  CB  . ASP   D 1 244 ? 37.597  -25.792 -4.220  1.00 82.53  ? 313  ASP   D CB  1 
ATOM   10605 C  CG  . ASP   D 1 244 ? 38.073  -24.348 -4.261  1.00 84.33  ? 313  ASP   D CG  1 
ATOM   10606 O  OD1 . ASP   D 1 244 ? 39.227  -24.154 -4.705  1.00 82.77  ? 313  ASP   D OD1 1 
ATOM   10607 O  OD2 . ASP   D 1 244 ? 37.322  -23.419 -3.856  1.00 85.60  ? 313  ASP   D OD2 1 
ATOM   10608 N  N   . ILE   D 1 245 ? 38.306  -28.308 -2.349  1.00 82.14  ? 314  ILE   D N   1 
ATOM   10609 C  CA  . ILE   D 1 245 ? 38.534  -28.858 -1.025  1.00 81.96  ? 314  ILE   D CA  1 
ATOM   10610 C  C   . ILE   D 1 245 ? 39.954  -29.405 -0.921  1.00 82.75  ? 314  ILE   D C   1 
ATOM   10611 O  O   . ILE   D 1 245 ? 40.661  -29.147 0.055   1.00 83.70  ? 314  ILE   D O   1 
ATOM   10612 C  CB  . ILE   D 1 245 ? 37.476  -29.927 -0.713  1.00 79.50  ? 314  ILE   D CB  1 
ATOM   10613 C  CG1 . ILE   D 1 245 ? 36.070  -29.361 -0.936  1.00 75.76  ? 314  ILE   D CG1 1 
ATOM   10614 C  CG2 . ILE   D 1 245 ? 37.653  -30.413 0.698   1.00 82.08  ? 314  ILE   D CG2 1 
ATOM   10615 C  CD1 . ILE   D 1 245 ? 34.998  -30.423 -0.909  1.00 80.26  ? 314  ILE   D CD1 1 
ATOM   10616 N  N   . MET   D 1 246 ? 40.403  -30.153 -1.933  1.00 81.62  ? 315  MET   D N   1 
ATOM   10617 C  CA  . MET   D 1 246 ? 41.734  -30.758 -1.881  1.00 81.56  ? 315  MET   D CA  1 
ATOM   10618 C  C   . MET   D 1 246 ? 42.840  -29.719 -1.920  1.00 86.65  ? 315  MET   D C   1 
ATOM   10619 O  O   . MET   D 1 246 ? 43.975  -30.000 -1.513  1.00 89.37  ? 315  MET   D O   1 
ATOM   10620 C  CB  . MET   D 1 246 ? 41.916  -31.740 -3.028  1.00 80.45  ? 315  MET   D CB  1 
ATOM   10621 C  CG  . MET   D 1 246 ? 40.705  -32.632 -3.218  1.00 83.56  ? 315  MET   D CG  1 
ATOM   10622 S  SD  . MET   D 1 246 ? 40.995  -33.838 -4.523  1.00 91.46  ? 315  MET   D SD  1 
ATOM   10623 C  CE  . MET   D 1 246 ? 42.759  -34.119 -4.310  1.00 83.08  ? 315  MET   D CE  1 
ATOM   10624 N  N   . ASN   D 1 247 ? 42.545  -28.529 -2.405  1.00 85.33  ? 316  ASN   D N   1 
ATOM   10625 C  CA  . ASN   D 1 247 ? 43.569  -27.505 -2.439  1.00 83.56  ? 316  ASN   D CA  1 
ATOM   10626 C  C   . ASN   D 1 247 ? 43.478  -26.551 -1.269  1.00 85.55  ? 316  ASN   D C   1 
ATOM   10627 O  O   . ASN   D 1 247 ? 44.509  -26.039 -0.823  1.00 83.24  ? 316  ASN   D O   1 
ATOM   10628 C  CB  . ASN   D 1 247 ? 43.477  -26.717 -3.745  1.00 85.31  ? 316  ASN   D CB  1 
ATOM   10629 C  CG  . ASN   D 1 247 ? 43.925  -27.518 -4.931  1.00 84.91  ? 316  ASN   D CG  1 
ATOM   10630 O  OD1 . ASN   D 1 247 ? 44.934  -28.204 -4.876  1.00 84.53  ? 316  ASN   D OD1 1 
ATOM   10631 N  ND2 . ASN   D 1 247 ? 43.175  -27.434 -6.020  1.00 88.07  ? 316  ASN   D ND2 1 
ATOM   10632 N  N   . LYS   D 1 248 ? 42.268  -26.314 -0.760  1.00 86.35  ? 317  LYS   D N   1 
ATOM   10633 C  CA  . LYS   D 1 248 ? 42.009  -25.309 0.263   1.00 80.12  ? 317  LYS   D CA  1 
ATOM   10634 C  C   . LYS   D 1 248 ? 41.855  -25.861 1.676   1.00 85.02  ? 317  LYS   D C   1 
ATOM   10635 O  O   . LYS   D 1 248 ? 42.138  -25.138 2.629   1.00 85.87  ? 317  LYS   D O   1 
ATOM   10636 C  CB  . LYS   D 1 248 ? 40.746  -24.514 -0.078  1.00 82.07  ? 317  LYS   D CB  1 
ATOM   10637 C  CG  . LYS   D 1 248 ? 40.934  -23.421 -1.130  1.00 84.67  ? 317  LYS   D CG  1 
ATOM   10638 C  CD  . LYS   D 1 248 ? 39.741  -22.428 -1.138  1.00 87.53  ? 317  LYS   D CD  1 
ATOM   10639 C  CE  . LYS   D 1 248 ? 39.662  -21.616 -2.433  1.00 87.02  ? 317  LYS   D CE  1 
ATOM   10640 N  NZ  . LYS   D 1 248 ? 38.248  -21.271 -2.792  1.00 90.24  ? 317  LYS   D NZ  1 
ATOM   10641 N  N   . CYS   D 1 249 ? 41.393  -27.106 1.845   1.00 88.85  ? 318  CYS   D N   1 
ATOM   10642 C  CA  . CYS   D 1 249 ? 41.135  -27.686 3.176   1.00 85.49  ? 318  CYS   D CA  1 
ATOM   10643 C  C   . CYS   D 1 249 ? 42.278  -28.607 3.593   1.00 83.23  ? 318  CYS   D C   1 
ATOM   10644 O  O   . CYS   D 1 249 ? 42.125  -29.827 3.761   1.00 84.04  ? 318  CYS   D O   1 
ATOM   10645 C  CB  . CYS   D 1 249 ? 39.814  -28.446 3.186   1.00 84.64  ? 318  CYS   D CB  1 
ATOM   10646 S  SG  . CYS   D 1 249 ? 38.405  -27.407 2.938   1.00 92.48  ? 318  CYS   D SG  1 
ATOM   10647 N  N   . THR   D 1 250 ? 43.436  -27.990 3.774   1.00 82.42  ? 319  THR   D N   1 
ATOM   10648 C  CA  . THR   D 1 250 ? 44.682  -28.725 3.919   1.00 87.99  ? 319  THR   D CA  1 
ATOM   10649 C  C   . THR   D 1 250 ? 45.000  -29.075 5.368   1.00 87.85  ? 319  THR   D C   1 
ATOM   10650 O  O   . THR   D 1 250 ? 46.080  -29.609 5.654   1.00 87.89  ? 319  THR   D O   1 
ATOM   10651 C  CB  . THR   D 1 250 ? 45.798  -27.907 3.289   1.00 86.63  ? 319  THR   D CB  1 
ATOM   10652 O  OG1 . THR   D 1 250 ? 45.973  -26.706 4.040   1.00 90.33  ? 319  THR   D OG1 1 
ATOM   10653 C  CG2 . THR   D 1 250 ? 45.382  -27.514 1.906   1.00 84.68  ? 319  THR   D CG2 1 
ATOM   10654 N  N   . SER   D 1 251 ? 44.078  -28.794 6.283   1.00 88.89  ? 320  SER   D N   1 
ATOM   10655 C  CA  . SER   D 1 251 ? 44.251  -29.080 7.700   1.00 89.69  ? 320  SER   D CA  1 
ATOM   10656 C  C   . SER   D 1 251 ? 43.066  -29.898 8.199   1.00 85.58  ? 320  SER   D C   1 
ATOM   10657 O  O   . SER   D 1 251 ? 41.915  -29.544 7.929   1.00 84.16  ? 320  SER   D O   1 
ATOM   10658 C  CB  . SER   D 1 251 ? 44.386  -27.774 8.492   1.00 84.81  ? 320  SER   D CB  1 
ATOM   10659 O  OG  . SER   D 1 251 ? 45.571  -27.091 8.119   1.00 88.19  ? 320  SER   D OG  1 
ATOM   10660 N  N   . LEU   D 1 252 ? 43.346  -30.984 8.928   1.00 83.44  ? 321  LEU   D N   1 
ATOM   10661 C  CA  . LEU   D 1 252 ? 42.320  -31.854 9.498   1.00 87.13  ? 321  LEU   D CA  1 
ATOM   10662 C  C   . LEU   D 1 252 ? 42.264  -31.690 11.019  1.00 87.44  ? 321  LEU   D C   1 
ATOM   10663 O  O   . LEU   D 1 252 ? 43.225  -32.027 11.723  1.00 84.22  ? 321  LEU   D O   1 
ATOM   10664 C  CB  . LEU   D 1 252 ? 42.586  -33.316 9.119   1.00 85.47  ? 321  LEU   D CB  1 
ATOM   10665 C  CG  . LEU   D 1 252 ? 42.433  -33.734 7.652   1.00 78.97  ? 321  LEU   D CG  1 
ATOM   10666 C  CD1 . LEU   D 1 252 ? 42.932  -35.149 7.412   1.00 78.28  ? 321  LEU   D CD1 1 
ATOM   10667 C  CD2 . LEU   D 1 252 ? 40.987  -33.599 7.185   1.00 80.05  ? 321  LEU   D CD2 1 
ATOM   10668 N  N   . CYS   D 1 253 ? 41.124  -31.212 11.526  1.00 84.35  ? 322  CYS   D N   1 
ATOM   10669 C  CA  . CYS   D 1 253 ? 40.952  -30.914 12.944  1.00 90.18  ? 322  CYS   D CA  1 
ATOM   10670 C  C   . CYS   D 1 253 ? 39.896  -31.806 13.584  1.00 88.88  ? 322  CYS   D C   1 
ATOM   10671 O  O   . CYS   D 1 253 ? 39.120  -32.478 12.909  1.00 89.96  ? 322  CYS   D O   1 
ATOM   10672 C  CB  . CYS   D 1 253 ? 40.564  -29.448 13.164  1.00 95.48  ? 322  CYS   D CB  1 
ATOM   10673 S  SG  . CYS   D 1 253 ? 41.499  -28.278 12.191  1.00 94.94  ? 322  CYS   D SG  1 
ATOM   10674 N  N   . CYS   D 1 254 ? 39.877  -31.789 14.920  1.00 93.15  ? 323  CYS   D N   1 
ATOM   10675 C  CA  . CYS   D 1 254 ? 38.919  -32.571 15.690  1.00 89.91  ? 323  CYS   D CA  1 
ATOM   10676 C  C   . CYS   D 1 254 ? 37.522  -32.000 15.488  1.00 93.58  ? 323  CYS   D C   1 
ATOM   10677 O  O   . CYS   D 1 254 ? 37.292  -30.813 15.733  1.00 100.02 ? 323  CYS   D O   1 
ATOM   10678 C  CB  . CYS   D 1 254 ? 39.311  -32.556 17.164  1.00 84.52  ? 323  CYS   D CB  1 
ATOM   10679 S  SG  . CYS   D 1 254 ? 38.027  -33.104 18.294  1.00 85.14  ? 323  CYS   D SG  1 
ATOM   10680 N  N   . LYS   D 1 255 ? 36.577  -32.841 15.056  1.00 91.79  ? 324  LYS   D N   1 
ATOM   10681 C  CA  . LYS   D 1 255 ? 35.247  -32.333 14.734  1.00 91.43  ? 324  LYS   D CA  1 
ATOM   10682 C  C   . LYS   D 1 255 ? 34.488  -31.857 15.966  1.00 97.29  ? 324  LYS   D C   1 
ATOM   10683 O  O   . LYS   D 1 255 ? 33.559  -31.050 15.831  1.00 93.55  ? 324  LYS   D O   1 
ATOM   10684 C  CB  . LYS   D 1 255 ? 34.443  -33.410 14.006  1.00 92.05  ? 324  LYS   D CB  1 
ATOM   10685 C  CG  . LYS   D 1 255 ? 33.039  -32.971 13.584  1.00 94.00  ? 324  LYS   D CG  1 
ATOM   10686 C  CD  . LYS   D 1 255 ? 32.325  -34.101 12.823  1.00 98.08  ? 324  LYS   D CD  1 
ATOM   10687 C  CE  . LYS   D 1 255 ? 31.062  -34.606 13.535  1.00 100.75 ? 324  LYS   D CE  1 
ATOM   10688 N  NZ  . LYS   D 1 255 ? 30.550  -35.876 12.915  1.00 92.04  ? 324  LYS   D NZ  1 
ATOM   10689 N  N   . GLN   D 1 256 ? 34.878  -32.326 17.155  1.00 100.00 ? 325  GLN   D N   1 
ATOM   10690 C  CA  . GLN   D 1 256 ? 34.149  -32.092 18.395  1.00 98.30  ? 325  GLN   D CA  1 
ATOM   10691 C  C   . GLN   D 1 256 ? 34.510  -30.781 19.087  1.00 98.60  ? 325  GLN   D C   1 
ATOM   10692 O  O   . GLN   D 1 256 ? 33.618  -30.081 19.584  1.00 94.38  ? 325  GLN   D O   1 
ATOM   10693 C  CB  . GLN   D 1 256 ? 34.370  -33.267 19.342  1.00 96.60  ? 325  GLN   D CB  1 
ATOM   10694 C  CG  . GLN   D 1 256 ? 33.462  -34.425 18.996  1.00 103.63 ? 325  GLN   D CG  1 
ATOM   10695 C  CD  . GLN   D 1 256 ? 31.994  -34.002 18.905  1.00 112.30 ? 325  GLN   D CD  1 
ATOM   10696 O  OE1 . GLN   D 1 256 ? 31.514  -33.181 19.699  1.00 112.31 ? 325  GLN   D OE1 1 
ATOM   10697 N  NE2 . GLN   D 1 256 ? 31.279  -34.559 17.930  1.00 116.86 ? 325  GLN   D NE2 1 
ATOM   10698 N  N   . CYS   D 1 257 ? 35.795  -30.438 19.153  1.00 98.83  ? 326  CYS   D N   1 
ATOM   10699 C  CA  . CYS   D 1 257 ? 36.237  -29.179 19.739  1.00 94.38  ? 326  CYS   D CA  1 
ATOM   10700 C  C   . CYS   D 1 257 ? 36.714  -28.185 18.691  1.00 103.58 ? 326  CYS   D C   1 
ATOM   10701 O  O   . CYS   D 1 257 ? 37.093  -27.059 19.039  1.00 107.19 ? 326  CYS   D O   1 
ATOM   10702 C  CB  . CYS   D 1 257 ? 37.347  -29.430 20.762  1.00 91.42  ? 326  CYS   D CB  1 
ATOM   10703 S  SG  . CYS   D 1 257 ? 38.845  -30.111 20.028  1.00 90.33  ? 326  CYS   D SG  1 
ATOM   10704 N  N   . GLN   D 1 258 ? 36.736  -28.590 17.420  1.00 106.07 ? 327  GLN   D N   1 
ATOM   10705 C  CA  . GLN   D 1 258 ? 37.062  -27.662 16.299  1.00 106.35 ? 327  GLN   D CA  1 
ATOM   10706 C  C   . GLN   D 1 258 ? 38.326  -26.819 16.534  1.00 108.84 ? 327  GLN   D C   1 
ATOM   10707 O  O   . GLN   D 1 258 ? 38.469  -25.809 15.824  1.00 114.67 ? 327  GLN   D O   1 
ATOM   10708 C  CB  . GLN   D 1 258 ? 35.974  -26.601 16.163  1.00 105.74 ? 327  GLN   D CB  1 
ATOM   10709 C  CG  . GLN   D 1 258 ? 36.137  -25.688 14.955  1.00 110.64 ? 327  GLN   D CG  1 
ATOM   10710 C  CD  . GLN   D 1 258 ? 34.957  -24.764 14.759  1.00 113.00 ? 327  GLN   D CD  1 
ATOM   10711 O  OE1 . GLN   D 1 258 ? 33.947  -24.845 15.466  1.00 115.28 ? 327  GLN   D OE1 1 
ATOM   10712 N  NE2 . GLN   D 1 258 ? 35.080  -23.862 13.796  1.00 118.04 ? 327  GLN   D NE2 1 
ATOM   10713 N  N   . GLU   D 1 259 ? 39.201  -27.179 17.469  1.00 103.50 ? 328  GLU   D N   1 
ATOM   10714 C  CA  . GLU   D 1 259 ? 40.369  -26.290 17.708  1.00 107.38 ? 328  GLU   D CA  1 
ATOM   10715 C  C   . GLU   D 1 259 ? 41.511  -27.231 18.091  1.00 108.25 ? 328  GLU   D C   1 
ATOM   10716 O  O   . GLU   D 1 259 ? 42.024  -27.112 19.222  1.00 107.18 ? 328  GLU   D O   1 
ATOM   10717 C  CB  . GLU   D 1 259 ? 40.278  -25.164 18.733  1.00 123.37 ? 328  GLU   D CB  1 
ATOM   10718 C  CG  . GLU   D 1 259 ? 41.545  -24.315 18.788  1.00 129.42 ? 328  GLU   D CG  1 
ATOM   10719 C  CD  . GLU   D 1 259 ? 41.887  -23.512 17.540  1.00 131.57 ? 328  GLU   D CD  1 
ATOM   10720 O  OE1 . GLU   D 1 259 ? 41.015  -23.389 16.653  1.00 127.90 ? 328  GLU   D OE1 1 
ATOM   10721 O  OE2 . GLU   D 1 259 ? 43.031  -23.020 17.444  1.00 130.66 ? 328  GLU   D OE2 1 
ATOM   10722 N  N   . THR   D 1 260 ? 41.890  -28.119 17.176  1.00 114.67 ? 329  THR   D N   1 
ATOM   10723 C  CA  . THR   D 1 260 ? 42.971  -29.082 17.443  1.00 115.92 ? 329  THR   D CA  1 
ATOM   10724 C  C   . THR   D 1 260 ? 43.467  -29.581 16.111  1.00 111.53 ? 329  THR   D C   1 
ATOM   10725 O  O   . THR   D 1 260 ? 42.875  -30.539 15.588  1.00 111.71 ? 329  THR   D O   1 
ATOM   10726 C  CB  . THR   D 1 260 ? 42.427  -30.228 18.292  1.00 115.39 ? 329  THR   D CB  1 
ATOM   10727 O  OG1 . THR   D 1 260 ? 41.951  -29.694 19.523  1.00 114.95 ? 329  THR   D OG1 1 
ATOM   10728 C  CG2 . THR   D 1 260 ? 43.484  -31.262 18.626  1.00 111.27 ? 329  THR   D CG2 1 
ATOM   10729 N  N   . GLU   D 1 261 ? 44.500  -28.949 15.558  1.00 104.78 ? 330  GLU   D N   1 
ATOM   10730 C  CA  . GLU   D 1 261 ? 45.079  -29.466 14.294  1.00 101.73 ? 330  GLU   D CA  1 
ATOM   10731 C  C   . GLU   D 1 261 ? 45.542  -30.905 14.530  1.00 99.05  ? 330  GLU   D C   1 
ATOM   10732 O  O   . GLU   D 1 261 ? 46.509  -31.103 15.289  1.00 98.32  ? 330  GLU   D O   1 
ATOM   10733 C  CB  . GLU   D 1 261 ? 46.263  -28.651 13.780  1.00 103.22 ? 330  GLU   D CB  1 
ATOM   10734 C  CG  . GLU   D 1 261 ? 46.593  -28.955 12.322  1.00 106.38 ? 330  GLU   D CG  1 
ATOM   10735 C  CD  . GLU   D 1 261 ? 47.947  -28.436 11.879  1.00 110.13 ? 330  GLU   D CD  1 
ATOM   10736 O  OE1 . GLU   D 1 261 ? 47.988  -27.353 11.262  1.00 109.47 ? 330  GLU   D OE1 1 
ATOM   10737 O  OE2 . GLU   D 1 261 ? 48.959  -29.112 12.155  1.00 117.04 ? 330  GLU   D OE2 1 
ATOM   10738 N  N   . ILE   D 1 262 ? 44.869  -31.860 13.895  1.00 94.29  ? 331  ILE   D N   1 
ATOM   10739 C  CA  . ILE   D 1 262 ? 45.275  -33.282 14.037  1.00 89.33  ? 331  ILE   D CA  1 
ATOM   10740 C  C   . ILE   D 1 262 ? 46.300  -33.612 12.951  1.00 87.57  ? 331  ILE   D C   1 
ATOM   10741 O  O   . ILE   D 1 262 ? 47.290  -34.286 13.289  1.00 90.00  ? 331  ILE   D O   1 
ATOM   10742 C  CB  . ILE   D 1 262 ? 44.055  -34.214 13.949  1.00 91.06  ? 331  ILE   D CB  1 
ATOM   10743 C  CG1 . ILE   D 1 262 ? 42.880  -33.688 14.762  1.00 87.98  ? 331  ILE   D CG1 1 
ATOM   10744 C  CG2 . ILE   D 1 262 ? 44.428  -35.639 14.355  1.00 91.36  ? 331  ILE   D CG2 1 
ATOM   10745 C  CD1 . ILE   D 1 262 ? 42.908  -34.094 16.222  1.00 93.25  ? 331  ILE   D CD1 1 
ATOM   10746 N  N   . THR   D 1 263 ? 46.122  -33.096 11.730  1.00 89.60  ? 332  THR   D N   1 
ATOM   10747 C  CA  . THR   D 1 263 ? 47.013  -33.551 10.666  1.00 91.54  ? 332  THR   D CA  1 
ATOM   10748 C  C   . THR   D 1 263 ? 46.807  -32.651 9.449   1.00 92.82  ? 332  THR   D C   1 
ATOM   10749 O  O   . THR   D 1 263 ? 45.952  -31.758 9.455   1.00 91.90  ? 332  THR   D O   1 
ATOM   10750 C  CB  . THR   D 1 263 ? 46.763  -35.036 10.365  1.00 82.45  ? 332  THR   D CB  1 
ATOM   10751 O  OG1 . THR   D 1 263 ? 47.888  -35.599 9.689   1.00 79.83  ? 332  THR   D OG1 1 
ATOM   10752 C  CG2 . THR   D 1 263 ? 45.530  -35.188 9.515   1.00 78.55  ? 332  THR   D CG2 1 
ATOM   10753 N  N   . THR   D 1 264 ? 47.606  -32.890 8.402   1.00 95.41  ? 333  THR   D N   1 
ATOM   10754 C  CA  . THR   D 1 264 ? 47.628  -32.050 7.205   1.00 90.36  ? 333  THR   D CA  1 
ATOM   10755 C  C   . THR   D 1 264 ? 47.724  -32.919 5.961   1.00 92.72  ? 333  THR   D C   1 
ATOM   10756 O  O   . THR   D 1 264 ? 48.101  -34.089 6.013   1.00 93.86  ? 333  THR   D O   1 
ATOM   10757 C  CB  . THR   D 1 264 ? 48.810  -31.084 7.174   1.00 89.78  ? 333  THR   D CB  1 
ATOM   10758 O  OG1 . THR   D 1 264 ? 49.998  -31.831 6.900   1.00 97.12  ? 333  THR   D OG1 1 
ATOM   10759 C  CG2 . THR   D 1 264 ? 48.960  -30.348 8.490   1.00 93.95  ? 333  THR   D CG2 1 
ATOM   10760 N  N   . LYS   D 1 265 ? 47.426  -32.307 4.823   1.00 94.10  ? 334  LYS   D N   1 
ATOM   10761 C  CA  . LYS   D 1 265 ? 47.289  -33.077 3.600   1.00 94.72  ? 334  LYS   D CA  1 
ATOM   10762 C  C   . LYS   D 1 265 ? 48.603  -33.747 3.236   1.00 98.08  ? 334  LYS   D C   1 
ATOM   10763 O  O   . LYS   D 1 265 ? 48.645  -34.952 2.946   1.00 100.23 ? 334  LYS   D O   1 
ATOM   10764 C  CB  . LYS   D 1 265 ? 46.793  -32.160 2.479   1.00 99.68  ? 334  LYS   D CB  1 
ATOM   10765 C  CG  . LYS   D 1 265 ? 47.458  -32.364 1.120   1.00 105.81 ? 334  LYS   D CG  1 
ATOM   10766 C  CD  . LYS   D 1 265 ? 46.760  -31.549 0.036   1.00 101.79 ? 334  LYS   D CD  1 
ATOM   10767 C  CE  . LYS   D 1 265 ? 47.476  -31.645 -1.307  1.00 102.73 ? 334  LYS   D CE  1 
ATOM   10768 N  NZ  . LYS   D 1 265 ? 46.657  -31.046 -2.399  1.00 91.90  ? 334  LYS   D NZ  1 
ATOM   10769 N  N   . ASN   D 1 266 ? 49.697  -32.987 3.271   1.00 108.31 ? 335  ASN   D N   1 
ATOM   10770 C  CA  . ASN   D 1 266 ? 50.951  -33.515 2.758   1.00 112.83 ? 335  ASN   D CA  1 
ATOM   10771 C  C   . ASN   D 1 266 ? 51.480  -34.643 3.627   1.00 112.13 ? 335  ASN   D C   1 
ATOM   10772 O  O   . ASN   D 1 266 ? 52.511  -35.247 3.320   1.00 112.21 ? 335  ASN   D O   1 
ATOM   10773 C  CB  . ASN   D 1 266 ? 51.962  -32.380 2.640   1.00 112.10 ? 335  ASN   D CB  1 
ATOM   10774 C  CG  . ASN   D 1 266 ? 52.245  -31.735 3.956   1.00 114.51 ? 335  ASN   D CG  1 
ATOM   10775 O  OD1 . ASN   D 1 266 ? 51.814  -32.233 4.996   1.00 114.79 ? 335  ASN   D OD1 1 
ATOM   10776 N  ND2 . ASN   D 1 266 ? 52.979  -30.623 3.934   1.00 120.15 ? 335  ASN   D ND2 1 
ATOM   10777 N  N   . GLU   D 1 267 ? 50.707  -34.998 4.650   1.00 103.52 ? 336  GLU   D N   1 
ATOM   10778 C  CA  . GLU   D 1 267 ? 51.105  -36.127 5.524   1.00 96.51  ? 336  GLU   D CA  1 
ATOM   10779 C  C   . GLU   D 1 267 ? 50.294  -37.373 5.146   1.00 94.26  ? 336  GLU   D C   1 
ATOM   10780 O  O   . GLU   D 1 267 ? 50.582  -38.451 5.696   1.00 94.94  ? 336  GLU   D O   1 
ATOM   10781 C  CB  . GLU   D 1 267 ? 50.870  -35.733 6.979   1.00 95.88  ? 336  GLU   D CB  1 
ATOM   10782 C  CG  . GLU   D 1 267 ? 52.061  -36.027 7.882   1.00 97.53  ? 336  GLU   D CG  1 
ATOM   10783 C  CD  . GLU   D 1 267 ? 53.187  -35.024 7.738   1.00 98.50  ? 336  GLU   D CD  1 
ATOM   10784 O  OE1 . GLU   D 1 267 ? 52.906  -33.811 7.814   1.00 104.84 ? 336  GLU   D OE1 1 
ATOM   10785 O  OE2 . GLU   D 1 267 ? 54.342  -35.456 7.550   1.00 100.54 ? 336  GLU   D OE2 1 
ATOM   10786 N  N   . ILE   D 1 268 ? 49.324  -37.232 4.242   1.00 93.93  ? 337  ILE   D N   1 
ATOM   10787 C  CA  . ILE   D 1 268 ? 48.439  -38.382 3.890   1.00 93.04  ? 337  ILE   D CA  1 
ATOM   10788 C  C   . ILE   D 1 268 ? 49.244  -39.386 3.054   1.00 93.88  ? 337  ILE   D C   1 
ATOM   10789 O  O   . ILE   D 1 268 ? 50.005  -38.941 2.175   1.00 95.61  ? 337  ILE   D O   1 
ATOM   10790 C  CB  . ILE   D 1 268 ? 47.183  -37.890 3.152   1.00 88.57  ? 337  ILE   D CB  1 
ATOM   10791 C  CG1 . ILE   D 1 268 ? 46.292  -37.060 4.067   1.00 86.89  ? 337  ILE   D CG1 1 
ATOM   10792 C  CG2 . ILE   D 1 268 ? 46.416  -39.053 2.525   1.00 89.48  ? 337  ILE   D CG2 1 
ATOM   10793 C  CD1 . ILE   D 1 268 ? 45.138  -36.386 3.350   1.00 82.24  ? 337  ILE   D CD1 1 
ATOM   10794 N  N   . PHE   D 1 269 ? 49.079  -40.682 3.329   1.00 94.91  ? 338  PHE   D N   1 
ATOM   10795 C  CA  . PHE   D 1 269 ? 49.815  -41.735 2.580   1.00 91.63  ? 338  PHE   D CA  1 
ATOM   10796 C  C   . PHE   D 1 269 ? 48.961  -42.986 2.493   1.00 90.84  ? 338  PHE   D C   1 
ATOM   10797 O  O   . PHE   D 1 269 ? 47.950  -43.085 3.210   1.00 90.24  ? 338  PHE   D O   1 
ATOM   10798 C  CB  . PHE   D 1 269 ? 51.147  -42.015 3.278   1.00 94.72  ? 338  PHE   D CB  1 
ATOM   10799 C  CG  . PHE   D 1 269 ? 51.126  -43.059 4.385   1.00 94.97  ? 338  PHE   D CG  1 
ATOM   10800 C  CD1 . PHE   D 1 269 ? 50.525  -42.791 5.609   1.00 95.76  ? 338  PHE   D CD1 1 
ATOM   10801 C  CD2 . PHE   D 1 269 ? 51.727  -44.299 4.208   1.00 96.50  ? 338  PHE   D CD2 1 
ATOM   10802 C  CE1 . PHE   D 1 269 ? 50.515  -43.742 6.615   1.00 93.06  ? 338  PHE   D CE1 1 
ATOM   10803 C  CE2 . PHE   D 1 269 ? 51.713  -45.245 5.218   1.00 98.60  ? 338  PHE   D CE2 1 
ATOM   10804 C  CZ  . PHE   D 1 269 ? 51.106  -44.965 6.417   1.00 95.54  ? 338  PHE   D CZ  1 
ATOM   10805 N  N   . SER   D 1 270 ? 49.358  -43.921 1.630   1.00 97.71  ? 339  SER   D N   1 
ATOM   10806 C  CA  . SER   D 1 270 ? 48.612  -45.195 1.485   1.00 100.43 ? 339  SER   D CA  1 
ATOM   10807 C  C   . SER   D 1 270 ? 49.516  -46.366 1.873   1.00 104.49 ? 339  SER   D C   1 
ATOM   10808 O  O   . SER   D 1 270 ? 50.457  -46.659 1.114   1.00 103.60 ? 339  SER   D O   1 
ATOM   10809 C  CB  . SER   D 1 270 ? 48.103  -45.369 0.092   1.00 102.47 ? 339  SER   D CB  1 
ATOM   10810 O  OG  . SER   D 1 270 ? 47.066  -44.441 -0.181  1.00 102.65 ? 339  SER   D OG  1 
ATOM   10811 N  N   . LEU   D 1 271 ? 49.242  -46.995 3.013   1.00 109.67 ? 340  LEU   D N   1 
ATOM   10812 C  CA  . LEU   D 1 271 ? 50.020  -48.188 3.423   1.00 117.55 ? 340  LEU   D CA  1 
ATOM   10813 C  C   . LEU   D 1 271 ? 49.491  -49.373 2.621   1.00 126.02 ? 340  LEU   D C   1 
ATOM   10814 O  O   . LEU   D 1 271 ? 50.259  -49.960 1.833   1.00 122.53 ? 340  LEU   D O   1 
ATOM   10815 C  CB  . LEU   D 1 271 ? 49.864  -48.435 4.920   1.00 110.54 ? 340  LEU   D CB  1 
ATOM   10816 C  CG  . LEU   D 1 271 ? 50.846  -49.437 5.532   1.00 105.73 ? 340  LEU   D CG  1 
ATOM   10817 C  CD1 . LEU   D 1 271 ? 51.665  -48.783 6.625   1.00 100.86 ? 340  LEU   D CD1 1 
ATOM   10818 C  CD2 . LEU   D 1 271 ? 50.124  -50.660 6.062   1.00 110.80 ? 340  LEU   D CD2 1 
ATOM   10819 N  N   . SER   D 1 272 ? 48.212  -49.691 2.812   1.00 161.76 ? 341  SER   D N   1 
ATOM   10820 C  CA  . SER   D 1 272 ? 47.629  -50.801 2.089   1.00 164.21 ? 341  SER   D CA  1 
ATOM   10821 C  C   . SER   D 1 272 ? 47.469  -50.443 0.613   1.00 163.96 ? 341  SER   D C   1 
ATOM   10822 O  O   . SER   D 1 272 ? 47.573  -49.281 0.206   1.00 162.55 ? 341  SER   D O   1 
ATOM   10823 C  CB  . SER   D 1 272 ? 46.280  -51.177 2.700   1.00 165.32 ? 341  SER   D CB  1 
ATOM   10824 O  OG  . SER   D 1 272 ? 45.630  -52.163 1.923   1.00 170.94 ? 341  SER   D OG  1 
ATOM   10825 N  N   . LEU   D 1 273 ? 47.231  -51.466 -0.197  1.00 138.92 ? 342  LEU   D N   1 
ATOM   10826 C  CA  . LEU   D 1 273 ? 46.900  -51.250 -1.594  1.00 130.01 ? 342  LEU   D CA  1 
ATOM   10827 C  C   . LEU   D 1 273 ? 45.446  -50.869 -1.785  1.00 130.30 ? 342  LEU   D C   1 
ATOM   10828 O  O   . LEU   D 1 273 ? 44.984  -50.788 -2.924  1.00 128.98 ? 342  LEU   D O   1 
ATOM   10829 C  CB  . LEU   D 1 273 ? 47.216  -52.498 -2.415  1.00 122.89 ? 342  LEU   D CB  1 
ATOM   10830 C  CG  . LEU   D 1 273 ? 48.565  -53.171 -2.161  1.00 120.07 ? 342  LEU   D CG  1 
ATOM   10831 C  CD1 . LEU   D 1 273 ? 49.000  -53.922 -3.389  1.00 102.04 ? 342  LEU   D CD1 1 
ATOM   10832 C  CD2 . LEU   D 1 273 ? 49.624  -52.167 -1.756  1.00 121.74 ? 342  LEU   D CD2 1 
ATOM   10833 N  N   . CYS   D 1 274 ? 44.722  -50.632 -0.695  1.00 131.53 ? 343  CYS   D N   1 
ATOM   10834 C  CA  . CYS   D 1 274 ? 43.325  -50.232 -0.746  1.00 127.78 ? 343  CYS   D CA  1 
ATOM   10835 C  C   . CYS   D 1 274 ? 43.120  -48.726 -0.773  1.00 122.37 ? 343  CYS   D C   1 
ATOM   10836 O  O   . CYS   D 1 274 ? 41.973  -48.286 -0.868  1.00 120.69 ? 343  CYS   D O   1 
ATOM   10837 C  CB  . CYS   D 1 274 ? 42.563  -50.784 0.463   1.00 134.15 ? 343  CYS   D CB  1 
ATOM   10838 S  SG  . CYS   D 1 274 ? 42.564  -52.570 0.629   1.00 147.49 ? 343  CYS   D SG  1 
ATOM   10839 N  N   . GLY   D 1 275 ? 44.174  -47.923 -0.654  1.00 119.92 ? 344  GLY   D N   1 
ATOM   10840 C  CA  . GLY   D 1 275 ? 44.016  -46.488 -0.675  1.00 109.57 ? 344  GLY   D CA  1 
ATOM   10841 C  C   . GLY   D 1 275 ? 44.452  -45.818 0.609   1.00 101.97 ? 344  GLY   D C   1 
ATOM   10842 O  O   . GLY   D 1 275 ? 45.017  -46.446 1.514   1.00 107.28 ? 344  GLY   D O   1 
ATOM   10843 N  N   . PRO   D 1 276 ? 44.205  -44.513 0.706   1.00 98.39  ? 345  PRO   D N   1 
ATOM   10844 C  CA  . PRO   D 1 276 ? 44.598  -43.765 1.908   1.00 95.83  ? 345  PRO   D CA  1 
ATOM   10845 C  C   . PRO   D 1 276 ? 43.505  -43.724 2.968   1.00 90.91  ? 345  PRO   D C   1 
ATOM   10846 O  O   . PRO   D 1 276 ? 43.778  -43.476 4.144   1.00 88.67  ? 345  PRO   D O   1 
ATOM   10847 C  CB  . PRO   D 1 276 ? 44.879  -42.369 1.347   1.00 94.95  ? 345  PRO   D CB  1 
ATOM   10848 C  CG  . PRO   D 1 276 ? 43.835  -42.230 0.276   1.00 93.62  ? 345  PRO   D CG  1 
ATOM   10849 C  CD  . PRO   D 1 276 ? 43.656  -43.618 -0.326  1.00 99.80  ? 345  PRO   D CD  1 
ATOM   10850 N  N   . MET   D 1 277 ? 42.262  -43.976 2.558   1.00 93.76  ? 346  MET   D N   1 
ATOM   10851 C  CA  . MET   D 1 277 ? 41.123  -44.024 3.464   1.00 84.85  ? 346  MET   D CA  1 
ATOM   10852 C  C   . MET   D 1 277 ? 40.238  -45.236 3.154   1.00 89.43  ? 346  MET   D C   1 
ATOM   10853 O  O   . MET   D 1 277 ? 39.054  -45.136 2.833   1.00 78.64  ? 346  MET   D O   1 
ATOM   10854 C  CB  . MET   D 1 277 ? 40.335  -42.758 3.357   1.00 80.33  ? 346  MET   D CB  1 
ATOM   10855 C  CG  . MET   D 1 277 ? 39.809  -42.316 4.637   1.00 83.58  ? 346  MET   D CG  1 
ATOM   10856 S  SD  . MET   D 1 277 ? 38.574  -41.086 4.212   1.00 89.45  ? 346  MET   D SD  1 
ATOM   10857 C  CE  . MET   D 1 277 ? 37.355  -42.055 3.337   1.00 85.95  ? 346  MET   D CE  1 
ATOM   10858 N  N   . ALA   D 1 278 ? 40.815  -46.415 3.263   1.00 92.33  ? 347  ALA   D N   1 
ATOM   10859 C  CA  . ALA   D 1 278 ? 39.947  -47.549 3.037   1.00 92.51  ? 347  ALA   D CA  1 
ATOM   10860 C  C   . ALA   D 1 278 ? 39.059  -47.772 4.257   1.00 83.97  ? 347  ALA   D C   1 
ATOM   10861 O  O   . ALA   D 1 278 ? 39.319  -47.264 5.349   1.00 85.83  ? 347  ALA   D O   1 
ATOM   10862 C  CB  . ALA   D 1 278 ? 40.773  -48.788 2.708   1.00 100.43 ? 347  ALA   D CB  1 
ATOM   10863 N  N   . ALA   D 1 279 ? 37.979  -48.516 4.058   1.00 81.23  ? 348  ALA   D N   1 
ATOM   10864 C  CA  . ALA   D 1 279 ? 37.081  -48.866 5.153   1.00 83.04  ? 348  ALA   D CA  1 
ATOM   10865 C  C   . ALA   D 1 279 ? 37.486  -50.209 5.766   1.00 89.30  ? 348  ALA   D C   1 
ATOM   10866 O  O   . ALA   D 1 279 ? 37.560  -51.227 5.068   1.00 96.59  ? 348  ALA   D O   1 
ATOM   10867 C  CB  . ALA   D 1 279 ? 35.633  -48.912 4.668   1.00 80.94  ? 348  ALA   D CB  1 
ATOM   10868 N  N   . TYR   D 1 280 ? 37.736  -50.218 7.065   1.00 83.99  ? 349  TYR   D N   1 
ATOM   10869 C  CA  . TYR   D 1 280 ? 38.045  -51.437 7.781   1.00 82.21  ? 349  TYR   D CA  1 
ATOM   10870 C  C   . TYR   D 1 280 ? 36.879  -51.764 8.694   1.00 88.36  ? 349  TYR   D C   1 
ATOM   10871 O  O   . TYR   D 1 280 ? 36.052  -50.904 9.005   1.00 85.87  ? 349  TYR   D O   1 
ATOM   10872 C  CB  . TYR   D 1 280 ? 39.357  -51.295 8.557   1.00 88.35  ? 349  TYR   D CB  1 
ATOM   10873 C  CG  . TYR   D 1 280 ? 40.471  -50.758 7.669   1.00 91.76  ? 349  TYR   D CG  1 
ATOM   10874 C  CD1 . TYR   D 1 280 ? 40.617  -49.396 7.457   1.00 92.81  ? 349  TYR   D CD1 1 
ATOM   10875 C  CD2 . TYR   D 1 280 ? 41.351  -51.609 7.016   1.00 92.34  ? 349  TYR   D CD2 1 
ATOM   10876 C  CE1 . TYR   D 1 280 ? 41.617  -48.895 6.627   1.00 95.13  ? 349  TYR   D CE1 1 
ATOM   10877 C  CE2 . TYR   D 1 280 ? 42.349  -51.116 6.189   1.00 93.05  ? 349  TYR   D CE2 1 
ATOM   10878 C  CZ  . TYR   D 1 280 ? 42.484  -49.769 6.000   1.00 96.19  ? 349  TYR   D CZ  1 
ATOM   10879 O  OH  . TYR   D 1 280 ? 43.485  -49.307 5.170   1.00 108.73 ? 349  TYR   D OH  1 
ATOM   10880 N  N   . VAL   D 1 281 ? 36.775  -53.031 9.083   1.00 93.79  ? 350  VAL   D N   1 
ATOM   10881 C  CA  . VAL   D 1 281 ? 35.679  -53.463 9.940   1.00 91.64  ? 350  VAL   D CA  1 
ATOM   10882 C  C   . VAL   D 1 281 ? 36.268  -54.010 11.231  1.00 93.85  ? 350  VAL   D C   1 
ATOM   10883 O  O   . VAL   D 1 281 ? 37.032  -54.983 11.208  1.00 95.17  ? 350  VAL   D O   1 
ATOM   10884 C  CB  . VAL   D 1 281 ? 34.764  -54.488 9.252   1.00 90.14  ? 350  VAL   D CB  1 
ATOM   10885 C  CG1 . VAL   D 1 281 ? 35.428  -55.864 9.182   1.00 100.38 ? 350  VAL   D CG1 1 
ATOM   10886 C  CG2 . VAL   D 1 281 ? 33.445  -54.570 9.999   1.00 87.96  ? 350  VAL   D CG2 1 
ATOM   10887 N  N   . ASN   D 1 282 ? 35.953  -53.343 12.356  1.00 96.55  ? 351  ASN   D N   1 
ATOM   10888 C  CA  . ASN   D 1 282 ? 36.381  -53.833 13.662  1.00 95.36  ? 351  ASN   D CA  1 
ATOM   10889 C  C   . ASN   D 1 282 ? 35.651  -55.144 13.928  1.00 97.06  ? 351  ASN   D C   1 
ATOM   10890 O  O   . ASN   D 1 282 ? 34.752  -55.515 13.157  1.00 94.13  ? 351  ASN   D O   1 
ATOM   10891 C  CB  . ASN   D 1 282 ? 36.117  -52.809 14.770  1.00 89.07  ? 351  ASN   D CB  1 
ATOM   10892 C  CG  . ASN   D 1 282 ? 34.693  -52.885 15.330  1.00 92.77  ? 351  ASN   D CG  1 
ATOM   10893 O  OD1 . ASN   D 1 282 ? 33.796  -53.479 14.734  1.00 94.73  ? 351  ASN   D OD1 1 
ATOM   10894 N  ND2 . ASN   D 1 282 ? 34.483  -52.251 16.484  1.00 93.17  ? 351  ASN   D ND2 1 
ATOM   10895 N  N   . PRO   D 1 283 ? 35.991  -55.855 15.018  1.00 98.54  ? 352  PRO   D N   1 
ATOM   10896 C  CA  . PRO   D 1 283 ? 35.364  -57.153 15.289  1.00 95.62  ? 352  PRO   D CA  1 
ATOM   10897 C  C   . PRO   D 1 283 ? 33.961  -57.043 15.865  1.00 92.55  ? 352  PRO   D C   1 
ATOM   10898 O  O   . PRO   D 1 283 ? 33.482  -57.980 16.504  1.00 94.53  ? 352  PRO   D O   1 
ATOM   10899 C  CB  . PRO   D 1 283 ? 36.319  -57.801 16.299  1.00 92.68  ? 352  PRO   D CB  1 
ATOM   10900 C  CG  . PRO   D 1 283 ? 37.354  -56.757 16.637  1.00 95.63  ? 352  PRO   D CG  1 
ATOM   10901 C  CD  . PRO   D 1 283 ? 36.881  -55.451 16.113  1.00 99.50  ? 352  PRO   D CD  1 
ATOM   10902 N  N   . HIS   D 1 284 ? 33.289  -55.919 15.662  1.00 90.75  ? 353  HIS   D N   1 
ATOM   10903 C  CA  . HIS   D 1 284 ? 31.904  -55.797 16.090  1.00 92.23  ? 353  HIS   D CA  1 
ATOM   10904 C  C   . HIS   D 1 284 ? 31.028  -55.233 14.989  1.00 93.25  ? 353  HIS   D C   1 
ATOM   10905 O  O   . HIS   D 1 284 ? 29.956  -54.683 15.284  1.00 95.40  ? 353  HIS   D O   1 
ATOM   10906 C  CB  . HIS   D 1 284 ? 31.783  -54.919 17.330  1.00 97.04  ? 353  HIS   D CB  1 
ATOM   10907 C  CG  . HIS   D 1 284 ? 32.175  -55.609 18.595  1.00 102.33 ? 353  HIS   D CG  1 
ATOM   10908 N  ND1 . HIS   D 1 284 ? 31.249  -56.123 19.481  1.00 104.96 ? 353  HIS   D ND1 1 
ATOM   10909 C  CD2 . HIS   D 1 284 ? 33.392  -55.859 19.130  1.00 101.40 ? 353  HIS   D CD2 1 
ATOM   10910 C  CE1 . HIS   D 1 284 ? 31.882  -56.659 20.508  1.00 104.82 ? 353  HIS   D CE1 1 
ATOM   10911 N  NE2 . HIS   D 1 284 ? 33.182  -56.508 20.319  1.00 102.48 ? 353  HIS   D NE2 1 
ATOM   10912 N  N   . GLY   D 1 285 ? 31.486  -55.326 13.739  1.00 97.63  ? 354  GLY   D N   1 
ATOM   10913 C  CA  . GLY   D 1 285 ? 30.766  -54.802 12.602  1.00 99.25  ? 354  GLY   D CA  1 
ATOM   10914 C  C   . GLY   D 1 285 ? 30.865  -53.305 12.406  1.00 96.95  ? 354  GLY   D C   1 
ATOM   10915 O  O   . GLY   D 1 285 ? 30.609  -52.822 11.298  1.00 97.17  ? 354  GLY   D O   1 
ATOM   10916 N  N   . TYR   D 1 286 ? 31.202  -52.550 13.449  1.00 93.87  ? 355  TYR   D N   1 
ATOM   10917 C  CA  . TYR   D 1 286 ? 31.492  -51.144 13.274  1.00 84.70  ? 355  TYR   D CA  1 
ATOM   10918 C  C   . TYR   D 1 286 ? 32.505  -50.962 12.143  1.00 86.23  ? 355  TYR   D C   1 
ATOM   10919 O  O   . TYR   D 1 286 ? 33.493  -51.692 12.052  1.00 86.28  ? 355  TYR   D O   1 
ATOM   10920 C  CB  . TYR   D 1 286 ? 32.015  -50.585 14.593  1.00 87.21  ? 355  TYR   D CB  1 
ATOM   10921 C  CG  . TYR   D 1 286 ? 30.973  -50.532 15.710  1.00 91.31  ? 355  TYR   D CG  1 
ATOM   10922 C  CD1 . TYR   D 1 286 ? 29.971  -49.566 15.708  1.00 89.36  ? 355  TYR   D CD1 1 
ATOM   10923 C  CD2 . TYR   D 1 286 ? 31.015  -51.419 16.787  1.00 93.20  ? 355  TYR   D CD2 1 
ATOM   10924 C  CE1 . TYR   D 1 286 ? 29.041  -49.501 16.710  1.00 82.92  ? 355  TYR   D CE1 1 
ATOM   10925 C  CE2 . TYR   D 1 286 ? 30.080  -51.351 17.810  1.00 88.47  ? 355  TYR   D CE2 1 
ATOM   10926 C  CZ  . TYR   D 1 286 ? 29.096  -50.389 17.750  1.00 86.66  ? 355  TYR   D CZ  1 
ATOM   10927 O  OH  . TYR   D 1 286 ? 28.141  -50.283 18.722  1.00 99.17  ? 355  TYR   D OH  1 
ATOM   10928 N  N   . VAL   D 1 287 ? 32.239  -50.014 11.249  1.00 84.84  ? 356  VAL   D N   1 
ATOM   10929 C  CA  . VAL   D 1 287 ? 33.129  -49.738 10.122  1.00 87.21  ? 356  VAL   D CA  1 
ATOM   10930 C  C   . VAL   D 1 287 ? 33.792  -48.383 10.311  1.00 87.66  ? 356  VAL   D C   1 
ATOM   10931 O  O   . VAL   D 1 287 ? 33.122  -47.399 10.649  1.00 88.85  ? 356  VAL   D O   1 
ATOM   10932 C  CB  . VAL   D 1 287 ? 32.379  -49.770 8.784   1.00 81.77  ? 356  VAL   D CB  1 
ATOM   10933 C  CG1 . VAL   D 1 287 ? 33.376  -49.901 7.624   1.00 78.18  ? 356  VAL   D CG1 1 
ATOM   10934 C  CG2 . VAL   D 1 287 ? 31.358  -50.859 8.810   1.00 86.98  ? 356  VAL   D CG2 1 
ATOM   10935 N  N   . HIS   D 1 288 ? 35.095  -48.325 10.047  1.00 83.40  ? 357  HIS   D N   1 
ATOM   10936 C  CA  . HIS   D 1 288 ? 35.853  -47.086 10.099  1.00 82.07  ? 357  HIS   D CA  1 
ATOM   10937 C  C   . HIS   D 1 288 ? 36.546  -46.872 8.767   1.00 84.77  ? 357  HIS   D C   1 
ATOM   10938 O  O   . HIS   D 1 288 ? 37.486  -47.599 8.433   1.00 80.65  ? 357  HIS   D O   1 
ATOM   10939 C  CB  . HIS   D 1 288 ? 36.893  -47.092 11.215  1.00 83.14  ? 357  HIS   D CB  1 
ATOM   10940 C  CG  . HIS   D 1 288 ? 36.319  -47.288 12.583  1.00 90.37  ? 357  HIS   D CG  1 
ATOM   10941 N  ND1 . HIS   D 1 288 ? 35.982  -46.234 13.406  1.00 86.27  ? 357  HIS   D ND1 1 
ATOM   10942 C  CD2 . HIS   D 1 288 ? 36.063  -48.417 13.291  1.00 84.84  ? 357  HIS   D CD2 1 
ATOM   10943 C  CE1 . HIS   D 1 288 ? 35.518  -46.705 14.550  1.00 89.41  ? 357  HIS   D CE1 1 
ATOM   10944 N  NE2 . HIS   D 1 288 ? 35.561  -48.026 14.508  1.00 81.95  ? 357  HIS   D NE2 1 
ATOM   10945 N  N   . GLU   D 1 289 ? 36.109  -45.852 8.023   1.00 90.19  ? 358  GLU   D N   1 
ATOM   10946 C  CA  . GLU   D 1 289 ? 36.983  -45.277 7.005   1.00 85.87  ? 358  GLU   D CA  1 
ATOM   10947 C  C   . GLU   D 1 289 ? 38.175  -44.652 7.722   1.00 84.50  ? 358  GLU   D C   1 
ATOM   10948 O  O   . GLU   D 1 289 ? 38.010  -43.658 8.439   1.00 82.44  ? 358  GLU   D O   1 
ATOM   10949 C  CB  . GLU   D 1 289 ? 36.257  -44.229 6.151   1.00 81.23  ? 358  GLU   D CB  1 
ATOM   10950 C  CG  . GLU   D 1 289 ? 34.961  -44.668 5.442   1.00 82.29  ? 358  GLU   D CG  1 
ATOM   10951 C  CD  . GLU   D 1 289 ? 33.725  -43.939 5.980   1.00 84.96  ? 358  GLU   D CD  1 
ATOM   10952 O  OE1 . GLU   D 1 289 ? 33.477  -44.041 7.214   1.00 84.59  ? 358  GLU   D OE1 1 
ATOM   10953 O  OE2 . GLU   D 1 289 ? 33.002  -43.280 5.177   1.00 81.10  ? 358  GLU   D OE2 1 
ATOM   10954 N  N   . THR   D 1 290 ? 39.373  -45.229 7.557   1.00 83.50  ? 359  THR   D N   1 
ATOM   10955 C  CA  . THR   D 1 290 ? 40.555  -44.811 8.310   1.00 82.69  ? 359  THR   D CA  1 
ATOM   10956 C  C   . THR   D 1 290 ? 41.588  -44.187 7.383   1.00 81.84  ? 359  THR   D C   1 
ATOM   10957 O  O   . THR   D 1 290 ? 42.250  -44.896 6.619   1.00 86.43  ? 359  THR   D O   1 
ATOM   10958 C  CB  . THR   D 1 290 ? 41.154  -45.996 9.067   1.00 83.21  ? 359  THR   D CB  1 
ATOM   10959 O  OG1 . THR   D 1 290 ? 40.124  -46.613 9.850   1.00 84.73  ? 359  THR   D OG1 1 
ATOM   10960 C  CG2 . THR   D 1 290 ? 42.293  -45.527 9.977   1.00 80.05  ? 359  THR   D CG2 1 
ATOM   10961 N  N   . LEU   D 1 291 ? 41.738  -42.868 7.468   1.00 79.41  ? 360  LEU   D N   1 
ATOM   10962 C  CA  . LEU   D 1 291 ? 42.832  -42.202 6.779   1.00 83.99  ? 360  LEU   D CA  1 
ATOM   10963 C  C   . LEU   D 1 291 ? 44.144  -42.604 7.433   1.00 81.38  ? 360  LEU   D C   1 
ATOM   10964 O  O   . LEU   D 1 291 ? 44.247  -42.637 8.656   1.00 84.28  ? 360  LEU   D O   1 
ATOM   10965 C  CB  . LEU   D 1 291 ? 42.656  -40.682 6.825   1.00 80.17  ? 360  LEU   D CB  1 
ATOM   10966 C  CG  . LEU   D 1 291 ? 43.692  -39.816 6.102   1.00 83.13  ? 360  LEU   D CG  1 
ATOM   10967 C  CD1 . LEU   D 1 291 ? 43.717  -40.153 4.628   1.00 79.08  ? 360  LEU   D CD1 1 
ATOM   10968 C  CD2 . LEU   D 1 291 ? 43.404  -38.313 6.293   1.00 85.04  ? 360  LEU   D CD2 1 
ATOM   10969 N  N   . THR   D 1 292 ? 45.144  -42.920 6.631   1.00 81.27  ? 361  THR   D N   1 
ATOM   10970 C  CA  . THR   D 1 292 ? 46.481  -43.175 7.136   1.00 85.88  ? 361  THR   D CA  1 
ATOM   10971 C  C   . THR   D 1 292 ? 47.335  -41.912 6.968   1.00 89.49  ? 361  THR   D C   1 
ATOM   10972 O  O   . THR   D 1 292 ? 47.431  -41.347 5.872   1.00 89.01  ? 361  THR   D O   1 
ATOM   10973 C  CB  . THR   D 1 292 ? 47.074  -44.400 6.428   1.00 88.36  ? 361  THR   D CB  1 
ATOM   10974 O  OG1 . THR   D 1 292 ? 46.807  -44.333 5.021   1.00 90.62  ? 361  THR   D OG1 1 
ATOM   10975 C  CG2 . THR   D 1 292 ? 46.429  -45.683 6.960   1.00 87.69  ? 361  THR   D CG2 1 
ATOM   10976 N  N   . VAL   D 1 293 ? 47.893  -41.419 8.065   1.00 88.16  ? 362  VAL   D N   1 
ATOM   10977 C  CA  . VAL   D 1 293 ? 48.784  -40.273 7.963   1.00 93.85  ? 362  VAL   D CA  1 
ATOM   10978 C  C   . VAL   D 1 293 ? 50.137  -40.685 8.517   1.00 92.94  ? 362  VAL   D C   1 
ATOM   10979 O  O   . VAL   D 1 293 ? 50.235  -41.590 9.348   1.00 93.32  ? 362  VAL   D O   1 
ATOM   10980 C  CB  . VAL   D 1 293 ? 48.246  -39.001 8.678   1.00 84.47  ? 362  VAL   D CB  1 
ATOM   10981 C  CG1 . VAL   D 1 293 ? 46.811  -38.749 8.297   1.00 83.20  ? 362  VAL   D CG1 1 
ATOM   10982 C  CG2 . VAL   D 1 293 ? 48.371  -39.138 10.166  1.00 86.73  ? 362  VAL   D CG2 1 
ATOM   10983 N  N   . TYR   D 1 294 ? 51.189  -40.016 8.043   1.00 94.37  ? 363  TYR   D N   1 
ATOM   10984 C  CA  . TYR   D 1 294 ? 52.522  -40.277 8.574   1.00 95.00  ? 363  TYR   D CA  1 
ATOM   10985 C  C   . TYR   D 1 294 ? 52.702  -39.673 9.976   1.00 90.90  ? 363  TYR   D C   1 
ATOM   10986 O  O   . TYR   D 1 294 ? 53.256  -40.326 10.870  1.00 86.73  ? 363  TYR   D O   1 
ATOM   10987 C  CB  . TYR   D 1 294 ? 53.580  -39.764 7.589   1.00 94.05  ? 363  TYR   D CB  1 
ATOM   10988 N  N   . LYS   D 1 295 ? 52.222  -38.442 10.194  1.00 91.65  ? 364  LYS   D N   1 
ATOM   10989 C  CA  . LYS   D 1 295 ? 52.368  -37.719 11.459  1.00 93.47  ? 364  LYS   D CA  1 
ATOM   10990 C  C   . LYS   D 1 295 ? 51.020  -37.148 11.913  1.00 91.34  ? 364  LYS   D C   1 
ATOM   10991 O  O   . LYS   D 1 295 ? 50.285  -36.574 11.105  1.00 94.54  ? 364  LYS   D O   1 
ATOM   10992 C  CB  . LYS   D 1 295 ? 53.432  -36.576 11.342  1.00 82.70  ? 364  LYS   D CB  1 
ATOM   10993 N  N   . ALA   D 1 296 ? 50.683  -37.332 13.200  1.00 92.41  ? 365  ALA   D N   1 
ATOM   10994 C  CA  . ALA   D 1 296 ? 49.503  -36.744 13.838  1.00 92.40  ? 365  ALA   D CA  1 
ATOM   10995 C  C   . ALA   D 1 296 ? 49.916  -36.071 15.142  1.00 97.11  ? 365  ALA   D C   1 
ATOM   10996 O  O   . ALA   D 1 296 ? 50.876  -36.500 15.795  1.00 96.67  ? 365  ALA   D O   1 
ATOM   10997 C  CB  . ALA   D 1 296 ? 48.407  -37.782 14.135  1.00 89.57  ? 365  ALA   D CB  1 
ATOM   10998 N  N   . CYS   D 1 297 ? 49.167  -35.031 15.530  1.00 94.40  ? 366  CYS   D N   1 
ATOM   10999 C  CA  . CYS   D 1 297 ? 49.527  -34.184 16.665  1.00 97.62  ? 366  CYS   D CA  1 
ATOM   11000 C  C   . CYS   D 1 297 ? 48.344  -34.009 17.617  1.00 97.84  ? 366  CYS   D C   1 
ATOM   11001 O  O   . CYS   D 1 297 ? 47.199  -34.342 17.293  1.00 92.90  ? 366  CYS   D O   1 
ATOM   11002 C  CB  . CYS   D 1 297 ? 50.042  -32.816 16.187  1.00 102.13 ? 366  CYS   D CB  1 
ATOM   11003 S  SG  . CYS   D 1 297 ? 51.801  -32.835 15.685  1.00 129.50 ? 366  CYS   D SG  1 
ATOM   11004 N  N   . ASN   D 1 298 ? 48.635  -33.488 18.817  1.00 99.83  ? 367  ASN   D N   1 
ATOM   11005 C  CA  . ASN   D 1 298 ? 47.607  -33.214 19.826  1.00 94.40  ? 367  ASN   D CA  1 
ATOM   11006 C  C   . ASN   D 1 298 ? 46.760  -34.440 20.125  1.00 90.20  ? 367  ASN   D C   1 
ATOM   11007 O  O   . ASN   D 1 298 ? 45.561  -34.326 20.360  1.00 90.32  ? 367  ASN   D O   1 
ATOM   11008 C  CB  . ASN   D 1 298 ? 46.690  -32.068 19.405  1.00 93.43  ? 367  ASN   D CB  1 
ATOM   11009 C  CG  . ASN   D 1 298 ? 47.452  -30.868 18.956  1.00 96.94  ? 367  ASN   D CG  1 
ATOM   11010 O  OD1 . ASN   D 1 298 ? 48.647  -30.755 19.233  1.00 101.41 ? 367  ASN   D OD1 1 
ATOM   11011 N  ND2 . ASN   D 1 298 ? 46.781  -29.958 18.261  1.00 103.40 ? 367  ASN   D ND2 1 
ATOM   11012 N  N   . LEU   D 1 299 ? 47.339  -35.629 20.088  1.00 92.01  ? 368  LEU   D N   1 
ATOM   11013 C  CA  . LEU   D 1 299 ? 46.587  -36.822 20.434  1.00 92.72  ? 368  LEU   D CA  1 
ATOM   11014 C  C   . LEU   D 1 299 ? 47.100  -37.386 21.748  1.00 92.86  ? 368  LEU   D C   1 
ATOM   11015 O  O   . LEU   D 1 299 ? 48.307  -37.429 21.999  1.00 98.95  ? 368  LEU   D O   1 
ATOM   11016 C  CB  . LEU   D 1 299 ? 46.659  -37.877 19.328  1.00 92.06  ? 368  LEU   D CB  1 
ATOM   11017 C  CG  . LEU   D 1 299 ? 46.021  -37.412 18.013  1.00 93.27  ? 368  LEU   D CG  1 
ATOM   11018 C  CD1 . LEU   D 1 299 ? 45.541  -38.593 17.247  1.00 84.56  ? 368  LEU   D CD1 1 
ATOM   11019 C  CD2 . LEU   D 1 299 ? 44.861  -36.420 18.222  1.00 87.71  ? 368  LEU   D CD2 1 
ATOM   11020 N  N   . ASN   D 1 300 ? 46.188  -37.790 22.601  1.00 89.60  ? 369  ASN   D N   1 
ATOM   11021 C  CA  . ASN   D 1 300 ? 46.570  -38.544 23.773  1.00 90.66  ? 369  ASN   D CA  1 
ATOM   11022 C  C   . ASN   D 1 300 ? 46.307  -39.998 23.470  1.00 92.20  ? 369  ASN   D C   1 
ATOM   11023 O  O   . ASN   D 1 300 ? 45.234  -40.342 22.966  1.00 95.14  ? 369  ASN   D O   1 
ATOM   11024 C  CB  . ASN   D 1 300 ? 45.793  -38.094 25.004  1.00 96.06  ? 369  ASN   D CB  1 
ATOM   11025 C  CG  . ASN   D 1 300 ? 46.398  -36.856 25.658  1.00 100.90 ? 369  ASN   D CG  1 
ATOM   11026 O  OD1 . ASN   D 1 300 ? 47.572  -36.539 25.458  1.00 103.42 ? 369  ASN   D OD1 1 
ATOM   11027 N  ND2 . ASN   D 1 300 ? 45.596  -36.161 26.459  1.00 98.24  ? 369  ASN   D ND2 1 
ATOM   11028 N  N   . LEU   D 1 301 ? 47.301  -40.838 23.719  1.00 95.29  ? 370  LEU   D N   1 
ATOM   11029 C  CA  . LEU   D 1 301 ? 47.136  -42.279 23.563  1.00 92.04  ? 370  LEU   D CA  1 
ATOM   11030 C  C   . LEU   D 1 301 ? 46.458  -42.853 24.806  1.00 91.24  ? 370  LEU   D C   1 
ATOM   11031 O  O   . LEU   D 1 301 ? 46.847  -42.537 25.928  1.00 97.62  ? 370  LEU   D O   1 
ATOM   11032 C  CB  . LEU   D 1 301 ? 48.483  -42.966 23.348  1.00 92.77  ? 370  LEU   D CB  1 
ATOM   11033 C  CG  . LEU   D 1 301 ? 49.552  -42.395 22.411  1.00 93.01  ? 370  LEU   D CG  1 
ATOM   11034 C  CD1 . LEU   D 1 301 ? 50.835  -43.193 22.606  1.00 88.50  ? 370  LEU   D CD1 1 
ATOM   11035 C  CD2 . LEU   D 1 301 ? 49.117  -42.406 20.951  1.00 92.25  ? 370  LEU   D CD2 1 
ATOM   11036 N  N   . ILE   D 1 302 ? 45.448  -43.699 24.604  1.00 93.31  ? 371  ILE   D N   1 
ATOM   11037 C  CA  . ILE   D 1 302 ? 44.760  -44.415 25.675  1.00 88.76  ? 371  ILE   D CA  1 
ATOM   11038 C  C   . ILE   D 1 302 ? 45.234  -45.869 25.649  1.00 97.71  ? 371  ILE   D C   1 
ATOM   11039 O  O   . ILE   D 1 302 ? 45.456  -46.437 24.569  1.00 98.50  ? 371  ILE   D O   1 
ATOM   11040 C  CB  . ILE   D 1 302 ? 43.227  -44.329 25.516  1.00 84.64  ? 371  ILE   D CB  1 
ATOM   11041 C  CG1 . ILE   D 1 302 ? 42.695  -42.922 25.802  1.00 94.44  ? 371  ILE   D CG1 1 
ATOM   11042 C  CG2 . ILE   D 1 302 ? 42.535  -45.271 26.425  1.00 91.67  ? 371  ILE   D CG2 1 
ATOM   11043 C  CD1 . ILE   D 1 302 ? 43.503  -42.123 26.777  1.00 99.68  ? 371  ILE   D CD1 1 
ATOM   11044 N  N   . GLY   D 1 303 ? 45.386  -46.477 26.834  1.00 97.59  ? 372  GLY   D N   1 
ATOM   11045 C  CA  . GLY   D 1 303 ? 45.811  -47.865 26.937  1.00 97.62  ? 372  GLY   D CA  1 
ATOM   11046 C  C   . GLY   D 1 303 ? 47.257  -48.070 26.505  1.00 100.73 ? 372  GLY   D C   1 
ATOM   11047 O  O   . GLY   D 1 303 ? 48.056  -47.127 26.423  1.00 101.59 ? 372  GLY   D O   1 
ATOM   11048 N  N   . ARG   D 1 304 ? 47.596  -49.324 26.225  1.00 99.29  ? 373  ARG   D N   1 
ATOM   11049 C  CA  . ARG   D 1 304 ? 48.900  -49.683 25.691  1.00 98.01  ? 373  ARG   D CA  1 
ATOM   11050 C  C   . ARG   D 1 304 ? 48.692  -50.501 24.427  1.00 98.21  ? 373  ARG   D C   1 
ATOM   11051 O  O   . ARG   D 1 304 ? 47.597  -51.020 24.196  1.00 100.23 ? 373  ARG   D O   1 
ATOM   11052 C  CB  . ARG   D 1 304 ? 49.717  -50.455 26.731  1.00 102.00 ? 373  ARG   D CB  1 
ATOM   11053 N  N   . PRO   D 1 305 ? 49.733  -50.635 23.571  1.00 101.99 ? 374  PRO   D N   1 
ATOM   11054 C  CA  . PRO   D 1 305 ? 49.519  -51.190 22.213  1.00 101.58 ? 374  PRO   D CA  1 
ATOM   11055 C  C   . PRO   D 1 305 ? 48.913  -52.590 22.200  1.00 96.54  ? 374  PRO   D C   1 
ATOM   11056 O  O   . PRO   D 1 305 ? 48.899  -53.275 23.221  1.00 95.54  ? 374  PRO   D O   1 
ATOM   11057 C  CB  . PRO   D 1 305 ? 50.937  -51.197 21.606  1.00 98.82  ? 374  PRO   D CB  1 
ATOM   11058 C  CG  . PRO   D 1 305 ? 51.722  -50.234 22.415  1.00 96.12  ? 374  PRO   D CG  1 
ATOM   11059 C  CD  . PRO   D 1 305 ? 51.159  -50.337 23.814  1.00 100.16 ? 374  PRO   D CD  1 
ATOM   11060 N  N   . SER   D 1 306 ? 48.417  -53.020 21.039  1.00 95.72  ? 375  SER   D N   1 
ATOM   11061 C  CA  . SER   D 1 306 ? 47.820  -54.342 20.870  1.00 97.29  ? 375  SER   D CA  1 
ATOM   11062 C  C   . SER   D 1 306 ? 47.868  -54.762 19.400  1.00 98.83  ? 375  SER   D C   1 
ATOM   11063 O  O   . SER   D 1 306 ? 48.064  -53.937 18.499  1.00 98.74  ? 375  SER   D O   1 
ATOM   11064 C  CB  . SER   D 1 306 ? 46.380  -54.373 21.402  1.00 96.99  ? 375  SER   D CB  1 
ATOM   11065 O  OG  . SER   D 1 306 ? 45.654  -55.535 21.011  1.00 98.61  ? 375  SER   D OG  1 
ATOM   11066 N  N   . THR   D 1 307 ? 47.675  -56.074 19.167  1.00 103.28 ? 376  THR   D N   1 
ATOM   11067 C  CA  . THR   D 1 307 ? 47.595  -56.634 17.824  1.00 98.18  ? 376  THR   D CA  1 
ATOM   11068 C  C   . THR   D 1 307 ? 46.254  -57.304 17.508  1.00 99.10  ? 376  THR   D C   1 
ATOM   11069 O  O   . THR   D 1 307 ? 46.013  -57.626 16.340  1.00 97.25  ? 376  THR   D O   1 
ATOM   11070 C  CB  . THR   D 1 307 ? 48.740  -57.630 17.587  1.00 89.54  ? 376  THR   D CB  1 
ATOM   11071 O  OG1 . THR   D 1 307 ? 48.643  -58.680 18.542  1.00 95.12  ? 376  THR   D OG1 1 
ATOM   11072 C  CG2 . THR   D 1 307 ? 50.076  -56.949 17.741  1.00 90.09  ? 376  THR   D CG2 1 
ATOM   11073 N  N   . GLU   D 1 308 ? 45.355  -57.469 18.477  1.00 107.50 ? 377  GLU   D N   1 
ATOM   11074 C  CA  . GLU   D 1 308 ? 44.087  -58.139 18.209  1.00 108.98 ? 377  GLU   D CA  1 
ATOM   11075 C  C   . GLU   D 1 308 ? 43.318  -57.411 17.102  1.00 106.80 ? 377  GLU   D C   1 
ATOM   11076 O  O   . GLU   D 1 308 ? 42.934  -56.249 17.262  1.00 107.28 ? 377  GLU   D O   1 
ATOM   11077 C  CB  . GLU   D 1 308 ? 43.246  -58.219 19.490  1.00 108.44 ? 377  GLU   D CB  1 
ATOM   11078 N  N   . HIS   D 1 309 ? 43.107  -58.083 15.969  1.00 106.18 ? 378  HIS   D N   1 
ATOM   11079 C  CA  . HIS   D 1 309 ? 42.340  -57.572 14.835  1.00 110.81 ? 378  HIS   D CA  1 
ATOM   11080 C  C   . HIS   D 1 309 ? 43.016  -56.407 14.114  1.00 108.60 ? 378  HIS   D C   1 
ATOM   11081 O  O   . HIS   D 1 309 ? 42.356  -55.701 13.333  1.00 109.47 ? 378  HIS   D O   1 
ATOM   11082 C  CB  . HIS   D 1 309 ? 40.911  -57.162 15.246  1.00 110.07 ? 378  HIS   D CB  1 
ATOM   11083 C  CG  . HIS   D 1 309 ? 39.846  -57.527 14.238  1.00 114.49 ? 378  HIS   D CG  1 
ATOM   11084 N  ND1 . HIS   D 1 309 ? 39.717  -56.896 13.013  1.00 111.79 ? 378  HIS   D ND1 1 
ATOM   11085 C  CD2 . HIS   D 1 309 ? 38.856  -58.454 14.285  1.00 115.48 ? 378  HIS   D CD2 1 
ATOM   11086 C  CE1 . HIS   D 1 309 ? 38.701  -57.421 12.351  1.00 109.07 ? 378  HIS   D CE1 1 
ATOM   11087 N  NE2 . HIS   D 1 309 ? 38.168  -58.374 13.096  1.00 114.08 ? 378  HIS   D NE2 1 
ATOM   11088 N  N   . SER   D 1 310 ? 44.309  -56.198 14.319  1.00 95.88  ? 379  SER   D N   1 
ATOM   11089 C  CA  . SER   D 1 310 ? 45.028  -55.129 13.639  1.00 98.41  ? 379  SER   D CA  1 
ATOM   11090 C  C   . SER   D 1 310 ? 44.733  -55.115 12.148  1.00 100.91 ? 379  SER   D C   1 
ATOM   11091 O  O   . SER   D 1 310 ? 45.004  -56.091 11.435  1.00 102.16 ? 379  SER   D O   1 
ATOM   11092 C  CB  . SER   D 1 310 ? 46.533  -55.243 13.885  1.00 96.44  ? 379  SER   D CB  1 
ATOM   11093 O  OG  . SER   D 1 310 ? 47.263  -54.271 13.139  1.00 100.69 ? 379  SER   D OG  1 
ATOM   11094 N  N   . TRP   D 1 311 ? 44.180  -54.008 11.668  1.00 98.06  ? 380  TRP   D N   1 
ATOM   11095 C  CA  . TRP   D 1 311 ? 43.902  -53.917 10.245  1.00 97.62  ? 380  TRP   D CA  1 
ATOM   11096 C  C   . TRP   D 1 311 ? 45.162  -53.817 9.404   1.00 95.25  ? 380  TRP   D C   1 
ATOM   11097 O  O   . TRP   D 1 311 ? 45.088  -53.942 8.179   1.00 98.10  ? 380  TRP   D O   1 
ATOM   11098 C  CB  . TRP   D 1 311 ? 43.014  -52.725 9.978   1.00 95.82  ? 380  TRP   D CB  1 
ATOM   11099 C  CG  . TRP   D 1 311 ? 41.689  -52.855 10.617  1.00 93.48  ? 380  TRP   D CG  1 
ATOM   11100 C  CD1 . TRP   D 1 311 ? 40.930  -53.982 10.746  1.00 96.46  ? 380  TRP   D CD1 1 
ATOM   11101 C  CD2 . TRP   D 1 311 ? 40.961  -51.808 11.233  1.00 93.57  ? 380  TRP   D CD2 1 
ATOM   11102 N  NE1 . TRP   D 1 311 ? 39.756  -53.688 11.394  1.00 96.30  ? 380  TRP   D NE1 1 
ATOM   11103 C  CE2 . TRP   D 1 311 ? 39.756  -52.357 11.708  1.00 93.61  ? 380  TRP   D CE2 1 
ATOM   11104 C  CE3 . TRP   D 1 311 ? 41.213  -50.448 11.431  1.00 90.25  ? 380  TRP   D CE3 1 
ATOM   11105 C  CZ2 . TRP   D 1 311 ? 38.811  -51.598 12.366  1.00 91.56  ? 380  TRP   D CZ2 1 
ATOM   11106 C  CZ3 . TRP   D 1 311 ? 40.291  -49.707 12.075  1.00 86.81  ? 380  TRP   D CZ3 1 
ATOM   11107 C  CH2 . TRP   D 1 311 ? 39.095  -50.274 12.542  1.00 89.86  ? 380  TRP   D CH2 1 
ATOM   11108 N  N   . PHE   D 1 312 ? 46.317  -53.598 10.022  1.00 94.69  ? 381  PHE   D N   1 
ATOM   11109 C  CA  . PHE   D 1 312 ? 47.574  -53.427 9.305   1.00 98.96  ? 381  PHE   D CA  1 
ATOM   11110 C  C   . PHE   D 1 312 ? 48.564  -54.434 9.863   1.00 103.93 ? 381  PHE   D C   1 
ATOM   11111 O  O   . PHE   D 1 312 ? 49.337  -54.127 10.809  1.00 98.67  ? 381  PHE   D O   1 
ATOM   11112 C  CB  . PHE   D 1 312 ? 48.079  -52.010 9.459   1.00 99.16  ? 381  PHE   D CB  1 
ATOM   11113 C  CG  . PHE   D 1 312 ? 47.055  -50.966 9.111   1.00 100.14 ? 381  PHE   D CG  1 
ATOM   11114 C  CD1 . PHE   D 1 312 ? 45.966  -50.729 9.939   1.00 98.20  ? 381  PHE   D CD1 1 
ATOM   11115 C  CD2 . PHE   D 1 312 ? 47.195  -50.208 7.961   1.00 101.16 ? 381  PHE   D CD2 1 
ATOM   11116 C  CE1 . PHE   D 1 312 ? 45.040  -49.772 9.621   1.00 97.10  ? 381  PHE   D CE1 1 
ATOM   11117 C  CE2 . PHE   D 1 312 ? 46.275  -49.232 7.623   1.00 99.74  ? 381  PHE   D CE2 1 
ATOM   11118 C  CZ  . PHE   D 1 312 ? 45.190  -49.012 8.453   1.00 100.22 ? 381  PHE   D CZ  1 
ATOM   11119 N  N   . PRO   D 1 313 ? 48.569  -55.658 9.318   1.00 108.33 ? 382  PRO   D N   1 
ATOM   11120 C  CA  . PRO   D 1 313 ? 49.430  -56.717 9.881   1.00 105.38 ? 382  PRO   D CA  1 
ATOM   11121 C  C   . PRO   D 1 313 ? 50.895  -56.304 9.907   1.00 107.28 ? 382  PRO   D C   1 
ATOM   11122 O  O   . PRO   D 1 313 ? 51.429  -55.752 8.941   1.00 107.62 ? 382  PRO   D O   1 
ATOM   11123 C  CB  . PRO   D 1 313 ? 49.213  -57.910 8.945   1.00 104.83 ? 382  PRO   D CB  1 
ATOM   11124 C  CG  . PRO   D 1 313 ? 48.837  -57.221 7.640   1.00 109.96 ? 382  PRO   D CG  1 
ATOM   11125 C  CD  . PRO   D 1 313 ? 47.971  -56.082 8.052   1.00 107.16 ? 382  PRO   D CD  1 
ATOM   11126 N  N   . GLY   D 1 314 ? 51.536  -56.563 11.043  1.00 106.25 ? 383  GLY   D N   1 
ATOM   11127 C  CA  . GLY   D 1 314 ? 52.869  -56.060 11.336  1.00 108.64 ? 383  GLY   D CA  1 
ATOM   11128 C  C   . GLY   D 1 314 ? 52.886  -54.912 12.316  1.00 109.38 ? 383  GLY   D C   1 
ATOM   11129 O  O   . GLY   D 1 314 ? 53.947  -54.629 12.882  1.00 109.59 ? 383  GLY   D O   1 
ATOM   11130 N  N   . TYR   D 1 315 ? 51.739  -54.255 12.538  1.00 108.97 ? 384  TYR   D N   1 
ATOM   11131 C  CA  . TYR   D 1 315 ? 51.638  -53.071 13.378  1.00 102.33 ? 384  TYR   D CA  1 
ATOM   11132 C  C   . TYR   D 1 315 ? 50.735  -53.332 14.576  1.00 100.05 ? 384  TYR   D C   1 
ATOM   11133 O  O   . TYR   D 1 315 ? 49.789  -54.118 14.505  1.00 102.12 ? 384  TYR   D O   1 
ATOM   11134 C  CB  . TYR   D 1 315 ? 51.095  -51.879 12.572  1.00 100.94 ? 384  TYR   D CB  1 
ATOM   11135 C  CG  . TYR   D 1 315 ? 52.034  -51.414 11.482  1.00 100.72 ? 384  TYR   D CG  1 
ATOM   11136 C  CD1 . TYR   D 1 315 ? 52.061  -52.047 10.240  1.00 100.76 ? 384  TYR   D CD1 1 
ATOM   11137 C  CD2 . TYR   D 1 315 ? 52.907  -50.356 11.699  1.00 99.40  ? 384  TYR   D CD2 1 
ATOM   11138 C  CE1 . TYR   D 1 315 ? 52.929  -51.629 9.247   1.00 98.14  ? 384  TYR   D CE1 1 
ATOM   11139 C  CE2 . TYR   D 1 315 ? 53.779  -49.929 10.707  1.00 102.04 ? 384  TYR   D CE2 1 
ATOM   11140 C  CZ  . TYR   D 1 315 ? 53.784  -50.573 9.483   1.00 101.21 ? 384  TYR   D CZ  1 
ATOM   11141 O  OH  . TYR   D 1 315 ? 54.645  -50.152 8.496   1.00 106.35 ? 384  TYR   D OH  1 
ATOM   11142 N  N   . ALA   D 1 316 ? 51.037  -52.654 15.675  1.00 100.20 ? 385  ALA   D N   1 
ATOM   11143 C  CA  . ALA   D 1 316 ? 50.172  -52.593 16.839  1.00 96.47  ? 385  ALA   D CA  1 
ATOM   11144 C  C   . ALA   D 1 316 ? 49.381  -51.290 16.832  1.00 100.22 ? 385  ALA   D C   1 
ATOM   11145 O  O   . ALA   D 1 316 ? 49.826  -50.281 16.277  1.00 98.64  ? 385  ALA   D O   1 
ATOM   11146 C  CB  . ALA   D 1 316 ? 50.992  -52.686 18.121  1.00 95.97  ? 385  ALA   D CB  1 
ATOM   11147 N  N   . TRP   D 1 317 ? 48.202  -51.316 17.455  1.00 99.44  ? 386  TRP   D N   1 
ATOM   11148 C  CA  . TRP   D 1 317 ? 47.344  -50.141 17.573  1.00 97.00  ? 386  TRP   D CA  1 
ATOM   11149 C  C   . TRP   D 1 317 ? 47.184  -49.742 19.035  1.00 97.48  ? 386  TRP   D C   1 
ATOM   11150 O  O   . TRP   D 1 317 ? 47.139  -50.603 19.922  1.00 95.38  ? 386  TRP   D O   1 
ATOM   11151 C  CB  . TRP   D 1 317 ? 45.959  -50.381 16.956  1.00 91.50  ? 386  TRP   D CB  1 
ATOM   11152 C  CG  . TRP   D 1 317 ? 45.308  -51.572 17.494  1.00 90.35  ? 386  TRP   D CG  1 
ATOM   11153 C  CD1 . TRP   D 1 317 ? 45.409  -52.839 17.010  1.00 96.37  ? 386  TRP   D CD1 1 
ATOM   11154 C  CD2 . TRP   D 1 317 ? 44.468  -51.648 18.648  1.00 94.13  ? 386  TRP   D CD2 1 
ATOM   11155 N  NE1 . TRP   D 1 317 ? 44.676  -53.700 17.784  1.00 99.89  ? 386  TRP   D NE1 1 
ATOM   11156 C  CE2 . TRP   D 1 317 ? 44.089  -52.993 18.800  1.00 100.48 ? 386  TRP   D CE2 1 
ATOM   11157 C  CE3 . TRP   D 1 317 ? 43.995  -50.716 19.564  1.00 95.90  ? 386  TRP   D CE3 1 
ATOM   11158 C  CZ2 . TRP   D 1 317 ? 43.264  -53.426 19.836  1.00 97.12  ? 386  TRP   D CZ2 1 
ATOM   11159 C  CZ3 . TRP   D 1 317 ? 43.169  -51.154 20.587  1.00 97.42  ? 386  TRP   D CZ3 1 
ATOM   11160 C  CH2 . TRP   D 1 317 ? 42.810  -52.491 20.709  1.00 87.88  ? 386  TRP   D CH2 1 
ATOM   11161 N  N   . THR   D 1 318 ? 47.076  -48.428 19.265  1.00 94.61  ? 387  THR   D N   1 
ATOM   11162 C  CA  . THR   D 1 318 ? 46.830  -47.847 20.581  1.00 95.71  ? 387  THR   D CA  1 
ATOM   11163 C  C   . THR   D 1 318 ? 45.820  -46.724 20.372  1.00 92.87  ? 387  THR   D C   1 
ATOM   11164 O  O   . THR   D 1 318 ? 46.112  -45.780 19.629  1.00 97.04  ? 387  THR   D O   1 
ATOM   11165 C  CB  . THR   D 1 318 ? 48.128  -47.316 21.214  1.00 96.60  ? 387  THR   D CB  1 
ATOM   11166 O  OG1 . THR   D 1 318 ? 49.223  -48.223 20.965  1.00 98.91  ? 387  THR   D OG1 1 
ATOM   11167 C  CG2 . THR   D 1 318 ? 47.950  -47.171 22.690  1.00 95.39  ? 387  THR   D CG2 1 
ATOM   11168 N  N   . VAL   D 1 319 ? 44.626  -46.821 20.978  1.00 93.15  ? 388  VAL   D N   1 
ATOM   11169 C  CA  . VAL   D 1 319 ? 43.575  -45.846 20.676  1.00 89.87  ? 388  VAL   D CA  1 
ATOM   11170 C  C   . VAL   D 1 319 ? 44.075  -44.434 20.938  1.00 91.64  ? 388  VAL   D C   1 
ATOM   11171 O  O   . VAL   D 1 319 ? 44.774  -44.184 21.924  1.00 94.27  ? 388  VAL   D O   1 
ATOM   11172 C  CB  . VAL   D 1 319 ? 42.308  -46.104 21.510  1.00 88.81  ? 388  VAL   D CB  1 
ATOM   11173 C  CG1 . VAL   D 1 319 ? 41.376  -44.895 21.387  1.00 86.62  ? 388  VAL   D CG1 1 
ATOM   11174 C  CG2 . VAL   D 1 319 ? 41.598  -47.370 21.071  1.00 86.11  ? 388  VAL   D CG2 1 
ATOM   11175 N  N   . ALA   D 1 320 ? 43.695  -43.487 20.074  1.00 95.06  ? 389  ALA   D N   1 
ATOM   11176 C  CA  . ALA   D 1 320 ? 44.150  -42.103 20.214  1.00 91.15  ? 389  ALA   D CA  1 
ATOM   11177 C  C   . ALA   D 1 320 ? 42.971  -41.143 20.201  1.00 86.85  ? 389  ALA   D C   1 
ATOM   11178 O  O   . ALA   D 1 320 ? 42.097  -41.214 19.329  1.00 79.98  ? 389  ALA   D O   1 
ATOM   11179 C  CB  . ALA   D 1 320 ? 45.152  -41.721 19.115  1.00 85.28  ? 389  ALA   D CB  1 
ATOM   11180 N  N   . GLN   D 1 321 ? 42.958  -40.238 21.171  1.00 88.04  ? 390  GLN   D N   1 
ATOM   11181 C  CA  . GLN   D 1 321 ? 41.857  -39.311 21.336  1.00 86.64  ? 390  GLN   D CA  1 
ATOM   11182 C  C   . GLN   D 1 321 ? 42.385  -37.901 21.504  1.00 85.58  ? 390  GLN   D C   1 
ATOM   11183 O  O   . GLN   D 1 321 ? 43.533  -37.676 21.896  1.00 86.78  ? 390  GLN   D O   1 
ATOM   11184 C  CB  . GLN   D 1 321 ? 40.984  -39.672 22.536  1.00 87.43  ? 390  GLN   D CB  1 
ATOM   11185 C  CG  . GLN   D 1 321 ? 41.786  -39.881 23.807  1.00 89.46  ? 390  GLN   D CG  1 
ATOM   11186 C  CD  . GLN   D 1 321 ? 40.906  -39.973 25.049  1.00 99.61  ? 390  GLN   D CD  1 
ATOM   11187 O  OE1 . GLN   D 1 321 ? 41.169  -39.310 26.076  1.00 98.80  ? 390  GLN   D OE1 1 
ATOM   11188 N  NE2 . GLN   D 1 321 ? 39.846  -40.796 24.962  1.00 93.15  ? 390  GLN   D NE2 1 
ATOM   11189 N  N   . CYS   D 1 322 ? 41.493  -36.958 21.238  1.00 86.24  ? 391  CYS   D N   1 
ATOM   11190 C  CA  . CYS   D 1 322 ? 41.854  -35.549 21.227  1.00 88.57  ? 391  CYS   D CA  1 
ATOM   11191 C  C   . CYS   D 1 322 ? 42.308  -35.083 22.604  1.00 88.66  ? 391  CYS   D C   1 
ATOM   11192 O  O   . CYS   D 1 322 ? 41.624  -35.306 23.602  1.00 90.71  ? 391  CYS   D O   1 
ATOM   11193 C  CB  . CYS   D 1 322 ? 40.666  -34.726 20.761  1.00 86.11  ? 391  CYS   D CB  1 
ATOM   11194 S  SG  . CYS   D 1 322 ? 40.943  -33.022 20.927  1.00 81.92  ? 391  CYS   D SG  1 
ATOM   11195 N  N   . LYS   D 1 323 ? 43.452  -34.418 22.654  1.00 91.06  ? 392  LYS   D N   1 
ATOM   11196 C  CA  . LYS   D 1 323 ? 44.025  -33.951 23.918  1.00 87.23  ? 392  LYS   D CA  1 
ATOM   11197 C  C   . LYS   D 1 323 ? 43.114  -33.001 24.596  1.00 85.62  ? 392  LYS   D C   1 
ATOM   11198 O  O   . LYS   D 1 323 ? 43.199  -32.811 25.811  1.00 93.45  ? 392  LYS   D O   1 
ATOM   11199 C  CB  . LYS   D 1 323 ? 45.490  -33.553 23.730  1.00 89.66  ? 392  LYS   D CB  1 
ATOM   11200 C  CG  . LYS   D 1 323 ? 45.655  -32.171 23.079  1.00 90.21  ? 392  LYS   D CG  1 
ATOM   11201 C  CD  . LYS   D 1 323 ? 47.133  -31.732 23.064  1.00 91.52  ? 392  LYS   D CD  1 
ATOM   11202 C  CE  . LYS   D 1 323 ? 47.386  -30.366 22.421  1.00 83.92  ? 392  LYS   D CE  1 
ATOM   11203 N  NZ  . LYS   D 1 323 ? 48.858  -30.209 22.255  1.00 80.14  ? 392  LYS   D NZ  1 
ATOM   11204 N  N   . ILE   D 1 324 ? 42.204  -32.369 23.868  1.00 85.84  ? 393  ILE   D N   1 
ATOM   11205 C  CA  . ILE   D 1 324 ? 41.315  -31.385 24.466  1.00 86.62  ? 393  ILE   D CA  1 
ATOM   11206 C  C   . ILE   D 1 324 ? 39.950  -31.811 24.989  1.00 90.71  ? 393  ILE   D C   1 
ATOM   11207 O  O   . ILE   D 1 324 ? 39.612  -31.538 26.147  1.00 89.95  ? 393  ILE   D O   1 
ATOM   11208 C  CB  . ILE   D 1 324 ? 41.186  -30.351 23.343  1.00 89.44  ? 393  ILE   D CB  1 
ATOM   11209 C  CG1 . ILE   D 1 324 ? 42.577  -29.921 22.867  1.00 90.00  ? 393  ILE   D CG1 1 
ATOM   11210 C  CG2 . ILE   D 1 324 ? 40.356  -29.197 23.818  1.00 88.80  ? 393  ILE   D CG2 1 
ATOM   11211 C  CD1 . ILE   D 1 324 ? 43.201  -28.815 23.687  1.00 85.93  ? 393  ILE   D CD1 1 
ATOM   11212 N  N   . CYS   D 1 325 ? 39.179  -32.500 24.139  1.00 93.06  ? 394  CYS   D N   1 
ATOM   11213 C  CA  . CYS   D 1 325 ? 37.848  -33.011 24.449  1.00 89.62  ? 394  CYS   D CA  1 
ATOM   11214 C  C   . CYS   D 1 325 ? 37.812  -34.528 24.557  1.00 80.76  ? 394  CYS   D C   1 
ATOM   11215 O  O   . CYS   D 1 325 ? 36.727  -35.113 24.591  1.00 80.95  ? 394  CYS   D O   1 
ATOM   11216 C  CB  . CYS   D 1 325 ? 36.854  -32.547 23.383  1.00 88.75  ? 394  CYS   D CB  1 
ATOM   11217 S  SG  . CYS   D 1 325 ? 37.238  -33.156 21.721  1.00 91.53  ? 394  CYS   D SG  1 
ATOM   11218 N  N   . ALA   D 1 326 ? 38.972  -35.175 24.569  1.00 85.51  ? 395  ALA   D N   1 
ATOM   11219 C  CA  . ALA   D 1 326 ? 39.114  -36.642 24.670  1.00 90.58  ? 395  ALA   D CA  1 
ATOM   11220 C  C   . ALA   D 1 326 ? 38.190  -37.410 23.719  1.00 87.30  ? 395  ALA   D C   1 
ATOM   11221 O  O   . ALA   D 1 326 ? 37.961  -38.611 23.915  1.00 88.41  ? 395  ALA   D O   1 
ATOM   11222 C  CB  . ALA   D 1 326 ? 38.907  -37.134 26.108  1.00 89.91  ? 395  ALA   D CB  1 
ATOM   11223 N  N   . SER   D 1 327 ? 37.670  -36.736 22.691  1.00 88.95  ? 396  SER   D N   1 
ATOM   11224 C  CA  . SER   D 1 327 ? 36.893  -37.395 21.655  1.00 87.38  ? 396  SER   D CA  1 
ATOM   11225 C  C   . SER   D 1 327 ? 37.737  -38.425 20.914  1.00 85.38  ? 396  SER   D C   1 
ATOM   11226 O  O   . SER   D 1 327 ? 38.951  -38.276 20.753  1.00 83.54  ? 396  SER   D O   1 
ATOM   11227 C  CB  . SER   D 1 327 ? 36.345  -36.356 20.681  1.00 85.09  ? 396  SER   D CB  1 
ATOM   11228 O  OG  . SER   D 1 327 ? 35.218  -35.702 21.233  1.00 87.49  ? 396  SER   D OG  1 
ATOM   11229 N  N   . HIS   D 1 328 ? 37.089  -39.478 20.459  1.00 82.15  ? 397  HIS   D N   1 
ATOM   11230 C  CA  . HIS   D 1 328 ? 37.839  -40.490 19.746  1.00 80.22  ? 397  HIS   D CA  1 
ATOM   11231 C  C   . HIS   D 1 328 ? 38.248  -39.994 18.378  1.00 82.00  ? 397  HIS   D C   1 
ATOM   11232 O  O   . HIS   D 1 328 ? 37.404  -39.580 17.580  1.00 83.05  ? 397  HIS   D O   1 
ATOM   11233 C  CB  . HIS   D 1 328 ? 37.033  -41.750 19.592  1.00 85.76  ? 397  HIS   D CB  1 
ATOM   11234 C  CG  . HIS   D 1 328 ? 37.772  -42.815 18.863  1.00 86.28  ? 397  HIS   D CG  1 
ATOM   11235 N  ND1 . HIS   D 1 328 ? 37.284  -43.417 17.725  1.00 86.22  ? 397  HIS   D ND1 1 
ATOM   11236 C  CD2 . HIS   D 1 328 ? 38.992  -43.356 19.089  1.00 86.24  ? 397  HIS   D CD2 1 
ATOM   11237 C  CE1 . HIS   D 1 328 ? 38.164  -44.305 17.295  1.00 85.30  ? 397  HIS   D CE1 1 
ATOM   11238 N  NE2 . HIS   D 1 328 ? 39.207  -44.288 18.107  1.00 81.76  ? 397  HIS   D NE2 1 
ATOM   11239 N  N   . ILE   D 1 329 ? 39.542  -40.036 18.096  1.00 83.94  ? 398  ILE   D N   1 
ATOM   11240 C  CA  . ILE   D 1 329 ? 40.037  -39.658 16.782  1.00 81.95  ? 398  ILE   D CA  1 
ATOM   11241 C  C   . ILE   D 1 329 ? 40.450  -40.869 15.945  1.00 84.87  ? 398  ILE   D C   1 
ATOM   11242 O  O   . ILE   D 1 329 ? 40.378  -40.806 14.712  1.00 88.37  ? 398  ILE   D O   1 
ATOM   11243 C  CB  . ILE   D 1 329 ? 41.207  -38.646 16.900  1.00 77.89  ? 398  ILE   D CB  1 
ATOM   11244 C  CG1 . ILE   D 1 329 ? 40.683  -37.315 17.459  1.00 78.11  ? 398  ILE   D CG1 1 
ATOM   11245 C  CG2 . ILE   D 1 329 ? 41.870  -38.407 15.596  1.00 77.22  ? 398  ILE   D CG2 1 
ATOM   11246 C  CD1 . ILE   D 1 329 ? 39.460  -36.792 16.730  1.00 81.07  ? 398  ILE   D CD1 1 
ATOM   11247 N  N   . GLY   D 1 330 ? 40.838  -41.986 16.571  1.00 88.52  ? 399  GLY   D N   1 
ATOM   11248 C  CA  . GLY   D 1 330 ? 41.437  -43.110 15.855  1.00 86.02  ? 399  GLY   D CA  1 
ATOM   11249 C  C   . GLY   D 1 330 ? 42.436  -43.974 16.636  1.00 87.39  ? 399  GLY   D C   1 
ATOM   11250 O  O   . GLY   D 1 330 ? 42.175  -44.370 17.774  1.00 87.88  ? 399  GLY   D O   1 
ATOM   11251 N  N   . TRP   D 1 331 ? 43.563  -44.302 16.002  1.00 86.07  ? 400  TRP   D N   1 
ATOM   11252 C  CA  . TRP   D 1 331 ? 44.534  -45.231 16.587  1.00 88.90  ? 400  TRP   D CA  1 
ATOM   11253 C  C   . TRP   D 1 331 ? 45.945  -44.852 16.151  1.00 86.29  ? 400  TRP   D C   1 
ATOM   11254 O  O   . TRP   D 1 331 ? 46.166  -44.264 15.090  1.00 80.07  ? 400  TRP   D O   1 
ATOM   11255 C  CB  . TRP   D 1 331 ? 44.238  -46.703 16.196  1.00 88.58  ? 400  TRP   D CB  1 
ATOM   11256 C  CG  . TRP   D 1 331 ? 42.816  -47.099 16.427  1.00 81.87  ? 400  TRP   D CG  1 
ATOM   11257 C  CD1 . TRP   D 1 331 ? 42.302  -47.708 17.528  1.00 86.73  ? 400  TRP   D CD1 1 
ATOM   11258 C  CD2 . TRP   D 1 331 ? 41.715  -46.859 15.555  1.00 79.95  ? 400  TRP   D CD2 1 
ATOM   11259 N  NE1 . TRP   D 1 331 ? 40.951  -47.879 17.388  1.00 84.48  ? 400  TRP   D NE1 1 
ATOM   11260 C  CE2 . TRP   D 1 331 ? 40.566  -47.366 16.183  1.00 81.22  ? 400  TRP   D CE2 1 
ATOM   11261 C  CE3 . TRP   D 1 331 ? 41.589  -46.274 14.294  1.00 81.67  ? 400  TRP   D CE3 1 
ATOM   11262 C  CZ2 . TRP   D 1 331 ? 39.307  -47.313 15.599  1.00 84.79  ? 400  TRP   D CZ2 1 
ATOM   11263 C  CZ3 . TRP   D 1 331 ? 40.334  -46.221 13.713  1.00 85.42  ? 400  TRP   D CZ3 1 
ATOM   11264 C  CH2 . TRP   D 1 331 ? 39.208  -46.735 14.369  1.00 82.64  ? 400  TRP   D CH2 1 
ATOM   11265 N  N   . LYS   D 1 332 ? 46.907  -45.198 16.991  1.00 90.40  ? 401  LYS   D N   1 
ATOM   11266 C  CA  . LYS   D 1 332 ? 48.308  -45.060 16.638  1.00 91.14  ? 401  LYS   D CA  1 
ATOM   11267 C  C   . LYS   D 1 332 ? 48.844  -46.441 16.325  1.00 92.58  ? 401  LYS   D C   1 
ATOM   11268 O  O   . LYS   D 1 332 ? 48.648  -47.371 17.110  1.00 95.08  ? 401  LYS   D O   1 
ATOM   11269 C  CB  . LYS   D 1 332 ? 49.117  -44.416 17.759  1.00 92.48  ? 401  LYS   D CB  1 
ATOM   11270 C  CG  . LYS   D 1 332 ? 50.493  -43.973 17.309  1.00 93.24  ? 401  LYS   D CG  1 
ATOM   11271 C  CD  . LYS   D 1 332 ? 51.357  -43.562 18.494  1.00 90.95  ? 401  LYS   D CD  1 
ATOM   11272 C  CE  . LYS   D 1 332 ? 52.763  -43.220 18.020  1.00 92.30  ? 401  LYS   D CE  1 
ATOM   11273 N  NZ  . LYS   D 1 332 ? 53.791  -43.105 19.101  1.00 93.37  ? 401  LYS   D NZ  1 
ATOM   11274 N  N   . PHE   D 1 333 ? 49.507  -46.571 15.179  1.00 95.41  ? 402  PHE   D N   1 
ATOM   11275 C  CA  . PHE   D 1 333 ? 49.972  -47.855 14.677  1.00 96.32  ? 402  PHE   D CA  1 
ATOM   11276 C  C   . PHE   D 1 333 ? 51.495  -47.923 14.719  1.00 99.66  ? 402  PHE   D C   1 
ATOM   11277 O  O   . PHE   D 1 333 ? 52.175  -47.116 14.070  1.00 97.40  ? 402  PHE   D O   1 
ATOM   11278 C  CB  . PHE   D 1 333 ? 49.447  -48.087 13.268  1.00 94.96  ? 402  PHE   D CB  1 
ATOM   11279 C  CG  . PHE   D 1 333 ? 48.005  -48.492 13.238  1.00 96.16  ? 402  PHE   D CG  1 
ATOM   11280 C  CD1 . PHE   D 1 333 ? 47.657  -49.833 13.306  1.00 96.39  ? 402  PHE   D CD1 1 
ATOM   11281 C  CD2 . PHE   D 1 333 ? 46.996  -47.537 13.151  1.00 90.50  ? 402  PHE   D CD2 1 
ATOM   11282 C  CE1 . PHE   D 1 333 ? 46.332  -50.221 13.280  1.00 95.49  ? 402  PHE   D CE1 1 
ATOM   11283 C  CE2 . PHE   D 1 333 ? 45.670  -47.913 13.125  1.00 85.10  ? 402  PHE   D CE2 1 
ATOM   11284 C  CZ  . PHE   D 1 333 ? 45.338  -49.260 13.193  1.00 93.20  ? 402  PHE   D CZ  1 
ATOM   11285 N  N   . THR   D 1 334 ? 52.014  -48.921 15.448  1.00 98.42  ? 403  THR   D N   1 
ATOM   11286 C  CA  . THR   D 1 334 ? 53.430  -49.092 15.750  1.00 100.12 ? 403  THR   D CA  1 
ATOM   11287 C  C   . THR   D 1 334 ? 53.914  -50.457 15.255  1.00 102.20 ? 403  THR   D C   1 
ATOM   11288 O  O   . THR   D 1 334 ? 53.225  -51.468 15.430  1.00 103.95 ? 403  THR   D O   1 
ATOM   11289 C  CB  . THR   D 1 334 ? 53.652  -48.947 17.275  1.00 102.50 ? 403  THR   D CB  1 
ATOM   11290 O  OG1 . THR   D 1 334 ? 53.492  -50.222 17.918  1.00 106.59 ? 403  THR   D OG1 1 
ATOM   11291 C  CG2 . THR   D 1 334 ? 52.616  -47.990 17.863  1.00 90.52  ? 403  THR   D CG2 1 
ATOM   11292 N  N   . ALA   D 1 335 ? 55.114  -50.490 14.661  1.00 104.98 ? 404  ALA   D N   1 
ATOM   11293 C  CA  . ALA   D 1 335 ? 55.641  -51.708 14.043  1.00 105.54 ? 404  ALA   D CA  1 
ATOM   11294 C  C   . ALA   D 1 335 ? 55.982  -52.780 15.075  1.00 111.46 ? 404  ALA   D C   1 
ATOM   11295 O  O   . ALA   D 1 335 ? 56.671  -52.520 16.063  1.00 114.81 ? 404  ALA   D O   1 
ATOM   11296 C  CB  . ALA   D 1 335 ? 56.893  -51.389 13.229  1.00 106.62 ? 404  ALA   D CB  1 
ATOM   11297 N  N   . THR   D 1 336 ? 55.547  -54.012 14.817  1.00 112.77 ? 405  THR   D N   1 
ATOM   11298 C  CA  . THR   D 1 336 ? 55.977  -55.152 15.620  1.00 108.29 ? 405  THR   D CA  1 
ATOM   11299 C  C   . THR   D 1 336 ? 57.286  -55.771 15.125  1.00 115.42 ? 405  THR   D C   1 
ATOM   11300 O  O   . THR   D 1 336 ? 57.709  -56.785 15.688  1.00 125.52 ? 405  THR   D O   1 
ATOM   11301 C  CB  . THR   D 1 336 ? 54.894  -56.236 15.653  1.00 109.81 ? 405  THR   D CB  1 
ATOM   11302 O  OG1 . THR   D 1 336 ? 55.017  -57.109 14.523  1.00 108.36 ? 405  THR   D OG1 1 
ATOM   11303 C  CG2 . THR   D 1 336 ? 53.512  -55.612 15.627  1.00 110.26 ? 405  THR   D CG2 1 
ATOM   11304 N  N   . LYS   D 1 337 ? 57.914  -55.225 14.081  1.00 124.61 ? 406  LYS   D N   1 
ATOM   11305 C  CA  . LYS   D 1 337 ? 59.240  -55.673 13.645  1.00 122.93 ? 406  LYS   D CA  1 
ATOM   11306 C  C   . LYS   D 1 337 ? 60.166  -54.470 13.697  1.00 125.57 ? 406  LYS   D C   1 
ATOM   11307 O  O   . LYS   D 1 337 ? 59.823  -53.426 14.265  1.00 127.90 ? 406  LYS   D O   1 
ATOM   11308 C  CB  . LYS   D 1 337 ? 59.219  -56.287 12.254  1.00 118.88 ? 406  LYS   D CB  1 
ATOM   11309 N  N   . LYS   D 1 338 ? 61.322  -54.581 13.077  1.00 125.07 ? 407  LYS   D N   1 
ATOM   11310 C  CA  . LYS   D 1 338 ? 62.203  -53.433 12.948  1.00 119.82 ? 407  LYS   D CA  1 
ATOM   11311 C  C   . LYS   D 1 338 ? 62.457  -53.033 11.513  1.00 120.59 ? 407  LYS   D C   1 
ATOM   11312 O  O   . LYS   D 1 338 ? 62.787  -51.873 11.265  1.00 119.44 ? 407  LYS   D O   1 
ATOM   11313 C  CB  . LYS   D 1 338 ? 63.547  -53.707 13.635  1.00 111.00 ? 407  LYS   D CB  1 
ATOM   11314 N  N   . ASP   D 1 339 ? 62.331  -53.949 10.561  1.00 122.55 ? 408  ASP   D N   1 
ATOM   11315 C  CA  . ASP   D 1 339 ? 62.546  -53.559 9.179   1.00 119.15 ? 408  ASP   D CA  1 
ATOM   11316 C  C   . ASP   D 1 339 ? 61.398  -52.694 8.670   1.00 121.94 ? 408  ASP   D C   1 
ATOM   11317 O  O   . ASP   D 1 339 ? 61.614  -51.831 7.813   1.00 121.09 ? 408  ASP   D O   1 
ATOM   11318 C  CB  . ASP   D 1 339 ? 62.744  -54.812 8.315   1.00 114.36 ? 408  ASP   D CB  1 
ATOM   11319 N  N   . MET   D 1 340 ? 60.200  -52.855 9.235   1.00 127.33 ? 409  MET   D N   1 
ATOM   11320 C  CA  . MET   D 1 340 ? 58.988  -52.343 8.593   1.00 124.33 ? 409  MET   D CA  1 
ATOM   11321 C  C   . MET   D 1 340 ? 59.051  -50.835 8.374   1.00 123.39 ? 409  MET   D C   1 
ATOM   11322 O  O   . MET   D 1 340 ? 59.415  -50.078 9.279   1.00 124.41 ? 409  MET   D O   1 
ATOM   11323 C  CB  . MET   D 1 340 ? 57.744  -52.664 9.426   1.00 119.68 ? 409  MET   D CB  1 
ATOM   11324 C  CG  . MET   D 1 340 ? 57.847  -53.852 10.329  1.00 123.51 ? 409  MET   D CG  1 
ATOM   11325 S  SD  . MET   D 1 340 ? 56.137  -54.355 10.493  1.00 129.34 ? 409  MET   D SD  1 
ATOM   11326 C  CE  . MET   D 1 340 ? 55.902  -55.226 8.942   1.00 122.67 ? 409  MET   D CE  1 
ATOM   11327 N  N   . SER   D 1 341 ? 58.656  -50.400 7.176   1.00 113.75 ? 410  SER   D N   1 
ATOM   11328 C  CA  . SER   D 1 341 ? 58.545  -48.992 6.843   1.00 107.54 ? 410  SER   D CA  1 
ATOM   11329 C  C   . SER   D 1 341 ? 57.112  -48.675 6.427   1.00 101.55 ? 410  SER   D C   1 
ATOM   11330 O  O   . SER   D 1 341 ? 56.539  -49.404 5.606   1.00 98.50  ? 410  SER   D O   1 
ATOM   11331 C  CB  . SER   D 1 341 ? 59.530  -48.624 5.716   1.00 103.68 ? 410  SER   D CB  1 
ATOM   11332 O  OG  . SER   D 1 341 ? 59.710  -47.219 5.601   1.00 110.05 ? 410  SER   D OG  1 
ATOM   11333 N  N   . PRO   D 1 342 ? 56.485  -47.626 6.988   1.00 105.80 ? 411  PRO   D N   1 
ATOM   11334 C  CA  . PRO   D 1 342 ? 57.012  -46.738 8.028   1.00 105.65 ? 411  PRO   D CA  1 
ATOM   11335 C  C   . PRO   D 1 342 ? 57.008  -47.440 9.378   1.00 105.49 ? 411  PRO   D C   1 
ATOM   11336 O  O   . PRO   D 1 342 ? 56.283  -48.417 9.587   1.00 99.59  ? 411  PRO   D O   1 
ATOM   11337 C  CB  . PRO   D 1 342 ? 56.051  -45.544 7.975   1.00 99.10  ? 411  PRO   D CB  1 
ATOM   11338 C  CG  . PRO   D 1 342 ? 54.749  -46.149 7.547   1.00 97.79  ? 411  PRO   D CG  1 
ATOM   11339 C  CD  . PRO   D 1 342 ? 55.132  -47.222 6.564   1.00 102.61 ? 411  PRO   D CD  1 
ATOM   11340 N  N   . GLN   D 1 343 ? 57.824  -46.940 10.309  1.00 106.73 ? 412  GLN   D N   1 
ATOM   11341 C  CA  . GLN   D 1 343 ? 57.883  -47.525 11.649  1.00 111.36 ? 412  GLN   D CA  1 
ATOM   11342 C  C   . GLN   D 1 343 ? 56.665  -47.174 12.497  1.00 112.38 ? 412  GLN   D C   1 
ATOM   11343 O  O   . GLN   D 1 343 ? 56.302  -47.944 13.398  1.00 107.37 ? 412  GLN   D O   1 
ATOM   11344 C  CB  . GLN   D 1 343 ? 59.150  -47.070 12.369  1.00 111.06 ? 412  GLN   D CB  1 
ATOM   11345 C  CG  . GLN   D 1 343 ? 60.414  -47.712 11.851  1.00 113.96 ? 412  GLN   D CG  1 
ATOM   11346 C  CD  . GLN   D 1 343 ? 60.471  -49.179 12.191  1.00 113.95 ? 412  GLN   D CD  1 
ATOM   11347 O  OE1 . GLN   D 1 343 ? 61.023  -49.983 11.436  1.00 118.32 ? 412  GLN   D OE1 1 
ATOM   11348 N  NE2 . GLN   D 1 343 ? 59.889  -49.543 13.330  1.00 114.98 ? 412  GLN   D NE2 1 
ATOM   11349 N  N   . LYS   D 1 344 ? 56.041  -46.018 12.241  1.00 117.62 ? 413  LYS   D N   1 
ATOM   11350 C  CA  . LYS   D 1 344 ? 54.881  -45.554 12.993  1.00 113.34 ? 413  LYS   D CA  1 
ATOM   11351 C  C   . LYS   D 1 344 ? 53.986  -44.741 12.068  1.00 109.10 ? 413  LYS   D C   1 
ATOM   11352 O  O   . LYS   D 1 344 ? 54.477  -44.058 11.167  1.00 107.78 ? 413  LYS   D O   1 
ATOM   11353 C  CB  . LYS   D 1 344 ? 55.296  -44.708 14.213  1.00 117.95 ? 413  LYS   D CB  1 
ATOM   11354 N  N   . PHE   D 1 345 ? 52.675  -44.830 12.286  1.00 104.58 ? 414  PHE   D N   1 
ATOM   11355 C  CA  . PHE   D 1 345 ? 51.718  -43.995 11.565  1.00 98.57  ? 414  PHE   D CA  1 
ATOM   11356 C  C   . PHE   D 1 345 ? 50.404  -43.996 12.326  1.00 94.16  ? 414  PHE   D C   1 
ATOM   11357 O  O   . PHE   D 1 345 ? 50.160  -44.863 13.168  1.00 98.97  ? 414  PHE   D O   1 
ATOM   11358 C  CB  . PHE   D 1 345 ? 51.495  -44.483 10.127  1.00 96.18  ? 414  PHE   D CB  1 
ATOM   11359 C  CG  . PHE   D 1 345 ? 50.857  -45.834 10.046  1.00 96.86  ? 414  PHE   D CG  1 
ATOM   11360 C  CD1 . PHE   D 1 345 ? 51.631  -46.973 10.138  1.00 94.99  ? 414  PHE   D CD1 1 
ATOM   11361 C  CD2 . PHE   D 1 345 ? 49.480  -45.971 9.897   1.00 95.81  ? 414  PHE   D CD2 1 
ATOM   11362 C  CE1 . PHE   D 1 345 ? 51.052  -48.215 10.065  1.00 98.03  ? 414  PHE   D CE1 1 
ATOM   11363 C  CE2 . PHE   D 1 345 ? 48.889  -47.239 9.824   1.00 94.33  ? 414  PHE   D CE2 1 
ATOM   11364 C  CZ  . PHE   D 1 345 ? 49.676  -48.352 9.906   1.00 94.72  ? 414  PHE   D CZ  1 
ATOM   11365 N  N   . TRP   D 1 346 ? 49.549  -43.032 11.998  1.00 90.03  ? 415  TRP   D N   1 
ATOM   11366 C  CA  . TRP   D 1 346 ? 48.255  -42.867 12.647  1.00 89.41  ? 415  TRP   D CA  1 
ATOM   11367 C  C   . TRP   D 1 346 ? 47.107  -43.196 11.694  1.00 88.07  ? 415  TRP   D C   1 
ATOM   11368 O  O   . TRP   D 1 346 ? 47.072  -42.721 10.551  1.00 89.47  ? 415  TRP   D O   1 
ATOM   11369 C  CB  . TRP   D 1 346 ? 48.073  -41.434 13.141  1.00 91.50  ? 415  TRP   D CB  1 
ATOM   11370 C  CG  . TRP   D 1 346 ? 49.119  -40.961 14.056  1.00 91.02  ? 415  TRP   D CG  1 
ATOM   11371 C  CD1 . TRP   D 1 346 ? 50.293  -40.369 13.719  1.00 90.25  ? 415  TRP   D CD1 1 
ATOM   11372 C  CD2 . TRP   D 1 346 ? 49.089  -41.019 15.483  1.00 90.87  ? 415  TRP   D CD2 1 
ATOM   11373 N  NE1 . TRP   D 1 346 ? 51.001  -40.050 14.852  1.00 89.64  ? 415  TRP   D NE1 1 
ATOM   11374 C  CE2 . TRP   D 1 346 ? 50.278  -40.438 15.948  1.00 91.22  ? 415  TRP   D CE2 1 
ATOM   11375 C  CE3 . TRP   D 1 346 ? 48.166  -41.503 16.414  1.00 90.78  ? 415  TRP   D CE3 1 
ATOM   11376 C  CZ2 . TRP   D 1 346 ? 50.571  -40.330 17.298  1.00 96.10  ? 415  TRP   D CZ2 1 
ATOM   11377 C  CZ3 . TRP   D 1 346 ? 48.454  -41.385 17.753  1.00 90.91  ? 415  TRP   D CZ3 1 
ATOM   11378 C  CH2 . TRP   D 1 346 ? 49.648  -40.812 18.184  1.00 94.92  ? 415  TRP   D CH2 1 
ATOM   11379 N  N   . GLY   D 1 347 ? 46.154  -43.991 12.177  1.00 86.57  ? 416  GLY   D N   1 
ATOM   11380 C  CA  . GLY   D 1 347 ? 44.892  -44.152 11.485  1.00 81.79  ? 416  GLY   D CA  1 
ATOM   11381 C  C   . GLY   D 1 347 ? 43.831  -43.263 12.109  1.00 83.99  ? 416  GLY   D C   1 
ATOM   11382 O  O   . GLY   D 1 347 ? 43.496  -43.427 13.282  1.00 87.66  ? 416  GLY   D O   1 
ATOM   11383 N  N   . LEU   D 1 348 ? 43.292  -42.297 11.358  1.00 85.67  ? 417  LEU   D N   1 
ATOM   11384 C  CA  . LEU   D 1 348 ? 42.307  -41.351 11.878  1.00 80.50  ? 417  LEU   D CA  1 
ATOM   11385 C  C   . LEU   D 1 348 ? 40.968  -41.623 11.203  1.00 79.86  ? 417  LEU   D C   1 
ATOM   11386 O  O   . LEU   D 1 348 ? 40.876  -41.590 9.970   1.00 85.46  ? 417  LEU   D O   1 
ATOM   11387 C  CB  . LEU   D 1 348 ? 42.766  -39.910 11.628  1.00 83.05  ? 417  LEU   D CB  1 
ATOM   11388 C  CG  . LEU   D 1 348 ? 44.296  -39.731 11.601  1.00 83.32  ? 417  LEU   D CG  1 
ATOM   11389 C  CD1 . LEU   D 1 348 ? 44.774  -38.334 11.138  1.00 76.06  ? 417  LEU   D CD1 1 
ATOM   11390 C  CD2 . LEU   D 1 348 ? 44.893  -40.113 12.967  1.00 84.39  ? 417  LEU   D CD2 1 
ATOM   11391 N  N   . THR   D 1 349 ? 39.941  -41.917 11.998  1.00 78.03  ? 418  THR   D N   1 
ATOM   11392 C  CA  . THR   D 1 349 ? 38.645  -42.269 11.433  1.00 82.09  ? 418  THR   D CA  1 
ATOM   11393 C  C   . THR   D 1 349 ? 37.917  -41.016 10.945  1.00 81.97  ? 418  THR   D C   1 
ATOM   11394 O  O   . THR   D 1 349 ? 37.953  -39.963 11.591  1.00 87.16  ? 418  THR   D O   1 
ATOM   11395 C  CB  . THR   D 1 349 ? 37.789  -43.060 12.446  1.00 84.60  ? 418  THR   D CB  1 
ATOM   11396 O  OG1 . THR   D 1 349 ? 36.441  -43.244 11.953  1.00 81.33  ? 418  THR   D OG1 1 
ATOM   11397 C  CG2 . THR   D 1 349 ? 37.774  -42.395 13.845  1.00 83.26  ? 418  THR   D CG2 1 
ATOM   11398 N  N   . ARG   D 1 350 ? 37.295  -41.140 9.766   1.00 76.86  ? 419  ARG   D N   1 
ATOM   11399 C  CA  . ARG   D 1 350 ? 36.579  -40.050 9.106   1.00 75.27  ? 419  ARG   D CA  1 
ATOM   11400 C  C   . ARG   D 1 350 ? 35.637  -39.310 10.043  1.00 85.86  ? 419  ARG   D C   1 
ATOM   11401 O  O   . ARG   D 1 350 ? 35.705  -38.077 10.191  1.00 87.98  ? 419  ARG   D O   1 
ATOM   11402 C  CB  . ARG   D 1 350 ? 35.751  -40.620 7.962   1.00 78.17  ? 419  ARG   D CB  1 
ATOM   11403 C  CG  . ARG   D 1 350 ? 35.929  -39.954 6.660   1.00 77.69  ? 419  ARG   D CG  1 
ATOM   11404 C  CD  . ARG   D 1 350 ? 34.789  -40.312 5.793   1.00 78.25  ? 419  ARG   D CD  1 
ATOM   11405 N  NE  . ARG   D 1 350 ? 33.622  -39.501 6.112   1.00 80.48  ? 419  ARG   D NE  1 
ATOM   11406 C  CZ  . ARG   D 1 350 ? 32.454  -39.987 6.496   1.00 80.46  ? 419  ARG   D CZ  1 
ATOM   11407 N  NH1 . ARG   D 1 350 ? 32.291  -41.281 6.726   1.00 84.65  ? 419  ARG   D NH1 1 
ATOM   11408 N  NH2 . ARG   D 1 350 ? 31.416  -39.159 6.619   1.00 81.04  ? 419  ARG   D NH2 1 
ATOM   11409 N  N   . SER   D 1 351 ? 34.685  -40.048 10.618  1.00 80.31  ? 420  SER   D N   1 
ATOM   11410 C  CA  . SER   D 1 351 ? 33.630  -39.430 11.415  1.00 86.14  ? 420  SER   D CA  1 
ATOM   11411 C  C   . SER   D 1 351 ? 34.172  -38.480 12.488  1.00 83.89  ? 420  SER   D C   1 
ATOM   11412 O  O   . SER   D 1 351 ? 33.431  -37.605 12.967  1.00 79.44  ? 420  SER   D O   1 
ATOM   11413 C  CB  . SER   D 1 351 ? 32.747  -40.529 12.040  1.00 89.00  ? 420  SER   D CB  1 
ATOM   11414 O  OG  . SER   D 1 351 ? 33.491  -41.685 12.429  1.00 89.29  ? 420  SER   D OG  1 
ATOM   11415 N  N   . ALA   D 1 352 ? 35.450  -38.609 12.852  1.00 77.73  ? 421  ALA   D N   1 
ATOM   11416 C  CA  . ALA   D 1 352 ? 36.041  -37.823 13.925  1.00 82.83  ? 421  ALA   D CA  1 
ATOM   11417 C  C   . ALA   D 1 352 ? 36.728  -36.557 13.445  1.00 88.43  ? 421  ALA   D C   1 
ATOM   11418 O  O   . ALA   D 1 352 ? 37.207  -35.770 14.275  1.00 88.93  ? 421  ALA   D O   1 
ATOM   11419 C  CB  . ALA   D 1 352 ? 37.042  -38.674 14.703  1.00 85.32  ? 421  ALA   D CB  1 
ATOM   11420 N  N   . LEU   D 1 353 ? 36.795  -36.342 12.136  1.00 85.48  ? 422  LEU   D N   1 
ATOM   11421 C  CA  . LEU   D 1 353 ? 37.630  -35.300 11.570  1.00 81.46  ? 422  LEU   D CA  1 
ATOM   11422 C  C   . LEU   D 1 353 ? 36.783  -34.212 10.932  1.00 86.21  ? 422  LEU   D C   1 
ATOM   11423 O  O   . LEU   D 1 353 ? 35.592  -34.383 10.659  1.00 89.02  ? 422  LEU   D O   1 
ATOM   11424 C  CB  . LEU   D 1 353 ? 38.605  -35.874 10.530  1.00 84.83  ? 422  LEU   D CB  1 
ATOM   11425 C  CG  . LEU   D 1 353 ? 39.819  -36.712 10.955  1.00 83.71  ? 422  LEU   D CG  1 
ATOM   11426 C  CD1 . LEU   D 1 353 ? 40.367  -37.496 9.777   1.00 78.25  ? 422  LEU   D CD1 1 
ATOM   11427 C  CD2 . LEU   D 1 353 ? 40.903  -35.828 11.500  1.00 86.55  ? 422  LEU   D CD2 1 
ATOM   11428 N  N   . LEU   D 1 354 ? 37.442  -33.091 10.681  1.00 88.05  ? 423  LEU   D N   1 
ATOM   11429 C  CA  . LEU   D 1 354 ? 36.845  -31.883 10.137  1.00 87.27  ? 423  LEU   D CA  1 
ATOM   11430 C  C   . LEU   D 1 354 ? 37.828  -31.148 9.229   1.00 88.30  ? 423  LEU   D C   1 
ATOM   11431 O  O   . LEU   D 1 354 ? 38.802  -30.547 9.715   1.00 85.70  ? 423  LEU   D O   1 
ATOM   11432 C  CB  . LEU   D 1 354 ? 36.386  -30.969 11.273  1.00 88.69  ? 423  LEU   D CB  1 
ATOM   11433 C  CG  . LEU   D 1 354 ? 35.953  -29.573 10.825  1.00 82.28  ? 423  LEU   D CG  1 
ATOM   11434 C  CD1 . LEU   D 1 354 ? 35.111  -29.652 9.552   1.00 80.96  ? 423  LEU   D CD1 1 
ATOM   11435 C  CD2 . LEU   D 1 354 ? 35.214  -28.868 11.953  1.00 84.44  ? 423  LEU   D CD2 1 
ATOM   11436 N  N   . PRO   D 1 355 ? 37.595  -31.179 7.914   1.00 85.86  ? 424  PRO   D N   1 
ATOM   11437 C  CA  . PRO   D 1 355 ? 38.423  -30.403 6.982   1.00 85.73  ? 424  PRO   D CA  1 
ATOM   11438 C  C   . PRO   D 1 355 ? 38.353  -28.918 7.294   1.00 85.53  ? 424  PRO   D C   1 
ATOM   11439 O  O   . PRO   D 1 355 ? 37.273  -28.376 7.531   1.00 85.64  ? 424  PRO   D O   1 
ATOM   11440 C  CB  . PRO   D 1 355 ? 37.791  -30.693 5.613   1.00 86.19  ? 424  PRO   D CB  1 
ATOM   11441 C  CG  . PRO   D 1 355 ? 36.862  -31.851 5.840   1.00 87.76  ? 424  PRO   D CG  1 
ATOM   11442 C  CD  . PRO   D 1 355 ? 36.416  -31.754 7.254   1.00 85.16  ? 424  PRO   D CD  1 
ATOM   11443 N  N   . THR   D 1 356 ? 39.510  -28.250 7.271   1.00 84.34  ? 425  THR   D N   1 
ATOM   11444 C  CA  . THR   D 1 356 ? 39.546  -26.823 7.578   1.00 91.55  ? 425  THR   D CA  1 
ATOM   11445 C  C   . THR   D 1 356 ? 40.579  -26.115 6.705   1.00 92.38  ? 425  THR   D C   1 
ATOM   11446 O  O   . THR   D 1 356 ? 41.517  -26.728 6.176   1.00 83.70  ? 425  THR   D O   1 
ATOM   11447 C  CB  . THR   D 1 356 ? 39.849  -26.534 9.068   1.00 82.69  ? 425  THR   D CB  1 
ATOM   11448 O  OG1 . THR   D 1 356 ? 41.259  -26.600 9.303   1.00 83.81  ? 425  THR   D OG1 1 
ATOM   11449 C  CG2 . THR   D 1 356 ? 39.157  -27.529 9.974   1.00 89.95  ? 425  THR   D CG2 1 
ATOM   11450 N  N   . ILE   D 1 357 ? 40.407  -24.795 6.603   1.00 89.78  ? 426  ILE   D N   1 
ATOM   11451 C  CA  . ILE   D 1 357 ? 41.234  -23.928 5.770   1.00 83.99  ? 426  ILE   D CA  1 
ATOM   11452 C  C   . ILE   D 1 357 ? 42.104  -23.025 6.636   1.00 81.49  ? 426  ILE   D C   1 
ATOM   11453 O  O   . ILE   D 1 357 ? 41.591  -22.050 7.195   1.00 86.51  ? 426  ILE   D O   1 
ATOM   11454 C  CB  . ILE   D 1 357 ? 40.370  -23.085 4.815   1.00 86.01  ? 426  ILE   D CB  1 
ATOM   11455 C  CG1 . ILE   D 1 357 ? 39.847  -23.933 3.652   1.00 87.76  ? 426  ILE   D CG1 1 
ATOM   11456 C  CG2 . ILE   D 1 357 ? 41.150  -21.890 4.317   1.00 89.41  ? 426  ILE   D CG2 1 
ATOM   11457 C  CD1 . ILE   D 1 357 ? 38.857  -23.212 2.787   1.00 89.11  ? 426  ILE   D CD1 1 
ATOM   11458 N  N   . PRO   D 1 358 ? 43.416  -23.278 6.754   1.00 81.10  ? 427  PRO   D N   1 
ATOM   11459 C  CA  . PRO   D 1 358 ? 44.389  -22.484 7.528   1.00 82.42  ? 427  PRO   D CA  1 
ATOM   11460 C  C   . PRO   D 1 358 ? 44.310  -20.949 7.333   1.00 92.19  ? 427  PRO   D C   1 
ATOM   11461 O  O   . PRO   D 1 358 ? 44.885  -20.161 8.120   1.00 95.65  ? 427  PRO   D O   1 
ATOM   11462 C  CB  . PRO   D 1 358 ? 45.732  -23.008 7.024   1.00 83.20  ? 427  PRO   D CB  1 
ATOM   11463 C  CG  . PRO   D 1 358 ? 45.463  -24.424 6.623   1.00 80.27  ? 427  PRO   D CG  1 
ATOM   11464 C  CD  . PRO   D 1 358 ? 44.049  -24.437 6.096   1.00 82.90  ? 427  PRO   D CD  1 
ATOM   11465 N  N   . VAL   D 1 369 ? 38.730  -16.805 2.872   1.00 131.62 ? 438  VAL   D N   1 
ATOM   11466 C  CA  . VAL   D 1 369 ? 38.679  -17.906 1.909   1.00 129.93 ? 438  VAL   D CA  1 
ATOM   11467 C  C   . VAL   D 1 369 ? 37.431  -18.771 2.096   1.00 127.77 ? 438  VAL   D C   1 
ATOM   11468 O  O   . VAL   D 1 369 ? 36.981  -18.987 3.218   1.00 129.93 ? 438  VAL   D O   1 
ATOM   11469 C  CB  . VAL   D 1 369 ? 39.933  -18.777 1.999   1.00 128.87 ? 438  VAL   D CB  1 
ATOM   11470 C  CG1 . VAL   D 1 369 ? 39.732  -20.045 1.213   1.00 123.28 ? 438  VAL   D CG1 1 
ATOM   11471 C  CG2 . VAL   D 1 369 ? 41.113  -18.033 1.455   1.00 132.29 ? 438  VAL   D CG2 1 
ATOM   11472 N  N   . ILE   D 1 370 ? 36.894  -19.282 0.987   1.00 111.89 ? 439  ILE   D N   1 
ATOM   11473 C  CA  . ILE   D 1 370 ? 35.611  -19.976 0.982   1.00 106.50 ? 439  ILE   D CA  1 
ATOM   11474 C  C   . ILE   D 1 370 ? 35.608  -20.976 -0.172  1.00 101.92 ? 439  ILE   D C   1 
ATOM   11475 O  O   . ILE   D 1 370 ? 36.308  -20.793 -1.173  1.00 101.04 ? 439  ILE   D O   1 
ATOM   11476 C  CB  . ILE   D 1 370 ? 34.464  -18.947 0.885   1.00 98.16  ? 439  ILE   D CB  1 
ATOM   11477 C  CG1 . ILE   D 1 370 ? 33.107  -19.620 0.867   1.00 103.99 ? 439  ILE   D CG1 1 
ATOM   11478 C  CG2 . ILE   D 1 370 ? 34.636  -18.070 -0.348  1.00 102.75 ? 439  ILE   D CG2 1 
ATOM   11479 C  CD1 . ILE   D 1 370 ? 32.029  -18.613 0.563   1.00 104.93 ? 439  ILE   D CD1 1 
ATOM   11480 N  N   . LEU   D 1 371 ? 34.839  -22.061 -0.028  1.00 95.32  ? 440  LEU   D N   1 
ATOM   11481 C  CA  . LEU   D 1 371 ? 34.840  -23.076 -1.080  1.00 94.19  ? 440  LEU   D CA  1 
ATOM   11482 C  C   . LEU   D 1 371 ? 34.037  -22.584 -2.278  1.00 94.59  ? 440  LEU   D C   1 
ATOM   11483 O  O   . LEU   D 1 371 ? 32.863  -22.221 -2.153  1.00 95.04  ? 440  LEU   D O   1 
ATOM   11484 C  CB  . LEU   D 1 371 ? 34.307  -24.412 -0.570  1.00 89.62  ? 440  LEU   D CB  1 
ATOM   11485 C  CG  . LEU   D 1 371 ? 35.368  -25.221 0.168   1.00 85.60  ? 440  LEU   D CG  1 
ATOM   11486 C  CD1 . LEU   D 1 371 ? 34.787  -26.547 0.663   1.00 81.26  ? 440  LEU   D CD1 1 
ATOM   11487 C  CD2 . LEU   D 1 371 ? 36.620  -25.436 -0.708  1.00 83.33  ? 440  LEU   D CD2 1 
ATOM   11488 N  N   . CYS   D 1 372 ? 34.682  -22.573 -3.436  1.00 89.84  ? 441  CYS   D N   1 
ATOM   11489 C  CA  . CYS   D 1 372 ? 34.130  -22.051 -4.671  1.00 91.33  ? 441  CYS   D CA  1 
ATOM   11490 C  C   . CYS   D 1 372 ? 33.761  -23.211 -5.593  1.00 94.49  ? 441  CYS   D C   1 
ATOM   11491 O  O   . CYS   D 1 372 ? 34.516  -24.182 -5.723  1.00 93.85  ? 441  CYS   D O   1 
ATOM   11492 C  CB  . CYS   D 1 372 ? 35.179  -21.126 -5.298  1.00 92.81  ? 441  CYS   D CB  1 
ATOM   11493 S  SG  . CYS   D 1 372 ? 34.769  -20.270 -6.813  1.00 100.81 ? 441  CYS   D SG  1 
ATOM   11494 N  N   . LEU   D 1 373 ? 32.589  -23.144 -6.208  1.00 94.59  ? 442  LEU   D N   1 
ATOM   11495 C  CA  . LEU   D 1 373 ? 32.249  -24.208 -7.148  1.00 97.75  ? 442  LEU   D CA  1 
ATOM   11496 C  C   . LEU   D 1 373 ? 32.284  -23.700 -8.616  1.00 101.18 ? 442  LEU   D C   1 
ATOM   11497 O  O   . LEU   D 1 373 ? 31.422  -24.002 -9.465  1.00 98.10  ? 442  LEU   D O   1 
ATOM   11498 C  CB  . LEU   D 1 373 ? 30.886  -24.823 -6.803  1.00 92.60  ? 442  LEU   D CB  1 
ATOM   11499 C  CG  . LEU   D 1 373 ? 29.626  -24.031 -7.148  1.00 91.43  ? 442  LEU   D CG  1 
ATOM   11500 C  CD1 . LEU   D 1 373 ? 28.396  -24.827 -6.779  1.00 91.16  ? 442  LEU   D CD1 1 
ATOM   11501 C  CD2 . LEU   D 1 373 ? 29.621  -22.681 -6.464  1.00 95.36  ? 442  LEU   D CD2 1 
ATOM   11502 O  OXT . LEU   D 1 373 ? 33.211  -22.966 -9.009  1.00 97.93  ? 442  LEU   D OXT 1 
ATOM   11503 N  N   . SER   E 2 2   ? 9.932   -8.953  -16.121 1.00 95.21  ? 2    SER   E N   1 
ATOM   11504 C  CA  . SER   E 2 2   ? 9.606   -8.054  -17.220 1.00 100.41 ? 2    SER   E CA  1 
ATOM   11505 C  C   . SER   E 2 2   ? 9.350   -8.778  -18.550 1.00 102.12 ? 2    SER   E C   1 
ATOM   11506 O  O   . SER   E 2 2   ? 9.425   -10.012 -18.645 1.00 100.48 ? 2    SER   E O   1 
ATOM   11507 C  CB  . SER   E 2 2   ? 10.726  -7.010  -17.409 1.00 95.73  ? 2    SER   E CB  1 
ATOM   11508 O  OG  . SER   E 2 2   ? 11.827  -7.511  -18.163 1.00 83.79  ? 2    SER   E OG  1 
ATOM   11509 N  N   . TYR   E 2 3   ? 9.050   -7.979  -19.576 1.00 99.15  ? 3    TYR   E N   1 
ATOM   11510 C  CA  . TYR   E 2 3   ? 8.746   -8.462  -20.913 1.00 97.27  ? 3    TYR   E CA  1 
ATOM   11511 C  C   . TYR   E 2 3   ? 9.589   -7.719  -21.937 1.00 93.09  ? 3    TYR   E C   1 
ATOM   11512 O  O   . TYR   E 2 3   ? 9.828   -6.521  -21.805 1.00 95.33  ? 3    TYR   E O   1 
ATOM   11513 C  CB  . TYR   E 2 3   ? 7.283   -8.273  -21.231 1.00 98.99  ? 3    TYR   E CB  1 
ATOM   11514 C  CG  . TYR   E 2 3   ? 6.387   -8.532  -20.057 1.00 101.44 ? 3    TYR   E CG  1 
ATOM   11515 C  CD1 . TYR   E 2 3   ? 6.145   -9.825  -19.612 1.00 103.50 ? 3    TYR   E CD1 1 
ATOM   11516 C  CD2 . TYR   E 2 3   ? 5.765   -7.484  -19.405 1.00 104.49 ? 3    TYR   E CD2 1 
ATOM   11517 C  CE1 . TYR   E 2 3   ? 5.298   -10.061 -18.546 1.00 105.61 ? 3    TYR   E CE1 1 
ATOM   11518 C  CE2 . TYR   E 2 3   ? 4.923   -7.705  -18.348 1.00 108.25 ? 3    TYR   E CE2 1 
ATOM   11519 C  CZ  . TYR   E 2 3   ? 4.688   -8.991  -17.917 1.00 107.31 ? 3    TYR   E CZ  1 
ATOM   11520 O  OH  . TYR   E 2 3   ? 3.837   -9.190  -16.857 1.00 103.12 ? 3    TYR   E OH  1 
ATOM   11521 N  N   . ASN   E 2 4   ? 10.026  -8.419  -22.971 1.00 93.85  ? 4    ASN   E N   1 
ATOM   11522 C  CA  . ASN   E 2 4   ? 11.076  -7.859  -23.792 1.00 91.23  ? 4    ASN   E CA  1 
ATOM   11523 C  C   . ASN   E 2 4   ? 10.864  -8.226  -25.250 1.00 94.17  ? 4    ASN   E C   1 
ATOM   11524 O  O   . ASN   E 2 4   ? 10.119  -9.151  -25.589 1.00 94.94  ? 4    ASN   E O   1 
ATOM   11525 C  CB  . ASN   E 2 4   ? 12.436  -8.312  -23.272 1.00 89.65  ? 4    ASN   E CB  1 
ATOM   11526 C  CG  . ASN   E 2 4   ? 12.805  -7.615  -21.984 1.00 89.72  ? 4    ASN   E CG  1 
ATOM   11527 O  OD1 . ASN   E 2 4   ? 12.938  -6.402  -21.954 1.00 95.38  ? 4    ASN   E OD1 1 
ATOM   11528 N  ND2 . ASN   E 2 4   ? 12.964  -8.369  -20.915 1.00 89.36  ? 4    ASN   E ND2 1 
ATOM   11529 N  N   . TYR   E 2 5   ? 11.542  -7.468  -26.106 1.00 92.30  ? 5    TYR   E N   1 
ATOM   11530 C  CA  . TYR   E 2 5   ? 11.311  -7.447  -27.544 1.00 89.75  ? 5    TYR   E CA  1 
ATOM   11531 C  C   . TYR   E 2 5   ? 12.687  -7.407  -28.196 1.00 89.94  ? 5    TYR   E C   1 
ATOM   11532 O  O   . TYR   E 2 5   ? 13.509  -6.558  -27.834 1.00 91.92  ? 5    TYR   E O   1 
ATOM   11533 C  CB  . TYR   E 2 5   ? 10.449  -6.219  -27.900 1.00 90.80  ? 5    TYR   E CB  1 
ATOM   11534 C  CG  . TYR   E 2 5   ? 10.272  -5.871  -29.371 1.00 89.36  ? 5    TYR   E CG  1 
ATOM   11535 C  CD1 . TYR   E 2 5   ? 11.241  -5.145  -30.056 1.00 86.58  ? 5    TYR   E CD1 1 
ATOM   11536 C  CD2 . TYR   E 2 5   ? 9.109   -6.212  -30.058 1.00 88.27  ? 5    TYR   E CD2 1 
ATOM   11537 C  CE1 . TYR   E 2 5   ? 11.072  -4.803  -31.406 1.00 88.49  ? 5    TYR   E CE1 1 
ATOM   11538 C  CE2 . TYR   E 2 5   ? 8.929   -5.873  -31.404 1.00 88.13  ? 5    TYR   E CE2 1 
ATOM   11539 C  CZ  . TYR   E 2 5   ? 9.911   -5.171  -32.078 1.00 90.55  ? 5    TYR   E CZ  1 
ATOM   11540 O  OH  . TYR   E 2 5   ? 9.741   -4.840  -33.419 1.00 88.72  ? 5    TYR   E OH  1 
ATOM   11541 N  N   . VAL   E 2 6   ? 12.975  -8.354  -29.094 1.00 86.72  ? 6    VAL   E N   1 
ATOM   11542 C  CA  . VAL   E 2 6   ? 14.286  -8.457  -29.742 1.00 82.21  ? 6    VAL   E CA  1 
ATOM   11543 C  C   . VAL   E 2 6   ? 14.079  -8.253  -31.231 1.00 83.23  ? 6    VAL   E C   1 
ATOM   11544 O  O   . VAL   E 2 6   ? 13.116  -8.781  -31.804 1.00 89.13  ? 6    VAL   E O   1 
ATOM   11545 C  CB  . VAL   E 2 6   ? 14.988  -9.813  -29.484 1.00 81.11  ? 6    VAL   E CB  1 
ATOM   11546 C  CG1 . VAL   E 2 6   ? 15.067  -10.114 -28.013 1.00 85.47  ? 6    VAL   E CG1 1 
ATOM   11547 C  CG2 . VAL   E 2 6   ? 14.258  -10.950 -30.192 1.00 83.39  ? 6    VAL   E CG2 1 
ATOM   11548 N  N   . VAL   E 2 7   ? 14.973  -7.495  -31.863 1.00 79.14  ? 7    VAL   E N   1 
ATOM   11549 C  CA  . VAL   E 2 7   ? 14.880  -7.303  -33.305 1.00 84.83  ? 7    VAL   E CA  1 
ATOM   11550 C  C   . VAL   E 2 7   ? 16.280  -7.244  -33.899 1.00 84.13  ? 7    VAL   E C   1 
ATOM   11551 O  O   . VAL   E 2 7   ? 17.242  -6.786  -33.268 1.00 77.66  ? 7    VAL   E O   1 
ATOM   11552 C  CB  . VAL   E 2 7   ? 14.054  -6.049  -33.696 1.00 84.42  ? 7    VAL   E CB  1 
ATOM   11553 C  CG1 . VAL   E 2 7   ? 14.700  -4.804  -33.149 1.00 86.10  ? 7    VAL   E CG1 1 
ATOM   11554 C  CG2 . VAL   E 2 7   ? 13.857  -5.970  -35.223 1.00 85.24  ? 7    VAL   E CG2 1 
ATOM   11555 N  N   . THR   E 2 8   ? 16.391  -7.746  -35.120 1.00 82.21  ? 8    THR   E N   1 
ATOM   11556 C  CA  . THR   E 2 8   ? 17.685  -7.811  -35.765 1.00 83.76  ? 8    THR   E CA  1 
ATOM   11557 C  C   . THR   E 2 8   ? 18.006  -6.452  -36.343 1.00 84.81  ? 8    THR   E C   1 
ATOM   11558 O  O   . THR   E 2 8   ? 17.298  -5.966  -37.236 1.00 89.13  ? 8    THR   E O   1 
ATOM   11559 C  CB  . THR   E 2 8   ? 17.724  -8.868  -36.857 1.00 82.59  ? 8    THR   E CB  1 
ATOM   11560 O  OG1 . THR   E 2 8   ? 17.534  -10.161 -36.266 1.00 85.81  ? 8    THR   E OG1 1 
ATOM   11561 C  CG2 . THR   E 2 8   ? 19.085  -8.813  -37.544 1.00 79.86  ? 8    THR   E CG2 1 
ATOM   11562 N  N   . ALA   E 2 9   ? 19.059  -5.839  -35.818 1.00 78.77  ? 9    ALA   E N   1 
ATOM   11563 C  CA  . ALA   E 2 9   ? 19.559  -4.617  -36.425 1.00 83.59  ? 9    ALA   E CA  1 
ATOM   11564 C  C   . ALA   E 2 9   ? 20.489  -4.931  -37.581 1.00 80.87  ? 9    ALA   E C   1 
ATOM   11565 O  O   . ALA   E 2 9   ? 20.450  -4.262  -38.617 1.00 86.90  ? 9    ALA   E O   1 
ATOM   11566 C  CB  . ALA   E 2 9   ? 20.277  -3.768  -35.372 1.00 85.98  ? 9    ALA   E CB  1 
ATOM   11567 N  N   . GLN   E 2 10  ? 21.324  -5.950  -37.417 1.00 83.50  ? 10   GLN   E N   1 
ATOM   11568 C  CA  . GLN   E 2 10  ? 22.238  -6.401  -38.455 1.00 83.44  ? 10   GLN   E CA  1 
ATOM   11569 C  C   . GLN   E 2 10  ? 22.123  -7.913  -38.558 1.00 85.44  ? 10   GLN   E C   1 
ATOM   11570 O  O   . GLN   E 2 10  ? 22.399  -8.623  -37.584 1.00 84.34  ? 10   GLN   E O   1 
ATOM   11571 C  CB  . GLN   E 2 10  ? 23.682  -5.981  -38.146 1.00 81.65  ? 10   GLN   E CB  1 
ATOM   11572 C  CG  . GLN   E 2 10  ? 24.731  -6.590  -39.060 1.00 83.18  ? 10   GLN   E CG  1 
ATOM   11573 C  CD  . GLN   E 2 10  ? 24.352  -6.506  -40.538 1.00 91.08  ? 10   GLN   E CD  1 
ATOM   11574 O  OE1 . GLN   E 2 10  ? 23.185  -6.705  -40.928 1.00 97.04  ? 10   GLN   E OE1 1 
ATOM   11575 N  NE2 . GLN   E 2 10  ? 25.346  -6.222  -41.375 1.00 93.31  ? 10   GLN   E NE2 1 
ATOM   11576 N  N   . LYS   E 2 11  ? 21.715  -8.398  -39.734 1.00 87.53  ? 11   LYS   E N   1 
ATOM   11577 C  CA  . LYS   E 2 11  ? 21.672  -9.834  -39.977 1.00 81.62  ? 11   LYS   E CA  1 
ATOM   11578 C  C   . LYS   E 2 11  ? 23.088  -10.415 -39.904 1.00 81.53  ? 11   LYS   E C   1 
ATOM   11579 O  O   . LYS   E 2 11  ? 24.068  -9.702  -40.124 1.00 81.35  ? 11   LYS   E O   1 
ATOM   11580 C  CB  . LYS   E 2 11  ? 21.020  -10.129 -41.333 1.00 76.03  ? 11   LYS   E CB  1 
ATOM   11581 N  N   . PRO   E 2 12  ? 23.220  -11.703 -39.574 1.00 80.56  ? 12   PRO   E N   1 
ATOM   11582 C  CA  . PRO   E 2 12  ? 24.552  -12.337 -39.483 1.00 79.36  ? 12   PRO   E CA  1 
ATOM   11583 C  C   . PRO   E 2 12  ? 25.369  -12.231 -40.770 1.00 77.31  ? 12   PRO   E C   1 
ATOM   11584 O  O   . PRO   E 2 12  ? 24.861  -12.462 -41.863 1.00 75.75  ? 12   PRO   E O   1 
ATOM   11585 C  CB  . PRO   E 2 12  ? 24.215  -13.802 -39.182 1.00 82.25  ? 12   PRO   E CB  1 
ATOM   11586 C  CG  . PRO   E 2 12  ? 22.782  -13.968 -39.740 1.00 86.22  ? 12   PRO   E CG  1 
ATOM   11587 C  CD  . PRO   E 2 12  ? 22.132  -12.664 -39.353 1.00 82.56  ? 12   PRO   E CD  1 
ATOM   11588 N  N   . THR   E 2 13  ? 26.670  -11.964 -40.624 1.00 77.27  ? 13   THR   E N   1 
ATOM   11589 C  CA  . THR   E 2 13  ? 27.527  -11.651 -41.765 1.00 77.12  ? 13   THR   E CA  1 
ATOM   11590 C  C   . THR   E 2 13  ? 28.513  -12.743 -42.146 1.00 76.93  ? 13   THR   E C   1 
ATOM   11591 O  O   . THR   E 2 13  ? 28.959  -12.761 -43.296 1.00 76.79  ? 13   THR   E O   1 
ATOM   11592 C  CB  . THR   E 2 13  ? 28.302  -10.341 -41.497 1.00 80.95  ? 13   THR   E CB  1 
ATOM   11593 O  OG1 . THR   E 2 13  ? 29.537  -10.606 -40.819 1.00 80.88  ? 13   THR   E OG1 1 
ATOM   11594 C  CG2 . THR   E 2 13  ? 27.478  -9.435  -40.618 1.00 80.68  ? 13   THR   E CG2 1 
ATOM   11595 N  N   . ALA   E 2 14  ? 28.875  -13.633 -41.219 1.00 81.62  ? 14   ALA   E N   1 
ATOM   11596 C  CA  . ALA   E 2 14  ? 29.766  -14.756 -41.512 1.00 81.27  ? 14   ALA   E CA  1 
ATOM   11597 C  C   . ALA   E 2 14  ? 29.065  -15.784 -42.385 1.00 79.30  ? 14   ALA   E C   1 
ATOM   11598 O  O   . ALA   E 2 14  ? 27.847  -15.939 -42.320 1.00 80.33  ? 14   ALA   E O   1 
ATOM   11599 C  CB  . ALA   E 2 14  ? 30.231  -15.426 -40.220 1.00 81.19  ? 14   ALA   E CB  1 
ATOM   11600 N  N   . VAL   E 2 15  ? 29.847  -16.525 -43.169 1.00 79.78  ? 15   VAL   E N   1 
ATOM   11601 C  CA  . VAL   E 2 15  ? 29.242  -17.605 -44.002 1.00 83.98  ? 15   VAL   E CA  1 
ATOM   11602 C  C   . VAL   E 2 15  ? 29.549  -18.966 -43.361 1.00 81.65  ? 15   VAL   E C   1 
ATOM   11603 O  O   . VAL   E 2 15  ? 30.653  -19.129 -42.805 1.00 83.35  ? 15   VAL   E O   1 
ATOM   11604 C  CB  . VAL   E 2 15  ? 29.680  -17.550 -45.475 1.00 85.17  ? 15   VAL   E CB  1 
ATOM   11605 C  CG1 . VAL   E 2 15  ? 29.953  -16.127 -45.938 1.00 83.91  ? 15   VAL   E CG1 1 
ATOM   11606 C  CG2 . VAL   E 2 15  ? 30.852  -18.470 -45.775 1.00 84.57  ? 15   VAL   E CG2 1 
ATOM   11607 N  N   . ASN   E 2 16  ? 28.585  -19.887 -43.409 1.00 83.37  ? 16   ASN   E N   1 
ATOM   11608 C  CA  . ASN   E 2 16  ? 28.772  -21.227 -42.794 1.00 88.81  ? 16   ASN   E CA  1 
ATOM   11609 C  C   . ASN   E 2 16  ? 28.764  -22.292 -43.893 1.00 86.43  ? 16   ASN   E C   1 
ATOM   11610 O  O   . ASN   E 2 16  ? 29.023  -23.466 -43.579 1.00 94.05  ? 16   ASN   E O   1 
ATOM   11611 C  CB  . ASN   E 2 16  ? 27.726  -21.498 -41.721 1.00 86.68  ? 16   ASN   E CB  1 
ATOM   11612 C  CG  . ASN   E 2 16  ? 26.324  -21.540 -42.274 1.00 86.04  ? 16   ASN   E CG  1 
ATOM   11613 O  OD1 . ASN   E 2 16  ? 25.723  -20.489 -42.508 1.00 92.30  ? 16   ASN   E OD1 1 
ATOM   11614 N  ND2 . ASN   E 2 16  ? 25.785  -22.733 -42.471 1.00 84.80  ? 16   ASN   E ND2 1 
ATOM   11615 N  N   . GLY   E 2 17  ? 28.482  -21.891 -45.132 1.00 88.27  ? 17   GLY   E N   1 
ATOM   11616 C  CA  . GLY   E 2 17  ? 28.406  -22.861 -46.237 1.00 93.11  ? 17   GLY   E CA  1 
ATOM   11617 C  C   . GLY   E 2 17  ? 28.252  -22.180 -47.580 1.00 93.45  ? 17   GLY   E C   1 
ATOM   11618 O  O   . GLY   E 2 17  ? 27.567  -21.142 -47.643 1.00 95.32  ? 17   GLY   E O   1 
ATOM   11619 N  N   . CYS   E 2 18  ? 28.856  -22.752 -48.621 1.00 90.63  ? 18   CYS   E N   1 
ATOM   11620 C  CA  . CYS   E 2 18  ? 28.795  -22.153 -49.975 1.00 86.75  ? 18   CYS   E CA  1 
ATOM   11621 C  C   . CYS   E 2 18  ? 28.839  -23.279 -51.019 1.00 91.39  ? 18   CYS   E C   1 
ATOM   11622 O  O   . CYS   E 2 18  ? 29.869  -23.971 -51.090 1.00 96.15  ? 18   CYS   E O   1 
ATOM   11623 C  CB  . CYS   E 2 18  ? 29.924  -21.146 -50.157 1.00 84.77  ? 18   CYS   E CB  1 
ATOM   11624 S  SG  . CYS   E 2 18  ? 31.576  -21.773 -49.760 1.00 98.23  ? 18   CYS   E SG  1 
ATOM   11625 N  N   . VAL   E 2 19  ? 27.757  -23.454 -51.785 1.00 89.81  ? 19   VAL   E N   1 
ATOM   11626 C  CA  . VAL   E 2 19  ? 27.701  -24.537 -52.813 1.00 90.34  ? 19   VAL   E CA  1 
ATOM   11627 C  C   . VAL   E 2 19  ? 27.348  -23.945 -54.185 1.00 90.00  ? 19   VAL   E C   1 
ATOM   11628 O  O   . VAL   E 2 19  ? 26.676  -22.898 -54.225 1.00 90.10  ? 19   VAL   E O   1 
ATOM   11629 C  CB  . VAL   E 2 19  ? 26.710  -25.659 -52.452 1.00 92.48  ? 19   VAL   E CB  1 
ATOM   11630 C  CG1 . VAL   E 2 19  ? 27.125  -26.414 -51.196 1.00 90.95  ? 19   VAL   E CG1 1 
ATOM   11631 C  CG2 . VAL   E 2 19  ? 25.278  -25.152 -52.341 1.00 89.43  ? 19   VAL   E CG2 1 
ATOM   11632 N  N   . THR   E 2 20  ? 27.788  -24.601 -55.258 1.00 92.66  ? 20   THR   E N   1 
ATOM   11633 C  CA  . THR   E 2 20  ? 27.449  -24.160 -56.624 1.00 92.66  ? 20   THR   E CA  1 
ATOM   11634 C  C   . THR   E 2 20  ? 26.472  -25.155 -57.197 1.00 96.77  ? 20   THR   E C   1 
ATOM   11635 O  O   . THR   E 2 20  ? 26.415  -26.281 -56.672 1.00 96.42  ? 20   THR   E O   1 
ATOM   11636 C  CB  . THR   E 2 20  ? 28.718  -24.086 -57.466 1.00 93.15  ? 20   THR   E CB  1 
ATOM   11637 O  OG1 . THR   E 2 20  ? 29.527  -25.175 -57.033 1.00 106.83 ? 20   THR   E OG1 1 
ATOM   11638 C  CG2 . THR   E 2 20  ? 29.461  -22.777 -57.277 1.00 88.70  ? 20   THR   E CG2 1 
ATOM   11639 N  N   . GLY   E 2 21  ? 25.728  -24.777 -58.237 1.00 97.23  ? 21   GLY   E N   1 
ATOM   11640 C  CA  . GLY   E 2 21  ? 24.723  -25.674 -58.761 1.00 99.69  ? 21   GLY   E CA  1 
ATOM   11641 C  C   . GLY   E 2 21  ? 23.857  -24.961 -59.777 1.00 104.47 ? 21   GLY   E C   1 
ATOM   11642 O  O   . GLY   E 2 21  ? 24.203  -23.882 -60.273 1.00 101.92 ? 21   GLY   E O   1 
ATOM   11643 N  N   . HIS   E 2 22  ? 22.722  -25.598 -60.079 1.00 103.85 ? 22   HIS   E N   1 
ATOM   11644 C  CA  . HIS   E 2 22  ? 21.729  -25.077 -61.016 1.00 105.82 ? 22   HIS   E CA  1 
ATOM   11645 C  C   . HIS   E 2 22  ? 20.357  -25.252 -60.365 1.00 108.62 ? 22   HIS   E C   1 
ATOM   11646 O  O   . HIS   E 2 22  ? 19.623  -26.204 -60.636 1.00 112.26 ? 22   HIS   E O   1 
ATOM   11647 C  CB  . HIS   E 2 22  ? 21.831  -25.778 -62.343 1.00 106.11 ? 22   HIS   E CB  1 
ATOM   11648 C  CG  . HIS   E 2 22  ? 23.211  -26.264 -62.651 1.00 104.73 ? 22   HIS   E CG  1 
ATOM   11649 N  ND1 . HIS   E 2 22  ? 24.152  -25.477 -63.284 1.00 102.68 ? 22   HIS   E ND1 1 
ATOM   11650 C  CD2 . HIS   E 2 22  ? 23.817  -27.450 -62.397 1.00 106.34 ? 22   HIS   E CD2 1 
ATOM   11651 C  CE1 . HIS   E 2 22  ? 25.274  -26.164 -63.420 1.00 105.36 ? 22   HIS   E CE1 1 
ATOM   11652 N  NE2 . HIS   E 2 22  ? 25.099  -27.364 -62.889 1.00 108.66 ? 22   HIS   E NE2 1 
ATOM   11653 N  N   . PHE   E 2 23  ? 20.028  -24.306 -59.494 1.00 108.51 ? 23   PHE   E N   1 
ATOM   11654 C  CA  . PHE   E 2 23  ? 18.817  -24.254 -58.694 1.00 110.97 ? 23   PHE   E CA  1 
ATOM   11655 C  C   . PHE   E 2 23  ? 17.702  -23.432 -59.354 1.00 114.96 ? 23   PHE   E C   1 
ATOM   11656 O  O   . PHE   E 2 23  ? 16.532  -23.860 -59.319 1.00 115.56 ? 23   PHE   E O   1 
ATOM   11657 C  CB  . PHE   E 2 23  ? 19.182  -23.666 -57.325 1.00 109.46 ? 23   PHE   E CB  1 
ATOM   11658 C  CG  . PHE   E 2 23  ? 18.144  -23.888 -56.268 1.00 108.70 ? 23   PHE   E CG  1 
ATOM   11659 C  CD1 . PHE   E 2 23  ? 17.578  -25.135 -56.098 1.00 109.96 ? 23   PHE   E CD1 1 
ATOM   11660 C  CD2 . PHE   E 2 23  ? 17.708  -22.836 -55.475 1.00 104.66 ? 23   PHE   E CD2 1 
ATOM   11661 C  CE1 . PHE   E 2 23  ? 16.613  -25.350 -55.151 1.00 106.54 ? 23   PHE   E CE1 1 
ATOM   11662 C  CE2 . PHE   E 2 23  ? 16.746  -23.036 -54.533 1.00 105.64 ? 23   PHE   E CE2 1 
ATOM   11663 C  CZ  . PHE   E 2 23  ? 16.195  -24.302 -54.367 1.00 107.86 ? 23   PHE   E CZ  1 
ATOM   11664 N  N   . THR   E 2 24  ? 18.057  -22.272 -59.953 1.00 117.30 ? 24   THR   E N   1 
ATOM   11665 C  CA  . THR   E 2 24  ? 17.128  -21.380 -60.663 1.00 120.96 ? 24   THR   E CA  1 
ATOM   11666 C  C   . THR   E 2 24  ? 16.712  -21.944 -62.032 1.00 123.63 ? 24   THR   E C   1 
ATOM   11667 O  O   . THR   E 2 24  ? 15.515  -22.036 -62.324 1.00 125.00 ? 24   THR   E O   1 
ATOM   11668 C  CB  . THR   E 2 24  ? 17.737  -19.956 -60.797 1.00 122.89 ? 24   THR   E CB  1 
ATOM   11669 O  OG1 . THR   E 2 24  ? 18.639  -19.845 -61.916 1.00 122.06 ? 24   THR   E OG1 1 
ATOM   11670 C  CG2 . THR   E 2 24  ? 18.472  -19.525 -59.527 1.00 118.87 ? 24   THR   E CG2 1 
ATOM   11671 N  N   . SER   E 2 25  ? 17.678  -22.326 -62.876 1.00 118.60 ? 25   SER   E N   1 
ATOM   11672 C  CA  . SER   E 2 25  ? 17.452  -23.011 -64.147 1.00 113.87 ? 25   SER   E CA  1 
ATOM   11673 C  C   . SER   E 2 25  ? 18.645  -23.916 -64.418 1.00 114.11 ? 25   SER   E C   1 
ATOM   11674 O  O   . SER   E 2 25  ? 19.741  -23.696 -63.886 1.00 108.66 ? 25   SER   E O   1 
ATOM   11675 C  CB  . SER   E 2 25  ? 17.259  -22.014 -65.309 1.00 116.49 ? 25   SER   E CB  1 
ATOM   11676 O  OG  . SER   E 2 25  ? 16.080  -21.224 -65.167 1.00 116.61 ? 25   SER   E OG  1 
ATOM   11677 N  N   . ALA   E 2 26  ? 18.419  -24.950 -65.238 1.00 114.45 ? 26   ALA   E N   1 
ATOM   11678 C  CA  . ALA   E 2 26  ? 19.543  -25.780 -65.669 1.00 111.49 ? 26   ALA   E CA  1 
ATOM   11679 C  C   . ALA   E 2 26  ? 20.553  -24.971 -66.499 1.00 113.07 ? 26   ALA   E C   1 
ATOM   11680 O  O   . ALA   E 2 26  ? 21.724  -25.362 -66.602 1.00 109.89 ? 26   ALA   E O   1 
ATOM   11681 C  CB  . ALA   E 2 26  ? 19.026  -27.007 -66.436 1.00 99.75  ? 26   ALA   E CB  1 
ATOM   11682 N  N   . GLU   E 2 27  ? 20.145  -23.811 -67.018 1.00 113.91 ? 27   GLU   E N   1 
ATOM   11683 C  CA  . GLU   E 2 27  ? 20.983  -22.982 -67.862 1.00 110.89 ? 27   GLU   E CA  1 
ATOM   11684 C  C   . GLU   E 2 27  ? 21.690  -21.856 -67.088 1.00 113.78 ? 27   GLU   E C   1 
ATOM   11685 O  O   . GLU   E 2 27  ? 22.440  -21.082 -67.704 1.00 115.13 ? 27   GLU   E O   1 
ATOM   11686 C  CB  . GLU   E 2 27  ? 20.145  -22.408 -69.016 1.00 107.45 ? 27   GLU   E CB  1 
ATOM   11687 N  N   . ASP   E 2 28  ? 21.486  -21.750 -65.772 1.00 114.72 ? 28   ASP   E N   1 
ATOM   11688 C  CA  . ASP   E 2 28  ? 22.114  -20.749 -64.912 1.00 112.82 ? 28   ASP   E CA  1 
ATOM   11689 C  C   . ASP   E 2 28  ? 23.137  -21.379 -63.966 1.00 111.54 ? 28   ASP   E C   1 
ATOM   11690 O  O   . ASP   E 2 28  ? 22.939  -22.483 -63.453 1.00 114.14 ? 28   ASP   E O   1 
ATOM   11691 C  CB  . ASP   E 2 28  ? 21.072  -19.996 -64.059 1.00 112.59 ? 28   ASP   E CB  1 
ATOM   11692 C  CG  . ASP   E 2 28  ? 20.160  -19.103 -64.881 1.00 118.91 ? 28   ASP   E CG  1 
ATOM   11693 O  OD1 . ASP   E 2 28  ? 20.542  -18.754 -66.020 1.00 125.27 ? 28   ASP   E OD1 1 
ATOM   11694 O  OD2 . ASP   E 2 28  ? 19.061  -18.743 -64.386 1.00 121.04 ? 28   ASP   E OD2 1 
ATOM   11695 N  N   . LEU   E 2 29  ? 24.239  -20.661 -63.722 1.00 107.34 ? 29   LEU   E N   1 
ATOM   11696 C  CA  . LEU   E 2 29  ? 25.217  -21.027 -62.692 1.00 105.72 ? 29   LEU   E CA  1 
ATOM   11697 C  C   . LEU   E 2 29  ? 24.880  -20.279 -61.405 1.00 104.93 ? 29   LEU   E C   1 
ATOM   11698 O  O   . LEU   E 2 29  ? 25.038  -19.052 -61.328 1.00 103.71 ? 29   LEU   E O   1 
ATOM   11699 C  CB  . LEU   E 2 29  ? 26.638  -20.704 -63.126 1.00 101.06 ? 29   LEU   E CB  1 
ATOM   11700 C  CG  . LEU   E 2 29  ? 27.564  -21.362 -62.115 1.00 97.43  ? 29   LEU   E CG  1 
ATOM   11701 C  CD1 . LEU   E 2 29  ? 26.960  -22.708 -61.659 1.00 96.69  ? 29   LEU   E CD1 1 
ATOM   11702 C  CD2 . LEU   E 2 29  ? 28.948  -21.487 -62.728 1.00 90.62  ? 29   LEU   E CD2 1 
ATOM   11703 N  N   . ASN   E 2 30  ? 24.431  -21.017 -60.393 1.00 101.31 ? 30   ASN   E N   1 
ATOM   11704 C  CA  . ASN   E 2 30  ? 24.013  -20.423 -59.131 1.00 100.78 ? 30   ASN   E CA  1 
ATOM   11705 C  C   . ASN   E 2 30  ? 25.107  -20.528 -58.086 1.00 100.54 ? 30   ASN   E C   1 
ATOM   11706 O  O   . ASN   E 2 30  ? 25.817  -21.539 -58.011 1.00 99.95  ? 30   ASN   E O   1 
ATOM   11707 C  CB  . ASN   E 2 30  ? 22.753  -21.098 -58.595 1.00 100.50 ? 30   ASN   E CB  1 
ATOM   11708 C  CG  . ASN   E 2 30  ? 21.553  -20.805 -59.432 1.00 106.11 ? 30   ASN   E CG  1 
ATOM   11709 O  OD1 . ASN   E 2 30  ? 21.330  -19.669 -59.837 1.00 108.00 ? 30   ASN   E OD1 1 
ATOM   11710 N  ND2 . ASN   E 2 30  ? 20.747  -21.827 -59.678 1.00 104.63 ? 30   ASN   E ND2 1 
ATOM   11711 N  N   . LEU   E 2 31  ? 25.227  -19.479 -57.283 1.00 99.69  ? 31   LEU   E N   1 
ATOM   11712 C  CA  . LEU   E 2 31  ? 26.023  -19.513 -56.069 1.00 94.44  ? 31   LEU   E CA  1 
ATOM   11713 C  C   . LEU   E 2 31  ? 25.062  -19.364 -54.902 1.00 93.37  ? 31   LEU   E C   1 
ATOM   11714 O  O   . LEU   E 2 31  ? 24.446  -18.304 -54.736 1.00 91.87  ? 31   LEU   E O   1 
ATOM   11715 C  CB  . LEU   E 2 31  ? 27.082  -18.422 -56.078 1.00 90.95  ? 31   LEU   E CB  1 
ATOM   11716 C  CG  . LEU   E 2 31  ? 27.863  -18.402 -54.783 1.00 91.64  ? 31   LEU   E CG  1 
ATOM   11717 C  CD1 . LEU   E 2 31  ? 28.136  -19.825 -54.372 1.00 87.01  ? 31   LEU   E CD1 1 
ATOM   11718 C  CD2 . LEU   E 2 31  ? 29.162  -17.639 -54.970 1.00 93.51  ? 31   LEU   E CD2 1 
ATOM   11719 N  N   . LEU   E 2 32  ? 24.904  -20.449 -54.130 1.00 93.31  ? 32   LEU   E N   1 
ATOM   11720 C  CA  . LEU   E 2 32  ? 24.094  -20.463 -52.915 1.00 88.36  ? 32   LEU   E CA  1 
ATOM   11721 C  C   . LEU   E 2 32  ? 24.992  -20.246 -51.709 1.00 90.37  ? 32   LEU   E C   1 
ATOM   11722 O  O   . LEU   E 2 32  ? 25.873  -21.067 -51.441 1.00 89.16  ? 32   LEU   E O   1 
ATOM   11723 C  CB  . LEU   E 2 32  ? 23.347  -21.780 -52.760 1.00 84.05  ? 32   LEU   E CB  1 
ATOM   11724 C  CG  . LEU   E 2 32  ? 22.207  -21.899 -53.753 1.00 91.78  ? 32   LEU   E CG  1 
ATOM   11725 C  CD1 . LEU   E 2 32  ? 21.165  -22.916 -53.271 1.00 90.78  ? 32   LEU   E CD1 1 
ATOM   11726 C  CD2 . LEU   E 2 32  ? 21.605  -20.517 -53.980 1.00 93.63  ? 32   LEU   E CD2 1 
ATOM   11727 N  N   . ILE   E 2 33  ? 24.769  -19.150 -50.979 1.00 92.67  ? 33   ILE   E N   1 
ATOM   11728 C  CA  . ILE   E 2 33  ? 25.542  -18.818 -49.789 1.00 86.47  ? 33   ILE   E CA  1 
ATOM   11729 C  C   . ILE   E 2 33  ? 24.664  -18.978 -48.553 1.00 86.69  ? 33   ILE   E C   1 
ATOM   11730 O  O   . ILE   E 2 33  ? 23.481  -18.605 -48.562 1.00 84.32  ? 33   ILE   E O   1 
ATOM   11731 C  CB  . ILE   E 2 33  ? 26.128  -17.398 -49.882 1.00 84.80  ? 33   ILE   E CB  1 
ATOM   11732 C  CG1 . ILE   E 2 33  ? 27.402  -17.425 -50.709 1.00 89.54  ? 33   ILE   E CG1 1 
ATOM   11733 C  CG2 . ILE   E 2 33  ? 26.447  -16.870 -48.505 1.00 82.69  ? 33   ILE   E CG2 1 
ATOM   11734 C  CD1 . ILE   E 2 33  ? 27.972  -16.042 -50.939 1.00 92.05  ? 33   ILE   E CD1 1 
ATOM   11735 N  N   . ALA   E 2 34  ? 25.247  -19.552 -47.496 1.00 84.90  ? 34   ALA   E N   1 
ATOM   11736 C  CA  . ALA   E 2 34  ? 24.569  -19.800 -46.233 1.00 83.23  ? 34   ALA   E CA  1 
ATOM   11737 C  C   . ALA   E 2 34  ? 25.211  -18.961 -45.141 1.00 85.64  ? 34   ALA   E C   1 
ATOM   11738 O  O   . ALA   E 2 34  ? 26.434  -18.998 -44.950 1.00 83.49  ? 34   ALA   E O   1 
ATOM   11739 C  CB  . ALA   E 2 34  ? 24.618  -21.276 -45.854 1.00 75.48  ? 34   ALA   E CB  1 
ATOM   11740 N  N   . LYS   E 2 35  ? 24.377  -18.211 -44.418 1.00 84.47  ? 35   LYS   E N   1 
ATOM   11741 C  CA  . LYS   E 2 35  ? 24.817  -17.313 -43.353 1.00 78.46  ? 35   LYS   E CA  1 
ATOM   11742 C  C   . LYS   E 2 35  ? 23.888  -17.603 -42.173 1.00 84.00  ? 35   LYS   E C   1 
ATOM   11743 O  O   . LYS   E 2 35  ? 22.946  -16.863 -41.892 1.00 87.94  ? 35   LYS   E O   1 
ATOM   11744 C  CB  . LYS   E 2 35  ? 24.788  -15.846 -43.809 1.00 82.32  ? 35   LYS   E CB  1 
ATOM   11745 C  CG  . LYS   E 2 35  ? 25.954  -15.356 -44.714 1.00 74.14  ? 35   LYS   E CG  1 
ATOM   11746 C  CD  . LYS   E 2 35  ? 25.518  -14.151 -45.562 1.00 76.78  ? 35   LYS   E CD  1 
ATOM   11747 C  CE  . LYS   E 2 35  ? 26.675  -13.485 -46.323 1.00 82.49  ? 35   LYS   E CE  1 
ATOM   11748 N  NZ  . LYS   E 2 35  ? 26.275  -12.326 -47.190 1.00 70.56  ? 35   LYS   E NZ  1 
ATOM   11749 N  N   . ASN   E 2 36  ? 24.154  -18.721 -41.495 1.00 85.04  ? 36   ASN   E N   1 
ATOM   11750 C  CA  . ASN   E 2 36  ? 23.408  -19.146 -40.312 1.00 87.32  ? 36   ASN   E CA  1 
ATOM   11751 C  C   . ASN   E 2 36  ? 21.989  -19.121 -40.880 1.00 86.43  ? 36   ASN   E C   1 
ATOM   11752 O  O   . ASN   E 2 36  ? 21.731  -19.719 -41.932 1.00 86.41  ? 36   ASN   E O   1 
ATOM   11753 C  CB  . ASN   E 2 36  ? 23.602  -18.145 -39.170 1.00 85.29  ? 36   ASN   E CB  1 
ATOM   11754 C  CG  . ASN   E 2 36  ? 23.193  -18.745 -37.821 1.00 84.66  ? 36   ASN   E CG  1 
ATOM   11755 O  OD1 . ASN   E 2 36  ? 22.768  -19.916 -37.738 1.00 85.74  ? 36   ASN   E OD1 1 
ATOM   11756 N  ND2 . ASN   E 2 36  ? 23.338  -17.965 -36.762 1.00 82.44  ? 36   ASN   E ND2 1 
ATOM   11757 N  N   . THR   E 2 37  ? 21.060  -18.480 -40.167 1.00 86.72  ? 37   THR   E N   1 
ATOM   11758 C  CA  . THR   E 2 37  ? 19.667  -18.387 -40.590 1.00 84.81  ? 37   THR   E CA  1 
ATOM   11759 C  C   . THR   E 2 37  ? 19.285  -17.983 -42.003 1.00 88.54  ? 37   THR   E C   1 
ATOM   11760 O  O   . THR   E 2 37  ? 18.170  -18.292 -42.446 1.00 91.48  ? 37   THR   E O   1 
ATOM   11761 C  CB  . THR   E 2 37  ? 18.923  -17.615 -39.496 1.00 85.77  ? 37   THR   E CB  1 
ATOM   11762 O  OG1 . THR   E 2 37  ? 18.923  -16.227 -39.827 1.00 92.56  ? 37   THR   E OG1 1 
ATOM   11763 C  CG2 . THR   E 2 37  ? 19.604  -17.778 -38.151 1.00 88.61  ? 37   THR   E CG2 1 
ATOM   11764 N  N   . ARG   E 2 38  ? 20.171  -17.286 -42.713 1.00 88.32  ? 38   ARG   E N   1 
ATOM   11765 C  CA  . ARG   E 2 38  ? 19.878  -16.745 -44.033 1.00 89.58  ? 38   ARG   E CA  1 
ATOM   11766 C  C   . ARG   E 2 38  ? 20.445  -17.569 -45.181 1.00 89.73  ? 38   ARG   E C   1 
ATOM   11767 O  O   . ARG   E 2 38  ? 21.525  -18.158 -45.063 1.00 89.34  ? 38   ARG   E O   1 
ATOM   11768 C  CB  . ARG   E 2 38  ? 20.447  -15.322 -44.068 1.00 84.30  ? 38   ARG   E CB  1 
ATOM   11769 C  CG  . ARG   E 2 38  ? 20.135  -14.554 -42.799 1.00 85.21  ? 38   ARG   E CG  1 
ATOM   11770 C  CD  . ARG   E 2 38  ? 18.630  -14.442 -42.618 1.00 87.38  ? 38   ARG   E CD  1 
ATOM   11771 N  NE  . ARG   E 2 38  ? 18.016  -13.781 -43.766 1.00 89.91  ? 38   ARG   E NE  1 
ATOM   11772 C  CZ  . ARG   E 2 38  ? 16.753  -13.373 -43.810 1.00 92.47  ? 38   ARG   E CZ  1 
ATOM   11773 N  NH1 . ARG   E 2 38  ? 15.929  -13.572 -42.787 1.00 89.92  ? 38   ARG   E NH1 1 
ATOM   11774 N  NH2 . ARG   E 2 38  ? 16.309  -12.744 -44.902 1.00 89.01  ? 38   ARG   E NH2 1 
ATOM   11775 N  N   . LEU   E 2 39  ? 19.701  -17.618 -46.285 1.00 90.64  ? 39   LEU   E N   1 
ATOM   11776 C  CA  . LEU   E 2 39  ? 20.126  -18.278 -47.510 1.00 87.94  ? 39   LEU   E CA  1 
ATOM   11777 C  C   . LEU   E 2 39  ? 20.244  -17.224 -48.602 1.00 90.21  ? 39   LEU   E C   1 
ATOM   11778 O  O   . LEU   E 2 39  ? 19.280  -16.499 -48.867 1.00 90.67  ? 39   LEU   E O   1 
ATOM   11779 C  CB  . LEU   E 2 39  ? 19.132  -19.373 -47.907 1.00 83.70  ? 39   LEU   E CB  1 
ATOM   11780 C  CG  . LEU   E 2 39  ? 19.451  -20.000 -49.260 1.00 92.32  ? 39   LEU   E CG  1 
ATOM   11781 C  CD1 . LEU   E 2 39  ? 20.905  -20.458 -49.292 1.00 92.66  ? 39   LEU   E CD1 1 
ATOM   11782 C  CD2 . LEU   E 2 39  ? 18.534  -21.161 -49.556 1.00 86.33  ? 39   LEU   E CD2 1 
ATOM   11783 N  N   . GLU   E 2 40  ? 21.415  -17.122 -49.221 1.00 86.28  ? 40   GLU   E N   1 
ATOM   11784 C  CA  . GLU   E 2 40  ? 21.607  -16.183 -50.320 1.00 92.60  ? 40   GLU   E CA  1 
ATOM   11785 C  C   . GLU   E 2 40  ? 21.740  -16.953 -51.619 1.00 92.96  ? 40   GLU   E C   1 
ATOM   11786 O  O   . GLU   E 2 40  ? 22.508  -17.916 -51.698 1.00 92.93  ? 40   GLU   E O   1 
ATOM   11787 C  CB  . GLU   E 2 40  ? 22.824  -15.281 -50.103 1.00 88.02  ? 40   GLU   E CB  1 
ATOM   11788 C  CG  . GLU   E 2 40  ? 22.610  -14.396 -48.919 1.00 89.25  ? 40   GLU   E CG  1 
ATOM   11789 C  CD  . GLU   E 2 40  ? 23.726  -13.412 -48.680 1.00 92.60  ? 40   GLU   E CD  1 
ATOM   11790 O  OE1 . GLU   E 2 40  ? 24.833  -13.613 -49.247 1.00 91.13  ? 40   GLU   E OE1 1 
ATOM   11791 O  OE2 . GLU   E 2 40  ? 23.479  -12.438 -47.913 1.00 87.91  ? 40   GLU   E OE2 1 
ATOM   11792 N  N   . ILE   E 2 41  ? 20.975  -16.538 -52.624 1.00 93.87  ? 41   ILE   E N   1 
ATOM   11793 C  CA  . ILE   E 2 41  ? 20.998  -17.156 -53.941 1.00 96.34  ? 41   ILE   E CA  1 
ATOM   11794 C  C   . ILE   E 2 41  ? 21.471  -16.130 -54.955 1.00 99.47  ? 41   ILE   E C   1 
ATOM   11795 O  O   . ILE   E 2 41  ? 20.809  -15.102 -55.155 1.00 99.00  ? 41   ILE   E O   1 
ATOM   11796 C  CB  . ILE   E 2 41  ? 19.623  -17.689 -54.346 1.00 94.16  ? 41   ILE   E CB  1 
ATOM   11797 C  CG1 . ILE   E 2 41  ? 19.157  -18.753 -53.360 1.00 89.66  ? 41   ILE   E CG1 1 
ATOM   11798 C  CG2 . ILE   E 2 41  ? 19.693  -18.173 -55.789 1.00 95.82  ? 41   ILE   E CG2 1 
ATOM   11799 C  CD1 . ILE   E 2 41  ? 17.686  -18.961 -53.413 1.00 90.89  ? 41   ILE   E CD1 1 
ATOM   11800 N  N   . TYR   E 2 42  ? 22.583  -16.440 -55.625 1.00 97.04  ? 42   TYR   E N   1 
ATOM   11801 C  CA  . TYR   E 2 42  ? 23.169  -15.610 -56.662 1.00 97.29  ? 42   TYR   E CA  1 
ATOM   11802 C  C   . TYR   E 2 42  ? 23.225  -16.383 -57.974 1.00 100.01 ? 42   TYR   E C   1 
ATOM   11803 O  O   . TYR   E 2 42  ? 23.196  -17.618 -58.004 1.00 96.06  ? 42   TYR   E O   1 
ATOM   11804 C  CB  . TYR   E 2 42  ? 24.587  -15.151 -56.286 1.00 97.72  ? 42   TYR   E CB  1 
ATOM   11805 C  CG  . TYR   E 2 42  ? 24.674  -14.273 -55.045 1.00 98.30  ? 42   TYR   E CG  1 
ATOM   11806 C  CD1 . TYR   E 2 42  ? 24.074  -13.016 -55.012 1.00 102.94 ? 42   TYR   E CD1 1 
ATOM   11807 C  CD2 . TYR   E 2 42  ? 25.366  -14.693 -53.908 1.00 96.94  ? 42   TYR   E CD2 1 
ATOM   11808 C  CE1 . TYR   E 2 42  ? 24.148  -12.200 -53.870 1.00 102.08 ? 42   TYR   E CE1 1 
ATOM   11809 C  CE2 . TYR   E 2 42  ? 25.443  -13.879 -52.757 1.00 100.34 ? 42   TYR   E CE2 1 
ATOM   11810 C  CZ  . TYR   E 2 42  ? 24.832  -12.634 -52.751 1.00 99.15  ? 42   TYR   E CZ  1 
ATOM   11811 O  OH  . TYR   E 2 42  ? 24.891  -11.817 -51.640 1.00 96.34  ? 42   TYR   E OH  1 
ATOM   11812 N  N   . VAL   E 2 43  ? 23.318  -15.619 -59.058 1.00 106.21 ? 43   VAL   E N   1 
ATOM   11813 C  CA  . VAL   E 2 43  ? 23.606  -16.141 -60.384 1.00 105.27 ? 43   VAL   E CA  1 
ATOM   11814 C  C   . VAL   E 2 43  ? 24.990  -15.676 -60.810 1.00 107.42 ? 43   VAL   E C   1 
ATOM   11815 O  O   . VAL   E 2 43  ? 25.292  -14.472 -60.784 1.00 106.26 ? 43   VAL   E O   1 
ATOM   11816 C  CB  . VAL   E 2 43  ? 22.560  -15.708 -61.413 1.00 99.89  ? 43   VAL   E CB  1 
ATOM   11817 C  CG1 . VAL   E 2 43  ? 23.057  -16.119 -62.780 1.00 99.81  ? 43   VAL   E CG1 1 
ATOM   11818 C  CG2 . VAL   E 2 43  ? 21.238  -16.355 -61.083 1.00 98.67  ? 43   VAL   E CG2 1 
ATOM   11819 N  N   . VAL   E 2 44  ? 25.815  -16.633 -61.225 1.00 104.59 ? 44   VAL   E N   1 
ATOM   11820 C  CA  . VAL   E 2 44  ? 27.206  -16.366 -61.552 1.00 109.13 ? 44   VAL   E CA  1 
ATOM   11821 C  C   . VAL   E 2 44  ? 27.244  -15.754 -62.952 1.00 116.48 ? 44   VAL   E C   1 
ATOM   11822 O  O   . VAL   E 2 44  ? 27.065  -16.449 -63.955 1.00 118.16 ? 44   VAL   E O   1 
ATOM   11823 C  CB  . VAL   E 2 44  ? 28.062  -17.636 -61.452 1.00 99.68  ? 44   VAL   E CB  1 
ATOM   11824 C  CG1 . VAL   E 2 44  ? 29.293  -17.502 -62.294 1.00 102.23 ? 44   VAL   E CG1 1 
ATOM   11825 C  CG2 . VAL   E 2 44  ? 28.463  -17.891 -60.016 1.00 98.50  ? 44   VAL   E CG2 1 
ATOM   11826 N  N   . THR   E 2 45  ? 27.486  -14.447 -63.027 1.00 120.57 ? 45   THR   E N   1 
ATOM   11827 C  CA  . THR   E 2 45  ? 27.674  -13.786 -64.311 1.00 121.70 ? 45   THR   E CA  1 
ATOM   11828 C  C   . THR   E 2 45  ? 29.152  -13.827 -64.715 1.00 125.65 ? 45   THR   E C   1 
ATOM   11829 O  O   . THR   E 2 45  ? 30.028  -14.231 -63.941 1.00 127.63 ? 45   THR   E O   1 
ATOM   11830 C  CB  . THR   E 2 45  ? 27.184  -12.342 -64.241 1.00 122.32 ? 45   THR   E CB  1 
ATOM   11831 O  OG1 . THR   E 2 45  ? 27.911  -11.646 -63.221 1.00 126.66 ? 45   THR   E OG1 1 
ATOM   11832 C  CG2 . THR   E 2 45  ? 25.700  -12.322 -63.899 1.00 120.47 ? 45   THR   E CG2 1 
ATOM   11833 N  N   . ALA   E 2 46  ? 29.428  -13.424 -65.959 1.00 126.31 ? 46   ALA   E N   1 
ATOM   11834 C  CA  . ALA   E 2 46  ? 30.814  -13.317 -66.391 1.00 122.60 ? 46   ALA   E CA  1 
ATOM   11835 C  C   . ALA   E 2 46  ? 31.533  -12.198 -65.650 1.00 127.47 ? 46   ALA   E C   1 
ATOM   11836 O  O   . ALA   E 2 46  ? 32.713  -12.353 -65.310 1.00 131.86 ? 46   ALA   E O   1 
ATOM   11837 C  CB  . ALA   E 2 46  ? 30.898  -13.094 -67.898 1.00 120.46 ? 46   ALA   E CB  1 
ATOM   11838 N  N   . GLU   E 2 47  ? 30.848  -11.082 -65.371 1.00 124.44 ? 47   GLU   E N   1 
ATOM   11839 C  CA  . GLU   E 2 47  ? 31.480  -9.958  -64.688 1.00 122.59 ? 47   GLU   E CA  1 
ATOM   11840 C  C   . GLU   E 2 47  ? 31.566  -10.169 -63.175 1.00 122.74 ? 47   GLU   E C   1 
ATOM   11841 O  O   . GLU   E 2 47  ? 32.529  -9.711  -62.540 1.00 116.98 ? 47   GLU   E O   1 
ATOM   11842 C  CB  . GLU   E 2 47  ? 30.730  -8.658  -65.008 1.00 118.73 ? 47   GLU   E CB  1 
ATOM   11843 N  N   . GLY   E 2 48  ? 30.587  -10.851 -62.585 1.00 123.61 ? 48   GLY   E N   1 
ATOM   11844 C  CA  . GLY   E 2 48  ? 30.604  -11.127 -61.163 1.00 118.83 ? 48   GLY   E CA  1 
ATOM   11845 C  C   . GLY   E 2 48  ? 29.402  -11.938 -60.726 1.00 113.94 ? 48   GLY   E C   1 
ATOM   11846 O  O   . GLY   E 2 48  ? 29.150  -13.014 -61.273 1.00 114.20 ? 48   GLY   E O   1 
ATOM   11847 N  N   . LEU   E 2 49  ? 28.645  -11.434 -59.763 1.00 111.90 ? 49   LEU   E N   1 
ATOM   11848 C  CA  . LEU   E 2 49  ? 27.486  -12.142 -59.258 1.00 113.21 ? 49   LEU   E CA  1 
ATOM   11849 C  C   . LEU   E 2 49  ? 26.236  -11.289 -59.477 1.00 113.91 ? 49   LEU   E C   1 
ATOM   11850 O  O   . LEU   E 2 49  ? 26.309  -10.061 -59.525 1.00 113.69 ? 49   LEU   E O   1 
ATOM   11851 C  CB  . LEU   E 2 49  ? 27.669  -12.486 -57.774 1.00 106.90 ? 49   LEU   E CB  1 
ATOM   11852 C  CG  . LEU   E 2 49  ? 28.818  -13.473 -57.523 1.00 98.80  ? 49   LEU   E CG  1 
ATOM   11853 C  CD1 . LEU   E 2 49  ? 29.430  -13.325 -56.145 1.00 93.04  ? 49   LEU   E CD1 1 
ATOM   11854 C  CD2 . LEU   E 2 49  ? 28.299  -14.868 -57.697 1.00 96.64  ? 49   LEU   E CD2 1 
ATOM   11855 N  N   . ARG   E 2 50  ? 25.091  -11.946 -59.658 1.00 115.91 ? 50   ARG   E N   1 
ATOM   11856 C  CA  . ARG   E 2 50  ? 23.818  -11.247 -59.812 1.00 112.21 ? 50   ARG   E CA  1 
ATOM   11857 C  C   . ARG   E 2 50  ? 22.885  -11.710 -58.710 1.00 111.10 ? 50   ARG   E C   1 
ATOM   11858 O  O   . ARG   E 2 50  ? 22.544  -12.910 -58.660 1.00 110.61 ? 50   ARG   E O   1 
ATOM   11859 C  CB  . ARG   E 2 50  ? 23.185  -11.484 -61.175 1.00 111.72 ? 50   ARG   E CB  1 
ATOM   11860 N  N   . PRO   E 2 51  ? 22.450  -10.814 -57.826 1.00 106.43 ? 51   PRO   E N   1 
ATOM   11861 C  CA  . PRO   E 2 51  ? 21.548  -11.217 -56.744 1.00 102.73 ? 51   PRO   E CA  1 
ATOM   11862 C  C   . PRO   E 2 51  ? 20.186  -11.671 -57.257 1.00 106.19 ? 51   PRO   E C   1 
ATOM   11863 O  O   . PRO   E 2 51  ? 19.535  -10.937 -58.017 1.00 112.89 ? 51   PRO   E O   1 
ATOM   11864 C  CB  . PRO   E 2 51  ? 21.430  -9.939  -55.891 1.00 103.88 ? 51   PRO   E CB  1 
ATOM   11865 C  CG  . PRO   E 2 51  ? 22.668  -9.154  -56.225 1.00 108.36 ? 51   PRO   E CG  1 
ATOM   11866 C  CD  . PRO   E 2 51  ? 23.005  -9.480  -57.645 1.00 104.83 ? 51   PRO   E CD  1 
ATOM   11867 N  N   . VAL   E 2 52  ? 19.765  -12.863 -56.830 1.00 102.74 ? 52   VAL   E N   1 
ATOM   11868 C  CA  . VAL   E 2 52  ? 18.520  -13.476 -57.274 1.00 102.38 ? 52   VAL   E CA  1 
ATOM   11869 C  C   . VAL   E 2 52  ? 17.450  -13.447 -56.167 1.00 101.40 ? 52   VAL   E C   1 
ATOM   11870 O  O   . VAL   E 2 52  ? 16.367  -12.868 -56.351 1.00 102.58 ? 52   VAL   E O   1 
ATOM   11871 C  CB  . VAL   E 2 52  ? 18.757  -14.913 -57.792 1.00 101.62 ? 52   VAL   E CB  1 
ATOM   11872 C  CG1 . VAL   E 2 52  ? 17.499  -15.449 -58.405 1.00 105.45 ? 52   VAL   E CG1 1 
ATOM   11873 C  CG2 . VAL   E 2 52  ? 19.897  -14.939 -58.782 1.00 101.51 ? 52   VAL   E CG2 1 
ATOM   11874 N  N   . LYS   E 2 53  ? 17.714  -14.105 -55.032 1.00 97.10  ? 53   LYS   E N   1 
ATOM   11875 C  CA  . LYS   E 2 53  ? 16.836  -13.948 -53.872 1.00 97.56  ? 53   LYS   E CA  1 
ATOM   11876 C  C   . LYS   E 2 53  ? 17.609  -14.292 -52.602 1.00 99.83  ? 53   LYS   E C   1 
ATOM   11877 O  O   . LYS   E 2 53  ? 18.599  -15.038 -52.645 1.00 99.60  ? 53   LYS   E O   1 
ATOM   11878 C  CB  . LYS   E 2 53  ? 15.568  -14.816 -53.954 1.00 91.10  ? 53   LYS   E CB  1 
ATOM   11879 N  N   . GLU   E 2 54  ? 17.153  -13.729 -51.480 1.00 94.19  ? 54   GLU   E N   1 
ATOM   11880 C  CA  . GLU   E 2 54  ? 17.724  -13.993 -50.163 1.00 93.64  ? 54   GLU   E CA  1 
ATOM   11881 C  C   . GLU   E 2 54  ? 16.574  -14.317 -49.220 1.00 92.68  ? 54   GLU   E C   1 
ATOM   11882 O  O   . GLU   E 2 54  ? 15.604  -13.560 -49.129 1.00 94.40  ? 54   GLU   E O   1 
ATOM   11883 C  CB  . GLU   E 2 54  ? 18.547  -12.792 -49.637 1.00 91.23  ? 54   GLU   E CB  1 
ATOM   11884 C  CG  . GLU   E 2 54  ? 19.420  -13.038 -48.406 1.00 91.60  ? 54   GLU   E CG  1 
ATOM   11885 C  CD  . GLU   E 2 54  ? 18.818  -12.470 -47.115 1.00 92.62  ? 54   GLU   E CD  1 
ATOM   11886 O  OE1 . GLU   E 2 54  ? 17.574  -12.329 -47.054 1.00 90.19  ? 54   GLU   E OE1 1 
ATOM   11887 O  OE2 . GLU   E 2 54  ? 19.588  -12.162 -46.167 1.00 89.48  ? 54   GLU   E OE2 1 
ATOM   11888 N  N   . VAL   E 2 55  ? 16.663  -15.447 -48.544 1.00 91.69  ? 55   VAL   E N   1 
ATOM   11889 C  CA  . VAL   E 2 55  ? 15.544  -15.950 -47.768 1.00 90.67  ? 55   VAL   E CA  1 
ATOM   11890 C  C   . VAL   E 2 55  ? 16.012  -16.133 -46.334 1.00 90.45  ? 55   VAL   E C   1 
ATOM   11891 O  O   . VAL   E 2 55  ? 17.212  -16.155 -46.045 1.00 90.37  ? 55   VAL   E O   1 
ATOM   11892 C  CB  . VAL   E 2 55  ? 15.007  -17.273 -48.351 1.00 91.48  ? 55   VAL   E CB  1 
ATOM   11893 C  CG1 . VAL   E 2 55  ? 16.050  -18.372 -48.203 1.00 88.98  ? 55   VAL   E CG1 1 
ATOM   11894 C  CG2 . VAL   E 2 55  ? 13.749  -17.661 -47.671 1.00 94.48  ? 55   VAL   E CG2 1 
ATOM   11895 N  N   . GLY   E 2 56  ? 15.047  -16.259 -45.431 1.00 92.19  ? 56   GLY   E N   1 
ATOM   11896 C  CA  . GLY   E 2 56  ? 15.327  -16.555 -44.041 1.00 88.71  ? 56   GLY   E CA  1 
ATOM   11897 C  C   . GLY   E 2 56  ? 14.665  -17.859 -43.647 1.00 92.74  ? 56   GLY   E C   1 
ATOM   11898 O  O   . GLY   E 2 56  ? 13.621  -18.236 -44.193 1.00 93.15  ? 56   GLY   E O   1 
ATOM   11899 N  N   . MET   E 2 57  ? 15.284  -18.545 -42.691 1.00 90.44  ? 57   MET   E N   1 
ATOM   11900 C  CA  . MET   E 2 57  ? 14.804  -19.826 -42.191 1.00 90.27  ? 57   MET   E CA  1 
ATOM   11901 C  C   . MET   E 2 57  ? 14.589  -19.753 -40.695 1.00 89.22  ? 57   MET   E C   1 
ATOM   11902 O  O   . MET   E 2 57  ? 15.296  -19.025 -39.998 1.00 93.80  ? 57   MET   E O   1 
ATOM   11903 C  CB  . MET   E 2 57  ? 15.802  -20.947 -42.450 1.00 89.54  ? 57   MET   E CB  1 
ATOM   11904 C  CG  . MET   E 2 57  ? 16.160  -21.143 -43.881 1.00 94.31  ? 57   MET   E CG  1 
ATOM   11905 S  SD  . MET   E 2 57  ? 16.086  -22.902 -44.134 1.00 103.95 ? 57   MET   E SD  1 
ATOM   11906 C  CE  . MET   E 2 57  ? 14.462  -23.233 -43.449 1.00 99.69  ? 57   MET   E CE  1 
ATOM   11907 N  N   . TYR   E 2 58  ? 13.639  -20.540 -40.199 1.00 89.08  ? 58   TYR   E N   1 
ATOM   11908 C  CA  . TYR   E 2 58  ? 13.489  -20.721 -38.755 1.00 84.20  ? 58   TYR   E CA  1 
ATOM   11909 C  C   . TYR   E 2 58  ? 14.408  -21.846 -38.276 1.00 84.61  ? 58   TYR   E C   1 
ATOM   11910 O  O   . TYR   E 2 58  ? 13.965  -22.910 -37.828 1.00 86.81  ? 58   TYR   E O   1 
ATOM   11911 C  CB  . TYR   E 2 58  ? 12.035  -21.011 -38.400 1.00 87.19  ? 58   TYR   E CB  1 
ATOM   11912 C  CG  . TYR   E 2 58  ? 11.087  -19.846 -38.567 1.00 89.98  ? 58   TYR   E CG  1 
ATOM   11913 C  CD1 . TYR   E 2 58  ? 11.529  -18.540 -38.476 1.00 85.89  ? 58   TYR   E CD1 1 
ATOM   11914 C  CD2 . TYR   E 2 58  ? 9.736   -20.061 -38.819 1.00 93.41  ? 58   TYR   E CD2 1 
ATOM   11915 C  CE1 . TYR   E 2 58  ? 10.653  -17.473 -38.630 1.00 84.73  ? 58   TYR   E CE1 1 
ATOM   11916 C  CE2 . TYR   E 2 58  ? 8.863   -19.007 -38.967 1.00 95.43  ? 58   TYR   E CE2 1 
ATOM   11917 C  CZ  . TYR   E 2 58  ? 9.326   -17.711 -38.872 1.00 89.79  ? 58   TYR   E CZ  1 
ATOM   11918 O  OH  . TYR   E 2 58  ? 8.451   -16.650 -39.022 1.00 93.68  ? 58   TYR   E OH  1 
ATOM   11919 N  N   . GLY   E 2 59  ? 15.710  -21.608 -38.408 1.00 79.87  ? 59   GLY   E N   1 
ATOM   11920 C  CA  . GLY   E 2 59  ? 16.677  -22.591 -37.969 1.00 81.82  ? 59   GLY   E CA  1 
ATOM   11921 C  C   . GLY   E 2 59  ? 18.079  -22.350 -38.477 1.00 82.37  ? 59   GLY   E C   1 
ATOM   11922 O  O   . GLY   E 2 59  ? 18.275  -21.721 -39.523 1.00 83.89  ? 59   GLY   E O   1 
ATOM   11923 N  N   . LYS   E 2 60  ? 19.067  -22.859 -37.739 1.00 84.90  ? 60   LYS   E N   1 
ATOM   11924 C  CA  . LYS   E 2 60  ? 20.471  -22.717 -38.117 1.00 83.76  ? 60   LYS   E CA  1 
ATOM   11925 C  C   . LYS   E 2 60  ? 20.786  -23.733 -39.207 1.00 82.44  ? 60   LYS   E C   1 
ATOM   11926 O  O   . LYS   E 2 60  ? 20.715  -24.942 -38.988 1.00 80.71  ? 60   LYS   E O   1 
ATOM   11927 C  CB  . LYS   E 2 60  ? 21.374  -22.878 -36.894 1.00 80.02  ? 60   LYS   E CB  1 
ATOM   11928 C  CG  . LYS   E 2 60  ? 21.108  -21.791 -35.856 1.00 75.29  ? 60   LYS   E CG  1 
ATOM   11929 C  CD  . LYS   E 2 60  ? 21.838  -21.973 -34.554 1.00 69.85  ? 60   LYS   E CD  1 
ATOM   11930 C  CE  . LYS   E 2 60  ? 23.325  -22.037 -34.753 1.00 71.31  ? 60   LYS   E CE  1 
ATOM   11931 N  NZ  . LYS   E 2 60  ? 23.921  -20.677 -34.805 1.00 76.47  ? 60   LYS   E NZ  1 
ATOM   11932 N  N   . ILE   E 2 61  ? 21.090  -23.239 -40.394 1.00 79.71  ? 61   ILE   E N   1 
ATOM   11933 C  CA  . ILE   E 2 61  ? 21.458  -24.097 -41.500 1.00 79.92  ? 61   ILE   E CA  1 
ATOM   11934 C  C   . ILE   E 2 61  ? 22.632  -24.893 -40.959 1.00 83.35  ? 61   ILE   E C   1 
ATOM   11935 O  O   . ILE   E 2 61  ? 23.651  -24.314 -40.580 1.00 88.17  ? 61   ILE   E O   1 
ATOM   11936 C  CB  . ILE   E 2 61  ? 21.723  -23.244 -42.745 1.00 83.83  ? 61   ILE   E CB  1 
ATOM   11937 C  CG1 . ILE   E 2 61  ? 20.453  -22.439 -43.064 1.00 82.39  ? 61   ILE   E CG1 1 
ATOM   11938 C  CG2 . ILE   E 2 61  ? 22.219  -24.120 -43.882 1.00 82.50  ? 61   ILE   E CG2 1 
ATOM   11939 C  CD1 . ILE   E 2 61  ? 20.542  -21.544 -44.257 1.00 80.21  ? 61   ILE   E CD1 1 
ATOM   11940 N  N   . ALA   E 2 62  ? 22.512  -26.219 -40.921 1.00 86.20  ? 62   ALA   E N   1 
ATOM   11941 C  CA  . ALA   E 2 62  ? 23.596  -27.058 -40.407 1.00 87.01  ? 62   ALA   E CA  1 
ATOM   11942 C  C   . ALA   E 2 62  ? 24.119  -27.894 -41.571 1.00 87.81  ? 62   ALA   E C   1 
ATOM   11943 O  O   . ALA   E 2 62  ? 25.299  -28.269 -41.578 1.00 87.63  ? 62   ALA   E O   1 
ATOM   11944 C  CB  . ALA   E 2 62  ? 23.190  -27.977 -39.245 1.00 83.59  ? 62   ALA   E CB  1 
ATOM   11945 N  N   . VAL   E 2 63  ? 23.266  -28.203 -42.541 1.00 82.77  ? 63   VAL   E N   1 
ATOM   11946 C  CA  . VAL   E 2 63  ? 23.670  -28.878 -43.766 1.00 85.64  ? 63   VAL   E CA  1 
ATOM   11947 C  C   . VAL   E 2 63  ? 22.958  -28.198 -44.934 1.00 87.66  ? 63   VAL   E C   1 
ATOM   11948 O  O   . VAL   E 2 63  ? 21.792  -27.805 -44.814 1.00 90.35  ? 63   VAL   E O   1 
ATOM   11949 C  CB  . VAL   E 2 63  ? 23.346  -30.391 -43.712 1.00 87.97  ? 63   VAL   E CB  1 
ATOM   11950 C  CG1 . VAL   E 2 63  ? 23.587  -31.045 -45.063 1.00 84.74  ? 63   VAL   E CG1 1 
ATOM   11951 C  CG2 . VAL   E 2 63  ? 24.168  -31.075 -42.628 1.00 84.31  ? 63   VAL   E CG2 1 
ATOM   11952 N  N   . MET   E 2 64  ? 23.656  -28.056 -46.066 1.00 82.27  ? 64   MET   E N   1 
ATOM   11953 C  CA  . MET   E 2 64  ? 23.085  -27.401 -47.241 1.00 81.59  ? 64   MET   E CA  1 
ATOM   11954 C  C   . MET   E 2 64  ? 23.680  -28.035 -48.492 1.00 87.89  ? 64   MET   E C   1 
ATOM   11955 O  O   . MET   E 2 64  ? 24.872  -27.860 -48.768 1.00 86.21  ? 64   MET   E O   1 
ATOM   11956 C  CB  . MET   E 2 64  ? 23.357  -25.898 -47.204 1.00 85.48  ? 64   MET   E CB  1 
ATOM   11957 C  CG  . MET   E 2 64  ? 22.751  -25.104 -48.367 1.00 87.35  ? 64   MET   E CG  1 
ATOM   11958 S  SD  . MET   E 2 64  ? 23.498  -23.468 -48.634 1.00 90.81  ? 64   MET   E SD  1 
ATOM   11959 C  CE  . MET   E 2 64  ? 25.245  -23.824 -48.938 1.00 81.85  ? 64   MET   E CE  1 
ATOM   11960 N  N   . GLU   E 2 65  ? 22.856  -28.745 -49.263 1.00 88.24  ? 65   GLU   E N   1 
ATOM   11961 C  CA  . GLU   E 2 65  ? 23.355  -29.475 -50.416 1.00 88.99  ? 65   GLU   E CA  1 
ATOM   11962 C  C   . GLU   E 2 65  ? 22.414  -29.360 -51.604 1.00 91.01  ? 65   GLU   E C   1 
ATOM   11963 O  O   . GLU   E 2 65  ? 21.192  -29.249 -51.455 1.00 90.24  ? 65   GLU   E O   1 
ATOM   11964 C  CB  . GLU   E 2 65  ? 23.575  -30.948 -50.075 1.00 88.73  ? 65   GLU   E CB  1 
ATOM   11965 C  CG  . GLU   E 2 65  ? 24.888  -31.188 -49.349 1.00 92.61  ? 65   GLU   E CG  1 
ATOM   11966 C  CD  . GLU   E 2 65  ? 26.067  -30.582 -50.093 1.00 101.06 ? 65   GLU   E CD  1 
ATOM   11967 O  OE1 . GLU   E 2 65  ? 26.053  -30.630 -51.352 1.00 103.21 ? 65   GLU   E OE1 1 
ATOM   11968 O  OE2 . GLU   E 2 65  ? 26.997  -30.052 -49.430 1.00 102.84 ? 65   GLU   E OE2 1 
ATOM   11969 N  N   . LEU   E 2 66  ? 23.008  -29.412 -52.791 1.00 93.91  ? 66   LEU   E N   1 
ATOM   11970 C  CA  . LEU   E 2 66  ? 22.262  -29.485 -54.040 1.00 101.39 ? 66   LEU   E CA  1 
ATOM   11971 C  C   . LEU   E 2 66  ? 22.249  -30.912 -54.606 1.00 97.83  ? 66   LEU   E C   1 
ATOM   11972 O  O   . LEU   E 2 66  ? 23.030  -31.779 -54.204 1.00 97.19  ? 66   LEU   E O   1 
ATOM   11973 C  CB  . LEU   E 2 66  ? 22.839  -28.507 -55.071 1.00 99.11  ? 66   LEU   E CB  1 
ATOM   11974 C  CG  . LEU   E 2 66  ? 22.507  -27.021 -54.856 1.00 93.86  ? 66   LEU   E CG  1 
ATOM   11975 C  CD1 . LEU   E 2 66  ? 22.914  -26.182 -56.076 1.00 94.74  ? 66   LEU   E CD1 1 
ATOM   11976 C  CD2 . LEU   E 2 66  ? 21.027  -26.828 -54.515 1.00 93.14  ? 66   LEU   E CD2 1 
ATOM   11977 N  N   . PHE   E 2 67  ? 21.330  -31.143 -55.548 1.00 99.71  ? 67   PHE   E N   1 
ATOM   11978 C  CA  . PHE   E 2 67  ? 21.167  -32.439 -56.192 1.00 103.84 ? 67   PHE   E CA  1 
ATOM   11979 C  C   . PHE   E 2 67  ? 20.104  -32.279 -57.274 1.00 105.40 ? 67   PHE   E C   1 
ATOM   11980 O  O   . PHE   E 2 67  ? 19.393  -31.267 -57.310 1.00 105.49 ? 67   PHE   E O   1 
ATOM   11981 C  CB  . PHE   E 2 67  ? 20.978  -33.542 -55.141 1.00 103.42 ? 67   PHE   E CB  1 
ATOM   11982 C  CG  . PHE   E 2 67  ? 19.666  -33.477 -54.413 1.00 102.02 ? 67   PHE   E CG  1 
ATOM   11983 C  CD1 . PHE   E 2 67  ? 19.464  -32.575 -53.382 1.00 100.80 ? 67   PHE   E CD1 1 
ATOM   11984 C  CD2 . PHE   E 2 67  ? 18.636  -34.327 -54.758 1.00 105.45 ? 67   PHE   E CD2 1 
ATOM   11985 C  CE1 . PHE   E 2 67  ? 18.249  -32.520 -52.717 1.00 99.88  ? 67   PHE   E CE1 1 
ATOM   11986 C  CE2 . PHE   E 2 67  ? 17.426  -34.275 -54.098 1.00 104.15 ? 67   PHE   E CE2 1 
ATOM   11987 C  CZ  . PHE   E 2 67  ? 17.232  -33.374 -53.082 1.00 99.79  ? 67   PHE   E CZ  1 
ATOM   11988 N  N   . ARG   E 2 68  ? 20.014  -33.254 -58.176 1.00 110.40 ? 68   ARG   E N   1 
ATOM   11989 C  CA  . ARG   E 2 68  ? 18.980  -33.291 -59.216 1.00 119.09 ? 68   ARG   E CA  1 
ATOM   11990 C  C   . ARG   E 2 68  ? 18.557  -34.751 -59.245 1.00 118.10 ? 68   ARG   E C   1 
ATOM   11991 O  O   . ARG   E 2 68  ? 19.236  -35.578 -59.878 1.00 118.00 ? 68   ARG   E O   1 
ATOM   11992 C  CB  . ARG   E 2 68  ? 19.392  -32.829 -60.619 1.00 115.60 ? 68   ARG   E CB  1 
ATOM   11993 N  N   . PRO   E 2 69  ? 17.462  -35.128 -58.581 1.00 118.53 ? 69   PRO   E N   1 
ATOM   11994 C  CA  . PRO   E 2 69  ? 17.008  -36.516 -58.666 1.00 124.54 ? 69   PRO   E CA  1 
ATOM   11995 C  C   . PRO   E 2 69  ? 16.717  -36.827 -60.125 1.00 132.61 ? 69   PRO   E C   1 
ATOM   11996 O  O   . PRO   E 2 69  ? 16.439  -35.927 -60.923 1.00 136.52 ? 69   PRO   E O   1 
ATOM   11997 C  CB  . PRO   E 2 69  ? 15.780  -36.552 -57.745 1.00 120.15 ? 69   PRO   E CB  1 
ATOM   11998 C  CG  . PRO   E 2 69  ? 15.795  -35.280 -56.998 1.00 118.04 ? 69   PRO   E CG  1 
ATOM   11999 C  CD  . PRO   E 2 69  ? 16.482  -34.292 -57.877 1.00 121.21 ? 69   PRO   E CD  1 
ATOM   12000 N  N   . LYS   E 2 70  ? 16.813  -38.110 -60.482 1.00 138.06 ? 70   LYS   E N   1 
ATOM   12001 C  CA  . LYS   E 2 70  ? 16.533  -38.515 -61.855 1.00 140.54 ? 70   LYS   E CA  1 
ATOM   12002 C  C   . LYS   E 2 70  ? 15.107  -37.983 -61.970 1.00 140.40 ? 70   LYS   E C   1 
ATOM   12003 O  O   . LYS   E 2 70  ? 14.272  -38.228 -61.096 1.00 138.34 ? 70   LYS   E O   1 
ATOM   12004 C  CB  . LYS   E 2 70  ? 16.792  -40.014 -62.048 1.00 139.35 ? 70   LYS   E CB  1 
ATOM   12005 N  N   . GLY   E 2 71  ? 14.828  -37.230 -63.030 1.00 137.09 ? 71   GLY   E N   1 
ATOM   12006 C  CA  . GLY   E 2 71  ? 13.508  -36.671 -63.208 1.00 132.62 ? 71   GLY   E CA  1 
ATOM   12007 C  C   . GLY   E 2 71  ? 13.204  -35.236 -62.839 1.00 134.06 ? 71   GLY   E C   1 
ATOM   12008 O  O   . GLY   E 2 71  ? 12.035  -34.872 -62.679 1.00 133.84 ? 71   GLY   E O   1 
ATOM   12009 N  N   . GLU   E 2 72  ? 14.242  -34.415 -62.698 1.00 129.92 ? 72   GLU   E N   1 
ATOM   12010 C  CA  . GLU   E 2 72  ? 14.098  -32.982 -62.480 1.00 128.58 ? 72   GLU   E CA  1 
ATOM   12011 C  C   . GLU   E 2 72  ? 14.914  -32.235 -63.526 1.00 128.33 ? 72   GLU   E C   1 
ATOM   12012 O  O   . GLU   E 2 72  ? 15.974  -32.704 -63.952 1.00 130.50 ? 72   GLU   E O   1 
ATOM   12013 C  CB  . GLU   E 2 72  ? 14.577  -32.556 -61.076 1.00 130.82 ? 72   GLU   E CB  1 
ATOM   12014 C  CG  . GLU   E 2 72  ? 14.207  -33.497 -59.937 1.00 132.33 ? 72   GLU   E CG  1 
ATOM   12015 C  CD  . GLU   E 2 72  ? 12.706  -33.617 -59.719 1.00 137.24 ? 72   GLU   E CD  1 
ATOM   12016 O  OE1 . GLU   E 2 72  ? 12.094  -32.700 -59.108 1.00 134.11 ? 72   GLU   E OE1 1 
ATOM   12017 O  OE2 . GLU   E 2 72  ? 12.142  -34.645 -60.162 1.00 141.54 ? 72   GLU   E OE2 1 
ATOM   12018 N  N   . SER   E 2 73  ? 14.413  -31.066 -63.940 1.00 117.76 ? 73   SER   E N   1 
ATOM   12019 C  CA  . SER   E 2 73  ? 15.193  -30.195 -64.819 1.00 115.65 ? 73   SER   E CA  1 
ATOM   12020 C  C   . SER   E 2 73  ? 16.203  -29.365 -64.030 1.00 120.34 ? 73   SER   E C   1 
ATOM   12021 O  O   . SER   E 2 73  ? 17.374  -29.252 -64.418 1.00 119.99 ? 73   SER   E O   1 
ATOM   12022 C  CB  . SER   E 2 73  ? 14.265  -29.285 -65.621 1.00 112.31 ? 73   SER   E CB  1 
ATOM   12023 O  OG  . SER   E 2 73  ? 13.465  -28.466 -64.779 1.00 113.90 ? 73   SER   E OG  1 
ATOM   12024 N  N   . LYS   E 2 74  ? 15.771  -28.783 -62.920 1.00 121.71 ? 74   LYS   E N   1 
ATOM   12025 C  CA  . LYS   E 2 74  ? 16.646  -27.987 -62.084 1.00 111.69 ? 74   LYS   E CA  1 
ATOM   12026 C  C   . LYS   E 2 74  ? 17.105  -28.810 -60.893 1.00 113.17 ? 74   LYS   E C   1 
ATOM   12027 O  O   . LYS   E 2 74  ? 16.439  -29.761 -60.479 1.00 114.86 ? 74   LYS   E O   1 
ATOM   12028 C  CB  . LYS   E 2 74  ? 15.940  -26.729 -61.598 1.00 108.22 ? 74   LYS   E CB  1 
ATOM   12029 C  CG  . LYS   E 2 74  ? 15.416  -25.852 -62.693 1.00 109.98 ? 74   LYS   E CG  1 
ATOM   12030 C  CD  . LYS   E 2 74  ? 14.420  -24.873 -62.101 1.00 113.50 ? 74   LYS   E CD  1 
ATOM   12031 C  CE  . LYS   E 2 74  ? 13.569  -25.544 -61.024 1.00 114.60 ? 74   LYS   E CE  1 
ATOM   12032 N  NZ  . LYS   E 2 74  ? 12.267  -24.861 -60.772 1.00 110.56 ? 74   LYS   E NZ  1 
ATOM   12033 N  N   . ASP   E 2 75  ? 18.260  -28.438 -60.352 1.00 113.18 ? 75   ASP   E N   1 
ATOM   12034 C  CA  . ASP   E 2 75  ? 18.704  -28.974 -59.075 1.00 109.06 ? 75   ASP   E CA  1 
ATOM   12035 C  C   . ASP   E 2 75  ? 17.704  -28.636 -57.972 1.00 106.64 ? 75   ASP   E C   1 
ATOM   12036 O  O   . ASP   E 2 75  ? 16.974  -27.635 -58.033 1.00 105.91 ? 75   ASP   E O   1 
ATOM   12037 C  CB  . ASP   E 2 75  ? 20.077  -28.412 -58.705 1.00 102.74 ? 75   ASP   E CB  1 
ATOM   12038 C  CG  . ASP   E 2 75  ? 21.193  -28.949 -59.582 1.00 106.12 ? 75   ASP   E CG  1 
ATOM   12039 O  OD1 . ASP   E 2 75  ? 21.047  -30.074 -60.117 1.00 110.33 ? 75   ASP   E OD1 1 
ATOM   12040 O  OD2 . ASP   E 2 75  ? 22.223  -28.249 -59.709 1.00 105.09 ? 75   ASP   E OD2 1 
ATOM   12041 N  N   . LEU   E 2 76  ? 17.697  -29.479 -56.941 1.00 104.00 ? 76   LEU   E N   1 
ATOM   12042 C  CA  . LEU   E 2 76  ? 16.934  -29.255 -55.723 1.00 102.06 ? 76   LEU   E CA  1 
ATOM   12043 C  C   . LEU   E 2 76  ? 17.874  -29.037 -54.546 1.00 100.92 ? 76   LEU   E C   1 
ATOM   12044 O  O   . LEU   E 2 76  ? 19.012  -29.510 -54.542 1.00 101.18 ? 76   LEU   E O   1 
ATOM   12045 C  CB  . LEU   E 2 76  ? 16.015  -30.431 -55.432 1.00 105.07 ? 76   LEU   E CB  1 
ATOM   12046 C  CG  . LEU   E 2 76  ? 14.921  -30.481 -56.470 1.00 107.37 ? 76   LEU   E CG  1 
ATOM   12047 C  CD1 . LEU   E 2 76  ? 13.706  -31.069 -55.826 1.00 113.15 ? 76   LEU   E CD1 1 
ATOM   12048 C  CD2 . LEU   E 2 76  ? 14.647  -29.070 -56.993 1.00 107.50 ? 76   LEU   E CD2 1 
ATOM   12049 N  N   . LEU   E 2 77  ? 17.372  -28.338 -53.528 1.00 101.22 ? 77   LEU   E N   1 
ATOM   12050 C  CA  . LEU   E 2 77  ? 18.159  -27.952 -52.365 1.00 97.28  ? 77   LEU   E CA  1 
ATOM   12051 C  C   . LEU   E 2 77  ? 17.750  -28.789 -51.168 1.00 95.26  ? 77   LEU   E C   1 
ATOM   12052 O  O   . LEU   E 2 77  ? 16.559  -28.860 -50.836 1.00 95.25  ? 77   LEU   E O   1 
ATOM   12053 C  CB  . LEU   E 2 77  ? 17.959  -26.477 -52.032 1.00 94.83  ? 77   LEU   E CB  1 
ATOM   12054 C  CG  . LEU   E 2 77  ? 18.925  -25.970 -50.980 1.00 85.30  ? 77   LEU   E CG  1 
ATOM   12055 C  CD1 . LEU   E 2 77  ? 20.315  -26.380 -51.363 1.00 91.17  ? 77   LEU   E CD1 1 
ATOM   12056 C  CD2 . LEU   E 2 77  ? 18.845  -24.495 -50.927 1.00 83.80  ? 77   LEU   E CD2 1 
ATOM   12057 N  N   . PHE   E 2 78  ? 18.734  -29.408 -50.516 1.00 93.78  ? 78   PHE   E N   1 
ATOM   12058 C  CA  . PHE   E 2 78  ? 18.501  -30.053 -49.232 1.00 93.78  ? 78   PHE   E CA  1 
ATOM   12059 C  C   . PHE   E 2 78  ? 19.111  -29.239 -48.103 1.00 89.70  ? 78   PHE   E C   1 
ATOM   12060 O  O   . PHE   E 2 78  ? 20.252  -28.768 -48.189 1.00 85.66  ? 78   PHE   E O   1 
ATOM   12061 C  CB  . PHE   E 2 78  ? 19.054  -31.472 -49.154 1.00 89.65  ? 78   PHE   E CB  1 
ATOM   12062 C  CG  . PHE   E 2 78  ? 18.832  -32.107 -47.806 1.00 85.38  ? 78   PHE   E CG  1 
ATOM   12063 C  CD1 . PHE   E 2 78  ? 17.594  -32.624 -47.461 1.00 87.26  ? 78   PHE   E CD1 1 
ATOM   12064 C  CD2 . PHE   E 2 78  ? 19.836  -32.139 -46.870 1.00 82.65  ? 78   PHE   E CD2 1 
ATOM   12065 C  CE1 . PHE   E 2 78  ? 17.378  -33.188 -46.227 1.00 86.24  ? 78   PHE   E CE1 1 
ATOM   12066 C  CE2 . PHE   E 2 78  ? 19.620  -32.704 -45.633 1.00 84.65  ? 78   PHE   E CE2 1 
ATOM   12067 C  CZ  . PHE   E 2 78  ? 18.393  -33.229 -45.311 1.00 82.04  ? 78   PHE   E CZ  1 
ATOM   12068 N  N   . ILE   E 2 79  ? 18.343  -29.103 -47.033 1.00 85.68  ? 79   ILE   E N   1 
ATOM   12069 C  CA  . ILE   E 2 79  ? 18.767  -28.354 -45.870 1.00 85.65  ? 79   ILE   E CA  1 
ATOM   12070 C  C   . ILE   E 2 79  ? 18.389  -29.163 -44.651 1.00 88.87  ? 79   ILE   E C   1 
ATOM   12071 O  O   . ILE   E 2 79  ? 17.259  -29.657 -44.550 1.00 85.11  ? 79   ILE   E O   1 
ATOM   12072 C  CB  . ILE   E 2 79  ? 18.124  -26.958 -45.813 1.00 88.30  ? 79   ILE   E CB  1 
ATOM   12073 C  CG1 . ILE   E 2 79  ? 19.000  -25.960 -46.560 1.00 87.56  ? 79   ILE   E CG1 1 
ATOM   12074 C  CG2 . ILE   E 2 79  ? 17.895  -26.538 -44.376 1.00 86.72  ? 79   ILE   E CG2 1 
ATOM   12075 C  CD1 . ILE   E 2 79  ? 18.270  -24.687 -46.951 1.00 91.58  ? 79   ILE   E CD1 1 
ATOM   12076 N  N   . LEU   E 2 80  ? 19.349  -29.324 -43.748 1.00 88.55  ? 80   LEU   E N   1 
ATOM   12077 C  CA  . LEU   E 2 80  ? 19.100  -29.777 -42.395 1.00 84.16  ? 80   LEU   E CA  1 
ATOM   12078 C  C   . LEU   E 2 80  ? 19.524  -28.666 -41.454 1.00 87.98  ? 80   LEU   E C   1 
ATOM   12079 O  O   . LEU   E 2 80  ? 20.620  -28.112 -41.602 1.00 86.34  ? 80   LEU   E O   1 
ATOM   12080 C  CB  . LEU   E 2 80  ? 19.875  -31.048 -42.091 1.00 83.88  ? 80   LEU   E CB  1 
ATOM   12081 C  CG  . LEU   E 2 80  ? 19.581  -31.539 -40.690 1.00 85.07  ? 80   LEU   E CG  1 
ATOM   12082 C  CD1 . LEU   E 2 80  ? 18.098  -31.824 -40.522 1.00 85.40  ? 80   LEU   E CD1 1 
ATOM   12083 C  CD2 . LEU   E 2 80  ? 20.381  -32.778 -40.476 1.00 88.36  ? 80   LEU   E CD2 1 
ATOM   12084 N  N   . THR   E 2 81  ? 18.649  -28.319 -40.513 1.00 90.16  ? 81   THR   E N   1 
ATOM   12085 C  CA  . THR   E 2 81  ? 18.937  -27.300 -39.510 1.00 86.22  ? 81   THR   E CA  1 
ATOM   12086 C  C   . THR   E 2 81  ? 19.376  -27.953 -38.205 1.00 84.58  ? 81   THR   E C   1 
ATOM   12087 O  O   . THR   E 2 81  ? 18.965  -29.067 -37.880 1.00 83.17  ? 81   THR   E O   1 
ATOM   12088 C  CB  . THR   E 2 81  ? 17.719  -26.401 -39.232 1.00 84.80  ? 81   THR   E CB  1 
ATOM   12089 O  OG1 . THR   E 2 81  ? 16.658  -27.175 -38.659 1.00 88.42  ? 81   THR   E OG1 1 
ATOM   12090 C  CG2 . THR   E 2 81  ? 17.221  -25.724 -40.488 1.00 83.90  ? 81   THR   E CG2 1 
ATOM   12091 N  N   . ALA   E 2 82  ? 20.185  -27.207 -37.441 1.00 86.22  ? 82   ALA   E N   1 
ATOM   12092 C  CA  . ALA   E 2 82  ? 20.677  -27.655 -36.140 1.00 81.79  ? 82   ALA   E CA  1 
ATOM   12093 C  C   . ALA   E 2 82  ? 19.592  -28.255 -35.258 1.00 83.22  ? 82   ALA   E C   1 
ATOM   12094 O  O   . ALA   E 2 82  ? 19.885  -29.127 -34.436 1.00 84.91  ? 82   ALA   E O   1 
ATOM   12095 C  CB  . ALA   E 2 82  ? 21.338  -26.490 -35.395 1.00 84.44  ? 82   ALA   E CB  1 
ATOM   12096 N  N   . LYS   E 2 83  ? 18.354  -27.774 -35.353 1.00 86.80  ? 83   LYS   E N   1 
ATOM   12097 C  CA  . LYS   E 2 83  ? 17.296  -28.373 -34.549 1.00 84.53  ? 83   LYS   E CA  1 
ATOM   12098 C  C   . LYS   E 2 83  ? 16.731  -29.613 -35.193 1.00 89.69  ? 83   LYS   E C   1 
ATOM   12099 O  O   . LYS   E 2 83  ? 15.690  -30.105 -34.742 1.00 91.23  ? 83   LYS   E O   1 
ATOM   12100 C  CB  . LYS   E 2 83  ? 16.180  -27.367 -34.283 1.00 84.10  ? 83   LYS   E CB  1 
ATOM   12101 C  CG  . LYS   E 2 83  ? 16.502  -26.422 -33.134 1.00 86.29  ? 83   LYS   E CG  1 
ATOM   12102 C  CD  . LYS   E 2 83  ? 15.273  -25.647 -32.703 1.00 86.37  ? 83   LYS   E CD  1 
ATOM   12103 C  CE  . LYS   E 2 83  ? 15.609  -24.706 -31.567 1.00 86.62  ? 83   LYS   E CE  1 
ATOM   12104 N  NZ  . LYS   E 2 83  ? 14.406  -24.318 -30.769 1.00 89.98  ? 83   LYS   E NZ  1 
ATOM   12105 N  N   . TYR   E 2 84  ? 17.410  -30.104 -36.238 1.00 91.58  ? 84   TYR   E N   1 
ATOM   12106 C  CA  . TYR   E 2 84  ? 17.114  -31.336 -36.971 1.00 94.25  ? 84   TYR   E CA  1 
ATOM   12107 C  C   . TYR   E 2 84  ? 15.952  -31.160 -37.940 1.00 93.66  ? 84   TYR   E C   1 
ATOM   12108 O  O   . TYR   E 2 84  ? 15.346  -32.153 -38.380 1.00 92.16  ? 84   TYR   E O   1 
ATOM   12109 C  CB  . TYR   E 2 84  ? 16.900  -32.521 -36.011 1.00 93.34  ? 84   TYR   E CB  1 
ATOM   12110 C  CG  . TYR   E 2 84  ? 18.196  -32.821 -35.274 1.00 90.42  ? 84   TYR   E CG  1 
ATOM   12111 C  CD1 . TYR   E 2 84  ? 19.365  -33.027 -35.983 1.00 89.20  ? 84   TYR   E CD1 1 
ATOM   12112 C  CD2 . TYR   E 2 84  ? 18.273  -32.817 -33.886 1.00 92.48  ? 84   TYR   E CD2 1 
ATOM   12113 C  CE1 . TYR   E 2 84  ? 20.566  -33.270 -35.345 1.00 89.36  ? 84   TYR   E CE1 1 
ATOM   12114 C  CE2 . TYR   E 2 84  ? 19.488  -33.060 -33.231 1.00 90.37  ? 84   TYR   E CE2 1 
ATOM   12115 C  CZ  . TYR   E 2 84  ? 20.637  -33.288 -33.973 1.00 87.65  ? 84   TYR   E CZ  1 
ATOM   12116 O  OH  . TYR   E 2 84  ? 21.866  -33.529 -33.372 1.00 86.80  ? 84   TYR   E OH  1 
ATOM   12117 N  N   . ASN   E 2 85  ? 15.641  -29.911 -38.310 1.00 90.98  ? 85   ASN   E N   1 
ATOM   12118 C  CA  . ASN   E 2 85  ? 14.642  -29.663 -39.347 1.00 92.72  ? 85   ASN   E CA  1 
ATOM   12119 C  C   . ASN   E 2 85  ? 15.246  -29.974 -40.712 1.00 90.26  ? 85   ASN   E C   1 
ATOM   12120 O  O   . ASN   E 2 85  ? 16.266  -29.391 -41.097 1.00 89.12  ? 85   ASN   E O   1 
ATOM   12121 C  CB  . ASN   E 2 85  ? 14.154  -28.214 -39.285 1.00 89.14  ? 85   ASN   E CB  1 
ATOM   12122 C  CG  . ASN   E 2 85  ? 13.783  -27.778 -37.874 1.00 89.65  ? 85   ASN   E CG  1 
ATOM   12123 O  OD1 . ASN   E 2 85  ? 14.063  -26.642 -37.454 1.00 89.26  ? 85   ASN   E OD1 1 
ATOM   12124 N  ND2 . ASN   E 2 85  ? 13.149  -28.685 -37.131 1.00 89.63  ? 85   ASN   E ND2 1 
ATOM   12125 N  N   . ALA   E 2 86  ? 14.638  -30.913 -41.430 1.00 93.16  ? 86   ALA   E N   1 
ATOM   12126 C  CA  . ALA   E 2 86  ? 15.132  -31.331 -42.729 1.00 89.28  ? 86   ALA   E CA  1 
ATOM   12127 C  C   . ALA   E 2 86  ? 14.101  -30.967 -43.777 1.00 88.97  ? 86   ALA   E C   1 
ATOM   12128 O  O   . ALA   E 2 86  ? 12.904  -31.112 -43.550 1.00 93.63  ? 86   ALA   E O   1 
ATOM   12129 C  CB  . ALA   E 2 86  ? 15.407  -32.830 -42.769 1.00 94.93  ? 86   ALA   E CB  1 
ATOM   12130 N  N   . CYS   E 2 87  ? 14.566  -30.492 -44.924 1.00 92.35  ? 87   CYS   E N   1 
ATOM   12131 C  CA  . CYS   E 2 87  ? 13.637  -30.143 -45.990 1.00 97.69  ? 87   CYS   E CA  1 
ATOM   12132 C  C   . CYS   E 2 87  ? 14.339  -30.218 -47.339 1.00 93.30  ? 87   CYS   E C   1 
ATOM   12133 O  O   . CYS   E 2 87  ? 15.569  -30.150 -47.431 1.00 92.00  ? 87   CYS   E O   1 
ATOM   12134 C  CB  . CYS   E 2 87  ? 13.059  -28.739 -45.786 1.00 93.78  ? 87   CYS   E CB  1 
ATOM   12135 S  SG  . CYS   E 2 87  ? 14.396  -27.526 -45.645 1.00 97.82  ? 87   CYS   E SG  1 
ATOM   12136 N  N   . ILE   E 2 88  ? 13.531  -30.331 -48.384 1.00 96.57  ? 88   ILE   E N   1 
ATOM   12137 C  CA  . ILE   E 2 88  ? 13.986  -30.183 -49.753 1.00 99.02  ? 88   ILE   E CA  1 
ATOM   12138 C  C   . ILE   E 2 88  ? 13.215  -29.036 -50.370 1.00 96.83  ? 88   ILE   E C   1 
ATOM   12139 O  O   . ILE   E 2 88  ? 11.990  -28.957 -50.222 1.00 95.03  ? 88   ILE   E O   1 
ATOM   12140 C  CB  . ILE   E 2 88  ? 13.775  -31.467 -50.575 1.00 97.60  ? 88   ILE   E CB  1 
ATOM   12141 C  CG1 . ILE   E 2 88  ? 14.914  -32.440 -50.336 1.00 94.71  ? 88   ILE   E CG1 1 
ATOM   12142 C  CG2 . ILE   E 2 88  ? 13.657  -31.116 -52.033 1.00 99.81  ? 88   ILE   E CG2 1 
ATOM   12143 C  CD1 . ILE   E 2 88  ? 14.475  -33.844 -50.533 1.00 93.45  ? 88   ILE   E CD1 1 
ATOM   12144 N  N   . LEU   E 2 89  ? 13.929  -28.162 -51.074 1.00 94.62  ? 89   LEU   E N   1 
ATOM   12145 C  CA  . LEU   E 2 89  ? 13.359  -26.936 -51.605 1.00 100.62 ? 89   LEU   E CA  1 
ATOM   12146 C  C   . LEU   E 2 89  ? 13.620  -26.856 -53.108 1.00 102.05 ? 89   LEU   E C   1 
ATOM   12147 O  O   . LEU   E 2 89  ? 14.626  -27.381 -53.597 1.00 101.91 ? 89   LEU   E O   1 
ATOM   12148 C  CB  . LEU   E 2 89  ? 13.957  -25.741 -50.862 1.00 98.33  ? 89   LEU   E CB  1 
ATOM   12149 C  CG  . LEU   E 2 89  ? 14.002  -25.857 -49.335 1.00 98.64  ? 89   LEU   E CG  1 
ATOM   12150 C  CD1 . LEU   E 2 89  ? 14.887  -24.743 -48.798 1.00 99.85  ? 89   LEU   E CD1 1 
ATOM   12151 C  CD2 . LEU   E 2 89  ? 12.596  -25.785 -48.725 1.00 96.80  ? 89   LEU   E CD2 1 
ATOM   12152 N  N   . GLU   E 2 90  ? 12.698  -26.208 -53.842 1.00 105.58 ? 90   GLU   E N   1 
ATOM   12153 C  CA  . GLU   E 2 90  ? 12.887  -25.884 -55.259 1.00 115.52 ? 90   GLU   E CA  1 
ATOM   12154 C  C   . GLU   E 2 90  ? 12.586  -24.409 -55.522 1.00 117.25 ? 90   GLU   E C   1 
ATOM   12155 O  O   . GLU   E 2 90  ? 11.913  -23.737 -54.736 1.00 111.59 ? 90   GLU   E O   1 
ATOM   12156 C  CB  . GLU   E 2 90  ? 12.006  -26.741 -56.200 1.00 115.75 ? 90   GLU   E CB  1 
ATOM   12157 N  N   . TYR   E 2 91  ? 13.086  -23.919 -56.659 1.00 130.45 ? 91   TYR   E N   1 
ATOM   12158 C  CA  . TYR   E 2 91  ? 12.908  -22.532 -57.081 1.00 132.15 ? 91   TYR   E CA  1 
ATOM   12159 C  C   . TYR   E 2 91  ? 11.690  -22.431 -57.999 1.00 135.69 ? 91   TYR   E C   1 
ATOM   12160 O  O   . TYR   E 2 91  ? 11.593  -23.159 -58.992 1.00 135.87 ? 91   TYR   E O   1 
ATOM   12161 C  CB  . TYR   E 2 91  ? 14.179  -22.036 -57.776 1.00 131.33 ? 91   TYR   E CB  1 
ATOM   12162 C  CG  . TYR   E 2 91  ? 14.257  -20.544 -58.068 1.00 133.66 ? 91   TYR   E CG  1 
ATOM   12163 C  CD1 . TYR   E 2 91  ? 13.245  -19.679 -57.679 1.00 136.30 ? 91   TYR   E CD1 1 
ATOM   12164 C  CD2 . TYR   E 2 91  ? 15.370  -20.006 -58.714 1.00 138.74 ? 91   TYR   E CD2 1 
ATOM   12165 C  CE1 . TYR   E 2 91  ? 13.317  -18.316 -57.941 1.00 140.23 ? 91   TYR   E CE1 1 
ATOM   12166 C  CE2 . TYR   E 2 91  ? 15.456  -18.657 -58.987 1.00 142.80 ? 91   TYR   E CE2 1 
ATOM   12167 C  CZ  . TYR   E 2 91  ? 14.430  -17.808 -58.599 1.00 141.81 ? 91   TYR   E CZ  1 
ATOM   12168 O  OH  . TYR   E 2 91  ? 14.526  -16.453 -58.868 1.00 140.45 ? 91   TYR   E OH  1 
ATOM   12169 N  N   . LYS   E 2 92  ? 10.742  -21.560 -57.639 1.00 130.45 ? 92   LYS   E N   1 
ATOM   12170 C  CA  . LYS   E 2 92  ? 9.513   -21.353 -58.413 1.00 134.96 ? 92   LYS   E CA  1 
ATOM   12171 C  C   . LYS   E 2 92  ? 9.321   -19.853 -58.624 1.00 138.50 ? 92   LYS   E C   1 
ATOM   12172 O  O   . LYS   E 2 92  ? 8.847   -19.143 -57.730 1.00 131.80 ? 92   LYS   E O   1 
ATOM   12173 C  CB  . LYS   E 2 92  ? 8.296   -21.980 -57.719 1.00 129.01 ? 92   LYS   E CB  1 
ATOM   12174 N  N   . GLN   E 2 93  ? 9.679   -19.380 -59.815 1.00 149.06 ? 93   GLN   E N   1 
ATOM   12175 C  CA  . GLN   E 2 93  ? 9.535   -17.985 -60.201 1.00 151.13 ? 93   GLN   E CA  1 
ATOM   12176 C  C   . GLN   E 2 93  ? 8.259   -17.911 -61.039 1.00 155.51 ? 93   GLN   E C   1 
ATOM   12177 O  O   . GLN   E 2 93  ? 8.163   -18.545 -62.091 1.00 156.85 ? 93   GLN   E O   1 
ATOM   12178 C  CB  . GLN   E 2 93  ? 10.774  -17.504 -60.964 1.00 149.66 ? 93   GLN   E CB  1 
ATOM   12179 C  CG  . GLN   E 2 93  ? 10.869  -16.009 -61.153 1.00 149.42 ? 93   GLN   E CG  1 
ATOM   12180 C  CD  . GLN   E 2 93  ? 10.182  -15.482 -62.420 1.00 161.77 ? 93   GLN   E CD  1 
ATOM   12181 O  OE1 . GLN   E 2 93  ? 9.197   -16.078 -62.897 1.00 167.34 ? 93   GLN   E OE1 1 
ATOM   12182 N  NE2 . GLN   E 2 93  ? 10.681  -14.366 -62.964 1.00 164.63 ? 93   GLN   E NE2 1 
ATOM   12183 N  N   . SER   E 2 94  ? 7.284   -17.141 -60.569 1.00 156.32 ? 94   SER   E N   1 
ATOM   12184 C  CA  . SER   E 2 94  ? 6.058   -16.879 -61.313 1.00 152.51 ? 94   SER   E CA  1 
ATOM   12185 C  C   . SER   E 2 94  ? 5.997   -15.392 -61.643 1.00 161.76 ? 94   SER   E C   1 
ATOM   12186 O  O   . SER   E 2 94  ? 5.215   -14.636 -61.067 1.00 158.67 ? 94   SER   E O   1 
ATOM   12187 C  CB  . SER   E 2 94  ? 4.839   -17.321 -60.507 1.00 147.81 ? 94   SER   E CB  1 
ATOM   12188 O  OG  . SER   E 2 94  ? 3.657   -16.746 -61.030 1.00 142.95 ? 94   SER   E OG  1 
ATOM   12189 N  N   . GLY   E 2 95  ? 6.840   -14.974 -62.594 1.00 162.15 ? 95   GLY   E N   1 
ATOM   12190 C  CA  . GLY   E 2 95  ? 6.925   -13.564 -62.952 1.00 160.14 ? 95   GLY   E CA  1 
ATOM   12191 C  C   . GLY   E 2 95  ? 7.863   -12.789 -62.033 1.00 158.79 ? 95   GLY   E C   1 
ATOM   12192 O  O   . GLY   E 2 95  ? 8.851   -13.321 -61.533 1.00 158.97 ? 95   GLY   E O   1 
ATOM   12193 N  N   . GLU   E 2 96  ? 7.550   -11.506 -61.815 1.00 155.36 ? 96   GLU   E N   1 
ATOM   12194 C  CA  . GLU   E 2 96  ? 8.311   -10.722 -60.845 1.00 151.42 ? 96   GLU   E CA  1 
ATOM   12195 C  C   . GLU   E 2 96  ? 8.370   -11.421 -59.486 1.00 153.54 ? 96   GLU   E C   1 
ATOM   12196 O  O   . GLU   E 2 96  ? 9.329   -11.231 -58.729 1.00 148.19 ? 96   GLU   E O   1 
ATOM   12197 C  CB  . GLU   E 2 96  ? 7.695   -9.326  -60.700 1.00 141.66 ? 96   GLU   E CB  1 
ATOM   12198 N  N   . SER   E 2 97  ? 7.362   -12.239 -59.173 1.00 169.33 ? 97   SER   E N   1 
ATOM   12199 C  CA  . SER   E 2 97  ? 7.282   -12.923 -57.886 1.00 167.02 ? 97   SER   E CA  1 
ATOM   12200 C  C   . SER   E 2 97  ? 8.191   -14.155 -57.851 1.00 164.21 ? 97   SER   E C   1 
ATOM   12201 O  O   . SER   E 2 97  ? 8.162   -14.991 -58.764 1.00 162.78 ? 97   SER   E O   1 
ATOM   12202 C  CB  . SER   E 2 97  ? 5.840   -13.344 -57.594 1.00 168.26 ? 97   SER   E CB  1 
ATOM   12203 O  OG  . SER   E 2 97  ? 5.794   -14.568 -56.873 1.00 166.54 ? 97   SER   E OG  1 
ATOM   12204 N  N   . ILE   E 2 98  ? 8.980   -14.273 -56.784 1.00 142.57 ? 98   ILE   E N   1 
ATOM   12205 C  CA  . ILE   E 2 98  ? 9.821   -15.436 -56.537 1.00 132.91 ? 98   ILE   E CA  1 
ATOM   12206 C  C   . ILE   E 2 98  ? 9.396   -16.046 -55.213 1.00 126.35 ? 98   ILE   E C   1 
ATOM   12207 O  O   . ILE   E 2 98  ? 9.025   -15.328 -54.278 1.00 129.18 ? 98   ILE   E O   1 
ATOM   12208 C  CB  . ILE   E 2 98  ? 11.318  -15.072 -56.523 1.00 124.95 ? 98   ILE   E CB  1 
ATOM   12209 C  CG1 . ILE   E 2 98  ? 11.530  -13.707 -55.879 1.00 125.66 ? 98   ILE   E CG1 1 
ATOM   12210 C  CG2 . ILE   E 2 98  ? 11.853  -14.991 -57.906 1.00 128.53 ? 98   ILE   E CG2 1 
ATOM   12211 C  CD1 . ILE   E 2 98  ? 11.283  -13.678 -54.379 1.00 125.95 ? 98   ILE   E CD1 1 
ATOM   12212 N  N   . ASP   E 2 99  ? 9.431   -17.368 -55.131 1.00 121.81 ? 99   ASP   E N   1 
ATOM   12213 C  CA  . ASP   E 2 99  ? 9.087   -18.015 -53.871 1.00 115.52 ? 99   ASP   E CA  1 
ATOM   12214 C  C   . ASP   E 2 99  ? 9.687   -19.417 -53.857 1.00 114.87 ? 99   ASP   E C   1 
ATOM   12215 O  O   . ASP   E 2 99  ? 9.632   -20.131 -54.865 1.00 114.98 ? 99   ASP   E O   1 
ATOM   12216 C  CB  . ASP   E 2 99  ? 7.568   -18.050 -53.664 1.00 107.26 ? 99   ASP   E CB  1 
ATOM   12217 N  N   . ILE   E 2 100 ? 10.279  -19.788 -52.727 1.00 111.58 ? 100  ILE   E N   1 
ATOM   12218 C  CA  . ILE   E 2 100 ? 10.943  -21.075 -52.579 1.00 106.87 ? 100  ILE   E CA  1 
ATOM   12219 C  C   . ILE   E 2 100 ? 9.959   -22.050 -51.953 1.00 106.48 ? 100  ILE   E C   1 
ATOM   12220 O  O   . ILE   E 2 100 ? 9.593   -21.919 -50.787 1.00 107.08 ? 100  ILE   E O   1 
ATOM   12221 C  CB  . ILE   E 2 100 ? 12.200  -20.968 -51.708 1.00 102.62 ? 100  ILE   E CB  1 
ATOM   12222 C  CG1 . ILE   E 2 100 ? 13.362  -20.329 -52.470 1.00 102.17 ? 100  ILE   E CG1 1 
ATOM   12223 C  CG2 . ILE   E 2 100 ? 12.583  -22.351 -51.255 1.00 106.37 ? 100  ILE   E CG2 1 
ATOM   12224 C  CD1 . ILE   E 2 100 ? 14.150  -21.310 -53.319 1.00 110.31 ? 100  ILE   E CD1 1 
ATOM   12225 N  N   . ILE   E 2 101 ? 9.588   -23.070 -52.702 1.00 106.24 ? 101  ILE   E N   1 
ATOM   12226 C  CA  . ILE   E 2 101 ? 8.595   -24.043 -52.267 1.00 106.25 ? 101  ILE   E CA  1 
ATOM   12227 C  C   . ILE   E 2 101 ? 9.284   -25.208 -51.567 1.00 105.53 ? 101  ILE   E C   1 
ATOM   12228 O  O   . ILE   E 2 101 ? 10.412  -25.585 -51.897 1.00 103.69 ? 101  ILE   E O   1 
ATOM   12229 C  CB  . ILE   E 2 101 ? 7.736   -24.502 -53.460 1.00 113.53 ? 101  ILE   E CB  1 
ATOM   12230 C  CG1 . ILE   E 2 101 ? 8.600   -24.784 -54.708 1.00 114.55 ? 101  ILE   E CG1 1 
ATOM   12231 C  CG2 . ILE   E 2 101 ? 6.718   -23.424 -53.783 1.00 114.03 ? 101  ILE   E CG2 1 
ATOM   12232 C  CD1 . ILE   E 2 101 ? 9.633   -25.916 -54.561 1.00 113.30 ? 101  ILE   E CD1 1 
ATOM   12233 N  N   . THR   E 2 102 ? 8.604   -25.784 -50.570 1.00 108.79 ? 102  THR   E N   1 
ATOM   12234 C  CA  . THR   E 2 102 ? 9.146   -26.907 -49.801 1.00 105.47 ? 102  THR   E CA  1 
ATOM   12235 C  C   . THR   E 2 102 ? 8.508   -28.170 -50.376 1.00 105.81 ? 102  THR   E C   1 
ATOM   12236 O  O   . THR   E 2 102 ? 7.331   -28.464 -50.136 1.00 106.81 ? 102  THR   E O   1 
ATOM   12237 C  CB  . THR   E 2 102 ? 8.915   -26.733 -48.299 1.00 104.91 ? 102  THR   E CB  1 
ATOM   12238 O  OG1 . THR   E 2 102 ? 7.521   -26.620 -47.990 1.00 112.48 ? 102  THR   E OG1 1 
ATOM   12239 C  CG2 . THR   E 2 102 ? 9.644   -25.488 -47.767 1.00 107.70 ? 102  THR   E CG2 1 
ATOM   12240 N  N   . ARG   E 2 103 ? 9.284   -28.887 -51.198 1.00 106.87 ? 103  ARG   E N   1 
ATOM   12241 C  CA  . ARG   E 2 103 ? 8.819   -30.162 -51.737 1.00 104.45 ? 103  ARG   E CA  1 
ATOM   12242 C  C   . ARG   E 2 103 ? 8.599   -31.161 -50.605 1.00 108.38 ? 103  ARG   E C   1 
ATOM   12243 O  O   . ARG   E 2 103 ? 7.493   -31.680 -50.423 1.00 109.47 ? 103  ARG   E O   1 
ATOM   12244 C  CB  . ARG   E 2 103 ? 9.804   -30.690 -52.781 1.00 95.07  ? 103  ARG   E CB  1 
ATOM   12245 N  N   . ALA   E 2 104 ? 9.625   -31.398 -49.792 1.00 106.23 ? 104  ALA   E N   1 
ATOM   12246 C  CA  . ALA   E 2 104 ? 9.491   -32.234 -48.608 1.00 103.03 ? 104  ALA   E CA  1 
ATOM   12247 C  C   . ALA   E 2 104 ? 9.795   -31.418 -47.351 1.00 106.25 ? 104  ALA   E C   1 
ATOM   12248 O  O   . ALA   E 2 104 ? 10.275  -30.279 -47.412 1.00 103.63 ? 104  ALA   E O   1 
ATOM   12249 C  CB  . ALA   E 2 104 ? 10.411  -33.457 -48.682 1.00 103.12 ? 104  ALA   E CB  1 
ATOM   12250 N  N   . HIS   E 2 105 ? 9.470   -32.005 -46.201 1.00 105.02 ? 105  HIS   E N   1 
ATOM   12251 C  CA  . HIS   E 2 105 ? 9.885   -31.463 -44.916 1.00 100.61 ? 105  HIS   E CA  1 
ATOM   12252 C  C   . HIS   E 2 105 ? 9.608   -32.497 -43.838 1.00 99.49  ? 105  HIS   E C   1 
ATOM   12253 O  O   . HIS   E 2 105 ? 8.651   -33.269 -43.922 1.00 103.35 ? 105  HIS   E O   1 
ATOM   12254 C  CB  . HIS   E 2 105 ? 9.202   -30.121 -44.582 1.00 101.14 ? 105  HIS   E CB  1 
ATOM   12255 C  CG  . HIS   E 2 105 ? 7.715   -30.199 -44.387 1.00 102.42 ? 105  HIS   E CG  1 
ATOM   12256 N  ND1 . HIS   E 2 105 ? 7.115   -30.091 -43.148 1.00 97.72  ? 105  HIS   E ND1 1 
ATOM   12257 C  CD2 . HIS   E 2 105 ? 6.705   -30.321 -45.285 1.00 108.92 ? 105  HIS   E CD2 1 
ATOM   12258 C  CE1 . HIS   E 2 105 ? 5.801   -30.160 -43.290 1.00 105.19 ? 105  HIS   E CE1 1 
ATOM   12259 N  NE2 . HIS   E 2 105 ? 5.526   -30.300 -44.577 1.00 109.42 ? 105  HIS   E NE2 1 
ATOM   12260 N  N   . GLY   E 2 106 ? 10.484  -32.524 -42.851 1.00 97.29  ? 106  GLY   E N   1 
ATOM   12261 C  CA  . GLY   E 2 106 ? 10.304  -33.381 -41.704 1.00 94.73  ? 106  GLY   E CA  1 
ATOM   12262 C  C   . GLY   E 2 106 ? 11.463  -33.167 -40.757 1.00 97.00  ? 106  GLY   E C   1 
ATOM   12263 O  O   . GLY   E 2 106 ? 12.512  -32.626 -41.135 1.00 98.65  ? 106  GLY   E O   1 
ATOM   12264 N  N   . ASN   E 2 107 ? 11.252  -33.592 -39.512 1.00 94.25  ? 107  ASN   E N   1 
ATOM   12265 C  CA  . ASN   E 2 107 ? 12.282  -33.514 -38.486 1.00 94.13  ? 107  ASN   E CA  1 
ATOM   12266 C  C   . ASN   E 2 107 ? 12.902  -34.881 -38.229 1.00 99.38  ? 107  ASN   E C   1 
ATOM   12267 O  O   . ASN   E 2 107 ? 12.205  -35.894 -38.157 1.00 103.96 ? 107  ASN   E O   1 
ATOM   12268 C  CB  . ASN   E 2 107 ? 11.733  -32.984 -37.177 1.00 91.34  ? 107  ASN   E CB  1 
ATOM   12269 C  CG  . ASN   E 2 107 ? 12.813  -32.758 -36.203 1.00 94.54  ? 107  ASN   E CG  1 
ATOM   12270 O  OD1 . ASN   E 2 107 ? 13.584  -31.825 -36.360 1.00 98.39  ? 107  ASN   E OD1 1 
ATOM   12271 N  ND2 . ASN   E 2 107 ? 12.931  -33.634 -35.218 1.00 99.32  ? 107  ASN   E ND2 1 
ATOM   12272 N  N   . VAL   E 2 108 ? 14.215  -34.898 -38.031 1.00 99.91  ? 108  VAL   E N   1 
ATOM   12273 C  CA  . VAL   E 2 108 ? 14.945  -36.156 -37.995 1.00 96.96  ? 108  VAL   E CA  1 
ATOM   12274 C  C   . VAL   E 2 108 ? 15.664  -36.304 -36.658 1.00 102.10 ? 108  VAL   E C   1 
ATOM   12275 O  O   . VAL   E 2 108 ? 16.761  -36.866 -36.589 1.00 101.85 ? 108  VAL   E O   1 
ATOM   12276 C  CB  . VAL   E 2 108 ? 15.923  -36.246 -39.188 1.00 94.50  ? 108  VAL   E CB  1 
ATOM   12277 C  CG1 . VAL   E 2 108 ? 15.164  -36.315 -40.516 1.00 88.72  ? 108  VAL   E CG1 1 
ATOM   12278 C  CG2 . VAL   E 2 108 ? 16.866  -35.054 -39.193 1.00 102.54 ? 108  VAL   E CG2 1 
ATOM   12279 N  N   . GLN   E 2 109 ? 15.059  -35.820 -35.580 1.00 112.99 ? 109  GLN   E N   1 
ATOM   12280 C  CA  . GLN   E 2 109 ? 15.662  -36.032 -34.271 1.00 116.18 ? 109  GLN   E CA  1 
ATOM   12281 C  C   . GLN   E 2 109 ? 15.430  -37.475 -33.832 1.00 116.04 ? 109  GLN   E C   1 
ATOM   12282 O  O   . GLN   E 2 109 ? 14.380  -38.059 -34.106 1.00 116.14 ? 109  GLN   E O   1 
ATOM   12283 C  CB  . GLN   E 2 109 ? 15.076  -35.054 -33.252 1.00 115.65 ? 109  GLN   E CB  1 
ATOM   12284 C  CG  . GLN   E 2 109 ? 15.988  -34.738 -32.084 1.00 115.24 ? 109  GLN   E CG  1 
ATOM   12285 C  CD  . GLN   E 2 109 ? 15.597  -33.438 -31.388 1.00 120.52 ? 109  GLN   E CD  1 
ATOM   12286 O  OE1 . GLN   E 2 109 ? 14.496  -32.917 -31.600 1.00 123.42 ? 109  GLN   E OE1 1 
ATOM   12287 N  NE2 . GLN   E 2 109 ? 16.502  -32.901 -30.562 1.00 122.60 ? 109  GLN   E NE2 1 
ATOM   12288 N  N   . ASP   E 2 110 ? 16.428  -38.074 -33.190 1.00 110.17 ? 110  ASP   E N   1 
ATOM   12289 C  CA  . ASP   E 2 110 ? 16.243  -39.363 -32.532 1.00 108.09 ? 110  ASP   E CA  1 
ATOM   12290 C  C   . ASP   E 2 110 ? 16.080  -39.108 -31.043 1.00 110.64 ? 110  ASP   E C   1 
ATOM   12291 O  O   . ASP   E 2 110 ? 16.883  -38.378 -30.452 1.00 114.53 ? 110  ASP   E O   1 
ATOM   12292 C  CB  . ASP   E 2 110 ? 17.418  -40.311 -32.792 1.00 105.85 ? 110  ASP   E CB  1 
ATOM   12293 C  CG  . ASP   E 2 110 ? 17.371  -40.934 -34.178 1.00 104.14 ? 110  ASP   E CG  1 
ATOM   12294 O  OD1 . ASP   E 2 110 ? 16.245  -41.198 -34.677 1.00 102.63 ? 110  ASP   E OD1 1 
ATOM   12295 O  OD2 . ASP   E 2 110 ? 18.453  -41.158 -34.765 1.00 98.87  ? 110  ASP   E OD2 1 
ATOM   12296 N  N   . ARG   E 2 111 ? 15.022  -39.674 -30.449 1.00 113.79 ? 111  ARG   E N   1 
ATOM   12297 C  CA  . ARG   E 2 111 ? 14.770  -39.476 -29.022 1.00 107.56 ? 111  ARG   E CA  1 
ATOM   12298 C  C   . ARG   E 2 111 ? 16.007  -39.825 -28.207 1.00 104.71 ? 111  ARG   E C   1 
ATOM   12299 O  O   . ARG   E 2 111 ? 16.567  -38.988 -27.490 1.00 105.82 ? 111  ARG   E O   1 
ATOM   12300 C  CB  . ARG   E 2 111 ? 13.576  -40.321 -28.571 1.00 97.93  ? 111  ARG   E CB  1 
ATOM   12301 N  N   . ILE   E 2 112 ? 16.452  -41.066 -28.324 1.00 103.85 ? 112  ILE   E N   1 
ATOM   12302 C  CA  . ILE   E 2 112 ? 17.707  -41.504 -27.729 1.00 108.86 ? 112  ILE   E CA  1 
ATOM   12303 C  C   . ILE   E 2 112 ? 18.828  -41.242 -28.722 1.00 114.98 ? 112  ILE   E C   1 
ATOM   12304 O  O   . ILE   E 2 112 ? 18.706  -41.590 -29.906 1.00 116.28 ? 112  ILE   E O   1 
ATOM   12305 C  CB  . ILE   E 2 112 ? 17.648  -42.996 -27.358 1.00 107.27 ? 112  ILE   E CB  1 
ATOM   12306 N  N   . GLY   E 2 113 ? 19.924  -40.637 -28.251 1.00 109.39 ? 113  GLY   E N   1 
ATOM   12307 C  CA  . GLY   E 2 113 ? 21.094  -40.554 -29.105 1.00 108.96 ? 113  GLY   E CA  1 
ATOM   12308 C  C   . GLY   E 2 113 ? 22.159  -39.566 -28.687 1.00 111.84 ? 113  GLY   E C   1 
ATOM   12309 O  O   . GLY   E 2 113 ? 21.858  -38.394 -28.437 1.00 110.45 ? 113  GLY   E O   1 
ATOM   12310 N  N   . ARG   E 2 114 ? 23.416  -40.032 -28.628 1.00 114.85 ? 114  ARG   E N   1 
ATOM   12311 C  CA  . ARG   E 2 114 ? 24.557  -39.164 -28.351 1.00 111.84 ? 114  ARG   E CA  1 
ATOM   12312 C  C   . ARG   E 2 114 ? 24.988  -38.467 -29.639 1.00 113.51 ? 114  ARG   E C   1 
ATOM   12313 O  O   . ARG   E 2 114 ? 25.312  -39.153 -30.621 1.00 114.32 ? 114  ARG   E O   1 
ATOM   12314 C  CB  . ARG   E 2 114 ? 25.721  -39.956 -27.769 1.00 111.87 ? 114  ARG   E CB  1 
ATOM   12315 N  N   . PRO   E 2 115 ? 24.981  -37.132 -29.691 1.00 108.92 ? 115  PRO   E N   1 
ATOM   12316 C  CA  . PRO   E 2 115 ? 25.411  -36.423 -30.901 1.00 103.49 ? 115  PRO   E CA  1 
ATOM   12317 C  C   . PRO   E 2 115 ? 26.909  -36.570 -31.107 1.00 101.19 ? 115  PRO   E C   1 
ATOM   12318 O  O   . PRO   E 2 115 ? 27.692  -36.450 -30.167 1.00 102.81 ? 115  PRO   E O   1 
ATOM   12319 C  CB  . PRO   E 2 115 ? 25.028  -34.968 -30.609 1.00 104.20 ? 115  PRO   E CB  1 
ATOM   12320 C  CG  . PRO   E 2 115 ? 24.006  -35.049 -29.551 1.00 103.66 ? 115  PRO   E CG  1 
ATOM   12321 C  CD  . PRO   E 2 115 ? 24.373  -36.224 -28.713 1.00 108.69 ? 115  PRO   E CD  1 
ATOM   12322 N  N   . SER   E 2 116 ? 27.306  -36.798 -32.352 1.00 98.06  ? 116  SER   E N   1 
ATOM   12323 C  CA  . SER   E 2 116 ? 28.687  -37.156 -32.625 1.00 103.21 ? 116  SER   E CA  1 
ATOM   12324 C  C   . SER   E 2 116 ? 29.650  -36.010 -32.349 1.00 104.58 ? 116  SER   E C   1 
ATOM   12325 O  O   . SER   E 2 116 ? 29.352  -34.839 -32.601 1.00 109.76 ? 116  SER   E O   1 
ATOM   12326 C  CB  . SER   E 2 116 ? 28.856  -37.584 -34.074 1.00 104.73 ? 116  SER   E CB  1 
ATOM   12327 O  OG  . SER   E 2 116 ? 30.239  -37.727 -34.350 1.00 106.45 ? 116  SER   E OG  1 
ATOM   12328 N  N   . GLU   E 2 117 ? 30.851  -36.383 -31.893 1.00 107.53 ? 117  GLU   E N   1 
ATOM   12329 C  CA  . GLU   E 2 117 ? 31.888  -35.399 -31.587 1.00 107.60 ? 117  GLU   E CA  1 
ATOM   12330 C  C   . GLU   E 2 117 ? 32.205  -34.515 -32.794 1.00 106.56 ? 117  GLU   E C   1 
ATOM   12331 O  O   . GLU   E 2 117 ? 32.231  -33.286 -32.683 1.00 109.87 ? 117  GLU   E O   1 
ATOM   12332 C  CB  . GLU   E 2 117 ? 33.144  -36.107 -31.080 1.00 105.02 ? 117  GLU   E CB  1 
ATOM   12333 N  N   . THR   E 2 118 ? 32.429  -35.110 -33.960 1.00 105.22 ? 118  THR   E N   1 
ATOM   12334 C  CA  . THR   E 2 118 ? 32.691  -34.330 -35.180 1.00 106.11 ? 118  THR   E CA  1 
ATOM   12335 C  C   . THR   E 2 118 ? 31.405  -33.693 -35.829 1.00 102.36 ? 118  THR   E C   1 
ATOM   12336 O  O   . THR   E 2 118 ? 31.435  -33.162 -36.962 1.00 102.72 ? 118  THR   E O   1 
ATOM   12337 C  CB  . THR   E 2 118 ? 33.442  -35.196 -36.212 1.00 107.81 ? 118  THR   E CB  1 
ATOM   12338 O  OG1 . THR   E 2 118 ? 32.615  -36.279 -36.671 1.00 108.57 ? 118  THR   E OG1 1 
ATOM   12339 C  CG2 . THR   E 2 118 ? 34.776  -35.743 -35.663 1.00 103.66 ? 118  THR   E CG2 1 
ATOM   12340 N  N   . GLY   E 2 119 ? 30.272  -33.726 -35.140 1.00 102.55 ? 119  GLY   E N   1 
ATOM   12341 C  CA  . GLY   E 2 119 ? 29.102  -32.978 -35.569 1.00 100.26 ? 119  GLY   E CA  1 
ATOM   12342 C  C   . GLY   E 2 119 ? 28.402  -33.573 -36.774 1.00 96.10  ? 119  GLY   E C   1 
ATOM   12343 O  O   . GLY   E 2 119 ? 28.800  -34.584 -37.354 1.00 94.08  ? 119  GLY   E O   1 
ATOM   12344 N  N   . ILE   E 2 120 ? 27.317  -32.900 -37.152 1.00 92.96  ? 120  ILE   E N   1 
ATOM   12345 C  CA  . ILE   E 2 120 ? 26.432  -33.405 -38.195 1.00 88.92  ? 120  ILE   E CA  1 
ATOM   12346 C  C   . ILE   E 2 120 ? 27.198  -33.467 -39.508 1.00 93.32  ? 120  ILE   E C   1 
ATOM   12347 O  O   . ILE   E 2 120 ? 27.673  -32.440 -40.007 1.00 89.41  ? 120  ILE   E O   1 
ATOM   12348 C  CB  . ILE   E 2 120 ? 25.183  -32.527 -38.349 1.00 83.51  ? 120  ILE   E CB  1 
ATOM   12349 C  CG1 . ILE   E 2 120 ? 24.305  -32.562 -37.106 1.00 82.39  ? 120  ILE   E CG1 1 
ATOM   12350 C  CG2 . ILE   E 2 120 ? 24.401  -32.972 -39.540 1.00 85.92  ? 120  ILE   E CG2 1 
ATOM   12351 C  CD1 . ILE   E 2 120 ? 24.960  -31.984 -35.876 1.00 100.21 ? 120  ILE   E CD1 1 
ATOM   12352 N  N   . ILE   E 2 121 ? 27.339  -34.683 -40.064 1.00 94.61  ? 121  ILE   E N   1 
ATOM   12353 C  CA  . ILE   E 2 121 ? 27.724  -34.875 -41.462 1.00 87.70  ? 121  ILE   E CA  1 
ATOM   12354 C  C   . ILE   E 2 121 ? 26.454  -35.151 -42.251 1.00 87.01  ? 121  ILE   E C   1 
ATOM   12355 O  O   . ILE   E 2 121 ? 25.543  -35.830 -41.760 1.00 91.23  ? 121  ILE   E O   1 
ATOM   12356 C  CB  . ILE   E 2 121 ? 28.747  -36.016 -41.646 1.00 85.42  ? 121  ILE   E CB  1 
ATOM   12357 C  CG1 . ILE   E 2 121 ? 30.080  -35.717 -40.956 1.00 90.10  ? 121  ILE   E CG1 1 
ATOM   12358 C  CG2 . ILE   E 2 121 ? 29.046  -36.210 -43.120 1.00 84.95  ? 121  ILE   E CG2 1 
ATOM   12359 C  CD1 . ILE   E 2 121 ? 31.274  -36.413 -41.651 1.00 90.85  ? 121  ILE   E CD1 1 
ATOM   12360 N  N   . GLY   E 2 122 ? 26.374  -34.611 -43.459 1.00 86.85  ? 122  GLY   E N   1 
ATOM   12361 C  CA  . GLY   E 2 122 ? 25.252  -34.913 -44.323 1.00 83.94  ? 122  GLY   E CA  1 
ATOM   12362 C  C   . GLY   E 2 122 ? 25.758  -35.038 -45.741 1.00 90.73  ? 122  GLY   E C   1 
ATOM   12363 O  O   . GLY   E 2 122 ? 26.457  -34.139 -46.225 1.00 96.15  ? 122  GLY   E O   1 
ATOM   12364 N  N   . ILE   E 2 123 ? 25.436  -36.144 -46.411 1.00 89.78  ? 123  ILE   E N   1 
ATOM   12365 C  CA  . ILE   E 2 123 ? 25.952  -36.445 -47.741 1.00 92.24  ? 123  ILE   E CA  1 
ATOM   12366 C  C   . ILE   E 2 123 ? 24.795  -36.904 -48.637 1.00 98.99  ? 123  ILE   E C   1 
ATOM   12367 O  O   . ILE   E 2 123 ? 23.689  -37.185 -48.165 1.00 98.37  ? 123  ILE   E O   1 
ATOM   12368 C  CB  . ILE   E 2 123 ? 27.064  -37.505 -47.668 1.00 94.42  ? 123  ILE   E CB  1 
ATOM   12369 C  CG1 . ILE   E 2 123 ? 26.554  -38.750 -46.951 1.00 98.54  ? 123  ILE   E CG1 1 
ATOM   12370 C  CG2 . ILE   E 2 123 ? 28.244  -36.982 -46.870 1.00 90.89  ? 123  ILE   E CG2 1 
ATOM   12371 C  CD1 . ILE   E 2 123 ? 27.583  -39.840 -46.930 1.00 98.03  ? 123  ILE   E CD1 1 
ATOM   12372 N  N   . ILE   E 2 124 ? 25.045  -36.974 -49.951 1.00 99.79  ? 124  ILE   E N   1 
ATOM   12373 C  CA  . ILE   E 2 124 ? 24.022  -37.424 -50.899 1.00 101.05 ? 124  ILE   E CA  1 
ATOM   12374 C  C   . ILE   E 2 124 ? 24.627  -38.367 -51.932 1.00 102.22 ? 124  ILE   E C   1 
ATOM   12375 O  O   . ILE   E 2 124 ? 25.621  -38.042 -52.588 1.00 102.94 ? 124  ILE   E O   1 
ATOM   12376 C  CB  . ILE   E 2 124 ? 23.300  -36.257 -51.597 1.00 100.90 ? 124  ILE   E CB  1 
ATOM   12377 C  CG1 . ILE   E 2 124 ? 22.284  -35.643 -50.639 1.00 92.55  ? 124  ILE   E CG1 1 
ATOM   12378 C  CG2 . ILE   E 2 124 ? 22.598  -36.736 -52.880 1.00 103.66 ? 124  ILE   E CG2 1 
ATOM   12379 C  CD1 . ILE   E 2 124 ? 21.209  -34.818 -51.332 1.00 98.42  ? 124  ILE   E CD1 1 
ATOM   12380 N  N   . ASP   E 2 125 ? 24.008  -39.521 -52.082 1.00 110.61 ? 125  ASP   E N   1 
ATOM   12381 C  CA  . ASP   E 2 125 ? 24.458  -40.498 -53.055 1.00 111.40 ? 125  ASP   E CA  1 
ATOM   12382 C  C   . ASP   E 2 125 ? 24.533  -39.847 -54.437 1.00 111.76 ? 125  ASP   E C   1 
ATOM   12383 O  O   . ASP   E 2 125 ? 23.653  -39.049 -54.797 1.00 111.49 ? 125  ASP   E O   1 
ATOM   12384 C  CB  . ASP   E 2 125 ? 23.509  -41.705 -53.019 1.00 114.12 ? 125  ASP   E CB  1 
ATOM   12385 C  CG  . ASP   E 2 125 ? 23.509  -42.516 -54.299 1.00 118.59 ? 125  ASP   E CG  1 
ATOM   12386 O  OD1 . ASP   E 2 125 ? 24.593  -42.971 -54.734 1.00 119.15 ? 125  ASP   E OD1 1 
ATOM   12387 O  OD2 . ASP   E 2 125 ? 22.407  -42.707 -54.869 1.00 121.91 ? 125  ASP   E OD2 1 
ATOM   12388 N  N   . PRO   E 2 126 ? 25.595  -40.112 -55.209 1.00 110.92 ? 126  PRO   E N   1 
ATOM   12389 C  CA  . PRO   E 2 126 ? 25.734  -39.464 -56.527 1.00 110.53 ? 126  PRO   E CA  1 
ATOM   12390 C  C   . PRO   E 2 126 ? 24.589  -39.756 -57.474 1.00 112.20 ? 126  PRO   E C   1 
ATOM   12391 O  O   . PRO   E 2 126 ? 24.440  -39.044 -58.475 1.00 115.24 ? 126  PRO   E O   1 
ATOM   12392 C  CB  . PRO   E 2 126 ? 27.058  -40.027 -57.068 1.00 104.03 ? 126  PRO   E CB  1 
ATOM   12393 C  CG  . PRO   E 2 126 ? 27.796  -40.527 -55.884 1.00 108.06 ? 126  PRO   E CG  1 
ATOM   12394 C  CD  . PRO   E 2 126 ? 26.767  -40.933 -54.858 1.00 108.91 ? 126  PRO   E CD  1 
ATOM   12395 N  N   . GLU   E 2 127 ? 23.794  -40.792 -57.209 1.00 114.16 ? 127  GLU   E N   1 
ATOM   12396 C  CA  . GLU   E 2 127 ? 22.643  -41.138 -58.027 1.00 112.82 ? 127  GLU   E CA  1 
ATOM   12397 C  C   . GLU   E 2 127 ? 21.336  -40.587 -57.460 1.00 116.15 ? 127  GLU   E C   1 
ATOM   12398 O  O   . GLU   E 2 127 ? 20.274  -40.862 -58.013 1.00 118.79 ? 127  GLU   E O   1 
ATOM   12399 C  CB  . GLU   E 2 127 ? 22.551  -42.661 -58.195 1.00 115.54 ? 127  GLU   E CB  1 
ATOM   12400 N  N   . CYS   E 2 128 ? 21.393  -39.808 -56.381 1.00 117.76 ? 128  CYS   E N   1 
ATOM   12401 C  CA  . CYS   E 2 128 ? 20.200  -39.313 -55.694 1.00 116.74 ? 128  CYS   E CA  1 
ATOM   12402 C  C   . CYS   E 2 128 ? 19.299  -40.448 -55.182 1.00 118.62 ? 128  CYS   E C   1 
ATOM   12403 O  O   . CYS   E 2 128 ? 18.114  -40.213 -54.902 1.00 111.08 ? 128  CYS   E O   1 
ATOM   12404 C  CB  . CYS   E 2 128 ? 19.401  -38.356 -56.591 1.00 117.03 ? 128  CYS   E CB  1 
ATOM   12405 S  SG  . CYS   E 2 128 ? 20.216  -36.794 -56.971 1.00 120.16 ? 128  CYS   E SG  1 
ATOM   12406 N  N   . ARG   E 2 129 ? 19.852  -41.670 -55.022 1.00 133.24 ? 129  ARG   E N   1 
ATOM   12407 C  CA  . ARG   E 2 129 ? 19.065  -42.802 -54.519 1.00 132.35 ? 129  ARG   E CA  1 
ATOM   12408 C  C   . ARG   E 2 129 ? 18.727  -42.655 -53.031 1.00 132.79 ? 129  ARG   E C   1 
ATOM   12409 O  O   . ARG   E 2 129 ? 17.729  -43.227 -52.571 1.00 133.00 ? 129  ARG   E O   1 
ATOM   12410 C  CB  . ARG   E 2 129 ? 19.790  -44.124 -54.787 1.00 129.29 ? 129  ARG   E CB  1 
ATOM   12411 N  N   . MET   E 2 130 ? 19.525  -41.845 -52.321 1.00 121.87 ? 130  MET   E N   1 
ATOM   12412 C  CA  . MET   E 2 130 ? 19.245  -41.597 -50.884 1.00 118.00 ? 130  MET   E CA  1 
ATOM   12413 C  C   . MET   E 2 130 ? 20.145  -40.516 -50.275 1.00 113.57 ? 130  MET   E C   1 
ATOM   12414 O  O   . MET   E 2 130 ? 21.261  -40.303 -50.799 1.00 110.91 ? 130  MET   E O   1 
ATOM   12415 C  CB  . MET   E 2 130 ? 19.468  -42.872 -50.061 1.00 114.55 ? 130  MET   E CB  1 
ATOM   12416 C  CG  . MET   E 2 130 ? 20.911  -43.331 -49.992 1.00 115.09 ? 130  MET   E CG  1 
ATOM   12417 S  SD  . MET   E 2 130 ? 21.175  -44.728 -48.884 1.00 126.13 ? 130  MET   E SD  1 
ATOM   12418 C  CE  . MET   E 2 130 ? 21.148  -43.885 -47.298 1.00 111.37 ? 130  MET   E CE  1 
ATOM   12419 N  N   . ILE   E 2 131 ? 19.640  -39.806 -49.266 1.00 110.32 ? 131  ILE   E N   1 
ATOM   12420 C  CA  . ILE   E 2 131 ? 20.440  -38.878 -48.472 1.00 102.66 ? 131  ILE   E CA  1 
ATOM   12421 C  C   . ILE   E 2 131 ? 20.981  -39.618 -47.253 1.00 101.08 ? 131  ILE   E C   1 
ATOM   12422 O  O   . ILE   E 2 131 ? 20.257  -40.407 -46.631 1.00 101.72 ? 131  ILE   E O   1 
ATOM   12423 C  CB  . ILE   E 2 131 ? 19.578  -37.676 -48.044 1.00 98.45  ? 131  ILE   E CB  1 
ATOM   12424 C  CG1 . ILE   E 2 131 ? 19.533  -36.623 -49.144 1.00 101.67 ? 131  ILE   E CG1 1 
ATOM   12425 C  CG2 . ILE   E 2 131 ? 20.075  -37.096 -46.745 1.00 92.52  ? 131  ILE   E CG2 1 
ATOM   12426 C  CD1 . ILE   E 2 131 ? 18.417  -35.617 -48.966 1.00 96.51  ? 131  ILE   E CD1 1 
ATOM   12427 N  N   . GLY   E 2 132 ? 22.243  -39.375 -46.904 1.00 97.54  ? 132  GLY   E N   1 
ATOM   12428 C  CA  . GLY   E 2 132 ? 22.852  -39.939 -45.700 1.00 95.30  ? 132  GLY   E CA  1 
ATOM   12429 C  C   . GLY   E 2 132 ? 23.058  -38.867 -44.643 1.00 92.36  ? 132  GLY   E C   1 
ATOM   12430 O  O   . GLY   E 2 132 ? 23.497  -37.762 -44.961 1.00 97.92  ? 132  GLY   E O   1 
ATOM   12431 N  N   . LEU   E 2 133 ? 22.754  -39.206 -43.381 1.00 90.11  ? 133  LEU   E N   1 
ATOM   12432 C  CA  . LEU   E 2 133 ? 22.830  -38.267 -42.250 1.00 94.03  ? 133  LEU   E CA  1 
ATOM   12433 C  C   . LEU   E 2 133 ? 23.532  -38.920 -41.060 1.00 92.33  ? 133  LEU   E C   1 
ATOM   12434 O  O   . LEU   E 2 133 ? 22.982  -39.854 -40.467 1.00 96.53  ? 133  LEU   E O   1 
ATOM   12435 C  CB  . LEU   E 2 133 ? 21.431  -37.805 -41.826 1.00 93.34  ? 133  LEU   E CB  1 
ATOM   12436 C  CG  . LEU   E 2 133 ? 20.882  -36.478 -42.340 1.00 92.62  ? 133  LEU   E CG  1 
ATOM   12437 C  CD1 . LEU   E 2 133 ? 21.133  -36.360 -43.824 1.00 93.11  ? 133  LEU   E CD1 1 
ATOM   12438 C  CD2 . LEU   E 2 133 ? 19.385  -36.398 -42.038 1.00 91.14  ? 133  LEU   E CD2 1 
ATOM   12439 N  N   . ARG   E 2 134 ? 24.721  -38.417 -40.671 1.00 87.79  ? 134  ARG   E N   1 
ATOM   12440 C  CA  . ARG   E 2 134 ? 25.373  -38.856 -39.427 1.00 95.75  ? 134  ARG   E CA  1 
ATOM   12441 C  C   . ARG   E 2 134 ? 25.101  -37.836 -38.325 1.00 97.32  ? 134  ARG   E C   1 
ATOM   12442 O  O   . ARG   E 2 134 ? 25.807  -36.830 -38.184 1.00 91.78  ? 134  ARG   E O   1 
ATOM   12443 C  CB  . ARG   E 2 134 ? 26.878  -39.056 -39.588 1.00 92.91  ? 134  ARG   E CB  1 
ATOM   12444 C  CG  . ARG   E 2 134 ? 27.484  -39.871 -38.424 1.00 92.68  ? 134  ARG   E CG  1 
ATOM   12445 C  CD  . ARG   E 2 134 ? 27.458  -39.144 -37.074 1.00 96.00  ? 134  ARG   E CD  1 
ATOM   12446 N  NE  . ARG   E 2 134 ? 28.387  -38.024 -37.083 1.00 100.20 ? 134  ARG   E NE  1 
ATOM   12447 C  CZ  . ARG   E 2 134 ? 29.703  -38.141 -36.963 1.00 103.13 ? 134  ARG   E CZ  1 
ATOM   12448 N  NH1 . ARG   E 2 134 ? 30.279  -39.321 -36.749 1.00 97.80  ? 134  ARG   E NH1 1 
ATOM   12449 N  NH2 . ARG   E 2 134 ? 30.461  -37.046 -37.056 1.00 100.71 ? 134  ARG   E NH2 1 
ATOM   12450 N  N   . LEU   E 2 135 ? 24.105  -38.139 -37.493 1.00 96.28  ? 135  LEU   E N   1 
ATOM   12451 C  CA  . LEU   E 2 135 ? 23.713  -37.282 -36.390 1.00 92.55  ? 135  LEU   E CA  1 
ATOM   12452 C  C   . LEU   E 2 135 ? 24.297  -37.728 -35.071 1.00 99.25  ? 135  LEU   E C   1 
ATOM   12453 O  O   . LEU   E 2 135 ? 24.706  -36.893 -34.259 1.00 103.24 ? 135  LEU   E O   1 
ATOM   12454 C  CB  . LEU   E 2 135 ? 22.192  -37.262 -36.258 1.00 93.49  ? 135  LEU   E CB  1 
ATOM   12455 C  CG  . LEU   E 2 135 ? 21.454  -36.207 -37.060 1.00 95.63  ? 135  LEU   E CG  1 
ATOM   12456 C  CD1 . LEU   E 2 135 ? 21.947  -36.206 -38.506 1.00 95.30  ? 135  LEU   E CD1 1 
ATOM   12457 C  CD2 . LEU   E 2 135 ? 19.950  -36.461 -36.960 1.00 94.93  ? 135  LEU   E CD2 1 
ATOM   12458 N  N   . TYR   E 2 136 ? 24.317  -39.029 -34.835 1.00 107.32 ? 136  TYR   E N   1 
ATOM   12459 C  CA  . TYR   E 2 136 ? 24.603  -39.576 -33.524 1.00 108.04 ? 136  TYR   E CA  1 
ATOM   12460 C  C   . TYR   E 2 136 ? 25.630  -40.691 -33.661 1.00 108.57 ? 136  TYR   E C   1 
ATOM   12461 O  O   . TYR   E 2 136 ? 25.707  -41.378 -34.690 1.00 105.98 ? 136  TYR   E O   1 
ATOM   12462 C  CB  . TYR   E 2 136 ? 23.307  -40.091 -32.834 1.00 106.04 ? 136  TYR   E CB  1 
ATOM   12463 C  CG  . TYR   E 2 136 ? 22.146  -39.089 -32.732 1.00 102.10 ? 136  TYR   E CG  1 
ATOM   12464 C  CD1 . TYR   E 2 136 ? 22.064  -38.189 -31.677 1.00 105.47 ? 136  TYR   E CD1 1 
ATOM   12465 C  CD2 . TYR   E 2 136 ? 21.119  -39.072 -33.670 1.00 98.62  ? 136  TYR   E CD2 1 
ATOM   12466 C  CE1 . TYR   E 2 136 ? 20.999  -37.289 -31.571 1.00 106.17 ? 136  TYR   E CE1 1 
ATOM   12467 C  CE2 . TYR   E 2 136 ? 20.056  -38.174 -33.574 1.00 96.47  ? 136  TYR   E CE2 1 
ATOM   12468 C  CZ  . TYR   E 2 136 ? 19.998  -37.286 -32.522 1.00 99.51  ? 136  TYR   E CZ  1 
ATOM   12469 O  OH  . TYR   E 2 136 ? 18.945  -36.394 -32.398 1.00 97.05  ? 136  TYR   E OH  1 
ATOM   12470 N  N   . ASP   E 2 137 ? 26.427  -40.845 -32.608 1.00 110.03 ? 137  ASP   E N   1 
ATOM   12471 C  CA  . ASP   E 2 137 ? 27.510  -41.812 -32.616 1.00 110.80 ? 137  ASP   E CA  1 
ATOM   12472 C  C   . ASP   E 2 137 ? 26.951  -43.225 -32.586 1.00 113.55 ? 137  ASP   E C   1 
ATOM   12473 O  O   . ASP   E 2 137 ? 26.101  -43.551 -31.748 1.00 109.51 ? 137  ASP   E O   1 
ATOM   12474 C  CB  . ASP   E 2 137 ? 28.443  -41.561 -31.439 1.00 112.10 ? 137  ASP   E CB  1 
ATOM   12475 C  CG  . ASP   E 2 137 ? 29.689  -40.812 -31.857 1.00 114.96 ? 137  ASP   E CG  1 
ATOM   12476 O  OD1 . ASP   E 2 137 ? 30.146  -41.108 -32.983 1.00 120.69 ? 137  ASP   E OD1 1 
ATOM   12477 O  OD2 . ASP   E 2 137 ? 30.206  -39.942 -31.104 1.00 110.96 ? 137  ASP   E OD2 1 
ATOM   12478 N  N   . GLY   E 2 138 ? 27.404  -44.049 -33.536 1.00 115.26 ? 138  GLY   E N   1 
ATOM   12479 C  CA  . GLY   E 2 138 ? 26.966  -45.420 -33.661 1.00 109.03 ? 138  GLY   E CA  1 
ATOM   12480 C  C   . GLY   E 2 138 ? 25.855  -45.668 -34.662 1.00 112.77 ? 138  GLY   E C   1 
ATOM   12481 O  O   . GLY   E 2 138 ? 25.540  -46.834 -34.935 1.00 113.76 ? 138  GLY   E O   1 
ATOM   12482 N  N   . LEU   E 2 139 ? 25.257  -44.623 -35.227 1.00 113.82 ? 139  LEU   E N   1 
ATOM   12483 C  CA  . LEU   E 2 139 ? 24.125  -44.775 -36.131 1.00 110.60 ? 139  LEU   E CA  1 
ATOM   12484 C  C   . LEU   E 2 139 ? 24.386  -44.078 -37.457 1.00 105.46 ? 139  LEU   E C   1 
ATOM   12485 O  O   . LEU   E 2 139 ? 25.302  -43.264 -37.583 1.00 107.05 ? 139  LEU   E O   1 
ATOM   12486 C  CB  . LEU   E 2 139 ? 22.844  -44.211 -35.511 1.00 109.01 ? 139  LEU   E CB  1 
ATOM   12487 C  CG  . LEU   E 2 139 ? 21.915  -45.261 -34.919 1.00 107.84 ? 139  LEU   E CG  1 
ATOM   12488 C  CD1 . LEU   E 2 139 ? 22.719  -46.287 -34.136 1.00 107.59 ? 139  LEU   E CD1 1 
ATOM   12489 C  CD2 . LEU   E 2 139 ? 20.885  -44.580 -34.035 1.00 105.45 ? 139  LEU   E CD2 1 
ATOM   12490 N  N   . PHE   E 2 140 ? 23.540  -44.394 -38.440 1.00 96.93  ? 140  PHE   E N   1 
ATOM   12491 C  CA  . PHE   E 2 140 ? 23.571  -43.751 -39.753 1.00 97.00  ? 140  PHE   E CA  1 
ATOM   12492 C  C   . PHE   E 2 140 ? 22.148  -43.658 -40.300 1.00 99.04  ? 140  PHE   E C   1 
ATOM   12493 O  O   . PHE   E 2 140 ? 21.553  -44.684 -40.647 1.00 101.71 ? 140  PHE   E O   1 
ATOM   12494 C  CB  . PHE   E 2 140 ? 24.469  -44.519 -40.709 1.00 99.07  ? 140  PHE   E CB  1 
ATOM   12495 C  CG  . PHE   E 2 140 ? 24.770  -43.780 -41.979 1.00 98.12  ? 140  PHE   E CG  1 
ATOM   12496 C  CD1 . PHE   E 2 140 ? 25.332  -42.522 -41.944 1.00 100.77 ? 140  PHE   E CD1 1 
ATOM   12497 C  CD2 . PHE   E 2 140 ? 24.500  -44.358 -43.218 1.00 91.22  ? 140  PHE   E CD2 1 
ATOM   12498 C  CE1 . PHE   E 2 140 ? 25.624  -41.834 -43.115 1.00 99.09  ? 140  PHE   E CE1 1 
ATOM   12499 C  CE2 . PHE   E 2 140 ? 24.788  -43.682 -44.384 1.00 96.51  ? 140  PHE   E CE2 1 
ATOM   12500 C  CZ  . PHE   E 2 140 ? 25.347  -42.427 -44.343 1.00 99.71  ? 140  PHE   E CZ  1 
ATOM   12501 N  N   . LYS   E 2 141 ? 21.608  -42.429 -40.394 1.00 98.58  ? 141  LYS   E N   1 
ATOM   12502 C  CA  . LYS   E 2 141 ? 20.268  -42.218 -40.944 1.00 98.55  ? 141  LYS   E CA  1 
ATOM   12503 C  C   . LYS   E 2 141 ? 20.294  -42.170 -42.464 1.00 100.09 ? 141  LYS   E C   1 
ATOM   12504 O  O   . LYS   E 2 141 ? 21.194  -41.587 -43.082 1.00 97.46  ? 141  LYS   E O   1 
ATOM   12505 C  CB  . LYS   E 2 141 ? 19.620  -40.935 -40.426 1.00 90.90  ? 141  LYS   E CB  1 
ATOM   12506 N  N   . VAL   E 2 142 ? 19.281  -42.775 -43.056 1.00 102.84 ? 142  VAL   E N   1 
ATOM   12507 C  CA  . VAL   E 2 142 ? 19.160  -42.922 -44.492 1.00 104.07 ? 142  VAL   E CA  1 
ATOM   12508 C  C   . VAL   E 2 142 ? 17.775  -42.409 -44.849 1.00 103.71 ? 142  VAL   E C   1 
ATOM   12509 O  O   . VAL   E 2 142 ? 16.763  -42.984 -44.432 1.00 104.86 ? 142  VAL   E O   1 
ATOM   12510 C  CB  . VAL   E 2 142 ? 19.376  -44.379 -44.935 1.00 101.03 ? 142  VAL   E CB  1 
ATOM   12511 C  CG1 . VAL   E 2 142 ? 19.123  -44.538 -46.439 1.00 102.38 ? 142  VAL   E CG1 1 
ATOM   12512 C  CG2 . VAL   E 2 142 ? 20.783  -44.809 -44.576 1.00 97.88  ? 142  VAL   E CG2 1 
ATOM   12513 N  N   . ILE   E 2 143 ? 17.725  -41.290 -45.558 1.00 98.69  ? 143  ILE   E N   1 
ATOM   12514 C  CA  . ILE   E 2 143 ? 16.453  -40.777 -46.042 1.00 103.56 ? 143  ILE   E CA  1 
ATOM   12515 C  C   . ILE   E 2 143 ? 16.270  -41.199 -47.491 1.00 108.95 ? 143  ILE   E C   1 
ATOM   12516 O  O   . ILE   E 2 143 ? 16.661  -40.454 -48.401 1.00 109.72 ? 143  ILE   E O   1 
ATOM   12517 C  CB  . ILE   E 2 143 ? 16.375  -39.252 -45.932 1.00 105.31 ? 143  ILE   E CB  1 
ATOM   12518 C  CG1 . ILE   E 2 143 ? 16.756  -38.768 -44.530 1.00 99.70  ? 143  ILE   E CG1 1 
ATOM   12519 C  CG2 . ILE   E 2 143 ? 14.982  -38.806 -46.308 1.00 105.56 ? 143  ILE   E CG2 1 
ATOM   12520 C  CD1 . ILE   E 2 143 ? 17.514  -37.458 -44.531 1.00 98.30  ? 143  ILE   E CD1 1 
ATOM   12521 N  N   . PRO   E 2 144 ? 15.676  -42.361 -47.754 1.00 108.36 ? 144  PRO   E N   1 
ATOM   12522 C  CA  . PRO   E 2 144 ? 15.440  -42.765 -49.147 1.00 111.58 ? 144  PRO   E CA  1 
ATOM   12523 C  C   . PRO   E 2 144 ? 14.744  -41.646 -49.923 1.00 117.96 ? 144  PRO   E C   1 
ATOM   12524 O  O   . PRO   E 2 144 ? 13.829  -40.992 -49.409 1.00 112.44 ? 144  PRO   E O   1 
ATOM   12525 C  CB  . PRO   E 2 144 ? 14.555  -44.014 -49.006 1.00 107.36 ? 144  PRO   E CB  1 
ATOM   12526 C  CG  . PRO   E 2 144 ? 13.937  -43.890 -47.652 1.00 110.08 ? 144  PRO   E CG  1 
ATOM   12527 C  CD  . PRO   E 2 144 ? 14.987  -43.244 -46.798 1.00 108.82 ? 144  PRO   E CD  1 
ATOM   12528 N  N   . LEU   E 2 145 ? 15.206  -41.429 -51.161 1.00 121.02 ? 145  LEU   E N   1 
ATOM   12529 C  CA  . LEU   E 2 145 ? 14.741  -40.354 -52.033 1.00 122.11 ? 145  LEU   E CA  1 
ATOM   12530 C  C   . LEU   E 2 145 ? 13.773  -40.907 -53.076 1.00 131.97 ? 145  LEU   E C   1 
ATOM   12531 O  O   . LEU   E 2 145 ? 14.115  -41.114 -54.239 1.00 133.89 ? 145  LEU   E O   1 
ATOM   12532 C  CB  . LEU   E 2 145 ? 15.934  -39.664 -52.706 1.00 119.51 ? 145  LEU   E CB  1 
ATOM   12533 C  CG  . LEU   E 2 145 ? 16.688  -38.651 -51.845 1.00 118.69 ? 145  LEU   E CG  1 
ATOM   12534 C  CD1 . LEU   E 2 145 ? 17.838  -38.000 -52.608 1.00 114.98 ? 145  LEU   E CD1 1 
ATOM   12535 C  CD2 . LEU   E 2 145 ? 15.741  -37.585 -51.310 1.00 115.24 ? 145  LEU   E CD2 1 
ATOM   12536 N  N   . ASP   E 2 146 ? 12.541  -41.150 -52.640 1.00 143.92 ? 146  ASP   E N   1 
ATOM   12537 C  CA  . ASP   E 2 146 ? 11.475  -41.610 -53.520 1.00 145.93 ? 146  ASP   E CA  1 
ATOM   12538 C  C   . ASP   E 2 146 ? 10.435  -40.511 -53.670 1.00 149.97 ? 146  ASP   E C   1 
ATOM   12539 O  O   . ASP   E 2 146 ? 10.213  -39.708 -52.757 1.00 149.50 ? 146  ASP   E O   1 
ATOM   12540 C  CB  . ASP   E 2 146 ? 10.810  -42.881 -53.005 1.00 143.04 ? 146  ASP   E CB  1 
ATOM   12541 C  CG  . ASP   E 2 146 ? 11.652  -44.112 -53.250 1.00 146.01 ? 146  ASP   E CG  1 
ATOM   12542 O  OD1 . ASP   E 2 146 ? 12.795  -43.992 -53.744 1.00 144.72 ? 146  ASP   E OD1 1 
ATOM   12543 O  OD2 . ASP   E 2 146 ? 11.162  -45.210 -52.953 1.00 157.38 ? 146  ASP   E OD2 1 
ATOM   12544 N  N   . ARG   E 2 147 ? 9.797   -40.486 -54.844 1.00 150.98 ? 147  ARG   E N   1 
ATOM   12545 C  CA  . ARG   E 2 147 ? 8.908   -39.377 -55.151 1.00 149.89 ? 147  ARG   E CA  1 
ATOM   12546 C  C   . ARG   E 2 147 ? 7.791   -39.276 -54.132 1.00 151.38 ? 147  ARG   E C   1 
ATOM   12547 O  O   . ARG   E 2 147 ? 7.236   -38.194 -53.933 1.00 146.32 ? 147  ARG   E O   1 
ATOM   12548 C  CB  . ARG   E 2 147 ? 8.336   -39.535 -56.559 1.00 151.28 ? 147  ARG   E CB  1 
ATOM   12549 N  N   . ASP   E 2 148 ? 7.445   -40.385 -53.477 1.00 160.97 ? 148  ASP   E N   1 
ATOM   12550 C  CA  . ASP   E 2 148 ? 6.378   -40.338 -52.490 1.00 161.49 ? 148  ASP   E CA  1 
ATOM   12551 C  C   . ASP   E 2 148 ? 6.849   -39.781 -51.143 1.00 161.65 ? 148  ASP   E C   1 
ATOM   12552 O  O   . ASP   E 2 148 ? 6.013   -39.274 -50.383 1.00 164.25 ? 148  ASP   E O   1 
ATOM   12553 C  CB  . ASP   E 2 148 ? 5.768   -41.728 -52.310 1.00 158.28 ? 148  ASP   E CB  1 
ATOM   12554 N  N   . ASN   E 2 149 ? 8.153   -39.843 -50.833 1.00 145.58 ? 149  ASN   E N   1 
ATOM   12555 C  CA  . ASN   E 2 149 ? 8.608   -39.387 -49.519 1.00 132.38 ? 149  ASN   E CA  1 
ATOM   12556 C  C   . ASN   E 2 149 ? 8.554   -37.864 -49.445 1.00 128.83 ? 149  ASN   E C   1 
ATOM   12557 O  O   . ASN   E 2 149 ? 9.538   -37.181 -49.743 1.00 125.22 ? 149  ASN   E O   1 
ATOM   12558 C  CB  . ASN   E 2 149 ? 10.021  -39.883 -49.199 1.00 124.26 ? 149  ASN   E CB  1 
ATOM   12559 C  CG  . ASN   E 2 149 ? 10.254  -40.022 -47.696 1.00 111.20 ? 149  ASN   E CG  1 
ATOM   12560 O  OD1 . ASN   E 2 149 ? 9.433   -39.582 -46.896 1.00 113.03 ? 149  ASN   E OD1 1 
ATOM   12561 N  ND2 . ASN   E 2 149 ? 11.369  -40.650 -47.313 1.00 106.12 ? 149  ASN   E ND2 1 
ATOM   12562 N  N   . LYS   E 2 150 ? 7.387   -37.332 -49.059 1.00 122.45 ? 150  LYS   E N   1 
ATOM   12563 C  CA  . LYS   E 2 150 ? 7.257   -35.903 -48.832 1.00 117.42 ? 150  LYS   E CA  1 
ATOM   12564 C  C   . LYS   E 2 150 ? 7.504   -35.538 -47.379 1.00 113.78 ? 150  LYS   E C   1 
ATOM   12565 O  O   . LYS   E 2 150 ? 7.968   -34.428 -47.090 1.00 112.88 ? 150  LYS   E O   1 
ATOM   12566 C  CB  . LYS   E 2 150 ? 5.873   -35.428 -49.271 1.00 118.17 ? 150  LYS   E CB  1 
ATOM   12567 N  N   . GLU   E 2 151 ? 7.207   -36.447 -46.462 1.00 111.91 ? 151  GLU   E N   1 
ATOM   12568 C  CA  . GLU   E 2 151 ? 7.460   -36.225 -45.053 1.00 105.00 ? 151  GLU   E CA  1 
ATOM   12569 C  C   . GLU   E 2 151 ? 8.873   -36.630 -44.647 1.00 107.12 ? 151  GLU   E C   1 
ATOM   12570 O  O   . GLU   E 2 151 ? 9.194   -36.581 -43.457 1.00 112.16 ? 151  GLU   E O   1 
ATOM   12571 C  CB  . GLU   E 2 151 ? 6.422   -36.980 -44.216 1.00 104.18 ? 151  GLU   E CB  1 
ATOM   12572 N  N   . LEU   E 2 152 ? 9.726   -37.024 -45.604 1.00 108.52 ? 152  LEU   E N   1 
ATOM   12573 C  CA  . LEU   E 2 152 ? 11.145  -37.335 -45.340 1.00 105.81 ? 152  LEU   E CA  1 
ATOM   12574 C  C   . LEU   E 2 152 ? 11.324  -38.465 -44.323 1.00 101.28 ? 152  LEU   E C   1 
ATOM   12575 O  O   . LEU   E 2 152 ? 12.255  -38.455 -43.514 1.00 97.53  ? 152  LEU   E O   1 
ATOM   12576 C  CB  . LEU   E 2 152 ? 11.905  -36.086 -44.891 1.00 105.24 ? 152  LEU   E CB  1 
ATOM   12577 C  CG  . LEU   E 2 152 ? 11.921  -34.953 -45.917 1.00 108.52 ? 152  LEU   E CG  1 
ATOM   12578 C  CD1 . LEU   E 2 152 ? 12.163  -33.590 -45.245 1.00 103.19 ? 152  LEU   E CD1 1 
ATOM   12579 C  CD2 . LEU   E 2 152 ? 12.974  -35.241 -46.982 1.00 101.32 ? 152  LEU   E CD2 1 
ATOM   12580 N  N   . LYS   E 2 153 ? 10.434  -39.454 -44.380 1.00 105.18 ? 153  LYS   E N   1 
ATOM   12581 C  CA  . LYS   E 2 153 ? 10.547  -40.641 -43.540 1.00 102.39 ? 153  LYS   E CA  1 
ATOM   12582 C  C   . LYS   E 2 153 ? 11.886  -41.335 -43.767 1.00 105.28 ? 153  LYS   E C   1 
ATOM   12583 O  O   . LYS   E 2 153 ? 12.345  -41.469 -44.907 1.00 106.28 ? 153  LYS   E O   1 
ATOM   12584 C  CB  . LYS   E 2 153 ? 9.388   -41.590 -43.847 1.00 93.32  ? 153  LYS   E CB  1 
ATOM   12585 N  N   . ALA   E 2 154 ? 12.513  -41.784 -42.676 1.00 98.40  ? 154  ALA   E N   1 
ATOM   12586 C  CA  . ALA   E 2 154 ? 13.877  -42.304 -42.731 1.00 104.03 ? 154  ALA   E CA  1 
ATOM   12587 C  C   . ALA   E 2 154 ? 14.015  -43.543 -41.856 1.00 108.23 ? 154  ALA   E C   1 
ATOM   12588 O  O   . ALA   E 2 154 ? 13.114  -43.898 -41.098 1.00 113.39 ? 154  ALA   E O   1 
ATOM   12589 C  CB  . ALA   E 2 154 ? 14.902  -41.257 -42.284 1.00 110.01 ? 154  ALA   E CB  1 
ATOM   12590 N  N   . PHE   E 2 155 ? 15.169  -44.203 -41.969 1.00 108.38 ? 155  PHE   E N   1 
ATOM   12591 C  CA  . PHE   E 2 155 ? 15.502  -45.371 -41.163 1.00 110.10 ? 155  PHE   E CA  1 
ATOM   12592 C  C   . PHE   E 2 155 ? 16.965  -45.292 -40.718 1.00 108.21 ? 155  PHE   E C   1 
ATOM   12593 O  O   . PHE   E 2 155 ? 17.813  -44.764 -41.439 1.00 107.87 ? 155  PHE   E O   1 
ATOM   12594 C  CB  . PHE   E 2 155 ? 15.215  -46.699 -41.916 1.00 111.78 ? 155  PHE   E CB  1 
ATOM   12595 C  CG  . PHE   E 2 155 ? 16.145  -47.002 -43.089 1.00 109.62 ? 155  PHE   E CG  1 
ATOM   12596 C  CD1 . PHE   E 2 155 ? 17.524  -47.233 -42.898 1.00 110.53 ? 155  PHE   E CD1 1 
ATOM   12597 C  CD2 . PHE   E 2 155 ? 15.620  -47.111 -44.365 1.00 109.93 ? 155  PHE   E CD2 1 
ATOM   12598 C  CE1 . PHE   E 2 155 ? 18.335  -47.541 -43.972 1.00 112.31 ? 155  PHE   E CE1 1 
ATOM   12599 C  CE2 . PHE   E 2 155 ? 16.421  -47.421 -45.447 1.00 113.23 ? 155  PHE   E CE2 1 
ATOM   12600 C  CZ  . PHE   E 2 155 ? 17.777  -47.638 -45.258 1.00 113.30 ? 155  PHE   E CZ  1 
ATOM   12601 N  N   . ASN   E 2 156 ? 17.257  -45.810 -39.525 1.00 105.27 ? 156  ASN   E N   1 
ATOM   12602 C  CA  . ASN   E 2 156 ? 18.620  -45.907 -39.017 1.00 106.37 ? 156  ASN   E CA  1 
ATOM   12603 C  C   . ASN   E 2 156 ? 19.187  -47.309 -39.287 1.00 109.44 ? 156  ASN   E C   1 
ATOM   12604 O  O   . ASN   E 2 156 ? 18.473  -48.200 -39.746 1.00 116.24 ? 156  ASN   E O   1 
ATOM   12605 C  CB  . ASN   E 2 156 ? 18.644  -45.553 -37.525 1.00 107.27 ? 156  ASN   E CB  1 
ATOM   12606 C  CG  . ASN   E 2 156 ? 19.055  -44.148 -37.280 1.00 104.85 ? 156  ASN   E CG  1 
ATOM   12607 O  OD1 . ASN   E 2 156 ? 20.058  -43.716 -37.830 1.00 109.07 ? 156  ASN   E OD1 1 
ATOM   12608 N  ND2 . ASN   E 2 156 ? 18.306  -43.418 -36.445 1.00 113.07 ? 156  ASN   E ND2 1 
ATOM   12609 N  N   . ILE   E 2 157 ? 20.506  -47.476 -39.102 1.00 104.97 ? 157  ILE   E N   1 
ATOM   12610 C  CA  . ILE   E 2 157 ? 21.163  -48.791 -39.026 1.00 116.89 ? 157  ILE   E CA  1 
ATOM   12611 C  C   . ILE   E 2 157 ? 22.473  -48.671 -38.223 1.00 113.82 ? 157  ILE   E C   1 
ATOM   12612 O  O   . ILE   E 2 157 ? 23.145  -47.630 -38.234 1.00 113.49 ? 157  ILE   E O   1 
ATOM   12613 C  CB  . ILE   E 2 157 ? 21.365  -49.407 -40.429 1.00 121.76 ? 157  ILE   E CB  1 
ATOM   12614 C  CG1 . ILE   E 2 157 ? 22.240  -48.576 -41.341 1.00 107.43 ? 157  ILE   E CG1 1 
ATOM   12615 C  CG2 . ILE   E 2 157 ? 20.047  -49.461 -41.245 1.00 117.90 ? 157  ILE   E CG2 1 
ATOM   12616 C  CD1 . ILE   E 2 157 ? 22.610  -49.347 -42.685 1.00 122.48 ? 157  ILE   E CD1 1 
ATOM   12617 N  N   . ARG   E 2 158 ? 22.825  -49.739 -37.509 1.00 116.15 ? 158  ARG   E N   1 
ATOM   12618 C  CA  . ARG   E 2 158 ? 23.911  -49.689 -36.553 1.00 114.66 ? 158  ARG   E CA  1 
ATOM   12619 C  C   . ARG   E 2 158 ? 25.227  -49.506 -37.281 1.00 117.79 ? 158  ARG   E C   1 
ATOM   12620 O  O   . ARG   E 2 158 ? 25.418  -50.007 -38.395 1.00 118.45 ? 158  ARG   E O   1 
ATOM   12621 C  CB  . ARG   E 2 158 ? 23.935  -50.969 -35.716 1.00 120.41 ? 158  ARG   E CB  1 
ATOM   12622 N  N   . LEU   E 2 159 ? 26.133  -48.771 -36.632 1.00 118.52 ? 159  LEU   E N   1 
ATOM   12623 C  CA  . LEU   E 2 159 ? 27.478  -48.498 -37.134 1.00 119.86 ? 159  LEU   E CA  1 
ATOM   12624 C  C   . LEU   E 2 159 ? 28.482  -48.919 -36.057 1.00 119.91 ? 159  LEU   E C   1 
ATOM   12625 O  O   . LEU   E 2 159 ? 28.678  -48.199 -35.070 1.00 113.79 ? 159  LEU   E O   1 
ATOM   12626 C  CB  . LEU   E 2 159 ? 27.630  -47.026 -37.508 1.00 107.09 ? 159  LEU   E CB  1 
ATOM   12627 N  N   . GLU   E 2 160 ? 29.120  -50.079 -36.263 1.00 121.03 ? 160  GLU   E N   1 
ATOM   12628 C  CA  . GLU   E 2 160 ? 30.025  -50.634 -35.261 1.00 118.13 ? 160  GLU   E CA  1 
ATOM   12629 C  C   . GLU   E 2 160 ? 31.149  -49.663 -34.927 1.00 117.09 ? 160  GLU   E C   1 
ATOM   12630 O  O   . GLU   E 2 160 ? 31.558  -49.557 -33.770 1.00 116.47 ? 160  GLU   E O   1 
ATOM   12631 C  CB  . GLU   E 2 160 ? 30.575  -51.972 -35.748 1.00 117.45 ? 160  GLU   E CB  1 
ATOM   12632 N  N   . GLU   E 2 161 ? 31.660  -48.942 -35.931 1.00 118.33 ? 161  GLU   E N   1 
ATOM   12633 C  CA  . GLU   E 2 161 ? 32.620  -47.864 -35.700 1.00 117.01 ? 161  GLU   E CA  1 
ATOM   12634 C  C   . GLU   E 2 161 ? 31.919  -46.712 -34.994 1.00 117.89 ? 161  GLU   E C   1 
ATOM   12635 O  O   . GLU   E 2 161 ? 31.041  -46.068 -35.570 1.00 120.29 ? 161  GLU   E O   1 
ATOM   12636 C  CB  . GLU   E 2 161 ? 33.253  -47.404 -37.013 1.00 113.51 ? 161  GLU   E CB  1 
ATOM   12637 N  N   . LEU   E 2 162 ? 32.288  -46.447 -33.747 1.00 116.59 ? 162  LEU   E N   1 
ATOM   12638 C  CA  . LEU   E 2 162 ? 31.550  -45.497 -32.936 1.00 115.53 ? 162  LEU   E CA  1 
ATOM   12639 C  C   . LEU   E 2 162 ? 32.175  -44.108 -32.925 1.00 114.97 ? 162  LEU   E C   1 
ATOM   12640 O  O   . LEU   E 2 162 ? 31.675  -43.227 -32.221 1.00 115.48 ? 162  LEU   E O   1 
ATOM   12641 C  CB  . LEU   E 2 162 ? 31.438  -46.015 -31.503 1.00 116.02 ? 162  LEU   E CB  1 
ATOM   12642 C  CG  . LEU   E 2 162 ? 30.130  -46.711 -31.112 1.00 111.21 ? 162  LEU   E CG  1 
ATOM   12643 C  CD1 . LEU   E 2 162 ? 28.955  -45.815 -31.404 1.00 117.34 ? 162  LEU   E CD1 1 
ATOM   12644 C  CD2 . LEU   E 2 162 ? 29.970  -48.020 -31.834 1.00 115.06 ? 162  LEU   E CD2 1 
ATOM   12645 N  N   . HIS   E 2 163 ? 33.274  -43.897 -33.657 1.00 114.01 ? 163  HIS   E N   1 
ATOM   12646 C  CA  . HIS   E 2 163 ? 34.013  -42.639 -33.636 1.00 114.68 ? 163  HIS   E CA  1 
ATOM   12647 C  C   . HIS   E 2 163 ? 34.508  -42.337 -35.058 1.00 112.75 ? 163  HIS   E C   1 
ATOM   12648 O  O   . HIS   E 2 163 ? 35.664  -42.585 -35.419 1.00 110.45 ? 163  HIS   E O   1 
ATOM   12649 C  CB  . HIS   E 2 163 ? 35.168  -42.670 -32.641 1.00 114.93 ? 163  HIS   E CB  1 
ATOM   12650 C  CG  . HIS   E 2 163 ? 34.800  -43.206 -31.291 1.00 121.29 ? 163  HIS   E CG  1 
ATOM   12651 N  ND1 . HIS   E 2 163 ? 33.867  -42.603 -30.468 1.00 126.88 ? 163  HIS   E ND1 1 
ATOM   12652 C  CD2 . HIS   E 2 163 ? 35.266  -44.280 -30.607 1.00 123.49 ? 163  HIS   E CD2 1 
ATOM   12653 C  CE1 . HIS   E 2 163 ? 33.769  -43.291 -29.341 1.00 124.69 ? 163  HIS   E CE1 1 
ATOM   12654 N  NE2 . HIS   E 2 163 ? 34.606  -44.312 -29.400 1.00 124.33 ? 163  HIS   E NE2 1 
ATOM   12655 N  N   . VAL   E 2 164 ? 33.609  -41.776 -35.863 1.00 108.14 ? 164  VAL   E N   1 
ATOM   12656 C  CA  . VAL   E 2 164 ? 33.871  -41.476 -37.260 1.00 104.29 ? 164  VAL   E CA  1 
ATOM   12657 C  C   . VAL   E 2 164 ? 34.302  -40.025 -37.411 1.00 100.33 ? 164  VAL   E C   1 
ATOM   12658 O  O   . VAL   E 2 164 ? 33.584  -39.108 -36.989 1.00 100.12 ? 164  VAL   E O   1 
ATOM   12659 C  CB  . VAL   E 2 164 ? 32.629  -41.749 -38.110 1.00 102.97 ? 164  VAL   E CB  1 
ATOM   12660 C  CG1 . VAL   E 2 164 ? 33.052  -41.924 -39.529 1.00 97.85  ? 164  VAL   E CG1 1 
ATOM   12661 C  CG2 . VAL   E 2 164 ? 31.909  -42.979 -37.556 1.00 108.88 ? 164  VAL   E CG2 1 
ATOM   12662 N  N   . ILE   E 2 165 ? 35.458  -39.820 -38.045 1.00 97.92  ? 165  ILE   E N   1 
ATOM   12663 C  CA  . ILE   E 2 165 ? 35.927  -38.473 -38.348 1.00 99.69  ? 165  ILE   E CA  1 
ATOM   12664 C  C   . ILE   E 2 165 ? 35.097  -37.855 -39.475 1.00 99.76  ? 165  ILE   E C   1 
ATOM   12665 O  O   . ILE   E 2 165 ? 34.439  -36.828 -39.280 1.00 103.54 ? 165  ILE   E O   1 
ATOM   12666 C  CB  . ILE   E 2 165 ? 37.436  -38.477 -38.679 1.00 101.04 ? 165  ILE   E CB  1 
ATOM   12667 C  CG1 . ILE   E 2 165 ? 38.279  -39.312 -37.677 1.00 102.01 ? 165  ILE   E CG1 1 
ATOM   12668 C  CG2 . ILE   E 2 165 ? 37.974  -37.055 -38.768 1.00 97.35  ? 165  ILE   E CG2 1 
ATOM   12669 C  CD1 . ILE   E 2 165 ? 37.847  -39.293 -36.228 1.00 104.74 ? 165  ILE   E CD1 1 
ATOM   12670 N  N   . ASP   E 2 166 ? 35.080  -38.488 -40.654 1.00 94.07  ? 166  ASP   E N   1 
ATOM   12671 C  CA  . ASP   E 2 166 ? 34.467  -37.889 -41.841 1.00 95.73  ? 166  ASP   E CA  1 
ATOM   12672 C  C   . ASP   E 2 166 ? 34.028  -38.959 -42.836 1.00 94.73  ? 166  ASP   E C   1 
ATOM   12673 O  O   . ASP   E 2 166 ? 34.808  -39.843 -43.187 1.00 93.56  ? 166  ASP   E O   1 
ATOM   12674 C  CB  . ASP   E 2 166 ? 35.451  -36.912 -42.516 1.00 100.65 ? 166  ASP   E CB  1 
ATOM   12675 C  CG  . ASP   E 2 166 ? 34.920  -36.315 -43.828 1.00 98.53  ? 166  ASP   E CG  1 
ATOM   12676 O  OD1 . ASP   E 2 166 ? 33.680  -36.247 -44.037 1.00 93.81  ? 166  ASP   E OD1 1 
ATOM   12677 O  OD2 . ASP   E 2 166 ? 35.774  -35.898 -44.647 1.00 99.57  ? 166  ASP   E OD2 1 
ATOM   12678 N  N   . VAL   E 2 167 ? 32.796  -38.848 -43.321 1.00 96.30  ? 167  VAL   E N   1 
ATOM   12679 C  CA  . VAL   E 2 167 ? 32.220  -39.816 -44.235 1.00 94.27  ? 167  VAL   E CA  1 
ATOM   12680 C  C   . VAL   E 2 167 ? 31.843  -39.105 -45.539 1.00 96.80  ? 167  VAL   E C   1 
ATOM   12681 O  O   . VAL   E 2 167 ? 31.785  -37.880 -45.619 1.00 99.95  ? 167  VAL   E O   1 
ATOM   12682 C  CB  . VAL   E 2 167 ? 31.010  -40.496 -43.583 1.00 90.95  ? 167  VAL   E CB  1 
ATOM   12683 C  CG1 . VAL   E 2 167 ? 30.101  -39.444 -43.015 1.00 79.74  ? 167  VAL   E CG1 1 
ATOM   12684 C  CG2 . VAL   E 2 167 ? 30.279  -41.396 -44.565 1.00 96.05  ? 167  VAL   E CG2 1 
ATOM   12685 N  N   . LYS   E 2 168 ? 31.608  -39.891 -46.576 1.00 98.40  ? 168  LYS   E N   1 
ATOM   12686 C  CA  . LYS   E 2 168 ? 31.209  -39.308 -47.841 1.00 97.25  ? 168  LYS   E CA  1 
ATOM   12687 C  C   . LYS   E 2 168 ? 30.946  -40.456 -48.799 1.00 99.98  ? 168  LYS   E C   1 
ATOM   12688 O  O   . LYS   E 2 168 ? 31.693  -41.443 -48.799 1.00 101.79 ? 168  LYS   E O   1 
ATOM   12689 C  CB  . LYS   E 2 168 ? 32.282  -38.344 -48.379 1.00 91.91  ? 168  LYS   E CB  1 
ATOM   12690 N  N   . PHE   E 2 169 ? 29.858  -40.372 -49.555 1.00 101.93 ? 169  PHE   E N   1 
ATOM   12691 C  CA  . PHE   E 2 169 ? 29.532  -41.379 -50.562 1.00 100.31 ? 169  PHE   E CA  1 
ATOM   12692 C  C   . PHE   E 2 169 ? 30.601  -41.440 -51.654 1.00 101.34 ? 169  PHE   E C   1 
ATOM   12693 O  O   . PHE   E 2 169 ? 31.188  -40.427 -52.041 1.00 98.42  ? 169  PHE   E O   1 
ATOM   12694 C  CB  . PHE   E 2 169 ? 28.186  -41.069 -51.214 1.00 99.81  ? 169  PHE   E CB  1 
ATOM   12695 C  CG  . PHE   E 2 169 ? 27.006  -41.554 -50.440 1.00 100.47 ? 169  PHE   E CG  1 
ATOM   12696 C  CD1 . PHE   E 2 169 ? 26.657  -42.883 -50.469 1.00 107.20 ? 169  PHE   E CD1 1 
ATOM   12697 C  CD2 . PHE   E 2 169 ? 26.222  -40.674 -49.711 1.00 104.38 ? 169  PHE   E CD2 1 
ATOM   12698 C  CE1 . PHE   E 2 169 ? 25.560  -43.338 -49.774 1.00 108.21 ? 169  PHE   E CE1 1 
ATOM   12699 C  CE2 . PHE   E 2 169 ? 25.121  -41.121 -49.017 1.00 104.61 ? 169  PHE   E CE2 1 
ATOM   12700 C  CZ  . PHE   E 2 169 ? 24.794  -42.458 -49.050 1.00 109.37 ? 169  PHE   E CZ  1 
ATOM   12701 N  N   . LEU   E 2 170 ? 30.805  -42.626 -52.208 1.00 105.70 ? 170  LEU   E N   1 
ATOM   12702 C  CA  . LEU   E 2 170 ? 31.839  -42.816 -53.208 1.00 102.28 ? 170  LEU   E CA  1 
ATOM   12703 C  C   . LEU   E 2 170 ? 31.267  -42.757 -54.615 1.00 99.33  ? 170  LEU   E C   1 
ATOM   12704 O  O   . LEU   E 2 170 ? 30.096  -43.066 -54.850 1.00 98.20  ? 170  LEU   E O   1 
ATOM   12705 C  CB  . LEU   E 2 170 ? 32.560  -44.138 -52.987 1.00 105.82 ? 170  LEU   E CB  1 
ATOM   12706 C  CG  . LEU   E 2 170 ? 33.905  -43.833 -52.343 1.00 107.13 ? 170  LEU   E CG  1 
ATOM   12707 C  CD1 . LEU   E 2 170 ? 34.658  -45.113 -52.026 1.00 100.32 ? 170  LEU   E CD1 1 
ATOM   12708 C  CD2 . LEU   E 2 170 ? 34.699  -42.911 -53.289 1.00 110.75 ? 170  LEU   E CD2 1 
ATOM   12709 N  N   . TYR   E 2 171 ? 32.109  -42.341 -55.551 1.00 102.53 ? 171  TYR   E N   1 
ATOM   12710 C  CA  . TYR   E 2 171 ? 31.698  -42.213 -56.936 1.00 107.82 ? 171  TYR   E CA  1 
ATOM   12711 C  C   . TYR   E 2 171 ? 31.943  -43.525 -57.684 1.00 115.83 ? 171  TYR   E C   1 
ATOM   12712 O  O   . TYR   E 2 171 ? 32.776  -44.349 -57.287 1.00 118.03 ? 171  TYR   E O   1 
ATOM   12713 C  CB  . TYR   E 2 171 ? 32.458  -41.064 -57.610 1.00 109.84 ? 171  TYR   E CB  1 
ATOM   12714 C  CG  . TYR   E 2 171 ? 31.849  -39.660 -57.489 1.00 107.75 ? 171  TYR   E CG  1 
ATOM   12715 C  CD1 . TYR   E 2 171 ? 30.629  -39.339 -58.087 1.00 109.23 ? 171  TYR   E CD1 1 
ATOM   12716 C  CD2 . TYR   E 2 171 ? 32.527  -38.639 -56.817 1.00 107.58 ? 171  TYR   E CD2 1 
ATOM   12717 C  CE1 . TYR   E 2 171 ? 30.096  -38.037 -57.996 1.00 114.80 ? 171  TYR   E CE1 1 
ATOM   12718 C  CE2 . TYR   E 2 171 ? 32.000  -37.338 -56.727 1.00 106.50 ? 171  TYR   E CE2 1 
ATOM   12719 C  CZ  . TYR   E 2 171 ? 30.787  -37.038 -57.314 1.00 106.84 ? 171  TYR   E CZ  1 
ATOM   12720 O  OH  . TYR   E 2 171 ? 30.273  -35.754 -57.217 1.00 83.92  ? 171  TYR   E OH  1 
ATOM   12721 N  N   . GLY   E 2 172 ? 31.186  -43.719 -58.764 1.00 108.48 ? 172  GLY   E N   1 
ATOM   12722 C  CA  . GLY   E 2 172 ? 31.369  -44.857 -59.641 1.00 122.43 ? 172  GLY   E CA  1 
ATOM   12723 C  C   . GLY   E 2 172 ? 31.429  -46.234 -58.995 1.00 132.17 ? 172  GLY   E C   1 
ATOM   12724 O  O   . GLY   E 2 172 ? 32.428  -46.953 -59.135 1.00 132.98 ? 172  GLY   E O   1 
ATOM   12725 N  N   . CYS   E 2 173 ? 30.352  -46.632 -58.313 1.00 133.27 ? 173  CYS   E N   1 
ATOM   12726 C  CA  . CYS   E 2 173 ? 30.280  -47.917 -57.629 1.00 131.04 ? 173  CYS   E CA  1 
ATOM   12727 C  C   . CYS   E 2 173 ? 28.934  -48.574 -57.941 1.00 129.50 ? 173  CYS   E C   1 
ATOM   12728 O  O   . CYS   E 2 173 ? 27.927  -47.886 -58.132 1.00 129.58 ? 173  CYS   E O   1 
ATOM   12729 C  CB  . CYS   E 2 173 ? 30.473  -47.733 -56.113 1.00 128.20 ? 173  CYS   E CB  1 
ATOM   12730 S  SG  . CYS   E 2 173 ? 32.211  -47.707 -55.536 1.00 133.61 ? 173  CYS   E SG  1 
ATOM   12731 N  N   . GLN   E 2 174 ? 28.927  -49.914 -58.008 1.00 126.56 ? 174  GLN   E N   1 
ATOM   12732 C  CA  . GLN   E 2 174 ? 27.706  -50.680 -58.289 1.00 124.40 ? 174  GLN   E CA  1 
ATOM   12733 C  C   . GLN   E 2 174 ? 26.462  -50.350 -57.467 1.00 124.12 ? 174  GLN   E C   1 
ATOM   12734 O  O   . GLN   E 2 174 ? 25.361  -50.176 -58.015 1.00 121.09 ? 174  GLN   E O   1 
ATOM   12735 C  CB  . GLN   E 2 174 ? 27.940  -52.170 -58.020 1.00 121.42 ? 174  GLN   E CB  1 
ATOM   12736 C  CG  . GLN   E 2 174 ? 28.638  -52.422 -56.664 1.00 126.20 ? 174  GLN   E CG  1 
ATOM   12737 C  CD  . GLN   E 2 174 ? 28.830  -53.902 -56.328 1.00 119.44 ? 174  GLN   E CD  1 
ATOM   12738 O  OE1 . GLN   E 2 174 ? 29.291  -54.687 -57.167 1.00 124.22 ? 174  GLN   E OE1 1 
ATOM   12739 N  NE2 . GLN   E 2 174 ? 28.477  -54.286 -55.106 1.00 113.69 ? 174  GLN   E NE2 1 
ATOM   12740 N  N   . ALA   E 2 175 ? 26.616  -50.296 -56.153 1.00 123.76 ? 175  ALA   E N   1 
ATOM   12741 C  CA  . ALA   E 2 175 ? 25.541  -49.921 -55.259 1.00 118.65 ? 175  ALA   E CA  1 
ATOM   12742 C  C   . ALA   E 2 175 ? 26.030  -48.689 -54.520 1.00 120.83 ? 175  ALA   E C   1 
ATOM   12743 O  O   . ALA   E 2 175 ? 27.202  -48.318 -54.611 1.00 120.94 ? 175  ALA   E O   1 
ATOM   12744 C  CB  . ALA   E 2 175 ? 25.155  -51.019 -54.273 1.00 116.64 ? 175  ALA   E CB  1 
ATOM   12745 N  N   . PRO   E 2 176 ? 25.147  -48.010 -53.790 1.00 117.67 ? 176  PRO   E N   1 
ATOM   12746 C  CA  . PRO   E 2 176 ? 25.587  -46.864 -52.989 1.00 114.70 ? 176  PRO   E CA  1 
ATOM   12747 C  C   . PRO   E 2 176 ? 26.571  -47.290 -51.912 1.00 113.60 ? 176  PRO   E C   1 
ATOM   12748 O  O   . PRO   E 2 176 ? 26.317  -48.229 -51.150 1.00 113.89 ? 176  PRO   E O   1 
ATOM   12749 C  CB  . PRO   E 2 176 ? 24.279  -46.337 -52.389 1.00 114.40 ? 176  PRO   E CB  1 
ATOM   12750 C  CG  . PRO   E 2 176 ? 23.243  -46.761 -53.373 1.00 115.80 ? 176  PRO   E CG  1 
ATOM   12751 C  CD  . PRO   E 2 176 ? 23.682  -48.134 -53.810 1.00 118.90 ? 176  PRO   E CD  1 
ATOM   12752 N  N   . THR   E 2 177 ? 27.691  -46.570 -51.841 1.00 110.24 ? 177  THR   E N   1 
ATOM   12753 C  CA  . THR   E 2 177 ? 28.800  -46.929 -50.966 1.00 111.68 ? 177  THR   E CA  1 
ATOM   12754 C  C   . THR   E 2 177 ? 29.385  -45.702 -50.276 1.00 111.35 ? 177  THR   E C   1 
ATOM   12755 O  O   . THR   E 2 177 ? 29.663  -44.680 -50.918 1.00 106.79 ? 177  THR   E O   1 
ATOM   12756 C  CB  . THR   E 2 177 ? 29.907  -47.637 -51.746 1.00 109.87 ? 177  THR   E CB  1 
ATOM   12757 O  OG1 . THR   E 2 177 ? 29.325  -48.438 -52.777 1.00 120.13 ? 177  THR   E OG1 1 
ATOM   12758 C  CG2 . THR   E 2 177 ? 30.706  -48.527 -50.810 1.00 114.17 ? 177  THR   E CG2 1 
ATOM   12759 N  N   . ILE   E 2 178 ? 29.611  -45.828 -48.975 1.00 110.13 ? 178  ILE   E N   1 
ATOM   12760 C  CA  . ILE   E 2 178 ? 30.188  -44.756 -48.209 1.00 107.29 ? 178  ILE   E CA  1 
ATOM   12761 C  C   . ILE   E 2 178 ? 31.649  -45.081 -47.930 1.00 107.67 ? 178  ILE   E C   1 
ATOM   12762 O  O   . ILE   E 2 178 ? 32.115  -46.214 -48.066 1.00 105.39 ? 178  ILE   E O   1 
ATOM   12763 C  CB  . ILE   E 2 178 ? 29.381  -44.489 -46.919 1.00 105.36 ? 178  ILE   E CB  1 
ATOM   12764 C  CG1 . ILE   E 2 178 ? 29.265  -45.737 -46.057 1.00 101.04 ? 178  ILE   E CG1 1 
ATOM   12765 C  CG2 . ILE   E 2 178 ? 27.986  -44.086 -47.311 1.00 102.99 ? 178  ILE   E CG2 1 
ATOM   12766 C  CD1 . ILE   E 2 178 ? 30.558  -46.222 -45.460 1.00 105.13 ? 178  ILE   E CD1 1 
ATOM   12767 N  N   . CYS   E 2 179 ? 32.391  -44.043 -47.577 1.00 106.72 ? 179  CYS   E N   1 
ATOM   12768 C  CA  . CYS   E 2 179 ? 33.809  -44.153 -47.296 1.00 101.90 ? 179  CYS   E CA  1 
ATOM   12769 C  C   . CYS   E 2 179 ? 34.066  -43.237 -46.123 1.00 100.08 ? 179  CYS   E C   1 
ATOM   12770 O  O   . CYS   E 2 179 ? 33.825  -42.028 -46.214 1.00 98.65  ? 179  CYS   E O   1 
ATOM   12771 C  CB  . CYS   E 2 179 ? 34.645  -43.753 -48.510 1.00 101.93 ? 179  CYS   E CB  1 
ATOM   12772 S  SG  . CYS   E 2 179 ? 36.406  -43.835 -48.205 1.00 100.05 ? 179  CYS   E SG  1 
ATOM   12773 N  N   . PHE   E 2 180 ? 34.507  -43.800 -45.018 1.00 99.75  ? 180  PHE   E N   1 
ATOM   12774 C  CA  . PHE   E 2 180 ? 34.676  -43.006 -43.819 1.00 96.39  ? 180  PHE   E CA  1 
ATOM   12775 C  C   . PHE   E 2 180 ? 36.034  -43.283 -43.197 1.00 97.91  ? 180  PHE   E C   1 
ATOM   12776 O  O   . PHE   E 2 180 ? 36.607  -44.362 -43.374 1.00 103.30 ? 180  PHE   E O   1 
ATOM   12777 C  CB  . PHE   E 2 180 ? 33.560  -43.290 -42.817 1.00 95.82  ? 180  PHE   E CB  1 
ATOM   12778 C  CG  . PHE   E 2 180 ? 33.577  -44.690 -42.274 1.00 99.73  ? 180  PHE   E CG  1 
ATOM   12779 C  CD1 . PHE   E 2 180 ? 34.446  -45.037 -41.244 1.00 102.98 ? 180  PHE   E CD1 1 
ATOM   12780 C  CD2 . PHE   E 2 180 ? 32.734  -45.655 -42.783 1.00 102.21 ? 180  PHE   E CD2 1 
ATOM   12781 C  CE1 . PHE   E 2 180 ? 34.471  -46.314 -40.727 1.00 105.98 ? 180  PHE   E CE1 1 
ATOM   12782 C  CE2 . PHE   E 2 180 ? 32.752  -46.946 -42.273 1.00 111.29 ? 180  PHE   E CE2 1 
ATOM   12783 C  CZ  . PHE   E 2 180 ? 33.623  -47.275 -41.240 1.00 115.60 ? 180  PHE   E CZ  1 
ATOM   12784 N  N   . VAL   E 2 181 ? 36.545  -42.285 -42.474 1.00 96.92  ? 181  VAL   E N   1 
ATOM   12785 C  CA  . VAL   E 2 181 ? 37.714  -42.413 -41.607 1.00 96.77  ? 181  VAL   E CA  1 
ATOM   12786 C  C   . VAL   E 2 181 ? 37.234  -42.550 -40.173 1.00 98.68  ? 181  VAL   E C   1 
ATOM   12787 O  O   . VAL   E 2 181 ? 36.305  -41.848 -39.760 1.00 103.10 ? 181  VAL   E O   1 
ATOM   12788 C  CB  . VAL   E 2 181 ? 38.643  -41.196 -41.749 1.00 93.30  ? 181  VAL   E CB  1 
ATOM   12789 C  CG1 . VAL   E 2 181 ? 39.521  -41.061 -40.518 1.00 92.15  ? 181  VAL   E CG1 1 
ATOM   12790 C  CG2 . VAL   E 2 181 ? 39.467  -41.293 -43.030 1.00 95.15  ? 181  VAL   E CG2 1 
ATOM   12791 N  N   . TYR   E 2 182 ? 37.857  -43.446 -39.407 1.00 100.31 ? 182  TYR   E N   1 
ATOM   12792 C  CA  . TYR   E 2 182 ? 37.466  -43.657 -38.020 1.00 102.08 ? 182  TYR   E CA  1 
ATOM   12793 C  C   . TYR   E 2 182 ? 38.698  -43.874 -37.165 1.00 105.07 ? 182  TYR   E C   1 
ATOM   12794 O  O   . TYR   E 2 182 ? 39.754  -44.300 -37.641 1.00 104.54 ? 182  TYR   E O   1 
ATOM   12795 C  CB  . TYR   E 2 182 ? 36.517  -44.854 -37.843 1.00 105.57 ? 182  TYR   E CB  1 
ATOM   12796 C  CG  . TYR   E 2 182 ? 37.096  -46.177 -38.291 1.00 107.65 ? 182  TYR   E CG  1 
ATOM   12797 C  CD1 . TYR   E 2 182 ? 37.497  -46.373 -39.608 1.00 106.21 ? 182  TYR   E CD1 1 
ATOM   12798 C  CD2 . TYR   E 2 182 ? 37.229  -47.233 -37.400 1.00 108.40 ? 182  TYR   E CD2 1 
ATOM   12799 C  CE1 . TYR   E 2 182 ? 38.021  -47.579 -40.015 1.00 106.42 ? 182  TYR   E CE1 1 
ATOM   12800 C  CE2 . TYR   E 2 182 ? 37.744  -48.435 -37.801 1.00 111.69 ? 182  TYR   E CE2 1 
ATOM   12801 C  CZ  . TYR   E 2 182 ? 38.140  -48.603 -39.101 1.00 108.61 ? 182  TYR   E CZ  1 
ATOM   12802 O  OH  . TYR   E 2 182 ? 38.658  -49.813 -39.473 1.00 121.28 ? 182  TYR   E OH  1 
ATOM   12803 N  N   . GLN   E 2 183 ? 38.534  -43.615 -35.878 1.00 109.90 ? 183  GLN   E N   1 
ATOM   12804 C  CA  . GLN   E 2 183 ? 39.580  -43.852 -34.906 1.00 109.52 ? 183  GLN   E CA  1 
ATOM   12805 C  C   . GLN   E 2 183 ? 39.079  -44.889 -33.922 1.00 111.56 ? 183  GLN   E C   1 
ATOM   12806 O  O   . GLN   E 2 183 ? 37.925  -44.831 -33.484 1.00 111.98 ? 183  GLN   E O   1 
ATOM   12807 C  CB  . GLN   E 2 183 ? 39.961  -42.558 -34.195 1.00 110.48 ? 183  GLN   E CB  1 
ATOM   12808 C  CG  . GLN   E 2 183 ? 41.109  -42.682 -33.224 1.00 113.99 ? 183  GLN   E CG  1 
ATOM   12809 C  CD  . GLN   E 2 183 ? 41.836  -41.368 -33.033 1.00 119.53 ? 183  GLN   E CD  1 
ATOM   12810 O  OE1 . GLN   E 2 183 ? 42.642  -40.953 -33.880 1.00 116.70 ? 183  GLN   E OE1 1 
ATOM   12811 N  NE2 . GLN   E 2 183 ? 41.545  -40.694 -31.925 1.00 127.52 ? 183  GLN   E NE2 1 
ATOM   12812 N  N   . ASP   E 2 184 ? 39.915  -45.868 -33.640 1.00 111.85 ? 184  ASP   E N   1 
ATOM   12813 C  CA  . ASP   E 2 184 ? 39.708  -46.809 -32.552 1.00 116.89 ? 184  ASP   E CA  1 
ATOM   12814 C  C   . ASP   E 2 184 ? 41.050  -46.947 -31.867 1.00 122.39 ? 184  ASP   E C   1 
ATOM   12815 O  O   . ASP   E 2 184 ? 42.062  -46.439 -32.363 1.00 122.56 ? 184  ASP   E O   1 
ATOM   12816 C  CB  . ASP   E 2 184 ? 39.183  -48.166 -33.049 1.00 111.72 ? 184  ASP   E CB  1 
ATOM   12817 C  CG  . ASP   E 2 184 ? 40.153  -48.862 -33.970 1.00 119.38 ? 184  ASP   E CG  1 
ATOM   12818 O  OD1 . ASP   E 2 184 ? 41.317  -48.421 -34.052 1.00 120.42 ? 184  ASP   E OD1 1 
ATOM   12819 O  OD2 . ASP   E 2 184 ? 39.749  -49.852 -34.619 1.00 126.79 ? 184  ASP   E OD2 1 
ATOM   12820 N  N   . PRO   E 2 185 ? 41.091  -47.610 -30.708 1.00 124.16 ? 185  PRO   E N   1 
ATOM   12821 C  CA  . PRO   E 2 185 ? 42.347  -47.766 -29.959 1.00 121.56 ? 185  PRO   E CA  1 
ATOM   12822 C  C   . PRO   E 2 185 ? 43.593  -47.984 -30.806 1.00 128.68 ? 185  PRO   E C   1 
ATOM   12823 O  O   . PRO   E 2 185 ? 44.636  -47.378 -30.528 1.00 125.02 ? 185  PRO   E O   1 
ATOM   12824 C  CB  . PRO   E 2 185 ? 42.055  -48.990 -29.095 1.00 116.41 ? 185  PRO   E CB  1 
ATOM   12825 C  CG  . PRO   E 2 185 ? 40.589  -48.855 -28.804 1.00 113.95 ? 185  PRO   E CG  1 
ATOM   12826 C  CD  . PRO   E 2 185 ? 39.953  -48.236 -30.012 1.00 119.74 ? 185  PRO   E CD  1 
ATOM   12827 N  N   . GLN   E 2 186 ? 43.482  -48.832 -31.840 1.00 136.72 ? 186  GLN   E N   1 
ATOM   12828 C  CA  . GLN   E 2 186 ? 44.639  -49.217 -32.651 1.00 136.31 ? 186  GLN   E CA  1 
ATOM   12829 C  C   . GLN   E 2 186 ? 45.241  -48.039 -33.410 1.00 135.20 ? 186  GLN   E C   1 
ATOM   12830 O  O   . GLN   E 2 186 ? 46.466  -47.958 -33.566 1.00 133.94 ? 186  GLN   E O   1 
ATOM   12831 C  CB  . GLN   E 2 186 ? 44.242  -50.299 -33.644 1.00 136.29 ? 186  GLN   E CB  1 
ATOM   12832 C  CG  . GLN   E 2 186 ? 43.871  -51.627 -33.046 1.00 141.26 ? 186  GLN   E CG  1 
ATOM   12833 C  CD  . GLN   E 2 186 ? 43.629  -52.665 -34.124 1.00 147.29 ? 186  GLN   E CD  1 
ATOM   12834 O  OE1 . GLN   E 2 186 ? 43.842  -52.406 -35.316 1.00 145.60 ? 186  GLN   E OE1 1 
ATOM   12835 N  NE2 . GLN   E 2 186 ? 43.182  -53.846 -33.715 1.00 152.08 ? 186  GLN   E NE2 1 
ATOM   12836 N  N   . GLY   E 2 187 ? 44.402  -47.150 -33.932 1.00 128.23 ? 187  GLY   E N   1 
ATOM   12837 C  CA  . GLY   E 2 187 ? 44.893  -46.014 -34.703 1.00 122.57 ? 187  GLY   E CA  1 
ATOM   12838 C  C   . GLY   E 2 187 ? 43.772  -45.405 -35.534 1.00 115.61 ? 187  GLY   E C   1 
ATOM   12839 O  O   . GLY   E 2 187 ? 42.591  -45.516 -35.186 1.00 112.16 ? 187  GLY   E O   1 
ATOM   12840 N  N   . ARG   E 2 188 ? 44.178  -44.758 -36.625 1.00 111.73 ? 188  ARG   E N   1 
ATOM   12841 C  CA  . ARG   E 2 188 ? 43.269  -44.193 -37.619 1.00 112.31 ? 188  ARG   E CA  1 
ATOM   12842 C  C   . ARG   E 2 188 ? 43.332  -45.024 -38.903 1.00 116.60 ? 188  ARG   E C   1 
ATOM   12843 O  O   . ARG   E 2 188 ? 44.421  -45.278 -39.430 1.00 120.87 ? 188  ARG   E O   1 
ATOM   12844 C  CB  . ARG   E 2 188 ? 43.629  -42.730 -37.931 1.00 112.68 ? 188  ARG   E CB  1 
ATOM   12845 N  N   . HIS   E 2 189 ? 42.165  -45.419 -39.428 1.00 113.47 ? 189  HIS   E N   1 
ATOM   12846 C  CA  . HIS   E 2 189 ? 42.087  -46.232 -40.642 1.00 116.07 ? 189  HIS   E CA  1 
ATOM   12847 C  C   . HIS   E 2 189 ? 40.943  -45.722 -41.518 1.00 110.11 ? 189  HIS   E C   1 
ATOM   12848 O  O   . HIS   E 2 189 ? 40.223  -44.791 -41.147 1.00 105.81 ? 189  HIS   E O   1 
ATOM   12849 C  CB  . HIS   E 2 189 ? 41.899  -47.716 -40.290 1.00 116.59 ? 189  HIS   E CB  1 
ATOM   12850 C  CG  . HIS   E 2 189 ? 42.381  -48.067 -38.920 1.00 114.18 ? 189  HIS   E CG  1 
ATOM   12851 N  ND1 . HIS   E 2 189 ? 43.718  -48.071 -38.584 1.00 119.56 ? 189  HIS   E ND1 1 
ATOM   12852 C  CD2 . HIS   E 2 189 ? 41.706  -48.404 -37.796 1.00 112.22 ? 189  HIS   E CD2 1 
ATOM   12853 C  CE1 . HIS   E 2 189 ? 43.848  -48.408 -37.314 1.00 122.39 ? 189  HIS   E CE1 1 
ATOM   12854 N  NE2 . HIS   E 2 189 ? 42.642  -48.615 -36.813 1.00 122.49 ? 189  HIS   E NE2 1 
ATOM   12855 N  N   . VAL   E 2 190 ? 40.774  -46.348 -42.691 1.00 109.41 ? 190  VAL   E N   1 
ATOM   12856 C  CA  . VAL   E 2 190 ? 39.665  -46.067 -43.599 1.00 104.89 ? 190  VAL   E CA  1 
ATOM   12857 C  C   . VAL   E 2 190 ? 38.918  -47.369 -43.869 1.00 107.75 ? 190  VAL   E C   1 
ATOM   12858 O  O   . VAL   E 2 190 ? 39.546  -48.422 -44.029 1.00 109.77 ? 190  VAL   E O   1 
ATOM   12859 C  CB  . VAL   E 2 190 ? 40.154  -45.414 -44.915 1.00 103.87 ? 190  VAL   E CB  1 
ATOM   12860 C  CG1 . VAL   E 2 190 ? 41.232  -46.255 -45.578 1.00 109.62 ? 190  VAL   E CG1 1 
ATOM   12861 C  CG2 . VAL   E 2 190 ? 38.994  -45.179 -45.873 1.00 102.86 ? 190  VAL   E CG2 1 
ATOM   12862 N  N   . LYS   E 2 191 ? 37.576  -47.299 -43.889 1.00 109.19 ? 191  LYS   E N   1 
ATOM   12863 C  CA  . LYS   E 2 191 ? 36.700  -48.431 -44.203 1.00 107.10 ? 191  LYS   E CA  1 
ATOM   12864 C  C   . LYS   E 2 191 ? 35.523  -47.957 -45.055 1.00 109.60 ? 191  LYS   E C   1 
ATOM   12865 O  O   . LYS   E 2 191 ? 35.116  -46.789 -44.997 1.00 108.00 ? 191  LYS   E O   1 
ATOM   12866 C  CB  . LYS   E 2 191 ? 36.173  -49.136 -42.934 1.00 93.21  ? 191  LYS   E CB  1 
ATOM   12867 N  N   . THR   E 2 192 ? 34.980  -48.875 -45.859 1.00 110.74 ? 192  THR   E N   1 
ATOM   12868 C  CA  . THR   E 2 192 ? 33.826  -48.599 -46.706 1.00 106.72 ? 192  THR   E CA  1 
ATOM   12869 C  C   . THR   E 2 192 ? 32.765  -49.664 -46.474 1.00 110.16 ? 192  THR   E C   1 
ATOM   12870 O  O   . THR   E 2 192 ? 33.085  -50.835 -46.254 1.00 116.44 ? 192  THR   E O   1 
ATOM   12871 C  CB  . THR   E 2 192 ? 34.181  -48.612 -48.179 1.00 107.99 ? 192  THR   E CB  1 
ATOM   12872 O  OG1 . THR   E 2 192 ? 34.086  -49.959 -48.658 1.00 111.66 ? 192  THR   E OG1 1 
ATOM   12873 C  CG2 . THR   E 2 192 ? 35.601  -48.106 -48.406 1.00 113.18 ? 192  THR   E CG2 1 
ATOM   12874 N  N   . TYR   E 2 193 ? 31.501  -49.246 -46.535 1.00 110.03 ? 193  TYR   E N   1 
ATOM   12875 C  CA  . TYR   E 2 193 ? 30.353  -50.130 -46.406 1.00 112.62 ? 193  TYR   E CA  1 
ATOM   12876 C  C   . TYR   E 2 193 ? 29.399  -49.834 -47.546 1.00 114.73 ? 193  TYR   E C   1 
ATOM   12877 O  O   . TYR   E 2 193 ? 29.430  -48.749 -48.134 1.00 115.45 ? 193  TYR   E O   1 
ATOM   12878 C  CB  . TYR   E 2 193 ? 29.618  -49.956 -45.059 1.00 110.91 ? 193  TYR   E CB  1 
ATOM   12879 C  CG  . TYR   E 2 193 ? 30.333  -50.554 -43.858 1.00 109.88 ? 193  TYR   E CG  1 
ATOM   12880 C  CD1 . TYR   E 2 193 ? 31.226  -51.598 -44.014 1.00 113.93 ? 193  TYR   E CD1 1 
ATOM   12881 C  CD2 . TYR   E 2 193 ? 30.128  -50.064 -42.572 1.00 111.70 ? 193  TYR   E CD2 1 
ATOM   12882 C  CE1 . TYR   E 2 193 ? 31.881  -52.143 -42.925 1.00 116.21 ? 193  TYR   E CE1 1 
ATOM   12883 C  CE2 . TYR   E 2 193 ? 30.766  -50.607 -41.474 1.00 110.83 ? 193  TYR   E CE2 1 
ATOM   12884 C  CZ  . TYR   E 2 193 ? 31.649  -51.644 -41.658 1.00 112.97 ? 193  TYR   E CZ  1 
ATOM   12885 O  OH  . TYR   E 2 193 ? 32.314  -52.200 -40.589 1.00 111.15 ? 193  TYR   E OH  1 
ATOM   12886 N  N   . GLU   E 2 194 ? 28.545  -50.804 -47.851 1.00 125.46 ? 194  GLU   E N   1 
ATOM   12887 C  CA  . GLU   E 2 194 ? 27.541  -50.662 -48.894 1.00 128.07 ? 194  GLU   E CA  1 
ATOM   12888 C  C   . GLU   E 2 194 ? 26.158  -50.508 -48.270 1.00 127.65 ? 194  GLU   E C   1 
ATOM   12889 O  O   . GLU   E 2 194 ? 25.911  -50.960 -47.148 1.00 125.53 ? 194  GLU   E O   1 
ATOM   12890 C  CB  . GLU   E 2 194 ? 27.560  -51.860 -49.843 1.00 129.86 ? 194  GLU   E CB  1 
ATOM   12891 C  CG  . GLU   E 2 194 ? 28.547  -51.715 -50.992 1.00 130.22 ? 194  GLU   E CG  1 
ATOM   12892 C  CD  . GLU   E 2 194 ? 28.334  -52.760 -52.080 1.00 135.87 ? 194  GLU   E CD  1 
ATOM   12893 O  OE1 . GLU   E 2 194 ? 29.105  -52.747 -53.071 1.00 139.95 ? 194  GLU   E OE1 1 
ATOM   12894 O  OE2 . GLU   E 2 194 ? 27.402  -53.592 -51.937 1.00 139.82 ? 194  GLU   E OE2 1 
ATOM   12895 N  N   . VAL   E 2 195 ? 25.253  -49.865 -49.001 1.00 119.65 ? 195  VAL   E N   1 
ATOM   12896 C  CA  . VAL   E 2 195 ? 23.977  -49.435 -48.442 1.00 119.75 ? 195  VAL   E CA  1 
ATOM   12897 C  C   . VAL   E 2 195 ? 22.847  -50.048 -49.252 1.00 119.94 ? 195  VAL   E C   1 
ATOM   12898 O  O   . VAL   E 2 195 ? 22.729  -49.792 -50.460 1.00 117.57 ? 195  VAL   E O   1 
ATOM   12899 C  CB  . VAL   E 2 195 ? 23.866  -47.907 -48.414 1.00 115.80 ? 195  VAL   E CB  1 
ATOM   12900 C  CG1 . VAL   E 2 195 ? 22.412  -47.501 -48.533 1.00 114.82 ? 195  VAL   E CG1 1 
ATOM   12901 C  CG2 . VAL   E 2 195 ? 24.494  -47.378 -47.136 1.00 111.89 ? 195  VAL   E CG2 1 
ATOM   12902 N  N   . SER   E 2 196 ? 22.013  -50.848 -48.583 1.00 118.63 ? 196  SER   E N   1 
ATOM   12903 C  CA  . SER   E 2 196 ? 20.878  -51.524 -49.205 1.00 124.17 ? 196  SER   E CA  1 
ATOM   12904 C  C   . SER   E 2 196 ? 19.583  -50.945 -48.649 1.00 121.47 ? 196  SER   E C   1 
ATOM   12905 O  O   . SER   E 2 196 ? 19.202  -51.237 -47.509 1.00 121.19 ? 196  SER   E O   1 
ATOM   12906 C  CB  . SER   E 2 196 ? 20.937  -53.037 -48.979 1.00 129.72 ? 196  SER   E CB  1 
ATOM   12907 O  OG  . SER   E 2 196 ? 19.773  -53.681 -49.490 1.00 132.47 ? 196  SER   E OG  1 
ATOM   12908 N  N   . LEU   E 2 197 ? 18.897  -50.148 -49.472 1.00 116.51 ? 197  LEU   E N   1 
ATOM   12909 C  CA  . LEU   E 2 197 ? 17.541  -49.713 -49.161 1.00 118.23 ? 197  LEU   E CA  1 
ATOM   12910 C  C   . LEU   E 2 197 ? 16.513  -50.843 -49.234 1.00 125.57 ? 197  LEU   E C   1 
ATOM   12911 O  O   . LEU   E 2 197 ? 15.363  -50.625 -48.832 1.00 124.95 ? 197  LEU   E O   1 
ATOM   12912 C  CB  . LEU   E 2 197 ? 17.136  -48.582 -50.105 1.00 117.05 ? 197  LEU   E CB  1 
ATOM   12913 C  CG  . LEU   E 2 197 ? 18.256  -47.623 -50.517 1.00 121.18 ? 197  LEU   E CG  1 
ATOM   12914 C  CD1 . LEU   E 2 197 ? 17.691  -46.421 -51.245 1.00 120.50 ? 197  LEU   E CD1 1 
ATOM   12915 C  CD2 . LEU   E 2 197 ? 19.087  -47.168 -49.323 1.00 119.10 ? 197  LEU   E CD2 1 
ATOM   12916 N  N   . ARG   E 2 198 ? 16.889  -52.027 -49.743 1.00 129.69 ? 198  ARG   E N   1 
ATOM   12917 C  CA  . ARG   E 2 198 ? 15.985  -53.173 -49.766 1.00 123.22 ? 198  ARG   E CA  1 
ATOM   12918 C  C   . ARG   E 2 198 ? 16.022  -53.926 -48.441 1.00 125.26 ? 198  ARG   E C   1 
ATOM   12919 O  O   . ARG   E 2 198 ? 15.005  -54.032 -47.749 1.00 122.53 ? 198  ARG   E O   1 
ATOM   12920 C  CB  . ARG   E 2 198 ? 16.333  -54.097 -50.935 1.00 125.87 ? 198  ARG   E CB  1 
ATOM   12921 N  N   . GLU   E 2 199 ? 17.185  -54.450 -48.067 1.00 141.60 ? 199  GLU   E N   1 
ATOM   12922 C  CA  . GLU   E 2 199 ? 17.353  -55.022 -46.736 1.00 145.69 ? 199  GLU   E CA  1 
ATOM   12923 C  C   . GLU   E 2 199 ? 17.588  -53.950 -45.672 1.00 142.92 ? 199  GLU   E C   1 
ATOM   12924 O  O   . GLU   E 2 199 ? 17.868  -54.292 -44.515 1.00 141.97 ? 199  GLU   E O   1 
ATOM   12925 C  CB  . GLU   E 2 199 ? 18.509  -56.033 -46.722 1.00 149.53 ? 199  GLU   E CB  1 
ATOM   12926 C  CG  . GLU   E 2 199 ? 19.900  -55.389 -46.610 1.00 150.11 ? 199  GLU   E CG  1 
ATOM   12927 C  CD  . GLU   E 2 199 ? 21.011  -56.413 -46.406 1.00 151.61 ? 199  GLU   E CD  1 
ATOM   12928 O  OE1 . GLU   E 2 199 ? 21.239  -56.831 -45.242 1.00 149.73 ? 199  GLU   E OE1 1 
ATOM   12929 O  OE2 . GLU   E 2 199 ? 21.632  -56.815 -47.423 1.00 153.33 ? 199  GLU   E OE2 1 
ATOM   12930 N  N   . LYS   E 2 200 ? 17.474  -52.672 -46.051 1.00 134.49 ? 200  LYS   E N   1 
ATOM   12931 C  CA  . LYS   E 2 200 ? 17.688  -51.532 -45.166 1.00 125.46 ? 200  LYS   E CA  1 
ATOM   12932 C  C   . LYS   E 2 200 ? 18.791  -51.808 -44.147 1.00 125.16 ? 200  LYS   E C   1 
ATOM   12933 O  O   . LYS   E 2 200 ? 18.608  -51.544 -42.956 1.00 123.72 ? 200  LYS   E O   1 
ATOM   12934 C  CB  . LYS   E 2 200 ? 16.378  -51.145 -44.464 1.00 112.61 ? 200  LYS   E CB  1 
ATOM   12935 N  N   . GLU   E 2 201 ? 19.908  -52.349 -44.640 1.00 121.40 ? 201  GLU   E N   1 
ATOM   12936 C  CA  . GLU   E 2 201 ? 21.047  -52.685 -43.751 1.00 124.56 ? 201  GLU   E CA  1 
ATOM   12937 C  C   . GLU   E 2 201 ? 22.364  -52.489 -44.509 1.00 124.47 ? 201  GLU   E C   1 
ATOM   12938 O  O   . GLU   E 2 201 ? 22.314  -52.192 -45.718 1.00 125.13 ? 201  GLU   E O   1 
ATOM   12939 C  CB  . GLU   E 2 201 ? 20.951  -54.133 -43.282 1.00 131.02 ? 201  GLU   E CB  1 
ATOM   12940 C  CG  . GLU   E 2 201 ? 19.741  -54.419 -42.397 1.00 135.65 ? 201  GLU   E CG  1 
ATOM   12941 C  CD  . GLU   E 2 201 ? 19.634  -53.590 -41.131 1.00 130.86 ? 201  GLU   E CD  1 
ATOM   12942 O  OE1 . GLU   E 2 201 ? 20.678  -53.354 -40.488 1.00 126.96 ? 201  GLU   E OE1 1 
ATOM   12943 O  OE2 . GLU   E 2 201 ? 18.505  -53.165 -40.803 1.00 130.59 ? 201  GLU   E OE2 1 
ATOM   12944 N  N   . PHE   E 2 202 ? 23.492  -52.667 -43.822 1.00 122.78 ? 202  PHE   E N   1 
ATOM   12945 C  CA  . PHE   E 2 202 ? 24.819  -52.425 -44.444 1.00 122.15 ? 202  PHE   E CA  1 
ATOM   12946 C  C   . PHE   E 2 202 ? 25.353  -53.701 -45.063 1.00 126.10 ? 202  PHE   E C   1 
ATOM   12947 O  O   . PHE   E 2 202 ? 24.923  -54.798 -44.657 1.00 131.92 ? 202  PHE   E O   1 
ATOM   12948 C  CB  . PHE   E 2 202 ? 25.810  -51.973 -43.370 1.00 119.88 ? 202  PHE   E CB  1 
ATOM   12949 C  CG  . PHE   E 2 202 ? 25.511  -50.647 -42.686 1.00 123.81 ? 202  PHE   E CG  1 
ATOM   12950 C  CD1 . PHE   E 2 202 ? 25.887  -49.447 -43.274 1.00 125.58 ? 202  PHE   E CD1 1 
ATOM   12951 C  CD2 . PHE   E 2 202 ? 24.854  -50.601 -41.466 1.00 131.32 ? 202  PHE   E CD2 1 
ATOM   12952 C  CE1 . PHE   E 2 202 ? 25.615  -48.238 -42.654 1.00 114.95 ? 202  PHE   E CE1 1 
ATOM   12953 C  CE2 . PHE   E 2 202 ? 24.582  -49.391 -40.852 1.00 115.49 ? 202  PHE   E CE2 1 
ATOM   12954 C  CZ  . PHE   E 2 202 ? 24.964  -48.213 -41.445 1.00 113.88 ? 202  PHE   E CZ  1 
ATOM   12955 N  N   . ASN   E 2 203 ? 26.282  -53.566 -46.010 1.00 127.37 ? 203  ASN   E N   1 
ATOM   12956 C  CA  . ASN   E 2 203 ? 26.926  -54.750 -46.640 1.00 123.87 ? 203  ASN   E CA  1 
ATOM   12957 C  C   . ASN   E 2 203 ? 28.414  -54.439 -46.804 1.00 123.63 ? 203  ASN   E C   1 
ATOM   12958 O  O   . ASN   E 2 203 ? 28.766  -53.245 -46.797 1.00 124.33 ? 203  ASN   E O   1 
ATOM   12959 C  CB  . ASN   E 2 203 ? 26.259  -55.125 -47.958 1.00 121.01 ? 203  ASN   E CB  1 
ATOM   12960 C  CG  . ASN   E 2 203 ? 24.889  -55.725 -47.757 1.00 123.47 ? 203  ASN   E CG  1 
ATOM   12961 O  OD1 . ASN   E 2 203 ? 24.741  -56.703 -47.017 1.00 124.18 ? 203  ASN   E OD1 1 
ATOM   12962 N  ND2 . ASN   E 2 203 ? 23.879  -55.156 -48.397 1.00 124.50 ? 203  ASN   E ND2 1 
ATOM   12963 N  N   . LYS   E 2 204 ? 29.253  -55.464 -46.950 1.00 125.07 ? 204  LYS   E N   1 
ATOM   12964 C  CA  . LYS   E 2 204 ? 30.721  -55.248 -47.021 1.00 120.70 ? 204  LYS   E CA  1 
ATOM   12965 C  C   . LYS   E 2 204 ? 31.060  -54.284 -48.160 1.00 120.72 ? 204  LYS   E C   1 
ATOM   12966 O  O   . LYS   E 2 204 ? 30.438  -54.385 -49.235 1.00 120.81 ? 204  LYS   E O   1 
ATOM   12967 C  CB  . LYS   E 2 204 ? 31.453  -56.573 -47.248 1.00 112.83 ? 204  LYS   E CB  1 
ATOM   12968 N  N   . GLY   E 2 205 ? 32.033  -53.403 -47.933 1.00 117.53 ? 205  GLY   E N   1 
ATOM   12969 C  CA  . GLY   E 2 205 ? 32.407  -52.467 -48.966 1.00 114.73 ? 205  GLY   E CA  1 
ATOM   12970 C  C   . GLY   E 2 205 ? 33.597  -52.936 -49.788 1.00 114.09 ? 205  GLY   E C   1 
ATOM   12971 O  O   . GLY   E 2 205 ? 34.305  -53.894 -49.440 1.00 118.79 ? 205  GLY   E O   1 
ATOM   12972 N  N   . PRO   E 2 206 ? 33.846  -52.244 -50.903 1.00 115.33 ? 206  PRO   E N   1 
ATOM   12973 C  CA  . PRO   E 2 206 ? 34.883  -52.717 -51.844 1.00 115.16 ? 206  PRO   E CA  1 
ATOM   12974 C  C   . PRO   E 2 206 ? 36.320  -52.724 -51.314 1.00 119.09 ? 206  PRO   E C   1 
ATOM   12975 O  O   . PRO   E 2 206 ? 37.098  -53.565 -51.789 1.00 118.62 ? 206  PRO   E O   1 
ATOM   12976 C  CB  . PRO   E 2 206 ? 34.732  -51.763 -53.039 1.00 112.51 ? 206  PRO   E CB  1 
ATOM   12977 C  CG  . PRO   E 2 206 ? 33.732  -50.736 -52.643 1.00 112.74 ? 206  PRO   E CG  1 
ATOM   12978 C  CD  . PRO   E 2 206 ? 32.913  -51.296 -51.537 1.00 113.83 ? 206  PRO   E CD  1 
ATOM   12979 N  N   . TRP   E 2 207 ? 36.722  -51.840 -50.378 1.00 118.43 ? 207  TRP   E N   1 
ATOM   12980 C  CA  . TRP   E 2 207 ? 38.121  -51.818 -49.928 1.00 119.89 ? 207  TRP   E CA  1 
ATOM   12981 C  C   . TRP   E 2 207 ? 38.267  -51.188 -48.535 1.00 117.42 ? 207  TRP   E C   1 
ATOM   12982 O  O   . TRP   E 2 207 ? 37.297  -50.734 -47.920 1.00 117.58 ? 207  TRP   E O   1 
ATOM   12983 C  CB  . TRP   E 2 207 ? 39.031  -51.097 -50.935 1.00 123.30 ? 207  TRP   E CB  1 
ATOM   12984 C  CG  . TRP   E 2 207 ? 38.492  -49.811 -51.526 1.00 121.65 ? 207  TRP   E CG  1 
ATOM   12985 C  CD1 . TRP   E 2 207 ? 37.844  -49.671 -52.723 1.00 119.09 ? 207  TRP   E CD1 1 
ATOM   12986 C  CD2 . TRP   E 2 207 ? 38.583  -48.489 -50.961 1.00 122.72 ? 207  TRP   E CD2 1 
ATOM   12987 N  NE1 . TRP   E 2 207 ? 37.520  -48.352 -52.931 1.00 122.22 ? 207  TRP   E NE1 1 
ATOM   12988 C  CE2 . TRP   E 2 207 ? 37.959  -47.607 -51.865 1.00 120.85 ? 207  TRP   E CE2 1 
ATOM   12989 C  CE3 . TRP   E 2 207 ? 39.127  -47.971 -49.778 1.00 118.37 ? 207  TRP   E CE3 1 
ATOM   12990 C  CZ2 . TRP   E 2 207 ? 37.859  -46.236 -51.621 1.00 114.81 ? 207  TRP   E CZ2 1 
ATOM   12991 C  CZ3 . TRP   E 2 207 ? 39.033  -46.611 -49.543 1.00 115.07 ? 207  TRP   E CZ3 1 
ATOM   12992 C  CH2 . TRP   E 2 207 ? 38.402  -45.760 -50.461 1.00 113.97 ? 207  TRP   E CH2 1 
ATOM   12993 N  N   . LYS   E 2 208 ? 39.511  -51.181 -48.037 1.00 117.90 ? 208  LYS   E N   1 
ATOM   12994 C  CA  . LYS   E 2 208 ? 39.877  -50.593 -46.745 1.00 117.99 ? 208  LYS   E CA  1 
ATOM   12995 C  C   . LYS   E 2 208 ? 41.393  -50.402 -46.694 1.00 118.36 ? 208  LYS   E C   1 
ATOM   12996 O  O   . LYS   E 2 208 ? 42.125  -50.861 -47.577 1.00 117.02 ? 208  LYS   E O   1 
ATOM   12997 C  CB  . LYS   E 2 208 ? 39.385  -51.455 -45.570 1.00 113.34 ? 208  LYS   E CB  1 
ATOM   12998 C  CG  . LYS   E 2 208 ? 39.636  -52.940 -45.740 1.00 113.12 ? 208  LYS   E CG  1 
ATOM   12999 C  CD  . LYS   E 2 208 ? 39.633  -53.644 -44.405 1.00 112.85 ? 208  LYS   E CD  1 
ATOM   13000 C  CE  . LYS   E 2 208 ? 41.056  -53.858 -43.893 1.00 115.42 ? 208  LYS   E CE  1 
ATOM   13001 N  NZ  . LYS   E 2 208 ? 41.074  -54.500 -42.543 1.00 115.87 ? 208  LYS   E NZ  1 
ATOM   13002 N  N   . GLN   E 2 209 ? 41.854  -49.703 -45.654 1.00 114.73 ? 209  GLN   E N   1 
ATOM   13003 C  CA  . GLN   E 2 209 ? 43.284  -49.448 -45.463 1.00 120.67 ? 209  GLN   E CA  1 
ATOM   13004 C  C   . GLN   E 2 209 ? 43.537  -49.351 -43.968 1.00 121.41 ? 209  GLN   E C   1 
ATOM   13005 O  O   . GLN   E 2 209 ? 43.129  -48.381 -43.324 1.00 118.41 ? 209  GLN   E O   1 
ATOM   13006 C  CB  . GLN   E 2 209 ? 43.750  -48.180 -46.187 1.00 118.00 ? 209  GLN   E CB  1 
ATOM   13007 N  N   . GLU   E 2 210 ? 44.213  -50.358 -43.420 1.00 125.30 ? 210  GLU   E N   1 
ATOM   13008 C  CA  . GLU   E 2 210 ? 44.206  -50.570 -41.980 1.00 123.91 ? 210  GLU   E CA  1 
ATOM   13009 C  C   . GLU   E 2 210 ? 44.942  -49.480 -41.207 1.00 129.70 ? 210  GLU   E C   1 
ATOM   13010 O  O   . GLU   E 2 210 ? 44.792  -49.422 -39.985 1.00 132.44 ? 210  GLU   E O   1 
ATOM   13011 C  CB  . GLU   E 2 210 ? 44.789  -51.952 -41.652 1.00 125.64 ? 210  GLU   E CB  1 
ATOM   13012 N  N   . ASN   E 2 211 ? 45.713  -48.606 -41.854 1.00 135.79 ? 211  ASN   E N   1 
ATOM   13013 C  CA  . ASN   E 2 211 ? 46.358  -47.557 -41.069 1.00 133.82 ? 211  ASN   E CA  1 
ATOM   13014 C  C   . ASN   E 2 211 ? 46.716  -46.374 -41.942 1.00 136.38 ? 211  ASN   E C   1 
ATOM   13015 O  O   . ASN   E 2 211 ? 47.260  -46.553 -43.034 1.00 144.17 ? 211  ASN   E O   1 
ATOM   13016 C  CB  . ASN   E 2 211 ? 47.613  -48.073 -40.375 1.00 137.46 ? 211  ASN   E CB  1 
ATOM   13017 C  CG  . ASN   E 2 211 ? 47.352  -48.444 -38.945 1.00 141.50 ? 211  ASN   E CG  1 
ATOM   13018 O  OD1 . ASN   E 2 211 ? 47.674  -47.688 -38.033 1.00 143.72 ? 211  ASN   E OD1 1 
ATOM   13019 N  ND2 . ASN   E 2 211 ? 46.727  -49.596 -38.735 1.00 142.24 ? 211  ASN   E ND2 1 
ATOM   13020 N  N   . VAL   E 2 212 ? 46.442  -45.167 -41.438 1.00 126.69 ? 212  VAL   E N   1 
ATOM   13021 C  CA  . VAL   E 2 212 ? 46.710  -43.930 -42.174 1.00 126.62 ? 212  VAL   E CA  1 
ATOM   13022 C  C   . VAL   E 2 212 ? 47.109  -42.843 -41.176 1.00 122.22 ? 212  VAL   E C   1 
ATOM   13023 O  O   . VAL   E 2 212 ? 47.189  -43.096 -39.968 1.00 120.85 ? 212  VAL   E O   1 
ATOM   13024 C  CB  . VAL   E 2 212 ? 45.490  -43.532 -43.042 1.00 124.77 ? 212  VAL   E CB  1 
ATOM   13025 C  CG1 . VAL   E 2 212 ? 44.352  -42.971 -42.192 1.00 118.65 ? 212  VAL   E CG1 1 
ATOM   13026 C  CG2 . VAL   E 2 212 ? 45.887  -42.576 -44.198 1.00 119.87 ? 212  VAL   E CG2 1 
ATOM   13027 N  N   . GLU   E 2 213 ? 47.393  -41.631 -41.672 1.00 118.31 ? 213  GLU   E N   1 
ATOM   13028 C  CA  . GLU   E 2 213 ? 47.860  -40.548 -40.800 1.00 120.73 ? 213  GLU   E CA  1 
ATOM   13029 C  C   . GLU   E 2 213 ? 46.912  -40.354 -39.618 1.00 116.24 ? 213  GLU   E C   1 
ATOM   13030 O  O   . GLU   E 2 213 ? 45.712  -40.125 -39.798 1.00 116.08 ? 213  GLU   E O   1 
ATOM   13031 C  CB  . GLU   E 2 213 ? 48.004  -39.239 -41.592 1.00 118.29 ? 213  GLU   E CB  1 
ATOM   13032 N  N   . ALA   E 2 214 ? 47.462  -40.427 -38.406 1.00 114.63 ? 214  ALA   E N   1 
ATOM   13033 C  CA  . ALA   E 2 214 ? 46.682  -40.234 -37.189 1.00 118.59 ? 214  ALA   E CA  1 
ATOM   13034 C  C   . ALA   E 2 214 ? 46.019  -38.862 -37.165 1.00 117.56 ? 214  ALA   E C   1 
ATOM   13035 O  O   . ALA   E 2 214 ? 45.109  -38.617 -36.361 1.00 117.65 ? 214  ALA   E O   1 
ATOM   13036 C  CB  . ALA   E 2 214 ? 47.560  -40.425 -35.947 1.00 119.07 ? 214  ALA   E CB  1 
ATOM   13037 N  N   . GLU   E 2 215 ? 46.470  -37.962 -38.043 1.00 118.08 ? 215  GLU   E N   1 
ATOM   13038 C  CA  . GLU   E 2 215 ? 45.885  -36.639 -38.216 1.00 117.41 ? 215  GLU   E CA  1 
ATOM   13039 C  C   . GLU   E 2 215 ? 45.027  -36.561 -39.469 1.00 113.87 ? 215  GLU   E C   1 
ATOM   13040 O  O   . GLU   E 2 215 ? 45.003  -35.526 -40.142 1.00 115.85 ? 215  GLU   E O   1 
ATOM   13041 C  CB  . GLU   E 2 215 ? 46.967  -35.558 -38.262 1.00 119.69 ? 215  GLU   E CB  1 
ATOM   13042 C  CG  . GLU   E 2 215 ? 47.448  -35.093 -36.892 1.00 120.64 ? 215  GLU   E CG  1 
ATOM   13043 C  CD  . GLU   E 2 215 ? 46.371  -35.197 -35.815 1.00 121.20 ? 215  GLU   E CD  1 
ATOM   13044 O  OE1 . GLU   E 2 215 ? 45.196  -34.844 -36.081 1.00 120.54 ? 215  GLU   E OE1 1 
ATOM   13045 O  OE2 . GLU   E 2 215 ? 46.709  -35.643 -34.694 1.00 123.08 ? 215  GLU   E OE2 1 
ATOM   13046 N  N   . ALA   E 2 216 ? 44.315  -37.629 -39.804 1.00 110.74 ? 216  ALA   E N   1 
ATOM   13047 C  CA  . ALA   E 2 216 ? 43.539  -37.647 -41.036 1.00 109.24 ? 216  ALA   E CA  1 
ATOM   13048 C  C   . ALA   E 2 216 ? 42.112  -37.188 -40.753 1.00 104.86 ? 216  ALA   E C   1 
ATOM   13049 O  O   . ALA   E 2 216 ? 41.463  -37.696 -39.827 1.00 98.28  ? 216  ALA   E O   1 
ATOM   13050 C  CB  . ALA   E 2 216 ? 43.561  -39.043 -41.661 1.00 106.09 ? 216  ALA   E CB  1 
ATOM   13051 N  N   . SER   E 2 217 ? 41.629  -36.215 -41.550 1.00 99.87  ? 217  SER   E N   1 
ATOM   13052 C  CA  . SER   E 2 217 ? 40.311  -35.638 -41.291 1.00 98.27  ? 217  SER   E CA  1 
ATOM   13053 C  C   . SER   E 2 217 ? 39.449  -35.358 -42.520 1.00 96.03  ? 217  SER   E C   1 
ATOM   13054 O  O   . SER   E 2 217 ? 38.272  -35.048 -42.341 1.00 103.15 ? 217  SER   E O   1 
ATOM   13055 C  CB  . SER   E 2 217 ? 40.453  -34.335 -40.477 1.00 100.57 ? 217  SER   E CB  1 
ATOM   13056 O  OG  . SER   E 2 217 ? 41.149  -33.337 -41.204 1.00 102.60 ? 217  SER   E OG  1 
ATOM   13057 N  N   . MET   E 2 218 ? 39.954  -35.456 -43.746 1.00 94.15  ? 218  MET   E N   1 
ATOM   13058 C  CA  . MET   E 2 218 ? 39.149  -35.174 -44.931 1.00 99.49  ? 218  MET   E CA  1 
ATOM   13059 C  C   . MET   E 2 218 ? 38.955  -36.408 -45.812 1.00 103.63 ? 218  MET   E C   1 
ATOM   13060 O  O   . MET   E 2 218 ? 39.926  -37.057 -46.225 1.00 94.83  ? 218  MET   E O   1 
ATOM   13061 C  CB  . MET   E 2 218 ? 39.773  -34.064 -45.776 1.00 103.89 ? 218  MET   E CB  1 
ATOM   13062 C  CG  . MET   E 2 218 ? 39.690  -32.682 -45.180 1.00 104.64 ? 218  MET   E CG  1 
ATOM   13063 S  SD  . MET   E 2 218 ? 39.344  -31.444 -46.461 1.00 108.04 ? 218  MET   E SD  1 
ATOM   13064 C  CE  . MET   E 2 218 ? 40.238  -32.140 -47.850 1.00 97.53  ? 218  MET   E CE  1 
ATOM   13065 N  N   . VAL   E 2 219 ? 37.696  -36.678 -46.149 1.00 107.50 ? 219  VAL   E N   1 
ATOM   13066 C  CA  . VAL   E 2 219 ? 37.311  -37.666 -47.148 1.00 108.53 ? 219  VAL   E CA  1 
ATOM   13067 C  C   . VAL   E 2 219 ? 36.856  -36.934 -48.400 1.00 107.61 ? 219  VAL   E C   1 
ATOM   13068 O  O   . VAL   E 2 219 ? 35.833  -36.233 -48.384 1.00 106.73 ? 219  VAL   E O   1 
ATOM   13069 C  CB  . VAL   E 2 219 ? 36.187  -38.575 -46.640 1.00 108.03 ? 219  VAL   E CB  1 
ATOM   13070 C  CG1 . VAL   E 2 219 ? 35.367  -39.109 -47.831 1.00 108.41 ? 219  VAL   E CG1 1 
ATOM   13071 C  CG2 . VAL   E 2 219 ? 36.762  -39.691 -45.815 1.00 108.53 ? 219  VAL   E CG2 1 
ATOM   13072 N  N   . ILE   E 2 220 ? 37.586  -37.117 -49.492 1.00 101.28 ? 220  ILE   E N   1 
ATOM   13073 C  CA  . ILE   E 2 220 ? 37.219  -36.515 -50.760 1.00 101.52 ? 220  ILE   E CA  1 
ATOM   13074 C  C   . ILE   E 2 220 ? 36.870  -37.635 -51.716 1.00 107.77 ? 220  ILE   E C   1 
ATOM   13075 O  O   . ILE   E 2 220 ? 37.708  -38.499 -51.995 1.00 112.41 ? 220  ILE   E O   1 
ATOM   13076 C  CB  . ILE   E 2 220 ? 38.347  -35.654 -51.340 1.00 102.87 ? 220  ILE   E CB  1 
ATOM   13077 C  CG1 . ILE   E 2 220 ? 38.648  -34.458 -50.456 1.00 100.73 ? 220  ILE   E CG1 1 
ATOM   13078 C  CG2 . ILE   E 2 220 ? 37.969  -35.165 -52.726 1.00 105.77 ? 220  ILE   E CG2 1 
ATOM   13079 C  CD1 . ILE   E 2 220 ? 39.772  -33.638 -51.029 1.00 95.08  ? 220  ILE   E CD1 1 
ATOM   13080 N  N   . ALA   E 2 221 ? 35.654  -37.606 -52.251 1.00 108.30 ? 221  ALA   E N   1 
ATOM   13081 C  CA  . ALA   E 2 221 ? 35.212  -38.620 -53.203 1.00 100.62 ? 221  ALA   E CA  1 
ATOM   13082 C  C   . ALA   E 2 221 ? 35.606  -38.197 -54.613 1.00 104.37 ? 221  ALA   E C   1 
ATOM   13083 O  O   . ALA   E 2 221 ? 35.026  -37.258 -55.160 1.00 111.81 ? 221  ALA   E O   1 
ATOM   13084 C  CB  . ALA   E 2 221 ? 33.704  -38.818 -53.099 1.00 95.23  ? 221  ALA   E CB  1 
ATOM   13085 N  N   . VAL   E 2 222 ? 36.571  -38.892 -55.212 1.00 108.01 ? 222  VAL   E N   1 
ATOM   13086 C  CA  . VAL   E 2 222 ? 36.959  -38.566 -56.594 1.00 110.53 ? 222  VAL   E CA  1 
ATOM   13087 C  C   . VAL   E 2 222 ? 35.832  -38.972 -57.543 1.00 112.71 ? 222  VAL   E C   1 
ATOM   13088 O  O   . VAL   E 2 222 ? 35.241  -40.057 -57.372 1.00 112.78 ? 222  VAL   E O   1 
ATOM   13089 C  CB  . VAL   E 2 222 ? 38.275  -39.254 -56.968 1.00 111.72 ? 222  VAL   E CB  1 
ATOM   13090 C  CG1 . VAL   E 2 222 ? 38.534  -39.118 -58.483 1.00 113.74 ? 222  VAL   E CG1 1 
ATOM   13091 C  CG2 . VAL   E 2 222 ? 39.427  -38.653 -56.178 1.00 105.79 ? 222  VAL   E CG2 1 
ATOM   13092 N  N   . PRO   E 2 223 ? 35.492  -38.150 -58.542 1.00 117.41 ? 223  PRO   E N   1 
ATOM   13093 C  CA  . PRO   E 2 223 ? 34.333  -38.445 -59.396 1.00 120.76 ? 223  PRO   E CA  1 
ATOM   13094 C  C   . PRO   E 2 223 ? 34.665  -39.523 -60.416 1.00 128.46 ? 223  PRO   E C   1 
ATOM   13095 O  O   . PRO   E 2 223 ? 35.812  -39.926 -60.593 1.00 123.13 ? 223  PRO   E O   1 
ATOM   13096 C  CB  . PRO   E 2 223 ? 34.032  -37.097 -60.059 1.00 117.49 ? 223  PRO   E CB  1 
ATOM   13097 C  CG  . PRO   E 2 223 ? 35.329  -36.402 -60.098 1.00 120.45 ? 223  PRO   E CG  1 
ATOM   13098 C  CD  . PRO   E 2 223 ? 36.083  -36.829 -58.845 1.00 117.44 ? 223  PRO   E CD  1 
ATOM   13099 N  N   . GLU   E 2 224 ? 33.613  -39.966 -61.121 1.00 142.66 ? 224  GLU   E N   1 
ATOM   13100 C  CA  . GLU   E 2 224 ? 33.609  -41.202 -61.904 1.00 145.78 ? 224  GLU   E CA  1 
ATOM   13101 C  C   . GLU   E 2 224 ? 34.892  -41.509 -62.651 1.00 146.66 ? 224  GLU   E C   1 
ATOM   13102 O  O   . GLU   E 2 224 ? 35.363  -42.657 -62.572 1.00 145.35 ? 224  GLU   E O   1 
ATOM   13103 C  CB  . GLU   E 2 224 ? 32.451  -41.192 -62.906 1.00 147.48 ? 224  GLU   E CB  1 
ATOM   13104 C  CG  . GLU   E 2 224 ? 31.111  -41.359 -62.239 1.00 150.06 ? 224  GLU   E CG  1 
ATOM   13105 C  CD  . GLU   E 2 224 ? 30.312  -40.064 -62.103 1.00 155.85 ? 224  GLU   E CD  1 
ATOM   13106 O  OE1 . GLU   E 2 224 ? 29.139  -40.141 -61.675 1.00 157.32 ? 224  GLU   E OE1 1 
ATOM   13107 O  OE2 . GLU   E 2 224 ? 30.855  -38.974 -62.426 1.00 155.03 ? 224  GLU   E OE2 1 
ATOM   13108 N  N   . PRO   E 2 225 ? 35.491  -40.580 -63.379 1.00 138.45 ? 225  PRO   E N   1 
ATOM   13109 C  CA  . PRO   E 2 225 ? 36.724  -40.913 -64.112 1.00 137.20 ? 225  PRO   E CA  1 
ATOM   13110 C  C   . PRO   E 2 225 ? 37.683  -41.825 -63.338 1.00 133.51 ? 225  PRO   E C   1 
ATOM   13111 O  O   . PRO   E 2 225 ? 37.786  -43.019 -63.632 1.00 127.18 ? 225  PRO   E O   1 
ATOM   13112 C  CB  . PRO   E 2 225 ? 37.349  -39.533 -64.378 1.00 138.21 ? 225  PRO   E CB  1 
ATOM   13113 C  CG  . PRO   E 2 225 ? 36.160  -38.566 -64.412 1.00 135.75 ? 225  PRO   E CG  1 
ATOM   13114 C  CD  . PRO   E 2 225 ? 35.105  -39.161 -63.521 1.00 133.17 ? 225  PRO   E CD  1 
ATOM   13115 N  N   . PHE   E 2 226 ? 38.379  -41.280 -62.328 1.00 133.93 ? 226  PHE   E N   1 
ATOM   13116 C  CA  . PHE   E 2 226 ? 39.362  -42.023 -61.539 1.00 123.71 ? 226  PHE   E CA  1 
ATOM   13117 C  C   . PHE   E 2 226 ? 38.761  -42.726 -60.325 1.00 123.67 ? 226  PHE   E C   1 
ATOM   13118 O  O   . PHE   E 2 226 ? 39.373  -43.667 -59.808 1.00 123.38 ? 226  PHE   E O   1 
ATOM   13119 C  CB  . PHE   E 2 226 ? 40.475  -41.076 -61.063 1.00 119.65 ? 226  PHE   E CB  1 
ATOM   13120 N  N   . GLY   E 2 227 ? 37.607  -42.274 -59.828 1.00 127.65 ? 227  GLY   E N   1 
ATOM   13121 C  CA  . GLY   E 2 227 ? 36.982  -42.896 -58.681 1.00 122.19 ? 227  GLY   E CA  1 
ATOM   13122 C  C   . GLY   E 2 227 ? 37.814  -42.979 -57.412 1.00 114.25 ? 227  GLY   E C   1 
ATOM   13123 O  O   . GLY   E 2 227 ? 38.986  -42.601 -57.397 1.00 111.08 ? 227  GLY   E O   1 
ATOM   13124 N  N   . GLY   E 2 228 ? 37.219  -43.472 -56.363 1.00 116.37 ? 228  GLY   E N   1 
ATOM   13125 C  CA  . GLY   E 2 228 ? 38.009  -43.615 -55.168 1.00 119.60 ? 228  GLY   E CA  1 
ATOM   13126 C  C   . GLY   E 2 228 ? 37.910  -42.381 -54.297 1.00 118.49 ? 228  GLY   E C   1 
ATOM   13127 O  O   . GLY   E 2 228 ? 37.050  -41.508 -54.492 1.00 116.74 ? 228  GLY   E O   1 
ATOM   13128 N  N   . ALA   E 2 229 ? 38.830  -42.316 -53.322 1.00 112.91 ? 229  ALA   E N   1 
ATOM   13129 C  CA  . ALA   E 2 229 ? 38.779  -41.356 -52.230 1.00 109.10 ? 229  ALA   E CA  1 
ATOM   13130 C  C   . ALA   E 2 229 ? 40.170  -40.790 -51.943 1.00 113.09 ? 229  ALA   E C   1 
ATOM   13131 O  O   . ALA   E 2 229 ? 41.171  -41.515 -51.979 1.00 105.37 ? 229  ALA   E O   1 
ATOM   13132 C  CB  . ALA   E 2 229 ? 38.198  -42.011 -50.974 1.00 105.72 ? 229  ALA   E CB  1 
ATOM   13133 N  N   . ILE   E 2 230 ? 40.214  -39.477 -51.685 1.00 112.22 ? 230  ILE   E N   1 
ATOM   13134 C  CA  . ILE   E 2 230 ? 41.423  -38.753 -51.291 1.00 107.40 ? 230  ILE   E CA  1 
ATOM   13135 C  C   . ILE   E 2 230 ? 41.335  -38.472 -49.800 1.00 105.82 ? 230  ILE   E C   1 
ATOM   13136 O  O   . ILE   E 2 230 ? 40.377  -37.837 -49.339 1.00 104.11 ? 230  ILE   E O   1 
ATOM   13137 C  CB  . ILE   E 2 230 ? 41.584  -37.435 -52.067 1.00 106.75 ? 230  ILE   E CB  1 
ATOM   13138 C  CG1 . ILE   E 2 230 ? 41.829  -37.686 -53.558 1.00 109.33 ? 230  ILE   E CG1 1 
ATOM   13139 C  CG2 . ILE   E 2 230 ? 42.730  -36.607 -51.487 1.00 105.89 ? 230  ILE   E CG2 1 
ATOM   13140 C  CD1 . ILE   E 2 230 ? 43.302  -37.660 -53.967 1.00 111.11 ? 230  ILE   E CD1 1 
ATOM   13141 N  N   . ILE   E 2 231 ? 42.336  -38.933 -49.050 1.00 108.95 ? 231  ILE   E N   1 
ATOM   13142 C  CA  . ILE   E 2 231 ? 42.394  -38.766 -47.602 1.00 105.13 ? 231  ILE   E CA  1 
ATOM   13143 C  C   . ILE   E 2 231 ? 43.518  -37.794 -47.288 1.00 107.26 ? 231  ILE   E C   1 
ATOM   13144 O  O   . ILE   E 2 231 ? 44.687  -38.048 -47.621 1.00 103.96 ? 231  ILE   E O   1 
ATOM   13145 C  CB  . ILE   E 2 231 ? 42.606  -40.101 -46.878 1.00 101.19 ? 231  ILE   E CB  1 
ATOM   13146 C  CG1 . ILE   E 2 231 ? 41.539  -41.110 -47.300 1.00 102.78 ? 231  ILE   E CG1 1 
ATOM   13147 C  CG2 . ILE   E 2 231 ? 42.565  -39.894 -45.387 1.00 94.68  ? 231  ILE   E CG2 1 
ATOM   13148 C  CD1 . ILE   E 2 231 ? 40.192  -40.858 -46.708 1.00 96.13  ? 231  ILE   E CD1 1 
ATOM   13149 N  N   . ILE   E 2 232 ? 43.161  -36.698 -46.613 1.00 107.68 ? 232  ILE   E N   1 
ATOM   13150 C  CA  . ILE   E 2 232 ? 44.064  -35.590 -46.303 1.00 106.14 ? 232  ILE   E CA  1 
ATOM   13151 C  C   . ILE   E 2 232 ? 44.282  -35.525 -44.792 1.00 101.55 ? 232  ILE   E C   1 
ATOM   13152 O  O   . ILE   E 2 232 ? 43.327  -35.391 -44.016 1.00 99.65  ? 232  ILE   E O   1 
ATOM   13153 C  CB  . ILE   E 2 232 ? 43.520  -34.264 -46.855 1.00 101.50 ? 232  ILE   E CB  1 
ATOM   13154 C  CG1 . ILE   E 2 232 ? 43.759  -34.210 -48.366 1.00 100.32 ? 232  ILE   E CG1 1 
ATOM   13155 C  CG2 . ILE   E 2 232 ? 44.128  -33.066 -46.125 1.00 101.08 ? 232  ILE   E CG2 1 
ATOM   13156 C  CD1 . ILE   E 2 232 ? 42.719  -33.436 -49.136 1.00 101.62 ? 232  ILE   E CD1 1 
ATOM   13157 N  N   . GLY   E 2 233 ? 45.542  -35.646 -44.382 1.00 105.16 ? 233  GLY   E N   1 
ATOM   13158 C  CA  . GLY   E 2 233 ? 45.945  -35.540 -42.994 1.00 109.44 ? 233  GLY   E CA  1 
ATOM   13159 C  C   . GLY   E 2 233 ? 46.906  -34.388 -42.810 1.00 111.19 ? 233  GLY   E C   1 
ATOM   13160 O  O   . GLY   E 2 233 ? 47.094  -33.594 -43.734 1.00 113.03 ? 233  GLY   E O   1 
ATOM   13161 N  N   . GLN   E 2 234 ? 47.536  -34.273 -41.641 1.00 113.30 ? 234  GLN   E N   1 
ATOM   13162 C  CA  . GLN   E 2 234 ? 48.271  -33.046 -41.367 1.00 112.24 ? 234  GLN   E CA  1 
ATOM   13163 C  C   . GLN   E 2 234 ? 49.517  -32.932 -42.237 1.00 115.26 ? 234  GLN   E C   1 
ATOM   13164 O  O   . GLN   E 2 234 ? 49.862  -31.830 -42.690 1.00 117.66 ? 234  GLN   E O   1 
ATOM   13165 C  CB  . GLN   E 2 234 ? 48.601  -32.957 -39.883 1.00 114.87 ? 234  GLN   E CB  1 
ATOM   13166 C  CG  . GLN   E 2 234 ? 47.387  -32.541 -39.071 1.00 116.73 ? 234  GLN   E CG  1 
ATOM   13167 C  CD  . GLN   E 2 234 ? 47.746  -31.605 -37.931 1.00 119.66 ? 234  GLN   E CD  1 
ATOM   13168 O  OE1 . GLN   E 2 234 ? 46.949  -30.751 -37.533 1.00 116.39 ? 234  GLN   E OE1 1 
ATOM   13169 N  NE2 . GLN   E 2 234 ? 48.957  -31.766 -37.393 1.00 120.10 ? 234  GLN   E NE2 1 
ATOM   13170 N  N   . GLU   E 2 235 ? 50.184  -34.047 -42.517 1.00 117.31 ? 235  GLU   E N   1 
ATOM   13171 C  CA  . GLU   E 2 235 ? 51.394  -34.009 -43.329 1.00 117.44 ? 235  GLU   E CA  1 
ATOM   13172 C  C   . GLU   E 2 235 ? 51.288  -34.810 -44.620 1.00 118.68 ? 235  GLU   E C   1 
ATOM   13173 O  O   . GLU   E 2 235 ? 52.197  -34.729 -45.465 1.00 118.79 ? 235  GLU   E O   1 
ATOM   13174 C  CB  . GLU   E 2 235 ? 52.600  -34.513 -42.512 1.00 110.50 ? 235  GLU   E CB  1 
ATOM   13175 N  N   . SER   E 2 236 ? 50.201  -35.549 -44.816 1.00 116.19 ? 236  SER   E N   1 
ATOM   13176 C  CA  . SER   E 2 236 ? 50.140  -36.567 -45.853 1.00 115.58 ? 236  SER   E CA  1 
ATOM   13177 C  C   . SER   E 2 236 ? 48.811  -36.498 -46.575 1.00 113.74 ? 236  SER   E C   1 
ATOM   13178 O  O   . SER   E 2 236 ? 47.756  -36.504 -45.937 1.00 114.16 ? 236  SER   E O   1 
ATOM   13179 C  CB  . SER   E 2 236 ? 50.277  -37.949 -45.231 1.00 121.28 ? 236  SER   E CB  1 
ATOM   13180 O  OG  . SER   E 2 236 ? 49.316  -38.051 -44.194 1.00 124.01 ? 236  SER   E OG  1 
ATOM   13181 N  N   . ILE   E 2 237 ? 48.866  -36.466 -47.897 1.00 116.13 ? 237  ILE   E N   1 
ATOM   13182 C  CA  . ILE   E 2 237 ? 47.699  -36.641 -48.756 1.00 118.43 ? 237  ILE   E CA  1 
ATOM   13183 C  C   . ILE   E 2 237 ? 47.829  -38.002 -49.435 1.00 117.31 ? 237  ILE   E C   1 
ATOM   13184 O  O   . ILE   E 2 237 ? 48.787  -38.241 -50.178 1.00 115.20 ? 237  ILE   E O   1 
ATOM   13185 C  CB  . ILE   E 2 237 ? 47.584  -35.518 -49.802 1.00 119.14 ? 237  ILE   E CB  1 
ATOM   13186 C  CG1 . ILE   E 2 237 ? 47.005  -34.251 -49.190 1.00 115.28 ? 237  ILE   E CG1 1 
ATOM   13187 C  CG2 . ILE   E 2 237 ? 46.698  -35.927 -50.981 1.00 117.25 ? 237  ILE   E CG2 1 
ATOM   13188 C  CD1 . ILE   E 2 237 ? 46.849  -33.170 -50.215 1.00 116.88 ? 237  ILE   E CD1 1 
ATOM   13189 N  N   . THR   E 2 238 ? 46.883  -38.900 -49.185 1.00 118.67 ? 238  THR   E N   1 
ATOM   13190 C  CA  . THR   E 2 238 ? 46.928  -40.229 -49.782 1.00 121.90 ? 238  THR   E CA  1 
ATOM   13191 C  C   . THR   E 2 238 ? 45.677  -40.458 -50.629 1.00 120.21 ? 238  THR   E C   1 
ATOM   13192 O  O   . THR   E 2 238 ? 44.572  -40.062 -50.245 1.00 118.47 ? 238  THR   E O   1 
ATOM   13193 C  CB  . THR   E 2 238 ? 47.093  -41.349 -48.707 1.00 124.04 ? 238  THR   E CB  1 
ATOM   13194 O  OG1 . THR   E 2 238 ? 46.008  -41.312 -47.768 1.00 124.46 ? 238  THR   E OG1 1 
ATOM   13195 C  CG2 . THR   E 2 238 ? 48.404  -41.186 -47.939 1.00 126.36 ? 238  THR   E CG2 1 
ATOM   13196 N  N   . TYR   E 2 239 ? 45.865  -41.048 -51.805 1.00 122.27 ? 239  TYR   E N   1 
ATOM   13197 C  CA  . TYR   E 2 239 ? 44.771  -41.580 -52.614 1.00 119.60 ? 239  TYR   E CA  1 
ATOM   13198 C  C   . TYR   E 2 239 ? 44.632  -43.091 -52.378 1.00 119.81 ? 239  TYR   E C   1 
ATOM   13199 O  O   . TYR   E 2 239 ? 45.636  -43.788 -52.176 1.00 117.87 ? 239  TYR   E O   1 
ATOM   13200 C  CB  . TYR   E 2 239 ? 45.013  -41.259 -54.096 1.00 111.06 ? 239  TYR   E CB  1 
ATOM   13201 C  CG  . TYR   E 2 239 ? 44.071  -41.903 -55.110 1.00 113.81 ? 239  TYR   E CG  1 
ATOM   13202 C  CD1 . TYR   E 2 239 ? 42.757  -42.238 -54.777 1.00 118.70 ? 239  TYR   E CD1 1 
ATOM   13203 C  CD2 . TYR   E 2 239 ? 44.508  -42.167 -56.419 1.00 110.45 ? 239  TYR   E CD2 1 
ATOM   13204 C  CE1 . TYR   E 2 239 ? 41.919  -42.815 -55.708 1.00 113.55 ? 239  TYR   E CE1 1 
ATOM   13205 C  CE2 . TYR   E 2 239 ? 43.663  -42.769 -57.377 1.00 105.01 ? 239  TYR   E CE2 1 
ATOM   13206 C  CZ  . TYR   E 2 239 ? 42.358  -43.092 -56.989 1.00 107.21 ? 239  TYR   E CZ  1 
ATOM   13207 O  OH  . TYR   E 2 239 ? 41.418  -43.667 -57.806 1.00 116.23 ? 239  TYR   E OH  1 
ATOM   13208 N  N   . HIS   E 2 240 ? 43.375  -43.564 -52.320 1.00 116.72 ? 240  HIS   E N   1 
ATOM   13209 C  CA  . HIS   E 2 240 ? 42.988  -44.964 -52.119 1.00 116.13 ? 240  HIS   E CA  1 
ATOM   13210 C  C   . HIS   E 2 240 ? 41.930  -45.365 -53.138 1.00 117.78 ? 240  HIS   E C   1 
ATOM   13211 O  O   . HIS   E 2 240 ? 40.910  -44.681 -53.273 1.00 118.21 ? 240  HIS   E O   1 
ATOM   13212 C  CB  . HIS   E 2 240 ? 42.427  -45.209 -50.715 1.00 116.17 ? 240  HIS   E CB  1 
ATOM   13213 C  CG  . HIS   E 2 240 ? 43.361  -44.787 -49.637 1.00 115.15 ? 240  HIS   E CG  1 
ATOM   13214 N  ND1 . HIS   E 2 240 ? 44.104  -45.673 -48.880 1.00 121.17 ? 240  HIS   E ND1 1 
ATOM   13215 C  CD2 . HIS   E 2 240 ? 43.743  -43.550 -49.257 1.00 115.14 ? 240  HIS   E CD2 1 
ATOM   13216 C  CE1 . HIS   E 2 240 ? 44.877  -44.992 -48.050 1.00 122.47 ? 240  HIS   E CE1 1 
ATOM   13217 N  NE2 . HIS   E 2 240 ? 44.677  -43.702 -48.263 1.00 123.42 ? 240  HIS   E NE2 1 
ATOM   13218 N  N   . ASN   E 2 241 ? 42.161  -46.487 -53.837 1.00 122.78 ? 241  ASN   E N   1 
ATOM   13219 C  CA  . ASN   E 2 241 ? 41.151  -47.056 -54.746 1.00 123.40 ? 241  ASN   E CA  1 
ATOM   13220 C  C   . ASN   E 2 241 ? 41.484  -48.534 -55.000 1.00 131.17 ? 241  ASN   E C   1 
ATOM   13221 O  O   . ASN   E 2 241 ? 42.167  -48.857 -55.973 1.00 137.32 ? 241  ASN   E O   1 
ATOM   13222 C  CB  . ASN   E 2 241 ? 41.075  -46.283 -56.048 1.00 118.34 ? 241  ASN   E CB  1 
ATOM   13223 C  CG  . ASN   E 2 241 ? 39.765  -46.533 -56.810 1.00 117.04 ? 241  ASN   E CG  1 
ATOM   13224 O  OD1 . ASN   E 2 241 ? 38.947  -47.375 -56.430 1.00 116.08 ? 241  ASN   E OD1 1 
ATOM   13225 N  ND2 . ASN   E 2 241 ? 39.572  -45.796 -57.892 1.00 116.31 ? 241  ASN   E ND2 1 
ATOM   13226 N  N   . GLY   E 2 242 ? 40.958  -49.413 -54.139 1.00 136.95 ? 242  GLY   E N   1 
ATOM   13227 C  CA  . GLY   E 2 242 ? 41.131  -50.838 -54.335 1.00 138.26 ? 242  GLY   E CA  1 
ATOM   13228 C  C   . GLY   E 2 242 ? 42.613  -51.196 -54.309 1.00 144.71 ? 242  GLY   E C   1 
ATOM   13229 O  O   . GLY   E 2 242 ? 43.314  -50.991 -53.300 1.00 143.38 ? 242  GLY   E O   1 
ATOM   13230 N  N   . ASP   E 2 243 ? 43.110  -51.738 -55.427 1.00 141.55 ? 243  ASP   E N   1 
ATOM   13231 C  CA  . ASP   E 2 243 ? 44.529  -52.085 -55.515 1.00 144.08 ? 243  ASP   E CA  1 
ATOM   13232 C  C   . ASP   E 2 243 ? 45.415  -50.840 -55.466 1.00 145.95 ? 243  ASP   E C   1 
ATOM   13233 O  O   . ASP   E 2 243 ? 46.559  -50.916 -55.005 1.00 148.40 ? 243  ASP   E O   1 
ATOM   13234 C  CB  . ASP   E 2 243 ? 44.794  -52.881 -56.799 1.00 143.53 ? 243  ASP   E CB  1 
ATOM   13235 N  N   . LYS   E 2 244 ? 44.899  -49.688 -55.906 1.00 145.43 ? 244  LYS   E N   1 
ATOM   13236 C  CA  . LYS   E 2 244 ? 45.698  -48.474 -55.985 1.00 138.39 ? 244  LYS   E CA  1 
ATOM   13237 C  C   . LYS   E 2 244 ? 45.823  -47.792 -54.622 1.00 134.05 ? 244  LYS   E C   1 
ATOM   13238 O  O   . LYS   E 2 244 ? 44.891  -47.808 -53.810 1.00 127.85 ? 244  LYS   E O   1 
ATOM   13239 C  CB  . LYS   E 2 244 ? 45.099  -47.499 -57.010 1.00 121.45 ? 244  LYS   E CB  1 
ATOM   13240 N  N   . TYR   E 2 245 ? 47.003  -47.212 -54.367 1.00 131.91 ? 245  TYR   E N   1 
ATOM   13241 C  CA  . TYR   E 2 245 ? 47.260  -46.419 -53.154 1.00 130.42 ? 245  TYR   E CA  1 
ATOM   13242 C  C   . TYR   E 2 245 ? 48.517  -45.589 -53.404 1.00 131.87 ? 245  TYR   E C   1 
ATOM   13243 O  O   . TYR   E 2 245 ? 49.625  -46.140 -53.422 1.00 135.04 ? 245  TYR   E O   1 
ATOM   13244 C  CB  . TYR   E 2 245 ? 47.422  -47.316 -51.926 1.00 130.54 ? 245  TYR   E CB  1 
ATOM   13245 C  CG  . TYR   E 2 245 ? 48.369  -46.768 -50.865 1.00 130.99 ? 245  TYR   E CG  1 
ATOM   13246 C  CD1 . TYR   E 2 245 ? 47.936  -45.852 -49.912 1.00 130.93 ? 245  TYR   E CD1 1 
ATOM   13247 C  CD2 . TYR   E 2 245 ? 49.698  -47.181 -50.814 1.00 136.50 ? 245  TYR   E CD2 1 
ATOM   13248 C  CE1 . TYR   E 2 245 ? 48.803  -45.354 -48.935 1.00 132.63 ? 245  TYR   E CE1 1 
ATOM   13249 C  CE2 . TYR   E 2 245 ? 50.572  -46.692 -49.846 1.00 141.12 ? 245  TYR   E CE2 1 
ATOM   13250 C  CZ  . TYR   E 2 245 ? 50.124  -45.776 -48.907 1.00 139.60 ? 245  TYR   E CZ  1 
ATOM   13251 O  OH  . TYR   E 2 245 ? 50.991  -45.291 -47.944 1.00 136.32 ? 245  TYR   E OH  1 
ATOM   13252 N  N   . LEU   E 2 246 ? 48.339  -44.287 -53.640 1.00 130.55 ? 246  LEU   E N   1 
ATOM   13253 C  CA  . LEU   E 2 246 ? 49.430  -43.327 -53.787 1.00 123.63 ? 246  LEU   E CA  1 
ATOM   13254 C  C   . LEU   E 2 246 ? 49.352  -42.318 -52.649 1.00 119.68 ? 246  LEU   E C   1 
ATOM   13255 O  O   . LEU   E 2 246 ? 48.261  -41.856 -52.309 1.00 121.03 ? 246  LEU   E O   1 
ATOM   13256 C  CB  . LEU   E 2 246 ? 49.355  -42.594 -55.130 1.00 119.76 ? 246  LEU   E CB  1 
ATOM   13257 C  CG  . LEU   E 2 246 ? 50.645  -41.916 -55.586 1.00 126.39 ? 246  LEU   E CG  1 
ATOM   13258 C  CD1 . LEU   E 2 246 ? 51.804  -42.927 -55.682 1.00 125.16 ? 246  LEU   E CD1 1 
ATOM   13259 C  CD2 . LEU   E 2 246 ? 50.410  -41.189 -56.917 1.00 121.66 ? 246  LEU   E CD2 1 
ATOM   13260 N  N   . ALA   E 2 247 ? 50.505  -41.975 -52.067 1.00 122.34 ? 247  ALA   E N   1 
ATOM   13261 C  CA  . ALA   E 2 247 ? 50.563  -41.068 -50.922 1.00 124.04 ? 247  ALA   E CA  1 
ATOM   13262 C  C   . ALA   E 2 247 ? 51.690  -40.060 -51.107 1.00 122.30 ? 247  ALA   E C   1 
ATOM   13263 O  O   . ALA   E 2 247 ? 52.814  -40.436 -51.459 1.00 122.36 ? 247  ALA   E O   1 
ATOM   13264 C  CB  . ALA   E 2 247 ? 50.753  -41.827 -49.604 1.00 120.73 ? 247  ALA   E CB  1 
ATOM   13265 N  N   . ILE   E 2 248 ? 51.384  -38.784 -50.877 1.00 123.86 ? 248  ILE   E N   1 
ATOM   13266 C  CA  . ILE   E 2 248 ? 52.350  -37.699 -50.969 1.00 121.84 ? 248  ILE   E CA  1 
ATOM   13267 C  C   . ILE   E 2 248 ? 52.471  -37.049 -49.598 1.00 122.20 ? 248  ILE   E C   1 
ATOM   13268 O  O   . ILE   E 2 248 ? 51.504  -37.001 -48.828 1.00 120.09 ? 248  ILE   E O   1 
ATOM   13269 C  CB  . ILE   E 2 248 ? 51.941  -36.685 -52.066 1.00 117.20 ? 248  ILE   E CB  1 
ATOM   13270 C  CG1 . ILE   E 2 248 ? 52.767  -35.404 -51.982 1.00 120.80 ? 248  ILE   E CG1 1 
ATOM   13271 C  CG2 . ILE   E 2 248 ? 50.443  -36.377 -52.038 1.00 116.40 ? 248  ILE   E CG2 1 
ATOM   13272 C  CD1 . ILE   E 2 248 ? 52.513  -34.467 -53.131 1.00 117.97 ? 248  ILE   E CD1 1 
ATOM   13273 N  N   . ALA   E 2 249 ? 53.684  -36.618 -49.261 1.00 121.13 ? 249  ALA   E N   1 
ATOM   13274 C  CA  . ALA   E 2 249 ? 53.956  -35.859 -48.042 1.00 122.16 ? 249  ALA   E CA  1 
ATOM   13275 C  C   . ALA   E 2 249 ? 54.608  -34.549 -48.457 1.00 130.59 ? 249  ALA   E C   1 
ATOM   13276 O  O   . ALA   E 2 249 ? 55.827  -34.381 -48.325 1.00 130.60 ? 249  ALA   E O   1 
ATOM   13277 C  CB  . ALA   E 2 249 ? 54.852  -36.632 -47.080 1.00 122.49 ? 249  ALA   E CB  1 
ATOM   13278 N  N   . PRO   E 2 250 ? 53.826  -33.613 -48.999 1.00 136.73 ? 250  PRO   E N   1 
ATOM   13279 C  CA  . PRO   E 2 250 ? 54.394  -32.335 -49.392 1.00 134.14 ? 250  PRO   E CA  1 
ATOM   13280 C  C   . PRO   E 2 250 ? 54.785  -31.537 -48.166 1.00 134.04 ? 250  PRO   E C   1 
ATOM   13281 O  O   . PRO   E 2 250 ? 54.174  -31.670 -47.090 1.00 134.14 ? 250  PRO   E O   1 
ATOM   13282 C  CB  . PRO   E 2 250 ? 53.247  -31.649 -50.152 1.00 135.27 ? 250  PRO   E CB  1 
ATOM   13283 C  CG  . PRO   E 2 250 ? 52.240  -32.697 -50.394 1.00 137.84 ? 250  PRO   E CG  1 
ATOM   13284 C  CD  . PRO   E 2 250 ? 52.388  -33.684 -49.289 1.00 138.15 ? 250  PRO   E CD  1 
ATOM   13285 N  N   . PRO   E 2 251 ? 55.762  -30.712 -48.279 1.00 124.11 ? 251  PRO   E N   1 
ATOM   13286 C  CA  . PRO   E 2 251 ? 56.187  -29.918 -47.128 1.00 123.97 ? 251  PRO   E CA  1 
ATOM   13287 C  C   . PRO   E 2 251 ? 55.377  -28.638 -46.997 1.00 123.20 ? 251  PRO   E C   1 
ATOM   13288 O  O   . PRO   E 2 251 ? 55.146  -28.134 -45.889 1.00 122.97 ? 251  PRO   E O   1 
ATOM   13289 C  CB  . PRO   E 2 251 ? 57.655  -29.635 -47.443 1.00 120.22 ? 251  PRO   E CB  1 
ATOM   13290 C  CG  . PRO   E 2 251 ? 57.696  -29.613 -48.950 1.00 119.28 ? 251  PRO   E CG  1 
ATOM   13291 C  CD  . PRO   E 2 251 ? 56.667  -30.589 -49.430 1.00 119.93 ? 251  PRO   E CD  1 
ATOM   13292 N  N   . ILE   E 2 252 ? 54.936  -28.111 -48.144 1.00 116.96 ? 252  ILE   E N   1 
ATOM   13293 C  CA  . ILE   E 2 252 ? 54.207  -26.853 -48.146 1.00 111.90 ? 252  ILE   E CA  1 
ATOM   13294 C  C   . ILE   E 2 252 ? 52.986  -26.945 -47.243 1.00 117.74 ? 252  ILE   E C   1 
ATOM   13295 O  O   . ILE   E 2 252 ? 52.626  -25.984 -46.550 1.00 124.92 ? 252  ILE   E O   1 
ATOM   13296 C  CB  . ILE   E 2 252 ? 53.827  -26.473 -49.592 1.00 115.39 ? 252  ILE   E CB  1 
ATOM   13297 C  CG1 . ILE   E 2 252 ? 53.291  -25.034 -49.667 1.00 112.10 ? 252  ILE   E CG1 1 
ATOM   13298 C  CG2 . ILE   E 2 252 ? 52.790  -27.447 -50.125 1.00 118.72 ? 252  ILE   E CG2 1 
ATOM   13299 C  CD1 . ILE   E 2 252 ? 54.274  -23.965 -49.243 1.00 113.72 ? 252  ILE   E CD1 1 
ATOM   13300 N  N   . ILE   E 2 253 ? 52.324  -28.103 -47.230 1.00 121.58 ? 253  ILE   E N   1 
ATOM   13301 C  CA  . ILE   E 2 253 ? 51.119  -28.247 -46.419 1.00 121.00 ? 253  ILE   E CA  1 
ATOM   13302 C  C   . ILE   E 2 253 ? 51.440  -28.446 -44.955 1.00 121.79 ? 253  ILE   E C   1 
ATOM   13303 O  O   . ILE   E 2 253 ? 50.519  -28.549 -44.132 1.00 125.39 ? 253  ILE   E O   1 
ATOM   13304 C  CB  . ILE   E 2 253 ? 50.268  -29.433 -46.909 1.00 121.94 ? 253  ILE   E CB  1 
ATOM   13305 C  CG1 . ILE   E 2 253 ? 50.769  -30.741 -46.300 1.00 122.11 ? 253  ILE   E CG1 1 
ATOM   13306 C  CG2 . ILE   E 2 253 ? 50.333  -29.510 -48.416 1.00 120.44 ? 253  ILE   E CG2 1 
ATOM   13307 C  CD1 . ILE   E 2 253 ? 49.825  -31.884 -46.566 1.00 118.76 ? 253  ILE   E CD1 1 
ATOM   13308 N  N   . LYS   E 2 254 ? 52.720  -28.503 -44.605 1.00 123.48 ? 254  LYS   E N   1 
ATOM   13309 C  CA  . LYS   E 2 254 ? 53.142  -28.886 -43.269 1.00 128.37 ? 254  LYS   E CA  1 
ATOM   13310 C  C   . LYS   E 2 254 ? 53.173  -27.712 -42.299 1.00 128.27 ? 254  LYS   E C   1 
ATOM   13311 O  O   . LYS   E 2 254 ? 53.811  -27.819 -41.251 1.00 128.47 ? 254  LYS   E O   1 
ATOM   13312 C  CB  . LYS   E 2 254 ? 54.516  -29.564 -43.326 1.00 126.12 ? 254  LYS   E CB  1 
ATOM   13313 N  N   . GLN   E 2 255 ? 52.503  -26.597 -42.621 1.00 133.25 ? 255  GLN   E N   1 
ATOM   13314 C  CA  . GLN   E 2 255 ? 52.535  -25.403 -41.783 1.00 132.59 ? 255  GLN   E CA  1 
ATOM   13315 C  C   . GLN   E 2 255 ? 51.218  -25.113 -41.090 1.00 130.38 ? 255  GLN   E C   1 
ATOM   13316 O  O   . GLN   E 2 255 ? 51.202  -24.327 -40.136 1.00 129.56 ? 255  GLN   E O   1 
ATOM   13317 C  CB  . GLN   E 2 255 ? 52.897  -24.165 -42.613 1.00 132.06 ? 255  GLN   E CB  1 
ATOM   13318 C  CG  . GLN   E 2 255 ? 53.900  -24.419 -43.693 1.00 135.71 ? 255  GLN   E CG  1 
ATOM   13319 C  CD  . GLN   E 2 255 ? 55.317  -24.415 -43.164 1.00 141.47 ? 255  GLN   E CD  1 
ATOM   13320 O  OE1 . GLN   E 2 255 ? 55.555  -24.093 -41.991 1.00 140.83 ? 255  GLN   E OE1 1 
ATOM   13321 N  NE2 . GLN   E 2 255 ? 56.275  -24.766 -44.029 1.00 140.42 ? 255  GLN   E NE2 1 
ATOM   13322 N  N   . SER   E 2 256 ? 50.125  -25.706 -41.567 1.00 120.98 ? 256  SER   E N   1 
ATOM   13323 C  CA  . SER   E 2 256 ? 48.775  -25.466 -41.074 1.00 112.04 ? 256  SER   E CA  1 
ATOM   13324 C  C   . SER   E 2 256 ? 47.882  -26.538 -41.681 1.00 104.81 ? 256  SER   E C   1 
ATOM   13325 O  O   . SER   E 2 256 ? 48.213  -27.131 -42.709 1.00 103.69 ? 256  SER   E O   1 
ATOM   13326 C  CB  . SER   E 2 256 ? 48.284  -24.048 -41.427 1.00 104.27 ? 256  SER   E CB  1 
ATOM   13327 O  OG  . SER   E 2 256 ? 46.988  -23.774 -40.901 1.00 96.37  ? 256  SER   E OG  1 
ATOM   13328 N  N   . THR   E 2 257 ? 46.741  -26.770 -41.032 1.00 98.64  ? 257  THR   E N   1 
ATOM   13329 C  CA  . THR   E 2 257 ? 45.853  -27.881 -41.362 1.00 97.30  ? 257  THR   E CA  1 
ATOM   13330 C  C   . THR   E 2 257 ? 44.884  -27.525 -42.482 1.00 94.32  ? 257  THR   E C   1 
ATOM   13331 O  O   . THR   E 2 257 ? 44.321  -26.427 -42.503 1.00 98.71  ? 257  THR   E O   1 
ATOM   13332 C  CB  . THR   E 2 257 ? 45.063  -28.299 -40.123 1.00 90.83  ? 257  THR   E CB  1 
ATOM   13333 O  OG1 . THR   E 2 257 ? 45.976  -28.740 -39.121 1.00 89.99  ? 257  THR   E OG1 1 
ATOM   13334 C  CG2 . THR   E 2 257 ? 44.094  -29.425 -40.473 1.00 97.75  ? 257  THR   E CG2 1 
ATOM   13335 N  N   . ILE   E 2 258 ? 44.670  -28.458 -43.399 1.00 91.56  ? 258  ILE   E N   1 
ATOM   13336 C  CA  . ILE   E 2 258 ? 43.710  -28.214 -44.465 1.00 89.81  ? 258  ILE   E CA  1 
ATOM   13337 C  C   . ILE   E 2 258 ? 42.309  -28.512 -43.943 1.00 88.68  ? 258  ILE   E C   1 
ATOM   13338 O  O   . ILE   E 2 258 ? 42.013  -29.635 -43.533 1.00 92.63  ? 258  ILE   E O   1 
ATOM   13339 C  CB  . ILE   E 2 258 ? 44.040  -29.038 -45.713 1.00 92.06  ? 258  ILE   E CB  1 
ATOM   13340 C  CG1 . ILE   E 2 258 ? 45.527  -28.944 -46.043 1.00 92.92  ? 258  ILE   E CG1 1 
ATOM   13341 C  CG2 . ILE   E 2 258 ? 43.246  -28.515 -46.874 1.00 97.75  ? 258  ILE   E CG2 1 
ATOM   13342 C  CD1 . ILE   E 2 258 ? 45.978  -27.564 -46.466 1.00 95.60  ? 258  ILE   E CD1 1 
ATOM   13343 N  N   . VAL   E 2 259 ? 41.447  -27.501 -43.947 1.00 92.25  ? 259  VAL   E N   1 
ATOM   13344 C  CA  . VAL   E 2 259 ? 40.119  -27.624 -43.361 1.00 93.95  ? 259  VAL   E CA  1 
ATOM   13345 C  C   . VAL   E 2 259 ? 38.998  -27.517 -44.382 1.00 93.95  ? 259  VAL   E C   1 
ATOM   13346 O  O   . VAL   E 2 259 ? 37.856  -27.884 -44.060 1.00 95.50  ? 259  VAL   E O   1 
ATOM   13347 C  CB  . VAL   E 2 259 ? 39.904  -26.594 -42.234 1.00 93.33  ? 259  VAL   E CB  1 
ATOM   13348 C  CG1 . VAL   E 2 259 ? 40.836  -26.893 -41.067 1.00 93.61  ? 259  VAL   E CG1 1 
ATOM   13349 C  CG2 . VAL   E 2 259 ? 40.150  -25.186 -42.760 1.00 92.91  ? 259  VAL   E CG2 1 
ATOM   13350 N  N   . CYS   E 2 260 ? 39.249  -27.039 -45.593 1.00 88.87  ? 260  CYS   E N   1 
ATOM   13351 C  CA  . CYS   E 2 260 ? 38.183  -27.095 -46.579 1.00 93.36  ? 260  CYS   E CA  1 
ATOM   13352 C  C   . CYS   E 2 260 ? 38.763  -27.343 -47.957 1.00 97.72  ? 260  CYS   E C   1 
ATOM   13353 O  O   . CYS   E 2 260 ? 39.908  -26.984 -48.251 1.00 95.57  ? 260  CYS   E O   1 
ATOM   13354 C  CB  . CYS   E 2 260 ? 37.320  -25.824 -46.593 1.00 96.33  ? 260  CYS   E CB  1 
ATOM   13355 S  SG  . CYS   E 2 260 ? 38.294  -24.287 -46.646 1.00 97.36  ? 260  CYS   E SG  1 
ATOM   13356 N  N   . HIS   E 2 261 ? 37.937  -27.967 -48.793 1.00 100.01 ? 261  HIS   E N   1 
ATOM   13357 C  CA  . HIS   E 2 261 ? 38.312  -28.406 -50.121 1.00 97.32  ? 261  HIS   E CA  1 
ATOM   13358 C  C   . HIS   E 2 261 ? 37.177  -28.058 -51.067 1.00 97.66  ? 261  HIS   E C   1 
ATOM   13359 O  O   . HIS   E 2 261 ? 36.064  -27.709 -50.653 1.00 93.89  ? 261  HIS   E O   1 
ATOM   13360 C  CB  . HIS   E 2 261 ? 38.593  -29.917 -50.149 1.00 98.19  ? 261  HIS   E CB  1 
ATOM   13361 C  CG  . HIS   E 2 261 ? 37.363  -30.759 -49.962 1.00 98.54  ? 261  HIS   E CG  1 
ATOM   13362 N  ND1 . HIS   E 2 261 ? 36.712  -31.374 -51.012 1.00 93.62  ? 261  HIS   E ND1 1 
ATOM   13363 C  CD2 . HIS   E 2 261 ? 36.647  -31.061 -48.851 1.00 98.81  ? 261  HIS   E CD2 1 
ATOM   13364 C  CE1 . HIS   E 2 261 ? 35.662  -32.033 -50.555 1.00 93.96  ? 261  HIS   E CE1 1 
ATOM   13365 N  NE2 . HIS   E 2 261 ? 35.598  -31.859 -49.247 1.00 97.80  ? 261  HIS   E NE2 1 
ATOM   13366 N  N   . ASN   E 2 262 ? 37.464  -28.162 -52.355 1.00 98.40  ? 262  ASN   E N   1 
ATOM   13367 C  CA  . ASN   E 2 262 ? 36.404  -28.007 -53.328 1.00 95.12  ? 262  ASN   E CA  1 
ATOM   13368 C  C   . ASN   E 2 262 ? 36.895  -28.582 -54.633 1.00 100.35 ? 262  ASN   E C   1 
ATOM   13369 O  O   . ASN   E 2 262 ? 38.092  -28.524 -54.927 1.00 99.00  ? 262  ASN   E O   1 
ATOM   13370 C  CB  . ASN   E 2 262 ? 36.014  -26.549 -53.505 1.00 95.66  ? 262  ASN   E CB  1 
ATOM   13371 C  CG  . ASN   E 2 262 ? 34.829  -26.394 -54.406 1.00 98.67  ? 262  ASN   E CG  1 
ATOM   13372 O  OD1 . ASN   E 2 262 ? 34.874  -25.660 -55.403 1.00 95.53  ? 262  ASN   E OD1 1 
ATOM   13373 N  ND2 . ASN   E 2 262 ? 33.752  -27.117 -54.084 1.00 100.00 ? 262  ASN   E ND2 1 
ATOM   13374 N  N   . ARG   E 2 263 ? 35.968  -29.152 -55.399 1.00 105.47 ? 263  ARG   E N   1 
ATOM   13375 C  CA  . ARG   E 2 263 ? 36.294  -29.727 -56.695 1.00 107.12 ? 263  ARG   E CA  1 
ATOM   13376 C  C   . ARG   E 2 263 ? 36.150  -28.641 -57.756 1.00 106.16 ? 263  ARG   E C   1 
ATOM   13377 O  O   . ARG   E 2 263 ? 35.051  -28.130 -57.991 1.00 100.87 ? 263  ARG   E O   1 
ATOM   13378 C  CB  . ARG   E 2 263 ? 35.410  -30.940 -56.986 1.00 109.34 ? 263  ARG   E CB  1 
ATOM   13379 C  CG  . ARG   E 2 263 ? 35.334  -31.288 -58.467 1.00 118.82 ? 263  ARG   E CG  1 
ATOM   13380 C  CD  . ARG   E 2 263 ? 34.918  -32.725 -58.694 1.00 113.44 ? 263  ARG   E CD  1 
ATOM   13381 N  NE  . ARG   E 2 263 ? 33.778  -33.082 -57.864 1.00 108.72 ? 263  ARG   E NE  1 
ATOM   13382 C  CZ  . ARG   E 2 263 ? 32.522  -32.775 -58.151 1.00 106.76 ? 263  ARG   E CZ  1 
ATOM   13383 N  NH1 . ARG   E 2 263 ? 32.210  -32.089 -59.241 1.00 108.09 ? 263  ARG   E NH1 1 
ATOM   13384 N  NH2 . ARG   E 2 263 ? 31.556  -33.165 -57.322 1.00 104.93 ? 263  ARG   E NH2 1 
ATOM   13385 N  N   . VAL   E 2 264 ? 37.265  -28.277 -58.380 1.00 109.74 ? 264  VAL   E N   1 
ATOM   13386 C  CA  . VAL   E 2 264 ? 37.230  -27.374 -59.518 1.00 111.55 ? 264  VAL   E CA  1 
ATOM   13387 C  C   . VAL   E 2 264 ? 36.519  -27.944 -60.732 1.00 129.05 ? 264  VAL   E C   1 
ATOM   13388 O  O   . VAL   E 2 264 ? 35.525  -27.387 -61.206 1.00 131.59 ? 264  VAL   E O   1 
ATOM   13389 C  CB  . VAL   E 2 264 ? 38.641  -27.002 -59.992 1.00 109.88 ? 264  VAL   E CB  1 
ATOM   13390 C  CG1 . VAL   E 2 264 ? 38.592  -25.707 -60.769 1.00 109.18 ? 264  VAL   E CG1 1 
ATOM   13391 C  CG2 . VAL   E 2 264 ? 39.593  -26.903 -58.815 1.00 107.27 ? 264  VAL   E CG2 1 
ATOM   13392 N  N   . ASP   E 2 265 ? 37.016  -29.057 -61.237 1.00 155.38 ? 265  ASP   E N   1 
ATOM   13393 C  CA  . ASP   E 2 265 ? 36.443  -29.652 -62.439 1.00 157.51 ? 265  ASP   E CA  1 
ATOM   13394 C  C   . ASP   E 2 265 ? 35.609  -30.837 -61.951 1.00 156.30 ? 265  ASP   E C   1 
ATOM   13395 O  O   . ASP   E 2 265 ? 36.007  -31.525 -61.010 1.00 155.35 ? 265  ASP   E O   1 
ATOM   13396 C  CB  . ASP   E 2 265 ? 37.495  -30.137 -63.431 1.00 159.33 ? 265  ASP   E CB  1 
ATOM   13397 C  CG  . ASP   E 2 265 ? 38.703  -30.750 -62.732 1.00 160.81 ? 265  ASP   E CG  1 
ATOM   13398 O  OD1 . ASP   E 2 265 ? 38.493  -31.673 -61.915 1.00 160.01 ? 265  ASP   E OD1 1 
ATOM   13399 O  OD2 . ASP   E 2 265 ? 39.846  -30.283 -62.964 1.00 162.73 ? 265  ASP   E OD2 1 
ATOM   13400 N  N   . PRO   E 2 266 ? 34.456  -31.114 -62.570 1.00 142.04 ? 266  PRO   E N   1 
ATOM   13401 C  CA  . PRO   E 2 266 ? 33.649  -32.278 -62.157 1.00 137.53 ? 266  PRO   E CA  1 
ATOM   13402 C  C   . PRO   E 2 266 ? 34.279  -33.640 -62.446 1.00 129.93 ? 266  PRO   E C   1 
ATOM   13403 O  O   . PRO   E 2 266 ? 33.680  -34.656 -62.077 1.00 122.78 ? 266  PRO   E O   1 
ATOM   13404 C  CB  . PRO   E 2 266 ? 32.343  -32.095 -62.948 1.00 129.95 ? 266  PRO   E CB  1 
ATOM   13405 C  CG  . PRO   E 2 266 ? 32.261  -30.635 -63.195 1.00 130.35 ? 266  PRO   E CG  1 
ATOM   13406 C  CD  . PRO   E 2 266 ? 33.686  -30.195 -63.426 1.00 137.80 ? 266  PRO   E CD  1 
ATOM   13407 N  N   . ASN   E 2 267 ? 35.461  -33.709 -63.065 1.00 132.73 ? 267  ASN   E N   1 
ATOM   13408 C  CA  . ASN   E 2 267 ? 36.125  -34.986 -63.310 1.00 132.36 ? 267  ASN   E CA  1 
ATOM   13409 C  C   . ASN   E 2 267 ? 37.216  -35.322 -62.295 1.00 127.14 ? 267  ASN   E C   1 
ATOM   13410 O  O   . ASN   E 2 267 ? 37.623  -36.486 -62.223 1.00 124.80 ? 267  ASN   E O   1 
ATOM   13411 C  CB  . ASN   E 2 267 ? 36.714  -35.027 -64.735 1.00 136.36 ? 267  ASN   E CB  1 
ATOM   13412 C  CG  . ASN   E 2 267 ? 37.435  -33.737 -65.120 1.00 140.73 ? 267  ASN   E CG  1 
ATOM   13413 O  OD1 . ASN   E 2 267 ? 37.613  -32.850 -64.290 1.00 140.50 ? 267  ASN   E OD1 1 
ATOM   13414 N  ND2 . ASN   E 2 267 ? 37.857  -33.635 -66.387 1.00 138.06 ? 267  ASN   E ND2 1 
ATOM   13415 N  N   . GLY   E 2 268 ? 37.694  -34.356 -61.507 1.00 130.05 ? 268  GLY   E N   1 
ATOM   13416 C  CA  . GLY   E 2 268 ? 38.573  -34.646 -60.387 1.00 124.30 ? 268  GLY   E CA  1 
ATOM   13417 C  C   . GLY   E 2 268 ? 40.031  -34.259 -60.544 1.00 121.53 ? 268  GLY   E C   1 
ATOM   13418 O  O   . GLY   E 2 268 ? 40.790  -34.403 -59.579 1.00 118.54 ? 268  GLY   E O   1 
ATOM   13419 N  N   . SER   E 2 269 ? 40.458  -33.766 -61.706 1.00 123.28 ? 269  SER   E N   1 
ATOM   13420 C  CA  . SER   E 2 269 ? 41.877  -33.484 -61.896 1.00 120.62 ? 269  SER   E CA  1 
ATOM   13421 C  C   . SER   E 2 269 ? 42.384  -32.424 -60.927 1.00 119.66 ? 269  SER   E C   1 
ATOM   13422 O  O   . SER   E 2 269 ? 43.529  -32.497 -60.467 1.00 118.28 ? 269  SER   E O   1 
ATOM   13423 C  CB  . SER   E 2 269 ? 42.139  -33.043 -63.330 1.00 122.07 ? 269  SER   E CB  1 
ATOM   13424 O  OG  . SER   E 2 269 ? 42.065  -31.629 -63.423 1.00 130.51 ? 269  SER   E OG  1 
ATOM   13425 N  N   . ARG   E 2 270 ? 41.563  -31.420 -60.622 1.00 124.54 ? 270  ARG   E N   1 
ATOM   13426 C  CA  . ARG   E 2 270 ? 41.994  -30.262 -59.842 1.00 117.99 ? 270  ARG   E CA  1 
ATOM   13427 C  C   . ARG   E 2 270 ? 41.085  -30.081 -58.632 1.00 112.07 ? 270  ARG   E C   1 
ATOM   13428 O  O   . ARG   E 2 270 ? 39.862  -30.200 -58.744 1.00 112.77 ? 270  ARG   E O   1 
ATOM   13429 C  CB  . ARG   E 2 270 ? 42.000  -28.999 -60.723 1.00 115.58 ? 270  ARG   E CB  1 
ATOM   13430 N  N   . TYR   E 2 271 ? 41.692  -29.822 -57.471 1.00 109.02 ? 271  TYR   E N   1 
ATOM   13431 C  CA  . TYR   E 2 271 ? 40.982  -29.518 -56.231 1.00 106.66 ? 271  TYR   E CA  1 
ATOM   13432 C  C   . TYR   E 2 271 ? 41.589  -28.271 -55.602 1.00 102.64 ? 271  TYR   E C   1 
ATOM   13433 O  O   . TYR   E 2 271 ? 42.759  -27.953 -55.825 1.00 105.36 ? 271  TYR   E O   1 
ATOM   13434 C  CB  . TYR   E 2 271 ? 41.031  -30.703 -55.213 1.00 106.51 ? 271  TYR   E CB  1 
ATOM   13435 C  CG  . TYR   E 2 271 ? 40.047  -31.821 -55.515 1.00 106.52 ? 271  TYR   E CG  1 
ATOM   13436 C  CD1 . TYR   E 2 271 ? 38.717  -31.735 -55.107 1.00 102.85 ? 271  TYR   E CD1 1 
ATOM   13437 C  CD2 . TYR   E 2 271 ? 40.444  -32.949 -56.223 1.00 109.78 ? 271  TYR   E CD2 1 
ATOM   13438 C  CE1 . TYR   E 2 271 ? 37.813  -32.741 -55.393 1.00 106.20 ? 271  TYR   E CE1 1 
ATOM   13439 C  CE2 . TYR   E 2 271 ? 39.547  -33.963 -56.516 1.00 107.93 ? 271  TYR   E CE2 1 
ATOM   13440 C  CZ  . TYR   E 2 271 ? 38.235  -33.853 -56.097 1.00 111.18 ? 271  TYR   E CZ  1 
ATOM   13441 O  OH  . TYR   E 2 271 ? 37.333  -34.852 -56.380 1.00 111.25 ? 271  TYR   E OH  1 
ATOM   13442 N  N   . LEU   E 2 272 ? 40.794  -27.558 -54.817 1.00 101.11 ? 272  LEU   E N   1 
ATOM   13443 C  CA  . LEU   E 2 272 ? 41.284  -26.399 -54.079 1.00 99.12  ? 272  LEU   E CA  1 
ATOM   13444 C  C   . LEU   E 2 272 ? 41.325  -26.731 -52.597 1.00 98.44  ? 272  LEU   E C   1 
ATOM   13445 O  O   . LEU   E 2 272 ? 40.348  -27.248 -52.039 1.00 99.62  ? 272  LEU   E O   1 
ATOM   13446 C  CB  . LEU   E 2 272 ? 40.412  -25.171 -54.333 1.00 96.77  ? 272  LEU   E CB  1 
ATOM   13447 C  CG  . LEU   E 2 272 ? 41.011  -24.120 -55.269 1.00 94.46  ? 272  LEU   E CG  1 
ATOM   13448 C  CD1 . LEU   E 2 272 ? 41.609  -24.744 -56.517 1.00 101.19 ? 272  LEU   E CD1 1 
ATOM   13449 C  CD2 . LEU   E 2 272 ? 39.955  -23.126 -55.665 1.00 92.61  ? 272  LEU   E CD2 1 
ATOM   13450 N  N   . LEU   E 2 273 ? 42.460  -26.455 -51.968 1.00 96.03  ? 273  LEU   E N   1 
ATOM   13451 C  CA  . LEU   E 2 273 ? 42.651  -26.726 -50.555 1.00 96.20  ? 273  LEU   E CA  1 
ATOM   13452 C  C   . LEU   E 2 273 ? 42.874  -25.420 -49.818 1.00 95.56  ? 273  LEU   E C   1 
ATOM   13453 O  O   . LEU   E 2 273 ? 43.559  -24.520 -50.314 1.00 95.57  ? 273  LEU   E O   1 
ATOM   13454 C  CB  . LEU   E 2 273 ? 43.835  -27.651 -50.316 1.00 94.63  ? 273  LEU   E CB  1 
ATOM   13455 C  CG  . LEU   E 2 273 ? 43.847  -28.864 -51.231 1.00 99.97  ? 273  LEU   E CG  1 
ATOM   13456 C  CD1 . LEU   E 2 273 ? 45.208  -29.543 -51.185 1.00 102.68 ? 273  LEU   E CD1 1 
ATOM   13457 C  CD2 . LEU   E 2 273 ? 42.742  -29.825 -50.818 1.00 97.25  ? 273  LEU   E CD2 1 
ATOM   13458 N  N   . GLY   E 2 274 ? 42.303  -25.329 -48.637 1.00 90.72  ? 274  GLY   E N   1 
ATOM   13459 C  CA  . GLY   E 2 274 ? 42.500  -24.168 -47.787 1.00 92.68  ? 274  GLY   E CA  1 
ATOM   13460 C  C   . GLY   E 2 274 ? 42.858  -24.581 -46.378 1.00 91.99  ? 274  GLY   E C   1 
ATOM   13461 O  O   . GLY   E 2 274 ? 42.252  -25.495 -45.815 1.00 91.26  ? 274  GLY   E O   1 
ATOM   13462 N  N   . ASP   E 2 275 ? 43.840  -23.873 -45.803 1.00 89.65  ? 275  ASP   E N   1 
ATOM   13463 C  CA  . ASP   E 2 275 ? 44.337  -24.102 -44.455 1.00 90.28  ? 275  ASP   E CA  1 
ATOM   13464 C  C   . ASP   E 2 275 ? 43.785  -23.038 -43.498 1.00 90.36  ? 275  ASP   E C   1 
ATOM   13465 O  O   . ASP   E 2 275 ? 43.103  -22.087 -43.904 1.00 92.47  ? 275  ASP   E O   1 
ATOM   13466 C  CB  . ASP   E 2 275 ? 45.872  -24.115 -44.447 1.00 93.03  ? 275  ASP   E CB  1 
ATOM   13467 C  CG  . ASP   E 2 275 ? 46.477  -22.716 -44.587 1.00 94.69  ? 275  ASP   E CG  1 
ATOM   13468 O  OD1 . ASP   E 2 275 ? 45.732  -21.762 -44.924 1.00 96.60  ? 275  ASP   E OD1 1 
ATOM   13469 O  OD2 . ASP   E 2 275 ? 47.700  -22.564 -44.357 1.00 92.21  ? 275  ASP   E OD2 1 
ATOM   13470 N  N   . MET   E 2 276 ? 44.108  -23.185 -42.208 1.00 86.30  ? 276  MET   E N   1 
ATOM   13471 C  CA  . MET   E 2 276 ? 43.557  -22.305 -41.185 1.00 89.65  ? 276  MET   E CA  1 
ATOM   13472 C  C   . MET   E 2 276 ? 44.272  -20.960 -41.096 1.00 91.77  ? 276  MET   E C   1 
ATOM   13473 O  O   . MET   E 2 276 ? 44.037  -20.211 -40.146 1.00 89.37  ? 276  MET   E O   1 
ATOM   13474 C  CB  . MET   E 2 276 ? 43.601  -22.992 -39.829 1.00 89.34  ? 276  MET   E CB  1 
ATOM   13475 C  CG  . MET   E 2 276 ? 43.189  -24.434 -39.892 1.00 93.51  ? 276  MET   E CG  1 
ATOM   13476 S  SD  . MET   E 2 276 ? 43.333  -25.246 -38.271 1.00 93.29  ? 276  MET   E SD  1 
ATOM   13477 C  CE  . MET   E 2 276 ? 44.972  -24.704 -37.768 1.00 87.06  ? 276  MET   E CE  1 
ATOM   13478 N  N   . GLU   E 2 277 ? 45.140  -20.637 -42.054 1.00 91.34  ? 277  GLU   E N   1 
ATOM   13479 C  CA  . GLU   E 2 277 ? 45.877  -19.385 -42.027 1.00 87.03  ? 277  GLU   E CA  1 
ATOM   13480 C  C   . GLU   E 2 277 ? 45.752  -18.588 -43.326 1.00 94.73  ? 277  GLU   E C   1 
ATOM   13481 O  O   . GLU   E 2 277 ? 46.446  -17.574 -43.485 1.00 96.57  ? 277  GLU   E O   1 
ATOM   13482 C  CB  . GLU   E 2 277 ? 47.355  -19.630 -41.692 1.00 86.97  ? 277  GLU   E CB  1 
ATOM   13483 C  CG  . GLU   E 2 277 ? 47.613  -20.212 -40.279 1.00 90.91  ? 277  GLU   E CG  1 
ATOM   13484 C  CD  . GLU   E 2 277 ? 49.075  -20.647 -40.044 1.00 103.21 ? 277  GLU   E CD  1 
ATOM   13485 O  OE1 . GLU   E 2 277 ? 49.901  -20.513 -40.970 1.00 108.33 ? 277  GLU   E OE1 1 
ATOM   13486 O  OE2 . GLU   E 2 277 ? 49.408  -21.131 -38.933 1.00 107.07 ? 277  GLU   E OE2 1 
ATOM   13487 N  N   . GLY   E 2 278 ? 44.880  -19.000 -44.259 1.00 93.00  ? 278  GLY   E N   1 
ATOM   13488 C  CA  . GLY   E 2 278 ? 44.675  -18.252 -45.485 1.00 91.76  ? 278  GLY   E CA  1 
ATOM   13489 C  C   . GLY   E 2 278 ? 45.353  -18.809 -46.718 1.00 94.80  ? 278  GLY   E C   1 
ATOM   13490 O  O   . GLY   E 2 278 ? 45.143  -18.265 -47.814 1.00 95.42  ? 278  GLY   E O   1 
ATOM   13491 N  N   . ARG   E 2 279 ? 46.159  -19.863 -46.579 1.00 96.32  ? 279  ARG   E N   1 
ATOM   13492 C  CA  . ARG   E 2 279 ? 46.788  -20.476 -47.743 1.00 94.55  ? 279  ARG   E CA  1 
ATOM   13493 C  C   . ARG   E 2 279 ? 45.729  -21.086 -48.651 1.00 93.32  ? 279  ARG   E C   1 
ATOM   13494 O  O   . ARG   E 2 279 ? 44.816  -21.782 -48.194 1.00 90.39  ? 279  ARG   E O   1 
ATOM   13495 C  CB  . ARG   E 2 279 ? 47.797  -21.548 -47.319 1.00 92.72  ? 279  ARG   E CB  1 
ATOM   13496 C  CG  . ARG   E 2 279 ? 49.244  -21.088 -47.209 1.00 88.84  ? 279  ARG   E CG  1 
ATOM   13497 C  CD  . ARG   E 2 279 ? 49.723  -21.309 -45.778 1.00 93.77  ? 279  ARG   E CD  1 
ATOM   13498 N  NE  . ARG   E 2 279 ? 51.036  -20.747 -45.476 1.00 100.38 ? 279  ARG   E NE  1 
ATOM   13499 C  CZ  . ARG   E 2 279 ? 51.640  -20.851 -44.296 1.00 106.30 ? 279  ARG   E CZ  1 
ATOM   13500 N  NH1 . ARG   E 2 279 ? 51.071  -21.485 -43.278 1.00 108.44 ? 279  ARG   E NH1 1 
ATOM   13501 N  NH2 . ARG   E 2 279 ? 52.844  -20.302 -44.131 1.00 106.90 ? 279  ARG   E NH2 1 
ATOM   13502 N  N   . LEU   E 2 280 ? 45.850  -20.814 -49.940 1.00 94.36  ? 280  LEU   E N   1 
ATOM   13503 C  CA  . LEU   E 2 280 ? 45.024  -21.449 -50.959 1.00 98.63  ? 280  LEU   E CA  1 
ATOM   13504 C  C   . LEU   E 2 280 ? 45.929  -22.338 -51.810 1.00 101.78 ? 280  LEU   E C   1 
ATOM   13505 O  O   . LEU   E 2 280 ? 46.680  -21.829 -52.651 1.00 101.73 ? 280  LEU   E O   1 
ATOM   13506 C  CB  . LEU   E 2 280 ? 44.315  -20.399 -51.808 1.00 94.55  ? 280  LEU   E CB  1 
ATOM   13507 C  CG  . LEU   E 2 280 ? 43.371  -21.009 -52.837 1.00 93.70  ? 280  LEU   E CG  1 
ATOM   13508 C  CD1 . LEU   E 2 280 ? 42.332  -21.880 -52.133 1.00 87.85  ? 280  LEU   E CD1 1 
ATOM   13509 C  CD2 . LEU   E 2 280 ? 42.718  -19.955 -53.743 1.00 91.56  ? 280  LEU   E CD2 1 
ATOM   13510 N  N   . PHE   E 2 281 ? 45.860  -23.661 -51.593 1.00 98.80  ? 281  PHE   E N   1 
ATOM   13511 C  CA  . PHE   E 2 281 ? 46.611  -24.618 -52.400 1.00 99.89  ? 281  PHE   E CA  1 
ATOM   13512 C  C   . PHE   E 2 281 ? 45.773  -25.180 -53.543 1.00 102.01 ? 281  PHE   E C   1 
ATOM   13513 O  O   . PHE   E 2 281 ? 44.541  -25.126 -53.549 1.00 100.81 ? 281  PHE   E O   1 
ATOM   13514 C  CB  . PHE   E 2 281 ? 47.106  -25.793 -51.574 1.00 100.94 ? 281  PHE   E CB  1 
ATOM   13515 C  CG  . PHE   E 2 281 ? 47.764  -25.414 -50.312 1.00 99.05  ? 281  PHE   E CG  1 
ATOM   13516 C  CD1 . PHE   E 2 281 ? 47.012  -25.092 -49.205 1.00 95.16  ? 281  PHE   E CD1 1 
ATOM   13517 C  CD2 . PHE   E 2 281 ? 49.140  -25.435 -50.211 1.00 102.89 ? 281  PHE   E CD2 1 
ATOM   13518 C  CE1 . PHE   E 2 281 ? 47.623  -24.767 -48.024 1.00 98.44  ? 281  PHE   E CE1 1 
ATOM   13519 C  CE2 . PHE   E 2 281 ? 49.760  -25.108 -49.032 1.00 103.82 ? 281  PHE   E CE2 1 
ATOM   13520 C  CZ  . PHE   E 2 281 ? 49.002  -24.773 -47.938 1.00 103.09 ? 281  PHE   E CZ  1 
ATOM   13521 N  N   . MET   E 2 282 ? 46.478  -25.791 -54.495 1.00 107.15 ? 282  MET   E N   1 
ATOM   13522 C  CA  . MET   E 2 282 ? 45.873  -26.509 -55.612 1.00 108.67 ? 282  MET   E CA  1 
ATOM   13523 C  C   . MET   E 2 282 ? 46.327  -27.966 -55.601 1.00 110.58 ? 282  MET   E C   1 
ATOM   13524 O  O   . MET   E 2 282 ? 47.514  -28.254 -55.788 1.00 112.50 ? 282  MET   E O   1 
ATOM   13525 C  CB  . MET   E 2 282 ? 46.238  -25.863 -56.939 1.00 114.79 ? 282  MET   E CB  1 
ATOM   13526 C  CG  . MET   E 2 282 ? 45.611  -26.590 -58.120 1.00 116.93 ? 282  MET   E CG  1 
ATOM   13527 S  SD  . MET   E 2 282 ? 43.820  -26.338 -58.157 1.00 113.89 ? 282  MET   E SD  1 
ATOM   13528 C  CE  . MET   E 2 282 ? 43.728  -25.353 -59.640 1.00 108.33 ? 282  MET   E CE  1 
ATOM   13529 N  N   . LEU   E 2 283 ? 45.386  -28.884 -55.399 1.00 107.82 ? 283  LEU   E N   1 
ATOM   13530 C  CA  . LEU   E 2 283 ? 45.664  -30.303 -55.544 1.00 110.73 ? 283  LEU   E CA  1 
ATOM   13531 C  C   . LEU   E 2 283 ? 45.412  -30.708 -56.995 1.00 114.78 ? 283  LEU   E C   1 
ATOM   13532 O  O   . LEU   E 2 283 ? 44.354  -30.407 -57.561 1.00 112.00 ? 283  LEU   E O   1 
ATOM   13533 C  CB  . LEU   E 2 283 ? 44.803  -31.127 -54.584 1.00 106.92 ? 283  LEU   E CB  1 
ATOM   13534 C  CG  . LEU   E 2 283 ? 45.212  -32.602 -54.510 1.00 108.40 ? 283  LEU   E CG  1 
ATOM   13535 C  CD1 . LEU   E 2 283 ? 46.688  -32.746 -54.165 1.00 107.58 ? 283  LEU   E CD1 1 
ATOM   13536 C  CD2 . LEU   E 2 283 ? 44.351  -33.387 -53.533 1.00 108.31 ? 283  LEU   E CD2 1 
ATOM   13537 N  N   . LEU   E 2 284 ? 46.394  -31.362 -57.609 1.00 113.79 ? 284  LEU   E N   1 
ATOM   13538 C  CA  . LEU   E 2 284 ? 46.274  -31.822 -58.985 1.00 114.34 ? 284  LEU   E CA  1 
ATOM   13539 C  C   . LEU   E 2 284 ? 46.350  -33.338 -59.007 1.00 113.01 ? 284  LEU   E C   1 
ATOM   13540 O  O   . LEU   E 2 284 ? 47.199  -33.930 -58.335 1.00 114.10 ? 284  LEU   E O   1 
ATOM   13541 C  CB  . LEU   E 2 284 ? 47.372  -31.230 -59.873 1.00 112.54 ? 284  LEU   E CB  1 
ATOM   13542 C  CG  . LEU   E 2 284 ? 47.391  -29.708 -59.937 1.00 116.13 ? 284  LEU   E CG  1 
ATOM   13543 C  CD1 . LEU   E 2 284 ? 48.800  -29.223 -59.655 1.00 117.81 ? 284  LEU   E CD1 1 
ATOM   13544 C  CD2 . LEU   E 2 284 ? 46.885  -29.221 -61.298 1.00 119.31 ? 284  LEU   E CD2 1 
ATOM   13545 N  N   . LEU   E 2 285 ? 45.460  -33.962 -59.770 1.00 113.75 ? 285  LEU   E N   1 
ATOM   13546 C  CA  . LEU   E 2 285 ? 45.531  -35.394 -60.049 1.00 114.94 ? 285  LEU   E CA  1 
ATOM   13547 C  C   . LEU   E 2 285 ? 46.099  -35.547 -61.459 1.00 125.91 ? 285  LEU   E C   1 
ATOM   13548 O  O   . LEU   E 2 285 ? 45.408  -35.285 -62.452 1.00 127.30 ? 285  LEU   E O   1 
ATOM   13549 C  CB  . LEU   E 2 285 ? 44.162  -36.049 -59.890 1.00 112.72 ? 285  LEU   E CB  1 
ATOM   13550 C  CG  . LEU   E 2 285 ? 43.774  -36.444 -58.456 1.00 114.92 ? 285  LEU   E CG  1 
ATOM   13551 C  CD1 . LEU   E 2 285 ? 44.139  -35.345 -57.478 1.00 114.82 ? 285  LEU   E CD1 1 
ATOM   13552 C  CD2 . LEU   E 2 285 ? 42.287  -36.763 -58.328 1.00 110.25 ? 285  LEU   E CD2 1 
ATOM   13553 N  N   . GLU   E 2 286 ? 47.377  -35.944 -61.544 1.00 131.54 ? 286  GLU   E N   1 
ATOM   13554 C  CA  . GLU   E 2 286 ? 48.050  -36.120 -62.834 1.00 133.42 ? 286  GLU   E CA  1 
ATOM   13555 C  C   . GLU   E 2 286 ? 47.632  -37.459 -63.441 1.00 133.20 ? 286  GLU   E C   1 
ATOM   13556 O  O   . GLU   E 2 286 ? 47.914  -38.520 -62.871 1.00 133.04 ? 286  GLU   E O   1 
ATOM   13557 C  CB  . GLU   E 2 286 ? 49.570  -36.032 -62.662 1.00 133.93 ? 286  GLU   E CB  1 
ATOM   13558 N  N   . LYS   E 2 287 ? 46.955  -37.410 -64.587 1.00 123.96 ? 287  LYS   E N   1 
ATOM   13559 C  CA  . LYS   E 2 287 ? 46.319  -38.563 -65.211 1.00 126.94 ? 287  LYS   E CA  1 
ATOM   13560 C  C   . LYS   E 2 287 ? 47.145  -39.097 -66.375 1.00 136.27 ? 287  LYS   E C   1 
ATOM   13561 O  O   . LYS   E 2 287 ? 47.934  -38.382 -66.989 1.00 135.52 ? 287  LYS   E O   1 
ATOM   13562 C  CB  . LYS   E 2 287 ? 44.924  -38.197 -65.717 1.00 125.26 ? 287  LYS   E CB  1 
ATOM   13563 N  N   . GLU   E 2 288 ? 46.894  -40.371 -66.715 1.00 142.08 ? 288  GLU   E N   1 
ATOM   13564 C  CA  . GLU   E 2 288 ? 47.670  -41.130 -67.711 1.00 138.60 ? 288  GLU   E CA  1 
ATOM   13565 C  C   . GLU   E 2 288 ? 46.760  -41.724 -68.795 1.00 144.04 ? 288  GLU   E C   1 
ATOM   13566 O  O   . GLU   E 2 288 ? 46.271  -42.846 -68.653 1.00 144.14 ? 288  GLU   E O   1 
ATOM   13567 C  CB  . GLU   E 2 288 ? 48.471  -42.219 -67.009 1.00 130.96 ? 288  GLU   E CB  1 
ATOM   13568 N  N   . GLU   E 2 289 ? 46.563  -40.978 -69.891 1.00 144.74 ? 289  GLU   E N   1 
ATOM   13569 C  CA  . GLU   E 2 289 ? 45.742  -41.407 -71.027 1.00 140.77 ? 289  GLU   E CA  1 
ATOM   13570 C  C   . GLU   E 2 289 ? 46.469  -42.497 -71.809 1.00 141.89 ? 289  GLU   E C   1 
ATOM   13571 O  O   . GLU   E 2 289 ? 47.291  -42.206 -72.681 1.00 142.80 ? 289  GLU   E O   1 
ATOM   13572 C  CB  . GLU   E 2 289 ? 45.428  -40.218 -71.931 1.00 132.48 ? 289  GLU   E CB  1 
ATOM   13573 N  N   . GLN   E 2 290 ? 46.143  -43.759 -71.525 1.00 143.44 ? 290  GLN   E N   1 
ATOM   13574 C  CA  . GLN   E 2 290 ? 46.805  -44.905 -72.138 1.00 144.71 ? 290  GLN   E CA  1 
ATOM   13575 C  C   . GLN   E 2 290 ? 46.138  -45.308 -73.466 1.00 144.00 ? 290  GLN   E C   1 
ATOM   13576 O  O   . GLN   E 2 290 ? 45.089  -44.787 -73.846 1.00 144.48 ? 290  GLN   E O   1 
ATOM   13577 C  CB  . GLN   E 2 290 ? 46.822  -46.067 -71.147 1.00 143.92 ? 290  GLN   E CB  1 
ATOM   13578 C  CG  . GLN   E 2 290 ? 47.577  -45.727 -69.870 1.00 141.05 ? 290  GLN   E CG  1 
ATOM   13579 C  CD  . GLN   E 2 290 ? 47.589  -46.872 -68.872 1.00 142.23 ? 290  GLN   E CD  1 
ATOM   13580 O  OE1 . GLN   E 2 290 ? 46.547  -47.449 -68.563 1.00 143.00 ? 290  GLN   E OE1 1 
ATOM   13581 N  NE2 . GLN   E 2 290 ? 48.772  -47.212 -68.369 1.00 139.09 ? 290  GLN   E NE2 1 
ATOM   13582 N  N   . MET   E 2 291 ? 46.763  -46.237 -74.198 1.00 142.42 ? 291  MET   E N   1 
ATOM   13583 C  CA  . MET   E 2 291 ? 46.200  -46.620 -75.496 1.00 138.80 ? 291  MET   E CA  1 
ATOM   13584 C  C   . MET   E 2 291 ? 45.104  -47.667 -75.383 1.00 136.61 ? 291  MET   E C   1 
ATOM   13585 O  O   . MET   E 2 291 ? 44.371  -47.868 -76.350 1.00 132.39 ? 291  MET   E O   1 
ATOM   13586 C  CB  . MET   E 2 291 ? 47.293  -47.127 -76.449 1.00 127.45 ? 291  MET   E CB  1 
ATOM   13587 C  CG  . MET   E 2 291 ? 48.328  -46.069 -76.881 1.00 126.99 ? 291  MET   E CG  1 
ATOM   13588 S  SD  . MET   E 2 291 ? 47.620  -44.647 -77.754 1.00 149.26 ? 291  MET   E SD  1 
ATOM   13589 C  CE  . MET   E 2 291 ? 47.053  -45.423 -79.274 1.00 139.22 ? 291  MET   E CE  1 
ATOM   13590 N  N   . ASP   E 2 292 ? 44.977  -48.343 -74.246 1.00 141.82 ? 292  ASP   E N   1 
ATOM   13591 C  CA  . ASP   E 2 292 ? 43.848  -49.238 -74.011 1.00 141.65 ? 292  ASP   E CA  1 
ATOM   13592 C  C   . ASP   E 2 292 ? 42.704  -48.459 -73.373 1.00 147.56 ? 292  ASP   E C   1 
ATOM   13593 O  O   . ASP   E 2 292 ? 41.956  -49.012 -72.551 1.00 147.05 ? 292  ASP   E O   1 
ATOM   13594 C  CB  . ASP   E 2 292 ? 44.255  -50.407 -73.108 1.00 140.75 ? 292  ASP   E CB  1 
ATOM   13595 C  CG  . ASP   E 2 292 ? 44.401  -49.988 -71.651 1.00 145.67 ? 292  ASP   E CG  1 
ATOM   13596 O  OD1 . ASP   E 2 292 ? 44.698  -48.792 -71.414 1.00 148.15 ? 292  ASP   E OD1 1 
ATOM   13597 O  OD2 . ASP   E 2 292 ? 44.215  -50.842 -70.758 1.00 145.81 ? 292  ASP   E OD2 1 
ATOM   13598 N  N   . GLY   E 2 293 ? 42.587  -47.170 -73.698 1.00 150.02 ? 293  GLY   E N   1 
ATOM   13599 C  CA  . GLY   E 2 293 ? 41.599  -46.294 -73.096 1.00 149.41 ? 293  GLY   E CA  1 
ATOM   13600 C  C   . GLY   E 2 293 ? 41.823  -45.964 -71.626 1.00 149.92 ? 293  GLY   E C   1 
ATOM   13601 O  O   . GLY   E 2 293 ? 41.564  -44.830 -71.201 1.00 149.28 ? 293  GLY   E O   1 
ATOM   13602 N  N   . THR   E 2 294 ? 42.284  -46.941 -70.839 1.00 144.22 ? 294  THR   E N   1 
ATOM   13603 C  CA  . THR   E 2 294 ? 42.447  -46.743 -69.406 1.00 149.50 ? 294  THR   E CA  1 
ATOM   13604 C  C   . THR   E 2 294 ? 43.180  -45.442 -69.123 1.00 152.10 ? 294  THR   E C   1 
ATOM   13605 O  O   . THR   E 2 294 ? 44.066  -45.025 -69.878 1.00 149.66 ? 294  THR   E O   1 
ATOM   13606 C  CB  . THR   E 2 294 ? 43.218  -47.911 -68.778 1.00 149.77 ? 294  THR   E CB  1 
ATOM   13607 O  OG1 . THR   E 2 294 ? 42.525  -49.133 -69.059 1.00 154.97 ? 294  THR   E OG1 1 
ATOM   13608 C  CG2 . THR   E 2 294 ? 43.359  -47.742 -67.249 1.00 142.05 ? 294  THR   E CG2 1 
ATOM   13609 N  N   . VAL   E 2 295 ? 42.786  -44.799 -68.027 1.00 154.18 ? 295  VAL   E N   1 
ATOM   13610 C  CA  . VAL   E 2 295 ? 43.493  -43.662 -67.467 1.00 149.12 ? 295  VAL   E CA  1 
ATOM   13611 C  C   . VAL   E 2 295 ? 43.844  -44.007 -66.029 1.00 147.03 ? 295  VAL   E C   1 
ATOM   13612 O  O   . VAL   E 2 295 ? 43.000  -44.515 -65.282 1.00 146.12 ? 295  VAL   E O   1 
ATOM   13613 C  CB  . VAL   E 2 295 ? 42.644  -42.380 -67.548 1.00 149.67 ? 295  VAL   E CB  1 
ATOM   13614 C  CG1 . VAL   E 2 295 ? 43.324  -41.274 -66.780 1.00 151.29 ? 295  VAL   E CG1 1 
ATOM   13615 C  CG2 . VAL   E 2 295 ? 42.425  -41.979 -69.014 1.00 148.48 ? 295  VAL   E CG2 1 
ATOM   13616 N  N   . THR   E 2 296 ? 45.097  -43.775 -65.650 1.00 148.84 ? 296  THR   E N   1 
ATOM   13617 C  CA  . THR   E 2 296 ? 45.580  -44.164 -64.333 1.00 153.73 ? 296  THR   E CA  1 
ATOM   13618 C  C   . THR   E 2 296 ? 46.183  -42.954 -63.630 1.00 154.08 ? 296  THR   E C   1 
ATOM   13619 O  O   . THR   E 2 296 ? 46.592  -41.981 -64.275 1.00 152.66 ? 296  THR   E O   1 
ATOM   13620 C  CB  . THR   E 2 296 ? 46.612  -45.287 -64.441 1.00 153.53 ? 296  THR   E CB  1 
ATOM   13621 O  OG1 . THR   E 2 296 ? 47.390  -45.082 -65.628 1.00 152.17 ? 296  THR   E OG1 1 
ATOM   13622 C  CG2 . THR   E 2 296 ? 45.928  -46.658 -64.499 1.00 150.59 ? 296  THR   E CG2 1 
ATOM   13623 N  N   . LEU   E 2 297 ? 46.234  -43.028 -62.291 1.00 139.17 ? 297  LEU   E N   1 
ATOM   13624 C  CA  . LEU   E 2 297 ? 46.783  -41.948 -61.465 1.00 128.94 ? 297  LEU   E CA  1 
ATOM   13625 C  C   . LEU   E 2 297 ? 48.293  -42.109 -61.408 1.00 125.03 ? 297  LEU   E C   1 
ATOM   13626 O  O   . LEU   E 2 297 ? 48.817  -42.936 -60.655 1.00 117.68 ? 297  LEU   E O   1 
ATOM   13627 C  CB  . LEU   E 2 297 ? 46.176  -41.955 -60.064 1.00 123.93 ? 297  LEU   E CB  1 
ATOM   13628 C  CG  . LEU   E 2 297 ? 46.535  -40.807 -59.102 1.00 115.58 ? 297  LEU   E CG  1 
ATOM   13629 C  CD1 . LEU   E 2 297 ? 47.810  -41.093 -58.314 1.00 115.81 ? 297  LEU   E CD1 1 
ATOM   13630 C  CD2 . LEU   E 2 297 ? 46.673  -39.491 -59.851 1.00 118.67 ? 297  LEU   E CD2 1 
ATOM   13631 N  N   . LYS   E 2 298 ? 48.998  -41.305 -62.207 1.00 122.25 ? 298  LYS   E N   1 
ATOM   13632 C  CA  . LYS   E 2 298 ? 50.454  -41.356 -62.221 1.00 123.49 ? 298  LYS   E CA  1 
ATOM   13633 C  C   . LYS   E 2 298 ? 51.027  -40.749 -60.943 1.00 125.52 ? 298  LYS   E C   1 
ATOM   13634 O  O   . LYS   E 2 298 ? 51.773  -41.410 -60.202 1.00 122.46 ? 298  LYS   E O   1 
ATOM   13635 C  CB  . LYS   E 2 298 ? 50.990  -40.643 -63.468 1.00 122.37 ? 298  LYS   E CB  1 
ATOM   13636 N  N   . ASP   E 2 299 ? 50.661  -39.501 -60.647 1.00 123.43 ? 299  ASP   E N   1 
ATOM   13637 C  CA  . ASP   E 2 299 ? 51.178  -38.836 -59.462 1.00 122.32 ? 299  ASP   E CA  1 
ATOM   13638 C  C   . ASP   E 2 299 ? 50.151  -37.836 -58.933 1.00 121.05 ? 299  ASP   E C   1 
ATOM   13639 O  O   . ASP   E 2 299 ? 49.046  -37.699 -59.469 1.00 118.98 ? 299  ASP   E O   1 
ATOM   13640 C  CB  . ASP   E 2 299 ? 52.519  -38.167 -59.775 1.00 124.17 ? 299  ASP   E CB  1 
ATOM   13641 C  CG  . ASP   E 2 299 ? 53.305  -37.829 -58.519 1.00 127.65 ? 299  ASP   E CG  1 
ATOM   13642 O  OD1 . ASP   E 2 299 ? 53.555  -38.747 -57.699 1.00 127.21 ? 299  ASP   E OD1 1 
ATOM   13643 O  OD2 . ASP   E 2 299 ? 53.672  -36.643 -58.354 1.00 126.07 ? 299  ASP   E OD2 1 
ATOM   13644 N  N   . LEU   E 2 300 ? 50.543  -37.144 -57.851 1.00 121.99 ? 300  LEU   E N   1 
ATOM   13645 C  CA  . LEU   E 2 300 ? 49.774  -36.108 -57.163 1.00 117.32 ? 300  LEU   E CA  1 
ATOM   13646 C  C   . LEU   E 2 300 ? 50.683  -34.914 -56.877 1.00 118.73 ? 300  LEU   E C   1 
ATOM   13647 O  O   . LEU   E 2 300 ? 51.724  -35.077 -56.233 1.00 122.50 ? 300  LEU   E O   1 
ATOM   13648 C  CB  . LEU   E 2 300 ? 49.205  -36.630 -55.835 1.00 113.53 ? 300  LEU   E CB  1 
ATOM   13649 C  CG  . LEU   E 2 300 ? 47.899  -37.421 -55.823 1.00 111.42 ? 300  LEU   E CG  1 
ATOM   13650 C  CD1 . LEU   E 2 300 ? 47.596  -37.914 -54.419 1.00 109.08 ? 300  LEU   E CD1 1 
ATOM   13651 C  CD2 . LEU   E 2 300 ? 46.763  -36.560 -56.338 1.00 114.13 ? 300  LEU   E CD2 1 
ATOM   13652 N  N   . ARG   E 2 301 ? 50.284  -33.713 -57.322 1.00 114.53 ? 301  ARG   E N   1 
ATOM   13653 C  CA  . ARG   E 2 301 ? 51.014  -32.477 -57.031 1.00 115.55 ? 301  ARG   E CA  1 
ATOM   13654 C  C   . ARG   E 2 301 ? 50.136  -31.488 -56.269 1.00 113.97 ? 301  ARG   E C   1 
ATOM   13655 O  O   . ARG   E 2 301 ? 48.979  -31.260 -56.636 1.00 113.19 ? 301  ARG   E O   1 
ATOM   13656 C  CB  . ARG   E 2 301 ? 51.523  -31.795 -58.319 1.00 110.97 ? 301  ARG   E CB  1 
ATOM   13657 N  N   . VAL   E 2 302 ? 50.690  -30.892 -55.212 1.00 117.96 ? 302  VAL   E N   1 
ATOM   13658 C  CA  . VAL   E 2 302 ? 50.047  -29.798 -54.493 1.00 119.17 ? 302  VAL   E CA  1 
ATOM   13659 C  C   . VAL   E 2 302 ? 50.792  -28.513 -54.803 1.00 121.57 ? 302  VAL   E C   1 
ATOM   13660 O  O   . VAL   E 2 302 ? 52.007  -28.427 -54.589 1.00 121.19 ? 302  VAL   E O   1 
ATOM   13661 C  CB  . VAL   E 2 302 ? 50.017  -30.030 -52.976 1.00 113.07 ? 302  VAL   E CB  1 
ATOM   13662 C  CG1 . VAL   E 2 302 ? 49.519  -28.770 -52.302 1.00 113.47 ? 302  VAL   E CG1 1 
ATOM   13663 C  CG2 . VAL   E 2 302 ? 49.120  -31.190 -52.645 1.00 110.81 ? 302  VAL   E CG2 1 
ATOM   13664 N  N   . GLU   E 2 303 ? 50.071  -27.517 -55.299 1.00 134.83 ? 303  GLU   E N   1 
ATOM   13665 C  CA  . GLU   E 2 303 ? 50.653  -26.224 -55.622 1.00 136.24 ? 303  GLU   E CA  1 
ATOM   13666 C  C   . GLU   E 2 303 ? 49.978  -25.148 -54.788 1.00 135.46 ? 303  GLU   E C   1 
ATOM   13667 O  O   . GLU   E 2 303 ? 48.759  -25.181 -54.588 1.00 135.42 ? 303  GLU   E O   1 
ATOM   13668 C  CB  . GLU   E 2 303 ? 50.516  -25.902 -57.112 1.00 138.12 ? 303  GLU   E CB  1 
ATOM   13669 C  CG  . GLU   E 2 303 ? 51.518  -26.640 -57.996 1.00 143.18 ? 303  GLU   E CG  1 
ATOM   13670 C  CD  . GLU   E 2 303 ? 52.938  -26.124 -57.834 1.00 145.73 ? 303  GLU   E CD  1 
ATOM   13671 O  OE1 . GLU   E 2 303 ? 53.117  -24.880 -57.801 1.00 144.73 ? 303  GLU   E OE1 1 
ATOM   13672 O  OE2 . GLU   E 2 303 ? 53.866  -26.966 -57.736 1.00 142.30 ? 303  GLU   E OE2 1 
ATOM   13673 N  N   . LEU   E 2 304 ? 50.775  -24.207 -54.291 1.00 121.57 ? 304  LEU   E N   1 
ATOM   13674 C  CA  . LEU   E 2 304 ? 50.264  -23.107 -53.486 1.00 113.83 ? 304  LEU   E CA  1 
ATOM   13675 C  C   . LEU   E 2 304 ? 49.964  -21.912 -54.378 1.00 108.61 ? 304  LEU   E C   1 
ATOM   13676 O  O   . LEU   E 2 304 ? 50.805  -21.502 -55.181 1.00 106.40 ? 304  LEU   E O   1 
ATOM   13677 C  CB  . LEU   E 2 304 ? 51.269  -22.715 -52.407 1.00 108.80 ? 304  LEU   E CB  1 
ATOM   13678 C  CG  . LEU   E 2 304 ? 51.024  -21.364 -51.752 1.00 102.56 ? 304  LEU   E CG  1 
ATOM   13679 C  CD1 . LEU   E 2 304 ? 51.692  -21.376 -50.404 1.00 98.20  ? 304  LEU   E CD1 1 
ATOM   13680 C  CD2 . LEU   E 2 304 ? 51.549  -20.218 -52.616 1.00 107.79 ? 304  LEU   E CD2 1 
ATOM   13681 N  N   . LEU   E 2 305 ? 48.779  -21.337 -54.209 1.00 105.12 ? 305  LEU   E N   1 
ATOM   13682 C  CA  . LEU   E 2 305 ? 48.379  -20.238 -55.071 1.00 110.60 ? 305  LEU   E CA  1 
ATOM   13683 C  C   . LEU   E 2 305 ? 48.698  -18.887 -54.438 1.00 110.71 ? 305  LEU   E C   1 
ATOM   13684 O  O   . LEU   E 2 305 ? 49.312  -18.032 -55.086 1.00 114.85 ? 305  LEU   E O   1 
ATOM   13685 C  CB  . LEU   E 2 305 ? 46.889  -20.365 -55.413 1.00 104.21 ? 305  LEU   E CB  1 
ATOM   13686 C  CG  . LEU   E 2 305 ? 46.540  -21.676 -56.129 1.00 105.07 ? 305  LEU   E CG  1 
ATOM   13687 C  CD1 . LEU   E 2 305 ? 45.036  -21.898 -56.263 1.00 105.88 ? 305  LEU   E CD1 1 
ATOM   13688 C  CD2 . LEU   E 2 305 ? 47.195  -21.716 -57.487 1.00 111.21 ? 305  LEU   E CD2 1 
ATOM   13689 N  N   . GLY   E 2 306 ? 48.309  -18.692 -53.178 1.00 108.38 ? 306  GLY   E N   1 
ATOM   13690 C  CA  . GLY   E 2 306 ? 48.496  -17.410 -52.511 1.00 109.63 ? 306  GLY   E CA  1 
ATOM   13691 C  C   . GLY   E 2 306 ? 47.757  -17.356 -51.177 1.00 105.74 ? 306  GLY   E C   1 
ATOM   13692 O  O   . GLY   E 2 306 ? 47.447  -18.390 -50.586 1.00 105.44 ? 306  GLY   E O   1 
ATOM   13693 N  N   . GLU   E 2 307 ? 47.480  -16.135 -50.712 1.00 102.01 ? 307  GLU   E N   1 
ATOM   13694 C  CA  . GLU   E 2 307 ? 46.755  -15.919 -49.462 1.00 97.22  ? 307  GLU   E CA  1 
ATOM   13695 C  C   . GLU   E 2 307 ? 45.344  -15.400 -49.733 1.00 93.72  ? 307  GLU   E C   1 
ATOM   13696 O  O   . GLU   E 2 307 ? 45.144  -14.563 -50.615 1.00 93.26  ? 307  GLU   E O   1 
ATOM   13697 C  CB  . GLU   E 2 307 ? 47.499  -14.928 -48.558 1.00 101.29 ? 307  GLU   E CB  1 
ATOM   13698 C  CG  . GLU   E 2 307 ? 48.630  -15.530 -47.724 1.00 108.16 ? 307  GLU   E CG  1 
ATOM   13699 C  CD  . GLU   E 2 307 ? 48.601  -15.036 -46.272 1.00 113.02 ? 307  GLU   E CD  1 
ATOM   13700 O  OE1 . GLU   E 2 307 ? 48.095  -13.901 -46.031 1.00 106.36 ? 307  GLU   E OE1 1 
ATOM   13701 O  OE2 . GLU   E 2 307 ? 49.067  -15.795 -45.377 1.00 111.48 ? 307  GLU   E OE2 1 
ATOM   13702 N  N   . THR   E 2 308 ? 44.361  -15.904 -48.979 1.00 93.03  ? 308  THR   E N   1 
ATOM   13703 C  CA  . THR   E 2 308 ? 43.013  -15.330 -48.997 1.00 92.03  ? 308  THR   E CA  1 
ATOM   13704 C  C   . THR   E 2 308 ? 42.564  -15.103 -47.559 1.00 88.50  ? 308  THR   E C   1 
ATOM   13705 O  O   . THR   E 2 308 ? 43.375  -15.226 -46.638 1.00 89.36  ? 308  THR   E O   1 
ATOM   13706 C  CB  . THR   E 2 308 ? 42.000  -16.222 -49.746 1.00 94.00  ? 308  THR   E CB  1 
ATOM   13707 O  OG1 . THR   E 2 308 ? 41.566  -17.300 -48.903 1.00 86.95  ? 308  THR   E OG1 1 
ATOM   13708 C  CG2 . THR   E 2 308 ? 42.598  -16.791 -51.036 1.00 91.53  ? 308  THR   E CG2 1 
ATOM   13709 N  N   . SER   E 2 309 ? 41.295  -14.755 -47.342 1.00 86.28  ? 309  SER   E N   1 
ATOM   13710 C  CA  . SER   E 2 309 ? 40.800  -14.698 -45.971 1.00 90.94  ? 309  SER   E CA  1 
ATOM   13711 C  C   . SER   E 2 309 ? 40.793  -16.101 -45.380 1.00 89.77  ? 309  SER   E C   1 
ATOM   13712 O  O   . SER   E 2 309 ? 40.647  -17.096 -46.097 1.00 90.06  ? 309  SER   E O   1 
ATOM   13713 C  CB  . SER   E 2 309 ? 39.375  -14.121 -45.893 1.00 86.37  ? 309  SER   E CB  1 
ATOM   13714 O  OG  . SER   E 2 309 ? 39.279  -12.789 -46.348 1.00 82.02  ? 309  SER   E OG  1 
ATOM   13715 N  N   . ILE   E 2 310 ? 40.940  -16.175 -44.058 1.00 86.23  ? 310  ILE   E N   1 
ATOM   13716 C  CA  . ILE   E 2 310 ? 40.807  -17.436 -43.343 1.00 81.67  ? 310  ILE   E CA  1 
ATOM   13717 C  C   . ILE   E 2 310 ? 39.564  -17.999 -44.024 1.00 85.47  ? 310  ILE   E C   1 
ATOM   13718 O  O   . ILE   E 2 310 ? 38.498  -17.364 -44.007 1.00 82.17  ? 310  ILE   E O   1 
ATOM   13719 C  CB  . ILE   E 2 310 ? 40.731  -17.203 -41.825 1.00 88.57  ? 310  ILE   E CB  1 
ATOM   13720 C  CG1 . ILE   E 2 310 ? 42.048  -16.642 -41.278 1.00 86.98  ? 310  ILE   E CG1 1 
ATOM   13721 C  CG2 . ILE   E 2 310 ? 40.251  -18.468 -41.116 1.00 83.81  ? 310  ILE   E CG2 1 
ATOM   13722 C  CD1 . ILE   E 2 310 ? 43.157  -17.661 -41.159 1.00 91.85  ? 310  ILE   E CD1 1 
ATOM   13723 N  N   . ALA   E 2 311 ? 39.689  -19.204 -44.600 1.00 86.39  ? 311  ALA   E N   1 
ATOM   13724 C  CA  . ALA   E 2 311 ? 38.648  -19.800 -45.428 1.00 77.64  ? 311  ALA   E CA  1 
ATOM   13725 C  C   . ALA   E 2 311 ? 37.902  -20.765 -44.517 1.00 79.67  ? 311  ALA   E C   1 
ATOM   13726 O  O   . ALA   E 2 311 ? 38.509  -21.589 -43.826 1.00 83.29  ? 311  ALA   E O   1 
ATOM   13727 C  CB  . ALA   E 2 311 ? 39.182  -20.548 -46.643 1.00 82.77  ? 311  ALA   E CB  1 
ATOM   13728 N  N   . GLU   E 2 312 ? 36.580  -20.642 -44.504 1.00 77.83  ? 312  GLU   E N   1 
ATOM   13729 C  CA  . GLU   E 2 312 ? 35.698  -21.617 -43.884 1.00 81.44  ? 312  GLU   E CA  1 
ATOM   13730 C  C   . GLU   E 2 312 ? 35.166  -22.581 -44.925 1.00 88.82  ? 312  GLU   E C   1 
ATOM   13731 O  O   . GLU   E 2 312 ? 35.245  -23.793 -44.743 1.00 96.68  ? 312  GLU   E O   1 
ATOM   13732 C  CB  . GLU   E 2 312 ? 34.525  -20.926 -43.168 1.00 80.48  ? 312  GLU   E CB  1 
ATOM   13733 C  CG  . GLU   E 2 312 ? 33.524  -21.892 -42.588 1.00 81.93  ? 312  GLU   E CG  1 
ATOM   13734 C  CD  . GLU   E 2 312 ? 34.119  -22.705 -41.459 1.00 92.24  ? 312  GLU   E CD  1 
ATOM   13735 O  OE1 . GLU   E 2 312 ? 35.359  -22.674 -41.288 1.00 90.49  ? 312  GLU   E OE1 1 
ATOM   13736 O  OE2 . GLU   E 2 312 ? 33.350  -23.360 -40.726 1.00 97.53  ? 312  GLU   E OE2 1 
ATOM   13737 N  N   . CYS   E 2 313 ? 34.642  -22.046 -46.027 1.00 91.00  ? 313  CYS   E N   1 
ATOM   13738 C  CA  . CYS   E 2 313 ? 34.169  -22.817 -47.161 1.00 91.84  ? 313  CYS   E CA  1 
ATOM   13739 C  C   . CYS   E 2 313 ? 34.755  -22.229 -48.445 1.00 92.01  ? 313  CYS   E C   1 
ATOM   13740 O  O   . CYS   E 2 313 ? 35.037  -21.033 -48.511 1.00 91.94  ? 313  CYS   E O   1 
ATOM   13741 C  CB  . CYS   E 2 313 ? 32.636  -22.820 -47.182 1.00 92.68  ? 313  CYS   E CB  1 
ATOM   13742 S  SG  . CYS   E 2 313 ? 31.923  -21.281 -47.809 1.00 102.32 ? 313  CYS   E SG  1 
ATOM   13743 N  N   . LEU   E 2 314 ? 34.961  -23.084 -49.464 1.00 93.83  ? 314  LEU   E N   1 
ATOM   13744 C  CA  . LEU   E 2 314 ? 35.528  -22.687 -50.753 1.00 89.38  ? 314  LEU   E CA  1 
ATOM   13745 C  C   . LEU   E 2 314 ? 34.686  -23.217 -51.903 1.00 93.25  ? 314  LEU   E C   1 
ATOM   13746 O  O   . LEU   E 2 314 ? 34.148  -24.327 -51.844 1.00 97.72  ? 314  LEU   E O   1 
ATOM   13747 C  CB  . LEU   E 2 314 ? 36.966  -23.180 -50.943 1.00 88.35  ? 314  LEU   E CB  1 
ATOM   13748 C  CG  . LEU   E 2 314 ? 38.063  -22.269 -50.390 1.00 91.39  ? 314  LEU   E CG  1 
ATOM   13749 C  CD1 . LEU   E 2 314 ? 39.405  -22.575 -51.055 1.00 91.23  ? 314  LEU   E CD1 1 
ATOM   13750 C  CD2 . LEU   E 2 314 ? 37.694  -20.796 -50.532 1.00 85.62  ? 314  LEU   E CD2 1 
ATOM   13751 N  N   . THR   E 2 315 ? 34.605  -22.432 -52.969 1.00 92.70  ? 315  THR   E N   1 
ATOM   13752 C  CA  . THR   E 2 315 ? 33.759  -22.791 -54.097 1.00 90.81  ? 315  THR   E CA  1 
ATOM   13753 C  C   . THR   E 2 315 ? 34.306  -22.099 -55.344 1.00 91.00  ? 315  THR   E C   1 
ATOM   13754 O  O   . THR   E 2 315 ? 34.406  -20.873 -55.385 1.00 93.16  ? 315  THR   E O   1 
ATOM   13755 C  CB  . THR   E 2 315 ? 32.291  -22.421 -53.785 1.00 91.16  ? 315  THR   E CB  1 
ATOM   13756 O  OG1 . THR   E 2 315 ? 31.398  -23.239 -54.543 1.00 100.38 ? 315  THR   E OG1 1 
ATOM   13757 C  CG2 . THR   E 2 315 ? 31.970  -20.958 -54.071 1.00 100.35 ? 315  THR   E CG2 1 
ATOM   13758 N  N   . TYR   E 2 316 ? 34.737  -22.883 -56.331 1.00 96.62  ? 316  TYR   E N   1 
ATOM   13759 C  CA  . TYR   E 2 316 ? 35.180  -22.318 -57.596 1.00 98.72  ? 316  TYR   E CA  1 
ATOM   13760 C  C   . TYR   E 2 316 ? 33.960  -21.967 -58.430 1.00 98.18  ? 316  TYR   E C   1 
ATOM   13761 O  O   . TYR   E 2 316 ? 33.002  -22.740 -58.511 1.00 98.28  ? 316  TYR   E O   1 
ATOM   13762 C  CB  . TYR   E 2 316 ? 36.086  -23.294 -58.353 1.00 95.84  ? 316  TYR   E CB  1 
ATOM   13763 C  CG  . TYR   E 2 316 ? 36.423  -22.880 -59.775 1.00 107.26 ? 316  TYR   E CG  1 
ATOM   13764 C  CD1 . TYR   E 2 316 ? 35.458  -22.916 -60.788 1.00 112.22 ? 316  TYR   E CD1 1 
ATOM   13765 C  CD2 . TYR   E 2 316 ? 37.717  -22.464 -60.124 1.00 113.25 ? 316  TYR   E CD2 1 
ATOM   13766 C  CE1 . TYR   E 2 316 ? 35.759  -22.540 -62.110 1.00 113.29 ? 316  TYR   E CE1 1 
ATOM   13767 C  CE2 . TYR   E 2 316 ? 38.035  -22.092 -61.456 1.00 115.34 ? 316  TYR   E CE2 1 
ATOM   13768 C  CZ  . TYR   E 2 316 ? 37.043  -22.135 -62.435 1.00 114.20 ? 316  TYR   E CZ  1 
ATOM   13769 O  OH  . TYR   E 2 316 ? 37.307  -21.783 -63.739 1.00 115.11 ? 316  TYR   E OH  1 
ATOM   13770 N  N   . LEU   E 2 317 ? 33.996  -20.793 -59.049 1.00 99.61  ? 317  LEU   E N   1 
ATOM   13771 C  CA  . LEU   E 2 317 ? 32.850  -20.331 -59.818 1.00 102.17 ? 317  LEU   E CA  1 
ATOM   13772 C  C   . LEU   E 2 317 ? 33.097  -20.507 -61.316 1.00 111.13 ? 317  LEU   E C   1 
ATOM   13773 O  O   . LEU   E 2 317 ? 32.497  -21.381 -61.958 1.00 106.43 ? 317  LEU   E O   1 
ATOM   13774 C  CB  . LEU   E 2 317 ? 32.538  -18.875 -59.468 1.00 101.13 ? 317  LEU   E CB  1 
ATOM   13775 C  CG  . LEU   E 2 317 ? 32.236  -18.644 -57.984 1.00 102.33 ? 317  LEU   E CG  1 
ATOM   13776 C  CD1 . LEU   E 2 317 ? 32.264  -17.155 -57.661 1.00 100.35 ? 317  LEU   E CD1 1 
ATOM   13777 C  CD2 . LEU   E 2 317 ? 30.895  -19.249 -57.604 1.00 94.08  ? 317  LEU   E CD2 1 
ATOM   13778 N  N   . ASP   E 2 318 ? 33.975  -19.688 -61.888 1.00 116.32 ? 318  ASP   E N   1 
ATOM   13779 C  CA  . ASP   E 2 318 ? 34.273  -19.786 -63.311 1.00 115.63 ? 318  ASP   E CA  1 
ATOM   13780 C  C   . ASP   E 2 318 ? 35.327  -18.747 -63.662 1.00 113.95 ? 318  ASP   E C   1 
ATOM   13781 O  O   . ASP   E 2 318 ? 35.549  -17.782 -62.925 1.00 113.63 ? 318  ASP   E O   1 
ATOM   13782 C  CB  . ASP   E 2 318 ? 33.022  -19.591 -64.174 1.00 115.24 ? 318  ASP   E CB  1 
ATOM   13783 C  CG  . ASP   E 2 318 ? 33.202  -20.115 -65.577 1.00 119.88 ? 318  ASP   E CG  1 
ATOM   13784 O  OD1 . ASP   E 2 318 ? 33.628  -21.283 -65.717 1.00 125.43 ? 318  ASP   E OD1 1 
ATOM   13785 O  OD2 . ASP   E 2 318 ? 32.909  -19.371 -66.535 1.00 122.52 ? 318  ASP   E OD2 1 
ATOM   13786 N  N   . ASN   E 2 319 ? 35.977  -18.969 -64.798 1.00 114.93 ? 319  ASN   E N   1 
ATOM   13787 C  CA  . ASN   E 2 319 ? 37.009  -18.066 -65.269 1.00 116.05 ? 319  ASN   E CA  1 
ATOM   13788 C  C   . ASN   E 2 319 ? 37.992  -17.738 -64.146 1.00 110.82 ? 319  ASN   E C   1 
ATOM   13789 O  O   . ASN   E 2 319 ? 38.537  -16.638 -64.074 1.00 112.44 ? 319  ASN   E O   1 
ATOM   13790 C  CB  . ASN   E 2 319 ? 36.365  -16.806 -65.850 1.00 116.48 ? 319  ASN   E CB  1 
ATOM   13791 C  CG  . ASN   E 2 319 ? 35.073  -17.118 -66.583 1.00 119.68 ? 319  ASN   E CG  1 
ATOM   13792 O  OD1 . ASN   E 2 319 ? 33.986  -16.756 -66.133 1.00 119.54 ? 319  ASN   E OD1 1 
ATOM   13793 N  ND2 . ASN   E 2 319 ? 35.186  -17.808 -67.713 1.00 124.91 ? 319  ASN   E ND2 1 
ATOM   13794 N  N   . GLY   E 2 320 ? 38.203  -18.699 -63.244 1.00 114.45 ? 320  GLY   E N   1 
ATOM   13795 C  CA  . GLY   E 2 320 ? 39.202  -18.581 -62.200 1.00 117.06 ? 320  GLY   E CA  1 
ATOM   13796 C  C   . GLY   E 2 320 ? 38.823  -17.741 -61.004 1.00 108.74 ? 320  GLY   E C   1 
ATOM   13797 O  O   . GLY   E 2 320 ? 39.700  -17.406 -60.199 1.00 104.70 ? 320  GLY   E O   1 
ATOM   13798 N  N   . VAL   E 2 321 ? 37.568  -17.367 -60.865 1.00 105.40 ? 321  VAL   E N   1 
ATOM   13799 C  CA  . VAL   E 2 321 ? 37.115  -16.684 -59.661 1.00 105.50 ? 321  VAL   E CA  1 
ATOM   13800 C  C   . VAL   E 2 321 ? 36.656  -17.740 -58.668 1.00 104.12 ? 321  VAL   E C   1 
ATOM   13801 O  O   . VAL   E 2 321 ? 35.826  -18.600 -58.995 1.00 103.24 ? 321  VAL   E O   1 
ATOM   13802 C  CB  . VAL   E 2 321 ? 35.996  -15.683 -59.965 1.00 102.15 ? 321  VAL   E CB  1 
ATOM   13803 C  CG1 . VAL   E 2 321 ? 36.538  -14.529 -60.757 1.00 102.67 ? 321  VAL   E CG1 1 
ATOM   13804 C  CG2 . VAL   E 2 321 ? 34.882  -16.374 -60.716 1.00 105.57 ? 321  VAL   E CG2 1 
ATOM   13805 N  N   . VAL   E 2 322 ? 37.217  -17.686 -57.464 1.00 96.13  ? 322  VAL   E N   1 
ATOM   13806 C  CA  . VAL   E 2 322 ? 36.859  -18.572 -56.373 1.00 92.99  ? 322  VAL   E CA  1 
ATOM   13807 C  C   . VAL   E 2 322 ? 36.184  -17.724 -55.320 1.00 94.66  ? 322  VAL   E C   1 
ATOM   13808 O  O   . VAL   E 2 322 ? 36.774  -16.752 -54.835 1.00 100.72 ? 322  VAL   E O   1 
ATOM   13809 C  CB  . VAL   E 2 322 ? 38.082  -19.291 -55.786 1.00 91.29  ? 322  VAL   E CB  1 
ATOM   13810 C  CG1 . VAL   E 2 322 ? 37.772  -19.775 -54.407 1.00 86.40  ? 322  VAL   E CG1 1 
ATOM   13811 C  CG2 . VAL   E 2 322 ? 38.444  -20.456 -56.664 1.00 102.45 ? 322  VAL   E CG2 1 
ATOM   13812 N  N   . PHE   E 2 323 ? 34.951  -18.067 -54.978 1.00 91.37  ? 323  PHE   E N   1 
ATOM   13813 C  CA  . PHE   E 2 323 ? 34.326  -17.451 -53.822 1.00 90.50  ? 323  PHE   E CA  1 
ATOM   13814 C  C   . PHE   E 2 323 ? 34.927  -18.056 -52.562 1.00 90.97  ? 323  PHE   E C   1 
ATOM   13815 O  O   . PHE   E 2 323 ? 34.819  -19.267 -52.350 1.00 92.71  ? 323  PHE   E O   1 
ATOM   13816 C  CB  . PHE   E 2 323 ? 32.815  -17.651 -53.825 1.00 90.54  ? 323  PHE   E CB  1 
ATOM   13817 C  CG  . PHE   E 2 323 ? 32.165  -17.167 -52.567 1.00 93.34  ? 323  PHE   E CG  1 
ATOM   13818 C  CD1 . PHE   E 2 323 ? 32.140  -15.810 -52.278 1.00 87.48  ? 323  PHE   E CD1 1 
ATOM   13819 C  CD2 . PHE   E 2 323 ? 31.620  -18.058 -51.652 1.00 89.99  ? 323  PHE   E CD2 1 
ATOM   13820 C  CE1 . PHE   E 2 323 ? 31.568  -15.351 -51.139 1.00 83.67  ? 323  PHE   E CE1 1 
ATOM   13821 C  CE2 . PHE   E 2 323 ? 31.040  -17.591 -50.493 1.00 88.09  ? 323  PHE   E CE2 1 
ATOM   13822 C  CZ  . PHE   E 2 323 ? 31.019  -16.237 -50.238 1.00 87.96  ? 323  PHE   E CZ  1 
ATOM   13823 N  N   . VAL   E 2 324 ? 35.546  -17.226 -51.727 1.00 89.33  ? 324  VAL   E N   1 
ATOM   13824 C  CA  . VAL   E 2 324 ? 36.146  -17.667 -50.474 1.00 83.59  ? 324  VAL   E CA  1 
ATOM   13825 C  C   . VAL   E 2 324 ? 35.211  -17.257 -49.346 1.00 85.81  ? 324  VAL   E C   1 
ATOM   13826 O  O   . VAL   E 2 324 ? 35.086  -16.072 -49.028 1.00 88.26  ? 324  VAL   E O   1 
ATOM   13827 C  CB  . VAL   E 2 324 ? 37.542  -17.069 -50.286 1.00 83.01  ? 324  VAL   E CB  1 
ATOM   13828 C  CG1 . VAL   E 2 324 ? 38.227  -17.681 -49.109 1.00 81.65  ? 324  VAL   E CG1 1 
ATOM   13829 C  CG2 . VAL   E 2 324 ? 38.368  -17.263 -51.544 1.00 86.90  ? 324  VAL   E CG2 1 
ATOM   13830 N  N   . GLY   E 2 325 ? 34.541  -18.227 -48.728 1.00 87.03  ? 325  GLY   E N   1 
ATOM   13831 C  CA  . GLY   E 2 325 ? 33.648  -17.952 -47.607 1.00 85.58  ? 325  GLY   E CA  1 
ATOM   13832 C  C   . GLY   E 2 325 ? 34.391  -17.982 -46.282 1.00 78.35  ? 325  GLY   E C   1 
ATOM   13833 O  O   . GLY   E 2 325 ? 35.135  -18.921 -46.001 1.00 74.62  ? 325  GLY   E O   1 
ATOM   13834 N  N   . SER   E 2 326 ? 34.188  -16.939 -45.470 1.00 84.43  ? 326  SER   E N   1 
ATOM   13835 C  CA  . SER   E 2 326 ? 34.963  -16.694 -44.256 1.00 80.72  ? 326  SER   E CA  1 
ATOM   13836 C  C   . SER   E 2 326 ? 34.038  -16.532 -43.057 1.00 79.80  ? 326  SER   E C   1 
ATOM   13837 O  O   . SER   E 2 326 ? 32.956  -15.943 -43.175 1.00 78.54  ? 326  SER   E O   1 
ATOM   13838 C  CB  . SER   E 2 326 ? 35.852  -15.442 -44.402 1.00 77.81  ? 326  SER   E CB  1 
ATOM   13839 O  OG  . SER   E 2 326 ? 36.921  -15.444 -43.476 1.00 83.84  ? 326  SER   E OG  1 
ATOM   13840 N  N   . ARG   E 2 327 ? 34.477  -17.078 -41.911 1.00 80.63  ? 327  ARG   E N   1 
ATOM   13841 C  CA  . ARG   E 2 327 ? 33.819  -16.946 -40.608 1.00 80.36  ? 327  ARG   E CA  1 
ATOM   13842 C  C   . ARG   E 2 327 ? 34.528  -15.942 -39.719 1.00 78.53  ? 327  ARG   E C   1 
ATOM   13843 O  O   . ARG   E 2 327 ? 33.935  -15.450 -38.747 1.00 76.34  ? 327  ARG   E O   1 
ATOM   13844 C  CB  . ARG   E 2 327 ? 33.782  -18.309 -39.877 1.00 79.10  ? 327  ARG   E CB  1 
ATOM   13845 C  CG  . ARG   E 2 327 ? 32.452  -19.009 -39.875 1.00 77.77  ? 327  ARG   E CG  1 
ATOM   13846 C  CD  . ARG   E 2 327 ? 31.454  -18.293 -38.972 1.00 86.15  ? 327  ARG   E CD  1 
ATOM   13847 N  NE  . ARG   E 2 327 ? 31.386  -18.920 -37.658 1.00 95.55  ? 327  ARG   E NE  1 
ATOM   13848 C  CZ  . ARG   E 2 327 ? 30.698  -20.030 -37.414 1.00 105.32 ? 327  ARG   E CZ  1 
ATOM   13849 N  NH1 . ARG   E 2 327 ? 29.924  -20.579 -38.341 1.00 105.95 ? 327  ARG   E NH1 1 
ATOM   13850 N  NH2 . ARG   E 2 327 ? 30.810  -20.623 -36.224 1.00 108.64 ? 327  ARG   E NH2 1 
ATOM   13851 N  N   . LEU   E 2 328 ? 35.788  -15.657 -40.043 1.00 77.12  ? 328  LEU   E N   1 
ATOM   13852 C  CA  . LEU   E 2 328 ? 36.678  -14.829 -39.252 1.00 80.46  ? 328  LEU   E CA  1 
ATOM   13853 C  C   . LEU   E 2 328 ? 37.026  -13.521 -39.928 1.00 83.98  ? 328  LEU   E C   1 
ATOM   13854 O  O   . LEU   E 2 328 ? 37.230  -12.521 -39.245 1.00 84.66  ? 328  LEU   E O   1 
ATOM   13855 C  CB  . LEU   E 2 328 ? 37.979  -15.586 -38.960 1.00 81.22  ? 328  LEU   E CB  1 
ATOM   13856 C  CG  . LEU   E 2 328 ? 37.963  -16.455 -37.709 1.00 80.95  ? 328  LEU   E CG  1 
ATOM   13857 C  CD1 . LEU   E 2 328 ? 36.765  -17.378 -37.731 1.00 75.01  ? 328  LEU   E CD1 1 
ATOM   13858 C  CD2 . LEU   E 2 328 ? 39.266  -17.242 -37.617 1.00 76.64  ? 328  LEU   E CD2 1 
ATOM   13859 N  N   . GLY   E 2 329 ? 37.126  -13.507 -41.244 1.00 84.80  ? 329  GLY   E N   1 
ATOM   13860 C  CA  . GLY   E 2 329 ? 37.352  -12.263 -41.946 1.00 85.46  ? 329  GLY   E CA  1 
ATOM   13861 C  C   . GLY   E 2 329 ? 36.243  -11.935 -42.928 1.00 82.27  ? 329  GLY   E C   1 
ATOM   13862 O  O   . GLY   E 2 329 ? 35.136  -12.482 -42.853 1.00 76.90  ? 329  GLY   E O   1 
ATOM   13863 N  N   . ASP   E 2 330 ? 36.521  -11.033 -43.857 1.00 81.03  ? 330  ASP   E N   1 
ATOM   13864 C  CA  . ASP   E 2 330 ? 35.543  -10.775 -44.891 1.00 82.71  ? 330  ASP   E CA  1 
ATOM   13865 C  C   . ASP   E 2 330 ? 35.567  -11.926 -45.887 1.00 83.80  ? 330  ASP   E C   1 
ATOM   13866 O  O   . ASP   E 2 330 ? 36.617  -12.539 -46.130 1.00 81.85  ? 330  ASP   E O   1 
ATOM   13867 C  CB  . ASP   E 2 330 ? 35.821  -9.426  -45.561 1.00 85.60  ? 330  ASP   E CB  1 
ATOM   13868 C  CG  . ASP   E 2 330 ? 35.807  -8.275  -44.556 1.00 87.40  ? 330  ASP   E CG  1 
ATOM   13869 O  OD1 . ASP   E 2 330 ? 34.993  -8.351  -43.605 1.00 86.04  ? 330  ASP   E OD1 1 
ATOM   13870 O  OD2 . ASP   E 2 330 ? 36.619  -7.321  -44.685 1.00 90.42  ? 330  ASP   E OD2 1 
ATOM   13871 N  N   . SER   E 2 331 ? 34.388  -12.271 -46.401 1.00 81.91  ? 331  SER   E N   1 
ATOM   13872 C  CA  . SER   E 2 331 ? 34.344  -13.160 -47.538 1.00 82.04  ? 331  SER   E CA  1 
ATOM   13873 C  C   . SER   E 2 331 ? 34.715  -12.366 -48.771 1.00 83.01  ? 331  SER   E C   1 
ATOM   13874 O  O   . SER   E 2 331 ? 34.624  -11.145 -48.792 1.00 83.15  ? 331  SER   E O   1 
ATOM   13875 C  CB  . SER   E 2 331 ? 32.963  -13.793 -47.685 1.00 83.71  ? 331  SER   E CB  1 
ATOM   13876 O  OG  . SER   E 2 331 ? 32.627  -14.513 -46.506 1.00 88.15  ? 331  SER   E OG  1 
ATOM   13877 N  N   . GLN   E 2 332 ? 35.145  -13.066 -49.809 1.00 90.04  ? 332  GLN   E N   1 
ATOM   13878 C  CA  . GLN   E 2 332 ? 35.742  -12.379 -50.938 1.00 83.93  ? 332  GLN   E CA  1 
ATOM   13879 C  C   . GLN   E 2 332 ? 35.652  -13.258 -52.181 1.00 89.43  ? 332  GLN   E C   1 
ATOM   13880 O  O   . GLN   E 2 332 ? 35.609  -14.487 -52.092 1.00 89.08  ? 332  GLN   E O   1 
ATOM   13881 C  CB  . GLN   E 2 332 ? 37.192  -12.033 -50.615 1.00 79.00  ? 332  GLN   E CB  1 
ATOM   13882 C  CG  . GLN   E 2 332 ? 37.901  -13.234 -50.074 1.00 84.06  ? 332  GLN   E CG  1 
ATOM   13883 C  CD  . GLN   E 2 332 ? 39.347  -12.975 -49.769 1.00 88.33  ? 332  GLN   E CD  1 
ATOM   13884 O  OE1 . GLN   E 2 332 ? 40.063  -13.859 -49.277 1.00 90.59  ? 332  GLN   E OE1 1 
ATOM   13885 N  NE2 . GLN   E 2 332 ? 39.799  -11.758 -50.064 1.00 84.83  ? 332  GLN   E NE2 1 
ATOM   13886 N  N   . LEU   E 2 333 ? 35.599  -12.604 -53.341 1.00 94.98  ? 333  LEU   E N   1 
ATOM   13887 C  CA  . LEU   E 2 333 ? 35.842  -13.227 -54.639 1.00 92.13  ? 333  LEU   E CA  1 
ATOM   13888 C  C   . LEU   E 2 333 ? 37.313  -13.035 -55.008 1.00 96.26  ? 333  LEU   E C   1 
ATOM   13889 O  O   . LEU   E 2 333 ? 37.799  -11.901 -55.052 1.00 98.77  ? 333  LEU   E O   1 
ATOM   13890 C  CB  . LEU   E 2 333 ? 34.945  -12.604 -55.716 1.00 92.15  ? 333  LEU   E CB  1 
ATOM   13891 C  CG  . LEU   E 2 333 ? 33.435  -12.839 -55.687 1.00 94.39  ? 333  LEU   E CG  1 
ATOM   13892 C  CD1 . LEU   E 2 333 ? 32.763  -12.159 -56.877 1.00 90.61  ? 333  LEU   E CD1 1 
ATOM   13893 C  CD2 . LEU   E 2 333 ? 33.123  -14.329 -55.671 1.00 95.70  ? 333  LEU   E CD2 1 
ATOM   13894 N  N   . VAL   E 2 334 ? 38.018  -14.126 -55.279 1.00 95.97  ? 334  VAL   E N   1 
ATOM   13895 C  CA  . VAL   E 2 334 ? 39.405  -14.038 -55.723 1.00 97.72  ? 334  VAL   E CA  1 
ATOM   13896 C  C   . VAL   E 2 334 ? 39.490  -14.504 -57.173 1.00 98.30  ? 334  VAL   E C   1 
ATOM   13897 O  O   . VAL   E 2 334 ? 38.664  -15.287 -57.654 1.00 98.26  ? 334  VAL   E O   1 
ATOM   13898 C  CB  . VAL   E 2 334 ? 40.354  -14.844 -54.809 1.00 100.56 ? 334  VAL   E CB  1 
ATOM   13899 C  CG1 . VAL   E 2 334 ? 40.306  -14.287 -53.409 1.00 96.63  ? 334  VAL   E CG1 1 
ATOM   13900 C  CG2 . VAL   E 2 334 ? 39.965  -16.304 -54.788 1.00 92.90  ? 334  VAL   E CG2 1 
ATOM   13901 N  N   . LYS   E 2 335 ? 40.470  -13.978 -57.888 1.00 101.30 ? 335  LYS   E N   1 
ATOM   13902 C  CA  . LYS   E 2 335 ? 40.713  -14.371 -59.268 1.00 103.70 ? 335  LYS   E CA  1 
ATOM   13903 C  C   . LYS   E 2 335 ? 42.049  -15.090 -59.311 1.00 105.45 ? 335  LYS   E C   1 
ATOM   13904 O  O   . LYS   E 2 335 ? 43.078  -14.519 -58.941 1.00 106.43 ? 335  LYS   E O   1 
ATOM   13905 C  CB  . LYS   E 2 335 ? 40.716  -13.167 -60.215 1.00 100.03 ? 335  LYS   E CB  1 
ATOM   13906 N  N   . LEU   E 2 336 ? 42.028  -16.343 -59.733 1.00 110.20 ? 336  LEU   E N   1 
ATOM   13907 C  CA  . LEU   E 2 336 ? 43.265  -17.070 -59.962 1.00 114.08 ? 336  LEU   E CA  1 
ATOM   13908 C  C   . LEU   E 2 336 ? 43.901  -16.580 -61.258 1.00 115.89 ? 336  LEU   E C   1 
ATOM   13909 O  O   . LEU   E 2 336 ? 43.204  -16.308 -62.240 1.00 114.58 ? 336  LEU   E O   1 
ATOM   13910 C  CB  . LEU   E 2 336 ? 42.993  -18.576 -59.993 1.00 110.48 ? 336  LEU   E CB  1 
ATOM   13911 C  CG  . LEU   E 2 336 ? 42.453  -19.002 -58.622 1.00 104.50 ? 336  LEU   E CG  1 
ATOM   13912 C  CD1 . LEU   E 2 336 ? 42.475  -20.492 -58.397 1.00 100.37 ? 336  LEU   E CD1 1 
ATOM   13913 C  CD2 . LEU   E 2 336 ? 43.303  -18.323 -57.594 1.00 105.17 ? 336  LEU   E CD2 1 
ATOM   13914 N  N   . ASN   E 2 337 ? 45.221  -16.410 -61.233 1.00 119.22 ? 337  ASN   E N   1 
ATOM   13915 C  CA  . ASN   E 2 337 ? 46.008  -15.959 -62.374 1.00 124.46 ? 337  ASN   E CA  1 
ATOM   13916 C  C   . ASN   E 2 337 ? 46.999  -17.033 -62.796 1.00 132.41 ? 337  ASN   E C   1 
ATOM   13917 O  O   . ASN   E 2 337 ? 47.310  -17.958 -62.042 1.00 135.10 ? 337  ASN   E O   1 
ATOM   13918 C  CB  . ASN   E 2 337 ? 46.775  -14.672 -62.056 1.00 124.72 ? 337  ASN   E CB  1 
ATOM   13919 C  CG  . ASN   E 2 337 ? 45.890  -13.468 -62.083 1.00 117.38 ? 337  ASN   E CG  1 
ATOM   13920 O  OD1 . ASN   E 2 337 ? 44.945  -13.410 -62.877 1.00 110.99 ? 337  ASN   E OD1 1 
ATOM   13921 N  ND2 . ASN   E 2 337 ? 46.166  -12.499 -61.206 1.00 109.66 ? 337  ASN   E ND2 1 
ATOM   13922 N  N   . VAL   E 2 338 ? 47.518  -16.885 -64.018 1.00 135.34 ? 338  VAL   E N   1 
ATOM   13923 C  CA  . VAL   E 2 338 ? 48.535  -17.799 -64.520 1.00 136.42 ? 338  VAL   E CA  1 
ATOM   13924 C  C   . VAL   E 2 338 ? 49.940  -17.239 -64.358 1.00 139.08 ? 338  VAL   E C   1 
ATOM   13925 O  O   . VAL   E 2 338 ? 50.915  -17.948 -64.651 1.00 138.63 ? 338  VAL   E O   1 
ATOM   13926 C  CB  . VAL   E 2 338 ? 48.272  -18.164 -65.995 1.00 135.17 ? 338  VAL   E CB  1 
ATOM   13927 C  CG1 . VAL   E 2 338 ? 48.742  -17.039 -66.897 1.00 129.57 ? 338  VAL   E CG1 1 
ATOM   13928 C  CG2 . VAL   E 2 338 ? 48.941  -19.490 -66.347 1.00 137.26 ? 338  VAL   E CG2 1 
ATOM   13929 N  N   . ASP   E 2 339 ? 50.079  -16.004 -63.898 1.00 145.35 ? 339  ASP   E N   1 
ATOM   13930 C  CA  . ASP   E 2 339 ? 51.378  -15.420 -63.625 1.00 147.76 ? 339  ASP   E CA  1 
ATOM   13931 C  C   . ASP   E 2 339 ? 51.358  -14.832 -62.221 1.00 149.60 ? 339  ASP   E C   1 
ATOM   13932 O  O   . ASP   E 2 339 ? 50.299  -14.451 -61.712 1.00 148.83 ? 339  ASP   E O   1 
ATOM   13933 C  CB  . ASP   E 2 339 ? 51.739  -14.355 -64.674 1.00 150.57 ? 339  ASP   E CB  1 
ATOM   13934 N  N   . SER   E 2 340 ? 52.531  -14.777 -61.587 1.00 149.71 ? 340  SER   E N   1 
ATOM   13935 C  CA  . SER   E 2 340 ? 52.596  -14.330 -60.202 1.00 152.64 ? 340  SER   E CA  1 
ATOM   13936 C  C   . SER   E 2 340 ? 52.631  -12.805 -60.106 1.00 151.42 ? 340  SER   E C   1 
ATOM   13937 O  O   . SER   E 2 340 ? 52.909  -12.091 -61.072 1.00 147.64 ? 340  SER   E O   1 
ATOM   13938 C  CB  . SER   E 2 340 ? 53.822  -14.915 -59.487 1.00 155.85 ? 340  SER   E CB  1 
ATOM   13939 O  OG  . SER   E 2 340 ? 55.022  -14.255 -59.846 1.00 159.05 ? 340  SER   E OG  1 
ATOM   13940 N  N   . ASN   E 2 341 ? 52.335  -12.316 -58.906 1.00 159.20 ? 341  ASN   E N   1 
ATOM   13941 C  CA  . ASN   E 2 341 ? 52.517  -10.918 -58.563 1.00 159.26 ? 341  ASN   E CA  1 
ATOM   13942 C  C   . ASN   E 2 341 ? 53.910  -10.748 -57.967 1.00 171.18 ? 341  ASN   E C   1 
ATOM   13943 O  O   . ASN   E 2 341 ? 54.737  -11.667 -57.986 1.00 170.28 ? 341  ASN   E O   1 
ATOM   13944 C  CB  . ASN   E 2 341 ? 51.424  -10.454 -57.600 1.00 145.48 ? 341  ASN   E CB  1 
ATOM   13945 N  N   . GLU   E 2 342 ? 54.188  -9.560  -57.426 1.00 189.35 ? 342  GLU   E N   1 
ATOM   13946 C  CA  . GLU   E 2 342 ? 55.477  -9.334  -56.779 1.00 193.40 ? 342  GLU   E CA  1 
ATOM   13947 C  C   . GLU   E 2 342 ? 55.657  -10.304 -55.614 1.00 194.66 ? 342  GLU   E C   1 
ATOM   13948 O  O   . GLU   E 2 342 ? 56.702  -10.958 -55.490 1.00 198.98 ? 342  GLU   E O   1 
ATOM   13949 C  CB  . GLU   E 2 342 ? 55.589  -7.885  -56.300 1.00 193.97 ? 342  GLU   E CB  1 
ATOM   13950 N  N   . GLN   E 2 343 ? 54.640  -10.428 -54.765 1.00 179.36 ? 343  GLN   E N   1 
ATOM   13951 C  CA  . GLN   E 2 343 ? 54.701  -11.374 -53.668 1.00 176.70 ? 343  GLN   E CA  1 
ATOM   13952 C  C   . GLN   E 2 343 ? 54.605  -12.814 -54.135 1.00 176.86 ? 343  GLN   E C   1 
ATOM   13953 O  O   . GLN   E 2 343 ? 54.500  -13.703 -53.286 1.00 171.58 ? 343  GLN   E O   1 
ATOM   13954 C  CB  . GLN   E 2 343 ? 53.597  -11.049 -52.652 1.00 166.61 ? 343  GLN   E CB  1 
ATOM   13955 N  N   . GLY   E 2 344 ? 54.635  -13.043 -55.450 1.00 190.92 ? 344  GLY   E N   1 
ATOM   13956 C  CA  . GLY   E 2 344 ? 54.564  -14.373 -56.026 1.00 189.03 ? 344  GLY   E CA  1 
ATOM   13957 C  C   . GLY   E 2 344 ? 53.185  -14.993 -56.039 1.00 185.74 ? 344  GLY   E C   1 
ATOM   13958 O  O   . GLY   E 2 344 ? 53.031  -16.124 -56.525 1.00 184.34 ? 344  GLY   E O   1 
ATOM   13959 N  N   . SER   E 2 345 ? 52.178  -14.295 -55.521 1.00 159.74 ? 345  SER   E N   1 
ATOM   13960 C  CA  . SER   E 2 345 ? 50.841  -14.857 -55.478 1.00 142.49 ? 345  SER   E CA  1 
ATOM   13961 C  C   . SER   E 2 345 ? 50.249  -14.970 -56.873 1.00 138.42 ? 345  SER   E C   1 
ATOM   13962 O  O   . SER   E 2 345 ? 50.632  -14.256 -57.805 1.00 141.75 ? 345  SER   E O   1 
ATOM   13963 C  CB  . SER   E 2 345 ? 49.917  -14.005 -54.612 1.00 136.93 ? 345  SER   E CB  1 
ATOM   13964 O  OG  . SER   E 2 345 ? 48.568  -14.411 -54.808 1.00 126.03 ? 345  SER   E OG  1 
ATOM   13965 N  N   . TYR   E 2 346 ? 49.313  -15.902 -57.011 1.00 127.39 ? 346  TYR   E N   1 
ATOM   13966 C  CA  . TYR   E 2 346 ? 48.447  -15.972 -58.175 1.00 125.34 ? 346  TYR   E CA  1 
ATOM   13967 C  C   . TYR   E 2 346 ? 47.023  -15.565 -57.835 1.00 120.38 ? 346  TYR   E C   1 
ATOM   13968 O  O   . TYR   E 2 346 ? 46.220  -15.326 -58.750 1.00 119.28 ? 346  TYR   E O   1 
ATOM   13969 C  CB  . TYR   E 2 346 ? 48.464  -17.392 -58.775 1.00 133.69 ? 346  TYR   E CB  1 
ATOM   13970 C  CG  . TYR   E 2 346 ? 49.855  -17.897 -59.161 1.00 141.61 ? 346  TYR   E CG  1 
ATOM   13971 C  CD1 . TYR   E 2 346 ? 50.957  -17.042 -59.144 1.00 149.06 ? 346  TYR   E CD1 1 
ATOM   13972 C  CD2 . TYR   E 2 346 ? 50.067  -19.222 -59.544 1.00 135.40 ? 346  TYR   E CD2 1 
ATOM   13973 C  CE1 . TYR   E 2 346 ? 52.224  -17.485 -59.489 1.00 148.64 ? 346  TYR   E CE1 1 
ATOM   13974 C  CE2 . TYR   E 2 346 ? 51.344  -19.670 -59.893 1.00 143.83 ? 346  TYR   E CE2 1 
ATOM   13975 C  CZ  . TYR   E 2 346 ? 52.414  -18.789 -59.861 1.00 146.03 ? 346  TYR   E CZ  1 
ATOM   13976 O  OH  . TYR   E 2 346 ? 53.685  -19.195 -60.197 1.00 149.66 ? 346  TYR   E OH  1 
ATOM   13977 N  N   . VAL   E 2 347 ? 46.700  -15.465 -56.549 1.00 117.35 ? 347  VAL   E N   1 
ATOM   13978 C  CA  . VAL   E 2 347 ? 45.393  -14.999 -56.116 1.00 114.14 ? 347  VAL   E CA  1 
ATOM   13979 C  C   . VAL   E 2 347 ? 45.410  -13.483 -56.052 1.00 111.38 ? 347  VAL   E C   1 
ATOM   13980 O  O   . VAL   E 2 347 ? 46.389  -12.874 -55.606 1.00 112.93 ? 347  VAL   E O   1 
ATOM   13981 C  CB  . VAL   E 2 347 ? 45.030  -15.607 -54.756 1.00 103.88 ? 347  VAL   E CB  1 
ATOM   13982 C  CG1 . VAL   E 2 347 ? 43.528  -15.512 -54.523 1.00 97.80  ? 347  VAL   E CG1 1 
ATOM   13983 C  CG2 . VAL   E 2 347 ? 45.523  -17.028 -54.691 1.00 103.03 ? 347  VAL   E CG2 1 
ATOM   13984 N  N   . VAL   E 2 348 ? 44.330  -12.863 -56.510 1.00 103.77 ? 348  VAL   E N   1 
ATOM   13985 C  CA  . VAL   E 2 348 ? 44.190  -11.421 -56.403 1.00 102.99 ? 348  VAL   E CA  1 
ATOM   13986 C  C   . VAL   E 2 348 ? 42.729  -11.128 -56.110 1.00 103.59 ? 348  VAL   E C   1 
ATOM   13987 O  O   . VAL   E 2 348 ? 41.849  -11.483 -56.903 1.00 104.33 ? 348  VAL   E O   1 
ATOM   13988 C  CB  . VAL   E 2 348 ? 44.657  -10.692 -57.670 1.00 98.95  ? 348  VAL   E CB  1 
ATOM   13989 C  CG1 . VAL   E 2 348 ? 43.594  -10.742 -58.747 1.00 102.17 ? 348  VAL   E CG1 1 
ATOM   13990 C  CG2 . VAL   E 2 348 ? 45.011  -9.283  -57.324 1.00 106.23 ? 348  VAL   E CG2 1 
ATOM   13991 N  N   . ALA   E 2 349 ? 42.460  -10.530 -54.956 1.00 100.99 ? 349  ALA   E N   1 
ATOM   13992 C  CA  . ALA   E 2 349 ? 41.078  -10.326 -54.557 1.00 100.00 ? 349  ALA   E CA  1 
ATOM   13993 C  C   . ALA   E 2 349 ? 40.423  -9.332  -55.503 1.00 108.19 ? 349  ALA   E C   1 
ATOM   13994 O  O   . ALA   E 2 349 ? 40.974  -8.263  -55.779 1.00 109.40 ? 349  ALA   E O   1 
ATOM   13995 C  CB  . ALA   E 2 349 ? 40.994  -9.831  -53.117 1.00 95.62  ? 349  ALA   E CB  1 
ATOM   13996 N  N   . MET   E 2 350 ? 39.250  -9.694  -56.014 1.00 108.15 ? 350  MET   E N   1 
ATOM   13997 C  CA  . MET   E 2 350 ? 38.495  -8.821  -56.897 1.00 104.17 ? 350  MET   E CA  1 
ATOM   13998 C  C   . MET   E 2 350 ? 37.196  -8.335  -56.280 1.00 102.21 ? 350  MET   E C   1 
ATOM   13999 O  O   . MET   E 2 350 ? 36.453  -7.605  -56.937 1.00 107.39 ? 350  MET   E O   1 
ATOM   14000 C  CB  . MET   E 2 350 ? 38.199  -9.537  -58.211 1.00 107.82 ? 350  MET   E CB  1 
ATOM   14001 C  CG  . MET   E 2 350 ? 37.389  -10.804 -58.037 1.00 106.54 ? 350  MET   E CG  1 
ATOM   14002 S  SD  . MET   E 2 350 ? 37.040  -11.543 -59.653 1.00 114.84 ? 350  MET   E SD  1 
ATOM   14003 C  CE  . MET   E 2 350 ? 35.504  -10.712 -60.089 1.00 106.77 ? 350  MET   E CE  1 
ATOM   14004 N  N   . GLU   E 2 351 ? 36.893  -8.735  -55.053 1.00 97.80  ? 351  GLU   E N   1 
ATOM   14005 C  CA  . GLU   E 2 351 ? 35.733  -8.232  -54.337 1.00 94.67  ? 351  GLU   E CA  1 
ATOM   14006 C  C   . GLU   E 2 351 ? 35.918  -8.626  -52.883 1.00 91.65  ? 351  GLU   E C   1 
ATOM   14007 O  O   . GLU   E 2 351 ? 36.800  -9.420  -52.556 1.00 94.36  ? 351  GLU   E O   1 
ATOM   14008 C  CB  . GLU   E 2 351 ? 34.436  -8.790  -54.921 1.00 96.24  ? 351  GLU   E CB  1 
ATOM   14009 C  CG  . GLU   E 2 351 ? 33.205  -7.966  -54.589 1.00 99.20  ? 351  GLU   E CG  1 
ATOM   14010 C  CD  . GLU   E 2 351 ? 32.111  -8.084  -55.657 1.00 108.76 ? 351  GLU   E CD  1 
ATOM   14011 O  OE1 . GLU   E 2 351 ? 31.040  -7.448  -55.489 1.00 111.76 ? 351  GLU   E OE1 1 
ATOM   14012 O  OE2 . GLU   E 2 351 ? 32.320  -8.817  -56.664 1.00 110.55 ? 351  GLU   E OE2 1 
ATOM   14013 N  N   . THR   E 2 352 ? 35.105  -8.042  -52.007 1.00 86.45  ? 352  THR   E N   1 
ATOM   14014 C  CA  . THR   E 2 352 ? 35.135  -8.393  -50.593 1.00 83.64  ? 352  THR   E CA  1 
ATOM   14015 C  C   . THR   E 2 352 ? 33.754  -8.119  -50.025 1.00 84.28  ? 352  THR   E C   1 
ATOM   14016 O  O   . THR   E 2 352 ? 33.104  -7.162  -50.434 1.00 94.59  ? 352  THR   E O   1 
ATOM   14017 C  CB  . THR   E 2 352 ? 36.205  -7.605  -49.820 1.00 77.42  ? 352  THR   E CB  1 
ATOM   14018 O  OG1 . THR   E 2 352 ? 36.043  -6.214  -50.084 1.00 97.05  ? 352  THR   E OG1 1 
ATOM   14019 C  CG2 . THR   E 2 352 ? 37.625  -7.995  -50.244 1.00 79.90  ? 352  THR   E CG2 1 
ATOM   14020 N  N   . PHE   E 2 353 ? 33.300  -8.951  -49.095 1.00 81.62  ? 353  PHE   E N   1 
ATOM   14021 C  CA  . PHE   E 2 353 ? 31.947  -8.863  -48.551 1.00 82.46  ? 353  PHE   E CA  1 
ATOM   14022 C  C   . PHE   E 2 353 ? 32.073  -8.743  -47.039 1.00 81.23  ? 353  PHE   E C   1 
ATOM   14023 O  O   . PHE   E 2 353 ? 32.752  -9.559  -46.409 1.00 85.23  ? 353  PHE   E O   1 
ATOM   14024 C  CB  . PHE   E 2 353 ? 31.118  -10.093 -48.949 1.00 88.93  ? 353  PHE   E CB  1 
ATOM   14025 C  CG  . PHE   E 2 353 ? 31.025  -10.297 -50.440 1.00 88.91  ? 353  PHE   E CG  1 
ATOM   14026 C  CD1 . PHE   E 2 353 ? 31.989  -11.029 -51.116 1.00 86.04  ? 353  PHE   E CD1 1 
ATOM   14027 C  CD2 . PHE   E 2 353 ? 29.992  -9.723  -51.170 1.00 91.68  ? 353  PHE   E CD2 1 
ATOM   14028 C  CE1 . PHE   E 2 353 ? 31.919  -11.195 -52.495 1.00 88.78  ? 353  PHE   E CE1 1 
ATOM   14029 C  CE2 . PHE   E 2 353 ? 29.915  -9.889  -52.551 1.00 90.32  ? 353  PHE   E CE2 1 
ATOM   14030 C  CZ  . PHE   E 2 353 ? 30.883  -10.629 -53.211 1.00 90.17  ? 353  PHE   E CZ  1 
ATOM   14031 N  N   . THR   E 2 354 ? 31.486  -7.710  -46.444 1.00 74.56  ? 354  THR   E N   1 
ATOM   14032 C  CA  . THR   E 2 354 ? 31.898  -7.457  -45.075 1.00 78.94  ? 354  THR   E CA  1 
ATOM   14033 C  C   . THR   E 2 354 ? 31.294  -8.520  -44.173 1.00 78.66  ? 354  THR   E C   1 
ATOM   14034 O  O   . THR   E 2 354 ? 30.126  -8.888  -44.324 1.00 76.58  ? 354  THR   E O   1 
ATOM   14035 C  CB  . THR   E 2 354 ? 31.555  -6.032  -44.611 1.00 81.18  ? 354  THR   E CB  1 
ATOM   14036 O  OG1 . THR   E 2 354 ? 30.166  -5.920  -44.325 1.00 91.16  ? 354  THR   E OG1 1 
ATOM   14037 C  CG2 . THR   E 2 354 ? 31.931  -5.031  -45.661 1.00 78.98  ? 354  THR   E CG2 1 
ATOM   14038 N  N   . ASN   E 2 355 ? 32.128  -9.039  -43.268 1.00 72.69  ? 355  ASN   E N   1 
ATOM   14039 C  CA  . ASN   E 2 355 ? 31.718  -9.892  -42.165 1.00 74.28  ? 355  ASN   E CA  1 
ATOM   14040 C  C   . ASN   E 2 355 ? 32.215  -9.266  -40.865 1.00 76.80  ? 355  ASN   E C   1 
ATOM   14041 O  O   . ASN   E 2 355 ? 33.428  -9.089  -40.659 1.00 73.28  ? 355  ASN   E O   1 
ATOM   14042 C  CB  . ASN   E 2 355 ? 32.240  -11.322 -42.361 1.00 83.26  ? 355  ASN   E CB  1 
ATOM   14043 C  CG  . ASN   E 2 355 ? 32.161  -12.185 -41.098 1.00 78.02  ? 355  ASN   E CG  1 
ATOM   14044 O  OD1 . ASN   E 2 355 ? 31.172  -12.181 -40.342 1.00 75.80  ? 355  ASN   E OD1 1 
ATOM   14045 N  ND2 . ASN   E 2 355 ? 33.238  -12.934 -40.863 1.00 79.32  ? 355  ASN   E ND2 1 
ATOM   14046 N  N   . LEU   E 2 356 ? 31.260  -8.887  -40.016 1.00 73.88  ? 356  LEU   E N   1 
ATOM   14047 C  CA  . LEU   E 2 356 ? 31.550  -8.247  -38.746 1.00 72.79  ? 356  LEU   E CA  1 
ATOM   14048 C  C   . LEU   E 2 356 ? 32.074  -9.234  -37.717 1.00 82.77  ? 356  LEU   E C   1 
ATOM   14049 O  O   . LEU   E 2 356 ? 32.794  -8.819  -36.791 1.00 81.24  ? 356  LEU   E O   1 
ATOM   14050 C  CB  . LEU   E 2 356 ? 30.285  -7.587  -38.192 1.00 75.16  ? 356  LEU   E CB  1 
ATOM   14051 C  CG  . LEU   E 2 356 ? 29.637  -6.565  -39.110 1.00 77.46  ? 356  LEU   E CG  1 
ATOM   14052 C  CD1 . LEU   E 2 356 ? 28.352  -5.942  -38.525 1.00 69.83  ? 356  LEU   E CD1 1 
ATOM   14053 C  CD2 . LEU   E 2 356 ? 30.703  -5.520  -39.457 1.00 79.44  ? 356  LEU   E CD2 1 
ATOM   14054 N  N   . GLY   E 2 357 ? 31.702  -10.522 -37.848 1.00 79.83  ? 357  GLY   E N   1 
ATOM   14055 C  CA  . GLY   E 2 357 ? 31.980  -11.507 -36.834 1.00 73.91  ? 357  GLY   E CA  1 
ATOM   14056 C  C   . GLY   E 2 357 ? 33.339  -12.159 -37.006 1.00 77.42  ? 357  GLY   E C   1 
ATOM   14057 O  O   . GLY   E 2 357 ? 33.986  -12.058 -38.059 1.00 74.44  ? 357  GLY   E O   1 
ATOM   14058 N  N   . PRO   E 2 358 ? 33.811  -12.823 -35.931 1.00 77.97  ? 358  PRO   E N   1 
ATOM   14059 C  CA  . PRO   E 2 358 ? 33.184  -12.825 -34.601 1.00 76.59  ? 358  PRO   E CA  1 
ATOM   14060 C  C   . PRO   E 2 358 ? 33.301  -11.441 -34.000 1.00 78.22  ? 358  PRO   E C   1 
ATOM   14061 O  O   . PRO   E 2 358 ? 34.383  -10.847 -34.095 1.00 73.44  ? 358  PRO   E O   1 
ATOM   14062 C  CB  . PRO   E 2 358 ? 34.008  -13.855 -33.814 1.00 71.29  ? 358  PRO   E CB  1 
ATOM   14063 C  CG  . PRO   E 2 358 ? 35.337  -13.843 -34.490 1.00 75.36  ? 358  PRO   E CG  1 
ATOM   14064 C  CD  . PRO   E 2 358 ? 35.011  -13.675 -35.960 1.00 75.56  ? 358  PRO   E CD  1 
ATOM   14065 N  N   . ILE   E 2 359 ? 32.230  -10.923 -33.401 1.00 75.07  ? 359  ILE   E N   1 
ATOM   14066 C  CA  . ILE   E 2 359 ? 32.274  -9.672  -32.656 1.00 74.98  ? 359  ILE   E CA  1 
ATOM   14067 C  C   . ILE   E 2 359 ? 32.511  -10.021 -31.189 1.00 74.01  ? 359  ILE   E C   1 
ATOM   14068 O  O   . ILE   E 2 359 ? 31.638  -10.593 -30.533 1.00 77.99  ? 359  ILE   E O   1 
ATOM   14069 C  CB  . ILE   E 2 359 ? 30.985  -8.863  -32.853 1.00 75.35  ? 359  ILE   E CB  1 
ATOM   14070 C  CG1 . ILE   E 2 359 ? 31.057  -8.075  -34.164 1.00 66.80  ? 359  ILE   E CG1 1 
ATOM   14071 C  CG2 . ILE   E 2 359 ? 30.708  -7.952  -31.641 1.00 75.32  ? 359  ILE   E CG2 1 
ATOM   14072 C  CD1 . ILE   E 2 359 ? 29.693  -7.773  -34.798 1.00 67.23  ? 359  ILE   E CD1 1 
ATOM   14073 N  N   . VAL   E 2 360 ? 33.696  -9.686  -30.678 1.00 70.14  ? 360  VAL   E N   1 
ATOM   14074 C  CA  . VAL   E 2 360 ? 34.102  -10.098 -29.335 1.00 75.07  ? 360  VAL   E CA  1 
ATOM   14075 C  C   . VAL   E 2 360 ? 33.955  -8.995  -28.292 1.00 79.61  ? 360  VAL   E C   1 
ATOM   14076 O  O   . VAL   E 2 360 ? 34.004  -9.285  -27.081 1.00 79.88  ? 360  VAL   E O   1 
ATOM   14077 C  CB  . VAL   E 2 360 ? 35.560  -10.582 -29.331 1.00 75.42  ? 360  VAL   E CB  1 
ATOM   14078 C  CG1 . VAL   E 2 360 ? 35.717  -11.791 -30.253 1.00 73.06  ? 360  VAL   E CG1 1 
ATOM   14079 C  CG2 . VAL   E 2 360 ? 36.496  -9.396  -29.681 1.00 69.68  ? 360  VAL   E CG2 1 
ATOM   14080 N  N   . ASP   E 2 361 ? 33.826  -7.749  -28.720 1.00 78.86  ? 361  ASP   E N   1 
ATOM   14081 C  CA  . ASP   E 2 361 ? 33.634  -6.637  -27.815 1.00 76.15  ? 361  ASP   E CA  1 
ATOM   14082 C  C   . ASP   E 2 361 ? 33.149  -5.469  -28.652 1.00 77.79  ? 361  ASP   E C   1 
ATOM   14083 O  O   . ASP   E 2 361 ? 33.371  -5.422  -29.870 1.00 75.74  ? 361  ASP   E O   1 
ATOM   14084 C  CB  . ASP   E 2 361 ? 34.917  -6.301  -27.061 1.00 71.77  ? 361  ASP   E CB  1 
ATOM   14085 C  CG  . ASP   E 2 361 ? 34.650  -5.520  -25.771 1.00 76.54  ? 361  ASP   E CG  1 
ATOM   14086 O  OD1 . ASP   E 2 361 ? 33.456  -5.298  -25.391 1.00 70.33  ? 361  ASP   E OD1 1 
ATOM   14087 O  OD2 . ASP   E 2 361 ? 35.658  -5.127  -25.134 1.00 77.93  ? 361  ASP   E OD2 1 
ATOM   14088 N  N   . MET   E 2 362 ? 32.479  -4.532  -27.990 1.00 76.15  ? 362  MET   E N   1 
ATOM   14089 C  CA  . MET   E 2 362 ? 31.983  -3.375  -28.713 1.00 75.63  ? 362  MET   E CA  1 
ATOM   14090 C  C   . MET   E 2 362 ? 31.560  -2.306  -27.717 1.00 78.85  ? 362  MET   E C   1 
ATOM   14091 O  O   . MET   E 2 362 ? 31.355  -2.574  -26.531 1.00 83.83  ? 362  MET   E O   1 
ATOM   14092 C  CB  . MET   E 2 362 ? 30.829  -3.762  -29.635 1.00 72.20  ? 362  MET   E CB  1 
ATOM   14093 C  CG  . MET   E 2 362 ? 29.615  -4.268  -28.916 1.00 74.03  ? 362  MET   E CG  1 
ATOM   14094 S  SD  . MET   E 2 362 ? 28.313  -4.419  -30.147 1.00 88.02  ? 362  MET   E SD  1 
ATOM   14095 C  CE  . MET   E 2 362 ? 26.986  -5.198  -29.209 1.00 74.66  ? 362  MET   E CE  1 
ATOM   14096 N  N   . CYS   E 2 363 ? 31.460  -1.077  -28.217 1.00 83.95  ? 363  CYS   E N   1 
ATOM   14097 C  CA  . CYS   E 2 363 ? 30.946  0.050   -27.446 1.00 80.19  ? 363  CYS   E CA  1 
ATOM   14098 C  C   . CYS   E 2 363 ? 30.289  1.035   -28.391 1.00 77.30  ? 363  CYS   E C   1 
ATOM   14099 O  O   . CYS   E 2 363 ? 30.625  1.110   -29.574 1.00 78.56  ? 363  CYS   E O   1 
ATOM   14100 C  CB  . CYS   E 2 363 ? 32.046  0.759   -26.671 1.00 79.87  ? 363  CYS   E CB  1 
ATOM   14101 S  SG  . CYS   E 2 363 ? 33.430  1.181   -27.754 1.00 83.80  ? 363  CYS   E SG  1 
ATOM   14102 N  N   . VAL   E 2 364 ? 29.367  1.801   -27.852 1.00 83.31  ? 364  VAL   E N   1 
ATOM   14103 C  CA  . VAL   E 2 364 ? 28.640  2.797   -28.629 1.00 82.41  ? 364  VAL   E CA  1 
ATOM   14104 C  C   . VAL   E 2 364 ? 29.202  4.174   -28.343 1.00 86.42  ? 364  VAL   E C   1 
ATOM   14105 O  O   . VAL   E 2 364 ? 29.503  4.508   -27.191 1.00 89.87  ? 364  VAL   E O   1 
ATOM   14106 C  CB  . VAL   E 2 364 ? 27.147  2.759   -28.316 1.00 81.13  ? 364  VAL   E CB  1 
ATOM   14107 C  CG1 . VAL   E 2 364 ? 26.435  3.751   -29.214 1.00 89.33  ? 364  VAL   E CG1 1 
ATOM   14108 C  CG2 . VAL   E 2 364 ? 26.653  1.358   -28.522 1.00 85.36  ? 364  VAL   E CG2 1 
ATOM   14109 N  N   . VAL   E 2 365 ? 29.313  4.988   -29.388 1.00 90.87  ? 365  VAL   E N   1 
ATOM   14110 C  CA  . VAL   E 2 365 ? 30.080  6.223   -29.338 1.00 86.51  ? 365  VAL   E CA  1 
ATOM   14111 C  C   . VAL   E 2 365 ? 29.577  7.156   -30.423 1.00 103.42 ? 365  VAL   E C   1 
ATOM   14112 O  O   . VAL   E 2 365 ? 29.394  6.749   -31.573 1.00 103.27 ? 365  VAL   E O   1 
ATOM   14113 C  CB  . VAL   E 2 365 ? 31.579  5.950   -29.513 1.00 86.36  ? 365  VAL   E CB  1 
ATOM   14114 C  CG1 . VAL   E 2 365 ? 32.324  7.229   -29.732 1.00 98.06  ? 365  VAL   E CG1 1 
ATOM   14115 C  CG2 . VAL   E 2 365 ? 32.133  5.238   -28.300 1.00 87.20  ? 365  VAL   E CG2 1 
ATOM   14116 N  N   . ASP   E 2 366 ? 29.369  8.428   -30.060 1.00 115.78 ? 366  ASP   E N   1 
ATOM   14117 C  CA  . ASP   E 2 366 ? 28.929  9.442   -31.019 1.00 116.88 ? 366  ASP   E CA  1 
ATOM   14118 C  C   . ASP   E 2 366 ? 30.157  10.181  -31.545 1.00 114.34 ? 366  ASP   E C   1 
ATOM   14119 O  O   . ASP   E 2 366 ? 30.499  11.275  -31.109 1.00 116.32 ? 366  ASP   E O   1 
ATOM   14120 C  CB  . ASP   E 2 366 ? 27.932  10.391  -30.382 1.00 118.31 ? 366  ASP   E CB  1 
ATOM   14121 C  CG  . ASP   E 2 366 ? 27.213  11.228  -31.407 1.00 122.53 ? 366  ASP   E CG  1 
ATOM   14122 O  OD1 . ASP   E 2 366 ? 27.592  11.160  -32.606 1.00 123.47 ? 366  ASP   E OD1 1 
ATOM   14123 O  OD2 . ASP   E 2 366 ? 26.264  11.943  -31.013 1.00 125.40 ? 366  ASP   E OD2 1 
ATOM   14124 N  N   . LEU   E 2 367 ? 30.826  9.562   -32.516 1.00 108.84 ? 367  LEU   E N   1 
ATOM   14125 C  CA  . LEU   E 2 367 ? 32.118  10.079  -32.934 1.00 106.25 ? 367  LEU   E CA  1 
ATOM   14126 C  C   . LEU   E 2 367 ? 31.983  11.457  -33.564 1.00 111.48 ? 367  LEU   E C   1 
ATOM   14127 O  O   . LEU   E 2 367 ? 32.949  12.236  -33.586 1.00 108.99 ? 367  LEU   E O   1 
ATOM   14128 C  CB  . LEU   E 2 367 ? 32.784  9.090   -33.886 1.00 100.74 ? 367  LEU   E CB  1 
ATOM   14129 C  CG  . LEU   E 2 367 ? 33.538  7.960   -33.189 1.00 96.80  ? 367  LEU   E CG  1 
ATOM   14130 C  CD1 . LEU   E 2 367 ? 34.415  7.227   -34.177 1.00 94.21  ? 367  LEU   E CD1 1 
ATOM   14131 C  CD2 . LEU   E 2 367 ? 34.384  8.485   -32.051 1.00 94.45  ? 367  LEU   E CD2 1 
ATOM   14132 N  N   . GLU   E 2 368 ? 30.788  11.793  -34.038 1.00 114.57 ? 368  GLU   E N   1 
ATOM   14133 C  CA  . GLU   E 2 368 ? 30.552  13.080  -34.672 1.00 119.31 ? 368  GLU   E CA  1 
ATOM   14134 C  C   . GLU   E 2 368 ? 29.694  14.016  -33.832 1.00 124.42 ? 368  GLU   E C   1 
ATOM   14135 O  O   . GLU   E 2 368 ? 29.258  15.055  -34.334 1.00 126.15 ? 368  GLU   E O   1 
ATOM   14136 C  CB  . GLU   E 2 368 ? 29.908  12.865  -36.032 1.00 112.11 ? 368  GLU   E CB  1 
ATOM   14137 C  CG  . GLU   E 2 368 ? 30.787  12.101  -36.943 1.00 102.35 ? 368  GLU   E CG  1 
ATOM   14138 C  CD  . GLU   E 2 368 ? 30.095  11.851  -38.231 1.00 108.87 ? 368  GLU   E CD  1 
ATOM   14139 O  OE1 . GLU   E 2 368 ? 29.047  12.513  -38.449 1.00 111.24 ? 368  GLU   E OE1 1 
ATOM   14140 O  OE2 . GLU   E 2 368 ? 30.574  10.997  -39.007 1.00 109.63 ? 368  GLU   E OE2 1 
ATOM   14141 N  N   . ARG   E 2 369 ? 29.437  13.670  -32.575 1.00 131.05 ? 369  ARG   E N   1 
ATOM   14142 C  CA  . ARG   E 2 369 ? 28.631  14.496  -31.682 1.00 132.93 ? 369  ARG   E CA  1 
ATOM   14143 C  C   . ARG   E 2 369 ? 27.374  15.013  -32.390 1.00 135.14 ? 369  ARG   E C   1 
ATOM   14144 O  O   . ARG   E 2 369 ? 27.002  16.183  -32.270 1.00 137.24 ? 369  ARG   E O   1 
ATOM   14145 C  CB  . ARG   E 2 369 ? 29.469  15.646  -31.109 1.00 129.12 ? 369  ARG   E CB  1 
ATOM   14146 N  N   . GLN   E 2 370 ? 26.718  14.133  -33.156 1.00 130.74 ? 370  GLN   E N   1 
ATOM   14147 C  CA  . GLN   E 2 370 ? 25.450  14.443  -33.814 1.00 130.00 ? 370  GLN   E CA  1 
ATOM   14148 C  C   . GLN   E 2 370 ? 24.248  13.801  -33.119 1.00 130.22 ? 370  GLN   E C   1 
ATOM   14149 O  O   . GLN   E 2 370 ? 23.139  13.850  -33.663 1.00 126.78 ? 370  GLN   E O   1 
ATOM   14150 C  CB  . GLN   E 2 370 ? 25.477  14.006  -35.287 1.00 127.20 ? 370  GLN   E CB  1 
ATOM   14151 C  CG  . GLN   E 2 370 ? 26.768  14.333  -36.040 1.00 129.88 ? 370  GLN   E CG  1 
ATOM   14152 C  CD  . GLN   E 2 370 ? 26.882  15.795  -36.474 1.00 132.27 ? 370  GLN   E CD  1 
ATOM   14153 O  OE1 . GLN   E 2 370 ? 27.077  16.694  -35.650 1.00 134.57 ? 370  GLN   E OE1 1 
ATOM   14154 N  NE2 . GLN   E 2 370 ? 26.774  16.032  -37.781 1.00 127.14 ? 370  GLN   E NE2 1 
ATOM   14155 N  N   . GLY   E 2 371 ? 24.442  13.196  -31.939 1.00 130.40 ? 371  GLY   E N   1 
ATOM   14156 C  CA  . GLY   E 2 371 ? 23.374  12.542  -31.200 1.00 127.20 ? 371  GLY   E CA  1 
ATOM   14157 C  C   . GLY   E 2 371 ? 22.809  11.295  -31.857 1.00 126.69 ? 371  GLY   E C   1 
ATOM   14158 O  O   . GLY   E 2 371 ? 21.666  10.913  -31.572 1.00 121.17 ? 371  GLY   E O   1 
ATOM   14159 N  N   . GLN   E 2 372 ? 23.599  10.663  -32.734 1.00 126.49 ? 372  GLN   E N   1 
ATOM   14160 C  CA  . GLN   E 2 372 ? 23.208  9.504   -33.519 1.00 121.86 ? 372  GLN   E CA  1 
ATOM   14161 C  C   . GLN   E 2 372 ? 23.662  8.204   -32.862 1.00 119.85 ? 372  GLN   E C   1 
ATOM   14162 O  O   . GLN   E 2 372 ? 22.838  7.349   -32.504 1.00 117.63 ? 372  GLN   E O   1 
ATOM   14163 C  CB  . GLN   E 2 372 ? 23.800  9.622   -34.934 1.00 120.12 ? 372  GLN   E CB  1 
ATOM   14164 C  CG  . GLN   E 2 372 ? 23.406  8.521   -35.916 1.00 122.11 ? 372  GLN   E CG  1 
ATOM   14165 C  CD  . GLN   E 2 372 ? 21.930  8.555   -36.299 1.00 123.45 ? 372  GLN   E CD  1 
ATOM   14166 O  OE1 . GLN   E 2 372 ? 21.064  8.935   -35.489 1.00 122.23 ? 372  GLN   E OE1 1 
ATOM   14167 N  NE2 . GLN   E 2 372 ? 21.635  8.156   -37.539 1.00 120.14 ? 372  GLN   E NE2 1 
ATOM   14168 N  N   . GLY   E 2 373 ? 24.970  8.045   -32.669 1.00 116.80 ? 373  GLY   E N   1 
ATOM   14169 C  CA  . GLY   E 2 373 ? 25.475  6.803   -32.120 1.00 110.17 ? 373  GLY   E CA  1 
ATOM   14170 C  C   . GLY   E 2 373 ? 26.008  5.863   -33.182 1.00 106.68 ? 373  GLY   E C   1 
ATOM   14171 O  O   . GLY   E 2 373 ? 25.319  5.531   -34.158 1.00 106.08 ? 373  GLY   E O   1 
ATOM   14172 N  N   . GLN   E 2 374 ? 27.257  5.446   -33.008 1.00 99.29  ? 374  GLN   E N   1 
ATOM   14173 C  CA  . GLN   E 2 374 ? 27.884  4.475   -33.890 1.00 95.95  ? 374  GLN   E CA  1 
ATOM   14174 C  C   . GLN   E 2 374 ? 28.415  3.305   -33.064 1.00 94.05  ? 374  GLN   E C   1 
ATOM   14175 O  O   . GLN   E 2 374 ? 28.926  3.496   -31.954 1.00 92.04  ? 374  GLN   E O   1 
ATOM   14176 C  CB  . GLN   E 2 374 ? 29.013  5.118   -34.703 1.00 95.93  ? 374  GLN   E CB  1 
ATOM   14177 C  CG  . GLN   E 2 374 ? 28.547  6.181   -35.690 1.00 102.34 ? 374  GLN   E CG  1 
ATOM   14178 C  CD  . GLN   E 2 374 ? 29.297  7.496   -35.502 1.00 109.77 ? 374  GLN   E CD  1 
ATOM   14179 O  OE1 . GLN   E 2 374 ? 30.536  7.543   -35.614 1.00 102.79 ? 374  GLN   E OE1 1 
ATOM   14180 N  NE2 . GLN   E 2 374 ? 28.550  8.572   -35.191 1.00 110.69 ? 374  GLN   E NE2 1 
ATOM   14181 N  N   . LEU   E 2 375 ? 28.285  2.089   -33.593 1.00 89.18  ? 375  LEU   E N   1 
ATOM   14182 C  CA  . LEU   E 2 375 ? 28.814  0.918   -32.911 1.00 84.87  ? 375  LEU   E CA  1 
ATOM   14183 C  C   . LEU   E 2 375 ? 30.238  0.665   -33.387 1.00 81.46  ? 375  LEU   E C   1 
ATOM   14184 O  O   . LEU   E 2 375 ? 30.487  0.601   -34.595 1.00 81.01  ? 375  LEU   E O   1 
ATOM   14185 C  CB  . LEU   E 2 375 ? 27.924  -0.300  -33.160 1.00 84.28  ? 375  LEU   E CB  1 
ATOM   14186 C  CG  . LEU   E 2 375 ? 27.843  -1.379  -32.077 1.00 78.53  ? 375  LEU   E CG  1 
ATOM   14187 C  CD1 . LEU   E 2 375 ? 27.995  -0.818  -30.656 1.00 78.66  ? 375  LEU   E CD1 1 
ATOM   14188 C  CD2 . LEU   E 2 375 ? 26.517  -2.069  -32.204 1.00 77.34  ? 375  LEU   E CD2 1 
ATOM   14189 N  N   . VAL   E 2 376 ? 31.175  0.565   -32.447 1.00 74.74  ? 376  VAL   E N   1 
ATOM   14190 C  CA  . VAL   E 2 376 ? 32.560  0.252   -32.776 1.00 78.72  ? 376  VAL   E CA  1 
ATOM   14191 C  C   . VAL   E 2 376 ? 32.905  -1.092  -32.148 1.00 82.87  ? 376  VAL   E C   1 
ATOM   14192 O  O   . VAL   E 2 376 ? 32.820  -1.252  -30.924 1.00 80.31  ? 376  VAL   E O   1 
ATOM   14193 C  CB  . VAL   E 2 376 ? 33.528  1.359   -32.328 1.00 77.96  ? 376  VAL   E CB  1 
ATOM   14194 C  CG1 . VAL   E 2 376 ? 34.931  0.782   -32.149 1.00 76.74  ? 376  VAL   E CG1 1 
ATOM   14195 C  CG2 . VAL   E 2 376 ? 33.578  2.433   -33.381 1.00 80.34  ? 376  VAL   E CG2 1 
ATOM   14196 N  N   . THR   E 2 377 ? 33.325  -2.050  -32.992 1.00 80.19  ? 377  THR   E N   1 
ATOM   14197 C  CA  . THR   E 2 377 ? 33.410  -3.467  -32.656 1.00 73.64  ? 377  THR   E CA  1 
ATOM   14198 C  C   . THR   E 2 377 ? 34.830  -3.985  -32.813 1.00 77.46  ? 377  THR   E C   1 
ATOM   14199 O  O   . THR   E 2 377 ? 35.504  -3.656  -33.794 1.00 77.12  ? 377  THR   E O   1 
ATOM   14200 C  CB  . THR   E 2 377 ? 32.505  -4.297  -33.575 1.00 72.38  ? 377  THR   E CB  1 
ATOM   14201 O  OG1 . THR   E 2 377 ? 33.058  -4.305  -34.895 1.00 67.14  ? 377  THR   E OG1 1 
ATOM   14202 C  CG2 . THR   E 2 377 ? 31.083  -3.738  -33.607 1.00 74.13  ? 377  THR   E CG2 1 
ATOM   14203 N  N   . CYS   E 2 378 ? 35.275  -4.821  -31.860 1.00 78.97  ? 378  CYS   E N   1 
ATOM   14204 C  CA  . CYS   E 2 378 ? 36.424  -5.706  -32.091 1.00 78.95  ? 378  CYS   E CA  1 
ATOM   14205 C  C   . CYS   E 2 378 ? 35.970  -6.914  -32.892 1.00 73.23  ? 378  CYS   E C   1 
ATOM   14206 O  O   . CYS   E 2 378 ? 35.103  -7.667  -32.436 1.00 71.38  ? 378  CYS   E O   1 
ATOM   14207 C  CB  . CYS   E 2 378 ? 37.033  -6.189  -30.781 1.00 78.82  ? 378  CYS   E CB  1 
ATOM   14208 S  SG  . CYS   E 2 378 ? 37.552  -4.869  -29.701 1.00 82.00  ? 378  CYS   E SG  1 
ATOM   14209 N  N   . SER   E 2 379 ? 36.583  -7.135  -34.049 1.00 72.71  ? 379  SER   E N   1 
ATOM   14210 C  CA  . SER   E 2 379 ? 35.988  -8.026  -35.028 1.00 73.11  ? 379  SER   E CA  1 
ATOM   14211 C  C   . SER   E 2 379 ? 37.024  -8.941  -35.661 1.00 77.36  ? 379  SER   E C   1 
ATOM   14212 O  O   . SER   E 2 379 ? 38.165  -8.537  -35.917 1.00 76.73  ? 379  SER   E O   1 
ATOM   14213 C  CB  . SER   E 2 379 ? 35.262  -7.224  -36.092 1.00 70.90  ? 379  SER   E CB  1 
ATOM   14214 O  OG  . SER   E 2 379 ? 33.941  -6.960  -35.665 1.00 76.34  ? 379  SER   E OG  1 
ATOM   14215 N  N   . GLY   E 2 380 ? 36.598  -10.193 -35.904 1.00 74.16  ? 380  GLY   E N   1 
ATOM   14216 C  CA  . GLY   E 2 380 ? 37.496  -11.173 -36.453 1.00 78.29  ? 380  GLY   E CA  1 
ATOM   14217 C  C   . GLY   E 2 380 ? 38.517  -11.644 -35.436 1.00 79.36  ? 380  GLY   E C   1 
ATOM   14218 O  O   . GLY   E 2 380 ? 38.414  -11.413 -34.229 1.00 79.59  ? 380  GLY   E O   1 
ATOM   14219 N  N   . ALA   E 2 381 ? 39.534  -12.319 -35.957 1.00 81.32  ? 381  ALA   E N   1 
ATOM   14220 C  CA  . ALA   E 2 381 ? 40.589  -12.853 -35.108 1.00 79.58  ? 381  ALA   E CA  1 
ATOM   14221 C  C   . ALA   E 2 381 ? 41.817  -12.996 -35.994 1.00 81.17  ? 381  ALA   E C   1 
ATOM   14222 O  O   . ALA   E 2 381 ? 41.706  -13.048 -37.220 1.00 83.77  ? 381  ALA   E O   1 
ATOM   14223 C  CB  . ALA   E 2 381 ? 40.152  -14.151 -34.407 1.00 75.45  ? 381  ALA   E CB  1 
ATOM   14224 N  N   . PHE   E 2 382 ? 42.983  -13.030 -35.370 1.00 76.91  ? 382  PHE   E N   1 
ATOM   14225 C  CA  . PHE   E 2 382 ? 44.225  -13.245 -36.089 1.00 82.69  ? 382  PHE   E CA  1 
ATOM   14226 C  C   . PHE   E 2 382 ? 44.485  -12.220 -37.188 1.00 87.04  ? 382  PHE   E C   1 
ATOM   14227 O  O   . PHE   E 2 382 ? 44.368  -11.021 -36.943 1.00 88.44  ? 382  PHE   E O   1 
ATOM   14228 C  CB  . PHE   E 2 382 ? 44.214  -14.698 -36.585 1.00 82.86  ? 382  PHE   E CB  1 
ATOM   14229 C  CG  . PHE   E 2 382 ? 43.696  -15.671 -35.566 1.00 82.76  ? 382  PHE   E CG  1 
ATOM   14230 C  CD1 . PHE   E 2 382 ? 44.265  -15.771 -34.279 1.00 82.98  ? 382  PHE   E CD1 1 
ATOM   14231 C  CD2 . PHE   E 2 382 ? 42.649  -16.517 -35.868 1.00 81.64  ? 382  PHE   E CD2 1 
ATOM   14232 C  CE1 . PHE   E 2 382 ? 43.773  -16.701 -33.358 1.00 84.03  ? 382  PHE   E CE1 1 
ATOM   14233 C  CE2 . PHE   E 2 382 ? 42.158  -17.448 -34.952 1.00 84.86  ? 382  PHE   E CE2 1 
ATOM   14234 C  CZ  . PHE   E 2 382 ? 42.719  -17.538 -33.697 1.00 80.73  ? 382  PHE   E CZ  1 
ATOM   14235 N  N   . LYS   E 2 383 ? 44.828  -12.636 -38.410 1.00 85.66  ? 383  LYS   E N   1 
ATOM   14236 C  CA  . LYS   E 2 383 ? 45.149  -11.660 -39.450 1.00 89.68  ? 383  LYS   E CA  1 
ATOM   14237 C  C   . LYS   E 2 383 ? 43.868  -10.979 -39.888 1.00 91.97  ? 383  LYS   E C   1 
ATOM   14238 O  O   . LYS   E 2 383 ? 43.935  -9.934  -40.535 1.00 95.17  ? 383  LYS   E O   1 
ATOM   14239 C  CB  . LYS   E 2 383 ? 45.857  -12.342 -40.637 1.00 96.14  ? 383  LYS   E CB  1 
ATOM   14240 C  CG  . LYS   E 2 383 ? 44.991  -13.228 -41.544 1.00 94.18  ? 383  LYS   E CG  1 
ATOM   14241 C  CD  . LYS   E 2 383 ? 45.857  -14.103 -42.462 1.00 93.40  ? 383  LYS   E CD  1 
ATOM   14242 C  CE  . LYS   E 2 383 ? 45.123  -14.506 -43.739 1.00 95.40  ? 383  LYS   E CE  1 
ATOM   14243 N  NZ  . LYS   E 2 383 ? 45.205  -13.457 -44.800 1.00 97.24  ? 383  LYS   E NZ  1 
ATOM   14244 N  N   . GLU   E 2 384 ? 42.708  -11.531 -39.543 1.00 97.10  ? 384  GLU   E N   1 
ATOM   14245 C  CA  . GLU   E 2 384 ? 41.451  -10.887 -39.880 1.00 97.56  ? 384  GLU   E CA  1 
ATOM   14246 C  C   . GLU   E 2 384 ? 41.003  -9.886  -38.821 1.00 93.45  ? 384  GLU   E C   1 
ATOM   14247 O  O   . GLU   E 2 384 ? 39.932  -9.287  -38.967 1.00 94.24  ? 384  GLU   E O   1 
ATOM   14248 C  CB  . GLU   E 2 384 ? 40.366  -11.940 -40.108 1.00 98.42  ? 384  GLU   E CB  1 
ATOM   14249 C  CG  . GLU   E 2 384 ? 40.709  -13.042 -41.126 1.00 99.27  ? 384  GLU   E CG  1 
ATOM   14250 C  CD  . GLU   E 2 384 ? 41.380  -12.553 -42.417 1.00 103.96 ? 384  GLU   E CD  1 
ATOM   14251 O  OE1 . GLU   E 2 384 ? 41.078  -11.431 -42.901 1.00 108.32 ? 384  GLU   E OE1 1 
ATOM   14252 O  OE2 . GLU   E 2 384 ? 42.215  -13.315 -42.964 1.00 105.97 ? 384  GLU   E OE2 1 
ATOM   14253 N  N   . GLY   E 2 385 ? 41.795  -9.679  -37.772 1.00 82.33  ? 385  GLY   E N   1 
ATOM   14254 C  CA  . GLY   E 2 385 ? 41.429  -8.752  -36.711 1.00 81.61  ? 385  GLY   E CA  1 
ATOM   14255 C  C   . GLY   E 2 385 ? 41.181  -7.321  -37.164 1.00 80.11  ? 385  GLY   E C   1 
ATOM   14256 O  O   . GLY   E 2 385 ? 41.971  -6.740  -37.915 1.00 80.71  ? 385  GLY   E O   1 
ATOM   14257 N  N   . SER   E 2 386 ? 40.100  -6.711  -36.702 1.00 74.71  ? 386  SER   E N   1 
ATOM   14258 C  CA  . SER   E 2 386 ? 39.723  -5.458  -37.327 1.00 72.61  ? 386  SER   E CA  1 
ATOM   14259 C  C   . SER   E 2 386 ? 38.821  -4.654  -36.411 1.00 77.67  ? 386  SER   E C   1 
ATOM   14260 O  O   . SER   E 2 386 ? 37.952  -5.213  -35.737 1.00 79.17  ? 386  SER   E O   1 
ATOM   14261 C  CB  . SER   E 2 386 ? 38.994  -5.726  -38.637 1.00 76.27  ? 386  SER   E CB  1 
ATOM   14262 O  OG  . SER   E 2 386 ? 37.646  -6.112  -38.372 1.00 75.36  ? 386  SER   E OG  1 
ATOM   14263 N  N   . LEU   E 2 387 ? 38.997  -3.335  -36.423 1.00 79.05  ? 387  LEU   E N   1 
ATOM   14264 C  CA  . LEU   E 2 387 ? 37.956  -2.466  -35.909 1.00 78.82  ? 387  LEU   E CA  1 
ATOM   14265 C  C   . LEU   E 2 387 ? 36.936  -2.214  -37.007 1.00 76.90  ? 387  LEU   E C   1 
ATOM   14266 O  O   . LEU   E 2 387 ? 37.286  -2.065  -38.182 1.00 74.26  ? 387  LEU   E O   1 
ATOM   14267 C  CB  . LEU   E 2 387 ? 38.525  -1.152  -35.374 1.00 72.47  ? 387  LEU   E CB  1 
ATOM   14268 C  CG  . LEU   E 2 387 ? 39.373  -1.462  -34.149 1.00 71.30  ? 387  LEU   E CG  1 
ATOM   14269 C  CD1 . LEU   E 2 387 ? 39.446  -0.286  -33.204 1.00 79.08  ? 387  LEU   E CD1 1 
ATOM   14270 C  CD2 . LEU   E 2 387 ? 38.820  -2.697  -33.437 1.00 77.46  ? 387  LEU   E CD2 1 
ATOM   14271 N  N   . ARG   E 2 388 ? 35.665  -2.215  -36.609 1.00 75.53  ? 388  ARG   E N   1 
ATOM   14272 C  CA  . ARG   E 2 388 ? 34.535  -1.939  -37.481 1.00 76.80  ? 388  ARG   E CA  1 
ATOM   14273 C  C   . ARG   E 2 388 ? 33.732  -0.800  -36.869 1.00 80.15  ? 388  ARG   E C   1 
ATOM   14274 O  O   . ARG   E 2 388 ? 33.500  -0.791  -35.656 1.00 80.99  ? 388  ARG   E O   1 
ATOM   14275 C  CB  . ARG   E 2 388 ? 33.666  -3.190  -37.655 1.00 74.10  ? 388  ARG   E CB  1 
ATOM   14276 C  CG  . ARG   E 2 388 ? 34.414  -4.382  -38.229 1.00 72.59  ? 388  ARG   E CG  1 
ATOM   14277 C  CD  . ARG   E 2 388 ? 34.492  -4.345  -39.733 1.00 70.21  ? 388  ARG   E CD  1 
ATOM   14278 N  NE  . ARG   E 2 388 ? 35.438  -5.340  -40.230 1.00 74.13  ? 388  ARG   E NE  1 
ATOM   14279 C  CZ  . ARG   E 2 388 ? 35.342  -5.979  -41.394 1.00 77.74  ? 388  ARG   E CZ  1 
ATOM   14280 N  NH1 . ARG   E 2 388 ? 34.333  -5.759  -42.224 1.00 76.55  ? 388  ARG   E NH1 1 
ATOM   14281 N  NH2 . ARG   E 2 388 ? 36.277  -6.872  -41.727 1.00 78.61  ? 388  ARG   E NH2 1 
ATOM   14282 N  N   . ILE   E 2 389 ? 33.335  0.175   -37.691 1.00 79.03  ? 389  ILE   E N   1 
ATOM   14283 C  CA  . ILE   E 2 389 ? 32.504  1.290   -37.232 1.00 80.85  ? 389  ILE   E CA  1 
ATOM   14284 C  C   . ILE   E 2 389 ? 31.205  1.290   -38.024 1.00 83.89  ? 389  ILE   E C   1 
ATOM   14285 O  O   . ILE   E 2 389 ? 31.229  1.291   -39.261 1.00 84.73  ? 389  ILE   E O   1 
ATOM   14286 C  CB  . ILE   E 2 389 ? 33.216  2.638   -37.365 1.00 80.76  ? 389  ILE   E CB  1 
ATOM   14287 C  CG1 . ILE   E 2 389 ? 34.509  2.637   -36.533 1.00 79.73  ? 389  ILE   E CG1 1 
ATOM   14288 C  CG2 . ILE   E 2 389 ? 32.249  3.765   -36.976 1.00 83.39  ? 389  ILE   E CG2 1 
ATOM   14289 C  CD1 . ILE   E 2 389 ? 35.739  2.135   -37.305 1.00 78.96  ? 389  ILE   E CD1 1 
ATOM   14290 N  N   . ILE   E 2 390 ? 30.078  1.283   -37.309 1.00 82.54  ? 390  ILE   E N   1 
ATOM   14291 C  CA  . ILE   E 2 390 ? 28.761  1.027   -37.889 1.00 87.37  ? 390  ILE   E CA  1 
ATOM   14292 C  C   . ILE   E 2 390 ? 27.861  2.210   -37.551 1.00 92.08  ? 390  ILE   E C   1 
ATOM   14293 O  O   . ILE   E 2 390 ? 27.638  2.506   -36.367 1.00 92.49  ? 390  ILE   E O   1 
ATOM   14294 C  CB  . ILE   E 2 390 ? 28.155  -0.298  -37.374 1.00 86.82  ? 390  ILE   E CB  1 
ATOM   14295 C  CG1 . ILE   E 2 390 ? 29.053  -1.498  -37.732 1.00 82.50  ? 390  ILE   E CG1 1 
ATOM   14296 C  CG2 . ILE   E 2 390 ? 26.723  -0.525  -37.897 1.00 78.56  ? 390  ILE   E CG2 1 
ATOM   14297 C  CD1 . ILE   E 2 390 ? 29.301  -2.454  -36.567 1.00 79.41  ? 390  ILE   E CD1 1 
ATOM   14298 N  N   . ARG   E 2 391 ? 27.330  2.868   -38.590 1.00 93.90  ? 391  ARG   E N   1 
ATOM   14299 C  CA  . ARG   E 2 391 ? 26.495  4.050   -38.449 1.00 96.35  ? 391  ARG   E CA  1 
ATOM   14300 C  C   . ARG   E 2 391 ? 25.229  3.873   -39.271 1.00 97.05  ? 391  ARG   E C   1 
ATOM   14301 O  O   . ARG   E 2 391 ? 25.223  3.154   -40.270 1.00 99.73  ? 391  ARG   E O   1 
ATOM   14302 C  CB  . ARG   E 2 391 ? 27.244  5.319   -38.907 1.00 91.99  ? 391  ARG   E CB  1 
ATOM   14303 N  N   . ASN   E 2 392 ? 24.133  4.472   -38.813 1.00 99.37  ? 392  ASN   E N   1 
ATOM   14304 C  CA  . ASN   E 2 392 ? 22.840  4.341   -39.537 1.00 101.98 ? 392  ASN   E CA  1 
ATOM   14305 C  C   . ASN   E 2 392 ? 22.658  5.558   -40.449 1.00 99.52  ? 392  ASN   E C   1 
ATOM   14306 O  O   . ASN   E 2 392 ? 22.907  5.403   -41.662 1.00 98.10  ? 392  ASN   E O   1 
ATOM   14307 C  CB  . ASN   E 2 392 ? 21.674  4.159   -38.574 1.00 102.56 ? 392  ASN   E CB  1 
ATOM   14308 C  CG  . ASN   E 2 392 ? 21.598  2.752   -38.034 1.00 99.23  ? 392  ASN   E CG  1 
ATOM   14309 O  OD1 . ASN   E 2 392 ? 22.435  1.911   -38.378 1.00 103.40 ? 392  ASN   E OD1 1 
ATOM   14310 N  ND2 . ASN   E 2 392 ? 20.611  2.478   -37.195 1.00 97.10  ? 392  ASN   E ND2 1 
ATOM   14311 N  N   . LEU   E 2 406 ? 22.641  0.846   -43.190 1.00 88.16  ? 710  LEU   E N   1 
ATOM   14312 C  CA  . LEU   E 2 406 ? 23.755  0.997   -42.219 1.00 96.58  ? 710  LEU   E CA  1 
ATOM   14313 C  C   . LEU   E 2 406 ? 25.087  1.090   -42.977 1.00 91.59  ? 710  LEU   E C   1 
ATOM   14314 O  O   . LEU   E 2 406 ? 25.156  0.604   -44.120 1.00 97.16  ? 710  LEU   E O   1 
ATOM   14315 C  CB  . LEU   E 2 406 ? 23.737  -0.151  -41.211 1.00 100.95 ? 710  LEU   E CB  1 
ATOM   14316 C  CG  . LEU   E 2 406 ? 24.483  -1.432  -41.595 1.00 93.66  ? 710  LEU   E CG  1 
ATOM   14317 C  CD1 . LEU   E 2 406 ? 24.653  -2.288  -40.356 1.00 98.10  ? 710  LEU   E CD1 1 
ATOM   14318 C  CD2 . LEU   E 2 406 ? 23.751  -2.216  -42.672 1.00 83.58  ? 710  LEU   E CD2 1 
ATOM   14319 N  N   . HIS   E 2 407 ? 26.090  1.723   -42.371 1.00 99.55  ? 711  HIS   E N   1 
ATOM   14320 C  CA  . HIS   E 2 407 ? 27.395  1.912   -43.055 1.00 101.14 ? 711  HIS   E CA  1 
ATOM   14321 C  C   . HIS   E 2 407 ? 28.494  1.290   -42.199 1.00 99.95  ? 711  HIS   E C   1 
ATOM   14322 O  O   . HIS   E 2 407 ? 28.427  1.425   -40.969 1.00 98.48  ? 711  HIS   E O   1 
ATOM   14323 C  CB  . HIS   E 2 407 ? 27.661  3.398   -43.300 1.00 106.24 ? 711  HIS   E CB  1 
ATOM   14324 C  CG  . HIS   E 2 407 ? 26.423  4.155   -43.638 1.00 111.32 ? 711  HIS   E CG  1 
ATOM   14325 N  ND1 . HIS   E 2 407 ? 25.662  3.869   -44.750 1.00 108.24 ? 711  HIS   E ND1 1 
ATOM   14326 C  CD2 . HIS   E 2 407 ? 25.806  5.164   -43.014 1.00 113.13 ? 711  HIS   E CD2 1 
ATOM   14327 C  CE1 . HIS   E 2 407 ? 24.623  4.689   -44.789 1.00 109.09 ? 711  HIS   E CE1 1 
ATOM   14328 N  NE2 . HIS   E 2 407 ? 24.691  5.484   -43.744 1.00 113.96 ? 711  HIS   E NE2 1 
ATOM   14329 N  N   . ILE   E 2 408 ? 29.473  0.645   -42.833 1.00 89.41  ? 712  ILE   E N   1 
ATOM   14330 C  CA  . ILE   E 2 408 ? 30.529  -0.070  -42.060 1.00 90.70  ? 712  ILE   E CA  1 
ATOM   14331 C  C   . ILE   E 2 408 ? 31.909  0.392   -42.543 1.00 85.73  ? 712  ILE   E C   1 
ATOM   14332 O  O   . ILE   E 2 408 ? 32.173  0.290   -43.755 1.00 85.69  ? 712  ILE   E O   1 
ATOM   14333 C  CB  . ILE   E 2 408 ? 30.368  -1.597  -42.171 1.00 90.93  ? 712  ILE   E CB  1 
ATOM   14334 C  CG1 . ILE   E 2 408 ? 29.147  -2.089  -41.400 1.00 80.29  ? 712  ILE   E CG1 1 
ATOM   14335 C  CG2 . ILE   E 2 408 ? 31.639  -2.317  -41.721 1.00 82.03  ? 712  ILE   E CG2 1 
ATOM   14336 C  CD1 . ILE   E 2 408 ? 28.028  -2.607  -42.283 1.00 84.56  ? 712  ILE   E CD1 1 
ATOM   14337 N  N   . ARG   E 2 409 ? 32.734  0.901   -41.630 1.00 81.90  ? 713  ARG   E N   1 
ATOM   14338 C  CA  . ARG   E 2 409 ? 34.124  1.272   -41.989 1.00 81.51  ? 713  ARG   E CA  1 
ATOM   14339 C  C   . ARG   E 2 409 ? 35.038  0.245   -41.323 1.00 81.66  ? 713  ARG   E C   1 
ATOM   14340 O  O   . ARG   E 2 409 ? 34.858  -0.003  -40.120 1.00 80.12  ? 713  ARG   E O   1 
ATOM   14341 C  CB  . ARG   E 2 409 ? 34.455  2.692   -41.526 1.00 88.76  ? 713  ARG   E CB  1 
ATOM   14342 C  CG  . ARG   E 2 409 ? 35.920  3.085   -41.640 1.00 91.27  ? 713  ARG   E CG  1 
ATOM   14343 C  CD  . ARG   E 2 409 ? 36.276  4.179   -40.649 1.00 92.65  ? 713  ARG   E CD  1 
ATOM   14344 N  NE  . ARG   E 2 409 ? 37.554  4.820   -40.971 1.00 104.39 ? 713  ARG   E NE  1 
ATOM   14345 C  CZ  . ARG   E 2 409 ? 37.785  6.122   -40.879 1.00 104.76 ? 713  ARG   E CZ  1 
ATOM   14346 N  NH1 . ARG   E 2 409 ? 36.778  6.962   -40.727 1.00 100.18 ? 713  ARG   E NH1 1 
ATOM   14347 N  NH2 . ARG   E 2 409 ? 39.022  6.581   -40.938 1.00 106.66 ? 713  ARG   E NH2 1 
ATOM   14348 N  N   . THR   E 2 410 ? 35.961  -0.340  -42.079 1.00 77.61  ? 714  THR   E N   1 
ATOM   14349 C  CA  . THR   E 2 410 ? 36.793  -1.410  -41.507 1.00 79.00  ? 714  THR   E CA  1 
ATOM   14350 C  C   . THR   E 2 410 ? 38.191  -0.904  -41.264 1.00 79.86  ? 714  THR   E C   1 
ATOM   14351 O  O   . THR   E 2 410 ? 38.763  -0.299  -42.187 1.00 78.60  ? 714  THR   E O   1 
ATOM   14352 C  CB  . THR   E 2 410 ? 36.777  -2.614  -42.445 1.00 80.43  ? 714  THR   E CB  1 
ATOM   14353 O  OG1 . THR   E 2 410 ? 35.419  -3.033  -42.528 1.00 82.75  ? 714  THR   E OG1 1 
ATOM   14354 C  CG2 . THR   E 2 410 ? 37.636  -3.758  -41.939 1.00 74.69  ? 714  THR   E CG2 1 
ATOM   14355 N  N   . VAL   E 2 411 ? 38.711  -1.101  -40.053 1.00 78.84  ? 715  VAL   E N   1 
ATOM   14356 C  CA  . VAL   E 2 411 ? 40.097  -0.751  -39.758 1.00 76.95  ? 715  VAL   E CA  1 
ATOM   14357 C  C   . VAL   E 2 411 ? 40.884  -2.026  -39.482 1.00 81.58  ? 715  VAL   E C   1 
ATOM   14358 O  O   . VAL   E 2 411 ? 40.980  -2.452  -38.315 1.00 77.05  ? 715  VAL   E O   1 
ATOM   14359 C  CB  . VAL   E 2 411 ? 40.205  0.187   -38.548 1.00 78.78  ? 715  VAL   E CB  1 
ATOM   14360 C  CG1 . VAL   E 2 411 ? 41.632  0.675   -38.397 1.00 79.27  ? 715  VAL   E CG1 1 
ATOM   14361 C  CG2 . VAL   E 2 411 ? 39.252  1.369   -38.654 1.00 79.87  ? 715  VAL   E CG2 1 
ATOM   14362 N  N   . PRO   E 2 412 ? 41.458  -2.661  -40.525 1.00 77.52  ? 716  PRO   E N   1 
ATOM   14363 C  CA  . PRO   E 2 412 ? 42.305  -3.857  -40.338 1.00 74.45  ? 716  PRO   E CA  1 
ATOM   14364 C  C   . PRO   E 2 412 ? 43.441  -3.719  -39.334 1.00 79.72  ? 716  PRO   E C   1 
ATOM   14365 O  O   . PRO   E 2 412 ? 44.321  -2.890  -39.530 1.00 82.88  ? 716  PRO   E O   1 
ATOM   14366 C  CB  . PRO   E 2 412 ? 42.896  -4.085  -41.737 1.00 80.51  ? 716  PRO   E CB  1 
ATOM   14367 C  CG  . PRO   E 2 412 ? 42.593  -2.821  -42.513 1.00 88.05  ? 716  PRO   E CG  1 
ATOM   14368 C  CD  . PRO   E 2 412 ? 41.320  -2.283  -41.938 1.00 77.97  ? 716  PRO   E CD  1 
ATOM   14369 N  N   . LEU   E 2 413 ? 43.471  -4.565  -38.301 1.00 81.27  ? 717  LEU   E N   1 
ATOM   14370 C  CA  . LEU   E 2 413 ? 44.594  -4.597  -37.371 1.00 75.30  ? 717  LEU   E CA  1 
ATOM   14371 C  C   . LEU   E 2 413 ? 45.628  -5.670  -37.680 1.00 82.57  ? 717  LEU   E C   1 
ATOM   14372 O  O   . LEU   E 2 413 ? 46.765  -5.569  -37.189 1.00 83.93  ? 717  LEU   E O   1 
ATOM   14373 C  CB  . LEU   E 2 413 ? 44.079  -4.808  -35.956 1.00 73.68  ? 717  LEU   E CB  1 
ATOM   14374 C  CG  . LEU   E 2 413 ? 43.130  -3.669  -35.649 1.00 81.51  ? 717  LEU   E CG  1 
ATOM   14375 C  CD1 . LEU   E 2 413 ? 42.314  -3.931  -34.387 1.00 75.46  ? 717  LEU   E CD1 1 
ATOM   14376 C  CD2 . LEU   E 2 413 ? 43.990  -2.412  -35.520 1.00 78.87  ? 717  LEU   E CD2 1 
ATOM   14377 N  N   . TYR   E 2 414 ? 45.261  -6.693  -38.463 1.00 81.21  ? 718  TYR   E N   1 
ATOM   14378 C  CA  . TYR   E 2 414 ? 46.106  -7.860  -38.716 1.00 83.65  ? 718  TYR   E CA  1 
ATOM   14379 C  C   . TYR   E 2 414 ? 46.515  -8.595  -37.429 1.00 84.44  ? 718  TYR   E C   1 
ATOM   14380 O  O   . TYR   E 2 414 ? 47.517  -9.324  -37.418 1.00 90.67  ? 718  TYR   E O   1 
ATOM   14381 C  CB  . TYR   E 2 414 ? 47.342  -7.467  -39.532 1.00 84.51  ? 718  TYR   E CB  1 
ATOM   14382 C  CG  . TYR   E 2 414 ? 46.960  -6.750  -40.799 1.00 83.68  ? 718  TYR   E CG  1 
ATOM   14383 C  CD1 . TYR   E 2 414 ? 46.348  -7.427  -41.833 1.00 88.46  ? 718  TYR   E CD1 1 
ATOM   14384 C  CD2 . TYR   E 2 414 ? 47.178  -5.397  -40.948 1.00 85.77  ? 718  TYR   E CD2 1 
ATOM   14385 C  CE1 . TYR   E 2 414 ? 45.979  -6.792  -42.981 1.00 84.44  ? 718  TYR   E CE1 1 
ATOM   14386 C  CE2 . TYR   E 2 414 ? 46.812  -4.747  -42.103 1.00 89.30  ? 718  TYR   E CE2 1 
ATOM   14387 C  CZ  . TYR   E 2 414 ? 46.208  -5.453  -43.118 1.00 89.91  ? 718  TYR   E CZ  1 
ATOM   14388 O  OH  . TYR   E 2 414 ? 45.822  -4.835  -44.290 1.00 98.89  ? 718  TYR   E OH  1 
ATOM   14389 N  N   . GLU   E 2 415 ? 45.763  -8.425  -36.336 1.00 77.88  ? 719  GLU   E N   1 
ATOM   14390 C  CA  . GLU   E 2 415 ? 45.932  -9.188  -35.102 1.00 77.46  ? 719  GLU   E CA  1 
ATOM   14391 C  C   . GLU   E 2 415 ? 44.614  -9.089  -34.341 1.00 78.80  ? 719  GLU   E C   1 
ATOM   14392 O  O   . GLU   E 2 415 ? 43.648  -8.499  -34.830 1.00 76.68  ? 719  GLU   E O   1 
ATOM   14393 C  CB  . GLU   E 2 415 ? 47.144  -8.708  -34.306 1.00 74.99  ? 719  GLU   E CB  1 
ATOM   14394 C  CG  . GLU   E 2 415 ? 46.927  -7.377  -33.681 1.00 83.49  ? 719  GLU   E CG  1 
ATOM   14395 C  CD  . GLU   E 2 415 ? 48.175  -6.847  -33.033 1.00 86.35  ? 719  GLU   E CD  1 
ATOM   14396 O  OE1 . GLU   E 2 415 ? 49.269  -7.053  -33.608 1.00 85.43  ? 719  GLU   E OE1 1 
ATOM   14397 O  OE2 . GLU   E 2 415 ? 48.064  -6.221  -31.951 1.00 87.70  ? 719  GLU   E OE2 1 
ATOM   14398 N  N   . SER   E 2 416 ? 44.554  -9.688  -33.145 1.00 77.08  ? 720  SER   E N   1 
ATOM   14399 C  CA  . SER   E 2 416 ? 43.215  -9.960  -32.616 1.00 77.14  ? 720  SER   E CA  1 
ATOM   14400 C  C   . SER   E 2 416 ? 42.731  -8.899  -31.608 1.00 83.97  ? 720  SER   E C   1 
ATOM   14401 O  O   . SER   E 2 416 ? 43.197  -8.883  -30.457 1.00 83.06  ? 720  SER   E O   1 
ATOM   14402 C  CB  . SER   E 2 416 ? 43.187  -11.358 -31.994 1.00 75.20  ? 720  SER   E CB  1 
ATOM   14403 O  OG  . SER   E 2 416 ? 43.781  -12.290 -32.881 1.00 78.01  ? 720  SER   E OG  1 
ATOM   14404 N  N   . PRO   E 2 417 ? 41.804  -8.005  -31.980 1.00 80.17  ? 721  PRO   E N   1 
ATOM   14405 C  CA  . PRO   E 2 417 ? 41.183  -7.137  -30.972 1.00 75.81  ? 721  PRO   E CA  1 
ATOM   14406 C  C   . PRO   E 2 417 ? 40.408  -7.968  -29.968 1.00 73.05  ? 721  PRO   E C   1 
ATOM   14407 O  O   . PRO   E 2 417 ? 39.673  -8.880  -30.341 1.00 79.66  ? 721  PRO   E O   1 
ATOM   14408 C  CB  . PRO   E 2 417 ? 40.238  -6.244  -31.799 1.00 75.32  ? 721  PRO   E CB  1 
ATOM   14409 C  CG  . PRO   E 2 417 ? 40.004  -6.995  -33.066 1.00 74.38  ? 721  PRO   E CG  1 
ATOM   14410 C  CD  . PRO   E 2 417 ? 41.295  -7.712  -33.335 1.00 76.61  ? 721  PRO   E CD  1 
ATOM   14411 N  N   . ARG   E 2 418 ? 40.564  -7.645  -28.690 1.00 76.26  ? 722  ARG   E N   1 
ATOM   14412 C  CA  . ARG   E 2 418 ? 39.840  -8.354  -27.642 1.00 76.67  ? 722  ARG   E CA  1 
ATOM   14413 C  C   . ARG   E 2 418 ? 38.888  -7.462  -26.862 1.00 71.47  ? 722  ARG   E C   1 
ATOM   14414 O  O   . ARG   E 2 418 ? 37.696  -7.769  -26.776 1.00 79.49  ? 722  ARG   E O   1 
ATOM   14415 C  CB  . ARG   E 2 418 ? 40.826  -9.038  -26.684 1.00 82.87  ? 722  ARG   E CB  1 
ATOM   14416 C  CG  . ARG   E 2 418 ? 41.750  -10.013 -27.387 1.00 78.38  ? 722  ARG   E CG  1 
ATOM   14417 C  CD  . ARG   E 2 418 ? 40.956  -11.146 -27.932 1.00 77.36  ? 722  ARG   E CD  1 
ATOM   14418 N  NE  . ARG   E 2 418 ? 40.294  -11.890 -26.867 1.00 83.79  ? 722  ARG   E NE  1 
ATOM   14419 C  CZ  . ARG   E 2 418 ? 39.288  -12.736 -27.065 1.00 85.57  ? 722  ARG   E CZ  1 
ATOM   14420 N  NH1 . ARG   E 2 418 ? 38.776  -12.926 -28.277 1.00 82.05  ? 722  ARG   E NH1 1 
ATOM   14421 N  NH2 . ARG   E 2 418 ? 38.782  -13.403 -26.024 1.00 78.13  ? 722  ARG   E NH2 1 
ATOM   14422 N  N   . LYS   E 2 419 ? 39.357  -6.359  -26.304 1.00 73.41  ? 723  LYS   E N   1 
ATOM   14423 C  CA  . LYS   E 2 419 ? 38.474  -5.434  -25.611 1.00 77.44  ? 723  LYS   E CA  1 
ATOM   14424 C  C   . LYS   E 2 419 ? 38.637  -4.023  -26.181 1.00 78.11  ? 723  LYS   E C   1 
ATOM   14425 O  O   . LYS   E 2 419 ? 39.587  -3.725  -26.916 1.00 75.36  ? 723  LYS   E O   1 
ATOM   14426 C  CB  . LYS   E 2 419 ? 38.722  -5.469  -24.105 1.00 74.47  ? 723  LYS   E CB  1 
ATOM   14427 C  CG  . LYS   E 2 419 ? 38.518  -6.849  -23.469 1.00 77.54  ? 723  LYS   E CG  1 
ATOM   14428 C  CD  . LYS   E 2 419 ? 37.044  -7.271  -23.480 1.00 80.43  ? 723  LYS   E CD  1 
ATOM   14429 C  CE  . LYS   E 2 419 ? 36.853  -8.745  -23.171 1.00 83.22  ? 723  LYS   E CE  1 
ATOM   14430 N  NZ  . LYS   E 2 419 ? 36.544  -8.922  -21.734 1.00 97.40  ? 723  LYS   E NZ  1 
ATOM   14431 N  N   . ILE   E 2 420 ? 37.688  -3.152  -25.838 1.00 78.67  ? 724  ILE   E N   1 
ATOM   14432 C  CA  . ILE   E 2 420 ? 37.667  -1.797  -26.396 1.00 83.47  ? 724  ILE   E CA  1 
ATOM   14433 C  C   . ILE   E 2 420 ? 36.867  -0.854  -25.507 1.00 81.33  ? 724  ILE   E C   1 
ATOM   14434 O  O   . ILE   E 2 420 ? 35.769  -1.180  -25.045 1.00 79.70  ? 724  ILE   E O   1 
ATOM   14435 C  CB  . ILE   E 2 420 ? 37.069  -1.782  -27.804 1.00 81.68  ? 724  ILE   E CB  1 
ATOM   14436 C  CG1 . ILE   E 2 420 ? 36.847  -0.358  -28.255 1.00 77.73  ? 724  ILE   E CG1 1 
ATOM   14437 C  CG2 . ILE   E 2 420 ? 35.731  -2.478  -27.808 1.00 83.22  ? 724  ILE   E CG2 1 
ATOM   14438 C  CD1 . ILE   E 2 420 ? 36.715  -0.296  -29.722 1.00 78.89  ? 724  ILE   E CD1 1 
ATOM   14439 N  N   . CYS   E 2 421 ? 37.410  0.343   -25.316 1.00 85.54  ? 725  CYS   E N   1 
ATOM   14440 C  CA  . CYS   E 2 421 ? 36.667  1.416   -24.669 1.00 91.61  ? 725  CYS   E CA  1 
ATOM   14441 C  C   . CYS   E 2 421 ? 37.097  2.750   -25.265 1.00 86.83  ? 725  CYS   E C   1 
ATOM   14442 O  O   . CYS   E 2 421 ? 38.199  2.897   -25.810 1.00 84.54  ? 725  CYS   E O   1 
ATOM   14443 C  CB  . CYS   E 2 421 ? 36.866  1.399   -23.151 1.00 86.24  ? 725  CYS   E CB  1 
ATOM   14444 S  SG  . CYS   E 2 421 ? 38.588  1.681   -22.709 1.00 97.29  ? 725  CYS   E SG  1 
ATOM   14445 N  N   . TYR   E 2 422 ? 36.200  3.723   -25.155 1.00 90.82  ? 726  TYR   E N   1 
ATOM   14446 C  CA  . TYR   E 2 422 ? 36.395  5.044   -25.738 1.00 90.99  ? 726  TYR   E CA  1 
ATOM   14447 C  C   . TYR   E 2 422 ? 36.845  6.024   -24.662 1.00 87.04  ? 726  TYR   E C   1 
ATOM   14448 O  O   . TYR   E 2 422 ? 36.427  5.922   -23.507 1.00 84.80  ? 726  TYR   E O   1 
ATOM   14449 C  CB  . TYR   E 2 422 ? 35.103  5.511   -26.384 1.00 87.71  ? 726  TYR   E CB  1 
ATOM   14450 C  CG  . TYR   E 2 422 ? 35.188  6.875   -26.969 1.00 89.51  ? 726  TYR   E CG  1 
ATOM   14451 C  CD1 . TYR   E 2 422 ? 36.240  7.230   -27.783 1.00 90.09  ? 726  TYR   E CD1 1 
ATOM   14452 C  CD2 . TYR   E 2 422 ? 34.196  7.817   -26.708 1.00 90.25  ? 726  TYR   E CD2 1 
ATOM   14453 C  CE1 . TYR   E 2 422 ? 36.313  8.514   -28.321 1.00 96.79  ? 726  TYR   E CE1 1 
ATOM   14454 C  CE2 . TYR   E 2 422 ? 34.255  9.078   -27.233 1.00 89.00  ? 726  TYR   E CE2 1 
ATOM   14455 C  CZ  . TYR   E 2 422 ? 35.315  9.433   -28.037 1.00 92.44  ? 726  TYR   E CZ  1 
ATOM   14456 O  OH  . TYR   E 2 422 ? 35.376  10.704  -28.565 1.00 88.91  ? 726  TYR   E OH  1 
ATOM   14457 N  N   . GLN   E 2 423 ? 37.731  6.952   -25.030 1.00 88.75  ? 727  GLN   E N   1 
ATOM   14458 C  CA  . GLN   E 2 423 ? 38.252  7.936   -24.074 1.00 94.85  ? 727  GLN   E CA  1 
ATOM   14459 C  C   . GLN   E 2 423 ? 38.046  9.319   -24.672 1.00 93.77  ? 727  GLN   E C   1 
ATOM   14460 O  O   . GLN   E 2 423 ? 38.958  9.881   -25.291 1.00 92.62  ? 727  GLN   E O   1 
ATOM   14461 C  CB  . GLN   E 2 423 ? 39.729  7.698   -23.741 1.00 93.78  ? 727  GLN   E CB  1 
ATOM   14462 C  CG  . GLN   E 2 423 ? 40.311  8.725   -22.774 1.00 88.17  ? 727  GLN   E CG  1 
ATOM   14463 C  CD  . GLN   E 2 423 ? 41.400  8.137   -21.877 1.00 93.01  ? 727  GLN   E CD  1 
ATOM   14464 O  OE1 . GLN   E 2 423 ? 42.597  8.449   -22.028 1.00 95.74  ? 727  GLN   E OE1 1 
ATOM   14465 N  NE2 . GLN   E 2 423 ? 40.990  7.291   -20.930 1.00 88.43  ? 727  GLN   E NE2 1 
ATOM   14466 N  N   . GLU   E 2 424 ? 36.844  9.864   -24.473 1.00 93.24  ? 728  GLU   E N   1 
ATOM   14467 C  CA  . GLU   E 2 424 ? 36.474  11.123  -25.114 1.00 95.26  ? 728  GLU   E CA  1 
ATOM   14468 C  C   . GLU   E 2 424 ? 37.452  12.240  -24.781 1.00 95.14  ? 728  GLU   E C   1 
ATOM   14469 O  O   . GLU   E 2 424 ? 37.811  13.040  -25.654 1.00 91.16  ? 728  GLU   E O   1 
ATOM   14470 C  CB  . GLU   E 2 424 ? 35.065  11.508  -24.690 1.00 95.93  ? 728  GLU   E CB  1 
ATOM   14471 C  CG  . GLU   E 2 424 ? 34.555  12.792  -25.244 1.00 96.81  ? 728  GLU   E CG  1 
ATOM   14472 C  CD  . GLU   E 2 424 ? 33.190  13.098  -24.677 1.00 109.20 ? 728  GLU   E CD  1 
ATOM   14473 O  OE1 . GLU   E 2 424 ? 32.288  12.226  -24.795 1.00 110.95 ? 728  GLU   E OE1 1 
ATOM   14474 O  OE2 . GLU   E 2 424 ? 33.033  14.182  -24.070 1.00 115.52 ? 728  GLU   E OE2 1 
ATOM   14475 N  N   . VAL   E 2 425 ? 37.898  12.306  -23.526 1.00 95.45  ? 729  VAL   E N   1 
ATOM   14476 C  CA  . VAL   E 2 425 ? 38.788  13.388  -23.124 1.00 92.62  ? 729  VAL   E CA  1 
ATOM   14477 C  C   . VAL   E 2 425 ? 40.054  13.385  -23.968 1.00 95.09  ? 729  VAL   E C   1 
ATOM   14478 O  O   . VAL   E 2 425 ? 40.612  14.446  -24.270 1.00 102.70 ? 729  VAL   E O   1 
ATOM   14479 C  CB  . VAL   E 2 425 ? 39.104  13.291  -21.621 1.00 95.53  ? 729  VAL   E CB  1 
ATOM   14480 C  CG1 . VAL   E 2 425 ? 40.567  13.690  -21.338 1.00 97.92  ? 729  VAL   E CG1 1 
ATOM   14481 C  CG2 . VAL   E 2 425 ? 38.115  14.162  -20.830 1.00 96.97  ? 729  VAL   E CG2 1 
ATOM   14482 N  N   . SER   E 2 426 ? 40.522  12.206  -24.371 1.00 91.33  ? 730  SER   E N   1 
ATOM   14483 C  CA  . SER   E 2 426 ? 41.759  12.085  -25.125 1.00 90.44  ? 730  SER   E CA  1 
ATOM   14484 C  C   . SER   E 2 426 ? 41.516  11.810  -26.597 1.00 96.30  ? 730  SER   E C   1 
ATOM   14485 O  O   . SER   E 2 426 ? 42.477  11.589  -27.341 1.00 99.59  ? 730  SER   E O   1 
ATOM   14486 C  CB  . SER   E 2 426 ? 42.641  10.981  -24.530 1.00 99.23  ? 730  SER   E CB  1 
ATOM   14487 O  OG  . SER   E 2 426 ? 42.939  11.212  -23.160 1.00 103.20 ? 730  SER   E OG  1 
ATOM   14488 N  N   . GLN   E 2 427 ? 40.255  11.798  -27.025 1.00 98.31  ? 731  GLN   E N   1 
ATOM   14489 C  CA  . GLN   E 2 427 ? 39.857  11.507  -28.408 1.00 99.88  ? 731  GLN   E CA  1 
ATOM   14490 C  C   . GLN   E 2 427 ? 40.608  10.299  -28.968 1.00 98.37  ? 731  GLN   E C   1 
ATOM   14491 O  O   . GLN   E 2 427 ? 41.363  10.377  -29.945 1.00 96.38  ? 731  GLN   E O   1 
ATOM   14492 C  CB  . GLN   E 2 427 ? 40.044  12.731  -29.296 1.00 100.64 ? 731  GLN   E CB  1 
ATOM   14493 C  CG  . GLN   E 2 427 ? 38.920  13.739  -29.207 1.00 101.36 ? 731  GLN   E CG  1 
ATOM   14494 C  CD  . GLN   E 2 427 ? 39.254  14.995  -29.974 1.00 110.46 ? 731  GLN   E CD  1 
ATOM   14495 O  OE1 . GLN   E 2 427 ? 38.689  15.254  -31.047 1.00 111.73 ? 731  GLN   E OE1 1 
ATOM   14496 N  NE2 . GLN   E 2 427 ? 40.185  15.787  -29.434 1.00 111.30 ? 731  GLN   E NE2 1 
ATOM   14497 N  N   . CYS   E 2 428 ? 40.355  9.156   -28.341 1.00 96.83  ? 732  CYS   E N   1 
ATOM   14498 C  CA  . CYS   E 2 428 ? 41.074  7.947   -28.699 1.00 96.01  ? 732  CYS   E CA  1 
ATOM   14499 C  C   . CYS   E 2 428 ? 40.349  6.751   -28.105 1.00 92.92  ? 732  CYS   E C   1 
ATOM   14500 O  O   . CYS   E 2 428 ? 39.509  6.882   -27.205 1.00 89.14  ? 732  CYS   E O   1 
ATOM   14501 C  CB  . CYS   E 2 428 ? 42.511  7.994   -28.191 1.00 97.68  ? 732  CYS   E CB  1 
ATOM   14502 S  SG  . CYS   E 2 428 ? 42.484  8.128   -26.413 1.00 103.25 ? 732  CYS   E SG  1 
ATOM   14503 N  N   . PHE   E 2 429 ? 40.703  5.580   -28.619 1.00 90.03  ? 733  PHE   E N   1 
ATOM   14504 C  CA  . PHE   E 2 429 ? 40.147  4.315   -28.177 1.00 86.20  ? 733  PHE   E CA  1 
ATOM   14505 C  C   . PHE   E 2 429 ? 41.226  3.482   -27.510 1.00 87.13  ? 733  PHE   E C   1 
ATOM   14506 O  O   . PHE   E 2 429 ? 42.384  3.472   -27.946 1.00 88.08  ? 733  PHE   E O   1 
ATOM   14507 C  CB  . PHE   E 2 429 ? 39.579  3.534   -29.354 1.00 85.43  ? 733  PHE   E CB  1 
ATOM   14508 C  CG  . PHE   E 2 429 ? 38.265  4.027   -29.833 1.00 80.38  ? 733  PHE   E CG  1 
ATOM   14509 C  CD1 . PHE   E 2 429 ? 37.110  3.643   -29.184 1.00 78.88  ? 733  PHE   E CD1 1 
ATOM   14510 C  CD2 . PHE   E 2 429 ? 38.180  4.855   -30.950 1.00 85.83  ? 733  PHE   E CD2 1 
ATOM   14511 C  CE1 . PHE   E 2 429 ? 35.877  4.078   -29.619 1.00 84.03  ? 733  PHE   E CE1 1 
ATOM   14512 C  CE2 . PHE   E 2 429 ? 36.946  5.298   -31.407 1.00 87.27  ? 733  PHE   E CE2 1 
ATOM   14513 C  CZ  . PHE   E 2 429 ? 35.791  4.910   -30.733 1.00 89.82  ? 733  PHE   E CZ  1 
ATOM   14514 N  N   . GLY   E 2 430 ? 40.833  2.764   -26.462 1.00 85.60  ? 734  GLY   E N   1 
ATOM   14515 C  CA  . GLY   E 2 430 ? 41.680  1.744   -25.869 1.00 86.28  ? 734  GLY   E CA  1 
ATOM   14516 C  C   . GLY   E 2 430 ? 41.263  0.367   -26.356 1.00 85.01  ? 734  GLY   E C   1 
ATOM   14517 O  O   . GLY   E 2 430 ? 40.082  0.007   -26.311 1.00 80.13  ? 734  GLY   E O   1 
ATOM   14518 N  N   . VAL   E 2 431 ? 42.247  -0.398  -26.822 1.00 84.84  ? 735  VAL   E N   1 
ATOM   14519 C  CA  . VAL   E 2 431 ? 41.992  -1.732  -27.342 1.00 78.76  ? 735  VAL   E CA  1 
ATOM   14520 C  C   . VAL   E 2 431 ? 43.077  -2.674  -26.835 1.00 79.58  ? 735  VAL   E C   1 
ATOM   14521 O  O   . VAL   E 2 431 ? 44.272  -2.426  -27.048 1.00 77.33  ? 735  VAL   E O   1 
ATOM   14522 C  CB  . VAL   E 2 431 ? 41.915  -1.727  -28.882 1.00 81.12  ? 735  VAL   E CB  1 
ATOM   14523 C  CG1 . VAL   E 2 431 ? 42.268  -3.094  -29.491 1.00 80.93  ? 735  VAL   E CG1 1 
ATOM   14524 C  CG2 . VAL   E 2 431 ? 40.503  -1.294  -29.318 1.00 80.71  ? 735  VAL   E CG2 1 
ATOM   14525 N  N   . LEU   E 2 432 ? 42.662  -3.724  -26.124 1.00 78.29  ? 736  LEU   E N   1 
ATOM   14526 C  CA  . LEU   E 2 432 ? 43.531  -4.858  -25.816 1.00 81.86  ? 736  LEU   E CA  1 
ATOM   14527 C  C   . LEU   E 2 432 ? 43.662  -5.752  -27.045 1.00 79.67  ? 736  LEU   E C   1 
ATOM   14528 O  O   . LEU   E 2 432 ? 42.651  -6.167  -27.616 1.00 76.81  ? 736  LEU   E O   1 
ATOM   14529 C  CB  . LEU   E 2 432 ? 42.954  -5.672  -24.654 1.00 78.90  ? 736  LEU   E CB  1 
ATOM   14530 C  CG  . LEU   E 2 432 ? 42.830  -4.986  -23.315 1.00 77.32  ? 736  LEU   E CG  1 
ATOM   14531 C  CD1 . LEU   E 2 432 ? 42.458  -6.030  -22.271 1.00 71.80  ? 736  LEU   E CD1 1 
ATOM   14532 C  CD2 . LEU   E 2 432 ? 44.173  -4.329  -23.027 1.00 80.47  ? 736  LEU   E CD2 1 
ATOM   14533 N  N   . SER   E 2 433 ? 44.896  -6.050  -27.456 1.00 79.46  ? 737  SER   E N   1 
ATOM   14534 C  CA  . SER   E 2 433 ? 45.114  -6.866  -28.642 1.00 81.59  ? 737  SER   E CA  1 
ATOM   14535 C  C   . SER   E 2 433 ? 46.006  -8.054  -28.313 1.00 85.06  ? 737  SER   E C   1 
ATOM   14536 O  O   . SER   E 2 433 ? 46.724  -8.067  -27.308 1.00 85.32  ? 737  SER   E O   1 
ATOM   14537 C  CB  . SER   E 2 433 ? 45.745  -6.068  -29.803 1.00 81.01  ? 737  SER   E CB  1 
ATOM   14538 O  OG  . SER   E 2 433 ? 47.156  -5.951  -29.645 1.00 80.54  ? 737  SER   E OG  1 
ATOM   14539 N  N   . SER   E 2 434 ? 45.946  -9.060  -29.183 1.00 83.69  ? 738  SER   E N   1 
ATOM   14540 C  CA  . SER   E 2 434 ? 46.850  -10.195 -29.133 1.00 83.18  ? 738  SER   E CA  1 
ATOM   14541 C  C   . SER   E 2 434 ? 47.516  -10.367 -30.489 1.00 84.92  ? 738  SER   E C   1 
ATOM   14542 O  O   . SER   E 2 434 ? 46.951  -9.994  -31.526 1.00 85.84  ? 738  SER   E O   1 
ATOM   14543 C  CB  . SER   E 2 434 ? 46.120  -11.468 -28.730 1.00 83.75  ? 738  SER   E CB  1 
ATOM   14544 O  OG  . SER   E 2 434 ? 46.807  -12.595 -29.241 1.00 94.45  ? 738  SER   E OG  1 
ATOM   14545 N  N   . ARG   E 2 435 ? 48.728  -10.918 -30.471 1.00 84.88  ? 739  ARG   E N   1 
ATOM   14546 C  CA  . ARG   E 2 435 ? 49.504  -11.145 -31.682 1.00 85.89  ? 739  ARG   E CA  1 
ATOM   14547 C  C   . ARG   E 2 435 ? 50.245  -12.456 -31.498 1.00 92.39  ? 739  ARG   E C   1 
ATOM   14548 O  O   . ARG   E 2 435 ? 50.963  -12.620 -30.511 1.00 97.58  ? 739  ARG   E O   1 
ATOM   14549 C  CB  . ARG   E 2 435 ? 50.486  -9.996  -31.945 1.00 86.28  ? 739  ARG   E CB  1 
ATOM   14550 C  CG  . ARG   E 2 435 ? 51.744  -10.423 -32.697 1.00 94.22  ? 739  ARG   E CG  1 
ATOM   14551 C  CD  . ARG   E 2 435 ? 52.673  -9.249  -33.049 1.00 97.16  ? 739  ARG   E CD  1 
ATOM   14552 N  NE  . ARG   E 2 435 ? 53.809  -9.074  -32.146 1.00 92.41  ? 739  ARG   E NE  1 
ATOM   14553 C  CZ  . ARG   E 2 435 ? 53.808  -8.276  -31.088 1.00 92.98  ? 739  ARG   E CZ  1 
ATOM   14554 N  NH1 . ARG   E 2 435 ? 52.712  -7.639  -30.706 1.00 92.56  ? 739  ARG   E NH1 1 
ATOM   14555 N  NH2 . ARG   E 2 435 ? 54.936  -8.101  -30.404 1.00 96.92  ? 739  ARG   E NH2 1 
ATOM   14556 N  N   . ILE   E 2 436 ? 50.055  -13.399 -32.398 1.00 91.48  ? 740  ILE   E N   1 
ATOM   14557 C  CA  . ILE   E 2 436 ? 50.805  -14.639 -32.283 1.00 94.84  ? 740  ILE   E CA  1 
ATOM   14558 C  C   . ILE   E 2 436 ? 52.211  -14.418 -32.810 1.00 99.66  ? 740  ILE   E C   1 
ATOM   14559 O  O   . ILE   E 2 436 ? 52.397  -13.809 -33.872 1.00 100.22 ? 740  ILE   E O   1 
ATOM   14560 C  CB  . ILE   E 2 436 ? 50.109  -15.779 -33.036 1.00 95.37  ? 740  ILE   E CB  1 
ATOM   14561 C  CG1 . ILE   E 2 436 ? 48.683  -15.956 -32.509 1.00 98.04  ? 740  ILE   E CG1 1 
ATOM   14562 C  CG2 . ILE   E 2 436 ? 50.917  -17.052 -32.898 1.00 93.20  ? 740  ILE   E CG2 1 
ATOM   14563 C  CD1 . ILE   E 2 436 ? 48.608  -16.090 -31.005 1.00 102.61 ? 740  ILE   E CD1 1 
ATOM   14564 N  N   . GLU   E 2 437 ? 53.205  -14.905 -32.062 1.00 103.40 ? 741  GLU   E N   1 
ATOM   14565 C  CA  . GLU   E 2 437 ? 54.592  -14.993 -32.510 1.00 106.86 ? 741  GLU   E CA  1 
ATOM   14566 C  C   . GLU   E 2 437 ? 55.083  -16.436 -32.407 1.00 108.89 ? 741  GLU   E C   1 
ATOM   14567 O  O   . GLU   E 2 437 ? 54.398  -17.316 -31.880 1.00 107.29 ? 741  GLU   E O   1 
ATOM   14568 C  CB  . GLU   E 2 437 ? 55.501  -14.050 -31.703 1.00 111.24 ? 741  GLU   E CB  1 
ATOM   14569 C  CG  . GLU   E 2 437 ? 55.602  -12.658 -32.316 1.00 114.51 ? 741  GLU   E CG  1 
ATOM   14570 C  CD  . GLU   E 2 437 ? 56.350  -11.655 -31.444 1.00 119.60 ? 741  GLU   E CD  1 
ATOM   14571 O  OE1 . GLU   E 2 437 ? 57.412  -12.023 -30.890 1.00 126.69 ? 741  GLU   E OE1 1 
ATOM   14572 O  OE2 . GLU   E 2 437 ? 55.878  -10.499 -31.317 1.00 123.60 ? 741  GLU   E OE2 1 
ATOM   14573 N  N   . VAL   E 2 438 ? 56.285  -16.669 -32.936 1.00 116.83 ? 742  VAL   E N   1 
ATOM   14574 C  CA  . VAL   E 2 438 ? 56.893  -17.995 -33.007 1.00 122.97 ? 742  VAL   E CA  1 
ATOM   14575 C  C   . VAL   E 2 438 ? 58.237  -17.940 -32.293 1.00 132.33 ? 742  VAL   E C   1 
ATOM   14576 O  O   . VAL   E 2 438 ? 59.090  -17.112 -32.634 1.00 136.73 ? 742  VAL   E O   1 
ATOM   14577 C  CB  . VAL   E 2 438 ? 57.062  -18.473 -34.462 1.00 120.20 ? 742  VAL   E CB  1 
ATOM   14578 C  CG1 . VAL   E 2 438 ? 58.180  -19.490 -34.568 1.00 129.12 ? 742  VAL   E CG1 1 
ATOM   14579 C  CG2 . VAL   E 2 438 ? 55.772  -19.083 -34.979 1.00 115.25 ? 742  VAL   E CG2 1 
ATOM   14580 N  N   . GLN   E 2 439 ? 58.414  -18.809 -31.296 1.00 134.94 ? 743  GLN   E N   1 
ATOM   14581 C  CA  . GLN   E 2 439 ? 59.694  -19.003 -30.629 1.00 142.63 ? 743  GLN   E CA  1 
ATOM   14582 C  C   . GLN   E 2 439 ? 60.796  -19.258 -31.652 1.00 152.63 ? 743  GLN   E C   1 
ATOM   14583 O  O   . GLN   E 2 439 ? 60.800  -20.304 -32.308 1.00 152.08 ? 743  GLN   E O   1 
ATOM   14584 C  CB  . GLN   E 2 439 ? 59.577  -20.172 -29.650 1.00 144.84 ? 743  GLN   E CB  1 
ATOM   14585 C  CG  . GLN   E 2 439 ? 60.879  -20.854 -29.327 1.00 152.94 ? 743  GLN   E CG  1 
ATOM   14586 C  CD  . GLN   E 2 439 ? 61.652  -20.123 -28.259 1.00 155.82 ? 743  GLN   E CD  1 
ATOM   14587 O  OE1 . GLN   E 2 439 ? 61.335  -18.976 -27.931 1.00 152.17 ? 743  GLN   E OE1 1 
ATOM   14588 N  NE2 . GLN   E 2 439 ? 62.666  -20.780 -27.698 1.00 153.91 ? 743  GLN   E NE2 1 
ATOM   14589 N  N   . ASP   E 2 440 ? 61.730  -18.316 -31.803 1.00 185.46 ? 744  ASP   E N   1 
ATOM   14590 C  CA  . ASP   E 2 440 ? 62.747  -18.396 -32.846 1.00 186.57 ? 744  ASP   E CA  1 
ATOM   14591 C  C   . ASP   E 2 440 ? 64.024  -19.028 -32.284 1.00 188.38 ? 744  ASP   E C   1 
ATOM   14592 O  O   . ASP   E 2 440 ? 64.012  -19.665 -31.227 1.00 188.14 ? 744  ASP   E O   1 
ATOM   14593 C  CB  . ASP   E 2 440 ? 63.008  -17.009 -33.453 1.00 183.80 ? 744  ASP   E CB  1 
ATOM   14594 C  CG  . ASP   E 2 440 ? 63.516  -15.999 -32.431 1.00 183.03 ? 744  ASP   E CG  1 
ATOM   14595 O  OD1 . ASP   E 2 440 ? 64.402  -16.356 -31.628 1.00 182.97 ? 744  ASP   E OD1 1 
ATOM   14596 O  OD2 . ASP   E 2 440 ? 63.038  -14.839 -32.446 1.00 182.93 ? 744  ASP   E OD2 1 
ATOM   14597 N  N   . THR   E 2 441 ? 65.144  -18.851 -32.983 1.00 174.01 ? 745  THR   E N   1 
ATOM   14598 C  CA  . THR   E 2 441 ? 66.386  -19.511 -32.608 1.00 169.27 ? 745  THR   E CA  1 
ATOM   14599 C  C   . THR   E 2 441 ? 67.358  -18.646 -31.808 1.00 165.64 ? 745  THR   E C   1 
ATOM   14600 O  O   . THR   E 2 441 ? 68.371  -19.161 -31.322 1.00 162.46 ? 745  THR   E O   1 
ATOM   14601 C  CB  . THR   E 2 441 ? 67.174  -19.871 -33.879 1.00 166.23 ? 745  THR   E CB  1 
ATOM   14602 O  OG1 . THR   E 2 441 ? 68.522  -20.215 -33.551 1.00 166.18 ? 745  THR   E OG1 1 
ATOM   14603 C  CG2 . THR   E 2 441 ? 67.154  -18.715 -34.891 1.00 163.31 ? 745  THR   E CG2 1 
ATOM   14604 N  N   . SER   E 2 442 ? 67.061  -17.356 -31.613 1.00 165.52 ? 746  SER   E N   1 
ATOM   14605 C  CA  . SER   E 2 442 ? 67.924  -16.477 -30.817 1.00 164.11 ? 746  SER   E CA  1 
ATOM   14606 C  C   . SER   E 2 442 ? 67.388  -16.519 -29.389 1.00 156.44 ? 746  SER   E C   1 
ATOM   14607 O  O   . SER   E 2 442 ? 67.617  -15.585 -28.616 1.00 152.83 ? 746  SER   E O   1 
ATOM   14608 C  CB  . SER   E 2 442 ? 67.963  -15.025 -31.325 1.00 161.40 ? 746  SER   E CB  1 
ATOM   14609 O  OG  . SER   E 2 442 ? 68.738  -14.890 -32.502 1.00 159.74 ? 746  SER   E OG  1 
ATOM   14610 N  N   . GLY   E 2 443 ? 66.673  -17.578 -29.028 1.00 156.59 ? 747  GLY   E N   1 
ATOM   14611 C  CA  . GLY   E 2 443 ? 66.024  -17.603 -27.732 1.00 152.29 ? 747  GLY   E CA  1 
ATOM   14612 C  C   . GLY   E 2 443 ? 64.903  -16.598 -27.602 1.00 152.25 ? 747  GLY   E C   1 
ATOM   14613 O  O   . GLY   E 2 443 ? 64.508  -16.270 -26.479 1.00 145.12 ? 747  GLY   E O   1 
ATOM   14614 N  N   . GLY   E 2 444 ? 64.364  -16.102 -28.715 1.00 153.11 ? 748  GLY   E N   1 
ATOM   14615 C  CA  . GLY   E 2 444 ? 63.331  -15.090 -28.656 1.00 146.98 ? 748  GLY   E CA  1 
ATOM   14616 C  C   . GLY   E 2 444 ? 62.049  -15.455 -29.374 1.00 147.38 ? 748  GLY   E C   1 
ATOM   14617 O  O   . GLY   E 2 444 ? 61.701  -16.632 -29.466 1.00 149.60 ? 748  GLY   E O   1 
ATOM   14618 N  N   . THR   E 2 445 ? 61.343  -14.446 -29.887 1.00 145.09 ? 749  THR   E N   1 
ATOM   14619 C  CA  . THR   E 2 445 ? 60.112  -14.670 -30.641 1.00 137.20 ? 749  THR   E CA  1 
ATOM   14620 C  C   . THR   E 2 445 ? 60.080  -13.713 -31.821 1.00 132.17 ? 749  THR   E C   1 
ATOM   14621 O  O   . THR   E 2 445 ? 60.109  -12.493 -31.639 1.00 133.26 ? 749  THR   E O   1 
ATOM   14622 C  CB  . THR   E 2 445 ? 58.874  -14.482 -29.755 1.00 129.78 ? 749  THR   E CB  1 
ATOM   14623 O  OG1 . THR   E 2 445 ? 59.066  -13.350 -28.896 1.00 132.04 ? 749  THR   E OG1 1 
ATOM   14624 C  CG2 . THR   E 2 445 ? 58.594  -15.725 -28.914 1.00 126.30 ? 749  THR   E CG2 1 
ATOM   14625 N  N   . THR   E 2 446 ? 60.019  -14.270 -33.020 1.00 132.42 ? 750  THR   E N   1 
ATOM   14626 C  CA  . THR   E 2 446 ? 59.892  -13.494 -34.243 1.00 128.37 ? 750  THR   E CA  1 
ATOM   14627 C  C   . THR   E 2 446 ? 58.419  -13.364 -34.618 1.00 124.12 ? 750  THR   E C   1 
ATOM   14628 O  O   . THR   E 2 446 ? 57.627  -14.282 -34.395 1.00 123.69 ? 750  THR   E O   1 
ATOM   14629 C  CB  . THR   E 2 446 ? 60.677  -14.161 -35.377 1.00 130.76 ? 750  THR   E CB  1 
ATOM   14630 O  OG1 . THR   E 2 446 ? 60.188  -15.485 -35.595 1.00 127.86 ? 750  THR   E OG1 1 
ATOM   14631 C  CG2 . THR   E 2 446 ? 62.163  -14.236 -35.038 1.00 134.76 ? 750  THR   E CG2 1 
ATOM   14632 N  N   . ALA   E 2 447 ? 58.050  -12.212 -35.178 1.00 124.42 ? 751  ALA   E N   1 
ATOM   14633 C  CA  . ALA   E 2 447 ? 56.662  -11.958 -35.546 1.00 122.56 ? 751  ALA   E CA  1 
ATOM   14634 C  C   . ALA   E 2 447 ? 56.294  -12.691 -36.839 1.00 123.76 ? 751  ALA   E C   1 
ATOM   14635 O  O   . ALA   E 2 447 ? 57.155  -13.147 -37.602 1.00 125.36 ? 751  ALA   E O   1 
ATOM   14636 C  CB  . ALA   E 2 447 ? 56.413  -10.456 -35.698 1.00 119.12 ? 751  ALA   E CB  1 
ATOM   14637 N  N   . LEU   E 2 448 ? 54.985  -12.817 -37.077 1.00 113.36 ? 752  LEU   E N   1 
ATOM   14638 C  CA  . LEU   E 2 448 ? 54.484  -13.517 -38.257 1.00 111.44 ? 752  LEU   E CA  1 
ATOM   14639 C  C   . LEU   E 2 448 ? 54.190  -12.569 -39.413 1.00 109.95 ? 752  LEU   E C   1 
ATOM   14640 O  O   . LEU   E 2 448 ? 54.599  -12.824 -40.550 1.00 108.42 ? 752  LEU   E O   1 
ATOM   14641 C  CB  . LEU   E 2 448 ? 53.215  -14.315 -37.916 1.00 108.60 ? 752  LEU   E CB  1 
ATOM   14642 C  CG  . LEU   E 2 448 ? 53.260  -15.556 -37.008 1.00 103.44 ? 752  LEU   E CG  1 
ATOM   14643 C  CD1 . LEU   E 2 448 ? 54.083  -16.685 -37.576 1.00 99.53  ? 752  LEU   E CD1 1 
ATOM   14644 C  CD2 . LEU   E 2 448 ? 53.810  -15.173 -35.677 1.00 109.21 ? 752  LEU   E CD2 1 
ATOM   14645 N  N   . ARG   E 2 449 ? 53.511  -11.465 -39.127 1.00 109.52 ? 753  ARG   E N   1 
ATOM   14646 C  CA  . ARG   E 2 449 ? 53.122  -10.468 -40.107 1.00 99.74  ? 753  ARG   E CA  1 
ATOM   14647 C  C   . ARG   E 2 449 ? 53.086  -9.124  -39.402 1.00 98.33  ? 753  ARG   E C   1 
ATOM   14648 O  O   . ARG   E 2 449 ? 52.773  -9.055  -38.204 1.00 97.99  ? 753  ARG   E O   1 
ATOM   14649 C  CB  . ARG   E 2 449 ? 51.746  -10.778 -40.709 1.00 99.24  ? 753  ARG   E CB  1 
ATOM   14650 C  CG  . ARG   E 2 449 ? 50.615  -10.365 -39.764 1.00 104.70 ? 753  ARG   E CG  1 
ATOM   14651 C  CD  . ARG   E 2 449 ? 49.325  -11.133 -39.993 1.00 103.43 ? 753  ARG   E CD  1 
ATOM   14652 N  NE  . ARG   E 2 449 ? 49.439  -12.528 -39.593 1.00 101.99 ? 753  ARG   E NE  1 
ATOM   14653 C  CZ  . ARG   E 2 449 ? 49.583  -13.521 -40.452 1.00 104.35 ? 753  ARG   E CZ  1 
ATOM   14654 N  NH1 . ARG   E 2 449 ? 49.664  -13.289 -41.763 1.00 101.62 ? 753  ARG   E NH1 1 
ATOM   14655 N  NH2 . ARG   E 2 449 ? 49.627  -14.772 -39.990 1.00 110.18 ? 753  ARG   E NH2 1 
ATOM   14656 N  N   . PRO   E 2 450 ? 53.379  -8.039  -40.118 1.00 100.34 ? 754  PRO   E N   1 
ATOM   14657 C  CA  . PRO   E 2 450 ? 53.230  -6.712  -39.524 1.00 96.90  ? 754  PRO   E CA  1 
ATOM   14658 C  C   . PRO   E 2 450 ? 51.783  -6.522  -39.118 1.00 91.67  ? 754  PRO   E C   1 
ATOM   14659 O  O   . PRO   E 2 450 ? 50.870  -6.659  -39.936 1.00 94.30  ? 754  PRO   E O   1 
ATOM   14660 C  CB  . PRO   E 2 450 ? 53.641  -5.772  -40.653 1.00 101.21 ? 754  PRO   E CB  1 
ATOM   14661 C  CG  . PRO   E 2 450 ? 53.216  -6.506  -41.872 1.00 98.64  ? 754  PRO   E CG  1 
ATOM   14662 C  CD  . PRO   E 2 450 ? 53.471  -7.954  -41.585 1.00 101.36 ? 754  PRO   E CD  1 
ATOM   14663 N  N   . SER   E 2 451 ? 51.567  -6.262  -37.852 1.00 88.86  ? 755  SER   E N   1 
ATOM   14664 C  CA  . SER   E 2 451 ? 50.243  -6.170  -37.276 1.00 89.13  ? 755  SER   E CA  1 
ATOM   14665 C  C   . SER   E 2 451 ? 50.186  -4.846  -36.531 1.00 88.03  ? 755  SER   E C   1 
ATOM   14666 O  O   . SER   E 2 451 ? 51.154  -4.088  -36.522 1.00 91.83  ? 755  SER   E O   1 
ATOM   14667 C  CB  . SER   E 2 451 ? 49.961  -7.367  -36.357 1.00 91.88  ? 755  SER   E CB  1 
ATOM   14668 O  OG  . SER   E 2 451 ? 50.919  -7.417  -35.300 1.00 94.68  ? 755  SER   E OG  1 
ATOM   14669 N  N   . ALA   E 2 452 ? 49.047  -4.566  -35.900 1.00 83.67  ? 756  ALA   E N   1 
ATOM   14670 C  CA  . ALA   E 2 452 ? 48.867  -3.256  -35.280 1.00 86.11  ? 756  ALA   E CA  1 
ATOM   14671 C  C   . ALA   E 2 452 ? 50.044  -2.909  -34.380 1.00 90.63  ? 756  ALA   E C   1 
ATOM   14672 O  O   . ALA   E 2 452 ? 50.775  -1.950  -34.638 1.00 99.43  ? 756  ALA   E O   1 
ATOM   14673 C  CB  . ALA   E 2 452 ? 47.554  -3.206  -34.493 1.00 84.50  ? 756  ALA   E CB  1 
ATOM   14674 N  N   . SER   E 2 453 ? 50.247  -3.688  -33.319 1.00 86.72  ? 757  SER   E N   1 
ATOM   14675 C  CA  . SER   E 2 453 ? 51.299  -3.381  -32.354 1.00 90.91  ? 757  SER   E CA  1 
ATOM   14676 C  C   . SER   E 2 453 ? 52.670  -3.210  -33.026 1.00 98.42  ? 757  SER   E C   1 
ATOM   14677 O  O   . SER   E 2 453 ? 53.372  -2.216  -32.786 1.00 98.30  ? 757  SER   E O   1 
ATOM   14678 C  CB  . SER   E 2 453 ? 51.332  -4.474  -31.293 1.00 91.53  ? 757  SER   E CB  1 
ATOM   14679 O  OG  . SER   E 2 453 ? 51.098  -5.741  -31.897 1.00 94.48  ? 757  SER   E OG  1 
ATOM   14680 N  N   . THR   E 2 454 ? 53.060  -4.156  -33.894 1.00 100.18 ? 758  THR   E N   1 
ATOM   14681 C  CA  . THR   E 2 454 ? 54.414  -4.132  -34.460 1.00 100.14 ? 758  THR   E CA  1 
ATOM   14682 C  C   . THR   E 2 454 ? 54.727  -2.802  -35.151 1.00 100.54 ? 758  THR   E C   1 
ATOM   14683 O  O   . THR   E 2 454 ? 55.828  -2.257  -34.997 1.00 103.58 ? 758  THR   E O   1 
ATOM   14684 C  CB  . THR   E 2 454 ? 54.615  -5.311  -35.420 1.00 97.30  ? 758  THR   E CB  1 
ATOM   14685 O  OG1 . THR   E 2 454 ? 53.923  -5.071  -36.658 1.00 96.73  ? 758  THR   E OG1 1 
ATOM   14686 C  CG2 . THR   E 2 454 ? 54.099  -6.598  -34.777 1.00 97.40  ? 758  THR   E CG2 1 
ATOM   14687 N  N   . GLN   E 2 455 ? 53.772  -2.250  -35.893 1.00 99.79  ? 759  GLN   E N   1 
ATOM   14688 C  CA  . GLN   E 2 455 ? 54.033  -1.049  -36.674 1.00 99.12  ? 759  GLN   E CA  1 
ATOM   14689 C  C   . GLN   E 2 455 ? 53.284  0.152   -36.098 1.00 99.40  ? 759  GLN   E C   1 
ATOM   14690 O  O   . GLN   E 2 455 ? 52.566  0.857   -36.811 1.00 100.35 ? 759  GLN   E O   1 
ATOM   14691 C  CB  . GLN   E 2 455 ? 53.658  -1.297  -38.135 1.00 98.12  ? 759  GLN   E CB  1 
ATOM   14692 C  CG  . GLN   E 2 455 ? 54.525  -2.349  -38.819 1.00 100.28 ? 759  GLN   E CG  1 
ATOM   14693 C  CD  . GLN   E 2 455 ? 54.097  -2.599  -40.260 1.00 113.95 ? 759  GLN   E CD  1 
ATOM   14694 O  OE1 . GLN   E 2 455 ? 52.929  -2.380  -40.623 1.00 114.20 ? 759  GLN   E OE1 1 
ATOM   14695 N  NE2 . GLN   E 2 455 ? 55.042  -3.047  -41.098 1.00 115.56 ? 759  GLN   E NE2 1 
ATOM   14696 N  N   . ALA   E 2 456 ? 53.436  0.392   -34.804 1.00 101.75 ? 760  ALA   E N   1 
ATOM   14697 C  CA  . ALA   E 2 456 ? 52.782  1.524   -34.167 1.00 97.03  ? 760  ALA   E CA  1 
ATOM   14698 C  C   . ALA   E 2 456 ? 53.719  2.718   -34.122 1.00 99.61  ? 760  ALA   E C   1 
ATOM   14699 O  O   . ALA   E 2 456 ? 54.936  2.582   -34.256 1.00 106.35 ? 760  ALA   E O   1 
ATOM   14700 C  CB  . ALA   E 2 456 ? 52.335  1.169   -32.750 1.00 100.20 ? 760  ALA   E CB  1 
ATOM   14701 N  N   . LEU   E 2 457 ? 53.134  3.899   -33.906 1.00 102.80 ? 761  LEU   E N   1 
ATOM   14702 C  CA  . LEU   E 2 457 ? 53.910  5.143   -33.924 1.00 103.48 ? 761  LEU   E CA  1 
ATOM   14703 C  C   . LEU   E 2 457 ? 54.813  5.270   -32.696 1.00 99.36  ? 761  LEU   E C   1 
ATOM   14704 O  O   . LEU   E 2 457 ? 56.040  5.350   -32.815 1.00 99.96  ? 761  LEU   E O   1 
ATOM   14705 C  CB  . LEU   E 2 457 ? 52.969  6.342   -34.048 1.00 100.78 ? 761  LEU   E CB  1 
ATOM   14706 C  CG  . LEU   E 2 457 ? 52.619  6.634   -35.512 1.00 103.86 ? 761  LEU   E CG  1 
ATOM   14707 C  CD1 . LEU   E 2 457 ? 52.212  8.086   -35.714 1.00 108.37 ? 761  LEU   E CD1 1 
ATOM   14708 C  CD2 . LEU   E 2 457 ? 53.783  6.250   -36.430 1.00 105.66 ? 761  LEU   E CD2 1 
ATOM   14709 N  N   . SER   E 2 458 ? 54.232  5.300   -31.511 1.00 97.72  ? 762  SER   E N   1 
ATOM   14710 C  CA  . SER   E 2 458 ? 55.012  5.118   -30.300 1.00 103.49 ? 762  SER   E CA  1 
ATOM   14711 C  C   . SER   E 2 458 ? 54.820  3.693   -29.791 1.00 99.94  ? 762  SER   E C   1 
ATOM   14712 O  O   . SER   E 2 458 ? 53.761  3.090   -29.978 1.00 100.06 ? 762  SER   E O   1 
ATOM   14713 C  CB  . SER   E 2 458 ? 54.605  6.131   -29.220 1.00 107.26 ? 762  SER   E CB  1 
ATOM   14714 O  OG  . SER   E 2 458 ? 54.907  7.461   -29.611 1.00 108.19 ? 762  SER   E OG  1 
ATOM   14715 N  N   . SER   E 2 459 ? 55.850  3.153   -29.152 1.00 98.52  ? 763  SER   E N   1 
ATOM   14716 C  CA  . SER   E 2 459 ? 55.734  1.863   -28.492 1.00 96.96  ? 763  SER   E CA  1 
ATOM   14717 C  C   . SER   E 2 459 ? 56.382  1.927   -27.122 1.00 99.48  ? 763  SER   E C   1 
ATOM   14718 O  O   . SER   E 2 459 ? 57.363  2.641   -26.914 1.00 108.39 ? 763  SER   E O   1 
ATOM   14719 C  CB  . SER   E 2 459 ? 56.387  0.748   -29.307 1.00 96.35  ? 763  SER   E CB  1 
ATOM   14720 O  OG  . SER   E 2 459 ? 57.778  0.974   -29.413 1.00 107.06 ? 763  SER   E OG  1 
ATOM   14721 N  N   . SER   E 2 460 ? 55.827  1.163   -26.189 1.00 102.04 ? 764  SER   E N   1 
ATOM   14722 C  CA  . SER   E 2 460 ? 56.398  1.015   -24.859 1.00 98.55  ? 764  SER   E CA  1 
ATOM   14723 C  C   . SER   E 2 460 ? 56.204  -0.430  -24.417 1.00 103.22 ? 764  SER   E C   1 
ATOM   14724 O  O   . SER   E 2 460 ? 55.307  -1.125  -24.906 1.00 102.29 ? 764  SER   E O   1 
ATOM   14725 C  CB  . SER   E 2 460 ? 55.733  1.976   -23.880 1.00 97.80  ? 764  SER   E CB  1 
ATOM   14726 O  OG  . SER   E 2 460 ? 54.344  1.724   -23.829 1.00 97.39  ? 764  SER   E OG  1 
ATOM   14727 N  N   . VAL   E 2 461 ? 57.061  -0.888  -23.497 1.00 107.67 ? 765  VAL   E N   1 
ATOM   14728 C  CA  . VAL   E 2 461 ? 56.961  -2.229  -22.919 1.00 103.52 ? 765  VAL   E CA  1 
ATOM   14729 C  C   . VAL   E 2 461 ? 56.933  -2.111  -21.402 1.00 105.51 ? 765  VAL   E C   1 
ATOM   14730 O  O   . VAL   E 2 461 ? 57.676  -1.314  -20.817 1.00 110.12 ? 765  VAL   E O   1 
ATOM   14731 C  CB  . VAL   E 2 461 ? 58.121  -3.134  -23.367 1.00 100.93 ? 765  VAL   E CB  1 
ATOM   14732 C  CG1 . VAL   E 2 461 ? 57.912  -3.582  -24.805 1.00 100.78 ? 765  VAL   E CG1 1 
ATOM   14733 C  CG2 . VAL   E 2 461 ? 59.423  -2.374  -23.260 1.00 104.87 ? 765  VAL   E CG2 1 
ATOM   14734 N  N   . SER   E 2 462 ? 56.065  -2.889  -20.762 1.00 106.81 ? 766  SER   E N   1 
ATOM   14735 C  CA  . SER   E 2 462 ? 55.939  -2.798  -19.315 1.00 108.94 ? 766  SER   E CA  1 
ATOM   14736 C  C   . SER   E 2 462 ? 57.196  -3.360  -18.673 1.00 115.62 ? 766  SER   E C   1 
ATOM   14737 O  O   . SER   E 2 462 ? 57.810  -4.297  -19.192 1.00 109.19 ? 766  SER   E O   1 
ATOM   14738 C  CB  . SER   E 2 462 ? 54.702  -3.555  -18.834 1.00 103.36 ? 766  SER   E CB  1 
ATOM   14739 O  OG  . SER   E 2 462 ? 54.586  -3.517  -17.421 1.00 105.34 ? 766  SER   E OG  1 
ATOM   14740 N  N   . SER   E 2 463 ? 57.610  -2.759  -17.564 1.00 129.48 ? 767  SER   E N   1 
ATOM   14741 C  CA  . SER   E 2 463 ? 58.762  -3.279  -16.821 1.00 135.13 ? 767  SER   E CA  1 
ATOM   14742 C  C   . SER   E 2 463 ? 58.491  -3.057  -15.338 1.00 139.50 ? 767  SER   E C   1 
ATOM   14743 O  O   . SER   E 2 463 ? 58.837  -2.009  -14.785 1.00 139.63 ? 767  SER   E O   1 
ATOM   14744 C  CB  . SER   E 2 463 ? 60.062  -2.617  -17.241 1.00 138.99 ? 767  SER   E CB  1 
ATOM   14745 O  OG  . SER   E 2 463 ? 60.375  -1.604  -16.307 1.00 142.70 ? 767  SER   E OG  1 
ATOM   14746 N  N   . SER   E 2 464 ? 57.874  -4.045  -14.706 1.00 135.00 ? 768  SER   E N   1 
ATOM   14747 C  CA  . SER   E 2 464 ? 57.572  -3.981  -13.286 1.00 135.58 ? 768  SER   E CA  1 
ATOM   14748 C  C   . SER   E 2 464 ? 58.401  -4.946  -12.462 1.00 138.40 ? 768  SER   E C   1 
ATOM   14749 O  O   . SER   E 2 464 ? 58.814  -4.603  -11.352 1.00 135.01 ? 768  SER   E O   1 
ATOM   14750 C  CB  . SER   E 2 464 ? 56.085  -4.268  -13.048 1.00 132.13 ? 768  SER   E CB  1 
ATOM   14751 O  OG  . SER   E 2 464 ? 55.811  -4.366  -11.661 1.00 134.05 ? 768  SER   E OG  1 
ATOM   14752 N  N   . LYS   E 2 465 ? 58.665  -6.142  -12.988 1.00 138.02 ? 769  LYS   E N   1 
ATOM   14753 C  CA  . LYS   E 2 465 ? 59.407  -7.168  -12.265 1.00 141.79 ? 769  LYS   E CA  1 
ATOM   14754 C  C   . LYS   E 2 465 ? 58.722  -7.539  -10.948 1.00 144.64 ? 769  LYS   E C   1 
ATOM   14755 O  O   . LYS   E 2 465 ? 59.382  -7.986  -10.004 1.00 142.53 ? 769  LYS   E O   1 
ATOM   14756 C  CB  . LYS   E 2 465 ? 60.855  -6.722  -12.017 1.00 139.97 ? 769  LYS   E CB  1 
ATOM   14757 N  N   . LEU   E 2 466 ? 57.390  -7.361  -10.874 1.00 147.15 ? 770  LEU   E N   1 
ATOM   14758 C  CA  . LEU   E 2 466 ? 56.633  -7.704  -9.666  1.00 145.91 ? 770  LEU   E CA  1 
ATOM   14759 C  C   . LEU   E 2 466 ? 56.551  -9.207  -9.458  1.00 143.07 ? 770  LEU   E C   1 
ATOM   14760 O  O   . LEU   E 2 466 ? 56.213  -9.661  -8.356  1.00 138.86 ? 770  LEU   E O   1 
ATOM   14761 C  CB  . LEU   E 2 466 ? 55.210  -7.119  -9.730  1.00 138.97 ? 770  LEU   E CB  1 
ATOM   14762 N  N   . PHE   E 2 467 ? 56.859  -9.977  -10.492 1.00 143.34 ? 771  PHE   E N   1 
ATOM   14763 C  CA  . PHE   E 2 467 ? 56.806  -11.424 -10.428 1.00 141.68 ? 771  PHE   E CA  1 
ATOM   14764 C  C   . PHE   E 2 467 ? 58.049  -12.039 -11.053 1.00 141.82 ? 771  PHE   E C   1 
ATOM   14765 O  O   . PHE   E 2 467 ? 59.043  -11.349 -11.267 1.00 138.88 ? 771  PHE   E O   1 
ATOM   14766 C  CB  . PHE   E 2 467 ? 55.556  -11.929 -11.142 1.00 134.12 ? 771  PHE   E CB  1 
ATOM   14767 C  CG  . PHE   E 2 467 ? 54.317  -11.154 -10.811 1.00 133.90 ? 771  PHE   E CG  1 
ATOM   14768 C  CD1 . PHE   E 2 467 ? 53.715  -11.280 -9.564  1.00 130.19 ? 771  PHE   E CD1 1 
ATOM   14769 C  CD2 . PHE   E 2 467 ? 53.743  -10.310 -11.753 1.00 134.25 ? 771  PHE   E CD2 1 
ATOM   14770 C  CE1 . PHE   E 2 467 ? 52.581  -10.570 -9.256  1.00 128.87 ? 771  PHE   E CE1 1 
ATOM   14771 C  CE2 . PHE   E 2 467 ? 52.595  -9.602  -11.468 1.00 130.12 ? 771  PHE   E CE2 1 
ATOM   14772 C  CZ  . PHE   E 2 467 ? 52.009  -9.728  -10.218 1.00 127.89 ? 771  PHE   E CZ  1 
ATOM   14773 N  N   . THR   E 2 476 ? 62.164  -24.758 -22.631 1.00 165.86 ? 780  THR   E N   1 
ATOM   14774 C  CA  . THR   E 2 476 ? 60.885  -24.218 -22.171 1.00 168.81 ? 780  THR   E CA  1 
ATOM   14775 C  C   . THR   E 2 476 ? 59.906  -24.039 -23.351 1.00 173.60 ? 780  THR   E C   1 
ATOM   14776 O  O   . THR   E 2 476 ? 58.689  -24.143 -23.176 1.00 171.07 ? 780  THR   E O   1 
ATOM   14777 C  CB  . THR   E 2 476 ? 61.078  -22.869 -21.409 1.00 162.75 ? 780  THR   E CB  1 
ATOM   14778 O  OG1 . THR   E 2 476 ? 62.070  -22.072 -22.069 1.00 165.41 ? 780  THR   E OG1 1 
ATOM   14779 C  CG2 . THR   E 2 476 ? 61.501  -23.108 -19.953 1.00 153.53 ? 780  THR   E CG2 1 
ATOM   14780 N  N   . SER   E 2 477 ? 60.446  -23.770 -24.542 1.00 180.18 ? 781  SER   E N   1 
ATOM   14781 C  CA  . SER   E 2 477 ? 59.685  -23.791 -25.787 1.00 177.44 ? 781  SER   E CA  1 
ATOM   14782 C  C   . SER   E 2 477 ? 60.675  -23.876 -26.940 1.00 174.83 ? 781  SER   E C   1 
ATOM   14783 O  O   . SER   E 2 477 ? 61.820  -23.432 -26.817 1.00 176.17 ? 781  SER   E O   1 
ATOM   14784 C  CB  . SER   E 2 477 ? 58.775  -22.560 -25.941 1.00 175.56 ? 781  SER   E CB  1 
ATOM   14785 O  OG  . SER   E 2 477 ? 59.513  -21.355 -26.035 1.00 176.66 ? 781  SER   E OG  1 
ATOM   14786 N  N   . PHE   E 2 478 ? 60.234  -24.460 -28.057 1.00 155.93 ? 782  PHE   E N   1 
ATOM   14787 C  CA  . PHE   E 2 478 ? 61.130  -24.666 -29.195 1.00 147.34 ? 782  PHE   E CA  1 
ATOM   14788 C  C   . PHE   E 2 478 ? 60.293  -24.583 -30.468 1.00 139.61 ? 782  PHE   E C   1 
ATOM   14789 O  O   . PHE   E 2 478 ? 59.644  -25.558 -30.846 1.00 137.63 ? 782  PHE   E O   1 
ATOM   14790 C  CB  . PHE   E 2 478 ? 61.858  -25.997 -29.085 1.00 142.39 ? 782  PHE   E CB  1 
ATOM   14791 N  N   . GLY   E 2 479 ? 60.310  -23.417 -31.119 1.00 138.66 ? 783  GLY   E N   1 
ATOM   14792 C  CA  . GLY   E 2 479 ? 59.529  -23.188 -32.322 1.00 135.32 ? 783  GLY   E CA  1 
ATOM   14793 C  C   . GLY   E 2 479 ? 58.031  -23.013 -32.128 1.00 134.54 ? 783  GLY   E C   1 
ATOM   14794 O  O   . GLY   E 2 479 ? 57.313  -22.870 -33.126 1.00 124.34 ? 783  GLY   E O   1 
ATOM   14795 N  N   . GLU   E 2 480 ? 57.540  -22.998 -30.879 1.00 132.63 ? 784  GLU   E N   1 
ATOM   14796 C  CA  . GLU   E 2 480 ? 56.114  -23.011 -30.563 1.00 122.68 ? 784  GLU   E CA  1 
ATOM   14797 C  C   . GLU   E 2 480 ? 55.495  -21.620 -30.722 1.00 118.34 ? 784  GLU   E C   1 
ATOM   14798 O  O   . GLU   E 2 480 ? 56.192  -20.606 -30.800 1.00 121.82 ? 784  GLU   E O   1 
ATOM   14799 C  CB  . GLU   E 2 480 ? 55.892  -23.526 -29.141 1.00 121.90 ? 784  GLU   E CB  1 
ATOM   14800 N  N   . GLU   E 2 481 ? 54.160  -21.577 -30.764 1.00 112.45 ? 785  GLU   E N   1 
ATOM   14801 C  CA  . GLU   E 2 481 ? 53.442  -20.313 -30.873 1.00 103.69 ? 785  GLU   E CA  1 
ATOM   14802 C  C   . GLU   E 2 481 ? 53.352  -19.624 -29.517 1.00 106.31 ? 785  GLU   E C   1 
ATOM   14803 O  O   . GLU   E 2 481 ? 53.230  -20.277 -28.477 1.00 102.38 ? 785  GLU   E O   1 
ATOM   14804 C  CB  . GLU   E 2 481 ? 52.037  -20.527 -31.437 1.00 98.21  ? 785  GLU   E CB  1 
ATOM   14805 C  CG  . GLU   E 2 481 ? 52.029  -21.075 -32.850 1.00 106.52 ? 785  GLU   E CG  1 
ATOM   14806 C  CD  . GLU   E 2 481 ? 50.648  -21.063 -33.512 1.00 109.98 ? 785  GLU   E CD  1 
ATOM   14807 O  OE1 . GLU   E 2 481 ? 49.627  -21.123 -32.778 1.00 107.04 ? 785  GLU   E OE1 1 
ATOM   14808 O  OE2 . GLU   E 2 481 ? 50.595  -20.993 -34.775 1.00 105.01 ? 785  GLU   E OE2 1 
ATOM   14809 N  N   . VAL   E 2 482 ? 53.398  -18.289 -29.541 1.00 108.46 ? 786  VAL   E N   1 
ATOM   14810 C  CA  . VAL   E 2 482 ? 53.388  -17.457 -28.342 1.00 102.17 ? 786  VAL   E CA  1 
ATOM   14811 C  C   . VAL   E 2 482 ? 52.454  -16.276 -28.572 1.00 98.02  ? 786  VAL   E C   1 
ATOM   14812 O  O   . VAL   E 2 482 ? 52.201  -15.872 -29.711 1.00 99.41  ? 786  VAL   E O   1 
ATOM   14813 C  CB  . VAL   E 2 482 ? 54.814  -16.974 -27.982 1.00 104.07 ? 786  VAL   E CB  1 
ATOM   14814 C  CG1 . VAL   E 2 482 ? 54.798  -15.971 -26.840 1.00 105.36 ? 786  VAL   E CG1 1 
ATOM   14815 C  CG2 . VAL   E 2 482 ? 55.707  -18.162 -27.653 1.00 101.83 ? 786  VAL   E CG2 1 
ATOM   14816 N  N   . GLU   E 2 483 ? 51.922  -15.730 -27.483 1.00 97.20  ? 787  GLU   E N   1 
ATOM   14817 C  CA  . GLU   E 2 483 ? 51.017  -14.587 -27.537 1.00 93.45  ? 787  GLU   E CA  1 
ATOM   14818 C  C   . GLU   E 2 483 ? 51.678  -13.362 -26.942 1.00 94.33  ? 787  GLU   E C   1 
ATOM   14819 O  O   . GLU   E 2 483 ? 52.187  -13.410 -25.821 1.00 92.72  ? 787  GLU   E O   1 
ATOM   14820 C  CB  . GLU   E 2 483 ? 49.729  -14.824 -26.759 1.00 94.57  ? 787  GLU   E CB  1 
ATOM   14821 C  CG  . GLU   E 2 483 ? 48.814  -15.803 -27.396 1.00 102.53 ? 787  GLU   E CG  1 
ATOM   14822 C  CD  . GLU   E 2 483 ? 47.464  -15.878 -26.698 1.00 106.28 ? 787  GLU   E CD  1 
ATOM   14823 O  OE1 . GLU   E 2 483 ? 47.397  -15.875 -25.441 1.00 109.75 ? 787  GLU   E OE1 1 
ATOM   14824 O  OE2 . GLU   E 2 483 ? 46.458  -15.981 -27.432 1.00 114.08 ? 787  GLU   E OE2 1 
ATOM   14825 N  N   . VAL   E 2 484 ? 51.592  -12.252 -27.664 1.00 98.04  ? 788  VAL   E N   1 
ATOM   14826 C  CA  . VAL   E 2 484 ? 51.991  -10.938 -27.178 1.00 90.55  ? 788  VAL   E CA  1 
ATOM   14827 C  C   . VAL   E 2 484 ? 50.720  -10.132 -26.970 1.00 86.77  ? 788  VAL   E C   1 
ATOM   14828 O  O   . VAL   E 2 484 ? 49.932  -9.974  -27.909 1.00 86.81  ? 788  VAL   E O   1 
ATOM   14829 C  CB  . VAL   E 2 484 ? 52.937  -10.240 -28.168 1.00 93.28  ? 788  VAL   E CB  1 
ATOM   14830 C  CG1 . VAL   E 2 484 ? 53.530  -8.963  -27.559 1.00 96.46  ? 788  VAL   E CG1 1 
ATOM   14831 C  CG2 . VAL   E 2 484 ? 54.032  -11.208 -28.627 1.00 95.12  ? 788  VAL   E CG2 1 
ATOM   14832 N  N   . HIS   E 2 485 ? 50.499  -9.652  -25.745 1.00 88.55  ? 789  HIS   E N   1 
ATOM   14833 C  CA  . HIS   E 2 485 ? 49.343  -8.811  -25.434 1.00 88.41  ? 789  HIS   E CA  1 
ATOM   14834 C  C   . HIS   E 2 485 ? 49.769  -7.349  -25.381 1.00 87.06  ? 789  HIS   E C   1 
ATOM   14835 O  O   . HIS   E 2 485 ? 50.783  -7.013  -24.759 1.00 85.71  ? 789  HIS   E O   1 
ATOM   14836 C  CB  . HIS   E 2 485 ? 48.683  -9.209  -24.112 1.00 84.03  ? 789  HIS   E CB  1 
ATOM   14837 C  CG  . HIS   E 2 485 ? 47.873  -10.464 -24.196 1.00 92.27  ? 789  HIS   E CG  1 
ATOM   14838 N  ND1 . HIS   E 2 485 ? 46.651  -10.602 -23.570 1.00 94.00  ? 789  HIS   E ND1 1 
ATOM   14839 C  CD2 . HIS   E 2 485 ? 48.111  -11.641 -24.829 1.00 92.36  ? 789  HIS   E CD2 1 
ATOM   14840 C  CE1 . HIS   E 2 485 ? 46.170  -11.809 -23.822 1.00 93.93  ? 789  HIS   E CE1 1 
ATOM   14841 N  NE2 . HIS   E 2 485 ? 47.035  -12.458 -24.584 1.00 91.33  ? 789  HIS   E NE2 1 
ATOM   14842 N  N   . ASN   E 2 486 ? 49.003  -6.486  -26.045 1.00 83.32  ? 790  ASN   E N   1 
ATOM   14843 C  CA  . ASN   E 2 486 ? 49.294  -5.064  -26.048 1.00 85.89  ? 790  ASN   E CA  1 
ATOM   14844 C  C   . ASN   E 2 486 ? 48.020  -4.280  -25.755 1.00 86.62  ? 790  ASN   E C   1 
ATOM   14845 O  O   . ASN   E 2 486 ? 46.901  -4.734  -26.030 1.00 82.63  ? 790  ASN   E O   1 
ATOM   14846 C  CB  . ASN   E 2 486 ? 49.928  -4.610  -27.388 1.00 84.22  ? 790  ASN   E CB  1 
ATOM   14847 C  CG  . ASN   E 2 486 ? 51.118  -5.477  -27.797 1.00 91.36  ? 790  ASN   E CG  1 
ATOM   14848 O  OD1 . ASN   E 2 486 ? 50.970  -6.684  -27.990 1.00 92.21  ? 790  ASN   E OD1 1 
ATOM   14849 N  ND2 . ASN   E 2 486 ? 52.296  -4.859  -27.957 1.00 95.99  ? 790  ASN   E ND2 1 
ATOM   14850 N  N   . LEU   E 2 487 ? 48.214  -3.126  -25.123 1.00 86.67  ? 791  LEU   E N   1 
ATOM   14851 C  CA  . LEU   E 2 487 ? 47.221  -2.070  -25.080 1.00 84.97  ? 791  LEU   E CA  1 
ATOM   14852 C  C   . LEU   E 2 487 ? 47.511  -1.186  -26.282 1.00 86.66  ? 791  LEU   E C   1 
ATOM   14853 O  O   . LEU   E 2 487 ? 48.619  -0.650  -26.403 1.00 89.25  ? 791  LEU   E O   1 
ATOM   14854 C  CB  . LEU   E 2 487 ? 47.308  -1.294  -23.766 1.00 83.79  ? 791  LEU   E CB  1 
ATOM   14855 C  CG  . LEU   E 2 487 ? 46.471  -0.027  -23.636 1.00 81.36  ? 791  LEU   E CG  1 
ATOM   14856 C  CD1 . LEU   E 2 487 ? 45.048  -0.291  -24.056 1.00 81.00  ? 791  LEU   E CD1 1 
ATOM   14857 C  CD2 . LEU   E 2 487 ? 46.517  0.483   -22.214 1.00 81.97  ? 791  LEU   E CD2 1 
ATOM   14858 N  N   . LEU   E 2 488 ? 46.563  -1.112  -27.213 1.00 82.75  ? 792  LEU   E N   1 
ATOM   14859 C  CA  . LEU   E 2 488 ? 46.708  -0.248  -28.375 1.00 85.14  ? 792  LEU   E CA  1 
ATOM   14860 C  C   . LEU   E 2 488 ? 46.007  1.074   -28.099 1.00 85.65  ? 792  LEU   E C   1 
ATOM   14861 O  O   . LEU   E 2 488 ? 45.039  1.140   -27.334 1.00 87.10  ? 792  LEU   E O   1 
ATOM   14862 C  CB  . LEU   E 2 488 ? 46.123  -0.889  -29.644 1.00 87.29  ? 792  LEU   E CB  1 
ATOM   14863 C  CG  . LEU   E 2 488 ? 46.518  -2.293  -30.153 1.00 82.36  ? 792  LEU   E CG  1 
ATOM   14864 C  CD1 . LEU   E 2 488 ? 45.589  -2.701  -31.282 1.00 75.91  ? 792  LEU   E CD1 1 
ATOM   14865 C  CD2 . LEU   E 2 488 ? 47.985  -2.420  -30.608 1.00 83.23  ? 792  LEU   E CD2 1 
ATOM   14866 N  N   . ILE   E 2 489 ? 46.502  2.131   -28.728 1.00 85.95  ? 793  ILE   E N   1 
ATOM   14867 C  CA  . ILE   E 2 489 ? 45.925  3.463   -28.597 1.00 91.74  ? 793  ILE   E CA  1 
ATOM   14868 C  C   . ILE   E 2 489 ? 45.575  3.923   -30.007 1.00 91.38  ? 793  ILE   E C   1 
ATOM   14869 O  O   . ILE   E 2 489 ? 46.466  4.200   -30.820 1.00 94.14  ? 793  ILE   E O   1 
ATOM   14870 C  CB  . ILE   E 2 489 ? 46.882  4.439   -27.885 1.00 94.01  ? 793  ILE   E CB  1 
ATOM   14871 C  CG1 . ILE   E 2 489 ? 46.852  4.213   -26.366 1.00 87.53  ? 793  ILE   E CG1 1 
ATOM   14872 C  CG2 . ILE   E 2 489 ? 46.542  5.876   -28.218 1.00 95.50  ? 793  ILE   E CG2 1 
ATOM   14873 C  CD1 . ILE   E 2 489 ? 45.475  4.332   -25.759 1.00 83.83  ? 793  ILE   E CD1 1 
ATOM   14874 N  N   . ILE   E 2 490 ? 44.283  3.972   -30.317 1.00 89.40  ? 794  ILE   E N   1 
ATOM   14875 C  CA  . ILE   E 2 490 ? 43.821  4.280   -31.665 1.00 89.64  ? 794  ILE   E CA  1 
ATOM   14876 C  C   . ILE   E 2 490 ? 43.229  5.685   -31.680 1.00 92.36  ? 794  ILE   E C   1 
ATOM   14877 O  O   . ILE   E 2 490 ? 42.585  6.125   -30.715 1.00 90.13  ? 794  ILE   E O   1 
ATOM   14878 C  CB  . ILE   E 2 490 ? 42.806  3.230   -32.167 1.00 86.95  ? 794  ILE   E CB  1 
ATOM   14879 C  CG1 . ILE   E 2 490 ? 43.492  1.872   -32.299 1.00 86.48  ? 794  ILE   E CG1 1 
ATOM   14880 C  CG2 . ILE   E 2 490 ? 42.170  3.652   -33.496 1.00 84.97  ? 794  ILE   E CG2 1 
ATOM   14881 C  CD1 . ILE   E 2 490 ? 43.020  0.846   -31.278 1.00 86.79  ? 794  ILE   E CD1 1 
ATOM   14882 N  N   . ASP   E 2 491 ? 43.468  6.393   -32.775 1.00 90.44  ? 795  ASP   E N   1 
ATOM   14883 C  CA  . ASP   E 2 491 ? 43.015  7.761   -32.914 1.00 89.49  ? 795  ASP   E CA  1 
ATOM   14884 C  C   . ASP   E 2 491 ? 41.595  7.761   -33.440 1.00 89.89  ? 795  ASP   E C   1 
ATOM   14885 O  O   . ASP   E 2 491 ? 41.332  7.264   -34.539 1.00 90.14  ? 795  ASP   E O   1 
ATOM   14886 C  CB  . ASP   E 2 491 ? 43.923  8.544   -33.848 1.00 93.63  ? 795  ASP   E CB  1 
ATOM   14887 C  CG  . ASP   E 2 491 ? 43.708  10.018  -33.718 1.00 98.54  ? 795  ASP   E CG  1 
ATOM   14888 O  OD1 . ASP   E 2 491 ? 44.253  10.600  -32.740 1.00 93.20  ? 795  ASP   E OD1 1 
ATOM   14889 O  OD2 . ASP   E 2 491 ? 42.960  10.579  -34.560 1.00 95.07  ? 795  ASP   E OD2 1 
ATOM   14890 N  N   . GLN   E 2 492 ? 40.683  8.334   -32.662 1.00 93.25  ? 796  GLN   E N   1 
ATOM   14891 C  CA  . GLN   E 2 492 ? 39.285  8.293   -33.061 1.00 92.91  ? 796  GLN   E CA  1 
ATOM   14892 C  C   . GLN   E 2 492 ? 39.067  8.844   -34.463 1.00 89.79  ? 796  GLN   E C   1 
ATOM   14893 O  O   . GLN   E 2 492 ? 38.091  8.472   -35.120 1.00 84.35  ? 796  GLN   E O   1 
ATOM   14894 C  CB  . GLN   E 2 492 ? 38.429  9.036   -32.025 1.00 93.75  ? 796  GLN   E CB  1 
ATOM   14895 C  CG  . GLN   E 2 492 ? 38.357  10.537  -32.176 1.00 92.28  ? 796  GLN   E CG  1 
ATOM   14896 C  CD  . GLN   E 2 492 ? 37.267  11.133  -31.304 1.00 94.45  ? 796  GLN   E CD  1 
ATOM   14897 O  OE1 . GLN   E 2 492 ? 37.411  11.205  -30.084 1.00 96.35  ? 796  GLN   E OE1 1 
ATOM   14898 N  NE2 . GLN   E 2 492 ? 36.161  11.551  -31.925 1.00 92.84  ? 796  GLN   E NE2 1 
ATOM   14899 N  N   . HIS   E 2 493 ? 39.957  9.701   -34.967 1.00 94.96  ? 797  HIS   E N   1 
ATOM   14900 C  CA  . HIS   E 2 493 ? 39.763  10.321  -36.278 1.00 94.12  ? 797  HIS   E CA  1 
ATOM   14901 C  C   . HIS   E 2 493 ? 40.417  9.484   -37.371 1.00 94.98  ? 797  HIS   E C   1 
ATOM   14902 O  O   . HIS   E 2 493 ? 39.742  8.934   -38.247 1.00 92.94  ? 797  HIS   E O   1 
ATOM   14903 C  CB  . HIS   E 2 493 ? 40.330  11.744  -36.278 1.00 96.91  ? 797  HIS   E CB  1 
ATOM   14904 C  CG  . HIS   E 2 493 ? 39.696  12.660  -35.277 1.00 96.87  ? 797  HIS   E CG  1 
ATOM   14905 N  ND1 . HIS   E 2 493 ? 38.395  13.107  -35.389 1.00 95.81  ? 797  HIS   E ND1 1 
ATOM   14906 C  CD2 . HIS   E 2 493 ? 40.203  13.246  -34.166 1.00 95.90  ? 797  HIS   E CD2 1 
ATOM   14907 C  CE1 . HIS   E 2 493 ? 38.123  13.913  -34.376 1.00 98.54  ? 797  HIS   E CE1 1 
ATOM   14908 N  NE2 . HIS   E 2 493 ? 39.202  14.011  -33.619 1.00 98.78  ? 797  HIS   E NE2 1 
ATOM   14909 N  N   . THR   E 2 494 ? 41.740  9.397   -37.322 1.00 96.11  ? 798  THR   E N   1 
ATOM   14910 C  CA  . THR   E 2 494 ? 42.493  8.648   -38.314 1.00 97.89  ? 798  THR   E CA  1 
ATOM   14911 C  C   . THR   E 2 494 ? 42.356  7.142   -38.123 1.00 95.21  ? 798  THR   E C   1 
ATOM   14912 O  O   . THR   E 2 494 ? 42.426  6.387   -39.100 1.00 95.19  ? 798  THR   E O   1 
ATOM   14913 C  CB  . THR   E 2 494 ? 43.960  9.060   -38.239 1.00 98.63  ? 798  THR   E CB  1 
ATOM   14914 O  OG1 . THR   E 2 494 ? 44.451  8.794   -36.922 1.00 101.91 ? 798  THR   E OG1 1 
ATOM   14915 C  CG2 . THR   E 2 494 ? 44.104  10.545  -38.541 1.00 97.54  ? 798  THR   E CG2 1 
ATOM   14916 N  N   . PHE   E 2 495 ? 42.151  6.688   -36.890 1.00 94.36  ? 799  PHE   E N   1 
ATOM   14917 C  CA  . PHE   E 2 495 ? 42.122  5.262   -36.590 1.00 90.01  ? 799  PHE   E CA  1 
ATOM   14918 C  C   . PHE   E 2 495 ? 43.474  4.609   -36.868 1.00 90.37  ? 799  PHE   E C   1 
ATOM   14919 O  O   . PHE   E 2 495 ? 43.549  3.523   -37.429 1.00 100.06 ? 799  PHE   E O   1 
ATOM   14920 C  CB  . PHE   E 2 495 ? 41.021  4.554   -37.377 1.00 85.98  ? 799  PHE   E CB  1 
ATOM   14921 C  CG  . PHE   E 2 495 ? 39.671  4.708   -36.780 1.00 89.56  ? 799  PHE   E CG  1 
ATOM   14922 C  CD1 . PHE   E 2 495 ? 39.407  4.200   -35.519 1.00 91.96  ? 799  PHE   E CD1 1 
ATOM   14923 C  CD2 . PHE   E 2 495 ? 38.649  5.338   -37.472 1.00 88.51  ? 799  PHE   E CD2 1 
ATOM   14924 C  CE1 . PHE   E 2 495 ? 38.146  4.330   -34.942 1.00 87.05  ? 799  PHE   E CE1 1 
ATOM   14925 C  CE2 . PHE   E 2 495 ? 37.389  5.461   -36.909 1.00 84.31  ? 799  PHE   E CE2 1 
ATOM   14926 C  CZ  . PHE   E 2 495 ? 37.137  4.956   -35.640 1.00 82.53  ? 799  PHE   E CZ  1 
ATOM   14927 N  N   . GLU   E 2 496 ? 44.551  5.283   -36.498 1.00 88.52  ? 800  GLU   E N   1 
ATOM   14928 C  CA  . GLU   E 2 496 ? 45.886  4.712   -36.582 1.00 90.41  ? 800  GLU   E CA  1 
ATOM   14929 C  C   . GLU   E 2 496 ? 46.412  4.512   -35.167 1.00 95.01  ? 800  GLU   E C   1 
ATOM   14930 O  O   . GLU   E 2 496 ? 45.906  5.112   -34.214 1.00 92.49  ? 800  GLU   E O   1 
ATOM   14931 C  CB  . GLU   E 2 496 ? 46.835  5.610   -37.390 1.00 98.06  ? 800  GLU   E CB  1 
ATOM   14932 C  CG  . GLU   E 2 496 ? 47.087  6.955   -36.698 1.00 108.20 ? 800  GLU   E CG  1 
ATOM   14933 C  CD  . GLU   E 2 496 ? 47.895  7.928   -37.544 1.00 115.64 ? 800  GLU   E CD  1 
ATOM   14934 O  OE1 . GLU   E 2 496 ? 48.545  7.453   -38.510 1.00 120.21 ? 800  GLU   E OE1 1 
ATOM   14935 O  OE2 . GLU   E 2 496 ? 47.871  9.155   -37.241 1.00 114.99 ? 800  GLU   E OE2 1 
ATOM   14936 N  N   . VAL   E 2 497 ? 47.422  3.655   -35.028 1.00 97.67  ? 801  VAL   E N   1 
ATOM   14937 C  CA  . VAL   E 2 497 ? 47.847  3.181   -33.711 1.00 96.59  ? 801  VAL   E CA  1 
ATOM   14938 C  C   . VAL   E 2 497 ? 48.861  4.193   -33.171 1.00 93.58  ? 801  VAL   E C   1 
ATOM   14939 O  O   . VAL   E 2 497 ? 50.033  4.217   -33.560 1.00 92.14  ? 801  VAL   E O   1 
ATOM   14940 C  CB  . VAL   E 2 497 ? 48.393  1.747   -33.766 1.00 99.15  ? 801  VAL   E CB  1 
ATOM   14941 C  CG1 . VAL   E 2 497 ? 47.430  0.854   -34.539 1.00 93.58  ? 801  VAL   E CG1 1 
ATOM   14942 C  CG2 . VAL   E 2 497 ? 49.774  1.676   -34.414 1.00 104.13 ? 801  VAL   E CG2 1 
ATOM   14943 N  N   . LEU   E 2 498 ? 48.390  5.061   -32.270 1.00 96.62  ? 802  LEU   E N   1 
ATOM   14944 C  CA  . LEU   E 2 498 ? 49.233  6.128   -31.744 1.00 93.79  ? 802  LEU   E CA  1 
ATOM   14945 C  C   . LEU   E 2 498 ? 50.307  5.561   -30.835 1.00 97.60  ? 802  LEU   E C   1 
ATOM   14946 O  O   . LEU   E 2 498 ? 51.482  5.927   -30.949 1.00 99.82  ? 802  LEU   E O   1 
ATOM   14947 C  CB  . LEU   E 2 498 ? 48.370  7.152   -30.997 1.00 93.06  ? 802  LEU   E CB  1 
ATOM   14948 C  CG  . LEU   E 2 498 ? 47.307  7.878   -31.834 1.00 93.17  ? 802  LEU   E CG  1 
ATOM   14949 C  CD1 . LEU   E 2 498 ? 46.459  8.838   -31.002 1.00 95.89  ? 802  LEU   E CD1 1 
ATOM   14950 C  CD2 . LEU   E 2 498 ? 47.949  8.615   -32.987 1.00 93.06  ? 802  LEU   E CD2 1 
ATOM   14951 N  N   . HIS   E 2 499 ? 49.919  4.655   -29.935 1.00 97.18  ? 803  HIS   E N   1 
ATOM   14952 C  CA  . HIS   E 2 499 ? 50.827  4.018   -28.987 1.00 98.65  ? 803  HIS   E CA  1 
ATOM   14953 C  C   . HIS   E 2 499 ? 50.453  2.547   -28.841 1.00 96.52  ? 803  HIS   E C   1 
ATOM   14954 O  O   . HIS   E 2 499 ? 49.288  2.161   -28.999 1.00 95.33  ? 803  HIS   E O   1 
ATOM   14955 C  CB  . HIS   E 2 499 ? 50.789  4.697   -27.605 1.00 101.61 ? 803  HIS   E CB  1 
ATOM   14956 C  CG  . HIS   E 2 499 ? 51.915  4.286   -26.712 1.00 102.12 ? 803  HIS   E CG  1 
ATOM   14957 N  ND1 . HIS   E 2 499 ? 53.231  4.586   -26.996 1.00 103.44 ? 803  HIS   E ND1 1 
ATOM   14958 C  CD2 . HIS   E 2 499 ? 51.930  3.568   -25.563 1.00 102.95 ? 803  HIS   E CD2 1 
ATOM   14959 C  CE1 . HIS   E 2 499 ? 54.008  4.080   -26.054 1.00 103.61 ? 803  HIS   E CE1 1 
ATOM   14960 N  NE2 . HIS   E 2 499 ? 53.244  3.459   -25.173 1.00 103.03 ? 803  HIS   E NE2 1 
ATOM   14961 N  N   . ALA   E 2 500 ? 51.463  1.727   -28.541 1.00 99.58  ? 804  ALA   E N   1 
ATOM   14962 C  CA  . ALA   E 2 500 ? 51.275  0.304   -28.279 1.00 93.66  ? 804  ALA   E CA  1 
ATOM   14963 C  C   . ALA   E 2 500 ? 52.154  -0.074  -27.095 1.00 93.24  ? 804  ALA   E C   1 
ATOM   14964 O  O   . ALA   E 2 500 ? 53.377  -0.174  -27.237 1.00 91.52  ? 804  ALA   E O   1 
ATOM   14965 C  CB  . ALA   E 2 500 ? 51.624  -0.538  -29.504 1.00 94.74  ? 804  ALA   E CB  1 
ATOM   14966 N  N   . HIS   E 2 501 ? 51.533  -0.290  -25.937 1.00 93.22  ? 805  HIS   E N   1 
ATOM   14967 C  CA  . HIS   E 2 501 ? 52.226  -0.755  -24.741 1.00 97.32  ? 805  HIS   E CA  1 
ATOM   14968 C  C   . HIS   E 2 501 ? 52.087  -2.272  -24.618 1.00 92.84  ? 805  HIS   E C   1 
ATOM   14969 O  O   . HIS   E 2 501 ? 50.969  -2.792  -24.536 1.00 89.21  ? 805  HIS   E O   1 
ATOM   14970 C  CB  . HIS   E 2 501 ? 51.681  -0.079  -23.487 1.00 94.11  ? 805  HIS   E CB  1 
ATOM   14971 C  CG  . HIS   E 2 501 ? 52.245  -0.640  -22.222 1.00 94.22  ? 805  HIS   E CG  1 
ATOM   14972 N  ND1 . HIS   E 2 501 ? 53.430  -0.195  -21.680 1.00 97.39  ? 805  HIS   E ND1 1 
ATOM   14973 C  CD2 . HIS   E 2 501 ? 51.806  -1.633  -21.412 1.00 95.75  ? 805  HIS   E CD2 1 
ATOM   14974 C  CE1 . HIS   E 2 501 ? 53.685  -0.874  -20.576 1.00 101.78 ? 805  HIS   E CE1 1 
ATOM   14975 N  NE2 . HIS   E 2 501 ? 52.717  -1.755  -20.393 1.00 99.71  ? 805  HIS   E NE2 1 
ATOM   14976 N  N   . GLN   E 2 502 ? 53.221  -2.969  -24.599 1.00 92.90  ? 806  GLN   E N   1 
ATOM   14977 C  CA  . GLN   E 2 502 ? 53.261  -4.416  -24.452 1.00 93.82  ? 806  GLN   E CA  1 
ATOM   14978 C  C   . GLN   E 2 502 ? 53.386  -4.789  -22.979 1.00 97.20  ? 806  GLN   E C   1 
ATOM   14979 O  O   . GLN   E 2 502 ? 54.303  -4.329  -22.293 1.00 101.58 ? 806  GLN   E O   1 
ATOM   14980 C  CB  . GLN   E 2 502 ? 54.436  -5.000  -25.234 1.00 92.86  ? 806  GLN   E CB  1 
ATOM   14981 C  CG  . GLN   E 2 502 ? 54.883  -6.366  -24.742 1.00 88.22  ? 806  GLN   E CG  1 
ATOM   14982 C  CD  . GLN   E 2 502 ? 56.089  -6.880  -25.502 1.00 93.22  ? 806  GLN   E CD  1 
ATOM   14983 O  OE1 . GLN   E 2 502 ? 56.201  -6.690  -26.717 1.00 93.03  ? 806  GLN   E OE1 1 
ATOM   14984 N  NE2 . GLN   E 2 502 ? 57.011  -7.528  -24.789 1.00 97.15  ? 806  GLN   E NE2 1 
ATOM   14985 N  N   . PHE   E 2 503 ? 52.487  -5.644  -22.503 1.00 93.74  ? 807  PHE   E N   1 
ATOM   14986 C  CA  . PHE   E 2 503 ? 52.504  -6.028  -21.102 1.00 95.55  ? 807  PHE   E CA  1 
ATOM   14987 C  C   . PHE   E 2 503 ? 53.629  -7.018  -20.824 1.00 92.95  ? 807  PHE   E C   1 
ATOM   14988 O  O   . PHE   E 2 503 ? 54.443  -7.343  -21.697 1.00 89.60  ? 807  PHE   E O   1 
ATOM   14989 C  CB  . PHE   E 2 503 ? 51.165  -6.620  -20.698 1.00 94.16  ? 807  PHE   E CB  1 
ATOM   14990 C  CG  . PHE   E 2 503 ? 50.020  -5.654  -20.746 1.00 88.73  ? 807  PHE   E CG  1 
ATOM   14991 C  CD1 . PHE   E 2 503 ? 49.702  -4.867  -19.642 1.00 87.25  ? 807  PHE   E CD1 1 
ATOM   14992 C  CD2 . PHE   E 2 503 ? 49.231  -5.566  -21.878 1.00 84.48  ? 807  PHE   E CD2 1 
ATOM   14993 C  CE1 . PHE   E 2 503 ? 48.617  -3.997  -19.676 1.00 86.78  ? 807  PHE   E CE1 1 
ATOM   14994 C  CE2 . PHE   E 2 503 ? 48.149  -4.712  -21.924 1.00 88.61  ? 807  PHE   E CE2 1 
ATOM   14995 C  CZ  . PHE   E 2 503 ? 47.838  -3.918  -20.818 1.00 90.49  ? 807  PHE   E CZ  1 
ATOM   14996 N  N   . LEU   E 2 504 ? 53.641  -7.536  -19.595 1.00 93.44  ? 808  LEU   E N   1 
ATOM   14997 C  CA  . LEU   E 2 504 ? 54.698  -8.424  -19.132 1.00 96.48  ? 808  LEU   E CA  1 
ATOM   14998 C  C   . LEU   E 2 504 ? 54.590  -9.794  -19.784 1.00 95.19  ? 808  LEU   E C   1 
ATOM   14999 O  O   . LEU   E 2 504 ? 53.508  -10.246 -20.171 1.00 95.72  ? 808  LEU   E O   1 
ATOM   15000 C  CB  . LEU   E 2 504 ? 54.633  -8.582  -17.616 1.00 95.15  ? 808  LEU   E CB  1 
ATOM   15001 C  CG  . LEU   E 2 504 ? 55.475  -7.618  -16.786 1.00 101.10 ? 808  LEU   E CG  1 
ATOM   15002 C  CD1 . LEU   E 2 504 ? 56.964  -7.892  -16.994 1.00 102.39 ? 808  LEU   E CD1 1 
ATOM   15003 C  CD2 . LEU   E 2 504 ? 55.137  -6.169  -17.126 1.00 104.32 ? 808  LEU   E CD2 1 
ATOM   15004 N  N   . GLN   E 2 505 ? 55.730  -10.464 -19.893 1.00 91.26  ? 809  GLN   E N   1 
ATOM   15005 C  CA  . GLN   E 2 505 ? 55.730  -11.795 -20.474 1.00 99.14  ? 809  GLN   E CA  1 
ATOM   15006 C  C   . GLN   E 2 505 ? 54.817  -12.712 -19.667 1.00 101.16 ? 809  GLN   E C   1 
ATOM   15007 O  O   . GLN   E 2 505 ? 54.771  -12.651 -18.432 1.00 102.51 ? 809  GLN   E O   1 
ATOM   15008 C  CB  . GLN   E 2 505 ? 57.153  -12.347 -20.521 1.00 98.84  ? 809  GLN   E CB  1 
ATOM   15009 N  N   . ASN   E 2 506 ? 54.068  -13.547 -20.376 1.00 101.50 ? 810  ASN   E N   1 
ATOM   15010 C  CA  . ASN   E 2 506 ? 53.107  -14.452 -19.760 1.00 103.03 ? 810  ASN   E CA  1 
ATOM   15011 C  C   . ASN   E 2 506 ? 51.946  -13.708 -19.122 1.00 101.94 ? 810  ASN   E C   1 
ATOM   15012 O  O   . ASN   E 2 506 ? 51.182  -14.288 -18.346 1.00 102.75 ? 810  ASN   E O   1 
ATOM   15013 C  CB  . ASN   E 2 506 ? 53.764  -15.359 -18.711 1.00 105.55 ? 810  ASN   E CB  1 
ATOM   15014 C  CG  . ASN   E 2 506 ? 54.857  -16.212 -19.282 1.00 110.05 ? 810  ASN   E CG  1 
ATOM   15015 O  OD1 . ASN   E 2 506 ? 54.913  -16.467 -20.483 1.00 116.57 ? 810  ASN   E OD1 1 
ATOM   15016 N  ND2 . ASN   E 2 506 ? 55.734  -16.685 -18.408 1.00 115.17 ? 810  ASN   E ND2 1 
ATOM   15017 N  N   . GLU   E 2 507 ? 51.793  -12.421 -19.390 1.00 98.83  ? 811  GLU   E N   1 
ATOM   15018 C  CA  . GLU   E 2 507 ? 50.718  -11.665 -18.774 1.00 96.28  ? 811  GLU   E CA  1 
ATOM   15019 C  C   . GLU   E 2 507 ? 49.528  -11.656 -19.728 1.00 92.16  ? 811  GLU   E C   1 
ATOM   15020 O  O   . GLU   E 2 507 ? 49.660  -11.271 -20.890 1.00 93.32  ? 811  GLU   E O   1 
ATOM   15021 C  CB  . GLU   E 2 507 ? 51.176  -10.255 -18.423 1.00 94.25  ? 811  GLU   E CB  1 
ATOM   15022 C  CG  . GLU   E 2 507 ? 50.088  -9.434  -17.790 1.00 95.88  ? 811  GLU   E CG  1 
ATOM   15023 C  CD  . GLU   E 2 507 ? 50.613  -8.166  -17.137 1.00 98.73  ? 811  GLU   E CD  1 
ATOM   15024 O  OE1 . GLU   E 2 507 ? 51.255  -7.325  -17.827 1.00 97.70  ? 811  GLU   E OE1 1 
ATOM   15025 O  OE2 . GLU   E 2 507 ? 50.363  -8.000  -15.923 1.00 102.42 ? 811  GLU   E OE2 1 
ATOM   15026 N  N   . TYR   E 2 508 ? 48.383  -12.124 -19.249 1.00 88.28  ? 812  TYR   E N   1 
ATOM   15027 C  CA  . TYR   E 2 508 ? 47.158  -12.135 -20.029 1.00 85.81  ? 812  TYR   E CA  1 
ATOM   15028 C  C   . TYR   E 2 508 ? 46.363  -10.909 -19.630 1.00 88.72  ? 812  TYR   E C   1 
ATOM   15029 O  O   . TYR   E 2 508 ? 46.083  -10.716 -18.442 1.00 90.33  ? 812  TYR   E O   1 
ATOM   15030 C  CB  . TYR   E 2 508 ? 46.340  -13.404 -19.782 1.00 89.61  ? 812  TYR   E CB  1 
ATOM   15031 C  CG  . TYR   E 2 508 ? 45.684  -13.907 -21.033 1.00 87.48  ? 812  TYR   E CG  1 
ATOM   15032 C  CD1 . TYR   E 2 508 ? 44.475  -13.372 -21.464 1.00 86.86  ? 812  TYR   E CD1 1 
ATOM   15033 C  CD2 . TYR   E 2 508 ? 46.297  -14.871 -21.824 1.00 87.94  ? 812  TYR   E CD2 1 
ATOM   15034 C  CE1 . TYR   E 2 508 ? 43.871  -13.798 -22.638 1.00 87.25  ? 812  TYR   E CE1 1 
ATOM   15035 C  CE2 . TYR   E 2 508 ? 45.702  -15.307 -23.006 1.00 91.46  ? 812  TYR   E CE2 1 
ATOM   15036 C  CZ  . TYR   E 2 508 ? 44.487  -14.759 -23.408 1.00 92.66  ? 812  TYR   E CZ  1 
ATOM   15037 O  OH  . TYR   E 2 508 ? 43.877  -15.170 -24.575 1.00 102.67 ? 812  TYR   E OH  1 
ATOM   15038 N  N   . ALA   E 2 509 ? 46.008  -10.073 -20.610 1.00 86.99  ? 813  ALA   E N   1 
ATOM   15039 C  CA  . ALA   E 2 509 ? 45.201  -8.883  -20.344 1.00 83.84  ? 813  ALA   E CA  1 
ATOM   15040 C  C   . ALA   E 2 509 ? 43.723  -9.202  -20.574 1.00 80.26  ? 813  ALA   E C   1 
ATOM   15041 O  O   . ALA   E 2 509 ? 43.341  -9.588  -21.681 1.00 84.33  ? 813  ALA   E O   1 
ATOM   15042 C  CB  . ALA   E 2 509 ? 45.660  -7.719  -21.219 1.00 80.39  ? 813  ALA   E CB  1 
ATOM   15043 N  N   . LEU   E 2 510 ? 42.896  -9.026  -19.538 1.00 73.94  ? 814  LEU   E N   1 
ATOM   15044 C  CA  . LEU   E 2 510 ? 41.510  -9.473  -19.575 1.00 76.47  ? 814  LEU   E CA  1 
ATOM   15045 C  C   . LEU   E 2 510 ? 40.490  -8.355  -19.520 1.00 80.88  ? 814  LEU   E C   1 
ATOM   15046 O  O   . LEU   E 2 510 ? 39.450  -8.443  -20.172 1.00 84.68  ? 814  LEU   E O   1 
ATOM   15047 C  CB  . LEU   E 2 510 ? 41.217  -10.424 -18.416 1.00 83.88  ? 814  LEU   E CB  1 
ATOM   15048 C  CG  . LEU   E 2 510 ? 42.219  -11.550 -18.163 1.00 88.04  ? 814  LEU   E CG  1 
ATOM   15049 C  CD1 . LEU   E 2 510 ? 41.774  -12.376 -16.978 1.00 88.44  ? 814  LEU   E CD1 1 
ATOM   15050 C  CD2 . LEU   E 2 510 ? 42.334  -12.422 -19.383 1.00 83.59  ? 814  LEU   E CD2 1 
ATOM   15051 N  N   . SER   E 2 511 ? 40.725  -7.323  -18.730 1.00 82.24  ? 815  SER   E N   1 
ATOM   15052 C  CA  . SER   E 2 511 ? 39.720  -6.293  -18.531 1.00 80.50  ? 815  SER   E CA  1 
ATOM   15053 C  C   . SER   E 2 511 ? 40.273  -4.953  -18.971 1.00 81.17  ? 815  SER   E C   1 
ATOM   15054 O  O   . SER   E 2 511 ? 41.483  -4.722  -18.928 1.00 83.02  ? 815  SER   E O   1 
ATOM   15055 C  CB  . SER   E 2 511 ? 39.291  -6.238  -17.073 1.00 84.13  ? 815  SER   E CB  1 
ATOM   15056 O  OG  . SER   E 2 511 ? 40.390  -5.857  -16.271 1.00 85.61  ? 815  SER   E OG  1 
ATOM   15057 N  N   . LEU   E 2 512 ? 39.376  -4.067  -19.398 1.00 84.88  ? 816  LEU   E N   1 
ATOM   15058 C  CA  . LEU   E 2 512 ? 39.771  -2.722  -19.806 1.00 82.12  ? 816  LEU   E CA  1 
ATOM   15059 C  C   . LEU   E 2 512 ? 38.676  -1.728  -19.451 1.00 78.42  ? 816  LEU   E C   1 
ATOM   15060 O  O   . LEU   E 2 512 ? 37.489  -1.984  -19.663 1.00 84.11  ? 816  LEU   E O   1 
ATOM   15061 C  CB  . LEU   E 2 512 ? 40.074  -2.682  -21.307 1.00 78.37  ? 816  LEU   E CB  1 
ATOM   15062 C  CG  . LEU   E 2 512 ? 40.662  -1.445  -21.956 1.00 80.63  ? 816  LEU   E CG  1 
ATOM   15063 C  CD1 . LEU   E 2 512 ? 42.005  -1.077  -21.333 1.00 79.39  ? 816  LEU   E CD1 1 
ATOM   15064 C  CD2 . LEU   E 2 512 ? 40.809  -1.766  -23.435 1.00 80.82  ? 816  LEU   E CD2 1 
ATOM   15065 N  N   . VAL   E 2 513 ? 39.072  -0.604  -18.885 1.00 84.22  ? 817  VAL   E N   1 
ATOM   15066 C  CA  . VAL   E 2 513 ? 38.114  0.434   -18.533 1.00 92.53  ? 817  VAL   E CA  1 
ATOM   15067 C  C   . VAL   E 2 513 ? 38.808  1.779   -18.660 1.00 89.88  ? 817  VAL   E C   1 
ATOM   15068 O  O   . VAL   E 2 513 ? 40.001  1.920   -18.369 1.00 87.07  ? 817  VAL   E O   1 
ATOM   15069 C  CB  . VAL   E 2 513 ? 37.511  0.240   -17.113 1.00 83.51  ? 817  VAL   E CB  1 
ATOM   15070 C  CG1 . VAL   E 2 513 ? 38.526  0.569   -16.044 1.00 82.28  ? 817  VAL   E CG1 1 
ATOM   15071 C  CG2 . VAL   E 2 513 ? 36.289  1.116   -16.946 1.00 82.12  ? 817  VAL   E CG2 1 
ATOM   15072 N  N   . SER   E 2 514 ? 38.058  2.756   -19.149 1.00 89.65  ? 818  SER   E N   1 
ATOM   15073 C  CA  . SER   E 2 514 ? 38.459  4.148   -19.102 1.00 92.92  ? 818  SER   E CA  1 
ATOM   15074 C  C   . SER   E 2 514 ? 37.534  4.859   -18.127 1.00 91.50  ? 818  SER   E C   1 
ATOM   15075 O  O   . SER   E 2 514 ? 36.310  4.702   -18.200 1.00 90.96  ? 818  SER   E O   1 
ATOM   15076 C  CB  . SER   E 2 514 ? 38.394  4.789   -20.487 1.00 92.09  ? 818  SER   E CB  1 
ATOM   15077 O  OG  . SER   E 2 514 ? 38.297  6.203   -20.397 1.00 92.77  ? 818  SER   E OG  1 
ATOM   15078 N  N   . CYS   E 2 515 ? 38.114  5.600   -17.192 1.00 92.59  ? 819  CYS   E N   1 
ATOM   15079 C  CA  . CYS   E 2 515 ? 37.299  6.452   -16.332 1.00 102.30 ? 819  CYS   E CA  1 
ATOM   15080 C  C   . CYS   E 2 515 ? 38.205  7.394   -15.545 1.00 99.78  ? 819  CYS   E C   1 
ATOM   15081 O  O   . CYS   E 2 515 ? 39.433  7.396   -15.691 1.00 99.56  ? 819  CYS   E O   1 
ATOM   15082 C  CB  . CYS   E 2 515 ? 36.435  5.611   -15.392 1.00 101.54 ? 819  CYS   E CB  1 
ATOM   15083 S  SG  . CYS   E 2 515 ? 37.463  4.530   -14.404 1.00 88.09  ? 819  CYS   E SG  1 
ATOM   15084 N  N   . LYS   E 2 516 ? 37.564  8.212   -14.720 1.00 99.81  ? 820  LYS   E N   1 
ATOM   15085 C  CA  . LYS   E 2 516 ? 38.218  9.051   -13.728 1.00 105.94 ? 820  LYS   E CA  1 
ATOM   15086 C  C   . LYS   E 2 516 ? 37.722  8.591   -12.358 1.00 106.49 ? 820  LYS   E C   1 
ATOM   15087 O  O   . LYS   E 2 516 ? 36.515  8.407   -12.167 1.00 108.45 ? 820  LYS   E O   1 
ATOM   15088 C  CB  . LYS   E 2 516 ? 37.907  10.544  -13.984 1.00 97.11  ? 820  LYS   E CB  1 
ATOM   15089 N  N   . LEU   E 2 517 ? 38.646  8.377   -11.414 1.00 109.91 ? 821  LEU   E N   1 
ATOM   15090 C  CA  . LEU   E 2 517 ? 38.317  7.898   -10.070 1.00 108.72 ? 821  LEU   E CA  1 
ATOM   15091 C  C   . LEU   E 2 517 ? 38.685  8.937   -9.013  1.00 107.57 ? 821  LEU   E C   1 
ATOM   15092 O  O   . LEU   E 2 517 ? 39.601  9.741   -9.204  1.00 109.82 ? 821  LEU   E O   1 
ATOM   15093 C  CB  . LEU   E 2 517 ? 39.043  6.583   -9.736  1.00 104.84 ? 821  LEU   E CB  1 
ATOM   15094 C  CG  . LEU   E 2 517 ? 38.791  5.417   -10.677 1.00 100.90 ? 821  LEU   E CG  1 
ATOM   15095 C  CD1 . LEU   E 2 517 ? 37.342  5.450   -11.097 1.00 105.75 ? 821  LEU   E CD1 1 
ATOM   15096 C  CD2 . LEU   E 2 517 ? 39.701  5.484   -11.876 1.00 100.51 ? 821  LEU   E CD2 1 
ATOM   15097 N  N   . GLY   E 2 518 ? 37.980  8.904   -7.880  1.00 106.98 ? 822  GLY   E N   1 
ATOM   15098 C  CA  . GLY   E 2 518 ? 38.265  9.868   -6.821  1.00 108.98 ? 822  GLY   E CA  1 
ATOM   15099 C  C   . GLY   E 2 518 ? 38.070  11.311  -7.268  1.00 110.01 ? 822  GLY   E C   1 
ATOM   15100 O  O   . GLY   E 2 518 ? 37.503  11.612  -8.317  1.00 111.46 ? 822  GLY   E O   1 
ATOM   15101 N  N   . LYS   E 2 519 ? 38.557  12.220  -6.424  1.00 109.95 ? 823  LYS   E N   1 
ATOM   15102 C  CA  . LYS   E 2 519 ? 38.534  13.636  -6.783  1.00 105.17 ? 823  LYS   E CA  1 
ATOM   15103 C  C   . LYS   E 2 519 ? 39.592  13.984  -7.844  1.00 108.47 ? 823  LYS   E C   1 
ATOM   15104 O  O   . LYS   E 2 519 ? 39.660  15.139  -8.286  1.00 106.84 ? 823  LYS   E O   1 
ATOM   15105 C  CB  . LYS   E 2 519 ? 38.713  14.492  -5.517  1.00 90.39  ? 823  LYS   E CB  1 
ATOM   15106 N  N   . ASP   E 2 520 ? 40.400  13.014  -8.269  1.00 109.27 ? 824  ASP   E N   1 
ATOM   15107 C  CA  . ASP   E 2 520 ? 41.303  13.223  -9.395  1.00 107.00 ? 824  ASP   E CA  1 
ATOM   15108 C  C   . ASP   E 2 520 ? 40.502  13.606  -10.639 1.00 107.89 ? 824  ASP   E C   1 
ATOM   15109 O  O   . ASP   E 2 520 ? 39.380  13.125  -10.826 1.00 108.84 ? 824  ASP   E O   1 
ATOM   15110 C  CB  . ASP   E 2 520 ? 42.095  11.944  -9.651  1.00 104.18 ? 824  ASP   E CB  1 
ATOM   15111 C  CG  . ASP   E 2 520 ? 43.295  12.173  -10.514 1.00 103.18 ? 824  ASP   E CG  1 
ATOM   15112 O  OD1 . ASP   E 2 520 ? 43.200  12.953  -11.485 1.00 105.77 ? 824  ASP   E OD1 1 
ATOM   15113 O  OD2 . ASP   E 2 520 ? 44.338  11.556  -10.216 1.00 99.86  ? 824  ASP   E OD2 1 
ATOM   15114 N  N   . PRO   E 2 521 ? 41.030  14.478  -11.503 1.00 108.48 ? 825  PRO   E N   1 
ATOM   15115 C  CA  . PRO   E 2 521 ? 40.247  14.915  -12.665 1.00 106.65 ? 825  PRO   E CA  1 
ATOM   15116 C  C   . PRO   E 2 521 ? 40.612  14.229  -13.968 1.00 109.66 ? 825  PRO   E C   1 
ATOM   15117 O  O   . PRO   E 2 521 ? 39.796  14.230  -14.895 1.00 114.20 ? 825  PRO   E O   1 
ATOM   15118 C  CB  . PRO   E 2 521 ? 40.570  16.408  -12.749 1.00 107.21 ? 825  PRO   E CB  1 
ATOM   15119 C  CG  . PRO   E 2 521 ? 42.019  16.437  -12.365 1.00 110.12 ? 825  PRO   E CG  1 
ATOM   15120 C  CD  . PRO   E 2 521 ? 42.180  15.374  -11.274 1.00 110.37 ? 825  PRO   E CD  1 
ATOM   15121 N  N   . ASN   E 2 522 ? 41.818  13.673  -14.077 1.00 106.20 ? 826  ASN   E N   1 
ATOM   15122 C  CA  . ASN   E 2 522 ? 42.222  13.106  -15.359 1.00 111.55 ? 826  ASN   E CA  1 
ATOM   15123 C  C   . ASN   E 2 522 ? 41.463  11.797  -15.623 1.00 107.43 ? 826  ASN   E C   1 
ATOM   15124 O  O   . ASN   E 2 522 ? 40.808  11.230  -14.739 1.00 105.31 ? 826  ASN   E O   1 
ATOM   15125 C  CB  . ASN   E 2 522 ? 43.746  12.887  -15.431 1.00 106.27 ? 826  ASN   E CB  1 
ATOM   15126 C  CG  . ASN   E 2 522 ? 44.559  14.192  -15.529 1.00 105.12 ? 826  ASN   E CG  1 
ATOM   15127 O  OD1 . ASN   E 2 522 ? 44.032  15.221  -15.963 1.00 105.28 ? 826  ASN   E OD1 1 
ATOM   15128 N  ND2 . ASN   E 2 522 ? 45.815  14.167  -15.083 1.00 108.17 ? 826  ASN   E ND2 1 
ATOM   15129 N  N   . THR   E 2 523 ? 41.527  11.326  -16.864 1.00 103.11 ? 827  THR   E N   1 
ATOM   15130 C  CA  . THR   E 2 523 ? 40.940  10.038  -17.202 1.00 101.68 ? 827  THR   E CA  1 
ATOM   15131 C  C   . THR   E 2 523 ? 42.049  9.036   -17.496 1.00 101.65 ? 827  THR   E C   1 
ATOM   15132 O  O   . THR   E 2 523 ? 43.052  9.367   -18.143 1.00 100.83 ? 827  THR   E O   1 
ATOM   15133 C  CB  . THR   E 2 523 ? 39.990  10.137  -18.394 1.00 97.79  ? 827  THR   E CB  1 
ATOM   15134 O  OG1 . THR   E 2 523 ? 39.346  11.417  -18.387 1.00 104.39 ? 827  THR   E OG1 1 
ATOM   15135 C  CG2 . THR   E 2 523 ? 38.927  9.087   -18.262 1.00 99.87  ? 827  THR   E CG2 1 
ATOM   15136 N  N   . TYR   E 2 524 ? 41.881  7.820   -16.994 1.00 98.29  ? 828  TYR   E N   1 
ATOM   15137 C  CA  . TYR   E 2 524 ? 42.908  6.800   -17.113 1.00 95.69  ? 828  TYR   E CA  1 
ATOM   15138 C  C   . TYR   E 2 524 ? 42.359  5.580   -17.840 1.00 97.31  ? 828  TYR   E C   1 
ATOM   15139 O  O   . TYR   E 2 524 ? 41.156  5.290   -17.786 1.00 97.58  ? 828  TYR   E O   1 
ATOM   15140 C  CB  . TYR   E 2 524 ? 43.420  6.383   -15.741 1.00 94.18  ? 828  TYR   E CB  1 
ATOM   15141 C  CG  . TYR   E 2 524 ? 43.793  7.526   -14.833 1.00 100.80 ? 828  TYR   E CG  1 
ATOM   15142 C  CD1 . TYR   E 2 524 ? 42.813  8.293   -14.200 1.00 101.94 ? 828  TYR   E CD1 1 
ATOM   15143 C  CD2 . TYR   E 2 524 ? 45.138  7.835   -14.592 1.00 103.93 ? 828  TYR   E CD2 1 
ATOM   15144 C  CE1 . TYR   E 2 524 ? 43.162  9.344   -13.347 1.00 103.58 ? 828  TYR   E CE1 1 
ATOM   15145 C  CE2 . TYR   E 2 524 ? 45.501  8.874   -13.746 1.00 103.95 ? 828  TYR   E CE2 1 
ATOM   15146 C  CZ  . TYR   E 2 524 ? 44.512  9.623   -13.126 1.00 105.86 ? 828  TYR   E CZ  1 
ATOM   15147 O  OH  . TYR   E 2 524 ? 44.883  10.651  -12.288 1.00 109.17 ? 828  TYR   E OH  1 
ATOM   15148 N  N   . PHE   E 2 525 ? 43.251  4.871   -18.528 1.00 94.60  ? 829  PHE   E N   1 
ATOM   15149 C  CA  . PHE   E 2 525 ? 42.969  3.524   -19.014 1.00 88.58  ? 829  PHE   E CA  1 
ATOM   15150 C  C   . PHE   E 2 525 ? 43.411  2.557   -17.928 1.00 87.46  ? 829  PHE   E C   1 
ATOM   15151 O  O   . PHE   E 2 525 ? 44.613  2.419   -17.684 1.00 88.03  ? 829  PHE   E O   1 
ATOM   15152 C  CB  . PHE   E 2 525 ? 43.718  3.225   -20.310 1.00 86.05  ? 829  PHE   E CB  1 
ATOM   15153 C  CG  . PHE   E 2 525 ? 43.174  3.933   -21.520 1.00 89.46  ? 829  PHE   E CG  1 
ATOM   15154 C  CD1 . PHE   E 2 525 ? 41.845  3.784   -21.893 1.00 93.44  ? 829  PHE   E CD1 1 
ATOM   15155 C  CD2 . PHE   E 2 525 ? 43.998  4.722   -22.305 1.00 86.39  ? 829  PHE   E CD2 1 
ATOM   15156 C  CE1 . PHE   E 2 525 ? 41.347  4.432   -23.022 1.00 90.98  ? 829  PHE   E CE1 1 
ATOM   15157 C  CE2 . PHE   E 2 525 ? 43.509  5.369   -23.421 1.00 85.99  ? 829  PHE   E CE2 1 
ATOM   15158 C  CZ  . PHE   E 2 525 ? 42.185  5.227   -23.784 1.00 84.71  ? 829  PHE   E CZ  1 
ATOM   15159 N  N   . ILE   E 2 526 ? 42.457  1.887   -17.274 1.00 84.27  ? 830  ILE   E N   1 
ATOM   15160 C  CA  . ILE   E 2 526 ? 42.765  0.855   -16.272 1.00 88.65  ? 830  ILE   E CA  1 
ATOM   15161 C  C   . ILE   E 2 526 ? 42.683  -0.542  -16.913 1.00 85.44  ? 830  ILE   E C   1 
ATOM   15162 O  O   . ILE   E 2 526 ? 41.700  -0.879  -17.589 1.00 84.64  ? 830  ILE   E O   1 
ATOM   15163 C  CB  . ILE   E 2 526 ? 41.829  0.968   -15.053 1.00 86.38  ? 830  ILE   E CB  1 
ATOM   15164 C  CG1 . ILE   E 2 526 ? 41.737  2.426   -14.597 1.00 89.00  ? 830  ILE   E CG1 1 
ATOM   15165 C  CG2 . ILE   E 2 526 ? 42.319  0.076   -13.896 1.00 84.17  ? 830  ILE   E CG2 1 
ATOM   15166 C  CD1 . ILE   E 2 526 ? 40.362  2.802   -14.020 1.00 88.14  ? 830  ILE   E CD1 1 
ATOM   15167 N  N   . VAL   E 2 527 ? 43.706  -1.361  -16.699 1.00 81.19  ? 831  VAL   E N   1 
ATOM   15168 C  CA  . VAL   E 2 527 ? 43.785  -2.663  -17.330 1.00 84.53  ? 831  VAL   E CA  1 
ATOM   15169 C  C   . VAL   E 2 527 ? 43.862  -3.735  -16.243 1.00 86.82  ? 831  VAL   E C   1 
ATOM   15170 O  O   . VAL   E 2 527 ? 44.627  -3.610  -15.277 1.00 83.96  ? 831  VAL   E O   1 
ATOM   15171 C  CB  . VAL   E 2 527 ? 44.986  -2.724  -18.290 1.00 88.69  ? 831  VAL   E CB  1 
ATOM   15172 C  CG1 . VAL   E 2 527 ? 45.299  -4.168  -18.668 1.00 88.21  ? 831  VAL   E CG1 1 
ATOM   15173 C  CG2 . VAL   E 2 527 ? 44.705  -1.892  -19.546 1.00 86.13  ? 831  VAL   E CG2 1 
ATOM   15174 N  N   . GLY   E 2 528 ? 43.043  -4.772  -16.384 1.00 88.56  ? 832  GLY   E N   1 
ATOM   15175 C  CA  . GLY   E 2 528 ? 43.125  -5.959  -15.534 1.00 92.06  ? 832  GLY   E CA  1 
ATOM   15176 C  C   . GLY   E 2 528 ? 43.810  -7.104  -16.264 1.00 87.02  ? 832  GLY   E C   1 
ATOM   15177 O  O   . GLY   E 2 528 ? 43.559  -7.338  -17.450 1.00 85.19  ? 832  GLY   E O   1 
ATOM   15178 N  N   . THR   E 2 529 ? 44.675  -7.815  -15.555 1.00 87.65  ? 833  THR   E N   1 
ATOM   15179 C  CA  . THR   E 2 529 ? 45.501  -8.847  -16.171 1.00 88.82  ? 833  THR   E CA  1 
ATOM   15180 C  C   . THR   E 2 529 ? 45.539  -10.100 -15.307 1.00 91.65  ? 833  THR   E C   1 
ATOM   15181 O  O   . THR   E 2 529 ? 45.021  -10.144 -14.184 1.00 91.62  ? 833  THR   E O   1 
ATOM   15182 C  CB  . THR   E 2 529 ? 46.933  -8.365  -16.386 1.00 90.32  ? 833  THR   E CB  1 
ATOM   15183 O  OG1 . THR   E 2 529 ? 47.528  -8.100  -15.107 1.00 93.95  ? 833  THR   E OG1 1 
ATOM   15184 C  CG2 . THR   E 2 529 ? 46.924  -7.112  -17.197 1.00 91.59  ? 833  THR   E CG2 1 
ATOM   15185 N  N   . ALA   E 2 530 ? 46.180  -11.130 -15.852 1.00 95.06  ? 834  ALA   E N   1 
ATOM   15186 C  CA  . ALA   E 2 530 ? 46.465  -12.344 -15.106 1.00 92.11  ? 834  ALA   E CA  1 
ATOM   15187 C  C   . ALA   E 2 530 ? 47.781  -12.898 -15.617 1.00 89.73  ? 834  ALA   E C   1 
ATOM   15188 O  O   . ALA   E 2 530 ? 48.061  -12.833 -16.818 1.00 87.08  ? 834  ALA   E O   1 
ATOM   15189 C  CB  . ALA   E 2 530 ? 45.341  -13.371 -15.246 1.00 89.13  ? 834  ALA   E CB  1 
ATOM   15190 N  N   . MET   E 2 531 ? 48.603  -13.389 -14.694 1.00 90.30  ? 835  MET   E N   1 
ATOM   15191 C  CA  . MET   E 2 531 ? 49.826  -14.093 -15.050 1.00 95.81  ? 835  MET   E CA  1 
ATOM   15192 C  C   . MET   E 2 531 ? 49.452  -15.545 -15.284 1.00 94.25  ? 835  MET   E C   1 
ATOM   15193 O  O   . MET   E 2 531 ? 48.660  -16.102 -14.520 1.00 96.29  ? 835  MET   E O   1 
ATOM   15194 C  CB  . MET   E 2 531 ? 50.883  -13.975 -13.948 1.00 98.52  ? 835  MET   E CB  1 
ATOM   15195 C  CG  . MET   E 2 531 ? 51.384  -12.550 -13.721 1.00 103.92 ? 835  MET   E CG  1 
ATOM   15196 S  SD  . MET   E 2 531 ? 51.927  -11.746 -15.257 1.00 101.82 ? 835  MET   E SD  1 
ATOM   15197 C  CE  . MET   E 2 531 ? 53.524  -12.510 -15.536 1.00 99.00  ? 835  MET   E CE  1 
ATOM   15198 N  N   . VAL   E 2 532 ? 49.974  -16.146 -16.351 1.00 91.56  ? 836  VAL   E N   1 
ATOM   15199 C  CA  . VAL   E 2 532 ? 49.528  -17.482 -16.725 1.00 96.11  ? 836  VAL   E CA  1 
ATOM   15200 C  C   . VAL   E 2 532 ? 50.722  -18.330 -17.144 1.00 104.24 ? 836  VAL   E C   1 
ATOM   15201 O  O   . VAL   E 2 532 ? 51.573  -17.880 -17.922 1.00 102.32 ? 836  VAL   E O   1 
ATOM   15202 C  CB  . VAL   E 2 532 ? 48.471  -17.438 -17.843 1.00 95.19  ? 836  VAL   E CB  1 
ATOM   15203 C  CG1 . VAL   E 2 532 ? 47.449  -16.321 -17.565 1.00 90.72  ? 836  VAL   E CG1 1 
ATOM   15204 C  CG2 . VAL   E 2 532 ? 49.125  -17.267 -19.192 1.00 97.84  ? 836  VAL   E CG2 1 
ATOM   15205 N  N   . TYR   E 2 533 ? 50.781  -19.566 -16.631 1.00 103.07 ? 837  TYR   E N   1 
ATOM   15206 C  CA  . TYR   E 2 533 ? 51.875  -20.493 -16.921 1.00 102.47 ? 837  TYR   E CA  1 
ATOM   15207 C  C   . TYR   E 2 533 ? 51.303  -21.890 -17.132 1.00 103.42 ? 837  TYR   E C   1 
ATOM   15208 O  O   . TYR   E 2 533 ? 50.444  -22.329 -16.349 1.00 106.87 ? 837  TYR   E O   1 
ATOM   15209 C  CB  . TYR   E 2 533 ? 52.918  -20.521 -15.794 1.00 106.20 ? 837  TYR   E CB  1 
ATOM   15210 C  CG  . TYR   E 2 533 ? 53.326  -19.160 -15.281 1.00 102.09 ? 837  TYR   E CG  1 
ATOM   15211 C  CD1 . TYR   E 2 533 ? 54.102  -18.306 -16.059 1.00 103.84 ? 837  TYR   E CD1 1 
ATOM   15212 C  CD2 . TYR   E 2 533 ? 52.957  -18.744 -14.017 1.00 101.48 ? 837  TYR   E CD2 1 
ATOM   15213 C  CE1 . TYR   E 2 533 ? 54.486  -17.065 -15.579 1.00 108.60 ? 837  TYR   E CE1 1 
ATOM   15214 C  CE2 . TYR   E 2 533 ? 53.331  -17.512 -13.530 1.00 104.63 ? 837  TYR   E CE2 1 
ATOM   15215 C  CZ  . TYR   E 2 533 ? 54.093  -16.671 -14.311 1.00 108.66 ? 837  TYR   E CZ  1 
ATOM   15216 O  OH  . TYR   E 2 533 ? 54.459  -15.437 -13.810 1.00 107.09 ? 837  TYR   E OH  1 
ATOM   15217 N  N   . PRO   E 2 534 ? 51.790  -22.624 -18.139 1.00 104.53 ? 838  PRO   E N   1 
ATOM   15218 C  CA  . PRO   E 2 534 ? 51.161  -23.914 -18.471 1.00 106.95 ? 838  PRO   E CA  1 
ATOM   15219 C  C   . PRO   E 2 534 ? 51.005  -24.803 -17.258 1.00 108.61 ? 838  PRO   E C   1 
ATOM   15220 O  O   . PRO   E 2 534 ? 49.949  -25.413 -17.043 1.00 107.16 ? 838  PRO   E O   1 
ATOM   15221 C  CB  . PRO   E 2 534 ? 52.142  -24.522 -19.484 1.00 108.10 ? 838  PRO   E CB  1 
ATOM   15222 C  CG  . PRO   E 2 534 ? 52.824  -23.352 -20.073 1.00 107.38 ? 838  PRO   E CG  1 
ATOM   15223 C  CD  . PRO   E 2 534 ? 53.001  -22.385 -18.940 1.00 103.84 ? 838  PRO   E CD  1 
ATOM   15224 N  N   . GLU   E 2 535 ? 52.061  -24.850 -16.442 1.00 106.02 ? 839  GLU   E N   1 
ATOM   15225 C  CA  . GLU   E 2 535 ? 52.053  -25.668 -15.240 1.00 105.91 ? 839  GLU   E CA  1 
ATOM   15226 C  C   . GLU   E 2 535 ? 50.880  -25.303 -14.329 1.00 103.63 ? 839  GLU   E C   1 
ATOM   15227 O  O   . GLU   E 2 535 ? 50.090  -26.175 -13.949 1.00 104.23 ? 839  GLU   E O   1 
ATOM   15228 C  CB  . GLU   E 2 535 ? 53.396  -25.523 -14.522 1.00 107.76 ? 839  GLU   E CB  1 
ATOM   15229 N  N   . GLU   E 2 536 ? 50.728  -24.014 -13.999 1.00 100.67 ? 840  GLU   E N   1 
ATOM   15230 C  CA  . GLU   E 2 536 ? 49.719  -23.581 -13.031 1.00 98.06  ? 840  GLU   E CA  1 
ATOM   15231 C  C   . GLU   E 2 536 ? 48.350  -23.514 -13.703 1.00 93.69  ? 840  GLU   E C   1 
ATOM   15232 O  O   . GLU   E 2 536 ? 48.191  -22.854 -14.734 1.00 95.89  ? 840  GLU   E O   1 
ATOM   15233 C  CB  . GLU   E 2 536 ? 50.094  -22.228 -12.423 1.00 95.00  ? 840  GLU   E CB  1 
ATOM   15234 N  N   . ALA   E 2 537 ? 47.358  -24.187 -13.113 1.00 93.91  ? 841  ALA   E N   1 
ATOM   15235 C  CA  . ALA   E 2 537 ? 46.077  -24.358 -13.788 1.00 83.20  ? 841  ALA   E CA  1 
ATOM   15236 C  C   . ALA   E 2 537 ? 45.166  -23.163 -13.571 1.00 83.65  ? 841  ALA   E C   1 
ATOM   15237 O  O   . ALA   E 2 537 ? 44.622  -22.610 -14.530 1.00 84.44  ? 841  ALA   E O   1 
ATOM   15238 C  CB  . ALA   E 2 537 ? 45.404  -25.639 -13.315 1.00 88.10  ? 841  ALA   E CB  1 
ATOM   15239 N  N   . GLU   E 2 538 ? 44.982  -22.763 -12.330 1.00 90.67  ? 842  GLU   E N   1 
ATOM   15240 C  CA  . GLU   E 2 538 ? 44.242  -21.589 -11.897 1.00 91.13  ? 842  GLU   E CA  1 
ATOM   15241 C  C   . GLU   E 2 538 ? 45.160  -20.388 -11.750 1.00 92.27  ? 842  GLU   E C   1 
ATOM   15242 O  O   . GLU   E 2 538 ? 46.324  -20.526 -11.362 1.00 93.81  ? 842  GLU   E O   1 
ATOM   15243 C  CB  . GLU   E 2 538 ? 43.567  -21.838 -10.557 1.00 93.51  ? 842  GLU   E CB  1 
ATOM   15244 C  CG  . GLU   E 2 538 ? 42.094  -22.198 -10.640 1.00 102.45 ? 842  GLU   E CG  1 
ATOM   15245 C  CD  . GLU   E 2 538 ? 41.732  -23.309 -9.659  1.00 117.84 ? 842  GLU   E CD  1 
ATOM   15246 O  OE1 . GLU   E 2 538 ? 42.267  -23.284 -8.522  1.00 114.29 ? 842  GLU   E OE1 1 
ATOM   15247 O  OE2 . GLU   E 2 538 ? 40.937  -24.221 -10.036 1.00 121.20 ? 842  GLU   E OE2 1 
ATOM   15248 N  N   . PRO   E 2 539 ? 44.612  -19.201 -12.015 1.00 97.65  ? 843  PRO   E N   1 
ATOM   15249 C  CA  . PRO   E 2 539 ? 45.397  -17.958 -11.952 1.00 94.61  ? 843  PRO   E CA  1 
ATOM   15250 C  C   . PRO   E 2 539 ? 45.561  -17.502 -10.510 1.00 95.18  ? 843  PRO   E C   1 
ATOM   15251 O  O   . PRO   E 2 539 ? 44.596  -17.099 -9.851  1.00 91.08  ? 843  PRO   E O   1 
ATOM   15252 C  CB  . PRO   E 2 539 ? 44.552  -16.964 -12.761 1.00 89.19  ? 843  PRO   E CB  1 
ATOM   15253 C  CG  . PRO   E 2 539 ? 43.370  -17.756 -13.292 1.00 88.07  ? 843  PRO   E CG  1 
ATOM   15254 C  CD  . PRO   E 2 539 ? 43.216  -18.940 -12.398 1.00 92.63  ? 843  PRO   E CD  1 
ATOM   15255 N  N   . LYS   E 2 540 ? 46.797  -17.542 -10.026 1.00 98.72  ? 844  LYS   E N   1 
ATOM   15256 C  CA  . LYS   E 2 540 ? 47.050  -17.158 -8.650  1.00 102.14 ? 844  LYS   E CA  1 
ATOM   15257 C  C   . LYS   E 2 540 ? 47.629  -15.748 -8.497  1.00 99.39  ? 844  LYS   E C   1 
ATOM   15258 O  O   . LYS   E 2 540 ? 47.720  -15.258 -7.369  1.00 98.62  ? 844  LYS   E O   1 
ATOM   15259 C  CB  . LYS   E 2 540 ? 47.953  -18.206 -7.984  1.00 102.91 ? 844  LYS   E CB  1 
ATOM   15260 C  CG  . LYS   E 2 540 ? 47.163  -19.156 -7.102  1.00 103.42 ? 844  LYS   E CG  1 
ATOM   15261 C  CD  . LYS   E 2 540 ? 46.520  -18.362 -5.955  1.00 113.39 ? 844  LYS   E CD  1 
ATOM   15262 C  CE  . LYS   E 2 540 ? 45.986  -19.288 -4.861  1.00 119.04 ? 844  LYS   E CE  1 
ATOM   15263 N  NZ  . LYS   E 2 540 ? 45.974  -18.673 -3.490  1.00 102.02 ? 844  LYS   E NZ  1 
ATOM   15264 N  N   . GLN   E 2 541 ? 47.969  -15.055 -9.580  1.00 101.35 ? 845  GLN   E N   1 
ATOM   15265 C  CA  . GLN   E 2 541 ? 48.442  -13.690 -9.403  1.00 99.60  ? 845  GLN   E CA  1 
ATOM   15266 C  C   . GLN   E 2 541 ? 48.320  -12.917 -10.711 1.00 95.20  ? 845  GLN   E C   1 
ATOM   15267 O  O   . GLN   E 2 541 ? 48.799  -13.373 -11.749 1.00 95.70  ? 845  GLN   E O   1 
ATOM   15268 C  CB  . GLN   E 2 541 ? 49.885  -13.692 -8.925  1.00 102.53 ? 845  GLN   E CB  1 
ATOM   15269 C  CG  . GLN   E 2 541 ? 50.836  -14.110 -10.009 1.00 106.82 ? 845  GLN   E CG  1 
ATOM   15270 C  CD  . GLN   E 2 541 ? 52.269  -14.013 -9.581  1.00 116.50 ? 845  GLN   E CD  1 
ATOM   15271 O  OE1 . GLN   E 2 541 ? 52.563  -13.572 -8.467  1.00 121.35 ? 845  GLN   E OE1 1 
ATOM   15272 N  NE2 . GLN   E 2 541 ? 53.182  -14.418 -10.464 1.00 119.06 ? 845  GLN   E NE2 1 
ATOM   15273 N  N   . GLY   E 2 542 ? 47.700  -11.742 -10.653 1.00 95.52  ? 846  GLY   E N   1 
ATOM   15274 C  CA  . GLY   E 2 542 ? 47.655  -10.819 -11.778 1.00 95.54  ? 846  GLY   E CA  1 
ATOM   15275 C  C   . GLY   E 2 542 ? 47.801  -9.391  -11.263 1.00 96.33  ? 846  GLY   E C   1 
ATOM   15276 O  O   . GLY   E 2 542 ? 48.065  -9.212  -10.077 1.00 97.34  ? 846  GLY   E O   1 
ATOM   15277 N  N   . ARG   E 2 543 ? 47.640  -8.377  -12.104 1.00 97.16  ? 847  ARG   E N   1 
ATOM   15278 C  CA  . ARG   E 2 543 ? 47.765  -7.007  -11.608 1.00 92.34  ? 847  ARG   E CA  1 
ATOM   15279 C  C   . ARG   E 2 543 ? 46.684  -6.121  -12.210 1.00 90.98  ? 847  ARG   E C   1 
ATOM   15280 O  O   . ARG   E 2 543 ? 46.131  -6.405  -13.274 1.00 91.16  ? 847  ARG   E O   1 
ATOM   15281 C  CB  . ARG   E 2 543 ? 49.173  -6.420  -11.879 1.00 92.53  ? 847  ARG   E CB  1 
ATOM   15282 C  CG  . ARG   E 2 543 ? 50.367  -7.020  -11.117 1.00 91.78  ? 847  ARG   E CG  1 
ATOM   15283 C  CD  . ARG   E 2 543 ? 51.702  -6.305  -11.482 1.00 94.67  ? 847  ARG   E CD  1 
ATOM   15284 N  NE  . ARG   E 2 543 ? 52.098  -6.492  -12.879 1.00 100.51 ? 847  ARG   E NE  1 
ATOM   15285 C  CZ  . ARG   E 2 543 ? 51.968  -5.586  -13.846 1.00 101.34 ? 847  ARG   E CZ  1 
ATOM   15286 N  NH1 . ARG   E 2 543 ? 51.342  -4.434  -13.639 1.00 99.90  ? 847  ARG   E NH1 1 
ATOM   15287 N  NH2 . ARG   E 2 543 ? 52.485  -5.839  -15.052 1.00 95.31  ? 847  ARG   E NH2 1 
ATOM   15288 N  N   . ILE   E 2 544 ? 46.362  -5.054  -11.489 1.00 91.10  ? 848  ILE   E N   1 
ATOM   15289 C  CA  . ILE   E 2 544 ? 45.622  -3.931  -12.047 1.00 88.08  ? 848  ILE   E CA  1 
ATOM   15290 C  C   . ILE   E 2 544 ? 46.649  -2.871  -12.389 1.00 88.14  ? 848  ILE   E C   1 
ATOM   15291 O  O   . ILE   E 2 544 ? 47.553  -2.605  -11.593 1.00 89.93  ? 848  ILE   E O   1 
ATOM   15292 C  CB  . ILE   E 2 544 ? 44.567  -3.406  -11.067 1.00 84.36  ? 848  ILE   E CB  1 
ATOM   15293 C  CG1 . ILE   E 2 544 ? 43.584  -4.535  -10.738 1.00 87.38  ? 848  ILE   E CG1 1 
ATOM   15294 C  CG2 . ILE   E 2 544 ? 43.872  -2.179  -11.642 1.00 83.56  ? 848  ILE   E CG2 1 
ATOM   15295 C  CD1 . ILE   E 2 544 ? 42.487  -4.160  -9.780  1.00 85.64  ? 848  ILE   E CD1 1 
ATOM   15296 N  N   . VAL   E 2 545 ? 46.582  -2.336  -13.596 1.00 87.91  ? 849  VAL   E N   1 
ATOM   15297 C  CA  . VAL   E 2 545 ? 47.508  -1.297  -14.009 1.00 86.82  ? 849  VAL   E CA  1 
ATOM   15298 C  C   . VAL   E 2 545 ? 46.710  -0.066  -14.380 1.00 87.09  ? 849  VAL   E C   1 
ATOM   15299 O  O   . VAL   E 2 545 ? 45.629  -0.168  -14.967 1.00 86.70  ? 849  VAL   E O   1 
ATOM   15300 C  CB  . VAL   E 2 545 ? 48.402  -1.725  -15.184 1.00 90.98  ? 849  VAL   E CB  1 
ATOM   15301 C  CG1 . VAL   E 2 545 ? 49.199  -0.535  -15.663 1.00 91.91  ? 849  VAL   E CG1 1 
ATOM   15302 C  CG2 . VAL   E 2 545 ? 49.319  -2.846  -14.764 1.00 92.40  ? 849  VAL   E CG2 1 
ATOM   15303 N  N   . VAL   E 2 546 ? 47.245  1.099   -14.028 1.00 94.69  ? 850  VAL   E N   1 
ATOM   15304 C  CA  . VAL   E 2 546 ? 46.653  2.388   -14.374 1.00 95.07  ? 850  VAL   E CA  1 
ATOM   15305 C  C   . VAL   E 2 546 ? 47.566  3.103   -15.357 1.00 93.32  ? 850  VAL   E C   1 
ATOM   15306 O  O   . VAL   E 2 546 ? 48.740  3.345   -15.056 1.00 94.65  ? 850  VAL   E O   1 
ATOM   15307 C  CB  . VAL   E 2 546 ? 46.429  3.275   -13.143 1.00 91.58  ? 850  VAL   E CB  1 
ATOM   15308 C  CG1 . VAL   E 2 546 ? 45.837  4.597   -13.614 1.00 87.93  ? 850  VAL   E CG1 1 
ATOM   15309 C  CG2 . VAL   E 2 546 ? 45.541  2.568   -12.115 1.00 92.10  ? 850  VAL   E CG2 1 
ATOM   15310 N  N   . PHE   E 2 547 ? 47.023  3.472   -16.511 1.00 95.35  ? 851  PHE   E N   1 
ATOM   15311 C  CA  . PHE   E 2 547 ? 47.753  4.261   -17.491 1.00 96.59  ? 851  PHE   E CA  1 
ATOM   15312 C  C   . PHE   E 2 547 ? 47.113  5.635   -17.628 1.00 98.92  ? 851  PHE   E C   1 
ATOM   15313 O  O   . PHE   E 2 547 ? 45.990  5.892   -17.170 1.00 95.75  ? 851  PHE   E O   1 
ATOM   15314 C  CB  . PHE   E 2 547 ? 47.785  3.588   -18.866 1.00 92.64  ? 851  PHE   E CB  1 
ATOM   15315 C  CG  . PHE   E 2 547 ? 48.393  2.219   -18.868 1.00 95.12  ? 851  PHE   E CG  1 
ATOM   15316 C  CD1 . PHE   E 2 547 ? 47.601  1.089   -18.658 1.00 93.46  ? 851  PHE   E CD1 1 
ATOM   15317 C  CD2 . PHE   E 2 547 ? 49.754  2.051   -19.101 1.00 97.98  ? 851  PHE   E CD2 1 
ATOM   15318 C  CE1 . PHE   E 2 547 ? 48.165  -0.188  -18.668 1.00 92.35  ? 851  PHE   E CE1 1 
ATOM   15319 C  CE2 . PHE   E 2 547 ? 50.328  0.773   -19.122 1.00 95.42  ? 851  PHE   E CE2 1 
ATOM   15320 C  CZ  . PHE   E 2 547 ? 49.534  -0.341  -18.906 1.00 93.30  ? 851  PHE   E CZ  1 
ATOM   15321 N  N   . GLN   E 2 548 ? 47.803  6.499   -18.371 1.00 105.61 ? 852  GLN   E N   1 
ATOM   15322 C  CA  . GLN   E 2 548 ? 47.234  7.832   -18.683 1.00 105.95 ? 852  GLN   E CA  1 
ATOM   15323 C  C   . GLN   E 2 548 ? 47.831  8.260   -20.029 1.00 105.83 ? 852  GLN   E C   1 
ATOM   15324 O  O   . GLN   E 2 548 ? 49.071  8.257   -20.154 1.00 103.26 ? 852  GLN   E O   1 
ATOM   15325 C  CB  . GLN   E 2 548 ? 47.533  8.860   -17.597 1.00 106.64 ? 852  GLN   E CB  1 
ATOM   15326 C  CG  . GLN   E 2 548 ? 46.842  10.201  -17.814 1.00 111.49 ? 852  GLN   E CG  1 
ATOM   15327 C  CD  . GLN   E 2 548 ? 47.013  11.148  -16.647 1.00 110.86 ? 852  GLN   E CD  1 
ATOM   15328 O  OE1 . GLN   E 2 548 ? 47.576  10.791  -15.607 1.00 109.06 ? 852  GLN   E OE1 1 
ATOM   15329 N  NE2 . GLN   E 2 548 ? 46.530  12.370  -16.812 1.00 109.85 ? 852  GLN   E NE2 1 
ATOM   15330 N  N   . TYR   E 2 549 ? 46.978  8.565   -21.005 1.00 108.36 ? 853  TYR   E N   1 
ATOM   15331 C  CA  . TYR   E 2 549 ? 47.470  9.035   -22.326 1.00 117.78 ? 853  TYR   E CA  1 
ATOM   15332 C  C   . TYR   E 2 549 ? 47.226  10.524  -22.408 1.00 120.25 ? 853  TYR   E C   1 
ATOM   15333 O  O   . TYR   E 2 549 ? 46.054  10.947  -22.372 1.00 117.10 ? 853  TYR   E O   1 
ATOM   15334 C  CB  . TYR   E 2 549 ? 46.765  8.321   -23.480 1.00 108.64 ? 853  TYR   E CB  1 
ATOM   15335 C  CG  . TYR   E 2 549 ? 47.334  8.627   -24.857 1.00 106.06 ? 853  TYR   E CG  1 
ATOM   15336 C  CD1 . TYR   E 2 549 ? 48.499  8.019   -25.302 1.00 111.66 ? 853  TYR   E CD1 1 
ATOM   15337 C  CD2 . TYR   E 2 549 ? 46.701  9.522   -25.708 1.00 105.01 ? 853  TYR   E CD2 1 
ATOM   15338 C  CE1 . TYR   E 2 549 ? 49.017  8.291   -26.555 1.00 114.04 ? 853  TYR   E CE1 1 
ATOM   15339 C  CE2 . TYR   E 2 549 ? 47.211  9.806   -26.963 1.00 106.59 ? 853  TYR   E CE2 1 
ATOM   15340 C  CZ  . TYR   E 2 549 ? 48.373  9.188   -27.386 1.00 108.63 ? 853  TYR   E CZ  1 
ATOM   15341 O  OH  . TYR   E 2 549 ? 48.876  9.469   -28.622 1.00 103.70 ? 853  TYR   E OH  1 
ATOM   15342 N  N   . SER   E 2 550 ? 48.302  11.301  -22.516 1.00 133.47 ? 854  SER   E N   1 
ATOM   15343 C  CA  . SER   E 2 550 ? 48.170  12.777  -22.554 1.00 139.30 ? 854  SER   E CA  1 
ATOM   15344 C  C   . SER   E 2 550 ? 49.366  13.347  -23.321 1.00 143.33 ? 854  SER   E C   1 
ATOM   15345 O  O   . SER   E 2 550 ? 49.297  14.523  -23.732 1.00 145.10 ? 854  SER   E O   1 
ATOM   15346 C  CB  . SER   E 2 550 ? 47.887  13.312  -21.178 1.00 138.04 ? 854  SER   E CB  1 
ATOM   15347 O  OG  . SER   E 2 550 ? 48.731  12.694  -20.217 1.00 133.65 ? 854  SER   E OG  1 
ATOM   15348 N  N   . ASP   E 2 551 ? 50.406  12.541  -23.523 1.00 137.34 ? 855  ASP   E N   1 
ATOM   15349 C  CA  . ASP   E 2 551 ? 51.639  13.087  -24.143 1.00 141.38 ? 855  ASP   E CA  1 
ATOM   15350 C  C   . ASP   E 2 551 ? 52.097  12.354  -25.397 1.00 135.83 ? 855  ASP   E C   1 
ATOM   15351 O  O   . ASP   E 2 551 ? 53.319  12.291  -25.632 1.00 140.54 ? 855  ASP   E O   1 
ATOM   15352 C  CB  . ASP   E 2 551 ? 52.660  12.877  -23.042 1.00 147.78 ? 855  ASP   E CB  1 
ATOM   15353 C  CG  . ASP   E 2 551 ? 52.542  11.543  -22.322 1.00 147.28 ? 855  ASP   E CG  1 
ATOM   15354 O  OD1 . ASP   E 2 551 ? 51.521  11.336  -21.632 1.00 150.78 ? 855  ASP   E OD1 1 
ATOM   15355 O  OD2 . ASP   E 2 551 ? 53.464  10.716  -22.467 1.00 148.05 ? 855  ASP   E OD2 1 
ATOM   15356 N  N   . GLY   E 2 552 ? 51.162  11.790  -26.154 1.00 128.40 ? 856  GLY   E N   1 
ATOM   15357 C  CA  . GLY   E 2 552 ? 51.573  10.989  -27.318 1.00 134.76 ? 856  GLY   E CA  1 
ATOM   15358 C  C   . GLY   E 2 552 ? 52.139  9.656   -26.874 1.00 136.23 ? 856  GLY   E C   1 
ATOM   15359 O  O   . GLY   E 2 552 ? 52.539  8.862   -27.751 1.00 126.12 ? 856  GLY   E O   1 
ATOM   15360 N  N   . LYS   E 2 553 ? 52.153  9.405   -25.563 1.00 151.01 ? 857  LYS   E N   1 
ATOM   15361 C  CA  . LYS   E 2 553 ? 52.657  8.113   -25.038 1.00 148.18 ? 857  LYS   E CA  1 
ATOM   15362 C  C   . LYS   E 2 553 ? 51.865  7.712   -23.786 1.00 146.95 ? 857  LYS   E C   1 
ATOM   15363 O  O   . LYS   E 2 553 ? 51.278  8.603   -23.139 1.00 144.24 ? 857  LYS   E O   1 
ATOM   15364 C  CB  . LYS   E 2 553 ? 54.152  8.225   -24.728 1.00 148.40 ? 857  LYS   E CB  1 
ATOM   15365 N  N   . LEU   E 2 554 ? 51.848  6.415   -23.474 1.00 129.08 ? 858  LEU   E N   1 
ATOM   15366 C  CA  . LEU   E 2 554 ? 51.150  5.926   -22.261 1.00 122.25 ? 858  LEU   E CA  1 
ATOM   15367 C  C   . LEU   E 2 554 ? 52.070  6.146   -21.061 1.00 119.68 ? 858  LEU   E C   1 
ATOM   15368 O  O   . LEU   E 2 554 ? 53.283  5.896   -21.195 1.00 122.61 ? 858  LEU   E O   1 
ATOM   15369 C  CB  . LEU   E 2 554 ? 50.825  4.445   -22.428 1.00 108.40 ? 858  LEU   E CB  1 
ATOM   15370 C  CG  . LEU   E 2 554 ? 49.833  4.084   -23.535 1.00 104.61 ? 858  LEU   E CG  1 
ATOM   15371 C  CD1 . LEU   E 2 554 ? 49.708  2.582   -23.693 1.00 105.31 ? 858  LEU   E CD1 1 
ATOM   15372 C  CD2 . LEU   E 2 554 ? 48.484  4.704   -23.235 1.00 102.72 ? 858  LEU   E CD2 1 
ATOM   15373 N  N   . GLN   E 2 555 ? 51.513  6.590   -19.937 1.00 111.18 ? 859  GLN   E N   1 
ATOM   15374 C  CA  . GLN   E 2 555 ? 52.337  6.734   -18.712 1.00 111.88 ? 859  GLN   E CA  1 
ATOM   15375 C  C   . GLN   E 2 555 ? 51.743  5.832   -17.627 1.00 104.26 ? 859  GLN   E C   1 
ATOM   15376 O  O   . GLN   E 2 555 ? 50.563  6.019   -17.283 1.00 101.98 ? 859  GLN   E O   1 
ATOM   15377 C  CB  . GLN   E 2 555 ? 52.374  8.191   -18.257 1.00 112.01 ? 859  GLN   E CB  1 
ATOM   15378 N  N   . THR   E 2 556 ? 52.534  4.888   -17.124 1.00 101.42 ? 860  THR   E N   1 
ATOM   15379 C  CA  . THR   E 2 556 ? 52.040  4.028   -16.050 1.00 102.50 ? 860  THR   E CA  1 
ATOM   15380 C  C   . THR   E 2 556 ? 51.888  4.868   -14.781 1.00 97.67  ? 860  THR   E C   1 
ATOM   15381 O  O   . THR   E 2 556 ? 52.871  5.389   -14.244 1.00 95.30  ? 860  THR   E O   1 
ATOM   15382 C  CB  . THR   E 2 556 ? 52.971  2.837   -15.818 1.00 101.76 ? 860  THR   E CB  1 
ATOM   15383 O  OG1 . THR   E 2 556 ? 53.201  2.143   -17.056 1.00 102.21 ? 860  THR   E OG1 1 
ATOM   15384 C  CG2 . THR   E 2 556 ? 52.360  1.864   -14.789 1.00 98.44  ? 860  THR   E CG2 1 
ATOM   15385 N  N   . VAL   E 2 557 ? 50.652  5.040   -14.322 1.00 98.10  ? 861  VAL   E N   1 
ATOM   15386 C  CA  . VAL   E 2 557 ? 50.406  5.844   -13.130 1.00 97.54  ? 861  VAL   E CA  1 
ATOM   15387 C  C   . VAL   E 2 557 ? 50.444  4.997   -11.853 1.00 100.41 ? 861  VAL   E C   1 
ATOM   15388 O  O   . VAL   E 2 557 ? 50.772  5.516   -10.781 1.00 104.44 ? 861  VAL   E O   1 
ATOM   15389 C  CB  . VAL   E 2 557 ? 49.069  6.600   -13.253 1.00 91.67  ? 861  VAL   E CB  1 
ATOM   15390 C  CG1 . VAL   E 2 557 ? 48.735  7.292   -11.955 1.00 94.08  ? 861  VAL   E CG1 1 
ATOM   15391 C  CG2 . VAL   E 2 557 ? 49.103  7.604   -14.395 1.00 94.79  ? 861  VAL   E CG2 1 
ATOM   15392 N  N   . ALA   E 2 558 ? 50.139  3.701   -11.932 1.00 98.50  ? 862  ALA   E N   1 
ATOM   15393 C  CA  . ALA   E 2 558 ? 50.048  2.900   -10.716 1.00 98.39  ? 862  ALA   E CA  1 
ATOM   15394 C  C   . ALA   E 2 558 ? 49.855  1.444   -11.101 1.00 96.37  ? 862  ALA   E C   1 
ATOM   15395 O  O   . ALA   E 2 558 ? 49.272  1.146   -12.143 1.00 94.91  ? 862  ALA   E O   1 
ATOM   15396 C  CB  . ALA   E 2 558 ? 48.891  3.379   -9.827  1.00 95.54  ? 862  ALA   E CB  1 
ATOM   15397 N  N   . GLU   E 2 559 ? 50.351  0.537   -10.261 1.00 98.52  ? 863  GLU   E N   1 
ATOM   15398 C  CA  . GLU   E 2 559 ? 50.077  -0.882  -10.474 1.00 99.12  ? 863  GLU   E CA  1 
ATOM   15399 C  C   . GLU   E 2 559 ? 49.888  -1.583  -9.136  1.00 98.08  ? 863  GLU   E C   1 
ATOM   15400 O  O   . GLU   E 2 559 ? 50.789  -1.555  -8.294  1.00 103.54 ? 863  GLU   E O   1 
ATOM   15401 C  CB  . GLU   E 2 559 ? 51.191  -1.543  -11.285 1.00 100.86 ? 863  GLU   E CB  1 
ATOM   15402 C  CG  . GLU   E 2 559 ? 52.563  -1.464  -10.664 1.00 108.10 ? 863  GLU   E CG  1 
ATOM   15403 C  CD  . GLU   E 2 559 ? 53.631  -2.124  -11.529 1.00 120.07 ? 863  GLU   E CD  1 
ATOM   15404 O  OE1 . GLU   E 2 559 ? 53.605  -3.374  -11.673 1.00 115.35 ? 863  GLU   E OE1 1 
ATOM   15405 O  OE2 . GLU   E 2 559 ? 54.485  -1.384  -12.078 1.00 127.91 ? 863  GLU   E OE2 1 
ATOM   15406 N  N   . LYS   E 2 560 ? 48.718  -2.213  -8.941  1.00 93.38  ? 864  LYS   E N   1 
ATOM   15407 C  CA  . LYS   E 2 560 ? 48.380  -2.949  -7.722  1.00 93.87  ? 864  LYS   E CA  1 
ATOM   15408 C  C   . LYS   E 2 560 ? 48.382  -4.444  -8.035  1.00 93.94  ? 864  LYS   E C   1 
ATOM   15409 O  O   . LYS   E 2 560 ? 47.533  -4.921  -8.797  1.00 96.32  ? 864  LYS   E O   1 
ATOM   15410 C  CB  . LYS   E 2 560 ? 47.023  -2.507  -7.159  1.00 91.79  ? 864  LYS   E CB  1 
ATOM   15411 C  CG  . LYS   E 2 560 ? 46.590  -3.260  -5.883  1.00 92.60  ? 864  LYS   E CG  1 
ATOM   15412 C  CD  . LYS   E 2 560 ? 47.543  -3.062  -4.689  1.00 89.99  ? 864  LYS   E CD  1 
ATOM   15413 C  CE  . LYS   E 2 560 ? 46.956  -3.701  -3.399  1.00 96.28  ? 864  LYS   E CE  1 
ATOM   15414 N  NZ  . LYS   E 2 560 ? 47.849  -3.783  -2.179  1.00 93.78  ? 864  LYS   E NZ  1 
ATOM   15415 N  N   . GLU   E 2 561 ? 49.323  -5.181  -7.436  1.00 93.49  ? 865  GLU   E N   1 
ATOM   15416 C  CA  . GLU   E 2 561 ? 49.396  -6.631  -7.617  1.00 96.69  ? 865  GLU   E CA  1 
ATOM   15417 C  C   . GLU   E 2 561 ? 48.283  -7.323  -6.834  1.00 100.70 ? 865  GLU   E C   1 
ATOM   15418 O  O   . GLU   E 2 561 ? 48.107  -7.073  -5.635  1.00 102.32 ? 865  GLU   E O   1 
ATOM   15419 C  CB  . GLU   E 2 561 ? 50.771  -7.164  -7.179  1.00 101.11 ? 865  GLU   E CB  1 
ATOM   15420 C  CG  . GLU   E 2 561 ? 50.811  -8.649  -6.736  1.00 109.65 ? 865  GLU   E CG  1 
ATOM   15421 C  CD  . GLU   E 2 561 ? 52.199  -9.111  -6.236  1.00 119.95 ? 865  GLU   E CD  1 
ATOM   15422 O  OE1 . GLU   E 2 561 ? 52.937  -8.280  -5.661  1.00 121.68 ? 865  GLU   E OE1 1 
ATOM   15423 O  OE2 . GLU   E 2 561 ? 52.550  -10.305 -6.416  1.00 122.79 ? 865  GLU   E OE2 1 
ATOM   15424 N  N   . VAL   E 2 562 ? 47.526  -8.183  -7.523  1.00 102.27 ? 866  VAL   E N   1 
ATOM   15425 C  CA  . VAL   E 2 562 ? 46.476  -8.996  -6.918  1.00 95.93  ? 866  VAL   E CA  1 
ATOM   15426 C  C   . VAL   E 2 562 ? 46.898  -10.464 -6.933  1.00 94.26  ? 866  VAL   E C   1 
ATOM   15427 O  O   . VAL   E 2 562 ? 47.741  -10.906 -7.730  1.00 90.83  ? 866  VAL   E O   1 
ATOM   15428 C  CB  . VAL   E 2 562 ? 45.120  -8.820  -7.622  1.00 92.73  ? 866  VAL   E CB  1 
ATOM   15429 C  CG1 . VAL   E 2 562 ? 44.500  -7.476  -7.244  1.00 95.77  ? 866  VAL   E CG1 1 
ATOM   15430 C  CG2 . VAL   E 2 562 ? 45.288  -8.957  -9.148  1.00 94.57  ? 866  VAL   E CG2 1 
ATOM   15431 N  N   . LYS   E 2 563 ? 46.304  -11.227 -6.023  1.00 92.95  ? 867  LYS   E N   1 
ATOM   15432 C  CA  . LYS   E 2 563 ? 46.603  -12.648 -5.892  1.00 91.46  ? 867  LYS   E CA  1 
ATOM   15433 C  C   . LYS   E 2 563 ? 45.638  -13.483 -6.708  1.00 91.53  ? 867  LYS   E C   1 
ATOM   15434 O  O   . LYS   E 2 563 ? 45.186  -14.545 -6.274  1.00 99.50  ? 867  LYS   E O   1 
ATOM   15435 C  CB  . LYS   E 2 563 ? 46.581  -13.066 -4.424  1.00 93.31  ? 867  LYS   E CB  1 
ATOM   15436 N  N   . GLY   E 2 564 ? 45.291  -13.020 -7.897  1.00 92.71  ? 868  GLY   E N   1 
ATOM   15437 C  CA  . GLY   E 2 564 ? 44.349  -13.745 -8.725  1.00 91.84  ? 868  GLY   E CA  1 
ATOM   15438 C  C   . GLY   E 2 564 ? 44.321  -13.205 -10.136 1.00 92.04  ? 868  GLY   E C   1 
ATOM   15439 O  O   . GLY   E 2 564 ? 45.345  -12.718 -10.624 1.00 92.06  ? 868  GLY   E O   1 
ATOM   15440 N  N   . ALA   E 2 565 ? 43.161  -13.273 -10.795 1.00 91.78  ? 869  ALA   E N   1 
ATOM   15441 C  CA  . ALA   E 2 565 ? 43.003  -12.833 -12.177 1.00 86.80  ? 869  ALA   E CA  1 
ATOM   15442 C  C   . ALA   E 2 565 ? 41.906  -11.782 -12.240 1.00 91.21  ? 869  ALA   E C   1 
ATOM   15443 O  O   . ALA   E 2 565 ? 40.739  -12.082 -11.949 1.00 89.88  ? 869  ALA   E O   1 
ATOM   15444 C  CB  . ALA   E 2 565 ? 42.658  -14.005 -13.096 1.00 83.41  ? 869  ALA   E CB  1 
ATOM   15445 N  N   . VAL   E 2 566 ? 42.271  -10.561 -12.630 1.00 84.77  ? 870  VAL   E N   1 
ATOM   15446 C  CA  . VAL   E 2 566 ? 41.264  -9.534  -12.841 1.00 86.64  ? 870  VAL   E CA  1 
ATOM   15447 C  C   . VAL   E 2 566 ? 40.399  -9.969  -14.015 1.00 87.87  ? 870  VAL   E C   1 
ATOM   15448 O  O   . VAL   E 2 566 ? 40.835  -9.904  -15.168 1.00 90.71  ? 870  VAL   E O   1 
ATOM   15449 C  CB  . VAL   E 2 566 ? 41.894  -8.152  -13.100 1.00 89.25  ? 870  VAL   E CB  1 
ATOM   15450 C  CG1 . VAL   E 2 566 ? 40.846  -7.058  -12.930 1.00 88.17  ? 870  VAL   E CG1 1 
ATOM   15451 C  CG2 . VAL   E 2 566 ? 43.082  -7.916  -12.173 1.00 91.20  ? 870  VAL   E CG2 1 
ATOM   15452 N  N   . TYR   E 2 567 ? 39.175  -10.421 -13.746 1.00 85.12  ? 871  TYR   E N   1 
ATOM   15453 C  CA  . TYR   E 2 567 ? 38.291  -10.784 -14.845 1.00 84.86  ? 871  TYR   E CA  1 
ATOM   15454 C  C   . TYR   E 2 567 ? 37.395  -9.643  -15.285 1.00 83.93  ? 871  TYR   E C   1 
ATOM   15455 O  O   . TYR   E 2 567 ? 36.949  -9.622  -16.437 1.00 91.68  ? 871  TYR   E O   1 
ATOM   15456 C  CB  . TYR   E 2 567 ? 37.399  -11.962 -14.466 1.00 89.47  ? 871  TYR   E CB  1 
ATOM   15457 C  CG  . TYR   E 2 567 ? 38.116  -13.284 -14.298 1.00 90.12  ? 871  TYR   E CG  1 
ATOM   15458 C  CD1 . TYR   E 2 567 ? 38.737  -13.905 -15.366 1.00 86.88  ? 871  TYR   E CD1 1 
ATOM   15459 C  CD2 . TYR   E 2 567 ? 38.157  -13.914 -13.064 1.00 91.27  ? 871  TYR   E CD2 1 
ATOM   15460 C  CE1 . TYR   E 2 567 ? 39.383  -15.111 -15.209 1.00 88.96  ? 871  TYR   E CE1 1 
ATOM   15461 C  CE2 . TYR   E 2 567 ? 38.797  -15.116 -12.897 1.00 90.66  ? 871  TYR   E CE2 1 
ATOM   15462 C  CZ  . TYR   E 2 567 ? 39.410  -15.719 -13.971 1.00 91.56  ? 871  TYR   E CZ  1 
ATOM   15463 O  OH  . TYR   E 2 567 ? 40.045  -16.935 -13.790 1.00 90.39  ? 871  TYR   E OH  1 
ATOM   15464 N  N   . SER   E 2 568 ? 37.088  -8.706  -14.404 1.00 85.39  ? 872  SER   E N   1 
ATOM   15465 C  CA  . SER   E 2 568 ? 36.174  -7.634  -14.773 1.00 88.36  ? 872  SER   E CA  1 
ATOM   15466 C  C   . SER   E 2 568 ? 36.513  -6.408  -13.943 1.00 88.75  ? 872  SER   E C   1 
ATOM   15467 O  O   . SER   E 2 568 ? 36.877  -6.530  -12.768 1.00 92.55  ? 872  SER   E O   1 
ATOM   15468 C  CB  . SER   E 2 568 ? 34.705  -8.033  -14.546 1.00 87.89  ? 872  SER   E CB  1 
ATOM   15469 O  OG  . SER   E 2 568 ? 34.193  -8.788  -15.639 1.00 90.81  ? 872  SER   E OG  1 
ATOM   15470 N  N   . MET   E 2 569 ? 36.395  -5.229  -14.557 1.00 86.67  ? 873  MET   E N   1 
ATOM   15471 C  CA  . MET   E 2 569 ? 36.514  -3.972  -13.828 1.00 88.08  ? 873  MET   E CA  1 
ATOM   15472 C  C   . MET   E 2 569 ? 35.334  -3.072  -14.180 1.00 86.39  ? 873  MET   E C   1 
ATOM   15473 O  O   . MET   E 2 569 ? 35.013  -2.889  -15.357 1.00 90.29  ? 873  MET   E O   1 
ATOM   15474 C  CB  . MET   E 2 569 ? 37.854  -3.285  -14.126 1.00 80.38  ? 873  MET   E CB  1 
ATOM   15475 C  CG  . MET   E 2 569 ? 39.015  -3.798  -13.275 1.00 79.76  ? 873  MET   E CG  1 
ATOM   15476 S  SD  . MET   E 2 569 ? 40.607  -3.580  -14.121 1.00 85.42  ? 873  MET   E SD  1 
ATOM   15477 C  CE  . MET   E 2 569 ? 40.184  -2.316  -15.310 1.00 88.04  ? 873  MET   E CE  1 
ATOM   15478 N  N   . VAL   E 2 570 ? 34.671  -2.527  -13.164 1.00 84.74  ? 874  VAL   E N   1 
ATOM   15479 C  CA  . VAL   E 2 570 ? 33.563  -1.603  -13.373 1.00 88.99  ? 874  VAL   E CA  1 
ATOM   15480 C  C   . VAL   E 2 570 ? 33.809  -0.352  -12.535 1.00 95.11  ? 874  VAL   E C   1 
ATOM   15481 O  O   . VAL   E 2 570 ? 34.050  -0.451  -11.324 1.00 92.80  ? 874  VAL   E O   1 
ATOM   15482 C  CB  . VAL   E 2 570 ? 32.221  -2.255  -13.006 1.00 85.52  ? 874  VAL   E CB  1 
ATOM   15483 C  CG1 . VAL   E 2 570 ? 31.087  -1.283  -13.222 1.00 83.25  ? 874  VAL   E CG1 1 
ATOM   15484 C  CG2 . VAL   E 2 570 ? 32.047  -3.508  -13.828 1.00 88.31  ? 874  VAL   E CG2 1 
ATOM   15485 N  N   . GLU   E 2 571 ? 33.795  0.818   -13.182 1.00 89.25  ? 875  GLU   E N   1 
ATOM   15486 C  CA  . GLU   E 2 571 ? 33.779  2.065   -12.430 1.00 91.61  ? 875  GLU   E CA  1 
ATOM   15487 C  C   . GLU   E 2 571 ? 32.448  2.159   -11.694 1.00 94.68  ? 875  GLU   E C   1 
ATOM   15488 O  O   . GLU   E 2 571 ? 31.383  1.978   -12.293 1.00 97.64  ? 875  GLU   E O   1 
ATOM   15489 C  CB  . GLU   E 2 571 ? 33.993  3.259   -13.364 1.00 96.05  ? 875  GLU   E CB  1 
ATOM   15490 C  CG  . GLU   E 2 571 ? 33.909  4.630   -12.693 1.00 99.72  ? 875  GLU   E CG  1 
ATOM   15491 C  CD  . GLU   E 2 571 ? 32.494  5.217   -12.714 1.00 106.44 ? 875  GLU   E CD  1 
ATOM   15492 O  OE1 . GLU   E 2 571 ? 31.563  4.544   -13.225 1.00 107.16 ? 875  GLU   E OE1 1 
ATOM   15493 O  OE2 . GLU   E 2 571 ? 32.316  6.358   -12.223 1.00 107.81 ? 875  GLU   E OE2 1 
ATOM   15494 N  N   . PHE   E 2 572 ? 32.504  2.400   -10.388 1.00 96.58  ? 876  PHE   E N   1 
ATOM   15495 C  CA  . PHE   E 2 572 ? 31.349  2.209   -9.512  1.00 100.86 ? 876  PHE   E CA  1 
ATOM   15496 C  C   . PHE   E 2 572 ? 31.233  3.411   -8.582  1.00 106.99 ? 876  PHE   E C   1 
ATOM   15497 O  O   . PHE   E 2 572 ? 31.889  3.464   -7.537  1.00 105.02 ? 876  PHE   E O   1 
ATOM   15498 C  CB  . PHE   E 2 572 ? 31.492  0.908   -8.727  1.00 98.94  ? 876  PHE   E CB  1 
ATOM   15499 C  CG  . PHE   E 2 572 ? 30.298  0.555   -7.915  1.00 94.05  ? 876  PHE   E CG  1 
ATOM   15500 C  CD1 . PHE   E 2 572 ? 29.164  0.065   -8.522  1.00 94.18  ? 876  PHE   E CD1 1 
ATOM   15501 C  CD2 . PHE   E 2 572 ? 30.322  0.697   -6.543  1.00 93.73  ? 876  PHE   E CD2 1 
ATOM   15502 C  CE1 . PHE   E 2 572 ? 28.063  -0.273  -7.775  1.00 100.35 ? 876  PHE   E CE1 1 
ATOM   15503 C  CE2 . PHE   E 2 572 ? 29.229  0.367   -5.787  1.00 101.77 ? 876  PHE   E CE2 1 
ATOM   15504 C  CZ  . PHE   E 2 572 ? 28.088  -0.119  -6.402  1.00 104.71 ? 876  PHE   E CZ  1 
ATOM   15505 N  N   . ASN   E 2 573 ? 30.397  4.374   -8.960  1.00 118.13 ? 877  ASN   E N   1 
ATOM   15506 C  CA  . ASN   E 2 573 ? 30.186  5.583   -8.165  1.00 117.14 ? 877  ASN   E CA  1 
ATOM   15507 C  C   . ASN   E 2 573 ? 31.521  6.252   -7.839  1.00 115.39 ? 877  ASN   E C   1 
ATOM   15508 O  O   . ASN   E 2 573 ? 31.837  6.535   -6.686  1.00 117.22 ? 877  ASN   E O   1 
ATOM   15509 C  CB  . ASN   E 2 573 ? 29.412  5.264   -6.884  1.00 115.92 ? 877  ASN   E CB  1 
ATOM   15510 C  CG  . ASN   E 2 573 ? 28.071  4.596   -7.160  1.00 120.19 ? 877  ASN   E CG  1 
ATOM   15511 O  OD1 . ASN   E 2 573 ? 27.589  4.590   -8.293  1.00 123.77 ? 877  ASN   E OD1 1 
ATOM   15512 N  ND2 . ASN   E 2 573 ? 27.448  4.046   -6.112  1.00 118.44 ? 877  ASN   E ND2 1 
ATOM   15513 N  N   . GLY   E 2 574 ? 32.322  6.481   -8.881  1.00 104.52 ? 878  GLY   E N   1 
ATOM   15514 C  CA  . GLY   E 2 574 ? 33.618  7.104   -8.733  1.00 99.68  ? 878  GLY   E CA  1 
ATOM   15515 C  C   . GLY   E 2 574 ? 34.719  6.186   -8.263  1.00 102.46 ? 878  GLY   E C   1 
ATOM   15516 O  O   . GLY   E 2 574 ? 35.901  6.518   -8.435  1.00 100.51 ? 878  GLY   E O   1 
ATOM   15517 N  N   . LYS   E 2 575 ? 34.376  5.044   -7.668  1.00 103.92 ? 879  LYS   E N   1 
ATOM   15518 C  CA  . LYS   E 2 575 ? 35.318  4.004   -7.274  1.00 98.59  ? 879  LYS   E CA  1 
ATOM   15519 C  C   . LYS   E 2 575 ? 35.433  2.952   -8.381  1.00 95.29  ? 879  LYS   E C   1 
ATOM   15520 O  O   . LYS   E 2 575 ? 34.693  2.967   -9.368  1.00 98.67  ? 879  LYS   E O   1 
ATOM   15521 C  CB  . LYS   E 2 575 ? 34.868  3.367   -5.965  1.00 94.24  ? 879  LYS   E CB  1 
ATOM   15522 C  CG  . LYS   E 2 575 ? 34.673  4.359   -4.815  1.00 93.18  ? 879  LYS   E CG  1 
ATOM   15523 C  CD  . LYS   E 2 575 ? 33.638  3.856   -3.790  1.00 91.20  ? 879  LYS   E CD  1 
ATOM   15524 C  CE  . LYS   E 2 575 ? 33.934  4.328   -2.360  1.00 87.51  ? 879  LYS   E CE  1 
ATOM   15525 N  NZ  . LYS   E 2 575 ? 33.972  3.227   -1.322  1.00 97.43  ? 879  LYS   E NZ  1 
ATOM   15526 N  N   . LEU   E 2 576 ? 36.370  2.019   -8.226  1.00 91.70  ? 880  LEU   E N   1 
ATOM   15527 C  CA  . LEU   E 2 576 ? 36.559  0.948   -9.209  1.00 95.54  ? 880  LEU   E CA  1 
ATOM   15528 C  C   . LEU   E 2 576 ? 36.195  -0.410  -8.601  1.00 94.14  ? 880  LEU   E C   1 
ATOM   15529 O  O   . LEU   E 2 576 ? 36.845  -0.863  -7.647  1.00 88.59  ? 880  LEU   E O   1 
ATOM   15530 C  CB  . LEU   E 2 576 ? 38.000  0.941   -9.748  1.00 89.82  ? 880  LEU   E CB  1 
ATOM   15531 C  CG  . LEU   E 2 576 ? 38.532  -0.312  -10.478 1.00 86.01  ? 880  LEU   E CG  1 
ATOM   15532 C  CD1 . LEU   E 2 576 ? 39.390  -0.030  -11.731 1.00 82.06  ? 880  LEU   E CD1 1 
ATOM   15533 C  CD2 . LEU   E 2 576 ? 39.308  -1.208  -9.506  1.00 86.34  ? 880  LEU   E CD2 1 
ATOM   15534 N  N   . LEU   E 2 577 ? 35.151  -1.050  -9.159  1.00 90.04  ? 881  LEU   E N   1 
ATOM   15535 C  CA  . LEU   E 2 577 ? 34.785  -2.428  -8.832  1.00 90.82  ? 881  LEU   E CA  1 
ATOM   15536 C  C   . LEU   E 2 577 ? 35.611  -3.398  -9.675  1.00 88.56  ? 881  LEU   E C   1 
ATOM   15537 O  O   . LEU   E 2 577 ? 35.774  -3.204  -10.887 1.00 88.44  ? 881  LEU   E O   1 
ATOM   15538 C  CB  . LEU   E 2 577 ? 33.289  -2.654  -9.067  1.00 88.90  ? 881  LEU   E CB  1 
ATOM   15539 C  CG  . LEU   E 2 577 ? 32.650  -3.749  -8.225  1.00 87.38  ? 881  LEU   E CG  1 
ATOM   15540 C  CD1 . LEU   E 2 577 ? 33.351  -3.800  -6.881  1.00 90.62  ? 881  LEU   E CD1 1 
ATOM   15541 C  CD2 . LEU   E 2 577 ? 31.163  -3.486  -8.020  1.00 84.13  ? 881  LEU   E CD2 1 
ATOM   15542 N  N   . ALA   E 2 578 ? 36.148  -4.430  -9.030  1.00 87.20  ? 882  ALA   E N   1 
ATOM   15543 C  CA  . ALA   E 2 578 ? 37.030  -5.375  -9.705  1.00 91.39  ? 882  ALA   E CA  1 
ATOM   15544 C  C   . ALA   E 2 578 ? 36.813  -6.769  -9.148  1.00 89.81  ? 882  ALA   E C   1 
ATOM   15545 O  O   . ALA   E 2 578 ? 36.696  -6.948  -7.933  1.00 91.79  ? 882  ALA   E O   1 
ATOM   15546 C  CB  . ALA   E 2 578 ? 38.507  -4.994  -9.546  1.00 85.72  ? 882  ALA   E CB  1 
ATOM   15547 N  N   . SER   E 2 579 ? 36.765  -7.751  -10.031 1.00 88.88  ? 883  SER   E N   1 
ATOM   15548 C  CA  . SER   E 2 579 ? 36.675  -9.139  -9.601  1.00 93.42  ? 883  SER   E CA  1 
ATOM   15549 C  C   . SER   E 2 579 ? 38.053  -9.788  -9.726  1.00 91.67  ? 883  SER   E C   1 
ATOM   15550 O  O   . SER   E 2 579 ? 38.744  -9.604  -10.740 1.00 92.84  ? 883  SER   E O   1 
ATOM   15551 C  CB  . SER   E 2 579 ? 35.609  -9.891  -10.405 1.00 86.76  ? 883  SER   E CB  1 
ATOM   15552 O  OG  . SER   E 2 579 ? 35.861  -9.829  -11.799 1.00 90.72  ? 883  SER   E OG  1 
ATOM   15553 N  N   . ILE   E 2 580 ? 38.476  -10.476 -8.669  1.00 88.02  ? 884  ILE   E N   1 
ATOM   15554 C  CA  . ILE   E 2 580 ? 39.691  -11.285 -8.692  1.00 89.60  ? 884  ILE   E CA  1 
ATOM   15555 C  C   . ILE   E 2 580 ? 39.300  -12.703 -8.315  1.00 90.91  ? 884  ILE   E C   1 
ATOM   15556 O  O   . ILE   E 2 580 ? 38.988  -12.990 -7.149  1.00 93.71  ? 884  ILE   E O   1 
ATOM   15557 C  CB  . ILE   E 2 580 ? 40.780  -10.770 -7.748  1.00 90.39  ? 884  ILE   E CB  1 
ATOM   15558 C  CG1 . ILE   E 2 580 ? 41.003  -9.277  -7.956  1.00 92.56  ? 884  ILE   E CG1 1 
ATOM   15559 C  CG2 . ILE   E 2 580 ? 42.068  -11.525 -8.029  1.00 86.80  ? 884  ILE   E CG2 1 
ATOM   15560 C  CD1 . ILE   E 2 580 ? 40.291  -8.444  -6.946  1.00 90.30  ? 884  ILE   E CD1 1 
ATOM   15561 N  N   . ASN   E 2 581 ? 39.316  -13.589 -9.305  1.00 91.81  ? 885  ASN   E N   1 
ATOM   15562 C  CA  . ASN   E 2 581 ? 38.955  -14.997 -9.163  1.00 85.50  ? 885  ASN   E CA  1 
ATOM   15563 C  C   . ASN   E 2 581 ? 37.584  -14.900 -8.457  1.00 86.46  ? 885  ASN   E C   1 
ATOM   15564 O  O   . ASN   E 2 581 ? 36.694  -14.220 -8.967  1.00 86.22  ? 885  ASN   E O   1 
ATOM   15565 C  CB  . ASN   E 2 581 ? 40.013  -15.718 -8.344  1.00 83.12  ? 885  ASN   E CB  1 
ATOM   15566 C  CG  . ASN   E 2 581 ? 41.334  -15.904 -9.140  1.00 84.31  ? 885  ASN   E CG  1 
ATOM   15567 O  OD1 . ASN   E 2 581 ? 41.439  -15.542 -10.314 1.00 87.96  ? 885  ASN   E OD1 1 
ATOM   15568 N  ND2 . ASN   E 2 581 ? 42.340  -16.473 -8.488  1.00 87.15  ? 885  ASN   E ND2 1 
ATOM   15569 N  N   . SER   E 2 582 ? 37.386  -15.561 -7.314  1.00 89.39  ? 886  SER   E N   1 
ATOM   15570 C  CA  . SER   E 2 582 ? 36.107  -15.536 -6.654  1.00 88.64  ? 886  SER   E CA  1 
ATOM   15571 C  C   . SER   E 2 582 ? 35.696  -14.287 -5.844  1.00 94.04  ? 886  SER   E C   1 
ATOM   15572 O  O   . SER   E 2 582 ? 34.561  -14.221 -5.354  1.00 93.94  ? 886  SER   E O   1 
ATOM   15573 C  CB  . SER   E 2 582 ? 36.031  -16.751 -5.723  1.00 88.63  ? 886  SER   E CB  1 
ATOM   15574 O  OG  . SER   E 2 582 ? 36.310  -16.391 -4.371  1.00 89.82  ? 886  SER   E OG  1 
ATOM   15575 N  N   . THR   E 2 583 ? 36.590  -13.303 -5.727  1.00 90.34  ? 887  THR   E N   1 
ATOM   15576 C  CA  . THR   E 2 583 ? 36.434  -12.165 -4.832  1.00 90.51  ? 887  THR   E CA  1 
ATOM   15577 C  C   . THR   E 2 583 ? 36.063  -10.915 -5.614  1.00 91.62  ? 887  THR   E C   1 
ATOM   15578 O  O   . THR   E 2 583 ? 36.756  -10.553 -6.572  1.00 92.81  ? 887  THR   E O   1 
ATOM   15579 C  CB  . THR   E 2 583 ? 37.730  -11.894 -4.077  1.00 98.74  ? 887  THR   E CB  1 
ATOM   15580 O  OG1 . THR   E 2 583 ? 38.091  -13.043 -3.277  1.00 104.09 ? 887  THR   E OG1 1 
ATOM   15581 C  CG2 . THR   E 2 583 ? 37.574  -10.657 -3.195  1.00 94.24  ? 887  THR   E CG2 1 
ATOM   15582 N  N   . VAL   E 2 584 ? 34.997  -10.237 -5.185  1.00 91.79  ? 888  VAL   E N   1 
ATOM   15583 C  CA  . VAL   E 2 584 ? 34.640  -8.904  -5.683  1.00 95.08  ? 888  VAL   E CA  1 
ATOM   15584 C  C   . VAL   E 2 584 ? 35.181  -7.848  -4.727  1.00 94.26  ? 888  VAL   E C   1 
ATOM   15585 O  O   . VAL   E 2 584 ? 34.934  -7.908  -3.518  1.00 97.67  ? 888  VAL   E O   1 
ATOM   15586 C  CB  . VAL   E 2 584 ? 33.122  -8.752  -5.831  1.00 93.43  ? 888  VAL   E CB  1 
ATOM   15587 C  CG1 . VAL   E 2 584 ? 32.785  -7.325  -6.272  1.00 89.87  ? 888  VAL   E CG1 1 
ATOM   15588 C  CG2 . VAL   E 2 584 ? 32.634  -9.777  -6.800  1.00 90.09  ? 888  VAL   E CG2 1 
ATOM   15589 N  N   . ARG   E 2 585 ? 35.888  -6.862  -5.266  1.00 91.18  ? 889  ARG   E N   1 
ATOM   15590 C  CA  . ARG   E 2 585 ? 36.645  -5.919  -4.453  1.00 92.52  ? 889  ARG   E CA  1 
ATOM   15591 C  C   . ARG   E 2 585 ? 36.410  -4.495  -4.927  1.00 95.52  ? 889  ARG   E C   1 
ATOM   15592 O  O   . ARG   E 2 585 ? 36.576  -4.192  -6.119  1.00 93.01  ? 889  ARG   E O   1 
ATOM   15593 C  CB  . ARG   E 2 585 ? 38.134  -6.233  -4.503  1.00 89.03  ? 889  ARG   E CB  1 
ATOM   15594 C  CG  . ARG   E 2 585 ? 39.024  -5.040  -4.267  1.00 86.95  ? 889  ARG   E CG  1 
ATOM   15595 C  CD  . ARG   E 2 585 ? 40.431  -5.542  -4.183  1.00 85.94  ? 889  ARG   E CD  1 
ATOM   15596 N  NE  . ARG   E 2 585 ? 40.507  -6.590  -3.177  1.00 87.71  ? 889  ARG   E NE  1 
ATOM   15597 C  CZ  . ARG   E 2 585 ? 41.438  -7.533  -3.131  1.00 89.28  ? 889  ARG   E CZ  1 
ATOM   15598 N  NH1 . ARG   E 2 585 ? 42.436  -7.564  -4.002  1.00 87.21  ? 889  ARG   E NH1 1 
ATOM   15599 N  NH2 . ARG   E 2 585 ? 41.347  -8.489  -2.204  1.00 91.00  ? 889  ARG   E NH2 1 
ATOM   15600 N  N   . LEU   E 2 586 ? 36.044  -3.628  -3.988  1.00 93.93  ? 890  LEU   E N   1 
ATOM   15601 C  CA  . LEU   E 2 586 ? 35.877  -2.214  -4.271  1.00 90.61  ? 890  LEU   E CA  1 
ATOM   15602 C  C   . LEU   E 2 586 ? 37.176  -1.497  -3.940  1.00 90.32  ? 890  LEU   E C   1 
ATOM   15603 O  O   . LEU   E 2 586 ? 37.715  -1.664  -2.845  1.00 94.77  ? 890  LEU   E O   1 
ATOM   15604 C  CB  . LEU   E 2 586 ? 34.728  -1.640  -3.455  1.00 87.41  ? 890  LEU   E CB  1 
ATOM   15605 C  CG  . LEU   E 2 586 ? 34.320  -0.283  -3.991  1.00 89.12  ? 890  LEU   E CG  1 
ATOM   15606 C  CD1 . LEU   E 2 586 ? 34.539  -0.221  -5.503  1.00 90.75  ? 890  LEU   E CD1 1 
ATOM   15607 C  CD2 . LEU   E 2 586 ? 32.874  -0.021  -3.633  1.00 91.49  ? 890  LEU   E CD2 1 
ATOM   15608 N  N   . TYR   E 2 587 ? 37.687  -0.724  -4.886  1.00 91.67  ? 891  TYR   E N   1 
ATOM   15609 C  CA  . TYR   E 2 587 ? 38.907  0.044   -4.690  1.00 92.96  ? 891  TYR   E CA  1 
ATOM   15610 C  C   . TYR   E 2 587 ? 38.588  1.539   -4.693  1.00 93.27  ? 891  TYR   E C   1 
ATOM   15611 O  O   . TYR   E 2 587 ? 37.553  1.973   -5.214  1.00 89.23  ? 891  TYR   E O   1 
ATOM   15612 C  CB  . TYR   E 2 587 ? 39.931  -0.263  -5.788  1.00 92.51  ? 891  TYR   E CB  1 
ATOM   15613 C  CG  . TYR   E 2 587 ? 40.801  -1.495  -5.616  1.00 88.26  ? 891  TYR   E CG  1 
ATOM   15614 C  CD1 . TYR   E 2 587 ? 41.726  -1.587  -4.585  1.00 90.51  ? 891  TYR   E CD1 1 
ATOM   15615 C  CD2 . TYR   E 2 587 ? 40.758  -2.533  -6.542  1.00 89.23  ? 891  TYR   E CD2 1 
ATOM   15616 C  CE1 . TYR   E 2 587 ? 42.557  -2.709  -4.452  1.00 92.41  ? 891  TYR   E CE1 1 
ATOM   15617 C  CE2 . TYR   E 2 587 ? 41.584  -3.653  -6.419  1.00 85.83  ? 891  TYR   E CE2 1 
ATOM   15618 C  CZ  . TYR   E 2 587 ? 42.480  -3.735  -5.384  1.00 89.87  ? 891  TYR   E CZ  1 
ATOM   15619 O  OH  . TYR   E 2 587 ? 43.273  -4.856  -5.282  1.00 89.57  ? 891  TYR   E OH  1 
ATOM   15620 N  N   . GLU   E 2 588 ? 39.515  2.326   -4.124  1.00 97.89  ? 892  GLU   E N   1 
ATOM   15621 C  CA  . GLU   E 2 588 ? 39.414  3.783   -4.028  1.00 95.64  ? 892  GLU   E CA  1 
ATOM   15622 C  C   . GLU   E 2 588 ? 40.685  4.468   -4.502  1.00 94.65  ? 892  GLU   E C   1 
ATOM   15623 O  O   . GLU   E 2 588 ? 41.799  3.984   -4.259  1.00 94.37  ? 892  GLU   E O   1 
ATOM   15624 C  CB  . GLU   E 2 588 ? 39.169  4.242   -2.609  1.00 94.26  ? 892  GLU   E CB  1 
ATOM   15625 C  CG  . GLU   E 2 588 ? 37.738  4.484   -2.268  1.00 98.58  ? 892  GLU   E CG  1 
ATOM   15626 C  CD  . GLU   E 2 588 ? 37.542  4.396   -0.776  1.00 110.45 ? 892  GLU   E CD  1 
ATOM   15627 O  OE1 . GLU   E 2 588 ? 36.367  4.363   -0.333  1.00 122.74 ? 892  GLU   E OE1 1 
ATOM   15628 O  OE2 . GLU   E 2 588 ? 38.557  4.361   -0.047  1.00 120.71 ? 892  GLU   E OE2 1 
ATOM   15629 N  N   . TRP   E 2 589 ? 40.503  5.632   -5.133  1.00 96.35  ? 893  TRP   E N   1 
ATOM   15630 C  CA  . TRP   E 2 589 ? 41.612  6.432   -5.653  1.00 103.87 ? 893  TRP   E CA  1 
ATOM   15631 C  C   . TRP   E 2 589 ? 42.023  7.445   -4.581  1.00 107.40 ? 893  TRP   E C   1 
ATOM   15632 O  O   . TRP   E 2 589 ? 41.272  8.382   -4.282  1.00 104.41 ? 893  TRP   E O   1 
ATOM   15633 C  CB  . TRP   E 2 589 ? 41.209  7.122   -6.957  1.00 100.72 ? 893  TRP   E CB  1 
ATOM   15634 C  CG  . TRP   E 2 589 ? 42.373  7.536   -7.857  1.00 100.59 ? 893  TRP   E CG  1 
ATOM   15635 C  CD1 . TRP   E 2 589 ? 42.493  8.713   -8.531  1.00 102.79 ? 893  TRP   E CD1 1 
ATOM   15636 C  CD2 . TRP   E 2 589 ? 43.555  6.777   -8.176  1.00 100.53 ? 893  TRP   E CD2 1 
ATOM   15637 N  NE1 . TRP   E 2 589 ? 43.672  8.744   -9.244  1.00 98.77  ? 893  TRP   E NE1 1 
ATOM   15638 C  CE2 . TRP   E 2 589 ? 44.341  7.568   -9.044  1.00 100.41 ? 893  TRP   E CE2 1 
ATOM   15639 C  CE3 . TRP   E 2 589 ? 44.023  5.509   -7.820  1.00 103.06 ? 893  TRP   E CE3 1 
ATOM   15640 C  CZ2 . TRP   E 2 589 ? 45.566  7.132   -9.556  1.00 102.65 ? 893  TRP   E CZ2 1 
ATOM   15641 C  CZ3 . TRP   E 2 589 ? 45.248  5.078   -8.333  1.00 104.34 ? 893  TRP   E CZ3 1 
ATOM   15642 C  CH2 . TRP   E 2 589 ? 46.000  5.887   -9.187  1.00 101.72 ? 893  TRP   E CH2 1 
ATOM   15643 N  N   . THR   E 2 590 ? 43.211  7.251   -4.004  1.00 107.67 ? 894  THR   E N   1 
ATOM   15644 C  CA  . THR   E 2 590 ? 43.729  8.101   -2.941  1.00 112.64 ? 894  THR   E CA  1 
ATOM   15645 C  C   . THR   E 2 590 ? 44.303  9.398   -3.513  1.00 120.51 ? 894  THR   E C   1 
ATOM   15646 O  O   . THR   E 2 590 ? 44.591  9.512   -4.715  1.00 115.42 ? 894  THR   E O   1 
ATOM   15647 C  CB  . THR   E 2 590 ? 44.818  7.395   -2.117  1.00 115.91 ? 894  THR   E CB  1 
ATOM   15648 O  OG1 . THR   E 2 590 ? 46.019  7.227   -2.892  1.00 115.99 ? 894  THR   E OG1 1 
ATOM   15649 C  CG2 . THR   E 2 590 ? 44.324  6.056   -1.578  1.00 104.75 ? 894  THR   E CG2 1 
ATOM   15650 N  N   . THR   E 2 591 ? 44.454  10.382  -2.619  1.00 122.81 ? 895  THR   E N   1 
ATOM   15651 C  CA  . THR   E 2 591 ? 45.075  11.637  -2.999  1.00 124.24 ? 895  THR   E CA  1 
ATOM   15652 C  C   . THR   E 2 591 ? 46.549  11.461  -3.331  1.00 122.51 ? 895  THR   E C   1 
ATOM   15653 O  O   . THR   E 2 591 ? 47.099  12.301  -4.036  1.00 124.42 ? 895  THR   E O   1 
ATOM   15654 C  CB  . THR   E 2 591 ? 44.932  12.694  -1.905  1.00 127.65 ? 895  THR   E CB  1 
ATOM   15655 O  OG1 . THR   E 2 591 ? 45.537  12.225  -0.690  1.00 135.56 ? 895  THR   E OG1 1 
ATOM   15656 C  CG2 . THR   E 2 591 ? 43.472  12.962  -1.664  1.00 124.27 ? 895  THR   E CG2 1 
ATOM   15657 N  N   . GLU   E 2 592 ? 47.184  10.401  -2.834  1.00 118.28 ? 896  GLU   E N   1 
ATOM   15658 C  CA  . GLU   E 2 592 ? 48.542  10.058  -3.223  1.00 116.96 ? 896  GLU   E CA  1 
ATOM   15659 C  C   . GLU   E 2 592 ? 48.565  9.127   -4.458  1.00 120.57 ? 896  GLU   E C   1 
ATOM   15660 O  O   . GLU   E 2 592 ? 49.557  8.405   -4.666  1.00 121.02 ? 896  GLU   E O   1 
ATOM   15661 C  CB  . GLU   E 2 592 ? 49.286  9.421   -2.037  1.00 113.50 ? 896  GLU   E CB  1 
ATOM   15662 N  N   . LYS   E 2 593 ? 47.485  9.111   -5.246  1.00 116.86 ? 897  LYS   E N   1 
ATOM   15663 C  CA  . LYS   E 2 593 ? 47.403  8.415   -6.543  1.00 110.26 ? 897  LYS   E CA  1 
ATOM   15664 C  C   . LYS   E 2 593 ? 47.823  6.941   -6.453  1.00 116.33 ? 897  LYS   E C   1 
ATOM   15665 O  O   . LYS   E 2 593 ? 48.706  6.462   -7.170  1.00 116.70 ? 897  LYS   E O   1 
ATOM   15666 C  CB  . LYS   E 2 593 ? 48.207  9.168   -7.605  1.00 101.47 ? 897  LYS   E CB  1 
ATOM   15667 N  N   . GLU   E 2 594 ? 47.139  6.210   -5.576  1.00 120.18 ? 898  GLU   E N   1 
ATOM   15668 C  CA  . GLU   E 2 594 ? 47.277  4.760   -5.481  1.00 117.86 ? 898  GLU   E CA  1 
ATOM   15669 C  C   . GLU   E 2 594 ? 45.880  4.156   -5.292  1.00 116.38 ? 898  GLU   E C   1 
ATOM   15670 O  O   . GLU   E 2 594 ? 44.875  4.868   -5.217  1.00 116.52 ? 898  GLU   E O   1 
ATOM   15671 C  CB  . GLU   E 2 594 ? 48.232  4.361   -4.340  1.00 117.95 ? 898  GLU   E CB  1 
ATOM   15672 C  CG  . GLU   E 2 594 ? 47.589  4.379   -2.946  1.00 123.37 ? 898  GLU   E CG  1 
ATOM   15673 C  CD  . GLU   E 2 594 ? 48.596  4.441   -1.790  1.00 130.92 ? 898  GLU   E CD  1 
ATOM   15674 O  OE1 . GLU   E 2 594 ? 48.419  5.307   -0.894  1.00 128.69 ? 898  GLU   E OE1 1 
ATOM   15675 O  OE2 . GLU   E 2 594 ? 49.547  3.619   -1.773  1.00 137.41 ? 898  GLU   E OE2 1 
ATOM   15676 N  N   . LEU   E 2 595 ? 45.808  2.832   -5.230  1.00 107.97 ? 899  LEU   E N   1 
ATOM   15677 C  CA  . LEU   E 2 595 ? 44.535  2.138   -5.062  1.00 102.91 ? 899  LEU   E CA  1 
ATOM   15678 C  C   . LEU   E 2 595 ? 44.466  1.541   -3.658  1.00 100.61 ? 899  LEU   E C   1 
ATOM   15679 O  O   . LEU   E 2 595 ? 45.367  0.791   -3.259  1.00 97.79  ? 899  LEU   E O   1 
ATOM   15680 C  CB  . LEU   E 2 595 ? 44.378  1.044   -6.120  1.00 102.79 ? 899  LEU   E CB  1 
ATOM   15681 C  CG  . LEU   E 2 595 ? 43.868  1.432   -7.513  1.00 95.60  ? 899  LEU   E CG  1 
ATOM   15682 C  CD1 . LEU   E 2 595 ? 44.232  0.337   -8.503  1.00 91.57  ? 899  LEU   E CD1 1 
ATOM   15683 C  CD2 . LEU   E 2 595 ? 42.362  1.651   -7.504  1.00 92.85  ? 899  LEU   E CD2 1 
ATOM   15684 N  N   . ARG   E 2 596 ? 43.405  1.877   -2.916  1.00 99.18  ? 900  ARG   E N   1 
ATOM   15685 C  CA  . ARG   E 2 596 ? 43.188  1.395   -1.552  1.00 98.77  ? 900  ARG   E CA  1 
ATOM   15686 C  C   . ARG   E 2 596 ? 41.896  0.595   -1.498  1.00 97.73  ? 900  ARG   E C   1 
ATOM   15687 O  O   . ARG   E 2 596 ? 40.854  1.067   -1.968  1.00 97.60  ? 900  ARG   E O   1 
ATOM   15688 C  CB  . ARG   E 2 596 ? 43.123  2.550   -0.534  1.00 94.94  ? 900  ARG   E CB  1 
ATOM   15689 N  N   . THR   E 2 597 ? 41.953  -0.596  -0.899  1.00 92.97  ? 901  THR   E N   1 
ATOM   15690 C  CA  . THR   E 2 597 ? 40.769  -1.450  -0.838  1.00 91.23  ? 901  THR   E CA  1 
ATOM   15691 C  C   . THR   E 2 597 ? 39.711  -0.885  0.107   1.00 89.92  ? 901  THR   E C   1 
ATOM   15692 O  O   . THR   E 2 597 ? 40.004  -0.601  1.271   1.00 98.46  ? 901  THR   E O   1 
ATOM   15693 C  CB  . THR   E 2 597 ? 41.161  -2.840  -0.383  1.00 91.14  ? 901  THR   E CB  1 
ATOM   15694 O  OG1 . THR   E 2 597 ? 42.378  -3.225  -1.045  1.00 92.41  ? 901  THR   E OG1 1 
ATOM   15695 C  CG2 . THR   E 2 597 ? 40.023  -3.802  -0.699  1.00 89.87  ? 901  THR   E CG2 1 
ATOM   15696 N  N   . GLU   E 2 598 ? 38.471  -0.740  -0.387  1.00 90.03  ? 902  GLU   E N   1 
ATOM   15697 C  CA  . GLU   E 2 598 ? 37.359  -0.247  0.444   1.00 95.84  ? 902  GLU   E CA  1 
ATOM   15698 C  C   . GLU   E 2 598 ? 36.674  -1.404  1.175   1.00 98.30  ? 902  GLU   E C   1 
ATOM   15699 O  O   . GLU   E 2 598 ? 36.786  -1.519  2.398   1.00 101.36 ? 902  GLU   E O   1 
ATOM   15700 C  CB  . GLU   E 2 598 ? 36.364  0.573   -0.388  1.00 95.16  ? 902  GLU   E CB  1 
ATOM   15701 N  N   . CYS   E 2 599 ? 35.961  -2.273  0.452   1.00 99.12  ? 903  CYS   E N   1 
ATOM   15702 C  CA  . CYS   E 2 599 ? 35.430  -3.503  1.046   1.00 98.68  ? 903  CYS   E CA  1 
ATOM   15703 C  C   . CYS   E 2 599 ? 35.726  -4.699  0.151   1.00 98.12  ? 903  CYS   E C   1 
ATOM   15704 O  O   . CYS   E 2 599 ? 36.220  -4.562  -0.974  1.00 94.76  ? 903  CYS   E O   1 
ATOM   15705 C  CB  . CYS   E 2 599 ? 33.925  -3.405  1.297   1.00 103.23 ? 903  CYS   E CB  1 
ATOM   15706 S  SG  . CYS   E 2 599 ? 33.116  -2.441  0.017   1.00 97.88  ? 903  CYS   E SG  1 
ATOM   15707 N  N   . ASN   E 2 600 ? 35.423  -5.888  0.677   1.00 102.55 ? 904  ASN   E N   1 
ATOM   15708 C  CA  . ASN   E 2 600 ? 35.618  -7.146  -0.035  1.00 96.06  ? 904  ASN   E CA  1 
ATOM   15709 C  C   . ASN   E 2 600 ? 34.392  -8.018  0.143   1.00 96.37  ? 904  ASN   E C   1 
ATOM   15710 O  O   . ASN   E 2 600 ? 33.832  -8.104  1.245   1.00 102.37 ? 904  ASN   E O   1 
ATOM   15711 C  CB  . ASN   E 2 600 ? 36.848  -7.924  0.465   1.00 95.88  ? 904  ASN   E CB  1 
ATOM   15712 C  CG  . ASN   E 2 600 ? 38.031  -7.836  -0.488  1.00 95.44  ? 904  ASN   E CG  1 
ATOM   15713 O  OD1 . ASN   E 2 600 ? 38.055  -6.995  -1.389  1.00 97.19  ? 904  ASN   E OD1 1 
ATOM   15714 N  ND2 . ASN   E 2 600 ? 39.026  -8.700  -0.287  1.00 94.35  ? 904  ASN   E ND2 1 
ATOM   15715 N  N   . HIS   E 2 601 ? 33.991  -8.674  -0.944  1.00 96.09  ? 905  HIS   E N   1 
ATOM   15716 C  CA  . HIS   E 2 601 ? 32.965  -9.709  -0.899  1.00 97.70  ? 905  HIS   E CA  1 
ATOM   15717 C  C   . HIS   E 2 601 ? 33.511  -10.974 -1.548  1.00 98.06  ? 905  HIS   E C   1 
ATOM   15718 O  O   . HIS   E 2 601 ? 33.916  -10.955 -2.719  1.00 95.97  ? 905  HIS   E O   1 
ATOM   15719 C  CB  . HIS   E 2 601 ? 31.681  -9.266  -1.590  1.00 88.78  ? 905  HIS   E CB  1 
ATOM   15720 C  CG  . HIS   E 2 601 ? 30.525  -10.149 -1.271  1.00 93.72  ? 905  HIS   E CG  1 
ATOM   15721 N  ND1 . HIS   E 2 601 ? 30.578  -11.520 -1.429  1.00 97.85  ? 905  HIS   E ND1 1 
ATOM   15722 C  CD2 . HIS   E 2 601 ? 29.302  -9.873  -0.763  1.00 95.88  ? 905  HIS   E CD2 1 
ATOM   15723 C  CE1 . HIS   E 2 601 ? 29.427  -12.048 -1.053  1.00 99.99  ? 905  HIS   E CE1 1 
ATOM   15724 N  NE2 . HIS   E 2 601 ? 28.637  -11.071 -0.642  1.00 103.24 ? 905  HIS   E NE2 1 
ATOM   15725 N  N   . TYR   E 2 602 ? 33.523  -12.068 -0.792  1.00 98.27  ? 906  TYR   E N   1 
ATOM   15726 C  CA  . TYR   E 2 602 ? 34.101  -13.323 -1.256  1.00 97.38  ? 906  TYR   E CA  1 
ATOM   15727 C  C   . TYR   E 2 602 ? 32.998  -14.272 -1.699  1.00 93.90  ? 906  TYR   E C   1 
ATOM   15728 O  O   . TYR   E 2 602 ? 32.024  -14.487 -0.973  1.00 96.88  ? 906  TYR   E O   1 
ATOM   15729 C  CB  . TYR   E 2 602 ? 34.938  -13.953 -0.154  1.00 98.04  ? 906  TYR   E CB  1 
ATOM   15730 C  CG  . TYR   E 2 602 ? 36.097  -13.091 0.274   1.00 101.40 ? 906  TYR   E CG  1 
ATOM   15731 C  CD1 . TYR   E 2 602 ? 35.911  -11.992 1.117   1.00 100.54 ? 906  TYR   E CD1 1 
ATOM   15732 C  CD2 . TYR   E 2 602 ? 37.392  -13.384 -0.153  1.00 106.17 ? 906  TYR   E CD2 1 
ATOM   15733 C  CE1 . TYR   E 2 602 ? 36.990  -11.211 1.524   1.00 99.62  ? 906  TYR   E CE1 1 
ATOM   15734 C  CE2 . TYR   E 2 602 ? 38.468  -12.623 0.248   1.00 103.88 ? 906  TYR   E CE2 1 
ATOM   15735 C  CZ  . TYR   E 2 602 ? 38.264  -11.537 1.085   1.00 103.79 ? 906  TYR   E CZ  1 
ATOM   15736 O  OH  . TYR   E 2 602 ? 39.346  -10.782 1.470   1.00 103.20 ? 906  TYR   E OH  1 
ATOM   15737 N  N   . ASN   E 2 603 ? 33.144  -14.832 -2.888  1.00 91.25  ? 907  ASN   E N   1 
ATOM   15738 C  CA  . ASN   E 2 603 ? 32.046  -15.554 -3.511  1.00 93.71  ? 907  ASN   E CA  1 
ATOM   15739 C  C   . ASN   E 2 603 ? 32.373  -17.037 -3.648  1.00 98.35  ? 907  ASN   E C   1 
ATOM   15740 O  O   . ASN   E 2 603 ? 33.544  -17.434 -3.700  1.00 101.36 ? 907  ASN   E O   1 
ATOM   15741 C  CB  . ASN   E 2 603 ? 31.734  -14.940 -4.870  1.00 93.72  ? 907  ASN   E CB  1 
ATOM   15742 C  CG  . ASN   E 2 603 ? 31.554  -13.428 -4.787  1.00 96.27  ? 907  ASN   E CG  1 
ATOM   15743 O  OD1 . ASN   E 2 603 ? 32.449  -12.654 -5.159  1.00 93.96  ? 907  ASN   E OD1 1 
ATOM   15744 N  ND2 . ASN   E 2 603 ? 30.404  -13.000 -4.261  1.00 91.35  ? 907  ASN   E ND2 1 
ATOM   15745 N  N   . ASN   E 2 604 ? 31.321  -17.868 -3.670  1.00 97.24  ? 908  ASN   E N   1 
ATOM   15746 C  CA  . ASN   E 2 604 ? 31.482  -19.301 -3.907  1.00 94.56  ? 908  ASN   E CA  1 
ATOM   15747 C  C   . ASN   E 2 604 ? 31.379  -19.658 -5.377  1.00 94.28  ? 908  ASN   E C   1 
ATOM   15748 O  O   . ASN   E 2 604 ? 31.371  -20.847 -5.712  1.00 95.99  ? 908  ASN   E O   1 
ATOM   15749 C  CB  . ASN   E 2 604 ? 30.456  -20.114 -3.112  1.00 93.06  ? 908  ASN   E CB  1 
ATOM   15750 C  CG  . ASN   E 2 604 ? 29.039  -19.978 -3.649  1.00 98.04  ? 908  ASN   E CG  1 
ATOM   15751 O  OD1 . ASN   E 2 604 ? 28.702  -19.011 -4.324  1.00 101.61 ? 908  ASN   E OD1 1 
ATOM   15752 N  ND2 . ASN   E 2 604 ? 28.192  -20.949 -3.325  1.00 101.68 ? 908  ASN   E ND2 1 
ATOM   15753 N  N   . ILE   E 2 605 ? 31.253  -18.660 -6.244  1.00 92.59  ? 909  ILE   E N   1 
ATOM   15754 C  CA  . ILE   E 2 605 ? 31.485  -18.796 -7.670  1.00 89.34  ? 909  ILE   E CA  1 
ATOM   15755 C  C   . ILE   E 2 605 ? 32.631  -17.859 -8.008  1.00 92.71  ? 909  ILE   E C   1 
ATOM   15756 O  O   . ILE   E 2 605 ? 32.981  -16.959 -7.239  1.00 95.74  ? 909  ILE   E O   1 
ATOM   15757 C  CB  . ILE   E 2 605 ? 30.251  -18.470 -8.518  1.00 88.98  ? 909  ILE   E CB  1 
ATOM   15758 C  CG1 . ILE   E 2 605 ? 30.011  -16.960 -8.556  1.00 87.35  ? 909  ILE   E CG1 1 
ATOM   15759 C  CG2 . ILE   E 2 605 ? 29.030  -19.153 -7.932  1.00 93.28  ? 909  ILE   E CG2 1 
ATOM   15760 C  CD1 . ILE   E 2 605 ? 28.726  -16.576 -9.277  1.00 84.88  ? 909  ILE   E CD1 1 
ATOM   15761 N  N   . MET   E 2 606 ? 33.256  -18.114 -9.144  1.00 93.59  ? 910  MET   E N   1 
ATOM   15762 C  CA  . MET   E 2 606 ? 34.348  -17.281 -9.605  1.00 82.52  ? 910  MET   E CA  1 
ATOM   15763 C  C   . MET   E 2 606 ? 33.706  -16.203 -10.452 1.00 85.10  ? 910  MET   E C   1 
ATOM   15764 O  O   . MET   E 2 606 ? 32.858  -16.506 -11.289 1.00 88.98  ? 910  MET   E O   1 
ATOM   15765 C  CB  . MET   E 2 606 ? 35.372  -18.123 -10.370 1.00 87.64  ? 910  MET   E CB  1 
ATOM   15766 C  CG  . MET   E 2 606 ? 34.909  -18.708 -11.691 1.00 90.60  ? 910  MET   E CG  1 
ATOM   15767 S  SD  . MET   E 2 606 ? 36.302  -19.529 -12.549 1.00 103.62 ? 910  MET   E SD  1 
ATOM   15768 C  CE  . MET   E 2 606 ? 37.186  -18.118 -13.234 1.00 92.90  ? 910  MET   E CE  1 
ATOM   15769 N  N   . ALA   E 2 607 ? 34.026  -14.944 -10.170 1.00 91.79  ? 911  ALA   E N   1 
ATOM   15770 C  CA  . ALA   E 2 607 ? 33.272  -13.806 -10.705 1.00 87.76  ? 911  ALA   E CA  1 
ATOM   15771 C  C   . ALA   E 2 607 ? 33.817  -13.407 -12.072 1.00 86.17  ? 911  ALA   E C   1 
ATOM   15772 O  O   . ALA   E 2 607 ? 34.720  -12.575 -12.186 1.00 87.66  ? 911  ALA   E O   1 
ATOM   15773 C  CB  . ALA   E 2 607 ? 33.322  -12.635 -9.728  1.00 85.01  ? 911  ALA   E CB  1 
ATOM   15774 N  N   . LEU   E 2 608 ? 33.235  -13.983 -13.132 1.00 86.90  ? 912  LEU   E N   1 
ATOM   15775 C  CA  . LEU   E 2 608 ? 33.647  -13.648 -14.496 1.00 89.62  ? 912  LEU   E CA  1 
ATOM   15776 C  C   . LEU   E 2 608 ? 32.948  -12.418 -15.040 1.00 90.28  ? 912  LEU   E C   1 
ATOM   15777 O  O   . LEU   E 2 608 ? 33.561  -11.615 -15.768 1.00 91.36  ? 912  LEU   E O   1 
ATOM   15778 C  CB  . LEU   E 2 608 ? 33.387  -14.810 -15.451 1.00 87.47  ? 912  LEU   E CB  1 
ATOM   15779 C  CG  . LEU   E 2 608 ? 34.721  -15.523 -15.602 1.00 90.41  ? 912  LEU   E CG  1 
ATOM   15780 C  CD1 . LEU   E 2 608 ? 34.847  -16.437 -14.399 1.00 92.71  ? 912  LEU   E CD1 1 
ATOM   15781 C  CD2 . LEU   E 2 608 ? 34.873  -16.261 -16.930 1.00 89.68  ? 912  LEU   E CD2 1 
ATOM   15782 N  N   . TYR   E 2 609 ? 31.671  -12.278 -14.712 1.00 86.63  ? 913  TYR   E N   1 
ATOM   15783 C  CA  . TYR   E 2 609 ? 30.827  -11.212 -15.220 1.00 87.28  ? 913  TYR   E CA  1 
ATOM   15784 C  C   . TYR   E 2 609 ? 30.566  -10.222 -14.093 1.00 90.35  ? 913  TYR   E C   1 
ATOM   15785 O  O   . TYR   E 2 609 ? 30.188  -10.622 -12.981 1.00 89.63  ? 913  TYR   E O   1 
ATOM   15786 C  CB  . TYR   E 2 609 ? 29.533  -11.793 -15.779 1.00 83.45  ? 913  TYR   E CB  1 
ATOM   15787 C  CG  . TYR   E 2 609 ? 29.810  -12.764 -16.893 1.00 82.36  ? 913  TYR   E CG  1 
ATOM   15788 C  CD1 . TYR   E 2 609 ? 30.523  -12.364 -18.011 1.00 83.75  ? 913  TYR   E CD1 1 
ATOM   15789 C  CD2 . TYR   E 2 609 ? 29.372  -14.087 -16.831 1.00 83.83  ? 913  TYR   E CD2 1 
ATOM   15790 C  CE1 . TYR   E 2 609 ? 30.796  -13.240 -19.055 1.00 81.24  ? 913  TYR   E CE1 1 
ATOM   15791 C  CE2 . TYR   E 2 609 ? 29.637  -14.978 -17.876 1.00 83.90  ? 913  TYR   E CE2 1 
ATOM   15792 C  CZ  . TYR   E 2 609 ? 30.352  -14.543 -18.990 1.00 82.33  ? 913  TYR   E CZ  1 
ATOM   15793 O  OH  . TYR   E 2 609 ? 30.620  -15.413 -20.030 1.00 82.27  ? 913  TYR   E OH  1 
ATOM   15794 N  N   . LEU   E 2 610 ? 30.809  -8.938  -14.363 1.00 85.79  ? 914  LEU   E N   1 
ATOM   15795 C  CA  . LEU   E 2 610 ? 30.586  -7.902  -13.372 1.00 83.59  ? 914  LEU   E CA  1 
ATOM   15796 C  C   . LEU   E 2 610 ? 29.825  -6.780  -14.063 1.00 84.80  ? 914  LEU   E C   1 
ATOM   15797 O  O   . LEU   E 2 610 ? 30.299  -6.207  -15.051 1.00 85.27  ? 914  LEU   E O   1 
ATOM   15798 C  CB  . LEU   E 2 610 ? 31.907  -7.422  -12.779 1.00 85.58  ? 914  LEU   E CB  1 
ATOM   15799 C  CG  . LEU   E 2 610 ? 31.874  -7.027  -11.308 1.00 84.11  ? 914  LEU   E CG  1 
ATOM   15800 C  CD1 . LEU   E 2 610 ? 31.371  -8.180  -10.480 1.00 83.98  ? 914  LEU   E CD1 1 
ATOM   15801 C  CD2 . LEU   E 2 610 ? 33.266  -6.628  -10.878 1.00 88.46  ? 914  LEU   E CD2 1 
ATOM   15802 N  N   . LYS   E 2 611 ? 28.618  -6.512  -13.593 1.00 82.76  ? 915  LYS   E N   1 
ATOM   15803 C  CA  . LYS   E 2 611 ? 27.798  -5.456  -14.163 1.00 84.56  ? 915  LYS   E CA  1 
ATOM   15804 C  C   . LYS   E 2 611 ? 27.138  -4.706  -13.018 1.00 89.33  ? 915  LYS   E C   1 
ATOM   15805 O  O   . LYS   E 2 611 ? 26.657  -5.333  -12.064 1.00 86.12  ? 915  LYS   E O   1 
ATOM   15806 C  CB  . LYS   E 2 611 ? 26.742  -6.014  -15.122 1.00 79.57  ? 915  LYS   E CB  1 
ATOM   15807 C  CG  . LYS   E 2 611 ? 27.297  -6.751  -16.329 1.00 81.26  ? 915  LYS   E CG  1 
ATOM   15808 C  CD  . LYS   E 2 611 ? 28.148  -5.867  -17.237 1.00 80.39  ? 915  LYS   E CD  1 
ATOM   15809 C  CE  . LYS   E 2 611 ? 28.374  -6.471  -18.639 1.00 78.72  ? 915  LYS   E CE  1 
ATOM   15810 N  NZ  . LYS   E 2 611 ? 27.373  -6.099  -19.706 1.00 83.30  ? 915  LYS   E NZ  1 
ATOM   15811 N  N   . THR   E 2 612 ? 27.106  -3.363  -13.128 1.00 89.38  ? 916  THR   E N   1 
ATOM   15812 C  CA  . THR   E 2 612 ? 26.597  -2.502  -12.066 1.00 85.48  ? 916  THR   E CA  1 
ATOM   15813 C  C   . THR   E 2 612 ? 25.545  -1.533  -12.603 1.00 82.21  ? 916  THR   E C   1 
ATOM   15814 O  O   . THR   E 2 612 ? 25.635  -1.040  -13.731 1.00 82.06  ? 916  THR   E O   1 
ATOM   15815 C  CB  . THR   E 2 612 ? 27.730  -1.725  -11.405 1.00 84.61  ? 916  THR   E CB  1 
ATOM   15816 O  OG1 . THR   E 2 612 ? 28.095  -0.637  -12.247 1.00 93.28  ? 916  THR   E OG1 1 
ATOM   15817 C  CG2 . THR   E 2 612 ? 28.964  -2.606  -11.235 1.00 85.75  ? 916  THR   E CG2 1 
ATOM   15818 N  N   . LYS   E 2 613 ? 24.540  -1.265  -11.776 1.00 81.61  ? 917  LYS   E N   1 
ATOM   15819 C  CA  . LYS   E 2 613 ? 23.502  -0.269  -12.034 1.00 78.36  ? 917  LYS   E CA  1 
ATOM   15820 C  C   . LYS   E 2 613 ? 23.351  0.470   -10.709 1.00 99.29  ? 917  LYS   E C   1 
ATOM   15821 O  O   . LYS   E 2 613 ? 22.617  0.015   -9.820  1.00 99.29  ? 917  LYS   E O   1 
ATOM   15822 C  CB  . LYS   E 2 613 ? 22.198  -0.878  -12.475 1.00 80.41  ? 917  LYS   E CB  1 
ATOM   15823 C  CG  . LYS   E 2 613 ? 21.223  0.064   -13.138 1.00 77.68  ? 917  LYS   E CG  1 
ATOM   15824 C  CD  . LYS   E 2 613 ? 21.722  0.367   -14.545 1.00 96.56  ? 917  LYS   E CD  1 
ATOM   15825 C  CE  . LYS   E 2 613 ? 22.149  -0.931  -15.291 1.00 93.94  ? 917  LYS   E CE  1 
ATOM   15826 N  NZ  . LYS   E 2 613 ? 23.454  -0.829  -16.059 1.00 91.33  ? 917  LYS   E NZ  1 
ATOM   15827 N  N   . GLY   E 2 614 ? 24.063  1.601   -10.582 1.00 102.46 ? 918  GLY   E N   1 
ATOM   15828 C  CA  . GLY   E 2 614 ? 24.071  2.387   -9.361  1.00 103.83 ? 918  GLY   E CA  1 
ATOM   15829 C  C   . GLY   E 2 614 ? 24.773  1.680   -8.225  1.00 106.09 ? 918  GLY   E C   1 
ATOM   15830 O  O   . GLY   E 2 614 ? 25.987  1.479   -8.273  1.00 105.73 ? 918  GLY   E O   1 
ATOM   15831 N  N   . ASP   E 2 615 ? 24.020  1.318   -7.191  1.00 112.76 ? 919  ASP   E N   1 
ATOM   15832 C  CA  . ASP   E 2 615 ? 24.564  0.589   -6.052  1.00 112.67 ? 919  ASP   E CA  1 
ATOM   15833 C  C   . ASP   E 2 615 ? 24.455  -0.919  -6.209  1.00 110.67 ? 919  ASP   E C   1 
ATOM   15834 O  O   . ASP   E 2 615 ? 25.115  -1.652  -5.460  1.00 110.29 ? 919  ASP   E O   1 
ATOM   15835 C  CB  . ASP   E 2 615 ? 23.835  1.001   -4.768  1.00 119.53 ? 919  ASP   E CB  1 
ATOM   15836 C  CG  . ASP   E 2 615 ? 22.336  0.653   -4.804  1.00 125.07 ? 919  ASP   E CG  1 
ATOM   15837 O  OD1 . ASP   E 2 615 ? 21.774  0.524   -5.923  1.00 121.33 ? 919  ASP   E OD1 1 
ATOM   15838 O  OD2 . ASP   E 2 615 ? 21.727  0.502   -3.711  1.00 130.26 ? 919  ASP   E OD2 1 
ATOM   15839 N  N   . PHE   E 2 616 ? 23.625  -1.391  -7.142  1.00 107.30 ? 920  PHE   E N   1 
ATOM   15840 C  CA  . PHE   E 2 616 ? 23.453  -2.816  -7.395  1.00 99.05  ? 920  PHE   E CA  1 
ATOM   15841 C  C   . PHE   E 2 616 ? 24.621  -3.360  -8.219  1.00 98.58  ? 920  PHE   E C   1 
ATOM   15842 O  O   . PHE   E 2 616 ? 25.117  -2.689  -9.137  1.00 94.64  ? 920  PHE   E O   1 
ATOM   15843 C  CB  . PHE   E 2 616 ? 22.136  -3.054  -8.132  1.00 97.01  ? 920  PHE   E CB  1 
ATOM   15844 C  CG  . PHE   E 2 616 ? 20.915  -2.964  -7.251  1.00 105.70 ? 920  PHE   E CG  1 
ATOM   15845 C  CD1 . PHE   E 2 616 ? 21.027  -3.021  -5.867  1.00 104.60 ? 920  PHE   E CD1 1 
ATOM   15846 C  CD2 . PHE   E 2 616 ? 19.642  -2.842  -7.818  1.00 106.94 ? 920  PHE   E CD2 1 
ATOM   15847 C  CE1 . PHE   E 2 616 ? 19.901  -2.950  -5.060  1.00 104.40 ? 920  PHE   E CE1 1 
ATOM   15848 C  CE2 . PHE   E 2 616 ? 18.507  -2.773  -7.018  1.00 103.66 ? 920  PHE   E CE2 1 
ATOM   15849 C  CZ  . PHE   E 2 616 ? 18.636  -2.826  -5.638  1.00 107.64 ? 920  PHE   E CZ  1 
ATOM   15850 N  N   . ILE   E 2 617 ? 25.056  -4.589  -7.893  1.00 95.72  ? 921  ILE   E N   1 
ATOM   15851 C  CA  . ILE   E 2 617 ? 26.166  -5.256  -8.581  1.00 90.11  ? 921  ILE   E CA  1 
ATOM   15852 C  C   . ILE   E 2 617 ? 25.727  -6.647  -9.046  1.00 87.52  ? 921  ILE   E C   1 
ATOM   15853 O  O   . ILE   E 2 617 ? 25.132  -7.409  -8.273  1.00 91.34  ? 921  ILE   E O   1 
ATOM   15854 C  CB  . ILE   E 2 617 ? 27.407  -5.357  -7.674  1.00 90.75  ? 921  ILE   E CB  1 
ATOM   15855 C  CG1 . ILE   E 2 617 ? 27.770  -3.983  -7.119  1.00 93.09  ? 921  ILE   E CG1 1 
ATOM   15856 C  CG2 . ILE   E 2 617 ? 28.601  -5.841  -8.456  1.00 89.35  ? 921  ILE   E CG2 1 
ATOM   15857 C  CD1 . ILE   E 2 617 ? 28.622  -4.052  -5.872  1.00 94.03  ? 921  ILE   E CD1 1 
ATOM   15858 N  N   . LEU   E 2 618 ? 26.032  -6.988  -10.300 1.00 86.24  ? 922  LEU   E N   1 
ATOM   15859 C  CA  . LEU   E 2 618 ? 25.700  -8.296  -10.870 1.00 87.21  ? 922  LEU   E CA  1 
ATOM   15860 C  C   . LEU   E 2 618 ? 26.965  -9.136  -11.084 1.00 80.56  ? 922  LEU   E C   1 
ATOM   15861 O  O   . LEU   E 2 618 ? 27.896  -8.696  -11.760 1.00 84.84  ? 922  LEU   E O   1 
ATOM   15862 C  CB  . LEU   E 2 618 ? 24.944  -8.118  -12.187 1.00 82.24  ? 922  LEU   E CB  1 
ATOM   15863 C  CG  . LEU   E 2 618 ? 24.330  -9.416  -12.697 1.00 86.00  ? 922  LEU   E CG  1 
ATOM   15864 C  CD1 . LEU   E 2 618 ? 23.562  -10.108 -11.576 1.00 87.31  ? 922  LEU   E CD1 1 
ATOM   15865 C  CD2 . LEU   E 2 618 ? 23.427  -9.128  -13.874 1.00 86.25  ? 922  LEU   E CD2 1 
ATOM   15866 N  N   . VAL   E 2 619 ? 26.996  -10.348 -10.535 1.00 80.63  ? 923  VAL   E N   1 
ATOM   15867 C  CA  . VAL   E 2 619 ? 28.144  -11.244 -10.677 1.00 86.29  ? 923  VAL   E CA  1 
ATOM   15868 C  C   . VAL   E 2 619 ? 27.719  -12.557 -11.338 1.00 86.39  ? 923  VAL   E C   1 
ATOM   15869 O  O   . VAL   E 2 619 ? 26.672  -13.124 -11.005 1.00 88.73  ? 923  VAL   E O   1 
ATOM   15870 C  CB  . VAL   E 2 619 ? 28.805  -11.527 -9.312  1.00 86.76  ? 923  VAL   E CB  1 
ATOM   15871 C  CG1 . VAL   E 2 619 ? 30.089  -12.330 -9.506  1.00 80.80  ? 923  VAL   E CG1 1 
ATOM   15872 C  CG2 . VAL   E 2 619 ? 29.081  -10.215 -8.578  1.00 88.90  ? 923  VAL   E CG2 1 
ATOM   15873 N  N   . GLY   E 2 620 ? 28.547  -13.057 -12.255 1.00 85.38  ? 924  GLY   E N   1 
ATOM   15874 C  CA  . GLY   E 2 620 ? 28.214  -14.273 -12.979 1.00 85.52  ? 924  GLY   E CA  1 
ATOM   15875 C  C   . GLY   E 2 620 ? 29.435  -15.104 -13.307 1.00 84.71  ? 924  GLY   E C   1 
ATOM   15876 O  O   . GLY   E 2 620 ? 30.571  -14.613 -13.318 1.00 85.60  ? 924  GLY   E O   1 
ATOM   15877 N  N   . ASP   E 2 621 ? 29.188  -16.387 -13.567 1.00 85.60  ? 925  ASP   E N   1 
ATOM   15878 C  CA  . ASP   E 2 621 ? 30.255  -17.307 -13.943 1.00 83.95  ? 925  ASP   E CA  1 
ATOM   15879 C  C   . ASP   E 2 621 ? 29.852  -18.053 -15.200 1.00 82.59  ? 925  ASP   E C   1 
ATOM   15880 O  O   . ASP   E 2 621 ? 28.761  -17.861 -15.752 1.00 82.44  ? 925  ASP   E O   1 
ATOM   15881 C  CB  . ASP   E 2 621 ? 30.603  -18.295 -12.816 1.00 83.00  ? 925  ASP   E CB  1 
ATOM   15882 C  CG  . ASP   E 2 621 ? 29.471  -19.235 -12.480 1.00 84.20  ? 925  ASP   E CG  1 
ATOM   15883 O  OD1 . ASP   E 2 621 ? 28.457  -19.267 -13.216 1.00 85.90  ? 925  ASP   E OD1 1 
ATOM   15884 O  OD2 . ASP   E 2 621 ? 29.599  -19.944 -11.458 1.00 85.48  ? 925  ASP   E OD2 1 
ATOM   15885 N  N   . LEU   E 2 622 ? 30.742  -18.937 -15.637 1.00 82.82  ? 926  LEU   E N   1 
ATOM   15886 C  CA  . LEU   E 2 622 ? 30.493  -19.632 -16.886 1.00 80.20  ? 926  LEU   E CA  1 
ATOM   15887 C  C   . LEU   E 2 622 ? 29.278  -20.557 -16.841 1.00 81.83  ? 926  LEU   E C   1 
ATOM   15888 O  O   . LEU   E 2 622 ? 28.826  -20.976 -17.909 1.00 84.58  ? 926  LEU   E O   1 
ATOM   15889 C  CB  . LEU   E 2 622 ? 31.737  -20.409 -17.283 1.00 77.28  ? 926  LEU   E CB  1 
ATOM   15890 C  CG  . LEU   E 2 622 ? 31.990  -20.409 -18.776 1.00 75.14  ? 926  LEU   E CG  1 
ATOM   15891 C  CD1 . LEU   E 2 622 ? 31.558  -19.084 -19.395 1.00 73.93  ? 926  LEU   E CD1 1 
ATOM   15892 C  CD2 . LEU   E 2 622 ? 33.467  -20.655 -18.993 1.00 80.69  ? 926  LEU   E CD2 1 
ATOM   15893 N  N   . MET   E 2 623 ? 28.731  -20.866 -15.662 1.00 79.61  ? 927  MET   E N   1 
ATOM   15894 C  CA  . MET   E 2 623 ? 27.685  -21.867 -15.536 1.00 75.21  ? 927  MET   E CA  1 
ATOM   15895 C  C   . MET   E 2 623 ? 26.310  -21.278 -15.229 1.00 80.85  ? 927  MET   E C   1 
ATOM   15896 O  O   . MET   E 2 623 ? 25.449  -21.975 -14.687 1.00 78.02  ? 927  MET   E O   1 
ATOM   15897 C  CB  . MET   E 2 623 ? 28.063  -22.865 -14.456 1.00 87.79  ? 927  MET   E CB  1 
ATOM   15898 C  CG  . MET   E 2 623 ? 29.382  -23.554 -14.714 1.00 89.63  ? 927  MET   E CG  1 
ATOM   15899 S  SD  . MET   E 2 623 ? 29.189  -25.309 -15.116 1.00 85.65  ? 927  MET   E SD  1 
ATOM   15900 C  CE  . MET   E 2 623 ? 30.870  -25.640 -15.608 1.00 86.73  ? 927  MET   E CE  1 
ATOM   15901 N  N   . ARG   E 2 624 ? 26.074  -20.014 -15.589 1.00 83.68  ? 928  ARG   E N   1 
ATOM   15902 C  CA  . ARG   E 2 624 ? 24.787  -19.378 -15.334 1.00 81.89  ? 928  ARG   E CA  1 
ATOM   15903 C  C   . ARG   E 2 624 ? 24.531  -19.252 -13.837 1.00 84.03  ? 928  ARG   E C   1 
ATOM   15904 O  O   . ARG   E 2 624 ? 23.372  -19.165 -13.413 1.00 82.39  ? 928  ARG   E O   1 
ATOM   15905 C  CB  . ARG   E 2 624 ? 23.643  -20.156 -16.027 1.00 83.65  ? 928  ARG   E CB  1 
ATOM   15906 C  CG  . ARG   E 2 624 ? 22.404  -19.364 -16.596 1.00 83.66  ? 928  ARG   E CG  1 
ATOM   15907 C  CD  . ARG   E 2 624 ? 21.365  -19.187 -15.481 1.00 94.65  ? 928  ARG   E CD  1 
ATOM   15908 N  NE  . ARG   E 2 624 ? 19.948  -19.078 -15.801 1.00 96.60  ? 928  ARG   E NE  1 
ATOM   15909 C  CZ  . ARG   E 2 624 ? 18.999  -19.300 -14.901 1.00 108.20 ? 928  ARG   E CZ  1 
ATOM   15910 N  NH1 . ARG   E 2 624 ? 19.286  -19.770 -13.686 1.00 106.47 ? 928  ARG   E NH1 1 
ATOM   15911 N  NH2 . ARG   E 2 624 ? 17.738  -19.033 -15.218 1.00 113.86 ? 928  ARG   E NH2 1 
ATOM   15912 N  N   . SER   E 2 625 ? 25.582  -19.259 -13.012 1.00 84.69  ? 929  SER   E N   1 
ATOM   15913 C  CA  . SER   E 2 625 ? 25.413  -18.876 -11.617 1.00 83.63  ? 929  SER   E CA  1 
ATOM   15914 C  C   . SER   E 2 625 ? 25.290  -17.366 -11.615 1.00 89.11  ? 929  SER   E C   1 
ATOM   15915 O  O   . SER   E 2 625 ? 26.188  -16.655 -12.083 1.00 87.67  ? 929  SER   E O   1 
ATOM   15916 C  CB  . SER   E 2 625 ? 26.571  -19.357 -10.751 1.00 86.21  ? 929  SER   E CB  1 
ATOM   15917 O  OG  . SER   E 2 625 ? 26.895  -20.693 -11.070 1.00 91.13  ? 929  SER   E OG  1 
ATOM   15918 N  N   . VAL   E 2 626 ? 24.148  -16.868 -11.161 1.00 92.93  ? 930  VAL   E N   1 
ATOM   15919 C  CA  . VAL   E 2 626 ? 23.923  -15.432 -11.090 1.00 90.06  ? 930  VAL   E CA  1 
ATOM   15920 C  C   . VAL   E 2 626 ? 23.680  -15.027 -9.648  1.00 90.98  ? 930  VAL   E C   1 
ATOM   15921 O  O   . VAL   E 2 626 ? 22.979  -15.708 -8.893  1.00 93.07  ? 930  VAL   E O   1 
ATOM   15922 C  CB  . VAL   E 2 626 ? 22.769  -14.973 -11.996 1.00 86.98  ? 930  VAL   E CB  1 
ATOM   15923 C  CG1 . VAL   E 2 626 ? 22.214  -13.627 -11.513 1.00 90.55  ? 930  VAL   E CG1 1 
ATOM   15924 C  CG2 . VAL   E 2 626 ? 23.278  -14.878 -13.423 1.00 81.66  ? 930  VAL   E CG2 1 
ATOM   15925 N  N   . LEU   E 2 627 ? 24.250  -13.890 -9.287  1.00 95.31  ? 931  LEU   E N   1 
ATOM   15926 C  CA  . LEU   E 2 627 ? 24.362  -13.426 -7.913  1.00 95.06  ? 931  LEU   E CA  1 
ATOM   15927 C  C   . LEU   E 2 627 ? 24.129  -11.922 -7.910  1.00 93.17  ? 931  LEU   E C   1 
ATOM   15928 O  O   . LEU   E 2 627 ? 24.763  -11.204 -8.691  1.00 92.86  ? 931  LEU   E O   1 
ATOM   15929 C  CB  . LEU   E 2 627 ? 25.751  -13.776 -7.372  1.00 88.28  ? 931  LEU   E CB  1 
ATOM   15930 C  CG  . LEU   E 2 627 ? 26.046  -13.187 -6.026  1.00 87.06  ? 931  LEU   E CG  1 
ATOM   15931 C  CD1 . LEU   E 2 627 ? 24.792  -13.370 -5.202  1.00 95.01  ? 931  LEU   E CD1 1 
ATOM   15932 C  CD2 . LEU   E 2 627 ? 27.214  -13.931 -5.445  1.00 92.88  ? 931  LEU   E CD2 1 
ATOM   15933 N  N   . LEU   E 2 628 ? 23.213  -11.431 -7.073  1.00 95.10  ? 932  LEU   E N   1 
ATOM   15934 C  CA  . LEU   E 2 628 ? 22.915  -9.999  -7.046  1.00 93.92  ? 932  LEU   E CA  1 
ATOM   15935 C  C   . LEU   E 2 628 ? 23.358  -9.399  -5.716  1.00 95.19  ? 932  LEU   E C   1 
ATOM   15936 O  O   . LEU   E 2 628 ? 22.815  -9.750  -4.661  1.00 94.18  ? 932  LEU   E O   1 
ATOM   15937 C  CB  . LEU   E 2 628 ? 21.434  -9.731  -7.305  1.00 90.71  ? 932  LEU   E CB  1 
ATOM   15938 C  CG  . LEU   E 2 628 ? 21.178  -8.234  -7.438  1.00 97.96  ? 932  LEU   E CG  1 
ATOM   15939 C  CD1 . LEU   E 2 628 ? 22.143  -7.620  -8.448  1.00 95.51  ? 932  LEU   E CD1 1 
ATOM   15940 C  CD2 . LEU   E 2 628 ? 19.730  -7.935  -7.813  1.00 98.57  ? 932  LEU   E CD2 1 
ATOM   15941 N  N   . LEU   E 2 629 ? 24.338  -8.491  -5.783  1.00 95.39  ? 933  LEU   E N   1 
ATOM   15942 C  CA  . LEU   E 2 629 ? 24.947  -7.824  -4.635  1.00 97.17  ? 933  LEU   E CA  1 
ATOM   15943 C  C   . LEU   E 2 629 ? 24.485  -6.371  -4.538  1.00 97.31  ? 933  LEU   E C   1 
ATOM   15944 O  O   . LEU   E 2 629 ? 24.175  -5.737  -5.553  1.00 99.54  ? 933  LEU   E O   1 
ATOM   15945 C  CB  . LEU   E 2 629 ? 26.479  -7.853  -4.744  1.00 93.97  ? 933  LEU   E CB  1 
ATOM   15946 C  CG  . LEU   E 2 629 ? 27.247  -8.839  -3.873  1.00 92.26  ? 933  LEU   E CG  1 
ATOM   15947 C  CD1 . LEU   E 2 629 ? 26.944  -10.274 -4.265  1.00 90.37  ? 933  LEU   E CD1 1 
ATOM   15948 C  CD2 . LEU   E 2 629 ? 28.724  -8.554  -3.985  1.00 92.20  ? 933  LEU   E CD2 1 
ATOM   15949 N  N   . ALA   E 2 630 ? 24.469  -5.831  -3.312  1.00 103.20 ? 934  ALA   E N   1 
ATOM   15950 C  CA  . ALA   E 2 630 ? 24.183  -4.413  -3.069  1.00 101.28 ? 934  ALA   E CA  1 
ATOM   15951 C  C   . ALA   E 2 630 ? 25.274  -3.791  -2.207  1.00 105.21 ? 934  ALA   E C   1 
ATOM   15952 O  O   . ALA   E 2 630 ? 25.673  -4.373  -1.190  1.00 107.59 ? 934  ALA   E O   1 
ATOM   15953 C  CB  . ALA   E 2 630 ? 22.828  -4.213  -2.379  1.00 95.06  ? 934  ALA   E CB  1 
ATOM   15954 N  N   . TYR   E 2 631 ? 25.745  -2.601  -2.603  1.00 106.88 ? 935  TYR   E N   1 
ATOM   15955 C  CA  . TYR   E 2 631 ? 26.705  -1.842  -1.798  1.00 105.11 ? 935  TYR   E CA  1 
ATOM   15956 C  C   . TYR   E 2 631 ? 25.964  -1.110  -0.681  1.00 104.25 ? 935  TYR   E C   1 
ATOM   15957 O  O   . TYR   E 2 631 ? 25.039  -0.327  -0.944  1.00 100.49 ? 935  TYR   E O   1 
ATOM   15958 C  CB  . TYR   E 2 631 ? 27.494  -0.856  -2.662  1.00 105.20 ? 935  TYR   E CB  1 
ATOM   15959 C  CG  . TYR   E 2 631 ? 28.561  -0.051  -1.910  1.00 112.62 ? 935  TYR   E CG  1 
ATOM   15960 C  CD1 . TYR   E 2 631 ? 29.744  -0.655  -1.483  1.00 111.28 ? 935  TYR   E CD1 1 
ATOM   15961 C  CD2 . TYR   E 2 631 ? 28.401  1.323   -1.641  1.00 108.78 ? 935  TYR   E CD2 1 
ATOM   15962 C  CE1 . TYR   E 2 631 ? 30.736  0.073   -0.801  1.00 113.57 ? 935  TYR   E CE1 1 
ATOM   15963 C  CE2 . TYR   E 2 631 ? 29.398  2.059   -0.951  1.00 101.77 ? 935  TYR   E CE2 1 
ATOM   15964 C  CZ  . TYR   E 2 631 ? 30.566  1.422   -0.536  1.00 104.92 ? 935  TYR   E CZ  1 
ATOM   15965 O  OH  . TYR   E 2 631 ? 31.590  2.077   0.142   1.00 101.09 ? 935  TYR   E OH  1 
ATOM   15966 N  N   . LYS   E 2 632 ? 26.354  -1.388  0.561   1.00 106.01 ? 936  LYS   E N   1 
ATOM   15967 C  CA  . LYS   E 2 632 ? 25.740  -0.742  1.711   1.00 107.99 ? 936  LYS   E CA  1 
ATOM   15968 C  C   . LYS   E 2 632 ? 26.551  0.525   1.944   1.00 111.04 ? 936  LYS   E C   1 
ATOM   15969 O  O   . LYS   E 2 632 ? 27.604  0.475   2.594   1.00 113.03 ? 936  LYS   E O   1 
ATOM   15970 C  CB  . LYS   E 2 632 ? 25.749  -1.671  2.926   1.00 110.77 ? 936  LYS   E CB  1 
ATOM   15971 N  N   . PRO   E 2 633 ? 26.086  1.681   1.450   1.00 112.02 ? 937  PRO   E N   1 
ATOM   15972 C  CA  . PRO   E 2 633 ? 26.979  2.855   1.385   1.00 106.71 ? 937  PRO   E CA  1 
ATOM   15973 C  C   . PRO   E 2 633 ? 27.293  3.388   2.781   1.00 107.91 ? 937  PRO   E C   1 
ATOM   15974 O  O   . PRO   E 2 633 ? 28.430  3.816   3.038   1.00 105.54 ? 937  PRO   E O   1 
ATOM   15975 C  CB  . PRO   E 2 633 ? 26.196  3.857   0.521   1.00 94.96  ? 937  PRO   E CB  1 
ATOM   15976 C  CG  . PRO   E 2 633 ? 24.763  3.459   0.691   1.00 97.96  ? 937  PRO   E CG  1 
ATOM   15977 C  CD  . PRO   E 2 633 ? 24.754  1.967   0.843   1.00 105.79 ? 937  PRO   E CD  1 
ATOM   15978 N  N   . MET   E 2 634 ? 26.323  3.350   3.704   1.00 104.37 ? 938  MET   E N   1 
ATOM   15979 C  CA  . MET   E 2 634 ? 26.586  3.803   5.069   1.00 109.48 ? 938  MET   E CA  1 
ATOM   15980 C  C   . MET   E 2 634 ? 27.494  2.839   5.841   1.00 110.27 ? 938  MET   E C   1 
ATOM   15981 O  O   . MET   E 2 634 ? 28.266  3.281   6.699   1.00 109.25 ? 938  MET   E O   1 
ATOM   15982 C  CB  . MET   E 2 634 ? 25.264  4.025   5.814   1.00 107.10 ? 938  MET   E CB  1 
ATOM   15983 N  N   . GLU   E 2 635 ? 27.424  1.535   5.564   1.00 110.29 ? 939  GLU   E N   1 
ATOM   15984 C  CA  . GLU   E 2 635 ? 28.259  0.561   6.259   1.00 113.89 ? 939  GLU   E CA  1 
ATOM   15985 C  C   . GLU   E 2 635 ? 29.524  0.214   5.487   1.00 115.79 ? 939  GLU   E C   1 
ATOM   15986 O  O   . GLU   E 2 635 ? 30.316  -0.609  5.961   1.00 116.00 ? 939  GLU   E O   1 
ATOM   15987 C  CB  . GLU   E 2 635 ? 27.466  -0.715  6.550   1.00 117.69 ? 939  GLU   E CB  1 
ATOM   15988 N  N   . GLY   E 2 636 ? 29.707  0.808   4.318   1.00 128.09 ? 940  GLY   E N   1 
ATOM   15989 C  CA  . GLY   E 2 636 ? 30.870  0.550   3.465   1.00 129.41 ? 940  GLY   E CA  1 
ATOM   15990 C  C   . GLY   E 2 636 ? 31.172  -0.916  3.216   1.00 131.77 ? 940  GLY   E C   1 
ATOM   15991 O  O   . GLY   E 2 636 ? 32.347  -1.305  3.172   1.00 131.84 ? 940  GLY   E O   1 
ATOM   15992 N  N   . ASN   E 2 637 ? 30.138  -1.743  3.047   1.00 125.89 ? 941  ASN   E N   1 
ATOM   15993 C  CA  . ASN   E 2 637 ? 30.350  -3.138  2.728   1.00 122.78 ? 941  ASN   E CA  1 
ATOM   15994 C  C   . ASN   E 2 637 ? 29.285  -3.602  1.744   1.00 124.75 ? 941  ASN   E C   1 
ATOM   15995 O  O   . ASN   E 2 637 ? 28.277  -2.918  1.524   1.00 123.82 ? 941  ASN   E O   1 
ATOM   15996 C  CB  . ASN   E 2 637 ? 30.338  -4.010  3.981   1.00 121.70 ? 941  ASN   E CB  1 
ATOM   15997 C  CG  . ASN   E 2 637 ? 31.279  -5.179  3.857   1.00 126.91 ? 941  ASN   E CG  1 
ATOM   15998 O  OD1 . ASN   E 2 637 ? 32.336  -5.066  3.224   1.00 125.11 ? 941  ASN   E OD1 1 
ATOM   15999 N  ND2 . ASN   E 2 637 ? 30.900  -6.317  4.428   1.00 128.79 ? 941  ASN   E ND2 1 
ATOM   16000 N  N   . PHE   E 2 638 ? 29.527  -4.775  1.131   1.00 120.14 ? 942  PHE   E N   1 
ATOM   16001 C  CA  . PHE   E 2 638 ? 28.569  -5.405  0.227   1.00 110.53 ? 942  PHE   E CA  1 
ATOM   16002 C  C   . PHE   E 2 638 ? 27.614  -6.302  1.004   1.00 114.14 ? 942  PHE   E C   1 
ATOM   16003 O  O   . PHE   E 2 638 ? 27.988  -6.912  2.013   1.00 113.36 ? 942  PHE   E O   1 
ATOM   16004 C  CB  . PHE   E 2 638 ? 29.256  -6.275  -0.828  1.00 104.55 ? 942  PHE   E CB  1 
ATOM   16005 C  CG  . PHE   E 2 638 ? 30.296  -5.583  -1.643  1.00 93.78  ? 942  PHE   E CG  1 
ATOM   16006 C  CD1 . PHE   E 2 638 ? 29.948  -4.845  -2.752  1.00 89.09  ? 942  PHE   E CD1 1 
ATOM   16007 C  CD2 . PHE   E 2 638 ? 31.636  -5.744  -1.338  1.00 95.76  ? 942  PHE   E CD2 1 
ATOM   16008 C  CE1 . PHE   E 2 638 ? 30.913  -4.246  -3.516  1.00 91.85  ? 942  PHE   E CE1 1 
ATOM   16009 C  CE2 . PHE   E 2 638 ? 32.607  -5.147  -2.103  1.00 91.48  ? 942  PHE   E CE2 1 
ATOM   16010 C  CZ  . PHE   E 2 638 ? 32.252  -4.401  -3.192  1.00 90.21  ? 942  PHE   E CZ  1 
ATOM   16011 N  N   . GLU   E 2 639 ? 26.393  -6.435  0.478   1.00 113.06 ? 943  GLU   E N   1 
ATOM   16012 C  CA  . GLU   E 2 639 ? 25.361  -7.275  1.074   1.00 113.76 ? 943  GLU   E CA  1 
ATOM   16013 C  C   . GLU   E 2 639 ? 24.736  -8.166  0.011   1.00 113.88 ? 943  GLU   E C   1 
ATOM   16014 O  O   . GLU   E 2 639 ? 24.194  -7.654  -0.974  1.00 115.57 ? 943  GLU   E O   1 
ATOM   16015 C  CB  . GLU   E 2 639 ? 24.270  -6.428  1.720   1.00 115.68 ? 943  GLU   E CB  1 
ATOM   16016 C  CG  . GLU   E 2 639 ? 23.424  -7.206  2.699   1.00 122.63 ? 943  GLU   E CG  1 
ATOM   16017 C  CD  . GLU   E 2 639 ? 24.275  -8.041  3.666   1.00 131.12 ? 943  GLU   E CD  1 
ATOM   16018 O  OE1 . GLU   E 2 639 ? 25.093  -8.873  3.196   1.00 133.14 ? 943  GLU   E OE1 1 
ATOM   16019 O  OE2 . GLU   E 2 639 ? 24.128  -7.868  4.903   1.00 134.24 ? 943  GLU   E OE2 1 
ATOM   16020 N  N   . GLU   E 2 640 ? 24.763  -9.489  0.223   1.00 112.59 ? 944  GLU   E N   1 
ATOM   16021 C  CA  . GLU   E 2 640 ? 24.236  -10.405 -0.788  1.00 103.97 ? 944  GLU   E CA  1 
ATOM   16022 C  C   . GLU   E 2 640 ? 22.711  -10.378 -0.798  1.00 101.85 ? 944  GLU   E C   1 
ATOM   16023 O  O   . GLU   E 2 640 ? 22.070  -10.574 0.239   1.00 103.63 ? 944  GLU   E O   1 
ATOM   16024 C  CB  . GLU   E 2 640 ? 24.726  -11.828 -0.557  1.00 105.33 ? 944  GLU   E CB  1 
ATOM   16025 C  CG  . GLU   E 2 640 ? 24.428  -12.722 -1.751  1.00 108.04 ? 944  GLU   E CG  1 
ATOM   16026 C  CD  . GLU   E 2 640 ? 23.927  -14.099 -1.360  1.00 113.89 ? 944  GLU   E CD  1 
ATOM   16027 O  OE1 . GLU   E 2 640 ? 24.778  -14.909 -0.913  1.00 118.20 ? 944  GLU   E OE1 1 
ATOM   16028 O  OE2 . GLU   E 2 640 ? 22.695  -14.359 -1.501  1.00 106.23 ? 944  GLU   E OE2 1 
ATOM   16029 N  N   . ILE   E 2 641 ? 22.132  -10.158 -1.976  1.00 99.73  ? 945  ILE   E N   1 
ATOM   16030 C  CA  . ILE   E 2 641 ? 20.709  -9.854  -2.096  1.00 98.66  ? 945  ILE   E CA  1 
ATOM   16031 C  C   . ILE   E 2 641 ? 19.903  -11.038 -2.619  1.00 103.37 ? 945  ILE   E C   1 
ATOM   16032 O  O   . ILE   E 2 641 ? 18.890  -11.427 -2.024  1.00 104.01 ? 945  ILE   E O   1 
ATOM   16033 C  CB  . ILE   E 2 641 ? 20.511  -8.638  -3.009  1.00 97.19  ? 945  ILE   E CB  1 
ATOM   16034 C  CG1 . ILE   E 2 641 ? 21.271  -7.447  -2.441  1.00 101.22 ? 945  ILE   E CG1 1 
ATOM   16035 C  CG2 . ILE   E 2 641 ? 19.048  -8.339  -3.159  1.00 92.38  ? 945  ILE   E CG2 1 
ATOM   16036 C  CD1 . ILE   E 2 641 ? 21.399  -7.481  -0.935  1.00 102.27 ? 945  ILE   E CD1 1 
ATOM   16037 N  N   . ALA   E 2 642 ? 20.327  -11.591 -3.752  1.00 103.40 ? 946  ALA   E N   1 
ATOM   16038 C  CA  . ALA   E 2 642 ? 19.651  -12.733 -4.342  1.00 101.47 ? 946  ALA   E CA  1 
ATOM   16039 C  C   . ALA   E 2 642 ? 20.652  -13.527 -5.160  1.00 101.00 ? 946  ALA   E C   1 
ATOM   16040 O  O   . ALA   E 2 642 ? 21.770  -13.081 -5.436  1.00 98.56  ? 946  ALA   E O   1 
ATOM   16041 C  CB  . ALA   E 2 642 ? 18.481  -12.307 -5.226  1.00 100.26 ? 946  ALA   E CB  1 
ATOM   16042 N  N   . ARG   E 2 643 ? 20.222  -14.717 -5.566  1.00 106.14 ? 947  ARG   E N   1 
ATOM   16043 C  CA  . ARG   E 2 643 ? 21.021  -15.507 -6.488  1.00 100.97 ? 947  ARG   E CA  1 
ATOM   16044 C  C   . ARG   E 2 643 ? 20.145  -16.591 -7.080  1.00 97.78  ? 947  ARG   E C   1 
ATOM   16045 O  O   . ARG   E 2 643 ? 19.068  -16.901 -6.572  1.00 98.96  ? 947  ARG   E O   1 
ATOM   16046 C  CB  . ARG   E 2 643 ? 22.232  -16.119 -5.796  1.00 98.28  ? 947  ARG   E CB  1 
ATOM   16047 C  CG  . ARG   E 2 643 ? 21.840  -17.189 -4.833  1.00 96.36  ? 947  ARG   E CG  1 
ATOM   16048 C  CD  . ARG   E 2 643 ? 22.877  -17.292 -3.774  1.00 99.32  ? 947  ARG   E CD  1 
ATOM   16049 N  NE  . ARG   E 2 643 ? 24.205  -17.381 -4.367  1.00 104.69 ? 947  ARG   E NE  1 
ATOM   16050 C  CZ  . ARG   E 2 643 ? 25.338  -17.443 -3.674  1.00 113.39 ? 947  ARG   E CZ  1 
ATOM   16051 N  NH1 . ARG   E 2 643 ? 25.349  -17.358 -2.347  1.00 118.88 ? 947  ARG   E NH1 1 
ATOM   16052 N  NH2 . ARG   E 2 643 ? 26.490  -17.609 -4.324  1.00 109.26 ? 947  ARG   E NH2 1 
ATOM   16053 N  N   . ASP   E 2 644 ? 20.617  -17.139 -8.183  1.00 99.46  ? 948  ASP   E N   1 
ATOM   16054 C  CA  . ASP   E 2 644 ? 19.981  -18.280 -8.817  1.00 99.40  ? 948  ASP   E CA  1 
ATOM   16055 C  C   . ASP   E 2 644 ? 21.102  -19.088 -9.446  1.00 98.86  ? 948  ASP   E C   1 
ATOM   16056 O  O   . ASP   E 2 644 ? 22.015  -18.522 -10.054 1.00 98.49  ? 948  ASP   E O   1 
ATOM   16057 C  CB  . ASP   E 2 644 ? 18.956  -17.839 -9.870  1.00 100.45 ? 948  ASP   E CB  1 
ATOM   16058 C  CG  . ASP   E 2 644 ? 18.183  -19.012 -10.489 1.00 105.86 ? 948  ASP   E CG  1 
ATOM   16059 O  OD1 . ASP   E 2 644 ? 17.993  -20.048 -9.797  1.00 112.98 ? 948  ASP   E OD1 1 
ATOM   16060 O  OD2 . ASP   E 2 644 ? 17.786  -18.906 -11.682 1.00 104.37 ? 948  ASP   E OD2 1 
ATOM   16061 N  N   . PHE   E 2 645 ? 21.067  -20.396 -9.262  1.00 96.44  ? 949  PHE   E N   1 
ATOM   16062 C  CA  . PHE   E 2 645 ? 21.994  -21.290 -9.938  1.00 95.95  ? 949  PHE   E CA  1 
ATOM   16063 C  C   . PHE   E 2 645 ? 21.184  -22.267 -10.779 1.00 92.60  ? 949  PHE   E C   1 
ATOM   16064 O  O   . PHE   E 2 645 ? 20.279  -22.937 -10.271 1.00 97.92  ? 949  PHE   E O   1 
ATOM   16065 C  CB  . PHE   E 2 645 ? 22.888  -22.017 -8.927  1.00 97.61  ? 949  PHE   E CB  1 
ATOM   16066 C  CG  . PHE   E 2 645 ? 23.766  -21.095 -8.107  1.00 100.31 ? 949  PHE   E CG  1 
ATOM   16067 C  CD1 . PHE   E 2 645 ? 24.053  -19.792 -8.558  1.00 99.85  ? 949  PHE   E CD1 1 
ATOM   16068 C  CD2 . PHE   E 2 645 ? 24.305  -21.516 -6.889  1.00 94.58  ? 949  PHE   E CD2 1 
ATOM   16069 C  CE1 . PHE   E 2 645 ? 24.868  -18.918 -7.807  1.00 97.97  ? 949  PHE   E CE1 1 
ATOM   16070 C  CE2 . PHE   E 2 645 ? 25.123  -20.653 -6.131  1.00 104.94 ? 949  PHE   E CE2 1 
ATOM   16071 C  CZ  . PHE   E 2 645 ? 25.405  -19.352 -6.590  1.00 103.26 ? 949  PHE   E CZ  1 
ATOM   16072 N  N   . ASN   E 2 646 ? 21.476  -22.313 -12.073 1.00 88.62  ? 950  ASN   E N   1 
ATOM   16073 C  CA  . ASN   E 2 646 ? 20.829  -23.256 -12.980 1.00 89.85  ? 950  ASN   E CA  1 
ATOM   16074 C  C   . ASN   E 2 646 ? 21.896  -23.655 -13.976 1.00 87.85  ? 950  ASN   E C   1 
ATOM   16075 O  O   . ASN   E 2 646 ? 22.074  -23.016 -15.025 1.00 88.05  ? 950  ASN   E O   1 
ATOM   16076 C  CB  . ASN   E 2 646 ? 19.584  -22.659 -13.647 1.00 92.64  ? 950  ASN   E CB  1 
ATOM   16077 C  CG  . ASN   E 2 646 ? 18.786  -23.697 -14.432 1.00 98.26  ? 950  ASN   E CG  1 
ATOM   16078 O  OD1 . ASN   E 2 646 ? 19.264  -24.811 -14.669 1.00 102.85 ? 950  ASN   E OD1 1 
ATOM   16079 N  ND2 . ASN   E 2 646 ? 17.578  -23.332 -14.849 1.00 104.45 ? 950  ASN   E ND2 1 
ATOM   16080 N  N   . PRO   E 2 647 ? 22.621  -24.730 -13.684 1.00 85.46  ? 951  PRO   E N   1 
ATOM   16081 C  CA  . PRO   E 2 647 ? 23.867  -25.004 -14.409 1.00 86.71  ? 951  PRO   E CA  1 
ATOM   16082 C  C   . PRO   E 2 647 ? 23.615  -25.106 -15.905 1.00 85.23  ? 951  PRO   E C   1 
ATOM   16083 O  O   . PRO   E 2 647 ? 22.743  -25.847 -16.357 1.00 86.20  ? 951  PRO   E O   1 
ATOM   16084 C  CB  . PRO   E 2 647 ? 24.350  -26.329 -13.803 1.00 85.68  ? 951  PRO   E CB  1 
ATOM   16085 C  CG  . PRO   E 2 647 ? 23.529  -26.521 -12.596 1.00 85.46  ? 951  PRO   E CG  1 
ATOM   16086 C  CD  . PRO   E 2 647 ? 22.224  -25.858 -12.846 1.00 84.45  ? 951  PRO   E CD  1 
ATOM   16087 N  N   . ASN   E 2 648 ? 24.376  -24.322 -16.663 1.00 83.87  ? 952  ASN   E N   1 
ATOM   16088 C  CA  . ASN   E 2 648 ? 24.342  -24.241 -18.109 1.00 79.99  ? 952  ASN   E CA  1 
ATOM   16089 C  C   . ASN   E 2 648 ? 25.430  -23.266 -18.508 1.00 83.24  ? 952  ASN   E C   1 
ATOM   16090 O  O   . ASN   E 2 648 ? 25.803  -22.387 -17.716 1.00 85.46  ? 952  ASN   E O   1 
ATOM   16091 C  CB  . ASN   E 2 648 ? 22.980  -23.774 -18.644 1.00 80.46  ? 952  ASN   E CB  1 
ATOM   16092 C  CG  . ASN   E 2 648 ? 22.911  -23.811 -20.176 1.00 83.21  ? 952  ASN   E CG  1 
ATOM   16093 O  OD1 . ASN   E 2 648 ? 23.801  -24.334 -20.837 1.00 83.14  ? 952  ASN   E OD1 1 
ATOM   16094 N  ND2 . ASN   E 2 648 ? 21.843  -23.260 -20.738 1.00 88.01  ? 952  ASN   E ND2 1 
ATOM   16095 N  N   . TRP   E 2 649 ? 25.946  -23.412 -19.721 1.00 82.23  ? 953  TRP   E N   1 
ATOM   16096 C  CA  . TRP   E 2 649 ? 26.968  -22.491 -20.210 1.00 80.91  ? 953  TRP   E CA  1 
ATOM   16097 C  C   . TRP   E 2 649 ? 26.362  -21.109 -20.492 1.00 81.25  ? 953  TRP   E C   1 
ATOM   16098 O  O   . TRP   E 2 649 ? 25.387  -20.997 -21.244 1.00 80.33  ? 953  TRP   E O   1 
ATOM   16099 C  CB  . TRP   E 2 649 ? 27.627  -23.048 -21.472 1.00 82.46  ? 953  TRP   E CB  1 
ATOM   16100 C  CG  . TRP   E 2 649 ? 28.222  -24.451 -21.368 1.00 86.28  ? 953  TRP   E CG  1 
ATOM   16101 C  CD1 . TRP   E 2 649 ? 27.984  -25.511 -22.208 1.00 90.19  ? 953  TRP   E CD1 1 
ATOM   16102 C  CD2 . TRP   E 2 649 ? 29.165  -24.928 -20.402 1.00 87.87  ? 953  TRP   E CD2 1 
ATOM   16103 N  NE1 . TRP   E 2 649 ? 28.714  -26.612 -21.821 1.00 83.87  ? 953  TRP   E NE1 1 
ATOM   16104 C  CE2 . TRP   E 2 649 ? 29.443  -26.279 -20.714 1.00 85.22  ? 953  TRP   E CE2 1 
ATOM   16105 C  CE3 . TRP   E 2 649 ? 29.802  -24.349 -19.301 1.00 86.07  ? 953  TRP   E CE3 1 
ATOM   16106 C  CZ2 . TRP   E 2 649 ? 30.319  -27.044 -19.970 1.00 88.60  ? 953  TRP   E CZ2 1 
ATOM   16107 C  CZ3 . TRP   E 2 649 ? 30.682  -25.106 -18.577 1.00 82.44  ? 953  TRP   E CZ3 1 
ATOM   16108 C  CH2 . TRP   E 2 649 ? 30.928  -26.440 -18.906 1.00 89.01  ? 953  TRP   E CH2 1 
ATOM   16109 N  N   . MET   E 2 650 ? 26.949  -20.055 -19.892 1.00 82.75  ? 954  MET   E N   1 
ATOM   16110 C  CA  . MET   E 2 650 ? 26.484  -18.663 -19.994 1.00 81.08  ? 954  MET   E CA  1 
ATOM   16111 C  C   . MET   E 2 650 ? 27.544  -17.762 -20.602 1.00 76.14  ? 954  MET   E C   1 
ATOM   16112 O  O   . MET   E 2 650 ? 28.658  -17.670 -20.081 1.00 74.97  ? 954  MET   E O   1 
ATOM   16113 C  CB  . MET   E 2 650 ? 26.099  -18.057 -18.642 1.00 82.49  ? 954  MET   E CB  1 
ATOM   16114 C  CG  . MET   E 2 650 ? 25.557  -16.644 -18.800 1.00 77.73  ? 954  MET   E CG  1 
ATOM   16115 S  SD  . MET   E 2 650 ? 24.865  -15.903 -17.324 1.00 79.09  ? 954  MET   E SD  1 
ATOM   16116 C  CE  . MET   E 2 650 ? 26.351  -15.875 -16.345 1.00 85.89  ? 954  MET   E CE  1 
ATOM   16117 N  N   . SER   E 2 651 ? 27.155  -17.029 -21.641 1.00 76.69  ? 955  SER   E N   1 
ATOM   16118 C  CA  . SER   E 2 651 ? 28.092  -16.344 -22.516 1.00 73.77  ? 955  SER   E CA  1 
ATOM   16119 C  C   . SER   E 2 651 ? 28.245  -14.860 -22.223 1.00 76.19  ? 955  SER   E C   1 
ATOM   16120 O  O   . SER   E 2 651 ? 29.335  -14.312 -22.434 1.00 73.68  ? 955  SER   E O   1 
ATOM   16121 C  CB  . SER   E 2 651 ? 27.642  -16.527 -23.964 1.00 71.48  ? 955  SER   E CB  1 
ATOM   16122 O  OG  . SER   E 2 651 ? 28.469  -15.773 -24.809 1.00 81.44  ? 955  SER   E OG  1 
ATOM   16123 N  N   . ALA   E 2 652 ? 27.173  -14.209 -21.773 1.00 75.28  ? 956  ALA   E N   1 
ATOM   16124 C  CA  . ALA   E 2 652 ? 27.129  -12.769 -21.561 1.00 77.37  ? 956  ALA   E CA  1 
ATOM   16125 C  C   . ALA   E 2 652 ? 25.976  -12.474 -20.618 1.00 81.36  ? 956  ALA   E C   1 
ATOM   16126 O  O   . ALA   E 2 652 ? 25.036  -13.266 -20.505 1.00 77.52  ? 956  ALA   E O   1 
ATOM   16127 C  CB  . ALA   E 2 652 ? 26.956  -12.008 -22.877 1.00 73.82  ? 956  ALA   E CB  1 
ATOM   16128 N  N   . VAL   E 2 653 ? 26.036  -11.302 -19.972 1.00 85.48  ? 957  VAL   E N   1 
ATOM   16129 C  CA  . VAL   E 2 653 ? 25.063  -10.931 -18.943 1.00 84.37  ? 957  VAL   E CA  1 
ATOM   16130 C  C   . VAL   E 2 653 ? 24.987  -9.412  -18.823 1.00 81.84  ? 957  VAL   E C   1 
ATOM   16131 O  O   . VAL   E 2 653 ? 25.944  -8.703  -19.128 1.00 84.63  ? 957  VAL   E O   1 
ATOM   16132 C  CB  . VAL   E 2 653 ? 25.453  -11.557 -17.592 1.00 77.80  ? 957  VAL   E CB  1 
ATOM   16133 C  CG1 . VAL   E 2 653 ? 26.554  -10.718 -16.952 1.00 78.71  ? 957  VAL   E CG1 1 
ATOM   16134 C  CG2 . VAL   E 2 653 ? 24.236  -11.694 -16.721 1.00 77.35  ? 957  VAL   E CG2 1 
ATOM   16135 N  N   . GLU   E 2 654 ? 23.852  -8.909  -18.344 1.00 86.21  ? 958  GLU   E N   1 
ATOM   16136 C  CA  . GLU   E 2 654 ? 23.598  -7.478  -18.455 1.00 85.85  ? 958  GLU   E CA  1 
ATOM   16137 C  C   . GLU   E 2 654 ? 22.401  -7.088  -17.601 1.00 87.39  ? 958  GLU   E C   1 
ATOM   16138 O  O   . GLU   E 2 654 ? 21.410  -7.823  -17.562 1.00 89.98  ? 958  GLU   E O   1 
ATOM   16139 C  CB  . GLU   E 2 654 ? 23.326  -7.098  -19.914 1.00 88.13  ? 958  GLU   E CB  1 
ATOM   16140 C  CG  . GLU   E 2 654 ? 22.996  -5.636  -20.144 1.00 90.02  ? 958  GLU   E CG  1 
ATOM   16141 C  CD  . GLU   E 2 654 ? 24.206  -4.735  -19.973 1.00 92.73  ? 958  GLU   E CD  1 
ATOM   16142 O  OE1 . GLU   E 2 654 ? 24.205  -3.949  -18.982 1.00 99.24  ? 958  GLU   E OE1 1 
ATOM   16143 O  OE2 . GLU   E 2 654 ? 25.139  -4.815  -20.820 1.00 93.36  ? 958  GLU   E OE2 1 
ATOM   16144 N  N   . ILE   E 2 655 ? 22.472  -5.915  -16.967 1.00 85.84  ? 959  ILE   E N   1 
ATOM   16145 C  CA  . ILE   E 2 655 ? 21.379  -5.429  -16.132 1.00 88.28  ? 959  ILE   E CA  1 
ATOM   16146 C  C   . ILE   E 2 655 ? 20.377  -4.724  -17.034 1.00 89.51  ? 959  ILE   E C   1 
ATOM   16147 O  O   . ILE   E 2 655 ? 20.732  -3.792  -17.762 1.00 85.93  ? 959  ILE   E O   1 
ATOM   16148 C  CB  . ILE   E 2 655 ? 21.889  -4.496  -15.023 1.00 89.08  ? 959  ILE   E CB  1 
ATOM   16149 C  CG1 . ILE   E 2 655 ? 22.859  -5.251  -14.112 1.00 84.37  ? 959  ILE   E CG1 1 
ATOM   16150 C  CG2 . ILE   E 2 655 ? 20.721  -3.926  -14.215 1.00 88.60  ? 959  ILE   E CG2 1 
ATOM   16151 C  CD1 . ILE   E 2 655 ? 23.950  -4.408  -13.541 1.00 79.04  ? 959  ILE   E CD1 1 
ATOM   16152 N  N   . LEU   E 2 656 ? 19.128  -5.183  -17.010 1.00 88.69  ? 960  LEU   E N   1 
ATOM   16153 C  CA  . LEU   E 2 656 ? 18.116  -4.581  -17.869 1.00 88.63  ? 960  LEU   E CA  1 
ATOM   16154 C  C   . LEU   E 2 656 ? 17.541  -3.339  -17.218 1.00 95.79  ? 960  LEU   E C   1 
ATOM   16155 O  O   . LEU   E 2 656 ? 17.557  -2.244  -17.797 1.00 99.75  ? 960  LEU   E O   1 
ATOM   16156 C  CB  . LEU   E 2 656 ? 16.990  -5.573  -18.149 1.00 87.20  ? 960  LEU   E CB  1 
ATOM   16157 C  CG  . LEU   E 2 656 ? 17.269  -6.492  -19.313 1.00 87.45  ? 960  LEU   E CG  1 
ATOM   16158 C  CD1 . LEU   E 2 656 ? 16.008  -7.257  -19.738 1.00 92.35  ? 960  LEU   E CD1 1 
ATOM   16159 C  CD2 . LEU   E 2 656 ? 17.803  -5.633  -20.430 1.00 81.06  ? 960  LEU   E CD2 1 
ATOM   16160 N  N   . ASP   E 2 657 ? 16.967  -3.527  -16.037 1.00 97.00  ? 961  ASP   E N   1 
ATOM   16161 C  CA  . ASP   E 2 657 ? 16.503  -2.453  -15.179 1.00 96.66  ? 961  ASP   E CA  1 
ATOM   16162 C  C   . ASP   E 2 657 ? 16.957  -2.838  -13.778 1.00 102.90 ? 961  ASP   E C   1 
ATOM   16163 O  O   . ASP   E 2 657 ? 17.886  -3.635  -13.608 1.00 104.59 ? 961  ASP   E O   1 
ATOM   16164 C  CB  . ASP   E 2 657 ? 14.985  -2.226  -15.342 1.00 102.28 ? 961  ASP   E CB  1 
ATOM   16165 C  CG  . ASP   E 2 657 ? 14.119  -3.253  -14.586 1.00 108.76 ? 961  ASP   E CG  1 
ATOM   16166 O  OD1 . ASP   E 2 657 ? 14.592  -3.893  -13.624 1.00 109.74 ? 961  ASP   E OD1 1 
ATOM   16167 O  OD2 . ASP   E 2 657 ? 12.925  -3.400  -14.950 1.00 108.06 ? 961  ASP   E OD2 1 
ATOM   16168 N  N   . ASP   E 2 658 ? 16.304  -2.280  -12.762 1.00 107.73 ? 962  ASP   E N   1 
ATOM   16169 C  CA  . ASP   E 2 658 ? 16.674  -2.570  -11.385 1.00 110.33 ? 962  ASP   E CA  1 
ATOM   16170 C  C   . ASP   E 2 658 ? 16.282  -3.978  -10.967 1.00 111.49 ? 962  ASP   E C   1 
ATOM   16171 O  O   . ASP   E 2 658 ? 16.859  -4.511  -10.017 1.00 111.62 ? 962  ASP   E O   1 
ATOM   16172 C  CB  . ASP   E 2 658 ? 16.025  -1.549  -10.448 1.00 112.71 ? 962  ASP   E CB  1 
ATOM   16173 C  CG  . ASP   E 2 658 ? 17.035  -0.608  -9.817  1.00 117.47 ? 962  ASP   E CG  1 
ATOM   16174 O  OD1 . ASP   E 2 658 ? 18.202  -0.619  -10.268 1.00 117.35 ? 962  ASP   E OD1 1 
ATOM   16175 O  OD2 . ASP   E 2 658 ? 16.664  0.129   -8.869  1.00 117.14 ? 962  ASP   E OD2 1 
ATOM   16176 N  N   . ASP   E 2 659 ? 15.309  -4.591  -11.646 1.00 119.95 ? 963  ASP   E N   1 
ATOM   16177 C  CA  . ASP   E 2 659 ? 14.742  -5.854  -11.204 1.00 121.29 ? 963  ASP   E CA  1 
ATOM   16178 C  C   . ASP   E 2 659 ? 14.925  -6.978  -12.198 1.00 118.72 ? 963  ASP   E C   1 
ATOM   16179 O  O   . ASP   E 2 659 ? 14.674  -8.134  -11.850 1.00 120.93 ? 963  ASP   E O   1 
ATOM   16180 C  CB  . ASP   E 2 659 ? 13.239  -5.709  -10.949 1.00 125.75 ? 963  ASP   E CB  1 
ATOM   16181 C  CG  . ASP   E 2 659 ? 12.933  -4.684  -9.899  1.00 130.27 ? 963  ASP   E CG  1 
ATOM   16182 O  OD1 . ASP   E 2 659 ? 13.502  -4.803  -8.786  1.00 125.89 ? 963  ASP   E OD1 1 
ATOM   16183 O  OD2 . ASP   E 2 659 ? 12.138  -3.761  -10.208 1.00 132.77 ? 963  ASP   E OD2 1 
ATOM   16184 N  N   . ASN   E 2 660 ? 15.309  -6.673  -13.424 1.00 110.00 ? 964  ASN   E N   1 
ATOM   16185 C  CA  . ASN   E 2 660 ? 15.375  -7.672  -14.470 1.00 104.54 ? 964  ASN   E CA  1 
ATOM   16186 C  C   . ASN   E 2 660 ? 16.790  -7.684  -15.017 1.00 103.41 ? 964  ASN   E C   1 
ATOM   16187 O  O   . ASN   E 2 660 ? 17.386  -6.626  -15.257 1.00 101.86 ? 964  ASN   E O   1 
ATOM   16188 C  CB  . ASN   E 2 660 ? 14.336  -7.382  -15.548 1.00 98.92  ? 964  ASN   E CB  1 
ATOM   16189 C  CG  . ASN   E 2 660 ? 12.916  -7.435  -15.006 1.00 101.07 ? 964  ASN   E CG  1 
ATOM   16190 O  OD1 . ASN   E 2 660 ? 12.346  -8.508  -14.832 1.00 98.80  ? 964  ASN   E OD1 1 
ATOM   16191 N  ND2 . ASN   E 2 660 ? 12.342  -6.269  -14.726 1.00 107.88 ? 964  ASN   E ND2 1 
ATOM   16192 N  N   . PHE   E 2 661 ? 17.337  -8.881  -15.158 1.00 104.62 ? 965  PHE   E N   1 
ATOM   16193 C  CA  . PHE   E 2 661 ? 18.673  -9.081  -15.687 1.00 102.98 ? 965  PHE   E CA  1 
ATOM   16194 C  C   . PHE   E 2 661 ? 18.567  -9.941  -16.932 1.00 100.55 ? 965  PHE   E C   1 
ATOM   16195 O  O   . PHE   E 2 661 ? 17.709  -10.824 -17.011 1.00 104.08 ? 965  PHE   E O   1 
ATOM   16196 C  CB  . PHE   E 2 661 ? 19.547  -9.721  -14.625 1.00 103.32 ? 965  PHE   E CB  1 
ATOM   16197 C  CG  . PHE   E 2 661 ? 19.354  -9.098  -13.285 1.00 106.16 ? 965  PHE   E CG  1 
ATOM   16198 C  CD1 . PHE   E 2 661 ? 19.902  -7.847  -13.010 1.00 105.45 ? 965  PHE   E CD1 1 
ATOM   16199 C  CD2 . PHE   E 2 661 ? 18.567  -9.710  -12.329 1.00 106.09 ? 965  PHE   E CD2 1 
ATOM   16200 C  CE1 . PHE   E 2 661 ? 19.705  -7.239  -11.796 1.00 108.15 ? 965  PHE   E CE1 1 
ATOM   16201 C  CE2 . PHE   E 2 661 ? 18.364  -9.102  -11.105 1.00 111.02 ? 965  PHE   E CE2 1 
ATOM   16202 C  CZ  . PHE   E 2 661 ? 18.936  -7.861  -10.842 1.00 112.50 ? 965  PHE   E CZ  1 
ATOM   16203 N  N   . LEU   E 2 662 ? 19.396  -9.659  -17.925 1.00 87.61  ? 966  LEU   E N   1 
ATOM   16204 C  CA  . LEU   E 2 662 ? 19.354  -10.395 -19.174 1.00 82.01  ? 966  LEU   E CA  1 
ATOM   16205 C  C   . LEU   E 2 662 ? 20.673  -11.122 -19.381 1.00 86.05  ? 966  LEU   E C   1 
ATOM   16206 O  O   . LEU   E 2 662 ? 21.753  -10.555 -19.169 1.00 83.49  ? 966  LEU   E O   1 
ATOM   16207 C  CB  . LEU   E 2 662 ? 19.073  -9.464  -20.345 1.00 83.16  ? 966  LEU   E CB  1 
ATOM   16208 C  CG  . LEU   E 2 662 ? 19.197  -10.027 -21.767 1.00 88.75  ? 966  LEU   E CG  1 
ATOM   16209 C  CD1 . LEU   E 2 662 ? 17.841  -10.552 -22.275 1.00 87.39  ? 966  LEU   E CD1 1 
ATOM   16210 C  CD2 . LEU   E 2 662 ? 19.773  -8.970  -22.712 1.00 79.24  ? 966  LEU   E CD2 1 
ATOM   16211 N  N   . GLY   E 2 663 ? 20.575  -12.385 -19.791 1.00 87.61  ? 967  GLY   E N   1 
ATOM   16212 C  CA  . GLY   E 2 663 ? 21.750  -13.214 -19.963 1.00 83.91  ? 967  GLY   E CA  1 
ATOM   16213 C  C   . GLY   E 2 663 ? 21.677  -14.013 -21.247 1.00 83.88  ? 967  GLY   E C   1 
ATOM   16214 O  O   . GLY   E 2 663 ? 20.609  -14.167 -21.847 1.00 84.39  ? 967  GLY   E O   1 
ATOM   16215 N  N   . ALA   E 2 664 ? 22.838  -14.525 -21.657 1.00 80.60  ? 968  ALA   E N   1 
ATOM   16216 C  CA  . ALA   E 2 664 ? 22.982  -15.353 -22.854 1.00 82.09  ? 968  ALA   E CA  1 
ATOM   16217 C  C   . ALA   E 2 664 ? 23.536  -16.728 -22.472 1.00 82.59  ? 968  ALA   E C   1 
ATOM   16218 O  O   . ALA   E 2 664 ? 24.562  -16.807 -21.784 1.00 78.81  ? 968  ALA   E O   1 
ATOM   16219 C  CB  . ALA   E 2 664 ? 23.911  -14.661 -23.863 1.00 75.89  ? 968  ALA   E CB  1 
ATOM   16220 N  N   . GLU   E 2 665 ? 22.881  -17.810 -22.921 1.00 83.40  ? 969  GLU   E N   1 
ATOM   16221 C  CA  . GLU   E 2 665 ? 23.298  -19.158 -22.520 1.00 85.84  ? 969  GLU   E CA  1 
ATOM   16222 C  C   . GLU   E 2 665 ? 23.057  -20.175 -23.629 1.00 86.04  ? 969  GLU   E C   1 
ATOM   16223 O  O   . GLU   E 2 665 ? 22.427  -19.880 -24.646 1.00 86.81  ? 969  GLU   E O   1 
ATOM   16224 C  CB  . GLU   E 2 665 ? 22.574  -19.621 -21.255 1.00 86.81  ? 969  GLU   E CB  1 
ATOM   16225 C  CG  . GLU   E 2 665 ? 21.056  -19.723 -21.400 1.00 86.68  ? 969  GLU   E CG  1 
ATOM   16226 C  CD  . GLU   E 2 665 ? 20.406  -20.291 -20.150 1.00 92.28  ? 969  GLU   E CD  1 
ATOM   16227 O  OE1 . GLU   E 2 665 ? 20.666  -21.482 -19.870 1.00 101.31 ? 969  GLU   E OE1 1 
ATOM   16228 O  OE2 . GLU   E 2 665 ? 19.687  -19.563 -19.420 1.00 92.49  ? 969  GLU   E OE2 1 
ATOM   16229 N  N   . ASN   E 2 666 ? 23.538  -21.402 -23.390 1.00 86.11  ? 970  ASN   E N   1 
ATOM   16230 C  CA  . ASN   E 2 666 ? 23.499  -22.475 -24.389 1.00 87.44  ? 970  ASN   E CA  1 
ATOM   16231 C  C   . ASN   E 2 666 ? 22.090  -23.056 -24.537 1.00 86.27  ? 970  ASN   E C   1 
ATOM   16232 O  O   . ASN   E 2 666 ? 21.333  -23.140 -23.569 1.00 87.34  ? 970  ASN   E O   1 
ATOM   16233 C  CB  . ASN   E 2 666 ? 24.500  -23.589 -24.024 1.00 81.94  ? 970  ASN   E CB  1 
ATOM   16234 C  CG  . ASN   E 2 666 ? 24.408  -24.819 -24.956 1.00 85.23  ? 970  ASN   E CG  1 
ATOM   16235 O  OD1 . ASN   E 2 666 ? 23.570  -25.703 -24.764 1.00 97.26  ? 970  ASN   E OD1 1 
ATOM   16236 N  ND2 . ASN   E 2 666 ? 25.307  -24.895 -25.930 1.00 86.93  ? 970  ASN   E ND2 1 
ATOM   16237 N  N   . ALA   E 2 667 ? 21.727  -23.432 -25.766 1.00 86.27  ? 971  ALA   E N   1 
ATOM   16238 C  CA  . ALA   E 2 667 ? 22.554  -23.157 -26.939 1.00 86.52  ? 971  ALA   E CA  1 
ATOM   16239 C  C   . ALA   E 2 667 ? 21.906  -22.059 -27.765 1.00 84.31  ? 971  ALA   E C   1 
ATOM   16240 O  O   . ALA   E 2 667 ? 20.822  -22.298 -28.311 1.00 83.79  ? 971  ALA   E O   1 
ATOM   16241 C  CB  . ALA   E 2 667 ? 22.736  -24.400 -27.778 1.00 75.01  ? 971  ALA   E CB  1 
ATOM   16242 N  N   . PHE   E 2 668 ? 22.538  -20.875 -27.854 1.00 78.31  ? 972  PHE   E N   1 
ATOM   16243 C  CA  . PHE   E 2 668 ? 21.980  -19.748 -28.628 1.00 79.21  ? 972  PHE   E CA  1 
ATOM   16244 C  C   . PHE   E 2 668 ? 20.628  -19.304 -28.061 1.00 75.49  ? 972  PHE   E C   1 
ATOM   16245 O  O   . PHE   E 2 668 ? 19.642  -19.154 -28.786 1.00 76.61  ? 972  PHE   E O   1 
ATOM   16246 C  CB  . PHE   E 2 668 ? 21.839  -20.082 -30.130 1.00 78.77  ? 972  PHE   E CB  1 
ATOM   16247 C  CG  . PHE   E 2 668 ? 22.995  -20.855 -30.707 1.00 77.93  ? 972  PHE   E CG  1 
ATOM   16248 C  CD1 . PHE   E 2 668 ? 24.182  -20.210 -31.045 1.00 76.86  ? 972  PHE   E CD1 1 
ATOM   16249 C  CD2 . PHE   E 2 668 ? 22.910  -22.224 -30.887 1.00 71.49  ? 972  PHE   E CD2 1 
ATOM   16250 C  CE1 . PHE   E 2 668 ? 25.258  -20.931 -31.564 1.00 79.80  ? 972  PHE   E CE1 1 
ATOM   16251 C  CE2 . PHE   E 2 668 ? 23.986  -22.929 -31.388 1.00 76.17  ? 972  PHE   E CE2 1 
ATOM   16252 C  CZ  . PHE   E 2 668 ? 25.156  -22.292 -31.731 1.00 76.35  ? 972  PHE   E CZ  1 
ATOM   16253 N  N   . ASN   E 2 669 ? 20.586  -19.099 -26.748 1.00 75.12  ? 973  ASN   E N   1 
ATOM   16254 C  CA  . ASN   E 2 669 ? 19.373  -18.702 -26.050 1.00 77.74  ? 973  ASN   E CA  1 
ATOM   16255 C  C   . ASN   E 2 669 ? 19.617  -17.411 -25.281 1.00 83.04  ? 973  ASN   E C   1 
ATOM   16256 O  O   . ASN   E 2 669 ? 20.752  -17.058 -24.948 1.00 82.98  ? 973  ASN   E O   1 
ATOM   16257 C  CB  . ASN   E 2 669 ? 18.888  -19.825 -25.108 1.00 80.96  ? 973  ASN   E CB  1 
ATOM   16258 C  CG  . ASN   E 2 669 ? 18.465  -21.083 -25.886 1.00 88.71  ? 973  ASN   E CG  1 
ATOM   16259 O  OD1 . ASN   E 2 669 ? 17.832  -20.974 -26.945 1.00 88.92  ? 973  ASN   E OD1 1 
ATOM   16260 N  ND2 . ASN   E 2 669 ? 18.828  -22.276 -25.380 1.00 87.20  ? 973  ASN   E ND2 1 
ATOM   16261 N  N   . LEU   E 2 670 ? 18.537  -16.686 -25.030 1.00 79.29  ? 974  LEU   E N   1 
ATOM   16262 C  CA  . LEU   E 2 670 ? 18.540  -15.625 -24.047 1.00 76.06  ? 974  LEU   E CA  1 
ATOM   16263 C  C   . LEU   E 2 670 ? 17.680  -16.049 -22.875 1.00 80.41  ? 974  LEU   E C   1 
ATOM   16264 O  O   . LEU   E 2 670 ? 16.762  -16.860 -23.015 1.00 87.01  ? 974  LEU   E O   1 
ATOM   16265 C  CB  . LEU   E 2 670 ? 17.985  -14.328 -24.614 1.00 80.87  ? 974  LEU   E CB  1 
ATOM   16266 C  CG  . LEU   E 2 670 ? 18.926  -13.489 -25.452 1.00 79.42  ? 974  LEU   E CG  1 
ATOM   16267 C  CD1 . LEU   E 2 670 ? 19.772  -14.403 -26.282 1.00 81.74  ? 974  LEU   E CD1 1 
ATOM   16268 C  CD2 . LEU   E 2 670 ? 18.054  -12.613 -26.315 1.00 79.15  ? 974  LEU   E CD2 1 
ATOM   16269 N  N   . PHE   E 2 671 ? 17.964  -15.474 -21.716 1.00 85.42  ? 975  PHE   E N   1 
ATOM   16270 C  CA  . PHE   E 2 671 ? 17.089  -15.597 -20.562 1.00 85.27  ? 975  PHE   E CA  1 
ATOM   16271 C  C   . PHE   E 2 671 ? 17.039  -14.258 -19.851 1.00 86.52  ? 975  PHE   E C   1 
ATOM   16272 O  O   . PHE   E 2 671 ? 17.917  -13.404 -20.022 1.00 85.35  ? 975  PHE   E O   1 
ATOM   16273 C  CB  . PHE   E 2 671 ? 17.574  -16.667 -19.604 1.00 79.73  ? 975  PHE   E CB  1 
ATOM   16274 C  CG  . PHE   E 2 671 ? 18.864  -16.320 -18.964 1.00 85.25  ? 975  PHE   E CG  1 
ATOM   16275 C  CD1 . PHE   E 2 671 ? 18.884  -15.598 -17.791 1.00 89.11  ? 975  PHE   E CD1 1 
ATOM   16276 C  CD2 . PHE   E 2 671 ? 20.074  -16.667 -19.557 1.00 88.72  ? 975  PHE   E CD2 1 
ATOM   16277 C  CE1 . PHE   E 2 671 ? 20.093  -15.250 -17.187 1.00 91.38  ? 975  PHE   E CE1 1 
ATOM   16278 C  CE2 . PHE   E 2 671 ? 21.297  -16.320 -18.955 1.00 88.98  ? 975  PHE   E CE2 1 
ATOM   16279 C  CZ  . PHE   E 2 671 ? 21.299  -15.610 -17.768 1.00 89.59  ? 975  PHE   E CZ  1 
ATOM   16280 N  N   . VAL   E 2 672 ? 16.001  -14.103 -19.032 1.00 89.86  ? 976  VAL   E N   1 
ATOM   16281 C  CA  . VAL   E 2 672 ? 15.813  -12.947 -18.159 1.00 90.11  ? 976  VAL   E CA  1 
ATOM   16282 C  C   . VAL   E 2 672 ? 15.325  -13.456 -16.803 1.00 92.65  ? 976  VAL   E C   1 
ATOM   16283 O  O   . VAL   E 2 672 ? 14.411  -14.286 -16.734 1.00 95.94  ? 976  VAL   E O   1 
ATOM   16284 C  CB  . VAL   E 2 672 ? 14.815  -11.941 -18.764 1.00 84.66  ? 976  VAL   E CB  1 
ATOM   16285 C  CG1 . VAL   E 2 672 ? 14.311  -10.944 -17.701 1.00 87.23  ? 976  VAL   E CG1 1 
ATOM   16286 C  CG2 . VAL   E 2 672 ? 15.443  -11.240 -19.968 1.00 85.38  ? 976  VAL   E CG2 1 
ATOM   16287 N  N   . CYS   E 2 673 ? 15.938  -12.974 -15.727 1.00 90.49  ? 977  CYS   E N   1 
ATOM   16288 C  CA  . CYS   E 2 673 ? 15.506  -13.309 -14.379 1.00 96.91  ? 977  CYS   E CA  1 
ATOM   16289 C  C   . CYS   E 2 673 ? 15.290  -12.026 -13.586 1.00 99.10  ? 977  CYS   E C   1 
ATOM   16290 O  O   . CYS   E 2 673 ? 15.821  -10.962 -13.927 1.00 102.26 ? 977  CYS   E O   1 
ATOM   16291 C  CB  . CYS   E 2 673 ? 16.524  -14.190 -13.685 1.00 96.79  ? 977  CYS   E CB  1 
ATOM   16292 S  SG  . CYS   E 2 673 ? 18.125  -13.402 -13.758 1.00 105.73 ? 977  CYS   E SG  1 
ATOM   16293 N  N   . GLN   E 2 674 ? 14.508  -12.138 -12.514 1.00 99.04  ? 978  GLN   E N   1 
ATOM   16294 C  CA  . GLN   E 2 674 ? 13.942  -10.966 -11.870 1.00 105.04 ? 978  GLN   E CA  1 
ATOM   16295 C  C   . GLN   E 2 674 ? 13.976  -11.105 -10.357 1.00 111.08 ? 978  GLN   E C   1 
ATOM   16296 O  O   . GLN   E 2 674 ? 13.821  -12.199 -9.808  1.00 109.77 ? 978  GLN   E O   1 
ATOM   16297 C  CB  . GLN   E 2 674 ? 12.503  -10.739 -12.338 1.00 104.47 ? 978  GLN   E CB  1 
ATOM   16298 C  CG  . GLN   E 2 674 ? 11.594  -10.136 -11.295 1.00 110.42 ? 978  GLN   E CG  1 
ATOM   16299 C  CD  . GLN   E 2 674 ? 10.133  -10.299 -11.655 1.00 108.83 ? 978  GLN   E CD  1 
ATOM   16300 O  OE1 . GLN   E 2 674 ? 9.775   -10.336 -12.836 1.00 104.61 ? 978  GLN   E OE1 1 
ATOM   16301 N  NE2 . GLN   E 2 674 ? 9.278   -10.413 -10.637 1.00 116.32 ? 978  GLN   E NE2 1 
ATOM   16302 N  N   . LYS   E 2 675 ? 14.157  -9.967  -9.692  1.00 116.44 ? 979  LYS   E N   1 
ATOM   16303 C  CA  . LYS   E 2 675 ? 14.073  -9.896  -8.238  1.00 121.82 ? 979  LYS   E CA  1 
ATOM   16304 C  C   . LYS   E 2 675 ? 12.610  -9.942  -7.795  1.00 128.72 ? 979  LYS   E C   1 
ATOM   16305 O  O   . LYS   E 2 675 ? 11.808  -9.097  -8.207  1.00 130.52 ? 979  LYS   E O   1 
ATOM   16306 C  CB  . LYS   E 2 675 ? 14.746  -8.616  -7.743  1.00 120.42 ? 979  LYS   E CB  1 
ATOM   16307 N  N   . ASP   E 2 676 ? 12.258  -10.928 -6.967  1.00 144.92 ? 980  ASP   E N   1 
ATOM   16308 C  CA  . ASP   E 2 676 ? 10.892  -11.031 -6.454  1.00 150.81 ? 980  ASP   E CA  1 
ATOM   16309 C  C   . ASP   E 2 676 ? 10.596  -9.825  -5.562  1.00 151.86 ? 980  ASP   E C   1 
ATOM   16310 O  O   . ASP   E 2 676 ? 11.287  -9.597  -4.563  1.00 151.23 ? 980  ASP   E O   1 
ATOM   16311 C  CB  . ASP   E 2 676 ? 10.685  -12.344 -5.673  1.00 156.14 ? 980  ASP   E CB  1 
ATOM   16312 C  CG  . ASP   E 2 676 ? 10.829  -13.620 -6.541  1.00 155.01 ? 980  ASP   E CG  1 
ATOM   16313 O  OD1 . ASP   E 2 676 ? 11.553  -13.587 -7.563  1.00 149.37 ? 980  ASP   E OD1 1 
ATOM   16314 O  OD2 . ASP   E 2 676 ? 10.222  -14.662 -6.196  1.00 152.39 ? 980  ASP   E OD2 1 
ATOM   16315 N  N   . SER   E 2 677 ? 9.577   -9.046  -5.925  1.00 151.37 ? 981  SER   E N   1 
ATOM   16316 C  CA  . SER   E 2 677 ? 9.232   -7.835  -5.171  1.00 156.49 ? 981  SER   E CA  1 
ATOM   16317 C  C   . SER   E 2 677 ? 9.204   -8.105  -3.663  1.00 152.55 ? 981  SER   E C   1 
ATOM   16318 O  O   . SER   E 2 677 ? 9.297   -7.183  -2.854  1.00 146.39 ? 981  SER   E O   1 
ATOM   16319 C  CB  . SER   E 2 677 ? 7.877   -7.283  -5.632  1.00 157.29 ? 981  SER   E CB  1 
ATOM   16320 O  OG  . SER   E 2 677 ? 7.522   -7.811  -6.900  1.00 153.50 ? 981  SER   E OG  1 
ATOM   16321 N  N   . ALA   E 2 679 ? 7.898   -10.429 -2.385  1.00 138.42 ? 983  ALA   E N   1 
ATOM   16322 C  CA  . ALA   E 2 679 ? 8.722   -10.440 -1.181  1.00 144.06 ? 983  ALA   E CA  1 
ATOM   16323 C  C   . ALA   E 2 679 ? 8.089   -11.303 -0.071  1.00 150.28 ? 983  ALA   E C   1 
ATOM   16324 O  O   . ALA   E 2 679 ? 8.480   -11.196 1.098   1.00 149.25 ? 983  ALA   E O   1 
ATOM   16325 C  CB  . ALA   E 2 679 ? 8.946   -9.018  -0.690  1.00 136.25 ? 983  ALA   E CB  1 
ATOM   16326 N  N   . THR   E 2 680 ? 7.138   -12.160 -0.469  1.00 150.69 ? 984  THR   E N   1 
ATOM   16327 C  CA  . THR   E 2 680 ? 6.376   -13.045 0.419   1.00 149.65 ? 984  THR   E CA  1 
ATOM   16328 C  C   . THR   E 2 680 ? 7.205   -13.748 1.521   1.00 153.35 ? 984  THR   E C   1 
ATOM   16329 O  O   . THR   E 2 680 ? 6.833   -13.716 2.698   1.00 151.97 ? 984  THR   E O   1 
ATOM   16330 C  CB  . THR   E 2 680 ? 5.768   -14.227 -0.331  1.00 146.86 ? 984  THR   E CB  1 
ATOM   16331 O  OG1 . THR   E 2 680 ? 4.961   -13.741 -1.409  1.00 145.04 ? 984  THR   E OG1 1 
ATOM   16332 C  CG2 . THR   E 2 680 ? 4.903   -15.042 0.592   1.00 145.32 ? 984  THR   E CG2 1 
ATOM   16333 N  N   . THR   E 2 681 ? 8.302   -14.385 1.130   1.00 161.72 ? 985  THR   E N   1 
ATOM   16334 C  CA  . THR   E 2 681 ? 9.116   -15.135 2.020   1.00 163.82 ? 985  THR   E CA  1 
ATOM   16335 C  C   . THR   E 2 681 ? 10.580  -14.741 1.711   1.00 161.81 ? 985  THR   E C   1 
ATOM   16336 O  O   . THR   E 2 681 ? 10.878  -14.313 0.592   1.00 160.85 ? 985  THR   E O   1 
ATOM   16337 C  CB  . THR   E 2 681 ? 8.960   -16.664 1.941   1.00 163.21 ? 985  THR   E CB  1 
ATOM   16338 O  OG1 . THR   E 2 681 ? 9.260   -17.162 0.627   1.00 163.46 ? 985  THR   E OG1 1 
ATOM   16339 C  CG2 . THR   E 2 681 ? 7.529   -17.033 2.334   1.00 158.56 ? 985  THR   E CG2 1 
ATOM   16340 N  N   . ASP   E 2 682 ? 11.464  -14.854 2.708   1.00 157.69 ? 986  ASP   E N   1 
ATOM   16341 C  CA  . ASP   E 2 682 ? 12.888  -14.621 2.462   1.00 156.89 ? 986  ASP   E CA  1 
ATOM   16342 C  C   . ASP   E 2 682 ? 13.424  -15.508 1.348   1.00 154.03 ? 986  ASP   E C   1 
ATOM   16343 O  O   . ASP   E 2 682 ? 14.252  -15.081 0.535   1.00 151.10 ? 986  ASP   E O   1 
ATOM   16344 C  CB  . ASP   E 2 682 ? 13.683  -14.870 3.744   1.00 157.19 ? 986  ASP   E CB  1 
ATOM   16345 C  CG  . ASP   E 2 682 ? 13.876  -13.627 4.548   1.00 161.55 ? 986  ASP   E CG  1 
ATOM   16346 O  OD1 . ASP   E 2 682 ? 13.213  -12.612 4.252   1.00 163.13 ? 986  ASP   E OD1 1 
ATOM   16347 O  OD2 . ASP   E 2 682 ? 14.729  -13.674 5.468   1.00 166.24 ? 986  ASP   E OD2 1 
ATOM   16348 N  N   . GLU   E 2 683 ? 12.999  -16.769 1.325   1.00 154.78 ? 987  GLU   E N   1 
ATOM   16349 C  CA  . GLU   E 2 683 ? 13.388  -17.659 0.239   1.00 145.47 ? 987  GLU   E CA  1 
ATOM   16350 C  C   . GLU   E 2 683 ? 13.092  -17.033 -1.119  1.00 147.23 ? 987  GLU   E C   1 
ATOM   16351 O  O   . GLU   E 2 683 ? 13.933  -17.064 -2.025  1.00 141.19 ? 987  GLU   E O   1 
ATOM   16352 C  CB  . GLU   E 2 683 ? 12.668  -19.001 0.394   1.00 139.29 ? 987  GLU   E CB  1 
ATOM   16353 N  N   . GLU   E 2 684 ? 11.900  -16.442 -1.268  1.00 156.94 ? 988  GLU   E N   1 
ATOM   16354 C  CA  . GLU   E 2 684 ? 11.472  -15.923 -2.568  1.00 157.37 ? 988  GLU   E CA  1 
ATOM   16355 C  C   . GLU   E 2 684 ? 12.318  -14.729 -3.006  1.00 155.35 ? 988  GLU   E C   1 
ATOM   16356 O  O   . GLU   E 2 684 ? 12.833  -14.693 -4.130  1.00 153.45 ? 988  GLU   E O   1 
ATOM   16357 C  CB  . GLU   E 2 684 ? 9.990   -15.539 -2.525  1.00 158.48 ? 988  GLU   E CB  1 
ATOM   16358 N  N   . ARG   E 2 685 ? 12.470  -13.734 -2.124  1.00 146.33 ? 989  ARG   E N   1 
ATOM   16359 C  CA  . ARG   E 2 685 ? 13.222  -12.538 -2.483  1.00 143.39 ? 989  ARG   E CA  1 
ATOM   16360 C  C   . ARG   E 2 685 ? 14.714  -12.841 -2.675  1.00 134.75 ? 989  ARG   E C   1 
ATOM   16361 O  O   . ARG   E 2 685 ? 15.356  -12.211 -3.523  1.00 131.43 ? 989  ARG   E O   1 
ATOM   16362 C  CB  . ARG   E 2 685 ? 12.980  -11.441 -1.435  1.00 143.66 ? 989  ARG   E CB  1 
ATOM   16363 C  CG  . ARG   E 2 685 ? 13.060  -11.897 0.025   1.00 150.25 ? 989  ARG   E CG  1 
ATOM   16364 C  CD  . ARG   E 2 685 ? 12.434  -10.868 0.987   1.00 155.52 ? 989  ARG   E CD  1 
ATOM   16365 N  NE  . ARG   E 2 685 ? 12.995  -10.919 2.338   1.00 162.32 ? 989  ARG   E NE  1 
ATOM   16366 C  CZ  . ARG   E 2 685 ? 12.994  -9.900  3.195   1.00 163.51 ? 989  ARG   E CZ  1 
ATOM   16367 N  NH1 . ARG   E 2 685 ? 12.461  -8.727  2.879   1.00 164.06 ? 989  ARG   E NH1 1 
ATOM   16368 N  NH2 . ARG   E 2 685 ? 13.550  -10.057 4.397   1.00 156.48 ? 989  ARG   E NH2 1 
ATOM   16369 N  N   . GLN   E 2 686 ? 15.275  -13.817 -1.943  1.00 131.46 ? 990  GLN   E N   1 
ATOM   16370 C  CA  . GLN   E 2 686 ? 16.672  -14.202 -2.117  1.00 123.12 ? 990  GLN   E CA  1 
ATOM   16371 C  C   . GLN   E 2 686 ? 16.900  -15.082 -3.346  1.00 121.91 ? 990  GLN   E C   1 
ATOM   16372 O  O   . GLN   E 2 686 ? 18.048  -15.493 -3.593  1.00 113.84 ? 990  GLN   E O   1 
ATOM   16373 C  CB  . GLN   E 2 686 ? 17.195  -14.918 -0.858  1.00 119.16 ? 990  GLN   E CB  1 
ATOM   16374 N  N   . HIS   E 2 687 ? 15.853  -15.396 -4.115  1.00 120.85 ? 991  HIS   E N   1 
ATOM   16375 C  CA  . HIS   E 2 687 ? 15.975  -16.162 -5.352  1.00 114.49 ? 991  HIS   E CA  1 
ATOM   16376 C  C   . HIS   E 2 687 ? 15.527  -15.323 -6.539  1.00 110.51 ? 991  HIS   E C   1 
ATOM   16377 O  O   . HIS   E 2 687 ? 14.475  -14.676 -6.494  1.00 112.76 ? 991  HIS   E O   1 
ATOM   16378 C  CB  . HIS   E 2 687 ? 15.161  -17.459 -5.337  1.00 116.42 ? 991  HIS   E CB  1 
ATOM   16379 C  CG  . HIS   E 2 687 ? 15.169  -18.179 -6.657  1.00 111.52 ? 991  HIS   E CG  1 
ATOM   16380 N  ND1 . HIS   E 2 687 ? 14.041  -18.321 -7.446  1.00 109.30 ? 991  HIS   E ND1 1 
ATOM   16381 C  CD2 . HIS   E 2 687 ? 16.184  -18.761 -7.342  1.00 107.02 ? 991  HIS   E CD2 1 
ATOM   16382 C  CE1 . HIS   E 2 687 ? 14.359  -18.976 -8.550  1.00 108.02 ? 991  HIS   E CE1 1 
ATOM   16383 N  NE2 . HIS   E 2 687 ? 15.651  -19.255 -8.510  1.00 110.06 ? 991  HIS   E NE2 1 
ATOM   16384 N  N   . LEU   E 2 688 ? 16.319  -15.373 -7.606  1.00 105.92 ? 992  LEU   E N   1 
ATOM   16385 C  CA  . LEU   E 2 688 ? 16.028  -14.671 -8.847  1.00 103.90 ? 992  LEU   E CA  1 
ATOM   16386 C  C   . LEU   E 2 688 ? 15.182  -15.569 -9.751  1.00 103.92 ? 992  LEU   E C   1 
ATOM   16387 O  O   . LEU   E 2 688 ? 15.668  -16.589 -10.242 1.00 107.95 ? 992  LEU   E O   1 
ATOM   16388 C  CB  . LEU   E 2 688 ? 17.343  -14.277 -9.503  1.00 100.26 ? 992  LEU   E CB  1 
ATOM   16389 C  CG  . LEU   E 2 688 ? 18.108  -13.194 -8.751  1.00 103.06 ? 992  LEU   E CG  1 
ATOM   16390 C  CD1 . LEU   E 2 688 ? 19.572  -13.221 -9.174  1.00 99.17  ? 992  LEU   E CD1 1 
ATOM   16391 C  CD2 . LEU   E 2 688 ? 17.459  -11.837 -9.043  1.00 105.48 ? 992  LEU   E CD2 1 
ATOM   16392 N  N   . GLN   E 2 689 ? 13.912  -15.209 -9.958  1.00 103.37 ? 993  GLN   E N   1 
ATOM   16393 C  CA  . GLN   E 2 689 ? 12.965  -16.037 -10.695 1.00 102.85 ? 993  GLN   E CA  1 
ATOM   16394 C  C   . GLN   E 2 689 ? 13.137  -15.817 -12.195 1.00 104.27 ? 993  GLN   E C   1 
ATOM   16395 O  O   . GLN   E 2 689 ? 13.483  -14.719 -12.643 1.00 99.77  ? 993  GLN   E O   1 
ATOM   16396 C  CB  . GLN   E 2 689 ? 11.526  -15.723 -10.263 1.00 103.77 ? 993  GLN   E CB  1 
ATOM   16397 C  CG  . GLN   E 2 689 ? 10.549  -16.881 -10.371 1.00 112.41 ? 993  GLN   E CG  1 
ATOM   16398 C  CD  . GLN   E 2 689 ? 11.107  -18.193 -9.787  1.00 120.36 ? 993  GLN   E CD  1 
ATOM   16399 O  OE1 . GLN   E 2 689 ? 11.903  -18.896 -10.435 1.00 115.28 ? 993  GLN   E OE1 1 
ATOM   16400 N  NE2 . GLN   E 2 689 ? 10.685  -18.527 -8.563  1.00 114.47 ? 993  GLN   E NE2 1 
ATOM   16401 N  N   . GLU   E 2 690 ? 12.922  -16.885 -12.970 1.00 107.31 ? 994  GLU   E N   1 
ATOM   16402 C  CA  . GLU   E 2 690 ? 13.033  -16.826 -14.424 1.00 104.63 ? 994  GLU   E CA  1 
ATOM   16403 C  C   . GLU   E 2 690 ? 11.722  -16.354 -15.027 1.00 103.15 ? 994  GLU   E C   1 
ATOM   16404 O  O   . GLU   E 2 690 ? 10.669  -16.963 -14.804 1.00 104.86 ? 994  GLU   E O   1 
ATOM   16405 C  CB  . GLU   E 2 690 ? 13.400  -18.189 -15.000 1.00 107.37 ? 994  GLU   E CB  1 
ATOM   16406 C  CG  . GLU   E 2 690 ? 14.778  -18.676 -14.622 1.00 114.01 ? 994  GLU   E CG  1 
ATOM   16407 C  CD  . GLU   E 2 690 ? 15.030  -20.106 -15.097 1.00 123.70 ? 994  GLU   E CD  1 
ATOM   16408 O  OE1 . GLU   E 2 690 ? 14.299  -20.555 -16.025 1.00 115.80 ? 994  GLU   E OE1 1 
ATOM   16409 O  OE2 . GLU   E 2 690 ? 15.940  -20.775 -14.528 1.00 120.74 ? 994  GLU   E OE2 1 
ATOM   16410 N  N   . VAL   E 2 691 ? 11.790  -15.276 -15.804 1.00 104.26 ? 995  VAL   E N   1 
ATOM   16411 C  CA  . VAL   E 2 691 ? 10.578  -14.668 -16.337 1.00 106.70 ? 995  VAL   E CA  1 
ATOM   16412 C  C   . VAL   E 2 691 ? 10.686  -14.517 -17.851 1.00 102.89 ? 995  VAL   E C   1 
ATOM   16413 O  O   . VAL   E 2 691 ? 9.906   -13.768 -18.459 1.00 103.36 ? 995  VAL   E O   1 
ATOM   16414 C  CB  . VAL   E 2 691 ? 10.289  -13.312 -15.648 1.00 105.42 ? 995  VAL   E CB  1 
ATOM   16415 C  CG1 . VAL   E 2 691 ? 10.520  -13.427 -14.143 1.00 105.22 ? 995  VAL   E CG1 1 
ATOM   16416 C  CG2 . VAL   E 2 691 ? 11.132  -12.185 -16.243 1.00 101.67 ? 995  VAL   E CG2 1 
ATOM   16417 N  N   . GLY   E 2 692 ? 11.630  -15.236 -18.473 1.00 89.98  ? 996  GLY   E N   1 
ATOM   16418 C  CA  . GLY   E 2 692 ? 11.792  -15.124 -19.909 1.00 89.34  ? 996  GLY   E CA  1 
ATOM   16419 C  C   . GLY   E 2 692 ? 12.829  -16.069 -20.484 1.00 88.46  ? 996  GLY   E C   1 
ATOM   16420 O  O   . GLY   E 2 692 ? 13.956  -16.153 -19.986 1.00 82.66  ? 996  GLY   E O   1 
ATOM   16421 N  N   . LEU   E 2 693 ? 12.462  -16.762 -21.564 1.00 89.64  ? 997  LEU   E N   1 
ATOM   16422 C  CA  . LEU   E 2 693 ? 13.383  -17.600 -22.318 1.00 83.82  ? 997  LEU   E CA  1 
ATOM   16423 C  C   . LEU   E 2 693 ? 13.176  -17.288 -23.793 1.00 81.74  ? 997  LEU   E C   1 
ATOM   16424 O  O   . LEU   E 2 693 ? 12.107  -16.827 -24.208 1.00 84.25  ? 997  LEU   E O   1 
ATOM   16425 C  CB  . LEU   E 2 693 ? 13.198  -19.097 -22.085 1.00 85.06  ? 997  LEU   E CB  1 
ATOM   16426 C  CG  . LEU   E 2 693 ? 13.276  -19.551 -20.633 1.00 86.60  ? 997  LEU   E CG  1 
ATOM   16427 C  CD1 . LEU   E 2 693 ? 13.632  -21.027 -20.556 1.00 91.72  ? 997  LEU   E CD1 1 
ATOM   16428 C  CD2 . LEU   E 2 693 ? 14.269  -18.704 -19.836 1.00 86.91  ? 997  LEU   E CD2 1 
ATOM   16429 N  N   . PHE   E 2 694 ? 14.213  -17.565 -24.587 1.00 74.98  ? 998  PHE   E N   1 
ATOM   16430 C  CA  . PHE   E 2 694 ? 14.153  -17.314 -26.025 1.00 80.48  ? 998  PHE   E CA  1 
ATOM   16431 C  C   . PHE   E 2 694 ? 15.380  -17.865 -26.759 1.00 83.09  ? 998  PHE   E C   1 
ATOM   16432 O  O   . PHE   E 2 694 ? 16.531  -17.609 -26.380 1.00 79.16  ? 998  PHE   E O   1 
ATOM   16433 C  CB  . PHE   E 2 694 ? 13.972  -15.812 -26.269 1.00 79.77  ? 998  PHE   E CB  1 
ATOM   16434 C  CG  . PHE   E 2 694 ? 13.761  -15.412 -27.713 1.00 78.46  ? 998  PHE   E CG  1 
ATOM   16435 C  CD1 . PHE   E 2 694 ? 12.503  -15.437 -28.280 1.00 80.66  ? 998  PHE   E CD1 1 
ATOM   16436 C  CD2 . PHE   E 2 694 ? 14.809  -14.910 -28.469 1.00 82.01  ? 998  PHE   E CD2 1 
ATOM   16437 C  CE1 . PHE   E 2 694 ? 12.305  -15.024 -29.593 1.00 82.24  ? 998  PHE   E CE1 1 
ATOM   16438 C  CE2 . PHE   E 2 694 ? 14.619  -14.492 -29.778 1.00 81.33  ? 998  PHE   E CE2 1 
ATOM   16439 C  CZ  . PHE   E 2 694 ? 13.364  -14.552 -30.340 1.00 83.31  ? 998  PHE   E CZ  1 
ATOM   16440 N  N   . HIS   E 2 695 ? 15.121  -18.666 -27.794 1.00 80.31  ? 999  HIS   E N   1 
ATOM   16441 C  CA  . HIS   E 2 695 ? 16.140  -19.152 -28.716 1.00 77.18  ? 999  HIS   E CA  1 
ATOM   16442 C  C   . HIS   E 2 695 ? 16.426  -18.020 -29.703 1.00 81.76  ? 999  HIS   E C   1 
ATOM   16443 O  O   . HIS   E 2 695 ? 15.691  -17.821 -30.677 1.00 81.42  ? 999  HIS   E O   1 
ATOM   16444 C  CB  . HIS   E 2 695 ? 15.663  -20.429 -29.409 1.00 82.23  ? 999  HIS   E CB  1 
ATOM   16445 C  CG  . HIS   E 2 695 ? 16.723  -21.136 -30.200 1.00 81.35  ? 999  HIS   E CG  1 
ATOM   16446 N  ND1 . HIS   E 2 695 ? 17.745  -21.843 -29.610 1.00 82.32  ? 999  HIS   E ND1 1 
ATOM   16447 C  CD2 . HIS   E 2 695 ? 16.923  -21.237 -31.536 1.00 82.33  ? 999  HIS   E CD2 1 
ATOM   16448 C  CE1 . HIS   E 2 695 ? 18.539  -22.334 -30.545 1.00 82.50  ? 999  HIS   E CE1 1 
ATOM   16449 N  NE2 . HIS   E 2 695 ? 18.062  -21.982 -31.724 1.00 79.75  ? 999  HIS   E NE2 1 
ATOM   16450 N  N   . LEU   E 2 696 ? 17.482  -17.246 -29.434 1.00 79.09  ? 1000 LEU   E N   1 
ATOM   16451 C  CA  . LEU   E 2 696 ? 17.945  -16.252 -30.397 1.00 75.46  ? 1000 LEU   E CA  1 
ATOM   16452 C  C   . LEU   E 2 696 ? 18.358  -16.924 -31.693 1.00 75.37  ? 1000 LEU   E C   1 
ATOM   16453 O  O   . LEU   E 2 696 ? 17.749  -16.715 -32.747 1.00 83.59  ? 1000 LEU   E O   1 
ATOM   16454 C  CB  . LEU   E 2 696 ? 19.122  -15.456 -29.830 1.00 77.33  ? 1000 LEU   E CB  1 
ATOM   16455 C  CG  . LEU   E 2 696 ? 19.475  -14.219 -30.662 1.00 78.72  ? 1000 LEU   E CG  1 
ATOM   16456 C  CD1 . LEU   E 2 696 ? 18.257  -13.287 -30.660 1.00 76.25  ? 1000 LEU   E CD1 1 
ATOM   16457 C  CD2 . LEU   E 2 696 ? 20.734  -13.520 -30.119 1.00 70.70  ? 1000 LEU   E CD2 1 
ATOM   16458 N  N   . GLY   E 2 697 ? 19.391  -17.746 -31.629 1.00 73.60  ? 1001 GLY   E N   1 
ATOM   16459 C  CA  . GLY   E 2 697 ? 19.938  -18.384 -32.805 1.00 71.82  ? 1001 GLY   E CA  1 
ATOM   16460 C  C   . GLY   E 2 697 ? 21.311  -17.883 -33.175 1.00 74.86  ? 1001 GLY   E C   1 
ATOM   16461 O  O   . GLY   E 2 697 ? 21.834  -18.281 -34.226 1.00 72.57  ? 1001 GLY   E O   1 
ATOM   16462 N  N   . GLU   E 2 698 ? 21.893  -16.991 -32.366 1.00 74.75  ? 1002 GLU   E N   1 
ATOM   16463 C  CA  . GLU   E 2 698 ? 23.288  -16.573 -32.474 1.00 72.17  ? 1002 GLU   E CA  1 
ATOM   16464 C  C   . GLU   E 2 698 ? 23.922  -16.734 -31.106 1.00 77.16  ? 1002 GLU   E C   1 
ATOM   16465 O  O   . GLU   E 2 698 ? 23.247  -17.034 -30.119 1.00 75.06  ? 1002 GLU   E O   1 
ATOM   16466 C  CB  . GLU   E 2 698 ? 23.449  -15.121 -32.947 1.00 73.23  ? 1002 GLU   E CB  1 
ATOM   16467 C  CG  . GLU   E 2 698 ? 22.487  -14.698 -34.029 1.00 71.00  ? 1002 GLU   E CG  1 
ATOM   16468 C  CD  . GLU   E 2 698 ? 22.937  -15.190 -35.377 1.00 75.52  ? 1002 GLU   E CD  1 
ATOM   16469 O  OE1 . GLU   E 2 698 ? 24.146  -15.500 -35.484 1.00 79.09  ? 1002 GLU   E OE1 1 
ATOM   16470 O  OE2 . GLU   E 2 698 ? 22.103  -15.274 -36.318 1.00 76.45  ? 1002 GLU   E OE2 1 
ATOM   16471 N  N   . PHE   E 2 699 ? 25.226  -16.519 -31.043 1.00 78.90  ? 1003 PHE   E N   1 
ATOM   16472 C  CA  . PHE   E 2 699 ? 25.981  -16.728 -29.816 1.00 75.82  ? 1003 PHE   E CA  1 
ATOM   16473 C  C   . PHE   E 2 699 ? 26.449  -15.361 -29.344 1.00 74.63  ? 1003 PHE   E C   1 
ATOM   16474 O  O   . PHE   E 2 699 ? 27.253  -14.715 -30.023 1.00 76.72  ? 1003 PHE   E O   1 
ATOM   16475 C  CB  . PHE   E 2 699 ? 27.146  -17.685 -30.066 1.00 77.26  ? 1003 PHE   E CB  1 
ATOM   16476 C  CG  . PHE   E 2 699 ? 28.029  -17.891 -28.878 1.00 78.12  ? 1003 PHE   E CG  1 
ATOM   16477 C  CD1 . PHE   E 2 699 ? 29.126  -17.071 -28.658 1.00 74.77  ? 1003 PHE   E CD1 1 
ATOM   16478 C  CD2 . PHE   E 2 699 ? 27.764  -18.901 -27.970 1.00 76.26  ? 1003 PHE   E CD2 1 
ATOM   16479 C  CE1 . PHE   E 2 699 ? 29.934  -17.271 -27.562 1.00 73.67  ? 1003 PHE   E CE1 1 
ATOM   16480 C  CE2 . PHE   E 2 699 ? 28.564  -19.083 -26.873 1.00 74.17  ? 1003 PHE   E CE2 1 
ATOM   16481 C  CZ  . PHE   E 2 699 ? 29.648  -18.277 -26.670 1.00 70.24  ? 1003 PHE   E CZ  1 
ATOM   16482 N  N   . VAL   E 2 700 ? 25.950  -14.909 -28.197 1.00 71.96  ? 1004 VAL   E N   1 
ATOM   16483 C  CA  . VAL   E 2 700 ? 26.164  -13.524 -27.788 1.00 75.63  ? 1004 VAL   E CA  1 
ATOM   16484 C  C   . VAL   E 2 700 ? 27.444  -13.400 -26.964 1.00 70.88  ? 1004 VAL   E C   1 
ATOM   16485 O  O   . VAL   E 2 700 ? 27.550  -13.968 -25.881 1.00 73.42  ? 1004 VAL   E O   1 
ATOM   16486 C  CB  . VAL   E 2 700 ? 24.950  -12.970 -27.027 1.00 76.09  ? 1004 VAL   E CB  1 
ATOM   16487 C  CG1 . VAL   E 2 700 ? 25.239  -11.549 -26.543 1.00 75.46  ? 1004 VAL   E CG1 1 
ATOM   16488 C  CG2 . VAL   E 2 700 ? 23.752  -12.943 -27.949 1.00 73.35  ? 1004 VAL   E CG2 1 
ATOM   16489 N  N   . ASN   E 2 701 ? 28.391  -12.613 -27.462 1.00 69.87  ? 1005 ASN   E N   1 
ATOM   16490 C  CA  . ASN   E 2 701 ? 29.633  -12.320 -26.764 1.00 71.60  ? 1005 ASN   E CA  1 
ATOM   16491 C  C   . ASN   E 2 701 ? 29.593  -11.055 -25.912 1.00 71.90  ? 1005 ASN   E C   1 
ATOM   16492 O  O   . ASN   E 2 701 ? 30.440  -10.898 -25.025 1.00 70.36  ? 1005 ASN   E O   1 
ATOM   16493 C  CB  . ASN   E 2 701 ? 30.772  -12.165 -27.773 1.00 73.55  ? 1005 ASN   E CB  1 
ATOM   16494 C  CG  . ASN   E 2 701 ? 31.463  -13.457 -28.049 1.00 77.26  ? 1005 ASN   E CG  1 
ATOM   16495 O  OD1 . ASN   E 2 701 ? 31.589  -14.315 -27.158 1.00 79.85  ? 1005 ASN   E OD1 1 
ATOM   16496 N  ND2 . ASN   E 2 701 ? 31.918  -13.623 -29.287 1.00 73.00  ? 1005 ASN   E ND2 1 
ATOM   16497 N  N   . VAL   E 2 702 ? 28.658  -10.147 -26.152 1.00 68.60  ? 1006 VAL   E N   1 
ATOM   16498 C  CA  . VAL   E 2 702 ? 28.748  -8.824  -25.557 1.00 69.04  ? 1006 VAL   E CA  1 
ATOM   16499 C  C   . VAL   E 2 702 ? 27.376  -8.182  -25.589 1.00 72.65  ? 1006 VAL   E C   1 
ATOM   16500 O  O   . VAL   E 2 702 ? 26.769  -8.069  -26.658 1.00 74.02  ? 1006 VAL   E O   1 
ATOM   16501 C  CB  . VAL   E 2 702 ? 29.776  -7.955  -26.309 1.00 75.78  ? 1006 VAL   E CB  1 
ATOM   16502 C  CG1 . VAL   E 2 702 ? 29.482  -7.960  -27.812 1.00 74.50  ? 1006 VAL   E CG1 1 
ATOM   16503 C  CG2 . VAL   E 2 702 ? 29.757  -6.528  -25.797 1.00 76.44  ? 1006 VAL   E CG2 1 
ATOM   16504 N  N   . PHE   E 2 703 ? 26.931  -7.677  -24.442 1.00 68.98  ? 1007 PHE   E N   1 
ATOM   16505 C  CA  . PHE   E 2 703 ? 25.676  -6.888  -24.409 1.00 76.95  ? 1007 PHE   E CA  1 
ATOM   16506 C  C   . PHE   E 2 703 ? 26.099  -5.462  -24.077 1.00 81.57  ? 1007 PHE   E C   1 
ATOM   16507 O  O   . PHE   E 2 703 ? 26.967  -5.295  -23.204 1.00 84.77  ? 1007 PHE   E O   1 
ATOM   16508 C  CB  . PHE   E 2 703 ? 24.699  -7.347  -23.328 1.00 77.65  ? 1007 PHE   E CB  1 
ATOM   16509 C  CG  . PHE   E 2 703 ? 23.969  -8.666  -23.533 1.00 80.50  ? 1007 PHE   E CG  1 
ATOM   16510 C  CD1 . PHE   E 2 703 ? 23.114  -8.851  -24.610 1.00 82.50  ? 1007 PHE   E CD1 1 
ATOM   16511 C  CD2 . PHE   E 2 703 ? 24.111  -9.704  -22.621 1.00 79.38  ? 1007 PHE   E CD2 1 
ATOM   16512 C  CE1 . PHE   E 2 703 ? 22.444  -10.050 -24.784 1.00 77.17  ? 1007 PHE   E CE1 1 
ATOM   16513 C  CE2 . PHE   E 2 703 ? 23.436  -10.898 -22.798 1.00 76.24  ? 1007 PHE   E CE2 1 
ATOM   16514 C  CZ  . PHE   E 2 703 ? 22.606  -11.070 -23.878 1.00 80.29  ? 1007 PHE   E CZ  1 
ATOM   16515 N  N   . CYS   E 2 704 ? 25.531  -4.463  -24.752 1.00 80.65  ? 1008 CYS   E N   1 
ATOM   16516 C  CA  . CYS   E 2 704 ? 25.941  -3.055  -24.521 1.00 83.60  ? 1008 CYS   E CA  1 
ATOM   16517 C  C   . CYS   E 2 704 ? 24.719  -2.137  -24.535 1.00 82.09  ? 1008 CYS   E C   1 
ATOM   16518 O  O   . CYS   E 2 704 ? 23.955  -2.194  -25.507 1.00 82.83  ? 1008 CYS   E O   1 
ATOM   16519 C  CB  . CYS   E 2 704 ? 26.856  -2.548  -25.621 1.00 84.86  ? 1008 CYS   E CB  1 
ATOM   16520 S  SG  . CYS   E 2 704 ? 26.985  -0.744  -25.650 1.00 85.22  ? 1008 CYS   E SG  1 
ATOM   16521 N  N   . HIS   E 2 705 ? 24.561  -1.315  -23.501 1.00 84.47  ? 1009 HIS   E N   1 
ATOM   16522 C  CA  . HIS   E 2 705 ? 23.435  -0.348  -23.468 1.00 80.82  ? 1009 HIS   E CA  1 
ATOM   16523 C  C   . HIS   E 2 705 ? 23.736  0.764   -24.470 1.00 83.27  ? 1009 HIS   E C   1 
ATOM   16524 O  O   . HIS   E 2 705 ? 24.872  1.270   -24.483 1.00 81.73  ? 1009 HIS   E O   1 
ATOM   16525 C  CB  . HIS   E 2 705 ? 23.206  0.158   -22.044 1.00 80.03  ? 1009 HIS   E CB  1 
ATOM   16526 C  CG  . HIS   E 2 705 ? 22.328  -0.718  -21.221 1.00 81.49  ? 1009 HIS   E CG  1 
ATOM   16527 N  ND1 . HIS   E 2 705 ? 20.954  -0.689  -21.298 1.00 82.78  ? 1009 HIS   E ND1 1 
ATOM   16528 C  CD2 . HIS   E 2 705 ? 22.630  -1.635  -20.300 1.00 80.80  ? 1009 HIS   E CD2 1 
ATOM   16529 C  CE1 . HIS   E 2 705 ? 20.453  -1.569  -20.444 1.00 90.25  ? 1009 HIS   E CE1 1 
ATOM   16530 N  NE2 . HIS   E 2 705 ? 21.455  -2.157  -19.830 1.00 94.07  ? 1009 HIS   E NE2 1 
ATOM   16531 N  N   . GLY   E 2 706 ? 22.748  1.139   -25.280 1.00 81.92  ? 1010 GLY   E N   1 
ATOM   16532 C  CA  . GLY   E 2 706 ? 22.952  2.126   -26.314 1.00 80.72  ? 1010 GLY   E CA  1 
ATOM   16533 C  C   . GLY   E 2 706 ? 21.887  1.995   -27.376 1.00 83.47  ? 1010 GLY   E C   1 
ATOM   16534 O  O   . GLY   E 2 706 ? 20.994  1.150   -27.305 1.00 82.78  ? 1010 GLY   E O   1 
ATOM   16535 N  N   . SER   E 2 707 ? 22.003  2.873   -28.361 1.00 82.38  ? 1011 SER   E N   1 
ATOM   16536 C  CA  . SER   E 2 707 ? 21.138  2.864   -29.518 1.00 83.38  ? 1011 SER   E CA  1 
ATOM   16537 C  C   . SER   E 2 707 ? 21.923  3.489   -30.659 1.00 88.65  ? 1011 SER   E C   1 
ATOM   16538 O  O   . SER   E 2 707 ? 22.900  4.211   -30.435 1.00 93.22  ? 1011 SER   E O   1 
ATOM   16539 C  CB  . SER   E 2 707 ? 19.832  3.612   -29.242 1.00 83.49  ? 1011 SER   E CB  1 
ATOM   16540 O  OG  . SER   E 2 707 ? 19.040  3.702   -30.414 1.00 89.45  ? 1011 SER   E OG  1 
ATOM   16541 N  N   . LEU   E 2 708 ? 21.518  3.172   -31.886 1.00 85.95  ? 1012 LEU   E N   1 
ATOM   16542 C  CA  . LEU   E 2 708 ? 22.146  3.736   -33.066 1.00 93.92  ? 1012 LEU   E CA  1 
ATOM   16543 C  C   . LEU   E 2 708 ? 21.237  4.737   -33.764 1.00 100.47 ? 1012 LEU   E C   1 
ATOM   16544 O  O   . LEU   E 2 708 ? 21.641  5.315   -34.782 1.00 97.95  ? 1012 LEU   E O   1 
ATOM   16545 C  CB  . LEU   E 2 708 ? 22.560  2.624   -34.043 1.00 98.35  ? 1012 LEU   E CB  1 
ATOM   16546 C  CG  . LEU   E 2 708 ? 23.630  1.547   -33.754 1.00 91.48  ? 1012 LEU   E CG  1 
ATOM   16547 C  CD1 . LEU   E 2 708 ? 24.142  1.001   -35.090 1.00 84.53  ? 1012 LEU   E CD1 1 
ATOM   16548 C  CD2 . LEU   E 2 708 ? 24.796  1.991   -32.839 1.00 83.71  ? 1012 LEU   E CD2 1 
ATOM   16549 N  N   . VAL   E 2 709 ? 20.024  4.947   -33.232 1.00 98.17  ? 1013 VAL   E N   1 
ATOM   16550 C  CA  . VAL   E 2 709 ? 19.038  5.914   -33.711 1.00 100.78 ? 1013 VAL   E CA  1 
ATOM   16551 C  C   . VAL   E 2 709 ? 19.156  7.192   -32.885 1.00 107.06 ? 1013 VAL   E C   1 
ATOM   16552 O  O   . VAL   E 2 709 ? 20.064  7.323   -32.056 1.00 110.25 ? 1013 VAL   E O   1 
ATOM   16553 C  CB  . VAL   E 2 709 ? 17.616  5.325   -33.662 1.00 94.46  ? 1013 VAL   E CB  1 
ATOM   16554 C  CG1 . VAL   E 2 709 ? 17.495  4.140   -34.591 1.00 90.37  ? 1013 VAL   E CG1 1 
ATOM   16555 C  CG2 . VAL   E 2 709 ? 17.245  4.920   -32.245 1.00 94.01  ? 1013 VAL   E CG2 1 
ATOM   16556 N  N   . MET   E 2 710 ? 18.241  8.139   -33.087 1.00 107.77 ? 1014 MET   E N   1 
ATOM   16557 C  CA  . MET   E 2 710 ? 18.397  9.445   -32.445 1.00 113.80 ? 1014 MET   E CA  1 
ATOM   16558 C  C   . MET   E 2 710 ? 17.323  9.732   -31.391 1.00 112.29 ? 1014 MET   E C   1 
ATOM   16559 O  O   . MET   E 2 710 ? 17.588  10.420  -30.397 1.00 109.06 ? 1014 MET   E O   1 
ATOM   16560 C  CB  . MET   E 2 710 ? 18.406  10.555  -33.495 1.00 118.63 ? 1014 MET   E CB  1 
ATOM   16561 C  CG  . MET   E 2 710 ? 19.155  11.802  -33.041 1.00 125.05 ? 1014 MET   E CG  1 
ATOM   16562 S  SD  . MET   E 2 710 ? 19.595  12.928  -34.404 1.00 131.08 ? 1014 MET   E SD  1 
ATOM   16563 C  CE  . MET   E 2 710 ? 21.179  12.296  -34.960 1.00 124.13 ? 1014 MET   E CE  1 
ATOM   16564 N  N   . PRO   E 2 719 ? 6.362   3.805   -25.456 1.00 115.40 ? 1023 PRO   E N   1 
ATOM   16565 C  CA  . PRO   E 2 719 ? 6.062   2.648   -26.318 1.00 117.27 ? 1023 PRO   E CA  1 
ATOM   16566 C  C   . PRO   E 2 719 ? 7.011   1.495   -26.021 1.00 116.40 ? 1023 PRO   E C   1 
ATOM   16567 O  O   . PRO   E 2 719 ? 6.625   0.337   -25.794 1.00 110.26 ? 1023 PRO   E O   1 
ATOM   16568 C  CB  . PRO   E 2 719 ? 6.294   3.194   -27.727 1.00 112.48 ? 1023 PRO   E CB  1 
ATOM   16569 C  CG  . PRO   E 2 719 ? 7.377   4.252   -27.528 1.00 116.80 ? 1023 PRO   E CG  1 
ATOM   16570 C  CD  . PRO   E 2 719 ? 7.128   4.853   -26.158 1.00 113.43 ? 1023 PRO   E CD  1 
ATOM   16571 N  N   . THR   E 2 720 ? 8.289   1.870   -26.022 1.00 114.07 ? 1024 THR   E N   1 
ATOM   16572 C  CA  . THR   E 2 720 ? 9.413   0.963   -25.858 1.00 111.90 ? 1024 THR   E CA  1 
ATOM   16573 C  C   . THR   E 2 720 ? 10.320  1.550   -24.784 1.00 112.38 ? 1024 THR   E C   1 
ATOM   16574 O  O   . THR   E 2 720 ? 10.754  2.700   -24.903 1.00 120.41 ? 1024 THR   E O   1 
ATOM   16575 C  CB  . THR   E 2 720 ? 10.163  0.799   -27.192 1.00 111.82 ? 1024 THR   E CB  1 
ATOM   16576 O  OG1 . THR   E 2 720 ? 11.400  0.094   -26.987 1.00 110.25 ? 1024 THR   E OG1 1 
ATOM   16577 C  CG2 . THR   E 2 720 ? 10.445  2.163   -27.823 1.00 114.19 ? 1024 THR   E CG2 1 
ATOM   16578 N  N   . GLN   E 2 721 ? 10.581  0.781   -23.731 1.00 115.60 ? 1025 GLN   E N   1 
ATOM   16579 C  CA  . GLN   E 2 721 ? 11.393  1.223   -22.599 1.00 114.70 ? 1025 GLN   E CA  1 
ATOM   16580 C  C   . GLN   E 2 721 ? 12.777  0.591   -22.694 1.00 115.99 ? 1025 GLN   E C   1 
ATOM   16581 O  O   . GLN   E 2 721 ? 12.928  -0.613  -22.453 1.00 117.16 ? 1025 GLN   E O   1 
ATOM   16582 C  CB  . GLN   E 2 721 ? 10.757  0.836   -21.264 1.00 116.86 ? 1025 GLN   E CB  1 
ATOM   16583 C  CG  . GLN   E 2 721 ? 9.302   1.253   -21.104 1.00 125.94 ? 1025 GLN   E CG  1 
ATOM   16584 C  CD  . GLN   E 2 721 ? 8.500   0.415   -20.076 1.00 129.15 ? 1025 GLN   E CD  1 
ATOM   16585 O  OE1 . GLN   E 2 721 ? 9.023   -0.490  -19.405 1.00 122.63 ? 1025 GLN   E OE1 1 
ATOM   16586 N  NE2 . GLN   E 2 721 ? 7.210   0.727   -19.965 1.00 134.44 ? 1025 GLN   E NE2 1 
ATOM   16587 N  N   . GLY   E 2 722 ? 13.791  1.398   -23.008 1.00 107.14 ? 1026 GLY   E N   1 
ATOM   16588 C  CA  . GLY   E 2 722 ? 15.178  0.969   -22.881 1.00 100.54 ? 1026 GLY   E CA  1 
ATOM   16589 C  C   . GLY   E 2 722 ? 15.790  0.507   -24.194 1.00 90.65  ? 1026 GLY   E C   1 
ATOM   16590 O  O   . GLY   E 2 722 ? 15.169  0.527   -25.262 1.00 93.39  ? 1026 GLY   E O   1 
ATOM   16591 N  N   . SER   E 2 723 ? 17.050  0.077   -24.108 1.00 82.04  ? 1027 SER   E N   1 
ATOM   16592 C  CA  . SER   E 2 723 ? 17.720  -0.307  -25.340 1.00 79.10  ? 1027 SER   E CA  1 
ATOM   16593 C  C   . SER   E 2 723 ? 19.035  -0.956  -24.925 1.00 86.10  ? 1027 SER   E C   1 
ATOM   16594 O  O   . SER   E 2 723 ? 19.836  -0.352  -24.195 1.00 84.44  ? 1027 SER   E O   1 
ATOM   16595 C  CB  . SER   E 2 723 ? 17.775  0.895   -26.270 1.00 75.86  ? 1027 SER   E CB  1 
ATOM   16596 O  OG  . SER   E 2 723 ? 18.728  0.709   -27.288 1.00 79.36  ? 1027 SER   E OG  1 
ATOM   16597 N  N   . VAL   E 2 724 ? 19.253  -2.194  -25.396 1.00 85.52  ? 1028 VAL   E N   1 
ATOM   16598 C  CA  . VAL   E 2 724 ? 20.471  -2.955  -25.141 1.00 81.21  ? 1028 VAL   E CA  1 
ATOM   16599 C  C   . VAL   E 2 724 ? 20.837  -3.546  -26.488 1.00 81.65  ? 1028 VAL   E C   1 
ATOM   16600 O  O   . VAL   E 2 724 ? 20.017  -4.223  -27.121 1.00 85.56  ? 1028 VAL   E O   1 
ATOM   16601 C  CB  . VAL   E 2 724 ? 20.394  -4.077  -24.095 1.00 80.09  ? 1028 VAL   E CB  1 
ATOM   16602 C  CG1 . VAL   E 2 724 ? 21.784  -4.377  -23.588 1.00 81.39  ? 1028 VAL   E CG1 1 
ATOM   16603 C  CG2 . VAL   E 2 724 ? 19.462  -3.712  -22.965 1.00 78.08  ? 1028 VAL   E CG2 1 
ATOM   16604 N  N   . LEU   E 2 725 ? 22.072  -3.315  -26.905 1.00 81.45  ? 1029 LEU   E N   1 
ATOM   16605 C  CA  . LEU   E 2 725 ? 22.609  -3.872  -28.135 1.00 81.72  ? 1029 LEU   E CA  1 
ATOM   16606 C  C   . LEU   E 2 725 ? 23.430  -5.116  -27.813 1.00 81.68  ? 1029 LEU   E C   1 
ATOM   16607 O  O   . LEU   E 2 725 ? 24.029  -5.218  -26.733 1.00 82.38  ? 1029 LEU   E O   1 
ATOM   16608 C  CB  . LEU   E 2 725 ? 23.464  -2.825  -28.856 1.00 80.70  ? 1029 LEU   E CB  1 
ATOM   16609 C  CG  . LEU   E 2 725 ? 22.676  -1.655  -29.448 1.00 79.36  ? 1029 LEU   E CG  1 
ATOM   16610 C  CD1 . LEU   E 2 725 ? 23.614  -0.590  -30.007 1.00 76.92  ? 1029 LEU   E CD1 1 
ATOM   16611 C  CD2 . LEU   E 2 725 ? 21.742  -2.187  -30.515 1.00 76.73  ? 1029 LEU   E CD2 1 
ATOM   16612 N  N   . PHE   E 2 726 ? 23.441  -6.081  -28.741 1.00 78.69  ? 1030 PHE   E N   1 
ATOM   16613 C  CA  . PHE   E 2 726 ? 24.318  -7.222  -28.545 1.00 73.84  ? 1030 PHE   E CA  1 
ATOM   16614 C  C   . PHE   E 2 726 ? 25.044  -7.610  -29.826 1.00 73.28  ? 1030 PHE   E C   1 
ATOM   16615 O  O   . PHE   E 2 726 ? 24.482  -7.545  -30.922 1.00 73.47  ? 1030 PHE   E O   1 
ATOM   16616 C  CB  . PHE   E 2 726 ? 23.560  -8.415  -27.952 1.00 72.93  ? 1030 PHE   E CB  1 
ATOM   16617 C  CG  . PHE   E 2 726 ? 22.342  -8.849  -28.715 1.00 73.06  ? 1030 PHE   E CG  1 
ATOM   16618 C  CD1 . PHE   E 2 726 ? 22.457  -9.696  -29.820 1.00 73.14  ? 1030 PHE   E CD1 1 
ATOM   16619 C  CD2 . PHE   E 2 726 ? 21.069  -8.504  -28.270 1.00 72.75  ? 1030 PHE   E CD2 1 
ATOM   16620 C  CE1 . PHE   E 2 726 ? 21.318  -10.139 -30.509 1.00 72.12  ? 1030 PHE   E CE1 1 
ATOM   16621 C  CE2 . PHE   E 2 726 ? 19.926  -8.963  -28.954 1.00 73.79  ? 1030 PHE   E CE2 1 
ATOM   16622 C  CZ  . PHE   E 2 726 ? 20.059  -9.773  -30.072 1.00 71.98  ? 1030 PHE   E CZ  1 
ATOM   16623 N  N   . GLY   E 2 727 ? 26.311  -7.995  -29.658 1.00 72.73  ? 1031 GLY   E N   1 
ATOM   16624 C  CA  . GLY   E 2 727 ? 27.122  -8.563  -30.717 1.00 72.88  ? 1031 GLY   E CA  1 
ATOM   16625 C  C   . GLY   E 2 727 ? 27.313  -10.069 -30.585 1.00 76.06  ? 1031 GLY   E C   1 
ATOM   16626 O  O   . GLY   E 2 727 ? 27.343  -10.628 -29.487 1.00 73.17  ? 1031 GLY   E O   1 
ATOM   16627 N  N   . THR   E 2 728 ? 27.451  -10.734 -31.720 1.00 78.08  ? 1032 THR   E N   1 
ATOM   16628 C  CA  . THR   E 2 728 ? 27.456  -12.183 -31.763 1.00 74.19  ? 1032 THR   E CA  1 
ATOM   16629 C  C   . THR   E 2 728 ? 28.636  -12.662 -32.583 1.00 80.42  ? 1032 THR   E C   1 
ATOM   16630 O  O   . THR   E 2 728 ? 29.380  -11.876 -33.189 1.00 78.08  ? 1032 THR   E O   1 
ATOM   16631 C  CB  . THR   E 2 728 ? 26.168  -12.724 -32.362 1.00 71.05  ? 1032 THR   E CB  1 
ATOM   16632 O  OG1 . THR   E 2 728 ? 26.073  -12.290 -33.726 1.00 69.41  ? 1032 THR   E OG1 1 
ATOM   16633 C  CG2 . THR   E 2 728 ? 24.992  -12.197 -31.584 1.00 70.51  ? 1032 THR   E CG2 1 
ATOM   16634 N  N   . VAL   E 2 729 ? 28.792  -13.984 -32.596 1.00 78.08  ? 1033 VAL   E N   1 
ATOM   16635 C  CA  . VAL   E 2 729 ? 29.954  -14.579 -33.237 1.00 76.05  ? 1033 VAL   E CA  1 
ATOM   16636 C  C   . VAL   E 2 729 ? 29.829  -14.604 -34.759 1.00 75.74  ? 1033 VAL   E C   1 
ATOM   16637 O  O   . VAL   E 2 729 ? 30.846  -14.752 -35.453 1.00 77.63  ? 1033 VAL   E O   1 
ATOM   16638 C  CB  . VAL   E 2 729 ? 30.188  -15.979 -32.646 1.00 74.77  ? 1033 VAL   E CB  1 
ATOM   16639 C  CG1 . VAL   E 2 729 ? 31.041  -16.828 -33.578 1.00 77.60  ? 1033 VAL   E CG1 1 
ATOM   16640 C  CG2 . VAL   E 2 729 ? 30.836  -15.852 -31.279 1.00 80.95  ? 1033 VAL   E CG2 1 
ATOM   16641 N  N   . ASN   E 2 730 ? 28.618  -14.456 -35.303 1.00 73.76  ? 1034 ASN   E N   1 
ATOM   16642 C  CA  . ASN   E 2 730 ? 28.432  -14.386 -36.747 1.00 75.41  ? 1034 ASN   E CA  1 
ATOM   16643 C  C   . ASN   E 2 730 ? 28.333  -12.966 -37.259 1.00 79.81  ? 1034 ASN   E C   1 
ATOM   16644 O  O   . ASN   E 2 730 ? 28.008  -12.765 -38.435 1.00 77.45  ? 1034 ASN   E O   1 
ATOM   16645 C  CB  . ASN   E 2 730 ? 27.197  -15.174 -37.156 1.00 77.75  ? 1034 ASN   E CB  1 
ATOM   16646 C  CG  . ASN   E 2 730 ? 27.316  -16.624 -36.781 1.00 82.76  ? 1034 ASN   E CG  1 
ATOM   16647 O  OD1 . ASN   E 2 730 ? 28.293  -17.305 -37.148 1.00 82.43  ? 1034 ASN   E OD1 1 
ATOM   16648 N  ND2 . ASN   E 2 730 ? 26.357  -17.101 -36.000 1.00 81.84  ? 1034 ASN   E ND2 1 
ATOM   16649 N  N   . GLY   E 2 731 ? 28.601  -11.982 -36.403 1.00 78.03  ? 1035 GLY   E N   1 
ATOM   16650 C  CA  . GLY   E 2 731 ? 28.479  -10.615 -36.852 1.00 77.53  ? 1035 GLY   E CA  1 
ATOM   16651 C  C   . GLY   E 2 731 ? 27.046  -10.147 -36.980 1.00 78.69  ? 1035 GLY   E C   1 
ATOM   16652 O  O   . GLY   E 2 731 ? 26.788  -9.111  -37.601 1.00 81.07  ? 1035 GLY   E O   1 
ATOM   16653 N  N   . MET   E 2 732 ? 26.097  -10.899 -36.437 1.00 77.91  ? 1036 MET   E N   1 
ATOM   16654 C  CA  . MET   E 2 732 ? 24.747  -10.401 -36.236 1.00 75.78  ? 1036 MET   E CA  1 
ATOM   16655 C  C   . MET   E 2 732 ? 24.766  -9.389  -35.093 1.00 75.56  ? 1036 MET   E C   1 
ATOM   16656 O  O   . MET   E 2 732 ? 25.527  -9.534  -34.135 1.00 76.77  ? 1036 MET   E O   1 
ATOM   16657 C  CB  . MET   E 2 732 ? 23.817  -11.585 -35.932 1.00 75.48  ? 1036 MET   E CB  1 
ATOM   16658 C  CG  . MET   E 2 732 ? 22.322  -11.332 -35.850 1.00 72.54  ? 1036 MET   E CG  1 
ATOM   16659 S  SD  . MET   E 2 732 ? 21.898  -10.756 -34.196 1.00 82.01  ? 1036 MET   E SD  1 
ATOM   16660 C  CE  . MET   E 2 732 ? 20.085  -10.857 -34.233 1.00 76.96  ? 1036 MET   E CE  1 
ATOM   16661 N  N   . ILE   E 2 733 ? 23.958  -8.337  -35.207 1.00 75.63  ? 1037 ILE   E N   1 
ATOM   16662 C  CA  . ILE   E 2 733 ? 23.821  -7.346  -34.143 1.00 75.20  ? 1037 ILE   E CA  1 
ATOM   16663 C  C   . ILE   E 2 733 ? 22.353  -7.218  -33.793 1.00 74.93  ? 1037 ILE   E C   1 
ATOM   16664 O  O   . ILE   E 2 733 ? 21.505  -7.110  -34.687 1.00 79.67  ? 1037 ILE   E O   1 
ATOM   16665 C  CB  . ILE   E 2 733 ? 24.395  -5.974  -34.541 1.00 72.53  ? 1037 ILE   E CB  1 
ATOM   16666 C  CG1 . ILE   E 2 733 ? 25.873  -6.107  -34.906 1.00 75.59  ? 1037 ILE   E CG1 1 
ATOM   16667 C  CG2 . ILE   E 2 733 ? 24.248  -5.026  -33.403 1.00 64.99  ? 1037 ILE   E CG2 1 
ATOM   16668 C  CD1 . ILE   E 2 733 ? 26.283  -5.328  -36.147 1.00 69.54  ? 1037 ILE   E CD1 1 
ATOM   16669 N  N   . GLY   E 2 734 ? 22.050  -7.222  -32.498 1.00 70.40  ? 1038 GLY   E N   1 
ATOM   16670 C  CA  . GLY   E 2 734 ? 20.679  -7.295  -32.052 1.00 75.98  ? 1038 GLY   E CA  1 
ATOM   16671 C  C   . GLY   E 2 734 ? 20.359  -6.222  -31.029 1.00 77.57  ? 1038 GLY   E C   1 
ATOM   16672 O  O   . GLY   E 2 734 ? 21.244  -5.637  -30.390 1.00 76.21  ? 1038 GLY   E O   1 
ATOM   16673 N  N   . LEU   E 2 735 ? 19.059  -5.983  -30.869 1.00 76.28  ? 1039 LEU   E N   1 
ATOM   16674 C  CA  . LEU   E 2 735 ? 18.583  -5.003  -29.909 1.00 78.25  ? 1039 LEU   E CA  1 
ATOM   16675 C  C   . LEU   E 2 735 ? 17.501  -5.636  -29.051 1.00 78.75  ? 1039 LEU   E C   1 
ATOM   16676 O  O   . LEU   E 2 735 ? 16.600  -6.303  -29.566 1.00 83.68  ? 1039 LEU   E O   1 
ATOM   16677 C  CB  . LEU   E 2 735 ? 18.057  -3.754  -30.612 1.00 83.35  ? 1039 LEU   E CB  1 
ATOM   16678 C  CG  . LEU   E 2 735 ? 17.697  -2.566  -29.719 1.00 77.28  ? 1039 LEU   E CG  1 
ATOM   16679 C  CD1 . LEU   E 2 735 ? 18.618  -1.418  -30.064 1.00 74.41  ? 1039 LEU   E CD1 1 
ATOM   16680 C  CD2 . LEU   E 2 735 ? 16.234  -2.149  -29.850 1.00 84.32  ? 1039 LEU   E CD2 1 
ATOM   16681 N  N   . VAL   E 2 736 ? 17.624  -5.458  -27.740 1.00 82.06  ? 1040 VAL   E N   1 
ATOM   16682 C  CA  . VAL   E 2 736 ? 16.589  -5.810  -26.783 1.00 85.44  ? 1040 VAL   E CA  1 
ATOM   16683 C  C   . VAL   E 2 736 ? 16.098  -4.535  -26.116 1.00 92.08  ? 1040 VAL   E C   1 
ATOM   16684 O  O   . VAL   E 2 736 ? 16.911  -3.696  -25.688 1.00 86.06  ? 1040 VAL   E O   1 
ATOM   16685 C  CB  . VAL   E 2 736 ? 17.107  -6.788  -25.726 1.00 79.61  ? 1040 VAL   E CB  1 
ATOM   16686 C  CG1 . VAL   E 2 736 ? 16.001  -7.090  -24.743 1.00 83.81  ? 1040 VAL   E CG1 1 
ATOM   16687 C  CG2 . VAL   E 2 736 ? 17.585  -8.043  -26.395 1.00 87.33  ? 1040 VAL   E CG2 1 
ATOM   16688 N  N   . THR   E 2 737 ? 14.770  -4.404  -26.020 1.00 96.60  ? 1041 THR   E N   1 
ATOM   16689 C  CA  . THR   E 2 737 ? 14.118  -3.366  -25.238 1.00 98.77  ? 1041 THR   E CA  1 
ATOM   16690 C  C   . THR   E 2 737 ? 12.908  -3.945  -24.510 1.00 102.03 ? 1041 THR   E C   1 
ATOM   16691 O  O   . THR   E 2 737 ? 12.376  -4.999  -24.889 1.00 102.23 ? 1041 THR   E O   1 
ATOM   16692 C  CB  . THR   E 2 737 ? 13.636  -2.213  -26.094 1.00 97.36  ? 1041 THR   E CB  1 
ATOM   16693 O  OG1 . THR   E 2 737 ? 13.285  -1.126  -25.227 1.00 101.27 ? 1041 THR   E OG1 1 
ATOM   16694 C  CG2 . THR   E 2 737 ? 12.403  -2.644  -26.853 1.00 102.75 ? 1041 THR   E CG2 1 
ATOM   16695 N  N   . SER   E 2 738 ? 12.445  -3.215  -23.488 1.00 102.99 ? 1042 SER   E N   1 
ATOM   16696 C  CA  . SER   E 2 738 ? 11.389  -3.687  -22.604 1.00 98.81  ? 1042 SER   E CA  1 
ATOM   16697 C  C   . SER   E 2 738 ? 10.025  -3.186  -23.044 1.00 102.67 ? 1042 SER   E C   1 
ATOM   16698 O  O   . SER   E 2 738 ? 9.895   -2.186  -23.751 1.00 108.61 ? 1042 SER   E O   1 
ATOM   16699 C  CB  . SER   E 2 738 ? 11.648  -3.254  -21.170 1.00 99.85  ? 1042 SER   E CB  1 
ATOM   16700 O  OG  . SER   E 2 738 ? 12.601  -4.111  -20.573 1.00 101.97 ? 1042 SER   E OG  1 
ATOM   16701 N  N   . LEU   E 2 739 ? 9.002   -3.904  -22.608 1.00 102.27 ? 1043 LEU   E N   1 
ATOM   16702 C  CA  . LEU   E 2 739 ? 7.629   -3.618  -22.965 1.00 104.45 ? 1043 LEU   E CA  1 
ATOM   16703 C  C   . LEU   E 2 739 ? 6.799   -3.570  -21.693 1.00 110.94 ? 1043 LEU   E C   1 
ATOM   16704 O  O   . LEU   E 2 739 ? 7.163   -4.153  -20.668 1.00 108.13 ? 1043 LEU   E O   1 
ATOM   16705 C  CB  . LEU   E 2 739 ? 7.064   -4.687  -23.916 1.00 106.43 ? 1043 LEU   E CB  1 
ATOM   16706 C  CG  . LEU   E 2 739 ? 7.857   -5.060  -25.171 1.00 101.44 ? 1043 LEU   E CG  1 
ATOM   16707 C  CD1 . LEU   E 2 739 ? 7.699   -6.528  -25.454 1.00 100.66 ? 1043 LEU   E CD1 1 
ATOM   16708 C  CD2 . LEU   E 2 739 ? 7.333   -4.292  -26.341 1.00 101.65 ? 1043 LEU   E CD2 1 
ATOM   16709 N  N   . SER   E 2 740 ? 5.678   -2.864  -21.768 1.00 127.42 ? 1044 SER   E N   1 
ATOM   16710 C  CA  . SER   E 2 740 ? 4.668   -2.952  -20.725 1.00 129.00 ? 1044 SER   E CA  1 
ATOM   16711 C  C   . SER   E 2 740 ? 3.846   -4.225  -20.898 1.00 129.54 ? 1044 SER   E C   1 
ATOM   16712 O  O   . SER   E 2 740 ? 3.676   -4.718  -22.019 1.00 129.93 ? 1044 SER   E O   1 
ATOM   16713 C  CB  . SER   E 2 740 ? 3.728   -1.761  -20.788 1.00 132.16 ? 1044 SER   E CB  1 
ATOM   16714 O  OG  . SER   E 2 740 ? 2.662   -2.054  -21.678 1.00 132.31 ? 1044 SER   E OG  1 
ATOM   16715 N  N   . GLU   E 2 741 ? 3.303   -4.737  -19.783 1.00 120.43 ? 1045 GLU   E N   1 
ATOM   16716 C  CA  . GLU   E 2 741 ? 2.414   -5.899  -19.847 1.00 116.31 ? 1045 GLU   E CA  1 
ATOM   16717 C  C   . GLU   E 2 741 ? 1.369   -5.739  -20.946 1.00 114.13 ? 1045 GLU   E C   1 
ATOM   16718 O  O   . GLU   E 2 741 ? 1.146   -6.653  -21.744 1.00 114.21 ? 1045 GLU   E O   1 
ATOM   16719 C  CB  . GLU   E 2 741 ? 1.726   -6.134  -18.498 1.00 113.10 ? 1045 GLU   E CB  1 
ATOM   16720 C  CG  . GLU   E 2 741 ? 0.753   -7.308  -18.520 1.00 117.63 ? 1045 GLU   E CG  1 
ATOM   16721 C  CD  . GLU   E 2 741 ? 0.645   -8.053  -17.190 1.00 120.51 ? 1045 GLU   E CD  1 
ATOM   16722 O  OE1 . GLU   E 2 741 ? 0.118   -7.457  -16.224 1.00 122.58 ? 1045 GLU   E OE1 1 
ATOM   16723 O  OE2 . GLU   E 2 741 ? 1.078   -9.234  -17.118 1.00 116.97 ? 1045 GLU   E OE2 1 
ATOM   16724 N  N   . SER   E 2 742 ? 0.718   -4.577  -20.996 1.00 116.29 ? 1046 SER   E N   1 
ATOM   16725 C  CA  . SER   E 2 742 ? -0.154  -4.219  -22.110 1.00 117.29 ? 1046 SER   E CA  1 
ATOM   16726 C  C   . SER   E 2 742 ? 0.350   -4.500  -23.515 1.00 116.04 ? 1046 SER   E C   1 
ATOM   16727 O  O   . SER   E 2 742 ? -0.382  -5.042  -24.351 1.00 114.02 ? 1046 SER   E O   1 
ATOM   16728 C  CB  . SER   E 2 742 ? -0.415  -2.716  -22.139 1.00 122.36 ? 1046 SER   E CB  1 
ATOM   16729 O  OG  . SER   E 2 742 ? -0.534  -2.274  -23.487 1.00 117.62 ? 1046 SER   E OG  1 
ATOM   16730 N  N   . TRP   E 2 743 ? 1.597   -4.108  -23.788 1.00 115.13 ? 1047 TRP   E N   1 
ATOM   16731 C  CA  . TRP   E 2 743 ? 2.102   -4.209  -25.151 1.00 113.97 ? 1047 TRP   E CA  1 
ATOM   16732 C  C   . TRP   E 2 743 ? 2.518   -5.664  -25.369 1.00 112.18 ? 1047 TRP   E C   1 
ATOM   16733 O  O   . TRP   E 2 743 ? 2.325   -6.210  -26.464 1.00 108.28 ? 1047 TRP   E O   1 
ATOM   16734 C  CB  . TRP   E 2 743 ? 3.269   -3.262  -25.394 1.00 116.25 ? 1047 TRP   E CB  1 
ATOM   16735 C  CG  . TRP   E 2 743 ? 2.853   -1.829  -25.699 1.00 121.59 ? 1047 TRP   E CG  1 
ATOM   16736 C  CD1 . TRP   E 2 743 ? 2.602   -0.840  -24.789 1.00 125.36 ? 1047 TRP   E CD1 1 
ATOM   16737 C  CD2 . TRP   E 2 743 ? 2.666   -1.232  -26.995 1.00 118.55 ? 1047 TRP   E CD2 1 
ATOM   16738 N  NE1 . TRP   E 2 743 ? 2.267   0.329   -25.437 1.00 120.56 ? 1047 TRP   E NE1 1 
ATOM   16739 C  CE2 . TRP   E 2 743 ? 2.299   0.114   -26.789 1.00 118.36 ? 1047 TRP   E CE2 1 
ATOM   16740 C  CE3 . TRP   E 2 743 ? 2.771   -1.704  -28.303 1.00 117.57 ? 1047 TRP   E CE3 1 
ATOM   16741 C  CZ2 . TRP   E 2 743 ? 2.036   0.985   -27.840 1.00 117.34 ? 1047 TRP   E CZ2 1 
ATOM   16742 C  CZ3 . TRP   E 2 743 ? 2.510   -0.828  -29.353 1.00 118.87 ? 1047 TRP   E CZ3 1 
ATOM   16743 C  CH2 . TRP   E 2 743 ? 2.147   0.496   -29.113 1.00 117.18 ? 1047 TRP   E CH2 1 
ATOM   16744 N  N   . TYR   E 2 744 ? 3.069   -6.320  -24.343 1.00 114.03 ? 1048 TYR   E N   1 
ATOM   16745 C  CA  . TYR   E 2 744 ? 3.532   -7.697  -24.530 1.00 111.30 ? 1048 TYR   E CA  1 
ATOM   16746 C  C   . TYR   E 2 744 ? 2.405   -8.615  -24.984 1.00 108.41 ? 1048 TYR   E C   1 
ATOM   16747 O  O   . TYR   E 2 744 ? 2.608   -9.477  -25.848 1.00 107.69 ? 1048 TYR   E O   1 
ATOM   16748 C  CB  . TYR   E 2 744 ? 4.148   -8.235  -23.250 1.00 104.86 ? 1048 TYR   E CB  1 
ATOM   16749 C  CG  . TYR   E 2 744 ? 4.439   -9.712  -23.291 1.00 105.57 ? 1048 TYR   E CG  1 
ATOM   16750 C  CD1 . TYR   E 2 744 ? 5.585   -10.189 -23.900 1.00 102.77 ? 1048 TYR   E CD1 1 
ATOM   16751 C  CD2 . TYR   E 2 744 ? 3.572   -10.631 -22.703 1.00 106.22 ? 1048 TYR   E CD2 1 
ATOM   16752 C  CE1 . TYR   E 2 744 ? 5.863   -11.534 -23.918 1.00 106.04 ? 1048 TYR   E CE1 1 
ATOM   16753 C  CE2 . TYR   E 2 744 ? 3.839   -11.977 -22.711 1.00 99.70  ? 1048 TYR   E CE2 1 
ATOM   16754 C  CZ  . TYR   E 2 744 ? 4.987   -12.428 -23.319 1.00 106.12 ? 1048 TYR   E CZ  1 
ATOM   16755 O  OH  . TYR   E 2 744 ? 5.263   -13.783 -23.335 1.00 110.83 ? 1048 TYR   E OH  1 
ATOM   16756 N  N   . ASN   E 2 745 ? 1.210   -8.445  -24.421 1.00 107.17 ? 1049 ASN   E N   1 
ATOM   16757 C  CA  . ASN   E 2 745 ? 0.104   -9.321  -24.784 1.00 111.02 ? 1049 ASN   E CA  1 
ATOM   16758 C  C   . ASN   E 2 745 ? -0.516  -8.953  -26.132 1.00 109.81 ? 1049 ASN   E C   1 
ATOM   16759 O  O   . ASN   E 2 745 ? -0.966  -9.843  -26.856 1.00 111.05 ? 1049 ASN   E O   1 
ATOM   16760 C  CB  . ASN   E 2 745 ? -0.934  -9.321  -23.661 1.00 107.74 ? 1049 ASN   E CB  1 
ATOM   16761 C  CG  . ASN   E 2 745 ? -0.392  -9.951  -22.378 1.00 112.31 ? 1049 ASN   E CG  1 
ATOM   16762 O  OD1 . ASN   E 2 745 ? 0.319   -10.961 -22.422 1.00 114.16 ? 1049 ASN   E OD1 1 
ATOM   16763 N  ND2 . ASN   E 2 745 ? -0.710  -9.351  -21.238 1.00 113.91 ? 1049 ASN   E ND2 1 
ATOM   16764 N  N   . LEU   E 2 746 ? -0.539  -7.669  -26.494 1.00 111.12 ? 1050 LEU   E N   1 
ATOM   16765 C  CA  . LEU   E 2 746 ? -0.988  -7.298  -27.833 1.00 108.47 ? 1050 LEU   E CA  1 
ATOM   16766 C  C   . LEU   E 2 746 ? -0.089  -7.915  -28.892 1.00 109.87 ? 1050 LEU   E C   1 
ATOM   16767 O  O   . LEU   E 2 746 ? -0.572  -8.509  -29.863 1.00 110.18 ? 1050 LEU   E O   1 
ATOM   16768 C  CB  . LEU   E 2 746 ? -1.014  -5.777  -27.991 1.00 103.21 ? 1050 LEU   E CB  1 
ATOM   16769 C  CG  . LEU   E 2 746 ? -1.547  -5.162  -29.300 1.00 105.54 ? 1050 LEU   E CG  1 
ATOM   16770 C  CD1 . LEU   E 2 746 ? -1.584  -3.651  -29.154 1.00 103.98 ? 1050 LEU   E CD1 1 
ATOM   16771 C  CD2 . LEU   E 2 746 ? -0.764  -5.522  -30.572 1.00 109.80 ? 1050 LEU   E CD2 1 
ATOM   16772 N  N   . LEU   E 2 747 ? 1.229   -7.746  -28.736 1.00 110.92 ? 1051 LEU   E N   1 
ATOM   16773 C  CA  . LEU   E 2 747 ? 2.181   -8.223  -29.738 1.00 111.55 ? 1051 LEU   E CA  1 
ATOM   16774 C  C   . LEU   E 2 747 ? 2.348   -9.735  -29.675 1.00 112.51 ? 1051 LEU   E C   1 
ATOM   16775 O  O   . LEU   E 2 747 ? 2.641   -10.372 -30.696 1.00 111.74 ? 1051 LEU   E O   1 
ATOM   16776 C  CB  . LEU   E 2 747 ? 3.549   -7.555  -29.556 1.00 105.98 ? 1051 LEU   E CB  1 
ATOM   16777 C  CG  . LEU   E 2 747 ? 3.742   -6.090  -29.919 1.00 102.01 ? 1051 LEU   E CG  1 
ATOM   16778 C  CD1 . LEU   E 2 747 ? 3.223   -5.864  -31.309 1.00 100.02 ? 1051 LEU   E CD1 1 
ATOM   16779 C  CD2 . LEU   E 2 747 ? 3.003   -5.229  -28.932 1.00 109.24 ? 1051 LEU   E CD2 1 
ATOM   16780 N  N   . LEU   E 2 748 ? 2.218   -10.317 -28.482 1.00 112.99 ? 1052 LEU   E N   1 
ATOM   16781 C  CA  . LEU   E 2 748 ? 2.087   -11.763 -28.385 1.00 112.83 ? 1052 LEU   E CA  1 
ATOM   16782 C  C   . LEU   E 2 748 ? 0.902   -12.233 -29.220 1.00 116.77 ? 1052 LEU   E C   1 
ATOM   16783 O  O   . LEU   E 2 748 ? 1.059   -13.012 -30.171 1.00 118.16 ? 1052 LEU   E O   1 
ATOM   16784 C  CB  . LEU   E 2 748 ? 1.940   -12.168 -26.917 1.00 109.51 ? 1052 LEU   E CB  1 
ATOM   16785 C  CG  . LEU   E 2 748 ? 1.898   -13.649 -26.530 1.00 110.38 ? 1052 LEU   E CG  1 
ATOM   16786 C  CD1 . LEU   E 2 748 ? 2.823   -14.518 -27.385 1.00 112.51 ? 1052 LEU   E CD1 1 
ATOM   16787 C  CD2 . LEU   E 2 748 ? 2.260   -13.771 -25.064 1.00 107.63 ? 1052 LEU   E CD2 1 
ATOM   16788 N  N   . ASP   E 2 749 ? -0.297  -11.740 -28.890 1.00 122.54 ? 1053 ASP   E N   1 
ATOM   16789 C  CA  . ASP   E 2 749 ? -1.464  -11.993 -29.727 1.00 125.20 ? 1053 ASP   E CA  1 
ATOM   16790 C  C   . ASP   E 2 749 ? -1.120  -11.776 -31.194 1.00 125.61 ? 1053 ASP   E C   1 
ATOM   16791 O  O   . ASP   E 2 749 ? -1.268  -12.685 -32.016 1.00 127.67 ? 1053 ASP   E O   1 
ATOM   16792 C  CB  . ASP   E 2 749 ? -2.623  -11.094 -29.301 1.00 127.58 ? 1053 ASP   E CB  1 
ATOM   16793 C  CG  . ASP   E 2 749 ? -3.985  -11.721 -29.551 1.00 134.24 ? 1053 ASP   E CG  1 
ATOM   16794 O  OD1 . ASP   E 2 749 ? -4.437  -12.507 -28.691 1.00 138.89 ? 1053 ASP   E OD1 1 
ATOM   16795 O  OD2 . ASP   E 2 749 ? -4.611  -11.414 -30.591 1.00 138.12 ? 1053 ASP   E OD2 1 
ATOM   16796 N  N   . MET   E 2 750 ? -0.639  -10.576 -31.534 1.00 118.01 ? 1054 MET   E N   1 
ATOM   16797 C  CA  . MET   E 2 750 ? -0.180  -10.281 -32.889 1.00 115.27 ? 1054 MET   E CA  1 
ATOM   16798 C  C   . MET   E 2 750 ? 0.649   -11.422 -33.498 1.00 115.04 ? 1054 MET   E C   1 
ATOM   16799 O  O   . MET   E 2 750 ? 0.273   -11.988 -34.534 1.00 116.26 ? 1054 MET   E O   1 
ATOM   16800 C  CB  . MET   E 2 750 ? 0.614   -8.971  -32.863 1.00 113.88 ? 1054 MET   E CB  1 
ATOM   16801 C  CG  . MET   E 2 750 ? -0.205  -7.751  -32.520 1.00 114.42 ? 1054 MET   E CG  1 
ATOM   16802 S  SD  . MET   E 2 750 ? -1.508  -7.579  -33.763 1.00 130.22 ? 1054 MET   E SD  1 
ATOM   16803 C  CE  . MET   E 2 750 ? -0.589  -7.193  -35.250 1.00 127.49 ? 1054 MET   E CE  1 
ATOM   16804 N  N   . GLN   E 2 751 ? 1.765   -11.790 -32.845 1.00 113.53 ? 1055 GLN   E N   1 
ATOM   16805 C  CA  . GLN   E 2 751 ? 2.670   -12.818 -33.371 1.00 110.67 ? 1055 GLN   E CA  1 
ATOM   16806 C  C   . GLN   E 2 751 ? 1.920   -14.042 -33.886 1.00 113.12 ? 1055 GLN   E C   1 
ATOM   16807 O  O   . GLN   E 2 751 ? 2.183   -14.526 -34.994 1.00 110.06 ? 1055 GLN   E O   1 
ATOM   16808 C  CB  . GLN   E 2 751 ? 3.663   -13.256 -32.294 1.00 111.63 ? 1055 GLN   E CB  1 
ATOM   16809 C  CG  . GLN   E 2 751 ? 4.914   -12.403 -32.124 1.00 108.92 ? 1055 GLN   E CG  1 
ATOM   16810 C  CD  . GLN   E 2 751 ? 5.900   -13.017 -31.121 1.00 106.36 ? 1055 GLN   E CD  1 
ATOM   16811 O  OE1 . GLN   E 2 751 ? 5.831   -14.212 -30.809 1.00 101.49 ? 1055 GLN   E OE1 1 
ATOM   16812 N  NE2 . GLN   E 2 751 ? 6.816   -12.195 -30.610 1.00 104.60 ? 1055 GLN   E NE2 1 
ATOM   16813 N  N   . ASN   E 2 752 ? 1.018   -14.590 -33.065 1.00 116.63 ? 1056 ASN   E N   1 
ATOM   16814 C  CA  . ASN   E 2 752 ? 0.274   -15.787 -33.458 1.00 116.46 ? 1056 ASN   E CA  1 
ATOM   16815 C  C   . ASN   E 2 752 ? -0.434  -15.576 -34.787 1.00 115.83 ? 1056 ASN   E C   1 
ATOM   16816 O  O   . ASN   E 2 752 ? -0.373  -16.431 -35.680 1.00 114.43 ? 1056 ASN   E O   1 
ATOM   16817 C  CB  . ASN   E 2 752 ? -0.749  -16.169 -32.384 1.00 117.64 ? 1056 ASN   E CB  1 
ATOM   16818 C  CG  . ASN   E 2 752 ? -0.096  -16.606 -31.065 1.00 127.17 ? 1056 ASN   E CG  1 
ATOM   16819 O  OD1 . ASN   E 2 752 ? -0.074  -17.799 -30.744 1.00 129.90 ? 1056 ASN   E OD1 1 
ATOM   16820 N  ND2 . ASN   E 2 752 ? 0.433   -15.638 -30.296 1.00 122.53 ? 1056 ASN   E ND2 1 
ATOM   16821 N  N   . ARG   E 2 753 ? -1.140  -14.447 -34.924 1.00 116.82 ? 1057 ARG   E N   1 
ATOM   16822 C  CA  . ARG   E 2 753 ? -1.883  -14.172 -36.149 1.00 114.71 ? 1057 ARG   E CA  1 
ATOM   16823 C  C   . ARG   E 2 753 ? -0.956  -14.200 -37.360 1.00 113.94 ? 1057 ARG   E C   1 
ATOM   16824 O  O   . ARG   E 2 753 ? -1.218  -14.900 -38.348 1.00 108.64 ? 1057 ARG   E O   1 
ATOM   16825 C  CB  . ARG   E 2 753 ? -2.608  -12.830 -36.037 1.00 108.80 ? 1057 ARG   E CB  1 
ATOM   16826 N  N   . LEU   E 2 754 ? 0.149   -13.448 -37.296 1.00 111.29 ? 1058 LEU   E N   1 
ATOM   16827 C  CA  . LEU   E 2 754 ? 1.094   -13.458 -38.407 1.00 108.09 ? 1058 LEU   E CA  1 
ATOM   16828 C  C   . LEU   E 2 754 ? 1.569   -14.872 -38.700 1.00 111.30 ? 1058 LEU   E C   1 
ATOM   16829 O  O   . LEU   E 2 754 ? 1.554   -15.313 -39.852 1.00 113.70 ? 1058 LEU   E O   1 
ATOM   16830 C  CB  . LEU   E 2 754 ? 2.281   -12.553 -38.118 1.00 106.10 ? 1058 LEU   E CB  1 
ATOM   16831 C  CG  . LEU   E 2 754 ? 1.936   -11.108 -37.833 1.00 110.25 ? 1058 LEU   E CG  1 
ATOM   16832 C  CD1 . LEU   E 2 754 ? 2.078   -10.904 -36.345 1.00 112.46 ? 1058 LEU   E CD1 1 
ATOM   16833 C  CD2 . LEU   E 2 754 ? 2.876   -10.209 -38.594 1.00 111.85 ? 1058 LEU   E CD2 1 
ATOM   16834 N  N   . ASN   E 2 755 ? 1.976   -15.609 -37.661 1.00 111.47 ? 1059 ASN   E N   1 
ATOM   16835 C  CA  . ASN   E 2 755 ? 2.536   -16.934 -37.899 1.00 107.18 ? 1059 ASN   E CA  1 
ATOM   16836 C  C   . ASN   E 2 755 ? 1.610   -17.804 -38.717 1.00 107.44 ? 1059 ASN   E C   1 
ATOM   16837 O  O   . ASN   E 2 755 ? 2.085   -18.670 -39.457 1.00 109.93 ? 1059 ASN   E O   1 
ATOM   16838 C  CB  . ASN   E 2 755 ? 2.874   -17.632 -36.597 1.00 102.29 ? 1059 ASN   E CB  1 
ATOM   16839 C  CG  . ASN   E 2 755 ? 4.340   -17.598 -36.327 1.00 105.82 ? 1059 ASN   E CG  1 
ATOM   16840 O  OD1 . ASN   E 2 755 ? 5.138   -17.349 -37.242 1.00 102.04 ? 1059 ASN   E OD1 1 
ATOM   16841 N  ND2 . ASN   E 2 755 ? 4.722   -17.826 -35.075 1.00 107.25 ? 1059 ASN   E ND2 1 
ATOM   16842 N  N   . LYS   E 2 756 ? 0.294   -17.592 -38.614 1.00 109.92 ? 1060 LYS   E N   1 
ATOM   16843 C  CA  . LYS   E 2 756 ? -0.620  -18.354 -39.460 1.00 109.87 ? 1060 LYS   E CA  1 
ATOM   16844 C  C   . LYS   E 2 756 ? -0.480  -17.965 -40.929 1.00 110.26 ? 1060 LYS   E C   1 
ATOM   16845 O  O   . LYS   E 2 756 ? -0.750  -18.789 -41.808 1.00 115.81 ? 1060 LYS   E O   1 
ATOM   16846 C  CB  . LYS   E 2 756 ? -2.063  -18.172 -38.989 1.00 102.32 ? 1060 LYS   E CB  1 
ATOM   16847 N  N   . VAL   E 2 757 ? -0.010  -16.747 -41.213 1.00 108.30 ? 1061 VAL   E N   1 
ATOM   16848 C  CA  . VAL   E 2 757 ? -0.025  -16.193 -42.566 1.00 107.44 ? 1061 VAL   E CA  1 
ATOM   16849 C  C   . VAL   E 2 757 ? 1.357   -16.182 -43.219 1.00 110.60 ? 1061 VAL   E C   1 
ATOM   16850 O  O   . VAL   E 2 757 ? 1.457   -16.238 -44.449 1.00 117.02 ? 1061 VAL   E O   1 
ATOM   16851 C  CB  . VAL   E 2 757 ? -0.617  -14.768 -42.574 1.00 109.23 ? 1061 VAL   E CB  1 
ATOM   16852 C  CG1 . VAL   E 2 757 ? -1.857  -14.693 -41.688 1.00 111.44 ? 1061 VAL   E CG1 1 
ATOM   16853 C  CG2 . VAL   E 2 757 ? 0.428   -13.729 -42.154 1.00 112.03 ? 1061 VAL   E CG2 1 
ATOM   16854 N  N   . ILE   E 2 758 ? 2.436   -16.083 -42.428 1.00 110.06 ? 1062 ILE   E N   1 
ATOM   16855 C  CA  . ILE   E 2 758 ? 3.776   -16.067 -43.017 1.00 110.66 ? 1062 ILE   E CA  1 
ATOM   16856 C  C   . ILE   E 2 758 ? 4.162   -17.482 -43.424 1.00 111.56 ? 1062 ILE   E C   1 
ATOM   16857 O  O   . ILE   E 2 758 ? 3.780   -18.468 -42.778 1.00 113.93 ? 1062 ILE   E O   1 
ATOM   16858 C  CB  . ILE   E 2 758 ? 4.836   -15.471 -42.064 1.00 113.44 ? 1062 ILE   E CB  1 
ATOM   16859 C  CG1 . ILE   E 2 758 ? 4.297   -14.267 -41.253 1.00 113.80 ? 1062 ILE   E CG1 1 
ATOM   16860 C  CG2 . ILE   E 2 758 ? 6.121   -15.155 -42.854 1.00 110.11 ? 1062 ILE   E CG2 1 
ATOM   16861 C  CD1 . ILE   E 2 758 ? 3.816   -13.053 -42.063 1.00 106.25 ? 1062 ILE   E CD1 1 
ATOM   16862 N  N   . LYS   E 2 759 ? 4.857   -17.583 -44.554 1.00 110.50 ? 1063 LYS   E N   1 
ATOM   16863 C  CA  . LYS   E 2 759 ? 5.263   -18.913 -45.061 1.00 109.98 ? 1063 LYS   E CA  1 
ATOM   16864 C  C   . LYS   E 2 759 ? 6.682   -19.210 -44.573 1.00 117.88 ? 1063 LYS   E C   1 
ATOM   16865 O  O   . LYS   E 2 759 ? 7.570   -18.363 -44.790 1.00 122.14 ? 1063 LYS   E O   1 
ATOM   16866 C  CB  . LYS   E 2 759 ? 5.211   -18.911 -46.589 1.00 104.95 ? 1063 LYS   E CB  1 
ATOM   16867 N  N   . SER   E 2 760 ? 6.878   -20.366 -43.942 1.00 117.53 ? 1064 SER   E N   1 
ATOM   16868 C  CA  . SER   E 2 760 ? 8.212   -20.723 -43.404 1.00 112.72 ? 1064 SER   E CA  1 
ATOM   16869 C  C   . SER   E 2 760 ? 8.922   -21.673 -44.366 1.00 112.94 ? 1064 SER   E C   1 
ATOM   16870 O  O   . SER   E 2 760 ? 8.430   -22.800 -44.548 1.00 117.34 ? 1064 SER   E O   1 
ATOM   16871 C  CB  . SER   E 2 760 ? 8.091   -21.354 -42.055 1.00 110.33 ? 1064 SER   E CB  1 
ATOM   16872 O  OG  . SER   E 2 760 ? 9.120   -22.314 -41.856 1.00 108.49 ? 1064 SER   E OG  1 
ATOM   16873 N  N   . VAL   E 2 761 ? 10.036  -21.240 -44.949 1.00 101.79 ? 1065 VAL   E N   1 
ATOM   16874 C  CA  . VAL   E 2 761 ? 10.815  -22.194 -45.785 1.00 102.41 ? 1065 VAL   E CA  1 
ATOM   16875 C  C   . VAL   E 2 761 ? 11.070  -23.424 -44.905 1.00 106.11 ? 1065 VAL   E C   1 
ATOM   16876 O  O   . VAL   E 2 761 ? 11.446  -23.239 -43.737 1.00 110.74 ? 1065 VAL   E O   1 
ATOM   16877 C  CB  . VAL   E 2 761 ? 12.118  -21.550 -46.285 1.00 99.07  ? 1065 VAL   E CB  1 
ATOM   16878 C  CG1 . VAL   E 2 761 ? 13.150  -22.590 -46.687 1.00 92.93  ? 1065 VAL   E CG1 1 
ATOM   16879 C  CG2 . VAL   E 2 761 ? 11.849  -20.605 -47.445 1.00 102.56 ? 1065 VAL   E CG2 1 
ATOM   16880 N  N   . GLY   E 2 762 ? 10.787  -24.618 -45.417 1.00 99.72  ? 1066 GLY   E N   1 
ATOM   16881 C  CA  . GLY   E 2 762 ? 10.986  -25.848 -44.634 1.00 97.21  ? 1066 GLY   E CA  1 
ATOM   16882 C  C   . GLY   E 2 762 ? 9.830   -26.116 -43.695 1.00 103.61 ? 1066 GLY   E C   1 
ATOM   16883 O  O   . GLY   E 2 762 ? 9.967   -27.006 -42.837 1.00 106.33 ? 1066 GLY   E O   1 
ATOM   16884 N  N   . LYS   E 2 763 ? 8.733   -25.380 -43.844 1.00 101.24 ? 1067 LYS   E N   1 
ATOM   16885 C  CA  . LYS   E 2 763 ? 7.525   -25.617 -43.012 1.00 100.24 ? 1067 LYS   E CA  1 
ATOM   16886 C  C   . LYS   E 2 763 ? 7.926   -25.733 -41.536 1.00 99.68  ? 1067 LYS   E C   1 
ATOM   16887 O  O   . LYS   E 2 763 ? 7.273   -26.506 -40.809 1.00 97.86  ? 1067 LYS   E O   1 
ATOM   16888 C  CB  . LYS   E 2 763 ? 6.776   -26.846 -43.529 1.00 91.75  ? 1067 LYS   E CB  1 
ATOM   16889 N  N   . ILE   E 2 764 ? 8.959   -25.004 -41.117 1.00 97.64  ? 1068 ILE   E N   1 
ATOM   16890 C  CA  . ILE   E 2 764 ? 9.352   -24.957 -39.705 1.00 94.47  ? 1068 ILE   E CA  1 
ATOM   16891 C  C   . ILE   E 2 764 ? 8.407   -24.040 -38.941 1.00 95.53  ? 1068 ILE   E C   1 
ATOM   16892 O  O   . ILE   E 2 764 ? 8.219   -22.875 -39.305 1.00 98.22  ? 1068 ILE   E O   1 
ATOM   16893 C  CB  . ILE   E 2 764 ? 10.798  -24.468 -39.542 1.00 93.05  ? 1068 ILE   E CB  1 
ATOM   16894 C  CG1 . ILE   E 2 764 ? 11.809  -25.528 -39.929 1.00 87.89  ? 1068 ILE   E CG1 1 
ATOM   16895 C  CG2 . ILE   E 2 764 ? 11.059  -24.085 -38.092 1.00 93.66  ? 1068 ILE   E CG2 1 
ATOM   16896 C  CD1 . ILE   E 2 764 ? 13.130  -24.929 -40.369 1.00 87.25  ? 1068 ILE   E CD1 1 
ATOM   16897 N  N   . GLU   E 2 765 ? 7.839   -24.543 -37.858 1.00 98.57  ? 1069 GLU   E N   1 
ATOM   16898 C  CA  . GLU   E 2 765 ? 6.885   -23.754 -37.110 1.00 100.01 ? 1069 GLU   E CA  1 
ATOM   16899 C  C   . GLU   E 2 765 ? 7.631   -22.785 -36.216 1.00 98.21  ? 1069 GLU   E C   1 
ATOM   16900 O  O   . GLU   E 2 765 ? 8.551   -23.187 -35.490 1.00 97.71  ? 1069 GLU   E O   1 
ATOM   16901 C  CB  . GLU   E 2 765 ? 5.983   -24.655 -36.284 1.00 102.83 ? 1069 GLU   E CB  1 
ATOM   16902 C  CG  . GLU   E 2 765 ? 4.614   -24.077 -36.090 1.00 110.92 ? 1069 GLU   E CG  1 
ATOM   16903 C  CD  . GLU   E 2 765 ? 3.955   -24.621 -34.843 1.00 126.90 ? 1069 GLU   E CD  1 
ATOM   16904 O  OE1 . GLU   E 2 765 ? 3.055   -23.942 -34.275 1.00 132.45 ? 1069 GLU   E OE1 1 
ATOM   16905 O  OE2 . GLU   E 2 765 ? 4.360   -25.740 -34.429 1.00 131.73 ? 1069 GLU   E OE2 1 
ATOM   16906 N  N   . HIS   E 2 766 ? 7.239   -21.503 -36.282 1.00 98.85  ? 1070 HIS   E N   1 
ATOM   16907 C  CA  . HIS   E 2 766 ? 7.959   -20.457 -35.557 1.00 92.98  ? 1070 HIS   E CA  1 
ATOM   16908 C  C   . HIS   E 2 766 ? 8.095   -20.815 -34.085 1.00 91.50  ? 1070 HIS   E C   1 
ATOM   16909 O  O   . HIS   E 2 766 ? 9.185   -20.720 -33.507 1.00 91.29  ? 1070 HIS   E O   1 
ATOM   16910 C  CB  . HIS   E 2 766 ? 7.253   -19.111 -35.725 1.00 98.53  ? 1070 HIS   E CB  1 
ATOM   16911 C  CG  . HIS   E 2 766 ? 7.913   -17.962 -35.011 1.00 95.56  ? 1070 HIS   E CG  1 
ATOM   16912 N  ND1 . HIS   E 2 766 ? 7.505   -17.523 -33.770 1.00 91.09  ? 1070 HIS   E ND1 1 
ATOM   16913 C  CD2 . HIS   E 2 766 ? 8.925   -17.137 -35.383 1.00 91.30  ? 1070 HIS   E CD2 1 
ATOM   16914 C  CE1 . HIS   E 2 766 ? 8.250   -16.496 -33.399 1.00 91.14  ? 1070 HIS   E CE1 1 
ATOM   16915 N  NE2 . HIS   E 2 766 ? 9.119   -16.239 -34.360 1.00 86.11  ? 1070 HIS   E NE2 1 
ATOM   16916 N  N   . SER   E 2 767 ? 6.998   -21.250 -33.468 1.00 93.66  ? 1071 SER   E N   1 
ATOM   16917 C  CA  . SER   E 2 767 ? 7.041   -21.745 -32.095 1.00 93.23  ? 1071 SER   E CA  1 
ATOM   16918 C  C   . SER   E 2 767 ? 8.217   -22.685 -31.850 1.00 89.99  ? 1071 SER   E C   1 
ATOM   16919 O  O   . SER   E 2 767 ? 9.019   -22.460 -30.938 1.00 88.15  ? 1071 SER   E O   1 
ATOM   16920 C  CB  . SER   E 2 767 ? 5.725   -22.452 -31.775 1.00 105.16 ? 1071 SER   E CB  1 
ATOM   16921 O  OG  . SER   E 2 767 ? 4.632   -21.626 -32.149 1.00 112.95 ? 1071 SER   E OG  1 
ATOM   16922 N  N   . PHE   E 2 768 ? 8.331   -23.741 -32.663 1.00 90.04  ? 1072 PHE   E N   1 
ATOM   16923 C  CA  . PHE   E 2 768 ? 9.405   -24.717 -32.490 1.00 90.74  ? 1072 PHE   E CA  1 
ATOM   16924 C  C   . PHE   E 2 768 ? 10.771  -24.047 -32.528 1.00 89.63  ? 1072 PHE   E C   1 
ATOM   16925 O  O   . PHE   E 2 768 ? 11.652  -24.353 -31.715 1.00 87.54  ? 1072 PHE   E O   1 
ATOM   16926 C  CB  . PHE   E 2 768 ? 9.319   -25.796 -33.576 1.00 93.48  ? 1072 PHE   E CB  1 
ATOM   16927 C  CG  . PHE   E 2 768 ? 10.460  -26.781 -33.547 1.00 86.43  ? 1072 PHE   E CG  1 
ATOM   16928 C  CD1 . PHE   E 2 768 ? 10.419  -27.873 -32.704 1.00 85.65  ? 1072 PHE   E CD1 1 
ATOM   16929 C  CD2 . PHE   E 2 768 ? 11.575  -26.611 -34.356 1.00 89.68  ? 1072 PHE   E CD2 1 
ATOM   16930 C  CE1 . PHE   E 2 768 ? 11.462  -28.777 -32.660 1.00 89.48  ? 1072 PHE   E CE1 1 
ATOM   16931 C  CE2 . PHE   E 2 768 ? 12.630  -27.513 -34.311 1.00 88.16  ? 1072 PHE   E CE2 1 
ATOM   16932 C  CZ  . PHE   E 2 768 ? 12.569  -28.594 -33.467 1.00 89.83  ? 1072 PHE   E CZ  1 
ATOM   16933 N  N   . TRP   E 2 769 ? 10.963  -23.137 -33.480 1.00 92.90  ? 1073 TRP   E N   1 
ATOM   16934 C  CA  . TRP   E 2 769 ? 12.266  -22.512 -33.678 1.00 90.11  ? 1073 TRP   E CA  1 
ATOM   16935 C  C   . TRP   E 2 769 ? 12.658  -21.642 -32.492 1.00 84.54  ? 1073 TRP   E C   1 
ATOM   16936 O  O   . TRP   E 2 769 ? 13.749  -21.793 -31.935 1.00 84.23  ? 1073 TRP   E O   1 
ATOM   16937 C  CB  . TRP   E 2 769 ? 12.223  -21.718 -34.981 1.00 86.72  ? 1073 TRP   E CB  1 
ATOM   16938 C  CG  . TRP   E 2 769 ? 13.088  -20.539 -35.084 1.00 80.74  ? 1073 TRP   E CG  1 
ATOM   16939 C  CD1 . TRP   E 2 769 ? 12.668  -19.264 -35.219 1.00 83.65  ? 1073 TRP   E CD1 1 
ATOM   16940 C  CD2 . TRP   E 2 769 ? 14.523  -20.502 -35.130 1.00 81.66  ? 1073 TRP   E CD2 1 
ATOM   16941 N  NE1 . TRP   E 2 769 ? 13.741  -18.414 -35.323 1.00 83.36  ? 1073 TRP   E NE1 1 
ATOM   16942 C  CE2 . TRP   E 2 769 ? 14.894  -19.152 -35.278 1.00 83.57  ? 1073 TRP   E CE2 1 
ATOM   16943 C  CE3 . TRP   E 2 769 ? 15.530  -21.472 -35.038 1.00 83.08  ? 1073 TRP   E CE3 1 
ATOM   16944 C  CZ2 . TRP   E 2 769 ? 16.231  -18.744 -35.337 1.00 82.63  ? 1073 TRP   E CZ2 1 
ATOM   16945 C  CZ3 . TRP   E 2 769 ? 16.864  -21.064 -35.110 1.00 78.77  ? 1073 TRP   E CZ3 1 
ATOM   16946 C  CH2 . TRP   E 2 769 ? 17.196  -19.716 -35.255 1.00 80.86  ? 1073 TRP   E CH2 1 
ATOM   16947 N  N   . ARG   E 2 770 ? 11.776  -20.727 -32.083 1.00 83.89  ? 1074 ARG   E N   1 
ATOM   16948 C  CA  . ARG   E 2 770 ? 12.076  -19.817 -30.977 1.00 85.33  ? 1074 ARG   E CA  1 
ATOM   16949 C  C   . ARG   E 2 770 ? 11.946  -20.481 -29.613 1.00 89.78  ? 1074 ARG   E C   1 
ATOM   16950 O  O   . ARG   E 2 770 ? 12.157  -19.799 -28.589 1.00 85.60  ? 1074 ARG   E O   1 
ATOM   16951 C  CB  . ARG   E 2 770 ? 11.171  -18.576 -31.047 1.00 84.15  ? 1074 ARG   E CB  1 
ATOM   16952 C  CG  . ARG   E 2 770 ? 11.432  -17.626 -32.227 1.00 82.18  ? 1074 ARG   E CG  1 
ATOM   16953 C  CD  . ARG   E 2 770 ? 12.890  -17.190 -32.282 1.00 80.07  ? 1074 ARG   E CD  1 
ATOM   16954 N  NE  . ARG   E 2 770 ? 13.094  -16.050 -33.174 1.00 85.77  ? 1074 ARG   E NE  1 
ATOM   16955 C  CZ  . ARG   E 2 770 ? 14.284  -15.553 -33.498 1.00 87.03  ? 1074 ARG   E CZ  1 
ATOM   16956 N  NH1 . ARG   E 2 770 ? 15.403  -16.089 -33.040 1.00 85.59  ? 1074 ARG   E NH1 1 
ATOM   16957 N  NH2 . ARG   E 2 770 ? 14.355  -14.496 -34.305 1.00 86.85  ? 1074 ARG   E NH2 1 
ATOM   16958 N  N   . SER   E 2 771 ? 11.617  -21.774 -29.561 1.00 91.06  ? 1075 SER   E N   1 
ATOM   16959 C  CA  . SER   E 2 771 ? 11.581  -22.490 -28.293 1.00 90.85  ? 1075 SER   E CA  1 
ATOM   16960 C  C   . SER   E 2 771 ? 12.989  -22.628 -27.736 1.00 89.49  ? 1075 SER   E C   1 
ATOM   16961 O  O   . SER   E 2 771 ? 13.944  -22.892 -28.472 1.00 87.21  ? 1075 SER   E O   1 
ATOM   16962 C  CB  . SER   E 2 771 ? 10.947  -23.874 -28.459 1.00 94.33  ? 1075 SER   E CB  1 
ATOM   16963 O  OG  . SER   E 2 771 ? 9.554   -23.790 -28.723 1.00 99.74  ? 1075 SER   E OG  1 
ATOM   16964 N  N   . PHE   E 2 772 ? 13.109  -22.425 -26.427 1.00 91.96  ? 1076 PHE   E N   1 
ATOM   16965 C  CA  . PHE   E 2 772 ? 14.387  -22.558 -25.743 1.00 94.51  ? 1076 PHE   E CA  1 
ATOM   16966 C  C   . PHE   E 2 772 ? 14.939  -23.970 -25.907 1.00 96.91  ? 1076 PHE   E C   1 
ATOM   16967 O  O   . PHE   E 2 772 ? 14.292  -24.941 -25.515 1.00 98.00  ? 1076 PHE   E O   1 
ATOM   16968 C  CB  . PHE   E 2 772 ? 14.195  -22.245 -24.261 1.00 97.07  ? 1076 PHE   E CB  1 
ATOM   16969 C  CG  . PHE   E 2 772 ? 15.456  -22.307 -23.447 1.00 93.39  ? 1076 PHE   E CG  1 
ATOM   16970 C  CD1 . PHE   E 2 772 ? 15.979  -23.516 -23.039 1.00 94.32  ? 1076 PHE   E CD1 1 
ATOM   16971 C  CD2 . PHE   E 2 772 ? 16.103  -21.145 -23.072 1.00 93.79  ? 1076 PHE   E CD2 1 
ATOM   16972 C  CE1 . PHE   E 2 772 ? 17.135  -23.565 -22.292 1.00 92.22  ? 1076 PHE   E CE1 1 
ATOM   16973 C  CE2 . PHE   E 2 772 ? 17.258  -21.190 -22.312 1.00 96.62  ? 1076 PHE   E CE2 1 
ATOM   16974 C  CZ  . PHE   E 2 772 ? 17.770  -22.406 -21.925 1.00 93.20  ? 1076 PHE   E CZ  1 
ATOM   16975 N  N   . HIS   E 2 773 ? 16.163  -24.078 -26.440 1.00 95.82  ? 1077 HIS   E N   1 
ATOM   16976 C  CA  . HIS   E 2 773 ? 16.757  -25.355 -26.830 1.00 101.35 ? 1077 HIS   E CA  1 
ATOM   16977 C  C   . HIS   E 2 773 ? 18.108  -25.554 -26.161 1.00 104.32 ? 1077 HIS   E C   1 
ATOM   16978 O  O   . HIS   E 2 773 ? 19.002  -24.713 -26.300 1.00 99.71  ? 1077 HIS   E O   1 
ATOM   16979 C  CB  . HIS   E 2 773 ? 16.897  -25.443 -28.357 1.00 106.39 ? 1077 HIS   E CB  1 
ATOM   16980 C  CG  . HIS   E 2 773 ? 17.692  -26.624 -28.837 1.00 108.85 ? 1077 HIS   E CG  1 
ATOM   16981 N  ND1 . HIS   E 2 773 ? 17.305  -27.932 -28.610 1.00 110.71 ? 1077 HIS   E ND1 1 
ATOM   16982 C  CD2 . HIS   E 2 773 ? 18.842  -26.689 -29.556 1.00 106.14 ? 1077 HIS   E CD2 1 
ATOM   16983 C  CE1 . HIS   E 2 773 ? 18.187  -28.749 -29.162 1.00 117.23 ? 1077 HIS   E CE1 1 
ATOM   16984 N  NE2 . HIS   E 2 773 ? 19.129  -28.022 -29.741 1.00 112.79 ? 1077 HIS   E NE2 1 
ATOM   16985 N  N   . THR   E 2 774 ? 18.234  -26.668 -25.426 1.00 115.47 ? 1078 THR   E N   1 
ATOM   16986 C  CA  . THR   E 2 774 ? 19.487  -27.243 -24.947 1.00 115.08 ? 1078 THR   E CA  1 
ATOM   16987 C  C   . THR   E 2 774 ? 19.674  -28.625 -25.577 1.00 122.47 ? 1078 THR   E C   1 
ATOM   16988 O  O   . THR   E 2 774 ? 18.745  -29.185 -26.178 1.00 118.90 ? 1078 THR   E O   1 
ATOM   16989 C  CB  . THR   E 2 774 ? 19.531  -27.350 -23.413 1.00 110.81 ? 1078 THR   E CB  1 
ATOM   16990 O  OG1 . THR   E 2 774 ? 18.233  -27.687 -22.894 1.00 117.56 ? 1078 THR   E OG1 1 
ATOM   16991 C  CG2 . THR   E 2 774 ? 19.976  -26.047 -22.816 1.00 99.63  ? 1078 THR   E CG2 1 
ATOM   16992 N  N   . GLU   E 2 775 ? 20.893  -29.162 -25.445 1.00 130.71 ? 1079 GLU   E N   1 
ATOM   16993 C  CA  . GLU   E 2 775 ? 21.219  -30.425 -26.099 1.00 136.23 ? 1079 GLU   E CA  1 
ATOM   16994 C  C   . GLU   E 2 775 ? 20.218  -31.521 -25.762 1.00 135.47 ? 1079 GLU   E C   1 
ATOM   16995 O  O   . GLU   E 2 775 ? 19.965  -32.402 -26.585 1.00 135.05 ? 1079 GLU   E O   1 
ATOM   16996 C  CB  . GLU   E 2 775 ? 22.639  -30.866 -25.725 1.00 137.47 ? 1079 GLU   E CB  1 
ATOM   16997 C  CG  . GLU   E 2 775 ? 23.744  -30.027 -26.368 1.00 138.74 ? 1079 GLU   E CG  1 
ATOM   16998 C  CD  . GLU   E 2 775 ? 24.638  -30.843 -27.298 1.00 141.13 ? 1079 GLU   E CD  1 
ATOM   16999 O  OE1 . GLU   E 2 775 ? 25.095  -30.296 -28.334 1.00 143.68 ? 1079 GLU   E OE1 1 
ATOM   17000 O  OE2 . GLU   E 2 775 ? 24.877  -32.031 -26.990 1.00 140.64 ? 1079 GLU   E OE2 1 
ATOM   17001 N  N   . ARG   E 2 776 ? 19.619  -31.482 -24.563 1.00 130.28 ? 1080 ARG   E N   1 
ATOM   17002 C  CA  . ARG   E 2 776 ? 18.659  -32.498 -24.146 1.00 130.92 ? 1080 ARG   E CA  1 
ATOM   17003 C  C   . ARG   E 2 776 ? 17.534  -31.886 -23.318 1.00 128.28 ? 1080 ARG   E C   1 
ATOM   17004 O  O   . ARG   E 2 776 ? 17.122  -32.439 -22.294 1.00 135.48 ? 1080 ARG   E O   1 
ATOM   17005 C  CB  . ARG   E 2 776 ? 19.347  -33.618 -23.362 1.00 136.06 ? 1080 ARG   E CB  1 
ATOM   17006 N  N   . LYS   E 2 777 ? 17.013  -30.738 -23.750 1.00 126.56 ? 1081 LYS   E N   1 
ATOM   17007 C  CA  . LYS   E 2 777 ? 15.807  -30.156 -23.166 1.00 124.28 ? 1081 LYS   E CA  1 
ATOM   17008 C  C   . LYS   E 2 777 ? 15.300  -29.049 -24.092 1.00 119.96 ? 1081 LYS   E C   1 
ATOM   17009 O  O   . LYS   E 2 777 ? 16.100  -28.314 -24.681 1.00 118.86 ? 1081 LYS   E O   1 
ATOM   17010 C  CB  . LYS   E 2 777 ? 16.071  -29.613 -21.747 1.00 124.03 ? 1081 LYS   E CB  1 
ATOM   17011 N  N   . THR   E 2 778 ? 13.972  -28.970 -24.254 1.00 111.44 ? 1082 THR   E N   1 
ATOM   17012 C  CA  . THR   E 2 778 ? 13.324  -27.923 -25.038 1.00 105.75 ? 1082 THR   E CA  1 
ATOM   17013 C  C   . THR   E 2 778 ? 12.117  -27.404 -24.278 1.00 109.15 ? 1082 THR   E C   1 
ATOM   17014 O  O   . THR   E 2 778 ? 11.465  -28.148 -23.536 1.00 103.91 ? 1082 THR   E O   1 
ATOM   17015 C  CB  . THR   E 2 778 ? 12.894  -28.399 -26.429 1.00 103.74 ? 1082 THR   E CB  1 
ATOM   17016 O  OG1 . THR   E 2 778 ? 12.385  -29.733 -26.352 1.00 121.89 ? 1082 THR   E OG1 1 
ATOM   17017 C  CG2 . THR   E 2 778 ? 14.083  -28.344 -27.392 1.00 108.83 ? 1082 THR   E CG2 1 
ATOM   17018 N  N   . GLU   E 2 779 ? 11.859  -26.109 -24.442 1.00 115.10 ? 1083 GLU   E N   1 
ATOM   17019 C  CA  . GLU   E 2 779 ? 10.919  -25.353 -23.630 1.00 114.13 ? 1083 GLU   E CA  1 
ATOM   17020 C  C   . GLU   E 2 779 ? 10.398  -24.182 -24.445 1.00 111.90 ? 1083 GLU   E C   1 
ATOM   17021 O  O   . GLU   E 2 779 ? 11.122  -23.642 -25.296 1.00 110.12 ? 1083 GLU   E O   1 
ATOM   17022 C  CB  . GLU   E 2 779 ? 11.568  -24.828 -22.343 1.00 114.80 ? 1083 GLU   E CB  1 
ATOM   17023 C  CG  . GLU   E 2 779 ? 10.610  -24.067 -21.431 1.00 121.13 ? 1083 GLU   E CG  1 
ATOM   17024 C  CD  . GLU   E 2 779 ? 11.076  -24.004 -19.966 1.00 127.87 ? 1083 GLU   E CD  1 
ATOM   17025 O  OE1 . GLU   E 2 779 ? 11.719  -24.972 -19.483 1.00 128.76 ? 1083 GLU   E OE1 1 
ATOM   17026 O  OE2 . GLU   E 2 779 ? 10.773  -22.996 -19.285 1.00 127.49 ? 1083 GLU   E OE2 1 
ATOM   17027 N  N   . PRO   E 2 780 ? 9.163   -23.758 -24.201 1.00 104.28 ? 1084 PRO   E N   1 
ATOM   17028 C  CA  . PRO   E 2 780 ? 8.542   -22.738 -25.052 1.00 101.93 ? 1084 PRO   E CA  1 
ATOM   17029 C  C   . PRO   E 2 780 ? 8.935   -21.343 -24.606 1.00 101.94 ? 1084 PRO   E C   1 
ATOM   17030 O  O   . PRO   E 2 780 ? 9.003   -21.032 -23.412 1.00 101.51 ? 1084 PRO   E O   1 
ATOM   17031 C  CB  . PRO   E 2 780 ? 7.045   -22.988 -24.853 1.00 100.16 ? 1084 PRO   E CB  1 
ATOM   17032 C  CG  . PRO   E 2 780 ? 6.962   -23.524 -23.456 1.00 104.25 ? 1084 PRO   E CG  1 
ATOM   17033 C  CD  . PRO   E 2 780 ? 8.218   -24.326 -23.223 1.00 103.64 ? 1084 PRO   E CD  1 
ATOM   17034 N  N   . ALA   E 2 781 ? 9.210   -20.493 -25.595 1.00 96.96  ? 1085 ALA   E N   1 
ATOM   17035 C  CA  . ALA   E 2 781 ? 9.694   -19.153 -25.314 1.00 92.99  ? 1085 ALA   E CA  1 
ATOM   17036 C  C   . ALA   E 2 781 ? 8.673   -18.354 -24.519 1.00 94.89  ? 1085 ALA   E C   1 
ATOM   17037 O  O   . ALA   E 2 781 ? 7.461   -18.587 -24.589 1.00 97.13  ? 1085 ALA   E O   1 
ATOM   17038 C  CB  . ALA   E 2 781 ? 10.027  -18.420 -26.611 1.00 89.38  ? 1085 ALA   E CB  1 
ATOM   17039 N  N   . THR   E 2 782 ? 9.171   -17.380 -23.769 1.00 92.66  ? 1086 THR   E N   1 
ATOM   17040 C  CA  . THR   E 2 782 ? 8.286   -16.725 -22.825 1.00 97.68  ? 1086 THR   E CA  1 
ATOM   17041 C  C   . THR   E 2 782 ? 8.840   -15.356 -22.477 1.00 96.43  ? 1086 THR   E C   1 
ATOM   17042 O  O   . THR   E 2 782 ? 10.015  -15.231 -22.120 1.00 96.51  ? 1086 THR   E O   1 
ATOM   17043 C  CB  . THR   E 2 782 ? 8.145   -17.568 -21.558 1.00 95.36  ? 1086 THR   E CB  1 
ATOM   17044 O  OG1 . THR   E 2 782 ? 7.222   -16.931 -20.667 1.00 101.13 ? 1086 THR   E OG1 1 
ATOM   17045 C  CG2 . THR   E 2 782 ? 9.500   -17.700 -20.893 1.00 91.33  ? 1086 THR   E CG2 1 
ATOM   17046 N  N   . GLY   E 2 783 ? 7.988   -14.340 -22.563 1.00 98.40  ? 1087 GLY   E N   1 
ATOM   17047 C  CA  . GLY   E 2 783 ? 8.433   -13.010 -22.212 1.00 96.88  ? 1087 GLY   E CA  1 
ATOM   17048 C  C   . GLY   E 2 783 ? 9.428   -12.424 -23.174 1.00 93.69  ? 1087 GLY   E C   1 
ATOM   17049 O  O   . GLY   E 2 783 ? 10.201  -11.548 -22.785 1.00 95.33  ? 1087 GLY   E O   1 
ATOM   17050 N  N   . PHE   E 2 784 ? 9.448   -12.905 -24.416 1.00 92.25  ? 1088 PHE   E N   1 
ATOM   17051 C  CA  . PHE   E 2 784 ? 10.170  -12.263 -25.506 1.00 92.04  ? 1088 PHE   E CA  1 
ATOM   17052 C  C   . PHE   E 2 784 ? 9.248   -12.143 -26.710 1.00 95.86  ? 1088 PHE   E C   1 
ATOM   17053 O  O   . PHE   E 2 784 ? 8.339   -12.960 -26.887 1.00 103.20 ? 1088 PHE   E O   1 
ATOM   17054 C  CB  . PHE   E 2 784 ? 11.418  -13.050 -25.896 1.00 91.06  ? 1088 PHE   E CB  1 
ATOM   17055 C  CG  . PHE   E 2 784 ? 12.600  -12.792 -25.013 1.00 88.66  ? 1088 PHE   E CG  1 
ATOM   17056 C  CD1 . PHE   E 2 784 ? 12.751  -13.471 -23.819 1.00 83.07  ? 1088 PHE   E CD1 1 
ATOM   17057 C  CD2 . PHE   E 2 784 ? 13.571  -11.866 -25.389 1.00 87.59  ? 1088 PHE   E CD2 1 
ATOM   17058 C  CE1 . PHE   E 2 784 ? 13.852  -13.226 -23.011 1.00 84.21  ? 1088 PHE   E CE1 1 
ATOM   17059 C  CE2 . PHE   E 2 784 ? 14.668  -11.623 -24.586 1.00 85.75  ? 1088 PHE   E CE2 1 
ATOM   17060 C  CZ  . PHE   E 2 784 ? 14.809  -12.301 -23.394 1.00 82.20  ? 1088 PHE   E CZ  1 
ATOM   17061 N  N   . ILE   E 2 785 ? 9.492   -11.133 -27.545 1.00 93.09  ? 1089 ILE   E N   1 
ATOM   17062 C  CA  . ILE   E 2 785 ? 8.745   -10.953 -28.789 1.00 92.41  ? 1089 ILE   E CA  1 
ATOM   17063 C  C   . ILE   E 2 785 ? 9.711   -10.831 -29.958 1.00 93.10  ? 1089 ILE   E C   1 
ATOM   17064 O  O   . ILE   E 2 785 ? 10.611  -9.979  -29.948 1.00 95.20  ? 1089 ILE   E O   1 
ATOM   17065 C  CB  . ILE   E 2 785 ? 7.817   -9.736  -28.726 1.00 94.16  ? 1089 ILE   E CB  1 
ATOM   17066 C  CG1 . ILE   E 2 785 ? 6.623   -10.108 -27.872 1.00 98.23  ? 1089 ILE   E CG1 1 
ATOM   17067 C  CG2 . ILE   E 2 785 ? 7.368   -9.290  -30.139 1.00 90.54  ? 1089 ILE   E CG2 1 
ATOM   17068 C  CD1 . ILE   E 2 785 ? 5.498   -9.188  -28.061 1.00 105.40 ? 1089 ILE   E CD1 1 
ATOM   17069 N  N   . ASP   E 2 786 ? 9.501   -11.670 -30.971 1.00 91.88  ? 1090 ASP   E N   1 
ATOM   17070 C  CA  . ASP   E 2 786 ? 10.356  -11.759 -32.152 1.00 91.16  ? 1090 ASP   E CA  1 
ATOM   17071 C  C   . ASP   E 2 786 ? 10.061  -10.563 -33.058 1.00 93.97  ? 1090 ASP   E C   1 
ATOM   17072 O  O   . ASP   E 2 786 ? 9.356   -10.657 -34.070 1.00 93.69  ? 1090 ASP   E O   1 
ATOM   17073 C  CB  . ASP   E 2 786 ? 10.119  -13.091 -32.858 1.00 91.16  ? 1090 ASP   E CB  1 
ATOM   17074 C  CG  . ASP   E 2 786 ? 11.001  -13.282 -34.064 1.00 88.55  ? 1090 ASP   E CG  1 
ATOM   17075 O  OD1 . ASP   E 2 786 ? 11.989  -12.533 -34.198 1.00 88.44  ? 1090 ASP   E OD1 1 
ATOM   17076 O  OD2 . ASP   E 2 786 ? 10.693  -14.183 -34.878 1.00 89.47  ? 1090 ASP   E OD2 1 
ATOM   17077 N  N   . GLY   E 2 787 ? 10.619  -9.413  -32.667 1.00 89.18  ? 1091 GLY   E N   1 
ATOM   17078 C  CA  . GLY   E 2 787 ? 10.505  -8.186  -33.424 1.00 89.59  ? 1091 GLY   E CA  1 
ATOM   17079 C  C   . GLY   E 2 787 ? 10.593  -8.359  -34.928 1.00 91.07  ? 1091 GLY   E C   1 
ATOM   17080 O  O   . GLY   E 2 787 ? 9.737   -7.865  -35.663 1.00 92.46  ? 1091 GLY   E O   1 
ATOM   17081 N  N   . ASP   E 2 788 ? 11.627  -9.054  -35.400 1.00 93.09  ? 1092 ASP   E N   1 
ATOM   17082 C  CA  . ASP   E 2 788 ? 11.699  -9.411  -36.809 1.00 94.06  ? 1092 ASP   E CA  1 
ATOM   17083 C  C   . ASP   E 2 788 ? 10.357  -9.928  -37.298 1.00 96.12  ? 1092 ASP   E C   1 
ATOM   17084 O  O   . ASP   E 2 788 ? 9.852   -9.481  -38.334 1.00 100.48 ? 1092 ASP   E O   1 
ATOM   17085 C  CB  . ASP   E 2 788 ? 12.785  -10.458 -37.034 1.00 92.02  ? 1092 ASP   E CB  1 
ATOM   17086 C  CG  . ASP   E 2 788 ? 14.160  -9.951  -36.679 1.00 94.60  ? 1092 ASP   E CG  1 
ATOM   17087 O  OD1 . ASP   E 2 788 ? 14.383  -8.717  -36.687 1.00 97.64  ? 1092 ASP   E OD1 1 
ATOM   17088 O  OD2 . ASP   E 2 788 ? 15.028  -10.797 -36.390 1.00 95.85  ? 1092 ASP   E OD2 1 
ATOM   17089 N  N   . LEU   E 2 789 ? 9.754   -10.867 -36.564 1.00 91.04  ? 1093 LEU   E N   1 
ATOM   17090 C  CA  . LEU   E 2 789 ? 8.459   -11.385 -36.990 1.00 92.01  ? 1093 LEU   E CA  1 
ATOM   17091 C  C   . LEU   E 2 789 ? 7.437   -10.265 -37.079 1.00 95.88  ? 1093 LEU   E C   1 
ATOM   17092 O  O   . LEU   E 2 789 ? 6.909   -9.964  -38.156 1.00 99.56  ? 1093 LEU   E O   1 
ATOM   17093 C  CB  . LEU   E 2 789 ? 7.966   -12.463 -36.038 1.00 95.78  ? 1093 LEU   E CB  1 
ATOM   17094 C  CG  . LEU   E 2 789 ? 6.602   -12.931 -36.543 1.00 98.54  ? 1093 LEU   E CG  1 
ATOM   17095 C  CD1 . LEU   E 2 789 ? 6.736   -13.563 -37.947 1.00 99.85  ? 1093 LEU   E CD1 1 
ATOM   17096 C  CD2 . LEU   E 2 789 ? 5.923   -13.884 -35.557 1.00 97.17  ? 1093 LEU   E CD2 1 
ATOM   17097 N  N   . ILE   E 2 790 ? 7.146   -9.637  -35.946 1.00 93.87  ? 1094 ILE   E N   1 
ATOM   17098 C  CA  . ILE   E 2 790 ? 6.286   -8.468  -35.878 1.00 92.94  ? 1094 ILE   E CA  1 
ATOM   17099 C  C   . ILE   E 2 790 ? 6.488   -7.483  -37.029 1.00 98.80  ? 1094 ILE   E C   1 
ATOM   17100 O  O   . ILE   E 2 790 ? 5.510   -6.994  -37.604 1.00 105.33 ? 1094 ILE   E O   1 
ATOM   17101 C  CB  . ILE   E 2 790 ? 6.530   -7.755  -34.547 1.00 94.64  ? 1094 ILE   E CB  1 
ATOM   17102 C  CG1 . ILE   E 2 790 ? 5.857   -8.535  -33.434 1.00 96.06  ? 1094 ILE   E CG1 1 
ATOM   17103 C  CG2 . ILE   E 2 790 ? 6.019   -6.327  -34.615 1.00 101.00 ? 1094 ILE   E CG2 1 
ATOM   17104 C  CD1 . ILE   E 2 790 ? 4.429   -8.140  -33.258 1.00 101.83 ? 1094 ILE   E CD1 1 
ATOM   17105 N  N   . GLU   E 2 791 ? 7.753   -7.192  -37.382 1.00 97.29  ? 1095 GLU   E N   1 
ATOM   17106 C  CA  . GLU   E 2 791 ? 8.051   -6.165  -38.389 1.00 97.69  ? 1095 GLU   E CA  1 
ATOM   17107 C  C   . GLU   E 2 791 ? 7.625   -6.623  -39.778 1.00 101.35 ? 1095 GLU   E C   1 
ATOM   17108 O  O   . GLU   E 2 791 ? 7.226   -5.798  -40.605 1.00 102.91 ? 1095 GLU   E O   1 
ATOM   17109 C  CB  . GLU   E 2 791 ? 9.547   -5.804  -38.408 1.00 95.18  ? 1095 GLU   E CB  1 
ATOM   17110 C  CG  . GLU   E 2 791 ? 10.029  -5.001  -37.179 1.00 97.72  ? 1095 GLU   E CG  1 
ATOM   17111 C  CD  . GLU   E 2 791 ? 11.350  -4.236  -37.387 1.00 100.34 ? 1095 GLU   E CD  1 
ATOM   17112 O  OE1 . GLU   E 2 791 ? 11.994  -4.351  -38.463 1.00 96.84  ? 1095 GLU   E OE1 1 
ATOM   17113 O  OE2 . GLU   E 2 791 ? 11.739  -3.505  -36.443 1.00 101.83 ? 1095 GLU   E OE2 1 
ATOM   17114 N  N   . SER   E 2 792 ? 7.710   -7.923  -40.060 1.00 104.29 ? 1096 SER   E N   1 
ATOM   17115 C  CA  . SER   E 2 792 ? 7.246   -8.437  -41.338 1.00 104.54 ? 1096 SER   E CA  1 
ATOM   17116 C  C   . SER   E 2 792 ? 5.749   -8.237  -41.539 1.00 111.05 ? 1096 SER   E C   1 
ATOM   17117 O  O   . SER   E 2 792 ? 5.283   -8.298  -42.678 1.00 114.63 ? 1096 SER   E O   1 
ATOM   17118 C  CB  . SER   E 2 792 ? 7.583   -9.908  -41.441 1.00 103.21 ? 1096 SER   E CB  1 
ATOM   17119 O  OG  . SER   E 2 792 ? 7.035   -10.569 -40.314 1.00 106.36 ? 1096 SER   E OG  1 
ATOM   17120 N  N   . PHE   E 2 793 ? 4.976   -8.022  -40.472 1.00 115.65 ? 1097 PHE   E N   1 
ATOM   17121 C  CA  . PHE   E 2 793 ? 3.581   -7.634  -40.659 1.00 117.61 ? 1097 PHE   E CA  1 
ATOM   17122 C  C   . PHE   E 2 793 ? 3.473   -6.446  -41.599 1.00 120.27 ? 1097 PHE   E C   1 
ATOM   17123 O  O   . PHE   E 2 793 ? 2.580   -6.398  -42.450 1.00 125.86 ? 1097 PHE   E O   1 
ATOM   17124 C  CB  . PHE   E 2 793 ? 2.936   -7.279  -39.320 1.00 119.37 ? 1097 PHE   E CB  1 
ATOM   17125 C  CG  . PHE   E 2 793 ? 1.743   -6.346  -39.438 1.00 127.69 ? 1097 PHE   E CG  1 
ATOM   17126 C  CD1 . PHE   E 2 793 ? 0.494   -6.831  -39.832 1.00 126.79 ? 1097 PHE   E CD1 1 
ATOM   17127 C  CD2 . PHE   E 2 793 ? 1.871   -4.984  -39.153 1.00 125.31 ? 1097 PHE   E CD2 1 
ATOM   17128 C  CE1 . PHE   E 2 793 ? -0.602  -5.978  -39.939 1.00 127.54 ? 1097 PHE   E CE1 1 
ATOM   17129 C  CE2 . PHE   E 2 793 ? 0.778   -4.126  -39.260 1.00 127.16 ? 1097 PHE   E CE2 1 
ATOM   17130 C  CZ  . PHE   E 2 793 ? -0.462  -4.628  -39.652 1.00 128.34 ? 1097 PHE   E CZ  1 
ATOM   17131 N  N   . LEU   E 2 794 ? 4.366   -5.459  -41.442 1.00 120.16 ? 1098 LEU   E N   1 
ATOM   17132 C  CA  . LEU   E 2 794 ? 4.337   -4.277  -42.296 1.00 117.30 ? 1098 LEU   E CA  1 
ATOM   17133 C  C   . LEU   E 2 794 ? 4.456   -4.647  -43.783 1.00 117.94 ? 1098 LEU   E C   1 
ATOM   17134 O  O   . LEU   E 2 794 ? 3.853   -3.978  -44.633 1.00 121.15 ? 1098 LEU   E O   1 
ATOM   17135 C  CB  . LEU   E 2 794 ? 5.451   -3.313  -41.875 1.00 114.49 ? 1098 LEU   E CB  1 
ATOM   17136 C  CG  . LEU   E 2 794 ? 5.235   -1.789  -41.923 1.00 117.54 ? 1098 LEU   E CG  1 
ATOM   17137 C  CD1 . LEU   E 2 794 ? 6.394   -1.072  -41.228 1.00 114.65 ? 1098 LEU   E CD1 1 
ATOM   17138 C  CD2 . LEU   E 2 794 ? 5.077   -1.290  -43.358 1.00 122.32 ? 1098 LEU   E CD2 1 
ATOM   17139 N  N   . ASP   E 2 795 ? 5.151   -5.734  -44.115 1.00 118.68 ? 1099 ASP   E N   1 
ATOM   17140 C  CA  . ASP   E 2 795 ? 5.331   -6.155  -45.505 1.00 124.33 ? 1099 ASP   E CA  1 
ATOM   17141 C  C   . ASP   E 2 795 ? 4.355   -7.264  -45.900 1.00 127.56 ? 1099 ASP   E C   1 
ATOM   17142 O  O   . ASP   E 2 795 ? 4.774   -8.250  -46.494 1.00 130.43 ? 1099 ASP   E O   1 
ATOM   17143 C  CB  . ASP   E 2 795 ? 6.793   -6.609  -45.645 1.00 128.84 ? 1099 ASP   E CB  1 
ATOM   17144 C  CG  . ASP   E 2 795 ? 7.233   -7.146  -47.034 1.00 139.64 ? 1099 ASP   E CG  1 
ATOM   17145 O  OD1 . ASP   E 2 795 ? 6.458   -7.030  -48.070 1.00 143.36 ? 1099 ASP   E OD1 1 
ATOM   17146 O  OD2 . ASP   E 2 795 ? 8.372   -7.659  -47.043 1.00 142.65 ? 1099 ASP   E OD2 1 
ATOM   17147 N  N   . ILE   E 2 796 ? 3.066   -7.152  -45.603 1.00 127.18 ? 1100 ILE   E N   1 
ATOM   17148 C  CA  . ILE   E 2 796 ? 2.133   -8.093  -46.214 1.00 128.71 ? 1100 ILE   E CA  1 
ATOM   17149 C  C   . ILE   E 2 796 ? 1.060   -7.325  -46.978 1.00 138.22 ? 1100 ILE   E C   1 
ATOM   17150 O  O   . ILE   E 2 796 ? 1.074   -6.084  -47.030 1.00 142.38 ? 1100 ILE   E O   1 
ATOM   17151 C  CB  . ILE   E 2 796 ? 1.518   -9.036  -45.169 1.00 127.23 ? 1100 ILE   E CB  1 
ATOM   17152 C  CG1 . ILE   E 2 796 ? 0.651   -8.250  -44.188 1.00 131.97 ? 1100 ILE   E CG1 1 
ATOM   17153 C  CG2 . ILE   E 2 796 ? 2.618   -9.851  -44.472 1.00 120.99 ? 1100 ILE   E CG2 1 
ATOM   17154 C  CD1 . ILE   E 2 796 ? -0.060  -9.148  -43.199 1.00 131.57 ? 1100 ILE   E CD1 1 
ATOM   17155 N  N   . SER   E 2 797 ? 0.150   -8.057  -47.611 1.00 144.44 ? 1101 SER   E N   1 
ATOM   17156 C  CA  . SER   E 2 797 ? -0.900  -7.432  -48.402 1.00 145.06 ? 1101 SER   E CA  1 
ATOM   17157 C  C   . SER   E 2 797 ? -2.003  -6.898  -47.499 1.00 144.57 ? 1101 SER   E C   1 
ATOM   17158 O  O   . SER   E 2 797 ? -2.386  -7.544  -46.514 1.00 144.93 ? 1101 SER   E O   1 
ATOM   17159 C  CB  . SER   E 2 797 ? -1.486  -8.425  -49.401 1.00 145.33 ? 1101 SER   E CB  1 
ATOM   17160 O  OG  . SER   E 2 797 ? -2.418  -9.300  -48.788 1.00 145.79 ? 1101 SER   E OG  1 
ATOM   17161 N  N   . ARG   E 2 798 ? -2.532  -5.723  -47.854 1.00 142.44 ? 1102 ARG   E N   1 
ATOM   17162 C  CA  . ARG   E 2 798 ? -3.523  -5.070  -46.999 1.00 140.61 ? 1102 ARG   E CA  1 
ATOM   17163 C  C   . ARG   E 2 798 ? -4.740  -5.942  -46.690 1.00 142.53 ? 1102 ARG   E C   1 
ATOM   17164 O  O   . ARG   E 2 798 ? -5.298  -5.788  -45.590 1.00 142.28 ? 1102 ARG   E O   1 
ATOM   17165 C  CB  . ARG   E 2 798 ? -3.975  -3.733  -47.613 1.00 136.06 ? 1102 ARG   E CB  1 
ATOM   17166 C  CG  . ARG   E 2 798 ? -3.100  -2.530  -47.233 1.00 138.24 ? 1102 ARG   E CG  1 
ATOM   17167 C  CD  . ARG   E 2 798 ? -3.913  -1.227  -47.103 1.00 142.18 ? 1102 ARG   E CD  1 
ATOM   17168 N  NE  . ARG   E 2 798 ? -4.713  -1.181  -45.881 1.00 143.08 ? 1102 ARG   E NE  1 
ATOM   17169 C  CZ  . ARG   E 2 798 ? -4.830  -0.119  -45.091 1.00 140.55 ? 1102 ARG   E CZ  1 
ATOM   17170 N  NH1 . ARG   E 2 798 ? -4.189  1.010   -45.346 1.00 133.59 ? 1102 ARG   E NH1 1 
ATOM   17171 N  NH2 . ARG   E 2 798 ? -5.604  -0.194  -44.013 1.00 139.32 ? 1102 ARG   E NH2 1 
ATOM   17172 N  N   . PRO   E 2 799 ? -5.199  -6.845  -47.567 1.00 141.88 ? 1103 PRO   E N   1 
ATOM   17173 C  CA  . PRO   E 2 799 ? -6.183  -7.836  -47.103 1.00 142.08 ? 1103 PRO   E CA  1 
ATOM   17174 C  C   . PRO   E 2 799 ? -5.664  -8.641  -45.929 1.00 141.07 ? 1103 PRO   E C   1 
ATOM   17175 O  O   . PRO   E 2 799 ? -6.378  -8.836  -44.936 1.00 139.05 ? 1103 PRO   E O   1 
ATOM   17176 C  CB  . PRO   E 2 799 ? -6.409  -8.708  -48.345 1.00 141.60 ? 1103 PRO   E CB  1 
ATOM   17177 C  CG  . PRO   E 2 799 ? -5.177  -8.517  -49.168 1.00 141.99 ? 1103 PRO   E CG  1 
ATOM   17178 C  CD  . PRO   E 2 799 ? -4.812  -7.077  -48.967 1.00 138.71 ? 1103 PRO   E CD  1 
ATOM   17179 N  N   . LYS   E 2 800 ? -4.412  -9.093  -46.014 1.00 139.95 ? 1104 LYS   E N   1 
ATOM   17180 C  CA  . LYS   E 2 800 ? -3.825  -9.891  -44.945 1.00 138.33 ? 1104 LYS   E CA  1 
ATOM   17181 C  C   . LYS   E 2 800 ? -3.830  -9.132  -43.623 1.00 135.88 ? 1104 LYS   E C   1 
ATOM   17182 O  O   . LYS   E 2 800 ? -4.209  -9.682  -42.583 1.00 136.46 ? 1104 LYS   E O   1 
ATOM   17183 C  CB  . LYS   E 2 800 ? -2.406  -10.305 -45.332 1.00 139.40 ? 1104 LYS   E CB  1 
ATOM   17184 N  N   . MET   E 2 801 ? -3.402  -7.868  -43.639 1.00 138.54 ? 1105 MET   E N   1 
ATOM   17185 C  CA  . MET   E 2 801 ? -3.442  -7.064  -42.420 1.00 137.60 ? 1105 MET   E CA  1 
ATOM   17186 C  C   . MET   E 2 801 ? -4.853  -7.002  -41.858 1.00 140.52 ? 1105 MET   E C   1 
ATOM   17187 O  O   . MET   E 2 801 ? -5.048  -6.902  -40.640 1.00 137.58 ? 1105 MET   E O   1 
ATOM   17188 C  CB  . MET   E 2 801 ? -2.939  -5.653  -42.697 1.00 135.34 ? 1105 MET   E CB  1 
ATOM   17189 C  CG  . MET   E 2 801 ? -1.875  -5.563  -43.759 1.00 134.65 ? 1105 MET   E CG  1 
ATOM   17190 S  SD  . MET   E 2 801 ? -0.894  -4.072  -43.528 1.00 136.04 ? 1105 MET   E SD  1 
ATOM   17191 C  CE  . MET   E 2 801 ? 0.047   -4.049  -45.050 1.00 131.54 ? 1105 MET   E CE  1 
ATOM   17192 N  N   . GLN   E 2 802 ? -5.850  -7.027  -42.740 1.00 140.51 ? 1106 GLN   E N   1 
ATOM   17193 C  CA  . GLN   E 2 802 ? -7.229  -7.092  -42.287 1.00 142.09 ? 1106 GLN   E CA  1 
ATOM   17194 C  C   . GLN   E 2 802 ? -7.453  -8.365  -41.486 1.00 139.97 ? 1106 GLN   E C   1 
ATOM   17195 O  O   . GLN   E 2 802 ? -7.909  -8.328  -40.336 1.00 141.48 ? 1106 GLN   E O   1 
ATOM   17196 C  CB  . GLN   E 2 802 ? -8.171  -7.015  -43.489 1.00 144.31 ? 1106 GLN   E CB  1 
ATOM   17197 C  CG  . GLN   E 2 802 ? -8.041  -5.730  -44.302 1.00 140.05 ? 1106 GLN   E CG  1 
ATOM   17198 C  CD  . GLN   E 2 802 ? -8.557  -4.519  -43.548 1.00 139.98 ? 1106 GLN   E CD  1 
ATOM   17199 O  OE1 . GLN   E 2 802 ? -7.803  -3.602  -43.215 1.00 139.17 ? 1106 GLN   E OE1 1 
ATOM   17200 N  NE2 . GLN   E 2 802 ? -9.856  -4.516  -43.269 1.00 143.81 ? 1106 GLN   E NE2 1 
ATOM   17201 N  N   . GLU   E 2 803 ? -7.110  -9.508  -42.074 1.00 138.62 ? 1107 GLU   E N   1 
ATOM   17202 C  CA  . GLU   E 2 803 ? -7.291  -10.770 -41.369 1.00 141.35 ? 1107 GLU   E CA  1 
ATOM   17203 C  C   . GLU   E 2 803 ? -6.524  -10.777 -40.050 1.00 141.14 ? 1107 GLU   E C   1 
ATOM   17204 O  O   . GLU   E 2 803 ? -7.072  -11.132 -38.999 1.00 143.35 ? 1107 GLU   E O   1 
ATOM   17205 C  CB  . GLU   E 2 803 ? -6.860  -11.931 -42.261 1.00 143.47 ? 1107 GLU   E CB  1 
ATOM   17206 C  CG  . GLU   E 2 803 ? -7.223  -13.297 -41.706 1.00 147.07 ? 1107 GLU   E CG  1 
ATOM   17207 C  CD  . GLU   E 2 803 ? -6.980  -14.406 -42.712 1.00 153.99 ? 1107 GLU   E CD  1 
ATOM   17208 O  OE1 . GLU   E 2 803 ? -6.601  -14.087 -43.863 1.00 153.95 ? 1107 GLU   E OE1 1 
ATOM   17209 O  OE2 . GLU   E 2 803 ? -7.165  -15.591 -42.356 1.00 159.82 ? 1107 GLU   E OE2 1 
ATOM   17210 N  N   . VAL   E 2 804 ? -5.250  -10.382 -40.081 1.00 140.12 ? 1108 VAL   E N   1 
ATOM   17211 C  CA  . VAL   E 2 804 ? -4.457  -10.391 -38.862 1.00 136.11 ? 1108 VAL   E CA  1 
ATOM   17212 C  C   . VAL   E 2 804 ? -4.982  -9.423  -37.814 1.00 141.98 ? 1108 VAL   E C   1 
ATOM   17213 O  O   . VAL   E 2 804 ? -4.584  -9.512  -36.651 1.00 142.71 ? 1108 VAL   E O   1 
ATOM   17214 C  CB  . VAL   E 2 804 ? -2.982  -10.074 -39.179 1.00 133.57 ? 1108 VAL   E CB  1 
ATOM   17215 C  CG1 . VAL   E 2 804 ? -2.540  -10.827 -40.417 1.00 128.24 ? 1108 VAL   E CG1 1 
ATOM   17216 C  CG2 . VAL   E 2 804 ? -2.793  -8.583  -39.369 1.00 139.94 ? 1108 VAL   E CG2 1 
ATOM   17217 N  N   . VAL   E 2 805 ? -5.871  -8.498  -38.180 1.00 148.31 ? 1109 VAL   E N   1 
ATOM   17218 C  CA  . VAL   E 2 805 ? -6.405  -7.555  -37.203 1.00 150.36 ? 1109 VAL   E CA  1 
ATOM   17219 C  C   . VAL   E 2 805 ? -7.831  -7.892  -36.786 1.00 149.29 ? 1109 VAL   E C   1 
ATOM   17220 O  O   . VAL   E 2 805 ? -8.321  -7.337  -35.788 1.00 148.87 ? 1109 VAL   E O   1 
ATOM   17221 C  CB  . VAL   E 2 805 ? -6.314  -6.106  -37.735 1.00 150.90 ? 1109 VAL   E CB  1 
ATOM   17222 C  CG1 . VAL   E 2 805 ? -4.858  -5.731  -37.946 1.00 147.06 ? 1109 VAL   E CG1 1 
ATOM   17223 C  CG2 . VAL   E 2 805 ? -7.104  -5.933  -39.036 1.00 149.43 ? 1109 VAL   E CG2 1 
ATOM   17224 N  N   . ALA   E 2 806 ? -8.490  -8.813  -37.483 1.00 142.70 ? 1110 ALA   E N   1 
ATOM   17225 C  CA  . ALA   E 2 806 ? -9.901  -9.092  -37.243 1.00 139.11 ? 1110 ALA   E CA  1 
ATOM   17226 C  C   . ALA   E 2 806 ? -10.135 -9.529  -35.798 1.00 138.21 ? 1110 ALA   E C   1 
ATOM   17227 O  O   . ALA   E 2 806 ? -9.564  -10.524 -35.344 1.00 140.08 ? 1110 ALA   E O   1 
ATOM   17228 C  CB  . ALA   E 2 806 ? -10.392 -10.161 -38.212 1.00 132.35 ? 1110 ALA   E CB  1 
ATOM   17229 N  N   . ASN   E 2 807 ? -10.977 -8.781  -35.085 1.00 135.82 ? 1111 ASN   E N   1 
ATOM   17230 C  CA  . ASN   E 2 807 ? -11.397 -9.156  -33.742 1.00 135.98 ? 1111 ASN   E CA  1 
ATOM   17231 C  C   . ASN   E 2 807 ? -10.408 -8.906  -32.604 1.00 135.20 ? 1111 ASN   E C   1 
ATOM   17232 O  O   . ASN   E 2 807 ? -10.440 -9.609  -31.597 1.00 134.99 ? 1111 ASN   E O   1 
ATOM   17233 C  CB  . ASN   E 2 807 ? -11.892 -10.605 -33.706 1.00 132.54 ? 1111 ASN   E CB  1 
ATOM   17234 C  CG  . ASN   E 2 807 ? -13.021 -10.862 -34.697 1.00 135.22 ? 1111 ASN   E CG  1 
ATOM   17235 O  OD1 . ASN   E 2 807 ? -12.802 -10.918 -35.907 1.00 134.45 ? 1111 ASN   E OD1 1 
ATOM   17236 N  ND2 . ASN   E 2 807 ? -14.240 -11.029 -34.179 1.00 132.03 ? 1111 ASN   E ND2 1 
ATOM   17237 N  N   . LEU   E 2 808 ? -9.545  -7.905  -32.745 1.00 135.85 ? 1112 LEU   E N   1 
ATOM   17238 C  CA  . LEU   E 2 808 ? -8.530  -7.649  -31.739 1.00 129.98 ? 1112 LEU   E CA  1 
ATOM   17239 C  C   . LEU   E 2 808 ? -8.852  -6.611  -30.680 1.00 130.16 ? 1112 LEU   E C   1 
ATOM   17240 O  O   . LEU   E 2 808 ? -9.043  -5.441  -30.998 1.00 137.31 ? 1112 LEU   E O   1 
ATOM   17241 C  CB  . LEU   E 2 808 ? -7.293  -7.230  -32.518 1.00 130.97 ? 1112 LEU   E CB  1 
ATOM   17242 C  CG  . LEU   E 2 808 ? -6.029  -7.294  -31.687 1.00 127.30 ? 1112 LEU   E CG  1 
ATOM   17243 C  CD1 . LEU   E 2 808 ? -6.075  -8.617  -30.995 1.00 126.16 ? 1112 LEU   E CD1 1 
ATOM   17244 C  CD2 . LEU   E 2 808 ? -4.830  -7.209  -32.590 1.00 121.14 ? 1112 LEU   E CD2 1 
ATOM   17245 N  N   . GLU   E 2 819 ? -11.717 -5.708  -32.743 1.00 155.24 ? 1123 GLU   E N   1 
ATOM   17246 C  CA  . GLU   E 2 819 ? -11.614 -5.390  -34.165 1.00 154.62 ? 1123 GLU   E CA  1 
ATOM   17247 C  C   . GLU   E 2 819 ? -10.801 -4.119  -34.366 1.00 158.48 ? 1123 GLU   E C   1 
ATOM   17248 O  O   . GLU   E 2 819 ? -11.334 -3.097  -34.805 1.00 160.23 ? 1123 GLU   E O   1 
ATOM   17249 C  CB  . GLU   E 2 819 ? -13.002 -5.232  -34.795 1.00 151.21 ? 1123 GLU   E CB  1 
ATOM   17250 N  N   . ALA   E 2 820 ? -9.512  -4.181  -34.030 1.00 152.03 ? 1124 ALA   E N   1 
ATOM   17251 C  CA  . ALA   E 2 820 ? -8.626  -3.050  -34.274 1.00 148.88 ? 1124 ALA   E CA  1 
ATOM   17252 C  C   . ALA   E 2 820 ? -8.358  -2.909  -35.772 1.00 153.94 ? 1124 ALA   E C   1 
ATOM   17253 O  O   . ALA   E 2 820 ? -8.196  -3.902  -36.484 1.00 157.03 ? 1124 ALA   E O   1 
ATOM   17254 C  CB  . ALA   E 2 820 ? -7.315  -3.224  -33.517 1.00 139.97 ? 1124 ALA   E CB  1 
ATOM   17255 N  N   . THR   E 2 821 ? -8.327  -1.667  -36.261 1.00 155.44 ? 1125 THR   E N   1 
ATOM   17256 C  CA  . THR   E 2 821 ? -8.192  -1.445  -37.700 1.00 156.25 ? 1125 THR   E CA  1 
ATOM   17257 C  C   . THR   E 2 821 ? -6.810  -1.877  -38.176 1.00 155.64 ? 1125 THR   E C   1 
ATOM   17258 O  O   . THR   E 2 821 ? -5.839  -1.825  -37.423 1.00 153.96 ? 1125 THR   E O   1 
ATOM   17259 C  CB  . THR   E 2 821 ? -8.419  0.034   -38.067 1.00 155.02 ? 1125 THR   E CB  1 
ATOM   17260 O  OG1 . THR   E 2 821 ? -7.463  0.842   -37.367 1.00 155.53 ? 1125 THR   E OG1 1 
ATOM   17261 C  CG2 . THR   E 2 821 ? -9.808  0.518   -37.698 1.00 151.56 ? 1125 THR   E CG2 1 
ATOM   17262 N  N   . ALA   E 2 822 ? -6.711  -2.303  -39.437 1.00 153.09 ? 1126 ALA   E N   1 
ATOM   17263 C  CA  . ALA   E 2 822 ? -5.379  -2.416  -40.013 1.00 147.99 ? 1126 ALA   E CA  1 
ATOM   17264 C  C   . ALA   E 2 822 ? -4.563  -1.156  -39.706 1.00 147.61 ? 1126 ALA   E C   1 
ATOM   17265 O  O   . ALA   E 2 822 ? -3.594  -1.199  -38.938 1.00 145.13 ? 1126 ALA   E O   1 
ATOM   17266 C  CB  . ALA   E 2 822 ? -5.491  -2.670  -41.509 1.00 141.68 ? 1126 ALA   E CB  1 
ATOM   17267 N  N   . ASP   E 2 823 ? -5.020  -0.006  -40.211 1.00 145.58 ? 1127 ASP   E N   1 
ATOM   17268 C  CA  . ASP   E 2 823 ? -4.239  1.222   -40.180 1.00 145.43 ? 1127 ASP   E CA  1 
ATOM   17269 C  C   . ASP   E 2 823 ? -3.771  1.643   -38.790 1.00 145.56 ? 1127 ASP   E C   1 
ATOM   17270 O  O   . ASP   E 2 823 ? -2.796  2.386   -38.702 1.00 141.77 ? 1127 ASP   E O   1 
ATOM   17271 C  CB  . ASP   E 2 823 ? -5.051  2.354   -40.798 1.00 148.91 ? 1127 ASP   E CB  1 
ATOM   17272 C  CG  . ASP   E 2 823 ? -4.477  2.831   -42.120 1.00 151.13 ? 1127 ASP   E CG  1 
ATOM   17273 O  OD1 . ASP   E 2 823 ? -3.769  2.006   -42.739 1.00 152.54 ? 1127 ASP   E OD1 1 
ATOM   17274 O  OD2 . ASP   E 2 823 ? -4.695  4.011   -42.518 1.00 154.52 ? 1127 ASP   E OD2 1 
ATOM   17275 N  N   . ASP   E 2 824 ? -4.449  1.256   -37.705 1.00 152.42 ? 1128 ASP   E N   1 
ATOM   17276 C  CA  . ASP   E 2 824 ? -3.842  1.563   -36.411 1.00 152.86 ? 1128 ASP   E CA  1 
ATOM   17277 C  C   . ASP   E 2 824 ? -2.750  0.568   -36.025 1.00 151.14 ? 1128 ASP   E C   1 
ATOM   17278 O  O   . ASP   E 2 824 ? -2.193  0.672   -34.928 1.00 148.93 ? 1128 ASP   E O   1 
ATOM   17279 C  CB  . ASP   E 2 824 ? -4.901  1.642   -35.297 1.00 156.15 ? 1128 ASP   E CB  1 
ATOM   17280 C  CG  . ASP   E 2 824 ? -5.531  0.294   -34.965 1.00 157.76 ? 1128 ASP   E CG  1 
ATOM   17281 O  OD1 . ASP   E 2 824 ? -4.803  -0.704  -34.850 1.00 161.06 ? 1128 ASP   E OD1 1 
ATOM   17282 O  OD2 . ASP   E 2 824 ? -6.771  0.242   -34.779 1.00 157.18 ? 1128 ASP   E OD2 1 
ATOM   17283 N  N   . LEU   E 2 825 ? -2.427  -0.389  -36.890 1.00 144.89 ? 1129 LEU   E N   1 
ATOM   17284 C  CA  . LEU   E 2 825 ? -1.369  -1.345  -36.611 1.00 137.59 ? 1129 LEU   E CA  1 
ATOM   17285 C  C   . LEU   E 2 825 ? -0.166  -1.199  -37.524 1.00 130.42 ? 1129 LEU   E C   1 
ATOM   17286 O  O   . LEU   E 2 825 ? 0.942   -1.536  -37.102 1.00 128.30 ? 1129 LEU   E O   1 
ATOM   17287 C  CB  . LEU   E 2 825 ? -1.920  -2.769  -36.695 1.00 136.19 ? 1129 LEU   E CB  1 
ATOM   17288 C  CG  . LEU   E 2 825 ? -2.413  -3.142  -35.296 1.00 134.86 ? 1129 LEU   E CG  1 
ATOM   17289 C  CD1 . LEU   E 2 825 ? -3.056  -4.586  -35.221 1.00 132.61 ? 1129 LEU   E CD1 1 
ATOM   17290 C  CD2 . LEU   E 2 825 ? -1.230  -2.995  -34.357 1.00 130.05 ? 1129 LEU   E CD2 1 
ATOM   17291 N  N   . ILE   E 2 826 ? -0.357  -0.724  -38.767 1.00 133.14 ? 1130 ILE   E N   1 
ATOM   17292 C  CA  . ILE   E 2 826 ? 0.793   -0.286  -39.558 1.00 129.59 ? 1130 ILE   E CA  1 
ATOM   17293 C  C   . ILE   E 2 826 ? 1.568   0.754   -38.778 1.00 128.38 ? 1130 ILE   E C   1 
ATOM   17294 O  O   . ILE   E 2 826 ? 2.799   0.704   -38.716 1.00 125.13 ? 1130 ILE   E O   1 
ATOM   17295 C  CB  . ILE   E 2 826 ? 0.384   0.276   -40.935 1.00 123.59 ? 1130 ILE   E CB  1 
ATOM   17296 C  CG1 . ILE   E 2 826 ? -0.390  -0.723  -41.755 1.00 124.84 ? 1130 ILE   E CG1 1 
ATOM   17297 C  CG2 . ILE   E 2 826 ? 1.580   0.471   -41.793 1.00 117.82 ? 1130 ILE   E CG2 1 
ATOM   17298 C  CD1 . ILE   E 2 826 ? -1.881  -0.308  -41.819 1.00 130.02 ? 1130 ILE   E CD1 1 
ATOM   17299 N  N   . LYS   E 2 827 ? 0.855   1.698   -38.151 1.00 126.13 ? 1131 LYS   E N   1 
ATOM   17300 C  CA  . LYS   E 2 827 ? 1.513   2.753   -37.387 1.00 127.11 ? 1131 LYS   E CA  1 
ATOM   17301 C  C   . LYS   E 2 827 ? 2.254   2.181   -36.185 1.00 127.32 ? 1131 LYS   E C   1 
ATOM   17302 O  O   . LYS   E 2 827 ? 3.409   2.546   -35.931 1.00 125.26 ? 1131 LYS   E O   1 
ATOM   17303 C  CB  . LYS   E 2 827 ? 0.495   3.807   -36.942 1.00 133.42 ? 1131 LYS   E CB  1 
ATOM   17304 C  CG  . LYS   E 2 827 ? -0.122  4.622   -38.073 1.00 141.22 ? 1131 LYS   E CG  1 
ATOM   17305 C  CD  . LYS   E 2 827 ? -1.145  5.639   -37.580 1.00 143.35 ? 1131 LYS   E CD  1 
ATOM   17306 C  CE  . LYS   E 2 827 ? -1.702  6.435   -38.767 1.00 145.78 ? 1131 LYS   E CE  1 
ATOM   17307 N  NZ  . LYS   E 2 827 ? -2.738  7.458   -38.431 1.00 143.86 ? 1131 LYS   E NZ  1 
ATOM   17308 N  N   . VAL   E 2 828 ? 1.608   1.280   -35.434 1.00 131.29 ? 1132 VAL   E N   1 
ATOM   17309 C  CA  . VAL   E 2 828 ? 2.268   0.661   -34.282 1.00 128.21 ? 1132 VAL   E CA  1 
ATOM   17310 C  C   . VAL   E 2 828 ? 3.604   0.068   -34.706 1.00 124.63 ? 1132 VAL   E C   1 
ATOM   17311 O  O   . VAL   E 2 828 ? 4.669   0.451   -34.206 1.00 121.22 ? 1132 VAL   E O   1 
ATOM   17312 C  CB  . VAL   E 2 828 ? 1.363   -0.409  -33.647 1.00 127.68 ? 1132 VAL   E CB  1 
ATOM   17313 C  CG1 . VAL   E 2 828 ? 2.196   -1.375  -32.824 1.00 121.37 ? 1132 VAL   E CG1 1 
ATOM   17314 C  CG2 . VAL   E 2 828 ? 0.318   0.246   -32.771 1.00 128.56 ? 1132 VAL   E CG2 1 
ATOM   17315 N  N   . VAL   E 2 829 ? 3.560   -0.850  -35.673 1.00 123.92 ? 1133 VAL   E N   1 
ATOM   17316 C  CA  . VAL   E 2 829 ? 4.766   -1.537  -36.118 1.00 119.81 ? 1133 VAL   E CA  1 
ATOM   17317 C  C   . VAL   E 2 829 ? 5.791   -0.551  -36.670 1.00 119.10 ? 1133 VAL   E C   1 
ATOM   17318 O  O   . VAL   E 2 829 ? 6.993   -0.669  -36.395 1.00 113.42 ? 1133 VAL   E O   1 
ATOM   17319 C  CB  . VAL   E 2 829 ? 4.380   -2.616  -37.136 1.00 116.11 ? 1133 VAL   E CB  1 
ATOM   17320 C  CG1 . VAL   E 2 829 ? 5.447   -2.763  -38.196 1.00 113.80 ? 1133 VAL   E CG1 1 
ATOM   17321 C  CG2 . VAL   E 2 829 ? 4.138   -3.909  -36.388 1.00 108.56 ? 1133 VAL   E CG2 1 
ATOM   17322 N  N   . GLU   E 2 830 ? 5.337   0.443   -37.447 1.00 123.42 ? 1134 GLU   E N   1 
ATOM   17323 C  CA  . GLU   E 2 830 ? 6.238   1.505   -37.909 1.00 118.77 ? 1134 GLU   E CA  1 
ATOM   17324 C  C   . GLU   E 2 830 ? 6.887   2.244   -36.746 1.00 117.44 ? 1134 GLU   E C   1 
ATOM   17325 O  O   . GLU   E 2 830 ? 8.022   2.713   -36.875 1.00 116.78 ? 1134 GLU   E O   1 
ATOM   17326 C  CB  . GLU   E 2 830 ? 5.487   2.498   -38.798 1.00 119.37 ? 1134 GLU   E CB  1 
ATOM   17327 C  CG  . GLU   E 2 830 ? 5.550   2.196   -40.288 1.00 122.00 ? 1134 GLU   E CG  1 
ATOM   17328 C  CD  . GLU   E 2 830 ? 4.282   2.617   -41.041 1.00 125.95 ? 1134 GLU   E CD  1 
ATOM   17329 O  OE1 . GLU   E 2 830 ? 3.177   2.549   -40.455 1.00 129.34 ? 1134 GLU   E OE1 1 
ATOM   17330 O  OE2 . GLU   E 2 830 ? 4.390   3.001   -42.226 1.00 124.41 ? 1134 GLU   E OE2 1 
ATOM   17331 N  N   . GLU   E 2 831 ? 6.179   2.381   -35.619 1.00 112.65 ? 1135 GLU   E N   1 
ATOM   17332 C  CA  . GLU   E 2 831 ? 6.797   2.925   -34.412 1.00 113.66 ? 1135 GLU   E CA  1 
ATOM   17333 C  C   . GLU   E 2 831 ? 7.916   2.022   -33.926 1.00 114.52 ? 1135 GLU   E C   1 
ATOM   17334 O  O   . GLU   E 2 831 ? 8.969   2.500   -33.478 1.00 111.81 ? 1135 GLU   E O   1 
ATOM   17335 C  CB  . GLU   E 2 831 ? 5.746   3.093   -33.314 1.00 116.42 ? 1135 GLU   E CB  1 
ATOM   17336 C  CG  . GLU   E 2 831 ? 6.293   3.457   -31.931 1.00 118.82 ? 1135 GLU   E CG  1 
ATOM   17337 C  CD  . GLU   E 2 831 ? 6.850   4.865   -31.884 1.00 125.00 ? 1135 GLU   E CD  1 
ATOM   17338 O  OE1 . GLU   E 2 831 ? 6.805   5.534   -32.946 1.00 126.50 ? 1135 GLU   E OE1 1 
ATOM   17339 O  OE2 . GLU   E 2 831 ? 7.332   5.295   -30.801 1.00 122.59 ? 1135 GLU   E OE2 1 
ATOM   17340 N  N   . LEU   E 2 832 ? 7.706   0.705   -34.008 1.00 114.87 ? 1136 LEU   E N   1 
ATOM   17341 C  CA  . LEU   E 2 832 ? 8.735   -0.220  -33.553 1.00 108.33 ? 1136 LEU   E CA  1 
ATOM   17342 C  C   . LEU   E 2 832 ? 9.931   -0.216  -34.501 1.00 105.94 ? 1136 LEU   E C   1 
ATOM   17343 O  O   . LEU   E 2 832 ? 11.078  -0.324  -34.050 1.00 108.39 ? 1136 LEU   E O   1 
ATOM   17344 C  CB  . LEU   E 2 832 ? 8.150   -1.624  -33.376 1.00 104.32 ? 1136 LEU   E CB  1 
ATOM   17345 C  CG  . LEU   E 2 832 ? 7.153   -1.853  -32.226 1.00 101.66 ? 1136 LEU   E CG  1 
ATOM   17346 C  CD1 . LEU   E 2 832 ? 5.730   -1.600  -32.670 1.00 111.73 ? 1136 LEU   E CD1 1 
ATOM   17347 C  CD2 . LEU   E 2 832 ? 7.235   -3.253  -31.693 1.00 98.03  ? 1136 LEU   E CD2 1 
ATOM   17348 N  N   . THR   E 2 833 ? 9.698   -0.039  -35.805 1.00 104.41 ? 1137 THR   E N   1 
ATOM   17349 C  CA  . THR   E 2 833 ? 10.823  0.031   -36.730 1.00 103.20 ? 1137 THR   E CA  1 
ATOM   17350 C  C   . THR   E 2 833 ? 11.761  1.211   -36.437 1.00 106.75 ? 1137 THR   E C   1 
ATOM   17351 O  O   . THR   E 2 833 ? 12.880  1.255   -36.971 1.00 106.07 ? 1137 THR   E O   1 
ATOM   17352 C  CB  . THR   E 2 833 ? 10.283  0.064   -38.166 1.00 108.15 ? 1137 THR   E CB  1 
ATOM   17353 O  OG1 . THR   E 2 833 ? 11.337  -0.251  -39.086 1.00 117.29 ? 1137 THR   E OG1 1 
ATOM   17354 C  CG2 . THR   E 2 833 ? 9.680   1.430   -38.524 1.00 110.18 ? 1137 THR   E CG2 1 
ATOM   17355 N  N   . ARG   E 2 834 ? 11.370  2.132   -35.550 1.00 105.52 ? 1138 ARG   E N   1 
ATOM   17356 C  CA  . ARG   E 2 834 ? 12.190  3.299   -35.250 1.00 102.19 ? 1138 ARG   E CA  1 
ATOM   17357 C  C   . ARG   E 2 834 ? 13.272  3.033   -34.212 1.00 100.63 ? 1138 ARG   E C   1 
ATOM   17358 O  O   . ARG   E 2 834 ? 14.139  3.899   -34.017 1.00 99.14  ? 1138 ARG   E O   1 
ATOM   17359 C  CB  . ARG   E 2 834 ? 11.322  4.466   -34.746 1.00 102.19 ? 1138 ARG   E CB  1 
ATOM   17360 C  CG  . ARG   E 2 834 ? 10.029  4.731   -35.509 1.00 108.55 ? 1138 ARG   E CG  1 
ATOM   17361 C  CD  . ARG   E 2 834 ? 10.237  5.394   -36.871 1.00 110.42 ? 1138 ARG   E CD  1 
ATOM   17362 N  NE  . ARG   E 2 834 ? 8.958   5.559   -37.556 1.00 109.05 ? 1138 ARG   E NE  1 
ATOM   17363 C  CZ  . ARG   E 2 834 ? 8.815   5.612   -38.873 1.00 112.49 ? 1138 ARG   E CZ  1 
ATOM   17364 N  NH1 . ARG   E 2 834 ? 9.863   5.564   -39.685 1.00 110.18 ? 1138 ARG   E NH1 1 
ATOM   17365 N  NH2 . ARG   E 2 834 ? 7.591   5.697   -39.390 1.00 114.92 ? 1138 ARG   E NH2 1 
ATOM   17366 N  N   . ILE   E 2 835 ? 13.248  1.882   -33.524 1.00 98.69  ? 1139 ILE   E N   1 
ATOM   17367 C  CA  . ILE   E 2 835 ? 14.267  1.635   -32.499 1.00 99.70  ? 1139 ILE   E CA  1 
ATOM   17368 C  C   . ILE   E 2 835 ? 15.569  1.085   -33.075 1.00 97.26  ? 1139 ILE   E C   1 
ATOM   17369 O  O   . ILE   E 2 835 ? 16.573  0.985   -32.349 1.00 91.72  ? 1139 ILE   E O   1 
ATOM   17370 C  CB  . ILE   E 2 835 ? 13.747  0.690   -31.402 1.00 95.17  ? 1139 ILE   E CB  1 
ATOM   17371 C  CG1 . ILE   E 2 835 ? 13.388  -0.670  -31.959 1.00 97.11  ? 1139 ILE   E CG1 1 
ATOM   17372 C  CG2 . ILE   E 2 835 ? 12.515  1.257   -30.746 1.00 98.51  ? 1139 ILE   E CG2 1 
ATOM   17373 C  CD1 . ILE   E 2 835 ? 12.668  -1.476  -30.923 1.00 96.11  ? 1139 ILE   E CD1 1 
ATOM   17374 N  N   . HIS   E 2 836 ? 15.586  0.732   -34.352 1.00 93.76  ? 1140 HIS   E N   1 
ATOM   17375 C  CA  . HIS   E 2 836 ? 16.828  0.466   -35.037 1.00 92.03  ? 1140 HIS   E CA  1 
ATOM   17376 C  C   . HIS   E 2 836 ? 16.690  1.050   -36.432 1.00 93.10  ? 1140 HIS   E C   1 
ATOM   17377 O  O   . HIS   E 2 836 ? 17.679  1.226   -37.136 1.00 99.10  ? 1140 HIS   E O   1 
ATOM   17378 C  CB  . HIS   E 2 836 ? 17.140  -1.038  -35.093 1.00 98.03  ? 1140 HIS   E CB  1 
ATOM   17379 C  CG  . HIS   E 2 836 ? 16.261  -1.806  -36.032 1.00 92.97  ? 1140 HIS   E CG  1 
ATOM   17380 N  ND1 . HIS   E 2 836 ? 16.692  -2.243  -37.269 1.00 91.16  ? 1140 HIS   E ND1 1 
ATOM   17381 C  CD2 . HIS   E 2 836 ? 14.968  -2.196  -35.923 1.00 91.70  ? 1140 HIS   E CD2 1 
ATOM   17382 C  CE1 . HIS   E 2 836 ? 15.702  -2.876  -37.877 1.00 97.06  ? 1140 HIS   E CE1 1 
ATOM   17383 N  NE2 . HIS   E 2 836 ? 14.645  -2.859  -37.083 1.00 93.83  ? 1140 HIS   E NE2 1 
ATOM   17384 N  N   . SER   F 3 3   ? 37.208  -57.572 29.282  1.00 106.86 ? 868  SER   F N   1 
ATOM   17385 C  CA  . SER   F 3 3   ? 35.844  -58.095 29.155  1.00 116.46 ? 868  SER   F CA  1 
ATOM   17386 C  C   . SER   F 3 3   ? 34.747  -56.997 29.134  1.00 118.46 ? 868  SER   F C   1 
ATOM   17387 O  O   . SER   F 3 3   ? 34.481  -56.393 28.091  1.00 110.86 ? 868  SER   F O   1 
ATOM   17388 C  CB  . SER   F 3 3   ? 35.563  -59.087 30.290  1.00 116.61 ? 868  SER   F CB  1 
ATOM   17389 O  OG  . SER   F 3 3   ? 36.053  -58.601 31.532  1.00 117.55 ? 868  SER   F OG  1 
ATOM   17390 N  N   . LEU   F 3 4   ? 34.106  -56.756 30.286  1.00 122.86 ? 869  LEU   F N   1 
ATOM   17391 C  CA  . LEU   F 3 4   ? 33.034  -55.764 30.413  1.00 120.98 ? 869  LEU   F CA  1 
ATOM   17392 C  C   . LEU   F 3 4   ? 33.547  -54.337 30.550  1.00 118.77 ? 869  LEU   F C   1 
ATOM   17393 O  O   . LEU   F 3 4   ? 32.779  -53.418 30.884  1.00 114.45 ? 869  LEU   F O   1 
ATOM   17394 C  CB  . LEU   F 3 4   ? 32.149  -56.084 31.617  1.00 121.99 ? 869  LEU   F CB  1 
ATOM   17395 C  CG  . LEU   F 3 4   ? 30.960  -56.974 31.276  1.00 127.16 ? 869  LEU   F CG  1 
ATOM   17396 C  CD1 . LEU   F 3 4   ? 29.829  -56.770 32.275  1.00 123.96 ? 869  LEU   F CD1 1 
ATOM   17397 C  CD2 . LEU   F 3 4   ? 30.517  -56.693 29.845  1.00 125.14 ? 869  LEU   F CD2 1 
ATOM   17398 N  N   . THR   F 3 5   ? 34.838  -54.150 30.318  1.00 116.75 ? 870  THR   F N   1 
ATOM   17399 C  CA  . THR   F 3 5   ? 35.479  -52.858 30.431  1.00 110.85 ? 870  THR   F CA  1 
ATOM   17400 C  C   . THR   F 3 5   ? 36.016  -52.372 29.091  1.00 107.27 ? 870  THR   F C   1 
ATOM   17401 O  O   . THR   F 3 5   ? 36.525  -51.252 29.023  1.00 105.53 ? 870  THR   F O   1 
ATOM   17402 C  CB  . THR   F 3 5   ? 36.596  -52.938 31.493  1.00 105.99 ? 870  THR   F CB  1 
ATOM   17403 O  OG1 . THR   F 3 5   ? 37.462  -51.805 31.398  1.00 111.12 ? 870  THR   F OG1 1 
ATOM   17404 C  CG2 . THR   F 3 5   ? 37.411  -54.182 31.299  1.00 110.10 ? 870  THR   F CG2 1 
ATOM   17405 N  N   . THR   F 3 6   ? 35.899  -53.168 28.026  1.00 105.18 ? 871  THR   F N   1 
ATOM   17406 C  CA  . THR   F 3 6   ? 36.389  -52.815 26.697  1.00 103.97 ? 871  THR   F CA  1 
ATOM   17407 C  C   . THR   F 3 6   ? 35.272  -52.246 25.826  1.00 104.67 ? 871  THR   F C   1 
ATOM   17408 O  O   . THR   F 3 6   ? 34.183  -52.819 25.748  1.00 105.31 ? 871  THR   F O   1 
ATOM   17409 C  CB  . THR   F 3 6   ? 36.985  -54.029 25.997  1.00 106.66 ? 871  THR   F CB  1 
ATOM   17410 O  OG1 . THR   F 3 6   ? 35.932  -54.955 25.735  1.00 116.95 ? 871  THR   F OG1 1 
ATOM   17411 C  CG2 . THR   F 3 6   ? 38.077  -54.663 26.870  1.00 101.07 ? 871  THR   F CG2 1 
ATOM   17412 N  N   . CYS   F 3 7   ? 35.573  -51.144 25.142  1.00 104.86 ? 872  CYS   F N   1 
ATOM   17413 C  CA  . CYS   F 3 7   ? 34.651  -50.481 24.234  1.00 100.02 ? 872  CYS   F CA  1 
ATOM   17414 C  C   . CYS   F 3 7   ? 34.540  -51.247 22.922  1.00 100.20 ? 872  CYS   F C   1 
ATOM   17415 O  O   . CYS   F 3 7   ? 35.545  -51.699 22.364  1.00 98.91  ? 872  CYS   F O   1 
ATOM   17416 C  CB  . CYS   F 3 7   ? 35.147  -49.056 23.985  1.00 95.42  ? 872  CYS   F CB  1 
ATOM   17417 S  SG  . CYS   F 3 7   ? 34.393  -48.195 22.582  1.00 90.16  ? 872  CYS   F SG  1 
ATOM   17418 N  N   . GLU   F 3 8   ? 33.311  -51.396 22.427  1.00 98.57  ? 873  GLU   F N   1 
ATOM   17419 C  CA  . GLU   F 3 8   ? 33.107  -52.175 21.212  1.00 98.57  ? 873  GLU   F CA  1 
ATOM   17420 C  C   . GLU   F 3 8   ? 33.337  -51.381 19.931  1.00 97.12  ? 873  GLU   F C   1 
ATOM   17421 O  O   . GLU   F 3 8   ? 33.432  -51.984 18.857  1.00 98.81  ? 873  GLU   F O   1 
ATOM   17422 C  CB  . GLU   F 3 8   ? 31.698  -52.774 21.192  1.00 100.83 ? 873  GLU   F CB  1 
ATOM   17423 C  CG  . GLU   F 3 8   ? 31.191  -53.139 22.569  1.00 112.13 ? 873  GLU   F CG  1 
ATOM   17424 C  CD  . GLU   F 3 8   ? 30.380  -54.419 22.583  1.00 114.49 ? 873  GLU   F CD  1 
ATOM   17425 O  OE1 . GLU   F 3 8   ? 30.821  -55.396 23.238  1.00 117.14 ? 873  GLU   F OE1 1 
ATOM   17426 O  OE2 . GLU   F 3 8   ? 29.311  -54.440 21.929  1.00 117.41 ? 873  GLU   F OE2 1 
ATOM   17427 N  N   . VAL   F 3 9   ? 33.432  -50.060 19.996  1.00 90.38  ? 874  VAL   F N   1 
ATOM   17428 C  CA  . VAL   F 3 9   ? 33.628  -49.294 18.776  1.00 91.11  ? 874  VAL   F CA  1 
ATOM   17429 C  C   . VAL   F 3 9   ? 35.106  -49.209 18.387  1.00 94.84  ? 874  VAL   F C   1 
ATOM   17430 O  O   . VAL   F 3 9   ? 35.475  -49.473 17.240  1.00 94.23  ? 874  VAL   F O   1 
ATOM   17431 C  CB  . VAL   F 3 9   ? 33.001  -47.896 18.925  1.00 84.91  ? 874  VAL   F CB  1 
ATOM   17432 C  CG1 . VAL   F 3 9   ? 33.673  -46.956 17.958  1.00 81.52  ? 874  VAL   F CG1 1 
ATOM   17433 C  CG2 . VAL   F 3 9   ? 31.512  -47.961 18.667  1.00 84.08  ? 874  VAL   F CG2 1 
ATOM   17434 N  N   . CYS   F 3 10  ? 35.983  -48.844 19.319  1.00 93.27  ? 875  CYS   F N   1 
ATOM   17435 C  CA  . CYS   F 3 10  ? 37.366  -48.521 18.995  1.00 88.05  ? 875  CYS   F CA  1 
ATOM   17436 C  C   . CYS   F 3 10  ? 38.392  -49.436 19.649  1.00 97.06  ? 875  CYS   F C   1 
ATOM   17437 O  O   . CYS   F 3 10  ? 39.591  -49.194 19.458  1.00 96.64  ? 875  CYS   F O   1 
ATOM   17438 C  CB  . CYS   F 3 10  ? 37.683  -47.077 19.415  1.00 89.55  ? 875  CYS   F CB  1 
ATOM   17439 S  SG  . CYS   F 3 10  ? 37.756  -46.843 21.222  1.00 83.36  ? 875  CYS   F SG  1 
ATOM   17440 N  N   . GLY   F 3 11  ? 37.967  -50.430 20.454  1.00 98.85  ? 876  GLY   F N   1 
ATOM   17441 C  CA  . GLY   F 3 11  ? 38.862  -51.343 21.157  1.00 97.02  ? 876  GLY   F CA  1 
ATOM   17442 C  C   . GLY   F 3 11  ? 39.451  -50.855 22.474  1.00 97.43  ? 876  GLY   F C   1 
ATOM   17443 O  O   . GLY   F 3 11  ? 40.336  -51.522 23.027  1.00 98.22  ? 876  GLY   F O   1 
ATOM   17444 N  N   . ALA   F 3 12  ? 38.994  -49.722 23.002  1.00 97.71  ? 877  ALA   F N   1 
ATOM   17445 C  CA  . ALA   F 3 12  ? 39.500  -49.227 24.276  1.00 97.28  ? 877  ALA   F CA  1 
ATOM   17446 C  C   . ALA   F 3 12  ? 39.335  -50.263 25.390  1.00 96.88  ? 877  ALA   F C   1 
ATOM   17447 O  O   . ALA   F 3 12  ? 38.308  -50.932 25.467  1.00 102.58 ? 877  ALA   F O   1 
ATOM   17448 C  CB  . ALA   F 3 12  ? 38.755  -47.941 24.641  1.00 94.55  ? 877  ALA   F CB  1 
ATOM   17449 N  N   . CYS   F 3 13  ? 40.343  -50.403 26.266  1.00 92.56  ? 878  CYS   F N   1 
ATOM   17450 C  CA  . CYS   F 3 13  ? 40.183  -51.176 27.503  1.00 102.28 ? 878  CYS   F CA  1 
ATOM   17451 C  C   . CYS   F 3 13  ? 40.474  -50.331 28.750  1.00 103.48 ? 878  CYS   F C   1 
ATOM   17452 O  O   . CYS   F 3 13  ? 41.634  -49.995 29.029  1.00 102.09 ? 878  CYS   F O   1 
ATOM   17453 C  CB  . CYS   F 3 13  ? 41.056  -52.429 27.531  1.00 100.27 ? 878  CYS   F CB  1 
ATOM   17454 S  SG  . CYS   F 3 13  ? 40.556  -53.451 28.972  1.00 113.68 ? 878  CYS   F SG  1 
ATOM   17455 N  N   . PHE   F 3 14  ? 39.434  -50.067 29.550  1.00 100.32 ? 879  PHE   F N   1 
ATOM   17456 C  CA  . PHE   F 3 14  ? 39.593  -49.346 30.806  1.00 106.70 ? 879  PHE   F CA  1 
ATOM   17457 C  C   . PHE   F 3 14  ? 39.843  -50.293 31.972  1.00 111.18 ? 879  PHE   F C   1 
ATOM   17458 O  O   . PHE   F 3 14  ? 40.078  -51.488 31.804  1.00 109.04 ? 879  PHE   F O   1 
ATOM   17459 C  CB  . PHE   F 3 14  ? 38.371  -48.483 31.085  1.00 103.54 ? 879  PHE   F CB  1 
ATOM   17460 C  CG  . PHE   F 3 14  ? 38.108  -47.529 30.015  1.00 101.82 ? 879  PHE   F CG  1 
ATOM   17461 C  CD1 . PHE   F 3 14  ? 38.879  -46.381 29.897  1.00 95.09  ? 879  PHE   F CD1 1 
ATOM   17462 C  CD2 . PHE   F 3 14  ? 37.149  -47.814 29.060  1.00 102.60 ? 879  PHE   F CD2 1 
ATOM   17463 C  CE1 . PHE   F 3 14  ? 38.658  -45.503 28.876  1.00 94.87  ? 879  PHE   F CE1 1 
ATOM   17464 C  CE2 . PHE   F 3 14  ? 36.926  -46.940 28.015  1.00 101.06 ? 879  PHE   F CE2 1 
ATOM   17465 C  CZ  . PHE   F 3 14  ? 37.678  -45.780 27.921  1.00 99.02  ? 879  PHE   F CZ  1 
ATOM   17466 N  N   . GLU   F 3 15  ? 39.760  -49.758 33.178  1.00 113.60 ? 880  GLU   F N   1 
ATOM   17467 C  CA  . GLU   F 3 15  ? 39.889  -50.567 34.368  1.00 110.67 ? 880  GLU   F CA  1 
ATOM   17468 C  C   . GLU   F 3 15  ? 38.588  -50.636 35.135  1.00 114.42 ? 880  GLU   F C   1 
ATOM   17469 O  O   . GLU   F 3 15  ? 38.371  -51.590 35.889  1.00 123.22 ? 880  GLU   F O   1 
ATOM   17470 C  CB  . GLU   F 3 15  ? 40.992  -49.997 35.268  1.00 120.53 ? 880  GLU   F CB  1 
ATOM   17471 C  CG  . GLU   F 3 15  ? 42.411  -50.127 34.695  1.00 128.77 ? 880  GLU   F CG  1 
ATOM   17472 C  CD  . GLU   F 3 15  ? 43.506  -49.803 35.716  1.00 138.85 ? 880  GLU   F CD  1 
ATOM   17473 O  OE1 . GLU   F 3 15  ? 44.706  -50.043 35.435  1.00 144.81 ? 880  GLU   F OE1 1 
ATOM   17474 O  OE2 . GLU   F 3 15  ? 43.160  -49.304 36.807  1.00 145.06 ? 880  GLU   F OE2 1 
ATOM   17475 N  N   . THR   F 3 16  ? 37.708  -49.669 34.956  1.00 122.57 ? 881  THR   F N   1 
ATOM   17476 C  CA  . THR   F 3 16  ? 36.423  -49.722 35.620  1.00 120.16 ? 881  THR   F CA  1 
ATOM   17477 C  C   . THR   F 3 16  ? 35.312  -49.595 34.596  1.00 116.62 ? 881  THR   F C   1 
ATOM   17478 O  O   . THR   F 3 16  ? 35.481  -48.953 33.555  1.00 115.65 ? 881  THR   F O   1 
ATOM   17479 C  CB  . THR   F 3 16  ? 36.242  -48.627 36.584  1.00 118.42 ? 881  THR   F CB  1 
ATOM   17480 O  OG1 . THR   F 3 16  ? 34.854  -48.627 36.992  1.00 117.85 ? 881  THR   F OG1 1 
ATOM   17481 C  CG2 . THR   F 3 16  ? 36.600  -47.362 35.838  1.00 113.58 ? 881  THR   F CG2 1 
ATOM   17482 N  N   . ARG   F 3 17  ? 34.169  -50.208 34.919  1.00 108.46 ? 882  ARG   F N   1 
ATOM   17483 C  CA  . ARG   F 3 17  ? 32.989  -50.066 34.078  1.00 104.23 ? 882  ARG   F CA  1 
ATOM   17484 C  C   . ARG   F 3 17  ? 32.667  -48.595 33.839  1.00 100.71 ? 882  ARG   F C   1 
ATOM   17485 O  O   . ARG   F 3 17  ? 32.202  -48.227 32.754  1.00 99.70  ? 882  ARG   F O   1 
ATOM   17486 C  CB  . ARG   F 3 17  ? 31.785  -50.777 34.708  1.00 102.48 ? 882  ARG   F CB  1 
ATOM   17487 C  CG  . ARG   F 3 17  ? 31.874  -52.293 34.785  1.00 105.62 ? 882  ARG   F CG  1 
ATOM   17488 C  CD  . ARG   F 3 17  ? 30.579  -52.925 35.396  1.00 123.88 ? 882  ARG   F CD  1 
ATOM   17489 N  NE  . ARG   F 3 17  ? 30.644  -54.381 35.556  1.00 121.55 ? 882  ARG   F NE  1 
ATOM   17490 C  CZ  . ARG   F 3 17  ? 29.719  -55.125 36.153  1.00 116.49 ? 882  ARG   F CZ  1 
ATOM   17491 N  NH1 . ARG   F 3 17  ? 28.650  -54.584 36.714  1.00 120.79 ? 882  ARG   F NH1 1 
ATOM   17492 N  NH2 . ARG   F 3 17  ? 29.866  -56.444 36.176  1.00 110.62 ? 882  ARG   F NH2 1 
ATOM   17493 N  N   . LYS   F 3 18  ? 32.884  -47.743 34.853  1.00 97.97  ? 883  LYS   F N   1 
ATOM   17494 C  CA  . LYS   F 3 18  ? 32.688  -46.306 34.664  1.00 100.06 ? 883  LYS   F CA  1 
ATOM   17495 C  C   . LYS   F 3 18  ? 33.701  -45.738 33.682  1.00 102.17 ? 883  LYS   F C   1 
ATOM   17496 O  O   . LYS   F 3 18  ? 33.409  -44.769 32.961  1.00 98.90  ? 883  LYS   F O   1 
ATOM   17497 C  CB  . LYS   F 3 18  ? 32.781  -45.567 35.997  1.00 98.91  ? 883  LYS   F CB  1 
ATOM   17498 C  CG  . LYS   F 3 18  ? 32.652  -44.061 35.907  1.00 92.07  ? 883  LYS   F CG  1 
ATOM   17499 C  CD  . LYS   F 3 18  ? 31.325  -43.584 36.442  1.00 94.69  ? 883  LYS   F CD  1 
ATOM   17500 C  CE  . LYS   F 3 18  ? 30.953  -42.220 35.888  1.00 93.32  ? 883  LYS   F CE  1 
ATOM   17501 N  NZ  . LYS   F 3 18  ? 29.909  -41.532 36.686  1.00 92.06  ? 883  LYS   F NZ  1 
ATOM   17502 N  N   . GLY   F 3 19  ? 34.894  -46.320 33.641  1.00 100.77 ? 884  GLY   F N   1 
ATOM   17503 C  CA  . GLY   F 3 19  ? 35.817  -45.961 32.588  1.00 103.20 ? 884  GLY   F CA  1 
ATOM   17504 C  C   . GLY   F 3 19  ? 35.134  -46.033 31.240  1.00 99.23  ? 884  GLY   F C   1 
ATOM   17505 O  O   . GLY   F 3 19  ? 35.113  -45.055 30.487  1.00 99.43  ? 884  GLY   F O   1 
ATOM   17506 N  N   . LEU   F 3 20  ? 34.553  -47.199 30.934  1.00 98.08  ? 885  LEU   F N   1 
ATOM   17507 C  CA  . LEU   F 3 20  ? 33.805  -47.362 29.700  1.00 93.28  ? 885  LEU   F CA  1 
ATOM   17508 C  C   . LEU   F 3 20  ? 32.638  -46.391 29.637  1.00 94.03  ? 885  LEU   F C   1 
ATOM   17509 O  O   . LEU   F 3 20  ? 32.430  -45.716 28.624  1.00 94.83  ? 885  LEU   F O   1 
ATOM   17510 C  CB  . LEU   F 3 20  ? 33.290  -48.788 29.584  1.00 91.17  ? 885  LEU   F CB  1 
ATOM   17511 C  CG  . LEU   F 3 20  ? 33.786  -49.582 28.391  1.00 98.50  ? 885  LEU   F CG  1 
ATOM   17512 C  CD1 . LEU   F 3 20  ? 32.973  -50.853 28.293  1.00 110.83 ? 885  LEU   F CD1 1 
ATOM   17513 C  CD2 . LEU   F 3 20  ? 33.710  -48.810 27.099  1.00 92.64  ? 885  LEU   F CD2 1 
ATOM   17514 N  N   . SER   F 3 21  ? 31.856  -46.319 30.713  1.00 93.36  ? 886  SER   F N   1 
ATOM   17515 C  CA  . SER   F 3 21  ? 30.639  -45.520 30.703  1.00 94.69  ? 886  SER   F CA  1 
ATOM   17516 C  C   . SER   F 3 21  ? 30.884  -44.114 30.172  1.00 97.32  ? 886  SER   F C   1 
ATOM   17517 O  O   . SER   F 3 21  ? 30.106  -43.610 29.354  1.00 92.89  ? 886  SER   F O   1 
ATOM   17518 C  CB  . SER   F 3 21  ? 30.048  -45.467 32.109  1.00 97.32  ? 886  SER   F CB  1 
ATOM   17519 O  OG  . SER   F 3 21  ? 28.639  -45.360 32.047  1.00 108.37 ? 886  SER   F OG  1 
ATOM   17520 N  N   . SER   F 3 22  ? 31.955  -43.459 30.629  1.00 95.51  ? 887  SER   F N   1 
ATOM   17521 C  CA  . SER   F 3 22  ? 32.262  -42.125 30.120  1.00 94.11  ? 887  SER   F CA  1 
ATOM   17522 C  C   . SER   F 3 22  ? 32.713  -42.182 28.666  1.00 94.37  ? 887  SER   F C   1 
ATOM   17523 O  O   . SER   F 3 22  ? 32.201  -41.445 27.819  1.00 100.63 ? 887  SER   F O   1 
ATOM   17524 C  CB  . SER   F 3 22  ? 33.330  -41.455 30.982  1.00 98.08  ? 887  SER   F CB  1 
ATOM   17525 O  OG  . SER   F 3 22  ? 34.604  -41.634 30.397  1.00 104.33 ? 887  SER   F OG  1 
ATOM   17526 N  N   . HIS   F 3 23  ? 33.679  -43.050 28.361  1.00 96.87  ? 888  HIS   F N   1 
ATOM   17527 C  CA  . HIS   F 3 23  ? 34.197  -43.176 26.999  1.00 97.51  ? 888  HIS   F CA  1 
ATOM   17528 C  C   . HIS   F 3 23  ? 33.079  -43.316 25.979  1.00 98.48  ? 888  HIS   F C   1 
ATOM   17529 O  O   . HIS   F 3 23  ? 33.189  -42.831 24.845  1.00 100.01 ? 888  HIS   F O   1 
ATOM   17530 C  CB  . HIS   F 3 23  ? 35.114  -44.388 26.895  1.00 92.41  ? 888  HIS   F CB  1 
ATOM   17531 C  CG  . HIS   F 3 23  ? 35.631  -44.616 25.517  1.00 88.12  ? 888  HIS   F CG  1 
ATOM   17532 N  ND1 . HIS   F 3 23  ? 36.679  -43.897 24.999  1.00 93.98  ? 888  HIS   F ND1 1 
ATOM   17533 C  CD2 . HIS   F 3 23  ? 35.238  -45.465 24.542  1.00 87.18  ? 888  HIS   F CD2 1 
ATOM   17534 C  CE1 . HIS   F 3 23  ? 36.925  -44.304 23.769  1.00 93.59  ? 888  HIS   F CE1 1 
ATOM   17535 N  NE2 . HIS   F 3 23  ? 36.068  -45.259 23.470  1.00 91.18  ? 888  HIS   F NE2 1 
ATOM   17536 N  N   . ALA   F 3 24  ? 32.028  -44.050 26.350  1.00 95.25  ? 889  ALA   F N   1 
ATOM   17537 C  CA  . ALA   F 3 24  ? 30.824  -44.154 25.546  1.00 93.43  ? 889  ALA   F CA  1 
ATOM   17538 C  C   . ALA   F 3 24  ? 30.441  -42.810 24.937  1.00 103.26 ? 889  ALA   F C   1 
ATOM   17539 O  O   . ALA   F 3 24  ? 30.311  -42.691 23.715  1.00 110.97 ? 889  ALA   F O   1 
ATOM   17540 C  CB  . ALA   F 3 24  ? 29.699  -44.716 26.411  1.00 97.09  ? 889  ALA   F CB  1 
ATOM   17541 N  N   . ARG   F 3 25  ? 30.286  -41.777 25.772  1.00 103.72 ? 890  ARG   F N   1 
ATOM   17542 C  CA  . ARG   F 3 25  ? 29.844  -40.473 25.282  1.00 101.28 ? 890  ARG   F CA  1 
ATOM   17543 C  C   . ARG   F 3 25  ? 30.795  -39.916 24.231  1.00 104.73 ? 890  ARG   F C   1 
ATOM   17544 O  O   . ARG   F 3 25  ? 30.359  -39.328 23.235  1.00 113.77 ? 890  ARG   F O   1 
ATOM   17545 C  CB  . ARG   F 3 25  ? 29.721  -39.497 26.449  1.00 114.71 ? 890  ARG   F CB  1 
ATOM   17546 N  N   . SER   F 3 26  ? 32.098  -40.076 24.444  1.00 106.35 ? 891  SER   F N   1 
ATOM   17547 C  CA  . SER   F 3 26  ? 33.088  -39.697 23.437  1.00 109.60 ? 891  SER   F CA  1 
ATOM   17548 C  C   . SER   F 3 26  ? 32.703  -40.154 22.015  1.00 110.61 ? 891  SER   F C   1 
ATOM   17549 O  O   . SER   F 3 26  ? 32.998  -39.462 21.031  1.00 110.79 ? 891  SER   F O   1 
ATOM   17550 C  CB  . SER   F 3 26  ? 34.458  -40.265 23.848  1.00 107.99 ? 891  SER   F CB  1 
ATOM   17551 O  OG  . SER   F 3 26  ? 35.257  -40.628 22.715  1.00 108.01 ? 891  SER   F OG  1 
ATOM   17552 N  N   . HIS   F 3 27  ? 32.073  -41.328 21.882  1.00 104.69 ? 892  HIS   F N   1 
ATOM   17553 C  CA  . HIS   F 3 27  ? 31.702  -41.865 20.572  1.00 105.72 ? 892  HIS   F CA  1 
ATOM   17554 C  C   . HIS   F 3 27  ? 30.362  -41.344 20.081  1.00 116.56 ? 892  HIS   F C   1 
ATOM   17555 O  O   . HIS   F 3 27  ? 30.203  -41.087 18.883  1.00 126.86 ? 892  HIS   F O   1 
ATOM   17556 C  CB  . HIS   F 3 27  ? 31.640  -43.393 20.600  1.00 100.70 ? 892  HIS   F CB  1 
ATOM   17557 C  CG  . HIS   F 3 27  ? 32.973  -44.056 20.493  1.00 93.28  ? 892  HIS   F CG  1 
ATOM   17558 N  ND1 . HIS   F 3 27  ? 33.867  -43.762 19.488  1.00 94.50  ? 892  HIS   F ND1 1 
ATOM   17559 C  CD2 . HIS   F 3 27  ? 33.562  -45.004 21.256  1.00 85.45  ? 892  HIS   F CD2 1 
ATOM   17560 C  CE1 . HIS   F 3 27  ? 34.957  -44.492 19.643  1.00 87.15  ? 892  HIS   F CE1 1 
ATOM   17561 N  NE2 . HIS   F 3 27  ? 34.795  -45.256 20.706  1.00 82.23  ? 892  HIS   F NE2 1 
ATOM   17562 N  N   . LEU   F 3 28  ? 29.390  -41.203 20.978  1.00 114.82 ? 893  LEU   F N   1 
ATOM   17563 C  CA  . LEU   F 3 28  ? 28.057  -40.778 20.582  1.00 120.24 ? 893  LEU   F CA  1 
ATOM   17564 C  C   . LEU   F 3 28  ? 27.847  -39.317 20.189  1.00 132.20 ? 893  LEU   F C   1 
ATOM   17565 O  O   . LEU   F 3 28  ? 27.430  -39.026 19.059  1.00 139.63 ? 893  LEU   F O   1 
ATOM   17566 C  CB  . LEU   F 3 28  ? 27.053  -41.019 21.716  1.00 120.58 ? 893  LEU   F CB  1 
ATOM   17567 C  CG  . LEU   F 3 28  ? 26.977  -42.407 22.382  1.00 122.89 ? 893  LEU   F CG  1 
ATOM   17568 C  CD1 . LEU   F 3 28  ? 25.973  -42.394 23.536  1.00 117.43 ? 893  LEU   F CD1 1 
ATOM   17569 C  CD2 . LEU   F 3 28  ? 26.652  -43.539 21.392  1.00 121.80 ? 893  LEU   F CD2 1 
ATOM   17570 N  N   . ARG   F 3 29  ? 28.144  -38.396 21.107  1.00 132.85 ? 894  ARG   F N   1 
ATOM   17571 C  CA  . ARG   F 3 29  ? 27.878  -36.970 20.909  1.00 134.19 ? 894  ARG   F CA  1 
ATOM   17572 C  C   . ARG   F 3 29  ? 28.853  -36.486 19.832  1.00 133.12 ? 894  ARG   F C   1 
ATOM   17573 O  O   . ARG   F 3 29  ? 30.038  -36.838 19.846  1.00 132.39 ? 894  ARG   F O   1 
ATOM   17574 C  CB  . ARG   F 3 29  ? 28.094  -36.185 22.211  1.00 135.06 ? 894  ARG   F CB  1 
HETATM 17575 ZN ZN  . ZN    G 4 .   ? 16.368  38.719  -61.971 1.00 92.50  2 501  ZN    A ZN  1 
HETATM 17576 S  S   . SO4   H 5 .   ? 9.915   42.215  -32.162 1.00 112.91 ? 502  SO4   A S   1 
HETATM 17577 O  O1  . SO4   H 5 .   ? 11.423  42.107  -32.023 1.00 99.24  ? 502  SO4   A O1  1 
HETATM 17578 O  O2  . SO4   H 5 .   ? 9.310   40.833  -32.311 1.00 104.99 ? 502  SO4   A O2  1 
HETATM 17579 O  O3  . SO4   H 5 .   ? 9.326   42.953  -30.963 1.00 105.43 ? 502  SO4   A O3  1 
HETATM 17580 O  O4  . SO4   H 5 .   ? 9.620   42.971  -33.438 1.00 109.55 ? 502  SO4   A O4  1 
HETATM 17581 C  C1  . A1A5H I 6 .   ? 19.438  17.016  -62.077 1.00 100.45 ? 503  A1A5H A C1  1 
HETATM 17582 C  C2  . A1A5H I 6 .   ? 18.412  16.135  -62.389 1.00 102.56 ? 503  A1A5H A C2  1 
HETATM 17583 C  C3  . A1A5H I 6 .   ? 17.255  16.109  -61.629 1.00 99.49  ? 503  A1A5H A C3  1 
HETATM 17584 C  C11 . A1A5H I 6 .   ? 19.421  14.223  -63.202 1.00 106.57 ? 503  A1A5H A C11 1 
HETATM 17585 C  C13 . A1A5H I 6 .   ? 19.813  13.567  -64.534 1.00 114.94 ? 503  A1A5H A C13 1 
HETATM 17586 C  C14 . A1A5H I 6 .   ? 18.573  13.073  -65.277 1.00 105.76 ? 503  A1A5H A C14 1 
HETATM 17587 C  C15 . A1A5H I 6 .   ? 17.731  12.193  -64.375 1.00 110.34 ? 503  A1A5H A C15 1 
HETATM 17588 C  C17 . A1A5H I 6 .   ? 18.699  13.168  -62.422 1.00 106.88 ? 503  A1A5H A C17 1 
HETATM 17589 C  C18 . A1A5H I 6 .   ? 21.011  13.978  -65.314 1.00 113.86 ? 503  A1A5H A C18 1 
HETATM 17590 C  C19 . A1A5H I 6 .   ? 21.018  12.695  -64.533 1.00 119.90 ? 503  A1A5H A C19 1 
HETATM 17591 C  C20 . A1A5H I 6 .   ? 16.522  12.056  -62.295 1.00 116.38 ? 503  A1A5H A C20 1 
HETATM 17592 C  C21 . A1A5H I 6 .   ? 17.101  11.264  -61.156 1.00 117.39 ? 503  A1A5H A C21 1 
HETATM 17593 C  C22 . A1A5H I 6 .   ? 15.694  18.842  -57.679 1.00 94.15  ? 503  A1A5H A C22 1 
HETATM 17594 C  C23 . A1A5H I 6 .   ? 14.366  19.401  -58.120 1.00 90.66  ? 503  A1A5H A C23 1 
HETATM 17595 C  C24 . A1A5H I 6 .   ? 13.633  19.949  -56.911 1.00 92.62  ? 503  A1A5H A C24 1 
HETATM 17596 C  C25 . A1A5H I 6 .   ? 13.445  18.891  -55.873 1.00 97.07  ? 503  A1A5H A C25 1 
HETATM 17597 C  C27 . A1A5H I 6 .   ? 15.525  17.824  -56.574 1.00 100.15 ? 503  A1A5H A C27 1 
HETATM 17598 C  C4  . A1A5H I 6 .   ? 17.127  16.979  -60.558 1.00 93.58  ? 503  A1A5H A C4  1 
HETATM 17599 C  C5  . A1A5H I 6 .   ? 18.140  17.863  -60.248 1.00 91.22  ? 503  A1A5H A C5  1 
HETATM 17600 C  C6  . A1A5H I 6 .   ? 19.301  17.884  -61.008 1.00 90.33  ? 503  A1A5H A C6  1 
HETATM 17601 C  C7  . A1A5H I 6 .   ? 15.989  17.164  -59.602 1.00 94.23  ? 503  A1A5H A C7  1 
HETATM 17602 C  C9  . A1A5H I 6 .   ? 17.717  18.688  -59.096 1.00 96.98  ? 503  A1A5H A C9  1 
HETATM 17603 N  N16 . A1A5H I 6 .   ? 17.448  12.859  -63.106 1.00 113.01 ? 503  A1A5H A N16 1 
HETATM 17604 N  N26 . A1A5H I 6 .   ? 14.408  17.930  -55.795 1.00 100.52 ? 503  A1A5H A N26 1 
HETATM 17605 N  N8  . A1A5H I 6 .   ? 16.472  18.259  -58.758 1.00 96.45  ? 503  A1A5H A N8  1 
HETATM 17606 O  O10 . A1A5H I 6 .   ? 18.325  19.579  -58.540 1.00 96.16  ? 503  A1A5H A O10 1 
HETATM 17607 O  O12 . A1A5H I 6 .   ? 18.543  15.282  -63.459 1.00 100.94 ? 503  A1A5H A O12 1 
HETATM 17608 O  O28 . A1A5H I 6 .   ? 16.365  16.955  -56.378 1.00 96.95  ? 503  A1A5H A O28 1 
HETATM 17609 O  O29 . A1A5H I 6 .   ? 12.477  18.862  -55.124 1.00 95.65  ? 503  A1A5H A O29 1 
HETATM 17610 H  H30 . A1A5H I 6 .   ? 20.358  17.024  -62.658 0.00 120.63 ? 503  A1A5H A H30 1 
HETATM 17611 H  H31 . A1A5H I 6 .   ? 16.459  15.405  -61.867 0.00 119.49 ? 503  A1A5H A H31 1 
HETATM 17612 H  H35 . A1A5H I 6 .   ? 20.328  14.561  -62.718 0.00 127.98 ? 503  A1A5H A H35 1 
HETATM 17613 H  H36 . A1A5H I 6 .   ? 18.899  12.535  -66.165 0.00 127.01 ? 503  A1A5H A H36 1 
HETATM 17614 H  H37 . A1A5H I 6 .   ? 17.991  13.908  -65.661 0.00 127.01 ? 503  A1A5H A H37 1 
HETATM 17615 H  H39 . A1A5H I 6 .   ? 18.227  11.244  -64.184 0.00 132.51 ? 503  A1A5H A H39 1 
HETATM 17616 H  H38 . A1A5H I 6 .   ? 16.794  11.929  -64.860 0.00 132.51 ? 503  A1A5H A H38 1 
HETATM 17617 H  H40 . A1A5H I 6 .   ? 18.519  13.502  -61.403 0.00 128.35 ? 503  A1A5H A H40 1 
HETATM 17618 H  H41 . A1A5H I 6 .   ? 19.317  12.279  -62.325 0.00 128.35 ? 503  A1A5H A H41 1 
HETATM 17619 H  H43 . A1A5H I 6 .   ? 21.617  14.824  -64.993 0.00 136.73 ? 503  A1A5H A H43 1 
HETATM 17620 H  H42 . A1A5H I 6 .   ? 20.996  13.958  -66.402 0.00 136.73 ? 503  A1A5H A H42 1 
HETATM 17621 H  H45 . A1A5H I 6 .   ? 20.986  11.736  -65.045 0.00 143.97 ? 503  A1A5H A H45 1 
HETATM 17622 H  H44 . A1A5H I 6 .   ? 21.609  12.595  -63.627 0.00 143.97 ? 503  A1A5H A H44 1 
HETATM 17623 H  H47 . A1A5H I 6 .   ? 16.082  11.315  -62.950 0.00 139.75 ? 503  A1A5H A H47 1 
HETATM 17624 H  H46 . A1A5H I 6 .   ? 15.690  12.623  -61.890 0.00 139.75 ? 503  A1A5H A H46 1 
HETATM 17625 H  H50 . A1A5H I 6 .   ? 17.956  10.660  -61.454 0.00 140.96 ? 503  A1A5H A H50 1 
HETATM 17626 H  H48 . A1A5H I 6 .   ? 16.354  10.581  -60.757 0.00 140.96 ? 503  A1A5H A H48 1 
HETATM 17627 H  H49 . A1A5H I 6 .   ? 17.422  11.878  -60.315 0.00 140.96 ? 503  A1A5H A H49 1 
HETATM 17628 H  H51 . A1A5H I 6 .   ? 16.241  19.677  -57.250 0.00 113.08 ? 503  A1A5H A H51 1 
HETATM 17629 H  H53 . A1A5H I 6 .   ? 13.770  18.623  -58.582 0.00 108.89 ? 503  A1A5H A H53 1 
HETATM 17630 H  H52 . A1A5H I 6 .   ? 14.507  20.153  -58.891 0.00 108.89 ? 503  A1A5H A H52 1 
HETATM 17631 H  H55 . A1A5H I 6 .   ? 12.666  20.366  -57.186 0.00 111.25 ? 503  A1A5H A H55 1 
HETATM 17632 H  H54 . A1A5H I 6 .   ? 14.184  20.783  -56.479 0.00 111.25 ? 503  A1A5H A H54 1 
HETATM 17633 H  H32 . A1A5H I 6 .   ? 20.077  18.601  -60.763 0.00 108.49 ? 503  A1A5H A H32 1 
HETATM 17634 H  H33 . A1A5H I 6 .   ? 15.755  16.253  -59.052 0.00 113.18 ? 503  A1A5H A H33 1 
HETATM 17635 H  H34 . A1A5H I 6 .   ? 15.086  17.456  -60.119 0.00 113.18 ? 503  A1A5H A H34 1 
HETATM 17636 H  H56 . A1A5H I 6 .   ? 14.271  17.202  -55.102 0.00 120.72 ? 503  A1A5H A H56 1 
HETATM 17637 ZN ZN  . ZN    J 4 .   ? 19.983  24.758  -63.582 1.00 97.56  2 900  ZN    C ZN  1 
HETATM 17638 ZN ZN  . ZN    K 4 .   ? 38.832  -32.352 20.336  1.00 102.97 2 501  ZN    D ZN  1 
HETATM 17639 S  S   . SO4   L 5 .   ? 45.739  -28.135 -9.152  1.00 128.37 ? 502  SO4   D S   1 
HETATM 17640 O  O1  . SO4   L 5 .   ? 47.033  -27.758 -9.849  1.00 127.34 ? 502  SO4   D O1  1 
HETATM 17641 O  O2  . SO4   L 5 .   ? 45.608  -27.280 -7.917  1.00 123.65 ? 502  SO4   D O2  1 
HETATM 17642 O  O3  . SO4   L 5 .   ? 44.533  -27.938 -10.052 1.00 119.00 ? 502  SO4   D O3  1 
HETATM 17643 O  O4  . SO4   L 5 .   ? 45.786  -29.597 -8.776  1.00 119.14 ? 502  SO4   D O4  1 
HETATM 17644 C  C1  . A1A5H M 6 .   ? 36.563  -54.100 20.267  1.00 104.01 ? 503  A1A5H D C1  1 
HETATM 17645 C  C2  . A1A5H M 6 .   ? 37.605  -54.965 20.572  1.00 104.23 ? 503  A1A5H D C2  1 
HETATM 17646 C  C3  . A1A5H M 6 .   ? 38.790  -54.914 19.857  1.00 102.57 ? 503  A1A5H D C3  1 
HETATM 17647 C  C11 . A1A5H M 6 .   ? 36.652  -56.967 21.380  1.00 111.76 ? 503  A1A5H D C11 1 
HETATM 17648 C  C13 . A1A5H M 6 .   ? 35.975  -57.340 22.708  1.00 117.08 ? 503  A1A5H D C13 1 
HETATM 17649 C  C14 . A1A5H M 6 .   ? 37.040  -57.751 23.719  1.00 104.50 ? 503  A1A5H D C14 1 
HETATM 17650 C  C15 . A1A5H M 6 .   ? 37.785  -58.963 23.196  1.00 101.50 ? 503  A1A5H D C15 1 
HETATM 17651 C  C17 . A1A5H M 6 .   ? 37.439  -58.175 20.917  1.00 103.99 ? 503  A1A5H D C17 1 
HETATM 17652 C  C18 . A1A5H M 6 .   ? 34.700  -58.108 22.691  1.00 117.88 ? 503  A1A5H D C18 1 
HETATM 17653 C  C19 . A1A5H M 6 .   ? 34.724  -56.690 23.187  1.00 109.30 ? 503  A1A5H D C19 1 
HETATM 17654 C  C20 . A1A5H M 6 .   ? 39.616  -57.881 22.018  1.00 110.54 ? 503  A1A5H D C20 1 
HETATM 17655 C  C21 . A1A5H M 6 .   ? 40.833  -58.692 22.330  1.00 111.12 ? 503  A1A5H D C21 1 
HETATM 17656 C  C22 . A1A5H M 6 .   ? 40.351  -52.039 16.009  1.00 94.12  ? 503  A1A5H D C22 1 
HETATM 17657 C  C23 . A1A5H M 6 .   ? 41.619  -51.378 16.488  1.00 94.54  ? 503  A1A5H D C23 1 
HETATM 17658 C  C24 . A1A5H M 6 .   ? 42.376  -50.816 15.300  1.00 93.75  ? 503  A1A5H D C24 1 
HETATM 17659 C  C25 . A1A5H M 6 .   ? 42.666  -51.874 14.285  1.00 96.38  ? 503  A1A5H D C25 1 
HETATM 17660 C  C27 . A1A5H M 6 .   ? 40.631  -53.060 14.928  1.00 97.35  ? 503  A1A5H D C27 1 
HETATM 17661 C  C4  . A1A5H M 6 .   ? 38.926  -53.991 18.831  1.00 99.50  ? 503  A1A5H D C4  1 
HETATM 17662 C  C5  . A1A5H M 6 .   ? 37.896  -53.127 18.526  1.00 94.57  ? 503  A1A5H D C5  1 
HETATM 17663 C  C6  . A1A5H M 6 .   ? 36.711  -53.176 19.248  1.00 93.57  ? 503  A1A5H D C6  1 
HETATM 17664 C  C7  . A1A5H M 6 .   ? 40.081  -53.744 17.910  1.00 99.41  ? 503  A1A5H D C7  1 
HETATM 17665 C  C9  . A1A5H M 6 .   ? 38.314  -52.268 17.398  1.00 92.16  ? 503  A1A5H D C9  1 
HETATM 17666 N  N16 . A1A5H M 6 .   ? 38.401  -58.689 21.893  1.00 103.58 ? 503  A1A5H D N16 1 
HETATM 17667 N  N26 . A1A5H M 6 .   ? 41.768  -52.897 14.189  1.00 96.09  ? 503  A1A5H D N26 1 
HETATM 17668 N  N8  . A1A5H M 6 .   ? 39.576  -52.655 17.070  1.00 94.95  ? 503  A1A5H D N8  1 
HETATM 17669 O  O10 . A1A5H M 6 .   ? 37.692  -51.382 16.854  1.00 89.32  ? 503  A1A5H D O10 1 
HETATM 17670 O  O12 . A1A5H M 6 .   ? 37.508  -55.867 21.605  1.00 105.96 ? 503  A1A5H D O12 1 
HETATM 17671 O  O28 . A1A5H M 6 .   ? 39.852  -53.980 14.714  1.00 100.51 ? 503  A1A5H D O28 1 
HETATM 17672 O  O29 . A1A5H M 6 .   ? 43.660  -51.850 13.571  1.00 90.52  ? 503  A1A5H D O29 1 
HETATM 17673 H  H30 . A1A5H M 6 .   ? 35.624  -54.145 20.817  0.00 124.90 ? 503  A1A5H D H30 1 
HETATM 17674 H  H31 . A1A5H M 6 .   ? 39.610  -55.585 20.093  0.00 123.19 ? 503  A1A5H D H31 1 
HETATM 17675 H  H35 . A1A5H M 6 .   ? 35.863  -56.702 20.683  0.00 134.20 ? 503  A1A5H D H35 1 
HETATM 17676 H  H36 . A1A5H M 6 .   ? 36.541  -57.971 24.660  0.00 125.50 ? 503  A1A5H D H36 1 
HETATM 17677 H  H37 . A1A5H M 6 .   ? 37.713  -56.930 23.959  0.00 125.50 ? 503  A1A5H D H37 1 
HETATM 17678 H  H39 . A1A5H M 6 .   ? 37.115  -59.815 23.111  0.00 121.90 ? 503  A1A5H D H39 1 
HETATM 17679 H  H38 . A1A5H M 6 .   ? 38.548  -59.277 23.903  0.00 121.90 ? 503  A1A5H D H38 1 
HETATM 17680 H  H40 . A1A5H M 6 .   ? 36.762  -58.978 20.633  0.00 124.89 ? 503  A1A5H D H40 1 
HETATM 17681 H  H41 . A1A5H M 6 .   ? 37.964  -57.939 19.993  0.00 124.89 ? 503  A1A5H D H41 1 
HETATM 17682 H  H43 . A1A5H M 6 .   ? 34.240  -58.378 21.745  0.00 141.56 ? 503  A1A5H D H43 1 
HETATM 17683 H  H42 . A1A5H M 6 .   ? 34.556  -58.934 23.385  0.00 141.56 ? 503  A1A5H D H42 1 
HETATM 17684 H  H45 . A1A5H M 6 .   ? 34.558  -56.504 24.243  0.00 131.25 ? 503  A1A5H D H45 1 
HETATM 17685 H  H44 . A1A5H M 6 .   ? 34.282  -55.878 22.613  0.00 131.25 ? 503  A1A5H D H44 1 
HETATM 17686 H  H47 . A1A5H M 6 .   ? 39.805  -57.396 21.066  0.00 132.75 ? 503  A1A5H D H47 1 
HETATM 17687 H  H46 . A1A5H M 6 .   ? 39.577  -57.070 22.741  0.00 132.75 ? 503  A1A5H D H46 1 
HETATM 17688 H  H50 . A1A5H M 6 .   ? 40.855  -59.013 23.370  0.00 133.44 ? 503  A1A5H D H50 1 
HETATM 17689 H  H48 . A1A5H M 6 .   ? 40.867  -59.588 21.714  0.00 133.44 ? 503  A1A5H D H48 1 
HETATM 17690 H  H49 . A1A5H M 6 .   ? 41.762  -58.156 22.151  0.00 133.44 ? 503  A1A5H D H49 1 
HETATM 17691 H  H51 . A1A5H M 6 .   ? 39.762  -51.254 15.541  0.00 113.04 ? 503  A1A5H D H51 1 
HETATM 17692 H  H53 . A1A5H M 6 .   ? 42.237  -52.097 17.011  0.00 113.55 ? 503  A1A5H D H53 1 
HETATM 17693 H  H52 . A1A5H M 6 .   ? 41.388  -50.607 17.219  0.00 113.55 ? 503  A1A5H D H52 1 
HETATM 17694 H  H55 . A1A5H M 6 .   ? 43.308  -50.347 15.608  0.00 112.60 ? 503  A1A5H D H55 1 
HETATM 17695 H  H54 . A1A5H M 6 .   ? 41.805  -50.014 14.833  0.00 112.60 ? 503  A1A5H D H54 1 
HETATM 17696 H  H32 . A1A5H M 6 .   ? 35.928  -52.464 19.012  0.00 112.38 ? 503  A1A5H D H32 1 
HETATM 17697 H  H33 . A1A5H M 6 .   ? 40.980  -53.473 18.448  0.00 119.38 ? 503  A1A5H D H33 1 
HETATM 17698 H  H34 . A1A5H M 6 .   ? 40.322  -54.632 17.328  0.00 119.38 ? 503  A1A5H D H34 1 
HETATM 17699 H  H56 . A1A5H M 6 .   ? 41.973  -53.623 13.512  0.00 115.41 ? 503  A1A5H D H56 1 
HETATM 17700 ZN ZN  . ZN    N 4 .   ? 35.668  -46.409 22.006  1.00 101.47 2 900  ZN    F ZN  1 
HETATM 17701 O  O   . HOH   O 7 .   ? 3.773   25.435  -41.550 1.00 92.71  ? 601  HOH   A O   1 
HETATM 17702 O  O   . HOH   O 7 .   ? 13.889  38.092  -43.285 1.00 69.94  ? 602  HOH   A O   1 
HETATM 17703 O  O   . HOH   O 7 .   ? 31.864  45.203  -33.126 1.00 71.68  ? 603  HOH   A O   1 
HETATM 17704 O  O   . HOH   O 7 .   ? 16.613  44.940  -31.758 1.00 77.62  ? 604  HOH   A O   1 
HETATM 17705 O  O   . HOH   O 7 .   ? 13.532  13.365  -49.806 1.00 83.13  ? 605  HOH   A O   1 
HETATM 17706 O  O   . HOH   O 7 .   ? 31.049  20.808  -29.999 1.00 81.15  ? 606  HOH   A O   1 
HETATM 17707 O  O   . HOH   P 7 .   ? 47.480  55.422  -11.273 1.00 92.77  ? 1201 HOH   B O   1 
HETATM 17708 O  O   . HOH   P 7 .   ? 26.663  57.479  7.812   1.00 72.74  ? 1202 HOH   B O   1 
HETATM 17709 O  O   . HOH   P 7 .   ? 29.133  50.604  -6.169  1.00 83.13  ? 1203 HOH   B O   1 
HETATM 17710 O  O   . HOH   P 7 .   ? 44.379  52.221  2.583   1.00 81.60  ? 1204 HOH   B O   1 
HETATM 17711 O  O   . HOH   P 7 .   ? 6.449   53.008  -29.891 1.00 74.04  ? 1205 HOH   B O   1 
HETATM 17712 O  O   . HOH   P 7 .   ? -2.187  71.260  -9.005  1.00 96.75  ? 1206 HOH   B O   1 
HETATM 17713 O  O   . HOH   P 7 .   ? 44.086  31.943  0.211   1.00 86.14  ? 1207 HOH   B O   1 
HETATM 17714 O  O   . HOH   P 7 .   ? 8.910   50.393  -25.851 1.00 71.96  ? 1208 HOH   B O   1 
HETATM 17715 O  O   . HOH   P 7 .   ? 22.844  42.169  16.261  1.00 94.35  ? 1209 HOH   B O   1 
HETATM 17716 O  O   . HOH   P 7 .   ? 5.420   52.319  2.218   1.00 92.83  ? 1210 HOH   B O   1 
HETATM 17717 O  O   . HOH   P 7 .   ? 25.201  51.924  25.088  1.00 99.89  ? 1211 HOH   B O   1 
HETATM 17718 O  O   . HOH   P 7 .   ? 10.341  68.685  -40.359 1.00 76.35  ? 1212 HOH   B O   1 
HETATM 17719 O  O   . HOH   P 7 .   ? 27.525  44.306  3.497   1.00 69.20  ? 1213 HOH   B O   1 
HETATM 17720 O  O   . HOH   P 7 .   ? 19.862  23.177  14.130  1.00 94.76  ? 1214 HOH   B O   1 
HETATM 17721 O  O   . HOH   P 7 .   ? 10.921  83.046  -22.393 1.00 92.03  ? 1215 HOH   B O   1 
HETATM 17722 O  O   . HOH   P 7 .   ? 15.870  61.535  1.508   1.00 80.64  ? 1216 HOH   B O   1 
HETATM 17723 O  O   . HOH   Q 7 .   ? 15.615  23.941  -75.274 1.00 98.67  ? 1001 HOH   C O   1 
HETATM 17724 O  O   . HOH   R 7 .   ? 38.572  -45.328 -5.537  1.00 96.49  ? 601  HOH   D O   1 
HETATM 17725 O  O   . HOH   R 7 .   ? 27.697  -47.484 3.081   1.00 98.06  ? 602  HOH   D O   1 
HETATM 17726 O  O   . HOH   R 7 .   ? 44.819  -46.173 -27.221 1.00 113.03 ? 603  HOH   D O   1 
HETATM 17727 O  O   . HOH   R 7 .   ? 41.904  -32.496 2.156   1.00 78.54  ? 604  HOH   D O   1 
HETATM 17728 O  O   . HOH   R 7 .   ? 49.881  -39.182 24.843  1.00 84.80  ? 605  HOH   D O   1 
HETATM 17729 O  O   . HOH   R 7 .   ? 32.027  -44.629 13.205  1.00 78.53  ? 606  HOH   D O   1 
HETATM 17730 O  O   . HOH   R 7 .   ? 29.480  -27.203 -34.293 1.00 103.97 ? 607  HOH   D O   1 
HETATM 17731 O  O   . HOH   S 7 .   ? 29.590  -9.339  -58.305 1.00 96.29  ? 1201 HOH   E O   1 
HETATM 17732 O  O   . HOH   S 7 .   ? 27.676  -12.249 -49.529 1.00 77.10  ? 1202 HOH   E O   1 
HETATM 17733 O  O   . HOH   S 7 .   ? 39.116  -9.434  -43.278 1.00 70.61  ? 1203 HOH   E O   1 
HETATM 17734 O  O   . HOH   S 7 .   ? 23.922  -30.379 -58.898 1.00 100.85 ? 1204 HOH   E O   1 
HETATM 17735 O  O   . HOH   S 7 .   ? 52.248  -21.381 -38.086 1.00 81.98  ? 1205 HOH   E O   1 
HETATM 17736 O  O   . HOH   S 7 .   ? 13.426  -25.491 -65.216 1.00 86.55  ? 1206 HOH   E O   1 
HETATM 17737 O  O   . HOH   S 7 .   ? 45.267  -2.320  -0.187  1.00 70.21  ? 1207 HOH   E O   1 
HETATM 17738 O  O   . HOH   S 7 .   ? 34.071  -26.038 -48.612 1.00 83.54  ? 1208 HOH   E O   1 
HETATM 17739 O  O   . HOH   S 7 .   ? 17.444  -16.340 -62.702 1.00 104.21 ? 1209 HOH   E O   1 
HETATM 17740 O  O   . HOH   S 7 .   ? 10.662  -17.282 -42.783 1.00 80.41  ? 1210 HOH   E O   1 
HETATM 17741 O  O   . HOH   S 7 .   ? 50.774  -14.688 -22.444 1.00 91.90  ? 1211 HOH   E O   1 
HETATM 17742 O  O   . HOH   T 7 .   ? 43.197  -46.689 31.048  1.00 89.14  ? 1001 HOH   F O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N  N   . HIS   A 4   ? 1.9923 2.1408 2.1959 -0.0855 -0.0194 0.0069  73   HIS   A N   
2     C  CA  . HIS   A 4   ? 2.0299 2.1781 2.2487 -0.0880 -0.0145 0.0070  73   HIS   A CA  
3     C  C   . HIS   A 4   ? 2.0878 2.2377 2.3148 -0.0890 -0.0205 0.0052  73   HIS   A C   
4     O  O   . HIS   A 4   ? 2.1302 2.2845 2.3573 -0.0876 -0.0288 0.0024  73   HIS   A O   
5     C  CB  . HIS   A 4   ? 2.0153 2.1547 2.2271 -0.0888 -0.0053 0.0112  73   HIS   A CB  
6     C  CG  . HIS   A 4   ? 2.0667 2.2031 2.2705 -0.0877 0.0014  0.0132  73   HIS   A CG  
7     N  ND1 . HIS   A 4   ? 2.1300 2.2620 2.3148 -0.0854 0.0005  0.0148  73   HIS   A ND1 
8     C  CD2 . HIS   A 4   ? 2.0383 2.1752 2.2504 -0.0884 0.0091  0.0137  73   HIS   A CD2 
9     C  CE1 . HIS   A 4   ? 2.0919 2.2211 2.2726 -0.0846 0.0071  0.0162  73   HIS   A CE1 
10    N  NE2 . HIS   A 4   ? 2.1032 2.2354 2.3002 -0.0864 0.0127  0.0156  73   HIS   A NE2 
11    N  N   . ASP   A 5   ? 2.0926 2.2384 2.3262 -0.0911 -0.0159 0.0067  74   ASP   A N   
12    C  CA  . ASP   A 5   ? 2.0702 2.2161 2.3112 -0.0922 -0.0207 0.0053  74   ASP   A CA  
13    C  C   . ASP   A 5   ? 2.0695 2.2066 2.2990 -0.0925 -0.0176 0.0089  74   ASP   A C   
14    O  O   . ASP   A 5   ? 2.0284 2.1594 2.2547 -0.0935 -0.0090 0.0122  74   ASP   A O   
15    C  CB  . ASP   A 5   ? 2.0608 2.2103 2.3238 -0.0950 -0.0189 0.0031  74   ASP   A CB  
16    C  CG  . ASP   A 5   ? 2.0805 2.2385 2.3558 -0.0945 -0.0217 -0.0006 74   ASP   A CG  
17    O  OD1 . ASP   A 5   ? 2.1093 2.2706 2.3762 -0.0920 -0.0268 -0.0019 74   ASP   A OD1 
18    O  OD2 . ASP   A 5   ? 2.0805 2.2418 2.3741 -0.0966 -0.0186 -0.0020 74   ASP   A OD2 
19    N  N   . ASP   A 6   ? 2.0747 2.2107 2.2980 -0.0914 -0.0244 0.0083  75   ASP   A N   
20    C  CA  . ASP   A 6   ? 2.0703 2.1981 2.2793 -0.0907 -0.0230 0.0116  75   ASP   A CA  
21    C  C   . ASP   A 6   ? 2.0207 2.1411 2.2324 -0.0929 -0.0142 0.0147  75   ASP   A C   
22    O  O   . ASP   A 6   ? 1.9705 2.0830 2.1678 -0.0919 -0.0100 0.0183  75   ASP   A O   
23    C  CB  . ASP   A 6   ? 2.0865 2.2150 2.2939 -0.0896 -0.0314 0.0099  75   ASP   A CB  
24    C  CG  . ASP   A 6   ? 2.0149 2.1365 2.2049 -0.0878 -0.0318 0.0130  75   ASP   A CG  
25    O  OD1 . ASP   A 6   ? 1.9778 2.0974 2.1541 -0.0860 -0.0303 0.0150  75   ASP   A OD1 
26    O  OD2 . ASP   A 6   ? 1.9935 2.1115 2.1835 -0.0879 -0.0340 0.0132  75   ASP   A OD2 
27    N  N   . ASP   A 7   ? 1.8180 1.9405 2.0480 -0.0958 -0.0112 0.0134  76   ASP   A N   
28    C  CA  . ASP   A 7   ? 1.6579 1.7734 1.8928 -0.0983 -0.0023 0.0163  76   ASP   A CA  
29    C  C   . ASP   A 7   ? 1.5938 1.7134 1.8461 -0.1007 0.0043  0.0156  76   ASP   A C   
30    O  O   . ASP   A 7   ? 1.5680 1.6873 1.8364 -0.1037 0.0079  0.0153  76   ASP   A O   
31    C  CB  . ASP   A 7   ? 1.6948 1.8074 1.9357 -0.0998 -0.0055 0.0157  76   ASP   A CB  
32    C  CG  . ASP   A 7   ? 1.6631 1.7663 1.8855 -0.0981 -0.0051 0.0190  76   ASP   A CG  
33    O  OD1 . ASP   A 7   ? 1.6233 1.7193 1.8330 -0.0973 0.0019  0.0228  76   ASP   A OD1 
34    O  OD2 . ASP   A 7   ? 1.5733 1.6758 1.7936 -0.0974 -0.0120 0.0178  76   ASP   A OD2 
35    N  N   . SER   A 8   ? 1.6127 1.7360 1.8620 -0.0993 0.0061  0.0154  77   SER   A N   
36    C  CA  . SER   A 8   ? 1.5536 1.6809 1.8177 -0.1009 0.0125  0.0149  77   SER   A CA  
37    C  C   . SER   A 8   ? 1.4716 1.5901 1.7311 -0.1017 0.0250  0.0196  77   SER   A C   
38    O  O   . SER   A 8   ? 1.4177 1.5271 1.6588 -0.1002 0.0279  0.0231  77   SER   A O   
39    C  CB  . SER   A 8   ? 1.6208 1.7547 1.8815 -0.0986 0.0093  0.0129  77   SER   A CB  
40    O  OG  . SER   A 8   ? 1.5758 1.7139 1.8501 -0.0997 0.0154  0.0123  77   SER   A OG  
41    N  N   . CYS   A 9   ? 1.4817 1.6028 1.7584 -0.1040 0.0324  0.0196  78   CYS   A N   
42    C  CA  . CYS   A 9   ? 1.4551 1.5686 1.7277 -0.1042 0.0453  0.0240  78   CYS   A CA  
43    C  C   . CYS   A 9   ? 1.4809 1.5993 1.7549 -0.1027 0.0483  0.0233  78   CYS   A C   
44    O  O   . CYS   A 9   ? 1.5170 1.6428 1.8112 -0.1044 0.0504  0.0213  78   CYS   A O   
45    C  CB  . CYS   A 9   ? 1.4538 1.5654 1.7452 -0.1080 0.0531  0.0252  78   CYS   A CB  
46    S  SG  . CYS   A 9   ? 1.6809 1.7896 1.9792 -0.1107 0.0483  0.0245  78   CYS   A SG  
47    N  N   . GLN   A 10  ? 1.3611 1.4752 1.6141 -0.0994 0.0485  0.0250  79   GLN   A N   
48    C  CA  . GLN   A 10  ? 1.3525 1.4705 1.6044 -0.0976 0.0507  0.0243  79   GLN   A CA  
49    C  C   . GLN   A 10  ? 1.2847 1.3927 1.5238 -0.0960 0.0625  0.0289  79   GLN   A C   
50    O  O   . GLN   A 10  ? 1.2282 1.3255 1.4532 -0.0953 0.0671  0.0326  79   GLN   A O   
51    C  CB  . GLN   A 10  ? 1.4125 1.5342 1.6510 -0.0948 0.0406  0.0220  79   GLN   A CB  
52    C  CG  . GLN   A 10  ? 1.5142 1.6460 1.7645 -0.0956 0.0292  0.0172  79   GLN   A CG  
53    C  CD  . GLN   A 10  ? 1.5853 1.7269 1.8529 -0.0960 0.0281  0.0138  79   GLN   A CD  
54    O  OE1 . GLN   A 10  ? 1.5636 1.7052 1.8364 -0.0960 0.0363  0.0150  79   GLN   A OE1 
55    N  NE2 . GLN   A 10  ? 1.5939 1.7437 1.8702 -0.0960 0.0180  0.0095  79   GLN   A NE2 
56    N  N   . VAL   A 11  ? 1.3059 1.4170 1.5489 -0.0949 0.0672  0.0286  80   VAL   A N   
57    C  CA  . VAL   A 11  ? 1.3317 1.4332 1.5609 -0.0926 0.0780  0.0326  80   VAL   A CA  
58    C  C   . VAL   A 11  ? 1.3016 1.4024 1.5122 -0.0890 0.0734  0.0319  80   VAL   A C   
59    O  O   . VAL   A 11  ? 1.2917 1.4020 1.5083 -0.0887 0.0658  0.0281  80   VAL   A O   
60    C  CB  . VAL   A 11  ? 1.3132 1.4169 1.5604 -0.0940 0.0891  0.0336  80   VAL   A CB  
61    C  CG1 . VAL   A 11  ? 1.3043 1.4218 1.5717 -0.0950 0.0840  0.0290  80   VAL   A CG1 
62    C  CG2 . VAL   A 11  ? 1.3492 1.4423 1.5798 -0.0909 0.1002  0.0377  80   VAL   A CG2 
63    N  N   . ILE   A 12  ? 1.2952 1.3842 1.4831 -0.0861 0.0779  0.0354  81   ILE   A N   
64    C  CA  . ILE   A 12  ? 1.2331 1.3194 1.4007 -0.0827 0.0725  0.0349  81   ILE   A CA  
65    C  C   . ILE   A 12  ? 1.3612 1.4342 1.5097 -0.0796 0.0822  0.0389  81   ILE   A C   
66    O  O   . ILE   A 12  ? 1.3727 1.4353 1.5134 -0.0793 0.0889  0.0426  81   ILE   A O   
67    C  CB  . ILE   A 12  ? 1.1858 1.2714 1.3415 -0.0823 0.0619  0.0339  81   ILE   A CB  
68    C  CG1 . ILE   A 12  ? 1.1822 1.2803 1.3552 -0.0848 0.0522  0.0298  81   ILE   A CG1 
69    C  CG2 . ILE   A 12  ? 1.2635 1.3451 1.3979 -0.0788 0.0571  0.0337  81   ILE   A CG2 
70    C  CD1 . ILE   A 12  ? 1.1468 1.2435 1.3119 -0.0849 0.0441  0.0295  81   ILE   A CD1 
71    N  N   . PRO   A 13  ? 1.3614 1.4333 1.5005 -0.0768 0.0830  0.0385  82   PRO   A N   
72    C  CA  . PRO   A 13  ? 1.3810 1.4392 1.5002 -0.0732 0.0918  0.0423  82   PRO   A CA  
73    C  C   . PRO   A 13  ? 1.3580 1.4057 1.4520 -0.0705 0.0869  0.0437  82   PRO   A C   
74    O  O   . PRO   A 13  ? 1.3278 1.3800 1.4176 -0.0707 0.0757  0.0414  82   PRO   A O   
75    C  CB  . PRO   A 13  ? 1.3929 1.4546 1.5116 -0.0713 0.0925  0.0406  82   PRO   A CB  
76    C  CG  . PRO   A 13  ? 1.3690 1.4441 1.4980 -0.0729 0.0804  0.0359  82   PRO   A CG  
77    C  CD  . PRO   A 13  ? 1.2832 1.3662 1.4308 -0.0768 0.0768  0.0346  82   PRO   A CD  
78    N  N   . VAL   A 14  ? 1.4541 1.4873 1.5311 -0.0677 0.0956  0.0477  83   VAL   A N   
79    C  CA  . VAL   A 14  ? 1.5288 1.5499 1.5816 -0.0647 0.0924  0.0496  83   VAL   A CA  
80    C  C   . VAL   A 14  ? 1.6281 1.6402 1.6594 -0.0601 0.0933  0.0502  83   VAL   A C   
81    O  O   . VAL   A 14  ? 1.7341 1.7376 1.7595 -0.0578 0.1041  0.0528  83   VAL   A O   
82    C  CB  . VAL   A 14  ? 1.4638 1.4732 1.5114 -0.0645 0.1014  0.0539  83   VAL   A CB  
83    C  CG1 . VAL   A 14  ? 1.4972 1.4942 1.5193 -0.0610 0.0971  0.0555  83   VAL   A CG1 
84    C  CG2 . VAL   A 14  ? 1.4369 1.4548 1.5066 -0.0691 0.1010  0.0532  83   VAL   A CG2 
85    N  N   . LEU   A 15  ? 1.5713 1.5843 1.5903 -0.0586 0.0824  0.0479  84   LEU   A N   
86    C  CA  . LEU   A 15  ? 1.7507 1.7524 1.7464 -0.0540 0.0827  0.0487  84   LEU   A CA  
87    C  C   . LEU   A 15  ? 1.8878 1.8720 1.8649 -0.0506 0.0913  0.0531  84   LEU   A C   
88    O  O   . LEU   A 15  ? 1.8892 1.8687 1.8604 -0.0507 0.0888  0.0544  84   LEU   A O   
89    C  CB  . LEU   A 15  ? 1.6919 1.6959 1.6767 -0.0530 0.0693  0.0459  84   LEU   A CB  
90    C  CG  . LEU   A 15  ? 1.5740 1.5861 1.5635 -0.0531 0.0654  0.0427  84   LEU   A CG  
91    C  CD1 . LEU   A 15  ? 1.7209 1.7231 1.6984 -0.0494 0.0738  0.0443  84   LEU   A CD1 
92    C  CD2 . LEU   A 15  ? 1.5614 1.5894 1.5778 -0.0574 0.0651  0.0405  84   LEU   A CD2 
93    N  N   . PRO   A 16  ? 2.1858 2.1597 2.1535 -0.0474 0.1019  0.0556  85   PRO   A N   
94    C  CA  . PRO   A 16  ? 2.2244 2.1818 2.1779 -0.0446 0.1126  0.0603  85   PRO   A CA  
95    C  C   . PRO   A 16  ? 2.2343 2.1785 2.1624 -0.0408 0.1069  0.0614  85   PRO   A C   
96    O  O   . PRO   A 16  ? 2.2367 2.1796 2.1651 -0.0420 0.1044  0.0624  85   PRO   A O   
97    C  CB  . PRO   A 16  ? 2.2589 2.2083 2.2049 -0.0411 0.1232  0.0621  85   PRO   A CB  
98    C  CG  . PRO   A 16  ? 2.2465 2.2044 2.1936 -0.0409 0.1151  0.0581  85   PRO   A CG  
99    C  CD  . PRO   A 16  ? 2.1906 2.1670 2.1601 -0.0461 0.1050  0.0544  85   PRO   A CD  
100   N  N   . GLN   A 17  ? 2.0351 1.9694 1.9412 -0.0360 0.1044  0.0611  86   GLN   A N   
101   C  CA  . GLN   A 17  ? 1.9659 1.8854 1.8463 -0.0317 0.1001  0.0623  86   GLN   A CA  
102   C  C   . GLN   A 17  ? 1.9645 1.8922 1.8472 -0.0336 0.0859  0.0595  86   GLN   A C   
103   O  O   . GLN   A 17  ? 1.9490 1.8664 1.8151 -0.0309 0.0824  0.0607  86   GLN   A O   
104   C  CB  . GLN   A 17  ? 1.9086 1.8157 1.7653 -0.0260 0.0996  0.0621  86   GLN   A CB  
105   N  N   . VAL   A 18  ? 1.9412 1.8867 1.8437 -0.0380 0.0779  0.0558  87   VAL   A N   
106   C  CA  . VAL   A 18  ? 1.8863 1.8395 1.7910 -0.0397 0.0650  0.0533  87   VAL   A CA  
107   C  C   . VAL   A 18  ? 1.9401 1.8904 1.8469 -0.0408 0.0665  0.0556  87   VAL   A C   
108   O  O   . VAL   A 18  ? 1.9203 1.8718 1.8401 -0.0432 0.0755  0.0576  87   VAL   A O   
109   C  CB  . VAL   A 18  ? 1.7761 1.7484 1.7029 -0.0442 0.0578  0.0494  87   VAL   A CB  
110   C  CG1 . VAL   A 18  ? 1.7774 1.7519 1.7037 -0.0433 0.0587  0.0477  87   VAL   A CG1 
111   C  CG2 . VAL   A 18  ? 1.7970 1.7796 1.7477 -0.0488 0.0628  0.0498  87   VAL   A CG2 
112   N  N   . MET   A 19  ? 1.9105 1.8567 1.8047 -0.0389 0.0576  0.0551  88   MET   A N   
113   C  CA  . MET   A 19  ? 1.8584 1.7998 1.7506 -0.0391 0.0580  0.0572  88   MET   A CA  
114   C  C   . MET   A 19  ? 1.8494 1.7975 1.7404 -0.0393 0.0442  0.0544  88   MET   A C   
115   O  O   . MET   A 19  ? 1.9080 1.8518 1.7839 -0.0361 0.0368  0.0529  88   MET   A O   
116   C  CB  . MET   A 19  ? 1.9152 1.8360 1.7837 -0.0339 0.0656  0.0611  88   MET   A CB  
117   C  CG  . MET   A 19  ? 2.0100 1.9199 1.8533 -0.0284 0.0580  0.0602  88   MET   A CG  
118   S  SD  . MET   A 19  ? 2.1967 2.0806 2.0076 -0.0211 0.0640  0.0642  88   MET   A SD  
119   C  CE  . MET   A 19  ? 2.0507 1.9324 1.8469 -0.0181 0.0481  0.0618  88   MET   A CE  
120   N  N   . MET   A 20  ? 1.7481 1.7064 1.6549 -0.0429 0.0407  0.0537  89   MET   A N   
121   C  CA  . MET   A 20  ? 1.6649 1.6312 1.5725 -0.0433 0.0277  0.0508  89   MET   A CA  
122   C  C   . MET   A 20  ? 1.6077 1.5840 1.5327 -0.0471 0.0256  0.0504  89   MET   A C   
123   O  O   . MET   A 20  ? 1.5986 1.5783 1.5381 -0.0502 0.0330  0.0515  89   MET   A O   
124   C  CB  . MET   A 20  ? 1.6467 1.6239 1.5605 -0.0444 0.0209  0.0472  89   MET   A CB  
125   C  CG  . MET   A 20  ? 1.6488 1.6360 1.5664 -0.0453 0.0082  0.0442  89   MET   A CG  
126   S  SD  . MET   A 20  ? 1.7931 1.7946 1.7227 -0.0477 0.0019  0.0402  89   MET   A SD  
127   C  CE  . MET   A 20  ? 1.6297 1.6386 1.5588 -0.0476 -0.0122 0.0377  89   MET   A CE  
128   N  N   . ILE   A 21  ? 1.4986 1.4791 1.4220 -0.0467 0.0155  0.0489  90   ILE   A N   
129   C  CA  . ILE   A 21  ? 1.3787 1.3716 1.3196 -0.0503 0.0106  0.0474  90   ILE   A CA  
130   C  C   . ILE   A 21  ? 1.3639 1.3707 1.3145 -0.0520 0.0019  0.0436  90   ILE   A C   
131   O  O   . ILE   A 21  ? 1.3661 1.3724 1.3067 -0.0497 -0.0059 0.0422  90   ILE   A O   
132   C  CB  . ILE   A 21  ? 1.3537 1.3418 1.2867 -0.0485 0.0059  0.0484  90   ILE   A CB  
133   C  CG1 . ILE   A 21  ? 1.3516 1.3285 1.2806 -0.0481 0.0152  0.0520  90   ILE   A CG1 
134   C  CG2 . ILE   A 21  ? 1.2617 1.2635 1.2114 -0.0516 -0.0011 0.0462  90   ILE   A CG2 
135   C  CD1 . ILE   A 21  ? 1.4765 1.4405 1.3935 -0.0458 0.0251  0.0547  90   ILE   A CD1 
136   N  N   . LEU   A 22  ? 1.3121 1.3307 1.2821 -0.0559 0.0032  0.0420  91   LEU   A N   
137   C  CA  . LEU   A 22  ? 1.1840 1.2154 1.1640 -0.0576 -0.0038 0.0386  91   LEU   A CA  
138   C  C   . LEU   A 22  ? 1.1729 1.2154 1.1673 -0.0600 -0.0098 0.0369  91   LEU   A C   
139   O  O   . LEU   A 22  ? 1.1170 1.1636 1.1252 -0.0627 -0.0061 0.0371  91   LEU   A O   
140   C  CB  . LEU   A 22  ? 1.1824 1.2182 1.1726 -0.0595 0.0021  0.0378  91   LEU   A CB  
141   C  CG  . LEU   A 22  ? 1.1163 1.1651 1.1180 -0.0614 -0.0040 0.0343  91   LEU   A CG  
142   C  CD1 . LEU   A 22  ? 1.1565 1.2037 1.1454 -0.0590 -0.0108 0.0331  91   LEU   A CD1 
143   C  CD2 . LEU   A 22  ? 1.0922 1.1453 1.1058 -0.0632 0.0026  0.0337  91   LEU   A CD2 
144   N  N   . ILE   A 23  ? 1.1733 1.2202 1.1646 -0.0591 -0.0191 0.0353  92   ILE   A N   
145   C  CA  . ILE   A 23  ? 1.1413 1.1983 1.1451 -0.0609 -0.0248 0.0338  92   ILE   A CA  
146   C  C   . ILE   A 23  ? 1.1360 1.2053 1.1543 -0.0634 -0.0274 0.0310  92   ILE   A C   
147   O  O   . ILE   A 23  ? 1.1099 1.1814 1.1248 -0.0628 -0.0301 0.0296  92   ILE   A O   
148   C  CB  . ILE   A 23  ? 1.0602 1.1170 1.0557 -0.0587 -0.0332 0.0336  92   ILE   A CB  
149   C  CG1 . ILE   A 23  ? 1.0656 1.1092 1.0445 -0.0555 -0.0314 0.0362  92   ILE   A CG1 
150   C  CG2 . ILE   A 23  ? 0.9637 1.0291 0.9714 -0.0603 -0.0373 0.0325  92   ILE   A CG2 
151   C  CD1 . ILE   A 23  ? 1.1559 1.1906 1.1188 -0.0527 -0.0308 0.0367  92   ILE   A CD1 
152   N  N   . PRO   A 24  ? 1.1139 1.1907 1.1478 -0.0660 -0.0268 0.0299  93   PRO   A N   
153   C  CA  . PRO   A 24  ? 1.0826 1.1707 1.1295 -0.0679 -0.0298 0.0271  93   PRO   A CA  
154   C  C   . PRO   A 24  ? 1.0541 1.1473 1.0970 -0.0668 -0.0377 0.0253  93   PRO   A C   
155   O  O   . PRO   A 24  ? 1.0955 1.1901 1.1353 -0.0657 -0.0434 0.0253  93   PRO   A O   
156   C  CB  . PRO   A 24  ? 1.0309 1.1250 1.0918 -0.0698 -0.0310 0.0262  93   PRO   A CB  
157   C  CG  . PRO   A 24  ? 0.9701 1.0557 1.0291 -0.0700 -0.0244 0.0287  93   PRO   A CG  
158   C  CD  . PRO   A 24  ? 1.0297 1.1045 1.0701 -0.0672 -0.0233 0.0312  93   PRO   A CD  
159   N  N   . GLY   A 25  ? 1.0408 1.1370 1.0842 -0.0670 -0.0379 0.0239  94   GLY   A N   
160   C  CA  . GLY   A 25  ? 1.0550 1.1556 1.0951 -0.0663 -0.0448 0.0224  94   GLY   A CA  
161   C  C   . GLY   A 25  ? 1.1220 1.2147 1.1465 -0.0641 -0.0458 0.0232  94   GLY   A C   
162   O  O   . GLY   A 25  ? 1.1573 1.2529 1.1786 -0.0634 -0.0519 0.0221  94   GLY   A O   
163   N  N   . GLN   A 26  ? 1.1422 1.2247 1.1570 -0.0628 -0.0399 0.0252  95   GLN   A N   
164   C  CA  . GLN   A 26  ? 1.1313 1.2046 1.1302 -0.0604 -0.0398 0.0260  95   GLN   A CA  
165   C  C   . GLN   A 26  ? 1.1546 1.2271 1.1540 -0.0608 -0.0349 0.0254  95   GLN   A C   
166   O  O   . GLN   A 26  ? 1.1501 1.2258 1.1601 -0.0626 -0.0292 0.0253  95   GLN   A O   
167   C  CB  . GLN   A 26  ? 1.1679 1.2291 1.1543 -0.0581 -0.0357 0.0288  95   GLN   A CB  
168   C  CG  . GLN   A 26  ? 1.1805 1.2376 1.1569 -0.0558 -0.0418 0.0295  95   GLN   A CG  
169   C  CD  . GLN   A 26  ? 1.2528 1.2952 1.2128 -0.0527 -0.0374 0.0322  95   GLN   A CD  
170   O  OE1 . GLN   A 26  ? 1.2581 1.2946 1.2177 -0.0529 -0.0289 0.0341  95   GLN   A OE1 
171   N  NE2 . GLN   A 26  ? 1.2482 1.2843 1.1944 -0.0496 -0.0431 0.0323  95   GLN   A NE2 
172   N  N   . THR   A 27  ? 1.1285 1.1965 1.1168 -0.0591 -0.0374 0.0247  96   THR   A N   
173   C  CA  . THR   A 27  ? 1.1564 1.2229 1.1436 -0.0591 -0.0332 0.0241  96   THR   A CA  
174   C  C   . THR   A 27  ? 1.1945 1.2466 1.1643 -0.0560 -0.0282 0.0261  96   THR   A C   
175   O  O   . THR   A 27  ? 1.2149 1.2593 1.1708 -0.0535 -0.0320 0.0268  96   THR   A O   
176   C  CB  . THR   A 27  ? 1.0982 1.1709 1.0871 -0.0597 -0.0398 0.0214  96   THR   A CB  
177   O  OG1 . THR   A 27  ? 1.2068 1.2718 1.1803 -0.0573 -0.0441 0.0213  96   THR   A OG1 
178   C  CG2 . THR   A 27  ? 1.0724 1.1563 1.0730 -0.0616 -0.0465 0.0199  96   THR   A CG2 
179   N  N   . LEU   A 28  ? 1.1286 1.1768 1.0992 -0.0559 -0.0194 0.0272  97   LEU   A N   
180   C  CA  . LEU   A 28  ? 1.2119 1.2457 1.1653 -0.0526 -0.0137 0.0293  97   LEU   A CA  
181   C  C   . LEU   A 28  ? 1.3476 1.3796 1.2972 -0.0517 -0.0114 0.0282  97   LEU   A C   
182   O  O   . LEU   A 28  ? 1.3041 1.3429 1.2664 -0.0537 -0.0071 0.0275  97   LEU   A O   
183   C  CB  . LEU   A 28  ? 1.2857 1.3137 1.2405 -0.0525 -0.0038 0.0323  97   LEU   A CB  
184   C  CG  . LEU   A 28  ? 1.2735 1.3050 1.2409 -0.0543 0.0053  0.0328  97   LEU   A CG  
185   C  CD1 . LEU   A 28  ? 1.2011 1.2213 1.1624 -0.0528 0.0161  0.0363  97   LEU   A CD1 
186   C  CD2 . LEU   A 28  ? 1.2646 1.3105 1.2539 -0.0583 0.0030  0.0311  97   LEU   A CD2 
187   N  N   . PRO   A 29  ? 1.3781 1.4008 1.3104 -0.0487 -0.0148 0.0279  98   PRO   A N   
188   C  CA  . PRO   A 29  ? 1.2924 1.3118 1.2191 -0.0474 -0.0127 0.0268  98   PRO   A CA  
189   C  C   . PRO   A 29  ? 1.3158 1.3231 1.2324 -0.0447 -0.0020 0.0294  98   PRO   A C   
190   O  O   . PRO   A 29  ? 1.4153 1.4103 1.3166 -0.0416 0.0002  0.0316  98   PRO   A O   
191   C  CB  . PRO   A 29  ? 1.3982 1.4124 1.3106 -0.0453 -0.0218 0.0252  98   PRO   A CB  
192   C  CG  . PRO   A 29  ? 1.4294 1.4467 1.3431 -0.0458 -0.0291 0.0252  98   PRO   A CG  
193   C  CD  . PRO   A 29  ? 1.3622 1.3788 1.2811 -0.0464 -0.0224 0.0278  98   PRO   A CD  
194   N  N   . LEU   A 30  ? 1.3387 1.3492 1.2636 -0.0455 0.0048  0.0293  99   LEU   A N   
195   C  CA  . LEU   A 30  ? 1.4279 1.4282 1.3459 -0.0432 0.0162  0.0320  99   LEU   A CA  
196   C  C   . LEU   A 30  ? 1.4731 1.4698 1.3852 -0.0413 0.0189  0.0310  99   LEU   A C   
197   O  O   . LEU   A 30  ? 1.4758 1.4826 1.3987 -0.0434 0.0153  0.0284  99   LEU   A O   
198   C  CB  . LEU   A 30  ? 1.4356 1.4429 1.3721 -0.0460 0.0245  0.0335  99   LEU   A CB  
199   C  CG  . LEU   A 30  ? 1.4516 1.4579 1.3901 -0.0470 0.0247  0.0354  99   LEU   A CG  
200   C  CD1 . LEU   A 30  ? 1.4708 1.4822 1.4267 -0.0497 0.0336  0.0371  99   LEU   A CD1 
201   C  CD2 . LEU   A 30  ? 1.4329 1.4225 1.3483 -0.0427 0.0262  0.0379  99   LEU   A CD2 
202   N  N   . GLN   A 31  ? 1.5451 1.5266 1.4389 -0.0370 0.0254  0.0331  100  GLN   A N   
203   C  CA  . GLN   A 31  ? 1.5140 1.4892 1.3994 -0.0343 0.0298  0.0327  100  GLN   A CA  
204   C  C   . GLN   A 31  ? 1.5249 1.4933 1.4104 -0.0327 0.0438  0.0361  100  GLN   A C   
205   O  O   . GLN   A 31  ? 1.5836 1.5391 1.4550 -0.0297 0.0491  0.0391  100  GLN   A O   
206   C  CB  . GLN   A 31  ? 1.4407 1.4024 1.3019 -0.0300 0.0240  0.0320  100  GLN   A CB  
207   N  N   . LEU   A 32  ? 1.5361 1.5132 1.4378 -0.0346 0.0498  0.0357  101  LEU   A N   
208   C  CA  . LEU   A 32  ? 1.5958 1.5699 1.5035 -0.0340 0.0634  0.0386  101  LEU   A CA  
209   C  C   . LEU   A 32  ? 1.7140 1.6785 1.6094 -0.0299 0.0700  0.0392  101  LEU   A C   
210   O  O   . LEU   A 32  ? 1.6964 1.6684 1.5999 -0.0307 0.0685  0.0368  101  LEU   A O   
211   C  CB  . LEU   A 32  ? 1.6074 1.5981 1.5432 -0.0388 0.0656  0.0377  101  LEU   A CB  
212   C  CG  . LEU   A 32  ? 1.6447 1.6438 1.5956 -0.0427 0.0638  0.0382  101  LEU   A CG  
213   C  CD1 . LEU   A 32  ? 1.6924 1.6848 1.6454 -0.0423 0.0757  0.0421  101  LEU   A CD1 
214   C  CD2 . LEU   A 32  ? 1.6130 1.6103 1.5536 -0.0427 0.0531  0.0373  101  LEU   A CD2 
215   N  N   . PHE   A 33  ? 1.7678 1.7154 1.6436 -0.0253 0.0777  0.0423  102  PHE   A N   
216   C  CA  . PHE   A 33  ? 1.8423 1.7795 1.7055 -0.0209 0.0850  0.0431  102  PHE   A CA  
217   C  C   . PHE   A 33  ? 1.8874 1.8196 1.7549 -0.0195 0.1008  0.0470  102  PHE   A C   
218   O  O   . PHE   A 33  ? 1.9132 1.8447 1.7826 -0.0177 0.1077  0.0471  102  PHE   A O   
219   C  CB  . PHE   A 33  ? 1.8282 1.7477 1.6612 -0.0154 0.0806  0.0431  102  PHE   A CB  
220   C  CG  . PHE   A 33  ? 1.8676 1.7704 1.6815 -0.0115 0.0860  0.0468  102  PHE   A CG  
221   C  CD1 . PHE   A 33  ? 1.9630 1.8551 1.7715 -0.0084 0.1006  0.0508  102  PHE   A CD1 
222   C  CD2 . PHE   A 33  ? 1.9176 1.8141 1.7174 -0.0104 0.0763  0.0462  102  PHE   A CD2 
223   C  CE1 . PHE   A 33  ? 2.0001 1.8755 1.7894 -0.0044 0.1058  0.0543  102  PHE   A CE1 
224   C  CE2 . PHE   A 33  ? 2.0021 1.8823 1.7829 -0.0064 0.0808  0.0494  102  PHE   A CE2 
225   C  CZ  . PHE   A 33  ? 1.9890 1.8581 1.7638 -0.0033 0.0957  0.0536  102  PHE   A CZ  
226   N  N   . HIS   A 34  ? 1.9204 1.8490 1.7903 -0.0202 0.1073  0.0503  103  HIS   A N   
227   C  CA  . HIS   A 34  ? 1.9750 1.8982 1.8490 -0.0187 0.1230  0.0541  103  HIS   A CA  
228   C  C   . HIS   A 34  ? 1.9745 1.9151 1.8774 -0.0229 0.1264  0.0525  103  HIS   A C   
229   O  O   . HIS   A 34  ? 1.9540 1.9106 1.8771 -0.0280 0.1188  0.0500  103  HIS   A O   
230   C  CB  . HIS   A 34  ? 1.9975 1.9139 1.8708 -0.0191 0.1301  0.0580  103  HIS   A CB  
231   C  CG  . HIS   A 34  ? 1.9711 1.8708 1.8173 -0.0151 0.1264  0.0595  103  HIS   A CG  
232   N  ND1 . HIS   A 34  ? 2.0085 1.9119 1.8538 -0.0172 0.1150  0.0580  103  HIS   A ND1 
233   C  CD2 . HIS   A 34  ? 1.9667 1.8458 1.7863 -0.0088 0.1331  0.0626  103  HIS   A CD2 
234   C  CE1 . HIS   A 34  ? 1.9879 1.8741 1.8078 -0.0125 0.1143  0.0599  103  HIS   A CE1 
235   N  NE2 . HIS   A 34  ? 2.0237 1.8945 1.8269 -0.0073 0.1249  0.0626  103  HIS   A NE2 
236   N  N   . PRO   A 35  ? 2.0522 1.9904 1.9578 -0.0207 0.1373  0.0539  104  PRO   A N   
237   C  CA  . PRO   A 35  ? 2.0398 1.9950 1.9721 -0.0241 0.1387  0.0517  104  PRO   A CA  
238   C  C   . PRO   A 35  ? 2.0014 1.9708 1.9613 -0.0298 0.1401  0.0518  104  PRO   A C   
239   O  O   . PRO   A 35  ? 1.9682 1.9539 1.9483 -0.0339 0.1327  0.0483  104  PRO   A O   
240   C  CB  . PRO   A 35  ? 2.0662 2.0129 1.9938 -0.0199 0.1525  0.0542  104  PRO   A CB  
241   C  CG  . PRO   A 35  ? 2.1005 2.0263 1.9946 -0.0137 0.1535  0.0560  104  PRO   A CG  
242   C  CD  . PRO   A 35  ? 2.0738 1.9934 1.9571 -0.0144 0.1480  0.0572  104  PRO   A CD  
243   N  N   . GLN   A 36  ? 2.0401 2.0027 2.0005 -0.0300 0.1492  0.0556  105  GLN   A N   
244   C  CA  . GLN   A 36  ? 2.0195 1.9944 2.0054 -0.0355 0.1502  0.0557  105  GLN   A CA  
245   C  C   . GLN   A 36  ? 2.0067 1.9935 2.0002 -0.0394 0.1350  0.0519  105  GLN   A C   
246   O  O   . GLN   A 36  ? 1.9831 1.9859 2.0009 -0.0438 0.1310  0.0493  105  GLN   A O   
247   C  CB  . GLN   A 36  ? 2.0469 2.0101 2.0265 -0.0348 0.1600  0.0604  105  GLN   A CB  
248   N  N   . GLU   A 37  ? 1.9134 1.8923 1.8861 -0.0377 0.1262  0.0515  106  GLU   A N   
249   C  CA  . GLU   A 37  ? 1.8681 1.8574 1.8471 -0.0412 0.1123  0.0482  106  GLU   A CA  
250   C  C   . GLU   A 37  ? 1.8182 1.8213 1.8093 -0.0430 0.1039  0.0438  106  GLU   A C   
251   O  O   . GLU   A 37  ? 1.8035 1.8212 1.8154 -0.0472 0.0984  0.0414  106  GLU   A O   
252   C  CB  . GLU   A 37  ? 1.8750 1.8526 1.8287 -0.0384 0.1048  0.0486  106  GLU   A CB  
253   C  CG  . GLU   A 37  ? 1.9349 1.9000 1.8766 -0.0369 0.1100  0.0523  106  GLU   A CG  
254   C  CD  . GLU   A 37  ? 1.9852 1.9343 1.8970 -0.0319 0.1061  0.0530  106  GLU   A CD  
255   O  OE1 . GLU   A 37  ? 1.9702 1.9171 1.8720 -0.0293 0.1027  0.0511  106  GLU   A OE1 
256   O  OE2 . GLU   A 37  ? 2.0105 1.9493 1.9090 -0.0303 0.1061  0.0553  106  GLU   A OE2 
257   N  N   . VAL   A 38  ? 1.8188 1.8171 1.7969 -0.0396 0.1029  0.0427  107  VAL   A N   
258   C  CA  . VAL   A 38  ? 1.7743 1.7844 1.7615 -0.0411 0.0941  0.0385  107  VAL   A CA  
259   C  C   . VAL   A 38  ? 1.7367 1.7617 1.7518 -0.0444 0.0976  0.0372  107  VAL   A C   
260   O  O   . VAL   A 38  ? 1.6724 1.7104 1.7014 -0.0472 0.0891  0.0337  107  VAL   A O   
261   C  CB  . VAL   A 38  ? 1.7672 1.7686 1.7362 -0.0367 0.0941  0.0378  107  VAL   A CB  
262   C  CG1 . VAL   A 38  ? 1.7739 1.7581 1.7147 -0.0327 0.0930  0.0397  107  VAL   A CG1 
263   C  CG2 . VAL   A 38  ? 1.8232 1.8233 1.7986 -0.0348 0.1062  0.0392  107  VAL   A CG2 
264   N  N   . SER   A 39  ? 1.7630 1.7857 1.7867 -0.0439 0.1103  0.0399  108  SER   A N   
265   C  CA  . SER   A 39  ? 1.7490 1.7859 1.8010 -0.0472 0.1136  0.0386  108  SER   A CA  
266   C  C   . SER   A 39  ? 1.6985 1.7472 1.7670 -0.0520 0.1051  0.0366  108  SER   A C   
267   O  O   . SER   A 39  ? 1.6706 1.7322 1.7537 -0.0542 0.0972  0.0329  108  SER   A O   
268   C  CB  . SER   A 39  ? 1.7612 1.7931 1.8202 -0.0464 0.1288  0.0424  108  SER   A CB  
269   O  OG  . SER   A 39  ? 1.8535 1.8690 1.8890 -0.0414 0.1366  0.0455  108  SER   A OG  
270   N  N   . MET   A 40  ? 1.7808 1.8243 1.8459 -0.0532 0.1064  0.0390  109  MET   A N   
271   C  CA  . MET   A 40  ? 1.7633 1.8165 1.8429 -0.0574 0.0990  0.0374  109  MET   A CA  
272   C  C   . MET   A 40  ? 1.7060 1.7675 1.7848 -0.0585 0.0849  0.0334  109  MET   A C   
273   O  O   . MET   A 40  ? 1.6489 1.7235 1.7466 -0.0615 0.0791  0.0304  109  MET   A O   
274   C  CB  . MET   A 40  ? 1.7538 1.7971 1.8222 -0.0575 0.1008  0.0405  109  MET   A CB  
275   C  CG  . MET   A 40  ? 1.7329 1.7848 1.8123 -0.0614 0.0919  0.0388  109  MET   A CG  
276   S  SD  . MET   A 40  ? 1.8688 1.9093 1.9295 -0.0607 0.0890  0.0414  109  MET   A SD  
277   C  CE  . MET   A 40  ? 1.8168 1.8425 1.8461 -0.0553 0.0881  0.0426  109  MET   A CE  
278   N  N   . VAL   A 41  ? 1.6699 1.7232 1.7264 -0.0559 0.0793  0.0333  110  VAL   A N   
279   C  CA  . VAL   A 41  ? 1.5644 1.6242 1.6183 -0.0567 0.0665  0.0300  110  VAL   A CA  
280   C  C   . VAL   A 41  ? 1.5722 1.6441 1.6423 -0.0579 0.0637  0.0266  110  VAL   A C   
281   O  O   . VAL   A 41  ? 1.5307 1.6134 1.6124 -0.0603 0.0552  0.0237  110  VAL   A O   
282   C  CB  . VAL   A 41  ? 1.5400 1.5887 1.5687 -0.0533 0.0628  0.0303  110  VAL   A CB  
283   C  CG1 . VAL   A 41  ? 1.4969 1.5510 1.5228 -0.0546 0.0500  0.0276  110  VAL   A CG1 
284   C  CG2 . VAL   A 41  ? 1.5765 1.6105 1.5877 -0.0508 0.0688  0.0341  110  VAL   A CG2 
285   N  N   . ARG   A 42  ? 1.5476 1.6172 1.6178 -0.0557 0.0711  0.0270  111  ARG   A N   
286   C  CA  . ARG   A 42  ? 1.5021 1.5821 1.5873 -0.0561 0.0699  0.0241  111  ARG   A CA  
287   C  C   . ARG   A 42  ? 1.5124 1.6055 1.6234 -0.0598 0.0686  0.0224  111  ARG   A C   
288   O  O   . ARG   A 42  ? 1.5135 1.6167 1.6339 -0.0614 0.0595  0.0190  111  ARG   A O   
289   C  CB  . ARG   A 42  ? 1.4881 1.5627 1.5708 -0.0531 0.0804  0.0256  111  ARG   A CB  
290   N  N   . ASN   A 43  ? 1.5133 1.6060 1.6358 -0.0609 0.0776  0.0246  112  ASN   A N   
291   C  CA  . ASN   A 43  ? 1.4978 1.6020 1.6450 -0.0645 0.0765  0.0231  112  ASN   A CA  
292   C  C   . ASN   A 43  ? 1.4231 1.5321 1.5714 -0.0669 0.0654  0.0212  112  ASN   A C   
293   O  O   . ASN   A 43  ? 1.4121 1.5322 1.5752 -0.0686 0.0582  0.0178  112  ASN   A O   
294   C  CB  . ASN   A 43  ? 1.5689 1.6690 1.7244 -0.0655 0.0878  0.0265  112  ASN   A CB  
295   C  CG  . ASN   A 43  ? 1.6615 1.7544 1.8128 -0.0627 0.1002  0.0292  112  ASN   A CG  
296   O  OD1 . ASN   A 43  ? 1.6785 1.7601 1.8076 -0.0592 0.1028  0.0311  112  ASN   A OD1 
297   N  ND2 . ASN   A 43  ? 1.6732 1.7724 1.8459 -0.0639 0.1079  0.0293  112  ASN   A ND2 
298   N  N   . LEU   A 44  ? 1.4269 1.5275 1.5597 -0.0667 0.0642  0.0235  113  LEU   A N   
299   C  CA  . LEU   A 44  ? 1.4330 1.5374 1.5658 -0.0687 0.0543  0.0221  113  LEU   A CA  
300   C  C   . LEU   A 44  ? 1.4373 1.5495 1.5708 -0.0687 0.0437  0.0184  113  LEU   A C   
301   O  O   . LEU   A 44  ? 1.4066 1.5282 1.5534 -0.0707 0.0369  0.0158  113  LEU   A O   
302   C  CB  . LEU   A 44  ? 1.4495 1.5425 1.5611 -0.0674 0.0537  0.0248  113  LEU   A CB  
303   C  CG  . LEU   A 44  ? 1.4501 1.5357 1.5614 -0.0680 0.0621  0.0284  113  LEU   A CG  
304   C  CD1 . LEU   A 44  ? 1.4120 1.4893 1.5053 -0.0672 0.0578  0.0301  113  LEU   A CD1 
305   C  CD2 . LEU   A 44  ? 1.4828 1.5777 1.6183 -0.0716 0.0632  0.0274  113  LEU   A CD2 
306   N  N   . ILE   A 45  ? 1.4735 1.5810 1.5917 -0.0661 0.0422  0.0181  114  ILE   A N   
307   C  CA  . ILE   A 45  ? 1.4414 1.5542 1.5568 -0.0659 0.0323  0.0151  114  ILE   A CA  
308   C  C   . ILE   A 45  ? 1.4036 1.5275 1.5373 -0.0666 0.0304  0.0119  114  ILE   A C   
309   O  O   . ILE   A 45  ? 1.3050 1.4358 1.4426 -0.0673 0.0218  0.0091  114  ILE   A O   
310   C  CB  . ILE   A 45  ? 1.3997 1.5037 1.4945 -0.0630 0.0321  0.0157  114  ILE   A CB  
311   C  CG1 . ILE   A 45  ? 1.4240 1.5310 1.5121 -0.0633 0.0212  0.0135  114  ILE   A CG1 
312   C  CG2 . ILE   A 45  ? 1.3798 1.4835 1.4773 -0.0611 0.0385  0.0154  114  ILE   A CG2 
313   C  CD1 . ILE   A 45  ? 1.3603 1.4692 1.4490 -0.0652 0.0153  0.0138  114  ILE   A CD1 
314   N  N   . GLN   A 46  ? 1.3883 1.5137 1.5332 -0.0663 0.0386  0.0123  115  GLN   A N   
315   C  CA  . GLN   A 46  ? 1.3626 1.4988 1.5273 -0.0669 0.0372  0.0092  115  GLN   A CA  
316   C  C   . GLN   A 46  ? 1.3678 1.5120 1.5506 -0.0698 0.0336  0.0078  115  GLN   A C   
317   O  O   . GLN   A 46  ? 1.3001 1.4535 1.4967 -0.0703 0.0281  0.0044  115  GLN   A O   
318   C  CB  . GLN   A 46  ? 1.4010 1.5363 1.5731 -0.0656 0.0475  0.0102  115  GLN   A CB  
319   C  CG  . GLN   A 46  ? 1.4724 1.6003 1.6280 -0.0623 0.0508  0.0111  115  GLN   A CG  
320   C  CD  . GLN   A 46  ? 1.5730 1.7076 1.7393 -0.0608 0.0512  0.0084  115  GLN   A CD  
321   O  OE1 . GLN   A 46  ? 1.4786 1.6193 1.6473 -0.0607 0.0428  0.0052  115  GLN   A OE1 
322   N  NE2 . GLN   A 46  ? 1.6004 1.7336 1.7733 -0.0595 0.0614  0.0099  115  GLN   A NE2 
323   N  N   . LYS   A 47  ? 1.4186 1.5589 1.6010 -0.0715 0.0365  0.0102  116  LYS   A N   
324   C  CA  . LYS   A 47  ? 1.3856 1.5323 1.5851 -0.0743 0.0339  0.0091  116  LYS   A CA  
325   C  C   . LYS   A 47  ? 1.3899 1.5360 1.5814 -0.0753 0.0254  0.0088  116  LYS   A C   
326   O  O   . LYS   A 47  ? 1.4078 1.5573 1.5944 -0.0746 0.0169  0.0065  116  LYS   A O   
327   C  CB  . LYS   A 47  ? 1.3398 1.4831 1.5477 -0.0757 0.0441  0.0120  116  LYS   A CB  
328   C  CG  . LYS   A 47  ? 1.3219 1.4627 1.5320 -0.0740 0.0543  0.0134  116  LYS   A CG  
329   C  CD  . LYS   A 47  ? 1.3293 1.4739 1.5610 -0.0761 0.0621  0.0140  116  LYS   A CD  
330   C  CE  . LYS   A 47  ? 1.3902 1.5330 1.6252 -0.0742 0.0727  0.0155  116  LYS   A CE  
331   N  NZ  . LYS   A 47  ? 1.3798 1.5325 1.6295 -0.0733 0.0701  0.0118  116  LYS   A NZ  
332   N  N   . ASP   A 48  ? 1.4787 1.6202 1.6687 -0.0768 0.0280  0.0112  117  ASP   A N   
333   C  CA  . ASP   A 48  ? 1.4635 1.6044 1.6473 -0.0777 0.0206  0.0111  117  ASP   A CA  
334   C  C   . ASP   A 48  ? 1.4376 1.5707 1.5986 -0.0759 0.0180  0.0129  117  ASP   A C   
335   O  O   . ASP   A 48  ? 1.4103 1.5445 1.5660 -0.0762 0.0104  0.0122  117  ASP   A O   
336   C  CB  . ASP   A 48  ? 1.4712 1.6096 1.6619 -0.0799 0.0243  0.0130  117  ASP   A CB  
337   C  CG  . ASP   A 48  ? 1.5249 1.6520 1.7030 -0.0792 0.0338  0.0174  117  ASP   A CG  
338   O  OD1 . ASP   A 48  ? 1.5570 1.6765 1.7167 -0.0779 0.0319  0.0193  117  ASP   A OD1 
339   O  OD2 . ASP   A 48  ? 1.5080 1.6335 1.6948 -0.0796 0.0431  0.0189  117  ASP   A OD2 
340   N  N   . ARG   A 49  ? 1.4045 1.5296 1.5523 -0.0740 0.0242  0.0152  118  ARG   A N   
341   C  CA  . ARG   A 49  ? 1.3696 1.4865 1.4956 -0.0720 0.0217  0.0166  118  ARG   A CA  
342   C  C   . ARG   A 49  ? 1.3180 1.4287 1.4351 -0.0724 0.0209  0.0190  118  ARG   A C   
343   O  O   . ARG   A 49  ? 1.2619 1.3682 1.3638 -0.0712 0.0159  0.0194  118  ARG   A O   
344   C  CB  . ARG   A 49  ? 1.3577 1.4795 1.4792 -0.0714 0.0122  0.0139  118  ARG   A CB  
345   C  CG  . ARG   A 49  ? 1.3422 1.4739 1.4787 -0.0718 0.0095  0.0106  118  ARG   A CG  
346   C  CD  . ARG   A 49  ? 1.3183 1.4524 1.4473 -0.0708 0.0017  0.0085  118  ARG   A CD  
347   N  NE  . ARG   A 49  ? 1.2185 1.3542 1.3432 -0.0715 -0.0062 0.0080  118  ARG   A NE  
348   C  CZ  . ARG   A 49  ? 1.2642 1.4076 1.4000 -0.0726 -0.0121 0.0058  118  ARG   A CZ  
349   N  NH1 . ARG   A 49  ? 1.3102 1.4603 1.4626 -0.0733 -0.0113 0.0038  118  ARG   A NH1 
350   N  NH2 . ARG   A 49  ? 1.2300 1.3741 1.3601 -0.0728 -0.0189 0.0056  118  ARG   A NH2 
351   N  N   . THR   A 50  ? 1.3758 1.4861 1.5028 -0.0742 0.0257  0.0204  119  THR   A N   
352   C  CA  . THR   A 50  ? 1.2559 1.3601 1.3756 -0.0746 0.0254  0.0226  119  THR   A CA  
353   C  C   . THR   A 50  ? 1.2931 1.3878 1.4092 -0.0741 0.0364  0.0263  119  THR   A C   
354   O  O   . THR   A 50  ? 1.3403 1.4376 1.4712 -0.0756 0.0433  0.0265  119  THR   A O   
355   C  CB  . THR   A 50  ? 1.2124 1.3239 1.3466 -0.0771 0.0204  0.0211  119  THR   A CB  
356   O  OG1 . THR   A 50  ? 1.2603 1.3805 1.3986 -0.0773 0.0108  0.0177  119  THR   A OG1 
357   C  CG2 . THR   A 50  ? 1.1745 1.2791 1.2986 -0.0771 0.0194  0.0234  119  THR   A CG2 
358   N  N   . PHE   A 51  ? 1.2687 1.3521 1.3653 -0.0720 0.0381  0.0290  120  PHE   A N   
359   C  CA  . PHE   A 51  ? 1.2327 1.3053 1.3230 -0.0712 0.0483  0.0329  120  PHE   A CA  
360   C  C   . PHE   A 51  ? 1.1806 1.2480 1.2647 -0.0717 0.0461  0.0346  120  PHE   A C   
361   O  O   . PHE   A 51  ? 1.1460 1.2187 1.2315 -0.0726 0.0369  0.0328  120  PHE   A O   
362   C  CB  . PHE   A 51  ? 1.2885 1.3499 1.3592 -0.0675 0.0534  0.0349  120  PHE   A CB  
363   C  CG  . PHE   A 51  ? 1.2526 1.3090 1.3033 -0.0650 0.0453  0.0344  120  PHE   A CG  
364   C  CD1 . PHE   A 51  ? 1.1695 1.2330 1.2199 -0.0649 0.0369  0.0313  120  PHE   A CD1 
365   C  CD2 . PHE   A 51  ? 1.2210 1.2655 1.2537 -0.0629 0.0460  0.0371  120  PHE   A CD2 
366   C  CE1 . PHE   A 51  ? 1.1279 1.1871 1.1616 -0.0629 0.0295  0.0308  120  PHE   A CE1 
367   C  CE2 . PHE   A 51  ? 1.2729 1.3131 1.2885 -0.0606 0.0382  0.0364  120  PHE   A CE2 
368   C  CZ  . PHE   A 51  ? 1.1845 1.2323 1.2011 -0.0607 0.0298  0.0332  120  PHE   A CZ  
369   N  N   . ALA   A 52  ? 1.2337 1.2900 1.3105 -0.0708 0.0551  0.0383  121  ALA   A N   
370   C  CA  . ALA   A 52  ? 1.1968 1.2471 1.2691 -0.0712 0.0550  0.0404  121  ALA   A CA  
371   C  C   . ALA   A 52  ? 1.1863 1.2224 1.2330 -0.0673 0.0560  0.0431  121  ALA   A C   
372   O  O   . ALA   A 52  ? 1.2837 1.3099 1.3193 -0.0648 0.0642  0.0456  121  ALA   A O   
373   C  CB  . ALA   A 52  ? 1.1941 1.2430 1.2806 -0.0736 0.0647  0.0425  121  ALA   A CB  
374   N  N   . VAL   A 53  ? 1.1606 1.1955 1.1977 -0.0665 0.0475  0.0427  122  VAL   A N   
375   C  CA  . VAL   A 53  ? 1.2434 1.2648 1.2569 -0.0627 0.0472  0.0451  122  VAL   A CA  
376   C  C   . VAL   A 53  ? 1.3239 1.3385 1.3361 -0.0632 0.0504  0.0477  122  VAL   A C   
377   O  O   . VAL   A 53  ? 1.3021 1.3230 1.3225 -0.0652 0.0442  0.0465  122  VAL   A O   
378   C  CB  . VAL   A 53  ? 1.2004 1.2249 1.2040 -0.0611 0.0352  0.0427  122  VAL   A CB  
379   C  CG1 . VAL   A 53  ? 1.2975 1.3087 1.2785 -0.0574 0.0337  0.0448  122  VAL   A CG1 
380   C  CG2 . VAL   A 53  ? 1.1876 1.2159 1.1895 -0.0603 0.0333  0.0405  122  VAL   A CG2 
381   N  N   . LEU   A 54  ? 1.3820 1.3833 1.3834 -0.0611 0.0604  0.0515  123  LEU   A N   
382   C  CA  . LEU   A 54  ? 1.4745 1.4676 1.4743 -0.0615 0.0656  0.0545  123  LEU   A CA  
383   C  C   . LEU   A 54  ? 1.5898 1.5726 1.5679 -0.0579 0.0601  0.0557  123  LEU   A C   
384   O  O   . LEU   A 54  ? 1.6385 1.6162 1.5993 -0.0543 0.0555  0.0552  123  LEU   A O   
385   C  CB  . LEU   A 54  ? 1.4750 1.4580 1.4736 -0.0609 0.0799  0.0582  123  LEU   A CB  
386   C  CG  . LEU   A 54  ? 1.3455 1.3391 1.3697 -0.0652 0.0861  0.0573  123  LEU   A CG  
387   C  CD1 . LEU   A 54  ? 1.2225 1.2069 1.2474 -0.0647 0.1011  0.0611  123  LEU   A CD1 
388   C  CD2 . LEU   A 54  ? 1.3229 1.3253 1.3654 -0.0694 0.0819  0.0559  123  LEU   A CD2 
389   N  N   . ALA   A 55  ? 1.6663 1.6457 1.6457 -0.0588 0.0604  0.0572  124  ALA   A N   
390   C  CA  . ALA   A 55  ? 1.7217 1.6917 1.6827 -0.0555 0.0552  0.0584  124  ALA   A CA  
391   C  C   . ALA   A 55  ? 1.7729 1.7238 1.7135 -0.0515 0.0641  0.0628  124  ALA   A C   
392   O  O   . ALA   A 55  ? 1.7669 1.7082 1.6874 -0.0474 0.0594  0.0635  124  ALA   A O   
393   C  CB  . ALA   A 55  ? 1.6457 1.6222 1.6183 -0.0583 0.0499  0.0576  124  ALA   A CB  
394   N  N   . TYR   A 56  ? 1.8045 1.7492 1.7494 -0.0525 0.0768  0.0657  125  TYR   A N   
395   C  CA  . TYR   A 56  ? 1.7991 1.7245 1.7232 -0.0482 0.0863  0.0701  125  TYR   A CA  
396   C  C   . TYR   A 56  ? 1.8497 1.7636 1.7589 -0.0457 0.0845  0.0723  125  TYR   A C   
397   O  O   . TYR   A 56  ? 1.8958 1.7988 1.8023 -0.0455 0.0942  0.0760  125  TYR   A O   
398   C  CB  . TYR   A 56  ? 1.8333 1.7512 1.7376 -0.0434 0.0853  0.0698  125  TYR   A CB  
399   C  CG  . TYR   A 56  ? 1.8805 1.8058 1.7957 -0.0449 0.0899  0.0686  125  TYR   A CG  
400   C  CD1 . TYR   A 56  ? 1.8751 1.8052 1.8099 -0.0486 0.1002  0.0698  125  TYR   A CD1 
401   C  CD2 . TYR   A 56  ? 1.9163 1.8438 1.8229 -0.0426 0.0837  0.0661  125  TYR   A CD2 
402   C  CE1 . TYR   A 56  ? 1.8820 1.8192 1.8273 -0.0498 0.1043  0.0686  125  TYR   A CE1 
403   C  CE2 . TYR   A 56  ? 1.9306 1.8646 1.8468 -0.0437 0.0878  0.0649  125  TYR   A CE2 
404   C  CZ  . TYR   A 56  ? 1.9276 1.8664 1.8629 -0.0472 0.0981  0.0662  125  TYR   A CZ  
405   O  OH  . TYR   A 56  ? 1.9522 1.8976 1.8971 -0.0480 0.1020  0.0650  125  TYR   A OH  
406   N  N   . ALA   A 64  ? 1.8181 1.7364 1.7681 -0.0551 0.1057  0.0762  133  ALA   A N   
407   C  CA  . ALA   A 64  ? 1.8308 1.7653 1.7999 -0.0593 0.0952  0.0724  133  ALA   A CA  
408   C  C   . ALA   A 64  ? 1.7602 1.7110 1.7572 -0.0645 0.0963  0.0697  133  ALA   A C   
409   O  O   . ALA   A 64  ? 1.7410 1.6948 1.7419 -0.0645 0.1008  0.0693  133  ALA   A O   
410   C  CB  . ALA   A 64  ? 1.8428 1.7827 1.8014 -0.0568 0.0811  0.0692  133  ALA   A CB  
411   N  N   . GLN   A 65  ? 1.6220 1.5828 1.6376 -0.0687 0.0915  0.0677  134  GLN   A N   
412   C  CA  . GLN   A 65  ? 1.5006 1.4761 1.5435 -0.0737 0.0918  0.0650  134  GLN   A CA  
413   C  C   . GLN   A 65  ? 1.4804 1.4714 1.5329 -0.0751 0.0783  0.0601  134  GLN   A C   
414   O  O   . GLN   A 65  ? 1.4138 1.4166 1.4884 -0.0792 0.0758  0.0574  134  GLN   A O   
415   C  CB  . GLN   A 65  ? 1.4894 1.4637 1.5483 -0.0777 0.0979  0.0665  134  GLN   A CB  
416   C  CG  . GLN   A 65  ? 1.5726 1.5391 1.6217 -0.0769 0.0943  0.0678  134  GLN   A CG  
417   C  CD  . GLN   A 65  ? 1.5682 1.5164 1.6030 -0.0749 0.1059  0.0732  134  GLN   A CD  
418   O  OE1 . GLN   A 65  ? 1.5608 1.4989 1.5813 -0.0717 0.1139  0.0760  134  GLN   A OE1 
419   N  NE2 . GLN   A 65  ? 1.5209 1.4643 1.5590 -0.0766 0.1069  0.0746  134  GLN   A NE2 
420   N  N   . PHE   A 66  ? 1.5534 1.5444 1.5898 -0.0717 0.0695  0.0587  135  PHE   A N   
421   C  CA  . PHE   A 66  ? 1.5056 1.5104 1.5493 -0.0726 0.0571  0.0544  135  PHE   A CA  
422   C  C   . PHE   A 66  ? 1.4958 1.5035 1.5307 -0.0702 0.0537  0.0528  135  PHE   A C   
423   O  O   . PHE   A 66  ? 1.5440 1.5421 1.5648 -0.0673 0.0598  0.0550  135  PHE   A O   
424   C  CB  . PHE   A 66  ? 1.5229 1.5266 1.5582 -0.0713 0.0480  0.0539  135  PHE   A CB  
425   C  CG  . PHE   A 66  ? 1.4981 1.5025 1.5456 -0.0743 0.0486  0.0542  135  PHE   A CG  
426   C  CD1 . PHE   A 66  ? 1.4911 1.4920 1.5504 -0.0771 0.0587  0.0561  135  PHE   A CD1 
427   C  CD2 . PHE   A 66  ? 1.4770 1.4853 1.5244 -0.0741 0.0390  0.0525  135  PHE   A CD2 
428   C  CE1 . PHE   A 66  ? 1.5201 1.5213 1.5909 -0.0799 0.0588  0.0562  135  PHE   A CE1 
429   C  CE2 . PHE   A 66  ? 1.4545 1.4628 1.5123 -0.0766 0.0392  0.0526  135  PHE   A CE2 
430   C  CZ  . PHE   A 66  ? 1.5212 1.5260 1.5908 -0.0796 0.0489  0.0544  135  PHE   A CZ  
431   N  N   . GLY   A 67  ? 1.4138 1.4342 1.4565 -0.0712 0.0438  0.0490  136  GLY   A N   
432   C  CA  . GLY   A 67  ? 1.3602 1.3840 1.3963 -0.0693 0.0401  0.0472  136  GLY   A CA  
433   C  C   . GLY   A 67  ? 1.2103 1.2491 1.2594 -0.0712 0.0303  0.0430  136  GLY   A C   
434   O  O   . GLY   A 67  ? 1.1345 1.1804 1.1957 -0.0734 0.0256  0.0414  136  GLY   A O   
435   N  N   . THR   A 68  ? 1.2042 1.2471 1.2499 -0.0700 0.0274  0.0412  137  THR   A N   
436   C  CA  . THR   A 68  ? 1.1390 1.1953 1.1959 -0.0715 0.0189  0.0374  137  THR   A CA  
437   C  C   . THR   A 68  ? 1.1101 1.1716 1.1744 -0.0721 0.0220  0.0359  137  THR   A C   
438   O  O   . THR   A 68  ? 1.0692 1.1234 1.1236 -0.0702 0.0281  0.0376  137  THR   A O   
439   C  CB  . THR   A 68  ? 1.0689 1.1260 1.1133 -0.0692 0.0093  0.0362  137  THR   A CB  
440   O  OG1 . THR   A 68  ? 1.1312 1.1825 1.1674 -0.0681 0.0068  0.0378  137  THR   A OG1 
441   C  CG2 . THR   A 68  ? 1.0674 1.1379 1.1244 -0.0709 0.0012  0.0326  137  THR   A CG2 
442   N  N   . THR   A 69  ? 1.0812 1.1548 1.1627 -0.0745 0.0179  0.0328  138  THR   A N   
443   C  CA  . THR   A 69  ? 1.0546 1.1347 1.1436 -0.0749 0.0189  0.0308  138  THR   A CA  
444   C  C   . THR   A 69  ? 1.0740 1.1551 1.1507 -0.0727 0.0121  0.0294  138  THR   A C   
445   O  O   . THR   A 69  ? 1.0752 1.1584 1.1468 -0.0721 0.0040  0.0285  138  THR   A O   
446   C  CB  . THR   A 69  ? 1.0483 1.1404 1.1587 -0.0778 0.0156  0.0277  138  THR   A CB  
447   O  OG1 . THR   A 69  ? 1.0371 1.1360 1.1469 -0.0775 0.0052  0.0253  138  THR   A OG1 
448   C  CG2 . THR   A 69  ? 1.0720 1.1629 1.1927 -0.0799 0.0190  0.0288  138  THR   A CG2 
449   N  N   . ALA   A 70  ? 1.0709 1.1503 1.1432 -0.0715 0.0156  0.0293  139  ALA   A N   
450   C  CA  . ALA   A 70  ? 1.0906 1.1710 1.1524 -0.0697 0.0094  0.0278  139  ALA   A CA  
451   C  C   . ALA   A 70  ? 1.1262 1.2148 1.1987 -0.0705 0.0093  0.0252  139  ALA   A C   
452   O  O   . ALA   A 70  ? 1.1525 1.2391 1.2284 -0.0703 0.0169  0.0259  139  ALA   A O   
453   C  CB  . ALA   A 70  ? 1.1006 1.1685 1.1416 -0.0665 0.0124  0.0301  139  ALA   A CB  
454   N  N   . GLU   A 71  ? 1.1319 1.2292 1.2091 -0.0711 0.0008  0.0224  140  GLU   A N   
455   C  CA  . GLU   A 71  ? 1.1410 1.2465 1.2279 -0.0716 -0.0008 0.0196  140  GLU   A CA  
456   C  C   . GLU   A 71  ? 1.0816 1.1842 1.1554 -0.0697 -0.0035 0.0190  140  GLU   A C   
457   O  O   . GLU   A 71  ? 1.0853 1.1853 1.1476 -0.0687 -0.0092 0.0192  140  GLU   A O   
458   C  CB  . GLU   A 71  ? 1.0821 1.1981 1.1818 -0.0733 -0.0082 0.0169  140  GLU   A CB  
459   C  CG  . GLU   A 71  ? 1.1015 1.2253 1.2100 -0.0735 -0.0107 0.0141  140  GLU   A CG  
460   C  CD  . GLU   A 71  ? 1.1515 1.2816 1.2606 -0.0735 -0.0199 0.0119  140  GLU   A CD  
461   O  OE1 . GLU   A 71  ? 1.0222 1.1542 1.1341 -0.0742 -0.0236 0.0120  140  GLU   A OE1 
462   O  OE2 . GLU   A 71  ? 1.2844 1.4170 1.3907 -0.0728 -0.0230 0.0103  140  GLU   A OE2 
463   N  N   . ILE   A 72  ? 1.1280 1.2313 1.2041 -0.0691 0.0004  0.0183  141  ILE   A N   
464   C  CA  . ILE   A 72  ? 1.2061 1.3051 1.2690 -0.0671 -0.0011 0.0178  141  ILE   A CA  
465   C  C   . ILE   A 72  ? 1.1655 1.2730 1.2330 -0.0677 -0.0091 0.0148  141  ILE   A C   
466   O  O   . ILE   A 72  ? 1.1396 1.2558 1.2217 -0.0690 -0.0102 0.0128  141  ILE   A O   
467   C  CB  . ILE   A 72  ? 1.2282 1.3228 1.2898 -0.0658 0.0074  0.0186  141  ILE   A CB  
468   C  CG1 . ILE   A 72  ? 1.2344 1.3227 1.2972 -0.0657 0.0167  0.0216  141  ILE   A CG1 
469   C  CG2 . ILE   A 72  ? 1.2412 1.3275 1.2845 -0.0631 0.0063  0.0189  141  ILE   A CG2 
470   C  CD1 . ILE   A 72  ? 1.3253 1.4142 1.3973 -0.0655 0.0258  0.0219  141  ILE   A CD1 
471   N  N   . TYR   A 73  ? 1.0997 1.2044 1.1548 -0.0667 -0.0150 0.0145  142  TYR   A N   
472   C  CA  . TYR   A 73  ? 1.1596 1.2712 1.2178 -0.0672 -0.0222 0.0120  142  TYR   A CA  
473   C  C   . TYR   A 73  ? 1.2456 1.3523 1.2917 -0.0657 -0.0235 0.0114  142  TYR   A C   
474   O  O   . TYR   A 73  ? 1.2511 1.3612 1.2959 -0.0660 -0.0299 0.0097  142  TYR   A O   
475   C  CB  . TYR   A 73  ? 1.1670 1.2821 1.2254 -0.0681 -0.0295 0.0117  142  TYR   A CB  
476   C  CG  . TYR   A 73  ? 1.1915 1.2988 1.2352 -0.0669 -0.0316 0.0134  142  TYR   A CG  
477   C  CD1 . TYR   A 73  ? 1.1834 1.2871 1.2156 -0.0658 -0.0362 0.0129  142  TYR   A CD1 
478   C  CD2 . TYR   A 73  ? 1.1179 1.2213 1.1595 -0.0668 -0.0297 0.0155  142  TYR   A CD2 
479   C  CE1 . TYR   A 73  ? 1.1794 1.2760 1.1988 -0.0645 -0.0389 0.0141  142  TYR   A CE1 
480   C  CE2 . TYR   A 73  ? 1.1399 1.2360 1.1679 -0.0653 -0.0321 0.0169  142  TYR   A CE2 
481   C  CZ  . TYR   A 73  ? 1.1835 1.2764 1.2007 -0.0641 -0.0369 0.0162  142  TYR   A CZ  
482   O  OH  . TYR   A 73  ? 1.2266 1.3120 1.2307 -0.0624 -0.0398 0.0174  142  TYR   A OH  
483   N  N   . ALA   A 74  ? 1.2731 1.3714 1.3103 -0.0639 -0.0172 0.0127  143  ALA   A N   
484   C  CA  . ALA   A 74  ? 1.1898 1.2812 1.2132 -0.0621 -0.0183 0.0123  143  ALA   A CA  
485   C  C   . ALA   A 74  ? 1.3300 1.4123 1.3455 -0.0598 -0.0096 0.0140  143  ALA   A C   
486   O  O   . ALA   A 74  ? 1.3366 1.4104 1.3429 -0.0585 -0.0057 0.0164  143  ALA   A O   
487   C  CB  . ALA   A 74  ? 1.2053 1.2919 1.2160 -0.0615 -0.0249 0.0126  143  ALA   A CB  
488   N  N   . TYR   A 75  ? 1.3677 1.4513 1.3863 -0.0592 -0.0064 0.0128  144  TYR   A N   
489   C  CA  . TYR   A 75  ? 1.3541 1.4309 1.3687 -0.0571 0.0028  0.0143  144  TYR   A CA  
490   C  C   . TYR   A 75  ? 1.4613 1.5331 1.4652 -0.0550 0.0019  0.0130  144  TYR   A C   
491   O  O   . TYR   A 75  ? 1.4765 1.5552 1.4882 -0.0557 -0.0007 0.0107  144  TYR   A O   
492   C  CB  . TYR   A 75  ? 1.3488 1.4339 1.3823 -0.0585 0.0086  0.0140  144  TYR   A CB  
493   C  CG  . TYR   A 75  ? 1.4372 1.5170 1.4707 -0.0566 0.0192  0.0157  144  TYR   A CG  
494   C  CD1 . TYR   A 75  ? 1.4546 1.5296 1.4803 -0.0541 0.0221  0.0152  144  TYR   A CD1 
495   C  CD2 . TYR   A 75  ? 1.4621 1.5421 1.5047 -0.0574 0.0266  0.0177  144  TYR   A CD2 
496   C  CE1 . TYR   A 75  ? 1.4953 1.5655 1.5213 -0.0522 0.0325  0.0168  144  TYR   A CE1 
497   C  CE2 . TYR   A 75  ? 1.4923 1.5677 1.5361 -0.0558 0.0371  0.0195  144  TYR   A CE2 
498   C  CZ  . TYR   A 75  ? 1.4972 1.5679 1.5328 -0.0530 0.0401  0.0191  144  TYR   A CZ  
499   O  OH  . TYR   A 75  ? 1.5055 1.5718 1.5427 -0.0512 0.0511  0.0210  144  TYR   A OH  
500   N  N   . ARG   A 76  ? 1.5851 1.6442 1.5706 -0.0521 0.0041  0.0144  145  ARG   A N   
501   C  CA  . ARG   A 76  ? 1.6085 1.6605 1.5810 -0.0497 0.0032  0.0134  145  ARG   A CA  
502   C  C   . ARG   A 76  ? 1.6584 1.6988 1.6196 -0.0463 0.0128  0.0156  145  ARG   A C   
503   O  O   . ARG   A 76  ? 1.6587 1.6895 1.6080 -0.0445 0.0154  0.0179  145  ARG   A O   
504   C  CB  . ARG   A 76  ? 1.6102 1.6570 1.5686 -0.0493 -0.0059 0.0124  145  ARG   A CB  
505   C  CG  . ARG   A 76  ? 1.6247 1.6639 1.5699 -0.0470 -0.0078 0.0110  145  ARG   A CG  
506   C  CD  . ARG   A 76  ? 1.7038 1.7377 1.6362 -0.0468 -0.0172 0.0098  145  ARG   A CD  
507   N  NE  . ARG   A 76  ? 1.7161 1.7597 1.6586 -0.0500 -0.0248 0.0089  145  ARG   A NE  
508   C  CZ  . ARG   A 76  ? 1.6525 1.6940 1.5904 -0.0502 -0.0289 0.0098  145  ARG   A CZ  
509   N  NH1 . ARG   A 76  ? 1.6743 1.7039 1.5970 -0.0473 -0.0266 0.0115  145  ARG   A NH1 
510   N  NH2 . ARG   A 76  ? 1.5795 1.6306 1.5277 -0.0531 -0.0353 0.0090  145  ARG   A NH2 
511   N  N   . GLU   A 77  ? 1.6293 1.6702 1.5936 -0.0449 0.0180  0.0150  146  GLU   A N   
512   C  CA  . GLU   A 77  ? 1.6322 1.6620 1.5859 -0.0412 0.0277  0.0170  146  GLU   A CA  
513   C  C   . GLU   A 77  ? 1.6779 1.6966 1.6116 -0.0380 0.0246  0.0160  146  GLU   A C   
514   O  O   . GLU   A 77  ? 1.6573 1.6800 1.5931 -0.0384 0.0201  0.0135  146  GLU   A O   
515   C  CB  . GLU   A 77  ? 1.6012 1.6383 1.5714 -0.0415 0.0359  0.0171  146  GLU   A CB  
516   C  CG  . GLU   A 77  ? 1.5797 1.6195 1.5621 -0.0426 0.0443  0.0196  146  GLU   A CG  
517   C  CD  . GLU   A 77  ? 1.5767 1.6259 1.5793 -0.0435 0.0514  0.0193  146  GLU   A CD  
518   O  OE1 . GLU   A 77  ? 1.5695 1.6299 1.5913 -0.0467 0.0506  0.0187  146  GLU   A OE1 
519   O  OE2 . GLU   A 77  ? 1.6045 1.6496 1.6038 -0.0407 0.0577  0.0195  146  GLU   A OE2 
520   N  N   . GLU   A 78  ? 1.6788 1.6831 1.5927 -0.0347 0.0267  0.0179  147  GLU   A N   
521   C  CA  . GLU   A 78  ? 1.6852 1.6773 1.5783 -0.0313 0.0229  0.0168  147  GLU   A CA  
522   C  C   . GLU   A 78  ? 1.7658 1.7464 1.6472 -0.0267 0.0327  0.0183  147  GLU   A C   
523   O  O   . GLU   A 78  ? 1.7656 1.7430 1.6487 -0.0253 0.0431  0.0211  147  GLU   A O   
524   C  CB  . GLU   A 78  ? 1.7023 1.6844 1.5785 -0.0300 0.0170  0.0174  147  GLU   A CB  
525   C  CG  . GLU   A 78  ? 1.7837 1.7720 1.6622 -0.0329 0.0042  0.0147  147  GLU   A CG  
526   C  CD  . GLU   A 78  ? 1.9399 1.9149 1.7967 -0.0301 -0.0026 0.0141  147  GLU   A CD  
527   O  OE1 . GLU   A 78  ? 1.8896 1.8526 1.7301 -0.0263 -0.0011 0.0137  147  GLU   A OE1 
528   O  OE2 . GLU   A 78  ? 2.0174 1.9938 1.8734 -0.0314 -0.0097 0.0139  147  GLU   A OE2 
529   N  N   . ILE   A 85  ? 1.8171 1.7817 1.6977 -0.0231 0.0639  0.0298  154  ILE   A N   
530   C  CA  . ILE   A 85  ? 1.8335 1.8025 1.7206 -0.0261 0.0607  0.0308  154  ILE   A CA  
531   C  C   . ILE   A 85  ? 1.7902 1.7770 1.6983 -0.0315 0.0518  0.0280  154  ILE   A C   
532   O  O   . ILE   A 85  ? 1.7695 1.7622 1.6801 -0.0325 0.0444  0.0249  154  ILE   A O   
533   C  CB  . ILE   A 85  ? 1.8478 1.8036 1.7121 -0.0234 0.0545  0.0313  154  ILE   A CB  
534   C  CG1 . ILE   A 85  ? 1.8422 1.8067 1.7106 -0.0267 0.0404  0.0283  154  ILE   A CG1 
535   C  CG2 . ILE   A 85  ? 1.9103 1.8496 1.7503 -0.0178 0.0561  0.0314  154  ILE   A CG2 
536   C  CD1 . ILE   A 85  ? 1.8156 1.7806 1.6843 -0.0282 0.0364  0.0294  154  ILE   A CD1 
537   N  N   . VAL   A 86  ? 1.7343 1.7289 1.6566 -0.0347 0.0525  0.0290  155  VAL   A N   
538   C  CA  . VAL   A 86  ? 1.6121 1.6225 1.5535 -0.0395 0.0446  0.0267  155  VAL   A CA  
539   C  C   . VAL   A 86  ? 1.5804 1.5890 1.5144 -0.0404 0.0360  0.0266  155  VAL   A C   
540   O  O   . VAL   A 86  ? 1.6009 1.6011 1.5264 -0.0391 0.0395  0.0293  155  VAL   A O   
541   C  CB  . VAL   A 86  ? 1.5308 1.5517 1.4951 -0.0424 0.0514  0.0276  155  VAL   A CB  
542   C  CG1 . VAL   A 86  ? 1.4977 1.5335 1.4798 -0.0468 0.0429  0.0252  155  VAL   A CG1 
543   C  CG2 . VAL   A 86  ? 1.5286 1.5522 1.5016 -0.0414 0.0593  0.0274  155  VAL   A CG2 
544   N  N   . LYS   A 87  ? 1.5331 1.5492 1.4701 -0.0424 0.0251  0.0237  156  LYS   A N   
545   C  CA  . LYS   A 87  ? 1.5154 1.5316 1.4476 -0.0434 0.0162  0.0234  156  LYS   A CA  
546   C  C   . LYS   A 87  ? 1.4490 1.4807 1.4020 -0.0478 0.0116  0.0220  156  LYS   A C   
547   O  O   . LYS   A 87  ? 1.4425 1.4844 1.4081 -0.0498 0.0090  0.0197  156  LYS   A O   
548   C  CB  . LYS   A 87  ? 1.5197 1.5307 1.4372 -0.0419 0.0071  0.0212  156  LYS   A CB  
549   N  N   . VAL   A 88  ? 1.4332 1.4660 1.3891 -0.0490 0.0106  0.0234  157  VAL   A N   
550   C  CA  . VAL   A 88  ? 1.4034 1.4495 1.3787 -0.0528 0.0076  0.0224  157  VAL   A CA  
551   C  C   . VAL   A 88  ? 1.3257 1.3726 1.2973 -0.0536 -0.0005 0.0224  157  VAL   A C   
552   O  O   . VAL   A 88  ? 1.3226 1.3593 1.2778 -0.0512 -0.0025 0.0235  157  VAL   A O   
553   C  CB  . VAL   A 88  ? 1.3506 1.3992 1.3388 -0.0541 0.0166  0.0244  157  VAL   A CB  
554   C  CG1 . VAL   A 88  ? 1.3463 1.3943 1.3393 -0.0532 0.0254  0.0247  157  VAL   A CG1 
555   C  CG2 . VAL   A 88  ? 1.3698 1.4078 1.3470 -0.0526 0.0206  0.0275  157  VAL   A CG2 
556   N  N   . LYS   A 89  ? 1.2680 1.3268 1.2553 -0.0567 -0.0051 0.0210  158  LYS   A N   
557   C  CA  . LYS   A 89  ? 1.2626 1.3236 1.2492 -0.0575 -0.0120 0.0211  158  LYS   A CA  
558   C  C   . LYS   A 89  ? 1.2671 1.3384 1.2720 -0.0605 -0.0114 0.0209  158  LYS   A C   
559   O  O   . LYS   A 89  ? 1.1811 1.2624 1.1997 -0.0624 -0.0130 0.0188  158  LYS   A O   
560   C  CB  . LYS   A 89  ? 1.1541 1.2184 1.1369 -0.0577 -0.0219 0.0188  158  LYS   A CB  
561   N  N   . ALA   A 90  ? 1.2384 1.3064 1.2430 -0.0606 -0.0090 0.0229  159  ALA   A N   
562   C  CA  . ALA   A 90  ? 1.1226 1.1990 1.1438 -0.0632 -0.0082 0.0228  159  ALA   A CA  
563   C  C   . ALA   A 90  ? 1.1088 1.1875 1.1295 -0.0637 -0.0151 0.0229  159  ALA   A C   
564   O  O   . ALA   A 90  ? 1.1355 1.2072 1.1423 -0.0618 -0.0183 0.0238  159  ALA   A O   
565   C  CB  . ALA   A 90  ? 1.0677 1.1394 1.0928 -0.0633 0.0017  0.0252  159  ALA   A CB  
566   N  N   . ILE   A 91  ? 1.0915 1.1802 1.1276 -0.0661 -0.0177 0.0216  160  ILE   A N   
567   C  CA  . ILE   A 91  ? 1.0606 1.1524 1.0990 -0.0667 -0.0232 0.0217  160  ILE   A CA  
568   C  C   . ILE   A 91  ? 1.1211 1.2116 1.1669 -0.0678 -0.0179 0.0233  160  ILE   A C   
569   O  O   . ILE   A 91  ? 1.0824 1.1754 1.1393 -0.0692 -0.0122 0.0231  160  ILE   A O   
570   C  CB  . ILE   A 91  ? 0.9027 1.0059 0.9522 -0.0682 -0.0303 0.0189  160  ILE   A CB  
571   C  CG1 . ILE   A 91  ? 0.9797 1.0856 1.0294 -0.0683 -0.0364 0.0190  160  ILE   A CG1 
572   C  CG2 . ILE   A 91  ? 0.9643 1.0750 1.0304 -0.0701 -0.0275 0.0175  160  ILE   A CG2 
573   C  CD1 . ILE   A 91  ? 1.0815 1.1795 1.1163 -0.0662 -0.0387 0.0207  160  ILE   A CD1 
574   N  N   . GLY   A 92  ? 1.0518 1.1383 1.0921 -0.0672 -0.0197 0.0248  161  GLY   A N   
575   C  CA  . GLY   A 92  ? 1.0603 1.1452 1.1074 -0.0684 -0.0152 0.0263  161  GLY   A CA  
576   C  C   . GLY   A 92  ? 1.0135 1.1089 1.0763 -0.0705 -0.0197 0.0243  161  GLY   A C   
577   O  O   . GLY   A 92  ? 1.0427 1.1436 1.1060 -0.0703 -0.0272 0.0227  161  GLY   A O   
578   N  N   . ARG   A 93  ? 0.9830 1.0807 1.0590 -0.0725 -0.0150 0.0242  162  ARG   A N   
579   C  CA  . ARG   A 93  ? 1.0324 1.1398 1.1239 -0.0744 -0.0193 0.0218  162  ARG   A CA  
580   C  C   . ARG   A 93  ? 1.0745 1.1804 1.1729 -0.0757 -0.0177 0.0228  162  ARG   A C   
581   O  O   . ARG   A 93  ? 1.0597 1.1693 1.1607 -0.0757 -0.0237 0.0218  162  ARG   A O   
582   C  CB  . ARG   A 93  ? 1.0365 1.1504 1.1407 -0.0757 -0.0171 0.0197  162  ARG   A CB  
583   C  CG  . ARG   A 93  ? 1.0966 1.2117 1.1940 -0.0744 -0.0188 0.0187  162  ARG   A CG  
584   C  CD  . ARG   A 93  ? 1.0557 1.1768 1.1513 -0.0738 -0.0277 0.0167  162  ARG   A CD  
585   N  NE  . ARG   A 93  ? 1.0079 1.1353 1.1095 -0.0740 -0.0292 0.0143  162  ARG   A NE  
586   C  CZ  . ARG   A 93  ? 1.0191 1.1512 1.1191 -0.0734 -0.0355 0.0126  162  ARG   A CZ  
587   N  NH1 . ARG   A 93  ? 1.0548 1.1864 1.1470 -0.0726 -0.0408 0.0130  162  ARG   A NH1 
588   N  NH2 . ARG   A 93  ? 1.0511 1.1887 1.1580 -0.0736 -0.0363 0.0104  162  ARG   A NH2 
589   N  N   . GLN   A 94  ? 1.1102 1.2111 1.2123 -0.0767 -0.0097 0.0245  163  GLN   A N   
590   C  CA  . GLN   A 94  ? 1.0822 1.1818 1.1926 -0.0784 -0.0080 0.0252  163  GLN   A CA  
591   C  C   . GLN   A 94  ? 1.1343 1.2225 1.2355 -0.0778 -0.0003 0.0289  163  GLN   A C   
592   O  O   . GLN   A 94  ? 1.0918 1.1742 1.1866 -0.0770 0.0064  0.0306  163  GLN   A O   
593   C  CB  . GLN   A 94  ? 1.0973 1.2040 1.2275 -0.0810 -0.0061 0.0231  163  GLN   A CB  
594   C  CG  . GLN   A 94  ? 1.1697 1.2864 1.3097 -0.0814 -0.0144 0.0195  163  GLN   A CG  
595   C  CD  . GLN   A 94  ? 1.3919 1.5154 1.5495 -0.0832 -0.0126 0.0171  163  GLN   A CD  
596   O  OE1 . GLN   A 94  ? 1.4799 1.6042 1.6389 -0.0832 -0.0082 0.0171  163  GLN   A OE1 
597   N  NE2 . GLN   A 94  ? 1.4815 1.6097 1.6526 -0.0847 -0.0161 0.0150  163  GLN   A NE2 
598   N  N   . ARG   A 95  ? 1.1184 1.2027 1.2184 -0.0781 -0.0010 0.0301  164  ARG   A N   
599   C  CA  . ARG   A 95  ? 1.1111 1.1839 1.2029 -0.0776 0.0064  0.0337  164  ARG   A CA  
600   C  C   . ARG   A 95  ? 1.1626 1.2357 1.2706 -0.0807 0.0133  0.0341  164  ARG   A C   
601   O  O   . ARG   A 95  ? 1.1906 1.2722 1.3150 -0.0830 0.0098  0.0315  164  ARG   A O   
602   C  CB  . ARG   A 95  ? 1.1152 1.1829 1.1965 -0.0760 0.0020  0.0350  164  ARG   A CB  
603   C  CG  . ARG   A 95  ? 1.0778 1.1484 1.1485 -0.0736 -0.0067 0.0337  164  ARG   A CG  
604   C  CD  . ARG   A 95  ? 1.0649 1.1385 1.1378 -0.0735 -0.0135 0.0329  164  ARG   A CD  
605   N  NE  . ARG   A 95  ? 1.1354 1.2159 1.2264 -0.0764 -0.0140 0.0309  164  ARG   A NE  
606   C  CZ  . ARG   A 95  ? 1.1628 1.2438 1.2585 -0.0769 -0.0172 0.0305  164  ARG   A CZ  
607   N  NH1 . ARG   A 95  ? 1.1250 1.2008 1.2094 -0.0748 -0.0202 0.0320  164  ARG   A NH1 
608   N  NH2 . ARG   A 95  ? 1.2253 1.3121 1.3376 -0.0794 -0.0178 0.0284  164  ARG   A NH2 
609   N  N   . PHE   A 96  ? 1.1838 1.2474 1.2872 -0.0806 0.0232  0.0374  165  PHE   A N   
610   C  CA  . PHE   A 96  ? 1.1726 1.2362 1.2921 -0.0837 0.0310  0.0381  165  PHE   A CA  
611   C  C   . PHE   A 96  ? 1.2147 1.2649 1.3251 -0.0832 0.0397  0.0424  165  PHE   A C   
612   O  O   . PHE   A 96  ? 1.2492 1.2895 1.3395 -0.0800 0.0404  0.0448  165  PHE   A O   
613   C  CB  . PHE   A 96  ? 1.1573 1.2258 1.2869 -0.0846 0.0364  0.0372  165  PHE   A CB  
614   C  CG  . PHE   A 96  ? 1.1749 1.2357 1.2880 -0.0817 0.0420  0.0395  165  PHE   A CG  
615   C  CD1 . PHE   A 96  ? 1.1875 1.2346 1.2858 -0.0798 0.0500  0.0436  165  PHE   A CD1 
616   C  CD2 . PHE   A 96  ? 1.1134 1.1799 1.2251 -0.0805 0.0392  0.0375  165  PHE   A CD2 
617   C  CE1 . PHE   A 96  ? 1.2410 1.2800 1.3230 -0.0767 0.0548  0.0456  165  PHE   A CE1 
618   C  CE2 . PHE   A 96  ? 1.1237 1.1825 1.2197 -0.0776 0.0440  0.0394  165  PHE   A CE2 
619   C  CZ  . PHE   A 96  ? 1.1685 1.2135 1.2494 -0.0756 0.0517  0.0434  165  PHE   A CZ  
620   N  N   . LYS   A 97  ? 1.2073 1.2570 1.3331 -0.0863 0.0464  0.0432  166  LYS   A N   
621   C  CA  . LYS   A 97  ? 1.2401 1.2772 1.3605 -0.0865 0.0566  0.0474  166  LYS   A CA  
622   C  C   . LYS   A 97  ? 1.1706 1.2070 1.3019 -0.0881 0.0679  0.0488  166  LYS   A C   
623   O  O   . LYS   A 97  ? 1.1608 1.2073 1.3139 -0.0913 0.0680  0.0463  166  LYS   A O   
624   C  CB  . LYS   A 97  ? 1.2885 1.3245 1.4182 -0.0890 0.0553  0.0475  166  LYS   A CB  
625   C  CG  . LYS   A 97  ? 1.2857 1.3082 1.4107 -0.0894 0.0665  0.0520  166  LYS   A CG  
626   C  CD  . LYS   A 97  ? 1.3070 1.3279 1.4403 -0.0918 0.0648  0.0520  166  LYS   A CD  
627   C  CE  . LYS   A 97  ? 1.3657 1.3708 1.4863 -0.0908 0.0740  0.0569  166  LYS   A CE  
628   N  NZ  . LYS   A 97  ? 1.3479 1.3519 1.4874 -0.0951 0.0813  0.0578  166  LYS   A NZ  
629   N  N   . VAL   A 98  ? 1.1781 1.2025 1.2946 -0.0857 0.0774  0.0528  167  VAL   A N   
630   C  CA  . VAL   A 98  ? 1.1733 1.1969 1.2992 -0.0867 0.0887  0.0543  167  VAL   A CA  
631   C  C   . VAL   A 98  ? 1.2286 1.2521 1.3744 -0.0909 0.0960  0.0554  167  VAL   A C   
632   O  O   . VAL   A 98  ? 1.3049 1.3199 1.4461 -0.0914 0.0983  0.0578  167  VAL   A O   
633   C  CB  . VAL   A 98  ? 1.2523 1.2617 1.3559 -0.0826 0.0975  0.0584  167  VAL   A CB  
634   C  CG1 . VAL   A 98  ? 1.2550 1.2612 1.3692 -0.0839 0.1116  0.0611  167  VAL   A CG1 
635   C  CG2 . VAL   A 98  ? 1.2982 1.3096 1.3869 -0.0790 0.0911  0.0567  167  VAL   A CG2 
636   N  N   . LEU   A 99  ? 1.2139 1.2469 1.3821 -0.0939 0.0995  0.0537  168  LEU   A N   
637   C  CA  . LEU   A 99  ? 1.2066 1.2403 1.3965 -0.0981 0.1074  0.0546  168  LEU   A CA  
638   C  C   . LEU   A 99  ? 1.2450 1.2712 1.4360 -0.0978 0.1227  0.0587  168  LEU   A C   
639   O  O   . LEU   A 99  ? 1.3078 1.3250 1.5015 -0.0993 0.1322  0.0622  168  LEU   A O   
640   C  CB  . LEU   A 99  ? 1.1261 1.1760 1.3428 -0.1018 0.1003  0.0496  168  LEU   A CB  
641   C  CG  . LEU   A 99  ? 1.0507 1.1073 1.2671 -0.1020 0.0859  0.0457  168  LEU   A CG  
642   C  CD1 . LEU   A 99  ? 1.0632 1.1296 1.3065 -0.1064 0.0823  0.0423  168  LEU   A CD1 
643   C  CD2 . LEU   A 99  ? 1.0686 1.1142 1.2656 -0.1003 0.0839  0.0482  168  LEU   A CD2 
644   N  N   . GLU   A 100 ? 1.2624 1.2916 1.4513 -0.0958 0.1257  0.0583  169  GLU   A N   
645   C  CA  . GLU   A 100 ? 1.3206 1.3419 1.5076 -0.0945 0.1404  0.0623  169  GLU   A CA  
646   C  C   . GLU   A 100 ? 1.4208 1.4371 1.5849 -0.0894 0.1404  0.0630  169  GLU   A C   
647   O  O   . GLU   A 100 ? 1.3772 1.3969 1.5290 -0.0873 0.1290  0.0604  169  GLU   A O   
648   C  CB  . GLU   A 100 ? 1.2848 1.3169 1.5016 -0.0983 0.1461  0.0608  169  GLU   A CB  
649   C  CG  . GLU   A 100 ? 1.2658 1.3026 1.5065 -0.1035 0.1464  0.0599  169  GLU   A CG  
650   C  CD  . GLU   A 100 ? 1.4007 1.4483 1.6708 -0.1068 0.1518  0.0582  169  GLU   A CD  
651   O  OE1 . GLU   A 100 ? 1.4163 1.4661 1.6860 -0.1047 0.1569  0.0585  169  GLU   A OE1 
652   O  OE2 . GLU   A 100 ? 1.4871 1.5410 1.7810 -0.1114 0.1508  0.0565  169  GLU   A OE2 
653   N  N   . LEU   A 101 ? 1.5123 1.5203 1.6709 -0.0873 0.1534  0.0666  170  LEU   A N   
654   C  CA  . LEU   A 101 ? 1.5084 1.5097 1.6444 -0.0821 0.1546  0.0676  170  LEU   A CA  
655   C  C   . LEU   A 101 ? 1.6697 1.6691 1.8131 -0.0814 0.1684  0.0699  170  LEU   A C   
656   O  O   . LEU   A 101 ? 1.6807 1.6670 1.8170 -0.0801 0.1815  0.0748  170  LEU   A O   
657   C  CB  . LEU   A 101 ? 1.3773 1.3615 1.4825 -0.0777 0.1554  0.0711  170  LEU   A CB  
658   C  CG  . LEU   A 101 ? 1.4058 1.3905 1.4933 -0.0755 0.1410  0.0686  170  LEU   A CG  
659   C  CD1 . LEU   A 101 ? 1.2587 1.2257 1.3187 -0.0715 0.1430  0.0723  170  LEU   A CD1 
660   C  CD2 . LEU   A 101 ? 1.4813 1.4718 1.5616 -0.0729 0.1345  0.0657  170  LEU   A CD2 
661   N  N   . ARG   A 102 ? 1.8293 1.8411 1.9861 -0.0819 0.1657  0.0666  171  ARG   A N   
662   C  CA  . ARG   A 102 ? 1.8804 1.8910 2.0423 -0.0804 0.1776  0.0684  171  ARG   A CA  
663   C  C   . ARG   A 102 ? 1.9554 1.9544 2.0876 -0.0743 0.1791  0.0701  171  ARG   A C   
664   O  O   . ARG   A 102 ? 1.9714 1.9759 2.0957 -0.0725 0.1689  0.0668  171  ARG   A O   
665   C  CB  . ARG   A 102 ? 1.8524 1.8808 2.0398 -0.0830 0.1734  0.0639  171  ARG   A CB  
666   C  CG  . ARG   A 102 ? 1.8088 1.8466 2.0288 -0.0879 0.1794  0.0634  171  ARG   A CG  
667   C  CD  . ARG   A 102 ? 1.7762 1.8316 2.0169 -0.0912 0.1657  0.0574  171  ARG   A CD  
668   N  NE  . ARG   A 102 ? 1.8098 1.8647 2.0362 -0.0910 0.1524  0.0554  171  ARG   A NE  
669   C  CZ  . ARG   A 102 ? 1.7736 1.8260 2.0019 -0.0935 0.1491  0.0558  171  ARG   A CZ  
670   N  NH1 . ARG   A 102 ? 1.7436 1.7950 1.9894 -0.0971 0.1570  0.0577  171  ARG   A NH1 
671   N  NH2 . ARG   A 102 ? 1.7531 1.8039 1.9654 -0.0923 0.1378  0.0544  171  ARG   A NH2 
672   N  N   . THR   A 103 ? 2.0067 1.9893 2.1225 -0.0710 0.1919  0.0753  172  THR   A N   
673   C  CA  . THR   A 103 ? 2.0561 2.0264 2.1442 -0.0649 0.1948  0.0771  172  THR   A CA  
674   C  C   . THR   A 103 ? 2.0479 2.0217 2.1470 -0.0639 0.2050  0.0776  172  THR   A C   
675   O  O   . THR   A 103 ? 2.0825 2.0458 2.1787 -0.0620 0.2201  0.0821  172  THR   A O   
676   C  CB  . THR   A 103 ? 2.0529 2.0024 2.1146 -0.0610 0.2026  0.0822  172  THR   A CB  
677   O  OG1 . THR   A 103 ? 1.9535 1.9013 2.0104 -0.0626 0.1941  0.0818  172  THR   A OG1 
678   C  CG2 . THR   A 103 ? 2.0678 2.0047 2.0982 -0.0543 0.2012  0.0830  172  THR   A CG2 
679   N  N   . GLN   A 104 ? 2.0626 2.0513 2.1749 -0.0651 0.1969  0.0730  173  GLN   A N   
680   C  CA  . GLN   A 104 ? 2.0966 2.0908 2.2222 -0.0645 0.2052  0.0728  173  GLN   A CA  
681   C  C   . GLN   A 104 ? 2.1591 2.1372 2.2585 -0.0580 0.2147  0.0764  173  GLN   A C   
682   O  O   . GLN   A 104 ? 2.1688 2.1323 2.2393 -0.0540 0.2130  0.0783  173  GLN   A O   
683   C  CB  . GLN   A 104 ? 2.0915 2.1032 2.2318 -0.0661 0.1932  0.0671  173  GLN   A CB  
684   C  CG  . GLN   A 104 ? 2.0773 2.1055 2.2474 -0.0722 0.1860  0.0635  173  GLN   A CG  
685   C  CD  . GLN   A 104 ? 2.0585 2.1028 2.2417 -0.0733 0.1745  0.0579  173  GLN   A CD  
686   O  OE1 . GLN   A 104 ? 2.0552 2.0985 2.2216 -0.0702 0.1671  0.0560  173  GLN   A OE1 
687   N  NE2 . GLN   A 104 ? 1.9896 2.0483 2.2031 -0.0777 0.1727  0.0551  173  GLN   A NE2 
688   N  N   . SER   A 105 ? 2.1141 2.0950 2.2240 -0.0568 0.2246  0.0771  174  SER   A N   
689   C  CA  . SER   A 105 ? 2.0663 2.0317 2.1525 -0.0505 0.2348  0.0806  174  SER   A CA  
690   C  C   . SER   A 105 ? 2.0785 2.0394 2.1388 -0.0462 0.2235  0.0780  174  SER   A C   
691   O  O   . SER   A 105 ? 2.0638 2.0072 2.0940 -0.0410 0.2259  0.0807  174  SER   A O   
692   C  CB  . SER   A 105 ? 1.9600 1.9312 2.0653 -0.0503 0.2469  0.0814  174  SER   A CB  
693   O  OG  . SER   A 105 ? 1.9369 1.9279 2.0671 -0.0537 0.2384  0.0763  174  SER   A OG  
694   N  N   . ASP   A 106 ? 2.0624 2.0386 2.1339 -0.0482 0.2110  0.0728  175  ASP   A N   
695   C  CA  . ASP   A 106 ? 2.0536 2.0283 2.1050 -0.0450 0.1994  0.0697  175  ASP   A CA  
696   C  C   . ASP   A 106 ? 2.0845 2.0438 2.1049 -0.0416 0.1941  0.0712  175  ASP   A C   
697   O  O   . ASP   A 106 ? 2.0740 2.0236 2.0702 -0.0368 0.1911  0.0709  175  ASP   A O   
698   C  CB  . ASP   A 106 ? 2.0492 2.0427 2.1184 -0.0492 0.1843  0.0640  175  ASP   A CB  
699   C  CG  . ASP   A 106 ? 2.0657 2.0761 2.1694 -0.0536 0.1871  0.0620  175  ASP   A CG  
700   O  OD1 . ASP   A 106 ? 2.0842 2.0974 2.2058 -0.0571 0.1936  0.0638  175  ASP   A OD1 
701   O  OD2 . ASP   A 106 ? 2.0782 2.0993 2.1914 -0.0536 0.1822  0.0585  175  ASP   A OD2 
702   N  N   . GLY   A 107 ? 2.1122 2.0692 2.1334 -0.0441 0.1924  0.0725  176  GLY   A N   
703   C  CA  . GLY   A 107 ? 2.1112 2.0581 2.1083 -0.0420 0.1836  0.0727  176  GLY   A CA  
704   C  C   . GLY   A 107 ? 2.1156 2.0761 2.1231 -0.0463 0.1680  0.0685  176  GLY   A C   
705   O  O   . GLY   A 107 ? 2.1204 2.0743 2.1112 -0.0452 0.1602  0.0685  176  GLY   A O   
706   N  N   . ILE   A 108 ? 1.9920 1.9708 2.0264 -0.0508 0.1633  0.0649  177  ILE   A N   
707   C  CA  . ILE   A 108 ? 1.8666 1.8587 1.9129 -0.0549 0.1494  0.0609  177  ILE   A CA  
708   C  C   . ILE   A 108 ? 1.8655 1.8626 1.9317 -0.0595 0.1524  0.0620  177  ILE   A C   
709   O  O   . ILE   A 108 ? 1.9120 1.9128 1.9975 -0.0617 0.1626  0.0634  177  ILE   A O   
710   C  CB  . ILE   A 108 ? 1.7275 1.7355 1.7897 -0.0566 0.1419  0.0562  177  ILE   A CB  
711   N  N   . GLN   A 109 ? 1.7812 1.7786 1.8435 -0.0611 0.1435  0.0612  178  GLN   A N   
712   C  CA  . GLN   A 109 ? 1.7838 1.7838 1.8613 -0.0651 0.1454  0.0622  178  GLN   A CA  
713   C  C   . GLN   A 109 ? 1.7717 1.7895 1.8720 -0.0698 0.1342  0.0576  178  GLN   A C   
714   O  O   . GLN   A 109 ? 1.6704 1.6928 1.7639 -0.0696 0.1216  0.0546  178  GLN   A O   
715   C  CB  . GLN   A 109 ? 1.7359 1.7225 1.7922 -0.0632 0.1439  0.0649  178  GLN   A CB  
716   N  N   . GLN   A 110 ? 1.9676 1.9949 2.0948 -0.0739 0.1388  0.0569  179  GLN   A N   
717   C  CA  . GLN   A 110 ? 1.9271 1.9696 2.0766 -0.0782 0.1290  0.0527  179  GLN   A CA  
718   C  C   . GLN   A 110 ? 1.9253 1.9651 2.0766 -0.0807 0.1264  0.0537  179  GLN   A C   
719   O  O   . GLN   A 110 ? 1.9679 1.9955 2.1106 -0.0801 0.1353  0.0580  179  GLN   A O   
720   C  CB  . GLN   A 110 ? 1.9256 1.9793 2.1036 -0.0812 0.1344  0.0513  179  GLN   A CB  
721   C  CG  . GLN   A 110 ? 1.9716 2.0276 2.1490 -0.0786 0.1385  0.0507  179  GLN   A CG  
722   C  CD  . GLN   A 110 ? 1.9730 2.0354 2.1418 -0.0769 0.1260  0.0467  179  GLN   A CD  
723   O  OE1 . GLN   A 110 ? 1.8832 1.9537 2.0568 -0.0788 0.1142  0.0434  179  GLN   A OE1 
724   N  NE2 . GLN   A 110 ? 1.9803 2.0386 2.1360 -0.0732 0.1288  0.0471  179  GLN   A NE2 
725   N  N   . ALA   A 111 ? 1.6461 1.6966 1.8080 -0.0834 0.1145  0.0499  180  ALA   A N   
726   C  CA  . ALA   A 111 ? 1.4800 1.5270 1.6399 -0.0850 0.1107  0.0507  180  ALA   A CA  
727   C  C   . ALA   A 111 ? 1.3506 1.4108 1.5340 -0.0893 0.1025  0.0467  180  ALA   A C   
728   O  O   . ALA   A 111 ? 1.2284 1.2993 1.4169 -0.0895 0.0921  0.0426  180  ALA   A O   
729   C  CB  . ALA   A 111 ? 1.3781 1.4182 1.5124 -0.0817 0.1024  0.0509  180  ALA   A CB  
730   N  N   . LYS   A 112 ? 1.3152 1.3739 1.5120 -0.0925 0.1072  0.0481  181  LYS   A N   
731   C  CA  . LYS   A 112 ? 1.2430 1.3114 1.4586 -0.0962 0.0988  0.0447  181  LYS   A CA  
732   C  C   . LYS   A 112 ? 1.1976 1.2624 1.3971 -0.0950 0.0891  0.0443  181  LYS   A C   
733   O  O   . LYS   A 112 ? 1.2028 1.2555 1.3858 -0.0935 0.0929  0.0479  181  LYS   A O   
734   C  CB  . LYS   A 112 ? 1.1464 1.2138 1.3817 -0.1001 0.1070  0.0462  181  LYS   A CB  
735   N  N   . VAL   A 113 ? 1.1828 1.2577 1.3865 -0.0953 0.0767  0.0400  182  VAL   A N   
736   C  CA  . VAL   A 113 ? 1.1489 1.2213 1.3357 -0.0933 0.0672  0.0395  182  VAL   A CA  
737   C  C   . VAL   A 113 ? 1.1733 1.2536 1.3744 -0.0959 0.0580  0.0361  182  VAL   A C   
738   O  O   . VAL   A 113 ? 1.2752 1.3661 1.4962 -0.0981 0.0547  0.0326  182  VAL   A O   
739   C  CB  . VAL   A 113 ? 1.1661 1.2414 1.3389 -0.0901 0.0608  0.0378  182  VAL   A CB  
740   C  CG1 . VAL   A 113 ? 1.2053 1.2849 1.3721 -0.0894 0.0484  0.0353  182  VAL   A CG1 
741   C  CG2 . VAL   A 113 ? 1.1430 1.2061 1.2930 -0.0866 0.0673  0.0416  182  VAL   A CG2 
742   N  N   . GLN   A 114 ? 1.1452 1.2197 1.3357 -0.0954 0.0540  0.0372  183  GLN   A N   
743   C  CA  . GLN   A 114 ? 1.1949 1.2754 1.3944 -0.0970 0.0444  0.0341  183  GLN   A CA  
744   C  C   . GLN   A 114 ? 1.2295 1.3114 1.4126 -0.0939 0.0343  0.0328  183  GLN   A C   
745   O  O   . GLN   A 114 ? 1.2270 1.3001 1.3905 -0.0914 0.0348  0.0355  183  GLN   A O   
746   C  CB  . GLN   A 114 ? 1.2485 1.3210 1.4503 -0.0989 0.0483  0.0365  183  GLN   A CB  
747   C  CG  . GLN   A 114 ? 1.3410 1.4173 1.5496 -0.1002 0.0388  0.0338  183  GLN   A CG  
748   C  CD  . GLN   A 114 ? 1.3546 1.4410 1.5888 -0.1036 0.0358  0.0298  183  GLN   A CD  
749   O  OE1 . GLN   A 114 ? 1.3728 1.4604 1.6230 -0.1063 0.0433  0.0302  183  GLN   A OE1 
750   N  NE2 . GLN   A 114 ? 1.3754 1.4688 1.6137 -0.1034 0.0246  0.0260  183  GLN   A NE2 
751   N  N   . ILE   A 115 ? 1.3375 1.4301 1.5284 -0.0940 0.0253  0.0287  184  ILE   A N   
752   C  CA  . ILE   A 115 ? 1.3877 1.4825 1.5647 -0.0912 0.0161  0.0274  184  ILE   A CA  
753   C  C   . ILE   A 115 ? 1.3861 1.4773 1.5574 -0.0908 0.0109  0.0278  184  ILE   A C   
754   O  O   . ILE   A 115 ? 1.4680 1.5631 1.6522 -0.0927 0.0069  0.0257  184  ILE   A O   
755   C  CB  . ILE   A 115 ? 1.4025 1.5090 1.5893 -0.0911 0.0086  0.0231  184  ILE   A CB  
756   C  CG1 . ILE   A 115 ? 1.3474 1.4571 1.5400 -0.0913 0.0141  0.0228  184  ILE   A CG1 
757   C  CG2 . ILE   A 115 ? 1.3840 1.4923 1.5564 -0.0883 0.0002  0.0222  184  ILE   A CG2 
758   C  CD1 . ILE   A 115 ? 1.6267 1.7468 1.8267 -0.0908 0.0070  0.0189  184  ILE   A CD1 
759   N  N   . LEU   A 116 ? 1.3438 1.4272 1.4955 -0.0882 0.0107  0.0305  185  LEU   A N   
760   C  CA  . LEU   A 116 ? 1.3255 1.4051 1.4701 -0.0873 0.0056  0.0310  185  LEU   A CA  
761   C  C   . LEU   A 116 ? 1.4072 1.4964 1.5577 -0.0870 -0.0050 0.0272  185  LEU   A C   
762   O  O   . LEU   A 116 ? 1.3927 1.4902 1.5486 -0.0868 -0.0087 0.0245  185  LEU   A O   
763   C  CB  . LEU   A 116 ? 1.2785 1.3492 1.4009 -0.0840 0.0063  0.0340  185  LEU   A CB  
764   C  CG  . LEU   A 116 ? 1.2559 1.3137 1.3691 -0.0837 0.0159  0.0382  185  LEU   A CG  
765   C  CD1 . LEU   A 116 ? 1.2233 1.2802 1.3487 -0.0863 0.0259  0.0392  185  LEU   A CD1 
766   C  CD2 . LEU   A 116 ? 1.2365 1.2865 1.3277 -0.0799 0.0164  0.0405  185  LEU   A CD2 
767   N  N   . PRO   A 117 ? 1.4856 1.5731 1.6348 -0.0866 -0.0098 0.0269  186  PRO   A N   
768   C  CA  . PRO   A 117 ? 1.4832 1.5789 1.6386 -0.0862 -0.0193 0.0234  186  PRO   A CA  
769   C  C   . PRO   A 117 ? 1.4453 1.5433 1.5873 -0.0829 -0.0260 0.0231  186  PRO   A C   
770   O  O   . PRO   A 117 ? 1.4163 1.5082 1.5429 -0.0808 -0.0251 0.0257  186  PRO   A O   
771   C  CB  . PRO   A 117 ? 1.4604 1.5521 1.6202 -0.0872 -0.0207 0.0235  186  PRO   A CB  
772   C  CG  . PRO   A 117 ? 1.4424 1.5229 1.5919 -0.0870 -0.0135 0.0276  186  PRO   A CG  
773   C  CD  . PRO   A 117 ? 1.4515 1.5299 1.5991 -0.0876 -0.0053 0.0295  186  PRO   A CD  
774   N  N   . GLU   A 118 ? 1.4265 1.5333 1.5748 -0.0824 -0.0330 0.0198  187  GLU   A N   
775   C  CA  . GLU   A 118 ? 1.3393 1.4494 1.4780 -0.0796 -0.0400 0.0191  187  GLU   A CA  
776   C  C   . GLU   A 118 ? 1.2809 1.3955 1.4270 -0.0791 -0.0470 0.0164  187  GLU   A C   
777   O  O   . GLU   A 118 ? 1.3139 1.4357 1.4653 -0.0785 -0.0518 0.0136  187  GLU   A O   
778   C  CB  . GLU   A 118 ? 1.2545 1.3701 1.3911 -0.0788 -0.0409 0.0181  187  GLU   A CB  
779   C  CG  . GLU   A 118 ? 1.2457 1.3623 1.3693 -0.0760 -0.0459 0.0186  187  GLU   A CG  
780   C  CD  . GLU   A 118 ? 1.2486 1.3573 1.3572 -0.0747 -0.0424 0.0219  187  GLU   A CD  
781   O  OE1 . GLU   A 118 ? 1.2488 1.3541 1.3543 -0.0753 -0.0368 0.0232  187  GLU   A OE1 
782   O  OE2 . GLU   A 118 ? 1.2039 1.3094 1.3032 -0.0727 -0.0456 0.0232  187  GLU   A OE2 
783   N  N   . CYS   A 119 ? 1.2183 1.3279 1.3638 -0.0792 -0.0475 0.0172  188  CYS   A N   
784   C  CA  . CYS   A 119 ? 1.1635 1.2757 1.3148 -0.0785 -0.0540 0.0148  188  CYS   A CA  
785   C  C   . CYS   A 119 ? 1.0563 1.1729 1.1997 -0.0753 -0.0605 0.0140  188  CYS   A C   
786   O  O   . CYS   A 119 ? 1.0019 1.1158 1.1330 -0.0732 -0.0609 0.0162  188  CYS   A O   
787   C  CB  . CYS   A 119 ? 1.1356 1.2405 1.2854 -0.0787 -0.0532 0.0162  188  CYS   A CB  
788   S  SG  . CYS   A 119 ? 1.1940 1.2910 1.3477 -0.0820 -0.0437 0.0188  188  CYS   A SG  
789   N  N   . VAL   A 120 ? 1.0390 1.1621 1.1898 -0.0747 -0.0654 0.0108  189  VAL   A N   
790   C  CA  . VAL   A 120 ? 1.0246 1.1520 1.1696 -0.0716 -0.0714 0.0099  189  VAL   A CA  
791   C  C   . VAL   A 120 ? 0.9683 1.0948 1.1165 -0.0702 -0.0765 0.0081  189  VAL   A C   
792   O  O   . VAL   A 120 ? 1.0208 1.1478 1.1799 -0.0716 -0.0775 0.0057  189  VAL   A O   
793   C  CB  . VAL   A 120 ? 0.9160 1.0503 1.0650 -0.0715 -0.0728 0.0078  189  VAL   A CB  
794   C  CG1 . VAL   A 120 ? 1.0457 1.1824 1.2087 -0.0736 -0.0724 0.0050  189  VAL   A CG1 
795   C  CG2 . VAL   A 120 ? 0.8186 0.9568 0.9629 -0.0684 -0.0787 0.0068  189  VAL   A CG2 
796   N  N   . LEU   A 121 ? 0.9360 1.0611 1.0751 -0.0674 -0.0797 0.0092  190  LEU   A N   
797   C  CA  . LEU   A 121 ? 0.9177 1.0404 1.0580 -0.0657 -0.0840 0.0080  190  LEU   A CA  
798   C  C   . LEU   A 121 ? 0.9277 1.0547 1.0644 -0.0621 -0.0895 0.0067  190  LEU   A C   
799   O  O   . LEU   A 121 ? 1.0140 1.1443 1.1441 -0.0606 -0.0897 0.0079  190  LEU   A O   
800   C  CB  . LEU   A 121 ? 0.9882 1.1040 1.1211 -0.0651 -0.0825 0.0106  190  LEU   A CB  
801   C  CG  . LEU   A 121 ? 0.9886 1.0984 1.1241 -0.0683 -0.0767 0.0123  190  LEU   A CG  
802   C  CD1 . LEU   A 121 ? 1.0171 1.1196 1.1452 -0.0670 -0.0767 0.0143  190  LEU   A CD1 
803   C  CD2 . LEU   A 121 ? 0.9914 1.1019 1.1412 -0.0712 -0.0761 0.0097  190  LEU   A CD2 
804   N  N   . PRO   A 122 ? 0.9494 1.0756 1.0898 -0.0605 -0.0940 0.0042  191  PRO   A N   
805   C  CA  . PRO   A 122 ? 0.9403 1.0693 1.0761 -0.0565 -0.0988 0.0032  191  PRO   A CA  
806   C  C   . PRO   A 122 ? 1.0113 1.1381 1.1369 -0.0538 -0.0994 0.0058  191  PRO   A C   
807   O  O   . PRO   A 122 ? 1.0463 1.1689 1.1679 -0.0548 -0.0967 0.0082  191  PRO   A O   
808   C  CB  . PRO   A 122 ? 0.9648 1.0918 1.1070 -0.0556 -0.1032 -0.0001 191  PRO   A CB  
809   C  CG  . PRO   A 122 ? 0.9994 1.1210 1.1469 -0.0585 -0.1011 0.0001  191  PRO   A CG  
810   C  CD  . PRO   A 122 ? 1.0223 1.1447 1.1714 -0.0621 -0.0949 0.0022  191  PRO   A CD  
811   N  N   . SER   A 123 ? 1.0815 1.2108 1.2027 -0.0501 -0.1029 0.0054  192  SER   A N   
812   C  CA  . SER   A 123 ? 1.0435 1.1710 1.1561 -0.0470 -0.1039 0.0076  192  SER   A CA  
813   C  C   . SER   A 123 ? 1.0548 1.1754 1.1666 -0.0465 -0.1048 0.0077  192  SER   A C   
814   O  O   . SER   A 123 ? 1.0608 1.1783 1.1784 -0.0473 -0.1065 0.0053  192  SER   A O   
815   C  CB  . SER   A 123 ? 1.0456 1.1766 1.1553 -0.0429 -0.1071 0.0069  192  SER   A CB  
816   O  OG  . SER   A 123 ? 1.0263 1.1559 1.1289 -0.0396 -0.1081 0.0089  192  SER   A OG  
817   N  N   . THR   A 124 ? 1.0641 1.1817 1.1685 -0.0451 -0.1039 0.0103  193  THR   A N   
818   C  CA  . THR   A 124 ? 1.0916 1.2021 1.1939 -0.0442 -0.1048 0.0106  193  THR   A CA  
819   C  C   . THR   A 124 ? 1.0642 1.1731 1.1668 -0.0407 -0.1095 0.0083  193  THR   A C   
820   O  O   . THR   A 124 ? 1.0449 1.1485 1.1510 -0.0413 -0.1111 0.0066  193  THR   A O   
821   C  CB  . THR   A 124 ? 1.0696 1.1776 1.1629 -0.0425 -0.1035 0.0139  193  THR   A CB  
822   O  OG1 . THR   A 124 ? 1.1262 1.2396 1.2149 -0.0391 -0.1051 0.0148  193  THR   A OG1 
823   C  CG2 . THR   A 124 ? 1.0204 1.1269 1.1126 -0.0458 -0.0990 0.0159  193  THR   A CG2 
824   N  N   . MET   A 125 ? 1.0439 1.1571 1.1432 -0.0371 -0.1117 0.0081  194  MET   A N   
825   C  CA  . MET   A 125 ? 1.0744 1.1852 1.1721 -0.0331 -0.1158 0.0061  194  MET   A CA  
826   C  C   . MET   A 125 ? 1.1186 1.2307 1.2228 -0.0336 -0.1183 0.0025  194  MET   A C   
827   O  O   . MET   A 125 ? 1.1646 1.2744 1.2666 -0.0298 -0.1220 0.0006  194  MET   A O   
828   C  CB  . MET   A 125 ? 1.0324 1.1464 1.1232 -0.0285 -0.1166 0.0077  194  MET   A CB  
829   C  CG  . MET   A 125 ? 1.0189 1.1315 1.1030 -0.0268 -0.1153 0.0109  194  MET   A CG  
830   S  SD  . MET   A 125 ? 1.1342 1.2372 1.2144 -0.0257 -0.1164 0.0113  194  MET   A SD  
831   C  CE  . MET   A 125 ? 1.0578 1.1575 1.1438 -0.0320 -0.1134 0.0112  194  MET   A CE  
832   N  N   . SER   A 126 ? 1.1330 1.2480 1.2446 -0.0377 -0.1165 0.0015  195  SER   A N   
833   C  CA  . SER   A 126 ? 1.1527 1.2693 1.2707 -0.0379 -0.1191 -0.0020 195  SER   A CA  
834   C  C   . SER   A 126 ? 1.1711 1.2813 1.2918 -0.0367 -0.1235 -0.0050 195  SER   A C   
835   O  O   . SER   A 126 ? 1.2088 1.3180 1.3284 -0.0332 -0.1277 -0.0076 195  SER   A O   
836   C  CB  . SER   A 126 ? 1.1365 1.2568 1.2628 -0.0428 -0.1161 -0.0024 195  SER   A CB  
837   O  OG  . SER   A 126 ? 1.1325 1.2488 1.2654 -0.0464 -0.1148 -0.0030 195  SER   A OG  
838   N  N   . ALA   A 127 ? 1.1622 1.2674 1.2860 -0.0393 -0.1227 -0.0048 196  ALA   A N   
839   C  CA  . ALA   A 127 ? 1.1749 1.2736 1.3022 -0.0387 -0.1270 -0.0078 196  ALA   A CA  
840   C  C   . ALA   A 127 ? 1.1907 1.2840 1.3085 -0.0334 -0.1305 -0.0076 196  ALA   A C   
841   O  O   . ALA   A 127 ? 1.2186 1.3069 1.3370 -0.0311 -0.1355 -0.0108 196  ALA   A O   
842   C  CB  . ALA   A 127 ? 1.1431 1.2382 1.2775 -0.0435 -0.1244 -0.0073 196  ALA   A CB  
843   N  N   . VAL   A 128 ? 1.1835 1.2774 1.2925 -0.0312 -0.1282 -0.0043 197  VAL   A N   
844   C  CA  . VAL   A 128 ? 1.2029 1.2912 1.3031 -0.0263 -0.1308 -0.0038 197  VAL   A CA  
845   C  C   . VAL   A 128 ? 1.2088 1.3002 1.3021 -0.0210 -0.1322 -0.0037 197  VAL   A C   
846   O  O   . VAL   A 128 ? 1.1740 1.2623 1.2591 -0.0163 -0.1334 -0.0027 197  VAL   A O   
847   C  CB  . VAL   A 128 ? 1.1927 1.2787 1.2883 -0.0272 -0.1274 -0.0003 197  VAL   A CB  
848   C  CG1 . VAL   A 128 ? 1.1986 1.2827 1.2837 -0.0215 -0.1283 0.0016  197  VAL   A CG1 
849   C  CG2 . VAL   A 128 ? 1.1511 1.2303 1.2517 -0.0307 -0.1274 -0.0011 197  VAL   A CG2 
850   N  N   . GLN   A 129 ? 1.2618 1.3589 1.3587 -0.0217 -0.1319 -0.0048 198  GLN   A N   
851   C  CA  . GLN   A 129 ? 1.2807 1.3809 1.3715 -0.0171 -0.1322 -0.0043 198  GLN   A CA  
852   C  C   . GLN   A 129 ? 1.3034 1.3973 1.3895 -0.0119 -0.1372 -0.0071 198  GLN   A C   
853   O  O   . GLN   A 129 ? 1.3278 1.4181 1.4185 -0.0126 -0.1411 -0.0107 198  GLN   A O   
854   C  CB  . GLN   A 129 ? 1.3183 1.4257 1.4137 -0.0193 -0.1304 -0.0046 198  GLN   A CB  
855   C  CG  . GLN   A 129 ? 1.3445 1.4586 1.4369 -0.0195 -0.1262 -0.0010 198  GLN   A CG  
856   C  CD  . GLN   A 129 ? 1.3901 1.5039 1.4740 -0.0138 -0.1262 0.0008  198  GLN   A CD  
857   O  OE1 . GLN   A 129 ? 1.3640 1.4718 1.4427 -0.0099 -0.1286 0.0003  198  GLN   A OE1 
858   N  NE2 . GLN   A 129 ? 1.4804 1.6005 1.5632 -0.0134 -0.1234 0.0029  198  GLN   A NE2 
859   N  N   . LEU   A 130 ? 1.2247 1.3167 1.3016 -0.0065 -0.1372 -0.0055 199  LEU   A N   
860   C  CA  . LEU   A 130 ? 1.1811 1.2666 1.2515 -0.0006 -0.1414 -0.0079 199  LEU   A CA  
861   C  C   . LEU   A 130 ? 1.2552 1.3438 1.3252 0.0013  -0.1419 -0.0092 199  LEU   A C   
862   O  O   . LEU   A 130 ? 1.3054 1.4004 1.3740 0.0017  -0.1380 -0.0067 199  LEU   A O   
863   C  CB  . LEU   A 130 ? 1.1525 1.2351 1.2130 0.0049  -0.1404 -0.0054 199  LEU   A CB  
864   C  CG  . LEU   A 130 ? 1.1504 1.2242 1.2062 0.0073  -0.1432 -0.0059 199  LEU   A CG  
865   C  CD1 . LEU   A 130 ? 1.1918 1.2621 1.2367 0.0147  -0.1431 -0.0046 199  LEU   A CD1 
866   C  CD2 . LEU   A 130 ? 1.1386 1.2049 1.1974 0.0066  -0.1488 -0.0104 199  LEU   A CD2 
867   N  N   . GLU   A 131 ? 1.2246 1.3084 1.2958 0.0026  -0.1468 -0.0133 200  GLU   A N   
868   C  CA  . GLU   A 131 ? 1.2217 1.3074 1.2924 0.0045  -0.1477 -0.0150 200  GLU   A CA  
869   C  C   . GLU   A 131 ? 1.2024 1.2898 1.2641 0.0095  -0.1444 -0.0123 200  GLU   A C   
870   O  O   . GLU   A 131 ? 1.2637 1.3579 1.3273 0.0080  -0.1408 -0.0106 200  GLU   A O   
871   C  CB  . GLU   A 131 ? 1.2640 1.3416 1.3337 0.0075  -0.1546 -0.0199 200  GLU   A CB  
872   C  CG  . GLU   A 131 ? 1.2963 1.3748 1.3782 0.0020  -0.1576 -0.0233 200  GLU   A CG  
873   C  CD  . GLU   A 131 ? 1.3633 1.4413 1.4518 -0.0028 -0.1568 -0.0225 200  GLU   A CD  
874   O  OE1 . GLU   A 131 ? 1.2886 1.3612 1.3708 -0.0004 -0.1572 -0.0213 200  GLU   A OE1 
875   O  OE2 . GLU   A 131 ? 1.3812 1.4636 1.4809 -0.0089 -0.1554 -0.0230 200  GLU   A OE2 
876   N  N   . SER   A 132 ? 1.1763 1.2572 1.2283 0.0154  -0.1455 -0.0117 201  SER   A N   
877   C  CA  . SER   A 132 ? 1.1730 1.2551 1.2167 0.0205  -0.1417 -0.0086 201  SER   A CA  
878   C  C   . SER   A 132 ? 1.1999 1.2921 1.2481 0.0168  -0.1357 -0.0046 201  SER   A C   
879   O  O   . SER   A 132 ? 1.2889 1.3850 1.3348 0.0187  -0.1322 -0.0026 201  SER   A O   
880   C  CB  . SER   A 132 ? 1.1806 1.2554 1.2151 0.0260  -0.1426 -0.0078 201  SER   A CB  
881   O  OG  . SER   A 132 ? 1.1815 1.2562 1.2197 0.0227  -0.1428 -0.0069 201  SER   A OG  
882   N  N   . LEU   A 133 ? 1.2425 1.3385 1.2969 0.0117  -0.1343 -0.0032 202  LEU   A N   
883   C  CA  . LEU   A 133 ? 1.2629 1.3678 1.3210 0.0085  -0.1293 0.0005  202  LEU   A CA  
884   C  C   . LEU   A 133 ? 1.3428 1.4545 1.4081 0.0036  -0.1277 0.0001  202  LEU   A C   
885   O  O   . LEU   A 133 ? 1.3661 1.4850 1.4339 0.0014  -0.1238 0.0028  202  LEU   A O   
886   C  CB  . LEU   A 133 ? 1.2326 1.3380 1.2928 0.0056  -0.1285 0.0022  202  LEU   A CB  
887   C  CG  . LEU   A 133 ? 1.1966 1.2975 1.2495 0.0107  -0.1286 0.0039  202  LEU   A CG  
888   C  CD1 . LEU   A 133 ? 1.0912 1.1937 1.1383 0.0163  -0.1261 0.0058  202  LEU   A CD1 
889   C  CD2 . LEU   A 133 ? 1.2754 1.3664 1.3245 0.0131  -0.1333 0.0009  202  LEU   A CD2 
890   N  N   . ASN   A 134 ? 1.3819 1.4914 1.4507 0.0019  -0.1308 -0.0034 203  ASN   A N   
891   C  CA  . ASN   A 134 ? 1.3837 1.4993 1.4601 -0.0032 -0.1294 -0.0039 203  ASN   A CA  
892   C  C   . ASN   A 134 ? 1.3772 1.4981 1.4521 -0.0021 -0.1262 -0.0023 203  ASN   A C   
893   O  O   . ASN   A 134 ? 1.3784 1.5056 1.4587 -0.0064 -0.1237 -0.0014 203  ASN   A O   
894   C  CB  . ASN   A 134 ? 1.3702 1.4823 1.4511 -0.0044 -0.1337 -0.0082 203  ASN   A CB  
895   C  CG  . ASN   A 134 ? 1.3909 1.5026 1.4797 -0.0097 -0.1346 -0.0092 203  ASN   A CG  
896   O  OD1 . ASN   A 134 ? 1.4346 1.5449 1.5296 -0.0117 -0.1376 -0.0125 203  ASN   A OD1 
897   N  ND2 . ASN   A 134 ? 1.3945 1.5073 1.4832 -0.0117 -0.1320 -0.0065 203  ASN   A ND2 
898   N  N   . LYS   A 135 ? 1.3397 1.4574 1.4069 0.0038  -0.1261 -0.0018 204  LYS   A N   
899   C  CA  . LYS   A 135 ? 1.2991 1.4208 1.3645 0.0052  -0.1227 -0.0002 204  LYS   A CA  
900   C  C   . LYS   A 135 ? 1.2835 1.4114 1.3494 0.0047  -0.1180 0.0040  204  LYS   A C   
901   O  O   . LYS   A 135 ? 1.1949 1.3261 1.2597 0.0060  -0.1148 0.0057  204  LYS   A O   
902   C  CB  . LYS   A 135 ? 1.2486 1.3633 1.3052 0.0120  -0.1243 -0.0015 204  LYS   A CB  
903   N  N   . CYS   A 136 ? 1.3918 1.5212 1.4596 0.0028  -0.1176 0.0056  205  CYS   A N   
904   C  CA  . CYS   A 136 ? 1.4282 1.5640 1.4979 0.0017  -0.1139 0.0092  205  CYS   A CA  
905   C  C   . CYS   A 136 ? 1.4763 1.6174 1.5527 -0.0047 -0.1132 0.0098  205  CYS   A C   
906   O  O   . CYS   A 136 ? 1.4448 1.5912 1.5232 -0.0060 -0.1108 0.0125  205  CYS   A O   
907   C  CB  . CYS   A 136 ? 1.3999 1.5328 1.4651 0.0056  -0.1139 0.0109  205  CYS   A CB  
908   S  SG  . CYS   A 136 ? 1.2770 1.4011 1.3324 0.0138  -0.1153 0.0100  205  CYS   A SG  
909   N  N   . GLN   A 137 ? 1.7045 1.8441 1.7845 -0.0084 -0.1152 0.0074  206  GLN   A N   
910   C  CA  . GLN   A 137 ? 1.7391 1.8823 1.8243 -0.0139 -0.1142 0.0080  206  GLN   A CA  
911   C  C   . GLN   A 137 ? 1.7630 1.9130 1.8516 -0.0169 -0.1115 0.0093  206  GLN   A C   
912   O  O   . GLN   A 137 ? 1.7847 1.9383 1.8757 -0.0202 -0.1100 0.0109  206  GLN   A O   
913   C  CB  . GLN   A 137 ? 1.7296 1.8691 1.8183 -0.0169 -0.1164 0.0052  206  GLN   A CB  
914   C  CG  . GLN   A 137 ? 1.7311 1.8646 1.8178 -0.0157 -0.1186 0.0046  206  GLN   A CG  
915   C  CD  . GLN   A 137 ? 1.8013 1.9352 1.8836 -0.0133 -0.1173 0.0077  206  GLN   A CD  
916   O  OE1 . GLN   A 137 ? 1.7779 1.9077 1.8550 -0.0086 -0.1186 0.0078  206  GLN   A OE1 
917   N  NE2 . GLN   A 137 ? 1.7184 1.8570 1.8026 -0.0163 -0.1148 0.0100  206  GLN   A NE2 
918   N  N   . ILE   A 138 ? 1.5144 1.6656 1.6028 -0.0155 -0.1110 0.0084  207  ILE   A N   
919   C  CA  . ILE   A 138 ? 1.4668 1.6240 1.5580 -0.0180 -0.1083 0.0098  207  ILE   A CA  
920   C  C   . ILE   A 138 ? 1.4662 1.6273 1.5566 -0.0164 -0.1062 0.0129  207  ILE   A C   
921   O  O   . ILE   A 138 ? 1.4420 1.6016 1.5288 -0.0118 -0.1056 0.0139  207  ILE   A O   
922   C  CB  . ILE   A 138 ? 1.3917 1.5485 1.4823 -0.0166 -0.1082 0.0082  207  ILE   A CB  
923   C  CG1 . ILE   A 138 ? 1.3297 1.4917 1.4244 -0.0209 -0.1063 0.0085  207  ILE   A CG1 
924   C  CG2 . ILE   A 138 ? 1.2811 1.4366 1.3667 -0.0113 -0.1069 0.0095  207  ILE   A CG2 
925   C  CD1 . ILE   A 138 ? 1.2363 1.3982 1.3352 -0.0254 -0.1073 0.0066  207  ILE   A CD1 
926   N  N   . PHE   A 139 ? 1.5118 1.6775 1.6054 -0.0199 -0.1051 0.0145  208  PHE   A N   
927   C  CA  . PHE   A 139 ? 1.4988 1.6684 1.5926 -0.0182 -0.1035 0.0172  208  PHE   A CA  
928   C  C   . PHE   A 139 ? 1.4918 1.6667 1.5888 -0.0193 -0.1013 0.0182  208  PHE   A C   
929   O  O   . PHE   A 139 ? 1.4785 1.6544 1.5773 -0.0224 -0.1010 0.0169  208  PHE   A O   
930   C  CB  . PHE   A 139 ? 1.4748 1.6460 1.5697 -0.0203 -0.1041 0.0186  208  PHE   A CB  
931   C  CG  . PHE   A 139 ? 1.5131 1.6793 1.6045 -0.0182 -0.1058 0.0186  208  PHE   A CG  
932   C  CD1 . PHE   A 139 ? 1.5175 1.6805 1.6053 -0.0131 -0.1061 0.0187  208  PHE   A CD1 
933   C  CD2 . PHE   A 139 ? 1.4736 1.6375 1.5645 -0.0209 -0.1068 0.0184  208  PHE   A CD2 
934   C  CE1 . PHE   A 139 ? 1.4722 1.6300 1.5563 -0.0110 -0.1078 0.0186  208  PHE   A CE1 
935   C  CE2 . PHE   A 139 ? 1.4172 1.5758 1.5047 -0.0189 -0.1082 0.0184  208  PHE   A CE2 
936   C  CZ  . PHE   A 139 ? 1.4521 1.6079 1.5364 -0.0141 -0.1089 0.0184  208  PHE   A CZ  
937   N  N   . PRO   A 140 ? 1.3842 1.5625 1.4822 -0.0168 -0.0994 0.0204  209  PRO   A N   
938   C  CA  . PRO   A 140 ? 1.4129 1.5966 1.5151 -0.0184 -0.0972 0.0215  209  PRO   A CA  
939   C  C   . PRO   A 140 ? 1.5501 1.7377 1.6561 -0.0232 -0.0981 0.0218  209  PRO   A C   
940   O  O   . PRO   A 140 ? 1.5520 1.7397 1.6578 -0.0239 -0.0997 0.0223  209  PRO   A O   
941   C  CB  . PRO   A 140 ? 1.3520 1.5382 1.4552 -0.0145 -0.0949 0.0240  209  PRO   A CB  
942   C  CG  . PRO   A 140 ? 1.2515 1.4325 1.3494 -0.0100 -0.0959 0.0238  209  PRO   A CG  
943   C  CD  . PRO   A 140 ? 1.3172 1.4946 1.4131 -0.0124 -0.0991 0.0220  209  PRO   A CD  
944   N  N   . SER   A 141 ? 1.6459 1.8360 1.7545 -0.0263 -0.0972 0.0213  210  SER   A N   
945   C  CA  . SER   A 141 ? 1.7126 1.9049 1.8234 -0.0308 -0.0983 0.0210  210  SER   A CA  
946   C  C   . SER   A 141 ? 1.7073 1.9023 1.8197 -0.0313 -0.0997 0.0226  210  SER   A C   
947   O  O   . SER   A 141 ? 1.6924 1.8919 1.8086 -0.0301 -0.0992 0.0243  210  SER   A O   
948   C  CB  . SER   A 141 ? 1.7468 1.9424 1.8608 -0.0332 -0.0968 0.0210  210  SER   A CB  
949   O  OG  . SER   A 141 ? 1.8182 2.0147 1.9331 -0.0373 -0.0980 0.0204  210  SER   A OG  
950   N  N   . SER   A 151 ? 1.4006 1.6003 1.5088 -0.0269 -0.1214 0.0292  220  SER   A N   
951   C  CA  . SER   A 151 ? 1.5042 1.7084 1.6173 -0.0230 -0.1222 0.0305  220  SER   A CA  
952   C  C   . SER   A 151 ? 1.5392 1.7379 1.6460 -0.0197 -0.1214 0.0312  220  SER   A C   
953   O  O   . SER   A 151 ? 1.4400 1.6356 1.5444 -0.0197 -0.1184 0.0310  220  SER   A O   
954   C  CB  . SER   A 151 ? 1.4715 1.6830 1.5941 -0.0227 -0.1195 0.0311  220  SER   A CB  
955   O  OG  . SER   A 151 ? 1.4673 1.6851 1.5974 -0.0196 -0.1207 0.0323  220  SER   A OG  
956   N  N   . TYR   A 152 ? 1.7059 1.9031 1.8100 -0.0169 -0.1244 0.0319  221  TYR   A N   
957   C  CA  . TYR   A 152 ? 1.6758 1.8674 1.7736 -0.0136 -0.1242 0.0326  221  TYR   A CA  
958   C  C   . TYR   A 152 ? 1.6603 1.8520 1.7594 -0.0116 -0.1208 0.0330  221  TYR   A C   
959   O  O   . TYR   A 152 ? 1.6456 1.8304 1.7382 -0.0115 -0.1193 0.0326  221  TYR   A O   
960   C  CB  . TYR   A 152 ? 1.7117 1.9056 1.8109 -0.0099 -0.1278 0.0336  221  TYR   A CB  
961   C  CG  . TYR   A 152 ? 1.7570 1.9444 1.8486 -0.0062 -0.1285 0.0343  221  TYR   A CG  
962   C  CD1 . TYR   A 152 ? 1.7638 1.9422 1.8465 -0.0070 -0.1266 0.0341  221  TYR   A CD1 
963   C  CD2 . TYR   A 152 ? 1.7927 1.9829 1.8866 -0.0020 -0.1313 0.0353  221  TYR   A CD2 
964   C  CE1 . TYR   A 152 ? 1.7740 1.9461 1.8499 -0.0037 -0.1273 0.0348  221  TYR   A CE1 
965   C  CE2 . TYR   A 152 ? 1.8326 2.0166 1.9192 0.0016  -0.1321 0.0360  221  TYR   A CE2 
966   C  CZ  . TYR   A 152 ? 1.8062 1.9809 1.8835 0.0007  -0.1300 0.0358  221  TYR   A CZ  
967   O  OH  . TYR   A 152 ? 1.8059 1.9738 1.8759 0.0041  -0.1307 0.0366  221  TYR   A OH  
968   N  N   . LYS   A 153 ? 1.4677 1.6667 1.5750 -0.0099 -0.1194 0.0337  222  LYS   A N   
969   C  CA  . LYS   A 153 ? 1.2981 1.4966 1.4057 -0.0071 -0.1163 0.0342  222  LYS   A CA  
970   C  C   . LYS   A 153 ? 1.2328 1.4270 1.3369 -0.0097 -0.1138 0.0329  222  LYS   A C   
971   O  O   . LYS   A 153 ? 1.2166 1.4055 1.3158 -0.0079 -0.1125 0.0326  222  LYS   A O   
972   C  CB  . LYS   A 153 ? 1.1619 1.3688 1.2791 -0.0050 -0.1145 0.0354  222  LYS   A CB  
973   N  N   . TRP   A 154 ? 1.2334 1.4297 1.3401 -0.0139 -0.1134 0.0320  223  TRP   A N   
974   C  CA  . TRP   A 154 ? 1.1168 1.3099 1.2213 -0.0161 -0.1112 0.0306  223  TRP   A CA  
975   C  C   . TRP   A 154 ? 1.1246 1.3094 1.2214 -0.0171 -0.1117 0.0296  223  TRP   A C   
976   O  O   . TRP   A 154 ? 1.1098 1.2905 1.2040 -0.0165 -0.1103 0.0287  223  TRP   A O   
977   C  CB  . TRP   A 154 ? 1.0807 1.2771 1.1888 -0.0204 -0.1108 0.0298  223  TRP   A CB  
978   C  CG  . TRP   A 154 ? 1.0085 1.2032 1.1161 -0.0218 -0.1083 0.0286  223  TRP   A CG  
979   C  CD1 . TRP   A 154 ? 1.0390 1.2369 1.1504 -0.0206 -0.1059 0.0288  223  TRP   A CD1 
980   C  CD2 . TRP   A 154 ? 0.9173 1.1064 1.0203 -0.0244 -0.1080 0.0270  223  TRP   A CD2 
981   N  NE1 . TRP   A 154 ? 1.0419 1.2363 1.1508 -0.0221 -0.1046 0.0273  223  TRP   A NE1 
982   C  CE2 . TRP   A 154 ? 0.8767 1.0662 0.9812 -0.0245 -0.1059 0.0261  223  TRP   A CE2 
983   C  CE3 . TRP   A 154 ? 0.9684 1.1520 1.0664 -0.0265 -0.1090 0.0263  223  TRP   A CE3 
984   C  CZ2 . TRP   A 154 ? 0.9798 1.1651 1.0818 -0.0267 -0.1053 0.0242  223  TRP   A CZ2 
985   C  CZ3 . TRP   A 154 ? 0.9967 1.1763 1.0928 -0.0288 -0.1079 0.0247  223  TRP   A CZ3 
986   C  CH2 . TRP   A 154 ? 1.0031 1.1839 1.1017 -0.0289 -0.1063 0.0236  223  TRP   A CH2 
987   N  N   . TRP   A 155 ? 1.1631 1.3449 1.2561 -0.0184 -0.1137 0.0297  224  TRP   A N   
988   C  CA  . TRP   A 155 ? 1.1016 1.2752 1.1878 -0.0195 -0.1135 0.0290  224  TRP   A CA  
989   C  C   . TRP   A 155 ? 1.0240 1.1930 1.1061 -0.0157 -0.1140 0.0296  224  TRP   A C   
990   O  O   . TRP   A 155 ? 0.9712 1.1336 1.0491 -0.0162 -0.1133 0.0289  224  TRP   A O   
991   C  CB  . TRP   A 155 ? 1.0393 1.2101 1.1217 -0.0220 -0.1149 0.0291  224  TRP   A CB  
992   C  CG  . TRP   A 155 ? 1.0319 1.2045 1.1162 -0.0262 -0.1140 0.0280  224  TRP   A CG  
993   C  CD1 . TRP   A 155 ? 1.0450 1.2232 1.1335 -0.0275 -0.1151 0.0280  224  TRP   A CD1 
994   C  CD2 . TRP   A 155 ? 1.0018 1.1704 1.0845 -0.0294 -0.1119 0.0268  224  TRP   A CD2 
995   N  NE1 . TRP   A 155 ? 0.9537 1.1312 1.0421 -0.0313 -0.1138 0.0269  224  TRP   A NE1 
996   C  CE2 . TRP   A 155 ? 0.9223 1.0942 1.0075 -0.0324 -0.1116 0.0261  224  TRP   A CE2 
997   C  CE3 . TRP   A 155 ? 0.9595 1.1221 1.0395 -0.0300 -0.1102 0.0260  224  TRP   A CE3 
998   C  CZ2 . TRP   A 155 ? 0.9528 1.1223 1.0374 -0.0357 -0.1096 0.0249  224  TRP   A CZ2 
999   C  CZ3 . TRP   A 155 ? 0.9255 1.0863 1.0060 -0.0336 -0.1083 0.0247  224  TRP   A CZ3 
1000  C  CH2 . TRP   A 155 ? 0.9966 1.1608 1.0792 -0.0362 -0.1079 0.0242  224  TRP   A CH2 
1001  N  N   . GLN   A 156 ? 1.0415 1.2138 1.1252 -0.0118 -0.1151 0.0310  225  GLN   A N   
1002  C  CA  . GLN   A 156 ? 1.0794 1.2475 1.1594 -0.0077 -0.1151 0.0315  225  GLN   A CA  
1003  C  C   . GLN   A 156 ? 1.0949 1.2616 1.1754 -0.0067 -0.1132 0.0305  225  GLN   A C   
1004  O  O   . GLN   A 156 ? 1.0402 1.1998 1.1158 -0.0059 -0.1132 0.0297  225  GLN   A O   
1005  C  CB  . GLN   A 156 ? 1.1300 1.3027 1.2125 -0.0035 -0.1164 0.0331  225  GLN   A CB  
1006  C  CG  . GLN   A 156 ? 1.2450 1.4136 1.3223 -0.0019 -0.1189 0.0339  225  GLN   A CG  
1007  C  CD  . GLN   A 156 ? 1.4036 1.5782 1.4851 0.0017  -0.1208 0.0353  225  GLN   A CD  
1008  O  OE1 . GLN   A 156 ? 1.5060 1.6864 1.5924 0.0003  -0.1224 0.0355  225  GLN   A OE1 
1009  N  NE2 . GLN   A 156 ? 1.3890 1.5623 1.4690 0.0064  -0.1207 0.0363  225  GLN   A NE2 
1010  N  N   . LYS   A 157 ? 1.0681 1.2407 1.1540 -0.0067 -0.1116 0.0305  226  LYS   A N   
1011  C  CA  . LYS   A 157 ? 0.9542 1.1247 1.0395 -0.0054 -0.1099 0.0294  226  LYS   A CA  
1012  C  C   . LYS   A 157 ? 0.9556 1.1213 1.0389 -0.0093 -0.1099 0.0273  226  LYS   A C   
1013  O  O   . LYS   A 157 ? 0.9690 1.1289 1.0488 -0.0081 -0.1101 0.0261  226  LYS   A O   
1014  C  CB  . LYS   A 157 ? 0.9209 1.0983 1.0120 -0.0045 -0.1078 0.0300  226  LYS   A CB  
1015  N  N   . TYR   A 158 ? 1.0119 1.1797 1.0973 -0.0138 -0.1099 0.0269  227  TYR   A N   
1016  C  CA  . TYR   A 158 ? 0.9978 1.1615 1.0822 -0.0175 -0.1095 0.0250  227  TYR   A CA  
1017  C  C   . TYR   A 158 ? 0.9675 1.1232 1.0472 -0.0170 -0.1104 0.0243  227  TYR   A C   
1018  O  O   . TYR   A 158 ? 0.9428 1.0946 1.0222 -0.0176 -0.1103 0.0225  227  TYR   A O   
1019  C  CB  . TYR   A 158 ? 0.9326 1.0982 1.0183 -0.0219 -0.1094 0.0250  227  TYR   A CB  
1020  C  CG  . TYR   A 158 ? 0.8962 1.0574 0.9811 -0.0257 -0.1086 0.0234  227  TYR   A CG  
1021  C  CD1 . TYR   A 158 ? 0.9556 1.1187 1.0438 -0.0278 -0.1075 0.0218  227  TYR   A CD1 
1022  C  CD2 . TYR   A 158 ? 0.9191 1.0743 1.0001 -0.0271 -0.1086 0.0235  227  TYR   A CD2 
1023  C  CE1 . TYR   A 158 ? 0.9700 1.1296 1.0586 -0.0312 -0.1066 0.0202  227  TYR   A CE1 
1024  C  CE2 . TYR   A 158 ? 0.9290 1.0805 1.0103 -0.0307 -0.1073 0.0222  227  TYR   A CE2 
1025  C  CZ  . TYR   A 158 ? 0.9681 1.1222 1.0537 -0.0327 -0.1064 0.0205  227  TYR   A CZ  
1026  O  OH  . TYR   A 158 ? 1.0064 1.1572 1.0934 -0.0361 -0.1050 0.0192  227  TYR   A OH  
1027  N  N   . GLN   A 159 ? 0.9282 1.0811 1.0043 -0.0159 -0.1113 0.0256  228  GLN   A N   
1028  C  CA  . GLN   A 159 ? 0.9207 1.0655 0.9923 -0.0158 -0.1119 0.0252  228  GLN   A CA  
1029  C  C   . GLN   A 159 ? 0.9812 1.1225 1.0506 -0.0116 -0.1127 0.0247  228  GLN   A C   
1030  O  O   . GLN   A 159 ? 0.9776 1.1130 1.0457 -0.0121 -0.1132 0.0231  228  GLN   A O   
1031  C  CB  . GLN   A 159 ? 0.8852 1.0274 0.9526 -0.0158 -0.1125 0.0268  228  GLN   A CB  
1032  C  CG  . GLN   A 159 ? 0.8715 1.0051 0.9333 -0.0143 -0.1131 0.0271  228  GLN   A CG  
1033  C  CD  . GLN   A 159 ? 0.8749 1.0067 0.9318 -0.0124 -0.1142 0.0291  228  GLN   A CD  
1034  O  OE1 . GLN   A 159 ? 0.9793 1.1122 1.0348 -0.0081 -0.1156 0.0301  228  GLN   A OE1 
1035  N  NE2 . GLN   A 159 ? 0.8634 0.9919 0.9174 -0.0152 -0.1136 0.0296  228  GLN   A NE2 
1036  N  N   . LYS   A 160 ? 0.9593 1.1043 1.0287 -0.0074 -0.1130 0.0260  229  LYS   A N   
1037  C  CA  . LYS   A 160 ? 0.9107 1.0523 0.9773 -0.0027 -0.1135 0.0256  229  LYS   A CA  
1038  C  C   . LYS   A 160 ? 0.9380 1.0781 1.0056 -0.0029 -0.1133 0.0235  229  LYS   A C   
1039  O  O   . LYS   A 160 ? 1.0611 1.1955 1.1250 0.0003  -0.1143 0.0225  229  LYS   A O   
1040  C  CB  . LYS   A 160 ? 0.9529 1.0998 1.0205 0.0017  -0.1129 0.0276  229  LYS   A CB  
1041  C  CG  . LYS   A 160 ? 1.0589 1.2018 1.1224 0.0073  -0.1131 0.0277  229  LYS   A CG  
1042  C  CD  . LYS   A 160 ? 1.1562 1.2974 1.2164 0.0106  -0.1141 0.0295  229  LYS   A CD  
1043  C  CE  . LYS   A 160 ? 1.1984 1.3356 1.2543 0.0165  -0.1141 0.0296  229  LYS   A CE  
1044  N  NZ  . LYS   A 160 ? 1.2079 1.3362 1.2590 0.0164  -0.1154 0.0273  229  LYS   A NZ  
1045  N  N   . ARG   A 161 ? 0.9409 1.0853 1.0129 -0.0062 -0.1122 0.0226  230  ARG   A N   
1046  C  CA  . ARG   A 161 ? 0.9437 1.0868 1.0164 -0.0059 -0.1123 0.0206  230  ARG   A CA  
1047  C  C   . ARG   A 161 ? 1.0031 1.1427 1.0776 -0.0102 -0.1131 0.0182  230  ARG   A C   
1048  O  O   . ARG   A 161 ? 1.0644 1.1996 1.1380 -0.0091 -0.1145 0.0160  230  ARG   A O   
1049  C  CB  . ARG   A 161 ? 0.9364 1.0867 1.0128 -0.0059 -0.1103 0.0212  230  ARG   A CB  
1050  N  N   . LYS   A 162 ? 1.0108 1.1521 1.0878 -0.0147 -0.1123 0.0186  231  LYS   A N   
1051  C  CA  . LYS   A 162 ? 1.0103 1.1487 1.0899 -0.0189 -0.1124 0.0166  231  LYS   A CA  
1052  C  C   . LYS   A 162 ? 0.9379 1.0687 1.0155 -0.0191 -0.1136 0.0158  231  LYS   A C   
1053  O  O   . LYS   A 162 ? 0.9324 1.0599 1.0130 -0.0216 -0.1142 0.0136  231  LYS   A O   
1054  C  CB  . LYS   A 162 ? 0.9422 1.0844 1.0247 -0.0235 -0.1105 0.0174  231  LYS   A CB  
1055  C  CG  . LYS   A 162 ? 0.8827 1.0219 0.9684 -0.0278 -0.1099 0.0155  231  LYS   A CG  
1056  C  CD  . LYS   A 162 ? 0.8979 1.0400 0.9857 -0.0320 -0.1077 0.0161  231  LYS   A CD  
1057  C  CE  . LYS   A 162 ? 0.9892 1.1288 1.0815 -0.0357 -0.1068 0.0141  231  LYS   A CE  
1058  N  NZ  . LYS   A 162 ? 1.1005 1.2448 1.1966 -0.0387 -0.1051 0.0135  231  LYS   A NZ  
1059  N  N   . PHE   A 163 ? 0.9481 1.0759 1.0213 -0.0167 -0.1141 0.0174  232  PHE   A N   
1060  C  CA  . PHE   A 163 ? 0.9844 1.1043 1.0552 -0.0171 -0.1150 0.0170  232  PHE   A CA  
1061  C  C   . PHE   A 163 ? 1.0172 1.1326 1.0833 -0.0120 -0.1171 0.0168  232  PHE   A C   
1062  O  O   . PHE   A 163 ? 1.0288 1.1379 1.0913 -0.0112 -0.1178 0.0173  232  PHE   A O   
1063  C  CB  . PHE   A 163 ? 0.9445 1.0631 1.0129 -0.0190 -0.1135 0.0192  232  PHE   A CB  
1064  C  CG  . PHE   A 163 ? 0.9208 1.0433 0.9924 -0.0234 -0.1113 0.0196  232  PHE   A CG  
1065  C  CD1 . PHE   A 163 ? 0.9005 1.0214 0.9765 -0.0276 -0.1101 0.0179  232  PHE   A CD1 
1066  C  CD2 . PHE   A 163 ? 0.8924 1.0202 0.9629 -0.0232 -0.1106 0.0215  232  PHE   A CD2 
1067  C  CE1 . PHE   A 163 ? 0.9199 1.0439 0.9983 -0.0313 -0.1079 0.0184  232  PHE   A CE1 
1068  C  CE2 . PHE   A 163 ? 0.8866 1.0172 0.9590 -0.0269 -0.1088 0.0218  232  PHE   A CE2 
1069  C  CZ  . PHE   A 163 ? 0.9234 1.0519 0.9993 -0.0309 -0.1072 0.0203  232  PHE   A CZ  
1070  N  N   . HIS   A 164 ? 1.0198 1.1376 1.0851 -0.0082 -0.1178 0.0163  233  HIS   A N   
1071  C  CA  . HIS   A 164 ? 1.0361 1.1491 1.0961 -0.0028 -0.1196 0.0161  233  HIS   A CA  
1072  C  C   . HIS   A 164 ? 1.0257 1.1298 1.0844 -0.0032 -0.1221 0.0137  233  HIS   A C   
1073  O  O   . HIS   A 164 ? 0.9649 1.0629 1.0186 -0.0004 -0.1234 0.0142  233  HIS   A O   
1074  C  CB  . HIS   A 164 ? 0.9700 1.0860 1.0293 0.0010  -0.1196 0.0155  233  HIS   A CB  
1075  C  CG  . HIS   A 164 ? 0.9491 1.0591 1.0021 0.0070  -0.1213 0.0150  233  HIS   A CG  
1076  N  ND1 . HIS   A 164 ? 0.9754 1.0799 1.0262 0.0091  -0.1237 0.0123  233  HIS   A ND1 
1077  C  CD2 . HIS   A 164 ? 0.9776 1.0858 1.0255 0.0117  -0.1211 0.0169  233  HIS   A CD2 
1078  C  CE1 . HIS   A 164 ? 1.0550 1.1542 1.0991 0.0149  -0.1248 0.0124  233  HIS   A CE1 
1079  N  NE2 . HIS   A 164 ? 0.9918 1.0932 1.0341 0.0165  -0.1230 0.0153  233  HIS   A NE2 
1080  N  N   . CYS   A 165 ? 1.0079 1.1110 1.0716 -0.0070 -0.1229 0.0113  234  CYS   A N   
1081  C  CA  . CYS   A 165 ? 0.9772 1.0722 1.0415 -0.0078 -0.1256 0.0088  234  CYS   A CA  
1082  C  C   . CYS   A 165 ? 0.9102 1.0009 0.9749 -0.0112 -0.1245 0.0099  234  CYS   A C   
1083  O  O   . CYS   A 165 ? 0.9360 1.0210 1.0039 -0.0136 -0.1259 0.0079  234  CYS   A O   
1084  C  CB  . CYS   A 165 ? 1.0848 1.1806 1.1554 -0.0106 -0.1270 0.0056  234  CYS   A CB  
1085  S  SG  . CYS   A 165 ? 1.0731 1.1672 1.1403 -0.0051 -0.1303 0.0030  234  CYS   A SG  
1086  N  N   . ALA   A 166 ? 0.9400 1.0332 1.0020 -0.0114 -0.1220 0.0129  235  ALA   A N   
1087  C  CA  . ALA   A 166 ? 0.9409 1.0285 1.0013 -0.0136 -0.1209 0.0142  235  ALA   A CA  
1088  C  C   . ALA   A 166 ? 0.9717 1.0508 1.0263 -0.0099 -0.1233 0.0139  235  ALA   A C   
1089  O  O   . ALA   A 166 ? 0.9125 0.9845 0.9666 -0.0119 -0.1232 0.0139  235  ALA   A O   
1090  C  CB  . ALA   A 166 ? 0.9083 1.0002 0.9662 -0.0141 -0.1182 0.0174  235  ALA   A CB  
1091  N  N   . ASN   A 167 ? 0.9503 1.0296 1.0004 -0.0044 -0.1253 0.0137  236  ASN   A N   
1092  C  CA  . ASN   A 167 ? 0.9378 1.0089 0.9819 -0.0002 -0.1278 0.0132  236  ASN   A CA  
1093  C  C   . ASN   A 167 ? 0.9136 0.9770 0.9603 -0.0020 -0.1306 0.0100  236  ASN   A C   
1094  O  O   . ASN   A 167 ? 0.9667 1.0216 1.0092 -0.0002 -0.1325 0.0095  236  ASN   A O   
1095  C  CB  . ASN   A 167 ? 0.9524 1.0254 0.9914 0.0062  -0.1288 0.0135  236  ASN   A CB  
1096  C  CG  . ASN   A 167 ? 1.1105 1.1888 1.1464 0.0088  -0.1265 0.0169  236  ASN   A CG  
1097  O  OD1 . ASN   A 167 ? 1.0898 1.1637 1.1206 0.0109  -0.1266 0.0186  236  ASN   A OD1 
1098  N  ND2 . ASN   A 167 ? 1.1559 1.2434 1.1950 0.0087  -0.1246 0.0180  236  ASN   A ND2 
1099  N  N   . LEU   A 168 ? 0.8634 0.9295 0.9173 -0.0055 -0.1312 0.0076  237  LEU   A N   
1100  C  CA  . LEU   A 168 ? 0.9256 0.9847 0.9837 -0.0076 -0.1342 0.0043  237  LEU   A CA  
1101  C  C   . LEU   A 168 ? 0.9137 0.9697 0.9771 -0.0134 -0.1321 0.0048  237  LEU   A C   
1102  O  O   . LEU   A 168 ? 0.9251 0.9752 0.9934 -0.0158 -0.1343 0.0022  237  LEU   A O   
1103  C  CB  . LEU   A 168 ? 0.9170 0.9799 0.9812 -0.0087 -0.1361 0.0012  237  LEU   A CB  
1104  C  CG  . LEU   A 168 ? 0.8633 0.9304 0.9230 -0.0037 -0.1370 0.0010  237  LEU   A CG  
1105  C  CD1 . LEU   A 168 ? 0.9467 1.0173 1.0130 -0.0055 -0.1385 -0.0018 237  LEU   A CD1 
1106  C  CD2 . LEU   A 168 ? 0.8156 0.8752 0.8669 0.0026  -0.1405 0.0000  237  LEU   A CD2 
1107  N  N   . THR   A 169 ? 0.8729 0.9323 0.9357 -0.0157 -0.1278 0.0080  238  THR   A N   
1108  C  CA  . THR   A 169 ? 0.9643 1.0199 1.0311 -0.0209 -0.1250 0.0088  238  THR   A CA  
1109  C  C   . THR   A 169 ? 0.9605 1.0103 1.0192 -0.0192 -0.1235 0.0117  238  THR   A C   
1110  O  O   . THR   A 169 ? 0.9384 0.9873 0.9892 -0.0140 -0.1251 0.0128  238  THR   A O   
1111  C  CB  . THR   A 169 ? 0.9777 1.0405 1.0501 -0.0255 -0.1210 0.0099  238  THR   A CB  
1112  O  OG1 . THR   A 169 ? 0.9748 1.0433 1.0413 -0.0232 -0.1191 0.0128  238  THR   A OG1 
1113  C  CG2 . THR   A 169 ? 0.8523 0.9204 0.9330 -0.0273 -0.1224 0.0070  238  THR   A CG2 
1114  N  N   . SER   A 170 ? 0.9165 0.9623 0.9771 -0.0234 -0.1202 0.0131  239  SER   A N   
1115  C  CA  . SER   A 170 ? 0.9599 0.9987 1.0125 -0.0221 -0.1186 0.0158  239  SER   A CA  
1116  C  C   . SER   A 170 ? 0.9749 1.0181 1.0226 -0.0218 -0.1152 0.0192  239  SER   A C   
1117  O  O   . SER   A 170 ? 1.0335 1.0706 1.0749 -0.0215 -0.1132 0.0216  239  SER   A O   
1118  C  CB  . SER   A 170 ? 1.0406 1.0704 1.0971 -0.0263 -0.1170 0.0153  239  SER   A CB  
1119  O  OG  . SER   A 170 ? 1.0238 1.0559 1.0869 -0.0318 -0.1125 0.0161  239  SER   A OG  
1120  N  N   . TRP   A 171 ? 1.0056 1.0585 1.0556 -0.0218 -0.1147 0.0193  240  TRP   A N   
1121  C  CA  . TRP   A 171 ? 0.9233 0.9810 0.9695 -0.0217 -0.1121 0.0221  240  TRP   A CA  
1122  C  C   . TRP   A 171 ? 0.9691 1.0353 1.0134 -0.0176 -0.1141 0.0224  240  TRP   A C   
1123  O  O   . TRP   A 171 ? 0.9205 0.9904 0.9680 -0.0159 -0.1165 0.0204  240  TRP   A O   
1124  C  CB  . TRP   A 171 ? 0.9460 1.0073 0.9982 -0.0270 -0.1086 0.0221  240  TRP   A CB  
1125  C  CG  . TRP   A 171 ? 0.9478 1.0010 1.0021 -0.0311 -0.1055 0.0224  240  TRP   A CG  
1126  C  CD1 . TRP   A 171 ? 0.9298 0.9825 0.9934 -0.0357 -0.1040 0.0205  240  TRP   A CD1 
1127  C  CD2 . TRP   A 171 ? 1.0098 1.0542 1.0570 -0.0310 -0.1032 0.0249  240  TRP   A CD2 
1128  N  NE1 . TRP   A 171 ? 0.9503 0.9945 1.0138 -0.0387 -0.1005 0.0218  240  TRP   A NE1 
1129  C  CE2 . TRP   A 171 ? 1.0178 1.0564 1.0706 -0.0357 -0.0998 0.0245  240  TRP   A CE2 
1130  C  CE3 . TRP   A 171 ? 1.0486 1.0893 1.0853 -0.0271 -0.1035 0.0274  240  TRP   A CE3 
1131  C  CZ2 . TRP   A 171 ? 1.1190 1.1477 1.1666 -0.0368 -0.0964 0.0267  240  TRP   A CZ2 
1132  C  CZ3 . TRP   A 171 ? 1.0769 1.1077 1.1079 -0.0278 -0.1007 0.0294  240  TRP   A CZ3 
1133  C  CH2 . TRP   A 171 ? 1.1653 1.1899 1.2015 -0.0327 -0.0969 0.0292  240  TRP   A CH2 
1134  N  N   . PRO   A 172 ? 1.0032 1.0726 1.0426 -0.0159 -0.1132 0.0249  241  PRO   A N   
1135  C  CA  . PRO   A 172 ? 0.9803 1.0579 1.0188 -0.0120 -0.1148 0.0255  241  PRO   A CA  
1136  C  C   . PRO   A 172 ? 0.9502 1.0369 0.9941 -0.0147 -0.1135 0.0253  241  PRO   A C   
1137  O  O   . PRO   A 172 ? 0.9737 1.0599 1.0202 -0.0191 -0.1112 0.0252  241  PRO   A O   
1138  C  CB  . PRO   A 172 ? 1.0136 1.0889 1.0445 -0.0089 -0.1149 0.0281  241  PRO   A CB  
1139  C  CG  . PRO   A 172 ? 0.9719 1.0416 1.0008 -0.0129 -0.1120 0.0292  241  PRO   A CG  
1140  C  CD  . PRO   A 172 ? 0.9486 1.0128 0.9823 -0.0168 -0.1108 0.0274  241  PRO   A CD  
1141  N  N   . ARG   A 173 ? 0.9373 1.0318 0.9826 -0.0118 -0.1148 0.0253  242  ARG   A N   
1142  C  CA  . ARG   A 173 ? 0.9214 1.0245 0.9722 -0.0141 -0.1138 0.0249  242  ARG   A CA  
1143  C  C   . ARG   A 173 ? 0.9501 1.0546 0.9998 -0.0170 -0.1120 0.0265  242  ARG   A C   
1144  O  O   . ARG   A 173 ? 0.9126 1.0189 0.9660 -0.0211 -0.1102 0.0257  242  ARG   A O   
1145  C  CB  . ARG   A 173 ? 0.9088 1.0194 0.9606 -0.0101 -0.1151 0.0252  242  ARG   A CB  
1146  C  CG  . ARG   A 173 ? 0.9850 1.0954 1.0385 -0.0078 -0.1163 0.0234  242  ARG   A CG  
1147  C  CD  . ARG   A 173 ? 1.0523 1.1704 1.1073 -0.0042 -0.1164 0.0240  242  ARG   A CD  
1148  N  NE  . ARG   A 173 ? 1.0651 1.1822 1.1158 0.0013  -0.1173 0.0255  242  ARG   A NE  
1149  C  CZ  . ARG   A 173 ? 1.1644 1.2855 1.2143 0.0032  -0.1172 0.0276  242  ARG   A CZ  
1150  N  NH1 . ARG   A 173 ? 1.0372 1.1635 1.0899 0.0003  -0.1165 0.0286  242  ARG   A NH1 
1151  N  NH2 . ARG   A 173 ? 1.1630 1.2826 1.2093 0.0084  -0.1180 0.0288  242  ARG   A NH2 
1152  N  N   . TRP   A 174 ? 0.9344 1.0379 0.9786 -0.0145 -0.1126 0.0285  243  TRP   A N   
1153  C  CA  . TRP   A 174 ? 0.8648 0.9687 0.9064 -0.0163 -0.1115 0.0299  243  TRP   A CA  
1154  C  C   . TRP   A 174 ? 0.9674 1.0644 1.0078 -0.0207 -0.1086 0.0299  243  TRP   A C   
1155  O  O   . TRP   A 174 ? 0.9800 1.0782 1.0200 -0.0233 -0.1070 0.0304  243  TRP   A O   
1156  C  CB  . TRP   A 174 ? 0.9684 1.0704 1.0034 -0.0124 -0.1132 0.0319  243  TRP   A CB  
1157  C  CG  . TRP   A 174 ? 1.0512 1.1438 1.0800 -0.0100 -0.1135 0.0326  243  TRP   A CG  
1158  C  CD1 . TRP   A 174 ? 1.0557 1.1468 1.0837 -0.0062 -0.1152 0.0323  243  TRP   A CD1 
1159  C  CD2 . TRP   A 174 ? 1.0529 1.1358 1.0749 -0.0111 -0.1120 0.0338  243  TRP   A CD2 
1160  N  NE1 . TRP   A 174 ? 0.9691 1.0503 0.9904 -0.0050 -0.1151 0.0331  243  TRP   A NE1 
1161  C  CE2 . TRP   A 174 ? 1.0268 1.1027 1.0445 -0.0081 -0.1129 0.0341  243  TRP   A CE2 
1162  C  CE3 . TRP   A 174 ? 1.0436 1.1223 1.0621 -0.0141 -0.1096 0.0347  243  TRP   A CE3 
1163  C  CZ2 . TRP   A 174 ? 0.9895 1.0546 0.9999 -0.0082 -0.1116 0.0353  243  TRP   A CZ2 
1164  C  CZ3 . TRP   A 174 ? 1.0922 1.1599 1.1031 -0.0141 -0.1079 0.0361  243  TRP   A CZ3 
1165  C  CH2 . TRP   A 174 ? 0.9882 1.0493 0.9954 -0.0113 -0.1089 0.0364  243  TRP   A CH2 
1166  N  N   . LEU   A 175 ? 0.9822 1.0717 1.0221 -0.0215 -0.1077 0.0293  244  LEU   A N   
1167  C  CA  . LEU   A 175 ? 1.0064 1.0900 1.0469 -0.0259 -0.1043 0.0293  244  LEU   A CA  
1168  C  C   . LEU   A 175 ? 0.9601 1.0495 1.0087 -0.0298 -0.1029 0.0275  244  LEU   A C   
1169  O  O   . LEU   A 175 ? 0.9588 1.0482 1.0076 -0.0328 -0.1001 0.0280  244  LEU   A O   
1170  C  CB  . LEU   A 175 ? 0.9414 1.0160 0.9815 -0.0265 -0.1036 0.0288  244  LEU   A CB  
1171  C  CG  . LEU   A 175 ? 0.9210 0.9906 0.9634 -0.0314 -0.0993 0.0289  244  LEU   A CG  
1172  C  CD1 . LEU   A 175 ? 1.0007 1.0681 1.0365 -0.0320 -0.0966 0.0312  244  LEU   A CD1 
1173  C  CD2 . LEU   A 175 ? 0.9682 1.0282 1.0105 -0.0325 -0.0981 0.0288  244  LEU   A CD2 
1174  N  N   . TYR   A 176 ? 0.9222 1.0163 0.9769 -0.0293 -0.1048 0.0254  245  TYR   A N   
1175  C  CA  . TYR   A 176 ? 0.9528 1.0522 1.0151 -0.0325 -0.1039 0.0235  245  TYR   A CA  
1176  C  C   . TYR   A 176 ? 0.9966 1.1029 1.0589 -0.0333 -0.1032 0.0243  245  TYR   A C   
1177  O  O   . TYR   A 176 ? 1.0165 1.1250 1.0829 -0.0368 -0.1010 0.0236  245  TYR   A O   
1178  C  CB  . TYR   A 176 ? 0.9295 1.0320 0.9965 -0.0308 -0.1066 0.0212  245  TYR   A CB  
1179  C  CG  . TYR   A 176 ? 0.8749 0.9703 0.9436 -0.0311 -0.1075 0.0197  245  TYR   A CG  
1180  C  CD1 . TYR   A 176 ? 0.8840 0.9763 0.9587 -0.0354 -0.1056 0.0183  245  TYR   A CD1 
1181  C  CD2 . TYR   A 176 ? 0.8946 0.9864 0.9595 -0.0271 -0.1103 0.0195  245  TYR   A CD2 
1182  C  CE1 . TYR   A 176 ? 0.8735 0.9594 0.9509 -0.0359 -0.1068 0.0167  245  TYR   A CE1 
1183  C  CE2 . TYR   A 176 ? 0.9215 1.0062 0.9879 -0.0274 -0.1116 0.0178  245  TYR   A CE2 
1184  C  CZ  . TYR   A 176 ? 0.9284 1.0103 1.0014 -0.0319 -0.1100 0.0164  245  TYR   A CZ  
1185  O  OH  . TYR   A 176 ? 0.9630 1.0379 1.0386 -0.0325 -0.1116 0.0146  245  TYR   A OH  
1186  N  N   . SER   A 177 ? 0.9431 1.0528 1.0012 -0.0301 -0.1050 0.0257  246  SER   A N   
1187  C  CA  . SER   A 177 ? 0.9362 1.0520 0.9945 -0.0310 -0.1047 0.0263  246  SER   A CA  
1188  C  C   . SER   A 177 ? 0.9507 1.0619 1.0050 -0.0337 -0.1020 0.0275  246  SER   A C   
1189  O  O   . SER   A 177 ? 0.9905 1.1053 1.0463 -0.0358 -0.1009 0.0273  246  SER   A O   
1190  C  CB  . SER   A 177 ? 0.9138 1.0339 0.9693 -0.0271 -0.1074 0.0276  246  SER   A CB  
1191  O  OG  . SER   A 177 ? 0.8900 1.0122 0.9473 -0.0237 -0.1093 0.0271  246  SER   A OG  
1192  N  N   . LEU   A 178 ? 0.9680 1.0705 1.0166 -0.0334 -0.1006 0.0288  247  LEU   A N   
1193  C  CA  . LEU   A 178 ? 0.9635 1.0605 1.0070 -0.0355 -0.0975 0.0301  247  LEU   A CA  
1194  C  C   . LEU   A 178 ? 0.9910 1.0868 1.0399 -0.0400 -0.0936 0.0291  247  LEU   A C   
1195  O  O   . LEU   A 178 ? 1.0176 1.1088 1.0626 -0.0419 -0.0902 0.0302  247  LEU   A O   
1196  C  CB  . LEU   A 178 ? 0.9840 1.0711 1.0190 -0.0338 -0.0967 0.0320  247  LEU   A CB  
1197  C  CG  . LEU   A 178 ? 1.0489 1.1358 1.0777 -0.0291 -0.1004 0.0332  247  LEU   A CG  
1198  C  CD1 . LEU   A 178 ? 1.0667 1.1423 1.0864 -0.0278 -0.0988 0.0351  247  LEU   A CD1 
1199  C  CD2 . LEU   A 178 ? 1.0025 1.0956 1.0294 -0.0276 -0.1028 0.0336  247  LEU   A CD2 
1200  N  N   . TYR   A 179 ? 0.9461 1.0455 1.0037 -0.0414 -0.0940 0.0269  248  TYR   A N   
1201  C  CA  . TYR   A 179 ? 0.9632 1.0627 1.0278 -0.0455 -0.0908 0.0256  248  TYR   A CA  
1202  C  C   . TYR   A 179 ? 0.9847 1.0932 1.0566 -0.0462 -0.0925 0.0235  248  TYR   A C   
1203  O  O   . TYR   A 179 ? 1.0092 1.1190 1.0884 -0.0490 -0.0910 0.0217  248  TYR   A O   
1204  C  CB  . TYR   A 179 ? 0.9821 1.0761 1.0512 -0.0470 -0.0896 0.0247  248  TYR   A CB  
1205  C  CG  . TYR   A 179 ? 0.9899 1.0739 1.0529 -0.0473 -0.0866 0.0268  248  TYR   A CG  
1206  C  CD1 . TYR   A 179 ? 0.9649 1.0440 1.0214 -0.0441 -0.0887 0.0279  248  TYR   A CD1 
1207  C  CD2 . TYR   A 179 ? 1.0616 1.1405 1.1250 -0.0506 -0.0813 0.0278  248  TYR   A CD2 
1208  C  CE1 . TYR   A 179 ? 1.0616 1.1309 1.1119 -0.0442 -0.0858 0.0300  248  TYR   A CE1 
1209  C  CE2 . TYR   A 179 ? 1.0498 1.1187 1.1070 -0.0507 -0.0779 0.0300  248  TYR   A CE2 
1210  C  CZ  . TYR   A 179 ? 1.0861 1.1500 1.1365 -0.0475 -0.0803 0.0311  248  TYR   A CZ  
1211  O  OH  . TYR   A 179 ? 1.1856 1.2388 1.2290 -0.0475 -0.0769 0.0334  248  TYR   A OH  
1212  N  N   . ASP   A 180 ? 0.9551 1.0697 1.0254 -0.0436 -0.0956 0.0236  249  ASP   A N   
1213  C  CA  . ASP   A 180 ? 1.0173 1.1398 1.0936 -0.0438 -0.0972 0.0218  249  ASP   A CA  
1214  C  C   . ASP   A 180 ? 0.9837 1.1100 1.0593 -0.0455 -0.0959 0.0222  249  ASP   A C   
1215  O  O   . ASP   A 180 ? 0.9794 1.1077 1.0503 -0.0438 -0.0972 0.0235  249  ASP   A O   
1216  C  CB  . ASP   A 180 ? 0.9975 1.1242 1.0732 -0.0399 -0.1008 0.0217  249  ASP   A CB  
1217  C  CG  . ASP   A 180 ? 0.9939 1.1276 1.0751 -0.0399 -0.1019 0.0200  249  ASP   A CG  
1218  O  OD1 . ASP   A 180 ? 1.0293 1.1628 1.1157 -0.0412 -0.1017 0.0180  249  ASP   A OD1 
1219  O  OD2 . ASP   A 180 ? 0.9597 1.0989 1.0403 -0.0387 -0.1028 0.0207  249  ASP   A OD2 
1220  N  N   . ALA   A 181 ? 0.9867 1.1141 1.0673 -0.0486 -0.0935 0.0209  250  ALA   A N   
1221  C  CA  . ALA   A 181 ? 0.9691 1.0988 1.0485 -0.0504 -0.0918 0.0212  250  ALA   A CA  
1222  C  C   . ALA   A 181 ? 0.9981 1.1337 1.0754 -0.0485 -0.0947 0.0216  250  ALA   A C   
1223  O  O   . ALA   A 181 ? 0.9764 1.1110 1.0481 -0.0483 -0.0947 0.0230  250  ALA   A O   
1224  C  CB  . ALA   A 181 ? 0.9546 1.0868 1.0414 -0.0532 -0.0898 0.0193  250  ALA   A CB  
1225  N  N   . GLU   A 182 ? 1.1102 1.2514 1.1918 -0.0470 -0.0971 0.0205  251  GLU   A N   
1226  C  CA  . GLU   A 182 ? 1.1249 1.2722 1.2062 -0.0457 -0.0992 0.0209  251  GLU   A CA  
1227  C  C   . GLU   A 182 ? 1.0910 1.2374 1.1668 -0.0431 -0.1012 0.0228  251  GLU   A C   
1228  O  O   . GLU   A 182 ? 1.0695 1.2188 1.1437 -0.0430 -0.1024 0.0234  251  GLU   A O   
1229  C  CB  . GLU   A 182 ? 1.1670 1.3197 1.2536 -0.0442 -0.1008 0.0196  251  GLU   A CB  
1230  C  CG  . GLU   A 182 ? 1.2480 1.4016 1.3401 -0.0461 -0.0996 0.0174  251  GLU   A CG  
1231  C  CD  . GLU   A 182 ? 1.4314 1.5907 1.5263 -0.0470 -0.0995 0.0167  251  GLU   A CD  
1232  O  OE1 . GLU   A 182 ? 1.4726 1.6357 1.5664 -0.0457 -0.1007 0.0177  251  GLU   A OE1 
1233  O  OE2 . GLU   A 182 ? 1.3866 1.5464 1.4851 -0.0489 -0.0983 0.0150  251  GLU   A OE2 
1234  N  N   . THR   A 183 ? 0.9878 1.1299 1.0607 -0.0411 -0.1019 0.0236  252  THR   A N   
1235  C  CA  . THR   A 183 ? 0.9399 1.0806 1.0073 -0.0385 -0.1038 0.0253  252  THR   A CA  
1236  C  C   . THR   A 183 ? 0.9657 1.1011 1.0264 -0.0397 -0.1027 0.0264  252  THR   A C   
1237  O  O   . THR   A 183 ? 0.9088 1.0456 0.9662 -0.0387 -0.1047 0.0271  252  THR   A O   
1238  C  CB  . THR   A 183 ? 0.8947 1.0311 0.9598 -0.0358 -0.1046 0.0259  252  THR   A CB  
1239  O  OG1 . THR   A 183 ? 1.0164 1.1553 1.0866 -0.0349 -0.1051 0.0246  252  THR   A OG1 
1240  C  CG2 . THR   A 183 ? 0.9835 1.1214 1.0452 -0.0323 -0.1074 0.0274  252  THR   A CG2 
1241  N  N   . LEU   A 184 ? 0.9600 1.0887 1.0187 -0.0418 -0.0994 0.0264  253  LEU   A N   
1242  C  CA  . LEU   A 184 ? 0.9146 1.0371 0.9659 -0.0428 -0.0975 0.0276  253  LEU   A CA  
1243  C  C   . LEU   A 184 ? 0.9464 1.0728 0.9973 -0.0438 -0.0983 0.0272  253  LEU   A C   
1244  O  O   . LEU   A 184 ? 0.9656 1.0891 1.0094 -0.0426 -0.0996 0.0282  253  LEU   A O   
1245  C  CB  . LEU   A 184 ? 0.9429 1.0593 0.9949 -0.0456 -0.0928 0.0275  253  LEU   A CB  
1246  C  CG  . LEU   A 184 ? 0.9588 1.0689 1.0093 -0.0448 -0.0917 0.0282  253  LEU   A CG  
1247  C  CD1 . LEU   A 184 ? 0.9526 1.0560 1.0038 -0.0477 -0.0866 0.0284  253  LEU   A CD1 
1248  C  CD2 . LEU   A 184 ? 0.9767 1.0820 1.0181 -0.0414 -0.0938 0.0301  253  LEU   A CD2 
1249  N  N   . MET   A 185 ? 0.9739 1.1065 1.0319 -0.0458 -0.0978 0.0257  254  MET   A N   
1250  C  CA  . MET   A 185 ? 0.9289 1.0644 0.9864 -0.0471 -0.0982 0.0252  254  MET   A CA  
1251  C  C   . MET   A 185 ? 0.9168 1.0571 0.9737 -0.0450 -0.1026 0.0255  254  MET   A C   
1252  O  O   . MET   A 185 ? 0.9699 1.1088 1.0220 -0.0450 -0.1039 0.0258  254  MET   A O   
1253  C  CB  . MET   A 185 ? 0.9067 1.0474 0.9719 -0.0496 -0.0966 0.0235  254  MET   A CB  
1254  C  CG  . MET   A 185 ? 0.9197 1.0556 0.9858 -0.0521 -0.0922 0.0230  254  MET   A CG  
1255  S  SD  . MET   A 185 ? 1.0305 1.1723 1.1055 -0.0546 -0.0907 0.0208  254  MET   A SD  
1256  C  CE  . MET   A 185 ? 1.0552 1.2042 1.1309 -0.0537 -0.0944 0.0205  254  MET   A CE  
1257  N  N   . ASP   A 186 ? 0.9378 1.0834 0.9995 -0.0430 -0.1050 0.0255  255  ASP   A N   
1258  C  CA  . ASP   A 186 ? 0.9454 1.0960 1.0079 -0.0410 -0.1089 0.0259  255  ASP   A CA  
1259  C  C   . ASP   A 186 ? 1.0000 1.1450 1.0543 -0.0388 -0.1110 0.0271  255  ASP   A C   
1260  O  O   . ASP   A 186 ? 0.9946 1.1403 1.0464 -0.0383 -0.1138 0.0271  255  ASP   A O   
1261  C  CB  . ASP   A 186 ? 0.9352 1.0924 1.0046 -0.0390 -0.1103 0.0258  255  ASP   A CB  
1262  C  CG  . ASP   A 186 ? 1.0307 1.1949 1.1042 -0.0378 -0.1135 0.0260  255  ASP   A CG  
1263  O  OD1 . ASP   A 186 ? 1.1353 1.3036 1.2124 -0.0399 -0.1136 0.0252  255  ASP   A OD1 
1264  O  OD2 . ASP   A 186 ? 0.9998 1.1657 1.0736 -0.0348 -0.1160 0.0269  255  ASP   A OD2 
1265  N  N   . ARG   A 187 ? 1.0233 1.1621 1.0731 -0.0373 -0.1098 0.0281  256  ARG   A N   
1266  C  CA  . ARG   A 187 ? 0.9882 1.1197 1.0284 -0.0351 -0.1113 0.0294  256  ARG   A CA  
1267  C  C   . ARG   A 187 ? 0.9516 1.0783 0.9848 -0.0363 -0.1110 0.0293  256  ARG   A C   
1268  O  O   . ARG   A 187 ? 0.9794 1.1046 1.0073 -0.0343 -0.1147 0.0296  256  ARG   A O   
1269  C  CB  . ARG   A 187 ? 0.9439 1.0676 0.9797 -0.0344 -0.1085 0.0304  256  ARG   A CB  
1270  C  CG  . ARG   A 187 ? 0.9286 1.0540 0.9663 -0.0312 -0.1106 0.0309  256  ARG   A CG  
1271  C  CD  . ARG   A 187 ? 1.0086 1.1267 1.0437 -0.0313 -0.1077 0.0315  256  ARG   A CD  
1272  N  NE  . ARG   A 187 ? 1.0620 1.1706 1.0868 -0.0293 -0.1075 0.0331  256  ARG   A NE  
1273  C  CZ  . ARG   A 187 ? 1.0398 1.1395 1.0600 -0.0304 -0.1038 0.0339  256  ARG   A CZ  
1274  N  NH1 . ARG   A 187 ? 1.0636 1.1630 1.0893 -0.0336 -0.1001 0.0330  256  ARG   A NH1 
1275  N  NH2 . ARG   A 187 ? 1.0525 1.1431 1.0625 -0.0281 -0.1037 0.0355  256  ARG   A NH2 
1276  N  N   . ILE   A 188 ? 0.9136 1.0379 0.9468 -0.0394 -0.1069 0.0288  257  ILE   A N   
1277  C  CA  . ILE   A 188 ? 0.9300 1.0490 0.9559 -0.0404 -0.1060 0.0288  257  ILE   A CA  
1278  C  C   . ILE   A 188 ? 0.9711 1.0963 0.9996 -0.0407 -0.1100 0.0277  257  ILE   A C   
1279  O  O   . ILE   A 188 ? 0.9851 1.1064 1.0062 -0.0392 -0.1128 0.0278  257  ILE   A O   
1280  C  CB  . ILE   A 188 ? 0.9478 1.0635 0.9745 -0.0436 -0.1003 0.0286  257  ILE   A CB  
1281  C  CG1 . ILE   A 188 ? 0.9224 1.0313 0.9467 -0.0434 -0.0965 0.0298  257  ILE   A CG1 
1282  C  CG2 . ILE   A 188 ? 0.8969 1.0075 0.9162 -0.0445 -0.0990 0.0285  257  ILE   A CG2 
1283  C  CD1 . ILE   A 188 ? 0.9380 1.0419 0.9619 -0.0463 -0.0905 0.0299  257  ILE   A CD1 
1284  N  N   . LYS   A 189 ? 0.9928 1.1271 1.0317 -0.0424 -0.1102 0.0265  258  LYS   A N   
1285  C  CA  . LYS   A 189 ? 0.9499 1.0907 0.9929 -0.0429 -0.1138 0.0255  258  LYS   A CA  
1286  C  C   . LYS   A 189 ? 0.9964 1.1384 1.0377 -0.0400 -0.1194 0.0258  258  LYS   A C   
1287  O  O   . LYS   A 189 ? 0.9950 1.1363 1.0332 -0.0397 -0.1228 0.0252  258  LYS   A O   
1288  C  CB  . LYS   A 189 ? 0.9581 1.1082 1.0126 -0.0444 -0.1133 0.0246  258  LYS   A CB  
1289  C  CG  . LYS   A 189 ? 0.9672 1.1180 1.0252 -0.0473 -0.1090 0.0237  258  LYS   A CG  
1290  C  CD  . LYS   A 189 ? 1.1262 1.2856 1.1932 -0.0485 -0.1098 0.0226  258  LYS   A CD  
1291  C  CE  . LYS   A 189 ? 1.1671 1.3308 1.2412 -0.0481 -0.1082 0.0225  258  LYS   A CE  
1292  N  NZ  . LYS   A 189 ? 1.3499 1.5200 1.4310 -0.0496 -0.1079 0.0214  258  LYS   A NZ  
1293  N  N   . LYS   A 190 ? 0.9664 1.1104 1.0101 -0.0375 -0.1206 0.0267  259  LYS   A N   
1294  C  CA  . LYS   A 190 ? 0.9671 1.1137 1.0113 -0.0345 -0.1260 0.0269  259  LYS   A CA  
1295  C  C   . LYS   A 190 ? 1.0386 1.1766 1.0712 -0.0327 -0.1287 0.0271  259  LYS   A C   
1296  O  O   . LYS   A 190 ? 1.1090 1.2489 1.1416 -0.0316 -0.1338 0.0263  259  LYS   A O   
1297  C  CB  . LYS   A 190 ? 1.0086 1.1577 1.0562 -0.0318 -0.1263 0.0279  259  LYS   A CB  
1298  C  CG  . LYS   A 190 ? 0.9930 1.1506 1.0517 -0.0326 -0.1244 0.0277  259  LYS   A CG  
1299  C  CD  . LYS   A 190 ? 1.1191 1.2859 1.1870 -0.0337 -0.1267 0.0268  259  LYS   A CD  
1300  C  CE  . LYS   A 190 ? 1.1783 1.3499 1.2534 -0.0362 -0.1230 0.0262  259  LYS   A CE  
1301  N  NZ  . LYS   A 190 ? 1.3689 1.5494 1.4536 -0.0369 -0.1246 0.0258  259  LYS   A NZ  
1302  N  N   . GLN   A 191 ? 1.0284 1.1563 1.0507 -0.0323 -0.1254 0.0281  260  GLN   A N   
1303  C  CA  . GLN   A 191 ? 1.0576 1.1757 1.0670 -0.0303 -0.1273 0.0284  260  GLN   A CA  
1304  C  C   . GLN   A 191 ? 1.0748 1.1916 1.0814 -0.0322 -0.1281 0.0271  260  GLN   A C   
1305  O  O   . GLN   A 191 ? 1.1084 1.2244 1.1116 -0.0305 -0.1335 0.0263  260  GLN   A O   
1306  C  CB  . GLN   A 191 ? 1.0577 1.1649 1.0572 -0.0297 -0.1224 0.0300  260  GLN   A CB  
1307  C  CG  . GLN   A 191 ? 1.1370 1.2444 1.1379 -0.0273 -0.1227 0.0311  260  GLN   A CG  
1308  C  CD  . GLN   A 191 ? 1.1279 1.2238 1.1186 -0.0263 -0.1185 0.0328  260  GLN   A CD  
1309  O  OE1 . GLN   A 191 ? 1.1288 1.2144 1.1076 -0.0255 -0.1171 0.0335  260  GLN   A OE1 
1310  N  NE2 . GLN   A 191 ? 1.1768 1.2738 1.1719 -0.0262 -0.1162 0.0335  260  GLN   A NE2 
1311  N  N   . LEU   A 192 ? 1.0126 1.1296 1.0214 -0.0356 -0.1231 0.0268  261  LEU   A N   
1312  C  CA  . LEU   A 192 ? 0.9992 1.1151 1.0056 -0.0374 -0.1235 0.0256  261  LEU   A CA  
1313  C  C   . LEU   A 192 ? 1.1019 1.2262 1.1158 -0.0376 -0.1296 0.0240  261  LEU   A C   
1314  O  O   . LEU   A 192 ? 1.1452 1.2674 1.1554 -0.0382 -0.1318 0.0228  261  LEU   A O   
1315  C  CB  . LEU   A 192 ? 0.9819 1.0995 0.9930 -0.0410 -0.1174 0.0253  261  LEU   A CB  
1316  C  CG  . LEU   A 192 ? 0.9288 1.0367 0.9316 -0.0415 -0.1111 0.0265  261  LEU   A CG  
1317  C  CD1 . LEU   A 192 ? 0.9743 1.0867 0.9856 -0.0451 -0.1059 0.0260  261  LEU   A CD1 
1318  C  CD2 . LEU   A 192 ? 0.9736 1.0717 0.9634 -0.0405 -0.1113 0.0265  261  LEU   A CD2 
1319  N  N   . ARG   A 193 ? 1.0725 1.2061 1.0971 -0.0369 -0.1322 0.0240  262  ARG   A N   
1320  C  CA  . ARG   A 193 ? 1.0767 1.2184 1.1096 -0.0373 -0.1375 0.0227  262  ARG   A CA  
1321  C  C   . ARG   A 193 ? 1.1605 1.2993 1.1883 -0.0339 -0.1444 0.0223  262  ARG   A C   
1322  O  O   . ARG   A 193 ? 1.2551 1.3966 1.2857 -0.0343 -0.1494 0.0207  262  ARG   A O   
1323  C  CB  . ARG   A 193 ? 1.1560 1.3089 1.2030 -0.0379 -0.1369 0.0229  262  ARG   A CB  
1324  C  CG  . ARG   A 193 ? 1.2711 1.4324 1.3285 -0.0405 -0.1385 0.0216  262  ARG   A CG  
1325  C  CD  . ARG   A 193 ? 1.3169 1.4888 1.3875 -0.0399 -0.1398 0.0219  262  ARG   A CD  
1326  N  NE  . ARG   A 193 ? 1.3872 1.5616 1.4615 -0.0397 -0.1350 0.0231  262  ARG   A NE  
1327  C  CZ  . ARG   A 193 ? 1.4481 1.6242 1.5256 -0.0422 -0.1303 0.0229  262  ARG   A CZ  
1328  N  NH1 . ARG   A 193 ? 1.4198 1.5952 1.4969 -0.0451 -0.1291 0.0219  262  ARG   A NH1 
1329  N  NH2 . ARG   A 193 ? 1.4261 1.6043 1.5071 -0.0414 -0.1269 0.0238  262  ARG   A NH2 
1330  N  N   . GLU   A 194 ? 1.2632 1.3960 1.2834 -0.0305 -0.1451 0.0234  263  GLU   A N   
1331  C  CA  . GLU   A 194 ? 1.2882 1.4156 1.3004 -0.0268 -0.1515 0.0230  263  GLU   A CA  
1332  C  C   . GLU   A 194 ? 1.2836 1.4008 1.2827 -0.0267 -0.1528 0.0221  263  GLU   A C   
1333  O  O   . GLU   A 194 ? 1.2715 1.3839 1.2636 -0.0236 -0.1591 0.0211  263  GLU   A O   
1334  C  CB  . GLU   A 194 ? 1.2925 1.4142 1.2978 -0.0232 -0.1509 0.0247  263  GLU   A CB  
1335  C  CG  . GLU   A 194 ? 1.3224 1.4326 1.3150 -0.0233 -0.1446 0.0262  263  GLU   A CG  
1336  C  CD  . GLU   A 194 ? 1.4280 1.5332 1.4154 -0.0201 -0.1433 0.0279  263  GLU   A CD  
1337  O  OE1 . GLU   A 194 ? 1.4039 1.4978 1.3793 -0.0194 -0.1390 0.0293  263  GLU   A OE1 
1338  O  OE2 . GLU   A 194 ? 1.4901 1.6025 1.4856 -0.0183 -0.1465 0.0280  263  GLU   A OE2 
1339  N  N   . TRP   A 195 ? 1.2013 1.3146 1.1967 -0.0295 -0.1471 0.0222  264  TRP   A N   
1340  C  CA  . TRP   A 195 ? 1.1583 1.2620 1.1416 -0.0296 -0.1473 0.0214  264  TRP   A CA  
1341  C  C   . TRP   A 195 ? 1.2242 1.3337 1.2145 -0.0328 -0.1487 0.0195  264  TRP   A C   
1342  O  O   . TRP   A 195 ? 1.2265 1.3285 1.2072 -0.0326 -0.1500 0.0185  264  TRP   A O   
1343  C  CB  . TRP   A 195 ? 1.1059 1.2003 1.0794 -0.0303 -0.1392 0.0230  264  TRP   A CB  
1344  C  CG  . TRP   A 195 ? 1.0524 1.1383 1.0163 -0.0272 -0.1372 0.0249  264  TRP   A CG  
1345  C  CD1 . TRP   A 195 ? 1.1123 1.1967 1.0731 -0.0234 -0.1423 0.0252  264  TRP   A CD1 
1346  C  CD2 . TRP   A 195 ? 1.0260 1.1035 0.9823 -0.0276 -0.1295 0.0268  264  TRP   A CD2 
1347  N  NE1 . TRP   A 195 ? 1.1165 1.1914 1.0673 -0.0213 -0.1381 0.0273  264  TRP   A NE1 
1348  C  CE2 . TRP   A 195 ? 1.0882 1.1588 1.0365 -0.0240 -0.1301 0.0283  264  TRP   A CE2 
1349  C  CE3 . TRP   A 195 ? 1.0230 1.0981 0.9791 -0.0307 -0.1220 0.0274  264  TRP   A CE3 
1350  C  CZ2 . TRP   A 195 ? 1.0985 1.1596 1.0387 -0.0236 -0.1233 0.0305  264  TRP   A CZ2 
1351  C  CZ3 . TRP   A 195 ? 1.0641 1.1303 1.0130 -0.0303 -0.1152 0.0294  264  TRP   A CZ3 
1352  C  CH2 . TRP   A 195 ? 1.0343 1.0935 0.9754 -0.0269 -0.1158 0.0310  264  TRP   A CH2 
1353  N  N   . ASP   A 196 ? 1.2670 1.3888 1.2730 -0.0357 -0.1481 0.0191  265  ASP   A N   
1354  C  CA  . ASP   A 196 ? 1.2707 1.3976 1.2834 -0.0390 -0.1485 0.0175  265  ASP   A CA  
1355  C  C   . ASP   A 196 ? 1.3313 1.4717 1.3614 -0.0409 -0.1491 0.0174  265  ASP   A C   
1356  O  O   . ASP   A 196 ? 1.3781 1.5231 1.4145 -0.0424 -0.1437 0.0185  265  ASP   A O   
1357  C  CB  . ASP   A 196 ? 1.2667 1.3892 1.2750 -0.0415 -0.1415 0.0179  265  ASP   A CB  
1358  C  CG  . ASP   A 196 ? 1.3312 1.4560 1.3425 -0.0444 -0.1424 0.0161  265  ASP   A CG  
1359  O  OD1 . ASP   A 196 ? 1.3736 1.5039 1.3917 -0.0447 -0.1483 0.0147  265  ASP   A OD1 
1360  O  OD2 . ASP   A 196 ? 1.3219 1.4429 1.3293 -0.0462 -0.1371 0.0162  265  ASP   A OD2 
1361  N  N   . GLU   A 197 ? 1.4434 1.5896 1.4809 -0.0405 -0.1557 0.0161  266  GLU   A N   
1362  C  CA  . GLU   A 197 ? 1.4791 1.6380 1.5335 -0.0422 -0.1560 0.0161  266  GLU   A CA  
1363  C  C   . GLU   A 197 ? 1.5263 1.6885 1.5860 -0.0463 -0.1529 0.0153  266  GLU   A C   
1364  O  O   . GLU   A 197 ? 1.5168 1.6819 1.5813 -0.0479 -0.1568 0.0137  266  GLU   A O   
1365  C  CB  . GLU   A 197 ? 1.4827 1.6467 1.5443 -0.0406 -0.1638 0.0150  266  GLU   A CB  
1366  C  CG  . GLU   A 197 ? 1.5406 1.6986 1.5934 -0.0362 -0.1682 0.0153  266  GLU   A CG  
1367  C  CD  . GLU   A 197 ? 1.5316 1.6920 1.5865 -0.0341 -0.1649 0.0173  266  GLU   A CD  
1368  O  OE1 . GLU   A 197 ? 1.6200 1.7908 1.6886 -0.0343 -0.1650 0.0178  266  GLU   A OE1 
1369  O  OE2 . GLU   A 197 ? 1.4422 1.5938 1.4851 -0.0322 -0.1621 0.0185  266  GLU   A OE2 
1370  N  N   . ASN   A 198 ? 1.5475 1.7089 1.6060 -0.0478 -0.1459 0.0162  267  ASN   A N   
1371  C  CA  . ASN   A 198 ? 1.5709 1.7356 1.6345 -0.0513 -0.1424 0.0156  267  ASN   A CA  
1372  C  C   . ASN   A 198 ? 1.6549 1.8238 1.7241 -0.0523 -0.1360 0.0168  267  ASN   A C   
1373  O  O   . ASN   A 198 ? 1.7248 1.8995 1.8012 -0.0511 -0.1356 0.0178  267  ASN   A O   
1374  C  CB  . ASN   A 198 ? 1.5611 1.7167 1.6132 -0.0522 -0.1414 0.0146  267  ASN   A CB  
1375  C  CG  . ASN   A 198 ? 1.5866 1.7408 1.6376 -0.0527 -0.1475 0.0127  267  ASN   A CG  
1376  O  OD1 . ASN   A 198 ? 1.6108 1.7624 1.6584 -0.0504 -0.1536 0.0121  267  ASN   A OD1 
1377  N  ND2 . ASN   A 198 ? 1.5599 1.7157 1.6141 -0.0556 -0.1463 0.0116  267  ASN   A ND2 
1378  N  N   . LEU   A 199 ? 1.5769 1.7427 1.6428 -0.0543 -0.1312 0.0166  268  LEU   A N   
1379  C  CA  . LEU   A 199 ? 1.5088 1.6799 1.5821 -0.0558 -0.1263 0.0170  268  LEU   A CA  
1380  C  C   . LEU   A 199 ? 1.4957 1.6674 1.5699 -0.0540 -0.1237 0.0184  268  LEU   A C   
1381  O  O   . LEU   A 199 ? 1.6053 1.7731 1.6741 -0.0517 -0.1251 0.0192  268  LEU   A O   
1382  C  CB  . LEU   A 199 ? 1.4955 1.6625 1.5646 -0.0580 -0.1222 0.0162  268  LEU   A CB  
1383  N  N   . LYS   A 200 ? 1.4539 1.6302 1.5347 -0.0549 -0.1200 0.0186  269  LYS   A N   
1384  C  CA  . LYS   A 200 ? 1.5319 1.7077 1.6130 -0.0536 -0.1168 0.0195  269  LYS   A CA  
1385  C  C   . LYS   A 200 ? 1.5195 1.6960 1.6032 -0.0552 -0.1124 0.0189  269  LYS   A C   
1386  O  O   . LYS   A 200 ? 1.4153 1.5904 1.4989 -0.0544 -0.1098 0.0193  269  LYS   A O   
1387  C  CB  . LYS   A 200 ? 1.5044 1.6862 1.5925 -0.0514 -0.1182 0.0205  269  LYS   A CB  
1388  N  N   . ASP   A 201 ? 1.6169 1.7950 1.7028 -0.0574 -0.1116 0.0179  270  ASP   A N   
1389  C  CA  . ASP   A 201 ? 1.6852 1.8646 1.7743 -0.0586 -0.1080 0.0172  270  ASP   A CA  
1390  C  C   . ASP   A 201 ? 1.6872 1.8605 1.7704 -0.0598 -0.1051 0.0166  270  ASP   A C   
1391  O  O   . ASP   A 201 ? 1.5734 1.7414 1.6508 -0.0590 -0.1045 0.0172  270  ASP   A O   
1392  C  CB  . ASP   A 201 ? 1.7318 1.9159 1.8264 -0.0600 -0.1083 0.0165  270  ASP   A CB  
1393  C  CG  . ASP   A 201 ? 1.8075 1.9889 1.8983 -0.0620 -0.1095 0.0155  270  ASP   A CG  
1394  O  OD1 . ASP   A 201 ? 1.8314 2.0163 1.9264 -0.0631 -0.1111 0.0151  270  ASP   A OD1 
1395  O  OD2 . ASP   A 201 ? 1.8421 2.0174 1.9256 -0.0624 -0.1085 0.0152  270  ASP   A OD2 
1396  N  N   . ASP   A 202 ? 2.1193 2.2930 2.2039 -0.0615 -0.1030 0.0154  271  ASP   A N   
1397  C  CA  . ASP   A 202 ? 2.1297 2.2982 2.2097 -0.0628 -0.1000 0.0148  271  ASP   A CA  
1398  C  C   . ASP   A 202 ? 2.1150 2.2771 2.1861 -0.0625 -0.1009 0.0153  271  ASP   A C   
1399  O  O   . ASP   A 202 ? 2.1181 2.2747 2.1841 -0.0631 -0.0979 0.0152  271  ASP   A O   
1400  C  CB  . ASP   A 202 ? 2.2508 2.4208 2.3329 -0.0645 -0.0988 0.0135  271  ASP   A CB  
1401  C  CG  . ASP   A 202 ? 2.3119 2.4879 2.4016 -0.0644 -0.0986 0.0130  271  ASP   A CG  
1402  O  OD1 . ASP   A 202 ? 2.3061 2.4861 2.3991 -0.0642 -0.1009 0.0133  271  ASP   A OD1 
1403  O  OD2 . ASP   A 202 ? 2.3854 2.5616 2.4777 -0.0643 -0.0961 0.0122  271  ASP   A OD2 
1404  N  N   . SER   A 203 ? 1.7008 1.8634 1.7702 -0.0614 -0.1049 0.0159  272  SER   A N   
1405  C  CA  . SER   A 203 ? 1.5844 1.7401 1.6445 -0.0603 -0.1063 0.0165  272  SER   A CA  
1406  C  C   . SER   A 203 ? 1.4772 1.6271 1.5326 -0.0597 -0.1024 0.0174  272  SER   A C   
1407  O  O   . SER   A 203 ? 1.4078 1.5504 1.4551 -0.0597 -0.1002 0.0176  272  SER   A O   
1408  C  CB  . SER   A 203 ? 1.5553 1.7131 1.6159 -0.0586 -0.1114 0.0170  272  SER   A CB  
1409  O  OG  . SER   A 203 ? 1.5240 1.6888 1.5932 -0.0579 -0.1118 0.0175  272  SER   A OG  
1410  N  N   . LEU   A 204 ? 1.4022 1.5548 1.4628 -0.0591 -0.1011 0.0179  273  LEU   A N   
1411  C  CA  . LEU   A 204 ? 1.2565 1.4044 1.3148 -0.0589 -0.0972 0.0187  273  LEU   A CA  
1412  C  C   . LEU   A 204 ? 1.1481 1.3000 1.2147 -0.0601 -0.0943 0.0178  273  LEU   A C   
1413  O  O   . LEU   A 204 ? 1.2044 1.3627 1.2779 -0.0600 -0.0959 0.0172  273  LEU   A O   
1414  C  CB  . LEU   A 204 ? 1.2430 1.3888 1.2988 -0.0567 -0.0988 0.0200  273  LEU   A CB  
1415  C  CG  . LEU   A 204 ? 1.1367 1.2770 1.1831 -0.0549 -0.1016 0.0209  273  LEU   A CG  
1416  C  CD1 . LEU   A 204 ? 1.0425 1.1829 1.0887 -0.0526 -0.1039 0.0220  273  LEU   A CD1 
1417  C  CD2 . LEU   A 204 ? 1.0950 1.2258 1.1320 -0.0552 -0.0978 0.0215  273  LEU   A CD2 
1418  N  N   . PRO   A 205 ? 1.0621 1.2099 1.1282 -0.0610 -0.0901 0.0178  274  PRO   A N   
1419  C  CA  . PRO   A 205 ? 1.0510 1.2022 1.1252 -0.0619 -0.0879 0.0167  274  PRO   A CA  
1420  C  C   . PRO   A 205 ? 1.1299 1.2842 1.2088 -0.0605 -0.0897 0.0169  274  PRO   A C   
1421  O  O   . PRO   A 205 ? 1.1288 1.2815 1.2044 -0.0589 -0.0916 0.0182  274  PRO   A O   
1422  C  CB  . PRO   A 205 ? 0.9901 1.1355 1.0627 -0.0630 -0.0831 0.0170  274  PRO   A CB  
1423  C  CG  . PRO   A 205 ? 1.0404 1.1800 1.1035 -0.0630 -0.0822 0.0179  274  PRO   A CG  
1424  C  CD  . PRO   A 205 ? 1.1010 1.2407 1.1591 -0.0612 -0.0868 0.0188  274  PRO   A CD  
1425  N  N   . SER   A 206 ? 1.1243 1.2824 1.2105 -0.0608 -0.0893 0.0156  275  SER   A N   
1426  C  CA  . SER   A 206 ? 1.0675 1.2279 1.1577 -0.0592 -0.0909 0.0154  275  SER   A CA  
1427  C  C   . SER   A 206 ? 1.1067 1.2637 1.1994 -0.0596 -0.0888 0.0151  275  SER   A C   
1428  O  O   . SER   A 206 ? 1.1461 1.3026 1.2400 -0.0581 -0.0901 0.0153  275  SER   A O   
1429  C  CB  . SER   A 206 ? 1.0287 1.1948 1.1246 -0.0587 -0.0923 0.0141  275  SER   A CB  
1430  O  OG  . SER   A 206 ? 1.1098 1.2794 1.2045 -0.0582 -0.0945 0.0147  275  SER   A OG  
1431  N  N   . ASN   A 207 ? 1.0944 1.2491 1.1882 -0.0615 -0.0857 0.0145  276  ASN   A N   
1432  C  CA  . ASN   A 207 ? 1.1085 1.2601 1.2061 -0.0621 -0.0836 0.0142  276  ASN   A CA  
1433  C  C   . ASN   A 207 ? 1.1303 1.2754 1.2218 -0.0620 -0.0817 0.0162  276  ASN   A C   
1434  O  O   . ASN   A 207 ? 1.1519 1.2935 1.2371 -0.0626 -0.0798 0.0174  276  ASN   A O   
1435  C  CB  . ASN   A 207 ? 1.1450 1.2967 1.2479 -0.0642 -0.0804 0.0128  276  ASN   A CB  
1436  C  CG  . ASN   A 207 ? 1.1617 1.3103 1.2700 -0.0653 -0.0780 0.0124  276  ASN   A CG  
1437  O  OD1 . ASN   A 207 ? 1.2069 1.3515 1.3131 -0.0647 -0.0779 0.0136  276  ASN   A OD1 
1438  N  ND2 . ASN   A 207 ? 1.1991 1.3493 1.3149 -0.0667 -0.0762 0.0106  276  ASN   A ND2 
1439  N  N   . PRO   A 208 ? 1.1185 1.2610 1.2106 -0.0611 -0.0823 0.0167  277  PRO   A N   
1440  C  CA  . PRO   A 208 ? 1.0401 1.1755 1.1257 -0.0609 -0.0802 0.0188  277  PRO   A CA  
1441  C  C   . PRO   A 208 ? 1.0289 1.1594 1.1129 -0.0630 -0.0750 0.0194  277  PRO   A C   
1442  O  O   . PRO   A 208 ? 1.0357 1.1602 1.1108 -0.0625 -0.0732 0.0214  277  PRO   A O   
1443  C  CB  . PRO   A 208 ? 1.0285 1.1622 1.1181 -0.0603 -0.0809 0.0185  277  PRO   A CB  
1444  C  CG  . PRO   A 208 ? 1.0455 1.1853 1.1395 -0.0588 -0.0850 0.0170  277  PRO   A CG  
1445  C  CD  . PRO   A 208 ? 1.1374 1.2824 1.2354 -0.0600 -0.0848 0.0154  277  PRO   A CD  
1446  N  N   . ILE   A 209 ? 1.0250 1.1573 1.1171 -0.0650 -0.0724 0.0179  278  ILE   A N   
1447  C  CA  . ILE   A 209 ? 1.0912 1.2187 1.1827 -0.0669 -0.0667 0.0187  278  ILE   A CA  
1448  C  C   . ILE   A 209 ? 1.0933 1.2196 1.1768 -0.0666 -0.0656 0.0195  278  ILE   A C   
1449  O  O   . ILE   A 209 ? 1.0085 1.1277 1.0841 -0.0666 -0.0619 0.0214  278  ILE   A O   
1450  C  CB  . ILE   A 209 ? 1.0954 1.2258 1.1989 -0.0691 -0.0643 0.0168  278  ILE   A CB  
1451  C  CG1 . ILE   A 209 ? 1.1601 1.2910 1.2709 -0.0691 -0.0663 0.0157  278  ILE   A CG1 
1452  C  CG2 . ILE   A 209 ? 1.0365 1.1613 1.1405 -0.0709 -0.0577 0.0180  278  ILE   A CG2 
1453  C  CD1 . ILE   A 209 ? 1.0895 1.2281 1.2087 -0.0682 -0.0717 0.0127  278  ILE   A CD1 
1454  N  N   . ASP   A 210 ? 1.0949 1.2271 1.1792 -0.0663 -0.0689 0.0182  279  ASP   A N   
1455  C  CA  . ASP   A 210 ? 1.0502 1.1810 1.1264 -0.0658 -0.0690 0.0188  279  ASP   A CA  
1456  C  C   . ASP   A 210 ? 1.0274 1.1539 1.0930 -0.0638 -0.0715 0.0205  279  ASP   A C   
1457  O  O   . ASP   A 210 ? 1.0716 1.1911 1.1280 -0.0633 -0.0691 0.0220  279  ASP   A O   
1458  C  CB  . ASP   A 210 ? 1.0435 1.1816 1.1239 -0.0660 -0.0723 0.0169  279  ASP   A CB  
1459  C  CG  . ASP   A 210 ? 1.1433 1.2849 1.2329 -0.0677 -0.0699 0.0150  279  ASP   A CG  
1460  O  OD1 . ASP   A 210 ? 1.1796 1.3177 1.2715 -0.0689 -0.0651 0.0153  279  ASP   A OD1 
1461  O  OD2 . ASP   A 210 ? 1.1622 1.3099 1.2568 -0.0676 -0.0727 0.0133  279  ASP   A OD2 
1462  N  N   . PHE   A 211 ? 0.9261 1.0564 0.9928 -0.0624 -0.0762 0.0204  280  PHE   A N   
1463  C  CA  . PHE   A 211 ? 0.9720 1.0994 1.0301 -0.0602 -0.0794 0.0219  280  PHE   A CA  
1464  C  C   . PHE   A 211 ? 1.0414 1.1594 1.0913 -0.0594 -0.0763 0.0239  280  PHE   A C   
1465  O  O   . PHE   A 211 ? 1.0232 1.1356 1.0628 -0.0579 -0.0769 0.0250  280  PHE   A O   
1466  C  CB  . PHE   A 211 ? 0.9822 1.1151 1.0448 -0.0587 -0.0838 0.0215  280  PHE   A CB  
1467  C  CG  . PHE   A 211 ? 0.9381 1.0700 0.9942 -0.0563 -0.0878 0.0226  280  PHE   A CG  
1468  C  CD1 . PHE   A 211 ? 0.9232 1.0485 0.9725 -0.0547 -0.0874 0.0243  280  PHE   A CD1 
1469  C  CD2 . PHE   A 211 ? 0.9560 1.0942 1.0140 -0.0555 -0.0921 0.0220  280  PHE   A CD2 
1470  C  CE1 . PHE   A 211 ? 0.9608 1.0856 1.0048 -0.0521 -0.0916 0.0251  280  PHE   A CE1 
1471  C  CE2 . PHE   A 211 ? 0.9832 1.1214 1.0370 -0.0532 -0.0961 0.0229  280  PHE   A CE2 
1472  C  CZ  . PHE   A 211 ? 0.9472 1.0789 0.9940 -0.0514 -0.0961 0.0244  280  PHE   A CZ  
1473  N  N   . SER   A 212 ? 0.9559 1.0716 1.0101 -0.0601 -0.0733 0.0243  281  SER   A N   
1474  C  CA  . SER   A 212 ? 0.9671 1.0732 1.0138 -0.0596 -0.0694 0.0263  281  SER   A CA  
1475  C  C   . SER   A 212 ? 1.0175 1.1172 1.0561 -0.0599 -0.0653 0.0273  281  SER   A C   
1476  O  O   . SER   A 212 ? 1.0223 1.1139 1.0490 -0.0579 -0.0648 0.0290  281  SER   A O   
1477  C  CB  . SER   A 212 ? 1.0421 1.1468 1.0966 -0.0612 -0.0658 0.0263  281  SER   A CB  
1478  O  OG  . SER   A 212 ? 1.0739 1.1721 1.1271 -0.0628 -0.0591 0.0274  281  SER   A OG  
1479  N  N   . TYR   A 213 ? 1.0353 1.1380 1.0793 -0.0619 -0.0625 0.0261  282  TYR   A N   
1480  C  CA  . TYR   A 213 ? 1.0037 1.0995 1.0399 -0.0619 -0.0577 0.0271  282  TYR   A CA  
1481  C  C   . TYR   A 213 ? 1.0137 1.1076 1.0391 -0.0600 -0.0614 0.0271  282  TYR   A C   
1482  O  O   . TYR   A 213 ? 1.0185 1.1035 1.0324 -0.0586 -0.0588 0.0285  282  TYR   A O   
1483  C  CB  . TYR   A 213 ? 0.9839 1.0833 1.0294 -0.0644 -0.0534 0.0258  282  TYR   A CB  
1484  C  CG  . TYR   A 213 ? 1.0538 1.1507 1.1068 -0.0662 -0.0476 0.0265  282  TYR   A CG  
1485  C  CD1 . TYR   A 213 ? 1.0316 1.1185 1.0773 -0.0657 -0.0421 0.0290  282  TYR   A CD1 
1486  C  CD2 . TYR   A 213 ? 1.1114 1.2158 1.1789 -0.0683 -0.0477 0.0246  282  TYR   A CD2 
1487  C  CE1 . TYR   A 213 ? 1.0412 1.1259 1.0949 -0.0676 -0.0366 0.0297  282  TYR   A CE1 
1488  C  CE2 . TYR   A 213 ? 1.0227 1.1251 1.0984 -0.0702 -0.0429 0.0249  282  TYR   A CE2 
1489  C  CZ  . TYR   A 213 ? 1.0326 1.1254 1.1020 -0.0700 -0.0373 0.0275  282  TYR   A CZ  
1490  O  OH  . TYR   A 213 ? 1.0783 1.1693 1.1570 -0.0721 -0.0323 0.0279  282  TYR   A OH  
1491  N  N   . ARG   A 214 ? 1.0115 1.1133 1.0405 -0.0598 -0.0676 0.0255  283  ARG   A N   
1492  C  CA  . ARG   A 214 ? 1.0487 1.1490 1.0687 -0.0581 -0.0719 0.0253  283  ARG   A CA  
1493  C  C   . ARG   A 214 ? 0.9894 1.0823 0.9982 -0.0552 -0.0741 0.0269  283  ARG   A C   
1494  O  O   . ARG   A 214 ? 1.0275 1.1121 1.0240 -0.0534 -0.0738 0.0277  283  ARG   A O   
1495  C  CB  . ARG   A 214 ? 1.0864 1.1970 1.1141 -0.0586 -0.0777 0.0234  283  ARG   A CB  
1496  C  CG  . ARG   A 214 ? 1.1382 1.2486 1.1591 -0.0571 -0.0831 0.0229  283  ARG   A CG  
1497  C  CD  . ARG   A 214 ? 1.1550 1.2627 1.1714 -0.0579 -0.0815 0.0221  283  ARG   A CD  
1498  N  NE  . ARG   A 214 ? 1.2449 1.3600 1.2719 -0.0603 -0.0799 0.0206  283  ARG   A NE  
1499  C  CZ  . ARG   A 214 ? 1.2611 1.3846 1.2956 -0.0611 -0.0839 0.0191  283  ARG   A CZ  
1500  N  NH1 . ARG   A 214 ? 1.2763 1.4025 1.3098 -0.0600 -0.0896 0.0190  283  ARG   A NH1 
1501  N  NH2 . ARG   A 214 ? 1.1653 1.2945 1.2086 -0.0630 -0.0820 0.0179  283  ARG   A NH2 
1502  N  N   . VAL   A 215 ? 1.0276 1.1227 1.0397 -0.0543 -0.0765 0.0274  284  VAL   A N   
1503  C  CA  . VAL   A 215 ? 0.9916 1.0803 0.9938 -0.0513 -0.0791 0.0289  284  VAL   A CA  
1504  C  C   . VAL   A 215 ? 1.0537 1.1296 1.0434 -0.0501 -0.0739 0.0308  284  VAL   A C   
1505  O  O   . VAL   A 215 ? 1.0553 1.1237 1.0322 -0.0473 -0.0762 0.0315  284  VAL   A O   
1506  C  CB  . VAL   A 215 ? 0.9501 1.0421 0.9586 -0.0510 -0.0804 0.0293  284  VAL   A CB  
1507  C  CG1 . VAL   A 215 ? 1.0160 1.1000 1.0138 -0.0477 -0.0821 0.0310  284  VAL   A CG1 
1508  C  CG2 . VAL   A 215 ? 0.9480 1.0512 0.9662 -0.0512 -0.0858 0.0276  284  VAL   A CG2 
1509  N  N   . ALA   A 216 ? 1.0309 1.1038 1.0241 -0.0520 -0.0668 0.0317  285  ALA   A N   
1510  C  CA  . ALA   A 216 ? 1.0109 1.0713 0.9930 -0.0510 -0.0606 0.0339  285  ALA   A CA  
1511  C  C   . ALA   A 216 ? 1.1129 1.1670 1.0835 -0.0496 -0.0599 0.0339  285  ALA   A C   
1512  O  O   . ALA   A 216 ? 1.0989 1.1413 1.0546 -0.0467 -0.0584 0.0356  285  ALA   A O   
1513  C  CB  . ALA   A 216 ? 0.9589 1.0192 0.9500 -0.0539 -0.0529 0.0345  285  ALA   A CB  
1514  N  N   . ALA   A 217 ? 1.1248 1.1858 1.1014 -0.0513 -0.0609 0.0320  286  ALA   A N   
1515  C  CA  . ALA   A 217 ? 1.0730 1.1279 1.0389 -0.0500 -0.0603 0.0318  286  ALA   A CA  
1516  C  C   . ALA   A 217 ? 1.0926 1.1468 1.0500 -0.0474 -0.0684 0.0308  286  ALA   A C   
1517  O  O   . ALA   A 217 ? 1.1966 1.2440 1.1428 -0.0457 -0.0689 0.0306  286  ALA   A O   
1518  C  CB  . ALA   A 217 ? 0.9832 1.0448 0.9582 -0.0528 -0.0579 0.0302  286  ALA   A CB  
1519  N  N   . CYS   A 218 ? 1.0800 1.1407 1.0424 -0.0469 -0.0748 0.0301  287  CYS   A N   
1520  C  CA  . CYS   A 218 ? 1.1408 1.2021 1.0975 -0.0447 -0.0829 0.0290  287  CYS   A CA  
1521  C  C   . CYS   A 218 ? 1.1368 1.1928 1.0855 -0.0413 -0.0868 0.0301  287  CYS   A C   
1522  O  O   . CYS   A 218 ? 1.1596 1.2148 1.1026 -0.0389 -0.0938 0.0291  287  CYS   A O   
1523  C  CB  . CYS   A 218 ? 1.2028 1.2778 1.1734 -0.0469 -0.0881 0.0268  287  CYS   A CB  
1524  S  SG  . CYS   A 218 ? 1.3483 1.4314 1.3284 -0.0465 -0.0922 0.0270  287  CYS   A SG  
1525  N  N   . LEU   A 219 ? 1.1578 1.2101 1.1062 -0.0409 -0.0828 0.0320  288  LEU   A N   
1526  C  CA  . LEU   A 219 ? 1.0555 1.0999 0.9932 -0.0372 -0.0855 0.0333  288  LEU   A CA  
1527  C  C   . LEU   A 219 ? 1.1007 1.1302 1.0197 -0.0339 -0.0836 0.0345  288  LEU   A C   
1528  O  O   . LEU   A 219 ? 1.1605 1.1841 1.0754 -0.0349 -0.0768 0.0353  288  LEU   A O   
1529  C  CB  . LEU   A 219 ? 1.0186 1.0616 0.9602 -0.0377 -0.0810 0.0351  288  LEU   A CB  
1530  C  CG  . LEU   A 219 ? 0.9864 1.0419 0.9434 -0.0396 -0.0840 0.0341  288  LEU   A CG  
1531  C  CD1 . LEU   A 219 ? 0.9644 1.0173 0.9247 -0.0403 -0.0792 0.0358  288  LEU   A CD1 
1532  C  CD2 . LEU   A 219 ? 0.9928 1.0524 0.9487 -0.0368 -0.0927 0.0332  288  LEU   A CD2 
1533  N  N   . PRO   A 220 ? 1.0878 1.1106 0.9948 -0.0297 -0.0894 0.0347  289  PRO   A N   
1534  C  CA  . PRO   A 220 ? 1.0177 1.0239 0.9043 -0.0256 -0.0875 0.0361  289  PRO   A CA  
1535  C  C   . PRO   A 220 ? 1.1172 1.1132 0.9972 -0.0246 -0.0798 0.0391  289  PRO   A C   
1536  O  O   . PRO   A 220 ? 1.2057 1.1943 1.0764 -0.0212 -0.0817 0.0404  289  PRO   A O   
1537  C  CB  . PRO   A 220 ? 1.0297 1.0342 0.9087 -0.0216 -0.0976 0.0348  289  PRO   A CB  
1538  C  CG  . PRO   A 220 ? 1.1216 1.1393 1.0159 -0.0229 -0.1022 0.0341  289  PRO   A CG  
1539  C  CD  . PRO   A 220 ? 1.0765 1.1067 0.9886 -0.0282 -0.0981 0.0335  289  PRO   A CD  
1540  N  N   . ILE   A 221 ? 1.0926 1.0881 0.9778 -0.0278 -0.0708 0.0404  290  ILE   A N   
1541  C  CA  . ILE   A 221 ? 1.0995 1.0855 0.9802 -0.0275 -0.0626 0.0433  290  ILE   A CA  
1542  C  C   . ILE   A 221 ? 1.1197 1.0940 0.9894 -0.0269 -0.0543 0.0449  290  ILE   A C   
1543  O  O   . ILE   A 221 ? 1.1265 1.1028 0.9963 -0.0277 -0.0541 0.0436  290  ILE   A O   
1544  C  CB  . ILE   A 221 ? 1.1272 1.1235 1.0263 -0.0319 -0.0590 0.0435  290  ILE   A CB  
1545  C  CG1 . ILE   A 221 ? 1.1050 1.1112 1.0183 -0.0364 -0.0556 0.0420  290  ILE   A CG1 
1546  C  CG2 . ILE   A 221 ? 1.0817 1.0880 0.9894 -0.0317 -0.0670 0.0420  290  ILE   A CG2 
1547  C  CD1 . ILE   A 221 ? 1.0516 1.0695 0.9839 -0.0405 -0.0543 0.0413  290  ILE   A CD1 
1548  N  N   . ASP   A 222 ? 1.1909 1.1524 1.0507 -0.0252 -0.0471 0.0480  291  ASP   A N   
1549  C  CA  . ASP   A 222 ? 1.1947 1.1439 1.0436 -0.0243 -0.0377 0.0501  291  ASP   A CA  
1550  C  C   . ASP   A 222 ? 1.1903 1.1457 1.0554 -0.0294 -0.0287 0.0508  291  ASP   A C   
1551  O  O   . ASP   A 222 ? 1.2162 1.1840 1.0991 -0.0332 -0.0299 0.0498  291  ASP   A O   
1552  C  CB  . ASP   A 222 ? 1.2894 1.2207 1.1192 -0.0197 -0.0339 0.0532  291  ASP   A CB  
1553  C  CG  . ASP   A 222 ? 1.2407 1.1723 1.0778 -0.0213 -0.0301 0.0551  291  ASP   A CG  
1554  O  OD1 . ASP   A 222 ? 1.2033 1.1486 1.0604 -0.0260 -0.0303 0.0540  291  ASP   A OD1 
1555  O  OD2 . ASP   A 222 ? 1.2996 1.2169 1.1217 -0.0177 -0.0272 0.0577  291  ASP   A OD2 
1556  N  N   . ASP   A 223 ? 1.3640 1.3104 1.2228 -0.0292 -0.0193 0.0527  292  ASP   A N   
1557  C  CA  . ASP   A 223 ? 1.3855 1.3391 1.2612 -0.0341 -0.0113 0.0529  292  ASP   A CA  
1558  C  C   . ASP   A 223 ? 1.3718 1.3266 1.2583 -0.0367 -0.0064 0.0546  292  ASP   A C   
1559  O  O   . ASP   A 223 ? 1.3818 1.3478 1.2876 -0.0414 -0.0042 0.0536  292  ASP   A O   
1560  C  CB  . ASP   A 223 ? 1.4501 1.3936 1.3168 -0.0330 -0.0019 0.0547  292  ASP   A CB  
1561  C  CG  . ASP   A 223 ? 1.4792 1.4278 1.3452 -0.0329 -0.0057 0.0521  292  ASP   A CG  
1562  O  OD1 . ASP   A 223 ? 1.4539 1.4136 1.3262 -0.0337 -0.0156 0.0490  292  ASP   A OD1 
1563  O  OD2 . ASP   A 223 ? 1.5138 1.4548 1.3727 -0.0318 0.0015  0.0533  292  ASP   A OD2 
1564  N  N   . VAL   A 224 ? 1.2823 1.2256 1.1569 -0.0338 -0.0053 0.0570  293  VAL   A N   
1565  C  CA  . VAL   A 224 ? 1.2366 1.1805 1.1214 -0.0365 -0.0007 0.0586  293  VAL   A CA  
1566  C  C   . VAL   A 224 ? 1.2062 1.1655 1.1078 -0.0393 -0.0090 0.0559  293  VAL   A C   
1567  O  O   . VAL   A 224 ? 1.2154 1.1838 1.1352 -0.0437 -0.0063 0.0552  293  VAL   A O   
1568  C  CB  . VAL   A 224 ? 1.1866 1.1136 1.0536 -0.0324 0.0026  0.0619  293  VAL   A CB  
1569  C  CG1 . VAL   A 224 ? 1.2014 1.1122 1.0505 -0.0291 0.0112  0.0647  293  VAL   A CG1 
1570  C  CG2 . VAL   A 224 ? 1.2280 1.1539 1.0841 -0.0283 -0.0081 0.0608  293  VAL   A CG2 
1571  N  N   . LEU   A 225 ? 1.2047 1.1674 1.1008 -0.0366 -0.0192 0.0542  294  LEU   A N   
1572  C  CA  . LEU   A 225 ? 1.1416 1.1193 1.0532 -0.0389 -0.0270 0.0515  294  LEU   A CA  
1573  C  C   . LEU   A 225 ? 1.1324 1.1239 1.0617 -0.0433 -0.0266 0.0491  294  LEU   A C   
1574  O  O   . LEU   A 225 ? 1.1028 1.1041 1.0484 -0.0467 -0.0272 0.0479  294  LEU   A O   
1575  C  CB  . LEU   A 225 ? 1.1172 1.0975 1.0210 -0.0354 -0.0376 0.0499  294  LEU   A CB  
1576  C  CG  . LEU   A 225 ? 1.1576 1.1314 1.0529 -0.0321 -0.0410 0.0512  294  LEU   A CG  
1577  C  CD1 . LEU   A 225 ? 1.1364 1.1183 1.0317 -0.0299 -0.0523 0.0488  294  LEU   A CD1 
1578  C  CD2 . LEU   A 225 ? 1.1540 1.1301 1.0609 -0.0350 -0.0372 0.0521  294  LEU   A CD2 
1579  N  N   . ARG   A 226 ? 1.1352 1.1272 1.0609 -0.0430 -0.0263 0.0482  295  ARG   A N   
1580  C  CA  . ARG   A 226 ? 1.0928 1.0967 1.0343 -0.0469 -0.0254 0.0461  295  ARG   A CA  
1581  C  C   . ARG   A 226 ? 1.1374 1.1428 1.0925 -0.0507 -0.0171 0.0470  295  ARG   A C   
1582  O  O   . ARG   A 226 ? 1.1097 1.1267 1.0819 -0.0541 -0.0189 0.0451  295  ARG   A O   
1583  C  CB  . ARG   A 226 ? 1.1164 1.1173 1.0496 -0.0457 -0.0241 0.0456  295  ARG   A CB  
1584  C  CG  . ARG   A 226 ? 1.1163 1.1189 1.0407 -0.0429 -0.0335 0.0438  295  ARG   A CG  
1585  C  CD  . ARG   A 226 ? 1.1457 1.1497 1.0683 -0.0432 -0.0329 0.0424  295  ARG   A CD  
1586  N  NE  . ARG   A 226 ? 1.2059 1.2175 1.1290 -0.0426 -0.0425 0.0397  295  ARG   A NE  
1587  C  CZ  . ARG   A 226 ? 1.2095 1.2201 1.1267 -0.0417 -0.0443 0.0384  295  ARG   A CZ  
1588  N  NH1 . ARG   A 226 ? 1.1248 1.1271 1.0346 -0.0411 -0.0371 0.0396  295  ARG   A NH1 
1589  N  NH2 . ARG   A 226 ? 1.1704 1.1883 1.0894 -0.0414 -0.0533 0.0360  295  ARG   A NH2 
1590  N  N   . ILE   A 227 ? 1.1565 1.1496 1.1040 -0.0501 -0.0080 0.0500  296  ILE   A N   
1591  C  CA  . ILE   A 227 ? 1.1129 1.1072 1.0742 -0.0539 0.0005  0.0509  296  ILE   A CA  
1592  C  C   . ILE   A 227 ? 1.1007 1.1006 1.0745 -0.0561 -0.0022 0.0503  296  ILE   A C   
1593  O  O   . ILE   A 227 ? 1.0750 1.0830 1.0666 -0.0601 -0.0001 0.0491  296  ILE   A O   
1594  C  CB  . ILE   A 227 ? 1.0822 1.0611 1.0320 -0.0524 0.0113  0.0547  296  ILE   A CB  
1595  C  CG1 . ILE   A 227 ? 1.1088 1.0826 1.0474 -0.0502 0.0142  0.0550  296  ILE   A CG1 
1596  C  CG2 . ILE   A 227 ? 1.0879 1.0680 1.0535 -0.0565 0.0201  0.0557  296  ILE   A CG2 
1597  C  CD1 . ILE   A 227 ? 1.1360 1.0995 1.0720 -0.0504 0.0268  0.0581  296  ILE   A CD1 
1598  N  N   . GLN   A 228 ? 1.1174 1.1128 1.0818 -0.0535 -0.0071 0.0511  297  GLN   A N   
1599  C  CA  . GLN   A 228 ? 1.1242 1.1248 1.0994 -0.0552 -0.0103 0.0503  297  GLN   A CA  
1600  C  C   . GLN   A 228 ? 1.0916 1.1082 1.0830 -0.0577 -0.0172 0.0467  297  GLN   A C   
1601  O  O   . GLN   A 228 ? 1.1000 1.1230 1.1073 -0.0611 -0.0160 0.0455  297  GLN   A O   
1602  C  CB  . GLN   A 228 ? 1.1692 1.1627 1.1306 -0.0513 -0.0153 0.0515  297  GLN   A CB  
1603  C  CG  . GLN   A 228 ? 1.2496 1.2260 1.1921 -0.0479 -0.0093 0.0550  297  GLN   A CG  
1604  C  CD  . GLN   A 228 ? 1.3996 1.3684 1.3326 -0.0450 -0.0122 0.0565  297  GLN   A CD  
1605  O  OE1 . GLN   A 228 ? 1.4924 1.4495 1.4068 -0.0406 -0.0126 0.0584  297  GLN   A OE1 
1606  N  NE2 . GLN   A 228 ? 1.4772 1.4522 1.4226 -0.0473 -0.0146 0.0556  297  GLN   A NE2 
1607  N  N   . LEU   A 229 ? 1.0799 1.1027 1.0675 -0.0559 -0.0245 0.0448  298  LEU   A N   
1608  C  CA  . LEU   A 229 ? 1.0407 1.0778 1.0422 -0.0579 -0.0307 0.0416  298  LEU   A CA  
1609  C  C   . LEU   A 229 ? 1.0549 1.0984 1.0708 -0.0616 -0.0261 0.0403  298  LEU   A C   
1610  O  O   . LEU   A 229 ? 1.0438 1.0966 1.0745 -0.0640 -0.0285 0.0382  298  LEU   A O   
1611  C  CB  . LEU   A 229 ? 0.9970 1.0387 0.9916 -0.0555 -0.0380 0.0402  298  LEU   A CB  
1612  C  CG  . LEU   A 229 ? 0.9969 1.0334 0.9779 -0.0515 -0.0437 0.0411  298  LEU   A CG  
1613  C  CD1 . LEU   A 229 ? 0.9058 0.9455 0.8797 -0.0492 -0.0504 0.0397  298  LEU   A CD1 
1614  C  CD2 . LEU   A 229 ? 1.1245 1.1658 1.1126 -0.0515 -0.0480 0.0405  298  LEU   A CD2 
1615  N  N   . LEU   A 230 ? 1.0557 1.0939 1.0674 -0.0618 -0.0195 0.0415  299  LEU   A N   
1616  C  CA  . LEU   A 230 ? 1.0512 1.0956 1.0772 -0.0652 -0.0149 0.0402  299  LEU   A CA  
1617  C  C   . LEU   A 230 ? 1.0363 1.0799 1.0750 -0.0682 -0.0096 0.0408  299  LEU   A C   
1618  O  O   . LEU   A 230 ? 1.0501 1.1015 1.1046 -0.0712 -0.0082 0.0390  299  LEU   A O   
1619  C  CB  . LEU   A 230 ? 1.0473 1.0857 1.0653 -0.0644 -0.0087 0.0415  299  LEU   A CB  
1620  C  CG  . LEU   A 230 ? 1.0975 1.1377 1.1053 -0.0620 -0.0141 0.0403  299  LEU   A CG  
1621  C  CD1 . LEU   A 230 ? 1.0729 1.1038 1.0687 -0.0603 -0.0077 0.0420  299  LEU   A CD1 
1622  C  CD2 . LEU   A 230 ? 1.0464 1.1005 1.0670 -0.0639 -0.0199 0.0369  299  LEU   A CD2 
1623  N  N   . LYS   A 231 ? 1.0501 1.0844 1.0826 -0.0674 -0.0069 0.0432  300  LYS   A N   
1624  C  CA  . LYS   A 231 ? 1.0191 1.0521 1.0639 -0.0704 -0.0020 0.0438  300  LYS   A CA  
1625  C  C   . LYS   A 231 ? 1.0518 1.0913 1.1058 -0.0713 -0.0090 0.0417  300  LYS   A C   
1626  O  O   . LYS   A 231 ? 1.0835 1.1222 1.1483 -0.0738 -0.0064 0.0418  300  LYS   A O   
1627  C  CB  . LYS   A 231 ? 1.0630 1.0812 1.0964 -0.0692 0.0059  0.0477  300  LYS   A CB  
1628  C  CG  . LYS   A 231 ? 1.0544 1.0640 1.0762 -0.0676 0.0136  0.0502  300  LYS   A CG  
1629  C  CD  . LYS   A 231 ? 1.1544 1.1531 1.1769 -0.0690 0.0247  0.0535  300  LYS   A CD  
1630  C  CE  . LYS   A 231 ? 1.2245 1.2094 1.2282 -0.0657 0.0321  0.0570  300  LYS   A CE  
1631  N  NZ  . LYS   A 231 ? 1.2026 1.1739 1.1890 -0.0624 0.0328  0.0599  300  LYS   A NZ  
1632  N  N   . ILE   A 232 ? 1.0272 1.0731 1.0778 -0.0693 -0.0178 0.0399  301  ILE   A N   
1633  C  CA  . ILE   A 232 ? 0.9896 1.0413 1.0473 -0.0695 -0.0246 0.0380  301  ILE   A CA  
1634  C  C   . ILE   A 232 ? 1.0569 1.1203 1.1319 -0.0722 -0.0273 0.0346  301  ILE   A C   
1635  O  O   . ILE   A 232 ? 1.0313 1.1011 1.1087 -0.0724 -0.0282 0.0331  301  ILE   A O   
1636  C  CB  . ILE   A 232 ? 1.0548 1.1077 1.1009 -0.0658 -0.0322 0.0378  301  ILE   A CB  
1637  C  CG1 . ILE   A 232 ? 1.0668 1.1074 1.0963 -0.0629 -0.0299 0.0410  301  ILE   A CG1 
1638  C  CG2 . ILE   A 232 ? 1.0422 1.1029 1.0963 -0.0657 -0.0395 0.0355  301  ILE   A CG2 
1639  C  CD1 . ILE   A 232 ? 1.0490 1.0904 1.0673 -0.0590 -0.0374 0.0409  301  ILE   A CD1 
1640  N  N   . GLY   A 233 ? 1.0664 1.1320 1.1527 -0.0739 -0.0288 0.0333  302  GLY   A N   
1641  C  CA  . GLY   A 233 ? 1.0577 1.1324 1.1610 -0.0766 -0.0303 0.0301  302  GLY   A CA  
1642  C  C   . GLY   A 233 ? 1.0798 1.1644 1.1865 -0.0753 -0.0387 0.0271  302  GLY   A C   
1643  O  O   . GLY   A 233 ? 1.1808 1.2730 1.2991 -0.0769 -0.0401 0.0245  302  GLY   A O   
1644  N  N   . SER   A 234 ? 1.0651 1.1497 1.1621 -0.0724 -0.0443 0.0274  303  SER   A N   
1645  C  CA  . SER   A 234 ? 1.0618 1.1551 1.1621 -0.0710 -0.0518 0.0248  303  SER   A CA  
1646  C  C   . SER   A 234 ? 1.0311 1.1263 1.1199 -0.0682 -0.0552 0.0255  303  SER   A C   
1647  O  O   . SER   A 234 ? 1.0448 1.1335 1.1216 -0.0664 -0.0541 0.0280  303  SER   A O   
1648  C  CB  . SER   A 234 ? 1.0446 1.1373 1.1477 -0.0701 -0.0561 0.0240  303  SER   A CB  
1649  O  OG  . SER   A 234 ? 1.0445 1.1298 1.1359 -0.0679 -0.0560 0.0265  303  SER   A OG  
1650  N  N   . ALA   A 235 ? 0.9763 1.0800 1.0687 -0.0677 -0.0595 0.0234  304  ALA   A N   
1651  C  CA  . ALA   A 235 ? 0.9727 1.0787 1.0558 -0.0652 -0.0631 0.0240  304  ALA   A CA  
1652  C  C   . ALA   A 235 ? 0.9620 1.0658 1.0382 -0.0624 -0.0672 0.0250  304  ALA   A C   
1653  O  O   . ALA   A 235 ? 1.0125 1.1144 1.0787 -0.0603 -0.0687 0.0264  304  ALA   A O   
1654  C  CB  . ALA   A 235 ? 1.0072 1.1224 1.0961 -0.0653 -0.0667 0.0216  304  ALA   A CB  
1655  N  N   . ILE   A 236 ? 0.9786 1.0827 1.0601 -0.0621 -0.0693 0.0241  305  ILE   A N   
1656  C  CA  . ILE   A 236 ? 0.9632 1.0651 1.0384 -0.0592 -0.0730 0.0251  305  ILE   A CA  
1657  C  C   . ILE   A 236 ? 0.9360 1.0282 1.0012 -0.0584 -0.0698 0.0279  305  ILE   A C   
1658  O  O   . ILE   A 236 ? 0.9155 1.0055 0.9710 -0.0556 -0.0721 0.0293  305  ILE   A O   
1659  C  CB  . ILE   A 236 ? 0.9991 1.1025 1.0818 -0.0590 -0.0758 0.0234  305  ILE   A CB  
1660  C  CG1 . ILE   A 236 ? 0.9552 1.0673 1.0424 -0.0575 -0.0808 0.0213  305  ILE   A CG1 
1661  C  CG2 . ILE   A 236 ? 0.9830 1.0800 1.0593 -0.0568 -0.0768 0.0250  305  ILE   A CG2 
1662  C  CD1 . ILE   A 236 ? 1.0224 1.1356 1.1179 -0.0577 -0.0830 0.0190  305  ILE   A CD1 
1663  N  N   . GLN   A 237 ? 0.9510 1.0368 1.0187 -0.0607 -0.0645 0.0287  306  GLN   A N   
1664  C  CA  . GLN   A 237 ? 0.9979 1.0732 1.0555 -0.0599 -0.0605 0.0316  306  GLN   A CA  
1665  C  C   . GLN   A 237 ? 1.0375 1.1100 1.0839 -0.0586 -0.0591 0.0331  306  GLN   A C   
1666  O  O   . GLN   A 237 ? 1.0885 1.1534 1.1229 -0.0562 -0.0588 0.0353  306  GLN   A O   
1667  C  CB  . GLN   A 237 ? 0.9987 1.0680 1.0622 -0.0631 -0.0540 0.0322  306  GLN   A CB  
1668  C  CG  . GLN   A 237 ? 0.9933 1.0618 1.0654 -0.0642 -0.0551 0.0311  306  GLN   A CG  
1669  C  CD  . GLN   A 237 ? 1.0483 1.1119 1.1287 -0.0679 -0.0485 0.0316  306  GLN   A CD  
1670  O  OE1 . GLN   A 237 ? 1.0175 1.0823 1.1024 -0.0702 -0.0437 0.0316  306  GLN   A OE1 
1671  N  NE2 . GLN   A 237 ? 1.0682 1.1262 1.1511 -0.0684 -0.0481 0.0319  306  GLN   A NE2 
1672  N  N   . ARG   A 238 ? 1.0036 1.0817 1.0534 -0.0599 -0.0586 0.0320  307  ARG   A N   
1673  C  CA  . ARG   A 238 ? 0.9902 1.0652 1.0295 -0.0587 -0.0573 0.0332  307  ARG   A CA  
1674  C  C   . ARG   A 238 ? 0.9895 1.0680 1.0219 -0.0556 -0.0640 0.0329  307  ARG   A C   
1675  O  O   . ARG   A 238 ? 1.0324 1.1051 1.0527 -0.0533 -0.0643 0.0345  307  ARG   A O   
1676  C  CB  . ARG   A 238 ? 1.0302 1.1094 1.0755 -0.0611 -0.0543 0.0320  307  ARG   A CB  
1677  C  CG  . ARG   A 238 ? 1.0209 1.0923 1.0557 -0.0607 -0.0492 0.0339  307  ARG   A CG  
1678  C  CD  . ARG   A 238 ? 1.0076 1.0833 1.0480 -0.0628 -0.0463 0.0326  307  ARG   A CD  
1679  N  NE  . ARG   A 238 ? 0.9781 1.0553 1.0311 -0.0660 -0.0413 0.0320  307  ARG   A NE  
1680  C  CZ  . ARG   A 238 ? 1.0491 1.1355 1.1160 -0.0679 -0.0437 0.0295  307  ARG   A CZ  
1681  N  NH1 . ARG   A 238 ? 1.0312 1.1258 1.1006 -0.0670 -0.0503 0.0274  307  ARG   A NH1 
1682  N  NH2 . ARG   A 238 ? 1.0634 1.1502 1.1419 -0.0706 -0.0394 0.0289  307  ARG   A NH2 
1683  N  N   . LEU   A 239 ? 0.9731 1.0609 1.0130 -0.0553 -0.0692 0.0310  308  LEU   A N   
1684  C  CA  . LEU   A 239 ? 0.9799 1.0715 1.0150 -0.0523 -0.0753 0.0309  308  LEU   A CA  
1685  C  C   . LEU   A 239 ? 1.0051 1.0902 1.0319 -0.0494 -0.0769 0.0326  308  LEU   A C   
1686  O  O   . LEU   A 239 ? 0.9481 1.0306 0.9655 -0.0466 -0.0798 0.0336  308  LEU   A O   
1687  C  CB  . LEU   A 239 ? 0.9488 1.0510 0.9941 -0.0525 -0.0795 0.0287  308  LEU   A CB  
1688  C  CG  . LEU   A 239 ? 0.8994 1.0075 0.9524 -0.0552 -0.0781 0.0270  308  LEU   A CG  
1689  C  CD1 . LEU   A 239 ? 0.8822 0.9984 0.9459 -0.0557 -0.0807 0.0249  308  LEU   A CD1 
1690  C  CD2 . LEU   A 239 ? 0.9579 1.0684 1.0057 -0.0544 -0.0802 0.0269  308  LEU   A CD2 
1691  N  N   . ARG   A 240 ? 1.0299 1.1119 1.0600 -0.0497 -0.0755 0.0330  309  ARG   A N   
1692  C  CA  . ARG   A 240 ? 1.0287 1.1034 1.0503 -0.0469 -0.0765 0.0348  309  ARG   A CA  
1693  C  C   . ARG   A 240 ? 1.0133 1.0775 1.0219 -0.0456 -0.0734 0.0370  309  ARG   A C   
1694  O  O   . ARG   A 240 ? 1.0222 1.0825 1.0207 -0.0422 -0.0765 0.0381  309  ARG   A O   
1695  C  CB  . ARG   A 240 ? 1.0559 1.1273 1.0831 -0.0480 -0.0744 0.0348  309  ARG   A CB  
1696  C  CG  . ARG   A 240 ? 1.0519 1.1304 1.0864 -0.0469 -0.0793 0.0331  309  ARG   A CG  
1697  C  CD  . ARG   A 240 ? 0.9767 1.0521 1.0177 -0.0484 -0.0776 0.0326  309  ARG   A CD  
1698  N  NE  . ARG   A 240 ? 1.0116 1.0766 1.0445 -0.0470 -0.0757 0.0347  309  ARG   A NE  
1699  C  CZ  . ARG   A 240 ? 1.0854 1.1479 1.1116 -0.0434 -0.0793 0.0356  309  ARG   A CZ  
1700  N  NH1 . ARG   A 240 ? 1.1263 1.1964 1.1537 -0.0407 -0.0847 0.0346  309  ARG   A NH1 
1701  N  NH2 . ARG   A 240 ? 1.1671 1.2192 1.1852 -0.0422 -0.0771 0.0376  309  ARG   A NH2 
1702  N  N   . CYS   A 241 ? 0.9663 1.0258 0.9748 -0.0482 -0.0672 0.0376  310  CYS   A N   
1703  C  CA  . CYS   A 241 ? 1.0720 1.1207 1.0672 -0.0468 -0.0635 0.0398  310  CYS   A CA  
1704  C  C   . CYS   A 241 ? 1.0531 1.1033 1.0398 -0.0442 -0.0680 0.0395  310  CYS   A C   
1705  O  O   . CYS   A 241 ? 1.0398 1.0835 1.0145 -0.0406 -0.0706 0.0408  310  CYS   A O   
1706  C  CB  . CYS   A 241 ? 1.1443 1.1890 1.1423 -0.0500 -0.0558 0.0404  310  CYS   A CB  
1707  S  SG  . CYS   A 241 ? 1.2724 1.3001 1.2544 -0.0483 -0.0488 0.0440  310  CYS   A SG  
1708  N  N   . GLU   A 242 ? 1.0569 1.1153 1.0498 -0.0459 -0.0693 0.0377  311  GLU   A N   
1709  C  CA  . GLU   A 242 ? 1.0349 1.0946 1.0206 -0.0439 -0.0736 0.0372  311  GLU   A CA  
1710  C  C   . GLU   A 242 ? 1.0179 1.0800 1.0002 -0.0404 -0.0807 0.0370  311  GLU   A C   
1711  O  O   . GLU   A 242 ? 1.0056 1.0633 0.9773 -0.0374 -0.0840 0.0375  311  GLU   A O   
1712  C  CB  . GLU   A 242 ? 0.9719 1.0417 0.9671 -0.0464 -0.0747 0.0350  311  GLU   A CB  
1713  C  CG  . GLU   A 242 ? 0.9902 1.0575 0.9880 -0.0493 -0.0679 0.0352  311  GLU   A CG  
1714  C  CD  . GLU   A 242 ? 1.0163 1.0940 1.0251 -0.0519 -0.0689 0.0329  311  GLU   A CD  
1715  O  OE1 . GLU   A 242 ? 1.0233 1.1102 1.0398 -0.0519 -0.0739 0.0313  311  GLU   A OE1 
1716  O  OE2 . GLU   A 242 ? 1.0352 1.1114 1.0445 -0.0537 -0.0645 0.0327  311  GLU   A OE2 
1717  N  N   . LEU   A 243 ? 1.0254 1.0943 1.0167 -0.0405 -0.0833 0.0363  312  LEU   A N   
1718  C  CA  . LEU   A 243 ? 1.0182 1.0889 1.0067 -0.0370 -0.0894 0.0364  312  LEU   A CA  
1719  C  C   . LEU   A 243 ? 1.0094 1.0680 0.9845 -0.0338 -0.0886 0.0386  312  LEU   A C   
1720  O  O   . LEU   A 243 ? 1.0160 1.0723 0.9828 -0.0302 -0.0933 0.0389  312  LEU   A O   
1721  C  CB  . LEU   A 243 ? 1.0225 1.1013 1.0222 -0.0374 -0.0913 0.0355  312  LEU   A CB  
1722  C  CG  . LEU   A 243 ? 0.9810 1.0720 0.9894 -0.0374 -0.0962 0.0337  312  LEU   A CG  
1723  C  CD1 . LEU   A 243 ? 0.9551 1.0529 0.9744 -0.0383 -0.0964 0.0327  312  LEU   A CD1 
1724  C  CD2 . LEU   A 243 ? 1.0260 1.1183 1.0295 -0.0336 -0.1021 0.0340  312  LEU   A CD2 
1725  N  N   . ASP   A 244 ? 1.0143 1.0648 0.9873 -0.0349 -0.0828 0.0401  313  ASP   A N   
1726  C  CA  . ASP   A 244 ? 1.0723 1.1100 1.0318 -0.0318 -0.0814 0.0423  313  ASP   A CA  
1727  C  C   . ASP   A 244 ? 1.0676 1.0969 1.0131 -0.0296 -0.0811 0.0432  313  ASP   A C   
1728  O  O   . ASP   A 244 ? 1.0631 1.0851 0.9965 -0.0254 -0.0843 0.0442  313  ASP   A O   
1729  C  CB  . ASP   A 244 ? 1.1250 1.1553 1.0859 -0.0341 -0.0743 0.0438  313  ASP   A CB  
1730  C  CG  . ASP   A 244 ? 1.1664 1.1904 1.1225 -0.0315 -0.0752 0.0452  313  ASP   A CG  
1731  O  OD1 . ASP   A 244 ? 1.1612 1.1893 1.1161 -0.0283 -0.0816 0.0446  313  ASP   A OD1 
1732  O  OD2 . ASP   A 244 ? 1.1853 1.2001 1.1390 -0.0326 -0.0693 0.0469  313  ASP   A OD2 
1733  N  N   . ILE   A 245 ? 1.0617 1.0911 1.0080 -0.0321 -0.0775 0.0428  314  ILE   A N   
1734  C  CA  . ILE   A 245 ? 1.0705 1.0923 1.0033 -0.0298 -0.0778 0.0433  314  ILE   A CA  
1735  C  C   . ILE   A 245 ? 1.0545 1.0814 0.9846 -0.0267 -0.0868 0.0418  314  ILE   A C   
1736  O  O   . ILE   A 245 ? 1.0571 1.0754 0.9734 -0.0227 -0.0897 0.0425  314  ILE   A O   
1737  C  CB  . ILE   A 245 ? 1.0318 1.0549 0.9680 -0.0331 -0.0730 0.0427  314  ILE   A CB  
1738  C  CG1 . ILE   A 245 ? 1.1172 1.1355 1.0573 -0.0362 -0.0639 0.0442  314  ILE   A CG1 
1739  C  CG2 . ILE   A 245 ? 0.9904 1.0050 0.9118 -0.0304 -0.0737 0.0431  314  ILE   A CG2 
1740  C  CD1 . ILE   A 245 ? 1.0628 1.0795 1.0031 -0.0385 -0.0582 0.0442  314  ILE   A CD1 
1741  N  N   . MET   A 246 ? 1.0533 1.0940 0.9968 -0.0285 -0.0911 0.0397  315  MET   A N   
1742  C  CA  . MET   A 246 ? 1.0464 1.0933 0.9900 -0.0262 -0.0993 0.0381  315  MET   A CA  
1743  C  C   . MET   A 246 ? 1.0716 1.1177 1.0118 -0.0222 -0.1047 0.0385  315  MET   A C   
1744  O  O   . MET   A 246 ? 1.0498 1.0991 0.9883 -0.0196 -0.1117 0.0374  315  MET   A O   
1745  C  CB  . MET   A 246 ? 1.0329 1.0945 0.9922 -0.0293 -0.1016 0.0360  315  MET   A CB  
1746  C  CG  . MET   A 246 ? 1.0135 1.0773 0.9773 -0.0332 -0.0971 0.0352  315  MET   A CG  
1747  S  SD  . MET   A 246 ? 1.0159 1.0964 0.9979 -0.0362 -0.1000 0.0329  315  MET   A SD  
1748  C  CE  . MET   A 246 ? 0.9638 1.0493 0.9449 -0.0328 -0.1091 0.0320  315  MET   A CE  
1749  N  N   . ASN   A 247 ? 1.0827 1.1247 1.0224 -0.0216 -0.1018 0.0401  316  ASN   A N   
1750  C  CA  . ASN   A 247 ? 1.0495 1.0904 0.9861 -0.0176 -0.1063 0.0406  316  ASN   A CA  
1751  C  C   . ASN   A 247 ? 1.0761 1.1014 0.9959 -0.0139 -0.1047 0.0428  316  ASN   A C   
1752  O  O   . ASN   A 247 ? 1.0560 1.0787 0.9695 -0.0095 -0.1099 0.0430  316  ASN   A O   
1753  C  CB  . ASN   A 247 ? 0.9719 1.0197 0.9204 -0.0192 -0.1051 0.0406  316  ASN   A CB  
1754  C  CG  . ASN   A 247 ? 1.0903 1.1534 1.0537 -0.0209 -0.1089 0.0386  316  ASN   A CG  
1755  O  OD1 . ASN   A 247 ? 1.0827 1.1518 1.0477 -0.0188 -0.1149 0.0375  316  ASN   A OD1 
1756  N  ND2 . ASN   A 247 ? 1.0925 1.1616 1.0670 -0.0244 -0.1054 0.0379  316  ASN   A ND2 
1757  N  N   . LYS   A 248 ? 1.0816 1.0964 0.9938 -0.0154 -0.0975 0.0443  317  LYS   A N   
1758  C  CA  . LYS   A 248 ? 1.0563 1.0552 0.9520 -0.0120 -0.0946 0.0467  317  LYS   A CA  
1759  C  C   . LYS   A 248 ? 1.0887 1.0767 0.9688 -0.0097 -0.0939 0.0473  317  LYS   A C   
1760  O  O   . LYS   A 248 ? 1.1329 1.1090 0.9974 -0.0050 -0.0956 0.0485  317  LYS   A O   
1761  C  CB  . LYS   A 248 ? 1.0840 1.0769 0.9818 -0.0149 -0.0860 0.0486  317  LYS   A CB  
1762  C  CG  . LYS   A 248 ? 1.0234 1.0238 0.9331 -0.0160 -0.0871 0.0483  317  LYS   A CG  
1763  C  CD  . LYS   A 248 ? 1.0681 1.0575 0.9735 -0.0164 -0.0807 0.0506  317  LYS   A CD  
1764  C  CE  . LYS   A 248 ? 1.1241 1.1200 1.0449 -0.0216 -0.0761 0.0500  317  LYS   A CE  
1765  N  NZ  . LYS   A 248 ? 1.1382 1.1465 1.0716 -0.0218 -0.0816 0.0481  317  LYS   A NZ  
1766  N  N   . CYS   A 249 ? 1.0930 1.0841 0.9763 -0.0127 -0.0916 0.0463  318  CYS   A N   
1767  C  CA  . CYS   A 249 ? 1.1108 1.0911 0.9790 -0.0105 -0.0906 0.0467  318  CYS   A CA  
1768  C  C   . CYS   A 249 ? 1.1111 1.0978 0.9792 -0.0087 -0.0996 0.0441  318  CYS   A C   
1769  O  O   . CYS   A 249 ? 1.1608 1.1519 1.0321 -0.0108 -0.0999 0.0426  318  CYS   A O   
1770  C  CB  . CYS   A 249 ? 1.1278 1.1063 0.9987 -0.0146 -0.0819 0.0474  318  CYS   A CB  
1771  S  SG  . CYS   A 249 ? 1.1203 1.0929 0.9947 -0.0172 -0.0720 0.0501  318  CYS   A SG  
1772  N  N   . THR   A 250 ? 1.1191 1.1060 0.9836 -0.0045 -0.1070 0.0436  319  THR   A N   
1773  C  CA  . THR   A 250 ? 1.1638 1.1574 1.0298 -0.0022 -0.1169 0.0412  319  THR   A CA  
1774  C  C   . THR   A 250 ? 1.2258 1.2065 1.0731 0.0023  -0.1203 0.0409  319  THR   A C   
1775  O  O   . THR   A 250 ? 1.2216 1.2065 1.0691 0.0046  -0.1292 0.0386  319  THR   A O   
1776  C  CB  . THR   A 250 ? 1.1145 1.1134 0.9853 0.0005  -0.1229 0.0409  319  THR   A CB  
1777  O  OG1 . THR   A 250 ? 1.1697 1.1539 1.0229 0.0059  -0.1238 0.0426  319  THR   A OG1 
1778  C  CG2 . THR   A 250 ? 1.1038 1.1100 0.9877 -0.0028 -0.1181 0.0419  319  THR   A CG2 
1779  N  N   . SER   A 251 ? 1.2560 1.2209 1.0872 0.0038  -0.1137 0.0431  320  SER   A N   
1780  C  CA  . SER   A 251 ? 1.2528 1.2033 1.0638 0.0087  -0.1164 0.0430  320  SER   A CA  
1781  C  C   . SER   A 251 ? 1.2392 1.1819 1.0434 0.0066  -0.1082 0.0440  320  SER   A C   
1782  O  O   . SER   A 251 ? 1.2556 1.1964 1.0632 0.0034  -0.0985 0.0461  320  SER   A O   
1783  C  CB  . SER   A 251 ? 1.2661 1.2013 1.0595 0.0145  -0.1166 0.0451  320  SER   A CB  
1784  O  OG  . SER   A 251 ? 1.2986 1.2414 1.0996 0.0162  -0.1230 0.0444  320  SER   A OG  
1785  N  N   . LEU   A 252 ? 1.1834 1.1215 0.9782 0.0087  -0.1123 0.0423  321  LEU   A N   
1786  C  CA  . LEU   A 252 ? 1.1848 1.1159 0.9729 0.0071  -0.1051 0.0430  321  LEU   A CA  
1787  C  C   . LEU   A 252 ? 1.1922 1.1025 0.9542 0.0134  -0.1046 0.0443  321  LEU   A C   
1788  O  O   . LEU   A 252 ? 1.1873 1.0931 0.9390 0.0180  -0.1140 0.0423  321  LEU   A O   
1789  C  CB  . LEU   A 252 ? 1.1320 1.0754 0.9318 0.0037  -0.1094 0.0400  321  LEU   A CB  
1790  C  CG  . LEU   A 252 ? 1.0493 1.0086 0.8711 -0.0031 -0.1046 0.0397  321  LEU   A CG  
1791  C  CD1 . LEU   A 252 ? 1.2005 1.1713 1.0373 -0.0048 -0.1067 0.0398  321  LEU   A CD1 
1792  C  CD2 . LEU   A 252 ? 1.0666 1.0362 0.8975 -0.0056 -0.1095 0.0367  321  LEU   A CD2 
1793  N  N   . CYS   A 253 ? 1.1403 1.0375 0.8916 0.0136  -0.0936 0.0475  322  CYS   A N   
1794  C  CA  . CYS   A 253 ? 1.1685 1.0442 0.8936 0.0198  -0.0915 0.0492  322  CYS   A CA  
1795  C  C   . CYS   A 253 ? 1.1875 1.0551 0.9042 0.0192  -0.0841 0.0499  322  CYS   A C   
1796  O  O   . CYS   A 253 ? 1.1740 1.0519 0.9055 0.0136  -0.0788 0.0496  322  CYS   A O   
1797  C  CB  . CYS   A 253 ? 1.1996 1.0636 0.9158 0.0219  -0.0843 0.0529  322  CYS   A CB  
1798  S  SG  . CYS   A 253 ? 1.2815 1.1552 1.0078 0.0227  -0.0927 0.0521  322  CYS   A SG  
1799  N  N   . CYS   A 254 ? 1.2029 1.0512 0.8945 0.0256  -0.0843 0.0507  323  CYS   A N   
1800  C  CA  . CYS   A 254 ? 1.2294 1.0654 0.9082 0.0264  -0.0755 0.0523  323  CYS   A CA  
1801  C  C   . CYS   A 254 ? 1.2476 1.0807 0.9314 0.0228  -0.0608 0.0562  323  CYS   A C   
1802  O  O   . CYS   A 254 ? 1.3410 1.1626 1.0150 0.0253  -0.0553 0.0594  323  CYS   A O   
1803  C  CB  . CYS   A 254 ? 1.2571 1.0709 0.9061 0.0348  -0.0782 0.0529  323  CYS   A CB  
1804  S  SG  . CYS   A 254 ? 1.2407 1.0339 0.8684 0.0376  -0.0653 0.0559  323  CYS   A SG  
1805  N  N   . LYS   A 255 ? 1.2381 1.0819 0.9377 0.0169  -0.0545 0.0560  324  LYS   A N   
1806  C  CA  . LYS   A 255 ? 1.2402 1.0824 0.9467 0.0132  -0.0407 0.0594  324  LYS   A CA  
1807  C  C   . LYS   A 255 ? 1.3216 1.1406 1.0041 0.0181  -0.0309 0.0632  324  LYS   A C   
1808  O  O   . LYS   A 255 ? 1.3765 1.1899 1.0604 0.0167  -0.0204 0.0667  324  LYS   A O   
1809  C  CB  . LYS   A 255 ? 1.2287 1.0841 0.9529 0.0072  -0.0365 0.0581  324  LYS   A CB  
1810  C  CG  . LYS   A 255 ? 1.2268 1.0893 0.9687 0.0014  -0.0260 0.0603  324  LYS   A CG  
1811  C  CD  . LYS   A 255 ? 1.3151 1.1753 1.0590 -0.0008 -0.0154 0.0615  324  LYS   A CD  
1812  C  CE  . LYS   A 255 ? 1.3771 1.2424 1.1377 -0.0061 -0.0048 0.0639  324  LYS   A CE  
1813  N  NZ  . LYS   A 255 ? 1.4927 1.3458 1.2442 -0.0038 -0.0001 0.0672  324  LYS   A NZ  
1814  N  N   . GLN   A 256 ? 1.4410 1.2459 1.1014 0.0241  -0.0341 0.0626  325  GLN   A N   
1815  C  CA  . GLN   A 256 ? 1.4616 1.2440 1.0983 0.0291  -0.0239 0.0662  325  GLN   A CA  
1816  C  C   . GLN   A 256 ? 1.4694 1.2345 1.0869 0.0348  -0.0227 0.0691  325  GLN   A C   
1817  O  O   . GLN   A 256 ? 1.5185 1.2708 1.1283 0.0355  -0.0101 0.0733  325  GLN   A O   
1818  C  CB  . GLN   A 256 ? 1.4967 1.2697 1.1158 0.0337  -0.0281 0.0643  325  GLN   A CB  
1819  C  CG  . GLN   A 256 ? 1.5290 1.3112 1.1610 0.0289  -0.0222 0.0636  325  GLN   A CG  
1820  C  CD  . GLN   A 256 ? 1.5675 1.3516 1.2117 0.0241  -0.0074 0.0673  325  GLN   A CD  
1821  O  OE1 . GLN   A 256 ? 1.6593 1.4266 1.2889 0.0273  0.0027  0.0713  325  GLN   A OE1 
1822  N  NE2 . GLN   A 256 ? 1.5262 1.3305 1.1976 0.0166  -0.0061 0.0659  325  GLN   A NE2 
1823  N  N   . CYS   A 257 ? 1.3971 1.1606 1.0062 0.0392  -0.0351 0.0669  326  CYS   A N   
1824  C  CA  . CYS   A 257 ? 1.4252 1.1720 1.0156 0.0451  -0.0346 0.0695  326  CYS   A CA  
1825  C  C   . CYS   A 257 ? 1.4073 1.1658 1.0133 0.0423  -0.0390 0.0693  326  CYS   A C   
1826  O  O   . CYS   A 257 ? 1.5141 1.2600 1.1070 0.0464  -0.0376 0.0716  326  CYS   A O   
1827  C  CB  . CYS   A 257 ? 1.4587 1.1910 1.0237 0.0537  -0.0454 0.0675  326  CYS   A CB  
1828  S  SG  . CYS   A 257 ? 1.4103 1.1624 0.9907 0.0527  -0.0644 0.0618  326  CYS   A SG  
1829  N  N   . GLN   A 258 ? 1.3965 1.1781 1.0288 0.0360  -0.0444 0.0664  327  GLN   A N   
1830  C  CA  . GLN   A 258 ? 1.4257 1.2195 1.0756 0.0323  -0.0463 0.0665  327  GLN   A CA  
1831  C  C   . GLN   A 258 ? 1.4601 1.2493 1.0996 0.0380  -0.0569 0.0655  327  GLN   A C   
1832  O  O   . GLN   A 258 ? 1.4617 1.2601 1.1137 0.0360  -0.0595 0.0655  327  GLN   A O   
1833  C  CB  . GLN   A 258 ? 1.3972 1.1849 1.0501 0.0295  -0.0324 0.0708  327  GLN   A CB  
1834  C  CG  . GLN   A 258 ? 1.4047 1.2084 1.0831 0.0211  -0.0252 0.0709  327  GLN   A CG  
1835  C  CD  . GLN   A 258 ? 1.4953 1.2951 1.1796 0.0184  -0.0148 0.0745  327  GLN   A CD  
1836  O  OE1 . GLN   A 258 ? 1.4472 1.2390 1.1231 0.0215  -0.0165 0.0759  327  GLN   A OE1 
1837  N  NE2 . GLN   A 258 ? 1.4733 1.2780 1.1718 0.0126  -0.0041 0.0759  327  GLN   A NE2 
1838  N  N   . GLU   A 259 ? 1.5485 1.3230 1.1647 0.0454  -0.0632 0.0647  328  GLU   A N   
1839  C  CA  . GLU   A 259 ? 1.5952 1.3632 1.1995 0.0516  -0.0730 0.0639  328  GLU   A CA  
1840  C  C   . GLU   A 259 ? 1.5492 1.3233 1.1521 0.0545  -0.0876 0.0593  328  GLU   A C   
1841  O  O   . GLU   A 259 ? 1.5844 1.3434 1.1650 0.0619  -0.0940 0.0584  328  GLU   A O   
1842  C  CB  . GLU   A 259 ? 1.6436 1.3851 1.2188 0.0588  -0.0667 0.0677  328  GLU   A CB  
1843  N  N   . THR   A 260 ? 1.4008 1.1969 1.0281 0.0485  -0.0930 0.0561  329  THR   A N   
1844  C  CA  . THR   A 260 ? 1.4158 1.2201 1.0459 0.0501  -0.1064 0.0516  329  THR   A CA  
1845  C  C   . THR   A 260 ? 1.3181 1.1479 0.9781 0.0427  -0.1105 0.0490  329  THR   A C   
1846  O  O   . THR   A 260 ? 1.2669 1.1062 0.9401 0.0369  -0.1048 0.0488  329  THR   A O   
1847  C  CB  . THR   A 260 ? 1.4006 1.1942 1.0154 0.0525  -0.1063 0.0505  329  THR   A CB  
1848  O  OG1 . THR   A 260 ? 1.4400 1.2088 1.0264 0.0592  -0.1004 0.0535  329  THR   A OG1 
1849  C  CG2 . THR   A 260 ? 1.3328 1.1325 0.9483 0.0551  -0.1217 0.0456  329  THR   A CG2 
1850  N  N   . GLU   A 261 ? 1.3179 1.1585 0.9882 0.0433  -0.1201 0.0470  330  GLU   A N   
1851  C  CA  . GLU   A 261 ? 1.2854 1.1494 0.9829 0.0372  -0.1244 0.0447  330  GLU   A CA  
1852  C  C   . GLU   A 261 ? 1.2768 1.1472 0.9772 0.0374  -0.1340 0.0407  330  GLU   A C   
1853  O  O   . GLU   A 261 ? 1.3289 1.1917 1.0164 0.0432  -0.1439 0.0387  330  GLU   A O   
1854  C  CB  . GLU   A 261 ? 1.3639 1.2361 1.0708 0.0382  -0.1302 0.0444  330  GLU   A CB  
1855  C  CG  . GLU   A 261 ? 1.3194 1.2147 1.0537 0.0322  -0.1334 0.0425  330  GLU   A CG  
1856  C  CD  . GLU   A 261 ? 1.3867 1.2879 1.1286 0.0333  -0.1365 0.0430  330  GLU   A CD  
1857  O  OE1 . GLU   A 261 ? 1.4630 1.3539 1.1907 0.0397  -0.1421 0.0432  330  GLU   A OE1 
1858  O  OE2 . GLU   A 261 ? 1.4349 1.3504 1.1964 0.0281  -0.1332 0.0434  330  GLU   A OE2 
1859  N  N   . ILE   A 262 ? 1.2578 1.1410 0.9743 0.0312  -0.1310 0.0396  331  ILE   A N   
1860  C  CA  . ILE   A 262 ? 1.2551 1.1440 0.9748 0.0306  -0.1389 0.0360  331  ILE   A CA  
1861  C  C   . ILE   A 262 ? 1.2706 1.1793 1.0120 0.0279  -0.1487 0.0330  331  ILE   A C   
1862  O  O   . ILE   A 262 ? 1.2651 1.1749 1.0047 0.0310  -0.1600 0.0299  331  ILE   A O   
1863  C  CB  . ILE   A 262 ? 1.2648 1.1558 0.9891 0.0257  -0.1303 0.0364  331  ILE   A CB  
1864  C  CG1 . ILE   A 262 ? 1.2089 1.0801 0.9120 0.0285  -0.1197 0.0397  331  ILE   A CG1 
1865  C  CG2 . ILE   A 262 ? 1.2465 1.1428 0.9737 0.0251  -0.1385 0.0327  331  ILE   A CG2 
1866  C  CD1 . ILE   A 262 ? 1.1913 1.0423 0.8674 0.0367  -0.1247 0.0395  331  ILE   A CD1 
1867  N  N   . THR   A 263 ? 1.2482 1.1723 1.0104 0.0224  -0.1444 0.0338  332  THR   A N   
1868  C  CA  . THR   A 263 ? 1.2430 1.1868 1.0275 0.0190  -0.1517 0.0313  332  THR   A CA  
1869  C  C   . THR   A 263 ? 1.2931 1.2483 1.0940 0.0152  -0.1464 0.0331  332  THR   A C   
1870  O  O   . THR   A 263 ? 1.2472 1.1967 1.0449 0.0138  -0.1365 0.0360  332  THR   A O   
1871  C  CB  . THR   A 263 ? 1.1734 1.1268 0.9687 0.0145  -0.1527 0.0289  332  THR   A CB  
1872  O  OG1 . THR   A 263 ? 1.1892 1.1582 1.0015 0.0130  -0.1622 0.0260  332  THR   A OG1 
1873  C  CG2 . THR   A 263 ? 1.1496 1.1099 0.9565 0.0083  -0.1417 0.0307  332  THR   A CG2 
1874  N  N   . THR   A 264 ? 1.3324 1.3034 1.1510 0.0137  -0.1531 0.0313  333  THR   A N   
1875  C  CA  . THR   A 264 ? 1.2795 1.2608 1.1125 0.0113  -0.1501 0.0326  333  THR   A CA  
1876  C  C   . THR   A 264 ? 1.2531 1.2531 1.1089 0.0053  -0.1498 0.0312  333  THR   A C   
1877  O  O   . THR   A 264 ? 1.2596 1.2666 1.1219 0.0040  -0.1553 0.0287  333  THR   A O   
1878  C  CB  . THR   A 264 ? 1.2889 1.2712 1.1213 0.0160  -0.1581 0.0322  333  THR   A CB  
1879  O  OG1 . THR   A 264 ? 1.3569 1.3577 1.2112 0.0130  -0.1617 0.0308  333  THR   A OG1 
1880  C  CG2 . THR   A 264 ? 1.3028 1.2776 1.1229 0.0213  -0.1680 0.0299  333  THR   A CG2 
1881  N  N   . LYS   A 265 ? 1.1758 1.1833 1.0434 0.0018  -0.1435 0.0328  334  LYS   A N   
1882  C  CA  . LYS   A 265 ? 1.1614 1.1848 1.0489 -0.0037 -0.1417 0.0317  334  LYS   A CA  
1883  C  C   . LYS   A 265 ? 1.1840 1.2198 1.0835 -0.0038 -0.1509 0.0290  334  LYS   A C   
1884  O  O   . LYS   A 265 ? 1.1917 1.2358 1.1008 -0.0075 -0.1513 0.0274  334  LYS   A O   
1885  C  CB  . LYS   A 265 ? 1.2204 1.2497 1.1181 -0.0059 -0.1364 0.0335  334  LYS   A CB  
1886  C  CG  . LYS   A 265 ? 1.2181 1.2636 1.1361 -0.0108 -0.1351 0.0325  334  LYS   A CG  
1887  C  CD  . LYS   A 265 ? 1.2220 1.2710 1.1476 -0.0124 -0.1298 0.0341  334  LYS   A CD  
1888  C  CE  . LYS   A 265 ? 1.2334 1.2983 1.1782 -0.0163 -0.1298 0.0329  334  LYS   A CE  
1889  N  NZ  . LYS   A 265 ? 1.1828 1.2500 1.1335 -0.0167 -0.1262 0.0343  334  LYS   A NZ  
1890  N  N   . ASN   A 266 ? 1.1618 1.1988 1.0609 0.0003  -0.1584 0.0284  335  ASN   A N   
1891  C  CA  . ASN   A 266 ? 1.1612 1.2116 1.0749 -0.0001 -0.1665 0.0261  335  ASN   A CA  
1892  C  C   . ASN   A 266 ? 1.2028 1.2533 1.1154 -0.0008 -0.1716 0.0236  335  ASN   A C   
1893  O  O   . ASN   A 266 ? 1.2637 1.3270 1.1917 -0.0036 -0.1753 0.0217  335  ASN   A O   
1894  C  CB  . ASN   A 266 ? 1.2076 1.2573 1.1192 0.0052  -0.1737 0.0258  335  ASN   A CB  
1895  C  CG  . ASN   A 266 ? 1.3878 1.4335 1.2958 0.0068  -0.1689 0.0284  335  ASN   A CG  
1896  O  OD1 . ASN   A 266 ? 1.4425 1.4952 1.3608 0.0033  -0.1626 0.0296  335  ASN   A OD1 
1897  N  ND2 . ASN   A 266 ? 1.4344 1.4682 1.3273 0.0124  -0.1719 0.0291  335  ASN   A ND2 
1898  N  N   . GLU   A 267 ? 1.1715 1.2075 1.0659 0.0016  -0.1716 0.0235  336  GLU   A N   
1899  C  CA  . GLU   A 267 ? 1.1902 1.2243 1.0812 0.0017  -0.1773 0.0209  336  GLU   A CA  
1900  C  C   . GLU   A 267 ? 1.1629 1.2011 1.0599 -0.0037 -0.1717 0.0206  336  GLU   A C   
1901  O  O   . GLU   A 267 ? 1.2079 1.2430 1.1005 -0.0039 -0.1754 0.0186  336  GLU   A O   
1902  C  CB  . GLU   A 267 ? 1.1953 1.2106 1.0623 0.0072  -0.1799 0.0209  336  GLU   A CB  
1903  C  CG  . GLU   A 267 ? 1.2509 1.2592 1.1087 0.0131  -0.1845 0.0216  336  GLU   A CG  
1904  C  CD  . GLU   A 267 ? 1.2908 1.3030 1.1520 0.0167  -0.1973 0.0186  336  GLU   A CD  
1905  O  OE1 . GLU   A 267 ? 1.3130 1.3309 1.1812 0.0148  -0.2029 0.0159  336  GLU   A OE1 
1906  O  OE2 . GLU   A 267 ? 1.2236 1.2331 1.0809 0.0214  -0.2019 0.0189  336  GLU   A OE2 
1907  N  N   . ILE   A 268 ? 1.1045 1.1496 1.0114 -0.0080 -0.1633 0.0222  337  ILE   A N   
1908  C  CA  . ILE   A 268 ? 1.1170 1.1661 1.0297 -0.0128 -0.1582 0.0218  337  ILE   A CA  
1909  C  C   . ILE   A 268 ? 1.1596 1.2243 1.0911 -0.0161 -0.1628 0.0197  337  ILE   A C   
1910  O  O   . ILE   A 268 ? 1.1672 1.2430 1.1124 -0.0167 -0.1648 0.0198  337  ILE   A O   
1911  C  CB  . ILE   A 268 ? 1.1003 1.1496 1.0157 -0.0158 -0.1475 0.0242  337  ILE   A CB  
1912  C  CG1 . ILE   A 268 ? 1.0705 1.1032 0.9670 -0.0135 -0.1415 0.0262  337  ILE   A CG1 
1913  C  CG2 . ILE   A 268 ? 1.1084 1.1676 1.0368 -0.0212 -0.1437 0.0234  337  ILE   A CG2 
1914  C  CD1 . ILE   A 268 ? 0.9855 1.0179 0.8851 -0.0163 -0.1313 0.0285  337  ILE   A CD1 
1915  N  N   . PHE   A 269 ? 1.1536 1.2187 1.0855 -0.0182 -0.1643 0.0179  338  PHE   A N   
1916  C  CA  . PHE   A 269 ? 1.1537 1.2326 1.1031 -0.0219 -0.1675 0.0160  338  PHE   A CA  
1917  C  C   . PHE   A 269 ? 1.1532 1.2308 1.1016 -0.0255 -0.1633 0.0153  338  PHE   A C   
1918  O  O   . PHE   A 269 ? 1.1352 1.2017 1.0700 -0.0248 -0.1581 0.0163  338  PHE   A O   
1919  C  CB  . PHE   A 269 ? 1.1998 1.2815 1.1523 -0.0197 -0.1785 0.0136  338  PHE   A CB  
1920  C  CG  . PHE   A 269 ? 1.2521 1.3238 1.1922 -0.0182 -0.1834 0.0115  338  PHE   A CG  
1921  C  CD1 . PHE   A 269 ? 1.2610 1.3165 1.1799 -0.0136 -0.1840 0.0119  338  PHE   A CD1 
1922  C  CD2 . PHE   A 269 ? 1.2656 1.3434 1.2144 -0.0211 -0.1875 0.0091  338  PHE   A CD2 
1923  C  CE1 . PHE   A 269 ? 1.2351 1.2801 1.1410 -0.0118 -0.1887 0.0098  338  PHE   A CE1 
1924  C  CE2 . PHE   A 269 ? 1.2636 1.3314 1.2002 -0.0196 -0.1924 0.0069  338  PHE   A CE2 
1925  C  CZ  . PHE   A 269 ? 1.2395 1.2909 1.1545 -0.0148 -0.1932 0.0072  338  PHE   A CZ  
1926  N  N   . SER   A 270 ? 1.2235 1.3124 1.1866 -0.0292 -0.1650 0.0138  339  SER   A N   
1927  C  CA  . SER   A 270 ? 1.2322 1.3206 1.1953 -0.0325 -0.1617 0.0129  339  SER   A CA  
1928  C  C   . SER   A 270 ? 1.2607 1.3508 1.2264 -0.0328 -0.1700 0.0101  339  SER   A C   
1929  O  O   . SER   A 270 ? 1.2702 1.3707 1.2499 -0.0337 -0.1754 0.0090  339  SER   A O   
1930  C  CB  . SER   A 270 ? 1.2017 1.3013 1.1797 -0.0369 -0.1553 0.0138  339  SER   A CB  
1931  O  OG  . SER   A 270 ? 1.2328 1.3297 1.2078 -0.0369 -0.1474 0.0161  339  SER   A OG  
1932  N  N   . LEU   A 271 ? 1.2998 1.3792 1.2523 -0.0320 -0.1709 0.0089  340  LEU   A N   
1933  C  CA  . LEU   A 271 ? 1.3463 1.4253 1.2993 -0.0318 -0.1797 0.0059  340  LEU   A CA  
1934  C  C   . LEU   A 271 ? 1.3751 1.4655 1.3442 -0.0368 -0.1791 0.0048  340  LEU   A C   
1935  O  O   . LEU   A 271 ? 1.3988 1.4985 1.3813 -0.0382 -0.1854 0.0032  340  LEU   A O   
1936  C  CB  . LEU   A 271 ? 1.2998 1.3628 1.2322 -0.0288 -0.1812 0.0049  340  LEU   A CB  
1937  C  CG  . LEU   A 271 ? 1.2542 1.3143 1.1846 -0.0278 -0.1916 0.0015  340  LEU   A CG  
1938  C  CD1 . LEU   A 271 ? 1.4132 1.4799 1.3539 -0.0325 -0.1913 -0.0001 340  LEU   A CD1 
1939  C  CD2 . LEU   A 271 ? 1.2619 1.3290 1.2020 -0.0261 -0.2008 0.0003  340  LEU   A CD2 
1940  N  N   . SER   A 272 ? 1.3354 1.4252 1.3035 -0.0396 -0.1714 0.0056  341  SER   A N   
1941  C  CA  . SER   A 272 ? 1.4278 1.5277 1.4103 -0.0441 -0.1701 0.0047  341  SER   A CA  
1942  C  C   . SER   A 272 ? 1.4477 1.5580 1.4430 -0.0466 -0.1631 0.0068  341  SER   A C   
1943  O  O   . SER   A 272 ? 1.4351 1.5490 1.4341 -0.0451 -0.1628 0.0083  341  SER   A O   
1944  C  CB  . SER   A 272 ? 1.5532 1.6458 1.5269 -0.0455 -0.1670 0.0038  341  SER   A CB  
1945  O  OG  . SER   A 272 ? 1.6066 1.7081 1.5927 -0.0498 -0.1627 0.0038  341  SER   A OG  
1946  N  N   . LEU   A 273 ? 1.4539 1.5687 1.4556 -0.0501 -0.1579 0.0069  342  LEU   A N   
1947  C  CA  . LEU   A 273 ? 1.4999 1.6229 1.5116 -0.0521 -0.1510 0.0087  342  LEU   A CA  
1948  C  C   . LEU   A 273 ? 1.5126 1.6280 1.5138 -0.0509 -0.1438 0.0105  342  LEU   A C   
1949  O  O   . LEU   A 273 ? 1.4828 1.5989 1.4844 -0.0495 -0.1414 0.0122  342  LEU   A O   
1950  C  CB  . LEU   A 273 ? 1.5507 1.6810 1.5731 -0.0560 -0.1488 0.0079  342  LEU   A CB  
1951  C  CG  . LEU   A 273 ? 1.5484 1.6832 1.5785 -0.0573 -0.1560 0.0059  342  LEU   A CG  
1952  C  CD1 . LEU   A 273 ? 1.4153 1.5466 1.4424 -0.0595 -0.1558 0.0042  342  LEU   A CD1 
1953  C  CD2 . LEU   A 273 ? 1.5595 1.7072 1.6072 -0.0591 -0.1563 0.0065  342  LEU   A CD2 
1954  N  N   . CYS   A 274 ? 1.5110 1.6190 1.5032 -0.0514 -0.1403 0.0101  343  CYS   A N   
1955  C  CA  . CYS   A 274 ? 1.4929 1.5901 1.4714 -0.0496 -0.1346 0.0114  343  CYS   A CA  
1956  C  C   . CYS   A 274 ? 1.4437 1.5405 1.4218 -0.0481 -0.1307 0.0137  343  CYS   A C   
1957  O  O   . CYS   A 274 ? 1.3726 1.4701 1.3529 -0.0494 -0.1235 0.0150  343  CYS   A O   
1958  C  CB  . CYS   A 274 ? 1.4945 1.5792 1.4566 -0.0464 -0.1391 0.0104  343  CYS   A CB  
1959  S  SG  . CYS   A 274 ? 1.5847 1.6677 1.5437 -0.0427 -0.1491 0.0097  343  CYS   A SG  
1960  N  N   . GLY   A 275 ? 1.3544 1.4496 1.3295 -0.0453 -0.1356 0.0140  344  GLY   A N   
1961  C  CA  . GLY   A 275 ? 1.3097 1.4031 1.2829 -0.0436 -0.1324 0.0161  344  GLY   A CA  
1962  C  C   . GLY   A 275 ? 1.2991 1.3815 1.2576 -0.0392 -0.1361 0.0165  344  GLY   A C   
1963  O  O   . GLY   A 275 ? 1.3074 1.3841 1.2577 -0.0373 -0.1421 0.0149  344  GLY   A O   
1964  N  N   . PRO   A 276 ? 1.2086 1.2872 1.1630 -0.0373 -0.1327 0.0186  345  PRO   A N   
1965  C  CA  . PRO   A 276 ? 1.1462 1.2136 1.0858 -0.0327 -0.1359 0.0192  345  PRO   A CA  
1966  C  C   . PRO   A 276 ? 1.1882 1.2408 1.1105 -0.0308 -0.1303 0.0204  345  PRO   A C   
1967  O  O   . PRO   A 276 ? 1.1826 1.2237 1.0896 -0.0267 -0.1337 0.0204  345  PRO   A O   
1968  C  CB  . PRO   A 276 ? 1.0949 1.1664 1.0402 -0.0319 -0.1348 0.0209  345  PRO   A CB  
1969  C  CG  . PRO   A 276 ? 1.1578 1.2353 1.1128 -0.0355 -0.1270 0.0219  345  PRO   A CG  
1970  C  CD  . PRO   A 276 ? 1.2114 1.2965 1.1755 -0.0391 -0.1271 0.0202  345  PRO   A CD  
1971  N  N   . MET   A 277 ? 1.1653 1.2174 1.0893 -0.0335 -0.1217 0.0215  346  MET   A N   
1972  C  CA  . MET   A 277 ? 1.0938 1.1324 1.0025 -0.0319 -0.1156 0.0227  346  MET   A CA  
1973  C  C   . MET   A 277 ? 1.1175 1.1600 1.0325 -0.0356 -0.1103 0.0221  346  MET   A C   
1974  O  O   . MET   A 277 ? 1.0696 1.1135 0.9895 -0.0378 -0.1023 0.0235  346  MET   A O   
1975  C  CB  . MET   A 277 ? 1.0565 1.0876 0.9588 -0.0304 -0.1089 0.0256  346  MET   A CB  
1976  C  CG  . MET   A 277 ? 1.1584 1.1811 1.0541 -0.0311 -0.0989 0.0273  346  MET   A CG  
1977  S  SD  . MET   A 277 ? 1.1860 1.1992 1.0751 -0.0298 -0.0898 0.0308  346  MET   A SD  
1978  C  CE  . MET   A 277 ? 1.1559 1.1810 1.0597 -0.0310 -0.0939 0.0309  346  MET   A CE  
1979  N  N   . ALA   A 278 ? 1.1656 1.2100 1.0808 -0.0362 -0.1151 0.0198  347  ALA   A N   
1980  C  CA  . ALA   A 278 ? 1.1994 1.2455 1.1180 -0.0390 -0.1103 0.0192  347  ALA   A CA  
1981  C  C   . ALA   A 278 ? 1.1708 1.2023 1.0724 -0.0366 -0.1046 0.0203  347  ALA   A C   
1982  O  O   . ALA   A 278 ? 1.1453 1.1646 1.0314 -0.0325 -0.1052 0.0214  347  ALA   A O   
1983  C  CB  . ALA   A 278 ? 1.1625 1.2154 1.0875 -0.0407 -0.1169 0.0165  347  ALA   A CB  
1984  N  N   . ALA   A 279 ? 1.1369 1.1691 1.0408 -0.0387 -0.0990 0.0201  348  ALA   A N   
1985  C  CA  . ALA   A 279 ? 1.1044 1.1234 0.9931 -0.0365 -0.0933 0.0209  348  ALA   A CA  
1986  C  C   . ALA   A 279 ? 1.1256 1.1406 1.0068 -0.0355 -0.0988 0.0185  348  ALA   A C   
1987  O  O   . ALA   A 279 ? 1.2410 1.2652 1.1331 -0.0386 -0.1010 0.0166  348  ALA   A O   
1988  C  CB  . ALA   A 279 ? 1.0488 1.0708 0.9452 -0.0393 -0.0833 0.0222  348  ALA   A CB  
1989  N  N   . TYR   A 280 ? 1.1218 1.1222 0.9836 -0.0311 -0.1010 0.0185  349  TYR   A N   
1990  C  CA  . TYR   A 280 ? 1.1745 1.1688 1.0268 -0.0295 -0.1066 0.0161  349  TYR   A CA  
1991  C  C   . TYR   A 280 ? 1.2090 1.1888 1.0445 -0.0267 -0.0992 0.0172  349  TYR   A C   
1992  O  O   . TYR   A 280 ? 1.2113 1.1831 1.0389 -0.0248 -0.0914 0.0200  349  TYR   A O   
1993  C  CB  . TYR   A 280 ? 1.2048 1.1937 1.0479 -0.0261 -0.1174 0.0144  349  TYR   A CB  
1994  C  CG  . TYR   A 280 ? 1.2166 1.2192 1.0758 -0.0283 -0.1249 0.0133  349  TYR   A CG  
1995  C  CD1 . TYR   A 280 ? 1.2183 1.2320 1.0909 -0.0315 -0.1314 0.0108  349  TYR   A CD1 
1996  C  CD2 . TYR   A 280 ? 1.2101 1.2138 1.0707 -0.0269 -0.1251 0.0150  349  TYR   A CD2 
1997  C  CE1 . TYR   A 280 ? 1.2121 1.2381 1.0994 -0.0332 -0.1375 0.0100  349  TYR   A CE1 
1998  C  CE2 . TYR   A 280 ? 1.2342 1.2502 1.1093 -0.0286 -0.1315 0.0141  349  TYR   A CE2 
1999  C  CZ  . TYR   A 280 ? 1.2294 1.2566 1.1180 -0.0317 -0.1375 0.0117  349  TYR   A CZ  
2000  O  OH  . TYR   A 280 ? 1.2257 1.2648 1.1288 -0.0331 -0.1430 0.0111  349  TYR   A OH  
2001  N  N   . VAL   A 281 ? 1.2590 1.2353 1.0892 -0.0265 -0.1013 0.0152  350  VAL   A N   
2002  C  CA  . VAL   A 281 ? 1.2837 1.2466 1.0983 -0.0238 -0.0941 0.0162  350  VAL   A CA  
2003  C  C   . VAL   A 281 ? 1.3215 1.2693 1.1152 -0.0188 -0.1010 0.0145  350  VAL   A C   
2004  O  O   . VAL   A 281 ? 1.2911 1.2419 1.0867 -0.0192 -0.1114 0.0115  350  VAL   A O   
2005  C  CB  . VAL   A 281 ? 1.2516 1.2213 1.0760 -0.0272 -0.0891 0.0155  350  VAL   A CB  
2006  C  CG1 . VAL   A 281 ? 1.2810 1.2375 1.0910 -0.0243 -0.0791 0.0174  350  VAL   A CG1 
2007  C  CG2 . VAL   A 281 ? 1.2757 1.2623 1.1229 -0.0324 -0.0854 0.0162  350  VAL   A CG2 
2008  N  N   . ASN   A 282 ? 1.3952 1.3263 1.1688 -0.0140 -0.0951 0.0164  351  ASN   A N   
2009  C  CA  . ASN   A 282 ? 1.3835 1.2977 1.1343 -0.0085 -0.1006 0.0149  351  ASN   A CA  
2010  C  C   . ASN   A 282 ? 1.4070 1.3151 1.1507 -0.0080 -0.0966 0.0141  351  ASN   A C   
2011  O  O   . ASN   A 282 ? 1.3639 1.2790 1.1183 -0.0112 -0.0878 0.0153  351  ASN   A O   
2012  C  CB  . ASN   A 282 ? 1.3416 1.2394 1.0724 -0.0027 -0.0969 0.0176  351  ASN   A CB  
2013  C  CG  . ASN   A 282 ? 1.3642 1.2506 1.0837 -0.0005 -0.0832 0.0209  351  ASN   A CG  
2014  O  OD1 . ASN   A 282 ? 1.4361 1.3292 1.1659 -0.0039 -0.0754 0.0216  351  ASN   A OD1 
2015  N  ND2 . ASN   A 282 ? 1.3395 1.2085 1.0378 0.0053  -0.0800 0.0231  351  ASN   A ND2 
2016  N  N   . PRO   A 283 ? 1.4508 1.3454 1.1761 -0.0037 -0.1031 0.0119  352  PRO   A N   
2017  C  CA  . PRO   A 283 ? 1.4319 1.3203 1.1498 -0.0030 -0.1003 0.0107  352  PRO   A CA  
2018  C  C   . PRO   A 283 ? 1.4487 1.3300 1.1600 -0.0015 -0.0858 0.0141  352  PRO   A C   
2019  O  O   . PRO   A 283 ? 1.4597 1.3367 1.1661 -0.0010 -0.0820 0.0135  352  PRO   A O   
2020  C  CB  . PRO   A 283 ? 1.4335 1.3050 1.1285 0.0029  -0.1098 0.0082  352  PRO   A CB  
2021  C  CG  . PRO   A 283 ? 1.4064 1.2801 1.1029 0.0038  -0.1199 0.0071  352  PRO   A CG  
2022  C  CD  . PRO   A 283 ? 1.4391 1.3218 1.1477 0.0015  -0.1129 0.0105  352  PRO   A CD  
2023  N  N   . HIS   A 284 ? 1.4380 1.3175 1.1490 -0.0008 -0.0773 0.0178  353  HIS   A N   
2024  C  CA  . HIS   A 284 ? 1.4681 1.3402 1.1732 0.0007  -0.0630 0.0212  353  HIS   A CA  
2025  C  C   . HIS   A 284 ? 1.4409 1.3284 1.1687 -0.0047 -0.0543 0.0235  353  HIS   A C   
2026  O  O   . HIS   A 284 ? 1.4687 1.3508 1.1936 -0.0035 -0.0426 0.0270  353  HIS   A O   
2027  C  CB  . HIS   A 284 ? 1.4791 1.3307 1.1593 0.0075  -0.0589 0.0237  353  HIS   A CB  
2028  C  CG  . HIS   A 284 ? 1.5330 1.3665 1.1879 0.0137  -0.0654 0.0217  353  HIS   A CG  
2029  N  ND1 . HIS   A 284 ? 1.5555 1.3808 1.2002 0.0158  -0.0621 0.0209  353  HIS   A ND1 
2030  C  CD2 . HIS   A 284 ? 1.5400 1.3619 1.1777 0.0186  -0.0755 0.0201  353  HIS   A CD2 
2031  C  CE1 . HIS   A 284 ? 1.5876 1.3965 1.2094 0.0216  -0.0699 0.0188  353  HIS   A CE1 
2032  N  NE2 . HIS   A 284 ? 1.5297 1.3362 1.1470 0.0234  -0.0783 0.0182  353  HIS   A NE2 
2033  N  N   . GLY   A 285 ? 1.4643 1.3706 1.2147 -0.0104 -0.0596 0.0216  354  GLY   A N   
2034  C  CA  . GLY   A 285 ? 1.4987 1.4199 1.2710 -0.0155 -0.0528 0.0233  354  GLY   A CA  
2035  C  C   . GLY   A 285 ? 1.4858 1.4080 1.2615 -0.0156 -0.0499 0.0259  354  GLY   A C   
2036  O  O   . GLY   A 285 ? 1.4986 1.4342 1.2938 -0.0200 -0.0461 0.0268  354  GLY   A O   
2037  N  N   . TYR   A 286 ? 1.3790 1.2870 1.1361 -0.0107 -0.0515 0.0271  355  TYR   A N   
2038  C  CA  . TYR   A 286 ? 1.3139 1.2233 1.0742 -0.0108 -0.0508 0.0292  355  TYR   A CA  
2039  C  C   . TYR   A 286 ? 1.3226 1.2490 1.1017 -0.0150 -0.0603 0.0270  355  TYR   A C   
2040  O  O   . TYR   A 286 ? 1.3042 1.2342 1.0838 -0.0152 -0.0710 0.0239  355  TYR   A O   
2041  C  CB  . TYR   A 286 ? 1.3128 1.2032 1.0481 -0.0042 -0.0530 0.0303  355  TYR   A CB  
2042  C  CG  . TYR   A 286 ? 1.3261 1.1995 1.0436 0.0000  -0.0413 0.0334  355  TYR   A CG  
2043  C  CD1 . TYR   A 286 ? 1.3358 1.2101 1.0605 -0.0016 -0.0286 0.0371  355  TYR   A CD1 
2044  C  CD2 . TYR   A 286 ? 1.3221 1.1785 1.0163 0.0057  -0.0425 0.0328  355  TYR   A CD2 
2045  C  CE1 . TYR   A 286 ? 1.2691 1.1281 0.9788 0.0021  -0.0170 0.0402  355  TYR   A CE1 
2046  C  CE2 . TYR   A 286 ? 1.3626 1.2027 1.0400 0.0099  -0.0309 0.0359  355  TYR   A CE2 
2047  C  CZ  . TYR   A 286 ? 1.2913 1.1332 0.9771 0.0080  -0.0179 0.0397  355  TYR   A CZ  
2048  O  OH  . TYR   A 286 ? 1.2806 1.1070 0.9513 0.0119  -0.0055 0.0431  355  TYR   A OH  
2049  N  N   . VAL   A 287 ? 1.2840 1.2207 1.0789 -0.0185 -0.0563 0.0287  356  VAL   A N   
2050  C  CA  . VAL   A 287 ? 1.2399 1.1927 1.0532 -0.0224 -0.0638 0.0271  356  VAL   A CA  
2051  C  C   . VAL   A 287 ? 1.1894 1.1384 0.9978 -0.0202 -0.0667 0.0285  356  VAL   A C   
2052  O  O   . VAL   A 287 ? 1.2866 1.2239 1.0833 -0.0172 -0.0600 0.0313  356  VAL   A O   
2053  C  CB  . VAL   A 287 ? 1.2351 1.2036 1.0713 -0.0280 -0.0581 0.0274  356  VAL   A CB  
2054  C  CG1 . VAL   A 287 ? 1.0904 1.0750 0.9443 -0.0317 -0.0664 0.0253  356  VAL   A CG1 
2055  C  CG2 . VAL   A 287 ? 1.2491 1.2185 1.0878 -0.0293 -0.0528 0.0267  356  VAL   A CG2 
2056  N  N   . HIS   A 288 ? 1.1568 1.1156 0.9742 -0.0215 -0.0766 0.0265  357  HIS   A N   
2057  C  CA  . HIS   A 288 ? 1.1389 1.0943 0.9509 -0.0189 -0.0816 0.0272  357  HIS   A CA  
2058  C  C   . HIS   A 288 ? 1.0944 1.0670 0.9268 -0.0228 -0.0870 0.0261  357  HIS   A C   
2059  O  O   . HIS   A 288 ? 1.0993 1.0793 0.9377 -0.0236 -0.0965 0.0234  357  HIS   A O   
2060  C  CB  . HIS   A 288 ? 1.1294 1.0732 0.9231 -0.0138 -0.0907 0.0255  357  HIS   A CB  
2061  C  CG  . HIS   A 288 ? 1.2032 1.1267 0.9725 -0.0084 -0.0857 0.0271  357  HIS   A CG  
2062  N  ND1 . HIS   A 288 ? 1.2121 1.1231 0.9674 -0.0043 -0.0820 0.0299  357  HIS   A ND1 
2063  C  CD2 . HIS   A 288 ? 1.2836 1.1964 1.0391 -0.0059 -0.0839 0.0265  357  HIS   A CD2 
2064  C  CE1 . HIS   A 288 ? 1.2798 1.1731 1.0136 0.0004  -0.0778 0.0309  357  HIS   A CE1 
2065  N  NE2 . HIS   A 288 ? 1.2571 1.1511 0.9905 -0.0004 -0.0789 0.0289  357  HIS   A NE2 
2066  N  N   . GLU   A 289 ? 1.0775 1.0557 0.9203 -0.0250 -0.0813 0.0282  358  GLU   A N   
2067  C  CA  . GLU   A 289 ? 1.0757 1.0665 0.9331 -0.0270 -0.0868 0.0276  358  GLU   A CA  
2068  C  C   . GLU   A 289 ? 1.0770 1.0611 0.9229 -0.0227 -0.0953 0.0271  358  GLU   A C   
2069  O  O   . GLU   A 289 ? 1.0761 1.0484 0.9088 -0.0191 -0.0925 0.0293  358  GLU   A O   
2070  C  CB  . GLU   A 289 ? 1.0672 1.0622 0.9347 -0.0294 -0.0789 0.0300  358  GLU   A CB  
2071  C  CG  . GLU   A 289 ? 1.1147 1.1089 0.9859 -0.0317 -0.0684 0.0313  358  GLU   A CG  
2072  C  CD  . GLU   A 289 ? 1.2252 1.2275 1.1119 -0.0353 -0.0620 0.0328  358  GLU   A CD  
2073  O  OE1 . GLU   A 289 ? 1.2139 1.2291 1.1159 -0.0380 -0.0662 0.0316  358  GLU   A OE1 
2074  O  OE2 . GLU   A 289 ? 1.2462 1.2415 1.1298 -0.0353 -0.0526 0.0351  358  GLU   A OE2 
2075  N  N   . THR   A 290 ? 1.0672 1.0584 0.9182 -0.0229 -0.1055 0.0244  359  THR   A N   
2076  C  CA  . THR   A 290 ? 1.0844 1.0687 0.9240 -0.0184 -0.1148 0.0233  359  THR   A CA  
2077  C  C   . THR   A 290 ? 1.0878 1.0846 0.9414 -0.0194 -0.1220 0.0224  359  THR   A C   
2078  O  O   . THR   A 290 ? 1.0814 1.0891 0.9469 -0.0216 -0.1288 0.0200  359  THR   A O   
2079  C  CB  . THR   A 290 ? 1.0816 1.0606 0.9121 -0.0166 -0.1217 0.0205  359  THR   A CB  
2080  O  OG1 . THR   A 290 ? 1.0936 1.0615 0.9115 -0.0156 -0.1146 0.0214  359  THR   A OG1 
2081  C  CG2 . THR   A 290 ? 1.0684 1.0376 0.8845 -0.0111 -0.1311 0.0195  359  THR   A CG2 
2082  N  N   . LEU   A 291 ? 1.0492 1.0432 0.9004 -0.0175 -0.1204 0.0244  360  LEU   A N   
2083  C  CA  . LEU   A 291 ? 1.0437 1.0478 0.9061 -0.0176 -0.1268 0.0239  360  LEU   A CA  
2084  C  C   . LEU   A 291 ? 1.0354 1.0367 0.8914 -0.0140 -0.1383 0.0215  360  LEU   A C   
2085  O  O   . LEU   A 291 ? 1.0765 1.0635 0.9139 -0.0090 -0.1406 0.0217  360  LEU   A O   
2086  C  CB  . LEU   A 291 ? 1.0519 1.0514 0.9107 -0.0160 -0.1220 0.0267  360  LEU   A CB  
2087  C  CG  . LEU   A 291 ? 1.0148 1.0216 0.8816 -0.0149 -0.1278 0.0266  360  LEU   A CG  
2088  C  CD1 . LEU   A 291 ? 1.0430 1.0668 0.9318 -0.0199 -0.1262 0.0263  360  LEU   A CD1 
2089  C  CD2 . LEU   A 291 ? 1.0381 1.0340 0.8934 -0.0115 -0.1238 0.0293  360  LEU   A CD2 
2090  N  N   . THR   A 292 ? 1.0465 1.0612 0.9178 -0.0163 -0.1453 0.0192  361  THR   A N   
2091  C  CA  . THR   A 292 ? 1.0315 1.0461 0.9007 -0.0134 -0.1567 0.0167  361  THR   A CA  
2092  C  C   . THR   A 292 ? 1.0752 1.0934 0.9485 -0.0111 -0.1606 0.0174  361  THR   A C   
2093  O  O   . THR   A 292 ? 1.0867 1.1162 0.9746 -0.0138 -0.1574 0.0186  361  THR   A O   
2094  C  CB  . THR   A 292 ? 1.1327 1.1600 1.0176 -0.0173 -0.1619 0.0140  361  THR   A CB  
2095  O  OG1 . THR   A 292 ? 1.1732 1.2165 1.0786 -0.0215 -0.1595 0.0146  361  THR   A OG1 
2096  C  CG2 . THR   A 292 ? 1.1369 1.1603 1.0175 -0.0196 -0.1574 0.0133  361  THR   A CG2 
2097  N  N   . VAL   A 293 ? 1.1488 1.1566 1.0080 -0.0057 -0.1673 0.0168  362  VAL   A N   
2098  C  CA  . VAL   A 293 ? 1.1685 1.1786 1.0301 -0.0027 -0.1716 0.0174  362  VAL   A CA  
2099  C  C   . VAL   A 293 ? 1.2139 1.2232 1.0733 0.0009  -0.1842 0.0144  362  VAL   A C   
2100  O  O   . VAL   A 293 ? 1.2366 1.2376 1.0853 0.0027  -0.1889 0.0123  362  VAL   A O   
2101  C  CB  . VAL   A 293 ? 1.0964 1.0925 0.9412 0.0012  -0.1659 0.0204  362  VAL   A CB  
2102  C  CG1 . VAL   A 293 ? 1.0519 1.0500 0.9015 -0.0026 -0.1539 0.0232  362  VAL   A CG1 
2103  C  CG2 . VAL   A 293 ? 1.1693 1.1469 0.9906 0.0059  -0.1669 0.0201  362  VAL   A CG2 
2104  N  N   . TYR   A 294 ? 1.2633 1.2812 1.1331 0.0021  -0.1898 0.0140  363  TYR   A N   
2105  C  CA  . TYR   A 294 ? 1.2587 1.2775 1.1292 0.0054  -0.2023 0.0110  363  TYR   A CA  
2106  C  C   . TYR   A 294 ? 1.2473 1.2477 1.0940 0.0124  -0.2069 0.0107  363  TYR   A C   
2107  O  O   . TYR   A 294 ? 1.3109 1.3045 1.1492 0.0150  -0.2152 0.0079  363  TYR   A O   
2108  C  CB  . TYR   A 294 ? 1.2591 1.2927 1.1484 0.0050  -0.2066 0.0108  363  TYR   A CB  
2109  C  CG  . TYR   A 294 ? 1.2905 1.3418 1.2031 -0.0008 -0.2069 0.0096  363  TYR   A CG  
2110  C  CD1 . TYR   A 294 ? 1.2841 1.3367 1.1993 -0.0040 -0.2082 0.0075  363  TYR   A CD1 
2111  C  CD2 . TYR   A 294 ? 1.2803 1.3462 1.2115 -0.0030 -0.2054 0.0106  363  TYR   A CD2 
2112  C  CE1 . TYR   A 294 ? 1.2809 1.3488 1.2167 -0.0093 -0.2080 0.0066  363  TYR   A CE1 
2113  C  CE2 . TYR   A 294 ? 1.3158 1.3971 1.2675 -0.0080 -0.2050 0.0097  363  TYR   A CE2 
2114  C  CZ  . TYR   A 294 ? 1.3158 1.3978 1.2696 -0.0112 -0.2063 0.0078  363  TYR   A CZ  
2115  O  OH  . TYR   A 294 ? 1.3206 1.4169 1.2940 -0.0161 -0.2055 0.0071  363  TYR   A OH  
2116  N  N   . LYS   A 295 ? 1.2229 1.2144 1.0581 0.0157  -0.2019 0.0135  364  LYS   A N   
2117  C  CA  . LYS   A 295 ? 1.2214 1.1942 1.0326 0.0228  -0.2054 0.0137  364  LYS   A CA  
2118  C  C   . LYS   A 295 ? 1.2898 1.2488 1.0843 0.0236  -0.1936 0.0174  364  LYS   A C   
2119  O  O   . LYS   A 295 ? 1.3159 1.2811 1.1193 0.0201  -0.1845 0.0201  364  LYS   A O   
2120  C  CB  . LYS   A 295 ? 1.1015 1.0765 0.9148 0.0273  -0.2131 0.0133  364  LYS   A CB  
2121  N  N   . ALA   A 296 ? 1.2933 1.2334 1.0640 0.0284  -0.1936 0.0175  365  ALA   A N   
2122  C  CA  . ALA   A 296 ? 1.2654 1.1893 1.0172 0.0307  -0.1832 0.0211  365  ALA   A CA  
2123  C  C   . ALA   A 296 ? 1.3523 1.2574 1.0798 0.0391  -0.1888 0.0210  365  ALA   A C   
2124  O  O   . ALA   A 296 ? 1.3629 1.2653 1.0855 0.0430  -0.2005 0.0178  365  ALA   A O   
2125  C  CB  . ALA   A 296 ? 1.2248 1.1421 0.9694 0.0281  -0.1749 0.0218  365  ALA   A CB  
2126  N  N   . CYS   A 297 ? 1.3569 1.2482 1.0688 0.0420  -0.1804 0.0246  366  CYS   A N   
2127  C  CA  . CYS   A 297 ? 1.3916 1.2643 1.0795 0.0503  -0.1851 0.0249  366  CYS   A CA  
2128  C  C   . CYS   A 297 ? 1.4059 1.2569 1.0686 0.0536  -0.1752 0.0280  366  CYS   A C   
2129  O  O   . CYS   A 297 ? 1.3935 1.2449 1.0590 0.0491  -0.1637 0.0302  366  CYS   A O   
2130  C  CB  . CYS   A 297 ? 1.4061 1.2824 1.0989 0.0522  -0.1866 0.0264  366  CYS   A CB  
2131  S  SG  . CYS   A 297 ? 1.5349 1.4328 1.2524 0.0508  -0.2004 0.0224  366  CYS   A SG  
2132  N  N   . ASN   A 298 ? 1.3581 1.1898 0.9959 0.0618  -0.1799 0.0279  367  ASN   A N   
2133  C  CA  . ASN   A 298 ? 1.3036 1.1124 0.9148 0.0662  -0.1706 0.0311  367  ASN   A CA  
2134  C  C   . ASN   A 298 ? 1.2785 1.0832 0.8853 0.0636  -0.1643 0.0311  367  ASN   A C   
2135  O  O   . ASN   A 298 ? 1.2500 1.0452 0.8480 0.0627  -0.1513 0.0347  367  ASN   A O   
2136  C  CB  . ASN   A 298 ? 1.3337 1.1396 0.9451 0.0647  -0.1583 0.0358  367  ASN   A CB  
2137  C  CG  . ASN   A 298 ? 1.3769 1.1834 0.9886 0.0683  -0.1640 0.0362  367  ASN   A CG  
2138  O  OD1 . ASN   A 298 ? 1.3586 1.1505 0.9505 0.0761  -0.1715 0.0353  367  ASN   A OD1 
2139  N  ND2 . ASN   A 298 ? 1.4073 1.2308 1.0415 0.0629  -0.1611 0.0372  367  ASN   A ND2 
2140  N  N   . LEU   A 299 ? 1.3191 1.1310 0.9324 0.0624  -0.1733 0.0270  368  LEU   A N   
2141  C  CA  . LEU   A 299 ? 1.3250 1.1327 0.9334 0.0604  -0.1685 0.0265  368  LEU   A CA  
2142  C  C   . LEU   A 299 ? 1.4013 1.1940 0.9887 0.0671  -0.1789 0.0232  368  LEU   A C   
2143  O  O   . LEU   A 299 ? 1.4780 1.2746 1.0683 0.0698  -0.1929 0.0195  368  LEU   A O   
2144  C  CB  . LEU   A 299 ? 1.2617 1.0921 0.8982 0.0518  -0.1684 0.0247  368  LEU   A CB  
2145  C  CG  . LEU   A 299 ? 1.2147 1.0573 0.8691 0.0450  -0.1559 0.0281  368  LEU   A CG  
2146  C  CD1 . LEU   A 299 ? 1.1839 1.0472 0.8635 0.0376  -0.1576 0.0258  368  LEU   A CD1 
2147  C  CD2 . LEU   A 299 ? 1.2550 1.0827 0.8941 0.0457  -0.1415 0.0321  368  LEU   A CD2 
2148  N  N   . ASN   A 300 ? 1.4637 1.2389 1.0301 0.0701  -0.1722 0.0245  369  ASN   A N   
2149  C  CA  . ASN   A 300 ? 1.4869 1.2461 1.0315 0.0766  -0.1812 0.0214  369  ASN   A CA  
2150  C  C   . ASN   A 300 ? 1.5155 1.2822 1.0691 0.0719  -0.1814 0.0190  369  ASN   A C   
2151  O  O   . ASN   A 300 ? 1.5047 1.2776 1.0678 0.0663  -0.1694 0.0214  369  ASN   A O   
2152  C  CB  . ASN   A 300 ? 1.5318 1.2633 1.0429 0.0845  -0.1738 0.0245  369  ASN   A CB  
2153  C  CG  . ASN   A 300 ? 1.6526 1.3694 1.1441 0.0931  -0.1831 0.0238  369  ASN   A CG  
2154  O  OD1 . ASN   A 300 ? 1.8100 1.5276 1.3003 0.0966  -0.1985 0.0192  369  ASN   A OD1 
2155  N  ND2 . ASN   A 300 ? 1.6136 1.3170 1.0903 0.0968  -0.1739 0.0282  369  ASN   A ND2 
2156  N  N   . LEU   A 301 ? 1.3992 1.1649 0.9499 0.0743  -0.1951 0.0142  370  LEU   A N   
2157  C  CA  . LEU   A 301 ? 1.3682 1.1421 0.9291 0.0697  -0.1968 0.0115  370  LEU   A CA  
2158  C  C   . LEU   A 301 ? 1.4065 1.1579 0.9392 0.0753  -0.1947 0.0112  370  LEU   A C   
2159  O  O   . LEU   A 301 ? 1.5040 1.2354 1.0110 0.0838  -0.2012 0.0101  370  LEU   A O   
2160  C  CB  . LEU   A 301 ? 1.3612 1.1504 0.9405 0.0675  -0.2127 0.0062  370  LEU   A CB  
2161  C  CG  . LEU   A 301 ? 1.3099 1.1263 0.9236 0.0592  -0.2132 0.0060  370  LEU   A CG  
2162  C  CD1 . LEU   A 301 ? 1.3613 1.1835 0.9818 0.0611  -0.2184 0.0064  370  LEU   A CD1 
2163  C  CD2 . LEU   A 301 ? 1.4173 1.2471 1.0482 0.0551  -0.2237 0.0013  370  LEU   A CD2 
2164  N  N   . ILE   A 302 ? 1.3944 1.1487 0.9316 0.0709  -0.1856 0.0121  371  ILE   A N   
2165  C  CA  . ILE   A 302 ? 1.3842 1.1179 0.8959 0.0755  -0.1797 0.0129  371  ILE   A CA  
2166  C  C   . ILE   A 302 ? 1.5145 1.2525 1.0310 0.0736  -0.1885 0.0083  371  ILE   A C   
2167  O  O   . ILE   A 302 ? 1.5047 1.2598 1.0432 0.0659  -0.1848 0.0079  371  ILE   A O   
2168  C  CB  . ILE   A 302 ? 1.3245 1.0568 0.8367 0.0723  -0.1607 0.0181  371  ILE   A CB  
2169  C  CG1 . ILE   A 302 ? 1.4039 1.1245 0.9030 0.0762  -0.1518 0.0228  371  ILE   A CG1 
2170  C  CG2 . ILE   A 302 ? 1.3119 1.0298 0.8066 0.0747  -0.1547 0.0183  371  ILE   A CG2 
2171  C  CD1 . ILE   A 302 ? 1.4817 1.1827 0.9549 0.0857  -0.1607 0.0219  371  ILE   A CD1 
2172  N  N   . GLY   A 303 ? 1.4989 1.2211 0.9948 0.0806  -0.2003 0.0047  372  GLY   A N   
2173  C  CA  . GLY   A 303 ? 1.4433 1.1649 0.9385 0.0800  -0.2083 0.0004  372  GLY   A CA  
2174  C  C   . GLY   A 303 ? 1.4922 1.2297 1.0077 0.0770  -0.2249 -0.0049 372  GLY   A C   
2175  O  O   . GLY   A 303 ? 1.4756 1.2211 1.0009 0.0774  -0.2324 -0.0057 372  GLY   A O   
2176  N  N   . ARG   A 304 ? 1.5513 1.2928 1.0728 0.0742  -0.2304 -0.0084 373  ARG   A N   
2177  C  CA  . ARG   A 304 ? 1.5517 1.3089 1.0943 0.0705  -0.2452 -0.0134 373  ARG   A CA  
2178  C  C   . ARG   A 304 ? 1.4967 1.2791 1.0717 0.0601  -0.2395 -0.0128 373  ARG   A C   
2179  O  O   . ARG   A 304 ? 1.5075 1.2906 1.0833 0.0567  -0.2274 -0.0103 373  ARG   A O   
2180  C  CB  . ARG   A 304 ? 1.5599 1.3034 1.0866 0.0749  -0.2574 -0.0184 373  ARG   A CB  
2181  C  CG  . ARG   A 304 ? 1.6243 1.3428 1.1192 0.0859  -0.2661 -0.0200 373  ARG   A CG  
2182  C  CD  . ARG   A 304 ? 1.7498 1.4443 1.2146 0.0920  -0.2652 -0.0211 373  ARG   A CD  
2183  N  NE  . ARG   A 304 ? 1.8311 1.5337 1.3080 0.0866  -0.2679 -0.0241 373  ARG   A NE  
2184  C  CZ  . ARG   A 304 ? 1.9245 1.6397 1.4201 0.0829  -0.2821 -0.0293 373  ARG   A CZ  
2185  N  NH1 . ARG   A 304 ? 1.9663 1.6874 1.4706 0.0844  -0.2956 -0.0322 373  ARG   A NH1 
2186  N  NH2 . ARG   A 304 ? 1.9479 1.6707 1.4551 0.0774  -0.2824 -0.0314 373  ARG   A NH2 
2187  N  N   . PRO   A 305 ? 1.4289 1.2317 1.0306 0.0550  -0.2475 -0.0148 374  PRO   A N   
2188  C  CA  . PRO   A 305 ? 1.4122 1.2381 1.0438 0.0455  -0.2419 -0.0141 374  PRO   A CA  
2189  C  C   . PRO   A 305 ? 1.4559 1.2805 1.0871 0.0426  -0.2406 -0.0160 374  PRO   A C   
2190  O  O   . PRO   A 305 ? 1.4661 1.2767 1.0810 0.0469  -0.2493 -0.0194 374  PRO   A O   
2191  C  CB  . PRO   A 305 ? 1.3829 1.2263 1.0383 0.0425  -0.2544 -0.0172 374  PRO   A CB  
2192  C  CG  . PRO   A 305 ? 1.4292 1.2612 1.0695 0.0500  -0.2628 -0.0180 374  PRO   A CG  
2193  C  CD  . PRO   A 305 ? 1.4779 1.2833 1.0840 0.0581  -0.2628 -0.0183 374  PRO   A CD  
2194  N  N   . SER   A 306 ? 1.4114 1.2500 1.0603 0.0355  -0.2300 -0.0137 375  SER   A N   
2195  C  CA  . SER   A 306 ? 1.4045 1.2452 1.0573 0.0317  -0.2283 -0.0153 375  SER   A CA  
2196  C  C   . SER   A 306 ? 1.4574 1.3230 1.1428 0.0227  -0.2269 -0.0155 375  SER   A C   
2197  O  O   . SER   A 306 ? 1.4202 1.3007 1.1240 0.0196  -0.2264 -0.0141 375  SER   A O   
2198  C  CB  . SER   A 306 ? 1.4305 1.2582 1.0656 0.0335  -0.2142 -0.0119 375  SER   A CB  
2199  O  OG  . SER   A 306 ? 1.4348 1.2662 1.0757 0.0295  -0.2117 -0.0133 375  SER   A OG  
2200  N  N   . THR   A 307 ? 1.4666 1.3361 1.1585 0.0186  -0.2260 -0.0171 376  THR   A N   
2201  C  CA  . THR   A 307 ? 1.3926 1.2840 1.1133 0.0103  -0.2233 -0.0170 376  THR   A CA  
2202  C  C   . THR   A 307 ? 1.4127 1.3064 1.1356 0.0066  -0.2106 -0.0147 376  THR   A C   
2203  O  O   . THR   A 307 ? 1.4311 1.3424 1.1768 0.0001  -0.2063 -0.0138 376  THR   A O   
2204  C  CB  . THR   A 307 ? 1.3507 1.2497 1.0848 0.0076  -0.2366 -0.0217 376  THR   A CB  
2205  O  OG1 . THR   A 307 ? 1.4225 1.3088 1.1421 0.0092  -0.2393 -0.0243 376  THR   A OG1 
2206  C  CG2 . THR   A 307 ? 1.3118 1.2082 1.0439 0.0116  -0.2499 -0.0243 376  THR   A CG2 
2207  N  N   . GLU   A 308 ? 1.4689 1.3452 1.1689 0.0108  -0.2043 -0.0137 377  GLU   A N   
2208  C  CA  . GLU   A 308 ? 1.4844 1.3622 1.1861 0.0078  -0.1923 -0.0116 377  GLU   A CA  
2209  C  C   . GLU   A 308 ? 1.4525 1.3451 1.1718 0.0031  -0.1808 -0.0077 377  GLU   A C   
2210  O  O   . GLU   A 308 ? 1.4824 1.3716 1.1961 0.0055  -0.1751 -0.0046 377  GLU   A O   
2211  C  CB  . GLU   A 308 ? 1.5326 1.3885 1.2056 0.0142  -0.1858 -0.0102 377  GLU   A CB  
2212  C  CG  . GLU   A 308 ? 1.6783 1.5152 1.3277 0.0213  -0.1967 -0.0132 377  GLU   A CG  
2213  C  CD  . GLU   A 308 ? 1.7827 1.5967 1.4022 0.0281  -0.1892 -0.0114 377  GLU   A CD  
2214  O  OE1 . GLU   A 308 ? 1.7431 1.5476 1.3493 0.0325  -0.1832 -0.0082 377  GLU   A OE1 
2215  O  OE2 . GLU   A 308 ? 1.7191 1.5245 1.3287 0.0291  -0.1889 -0.0130 377  GLU   A OE2 
2216  N  N   . HIS   A 309 ? 1.4431 1.3513 1.1830 -0.0034 -0.1775 -0.0078 378  HIS   A N   
2217  C  CA  . HIS   A 309 ? 1.4668 1.3889 1.2236 -0.0080 -0.1668 -0.0045 378  HIS   A CA  
2218  C  C   . HIS   A 309 ? 1.4623 1.3966 1.2339 -0.0097 -0.1696 -0.0035 378  HIS   A C   
2219  O  O   . HIS   A 309 ? 1.4878 1.4332 1.2732 -0.0132 -0.1614 -0.0008 378  HIS   A O   
2220  C  CB  . HIS   A 309 ? 1.5021 1.4139 1.2452 -0.0054 -0.1535 -0.0007 378  HIS   A CB  
2221  C  CG  . HIS   A 309 ? 1.5692 1.4920 1.3268 -0.0104 -0.1427 0.0012  378  HIS   A CG  
2222  N  ND1 . HIS   A 309 ? 1.5739 1.4892 1.3226 -0.0090 -0.1303 0.0042  378  HIS   A ND1 
2223  C  CD2 . HIS   A 309 ? 1.5727 1.5130 1.3530 -0.0166 -0.1424 0.0005  378  HIS   A CD2 
2224  C  CE1 . HIS   A 309 ? 1.5671 1.4952 1.3328 -0.0141 -0.1235 0.0050  378  HIS   A CE1 
2225  N  NE2 . HIS   A 309 ? 1.5927 1.5357 1.3771 -0.0187 -0.1306 0.0028  378  HIS   A NE2 
2226  N  N   . SER   A 310 ? 1.3529 1.2853 1.1223 -0.0071 -0.1811 -0.0057 379  SER   A N   
2227  C  CA  . SER   A 310 ? 1.3426 1.2865 1.1261 -0.0083 -0.1843 -0.0050 379  SER   A CA  
2228  C  C   . SER   A 310 ? 1.3768 1.3405 1.1855 -0.0151 -0.1786 -0.0036 379  SER   A C   
2229  O  O   . SER   A 310 ? 1.3824 1.3580 1.2077 -0.0194 -0.1832 -0.0056 379  SER   A O   
2230  C  CB  . SER   A 310 ? 1.3877 1.3330 1.1743 -0.0070 -0.1989 -0.0087 379  SER   A CB  
2231  O  OG  . SER   A 310 ? 1.3576 1.3093 1.1514 -0.0061 -0.2016 -0.0076 379  SER   A OG  
2232  N  N   . TRP   A 311 ? 1.3464 1.3131 1.1580 -0.0158 -0.1686 0.0000  380  TRP   A N   
2233  C  CA  . TRP   A 311 ? 1.2702 1.2541 1.1038 -0.0216 -0.1626 0.0015  380  TRP   A CA  
2234  C  C   . TRP   A 311 ? 1.2870 1.2864 1.1407 -0.0247 -0.1707 -0.0002 380  TRP   A C   
2235  O  O   . TRP   A 311 ? 1.3235 1.3369 1.1956 -0.0298 -0.1683 -0.0002 380  TRP   A O   
2236  C  CB  . TRP   A 311 ? 1.2696 1.2530 1.1020 -0.0210 -0.1529 0.0052  380  TRP   A CB  
2237  C  CG  . TRP   A 311 ? 1.2450 1.2164 1.0627 -0.0191 -0.1428 0.0073  380  TRP   A CG  
2238  C  CD1 . TRP   A 311 ? 1.3139 1.2827 1.1290 -0.0204 -0.1381 0.0068  380  TRP   A CD1 
2239  C  CD2 . TRP   A 311 ? 1.3089 1.2693 1.1129 -0.0155 -0.1356 0.0104  380  TRP   A CD2 
2240  N  NE1 . TRP   A 311 ? 1.3021 1.2593 1.1033 -0.0179 -0.1282 0.0095  380  TRP   A NE1 
2241  C  CE2 . TRP   A 311 ? 1.2952 1.2469 1.0895 -0.0149 -0.1264 0.0117  380  TRP   A CE2 
2242  C  CE3 . TRP   A 311 ? 1.2977 1.2545 1.0969 -0.0126 -0.1359 0.0122  380  TRP   A CE3 
2243  C  CZ2 . TRP   A 311 ? 1.3291 1.2689 1.1097 -0.0117 -0.1171 0.0149  380  TRP   A CZ2 
2244  C  CZ3 . TRP   A 311 ? 1.1967 1.1412 0.9817 -0.0095 -0.1268 0.0153  380  TRP   A CZ3 
2245  C  CH2 . TRP   A 311 ? 1.2554 1.1916 1.0316 -0.0092 -0.1174 0.0167  380  TRP   A CH2 
2246  N  N   . PHE   A 312 ? 1.2602 1.2571 1.1107 -0.0216 -0.1799 -0.0016 381  PHE   A N   
2247  C  CA  . PHE   A 312 ? 1.3183 1.3293 1.1877 -0.0240 -0.1878 -0.0031 381  PHE   A CA  
2248  C  C   . PHE   A 312 ? 1.3206 1.3289 1.1890 -0.0234 -0.1992 -0.0070 381  PHE   A C   
2249  O  O   . PHE   A 312 ? 1.3160 1.3162 1.1743 -0.0190 -0.2081 -0.0088 381  PHE   A O   
2250  C  CB  . PHE   A 312 ? 1.3212 1.3329 1.1902 -0.0210 -0.1899 -0.0017 381  PHE   A CB  
2251  C  CG  . PHE   A 312 ? 1.3127 1.3231 1.1786 -0.0207 -0.1791 0.0020  381  PHE   A CG  
2252  C  CD1 . PHE   A 312 ? 1.3161 1.3409 1.2001 -0.0249 -0.1734 0.0039  381  PHE   A CD1 
2253  C  CD2 . PHE   A 312 ? 1.3102 1.3045 1.1548 -0.0163 -0.1743 0.0037  381  PHE   A CD2 
2254  C  CE1 . PHE   A 312 ? 1.3150 1.3385 1.1968 -0.0248 -0.1638 0.0071  381  PHE   A CE1 
2255  C  CE2 . PHE   A 312 ? 1.3213 1.3144 1.1641 -0.0164 -0.1640 0.0072  381  PHE   A CE2 
2256  C  CZ  . PHE   A 312 ? 1.2846 1.2926 1.1465 -0.0208 -0.1590 0.0088  381  PHE   A CZ  
2257  N  N   . PRO   A 313 ? 1.3418 1.3563 1.2200 -0.0277 -0.1996 -0.0086 382  PRO   A N   
2258  C  CA  . PRO   A 313 ? 1.3353 1.3458 1.2115 -0.0273 -0.2101 -0.0125 382  PRO   A CA  
2259  C  C   . PRO   A 313 ? 1.3705 1.3876 1.2573 -0.0266 -0.2212 -0.0146 382  PRO   A C   
2260  O  O   . PRO   A 313 ? 1.3887 1.4207 1.2949 -0.0296 -0.2207 -0.0136 382  PRO   A O   
2261  C  CB  . PRO   A 313 ? 1.2921 1.3120 1.1822 -0.0330 -0.2068 -0.0132 382  PRO   A CB  
2262  C  CG  . PRO   A 313 ? 1.3388 1.3585 1.2259 -0.0341 -0.1938 -0.0099 382  PRO   A CG  
2263  C  CD  . PRO   A 313 ? 1.3902 1.4134 1.2793 -0.0325 -0.1901 -0.0071 382  PRO   A CD  
2264  N  N   . GLY   A 314 ? 1.3151 1.3203 1.1882 -0.0220 -0.2312 -0.0173 383  GLY   A N   
2265  C  CA  . GLY   A 314 ? 1.3395 1.3488 1.2202 -0.0203 -0.2427 -0.0196 383  GLY   A CA  
2266  C  C   . GLY   A 314 ? 1.4381 1.4350 1.3006 -0.0135 -0.2462 -0.0192 383  GLY   A C   
2267  O  O   . GLY   A 314 ? 1.4350 1.4285 1.2956 -0.0102 -0.2581 -0.0222 383  GLY   A O   
2268  N  N   . TYR   A 315 ? 1.4224 1.4124 1.2720 -0.0112 -0.2364 -0.0157 384  TYR   A N   
2269  C  CA  . TYR   A 315 ? 1.3742 1.3502 1.2038 -0.0044 -0.2383 -0.0149 384  TYR   A CA  
2270  C  C   . TYR   A 315 ? 1.3605 1.3167 1.1634 -0.0003 -0.2338 -0.0144 384  TYR   A C   
2271  O  O   . TYR   A 315 ? 1.3126 1.2680 1.1142 -0.0032 -0.2253 -0.0132 384  TYR   A O   
2272  C  CB  . TYR   A 315 ? 1.3653 1.3474 1.1998 -0.0044 -0.2302 -0.0110 384  TYR   A CB  
2273  C  CG  . TYR   A 315 ? 1.3335 1.3354 1.1942 -0.0084 -0.2323 -0.0108 384  TYR   A CG  
2274  C  CD1 . TYR   A 315 ? 1.3494 1.3668 1.2303 -0.0149 -0.2261 -0.0097 384  TYR   A CD1 
2275  C  CD2 . TYR   A 315 ? 1.3539 1.3585 1.2183 -0.0053 -0.2401 -0.0115 384  TYR   A CD2 
2276  C  CE1 . TYR   A 315 ? 1.3397 1.3742 1.2434 -0.0182 -0.2273 -0.0093 384  TYR   A CE1 
2277  C  CE2 . TYR   A 315 ? 1.3748 1.3972 1.2628 -0.0086 -0.2414 -0.0111 384  TYR   A CE2 
2278  C  CZ  . TYR   A 315 ? 1.3445 1.3815 1.2518 -0.0150 -0.2349 -0.0100 384  TYR   A CZ  
2279  O  OH  . TYR   A 315 ? 1.3659 1.4197 1.2956 -0.0179 -0.2357 -0.0094 384  TYR   A OH  
2280  N  N   . ALA   A 316 ? 1.3608 1.3005 1.1422 0.0067  -0.2395 -0.0153 385  ALA   A N   
2281  C  CA  . ALA   A 316 ? 1.3400 1.2590 1.0936 0.0117  -0.2346 -0.0143 385  ALA   A CA  
2282  C  C   . ALA   A 316 ? 1.3440 1.2563 1.0863 0.0149  -0.2251 -0.0100 385  ALA   A C   
2283  O  O   . ALA   A 316 ? 1.3560 1.2762 1.1075 0.0150  -0.2260 -0.0087 385  ALA   A O   
2284  C  CB  . ALA   A 316 ? 1.3232 1.2260 1.0578 0.0180  -0.2472 -0.0182 385  ALA   A CB  
2285  N  N   . TRP   A 317 ? 1.3509 1.2485 1.0734 0.0176  -0.2156 -0.0077 386  TRP   A N   
2286  C  CA  . TRP   A 317 ? 1.3399 1.2309 1.0523 0.0199  -0.2046 -0.0032 386  TRP   A CA  
2287  C  C   . TRP   A 317 ? 1.3228 1.1900 1.0045 0.0285  -0.2060 -0.0028 386  TRP   A C   
2288  O  O   . TRP   A 317 ? 1.3384 1.1913 1.0024 0.0323  -0.2103 -0.0051 386  TRP   A O   
2289  C  CB  . TRP   A 317 ? 1.2918 1.1862 1.0085 0.0157  -0.1900 0.0000  386  TRP   A CB  
2290  C  CG  . TRP   A 317 ? 1.3135 1.1976 1.0177 0.0164  -0.1874 -0.0011 386  TRP   A CG  
2291  C  CD1 . TRP   A 317 ? 1.3497 1.2422 1.0656 0.0119  -0.1899 -0.0035 386  TRP   A CD1 
2292  C  CD2 . TRP   A 317 ? 1.3494 1.2124 1.0267 0.0220  -0.1813 0.0005  386  TRP   A CD2 
2293  N  NE1 . TRP   A 317 ? 1.3813 1.2594 1.0792 0.0144  -0.1861 -0.0038 386  TRP   A NE1 
2294  C  CE2 . TRP   A 317 ? 1.3882 1.2481 1.0623 0.0207  -0.1806 -0.0013 386  TRP   A CE2 
2295  C  CE3 . TRP   A 317 ? 1.3812 1.2272 1.0365 0.0282  -0.1761 0.0033  386  TRP   A CE3 
2296  C  CZ2 . TRP   A 317 ? 1.4488 1.2892 1.0983 0.0256  -0.1749 -0.0004 386  TRP   A CZ2 
2297  C  CZ3 . TRP   A 317 ? 1.3771 1.2036 1.0081 0.0330  -0.1700 0.0044  386  TRP   A CZ3 
2298  C  CH2 . TRP   A 317 ? 1.4443 1.2683 1.0726 0.0317  -0.1694 0.0025  386  TRP   A CH2 
2299  N  N   . THR   A 318 ? 1.3208 1.1834 0.9957 0.0317  -0.2022 0.0001  387  THR   A N   
2300  C  CA  . THR   A 318 ? 1.3128 1.1527 0.9584 0.0399  -0.2017 0.0013  387  THR   A CA  
2301  C  C   . THR   A 318 ? 1.3270 1.1643 0.9694 0.0396  -0.1872 0.0066  387  THR   A C   
2302  O  O   . THR   A 318 ? 1.2721 1.1232 0.9320 0.0361  -0.1846 0.0083  387  THR   A O   
2303  C  CB  . THR   A 318 ? 1.3248 1.1609 0.9653 0.0451  -0.2154 -0.0012 387  THR   A CB  
2304  O  OG1 . THR   A 318 ? 1.3623 1.2106 1.0192 0.0423  -0.2284 -0.0059 387  THR   A OG1 
2305  C  CG2 . THR   A 318 ? 1.3584 1.1685 0.9657 0.0544  -0.2186 -0.0016 387  THR   A CG2 
2306  N  N   . VAL   A 319 ? 1.3911 1.2107 1.0118 0.0433  -0.1775 0.0091  388  VAL   A N   
2307  C  CA  . VAL   A 319 ? 1.3355 1.1528 0.9546 0.0424  -0.1626 0.0142  388  VAL   A CA  
2308  C  C   . VAL   A 319 ? 1.3006 1.1129 0.9133 0.0463  -0.1640 0.0161  388  VAL   A C   
2309  O  O   . VAL   A 319 ? 1.3446 1.1436 0.9394 0.0532  -0.1731 0.0145  388  VAL   A O   
2310  C  CB  . VAL   A 319 ? 1.2996 1.0976 0.8956 0.0461  -0.1521 0.0165  388  VAL   A CB  
2311  C  CG1 . VAL   A 319 ? 1.2878 1.0869 0.8878 0.0435  -0.1359 0.0216  388  VAL   A CG1 
2312  C  CG2 . VAL   A 319 ? 1.3480 1.1487 0.9472 0.0435  -0.1535 0.0139  388  VAL   A CG2 
2313  N  N   . ALA   A 320 ? 1.3010 1.1233 0.9277 0.0423  -0.1550 0.0195  389  ALA   A N   
2314  C  CA  . ALA   A 320 ? 1.2956 1.1150 0.9188 0.0454  -0.1559 0.0213  389  ALA   A CA  
2315  C  C   . ALA   A 320 ? 1.2842 1.0948 0.8995 0.0457  -0.1406 0.0265  389  ALA   A C   
2316  O  O   . ALA   A 320 ? 1.2446 1.0618 0.8705 0.0405  -0.1296 0.0286  389  ALA   A O   
2317  C  CB  . ALA   A 320 ? 1.2223 1.0640 0.8728 0.0403  -0.1623 0.0199  389  ALA   A CB  
2318  N  N   . GLN   A 321 ? 1.3311 1.1266 0.9281 0.0519  -0.1402 0.0286  390  GLN   A N   
2319  C  CA  . GLN   A 321 ? 1.3252 1.1099 0.9125 0.0528  -0.1258 0.0336  390  GLN   A CA  
2320  C  C   . GLN   A 321 ? 1.3124 1.0909 0.8925 0.0569  -0.1276 0.0354  390  GLN   A C   
2321  O  O   . GLN   A 321 ? 1.2999 1.0758 0.8737 0.0614  -0.1402 0.0328  390  GLN   A O   
2322  C  CB  . GLN   A 321 ? 1.3797 1.1418 0.9400 0.0581  -0.1184 0.0353  390  GLN   A CB  
2323  C  CG  . GLN   A 321 ? 1.4185 1.1619 0.9523 0.0669  -0.1294 0.0327  390  GLN   A CG  
2324  C  CD  . GLN   A 321 ? 1.4841 1.2028 0.9886 0.0732  -0.1210 0.0350  390  GLN   A CD  
2325  O  OE1 . GLN   A 321 ? 1.4507 1.1689 0.9556 0.0708  -0.1135 0.0355  390  GLN   A OE1 
2326  N  NE2 . GLN   A 321 ? 1.4878 1.1852 0.9657 0.0815  -0.1220 0.0366  390  GLN   A NE2 
2327  N  N   . CYS   A 322 ? 1.3107 1.0867 0.8920 0.0552  -0.1149 0.0398  391  CYS   A N   
2328  C  CA  . CYS   A 322 ? 1.3699 1.1391 0.9443 0.0586  -0.1144 0.0422  391  CYS   A CA  
2329  C  C   . CYS   A 322 ? 1.3968 1.1421 0.9396 0.0685  -0.1197 0.0421  391  CYS   A C   
2330  O  O   . CYS   A 322 ? 1.4632 1.1901 0.9839 0.0730  -0.1146 0.0433  391  CYS   A O   
2331  C  CB  . CYS   A 322 ? 1.3696 1.1367 0.9475 0.0554  -0.0983 0.0472  391  CYS   A CB  
2332  S  SG  . CYS   A 322 ? 1.3039 1.0639 0.8760 0.0585  -0.0963 0.0503  391  CYS   A SG  
2333  N  N   . LYS   A 323 ? 1.3393 1.0842 0.8795 0.0724  -0.1299 0.0408  392  LYS   A N   
2334  C  CA  . LYS   A 323 ? 1.3356 1.0579 0.8459 0.0823  -0.1363 0.0404  392  LYS   A CA  
2335  C  C   . LYS   A 323 ? 1.4221 1.1237 0.9109 0.0868  -0.1241 0.0455  392  LYS   A C   
2336  O  O   . LYS   A 323 ? 1.4704 1.1503 0.9312 0.0957  -0.1276 0.0458  392  LYS   A O   
2337  C  CB  . LYS   A 323 ? 1.3549 1.0839 0.8701 0.0852  -0.1518 0.0370  392  LYS   A CB  
2338  C  CG  . LYS   A 323 ? 1.3140 1.0510 0.8411 0.0835  -0.1493 0.0394  392  LYS   A CG  
2339  C  CD  . LYS   A 323 ? 1.3158 1.0580 0.8458 0.0874  -0.1651 0.0358  392  LYS   A CD  
2340  C  CE  . LYS   A 323 ? 1.3120 1.0560 0.8459 0.0882  -0.1633 0.0383  392  LYS   A CE  
2341  N  NZ  . LYS   A 323 ? 1.2896 1.0373 0.8246 0.0929  -0.1793 0.0346  392  LYS   A NZ  
2342  N  N   . ILE   A 324 ? 1.3801 1.0875 0.8812 0.0811  -0.1100 0.0495  393  ILE   A N   
2343  C  CA  . ILE   A 324 ? 1.4584 1.1483 0.9431 0.0842  -0.0976 0.0547  393  ILE   A CA  
2344  C  C   . ILE   A 324 ? 1.4804 1.1600 0.9571 0.0829  -0.0821 0.0582  393  ILE   A C   
2345  O  O   . ILE   A 324 ? 1.4845 1.1409 0.9355 0.0890  -0.0741 0.0616  393  ILE   A O   
2346  C  CB  . ILE   A 324 ? 1.4021 1.1048 0.9064 0.0793  -0.0935 0.0569  393  ILE   A CB  
2347  C  CG1 . ILE   A 324 ? 1.3481 1.0602 0.8596 0.0812  -0.1082 0.0538  393  ILE   A CG1 
2348  C  CG2 . ILE   A 324 ? 1.3318 1.0158 0.8194 0.0823  -0.0805 0.0623  393  ILE   A CG2 
2349  C  CD1 . ILE   A 324 ? 1.3355 1.0273 0.8217 0.0901  -0.1115 0.0551  393  ILE   A CD1 
2350  N  N   . CYS   A 325 ? 1.4236 1.1200 0.9222 0.0751  -0.0772 0.0575  394  CYS   A N   
2351  C  CA  . CYS   A 325 ? 1.4039 1.0927 0.8979 0.0734  -0.0624 0.0607  394  CYS   A CA  
2352  C  C   . CYS   A 325 ? 1.4171 1.1099 0.9125 0.0723  -0.0657 0.0576  394  CYS   A C   
2353  O  O   . CYS   A 325 ? 1.4845 1.1720 0.9769 0.0709  -0.0541 0.0598  394  CYS   A O   
2354  C  CB  . CYS   A 325 ? 1.4305 1.1333 0.9489 0.0650  -0.0500 0.0638  394  CYS   A CB  
2355  S  SG  . CYS   A 325 ? 1.4133 1.1490 0.9709 0.0543  -0.0542 0.0604  394  CYS   A SG  
2356  N  N   . ALA   A 326 ? 1.5043 1.2054 1.0035 0.0731  -0.0812 0.0525  395  ALA   A N   
2357  C  CA  . ALA   A 326 ? 1.5196 1.2241 1.0194 0.0723  -0.0861 0.0491  395  ALA   A CA  
2358  C  C   . ALA   A 326 ? 1.4994 1.2192 1.0213 0.0640  -0.0759 0.0500  395  ALA   A C   
2359  O  O   . ALA   A 326 ? 1.5202 1.2348 1.0356 0.0644  -0.0719 0.0497  395  ALA   A O   
2360  C  CB  . ALA   A 326 ? 1.4870 1.1653 0.9531 0.0811  -0.0855 0.0494  395  ALA   A CB  
2361  N  N   . SER   A 327 ? 1.4076 1.1456 0.9551 0.0569  -0.0717 0.0513  396  SER   A N   
2362  C  CA  . SER   A 327 ? 1.4073 1.1625 0.9786 0.0488  -0.0646 0.0513  396  SER   A CA  
2363  C  C   . SER   A 327 ? 1.3771 1.1518 0.9673 0.0447  -0.0773 0.0463  396  SER   A C   
2364  O  O   . SER   A 327 ? 1.3453 1.1257 0.9388 0.0460  -0.0898 0.0436  396  SER   A O   
2365  C  CB  . SER   A 327 ? 1.3747 1.1399 0.9647 0.0431  -0.0545 0.0546  396  SER   A CB  
2366  O  OG  . SER   A 327 ? 1.4268 1.1779 1.0061 0.0442  -0.0391 0.0591  396  SER   A OG  
2367  N  N   . HIS   A 328 ? 1.2799 1.0642 0.8822 0.0400  -0.0741 0.0451  397  HIS   A N   
2368  C  CA  . HIS   A 328 ? 1.1873 0.9885 0.8061 0.0363  -0.0856 0.0405  397  HIS   A CA  
2369  C  C   . HIS   A 328 ? 1.1700 0.9931 0.8164 0.0300  -0.0886 0.0399  397  HIS   A C   
2370  O  O   . HIS   A 328 ? 1.1915 1.0226 0.8522 0.0252  -0.0788 0.0425  397  HIS   A O   
2371  C  CB  . HIS   A 328 ? 1.3255 1.1307 0.9496 0.0331  -0.0809 0.0396  397  HIS   A CB  
2372  C  CG  . HIS   A 328 ? 1.1905 1.0126 0.8317 0.0290  -0.0918 0.0351  397  HIS   A CG  
2373  N  ND1 . HIS   A 328 ? 1.1363 0.9783 0.8033 0.0215  -0.0890 0.0344  397  HIS   A ND1 
2374  C  CD2 . HIS   A 328 ? 1.1667 0.9884 0.8030 0.0315  -0.1055 0.0310  397  HIS   A CD2 
2375  C  CE1 . HIS   A 328 ? 1.1254 0.9783 0.8023 0.0195  -0.1000 0.0304  397  HIS   A CE1 
2376  N  NE2 . HIS   A 328 ? 1.1431 0.9844 0.8025 0.0253  -0.1102 0.0282  397  HIS   A NE2 
2377  N  N   . ILE   A 329 ? 1.1522 0.9847 0.8059 0.0301  -0.1021 0.0365  398  ILE   A N   
2378  C  CA  . ILE   A 329 ? 1.1522 1.0055 0.8316 0.0246  -0.1057 0.0356  398  ILE   A CA  
2379  C  C   . ILE   A 329 ? 1.1836 1.0546 0.8824 0.0195  -0.1125 0.0319  398  ILE   A C   
2380  O  O   . ILE   A 329 ? 1.1768 1.0654 0.8987 0.0133  -0.1102 0.0319  398  ILE   A O   
2381  C  CB  . ILE   A 329 ? 1.1659 1.0179 0.8417 0.0283  -0.1147 0.0351  398  ILE   A CB  
2382  C  CG1 . ILE   A 329 ? 1.2254 1.0594 0.8820 0.0333  -0.1072 0.0390  398  ILE   A CG1 
2383  C  CG2 . ILE   A 329 ? 1.1054 0.9791 0.8079 0.0227  -0.1182 0.0341  398  ILE   A CG2 
2384  C  CD1 . ILE   A 329 ? 1.1929 1.0311 0.8606 0.0288  -0.0939 0.0430  398  ILE   A CD1 
2385  N  N   . GLY   A 330 ? 1.1764 1.0427 0.8662 0.0220  -0.1207 0.0288  399  GLY   A N   
2386  C  CA  . GLY   A 330 ? 1.1383 1.0199 0.8452 0.0174  -0.1272 0.0253  399  GLY   A CA  
2387  C  C   . GLY   A 330 ? 1.1760 1.0513 0.8720 0.0214  -0.1399 0.0215  399  GLY   A C   
2388  O  O   . GLY   A 330 ? 1.2040 1.0605 0.8761 0.0272  -0.1402 0.0214  399  GLY   A O   
2389  N  N   . TRP   A 331 ? 1.1359 1.0260 0.8487 0.0186  -0.1505 0.0181  400  TRP   A N   
2390  C  CA  . TRP   A 331 ? 1.2125 1.0981 0.9178 0.0217  -0.1632 0.0141  400  TRP   A CA  
2391  C  C   . TRP   A 331 ? 1.2090 1.1054 0.9268 0.0218  -0.1750 0.0118  400  TRP   A C   
2392  O  O   . TRP   A 331 ? 1.1901 1.1009 0.9263 0.0181  -0.1732 0.0130  400  TRP   A O   
2393  C  CB  . TRP   A 331 ? 1.2441 1.1366 0.9583 0.0174  -0.1638 0.0117  400  TRP   A CB  
2394  C  CG  . TRP   A 331 ? 1.2093 1.0938 0.9147 0.0167  -0.1514 0.0141  400  TRP   A CG  
2395  C  CD1 . TRP   A 331 ? 1.2457 1.1123 0.9286 0.0212  -0.1496 0.0138  400  TRP   A CD1 
2396  C  CD2 . TRP   A 331 ? 1.0859 0.9795 0.8046 0.0116  -0.1390 0.0170  400  TRP   A CD2 
2397  N  NE1 . TRP   A 331 ? 1.2102 1.0750 0.8927 0.0190  -0.1365 0.0166  400  TRP   A NE1 
2398  C  CE2 . TRP   A 331 ? 1.1806 1.0620 0.8853 0.0130  -0.1300 0.0185  400  TRP   A CE2 
2399  C  CE3 . TRP   A 331 ? 1.1173 1.0280 0.8584 0.0061  -0.1348 0.0185  400  TRP   A CE3 
2400  C  CZ2 . TRP   A 331 ? 1.2481 1.1348 0.9619 0.0089  -0.1172 0.0212  400  TRP   A CZ2 
2401  C  CZ3 . TRP   A 331 ? 1.1668 1.0821 0.9162 0.0021  -0.1225 0.0210  400  TRP   A CZ3 
2402  C  CH2 . TRP   A 331 ? 1.1475 1.0511 0.8838 0.0035  -0.1140 0.0223  400  TRP   A CH2 
2403  N  N   . LYS   A 332 ? 1.2498 1.1395 0.9583 0.0260  -0.1874 0.0083  401  LYS   A N   
2404  C  CA  . LYS   A 332 ? 1.2609 1.1622 0.9836 0.0257  -0.1997 0.0054  401  LYS   A CA  
2405  C  C   . LYS   A 332 ? 1.2790 1.1897 1.0143 0.0223  -0.2082 0.0014  401  LYS   A C   
2406  O  O   . LYS   A 332 ? 1.2777 1.1765 0.9983 0.0253  -0.2133 -0.0011 401  LYS   A O   
2407  C  CB  . LYS   A 332 ? 1.2678 1.1547 0.9717 0.0336  -0.2086 0.0044  401  LYS   A CB  
2408  C  CG  . LYS   A 332 ? 1.2650 1.1637 0.9838 0.0338  -0.2215 0.0014  401  LYS   A CG  
2409  C  CD  . LYS   A 332 ? 1.2772 1.1598 0.9752 0.0423  -0.2309 0.0001  401  LYS   A CD  
2410  C  CE  . LYS   A 332 ? 1.3640 1.2576 1.0758 0.0431  -0.2386 -0.0007 401  LYS   A CE  
2411  N  NZ  . LYS   A 332 ? 1.5123 1.3888 1.2016 0.0515  -0.2428 -0.0002 401  LYS   A NZ  
2412  N  N   . PHE   A 333 ? 1.2864 1.2177 1.0482 0.0161  -0.2094 0.0007  402  PHE   A N   
2413  C  CA  . PHE   A 333 ? 1.2582 1.1999 1.0347 0.0121  -0.2164 -0.0028 402  PHE   A CA  
2414  C  C   . PHE   A 333 ? 1.3202 1.2677 1.1052 0.0138  -0.2307 -0.0062 402  PHE   A C   
2415  O  O   . PHE   A 333 ? 1.3235 1.2798 1.1192 0.0141  -0.2327 -0.0054 402  PHE   A O   
2416  C  CB  . PHE   A 333 ? 1.2104 1.1705 1.0105 0.0044  -0.2087 -0.0014 402  PHE   A CB  
2417  C  CG  . PHE   A 333 ? 1.2475 1.2026 1.0409 0.0025  -0.1957 0.0013  402  PHE   A CG  
2418  C  CD1 . PHE   A 333 ? 1.1809 1.1341 0.9712 0.0027  -0.1851 0.0053  402  PHE   A CD1 
2419  C  CD2 . PHE   A 333 ? 1.2603 1.2122 1.0504 0.0006  -0.1942 -0.0001 402  PHE   A CD2 
2420  C  CE1 . PHE   A 333 ? 1.1484 1.0975 0.9340 0.0009  -0.1732 0.0077  402  PHE   A CE1 
2421  C  CE2 . PHE   A 333 ? 1.2515 1.1994 1.0363 -0.0010 -0.1823 0.0024  402  PHE   A CE2 
2422  C  CZ  . PHE   A 333 ? 1.2621 1.2087 1.0451 -0.0009 -0.1718 0.0063  402  PHE   A CZ  
2423  N  N   . THR   A 334 ? 1.3626 1.3050 1.1431 0.0152  -0.2406 -0.0101 403  THR   A N   
2424  C  CA  . THR   A 334 ? 1.3209 1.2658 1.1067 0.0176  -0.2554 -0.0140 403  THR   A CA  
2425  C  C   . THR   A 334 ? 1.3715 1.3278 1.1752 0.0123  -0.2613 -0.0174 403  THR   A C   
2426  O  O   . THR   A 334 ? 1.3963 1.3479 1.1946 0.0103  -0.2579 -0.0179 403  THR   A O   
2427  C  CB  . THR   A 334 ? 1.3338 1.2569 1.0916 0.0259  -0.2628 -0.0158 403  THR   A CB  
2428  O  OG1 . THR   A 334 ? 1.4328 1.3488 1.1840 0.0260  -0.2695 -0.0195 403  THR   A OG1 
2429  C  CG2 . THR   A 334 ? 1.2563 1.1627 0.9901 0.0297  -0.2512 -0.0119 403  THR   A CG2 
2430  N  N   . ALA   A 335 ? 1.3824 1.3538 1.2080 0.0100  -0.2698 -0.0194 404  ALA   A N   
2431  C  CA  . ALA   A 335 ? 1.4510 1.4356 1.2973 0.0039  -0.2736 -0.0220 404  ALA   A CA  
2432  C  C   . ALA   A 335 ? 1.4364 1.4097 1.2720 0.0062  -0.2846 -0.0265 404  ALA   A C   
2433  O  O   . ALA   A 335 ? 1.4290 1.3925 1.2533 0.0120  -0.2955 -0.0291 404  ALA   A O   
2434  C  CB  . ALA   A 335 ? 1.4606 1.4645 1.3340 0.0009  -0.2789 -0.0227 404  ALA   A CB  
2435  N  N   . THR   A 336 ? 1.4792 1.4538 1.3184 0.0019  -0.2824 -0.0276 405  THR   A N   
2436  C  CA  . THR   A 336 ? 1.5314 1.4968 1.3634 0.0036  -0.2939 -0.0323 405  THR   A CA  
2437  C  C   . THR   A 336 ? 1.6109 1.5897 1.4659 0.0012  -0.3064 -0.0359 405  THR   A C   
2438  O  O   . THR   A 336 ? 1.6345 1.6053 1.4828 0.0055  -0.3195 -0.0399 405  THR   A O   
2439  C  CB  . THR   A 336 ? 1.4648 1.4271 1.2937 -0.0002 -0.2884 -0.0326 405  THR   A CB  
2440  O  OG1 . THR   A 336 ? 1.5211 1.5023 1.3751 -0.0079 -0.2817 -0.0311 405  THR   A OG1 
2441  C  CG2 . THR   A 336 ? 1.4169 1.3638 1.2212 0.0031  -0.2774 -0.0296 405  THR   A CG2 
2442  N  N   . LYS   A 337 ? 1.6202 1.6192 1.5026 -0.0053 -0.3024 -0.0346 406  LYS   A N   
2443  C  CA  . LYS   A 337 ? 1.6630 1.6752 1.5691 -0.0082 -0.3132 -0.0379 406  LYS   A CA  
2444  C  C   . LYS   A 337 ? 1.7282 1.7457 1.6408 -0.0045 -0.3192 -0.0378 406  LYS   A C   
2445  O  O   . LYS   A 337 ? 1.7105 1.7169 1.6042 0.0015  -0.3181 -0.0364 406  LYS   A O   
2446  C  CB  . LYS   A 337 ? 1.6620 1.6929 1.5945 -0.0164 -0.3065 -0.0365 406  LYS   A CB  
2447  C  CG  . LYS   A 337 ? 1.5501 1.5767 1.4766 -0.0201 -0.2987 -0.0359 406  LYS   A CG  
2448  C  CD  . LYS   A 337 ? 1.6305 1.6366 1.5311 -0.0157 -0.3040 -0.0387 406  LYS   A CD  
2449  C  CE  . LYS   A 337 ? 1.7428 1.7471 1.6493 -0.0162 -0.3183 -0.0440 406  LYS   A CE  
2450  N  NZ  . LYS   A 337 ? 1.7250 1.7081 1.6047 -0.0116 -0.3233 -0.0468 406  LYS   A NZ  
2451  N  N   . LYS   A 338 ? 1.9449 1.9785 1.8836 -0.0077 -0.3258 -0.0395 407  LYS   A N   
2452  C  CA  . LYS   A 338 ? 1.9342 1.9762 1.8832 -0.0051 -0.3294 -0.0389 407  LYS   A CA  
2453  C  C   . LYS   A 338 ? 1.9394 2.0024 1.9160 -0.0111 -0.3218 -0.0361 407  LYS   A C   
2454  O  O   . LYS   A 338 ? 1.9353 2.0061 1.9198 -0.0093 -0.3206 -0.0341 407  LYS   A O   
2455  C  CB  . LYS   A 338 ? 1.8698 1.9110 1.8246 -0.0019 -0.3462 -0.0439 407  LYS   A CB  
2456  N  N   . ASP   A 339 ? 1.9146 1.9865 1.9054 -0.0177 -0.3166 -0.0357 408  ASP   A N   
2457  C  CA  . ASP   A 339 ? 1.9303 2.0198 1.9430 -0.0231 -0.3069 -0.0324 408  ASP   A CA  
2458  C  C   . ASP   A 339 ? 1.9141 2.0018 1.9163 -0.0214 -0.2951 -0.0278 408  ASP   A C   
2459  O  O   . ASP   A 339 ? 1.9113 2.0082 1.9235 -0.0204 -0.2931 -0.0257 408  ASP   A O   
2460  C  CB  . ASP   A 339 ? 1.9321 2.0266 1.9545 -0.0297 -0.3020 -0.0326 408  ASP   A CB  
2461  C  CG  . ASP   A 339 ? 2.0170 2.1229 2.0506 -0.0343 -0.2883 -0.0283 408  ASP   A CG  
2462  O  OD1 . ASP   A 339 ? 2.0445 2.1613 2.0903 -0.0341 -0.2848 -0.0259 408  ASP   A OD1 
2463  O  OD2 . ASP   A 339 ? 2.0470 2.1508 2.0773 -0.0378 -0.2815 -0.0275 408  ASP   A OD2 
2464  N  N   . MET   A 340 ? 1.8040 1.8795 1.7858 -0.0207 -0.2876 -0.0262 409  MET   A N   
2465  C  CA  . MET   A 340 ? 1.7022 1.7788 1.6792 -0.0213 -0.2743 -0.0217 409  MET   A CA  
2466  C  C   . MET   A 340 ? 1.6210 1.6993 1.5967 -0.0172 -0.2736 -0.0196 409  MET   A C   
2467  O  O   . MET   A 340 ? 1.5593 1.6295 1.5249 -0.0117 -0.2822 -0.0213 409  MET   A O   
2468  C  CB  . MET   A 340 ? 1.6168 1.6770 1.5688 -0.0195 -0.2683 -0.0208 409  MET   A CB  
2469  C  CG  . MET   A 340 ? 1.6373 1.6884 1.5811 -0.0202 -0.2736 -0.0241 409  MET   A CG  
2470  S  SD  . MET   A 340 ? 1.5319 1.5655 1.4482 -0.0181 -0.2635 -0.0220 409  MET   A SD  
2471  C  CE  . MET   A 340 ? 1.3413 1.3867 1.2730 -0.0258 -0.2524 -0.0201 409  MET   A CE  
2472  N  N   . SER   A 341 ? 1.5092 1.5976 1.4949 -0.0198 -0.2634 -0.0160 410  SER   A N   
2473  C  CA  . SER   A 341 ? 1.4371 1.5248 1.4178 -0.0163 -0.2595 -0.0132 410  SER   A CA  
2474  C  C   . SER   A 341 ? 1.3808 1.4661 1.3539 -0.0181 -0.2461 -0.0095 410  SER   A C   
2475  O  O   . SER   A 341 ? 1.3506 1.4443 1.3349 -0.0233 -0.2391 -0.0084 410  SER   A O   
2476  C  CB  . SER   A 341 ? 1.4467 1.5506 1.4497 -0.0172 -0.2612 -0.0125 410  SER   A CB  
2477  O  OG  . SER   A 341 ? 1.4052 1.5071 1.4013 -0.0136 -0.2570 -0.0097 410  SER   A OG  
2478  N  N   . PRO   A 342 ? 1.3825 1.4563 1.3370 -0.0139 -0.2422 -0.0074 411  PRO   A N   
2479  C  CA  . PRO   A 342 ? 1.4006 1.4631 1.3398 -0.0072 -0.2491 -0.0082 411  PRO   A CA  
2480  C  C   . PRO   A 342 ? 1.4048 1.4516 1.3251 -0.0038 -0.2565 -0.0112 411  PRO   A C   
2481  O  O   . PRO   A 342 ? 1.3619 1.4040 1.2767 -0.0064 -0.2533 -0.0118 411  PRO   A O   
2482  C  CB  . PRO   A 342 ? 1.3361 1.3920 1.2628 -0.0053 -0.2391 -0.0044 411  PRO   A CB  
2483  C  CG  . PRO   A 342 ? 1.3281 1.3825 1.2519 -0.0096 -0.2288 -0.0028 411  PRO   A CG  
2484  C  CD  . PRO   A 342 ? 1.3301 1.3992 1.2754 -0.0154 -0.2299 -0.0043 411  PRO   A CD  
2485  N  N   . GLN   A 343 ? 1.4093 1.4472 1.3188 0.0021  -0.2665 -0.0132 412  GLN   A N   
2486  C  CA  . GLN   A 343 ? 1.4154 1.4368 1.3052 0.0060  -0.2740 -0.0162 412  GLN   A CA  
2487  C  C   . GLN   A 343 ? 1.3837 1.3869 1.2465 0.0094  -0.2658 -0.0138 412  GLN   A C   
2488  O  O   . GLN   A 343 ? 1.3872 1.3804 1.2376 0.0091  -0.2643 -0.0147 412  GLN   A O   
2489  C  CB  . GLN   A 343 ? 1.4281 1.4456 1.3151 0.0118  -0.2880 -0.0194 412  GLN   A CB  
2490  C  CG  . GLN   A 343 ? 1.4541 1.4862 1.3653 0.0088  -0.2986 -0.0230 412  GLN   A CG  
2491  C  CD  . GLN   A 343 ? 1.4758 1.5046 1.3870 0.0063  -0.3043 -0.0265 412  GLN   A CD  
2492  O  OE1 . GLN   A 343 ? 1.4933 1.5105 1.3922 0.0107  -0.3153 -0.0302 412  GLN   A OE1 
2493  N  NE2 . GLN   A 343 ? 1.5001 1.5384 1.4245 -0.0004 -0.2970 -0.0256 412  GLN   A NE2 
2494  N  N   . LYS   A 344 ? 1.3256 1.3239 1.1791 0.0127  -0.2603 -0.0107 413  LYS   A N   
2495  C  CA  . LYS   A 344 ? 1.2346 1.2177 1.0659 0.0151  -0.2504 -0.0077 413  LYS   A CA  
2496  C  C   . LYS   A 344 ? 1.2906 1.2827 1.1315 0.0110  -0.2374 -0.0035 413  LYS   A C   
2497  O  O   . LYS   A 344 ? 1.2619 1.2683 1.1210 0.0089  -0.2370 -0.0025 413  LYS   A O   
2498  C  CB  . LYS   A 344 ? 1.2967 1.2630 1.1054 0.0231  -0.2546 -0.0074 413  LYS   A CB  
2499  C  CG  . LYS   A 344 ? 1.4587 1.4049 1.2421 0.0282  -0.2595 -0.0096 413  LYS   A CG  
2500  C  CD  . LYS   A 344 ? 1.4896 1.4164 1.2467 0.0365  -0.2602 -0.0082 413  LYS   A CD  
2501  C  CE  . LYS   A 344 ? 1.5274 1.4368 1.2635 0.0433  -0.2721 -0.0120 413  LYS   A CE  
2502  N  NZ  . LYS   A 344 ? 1.5527 1.4392 1.2579 0.0511  -0.2693 -0.0100 413  LYS   A NZ  
2503  N  N   . PHE   A 345 ? 1.3056 1.2889 1.1342 0.0101  -0.2267 -0.0011 414  PHE   A N   
2504  C  CA  . PHE   A 345 ? 1.3230 1.3096 1.1545 0.0079  -0.2143 0.0030  414  PHE   A CA  
2505  C  C   . PHE   A 345 ? 1.2853 1.2546 1.0943 0.0101  -0.2055 0.0052  414  PHE   A C   
2506  O  O   . PHE   A 345 ? 1.2880 1.2437 1.0800 0.0132  -0.2086 0.0036  414  PHE   A O   
2507  C  CB  . PHE   A 345 ? 1.2390 1.2442 1.0946 0.0005  -0.2085 0.0037  414  PHE   A CB  
2508  C  CG  . PHE   A 345 ? 1.1578 1.1636 1.0150 -0.0036 -0.2049 0.0028  414  PHE   A CG  
2509  C  CD1 . PHE   A 345 ? 1.1669 1.1673 1.0168 -0.0053 -0.1935 0.0053  414  PHE   A CD1 
2510  C  CD2 . PHE   A 345 ? 1.1863 1.1992 1.0543 -0.0061 -0.2127 -0.0005 414  PHE   A CD2 
2511  C  CE1 . PHE   A 345 ? 1.2291 1.2307 1.0813 -0.0089 -0.1902 0.0043  414  PHE   A CE1 
2512  C  CE2 . PHE   A 345 ? 1.2235 1.2370 1.0932 -0.0098 -0.2094 -0.0014 414  PHE   A CE2 
2513  C  CZ  . PHE   A 345 ? 1.2287 1.2366 1.0902 -0.0111 -0.1982 0.0010  414  PHE   A CZ  
2514  N  N   . TRP   A 346 ? 1.2557 1.2252 1.0647 0.0087  -0.1944 0.0089  415  TRP   A N   
2515  C  CA  . TRP   A 346 ? 1.2016 1.1557 0.9914 0.0106  -0.1846 0.0115  415  TRP   A CA  
2516  C  C   . TRP   A 346 ? 1.1920 1.1544 0.9934 0.0046  -0.1728 0.0137  415  TRP   A C   
2517  O  O   . TRP   A 346 ? 1.2101 1.1872 1.0304 0.0004  -0.1697 0.0147  415  TRP   A O   
2518  C  CB  . TRP   A 346 ? 1.2288 1.1718 1.0046 0.0155  -0.1816 0.0142  415  TRP   A CB  
2519  C  CG  . TRP   A 346 ? 1.3004 1.2353 1.0650 0.0219  -0.1927 0.0125  415  TRP   A CG  
2520  C  CD1 . TRP   A 346 ? 1.3528 1.2984 1.1303 0.0225  -0.2010 0.0112  415  TRP   A CD1 
2521  C  CD2 . TRP   A 346 ? 1.3020 1.2159 1.0397 0.0292  -0.1963 0.0121  415  TRP   A CD2 
2522  N  NE1 . TRP   A 346 ? 1.3360 1.2690 1.0970 0.0296  -0.2101 0.0098  415  TRP   A NE1 
2523  C  CE2 . TRP   A 346 ? 1.3381 1.2512 1.0740 0.0339  -0.2075 0.0102  415  TRP   A CE2 
2524  C  CE3 . TRP   A 346 ? 1.2986 1.1940 1.0133 0.0325  -0.1910 0.0131  415  TRP   A CE3 
2525  C  CZ2 . TRP   A 346 ? 1.3723 1.2666 1.0839 0.0418  -0.2141 0.0092  415  TRP   A CZ2 
2526  C  CZ3 . TRP   A 346 ? 1.3262 1.2022 1.0160 0.0404  -0.1971 0.0122  415  TRP   A CZ3 
2527  C  CH2 . TRP   A 346 ? 1.3724 1.2478 1.0605 0.0450  -0.2088 0.0102  415  TRP   A CH2 
2528  N  N   . GLY   A 347 ? 1.1440 1.0963 0.9333 0.0046  -0.1660 0.0145  416  GLY   A N   
2529  C  CA  . GLY   A 347 ? 1.0847 1.0422 0.8821 -0.0001 -0.1541 0.0168  416  GLY   A CA  
2530  C  C   . GLY   A 347 ? 1.1050 1.0482 0.8862 0.0026  -0.1437 0.0204  416  GLY   A C   
2531  O  O   . GLY   A 347 ? 1.1578 1.0838 0.9175 0.0073  -0.1431 0.0206  416  GLY   A O   
2532  N  N   . LEU   A 348 ? 1.1334 1.0827 0.9243 -0.0001 -0.1357 0.0231  417  LEU   A N   
2533  C  CA  . LEU   A 348 ? 1.0875 1.0242 0.8655 0.0020  -0.1254 0.0268  417  LEU   A CA  
2534  C  C   . LEU   A 348 ? 1.0949 1.0380 0.8842 -0.0033 -0.1142 0.0285  417  LEU   A C   
2535  O  O   . LEU   A 348 ? 1.0904 1.0501 0.9006 -0.0084 -0.1138 0.0278  417  LEU   A O   
2536  C  CB  . LEU   A 348 ? 1.0767 1.0133 0.8553 0.0039  -0.1261 0.0285  417  LEU   A CB  
2537  C  CG  . LEU   A 348 ? 1.0580 0.9959 0.8349 0.0075  -0.1390 0.0261  417  LEU   A CG  
2538  C  CD1 . LEU   A 348 ? 1.0241 0.9699 0.8113 0.0072  -0.1401 0.0273  417  LEU   A CD1 
2539  C  CD2 . LEU   A 348 ? 1.0599 0.9779 0.8107 0.0147  -0.1433 0.0257  417  LEU   A CD2 
2540  N  N   . THR   A 349 ? 1.1337 1.0636 0.9090 -0.0017 -0.1050 0.0306  418  THR   A N   
2541  C  CA  . THR   A 349 ? 1.1712 1.1059 0.9560 -0.0062 -0.0945 0.0319  418  THR   A CA  
2542  C  C   . THR   A 349 ? 1.1455 1.0806 0.9358 -0.0079 -0.0849 0.0353  418  THR   A C   
2543  O  O   . THR   A 349 ? 1.0771 0.9982 0.8523 -0.0040 -0.0805 0.0379  418  THR   A O   
2544  C  CB  . THR   A 349 ? 1.1086 1.0297 0.8769 -0.0038 -0.0897 0.0322  418  THR   A CB  
2545  O  OG1 . THR   A 349 ? 1.1099 1.0341 0.8865 -0.0075 -0.0782 0.0340  418  THR   A OG1 
2546  C  CG2 . THR   A 349 ? 1.0622 0.9620 0.8042 0.0032  -0.0886 0.0340  418  THR   A CG2 
2547  N  N   . ARG   A 350 ? 1.1096 1.0602 0.9213 -0.0135 -0.0818 0.0352  419  ARG   A N   
2548  C  CA  . ARG   A 350 ? 1.1154 1.0691 0.9361 -0.0157 -0.0746 0.0377  419  ARG   A CA  
2549  C  C   . ARG   A 350 ? 1.1140 1.0515 0.9199 -0.0132 -0.0643 0.0412  419  ARG   A C   
2550  O  O   . ARG   A 350 ? 1.1351 1.0687 0.9397 -0.0124 -0.0611 0.0435  419  ARG   A O   
2551  C  CB  . ARG   A 350 ? 1.0649 1.0342 0.9074 -0.0218 -0.0707 0.0370  419  ARG   A CB  
2552  C  CG  . ARG   A 350 ? 1.0897 1.0651 0.9448 -0.0246 -0.0660 0.0387  419  ARG   A CG  
2553  C  CD  . ARG   A 350 ? 1.1647 1.1517 1.0375 -0.0298 -0.0609 0.0381  419  ARG   A CD  
2554  N  NE  . ARG   A 350 ? 1.1568 1.1362 1.0229 -0.0297 -0.0532 0.0389  419  ARG   A NE  
2555  C  CZ  . ARG   A 350 ? 1.2067 1.1761 1.0668 -0.0291 -0.0433 0.0418  419  ARG   A CZ  
2556  N  NH1 . ARG   A 350 ? 1.1854 1.1506 1.0449 -0.0287 -0.0398 0.0441  419  ARG   A NH1 
2557  N  NH2 . ARG   A 350 ? 1.3043 1.2675 1.1588 -0.0289 -0.0364 0.0425  419  ARG   A NH2 
2558  N  N   . SER   A 351 ? 1.0984 1.0261 0.8931 -0.0118 -0.0587 0.0419  420  SER   A N   
2559  C  CA  . SER   A 351 ? 1.1377 1.0509 0.9205 -0.0099 -0.0471 0.0455  420  SER   A CA  
2560  C  C   . SER   A 351 ? 1.1771 1.0730 0.9380 -0.0037 -0.0482 0.0474  420  SER   A C   
2561  O  O   . SER   A 351 ? 1.1681 1.0529 0.9212 -0.0024 -0.0388 0.0509  420  SER   A O   
2562  C  CB  . SER   A 351 ? 1.1231 1.0300 0.8990 -0.0095 -0.0410 0.0456  420  SER   A CB  
2563  O  OG  . SER   A 351 ? 1.1807 1.0908 0.9539 -0.0086 -0.0501 0.0422  420  SER   A OG  
2564  N  N   . ALA   A 352 ? 1.1588 1.0518 0.9097 0.0002  -0.0595 0.0452  421  ALA   A N   
2565  C  CA  . ALA   A 352 ? 1.1432 1.0196 0.8728 0.0066  -0.0615 0.0468  421  ALA   A CA  
2566  C  C   . ALA   A 352 ? 1.1642 1.0450 0.9003 0.0063  -0.0643 0.0477  421  ALA   A C   
2567  O  O   . ALA   A 352 ? 1.1983 1.0646 0.9175 0.0113  -0.0635 0.0497  421  ALA   A O   
2568  C  CB  . ALA   A 352 ? 1.1232 0.9927 0.8374 0.0116  -0.0729 0.0439  421  ALA   A CB  
2569  N  N   . LEU   A 353 ? 1.1209 1.0204 0.8802 0.0011  -0.0671 0.0463  422  LEU   A N   
2570  C  CA  . LEU   A 353 ? 1.1494 1.0547 0.9153 0.0013  -0.0725 0.0463  422  LEU   A CA  
2571  C  C   . LEU   A 353 ? 1.1513 1.0581 0.9264 -0.0017 -0.0631 0.0493  422  LEU   A C   
2572  O  O   . LEU   A 353 ? 1.1880 1.0976 0.9721 -0.0058 -0.0538 0.0505  422  LEU   A O   
2573  C  CB  . LEU   A 353 ? 1.1302 1.0545 0.9148 -0.0019 -0.0825 0.0428  422  LEU   A CB  
2574  C  CG  . LEU   A 353 ? 1.0888 1.0122 0.8658 0.0011  -0.0931 0.0396  422  LEU   A CG  
2575  C  CD1 . LEU   A 353 ? 1.0155 0.9581 0.8126 -0.0029 -0.1011 0.0363  422  LEU   A CD1 
2576  C  CD2 . LEU   A 353 ? 1.0549 0.9667 0.8150 0.0075  -0.0999 0.0398  422  LEU   A CD2 
2577  N  N   . LEU   A 354 ? 1.1419 1.0461 0.9144 0.0004  -0.0660 0.0503  423  LEU   A N   
2578  C  CA  . LEU   A 354 ? 1.1682 1.0735 0.9490 -0.0020 -0.0590 0.0528  423  LEU   A CA  
2579  C  C   . LEU   A 354 ? 1.1554 1.0710 0.9466 -0.0023 -0.0669 0.0516  423  LEU   A C   
2580  O  O   . LEU   A 354 ? 1.1467 1.0555 0.9258 0.0027  -0.0737 0.0514  423  LEU   A O   
2581  C  CB  . LEU   A 354 ? 1.1858 1.0708 0.9467 0.0021  -0.0512 0.0565  423  LEU   A CB  
2582  C  CG  . LEU   A 354 ? 1.1432 1.0271 0.9114 -0.0005 -0.0429 0.0593  423  LEU   A CG  
2583  C  CD1 . LEU   A 354 ? 1.1924 1.0740 0.9661 -0.0043 -0.0303 0.0615  423  LEU   A CD1 
2584  C  CD2 . LEU   A 354 ? 1.2599 1.1265 1.0080 0.0053  -0.0424 0.0619  423  LEU   A CD2 
2585  N  N   . PRO   A 355 ? 1.1850 1.1167 0.9980 -0.0076 -0.0666 0.0506  424  PRO   A N   
2586  C  CA  . PRO   A 355 ? 1.1563 1.0975 0.9792 -0.0077 -0.0732 0.0497  424  PRO   A CA  
2587  C  C   . PRO   A 355 ? 1.1759 1.1063 0.9903 -0.0052 -0.0698 0.0525  424  PRO   A C   
2588  O  O   . PRO   A 355 ? 1.2009 1.1218 1.0111 -0.0061 -0.0600 0.0553  424  PRO   A O   
2589  C  CB  . PRO   A 355 ? 1.1312 1.0893 0.9775 -0.0140 -0.0713 0.0484  424  PRO   A CB  
2590  C  CG  . PRO   A 355 ? 1.1446 1.1048 0.9936 -0.0168 -0.0672 0.0476  424  PRO   A CG  
2591  C  CD  . PRO   A 355 ? 1.1533 1.0953 0.9826 -0.0135 -0.0606 0.0501  424  PRO   A CD  
2592  N  N   . THR   A 356 ? 1.1504 1.0823 0.9628 -0.0019 -0.0778 0.0518  425  THR   A N   
2593  C  CA  . THR   A 356 ? 1.2170 1.1368 1.0181 0.0017  -0.0758 0.0543  425  THR   A CA  
2594  C  C   . THR   A 356 ? 1.2159 1.1456 1.0265 0.0024  -0.0834 0.0531  425  THR   A C   
2595  O  O   . THR   A 356 ? 1.1932 1.1362 1.0142 0.0019  -0.0916 0.0503  425  THR   A O   
2596  C  CB  . THR   A 356 ? 1.2452 1.1461 1.0207 0.0083  -0.0769 0.0556  425  THR   A CB  
2597  O  OG1 . THR   A 356 ? 1.2187 1.1227 0.9896 0.0124  -0.0888 0.0529  425  THR   A OG1 
2598  C  CG2 . THR   A 356 ? 1.1731 1.0645 0.9390 0.0079  -0.0694 0.0566  425  THR   A CG2 
2599  N  N   . ILE   A 357 ? 1.1578 1.0806 0.9649 0.0036  -0.0801 0.0553  426  ILE   A N   
2600  C  CA  . ILE   A 357 ? 1.1494 1.0811 0.9665 0.0039  -0.0855 0.0546  426  ILE   A CA  
2601  C  C   . ILE   A 357 ? 1.2289 1.1499 1.0296 0.0107  -0.0913 0.0553  426  ILE   A C   
2602  O  O   . ILE   A 357 ? 1.3865 1.2932 1.1747 0.0132  -0.0862 0.0580  426  ILE   A O   
2603  C  CB  . ILE   A 357 ? 1.1470 1.0803 0.9747 -0.0002 -0.0780 0.0562  426  ILE   A CB  
2604  C  CG1 . ILE   A 357 ? 1.0863 1.0306 0.9310 -0.0068 -0.0730 0.0553  426  ILE   A CG1 
2605  C  CG2 . ILE   A 357 ? 1.1980 1.1396 1.0347 0.0005  -0.0836 0.0554  426  ILE   A CG2 
2606  C  CD1 . ILE   A 357 ? 1.1513 1.0962 1.0062 -0.0107 -0.0660 0.0566  426  ILE   A CD1 
2607  N  N   . PRO   A 358 ? 1.1705 1.0977 0.9710 0.0141  -0.1018 0.0529  427  PRO   A N   
2608  C  CA  . PRO   A 358 ? 1.2254 1.1430 1.0105 0.0212  -0.1087 0.0530  427  PRO   A CA  
2609  C  C   . PRO   A 358 ? 1.3148 1.2324 1.1018 0.0232  -0.1102 0.0540  427  PRO   A C   
2610  O  O   . PRO   A 358 ? 1.3356 1.2434 1.1086 0.0294  -0.1149 0.0546  427  PRO   A O   
2611  C  CB  . PRO   A 358 ? 1.1265 1.0552 0.9174 0.0226  -0.1195 0.0496  427  PRO   A CB  
2612  C  CG  . PRO   A 358 ? 1.2100 1.1570 1.0232 0.0164  -0.1189 0.0479  427  PRO   A CG  
2613  C  CD  . PRO   A 358 ? 1.2225 1.1665 1.0382 0.0113  -0.1078 0.0497  427  PRO   A CD  
2614  N  N   . VAL   A 369 ? 1.6670 1.5758 1.5123 -0.0099 -0.0486 0.0657  438  VAL   A N   
2615  C  CA  . VAL   A 369 ? 1.5803 1.5071 1.4406 -0.0124 -0.0545 0.0623  438  VAL   A CA  
2616  C  C   . VAL   A 369 ? 1.5513 1.4828 1.4212 -0.0175 -0.0483 0.0619  438  VAL   A C   
2617  O  O   . VAL   A 369 ? 1.6047 1.5289 1.4645 -0.0166 -0.0446 0.0629  438  VAL   A O   
2618  C  CB  . VAL   A 369 ? 1.5677 1.4983 1.4200 -0.0076 -0.0635 0.0607  438  VAL   A CB  
2619  C  CG1 . VAL   A 369 ? 1.5521 1.4836 1.4012 -0.0032 -0.0710 0.0603  438  VAL   A CG1 
2620  C  CG2 . VAL   A 369 ? 1.6267 1.5430 1.4594 -0.0040 -0.0610 0.0625  438  VAL   A CG2 
2621  N  N   . ILE   A 370 ? 1.4865 1.4298 1.3753 -0.0226 -0.0474 0.0602  439  ILE   A N   
2622  C  CA  . ILE   A 370 ? 1.4497 1.3986 1.3495 -0.0275 -0.0419 0.0595  439  ILE   A CA  
2623  C  C   . ILE   A 370 ? 1.3630 1.3294 1.2772 -0.0296 -0.0483 0.0560  439  ILE   A C   
2624  O  O   . ILE   A 370 ? 1.3119 1.2867 1.2302 -0.0280 -0.0558 0.0543  439  ILE   A O   
2625  C  CB  . ILE   A 370 ? 1.3652 1.3112 1.2755 -0.0322 -0.0340 0.0605  439  ILE   A CB  
2626  C  CG1 . ILE   A 370 ? 1.3339 1.2637 1.2318 -0.0300 -0.0291 0.0638  439  ILE   A CG1 
2627  C  CG2 . ILE   A 370 ? 1.4117 1.3588 1.3283 -0.0361 -0.0267 0.0607  439  ILE   A CG2 
2628  C  CD1 . ILE   A 370 ? 1.3291 1.2561 1.2382 -0.0346 -0.0219 0.0647  439  ILE   A CD1 
2629  N  N   . LEU   A 371 ? 1.2951 1.2668 1.2171 -0.0332 -0.0446 0.0551  440  LEU   A N   
2630  C  CA  . LEU   A 371 ? 1.2874 1.2751 1.2244 -0.0359 -0.0491 0.0520  440  LEU   A CA  
2631  C  C   . LEU   A 371 ? 1.2932 1.2875 1.2473 -0.0403 -0.0468 0.0509  440  LEU   A C   
2632  O  O   . LEU   A 371 ? 1.2753 1.2637 1.2331 -0.0432 -0.0393 0.0523  440  LEU   A O   
2633  C  CB  . LEU   A 371 ? 1.2745 1.2644 1.2108 -0.0371 -0.0470 0.0514  440  LEU   A CB  
2634  C  CG  . LEU   A 371 ? 1.2287 1.2134 1.1491 -0.0327 -0.0507 0.0518  440  LEU   A CG  
2635  C  CD1 . LEU   A 371 ? 1.1965 1.1882 1.1162 -0.0295 -0.0606 0.0502  440  LEU   A CD1 
2636  C  CD2 . LEU   A 371 ? 1.3562 1.3233 1.2583 -0.0295 -0.0455 0.0550  440  LEU   A CD2 
2637  N  N   . CYS   A 372 ? 1.2643 1.2707 1.2292 -0.0408 -0.0533 0.0484  441  CYS   A N   
2638  C  CA  . CYS   A 372 ? 1.2285 1.2406 1.2077 -0.0438 -0.0533 0.0470  441  CYS   A CA  
2639  C  C   . CYS   A 372 ? 1.2056 1.2302 1.1999 -0.0474 -0.0540 0.0443  441  CYS   A C   
2640  O  O   . CYS   A 372 ? 1.1986 1.2301 1.1930 -0.0470 -0.0568 0.0431  441  CYS   A O   
2641  C  CB  . CYS   A 372 ? 1.2562 1.2712 1.2349 -0.0408 -0.0601 0.0464  441  CYS   A CB  
2642  S  SG  . CYS   A 372 ? 1.3461 1.3557 1.3303 -0.0421 -0.0580 0.0468  441  CYS   A SG  
2643  N  N   . LEU   A 373 ? 1.2052 1.2324 1.2123 -0.0508 -0.0519 0.0432  442  LEU   A N   
2644  C  CA  . LEU   A 373 ? 1.2275 1.2660 1.2496 -0.0540 -0.0529 0.0405  442  LEU   A CA  
2645  C  C   . LEU   A 373 ? 1.2113 1.2577 1.2421 -0.0536 -0.0592 0.0381  442  LEU   A C   
2646  O  O   . LEU   A 373 ? 1.1677 1.2180 1.2111 -0.0564 -0.0588 0.0362  442  LEU   A O   
2647  C  CB  . LEU   A 373 ? 1.1540 1.1900 1.1856 -0.0583 -0.0458 0.0406  442  LEU   A CB  
2648  C  CG  . LEU   A 373 ? 1.1750 1.1997 1.1986 -0.0589 -0.0376 0.0435  442  LEU   A CG  
2649  C  CD1 . LEU   A 373 ? 1.1938 1.2185 1.2311 -0.0635 -0.0311 0.0432  442  LEU   A CD1 
2650  C  CD2 . LEU   A 373 ? 1.2392 1.2631 1.2525 -0.0572 -0.0367 0.0444  442  LEU   A CD2 
2651  O  OXT . LEU   A 373 ? 1.1785 1.2274 1.2039 -0.0502 -0.0648 0.0380  442  LEU   A OXT 
2652  N  N   . SER   B 2   ? 1.2660 1.2718 1.6167 -0.1351 -0.0326 0.0057  2    SER   B N   
2653  C  CA  . SER   B 2   ? 1.2946 1.2976 1.6605 -0.1376 -0.0405 0.0011  2    SER   B CA  
2654  C  C   . SER   B 2   ? 1.2760 1.2898 1.6539 -0.1364 -0.0525 -0.0057 2    SER   B C   
2655  O  O   . SER   B 2   ? 1.2726 1.2970 1.6535 -0.1352 -0.0529 -0.0068 2    SER   B O   
2656  C  CB  . SER   B 2   ? 1.2767 1.2682 1.6251 -0.1346 -0.0451 0.0018  2    SER   B CB  
2657  O  OG  . SER   B 2   ? 1.2196 1.2137 1.5478 -0.1281 -0.0533 0.0007  2    SER   B OG  
2658  N  N   . TYR   B 3   ? 1.2645 1.2748 1.6487 -0.1364 -0.0624 -0.0102 3    TYR   B N   
2659  C  CA  . TYR   B 3   ? 1.2605 1.2786 1.6544 -0.1347 -0.0750 -0.0169 3    TYR   B CA  
2660  C  C   . TYR   B 3   ? 1.2870 1.2979 1.6657 -0.1301 -0.0855 -0.0193 3    TYR   B C   
2661  O  O   . TYR   B 3   ? 1.2883 1.2882 1.6639 -0.1314 -0.0848 -0.0181 3    TYR   B O   
2662  C  CB  . TYR   B 3   ? 1.3409 1.3619 1.7651 -0.1405 -0.0765 -0.0211 3    TYR   B CB  
2663  C  CG  . TYR   B 3   ? 1.3967 1.4214 1.8378 -0.1461 -0.0637 -0.0177 3    TYR   B CG  
2664  C  CD1 . TYR   B 3   ? 1.4047 1.4411 1.8538 -0.1461 -0.0611 -0.0182 3    TYR   B CD1 
2665  C  CD2 . TYR   B 3   ? 1.3803 1.3961 1.8296 -0.1512 -0.0542 -0.0141 3    TYR   B CD2 
2666  C  CE1 . TYR   B 3   ? 1.4349 1.4744 1.8996 -0.1509 -0.0491 -0.0151 3    TYR   B CE1 
2667  C  CE2 . TYR   B 3   ? 1.3828 1.4016 1.8479 -0.1562 -0.0419 -0.0110 3    TYR   B CE2 
2668  C  CZ  . TYR   B 3   ? 1.4019 1.4326 1.8747 -0.1559 -0.0394 -0.0115 3    TYR   B CZ  
2669  O  OH  . TYR   B 3   ? 1.3807 1.4142 1.8689 -0.1604 -0.0269 -0.0083 3    TYR   B OH  
2670  N  N   . ASN   B 4   ? 1.2228 1.2392 1.5909 -0.1246 -0.0948 -0.0224 4    ASN   B N   
2671  C  CA  . ASN   B 4   ? 1.2137 1.2232 1.5635 -0.1193 -0.1034 -0.0238 4    ASN   B CA  
2672  C  C   . ASN   B 4   ? 1.1806 1.1938 1.5355 -0.1162 -0.1170 -0.0307 4    ASN   B C   
2673  O  O   . ASN   B 4   ? 1.1799 1.2025 1.5483 -0.1168 -0.1202 -0.0342 4    ASN   B O   
2674  C  CB  . ASN   B 4   ? 1.1916 1.2013 1.5159 -0.1142 -0.0998 -0.0192 4    ASN   B CB  
2675  C  CG  . ASN   B 4   ? 1.2840 1.2859 1.5991 -0.1161 -0.0885 -0.0128 4    ASN   B CG  
2676  O  OD1 . ASN   B 4   ? 1.3133 1.3058 1.6127 -0.1135 -0.0892 -0.0107 4    ASN   B OD1 
2677  N  ND2 . ASN   B 4   ? 1.3304 1.3353 1.6548 -0.1204 -0.0781 -0.0096 4    ASN   B ND2 
2678  N  N   . TYR   B 5   ? 1.1641 1.1688 1.5083 -0.1126 -0.1250 -0.0327 5    TYR   B N   
2679  C  CA  . TYR   B 5   ? 1.1195 1.1245 1.4655 -0.1090 -0.1384 -0.0392 5    TYR   B CA  
2680  C  C   . TYR   B 5   ? 1.1788 1.1803 1.4987 -0.1014 -0.1433 -0.0384 5    TYR   B C   
2681  O  O   . TYR   B 5   ? 1.1641 1.1571 1.4690 -0.0998 -0.1403 -0.0349 5    TYR   B O   
2682  C  CB  . TYR   B 5   ? 1.0807 1.0774 1.4419 -0.1125 -0.1439 -0.0431 5    TYR   B CB  
2683  C  CG  . TYR   B 5   ? 1.0788 1.0722 1.4416 -0.1088 -0.1585 -0.0502 5    TYR   B CG  
2684  C  CD1 . TYR   B 5   ? 1.0862 1.0691 1.4314 -0.1040 -0.1648 -0.0509 5    TYR   B CD1 
2685  C  CD2 . TYR   B 5   ? 1.0905 1.0902 1.4730 -0.1102 -0.1660 -0.0562 5    TYR   B CD2 
2686  C  CE1 . TYR   B 5   ? 1.0927 1.0709 1.4380 -0.1002 -0.1782 -0.0574 5    TYR   B CE1 
2687  C  CE2 . TYR   B 5   ? 1.1213 1.1163 1.5044 -0.1064 -0.1802 -0.0630 5    TYR   B CE2 
2688  C  CZ  . TYR   B 5   ? 1.1580 1.1419 1.5218 -0.1014 -0.1861 -0.0635 5    TYR   B CZ  
2689  O  OH  . TYR   B 5   ? 1.1003 1.0781 1.4622 -0.0971 -0.1998 -0.0699 5    TYR   B OH  
2690  N  N   . VAL   B 6   ? 1.1690 1.1773 1.4835 -0.0965 -0.1501 -0.0414 6    VAL   B N   
2691  C  CA  . VAL   B 6   ? 1.0477 1.0543 1.3391 -0.0890 -0.1547 -0.0409 6    VAL   B CA  
2692  C  C   . VAL   B 6   ? 1.0291 1.0313 1.3207 -0.0850 -0.1677 -0.0473 6    VAL   B C   
2693  O  O   . VAL   B 6   ? 1.0296 1.0359 1.3372 -0.0864 -0.1737 -0.0524 6    VAL   B O   
2694  C  CB  . VAL   B 6   ? 1.0204 1.0377 1.3043 -0.0864 -0.1514 -0.0390 6    VAL   B CB  
2695  C  CG1 . VAL   B 6   ? 1.0464 1.0620 1.3074 -0.0791 -0.1548 -0.0378 6    VAL   B CG1 
2696  C  CG2 . VAL   B 6   ? 1.0520 1.0736 1.3380 -0.0907 -0.1392 -0.0334 6    VAL   B CG2 
2697  N  N   . VAL   B 7   ? 1.0189 1.0126 1.2924 -0.0796 -0.1723 -0.0473 7    VAL   B N   
2698  C  CA  . VAL   B 7   ? 1.0891 1.0776 1.3594 -0.0746 -0.1846 -0.0532 7    VAL   B CA  
2699  C  C   . VAL   B 7   ? 1.0767 1.0618 1.3221 -0.0667 -0.1868 -0.0514 7    VAL   B C   
2700  O  O   . VAL   B 7   ? 1.0496 1.0316 1.2816 -0.0657 -0.1805 -0.0464 7    VAL   B O   
2701  C  CB  . VAL   B 7   ? 1.1325 1.1101 1.4124 -0.0771 -0.1905 -0.0568 7    VAL   B CB  
2702  C  CG1 . VAL   B 7   ? 1.0788 1.0466 1.3463 -0.0771 -0.1857 -0.0525 7    VAL   B CG1 
2703  C  CG2 . VAL   B 7   ? 1.1065 1.0788 1.3830 -0.0715 -0.2041 -0.0634 7    VAL   B CG2 
2704  N  N   . THR   B 8   ? 1.0503 1.0357 1.2896 -0.0609 -0.1958 -0.0557 8    THR   B N   
2705  C  CA  . THR   B 8   ? 1.0510 1.0325 1.2674 -0.0530 -0.1981 -0.0544 8    THR   B CA  
2706  C  C   . THR   B 8   ? 1.1158 1.0838 1.3238 -0.0502 -0.2039 -0.0561 8    THR   B C   
2707  O  O   . THR   B 8   ? 1.1158 1.0774 1.3323 -0.0504 -0.2125 -0.0615 8    THR   B O   
2708  C  CB  . THR   B 8   ? 0.9966 0.9824 1.2078 -0.0473 -0.2047 -0.0579 8    THR   B CB  
2709  O  OG1 . THR   B 8   ? 1.0948 1.0925 1.3066 -0.0485 -0.1977 -0.0546 8    THR   B OG1 
2710  C  CG2 . THR   B 8   ? 0.9765 0.9547 1.1654 -0.0389 -0.2091 -0.0578 8    THR   B CG2 
2711  N  N   . ALA   B 9   ? 1.0950 1.0588 1.2866 -0.0474 -0.1992 -0.0515 9    ALA   B N   
2712  C  CA  . ALA   B 9   ? 0.9938 0.9447 1.1737 -0.0435 -0.2038 -0.0523 9    ALA   B CA  
2713  C  C   . ALA   B 9   ? 1.0188 0.9669 1.1789 -0.0343 -0.2088 -0.0531 9    ALA   B C   
2714  O  O   . ALA   B 9   ? 1.0769 1.0140 1.2281 -0.0297 -0.2158 -0.0558 9    ALA   B O   
2715  C  CB  . ALA   B 9   ? 1.0622 1.0092 1.2362 -0.0459 -0.1954 -0.0467 9    ALA   B CB  
2716  N  N   . GLN   B 10  ? 1.0116 0.9691 1.1646 -0.0314 -0.2052 -0.0507 10   GLN   B N   
2717  C  CA  . GLN   B 10  ? 1.0243 0.9800 1.1595 -0.0227 -0.2091 -0.0512 10   GLN   B CA  
2718  C  C   . GLN   B 10  ? 1.0654 1.0324 1.2027 -0.0218 -0.2078 -0.0513 10   GLN   B C   
2719  O  O   . GLN   B 10  ? 1.0994 1.0763 1.2394 -0.0251 -0.1997 -0.0471 10   GLN   B O   
2720  C  CB  . GLN   B 10  ? 1.0044 0.9574 1.1222 -0.0188 -0.2037 -0.0460 10   GLN   B CB  
2721  C  CG  . GLN   B 10  ? 0.9936 0.9475 1.0941 -0.0102 -0.2052 -0.0453 10   GLN   B CG  
2722  C  CD  . GLN   B 10  ? 1.0561 1.0010 1.1504 -0.0040 -0.2155 -0.0509 10   GLN   B CD  
2723  O  OE1 . GLN   B 10  ? 1.0898 1.0229 1.1771 -0.0010 -0.2204 -0.0527 10   GLN   B OE1 
2724  N  NE2 . GLN   B 10  ? 1.0698 1.0197 1.1657 -0.0018 -0.2189 -0.0536 10   GLN   B NE2 
2725  N  N   . LYS   B 11  ? 1.0387 1.0040 1.1745 -0.0173 -0.2161 -0.0562 11   LYS   B N   
2726  C  CA  . LYS   B 11  ? 1.0012 0.9759 1.1369 -0.0155 -0.2154 -0.0565 11   LYS   B CA  
2727  C  C   . LYS   B 11  ? 1.0291 1.0089 1.1496 -0.0116 -0.2084 -0.0510 11   LYS   B C   
2728  O  O   . LYS   B 11  ? 1.0051 0.9793 1.1123 -0.0079 -0.2066 -0.0483 11   LYS   B O   
2729  C  CB  . LYS   B 11  ? 1.0747 1.0439 1.2067 -0.0096 -0.2258 -0.0625 11   LYS   B CB  
2730  C  CG  . LYS   B 11  ? 1.1094 1.0809 1.2603 -0.0138 -0.2319 -0.0679 11   LYS   B CG  
2731  C  CD  . LYS   B 11  ? 1.1130 1.0773 1.2585 -0.0072 -0.2432 -0.0742 11   LYS   B CD  
2732  C  CE  . LYS   B 11  ? 1.1740 1.1255 1.3217 -0.0066 -0.2522 -0.0789 11   LYS   B CE  
2733  N  NZ  . LYS   B 11  ? 1.2276 1.1698 1.3652 0.0015  -0.2633 -0.0846 11   LYS   B NZ  
2734  N  N   . PRO   B 12  ? 1.0580 1.0486 1.1807 -0.0123 -0.2043 -0.0494 12   PRO   B N   
2735  C  CA  . PRO   B 12  ? 1.0209 1.0163 1.1297 -0.0081 -0.1986 -0.0448 12   PRO   B CA  
2736  C  C   . PRO   B 12  ? 0.9853 0.9726 1.0769 0.0009  -0.2035 -0.0461 12   PRO   B C   
2737  O  O   . PRO   B 12  ? 0.9978 0.9791 1.0879 0.0047  -0.2115 -0.0510 12   PRO   B O   
2738  C  CB  . PRO   B 12  ? 0.9984 1.0052 1.1144 -0.0103 -0.1958 -0.0446 12   PRO   B CB  
2739  C  CG  . PRO   B 12  ? 0.9701 0.9763 1.1005 -0.0131 -0.2023 -0.0501 12   PRO   B CG  
2740  C  CD  . PRO   B 12  ? 1.0425 1.0417 1.1813 -0.0173 -0.2041 -0.0515 12   PRO   B CD  
2741  N  N   . THR   B 13  ? 0.9468 0.9336 1.0251 0.0047  -0.1988 -0.0417 13   THR   B N   
2742  C  CA  . THR   B 13  ? 0.9863 0.9654 1.0476 0.0136  -0.2021 -0.0422 13   THR   B CA  
2743  C  C   . THR   B 13  ? 0.9962 0.9821 1.0480 0.0181  -0.1976 -0.0390 13   THR   B C   
2744  O  O   . THR   B 13  ? 1.0386 1.0186 1.0771 0.0257  -0.2004 -0.0399 13   THR   B O   
2745  C  CB  . THR   B 13  ? 1.0691 1.0400 1.1212 0.0158  -0.2012 -0.0400 13   THR   B CB  
2746  O  OG1 . THR   B 13  ? 1.0776 1.0558 1.1278 0.0138  -0.1926 -0.0342 13   THR   B OG1 
2747  C  CG2 . THR   B 13  ? 1.0150 0.9784 1.0764 0.0111  -0.2052 -0.0428 13   THR   B CG2 
2748  N  N   . ALA   B 14  ? 1.0588 1.0562 1.1165 0.0137  -0.1904 -0.0353 14   ALA   B N   
2749  C  CA  . ALA   B 14  ? 0.9945 0.9987 1.0445 0.0174  -0.1860 -0.0323 14   ALA   B CA  
2750  C  C   . ALA   B 14  ? 1.0039 1.0089 1.0544 0.0199  -0.1901 -0.0358 14   ALA   B C   
2751  O  O   . ALA   B 14  ? 0.9984 1.0053 1.0606 0.0157  -0.1934 -0.0392 14   ALA   B O   
2752  C  CB  . ALA   B 14  ? 1.0330 1.0489 1.0899 0.0118  -0.1780 -0.0278 14   ALA   B CB  
2753  N  N   . VAL   B 15  ? 1.0443 1.0476 1.0821 0.0271  -0.1899 -0.0351 15   VAL   B N   
2754  C  CA  . VAL   B 15  ? 1.0604 1.0638 1.0964 0.0303  -0.1931 -0.0379 15   VAL   B CA  
2755  C  C   . VAL   B 15  ? 1.0720 1.0878 1.1124 0.0275  -0.1864 -0.0346 15   VAL   B C   
2756  O  O   . VAL   B 15  ? 1.0928 1.1139 1.1288 0.0280  -0.1798 -0.0299 15   VAL   B O   
2757  C  CB  . VAL   B 15  ? 1.1060 1.0995 1.1248 0.0401  -0.1962 -0.0388 15   VAL   B CB  
2758  C  CG1 . VAL   B 15  ? 1.1079 1.1007 1.1239 0.0437  -0.1994 -0.0417 15   VAL   B CG1 
2759  C  CG2 . VAL   B 15  ? 1.0471 1.0274 1.0607 0.0432  -0.2030 -0.0421 15   VAL   B CG2 
2760  N  N   . ASN   B 16  ? 1.1842 1.2048 1.2338 0.0242  -0.1881 -0.0371 16   ASN   B N   
2761  C  CA  . ASN   B 16  ? 1.1724 1.2042 1.2259 0.0214  -0.1819 -0.0341 16   ASN   B CA  
2762  C  C   . ASN   B 16  ? 1.1777 1.2092 1.2252 0.0263  -0.1835 -0.0357 16   ASN   B C   
2763  O  O   . ASN   B 16  ? 1.2720 1.3122 1.3223 0.0243  -0.1787 -0.0335 16   ASN   B O   
2764  C  CB  . ASN   B 16  ? 1.2109 1.2509 1.2809 0.0127  -0.1801 -0.0344 16   ASN   B CB  
2765  C  CG  . ASN   B 16  ? 1.2032 1.2408 1.2822 0.0112  -0.1868 -0.0398 16   ASN   B CG  
2766  O  OD1 . ASN   B 16  ? 1.2207 1.2550 1.2948 0.0158  -0.1912 -0.0427 16   ASN   B OD1 
2767  N  ND2 . ASN   B 16  ? 1.2149 1.2538 1.3072 0.0048  -0.1876 -0.0411 16   ASN   B ND2 
2768  N  N   . GLY   B 17  ? 1.0815 1.1027 1.1202 0.0327  -0.1901 -0.0395 17   GLY   B N   
2769  C  CA  . GLY   B 17  ? 1.0731 1.0924 1.1048 0.0379  -0.1918 -0.0411 17   GLY   B CA  
2770  C  C   . GLY   B 17  ? 1.1383 1.1441 1.1600 0.0451  -0.2004 -0.0458 17   GLY   B C   
2771  O  O   . GLY   B 17  ? 1.0853 1.0852 1.1120 0.0438  -0.2070 -0.0497 17   GLY   B O   
2772  N  N   . CYS   B 18  ? 1.1311 1.1317 1.1388 0.0528  -0.2003 -0.0456 18   CYS   B N   
2773  C  CA  . CYS   B 18  ? 1.0238 1.0099 1.0176 0.0613  -0.2073 -0.0492 18   CYS   B CA  
2774  C  C   . CYS   B 18  ? 1.1392 1.1217 1.1225 0.0676  -0.2079 -0.0501 18   CYS   B C   
2775  O  O   . CYS   B 18  ? 1.1659 1.1519 1.1418 0.0702  -0.2005 -0.0457 18   CYS   B O   
2776  C  CB  . CYS   B 18  ? 1.0131 0.9928 0.9945 0.0661  -0.2046 -0.0462 18   CYS   B CB  
2777  S  SG  . CYS   B 18  ? 1.2046 1.1922 1.1792 0.0677  -0.1926 -0.0387 18   CYS   B SG  
2778  N  N   . VAL   B 19  ? 1.1564 1.1319 1.1392 0.0703  -0.2166 -0.0558 19   VAL   B N   
2779  C  CA  . VAL   B 19  ? 1.1042 1.0747 1.0760 0.0769  -0.2180 -0.0571 19   VAL   B CA  
2780  C  C   . VAL   B 19  ? 1.1468 1.1004 1.1034 0.0860  -0.2268 -0.0617 19   VAL   B C   
2781  O  O   . VAL   B 19  ? 1.0803 1.0275 1.0404 0.0855  -0.2347 -0.0659 19   VAL   B O   
2782  C  CB  . VAL   B 19  ? 1.1425 1.1205 1.1270 0.0722  -0.2203 -0.0598 19   VAL   B CB  
2783  C  CG1 . VAL   B 19  ? 1.1700 1.1637 1.1672 0.0640  -0.2112 -0.0550 19   VAL   B CG1 
2784  C  CG2 . VAL   B 19  ? 1.1050 1.0804 1.1017 0.0689  -0.2303 -0.0660 19   VAL   B CG2 
2785  N  N   . THR   B 20  ? 1.2476 1.1936 1.1870 0.0946  -0.2252 -0.0608 20   THR   B N   
2786  C  CA  . THR   B 20  ? 1.2334 1.1619 1.1542 0.1050  -0.2322 -0.0644 20   THR   B CA  
2787  C  C   . THR   B 20  ? 1.2346 1.1580 1.1496 0.1096  -0.2371 -0.0680 20   THR   B C   
2788  O  O   . THR   B 20  ? 1.2230 1.1505 1.1336 0.1110  -0.2305 -0.0648 20   THR   B O   
2789  C  CB  . THR   B 20  ? 1.1810 1.1030 1.0836 0.1124  -0.2251 -0.0596 20   THR   B CB  
2790  O  OG1 . THR   B 20  ? 1.2588 1.1636 1.1412 0.1233  -0.2307 -0.0627 20   THR   B OG1 
2791  C  CG2 . THR   B 20  ? 1.2613 1.1935 1.1634 0.1112  -0.2132 -0.0532 20   THR   B CG2 
2792  N  N   . GLY   B 21  ? 1.2812 1.1954 1.1964 0.1121  -0.2489 -0.0748 21   GLY   B N   
2793  C  CA  . GLY   B 21  ? 1.3003 1.2101 1.2123 0.1159  -0.2550 -0.0790 21   GLY   B CA  
2794  C  C   . GLY   B 21  ? 1.3380 1.2328 1.2437 0.1218  -0.2689 -0.0866 21   GLY   B C   
2795  O  O   . GLY   B 21  ? 1.3108 1.1942 1.2062 0.1265  -0.2729 -0.0880 21   GLY   B O   
2796  N  N   . HIS   B 22  ? 1.3483 1.2430 1.2605 0.1217  -0.2768 -0.0918 22   HIS   B N   
2797  C  CA  . HIS   B 22  ? 1.3405 1.2205 1.2462 0.1282  -0.2909 -0.0995 22   HIS   B CA  
2798  C  C   . HIS   B 22  ? 1.3196 1.2078 1.2494 0.1204  -0.2994 -0.1050 22   HIS   B C   
2799  O  O   . HIS   B 22  ? 1.3056 1.1936 1.2387 0.1219  -0.3055 -0.1091 22   HIS   B O   
2800  C  CB  . HIS   B 22  ? 1.3373 1.2054 1.2224 0.1388  -0.2933 -0.1010 22   HIS   B CB  
2801  C  CG  . HIS   B 22  ? 1.3803 1.2402 1.2423 0.1467  -0.2843 -0.0954 22   HIS   B CG  
2802  N  ND1 . HIS   B 22  ? 1.4369 1.2818 1.2811 0.1545  -0.2869 -0.0959 22   HIS   B ND1 
2803  C  CD2 . HIS   B 22  ? 1.3352 1.2000 1.1898 0.1479  -0.2725 -0.0891 22   HIS   B CD2 
2804  C  CE1 . HIS   B 22  ? 1.4186 1.2595 1.2454 0.1603  -0.2767 -0.0901 22   HIS   B CE1 
2805  N  NE2 . HIS   B 22  ? 1.3342 1.1872 1.1673 0.1564  -0.2679 -0.0859 22   HIS   B NE2 
2806  N  N   . PHE   B 23  ? 1.2945 1.1893 1.2407 0.1124  -0.2998 -0.1051 23   PHE   B N   
2807  C  CA  . PHE   B 23  ? 1.2891 1.1942 1.2612 0.1032  -0.3050 -0.1089 23   PHE   B CA  
2808  C  C   . PHE   B 23  ? 1.2876 1.1816 1.2632 0.1057  -0.3199 -0.1171 23   PHE   B C   
2809  O  O   . PHE   B 23  ? 1.3112 1.2099 1.3035 0.1021  -0.3273 -0.1221 23   PHE   B O   
2810  C  CB  . PHE   B 23  ? 1.2565 1.1752 1.2453 0.0927  -0.2962 -0.1041 23   PHE   B CB  
2811  C  CG  . PHE   B 23  ? 1.2345 1.1660 1.2502 0.0825  -0.2980 -0.1064 23   PHE   B CG  
2812  C  CD1 . PHE   B 23  ? 1.2150 1.1554 1.2401 0.0803  -0.2974 -0.1072 23   PHE   B CD1 
2813  C  CD2 . PHE   B 23  ? 1.1973 1.1317 1.2289 0.0755  -0.3001 -0.1076 23   PHE   B CD2 
2814  C  CE1 . PHE   B 23  ? 1.2121 1.1642 1.2621 0.0713  -0.2987 -0.1092 23   PHE   B CE1 
2815  C  CE2 . PHE   B 23  ? 1.2088 1.1548 1.2654 0.0664  -0.3011 -0.1094 23   PHE   B CE2 
2816  C  CZ  . PHE   B 23  ? 1.2099 1.1649 1.2759 0.0643  -0.3003 -0.1102 23   PHE   B CZ  
2817  N  N   . THR   B 24  ? 1.3673 1.2468 1.3280 0.1119  -0.3246 -0.1185 24   THR   B N   
2818  C  CA  . THR   B 24  ? 1.4277 1.2955 1.3908 0.1144  -0.3390 -0.1262 24   THR   B CA  
2819  C  C   . THR   B 24  ? 1.4063 1.2588 1.3522 0.1256  -0.3500 -0.1321 24   THR   B C   
2820  O  O   . THR   B 24  ? 1.3729 1.2193 1.3264 0.1265  -0.3633 -0.1396 24   THR   B O   
2821  C  CB  . THR   B 24  ? 1.3679 1.2266 1.3229 0.1158  -0.3394 -0.1253 24   THR   B CB  
2822  O  OG1 . THR   B 24  ? 1.4058 1.2502 1.3319 0.1268  -0.3373 -0.1232 24   THR   B OG1 
2823  C  CG2 . THR   B 24  ? 1.2914 1.1640 1.2600 0.1058  -0.3278 -0.1189 24   THR   B CG2 
2824  N  N   . SER   B 25  ? 1.3934 1.2395 1.3169 0.1340  -0.3447 -0.1289 25   SER   B N   
2825  C  CA  . SER   B 25  ? 1.4004 1.2318 1.3058 0.1450  -0.3538 -0.1337 25   SER   B CA  
2826  C  C   . SER   B 25  ? 1.4171 1.2463 1.3014 0.1514  -0.3427 -0.1275 25   SER   B C   
2827  O  O   . SER   B 25  ? 1.4580 1.2941 1.3399 0.1484  -0.3300 -0.1203 25   SER   B O   
2828  C  CB  . SER   B 25  ? 1.4307 1.2415 1.3198 0.1539  -0.3659 -0.1394 25   SER   B CB  
2829  O  OG  . SER   B 25  ? 1.5114 1.3089 1.3716 0.1639  -0.3604 -0.1356 25   SER   B OG  
2830  N  N   . ALA   B 26  ? 1.3727 1.1922 1.2421 0.1601  -0.3474 -0.1303 26   ALA   B N   
2831  C  CA  . ALA   B 26  ? 1.3991 1.2169 1.2497 0.1656  -0.3361 -0.1241 26   ALA   B CA  
2832  C  C   . ALA   B 26  ? 1.4901 1.2941 1.3159 0.1741  -0.3313 -0.1205 26   ALA   B C   
2833  O  O   . ALA   B 26  ? 1.5130 1.3196 1.3281 0.1759  -0.3186 -0.1136 26   ALA   B O   
2834  C  CB  . ALA   B 26  ? 1.4760 1.2862 1.3160 0.1731  -0.3419 -0.1277 26   ALA   B CB  
2835  N  N   . GLU   B 27  ? 1.6367 1.4266 1.4543 0.1788  -0.3409 -0.1250 27   GLU   B N   
2836  C  CA  . GLU   B 27  ? 1.6920 1.4659 1.4839 0.1884  -0.3381 -0.1226 27   GLU   B CA  
2837  C  C   . GLU   B 27  ? 1.7259 1.5064 1.5248 0.1824  -0.3307 -0.1180 27   GLU   B C   
2838  O  O   . GLU   B 27  ? 1.8058 1.5744 1.5846 0.1898  -0.3272 -0.1154 27   GLU   B O   
2839  C  CB  . GLU   B 27  ? 1.6902 1.4419 1.4654 0.1988  -0.3537 -0.1305 27   GLU   B CB  
2840  N  N   . ASP   B 28  ? 1.6220 1.4204 1.4479 0.1697  -0.3282 -0.1169 28   ASP   B N   
2841  C  CA  . ASP   B 28  ? 1.5542 1.3596 1.3883 0.1633  -0.3216 -0.1128 28   ASP   B CA  
2842  C  C   . ASP   B 28  ? 1.5097 1.3321 1.3511 0.1569  -0.3057 -0.1043 28   ASP   B C   
2843  O  O   . ASP   B 28  ? 1.4770 1.3123 1.3306 0.1515  -0.3015 -0.1028 28   ASP   B O   
2844  C  CB  . ASP   B 28  ? 1.4502 1.2630 1.3092 0.1535  -0.3295 -0.1172 28   ASP   B CB  
2845  C  CG  . ASP   B 28  ? 1.5224 1.3211 1.3794 0.1583  -0.3462 -0.1263 28   ASP   B CG  
2846  O  OD1 . ASP   B 28  ? 1.6339 1.4152 1.4675 0.1700  -0.3520 -0.1291 28   ASP   B OD1 
2847  O  OD2 . ASP   B 28  ? 1.5149 1.3196 1.3938 0.1505  -0.3536 -0.1307 28   ASP   B OD2 
2848  N  N   . LEU   B 29  ? 1.4787 1.3007 1.3124 0.1577  -0.2971 -0.0989 29   LEU   B N   
2849  C  CA  . LEU   B 29  ? 1.4278 1.2665 1.2716 0.1504  -0.2831 -0.0912 29   LEU   B CA  
2850  C  C   . LEU   B 29  ? 1.4144 1.2646 1.2809 0.1392  -0.2838 -0.0915 29   LEU   B C   
2851  O  O   . LEU   B 29  ? 1.4486 1.2919 1.3123 0.1400  -0.2868 -0.0923 29   LEU   B O   
2852  C  CB  . LEU   B 29  ? 1.3826 1.2150 1.2068 0.1574  -0.2735 -0.0853 29   LEU   B CB  
2853  C  CG  . LEU   B 29  ? 1.4116 1.2610 1.2443 0.1512  -0.2589 -0.0774 29   LEU   B CG  
2854  C  CD1 . LEU   B 29  ? 1.3597 1.2219 1.2056 0.1454  -0.2565 -0.0771 29   LEU   B CD1 
2855  C  CD2 . LEU   B 29  ? 1.3960 1.2389 1.2083 0.1596  -0.2490 -0.0717 29   LEU   B CD2 
2856  N  N   . ASN   B 30  ? 1.3685 1.2354 1.2569 0.1291  -0.2811 -0.0907 30   ASN   B N   
2857  C  CA  . ASN   B 30  ? 1.3321 1.2102 1.2422 0.1183  -0.2804 -0.0903 30   ASN   B CA  
2858  C  C   . ASN   B 30  ? 1.3216 1.2143 1.2381 0.1122  -0.2667 -0.0825 30   ASN   B C   
2859  O  O   . ASN   B 30  ? 1.2921 1.1904 1.2032 0.1136  -0.2582 -0.0781 30   ASN   B O   
2860  C  CB  . ASN   B 30  ? 1.2889 1.1760 1.2209 0.1106  -0.2867 -0.0948 30   ASN   B CB  
2861  C  CG  . ASN   B 30  ? 1.3495 1.2248 1.2759 0.1169  -0.2993 -0.1022 30   ASN   B CG  
2862  O  OD1 . ASN   B 30  ? 1.4402 1.3174 1.3652 0.1191  -0.2999 -0.1032 30   ASN   B OD1 
2863  N  ND2 . ASN   B 30  ? 1.3712 1.2337 1.2939 0.1203  -0.3099 -0.1075 30   ASN   B ND2 
2864  N  N   . LEU   B 31  ? 1.2877 1.1856 1.2158 0.1054  -0.2651 -0.0812 31   LEU   B N   
2865  C  CA  . LEU   B 31  ? 1.2079 1.1207 1.1467 0.0977  -0.2539 -0.0748 31   LEU   B CA  
2866  C  C   . LEU   B 31  ? 1.1999 1.1235 1.1629 0.0868  -0.2562 -0.0768 31   LEU   B C   
2867  O  O   . LEU   B 31  ? 1.2072 1.1262 1.1768 0.0842  -0.2623 -0.0800 31   LEU   B O   
2868  C  CB  . LEU   B 31  ? 1.1788 1.0870 1.1081 0.1001  -0.2494 -0.0711 31   LEU   B CB  
2869  C  CG  . LEU   B 31  ? 1.2056 1.1283 1.1442 0.0932  -0.2381 -0.0644 31   LEU   B CG  
2870  C  CD1 . LEU   B 31  ? 1.1667 1.0970 1.1009 0.0947  -0.2295 -0.0600 31   LEU   B CD1 
2871  C  CD2 . LEU   B 31  ? 1.2719 1.1889 1.2013 0.0960  -0.2351 -0.0615 31   LEU   B CD2 
2872  N  N   . LEU   B 32  ? 1.1878 1.1250 1.1638 0.0805  -0.2514 -0.0750 32   LEU   B N   
2873  C  CA  . LEU   B 32  ? 1.1074 1.0560 1.1060 0.0698  -0.2509 -0.0755 32   LEU   B CA  
2874  C  C   . LEU   B 32  ? 1.0995 1.0581 1.1023 0.0644  -0.2401 -0.0689 32   LEU   B C   
2875  O  O   . LEU   B 32  ? 1.1083 1.0714 1.1030 0.0664  -0.2318 -0.0639 32   LEU   B O   
2876  C  CB  . LEU   B 32  ? 1.1074 1.0652 1.1186 0.0659  -0.2517 -0.0774 32   LEU   B CB  
2877  C  CG  . LEU   B 32  ? 1.1533 1.1023 1.1657 0.0695  -0.2639 -0.0849 32   LEU   B CG  
2878  C  CD1 . LEU   B 32  ? 1.1495 1.0853 1.1390 0.0810  -0.2675 -0.0862 32   LEU   B CD1 
2879  C  CD2 . LEU   B 32  ? 1.1156 1.0752 1.1454 0.0638  -0.2651 -0.0870 32   LEU   B CD2 
2880  N  N   . ILE   B 33  ? 1.0589 1.0200 1.0740 0.0578  -0.2404 -0.0689 33   ILE   B N   
2881  C  CA  . ILE   B 33  ? 0.9773 0.9468 0.9968 0.0524  -0.2312 -0.0632 33   ILE   B CA  
2882  C  C   . ILE   B 33  ? 1.0373 1.0176 1.0784 0.0420  -0.2297 -0.0633 33   ILE   B C   
2883  O  O   . ILE   B 33  ? 1.0224 1.0002 1.0749 0.0389  -0.2368 -0.0681 33   ILE   B O   
2884  C  CB  . ILE   B 33  ? 1.0670 1.0274 1.0777 0.0552  -0.2321 -0.0622 33   ILE   B CB  
2885  C  CG1 . ILE   B 33  ? 1.0956 1.0511 1.0866 0.0635  -0.2274 -0.0585 33   ILE   B CG1 
2886  C  CG2 . ILE   B 33  ? 1.0748 1.0427 1.0978 0.0469  -0.2267 -0.0590 33   ILE   B CG2 
2887  C  CD1 . ILE   B 33  ? 1.1484 1.0930 1.1287 0.0677  -0.2292 -0.0582 33   ILE   B CD1 
2888  N  N   . ALA   B 34  ? 1.0756 1.0676 1.1222 0.0368  -0.2202 -0.0580 34   ALA   B N   
2889  C  CA  . ALA   B 34  ? 1.0583 1.0610 1.1238 0.0273  -0.2169 -0.0573 34   ALA   B CA  
2890  C  C   . ALA   B 34  ? 1.0625 1.0679 1.1310 0.0227  -0.2109 -0.0530 34   ALA   B C   
2891  O  O   . ALA   B 34  ? 1.1077 1.1157 1.1672 0.0244  -0.2043 -0.0481 34   ALA   B O   
2892  C  CB  . ALA   B 34  ? 0.9451 0.9590 1.0147 0.0250  -0.2113 -0.0550 34   ALA   B CB  
2893  N  N   . LYS   B 35  ? 1.0213 1.0261 1.1028 0.0167  -0.2131 -0.0549 35   LYS   B N   
2894  C  CA  . LYS   B 35  ? 1.0482 1.0556 1.1340 0.0115  -0.2073 -0.0510 35   LYS   B CA  
2895  C  C   . LYS   B 35  ? 1.0672 1.0835 1.1722 0.0026  -0.2045 -0.0511 35   LYS   B C   
2896  O  O   . LYS   B 35  ? 1.0267 1.0398 1.1435 -0.0013 -0.2089 -0.0545 35   LYS   B O   
2897  C  CB  . LYS   B 35  ? 1.0385 1.0342 1.1193 0.0138  -0.2121 -0.0527 35   LYS   B CB  
2898  C  CG  . LYS   B 35  ? 1.0640 1.0503 1.1252 0.0232  -0.2148 -0.0527 35   LYS   B CG  
2899  C  CD  . LYS   B 35  ? 0.9995 0.9733 1.0553 0.0257  -0.2203 -0.0549 35   LYS   B CD  
2900  C  CE  . LYS   B 35  ? 1.0985 1.0611 1.1364 0.0357  -0.2258 -0.0571 35   LYS   B CE  
2901  N  NZ  . LYS   B 35  ? 1.0105 0.9603 1.0380 0.0401  -0.2296 -0.0580 35   LYS   B NZ  
2902  N  N   . ASN   B 36  ? 1.0057 1.0327 1.1137 -0.0004 -0.1973 -0.0474 36   ASN   B N   
2903  C  CA  . ASN   B 36  ? 1.0117 1.0476 1.1360 -0.0084 -0.1931 -0.0467 36   ASN   B CA  
2904  C  C   . ASN   B 36  ? 0.9815 1.0171 1.1195 -0.0106 -0.1997 -0.0522 36   ASN   B C   
2905  O  O   . ASN   B 36  ? 0.9582 0.9981 1.0985 -0.0094 -0.2013 -0.0541 36   ASN   B O   
2906  C  CB  . ASN   B 36  ? 1.0594 1.0946 1.1887 -0.0137 -0.1885 -0.0437 36   ASN   B CB  
2907  C  CG  . ASN   B 36  ? 1.0397 1.0850 1.1791 -0.0206 -0.1804 -0.0402 36   ASN   B CG  
2908  O  OD1 . ASN   B 36  ? 1.1176 1.1708 1.2566 -0.0207 -0.1769 -0.0386 36   ASN   B OD1 
2909  N  ND2 . ASN   B 36  ? 0.9592 1.0035 1.1069 -0.0261 -0.1772 -0.0388 36   ASN   B ND2 
2910  N  N   . THR   B 37  ? 1.0136 1.0439 1.1611 -0.0138 -0.2036 -0.0549 37   THR   B N   
2911  C  CA  . THR   B 37  ? 0.9693 1.0001 1.1329 -0.0168 -0.2096 -0.0602 37   THR   B CA  
2912  C  C   . THR   B 37  ? 1.0186 1.0387 1.1779 -0.0114 -0.2205 -0.0659 37   THR   B C   
2913  O  O   . THR   B 37  ? 1.0829 1.1011 1.2562 -0.0141 -0.2267 -0.0707 37   THR   B O   
2914  C  CB  . THR   B 37  ? 1.0427 1.0752 1.2228 -0.0248 -0.2065 -0.0596 37   THR   B CB  
2915  O  OG1 . THR   B 37  ? 1.0470 1.0701 1.2216 -0.0242 -0.2079 -0.0591 37   THR   B OG1 
2916  C  CG2 . THR   B 37  ? 1.0736 1.1157 1.2574 -0.0300 -0.1958 -0.0542 37   THR   B CG2 
2917  N  N   . ARG   B 38  ? 1.0418 1.0543 1.1823 -0.0037 -0.2231 -0.0656 38   ARG   B N   
2918  C  CA  . ARG   B 38  ? 1.0800 1.0805 1.2143 0.0019  -0.2335 -0.0709 38   ARG   B CA  
2919  C  C   . ARG   B 38  ? 1.0963 1.0926 1.2131 0.0109  -0.2366 -0.0718 38   ARG   B C   
2920  O  O   . ARG   B 38  ? 1.0633 1.0613 1.1664 0.0143  -0.2305 -0.0672 38   ARG   B O   
2921  C  CB  . ARG   B 38  ? 1.0817 1.0730 1.2100 0.0024  -0.2340 -0.0698 38   ARG   B CB  
2922  C  CG  . ARG   B 38  ? 1.0894 1.0836 1.2335 -0.0063 -0.2299 -0.0683 38   ARG   B CG  
2923  C  CD  . ARG   B 38  ? 1.0978 1.0919 1.2620 -0.0112 -0.2363 -0.0737 38   ARG   B CD  
2924  N  NE  . ARG   B 38  ? 1.1337 1.1158 1.2954 -0.0070 -0.2476 -0.0796 38   ARG   B NE  
2925  C  CZ  . ARG   B 38  ? 1.1827 1.1629 1.3613 -0.0105 -0.2547 -0.0850 38   ARG   B CZ  
2926  N  NH1 . ARG   B 38  ? 1.1806 1.1700 1.3802 -0.0186 -0.2510 -0.0848 38   ARG   B NH1 
2927  N  NH2 . ARG   B 38  ? 1.2046 1.1731 1.3792 -0.0059 -0.2658 -0.0906 38   ARG   B NH2 
2928  N  N   . LEU   B 39  ? 1.1315 1.1223 1.2491 0.0147  -0.2462 -0.0777 39   LEU   B N   
2929  C  CA  . LEU   B 39  ? 1.1022 1.0865 1.2022 0.0239  -0.2503 -0.0793 39   LEU   B CA  
2930  C  C   . LEU   B 39  ? 1.1570 1.1261 1.2450 0.0304  -0.2588 -0.0829 39   LEU   B C   
2931  O  O   . LEU   B 39  ? 1.1590 1.1227 1.2569 0.0280  -0.2660 -0.0872 39   LEU   B O   
2932  C  CB  . LEU   B 39  ? 1.1476 1.1354 1.2548 0.0247  -0.2553 -0.0835 39   LEU   B CB  
2933  C  CG  . LEU   B 39  ? 1.2048 1.1859 1.2947 0.0341  -0.2598 -0.0855 39   LEU   B CG  
2934  C  CD1 . LEU   B 39  ? 1.1669 1.1522 1.2425 0.0371  -0.2501 -0.0793 39   LEU   B CD1 
2935  C  CD2 . LEU   B 39  ? 1.1370 1.1212 1.2368 0.0341  -0.2659 -0.0904 39   LEU   B CD2 
2936  N  N   . GLU   B 40  ? 1.1003 1.0623 1.1672 0.0386  -0.2577 -0.0809 40   GLU   B N   
2937  C  CA  . GLU   B 40  ? 1.1317 1.0783 1.1841 0.0459  -0.2652 -0.0839 40   GLU   B CA  
2938  C  C   . GLU   B 40  ? 1.1500 1.0890 1.1850 0.0557  -0.2696 -0.0861 40   GLU   B C   
2939  O  O   . GLU   B 40  ? 1.1661 1.1104 1.1929 0.0582  -0.2628 -0.0823 40   GLU   B O   
2940  C  CB  . GLU   B 40  ? 1.1252 1.0686 1.1670 0.0470  -0.2590 -0.0790 40   GLU   B CB  
2941  C  CG  . GLU   B 40  ? 1.1175 1.0613 1.1722 0.0398  -0.2587 -0.0788 40   GLU   B CG  
2942  C  CD  . GLU   B 40  ? 1.2181 1.1610 1.2628 0.0404  -0.2510 -0.0731 40   GLU   B CD  
2943  O  OE1 . GLU   B 40  ? 1.2016 1.1409 1.2283 0.0478  -0.2481 -0.0704 40   GLU   B OE1 
2944  O  OE2 . GLU   B 40  ? 1.2173 1.1631 1.2723 0.0338  -0.2477 -0.0712 40   GLU   B OE2 
2945  N  N   . ILE   B 41  ? 1.1878 1.1137 1.2171 0.0613  -0.2809 -0.0923 41   ILE   B N   
2946  C  CA  . ILE   B 41  ? 1.1926 1.1093 1.2054 0.0709  -0.2865 -0.0953 41   ILE   B CA  
2947  C  C   . ILE   B 41  ? 1.1846 1.0840 1.1783 0.0797  -0.2927 -0.0975 41   ILE   B C   
2948  O  O   . ILE   B 41  ? 1.2105 1.1014 1.2090 0.0792  -0.3020 -0.1025 41   ILE   B O   
2949  C  CB  . ILE   B 41  ? 1.1389 1.0563 1.1636 0.0700  -0.2959 -0.1017 41   ILE   B CB  
2950  C  CG1 . ILE   B 41  ? 1.1835 1.1179 1.2263 0.0619  -0.2893 -0.0994 41   ILE   B CG1 
2951  C  CG2 . ILE   B 41  ? 1.1815 1.0878 1.1874 0.0806  -0.3020 -0.1048 41   ILE   B CG2 
2952  C  CD1 . ILE   B 41  ? 1.1830 1.1218 1.2482 0.0560  -0.2971 -0.1052 41   ILE   B CD1 
2953  N  N   . TYR   B 42  ? 1.1681 1.0619 1.1405 0.0876  -0.2876 -0.0937 42   TYR   B N   
2954  C  CA  . TYR   B 42  ? 1.2626 1.1393 1.2136 0.0974  -0.2923 -0.0952 42   TYR   B CA  
2955  C  C   . TYR   B 42  ? 1.3284 1.1943 1.2612 0.1078  -0.2973 -0.0981 42   TYR   B C   
2956  O  O   . TYR   B 42  ? 1.2979 1.1702 1.2328 0.1079  -0.2955 -0.0979 42   TYR   B O   
2957  C  CB  . TYR   B 42  ? 1.2309 1.1083 1.1704 0.0992  -0.2819 -0.0884 42   TYR   B CB  
2958  C  CG  . TYR   B 42  ? 1.2529 1.1378 1.2069 0.0904  -0.2778 -0.0858 42   TYR   B CG  
2959  C  CD1 . TYR   B 42  ? 1.2522 1.1540 1.2221 0.0813  -0.2688 -0.0813 42   TYR   B CD1 
2960  C  CD2 . TYR   B 42  ? 1.2528 1.1273 1.2045 0.0911  -0.2832 -0.0881 42   TYR   B CD2 
2961  C  CE1 . TYR   B 42  ? 1.2321 1.1399 1.2146 0.0734  -0.2650 -0.0789 42   TYR   B CE1 
2962  C  CE2 . TYR   B 42  ? 1.2497 1.1304 1.2143 0.0831  -0.2794 -0.0857 42   TYR   B CE2 
2963  C  CZ  . TYR   B 42  ? 1.1935 1.0907 1.1732 0.0744  -0.2702 -0.0811 42   TYR   B CZ  
2964  O  OH  . TYR   B 42  ? 1.1880 1.0901 1.1793 0.0669  -0.2663 -0.0786 42   TYR   B OH  
2965  N  N   . VAL   B 43  ? 1.3746 1.2230 1.2882 0.1172  -0.3037 -0.1008 43   VAL   B N   
2966  C  CA  . VAL   B 43  ? 1.3925 1.2285 1.2829 0.1288  -0.3058 -0.1018 43   VAL   B CA  
2967  C  C   . VAL   B 43  ? 1.4087 1.2378 1.2787 0.1358  -0.2978 -0.0965 43   VAL   B C   
2968  O  O   . VAL   B 43  ? 1.4331 1.2573 1.3008 0.1355  -0.2981 -0.0958 43   VAL   B O   
2969  C  CB  . VAL   B 43  ? 1.3231 1.1424 1.2057 0.1356  -0.3211 -0.1103 43   VAL   B CB  
2970  C  CG1 . VAL   B 43  ? 1.3104 1.1164 1.1671 0.1481  -0.3219 -0.1106 43   VAL   B CG1 
2971  C  CG2 . VAL   B 43  ? 1.3619 1.1891 1.2664 0.1287  -0.3289 -0.1156 43   VAL   B CG2 
2972  N  N   . VAL   B 44  ? 1.4059 1.2348 1.2615 0.1419  -0.2904 -0.0925 44   VAL   B N   
2973  C  CA  . VAL   B 44  ? 1.4648 1.2890 1.3024 0.1484  -0.2813 -0.0868 44   VAL   B CA  
2974  C  C   . VAL   B 44  ? 1.5481 1.3503 1.3606 0.1612  -0.2887 -0.0905 44   VAL   B C   
2975  O  O   . VAL   B 44  ? 1.5619 1.3555 1.3595 0.1693  -0.2903 -0.0918 44   VAL   B O   
2976  C  CB  . VAL   B 44  ? 1.4690 1.3035 1.3039 0.1487  -0.2692 -0.0806 44   VAL   B CB  
2977  C  CG1 . VAL   B 44  ? 1.5358 1.3606 1.3479 0.1587  -0.2621 -0.0762 44   VAL   B CG1 
2978  C  CG2 . VAL   B 44  ? 1.4391 1.2938 1.2953 0.1371  -0.2604 -0.0758 44   VAL   B CG2 
2979  N  N   . THR   B 45  ? 1.6396 1.4317 1.4463 0.1634  -0.2930 -0.0920 45   THR   B N   
2980  C  CA  . THR   B 45  ? 1.6846 1.4551 1.4657 0.1760  -0.2989 -0.0948 45   THR   B CA  
2981  C  C   . THR   B 45  ? 1.7740 1.5416 1.5373 0.1829  -0.2869 -0.0878 45   THR   B C   
2982  O  O   . THR   B 45  ? 1.7862 1.5684 1.5589 0.1771  -0.2755 -0.0814 45   THR   B O   
2983  C  CB  . THR   B 45  ? 1.6898 1.4497 1.4728 0.1754  -0.3098 -0.1001 45   THR   B CB  
2984  O  OG1 . THR   B 45  ? 1.7170 1.4810 1.5023 0.1722  -0.3026 -0.0954 45   THR   B OG1 
2985  C  CG2 . THR   B 45  ? 1.4930 1.2610 1.3005 0.1654  -0.3187 -0.1055 45   THR   B CG2 
2986  N  N   . ALA   B 46  ? 1.8124 1.5609 1.5497 0.1957  -0.2896 -0.0892 46   ALA   B N   
2987  C  CA  . ALA   B 46  ? 1.8081 1.5521 1.5279 0.2031  -0.2787 -0.0830 46   ALA   B CA  
2988  C  C   . ALA   B 46  ? 1.7866 1.5299 1.5084 0.2011  -0.2773 -0.0812 46   ALA   B C   
2989  O  O   . ALA   B 46  ? 1.7233 1.4667 1.4352 0.2052  -0.2671 -0.0754 46   ALA   B O   
2990  C  CB  . ALA   B 46  ? 1.7616 1.4839 1.4519 0.2178  -0.2819 -0.0849 46   ALA   B CB  
2991  N  N   . GLU   B 47  ? 1.8535 1.5961 1.5880 0.1949  -0.2870 -0.0861 47   GLU   B N   
2992  C  CA  . GLU   B 47  ? 1.9099 1.6534 1.6487 0.1915  -0.2852 -0.0843 47   GLU   B CA  
2993  C  C   . GLU   B 47  ? 1.9242 1.6898 1.6883 0.1784  -0.2775 -0.0799 47   GLU   B C   
2994  O  O   . GLU   B 47  ? 1.9531 1.7238 1.7185 0.1767  -0.2698 -0.0750 47   GLU   B O   
2995  C  CB  . GLU   B 47  ? 1.9033 1.6325 1.6413 0.1922  -0.2995 -0.0916 47   GLU   B CB  
2996  N  N   . GLY   B 48  ? 2.1345 1.9130 1.9183 0.1694  -0.2794 -0.0816 48   GLY   B N   
2997  C  CA  . GLY   B 48  ? 2.1089 1.9079 1.9158 0.1573  -0.2720 -0.0775 48   GLY   B CA  
2998  C  C   . GLY   B 48  ? 2.0619 1.8732 1.8899 0.1479  -0.2754 -0.0803 48   GLY   B C   
2999  O  O   . GLY   B 48  ? 2.0479 1.8616 1.8740 0.1499  -0.2749 -0.0808 48   GLY   B O   
3000  N  N   . LEU   B 49  ? 1.6872 1.5063 1.5354 0.1379  -0.2785 -0.0819 49   LEU   B N   
3001  C  CA  . LEU   B 49  ? 1.5264 1.3571 1.3962 0.1286  -0.2817 -0.0846 49   LEU   B CA  
3002  C  C   . LEU   B 49  ? 1.4645 1.2868 1.3428 0.1261  -0.2948 -0.0920 49   LEU   B C   
3003  O  O   . LEU   B 49  ? 1.4830 1.3023 1.3661 0.1228  -0.2968 -0.0925 49   LEU   B O   
3004  C  CB  . LEU   B 49  ? 1.4722 1.3218 1.3612 0.1177  -0.2720 -0.0793 49   LEU   B CB  
3005  C  CG  . LEU   B 49  ? 1.3758 1.2403 1.2706 0.1146  -0.2628 -0.0748 49   LEU   B CG  
3006  C  CD1 . LEU   B 49  ? 1.4837 1.3469 1.3614 0.1218  -0.2533 -0.0690 49   LEU   B CD1 
3007  C  CD2 . LEU   B 49  ? 1.2591 1.1401 1.1761 0.1026  -0.2573 -0.0720 49   LEU   B CD2 
3008  N  N   . ARG   B 50  ? 1.4015 1.2205 1.2827 0.1273  -0.3037 -0.0977 50   ARG   B N   
3009  C  CA  . ARG   B 50  ? 1.3669 1.1801 1.2601 0.1239  -0.3165 -0.1050 50   ARG   B CA  
3010  C  C   . ARG   B 50  ? 1.3360 1.1662 1.2569 0.1119  -0.3153 -0.1054 50   ARG   B C   
3011  O  O   . ARG   B 50  ? 1.2962 1.1356 1.2227 0.1105  -0.3129 -0.1049 50   ARG   B O   
3012  C  CB  . ARG   B 50  ? 1.3605 1.1584 1.2402 0.1332  -0.3284 -0.1118 50   ARG   B CB  
3013  C  CG  . ARG   B 50  ? 1.3132 1.1031 1.2039 0.1308  -0.3430 -0.1199 50   ARG   B CG  
3014  C  CD  . ARG   B 50  ? 1.3233 1.1081 1.2137 0.1349  -0.3536 -0.1265 50   ARG   B CD  
3015  N  NE  . ARG   B 50  ? 1.3816 1.1540 1.2449 0.1474  -0.3538 -0.1263 50   ARG   B NE  
3016  C  CZ  . ARG   B 50  ? 1.4874 1.2597 1.3465 0.1515  -0.3564 -0.1283 50   ARG   B CZ  
3017  N  NH1 . ARG   B 50  ? 1.4070 1.1915 1.2872 0.1442  -0.3591 -0.1308 50   ARG   B NH1 
3018  N  NH2 . ARG   B 50  ? 1.5230 1.2823 1.3556 0.1635  -0.3558 -0.1277 50   ARG   B NH2 
3019  N  N   . PRO   B 51  ? 1.2875 1.1221 1.2258 0.1032  -0.3164 -0.1060 51   PRO   B N   
3020  C  CA  . PRO   B 51  ? 1.2316 1.0814 1.1966 0.0919  -0.3153 -0.1066 51   PRO   B CA  
3021  C  C   . PRO   B 51  ? 1.2584 1.1053 1.2320 0.0923  -0.3269 -0.1139 51   PRO   B C   
3022  O  O   . PRO   B 51  ? 1.3601 1.1917 1.3237 0.0991  -0.3384 -0.1199 51   PRO   B O   
3023  C  CB  . PRO   B 51  ? 1.2148 1.0647 1.1923 0.0846  -0.3156 -0.1064 51   PRO   B CB  
3024  C  CG  . PRO   B 51  ? 1.2701 1.1093 1.2275 0.0912  -0.3126 -0.1034 51   PRO   B CG  
3025  C  CD  . PRO   B 51  ? 1.2828 1.1081 1.2169 0.1035  -0.3182 -0.1061 51   PRO   B CD  
3026  N  N   . VAL   B 52  ? 1.2184 1.0799 1.2106 0.0851  -0.3241 -0.1136 52   VAL   B N   
3027  C  CA  . VAL   B 52  ? 1.2820 1.1425 1.2838 0.0853  -0.3346 -0.1204 52   VAL   B CA  
3028  C  C   . VAL   B 52  ? 1.2968 1.1707 1.3286 0.0735  -0.3347 -0.1218 52   VAL   B C   
3029  O  O   . VAL   B 52  ? 1.3293 1.1989 1.3740 0.0714  -0.3456 -0.1284 52   VAL   B O   
3030  C  CB  . VAL   B 52  ? 1.2620 1.1248 1.2531 0.0912  -0.3325 -0.1196 52   VAL   B CB  
3031  C  CG1 . VAL   B 52  ? 1.2019 1.0626 1.2023 0.0921  -0.3443 -0.1270 52   VAL   B CG1 
3032  C  CG2 . VAL   B 52  ? 1.2759 1.1253 1.2372 0.1030  -0.3311 -0.1177 52   VAL   B CG2 
3033  N  N   . LYS   B 53  ? 1.2616 1.1514 1.3046 0.0659  -0.3227 -0.1158 53   LYS   B N   
3034  C  CA  . LYS   B 53  ? 1.2257 1.1287 1.2964 0.0548  -0.3210 -0.1163 53   LYS   B CA  
3035  C  C   . LYS   B 53  ? 1.2713 1.1893 1.3478 0.0482  -0.3064 -0.1085 53   LYS   B C   
3036  O  O   . LYS   B 53  ? 1.2076 1.1302 1.2724 0.0516  -0.2992 -0.1042 53   LYS   B O   
3037  C  CB  . LYS   B 53  ? 1.2203 1.1275 1.3034 0.0544  -0.3284 -0.1217 53   LYS   B CB  
3038  C  CG  . LYS   B 53  ? 1.2136 1.1341 1.3262 0.0431  -0.3266 -0.1224 53   LYS   B CG  
3039  C  CD  . LYS   B 53  ? 1.3008 1.2246 1.4258 0.0433  -0.3349 -0.1283 53   LYS   B CD  
3040  C  CE  . LYS   B 53  ? 1.3214 1.2536 1.4765 0.0333  -0.3371 -0.1311 53   LYS   B CE  
3041  N  NZ  . LYS   B 53  ? 1.3313 1.2565 1.4914 0.0298  -0.3393 -0.1319 53   LYS   B NZ  
3042  N  N   . GLU   B 54  ? 1.2898 1.2149 1.3848 0.0387  -0.3023 -0.1068 54   GLU   B N   
3043  C  CA  . GLU   B 54  ? 1.2568 1.1946 1.3576 0.0320  -0.2890 -0.0996 54   GLU   B CA  
3044  C  C   . GLU   B 54  ? 1.2507 1.2005 1.3780 0.0220  -0.2872 -0.1004 54   GLU   B C   
3045  O  O   . GLU   B 54  ? 1.2762 1.2240 1.4184 0.0166  -0.2909 -0.1030 54   GLU   B O   
3046  C  CB  . GLU   B 54  ? 1.2671 1.1997 1.3605 0.0313  -0.2843 -0.0957 54   GLU   B CB  
3047  C  CG  . GLU   B 54  ? 1.2761 1.2206 1.3746 0.0247  -0.2712 -0.0884 54   GLU   B CG  
3048  C  CD  . GLU   B 54  ? 1.2738 1.2253 1.3955 0.0142  -0.2686 -0.0882 54   GLU   B CD  
3049  O  OE1 . GLU   B 54  ? 1.2623 1.2094 1.3973 0.0115  -0.2768 -0.0936 54   GLU   B OE1 
3050  O  OE2 . GLU   B 54  ? 1.2163 1.1774 1.3427 0.0087  -0.2581 -0.0825 54   GLU   B OE2 
3051  N  N   . VAL   B 55  ? 1.2924 1.2541 1.4254 0.0196  -0.2814 -0.0982 55   VAL   B N   
3052  C  CA  . VAL   B 55  ? 1.3503 1.3226 1.5075 0.0118  -0.2811 -0.1000 55   VAL   B CA  
3053  C  C   . VAL   B 55  ? 1.3430 1.3276 1.5091 0.0039  -0.2682 -0.0934 55   VAL   B C   
3054  O  O   . VAL   B 55  ? 1.3252 1.3118 1.4779 0.0053  -0.2598 -0.0876 55   VAL   B O   
3055  C  CB  . VAL   B 55  ? 1.3749 1.3509 1.5330 0.0153  -0.2856 -0.1034 55   VAL   B CB  
3056  C  CG1 . VAL   B 55  ? 1.3581 1.3365 1.4971 0.0208  -0.2788 -0.0987 55   VAL   B CG1 
3057  C  CG2 . VAL   B 55  ? 1.3562 1.3449 1.5389 0.0072  -0.2834 -0.1043 55   VAL   B CG2 
3058  N  N   . GLY   B 56  ? 1.2482 1.2408 1.4373 -0.0044 -0.2667 -0.0944 56   GLY   B N   
3059  C  CA  . GLY   B 56  ? 1.1557 1.1599 1.3545 -0.0119 -0.2549 -0.0886 56   GLY   B CA  
3060  C  C   . GLY   B 56  ? 1.1343 1.1507 1.3457 -0.0153 -0.2515 -0.0886 56   GLY   B C   
3061  O  O   . GLY   B 56  ? 1.1125 1.1312 1.3397 -0.0171 -0.2578 -0.0936 56   GLY   B O   
3062  N  N   . MET   B 57  ? 1.1198 1.1443 1.3249 -0.0163 -0.2416 -0.0828 57   MET   B N   
3063  C  CA  . MET   B 57  ? 1.0227 1.0590 1.2379 -0.0196 -0.2369 -0.0819 57   MET   B CA  
3064  C  C   . MET   B 57  ? 1.0105 1.0552 1.2394 -0.0282 -0.2268 -0.0774 57   MET   B C   
3065  O  O   . MET   B 57  ? 1.0376 1.0807 1.2605 -0.0301 -0.2204 -0.0729 57   MET   B O   
3066  C  CB  . MET   B 57  ? 0.9829 1.0220 1.1810 -0.0143 -0.2330 -0.0788 57   MET   B CB  
3067  C  CG  . MET   B 57  ? 1.0227 1.0547 1.2082 -0.0057 -0.2420 -0.0830 57   MET   B CG  
3068  S  SD  . MET   B 57  ? 1.1831 1.2240 1.3631 -0.0035 -0.2371 -0.0809 57   MET   B SD  
3069  C  CE  . MET   B 57  ? 1.1152 1.1452 1.2700 0.0078  -0.2428 -0.0823 57   MET   B CE  
3070  N  N   . TYR   B 58  ? 1.0442 1.0976 1.2910 -0.0330 -0.2252 -0.0787 58   TYR   B N   
3071  C  CA  . TYR   B 58  ? 0.9600 1.0219 1.2185 -0.0406 -0.2148 -0.0742 58   TYR   B CA  
3072  C  C   . TYR   B 58  ? 0.9323 1.0011 1.1797 -0.0399 -0.2060 -0.0689 58   TYR   B C   
3073  O  O   . TYR   B 58  ? 0.9246 1.0024 1.1819 -0.0436 -0.2009 -0.0677 58   TYR   B O   
3074  C  CB  . TYR   B 58  ? 0.9699 1.0385 1.2521 -0.0458 -0.2160 -0.0776 58   TYR   B CB  
3075  C  CG  . TYR   B 58  ? 1.0292 1.0925 1.3269 -0.0488 -0.2223 -0.0820 58   TYR   B CG  
3076  C  CD1 . TYR   B 58  ? 1.0250 1.0777 1.3144 -0.0470 -0.2264 -0.0825 58   TYR   B CD1 
3077  C  CD2 . TYR   B 58  ? 1.0504 1.1193 1.3718 -0.0536 -0.2243 -0.0855 58   TYR   B CD2 
3078  C  CE1 . TYR   B 58  ? 1.0677 1.1151 1.3718 -0.0499 -0.2324 -0.0867 58   TYR   B CE1 
3079  C  CE2 . TYR   B 58  ? 1.1154 1.1797 1.4527 -0.0567 -0.2301 -0.0896 58   TYR   B CE2 
3080  C  CZ  . TYR   B 58  ? 1.0797 1.1331 1.4084 -0.0550 -0.2343 -0.0902 58   TYR   B CZ  
3081  O  OH  . TYR   B 58  ? 1.0816 1.1301 1.4267 -0.0584 -0.2404 -0.0945 58   TYR   B OH  
3082  N  N   . GLY   B 59  ? 0.9351 0.9999 1.1624 -0.0350 -0.2044 -0.0658 59   GLY   B N   
3083  C  CA  . GLY   B 59  ? 0.9007 0.9718 1.1175 -0.0342 -0.1967 -0.0609 59   GLY   B CA  
3084  C  C   . GLY   B 59  ? 0.9588 1.0244 1.1559 -0.0296 -0.1950 -0.0575 59   GLY   B C   
3085  O  O   . GLY   B 59  ? 1.0208 1.0775 1.2116 -0.0267 -0.1997 -0.0589 59   GLY   B O   
3086  N  N   . LYS   B 60  ? 0.9526 1.0236 1.1402 -0.0288 -0.1880 -0.0529 60   LYS   B N   
3087  C  CA  . LYS   B 60  ? 0.9356 1.0028 1.1052 -0.0243 -0.1858 -0.0493 60   LYS   B CA  
3088  C  C   . LYS   B 60  ? 0.9125 0.9796 1.0703 -0.0177 -0.1885 -0.0503 60   LYS   B C   
3089  O  O   . LYS   B 60  ? 0.9252 0.9996 1.0850 -0.0186 -0.1854 -0.0494 60   LYS   B O   
3090  C  CB  . LYS   B 60  ? 0.9835 1.0563 1.1510 -0.0280 -0.1761 -0.0434 60   LYS   B CB  
3091  C  CG  . LYS   B 60  ? 0.9750 1.0433 1.1451 -0.0315 -0.1739 -0.0416 60   LYS   B CG  
3092  C  CD  . LYS   B 60  ? 0.9546 1.0292 1.1285 -0.0370 -0.1646 -0.0367 60   LYS   B CD  
3093  C  CE  . LYS   B 60  ? 0.9264 1.0041 1.0864 -0.0341 -0.1597 -0.0322 60   LYS   B CE  
3094  N  NZ  . LYS   B 60  ? 0.9785 1.0491 1.1252 -0.0295 -0.1614 -0.0309 60   LYS   B NZ  
3095  N  N   . ILE   B 61  ? 0.9339 0.9921 1.0794 -0.0112 -0.1942 -0.0521 61   ILE   B N   
3096  C  CA  . ILE   B 61  ? 0.9200 0.9760 1.0545 -0.0044 -0.1978 -0.0538 61   ILE   B CA  
3097  C  C   . ILE   B 61  ? 0.9285 0.9896 1.0522 -0.0029 -0.1902 -0.0486 61   ILE   B C   
3098  O  O   . ILE   B 61  ? 0.9739 1.0327 1.0875 -0.0009 -0.1868 -0.0451 61   ILE   B O   
3099  C  CB  . ILE   B 61  ? 0.9123 0.9563 1.0350 0.0027  -0.2055 -0.0570 61   ILE   B CB  
3100  C  CG1 . ILE   B 61  ? 0.9667 1.0058 1.1006 0.0018  -0.2146 -0.0632 61   ILE   B CG1 
3101  C  CG2 . ILE   B 61  ? 0.9396 0.9813 1.0471 0.0100  -0.2061 -0.0566 61   ILE   B CG2 
3102  C  CD1 . ILE   B 61  ? 1.0338 1.0604 1.1556 0.0098  -0.2238 -0.0674 61   ILE   B CD1 
3103  N  N   . ALA   B 62  ? 0.9330 1.0009 1.0588 -0.0034 -0.1879 -0.0482 62   ALA   B N   
3104  C  CA  . ALA   B 62  ? 0.8818 0.9553 0.9993 -0.0025 -0.1808 -0.0435 62   ALA   B CA  
3105  C  C   . ALA   B 62  ? 0.8900 0.9607 0.9957 0.0043  -0.1829 -0.0444 62   ALA   B C   
3106  O  O   . ALA   B 62  ? 0.8842 0.9555 0.9789 0.0074  -0.1783 -0.0407 62   ALA   B O   
3107  C  CB  . ALA   B 62  ? 0.8687 0.9527 0.9974 -0.0091 -0.1748 -0.0414 62   ALA   B CB  
3108  N  N   . VAL   B 63  ? 0.8648 0.9320 0.9726 0.0069  -0.1895 -0.0492 63   VAL   B N   
3109  C  CA  . VAL   B 63  ? 0.9330 0.9951 1.0279 0.0143  -0.1922 -0.0504 63   VAL   B CA  
3110  C  C   . VAL   B 63  ? 0.9746 1.0257 1.0658 0.0195  -0.2020 -0.0559 63   VAL   B C   
3111  O  O   . VAL   B 63  ? 0.9642 1.0151 1.0678 0.0167  -0.2078 -0.0602 63   VAL   B O   
3112  C  CB  . VAL   B 63  ? 1.0039 1.0728 1.1031 0.0131  -0.1905 -0.0508 63   VAL   B CB  
3113  C  CG1 . VAL   B 63  ? 1.0018 1.0664 1.0854 0.0203  -0.1899 -0.0500 63   VAL   B CG1 
3114  C  CG2 . VAL   B 63  ? 0.9445 1.0244 1.0521 0.0061  -0.1822 -0.0465 63   VAL   B CG2 
3115  N  N   . MET   B 64  ? 1.0203 1.0622 1.0951 0.0270  -0.2039 -0.0557 64   MET   B N   
3116  C  CA  . MET   B 64  ? 1.0348 1.0647 1.1034 0.0329  -0.2133 -0.0607 64   MET   B CA  
3117  C  C   . MET   B 64  ? 1.0797 1.1017 1.1295 0.0420  -0.2141 -0.0605 64   MET   B C   
3118  O  O   . MET   B 64  ? 1.0545 1.0736 1.0915 0.0457  -0.2092 -0.0566 64   MET   B O   
3119  C  CB  . MET   B 64  ? 0.9866 1.0108 1.0540 0.0325  -0.2149 -0.0605 64   MET   B CB  
3120  C  CG  . MET   B 64  ? 1.0487 1.0597 1.1093 0.0385  -0.2251 -0.0659 64   MET   B CG  
3121  S  SD  . MET   B 64  ? 1.1172 1.1195 1.1702 0.0402  -0.2257 -0.0646 64   MET   B SD  
3122  C  CE  . MET   B 64  ? 0.9843 0.9816 1.0143 0.0488  -0.2199 -0.0600 64   MET   B CE  
3123  N  N   . GLU   B 65  ? 1.0838 1.1024 1.1320 0.0456  -0.2198 -0.0646 65   GLU   B N   
3124  C  CA  . GLU   B 65  ? 1.1077 1.1188 1.1380 0.0542  -0.2198 -0.0642 65   GLU   B CA  
3125  C  C   . GLU   B 65  ? 1.1156 1.1164 1.1419 0.0600  -0.2307 -0.0708 65   GLU   B C   
3126  O  O   . GLU   B 65  ? 1.0961 1.1006 1.1364 0.0563  -0.2361 -0.0749 65   GLU   B O   
3127  C  CB  . GLU   B 65  ? 1.0750 1.0951 1.1057 0.0523  -0.2118 -0.0604 65   GLU   B CB  
3128  C  CG  . GLU   B 65  ? 1.1058 1.1327 1.1337 0.0497  -0.2013 -0.0536 65   GLU   B CG  
3129  C  CD  . GLU   B 65  ? 1.2267 1.2444 1.2353 0.0579  -0.1988 -0.0510 65   GLU   B CD  
3130  O  OE1 . GLU   B 65  ? 1.2558 1.2622 1.2519 0.0658  -0.2043 -0.0541 65   GLU   B OE1 
3131  O  OE2 . GLU   B 65  ? 1.2087 1.2304 1.2145 0.0567  -0.1913 -0.0459 65   GLU   B OE2 
3132  N  N   . LEU   B 66  ? 1.1285 1.1161 1.1356 0.0694  -0.2340 -0.0718 66   LEU   B N   
3133  C  CA  . LEU   B 66  ? 1.1437 1.1197 1.1433 0.0764  -0.2444 -0.0779 66   LEU   B CA  
3134  C  C   . LEU   B 66  ? 1.1446 1.1186 1.1326 0.0819  -0.2420 -0.0770 66   LEU   B C   
3135  O  O   . LEU   B 66  ? 1.1645 1.1414 1.1440 0.0830  -0.2326 -0.0715 66   LEU   B O   
3136  C  CB  . LEU   B 66  ? 1.1549 1.1157 1.1391 0.0842  -0.2503 -0.0801 66   LEU   B CB  
3137  C  CG  . LEU   B 66  ? 1.0749 1.0343 1.0665 0.0805  -0.2534 -0.0812 66   LEU   B CG  
3138  C  CD1 . LEU   B 66  ? 1.0230 0.9688 0.9941 0.0888  -0.2538 -0.0801 66   LEU   B CD1 
3139  C  CD2 . LEU   B 66  ? 1.0939 1.0511 1.0994 0.0779  -0.2649 -0.0882 66   LEU   B CD2 
3140  N  N   . PHE   B 67  ? 1.1292 1.0979 1.1173 0.0855  -0.2508 -0.0826 67   PHE   B N   
3141  C  CA  . PHE   B 67  ? 1.1503 1.1171 1.1294 0.0902  -0.2497 -0.0826 67   PHE   B CA  
3142  C  C   . PHE   B 67  ? 1.1677 1.1241 1.1437 0.0962  -0.2625 -0.0900 67   PHE   B C   
3143  O  O   . PHE   B 67  ? 1.1921 1.1474 1.1795 0.0940  -0.2715 -0.0952 67   PHE   B O   
3144  C  CB  . PHE   B 67  ? 1.1111 1.0935 1.1052 0.0822  -0.2426 -0.0797 67   PHE   B CB  
3145  C  CG  . PHE   B 67  ? 1.0889 1.0798 1.1051 0.0750  -0.2482 -0.0839 67   PHE   B CG  
3146  C  CD1 . PHE   B 67  ? 1.0953 1.0913 1.1263 0.0684  -0.2495 -0.0845 67   PHE   B CD1 
3147  C  CD2 . PHE   B 67  ? 1.1082 1.1019 1.1305 0.0752  -0.2521 -0.0872 67   PHE   B CD2 
3148  C  CE1 . PHE   B 67  ? 1.0903 1.0942 1.1425 0.0617  -0.2540 -0.0882 67   PHE   B CE1 
3149  C  CE2 . PHE   B 67  ? 1.0698 1.0718 1.1137 0.0686  -0.2569 -0.0910 67   PHE   B CE2 
3150  C  CZ  . PHE   B 67  ? 1.0786 1.0858 1.1377 0.0618  -0.2576 -0.0915 67   PHE   B CZ  
3151  N  N   . ARG   B 68  ? 1.1895 1.1378 1.1499 0.1040  -0.2633 -0.0907 68   ARG   B N   
3152  C  CA  . ARG   B 68  ? 1.2188 1.1538 1.1703 0.1122  -0.2755 -0.0975 68   ARG   B CA  
3153  C  C   . ARG   B 68  ? 1.2413 1.1788 1.1926 0.1137  -0.2755 -0.0984 68   ARG   B C   
3154  O  O   . ARG   B 68  ? 1.2551 1.1851 1.1879 0.1207  -0.2713 -0.0960 68   ARG   B O   
3155  C  CB  . ARG   B 68  ? 1.2380 1.1549 1.1634 0.1234  -0.2776 -0.0975 68   ARG   B CB  
3156  C  CG  . ARG   B 68  ? 1.2863 1.1876 1.1990 0.1330  -0.2899 -0.1043 68   ARG   B CG  
3157  C  CD  . ARG   B 68  ? 1.3113 1.2070 1.2317 0.1329  -0.3026 -0.1109 68   ARG   B CD  
3158  N  NE  . ARG   B 68  ? 1.3500 1.2382 1.2611 0.1351  -0.3015 -0.1093 68   ARG   B NE  
3159  C  CZ  . ARG   B 68  ? 1.3517 1.2227 1.2378 0.1457  -0.3033 -0.1093 68   ARG   B CZ  
3160  N  NH1 . ARG   B 68  ? 1.2808 1.1402 1.1470 0.1553  -0.3043 -0.1100 68   ARG   B NH1 
3161  N  NH2 . ARG   B 68  ? 1.3525 1.2171 1.2330 0.1470  -0.3039 -0.1088 68   ARG   B NH2 
3162  N  N   . PRO   B 69  ? 1.2466 1.1941 1.2182 0.1076  -0.2799 -0.1019 69   PRO   B N   
3163  C  CA  . PRO   B 69  ? 1.2599 1.2113 1.2331 0.1081  -0.2791 -0.1025 69   PRO   B CA  
3164  C  C   . PRO   B 69  ? 1.3384 1.2743 1.2958 0.1189  -0.2896 -0.1081 69   PRO   B C   
3165  O  O   . PRO   B 69  ? 1.3054 1.2279 1.2520 0.1255  -0.2980 -0.1119 69   PRO   B O   
3166  C  CB  . PRO   B 69  ? 1.2245 1.1911 1.2257 0.0981  -0.2812 -0.1049 69   PRO   B CB  
3167  C  CG  . PRO   B 69  ? 1.2328 1.2042 1.2460 0.0917  -0.2806 -0.1041 69   PRO   B CG  
3168  C  CD  . PRO   B 69  ? 1.2775 1.2332 1.2721 0.0997  -0.2855 -0.1054 69   PRO   B CD  
3169  N  N   . LYS   B 70  ? 1.3745 1.3113 1.3294 0.1211  -0.2890 -0.1086 70   LYS   B N   
3170  C  CA  . LYS   B 70  ? 1.3590 1.2811 1.2984 0.1317  -0.2989 -0.1139 70   LYS   B CA  
3171  C  C   . LYS   B 70  ? 1.4164 1.3362 1.3688 0.1319  -0.3137 -0.1222 70   LYS   B C   
3172  O  O   . LYS   B 70  ? 1.3760 1.3093 1.3532 0.1234  -0.3158 -0.1243 70   LYS   B O   
3173  C  CB  . LYS   B 70  ? 1.2646 1.1903 1.2024 0.1326  -0.2952 -0.1128 70   LYS   B CB  
3174  N  N   . GLY   B 71  ? 1.6077 1.5101 1.5435 0.1416  -0.3240 -0.1269 71   GLY   B N   
3175  C  CA  . GLY   B 71  ? 1.6105 1.5085 1.5565 0.1430  -0.3393 -0.1353 71   GLY   B CA  
3176  C  C   . GLY   B 71  ? 1.6338 1.5360 1.5950 0.1366  -0.3424 -0.1367 71   GLY   B C   
3177  O  O   . GLY   B 71  ? 1.6778 1.5876 1.6619 0.1310  -0.3503 -0.1418 71   GLY   B O   
3178  N  N   . GLU   B 72  ? 1.5361 1.4333 1.4853 0.1375  -0.3363 -0.1324 72   GLU   B N   
3179  C  CA  . GLU   B 72  ? 1.4225 1.3221 1.3830 0.1321  -0.3382 -0.1330 72   GLU   B CA  
3180  C  C   . GLU   B 72  ? 1.3715 1.2529 1.3083 0.1412  -0.3418 -0.1336 72   GLU   B C   
3181  O  O   . GLU   B 72  ? 1.3940 1.2676 1.3083 0.1474  -0.3340 -0.1287 72   GLU   B O   
3182  C  CB  . GLU   B 72  ? 1.3913 1.3073 1.3653 0.1214  -0.3243 -0.1257 72   GLU   B CB  
3183  C  CG  . GLU   B 72  ? 1.3909 1.3254 1.3918 0.1110  -0.3213 -0.1255 72   GLU   B CG  
3184  C  CD  . GLU   B 72  ? 1.4334 1.3718 1.4572 0.1061  -0.3323 -0.1322 72   GLU   B CD  
3185  O  OE1 . GLU   B 72  ? 1.4416 1.3939 1.4878 0.0985  -0.3312 -0.1330 72   GLU   B OE1 
3186  O  OE2 . GLU   B 72  ? 1.4668 1.3943 1.4867 0.1099  -0.3418 -0.1366 72   GLU   B OE2 
3187  N  N   . SER   B 73  ? 1.3417 1.2164 1.2838 0.1419  -0.3532 -0.1394 73   SER   B N   
3188  C  CA  . SER   B 73  ? 1.3169 1.1736 1.2368 0.1506  -0.3574 -0.1404 73   SER   B CA  
3189  C  C   . SER   B 73  ? 1.4005 1.2609 1.3167 0.1467  -0.3453 -0.1332 73   SER   B C   
3190  O  O   . SER   B 73  ? 1.4478 1.2981 1.3402 0.1540  -0.3391 -0.1291 73   SER   B O   
3191  C  CB  . SER   B 73  ? 1.3375 1.1858 1.2651 0.1521  -0.3736 -0.1490 73   SER   B CB  
3192  O  OG  . SER   B 73  ? 1.3670 1.2309 1.3262 0.1406  -0.3760 -0.1512 73   SER   B OG  
3193  N  N   . LYS   B 74  ? 1.3934 1.2677 1.3322 0.1357  -0.3418 -0.1316 74   LYS   B N   
3194  C  CA  . LYS   B 74  ? 1.3400 1.2188 1.2768 0.1316  -0.3306 -0.1248 74   LYS   B CA  
3195  C  C   . LYS   B 74  ? 1.3454 1.2444 1.3001 0.1208  -0.3180 -0.1187 74   LYS   B C   
3196  O  O   . LYS   B 74  ? 1.2504 1.1602 1.2217 0.1156  -0.3187 -0.1203 74   LYS   B O   
3197  C  CB  . LYS   B 74  ? 1.2628 1.1379 1.2074 0.1288  -0.3370 -0.1278 74   LYS   B CB  
3198  C  CG  . LYS   B 74  ? 1.2410 1.1197 1.2081 0.1238  -0.3490 -0.1351 74   LYS   B CG  
3199  C  CD  . LYS   B 74  ? 1.2751 1.1504 1.2496 0.1204  -0.3537 -0.1371 74   LYS   B CD  
3200  C  CE  . LYS   B 74  ? 1.2932 1.1676 1.2864 0.1179  -0.3679 -0.1454 74   LYS   B CE  
3201  N  NZ  . LYS   B 74  ? 1.2941 1.1848 1.3117 0.1099  -0.3668 -0.1463 74   LYS   B NZ  
3202  N  N   . ASP   B 75  ? 1.3031 1.2066 1.2539 0.1179  -0.3065 -0.1119 75   ASP   B N   
3203  C  CA  . ASP   B 75  ? 1.1794 1.1009 1.1449 0.1082  -0.2943 -0.1057 75   ASP   B CA  
3204  C  C   . ASP   B 75  ? 1.1748 1.1093 1.1683 0.0975  -0.2970 -0.1081 75   ASP   B C   
3205  O  O   . ASP   B 75  ? 1.2151 1.1456 1.2175 0.0962  -0.3062 -0.1132 75   ASP   B O   
3206  C  CB  . ASP   B 75  ? 1.1677 1.0911 1.1259 0.1068  -0.2834 -0.0988 75   ASP   B CB  
3207  C  CG  . ASP   B 75  ? 1.2744 1.1870 1.2066 0.1165  -0.2781 -0.0952 75   ASP   B CG  
3208  O  OD1 . ASP   B 75  ? 1.3160 1.2169 1.2335 0.1253  -0.2840 -0.0986 75   ASP   B OD1 
3209  O  OD2 . ASP   B 75  ? 1.2871 1.2028 1.2136 0.1156  -0.2678 -0.0890 75   ASP   B OD2 
3210  N  N   . LEU   B 76  ? 1.0995 1.0496 1.1071 0.0896  -0.2882 -0.1042 76   LEU   B N   
3211  C  CA  . LEU   B 76  ? 1.0973 1.0608 1.1310 0.0789  -0.2878 -0.1049 76   LEU   B CA  
3212  C  C   . LEU   B 76  ? 1.0915 1.0658 1.1304 0.0716  -0.2752 -0.0977 76   LEU   B C   
3213  O  O   . LEU   B 76  ? 1.0962 1.0698 1.1207 0.0743  -0.2667 -0.0922 76   LEU   B O   
3214  C  CB  . LEU   B 76  ? 1.1436 1.1158 1.1914 0.0759  -0.2899 -0.1076 76   LEU   B CB  
3215  C  CG  . LEU   B 76  ? 1.1740 1.1356 1.2185 0.0830  -0.3036 -0.1154 76   LEU   B CG  
3216  C  CD1 . LEU   B 76  ? 1.1026 1.0699 1.1519 0.0834  -0.3041 -0.1168 76   LEU   B CD1 
3217  C  CD2 . LEU   B 76  ? 1.1748 1.1363 1.2375 0.0789  -0.3134 -0.1211 76   LEU   B CD2 
3218  N  N   . LEU   B 77  ? 1.0908 1.0745 1.1504 0.0625  -0.2742 -0.0978 77   LEU   B N   
3219  C  CA  . LEU   B 77  ? 1.1122 1.1047 1.1768 0.0557  -0.2637 -0.0916 77   LEU   B CA  
3220  C  C   . LEU   B 77  ? 1.0836 1.0918 1.1673 0.0466  -0.2572 -0.0893 77   LEU   B C   
3221  O  O   . LEU   B 77  ? 0.9992 1.0123 1.1013 0.0418  -0.2620 -0.0933 77   LEU   B O   
3222  C  CB  . LEU   B 77  ? 1.1066 1.0949 1.1768 0.0530  -0.2672 -0.0929 77   LEU   B CB  
3223  C  CG  . LEU   B 77  ? 1.0660 1.0603 1.1375 0.0477  -0.2572 -0.0866 77   LEU   B CG  
3224  C  CD1 . LEU   B 77  ? 1.0873 1.0778 1.1380 0.0537  -0.2504 -0.0816 77   LEU   B CD1 
3225  C  CD2 . LEU   B 77  ? 1.0398 1.0279 1.1155 0.0460  -0.2619 -0.0887 77   LEU   B CD2 
3226  N  N   . PHE   B 78  ? 1.0793 1.0951 1.1589 0.0444  -0.2463 -0.0831 78   PHE   B N   
3227  C  CA  . PHE   B 78  ? 1.0845 1.1146 1.1801 0.0359  -0.2390 -0.0802 78   PHE   B CA  
3228  C  C   . PHE   B 78  ? 1.0314 1.0668 1.1327 0.0296  -0.2319 -0.0757 78   PHE   B C   
3229  O  O   . PHE   B 78  ? 1.0282 1.0610 1.1166 0.0319  -0.2266 -0.0714 78   PHE   B O   
3230  C  CB  . PHE   B 78  ? 1.0094 1.0445 1.0972 0.0374  -0.2321 -0.0766 78   PHE   B CB  
3231  C  CG  . PHE   B 78  ? 0.9524 1.0015 1.0547 0.0291  -0.2241 -0.0732 78   PHE   B CG  
3232  C  CD1 . PHE   B 78  ? 0.9642 1.0200 1.0833 0.0248  -0.2268 -0.0765 78   PHE   B CD1 
3233  C  CD2 . PHE   B 78  ? 0.9952 1.0505 1.0938 0.0260  -0.2138 -0.0669 78   PHE   B CD2 
3234  C  CE1 . PHE   B 78  ? 0.9580 1.0261 1.0893 0.0175  -0.2191 -0.0733 78   PHE   B CE1 
3235  C  CE2 . PHE   B 78  ? 0.9800 1.0473 1.0905 0.0188  -0.2067 -0.0639 78   PHE   B CE2 
3236  C  CZ  . PHE   B 78  ? 0.9782 1.0516 1.1045 0.0146  -0.2092 -0.0670 78   PHE   B CZ  
3237  N  N   . ILE   B 79  ? 1.0156 1.0575 1.1359 0.0220  -0.2321 -0.0769 79   ILE   B N   
3238  C  CA  . ILE   B 79  ? 1.0214 1.0690 1.1483 0.0154  -0.2249 -0.0725 79   ILE   B CA  
3239  C  C   . ILE   B 79  ? 0.9648 1.0252 1.1058 0.0082  -0.2180 -0.0701 79   ILE   B C   
3240  O  O   . ILE   B 79  ? 0.9304 0.9947 1.0823 0.0068  -0.2211 -0.0734 79   ILE   B O   
3241  C  CB  . ILE   B 79  ? 1.0516 1.0943 1.1874 0.0128  -0.2301 -0.0753 79   ILE   B CB  
3242  C  CG1 . ILE   B 79  ? 0.9494 0.9812 1.0687 0.0184  -0.2320 -0.0744 79   ILE   B CG1 
3243  C  CG2 . ILE   B 79  ? 0.9991 1.0506 1.1506 0.0037  -0.2234 -0.0723 79   ILE   B CG2 
3244  C  CD1 . ILE   B 79  ? 1.0097 1.0306 1.1128 0.0279  -0.2392 -0.0778 79   ILE   B CD1 
3245  N  N   . LEU   B 80  ? 0.9525 1.0189 1.0920 0.0044  -0.2087 -0.0643 80   LEU   B N   
3246  C  CA  . LEU   B 80  ? 0.8862 0.9637 1.0379 -0.0027 -0.2015 -0.0616 80   LEU   B CA  
3247  C  C   . LEU   B 80  ? 0.9195 0.9989 1.0752 -0.0079 -0.1960 -0.0579 80   LEU   B C   
3248  O  O   . LEU   B 80  ? 0.9138 0.9894 1.0573 -0.0055 -0.1934 -0.0547 80   LEU   B O   
3249  C  CB  . LEU   B 80  ? 0.9336 1.0162 1.0765 -0.0012 -0.1953 -0.0580 80   LEU   B CB  
3250  C  CG  . LEU   B 80  ? 0.9327 1.0262 1.0847 -0.0079 -0.1869 -0.0542 80   LEU   B CG  
3251  C  CD1 . LEU   B 80  ? 0.9372 1.0358 1.1083 -0.0135 -0.1884 -0.0571 80   LEU   B CD1 
3252  C  CD2 . LEU   B 80  ? 0.9769 1.0740 1.1212 -0.0055 -0.1834 -0.0523 80   LEU   B CD2 
3253  N  N   . THR   B 81  ? 0.9304 1.0147 1.1029 -0.0147 -0.1946 -0.0585 81   THR   B N   
3254  C  CA  . THR   B 81  ? 0.9277 1.0129 1.1044 -0.0197 -0.1894 -0.0552 81   THR   B CA  
3255  C  C   . THR   B 81  ? 0.9251 1.0189 1.1034 -0.0243 -0.1796 -0.0500 81   THR   B C   
3256  O  O   . THR   B 81  ? 0.9008 1.0012 1.0820 -0.0254 -0.1770 -0.0496 81   THR   B O   
3257  C  CB  . THR   B 81  ? 0.9096 0.9941 1.1035 -0.0245 -0.1926 -0.0585 81   THR   B CB  
3258  O  OG1 . THR   B 81  ? 0.9101 1.0036 1.1191 -0.0303 -0.1882 -0.0581 81   THR   B OG1 
3259  C  CG2 . THR   B 81  ? 0.8668 0.9441 1.0628 -0.0204 -0.2035 -0.0648 81   THR   B CG2 
3260  N  N   . ALA   B 82  ? 0.9551 1.0485 1.1317 -0.0273 -0.1745 -0.0462 82   ALA   B N   
3261  C  CA  . ALA   B 82  ? 0.9083 1.0088 1.0853 -0.0315 -0.1656 -0.0413 82   ALA   B CA  
3262  C  C   . ALA   B 82  ? 0.9388 1.0463 1.1311 -0.0371 -0.1624 -0.0419 82   ALA   B C   
3263  O  O   . ALA   B 82  ? 0.9467 1.0607 1.1385 -0.0393 -0.1562 -0.0388 82   ALA   B O   
3264  C  CB  . ALA   B 82  ? 0.9412 1.0389 1.1147 -0.0335 -0.1615 -0.0376 82   ALA   B CB  
3265  N  N   . LYS   B 83  ? 0.9469 1.0536 1.1536 -0.0397 -0.1664 -0.0457 83   LYS   B N   
3266  C  CA  . LYS   B 83  ? 0.9170 1.0307 1.1389 -0.0448 -0.1629 -0.0462 83   LYS   B CA  
3267  C  C   . LYS   B 83  ? 0.9763 1.0930 1.2008 -0.0419 -0.1676 -0.0499 83   LYS   B C   
3268  O  O   . LYS   B 83  ? 0.9932 1.1135 1.2329 -0.0446 -0.1693 -0.0530 83   LYS   B O   
3269  C  CB  . LYS   B 83  ? 0.9085 1.0209 1.1464 -0.0498 -0.1633 -0.0479 83   LYS   B CB  
3270  C  CG  . LYS   B 83  ? 0.9551 1.0664 1.1929 -0.0541 -0.1559 -0.0434 83   LYS   B CG  
3271  C  CD  . LYS   B 83  ? 1.0242 1.1367 1.2808 -0.0599 -0.1541 -0.0447 83   LYS   B CD  
3272  C  CE  . LYS   B 83  ? 1.0168 1.1244 1.2731 -0.0632 -0.1497 -0.0416 83   LYS   B CE  
3273  N  NZ  . LYS   B 83  ? 1.0099 1.1180 1.2861 -0.0686 -0.1488 -0.0435 83   LYS   B NZ  
3274  N  N   . TYR   B 84  ? 0.9477 1.0624 1.1577 -0.0362 -0.1700 -0.0498 84   TYR   B N   
3275  C  CA  . TYR   B 84  ? 0.9444 1.0615 1.1530 -0.0328 -0.1732 -0.0523 84   TYR   B CA  
3276  C  C   . TYR   B 84  ? 0.9790 1.0927 1.1961 -0.0305 -0.1826 -0.0586 84   TYR   B C   
3277  O  O   . TYR   B 84  ? 1.0038 1.1201 1.2237 -0.0285 -0.1855 -0.0613 84   TYR   B O   
3278  C  CB  . TYR   B 84  ? 0.9481 1.0740 1.1633 -0.0368 -0.1665 -0.0502 84   TYR   B CB  
3279  C  CG  . TYR   B 84  ? 0.9950 1.1231 1.1990 -0.0377 -0.1587 -0.0445 84   TYR   B CG  
3280  C  CD1 . TYR   B 84  ? 0.9873 1.1144 1.1762 -0.0330 -0.1585 -0.0428 84   TYR   B CD1 
3281  C  CD2 . TYR   B 84  ? 0.9959 1.1263 1.2038 -0.0429 -0.1519 -0.0407 84   TYR   B CD2 
3282  C  CE1 . TYR   B 84  ? 0.9886 1.1179 1.1683 -0.0339 -0.1519 -0.0377 84   TYR   B CE1 
3283  C  CE2 . TYR   B 84  ? 1.0207 1.1527 1.2180 -0.0434 -0.1456 -0.0358 84   TYR   B CE2 
3284  C  CZ  . TYR   B 84  ? 1.0222 1.1539 1.2061 -0.0390 -0.1458 -0.0344 84   TYR   B CZ  
3285  O  OH  . TYR   B 84  ? 0.9786 1.1123 1.1534 -0.0396 -0.1400 -0.0297 84   TYR   B OH  
3286  N  N   . ASN   B 85  ? 0.9825 1.0899 1.2030 -0.0302 -0.1879 -0.0612 85   ASN   B N   
3287  C  CA  . ASN   B 85  ? 0.9300 1.0329 1.1568 -0.0272 -0.1981 -0.0675 85   ASN   B CA  
3288  C  C   . ASN   B 85  ? 0.8750 0.9704 1.0841 -0.0189 -0.2042 -0.0692 85   ASN   B C   
3289  O  O   . ASN   B 85  ? 0.7888 0.8785 0.9828 -0.0156 -0.2032 -0.0668 85   ASN   B O   
3290  C  CB  . ASN   B 85  ? 0.9577 1.0562 1.1952 -0.0302 -0.2017 -0.0697 85   ASN   B CB  
3291  C  CG  . ASN   B 85  ? 0.9624 1.0671 1.2146 -0.0382 -0.1938 -0.0667 85   ASN   B CG  
3292  O  OD1 . ASN   B 85  ? 0.9232 1.0253 1.1722 -0.0407 -0.1894 -0.0633 85   ASN   B OD1 
3293  N  ND2 . ASN   B 85  ? 0.9764 1.0887 1.2444 -0.0420 -0.1919 -0.0679 85   ASN   B ND2 
3294  N  N   . ALA   B 86  ? 0.9001 0.9952 1.1105 -0.0152 -0.2103 -0.0734 86   ALA   B N   
3295  C  CA  . ALA   B 86  ? 0.9473 1.0348 1.1407 -0.0069 -0.2160 -0.0753 86   ALA   B CA  
3296  C  C   . ALA   B 86  ? 0.9780 1.0593 1.1771 -0.0033 -0.2276 -0.0823 86   ALA   B C   
3297  O  O   . ALA   B 86  ? 1.0149 1.1010 1.2306 -0.0061 -0.2308 -0.0859 86   ALA   B O   
3298  C  CB  . ALA   B 86  ? 1.0031 1.0950 1.1892 -0.0046 -0.2123 -0.0736 86   ALA   B CB  
3299  N  N   . CYS   B 87  ? 1.0162 1.0865 1.2013 0.0031  -0.2340 -0.0842 87   CYS   B N   
3300  C  CA  . CYS   B 87  ? 1.0260 1.0883 1.2136 0.0074  -0.2460 -0.0910 87   CYS   B CA  
3301  C  C   . CYS   B 87  ? 1.0588 1.1102 1.2237 0.0171  -0.2507 -0.0921 87   CYS   B C   
3302  O  O   . CYS   B 87  ? 1.0476 1.0966 1.1959 0.0198  -0.2446 -0.0874 87   CYS   B O   
3303  C  CB  . CYS   B 87  ? 1.0550 1.1130 1.2517 0.0044  -0.2501 -0.0931 87   CYS   B CB  
3304  S  SG  . CYS   B 87  ? 1.1597 1.2079 1.3371 0.0077  -0.2479 -0.0895 87   CYS   B SG  
3305  N  N   . ILE   B 88  ? 1.0953 1.1397 1.2598 0.0224  -0.2616 -0.0984 88   ILE   B N   
3306  C  CA  . ILE   B 88  ? 1.1040 1.1353 1.2471 0.0322  -0.2679 -0.1004 88   ILE   B CA  
3307  C  C   . ILE   B 88  ? 1.1275 1.1491 1.2742 0.0346  -0.2795 -0.1065 88   ILE   B C   
3308  O  O   . ILE   B 88  ? 1.1760 1.2000 1.3401 0.0322  -0.2868 -0.1118 88   ILE   B O   
3309  C  CB  . ILE   B 88  ? 1.0859 1.1160 1.2211 0.0380  -0.2706 -0.1023 88   ILE   B CB  
3310  C  CG1 . ILE   B 88  ? 1.0874 1.1244 1.2143 0.0370  -0.2590 -0.0958 88   ILE   B CG1 
3311  C  CG2 . ILE   B 88  ? 1.1261 1.1410 1.2419 0.0483  -0.2794 -0.1060 88   ILE   B CG2 
3312  C  CD1 . ILE   B 88  ? 1.0776 1.1094 1.1889 0.0446  -0.2605 -0.0966 88   ILE   B CD1 
3313  N  N   . LEU   B 89  ? 1.1454 1.1565 1.2771 0.0389  -0.2811 -0.1058 89   LEU   B N   
3314  C  CA  . LEU   B 89  ? 1.1758 1.1774 1.3108 0.0404  -0.2915 -0.1111 89   LEU   B CA  
3315  C  C   . LEU   B 89  ? 1.1478 1.1340 1.2619 0.0516  -0.3008 -0.1151 89   LEU   B C   
3316  O  O   . LEU   B 89  ? 1.1427 1.1240 1.2360 0.0580  -0.2968 -0.1120 89   LEU   B O   
3317  C  CB  . LEU   B 89  ? 1.1305 1.1312 1.2662 0.0362  -0.2866 -0.1076 89   LEU   B CB  
3318  C  CG  . LEU   B 89  ? 1.1089 1.1236 1.2601 0.0261  -0.2754 -0.1022 89   LEU   B CG  
3319  C  CD1 . LEU   B 89  ? 1.0797 1.0926 1.2366 0.0215  -0.2737 -0.1008 89   LEU   B CD1 
3320  C  CD2 . LEU   B 89  ? 1.1874 1.2128 1.3613 0.0201  -0.2762 -0.1047 89   LEU   B CD2 
3321  N  N   . GLU   B 90  ? 1.1783 1.1564 1.2980 0.0539  -0.3134 -0.1221 90   GLU   B N   
3322  C  CA  . GLU   B 90  ? 1.2579 1.2194 1.3578 0.0645  -0.3236 -0.1266 90   GLU   B CA  
3323  C  C   . GLU   B 90  ? 1.3049 1.2569 1.4068 0.0647  -0.3316 -0.1303 90   GLU   B C   
3324  O  O   . GLU   B 90  ? 1.2667 1.2250 1.3903 0.0567  -0.3329 -0.1318 90   GLU   B O   
3325  C  CB  . GLU   B 90  ? 1.2386 1.1973 1.3409 0.0694  -0.3339 -0.1330 90   GLU   B CB  
3326  C  CG  . GLU   B 90  ? 1.2890 1.2292 1.3697 0.0809  -0.3451 -0.1379 90   GLU   B CG  
3327  C  CD  . GLU   B 90  ? 1.3401 1.2765 1.4229 0.0861  -0.3564 -0.1448 90   GLU   B CD  
3328  O  OE1 . GLU   B 90  ? 1.3331 1.2816 1.4380 0.0800  -0.3570 -0.1466 90   GLU   B OE1 
3329  O  OE2 . GLU   B 90  ? 1.3631 1.2839 1.4249 0.0967  -0.3646 -0.1483 90   GLU   B OE2 
3330  N  N   . TYR   B 91  ? 1.2962 1.2324 1.3752 0.0741  -0.3370 -0.1318 91   TYR   B N   
3331  C  CA  . TYR   B 91  ? 1.3359 1.2604 1.4126 0.0759  -0.3454 -0.1355 91   TYR   B CA  
3332  C  C   . TYR   B 91  ? 1.3496 1.2650 1.4307 0.0805  -0.3616 -0.1447 91   TYR   B C   
3333  O  O   . TYR   B 91  ? 1.3411 1.2527 1.4141 0.0870  -0.3667 -0.1477 91   TYR   B O   
3334  C  CB  . TYR   B 91  ? 1.3739 1.2860 1.4225 0.0841  -0.3419 -0.1320 91   TYR   B CB  
3335  C  CG  . TYR   B 91  ? 1.4405 1.3409 1.4837 0.0858  -0.3475 -0.1339 91   TYR   B CG  
3336  C  CD1 . TYR   B 91  ? 1.4387 1.3454 1.4986 0.0768  -0.3442 -0.1323 91   TYR   B CD1 
3337  C  CD2 . TYR   B 91  ? 1.4389 1.3210 1.4585 0.0967  -0.3553 -0.1371 91   TYR   B CD2 
3338  C  CE1 . TYR   B 91  ? 1.3987 1.2938 1.4526 0.0787  -0.3494 -0.1342 91   TYR   B CE1 
3339  C  CE2 . TYR   B 91  ? 1.4366 1.3072 1.4498 0.0989  -0.3604 -0.1389 91   TYR   B CE2 
3340  C  CZ  . TYR   B 91  ? 1.4242 1.3013 1.4547 0.0898  -0.3576 -0.1375 91   TYR   B CZ  
3341  O  OH  . TYR   B 91  ? 1.4933 1.3577 1.5166 0.0922  -0.3633 -0.1396 91   TYR   B OH  
3342  N  N   . LYS   B 92  ? 1.4393 1.3507 1.5334 0.0773  -0.3700 -0.1493 92   LYS   B N   
3343  C  CA  . LYS   B 92  ? 1.5427 1.4456 1.6433 0.0811  -0.3863 -0.1585 92   LYS   B CA  
3344  C  C   . LYS   B 92  ? 1.6158 1.5096 1.7221 0.0797  -0.3948 -0.1626 92   LYS   B C   
3345  O  O   . LYS   B 92  ? 1.5755 1.4783 1.7044 0.0698  -0.3918 -0.1618 92   LYS   B O   
3346  C  CB  . LYS   B 92  ? 1.4429 1.3599 1.5703 0.0745  -0.3882 -0.1614 92   LYS   B CB  
3347  N  N   . GLN   B 93  ? 1.6915 1.5666 1.7774 0.0897  -0.4057 -0.1673 93   GLN   B N   
3348  C  CA  . GLN   B 93  ? 1.6950 1.5584 1.7810 0.0901  -0.4142 -0.1712 93   GLN   B CA  
3349  C  C   . GLN   B 93  ? 1.7263 1.5784 1.8162 0.0954  -0.4328 -0.1814 93   GLN   B C   
3350  O  O   . GLN   B 93  ? 1.7242 1.5609 1.7904 0.1068  -0.4411 -0.1849 93   GLN   B O   
3351  C  CB  . GLN   B 93  ? 1.6965 1.5462 1.7526 0.0978  -0.4102 -0.1673 93   GLN   B CB  
3352  C  CG  . GLN   B 93  ? 1.7541 1.5866 1.8026 0.1022  -0.4220 -0.1727 93   GLN   B CG  
3353  C  CD  . GLN   B 93  ? 1.7697 1.5887 1.7879 0.1104  -0.4173 -0.1686 93   GLN   B CD  
3354  O  OE1 . GLN   B 93  ? 1.7313 1.5558 1.7374 0.1110  -0.4038 -0.1609 93   GLN   B OE1 
3355  N  NE2 . GLN   B 93  ? 1.7117 1.5128 1.7178 0.1167  -0.4285 -0.1737 93   GLN   B NE2 
3356  N  N   . SER   B 94  ? 1.7859 1.6447 1.9050 0.0873  -0.4397 -0.1862 94   SER   B N   
3357  C  CA  . SER   B 94  ? 1.8056 1.6536 1.9303 0.0918  -0.4582 -0.1963 94   SER   B CA  
3358  C  C   . SER   B 94  ? 1.8471 1.6754 1.9547 0.0981  -0.4675 -0.1998 94   SER   B C   
3359  O  O   . SER   B 94  ? 1.9031 1.7293 2.0280 0.0929  -0.4749 -0.2041 94   SER   B O   
3360  C  CB  . SER   B 94  ? 1.7943 1.6555 1.9569 0.0810  -0.4625 -0.2003 94   SER   B CB  
3361  O  OG  . SER   B 94  ? 1.8063 1.6586 1.9767 0.0852  -0.4808 -0.2104 94   SER   B OG  
3362  N  N   . GLY   B 95  ? 1.8213 1.6347 1.8950 0.1093  -0.4671 -0.1981 95   GLY   B N   
3363  C  CA  . GLY   B 95  ? 1.7812 1.5761 1.8368 0.1152  -0.4736 -0.2002 95   GLY   B CA  
3364  C  C   . GLY   B 95  ? 1.8248 1.6248 1.8874 0.1069  -0.4632 -0.1944 95   GLY   B C   
3365  O  O   . GLY   B 95  ? 1.8220 1.6189 1.8640 0.1099  -0.4524 -0.1877 95   GLY   B O   
3366  N  N   . GLU   B 96  ? 1.8285 1.6364 1.9206 0.0965  -0.4661 -0.1970 96   GLU   B N   
3367  C  CA  . GLU   B 96  ? 1.8276 1.6410 1.9295 0.0876  -0.4565 -0.1918 96   GLU   B CA  
3368  C  C   . GLU   B 96  ? 1.8402 1.6756 1.9638 0.0762  -0.4414 -0.1849 96   GLU   B C   
3369  O  O   . GLU   B 96  ? 1.7776 1.6180 1.8993 0.0714  -0.4288 -0.1778 96   GLU   B O   
3370  C  CB  . GLU   B 96  ? 1.7263 1.5330 1.8462 0.0832  -0.4685 -0.1985 96   GLU   B CB  
3371  N  N   . SER   B 97  ? 1.9144 1.7626 2.0577 0.0722  -0.4424 -0.1869 97   SER   B N   
3372  C  CA  . SER   B 97  ? 1.9051 1.7738 2.0715 0.0610  -0.4294 -0.1814 97   SER   B CA  
3373  C  C   . SER   B 97  ? 1.8453 1.7219 1.9958 0.0637  -0.4162 -0.1740 97   SER   B C   
3374  O  O   . SER   B 97  ? 1.8167 1.6911 1.9556 0.0709  -0.4198 -0.1759 97   SER   B O   
3375  C  CB  . SER   B 97  ? 1.8780 1.7566 2.0742 0.0556  -0.4370 -0.1873 97   SER   B CB  
3376  O  OG  . SER   B 97  ? 1.8562 1.7539 2.0695 0.0475  -0.4245 -0.1820 97   SER   B OG  
3377  N  N   . ILE   B 98  ? 1.6958 1.5814 1.8463 0.0577  -0.4011 -0.1657 98   ILE   B N   
3378  C  CA  . ILE   B 98  ? 1.6498 1.5428 1.7856 0.0596  -0.3879 -0.1583 98   ILE   B CA  
3379  C  C   . ILE   B 98  ? 1.5663 1.4791 1.7248 0.0487  -0.3760 -0.1533 98   ILE   B C   
3380  O  O   . ILE   B 98  ? 1.4535 1.3725 1.6240 0.0405  -0.3683 -0.1494 98   ILE   B O   
3381  C  CB  . ILE   B 98  ? 1.5989 1.4840 1.7102 0.0638  -0.3801 -0.1523 98   ILE   B CB  
3382  C  CG1 . ILE   B 98  ? 1.6589 1.5253 1.7420 0.0768  -0.3893 -0.1559 98   ILE   B CG1 
3383  C  CG2 . ILE   B 98  ? 1.4904 1.3875 1.5953 0.0618  -0.3644 -0.1438 98   ILE   B CG2 
3384  C  CD1 . ILE   B 98  ? 1.5951 1.4546 1.6527 0.0820  -0.3804 -0.1496 98   ILE   B CD1 
3385  N  N   . ASP   B 99  ? 1.5714 1.4935 1.7340 0.0492  -0.3740 -0.1532 99   ASP   B N   
3386  C  CA  . ASP   B 99  ? 1.5353 1.4757 1.7181 0.0399  -0.3632 -0.1489 99   ASP   B CA  
3387  C  C   . ASP   B 99  ? 1.4880 1.4343 1.6550 0.0432  -0.3531 -0.1431 99   ASP   B C   
3388  O  O   . ASP   B 99  ? 1.4497 1.3877 1.5964 0.0526  -0.3573 -0.1445 99   ASP   B O   
3389  C  CB  . ASP   B 99  ? 1.5611 1.5089 1.7708 0.0356  -0.3713 -0.1551 99   ASP   B CB  
3390  C  CG  . ASP   B 99  ? 1.6425 1.5833 1.8683 0.0331  -0.3833 -0.1620 99   ASP   B CG  
3391  O  OD1 . ASP   B 99  ? 1.6865 1.6158 1.9016 0.0351  -0.3861 -0.1622 99   ASP   B OD1 
3392  O  OD2 . ASP   B 99  ? 1.6868 1.6336 1.9365 0.0292  -0.3902 -0.1673 99   ASP   B OD2 
3393  N  N   . ILE   B 100 ? 1.4341 1.3942 1.6103 0.0355  -0.3396 -0.1364 100  ILE   B N   
3394  C  CA  . ILE   B 100 ? 1.3342 1.3020 1.4996 0.0369  -0.3292 -0.1307 100  ILE   B CA  
3395  C  C   . ILE   B 100 ? 1.3247 1.3066 1.5119 0.0309  -0.3272 -0.1315 100  ILE   B C   
3396  O  O   . ILE   B 100 ? 1.3176 1.3109 1.5242 0.0216  -0.3198 -0.1287 100  ILE   B O   
3397  C  CB  . ILE   B 100 ? 1.2450 1.2174 1.4029 0.0332  -0.3155 -0.1224 100  ILE   B CB  
3398  C  CG1 . ILE   B 100 ? 1.3070 1.2659 1.4466 0.0383  -0.3176 -0.1217 100  ILE   B CG1 
3399  C  CG2 . ILE   B 100 ? 1.2170 1.1957 1.3620 0.0357  -0.3060 -0.1170 100  ILE   B CG2 
3400  C  CD1 . ILE   B 100 ? 1.2772 1.2248 1.3887 0.0495  -0.3198 -0.1215 100  ILE   B CD1 
3401  N  N   . ILE   B 101 ? 1.3223 1.3029 1.5057 0.0365  -0.3334 -0.1353 101  ILE   B N   
3402  C  CA  . ILE   B 101 ? 1.3065 1.2992 1.5102 0.0320  -0.3334 -0.1372 101  ILE   B CA  
3403  C  C   . ILE   B 101 ? 1.2713 1.2745 1.4697 0.0304  -0.3208 -0.1307 101  ILE   B C   
3404  O  O   . ILE   B 101 ? 1.2905 1.2888 1.4660 0.0367  -0.3171 -0.1274 101  ILE   B O   
3405  C  CB  . ILE   B 101 ? 1.3367 1.3223 1.5395 0.0392  -0.3475 -0.1451 101  ILE   B CB  
3406  C  CG1 . ILE   B 101 ? 1.3911 1.3669 1.5645 0.0497  -0.3482 -0.1441 101  ILE   B CG1 
3407  C  CG2 . ILE   B 101 ? 1.3867 1.3610 1.5941 0.0409  -0.3605 -0.1518 101  ILE   B CG2 
3408  C  CD1 . ILE   B 101 ? 1.4557 1.4346 1.6294 0.0536  -0.3517 -0.1468 101  ILE   B CD1 
3409  N  N   . THR   B 102 ? 1.2299 1.2473 1.4495 0.0219  -0.3139 -0.1286 102  THR   B N   
3410  C  CA  . THR   B 102 ? 1.2161 1.2439 1.4328 0.0197  -0.3024 -0.1228 102  THR   B CA  
3411  C  C   . THR   B 102 ? 1.2465 1.2767 1.4651 0.0237  -0.3076 -0.1267 102  THR   B C   
3412  O  O   . THR   B 102 ? 1.1782 1.2152 1.4184 0.0200  -0.3119 -0.1308 102  THR   B O   
3413  C  CB  . THR   B 102 ? 1.1905 1.2313 1.4270 0.0091  -0.2919 -0.1185 102  THR   B CB  
3414  O  OG1 . THR   B 102 ? 1.2319 1.2834 1.4879 0.0051  -0.2916 -0.1204 102  THR   B OG1 
3415  C  CG2 . THR   B 102 ? 1.1921 1.2299 1.4410 0.0042  -0.2945 -0.1199 102  THR   B CG2 
3416  N  N   . ARG   B 103 ? 1.2549 1.2793 1.4509 0.0315  -0.3071 -0.1253 103  ARG   B N   
3417  C  CA  . ARG   B 103 ? 1.1756 1.2006 1.3693 0.0364  -0.3116 -0.1284 103  ARG   B CA  
3418  C  C   . ARG   B 103 ? 1.1453 1.1845 1.3488 0.0309  -0.3013 -0.1242 103  ARG   B C   
3419  O  O   . ARG   B 103 ? 1.1841 1.2280 1.3978 0.0313  -0.3052 -0.1277 103  ARG   B O   
3420  C  CB  . ARG   B 103 ? 1.1827 1.1949 1.3473 0.0470  -0.3141 -0.1281 103  ARG   B CB  
3421  C  CG  . ARG   B 103 ? 1.2411 1.2376 1.3935 0.0537  -0.3248 -0.1326 103  ARG   B CG  
3422  C  CD  . ARG   B 103 ? 1.3540 1.3421 1.5042 0.0612  -0.3387 -0.1404 103  ARG   B CD  
3423  N  NE  . ARG   B 103 ? 1.2977 1.2852 1.4339 0.0670  -0.3363 -0.1391 103  ARG   B NE  
3424  C  CZ  . ARG   B 103 ? 1.2835 1.2583 1.3925 0.0766  -0.3373 -0.1383 103  ARG   B CZ  
3425  N  NH1 . ARG   B 103 ? 1.3121 1.2733 1.4048 0.0823  -0.3417 -0.1392 103  ARG   B NH1 
3426  N  NH2 . ARG   B 103 ? 1.2653 1.2408 1.3632 0.0807  -0.3334 -0.1363 103  ARG   B NH2 
3427  N  N   . ALA   B 104 ? 1.1319 1.1777 1.3323 0.0260  -0.2887 -0.1170 104  ALA   B N   
3428  C  CA  . ALA   B 104 ? 1.1337 1.1927 1.3443 0.0200  -0.2787 -0.1130 104  ALA   B CA  
3429  C  C   . ALA   B 104 ? 1.1824 1.2487 1.4010 0.0117  -0.2683 -0.1074 104  ALA   B C   
3430  O  O   . ALA   B 104 ? 1.1589 1.2193 1.3689 0.0119  -0.2670 -0.1053 104  ALA   B O   
3431  C  CB  . ALA   B 104 ? 1.1022 1.1608 1.2940 0.0248  -0.2732 -0.1094 104  ALA   B CB  
3432  N  N   . HIS   B 105 ? 1.1347 1.2131 1.3689 0.0047  -0.2608 -0.1049 105  HIS   B N   
3433  C  CA  . HIS   B 105 ? 1.1065 1.1918 1.3477 -0.0030 -0.2502 -0.0993 105  HIS   B CA  
3434  C  C   . HIS   B 105 ? 1.1036 1.2011 1.3559 -0.0083 -0.2417 -0.0964 105  HIS   B C   
3435  O  O   . HIS   B 105 ? 1.1642 1.2653 1.4222 -0.0067 -0.2447 -0.0993 105  HIS   B O   
3436  C  CB  . HIS   B 105 ? 1.1440 1.2283 1.4015 -0.0079 -0.2534 -0.1016 105  HIS   B CB  
3437  C  CG  . HIS   B 105 ? 1.1667 1.2565 1.4484 -0.0113 -0.2589 -0.1068 105  HIS   B CG  
3438  N  ND1 . HIS   B 105 ? 1.1407 1.2394 1.4440 -0.0198 -0.2531 -0.1054 105  HIS   B ND1 
3439  C  CD2 . HIS   B 105 ? 1.2159 1.3036 1.5038 -0.0072 -0.2696 -0.1134 105  HIS   B CD2 
3440  C  CE1 . HIS   B 105 ? 1.1733 1.2756 1.4962 -0.0210 -0.2597 -0.1109 105  HIS   B CE1 
3441  N  NE2 . HIS   B 105 ? 1.2674 1.3634 1.5817 -0.0134 -0.2702 -0.1159 105  HIS   B NE2 
3442  N  N   . GLY   B 106 ? 1.0813 1.1845 1.3356 -0.0142 -0.2312 -0.0907 106  GLY   B N   
3443  C  CA  . GLY   B 106 ? 0.9627 1.0767 1.2265 -0.0198 -0.2219 -0.0871 106  GLY   B CA  
3444  C  C   . GLY   B 106 ? 0.9515 1.0675 1.2060 -0.0231 -0.2112 -0.0802 106  GLY   B C   
3445  O  O   . GLY   B 106 ? 0.9987 1.1084 1.2367 -0.0199 -0.2107 -0.0778 106  GLY   B O   
3446  N  N   . ASN   B 107 ? 0.9231 1.0478 1.1882 -0.0294 -0.2026 -0.0768 107  ASN   B N   
3447  C  CA  . ASN   B 107 ? 0.8855 1.0126 1.1424 -0.0326 -0.1924 -0.0703 107  ASN   B CA  
3448  C  C   . ASN   B 107 ? 0.9284 1.0593 1.1743 -0.0307 -0.1874 -0.0674 107  ASN   B C   
3449  O  O   . ASN   B 107 ? 0.9393 1.0767 1.1939 -0.0325 -0.1853 -0.0680 107  ASN   B O   
3450  C  CB  . ASN   B 107 ? 0.8910 1.0239 1.1644 -0.0403 -0.1856 -0.0682 107  ASN   B CB  
3451  C  CG  . ASN   B 107 ? 1.0255 1.1588 1.2900 -0.0433 -0.1766 -0.0620 107  ASN   B CG  
3452  O  OD1 . ASN   B 107 ? 1.0713 1.1986 1.3268 -0.0421 -0.1773 -0.0606 107  ASN   B OD1 
3453  N  ND2 . ASN   B 107 ? 1.0291 1.1692 1.2958 -0.0469 -0.1681 -0.0584 107  ASN   B ND2 
3454  N  N   . VAL   B 108 ? 0.9368 1.0637 1.1640 -0.0272 -0.1854 -0.0641 108  VAL   B N   
3455  C  CA  . VAL   B 108 ? 0.9529 1.0820 1.1684 -0.0245 -0.1818 -0.0617 108  VAL   B CA  
3456  C  C   . VAL   B 108 ? 1.0345 1.1705 1.2506 -0.0296 -0.1716 -0.0564 108  VAL   B C   
3457  O  O   . VAL   B 108 ? 1.0317 1.1695 1.2375 -0.0281 -0.1676 -0.0536 108  VAL   B O   
3458  C  CB  . VAL   B 108 ? 0.9781 1.0997 1.1738 -0.0181 -0.1840 -0.0607 108  VAL   B CB  
3459  C  CG1 . VAL   B 108 ? 0.9724 1.0866 1.1648 -0.0117 -0.1942 -0.0662 108  VAL   B CG1 
3460  C  CG2 . VAL   B 108 ? 1.0176 1.1361 1.2073 -0.0194 -0.1809 -0.0573 108  VAL   B CG2 
3461  N  N   . GLN   B 109 ? 1.0297 1.1690 1.2575 -0.0355 -0.1674 -0.0549 109  GLN   B N   
3462  C  CA  . GLN   B 109 ? 1.0255 1.1698 1.2524 -0.0400 -0.1580 -0.0498 109  GLN   B CA  
3463  C  C   . GLN   B 109 ? 1.0285 1.1791 1.2583 -0.0410 -0.1543 -0.0493 109  GLN   B C   
3464  O  O   . GLN   B 109 ? 1.0514 1.2040 1.2899 -0.0401 -0.1583 -0.0531 109  GLN   B O   
3465  C  CB  . GLN   B 109 ? 1.0015 1.1471 1.2410 -0.0458 -0.1544 -0.0488 109  GLN   B CB  
3466  C  CG  . GLN   B 109 ? 1.0385 1.1885 1.2774 -0.0503 -0.1449 -0.0439 109  GLN   B CG  
3467  C  CD  . GLN   B 109 ? 1.0927 1.2414 1.3386 -0.0549 -0.1410 -0.0419 109  GLN   B CD  
3468  O  OE1 . GLN   B 109 ? 1.1238 1.2712 1.3825 -0.0567 -0.1442 -0.0449 109  GLN   B OE1 
3469  N  NE2 . GLN   B 109 ? 1.0513 1.2000 1.2890 -0.0568 -0.1342 -0.0371 109  GLN   B NE2 
3470  N  N   . ASP   B 110 ? 1.0498 1.2034 1.2720 -0.0428 -0.1471 -0.0447 110  ASP   B N   
3471  C  CA  . ASP   B 110 ? 1.0719 1.2312 1.2963 -0.0443 -0.1427 -0.0437 110  ASP   B CA  
3472  C  C   . ASP   B 110 ? 1.1236 1.2869 1.3549 -0.0501 -0.1348 -0.0404 110  ASP   B C   
3473  O  O   . ASP   B 110 ? 1.0840 1.2456 1.3090 -0.0518 -0.1308 -0.0367 110  ASP   B O   
3474  C  CB  . ASP   B 110 ? 1.0947 1.2536 1.3037 -0.0410 -0.1412 -0.0414 110  ASP   B CB  
3475  C  CG  . ASP   B 110 ? 1.0479 1.2025 1.2494 -0.0348 -0.1482 -0.0446 110  ASP   B CG  
3476  O  OD1 . ASP   B 110 ? 1.0041 1.1579 1.2137 -0.0330 -0.1541 -0.0492 110  ASP   B OD1 
3477  O  OD2 . ASP   B 110 ? 1.0302 1.1819 1.2177 -0.0315 -0.1476 -0.0425 110  ASP   B OD2 
3478  N  N   . ARG   B 111 ? 1.2387 1.4068 1.4826 -0.0528 -0.1326 -0.0417 111  ARG   B N   
3479  C  CA  . ARG   B 111 ? 1.2394 1.4107 1.4911 -0.0581 -0.1250 -0.0390 111  ARG   B CA  
3480  C  C   . ARG   B 111 ? 1.2568 1.4276 1.4956 -0.0592 -0.1186 -0.0339 111  ARG   B C   
3481  O  O   . ARG   B 111 ? 1.2988 1.4683 1.5378 -0.0624 -0.1138 -0.0309 111  ARG   B O   
3482  C  CB  . ARG   B 111 ? 1.2565 1.4332 1.5200 -0.0595 -0.1231 -0.0407 111  ARG   B CB  
3483  N  N   . ILE   B 112 ? 1.1398 1.3114 1.3675 -0.0566 -0.1186 -0.0329 112  ILE   B N   
3484  C  CA  . ILE   B 112 ? 1.1623 1.3336 1.3775 -0.0571 -0.1138 -0.0285 112  ILE   B CA  
3485  C  C   . ILE   B 112 ? 1.1517 1.3196 1.3542 -0.0529 -0.1179 -0.0282 112  ILE   B C   
3486  O  O   . ILE   B 112 ? 1.1548 1.3211 1.3565 -0.0491 -0.1238 -0.0313 112  ILE   B O   
3487  C  CB  . ILE   B 112 ? 1.3272 1.5022 1.5404 -0.0580 -0.1094 -0.0272 112  ILE   B CB  
3488  C  CG1 . ILE   B 112 ? 1.3533 1.5275 1.5530 -0.0580 -0.1058 -0.0231 112  ILE   B CG1 
3489  C  CG2 . ILE   B 112 ? 1.2131 1.3896 1.4271 -0.0546 -0.1139 -0.0305 112  ILE   B CG2 
3490  C  CD1 . ILE   B 112 ? 1.2530 1.4251 1.4498 -0.0606 -0.1019 -0.0197 112  ILE   B CD1 
3491  N  N   . GLY   B 113 ? 1.1449 1.3114 1.3375 -0.0533 -0.1149 -0.0245 113  GLY   B N   
3492  C  CA  . GLY   B 113 ? 1.0877 1.2518 1.2683 -0.0494 -0.1173 -0.0235 113  GLY   B CA  
3493  C  C   . GLY   B 113 ? 1.1254 1.2872 1.2999 -0.0501 -0.1154 -0.0203 113  GLY   B C   
3494  O  O   . GLY   B 113 ? 1.1750 1.3347 1.3547 -0.0519 -0.1154 -0.0205 113  GLY   B O   
3495  N  N   . ARG   B 114 ? 1.0234 1.1854 1.1875 -0.0489 -0.1136 -0.0174 114  ARG   B N   
3496  C  CA  . ARG   B 114 ? 1.0790 1.2388 1.2371 -0.0489 -0.1123 -0.0145 114  ARG   B CA  
3497  C  C   . ARG   B 114 ? 1.1109 1.2665 1.2652 -0.0449 -0.1172 -0.0159 114  ARG   B C   
3498  O  O   . ARG   B 114 ? 1.1497 1.3046 1.2988 -0.0411 -0.1199 -0.0170 114  ARG   B O   
3499  C  CB  . ARG   B 114 ? 1.0638 1.2257 1.2135 -0.0490 -0.1090 -0.0111 114  ARG   B CB  
3500  N  N   . PRO   B 115 ? 1.0802 1.2322 1.2362 -0.0453 -0.1184 -0.0160 115  PRO   B N   
3501  C  CA  . PRO   B 115 ? 1.0742 1.2216 1.2245 -0.0411 -0.1227 -0.0169 115  PRO   B CA  
3502  C  C   . PRO   B 115 ? 1.0933 1.2411 1.2327 -0.0382 -0.1214 -0.0140 115  PRO   B C   
3503  O  O   . PRO   B 115 ? 1.0867 1.2369 1.2232 -0.0401 -0.1174 -0.0108 115  PRO   B O   
3504  C  CB  . PRO   B 115 ? 1.0623 1.2062 1.2161 -0.0430 -0.1228 -0.0166 115  PRO   B CB  
3505  C  CG  . PRO   B 115 ? 1.0673 1.2135 1.2324 -0.0477 -0.1205 -0.0176 115  PRO   B CG  
3506  C  CD  . PRO   B 115 ? 1.0845 1.2359 1.2491 -0.0494 -0.1164 -0.0161 115  PRO   B CD  
3507  N  N   . SER   B 116 ? 1.0642 1.2095 1.1978 -0.0334 -0.1248 -0.0153 116  SER   B N   
3508  C  CA  . SER   B 116 ? 1.0491 1.1946 1.1732 -0.0304 -0.1232 -0.0126 116  SER   B CA  
3509  C  C   . SER   B 116 ? 1.0832 1.2264 1.2036 -0.0299 -0.1226 -0.0103 116  SER   B C   
3510  O  O   . SER   B 116 ? 1.0614 1.2004 1.1838 -0.0298 -0.1250 -0.0116 116  SER   B O   
3511  C  CB  . SER   B 116 ? 1.0026 1.1449 1.1208 -0.0249 -0.1265 -0.0143 116  SER   B CB  
3512  O  OG  . SER   B 116 ? 1.0687 1.2135 1.1885 -0.0251 -0.1262 -0.0156 116  SER   B OG  
3513  N  N   . GLU   B 117 ? 1.0753 1.2211 1.1903 -0.0294 -0.1194 -0.0069 117  GLU   B N   
3514  C  CA  . GLU   B 117 ? 0.9835 1.1277 1.0945 -0.0286 -0.1186 -0.0045 117  GLU   B CA  
3515  C  C   . GLU   B 117 ? 1.0399 1.1784 1.1455 -0.0235 -0.1220 -0.0055 117  GLU   B C   
3516  O  O   . GLU   B 117 ? 1.1908 1.3254 1.2958 -0.0232 -0.1234 -0.0055 117  GLU   B O   
3517  C  CB  . GLU   B 117 ? 1.0545 1.2032 1.1619 -0.0288 -0.1151 -0.0010 117  GLU   B CB  
3518  C  CG  . GLU   B 117 ? 1.2034 1.3569 1.3146 -0.0335 -0.1120 0.0002  117  GLU   B CG  
3519  C  CD  . GLU   B 117 ? 1.3507 1.5077 1.4587 -0.0339 -0.1093 0.0036  117  GLU   B CD  
3520  O  OE1 . GLU   B 117 ? 1.4162 1.5773 1.5253 -0.0362 -0.1072 0.0044  117  GLU   B OE1 
3521  O  OE2 . GLU   B 117 ? 1.3915 1.5471 1.4959 -0.0319 -0.1096 0.0052  117  GLU   B OE2 
3522  N  N   . THR   B 118 ? 1.0562 1.1937 1.1568 -0.0192 -0.1231 -0.0061 118  THR   B N   
3523  C  CA  . THR   B 118 ? 1.0765 1.2076 1.1707 -0.0137 -0.1263 -0.0072 118  THR   B CA  
3524  C  C   . THR   B 118 ? 1.0699 1.1954 1.1669 -0.0130 -0.1314 -0.0114 118  THR   B C   
3525  O  O   . THR   B 118 ? 1.1092 1.2283 1.2004 -0.0082 -0.1348 -0.0129 118  THR   B O   
3526  C  CB  . THR   B 118 ? 1.0372 1.1676 1.1243 -0.0089 -0.1255 -0.0066 118  THR   B CB  
3527  O  OG1 . THR   B 118 ? 1.0063 1.1370 1.0954 -0.0090 -0.1269 -0.0091 118  THR   B OG1 
3528  C  CG2 . THR   B 118 ? 1.0330 1.1692 1.1187 -0.0096 -0.1206 -0.0026 118  THR   B CG2 
3529  N  N   . GLY   B 119 ? 1.0165 1.1441 1.1224 -0.0175 -0.1321 -0.0134 119  GLY   B N   
3530  C  CA  . GLY   B 119 ? 1.0297 1.1526 1.1407 -0.0178 -0.1368 -0.0171 119  GLY   B CA  
3531  C  C   . GLY   B 119 ? 0.9076 1.0272 1.0180 -0.0143 -0.1416 -0.0210 119  GLY   B C   
3532  O  O   . GLY   B 119 ? 0.9398 1.0609 1.0461 -0.0120 -0.1408 -0.0209 119  GLY   B O   
3533  N  N   . ILE   B 120 ? 0.9108 1.0256 1.0256 -0.0139 -0.1468 -0.0247 120  ILE   B N   
3534  C  CA  . ILE   B 120 ? 0.8953 1.0070 1.0114 -0.0111 -0.1522 -0.0290 120  ILE   B CA  
3535  C  C   . ILE   B 120 ? 0.9032 1.0085 1.0061 -0.0037 -0.1547 -0.0294 120  ILE   B C   
3536  O  O   . ILE   B 120 ? 0.9382 1.0379 1.0343 -0.0004 -0.1562 -0.0289 120  ILE   B O   
3537  C  CB  . ILE   B 120 ? 0.8500 0.9582 0.9753 -0.0128 -0.1576 -0.0331 120  ILE   B CB  
3538  C  CG1 . ILE   B 120 ? 0.9061 1.0206 1.0450 -0.0200 -0.1543 -0.0326 120  ILE   B CG1 
3539  C  CG2 . ILE   B 120 ? 0.9381 1.0424 1.0636 -0.0089 -0.1641 -0.0378 120  ILE   B CG2 
3540  C  CD1 . ILE   B 120 ? 0.8379 0.9493 0.9878 -0.0229 -0.1581 -0.0356 120  ILE   B CD1 
3541  N  N   . ILE   B 121 ? 0.8823 0.9882 0.9812 -0.0009 -0.1547 -0.0300 121  ILE   B N   
3542  C  CA  . ILE   B 121 ? 0.8164 0.9153 0.9027 0.0065  -0.1571 -0.0308 121  ILE   B CA  
3543  C  C   . ILE   B 121 ? 0.9311 1.0254 1.0186 0.0093  -0.1638 -0.0359 121  ILE   B C   
3544  O  O   . ILE   B 121 ? 0.9263 1.0255 1.0224 0.0061  -0.1640 -0.0375 121  ILE   B O   
3545  C  CB  . ILE   B 121 ? 0.8046 0.9068 0.8835 0.0082  -0.1513 -0.0270 121  ILE   B CB  
3546  C  CG1 . ILE   B 121 ? 0.8412 0.9480 0.9194 0.0057  -0.1453 -0.0222 121  ILE   B CG1 
3547  C  CG2 . ILE   B 121 ? 0.8422 0.9360 0.9077 0.0162  -0.1533 -0.0279 121  ILE   B CG2 
3548  C  CD1 . ILE   B 121 ? 0.8550 0.9617 0.9233 0.0096  -0.1406 -0.0186 121  ILE   B CD1 
3549  N  N   . GLY   B 122 ? 0.9188 1.0036 0.9977 0.0156  -0.1694 -0.0386 122  GLY   B N   
3550  C  CA  . GLY   B 122 ? 0.9273 1.0069 1.0068 0.0189  -0.1766 -0.0437 122  GLY   B CA  
3551  C  C   . GLY   B 122 ? 0.9568 1.0266 1.0199 0.0276  -0.1791 -0.0444 122  GLY   B C   
3552  O  O   . GLY   B 122 ? 0.9966 1.0590 1.0512 0.0317  -0.1810 -0.0443 122  GLY   B O   
3553  N  N   . ILE   B 123 ? 0.9652 1.0341 1.0228 0.0308  -0.1787 -0.0449 123  ILE   B N   
3554  C  CA  . ILE   B 123 ? 0.9641 1.0229 1.0049 0.0395  -0.1802 -0.0452 123  ILE   B CA  
3555  C  C   . ILE   B 123 ? 0.9852 1.0375 1.0243 0.0438  -0.1882 -0.0507 123  ILE   B C   
3556  O  O   . ILE   B 123 ? 0.9818 1.0393 1.0330 0.0399  -0.1911 -0.0536 123  ILE   B O   
3557  C  CB  . ILE   B 123 ? 0.9518 1.0137 0.9848 0.0406  -0.1718 -0.0403 123  ILE   B CB  
3558  C  CG1 . ILE   B 123 ? 1.0393 1.1113 1.0828 0.0347  -0.1682 -0.0394 123  ILE   B CG1 
3559  C  CG2 . ILE   B 123 ? 0.9374 1.0025 0.9683 0.0391  -0.1653 -0.0353 123  ILE   B CG2 
3560  C  CD1 . ILE   B 123 ? 0.9845 1.0609 1.0229 0.0342  -0.1595 -0.0341 123  ILE   B CD1 
3561  N  N   . ILE   B 124 ? 0.9895 1.0300 1.0128 0.0525  -0.1917 -0.0522 124  ILE   B N   
3562  C  CA  . ILE   B 124 ? 1.0128 1.0453 1.0311 0.0581  -0.1995 -0.0573 124  ILE   B CA  
3563  C  C   . ILE   B 124 ? 1.1411 1.1660 1.1413 0.0656  -0.1961 -0.0552 124  ILE   B C   
3564  O  O   . ILE   B 124 ? 1.1310 1.1498 1.1182 0.0702  -0.1923 -0.0521 124  ILE   B O   
3565  C  CB  . ILE   B 124 ? 1.0277 1.0504 1.0441 0.0620  -0.2095 -0.0625 124  ILE   B CB  
3566  C  CG1 . ILE   B 124 ? 1.0743 1.1042 1.1109 0.0549  -0.2146 -0.0662 124  ILE   B CG1 
3567  C  CG2 . ILE   B 124 ? 1.1310 1.1410 1.1332 0.0713  -0.2165 -0.0666 124  ILE   B CG2 
3568  C  CD1 . ILE   B 124 ? 1.0108 1.0359 1.0510 0.0546  -0.2207 -0.0690 124  ILE   B CD1 
3569  N  N   . ASP   B 125 ? 1.1829 1.2083 1.1828 0.0667  -0.1969 -0.0566 125  ASP   B N   
3570  C  CA  . ASP   B 125 ? 1.1946 1.2125 1.1780 0.0738  -0.1938 -0.0549 125  ASP   B CA  
3571  C  C   . ASP   B 125 ? 1.2197 1.2214 1.1844 0.0839  -0.1988 -0.0570 125  ASP   B C   
3572  O  O   . ASP   B 125 ? 1.1864 1.1815 1.1516 0.0866  -0.2085 -0.0623 125  ASP   B O   
3573  C  CB  . ASP   B 125 ? 1.2128 1.2323 1.1998 0.0737  -0.1965 -0.0577 125  ASP   B CB  
3574  C  CG  . ASP   B 125 ? 1.2812 1.2896 1.2495 0.0824  -0.1957 -0.0574 125  ASP   B CG  
3575  O  OD1 . ASP   B 125 ? 1.3249 1.3207 1.2819 0.0903  -0.2036 -0.0616 125  ASP   B OD1 
3576  O  OD2 . ASP   B 125 ? 1.3131 1.3248 1.2777 0.0816  -0.1873 -0.0529 125  ASP   B OD2 
3577  N  N   . PRO   B 126 ? 1.1853 1.1801 1.1335 0.0899  -0.1926 -0.0531 126  PRO   B N   
3578  C  CA  . PRO   B 126 ? 1.2279 1.2066 1.1568 0.1000  -0.1964 -0.0545 126  PRO   B CA  
3579  C  C   . PRO   B 126 ? 1.3485 1.3156 1.2695 0.1069  -0.2068 -0.0608 126  PRO   B C   
3580  O  O   . PRO   B 126 ? 1.3611 1.3159 1.2716 0.1136  -0.2141 -0.0642 126  PRO   B O   
3581  C  CB  . PRO   B 126 ? 1.2028 1.1779 1.1174 0.1043  -0.1862 -0.0487 126  PRO   B CB  
3582  C  CG  . PRO   B 126 ? 1.2636 1.2543 1.1923 0.0952  -0.1771 -0.0437 126  PRO   B CG  
3583  C  CD  . PRO   B 126 ? 1.2551 1.2567 1.2022 0.0873  -0.1812 -0.0468 126  PRO   B CD  
3584  N  N   . GLU   B 127 ? 1.3917 1.3619 1.3168 0.1058  -0.2080 -0.0624 127  GLU   B N   
3585  C  CA  . GLU   B 127 ? 1.4331 1.3938 1.3531 0.1117  -0.2186 -0.0688 127  GLU   B CA  
3586  C  C   . GLU   B 127 ? 1.4214 1.3908 1.3622 0.1051  -0.2269 -0.0739 127  GLU   B C   
3587  O  O   . GLU   B 127 ? 1.4314 1.4005 1.3763 0.1061  -0.2330 -0.0781 127  GLU   B O   
3588  C  CB  . GLU   B 127 ? 1.4589 1.4165 1.3697 0.1154  -0.2153 -0.0676 127  GLU   B CB  
3589  C  CG  . GLU   B 127 ? 1.4916 1.4458 1.3879 0.1186  -0.2037 -0.0610 127  GLU   B CG  
3590  C  CD  . GLU   B 127 ? 1.7383 1.6856 1.6218 0.1241  -0.2011 -0.0602 127  GLU   B CD  
3591  O  OE1 . GLU   B 127 ? 1.7744 1.7224 1.6629 0.1240  -0.2073 -0.0644 127  GLU   B OE1 
3592  O  OE2 . GLU   B 127 ? 1.8070 1.7482 1.6759 0.1286  -0.1924 -0.0553 127  GLU   B OE2 
3593  N  N   . CYS   B 128 ? 1.3712 1.3483 1.3255 0.0985  -0.2269 -0.0735 128  CYS   B N   
3594  C  CA  . CYS   B 128 ? 1.3364 1.3227 1.3122 0.0912  -0.2330 -0.0775 128  CYS   B CA  
3595  C  C   . CYS   B 128 ? 1.3306 1.3250 1.3187 0.0875  -0.2344 -0.0797 128  CYS   B C   
3596  O  O   . CYS   B 128 ? 1.3663 1.3619 1.3662 0.0863  -0.2435 -0.0853 128  CYS   B O   
3597  C  CB  . CYS   B 128 ? 1.2747 1.2505 1.2485 0.0959  -0.2453 -0.0839 128  CYS   B CB  
3598  S  SG  . CYS   B 128 ? 1.3692 1.3372 1.3329 0.0985  -0.2442 -0.0818 128  CYS   B SG  
3599  N  N   . ARG   B 129 ? 1.4007 1.4010 1.3870 0.0856  -0.2257 -0.0753 129  ARG   B N   
3600  C  CA  . ARG   B 129 ? 1.4320 1.4398 1.4295 0.0822  -0.2268 -0.0772 129  ARG   B CA  
3601  C  C   . ARG   B 129 ? 1.4273 1.4507 1.4483 0.0714  -0.2244 -0.0767 129  ARG   B C   
3602  O  O   . ARG   B 129 ? 1.4282 1.4572 1.4630 0.0684  -0.2291 -0.0804 129  ARG   B O   
3603  C  CB  . ARG   B 129 ? 1.4420 1.4496 1.4287 0.0842  -0.2185 -0.0729 129  ARG   B CB  
3604  C  CG  . ARG   B 129 ? 1.4945 1.4860 1.4582 0.0954  -0.2211 -0.0739 129  ARG   B CG  
3605  C  CD  . ARG   B 129 ? 1.5808 1.5679 1.5428 0.0997  -0.2281 -0.0787 129  ARG   B CD  
3606  N  NE  . ARG   B 129 ? 1.6619 1.6560 1.6261 0.0965  -0.2205 -0.0753 129  ARG   B NE  
3607  C  CZ  . ARG   B 129 ? 1.6460 1.6508 1.6265 0.0907  -0.2216 -0.0771 129  ARG   B CZ  
3608  N  NH1 . ARG   B 129 ? 1.6226 1.6319 1.6188 0.0879  -0.2302 -0.0824 129  ARG   B NH1 
3609  N  NH2 . ARG   B 129 ? 1.5831 1.5940 1.5645 0.0875  -0.2136 -0.0733 129  ARG   B NH2 
3610  N  N   . MET   B 130 ? 1.3321 1.3622 1.3578 0.0658  -0.2174 -0.0722 130  MET   B N   
3611  C  CA  . MET   B 130 ? 1.2376 1.2816 1.2835 0.0558  -0.2138 -0.0709 130  MET   B CA  
3612  C  C   . MET   B 130 ? 1.1877 1.2339 1.2362 0.0521  -0.2105 -0.0680 130  MET   B C   
3613  O  O   . MET   B 130 ? 1.1535 1.1925 1.1879 0.0566  -0.2083 -0.0655 130  MET   B O   
3614  C  CB  . MET   B 130 ? 1.1481 1.2012 1.1969 0.0515  -0.2049 -0.0667 130  MET   B CB  
3615  C  CG  . MET   B 130 ? 1.1231 1.1741 1.1579 0.0533  -0.1962 -0.0607 130  MET   B CG  
3616  S  SD  . MET   B 130 ? 1.2900 1.3478 1.3239 0.0507  -0.1875 -0.0566 130  MET   B SD  
3617  C  CE  . MET   B 130 ? 1.1821 1.2551 1.2392 0.0400  -0.1856 -0.0567 130  MET   B CE  
3618  N  N   . ILE   B 131 ? 1.1430 1.1988 1.2094 0.0441  -0.2098 -0.0682 131  ILE   B N   
3619  C  CA  . ILE   B 131 ? 1.0460 1.1064 1.1170 0.0390  -0.2048 -0.0646 131  ILE   B CA  
3620  C  C   . ILE   B 131 ? 1.0643 1.1363 1.1421 0.0322  -0.1951 -0.0596 131  ILE   B C   
3621  O  O   . ILE   B 131 ? 1.0348 1.1143 1.1242 0.0278  -0.1943 -0.0605 131  ILE   B O   
3622  C  CB  . ILE   B 131 ? 1.0724 1.1342 1.1581 0.0351  -0.2109 -0.0684 131  ILE   B CB  
3623  C  CG1 . ILE   B 131 ? 1.0830 1.1328 1.1619 0.0421  -0.2216 -0.0740 131  ILE   B CG1 
3624  C  CG2 . ILE   B 131 ? 1.0235 1.0886 1.1123 0.0304  -0.2059 -0.0647 131  ILE   B CG2 
3625  C  CD1 . ILE   B 131 ? 1.0562 1.1068 1.1501 0.0384  -0.2282 -0.0780 131  ILE   B CD1 
3626  N  N   . GLY   B 132 ? 1.0418 1.1150 1.1124 0.0315  -0.1878 -0.0544 132  GLY   B N   
3627  C  CA  . GLY   B 132 ? 0.9474 1.0311 1.0241 0.0250  -0.1790 -0.0496 132  GLY   B CA  
3628  C  C   . GLY   B 132 ? 0.9478 1.0372 1.0347 0.0187  -0.1766 -0.0478 132  GLY   B C   
3629  O  O   . GLY   B 132 ? 0.9466 1.0311 1.0292 0.0204  -0.1781 -0.0475 132  GLY   B O   
3630  N  N   . LEU   B 133 ? 0.9625 1.0616 1.0623 0.0116  -0.1727 -0.0465 133  LEU   B N   
3631  C  CA  . LEU   B 133 ? 0.9028 1.0073 1.0120 0.0053  -0.1695 -0.0445 133  LEU   B CA  
3632  C  C   . LEU   B 133 ? 0.9252 1.0380 1.0360 0.0005  -0.1611 -0.0397 133  LEU   B C   
3633  O  O   . LEU   B 133 ? 0.9969 1.1144 1.1113 -0.0013 -0.1590 -0.0396 133  LEU   B O   
3634  C  CB  . LEU   B 133 ? 0.8408 0.9480 0.9657 0.0010  -0.1737 -0.0483 133  LEU   B CB  
3635  C  CG  . LEU   B 133 ? 0.8750 0.9739 0.9998 0.0050  -0.1825 -0.0531 133  LEU   B CG  
3636  C  CD1 . LEU   B 133 ? 0.8523 0.9548 0.9947 -0.0001 -0.1858 -0.0563 133  LEU   B CD1 
3637  C  CD2 . LEU   B 133 ? 0.8898 0.9824 1.0045 0.0077  -0.1825 -0.0512 133  LEU   B CD2 
3638  N  N   . ARG   B 134 ? 0.9058 1.0199 1.0133 -0.0010 -0.1565 -0.0357 134  ARG   B N   
3639  C  CA  . ARG   B 134 ? 0.9555 1.0772 1.0650 -0.0057 -0.1492 -0.0313 134  ARG   B CA  
3640  C  C   . ARG   B 134 ? 1.0092 1.1343 1.1279 -0.0113 -0.1476 -0.0303 134  ARG   B C   
3641  O  O   . ARG   B 134 ? 0.9419 1.0654 1.0569 -0.0112 -0.1462 -0.0280 134  ARG   B O   
3642  C  CB  . ARG   B 134 ? 0.8656 0.9861 0.9636 -0.0027 -0.1449 -0.0273 134  ARG   B CB  
3643  C  CG  . ARG   B 134 ? 0.8939 1.0220 0.9937 -0.0069 -0.1382 -0.0233 134  ARG   B CG  
3644  C  CD  . ARG   B 134 ? 0.9341 1.0674 1.0417 -0.0128 -0.1353 -0.0213 134  ARG   B CD  
3645  N  NE  . ARG   B 134 ? 1.0206 1.1507 1.1244 -0.0115 -0.1356 -0.0199 134  ARG   B NE  
3646  C  CZ  . ARG   B 134 ? 0.9949 1.1266 1.0937 -0.0112 -0.1316 -0.0161 134  ARG   B CZ  
3647  N  NH1 . ARG   B 134 ? 0.9881 1.1248 1.0856 -0.0126 -0.1270 -0.0132 134  ARG   B NH1 
3648  N  NH2 . ARG   B 134 ? 0.9074 1.0355 1.0027 -0.0094 -0.1325 -0.0152 134  ARG   B NH2 
3649  N  N   . LEU   B 135 ? 1.0274 1.1570 1.1579 -0.0160 -0.1475 -0.0319 135  LEU   B N   
3650  C  CA  . LEU   B 135 ? 0.9791 1.1114 1.1189 -0.0214 -0.1457 -0.0311 135  LEU   B CA  
3651  C  C   . LEU   B 135 ? 0.9826 1.1216 1.1247 -0.0263 -0.1387 -0.0272 135  LEU   B C   
3652  O  O   . LEU   B 135 ? 0.9778 1.1177 1.1203 -0.0291 -0.1355 -0.0245 135  LEU   B O   
3653  C  CB  . LEU   B 135 ? 0.9812 1.1138 1.1337 -0.0236 -0.1497 -0.0353 135  LEU   B CB  
3654  C  CG  . LEU   B 135 ? 0.9903 1.1164 1.1413 -0.0185 -0.1578 -0.0400 135  LEU   B CG  
3655  C  CD1 . LEU   B 135 ? 0.9902 1.1185 1.1551 -0.0206 -0.1616 -0.0443 135  LEU   B CD1 
3656  C  CD2 . LEU   B 135 ? 1.0084 1.1280 1.1558 -0.0166 -0.1610 -0.0404 135  LEU   B CD2 
3657  N  N   . TYR   B 136 ? 1.0290 1.1721 1.1716 -0.0271 -0.1365 -0.0269 136  TYR   B N   
3658  C  CA  . TYR   B 136 ? 1.0391 1.1880 1.1844 -0.0317 -0.1305 -0.0238 136  TYR   B CA  
3659  C  C   . TYR   B 136 ? 1.0237 1.1744 1.1603 -0.0301 -0.1274 -0.0212 136  TYR   B C   
3660  O  O   . TYR   B 136 ? 1.0430 1.1917 1.1745 -0.0261 -0.1295 -0.0225 136  TYR   B O   
3661  C  CB  . TYR   B 136 ? 1.0449 1.1974 1.2013 -0.0353 -0.1300 -0.0259 136  TYR   B CB  
3662  C  CG  . TYR   B 136 ? 1.0628 1.2138 1.2297 -0.0370 -0.1330 -0.0287 136  TYR   B CG  
3663  C  CD1 . TYR   B 136 ? 1.0508 1.2009 1.2209 -0.0402 -0.1309 -0.0271 136  TYR   B CD1 
3664  C  CD2 . TYR   B 136 ? 1.0519 1.2021 1.2260 -0.0356 -0.1381 -0.0332 136  TYR   B CD2 
3665  C  CE1 . TYR   B 136 ? 1.0354 1.1840 1.2161 -0.0422 -0.1333 -0.0296 136  TYR   B CE1 
3666  C  CE2 . TYR   B 136 ? 1.0021 1.1512 1.1875 -0.0375 -0.1410 -0.0359 136  TYR   B CE2 
3667  C  CZ  . TYR   B 136 ? 1.0170 1.1654 1.2058 -0.0410 -0.1383 -0.0340 136  TYR   B CZ  
3668  O  OH  . TYR   B 136 ? 1.0871 1.2343 1.2878 -0.0432 -0.1408 -0.0366 136  TYR   B OH  
3669  N  N   . ASP   B 137 ? 1.0206 1.1745 1.1552 -0.0329 -0.1226 -0.0175 137  ASP   B N   
3670  C  CA  . ASP   B 137 ? 1.0519 1.2083 1.1802 -0.0323 -0.1194 -0.0149 137  ASP   B CA  
3671  C  C   . ASP   B 137 ? 1.0216 1.1802 1.1524 -0.0327 -0.1192 -0.0166 137  ASP   B C   
3672  O  O   . ASP   B 137 ? 0.9740 1.1350 1.1126 -0.0360 -0.1185 -0.0179 137  ASP   B O   
3673  C  CB  . ASP   B 137 ? 1.0335 1.1935 1.1616 -0.0360 -0.1149 -0.0113 137  ASP   B CB  
3674  C  CG  . ASP   B 137 ? 1.1441 1.3021 1.2674 -0.0346 -0.1148 -0.0090 137  ASP   B CG  
3675  O  OD1 . ASP   B 137 ? 1.1484 1.3026 1.2670 -0.0304 -0.1175 -0.0097 137  ASP   B OD1 
3676  O  OD2 . ASP   B 137 ? 1.2083 1.3682 1.3318 -0.0375 -0.1120 -0.0065 137  ASP   B OD2 
3677  N  N   . GLY   B 138 ? 1.0694 1.2266 1.1936 -0.0291 -0.1197 -0.0166 138  GLY   B N   
3678  C  CA  . GLY   B 138 ? 1.0599 1.2186 1.1848 -0.0291 -0.1192 -0.0178 138  GLY   B CA  
3679  C  C   . GLY   B 138 ? 1.0551 1.2107 1.1819 -0.0259 -0.1240 -0.0219 138  GLY   B C   
3680  O  O   . GLY   B 138 ? 1.1011 1.2572 1.2272 -0.0250 -0.1239 -0.0230 138  GLY   B O   
3681  N  N   . LEU   B 139 ? 1.0816 1.2337 1.2107 -0.0241 -0.1284 -0.0244 139  LEU   B N   
3682  C  CA  . LEU   B 139 ? 1.0621 1.2109 1.1938 -0.0210 -0.1338 -0.0288 139  LEU   B CA  
3683  C  C   . LEU   B 139 ? 1.0695 1.2112 1.1936 -0.0153 -0.1384 -0.0303 139  LEU   B C   
3684  O  O   . LEU   B 139 ? 1.0592 1.1990 1.1775 -0.0143 -0.1372 -0.0279 139  LEU   B O   
3685  C  CB  . LEU   B 139 ? 1.0501 1.2017 1.1949 -0.0247 -0.1355 -0.0314 139  LEU   B CB  
3686  C  CG  . LEU   B 139 ? 1.0110 1.1683 1.1632 -0.0289 -0.1320 -0.0312 139  LEU   B CG  
3687  C  CD1 . LEU   B 139 ? 0.9710 1.1308 1.1363 -0.0328 -0.1324 -0.0329 139  LEU   B CD1 
3688  C  CD2 . LEU   B 139 ? 1.0371 1.1936 1.1873 -0.0256 -0.1343 -0.0336 139  LEU   B CD2 
3689  N  N   . PHE   B 140 ? 0.9740 1.1116 1.0978 -0.0114 -0.1440 -0.0343 140  PHE   B N   
3690  C  CA  . PHE   B 140 ? 0.8994 1.0289 1.0151 -0.0053 -0.1492 -0.0364 140  PHE   B CA  
3691  C  C   . PHE   B 140 ? 0.9990 1.1258 1.1208 -0.0033 -0.1563 -0.0417 140  PHE   B C   
3692  O  O   . PHE   B 140 ? 1.0548 1.1813 1.1761 -0.0013 -0.1578 -0.0437 140  PHE   B O   
3693  C  CB  . PHE   B 140 ? 0.9962 1.1212 1.0981 0.0000  -0.1475 -0.0345 140  PHE   B CB  
3694  C  CG  . PHE   B 140 ? 1.0603 1.1762 1.1516 0.0067  -0.1517 -0.0358 140  PHE   B CG  
3695  C  CD1 . PHE   B 140 ? 1.0186 1.1324 1.1064 0.0072  -0.1508 -0.0339 140  PHE   B CD1 
3696  C  CD2 . PHE   B 140 ? 1.0562 1.1649 1.1401 0.0129  -0.1564 -0.0390 140  PHE   B CD2 
3697  C  CE1 . PHE   B 140 ? 0.9584 1.0631 1.0354 0.0138  -0.1545 -0.0350 140  PHE   B CE1 
3698  C  CE2 . PHE   B 140 ? 1.0134 1.1125 1.0861 0.0196  -0.1602 -0.0402 140  PHE   B CE2 
3699  C  CZ  . PHE   B 140 ? 0.9567 1.0539 1.0261 0.0200  -0.1591 -0.0381 140  PHE   B CZ  
3700  N  N   . LYS   B 141 ? 1.0156 1.1403 1.1437 -0.0038 -0.1608 -0.0443 141  LYS   B N   
3701  C  CA  . LYS   B 141 ? 0.9759 1.0983 1.1114 -0.0020 -0.1682 -0.0497 141  LYS   B CA  
3702  C  C   . LYS   B 141 ? 0.9751 1.0878 1.0984 0.0060  -0.1745 -0.0525 141  LYS   B C   
3703  O  O   . LYS   B 141 ? 0.9377 1.0446 1.0487 0.0098  -0.1738 -0.0505 141  LYS   B O   
3704  C  CB  . LYS   B 141 ? 0.8982 1.0219 1.0463 -0.0059 -0.1709 -0.0516 141  LYS   B CB  
3705  C  CG  . LYS   B 141 ? 0.9249 1.0570 1.0895 -0.0124 -0.1683 -0.0520 141  LYS   B CG  
3706  C  CD  . LYS   B 141 ? 0.9698 1.1013 1.1476 -0.0145 -0.1733 -0.0556 141  LYS   B CD  
3707  C  CE  . LYS   B 141 ? 0.9901 1.1297 1.1846 -0.0211 -0.1695 -0.0555 141  LYS   B CE  
3708  N  NZ  . LYS   B 141 ? 0.9738 1.1141 1.1825 -0.0210 -0.1760 -0.0610 141  LYS   B NZ  
3709  N  N   . VAL   B 142 ? 0.9977 1.1082 1.1241 0.0089  -0.1805 -0.0570 142  VAL   B N   
3710  C  CA  . VAL   B 142 ? 1.0214 1.1221 1.1353 0.0170  -0.1866 -0.0599 142  VAL   B CA  
3711  C  C   . VAL   B 142 ? 1.0782 1.1764 1.2018 0.0184  -0.1961 -0.0661 142  VAL   B C   
3712  O  O   . VAL   B 142 ? 1.0725 1.1754 1.2071 0.0166  -0.1981 -0.0689 142  VAL   B O   
3713  C  CB  . VAL   B 142 ? 1.0090 1.1088 1.1140 0.0202  -0.1841 -0.0589 142  VAL   B CB  
3714  C  CG1 . VAL   B 142 ? 1.0856 1.1753 1.1808 0.0284  -0.1920 -0.0633 142  VAL   B CG1 
3715  C  CG2 . VAL   B 142 ? 0.9908 1.0906 1.0841 0.0203  -0.1760 -0.0532 142  VAL   B CG2 
3716  N  N   . ILE   B 143 ? 1.0790 1.1699 1.1991 0.0216  -0.2019 -0.0684 143  ILE   B N   
3717  C  CA  . ILE   B 143 ? 1.0686 1.1553 1.1961 0.0239  -0.2120 -0.0747 143  ILE   B CA  
3718  C  C   . ILE   B 143 ? 1.1288 1.2046 1.2407 0.0332  -0.2184 -0.0777 143  ILE   B C   
3719  O  O   . ILE   B 143 ? 1.1629 1.2292 1.2595 0.0387  -0.2199 -0.0771 143  ILE   B O   
3720  C  CB  . ILE   B 143 ? 1.1167 1.2003 1.2482 0.0226  -0.2154 -0.0758 143  ILE   B CB  
3721  C  CG1 . ILE   B 143 ? 1.0947 1.1881 1.2415 0.0136  -0.2092 -0.0729 143  ILE   B CG1 
3722  C  CG2 . ILE   B 143 ? 1.1250 1.2027 1.2626 0.0260  -0.2269 -0.0827 143  ILE   B CG2 
3723  C  CD1 . ILE   B 143 ? 1.1038 1.1934 1.2543 0.0124  -0.2126 -0.0740 143  ILE   B CD1 
3724  N  N   . PRO   B 144 ? 1.1630 1.2393 1.2773 0.0354  -0.2219 -0.0808 144  PRO   B N   
3725  C  CA  . PRO   B 144 ? 1.1906 1.2554 1.2888 0.0448  -0.2281 -0.0838 144  PRO   B CA  
3726  C  C   . PRO   B 144 ? 1.2196 1.2749 1.3163 0.0496  -0.2389 -0.0892 144  PRO   B C   
3727  O  O   . PRO   B 144 ? 1.1904 1.2496 1.3038 0.0457  -0.2441 -0.0928 144  PRO   B O   
3728  C  CB  . PRO   B 144 ? 1.2551 1.3243 1.3606 0.0448  -0.2299 -0.0864 144  PRO   B CB  
3729  C  CG  . PRO   B 144 ? 1.2437 1.3263 1.3630 0.0360  -0.2211 -0.0825 144  PRO   B CG  
3730  C  CD  . PRO   B 144 ? 1.1689 1.2560 1.2985 0.0299  -0.2190 -0.0810 144  PRO   B CD  
3731  N  N   . LEU   B 145 ? 1.2786 1.3210 1.3550 0.0582  -0.2422 -0.0897 145  LEU   B N   
3732  C  CA  . LEU   B 145 ? 1.3075 1.3389 1.3784 0.0638  -0.2520 -0.0943 145  LEU   B CA  
3733  C  C   . LEU   B 145 ? 1.3644 1.3859 1.4287 0.0720  -0.2629 -0.1006 145  LEU   B C   
3734  O  O   . LEU   B 145 ? 1.4229 1.4406 1.4947 0.0734  -0.2733 -0.1064 145  LEU   B O   
3735  C  CB  . LEU   B 145 ? 1.3250 1.3475 1.3769 0.0680  -0.2481 -0.0905 145  LEU   B CB  
3736  C  CG  . LEU   B 145 ? 1.2556 1.2851 1.3156 0.0609  -0.2418 -0.0864 145  LEU   B CG  
3737  C  CD1 . LEU   B 145 ? 1.2552 1.2737 1.2983 0.0665  -0.2420 -0.0850 145  LEU   B CD1 
3738  C  CD2 . LEU   B 145 ? 1.1469 1.1830 1.2287 0.0544  -0.2469 -0.0901 145  LEU   B CD2 
3739  N  N   . ASP   B 146 ? 1.4217 1.4384 1.4718 0.0776  -0.2611 -0.0996 146  ASP   B N   
3740  C  CA  . ASP   B 146 ? 1.4031 1.4108 1.4468 0.0855  -0.2711 -0.1055 146  ASP   B CA  
3741  C  C   . ASP   B 146 ? 1.4023 1.4185 1.4692 0.0811  -0.2785 -0.1110 146  ASP   B C   
3742  O  O   . ASP   B 146 ? 1.4038 1.4326 1.4854 0.0745  -0.2731 -0.1093 146  ASP   B O   
3743  C  CB  . ASP   B 146 ? 1.4210 1.4259 1.4500 0.0897  -0.2654 -0.1025 146  ASP   B CB  
3744  C  CG  . ASP   B 146 ? 1.5062 1.5239 1.5417 0.0817  -0.2521 -0.0957 146  ASP   B CG  
3745  O  OD1 . ASP   B 146 ? 1.4516 1.4785 1.4987 0.0740  -0.2467 -0.0927 146  ASP   B OD1 
3746  O  OD2 . ASP   B 146 ? 1.5635 1.5817 1.5921 0.0832  -0.2472 -0.0935 146  ASP   B OD2 
3747  N  N   . ARG   B 147 ? 1.4327 1.4417 1.5028 0.0851  -0.2910 -0.1177 147  ARG   B N   
3748  C  CA  . ARG   B 147 ? 1.4262 1.4430 1.5206 0.0808  -0.2989 -0.1234 147  ARG   B CA  
3749  C  C   . ARG   B 147 ? 1.4049 1.4307 1.5180 0.0717  -0.2963 -0.1222 147  ARG   B C   
3750  O  O   . ARG   B 147 ? 1.3926 1.4272 1.5093 0.0649  -0.2850 -0.1160 147  ARG   B O   
3751  C  CB  . ARG   B 147 ? 1.4238 1.4514 1.5304 0.0774  -0.2957 -0.1232 147  ARG   B CB  
3752  N  N   . ASP   B 148 ? 1.5562 1.5793 1.6807 0.0718  -0.3068 -0.1280 148  ASP   B N   
3753  C  CA  . ASP   B 148 ? 1.4869 1.5162 1.6277 0.0640  -0.3053 -0.1273 148  ASP   B CA  
3754  C  C   . ASP   B 148 ? 1.4729 1.5189 1.6341 0.0534  -0.2951 -0.1232 148  ASP   B C   
3755  O  O   . ASP   B 148 ? 1.4984 1.5530 1.6789 0.0499  -0.2976 -0.1263 148  ASP   B O   
3756  C  CB  . ASP   B 148 ? 1.5117 1.5374 1.6664 0.0651  -0.3190 -0.1351 148  ASP   B CB  
3757  C  CG  . ASP   B 148 ? 1.5635 1.5972 1.7372 0.0634  -0.3240 -0.1396 148  ASP   B CG  
3758  O  OD1 . ASP   B 148 ? 1.6115 1.6457 1.7767 0.0670  -0.3216 -0.1386 148  ASP   B OD1 
3759  O  OD2 . ASP   B 148 ? 1.6332 1.6734 1.8307 0.0583  -0.3293 -0.1437 148  ASP   B OD2 
3760  N  N   . ASN   B 149 ? 1.2826 1.3331 1.4401 0.0485  -0.2838 -0.1165 149  ASN   B N   
3761  C  CA  . ASN   B 149 ? 1.2045 1.2698 1.3799 0.0388  -0.2741 -0.1126 149  ASN   B CA  
3762  C  C   . ASN   B 149 ? 1.2025 1.2726 1.3963 0.0316  -0.2744 -0.1132 149  ASN   B C   
3763  O  O   . ASN   B 149 ? 1.1713 1.2476 1.3688 0.0252  -0.2651 -0.1080 149  ASN   B O   
3764  C  CB  . ASN   B 149 ? 1.1201 1.1884 1.2822 0.0372  -0.2616 -0.1050 149  ASN   B CB  
3765  C  CG  . ASN   B 149 ? 1.0799 1.1622 1.2574 0.0288  -0.2522 -0.1014 149  ASN   B CG  
3766  O  OD1 . ASN   B 149 ? 1.0590 1.1490 1.2572 0.0242  -0.2543 -0.1042 149  ASN   B OD1 
3767  N  ND2 . ASN   B 149 ? 1.1203 1.2058 1.2880 0.0269  -0.2417 -0.0950 149  ASN   B ND2 
3768  N  N   . LYS   B 150 ? 1.1676 1.2347 1.3735 0.0328  -0.2856 -0.1198 150  LYS   B N   
3769  C  CA  . LYS   B 150 ? 1.1169 1.1868 1.3409 0.0267  -0.2877 -0.1215 150  LYS   B CA  
3770  C  C   . LYS   B 150 ? 1.1577 1.2402 1.3968 0.0167  -0.2759 -0.1161 150  LYS   B C   
3771  O  O   . LYS   B 150 ? 1.2501 1.3328 1.4947 0.0121  -0.2734 -0.1144 150  LYS   B O   
3772  C  CB  . LYS   B 150 ? 1.0993 1.1694 1.3419 0.0274  -0.2999 -0.1294 150  LYS   B CB  
3773  N  N   . GLU   B 151 ? 1.0900 1.1824 1.3352 0.0134  -0.2684 -0.1134 151  GLU   B N   
3774  C  CA  . GLU   B 151 ? 1.1041 1.2075 1.3622 0.0044  -0.2571 -0.1082 151  GLU   B CA  
3775  C  C   . GLU   B 151 ? 1.1203 1.2246 1.3614 0.0037  -0.2460 -0.1009 151  GLU   B C   
3776  O  O   . GLU   B 151 ? 1.1002 1.2131 1.3493 -0.0032 -0.2363 -0.0964 151  GLU   B O   
3777  C  CB  . GLU   B 151 ? 1.1541 1.2685 1.4320 0.0002  -0.2550 -0.1095 151  GLU   B CB  
3778  C  CG  . GLU   B 151 ? 1.2360 1.3512 1.5337 0.0003  -0.2654 -0.1166 151  GLU   B CG  
3779  C  CD  . GLU   B 151 ? 1.4523 1.5800 1.7765 -0.0073 -0.2608 -0.1167 151  GLU   B CD  
3780  O  OE1 . GLU   B 151 ? 1.5118 1.6477 1.8376 -0.0108 -0.2508 -0.1123 151  GLU   B OE1 
3781  O  OE2 . GLU   B 151 ? 1.4964 1.6254 1.8403 -0.0097 -0.2673 -0.1214 151  GLU   B OE2 
3782  N  N   . LEU   B 152 ? 1.1061 1.2017 1.3244 0.0107  -0.2473 -0.0998 152  LEU   B N   
3783  C  CA  . LEU   B 152 ? 1.0717 1.1677 1.2739 0.0105  -0.2374 -0.0932 152  LEU   B CA  
3784  C  C   . LEU   B 152 ? 1.0523 1.1583 1.2593 0.0065  -0.2287 -0.0897 152  LEU   B C   
3785  O  O   . LEU   B 152 ? 1.0238 1.1350 1.2289 0.0019  -0.2190 -0.0841 152  LEU   B O   
3786  C  CB  . LEU   B 152 ? 1.0852 1.1808 1.2868 0.0063  -0.2324 -0.0894 152  LEU   B CB  
3787  C  CG  . LEU   B 152 ? 1.1419 1.2270 1.3372 0.0100  -0.2400 -0.0922 152  LEU   B CG  
3788  C  CD1 . LEU   B 152 ? 1.0929 1.1795 1.2909 0.0046  -0.2340 -0.0881 152  LEU   B CD1 
3789  C  CD2 . LEU   B 152 ? 1.1264 1.2004 1.2980 0.0191  -0.2434 -0.0923 152  LEU   B CD2 
3790  N  N   . LYS   B 153 ? 1.0356 1.1441 1.2487 0.0084  -0.2326 -0.0932 153  LYS   B N   
3791  C  CA  . LYS   B 153 ? 1.0238 1.1396 1.2374 0.0065  -0.2254 -0.0903 153  LYS   B CA  
3792  C  C   . LYS   B 153 ? 1.0079 1.1209 1.2010 0.0087  -0.2182 -0.0847 153  LYS   B C   
3793  O  O   . LYS   B 153 ? 1.0595 1.1631 1.2352 0.0155  -0.2218 -0.0852 153  LYS   B O   
3794  C  CB  . LYS   B 153 ? 0.9056 1.0208 1.1226 0.0110  -0.2326 -0.0954 153  LYS   B CB  
3795  N  N   . ALA   B 154 ? 0.9652 1.0858 1.1603 0.0031  -0.2081 -0.0794 154  ALA   B N   
3796  C  CA  . ALA   B 154 ? 1.0345 1.1533 1.2123 0.0043  -0.2009 -0.0740 154  ALA   B CA  
3797  C  C   . ALA   B 154 ? 1.0467 1.1725 1.2251 0.0017  -0.1937 -0.0710 154  ALA   B C   
3798  O  O   . ALA   B 154 ? 1.0275 1.1603 1.2201 -0.0020 -0.1928 -0.0724 154  ALA   B O   
3799  C  CB  . ALA   B 154 ? 1.0020 1.1216 1.1782 0.0003  -0.1954 -0.0697 154  ALA   B CB  
3800  N  N   . PHE   B 155 ? 1.0102 1.1339 1.1732 0.0036  -0.1883 -0.0668 155  PHE   B N   
3801  C  CA  . PHE   B 155 ? 0.9895 1.1195 1.1522 0.0006  -0.1809 -0.0634 155  PHE   B CA  
3802  C  C   . PHE   B 155 ? 1.0180 1.1485 1.1707 -0.0014 -0.1731 -0.0576 155  PHE   B C   
3803  O  O   . PHE   B 155 ? 1.0202 1.1447 1.1616 0.0020  -0.1739 -0.0563 155  PHE   B O   
3804  C  CB  . PHE   B 155 ? 0.9959 1.1228 1.1512 0.0058  -0.1834 -0.0654 155  PHE   B CB  
3805  C  CG  . PHE   B 155 ? 0.9680 1.0854 1.1039 0.0129  -0.1849 -0.0646 155  PHE   B CG  
3806  C  CD1 . PHE   B 155 ? 0.9858 1.1028 1.1097 0.0129  -0.1777 -0.0596 155  PHE   B CD1 
3807  C  CD2 . PHE   B 155 ? 1.0829 1.1914 1.2126 0.0198  -0.1936 -0.0691 155  PHE   B CD2 
3808  C  CE1 . PHE   B 155 ? 1.0185 1.1267 1.1251 0.0194  -0.1782 -0.0587 155  PHE   B CE1 
3809  C  CE2 . PHE   B 155 ? 1.1276 1.2264 1.2384 0.0268  -0.1944 -0.0683 155  PHE   B CE2 
3810  C  CZ  . PHE   B 155 ? 1.1378 1.2366 1.2374 0.0266  -0.1864 -0.0629 155  PHE   B CZ  
3811  N  N   . ASN   B 156 ? 0.9456 1.0836 1.1029 -0.0067 -0.1657 -0.0541 156  ASN   B N   
3812  C  CA  . ASN   B 156 ? 0.9250 1.0653 1.0767 -0.0100 -0.1584 -0.0487 156  ASN   B CA  
3813  C  C   . ASN   B 156 ? 0.9325 1.0731 1.0738 -0.0087 -0.1536 -0.0457 156  ASN   B C   
3814  O  O   . ASN   B 156 ? 1.0853 1.2314 1.2313 -0.0122 -0.1495 -0.0445 156  ASN   B O   
3815  C  CB  . ASN   B 156 ? 0.9893 1.1371 1.1537 -0.0172 -0.1536 -0.0470 156  ASN   B CB  
3816  C  CG  . ASN   B 156 ? 1.0263 1.1733 1.1932 -0.0194 -0.1534 -0.0458 156  ASN   B CG  
3817  O  OD1 . ASN   B 156 ? 1.0309 1.1730 1.1875 -0.0166 -0.1540 -0.0443 156  ASN   B OD1 
3818  N  ND2 . ASN   B 156 ? 1.0684 1.2197 1.2488 -0.0245 -0.1521 -0.0463 156  ASN   B ND2 
3819  N  N   . ILE   B 157 ? 0.9994 1.1340 1.1266 -0.0039 -0.1537 -0.0442 157  ILE   B N   
3820  C  CA  . ILE   B 157 ? 1.0011 1.1357 1.1188 -0.0031 -0.1485 -0.0409 157  ILE   B CA  
3821  C  C   . ILE   B 157 ? 1.0769 1.2172 1.1959 -0.0085 -0.1415 -0.0361 157  ILE   B C   
3822  O  O   . ILE   B 157 ? 1.0693 1.2094 1.1877 -0.0096 -0.1405 -0.0343 157  ILE   B O   
3823  C  CB  . ILE   B 157 ? 1.0548 1.1808 1.1574 0.0039  -0.1501 -0.0405 157  ILE   B CB  
3824  C  CG1 . ILE   B 157 ? 1.0665 1.1856 1.1668 0.0097  -0.1580 -0.0456 157  ILE   B CG1 
3825  C  CG2 . ILE   B 157 ? 1.0865 1.2122 1.1801 0.0047  -0.1447 -0.0372 157  ILE   B CG2 
3826  C  CD1 . ILE   B 157 ? 1.0850 1.1941 1.1690 0.0173  -0.1597 -0.0454 157  ILE   B CD1 
3827  N  N   . ARG   B 158 ? 1.0770 1.2221 1.1978 -0.0117 -0.1368 -0.0343 158  ARG   B N   
3828  C  CA  . ARG   B 158 ? 1.0530 1.2028 1.1736 -0.0163 -0.1305 -0.0299 158  ARG   B CA  
3829  C  C   . ARG   B 158 ? 1.0920 1.2383 1.2013 -0.0134 -0.1282 -0.0267 158  ARG   B C   
3830  O  O   . ARG   B 158 ? 1.1007 1.2414 1.2011 -0.0082 -0.1297 -0.0273 158  ARG   B O   
3831  C  CB  . ARG   B 158 ? 1.1906 1.3449 1.3140 -0.0194 -0.1268 -0.0290 158  ARG   B CB  
3832  C  CG  . ARG   B 158 ? 1.3058 1.4647 1.4292 -0.0242 -0.1208 -0.0249 158  ARG   B CG  
3833  C  CD  . ARG   B 158 ? 1.3592 1.5224 1.4877 -0.0278 -0.1180 -0.0250 158  ARG   B CD  
3834  N  NE  . ARG   B 158 ? 1.4601 1.6241 1.5972 -0.0276 -0.1213 -0.0288 158  ARG   B NE  
3835  C  CZ  . ARG   B 158 ? 1.3785 1.5435 1.5241 -0.0288 -0.1237 -0.0307 158  ARG   B CZ  
3836  N  NH1 . ARG   B 158 ? 1.3685 1.5334 1.5145 -0.0303 -0.1232 -0.0291 158  ARG   B NH1 
3837  N  NH2 . ARG   B 158 ? 1.2612 1.4271 1.4153 -0.0284 -0.1270 -0.0344 158  ARG   B NH2 
3838  N  N   . LEU   B 159 ? 1.1447 1.2942 1.2543 -0.0166 -0.1244 -0.0233 159  LEU   B N   
3839  C  CA  . LEU   B 159 ? 1.1562 1.3037 1.2572 -0.0144 -0.1217 -0.0200 159  LEU   B CA  
3840  C  C   . LEU   B 159 ? 1.1932 1.3465 1.2965 -0.0194 -0.1164 -0.0162 159  LEU   B C   
3841  O  O   . LEU   B 159 ? 1.1801 1.3372 1.2900 -0.0236 -0.1157 -0.0157 159  LEU   B O   
3842  C  CB  . LEU   B 159 ? 1.1393 1.2828 1.2377 -0.0116 -0.1245 -0.0204 159  LEU   B CB  
3843  C  CG  . LEU   B 159 ? 1.1504 1.2917 1.2407 -0.0090 -0.1218 -0.0170 159  LEU   B CG  
3844  C  CD1 . LEU   B 159 ? 1.1741 1.3101 1.2546 -0.0037 -0.1212 -0.0167 159  LEU   B CD1 
3845  C  CD2 . LEU   B 159 ? 1.0740 1.2119 1.1631 -0.0069 -0.1247 -0.0176 159  LEU   B CD2 
3846  N  N   . GLU   B 160 ? 1.2822 1.4358 1.3801 -0.0189 -0.1128 -0.0136 160  GLU   B N   
3847  C  CA  . GLU   B 160 ? 1.2807 1.4399 1.3815 -0.0238 -0.1085 -0.0106 160  GLU   B CA  
3848  C  C   . GLU   B 160 ? 1.2275 1.3884 1.3279 -0.0247 -0.1069 -0.0078 160  GLU   B C   
3849  O  O   . GLU   B 160 ? 1.2124 1.3777 1.3169 -0.0291 -0.1049 -0.0061 160  GLU   B O   
3850  C  CB  . GLU   B 160 ? 1.3065 1.4655 1.4029 -0.0233 -0.1055 -0.0091 160  GLU   B CB  
3851  C  CG  . GLU   B 160 ? 1.3902 1.5477 1.4869 -0.0225 -0.1069 -0.0118 160  GLU   B CG  
3852  C  CD  . GLU   B 160 ? 1.6138 1.7713 1.7070 -0.0229 -0.1036 -0.0101 160  GLU   B CD  
3853  O  OE1 . GLU   B 160 ? 1.6222 1.7773 1.7094 -0.0204 -0.1014 -0.0079 160  GLU   B OE1 
3854  O  OE2 . GLU   B 160 ? 1.7713 1.9311 1.8677 -0.0258 -0.1029 -0.0109 160  GLU   B OE2 
3855  N  N   . GLU   B 161 ? 1.1604 1.3175 1.2555 -0.0204 -0.1077 -0.0072 161  GLU   B N   
3856  C  CA  . GLU   B 161 ? 1.1328 1.2910 1.2273 -0.0205 -0.1066 -0.0047 161  GLU   B CA  
3857  C  C   . GLU   B 161 ? 1.1260 1.2846 1.2254 -0.0225 -0.1093 -0.0062 161  GLU   B C   
3858  O  O   . GLU   B 161 ? 1.1318 1.2864 1.2311 -0.0200 -0.1130 -0.0089 161  GLU   B O   
3859  C  CB  . GLU   B 161 ? 1.1074 1.2605 1.1942 -0.0148 -0.1066 -0.0039 161  GLU   B CB  
3860  C  CG  . GLU   B 161 ? 1.1271 1.2798 1.2093 -0.0130 -0.1027 -0.0016 161  GLU   B CG  
3861  C  CD  . GLU   B 161 ? 1.2211 1.3709 1.3006 -0.0116 -0.1032 -0.0035 161  GLU   B CD  
3862  O  OE1 . GLU   B 161 ? 1.2127 1.3595 1.2924 -0.0103 -0.1072 -0.0070 161  GLU   B OE1 
3863  O  OE2 . GLU   B 161 ? 1.2683 1.4189 1.3459 -0.0119 -0.0996 -0.0016 161  GLU   B OE2 
3864  N  N   . LEU   B 162 ? 1.1200 1.2830 1.2238 -0.0269 -0.1074 -0.0045 162  LEU   B N   
3865  C  CA  . LEU   B 162 ? 1.1256 1.2890 1.2346 -0.0296 -0.1091 -0.0056 162  LEU   B CA  
3866  C  C   . LEU   B 162 ? 1.1530 1.3152 1.2605 -0.0287 -0.1095 -0.0041 162  LEU   B C   
3867  O  O   . LEU   B 162 ? 1.1793 1.3411 1.2906 -0.0307 -0.1106 -0.0048 162  LEU   B O   
3868  C  CB  . LEU   B 162 ? 1.0713 1.2390 1.1853 -0.0348 -0.1067 -0.0049 162  LEU   B CB  
3869  C  CG  . LEU   B 162 ? 1.0164 1.1859 1.1312 -0.0361 -0.1054 -0.0056 162  LEU   B CG  
3870  C  CD1 . LEU   B 162 ? 0.9085 1.0815 1.0265 -0.0408 -0.1028 -0.0044 162  LEU   B CD1 
3871  C  CD2 . LEU   B 162 ? 1.0479 1.2153 1.1656 -0.0349 -0.1081 -0.0092 162  LEU   B CD2 
3872  N  N   . HIS   B 163 ? 1.1192 1.2808 1.2216 -0.0257 -0.1083 -0.0019 163  HIS   B N   
3873  C  CA  . HIS   B 163 ? 1.0988 1.2586 1.1990 -0.0238 -0.1090 -0.0007 163  HIS   B CA  
3874  C  C   . HIS   B 163 ? 1.0999 1.2550 1.1933 -0.0179 -0.1098 -0.0008 163  HIS   B C   
3875  O  O   . HIS   B 163 ? 1.1135 1.2696 1.2034 -0.0159 -0.1072 0.0017  163  HIS   B O   
3876  C  CB  . HIS   B 163 ? 1.0982 1.2622 1.1991 -0.0261 -0.1062 0.0026  163  HIS   B CB  
3877  C  CG  . HIS   B 163 ? 1.2142 1.3825 1.3195 -0.0312 -0.1046 0.0032  163  HIS   B CG  
3878  N  ND1 . HIS   B 163 ? 1.2457 1.4160 1.3526 -0.0330 -0.1034 0.0025  163  HIS   B ND1 
3879  C  CD2 . HIS   B 163 ? 1.2895 1.4597 1.3972 -0.0346 -0.1038 0.0044  163  HIS   B CD2 
3880  C  CE1 . HIS   B 163 ? 1.2337 1.4069 1.3436 -0.0373 -0.1021 0.0032  163  HIS   B CE1 
3881  N  NE2 . HIS   B 163 ? 1.3067 1.4798 1.4170 -0.0383 -0.1023 0.0044  163  HIS   B NE2 
3882  N  N   . VAL   B 164 ? 0.9987 1.1485 1.0902 -0.0149 -0.1135 -0.0039 164  VAL   B N   
3883  C  CA  . VAL   B 164 ? 0.9949 1.1387 1.0786 -0.0087 -0.1148 -0.0043 164  VAL   B CA  
3884  C  C   . VAL   B 164 ? 0.9904 1.1310 1.0722 -0.0068 -0.1165 -0.0040 164  VAL   B C   
3885  O  O   . VAL   B 164 ? 0.9174 1.0570 1.0033 -0.0088 -0.1194 -0.0059 164  VAL   B O   
3886  C  CB  . VAL   B 164 ? 1.0457 1.1844 1.1274 -0.0059 -0.1186 -0.0081 164  VAL   B CB  
3887  C  CG1 . VAL   B 164 ? 1.0326 1.1750 1.1183 -0.0090 -0.1174 -0.0088 164  VAL   B CG1 
3888  C  CG2 . VAL   B 164 ? 1.0483 1.1840 1.1338 -0.0064 -0.1235 -0.0113 164  VAL   B CG2 
3889  N  N   . ILE   B 165 ? 1.0079 1.1469 1.0837 -0.0029 -0.1145 -0.0016 165  ILE   B N   
3890  C  CA  . ILE   B 165 ? 0.9553 1.0910 1.0283 -0.0005 -0.1158 -0.0010 165  ILE   B CA  
3891  C  C   . ILE   B 165 ? 0.9574 1.0845 1.0249 0.0043  -0.1205 -0.0043 165  ILE   B C   
3892  O  O   . ILE   B 165 ? 1.0296 1.1541 1.0996 0.0033  -0.1242 -0.0064 165  ILE   B O   
3893  C  CB  . ILE   B 165 ? 0.9398 1.0773 1.0091 0.0021  -0.1117 0.0028  165  ILE   B CB  
3894  C  CG1 . ILE   B 165 ? 0.9617 1.1071 1.0360 -0.0020 -0.1075 0.0054  165  ILE   B CG1 
3895  C  CG2 . ILE   B 165 ? 0.9938 1.1302 1.0625 0.0028  -0.1125 0.0039  165  ILE   B CG2 
3896  C  CD1 . ILE   B 165 ? 0.9630 1.1138 1.0449 -0.0083 -0.1077 0.0054  165  ILE   B CD1 
3897  N  N   . ASP   B 166 ? 0.9386 1.0605 0.9982 0.0099  -0.1206 -0.0047 166  ASP   B N   
3898  C  CA  . ASP   B 166 ? 0.8608 0.9732 0.9128 0.0157  -0.1252 -0.0077 166  ASP   B CA  
3899  C  C   . ASP   B 166 ? 0.9871 1.0959 1.0342 0.0189  -0.1257 -0.0094 166  ASP   B C   
3900  O  O   . ASP   B 166 ? 0.9913 1.1033 1.0374 0.0187  -0.1211 -0.0069 166  ASP   B O   
3901  C  CB  . ASP   B 166 ? 0.8913 0.9987 0.9346 0.0214  -0.1238 -0.0057 166  ASP   B CB  
3902  C  CG  . ASP   B 166 ? 0.9779 1.0744 1.0126 0.0275  -0.1292 -0.0089 166  ASP   B CG  
3903  O  OD1 . ASP   B 166 ? 0.9619 1.0550 0.9987 0.0270  -0.1348 -0.0131 166  ASP   B OD1 
3904  O  OD2 . ASP   B 166 ? 1.0100 1.1013 1.0359 0.0332  -0.1277 -0.0073 166  ASP   B OD2 
3905  N  N   . VAL   B 167 ? 0.9856 1.0871 1.0294 0.0222  -0.1316 -0.0135 167  VAL   B N   
3906  C  CA  . VAL   B 167 ? 0.9656 1.0630 1.0047 0.0253  -0.1332 -0.0157 167  VAL   B CA  
3907  C  C   . VAL   B 167 ? 0.9671 1.0533 0.9970 0.0322  -0.1393 -0.0193 167  VAL   B C   
3908  O  O   . VAL   B 167 ? 1.0253 1.1090 1.0588 0.0316  -0.1449 -0.0225 167  VAL   B O   
3909  C  CB  . VAL   B 167 ? 0.9577 1.0607 1.0071 0.0198  -0.1351 -0.0181 167  VAL   B CB  
3910  C  CG1 . VAL   B 167 ? 0.8812 0.9845 0.9388 0.0167  -0.1404 -0.0213 167  VAL   B CG1 
3911  C  CG2 . VAL   B 167 ? 0.8959 0.9937 0.9399 0.0238  -0.1377 -0.0208 167  VAL   B CG2 
3912  N  N   . LYS   B 168 ? 1.0037 1.0826 1.0219 0.0388  -0.1384 -0.0191 168  LYS   B N   
3913  C  CA  . LYS   B 168 ? 1.0187 1.0857 1.0264 0.0461  -0.1445 -0.0228 168  LYS   B CA  
3914  C  C   . LYS   B 168 ? 1.0458 1.1077 1.0462 0.0502  -0.1452 -0.0243 168  LYS   B C   
3915  O  O   . LYS   B 168 ? 1.0159 1.0815 1.0155 0.0493  -0.1392 -0.0212 168  LYS   B O   
3916  C  CB  . LYS   B 168 ? 0.9727 1.0322 0.9687 0.0524  -0.1427 -0.0206 168  LYS   B CB  
3917  C  CG  . LYS   B 168 ? 1.0045 1.0682 1.0064 0.0490  -0.1421 -0.0191 168  LYS   B CG  
3918  C  CD  . LYS   B 168 ? 1.0401 1.0932 1.0325 0.0552  -0.1467 -0.0210 168  LYS   B CD  
3919  C  CE  . LYS   B 168 ? 1.0799 1.1361 1.0807 0.0508  -0.1493 -0.0217 168  LYS   B CE  
3920  N  NZ  . LYS   B 168 ? 1.0970 1.1615 1.1024 0.0471  -0.1425 -0.0167 168  LYS   B NZ  
3921  N  N   . PHE   B 169 ? 1.0392 1.0923 1.0346 0.0548  -0.1529 -0.0291 169  PHE   B N   
3922  C  CA  . PHE   B 169 ? 1.0578 1.1034 1.0429 0.0606  -0.1539 -0.0306 169  PHE   B CA  
3923  C  C   . PHE   B 169 ? 1.0994 1.1360 1.0680 0.0682  -0.1491 -0.0273 169  PHE   B C   
3924  O  O   . PHE   B 169 ? 1.1486 1.1810 1.1117 0.0712  -0.1486 -0.0261 169  PHE   B O   
3925  C  CB  . PHE   B 169 ? 1.0730 1.1106 1.0561 0.0644  -0.1641 -0.0368 169  PHE   B CB  
3926  C  CG  . PHE   B 169 ? 1.0996 1.1453 1.0980 0.0580  -0.1681 -0.0401 169  PHE   B CG  
3927  C  CD1 . PHE   B 169 ? 1.1671 1.2148 1.1667 0.0575  -0.1673 -0.0408 169  PHE   B CD1 
3928  C  CD2 . PHE   B 169 ? 1.0802 1.1310 1.0918 0.0527  -0.1724 -0.0425 169  PHE   B CD2 
3929  C  CE1 . PHE   B 169 ? 1.1199 1.1751 1.1337 0.0519  -0.1707 -0.0438 169  PHE   B CE1 
3930  C  CE2 . PHE   B 169 ? 1.0612 1.1192 1.0872 0.0470  -0.1754 -0.0453 169  PHE   B CE2 
3931  C  CZ  . PHE   B 169 ? 1.0872 1.1477 1.1144 0.0467  -0.1746 -0.0460 169  PHE   B CZ  
3932  N  N   . LEU   B 170 ? 1.0944 1.1280 1.0552 0.0714  -0.1450 -0.0257 170  LEU   B N   
3933  C  CA  . LEU   B 170 ? 1.1139 1.1388 1.0593 0.0787  -0.1393 -0.0222 170  LEU   B CA  
3934  C  C   . LEU   B 170 ? 1.1932 1.2023 1.1219 0.0884  -0.1451 -0.0258 170  LEU   B C   
3935  O  O   . LEU   B 170 ? 1.1899 1.1957 1.1192 0.0894  -0.1525 -0.0306 170  LEU   B O   
3936  C  CB  . LEU   B 170 ? 1.1283 1.1578 1.0739 0.0768  -0.1306 -0.0179 170  LEU   B CB  
3937  C  CG  . LEU   B 170 ? 1.1084 1.1515 1.0667 0.0690  -0.1232 -0.0132 170  LEU   B CG  
3938  C  CD1 . LEU   B 170 ? 1.1403 1.1841 1.0951 0.0695  -0.1153 -0.0094 170  LEU   B CD1 
3939  C  CD2 . LEU   B 170 ? 1.1093 1.1536 1.0673 0.0696  -0.1202 -0.0104 170  LEU   B CD2 
3940  N  N   . TYR   B 171 ? 1.2217 1.2208 1.1354 0.0960  -0.1415 -0.0234 171  TYR   B N   
3941  C  CA  . TYR   B 171 ? 1.2409 1.2235 1.1365 0.1061  -0.1466 -0.0265 171  TYR   B CA  
3942  C  C   . TYR   B 171 ? 1.2943 1.2708 1.1787 0.1106  -0.1413 -0.0245 171  TYR   B C   
3943  O  O   . TYR   B 171 ? 1.2903 1.2746 1.1798 0.1066  -0.1325 -0.0199 171  TYR   B O   
3944  C  CB  . TYR   B 171 ? 1.2578 1.2305 1.1408 0.1130  -0.1459 -0.0254 171  TYR   B CB  
3945  C  CG  . TYR   B 171 ? 1.1818 1.1543 1.0701 0.1116  -0.1542 -0.0292 171  TYR   B CG  
3946  C  CD1 . TYR   B 171 ? 1.1823 1.1467 1.0676 0.1148  -0.1654 -0.0356 171  TYR   B CD1 
3947  C  CD2 . TYR   B 171 ? 1.2136 1.1934 1.1097 0.1075  -0.1509 -0.0264 171  TYR   B CD2 
3948  C  CE1 . TYR   B 171 ? 1.1531 1.1168 1.0436 0.1134  -0.1729 -0.0391 171  TYR   B CE1 
3949  C  CE2 . TYR   B 171 ? 1.2173 1.1962 1.1179 0.1063  -0.1582 -0.0298 171  TYR   B CE2 
3950  C  CZ  . TYR   B 171 ? 1.2116 1.1823 1.1096 0.1091  -0.1691 -0.0361 171  TYR   B CZ  
3951  O  OH  . TYR   B 171 ? 1.0992 1.0687 1.0022 0.1077  -0.1764 -0.0395 171  TYR   B OH  
3952  N  N   . GLY   B 172 ? 1.3406 1.3024 1.2094 0.1193  -0.1470 -0.0281 172  GLY   B N   
3953  C  CA  . GLY   B 172 ? 1.4467 1.3981 1.2995 0.1263  -0.1416 -0.0258 172  GLY   B CA  
3954  C  C   . GLY   B 172 ? 1.4923 1.4514 1.3524 0.1212  -0.1371 -0.0242 172  GLY   B C   
3955  O  O   . GLY   B 172 ? 1.5234 1.4807 1.3770 0.1230  -0.1278 -0.0194 172  GLY   B O   
3956  N  N   . CYS   B 173 ? 1.4654 1.4330 1.3391 0.1151  -0.1434 -0.0280 173  CYS   B N   
3957  C  CA  . CYS   B 173 ? 1.4901 1.4659 1.3721 0.1096  -0.1394 -0.0265 173  CYS   B CA  
3958  C  C   . CYS   B 173 ? 1.5620 1.5346 1.4447 0.1109  -0.1489 -0.0325 173  CYS   B C   
3959  O  O   . CYS   B 173 ? 1.5693 1.5391 1.4540 0.1123  -0.1588 -0.0377 173  CYS   B O   
3960  C  CB  . CYS   B 173 ? 1.4381 1.4320 1.3406 0.0983  -0.1349 -0.0238 173  CYS   B CB  
3961  S  SG  . CYS   B 173 ? 1.5189 1.5240 1.4410 0.0903  -0.1445 -0.0290 173  CYS   B SG  
3962  N  N   . GLN   B 174 ? 1.6183 1.5910 1.4994 0.1105  -0.1459 -0.0317 174  GLN   B N   
3963  C  CA  . GLN   B 174 ? 1.5813 1.5473 1.4580 0.1145  -0.1542 -0.0370 174  GLN   B CA  
3964  C  C   . GLN   B 174 ? 1.5174 1.4938 1.4124 0.1079  -0.1629 -0.0419 174  GLN   B C   
3965  O  O   . GLN   B 174 ? 1.4676 1.4380 1.3609 0.1117  -0.1731 -0.0475 174  GLN   B O   
3966  C  CB  . GLN   B 174 ? 1.6709 1.6360 1.5433 0.1147  -0.1483 -0.0346 174  GLN   B CB  
3967  C  CG  . GLN   B 174 ? 1.8219 1.7834 1.6845 0.1166  -0.1363 -0.0279 174  GLN   B CG  
3968  C  CD  . GLN   B 174 ? 1.9371 1.8850 1.7815 0.1244  -0.1332 -0.0269 174  GLN   B CD  
3969  O  OE1 . GLN   B 174 ? 1.8869 1.8245 1.7216 0.1308  -0.1410 -0.0315 174  GLN   B OE1 
3970  N  NE2 . GLN   B 174 ? 1.9677 1.9152 1.8078 0.1241  -0.1217 -0.0208 174  GLN   B NE2 
3971  N  N   . ALA   B 175 ? 1.4461 1.4383 1.3591 0.0978  -0.1587 -0.0400 175  ALA   B N   
3972  C  CA  . ALA   B 175 ? 1.3586 1.3627 1.2910 0.0901  -0.1643 -0.0434 175  ALA   B CA  
3973  C  C   . ALA   B 175 ? 1.2928 1.3066 1.2374 0.0836  -0.1624 -0.0415 175  ALA   B C   
3974  O  O   . ALA   B 175 ? 1.2803 1.2964 1.2226 0.0823  -0.1544 -0.0365 175  ALA   B O   
3975  C  CB  . ALA   B 175 ? 1.3223 1.3363 1.2649 0.0838  -0.1603 -0.0421 175  ALA   B CB  
3976  N  N   . PRO   B 176 ? 1.1930 1.2125 1.1507 0.0796  -0.1696 -0.0456 176  PRO   B N   
3977  C  CA  . PRO   B 176 ? 1.2223 1.2496 1.1906 0.0739  -0.1683 -0.0441 176  PRO   B CA  
3978  C  C   . PRO   B 176 ? 1.2136 1.2522 1.1895 0.0668  -0.1583 -0.0383 176  PRO   B C   
3979  O  O   . PRO   B 176 ? 1.2064 1.2529 1.1904 0.0616  -0.1551 -0.0373 176  PRO   B O   
3980  C  CB  . PRO   B 176 ? 1.1872 1.2206 1.1712 0.0693  -0.1763 -0.0491 176  PRO   B CB  
3981  C  CG  . PRO   B 176 ? 1.2616 1.2851 1.2379 0.0763  -0.1847 -0.0544 176  PRO   B CG  
3982  C  CD  . PRO   B 176 ? 1.2166 1.2350 1.1803 0.0804  -0.1793 -0.0518 176  PRO   B CD  
3983  N  N   . THR   B 177 ? 1.1580 1.1968 1.1309 0.0667  -0.1537 -0.0346 177  THR   B N   
3984  C  CA  . THR   B 177 ? 1.1597 1.2077 1.1380 0.0611  -0.1443 -0.0290 177  THR   B CA  
3985  C  C   . THR   B 177 ? 1.1410 1.1955 1.1278 0.0567  -0.1436 -0.0276 177  THR   B C   
3986  O  O   . THR   B 177 ? 1.1429 1.1906 1.1226 0.0611  -0.1458 -0.0280 177  THR   B O   
3987  C  CB  . THR   B 177 ? 1.1405 1.1817 1.1047 0.0666  -0.1371 -0.0247 177  THR   B CB  
3988  O  OG1 . THR   B 177 ? 1.2126 1.2492 1.1702 0.0695  -0.1363 -0.0253 177  THR   B OG1 
3989  C  CG2 . THR   B 177 ? 1.1075 1.1586 1.0788 0.0609  -0.1282 -0.0191 177  THR   B CG2 
3990  N  N   . ILE   B 178 ? 1.1117 1.1784 1.1123 0.0484  -0.1402 -0.0257 178  ILE   B N   
3991  C  CA  . ILE   B 178 ? 1.0505 1.1237 1.0588 0.0439  -0.1384 -0.0236 178  ILE   B CA  
3992  C  C   . ILE   B 178 ? 1.0790 1.1568 1.0861 0.0422  -0.1295 -0.0179 178  ILE   B C   
3993  O  O   . ILE   B 178 ? 1.0933 1.1740 1.1004 0.0407  -0.1247 -0.0157 178  ILE   B O   
3994  C  CB  . ILE   B 178 ? 1.0119 1.0949 1.0362 0.0358  -0.1409 -0.0254 178  ILE   B CB  
3995  C  CG1 . ILE   B 178 ? 1.0120 1.1026 1.0435 0.0308  -0.1376 -0.0246 178  ILE   B CG1 
3996  C  CG2 . ILE   B 178 ? 1.0404 1.1190 1.0675 0.0374  -0.1498 -0.0309 178  ILE   B CG2 
3997  C  CD1 . ILE   B 178 ? 0.9531 1.0543 0.9995 0.0225  -0.1370 -0.0244 178  ILE   B CD1 
3998  N  N   . CYS   B 179 ? 1.0733 1.1519 1.0800 0.0424  -0.1276 -0.0156 179  CYS   B N   
3999  C  CA  . CYS   B 179 ? 1.0311 1.1149 1.0386 0.0407  -0.1198 -0.0104 179  CYS   B CA  
4000  C  C   . CYS   B 179 ? 1.0295 1.1222 1.0484 0.0343  -0.1196 -0.0094 179  CYS   B C   
4001  O  O   . CYS   B 179 ? 0.9975 1.0876 1.0167 0.0351  -0.1240 -0.0113 179  CYS   B O   
4002  C  CB  . CYS   B 179 ? 0.9774 1.0523 0.9717 0.0484  -0.1170 -0.0083 179  CYS   B CB  
4003  S  SG  . CYS   B 179 ? 1.0490 1.1305 1.0457 0.0466  -0.1075 -0.0020 179  CYS   B SG  
4004  N  N   . PHE   B 180 ? 1.0722 1.1748 1.1000 0.0280  -0.1149 -0.0065 180  PHE   B N   
4005  C  CA  . PHE   B 180 ? 1.0145 1.1252 1.0529 0.0218  -0.1152 -0.0059 180  PHE   B CA  
4006  C  C   . PHE   B 180 ? 1.0233 1.1416 1.0660 0.0185  -0.1088 -0.0012 180  PHE   B C   
4007  O  O   . PHE   B 180 ? 1.0215 1.1415 1.0630 0.0185  -0.1042 0.0011  180  PHE   B O   
4008  C  CB  . PHE   B 180 ? 0.9787 1.0942 1.0268 0.0161  -0.1188 -0.0089 180  PHE   B CB  
4009  C  CG  . PHE   B 180 ? 0.9866 1.1067 1.0383 0.0127  -0.1161 -0.0083 180  PHE   B CG  
4010  C  CD1 . PHE   B 180 ? 1.0336 1.1485 1.0793 0.0163  -0.1170 -0.0100 180  PHE   B CD1 
4011  C  CD2 . PHE   B 180 ? 1.0566 1.1857 1.1173 0.0061  -0.1129 -0.0063 180  PHE   B CD2 
4012  C  CE1 . PHE   B 180 ? 1.1537 1.2727 1.2027 0.0132  -0.1145 -0.0095 180  PHE   B CE1 
4013  C  CE2 . PHE   B 180 ? 1.0847 1.2177 1.1485 0.0029  -0.1106 -0.0059 180  PHE   B CE2 
4014  C  CZ  . PHE   B 180 ? 1.1476 1.2757 1.2057 0.0064  -0.1113 -0.0075 180  PHE   B CZ  
4015  N  N   . VAL   B 181 ? 1.0785 1.2009 1.1261 0.0159  -0.1089 0.0000  181  VAL   B N   
4016  C  CA  . VAL   B 181 ? 1.0198 1.1499 1.0729 0.0123  -0.1041 0.0038  181  VAL   B CA  
4017  C  C   . VAL   B 181 ? 1.0108 1.1483 1.0740 0.0051  -0.1054 0.0031  181  VAL   B C   
4018  O  O   . VAL   B 181 ? 0.9538 1.0907 1.0199 0.0034  -0.1092 0.0010  181  VAL   B O   
4019  C  CB  . VAL   B 181 ? 0.9727 1.1014 1.0230 0.0154  -0.1033 0.0058  181  VAL   B CB  
4020  C  CG1 . VAL   B 181 ? 0.9624 1.0999 1.0207 0.0106  -0.1003 0.0088  181  VAL   B CG1 
4021  C  CG2 . VAL   B 181 ? 0.9368 1.0593 0.9776 0.0223  -0.1001 0.0075  181  VAL   B CG2 
4022  N  N   . TYR   B 182 ? 1.0549 1.1988 1.1232 0.0009  -0.1020 0.0049  182  TYR   B N   
4023  C  CA  . TYR   B 182 ? 1.0199 1.1701 1.0966 -0.0057 -0.1027 0.0045  182  TYR   B CA  
4024  C  C   . TYR   B 182 ? 1.0120 1.1692 1.0933 -0.0090 -0.0989 0.0080  182  TYR   B C   
4025  O  O   . TYR   B 182 ? 1.0444 1.2024 1.1239 -0.0068 -0.0953 0.0106  182  TYR   B O   
4026  C  CB  . TYR   B 182 ? 1.0212 1.1719 1.0997 -0.0079 -0.1034 0.0024  182  TYR   B CB  
4027  C  CG  . TYR   B 182 ? 1.0628 1.2140 1.1389 -0.0070 -0.0996 0.0041  182  TYR   B CG  
4028  C  CD1 . TYR   B 182 ? 1.1067 1.2515 1.1748 -0.0012 -0.0988 0.0040  182  TYR   B CD1 
4029  C  CD2 . TYR   B 182 ? 1.1018 1.2592 1.1832 -0.0117 -0.0967 0.0058  182  TYR   B CD2 
4030  C  CE1 . TYR   B 182 ? 1.1499 1.2946 1.2156 -0.0004 -0.0948 0.0058  182  TYR   B CE1 
4031  C  CE2 . TYR   B 182 ? 1.0972 1.2548 1.1768 -0.0111 -0.0932 0.0074  182  TYR   B CE2 
4032  C  CZ  . TYR   B 182 ? 1.1163 1.2677 1.1884 -0.0056 -0.0920 0.0075  182  TYR   B CZ  
4033  O  OH  . TYR   B 182 ? 1.2124 1.3632 1.2825 -0.0049 -0.0880 0.0093  182  TYR   B OH  
4034  N  N   . GLN   B 183 ? 1.0692 1.2311 1.1566 -0.0142 -0.0997 0.0079  183  GLN   B N   
4035  C  CA  . GLN   B 183 ? 1.1049 1.2732 1.1969 -0.0176 -0.0972 0.0106  183  GLN   B CA  
4036  C  C   . GLN   B 183 ? 1.0909 1.2631 1.1875 -0.0228 -0.0969 0.0100  183  GLN   B C   
4037  O  O   . GLN   B 183 ? 1.0860 1.2570 1.1840 -0.0249 -0.0991 0.0076  183  GLN   B O   
4038  C  CB  . GLN   B 183 ? 1.0366 1.2063 1.1302 -0.0183 -0.0983 0.0116  183  GLN   B CB  
4039  C  CG  . GLN   B 183 ? 1.0843 1.2602 1.1825 -0.0215 -0.0964 0.0142  183  GLN   B CG  
4040  C  CD  . GLN   B 183 ? 1.2206 1.3974 1.3188 -0.0200 -0.0966 0.0160  183  GLN   B CD  
4041  O  OE1 . GLN   B 183 ? 1.2343 1.4111 1.3309 -0.0162 -0.0948 0.0178  183  GLN   B OE1 
4042  N  NE2 . GLN   B 183 ? 1.2718 1.4492 1.3716 -0.0226 -0.0985 0.0157  183  GLN   B NE2 
4043  N  N   . ASP   B 184 ? 1.1316 1.3079 1.2306 -0.0247 -0.0942 0.0120  184  ASP   B N   
4044  C  CA  . ASP   B 184 ? 1.1546 1.3345 1.2575 -0.0295 -0.0938 0.0117  184  ASP   B CA  
4045  C  C   . ASP   B 184 ? 1.1967 1.3818 1.3033 -0.0317 -0.0925 0.0144  184  ASP   B C   
4046  O  O   . ASP   B 184 ? 1.1989 1.3849 1.3055 -0.0295 -0.0920 0.0161  184  ASP   B O   
4047  C  CB  . ASP   B 184 ? 1.1627 1.3414 1.2643 -0.0294 -0.0925 0.0109  184  ASP   B CB  
4048  C  CG  . ASP   B 184 ? 1.2111 1.3899 1.3112 -0.0267 -0.0893 0.0132  184  ASP   B CG  
4049  O  OD1 . ASP   B 184 ? 1.1685 1.3494 1.2699 -0.0254 -0.0879 0.0155  184  ASP   B OD1 
4050  O  OD2 . ASP   B 184 ? 1.2342 1.4107 1.3319 -0.0257 -0.0879 0.0126  184  ASP   B OD2 
4051  N  N   . PRO   B 185 ? 1.2037 1.3920 1.3134 -0.0358 -0.0920 0.0145  185  PRO   B N   
4052  C  CA  . PRO   B 185 ? 1.2077 1.4008 1.3213 -0.0377 -0.0915 0.0167  185  PRO   B CA  
4053  C  C   . PRO   B 185 ? 1.2960 1.4911 1.4112 -0.0349 -0.0891 0.0190  185  PRO   B C   
4054  O  O   . PRO   B 185 ? 1.3209 1.5186 1.4384 -0.0341 -0.0894 0.0207  185  PRO   B O   
4055  C  CB  . PRO   B 185 ? 1.1303 1.3251 1.2458 -0.0417 -0.0912 0.0161  185  PRO   B CB  
4056  C  CG  . PRO   B 185 ? 1.1331 1.3245 1.2461 -0.0427 -0.0924 0.0137  185  PRO   B CG  
4057  C  CD  . PRO   B 185 ? 1.1881 1.3756 1.2979 -0.0387 -0.0925 0.0126  185  PRO   B CD  
4058  N  N   . GLN   B 186 ? 1.3277 1.5212 1.4416 -0.0331 -0.0866 0.0193  186  GLN   B N   
4059  C  CA  . GLN   B 186 ? 1.3322 1.5277 1.4485 -0.0309 -0.0834 0.0218  186  GLN   B CA  
4060  C  C   . GLN   B 186 ? 1.3689 1.5617 1.4817 -0.0256 -0.0824 0.0228  186  GLN   B C   
4061  O  O   . GLN   B 186 ? 1.4229 1.6174 1.5379 -0.0234 -0.0792 0.0252  186  GLN   B O   
4062  C  CB  . GLN   B 186 ? 1.3321 1.5263 1.4479 -0.0311 -0.0805 0.0221  186  GLN   B CB  
4063  C  CG  . GLN   B 186 ? 1.4025 1.5982 1.5204 -0.0359 -0.0817 0.0207  186  GLN   B CG  
4064  C  CD  . GLN   B 186 ? 1.4115 1.6022 1.5240 -0.0354 -0.0822 0.0183  186  GLN   B CD  
4065  O  OE1 . GLN   B 186 ? 1.4625 1.6492 1.5710 -0.0322 -0.0801 0.0184  186  GLN   B OE1 
4066  N  NE2 . GLN   B 186 ? 1.3445 1.5351 1.4568 -0.0383 -0.0849 0.0162  186  GLN   B NE2 
4067  N  N   . GLY   B 187 ? 1.2596 1.4481 1.3674 -0.0236 -0.0848 0.0211  187  GLY   B N   
4068  C  CA  . GLY   B 187 ? 1.1602 1.3462 1.2648 -0.0187 -0.0843 0.0220  187  GLY   B CA  
4069  C  C   . GLY   B 187 ? 1.1455 1.3246 1.2430 -0.0156 -0.0865 0.0196  187  GLY   B C   
4070  O  O   . GLY   B 187 ? 1.1458 1.3233 1.2427 -0.0179 -0.0893 0.0171  187  GLY   B O   
4071  N  N   . ARG   B 188 ? 1.1517 1.3265 1.2441 -0.0101 -0.0852 0.0203  188  ARG   B N   
4072  C  CA  . ARG   B 188 ? 1.0706 1.2378 1.1555 -0.0060 -0.0874 0.0181  188  ARG   B CA  
4073  C  C   . ARG   B 188 ? 1.0791 1.2414 1.1581 -0.0016 -0.0844 0.0186  188  ARG   B C   
4074  O  O   . ARG   B 188 ? 1.1096 1.2732 1.1891 0.0004  -0.0800 0.0214  188  ARG   B O   
4075  C  CB  . ARG   B 188 ? 1.0874 1.2521 1.1694 -0.0026 -0.0889 0.0184  188  ARG   B CB  
4076  C  CG  . ARG   B 188 ? 1.0832 1.2438 1.1630 -0.0030 -0.0938 0.0152  188  ARG   B CG  
4077  C  CD  . ARG   B 188 ? 1.1161 1.2746 1.1939 -0.0005 -0.0953 0.0157  188  ARG   B CD  
4078  N  NE  . ARG   B 188 ? 1.1211 1.2833 1.2039 -0.0050 -0.0974 0.0154  188  ARG   B NE  
4079  C  CZ  . ARG   B 188 ? 1.1357 1.2964 1.2175 -0.0038 -0.0990 0.0158  188  ARG   B CZ  
4080  N  NH1 . ARG   B 188 ? 1.1108 1.2668 1.1870 0.0016  -0.0990 0.0162  188  ARG   B NH1 
4081  N  NH2 . ARG   B 188 ? 1.2622 1.4257 1.3480 -0.0079 -0.1006 0.0157  188  ARG   B NH2 
4082  N  N   . HIS   B 189 ? 1.0641 1.2207 1.1378 -0.0001 -0.0868 0.0158  189  HIS   B N   
4083  C  CA  . HIS   B 189 ? 1.1404 1.2919 1.2081 0.0035  -0.0842 0.0160  189  HIS   B CA  
4084  C  C   . HIS   B 189 ? 1.1046 1.2473 1.1637 0.0084  -0.0879 0.0129  189  HIS   B C   
4085  O  O   . HIS   B 189 ? 1.0668 1.2085 1.1267 0.0072  -0.0927 0.0101  189  HIS   B O   
4086  C  CB  . HIS   B 189 ? 1.1620 1.3167 1.2336 -0.0008 -0.0830 0.0156  189  HIS   B CB  
4087  C  CG  . HIS   B 189 ? 1.1470 1.3105 1.2281 -0.0069 -0.0820 0.0172  189  HIS   B CG  
4088  N  ND1 . HIS   B 189 ? 1.1933 1.3614 1.2789 -0.0078 -0.0777 0.0205  189  HIS   B ND1 
4089  C  CD2 . HIS   B 189 ? 1.1327 1.3006 1.2194 -0.0122 -0.0849 0.0158  189  HIS   B CD2 
4090  C  CE1 . HIS   B 189 ? 1.1866 1.3616 1.2800 -0.0134 -0.0786 0.0208  189  HIS   B CE1 
4091  N  NE2 . HIS   B 189 ? 1.1846 1.3593 1.2782 -0.0160 -0.0827 0.0181  189  HIS   B NE2 
4092  N  N   . VAL   B 190 ? 1.0961 1.2318 1.1465 0.0140  -0.0856 0.0134  190  VAL   B N   
4093  C  CA  . VAL   B 190 ? 1.0769 1.2030 1.1178 0.0194  -0.0894 0.0104  190  VAL   B CA  
4094  C  C   . VAL   B 190 ? 1.0893 1.2119 1.1266 0.0200  -0.0893 0.0089  190  VAL   B C   
4095  O  O   . VAL   B 190 ? 1.1892 1.3120 1.2254 0.0204  -0.0842 0.0114  190  VAL   B O   
4096  C  CB  . VAL   B 190 ? 1.0852 1.2038 1.1164 0.0269  -0.0873 0.0119  190  VAL   B CB  
4097  C  CG1 . VAL   B 190 ? 1.0931 1.2008 1.1133 0.0328  -0.0916 0.0085  190  VAL   B CG1 
4098  C  CG2 . VAL   B 190 ? 1.1122 1.2333 1.1461 0.0268  -0.0883 0.0128  190  VAL   B CG2 
4099  N  N   . LYS   B 191 ? 1.0757 1.1951 1.1118 0.0200  -0.0950 0.0048  191  LYS   B N   
4100  C  CA  . LYS   B 191 ? 1.0820 1.1978 1.1147 0.0208  -0.0958 0.0029  191  LYS   B CA  
4101  C  C   . LYS   B 191 ? 1.1024 1.2089 1.1271 0.0263  -0.1018 -0.0011 191  LYS   B C   
4102  O  O   . LYS   B 191 ? 1.0328 1.1376 1.0576 0.0274  -0.1061 -0.0031 191  LYS   B O   
4103  C  CB  . LYS   B 191 ? 1.0865 1.2102 1.1293 0.0137  -0.0969 0.0018  191  LYS   B CB  
4104  C  CG  . LYS   B 191 ? 1.1622 1.2824 1.2017 0.0145  -0.0976 -0.0001 191  LYS   B CG  
4105  C  CD  . LYS   B 191 ? 1.1925 1.3206 1.2408 0.0078  -0.0958 0.0006  191  LYS   B CD  
4106  C  CE  . LYS   B 191 ? 1.2182 1.3514 1.2750 0.0030  -0.1002 -0.0021 191  LYS   B CE  
4107  N  NZ  . LYS   B 191 ? 1.2638 1.4016 1.3261 -0.0018 -0.0994 -0.0026 191  LYS   B NZ  
4108  N  N   . THR   B 192 ? 1.1632 1.2632 1.1804 0.0300  -0.1021 -0.0025 192  THR   B N   
4109  C  CA  . THR   B 192 ? 1.1303 1.2220 1.1410 0.0347  -0.1088 -0.0070 192  THR   B CA  
4110  C  C   . THR   B 192 ? 1.0725 1.1667 1.0883 0.0315  -0.1116 -0.0098 192  THR   B C   
4111  O  O   . THR   B 192 ? 1.1449 1.2451 1.1658 0.0270  -0.1076 -0.0079 192  THR   B O   
4112  C  CB  . THR   B 192 ? 1.1135 1.1930 1.1088 0.0435  -0.1078 -0.0067 192  THR   B CB  
4113  O  OG1 . THR   B 192 ? 1.0543 1.1327 1.0460 0.0440  -0.1025 -0.0045 192  THR   B OG1 
4114  C  CG2 . THR   B 192 ? 1.0966 1.1730 1.0863 0.0473  -0.1046 -0.0038 192  THR   B CG2 
4115  N  N   . TYR   B 193 ? 1.0029 1.0925 1.0174 0.0338  -0.1188 -0.0145 193  TYR   B N   
4116  C  CA  . TYR   B 193 ? 1.0900 1.1796 1.1071 0.0329  -0.1223 -0.0178 193  TYR   B CA  
4117  C  C   . TYR   B 193 ? 1.1458 1.2247 1.1538 0.0402  -0.1291 -0.0221 193  TYR   B C   
4118  O  O   . TYR   B 193 ? 1.1575 1.2314 1.1615 0.0438  -0.1327 -0.0234 193  TYR   B O   
4119  C  CB  . TYR   B 193 ? 1.1478 1.2468 1.1795 0.0258  -0.1252 -0.0199 193  TYR   B CB  
4120  C  CG  . TYR   B 193 ? 1.1579 1.2670 1.1989 0.0184  -0.1198 -0.0168 193  TYR   B CG  
4121  C  CD1 . TYR   B 193 ? 1.0989 1.2091 1.1373 0.0175  -0.1145 -0.0141 193  TYR   B CD1 
4122  C  CD2 . TYR   B 193 ? 1.1393 1.2564 1.1913 0.0123  -0.1202 -0.0167 193  TYR   B CD2 
4123  C  CE1 . TYR   B 193 ? 1.1270 1.2461 1.1739 0.0108  -0.1103 -0.0116 193  TYR   B CE1 
4124  C  CE2 . TYR   B 193 ? 1.1748 1.3002 1.2342 0.0061  -0.1159 -0.0141 193  TYR   B CE2 
4125  C  CZ  . TYR   B 193 ? 1.1638 1.2903 1.2208 0.0053  -0.1112 -0.0117 193  TYR   B CZ  
4126  O  OH  . TYR   B 193 ? 1.1833 1.3178 1.2479 -0.0010 -0.1075 -0.0094 193  TYR   B OH  
4127  N  N   . GLU   B 194 ? 1.1116 1.1870 1.1166 0.0423  -0.1314 -0.0245 194  GLU   B N   
4128  C  CA  . GLU   B 194 ? 1.1342 1.2004 1.1325 0.0486  -0.1393 -0.0294 194  GLU   B CA  
4129  C  C   . GLU   B 194 ? 1.1582 1.2305 1.1697 0.0443  -0.1455 -0.0338 194  GLU   B C   
4130  O  O   . GLU   B 194 ? 1.1628 1.2440 1.1846 0.0380  -0.1430 -0.0331 194  GLU   B O   
4131  C  CB  . GLU   B 194 ? 1.2096 1.2658 1.1941 0.0553  -0.1386 -0.0297 194  GLU   B CB  
4132  C  CG  . GLU   B 194 ? 1.2558 1.3032 1.2253 0.0614  -0.1332 -0.0259 194  GLU   B CG  
4133  C  CD  . GLU   B 194 ? 1.3418 1.3762 1.2952 0.0698  -0.1341 -0.0271 194  GLU   B CD  
4134  O  OE1 . GLU   B 194 ? 1.2839 1.3172 1.2381 0.0703  -0.1380 -0.0302 194  GLU   B OE1 
4135  O  OE2 . GLU   B 194 ? 1.4644 1.4892 1.4038 0.0762  -0.1308 -0.0247 194  GLU   B OE2 
4136  N  N   . VAL   B 195 ? 1.1350 1.2022 1.1463 0.0477  -0.1535 -0.0383 195  VAL   B N   
4137  C  CA  . VAL   B 195 ? 1.1559 1.2290 1.1813 0.0436  -0.1596 -0.0426 195  VAL   B CA  
4138  C  C   . VAL   B 195 ? 1.2239 1.2910 1.2455 0.0485  -0.1657 -0.0470 195  VAL   B C   
4139  O  O   . VAL   B 195 ? 1.2277 1.2837 1.2382 0.0562  -0.1714 -0.0499 195  VAL   B O   
4140  C  CB  . VAL   B 195 ? 1.1792 1.2515 1.2094 0.0433  -0.1648 -0.0448 195  VAL   B CB  
4141  C  CG1 . VAL   B 195 ? 1.1453 1.2251 1.1925 0.0378  -0.1696 -0.0485 195  VAL   B CG1 
4142  C  CG2 . VAL   B 195 ? 1.1428 1.2189 1.1731 0.0402  -0.1586 -0.0400 195  VAL   B CG2 
4143  N  N   . SER   B 196 ? 1.1949 1.2685 1.2249 0.0446  -0.1646 -0.0476 196  SER   B N   
4144  C  CA  . SER   B 196 ? 1.2788 1.3479 1.3071 0.0488  -0.1705 -0.0520 196  SER   B CA  
4145  C  C   . SER   B 196 ? 1.2764 1.3512 1.3207 0.0455  -0.1775 -0.0568 196  SER   B C   
4146  O  O   . SER   B 196 ? 1.2475 1.3330 1.3063 0.0383  -0.1749 -0.0562 196  SER   B O   
4147  C  CB  . SER   B 196 ? 1.3327 1.4044 1.3596 0.0473  -0.1654 -0.0500 196  SER   B CB  
4148  O  OG  . SER   B 196 ? 1.4245 1.4878 1.4434 0.0541  -0.1709 -0.0538 196  SER   B OG  
4149  N  N   . LEU   B 197 ? 1.2423 1.3097 1.2840 0.0509  -0.1864 -0.0616 197  LEU   B N   
4150  C  CA  . LEU   B 197 ? 1.3150 1.3874 1.3728 0.0483  -0.1936 -0.0666 197  LEU   B CA  
4151  C  C   . LEU   B 197 ? 1.4077 1.4819 1.4699 0.0491  -0.1961 -0.0695 197  LEU   B C   
4152  O  O   . LEU   B 197 ? 1.3992 1.4831 1.4781 0.0434  -0.1964 -0.0709 197  LEU   B O   
4153  C  CB  . LEU   B 197 ? 1.3195 1.3829 1.3735 0.0539  -0.2030 -0.0711 197  LEU   B CB  
4154  C  CG  . LEU   B 197 ? 1.3394 1.3981 1.3842 0.0551  -0.2005 -0.0681 197  LEU   B CG  
4155  C  CD1 . LEU   B 197 ? 1.4297 1.4755 1.4522 0.0639  -0.1997 -0.0668 197  LEU   B CD1 
4156  C  CD2 . LEU   B 197 ? 1.2875 1.3446 1.3397 0.0551  -0.2081 -0.0720 197  LEU   B CD2 
4157  N  N   . ARG   B 198 ? 1.4537 1.5184 1.5006 0.0564  -0.1975 -0.0701 198  ARG   B N   
4158  C  CA  . ARG   B 198 ? 1.3723 1.4381 1.4207 0.0575  -0.1984 -0.0720 198  ARG   B CA  
4159  C  C   . ARG   B 198 ? 1.3434 1.4220 1.4051 0.0488  -0.1910 -0.0688 198  ARG   B C   
4160  O  O   . ARG   B 198 ? 1.3737 1.4600 1.4507 0.0452  -0.1935 -0.0716 198  ARG   B O   
4161  C  CB  . ARG   B 198 ? 1.3469 1.4013 1.3746 0.0650  -0.1965 -0.0704 198  ARG   B CB  
4162  N  N   . GLU   B 199 ? 1.3708 1.4519 1.4273 0.0454  -0.1818 -0.0631 199  GLU   B N   
4163  C  CA  . GLU   B 199 ? 1.3529 1.4447 1.4191 0.0377  -0.1743 -0.0597 199  GLU   B CA  
4164  C  C   . GLU   B 199 ? 1.3440 1.4456 1.4246 0.0300  -0.1717 -0.0582 199  GLU   B C   
4165  O  O   . GLU   B 199 ? 1.3656 1.4760 1.4553 0.0236  -0.1664 -0.0560 199  GLU   B O   
4166  C  CB  . GLU   B 199 ? 1.4092 1.4984 1.4626 0.0380  -0.1660 -0.0543 199  GLU   B CB  
4167  C  CG  . GLU   B 199 ? 1.5083 1.5856 1.5443 0.0463  -0.1672 -0.0549 199  GLU   B CG  
4168  C  CD  . GLU   B 199 ? 1.5754 1.6512 1.6014 0.0457  -0.1583 -0.0496 199  GLU   B CD  
4169  O  OE1 . GLU   B 199 ? 1.4968 1.5807 1.5291 0.0389  -0.1514 -0.0455 199  GLU   B OE1 
4170  O  OE2 . GLU   B 199 ? 1.6195 1.6854 1.6312 0.0521  -0.1583 -0.0496 199  GLU   B OE2 
4171  N  N   . LYS   B 200 ? 1.3050 1.4048 1.3874 0.0305  -0.1754 -0.0593 200  LYS   B N   
4172  C  CA  . LYS   B 200 ? 1.1681 1.2763 1.2642 0.0235  -0.1734 -0.0582 200  LYS   B CA  
4173  C  C   . LYS   B 200 ? 1.2019 1.3163 1.2978 0.0178  -0.1640 -0.0524 200  LYS   B C   
4174  O  O   . LYS   B 200 ? 1.1183 1.2415 1.2264 0.0110  -0.1606 -0.0512 200  LYS   B O   
4175  C  CB  . LYS   B 200 ? 1.1303 1.2458 1.2443 0.0196  -0.1769 -0.0619 200  LYS   B CB  
4176  C  CG  . LYS   B 200 ? 1.2695 1.3807 1.3885 0.0236  -0.1869 -0.0678 200  LYS   B CG  
4177  C  CD  . LYS   B 200 ? 1.3386 1.4557 1.4735 0.0218  -0.1910 -0.0720 200  LYS   B CD  
4178  C  CE  . LYS   B 200 ? 1.2884 1.4157 1.4417 0.0136  -0.1877 -0.0712 200  LYS   B CE  
4179  N  NZ  . LYS   B 200 ? 1.3303 1.4620 1.5006 0.0128  -0.1935 -0.0763 200  LYS   B NZ  
4180  N  N   . GLU   B 201 ? 1.2191 1.3285 1.3008 0.0206  -0.1597 -0.0489 201  GLU   B N   
4181  C  CA  . GLU   B 201 ? 1.2206 1.3349 1.3012 0.0160  -0.1515 -0.0435 201  GLU   B CA  
4182  C  C   . GLU   B 201 ? 1.2444 1.3508 1.3095 0.0210  -0.1491 -0.0407 201  GLU   B C   
4183  O  O   . GLU   B 201 ? 1.2578 1.3550 1.3127 0.0280  -0.1535 -0.0429 201  GLU   B O   
4184  C  CB  . GLU   B 201 ? 1.3111 1.4314 1.3956 0.0117  -0.1463 -0.0416 201  GLU   B CB  
4185  C  CG  . GLU   B 201 ? 1.4053 1.5210 1.4771 0.0147  -0.1419 -0.0388 201  GLU   B CG  
4186  C  CD  . GLU   B 201 ? 1.4583 1.5685 1.5251 0.0197  -0.1455 -0.0420 201  GLU   B CD  
4187  O  OE1 . GLU   B 201 ? 1.4229 1.5321 1.4951 0.0218  -0.1524 -0.0466 201  GLU   B OE1 
4188  O  OE2 . GLU   B 201 ? 1.4650 1.5719 1.5229 0.0215  -0.1417 -0.0399 201  GLU   B OE2 
4189  N  N   . PHE   B 202 ? 1.1848 1.2949 1.2484 0.0176  -0.1421 -0.0358 202  PHE   B N   
4190  C  CA  . PHE   B 202 ? 1.1675 1.2720 1.2186 0.0214  -0.1383 -0.0324 202  PHE   B CA  
4191  C  C   . PHE   B 202 ? 1.2331 1.3339 1.2751 0.0239  -0.1343 -0.0305 202  PHE   B C   
4192  O  O   . PHE   B 202 ? 1.3028 1.4083 1.3497 0.0203  -0.1321 -0.0302 202  PHE   B O   
4193  C  CB  . PHE   B 202 ? 1.1500 1.2607 1.2050 0.0164  -0.1328 -0.0281 202  PHE   B CB  
4194  C  CG  . PHE   B 202 ? 1.1569 1.2690 1.2172 0.0151  -0.1358 -0.0290 202  PHE   B CG  
4195  C  CD1 . PHE   B 202 ? 1.1571 1.2614 1.2115 0.0207  -0.1413 -0.0316 202  PHE   B CD1 
4196  C  CD2 . PHE   B 202 ? 1.1369 1.2574 1.2073 0.0084  -0.1330 -0.0271 202  PHE   B CD2 
4197  C  CE1 . PHE   B 202 ? 1.1336 1.2388 1.1928 0.0194  -0.1439 -0.0324 202  PHE   B CE1 
4198  C  CE2 . PHE   B 202 ? 1.1099 1.2312 1.1848 0.0072  -0.1355 -0.0277 202  PHE   B CE2 
4199  C  CZ  . PHE   B 202 ? 1.1085 1.2223 1.1781 0.0126  -0.1409 -0.0304 202  PHE   B CZ  
4200  N  N   . ASN   B 203 ? 1.2080 1.2998 1.2364 0.0302  -0.1331 -0.0292 203  ASN   B N   
4201  C  CA  . ASN   B 203 ? 1.1597 1.2469 1.1781 0.0328  -0.1278 -0.0263 203  ASN   B CA  
4202  C  C   . ASN   B 203 ? 1.1097 1.1964 1.1230 0.0330  -0.1214 -0.0215 203  ASN   B C   
4203  O  O   . ASN   B 203 ? 1.2319 1.3198 1.2471 0.0327  -0.1221 -0.0209 203  ASN   B O   
4204  C  CB  . ASN   B 203 ? 1.2373 1.3127 1.2429 0.0411  -0.1319 -0.0292 203  ASN   B CB  
4205  C  CG  . ASN   B 203 ? 1.3844 1.4607 1.3950 0.0410  -0.1371 -0.0335 203  ASN   B CG  
4206  O  OD1 . ASN   B 203 ? 1.4349 1.5189 1.4542 0.0354  -0.1347 -0.0330 203  ASN   B OD1 
4207  N  ND2 . ASN   B 203 ? 1.3971 1.4654 1.4020 0.0474  -0.1446 -0.0380 203  ASN   B ND2 
4208  N  N   . LYS   B 204 ? 1.1028 1.1873 1.1098 0.0337  -0.1150 -0.0180 204  LYS   B N   
4209  C  CA  . LYS   B 204 ? 1.1795 1.2647 1.1838 0.0334  -0.1084 -0.0131 204  LYS   B CA  
4210  C  C   . LYS   B 204 ? 1.1579 1.2351 1.1528 0.0399  -0.1101 -0.0133 204  LYS   B C   
4211  O  O   . LYS   B 204 ? 1.1833 1.2517 1.1700 0.0460  -0.1156 -0.0168 204  LYS   B O   
4212  C  CB  . LYS   B 204 ? 1.1528 1.2345 1.1503 0.0346  -0.1016 -0.0097 204  LYS   B CB  
4213  N  N   . GLY   B 205 ? 1.0559 1.1359 1.0519 0.0388  -0.1055 -0.0096 205  GLY   B N   
4214  C  CA  . GLY   B 205 ? 1.1189 1.1915 1.1061 0.0449  -0.1064 -0.0094 205  GLY   B CA  
4215  C  C   . GLY   B 205 ? 1.1869 1.2519 1.1621 0.0503  -0.0996 -0.0054 205  GLY   B C   
4216  O  O   . GLY   B 205 ? 1.2591 1.3263 1.2352 0.0482  -0.0932 -0.0022 205  GLY   B O   
4217  N  N   . PRO   B 206 ? 1.1887 1.2442 1.1526 0.0576  -0.1006 -0.0056 206  PRO   B N   
4218  C  CA  . PRO   B 206 ? 1.1687 1.2160 1.1205 0.0634  -0.0933 -0.0015 206  PRO   B CA  
4219  C  C   . PRO   B 206 ? 1.1876 1.2431 1.1469 0.0591  -0.0847 0.0039  206  PRO   B C   
4220  O  O   . PRO   B 206 ? 1.2028 1.2551 1.1573 0.0608  -0.0774 0.0075  206  PRO   B O   
4221  C  CB  . PRO   B 206 ? 1.1850 1.2216 1.1247 0.0715  -0.0971 -0.0033 206  PRO   B CB  
4222  C  CG  . PRO   B 206 ? 1.1560 1.1974 1.1042 0.0684  -0.1054 -0.0074 206  PRO   B CG  
4223  C  CD  . PRO   B 206 ? 1.1591 1.2086 1.1187 0.0618  -0.1088 -0.0099 206  PRO   B CD  
4224  N  N   . TRP   B 207 ? 1.1913 1.2568 1.1623 0.0537  -0.0852 0.0047  207  TRP   B N   
4225  C  CA  . TRP   B 207 ? 1.2304 1.3032 1.2082 0.0504  -0.0776 0.0096  207  TRP   B CA  
4226  C  C   . TRP   B 207 ? 1.3021 1.3879 1.2954 0.0423  -0.0796 0.0095  207  TRP   B C   
4227  O  O   . TRP   B 207 ? 1.3004 1.3886 1.2979 0.0401  -0.0863 0.0060  207  TRP   B O   
4228  C  CB  . TRP   B 207 ? 1.2831 1.3487 1.2513 0.0572  -0.0738 0.0122  207  TRP   B CB  
4229  C  CG  . TRP   B 207 ? 1.2966 1.3569 1.2592 0.0615  -0.0803 0.0091  207  TRP   B CG  
4230  C  CD1 . TRP   B 207 ? 1.2955 1.3430 1.2440 0.0692  -0.0851 0.0060  207  TRP   B CD1 
4231  C  CD2 . TRP   B 207 ? 1.2739 1.3407 1.2443 0.0586  -0.0827 0.0090  207  TRP   B CD2 
4232  N  NE1 . TRP   B 207 ? 1.2396 1.2856 1.1874 0.0710  -0.0905 0.0037  207  TRP   B NE1 
4233  C  CE2 . TRP   B 207 ? 1.2800 1.3377 1.2410 0.0645  -0.0889 0.0057  207  TRP   B CE2 
4234  C  CE3 . TRP   B 207 ? 1.2379 1.3170 1.2220 0.0518  -0.0805 0.0112  207  TRP   B CE3 
4235  C  CZ2 . TRP   B 207 ? 1.2699 1.3304 1.2351 0.0635  -0.0925 0.0047  207  TRP   B CZ2 
4236  C  CZ3 . TRP   B 207 ? 1.2026 1.2843 1.1902 0.0511  -0.0841 0.0103  207  TRP   B CZ3 
4237  C  CH2 . TRP   B 207 ? 1.2245 1.2970 1.2029 0.0568  -0.0898 0.0072  207  TRP   B CH2 
4238  N  N   . LYS   B 208 ? 1.3479 1.4419 1.3497 0.0380  -0.0735 0.0136  208  LYS   B N   
4239  C  CA  . LYS   B 208 ? 1.2762 1.3822 1.2919 0.0305  -0.0746 0.0140  208  LYS   B CA  
4240  C  C   . LYS   B 208 ? 1.3052 1.4164 1.3259 0.0296  -0.0681 0.0186  208  LYS   B C   
4241  O  O   . LYS   B 208 ? 1.4296 1.5373 1.4462 0.0325  -0.0617 0.0218  208  LYS   B O   
4242  C  CB  . LYS   B 208 ? 1.2383 1.3512 1.2627 0.0236  -0.0757 0.0129  208  LYS   B CB  
4243  C  CG  . LYS   B 208 ? 1.4133 1.5309 1.4429 0.0203  -0.0690 0.0166  208  LYS   B CG  
4244  C  CD  . LYS   B 208 ? 1.5064 1.6277 1.5410 0.0150  -0.0700 0.0153  208  LYS   B CD  
4245  C  CE  . LYS   B 208 ? 1.3924 1.5193 1.4340 0.0103  -0.0762 0.0120  208  LYS   B CE  
4246  N  NZ  . LYS   B 208 ? 1.3455 1.4803 1.3965 0.0032  -0.0755 0.0123  208  LYS   B NZ  
4247  N  N   . GLN   B 209 ? 1.2730 1.3924 1.3030 0.0255  -0.0696 0.0191  209  GLN   B N   
4248  C  CA  . GLN   B 209 ? 1.3227 1.4490 1.3600 0.0236  -0.0643 0.0231  209  GLN   B CA  
4249  C  C   . GLN   B 209 ? 1.3031 1.4402 1.3530 0.0160  -0.0672 0.0226  209  GLN   B C   
4250  O  O   . GLN   B 209 ? 1.3035 1.4419 1.3549 0.0148  -0.0724 0.0203  209  GLN   B O   
4251  C  CB  . GLN   B 209 ? 1.3442 1.4665 1.3762 0.0295  -0.0630 0.0246  209  GLN   B CB  
4252  C  CG  . GLN   B 209 ? 1.3526 1.4766 1.3866 0.0315  -0.0548 0.0294  209  GLN   B CG  
4253  C  CD  . GLN   B 209 ? 1.4875 1.6239 1.5366 0.0247  -0.0524 0.0318  209  GLN   B CD  
4254  O  OE1 . GLN   B 209 ? 1.4612 1.6046 1.5183 0.0185  -0.0569 0.0300  209  GLN   B OE1 
4255  N  NE2 . GLN   B 209 ? 1.5297 1.6684 1.5825 0.0259  -0.0454 0.0359  209  GLN   B NE2 
4256  N  N   . GLU   B 210 ? 1.3187 1.4630 1.3775 0.0111  -0.0636 0.0249  210  GLU   B N   
4257  C  CA  . GLU   B 210 ? 1.3293 1.4825 1.3986 0.0039  -0.0665 0.0240  210  GLU   B CA  
4258  C  C   . GLU   B 210 ? 1.3184 1.4794 1.3963 0.0014  -0.0657 0.0262  210  GLU   B C   
4259  O  O   . GLU   B 210 ? 1.4136 1.5821 1.5004 -0.0044 -0.0667 0.0264  210  GLU   B O   
4260  C  CB  . GLU   B 210 ? 1.3784 1.5343 1.4518 -0.0003 -0.0642 0.0245  210  GLU   B CB  
4261  N  N   . ASN   B 211 ? 1.2854 1.4446 1.3606 0.0059  -0.0642 0.0278  211  ASN   B N   
4262  C  CA  . ASN   B 211 ? 1.3102 1.4766 1.3933 0.0036  -0.0651 0.0290  211  ASN   B CA  
4263  C  C   . ASN   B 211 ? 1.3653 1.5284 1.4437 0.0093  -0.0642 0.0302  211  ASN   B C   
4264  O  O   . ASN   B 211 ? 1.4689 1.6336 1.5496 0.0118  -0.0591 0.0334  211  ASN   B O   
4265  C  CB  . ASN   B 211 ? 1.2762 1.4509 1.3700 -0.0004 -0.0614 0.0319  211  ASN   B CB  
4266  C  CG  . ASN   B 211 ? 1.3247 1.5066 1.4268 -0.0073 -0.0653 0.0306  211  ASN   B CG  
4267  O  OD1 . ASN   B 211 ? 1.3503 1.5358 1.4557 -0.0088 -0.0685 0.0301  211  ASN   B OD1 
4268  N  ND2 . ASN   B 211 ? 1.3088 1.4919 1.4134 -0.0112 -0.0649 0.0300  211  ASN   B ND2 
4269  N  N   . VAL   B 212 ? 1.2707 1.4295 1.3435 0.0112  -0.0690 0.0276  212  VAL   B N   
4270  C  CA  . VAL   B 212 ? 1.2231 1.3769 1.2894 0.0172  -0.0688 0.0282  212  VAL   B CA  
4271  C  C   . VAL   B 212 ? 1.1424 1.3021 1.2151 0.0148  -0.0714 0.0286  212  VAL   B C   
4272  O  O   . VAL   B 212 ? 1.1915 1.3578 1.2720 0.0089  -0.0738 0.0279  212  VAL   B O   
4273  C  CB  . VAL   B 212 ? 1.2411 1.3847 1.2961 0.0216  -0.0727 0.0250  212  VAL   B CB  
4274  C  CG1 . VAL   B 212 ? 1.1343 1.2789 1.1914 0.0180  -0.0794 0.0217  212  VAL   B CG1 
4275  C  CG2 . VAL   B 212 ? 1.2846 1.4208 1.3304 0.0294  -0.0707 0.0262  212  VAL   B CG2 
4276  N  N   . GLU   B 213 ? 1.1382 1.2949 1.2068 0.0198  -0.0707 0.0297  213  GLU   B N   
4277  C  CA  . GLU   B 213 ? 1.1205 1.2818 1.1939 0.0186  -0.0729 0.0302  213  GLU   B CA  
4278  C  C   . GLU   B 213 ? 1.0921 1.2579 1.1711 0.0121  -0.0780 0.0280  213  GLU   B C   
4279  O  O   . GLU   B 213 ? 1.1317 1.2942 1.2079 0.0102  -0.0813 0.0251  213  GLU   B O   
4280  C  CB  . GLU   B 213 ? 1.1706 1.3241 1.2349 0.0246  -0.0747 0.0294  213  GLU   B CB  
4281  C  CG  . GLU   B 213 ? 1.1441 1.3009 1.2113 0.0265  -0.0739 0.0316  213  GLU   B CG  
4282  C  CD  . GLU   B 213 ? 1.1672 1.3252 1.2362 0.0235  -0.0795 0.0297  213  GLU   B CD  
4283  O  OE1 . GLU   B 213 ? 1.1973 1.3631 1.2750 0.0186  -0.0804 0.0304  213  GLU   B OE1 
4284  O  OE2 . GLU   B 213 ? 1.1855 1.3359 1.2467 0.0263  -0.0830 0.0275  213  GLU   B OE2 
4285  N  N   . ALA   B 214 ? 1.0654 1.2381 1.1519 0.0091  -0.0786 0.0293  214  ALA   B N   
4286  C  CA  . ALA   B 214 ? 1.1332 1.3096 1.2243 0.0031  -0.0827 0.0275  214  ALA   B CA  
4287  C  C   . ALA   B 214 ? 1.1122 1.2832 1.1982 0.0034  -0.0874 0.0249  214  ALA   B C   
4288  O  O   . ALA   B 214 ? 1.1260 1.2975 1.2136 -0.0010 -0.0904 0.0228  214  ALA   B O   
4289  C  CB  . ALA   B 214 ? 1.1261 1.3107 1.2260 0.0000  -0.0824 0.0295  214  ALA   B CB  
4290  N  N   . GLU   B 215 ? 1.1702 1.3358 1.2501 0.0085  -0.0878 0.0249  215  GLU   B N   
4291  C  CA  . GLU   B 215 ? 1.1868 1.3466 1.2620 0.0092  -0.0923 0.0225  215  GLU   B CA  
4292  C  C   . GLU   B 215 ? 1.1982 1.3489 1.2641 0.0145  -0.0931 0.0207  215  GLU   B C   
4293  O  O   . GLU   B 215 ? 1.2131 1.3578 1.2734 0.0182  -0.0953 0.0198  215  GLU   B O   
4294  C  CB  . GLU   B 215 ? 1.2115 1.3721 1.2871 0.0106  -0.0932 0.0237  215  GLU   B CB  
4295  C  CG  . GLU   B 215 ? 1.2338 1.3985 1.3147 0.0053  -0.0957 0.0234  215  GLU   B CG  
4296  C  CD  . GLU   B 215 ? 1.4126 1.5810 1.4960 0.0065  -0.0950 0.0258  215  GLU   B CD  
4297  O  OE1 . GLU   B 215 ? 1.4945 1.6587 1.5731 0.0114  -0.0951 0.0263  215  GLU   B OE1 
4298  O  OE2 . GLU   B 215 ? 1.4808 1.6562 1.5710 0.0029  -0.0945 0.0271  215  GLU   B OE2 
4299  N  N   . ALA   B 216 ? 1.1312 1.2802 1.1951 0.0153  -0.0915 0.0201  216  ALA   B N   
4300  C  CA  . ALA   B 216 ? 1.0631 1.2027 1.1175 0.0204  -0.0930 0.0180  216  ALA   B CA  
4301  C  C   . ALA   B 216 ? 1.0362 1.1720 1.0900 0.0181  -0.0989 0.0141  216  ALA   B C   
4302  O  O   . ALA   B 216 ? 1.0189 1.1593 1.0793 0.0123  -0.1005 0.0130  216  ALA   B O   
4303  C  CB  . ALA   B 216 ? 1.0425 1.1811 1.0949 0.0215  -0.0899 0.0183  216  ALA   B CB  
4304  N  N   . SER   B 217 ? 1.0166 1.1439 1.0628 0.0229  -0.1022 0.0121  217  SER   B N   
4305  C  CA  . SER   B 217 ? 0.9657 1.0898 1.0130 0.0205  -0.1079 0.0086  217  SER   B CA  
4306  C  C   . SER   B 217 ? 0.9900 1.1037 1.0287 0.0257  -0.1121 0.0053  217  SER   B C   
4307  O  O   . SER   B 217 ? 1.0370 1.1480 1.0776 0.0238  -0.1171 0.0020  217  SER   B O   
4308  C  CB  . SER   B 217 ? 1.0755 1.2016 1.1259 0.0187  -0.1089 0.0095  217  SER   B CB  
4309  O  OG  . SER   B 217 ? 1.0717 1.1956 1.1168 0.0240  -0.1065 0.0119  217  SER   B OG  
4310  N  N   . MET   B 218 ? 1.0146 1.1222 1.0439 0.0325  -0.1102 0.0061  218  MET   B N   
4311  C  CA  . MET   B 218 ? 0.9869 1.0833 1.0062 0.0385  -0.1144 0.0030  218  MET   B CA  
4312  C  C   . MET   B 218 ? 1.0021 1.0945 1.0148 0.0423  -0.1125 0.0028  218  MET   B C   
4313  O  O   . MET   B 218 ? 1.0553 1.1483 1.0644 0.0454  -0.1067 0.0062  218  MET   B O   
4314  C  CB  . MET   B 218 ? 0.9703 1.0604 0.9815 0.0445  -0.1141 0.0042  218  MET   B CB  
4315  C  CG  . MET   B 218 ? 1.0693 1.1470 1.0695 0.0509  -0.1193 0.0007  218  MET   B CG  
4316  S  SD  . MET   B 218 ? 1.2049 1.2772 1.2012 0.0537  -0.1221 0.0006  218  MET   B SD  
4317  C  CE  . MET   B 218 ? 1.1340 1.2058 1.1381 0.0479  -0.1301 -0.0042 218  MET   B CE  
4318  N  N   . VAL   B 219 ? 0.9684 1.0567 0.9799 0.0422  -0.1171 -0.0010 219  VAL   B N   
4319  C  CA  . VAL   B 219 ? 0.9663 1.0485 0.9693 0.0470  -0.1162 -0.0016 219  VAL   B CA  
4320  C  C   . VAL   B 219 ? 1.0060 1.0754 0.9970 0.0543  -0.1215 -0.0049 219  VAL   B C   
4321  O  O   . VAL   B 219 ? 1.0215 1.0878 1.0145 0.0533  -0.1285 -0.0090 219  VAL   B O   
4322  C  CB  . VAL   B 219 ? 0.9988 1.0852 1.0080 0.0424  -0.1174 -0.0035 219  VAL   B CB  
4323  C  CG1 . VAL   B 219 ? 1.0313 1.1300 1.0531 0.0344  -0.1139 -0.0011 219  VAL   B CG1 
4324  C  CG2 . VAL   B 219 ? 1.0456 1.1278 1.0561 0.0419  -0.1254 -0.0087 219  VAL   B CG2 
4325  N  N   . ILE   B 220 ? 1.0434 1.1050 1.0222 0.0618  -0.1182 -0.0030 220  ILE   B N   
4326  C  CA  . ILE   B 220 ? 1.0753 1.1231 1.0400 0.0701  -0.1227 -0.0058 220  ILE   B CA  
4327  C  C   . ILE   B 220 ? 1.0845 1.1255 1.0397 0.0748  -0.1214 -0.0063 220  ILE   B C   
4328  O  O   . ILE   B 220 ? 1.0944 1.1371 1.0470 0.0762  -0.1138 -0.0023 220  ILE   B O   
4329  C  CB  . ILE   B 220 ? 1.0749 1.1173 1.0309 0.0760  -0.1194 -0.0031 220  ILE   B CB  
4330  C  CG1 . ILE   B 220 ? 1.0273 1.0715 0.9885 0.0734  -0.1233 -0.0041 220  ILE   B CG1 
4331  C  CG2 . ILE   B 220 ? 1.1167 1.1440 1.0548 0.0860  -0.1208 -0.0044 220  ILE   B CG2 
4332  C  CD1 . ILE   B 220 ? 1.0430 1.0884 1.0017 0.0761  -0.1177 0.0000  220  ILE   B CD1 
4333  N  N   . ALA   B 221 ? 1.1212 1.1542 1.0712 0.0775  -0.1288 -0.0111 221  ALA   B N   
4334  C  CA  . ALA   B 221 ? 1.1036 1.1290 1.0436 0.0825  -0.1286 -0.0122 221  ALA   B CA  
4335  C  C   . ALA   B 221 ? 1.1124 1.1228 1.0336 0.0932  -0.1286 -0.0122 221  ALA   B C   
4336  O  O   . ALA   B 221 ? 1.1816 1.1825 1.0957 0.0976  -0.1360 -0.0161 221  ALA   B O   
4337  C  CB  . ALA   B 221 ? 1.1021 1.1266 1.0464 0.0804  -0.1369 -0.0176 221  ALA   B CB  
4338  N  N   . VAL   B 222 ? 1.1424 1.1500 1.0552 0.0975  -0.1203 -0.0078 222  VAL   B N   
4339  C  CA  . VAL   B 222 ? 1.2099 1.2022 1.1035 0.1082  -0.1193 -0.0074 222  VAL   B CA  
4340  C  C   . VAL   B 222 ? 1.2274 1.2070 1.1087 0.1142  -0.1262 -0.0121 222  VAL   B C   
4341  O  O   . VAL   B 222 ? 1.3119 1.2942 1.1966 0.1116  -0.1267 -0.0132 222  VAL   B O   
4342  C  CB  . VAL   B 222 ? 1.2063 1.1988 1.0947 0.1112  -0.1079 -0.0014 222  VAL   B CB  
4343  C  CG1 . VAL   B 222 ? 1.2639 1.2423 1.1345 0.1216  -0.1060 -0.0002 222  VAL   B CG1 
4344  C  CG2 . VAL   B 222 ? 1.1538 1.1620 1.0586 0.1033  -0.1015 0.0029  222  VAL   B CG2 
4345  N  N   . PRO   B 223 ? 1.2423 1.2077 1.1093 0.1223  -0.1321 -0.0152 223  PRO   B N   
4346  C  CA  . PRO   B 223 ? 1.2980 1.2508 1.1532 0.1283  -0.1401 -0.0203 223  PRO   B CA  
4347  C  C   . PRO   B 223 ? 1.4123 1.3555 1.2524 0.1353  -0.1346 -0.0182 223  PRO   B C   
4348  O  O   . PRO   B 223 ? 1.3858 1.3324 1.2250 0.1352  -0.1239 -0.0125 223  PRO   B O   
4349  C  CB  . PRO   B 223 ? 1.3029 1.2427 1.1462 0.1354  -0.1472 -0.0236 223  PRO   B CB  
4350  C  CG  . PRO   B 223 ? 1.3621 1.3114 1.2170 0.1298  -0.1457 -0.0218 223  PRO   B CG  
4351  C  CD  . PRO   B 223 ? 1.3311 1.2927 1.1946 0.1249  -0.1340 -0.0153 223  PRO   B CD  
4352  N  N   . GLU   B 224 ? 1.5095 1.4398 1.3372 0.1418  -0.1422 -0.0229 224  GLU   B N   
4353  C  CA  . GLU   B 224 ? 1.5779 1.4991 1.3923 0.1477  -0.1390 -0.0220 224  GLU   B CA  
4354  C  C   . GLU   B 224 ? 1.6215 1.5350 1.4213 0.1545  -0.1275 -0.0161 224  GLU   B C   
4355  O  O   . GLU   B 224 ? 1.6783 1.5928 1.4763 0.1544  -0.1202 -0.0128 224  GLU   B O   
4356  C  CB  . GLU   B 224 ? 1.6507 1.5565 1.4512 0.1554  -0.1503 -0.0285 224  GLU   B CB  
4357  C  CG  . GLU   B 224 ? 1.6761 1.5867 1.4856 0.1511  -0.1567 -0.0326 224  GLU   B CG  
4358  C  CD  . GLU   B 224 ? 1.7546 1.6617 1.5560 0.1538  -0.1500 -0.0299 224  GLU   B CD  
4359  O  OE1 . GLU   B 224 ? 1.7316 1.6461 1.5369 0.1505  -0.1386 -0.0238 224  GLU   B OE1 
4360  O  OE2 . GLU   B 224 ? 1.8222 1.7189 1.6132 0.1594  -0.1564 -0.0339 224  GLU   B OE2 
4361  N  N   . PRO   B 225 ? 1.4997 1.4054 1.2890 0.1606  -0.1251 -0.0143 225  PRO   B N   
4362  C  CA  . PRO   B 225 ? 1.4632 1.3607 1.2381 0.1678  -0.1136 -0.0085 225  PRO   B CA  
4363  C  C   . PRO   B 225 ? 1.5163 1.4279 1.3044 0.1608  -0.1017 -0.0023 225  PRO   B C   
4364  O  O   . PRO   B 225 ? 1.5369 1.4442 1.3180 0.1635  -0.0947 0.0006  225  PRO   B O   
4365  C  CB  . PRO   B 225 ? 1.4667 1.3590 1.2352 0.1723  -0.1133 -0.0076 225  PRO   B CB  
4366  C  CG  . PRO   B 225 ? 1.5492 1.4533 1.3352 0.1640  -0.1213 -0.0110 225  PRO   B CG  
4367  C  CD  . PRO   B 225 ? 1.4993 1.4045 1.2909 0.1605  -0.1315 -0.0168 225  PRO   B CD  
4368  N  N   . PHE   B 226 ? 1.4549 1.3829 1.2622 0.1518  -0.0993 -0.0002 226  PHE   B N   
4369  C  CA  . PHE   B 226 ? 1.4134 1.3560 1.2356 0.1442  -0.0896 0.0049  226  PHE   B CA  
4370  C  C   . PHE   B 226 ? 1.4592 1.4122 1.2952 0.1357  -0.0939 0.0023  226  PHE   B C   
4371  O  O   . PHE   B 226 ? 1.5268 1.4800 1.3620 0.1350  -0.0890 0.0042  226  PHE   B O   
4372  C  CB  . PHE   B 226 ? 1.3808 1.3367 1.2177 0.1383  -0.0854 0.0082  226  PHE   B CB  
4373  C  CG  . PHE   B 226 ? 1.4739 1.4212 1.2992 0.1461  -0.0818 0.0105  226  PHE   B CG  
4374  C  CD1 . PHE   B 226 ? 1.4714 1.4105 1.2892 0.1502  -0.0904 0.0064  226  PHE   B CD1 
4375  C  CD2 . PHE   B 226 ? 1.5132 1.4610 1.3364 0.1489  -0.0698 0.0167  226  PHE   B CD2 
4376  C  CE1 . PHE   B 226 ? 1.5076 1.4385 1.3144 0.1575  -0.0872 0.0084  226  PHE   B CE1 
4377  C  CE2 . PHE   B 226 ? 1.5359 1.4760 1.3488 0.1562  -0.0661 0.0189  226  PHE   B CE2 
4378  C  CZ  . PHE   B 226 ? 1.5703 1.5018 1.3746 0.1606  -0.0749 0.0147  226  PHE   B CZ  
4379  N  N   . GLY   B 227 ? 1.4138 1.3751 1.2627 0.1291  -0.1026 -0.0018 227  GLY   B N   
4380  C  CA  . GLY   B 227 ? 1.3483 1.3214 1.2126 0.1202  -0.1059 -0.0038 227  GLY   B CA  
4381  C  C   . GLY   B 227 ? 1.3075 1.2974 1.1897 0.1110  -0.0988 0.0006  227  GLY   B C   
4382  O  O   . GLY   B 227 ? 1.3013 1.2922 1.1819 0.1126  -0.0899 0.0056  227  GLY   B O   
4383  N  N   . GLY   B 228 ? 1.3410 1.3440 1.2404 0.1016  -0.1028 -0.0013 228  GLY   B N   
4384  C  CA  . GLY   B 228 ? 1.3266 1.3451 1.2425 0.0930  -0.0970 0.0025  228  GLY   B CA  
4385  C  C   . GLY   B 228 ? 1.3081 1.3354 1.2364 0.0871  -0.1022 0.0006  228  GLY   B C   
4386  O  O   . GLY   B 228 ? 1.3091 1.3329 1.2371 0.0873  -0.1110 -0.0042 228  GLY   B O   
4387  N  N   . ALA   B 229 ? 1.2145 1.2527 1.1537 0.0820  -0.0967 0.0045  229  ALA   B N   
4388  C  CA  . ALA   B 229 ? 1.0978 1.1447 1.0489 0.0760  -0.1005 0.0035  229  ALA   B CA  
4389  C  C   . ALA   B 229 ? 1.1480 1.2011 1.1035 0.0752  -0.0938 0.0082  229  ALA   B C   
4390  O  O   . ALA   B 229 ? 1.1737 1.2310 1.1316 0.0746  -0.0859 0.0124  229  ALA   B O   
4391  C  CB  . ALA   B 229 ? 1.0943 1.1527 1.0604 0.0667  -0.1031 0.0019  229  ALA   B CB  
4392  N  N   . ILE   B 230 ? 1.1197 1.1729 1.0765 0.0755  -0.0970 0.0075  230  ILE   B N   
4393  C  CA  . ILE   B 230 ? 1.0833 1.1432 1.0457 0.0742  -0.0920 0.0114  230  ILE   B CA  
4394  C  C   . ILE   B 230 ? 1.1458 1.2183 1.1241 0.0650  -0.0944 0.0110  230  ILE   B C   
4395  O  O   . ILE   B 230 ? 1.1004 1.1723 1.0811 0.0628  -0.1012 0.0075  230  ILE   B O   
4396  C  CB  . ILE   B 230 ? 1.0634 1.1142 1.0156 0.0812  -0.0937 0.0110  230  ILE   B CB  
4397  C  CG1 . ILE   B 230 ? 1.1233 1.1622 1.0596 0.0907  -0.0891 0.0128  230  ILE   B CG1 
4398  C  CG2 . ILE   B 230 ? 1.0822 1.1414 1.0429 0.0783  -0.0910 0.0140  230  ILE   B CG2 
4399  C  CD1 . ILE   B 230 ? 1.1264 1.1527 1.0490 0.0987  -0.0926 0.0112  230  ILE   B CD1 
4400  N  N   . ILE   B 231 ? 1.1702 1.2537 1.1591 0.0598  -0.0887 0.0145  231  ILE   B N   
4401  C  CA  . ILE   B 231 ? 1.0750 1.1702 1.0780 0.0515  -0.0901 0.0147  231  ILE   B CA  
4402  C  C   . ILE   B 231 ? 1.0875 1.1858 1.0929 0.0524  -0.0881 0.0173  231  ILE   B C   
4403  O  O   . ILE   B 231 ? 1.1131 1.2140 1.1191 0.0547  -0.0816 0.0212  231  ILE   B O   
4404  C  CB  . ILE   B 231 ? 1.0893 1.1942 1.1021 0.0456  -0.0859 0.0168  231  ILE   B CB  
4405  C  CG1 . ILE   B 231 ? 1.1240 1.2249 1.1331 0.0457  -0.0871 0.0146  231  ILE   B CG1 
4406  C  CG2 . ILE   B 231 ? 1.0268 1.1416 1.0520 0.0376  -0.0885 0.0162  231  ILE   B CG2 
4407  C  CD1 . ILE   B 231 ? 1.0759 1.1718 1.0826 0.0454  -0.0950 0.0097  231  ILE   B CD1 
4408  N  N   . ILE   B 232 ? 1.0856 1.1842 1.0933 0.0506  -0.0934 0.0152  232  ILE   B N   
4409  C  CA  . ILE   B 232 ? 1.1174 1.2190 1.1277 0.0511  -0.0921 0.0174  232  ILE   B CA  
4410  C  C   . ILE   B 232 ? 1.1021 1.2153 1.1258 0.0430  -0.0924 0.0183  232  ILE   B C   
4411  O  O   . ILE   B 232 ? 1.0608 1.1769 1.0899 0.0374  -0.0963 0.0158  232  ILE   B O   
4412  C  CB  . ILE   B 232 ? 1.0363 1.1287 1.0385 0.0553  -0.0974 0.0148  232  ILE   B CB  
4413  C  CG1 . ILE   B 232 ? 1.0561 1.1359 1.0440 0.0634  -0.0983 0.0133  232  ILE   B CG1 
4414  C  CG2 . ILE   B 232 ? 1.0596 1.1543 1.0628 0.0572  -0.0951 0.0176  232  ILE   B CG2 
4415  C  CD1 . ILE   B 232 ? 1.0726 1.1430 1.0508 0.0696  -0.1010 0.0123  232  ILE   B CD1 
4416  N  N   . GLY   B 233 ? 1.1167 1.2364 1.1456 0.0427  -0.0882 0.0218  233  GLY   B N   
4417  C  CA  . GLY   B 233 ? 1.1315 1.2616 1.1719 0.0361  -0.0884 0.0229  233  GLY   B CA  
4418  C  C   . GLY   B 233 ? 1.1876 1.3198 1.2295 0.0378  -0.0877 0.0250  233  GLY   B C   
4419  O  O   . GLY   B 233 ? 1.2094 1.3344 1.2430 0.0440  -0.0878 0.0251  233  GLY   B O   
4420  N  N   . GLN   B 234 ? 1.1955 1.3370 1.2473 0.0328  -0.0871 0.0266  234  GLN   B N   
4421  C  CA  . GLN   B 234 ? 1.2058 1.3496 1.2594 0.0342  -0.0871 0.0283  234  GLN   B CA  
4422  C  C   . GLN   B 234 ? 1.2480 1.3912 1.2991 0.0406  -0.0818 0.0315  234  GLN   B C   
4423  O  O   . GLN   B 234 ? 1.3277 1.4664 1.3734 0.0455  -0.0821 0.0320  234  GLN   B O   
4424  C  CB  . GLN   B 234 ? 1.1125 1.2664 1.1770 0.0280  -0.0875 0.0295  234  GLN   B CB  
4425  N  N   . GLU   B 235 ? 1.2734 1.4206 1.3281 0.0409  -0.0766 0.0337  235  GLU   B N   
4426  C  CA  . GLU   B 235 ? 1.3086 1.4568 1.3633 0.0462  -0.0705 0.0371  235  GLU   B CA  
4427  C  C   . GLU   B 235 ? 1.2742 1.4160 1.3215 0.0511  -0.0659 0.0379  235  GLU   B C   
4428  O  O   . GLU   B 235 ? 1.2866 1.4267 1.3314 0.0568  -0.0605 0.0407  235  GLU   B O   
4429  C  CB  . GLU   B 235 ? 1.3633 1.5237 1.4318 0.0423  -0.0673 0.0400  235  GLU   B CB  
4430  C  CG  . GLU   B 235 ? 1.3960 1.5617 1.4714 0.0363  -0.0666 0.0396  235  GLU   B CG  
4431  C  CD  . GLU   B 235 ? 1.5221 1.6979 1.6097 0.0344  -0.0618 0.0429  235  GLU   B CD  
4432  O  OE1 . GLU   B 235 ? 1.5492 1.7251 1.6372 0.0393  -0.0560 0.0458  235  GLU   B OE1 
4433  O  OE2 . GLU   B 235 ? 1.5697 1.7530 1.6665 0.0280  -0.0637 0.0425  235  GLU   B OE2 
4434  N  N   . SER   B 236 ? 1.1981 1.3358 1.2413 0.0494  -0.0677 0.0356  236  SER   B N   
4435  C  CA  . SER   B 236 ? 1.1754 1.3068 1.2113 0.0538  -0.0632 0.0364  236  SER   B CA  
4436  C  C   . SER   B 236 ? 1.1439 1.2636 1.1670 0.0569  -0.0679 0.0327  236  SER   B C   
4437  O  O   . SER   B 236 ? 1.1305 1.2498 1.1544 0.0529  -0.0743 0.0293  236  SER   B O   
4438  C  CB  . SER   B 236 ? 1.1872 1.3255 1.2315 0.0487  -0.0600 0.0375  236  SER   B CB  
4439  O  OG  . SER   B 236 ? 1.2212 1.3614 1.2684 0.0426  -0.0657 0.0343  236  SER   B OG  
4440  N  N   . ILE   B 237 ? 1.1438 1.2538 1.1553 0.0642  -0.0646 0.0334  237  ILE   B N   
4441  C  CA  . ILE   B 237 ? 1.1601 1.2581 1.1586 0.0681  -0.0689 0.0298  237  ILE   B CA  
4442  C  C   . ILE   B 237 ? 1.1799 1.2749 1.1745 0.0699  -0.0640 0.0310  237  ILE   B C   
4443  O  O   . ILE   B 237 ? 1.2191 1.3089 1.2069 0.0761  -0.0576 0.0339  237  ILE   B O   
4444  C  CB  . ILE   B 237 ? 1.1147 1.2013 1.0998 0.0764  -0.0702 0.0292  237  ILE   B CB  
4445  C  CG1 . ILE   B 237 ? 1.0980 1.1869 1.0867 0.0745  -0.0752 0.0279  237  ILE   B CG1 
4446  C  CG2 . ILE   B 237 ? 1.1199 1.1936 1.0915 0.0808  -0.0750 0.0254  237  ILE   B CG2 
4447  C  CD1 . ILE   B 237 ? 1.1195 1.1964 1.0948 0.0821  -0.0777 0.0265  237  ILE   B CD1 
4448  N  N   . THR   B 238 ? 1.1723 1.2700 1.1710 0.0646  -0.0666 0.0290  238  THR   B N   
4449  C  CA  . THR   B 238 ? 1.1856 1.2812 1.1817 0.0655  -0.0619 0.0302  238  THR   B CA  
4450  C  C   . THR   B 238 ? 1.2136 1.2974 1.1968 0.0694  -0.0663 0.0265  238  THR   B C   
4451  O  O   . THR   B 238 ? 1.1769 1.2575 1.1579 0.0685  -0.0741 0.0224  238  THR   B O   
4452  C  CB  . THR   B 238 ? 1.2039 1.3115 1.2143 0.0570  -0.0604 0.0312  238  THR   B CB  
4453  O  OG1 . THR   B 238 ? 1.2412 1.3453 1.2479 0.0574  -0.0575 0.0314  238  THR   B OG1 
4454  C  CG2 . THR   B 238 ? 1.2794 1.3933 1.2979 0.0498  -0.0678 0.0279  238  THR   B CG2 
4455  N  N   . TYR   B 239 ? 1.3086 1.3854 1.2832 0.0742  -0.0612 0.0281  239  TYR   B N   
4456  C  CA  . TYR   B 239 ? 1.2549 1.3199 1.2164 0.0787  -0.0646 0.0250  239  TYR   B CA  
4457  C  C   . TYR   B 239 ? 1.2777 1.3454 1.2426 0.0754  -0.0613 0.0258  239  TYR   B C   
4458  O  O   . TYR   B 239 ? 1.2913 1.3638 1.2613 0.0743  -0.0533 0.0300  239  TYR   B O   
4459  C  CB  . TYR   B 239 ? 1.2163 1.2672 1.1605 0.0892  -0.0617 0.0260  239  TYR   B CB  
4460  C  CG  . TYR   B 239 ? 1.2681 1.3060 1.1978 0.0946  -0.0645 0.0231  239  TYR   B CG  
4461  C  CD1 . TYR   B 239 ? 1.3159 1.3509 1.2419 0.0960  -0.0586 0.0253  239  TYR   B CD1 
4462  C  CD2 . TYR   B 239 ? 1.2214 1.2496 1.1413 0.0984  -0.0733 0.0183  239  TYR   B CD2 
4463  C  CE1 . TYR   B 239 ? 1.2637 1.2864 1.1757 0.1013  -0.0614 0.0226  239  TYR   B CE1 
4464  C  CE2 . TYR   B 239 ? 1.2335 1.2498 1.1402 0.1036  -0.0766 0.0154  239  TYR   B CE2 
4465  C  CZ  . TYR   B 239 ? 1.2692 1.2827 1.1717 0.1051  -0.0706 0.0177  239  TYR   B CZ  
4466  O  OH  . TYR   B 239 ? 1.3577 1.3587 1.2462 0.1108  -0.0740 0.0148  239  TYR   B OH  
4467  N  N   . HIS   B 240 ? 1.2813 1.3460 1.2438 0.0737  -0.0675 0.0217  240  HIS   B N   
4468  C  CA  . HIS   B 240 ? 1.2962 1.3630 1.2616 0.0703  -0.0657 0.0218  240  HIS   B CA  
4469  C  C   . HIS   B 240 ? 1.3292 1.3828 1.2799 0.0764  -0.0696 0.0184  240  HIS   B C   
4470  O  O   . HIS   B 240 ? 1.3088 1.3572 1.2548 0.0782  -0.0777 0.0141  240  HIS   B O   
4471  C  CB  . HIS   B 240 ? 1.2545 1.3333 1.2348 0.0607  -0.0699 0.0199  240  HIS   B CB  
4472  C  CG  . HIS   B 240 ? 1.2216 1.3132 1.2162 0.0545  -0.0670 0.0227  240  HIS   B CG  
4473  N  ND1 . HIS   B 240 ? 1.1992 1.2991 1.2033 0.0500  -0.0609 0.0261  240  HIS   B ND1 
4474  C  CD2 . HIS   B 240 ? 1.2573 1.3542 1.2580 0.0524  -0.0696 0.0226  240  HIS   B CD2 
4475  C  CE1 . HIS   B 240 ? 1.2932 1.4033 1.3088 0.0454  -0.0603 0.0277  240  HIS   B CE1 
4476  N  NE2 . HIS   B 240 ? 1.3162 1.4245 1.3296 0.0469  -0.0654 0.0257  240  HIS   B NE2 
4477  N  N   . ASN   B 241 ? 1.3885 1.4363 1.3320 0.0796  -0.0640 0.0204  241  ASN   B N   
4478  C  CA  . ASN   B 241 ? 1.3778 1.4140 1.3084 0.0845  -0.0681 0.0171  241  ASN   B CA  
4479  C  C   . ASN   B 241 ? 1.4667 1.5024 1.3965 0.0838  -0.0611 0.0199  241  ASN   B C   
4480  O  O   . ASN   B 241 ? 1.5858 1.6190 1.5120 0.0871  -0.0522 0.0245  241  ASN   B O   
4481  C  CB  . ASN   B 241 ? 1.2858 1.3066 1.1981 0.0949  -0.0696 0.0161  241  ASN   B CB  
4482  C  CG  . ASN   B 241 ? 1.3432 1.3520 1.2426 0.1000  -0.0761 0.0116  241  ASN   B CG  
4483  O  OD1 . ASN   B 241 ? 1.3957 1.4086 1.3012 0.0953  -0.0803 0.0089  241  ASN   B OD1 
4484  N  ND2 . ASN   B 241 ? 1.3555 1.3491 1.2369 0.1098  -0.0774 0.0106  241  ASN   B ND2 
4485  N  N   . GLY   B 242 ? 1.4210 1.4594 1.3549 0.0796  -0.0647 0.0174  242  GLY   B N   
4486  C  CA  . GLY   B 242 ? 1.5611 1.5992 1.4948 0.0784  -0.0584 0.0199  242  GLY   B CA  
4487  C  C   . GLY   B 242 ? 1.7193 1.7646 1.6613 0.0756  -0.0484 0.0257  242  GLY   B C   
4488  O  O   . GLY   B 242 ? 1.7137 1.7724 1.6718 0.0674  -0.0478 0.0267  242  GLY   B O   
4489  N  N   . ASP   B 243 ? 1.9583 1.9946 1.8897 0.0824  -0.0407 0.0293  243  ASP   B N   
4490  C  CA  . ASP   B 243 ? 2.0237 2.0664 1.9635 0.0801  -0.0305 0.0349  243  ASP   B CA  
4491  C  C   . ASP   B 243 ? 2.0152 2.0591 1.9557 0.0833  -0.0273 0.0375  243  ASP   B C   
4492  O  O   . ASP   B 243 ? 2.0191 2.0715 1.9708 0.0801  -0.0202 0.0417  243  ASP   B O   
4493  C  CB  . ASP   B 243 ? 2.0948 2.1276 2.0244 0.0848  -0.0222 0.0381  243  ASP   B CB  
4494  C  CG  . ASP   B 243 ? 2.1571 2.1719 2.0645 0.0958  -0.0230 0.0369  243  ASP   B CG  
4495  O  OD1 . ASP   B 243 ? 2.1180 2.1287 2.0189 0.0998  -0.0293 0.0340  243  ASP   B OD1 
4496  O  OD2 . ASP   B 243 ? 2.2476 2.2520 2.1437 0.1004  -0.0175 0.0387  243  ASP   B OD2 
4497  N  N   . LYS   B 244 ? 1.7629 1.7984 1.6921 0.0896  -0.0323 0.0350  244  LYS   B N   
4498  C  CA  . LYS   B 244 ? 1.6629 1.6999 1.5930 0.0924  -0.0299 0.0371  244  LYS   B CA  
4499  C  C   . LYS   B 244 ? 1.5868 1.6390 1.5347 0.0841  -0.0342 0.0363  244  LYS   B C   
4500  O  O   . LYS   B 244 ? 1.5149 1.5716 1.4679 0.0792  -0.0426 0.0322  244  LYS   B O   
4501  C  CB  . LYS   B 244 ? 1.5620 1.5849 1.4743 0.1016  -0.0348 0.0344  244  LYS   B CB  
4502  N  N   . TYR   B 245 ? 1.5027 1.5629 1.4602 0.0826  -0.0281 0.0403  245  TYR   B N   
4503  C  CA  . TYR   B 245 ? 1.4282 1.5021 1.4015 0.0756  -0.0315 0.0400  245  TYR   B CA  
4504  C  C   . TYR   B 245 ? 1.3808 1.4552 1.3543 0.0800  -0.0263 0.0434  245  TYR   B C   
4505  O  O   . TYR   B 245 ? 1.4228 1.5015 1.4028 0.0799  -0.0175 0.0480  245  TYR   B O   
4506  C  CB  . TYR   B 245 ? 1.4265 1.5137 1.4168 0.0664  -0.0297 0.0413  245  TYR   B CB  
4507  C  CG  . TYR   B 245 ? 1.4246 1.5258 1.4313 0.0601  -0.0308 0.0422  245  TYR   B CG  
4508  C  CD1 . TYR   B 245 ? 1.4115 1.5136 1.4178 0.0609  -0.0363 0.0404  245  TYR   B CD1 
4509  C  CD2 . TYR   B 245 ? 1.4203 1.5330 1.4424 0.0534  -0.0267 0.0449  245  TYR   B CD2 
4510  C  CE1 . TYR   B 245 ? 1.4238 1.5377 1.4439 0.0557  -0.0374 0.0413  245  TYR   B CE1 
4511  C  CE2 . TYR   B 245 ? 1.5018 1.6266 1.5382 0.0481  -0.0283 0.0456  245  TYR   B CE2 
4512  C  CZ  . TYR   B 245 ? 1.4785 1.6037 1.5133 0.0494  -0.0336 0.0438  245  TYR   B CZ  
4513  O  OH  . TYR   B 245 ? 1.4207 1.5568 1.4681 0.0449  -0.0355 0.0444  245  TYR   B OH  
4514  N  N   . LEU   B 246 ? 1.3810 1.4505 1.3473 0.0841  -0.0314 0.0413  246  LEU   B N   
4515  C  CA  . LEU   B 246 ? 1.3161 1.3860 1.2823 0.0883  -0.0274 0.0441  246  LEU   B CA  
4516  C  C   . LEU   B 246 ? 1.2883 1.3684 1.2659 0.0828  -0.0337 0.0423  246  LEU   B C   
4517  O  O   . LEU   B 246 ? 1.3027 1.3800 1.2765 0.0819  -0.0424 0.0380  246  LEU   B O   
4518  C  CB  . LEU   B 246 ? 1.2644 1.3181 1.2106 0.0989  -0.0274 0.0434  246  LEU   B CB  
4519  C  CG  . LEU   B 246 ? 1.4021 1.4548 1.3465 0.1043  -0.0224 0.0466  246  LEU   B CG  
4520  C  CD1 . LEU   B 246 ? 1.3546 1.4193 1.3145 0.1009  -0.0132 0.0518  246  LEU   B CD1 
4521  C  CD2 . LEU   B 246 ? 1.4677 1.5029 1.3909 0.1155  -0.0192 0.0471  246  LEU   B CD2 
4522  N  N   . ALA   B 247 ? 1.2487 1.3405 1.2404 0.0792  -0.0294 0.0456  247  ALA   B N   
4523  C  CA  . ALA   B 247 ? 1.2083 1.3103 1.2115 0.0737  -0.0346 0.0445  247  ALA   B CA  
4524  C  C   . ALA   B 247 ? 1.2122 1.3165 1.2178 0.0776  -0.0304 0.0476  247  ALA   B C   
4525  O  O   . ALA   B 247 ? 1.2376 1.3447 1.2477 0.0796  -0.0219 0.0519  247  ALA   B O   
4526  C  CB  . ALA   B 247 ? 1.1607 1.2762 1.1808 0.0641  -0.0352 0.0448  247  ALA   B CB  
4527  N  N   . ILE   B 248 ? 1.2160 1.3194 1.2193 0.0786  -0.0363 0.0455  248  ILE   B N   
4528  C  CA  . ILE   B 248 ? 1.1531 1.2590 1.1589 0.0820  -0.0336 0.0480  248  ILE   B CA  
4529  C  C   . ILE   B 248 ? 1.1915 1.3077 1.2089 0.0756  -0.0397 0.0465  248  ILE   B C   
4530  O  O   . ILE   B 248 ? 1.1388 1.2564 1.1580 0.0702  -0.0468 0.0429  248  ILE   B O   
4531  C  CB  . ILE   B 248 ? 1.1537 1.2457 1.1421 0.0914  -0.0343 0.0471  248  ILE   B CB  
4532  C  CG1 . ILE   B 248 ? 1.1702 1.2569 1.1522 0.0904  -0.0446 0.0421  248  ILE   B CG1 
4533  C  CG2 . ILE   B 248 ? 1.2503 1.3303 1.2248 0.0980  -0.0295 0.0480  248  ILE   B CG2 
4534  C  CD1 . ILE   B 248 ? 1.2444 1.3189 1.2115 0.0989  -0.0464 0.0411  248  ILE   B CD1 
4535  N  N   . ALA   B 249 ? 1.2258 1.3488 1.2512 0.0764  -0.0366 0.0493  249  ALA   B N   
4536  C  CA  . ALA   B 249 ? 1.2018 1.3326 1.2358 0.0722  -0.0419 0.0483  249  ALA   B CA  
4537  C  C   . ALA   B 249 ? 1.2530 1.3793 1.2808 0.0790  -0.0410 0.0494  249  ALA   B C   
4538  O  O   . ALA   B 249 ? 1.2861 1.4190 1.3218 0.0806  -0.0360 0.0528  249  ALA   B O   
4539  C  CB  . ALA   B 249 ? 1.0885 1.2340 1.1407 0.0653  -0.0399 0.0504  249  ALA   B CB  
4540  N  N   . PRO   B 250 ? 1.2750 1.3902 1.2892 0.0831  -0.0460 0.0465  250  PRO   B N   
4541  C  CA  . PRO   B 250 ? 1.2934 1.4030 1.3002 0.0899  -0.0458 0.0473  250  PRO   B CA  
4542  C  C   . PRO   B 250 ? 1.3016 1.4209 1.3196 0.0860  -0.0486 0.0477  250  PRO   B C   
4543  O  O   . PRO   B 250 ? 1.3132 1.4359 1.3355 0.0798  -0.0554 0.0449  250  PRO   B O   
4544  C  CB  . PRO   B 250 ? 1.3402 1.4361 1.3313 0.0932  -0.0525 0.0430  250  PRO   B CB  
4545  C  CG  . PRO   B 250 ? 1.3057 1.4037 1.3004 0.0860  -0.0580 0.0397  250  PRO   B CG  
4546  C  CD  . PRO   B 250 ? 1.2784 1.3858 1.2839 0.0816  -0.0525 0.0422  250  PRO   B CD  
4547  N  N   . PRO   B 251 ? 1.3060 1.4294 1.3284 0.0897  -0.0435 0.0511  251  PRO   B N   
4548  C  CA  . PRO   B 251 ? 1.3299 1.4611 1.3611 0.0873  -0.0465 0.0514  251  PRO   B CA  
4549  C  C   . PRO   B 251 ? 1.2932 1.4164 1.3148 0.0883  -0.0541 0.0481  251  PRO   B C   
4550  O  O   . PRO   B 251 ? 1.2901 1.4185 1.3179 0.0833  -0.0594 0.0466  251  PRO   B O   
4551  C  CB  . PRO   B 251 ? 1.3420 1.4757 1.3760 0.0937  -0.0390 0.0556  251  PRO   B CB  
4552  C  CG  . PRO   B 251 ? 1.3430 1.4743 1.3751 0.0968  -0.0311 0.0581  251  PRO   B CG  
4553  C  CD  . PRO   B 251 ? 1.3315 1.4516 1.3502 0.0971  -0.0345 0.0549  251  PRO   B CD  
4554  N  N   . ILE   B 252 ? 1.2800 1.3897 1.2858 0.0950  -0.0548 0.0466  252  ILE   B N   
4555  C  CA  . ILE   B 252 ? 1.2591 1.3603 1.2556 0.0969  -0.0615 0.0437  252  ILE   B CA  
4556  C  C   . ILE   B 252 ? 1.2907 1.3930 1.2901 0.0892  -0.0693 0.0398  252  ILE   B C   
4557  O  O   . ILE   B 252 ? 1.3558 1.4568 1.3548 0.0874  -0.0748 0.0379  252  ILE   B O   
4558  C  CB  . ILE   B 252 ? 1.2838 1.3696 1.2625 0.1057  -0.0609 0.0427  252  ILE   B CB  
4559  C  CG1 . ILE   B 252 ? 1.3878 1.4731 1.3644 0.1132  -0.0516 0.0471  252  ILE   B CG1 
4560  C  CG2 . ILE   B 252 ? 1.2042 1.2812 1.1737 0.1084  -0.0674 0.0400  252  ILE   B CG2 
4561  C  CD1 . ILE   B 252 ? 1.3039 1.3953 1.2873 0.1121  -0.0439 0.0501  252  ILE   B CD1 
4562  N  N   . ILE   B 253 ? 1.2659 1.3705 1.2685 0.0845  -0.0696 0.0386  253  ILE   B N   
4563  C  CA  . ILE   B 253 ? 1.2910 1.3960 1.2960 0.0778  -0.0766 0.0349  253  ILE   B CA  
4564  C  C   . ILE   B 253 ? 1.4010 1.5182 1.4201 0.0698  -0.0780 0.0355  253  ILE   B C   
4565  O  O   . ILE   B 253 ? 1.4240 1.5417 1.4454 0.0641  -0.0835 0.0327  253  ILE   B O   
4566  C  CB  . ILE   B 253 ? 1.2144 1.3166 1.2170 0.0757  -0.0772 0.0329  253  ILE   B CB  
4567  C  CG1 . ILE   B 253 ? 1.2640 1.3779 1.2792 0.0695  -0.0736 0.0348  253  ILE   B CG1 
4568  C  CG2 . ILE   B 253 ? 1.2607 1.3516 1.2497 0.0839  -0.0744 0.0330  253  ILE   B CG2 
4569  C  CD1 . ILE   B 253 ? 1.1695 1.2821 1.1844 0.0654  -0.0762 0.0321  253  ILE   B CD1 
4570  N  N   . LYS   B 254 ? 1.3517 1.4787 1.3804 0.0692  -0.0734 0.0390  254  LYS   B N   
4571  C  CA  . LYS   B 254 ? 1.3411 1.4793 1.3827 0.0619  -0.0751 0.0393  254  LYS   B CA  
4572  C  C   . LYS   B 254 ? 1.4123 1.5511 1.4549 0.0614  -0.0789 0.0390  254  LYS   B C   
4573  O  O   . LYS   B 254 ? 1.4406 1.5887 1.4933 0.0571  -0.0795 0.0401  254  LYS   B O   
4574  C  CB  . LYS   B 254 ? 1.3660 1.5147 1.4189 0.0608  -0.0690 0.0428  254  LYS   B CB  
4575  C  CG  . LYS   B 254 ? 1.3457 1.4953 1.3988 0.0675  -0.0636 0.0461  254  LYS   B CG  
4576  C  CD  . LYS   B 254 ? 1.4025 1.5628 1.4684 0.0656  -0.0577 0.0493  254  LYS   B CD  
4577  C  CE  . LYS   B 254 ? 1.4714 1.6369 1.5432 0.0701  -0.0536 0.0526  254  LYS   B CE  
4578  N  NZ  . LYS   B 254 ? 1.5467 1.7220 1.6315 0.0688  -0.0472 0.0558  254  LYS   B NZ  
4579  N  N   . GLN   B 255 ? 1.5888 1.7176 1.6207 0.0658  -0.0819 0.0374  255  GLN   B N   
4580  C  CA  . GLN   B 255 ? 1.6428 1.7706 1.6742 0.0652  -0.0860 0.0368  255  GLN   B CA  
4581  C  C   . GLN   B 255 ? 1.6256 1.7495 1.6555 0.0598  -0.0923 0.0334  255  GLN   B C   
4582  O  O   . GLN   B 255 ? 1.5936 1.7196 1.6267 0.0567  -0.0953 0.0331  255  GLN   B O   
4583  C  CB  . GLN   B 255 ? 1.6386 1.7573 1.6595 0.0734  -0.0855 0.0373  255  GLN   B CB  
4584  C  CG  . GLN   B 255 ? 1.6673 1.7914 1.6921 0.0782  -0.0801 0.0411  255  GLN   B CG  
4585  C  CD  . GLN   B 255 ? 1.6810 1.8092 1.7103 0.0772  -0.0826 0.0419  255  GLN   B CD  
4586  O  OE1 . GLN   B 255 ? 1.6575 1.7832 1.6856 0.0733  -0.0880 0.0397  255  GLN   B OE1 
4587  N  NE2 . GLN   B 255 ? 1.6956 1.8301 1.7304 0.0809  -0.0784 0.0450  255  GLN   B NE2 
4588  N  N   . SER   B 256 ? 1.4838 1.6019 1.5089 0.0588  -0.0942 0.0307  256  SER   B N   
4589  C  CA  . SER   B 256 ? 1.3946 1.5091 1.4193 0.0537  -0.0998 0.0273  256  SER   B CA  
4590  C  C   . SER   B 256 ? 1.2814 1.3944 1.3053 0.0519  -0.1000 0.0253  256  SER   B C   
4591  O  O   . SER   B 256 ? 1.2057 1.3175 1.2263 0.0559  -0.0963 0.0263  256  SER   B O   
4592  C  CB  . SER   B 256 ? 1.3056 1.4091 1.3211 0.0571  -0.1042 0.0251  256  SER   B CB  
4593  O  OG  . SER   B 256 ? 1.2090 1.3093 1.2255 0.0518  -0.1092 0.0219  256  SER   B OG  
4594  N  N   . THR   B 257 ? 1.2008 1.3136 1.2278 0.0461  -0.1040 0.0226  257  THR   B N   
4595  C  CA  . THR   B 257 ? 1.1300 1.2433 1.1585 0.0432  -0.1045 0.0207  257  THR   B CA  
4596  C  C   . THR   B 257 ? 1.1267 1.2289 1.1459 0.0469  -0.1081 0.0174  257  THR   B C   
4597  O  O   . THR   B 257 ? 1.1950 1.2901 1.2100 0.0478  -0.1125 0.0152  257  THR   B O   
4598  C  CB  . THR   B 257 ? 1.1401 1.2593 1.1773 0.0351  -0.1066 0.0196  257  THR   B CB  
4599  O  OG1 . THR   B 257 ? 1.1926 1.3212 1.2373 0.0323  -0.1039 0.0225  257  THR   B OG1 
4600  C  CG2 . THR   B 257 ? 1.1884 1.3091 1.2279 0.0321  -0.1067 0.0179  257  THR   B CG2 
4601  N  N   . ILE   B 258 ? 1.1380 1.2383 1.1540 0.0490  -0.1065 0.0169  258  ILE   B N   
4602  C  CA  . ILE   B 258 ? 1.1083 1.1978 1.1150 0.0531  -0.1102 0.0135  258  ILE   B CA  
4603  C  C   . ILE   B 258 ? 1.0949 1.1845 1.1066 0.0472  -0.1153 0.0098  258  ILE   B C   
4604  O  O   . ILE   B 258 ? 1.1251 1.2225 1.1450 0.0415  -0.1140 0.0101  258  ILE   B O   
4605  C  CB  . ILE   B 258 ? 1.1098 1.1966 1.1102 0.0581  -0.1063 0.0145  258  ILE   B CB  
4606  C  CG1 . ILE   B 258 ? 1.1284 1.2162 1.1255 0.0637  -0.1001 0.0187  258  ILE   B CG1 
4607  C  CG2 . ILE   B 258 ? 1.0790 1.1532 1.0678 0.0637  -0.1105 0.0111  258  ILE   B CG2 
4608  C  CD1 . ILE   B 258 ? 1.0257 1.1034 1.0118 0.0710  -0.1014 0.0184  258  ILE   B CD1 
4609  N  N   . VAL   B 259 ? 1.1141 1.1951 1.1213 0.0485  -0.1211 0.0063  259  VAL   B N   
4610  C  CA  . VAL   B 259 ? 1.1114 1.1920 1.1242 0.0431  -0.1262 0.0027  259  VAL   B CA  
4611  C  C   . VAL   B 259 ? 1.1359 1.2057 1.1412 0.0473  -0.1317 -0.0016 259  VAL   B C   
4612  O  O   . VAL   B 259 ? 1.1772 1.2469 1.1877 0.0434  -0.1359 -0.0049 259  VAL   B O   
4613  C  CB  . VAL   B 259 ? 1.1182 1.2008 1.1373 0.0382  -0.1283 0.0025  259  VAL   B CB  
4614  C  CG1 . VAL   B 259 ? 1.1474 1.2414 1.1762 0.0321  -0.1242 0.0054  259  VAL   B CG1 
4615  C  CG2 . VAL   B 259 ? 1.0640 1.1406 1.0759 0.0432  -0.1286 0.0036  259  VAL   B CG2 
4616  N  N   . CYS   B 260 ? 1.1299 1.1903 1.1233 0.0551  -0.1323 -0.0018 260  CYS   B N   
4617  C  CA  . CYS   B 260 ? 1.1375 1.1862 1.1219 0.0601  -0.1381 -0.0059 260  CYS   B CA  
4618  C  C   . CYS   B 260 ? 1.1500 1.1940 1.1241 0.0669  -0.1352 -0.0051 260  CYS   B C   
4619  O  O   . CYS   B 260 ? 1.1534 1.1999 1.1240 0.0701  -0.1287 -0.0010 260  CYS   B O   
4620  C  CB  . CYS   B 260 ? 1.1523 1.1907 1.1285 0.0649  -0.1421 -0.0074 260  CYS   B CB  
4621  S  SG  . CYS   B 260 ? 1.2249 1.2644 1.2095 0.0590  -0.1461 -0.0087 260  CYS   B SG  
4622  N  N   . HIS   B 261 ? 1.0792 1.1152 1.0476 0.0698  -0.1403 -0.0090 261  HIS   B N   
4623  C  CA  . HIS   B 261 ? 1.0630 1.0902 1.0177 0.0781  -0.1387 -0.0087 261  HIS   B CA  
4624  C  C   . HIS   B 261 ? 1.0705 1.0857 1.0176 0.0821  -0.1473 -0.0143 261  HIS   B C   
4625  O  O   . HIS   B 261 ? 1.1218 1.1390 1.0775 0.0769  -0.1529 -0.0179 261  HIS   B O   
4626  C  CB  . HIS   B 261 ? 1.0768 1.1109 1.0342 0.0766  -0.1329 -0.0063 261  HIS   B CB  
4627  C  CG  . HIS   B 261 ? 1.0459 1.0815 1.0088 0.0727  -0.1372 -0.0099 261  HIS   B CG  
4628  N  ND1 . HIS   B 261 ? 1.1122 1.1588 1.0899 0.0638  -0.1375 -0.0101 261  HIS   B ND1 
4629  C  CD2 . HIS   B 261 ? 1.0115 1.0385 0.9670 0.0768  -0.1419 -0.0136 261  HIS   B CD2 
4630  C  CE1 . HIS   B 261 ? 1.1496 1.1950 1.1294 0.0624  -0.1417 -0.0137 261  HIS   B CE1 
4631  N  NE2 . HIS   B 261 ? 1.1178 1.1514 1.0845 0.0702  -0.1448 -0.0159 261  HIS   B NE2 
4632  N  N   . ASN   B 262 ? 1.0434 1.0459 0.9746 0.0913  -0.1483 -0.0149 262  ASN   B N   
4633  C  CA  . ASN   B 262 ? 1.0909 1.0807 1.0124 0.0966  -0.1562 -0.0200 262  ASN   B CA  
4634  C  C   . ASN   B 262 ? 1.1530 1.1340 1.0587 0.1054  -0.1524 -0.0186 262  ASN   B C   
4635  O  O   . ASN   B 262 ? 1.1511 1.1320 1.0504 0.1094  -0.1448 -0.0140 262  ASN   B O   
4636  C  CB  . ASN   B 262 ? 1.1089 1.0880 1.0243 0.0999  -0.1635 -0.0234 262  ASN   B CB  
4637  C  CG  . ASN   B 262 ? 1.2196 1.1866 1.1280 0.1040  -0.1733 -0.0296 262  ASN   B CG  
4638  O  OD1 . ASN   B 262 ? 1.2368 1.1896 1.1286 0.1131  -0.1762 -0.0313 262  ASN   B OD1 
4639  N  ND2 . ASN   B 262 ? 1.2446 1.2171 1.1658 0.0974  -0.1786 -0.0332 262  ASN   B ND2 
4640  N  N   . ARG   B 263 ? 1.1865 1.1603 1.0862 0.1084  -0.1574 -0.0223 263  ARG   B N   
4641  C  CA  . ARG   B 263 ? 1.2217 1.1849 1.1044 0.1176  -0.1544 -0.0213 263  ARG   B CA  
4642  C  C   . ARG   B 263 ? 1.3238 1.2699 1.1891 0.1271  -0.1599 -0.0241 263  ARG   B C   
4643  O  O   . ARG   B 263 ? 1.3289 1.2681 1.1937 0.1275  -0.1700 -0.0296 263  ARG   B O   
4644  C  CB  . ARG   B 263 ? 1.2112 1.1738 1.0941 0.1171  -0.1570 -0.0239 263  ARG   B CB  
4645  C  CG  . ARG   B 263 ? 1.2917 1.2486 1.1613 0.1240  -0.1497 -0.0206 263  ARG   B CG  
4646  C  CD  . ARG   B 263 ? 1.2734 1.2193 1.1322 0.1294  -0.1555 -0.0248 263  ARG   B CD  
4647  N  NE  . ARG   B 263 ? 1.2467 1.2021 1.1196 0.1218  -0.1590 -0.0273 263  ARG   B NE  
4648  C  CZ  . ARG   B 263 ? 1.2100 1.1628 1.0873 0.1202  -0.1693 -0.0332 263  ARG   B CZ  
4649  N  NH1 . ARG   B 263 ? 1.2205 1.1609 1.0889 0.1258  -0.1780 -0.0377 263  ARG   B NH1 
4650  N  NH2 . ARG   B 263 ? 1.1711 1.1339 1.0625 0.1130  -0.1711 -0.0348 263  ARG   B NH2 
4651  N  N   . VAL   B 264 ? 1.3067 1.2458 1.1582 0.1349  -0.1534 -0.0203 264  VAL   B N   
4652  C  CA  . VAL   B 264 ? 1.3154 1.2374 1.1487 0.1446  -0.1578 -0.0226 264  VAL   B CA  
4653  C  C   . VAL   B 264 ? 1.4298 1.3373 1.2470 0.1527  -0.1623 -0.0259 264  VAL   B C   
4654  O  O   . VAL   B 264 ? 1.4737 1.3740 1.2893 0.1534  -0.1730 -0.0320 264  VAL   B O   
4655  C  CB  . VAL   B 264 ? 1.3759 1.2959 1.2007 0.1501  -0.1487 -0.0171 264  VAL   B CB  
4656  C  CG1 . VAL   B 264 ? 1.4584 1.3584 1.2596 0.1625  -0.1509 -0.0186 264  VAL   B CG1 
4657  C  CG2 . VAL   B 264 ? 1.3512 1.2799 1.1879 0.1443  -0.1486 -0.0158 264  VAL   B CG2 
4658  N  N   . ASP   B 265 ? 1.5323 1.4355 1.3379 0.1588  -0.1540 -0.0221 265  ASP   B N   
4659  C  CA  . ASP   B 265 ? 1.5981 1.4861 1.3858 0.1676  -0.1572 -0.0248 265  ASP   B CA  
4660  C  C   . ASP   B 265 ? 1.6037 1.4980 1.4008 0.1622  -0.1608 -0.0274 265  ASP   B C   
4661  O  O   . ASP   B 265 ? 1.5563 1.4660 1.3690 0.1539  -0.1549 -0.0243 265  ASP   B O   
4662  C  CB  . ASP   B 265 ? 1.6308 1.5115 1.4025 0.1761  -0.1461 -0.0193 265  ASP   B CB  
4663  C  CG  . ASP   B 265 ? 1.6374 1.5347 1.4228 0.1696  -0.1338 -0.0127 265  ASP   B CG  
4664  O  OD1 . ASP   B 265 ? 1.6055 1.5154 1.4062 0.1611  -0.1338 -0.0129 265  ASP   B OD1 
4665  O  OD2 . ASP   B 265 ? 1.6570 1.5542 1.4378 0.1733  -0.1244 -0.0074 265  ASP   B OD2 
4666  N  N   . PRO   B 266 ? 1.6017 1.4842 1.3898 0.1668  -0.1708 -0.0333 266  PRO   B N   
4667  C  CA  . PRO   B 266 ? 1.5533 1.4414 1.3501 0.1622  -0.1744 -0.0360 266  PRO   B CA  
4668  C  C   . PRO   B 266 ? 1.5447 1.4375 1.3400 0.1621  -0.1640 -0.0311 266  PRO   B C   
4669  O  O   . PRO   B 266 ? 1.5157 1.4192 1.3242 0.1551  -0.1641 -0.0316 266  PRO   B O   
4670  C  CB  . PRO   B 266 ? 1.5826 1.4531 1.3643 0.1704  -0.1861 -0.0426 266  PRO   B CB  
4671  C  CG  . PRO   B 266 ? 1.5611 1.4230 1.3372 0.1738  -0.1922 -0.0451 266  PRO   B CG  
4672  C  CD  . PRO   B 266 ? 1.5759 1.4410 1.3489 0.1749  -0.1809 -0.0385 266  PRO   B CD  
4673  N  N   . ASN   B 267 ? 1.5929 1.4781 1.3731 0.1696  -0.1547 -0.0263 267  ASN   B N   
4674  C  CA  . ASN   B 267 ? 1.5341 1.4245 1.3145 0.1689  -0.1441 -0.0212 267  ASN   B CA  
4675  C  C   . ASN   B 267 ? 1.4711 1.3813 1.2718 0.1586  -0.1354 -0.0161 267  ASN   B C   
4676  O  O   . ASN   B 267 ? 1.4231 1.3406 1.2290 0.1555  -0.1278 -0.0126 267  ASN   B O   
4677  C  CB  . ASN   B 267 ? 1.5646 1.4399 1.3225 0.1804  -0.1364 -0.0175 267  ASN   B CB  
4678  C  CG  . ASN   B 267 ? 1.6064 1.4830 1.3629 0.1822  -0.1291 -0.0130 267  ASN   B CG  
4679  O  OD1 . ASN   B 267 ? 1.5877 1.4794 1.3590 0.1754  -0.1206 -0.0081 267  ASN   B OD1 
4680  N  ND2 . ASN   B 267 ? 1.6039 1.4646 1.3427 0.1916  -0.1327 -0.0147 267  ASN   B ND2 
4681  N  N   . GLY   B 268 ? 1.4865 1.4049 1.2982 0.1537  -0.1363 -0.0156 268  GLY   B N   
4682  C  CA  . GLY   B 268 ? 1.4238 1.3611 1.2557 0.1435  -0.1298 -0.0116 268  GLY   B CA  
4683  C  C   . GLY   B 268 ? 1.3996 1.3417 1.2312 0.1447  -0.1171 -0.0047 268  GLY   B C   
4684  O  O   . GLY   B 268 ? 1.3701 1.3255 1.2148 0.1379  -0.1105 -0.0012 268  GLY   B O   
4685  N  N   . SER   B 269 ? 1.4314 1.3630 1.2487 0.1532  -0.1136 -0.0026 269  SER   B N   
4686  C  CA  . SER   B 269 ? 1.3965 1.3329 1.2146 0.1547  -0.1017 0.0040  269  SER   B CA  
4687  C  C   . SER   B 269 ? 1.4139 1.3545 1.2371 0.1536  -0.1014 0.0053  269  SER   B C   
4688  O  O   . SER   B 269 ? 1.3806 1.3252 1.2050 0.1552  -0.0921 0.0105  269  SER   B O   
4689  C  CB  . SER   B 269 ? 1.4536 1.3742 1.2504 0.1661  -0.0955 0.0063  269  SER   B CB  
4690  O  OG  . SER   B 269 ? 1.5373 1.4405 1.3159 0.1750  -0.1030 0.0023  269  SER   B OG  
4691  N  N   . ARG   B 270 ? 1.4514 1.3912 1.2780 0.1510  -0.1114 0.0006  270  ARG   B N   
4692  C  CA  . ARG   B 270 ? 1.3600 1.3059 1.1947 0.1479  -0.1122 0.0014  270  ARG   B CA  
4693  C  C   . ARG   B 270 ? 1.2703 1.2260 1.1213 0.1381  -0.1205 -0.0025 270  ARG   B C   
4694  O  O   . ARG   B 270 ? 1.2406 1.1895 1.0886 0.1382  -0.1302 -0.0079 270  ARG   B O   
4695  C  CB  . ARG   B 270 ? 1.4141 1.3442 1.2313 0.1576  -0.1153 -0.0001 270  ARG   B CB  
4696  C  CG  . ARG   B 270 ? 1.5052 1.4275 1.3083 0.1668  -0.1053 0.0048  270  ARG   B CG  
4697  C  CD  . ARG   B 270 ? 1.5672 1.4761 1.3553 0.1755  -0.1076 0.0040  270  ARG   B CD  
4698  N  NE  . ARG   B 270 ? 1.6759 1.5678 1.4480 0.1817  -0.1178 -0.0019 270  ARG   B NE  
4699  C  CZ  . ARG   B 270 ? 1.8525 1.7296 1.6089 0.1900  -0.1220 -0.0040 270  ARG   B CZ  
4700  N  NH1 . ARG   B 270 ? 1.9664 1.8437 1.7208 0.1930  -0.1167 -0.0006 270  ARG   B NH1 
4701  N  NH2 . ARG   B 270 ? 1.8203 1.6821 1.5630 0.1953  -0.1322 -0.0098 270  ARG   B NH2 
4702  N  N   . TYR   B 271 ? 1.2008 1.1725 1.0691 0.1296  -0.1166 0.0005  271  TYR   B N   
4703  C  CA  . TYR   B 271 ? 1.1718 1.1541 1.0566 0.1198  -0.1224 -0.0021 271  TYR   B CA  
4704  C  C   . TYR   B 271 ? 1.2042 1.1909 1.0944 0.1179  -0.1217 -0.0004 271  TYR   B C   
4705  O  O   . TYR   B 271 ? 1.2199 1.2119 1.1118 0.1191  -0.1137 0.0045  271  TYR   B O   
4706  C  CB  . TYR   B 271 ? 1.1692 1.1664 1.0695 0.1111  -0.1182 0.0000  271  TYR   B CB  
4707  C  CG  . TYR   B 271 ? 1.2022 1.1967 1.1005 0.1108  -0.1208 -0.0027 271  TYR   B CG  
4708  C  CD1 . TYR   B 271 ? 1.1843 1.1804 1.0898 0.1056  -0.1293 -0.0076 271  TYR   B CD1 
4709  C  CD2 . TYR   B 271 ? 1.1813 1.1714 1.0705 0.1158  -0.1147 -0.0003 271  TYR   B CD2 
4710  C  CE1 . TYR   B 271 ? 1.2328 1.2263 1.1365 0.1058  -0.1321 -0.0102 271  TYR   B CE1 
4711  C  CE2 . TYR   B 271 ? 1.1903 1.1772 1.0769 0.1159  -0.1173 -0.0028 271  TYR   B CE2 
4712  C  CZ  . TYR   B 271 ? 1.2464 1.2352 1.1402 0.1110  -0.1262 -0.0078 271  TYR   B CZ  
4713  O  OH  . TYR   B 271 ? 1.2407 1.2266 1.1323 0.1112  -0.1290 -0.0104 271  TYR   B OH  
4714  N  N   . LEU   B 272 ? 1.1986 1.1832 1.0921 0.1152  -0.1300 -0.0043 272  LEU   B N   
4715  C  CA  . LEU   B 272 ? 1.0903 1.0804 0.9908 0.1120  -0.1295 -0.0028 272  LEU   B CA  
4716  C  C   . LEU   B 272 ? 1.1035 1.1102 1.0229 0.1015  -0.1273 -0.0010 272  LEU   B C   
4717  O  O   . LEU   B 272 ? 1.1306 1.1422 1.0584 0.0956  -0.1305 -0.0034 272  LEU   B O   
4718  C  CB  . LEU   B 272 ? 1.0708 1.0520 0.9679 0.1128  -0.1389 -0.0075 272  LEU   B CB  
4719  C  CG  . LEU   B 272 ? 1.1411 1.1049 1.0191 0.1233  -0.1423 -0.0095 272  LEU   B CG  
4720  C  CD1 . LEU   B 272 ? 1.0834 1.0410 0.9624 0.1217  -0.1520 -0.0143 272  LEU   B CD1 
4721  C  CD2 . LEU   B 272 ? 1.1877 1.1503 1.0585 0.1291  -0.1344 -0.0046 272  LEU   B CD2 
4722  N  N   . LEU   B 273 ? 1.1165 1.1314 1.0423 0.0994  -0.1221 0.0029  273  LEU   B N   
4723  C  CA  . LEU   B 273 ? 1.1144 1.1442 1.0570 0.0900  -0.1202 0.0046  273  LEU   B CA  
4724  C  C   . LEU   B 273 ? 1.0938 1.1262 1.0410 0.0876  -0.1216 0.0053  273  LEU   B C   
4725  O  O   . LEU   B 273 ? 1.0989 1.1266 1.0388 0.0934  -0.1194 0.0072  273  LEU   B O   
4726  C  CB  . LEU   B 273 ? 1.1048 1.1446 1.0529 0.0888  -0.1113 0.0094  273  LEU   B CB  
4727  C  CG  . LEU   B 273 ? 1.0779 1.1174 1.0240 0.0894  -0.1088 0.0094  273  LEU   B CG  
4728  C  CD1 . LEU   B 273 ? 1.0234 1.0744 0.9781 0.0866  -0.1003 0.0142  273  LEU   B CD1 
4729  C  CD2 . LEU   B 273 ? 1.0858 1.1263 1.0375 0.0837  -0.1155 0.0050  273  LEU   B CD2 
4730  N  N   . GLY   B 274 ? 1.1069 1.1464 1.0660 0.0794  -0.1248 0.0039  274  GLY   B N   
4731  C  CA  . GLY   B 274 ? 1.1489 1.1912 1.1130 0.0765  -0.1260 0.0047  274  GLY   B CA  
4732  C  C   . GLY   B 274 ? 1.1091 1.1653 1.0874 0.0683  -0.1230 0.0070  274  GLY   B C   
4733  O  O   . GLY   B 274 ? 1.0766 1.1390 1.0628 0.0626  -0.1232 0.0061  274  GLY   B O   
4734  N  N   . ASP   B 275 ? 1.1187 1.1791 1.0998 0.0680  -0.1204 0.0099  275  ASP   B N   
4735  C  CA  . ASP   B 275 ? 1.1198 1.1922 1.1132 0.0608  -0.1180 0.0121  275  ASP   B CA  
4736  C  C   . ASP   B 275 ? 1.1381 1.2093 1.1353 0.0563  -0.1225 0.0105  275  ASP   B C   
4737  O  O   . ASP   B 275 ? 1.1434 1.2054 1.1359 0.0574  -0.1278 0.0072  275  ASP   B O   
4738  C  CB  . ASP   B 275 ? 1.1516 1.2310 1.1470 0.0631  -0.1117 0.0167  275  ASP   B CB  
4739  C  CG  . ASP   B 275 ? 1.1797 1.2536 1.1685 0.0686  -0.1118 0.0179  275  ASP   B CG  
4740  O  OD1 . ASP   B 275 ? 1.1594 1.2234 1.1413 0.0706  -0.1168 0.0151  275  ASP   B OD1 
4741  O  OD2 . ASP   B 275 ? 1.1949 1.2746 1.1859 0.0708  -0.1069 0.0216  275  ASP   B OD2 
4742  N  N   . MET   B 276 ? 1.1402 1.2204 1.1461 0.0513  -0.1204 0.0127  276  MET   B N   
4743  C  CA  . MET   B 276 ? 1.1211 1.2003 1.1307 0.0467  -0.1238 0.0116  276  MET   B CA  
4744  C  C   . MET   B 276 ? 1.1015 1.1769 1.1063 0.0504  -0.1238 0.0132  276  MET   B C   
4745  O  O   . MET   B 276 ? 1.1432 1.2176 1.1505 0.0470  -0.1260 0.0128  276  MET   B O   
4746  C  CB  . MET   B 276 ? 1.1747 1.2643 1.1951 0.0392  -0.1220 0.0129  276  MET   B CB  
4747  C  CG  . MET   B 276 ? 1.1572 1.2523 1.1828 0.0358  -0.1208 0.0122  276  MET   B CG  
4748  S  SD  . MET   B 276 ? 1.1247 1.2313 1.1617 0.0276  -0.1186 0.0140  276  MET   B SD  
4749  C  CE  . MET   B 276 ? 1.0945 1.2074 1.1320 0.0306  -0.1143 0.0184  276  MET   B CE  
4750  N  N   . GLU   B 277 ? 1.1293 1.2021 1.1270 0.0576  -0.1212 0.0150  277  GLU   B N   
4751  C  CA  . GLU   B 277 ? 1.1575 1.2258 1.1496 0.0620  -0.1212 0.0164  277  GLU   B CA  
4752  C  C   . GLU   B 277 ? 1.1917 1.2476 1.1713 0.0697  -0.1233 0.0147  277  GLU   B C   
4753  O  O   . GLU   B 277 ? 1.2565 1.3087 1.2297 0.0756  -0.1219 0.0164  277  GLU   B O   
4754  C  CB  . GLU   B 277 ? 1.1975 1.2750 1.1934 0.0638  -0.1157 0.0207  277  GLU   B CB  
4755  C  CG  . GLU   B 277 ? 1.2139 1.3033 1.2216 0.0567  -0.1139 0.0224  277  GLU   B CG  
4756  C  CD  . GLU   B 277 ? 1.3566 1.4553 1.3690 0.0588  -0.1088 0.0264  277  GLU   B CD  
4757  O  OE1 . GLU   B 277 ? 1.4141 1.5100 1.4210 0.0656  -0.1064 0.0280  277  GLU   B OE1 
4758  O  OE2 . GLU   B 277 ? 1.4127 1.5213 1.4345 0.0536  -0.1074 0.0278  277  GLU   B OE2 
4759  N  N   . GLY   B 278 ? 1.1470 1.1961 1.1226 0.0702  -0.1269 0.0112  278  GLY   B N   
4760  C  CA  . GLY   B 278 ? 1.1129 1.1489 1.0760 0.0774  -0.1301 0.0090  278  GLY   B CA  
4761  C  C   . GLY   B 278 ? 1.1523 1.1856 1.1066 0.0855  -0.1257 0.0109  278  GLY   B C   
4762  O  O   . GLY   B 278 ? 1.1672 1.1885 1.1091 0.0925  -0.1279 0.0093  278  GLY   B O   
4763  N  N   . ARG   B 279 ? 1.1572 1.2006 1.1170 0.0849  -0.1194 0.0143  279  ARG   B N   
4764  C  CA  . ARG   B 279 ? 1.1541 1.1945 1.1059 0.0921  -0.1147 0.0161  279  ARG   B CA  
4765  C  C   . ARG   B 279 ? 1.1604 1.1937 1.1062 0.0935  -0.1176 0.0128  279  ARG   B C   
4766  O  O   . ARG   B 279 ? 1.1211 1.1583 1.0740 0.0872  -0.1203 0.0107  279  ARG   B O   
4767  C  CB  . ARG   B 279 ? 1.0745 1.1277 1.0353 0.0905  -0.1072 0.0205  279  ARG   B CB  
4768  C  CG  . ARG   B 279 ? 1.1521 1.2095 1.1151 0.0929  -0.1039 0.0239  279  ARG   B CG  
4769  C  CD  . ARG   B 279 ? 1.1043 1.1745 1.0773 0.0914  -0.0971 0.0281  279  ARG   B CD  
4770  N  NE  . ARG   B 279 ? 1.2431 1.3242 1.2290 0.0828  -0.0984 0.0284  279  ARG   B NE  
4771  C  CZ  . ARG   B 279 ? 1.2936 1.3802 1.2852 0.0810  -0.0986 0.0299  279  ARG   B CZ  
4772  N  NH1 . ARG   B 279 ? 1.3427 1.4254 1.3290 0.0868  -0.0977 0.0314  279  ARG   B NH1 
4773  N  NH2 . ARG   B 279 ? 1.3471 1.4428 1.3495 0.0734  -0.0997 0.0301  279  ARG   B NH2 
4774  N  N   . LEU   B 280 ? 1.1690 1.1907 1.1008 0.1022  -0.1173 0.0123  280  LEU   B N   
4775  C  CA  . LEU   B 280 ? 1.1480 1.1607 1.0710 0.1055  -0.1202 0.0092  280  LEU   B CA  
4776  C  C   . LEU   B 280 ? 1.1677 1.1807 1.0853 0.1111  -0.1127 0.0125  280  LEU   B C   
4777  O  O   . LEU   B 280 ? 1.1927 1.2013 1.1020 0.1184  -0.1081 0.0152  280  LEU   B O   
4778  C  CB  . LEU   B 280 ? 1.1537 1.1504 1.0630 0.1116  -0.1269 0.0054  280  LEU   B CB  
4779  C  CG  . LEU   B 280 ? 1.1745 1.1603 1.0732 0.1162  -0.1307 0.0019  280  LEU   B CG  
4780  C  CD1 . LEU   B 280 ? 1.0666 1.0596 0.9758 0.1087  -0.1331 -0.0003 280  LEU   B CD1 
4781  C  CD2 . LEU   B 280 ? 1.1044 1.0751 0.9917 0.1209  -0.1388 -0.0025 280  LEU   B CD2 
4782  N  N   . PHE   B 281 ? 1.1666 1.1847 1.0890 0.1078  -0.1110 0.0124  281  PHE   B N   
4783  C  CA  . PHE   B 281 ? 1.1797 1.1989 1.0984 0.1121  -0.1034 0.0157  281  PHE   B CA  
4784  C  C   . PHE   B 281 ? 1.2534 1.2608 1.1596 0.1172  -0.1060 0.0128  281  PHE   B C   
4785  O  O   . PHE   B 281 ? 1.2321 1.2349 1.1375 0.1147  -0.1136 0.0082  281  PHE   B O   
4786  C  CB  . PHE   B 281 ? 1.1026 1.1371 1.0365 0.1046  -0.0985 0.0185  281  PHE   B CB  
4787  C  CG  . PHE   B 281 ? 1.1524 1.1985 1.0979 0.1008  -0.0949 0.0219  281  PHE   B CG  
4788  C  CD1 . PHE   B 281 ? 1.1974 1.2471 1.1431 0.1052  -0.0870 0.0265  281  PHE   B CD1 
4789  C  CD2 . PHE   B 281 ? 1.0756 1.1291 1.0320 0.0930  -0.0992 0.0206  281  PHE   B CD2 
4790  C  CE1 . PHE   B 281 ? 1.1915 1.2523 1.1485 0.1019  -0.0842 0.0294  281  PHE   B CE1 
4791  C  CE2 . PHE   B 281 ? 1.1247 1.1883 1.0908 0.0900  -0.0962 0.0237  281  PHE   B CE2 
4792  C  CZ  . PHE   B 281 ? 1.1530 1.2205 1.1196 0.0944  -0.0890 0.0280  281  PHE   B CZ  
4793  N  N   . MET   B 282 ? 1.3363 1.3384 1.2326 0.1246  -0.0993 0.0157  282  MET   B N   
4794  C  CA  . MET   B 282 ? 1.3133 1.3052 1.1976 0.1298  -0.0996 0.0140  282  MET   B CA  
4795  C  C   . MET   B 282 ? 1.3040 1.3040 1.1939 0.1283  -0.0909 0.0180  282  MET   B C   
4796  O  O   . MET   B 282 ? 1.3430 1.3482 1.2356 0.1304  -0.0824 0.0228  282  MET   B O   
4797  C  CB  . MET   B 282 ? 1.3180 1.2931 1.1823 0.1413  -0.0993 0.0137  282  MET   B CB  
4798  C  CG  . MET   B 282 ? 1.3033 1.2684 1.1549 0.1472  -0.0977 0.0131  282  MET   B CG  
4799  S  SD  . MET   B 282 ? 1.4094 1.3585 1.2478 0.1508  -0.1101 0.0060  282  MET   B SD  
4800  C  CE  . MET   B 282 ? 1.5864 1.5184 1.4038 0.1633  -0.1091 0.0066  282  MET   B CE  
4801  N  N   . LEU   B 283 ? 1.2578 1.2590 1.1501 0.1247  -0.0931 0.0160  283  LEU   B N   
4802  C  CA  . LEU   B 283 ? 1.2475 1.2543 1.1435 0.1235  -0.0856 0.0191  283  LEU   B CA  
4803  C  C   . LEU   B 283 ? 1.3062 1.2980 1.1844 0.1320  -0.0852 0.0180  283  LEU   B C   
4804  O  O   . LEU   B 283 ? 1.3321 1.3152 1.2031 0.1331  -0.0933 0.0131  283  LEU   B O   
4805  C  CB  . LEU   B 283 ? 1.1622 1.1813 1.0738 0.1132  -0.0882 0.0178  283  LEU   B CB  
4806  C  CG  . LEU   B 283 ? 1.1494 1.1717 1.0636 0.1109  -0.0847 0.0186  283  LEU   B CG  
4807  C  CD1 . LEU   B 283 ? 1.2228 1.2535 1.1435 0.1104  -0.0740 0.0243  283  LEU   B CD1 
4808  C  CD2 . LEU   B 283 ? 1.1220 1.1534 1.0491 0.1013  -0.0903 0.0156  283  LEU   B CD2 
4809  N  N   . LEU   B 284 ? 1.3223 1.3106 1.1932 0.1383  -0.0758 0.0224  284  LEU   B N   
4810  C  CA  . LEU   B 284 ? 1.3515 1.3240 1.2033 0.1477  -0.0741 0.0219  284  LEU   B CA  
4811  C  C   . LEU   B 284 ? 1.3503 1.3269 1.2055 0.1456  -0.0675 0.0244  284  LEU   B C   
4812  O  O   . LEU   B 284 ? 1.4046 1.3915 1.2700 0.1430  -0.0584 0.0294  284  LEU   B O   
4813  C  CB  . LEU   B 284 ? 1.3385 1.3008 1.1763 0.1579  -0.0680 0.0251  284  LEU   B CB  
4814  C  CG  . LEU   B 284 ? 1.3592 1.3148 1.1907 0.1613  -0.0744 0.0225  284  LEU   B CG  
4815  C  CD1 . LEU   B 284 ? 1.3941 1.3649 1.2430 0.1546  -0.0723 0.0250  284  LEU   B CD1 
4816  C  CD2 . LEU   B 284 ? 1.5235 1.4633 1.3350 0.1734  -0.0702 0.0242  284  LEU   B CD2 
4817  N  N   . LEU   B 285 ? 1.3333 1.3021 1.1806 0.1468  -0.0724 0.0209  285  LEU   B N   
4818  C  CA  . LEU   B 285 ? 1.4081 1.3786 1.2563 0.1457  -0.0665 0.0230  285  LEU   B CA  
4819  C  C   . LEU   B 285 ? 1.5545 1.5107 1.3841 0.1567  -0.0586 0.0262  285  LEU   B C   
4820  O  O   . LEU   B 285 ? 1.5952 1.5348 1.4058 0.1649  -0.0629 0.0232  285  LEU   B O   
4821  C  CB  . LEU   B 285 ? 1.4264 1.3948 1.2744 0.1424  -0.0750 0.0180  285  LEU   B CB  
4822  C  CG  . LEU   B 285 ? 1.3867 1.3700 1.2541 0.1309  -0.0812 0.0154  285  LEU   B CG  
4823  C  CD1 . LEU   B 285 ? 1.2837 1.2687 1.1540 0.1270  -0.0835 0.0133  285  LEU   B CD1 
4824  C  CD2 . LEU   B 285 ? 1.3014 1.3010 1.1864 0.1237  -0.0749 0.0197  285  LEU   B CD2 
4825  N  N   . GLU   B 286 ? 1.7080 1.6704 1.5430 0.1571  -0.0470 0.0322  286  GLU   B N   
4826  C  CA  . GLU   B 286 ? 1.7499 1.6995 1.5686 0.1673  -0.0377 0.0360  286  GLU   B CA  
4827  C  C   . GLU   B 286 ? 1.7685 1.7111 1.5791 0.1689  -0.0357 0.0358  286  GLU   B C   
4828  O  O   . GLU   B 286 ? 1.7562 1.7099 1.5803 0.1617  -0.0317 0.0377  286  GLU   B O   
4829  C  CB  . GLU   B 286 ? 1.7718 1.7315 1.6014 0.1664  -0.0257 0.0425  286  GLU   B CB  
4830  C  CG  . GLU   B 286 ? 1.8391 1.7954 1.6638 0.1724  -0.0237 0.0441  286  GLU   B CG  
4831  C  CD  . GLU   B 286 ? 1.8664 1.8410 1.7126 0.1656  -0.0194 0.0476  286  GLU   B CD  
4832  O  OE1 . GLU   B 286 ? 1.7951 1.7722 1.6440 0.1650  -0.0248 0.0459  286  GLU   B OE1 
4833  O  OE2 . GLU   B 286 ? 1.8788 1.8649 1.7390 0.1610  -0.0109 0.0519  286  GLU   B OE2 
4834  N  N   . LYS   B 287 ? 1.7763 1.6998 1.5644 0.1785  -0.0389 0.0332  287  LYS   B N   
4835  C  CA  . LYS   B 287 ? 1.8272 1.7418 1.6052 0.1809  -0.0394 0.0319  287  LYS   B CA  
4836  C  C   . LYS   B 287 ? 1.9269 1.8308 1.6912 0.1893  -0.0269 0.0372  287  LYS   B C   
4837  O  O   . LYS   B 287 ? 1.9736 1.8718 1.7301 0.1961  -0.0197 0.0408  287  LYS   B O   
4838  C  CB  . LYS   B 287 ? 1.7917 1.6914 1.5533 0.1863  -0.0520 0.0251  287  LYS   B CB  
4839  N  N   . GLU   B 288 ? 2.0114 1.9124 1.7727 0.1888  -0.0240 0.0378  288  GLU   B N   
4840  C  CA  . GLU   B 288 ? 2.0515 1.9428 1.8011 0.1957  -0.0115 0.0430  288  GLU   B CA  
4841  C  C   . GLU   B 288 ? 2.0882 1.9606 1.8154 0.2034  -0.0161 0.0397  288  GLU   B C   
4842  O  O   . GLU   B 288 ? 2.0883 1.9640 1.8202 0.1984  -0.0205 0.0372  288  GLU   B O   
4843  C  CB  . GLU   B 288 ? 2.0676 1.9748 1.8370 0.1867  -0.0023 0.0477  288  GLU   B CB  
4844  C  CG  . GLU   B 288 ? 2.1358 2.0347 1.8963 0.1927  0.0119  0.0537  288  GLU   B CG  
4845  C  CD  . GLU   B 288 ? 2.1796 2.0824 1.9451 0.1953  0.0238  0.0598  288  GLU   B CD  
4846  O  OE1 . GLU   B 288 ? 2.1656 2.0841 1.9517 0.1878  0.0316  0.0641  288  GLU   B OE1 
4847  O  OE2 . GLU   B 288 ? 2.2027 2.0929 1.9520 0.2050  0.0249  0.0602  288  GLU   B OE2 
4848  N  N   . GLU   B 289 ? 2.0732 1.9255 1.7757 0.2160  -0.0152 0.0396  289  GLU   B N   
4849  C  CA  . GLU   B 289 ? 2.0546 1.8861 1.7325 0.2252  -0.0202 0.0361  289  GLU   B CA  
4850  C  C   . GLU   B 289 ? 2.0651 1.8880 1.7329 0.2299  -0.0077 0.0413  289  GLU   B C   
4851  O  O   . GLU   B 289 ? 2.0760 1.8856 1.7274 0.2396  0.0022  0.0456  289  GLU   B O   
4852  C  CB  . GLU   B 289 ? 2.0248 1.8377 1.6799 0.2369  -0.0254 0.0335  289  GLU   B CB  
4853  N  N   . GLN   B 290 ? 1.9748 1.8044 1.6515 0.2233  -0.0082 0.0408  290  GLN   B N   
4854  C  CA  . GLN   B 290 ? 2.0223 1.8461 1.6928 0.2259  0.0037  0.0457  290  GLN   B CA  
4855  C  C   . GLN   B 290 ? 2.0404 1.8396 1.6814 0.2378  0.0008  0.0433  290  GLN   B C   
4856  O  O   . GLN   B 290 ? 2.0607 1.8511 1.6907 0.2412  -0.0127 0.0367  290  GLN   B O   
4857  C  CB  . GLN   B 290 ? 2.0485 1.8892 1.7406 0.2138  0.0041  0.0461  290  GLN   B CB  
4858  C  CG  . GLN   B 290 ? 2.0407 1.9055 1.7620 0.2017  0.0069  0.0484  290  GLN   B CG  
4859  C  CD  . GLN   B 290 ? 2.0478 1.9156 1.7732 0.2040  0.0204  0.0552  290  GLN   B CD  
4860  O  OE1 . GLN   B 290 ? 2.0643 1.9219 1.7765 0.2125  0.0219  0.0560  290  GLN   B OE1 
4861  N  NE2 . GLN   B 290 ? 2.0605 1.9421 1.8045 0.1965  0.0303  0.0602  290  GLN   B NE2 
4862  N  N   . MET   B 291 ? 2.0135 1.8015 1.6418 0.2440  0.0136  0.0487  291  MET   B N   
4863  C  CA  . MET   B 291 ? 1.9503 1.7125 1.5474 0.2572  0.0128  0.0474  291  MET   B CA  
4864  C  C   . MET   B 291 ? 1.9843 1.7428 1.5773 0.2555  0.0023  0.0420  291  MET   B C   
4865  O  O   . MET   B 291 ? 1.9256 1.6651 1.4954 0.2651  -0.0064 0.0373  291  MET   B O   
4866  C  CB  . MET   B 291 ? 1.9080 1.6591 1.4928 0.2642  0.0303  0.0551  291  MET   B CB  
4867  C  CG  . MET   B 291 ? 1.9325 1.6705 1.5007 0.2751  0.0377  0.0585  291  MET   B CG  
4868  S  SD  . MET   B 291 ? 2.0323 1.7553 1.5803 0.2841  0.0212  0.0507  291  MET   B SD  
4869  C  CE  . MET   B 291 ? 1.8388 1.5467 1.3690 0.2881  0.0088  0.0441  291  MET   B CE  
4870  N  N   . ASP   B 292 ? 2.0085 1.7847 1.6238 0.2436  0.0025  0.0422  292  ASP   B N   
4871  C  CA  . ASP   B 292 ? 1.9545 1.7299 1.5694 0.2407  -0.0062 0.0377  292  ASP   B CA  
4872  C  C   . ASP   B 292 ? 1.9741 1.7470 1.5857 0.2416  -0.0241 0.0292  292  ASP   B C   
4873  O  O   . ASP   B 292 ? 1.9066 1.6750 1.5135 0.2418  -0.0333 0.0243  292  ASP   B O   
4874  C  CB  . ASP   B 292 ? 1.9326 1.7308 1.5760 0.2265  -0.0031 0.0395  292  ASP   B CB  
4875  C  CG  . ASP   B 292 ? 2.0283 1.8484 1.6976 0.2159  -0.0066 0.0389  292  ASP   B CG  
4876  O  OD1 . ASP   B 292 ? 2.0593 1.8794 1.7278 0.2168  -0.0178 0.0338  292  ASP   B OD1 
4877  O  OD2 . ASP   B 292 ? 2.0888 1.9257 1.7792 0.2068  0.0017  0.0433  292  ASP   B OD2 
4878  N  N   . GLY   B 293 ? 2.0523 1.8286 1.6674 0.2418  -0.0288 0.0275  293  GLY   B N   
4879  C  CA  . GLY   B 293 ? 2.0326 1.8096 1.6491 0.2410  -0.0450 0.0200  293  GLY   B CA  
4880  C  C   . GLY   B 293 ? 2.0474 1.8488 1.6937 0.2273  -0.0503 0.0182  293  GLY   B C   
4881  O  O   . GLY   B 293 ? 2.0355 1.8388 1.6851 0.2263  -0.0618 0.0130  293  GLY   B O   
4882  N  N   . THR   B 294 ? 2.0777 1.8970 1.7453 0.2169  -0.0423 0.0224  294  THR   B N   
4883  C  CA  . THR   B 294 ? 2.0421 1.8844 1.7377 0.2038  -0.0465 0.0212  294  THR   B CA  
4884  C  C   . THR   B 294 ? 2.0490 1.8997 1.7537 0.2020  -0.0414 0.0245  294  THR   B C   
4885  O  O   . THR   B 294 ? 2.0725 1.9130 1.7640 0.2101  -0.0330 0.0285  294  THR   B O   
4886  C  CB  . THR   B 294 ? 1.9901 1.8476 1.7042 0.1937  -0.0403 0.0241  294  THR   B CB  
4887  O  OG1 . THR   B 294 ? 1.9966 1.8608 1.7183 0.1917  -0.0260 0.0314  294  THR   B OG1 
4888  C  CG2 . THR   B 294 ? 2.0039 1.8501 1.7051 0.1976  -0.0406 0.0230  294  THR   B CG2 
4889  N  N   . VAL   B 295 ? 1.9616 1.8309 1.6890 0.1915  -0.0465 0.0229  295  VAL   B N   
4890  C  CA  . VAL   B 295 ? 1.9334 1.8127 1.6719 0.1885  -0.0429 0.0256  295  VAL   B CA  
4891  C  C   . VAL   B 295 ? 1.8736 1.7758 1.6397 0.1753  -0.0401 0.0276  295  VAL   B C   
4892  O  O   . VAL   B 295 ? 1.8658 1.7768 1.6433 0.1677  -0.0465 0.0244  295  VAL   B O   
4893  C  CB  . VAL   B 295 ? 1.9057 1.7808 1.6398 0.1911  -0.0546 0.0203  295  VAL   B CB  
4894  C  CG1 . VAL   B 295 ? 1.9569 1.8363 1.6951 0.1919  -0.0493 0.0237  295  VAL   B CG1 
4895  C  CG2 . VAL   B 295 ? 1.8365 1.6887 1.5440 0.2032  -0.0612 0.0163  295  VAL   B CG2 
4896  N  N   . THR   B 296 ? 1.8270 1.7386 1.6035 0.1728  -0.0305 0.0330  296  THR   B N   
4897  C  CA  . THR   B 296 ? 1.8075 1.7405 1.6098 0.1609  -0.0277 0.0352  296  THR   B CA  
4898  C  C   . THR   B 296 ? 1.7375 1.6792 1.5496 0.1585  -0.0299 0.0353  296  THR   B C   
4899  O  O   . THR   B 296 ? 1.7862 1.7174 1.5851 0.1665  -0.0300 0.0353  296  THR   B O   
4900  C  CB  . THR   B 296 ? 1.8301 1.7676 1.6384 0.1594  -0.0139 0.0418  296  THR   B CB  
4901  O  OG1 . THR   B 296 ? 1.8801 1.8031 1.6709 0.1702  -0.0049 0.0457  296  THR   B OG1 
4902  C  CG2 . THR   B 296 ? 1.7146 1.6512 1.5229 0.1564  -0.0133 0.0413  296  THR   B CG2 
4903  N  N   . LEU   B 297 ? 1.6540 1.6143 1.4884 0.1476  -0.0317 0.0352  297  LEU   B N   
4904  C  CA  . LEU   B 297 ? 1.5947 1.5644 1.4399 0.1444  -0.0339 0.0353  297  LEU   B CA  
4905  C  C   . LEU   B 297 ? 1.5618 1.5393 1.4159 0.1439  -0.0219 0.0418  297  LEU   B C   
4906  O  O   . LEU   B 297 ? 1.5216 1.5129 1.3928 0.1361  -0.0170 0.0446  297  LEU   B O   
4907  C  CB  . LEU   B 297 ? 1.5237 1.5085 1.3875 0.1334  -0.0422 0.0319  297  LEU   B CB  
4908  C  CG  . LEU   B 297 ? 1.5364 1.5344 1.4154 0.1282  -0.0419 0.0335  297  LEU   B CG  
4909  C  CD1 . LEU   B 297 ? 1.5504 1.5389 1.4179 0.1348  -0.0469 0.0313  297  LEU   B CD1 
4910  C  CD2 . LEU   B 297 ? 1.4031 1.4169 1.3016 0.1167  -0.0478 0.0312  297  LEU   B CD2 
4911  N  N   . LYS   B 298 ? 1.5779 1.5464 1.4205 0.1525  -0.0172 0.0441  298  LYS   B N   
4912  C  CA  . LYS   B 298 ? 1.6041 1.5788 1.4544 0.1532  -0.0052 0.0504  298  LYS   B CA  
4913  C  C   . LYS   B 298 ? 1.6430 1.6365 1.5157 0.1443  -0.0064 0.0513  298  LYS   B C   
4914  O  O   . LYS   B 298 ? 1.6013 1.6084 1.4914 0.1374  -0.0005 0.0546  298  LYS   B O   
4915  C  CB  . LYS   B 298 ? 1.7503 1.7095 1.5814 0.1653  -0.0002 0.0525  298  LYS   B CB  
4916  C  CG  . LYS   B 298 ? 1.7849 1.7519 1.6253 0.1662  0.0081  0.0573  298  LYS   B CG  
4917  C  CD  . LYS   B 298 ? 1.8522 1.8153 1.6895 0.1714  0.0228  0.0637  298  LYS   B CD  
4918  C  CE  . LYS   B 298 ? 1.7944 1.7666 1.6430 0.1719  0.0305  0.0683  298  LYS   B CE  
4919  N  NZ  . LYS   B 298 ? 1.8361 1.8100 1.6897 0.1737  0.0453  0.0748  298  LYS   B NZ  
4920  N  N   . ASP   B 299 ? 1.6542 1.6485 1.5268 0.1444  -0.0143 0.0482  299  ASP   B N   
4921  C  CA  . ASP   B 299 ? 1.6086 1.6186 1.4997 0.1375  -0.0155 0.0490  299  ASP   B CA  
4922  C  C   . ASP   B 299 ? 1.5790 1.5896 1.4704 0.1345  -0.0279 0.0436  299  ASP   B C   
4923  O  O   . ASP   B 299 ? 1.5840 1.5813 1.4598 0.1398  -0.0347 0.0396  299  ASP   B O   
4924  C  CB  . ASP   B 299 ? 1.6803 1.6898 1.5705 0.1433  -0.0072 0.0535  299  ASP   B CB  
4925  C  CG  . ASP   B 299 ? 1.7296 1.7543 1.6392 0.1380  0.0021  0.0587  299  ASP   B CG  
4926  O  OD1 . ASP   B 299 ? 1.6865 1.7257 1.6140 0.1281  -0.0007 0.0580  299  ASP   B OD1 
4927  O  OD2 . ASP   B 299 ? 1.7958 1.8178 1.7029 0.1440  0.0123  0.0634  299  ASP   B OD2 
4928  N  N   . LEU   B 300 ? 1.5152 1.5409 1.4246 0.1262  -0.0306 0.0434  300  LEU   B N   
4929  C  CA  . LEU   B 300 ? 1.4402 1.4677 1.3518 0.1233  -0.0406 0.0393  300  LEU   B CA  
4930  C  C   . LEU   B 300 ? 1.4453 1.4770 1.3612 0.1252  -0.0380 0.0418  300  LEU   B C   
4931  O  O   . LEU   B 300 ? 1.3967 1.4410 1.3273 0.1211  -0.0320 0.0456  300  LEU   B O   
4932  C  CB  . LEU   B 300 ? 1.3661 1.4069 1.2944 0.1122  -0.0462 0.0371  300  LEU   B CB  
4933  C  CG  . LEU   B 300 ? 1.3310 1.3705 1.2585 0.1089  -0.0490 0.0346  300  LEU   B CG  
4934  C  CD1 . LEU   B 300 ? 1.2587 1.3141 1.2055 0.0981  -0.0501 0.0347  300  LEU   B CD1 
4935  C  CD2 . LEU   B 300 ? 1.2650 1.2941 1.1815 0.1114  -0.0591 0.0290  300  LEU   B CD2 
4936  N  N   . ARG   B 301 ? 1.4598 1.4813 1.3635 0.1311  -0.0430 0.0394  301  ARG   B N   
4937  C  CA  . ARG   B 301 ? 1.4681 1.4926 1.3747 0.1330  -0.0419 0.0411  301  ARG   B CA  
4938  C  C   . ARG   B 301 ? 1.3851 1.4105 1.2941 0.1292  -0.0525 0.0367  301  ARG   B C   
4939  O  O   . ARG   B 301 ? 1.3558 1.3745 1.2586 0.1283  -0.0608 0.0320  301  ARG   B O   
4940  C  CB  . ARG   B 301 ? 1.5275 1.5379 1.4166 0.1447  -0.0367 0.0431  301  ARG   B CB  
4941  C  CG  . ARG   B 301 ? 1.5956 1.6081 1.4865 0.1482  -0.0240 0.0490  301  ARG   B CG  
4942  C  CD  . ARG   B 301 ? 1.7077 1.7117 1.5877 0.1581  -0.0181 0.0519  301  ARG   B CD  
4943  N  NE  . ARG   B 301 ? 1.8159 1.8019 1.6744 0.1663  -0.0244 0.0482  301  ARG   B NE  
4944  C  CZ  . ARG   B 301 ? 1.8154 1.7967 1.6683 0.1694  -0.0297 0.0462  301  ARG   B CZ  
4945  N  NH1 . ARG   B 301 ? 1.7160 1.7089 1.5823 0.1656  -0.0293 0.0478  301  ARG   B NH1 
4946  N  NH2 . ARG   B 301 ? 1.7593 1.7233 1.5922 0.1768  -0.0359 0.0425  301  ARG   B NH2 
4947  N  N   . VAL   B 302 ? 1.4025 1.4365 1.3211 0.1269  -0.0521 0.0383  302  VAL   B N   
4948  C  CA  . VAL   B 302 ? 1.3545 1.3900 1.2763 0.1231  -0.0609 0.0348  302  VAL   B CA  
4949  C  C   . VAL   B 302 ? 1.4012 1.4320 1.3169 0.1294  -0.0597 0.0362  302  VAL   B C   
4950  O  O   . VAL   B 302 ? 1.4087 1.4458 1.3300 0.1313  -0.0521 0.0406  302  VAL   B O   
4951  C  CB  . VAL   B 302 ? 1.2940 1.3459 1.2354 0.1123  -0.0627 0.0350  302  VAL   B CB  
4952  C  CG1 . VAL   B 302 ? 1.3622 1.4155 1.3065 0.1099  -0.0694 0.0328  302  VAL   B CG1 
4953  C  CG2 . VAL   B 302 ? 1.2282 1.2828 1.1739 0.1060  -0.0663 0.0323  302  VAL   B CG2 
4954  N  N   . GLU   B 303 ? 1.5170 1.5370 1.4218 0.1327  -0.0673 0.0324  303  GLU   B N   
4955  C  CA  . GLU   B 303 ? 1.5505 1.5639 1.4472 0.1393  -0.0670 0.0332  303  GLU   B CA  
4956  C  C   . GLU   B 303 ? 1.4941 1.5091 1.3953 0.1347  -0.0758 0.0299  303  GLU   B C   
4957  O  O   . GLU   B 303 ? 1.4854 1.4973 1.3860 0.1307  -0.0839 0.0254  303  GLU   B O   
4958  C  CB  . GLU   B 303 ? 1.5918 1.5865 1.4667 0.1503  -0.0671 0.0320  303  GLU   B CB  
4959  C  CG  . GLU   B 303 ? 1.6798 1.6691 1.5460 0.1596  -0.0594 0.0360  303  GLU   B CG  
4960  C  CD  . GLU   B 303 ? 1.7782 1.7726 1.6480 0.1618  -0.0477 0.0413  303  GLU   B CD  
4961  O  OE1 . GLU   B 303 ? 1.8466 1.8435 1.7178 0.1663  -0.0401 0.0455  303  GLU   B OE1 
4962  O  OE2 . GLU   B 303 ? 1.7848 1.7807 1.6565 0.1591  -0.0459 0.0413  303  GLU   B OE2 
4963  N  N   . LEU   B 304 ? 1.3156 1.3355 1.2216 0.1352  -0.0740 0.0321  304  LEU   B N   
4964  C  CA  . LEU   B 304 ? 1.2599 1.2802 1.1690 0.1314  -0.0816 0.0293  304  LEU   B CA  
4965  C  C   . LEU   B 304 ? 1.2735 1.2771 1.1651 0.1395  -0.0862 0.0267  304  LEU   B C   
4966  O  O   . LEU   B 304 ? 1.3510 1.3480 1.2329 0.1480  -0.0814 0.0291  304  LEU   B O   
4967  C  CB  . LEU   B 304 ? 1.2369 1.2695 1.1587 0.1284  -0.0781 0.0327  304  LEU   B CB  
4968  C  CG  . LEU   B 304 ? 1.1353 1.1690 1.0610 0.1241  -0.0852 0.0304  304  LEU   B CG  
4969  C  CD1 . LEU   B 304 ? 1.2068 1.2365 1.1322 0.1185  -0.0938 0.0254  304  LEU   B CD1 
4970  C  CD2 . LEU   B 304 ? 1.0156 1.0649 0.9579 0.1177  -0.0826 0.0332  304  LEU   B CD2 
4971  N  N   . LEU   B 305 ? 1.2131 1.2098 1.1011 0.1370  -0.0954 0.0217  305  LEU   B N   
4972  C  CA  . LEU   B 305 ? 1.2833 1.2632 1.1547 0.1443  -0.1011 0.0184  305  LEU   B CA  
4973  C  C   . LEU   B 305 ? 1.3448 1.3233 1.2173 0.1434  -0.1057 0.0174  305  LEU   B C   
4974  O  O   . LEU   B 305 ? 1.4278 1.3946 1.2871 0.1513  -0.1064 0.0171  305  LEU   B O   
4975  C  CB  . LEU   B 305 ? 1.2682 1.2396 1.1340 0.1430  -0.1092 0.0131  305  LEU   B CB  
4976  C  CG  . LEU   B 305 ? 1.3466 1.3122 1.2041 0.1469  -0.1070 0.0127  305  LEU   B CG  
4977  C  CD1 . LEU   B 305 ? 1.3550 1.3345 1.2245 0.1424  -0.0988 0.0168  305  LEU   B CD1 
4978  C  CD2 . LEU   B 305 ? 1.3332 1.2920 1.1882 0.1444  -0.1167 0.0068  305  LEU   B CD2 
4979  N  N   . GLY   B 306 ? 1.2424 1.2316 1.1294 0.1342  -0.1086 0.0168  306  GLY   B N   
4980  C  CA  . GLY   B 306 ? 1.2520 1.2387 1.1393 0.1333  -0.1131 0.0157  306  GLY   B CA  
4981  C  C   . GLY   B 306 ? 1.2784 1.2755 1.1810 0.1225  -0.1170 0.0144  306  GLY   B C   
4982  O  O   . GLY   B 306 ? 1.2319 1.2407 1.1464 0.1160  -0.1146 0.0155  306  GLY   B O   
4983  N  N   . GLU   B 307 ? 1.2650 1.2571 1.1668 0.1209  -0.1229 0.0121  307  GLU   B N   
4984  C  CA  . GLU   B 307 ? 1.2334 1.2337 1.1484 0.1113  -0.1263 0.0110  307  GLU   B CA  
4985  C  C   . GLU   B 307 ? 1.2517 1.2412 1.1627 0.1098  -0.1351 0.0061  307  GLU   B C   
4986  O  O   . GLU   B 307 ? 1.2459 1.2231 1.1453 0.1159  -0.1384 0.0045  307  GLU   B O   
4987  C  CB  . GLU   B 307 ? 1.2506 1.2592 1.1726 0.1094  -0.1230 0.0145  307  GLU   B CB  
4988  C  CG  . GLU   B 307 ? 1.2843 1.2926 1.2120 0.1030  -0.1285 0.0125  307  GLU   B CG  
4989  C  CD  . GLU   B 307 ? 1.3084 1.3264 1.2445 0.0999  -0.1253 0.0159  307  GLU   B CD  
4990  O  OE1 . GLU   B 307 ? 1.3143 1.3272 1.2478 0.1003  -0.1282 0.0154  307  GLU   B OE1 
4991  O  OE2 . GLU   B 307 ? 1.2907 1.3212 1.2360 0.0971  -0.1202 0.0189  307  GLU   B OE2 
4992  N  N   . THR   B 308 ? 1.2352 1.2298 1.1566 0.1015  -0.1389 0.0036  308  THR   B N   
4993  C  CA  . THR   B 308 ? 1.2177 1.2037 1.1386 0.0987  -0.1471 -0.0013 308  THR   B CA  
4994  C  C   . THR   B 308 ? 1.1651 1.1598 1.1003 0.0889  -0.1485 -0.0015 308  THR   B C   
4995  O  O   . THR   B 308 ? 1.1511 1.1572 1.0946 0.0850  -0.1433 0.0022  308  THR   B O   
4996  C  CB  . THR   B 308 ? 1.1815 1.1628 1.0994 0.0996  -0.1508 -0.0049 308  THR   B CB  
4997  O  OG1 . THR   B 308 ? 1.1068 1.0998 1.0382 0.0914  -0.1496 -0.0048 308  THR   B OG1 
4998  C  CG2 . THR   B 308 ? 1.1608 1.1373 1.0663 0.1086  -0.1467 -0.0033 308  THR   B CG2 
4999  N  N   . SER   B 309 ? 1.1190 1.1081 1.0571 0.0848  -0.1552 -0.0057 309  SER   B N   
5000  C  CA  . SER   B 309 ? 1.1052 1.1022 1.0570 0.0753  -0.1559 -0.0059 309  SER   B CA  
5001  C  C   . SER   B 309 ? 1.0344 1.0441 0.9961 0.0702  -0.1518 -0.0043 309  SER   B C   
5002  O  O   . SER   B 309 ? 1.1029 1.1129 1.0620 0.0727  -0.1512 -0.0050 309  SER   B O   
5003  C  CB  . SER   B 309 ? 1.0733 1.0626 1.0281 0.0718  -0.1635 -0.0109 309  SER   B CB  
5004  O  OG  . SER   B 309 ? 1.1130 1.0912 1.0607 0.0750  -0.1675 -0.0123 309  SER   B OG  
5005  N  N   . ILE   B 310 ? 0.9909 1.0105 0.9633 0.0633  -0.1490 -0.0021 310  ILE   B N   
5006  C  CA  . ILE   B 310 ? 1.0522 1.0835 1.0341 0.0581  -0.1454 -0.0007 310  ILE   B CA  
5007  C  C   . ILE   B 310 ? 1.0158 1.0448 1.0006 0.0558  -0.1496 -0.0048 310  ILE   B C   
5008  O  O   . ILE   B 310 ? 1.0264 1.0519 1.0161 0.0516  -0.1544 -0.0080 310  ILE   B O   
5009  C  CB  . ILE   B 310 ? 1.0456 1.0858 1.0378 0.0508  -0.1429 0.0015  310  ILE   B CB  
5010  C  CG1 . ILE   B 310 ? 1.0287 1.0708 1.0177 0.0537  -0.1393 0.0053  310  ILE   B CG1 
5011  C  CG2 . ILE   B 310 ? 0.9154 0.9672 0.9167 0.0458  -0.1393 0.0029  310  ILE   B CG2 
5012  C  CD1 . ILE   B 310 ? 0.9194 0.9684 0.9168 0.0472  -0.1376 0.0073  310  ILE   B CD1 
5013  N  N   . ALA   B 311 ? 1.0217 1.0523 1.0034 0.0589  -0.1480 -0.0048 311  ALA   B N   
5014  C  CA  . ALA   B 311 ? 1.0058 1.0317 0.9868 0.0592  -0.1527 -0.0090 311  ALA   B CA  
5015  C  C   . ALA   B 311 ? 1.0222 1.0574 1.0158 0.0514  -0.1522 -0.0097 311  ALA   B C   
5016  O  O   . ALA   B 311 ? 1.0736 1.1189 1.0725 0.0485  -0.1468 -0.0066 311  ALA   B O   
5017  C  CB  . ALA   B 311 ? 1.0072 1.0290 0.9775 0.0668  -0.1509 -0.0086 311  ALA   B CB  
5018  N  N   . GLU   B 312 ? 1.0016 1.0332 1.0003 0.0480  -0.1580 -0.0139 312  GLU   B N   
5019  C  CA  . GLU   B 312 ? 1.0028 1.0421 1.0126 0.0416  -0.1579 -0.0151 312  GLU   B CA  
5020  C  C   . GLU   B 312 ? 1.0973 1.1336 1.1028 0.0452  -0.1602 -0.0177 312  GLU   B C   
5021  O  O   . GLU   B 312 ? 1.1201 1.1641 1.1310 0.0423  -0.1575 -0.0170 312  GLU   B O   
5022  C  CB  . GLU   B 312 ? 0.9938 1.0320 1.0135 0.0353  -0.1622 -0.0180 312  GLU   B CB  
5023  C  CG  . GLU   B 312 ? 1.0746 1.1194 1.1061 0.0290  -0.1628 -0.0199 312  GLU   B CG  
5024  C  CD  . GLU   B 312 ? 1.1760 1.2328 1.2155 0.0232  -0.1563 -0.0162 312  GLU   B CD  
5025  O  OE1 . GLU   B 312 ? 1.1248 1.1855 1.1603 0.0246  -0.1513 -0.0121 312  GLU   B OE1 
5026  O  OE2 . GLU   B 312 ? 1.2037 1.2658 1.2536 0.0173  -0.1564 -0.0175 312  GLU   B OE2 
5027  N  N   . CYS   B 313 ? 1.0462 1.0708 1.0412 0.0520  -0.1653 -0.0207 313  CYS   B N   
5028  C  CA  . CYS   B 313 ? 1.0135 1.0330 1.0017 0.0569  -0.1681 -0.0233 313  CYS   B CA  
5029  C  C   . CYS   B 313 ? 1.1109 1.1177 1.0827 0.0665  -0.1702 -0.0239 313  CYS   B C   
5030  O  O   . CYS   B 313 ? 1.1163 1.1168 1.0839 0.0685  -0.1721 -0.0241 313  CYS   B O   
5031  C  CB  . CYS   B 313 ? 1.0351 1.0527 1.0312 0.0534  -0.1751 -0.0285 313  CYS   B CB  
5032  S  SG  . CYS   B 313 ? 1.2019 1.2063 1.1954 0.0556  -0.1848 -0.0338 313  CYS   B SG  
5033  N  N   . LEU   B 314 ? 1.1649 1.1676 1.1269 0.0727  -0.1693 -0.0241 314  LEU   B N   
5034  C  CA  . LEU   B 314 ? 1.1291 1.1195 1.0738 0.0826  -0.1700 -0.0241 314  LEU   B CA  
5035  C  C   . LEU   B 314 ? 1.1890 1.1703 1.1259 0.0875  -0.1758 -0.0285 314  LEU   B C   
5036  O  O   . LEU   B 314 ? 1.2299 1.2164 1.1712 0.0854  -0.1747 -0.0288 314  LEU   B O   
5037  C  CB  . LEU   B 314 ? 1.1342 1.1286 1.0726 0.0866  -0.1609 -0.0186 314  LEU   B CB  
5038  C  CG  . LEU   B 314 ? 1.1517 1.1488 1.0885 0.0877  -0.1553 -0.0142 314  LEU   B CG  
5039  C  CD1 . LEU   B 314 ? 1.1694 1.1735 1.1189 0.0798  -0.1565 -0.0141 314  LEU   B CD1 
5040  C  CD2 . LEU   B 314 ? 1.1179 1.1246 1.0566 0.0877  -0.1461 -0.0091 314  LEU   B CD2 
5041  N  N   . THR   B 315 ? 1.1602 1.1271 1.0846 0.0946  -0.1820 -0.0317 315  THR   B N   
5042  C  CA  . THR   B 315 ? 1.1850 1.1412 1.0978 0.1016  -0.1867 -0.0353 315  THR   B CA  
5043  C  C   . THR   B 315 ? 1.2241 1.1655 1.1173 0.1121  -0.1875 -0.0352 315  THR   B C   
5044  O  O   . THR   B 315 ? 1.2221 1.1579 1.1127 0.1132  -0.1903 -0.0359 315  THR   B O   
5045  C  CB  . THR   B 315 ? 1.1961 1.1487 1.1160 0.0987  -0.1971 -0.0417 315  THR   B CB  
5046  O  OG1 . THR   B 315 ? 1.2491 1.1895 1.1626 0.1022  -0.2049 -0.0455 315  THR   B OG1 
5047  C  CG2 . THR   B 315 ? 1.2081 1.1747 1.1490 0.0873  -0.1965 -0.0417 315  THR   B CG2 
5048  N  N   . TYR   B 316 ? 1.2646 1.1997 1.1439 0.1197  -0.1842 -0.0339 316  TYR   B N   
5049  C  CA  . TYR   B 316 ? 1.2565 1.1747 1.1153 0.1308  -0.1867 -0.0351 316  TYR   B CA  
5050  C  C   . TYR   B 316 ? 1.2181 1.1238 1.0721 0.1336  -0.1990 -0.0423 316  TYR   B C   
5051  O  O   . TYR   B 316 ? 1.2837 1.1933 1.1468 0.1293  -0.2038 -0.0457 316  TYR   B O   
5052  C  CB  . TYR   B 316 ? 1.2889 1.2038 1.1344 0.1381  -0.1791 -0.0315 316  TYR   B CB  
5053  C  CG  . TYR   B 316 ? 1.3778 1.2745 1.2003 0.1504  -0.1802 -0.0322 316  TYR   B CG  
5054  C  CD1 . TYR   B 316 ? 1.4083 1.2954 1.2231 0.1544  -0.1841 -0.0335 316  TYR   B CD1 
5055  C  CD2 . TYR   B 316 ? 1.4351 1.3234 1.2427 0.1583  -0.1772 -0.0314 316  TYR   B CD2 
5056  C  CE1 . TYR   B 316 ? 1.4505 1.3199 1.2429 0.1662  -0.1851 -0.0341 316  TYR   B CE1 
5057  C  CE2 . TYR   B 316 ? 1.4853 1.3558 1.2703 0.1701  -0.1779 -0.0318 316  TYR   B CE2 
5058  C  CZ  . TYR   B 316 ? 1.4688 1.3300 1.2463 0.1741  -0.1818 -0.0333 316  TYR   B CZ  
5059  O  OH  . TYR   B 316 ? 1.5100 1.3529 1.2643 0.1862  -0.1824 -0.0337 316  TYR   B OH  
5060  N  N   . LEU   B 317 ? 1.3068 1.1979 1.1473 0.1407  -0.2043 -0.0447 317  LEU   B N   
5061  C  CA  . LEU   B 317 ? 1.3878 1.2649 1.2215 0.1447  -0.2167 -0.0517 317  LEU   B CA  
5062  C  C   . LEU   B 317 ? 1.4162 1.2760 1.2256 0.1574  -0.2180 -0.0528 317  LEU   B C   
5063  O  O   . LEU   B 317 ? 1.4087 1.2640 1.2132 0.1605  -0.2216 -0.0555 317  LEU   B O   
5064  C  CB  . LEU   B 317 ? 1.3300 1.2023 1.1671 0.1428  -0.2233 -0.0545 317  LEU   B CB  
5065  C  CG  . LEU   B 317 ? 1.3045 1.1917 1.1626 0.1314  -0.2206 -0.0526 317  LEU   B CG  
5066  C  CD1 . LEU   B 317 ? 1.3397 1.2187 1.1973 0.1314  -0.2273 -0.0554 317  LEU   B CD1 
5067  C  CD2 . LEU   B 317 ? 1.2665 1.1650 1.1435 0.1223  -0.2237 -0.0551 317  LEU   B CD2 
5068  N  N   . ASP   B 318 ? 1.4482 1.2976 1.2416 0.1653  -0.2151 -0.0506 318  ASP   B N   
5069  C  CA  . ASP   B 318 ? 1.4637 1.2951 1.2323 0.1781  -0.2157 -0.0513 318  ASP   B CA  
5070  C  C   . ASP   B 318 ? 1.5100 1.3333 1.2659 0.1844  -0.2118 -0.0485 318  ASP   B C   
5071  O  O   . ASP   B 318 ? 1.5353 1.3643 1.3011 0.1792  -0.2120 -0.0478 318  ASP   B O   
5072  C  CB  . ASP   B 318 ? 1.4962 1.3127 1.2564 0.1828  -0.2294 -0.0591 318  ASP   B CB  
5073  C  CG  . ASP   B 318 ? 1.6117 1.4104 1.3463 0.1958  -0.2297 -0.0598 318  ASP   B CG  
5074  O  OD1 . ASP   B 318 ? 1.6700 1.4725 1.4000 0.1980  -0.2203 -0.0553 318  ASP   B OD1 
5075  O  OD2 . ASP   B 318 ? 1.6425 1.4230 1.3615 0.2038  -0.2395 -0.0650 318  ASP   B OD2 
5076  N  N   . ASN   B 319 ? 1.5191 1.3287 1.2527 0.1960  -0.2080 -0.0467 319  ASN   B N   
5077  C  CA  . ASN   B 319 ? 1.5372 1.3364 1.2560 0.2036  -0.2048 -0.0444 319  ASN   B CA  
5078  C  C   . ASN   B 319 ? 1.4858 1.3006 1.2186 0.1970  -0.1954 -0.0386 319  ASN   B C   
5079  O  O   . ASN   B 319 ? 1.5503 1.3609 1.2800 0.1986  -0.1962 -0.0382 319  ASN   B O   
5080  C  CB  . ASN   B 319 ? 1.5288 1.3123 1.2392 0.2074  -0.2176 -0.0509 319  ASN   B CB  
5081  C  CG  . ASN   B 319 ? 1.6150 1.3877 1.3202 0.2099  -0.2298 -0.0580 319  ASN   B CG  
5082  O  OD1 . ASN   B 319 ? 1.6588 1.4389 1.3812 0.2014  -0.2378 -0.0623 319  ASN   B OD1 
5083  N  ND2 . ASN   B 319 ? 1.6526 1.4078 1.3341 0.2219  -0.2312 -0.0593 319  ASN   B ND2 
5084  N  N   . GLY   B 320 ? 1.4900 1.3226 1.2384 0.1894  -0.1871 -0.0343 320  GLY   B N   
5085  C  CA  . GLY   B 320 ? 1.5441 1.3922 1.3061 0.1833  -0.1780 -0.0286 320  GLY   B CA  
5086  C  C   . GLY   B 320 ? 1.4314 1.2897 1.2119 0.1730  -0.1826 -0.0302 320  GLY   B C   
5087  O  O   . GLY   B 320 ? 1.3666 1.2348 1.1555 0.1693  -0.1763 -0.0260 320  GLY   B O   
5088  N  N   . VAL   B 321 ? 1.3927 1.2489 1.1802 0.1684  -0.1933 -0.0361 321  VAL   B N   
5089  C  CA  . VAL   B 321 ? 1.3453 1.2111 1.1512 0.1582  -0.1973 -0.0376 321  VAL   B CA  
5090  C  C   . VAL   B 321 ? 1.3238 1.2077 1.1498 0.1477  -0.1940 -0.0361 321  VAL   B C   
5091  O  O   . VAL   B 321 ? 1.3322 1.2167 1.1601 0.1467  -0.1969 -0.0386 321  VAL   B O   
5092  C  CB  . VAL   B 321 ? 1.3692 1.2232 1.1735 0.1584  -0.2104 -0.0447 321  VAL   B CB  
5093  C  CG1 . VAL   B 321 ? 1.2883 1.1544 1.1146 0.1464  -0.2137 -0.0461 321  VAL   B CG1 
5094  C  CG2 . VAL   B 321 ? 1.4416 1.2804 1.2297 0.1665  -0.2131 -0.0454 321  VAL   B CG2 
5095  N  N   . VAL   B 322 ? 1.2927 1.1906 1.1329 0.1401  -0.1881 -0.0322 322  VAL   B N   
5096  C  CA  . VAL   B 322 ? 1.2575 1.1726 1.1174 0.1295  -0.1852 -0.0308 322  VAL   B CA  
5097  C  C   . VAL   B 322 ? 1.2423 1.1617 1.1166 0.1210  -0.1908 -0.0333 322  VAL   B C   
5098  O  O   . VAL   B 322 ? 1.1837 1.1013 1.0574 0.1210  -0.1903 -0.0321 322  VAL   B O   
5099  C  CB  . VAL   B 322 ? 1.2534 1.1818 1.1187 0.1273  -0.1735 -0.0240 322  VAL   B CB  
5100  C  CG1 . VAL   B 322 ? 1.1640 1.1089 1.0487 0.1167  -0.1712 -0.0230 322  VAL   B CG1 
5101  C  CG2 . VAL   B 322 ? 1.2777 1.2014 1.1293 0.1357  -0.1672 -0.0212 322  VAL   B CG2 
5102  N  N   . PHE   B 323 ? 1.2318 1.1569 1.1193 0.1139  -0.1955 -0.0367 323  PHE   B N   
5103  C  CA  . PHE   B 323 ? 1.1568 1.0895 1.0612 0.1044  -0.1982 -0.0379 323  PHE   B CA  
5104  C  C   . PHE   B 323 ? 1.1462 1.0956 1.0635 0.0969  -0.1893 -0.0326 323  PHE   B C   
5105  O  O   . PHE   B 323 ? 1.1706 1.1284 1.0904 0.0960  -0.1836 -0.0300 323  PHE   B O   
5106  C  CB  . PHE   B 323 ? 1.1042 1.0367 1.0188 0.0996  -0.2065 -0.0435 323  PHE   B CB  
5107  C  CG  . PHE   B 323 ? 1.1397 1.0800 1.0721 0.0896  -0.2084 -0.0444 323  PHE   B CG  
5108  C  CD1 . PHE   B 323 ? 1.1961 1.1289 1.1283 0.0892  -0.2129 -0.0462 323  PHE   B CD1 
5109  C  CD2 . PHE   B 323 ? 1.1273 1.0814 1.0761 0.0810  -0.2052 -0.0433 323  PHE   B CD2 
5110  C  CE1 . PHE   B 323 ? 1.1101 1.0492 1.0584 0.0801  -0.2141 -0.0468 323  PHE   B CE1 
5111  C  CE2 . PHE   B 323 ? 1.1760 1.1363 1.1406 0.0721  -0.2063 -0.0439 323  PHE   B CE2 
5112  C  CZ  . PHE   B 323 ? 1.1487 1.1015 1.1131 0.0717  -0.2105 -0.0455 323  PHE   B CZ  
5113  N  N   . VAL   B 324 ? 1.1368 1.0904 1.0619 0.0919  -0.1881 -0.0310 324  VAL   B N   
5114  C  CA  . VAL   B 324 ? 1.0970 1.0655 1.0347 0.0846  -0.1808 -0.0266 324  VAL   B CA  
5115  C  C   . VAL   B 324 ? 1.1248 1.0977 1.0777 0.0755  -0.1848 -0.0290 324  VAL   B C   
5116  O  O   . VAL   B 324 ? 1.1544 1.1210 1.1077 0.0746  -0.1888 -0.0307 324  VAL   B O   
5117  C  CB  . VAL   B 324 ? 1.0956 1.0655 1.0282 0.0873  -0.1747 -0.0218 324  VAL   B CB  
5118  C  CG1 . VAL   B 324 ? 1.0830 1.0672 1.0296 0.0790  -0.1690 -0.0180 324  VAL   B CG1 
5119  C  CG2 . VAL   B 324 ? 1.0755 1.0434 0.9957 0.0953  -0.1692 -0.0188 324  VAL   B CG2 
5120  N  N   . GLY   B 325 ? 1.0457 1.0289 1.0110 0.0688  -0.1835 -0.0292 325  GLY   B N   
5121  C  CA  . GLY   B 325 ? 0.9997 0.9892 0.9806 0.0597  -0.1850 -0.0303 325  GLY   B CA  
5122  C  C   . GLY   B 325 ? 1.0238 1.0236 1.0110 0.0549  -0.1775 -0.0252 325  GLY   B C   
5123  O  O   . GLY   B 325 ? 1.0237 1.0317 1.0104 0.0552  -0.1710 -0.0213 325  GLY   B O   
5124  N  N   . SER   B 326 ? 1.0540 1.0527 1.0466 0.0507  -0.1785 -0.0251 326  SER   B N   
5125  C  CA  . SER   B 326 ? 1.0251 1.0320 1.0222 0.0467  -0.1720 -0.0204 326  SER   B CA  
5126  C  C   . SER   B 326 ? 1.0474 1.0585 1.0583 0.0379  -0.1727 -0.0212 326  SER   B C   
5127  O  O   . SER   B 326 ? 1.0464 1.0511 1.0616 0.0359  -0.1785 -0.0253 326  SER   B O   
5128  C  CB  . SER   B 326 ? 0.9886 0.9889 0.9754 0.0519  -0.1710 -0.0183 326  SER   B CB  
5129  O  OG  . SER   B 326 ? 1.0088 1.0178 0.9962 0.0512  -0.1639 -0.0132 326  SER   B OG  
5130  N  N   . ARG   B 327 ? 0.9880 1.0095 1.0058 0.0328  -0.1666 -0.0175 327  ARG   B N   
5131  C  CA  . ARG   B 327 ? 0.9836 1.0088 1.0129 0.0249  -0.1656 -0.0172 327  ARG   B CA  
5132  C  C   . ARG   B 327 ? 0.9892 1.0151 1.0165 0.0240  -0.1616 -0.0133 327  ARG   B C   
5133  O  O   . ARG   B 327 ? 0.9840 1.0079 1.0171 0.0192  -0.1619 -0.0135 327  ARG   B O   
5134  C  CB  . ARG   B 327 ? 1.0228 1.0589 1.0626 0.0191  -0.1623 -0.0165 327  ARG   B CB  
5135  C  CG  . ARG   B 327 ? 1.0481 1.0841 1.0912 0.0194  -0.1662 -0.0204 327  ARG   B CG  
5136  C  CD  . ARG   B 327 ? 1.0650 1.1108 1.1203 0.0126  -0.1635 -0.0202 327  ARG   B CD  
5137  N  NE  . ARG   B 327 ? 1.0903 1.1373 1.1552 0.0059  -0.1623 -0.0198 327  ARG   B NE  
5138  C  CZ  . ARG   B 327 ? 1.1884 1.2433 1.2636 -0.0005 -0.1587 -0.0188 327  ARG   B CZ  
5139  N  NH1 . ARG   B 327 ? 1.1977 1.2602 1.2754 -0.0014 -0.1565 -0.0184 327  ARG   B NH1 
5140  N  NH2 . ARG   B 327 ? 1.1331 1.1876 1.2157 -0.0060 -0.1572 -0.0182 327  ARG   B NH2 
5141  N  N   . LEU   B 328 ? 0.9691 0.9975 0.9884 0.0286  -0.1578 -0.0098 328  LEU   B N   
5142  C  CA  . LEU   B 328 ? 0.9348 0.9633 0.9517 0.0284  -0.1547 -0.0064 328  LEU   B CA  
5143  C  C   . LEU   B 328 ? 1.0036 1.0205 1.0113 0.0335  -0.1583 -0.0075 328  LEU   B C   
5144  O  O   . LEU   B 328 ? 1.0037 1.0179 1.0106 0.0323  -0.1573 -0.0058 328  LEU   B O   
5145  C  CB  . LEU   B 328 ? 0.8954 0.9324 0.9094 0.0308  -0.1492 -0.0022 328  LEU   B CB  
5146  C  CG  . LEU   B 328 ? 0.9725 1.0207 0.9949 0.0261  -0.1457 -0.0011 328  LEU   B CG  
5147  C  CD1 . LEU   B 328 ? 0.8602 0.9169 0.8813 0.0276  -0.1404 0.0033  328  LEU   B CD1 
5148  C  CD2 . LEU   B 328 ? 0.9165 0.9666 0.9489 0.0181  -0.1459 -0.0020 328  LEU   B CD2 
5149  N  N   . GLY   B 329 ? 0.9688 0.9780 0.9689 0.0394  -0.1624 -0.0103 329  GLY   B N   
5150  C  CA  . GLY   B 329 ? 0.9852 0.9825 0.9753 0.0449  -0.1660 -0.0115 329  GLY   B CA  
5151  C  C   . GLY   B 329 ? 1.0889 1.0762 1.0758 0.0476  -0.1731 -0.0166 329  GLY   B C   
5152  O  O   . GLY   B 329 ? 1.0725 1.0618 1.0677 0.0435  -0.1759 -0.0196 329  GLY   B O   
5153  N  N   . ASP   B 330 ? 1.0599 1.0360 1.0347 0.0548  -0.1764 -0.0178 330  ASP   B N   
5154  C  CA  . ASP   B 330 ? 1.0552 1.0204 1.0257 0.0579  -0.1840 -0.0230 330  ASP   B CA  
5155  C  C   . ASP   B 330 ? 1.0643 1.0309 1.0299 0.0626  -0.1842 -0.0240 330  ASP   B C   
5156  O  O   . ASP   B 330 ? 1.0503 1.0218 1.0099 0.0667  -0.1787 -0.0205 330  ASP   B O   
5157  C  CB  . ASP   B 330 ? 1.1094 1.0611 1.0675 0.0644  -0.1877 -0.0240 330  ASP   B CB  
5158  C  CG  . ASP   B 330 ? 1.0991 1.0450 1.0626 0.0595  -0.1907 -0.0254 330  ASP   B CG  
5159  O  OD1 . ASP   B 330 ? 1.1125 1.0660 1.0884 0.0516  -0.1879 -0.0240 330  ASP   B OD1 
5160  O  OD2 . ASP   B 330 ? 1.1606 1.0938 1.1156 0.0638  -0.1957 -0.0277 330  ASP   B OD2 
5161  N  N   . SER   B 331 ? 1.0488 1.0114 1.0176 0.0617  -0.1904 -0.0288 331  SER   B N   
5162  C  CA  . SER   B 331 ? 1.0493 1.0086 1.0100 0.0678  -0.1925 -0.0308 331  SER   B CA  
5163  C  C   . SER   B 331 ? 1.1302 1.0749 1.0739 0.0773  -0.1965 -0.0324 331  SER   B C   
5164  O  O   . SER   B 331 ? 1.1369 1.0729 1.0773 0.0783  -0.2000 -0.0336 331  SER   B O   
5165  C  CB  . SER   B 331 ? 1.1051 1.0645 1.0749 0.0640  -0.1985 -0.0357 331  SER   B CB  
5166  O  OG  . SER   B 331 ? 1.1676 1.1405 1.1495 0.0575  -0.1939 -0.0339 331  SER   B OG  
5167  N  N   . GLN   B 332 ? 1.1692 1.1106 1.1017 0.0847  -0.1958 -0.0324 332  GLN   B N   
5168  C  CA  . GLN   B 332 ? 1.1270 1.0553 1.0416 0.0947  -0.1975 -0.0327 332  GLN   B CA  
5169  C  C   . GLN   B 332 ? 1.1887 1.1111 1.0925 0.1017  -0.1993 -0.0347 332  GLN   B C   
5170  O  O   . GLN   B 332 ? 1.1839 1.1148 1.0932 0.0994  -0.1966 -0.0340 332  GLN   B O   
5171  C  CB  . GLN   B 332 ? 1.1214 1.0536 1.0304 0.0978  -0.1893 -0.0270 332  GLN   B CB  
5172  C  CG  . GLN   B 332 ? 1.1691 1.1154 1.0830 0.0960  -0.1805 -0.0222 332  GLN   B CG  
5173  C  CD  . GLN   B 332 ? 1.1916 1.1434 1.1030 0.0982  -0.1726 -0.0166 332  GLN   B CD  
5174  O  OE1 . GLN   B 332 ? 1.1436 1.1075 1.0609 0.0960  -0.1656 -0.0126 332  GLN   B OE1 
5175  N  NE2 . GLN   B 332 ? 1.1878 1.1308 1.0909 0.1025  -0.1740 -0.0164 332  GLN   B NE2 
5176  N  N   . LEU   B 333 ? 1.2455 1.1524 1.1334 0.1105  -0.2044 -0.0374 333  LEU   B N   
5177  C  CA  . LEU   B 333 ? 1.1949 1.0936 1.0670 0.1199  -0.2043 -0.0379 333  LEU   B CA  
5178  C  C   . LEU   B 333 ? 1.2079 1.1055 1.0680 0.1269  -0.1961 -0.0327 333  LEU   B C   
5179  O  O   . LEU   B 333 ? 1.2710 1.1640 1.1270 0.1286  -0.1960 -0.0316 333  LEU   B O   
5180  C  CB  . LEU   B 333 ? 1.1489 1.0300 1.0094 0.1261  -0.2149 -0.0441 333  LEU   B CB  
5181  C  CG  . LEU   B 333 ? 1.2593 1.1396 1.1291 0.1217  -0.2237 -0.0500 333  LEU   B CG  
5182  C  CD1 . LEU   B 333 ? 1.2266 1.0897 1.0881 0.1262  -0.2355 -0.0564 333  LEU   B CD1 
5183  C  CD2 . LEU   B 333 ? 1.2909 1.1742 1.1572 0.1245  -0.2214 -0.0497 333  LEU   B CD2 
5184  N  N   . VAL   B 334 ? 1.2317 1.1336 1.0868 0.1306  -0.1892 -0.0293 334  VAL   B N   
5185  C  CA  . VAL   B 334 ? 1.2414 1.1427 1.0860 0.1376  -0.1808 -0.0242 334  VAL   B CA  
5186  C  C   . VAL   B 334 ? 1.2919 1.1822 1.1191 0.1476  -0.1803 -0.0248 334  VAL   B C   
5187  O  O   . VAL   B 334 ? 1.3353 1.2264 1.1636 0.1469  -0.1820 -0.0267 334  VAL   B O   
5188  C  CB  . VAL   B 334 ? 1.2416 1.1607 1.0987 0.1320  -0.1709 -0.0184 334  VAL   B CB  
5189  C  CG1 . VAL   B 334 ? 1.2177 1.1476 1.0921 0.1215  -0.1719 -0.0182 334  VAL   B CG1 
5190  C  CG2 . VAL   B 334 ? 1.2222 1.1481 1.0828 0.1306  -0.1678 -0.0178 334  VAL   B CG2 
5191  N  N   . LYS   B 335 ? 1.3299 1.2090 1.1405 0.1573  -0.1779 -0.0232 335  LYS   B N   
5192  C  CA  . LYS   B 335 ? 1.3705 1.2380 1.1626 0.1679  -0.1761 -0.0231 335  LYS   B CA  
5193  C  C   . LYS   B 335 ? 1.3998 1.2767 1.1921 0.1702  -0.1635 -0.0164 335  LYS   B C   
5194  O  O   . LYS   B 335 ? 1.3742 1.2584 1.1712 0.1692  -0.1574 -0.0122 335  LYS   B O   
5195  C  CB  . LYS   B 335 ? 1.2717 1.1196 1.0439 0.1781  -0.1810 -0.0256 335  LYS   B CB  
5196  N  N   . LEU   B 336 ? 1.4202 1.2973 1.2082 0.1729  -0.1599 -0.0155 336  LEU   B N   
5197  C  CA  . LEU   B 336 ? 1.4711 1.3561 1.2590 0.1754  -0.1479 -0.0093 336  LEU   B CA  
5198  C  C   . LEU   B 336 ? 1.5952 1.4640 1.3605 0.1885  -0.1446 -0.0082 336  LEU   B C   
5199  O  O   . LEU   B 336 ? 1.6927 1.5481 1.4437 0.1948  -0.1488 -0.0114 336  LEU   B O   
5200  C  CB  . LEU   B 336 ? 1.4499 1.3451 1.2472 0.1703  -0.1449 -0.0086 336  LEU   B CB  
5201  C  CG  . LEU   B 336 ? 1.4149 1.3256 1.2337 0.1577  -0.1476 -0.0097 336  LEU   B CG  
5202  C  CD1 . LEU   B 336 ? 1.3988 1.3101 1.2192 0.1557  -0.1501 -0.0121 336  LEU   B CD1 
5203  C  CD2 . LEU   B 336 ? 1.3998 1.3281 1.2335 0.1516  -0.1385 -0.0041 336  LEU   B CD2 
5204  N  N   . ASN   B 337 ? 1.6176 1.4872 1.3792 0.1930  -0.1371 -0.0037 337  ASN   B N   
5205  C  CA  . ASN   B 337 ? 1.6562 1.5100 1.3961 0.2058  -0.1334 -0.0023 337  ASN   B CA  
5206  C  C   . ASN   B 337 ? 1.7281 1.5847 1.4642 0.2101  -0.1224 0.0025  337  ASN   B C   
5207  O  O   . ASN   B 337 ? 1.7139 1.5863 1.4656 0.2029  -0.1169 0.0054  337  ASN   B O   
5208  C  CB  . ASN   B 337 ? 1.6716 1.5238 1.4087 0.2094  -0.1306 0.0002  337  ASN   B CB  
5209  C  CG  . ASN   B 337 ? 1.6073 1.4504 1.3414 0.2083  -0.1419 -0.0050 337  ASN   B CG  
5210  O  OD1 . ASN   B 337 ? 1.4552 1.3076 1.2026 0.2014  -0.1433 -0.0045 337  ASN   B OD1 
5211  N  ND2 . ASN   B 337 ? 1.5797 1.4039 1.2963 0.2153  -0.1501 -0.0100 337  ASN   B ND2 
5212  N  N   . VAL   B 338 ? 1.8151 1.6553 1.5295 0.2223  -0.1193 0.0033  338  VAL   B N   
5213  C  CA  . VAL   B 338 ? 1.7963 1.6361 1.5043 0.2278  -0.1085 0.0079  338  VAL   B CA  
5214  C  C   . VAL   B 338 ? 1.8206 1.6737 1.5390 0.2271  -0.0960 0.0148  338  VAL   B C   
5215  O  O   . VAL   B 338 ? 1.8152 1.6809 1.5447 0.2233  -0.0875 0.0189  338  VAL   B O   
5216  C  CB  . VAL   B 338 ? 1.7345 1.5509 1.4146 0.2416  -0.1093 0.0064  338  VAL   B CB  
5217  N  N   . ASP   B 339 ? 1.8682 1.7190 1.5838 0.2306  -0.0951 0.0161  339  ASP   B N   
5218  C  CA  . ASP   B 339 ? 1.8683 1.7328 1.5959 0.2293  -0.0850 0.0221  339  ASP   B CA  
5219  C  C   . ASP   B 339 ? 1.8380 1.7192 1.5873 0.2176  -0.0892 0.0214  339  ASP   B C   
5220  O  O   . ASP   B 339 ? 1.8284 1.7090 1.5820 0.2114  -0.0997 0.0164  339  ASP   B O   
5221  C  CB  . ASP   B 339 ? 1.9111 1.7631 1.6224 0.2407  -0.0809 0.0241  339  ASP   B CB  
5222  N  N   . SER   B 340 ? 1.8479 1.7437 1.6111 0.2149  -0.0809 0.0265  340  SER   B N   
5223  C  CA  . SER   B 340 ? 1.8536 1.7646 1.6359 0.2051  -0.0839 0.0265  340  SER   B CA  
5224  C  C   . SER   B 340 ? 1.9550 1.8587 1.7303 0.2096  -0.0870 0.0259  340  SER   B C   
5225  O  O   . SER   B 340 ? 1.9123 1.7990 1.6680 0.2197  -0.0879 0.0249  340  SER   B O   
5226  C  CB  . SER   B 340 ? 1.8155 1.7460 1.6168 0.1996  -0.0744 0.0319  340  SER   B CB  
5227  O  OG  . SER   B 340 ? 1.9110 1.8434 1.7114 0.2061  -0.0656 0.0367  340  SER   B OG  
5228  N  N   . ASN   B 341 ? 2.0173 1.9329 1.8076 0.2023  -0.0890 0.0264  341  ASN   B N   
5229  C  CA  . ASN   B 341 ? 2.0527 1.9627 1.8380 0.2056  -0.0920 0.0259  341  ASN   B CA  
5230  C  C   . ASN   B 341 ? 2.1200 2.0421 1.9152 0.2068  -0.0828 0.0316  341  ASN   B C   
5231  O  O   . ASN   B 341 ? 2.0736 2.0060 1.8768 0.2068  -0.0737 0.0358  341  ASN   B O   
5232  C  CB  . ASN   B 341 ? 2.0568 1.9676 1.8490 0.1972  -0.1028 0.0214  341  ASN   B CB  
5233  C  CG  . ASN   B 341 ? 2.0892 2.0189 1.9029 0.1871  -0.1015 0.0235  341  ASN   B CG  
5234  O  OD1 . ASN   B 341 ? 2.1388 2.0825 1.9643 0.1849  -0.0936 0.0279  341  ASN   B OD1 
5235  N  ND2 . ASN   B 341 ? 2.0760 2.0054 1.8944 0.1809  -0.1095 0.0203  341  ASN   B ND2 
5236  N  N   . GLU   B 342 ? 2.2318 2.1524 2.0263 0.2082  -0.0851 0.0316  342  GLU   B N   
5237  C  CA  . GLU   B 342 ? 2.2600 2.1918 2.0639 0.2096  -0.0775 0.0366  342  GLU   B CA  
5238  C  C   . GLU   B 342 ? 2.2940 2.2468 2.1205 0.2002  -0.0733 0.0394  342  GLU   B C   
5239  O  O   . GLU   B 342 ? 2.3254 2.2875 2.1591 0.2022  -0.0639 0.0440  342  GLU   B O   
5240  C  CB  . GLU   B 342 ? 2.2273 2.1549 2.0289 0.2103  -0.0829 0.0353  342  GLU   B CB  
5241  N  N   . GLN   B 343 ? 2.2915 2.2518 2.1295 0.1897  -0.0803 0.0367  343  GLN   B N   
5242  C  CA  . GLN   B 343 ? 2.2243 2.2032 2.0824 0.1805  -0.0774 0.0387  343  GLN   B CA  
5243  C  C   . GLN   B 343 ? 2.2037 2.1843 2.0624 0.1796  -0.0735 0.0392  343  GLN   B C   
5244  O  O   . GLN   B 343 ? 2.2409 2.2312 2.1078 0.1804  -0.0648 0.0433  343  GLN   B O   
5245  C  CB  . GLN   B 343 ? 2.1824 2.1666 2.0503 0.1702  -0.0857 0.0355  343  GLN   B CB  
5246  N  N   . GLY   B 344 ? 2.0595 2.0308 1.9102 0.1781  -0.0797 0.0350  344  GLY   B N   
5247  C  CA  . GLY   B 344 ? 1.9571 1.9275 1.8056 0.1784  -0.0766 0.0351  344  GLY   B CA  
5248  C  C   . GLY   B 344 ? 1.8163 1.7823 1.6634 0.1727  -0.0851 0.0300  344  GLY   B C   
5249  O  O   . GLY   B 344 ? 1.7384 1.7064 1.5871 0.1707  -0.0835 0.0298  344  GLY   B O   
5250  N  N   . SER   B 345 ? 1.7592 1.7189 1.6036 0.1702  -0.0943 0.0259  345  SER   B N   
5251  C  CA  . SER   B 345 ? 1.6099 1.5664 1.4553 0.1642  -0.1029 0.0209  345  SER   B CA  
5252  C  C   . SER   B 345 ? 1.6100 1.5482 1.4362 0.1720  -0.1070 0.0174  345  SER   B C   
5253  O  O   . SER   B 345 ? 1.6239 1.5484 1.4367 0.1783  -0.1113 0.0153  345  SER   B O   
5254  C  CB  . SER   B 345 ? 1.6098 1.5678 1.4619 0.1577  -0.1105 0.0182  345  SER   B CB  
5255  O  OG  . SER   B 345 ? 1.5184 1.4728 1.3719 0.1521  -0.1187 0.0133  345  SER   B OG  
5256  N  N   . TYR   B 346 ? 1.5123 1.4497 1.3367 0.1719  -0.1060 0.0167  346  TYR   B N   
5257  C  CA  . TYR   B 346 ? 1.5189 1.4397 1.3270 0.1775  -0.1121 0.0123  346  TYR   B CA  
5258  C  C   . TYR   B 346 ? 1.4349 1.3510 1.2450 0.1721  -0.1238 0.0065  346  TYR   B C   
5259  O  O   . TYR   B 346 ? 1.4392 1.3430 1.2388 0.1752  -0.1305 0.0020  346  TYR   B O   
5260  C  CB  . TYR   B 346 ? 1.5505 1.4726 1.3577 0.1776  -0.1086 0.0128  346  TYR   B CB  
5261  C  CG  . TYR   B 346 ? 1.6298 1.5567 1.4363 0.1822  -0.0965 0.0186  346  TYR   B CG  
5262  C  CD1 . TYR   B 346 ? 1.6436 1.5878 1.4670 0.1768  -0.0890 0.0233  346  TYR   B CD1 
5263  C  CD2 . TYR   B 346 ? 1.7294 1.6434 1.5187 0.1918  -0.0926 0.0193  346  TYR   B CD2 
5264  C  CE1 . TYR   B 346 ? 1.6542 1.6032 1.4786 0.1806  -0.0778 0.0286  346  TYR   B CE1 
5265  C  CE2 . TYR   B 346 ? 1.7647 1.6829 1.5539 0.1958  -0.0808 0.0248  346  TYR   B CE2 
5266  C  CZ  . TYR   B 346 ? 1.7227 1.6590 1.5305 0.1899  -0.0734 0.0295  346  TYR   B CZ  
5267  O  OH  . TYR   B 346 ? 1.6991 1.6406 1.5093 0.1932  -0.0616 0.0350  346  TYR   B OH  
5268  N  N   . VAL   B 347 ? 1.4013 1.3270 1.2252 0.1641  -0.1264 0.0063  347  VAL   B N   
5269  C  CA  . VAL   B 347 ? 1.3936 1.3171 1.2229 0.1575  -0.1364 0.0012  347  VAL   B CA  
5270  C  C   . VAL   B 347 ? 1.3934 1.3066 1.2150 0.1609  -0.1415 -0.0006 347  VAL   B C   
5271  O  O   . VAL   B 347 ? 1.4322 1.3475 1.2529 0.1638  -0.1365 0.0029  347  VAL   B O   
5272  C  CB  . VAL   B 347 ? 1.3628 1.3040 1.2131 0.1456  -0.1357 0.0022  347  VAL   B CB  
5273  C  CG1 . VAL   B 347 ? 1.3460 1.2851 1.2028 0.1386  -0.1454 -0.0029 347  VAL   B CG1 
5274  C  CG2 . VAL   B 347 ? 1.2900 1.2410 1.1471 0.1428  -0.1303 0.0042  347  VAL   B CG2 
5275  N  N   . VAL   B 348 ? 1.3233 1.2249 1.1394 0.1608  -0.1513 -0.0062 348  VAL   B N   
5276  C  CA  . VAL   B 348 ? 1.3321 1.2244 1.1433 0.1622  -0.1571 -0.0084 348  VAL   B CA  
5277  C  C   . VAL   B 348 ? 1.3451 1.2354 1.1641 0.1548  -0.1672 -0.0139 348  VAL   B C   
5278  O  O   . VAL   B 348 ? 1.3036 1.1882 1.1196 0.1552  -0.1726 -0.0179 348  VAL   B O   
5279  C  CB  . VAL   B 348 ? 1.2549 1.1288 1.0443 0.1744  -0.1586 -0.0095 348  VAL   B CB  
5280  C  CG1 . VAL   B 348 ? 1.2923 1.1512 1.0716 0.1772  -0.1687 -0.0158 348  VAL   B CG1 
5281  C  CG2 . VAL   B 348 ? 1.3472 1.2169 1.1337 0.1762  -0.1594 -0.0087 348  VAL   B CG2 
5282  N  N   . ALA   B 349 ? 1.2830 1.1787 1.1131 0.1478  -0.1693 -0.0140 349  ALA   B N   
5283  C  CA  . ALA   B 349 ? 1.2637 1.1587 1.1033 0.1400  -0.1778 -0.0189 349  ALA   B CA  
5284  C  C   . ALA   B 349 ? 1.2643 1.1403 1.0903 0.1460  -0.1873 -0.0243 349  ALA   B C   
5285  O  O   . ALA   B 349 ? 1.2800 1.1459 1.0955 0.1515  -0.1885 -0.0243 349  ALA   B O   
5286  C  CB  . ALA   B 349 ? 1.2017 1.1062 1.0554 0.1315  -0.1769 -0.0172 349  ALA   B CB  
5287  N  N   . MET   B 350 ? 1.2357 1.1065 1.0614 0.1453  -0.1942 -0.0291 350  MET   B N   
5288  C  CA  . MET   B 350 ? 1.2398 1.0923 1.0527 0.1512  -0.2040 -0.0347 350  MET   B CA  
5289  C  C   . MET   B 350 ? 1.2587 1.1097 1.0836 0.1433  -0.2135 -0.0399 350  MET   B C   
5290  O  O   . MET   B 350 ? 1.3657 1.2017 1.1820 0.1472  -0.2226 -0.0451 350  MET   B O   
5291  C  CB  . MET   B 350 ? 1.2173 1.0609 1.0168 0.1590  -0.2059 -0.0369 350  MET   B CB  
5292  C  CG  . MET   B 350 ? 1.3197 1.1667 1.1289 0.1535  -0.2118 -0.0411 350  MET   B CG  
5293  S  SD  . MET   B 350 ? 1.4279 1.2619 1.2185 0.1640  -0.2146 -0.0438 350  MET   B SD  
5294  C  CE  . MET   B 350 ? 1.3672 1.1853 1.1548 0.1647  -0.2306 -0.0528 350  MET   B CE  
5295  N  N   . GLU   B 351 ? 1.2499 1.1157 1.0944 0.1324  -0.2115 -0.0388 351  GLU   B N   
5296  C  CA  . GLU   B 351 ? 1.2101 1.0763 1.0684 0.1239  -0.2185 -0.0427 351  GLU   B CA  
5297  C  C   . GLU   B 351 ? 1.1852 1.0689 1.0617 0.1137  -0.2119 -0.0388 351  GLU   B C   
5298  O  O   . GLU   B 351 ? 1.1886 1.0838 1.0675 0.1132  -0.2034 -0.0340 351  GLU   B O   
5299  C  CB  . GLU   B 351 ? 1.1988 1.0610 1.0613 0.1222  -0.2273 -0.0487 351  GLU   B CB  
5300  C  CG  . GLU   B 351 ? 1.3247 1.1696 1.1797 0.1259  -0.2386 -0.0549 351  GLU   B CG  
5301  C  CD  . GLU   B 351 ? 1.4021 1.2471 1.2702 0.1199  -0.2476 -0.0609 351  GLU   B CD  
5302  O  OE1 . GLU   B 351 ? 1.3940 1.2344 1.2570 0.1239  -0.2525 -0.0644 351  GLU   B OE1 
5303  O  OE2 . GLU   B 351 ? 1.4297 1.2792 1.3134 0.1112  -0.2498 -0.0620 351  GLU   B OE2 
5304  N  N   . THR   B 352 ? 1.1896 1.0748 1.0791 0.1056  -0.2160 -0.0409 352  THR   B N   
5305  C  CA  . THR   B 352 ? 1.1710 1.0717 1.0783 0.0955  -0.2108 -0.0381 352  THR   B CA  
5306  C  C   . THR   B 352 ? 1.1628 1.0633 1.0845 0.0875  -0.2176 -0.0426 352  THR   B C   
5307  O  O   . THR   B 352 ? 1.2491 1.1372 1.1677 0.0892  -0.2260 -0.0474 352  THR   B O   
5308  C  CB  . THR   B 352 ? 1.0966 1.0010 1.0046 0.0939  -0.2049 -0.0334 352  THR   B CB  
5309  O  OG1 . THR   B 352 ? 1.2061 1.0983 1.1104 0.0947  -0.2109 -0.0361 352  THR   B OG1 
5310  C  CG2 . THR   B 352 ? 1.0727 0.9782 0.9681 0.1018  -0.1979 -0.0288 352  THR   B CG2 
5311  N  N   . PHE   B 353 ? 1.1396 1.0538 1.0775 0.0786  -0.2137 -0.0409 353  PHE   B N   
5312  C  CA  . PHE   B 353 ? 1.1458 1.0622 1.0999 0.0701  -0.2184 -0.0445 353  PHE   B CA  
5313  C  C   . PHE   B 353 ? 1.1613 1.0882 1.1285 0.0614  -0.2122 -0.0407 353  PHE   B C   
5314  O  O   . PHE   B 353 ? 1.1585 1.0971 1.1283 0.0595  -0.2044 -0.0361 353  PHE   B O   
5315  C  CB  . PHE   B 353 ? 1.1418 1.0634 1.1028 0.0684  -0.2209 -0.0474 353  PHE   B CB  
5316  C  CG  . PHE   B 353 ? 1.1391 1.0499 1.0865 0.0772  -0.2270 -0.0511 353  PHE   B CG  
5317  C  CD1 . PHE   B 353 ? 1.1361 1.0352 1.0831 0.0786  -0.2373 -0.0573 353  PHE   B CD1 
5318  C  CD2 . PHE   B 353 ? 1.1179 1.0296 1.0527 0.0842  -0.2226 -0.0485 353  PHE   B CD2 
5319  C  CE1 . PHE   B 353 ? 1.2009 1.0890 1.1341 0.0872  -0.2434 -0.0609 353  PHE   B CE1 
5320  C  CE2 . PHE   B 353 ? 1.1491 1.0497 1.0701 0.0927  -0.2279 -0.0518 353  PHE   B CE2 
5321  C  CZ  . PHE   B 353 ? 1.1548 1.0433 1.0743 0.0944  -0.2385 -0.0581 353  PHE   B CZ  
5322  N  N   . THR   B 354 ? 1.1302 1.0526 1.1055 0.0562  -0.2157 -0.0427 354  THR   B N   
5323  C  CA  . THR   B 354 ? 1.1069 1.0366 1.0918 0.0490  -0.2097 -0.0389 354  THR   B CA  
5324  C  C   . THR   B 354 ? 1.0744 1.0182 1.0742 0.0414  -0.2052 -0.0376 354  THR   B C   
5325  O  O   . THR   B 354 ? 1.0579 1.0036 1.0671 0.0383  -0.2092 -0.0412 354  THR   B O   
5326  C  CB  . THR   B 354 ? 1.1180 1.0386 1.1081 0.0453  -0.2143 -0.0415 354  THR   B CB  
5327  O  OG1 . THR   B 354 ? 1.2981 1.2055 1.2729 0.0529  -0.2180 -0.0424 354  THR   B OG1 
5328  C  CG2 . THR   B 354 ? 1.0739 1.0008 1.0725 0.0383  -0.2077 -0.0373 354  THR   B CG2 
5329  N  N   . ASN   B 355 ? 1.0275 0.9809 1.0290 0.0388  -0.1971 -0.0323 355  ASN   B N   
5330  C  CA  . ASN   B 355 ? 1.0162 0.9824 1.0311 0.0313  -0.1921 -0.0304 355  ASN   B CA  
5331  C  C   . ASN   B 355 ? 1.0357 1.0046 1.0543 0.0265  -0.1866 -0.0264 355  ASN   B C   
5332  O  O   . ASN   B 355 ? 1.0641 1.0340 1.0739 0.0300  -0.1824 -0.0225 355  ASN   B O   
5333  C  CB  . ASN   B 355 ? 1.0351 1.0112 1.0471 0.0337  -0.1876 -0.0279 355  ASN   B CB  
5334  C  CG  . ASN   B 355 ? 1.0583 1.0473 1.0824 0.0264  -0.1818 -0.0253 355  ASN   B CG  
5335  O  OD1 . ASN   B 355 ? 1.0261 1.0168 1.0623 0.0194  -0.1822 -0.0265 355  ASN   B OD1 
5336  N  ND2 . ASN   B 355 ? 1.0412 1.0392 1.0622 0.0279  -0.1761 -0.0216 355  ASN   B ND2 
5337  N  N   . LEU   B 356 ? 1.0243 0.9940 1.0557 0.0189  -0.1866 -0.0274 356  LEU   B N   
5338  C  CA  . LEU   B 356 ? 0.9997 0.9714 1.0342 0.0142  -0.1811 -0.0235 356  LEU   B CA  
5339  C  C   . LEU   B 356 ? 1.0300 1.0147 1.0710 0.0098  -0.1740 -0.0198 356  LEU   B C   
5340  O  O   . LEU   B 356 ? 1.0637 1.0504 1.1066 0.0062  -0.1691 -0.0164 356  LEU   B O   
5341  C  CB  . LEU   B 356 ? 1.0068 0.9724 1.0517 0.0082  -0.1834 -0.0258 356  LEU   B CB  
5342  C  CG  . LEU   B 356 ? 0.9587 0.9132 1.0027 0.0106  -0.1921 -0.0311 356  LEU   B CG  
5343  C  CD1 . LEU   B 356 ? 1.0192 0.9700 1.0763 0.0034  -0.1931 -0.0328 356  LEU   B CD1 
5344  C  CD2 . LEU   B 356 ? 1.0322 0.9768 1.0606 0.0179  -0.1941 -0.0305 356  LEU   B CD2 
5345  N  N   . GLY   B 357 ? 1.0227 1.0155 1.0665 0.0101  -0.1736 -0.0205 357  GLY   B N   
5346  C  CA  . GLY   B 357 ? 0.9685 0.9732 1.0178 0.0063  -0.1673 -0.0172 357  GLY   B CA  
5347  C  C   . GLY   B 357 ? 0.9943 1.0045 1.0339 0.0109  -0.1630 -0.0132 357  GLY   B C   
5348  O  O   . GLY   B 357 ? 1.0053 1.0118 1.0344 0.0179  -0.1648 -0.0132 357  GLY   B O   
5349  N  N   . PRO   B 358 ? 0.9955 1.0146 1.0390 0.0071  -0.1570 -0.0095 358  PRO   B N   
5350  C  CA  . PRO   B 358 ? 0.9938 1.0156 1.0475 -0.0005 -0.1539 -0.0086 358  PRO   B CA  
5351  C  C   . PRO   B 358 ? 0.9962 1.0096 1.0474 -0.0016 -0.1535 -0.0074 358  PRO   B C   
5352  O  O   . PRO   B 358 ? 0.9461 0.9554 0.9872 0.0031  -0.1533 -0.0055 358  PRO   B O   
5353  C  CB  . PRO   B 358 ? 0.9490 0.9817 1.0035 -0.0021 -0.1481 -0.0049 358  PRO   B CB  
5354  C  CG  . PRO   B 358 ? 0.9255 0.9602 0.9698 0.0047  -0.1476 -0.0030 358  PRO   B CG  
5355  C  CD  . PRO   B 358 ? 0.9505 0.9785 0.9900 0.0098  -0.1531 -0.0065 358  PRO   B CD  
5356  N  N   . ILE   B 359 ? 1.0200 1.0305 1.0807 -0.0077 -0.1533 -0.0086 359  ILE   B N   
5357  C  CA  . ILE   B 359 ? 1.0227 1.0254 1.0823 -0.0098 -0.1518 -0.0071 359  ILE   B CA  
5358  C  C   . ILE   B 359 ? 1.0453 1.0540 1.1064 -0.0136 -0.1450 -0.0029 359  ILE   B C   
5359  O  O   . ILE   B 359 ? 1.0488 1.0614 1.1199 -0.0196 -0.1421 -0.0029 359  ILE   B O   
5360  C  CB  . ILE   B 359 ? 1.0414 1.0373 1.1109 -0.0144 -0.1549 -0.0106 359  ILE   B CB  
5361  C  CG1 . ILE   B 359 ? 1.0430 1.0313 1.1095 -0.0100 -0.1626 -0.0150 359  ILE   B CG1 
5362  C  CG2 . ILE   B 359 ? 1.0697 1.0582 1.1390 -0.0175 -0.1519 -0.0084 359  ILE   B CG2 
5363  C  CD1 . ILE   B 359 ? 1.0808 1.0574 1.1370 -0.0060 -0.1650 -0.0147 359  ILE   B CD1 
5364  N  N   . VAL   B 360 ? 1.0052 1.0144 1.0564 -0.0100 -0.1425 0.0007  360  VAL   B N   
5365  C  CA  . VAL   B 360 ? 0.9942 1.0086 1.0451 -0.0127 -0.1367 0.0046  360  VAL   B CA  
5366  C  C   . VAL   B 360 ? 1.0230 1.0293 1.0738 -0.0161 -0.1339 0.0063  360  VAL   B C   
5367  O  O   . VAL   B 360 ? 1.0890 1.0977 1.1452 -0.0212 -0.1294 0.0079  360  VAL   B O   
5368  C  CB  . VAL   B 360 ? 0.9451 0.9647 0.9866 -0.0074 -0.1354 0.0075  360  VAL   B CB  
5369  C  CG1 . VAL   B 360 ? 0.9648 0.9932 1.0080 -0.0051 -0.1368 0.0062  360  VAL   B CG1 
5370  C  CG2 . VAL   B 360 ? 0.9100 0.9217 0.9412 -0.0017 -0.1377 0.0081  360  VAL   B CG2 
5371  N  N   . ASP   B 361 ? 1.0343 1.0306 1.0787 -0.0133 -0.1363 0.0060  361  ASP   B N   
5372  C  CA  . ASP   B 361 ? 1.0102 0.9970 1.0541 -0.0163 -0.1341 0.0074  361  ASP   B CA  
5373  C  C   . ASP   B 361 ? 1.0579 1.0341 1.1016 -0.0151 -0.1391 0.0043  361  ASP   B C   
5374  O  O   . ASP   B 361 ? 0.9987 0.9737 1.0381 -0.0102 -0.1441 0.0020  361  ASP   B O   
5375  C  CB  . ASP   B 361 ? 1.0171 1.0017 1.0498 -0.0132 -0.1310 0.0116  361  ASP   B CB  
5376  C  CG  . ASP   B 361 ? 1.0994 1.0752 1.1317 -0.0171 -0.1270 0.0137  361  ASP   B CG  
5377  O  OD1 . ASP   B 361 ? 1.0448 1.0184 1.0872 -0.0230 -0.1255 0.0124  361  ASP   B OD1 
5378  O  OD2 . ASP   B 361 ? 1.0525 1.0237 1.0747 -0.0142 -0.1253 0.0168  361  ASP   B OD2 
5379  N  N   . MET   B 362 ? 1.0687 1.0365 1.1170 -0.0196 -0.1376 0.0043  362  MET   B N   
5380  C  CA  . MET   B 362 ? 1.0699 1.0264 1.1181 -0.0190 -0.1422 0.0015  362  MET   B CA  
5381  C  C   . MET   B 362 ? 1.0632 1.0098 1.1103 -0.0223 -0.1384 0.0038  362  MET   B C   
5382  O  O   . MET   B 362 ? 1.0334 0.9819 1.0811 -0.0255 -0.1322 0.0072  362  MET   B O   
5383  C  CB  . MET   B 362 ? 1.0481 1.0055 1.1089 -0.0221 -0.1467 -0.0034 362  MET   B CB  
5384  C  CG  . MET   B 362 ? 1.0991 1.0554 1.1745 -0.0303 -0.1436 -0.0040 362  MET   B CG  
5385  S  SD  . MET   B 362 ? 1.0927 1.0563 1.1857 -0.0347 -0.1470 -0.0089 362  MET   B SD  
5386  C  CE  . MET   B 362 ? 1.0793 1.0411 1.1655 -0.0274 -0.1565 -0.0133 362  MET   B CE  
5387  N  N   . CYS   B 363 ? 1.1111 1.0461 1.1556 -0.0211 -0.1422 0.0020  363  CYS   B N   
5388  C  CA  . CYS   B 363 ? 1.1082 1.0322 1.1527 -0.0245 -0.1390 0.0037  363  CYS   B CA  
5389  C  C   . CYS   B 363 ? 1.1020 1.0159 1.1506 -0.0250 -0.1450 -0.0004 363  CYS   B C   
5390  O  O   . CYS   B 363 ? 1.1130 1.0260 1.1578 -0.0202 -0.1516 -0.0036 363  CYS   B O   
5391  C  CB  . CYS   B 363 ? 1.0686 0.9871 1.0980 -0.0199 -0.1365 0.0077  363  CYS   B CB  
5392  S  SG  . CYS   B 363 ? 1.1691 1.0815 1.1861 -0.0114 -0.1438 0.0056  363  CYS   B SG  
5393  N  N   . VAL   B 364 ? 1.1254 1.0309 1.1813 -0.0305 -0.1425 -0.0003 364  VAL   B N   
5394  C  CA  . VAL   B 364 ? 1.1725 1.0676 1.2339 -0.0320 -0.1481 -0.0042 364  VAL   B CA  
5395  C  C   . VAL   B 364 ? 1.1790 1.0605 1.2292 -0.0298 -0.1472 -0.0021 364  VAL   B C   
5396  O  O   . VAL   B 364 ? 1.1834 1.0622 1.2284 -0.0310 -0.1405 0.0023  364  VAL   B O   
5397  C  CB  . VAL   B 364 ? 1.1726 1.0686 1.2534 -0.0404 -0.1464 -0.0062 364  VAL   B CB  
5398  C  CG1 . VAL   B 364 ? 1.2097 1.1091 1.2941 -0.0454 -0.1365 -0.0015 364  VAL   B CG1 
5399  C  CG2 . VAL   B 364 ? 1.1738 1.0566 1.2601 -0.0428 -0.1505 -0.0093 364  VAL   B CG2 
5400  N  N   . VAL   B 365 ? 1.2193 1.0916 1.2646 -0.0260 -0.1542 -0.0053 365  VAL   B N   
5401  C  CA  . VAL   B 365 ? 1.2448 1.1046 1.2762 -0.0220 -0.1544 -0.0034 365  VAL   B CA  
5402  C  C   . VAL   B 365 ? 1.3328 1.1809 1.3653 -0.0210 -0.1622 -0.0080 365  VAL   B C   
5403  O  O   . VAL   B 365 ? 1.3342 1.1845 1.3688 -0.0184 -0.1692 -0.0124 365  VAL   B O   
5404  C  CB  . VAL   B 365 ? 1.2734 1.1371 1.2878 -0.0137 -0.1544 -0.0008 365  VAL   B CB  
5405  C  CG1 . VAL   B 365 ? 1.3350 1.1854 1.3351 -0.0088 -0.1555 0.0006  365  VAL   B CG1 
5406  C  CG2 . VAL   B 365 ? 1.1797 1.0540 1.1928 -0.0147 -0.1470 0.0038  365  VAL   B CG2 
5407  N  N   . ASP   B 366 ? 1.3804 1.2152 1.4106 -0.0228 -0.1609 -0.0071 366  ASP   B N   
5408  C  CA  . ASP   B 366 ? 1.4546 1.2762 1.4847 -0.0220 -0.1681 -0.0112 366  ASP   B CA  
5409  C  C   . ASP   B 366 ? 1.4824 1.2956 1.4925 -0.0134 -0.1707 -0.0100 366  ASP   B C   
5410  O  O   . ASP   B 366 ? 1.5079 1.3110 1.5097 -0.0128 -0.1676 -0.0071 366  ASP   B O   
5411  C  CB  . ASP   B 366 ? 1.5443 1.3560 1.5853 -0.0297 -0.1649 -0.0109 366  ASP   B CB  
5412  C  CG  . ASP   B 366 ? 1.6866 1.4851 1.7305 -0.0299 -0.1729 -0.0158 366  ASP   B CG  
5413  O  OD1 . ASP   B 366 ? 1.7373 1.5310 1.7695 -0.0227 -0.1801 -0.0183 366  ASP   B OD1 
5414  O  OD2 . ASP   B 366 ? 1.7299 1.5225 1.7882 -0.0372 -0.1719 -0.0170 366  ASP   B OD2 
5415  N  N   . LEU   B 367 ? 1.5037 1.3209 1.5059 -0.0063 -0.1765 -0.0123 367  LEU   B N   
5416  C  CA  . LEU   B 367 ? 1.5232 1.3337 1.5066 0.0026  -0.1789 -0.0113 367  LEU   B CA  
5417  C  C   . LEU   B 367 ? 1.6142 1.4077 1.5927 0.0043  -0.1848 -0.0142 367  LEU   B C   
5418  O  O   . LEU   B 367 ? 1.6808 1.4657 1.6440 0.0103  -0.1851 -0.0124 367  LEU   B O   
5419  C  CB  . LEU   B 367 ? 1.5603 1.3795 1.5375 0.0096  -0.1830 -0.0130 367  LEU   B CB  
5420  C  CG  . LEU   B 367 ? 1.5214 1.3536 1.4918 0.0136  -0.1780 -0.0090 367  LEU   B CG  
5421  C  CD1 . LEU   B 367 ? 1.4229 1.2645 1.4032 0.0066  -0.1703 -0.0054 367  LEU   B CD1 
5422  C  CD2 . LEU   B 367 ? 1.4338 1.2749 1.4045 0.0177  -0.1822 -0.0118 367  LEU   B CD2 
5423  N  N   . GLU   B 368 ? 1.6382 1.4266 1.6291 -0.0004 -0.1901 -0.0190 368  GLU   B N   
5424  C  CA  . GLU   B 368 ? 1.6678 1.4397 1.6542 0.0012  -0.1967 -0.0224 368  GLU   B CA  
5425  C  C   . GLU   B 368 ? 1.6944 1.4560 1.6891 -0.0062 -0.1934 -0.0214 368  GLU   B C   
5426  O  O   . GLU   B 368 ? 1.7221 1.4695 1.7154 -0.0061 -0.1987 -0.0243 368  GLU   B O   
5427  C  CB  . GLU   B 368 ? 1.6966 1.4674 1.6894 0.0021  -0.2062 -0.0289 368  GLU   B CB  
5428  C  CG  . GLU   B 368 ? 1.6397 1.4172 1.6208 0.0109  -0.2097 -0.0299 368  GLU   B CG  
5429  C  CD  . GLU   B 368 ? 1.7181 1.4991 1.7078 0.0108  -0.2175 -0.0357 368  GLU   B CD  
5430  O  OE1 . GLU   B 368 ? 1.7628 1.5353 1.7623 0.0069  -0.2237 -0.0404 368  GLU   B OE1 
5431  O  OE2 . GLU   B 368 ? 1.6930 1.4851 1.6799 0.0146  -0.2173 -0.0355 368  GLU   B OE2 
5432  N  N   . ARG   B 369 ? 1.7113 1.4791 1.7136 -0.0123 -0.1846 -0.0171 369  ARG   B N   
5433  C  CA  . ARG   B 369 ? 1.7332 1.4913 1.7432 -0.0194 -0.1800 -0.0155 369  ARG   B CA  
5434  C  C   . ARG   B 369 ? 1.8354 1.5870 1.8618 -0.0252 -0.1863 -0.0211 369  ARG   B C   
5435  O  O   . ARG   B 369 ? 1.7954 1.5326 1.8228 -0.0276 -0.1876 -0.0220 369  ARG   B O   
5436  C  CB  . ARG   B 369 ? 1.7201 1.4645 1.7129 -0.0149 -0.1781 -0.0123 369  ARG   B CB  
5437  C  CG  . ARG   B 369 ? 1.7617 1.5097 1.7464 -0.0146 -0.1684 -0.0057 369  ARG   B CG  
5438  C  CD  . ARG   B 369 ? 1.8592 1.5963 1.8489 -0.0214 -0.1618 -0.0028 369  ARG   B CD  
5439  N  NE  . ARG   B 369 ? 1.8863 1.6257 1.8676 -0.0210 -0.1526 0.0034  369  ARG   B NE  
5440  C  CZ  . ARG   B 369 ? 1.9154 1.6513 1.9035 -0.0277 -0.1444 0.0068  369  ARG   B CZ  
5441  N  NH1 . ARG   B 369 ? 1.9179 1.6495 1.9231 -0.0359 -0.1436 0.0047  369  ARG   B NH1 
5442  N  NH2 . ARG   B 369 ? 1.8598 1.5967 1.8374 -0.0259 -0.1369 0.0123  369  ARG   B NH2 
5443  N  N   . GLN   B 370 ? 1.9992 1.7612 2.0385 -0.0272 -0.1904 -0.0250 370  GLN   B N   
5444  C  CA  . GLN   B 370 ? 2.0207 1.7783 2.0765 -0.0321 -0.1978 -0.0310 370  GLN   B CA  
5445  C  C   . GLN   B 370 ? 2.0077 1.7735 2.0867 -0.0419 -0.1930 -0.0310 370  GLN   B C   
5446  O  O   . GLN   B 370 ? 2.0302 1.7926 2.1256 -0.0470 -0.1984 -0.0358 370  GLN   B O   
5447  C  CB  . GLN   B 370 ? 2.0377 1.7997 2.0912 -0.0264 -0.2077 -0.0364 370  GLN   B CB  
5448  C  CG  . GLN   B 370 ? 2.0656 1.8208 2.0964 -0.0159 -0.2125 -0.0367 370  GLN   B CG  
5449  C  CD  . GLN   B 370 ? 2.0717 1.8079 2.0942 -0.0140 -0.2171 -0.0383 370  GLN   B CD  
5450  O  OE1 . GLN   B 370 ? 2.0650 1.7926 2.1004 -0.0203 -0.2195 -0.0410 370  GLN   B OE1 
5451  N  NE2 . GLN   B 370 ? 2.0119 1.7416 2.0131 -0.0051 -0.2182 -0.0366 370  GLN   B NE2 
5452  N  N   . GLY   B 371 ? 1.8609 1.6374 1.9419 -0.0446 -0.1833 -0.0260 371  GLY   B N   
5453  C  CA  . GLY   B 371 ? 1.7581 1.5432 1.8605 -0.0533 -0.1783 -0.0259 371  GLY   B CA  
5454  C  C   . GLY   B 371 ? 1.7363 1.5352 1.8494 -0.0535 -0.1829 -0.0297 371  GLY   B C   
5455  O  O   . GLY   B 371 ? 1.6413 1.4463 1.7748 -0.0606 -0.1814 -0.0314 371  GLY   B O   
5456  N  N   . GLN   B 372 ? 1.7074 1.5110 1.8073 -0.0456 -0.1884 -0.0312 372  GLN   B N   
5457  C  CA  . GLN   B 372 ? 1.6579 1.4744 1.7658 -0.0449 -0.1925 -0.0345 372  GLN   B CA  
5458  C  C   . GLN   B 372 ? 1.6385 1.4690 1.7423 -0.0442 -0.1844 -0.0297 372  GLN   B C   
5459  O  O   . GLN   B 372 ? 1.6315 1.4711 1.7497 -0.0505 -0.1785 -0.0283 372  GLN   B O   
5460  C  CB  . GLN   B 372 ? 1.6745 1.4872 1.7705 -0.0366 -0.2032 -0.0391 372  GLN   B CB  
5461  C  CG  . GLN   B 372 ? 1.6853 1.5058 1.7933 -0.0370 -0.2107 -0.0448 372  GLN   B CG  
5462  C  CD  . GLN   B 372 ? 1.6980 1.5166 1.8296 -0.0455 -0.2134 -0.0488 372  GLN   B CD  
5463  O  OE1 . GLN   B 372 ? 1.6874 1.5105 1.8333 -0.0531 -0.2055 -0.0460 372  GLN   B OE1 
5464  N  NE2 . GLN   B 372 ? 1.7191 1.5307 1.8550 -0.0439 -0.2246 -0.0553 372  GLN   B NE2 
5465  N  N   . GLY   B 373 ? 1.5700 1.4022 1.6546 -0.0364 -0.1840 -0.0272 373  GLY   B N   
5466  C  CA  . GLY   B 373 ? 1.5090 1.3546 1.5892 -0.0351 -0.1775 -0.0231 373  GLY   B CA  
5467  C  C   . GLY   B 373 ? 1.3960 1.2515 1.4718 -0.0294 -0.1824 -0.0254 373  GLY   B C   
5468  O  O   . GLY   B 373 ? 1.3272 1.1888 1.4154 -0.0318 -0.1866 -0.0294 373  GLY   B O   
5469  N  N   . GLN   B 374 ? 1.3528 1.2095 1.4107 -0.0219 -0.1819 -0.0229 374  GLN   B N   
5470  C  CA  . GLN   B 374 ? 1.2767 1.1428 1.3276 -0.0159 -0.1844 -0.0236 374  GLN   B CA  
5471  C  C   . GLN   B 374 ? 1.2588 1.1389 1.3111 -0.0176 -0.1765 -0.0193 374  GLN   B C   
5472  O  O   . GLN   B 374 ? 1.2680 1.1487 1.3207 -0.0211 -0.1691 -0.0149 374  GLN   B O   
5473  C  CB  . GLN   B 374 ? 1.2591 1.1184 1.2904 -0.0066 -0.1877 -0.0232 374  GLN   B CB  
5474  C  CG  . GLN   B 374 ? 1.3592 1.2071 1.3870 -0.0027 -0.1975 -0.0286 374  GLN   B CG  
5475  C  CD  . GLN   B 374 ? 1.4894 1.3268 1.4978 0.0057  -0.1998 -0.0277 374  GLN   B CD  
5476  O  OE1 . GLN   B 374 ? 1.5104 1.3401 1.5126 0.0056  -0.1965 -0.0247 374  GLN   B OE1 
5477  N  NE2 . GLN   B 374 ? 1.5232 1.3597 1.5215 0.0134  -0.2055 -0.0302 374  GLN   B NE2 
5478  N  N   . LEU   B 375 ? 1.2360 1.1266 1.2882 -0.0147 -0.1782 -0.0204 375  LEU   B N   
5479  C  CA  . LEU   B 375 ? 1.1382 1.0422 1.1917 -0.0160 -0.1716 -0.0168 375  LEU   B CA  
5480  C  C   . LEU   B 375 ? 1.1182 1.0265 1.1564 -0.0078 -0.1718 -0.0149 375  LEU   B C   
5481  O  O   . LEU   B 375 ? 1.1549 1.0618 1.1876 -0.0023 -0.1778 -0.0180 375  LEU   B O   
5482  C  CB  . LEU   B 375 ? 1.1464 1.0602 1.2154 -0.0207 -0.1725 -0.0196 375  LEU   B CB  
5483  C  CG  . LEU   B 375 ? 1.1309 1.0579 1.2064 -0.0245 -0.1654 -0.0165 375  LEU   B CG  
5484  C  CD1 . LEU   B 375 ? 1.1337 1.0595 1.2101 -0.0291 -0.1570 -0.0116 375  LEU   B CD1 
5485  C  CD2 . LEU   B 375 ? 1.0589 0.9933 1.1512 -0.0294 -0.1674 -0.0201 375  LEU   B CD2 
5486  N  N   . VAL   B 376 ? 1.0736 0.9862 1.1047 -0.0068 -0.1654 -0.0099 376  VAL   B N   
5487  C  CA  . VAL   B 376 ? 1.0918 1.0096 1.1102 0.0005  -0.1647 -0.0076 376  VAL   B CA  
5488  C  C   . VAL   B 376 ? 1.1121 1.0443 1.1354 -0.0017 -0.1599 -0.0053 376  VAL   B C   
5489  O  O   . VAL   B 376 ? 1.1077 1.0435 1.1359 -0.0067 -0.1541 -0.0024 376  VAL   B O   
5490  C  CB  . VAL   B 376 ? 1.0982 1.0095 1.1036 0.0044  -0.1620 -0.0038 376  VAL   B CB  
5491  C  CG1 . VAL   B 376 ? 1.0541 0.9708 1.0478 0.0123  -0.1621 -0.0021 376  VAL   B CG1 
5492  C  CG2 . VAL   B 376 ? 1.0924 0.9884 1.0936 0.0054  -0.1661 -0.0058 376  VAL   B CG2 
5493  N  N   . THR   B 377 ? 1.0828 1.0226 1.1039 0.0025  -0.1621 -0.0065 377  THR   B N   
5494  C  CA  . THR   B 377 ? 1.0567 1.0100 1.0834 0.0004  -0.1584 -0.0052 377  THR   B CA  
5495  C  C   . THR   B 377 ? 1.0511 1.0111 1.0676 0.0063  -0.1561 -0.0020 377  THR   B C   
5496  O  O   . THR   B 377 ? 1.0475 1.0040 1.0543 0.0132  -0.1592 -0.0026 377  THR   B O   
5497  C  CB  . THR   B 377 ? 1.0452 1.0030 1.0803 -0.0005 -0.1627 -0.0094 377  THR   B CB  
5498  O  OG1 . THR   B 377 ? 0.9519 0.9084 0.9776 0.0069  -0.1670 -0.0111 377  THR   B OG1 
5499  C  CG2 . THR   B 377 ? 1.0196 0.9702 1.0653 -0.0055 -0.1665 -0.0134 377  THR   B CG2 
5500  N  N   . CYS   B 378 ? 1.0662 1.0358 1.0853 0.0038  -0.1507 0.0013  378  CYS   B N   
5501  C  CA  . CYS   B 378 ? 1.0055 0.9847 1.0195 0.0082  -0.1489 0.0034  378  CYS   B CA  
5502  C  C   . CYS   B 378 ? 0.9947 0.9806 1.0143 0.0082  -0.1511 0.0006  378  CYS   B C   
5503  O  O   . CYS   B 378 ? 0.9943 0.9859 1.0242 0.0026  -0.1498 -0.0003 378  CYS   B O   
5504  C  CB  . CYS   B 378 ? 0.9668 0.9535 0.9822 0.0053  -0.1431 0.0074  378  CYS   B CB  
5505  S  SG  . CYS   B 378 ? 1.0663 1.0453 1.0728 0.0067  -0.1405 0.0110  378  CYS   B SG  
5506  N  N   . SER   B 379 ? 0.9795 0.9645 0.9923 0.0147  -0.1544 -0.0008 379  SER   B N   
5507  C  CA  . SER   B 379 ? 0.9313 0.9204 0.9482 0.0152  -0.1572 -0.0039 379  SER   B CA  
5508  C  C   . SER   B 379 ? 0.9697 0.9668 0.9812 0.0203  -0.1554 -0.0021 379  SER   B C   
5509  O  O   . SER   B 379 ? 0.9514 0.9471 0.9535 0.0262  -0.1545 0.0001  379  SER   B O   
5510  C  CB  . SER   B 379 ? 0.9531 0.9316 0.9678 0.0177  -0.1637 -0.0082 379  SER   B CB  
5511  O  OG  . SER   B 379 ? 0.9694 0.9460 0.9956 0.0113  -0.1658 -0.0112 379  SER   B OG  
5512  N  N   . GLY   B 380 ? 0.9592 0.9648 0.9774 0.0181  -0.1547 -0.0031 380  GLY   B N   
5513  C  CA  . GLY   B 380 ? 0.9277 0.9407 0.9421 0.0225  -0.1531 -0.0019 380  GLY   B CA  
5514  C  C   . GLY   B 380 ? 0.9012 0.9231 0.9149 0.0225  -0.1476 0.0026  380  GLY   B C   
5515  O  O   . GLY   B 380 ? 0.9976 1.0205 1.0136 0.0187  -0.1450 0.0048  380  GLY   B O   
5516  N  N   . ALA   B 381 ? 0.8904 0.9182 0.9004 0.0271  -0.1460 0.0040  381  ALA   B N   
5517  C  CA  . ALA   B 381 ? 0.8720 0.9089 0.8821 0.0274  -0.1413 0.0080  381  ALA   B CA  
5518  C  C   . ALA   B 381 ? 0.8502 0.8885 0.8530 0.0349  -0.1403 0.0094  381  ALA   B C   
5519  O  O   . ALA   B 381 ? 0.8536 0.8879 0.8520 0.0392  -0.1424 0.0074  381  ALA   B O   
5520  C  CB  . ALA   B 381 ? 0.8461 0.8935 0.8652 0.0219  -0.1386 0.0085  381  ALA   B CB  
5521  N  N   . PHE   B 382 ? 0.8555 0.8994 0.8571 0.0366  -0.1370 0.0130  382  PHE   B N   
5522  C  CA  . PHE   B 382 ? 0.9418 0.9895 0.9388 0.0432  -0.1348 0.0151  382  PHE   B CA  
5523  C  C   . PHE   B 382 ? 0.9663 1.0032 0.9533 0.0500  -0.1373 0.0139  382  PHE   B C   
5524  O  O   . PHE   B 382 ? 0.9257 0.9542 0.9086 0.0504  -0.1396 0.0133  382  PHE   B O   
5525  C  CB  . PHE   B 382 ? 0.8780 0.9341 0.8794 0.0429  -0.1327 0.0151  382  PHE   B CB  
5526  C  CG  . PHE   B 382 ? 0.8811 0.9461 0.8921 0.0356  -0.1310 0.0155  382  PHE   B CG  
5527  C  CD1 . PHE   B 382 ? 0.9198 0.9920 0.9346 0.0332  -0.1283 0.0184  382  PHE   B CD1 
5528  C  CD2 . PHE   B 382 ? 0.8331 0.8986 0.8488 0.0316  -0.1323 0.0129  382  PHE   B CD2 
5529  C  CE1 . PHE   B 382 ? 0.9304 1.0097 0.9529 0.0269  -0.1269 0.0187  382  PHE   B CE1 
5530  C  CE2 . PHE   B 382 ? 0.8907 0.9639 0.9148 0.0252  -0.1306 0.0133  382  PHE   B CE2 
5531  C  CZ  . PHE   B 382 ? 0.8912 0.9709 0.9182 0.0229  -0.1278 0.0162  382  PHE   B CZ  
5532  N  N   . LYS   B 383 ? 0.9601 0.9964 0.9424 0.0557  -0.1369 0.0135  383  LYS   B N   
5533  C  CA  . LYS   B 383 ? 0.9814 1.0072 0.9529 0.0630  -0.1389 0.0126  383  LYS   B CA  
5534  C  C   . LYS   B 383 ? 1.0119 1.0259 0.9804 0.0618  -0.1446 0.0085  383  LYS   B C   
5535  O  O   . LYS   B 383 ? 1.0924 1.0960 1.0523 0.0663  -0.1472 0.0076  383  LYS   B O   
5536  C  CB  . LYS   B 383 ? 1.0148 1.0419 0.9813 0.0696  -0.1366 0.0133  383  LYS   B CB  
5537  C  CG  . LYS   B 383 ? 1.0077 1.0340 0.9751 0.0687  -0.1382 0.0106  383  LYS   B CG  
5538  C  CD  . LYS   B 383 ? 1.0369 1.0698 1.0034 0.0729  -0.1334 0.0128  383  LYS   B CD  
5539  C  CE  . LYS   B 383 ? 1.0572 1.0803 1.0116 0.0815  -0.1340 0.0118  383  LYS   B CE  
5540  N  NZ  . LYS   B 383 ? 1.1025 1.1180 1.0538 0.0812  -0.1388 0.0076  383  LYS   B NZ  
5541  N  N   . GLU   B 384 ? 0.9639 0.9794 0.9397 0.0556  -0.1466 0.0060  384  GLU   B N   
5542  C  CA  . GLU   B 384 ? 0.9717 0.9766 0.9463 0.0542  -0.1522 0.0019  384  GLU   B CA  
5543  C  C   . GLU   B 384 ? 1.0103 1.0114 0.9885 0.0491  -0.1534 0.0019  384  GLU   B C   
5544  O  O   . GLU   B 384 ? 1.0731 1.0647 1.0507 0.0479  -0.1580 -0.0013 384  GLU   B O   
5545  C  CB  . GLU   B 384 ? 0.9916 0.9989 0.9729 0.0502  -0.1544 -0.0012 384  GLU   B CB  
5546  C  CG  . GLU   B 384 ? 1.0188 1.0304 0.9976 0.0542  -0.1528 -0.0012 384  GLU   B CG  
5547  C  CD  . GLU   B 384 ? 1.1233 1.1261 1.0891 0.0634  -0.1541 -0.0017 384  GLU   B CD  
5548  O  OE1 . GLU   B 384 ? 1.1208 1.1117 1.0796 0.0666  -0.1588 -0.0041 384  GLU   B OE1 
5549  O  OE2 . GLU   B 384 ? 1.1558 1.1636 1.1187 0.0675  -0.1502 0.0004  384  GLU   B OE2 
5550  N  N   . GLY   B 385 ? 0.9586 0.9665 0.9405 0.0461  -0.1494 0.0054  385  GLY   B N   
5551  C  CA  . GLY   B 385 ? 0.9664 0.9700 0.9509 0.0414  -0.1499 0.0057  385  GLY   B CA  
5552  C  C   . GLY   B 385 ? 1.0392 1.0293 1.0156 0.0449  -0.1536 0.0041  385  GLY   B C   
5553  O  O   . GLY   B 385 ? 1.0355 1.0208 1.0023 0.0522  -0.1544 0.0045  385  GLY   B O   
5554  N  N   . SER   B 386 ? 0.9868 0.9705 0.9671 0.0398  -0.1557 0.0025  386  SER   B N   
5555  C  CA  . SER   B 386 ? 0.9620 0.9321 0.9356 0.0424  -0.1598 0.0005  386  SER   B CA  
5556  C  C   . SER   B 386 ? 0.9961 0.9613 0.9757 0.0356  -0.1601 0.0002  386  SER   B C   
5557  O  O   . SER   B 386 ? 1.0043 0.9761 0.9937 0.0288  -0.1575 0.0007  386  SER   B O   
5558  C  CB  . SER   B 386 ? 1.0045 0.9676 0.9756 0.0453  -0.1654 -0.0039 386  SER   B CB  
5559  O  OG  . SER   B 386 ? 1.0144 0.9789 0.9965 0.0387  -0.1676 -0.0070 386  SER   B OG  
5560  N  N   . LEU   B 387 ? 0.9927 0.9458 0.9661 0.0377  -0.1629 -0.0008 387  LEU   B N   
5561  C  CA  . LEU   B 387 ? 0.9829 0.9282 0.9620 0.0318  -0.1647 -0.0026 387  LEU   B CA  
5562  C  C   . LEU   B 387 ? 0.9594 0.8967 0.9400 0.0322  -0.1712 -0.0077 387  LEU   B C   
5563  O  O   . LEU   B 387 ? 1.0413 0.9724 1.0124 0.0391  -0.1749 -0.0093 387  LEU   B O   
5564  C  CB  . LEU   B 387 ? 0.9455 0.8817 0.9169 0.0335  -0.1639 -0.0004 387  LEU   B CB  
5565  C  CG  . LEU   B 387 ? 0.9565 0.9010 0.9266 0.0333  -0.1580 0.0044  387  LEU   B CG  
5566  C  CD1 . LEU   B 387 ? 0.9640 0.9004 0.9261 0.0354  -0.1569 0.0067  387  LEU   B CD1 
5567  C  CD2 . LEU   B 387 ? 0.9676 0.9200 0.9493 0.0252  -0.1545 0.0052  387  LEU   B CD2 
5568  N  N   . ARG   B 388 ? 0.9796 0.9173 0.9721 0.0253  -0.1726 -0.0102 388  ARG   B N   
5569  C  CA  . ARG   B 388 ? 1.0691 0.9975 1.0641 0.0251  -0.1796 -0.0153 388  ARG   B CA  
5570  C  C   . ARG   B 388 ? 1.1068 1.0256 1.1064 0.0201  -0.1806 -0.0161 388  ARG   B C   
5571  O  O   . ARG   B 388 ? 1.0882 1.0106 1.0955 0.0138  -0.1757 -0.0137 388  ARG   B O   
5572  C  CB  . ARG   B 388 ? 1.0318 0.9675 1.0379 0.0214  -0.1815 -0.0184 388  ARG   B CB  
5573  C  CG  . ARG   B 388 ? 1.0095 0.9550 1.0120 0.0255  -0.1797 -0.0173 388  ARG   B CG  
5574  C  CD  . ARG   B 388 ? 1.0320 0.9705 1.0211 0.0346  -0.1840 -0.0190 388  ARG   B CD  
5575  N  NE  . ARG   B 388 ? 0.9654 0.9126 0.9492 0.0393  -0.1808 -0.0169 388  ARG   B NE  
5576  C  CZ  . ARG   B 388 ? 1.0477 0.9974 1.0313 0.0418  -0.1832 -0.0193 388  ARG   B CZ  
5577  N  NH1 . ARG   B 388 ? 1.0732 1.0177 1.0615 0.0403  -0.1894 -0.0241 388  ARG   B NH1 
5578  N  NH2 . ARG   B 388 ? 1.1135 1.0707 1.0920 0.0460  -0.1794 -0.0167 388  ARG   B NH2 
5579  N  N   . ILE   B 389 ? 1.1072 1.0131 1.1016 0.0232  -0.1867 -0.0194 389  ILE   B N   
5580  C  CA  . ILE   B 389 ? 1.1672 1.0628 1.1668 0.0183  -0.1884 -0.0207 389  ILE   B CA  
5581  C  C   . ILE   B 389 ? 1.1600 1.0508 1.1693 0.0155  -0.1955 -0.0265 389  ILE   B C   
5582  O  O   . ILE   B 389 ? 1.1600 1.0440 1.1624 0.0211  -0.2023 -0.0303 389  ILE   B O   
5583  C  CB  . ILE   B 389 ? 1.1390 1.0221 1.1251 0.0235  -0.1896 -0.0196 389  ILE   B CB  
5584  C  CG1 . ILE   B 389 ? 1.0933 0.9813 1.0701 0.0267  -0.1830 -0.0140 389  ILE   B CG1 
5585  C  CG2 . ILE   B 389 ? 1.1391 1.0120 1.1316 0.0177  -0.1905 -0.0206 389  ILE   B CG2 
5586  C  CD1 . ILE   B 389 ? 1.0768 0.9721 1.0446 0.0340  -0.1822 -0.0127 389  ILE   B CD1 
5587  N  N   . ILE   B 390 ? 1.1165 1.0106 1.1418 0.0070  -0.1940 -0.0274 390  ILE   B N   
5588  C  CA  . ILE   B 390 ? 1.1644 1.0571 1.2026 0.0033  -0.2002 -0.0328 390  ILE   B CA  
5589  C  C   . ILE   B 390 ? 1.2659 1.1482 1.3125 -0.0022 -0.2022 -0.0346 390  ILE   B C   
5590  O  O   . ILE   B 390 ? 1.2325 1.1169 1.2875 -0.0087 -0.1959 -0.0316 390  ILE   B O   
5591  C  CB  . ILE   B 390 ? 1.1879 1.0944 1.2398 -0.0022 -0.1968 -0.0325 390  ILE   B CB  
5592  C  CG1 . ILE   B 390 ? 1.1985 1.1147 1.2423 0.0033  -0.1954 -0.0311 390  ILE   B CG1 
5593  C  CG2 . ILE   B 390 ? 1.1304 1.0360 1.1978 -0.0067 -0.2029 -0.0381 390  ILE   B CG2 
5594  C  CD1 . ILE   B 390 ? 1.1288 1.0564 1.1737 0.0007  -0.1866 -0.0259 390  ILE   B CD1 
5595  N  N   . ARG   B 391 ? 1.3343 1.2048 1.3786 0.0006  -0.2109 -0.0395 391  ARG   B N   
5596  C  CA  . ARG   B 391 ? 1.3126 1.1721 1.3660 -0.0043 -0.2145 -0.0423 391  ARG   B CA  
5597  C  C   . ARG   B 391 ? 1.3597 1.2175 1.4251 -0.0060 -0.2235 -0.0490 391  ARG   B C   
5598  O  O   . ARG   B 391 ? 1.4029 1.2620 1.4624 -0.0004 -0.2291 -0.0520 391  ARG   B O   
5599  C  CB  . ARG   B 391 ? 1.3209 1.1654 1.3594 0.0008  -0.2175 -0.0422 391  ARG   B CB  
5600  C  CG  . ARG   B 391 ? 1.4210 1.2592 1.4424 0.0110  -0.2242 -0.0447 391  ARG   B CG  
5601  C  CD  . ARG   B 391 ? 1.4793 1.3000 1.4948 0.0137  -0.2322 -0.0487 391  ARG   B CD  
5602  N  NE  . ARG   B 391 ? 1.5827 1.3997 1.6158 0.0070  -0.2381 -0.0538 391  ARG   B NE  
5603  C  CZ  . ARG   B 391 ? 1.6903 1.4932 1.7250 0.0061  -0.2448 -0.0576 391  ARG   B CZ  
5604  N  NH1 . ARG   B 391 ? 1.7540 1.5439 1.7729 0.0116  -0.2467 -0.0570 391  ARG   B NH1 
5605  N  NH2 . ARG   B 391 ? 1.7075 1.5092 1.7608 -0.0006 -0.2499 -0.0622 391  ARG   B NH2 
5606  N  N   . ASN   B 392 ? 1.4293 1.2836 1.5115 -0.0137 -0.2248 -0.0513 392  ASN   B N   
5607  C  CA  . ASN   B 392 ? 1.4642 1.3155 1.5592 -0.0155 -0.2343 -0.0581 392  ASN   B CA  
5608  C  C   . ASN   B 392 ? 1.4884 1.3244 1.5713 -0.0088 -0.2445 -0.0627 392  ASN   B C   
5609  O  O   . ASN   B 392 ? 1.4803 1.3048 1.5676 -0.0114 -0.2485 -0.0651 392  ASN   B O   
5610  C  CB  . ASN   B 392 ? 1.4458 1.2975 1.5635 -0.0258 -0.2324 -0.0591 392  ASN   B CB  
5611  C  CG  . ASN   B 392 ? 1.4140 1.2810 1.5490 -0.0317 -0.2280 -0.0586 392  ASN   B CG  
5612  O  OD1 . ASN   B 392 ? 1.4269 1.3003 1.5649 -0.0295 -0.2329 -0.0620 392  ASN   B OD1 
5613  N  ND2 . ASN   B 392 ? 1.4073 1.2793 1.5530 -0.0390 -0.2185 -0.0543 392  ASN   B ND2 
5614  N  N   . LEU   B 406 ? 1.3732 1.2488 1.4561 0.0025  -0.2498 -0.0678 710  LEU   B N   
5615  C  CA  . LEU   B 406 ? 1.4024 1.2731 1.4762 0.0025  -0.2436 -0.0629 710  LEU   B CA  
5616  C  C   . LEU   B 406 ? 1.4004 1.2671 1.4507 0.0124  -0.2428 -0.0604 710  LEU   B C   
5617  O  O   . LEU   B 406 ? 1.3378 1.2104 1.3809 0.0174  -0.2427 -0.0603 710  LEU   B O   
5618  C  CB  . LEU   B 406 ? 1.3730 1.2552 1.4565 -0.0048 -0.2323 -0.0571 710  LEU   B CB  
5619  C  CG  . LEU   B 406 ? 1.2854 1.1794 1.3901 -0.0130 -0.2294 -0.0578 710  LEU   B CG  
5620  C  CD1 . LEU   B 406 ? 1.1819 1.0894 1.2839 -0.0114 -0.2242 -0.0549 710  LEU   B CD1 
5621  C  CD2 . LEU   B 406 ? 1.3091 1.2047 1.4270 -0.0217 -0.2221 -0.0546 710  LEU   B CD2 
5622  N  N   . HIS   B 407 ? 1.4230 1.2797 1.4617 0.0152  -0.2417 -0.0584 711  HIS   B N   
5623  C  CA  . HIS   B 407 ? 1.3971 1.2497 1.4142 0.0245  -0.2404 -0.0557 711  HIS   B CA  
5624  C  C   . HIS   B 407 ? 1.3829 1.2470 1.3962 0.0240  -0.2295 -0.0488 711  HIS   B C   
5625  O  O   . HIS   B 407 ? 1.3486 1.2177 1.3711 0.0171  -0.2230 -0.0454 711  HIS   B O   
5626  C  CB  . HIS   B 407 ? 1.4326 1.2690 1.4392 0.0280  -0.2447 -0.0569 711  HIS   B CB  
5627  C  CG  . HIS   B 407 ? 1.5706 1.4034 1.5569 0.0361  -0.2409 -0.0529 711  HIS   B CG  
5628  N  ND1 . HIS   B 407 ? 1.5815 1.4193 1.5554 0.0436  -0.2392 -0.0514 711  HIS   B ND1 
5629  C  CD2 . HIS   B 407 ? 1.6599 1.4846 1.6366 0.0381  -0.2383 -0.0500 711  HIS   B CD2 
5630  C  CE1 . HIS   B 407 ? 1.5561 1.3896 1.5146 0.0497  -0.2357 -0.0477 711  HIS   B CE1 
5631  N  NE2 . HIS   B 407 ? 1.6474 1.4730 1.6070 0.0466  -0.2352 -0.0469 711  HIS   B NE2 
5632  N  N   . ILE   B 408 ? 1.3754 1.2432 1.3749 0.0315  -0.2275 -0.0467 712  ILE   B N   
5633  C  CA  . ILE   B 408 ? 1.2896 1.1693 1.2858 0.0316  -0.2180 -0.0406 712  ILE   B CA  
5634  C  C   . ILE   B 408 ? 1.2617 1.1366 1.2388 0.0407  -0.2164 -0.0379 712  ILE   B C   
5635  O  O   . ILE   B 408 ? 1.2460 1.1151 1.2117 0.0484  -0.2211 -0.0403 712  ILE   B O   
5636  C  CB  . ILE   B 408 ? 1.2910 1.1841 1.2933 0.0307  -0.2158 -0.0404 712  ILE   B CB  
5637  C  CG1 . ILE   B 408 ? 1.2348 1.1354 1.2569 0.0212  -0.2150 -0.0418 712  ILE   B CG1 
5638  C  CG2 . ILE   B 408 ? 1.2679 1.1714 1.2636 0.0329  -0.2073 -0.0346 712  ILE   B CG2 
5639  C  CD1 . ILE   B 408 ? 1.2292 1.1358 1.2573 0.0215  -0.2188 -0.0453 712  ILE   B CD1 
5640  N  N   . ARG   B 409 ? 1.2443 1.1216 1.2179 0.0400  -0.2097 -0.0328 713  ARG   B N   
5641  C  CA  . ARG   B 409 ? 1.1733 1.0486 1.1309 0.0480  -0.2067 -0.0294 713  ARG   B CA  
5642  C  C   . ARG   B 409 ? 1.1667 1.0571 1.1263 0.0470  -0.1985 -0.0244 713  ARG   B C   
5643  O  O   . ARG   B 409 ? 1.1322 1.0297 1.1013 0.0402  -0.1935 -0.0216 713  ARG   B O   
5644  C  CB  . ARG   B 409 ? 1.1712 1.0361 1.1227 0.0484  -0.2062 -0.0278 713  ARG   B CB  
5645  C  CG  . ARG   B 409 ? 1.3440 1.2008 1.2774 0.0583  -0.2071 -0.0268 713  ARG   B CG  
5646  C  CD  . ARG   B 409 ? 1.3525 1.2109 1.2801 0.0595  -0.2007 -0.0214 713  ARG   B CD  
5647  N  NE  . ARG   B 409 ? 1.4712 1.3221 1.3820 0.0694  -0.2014 -0.0205 713  ARG   B NE  
5648  C  CZ  . ARG   B 409 ? 1.4587 1.3078 1.3614 0.0727  -0.1975 -0.0166 713  ARG   B CZ  
5649  N  NH1 . ARG   B 409 ? 1.3569 1.2104 1.2657 0.0671  -0.1927 -0.0133 713  ARG   B NH1 
5650  N  NH2 . ARG   B 409 ? 1.5243 1.3666 1.4121 0.0821  -0.1984 -0.0161 713  ARG   B NH2 
5651  N  N   . THR   B 410 ? 1.1764 1.0714 1.1273 0.0538  -0.1972 -0.0233 714  THR   B N   
5652  C  CA  . THR   B 410 ? 1.1569 1.0663 1.1101 0.0532  -0.1899 -0.0188 714  THR   B CA  
5653  C  C   . THR   B 410 ? 1.0819 0.9912 1.0239 0.0591  -0.1855 -0.0144 714  THR   B C   
5654  O  O   . THR   B 410 ? 1.1302 1.0322 1.0596 0.0672  -0.1875 -0.0149 714  THR   B O   
5655  C  CB  . THR   B 410 ? 1.1426 1.0592 1.0955 0.0562  -0.1902 -0.0199 714  THR   B CB  
5656  O  OG1 . THR   B 410 ? 1.2811 1.1906 1.2191 0.0659  -0.1920 -0.0203 714  THR   B OG1 
5657  C  CG2 . THR   B 410 ? 1.0673 0.9831 1.0300 0.0519  -0.1957 -0.0249 714  THR   B CG2 
5658  N  N   . VAL   B 411 ? 1.0911 1.0085 1.0376 0.0552  -0.1796 -0.0103 715  VAL   B N   
5659  C  CA  . VAL   B 411 ? 1.0959 1.0158 1.0338 0.0605  -0.1751 -0.0059 715  VAL   B CA  
5660  C  C   . VAL   B 411 ? 1.1156 1.0500 1.0563 0.0614  -0.1701 -0.0031 715  VAL   B C   
5661  O  O   . VAL   B 411 ? 1.1124 1.0571 1.0626 0.0554  -0.1662 -0.0010 715  VAL   B O   
5662  C  CB  . VAL   B 411 ? 1.0739 0.9923 1.0136 0.0565  -0.1722 -0.0031 715  VAL   B CB  
5663  C  CG1 . VAL   B 411 ? 1.1042 1.0233 1.0340 0.0630  -0.1688 0.0008  715  VAL   B CG1 
5664  C  CG2 . VAL   B 411 ? 1.0981 1.0028 1.0382 0.0535  -0.1768 -0.0061 715  VAL   B CG2 
5665  N  N   . PRO   B 412 ? 1.0677 1.0030 1.0005 0.0689  -0.1698 -0.0028 716  PRO   B N   
5666  C  CA  . PRO   B 412 ? 0.9955 0.9444 0.9317 0.0696  -0.1648 0.0000  716  PRO   B CA  
5667  C  C   . PRO   B 412 ? 1.0406 0.9970 0.9777 0.0694  -0.1595 0.0047  716  PRO   B C   
5668  O  O   . PRO   B 412 ? 1.1642 1.1148 1.0933 0.0740  -0.1592 0.0063  716  PRO   B O   
5669  C  CB  . PRO   B 412 ? 1.0054 0.9505 0.9310 0.0786  -0.1656 -0.0007 716  PRO   B CB  
5670  C  CG  . PRO   B 412 ? 1.2128 1.1445 1.1274 0.0840  -0.1687 -0.0016 716  PRO   B CG  
5671  C  CD  . PRO   B 412 ? 1.1895 1.1132 1.1087 0.0776  -0.1729 -0.0041 716  PRO   B CD  
5672  N  N   . LEU   B 413 ? 1.0927 1.0617 1.0393 0.0642  -0.1556 0.0067  717  LEU   B N   
5673  C  CA  . LEU   B 413 ? 1.0264 1.0030 0.9746 0.0636  -0.1512 0.0109  717  LEU   B CA  
5674  C  C   . LEU   B 413 ? 1.0059 0.9946 0.9557 0.0668  -0.1470 0.0136  717  LEU   B C   
5675  O  O   . LEU   B 413 ? 0.9929 0.9862 0.9414 0.0693  -0.1440 0.0169  717  LEU   B O   
5676  C  CB  . LEU   B 413 ? 1.0116 0.9922 0.9692 0.0549  -0.1500 0.0114  717  LEU   B CB  
5677  C  CG  . LEU   B 413 ? 0.9796 0.9484 0.9361 0.0516  -0.1530 0.0096  717  LEU   B CG  
5678  C  CD1 . LEU   B 413 ? 0.9890 0.9619 0.9549 0.0431  -0.1508 0.0103  717  LEU   B CD1 
5679  C  CD2 . LEU   B 413 ? 0.9922 0.9534 0.9389 0.0569  -0.1530 0.0114  717  LEU   B CD2 
5680  N  N   . TYR   B 414 ? 1.0022 0.9958 0.9549 0.0670  -0.1467 0.0123  718  TYR   B N   
5681  C  CA  . TYR   B 414 ? 1.0064 1.0115 0.9616 0.0696  -0.1424 0.0149  718  TYR   B CA  
5682  C  C   . TYR   B 414 ? 1.0011 1.0180 0.9651 0.0645  -0.1388 0.0178  718  TYR   B C   
5683  O  O   . TYR   B 414 ? 0.9643 0.9901 0.9301 0.0672  -0.1352 0.0206  718  TYR   B O   
5684  C  CB  . TYR   B 414 ? 1.0139 1.0168 0.9602 0.0787  -0.1406 0.0168  718  TYR   B CB  
5685  C  CG  . TYR   B 414 ? 1.0918 1.0815 1.0273 0.0847  -0.1441 0.0141  718  TYR   B CG  
5686  C  CD1 . TYR   B 414 ? 1.1298 1.1072 1.0597 0.0846  -0.1484 0.0121  718  TYR   B CD1 
5687  C  CD2 . TYR   B 414 ? 1.1292 1.1177 1.0593 0.0905  -0.1433 0.0136  718  TYR   B CD2 
5688  C  CE1 . TYR   B 414 ? 1.1475 1.1119 1.0671 0.0901  -0.1524 0.0093  718  TYR   B CE1 
5689  C  CE2 . TYR   B 414 ? 1.1291 1.1043 1.0480 0.0964  -0.1469 0.0109  718  TYR   B CE2 
5690  C  CZ  . TYR   B 414 ? 1.1952 1.1584 1.1089 0.0962  -0.1518 0.0086  718  TYR   B CZ  
5691  O  OH  . TYR   B 414 ? 1.2752 1.2245 1.1775 0.1021  -0.1560 0.0057  718  TYR   B OH  
5692  N  N   . GLU   B 415 ? 0.9619 0.9782 0.9312 0.0574  -0.1398 0.0172  719  GLU   B N   
5693  C  CA  . GLU   B 415 ? 0.9345 0.9608 0.9122 0.0516  -0.1371 0.0192  719  GLU   B CA  
5694  C  C   . GLU   B 415 ? 0.9315 0.9542 0.9143 0.0441  -0.1387 0.0171  719  GLU   B C   
5695  O  O   . GLU   B 415 ? 0.9315 0.9445 0.9120 0.0436  -0.1420 0.0143  719  GLU   B O   
5696  C  CB  . GLU   B 415 ? 0.9286 0.9573 0.9043 0.0535  -0.1352 0.0225  719  GLU   B CB  
5697  C  CG  . GLU   B 415 ? 0.9665 0.9842 0.9333 0.0575  -0.1370 0.0228  719  GLU   B CG  
5698  C  CD  . GLU   B 415 ? 1.0848 1.1062 1.0492 0.0611  -0.1351 0.0262  719  GLU   B CD  
5699  O  OE1 . GLU   B 415 ? 1.0789 1.0998 1.0444 0.0575  -0.1348 0.0274  719  GLU   B OE1 
5700  O  OE2 . GLU   B 415 ? 1.0856 1.1100 1.0471 0.0677  -0.1339 0.0276  719  GLU   B OE2 
5701  N  N   . SER   B 416 ? 0.9356 0.9662 0.9259 0.0383  -0.1364 0.0183  720  SER   B N   
5702  C  CA  . SER   B 416 ? 0.9508 0.9800 0.9476 0.0311  -0.1370 0.0165  720  SER   B CA  
5703  C  C   . SER   B 416 ? 0.9734 0.9947 0.9682 0.0283  -0.1372 0.0171  720  SER   B C   
5704  O  O   . SER   B 416 ? 0.9629 0.9868 0.9564 0.0279  -0.1349 0.0200  720  SER   B O   
5705  C  CB  . SER   B 416 ? 0.9376 0.9779 0.9425 0.0263  -0.1342 0.0174  720  SER   B CB  
5706  O  OG  . SER   B 416 ? 0.9832 1.0320 0.9889 0.0296  -0.1329 0.0182  720  SER   B OG  
5707  N  N   . PRO   B 417 ? 0.9727 0.9840 0.9670 0.0266  -0.1399 0.0146  721  PRO   B N   
5708  C  CA  . PRO   B 417 ? 0.9736 0.9777 0.9677 0.0227  -0.1392 0.0153  721  PRO   B CA  
5709  C  C   . PRO   B 417 ? 0.9068 0.9163 0.9099 0.0153  -0.1366 0.0156  721  PRO   B C   
5710  O  O   . PRO   B 417 ? 0.9760 0.9898 0.9864 0.0121  -0.1371 0.0134  721  PRO   B O   
5711  C  CB  . PRO   B 417 ? 1.0126 1.0049 1.0050 0.0230  -0.1433 0.0121  721  PRO   B CB  
5712  C  CG  . PRO   B 417 ? 1.0193 1.0131 1.0113 0.0267  -0.1464 0.0094  721  PRO   B CG  
5713  C  CD  . PRO   B 417 ? 0.9890 0.9957 0.9845 0.0271  -0.1436 0.0108  721  PRO   B CD  
5714  N  N   . ARG   B 418 ? 0.9683 0.9770 0.9704 0.0128  -0.1336 0.0182  722  ARG   B N   
5715  C  CA  . ARG   B 418 ? 0.9843 0.9970 0.9937 0.0061  -0.1305 0.0187  722  ARG   B CA  
5716  C  C   . ARG   B 418 ? 1.0174 1.0205 1.0277 0.0015  -0.1291 0.0188  722  ARG   B C   
5717  O  O   . ARG   B 418 ? 1.0710 1.0740 1.0897 -0.0041 -0.1282 0.0172  722  ARG   B O   
5718  C  CB  . ARG   B 418 ? 0.9626 0.9843 0.9709 0.0066  -0.1276 0.0218  722  ARG   B CB  
5719  C  CG  . ARG   B 418 ? 0.8864 0.9186 0.8959 0.0102  -0.1283 0.0217  722  ARG   B CG  
5720  C  CD  . ARG   B 418 ? 0.9495 0.9883 0.9675 0.0066  -0.1283 0.0195  722  ARG   B CD  
5721  N  NE  . ARG   B 418 ? 1.0622 1.1062 1.0862 0.0009  -0.1253 0.0203  722  ARG   B NE  
5722  C  CZ  . ARG   B 418 ? 1.0242 1.0709 1.0562 -0.0038 -0.1249 0.0183  722  ARG   B CZ  
5723  N  NH1 . ARG   B 418 ? 0.9337 0.9789 0.9690 -0.0035 -0.1277 0.0151  722  ARG   B NH1 
5724  N  NH2 . ARG   B 418 ? 1.0021 1.0527 1.0384 -0.0086 -0.1217 0.0193  722  ARG   B NH2 
5725  N  N   . LYS   B 419 ? 1.0258 1.0204 1.0282 0.0038  -0.1289 0.0206  723  LYS   B N   
5726  C  CA  . LYS   B 419 ? 1.0309 1.0154 1.0342 -0.0005 -0.1272 0.0208  723  LYS   B CA  
5727  C  C   . LYS   B 419 ? 1.0198 0.9926 1.0158 0.0031  -0.1300 0.0202  723  LYS   B C   
5728  O  O   . LYS   B 419 ? 1.0057 0.9779 0.9934 0.0094  -0.1319 0.0211  723  LYS   B O   
5729  C  CB  . LYS   B 419 ? 1.0493 1.0340 1.0500 -0.0029 -0.1225 0.0242  723  LYS   B CB  
5730  C  CG  . LYS   B 419 ? 1.0542 1.0503 1.0610 -0.0060 -0.1199 0.0248  723  LYS   B CG  
5731  C  CD  . LYS   B 419 ? 1.0645 1.0614 1.0823 -0.0128 -0.1180 0.0230  723  LYS   B CD  
5732  C  CE  . LYS   B 419 ? 1.0781 1.0873 1.1022 -0.0146 -0.1171 0.0226  723  LYS   B CE  
5733  N  NZ  . LYS   B 419 ? 1.1314 1.1412 1.1635 -0.0211 -0.1132 0.0225  723  LYS   B NZ  
5734  N  N   . ILE   B 420 ? 1.0458 1.0092 1.0455 -0.0008 -0.1303 0.0187  724  ILE   B N   
5735  C  CA  . ILE   B 420 ? 1.0650 1.0162 1.0583 0.0022  -0.1332 0.0177  724  ILE   B CA  
5736  C  C   . ILE   B 420 ? 1.0534 0.9937 1.0476 -0.0026 -0.1304 0.0187  724  ILE   B C   
5737  O  O   . ILE   B 420 ? 1.0870 1.0281 1.0906 -0.0090 -0.1274 0.0184  724  ILE   B O   
5738  C  CB  . ILE   B 420 ? 1.0325 0.9816 1.0293 0.0035  -0.1387 0.0134  724  ILE   B CB  
5739  C  CG1 . ILE   B 420 ? 1.0772 1.0126 1.0670 0.0064  -0.1418 0.0125  724  ILE   B CG1 
5740  C  CG2 . ILE   B 420 ? 0.9895 0.9410 0.9998 -0.0032 -0.1388 0.0107  724  ILE   B CG2 
5741  C  CD1 . ILE   B 420 ? 1.0560 0.9885 1.0443 0.0105  -0.1478 0.0087  724  ILE   B CD1 
5742  N  N   . CYS   B 421 ? 1.0846 1.0144 1.0691 0.0009  -0.1310 0.0200  725  CYS   B N   
5743  C  CA  . CYS   B 421 ? 1.1227 1.0407 1.1068 -0.0031 -0.1282 0.0212  725  CYS   B CA  
5744  C  C   . CYS   B 421 ? 1.0741 0.9798 1.0493 0.0013  -0.1317 0.0205  725  CYS   B C   
5745  O  O   . CYS   B 421 ? 1.0569 0.9633 1.0229 0.0082  -0.1345 0.0208  725  CYS   B O   
5746  C  CB  . CYS   B 421 ? 1.1112 1.0292 1.0900 -0.0040 -0.1224 0.0255  725  CYS   B CB  
5747  S  SG  . CYS   B 421 ? 1.2491 1.1626 1.2111 0.0043  -0.1234 0.0285  725  CYS   B SG  
5748  N  N   . TYR   B 422 ? 1.0891 0.9833 1.0672 -0.0027 -0.1311 0.0197  726  TYR   B N   
5749  C  CA  . TYR   B 422 ? 1.1875 1.0686 1.1580 0.0007  -0.1346 0.0187  726  TYR   B CA  
5750  C  C   . TYR   B 422 ? 1.2279 1.0986 1.1885 0.0014  -0.1305 0.0226  726  TYR   B C   
5751  O  O   . TYR   B 422 ? 1.2539 1.1214 1.2186 -0.0042 -0.1252 0.0245  726  TYR   B O   
5752  C  CB  . TYR   B 422 ? 1.1607 1.0352 1.1414 -0.0039 -0.1379 0.0147  726  TYR   B CB  
5753  C  CG  . TYR   B 422 ? 1.2481 1.1083 1.2216 -0.0008 -0.1418 0.0133  726  TYR   B CG  
5754  C  CD1 . TYR   B 422 ? 1.2672 1.1259 1.2312 0.0067  -0.1472 0.0117  726  TYR   B CD1 
5755  C  CD2 . TYR   B 422 ? 1.2954 1.1430 1.2711 -0.0053 -0.1398 0.0137  726  TYR   B CD2 
5756  C  CE1 . TYR   B 422 ? 1.2982 1.1430 1.2546 0.0098  -0.1510 0.0104  726  TYR   B CE1 
5757  C  CE2 . TYR   B 422 ? 1.3379 1.1717 1.3067 -0.0026 -0.1435 0.0124  726  TYR   B CE2 
5758  C  CZ  . TYR   B 422 ? 1.3380 1.1704 1.2969 0.0050  -0.1493 0.0107  726  TYR   B CZ  
5759  O  OH  . TYR   B 422 ? 1.3461 1.1641 1.2974 0.0080  -0.1531 0.0093  726  TYR   B OH  
5760  N  N   . GLN   B 423 ? 1.2772 1.1428 1.2245 0.0084  -0.1325 0.0239  727  GLN   B N   
5761  C  CA  . GLN   B 423 ? 1.3513 1.2052 1.2879 0.0099  -0.1294 0.0272  727  GLN   B CA  
5762  C  C   . GLN   B 423 ? 1.3682 1.2078 1.3004 0.0116  -0.1332 0.0252  727  GLN   B C   
5763  O  O   . GLN   B 423 ? 1.2694 1.1066 1.1927 0.0185  -0.1375 0.0243  727  GLN   B O   
5764  C  CB  . GLN   B 423 ? 1.3167 1.1754 1.2416 0.0167  -0.1287 0.0303  727  GLN   B CB  
5765  C  CG  . GLN   B 423 ? 1.3081 1.1547 1.2201 0.0195  -0.1263 0.0337  727  GLN   B CG  
5766  C  CD  . GLN   B 423 ? 1.2434 1.0969 1.1482 0.0233  -0.1240 0.0371  727  GLN   B CD  
5767  O  OE1 . GLN   B 423 ? 1.2363 1.0953 1.1451 0.0192  -0.1199 0.0387  727  GLN   B OE1 
5768  N  NE2 . GLN   B 423 ? 1.2328 1.0865 1.1273 0.0311  -0.1268 0.0380  727  GLN   B NE2 
5769  N  N   . GLU   B 424 ? 1.4321 1.2622 1.3712 0.0052  -0.1315 0.0244  728  GLU   B N   
5770  C  CA  . GLU   B 424 ? 1.4507 1.2675 1.3884 0.0056  -0.1356 0.0218  728  GLU   B CA  
5771  C  C   . GLU   B 424 ? 1.4834 1.2880 1.4050 0.0115  -0.1356 0.0242  728  GLU   B C   
5772  O  O   . GLU   B 424 ? 1.5110 1.3071 1.4264 0.0157  -0.1406 0.0222  728  GLU   B O   
5773  C  CB  . GLU   B 424 ? 1.5206 1.3305 1.4709 -0.0032 -0.1331 0.0206  728  GLU   B CB  
5774  C  CG  . GLU   B 424 ? 1.5916 1.3890 1.5437 -0.0037 -0.1384 0.0170  728  GLU   B CG  
5775  C  CD  . GLU   B 424 ? 1.6516 1.4408 1.6158 -0.0123 -0.1351 0.0165  728  GLU   B CD  
5776  O  OE1 . GLU   B 424 ? 1.7250 1.5102 1.6878 -0.0156 -0.1278 0.0205  728  GLU   B OE1 
5777  O  OE2 . GLU   B 424 ? 1.7606 1.5470 1.7356 -0.0157 -0.1398 0.0122  728  GLU   B OE2 
5778  N  N   . VAL   B 425 ? 1.4305 1.2337 1.3445 0.0122  -0.1302 0.0286  729  VAL   B N   
5779  C  CA  . VAL   B 425 ? 1.3584 1.1493 1.2569 0.0177  -0.1299 0.0311  729  VAL   B CA  
5780  C  C   . VAL   B 425 ? 1.3486 1.1419 1.2374 0.0267  -0.1355 0.0300  729  VAL   B C   
5781  O  O   . VAL   B 425 ? 1.4205 1.2018 1.3000 0.0310  -0.1383 0.0295  729  VAL   B O   
5782  C  CB  . VAL   B 425 ? 1.4525 1.2436 1.3442 0.0177  -0.1237 0.0358  729  VAL   B CB  
5783  C  CG1 . VAL   B 425 ? 1.4182 1.1925 1.2959 0.0207  -0.1220 0.0385  729  VAL   B CG1 
5784  C  CG2 . VAL   B 425 ? 1.4245 1.2193 1.3285 0.0090  -0.1180 0.0366  729  VAL   B CG2 
5785  N  N   . SER   B 426 ? 1.3844 1.1929 1.2753 0.0298  -0.1369 0.0297  730  SER   B N   
5786  C  CA  . SER   B 426 ? 1.3385 1.1510 1.2212 0.0385  -0.1412 0.0290  730  SER   B CA  
5787  C  C   . SER   B 426 ? 1.3729 1.1901 1.2619 0.0394  -0.1464 0.0247  730  SER   B C   
5788  O  O   . SER   B 426 ? 1.3797 1.2019 1.2632 0.0464  -0.1494 0.0241  730  SER   B O   
5789  C  CB  . SER   B 426 ? 1.3510 1.1767 1.2306 0.0424  -0.1391 0.0319  730  SER   B CB  
5790  O  OG  . SER   B 426 ? 1.3575 1.1946 1.2478 0.0365  -0.1359 0.0323  730  SER   B OG  
5791  N  N   . GLN   B 427 ? 1.4033 1.2189 1.3039 0.0325  -0.1474 0.0217  731  GLN   B N   
5792  C  CA  . GLN   B 427 ? 1.3416 1.1586 1.2474 0.0332  -0.1530 0.0172  731  GLN   B CA  
5793  C  C   . GLN   B 427 ? 1.3698 1.2025 1.2776 0.0370  -0.1541 0.0167  731  GLN   B C   
5794  O  O   . GLN   B 427 ? 1.3165 1.1494 1.2196 0.0429  -0.1585 0.0146  731  GLN   B O   
5795  C  CB  . GLN   B 427 ? 1.3392 1.1422 1.2347 0.0388  -0.1580 0.0153  731  GLN   B CB  
5796  N  N   . CYS   B 428 ? 1.3926 1.2378 1.3070 0.0336  -0.1499 0.0188  732  CYS   B N   
5797  C  CA  . CYS   B 428 ? 1.3586 1.2188 1.2755 0.0366  -0.1503 0.0187  732  CYS   B CA  
5798  C  C   . CYS   B 428 ? 1.3356 1.2074 1.2650 0.0296  -0.1470 0.0189  732  CYS   B C   
5799  O  O   . CYS   B 428 ? 1.3125 1.1814 1.2473 0.0231  -0.1434 0.0200  732  CYS   B O   
5800  C  CB  . CYS   B 428 ? 1.3456 1.2105 1.2524 0.0437  -0.1488 0.0221  732  CYS   B CB  
5801  S  SG  . CYS   B 428 ? 1.4565 1.3236 1.3630 0.0399  -0.1427 0.0265  732  CYS   B SG  
5802  N  N   . PHE   B 429 ? 1.3188 1.2036 1.2524 0.0313  -0.1478 0.0181  733  PHE   B N   
5803  C  CA  . PHE   B 429 ? 1.2314 1.1283 1.1757 0.0257  -0.1448 0.0184  733  PHE   B CA  
5804  C  C   . PHE   B 429 ? 1.1565 1.0646 1.0977 0.0287  -0.1418 0.0217  733  PHE   B C   
5805  O  O   . PHE   B 429 ? 1.0901 1.0020 1.0246 0.0357  -0.1433 0.0224  733  PHE   B O   
5806  C  CB  . PHE   B 429 ? 1.1138 1.0175 1.0666 0.0247  -0.1481 0.0147  733  PHE   B CB  
5807  C  CG  . PHE   B 429 ? 1.1186 1.0134 1.0773 0.0208  -0.1516 0.0109  733  PHE   B CG  
5808  C  CD1 . PHE   B 429 ? 1.1001 0.9960 1.0711 0.0127  -0.1497 0.0099  733  PHE   B CD1 
5809  C  CD2 . PHE   B 429 ? 1.1481 1.0336 1.1008 0.0255  -0.1571 0.0081  733  PHE   B CD2 
5810  C  CE1 . PHE   B 429 ? 1.1318 1.0201 1.1100 0.0090  -0.1533 0.0061  733  PHE   B CE1 
5811  C  CE2 . PHE   B 429 ? 1.1434 1.0207 1.1023 0.0220  -0.1611 0.0041  733  PHE   B CE2 
5812  C  CZ  . PHE   B 429 ? 1.1376 1.0166 1.1098 0.0137  -0.1594 0.0031  733  PHE   B CZ  
5813  N  N   . GLY   B 430 ? 1.1227 1.0363 1.0693 0.0235  -0.1375 0.0237  734  GLY   B N   
5814  C  CA  . GLY   B 430 ? 1.1280 1.0540 1.0746 0.0250  -0.1351 0.0261  734  GLY   B CA  
5815  C  C   . GLY   B 430 ? 1.0758 1.0146 1.0329 0.0220  -0.1352 0.0244  734  GLY   B C   
5816  O  O   . GLY   B 430 ? 1.0869 1.0268 1.0533 0.0156  -0.1340 0.0230  734  GLY   B O   
5817  N  N   . VAL   B 431 ? 1.0424 0.9910 0.9984 0.0268  -0.1363 0.0246  735  VAL   B N   
5818  C  CA  . VAL   B 431 ? 1.0448 1.0054 1.0098 0.0244  -0.1361 0.0232  735  VAL   B CA  
5819  C  C   . VAL   B 431 ? 1.0095 0.9818 0.9743 0.0263  -0.1339 0.0259  735  VAL   B C   
5820  O  O   . VAL   B 431 ? 1.0343 1.0077 0.9921 0.0323  -0.1343 0.0277  735  VAL   B O   
5821  C  CB  . VAL   B 431 ? 1.0444 1.0055 1.0101 0.0279  -0.1401 0.0201  735  VAL   B CB  
5822  C  CG1 . VAL   B 431 ? 1.0756 1.0497 1.0487 0.0268  -0.1395 0.0193  735  VAL   B CG1 
5823  C  CG2 . VAL   B 431 ? 1.0216 0.9726 0.9904 0.0246  -0.1428 0.0168  735  VAL   B CG2 
5824  N  N   . LEU   B 432 ? 1.0108 0.9913 0.9834 0.0212  -0.1315 0.0261  736  LEU   B N   
5825  C  CA  . LEU   B 432 ? 1.0008 0.9933 0.9750 0.0224  -0.1299 0.0280  736  LEU   B CA  
5826  C  C   . LEU   B 432 ? 0.9992 1.0009 0.9791 0.0236  -0.1313 0.0260  736  LEU   B C   
5827  O  O   . LEU   B 432 ? 1.0007 1.0028 0.9872 0.0197  -0.1319 0.0235  736  LEU   B O   
5828  C  CB  . LEU   B 432 ? 0.9518 0.9474 0.9301 0.0165  -0.1265 0.0293  736  LEU   B CB  
5829  C  CG  . LEU   B 432 ? 1.0375 1.0245 1.0101 0.0147  -0.1240 0.0317  736  LEU   B CG  
5830  C  CD1 . LEU   B 432 ? 1.0129 1.0039 0.9908 0.0087  -0.1205 0.0325  736  LEU   B CD1 
5831  C  CD2 . LEU   B 432 ? 1.0302 1.0164 0.9934 0.0207  -0.1246 0.0343  736  LEU   B CD2 
5832  N  N   . SER   B 433 ? 0.9911 0.9997 0.9686 0.0291  -0.1318 0.0272  737  SER   B N   
5833  C  CA  . SER   B 433 ? 1.0069 1.0226 0.9878 0.0316  -0.1329 0.0257  737  SER   B CA  
5834  C  C   . SER   B 433 ? 1.0173 1.0455 1.0011 0.0334  -0.1311 0.0277  737  SER   B C   
5835  O  O   . SER   B 433 ? 1.0080 1.0381 0.9887 0.0358  -0.1304 0.0301  737  SER   B O   
5836  C  CB  . SER   B 433 ? 0.9662 0.9754 0.9403 0.0382  -0.1354 0.0246  737  SER   B CB  
5837  O  OG  . SER   B 433 ? 0.9951 1.0081 0.9646 0.0443  -0.1348 0.0271  737  SER   B OG  
5838  N  N   . SER   B 434 ? 0.9913 1.0278 0.9813 0.0324  -0.1307 0.0265  738  SER   B N   
5839  C  CA  . SER   B 434 ? 1.0273 1.0756 1.0209 0.0342  -0.1291 0.0282  738  SER   B CA  
5840  C  C   . SER   B 434 ? 0.9980 1.0490 0.9907 0.0398  -0.1295 0.0277  738  SER   B C   
5841  O  O   . SER   B 434 ? 0.9662 1.0118 0.9573 0.0407  -0.1311 0.0253  738  SER   B O   
5842  C  CB  . SER   B 434 ? 0.9637 1.0203 0.9656 0.0280  -0.1274 0.0280  738  SER   B CB  
5843  O  OG  . SER   B 434 ? 1.0589 1.1188 1.0657 0.0265  -0.1276 0.0258  738  SER   B OG  
5844  N  N   . ARG   B 435 ? 0.9433 1.0020 0.9367 0.0440  -0.1282 0.0299  739  ARG   B N   
5845  C  CA  . ARG   B 435 ? 0.9537 1.0164 0.9468 0.0496  -0.1274 0.0301  739  ARG   B CA  
5846  C  C   . ARG   B 435 ? 1.0854 1.1611 1.0867 0.0482  -0.1250 0.0315  739  ARG   B C   
5847  O  O   . ARG   B 435 ? 1.0608 1.1423 1.0654 0.0466  -0.1244 0.0332  739  ARG   B O   
5848  C  CB  . ARG   B 435 ? 0.9351 0.9942 0.9216 0.0567  -0.1276 0.0317  739  ARG   B CB  
5849  C  CG  . ARG   B 435 ? 1.0051 1.0688 0.9914 0.0633  -0.1258 0.0327  739  ARG   B CG  
5850  C  CD  . ARG   B 435 ? 1.0766 1.1376 1.0573 0.0700  -0.1259 0.0346  739  ARG   B CD  
5851  N  NE  . ARG   B 435 ? 1.0963 1.1600 1.0786 0.0683  -0.1264 0.0363  739  ARG   B NE  
5852  C  CZ  . ARG   B 435 ? 1.1489 1.2080 1.1255 0.0727  -0.1274 0.0376  739  ARG   B CZ  
5853  N  NH1 . ARG   B 435 ? 1.1924 1.2440 1.1614 0.0790  -0.1278 0.0375  739  ARG   B NH1 
5854  N  NH2 . ARG   B 435 ? 1.0559 1.1174 1.0337 0.0711  -0.1282 0.0391  739  ARG   B NH2 
5855  N  N   . ILE   B 436 ? 1.0188 1.0985 1.0230 0.0489  -0.1238 0.0306  740  ILE   B N   
5856  C  CA  . ILE   B 436 ? 0.9391 1.0309 0.9510 0.0485  -0.1212 0.0320  740  ILE   B CA  
5857  C  C   . ILE   B 436 ? 0.9986 1.0943 1.0100 0.0553  -0.1195 0.0343  740  ILE   B C   
5858  O  O   . ILE   B 436 ? 1.0385 1.1290 1.0441 0.0609  -0.1191 0.0341  740  ILE   B O   
5859  C  CB  . ILE   B 436 ? 1.0105 1.1046 1.0255 0.0468  -0.1202 0.0304  740  ILE   B CB  
5860  C  CG1 . ILE   B 436 ? 1.0037 1.0942 1.0202 0.0402  -0.1219 0.0280  740  ILE   B CG1 
5861  C  CG2 . ILE   B 436 ? 0.9727 1.0788 0.9956 0.0463  -0.1172 0.0321  740  ILE   B CG2 
5862  C  CD1 . ILE   B 436 ? 0.9908 1.0885 1.0141 0.0343  -0.1211 0.0287  740  ILE   B CD1 
5863  N  N   . GLU   B 437 ? 1.0988 1.2036 1.1162 0.0549  -0.1185 0.0364  741  GLU   B N   
5864  C  CA  . GLU   B 437 ? 1.1557 1.2674 1.1763 0.0606  -0.1162 0.0386  741  GLU   B CA  
5865  C  C   . GLU   B 437 ? 1.1488 1.2730 1.1802 0.0575  -0.1140 0.0396  741  GLU   B C   
5866  O  O   . GLU   B 437 ? 1.1194 1.2464 1.1548 0.0513  -0.1148 0.0387  741  GLU   B O   
5867  C  CB  . GLU   B 437 ? 1.1722 1.2825 1.1900 0.0644  -0.1175 0.0403  741  GLU   B CB  
5868  C  CG  . GLU   B 437 ? 1.2188 1.3162 1.2253 0.0687  -0.1192 0.0395  741  GLU   B CG  
5869  C  CD  . GLU   B 437 ? 1.2668 1.3621 1.2696 0.0733  -0.1205 0.0411  741  GLU   B CD  
5870  O  OE1 . GLU   B 437 ? 1.2946 1.3976 1.3033 0.0724  -0.1209 0.0426  741  GLU   B OE1 
5871  O  OE2 . GLU   B 437 ? 1.2408 1.3264 1.2347 0.0779  -0.1214 0.0409  741  GLU   B OE2 
5872  N  N   . VAL   B 438 ? 1.2079 1.3393 1.2443 0.0619  -0.1111 0.0415  742  VAL   B N   
5873  C  CA  . VAL   B 438 ? 1.1385 1.2812 1.1855 0.0597  -0.1085 0.0425  742  VAL   B CA  
5874  C  C   . VAL   B 438 ? 1.1679 1.3199 1.2228 0.0628  -0.1075 0.0449  742  VAL   B C   
5875  O  O   . VAL   B 438 ? 1.2387 1.3895 1.2914 0.0692  -0.1062 0.0462  742  VAL   B O   
5876  C  CB  . VAL   B 438 ? 1.0775 1.2196 1.1238 0.0621  -0.1048 0.0423  742  VAL   B CB  
5877  C  CG1 . VAL   B 438 ? 1.1003 1.2372 1.1402 0.0700  -0.1031 0.0434  742  VAL   B CG1 
5878  C  CG2 . VAL   B 438 ? 1.2534 1.4070 1.3107 0.0609  -0.1015 0.0439  742  VAL   B CG2 
5879  N  N   . GLN   B 439 ? 1.2041 1.3654 1.2686 0.0586  -0.1082 0.0453  743  GLN   B N   
5880  C  CA  . GLN   B 439 ? 1.2529 1.4235 1.3262 0.0610  -0.1083 0.0472  743  GLN   B CA  
5881  C  C   . GLN   B 439 ? 1.3212 1.4969 1.3996 0.0669  -0.1037 0.0492  743  GLN   B C   
5882  O  O   . GLN   B 439 ? 1.3237 1.5025 1.4060 0.0663  -0.0998 0.0495  743  GLN   B O   
5883  C  CB  . GLN   B 439 ? 1.2517 1.4316 1.3351 0.0553  -0.1095 0.0470  743  GLN   B CB  
5884  C  CG  . GLN   B 439 ? 1.3125 1.4877 1.3913 0.0492  -0.1130 0.0452  743  GLN   B CG  
5885  C  CD  . GLN   B 439 ? 1.3340 1.5076 1.4104 0.0493  -0.1173 0.0453  743  GLN   B CD  
5886  O  OE1 . GLN   B 439 ? 1.3240 1.4980 1.4000 0.0545  -0.1182 0.0465  743  GLN   B OE1 
5887  N  NE2 . GLN   B 439 ? 1.2177 1.3893 1.2922 0.0439  -0.1199 0.0441  743  GLN   B NE2 
5888  N  N   . ASP   B 440 ? 1.4589 1.6355 1.5377 0.0727  -0.1038 0.0507  744  ASP   B N   
5889  C  CA  . ASP   B 440 ? 1.4964 1.6760 1.5783 0.0793  -0.0990 0.0528  744  ASP   B CA  
5890  C  C   . ASP   B 440 ? 1.5191 1.7124 1.6167 0.0800  -0.0974 0.0547  744  ASP   B C   
5891  O  O   . ASP   B 440 ? 1.4516 1.6508 1.5559 0.0773  -0.1014 0.0544  744  ASP   B O   
5892  C  CB  . ASP   B 440 ? 1.5274 1.6989 1.5997 0.0862  -0.0997 0.0533  744  ASP   B CB  
5893  C  CG  . ASP   B 440 ? 1.6033 1.7750 1.6755 0.0937  -0.0940 0.0553  744  ASP   B CG  
5894  O  OD1 . ASP   B 440 ? 1.6059 1.7847 1.6866 0.0938  -0.0892 0.0566  744  ASP   B OD1 
5895  O  OD2 . ASP   B 440 ? 1.6266 1.7908 1.6900 0.0997  -0.0942 0.0556  744  ASP   B OD2 
5896  N  N   . THR   B 441 ? 1.6382 1.8359 1.7415 0.0840  -0.0915 0.0566  745  THR   B N   
5897  C  CA  . THR   B 441 ? 1.6225 1.8333 1.7420 0.0855  -0.0887 0.0588  745  THR   B CA  
5898  C  C   . THR   B 441 ? 1.5787 1.7930 1.7020 0.0906  -0.0908 0.0599  745  THR   B C   
5899  O  O   . THR   B 441 ? 1.5333 1.7591 1.6715 0.0914  -0.0898 0.0613  745  THR   B O   
5900  C  CB  . THR   B 441 ? 1.5582 1.7708 1.6809 0.0892  -0.0809 0.0608  745  THR   B CB  
5901  O  OG1 . THR   B 441 ? 1.5850 1.7910 1.6993 0.0972  -0.0782 0.0620  745  THR   B OG1 
5902  C  CG2 . THR   B 441 ? 1.4732 1.6800 1.5890 0.0853  -0.0789 0.0595  745  THR   B CG2 
5903  N  N   . SER   B 442 ? 1.5754 1.7800 1.6861 0.0941  -0.0937 0.0592  746  SER   B N   
5904  C  CA  . SER   B 442 ? 1.5680 1.7754 1.6817 0.0983  -0.0969 0.0599  746  SER   B CA  
5905  C  C   . SER   B 442 ? 1.5766 1.7864 1.6927 0.0933  -0.1039 0.0583  746  SER   B C   
5906  O  O   . SER   B 442 ? 1.6141 1.8275 1.7341 0.0963  -0.1073 0.0587  746  SER   B O   
5907  C  CB  . SER   B 442 ? 1.6068 1.8023 1.7055 0.1045  -0.0971 0.0600  746  SER   B CB  
5908  O  OG  . SER   B 442 ? 1.6431 1.8260 1.7270 0.1018  -0.0985 0.0580  746  SER   B OG  
5909  N  N   . GLY   B 443 ? 1.5059 1.7139 1.6198 0.0861  -0.1060 0.0566  747  GLY   B N   
5910  C  CA  . GLY   B 443 ? 1.5192 1.7281 1.6337 0.0817  -0.1123 0.0551  747  GLY   B CA  
5911  C  C   . GLY   B 443 ? 1.5877 1.7836 1.6862 0.0805  -0.1162 0.0536  747  GLY   B C   
5912  O  O   . GLY   B 443 ? 1.5603 1.7550 1.6570 0.0792  -0.1214 0.0528  747  GLY   B O   
5913  N  N   . GLY   B 444 ? 1.6010 1.7867 1.6880 0.0812  -0.1139 0.0531  748  GLY   B N   
5914  C  CA  . GLY   B 444 ? 1.5652 1.7383 1.6381 0.0793  -0.1170 0.0515  748  GLY   B CA  
5915  C  C   . GLY   B 444 ? 1.5603 1.7267 1.6267 0.0753  -0.1150 0.0501  748  GLY   B C   
5916  O  O   . GLY   B 444 ? 1.5242 1.6960 1.5969 0.0704  -0.1135 0.0496  748  GLY   B O   
5917  N  N   . THR   B 445 ? 1.4222 1.5767 1.4762 0.0772  -0.1152 0.0493  749  THR   B N   
5918  C  CA  . THR   B 445 ? 1.2911 1.4385 1.3389 0.0745  -0.1136 0.0478  749  THR   B CA  
5919  C  C   . THR   B 445 ? 1.2570 1.3952 1.2952 0.0806  -0.1120 0.0479  749  THR   B C   
5920  O  O   . THR   B 445 ? 1.3550 1.4877 1.3869 0.0851  -0.1136 0.0484  749  THR   B O   
5921  C  CB  . THR   B 445 ? 1.2657 1.4061 1.3076 0.0682  -0.1168 0.0459  749  THR   B CB  
5922  O  OG1 . THR   B 445 ? 1.3262 1.4574 1.3588 0.0701  -0.1197 0.0457  749  THR   B OG1 
5923  C  CG2 . THR   B 445 ? 1.2615 1.4101 1.3117 0.0624  -0.1182 0.0457  749  THR   B CG2 
5924  N  N   . THR   B 446 ? 1.2709 1.4070 1.3073 0.0808  -0.1091 0.0473  750  THR   B N   
5925  C  CA  . THR   B 446 ? 1.2011 1.3279 1.2279 0.0866  -0.1075 0.0470  750  THR   B CA  
5926  C  C   . THR   B 446 ? 1.1373 1.2531 1.1550 0.0829  -0.1098 0.0443  750  THR   B C   
5927  O  O   . THR   B 446 ? 1.1592 1.2770 1.1803 0.0767  -0.1103 0.0429  750  THR   B O   
5928  C  CB  . THR   B 446 ? 1.2219 1.3541 1.2533 0.0902  -0.1022 0.0484  750  THR   B CB  
5929  O  OG1 . THR   B 446 ? 1.3777 1.5172 1.4154 0.0957  -0.0997 0.0510  750  THR   B OG1 
5930  C  CG2 . THR   B 446 ? 1.1535 1.2748 1.1738 0.0940  -0.1009 0.0472  750  THR   B CG2 
5931  N  N   . ALA   B 447 ? 1.1604 1.2647 1.1672 0.0869  -0.1114 0.0434  751  ALA   B N   
5932  C  CA  . ALA   B 447 ? 1.1985 1.2924 1.1977 0.0839  -0.1136 0.0407  751  ALA   B CA  
5933  C  C   . ALA   B 447 ? 1.1500 1.2423 1.1472 0.0863  -0.1109 0.0399  751  ALA   B C   
5934  O  O   . ALA   B 447 ? 1.0708 1.1664 1.0688 0.0921  -0.1071 0.0417  751  ALA   B O   
5935  C  CB  . ALA   B 447 ? 1.1866 1.2678 1.1748 0.0868  -0.1167 0.0397  751  ALA   B CB  
5936  N  N   . LEU   B 448 ? 1.0753 1.1624 1.0700 0.0821  -0.1127 0.0373  752  LEU   B N   
5937  C  CA  . LEU   B 448 ? 1.0942 1.1792 1.0862 0.0846  -0.1106 0.0365  752  LEU   B CA  
5938  C  C   . LEU   B 448 ? 1.1151 1.1872 1.0947 0.0911  -0.1117 0.0353  752  LEU   B C   
5939  O  O   . LEU   B 448 ? 1.1764 1.2459 1.1518 0.0956  -0.1093 0.0351  752  LEU   B O   
5940  C  CB  . LEU   B 448 ? 1.1016 1.1871 1.0967 0.0778  -0.1121 0.0341  752  LEU   B CB  
5941  C  CG  . LEU   B 448 ? 1.0555 1.1540 1.0625 0.0725  -0.1100 0.0356  752  LEU   B CG  
5942  C  CD1 . LEU   B 448 ? 0.9878 1.0867 0.9978 0.0658  -0.1115 0.0332  752  LEU   B CD1 
5943  C  CD2 . LEU   B 448 ? 0.9939 1.1003 1.0055 0.0769  -0.1049 0.0381  752  LEU   B CD2 
5944  N  N   . ARG   B 449 ? 1.1436 1.2071 1.1166 0.0921  -0.1152 0.0344  753  ARG   B N   
5945  C  CA  . ARG   B 449 ? 1.0766 1.1268 1.0372 0.0982  -0.1170 0.0329  753  ARG   B CA  
5946  C  C   . ARG   B 449 ? 1.1274 1.1703 1.0833 0.0980  -0.1205 0.0325  753  ARG   B C   
5947  O  O   . ARG   B 449 ? 1.0861 1.1325 1.0475 0.0918  -0.1222 0.0325  753  ARG   B O   
5948  C  CB  . ARG   B 449 ? 1.0465 1.0885 1.0022 0.0965  -0.1197 0.0294  753  ARG   B CB  
5949  C  CG  . ARG   B 449 ? 1.0589 1.0959 1.0156 0.0895  -0.1246 0.0266  753  ARG   B CG  
5950  C  CD  . ARG   B 449 ? 1.1307 1.1651 1.0880 0.0860  -0.1266 0.0235  753  ARG   B CD  
5951  N  NE  . ARG   B 449 ? 1.1207 1.1666 1.0893 0.0791  -0.1248 0.0241  753  ARG   B NE  
5952  C  CZ  . ARG   B 449 ? 1.0848 1.1354 1.0565 0.0784  -0.1230 0.0237  753  ARG   B CZ  
5953  N  NH1 . ARG   B 449 ? 0.9926 1.0370 0.9567 0.0841  -0.1226 0.0226  753  ARG   B NH1 
5954  N  NH2 . ARG   B 449 ? 1.1802 1.2411 1.1620 0.0721  -0.1214 0.0243  753  ARG   B NH2 
5955  N  N   . PRO   B 450 ? 1.1462 1.1786 1.0914 0.1047  -0.1216 0.0322  754  PRO   B N   
5956  C  CA  . PRO   B 450 ? 1.1189 1.1423 1.0583 0.1046  -0.1253 0.0315  754  PRO   B CA  
5957  C  C   . PRO   B 450 ? 1.0713 1.0885 1.0111 0.0973  -0.1296 0.0283  754  PRO   B C   
5958  O  O   . PRO   B 450 ? 1.0934 1.1098 1.0346 0.0945  -0.1306 0.0261  754  PRO   B O   
5959  C  CB  . PRO   B 450 ? 1.1765 1.1885 1.1035 0.1134  -0.1257 0.0310  754  PRO   B CB  
5960  C  CG  . PRO   B 450 ? 1.1776 1.1882 1.1019 0.1159  -0.1243 0.0297  754  PRO   B CG  
5961  C  CD  . PRO   B 450 ? 1.1034 1.1288 1.0397 0.1121  -0.1202 0.0316  754  PRO   B CD  
5962  N  N   . SER   B 451 ? 1.0565 1.0688 0.9949 0.0945  -0.1321 0.0282  755  SER   B N   
5963  C  CA  . SER   B 451 ? 1.0843 1.0909 1.0243 0.0873  -0.1356 0.0254  755  SER   B CA  
5964  C  C   . SER   B 451 ? 1.1137 1.1147 1.0514 0.0853  -0.1373 0.0261  755  SER   B C   
5965  O  O   . SER   B 451 ? 1.1774 1.1792 1.1120 0.0896  -0.1360 0.0285  755  SER   B O   
5966  C  CB  . SER   B 451 ? 1.0707 1.0878 1.0215 0.0800  -0.1343 0.0252  755  SER   B CB  
5967  O  OG  . SER   B 451 ? 1.1594 1.1878 1.1169 0.0787  -0.1313 0.0283  755  SER   B OG  
5968  N  N   . ALA   B 452 ? 1.0545 1.0499 0.9940 0.0787  -0.1398 0.0240  756  ALA   B N   
5969  C  CA  . ALA   B 452 ? 1.0804 1.0675 1.0160 0.0771  -0.1413 0.0244  756  ALA   B CA  
5970  C  C   . ALA   B 452 ? 1.1392 1.1320 1.0747 0.0793  -0.1391 0.0279  756  ALA   B C   
5971  O  O   . ALA   B 452 ? 1.2420 1.2294 1.1699 0.0856  -0.1394 0.0291  756  ALA   B O   
5972  C  CB  . ALA   B 452 ? 1.0244 1.0094 0.9658 0.0684  -0.1425 0.0228  756  ALA   B CB  
5973  N  N   . SER   B 453 ? 1.1008 1.1038 1.0443 0.0744  -0.1371 0.0295  757  SER   B N   
5974  C  CA  . SER   B 453 ? 1.1270 1.1360 1.0710 0.0767  -0.1355 0.0326  757  SER   B CA  
5975  C  C   . SER   B 453 ? 1.1588 1.1710 1.0996 0.0854  -0.1344 0.0342  757  SER   B C   
5976  O  O   . SER   B 453 ? 1.1990 1.2069 1.1338 0.0902  -0.1348 0.0357  757  SER   B O   
5977  C  CB  . SER   B 453 ? 1.1700 1.1916 1.1239 0.0713  -0.1336 0.0337  757  SER   B CB  
5978  O  OG  . SER   B 453 ? 1.1162 1.1444 1.0769 0.0683  -0.1326 0.0323  757  SER   B OG  
5979  N  N   . THR   B 454 ? 1.1980 1.2171 1.1425 0.0876  -0.1326 0.0340  758  THR   B N   
5980  C  CA  . THR   B 454 ? 1.2031 1.2255 1.1454 0.0958  -0.1305 0.0357  758  THR   B CA  
5981  C  C   . THR   B 454 ? 1.1986 1.2084 1.1293 0.1024  -0.1322 0.0354  758  THR   B C   
5982  O  O   . THR   B 454 ? 1.2139 1.2247 1.1418 0.1084  -0.1312 0.0375  758  THR   B O   
5983  C  CB  . THR   B 454 ? 1.1661 1.1932 1.1112 0.0972  -0.1285 0.0349  758  THR   B CB  
5984  O  OG1 . THR   B 454 ? 1.2235 1.2610 1.1789 0.0906  -0.1272 0.0349  758  THR   B OG1 
5985  C  CG2 . THR   B 454 ? 1.1665 1.1988 1.1112 0.1053  -0.1252 0.0372  758  THR   B CG2 
5986  N  N   . GLN   B 455 ? 1.2381 1.2362 1.1621 0.1018  -0.1348 0.0326  759  GLN   B N   
5987  C  CA  . GLN   B 455 ? 1.2762 1.2619 1.1887 0.1086  -0.1364 0.0321  759  GLN   B CA  
5988  C  C   . GLN   B 455 ? 1.2944 1.2675 1.2013 0.1051  -0.1400 0.0306  759  GLN   B C   
5989  O  O   . GLN   B 455 ? 1.3695 1.3316 1.2710 0.1046  -0.1429 0.0278  759  GLN   B O   
5990  C  CB  . GLN   B 455 ? 1.2732 1.2536 1.1805 0.1127  -0.1367 0.0301  759  GLN   B CB  
5991  C  CG  . GLN   B 455 ? 1.2972 1.2735 1.2067 0.1063  -0.1395 0.0267  759  GLN   B CG  
5992  C  CD  . GLN   B 455 ? 1.3482 1.3244 1.2558 0.1095  -0.1389 0.0251  759  GLN   B CD  
5993  O  OE1 . GLN   B 455 ? 1.3562 1.3341 1.2598 0.1169  -0.1361 0.0267  759  GLN   B OE1 
5994  N  NE2 . GLN   B 455 ? 1.3249 1.2992 1.2356 0.1041  -0.1413 0.0221  759  GLN   B NE2 
5995  N  N   . ALA   B 456 ? 1.2492 1.2237 1.1575 0.1027  -0.1399 0.0324  760  ALA   B N   
5996  C  CA  . ALA   B 456 ? 1.2406 1.2022 1.1425 0.1005  -0.1426 0.0316  760  ALA   B CA  
5997  C  C   . ALA   B 456 ? 1.2943 1.2505 1.1876 0.1077  -0.1427 0.0335  760  ALA   B C   
5998  O  O   . ALA   B 456 ? 1.3498 1.3153 1.2457 0.1114  -0.1406 0.0361  760  ALA   B O   
5999  C  CB  . ALA   B 456 ? 1.2149 1.1792 1.1230 0.0922  -0.1423 0.0320  760  ALA   B CB  
6000  N  N   . LEU   B 457 ? 1.2888 1.2300 1.1723 0.1096  -0.1454 0.0322  761  LEU   B N   
6001  C  CA  . LEU   B 457 ? 1.2429 1.1774 1.1170 0.1169  -0.1457 0.0338  761  LEU   B CA  
6002  C  C   . LEU   B 457 ? 1.2809 1.2235 1.1584 0.1170  -0.1440 0.0369  761  LEU   B C   
6003  O  O   . LEU   B 457 ? 1.3722 1.3222 1.2502 0.1233  -0.1424 0.0390  761  LEU   B O   
6004  C  CB  . LEU   B 457 ? 1.2952 1.2121 1.1598 0.1163  -0.1489 0.0320  761  LEU   B CB  
6005  C  CG  . LEU   B 457 ? 1.4264 1.3357 1.2890 0.1155  -0.1514 0.0285  761  LEU   B CG  
6006  C  CD1 . LEU   B 457 ? 1.3841 1.2766 1.2401 0.1128  -0.1550 0.0261  761  LEU   B CD1 
6007  C  CD2 . LEU   B 457 ? 1.3356 1.2451 1.1924 0.1244  -0.1509 0.0283  761  LEU   B CD2 
6008  N  N   . SER   B 458 ? 1.2584 1.2000 1.1386 0.1102  -0.1444 0.0372  762  SER   B N   
6009  C  CA  . SER   B 458 ? 1.2695 1.2183 1.1525 0.1099  -0.1433 0.0399  762  SER   B CA  
6010  C  C   . SER   B 458 ? 1.2699 1.2306 1.1641 0.1025  -0.1418 0.0400  762  SER   B C   
6011  O  O   . SER   B 458 ? 1.2382 1.1977 1.1365 0.0960  -0.1418 0.0381  762  SER   B O   
6012  C  CB  . SER   B 458 ? 1.3049 1.2410 1.1792 0.1092  -0.1446 0.0406  762  SER   B CB  
6013  O  OG  . SER   B 458 ? 1.3755 1.3062 1.2518 0.1007  -0.1447 0.0395  762  SER   B OG  
6014  N  N   . SER   B 459 ? 1.2284 1.2004 1.1278 0.1037  -0.1407 0.0422  763  SER   B N   
6015  C  CA  . SER   B 459 ? 1.2014 1.1851 1.1110 0.0976  -0.1394 0.0425  763  SER   B CA  
6016  C  C   . SER   B 459 ? 1.1863 1.1718 1.0950 0.0975  -0.1399 0.0446  763  SER   B C   
6017  O  O   . SER   B 459 ? 1.2853 1.2665 1.1873 0.1033  -0.1410 0.0460  763  SER   B O   
6018  C  CB  . SER   B 459 ? 1.2585 1.2565 1.1771 0.0998  -0.1377 0.0428  763  SER   B CB  
6019  O  OG  . SER   B 459 ? 1.2774 1.2786 1.1942 0.1080  -0.1376 0.0445  763  SER   B OG  
6020  N  N   . SER   B 460 ? 1.2414 1.2332 1.1564 0.0912  -0.1392 0.0448  764  SER   B N   
6021  C  CA  . SER   B 460 ? 1.1856 1.1803 1.1002 0.0911  -0.1399 0.0466  764  SER   B CA  
6022  C  C   . SER   B 460 ? 1.2105 1.2177 1.1355 0.0857  -0.1389 0.0465  764  SER   B C   
6023  O  O   . SER   B 460 ? 1.2101 1.2205 1.1411 0.0806  -0.1375 0.0450  764  SER   B O   
6024  C  CB  . SER   B 460 ? 1.2179 1.1985 1.1229 0.0885  -0.1403 0.0470  764  SER   B CB  
6025  O  OG  . SER   B 460 ? 1.1991 1.1768 1.1069 0.0804  -0.1388 0.0458  764  SER   B OG  
6026  N  N   . VAL   B 461 ? 1.2351 1.2490 1.1622 0.0871  -0.1400 0.0480  765  VAL   B N   
6027  C  CA  . VAL   B 461 ? 1.2439 1.2697 1.1806 0.0827  -0.1396 0.0480  765  VAL   B CA  
6028  C  C   . VAL   B 461 ? 1.2897 1.3118 1.2217 0.0808  -0.1409 0.0490  765  VAL   B C   
6029  O  O   . VAL   B 461 ? 1.3720 1.3909 1.2981 0.0859  -0.1430 0.0503  765  VAL   B O   
6030  C  CB  . VAL   B 461 ? 1.2360 1.2766 1.1825 0.0868  -0.1398 0.0485  765  VAL   B CB  
6031  C  CG1 . VAL   B 461 ? 1.2461 1.2982 1.2024 0.0818  -0.1396 0.0484  765  VAL   B CG1 
6032  C  CG2 . VAL   B 461 ? 1.2105 1.2535 1.1601 0.0893  -0.1380 0.0477  765  VAL   B CG2 
6033  N  N   . SER   B 462 ? 1.3037 1.3258 1.2379 0.0738  -0.1396 0.0485  766  SER   B N   
6034  C  CA  . SER   B 462 ? 1.3417 1.3582 1.2698 0.0718  -0.1403 0.0494  766  SER   B CA  
6035  C  C   . SER   B 462 ? 1.3859 1.4107 1.3161 0.0761  -0.1433 0.0504  766  SER   B C   
6036  O  O   . SER   B 462 ? 1.3191 1.3572 1.2594 0.0779  -0.1442 0.0502  766  SER   B O   
6037  C  CB  . SER   B 462 ? 1.2791 1.2963 1.2108 0.0638  -0.1380 0.0487  766  SER   B CB  
6038  O  OG  . SER   B 462 ? 1.2492 1.2533 1.1712 0.0613  -0.1369 0.0495  766  SER   B OG  
6039  N  N   . SER   B 463 ? 1.5937 1.6102 1.5144 0.0780  -0.1450 0.0516  767  SER   B N   
6040  C  CA  . SER   B 463 ? 1.6768 1.6988 1.5976 0.0829  -0.1488 0.0523  767  SER   B CA  
6041  C  C   . SER   B 463 ? 1.7326 1.7470 1.6451 0.0803  -0.1495 0.0529  767  SER   B C   
6042  O  O   . SER   B 463 ? 1.8250 1.8269 1.7251 0.0831  -0.1503 0.0540  767  SER   B O   
6043  C  CB  . SER   B 463 ? 1.7622 1.7798 1.6769 0.0909  -0.1510 0.0532  767  SER   B CB  
6044  O  OG  . SER   B 463 ? 1.8514 1.8682 1.7614 0.0953  -0.1549 0.0541  767  SER   B OG  
6045  N  N   . SER   B 464 ? 1.6152 1.6366 1.5342 0.0751  -0.1489 0.0523  768  SER   B N   
6046  C  CA  . SER   B 464 ? 1.6769 1.6900 1.5877 0.0717  -0.1484 0.0528  768  SER   B CA  
6047  C  C   . SER   B 464 ? 1.7634 1.7819 1.6744 0.0741  -0.1527 0.0528  768  SER   B C   
6048  O  O   . SER   B 464 ? 1.7823 1.7905 1.6813 0.0763  -0.1543 0.0537  768  SER   B O   
6049  C  CB  . SER   B 464 ? 1.5901 1.6042 1.5058 0.0636  -0.1442 0.0519  768  SER   B CB  
6050  O  OG  . SER   B 464 ? 1.5398 1.5397 1.4447 0.0605  -0.1413 0.0528  768  SER   B OG  
6051  N  N   . LYS   B 465 ? 1.7600 1.7939 1.6841 0.0739  -0.1548 0.0518  769  LYS   B N   
6052  C  CA  . LYS   B 465 ? 1.7836 1.8236 1.7097 0.0754  -0.1594 0.0514  769  LYS   B CA  
6053  C  C   . LYS   B 465 ? 1.8132 1.8464 1.7323 0.0707  -0.1584 0.0514  769  LYS   B C   
6054  O  O   . LYS   B 465 ? 1.8263 1.8605 1.7431 0.0725  -0.1625 0.0511  769  LYS   B O   
6055  C  CB  . LYS   B 465 ? 1.7228 1.7592 1.6422 0.0833  -0.1644 0.0521  769  LYS   B CB  
6056  N  N   . LEU   B 466 ? 1.7708 1.7967 1.6865 0.0650  -0.1530 0.0516  770  LEU   B N   
6057  C  CA  . LEU   B 466 ? 1.7435 1.7629 1.6528 0.0606  -0.1513 0.0517  770  LEU   B CA  
6058  C  C   . LEU   B 466 ? 1.7443 1.7763 1.6647 0.0568  -0.1523 0.0503  770  LEU   B C   
6059  O  O   . LEU   B 466 ? 1.7109 1.7392 1.6262 0.0546  -0.1525 0.0503  770  LEU   B O   
6060  C  CB  . LEU   B 466 ? 1.6843 1.6934 1.5890 0.0554  -0.1450 0.0524  770  LEU   B CB  
6061  C  CG  . LEU   B 466 ? 1.7261 1.7179 1.6151 0.0583  -0.1437 0.0541  770  LEU   B CG  
6062  C  CD1 . LEU   B 466 ? 1.7751 1.7594 1.6520 0.0616  -0.1466 0.0549  770  LEU   B CD1 
6063  C  CD2 . LEU   B 466 ? 1.7471 1.7376 1.6349 0.0639  -0.1456 0.0544  770  LEU   B CD2 
6064  N  N   . PHE   B 467 ? 1.7986 1.8448 1.7335 0.0562  -0.1529 0.0493  771  PHE   B N   
6065  C  CA  . PHE   B 467 ? 1.8110 1.8696 1.7575 0.0525  -0.1535 0.0480  771  PHE   B CA  
6066  C  C   . PHE   B 467 ? 1.8884 1.9610 1.8469 0.0564  -0.1577 0.0474  771  PHE   B C   
6067  O  O   . PHE   B 467 ? 1.8944 1.9675 1.8531 0.0616  -0.1592 0.0479  771  PHE   B O   
6068  C  CB  . PHE   B 467 ? 1.6595 1.7207 1.6125 0.0461  -0.1481 0.0475  771  PHE   B CB  
6069  C  CG  . PHE   B 467 ? 1.6095 1.6567 1.5521 0.0427  -0.1436 0.0482  771  PHE   B CG  
6070  C  CD1 . PHE   B 467 ? 1.5933 1.6323 1.5273 0.0402  -0.1424 0.0486  771  PHE   B CD1 
6071  C  CD2 . PHE   B 467 ? 1.5512 1.5930 1.4927 0.0423  -0.1403 0.0485  771  PHE   B CD2 
6072  C  CE1 . PHE   B 467 ? 1.4808 1.5071 1.4062 0.0371  -0.1376 0.0496  771  PHE   B CE1 
6073  C  CE2 . PHE   B 467 ? 1.4856 1.5149 1.4191 0.0390  -0.1361 0.0492  771  PHE   B CE2 
6074  C  CZ  . PHE   B 467 ? 1.4102 1.4320 1.3361 0.0363  -0.1344 0.0498  771  PHE   B CZ  
6075  N  N   . SER   B 468 ? 2.1181 2.2019 2.0869 0.0540  -0.1595 0.0462  772  SER   B N   
6076  C  CA  . SER   B 468 ? 2.1176 2.2153 2.0995 0.0572  -0.1633 0.0456  772  SER   B CA  
6077  C  C   . SER   B 468 ? 2.1268 2.2371 2.1235 0.0538  -0.1602 0.0450  772  SER   B C   
6078  O  O   . SER   B 468 ? 2.1851 2.3048 2.1918 0.0571  -0.1609 0.0452  772  SER   B O   
6079  C  CB  . SER   B 468 ? 2.1154 2.2167 2.0985 0.0580  -0.1690 0.0446  772  SER   B CB  
6080  O  OG  . SER   B 468 ? 2.1411 2.2356 2.1150 0.0641  -0.1738 0.0450  772  SER   B OG  
6081  N  N   . SER   B 469 ? 1.9344 2.0450 1.9328 0.0476  -0.1567 0.0444  773  SER   B N   
6082  C  CA  . SER   B 469 ? 1.7987 1.9200 1.8099 0.0443  -0.1536 0.0439  773  SER   B CA  
6083  C  C   . SER   B 469 ? 1.7787 1.8945 1.7868 0.0433  -0.1487 0.0443  773  SER   B C   
6084  O  O   . SER   B 469 ? 1.7611 1.8651 1.7580 0.0443  -0.1477 0.0450  773  SER   B O   
6085  C  CB  . SER   B 469 ? 1.7482 1.8734 1.7635 0.0384  -0.1530 0.0428  773  SER   B CB  
6086  O  OG  . SER   B 469 ? 1.8245 1.9541 1.8424 0.0394  -0.1581 0.0421  773  SER   B OG  
6087  N  N   . HIS   B 474 ? 1.1993 1.4186 1.3250 0.0419  -0.1435 0.0443  778  HIS   B N   
6088  C  CA  . HIS   B 474 ? 1.2951 1.5151 1.4221 0.0450  -0.1379 0.0457  778  HIS   B CA  
6089  C  C   . HIS   B 474 ? 1.3980 1.6251 1.5347 0.0419  -0.1329 0.0461  778  HIS   B C   
6090  O  O   . HIS   B 474 ? 1.3861 1.6159 1.5267 0.0448  -0.1281 0.0474  778  HIS   B O   
6091  C  CB  . HIS   B 474 ? 1.1631 1.3881 1.2963 0.0516  -0.1386 0.0471  778  HIS   B CB  
6092  N  N   . GLU   B 475 ? 1.4186 1.6481 1.5586 0.0362  -0.1341 0.0448  779  GLU   B N   
6093  C  CA  . GLU   B 475 ? 1.3875 1.6217 1.5344 0.0327  -0.1293 0.0450  779  GLU   B CA  
6094  C  C   . GLU   B 475 ? 1.4447 1.6690 1.5790 0.0297  -0.1269 0.0442  779  GLU   B C   
6095  O  O   . GLU   B 475 ? 1.4022 1.6241 1.5335 0.0246  -0.1280 0.0428  779  GLU   B O   
6096  C  CB  . GLU   B 475 ? 1.3376 1.5800 1.4957 0.0284  -0.1318 0.0441  779  GLU   B CB  
6097  N  N   . THR   B 476 ? 1.4826 1.7009 1.6096 0.0332  -0.1237 0.0449  780  THR   B N   
6098  C  CA  . THR   B 476 ? 1.4741 1.6835 1.5906 0.0310  -0.1213 0.0441  780  THR   B CA  
6099  C  C   . THR   B 476 ? 1.4720 1.6846 1.5932 0.0309  -0.1159 0.0446  780  THR   B C   
6100  O  O   . THR   B 476 ? 1.5503 1.7683 1.6784 0.0269  -0.1147 0.0443  780  THR   B O   
6101  C  CB  . THR   B 476 ? 1.4579 1.6571 1.5622 0.0345  -0.1219 0.0441  780  THR   B CB  
6102  O  OG1 . THR   B 476 ? 1.4818 1.6758 1.5809 0.0356  -0.1180 0.0441  780  THR   B OG1 
6103  C  CG2 . THR   B 476 ? 1.3849 1.5863 1.4911 0.0405  -0.1236 0.0455  780  THR   B CG2 
6104  N  N   . SER   B 477 ? 1.4216 1.6303 1.5384 0.0354  -0.1126 0.0455  781  SER   B N   
6105  C  CA  . SER   B 477 ? 1.3747 1.5858 1.4950 0.0361  -0.1073 0.0462  781  SER   B CA  
6106  C  C   . SER   B 477 ? 1.2915 1.4969 1.4051 0.0421  -0.1043 0.0471  781  SER   B C   
6107  O  O   . SER   B 477 ? 1.3804 1.5760 1.4826 0.0430  -0.1057 0.0460  781  SER   B O   
6108  C  CB  . SER   B 477 ? 1.4311 1.6386 1.5477 0.0310  -0.1063 0.0446  781  SER   B CB  
6109  O  OG  . SER   B 477 ? 1.5597 1.7738 1.6843 0.0259  -0.1074 0.0441  781  SER   B OG  
6110  N  N   . PHE   B 478 ? 1.2493 1.4599 1.3694 0.0462  -0.1000 0.0490  782  PHE   B N   
6111  C  CA  . PHE   B 478 ? 1.2760 1.4799 1.3882 0.0521  -0.0968 0.0497  782  PHE   B CA  
6112  C  C   . PHE   B 478 ? 1.2894 1.4848 1.3920 0.0503  -0.0956 0.0481  782  PHE   B C   
6113  O  O   . PHE   B 478 ? 1.2778 1.4757 1.3838 0.0462  -0.0942 0.0475  782  PHE   B O   
6114  C  CB  . PHE   B 478 ? 1.1680 1.3790 1.2891 0.0568  -0.0915 0.0522  782  PHE   B CB  
6115  C  CG  . PHE   B 478 ? 1.1806 1.3997 1.3114 0.0592  -0.0928 0.0537  782  PHE   B CG  
6116  C  CD1 . PHE   B 478 ? 1.2285 1.4437 1.3538 0.0645  -0.0946 0.0541  782  PHE   B CD1 
6117  C  CD2 . PHE   B 478 ? 1.2516 1.4823 1.3975 0.0563  -0.0928 0.0544  782  PHE   B CD2 
6118  C  CE1 . PHE   B 478 ? 1.2821 1.5048 1.4165 0.0671  -0.0962 0.0553  782  PHE   B CE1 
6119  C  CE2 . PHE   B 478 ? 1.2713 1.5098 1.4271 0.0587  -0.0948 0.0554  782  PHE   B CE2 
6120  C  CZ  . PHE   B 478 ? 1.2553 1.4899 1.4054 0.0642  -0.0964 0.0559  782  PHE   B CZ  
6121  N  N   . GLY   B 479 ? 1.3984 1.5834 1.4891 0.0533  -0.0968 0.0472  783  GLY   B N   
6122  C  CA  . GLY   B 479 ? 1.4381 1.6144 1.5198 0.0520  -0.0965 0.0454  783  GLY   B CA  
6123  C  C   . GLY   B 479 ? 1.4375 1.6088 1.5145 0.0462  -0.1008 0.0430  783  GLY   B C   
6124  O  O   . GLY   B 479 ? 1.4563 1.6186 1.5246 0.0461  -0.1018 0.0412  783  GLY   B O   
6125  N  N   . GLU   B 480 ? 1.3728 1.5495 1.4556 0.0416  -0.1035 0.0428  784  GLU   B N   
6126  C  CA  . GLU   B 480 ? 1.3555 1.5267 1.4331 0.0368  -0.1071 0.0409  784  GLU   B CA  
6127  C  C   . GLU   B 480 ? 1.3224 1.4836 1.3900 0.0399  -0.1092 0.0404  784  GLU   B C   
6128  O  O   . GLU   B 480 ? 1.3139 1.4750 1.3804 0.0448  -0.1094 0.0418  784  GLU   B O   
6129  C  CB  . GLU   B 480 ? 1.4222 1.5993 1.5057 0.0330  -0.1098 0.0412  784  GLU   B CB  
6130  C  CG  . GLU   B 480 ? 1.5104 1.6957 1.6028 0.0285  -0.1087 0.0411  784  GLU   B CG  
6131  C  CD  . GLU   B 480 ? 1.5452 1.7339 1.6409 0.0242  -0.1121 0.0407  784  GLU   B CD  
6132  O  OE1 . GLU   B 480 ? 1.5384 1.7327 1.6404 0.0200  -0.1117 0.0403  784  GLU   B OE1 
6133  O  OE2 . GLU   B 480 ? 1.5461 1.7313 1.6374 0.0253  -0.1151 0.0408  784  GLU   B OE2 
6134  N  N   . GLU   B 481 ? 1.1559 1.3089 1.2168 0.0370  -0.1107 0.0384  785  GLU   B N   
6135  C  CA  . GLU   B 481 ? 1.0862 1.2291 1.1378 0.0397  -0.1126 0.0377  785  GLU   B CA  
6136  C  C   . GLU   B 481 ? 1.0283 1.1679 1.0774 0.0368  -0.1156 0.0375  785  GLU   B C   
6137  O  O   . GLU   B 481 ? 0.9895 1.1321 1.0419 0.0316  -0.1164 0.0372  785  GLU   B O   
6138  C  CB  . GLU   B 481 ? 1.1221 1.2566 1.1677 0.0392  -0.1126 0.0355  785  GLU   B CB  
6139  C  CG  . GLU   B 481 ? 1.1555 1.2922 1.2048 0.0340  -0.1120 0.0340  785  GLU   B CG  
6140  C  CD  . GLU   B 481 ? 1.1656 1.2937 1.2089 0.0345  -0.1128 0.0316  785  GLU   B CD  
6141  O  OE1 . GLU   B 481 ? 1.2441 1.3675 1.2860 0.0300  -0.1148 0.0297  785  GLU   B OE1 
6142  O  OE2 . GLU   B 481 ? 1.0916 1.2173 1.1316 0.0394  -0.1114 0.0316  785  GLU   B OE2 
6143  N  N   . VAL   B 482 ? 1.0536 1.1861 1.0957 0.0405  -0.1171 0.0379  786  VAL   B N   
6144  C  CA  . VAL   B 482 ? 0.9479 1.0750 0.9854 0.0386  -0.1196 0.0379  786  VAL   B CA  
6145  C  C   . VAL   B 482 ? 0.9549 1.0699 0.9834 0.0397  -0.1207 0.0367  786  VAL   B C   
6146  O  O   . VAL   B 482 ? 1.0194 1.1303 1.0440 0.0443  -0.1202 0.0364  786  VAL   B O   
6147  C  CB  . VAL   B 482 ? 0.9305 1.0613 0.9691 0.0424  -0.1208 0.0398  786  VAL   B CB  
6148  C  CG1 . VAL   B 482 ? 0.9846 1.1117 1.0198 0.0393  -0.1232 0.0399  786  VAL   B CG1 
6149  C  CG2 . VAL   B 482 ? 1.0651 1.2083 1.1139 0.0432  -0.1194 0.0410  786  VAL   B CG2 
6150  N  N   . GLU   B 483 ? 0.9069 1.0157 0.9319 0.0355  -0.1221 0.0359  787  GLU   B N   
6151  C  CA  . GLU   B 483 ? 0.9042 1.0011 0.9214 0.0358  -0.1233 0.0349  787  GLU   B CA  
6152  C  C   . GLU   B 483 ? 1.0141 1.1060 1.0252 0.0393  -0.1247 0.0364  787  GLU   B C   
6153  O  O   . GLU   B 483 ? 1.0371 1.1320 1.0491 0.0383  -0.1253 0.0377  787  GLU   B O   
6154  C  CB  . GLU   B 483 ? 0.8714 0.9641 0.8890 0.0291  -0.1234 0.0334  787  GLU   B CB  
6155  C  CG  . GLU   B 483 ? 0.9166 1.0113 0.9387 0.0259  -0.1225 0.0314  787  GLU   B CG  
6156  C  CD  . GLU   B 483 ? 1.0390 1.1304 1.0626 0.0194  -0.1223 0.0301  787  GLU   B CD  
6157  O  OE1 . GLU   B 483 ? 0.9671 1.0512 0.9865 0.0178  -0.1227 0.0304  787  GLU   B OE1 
6158  O  OE2 . GLU   B 483 ? 1.2738 1.3700 1.3031 0.0159  -0.1214 0.0289  787  GLU   B OE2 
6159  N  N   . VAL   B 484 ? 0.9984 1.0818 1.0027 0.0436  -0.1256 0.0361  788  VAL   B N   
6160  C  CA  . VAL   B 484 ? 0.9485 1.0253 0.9457 0.0471  -0.1270 0.0374  788  VAL   B CA  
6161  C  C   . VAL   B 484 ? 0.9976 1.0616 0.9880 0.0447  -0.1279 0.0361  788  VAL   B C   
6162  O  O   . VAL   B 484 ? 1.0691 1.1264 1.0561 0.0463  -0.1285 0.0346  788  VAL   B O   
6163  C  CB  . VAL   B 484 ? 1.0042 1.0818 0.9989 0.0548  -0.1270 0.0385  788  VAL   B CB  
6164  C  CG1 . VAL   B 484 ? 1.0380 1.1118 1.0272 0.0585  -0.1285 0.0401  788  VAL   B CG1 
6165  C  CG2 . VAL   B 484 ? 0.9969 1.0870 1.0000 0.0568  -0.1253 0.0394  788  VAL   B CG2 
6166  N  N   . HIS   B 485 ? 1.0193 1.0792 1.0074 0.0410  -0.1281 0.0367  789  HIS   B N   
6167  C  CA  . HIS   B 485 ? 1.0640 1.1120 1.0470 0.0379  -0.1283 0.0358  789  HIS   B CA  
6168  C  C   . HIS   B 485 ? 1.0568 1.0946 1.0305 0.0427  -0.1296 0.0367  789  HIS   B C   
6169  O  O   . HIS   B 485 ? 1.0393 1.0780 1.0094 0.0463  -0.1302 0.0386  789  HIS   B O   
6170  C  CB  . HIS   B 485 ? 0.9948 1.0426 0.9792 0.0320  -0.1270 0.0363  789  HIS   B CB  
6171  C  CG  . HIS   B 485 ? 1.0042 1.0580 0.9965 0.0264  -0.1257 0.0348  789  HIS   B CG  
6172  N  ND1 . HIS   B 485 ? 1.0632 1.1124 1.0568 0.0204  -0.1242 0.0341  789  HIS   B ND1 
6173  C  CD2 . HIS   B 485 ? 1.0013 1.0648 1.0006 0.0261  -0.1253 0.0339  789  HIS   B CD2 
6174  C  CE1 . HIS   B 485 ? 1.0083 1.0645 1.0095 0.0167  -0.1233 0.0327  789  HIS   B CE1 
6175  N  NE2 . HIS   B 485 ? 0.9827 1.0474 0.9871 0.0201  -0.1241 0.0326  789  HIS   B NE2 
6176  N  N   . ASN   B 486 ? 1.0578 1.0856 1.0275 0.0429  -0.1304 0.0351  790  ASN   B N   
6177  C  CA  . ASN   B 486 ? 1.0143 1.0312 0.9747 0.0473  -0.1318 0.0357  790  ASN   B CA  
6178  C  C   . ASN   B 486 ? 1.0466 1.0509 1.0036 0.0431  -0.1318 0.0346  790  ASN   B C   
6179  O  O   . ASN   B 486 ? 0.9897 0.9931 0.9519 0.0380  -0.1314 0.0326  790  ASN   B O   
6180  C  CB  . ASN   B 486 ? 1.0398 1.0551 0.9974 0.0535  -0.1331 0.0348  790  ASN   B CB  
6181  C  CG  . ASN   B 486 ? 1.1105 1.1360 1.0701 0.0590  -0.1327 0.0363  790  ASN   B CG  
6182  O  OD1 . ASN   B 486 ? 1.0816 1.1054 1.0361 0.0644  -0.1334 0.0380  790  ASN   B OD1 
6183  N  ND2 . ASN   B 486 ? 1.1056 1.1418 1.0731 0.0578  -0.1315 0.0359  790  ASN   B ND2 
6184  N  N   . LEU   B 487 ? 1.0941 1.0885 1.0426 0.0455  -0.1323 0.0359  791  LEU   B N   
6185  C  CA  . LEU   B 487 ? 1.0199 1.0008 0.9642 0.0430  -0.1326 0.0349  791  LEU   B CA  
6186  C  C   . LEU   B 487 ? 1.0477 1.0221 0.9868 0.0485  -0.1351 0.0335  791  LEU   B C   
6187  O  O   . LEU   B 487 ? 1.0809 1.0546 1.0137 0.0550  -0.1360 0.0349  791  LEU   B O   
6188  C  CB  . LEU   B 487 ? 1.0398 1.0122 0.9769 0.0426  -0.1314 0.0371  791  LEU   B CB  
6189  C  CG  . LEU   B 487 ? 1.0606 1.0184 0.9937 0.0399  -0.1312 0.0362  791  LEU   B CG  
6190  C  CD1 . LEU   B 487 ? 0.9853 0.9433 0.9270 0.0342  -0.1312 0.0334  791  LEU   B CD1 
6191  C  CD2 . LEU   B 487 ? 1.0227 0.9737 0.9510 0.0371  -0.1285 0.0385  791  LEU   B CD2 
6192  N  N   . LEU   B 488 ? 1.0645 1.0345 1.0064 0.0461  -0.1363 0.0308  792  LEU   B N   
6193  C  CA  . LEU   B 488 ? 1.1115 1.0730 1.0475 0.0509  -0.1391 0.0291  792  LEU   B CA  
6194  C  C   . LEU   B 488 ? 1.1228 1.0694 1.0538 0.0488  -0.1400 0.0285  792  LEU   B C   
6195  O  O   . LEU   B 488 ? 1.1173 1.0607 1.0529 0.0421  -0.1387 0.0279  792  LEU   B O   
6196  C  CB  . LEU   B 488 ? 1.0331 0.9976 0.9742 0.0504  -0.1408 0.0261  792  LEU   B CB  
6197  C  CG  . LEU   B 488 ? 0.9740 0.9525 0.9204 0.0521  -0.1396 0.0267  792  LEU   B CG  
6198  C  CD1 . LEU   B 488 ? 0.9265 0.9073 0.8793 0.0489  -0.1407 0.0237  792  LEU   B CD1 
6199  C  CD2 . LEU   B 488 ? 1.0386 1.0183 0.9786 0.0606  -0.1401 0.0278  792  LEU   B CD2 
6200  N  N   . ILE   B 489 ? 1.1483 1.0858 1.0701 0.0547  -0.1420 0.0285  793  ILE   B N   
6201  C  CA  . ILE   B 489 ? 1.1476 1.0698 1.0635 0.0537  -0.1433 0.0277  793  ILE   B CA  
6202  C  C   . ILE   B 489 ? 1.1718 1.0875 1.0847 0.0575  -0.1471 0.0247  793  ILE   B C   
6203  O  O   . ILE   B 489 ? 1.1822 1.0966 1.0876 0.0650  -0.1485 0.0251  793  ILE   B O   
6204  C  CB  . ILE   B 489 ? 1.1536 1.0691 1.0597 0.0578  -0.1424 0.0307  793  ILE   B CB  
6205  C  CG1 . ILE   B 489 ? 1.1736 1.0937 1.0820 0.0536  -0.1390 0.0333  793  ILE   B CG1 
6206  C  CG2 . ILE   B 489 ? 1.1848 1.0839 1.0842 0.0575  -0.1439 0.0298  793  ILE   B CG2 
6207  C  CD1 . ILE   B 489 ? 1.1140 1.0321 1.0301 0.0449  -0.1371 0.0323  793  ILE   B CD1 
6208  N  N   . ILE   B 490 ? 1.1591 1.0708 1.0780 0.0525  -0.1489 0.0215  794  ILE   B N   
6209  C  CA  . ILE   B 490 ? 1.1662 1.0721 1.0827 0.0558  -0.1532 0.0181  794  ILE   B CA  
6210  C  C   . ILE   B 490 ? 1.2467 1.1365 1.1590 0.0545  -0.1559 0.0164  794  ILE   B C   
6211  O  O   . ILE   B 490 ? 1.2347 1.1201 1.1527 0.0475  -0.1547 0.0161  794  ILE   B O   
6212  C  CB  . ILE   B 490 ? 1.1427 1.0559 1.0693 0.0517  -0.1544 0.0152  794  ILE   B CB  
6213  C  CG1 . ILE   B 490 ? 1.1337 1.0628 1.0658 0.0515  -0.1511 0.0172  794  ILE   B CG1 
6214  C  CG2 . ILE   B 490 ? 1.1992 1.1060 1.1215 0.0565  -0.1592 0.0117  794  ILE   B CG2 
6215  C  CD1 . ILE   B 490 ? 1.1195 1.0556 1.0635 0.0437  -0.1500 0.0159  794  ILE   B CD1 
6216  N  N   . ASP   B 491 ? 1.2449 1.1256 1.1476 0.0612  -0.1593 0.0151  795  ASP   B N   
6217  C  CA  . ASP   B 491 ? 1.2304 1.0950 1.1283 0.0606  -0.1624 0.0132  795  ASP   B CA  
6218  C  C   . ASP   B 491 ? 1.2306 1.0913 1.1374 0.0547  -0.1657 0.0090  795  ASP   B C   
6219  O  O   . ASP   B 491 ? 1.2149 1.0812 1.1257 0.0554  -0.1681 0.0064  795  ASP   B O   
6220  C  CB  . ASP   B 491 ? 1.2802 1.1358 1.1651 0.0696  -0.1655 0.0127  795  ASP   B CB  
6221  C  CG  . ASP   B 491 ? 1.3382 1.1764 1.2184 0.0689  -0.1694 0.0101  795  ASP   B CG  
6222  O  OD1 . ASP   B 491 ? 1.3478 1.1785 1.2266 0.0658  -0.1676 0.0118  795  ASP   B OD1 
6223  O  OD2 . ASP   B 491 ? 1.2848 1.1163 1.1626 0.0715  -0.1744 0.0064  795  ASP   B OD2 
6224  N  N   . GLN   B 492 ? 1.2768 1.1273 1.1866 0.0490  -0.1660 0.0083  796  GLN   B N   
6225  C  CA  . GLN   B 492 ? 1.2922 1.1397 1.2127 0.0425  -0.1691 0.0043  796  GLN   B CA  
6226  C  C   . GLN   B 492 ? 1.2388 1.0761 1.1549 0.0465  -0.1760 -0.0001 796  GLN   B C   
6227  O  O   . GLN   B 492 ? 1.2239 1.0602 1.1492 0.0423  -0.1796 -0.0040 796  GLN   B O   
6228  C  CB  . GLN   B 492 ? 1.2822 1.1224 1.2087 0.0350  -0.1666 0.0052  796  GLN   B CB  
6229  C  CG  . GLN   B 492 ? 1.2437 1.0674 1.1615 0.0370  -0.1686 0.0049  796  GLN   B CG  
6230  C  CD  . GLN   B 492 ? 1.3211 1.1370 1.2472 0.0287  -0.1666 0.0048  796  GLN   B CD  
6231  O  OE1 . GLN   B 492 ? 1.3384 1.1609 1.2724 0.0228  -0.1613 0.0072  796  GLN   B OE1 
6232  N  NE2 . GLN   B 492 ? 1.4138 1.2153 1.3384 0.0282  -0.1707 0.0021  796  GLN   B NE2 
6233  N  N   . HIS   B 493 ? 1.2296 1.0592 1.1319 0.0548  -0.1781 0.0002  797  HIS   B N   
6234  C  CA  . HIS   B 493 ? 1.3073 1.1260 1.2034 0.0594  -0.1849 -0.0040 797  HIS   B CA  
6235  C  C   . HIS   B 493 ? 1.2983 1.1233 1.1879 0.0672  -0.1863 -0.0047 797  HIS   B C   
6236  O  O   . HIS   B 493 ? 1.3162 1.1407 1.2086 0.0676  -0.1908 -0.0086 797  HIS   B O   
6237  C  CB  . HIS   B 493 ? 1.3196 1.1222 1.2040 0.0632  -0.1867 -0.0037 797  HIS   B CB  
6238  C  CG  . HIS   B 493 ? 1.3215 1.1170 1.2110 0.0560  -0.1845 -0.0026 797  HIS   B CG  
6239  N  ND1 . HIS   B 493 ? 1.3439 1.1386 1.2281 0.0564  -0.1793 0.0020  797  HIS   B ND1 
6240  C  CD2 . HIS   B 493 ? 1.3062 1.0942 1.2054 0.0486  -0.1867 -0.0053 797  HIS   B CD2 
6241  C  CE1 . HIS   B 493 ? 1.3582 1.1448 1.2479 0.0495  -0.1779 0.0022  797  HIS   B CE1 
6242  N  NE2 . HIS   B 493 ? 1.3802 1.1630 1.2797 0.0445  -0.1822 -0.0021 797  HIS   B NE2 
6243  N  N   . THR   B 494 ? 1.2778 1.1084 1.1589 0.0737  -0.1826 -0.0010 798  THR   B N   
6244  C  CA  . THR   B 494 ? 1.2750 1.1120 1.1504 0.0812  -0.1828 -0.0011 798  THR   B CA  
6245  C  C   . THR   B 494 ? 1.3194 1.1731 1.2054 0.0776  -0.1795 -0.0001 798  THR   B C   
6246  O  O   . THR   B 494 ? 1.3792 1.2382 1.2629 0.0824  -0.1800 -0.0009 798  THR   B O   
6247  C  CB  . THR   B 494 ? 1.2998 1.1373 1.1635 0.0896  -0.1798 0.0026  798  THR   B CB  
6248  O  OG1 . THR   B 494 ? 1.2708 1.1126 1.1367 0.0866  -0.1751 0.0066  798  THR   B OG1 
6249  C  CG2 . THR   B 494 ? 1.3774 1.1987 1.2273 0.0968  -0.1841 0.0008  798  THR   B CG2 
6250  N  N   . PHE   B 495 ? 1.3045 1.1658 1.2014 0.0696  -0.1760 0.0016  799  PHE   B N   
6251  C  CA  . PHE   B 495 ? 1.2628 1.1400 1.1693 0.0662  -0.1724 0.0029  799  PHE   B CA  
6252  C  C   . PHE   B 495 ? 1.2968 1.1830 1.1972 0.0733  -0.1691 0.0060  799  PHE   B C   
6253  O  O   . PHE   B 495 ? 1.3251 1.2209 1.2285 0.0748  -0.1682 0.0058  799  PHE   B O   
6254  C  CB  . PHE   B 495 ? 1.1574 1.0366 1.0715 0.0632  -0.1760 -0.0012 799  PHE   B CB  
6255  C  CG  . PHE   B 495 ? 1.1599 1.0369 1.0856 0.0540  -0.1770 -0.0031 799  PHE   B CG  
6256  C  CD1 . PHE   B 495 ? 1.2385 1.1248 1.1739 0.0471  -0.1720 -0.0005 799  PHE   B CD1 
6257  C  CD2 . PHE   B 495 ? 1.1552 1.0205 1.0821 0.0524  -0.1828 -0.0075 799  PHE   B CD2 
6258  C  CE1 . PHE   B 495 ? 1.2497 1.1340 1.1964 0.0386  -0.1721 -0.0020 799  PHE   B CE1 
6259  C  CE2 . PHE   B 495 ? 1.2145 1.0782 1.1537 0.0437  -0.1834 -0.0092 799  PHE   B CE2 
6260  C  CZ  . PHE   B 495 ? 1.2594 1.1327 1.2087 0.0368  -0.1777 -0.0063 799  PHE   B CZ  
6261  N  N   . GLU   B 496 ? 1.3402 1.2230 1.2322 0.0779  -0.1672 0.0090  800  GLU   B N   
6262  C  CA  . GLU   B 496 ? 1.3472 1.2389 1.2348 0.0844  -0.1638 0.0122  800  GLU   B CA  
6263  C  C   . GLU   B 496 ? 1.3446 1.2474 1.2387 0.0804  -0.1591 0.0160  800  GLU   B C   
6264  O  O   . GLU   B 496 ? 1.3520 1.2517 1.2496 0.0743  -0.1583 0.0166  800  GLU   B O   
6265  C  CB  . GLU   B 496 ? 1.4023 1.2837 1.2764 0.0930  -0.1650 0.0130  800  GLU   B CB  
6266  C  CG  . GLU   B 496 ? 1.5120 1.4021 1.3820 0.1007  -0.1617 0.0160  800  GLU   B CG  
6267  C  CD  . GLU   B 496 ? 1.6001 1.4794 1.4566 0.1097  -0.1629 0.0166  800  GLU   B CD  
6268  O  OE1 . GLU   B 496 ? 1.6615 1.5462 1.5139 0.1171  -0.1606 0.0183  800  GLU   B OE1 
6269  O  OE2 . GLU   B 496 ? 1.5757 1.4412 1.4258 0.1094  -0.1658 0.0153  800  GLU   B OE2 
6270  N  N   . VAL   B 497 ? 1.2657 1.1810 1.1615 0.0838  -0.1559 0.0184  801  VAL   B N   
6271  C  CA  . VAL   B 497 ? 1.2577 1.1841 1.1596 0.0804  -0.1520 0.0216  801  VAL   B CA  
6272  C  C   . VAL   B 497 ? 1.2559 1.1784 1.1496 0.0857  -0.1510 0.0245  801  VAL   B C   
6273  O  O   . VAL   B 497 ? 1.2111 1.1368 1.1000 0.0932  -0.1501 0.0260  801  VAL   B O   
6274  C  CB  . VAL   B 497 ? 1.2551 1.1969 1.1643 0.0807  -0.1493 0.0227  801  VAL   B CB  
6275  C  CG1 . VAL   B 497 ? 1.2537 1.2054 1.1709 0.0749  -0.1464 0.0249  801  VAL   B CG1 
6276  C  CG2 . VAL   B 497 ? 1.2474 1.1906 1.1615 0.0780  -0.1510 0.0195  801  VAL   B CG2 
6277  N  N   . LEU   B 498 ? 1.2580 1.1732 1.1501 0.0818  -0.1509 0.0253  802  LEU   B N   
6278  C  CA  . LEU   B 498 ? 1.2135 1.1221 1.0965 0.0866  -0.1506 0.0277  802  LEU   B CA  
6279  C  C   . LEU   B 498 ? 1.2589 1.1791 1.1445 0.0877  -0.1476 0.0311  802  LEU   B C   
6280  O  O   . LEU   B 498 ? 1.2893 1.2124 1.1703 0.0949  -0.1471 0.0330  802  LEU   B O   
6281  C  CB  . LEU   B 498 ? 1.2101 1.1052 1.0898 0.0820  -0.1515 0.0272  802  LEU   B CB  
6282  C  CG  . LEU   B 498 ? 1.2183 1.1007 1.0964 0.0800  -0.1551 0.0236  802  LEU   B CG  
6283  C  CD1 . LEU   B 498 ? 1.2369 1.1053 1.1101 0.0772  -0.1554 0.0240  802  LEU   B CD1 
6284  C  CD2 . LEU   B 498 ? 1.1758 1.0533 1.0463 0.0878  -0.1581 0.0217  802  LEU   B CD2 
6285  N  N   . HIS   B 499 ? 1.2416 1.1681 1.1348 0.0808  -0.1457 0.0320  803  HIS   B N   
6286  C  CA  . HIS   B 499 ? 1.2491 1.1867 1.1455 0.0812  -0.1434 0.0348  803  HIS   B CA  
6287  C  C   . HIS   B 499 ? 1.2406 1.1916 1.1484 0.0760  -0.1417 0.0344  803  HIS   B C   
6288  O  O   . HIS   B 499 ? 1.2106 1.1605 1.1238 0.0699  -0.1419 0.0323  803  HIS   B O   
6289  C  CB  . HIS   B 499 ? 1.3022 1.2333 1.1946 0.0785  -0.1424 0.0368  803  HIS   B CB  
6290  C  CG  . HIS   B 499 ? 1.3259 1.2662 1.2190 0.0808  -0.1412 0.0396  803  HIS   B CG  
6291  N  ND1 . HIS   B 499 ? 1.3197 1.2657 1.2103 0.0885  -0.1417 0.0410  803  HIS   B ND1 
6292  C  CD2 . HIS   B 499 ? 1.3067 1.2514 1.2028 0.0765  -0.1396 0.0411  803  HIS   B CD2 
6293  C  CE1 . HIS   B 499 ? 1.3105 1.2643 1.2034 0.0888  -0.1410 0.0431  803  HIS   B CE1 
6294  N  NE2 . HIS   B 499 ? 1.2785 1.2312 1.1740 0.0817  -0.1398 0.0432  803  HIS   B NE2 
6295  N  N   . ALA   B 500 ? 1.2332 1.1968 1.1451 0.0784  -0.1403 0.0363  804  ALA   B N   
6296  C  CA  . ALA   B 500 ? 1.1954 1.1721 1.1178 0.0737  -0.1387 0.0362  804  ALA   B CA  
6297  C  C   . ALA   B 500 ? 1.1498 1.1341 1.0740 0.0738  -0.1375 0.0388  804  ALA   B C   
6298  O  O   . ALA   B 500 ? 1.1396 1.1305 1.0636 0.0796  -0.1376 0.0404  804  ALA   B O   
6299  C  CB  . ALA   B 500 ? 1.1989 1.1845 1.1259 0.0770  -0.1383 0.0353  804  ALA   B CB  
6300  N  N   . HIS   B 501 ? 1.1356 1.1189 1.0618 0.0675  -0.1366 0.0392  805  HIS   B N   
6301  C  CA  . HIS   B 501 ? 1.1331 1.1225 1.0603 0.0671  -0.1359 0.0413  805  HIS   B CA  
6302  C  C   . HIS   B 501 ? 1.1504 1.1538 1.0883 0.0633  -0.1347 0.0411  805  HIS   B C   
6303  O  O   . HIS   B 501 ? 1.1373 1.1414 1.0803 0.0571  -0.1336 0.0396  805  HIS   B O   
6304  C  CB  . HIS   B 501 ? 1.1363 1.1152 1.0580 0.0629  -0.1352 0.0421  805  HIS   B CB  
6305  C  CG  . HIS   B 501 ? 1.1578 1.1412 1.0790 0.0625  -0.1348 0.0441  805  HIS   B CG  
6306  N  ND1 . HIS   B 501 ? 1.1410 1.1311 1.0613 0.0684  -0.1363 0.0456  805  HIS   B ND1 
6307  C  CD2 . HIS   B 501 ? 1.1336 1.1153 1.0550 0.0571  -0.1332 0.0448  805  HIS   B CD2 
6308  C  CE1 . HIS   B 501 ? 1.1626 1.1550 1.0824 0.0666  -0.1362 0.0469  805  HIS   B CE1 
6309  N  NE2 . HIS   B 501 ? 1.1709 1.1579 1.0907 0.0600  -0.1341 0.0465  805  HIS   B NE2 
6310  N  N   . GLN   B 502 ? 1.1294 1.1436 1.0710 0.0670  -0.1350 0.0424  806  GLN   B N   
6311  C  CA  . GLN   B 502 ? 1.0954 1.1229 1.0471 0.0636  -0.1339 0.0423  806  GLN   B CA  
6312  C  C   . GLN   B 502 ? 1.0740 1.1032 1.0258 0.0603  -0.1340 0.0435  806  GLN   B C   
6313  O  O   . GLN   B 502 ? 1.1364 1.1643 1.0835 0.0641  -0.1354 0.0451  806  GLN   B O   
6314  C  CB  . GLN   B 502 ? 1.1614 1.2002 1.1186 0.0690  -0.1340 0.0430  806  GLN   B CB  
6315  C  CG  . GLN   B 502 ? 1.0614 1.1140 1.0291 0.0660  -0.1331 0.0432  806  GLN   B CG  
6316  C  CD  . GLN   B 502 ? 1.0402 1.1035 1.0141 0.0714  -0.1326 0.0440  806  GLN   B CD  
6317  O  OE1 . GLN   B 502 ? 1.0626 1.1253 1.0364 0.0744  -0.1315 0.0434  806  GLN   B OE1 
6318  N  NE2 . GLN   B 502 ? 1.1291 1.2017 1.1083 0.0728  -0.1334 0.0453  806  GLN   B NE2 
6319  N  N   . PHE   B 503 ? 1.0732 1.1050 1.0300 0.0536  -0.1326 0.0427  807  PHE   B N   
6320  C  CA  . PHE   B 503 ? 1.0985 1.1309 1.0545 0.0503  -0.1323 0.0437  807  PHE   B CA  
6321  C  C   . PHE   B 503 ? 1.1490 1.1942 1.1111 0.0523  -0.1336 0.0446  807  PHE   B C   
6322  O  O   . PHE   B 503 ? 1.1694 1.2235 1.1373 0.0560  -0.1342 0.0445  807  PHE   B O   
6323  C  CB  . PHE   B 503 ? 1.0230 1.0538 0.9824 0.0427  -0.1301 0.0426  807  PHE   B CB  
6324  C  CG  . PHE   B 503 ? 1.0773 1.0946 1.0307 0.0400  -0.1288 0.0422  807  PHE   B CG  
6325  C  CD1 . PHE   B 503 ? 1.0647 1.0720 1.0099 0.0391  -0.1281 0.0436  807  PHE   B CD1 
6326  C  CD2 . PHE   B 503 ? 1.0565 1.0704 1.0124 0.0383  -0.1285 0.0402  807  PHE   B CD2 
6327  C  CE1 . PHE   B 503 ? 1.0701 1.0646 1.0105 0.0364  -0.1264 0.0434  807  PHE   B CE1 
6328  C  CE2 . PHE   B 503 ? 1.0991 1.1006 1.0509 0.0355  -0.1275 0.0396  807  PHE   B CE2 
6329  C  CZ  . PHE   B 503 ? 1.1038 1.0956 1.0482 0.0343  -0.1262 0.0413  807  PHE   B CZ  
6330  N  N   . LEU   B 504 ? 1.1362 1.1816 1.0969 0.0499  -0.1340 0.0453  808  LEU   B N   
6331  C  CA  . LEU   B 504 ? 1.1930 1.2494 1.1591 0.0514  -0.1359 0.0459  808  LEU   B CA  
6332  C  C   . LEU   B 504 ? 1.1239 1.1931 1.1020 0.0486  -0.1349 0.0449  808  LEU   B C   
6333  O  O   . LEU   B 504 ? 1.1612 1.2303 1.1425 0.0439  -0.1326 0.0437  808  LEU   B O   
6334  C  CB  . LEU   B 504 ? 1.2427 1.2951 1.2037 0.0488  -0.1365 0.0466  808  LEU   B CB  
6335  C  CG  . LEU   B 504 ? 1.2767 1.3230 1.2286 0.0539  -0.1394 0.0480  808  LEU   B CG  
6336  C  CD1 . LEU   B 504 ? 1.3082 1.3433 1.2511 0.0580  -0.1393 0.0487  808  LEU   B CD1 
6337  C  CD2 . LEU   B 504 ? 1.2617 1.3014 1.2066 0.0509  -0.1393 0.0486  808  LEU   B CD2 
6338  N  N   . GLN   B 505 ? 1.1190 1.1994 1.1040 0.0516  -0.1366 0.0453  809  GLN   B N   
6339  C  CA  . GLN   B 505 ? 1.1525 1.2450 1.1489 0.0490  -0.1354 0.0446  809  GLN   B CA  
6340  C  C   . GLN   B 505 ? 1.1682 1.2624 1.1667 0.0427  -0.1350 0.0439  809  GLN   B C   
6341  O  O   . GLN   B 505 ? 1.2009 1.2933 1.1958 0.0424  -0.1370 0.0445  809  GLN   B O   
6342  C  CB  . GLN   B 505 ? 1.2325 1.3365 1.2369 0.0536  -0.1372 0.0453  809  GLN   B CB  
6343  C  CG  . GLN   B 505 ? 1.2938 1.4099 1.3095 0.0501  -0.1367 0.0448  809  GLN   B CG  
6344  C  CD  . GLN   B 505 ? 1.3340 1.4618 1.3599 0.0542  -0.1368 0.0454  809  GLN   B CD  
6345  O  OE1 . GLN   B 505 ? 1.3906 1.5177 1.4158 0.0592  -0.1358 0.0461  809  GLN   B OE1 
6346  N  NE2 . GLN   B 505 ? 1.3549 1.4934 1.3907 0.0522  -0.1377 0.0453  809  GLN   B NE2 
6347  N  N   . ASN   B 506 ? 1.1056 1.2030 1.1096 0.0381  -0.1325 0.0428  810  ASN   B N   
6348  C  CA  . ASN   B 506 ? 1.1256 1.2236 1.1311 0.0320  -0.1315 0.0420  810  ASN   B CA  
6349  C  C   . ASN   B 506 ? 1.1188 1.2043 1.1154 0.0289  -0.1302 0.0420  810  ASN   B C   
6350  O  O   . ASN   B 506 ? 1.1066 1.1905 1.1018 0.0249  -0.1296 0.0419  810  ASN   B O   
6351  C  CB  . ASN   B 506 ? 1.2046 1.3093 1.2130 0.0320  -0.1340 0.0425  810  ASN   B CB  
6352  C  CG  . ASN   B 506 ? 1.1850 1.3029 1.2053 0.0310  -0.1339 0.0420  810  ASN   B CG  
6353  O  OD1 . ASN   B 506 ? 1.1606 1.2855 1.1870 0.0346  -0.1340 0.0423  810  ASN   B OD1 
6354  N  ND2 . ASN   B 506 ? 1.2027 1.3238 1.2262 0.0260  -0.1334 0.0413  810  ASN   B ND2 
6355  N  N   . GLU   B 507 ? 1.1407 1.2172 1.1315 0.0306  -0.1295 0.0420  811  GLU   B N   
6356  C  CA  . GLU   B 507 ? 1.0599 1.1241 1.0432 0.0276  -0.1278 0.0421  811  GLU   B CA  
6357  C  C   . GLU   B 507 ? 1.0511 1.1122 1.0373 0.0247  -0.1257 0.0405  811  GLU   B C   
6358  O  O   . GLU   B 507 ? 0.9991 1.0607 0.9864 0.0278  -0.1264 0.0399  811  GLU   B O   
6359  C  CB  . GLU   B 507 ? 1.0583 1.1125 1.0313 0.0321  -0.1291 0.0435  811  GLU   B CB  
6360  C  CG  . GLU   B 507 ? 1.1201 1.1615 1.0851 0.0289  -0.1270 0.0440  811  GLU   B CG  
6361  C  CD  . GLU   B 507 ? 1.1670 1.1972 1.1214 0.0334  -0.1280 0.0452  811  GLU   B CD  
6362  O  OE1 . GLU   B 507 ? 1.1671 1.1977 1.1210 0.0382  -0.1297 0.0452  811  GLU   B OE1 
6363  O  OE2 . GLU   B 507 ? 1.1662 1.1866 1.1123 0.0323  -0.1268 0.0464  811  GLU   B OE2 
6364  N  N   . TYR   B 508 ? 1.0760 1.1337 1.0633 0.0188  -0.1234 0.0398  812  TYR   B N   
6365  C  CA  . TYR   B 508 ? 1.0727 1.1290 1.0648 0.0151  -0.1218 0.0379  812  TYR   B CA  
6366  C  C   . TYR   B 508 ? 1.0663 1.1098 1.0528 0.0128  -0.1201 0.0380  812  TYR   B C   
6367  O  O   . TYR   B 508 ? 1.0597 1.0987 1.0439 0.0091  -0.1179 0.0387  812  TYR   B O   
6368  C  CB  . TYR   B 508 ? 1.1001 1.1642 1.0999 0.0101  -0.1203 0.0369  812  TYR   B CB  
6369  C  CG  . TYR   B 508 ? 1.1078 1.1730 1.1140 0.0072  -0.1194 0.0346  812  TYR   B CG  
6370  C  CD1 . TYR   B 508 ? 1.1148 1.1716 1.1208 0.0035  -0.1179 0.0336  812  TYR   B CD1 
6371  C  CD2 . TYR   B 508 ? 1.1062 1.1805 1.1188 0.0085  -0.1203 0.0335  812  TYR   B CD2 
6372  C  CE1 . TYR   B 508 ? 1.1388 1.1964 1.1509 0.0012  -0.1179 0.0313  812  TYR   B CE1 
6373  C  CE2 . TYR   B 508 ? 1.1231 1.1975 1.1405 0.0064  -0.1200 0.0313  812  TYR   B CE2 
6374  C  CZ  . TYR   B 508 ? 1.1270 1.1931 1.1443 0.0028  -0.1192 0.0300  812  TYR   B CZ  
6375  O  OH  . TYR   B 508 ? 1.1896 1.2555 1.2119 0.0009  -0.1196 0.0275  812  TYR   B OH  
6376  N  N   . ALA   B 509 ? 1.0196 1.0567 1.0039 0.0149  -0.1210 0.0372  813  ALA   B N   
6377  C  CA  . ALA   B 509 ? 0.9899 1.0143 0.9693 0.0130  -0.1197 0.0373  813  ALA   B CA  
6378  C  C   . ALA   B 509 ? 0.9795 1.0029 0.9659 0.0067  -0.1175 0.0355  813  ALA   B C   
6379  O  O   . ALA   B 509 ? 1.0786 1.1083 1.0723 0.0055  -0.1184 0.0335  813  ALA   B O   
6380  C  CB  . ALA   B 509 ? 1.0150 1.0327 0.9896 0.0175  -0.1218 0.0369  813  ALA   B CB  
6381  N  N   . LEU   B 510 ? 0.9636 0.9787 0.9477 0.0028  -0.1146 0.0363  814  LEU   B N   
6382  C  CA  . LEU   B 510 ? 0.9583 0.9729 0.9501 -0.0034 -0.1121 0.0348  814  LEU   B CA  
6383  C  C   . LEU   B 510 ? 1.0467 1.0494 1.0378 -0.0058 -0.1106 0.0344  814  LEU   B C   
6384  O  O   . LEU   B 510 ? 1.1033 1.1056 1.1016 -0.0083 -0.1115 0.0319  814  LEU   B O   
6385  C  CB  . LEU   B 510 ? 1.0014 1.0191 0.9941 -0.0070 -0.1087 0.0362  814  LEU   B CB  
6386  C  CG  . LEU   B 510 ? 1.0680 1.0976 1.0627 -0.0056 -0.1101 0.0364  814  LEU   B CG  
6387  C  CD1 . LEU   B 510 ? 1.0140 1.0437 1.0060 -0.0081 -0.1072 0.0380  814  LEU   B CD1 
6388  C  CD2 . LEU   B 510 ? 1.0128 1.0524 1.0175 -0.0071 -0.1113 0.0340  814  LEU   B CD2 
6389  N  N   . SER   B 511 ? 1.0352 1.0276 1.0176 -0.0050 -0.1088 0.0366  815  SER   B N   
6390  C  CA  . SER   B 511 ? 1.0191 0.9994 1.0009 -0.0077 -0.1068 0.0365  815  SER   B CA  
6391  C  C   . SER   B 511 ? 1.1035 1.0758 1.0781 -0.0029 -0.1098 0.0366  815  SER   B C   
6392  O  O   . SER   B 511 ? 1.0938 1.0663 1.0599 0.0026  -0.1117 0.0381  815  SER   B O   
6393  C  CB  . SER   B 511 ? 1.1489 1.1211 1.1255 -0.0104 -0.1018 0.0392  815  SER   B CB  
6394  O  OG  . SER   B 511 ? 1.0730 1.0525 1.0501 -0.0115 -0.0999 0.0403  815  SER   B OG  
6395  N  N   . LEU   B 512 ? 1.0803 1.0447 1.0581 -0.0051 -0.1100 0.0349  816  LEU   B N   
6396  C  CA  . LEU   B 512 ? 1.1105 1.0646 1.0806 -0.0012 -0.1122 0.0351  816  LEU   B CA  
6397  C  C   . LEU   B 512 ? 1.1106 1.0518 1.0815 -0.0055 -0.1093 0.0353  816  LEU   B C   
6398  O  O   . LEU   B 512 ? 1.1560 1.0977 1.1372 -0.0113 -0.1075 0.0337  816  LEU   B O   
6399  C  CB  . LEU   B 512 ? 1.0631 1.0209 1.0357 0.0023  -0.1173 0.0323  816  LEU   B CB  
6400  C  CG  . LEU   B 512 ? 1.0800 1.0282 1.0437 0.0075  -0.1201 0.0324  816  LEU   B CG  
6401  C  CD1 . LEU   B 512 ? 1.0778 1.0269 1.0311 0.0133  -0.1203 0.0353  816  LEU   B CD1 
6402  C  CD2 . LEU   B 512 ? 1.0724 1.0231 1.0389 0.0104  -0.1247 0.0294  816  LEU   B CD2 
6403  N  N   . VAL   B 513 ? 1.1755 1.1052 1.1359 -0.0027 -0.1087 0.0373  817  VAL   B N   
6404  C  CA  . VAL   B 513 ? 1.2028 1.1189 1.1629 -0.0065 -0.1055 0.0379  817  VAL   B CA  
6405  C  C   . VAL   B 513 ? 1.1509 1.0558 1.1002 -0.0015 -0.1079 0.0385  817  VAL   B C   
6406  O  O   . VAL   B 513 ? 1.1518 1.0573 1.0909 0.0046  -0.1097 0.0402  817  VAL   B O   
6407  C  CB  . VAL   B 513 ? 1.1786 1.0899 1.1357 -0.0100 -0.0990 0.0410  817  VAL   B CB  
6408  C  CG1 . VAL   B 513 ? 1.1927 1.0894 1.1498 -0.0137 -0.0953 0.0418  817  VAL   B CG1 
6409  C  CG2 . VAL   B 513 ? 1.2026 1.1245 1.1701 -0.0149 -0.0963 0.0404  817  VAL   B CG2 
6410  N  N   . SER   B 514 ? 1.2057 1.1001 1.1579 -0.0042 -0.1081 0.0371  818  SER   B N   
6411  C  CA  . SER   B 514 ? 1.2429 1.1241 1.1851 -0.0005 -0.1096 0.0379  818  SER   B CA  
6412  C  C   . SER   B 514 ? 1.2344 1.1026 1.1764 -0.0056 -0.1040 0.0397  818  SER   B C   
6413  O  O   . SER   B 514 ? 1.3167 1.1818 1.2696 -0.0113 -0.1030 0.0377  818  SER   B O   
6414  C  CB  . SER   B 514 ? 1.2441 1.1236 1.1893 0.0015  -0.1154 0.0343  818  SER   B CB  
6415  O  OG  . SER   B 514 ? 1.3222 1.1875 1.2578 0.0046  -0.1166 0.0349  818  SER   B OG  
6416  N  N   . CYS   B 515 ? 1.2789 1.1392 1.2089 -0.0034 -0.1003 0.0434  819  CYS   B N   
6417  C  CA  . CYS   B 515 ? 1.3833 1.2298 1.3116 -0.0077 -0.0943 0.0456  819  CYS   B CA  
6418  C  C   . CYS   B 515 ? 1.4102 1.2443 1.3214 -0.0023 -0.0933 0.0489  819  CYS   B C   
6419  O  O   . CYS   B 515 ? 1.3931 1.2314 1.2943 0.0040  -0.0960 0.0500  819  CYS   B O   
6420  C  CB  . CYS   B 515 ? 1.3270 1.1774 1.2613 -0.0132 -0.0879 0.0473  819  CYS   B CB  
6421  S  SG  . CYS   B 515 ? 1.3853 1.2413 1.3073 -0.0084 -0.0864 0.0506  819  CYS   B SG  
6422  N  N   . LYS   B 516 ? 1.4783 1.2968 1.3863 -0.0048 -0.0897 0.0502  820  LYS   B N   
6423  C  CA  . LYS   B 516 ? 1.5115 1.3166 1.4031 -0.0010 -0.0865 0.0541  820  LYS   B CA  
6424  C  C   . LYS   B 516 ? 1.4166 1.2207 1.3062 -0.0040 -0.0793 0.0572  820  LYS   B C   
6425  O  O   . LYS   B 516 ? 1.3876 1.1946 1.2893 -0.0108 -0.0749 0.0568  820  LYS   B O   
6426  C  CB  . LYS   B 516 ? 1.3660 1.1539 1.2544 -0.0022 -0.0852 0.0544  820  LYS   B CB  
6427  N  N   . LEU   B 517 ? 1.3900 1.1905 1.2644 0.0013  -0.0784 0.0603  821  LEU   B N   
6428  C  CA  . LEU   B 517 ? 1.4522 1.2509 1.3220 -0.0003 -0.0721 0.0633  821  LEU   B CA  
6429  C  C   . LEU   B 517 ? 1.5133 1.2937 1.3658 0.0029  -0.0680 0.0672  821  LEU   B C   
6430  O  O   . LEU   B 517 ? 1.5495 1.3229 1.3909 0.0087  -0.0717 0.0676  821  LEU   B O   
6431  C  CB  . LEU   B 517 ? 1.3879 1.2008 1.2555 0.0033  -0.0752 0.0632  821  LEU   B CB  
6432  C  CG  . LEU   B 517 ? 1.3861 1.2143 1.2699 -0.0020 -0.0750 0.0608  821  LEU   B CG  
6433  C  CD1 . LEU   B 517 ? 1.4177 1.2559 1.2976 0.0005  -0.0756 0.0617  821  LEU   B CD1 
6434  C  CD2 . LEU   B 517 ? 1.4308 1.2531 1.3240 -0.0098 -0.0678 0.0614  821  LEU   B CD2 
6435  N  N   . GLY   B 518 ? 1.4939 1.2661 1.3437 -0.0007 -0.0599 0.0701  822  GLY   B N   
6436  C  CA  . GLY   B 518 ? 1.5181 1.2719 1.3508 0.0019  -0.0546 0.0742  822  GLY   B CA  
6437  C  C   . GLY   B 518 ? 1.6109 1.3500 1.4390 0.0028  -0.0550 0.0745  822  GLY   B C   
6438  O  O   . GLY   B 518 ? 1.6001 1.3412 1.4399 -0.0004 -0.0578 0.0716  822  GLY   B O   
6439  N  N   . LYS   B 519 ? 1.6638 1.3869 1.4734 0.0074  -0.0522 0.0780  823  LYS   B N   
6440  C  CA  . LYS   B 519 ? 1.6640 1.3725 1.4674 0.0090  -0.0529 0.0784  823  LYS   B CA  
6441  C  C   . LYS   B 519 ? 1.6954 1.4105 1.4963 0.0153  -0.0626 0.0757  823  LYS   B C   
6442  O  O   . LYS   B 519 ? 1.7399 1.4433 1.5344 0.0176  -0.0642 0.0757  823  LYS   B O   
6443  C  CB  . LYS   B 519 ? 1.6360 1.3245 1.4193 0.0125  -0.0471 0.0830  823  LYS   B CB  
6444  N  N   . ASP   B 520 ? 1.5994 1.3324 1.4055 0.0179  -0.0687 0.0733  824  ASP   B N   
6445  C  CA  . ASP   B 520 ? 1.5554 1.2957 1.3610 0.0236  -0.0773 0.0707  824  ASP   B CA  
6446  C  C   . ASP   B 520 ? 1.5582 1.2988 1.3766 0.0195  -0.0796 0.0674  824  ASP   B C   
6447  O  O   . ASP   B 520 ? 1.5302 1.2764 1.3642 0.0121  -0.0772 0.0658  824  ASP   B O   
6448  C  CB  . ASP   B 520 ? 1.5471 1.3071 1.3578 0.0262  -0.0821 0.0690  824  ASP   B CB  
6449  C  CG  . ASP   B 520 ? 1.5732 1.3385 1.3771 0.0345  -0.0897 0.0679  824  ASP   B CG  
6450  O  OD1 . ASP   B 520 ? 1.5529 1.3166 1.3594 0.0358  -0.0935 0.0659  824  ASP   B OD1 
6451  O  OD2 . ASP   B 520 ? 1.5952 1.3658 1.3912 0.0399  -0.0919 0.0691  824  ASP   B OD2 
6452  N  N   . PRO   B 521 ? 1.5892 1.3232 1.4014 0.0242  -0.0844 0.0664  825  PRO   B N   
6453  C  CA  . PRO   B 521 ? 1.5796 1.3133 1.4031 0.0209  -0.0875 0.0629  825  PRO   B CA  
6454  C  C   . PRO   B 521 ? 1.5859 1.3365 1.4184 0.0231  -0.0948 0.0591  825  PRO   B C   
6455  O  O   . PRO   B 521 ? 1.5714 1.3247 1.4159 0.0194  -0.0973 0.0558  825  PRO   B O   
6456  C  CB  . PRO   B 521 ? 1.4677 1.1841 1.2779 0.0253  -0.0886 0.0640  825  PRO   B CB  
6457  C  CG  . PRO   B 521 ? 1.4852 1.2017 1.2791 0.0340  -0.0906 0.0664  825  PRO   B CG  
6458  C  CD  . PRO   B 521 ? 1.5469 1.2697 1.3403 0.0323  -0.0863 0.0686  825  PRO   B CD  
6459  N  N   . ASN   B 522 ? 1.5821 1.3438 1.4093 0.0293  -0.0983 0.0595  826  ASN   B N   
6460  C  CA  . ASN   B 522 ? 1.5489 1.3273 1.3853 0.0311  -0.1040 0.0563  826  ASN   B CA  
6461  C  C   . ASN   B 522 ? 1.5429 1.3326 1.3961 0.0235  -0.1022 0.0543  826  ASN   B C   
6462  O  O   . ASN   B 522 ? 1.5212 1.3119 1.3773 0.0190  -0.0969 0.0560  826  ASN   B O   
6463  C  CB  . ASN   B 522 ? 1.4870 1.2759 1.3164 0.0382  -0.1071 0.0573  826  ASN   B CB  
6464  C  CG  . ASN   B 522 ? 1.5638 1.3424 1.3768 0.0462  -0.1090 0.0593  826  ASN   B CG  
6465  O  OD1 . ASN   B 522 ? 1.6285 1.4035 1.4382 0.0505  -0.1131 0.0579  826  ASN   B OD1 
6466  N  ND2 . ASN   B 522 ? 1.5814 1.3549 1.3835 0.0486  -0.1063 0.0625  826  ASN   B ND2 
6467  N  N   . THR   B 523 ? 1.5246 1.3225 1.3883 0.0225  -0.1066 0.0506  827  THR   B N   
6468  C  CA  . THR   B 523 ? 1.5441 1.3560 1.4230 0.0171  -0.1063 0.0485  827  THR   B CA  
6469  C  C   . THR   B 523 ? 1.4868 1.3150 1.3661 0.0220  -0.1102 0.0479  827  THR   B C   
6470  O  O   . THR   B 523 ? 1.5042 1.3344 1.3780 0.0286  -0.1149 0.0471  827  THR   B O   
6471  C  CB  . THR   B 523 ? 1.5153 1.3259 1.4061 0.0127  -0.1088 0.0448  827  THR   B CB  
6472  O  OG1 . THR   B 523 ? 1.5251 1.3342 1.4110 0.0187  -0.1149 0.0427  827  THR   B OG1 
6473  C  CG2 . THR   B 523 ? 1.5196 1.3145 1.4120 0.0070  -0.1043 0.0456  827  THR   B CG2 
6474  N  N   . TYR   B 524 ? 1.4197 1.2591 1.3052 0.0190  -0.1078 0.0484  828  TYR   B N   
6475  C  CA  . TYR   B 524 ? 1.3865 1.2403 1.2713 0.0235  -0.1105 0.0485  828  TYR   B CA  
6476  C  C   . TYR   B 524 ? 1.3792 1.2481 1.2783 0.0201  -0.1121 0.0457  828  TYR   B C   
6477  O  O   . TYR   B 524 ? 1.3855 1.2546 1.2953 0.0136  -0.1103 0.0440  828  TYR   B O   
6478  C  CB  . TYR   B 524 ? 1.3984 1.2523 1.2759 0.0242  -0.1070 0.0518  828  TYR   B CB  
6479  C  CG  . TYR   B 524 ? 1.4527 1.2932 1.3144 0.0292  -0.1062 0.0547  828  TYR   B CG  
6480  C  CD1 . TYR   B 524 ? 1.4764 1.3138 1.3297 0.0364  -0.1106 0.0546  828  TYR   B CD1 
6481  C  CD2 . TYR   B 524 ? 1.5031 1.3333 1.3574 0.0271  -0.1008 0.0577  828  TYR   B CD2 
6482  C  CE1 . TYR   B 524 ? 1.5181 1.3429 1.3564 0.0414  -0.1101 0.0572  828  TYR   B CE1 
6483  C  CE2 . TYR   B 524 ? 1.5083 1.3252 1.3468 0.0321  -0.1001 0.0604  828  TYR   B CE2 
6484  C  CZ  . TYR   B 524 ? 1.5357 1.3502 1.3666 0.0392  -0.1050 0.0601  828  TYR   B CZ  
6485  O  OH  . TYR   B 524 ? 1.6043 1.4056 1.4194 0.0445  -0.1047 0.0627  828  TYR   B OH  
6486  N  N   . PHE   B 525 ? 1.3114 1.1933 1.2109 0.0247  -0.1154 0.0453  829  PHE   B N   
6487  C  CA  . PHE   B 525 ? 1.2315 1.1288 1.1429 0.0221  -0.1164 0.0433  829  PHE   B CA  
6488  C  C   . PHE   B 525 ? 1.1964 1.1013 1.1073 0.0212  -0.1138 0.0454  829  PHE   B C   
6489  O  O   . PHE   B 525 ? 1.2045 1.1121 1.1077 0.0265  -0.1152 0.0471  829  PHE   B O   
6490  C  CB  . PHE   B 525 ? 1.1263 1.0326 1.0388 0.0277  -0.1214 0.0414  829  PHE   B CB  
6491  C  CG  . PHE   B 525 ? 1.1609 1.0627 1.0766 0.0279  -0.1245 0.0385  829  PHE   B CG  
6492  C  CD1 . PHE   B 525 ? 1.1600 1.0609 1.0860 0.0214  -0.1239 0.0360  829  PHE   B CD1 
6493  C  CD2 . PHE   B 525 ? 1.1728 1.0710 1.0812 0.0348  -0.1282 0.0380  829  PHE   B CD2 
6494  C  CE1 . PHE   B 525 ? 1.2119 1.1081 1.1403 0.0219  -0.1275 0.0329  829  PHE   B CE1 
6495  C  CE2 . PHE   B 525 ? 1.1686 1.0617 1.0786 0.0355  -0.1314 0.0351  829  PHE   B CE2 
6496  C  CZ  . PHE   B 525 ? 1.2126 1.1044 1.1325 0.0291  -0.1313 0.0325  829  PHE   B CZ  
6497  N  N   . ILE   B 526 ? 1.1844 1.0925 1.1035 0.0146  -0.1102 0.0451  830  ILE   B N   
6498  C  CA  . ILE   B 526 ? 1.1982 1.1136 1.1172 0.0135  -0.1079 0.0467  830  ILE   B CA  
6499  C  C   . ILE   B 526 ? 1.1268 1.0580 1.0572 0.0119  -0.1097 0.0445  830  ILE   B C   
6500  O  O   . ILE   B 526 ? 1.1238 1.0580 1.0645 0.0076  -0.1098 0.0421  830  ILE   B O   
6501  C  CB  . ILE   B 526 ? 1.1624 1.0694 1.0807 0.0079  -0.1018 0.0485  830  ILE   B CB  
6502  C  CG1 . ILE   B 526 ? 1.2205 1.1105 1.1271 0.0096  -0.0996 0.0508  830  ILE   B CG1 
6503  C  CG2 . ILE   B 526 ? 1.1251 1.0373 1.0399 0.0082  -0.0998 0.0504  830  ILE   B CG2 
6504  C  CD1 . ILE   B 526 ? 1.0543 0.9349 0.9586 0.0048  -0.0927 0.0532  830  ILE   B CD1 
6505  N  N   . VAL   B 527 ? 1.1051 1.0462 1.0337 0.0154  -0.1116 0.0453  831  VAL   B N   
6506  C  CA  . VAL   B 527 ? 1.1229 1.0791 1.0613 0.0146  -0.1133 0.0435  831  VAL   B CA  
6507  C  C   . VAL   B 527 ? 1.1346 1.0967 1.0731 0.0128  -0.1112 0.0449  831  VAL   B C   
6508  O  O   . VAL   B 527 ? 1.1250 1.0860 1.0550 0.0166  -0.1119 0.0469  831  VAL   B O   
6509  C  CB  . VAL   B 527 ? 1.0856 1.0492 1.0233 0.0209  -0.1179 0.0428  831  VAL   B CB  
6510  C  CG1 . VAL   B 527 ? 1.0171 0.9957 0.9628 0.0204  -0.1188 0.0420  831  VAL   B CG1 
6511  C  CG2 . VAL   B 527 ? 1.1524 1.1123 1.0923 0.0219  -0.1200 0.0407  831  VAL   B CG2 
6512  N  N   . GLY   B 528 ? 1.1244 1.0927 1.0723 0.0072  -0.1090 0.0438  832  GLY   B N   
6513  C  CA  . GLY   B 528 ? 1.1720 1.1465 1.1206 0.0053  -0.1072 0.0448  832  GLY   B CA  
6514  C  C   . GLY   B 528 ? 1.0809 1.0705 1.0373 0.0063  -0.1102 0.0432  832  GLY   B C   
6515  O  O   . GLY   B 528 ? 1.0616 1.0574 1.0270 0.0045  -0.1112 0.0410  832  GLY   B O   
6516  N  N   . THR   B 529 ? 1.0338 1.0290 0.9866 0.0091  -0.1116 0.0444  833  THR   B N   
6517  C  CA  . THR   B 529 ? 1.0780 1.0873 1.0379 0.0105  -0.1144 0.0433  833  THR   B CA  
6518  C  C   . THR   B 529 ? 1.0987 1.1141 1.0600 0.0082  -0.1134 0.0438  833  THR   B C   
6519  O  O   . THR   B 529 ? 1.0227 1.0313 0.9790 0.0056  -0.1103 0.0451  833  THR   B O   
6520  C  CB  . THR   B 529 ? 1.0711 1.0830 1.0270 0.0174  -0.1184 0.0438  833  THR   B CB  
6521  O  OG1 . THR   B 529 ? 1.0740 1.0814 1.0204 0.0205  -0.1192 0.0459  833  THR   B OG1 
6522  C  CG2 . THR   B 529 ? 1.0702 1.0740 1.0229 0.0197  -0.1191 0.0434  833  THR   B CG2 
6523  N  N   . ALA   B 530 ? 1.0959 1.1241 1.0642 0.0091  -0.1158 0.0428  834  ALA   B N   
6524  C  CA  . ALA   B 530 ? 1.0893 1.1246 1.0597 0.0075  -0.1158 0.0430  834  ALA   B CA  
6525  C  C   . ALA   B 530 ? 1.0561 1.1035 1.0313 0.0111  -0.1196 0.0426  834  ALA   B C   
6526  O  O   . ALA   B 530 ? 1.0831 1.1370 1.0649 0.0123  -0.1208 0.0414  834  ALA   B O   
6527  C  CB  . ALA   B 530 ? 1.0552 1.0942 1.0335 0.0013  -0.1127 0.0417  834  ALA   B CB  
6528  N  N   . MET   B 531 ? 1.0758 1.1259 1.0478 0.0128  -0.1215 0.0435  835  MET   B N   
6529  C  CA  . MET   B 531 ? 1.1292 1.1910 1.1070 0.0159  -0.1251 0.0431  835  MET   B CA  
6530  C  C   . MET   B 531 ? 1.1251 1.1971 1.1125 0.0117  -0.1242 0.0418  835  MET   B C   
6531  O  O   . MET   B 531 ? 1.0928 1.1631 1.0786 0.0081  -0.1228 0.0418  835  MET   B O   
6532  C  CB  . MET   B 531 ? 1.2150 1.2748 1.1855 0.0198  -0.1283 0.0444  835  MET   B CB  
6533  C  CG  . MET   B 531 ? 1.2167 1.2665 1.1774 0.0246  -0.1293 0.0457  835  MET   B CG  
6534  S  SD  . MET   B 531 ? 1.1541 1.2097 1.1206 0.0292  -0.1312 0.0452  835  MET   B SD  
6535  C  CE  . MET   B 531 ? 1.1887 1.2582 1.1625 0.0330  -0.1356 0.0451  835  MET   B CE  
6536  N  N   . VAL   B 532 ? 1.1048 1.1865 1.1014 0.0122  -0.1249 0.0407  836  VAL   B N   
6537  C  CA  . VAL   B 532 ? 1.0941 1.1850 1.0998 0.0084  -0.1239 0.0395  836  VAL   B CA  
6538  C  C   . VAL   B 532 ? 1.1008 1.2033 1.1134 0.0111  -0.1267 0.0395  836  VAL   B C   
6539  O  O   . VAL   B 532 ? 1.1306 1.2362 1.1449 0.0155  -0.1282 0.0399  836  VAL   B O   
6540  C  CB  . VAL   B 532 ? 1.1356 1.2271 1.1467 0.0059  -0.1216 0.0381  836  VAL   B CB  
6541  C  CG1 . VAL   B 532 ? 1.1076 1.1873 1.1130 0.0041  -0.1194 0.0380  836  VAL   B CG1 
6542  C  CG2 . VAL   B 532 ? 1.1373 1.2348 1.1531 0.0100  -0.1230 0.0377  836  VAL   B CG2 
6543  N  N   . TYR   B 533 ? 1.1264 1.2351 1.1432 0.0084  -0.1271 0.0390  837  TYR   B N   
6544  C  CA  . TYR   B 533 ? 1.1709 1.2912 1.1962 0.0100  -0.1293 0.0388  837  TYR   B CA  
6545  C  C   . TYR   B 533 ? 1.1699 1.2969 1.2028 0.0054  -0.1275 0.0376  837  TYR   B C   
6546  O  O   . TYR   B 533 ? 1.1793 1.3022 1.2096 0.0012  -0.1257 0.0371  837  TYR   B O   
6547  C  CB  . TYR   B 533 ? 1.1545 1.2761 1.1774 0.0122  -0.1331 0.0395  837  TYR   B CB  
6548  C  CG  . TYR   B 533 ? 1.1765 1.2902 1.1902 0.0168  -0.1352 0.0406  837  TYR   B CG  
6549  C  CD1 . TYR   B 533 ? 1.2325 1.3495 1.2485 0.0220  -0.1372 0.0413  837  TYR   B CD1 
6550  C  CD2 . TYR   B 533 ? 1.2359 1.3383 1.2383 0.0161  -0.1350 0.0412  837  TYR   B CD2 
6551  C  CE1 . TYR   B 533 ? 1.3119 1.4215 1.3192 0.0265  -0.1393 0.0423  837  TYR   B CE1 
6552  C  CE2 . TYR   B 533 ? 1.2341 1.3284 1.2273 0.0206  -0.1368 0.0424  837  TYR   B CE2 
6553  C  CZ  . TYR   B 533 ? 1.3320 1.4300 1.3276 0.0258  -0.1392 0.0428  837  TYR   B CZ  
6554  O  OH  . TYR   B 533 ? 1.2918 1.3815 1.2779 0.0304  -0.1412 0.0439  837  TYR   B OH  
6555  N  N   . PRO   B 534 ? 1.1702 1.3070 1.2124 0.0061  -0.1275 0.0373  838  PRO   B N   
6556  C  CA  . PRO   B 534 ? 1.2317 1.3740 1.2805 0.0019  -0.1254 0.0361  838  PRO   B CA  
6557  C  C   . PRO   B 534 ? 1.2292 1.3731 1.2783 -0.0016 -0.1263 0.0357  838  PRO   B C   
6558  O  O   . PRO   B 534 ? 1.1732 1.3183 1.2249 -0.0058 -0.1242 0.0347  838  PRO   B O   
6559  C  CB  . PRO   B 534 ? 1.2604 1.4124 1.3182 0.0044  -0.1255 0.0363  838  PRO   B CB  
6560  C  CG  . PRO   B 534 ? 1.2213 1.3714 1.2765 0.0097  -0.1265 0.0373  838  PRO   B CG  
6561  C  CD  . PRO   B 534 ? 1.1609 1.3040 1.2079 0.0109  -0.1289 0.0380  838  PRO   B CD  
6562  N  N   . GLU   B 535 ? 1.1990 1.3426 1.2451 0.0002  -0.1296 0.0363  839  GLU   B N   
6563  C  CA  . GLU   B 535 ? 1.1243 1.2687 1.1697 -0.0025 -0.1310 0.0358  839  GLU   B CA  
6564  C  C   . GLU   B 535 ? 1.1146 1.2486 1.1502 -0.0051 -0.1291 0.0358  839  GLU   B C   
6565  O  O   . GLU   B 535 ? 1.1470 1.2810 1.1832 -0.0091 -0.1275 0.0350  839  GLU   B O   
6566  C  CB  . GLU   B 535 ? 1.1764 1.3236 1.2217 0.0009  -0.1359 0.0362  839  GLU   B CB  
6567  C  CG  . GLU   B 535 ? 1.2622 1.4179 1.3160 0.0048  -0.1376 0.0367  839  GLU   B CG  
6568  C  CD  . GLU   B 535 ? 1.2701 1.4206 1.3188 0.0091  -0.1372 0.0378  839  GLU   B CD  
6569  O  OE1 . GLU   B 535 ? 1.2348 1.3794 1.2794 0.0080  -0.1339 0.0378  839  GLU   B OE1 
6570  O  OE2 . GLU   B 535 ? 1.3007 1.4531 1.3499 0.0135  -0.1405 0.0385  839  GLU   B OE2 
6571  N  N   . GLU   B 536 ? 1.1289 1.2535 1.1555 -0.0029 -0.1289 0.0368  840  GLU   B N   
6572  C  CA  . GLU   B 536 ? 1.0939 1.2076 1.1106 -0.0049 -0.1269 0.0372  840  GLU   B CA  
6573  C  C   . GLU   B 536 ? 0.9930 1.1032 1.0109 -0.0084 -0.1222 0.0368  840  GLU   B C   
6574  O  O   . GLU   B 536 ? 1.0619 1.1708 1.0812 -0.0072 -0.1212 0.0368  840  GLU   B O   
6575  C  CB  . GLU   B 536 ? 1.0088 1.1134 1.0149 -0.0008 -0.1287 0.0385  840  GLU   B CB  
6576  N  N   . ALA   B 537 ? 0.9733 1.0819 0.9911 -0.0126 -0.1195 0.0362  841  ALA   B N   
6577  C  CA  . ALA   B 537 ? 0.9750 1.0821 0.9964 -0.0162 -0.1155 0.0354  841  ALA   B CA  
6578  C  C   . ALA   B 537 ? 1.0555 1.1515 1.0699 -0.0163 -0.1128 0.0363  841  ALA   B C   
6579  O  O   . ALA   B 537 ? 1.1129 1.2073 1.1300 -0.0163 -0.1116 0.0359  841  ALA   B O   
6580  C  CB  . ALA   B 537 ? 1.0449 1.1538 1.0686 -0.0205 -0.1133 0.0345  841  ALA   B CB  
6581  N  N   . GLU   B 538 ? 1.1089 1.1967 1.1142 -0.0162 -0.1119 0.0375  842  GLU   B N   
6582  C  CA  . GLU   B 538 ? 1.0807 1.1568 1.0783 -0.0163 -0.1088 0.0387  842  GLU   B CA  
6583  C  C   . GLU   B 538 ? 1.0642 1.1358 1.0552 -0.0114 -0.1116 0.0399  842  GLU   B C   
6584  O  O   . GLU   B 538 ? 1.0379 1.1124 1.0261 -0.0079 -0.1157 0.0402  842  GLU   B O   
6585  C  CB  . GLU   B 538 ? 1.0990 1.1675 1.0887 -0.0181 -0.1060 0.0396  842  GLU   B CB  
6586  C  CG  . GLU   B 538 ? 1.2480 1.3046 1.2318 -0.0195 -0.1011 0.0409  842  GLU   B CG  
6587  C  CD  . GLU   B 538 ? 1.3685 1.4256 1.3597 -0.0247 -0.0962 0.0400  842  GLU   B CD  
6588  O  OE1 . GLU   B 538 ? 1.3444 1.4084 1.3409 -0.0271 -0.0959 0.0389  842  GLU   B OE1 
6589  O  OE2 . GLU   B 538 ? 1.3899 1.4406 1.3820 -0.0263 -0.0928 0.0404  842  GLU   B OE2 
6590  N  N   . PRO   B 539 ? 1.1585 1.2232 1.1475 -0.0110 -0.1098 0.0404  843  PRO   B N   
6591  C  CA  . PRO   B 539 ? 1.0880 1.1477 1.0704 -0.0062 -0.1123 0.0415  843  PRO   B CA  
6592  C  C   . PRO   B 539 ? 1.0545 1.1033 1.0240 -0.0043 -0.1118 0.0434  843  PRO   B C   
6593  O  O   . PRO   B 539 ? 1.0491 1.0884 1.0135 -0.0069 -0.1073 0.0443  843  PRO   B O   
6594  C  CB  . PRO   B 539 ? 0.9889 1.0442 0.9738 -0.0071 -0.1102 0.0412  843  PRO   B CB  
6595  C  CG  . PRO   B 539 ? 1.0468 1.0990 1.0348 -0.0126 -0.1053 0.0408  843  PRO   B CG  
6596  C  CD  . PRO   B 539 ? 1.0856 1.1461 1.0784 -0.0150 -0.1054 0.0399  843  PRO   B CD  
6597  N  N   . LYS   B 540 ? 1.0593 1.1091 1.0235 0.0002  -0.1162 0.0440  844  LYS   B N   
6598  C  CA  . LYS   B 540 ? 1.1236 1.1630 1.0745 0.0027  -0.1167 0.0455  844  LYS   B CA  
6599  C  C   . LYS   B 540 ? 1.1390 1.1692 1.0805 0.0074  -0.1179 0.0470  844  LYS   B C   
6600  O  O   . LYS   B 540 ? 1.1077 1.1283 1.0369 0.0102  -0.1185 0.0483  844  LYS   B O   
6601  C  CB  . LYS   B 540 ? 0.9632 1.0091 0.9138 0.0046  -0.1214 0.0448  844  LYS   B CB  
6602  N  N   . GLN   B 541 ? 1.1124 1.1442 1.0584 0.0087  -0.1183 0.0467  845  GLN   B N   
6603  C  CA  . GLN   B 541 ? 1.1162 1.1401 1.0537 0.0136  -0.1201 0.0480  845  GLN   B CA  
6604  C  C   . GLN   B 541 ? 1.1366 1.1604 1.0793 0.0134  -0.1188 0.0476  845  GLN   B C   
6605  O  O   . GLN   B 541 ? 1.1437 1.1776 1.0974 0.0119  -0.1195 0.0461  845  GLN   B O   
6606  C  CB  . GLN   B 541 ? 1.2055 1.2354 1.1420 0.0192  -0.1263 0.0479  845  GLN   B CB  
6607  C  CG  . GLN   B 541 ? 1.2305 1.2765 1.1804 0.0187  -0.1294 0.0462  845  GLN   B CG  
6608  C  CD  . GLN   B 541 ? 1.3405 1.3919 1.2897 0.0236  -0.1354 0.0461  845  GLN   B CD  
6609  O  OE1 . GLN   B 541 ? 1.3588 1.4131 1.3094 0.0283  -0.1386 0.0462  845  GLN   B OE1 
6610  N  NE2 . GLN   B 541 ? 1.4303 1.4830 1.3777 0.0226  -0.1372 0.0456  845  GLN   B NE2 
6611  N  N   . GLY   B 542 ? 1.2147 1.2264 1.1484 0.0152  -0.1174 0.0489  846  GLY   B N   
6612  C  CA  . GLY   B 542 ? 1.1284 1.1376 1.0653 0.0152  -0.1164 0.0485  846  GLY   B CA  
6613  C  C   . GLY   B 542 ? 1.1337 1.1307 1.0592 0.0195  -0.1168 0.0501  846  GLY   B C   
6614  O  O   . GLY   B 542 ? 1.1476 1.1404 1.0637 0.0239  -0.1192 0.0514  846  GLY   B O   
6615  N  N   . ARG   B 543 ? 1.1296 1.1204 1.0557 0.0185  -0.1148 0.0500  847  ARG   B N   
6616  C  CA  . ARG   B 543 ? 1.0829 1.0631 0.9994 0.0230  -0.1158 0.0513  847  ARG   B CA  
6617  C  C   . ARG   B 543 ? 1.1347 1.1061 1.0523 0.0195  -0.1121 0.0511  847  ARG   B C   
6618  O  O   . ARG   B 543 ? 1.1143 1.0917 1.0423 0.0164  -0.1117 0.0492  847  ARG   B O   
6619  C  CB  . ARG   B 543 ? 1.0735 1.0612 0.9923 0.0287  -0.1208 0.0506  847  ARG   B CB  
6620  C  CG  . ARG   B 543 ? 1.2030 1.1977 1.1199 0.0332  -0.1250 0.0510  847  ARG   B CG  
6621  C  CD  . ARG   B 543 ? 1.3169 1.3122 1.2310 0.0401  -0.1290 0.0513  847  ARG   B CD  
6622  N  NE  . ARG   B 543 ? 1.2908 1.2956 1.2152 0.0406  -0.1300 0.0498  847  ARG   B NE  
6623  C  CZ  . ARG   B 543 ? 1.3120 1.3133 1.2346 0.0443  -0.1308 0.0498  847  ARG   B CZ  
6624  N  NH1 . ARG   B 543 ? 1.2811 1.2695 1.1925 0.0472  -0.1307 0.0511  847  ARG   B NH1 
6625  N  NH2 . ARG   B 543 ? 1.2839 1.2942 1.2154 0.0452  -0.1317 0.0485  847  ARG   B NH2 
6626  N  N   . ILE   B 544 ? 1.1951 1.1519 1.1020 0.0200  -0.1094 0.0529  848  ILE   B N   
6627  C  CA  . ILE   B 544 ? 1.1140 1.0608 1.0202 0.0186  -0.1073 0.0529  848  ILE   B CA  
6628  C  C   . ILE   B 544 ? 1.1009 1.0431 0.9991 0.0253  -0.1110 0.0535  848  ILE   B C   
6629  O  O   . ILE   B 544 ? 1.1558 1.0925 1.0429 0.0298  -0.1123 0.0553  848  ILE   B O   
6630  C  CB  . ILE   B 544 ? 1.1173 1.0504 1.0177 0.0147  -0.1013 0.0547  848  ILE   B CB  
6631  C  CG1 . ILE   B 544 ? 1.1542 1.0929 1.0609 0.0093  -0.0978 0.0544  848  ILE   B CG1 
6632  C  CG2 . ILE   B 544 ? 1.1527 1.0772 1.0558 0.0120  -0.0990 0.0542  848  ILE   B CG2 
6633  C  CD1 . ILE   B 544 ? 1.1596 1.0871 1.0649 0.0042  -0.0909 0.0558  848  ILE   B CD1 
6634  N  N   . VAL   B 545 ? 1.1264 1.0711 1.0299 0.0264  -0.1131 0.0519  849  VAL   B N   
6635  C  CA  . VAL   B 545 ? 1.1410 1.0807 1.0372 0.0328  -0.1164 0.0524  849  VAL   B CA  
6636  C  C   . VAL   B 545 ? 1.2184 1.1444 1.1112 0.0310  -0.1140 0.0525  849  VAL   B C   
6637  O  O   . VAL   B 545 ? 1.1926 1.1176 1.0932 0.0252  -0.1114 0.0512  849  VAL   B O   
6638  C  CB  . VAL   B 545 ? 1.1719 1.1244 1.0756 0.0364  -0.1207 0.0506  849  VAL   B CB  
6639  C  CG1 . VAL   B 545 ? 1.2005 1.1466 1.0977 0.0423  -0.1232 0.0508  849  VAL   B CG1 
6640  C  CG2 . VAL   B 545 ? 1.2268 1.1908 1.1323 0.0392  -0.1233 0.0510  849  VAL   B CG2 
6641  N  N   . VAL   B 546 ? 1.2902 1.2055 1.1717 0.0360  -0.1151 0.0539  850  VAL   B N   
6642  C  CA  . VAL   B 546 ? 1.2432 1.1447 1.1205 0.0352  -0.1135 0.0540  850  VAL   B CA  
6643  C  C   . VAL   B 546 ? 1.2703 1.1717 1.1447 0.0414  -0.1179 0.0532  850  VAL   B C   
6644  O  O   . VAL   B 546 ? 1.2096 1.1089 1.0747 0.0479  -0.1204 0.0546  850  VAL   B O   
6645  C  CB  . VAL   B 546 ? 1.2333 1.1187 1.0980 0.0351  -0.1098 0.0568  850  VAL   B CB  
6646  C  CG1 . VAL   B 546 ? 1.2585 1.1312 1.1234 0.0315  -0.1069 0.0566  850  VAL   B CG1 
6647  C  CG2 . VAL   B 546 ? 1.2978 1.1845 1.1624 0.0313  -0.1060 0.0581  850  VAL   B CG2 
6648  N  N   . PHE   B 547 ? 1.2969 1.2000 1.1788 0.0398  -0.1190 0.0509  851  PHE   B N   
6649  C  CA  . PHE   B 547 ? 1.2601 1.1615 1.1391 0.0455  -0.1227 0.0499  851  PHE   B CA  
6650  C  C   . PHE   B 547 ? 1.2917 1.1766 1.1646 0.0447  -0.1217 0.0499  851  PHE   B C   
6651  O  O   . PHE   B 547 ? 1.2465 1.1229 1.1206 0.0388  -0.1180 0.0502  851  PHE   B O   
6652  C  CB  . PHE   B 547 ? 1.1985 1.1118 1.0884 0.0452  -0.1252 0.0472  851  PHE   B CB  
6653  C  CG  . PHE   B 547 ? 1.2777 1.2073 1.1741 0.0464  -0.1264 0.0471  851  PHE   B CG  
6654  C  CD1 . PHE   B 547 ? 1.2787 1.2144 1.1715 0.0534  -0.1292 0.0481  851  PHE   B CD1 
6655  C  CD2 . PHE   B 547 ? 1.2322 1.1713 1.1392 0.0406  -0.1248 0.0459  851  PHE   B CD2 
6656  C  CE1 . PHE   B 547 ? 1.2225 1.1732 1.1225 0.0541  -0.1303 0.0479  851  PHE   B CE1 
6657  C  CE2 . PHE   B 547 ? 1.1844 1.1379 1.0976 0.0416  -0.1259 0.0457  851  PHE   B CE2 
6658  C  CZ  . PHE   B 547 ? 1.1959 1.1551 1.1058 0.0481  -0.1286 0.0467  851  PHE   B CZ  
6659  N  N   . GLN   B 548 ? 1.3566 1.2374 1.2234 0.0509  -0.1250 0.0496  852  GLN   B N   
6660  C  CA  . GLN   B 548 ? 1.3061 1.1724 1.1677 0.0511  -0.1252 0.0490  852  GLN   B CA  
6661  C  C   . GLN   B 548 ? 1.2937 1.1629 1.1552 0.0568  -0.1295 0.0471  852  GLN   B C   
6662  O  O   . GLN   B 548 ? 1.2787 1.1550 1.1370 0.0634  -0.1319 0.0478  852  GLN   B O   
6663  C  CB  . GLN   B 548 ? 1.3706 1.2226 1.2185 0.0539  -0.1236 0.0518  852  GLN   B CB  
6664  C  CG  . GLN   B 548 ? 1.4068 1.2419 1.2495 0.0525  -0.1227 0.0516  852  GLN   B CG  
6665  C  CD  . GLN   B 548 ? 1.3211 1.1442 1.1487 0.0589  -0.1233 0.0539  852  GLN   B CD  
6666  O  OE1 . GLN   B 548 ? 1.3818 1.1940 1.2015 0.0575  -0.1198 0.0563  852  GLN   B OE1 
6667  N  NE2 . GLN   B 548 ? 1.3362 1.1615 1.1592 0.0664  -0.1275 0.0533  852  GLN   B NE2 
6668  N  N   . TYR   B 549 ? 1.2869 1.1508 1.1523 0.0543  -0.1306 0.0446  853  TYR   B N   
6669  C  CA  . TYR   B 549 ? 1.4089 1.2729 1.2727 0.0598  -0.1346 0.0427  853  TYR   B CA  
6670  C  C   . TYR   B 549 ? 1.6090 1.4561 1.4615 0.0632  -0.1356 0.0431  853  TYR   B C   
6671  O  O   . TYR   B 549 ? 1.6347 1.4695 1.4864 0.0584  -0.1339 0.0429  853  TYR   B O   
6672  C  CB  . TYR   B 549 ? 1.3879 1.2564 1.2624 0.0557  -0.1360 0.0392  853  TYR   B CB  
6673  C  CG  . TYR   B 549 ? 1.3968 1.2683 1.2696 0.0622  -0.1399 0.0374  853  TYR   B CG  
6674  C  CD1 . TYR   B 549 ? 1.4515 1.3340 1.3230 0.0684  -0.1407 0.0385  853  TYR   B CD1 
6675  C  CD2 . TYR   B 549 ? 1.4044 1.2672 1.2768 0.0622  -0.1426 0.0346  853  TYR   B CD2 
6676  C  CE1 . TYR   B 549 ? 1.4846 1.3695 1.3543 0.0746  -0.1434 0.0372  853  TYR   B CE1 
6677  C  CE2 . TYR   B 549 ? 1.4037 1.2681 1.2730 0.0687  -0.1459 0.0330  853  TYR   B CE2 
6678  C  CZ  . TYR   B 549 ? 1.4583 1.3338 1.3261 0.0750  -0.1459 0.0345  853  TYR   B CZ  
6679  O  OH  . TYR   B 549 ? 1.4858 1.3628 1.3504 0.0818  -0.1484 0.0332  853  TYR   B OH  
6680  N  N   . SER   B 550 ? 1.8639 1.7103 1.7079 0.0716  -0.1381 0.0438  854  SER   B N   
6681  C  CA  . SER   B 550 ? 1.9033 1.7339 1.7362 0.0756  -0.1396 0.0439  854  SER   B CA  
6682  C  C   . SER   B 550 ? 1.9336 1.7669 1.7630 0.0837  -0.1434 0.0427  854  SER   B C   
6683  O  O   . SER   B 550 ? 1.9243 1.7576 1.7577 0.0832  -0.1455 0.0399  854  SER   B O   
6684  C  CB  . SER   B 550 ? 1.9725 1.7942 1.7941 0.0782  -0.1378 0.0472  854  SER   B CB  
6685  O  OG  . SER   B 550 ? 1.9875 1.8181 1.8052 0.0854  -0.1392 0.0489  854  SER   B OG  
6686  N  N   . ASP   B 551 ? 1.9152 1.7506 1.7369 0.0914  -0.1442 0.0448  855  ASP   B N   
6687  C  CA  . ASP   B 551 ? 1.8949 1.7319 1.7124 0.0997  -0.1470 0.0440  855  ASP   B CA  
6688  C  C   . ASP   B 551 ? 1.8210 1.6740 1.6487 0.1003  -0.1477 0.0425  855  ASP   B C   
6689  O  O   . ASP   B 551 ? 1.7691 1.6335 1.5981 0.1057  -0.1478 0.0437  855  ASP   B O   
6690  C  CB  . ASP   B 551 ? 1.9283 1.7645 1.7364 0.1077  -0.1476 0.0466  855  ASP   B CB  
6691  C  CG  . ASP   B 551 ? 1.9699 1.7880 1.7655 0.1089  -0.1474 0.0479  855  ASP   B CG  
6692  O  OD1 . ASP   B 551 ? 1.9745 1.7801 1.7687 0.1040  -0.1471 0.0466  855  ASP   B OD1 
6693  O  OD2 . ASP   B 551 ? 2.0132 1.8293 1.8006 0.1146  -0.1477 0.0503  855  ASP   B OD2 
6694  N  N   . GLY   B 552 ? 1.8620 1.7160 1.6972 0.0948  -0.1480 0.0398  856  GLY   B N   
6695  C  CA  . GLY   B 552 ? 1.8526 1.7201 1.6964 0.0957  -0.1485 0.0383  856  GLY   B CA  
6696  C  C   . GLY   B 552 ? 1.8413 1.7255 1.6931 0.0947  -0.1465 0.0400  856  GLY   B C   
6697  O  O   . GLY   B 552 ? 1.7903 1.6865 1.6501 0.0945  -0.1464 0.0390  856  GLY   B O   
6698  N  N   . LYS   B 553 ? 1.7242 1.6085 1.5734 0.0941  -0.1451 0.0425  857  LYS   B N   
6699  C  CA  . LYS   B 553 ? 1.6468 1.5458 1.5029 0.0933  -0.1437 0.0441  857  LYS   B CA  
6700  C  C   . LYS   B 553 ? 1.6043 1.5020 1.4636 0.0852  -0.1414 0.0448  857  LYS   B C   
6701  O  O   . LYS   B 553 ? 1.5909 1.4753 1.4437 0.0827  -0.1405 0.0454  857  LYS   B O   
6702  C  CB  . LYS   B 553 ? 1.7090 1.6107 1.5591 0.1010  -0.1446 0.0465  857  LYS   B CB  
6703  N  N   . LEU   B 554 ? 1.5167 1.4279 1.3861 0.0813  -0.1402 0.0446  858  LEU   B N   
6704  C  CA  . LEU   B 554 ? 1.4946 1.4064 1.3673 0.0743  -0.1378 0.0454  858  LEU   B CA  
6705  C  C   . LEU   B 554 ? 1.5626 1.4779 1.4312 0.0773  -0.1377 0.0480  858  LEU   B C   
6706  O  O   . LEU   B 554 ? 1.5717 1.4991 1.4439 0.0815  -0.1390 0.0485  858  LEU   B O   
6707  C  CB  . LEU   B 554 ? 1.3860 1.3101 1.2712 0.0687  -0.1367 0.0438  858  LEU   B CB  
6708  C  CG  . LEU   B 554 ? 1.2878 1.2114 1.1778 0.0604  -0.1339 0.0440  858  LEU   B CG  
6709  C  CD1 . LEU   B 554 ? 1.2527 1.1663 1.1446 0.0550  -0.1331 0.0420  858  LEU   B CD1 
6710  C  CD2 . LEU   B 554 ? 1.3099 1.2493 1.2105 0.0578  -0.1333 0.0434  858  LEU   B CD2 
6711  N  N   . GLN   B 555 ? 1.5105 1.4150 1.3715 0.0753  -0.1361 0.0496  859  GLN   B N   
6712  C  CA  . GLN   B 555 ? 1.5498 1.4567 1.4060 0.0782  -0.1364 0.0519  859  GLN   B CA  
6713  C  C   . GLN   B 555 ? 1.5079 1.4152 1.3665 0.0714  -0.1335 0.0526  859  GLN   B C   
6714  O  O   . GLN   B 555 ? 1.5100 1.4110 1.3709 0.0649  -0.1307 0.0520  859  GLN   B O   
6715  C  CB  . GLN   B 555 ? 1.6215 1.5147 1.4639 0.0839  -0.1374 0.0536  859  GLN   B CB  
6716  C  CG  . GLN   B 555 ? 1.7485 1.6440 1.5849 0.0887  -0.1389 0.0557  859  GLN   B CG  
6717  C  CD  . GLN   B 555 ? 1.7579 1.6718 1.6039 0.0912  -0.1411 0.0553  859  GLN   B CD  
6718  O  OE1 . GLN   B 555 ? 1.7276 1.6531 1.5848 0.0891  -0.1410 0.0537  859  GLN   B OE1 
6719  N  NE2 . GLN   B 555 ? 1.7880 1.7041 1.6296 0.0957  -0.1433 0.0568  859  GLN   B NE2 
6720  N  N   . THR   B 556 ? 1.3486 1.2637 1.2074 0.0730  -0.1343 0.0539  860  THR   B N   
6721  C  CA  . THR   B 556 ? 1.3900 1.3068 1.2508 0.0673  -0.1317 0.0545  860  THR   B CA  
6722  C  C   . THR   B 556 ? 1.3741 1.2762 1.2215 0.0681  -0.1302 0.0568  860  THR   B C   
6723  O  O   . THR   B 556 ? 1.4215 1.3206 1.2600 0.0746  -0.1328 0.0582  860  THR   B O   
6724  C  CB  . THR   B 556 ? 1.3779 1.3105 1.2459 0.0683  -0.1337 0.0544  860  THR   B CB  
6725  O  OG1 . THR   B 556 ? 1.3771 1.3232 1.2565 0.0688  -0.1351 0.0526  860  THR   B OG1 
6726  C  CG2 . THR   B 556 ? 1.2837 1.2178 1.1544 0.0618  -0.1309 0.0547  860  THR   B CG2 
6727  N  N   . VAL   B 557 ? 1.3366 1.2296 1.1826 0.0618  -0.1259 0.0573  861  VAL   B N   
6728  C  CA  . VAL   B 557 ? 1.2857 1.1629 1.1184 0.0622  -0.1233 0.0597  861  VAL   B CA  
6729  C  C   . VAL   B 557 ? 1.3178 1.1978 1.1476 0.0613  -0.1224 0.0610  861  VAL   B C   
6730  O  O   . VAL   B 557 ? 1.3193 1.1949 1.1384 0.0668  -0.1244 0.0626  861  VAL   B O   
6731  C  CB  . VAL   B 557 ? 1.2792 1.1437 1.1117 0.0561  -0.1186 0.0598  861  VAL   B CB  
6732  C  CG1 . VAL   B 557 ? 1.3166 1.1643 1.1354 0.0562  -0.1150 0.0625  861  VAL   B CG1 
6733  C  CG2 . VAL   B 557 ? 1.2456 1.1064 1.0801 0.0574  -0.1204 0.0581  861  VAL   B CG2 
6734  N  N   . ALA   B 558 ? 1.3091 1.1963 1.1481 0.0549  -0.1197 0.0603  862  ALA   B N   
6735  C  CA  . ALA   B 558 ? 1.2851 1.1759 1.1220 0.0541  -0.1191 0.0613  862  ALA   B CA  
6736  C  C   . ALA   B 558 ? 1.2914 1.1979 1.1428 0.0491  -0.1190 0.0594  862  ALA   B C   
6737  O  O   . ALA   B 558 ? 1.2442 1.1541 1.1057 0.0440  -0.1169 0.0579  862  ALA   B O   
6738  C  CB  . ALA   B 558 ? 1.3581 1.2334 1.1847 0.0511  -0.1137 0.0635  862  ALA   B CB  
6739  N  N   . GLU   B 559 ? 1.3001 1.2155 1.1523 0.0508  -0.1214 0.0594  863  GLU   B N   
6740  C  CA  . GLU   B 559 ? 1.2488 1.1777 1.1131 0.0460  -0.1209 0.0580  863  GLU   B CA  
6741  C  C   . GLU   B 559 ? 1.2396 1.1641 1.0974 0.0441  -0.1186 0.0593  863  GLU   B C   
6742  O  O   . GLU   B 559 ? 1.2643 1.1848 1.1118 0.0490  -0.1212 0.0605  863  GLU   B O   
6743  C  CB  . GLU   B 559 ? 1.2365 1.1818 1.1096 0.0496  -0.1261 0.0564  863  GLU   B CB  
6744  C  CG  . GLU   B 559 ? 1.3637 1.3093 1.2292 0.0574  -0.1311 0.0573  863  GLU   B CG  
6745  C  CD  . GLU   B 559 ? 1.4832 1.4462 1.3590 0.0598  -0.1358 0.0560  863  GLU   B CD  
6746  O  OE1 . GLU   B 559 ? 1.5131 1.4850 1.3964 0.0557  -0.1352 0.0552  863  GLU   B OE1 
6747  O  OE2 . GLU   B 559 ? 1.5257 1.4933 1.4023 0.0659  -0.1397 0.0559  863  GLU   B OE2 
6748  N  N   . LYS   B 560 ? 1.2139 1.1381 1.0770 0.0372  -0.1136 0.0591  864  LYS   B N   
6749  C  CA  . LYS   B 560 ? 1.2314 1.1533 1.0899 0.0350  -0.1112 0.0601  864  LYS   B CA  
6750  C  C   . LYS   B 560 ? 1.2196 1.1582 1.0906 0.0323  -0.1131 0.0581  864  LYS   B C   
6751  O  O   . LYS   B 560 ? 1.2065 1.1517 1.0893 0.0269  -0.1107 0.0567  864  LYS   B O   
6752  C  CB  . LYS   B 560 ? 1.1280 1.0375 0.9831 0.0295  -0.1038 0.0615  864  LYS   B CB  
6753  N  N   . GLU   B 561 ? 1.2329 1.1780 1.1016 0.0362  -0.1177 0.0579  865  GLU   B N   
6754  C  CA  . GLU   B 561 ? 1.2346 1.1951 1.1146 0.0341  -0.1200 0.0562  865  GLU   B CA  
6755  C  C   . GLU   B 561 ? 1.1942 1.1519 1.0730 0.0290  -0.1156 0.0566  865  GLU   B C   
6756  O  O   . GLU   B 561 ? 1.1918 1.1424 1.0597 0.0308  -0.1156 0.0578  865  GLU   B O   
6757  C  CB  . GLU   B 561 ? 1.2458 1.2133 1.1240 0.0401  -0.1266 0.0558  865  GLU   B CB  
6758  C  CG  . GLU   B 561 ? 1.3717 1.3537 1.2603 0.0379  -0.1290 0.0542  865  GLU   B CG  
6759  C  CD  . GLU   B 561 ? 1.5325 1.5141 1.4137 0.0418  -0.1334 0.0544  865  GLU   B CD  
6760  O  OE1 . GLU   B 561 ? 1.4997 1.4691 1.3682 0.0418  -0.1314 0.0557  865  GLU   B OE1 
6761  O  OE2 . GLU   B 561 ? 1.5964 1.5896 1.4846 0.0449  -0.1390 0.0532  865  GLU   B OE2 
6762  N  N   . VAL   B 562 ? 1.2135 1.1770 1.1037 0.0228  -0.1119 0.0554  866  VAL   B N   
6763  C  CA  . VAL   B 562 ? 1.2142 1.1759 1.1054 0.0175  -0.1070 0.0557  866  VAL   B CA  
6764  C  C   . VAL   B 562 ? 1.1857 1.1605 1.0840 0.0164  -0.1098 0.0542  866  VAL   B C   
6765  O  O   . VAL   B 562 ? 1.1493 1.1357 1.0540 0.0190  -0.1152 0.0528  866  VAL   B O   
6766  C  CB  . VAL   B 562 ? 1.1808 1.1415 1.0811 0.0115  -0.1017 0.0551  866  VAL   B CB  
6767  C  CG1 . VAL   B 562 ? 1.1982 1.1429 1.0895 0.0115  -0.0975 0.0571  866  VAL   B CG1 
6768  C  CG2 . VAL   B 562 ? 1.1236 1.0965 1.0372 0.0109  -0.1049 0.0528  866  VAL   B CG2 
6769  N  N   . LYS   B 563 ? 1.1220 1.0948 1.0193 0.0125  -0.1060 0.0545  867  LYS   B N   
6770  C  CA  . LYS   B 563 ? 1.1546 1.1381 1.0570 0.0117  -0.1087 0.0531  867  LYS   B CA  
6771  C  C   . LYS   B 563 ? 1.1829 1.1754 1.0990 0.0055  -0.1054 0.0516  867  LYS   B C   
6772  O  O   . LYS   B 563 ? 1.1416 1.1351 1.0584 0.0023  -0.1029 0.0514  867  LYS   B O   
6773  C  CB  . LYS   B 563 ? 1.1825 1.1570 1.0717 0.0132  -0.1080 0.0544  867  LYS   B CB  
6774  N  N   . GLY   B 564 ? 1.1612 1.1599 1.0877 0.0041  -0.1057 0.0504  868  GLY   B N   
6775  C  CA  . GLY   B 564 ? 1.1169 1.1228 1.0560 -0.0015 -0.1028 0.0488  868  GLY   B CA  
6776  C  C   . GLY   B 564 ? 1.1185 1.1276 1.0656 -0.0016 -0.1038 0.0477  868  GLY   B C   
6777  O  O   . GLY   B 564 ? 1.1167 1.1245 1.0605 0.0028  -0.1070 0.0480  868  GLY   B O   
6778  N  N   . ALA   B 565 ? 1.1534 1.1667 1.1110 -0.0064 -0.1011 0.0462  869  ALA   B N   
6779  C  CA  . ALA   B 565 ? 1.0947 1.1109 1.0602 -0.0070 -0.1020 0.0447  869  ALA   B CA  
6780  C  C   . ALA   B 565 ? 1.0733 1.0780 1.0374 -0.0097 -0.0978 0.0453  869  ALA   B C   
6781  O  O   . ALA   B 565 ? 1.0305 1.0320 0.9972 -0.0143 -0.0931 0.0454  869  ALA   B O   
6782  C  CB  . ALA   B 565 ? 1.0373 1.0656 1.0156 -0.0102 -0.1026 0.0424  869  ALA   B CB  
6783  N  N   . VAL   B 566 ? 1.0467 1.0454 1.0072 -0.0068 -0.0993 0.0455  870  VAL   B N   
6784  C  CA  . VAL   B 566 ? 1.0864 1.0744 1.0469 -0.0094 -0.0959 0.0458  870  VAL   B CA  
6785  C  C   . VAL   B 566 ? 1.0828 1.0773 1.0565 -0.0131 -0.0963 0.0430  870  VAL   B C   
6786  O  O   . VAL   B 566 ? 1.0748 1.0730 1.0516 -0.0106 -0.1002 0.0415  870  VAL   B O   
6787  C  CB  . VAL   B 566 ? 1.1026 1.0812 1.0540 -0.0049 -0.0977 0.0469  870  VAL   B CB  
6788  C  CG1 . VAL   B 566 ? 1.1514 1.1174 1.1017 -0.0080 -0.0935 0.0476  870  VAL   B CG1 
6789  C  CG2 . VAL   B 566 ? 1.0901 1.0649 1.0288 0.0001  -0.0992 0.0492  870  VAL   B CG2 
6790  N  N   . TYR   B 567 ? 1.1103 1.1059 1.0915 -0.0186 -0.0924 0.0424  871  TYR   B N   
6791  C  CA  . TYR   B 567 ? 1.1194 1.1213 1.1135 -0.0220 -0.0932 0.0395  871  TYR   B CA  
6792  C  C   . TYR   B 567 ? 1.1746 1.1676 1.1719 -0.0240 -0.0921 0.0387  871  TYR   B C   
6793  O  O   . TYR   B 567 ? 1.1488 1.1457 1.1547 -0.0250 -0.0947 0.0360  871  TYR   B O   
6794  C  CB  . TYR   B 567 ? 1.1813 1.1891 1.1834 -0.0269 -0.0898 0.0388  871  TYR   B CB  
6795  C  CG  . TYR   B 567 ? 1.1148 1.1329 1.1166 -0.0258 -0.0913 0.0388  871  TYR   B CG  
6796  C  CD1 . TYR   B 567 ? 1.0342 1.0619 1.0381 -0.0225 -0.0963 0.0375  871  TYR   B CD1 
6797  C  CD2 . TYR   B 567 ? 1.1135 1.1312 1.1129 -0.0280 -0.0876 0.0402  871  TYR   B CD2 
6798  C  CE1 . TYR   B 567 ? 1.1507 1.1876 1.1552 -0.0217 -0.0977 0.0375  871  TYR   B CE1 
6799  C  CE2 . TYR   B 567 ? 1.1321 1.1586 1.1313 -0.0270 -0.0893 0.0400  871  TYR   B CE2 
6800  C  CZ  . TYR   B 567 ? 1.1760 1.2124 1.1782 -0.0241 -0.0944 0.0387  871  TYR   B CZ  
6801  O  OH  . TYR   B 567 ? 1.1341 1.1791 1.1369 -0.0235 -0.0961 0.0385  871  TYR   B OH  
6802  N  N   . SER   B 568 ? 1.3098 1.2906 1.3002 -0.0247 -0.0883 0.0409  872  SER   B N   
6803  C  CA  . SER   B 568 ? 1.3248 1.2963 1.3184 -0.0269 -0.0871 0.0403  872  SER   B CA  
6804  C  C   . SER   B 568 ? 1.3405 1.2984 1.3217 -0.0247 -0.0846 0.0432  872  SER   B C   
6805  O  O   . SER   B 568 ? 1.3379 1.2914 1.3107 -0.0242 -0.0810 0.0459  872  SER   B O   
6806  C  CB  . SER   B 568 ? 1.3412 1.3126 1.3466 -0.0335 -0.0827 0.0393  872  SER   B CB  
6807  O  OG  . SER   B 568 ? 1.3670 1.3488 1.3846 -0.0352 -0.0860 0.0359  872  SER   B OG  
6808  N  N   . MET   B 569 ? 1.2176 1.1682 1.1973 -0.0232 -0.0867 0.0426  873  MET   B N   
6809  C  CA  . MET   B 569 ? 1.2004 1.1365 1.1698 -0.0218 -0.0842 0.0451  873  MET   B CA  
6810  C  C   . MET   B 569 ? 1.1979 1.1262 1.1754 -0.0262 -0.0823 0.0438  873  MET   B C   
6811  O  O   . MET   B 569 ? 1.2055 1.1382 1.1922 -0.0271 -0.0864 0.0407  873  MET   B O   
6812  C  CB  . MET   B 569 ? 1.1239 1.0579 1.0824 -0.0149 -0.0891 0.0456  873  MET   B CB  
6813  C  CG  . MET   B 569 ? 1.1329 1.0661 1.0786 -0.0104 -0.0890 0.0484  873  MET   B CG  
6814  S  SD  . MET   B 569 ? 1.2398 1.1787 1.1802 -0.0028 -0.0965 0.0475  873  MET   B SD  
6815  C  CE  . MET   B 569 ? 1.1969 1.1311 1.1435 -0.0037 -0.0988 0.0450  873  MET   B CE  
6816  N  N   . VAL   B 570 ? 1.2142 1.1305 1.1884 -0.0290 -0.0762 0.0463  874  VAL   B N   
6817  C  CA  . VAL   B 570 ? 1.2157 1.1226 1.1965 -0.0328 -0.0744 0.0455  874  VAL   B CA  
6818  C  C   . VAL   B 570 ? 1.2843 1.1753 1.2523 -0.0312 -0.0703 0.0489  874  VAL   B C   
6819  O  O   . VAL   B 570 ? 1.2597 1.1461 1.2184 -0.0305 -0.0654 0.0522  874  VAL   B O   
6820  C  CB  . VAL   B 570 ? 1.1554 1.0650 1.1515 -0.0400 -0.0697 0.0444  874  VAL   B CB  
6821  C  CG1 . VAL   B 570 ? 1.1593 1.0843 1.1666 -0.0411 -0.0736 0.0412  874  VAL   B CG1 
6822  C  CG2 . VAL   B 570 ? 1.2069 1.1108 1.1981 -0.0422 -0.0614 0.0481  874  VAL   B CG2 
6823  N  N   . GLU   B 571 ? 1.2944 1.1765 1.2610 -0.0303 -0.0726 0.0482  875  GLU   B N   
6824  C  CA  . GLU   B 571 ? 1.2907 1.1562 1.2485 -0.0305 -0.0678 0.0511  875  GLU   B CA  
6825  C  C   . GLU   B 571 ? 1.2960 1.1567 1.2620 -0.0373 -0.0594 0.0526  875  GLU   B C   
6826  O  O   . GLU   B 571 ? 1.2658 1.1313 1.2482 -0.0428 -0.0588 0.0501  875  GLU   B O   
6827  C  CB  . GLU   B 571 ? 1.2866 1.1443 1.2452 -0.0296 -0.0719 0.0493  875  GLU   B CB  
6828  C  CG  . GLU   B 571 ? 1.4514 1.2913 1.4005 -0.0295 -0.0674 0.0522  875  GLU   B CG  
6829  C  CD  . GLU   B 571 ? 1.5223 1.3545 1.4811 -0.0369 -0.0595 0.0533  875  GLU   B CD  
6830  O  OE1 . GLU   B 571 ? 1.4510 1.2916 1.4267 -0.0424 -0.0591 0.0508  875  GLU   B OE1 
6831  O  OE2 . GLU   B 571 ? 1.5135 1.3311 1.4631 -0.0370 -0.0535 0.0568  875  GLU   B OE2 
6832  N  N   . PHE   B 572 ? 1.3587 1.2098 1.3133 -0.0366 -0.0527 0.0567  876  PHE   B N   
6833  C  CA  . PHE   B 572 ? 1.3995 1.2445 1.3596 -0.0423 -0.0434 0.0589  876  PHE   B CA  
6834  C  C   . PHE   B 572 ? 1.4888 1.3150 1.4381 -0.0418 -0.0383 0.0622  876  PHE   B C   
6835  O  O   . PHE   B 572 ? 1.5025 1.3202 1.4341 -0.0371 -0.0361 0.0656  876  PHE   B O   
6836  C  CB  . PHE   B 572 ? 1.3739 1.2243 1.3292 -0.0418 -0.0394 0.0609  876  PHE   B CB  
6837  C  CG  . PHE   B 572 ? 1.3799 1.2247 1.3412 -0.0475 -0.0293 0.0632  876  PHE   B CG  
6838  C  CD1 . PHE   B 572 ? 1.3904 1.2403 1.3717 -0.0542 -0.0271 0.0610  876  PHE   B CD1 
6839  C  CD2 . PHE   B 572 ? 1.3966 1.2311 1.3435 -0.0457 -0.0222 0.0675  876  PHE   B CD2 
6840  C  CE1 . PHE   B 572 ? 1.4534 1.2987 1.4413 -0.0593 -0.0174 0.0632  876  PHE   B CE1 
6841  C  CE2 . PHE   B 572 ? 1.4145 1.2436 1.3666 -0.0505 -0.0123 0.0698  876  PHE   B CE2 
6842  C  CZ  . PHE   B 572 ? 1.4831 1.3180 1.4562 -0.0575 -0.0097 0.0677  876  PHE   B CZ  
6843  N  N   . ASN   B 573 ? 1.4826 1.3023 1.4431 -0.0465 -0.0365 0.0611  877  ASN   B N   
6844  C  CA  . ASN   B 573 ? 1.5043 1.3063 1.4573 -0.0465 -0.0329 0.0634  877  ASN   B CA  
6845  C  C   . ASN   B 573 ? 1.4644 1.2571 1.3943 -0.0389 -0.0342 0.0664  877  ASN   B C   
6846  O  O   . ASN   B 573 ? 1.4928 1.2746 1.4100 -0.0376 -0.0272 0.0706  877  ASN   B O   
6847  C  CB  . ASN   B 573 ? 1.4915 1.2839 1.4511 -0.0528 -0.0218 0.0663  877  ASN   B CB  
6848  C  CG  . ASN   B 573 ? 1.4977 1.2963 1.4581 -0.0543 -0.0156 0.0682  877  ASN   B CG  
6849  O  OD1 . ASN   B 573 ? 1.5323 1.3377 1.4821 -0.0496 -0.0185 0.0686  877  ASN   B OD1 
6850  N  ND2 . ASN   B 573 ? 1.4992 1.2951 1.4721 -0.0609 -0.0070 0.0693  877  ASN   B ND2 
6851  N  N   . GLY   B 574 ? 1.4463 1.2433 1.3706 -0.0335 -0.0431 0.0643  878  GLY   B N   
6852  C  CA  . GLY   B 574 ? 1.4832 1.2718 1.3874 -0.0261 -0.0455 0.0665  878  GLY   B CA  
6853  C  C   . GLY   B 574 ? 1.4867 1.2825 1.3794 -0.0206 -0.0474 0.0677  878  GLY   B C   
6854  O  O   . GLY   B 574 ? 1.4750 1.2680 1.3534 -0.0137 -0.0519 0.0685  878  GLY   B O   
6855  N  N   . LYS   B 575 ? 1.5022 1.3072 1.4009 -0.0234 -0.0443 0.0679  879  LYS   B N   
6856  C  CA  . LYS   B 575 ? 1.4815 1.2958 1.3723 -0.0189 -0.0472 0.0683  879  LYS   B CA  
6857  C  C   . LYS   B 575 ? 1.4219 1.2552 1.3255 -0.0191 -0.0546 0.0642  879  LYS   B C   
6858  O  O   . LYS   B 575 ? 1.4303 1.2682 1.3460 -0.0215 -0.0581 0.0611  879  LYS   B O   
6859  C  CB  . LYS   B 575 ? 1.5051 1.3164 1.3930 -0.0214 -0.0392 0.0711  879  LYS   B CB  
6860  N  N   . LEU   B 576 ? 1.3922 1.2360 1.2925 -0.0163 -0.0571 0.0640  880  LEU   B N   
6861  C  CA  . LEU   B 576 ? 1.3607 1.2223 1.2718 -0.0161 -0.0635 0.0606  880  LEU   B CA  
6862  C  C   . LEU   B 576 ? 1.2997 1.1705 1.2160 -0.0190 -0.0605 0.0607  880  LEU   B C   
6863  O  O   . LEU   B 576 ? 1.2335 1.1046 1.1390 -0.0155 -0.0604 0.0625  880  LEU   B O   
6864  C  CB  . LEU   B 576 ? 1.3167 1.1831 1.2185 -0.0087 -0.0710 0.0600  880  LEU   B CB  
6865  C  CG  . LEU   B 576 ? 1.2305 1.1148 1.1433 -0.0083 -0.0771 0.0567  880  LEU   B CG  
6866  C  CD1 . LEU   B 576 ? 1.1856 1.0721 1.1091 -0.0101 -0.0804 0.0537  880  LEU   B CD1 
6867  C  CD2 . LEU   B 576 ? 1.1927 1.0842 1.0969 -0.0014 -0.0828 0.0569  880  LEU   B CD2 
6868  N  N   . LEU   B 577 ? 1.2569 1.1349 1.1895 -0.0251 -0.0586 0.0586  881  LEU   B N   
6869  C  CA  . LEU   B 577 ? 1.2602 1.1471 1.1990 -0.0282 -0.0556 0.0585  881  LEU   B CA  
6870  C  C   . LEU   B 577 ? 1.2572 1.1607 1.2014 -0.0262 -0.0626 0.0557  881  LEU   B C   
6871  O  O   . LEU   B 577 ? 1.2315 1.1433 1.1876 -0.0277 -0.0668 0.0525  881  LEU   B O   
6872  C  CB  . LEU   B 577 ? 1.2317 1.1183 1.1859 -0.0356 -0.0500 0.0577  881  LEU   B CB  
6873  C  CG  . LEU   B 577 ? 1.2388 1.1333 1.1990 -0.0389 -0.0460 0.0578  881  LEU   B CG  
6874  C  CD1 . LEU   B 577 ? 1.2678 1.1514 1.2133 -0.0373 -0.0391 0.0620  881  LEU   B CD1 
6875  C  CD2 . LEU   B 577 ? 1.1607 1.0595 1.1400 -0.0459 -0.0425 0.0559  881  LEU   B CD2 
6876  N  N   . ALA   B 578 ? 1.2429 1.1511 1.1785 -0.0225 -0.0641 0.0567  882  ALA   B N   
6877  C  CA  . ALA   B 578 ? 1.2284 1.1521 1.1691 -0.0206 -0.0703 0.0543  882  ALA   B CA  
6878  C  C   . ALA   B 578 ? 1.2309 1.1623 1.1759 -0.0235 -0.0676 0.0543  882  ALA   B C   
6879  O  O   . ALA   B 578 ? 1.2319 1.1560 1.1701 -0.0245 -0.0619 0.0567  882  ALA   B O   
6880  C  CB  . ALA   B 578 ? 1.1704 1.0950 1.0990 -0.0135 -0.0760 0.0550  882  ALA   B CB  
6881  N  N   . SER   B 579 ? 1.2318 1.1774 1.1877 -0.0246 -0.0714 0.0515  883  SER   B N   
6882  C  CA  . SER   B 579 ? 1.2165 1.1710 1.1762 -0.0265 -0.0702 0.0511  883  SER   B CA  
6883  C  C   . SER   B 579 ? 1.2024 1.1651 1.1562 -0.0215 -0.0762 0.0507  883  SER   B C   
6884  O  O   . SER   B 579 ? 1.1993 1.1688 1.1563 -0.0188 -0.0819 0.0490  883  SER   B O   
6885  C  CB  . SER   B 579 ? 1.2224 1.1870 1.1989 -0.0315 -0.0702 0.0482  883  SER   B CB  
6886  O  OG  . SER   B 579 ? 1.2413 1.2121 1.2238 -0.0299 -0.0762 0.0457  883  SER   B OG  
6887  N  N   . ILE   B 580 ? 1.1853 1.1468 1.1304 -0.0200 -0.0749 0.0524  884  ILE   B N   
6888  C  CA  . ILE   B 580 ? 1.1403 1.1106 1.0819 -0.0160 -0.0805 0.0518  884  ILE   B CA  
6889  C  C   . ILE   B 580 ? 1.1456 1.1239 1.0930 -0.0192 -0.0788 0.0510  884  ILE   B C   
6890  O  O   . ILE   B 580 ? 1.1282 1.0998 1.0688 -0.0203 -0.0742 0.0527  884  ILE   B O   
6891  C  CB  . ILE   B 580 ? 1.1147 1.0763 1.0401 -0.0106 -0.0819 0.0541  884  ILE   B CB  
6892  C  CG1 . ILE   B 580 ? 1.1702 1.1226 1.0892 -0.0074 -0.0830 0.0551  884  ILE   B CG1 
6893  C  CG2 . ILE   B 580 ? 1.1701 1.1426 1.0951 -0.0069 -0.0883 0.0530  884  ILE   B CG2 
6894  C  CD1 . ILE   B 580 ? 1.2212 1.1822 1.1504 -0.0070 -0.0874 0.0527  884  ILE   B CD1 
6895  N  N   . ASN   B 581 ? 1.1457 1.1376 1.1045 -0.0204 -0.0823 0.0484  885  ASN   B N   
6896  C  CA  . ASN   B 581 ? 1.0999 1.0996 1.0649 -0.0237 -0.0808 0.0475  885  ASN   B CA  
6897  C  C   . ASN   B 581 ? 1.1517 1.1443 1.1188 -0.0284 -0.0733 0.0484  885  ASN   B C   
6898  O  O   . ASN   B 581 ? 1.1583 1.1494 1.1340 -0.0317 -0.0709 0.0476  885  ASN   B O   
6899  C  CB  . ASN   B 581 ? 1.0658 1.0676 1.0220 -0.0203 -0.0836 0.0482  885  ASN   B CB  
6900  C  CG  . ASN   B 581 ? 1.1032 1.1152 1.0616 -0.0164 -0.0909 0.0469  885  ASN   B CG  
6901  O  OD1 . ASN   B 581 ? 1.0854 1.1017 1.0500 -0.0155 -0.0935 0.0457  885  ASN   B OD1 
6902  N  ND2 . ASN   B 581 ? 1.2053 1.2209 1.1588 -0.0138 -0.0941 0.0470  885  ASN   B ND2 
6903  N  N   . SER   B 582 ? 1.1529 1.1405 1.1123 -0.0287 -0.0696 0.0501  886  SER   B N   
6904  C  CA  . SER   B 582 ? 1.1355 1.1171 1.0975 -0.0331 -0.0618 0.0512  886  SER   B CA  
6905  C  C   . SER   B 582 ? 1.1883 1.1538 1.1398 -0.0325 -0.0562 0.0542  886  SER   B C   
6906  O  O   . SER   B 582 ? 1.2003 1.1589 1.1511 -0.0353 -0.0489 0.0558  886  SER   B O   
6907  C  CB  . SER   B 582 ? 1.1430 1.1276 1.1024 -0.0338 -0.0600 0.0513  886  SER   B CB  
6908  O  OG  . SER   B 582 ? 1.0972 1.0794 1.0432 -0.0289 -0.0638 0.0523  886  SER   B OG  
6909  N  N   . THR   B 583 ? 1.2121 1.1711 1.1555 -0.0287 -0.0591 0.0551  887  THR   B N   
6910  C  CA  . THR   B 583 ? 1.2283 1.1711 1.1598 -0.0274 -0.0542 0.0582  887  THR   B CA  
6911  C  C   . THR   B 583 ? 1.1978 1.1367 1.1354 -0.0288 -0.0538 0.0578  887  THR   B C   
6912  O  O   . THR   B 583 ? 1.1624 1.1073 1.1037 -0.0269 -0.0601 0.0560  887  THR   B O   
6913  C  CB  . THR   B 583 ? 1.2151 1.1510 1.1289 -0.0209 -0.0577 0.0599  887  THR   B CB  
6914  O  OG1 . THR   B 583 ? 1.2887 1.2317 1.1991 -0.0190 -0.0613 0.0591  887  THR   B OG1 
6915  C  CG2 . THR   B 583 ? 1.2997 1.2181 1.1996 -0.0199 -0.0509 0.0634  887  THR   B CG2 
6916  N  N   . VAL   B 584 ? 1.1974 1.1258 1.1360 -0.0322 -0.0464 0.0596  888  VAL   B N   
6917  C  CA  . VAL   B 584 ? 1.2661 1.1876 1.2084 -0.0335 -0.0452 0.0597  888  VAL   B CA  
6918  C  C   . VAL   B 584 ? 1.2590 1.1650 1.1834 -0.0291 -0.0435 0.0629  888  VAL   B C   
6919  O  O   . VAL   B 584 ? 1.3594 1.2538 1.2747 -0.0294 -0.0365 0.0659  888  VAL   B O   
6920  C  CB  . VAL   B 584 ? 1.2967 1.2160 1.2523 -0.0401 -0.0381 0.0597  888  VAL   B CB  
6921  C  CG1 . VAL   B 584 ? 1.2359 1.1481 1.1964 -0.0417 -0.0376 0.0594  888  VAL   B CG1 
6922  C  CG2 . VAL   B 584 ? 1.2339 1.1683 1.2056 -0.0438 -0.0400 0.0565  888  VAL   B CG2 
6923  N  N   . ARG   B 585 ? 1.2640 1.1692 1.1826 -0.0247 -0.0497 0.0625  889  ARG   B N   
6924  C  CA  . ARG   B 585 ? 1.3303 1.2222 1.2309 -0.0193 -0.0498 0.0652  889  ARG   B CA  
6925  C  C   . ARG   B 585 ? 1.3251 1.2069 1.2258 -0.0198 -0.0484 0.0658  889  ARG   B C   
6926  O  O   . ARG   B 585 ? 1.3050 1.1935 1.2161 -0.0208 -0.0528 0.0633  889  ARG   B O   
6927  C  CB  . ARG   B 585 ? 1.3012 1.2000 1.1944 -0.0131 -0.0584 0.0642  889  ARG   B CB  
6928  C  CG  . ARG   B 585 ? 1.2816 1.1706 1.1618 -0.0075 -0.0614 0.0656  889  ARG   B CG  
6929  C  CD  . ARG   B 585 ? 1.2301 1.1253 1.1023 -0.0014 -0.0686 0.0650  889  ARG   B CD  
6930  N  NE  . ARG   B 585 ? 1.2111 1.1063 1.0771 -0.0012 -0.0668 0.0659  889  ARG   B NE  
6931  C  CZ  . ARG   B 585 ? 1.2976 1.2000 1.1593 0.0028  -0.0726 0.0650  889  ARG   B CZ  
6932  N  NH1 . ARG   B 585 ? 1.3052 1.2155 1.1682 0.0070  -0.0803 0.0635  889  ARG   B NH1 
6933  N  NH2 . ARG   B 585 ? 1.3545 1.2562 1.2109 0.0025  -0.0707 0.0656  889  ARG   B NH2 
6934  N  N   . LEU   B 586 ? 1.3042 1.1693 1.1928 -0.0190 -0.0423 0.0692  890  LEU   B N   
6935  C  CA  . LEU   B 586 ? 1.3382 1.1922 1.2259 -0.0195 -0.0406 0.0700  890  LEU   B CA  
6936  C  C   . LEU   B 586 ? 1.3462 1.1910 1.2162 -0.0123 -0.0447 0.0716  890  LEU   B C   
6937  O  O   . LEU   B 586 ? 1.3729 1.2106 1.2271 -0.0080 -0.0438 0.0739  890  LEU   B O   
6938  C  CB  . LEU   B 586 ? 1.3417 1.1827 1.2301 -0.0241 -0.0303 0.0727  890  LEU   B CB  
6939  C  CG  . LEU   B 586 ? 1.3579 1.1876 1.2477 -0.0257 -0.0281 0.0735  890  LEU   B CG  
6940  C  CD1 . LEU   B 586 ? 1.3051 1.1442 1.2054 -0.0255 -0.0364 0.0698  890  LEU   B CD1 
6941  C  CD2 . LEU   B 586 ? 1.3707 1.1943 1.2713 -0.0327 -0.0184 0.0747  890  LEU   B CD2 
6942  N  N   . TYR   B 587 ? 1.2956 1.1402 1.1680 -0.0108 -0.0494 0.0702  891  TYR   B N   
6943  C  CA  . TYR   B 587 ? 1.3182 1.1571 1.1763 -0.0036 -0.0547 0.0710  891  TYR   B CA  
6944  C  C   . TYR   B 587 ? 1.3874 1.2112 1.2406 -0.0036 -0.0520 0.0725  891  TYR   B C   
6945  O  O   . TYR   B 587 ? 1.3773 1.2005 1.2428 -0.0088 -0.0496 0.0714  891  TYR   B O   
6946  C  CB  . TYR   B 587 ? 1.3485 1.2023 1.2135 -0.0007 -0.0639 0.0678  891  TYR   B CB  
6947  C  CG  . TYR   B 587 ? 1.3393 1.2054 1.2024 0.0028  -0.0690 0.0668  891  TYR   B CG  
6948  C  CD1 . TYR   B 587 ? 1.3537 1.2143 1.2008 0.0087  -0.0709 0.0687  891  TYR   B CD1 
6949  C  CD2 . TYR   B 587 ? 1.3179 1.2010 1.1955 0.0003  -0.0726 0.0638  891  TYR   B CD2 
6950  C  CE1 . TYR   B 587 ? 1.3478 1.2201 1.1946 0.0118  -0.0763 0.0675  891  TYR   B CE1 
6951  C  CE2 . TYR   B 587 ? 1.3461 1.2407 1.2232 0.0033  -0.0774 0.0629  891  TYR   B CE2 
6952  C  CZ  . TYR   B 587 ? 1.3393 1.2288 1.2015 0.0088  -0.0794 0.0646  891  TYR   B CZ  
6953  O  OH  . TYR   B 587 ? 1.2481 1.1498 1.1119 0.0113  -0.0845 0.0633  891  TYR   B OH  
6954  N  N   . GLU   B 588 ? 1.4486 1.2599 1.2835 0.0026  -0.0528 0.0749  892  GLU   B N   
6955  C  CA  . GLU   B 588 ? 1.4257 1.2218 1.2535 0.0038  -0.0511 0.0764  892  GLU   B CA  
6956  C  C   . GLU   B 588 ? 1.3930 1.1894 1.2115 0.0113  -0.0591 0.0757  892  GLU   B C   
6957  O  O   . GLU   B 588 ? 1.4349 1.2371 1.2457 0.0168  -0.0642 0.0756  892  GLU   B O   
6958  C  CB  . GLU   B 588 ? 1.3722 1.1491 1.1853 0.0042  -0.0427 0.0807  892  GLU   B CB  
6959  C  CG  . GLU   B 588 ? 1.5193 1.2901 1.3424 -0.0037 -0.0332 0.0818  892  GLU   B CG  
6960  C  CD  . GLU   B 588 ? 1.6502 1.4029 1.4580 -0.0030 -0.0239 0.0864  892  GLU   B CD  
6961  O  OE1 . GLU   B 588 ? 1.6715 1.4114 1.4809 -0.0069 -0.0163 0.0884  892  GLU   B OE1 
6962  O  OE2 . GLU   B 588 ? 1.6551 1.4062 1.4492 0.0016  -0.0243 0.0878  892  GLU   B OE2 
6963  N  N   . TRP   B 589 ? 1.3903 1.1805 1.2102 0.0114  -0.0604 0.0751  893  TRP   B N   
6964  C  CA  . TRP   B 589 ? 1.4954 1.2847 1.3070 0.0184  -0.0675 0.0745  893  TRP   B CA  
6965  C  C   . TRP   B 589 ? 1.6114 1.3820 1.4025 0.0236  -0.0650 0.0781  893  TRP   B C   
6966  O  O   . TRP   B 589 ? 1.5966 1.3518 1.3837 0.0208  -0.0585 0.0802  893  TRP   B O   
6967  C  CB  . TRP   B 589 ? 1.4329 1.2238 1.2552 0.0163  -0.0702 0.0720  893  TRP   B CB  
6968  C  CG  . TRP   B 589 ? 1.4426 1.2391 1.2623 0.0226  -0.0784 0.0703  893  TRP   B CG  
6969  C  CD1 . TRP   B 589 ? 1.4768 1.2659 1.2946 0.0245  -0.0807 0.0696  893  TRP   B CD1 
6970  C  CD2 . TRP   B 589 ? 1.4707 1.2813 1.2903 0.0278  -0.0850 0.0689  893  TRP   B CD2 
6971  N  NE1 . TRP   B 589 ? 1.4919 1.2894 1.3078 0.0309  -0.0881 0.0680  893  TRP   B NE1 
6972  C  CE2 . TRP   B 589 ? 1.4963 1.3074 1.3138 0.0329  -0.0908 0.0676  893  TRP   B CE2 
6973  C  CE3 . TRP   B 589 ? 1.5398 1.3624 1.3611 0.0287  -0.0866 0.0686  893  TRP   B CE3 
6974  C  CZ2 . TRP   B 589 ? 1.4872 1.3107 1.3050 0.0388  -0.0975 0.0662  893  TRP   B CZ2 
6975  C  CZ3 . TRP   B 589 ? 1.5710 1.4060 1.3928 0.0342  -0.0937 0.0671  893  TRP   B CZ3 
6976  C  CH2 . TRP   B 589 ? 1.5357 1.3712 1.3561 0.0392  -0.0988 0.0660  893  TRP   B CH2 
6977  N  N   . THR   B 590 ? 1.6351 1.4065 1.4133 0.0310  -0.0698 0.0787  894  THR   B N   
6978  C  CA  . THR   B 590 ? 1.7044 1.4577 1.4617 0.0366  -0.0678 0.0821  894  THR   B CA  
6979  C  C   . THR   B 590 ? 1.7283 1.4735 1.4786 0.0415  -0.0717 0.0820  894  THR   B C   
6980  O  O   . THR   B 590 ? 1.6713 1.4264 1.4314 0.0420  -0.0771 0.0793  894  THR   B O   
6981  C  CB  . THR   B 590 ? 1.7417 1.4982 1.4874 0.0428  -0.0717 0.0827  894  THR   B CB  
6982  O  OG1 . THR   B 590 ? 1.7378 1.5115 1.4906 0.0465  -0.0806 0.0798  894  THR   B OG1 
6983  C  CG2 . THR   B 590 ? 1.6285 1.3870 1.3755 0.0388  -0.0665 0.0836  894  THR   B CG2 
6984  N  N   . THR   B 591 ? 1.7674 1.4937 1.4994 0.0456  -0.0687 0.0852  895  THR   B N   
6985  C  CA  . THR   B 591 ? 1.8420 1.5591 1.5649 0.0511  -0.0723 0.0855  895  THR   B CA  
6986  C  C   . THR   B 591 ? 1.8467 1.5770 1.5697 0.0581  -0.0821 0.0832  895  THR   B C   
6987  O  O   . THR   B 591 ? 1.7906 1.5212 1.5145 0.0612  -0.0864 0.0819  895  THR   B O   
6988  C  CB  . THR   B 591 ? 1.8747 1.5697 1.5758 0.0555  -0.0680 0.0893  895  THR   B CB  
6989  O  OG1 . THR   B 591 ? 1.9293 1.6254 1.6178 0.0618  -0.0712 0.0902  895  THR   B OG1 
6990  C  CG2 . THR   B 591 ? 1.8289 1.5112 1.5303 0.0485  -0.0573 0.0919  895  THR   B CG2 
6991  N  N   . GLU   B 592 ? 1.9277 1.6690 1.6500 0.0608  -0.0856 0.0826  896  GLU   B N   
6992  C  CA  . GLU   B 592 ? 1.9287 1.6832 1.6521 0.0674  -0.0946 0.0806  896  GLU   B CA  
6993  C  C   . GLU   B 592 ? 1.8570 1.6326 1.6007 0.0638  -0.0982 0.0772  896  GLU   B C   
6994  O  O   . GLU   B 592 ? 1.8615 1.6511 1.6091 0.0680  -0.1047 0.0756  896  GLU   B O   
6995  C  CB  . GLU   B 592 ? 1.9452 1.6997 1.6571 0.0726  -0.0971 0.0817  896  GLU   B CB  
6996  C  CG  . GLU   B 592 ? 1.9581 1.6928 1.6475 0.0796  -0.0968 0.0845  896  GLU   B CG  
6997  C  CD  . GLU   B 592 ? 2.0029 1.7326 1.6878 0.0850  -0.1008 0.0843  896  GLU   B CD  
6998  O  OE1 . GLU   B 592 ? 2.0440 1.7627 1.7285 0.0820  -0.0963 0.0852  896  GLU   B OE1 
6999  O  OE2 . GLU   B 592 ? 1.9977 1.7348 1.6803 0.0922  -0.1084 0.0831  896  GLU   B OE2 
7000  N  N   . LYS   B 593 ? 1.7315 1.5094 1.4882 0.0564  -0.0942 0.0761  897  LYS   B N   
7001  C  CA  . LYS   B 593 ? 1.6576 1.4531 1.4324 0.0533  -0.0977 0.0729  897  LYS   B CA  
7002  C  C   . LYS   B 593 ? 1.7580 1.5705 1.5409 0.0526  -0.1001 0.0716  897  LYS   B C   
7003  O  O   . LYS   B 593 ? 1.6813 1.5084 1.4709 0.0558  -0.1061 0.0696  897  LYS   B O   
7004  C  CB  . LYS   B 593 ? 1.4960 1.2944 1.2706 0.0591  -0.1038 0.0714  897  LYS   B CB  
7005  N  N   . GLU   B 594 ? 1.7386 1.5486 1.5206 0.0483  -0.0951 0.0728  898  GLU   B N   
7006  C  CA  . GLU   B 594 ? 1.7283 1.5529 1.5180 0.0467  -0.0967 0.0716  898  GLU   B CA  
7007  C  C   . GLU   B 594 ? 1.7327 1.5555 1.5285 0.0388  -0.0894 0.0722  898  GLU   B C   
7008  O  O   . GLU   B 594 ? 1.7231 1.5323 1.5156 0.0353  -0.0831 0.0739  898  GLU   B O   
7009  C  CB  . GLU   B 594 ? 1.7647 1.5880 1.5414 0.0533  -0.1004 0.0728  898  GLU   B CB  
7010  C  CG  . GLU   B 594 ? 1.8407 1.6450 1.5997 0.0546  -0.0953 0.0760  898  GLU   B CG  
7011  C  CD  . GLU   B 594 ? 2.0043 1.8095 1.7535 0.0588  -0.0980 0.0766  898  GLU   B CD  
7012  O  OE1 . GLU   B 594 ? 2.0378 1.8565 1.7915 0.0627  -0.1052 0.0747  898  GLU   B OE1 
7013  O  OE2 . GLU   B 594 ? 2.0794 1.8715 1.8166 0.0583  -0.0928 0.0790  898  GLU   B OE2 
7014  N  N   . LEU   B 595 ? 1.6404 1.4770 1.4457 0.0360  -0.0902 0.0708  899  LEU   B N   
7015  C  CA  . LEU   B 595 ? 1.5603 1.3978 1.3739 0.0285  -0.0837 0.0709  899  LEU   B CA  
7016  C  C   . LEU   B 595 ? 1.5386 1.3695 1.3409 0.0292  -0.0802 0.0731  899  LEU   B C   
7017  O  O   . LEU   B 595 ? 1.5775 1.4154 1.3759 0.0330  -0.0848 0.0726  899  LEU   B O   
7018  C  CB  . LEU   B 595 ? 1.4986 1.3552 1.3307 0.0243  -0.0864 0.0677  899  LEU   B CB  
7019  C  CG  . LEU   B 595 ? 1.4785 1.3386 1.3246 0.0195  -0.0855 0.0657  899  LEU   B CG  
7020  C  CD1 . LEU   B 595 ? 1.4139 1.2929 1.2751 0.0180  -0.0900 0.0626  899  LEU   B CD1 
7021  C  CD2 . LEU   B 595 ? 1.4721 1.3246 1.3232 0.0122  -0.0775 0.0667  899  LEU   B CD2 
7022  N  N   . ARG   B 596 ? 1.4875 1.3047 1.2850 0.0254  -0.0720 0.0755  900  ARG   B N   
7023  C  CA  . ARG   B 596 ? 1.5061 1.3148 1.2921 0.0258  -0.0673 0.0779  900  ARG   B CA  
7024  C  C   . ARG   B 596 ? 1.3718 1.1862 1.1707 0.0181  -0.0611 0.0774  900  ARG   B C   
7025  O  O   . ARG   B 596 ? 1.3887 1.2054 1.2011 0.0123  -0.0579 0.0765  900  ARG   B O   
7026  C  CB  . ARG   B 596 ? 1.4478 1.2339 1.2154 0.0285  -0.0617 0.0816  900  ARG   B CB  
7027  N  N   . THR   B 597 ? 1.3504 1.1665 1.1449 0.0182  -0.0596 0.0780  901  THR   B N   
7028  C  CA  . THR   B 597 ? 1.4069 1.2298 1.2134 0.0115  -0.0542 0.0775  901  THR   B CA  
7029  C  C   . THR   B 597 ? 1.3805 1.1867 1.1794 0.0087  -0.0437 0.0809  901  THR   B C   
7030  O  O   . THR   B 597 ? 1.4280 1.2231 1.2102 0.0123  -0.0410 0.0833  901  THR   B O   
7031  C  CB  . THR   B 597 ? 1.3828 1.2168 1.1891 0.0130  -0.0583 0.0761  901  THR   B CB  
7032  O  OG1 . THR   B 597 ? 1.3921 1.2398 1.2033 0.0167  -0.0680 0.0734  901  THR   B OG1 
7033  C  CG2 . THR   B 597 ? 1.3428 1.1861 1.1637 0.0060  -0.0535 0.0750  901  THR   B CG2 
7034  N  N   . GLU   B 598 ? 1.3789 1.1834 1.1901 0.0022  -0.0375 0.0810  902  GLU   B N   
7035  C  CA  . GLU   B 598 ? 1.4403 1.2303 1.2471 -0.0012 -0.0266 0.0843  902  GLU   B CA  
7036  C  C   . GLU   B 598 ? 1.4863 1.2812 1.2955 -0.0037 -0.0224 0.0845  902  GLU   B C   
7037  O  O   . GLU   B 598 ? 1.5397 1.3244 1.3326 -0.0002 -0.0191 0.0870  902  GLU   B O   
7038  C  CB  . GLU   B 598 ? 1.4986 1.2864 1.3204 -0.0078 -0.0214 0.0841  902  GLU   B CB  
7039  C  CG  . GLU   B 598 ? 1.5406 1.3158 1.3619 -0.0124 -0.0091 0.0874  902  GLU   B CG  
7040  C  CD  . GLU   B 598 ? 1.5261 1.2934 1.3575 -0.0177 -0.0034 0.0881  902  GLU   B CD  
7041  O  OE1 . GLU   B 598 ? 1.4604 1.2218 1.2981 -0.0230 0.0063  0.0900  902  GLU   B OE1 
7042  O  OE2 . GLU   B 598 ? 1.5566 1.3231 1.3898 -0.0166 -0.0086 0.0868  902  GLU   B OE2 
7043  N  N   . CYS   B 599 ? 1.4632 1.2734 1.2923 -0.0095 -0.0227 0.0819  903  CYS   B N   
7044  C  CA  . CYS   B 599 ? 1.4710 1.2867 1.3045 -0.0125 -0.0185 0.0819  903  CYS   B CA  
7045  C  C   . CYS   B 599 ? 1.4774 1.3141 1.3266 -0.0144 -0.0257 0.0778  903  CYS   B C   
7046  O  O   . CYS   B 599 ? 1.4324 1.2792 1.2928 -0.0152 -0.0319 0.0751  903  CYS   B O   
7047  C  CB  . CYS   B 599 ? 1.5224 1.3318 1.3652 -0.0191 -0.0076 0.0836  903  CYS   B CB  
7048  S  SG  . CYS   B 599 ? 1.4736 1.2861 1.3350 -0.0244 -0.0082 0.0817  903  CYS   B SG  
7049  N  N   . ASN   B 600 ? 1.5466 1.3889 1.3955 -0.0150 -0.0246 0.0775  904  ASN   B N   
7050  C  CA  . ASN   B 600 ? 1.4799 1.3410 1.3436 -0.0175 -0.0296 0.0741  904  ASN   B CA  
7051  C  C   . ASN   B 600 ? 1.4666 1.3307 1.3417 -0.0236 -0.0220 0.0742  904  ASN   B C   
7052  O  O   . ASN   B 600 ? 1.5130 1.3649 1.3804 -0.0244 -0.0132 0.0772  904  ASN   B O   
7053  C  CB  . ASN   B 600 ? 1.4682 1.3350 1.3220 -0.0123 -0.0365 0.0732  904  ASN   B CB  
7054  C  CG  . ASN   B 600 ? 1.4617 1.3342 1.3132 -0.0075 -0.0462 0.0715  904  ASN   B CG  
7055  O  OD1 . ASN   B 600 ? 1.4430 1.3253 1.3076 -0.0093 -0.0502 0.0692  904  ASN   B OD1 
7056  N  ND2 . ASN   B 600 ? 1.4906 1.3568 1.3252 -0.0010 -0.0502 0.0726  904  ASN   B ND2 
7057  N  N   . HIS   B 601 ? 1.4041 1.2844 1.2975 -0.0276 -0.0252 0.0709  905  HIS   B N   
7058  C  CA  . HIS   B 601 ? 1.3558 1.2417 1.2609 -0.0329 -0.0194 0.0704  905  HIS   B CA  
7059  C  C   . HIS   B 601 ? 1.2885 1.1916 1.2022 -0.0331 -0.0262 0.0671  905  HIS   B C   
7060  O  O   . HIS   B 601 ? 1.2929 1.2076 1.2177 -0.0338 -0.0328 0.0642  905  HIS   B O   
7061  C  CB  . HIS   B 601 ? 1.3185 1.2053 1.2410 -0.0391 -0.0145 0.0698  905  HIS   B CB  
7062  C  CG  . HIS   B 601 ? 1.3272 1.2171 1.2603 -0.0441 -0.0072 0.0699  905  HIS   B CG  
7063  N  ND1 . HIS   B 601 ? 1.3246 1.2290 1.2677 -0.0459 -0.0102 0.0673  905  HIS   B ND1 
7064  C  CD2 . HIS   B 601 ? 1.3819 1.2622 1.3169 -0.0475 0.0033  0.0726  905  HIS   B CD2 
7065  C  CE1 . HIS   B 601 ? 1.3295 1.2333 1.2804 -0.0501 -0.0022 0.0681  905  HIS   B CE1 
7066  N  NE2 . HIS   B 601 ? 1.3152 1.2047 1.2618 -0.0512 0.0062  0.0714  905  HIS   B NE2 
7067  N  N   . TYR   B 602 ? 1.3390 1.2431 1.2472 -0.0325 -0.0242 0.0677  906  TYR   B N   
7068  C  CA  . TYR   B 602 ? 1.3119 1.2305 1.2252 -0.0320 -0.0305 0.0649  906  TYR   B CA  
7069  C  C   . TYR   B 602 ? 1.2851 1.2125 1.2145 -0.0378 -0.0262 0.0635  906  TYR   B C   
7070  O  O   . TYR   B 602 ? 1.3149 1.2354 1.2420 -0.0397 -0.0181 0.0655  906  TYR   B O   
7071  C  CB  . TYR   B 602 ? 1.2771 1.1905 1.1728 -0.0271 -0.0321 0.0662  906  TYR   B CB  
7072  C  CG  . TYR   B 602 ? 1.3369 1.2406 1.2160 -0.0210 -0.0362 0.0677  906  TYR   B CG  
7073  C  CD1 . TYR   B 602 ? 1.3575 1.2699 1.2364 -0.0173 -0.0459 0.0656  906  TYR   B CD1 
7074  C  CD2 . TYR   B 602 ? 1.3561 1.2416 1.2197 -0.0186 -0.0301 0.0712  906  TYR   B CD2 
7075  C  CE1 . TYR   B 602 ? 1.3950 1.2991 1.2593 -0.0115 -0.0501 0.0668  906  TYR   B CE1 
7076  C  CE2 . TYR   B 602 ? 1.3107 1.1870 1.1583 -0.0125 -0.0343 0.0725  906  TYR   B CE2 
7077  C  CZ  . TYR   B 602 ? 1.3251 1.2112 1.1737 -0.0090 -0.0446 0.0701  906  TYR   B CZ  
7078  O  OH  . TYR   B 602 ? 1.2384 1.1172 1.0730 -0.0029 -0.0496 0.0710  906  TYR   B OH  
7079  N  N   . ASN   B 603 ? 1.2566 1.1985 1.2017 -0.0403 -0.0314 0.0602  907  ASN   B N   
7080  C  CA  . ASN   B 603 ? 1.2733 1.2240 1.2344 -0.0455 -0.0281 0.0585  907  ASN   B CA  
7081  C  C   . ASN   B 603 ? 1.3222 1.2857 1.2861 -0.0449 -0.0333 0.0562  907  ASN   B C   
7082  O  O   . ASN   B 603 ? 1.2914 1.2587 1.2477 -0.0408 -0.0402 0.0555  907  ASN   B O   
7083  C  CB  . ASN   B 603 ? 1.3188 1.2757 1.2973 -0.0494 -0.0294 0.0562  907  ASN   B CB  
7084  C  CG  . ASN   B 603 ? 1.3225 1.2687 1.2976 -0.0488 -0.0282 0.0577  907  ASN   B CG  
7085  O  OD1 . ASN   B 603 ? 1.2721 1.2165 1.2390 -0.0448 -0.0339 0.0576  907  ASN   B OD1 
7086  N  ND2 . ASN   B 603 ? 1.2311 1.1703 1.2133 -0.0530 -0.0206 0.0589  907  ASN   B ND2 
7087  N  N   . ASN   B 604 ? 1.4172 1.3875 1.3932 -0.0490 -0.0298 0.0549  908  ASN   B N   
7088  C  CA  . ASN   B 604 ? 1.3827 1.3650 1.3634 -0.0493 -0.0336 0.0527  908  ASN   B CA  
7089  C  C   . ASN   B 604 ? 1.3818 1.3780 1.3783 -0.0513 -0.0396 0.0491  908  ASN   B C   
7090  O  O   . ASN   B 604 ? 1.4179 1.4243 1.4217 -0.0527 -0.0414 0.0471  908  ASN   B O   
7091  C  CB  . ASN   B 604 ? 1.4043 1.3853 1.3878 -0.0523 -0.0261 0.0535  908  ASN   B CB  
7092  C  CG  . ASN   B 604 ? 1.4972 1.4756 1.4936 -0.0570 -0.0190 0.0539  908  ASN   B CG  
7093  O  OD1 . ASN   B 604 ? 1.5725 1.5434 1.5690 -0.0575 -0.0171 0.0550  908  ASN   B OD1 
7094  N  ND2 . ASN   B 604 ? 1.4728 1.4574 1.4806 -0.0606 -0.0152 0.0528  908  ASN   B ND2 
7095  N  N   . ILE   B 605 ? 1.2504 1.2465 1.2517 -0.0513 -0.0425 0.0483  909  ILE   B N   
7096  C  CA  . ILE   B 605 ? 1.2105 1.2181 1.2234 -0.0518 -0.0492 0.0451  909  ILE   B CA  
7097  C  C   . ILE   B 605 ? 1.1882 1.1939 1.1937 -0.0476 -0.0550 0.0453  909  ILE   B C   
7098  O  O   . ILE   B 605 ? 1.1965 1.1926 1.1885 -0.0445 -0.0542 0.0477  909  ILE   B O   
7099  C  CB  . ILE   B 605 ? 1.1946 1.2050 1.2240 -0.0565 -0.0469 0.0432  909  ILE   B CB  
7100  C  CG1 . ILE   B 605 ? 1.1519 1.1516 1.1812 -0.0574 -0.0438 0.0446  909  ILE   B CG1 
7101  C  CG2 . ILE   B 605 ? 1.1869 1.1985 1.2235 -0.0604 -0.0405 0.0434  909  ILE   B CG2 
7102  C  CD1 . ILE   B 605 ? 1.0964 1.0970 1.1267 -0.0553 -0.0503 0.0431  909  ILE   B CD1 
7103  N  N   . MET   B 606 ? 1.1176 1.1324 1.1309 -0.0470 -0.0612 0.0427  910  MET   B N   
7104  C  CA  . MET   B 606 ? 1.0847 1.0981 1.0926 -0.0431 -0.0664 0.0427  910  MET   B CA  
7105  C  C   . MET   B 606 ? 1.1196 1.1275 1.1334 -0.0448 -0.0654 0.0422  910  MET   B C   
7106  O  O   . MET   B 606 ? 1.1016 1.1141 1.1284 -0.0483 -0.0651 0.0399  910  MET   B O   
7107  C  CB  . MET   B 606 ? 1.0713 1.0969 1.0833 -0.0409 -0.0733 0.0404  910  MET   B CB  
7108  C  CG  . MET   B 606 ? 1.1977 1.2253 1.1992 -0.0367 -0.0768 0.0415  910  MET   B CG  
7109  S  SD  . MET   B 606 ? 1.5639 1.6063 1.5723 -0.0346 -0.0839 0.0390  910  MET   B SD  
7110  C  CE  . MET   B 606 ? 1.1740 1.2188 1.1943 -0.0365 -0.0849 0.0366  910  MET   B CE  
7111  N  N   . ALA   B 607 ? 1.1181 1.1159 1.1225 -0.0423 -0.0652 0.0441  911  ALA   B N   
7112  C  CA  . ALA   B 607 ? 1.1274 1.1183 1.1367 -0.0441 -0.0638 0.0438  911  ALA   B CA  
7113  C  C   . ALA   B 607 ? 1.1757 1.1726 1.1901 -0.0421 -0.0707 0.0411  911  ALA   B C   
7114  O  O   . ALA   B 607 ? 1.2019 1.1938 1.2093 -0.0386 -0.0736 0.0417  911  ALA   B O   
7115  C  CB  . ALA   B 607 ? 1.1204 1.0969 1.1173 -0.0423 -0.0602 0.0470  911  ALA   B CB  
7116  N  N   . LEU   B 608 ? 1.1905 1.1980 1.2170 -0.0442 -0.0732 0.0382  912  LEU   B N   
7117  C  CA  . LEU   B 608 ? 1.1830 1.1958 1.2144 -0.0422 -0.0794 0.0356  912  LEU   B CA  
7118  C  C   . LEU   B 608 ? 1.2332 1.2384 1.2692 -0.0438 -0.0794 0.0346  912  LEU   B C   
7119  O  O   . LEU   B 608 ? 1.2506 1.2538 1.2834 -0.0405 -0.0839 0.0338  912  LEU   B O   
7120  C  CB  . LEU   B 608 ? 1.1375 1.1625 1.1795 -0.0438 -0.0820 0.0327  912  LEU   B CB  
7121  C  CG  . LEU   B 608 ? 1.1349 1.1698 1.1739 -0.0411 -0.0848 0.0326  912  LEU   B CG  
7122  C  CD1 . LEU   B 608 ? 1.1623 1.1961 1.1904 -0.0357 -0.0884 0.0341  912  LEU   B CD1 
7123  C  CD2 . LEU   B 608 ? 1.1722 1.2094 1.2102 -0.0434 -0.0807 0.0339  912  LEU   B CD2 
7124  N  N   . TYR   B 609 ? 1.1916 1.1922 1.2354 -0.0487 -0.0744 0.0346  913  TYR   B N   
7125  C  CA  . TYR   B 609 ? 1.1864 1.1805 1.2375 -0.0511 -0.0745 0.0332  913  TYR   B CA  
7126  C  C   . TYR   B 609 ? 1.1897 1.1708 1.2354 -0.0528 -0.0681 0.0363  913  TYR   B C   
7127  O  O   . TYR   B 609 ? 1.1924 1.1714 1.2367 -0.0550 -0.0618 0.0386  913  TYR   B O   
7128  C  CB  . TYR   B 609 ? 1.1500 1.1502 1.2178 -0.0558 -0.0746 0.0300  913  TYR   B CB  
7129  C  CG  . TYR   B 609 ? 1.0592 1.0714 1.1323 -0.0542 -0.0804 0.0269  913  TYR   B CG  
7130  C  CD1 . TYR   B 609 ? 1.0564 1.0703 1.1281 -0.0506 -0.0871 0.0247  913  TYR   B CD1 
7131  C  CD2 . TYR   B 609 ? 1.0871 1.1083 1.1660 -0.0562 -0.0789 0.0263  913  TYR   B CD2 
7132  C  CE1 . TYR   B 609 ? 1.0756 1.0995 1.1512 -0.0489 -0.0919 0.0221  913  TYR   B CE1 
7133  C  CE2 . TYR   B 609 ? 1.1343 1.1658 1.2174 -0.0546 -0.0839 0.0236  913  TYR   B CE2 
7134  C  CZ  . TYR   B 609 ? 1.0914 1.1241 1.1728 -0.0510 -0.0903 0.0216  913  TYR   B CZ  
7135  O  OH  . TYR   B 609 ? 0.9603 1.0022 1.0450 -0.0491 -0.0948 0.0191  913  TYR   B OH  
7136  N  N   . LEU   B 610 ? 1.1664 1.1383 1.2089 -0.0517 -0.0694 0.0365  914  LEU   B N   
7137  C  CA  . LEU   B 610 ? 1.1330 1.0914 1.1690 -0.0527 -0.0635 0.0397  914  LEU   B CA  
7138  C  C   . LEU   B 610 ? 1.1650 1.1166 1.2096 -0.0555 -0.0641 0.0381  914  LEU   B C   
7139  O  O   . LEU   B 610 ? 1.2610 1.2117 1.3039 -0.0527 -0.0702 0.0362  914  LEU   B O   
7140  C  CB  . LEU   B 610 ? 1.1663 1.1184 1.1844 -0.0470 -0.0647 0.0424  914  LEU   B CB  
7141  C  CG  . LEU   B 610 ? 1.2372 1.1776 1.2445 -0.0471 -0.0575 0.0466  914  LEU   B CG  
7142  C  CD1 . LEU   B 610 ? 1.1865 1.1309 1.1977 -0.0504 -0.0517 0.0476  914  LEU   B CD1 
7143  C  CD2 . LEU   B 610 ? 1.2613 1.1978 1.2510 -0.0408 -0.0601 0.0488  914  LEU   B CD2 
7144  N  N   . LYS   B 611 ? 1.2046 1.1508 1.2582 -0.0608 -0.0577 0.0388  915  LYS   B N   
7145  C  CA  . LYS   B 611 ? 1.2512 1.1891 1.3129 -0.0638 -0.0577 0.0376  915  LYS   B CA  
7146  C  C   . LYS   B 611 ? 1.2609 1.1856 1.3192 -0.0665 -0.0488 0.0414  915  LYS   B C   
7147  O  O   . LYS   B 611 ? 1.2771 1.2005 1.3316 -0.0675 -0.0418 0.0443  915  LYS   B O   
7148  C  CB  . LYS   B 611 ? 1.1594 1.1050 1.2411 -0.0685 -0.0598 0.0335  915  LYS   B CB  
7149  C  CG  . LYS   B 611 ? 1.1397 1.0969 1.2246 -0.0657 -0.0687 0.0295  915  LYS   B CG  
7150  C  CD  . LYS   B 611 ? 1.1375 1.0912 1.2114 -0.0601 -0.0755 0.0288  915  LYS   B CD  
7151  C  CE  . LYS   B 611 ? 1.0891 1.0532 1.1676 -0.0577 -0.0836 0.0247  915  LYS   B CE  
7152  N  NZ  . LYS   B 611 ? 1.1364 1.1030 1.2318 -0.0617 -0.0866 0.0206  915  LYS   B NZ  
7153  N  N   . THR   B 612 ? 1.2541 1.1683 1.3132 -0.0674 -0.0491 0.0413  916  THR   B N   
7154  C  CA  . THR   B 612 ? 1.3150 1.2152 1.3714 -0.0700 -0.0405 0.0449  916  THR   B CA  
7155  C  C   . THR   B 612 ? 1.1862 1.0807 1.2570 -0.0747 -0.0408 0.0427  916  THR   B C   
7156  O  O   . THR   B 612 ? 1.1936 1.0877 1.2655 -0.0730 -0.0485 0.0398  916  THR   B O   
7157  C  CB  . THR   B 612 ? 1.2620 1.1508 1.2968 -0.0646 -0.0395 0.0486  916  THR   B CB  
7158  O  OG1 . THR   B 612 ? 1.2400 1.1211 1.2721 -0.0630 -0.0442 0.0474  916  THR   B OG1 
7159  C  CG2 . THR   B 612 ? 1.3006 1.1973 1.3224 -0.0587 -0.0442 0.0489  916  THR   B CG2 
7160  N  N   . LYS   B 613 ? 1.1864 1.0769 1.2690 -0.0806 -0.0327 0.0440  917  LYS   B N   
7161  C  CA  . LYS   B 613 ? 1.2570 1.1377 1.3503 -0.0851 -0.0304 0.0436  917  LYS   B CA  
7162  C  C   . LYS   B 613 ? 1.4193 1.2854 1.5025 -0.0859 -0.0198 0.0490  917  LYS   B C   
7163  O  O   . LYS   B 613 ? 1.4828 1.3493 1.5669 -0.0879 -0.0113 0.0519  917  LYS   B O   
7164  C  CB  . LYS   B 613 ? 0.9893 0.8774 1.1074 -0.0918 -0.0297 0.0403  917  LYS   B CB  
7165  N  N   . GLY   B 614 ? 1.3033 1.1561 1.3758 -0.0838 -0.0201 0.0506  918  GLY   B N   
7166  C  CA  . GLY   B 614 ? 1.4222 1.2599 1.4830 -0.0839 -0.0102 0.0559  918  GLY   B CA  
7167  C  C   . GLY   B 614 ? 1.5317 1.3685 1.5734 -0.0791 -0.0062 0.0598  918  GLY   B C   
7168  O  O   . GLY   B 614 ? 1.5472 1.3850 1.5728 -0.0728 -0.0122 0.0599  918  GLY   B O   
7169  N  N   . ASP   B 615 ? 1.7192 1.5537 1.7625 -0.0818 0.0038  0.0630  919  ASP   B N   
7170  C  CA  . ASP   B 615 ? 1.7401 1.5731 1.7653 -0.0773 0.0077  0.0665  919  ASP   B CA  
7171  C  C   . ASP   B 615 ? 1.7332 1.5813 1.7661 -0.0784 0.0074  0.0650  919  ASP   B C   
7172  O  O   . ASP   B 615 ? 1.7355 1.5828 1.7555 -0.0754 0.0112  0.0677  919  ASP   B O   
7173  C  CB  . ASP   B 615 ? 1.7934 1.6095 1.8088 -0.0781 0.0198  0.0720  919  ASP   B CB  
7174  C  CG  . ASP   B 615 ? 1.8508 1.6507 1.8469 -0.0736 0.0194  0.0747  919  ASP   B CG  
7175  O  OD1 . ASP   B 615 ? 1.8745 1.6688 1.8762 -0.0752 0.0166  0.0733  919  ASP   B OD1 
7176  O  OD2 . ASP   B 615 ? 1.8948 1.6869 1.8697 -0.0682 0.0220  0.0782  919  ASP   B OD2 
7177  N  N   . PHE   B 616 ? 1.6178 1.4791 1.6708 -0.0822 0.0025  0.0605  920  PHE   B N   
7178  C  CA  . PHE   B 616 ? 1.6146 1.4910 1.6752 -0.0828 0.0008  0.0585  920  PHE   B CA  
7179  C  C   . PHE   B 616 ? 1.5720 1.4585 1.6236 -0.0773 -0.0098 0.0560  920  PHE   B C   
7180  O  O   . PHE   B 616 ? 1.5606 1.4463 1.6088 -0.0747 -0.0175 0.0540  920  PHE   B O   
7181  C  CB  . PHE   B 616 ? 1.6046 1.4903 1.6910 -0.0892 0.0003  0.0548  920  PHE   B CB  
7182  C  CG  . PHE   B 616 ? 1.6614 1.5415 1.7596 -0.0949 0.0118  0.0573  920  PHE   B CG  
7183  C  CD1 . PHE   B 616 ? 1.6736 1.5463 1.7603 -0.0940 0.0221  0.0621  920  PHE   B CD1 
7184  C  CD2 . PHE   B 616 ? 1.6466 1.5288 1.7678 -0.1011 0.0124  0.0547  920  PHE   B CD2 
7185  C  CE1 . PHE   B 616 ? 1.6747 1.5421 1.7726 -0.0992 0.0335  0.0646  920  PHE   B CE1 
7186  C  CE2 . PHE   B 616 ? 1.6405 1.5181 1.7743 -0.1065 0.0234  0.0570  920  PHE   B CE2 
7187  C  CZ  . PHE   B 616 ? 1.6642 1.5344 1.7863 -0.1055 0.0344  0.0621  920  PHE   B CZ  
7188  N  N   . ILE   B 617 ? 1.4075 1.3033 1.4555 -0.0756 -0.0100 0.0560  921  ILE   B N   
7189  C  CA  . ILE   B 617 ? 1.3447 1.2507 1.3851 -0.0707 -0.0191 0.0539  921  ILE   B CA  
7190  C  C   . ILE   B 617 ? 1.3320 1.2534 1.3855 -0.0729 -0.0212 0.0510  921  ILE   B C   
7191  O  O   . ILE   B 617 ? 1.3082 1.2312 1.3649 -0.0752 -0.0144 0.0525  921  ILE   B O   
7192  C  CB  . ILE   B 617 ? 1.3308 1.2309 1.3488 -0.0649 -0.0180 0.0574  921  ILE   B CB  
7193  C  CG1 . ILE   B 617 ? 1.3824 1.2676 1.3870 -0.0620 -0.0174 0.0599  921  ILE   B CG1 
7194  C  CG2 . ILE   B 617 ? 1.2777 1.1902 1.2908 -0.0605 -0.0265 0.0552  921  ILE   B CG2 
7195  C  CD1 . ILE   B 617 ? 1.3326 1.2148 1.3165 -0.0548 -0.0215 0.0615  921  ILE   B CD1 
7196  N  N   . LEU   B 618 ? 1.2689 1.2010 1.3296 -0.0720 -0.0302 0.0469  922  LEU   B N   
7197  C  CA  . LEU   B 618 ? 1.2339 1.1805 1.3062 -0.0735 -0.0332 0.0439  922  LEU   B CA  
7198  C  C   . LEU   B 618 ? 1.2140 1.1687 1.2750 -0.0682 -0.0396 0.0433  922  LEU   B C   
7199  O  O   . LEU   B 618 ? 1.2253 1.1796 1.2789 -0.0642 -0.0461 0.0424  922  LEU   B O   
7200  C  CB  . LEU   B 618 ? 1.2103 1.1630 1.3007 -0.0767 -0.0385 0.0394  922  LEU   B CB  
7201  C  CG  . LEU   B 618 ? 1.1526 1.1188 1.2577 -0.0793 -0.0403 0.0362  922  LEU   B CG  
7202  C  CD1 . LEU   B 618 ? 1.1531 1.1199 1.2592 -0.0817 -0.0315 0.0389  922  LEU   B CD1 
7203  C  CD2 . LEU   B 618 ? 1.0931 1.0614 1.2175 -0.0835 -0.0431 0.0324  922  LEU   B CD2 
7204  N  N   . VAL   B 619 ? 1.1452 1.1070 1.2053 -0.0683 -0.0375 0.0438  923  VAL   B N   
7205  C  CA  . VAL   B 619 ? 1.1410 1.1109 1.1917 -0.0638 -0.0428 0.0434  923  VAL   B CA  
7206  C  C   . VAL   B 619 ? 1.1672 1.1507 1.2302 -0.0659 -0.0450 0.0404  923  VAL   B C   
7207  O  O   . VAL   B 619 ? 1.1833 1.1685 1.2559 -0.0700 -0.0395 0.0404  923  VAL   B O   
7208  C  CB  . VAL   B 619 ? 1.1456 1.1088 1.1794 -0.0609 -0.0383 0.0473  923  VAL   B CB  
7209  C  CG1 . VAL   B 619 ? 1.1135 1.0861 1.1406 -0.0572 -0.0433 0.0465  923  VAL   B CG1 
7210  C  CG2 . VAL   B 619 ? 1.1948 1.1450 1.2147 -0.0577 -0.0375 0.0499  923  VAL   B CG2 
7211  N  N   . GLY   B 620 ? 1.1461 1.1390 1.2089 -0.0630 -0.0527 0.0379  924  GLY   B N   
7212  C  CA  . GLY   B 620 ? 1.0787 1.0841 1.1513 -0.0643 -0.0552 0.0351  924  GLY   B CA  
7213  C  C   . GLY   B 620 ? 1.1179 1.1313 1.1829 -0.0598 -0.0614 0.0344  924  GLY   B C   
7214  O  O   . GLY   B 620 ? 1.1378 1.1484 1.1929 -0.0557 -0.0653 0.0351  924  GLY   B O   
7215  N  N   . ASP   B 621 ? 1.1269 1.1502 1.1969 -0.0607 -0.0622 0.0330  925  ASP   B N   
7216  C  CA  . ASP   B 621 ? 1.0933 1.1251 1.1584 -0.0569 -0.0680 0.0320  925  ASP   B CA  
7217  C  C   . ASP   B 621 ? 1.0595 1.1013 1.1369 -0.0580 -0.0723 0.0283  925  ASP   B C   
7218  O  O   . ASP   B 621 ? 1.0285 1.0704 1.1177 -0.0613 -0.0717 0.0262  925  ASP   B O   
7219  C  CB  . ASP   B 621 ? 1.0277 1.0617 1.0845 -0.0558 -0.0657 0.0340  925  ASP   B CB  
7220  C  CG  . ASP   B 621 ? 1.0745 1.1119 1.1392 -0.0597 -0.0609 0.0336  925  ASP   B CG  
7221  O  OD1 . ASP   B 621 ? 1.0576 1.0948 1.1343 -0.0635 -0.0586 0.0322  925  ASP   B OD1 
7222  O  OD2 . ASP   B 621 ? 1.1346 1.1746 1.1935 -0.0590 -0.0595 0.0347  925  ASP   B OD2 
7223  N  N   . LEU   B 622 ? 1.0402 1.0902 1.1146 -0.0551 -0.0768 0.0274  926  LEU   B N   
7224  C  CA  . LEU   B 622 ? 0.9719 1.0308 1.0555 -0.0552 -0.0812 0.0240  926  LEU   B CA  
7225  C  C   . LEU   B 622 ? 1.0082 1.0718 1.1029 -0.0593 -0.0784 0.0224  926  LEU   B C   
7226  O  O   . LEU   B 622 ? 1.0268 1.0968 1.1301 -0.0596 -0.0820 0.0194  926  LEU   B O   
7227  C  CB  . LEU   B 622 ? 1.0063 1.0723 1.0837 -0.0513 -0.0853 0.0240  926  LEU   B CB  
7228  C  CG  . LEU   B 622 ? 0.9325 1.0045 1.0138 -0.0489 -0.0911 0.0213  926  LEU   B CG  
7229  C  CD1 . LEU   B 622 ? 0.9368 1.0024 1.0151 -0.0464 -0.0940 0.0210  926  LEU   B CD1 
7230  C  CD2 . LEU   B 622 ? 0.9631 1.0422 1.0389 -0.0457 -0.0934 0.0219  926  LEU   B CD2 
7231  N  N   . MET   B 623 ? 1.0559 1.1165 1.1505 -0.0621 -0.0721 0.0244  927  MET   B N   
7232  C  CA  . MET   B 623 ? 1.0098 1.0757 1.1137 -0.0654 -0.0691 0.0233  927  MET   B CA  
7233  C  C   . MET   B 623 ? 1.0364 1.0973 1.1500 -0.0698 -0.0636 0.0234  927  MET   B C   
7234  O  O   . MET   B 623 ? 1.0414 1.1033 1.1593 -0.0725 -0.0583 0.0241  927  MET   B O   
7235  C  CB  . MET   B 623 ? 1.0000 1.0682 1.0957 -0.0646 -0.0664 0.0253  927  MET   B CB  
7236  C  CG  . MET   B 623 ? 1.0822 1.1587 1.1738 -0.0615 -0.0720 0.0243  927  MET   B CG  
7237  S  SD  . MET   B 623 ? 1.0250 1.1071 1.1125 -0.0616 -0.0700 0.0251  927  MET   B SD  
7238  C  CE  . MET   B 623 ? 0.9515 1.0405 1.0540 -0.0653 -0.0687 0.0222  927  MET   B CE  
7239  N  N   . ARG   B 624 ? 0.9980 1.0536 1.1162 -0.0705 -0.0650 0.0225  928  ARG   B N   
7240  C  CA  . ARG   B 624 ? 1.0136 1.0643 1.1430 -0.0748 -0.0604 0.0223  928  ARG   B CA  
7241  C  C   . ARG   B 624 ? 1.0533 1.0972 1.1778 -0.0767 -0.0515 0.0261  928  ARG   B C   
7242  O  O   . ARG   B 624 ? 1.0369 1.0794 1.1718 -0.0806 -0.0458 0.0263  928  ARG   B O   
7243  C  CB  . ARG   B 624 ? 0.9986 1.0570 1.1445 -0.0778 -0.0617 0.0187  928  ARG   B CB  
7244  C  CG  . ARG   B 624 ? 1.0521 1.1062 1.2122 -0.0820 -0.0589 0.0176  928  ARG   B CG  
7245  C  CD  . ARG   B 624 ? 1.1245 1.1868 1.3017 -0.0847 -0.0605 0.0140  928  ARG   B CD  
7246  N  NE  . ARG   B 624 ? 1.1299 1.1892 1.3224 -0.0895 -0.0559 0.0135  928  ARG   B NE  
7247  C  CZ  . ARG   B 624 ? 1.2287 1.2818 1.4215 -0.0922 -0.0471 0.0169  928  ARG   B CZ  
7248  N  NH1 . ARG   B 624 ? 1.2010 1.2483 1.3779 -0.0903 -0.0422 0.0210  928  ARG   B NH1 
7249  N  NH2 . ARG   B 624 ? 1.3193 1.3716 1.5287 -0.0967 -0.0429 0.0160  928  ARG   B NH2 
7250  N  N   . SER   B 625 ? 1.0473 1.0868 1.1557 -0.0735 -0.0504 0.0292  929  SER   B N   
7251  C  CA  . SER   B 625 ? 1.0866 1.1163 1.1868 -0.0742 -0.0426 0.0331  929  SER   B CA  
7252  C  C   . SER   B 625 ? 1.1009 1.1204 1.2004 -0.0748 -0.0411 0.0342  929  SER   B C   
7253  O  O   . SER   B 625 ? 1.1040 1.1214 1.1976 -0.0719 -0.0466 0.0337  929  SER   B O   
7254  C  CB  . SER   B 625 ? 1.1203 1.1482 1.2031 -0.0702 -0.0428 0.0356  929  SER   B CB  
7255  O  OG  . SER   B 625 ? 1.1437 1.1807 1.2267 -0.0696 -0.0445 0.0345  929  SER   B OG  
7256  N  N   . VAL   B 626 ? 1.1593 1.1722 1.2653 -0.0785 -0.0336 0.0357  930  VAL   B N   
7257  C  CA  . VAL   B 626 ? 1.1162 1.1186 1.2224 -0.0797 -0.0313 0.0370  930  VAL   B CA  
7258  C  C   . VAL   B 626 ? 1.1586 1.1495 1.2535 -0.0796 -0.0223 0.0417  930  VAL   B C   
7259  O  O   . VAL   B 626 ? 1.2494 1.2408 1.3447 -0.0809 -0.0159 0.0433  930  VAL   B O   
7260  C  CB  . VAL   B 626 ? 1.0688 1.0727 1.1951 -0.0845 -0.0305 0.0345  930  VAL   B CB  
7261  C  CG1 . VAL   B 626 ? 1.0838 1.0785 1.2094 -0.0847 -0.0319 0.0347  930  VAL   B CG1 
7262  C  CG2 . VAL   B 626 ? 1.0888 1.1054 1.2276 -0.0850 -0.0377 0.0298  930  VAL   B CG2 
7263  N  N   . LEU   B 627 ? 1.1670 1.1471 1.2515 -0.0777 -0.0217 0.0439  931  LEU   B N   
7264  C  CA  . LEU   B 627 ? 1.1725 1.1398 1.2430 -0.0765 -0.0139 0.0485  931  LEU   B CA  
7265  C  C   . LEU   B 627 ? 1.2785 1.2342 1.3478 -0.0772 -0.0122 0.0498  931  LEU   B C   
7266  O  O   . LEU   B 627 ? 1.2348 1.1887 1.2976 -0.0742 -0.0187 0.0490  931  LEU   B O   
7267  C  CB  . LEU   B 627 ? 1.0562 1.0227 1.1073 -0.0710 -0.0169 0.0501  931  LEU   B CB  
7268  C  CG  . LEU   B 627 ? 1.1053 1.0579 1.1370 -0.0677 -0.0120 0.0544  931  LEU   B CG  
7269  C  CD1 . LEU   B 627 ? 1.2238 1.1777 1.2432 -0.0648 -0.0109 0.0558  931  LEU   B CD1 
7270  C  CD2 . LEU   B 627 ? 1.2446 1.1923 1.2656 -0.0636 -0.0181 0.0546  931  LEU   B CD2 
7271  N  N   . LEU   B 628 ? 1.2889 1.2366 1.3649 -0.0811 -0.0032 0.0519  932  LEU   B N   
7272  C  CA  . LEU   B 628 ? 1.2396 1.1756 1.3164 -0.0826 -0.0005 0.0533  932  LEU   B CA  
7273  C  C   . LEU   B 628 ? 1.3023 1.2236 1.3594 -0.0796 0.0064  0.0583  932  LEU   B C   
7274  O  O   . LEU   B 628 ? 1.2863 1.2028 1.3401 -0.0806 0.0154  0.0613  932  LEU   B O   
7275  C  CB  . LEU   B 628 ? 1.2689 1.2053 1.3670 -0.0891 0.0052  0.0524  932  LEU   B CB  
7276  C  CG  . LEU   B 628 ? 1.3688 1.2955 1.4728 -0.0915 0.0060  0.0525  932  LEU   B CG  
7277  C  CD1 . LEU   B 628 ? 1.3311 1.2624 1.4365 -0.0895 -0.0056 0.0486  932  LEU   B CD1 
7278  C  CD2 . LEU   B 628 ? 1.3910 1.3179 1.5171 -0.0982 0.0125  0.0519  932  LEU   B CD2 
7279  N  N   . LEU   B 629 ? 1.3442 1.2579 1.3872 -0.0756 0.0022  0.0592  933  LEU   B N   
7280  C  CA  . LEU   B 629 ? 1.3496 1.2479 1.3730 -0.0722 0.0077  0.0637  933  LEU   B CA  
7281  C  C   . LEU   B 629 ? 1.3695 1.2553 1.3962 -0.0748 0.0123  0.0653  933  LEU   B C   
7282  O  O   . LEU   B 629 ? 1.3999 1.2892 1.4437 -0.0789 0.0101  0.0627  933  LEU   B O   
7283  C  CB  . LEU   B 629 ? 1.3355 1.2335 1.3404 -0.0655 -0.0002 0.0638  933  LEU   B CB  
7284  C  CG  . LEU   B 629 ? 1.2742 1.1840 1.2749 -0.0627 -0.0051 0.0624  933  LEU   B CG  
7285  C  CD1 . LEU   B 629 ? 1.2605 1.1693 1.2437 -0.0561 -0.0124 0.0627  933  LEU   B CD1 
7286  C  CD2 . LEU   B 629 ? 1.2136 1.1206 1.2103 -0.0636 0.0033  0.0649  933  LEU   B CD2 
7287  N  N   . ALA   B 630 ? 1.4517 1.3220 1.4613 -0.0721 0.0184  0.0697  934  ALA   B N   
7288  C  CA  . ALA   B 630 ? 1.4520 1.3083 1.4609 -0.0736 0.0226  0.0717  934  ALA   B CA  
7289  C  C   . ALA   B 630 ? 1.4482 1.2897 1.4317 -0.0677 0.0246  0.0757  934  ALA   B C   
7290  O  O   . ALA   B 630 ? 1.4641 1.3020 1.4335 -0.0645 0.0285  0.0783  934  ALA   B O   
7291  C  CB  . ALA   B 630 ? 1.3680 1.2190 1.3912 -0.0799 0.0339  0.0735  934  ALA   B CB  
7292  N  N   . TYR   B 631 ? 1.4795 1.3124 1.4568 -0.0658 0.0213  0.0759  935  TYR   B N   
7293  C  CA  . TYR   B 631 ? 1.5544 1.3728 1.5076 -0.0598 0.0222  0.0795  935  TYR   B CA  
7294  C  C   . TYR   B 631 ? 1.5579 1.3581 1.5065 -0.0619 0.0340  0.0840  935  TYR   B C   
7295  O  O   . TYR   B 631 ? 1.6357 1.4286 1.5910 -0.0647 0.0355  0.0841  935  TYR   B O   
7296  C  CB  . TYR   B 631 ? 1.5494 1.3683 1.4974 -0.0560 0.0121  0.0774  935  TYR   B CB  
7297  C  CG  . TYR   B 631 ? 1.5536 1.3557 1.4792 -0.0504 0.0133  0.0808  935  TYR   B CG  
7298  C  CD1 . TYR   B 631 ? 1.5556 1.3539 1.4605 -0.0440 0.0121  0.0829  935  TYR   B CD1 
7299  C  CD2 . TYR   B 631 ? 1.5864 1.3762 1.5117 -0.0515 0.0151  0.0819  935  TYR   B CD2 
7300  C  CE1 . TYR   B 631 ? 1.6532 1.4356 1.5373 -0.0385 0.0129  0.0860  935  TYR   B CE1 
7301  C  CE2 . TYR   B 631 ? 1.5339 1.3077 1.4382 -0.0462 0.0163  0.0852  935  TYR   B CE2 
7302  C  CZ  . TYR   B 631 ? 1.5562 1.3264 1.4399 -0.0396 0.0151  0.0872  935  TYR   B CZ  
7303  O  OH  . TYR   B 631 ? 1.5619 1.3161 1.4247 -0.0340 0.0158  0.0902  935  TYR   B OH  
7304  N  N   . LYS   B 632 ? 1.5565 1.3486 1.4932 -0.0604 0.0426  0.0878  936  LYS   B N   
7305  C  CA  . LYS   B 632 ? 1.6153 1.3888 1.5455 -0.0617 0.0549  0.0926  936  LYS   B CA  
7306  C  C   . LYS   B 632 ? 1.6701 1.4280 1.5811 -0.0567 0.0531  0.0948  936  LYS   B C   
7307  O  O   . LYS   B 632 ? 1.6828 1.4348 1.5716 -0.0498 0.0504  0.0964  936  LYS   B O   
7308  C  CB  . LYS   B 632 ? 1.6348 1.4026 1.5536 -0.0600 0.0639  0.0961  936  LYS   B CB  
7309  N  N   . PRO   B 633 ? 1.6832 1.4337 1.6017 -0.0598 0.0543  0.0949  937  PRO   B N   
7310  C  CA  . PRO   B 633 ? 1.6748 1.4129 1.5762 -0.0547 0.0502  0.0961  937  PRO   B CA  
7311  C  C   . PRO   B 633 ? 1.7079 1.4268 1.5830 -0.0491 0.0571  0.1013  937  PRO   B C   
7312  O  O   . PRO   B 633 ? 1.7268 1.4416 1.5824 -0.0419 0.0505  0.1016  937  PRO   B O   
7313  C  CB  . PRO   B 633 ? 1.5730 1.3060 1.4901 -0.0605 0.0525  0.0954  937  PRO   B CB  
7314  C  CG  . PRO   B 633 ? 1.6574 1.4065 1.6018 -0.0676 0.0520  0.0919  937  PRO   B CG  
7315  C  CD  . PRO   B 633 ? 1.6361 1.3899 1.5797 -0.0680 0.0585  0.0935  937  PRO   B CD  
7316  N  N   . MET   B 634 ? 1.6883 1.3946 1.5623 -0.0519 0.0703  0.1055  938  MET   B N   
7317  C  CA  . MET   B 634 ? 1.7681 1.4544 1.6157 -0.0462 0.0776  0.1107  938  MET   B CA  
7318  C  C   . MET   B 634 ? 1.7923 1.4825 1.6220 -0.0394 0.0730  0.1106  938  MET   B C   
7319  O  O   . MET   B 634 ? 1.8193 1.4975 1.6246 -0.0320 0.0708  0.1127  938  MET   B O   
7320  C  CB  . MET   B 634 ? 1.7844 1.4585 1.6362 -0.0508 0.0934  0.1151  938  MET   B CB  
7321  C  CG  . MET   B 634 ? 1.8112 1.4921 1.6923 -0.0600 0.0971  0.1133  938  MET   B CG  
7322  S  SD  . MET   B 634 ? 1.9648 1.6292 1.8513 -0.0653 0.1164  0.1190  938  MET   B SD  
7323  C  CE  . MET   B 634 ? 1.7367 1.4141 1.6611 -0.0760 0.1160  0.1151  938  MET   B CE  
7324  N  N   . GLU   B 635 ? 1.7598 1.4662 1.6012 -0.0416 0.0711  0.1082  939  GLU   B N   
7325  C  CA  . GLU   B 635 ? 1.7380 1.4486 1.5638 -0.0356 0.0662  0.1078  939  GLU   B CA  
7326  C  C   . GLU   B 635 ? 1.7345 1.4557 1.5557 -0.0308 0.0515  0.1040  939  GLU   B C   
7327  O  O   . GLU   B 635 ? 1.7426 1.4590 1.5432 -0.0235 0.0468  0.1047  939  GLU   B O   
7328  C  CB  . GLU   B 635 ? 1.6993 1.4234 1.5390 -0.0395 0.0690  0.1063  939  GLU   B CB  
7329  C  CG  . GLU   B 635 ? 1.7943 1.5286 1.6239 -0.0342 0.0600  0.1041  939  GLU   B CG  
7330  C  CD  . GLU   B 635 ? 1.8511 1.5693 1.6503 -0.0258 0.0605  0.1073  939  GLU   B CD  
7331  O  OE1 . GLU   B 635 ? 1.9246 1.6487 1.7144 -0.0215 0.0549  0.1061  939  GLU   B OE1 
7332  O  OE2 . GLU   B 635 ? 1.8558 1.5551 1.6411 -0.0234 0.0662  0.1110  939  GLU   B OE2 
7333  N  N   . GLY   B 636 ? 1.6909 1.4264 1.5312 -0.0345 0.0440  0.0999  940  GLY   B N   
7334  C  CA  . GLY   B 636 ? 1.6929 1.4402 1.5306 -0.0301 0.0307  0.0964  940  GLY   B CA  
7335  C  C   . GLY   B 636 ? 1.7148 1.4784 1.5559 -0.0291 0.0251  0.0937  940  GLY   B C   
7336  O  O   . GLY   B 636 ? 1.7009 1.4689 1.5308 -0.0232 0.0163  0.0924  940  GLY   B O   
7337  N  N   . ASN   B 637 ? 1.7401 1.5126 1.5966 -0.0346 0.0301  0.0929  941  ASN   B N   
7338  C  CA  . ASN   B 637 ? 1.6985 1.4886 1.5633 -0.0351 0.0246  0.0898  941  ASN   B CA  
7339  C  C   . ASN   B 637 ? 1.6779 1.4820 1.5695 -0.0428 0.0254  0.0868  941  ASN   B C   
7340  O  O   . ASN   B 637 ? 1.6736 1.4730 1.5770 -0.0477 0.0310  0.0874  941  ASN   B O   
7341  C  CB  . ASN   B 637 ? 1.6942 1.4793 1.5463 -0.0328 0.0304  0.0922  941  ASN   B CB  
7342  C  CG  . ASN   B 637 ? 1.7679 1.5389 1.5927 -0.0248 0.0289  0.0948  941  ASN   B CG  
7343  O  OD1 . ASN   B 637 ? 1.7632 1.5318 1.5792 -0.0204 0.0215  0.0942  941  ASN   B OD1 
7344  N  ND2 . ASN   B 637 ? 1.8316 1.5931 1.6425 -0.0225 0.0356  0.0976  941  ASN   B ND2 
7345  N  N   . PHE   B 638 ? 1.5587 1.3800 1.4602 -0.0437 0.0196  0.0835  942  PHE   B N   
7346  C  CA  . PHE   B 638 ? 1.4789 1.3140 1.4048 -0.0503 0.0201  0.0805  942  PHE   B CA  
7347  C  C   . PHE   B 638 ? 1.4849 1.3204 1.4143 -0.0531 0.0290  0.0821  942  PHE   B C   
7348  O  O   . PHE   B 638 ? 1.5003 1.3316 1.4143 -0.0492 0.0309  0.0839  942  PHE   B O   
7349  C  CB  . PHE   B 638 ? 1.4241 1.2778 1.3595 -0.0498 0.0086  0.0758  942  PHE   B CB  
7350  C  CG  . PHE   B 638 ? 1.4117 1.2662 1.3405 -0.0454 -0.0009 0.0743  942  PHE   B CG  
7351  C  CD1 . PHE   B 638 ? 1.4100 1.2628 1.3208 -0.0387 -0.0063 0.0750  942  PHE   B CD1 
7352  C  CD2 . PHE   B 638 ? 1.3519 1.2093 1.2929 -0.0479 -0.0048 0.0720  942  PHE   B CD2 
7353  C  CE1 . PHE   B 638 ? 1.3319 1.1862 1.2374 -0.0346 -0.0148 0.0736  942  PHE   B CE1 
7354  C  CE2 . PHE   B 638 ? 1.3616 1.2196 1.2960 -0.0435 -0.0132 0.0707  942  PHE   B CE2 
7355  C  CZ  . PHE   B 638 ? 1.3800 1.2368 1.2970 -0.0368 -0.0180 0.0716  942  PHE   B CZ  
7356  N  N   . GLU   B 639 ? 1.4642 1.3049 1.4144 -0.0597 0.0341  0.0811  943  GLU   B N   
7357  C  CA  . GLU   B 639 ? 1.3972 1.2398 1.3542 -0.0629 0.0427  0.0822  943  GLU   B CA  
7358  C  C   . GLU   B 639 ? 1.3839 1.2446 1.3652 -0.0681 0.0389  0.0779  943  GLU   B C   
7359  O  O   . GLU   B 639 ? 1.4187 1.2838 1.4168 -0.0722 0.0366  0.0756  943  GLU   B O   
7360  C  CB  . GLU   B 639 ? 1.3806 1.2080 1.3382 -0.0659 0.0559  0.0864  943  GLU   B CB  
7361  N  N   . GLU   B 640 ? 1.3645 1.2348 1.3469 -0.0676 0.0381  0.0768  944  GLU   B N   
7362  C  CA  . GLU   B 640 ? 1.3498 1.2373 1.3534 -0.0718 0.0343  0.0727  944  GLU   B CA  
7363  C  C   . GLU   B 640 ? 1.3234 1.2106 1.3470 -0.0784 0.0429  0.0730  944  GLU   B C   
7364  O  O   . GLU   B 640 ? 1.3982 1.2773 1.4196 -0.0795 0.0538  0.0764  944  GLU   B O   
7365  C  CB  . GLU   B 640 ? 1.3333 1.2288 1.3318 -0.0698 0.0333  0.0721  944  GLU   B CB  
7366  N  N   . ILE   B 641 ? 1.3425 1.2380 1.3856 -0.0824 0.0382  0.0695  945  ILE   B N   
7367  C  CA  . ILE   B 641 ? 1.3804 1.2771 1.4451 -0.0888 0.0452  0.0692  945  ILE   B CA  
7368  C  C   . ILE   B 641 ? 1.4227 1.3347 1.5038 -0.0917 0.0442  0.0662  945  ILE   B C   
7369  O  O   . ILE   B 641 ? 1.4341 1.3456 1.5251 -0.0950 0.0535  0.0677  945  ILE   B O   
7370  C  CB  . ILE   B 641 ? 1.3935 1.2895 1.4713 -0.0919 0.0409  0.0670  945  ILE   B CB  
7371  C  CG1 . ILE   B 641 ? 1.3593 1.2387 1.4209 -0.0893 0.0431  0.0703  945  ILE   B CG1 
7372  C  CG2 . ILE   B 641 ? 1.3771 1.2764 1.4802 -0.0989 0.0468  0.0659  945  ILE   B CG2 
7373  C  CD1 . ILE   B 641 ? 1.4953 1.3695 1.5709 -0.0937 0.0436  0.0695  945  ILE   B CD1 
7374  N  N   . ALA   B 642 ? 1.4858 1.4113 1.5700 -0.0902 0.0333  0.0621  946  ALA   B N   
7375  C  CA  . ALA   B 642 ? 1.4939 1.4340 1.5936 -0.0926 0.0313  0.0589  946  ALA   B CA  
7376  C  C   . ALA   B 642 ? 1.4645 1.4161 1.5593 -0.0891 0.0196  0.0554  946  ALA   B C   
7377  O  O   . ALA   B 642 ? 1.4330 1.3825 1.5166 -0.0855 0.0126  0.0550  946  ALA   B O   
7378  C  CB  . ALA   B 642 ? 1.5561 1.5019 1.6818 -0.0986 0.0320  0.0560  946  ALA   B CB  
7379  N  N   . ARG   B 643 ? 1.4864 1.4502 1.5903 -0.0901 0.0179  0.0530  947  ARG   B N   
7380  C  CA  . ARG   B 643 ? 1.3900 1.3654 1.4909 -0.0872 0.0080  0.0498  947  ARG   B CA  
7381  C  C   . ARG   B 643 ? 1.3822 1.3708 1.5022 -0.0906 0.0065  0.0463  947  ARG   B C   
7382  O  O   . ARG   B 643 ? 1.4235 1.4121 1.5560 -0.0944 0.0140  0.0469  947  ARG   B O   
7383  C  CB  . ARG   B 643 ? 1.1610 1.1341 1.2414 -0.0825 0.0081  0.0521  947  ARG   B CB  
7384  N  N   . ASP   B 644 ? 1.3274 1.3270 1.4499 -0.0890 -0.0032 0.0426  948  ASP   B N   
7385  C  CA  . ASP   B 644 ? 1.3094 1.3216 1.4466 -0.0910 -0.0056 0.0393  948  ASP   B CA  
7386  C  C   . ASP   B 644 ? 1.2755 1.2960 1.4040 -0.0871 -0.0141 0.0373  948  ASP   B C   
7387  O  O   . ASP   B 644 ? 1.2602 1.2792 1.3788 -0.0839 -0.0204 0.0371  948  ASP   B O   
7388  C  CB  . ASP   B 644 ? 1.3486 1.3658 1.5070 -0.0949 -0.0088 0.0356  948  ASP   B CB  
7389  C  CG  . ASP   B 644 ? 1.3877 1.4172 1.5619 -0.0970 -0.0106 0.0322  948  ASP   B CG  
7390  O  OD1 . ASP   B 644 ? 1.3845 1.4153 1.5616 -0.0984 -0.0035 0.0336  948  ASP   B OD1 
7391  O  OD2 . ASP   B 644 ? 1.4298 1.4672 1.6134 -0.0970 -0.0190 0.0280  948  ASP   B OD2 
7392  N  N   . PHE   B 645 ? 1.2224 1.2512 1.3540 -0.0873 -0.0138 0.0362  949  PHE   B N   
7393  C  CA  . PHE   B 645 ? 1.2270 1.2650 1.3536 -0.0843 -0.0216 0.0340  949  PHE   B CA  
7394  C  C   . PHE   B 645 ? 1.2072 1.2563 1.3512 -0.0869 -0.0241 0.0302  949  PHE   B C   
7395  O  O   . PHE   B 645 ? 1.2171 1.2689 1.3673 -0.0888 -0.0187 0.0305  949  PHE   B O   
7396  C  CB  . PHE   B 645 ? 1.2579 1.2943 1.3688 -0.0815 -0.0191 0.0365  949  PHE   B CB  
7397  C  CG  . PHE   B 645 ? 1.3041 1.3290 1.3967 -0.0785 -0.0169 0.0402  949  PHE   B CG  
7398  C  CD1 . PHE   B 645 ? 1.2995 1.3215 1.3847 -0.0759 -0.0227 0.0401  949  PHE   B CD1 
7399  C  CD2 . PHE   B 645 ? 1.2388 1.2552 1.3208 -0.0779 -0.0090 0.0437  949  PHE   B CD2 
7400  C  CE1 . PHE   B 645 ? 1.3125 1.3240 1.3809 -0.0728 -0.0210 0.0434  949  PHE   B CE1 
7401  C  CE2 . PHE   B 645 ? 1.2474 1.2526 1.3118 -0.0747 -0.0073 0.0470  949  PHE   B CE2 
7402  C  CZ  . PHE   B 645 ? 1.3654 1.3684 1.4232 -0.0722 -0.0134 0.0467  949  PHE   B CZ  
7403  N  N   . ASN   B 646 ? 1.1827 1.2377 1.3341 -0.0865 -0.0321 0.0267  950  ASN   B N   
7404  C  CA  . ASN   B 646 ? 1.0870 1.1525 1.2525 -0.0878 -0.0363 0.0227  950  ASN   B CA  
7405  C  C   . ASN   B 646 ? 1.0465 1.1178 1.2051 -0.0841 -0.0454 0.0206  950  ASN   B C   
7406  O  O   . ASN   B 646 ? 1.0748 1.1472 1.2375 -0.0833 -0.0517 0.0181  950  ASN   B O   
7407  C  CB  . ASN   B 646 ? 1.1217 1.1875 1.3056 -0.0914 -0.0365 0.0202  950  ASN   B CB  
7408  C  CG  . ASN   B 646 ? 1.2231 1.2991 1.4201 -0.0919 -0.0429 0.0156  950  ASN   B CG  
7409  O  OD1 . ASN   B 646 ? 1.2297 1.3076 1.4294 -0.0905 -0.0507 0.0126  950  ASN   B OD1 
7410  N  ND2 . ASN   B 646 ? 1.2989 1.3810 1.5032 -0.0933 -0.0397 0.0150  950  ASN   B ND2 
7411  N  N   . PRO   B 647 ? 1.0069 1.0818 1.1551 -0.0816 -0.0461 0.0216  951  PRO   B N   
7412  C  CA  . PRO   B 647 ? 1.0010 1.0794 1.1397 -0.0777 -0.0534 0.0208  951  PRO   B CA  
7413  C  C   . PRO   B 647 ? 1.0108 1.0965 1.1588 -0.0772 -0.0606 0.0167  951  PRO   B C   
7414  O  O   . PRO   B 647 ? 1.0332 1.1248 1.1927 -0.0790 -0.0609 0.0142  951  PRO   B O   
7415  C  CB  . PRO   B 647 ? 1.0402 1.1219 1.1699 -0.0763 -0.0518 0.0222  951  PRO   B CB  
7416  C  CG  . PRO   B 647 ? 1.0347 1.1112 1.1642 -0.0786 -0.0433 0.0246  951  PRO   B CG  
7417  C  CD  . PRO   B 647 ? 1.0592 1.1355 1.2049 -0.0824 -0.0404 0.0232  951  PRO   B CD  
7418  N  N   . ASN   B 648 ? 1.0043 1.0890 1.1464 -0.0742 -0.0665 0.0161  952  ASN   B N   
7419  C  CA  . ASN   B 648 ? 0.9812 1.0700 1.1292 -0.0727 -0.0737 0.0125  952  ASN   B CA  
7420  C  C   . ASN   B 648 ? 1.0172 1.1013 1.1549 -0.0692 -0.0775 0.0135  952  ASN   B C   
7421  O  O   . ASN   B 648 ? 1.0213 1.0982 1.1511 -0.0690 -0.0743 0.0164  952  ASN   B O   
7422  C  CB  . ASN   B 648 ? 0.9538 1.0420 1.1173 -0.0758 -0.0742 0.0097  952  ASN   B CB  
7423  C  CG  . ASN   B 648 ? 0.9824 1.0756 1.1519 -0.0740 -0.0819 0.0055  952  ASN   B CG  
7424  O  OD1 . ASN   B 648 ? 1.0034 1.1014 1.1668 -0.0708 -0.0859 0.0047  952  ASN   B OD1 
7425  N  ND2 . ASN   B 648 ? 0.9806 1.0722 1.1625 -0.0760 -0.0840 0.0027  952  ASN   B ND2 
7426  N  N   . TRP   B 649 ? 0.9435 1.0311 1.0807 -0.0663 -0.0841 0.0111  953  TRP   B N   
7427  C  CA  . TRP   B 649 ? 0.8735 0.9570 1.0017 -0.0627 -0.0878 0.0117  953  TRP   B CA  
7428  C  C   . TRP   B 649 ? 0.9962 1.0725 1.1296 -0.0639 -0.0888 0.0107  953  TRP   B C   
7429  O  O   . TRP   B 649 ? 1.0085 1.0859 1.1530 -0.0655 -0.0913 0.0074  953  TRP   B O   
7430  C  CB  . TRP   B 649 ? 0.8862 0.9754 1.0119 -0.0587 -0.0940 0.0097  953  TRP   B CB  
7431  C  CG  . TRP   B 649 ? 0.9731 1.0699 1.0955 -0.0577 -0.0937 0.0103  953  TRP   B CG  
7432  C  CD1 . TRP   B 649 ? 1.0238 1.1274 1.1513 -0.0572 -0.0964 0.0078  953  TRP   B CD1 
7433  C  CD2 . TRP   B 649 ? 1.1006 1.1985 1.2137 -0.0567 -0.0911 0.0133  953  TRP   B CD2 
7434  N  NE1 . TRP   B 649 ? 1.0331 1.1421 1.1556 -0.0564 -0.0952 0.0092  953  TRP   B NE1 
7435  C  CE2 . TRP   B 649 ? 1.0507 1.1565 1.1646 -0.0561 -0.0922 0.0125  953  TRP   B CE2 
7436  C  CE3 . TRP   B 649 ? 1.0441 1.1368 1.1481 -0.0562 -0.0881 0.0166  953  TRP   B CE3 
7437  C  CZ2 . TRP   B 649 ? 1.0554 1.1641 1.1622 -0.0553 -0.0906 0.0146  953  TRP   B CZ2 
7438  C  CZ3 . TRP   B 649 ? 0.9932 1.0888 1.0897 -0.0551 -0.0869 0.0186  953  TRP   B CZ3 
7439  C  CH2 . TRP   B 649 ? 1.0617 1.1654 1.1601 -0.0548 -0.0883 0.0176  953  TRP   B CH2 
7440  N  N   . MET   B 650 ? 1.0164 1.0850 1.1414 -0.0629 -0.0871 0.0133  954  MET   B N   
7441  C  CA  . MET   B 650 ? 0.9712 1.0314 1.0987 -0.0638 -0.0876 0.0128  954  MET   B CA  
7442  C  C   . MET   B 650 ? 0.9399 0.9966 1.0567 -0.0590 -0.0923 0.0132  954  MET   B C   
7443  O  O   . MET   B 650 ? 0.9773 1.0343 1.0827 -0.0560 -0.0917 0.0158  954  MET   B O   
7444  C  CB  . MET   B 650 ? 0.9865 1.0395 1.1129 -0.0669 -0.0804 0.0160  954  MET   B CB  
7445  C  CG  . MET   B 650 ? 1.0400 1.0837 1.1699 -0.0686 -0.0798 0.0159  954  MET   B CG  
7446  S  SD  . MET   B 650 ? 1.0117 1.0475 1.1436 -0.0731 -0.0698 0.0195  954  MET   B SD  
7447  C  CE  . MET   B 650 ? 1.0524 1.0812 1.1636 -0.0691 -0.0676 0.0240  954  MET   B CE  
7448  N  N   . SER   B 651 ? 0.8886 0.9417 1.0090 -0.0581 -0.0969 0.0106  955  SER   B N   
7449  C  CA  . SER   B 651 ? 0.9770 1.0271 1.0876 -0.0531 -0.1017 0.0106  955  SER   B CA  
7450  C  C   . SER   B 651 ? 1.0991 1.1386 1.2064 -0.0530 -0.1016 0.0115  955  SER   B C   
7451  O  O   . SER   B 651 ? 1.0773 1.1133 1.1752 -0.0486 -0.1048 0.0120  955  SER   B O   
7452  C  CB  . SER   B 651 ? 0.9710 1.0252 1.0856 -0.0506 -0.1084 0.0067  955  SER   B CB  
7453  O  OG  . SER   B 651 ? 1.0025 1.0536 1.1285 -0.0534 -0.1106 0.0034  955  SER   B OG  
7454  N  N   . ALA   B 652 ? 1.0682 1.1021 1.1828 -0.0576 -0.0976 0.0118  956  ALA   B N   
7455  C  CA  . ALA   B 652 ? 1.0133 1.0370 1.1279 -0.0581 -0.0982 0.0117  956  ALA   B CA  
7456  C  C   . ALA   B 652 ? 1.0752 1.0952 1.2008 -0.0641 -0.0926 0.0121  956  ALA   B C   
7457  O  O   . ALA   B 652 ? 1.0413 1.0675 1.1778 -0.0675 -0.0906 0.0109  956  ALA   B O   
7458  C  CB  . ALA   B 652 ? 0.9600 0.9825 1.0780 -0.0559 -0.1059 0.0076  956  ALA   B CB  
7459  N  N   . VAL   B 653 ? 1.1116 1.1212 1.2350 -0.0653 -0.0900 0.0138  957  VAL   B N   
7460  C  CA  . VAL   B 653 ? 1.0848 1.0897 1.2161 -0.0707 -0.0826 0.0156  957  VAL   B CA  
7461  C  C   . VAL   B 653 ? 1.1641 1.1566 1.2926 -0.0713 -0.0815 0.0167  957  VAL   B C   
7462  O  O   . VAL   B 653 ? 1.2083 1.1954 1.3235 -0.0671 -0.0838 0.0182  957  VAL   B O   
7463  C  CB  . VAL   B 653 ? 1.0878 1.0945 1.2115 -0.0709 -0.0756 0.0196  957  VAL   B CB  
7464  C  CG1 . VAL   B 653 ? 1.0739 1.0724 1.1807 -0.0674 -0.0738 0.0233  957  VAL   B CG1 
7465  C  CG2 . VAL   B 653 ? 1.0570 1.0629 1.1919 -0.0765 -0.0680 0.0207  957  VAL   B CG2 
7466  N  N   . GLU   B 654 ? 1.2231 1.2109 1.3646 -0.0765 -0.0780 0.0161  958  GLU   B N   
7467  C  CA  . GLU   B 654 ? 1.2642 1.2400 1.4050 -0.0775 -0.0777 0.0166  958  GLU   B CA  
7468  C  C   . GLU   B 654 ? 1.2856 1.2561 1.4382 -0.0837 -0.0696 0.0182  958  GLU   B C   
7469  O  O   . GLU   B 654 ? 1.2769 1.2542 1.4433 -0.0876 -0.0667 0.0172  958  GLU   B O   
7470  C  CB  . GLU   B 654 ? 1.2577 1.2329 1.4048 -0.0764 -0.0868 0.0119  958  GLU   B CB  
7471  C  CG  . GLU   B 654 ? 1.2604 1.2230 1.4069 -0.0773 -0.0873 0.0120  958  GLU   B CG  
7472  C  CD  . GLU   B 654 ? 1.2863 1.2407 1.4137 -0.0731 -0.0852 0.0160  958  GLU   B CD  
7473  O  OE1 . GLU   B 654 ? 1.2829 1.2410 1.3974 -0.0674 -0.0893 0.0162  958  GLU   B OE1 
7474  O  OE2 . GLU   B 654 ? 1.3235 1.2677 1.4488 -0.0754 -0.0792 0.0189  958  GLU   B OE2 
7475  N  N   . ILE   B 655 ? 1.1933 1.1515 1.3406 -0.0845 -0.0657 0.0209  959  ILE   B N   
7476  C  CA  . ILE   B 655 ? 1.2624 1.2140 1.4203 -0.0903 -0.0572 0.0228  959  ILE   B CA  
7477  C  C   . ILE   B 655 ? 1.2601 1.2091 1.4355 -0.0942 -0.0611 0.0189  959  ILE   B C   
7478  O  O   . ILE   B 655 ? 1.2058 1.1472 1.3772 -0.0926 -0.0663 0.0175  959  ILE   B O   
7479  C  CB  . ILE   B 655 ? 1.2349 1.1738 1.3780 -0.0893 -0.0500 0.0281  959  ILE   B CB  
7480  C  CG1 . ILE   B 655 ? 1.2195 1.1610 1.3449 -0.0849 -0.0473 0.0315  959  ILE   B CG1 
7481  C  CG2 . ILE   B 655 ? 1.2295 1.1616 1.3836 -0.0953 -0.0400 0.0305  959  ILE   B CG2 
7482  C  CD1 . ILE   B 655 ? 1.1519 1.0826 1.2662 -0.0851 -0.0376 0.0369  959  ILE   B CD1 
7483  N  N   . LEU   B 656 ? 1.2350 1.1903 1.4300 -0.0993 -0.0591 0.0168  960  LEU   B N   
7484  C  CA  . LEU   B 656 ? 1.2227 1.1758 1.4369 -0.1038 -0.0622 0.0130  960  LEU   B CA  
7485  C  C   . LEU   B 656 ? 1.2888 1.2292 1.5062 -0.1079 -0.0542 0.0162  960  LEU   B C   
7486  O  O   . LEU   B 656 ? 1.3063 1.2372 1.5221 -0.1077 -0.0577 0.0153  960  LEU   B O   
7487  C  CB  . LEU   B 656 ? 1.2191 1.1837 1.4538 -0.1076 -0.0625 0.0099  960  LEU   B CB  
7488  C  CG  . LEU   B 656 ? 1.2073 1.1821 1.4397 -0.1034 -0.0725 0.0056  960  LEU   B CG  
7489  C  CD1 . LEU   B 656 ? 1.2125 1.1964 1.4671 -0.1069 -0.0764 0.0007  960  LEU   B CD1 
7490  C  CD2 . LEU   B 656 ? 1.1381 1.1065 1.3589 -0.0988 -0.0814 0.0036  960  LEU   B CD2 
7491  N  N   . ASP   B 657 ? 1.3210 1.2608 1.5427 -0.1115 -0.0432 0.0200  961  ASP   B N   
7492  C  CA  . ASP   B 657 ? 1.3374 1.2643 1.5586 -0.1147 -0.0337 0.0242  961  ASP   B CA  
7493  C  C   . ASP   B 657 ? 1.3437 1.2680 1.5505 -0.1133 -0.0233 0.0301  961  ASP   B C   
7494  O  O   . ASP   B 657 ? 1.3802 1.3121 1.5759 -0.1093 -0.0248 0.0306  961  ASP   B O   
7495  C  CB  . ASP   B 657 ? 1.4023 1.3290 1.6497 -0.1220 -0.0301 0.0224  961  ASP   B CB  
7496  C  CG  . ASP   B 657 ? 1.3604 1.2990 1.6237 -0.1253 -0.0258 0.0217  961  ASP   B CG  
7497  O  OD1 . ASP   B 657 ? 1.3434 1.2870 1.5959 -0.1228 -0.0215 0.0244  961  ASP   B OD1 
7498  O  OD2 . ASP   B 657 ? 1.3664 1.3093 1.6536 -0.1303 -0.0271 0.0182  961  ASP   B OD2 
7499  N  N   . ASP   B 658 ? 1.3705 1.2834 1.5765 -0.1161 -0.0129 0.0345  962  ASP   B N   
7500  C  CA  . ASP   B 658 ? 1.4398 1.3485 1.6298 -0.1141 -0.0033 0.0400  962  ASP   B CA  
7501  C  C   . ASP   B 658 ? 1.4493 1.3686 1.6473 -0.1157 0.0019  0.0404  962  ASP   B C   
7502  O  O   . ASP   B 658 ? 1.5109 1.4270 1.6948 -0.1136 0.0093  0.0448  962  ASP   B O   
7503  C  CB  . ASP   B 658 ? 1.5056 1.3986 1.6928 -0.1167 0.0072  0.0447  962  ASP   B CB  
7504  C  CG  . ASP   B 658 ? 1.5612 1.4429 1.7412 -0.1153 0.0026  0.0443  962  ASP   B CG  
7505  O  OD1 . ASP   B 658 ? 1.5289 1.4106 1.7255 -0.1189 -0.0023 0.0406  962  ASP   B OD1 
7506  O  OD2 . ASP   B 658 ? 1.6059 1.4789 1.7633 -0.1103 0.0032  0.0476  962  ASP   B OD2 
7507  N  N   . ASP   B 659 ? 1.3752 1.3062 1.5942 -0.1191 -0.0019 0.0361  963  ASP   B N   
7508  C  CA  . ASP   B 659 ? 1.3785 1.3189 1.6063 -0.1210 0.0038  0.0366  963  ASP   B CA  
7509  C  C   . ASP   B 659 ? 1.3420 1.2974 1.5746 -0.1190 -0.0060 0.0319  963  ASP   B C   
7510  O  O   . ASP   B 659 ? 1.3632 1.3263 1.5924 -0.1176 -0.0036 0.0327  963  ASP   B O   
7511  C  CB  . ASP   B 659 ? 1.4491 1.3890 1.7014 -0.1279 0.0116  0.0366  963  ASP   B CB  
7512  C  CG  . ASP   B 659 ? 1.5328 1.4571 1.7829 -0.1305 0.0212  0.0410  963  ASP   B CG  
7513  O  OD1 . ASP   B 659 ? 1.5406 1.4566 1.7861 -0.1299 0.0163  0.0402  963  ASP   B OD1 
7514  O  OD2 . ASP   B 659 ? 1.5679 1.4874 1.8202 -0.1330 0.0337  0.0453  963  ASP   B OD2 
7515  N  N   . ASN   B 660 ? 1.3725 1.3316 1.6126 -0.1186 -0.0169 0.0269  964  ASN   B N   
7516  C  CA  . ASN   B 660 ? 1.2983 1.2704 1.5422 -0.1164 -0.0267 0.0222  964  ASN   B CA  
7517  C  C   . ASN   B 660 ? 1.2808 1.2529 1.5035 -0.1098 -0.0346 0.0220  964  ASN   B C   
7518  O  O   . ASN   B 660 ? 1.2768 1.2392 1.4869 -0.1075 -0.0360 0.0235  964  ASN   B O   
7519  C  CB  . ASN   B 660 ? 1.2458 1.2222 1.5113 -0.1196 -0.0344 0.0165  964  ASN   B CB  
7520  C  CG  . ASN   B 660 ? 1.2730 1.2512 1.5622 -0.1261 -0.0273 0.0163  964  ASN   B CG  
7521  O  OD1 . ASN   B 660 ? 1.2878 1.2763 1.5888 -0.1276 -0.0260 0.0148  964  ASN   B OD1 
7522  N  ND2 . ASN   B 660 ? 1.3111 1.2790 1.6079 -0.1300 -0.0223 0.0178  964  ASN   B ND2 
7523  N  N   . PHE   B 661 ? 1.3083 1.2914 1.5275 -0.1068 -0.0394 0.0201  965  PHE   B N   
7524  C  CA  . PHE   B 661 ? 1.2801 1.2649 1.4808 -0.1007 -0.0463 0.0199  965  PHE   B CA  
7525  C  C   . PHE   B 661 ? 1.2399 1.2363 1.4477 -0.0990 -0.0559 0.0148  965  PHE   B C   
7526  O  O   . PHE   B 661 ? 1.2167 1.2220 1.4377 -0.1015 -0.0551 0.0129  965  PHE   B O   
7527  C  CB  . PHE   B 661 ? 1.2826 1.2671 1.4657 -0.0977 -0.0404 0.0244  965  PHE   B CB  
7528  C  CG  . PHE   B 661 ? 1.3182 1.2916 1.4958 -0.0996 -0.0297 0.0295  965  PHE   B CG  
7529  C  CD1 . PHE   B 661 ? 1.3332 1.2941 1.5029 -0.0991 -0.0285 0.0315  965  PHE   B CD1 
7530  C  CD2 . PHE   B 661 ? 1.3049 1.2796 1.4845 -0.1018 -0.0205 0.0323  965  PHE   B CD2 
7531  C  CE1 . PHE   B 661 ? 1.3458 1.2955 1.5095 -0.1006 -0.0183 0.0363  965  PHE   B CE1 
7532  C  CE2 . PHE   B 661 ? 1.3450 1.3084 1.5183 -0.1031 -0.0102 0.0371  965  PHE   B CE2 
7533  C  CZ  . PHE   B 661 ? 1.3522 1.3030 1.5174 -0.1025 -0.0091 0.0391  965  PHE   B CZ  
7534  N  N   . LEU   B 662 ? 1.2079 1.2036 1.4066 -0.0947 -0.0647 0.0126  966  LEU   B N   
7535  C  CA  . LEU   B 662 ? 1.1309 1.1356 1.3346 -0.0924 -0.0742 0.0078  966  LEU   B CA  
7536  C  C   . LEU   B 662 ? 1.1188 1.1286 1.3055 -0.0867 -0.0774 0.0088  966  LEU   B C   
7537  O  O   . LEU   B 662 ? 1.0931 1.0974 1.2634 -0.0835 -0.0758 0.0121  966  LEU   B O   
7538  C  CB  . LEU   B 662 ? 1.0829 1.0825 1.2909 -0.0917 -0.0825 0.0039  966  LEU   B CB  
7539  C  CG  . LEU   B 662 ? 1.0570 1.0644 1.2675 -0.0885 -0.0925 -0.0010 966  LEU   B CG  
7540  C  CD1 . LEU   B 662 ? 1.0184 1.0347 1.2483 -0.0923 -0.0930 -0.0043 966  LEU   B CD1 
7541  C  CD2 . LEU   B 662 ? 1.0737 1.0741 1.2821 -0.0861 -0.1009 -0.0042 966  LEU   B CD2 
7542  N  N   . GLY   B 663 ? 1.1141 1.1343 1.3053 -0.0854 -0.0821 0.0058  967  GLY   B N   
7543  C  CA  . GLY   B 663 ? 1.0734 1.0993 1.2506 -0.0805 -0.0847 0.0066  967  GLY   B CA  
7544  C  C   . GLY   B 663 ? 0.9961 1.0309 1.1783 -0.0784 -0.0922 0.0023  967  GLY   B C   
7545  O  O   . GLY   B 663 ? 0.9925 1.0310 1.1900 -0.0811 -0.0945 -0.0012 967  GLY   B O   
7546  N  N   . ALA   B 664 ? 0.9847 1.0226 1.1536 -0.0732 -0.0960 0.0027  968  ALA   B N   
7547  C  CA  . ALA   B 664 ? 0.9964 1.0425 1.1663 -0.0703 -0.1023 -0.0006 968  ALA   B CA  
7548  C  C   . ALA   B 664 ? 1.0410 1.0950 1.2049 -0.0692 -0.0991 0.0016  968  ALA   B C   
7549  O  O   . ALA   B 664 ? 1.0489 1.1017 1.1998 -0.0669 -0.0964 0.0051  968  ALA   B O   
7550  C  CB  . ALA   B 664 ? 0.9796 1.0224 1.1393 -0.0649 -0.1095 -0.0020 968  ALA   B CB  
7551  N  N   . GLU   B 665 ? 1.0170 1.0790 1.1902 -0.0706 -0.0997 -0.0007 969  GLU   B N   
7552  C  CA  . GLU   B 665 ? 1.0556 1.1253 1.2240 -0.0697 -0.0972 0.0009  969  GLU   B CA  
7553  C  C   . GLU   B 665 ? 1.0195 1.0967 1.1917 -0.0676 -0.1030 -0.0027 969  GLU   B C   
7554  O  O   . GLU   B 665 ? 0.9943 1.0710 1.1744 -0.0673 -0.1086 -0.0066 969  GLU   B O   
7555  C  CB  . GLU   B 665 ? 1.0493 1.1207 1.2240 -0.0742 -0.0892 0.0031  969  GLU   B CB  
7556  C  CG  . GLU   B 665 ? 1.0638 1.1389 1.2565 -0.0783 -0.0885 0.0002  969  GLU   B CG  
7557  C  CD  . GLU   B 665 ? 1.1178 1.1943 1.3151 -0.0822 -0.0797 0.0028  969  GLU   B CD  
7558  O  OE1 . GLU   B 665 ? 1.1919 1.2740 1.3846 -0.0814 -0.0774 0.0041  969  GLU   B OE1 
7559  O  OE2 . GLU   B 665 ? 1.1449 1.2164 1.3505 -0.0860 -0.0748 0.0038  969  GLU   B OE2 
7560  N  N   . ASN   B 666 ? 1.0275 1.1112 1.1934 -0.0659 -0.1017 -0.0013 970  ASN   B N   
7561  C  CA  . ASN   B 666 ? 1.0283 1.1192 1.1965 -0.0638 -0.1060 -0.0042 970  ASN   B CA  
7562  C  C   . ASN   B 666 ? 1.0241 1.1187 1.2077 -0.0675 -0.1058 -0.0071 970  ASN   B C   
7563  O  O   . ASN   B 666 ? 1.0149 1.1094 1.2058 -0.0717 -0.0999 -0.0057 970  ASN   B O   
7564  C  CB  . ASN   B 666 ? 0.9215 1.0179 1.0801 -0.0620 -0.1037 -0.0016 970  ASN   B CB  
7565  C  CG  . ASN   B 666 ? 1.0107 1.1145 1.1720 -0.0605 -0.1067 -0.0041 970  ASN   B CG  
7566  O  OD1 . ASN   B 666 ? 1.0063 1.1110 1.1620 -0.0564 -0.1117 -0.0054 970  ASN   B OD1 
7567  N  ND2 . ASN   B 666 ? 1.0540 1.1626 1.2231 -0.0636 -0.1034 -0.0044 970  ASN   B ND2 
7568  N  N   . ALA   B 667 ? 1.0356 1.1331 1.2244 -0.0656 -0.1121 -0.0112 971  ALA   B N   
7569  C  CA  . ALA   B 667 ? 0.9709 1.0665 1.1509 -0.0604 -0.1187 -0.0128 971  ALA   B CA  
7570  C  C   . ALA   B 667 ? 1.0529 1.1424 1.2394 -0.0601 -0.1245 -0.0164 971  ALA   B C   
7571  O  O   . ALA   B 667 ? 1.0211 1.1123 1.2196 -0.0615 -0.1279 -0.0203 971  ALA   B O   
7572  C  CB  . ALA   B 667 ? 0.8224 0.9243 1.0006 -0.0576 -0.1216 -0.0145 971  ALA   B CB  
7573  N  N   . PHE   B 668 ? 1.0287 1.1111 1.2073 -0.0583 -0.1257 -0.0152 972  PHE   B N   
7574  C  CA  . PHE   B 668 ? 0.9445 1.0198 1.1274 -0.0578 -0.1312 -0.0184 972  PHE   B CA  
7575  C  C   . PHE   B 668 ? 0.9728 1.0470 1.1723 -0.0636 -0.1292 -0.0198 972  PHE   B C   
7576  O  O   . PHE   B 668 ? 1.0111 1.0832 1.2208 -0.0642 -0.1347 -0.0241 972  PHE   B O   
7577  C  CB  . PHE   B 668 ? 0.9271 1.0026 1.1086 -0.0532 -0.1395 -0.0227 972  PHE   B CB  
7578  C  CG  . PHE   B 668 ? 0.9702 1.0489 1.1378 -0.0479 -0.1402 -0.0212 972  PHE   B CG  
7579  C  CD1 . PHE   B 668 ? 0.9619 1.0361 1.1160 -0.0436 -0.1412 -0.0193 972  PHE   B CD1 
7580  C  CD2 . PHE   B 668 ? 0.9795 1.0658 1.1483 -0.0474 -0.1395 -0.0217 972  PHE   B CD2 
7581  C  CE1 . PHE   B 668 ? 0.9550 1.0324 1.0977 -0.0389 -0.1413 -0.0178 972  PHE   B CE1 
7582  C  CE2 . PHE   B 668 ? 0.9575 1.0467 1.1144 -0.0429 -0.1397 -0.0202 972  PHE   B CE2 
7583  C  CZ  . PHE   B 668 ? 0.9702 1.0551 1.1146 -0.0387 -0.1405 -0.0183 972  PHE   B CZ  
7584  N  N   . ASN   B 669 ? 0.9685 1.0437 1.1707 -0.0678 -0.1212 -0.0162 973  ASN   B N   
7585  C  CA  . ASN   B 669 ? 0.9937 1.0675 1.2113 -0.0734 -0.1177 -0.0168 973  ASN   B CA  
7586  C  C   . ASN   B 669 ? 1.0022 1.0675 1.2160 -0.0753 -0.1133 -0.0136 973  ASN   B C   
7587  O  O   . ASN   B 669 ? 1.0278 1.0904 1.2272 -0.0731 -0.1105 -0.0099 973  ASN   B O   
7588  C  CB  . ASN   B 669 ? 1.0079 1.0888 1.2330 -0.0769 -0.1110 -0.0152 973  ASN   B CB  
7589  C  CG  . ASN   B 669 ? 1.0236 1.1127 1.2504 -0.0748 -0.1145 -0.0178 973  ASN   B CG  
7590  O  OD1 . ASN   B 669 ? 1.0392 1.1291 1.2707 -0.0728 -0.1221 -0.0221 973  ASN   B OD1 
7591  N  ND2 . ASN   B 669 ? 1.0436 1.1383 1.2657 -0.0751 -0.1093 -0.0151 973  ASN   B ND2 
7592  N  N   . LEU   B 670 ? 0.9957 1.0567 1.2229 -0.0793 -0.1130 -0.0152 974  LEU   B N   
7593  C  CA  . LEU   B 670 ? 0.9627 1.0159 1.1898 -0.0824 -0.1072 -0.0120 974  LEU   B CA  
7594  C  C   . LEU   B 670 ? 1.0094 1.0653 1.2484 -0.0879 -0.0985 -0.0100 974  LEU   B C   
7595  O  O   . LEU   B 670 ? 1.0664 1.1297 1.3173 -0.0898 -0.0982 -0.0120 974  LEU   B O   
7596  C  CB  . LEU   B 670 ? 0.9788 1.0243 1.2130 -0.0833 -0.1126 -0.0151 974  LEU   B CB  
7597  C  CG  . LEU   B 670 ? 0.9613 1.0018 1.1820 -0.0777 -0.1202 -0.0165 974  LEU   B CG  
7598  C  CD1 . LEU   B 670 ? 0.9796 1.0135 1.2106 -0.0790 -0.1262 -0.0206 974  LEU   B CD1 
7599  C  CD2 . LEU   B 670 ? 1.0170 1.0515 1.2216 -0.0759 -0.1156 -0.0117 974  LEU   B CD2 
7600  N  N   . PHE   B 671 ? 1.0279 1.0770 1.2633 -0.0902 -0.0911 -0.0059 975  PHE   B N   
7601  C  CA  . PHE   B 671 ? 1.0621 1.1122 1.3071 -0.0951 -0.0817 -0.0033 975  PHE   B CA  
7602  C  C   . PHE   B 671 ? 1.0836 1.1231 1.3258 -0.0975 -0.0753 0.0003  975  PHE   B C   
7603  O  O   . PHE   B 671 ? 1.0361 1.0686 1.2631 -0.0945 -0.0762 0.0024  975  PHE   B O   
7604  C  CB  . PHE   B 671 ? 1.0797 1.1356 1.3156 -0.0939 -0.0764 -0.0002 975  PHE   B CB  
7605  C  CG  . PHE   B 671 ? 1.0443 1.0945 1.2607 -0.0913 -0.0723 0.0045  975  PHE   B CG  
7606  C  CD1 . PHE   B 671 ? 1.0335 1.0769 1.2474 -0.0938 -0.0632 0.0088  975  PHE   B CD1 
7607  C  CD2 . PHE   B 671 ? 1.0765 1.1277 1.2774 -0.0861 -0.0775 0.0047  975  PHE   B CD2 
7608  C  CE1 . PHE   B 671 ? 1.1195 1.1570 1.3150 -0.0910 -0.0602 0.0129  975  PHE   B CE1 
7609  C  CE2 . PHE   B 671 ? 1.0637 1.1099 1.2478 -0.0836 -0.0744 0.0088  975  PHE   B CE2 
7610  C  CZ  . PHE   B 671 ? 1.0974 1.1368 1.2785 -0.0859 -0.0661 0.0127  975  PHE   B CZ  
7611  N  N   . VAL   B 672 ? 1.1037 1.1419 1.3605 -0.1028 -0.0683 0.0012  976  VAL   B N   
7612  C  CA  . VAL   B 672 ? 1.1443 1.1721 1.4001 -0.1056 -0.0608 0.0049  976  VAL   B CA  
7613  C  C   . VAL   B 672 ? 1.2024 1.2312 1.4623 -0.1089 -0.0494 0.0087  976  VAL   B C   
7614  O  O   . VAL   B 672 ? 1.1514 1.1875 1.4274 -0.1119 -0.0475 0.0069  976  VAL   B O   
7615  C  CB  . VAL   B 672 ? 1.1187 1.1416 1.3907 -0.1092 -0.0639 0.0018  976  VAL   B CB  
7616  C  CG1 . VAL   B 672 ? 1.1371 1.1485 1.4078 -0.1122 -0.0555 0.0060  976  VAL   B CG1 
7617  C  CG2 . VAL   B 672 ? 1.0697 1.0912 1.3366 -0.1053 -0.0757 -0.0022 976  VAL   B CG2 
7618  N  N   . CYS   B 673 ? 1.2653 1.2864 1.5099 -0.1079 -0.0420 0.0139  977  CYS   B N   
7619  C  CA  . CYS   B 673 ? 1.3030 1.3213 1.5495 -0.1109 -0.0301 0.0181  977  CYS   B CA  
7620  C  C   . CYS   B 673 ? 1.3191 1.3242 1.5622 -0.1128 -0.0235 0.0216  977  CYS   B C   
7621  O  O   . CYS   B 673 ? 1.2806 1.2783 1.5130 -0.1105 -0.0277 0.0219  977  CYS   B O   
7622  C  CB  . CYS   B 673 ? 1.3571 1.3779 1.5866 -0.1074 -0.0265 0.0212  977  CYS   B CB  
7623  S  SG  . CYS   B 673 ? 1.4871 1.5017 1.6894 -0.1013 -0.0305 0.0237  977  CYS   B SG  
7624  N  N   . GLN   B 674 ? 1.3710 1.3727 1.6234 -0.1169 -0.0130 0.0244  978  GLN   B N   
7625  C  CA  . GLN   B 674 ? 1.4146 1.4034 1.6662 -0.1194 -0.0055 0.0279  978  GLN   B CA  
7626  C  C   . GLN   B 674 ? 1.4658 1.4486 1.7065 -0.1192 0.0067  0.0336  978  GLN   B C   
7627  O  O   . GLN   B 674 ? 1.4272 1.4167 1.6701 -0.1193 0.0110  0.0343  978  GLN   B O   
7628  C  CB  . GLN   B 674 ? 1.3351 1.3239 1.6123 -0.1254 -0.0039 0.0256  978  GLN   B CB  
7629  C  CG  . GLN   B 674 ? 1.3705 1.3624 1.6625 -0.1296 0.0068  0.0274  978  GLN   B CG  
7630  C  CD  . GLN   B 674 ? 1.3552 1.3496 1.6752 -0.1354 0.0068  0.0242  978  GLN   B CD  
7631  O  OE1 . GLN   B 674 ? 1.2671 1.2628 1.5960 -0.1361 -0.0029 0.0198  978  GLN   B OE1 
7632  N  NE2 . GLN   B 674 ? 1.4335 1.4284 1.7680 -0.1396 0.0177  0.0265  978  GLN   B NE2 
7633  N  N   . LYS   B 675 ? 1.5087 1.4780 1.7366 -0.1185 0.0122  0.0377  979  LYS   B N   
7634  C  CA  . LYS   B 675 ? 1.6092 1.5699 1.8282 -0.1188 0.0249  0.0433  979  LYS   B CA  
7635  C  C   . LYS   B 675 ? 1.7398 1.7042 1.9815 -0.1244 0.0333  0.0434  979  LYS   B C   
7636  O  O   . LYS   B 675 ? 1.7232 1.6914 1.9868 -0.1288 0.0307  0.0400  979  LYS   B O   
7637  C  CB  . LYS   B 675 ? 1.5662 1.5108 1.7720 -0.1181 0.0295  0.0473  979  LYS   B CB  
7638  C  CG  . LYS   B 675 ? 1.6848 1.6179 1.8769 -0.1173 0.0426  0.0535  979  LYS   B CG  
7639  C  CD  . LYS   B 675 ? 1.8107 1.7429 2.0217 -0.1228 0.0542  0.0552  979  LYS   B CD  
7640  C  CE  . LYS   B 675 ? 1.7894 1.7067 1.9873 -0.1224 0.0681  0.0617  979  LYS   B CE  
7641  N  NZ  . LYS   B 675 ? 1.9428 1.8592 2.1620 -0.1282 0.0796  0.0632  979  LYS   B NZ  
7642  N  N   . ASP   B 676 ? 1.9851 1.9489 2.2217 -0.1240 0.0429  0.0469  980  ASP   B N   
7643  C  CA  . ASP   B 676 ? 2.0241 1.9901 2.2809 -0.1289 0.0528  0.0477  980  ASP   B CA  
7644  C  C   . ASP   B 676 ? 2.0557 2.0092 2.3197 -0.1329 0.0615  0.0507  980  ASP   B C   
7645  O  O   . ASP   B 676 ? 2.0854 2.0275 2.3381 -0.1324 0.0730  0.0562  980  ASP   B O   
7646  C  CB  . ASP   B 676 ? 2.0699 2.0363 2.3166 -0.1269 0.0616  0.0512  980  ASP   B CB  
7647  C  CG  . ASP   B 676 ? 2.1075 2.0849 2.3768 -0.1305 0.0656  0.0494  980  ASP   B CG  
7648  O  OD1 . ASP   B 676 ? 2.1105 2.0898 2.4038 -0.1358 0.0680  0.0478  980  ASP   B OD1 
7649  O  OD2 . ASP   B 676 ? 2.0994 2.0834 2.3626 -0.1281 0.0661  0.0494  980  ASP   B OD2 
7650  N  N   . SER   B 677 ? 2.0212 1.9763 2.3038 -0.1367 0.0559  0.0471  981  SER   B N   
7651  C  CA  . SER   B 677 ? 2.0552 1.9991 2.3476 -0.1411 0.0631  0.0493  981  SER   B CA  
7652  C  C   . SER   B 677 ? 2.1456 2.0852 2.4455 -0.1441 0.0789  0.0540  981  SER   B C   
7653  O  O   . SER   B 677 ? 2.1559 2.0818 2.4512 -0.1455 0.0892  0.0587  981  SER   B O   
7654  C  CB  . SER   B 677 ? 2.0049 1.9551 2.3229 -0.1457 0.0549  0.0438  981  SER   B CB  
7655  O  OG  . SER   B 677 ? 1.8548 1.8101 2.1664 -0.1425 0.0401  0.0392  981  SER   B OG  
7656  N  N   . ALA   B 678 ? 2.2807 2.2318 2.5918 -0.1449 0.0812  0.0528  982  ALA   B N   
7657  C  CA  . ALA   B 678 ? 2.3314 2.2800 2.6487 -0.1470 0.0961  0.0570  982  ALA   B CA  
7658  C  C   . ALA   B 678 ? 2.3681 2.3062 2.6552 -0.1416 0.1034  0.0626  982  ALA   B C   
7659  O  O   . ALA   B 678 ? 2.3268 2.2707 2.6029 -0.1380 0.1026  0.0627  982  ALA   B O   
7660  C  CB  . ALA   B 678 ? 2.2309 2.1956 2.5687 -0.1489 0.0947  0.0535  982  ALA   B CB  
7661  N  N   . ALA   B 679 ? 2.2727 2.1945 2.5457 -0.1409 0.1102  0.0672  983  ALA   B N   
7662  C  CA  . ALA   B 679 ? 2.1782 2.0876 2.4216 -0.1356 0.1173  0.0726  983  ALA   B CA  
7663  C  C   . ALA   B 679 ? 2.1953 2.1028 2.4400 -0.1359 0.1315  0.0767  983  ALA   B C   
7664  O  O   . ALA   B 679 ? 2.2233 2.1168 2.4630 -0.1367 0.1448  0.0820  983  ALA   B O   
7665  C  CB  . ALA   B 679 ? 2.1303 2.0218 2.3602 -0.1351 0.1217  0.0765  983  ALA   B CB  
7666  N  N   . THR   B 680 ? 2.1630 2.0838 2.4139 -0.1352 0.1290  0.0742  984  THR   B N   
7667  C  CA  . THR   B 680 ? 2.1190 2.0397 2.3728 -0.1354 0.1416  0.0774  984  THR   B CA  
7668  C  C   . THR   B 680 ? 2.0742 1.9828 2.2960 -0.1291 0.1479  0.0823  984  THR   B C   
7669  O  O   . THR   B 680 ? 2.0488 1.9414 2.2592 -0.1284 0.1598  0.0879  984  THR   B O   
7670  C  CB  . THR   B 680 ? 2.0699 2.0090 2.3407 -0.1364 0.1362  0.0728  984  THR   B CB  
7671  O  OG1 . THR   B 680 ? 2.0296 1.9747 2.2817 -0.1312 0.1252  0.0704  984  THR   B OG1 
7672  C  CG2 . THR   B 680 ? 2.0747 2.0261 2.3765 -0.1420 0.1285  0.0673  984  THR   B CG2 
7673  N  N   . THR   B 681 ? 2.0330 1.9486 2.2403 -0.1246 0.1400  0.0804  985  THR   B N   
7674  C  CA  . THR   B 681 ? 2.0443 1.9493 2.2215 -0.1183 0.1441  0.0844  985  THR   B CA  
7675  C  C   . THR   B 681 ? 2.0298 1.9354 2.1862 -0.1135 0.1305  0.0822  985  THR   B C   
7676  O  O   . THR   B 681 ? 2.0102 1.9263 2.1761 -0.1148 0.1182  0.0775  985  THR   B O   
7677  C  CB  . THR   B 681 ? 2.0918 2.0034 2.2694 -0.1169 0.1488  0.0846  985  THR   B CB  
7678  O  OG1 . THR   B 681 ? 2.0824 2.0100 2.2635 -0.1158 0.1354  0.0792  985  THR   B OG1 
7679  C  CG2 . THR   B 681 ? 2.0858 2.0014 2.2900 -0.1222 0.1601  0.0854  985  THR   B CG2 
7680  N  N   . ASP   B 682 ? 2.0128 1.9070 2.1405 -0.1076 0.1330  0.0857  986  ASP   B N   
7681  C  CA  . ASP   B 682 ? 1.9844 1.8777 2.0911 -0.1026 0.1212  0.0843  986  ASP   B CA  
7682  C  C   . ASP   B 682 ? 1.9706 1.8823 2.0864 -0.1027 0.1075  0.0785  986  ASP   B C   
7683  O  O   . ASP   B 682 ? 1.9534 1.8700 2.0701 -0.1024 0.0962  0.0753  986  ASP   B O   
7684  C  CB  . ASP   B 682 ? 1.9802 1.8612 2.0571 -0.0962 0.1255  0.0882  986  ASP   B CB  
7685  N  N   . GLU   B 683 ? 2.0005 1.9217 2.1220 -0.1027 0.1086  0.0771  987  GLU   B N   
7686  C  CA  . GLU   B 683 ? 1.9463 1.8842 2.0753 -0.1025 0.0963  0.0719  987  GLU   B CA  
7687  C  C   . GLU   B 683 ? 1.9548 1.9033 2.1080 -0.1072 0.0890  0.0674  987  GLU   B C   
7688  O  O   . GLU   B 683 ? 1.9321 1.8893 2.0853 -0.1061 0.0765  0.0635  987  GLU   B O   
7689  C  CB  . GLU   B 683 ? 1.8717 1.8173 2.0057 -0.1025 0.1003  0.0714  987  GLU   B CB  
7690  N  N   . GLU   B 684 ? 2.0518 1.9993 2.2255 -0.1124 0.0965  0.0680  988  GLU   B N   
7691  C  CA  . GLU   B 684 ? 2.0304 1.9875 2.2280 -0.1169 0.0893  0.0636  988  GLU   B CA  
7692  C  C   . GLU   B 684 ? 2.0047 1.9550 2.1951 -0.1162 0.0828  0.0632  988  GLU   B C   
7693  O  O   . GLU   B 684 ? 1.9795 1.9381 2.1741 -0.1159 0.0706  0.0589  988  GLU   B O   
7694  C  CB  . GLU   B 684 ? 2.0255 1.9834 2.2482 -0.1227 0.0993  0.0642  988  GLU   B CB  
7695  N  N   . ARG   B 685 ? 1.9526 1.8870 2.1314 -0.1157 0.0910  0.0679  989  ARG   B N   
7696  C  CA  . ARG   B 685 ? 1.8487 1.7754 2.0215 -0.1153 0.0859  0.0679  989  ARG   B CA  
7697  C  C   . ARG   B 685 ? 1.7789 1.7079 1.9324 -0.1099 0.0738  0.0660  989  ARG   B C   
7698  O  O   . ARG   B 685 ? 1.6401 1.5694 1.7945 -0.1098 0.0652  0.0637  989  ARG   B O   
7699  C  CB  . ARG   B 685 ? 1.8859 1.7941 2.0467 -0.1150 0.0979  0.0737  989  ARG   B CB  
7700  C  CG  . ARG   B 685 ? 1.9766 1.8811 2.1552 -0.1200 0.1117  0.0764  989  ARG   B CG  
7701  C  CD  . ARG   B 685 ? 1.9577 1.8424 2.1222 -0.1193 0.1236  0.0824  989  ARG   B CD  
7702  N  NE  . ARG   B 685 ? 1.9925 1.8670 2.1280 -0.1130 0.1280  0.0865  989  ARG   B NE  
7703  C  CZ  . ARG   B 685 ? 1.9996 1.8653 2.1282 -0.1121 0.1414  0.0911  989  ARG   B CZ  
7704  N  NH1 . ARG   B 685 ? 2.0469 1.9129 2.1961 -0.1172 0.1527  0.0926  989  ARG   B NH1 
7705  N  NH2 . ARG   B 685 ? 1.9692 1.8254 2.0699 -0.1059 0.1435  0.0942  989  ARG   B NH2 
7706  N  N   . GLN   B 686 ? 1.8070 1.7374 1.9432 -0.1054 0.0730  0.0670  990  GLN   B N   
7707  C  CA  . GLN   B 686 ? 1.6990 1.6324 1.8174 -0.1002 0.0621  0.0654  990  GLN   B CA  
7708  C  C   . GLN   B 686 ? 1.6920 1.6428 1.8210 -0.1003 0.0520  0.0603  990  GLN   B C   
7709  O  O   . GLN   B 686 ? 1.6823 1.6375 1.7983 -0.0964 0.0471  0.0597  990  GLN   B O   
7710  C  CB  . GLN   B 686 ? 1.5500 1.4735 1.6428 -0.0949 0.0668  0.0695  990  GLN   B CB  
7711  N  N   . HIS   B 687 ? 1.6900 1.6504 1.8424 -0.1048 0.0485  0.0565  991  HIS   B N   
7712  C  CA  . HIS   B 687 ? 1.6295 1.6056 1.7930 -0.1050 0.0387  0.0515  991  HIS   B CA  
7713  C  C   . HIS   B 687 ? 1.6416 1.6229 1.8252 -0.1087 0.0326  0.0475  991  HIS   B C   
7714  O  O   . HIS   B 687 ? 1.6788 1.6548 1.8757 -0.1128 0.0385  0.0483  991  HIS   B O   
7715  C  CB  . HIS   B 687 ? 1.6111 1.5953 1.7842 -0.1065 0.0438  0.0510  991  HIS   B CB  
7716  C  CG  . HIS   B 687 ? 1.6147 1.6143 1.8054 -0.1082 0.0355  0.0457  991  HIS   B CG  
7717  N  ND1 . HIS   B 687 ? 1.6328 1.6377 1.8471 -0.1128 0.0338  0.0426  991  HIS   B ND1 
7718  C  CD2 . HIS   B 687 ? 1.6230 1.6332 1.8108 -0.1058 0.0280  0.0429  991  HIS   B CD2 
7719  C  CE1 . HIS   B 687 ? 1.5981 1.6160 1.8226 -0.1128 0.0256  0.0380  991  HIS   B CE1 
7720  N  NE2 . HIS   B 687 ? 1.6171 1.6384 1.8258 -0.1087 0.0222  0.0383  991  HIS   B NE2 
7721  N  N   . LEU   B 688 ? 1.5725 1.5634 1.7581 -0.1071 0.0207  0.0431  992  LEU   B N   
7722  C  CA  . LEU   B 688 ? 1.5178 1.5134 1.7204 -0.1097 0.0133  0.0388  992  LEU   B CA  
7723  C  C   . LEU   B 688 ? 1.4985 1.5081 1.7201 -0.1119 0.0092  0.0344  992  LEU   B C   
7724  O  O   . LEU   B 688 ? 1.5600 1.5782 1.7762 -0.1091 0.0041  0.0327  992  LEU   B O   
7725  C  CB  . LEU   B 688 ? 1.4381 1.4333 1.6286 -0.1058 0.0027  0.0370  992  LEU   B CB  
7726  C  CG  . LEU   B 688 ? 1.4255 1.4081 1.5952 -0.1025 0.0043  0.0408  992  LEU   B CG  
7727  C  CD1 . LEU   B 688 ? 1.2994 1.2855 1.4576 -0.0979 -0.0067 0.0386  992  LEU   B CD1 
7728  C  CD2 . LEU   B 688 ? 1.4855 1.4572 1.6618 -0.1057 0.0086  0.0422  992  LEU   B CD2 
7729  N  N   . GLN   B 689 ? 1.4687 1.4805 1.7129 -0.1167 0.0109  0.0323  993  GLN   B N   
7730  C  CA  . GLN   B 689 ? 1.4336 1.4583 1.6973 -0.1188 0.0067  0.0278  993  GLN   B CA  
7731  C  C   . GLN   B 689 ? 1.3825 1.4133 1.6515 -0.1176 -0.0065 0.0225  993  GLN   B C   
7732  O  O   . GLN   B 689 ? 1.3203 1.3449 1.5878 -0.1176 -0.0108 0.0218  993  GLN   B O   
7733  C  CB  . GLN   B 689 ? 1.4582 1.4831 1.7456 -0.1245 0.0142  0.0277  993  GLN   B CB  
7734  C  CG  . GLN   B 689 ? 1.6137 1.6294 1.8972 -0.1261 0.0284  0.0334  993  GLN   B CG  
7735  C  CD  . GLN   B 689 ? 1.6330 1.6534 1.9115 -0.1246 0.0345  0.0352  993  GLN   B CD  
7736  O  OE1 . GLN   B 689 ? 1.5269 1.5584 1.8090 -0.1233 0.0284  0.0320  993  GLN   B OE1 
7737  N  NE2 . GLN   B 689 ? 1.6856 1.6966 1.9549 -0.1246 0.0466  0.0405  993  GLN   B NE2 
7738  N  N   . GLU   B 690 ? 1.3254 1.3679 1.6004 -0.1165 -0.0128 0.0188  994  GLU   B N   
7739  C  CA  . GLU   B 690 ? 1.2522 1.3009 1.5323 -0.1149 -0.0252 0.0135  994  GLU   B CA  
7740  C  C   . GLU   B 690 ? 1.2266 1.2777 1.5316 -0.1193 -0.0275 0.0096  994  GLU   B C   
7741  O  O   . GLU   B 690 ? 1.2449 1.3032 1.5670 -0.1220 -0.0251 0.0080  994  GLU   B O   
7742  C  CB  . GLU   B 690 ? 1.1429 1.2022 1.4190 -0.1118 -0.0303 0.0113  994  GLU   B CB  
7743  N  N   . VAL   B 691 ? 1.1639 1.2089 1.4715 -0.1200 -0.0327 0.0080  995  VAL   B N   
7744  C  CA  . VAL   B 691 ? 1.1453 1.1908 1.4765 -0.1245 -0.0346 0.0045  995  VAL   B CA  
7745  C  C   . VAL   B 691 ? 1.1602 1.2088 1.4958 -0.1226 -0.0482 -0.0014 995  VAL   B C   
7746  O  O   . VAL   B 691 ? 1.1895 1.2356 1.5405 -0.1255 -0.0518 -0.0044 995  VAL   B O   
7747  C  CB  . VAL   B 691 ? 1.1862 1.2202 1.5208 -0.1282 -0.0270 0.0078  995  VAL   B CB  
7748  C  CG1 . VAL   B 691 ? 1.2610 1.2895 1.5850 -0.1286 -0.0138 0.0141  995  VAL   B CG1 
7749  C  CG2 . VAL   B 691 ? 1.2027 1.2277 1.5247 -0.1259 -0.0334 0.0074  995  VAL   B CG2 
7750  N  N   . GLY   B 692 ? 1.1047 1.1586 1.4274 -0.1176 -0.0557 -0.0032 996  GLY   B N   
7751  C  CA  . GLY   B 692 ? 1.0946 1.1507 1.4191 -0.1149 -0.0683 -0.0085 996  GLY   B CA  
7752  C  C   . GLY   B 692 ? 1.0959 1.1576 1.4048 -0.1093 -0.0748 -0.0097 996  GLY   B C   
7753  O  O   . GLY   B 692 ? 1.0611 1.1201 1.3501 -0.1060 -0.0726 -0.0061 996  GLY   B O   
7754  N  N   . LEU   B 693 ? 1.1100 1.1793 1.4280 -0.1080 -0.0830 -0.0147 997  LEU   B N   
7755  C  CA  . LEU   B 693 ? 1.0613 1.1364 1.3667 -0.1028 -0.0889 -0.0160 997  LEU   B CA  
7756  C  C   . LEU   B 693 ? 0.9992 1.0755 1.3095 -0.1003 -0.1008 -0.0219 997  LEU   B C   
7757  O  O   . LEU   B 693 ? 1.0335 1.1128 1.3629 -0.1029 -0.1042 -0.0260 997  LEU   B O   
7758  C  CB  . LEU   B 693 ? 1.0373 1.1217 1.3473 -0.1035 -0.0846 -0.0156 997  LEU   B CB  
7759  C  CG  . LEU   B 693 ? 1.0424 1.1252 1.3411 -0.1042 -0.0741 -0.0097 997  LEU   B CG  
7760  C  CD1 . LEU   B 693 ? 1.0992 1.1908 1.3957 -0.1027 -0.0727 -0.0096 997  LEU   B CD1 
7761  C  CD2 . LEU   B 693 ? 1.0355 1.1113 1.3129 -0.1007 -0.0747 -0.0066 997  LEU   B CD2 
7762  N  N   . PHE   B 694 ? 0.9772 1.0511 1.2706 -0.0950 -0.1072 -0.0224 998  PHE   B N   
7763  C  CA  . PHE   B 694 ? 1.0283 1.1012 1.3238 -0.0919 -0.1186 -0.0278 998  PHE   B CA  
7764  C  C   . PHE   B 694 ? 0.9965 1.0705 1.2729 -0.0855 -0.1235 -0.0278 998  PHE   B C   
7765  O  O   . PHE   B 694 ? 0.9758 1.0459 1.2357 -0.0831 -0.1208 -0.0240 998  PHE   B O   
7766  C  CB  . PHE   B 694 ? 1.0372 1.1004 1.3358 -0.0931 -0.1218 -0.0290 998  PHE   B CB  
7767  C  CG  . PHE   B 694 ? 1.0166 1.0774 1.3183 -0.0901 -0.1336 -0.0349 998  PHE   B CG  
7768  C  CD1 . PHE   B 694 ? 1.0101 1.0740 1.3321 -0.0926 -0.1388 -0.0400 998  PHE   B CD1 
7769  C  CD2 . PHE   B 694 ? 1.0074 1.0623 1.2918 -0.0846 -0.1397 -0.0353 998  PHE   B CD2 
7770  C  CE1 . PHE   B 694 ? 1.0230 1.0835 1.3467 -0.0894 -0.1504 -0.0457 998  PHE   B CE1 
7771  C  CE2 . PHE   B 694 ? 0.9506 1.0020 1.2362 -0.0813 -0.1505 -0.0407 998  PHE   B CE2 
7772  C  CZ  . PHE   B 694 ? 0.9837 1.0376 1.2885 -0.0836 -0.1561 -0.0459 998  PHE   B CZ  
7773  N  N   . HIS   B 695 ? 0.9767 1.0557 1.2557 -0.0825 -0.1307 -0.0320 999  HIS   B N   
7774  C  CA  . HIS   B 695 ? 0.9689 1.0485 1.2308 -0.0763 -0.1356 -0.0322 999  HIS   B CA  
7775  C  C   . HIS   B 695 ? 1.0029 1.0742 1.2588 -0.0728 -0.1437 -0.0350 999  HIS   B C   
7776  O  O   . HIS   B 695 ? 1.0272 1.0968 1.2931 -0.0725 -0.1513 -0.0400 999  HIS   B O   
7777  C  CB  . HIS   B 695 ? 0.9842 1.0717 1.2499 -0.0743 -0.1394 -0.0353 999  HIS   B CB  
7778  C  CG  . HIS   B 695 ? 0.9728 1.0608 1.2212 -0.0680 -0.1435 -0.0352 999  HIS   B CG  
7779  N  ND1 . HIS   B 695 ? 0.9964 1.0891 1.2334 -0.0666 -0.1383 -0.0314 999  HIS   B ND1 
7780  C  CD2 . HIS   B 695 ? 0.9629 1.0467 1.2031 -0.0627 -0.1519 -0.0383 999  HIS   B CD2 
7781  C  CE1 . HIS   B 695 ? 0.9875 1.0794 1.2112 -0.0609 -0.1430 -0.0321 999  HIS   B CE1 
7782  N  NE2 . HIS   B 695 ? 1.0118 1.0981 1.2367 -0.0583 -0.1511 -0.0362 999  HIS   B NE2 
7783  N  N   . LEU   B 696 ? 1.0021 1.0680 1.2417 -0.0700 -0.1424 -0.0318 1000 LEU   B N   
7784  C  CA  . LEU   B 696 ? 0.9925 1.0497 1.2253 -0.0664 -0.1496 -0.0340 1000 LEU   B CA  
7785  C  C   . LEU   B 696 ? 0.9013 0.9591 1.1239 -0.0598 -0.1573 -0.0370 1000 LEU   B C   
7786  O  O   . LEU   B 696 ? 0.9496 1.0040 1.1766 -0.0577 -0.1657 -0.0419 1000 LEU   B O   
7787  C  CB  . LEU   B 696 ? 0.9709 1.0215 1.1904 -0.0657 -0.1452 -0.0295 1000 LEU   B CB  
7788  C  CG  . LEU   B 696 ? 0.8839 0.9250 1.0949 -0.0617 -0.1518 -0.0314 1000 LEU   B CG  
7789  C  CD1 . LEU   B 696 ? 0.8343 0.8691 1.0593 -0.0659 -0.1541 -0.0340 1000 LEU   B CD1 
7790  C  CD2 . LEU   B 696 ? 0.8849 0.9222 1.0795 -0.0594 -0.1472 -0.0264 1000 LEU   B CD2 
7791  N  N   . GLY   B 697 ? 0.8724 0.9341 1.0813 -0.0563 -0.1545 -0.0340 1001 GLY   B N   
7792  C  CA  . GLY   B 697 ? 0.9068 0.9683 1.1040 -0.0498 -0.1604 -0.0358 1001 GLY   B CA  
7793  C  C   . GLY   B 697 ? 0.9543 1.0113 1.1336 -0.0451 -0.1597 -0.0327 1001 GLY   B C   
7794  O  O   . GLY   B 697 ? 1.0037 1.0610 1.1719 -0.0394 -0.1629 -0.0333 1001 GLY   B O   
7795  N  N   . GLU   B 698 ? 0.9668 1.0195 1.1429 -0.0470 -0.1553 -0.0294 1002 GLU   B N   
7796  C  CA  . GLU   B 698 ? 0.9439 0.9923 1.1037 -0.0427 -0.1543 -0.0262 1002 GLU   B CA  
7797  C  C   . GLU   B 698 ? 0.9143 0.9666 1.0703 -0.0453 -0.1457 -0.0208 1002 GLU   B C   
7798  O  O   . GLU   B 698 ? 0.9020 0.9585 1.0676 -0.0506 -0.1405 -0.0196 1002 GLU   B O   
7799  C  CB  . GLU   B 698 ? 0.9808 1.0185 1.1385 -0.0419 -0.1580 -0.0274 1002 GLU   B CB  
7800  C  CG  . GLU   B 698 ? 0.9002 0.9329 1.0633 -0.0401 -0.1669 -0.0332 1002 GLU   B CG  
7801  C  CD  . GLU   B 698 ? 0.9906 1.0227 1.1414 -0.0328 -0.1721 -0.0348 1002 GLU   B CD  
7802  O  OE1 . GLU   B 698 ? 1.0239 1.0525 1.1775 -0.0303 -0.1798 -0.0397 1002 GLU   B OE1 
7803  O  OE2 . GLU   B 698 ? 0.9870 1.0220 1.1254 -0.0295 -0.1683 -0.0311 1002 GLU   B OE2 
7804  N  N   . PHE   B 699 ? 0.9353 0.9860 1.0773 -0.0414 -0.1442 -0.0177 1003 PHE   B N   
7805  C  CA  . PHE   B 699 ? 0.9431 0.9972 1.0799 -0.0429 -0.1370 -0.0128 1003 PHE   B CA  
7806  C  C   . PHE   B 699 ? 0.9878 1.0334 1.1185 -0.0427 -0.1356 -0.0105 1003 PHE   B C   
7807  O  O   . PHE   B 699 ? 0.9779 1.0192 1.0973 -0.0377 -0.1382 -0.0099 1003 PHE   B O   
7808  C  CB  . PHE   B 699 ? 0.9004 0.9606 1.0270 -0.0386 -0.1364 -0.0110 1003 PHE   B CB  
7809  C  CG  . PHE   B 699 ? 0.8808 0.9454 1.0028 -0.0400 -0.1299 -0.0064 1003 PHE   B CG  
7810  C  CD1 . PHE   B 699 ? 0.9294 0.9896 1.0416 -0.0381 -0.1279 -0.0032 1003 PHE   B CD1 
7811  C  CD2 . PHE   B 699 ? 0.9660 1.0385 1.0923 -0.0426 -0.1263 -0.0056 1003 PHE   B CD2 
7812  C  CE1 . PHE   B 699 ? 0.9191 0.9830 1.0264 -0.0389 -0.1226 0.0007  1003 PHE   B CE1 
7813  C  CE2 . PHE   B 699 ? 0.9651 1.0410 1.0863 -0.0435 -0.1209 -0.0016 1003 PHE   B CE2 
7814  C  CZ  . PHE   B 699 ? 0.8958 0.9673 1.0075 -0.0416 -0.1192 0.0015  1003 PHE   B CZ  
7815  N  N   . VAL   B 700 ? 0.9945 1.0370 1.1324 -0.0480 -0.1312 -0.0092 1004 VAL   B N   
7816  C  CA  . VAL   B 700 ? 0.9323 0.9654 1.0656 -0.0482 -0.1301 -0.0075 1004 VAL   B CA  
7817  C  C   . VAL   B 700 ? 0.9492 0.9822 1.0690 -0.0456 -0.1259 -0.0028 1004 VAL   B C   
7818  O  O   . VAL   B 700 ? 0.9552 0.9942 1.0740 -0.0471 -0.1208 -0.0001 1004 VAL   B O   
7819  C  CB  . VAL   B 700 ? 0.9032 0.9327 1.0488 -0.0547 -0.1261 -0.0074 1004 VAL   B CB  
7820  C  CG1 . VAL   B 700 ? 0.9539 0.9733 1.0929 -0.0549 -0.1236 -0.0047 1004 VAL   B CG1 
7821  C  CG2 . VAL   B 700 ? 0.8483 0.8769 1.0079 -0.0569 -0.1313 -0.0124 1004 VAL   B CG2 
7822  N  N   . ASN   B 701 ? 0.9332 0.9593 1.0427 -0.0416 -0.1282 -0.0021 1005 ASN   B N   
7823  C  CA  . ASN   B 701 ? 0.9290 0.9545 1.0255 -0.0382 -0.1255 0.0019  1005 ASN   B CA  
7824  C  C   . ASN   B 701 ? 1.0164 1.0326 1.1085 -0.0394 -0.1223 0.0045  1005 ASN   B C   
7825  O  O   . ASN   B 701 ? 1.0360 1.0524 1.1198 -0.0384 -0.1183 0.0083  1005 ASN   B O   
7826  C  CB  . ASN   B 701 ? 0.9338 0.9589 1.0203 -0.0313 -0.1305 0.0011  1005 ASN   B CB  
7827  C  CG  . ASN   B 701 ? 0.9782 1.0133 1.0615 -0.0286 -0.1302 0.0018  1005 ASN   B CG  
7828  O  OD1 . ASN   B 701 ? 1.0284 1.0701 1.1135 -0.0311 -0.1258 0.0040  1005 ASN   B OD1 
7829  N  ND2 . ASN   B 701 ? 0.9636 0.9991 1.0415 -0.0232 -0.1347 0.0001  1005 ASN   B ND2 
7830  N  N   . VAL   B 702 ? 0.9832 0.9910 1.0807 -0.0416 -0.1242 0.0026  1006 VAL   B N   
7831  C  CA  . VAL   B 702 ? 0.9674 0.9650 1.0608 -0.0427 -0.1215 0.0048  1006 VAL   B CA  
7832  C  C   . VAL   B 702 ? 1.0610 1.0528 1.1673 -0.0478 -0.1220 0.0022  1006 VAL   B C   
7833  O  O   . VAL   B 702 ? 1.0292 1.0215 1.1432 -0.0478 -0.1277 -0.0021 1006 VAL   B O   
7834  C  CB  . VAL   B 702 ? 0.9974 0.9883 1.0781 -0.0366 -0.1254 0.0051  1006 VAL   B CB  
7835  C  CG1 . VAL   B 702 ? 1.0256 1.0170 1.1075 -0.0332 -0.1326 0.0009  1006 VAL   B CG1 
7836  C  CG2 . VAL   B 702 ? 1.0058 0.9845 1.0848 -0.0383 -0.1241 0.0060  1006 VAL   B CG2 
7837  N  N   . PHE   B 703 ? 1.0785 1.0647 1.1873 -0.0521 -0.1160 0.0048  1007 PHE   B N   
7838  C  CA  . PHE   B 703 ? 1.0512 1.0307 1.1725 -0.0574 -0.1152 0.0031  1007 PHE   B CA  
7839  C  C   . PHE   B 703 ? 1.1072 1.0741 1.2202 -0.0562 -0.1148 0.0048  1007 PHE   B C   
7840  O  O   . PHE   B 703 ? 1.2022 1.1655 1.3037 -0.0546 -0.1102 0.0089  1007 PHE   B O   
7841  C  CB  . PHE   B 703 ? 1.0724 1.0550 1.2042 -0.0636 -0.1075 0.0050  1007 PHE   B CB  
7842  C  CG  . PHE   B 703 ? 1.0534 1.0465 1.1986 -0.0662 -0.1084 0.0022  1007 PHE   B CG  
7843  C  CD1 . PHE   B 703 ? 1.0240 1.0176 1.1830 -0.0682 -0.1139 -0.0026 1007 PHE   B CD1 
7844  C  CD2 . PHE   B 703 ? 1.0627 1.0648 1.2070 -0.0667 -0.1040 0.0042  1007 PHE   B CD2 
7845  C  CE1 . PHE   B 703 ? 1.0021 1.0053 1.1736 -0.0705 -0.1150 -0.0053 1007 PHE   B CE1 
7846  C  CE2 . PHE   B 703 ? 1.0066 1.0180 1.1629 -0.0690 -0.1048 0.0017  1007 PHE   B CE2 
7847  C  CZ  . PHE   B 703 ? 0.9763 0.9883 1.1462 -0.0708 -0.1102 -0.0031 1007 PHE   B CZ  
7848  N  N   . CYS   B 704 ? 1.1042 1.0639 1.2226 -0.0568 -0.1198 0.0015  1008 CYS   B N   
7849  C  CA  . CYS   B 704 ? 1.1020 1.0492 1.2116 -0.0550 -0.1204 0.0027  1008 CYS   B CA  
7850  C  C   . CYS   B 704 ? 1.1301 1.0693 1.2532 -0.0607 -0.1201 0.0007  1008 CYS   B C   
7851  O  O   . CYS   B 704 ? 1.0855 1.0253 1.2198 -0.0620 -0.1262 -0.0040 1008 CYS   B O   
7852  C  CB  . CYS   B 704 ? 1.0818 1.0267 1.1805 -0.0481 -0.1283 0.0005  1008 CYS   B CB  
7853  S  SG  . CYS   B 704 ? 1.4007 1.3327 1.4828 -0.0437 -0.1280 0.0033  1008 CYS   B SG  
7854  N  N   . HIS   B 705 ? 1.1730 1.1044 1.2953 -0.0641 -0.1130 0.0044  1009 HIS   B N   
7855  C  CA  . HIS   B 705 ? 1.1918 1.1144 1.3267 -0.0697 -0.1117 0.0031  1009 HIS   B CA  
7856  C  C   . HIS   B 705 ? 1.1755 1.0877 1.3064 -0.0670 -0.1191 0.0002  1009 HIS   B C   
7857  O  O   . HIS   B 705 ? 1.1305 1.0348 1.2457 -0.0626 -0.1194 0.0025  1009 HIS   B O   
7858  C  CB  . HIS   B 705 ? 1.1651 1.0809 1.2974 -0.0731 -0.1016 0.0083  1009 HIS   B CB  
7859  C  CG  . HIS   B 705 ? 1.1669 1.0890 1.3128 -0.0791 -0.0943 0.0096  1009 HIS   B CG  
7860  N  ND1 . HIS   B 705 ? 1.1661 1.0893 1.3327 -0.0851 -0.0943 0.0066  1009 HIS   B ND1 
7861  C  CD2 . HIS   B 705 ? 1.1663 1.0935 1.3083 -0.0797 -0.0867 0.0134  1009 HIS   B CD2 
7862  C  CE1 . HIS   B 705 ? 1.2387 1.1679 1.4136 -0.0892 -0.0865 0.0087  1009 HIS   B CE1 
7863  N  NE2 . HIS   B 705 ? 1.2177 1.1490 1.3774 -0.0860 -0.0819 0.0129  1009 HIS   B NE2 
7864  N  N   . GLY   B 706 ? 1.1514 1.0631 1.2963 -0.0694 -0.1254 -0.0049 1010 GLY   B N   
7865  C  CA  . GLY   B 706 ? 1.1786 1.0806 1.3191 -0.0663 -0.1335 -0.0082 1010 GLY   B CA  
7866  C  C   . GLY   B 706 ? 1.1401 1.0441 1.2958 -0.0681 -0.1418 -0.0145 1010 GLY   B C   
7867  O  O   . GLY   B 706 ? 1.1008 1.0146 1.2708 -0.0716 -0.1416 -0.0164 1010 GLY   B O   
7868  N  N   . SER   B 707 ? 1.1224 1.0165 1.2745 -0.0654 -0.1495 -0.0178 1011 SER   B N   
7869  C  CA  . SER   B 707 ? 1.1752 1.0690 1.3398 -0.0662 -0.1589 -0.0242 1011 SER   B CA  
7870  C  C   . SER   B 707 ? 1.2922 1.1766 1.4427 -0.0593 -0.1679 -0.0271 1011 SER   B C   
7871  O  O   . SER   B 707 ? 1.3701 1.2449 1.5064 -0.0564 -0.1663 -0.0243 1011 SER   B O   
7872  C  CB  . SER   B 707 ? 1.1587 1.0475 1.3438 -0.0744 -0.1575 -0.0260 1011 SER   B CB  
7873  O  OG  . SER   B 707 ? 1.2072 1.0968 1.4060 -0.0753 -0.1670 -0.0326 1011 SER   B OG  
7874  N  N   . LEU   B 708 ? 1.2877 1.1742 1.4414 -0.0565 -0.1773 -0.0326 1012 LEU   B N   
7875  C  CA  . LEU   B 708 ? 1.3362 1.2141 1.4759 -0.0492 -0.1863 -0.0357 1012 LEU   B CA  
7876  C  C   . LEU   B 708 ? 1.3753 1.2428 1.5255 -0.0514 -0.1948 -0.0414 1012 LEU   B C   
7877  O  O   . LEU   B 708 ? 1.3737 1.2357 1.5168 -0.0458 -0.2043 -0.0458 1012 LEU   B O   
7878  C  CB  . LEU   B 708 ? 1.3415 1.2279 1.4732 -0.0428 -0.1910 -0.0375 1012 LEU   B CB  
7879  C  CG  . LEU   B 708 ? 1.2909 1.1850 1.4071 -0.0381 -0.1849 -0.0324 1012 LEU   B CG  
7880  C  CD1 . LEU   B 708 ? 1.2248 1.1242 1.3450 -0.0434 -0.1739 -0.0268 1012 LEU   B CD1 
7881  C  CD2 . LEU   B 708 ? 1.1700 1.0748 1.2851 -0.0343 -0.1882 -0.0344 1012 LEU   B CD2 
7882  N  N   . VAL   B 709 ? 1.3873 1.2518 1.5546 -0.0594 -0.1914 -0.0414 1013 VAL   B N   
7883  C  CA  . VAL   B 709 ? 1.4262 1.2811 1.6065 -0.0627 -0.1988 -0.0466 1013 VAL   B CA  
7884  C  C   . VAL   B 709 ? 1.5298 1.3746 1.7144 -0.0683 -0.1924 -0.0435 1013 VAL   B C   
7885  O  O   . VAL   B 709 ? 1.5228 1.3680 1.6991 -0.0690 -0.1826 -0.0373 1013 VAL   B O   
7886  C  CB  . VAL   B 709 ? 1.3217 1.1851 1.5255 -0.0680 -0.2026 -0.0513 1013 VAL   B CB  
7887  C  CG1 . VAL   B 709 ? 1.2477 1.1180 1.4464 -0.0619 -0.2108 -0.0554 1013 VAL   B CG1 
7888  C  CG2 . VAL   B 709 ? 1.2769 1.1507 1.4948 -0.0752 -0.1914 -0.0471 1013 VAL   B CG2 
7889  N  N   . MET   B 710 ? 1.4806 1.3164 1.6788 -0.0724 -0.1981 -0.0478 1014 MET   B N   
7890  C  CA  . MET   B 710 ? 1.5128 1.3362 1.7137 -0.0770 -0.1936 -0.0456 1014 MET   B CA  
7891  C  C   . MET   B 710 ? 1.5775 1.3893 1.7534 -0.0701 -0.1942 -0.0429 1014 MET   B C   
7892  O  O   . MET   B 710 ? 1.6025 1.4015 1.7738 -0.0678 -0.2018 -0.0463 1014 MET   B O   
7893  C  CB  . MET   B 710 ? 1.5167 1.3455 1.7282 -0.0843 -0.1802 -0.0398 1014 MET   B CB  
7894  C  CG  . MET   B 710 ? 1.5565 1.3734 1.7610 -0.0866 -0.1720 -0.0347 1014 MET   B CG  
7895  S  SD  . MET   B 710 ? 1.9066 1.7053 2.1190 -0.0898 -0.1786 -0.0387 1014 MET   B SD  
7896  C  CE  . MET   B 710 ? 1.7711 1.5592 1.9806 -0.0948 -0.1652 -0.0315 1014 MET   B CE  
7897  N  N   . PRO   B 719 ? 1.5613 1.4782 2.0061 -0.1501 -0.1345 -0.0445 1023 PRO   B N   
7898  C  CA  . PRO   B 719 ? 1.5396 1.4718 1.9981 -0.1502 -0.1370 -0.0476 1023 PRO   B CA  
7899  C  C   . PRO   B 719 ? 1.5747 1.5152 2.0127 -0.1449 -0.1319 -0.0435 1023 PRO   B C   
7900  O  O   . PRO   B 719 ? 1.5241 1.4765 1.9721 -0.1466 -0.1264 -0.0424 1023 PRO   B O   
7901  C  CB  . PRO   B 719 ? 1.5445 1.4766 2.0071 -0.1467 -0.1542 -0.0560 1023 PRO   B CB  
7902  C  CG  . PRO   B 719 ? 1.5712 1.4905 2.0083 -0.1409 -0.1598 -0.0557 1023 PRO   B CG  
7903  C  CD  . PRO   B 719 ? 1.6198 1.5281 2.0530 -0.1450 -0.1485 -0.0496 1023 PRO   B CD  
7904  N  N   . THR   B 720 ? 1.5768 1.5112 1.9865 -0.1383 -0.1340 -0.0413 1024 THR   B N   
7905  C  CA  . THR   B 720 ? 1.5469 1.4867 1.9348 -0.1334 -0.1280 -0.0364 1024 THR   B CA  
7906  C  C   . THR   B 720 ? 1.5658 1.4949 1.9344 -0.1326 -0.1190 -0.0298 1024 THR   B C   
7907  O  O   . THR   B 720 ? 1.5939 1.5106 1.9572 -0.1325 -0.1218 -0.0301 1024 THR   B O   
7908  C  CB  . THR   B 720 ? 1.5230 1.4664 1.8935 -0.1253 -0.1392 -0.0398 1024 THR   B CB  
7909  O  OG1 . THR   B 720 ? 1.5374 1.4686 1.8901 -0.1209 -0.1454 -0.0404 1024 THR   B OG1 
7910  C  CG2 . THR   B 720 ? 1.5011 1.4521 1.8895 -0.1255 -0.1501 -0.0471 1024 THR   B CG2 
7911  N  N   . GLN   B 721 ? 1.4395 1.3731 1.7972 -0.1318 -0.1084 -0.0239 1025 GLN   B N   
7912  C  CA  . GLN   B 721 ? 1.3898 1.3140 1.7276 -0.1304 -0.0995 -0.0174 1025 GLN   B CA  
7913  C  C   . GLN   B 721 ? 1.4162 1.3450 1.7292 -0.1232 -0.1002 -0.0150 1025 GLN   B C   
7914  O  O   . GLN   B 721 ? 1.4186 1.3590 1.7324 -0.1223 -0.0978 -0.0144 1025 GLN   B O   
7915  C  CB  . GLN   B 721 ? 1.3773 1.3006 1.7250 -0.1365 -0.0849 -0.0120 1025 GLN   B CB  
7916  N  N   . GLY   B 722 ? 1.3985 1.3186 1.6901 -0.1179 -0.1034 -0.0137 1026 GLY   B N   
7917  C  CA  . GLY   B 722 ? 1.2845 1.2083 1.5529 -0.1112 -0.1033 -0.0109 1026 GLY   B CA  
7918  C  C   . GLY   B 722 ? 1.1939 1.1190 1.4517 -0.1047 -0.1158 -0.0154 1026 GLY   B C   
7919  O  O   . GLY   B 722 ? 1.2441 1.1700 1.5135 -0.1050 -0.1251 -0.0212 1026 GLY   B O   
7920  N  N   . SER   B 723 ? 1.1628 1.0876 1.3980 -0.0983 -0.1159 -0.0126 1027 SER   B N   
7921  C  CA  . SER   B 723 ? 1.1350 1.0627 1.3594 -0.0916 -0.1262 -0.0162 1027 SER   B CA  
7922  C  C   . SER   B 723 ? 1.2164 1.1488 1.4206 -0.0861 -0.1228 -0.0120 1027 SER   B C   
7923  O  O   . SER   B 723 ? 1.1843 1.1091 1.3727 -0.0836 -0.1191 -0.0080 1027 SER   B O   
7924  C  CB  . SER   B 723 ? 1.0929 1.0084 1.3110 -0.0890 -0.1339 -0.0188 1027 SER   B CB  
7925  O  OG  . SER   B 723 ? 1.0728 0.9909 1.2846 -0.0831 -0.1445 -0.0233 1027 SER   B OG  
7926  N  N   . VAL   B 724 ? 1.1519 1.0967 1.3572 -0.0844 -0.1241 -0.0131 1028 VAL   B N   
7927  C  CA  . VAL   B 724 ? 1.1348 1.0855 1.3228 -0.0791 -0.1223 -0.0100 1028 VAL   B CA  
7928  C  C   . VAL   B 724 ? 1.1356 1.0921 1.3193 -0.0737 -0.1318 -0.0141 1028 VAL   B C   
7929  O  O   . VAL   B 724 ? 1.1640 1.1279 1.3604 -0.0751 -0.1357 -0.0180 1028 VAL   B O   
7930  C  CB  . VAL   B 724 ? 1.0732 1.0332 1.2650 -0.0820 -0.1137 -0.0066 1028 VAL   B CB  
7931  C  CG1 . VAL   B 724 ? 1.0984 1.0626 1.2711 -0.0765 -0.1120 -0.0032 1028 VAL   B CG1 
7932  C  CG2 . VAL   B 724 ? 1.0484 1.0028 1.2470 -0.0878 -0.1040 -0.0029 1028 VAL   B CG2 
7933  N  N   . LEU   B 725 ? 1.1033 1.0563 1.2689 -0.0672 -0.1352 -0.0132 1029 LEU   B N   
7934  C  CA  . LEU   B 725 ? 1.1119 1.0690 1.2707 -0.0612 -0.1433 -0.0165 1029 LEU   B CA  
7935  C  C   . LEU   B 725 ? 1.0785 1.0454 1.2271 -0.0579 -0.1398 -0.0134 1029 LEU   B C   
7936  O  O   . LEU   B 725 ? 1.1191 1.0861 1.2595 -0.0580 -0.1328 -0.0086 1029 LEU   B O   
7937  C  CB  . LEU   B 725 ? 1.0822 1.0288 1.2280 -0.0558 -0.1494 -0.0177 1029 LEU   B CB  
7938  C  CG  . LEU   B 725 ? 1.0865 1.0217 1.2407 -0.0589 -0.1529 -0.0205 1029 LEU   B CG  
7939  C  CD1 . LEU   B 725 ? 1.1681 1.0945 1.3095 -0.0524 -0.1611 -0.0230 1029 LEU   B CD1 
7940  C  CD2 . LEU   B 725 ? 1.1055 1.0443 1.2809 -0.0642 -0.1562 -0.0251 1029 LEU   B CD2 
7941  N  N   . PHE   B 726 ? 1.0568 1.0315 1.2060 -0.0549 -0.1447 -0.0163 1030 PHE   B N   
7942  C  CA  . PHE   B 726 ? 1.0491 1.0332 1.1895 -0.0518 -0.1417 -0.0136 1030 PHE   B CA  
7943  C  C   . PHE   B 726 ? 1.0468 1.0328 1.1781 -0.0451 -0.1489 -0.0162 1030 PHE   B C   
7944  O  O   . PHE   B 726 ? 1.0522 1.0362 1.1890 -0.0440 -0.1561 -0.0210 1030 PHE   B O   
7945  C  CB  . PHE   B 726 ? 0.9820 0.9765 1.1344 -0.0566 -0.1369 -0.0131 1030 PHE   B CB  
7946  C  CG  . PHE   B 726 ? 0.9791 0.9783 1.1465 -0.0586 -0.1421 -0.0182 1030 PHE   B CG  
7947  C  CD1 . PHE   B 726 ? 0.9728 0.9787 1.1374 -0.0546 -0.1471 -0.0208 1030 PHE   B CD1 
7948  C  CD2 . PHE   B 726 ? 1.0344 1.0317 1.2192 -0.0647 -0.1416 -0.0204 1030 PHE   B CD2 
7949  C  CE1 . PHE   B 726 ? 0.9726 0.9826 1.1506 -0.0561 -0.1521 -0.0255 1030 PHE   B CE1 
7950  C  CE2 . PHE   B 726 ? 0.9899 0.9920 1.1894 -0.0664 -0.1468 -0.0253 1030 PHE   B CE2 
7951  C  CZ  . PHE   B 726 ? 0.9575 0.9657 1.1530 -0.0620 -0.1522 -0.0278 1030 PHE   B CZ  
7952  N  N   . GLY   B 727 ? 1.0309 1.0202 1.1483 -0.0403 -0.1469 -0.0131 1031 GLY   B N   
7953  C  CA  . GLY   B 727 ? 0.9866 0.9799 1.0957 -0.0341 -0.1516 -0.0146 1031 GLY   B CA  
7954  C  C   . GLY   B 727 ? 0.9915 0.9970 1.1027 -0.0346 -0.1484 -0.0134 1031 GLY   B C   
7955  O  O   . GLY   B 727 ? 0.9602 0.9709 1.0745 -0.0384 -0.1419 -0.0102 1031 GLY   B O   
7956  N  N   . THR   B 728 ? 1.0221 1.0314 1.1305 -0.0304 -0.1530 -0.0159 1032 THR   B N   
7957  C  CA  . THR   B 728 ? 0.8832 0.9033 0.9942 -0.0306 -0.1510 -0.0155 1032 THR   B CA  
7958  C  C   . THR   B 728 ? 0.9413 0.9638 1.0394 -0.0238 -0.1527 -0.0147 1032 THR   B C   
7959  O  O   . THR   B 728 ? 0.9584 0.9745 1.0460 -0.0187 -0.1553 -0.0144 1032 THR   B O   
7960  C  CB  . THR   B 728 ? 0.9458 0.9687 1.0697 -0.0332 -0.1550 -0.0200 1032 THR   B CB  
7961  O  OG1 . THR   B 728 ? 0.8968 0.9127 1.0183 -0.0291 -0.1630 -0.0243 1032 THR   B OG1 
7962  C  CG2 . THR   B 728 ? 0.9298 0.9522 1.0683 -0.0406 -0.1519 -0.0203 1032 THR   B CG2 
7963  N  N   . VAL   B 729 ? 0.9905 1.0224 1.0899 -0.0235 -0.1511 -0.0142 1033 VAL   B N   
7964  C  CA  . VAL   B 729 ? 0.9749 1.0098 1.0630 -0.0174 -0.1515 -0.0129 1033 VAL   B CA  
7965  C  C   . VAL   B 729 ? 0.9698 0.9999 1.0539 -0.0121 -0.1583 -0.0169 1033 VAL   B C   
7966  O  O   . VAL   B 729 ? 0.9524 0.9800 1.0250 -0.0059 -0.1596 -0.0161 1033 VAL   B O   
7967  C  CB  . VAL   B 729 ? 0.8784 0.9244 0.9692 -0.0191 -0.1472 -0.0110 1033 VAL   B CB  
7968  C  CG1 . VAL   B 729 ? 0.8450 0.8942 0.9371 -0.0233 -0.1408 -0.0070 1033 VAL   B CG1 
7969  C  CG2 . VAL   B 729 ? 0.9939 1.0437 1.0958 -0.0222 -0.1492 -0.0144 1033 VAL   B CG2 
7970  N  N   . ASN   B 730 ? 0.9435 0.9718 1.0369 -0.0143 -0.1629 -0.0212 1034 ASN   B N   
7971  C  CA  . ASN   B 730 ? 0.9469 0.9697 1.0366 -0.0093 -0.1701 -0.0255 1034 ASN   B CA  
7972  C  C   . ASN   B 730 ? 0.9944 1.0053 1.0800 -0.0070 -0.1752 -0.0277 1034 ASN   B C   
7973  O  O   . ASN   B 730 ? 0.9611 0.9658 1.0456 -0.0037 -0.1823 -0.0320 1034 ASN   B O   
7974  C  CB  . ASN   B 730 ? 0.9802 1.0067 1.0820 -0.0123 -0.1733 -0.0294 1034 ASN   B CB  
7975  C  CG  . ASN   B 730 ? 1.0145 1.0517 1.1184 -0.0134 -0.1692 -0.0278 1034 ASN   B CG  
7976  O  OD1 . ASN   B 730 ? 1.0933 1.1321 1.1889 -0.0083 -0.1702 -0.0278 1034 ASN   B OD1 
7977  N  ND2 . ASN   B 730 ? 1.0953 1.1393 1.2100 -0.0198 -0.1644 -0.0263 1034 ASN   B ND2 
7978  N  N   . GLY   B 731 ? 1.0271 1.0341 1.1100 -0.0084 -0.1721 -0.0248 1035 GLY   B N   
7979  C  CA  . GLY   B 731 ? 0.9792 0.9744 1.0580 -0.0063 -0.1767 -0.0267 1035 GLY   B CA  
7980  C  C   . GLY   B 731 ? 0.9592 0.9495 1.0508 -0.0110 -0.1814 -0.0310 1035 GLY   B C   
7981  O  O   . GLY   B 731 ? 1.0124 0.9924 1.1013 -0.0086 -0.1874 -0.0341 1035 GLY   B O   
7982  N  N   . MET   B 732 ? 0.9782 0.9757 1.0842 -0.0174 -0.1789 -0.0315 1036 MET   B N   
7983  C  CA  . MET   B 732 ? 0.9776 0.9716 1.0984 -0.0228 -0.1822 -0.0351 1036 MET   B CA  
7984  C  C   . MET   B 732 ? 0.9801 0.9705 1.1054 -0.0280 -0.1772 -0.0323 1036 MET   B C   
7985  O  O   . MET   B 732 ? 1.0570 1.0523 1.1802 -0.0302 -0.1696 -0.0275 1036 MET   B O   
7986  C  CB  . MET   B 732 ? 0.9731 0.9766 1.1081 -0.0271 -0.1815 -0.0369 1036 MET   B CB  
7987  C  CG  . MET   B 732 ? 0.9504 0.9519 1.1032 -0.0334 -0.1837 -0.0401 1036 MET   B CG  
7988  S  SD  . MET   B 732 ? 1.0602 1.0672 1.2255 -0.0421 -0.1736 -0.0359 1036 MET   B SD  
7989  C  CE  . MET   B 732 ? 0.9439 0.9537 1.1324 -0.0480 -0.1773 -0.0410 1036 MET   B CE  
7990  N  N   . ILE   B 733 ? 0.9791 0.9602 1.1096 -0.0297 -0.1815 -0.0351 1037 ILE   B N   
7991  C  CA  . ILE   B 733 ? 1.0447 1.0210 1.1796 -0.0347 -0.1767 -0.0325 1037 ILE   B CA  
7992  C  C   . ILE   B 733 ? 1.0692 1.0467 1.2244 -0.0421 -0.1769 -0.0351 1037 ILE   B C   
7993  O  O   . ILE   B 733 ? 1.0668 1.0424 1.2308 -0.0421 -0.1843 -0.0404 1037 ILE   B O   
7994  C  CB  . ILE   B 733 ? 1.0264 0.9899 1.1509 -0.0312 -0.1802 -0.0328 1037 ILE   B CB  
7995  C  CG1 . ILE   B 733 ? 1.0089 0.9722 1.1148 -0.0250 -0.1773 -0.0287 1037 ILE   B CG1 
7996  C  CG2 . ILE   B 733 ? 0.9751 0.9328 1.1079 -0.0373 -0.1764 -0.0313 1037 ILE   B CG2 
7997  C  CD1 . ILE   B 733 ? 1.0130 0.9677 1.1057 -0.0173 -0.1844 -0.0312 1037 ILE   B CD1 
7998  N  N   . GLY   B 734 ? 1.0758 1.0559 1.2383 -0.0481 -0.1687 -0.0315 1038 GLY   B N   
7999  C  CA  . GLY   B 734 ? 1.0914 1.0742 1.2738 -0.0553 -0.1669 -0.0331 1038 GLY   B CA  
8000  C  C   . GLY   B 734 ? 1.0950 1.0703 1.2830 -0.0605 -0.1619 -0.0308 1038 GLY   B C   
8001  O  O   . GLY   B 734 ? 1.0747 1.0453 1.2508 -0.0594 -0.1570 -0.0264 1038 GLY   B O   
8002  N  N   . LEU   B 735 ? 1.1376 1.1118 1.3443 -0.0662 -0.1632 -0.0338 1039 LEU   B N   
8003  C  CA  . LEU   B 735 ? 1.1394 1.1077 1.3555 -0.0724 -0.1573 -0.0317 1039 LEU   B CA  
8004  C  C   . LEU   B 735 ? 1.1682 1.1450 1.4025 -0.0791 -0.1507 -0.0308 1039 LEU   B C   
8005  O  O   . LEU   B 735 ? 1.1888 1.1728 1.4360 -0.0803 -0.1545 -0.0347 1039 LEU   B O   
8006  C  CB  . LEU   B 735 ? 1.1606 1.1184 1.3839 -0.0734 -0.1647 -0.0361 1039 LEU   B CB  
8007  C  CG  . LEU   B 735 ? 1.2328 1.1818 1.4616 -0.0787 -0.1589 -0.0335 1039 LEU   B CG  
8008  C  CD1 . LEU   B 735 ? 1.3159 1.2518 1.5394 -0.0763 -0.1663 -0.0363 1039 LEU   B CD1 
8009  C  CD2 . LEU   B 735 ? 1.2549 1.2078 1.5082 -0.0866 -0.1554 -0.0347 1039 LEU   B CD2 
8010  N  N   . VAL   B 736 ? 1.1315 1.1068 1.3659 -0.0831 -0.1405 -0.0257 1040 VAL   B N   
8011  C  CA  . VAL   B 736 ? 1.1404 1.1212 1.3925 -0.0899 -0.1330 -0.0245 1040 VAL   B CA  
8012  C  C   . VAL   B 736 ? 1.2278 1.1988 1.4888 -0.0952 -0.1286 -0.0231 1040 VAL   B C   
8013  O  O   . VAL   B 736 ? 1.2095 1.1709 1.4573 -0.0937 -0.1263 -0.0201 1040 VAL   B O   
8014  C  CB  . VAL   B 736 ? 1.1240 1.1121 1.3684 -0.0899 -0.1237 -0.0193 1040 VAL   B CB  
8015  C  CG1 . VAL   B 736 ? 1.1610 1.1517 1.4215 -0.0967 -0.1146 -0.0172 1040 VAL   B CG1 
8016  C  CG2 . VAL   B 736 ? 1.1694 1.1683 1.4111 -0.0862 -0.1278 -0.0213 1040 VAL   B CG2 
8017  N  N   . THR   B 737 ? 1.2649 1.2381 1.5486 -0.1014 -0.1274 -0.0254 1041 THR   B N   
8018  C  CA  . THR   B 737 ? 1.2902 1.2550 1.5862 -0.1074 -0.1225 -0.0243 1041 THR   B CA  
8019  C  C   . THR   B 737 ? 1.3155 1.2873 1.6323 -0.1141 -0.1143 -0.0233 1041 THR   B C   
8020  O  O   . THR   B 737 ? 1.3059 1.2881 1.6352 -0.1148 -0.1173 -0.0265 1041 THR   B O   
8021  C  CB  . THR   B 737 ? 1.3026 1.2595 1.6074 -0.1079 -0.1326 -0.0298 1041 THR   B CB  
8022  O  OG1 . THR   B 737 ? 1.3769 1.3237 1.6895 -0.1131 -0.1272 -0.0279 1041 THR   B OG1 
8023  C  CG2 . THR   B 737 ? 1.2629 1.2275 1.5892 -0.1102 -0.1397 -0.0359 1041 THR   B CG2 
8024  N  N   . SER   B 738 ? 1.3433 1.3091 1.6634 -0.1187 -0.1038 -0.0186 1042 SER   B N   
8025  C  CA  . SER   B 738 ? 1.3353 1.3067 1.6728 -0.1246 -0.0940 -0.0166 1042 SER   B CA  
8026  C  C   . SER   B 738 ? 1.3358 1.3067 1.7009 -0.1308 -0.0963 -0.0207 1042 SER   B C   
8027  O  O   . SER   B 738 ? 1.3355 1.2968 1.7045 -0.1322 -0.1008 -0.0227 1042 SER   B O   
8028  C  CB  . SER   B 738 ? 1.3698 1.3344 1.6972 -0.1263 -0.0810 -0.0094 1042 SER   B CB  
8029  O  OG  . SER   B 738 ? 1.3814 1.3470 1.6843 -0.1205 -0.0795 -0.0059 1042 SER   B OG  
8030  N  N   . LEU   B 739 ? 1.3553 1.3364 1.7397 -0.1345 -0.0934 -0.0220 1043 LEU   B N   
8031  C  CA  . LEU   B 739 ? 1.3907 1.3743 1.8036 -0.1399 -0.0972 -0.0269 1043 LEU   B CA  
8032  C  C   . LEU   B 739 ? 1.4098 1.3931 1.8408 -0.1470 -0.0843 -0.0232 1043 LEU   B C   
8033  O  O   . LEU   B 739 ? 1.4242 1.4060 1.8453 -0.1475 -0.0723 -0.0170 1043 LEU   B O   
8034  C  CB  . LEU   B 739 ? 1.3599 1.3563 1.7834 -0.1382 -0.1055 -0.0323 1043 LEU   B CB  
8035  C  CG  . LEU   B 739 ? 1.3100 1.3047 1.7255 -0.1328 -0.1206 -0.0381 1043 LEU   B CG  
8036  C  CD1 . LEU   B 739 ? 1.3305 1.3362 1.7628 -0.1325 -0.1289 -0.0442 1043 LEU   B CD1 
8037  C  CD2 . LEU   B 739 ? 1.3540 1.3364 1.7737 -0.1346 -0.1258 -0.0404 1043 LEU   B CD2 
8038  N  N   . SER   B 740 ? 1.4737 1.4585 1.9321 -0.1525 -0.0870 -0.0273 1044 SER   B N   
8039  C  CA  . SER   B 740 ? 1.5130 1.4971 1.9931 -0.1599 -0.0755 -0.0246 1044 SER   B CA  
8040  C  C   . SER   B 740 ? 1.5304 1.5285 2.0335 -0.1626 -0.0745 -0.0272 1044 SER   B C   
8041  O  O   . SER   B 740 ? 1.5554 1.5604 2.0711 -0.1617 -0.0863 -0.0338 1044 SER   B O   
8042  C  CB  . SER   B 740 ? 1.4619 1.4365 1.9582 -0.1646 -0.0788 -0.0272 1044 SER   B CB  
8043  O  OG  . SER   B 740 ? 1.4869 1.4499 1.9620 -0.1606 -0.0848 -0.0271 1044 SER   B OG  
8044  N  N   . GLU   B 741 ? 1.5569 1.5585 2.0650 -0.1656 -0.0605 -0.0220 1045 GLU   B N   
8045  C  CA  . GLU   B 741 ? 1.5168 1.5320 2.0430 -0.1673 -0.0581 -0.0235 1045 GLU   B CA  
8046  C  C   . GLU   B 741 ? 1.5029 1.5247 2.0573 -0.1700 -0.0689 -0.0311 1045 GLU   B C   
8047  O  O   . GLU   B 741 ? 1.4393 1.4722 1.9997 -0.1677 -0.0762 -0.0354 1045 GLU   B O   
8048  C  CB  . GLU   B 741 ? 1.5241 1.5390 2.0598 -0.1721 -0.0409 -0.0174 1045 GLU   B CB  
8049  C  CG  . GLU   B 741 ? 1.5333 1.5620 2.0914 -0.1745 -0.0378 -0.0191 1045 GLU   B CG  
8050  C  CD  . GLU   B 741 ? 1.5582 1.5877 2.1147 -0.1763 -0.0208 -0.0122 1045 GLU   B CD  
8051  O  OE1 . GLU   B 741 ? 1.5619 1.5808 2.1134 -0.1789 -0.0094 -0.0066 1045 GLU   B OE1 
8052  O  OE2 . GLU   B 741 ? 1.5911 1.6316 2.1508 -0.1749 -0.0188 -0.0124 1045 GLU   B OE2 
8053  N  N   . SER   B 742 ? 1.7280 1.7428 2.2997 -0.1749 -0.0706 -0.0331 1046 SER   B N   
8054  C  CA  . SER   B 742 ? 1.7459 1.7658 2.3431 -0.1771 -0.0829 -0.0410 1046 SER   B CA  
8055  C  C   . SER   B 742 ? 1.7272 1.7482 2.3093 -0.1702 -0.0995 -0.0468 1046 SER   B C   
8056  O  O   . SER   B 742 ? 1.6942 1.7255 2.2862 -0.1683 -0.1081 -0.0520 1046 SER   B O   
8057  C  CB  . SER   B 742 ? 1.8116 1.8218 2.4268 -0.1831 -0.0826 -0.0421 1046 SER   B CB  
8058  O  OG  . SER   B 742 ? 1.8868 1.9007 2.5245 -0.1845 -0.0965 -0.0503 1046 SER   B OG  
8059  N  N   . TRP   B 743 ? 1.5615 1.5717 2.1192 -0.1662 -0.1039 -0.0458 1047 TRP   B N   
8060  C  CA  . TRP   B 743 ? 1.5124 1.5220 2.0554 -0.1596 -0.1193 -0.0511 1047 TRP   B CA  
8061  C  C   . TRP   B 743 ? 1.4702 1.4912 2.0030 -0.1543 -0.1217 -0.0518 1047 TRP   B C   
8062  O  O   . TRP   B 743 ? 1.3817 1.4093 1.9224 -0.1518 -0.1332 -0.0581 1047 TRP   B O   
8063  C  CB  . TRP   B 743 ? 1.4872 1.4837 2.0025 -0.1556 -0.1207 -0.0484 1047 TRP   B CB  
8064  C  CG  . TRP   B 743 ? 1.5586 1.5427 2.0817 -0.1591 -0.1241 -0.0501 1047 TRP   B CG  
8065  C  CD1 . TRP   B 743 ? 1.5794 1.5530 2.1003 -0.1630 -0.1139 -0.0449 1047 TRP   B CD1 
8066  C  CD2 . TRP   B 743 ? 1.5218 1.5016 2.0546 -0.1585 -0.1388 -0.0576 1047 TRP   B CD2 
8067  N  NE1 . TRP   B 743 ? 1.5681 1.5316 2.0976 -0.1653 -0.1212 -0.0486 1047 TRP   B NE1 
8068  C  CE2 . TRP   B 743 ? 1.5426 1.5097 2.0795 -0.1626 -0.1367 -0.0565 1047 TRP   B CE2 
8069  C  CE3 . TRP   B 743 ? 1.4415 1.4265 1.9795 -0.1548 -0.1537 -0.0651 1047 TRP   B CE3 
8070  C  CZ2 . TRP   B 743 ? 1.5435 1.5032 2.0897 -0.1632 -0.1493 -0.0628 1047 TRP   B CZ2 
8071  C  CZ3 . TRP   B 743 ? 1.3929 1.3702 1.9395 -0.1551 -0.1662 -0.0714 1047 TRP   B CZ3 
8072  C  CH2 . TRP   B 743 ? 1.4755 1.4404 2.0263 -0.1593 -0.1641 -0.0702 1047 TRP   B CH2 
8073  N  N   . TYR   B 744 ? 1.4729 1.4961 1.9885 -0.1526 -0.1107 -0.0454 1048 TYR   B N   
8074  C  CA  . TYR   B 744 ? 1.3775 1.4107 1.8813 -0.1476 -0.1121 -0.0454 1048 TYR   B CA  
8075  C  C   . TYR   B 744 ? 1.3727 1.4182 1.9010 -0.1495 -0.1159 -0.0502 1048 TYR   B C   
8076  O  O   . TYR   B 744 ? 1.3634 1.4150 1.8872 -0.1447 -0.1258 -0.0545 1048 TYR   B O   
8077  C  CB  . TYR   B 744 ? 1.3173 1.3511 1.8047 -0.1472 -0.0982 -0.0377 1048 TYR   B CB  
8078  C  CG  . TYR   B 744 ? 1.3402 1.3847 1.8181 -0.1430 -0.0980 -0.0373 1048 TYR   B CG  
8079  C  CD1 . TYR   B 744 ? 1.2829 1.3278 1.7380 -0.1361 -0.1059 -0.0384 1048 TYR   B CD1 
8080  C  CD2 . TYR   B 744 ? 1.2892 1.3432 1.7812 -0.1459 -0.0895 -0.0356 1048 TYR   B CD2 
8081  C  CE1 . TYR   B 744 ? 1.2457 1.3001 1.6926 -0.1325 -0.1055 -0.0379 1048 TYR   B CE1 
8082  C  CE2 . TYR   B 744 ? 1.2192 1.2824 1.7024 -0.1422 -0.0893 -0.0353 1048 TYR   B CE2 
8083  C  CZ  . TYR   B 744 ? 1.2392 1.3025 1.7000 -0.1356 -0.0974 -0.0364 1048 TYR   B CZ  
8084  O  OH  . TYR   B 744 ? 1.2765 1.3487 1.7288 -0.1321 -0.0970 -0.0360 1048 TYR   B OH  
8085  N  N   . ASN   B 745 ? 1.4107 1.4597 1.9650 -0.1562 -0.1080 -0.0494 1049 ASN   B N   
8086  C  CA  . ASN   B 745 ? 1.3690 1.4301 1.9484 -0.1581 -0.1110 -0.0539 1049 ASN   B CA  
8087  C  C   . ASN   B 745 ? 1.3380 1.3997 1.9288 -0.1564 -0.1279 -0.0624 1049 ASN   B C   
8088  O  O   . ASN   B 745 ? 1.3470 1.4171 1.9401 -0.1527 -0.1363 -0.0669 1049 ASN   B O   
8089  C  CB  . ASN   B 745 ? 1.3475 1.4113 1.9545 -0.1659 -0.0994 -0.0516 1049 ASN   B CB  
8090  C  CG  . ASN   B 745 ? 1.3732 1.4355 1.9693 -0.1674 -0.0822 -0.0431 1049 ASN   B CG  
8091  O  OD1 . ASN   B 745 ? 1.3757 1.4308 1.9783 -0.1724 -0.0721 -0.0390 1049 ASN   B OD1 
8092  N  ND2 . ASN   B 745 ? 1.3359 1.4041 1.9147 -0.1631 -0.0789 -0.0405 1049 ASN   B ND2 
8093  N  N   . LEU   B 746 ? 1.3380 1.3901 1.9354 -0.1588 -0.1332 -0.0648 1050 LEU   B N   
8094  C  CA  . LEU   B 746 ? 1.3275 1.3785 1.9361 -0.1573 -0.1496 -0.0731 1050 LEU   B CA  
8095  C  C   . LEU   B 746 ? 1.3245 1.3751 1.9084 -0.1487 -0.1614 -0.0762 1050 LEU   B C   
8096  O  O   . LEU   B 746 ? 1.2646 1.3215 1.8562 -0.1457 -0.1723 -0.0824 1050 LEU   B O   
8097  C  CB  . LEU   B 746 ? 1.3214 1.3599 1.9356 -0.1609 -0.1523 -0.0741 1050 LEU   B CB  
8098  C  CG  . LEU   B 746 ? 1.2816 1.3164 1.9073 -0.1598 -0.1694 -0.0828 1050 LEU   B CG  
8099  C  CD1 . LEU   B 746 ? 1.2478 1.2737 1.8431 -0.1519 -0.1799 -0.0845 1050 LEU   B CD1 
8100  C  CD2 . LEU   B 746 ? 1.1917 1.2389 1.8393 -0.1595 -0.1772 -0.0890 1050 LEU   B CD2 
8101  N  N   . LEU   B 747 ? 1.3049 1.3479 1.8589 -0.1444 -0.1589 -0.0719 1051 LEU   B N   
8102  C  CA  . LEU   B 747 ? 1.2682 1.3105 1.7971 -0.1361 -0.1680 -0.0738 1051 LEU   B CA  
8103  C  C   . LEU   B 747 ? 1.3265 1.3811 1.8540 -0.1332 -0.1670 -0.0740 1051 LEU   B C   
8104  O  O   . LEU   B 747 ? 1.3506 1.4081 1.8731 -0.1278 -0.1783 -0.0790 1051 LEU   B O   
8105  C  CB  . LEU   B 747 ? 1.2531 1.2865 1.7522 -0.1327 -0.1629 -0.0681 1051 LEU   B CB  
8106  C  CG  . LEU   B 747 ? 1.2044 1.2242 1.6971 -0.1325 -0.1684 -0.0693 1051 LEU   B CG  
8107  C  CD1 . LEU   B 747 ? 1.1407 1.1574 1.6324 -0.1276 -0.1853 -0.0771 1051 LEU   B CD1 
8108  C  CD2 . LEU   B 747 ? 1.3302 1.3462 1.8464 -0.1408 -0.1622 -0.0684 1051 LEU   B CD2 
8109  N  N   . LEU   B 748 ? 1.3032 1.3644 1.8334 -0.1363 -0.1535 -0.0683 1052 LEU   B N   
8110  C  CA  . LEU   B 748 ? 1.3019 1.3747 1.8318 -0.1339 -0.1518 -0.0683 1052 LEU   B CA  
8111  C  C   . LEU   B 748 ? 1.3273 1.4069 1.8771 -0.1331 -0.1637 -0.0761 1052 LEU   B C   
8112  O  O   . LEU   B 748 ? 1.3077 1.3913 1.8472 -0.1273 -0.1716 -0.0792 1052 LEU   B O   
8113  C  CB  . LEU   B 748 ? 1.2452 1.3240 1.7843 -0.1390 -0.1362 -0.0624 1052 LEU   B CB  
8114  C  CG  . LEU   B 748 ? 1.2403 1.3160 1.7520 -0.1364 -0.1267 -0.0553 1052 LEU   B CG  
8115  C  CD1 . LEU   B 748 ? 1.2880 1.3711 1.8057 -0.1393 -0.1134 -0.0505 1052 LEU   B CD1 
8116  C  CD2 . LEU   B 748 ? 1.2208 1.2974 1.7094 -0.1288 -0.1353 -0.0570 1052 LEU   B CD2 
8117  N  N   . ASP   B 749 ? 1.3053 1.3856 1.8836 -0.1389 -0.1652 -0.0794 1053 ASP   B N   
8118  C  CA  . ASP   B 749 ? 1.3578 1.4443 1.9576 -0.1384 -0.1770 -0.0872 1053 ASP   B CA  
8119  C  C   . ASP   B 749 ? 1.3473 1.4271 1.9332 -0.1318 -0.1934 -0.0933 1053 ASP   B C   
8120  O  O   . ASP   B 749 ? 1.3521 1.4370 1.9365 -0.1269 -0.2027 -0.0979 1053 ASP   B O   
8121  C  CB  . ASP   B 749 ? 1.3752 1.4626 2.0086 -0.1461 -0.1756 -0.0895 1053 ASP   B CB  
8122  C  CG  . ASP   B 749 ? 1.4325 1.5323 2.0939 -0.1478 -0.1792 -0.0944 1053 ASP   B CG  
8123  O  OD1 . ASP   B 749 ? 1.4508 1.5600 2.1107 -0.1468 -0.1723 -0.0918 1053 ASP   B OD1 
8124  O  OD2 . ASP   B 749 ? 1.4537 1.5534 2.1380 -0.1499 -0.1894 -0.1010 1053 ASP   B OD2 
8125  N  N   . MET   B 750 ? 1.3031 1.3708 1.8781 -0.1313 -0.1971 -0.0933 1054 MET   B N   
8126  C  CA  . MET   B 750 ? 1.2981 1.3579 1.8563 -0.1244 -0.2117 -0.0983 1054 MET   B CA  
8127  C  C   . MET   B 750 ? 1.2977 1.3610 1.8315 -0.1167 -0.2139 -0.0976 1054 MET   B C   
8128  O  O   . MET   B 750 ? 1.2464 1.3114 1.7790 -0.1115 -0.2257 -0.1034 1054 MET   B O   
8129  C  CB  . MET   B 750 ? 1.2973 1.3436 1.8400 -0.1243 -0.2114 -0.0960 1054 MET   B CB  
8130  C  CG  . MET   B 750 ? 1.3319 1.3721 1.8973 -0.1303 -0.2146 -0.0991 1054 MET   B CG  
8131  S  SD  . MET   B 750 ? 1.5708 1.6106 2.1533 -0.1276 -0.2345 -0.1102 1054 MET   B SD  
8132  C  CE  . MET   B 750 ? 1.4220 1.4506 1.9685 -0.1171 -0.2463 -0.1124 1054 MET   B CE  
8133  N  N   . GLN   B 751 ? 1.2813 1.3453 1.7952 -0.1158 -0.2026 -0.0904 1055 GLN   B N   
8134  C  CA  . GLN   B 751 ? 1.2581 1.3253 1.7485 -0.1090 -0.2031 -0.0888 1055 GLN   B CA  
8135  C  C   . GLN   B 751 ? 1.2306 1.3079 1.7320 -0.1068 -0.2088 -0.0933 1055 GLN   B C   
8136  O  O   . GLN   B 751 ? 1.2284 1.3042 1.7182 -0.1002 -0.2194 -0.0975 1055 GLN   B O   
8137  C  CB  . GLN   B 751 ? 1.2163 1.2860 1.6926 -0.1104 -0.1882 -0.0804 1055 GLN   B CB  
8138  C  CG  . GLN   B 751 ? 1.1627 1.2247 1.6077 -0.1047 -0.1882 -0.0769 1055 GLN   B CG  
8139  C  CD  . GLN   B 751 ? 1.1681 1.2308 1.6002 -0.1066 -0.1741 -0.0688 1055 GLN   B CD  
8140  O  OE1 . GLN   B 751 ? 1.1359 1.1910 1.5634 -0.1090 -0.1689 -0.0653 1055 GLN   B OE1 
8141  N  NE2 . GLN   B 751 ? 1.1630 1.2342 1.5883 -0.1051 -0.1682 -0.0659 1055 GLN   B NE2 
8142  N  N   . ASN   B 752 ? 1.2162 1.3033 1.7400 -0.1122 -0.2018 -0.0925 1056 ASN   B N   
8143  C  CA  . ASN   B 752 ? 1.2255 1.3224 1.7607 -0.1103 -0.2068 -0.0967 1056 ASN   B CA  
8144  C  C   . ASN   B 752 ? 1.2781 1.3727 1.8285 -0.1087 -0.2223 -0.1054 1056 ASN   B C   
8145  O  O   . ASN   B 752 ? 1.2331 1.3288 1.7768 -0.1025 -0.2325 -0.1100 1056 ASN   B O   
8146  C  CB  . ASN   B 752 ? 1.2232 1.3308 1.7797 -0.1165 -0.1952 -0.0937 1056 ASN   B CB  
8147  C  CG  . ASN   B 752 ? 1.3089 1.4173 1.8506 -0.1183 -0.1799 -0.0852 1056 ASN   B CG  
8148  O  OD1 . ASN   B 752 ? 1.3134 1.4198 1.8632 -0.1240 -0.1698 -0.0810 1056 ASN   B OD1 
8149  N  ND2 . ASN   B 752 ? 1.2303 1.3411 1.7497 -0.1131 -0.1781 -0.0826 1056 ASN   B ND2 
8150  N  N   . ARG   B 753 ? 1.3101 1.4007 1.8807 -0.1140 -0.2244 -0.1077 1057 ARG   B N   
8151  C  CA  . ARG   B 753 ? 1.2890 1.3757 1.8729 -0.1125 -0.2400 -0.1162 1057 ARG   B CA  
8152  C  C   . ARG   B 753 ? 1.3008 1.3789 1.8582 -0.1035 -0.2521 -0.1195 1057 ARG   B C   
8153  O  O   . ARG   B 753 ? 1.2840 1.3634 1.8429 -0.0985 -0.2639 -0.1257 1057 ARG   B O   
8154  C  CB  . ARG   B 753 ? 1.3565 1.4362 1.9571 -0.1187 -0.2403 -0.1171 1057 ARG   B CB  
8155  C  CG  . ARG   B 753 ? 1.3399 1.4273 1.9713 -0.1277 -0.2301 -0.1151 1057 ARG   B CG  
8156  C  CD  . ARG   B 753 ? 1.3617 1.4557 2.0244 -0.1297 -0.2398 -0.1227 1057 ARG   B CD  
8157  N  NE  . ARG   B 753 ? 1.4028 1.5022 2.0966 -0.1387 -0.2307 -0.1211 1057 ARG   B NE  
8158  C  CZ  . ARG   B 753 ? 1.5530 1.6487 2.2706 -0.1436 -0.2362 -0.1253 1057 ARG   B CZ  
8159  N  NH1 . ARG   B 753 ? 1.5817 1.6681 2.2959 -0.1403 -0.2516 -0.1318 1057 ARG   B NH1 
8160  N  NH2 . ARG   B 753 ? 1.6431 1.7444 2.3889 -0.1519 -0.2261 -0.1231 1057 ARG   B NH2 
8161  N  N   . LEU   B 754 ? 1.2935 1.3623 1.8257 -0.1010 -0.2490 -0.1153 1058 LEU   B N   
8162  C  CA  . LEU   B 754 ? 1.2973 1.3574 1.8028 -0.0922 -0.2590 -0.1177 1058 LEU   B CA  
8163  C  C   . LEU   B 754 ? 1.2759 1.3427 1.7675 -0.0863 -0.2592 -0.1173 1058 LEU   B C   
8164  O  O   . LEU   B 754 ? 1.2882 1.3527 1.7743 -0.0800 -0.2713 -0.1230 1058 LEU   B O   
8165  C  CB  . LEU   B 754 ? 1.2505 1.3006 1.7322 -0.0909 -0.2540 -0.1126 1058 LEU   B CB  
8166  C  CG  . LEU   B 754 ? 1.2250 1.2696 1.7184 -0.0977 -0.2489 -0.1105 1058 LEU   B CG  
8167  C  CD1 . LEU   B 754 ? 1.2401 1.2729 1.7072 -0.0941 -0.2484 -0.1073 1058 LEU   B CD1 
8168  C  CD2 . LEU   B 754 ? 1.3034 1.3452 1.8217 -0.1007 -0.2597 -0.1178 1058 LEU   B CD2 
8169  N  N   . ASN   B 755 ? 1.2275 1.3020 1.7130 -0.0882 -0.2460 -0.1106 1059 ASN   B N   
8170  C  CA  . ASN   B 755 ? 1.2851 1.3647 1.7539 -0.0823 -0.2455 -0.1095 1059 ASN   B CA  
8171  C  C   . ASN   B 755 ? 1.2931 1.3773 1.7729 -0.0788 -0.2564 -0.1164 1059 ASN   B C   
8172  O  O   . ASN   B 755 ? 1.2165 1.3007 1.6788 -0.0720 -0.2603 -0.1172 1059 ASN   B O   
8173  C  CB  . ASN   B 755 ? 1.2147 1.3034 1.6826 -0.0862 -0.2302 -0.1023 1059 ASN   B CB  
8174  C  CG  . ASN   B 755 ? 1.2050 1.2882 1.6506 -0.0858 -0.2214 -0.0954 1059 ASN   B CG  
8175  O  OD1 . ASN   B 755 ? 1.1628 1.2392 1.5847 -0.0796 -0.2256 -0.0951 1059 ASN   B OD1 
8176  N  ND2 . ASN   B 755 ? 1.2225 1.3079 1.6756 -0.0923 -0.2093 -0.0900 1059 ASN   B ND2 
8177  N  N   . LYS   B 756 ? 1.3164 1.4037 1.8244 -0.0831 -0.2618 -0.1216 1060 LYS   B N   
8178  C  CA  . LYS   B 756 ? 1.2666 1.3572 1.7870 -0.0796 -0.2741 -0.1291 1060 LYS   B CA  
8179  C  C   . LYS   B 756 ? 1.2569 1.3357 1.7629 -0.0721 -0.2897 -0.1352 1060 LYS   B C   
8180  O  O   . LYS   B 756 ? 1.3198 1.3987 1.8192 -0.0656 -0.2986 -0.1396 1060 LYS   B O   
8181  C  CB  . LYS   B 756 ? 1.2295 1.3269 1.7859 -0.0868 -0.2750 -0.1326 1060 LYS   B CB  
8182  C  CG  . LYS   B 756 ? 1.3516 1.4623 1.9244 -0.0928 -0.2613 -0.1280 1060 LYS   B CG  
8183  C  CD  . LYS   B 756 ? 1.3705 1.4833 1.9666 -0.1021 -0.2522 -0.1252 1060 LYS   B CD  
8184  C  CE  . LYS   B 756 ? 1.3434 1.4693 1.9578 -0.1073 -0.2398 -0.1216 1060 LYS   B CE  
8185  N  NZ  . LYS   B 756 ? 1.4330 1.5639 2.0831 -0.1147 -0.2390 -0.1243 1060 LYS   B NZ  
8186  N  N   . VAL   B 757 ? 1.2414 1.3091 1.7414 -0.0724 -0.2932 -0.1358 1061 VAL   B N   
8187  C  CA  . VAL   B 757 ? 1.2184 1.2741 1.7067 -0.0654 -0.3087 -0.1422 1061 VAL   B CA  
8188  C  C   . VAL   B 757 ? 1.2378 1.2845 1.6907 -0.0578 -0.3082 -0.1389 1061 VAL   B C   
8189  O  O   . VAL   B 757 ? 1.3034 1.3432 1.7408 -0.0495 -0.3189 -0.1433 1061 VAL   B O   
8190  C  CB  . VAL   B 757 ? 1.2715 1.3193 1.7759 -0.0695 -0.3156 -0.1463 1061 VAL   B CB  
8191  C  CG1 . VAL   B 757 ? 1.2811 1.3388 1.8218 -0.0784 -0.3127 -0.1479 1061 VAL   B CG1 
8192  C  CG2 . VAL   B 757 ? 1.2880 1.3268 1.7768 -0.0712 -0.3088 -0.1409 1061 VAL   B CG2 
8193  N  N   . ILE   B 758 ? 1.2094 1.2556 1.6491 -0.0602 -0.2958 -0.1313 1062 ILE   B N   
8194  C  CA  . ILE   B 758 ? 1.2301 1.2677 1.6375 -0.0532 -0.2950 -0.1281 1062 ILE   B CA  
8195  C  C   . ILE   B 758 ? 1.2023 1.2460 1.5948 -0.0480 -0.2920 -0.1261 1062 ILE   B C   
8196  O  O   . ILE   B 758 ? 1.2290 1.2841 1.6289 -0.0519 -0.2820 -0.1220 1062 ILE   B O   
8197  C  CB  . ILE   B 758 ? 1.2219 1.2570 1.6202 -0.0572 -0.2833 -0.1209 1062 ILE   B CB  
8198  C  CG1 . ILE   B 758 ? 1.2492 1.2771 1.6610 -0.0619 -0.2867 -0.1231 1062 ILE   B CG1 
8199  C  CG2 . ILE   B 758 ? 1.2167 1.2426 1.5843 -0.0500 -0.2838 -0.1183 1062 ILE   B CG2 
8200  C  CD1 . ILE   B 758 ? 1.2782 1.3157 1.7201 -0.0718 -0.2792 -0.1219 1062 ILE   B CD1 
8201  N  N   . LYS   B 759 ? 1.1574 1.1928 1.5282 -0.0390 -0.3005 -0.1287 1063 LYS   B N   
8202  C  CA  . LYS   B 759 ? 1.1661 1.2055 1.5239 -0.0331 -0.3007 -0.1285 1063 LYS   B CA  
8203  C  C   . LYS   B 759 ? 1.2491 1.2881 1.5823 -0.0306 -0.2901 -0.1210 1063 LYS   B C   
8204  O  O   . LYS   B 759 ? 1.2736 1.3033 1.5898 -0.0278 -0.2900 -0.1191 1063 LYS   B O   
8205  C  CB  . LYS   B 759 ? 1.0832 1.1128 1.4311 -0.0242 -0.3159 -0.1357 1063 LYS   B CB  
8206  N  N   . SER   B 760 ? 1.1773 1.2268 1.5098 -0.0319 -0.2811 -0.1169 1064 SER   B N   
8207  C  CA  . SER   B 760 ? 1.1238 1.1744 1.4352 -0.0300 -0.2710 -0.1099 1064 SER   B CA  
8208  C  C   . SER   B 760 ? 1.1397 1.1835 1.4271 -0.0203 -0.2767 -0.1112 1064 SER   B C   
8209  O  O   . SER   B 760 ? 1.2745 1.3162 1.5630 -0.0156 -0.2863 -0.1168 1064 SER   B O   
8210  C  CB  . SER   B 760 ? 1.1082 1.1719 1.4279 -0.0352 -0.2594 -0.1051 1064 SER   B CB  
8211  O  OG  . SER   B 760 ? 1.1622 1.2270 1.4605 -0.0316 -0.2524 -0.0998 1064 SER   B OG  
8212  N  N   . VAL   B 761 ? 1.1102 1.1505 1.3759 -0.0172 -0.2705 -0.1060 1065 VAL   B N   
8213  C  CA  . VAL   B 761 ? 1.1650 1.1974 1.4070 -0.0077 -0.2753 -0.1069 1065 VAL   B CA  
8214  C  C   . VAL   B 761 ? 1.1938 1.2339 1.4301 -0.0056 -0.2706 -0.1047 1065 VAL   B C   
8215  O  O   . VAL   B 761 ? 1.2475 1.2830 1.4725 0.0016  -0.2770 -0.1078 1065 VAL   B O   
8216  C  CB  . VAL   B 761 ? 1.1881 1.2126 1.4099 -0.0047 -0.2714 -0.1026 1065 VAL   B CB  
8217  C  CG1 . VAL   B 761 ? 1.1495 1.1663 1.3466 0.0051  -0.2747 -0.1028 1065 VAL   B CG1 
8218  C  CG2 . VAL   B 761 ? 1.1216 1.1372 1.3487 -0.0061 -0.2776 -0.1056 1065 VAL   B CG2 
8219  N  N   . GLY   B 762 ? 1.1589 1.2099 1.4018 -0.0115 -0.2594 -0.0995 1066 GLY   B N   
8220  C  CA  . GLY   B 762 ? 1.1428 1.2015 1.3832 -0.0103 -0.2554 -0.0980 1066 GLY   B CA  
8221  C  C   . GLY   B 762 ? 1.1017 1.1697 1.3660 -0.0155 -0.2562 -0.1009 1066 GLY   B C   
8222  O  O   . GLY   B 762 ? 1.1139 1.1905 1.3810 -0.0168 -0.2509 -0.0990 1066 GLY   B O   
8223  N  N   . LYS   B 763 ? 1.0454 1.1117 1.3273 -0.0186 -0.2629 -0.1055 1067 LYS   B N   
8224  C  CA  . LYS   B 763 ? 1.0617 1.1378 1.3697 -0.0253 -0.2615 -0.1073 1067 LYS   B CA  
8225  C  C   . LYS   B 763 ? 1.0652 1.1509 1.3783 -0.0323 -0.2474 -0.1004 1067 LYS   B C   
8226  O  O   . LYS   B 763 ? 1.0682 1.1630 1.3868 -0.0341 -0.2419 -0.0988 1067 LYS   B O   
8227  C  CB  . LYS   B 763 ? 1.1096 1.1895 1.4235 -0.0219 -0.2678 -0.1119 1067 LYS   B CB  
8228  C  CG  . LYS   B 763 ? 1.2053 1.2754 1.5159 -0.0150 -0.2828 -0.1194 1067 LYS   B CG  
8229  C  CD  . LYS   B 763 ? 1.2482 1.3241 1.5805 -0.0161 -0.2900 -0.1254 1067 LYS   B CD  
8230  C  CE  . LYS   B 763 ? 1.2557 1.3256 1.5761 -0.0070 -0.3006 -0.1306 1067 LYS   B CE  
8231  N  NZ  . LYS   B 763 ? 1.2833 1.3617 1.6235 -0.0081 -0.3047 -0.1349 1067 LYS   B NZ  
8232  N  N   . ILE   B 764 ? 1.0631 1.1459 1.3728 -0.0356 -0.2417 -0.0964 1068 ILE   B N   
8233  C  CA  . ILE   B 764 ? 0.9829 1.0726 1.2950 -0.0417 -0.2287 -0.0898 1068 ILE   B CA  
8234  C  C   . ILE   B 764 ? 1.0233 1.1154 1.3578 -0.0494 -0.2262 -0.0902 1068 ILE   B C   
8235  O  O   . ILE   B 764 ? 1.0638 1.1489 1.4034 -0.0499 -0.2324 -0.0933 1068 ILE   B O   
8236  C  CB  . ILE   B 764 ? 1.0009 1.0854 1.2908 -0.0392 -0.2235 -0.0845 1068 ILE   B CB  
8237  C  CG1 . ILE   B 764 ? 1.0155 1.0969 1.2844 -0.0314 -0.2265 -0.0846 1068 ILE   B CG1 
8238  C  CG2 . ILE   B 764 ? 0.9778 1.0691 1.2686 -0.0448 -0.2106 -0.0778 1068 ILE   B CG2 
8239  C  CD1 . ILE   B 764 ? 0.9826 1.0632 1.2321 -0.0297 -0.2184 -0.0782 1068 ILE   B CD1 
8240  N  N   . GLU   B 765 ? 0.9971 1.0988 1.3450 -0.0553 -0.2171 -0.0872 1069 GLU   B N   
8241  C  CA  . GLU   B 765 ? 1.0038 1.1082 1.3737 -0.0628 -0.2131 -0.0870 1069 GLU   B CA  
8242  C  C   . GLU   B 765 ? 1.0144 1.1138 1.3769 -0.0659 -0.2059 -0.0819 1069 GLU   B C   
8243  O  O   . GLU   B 765 ? 0.9596 1.0609 1.3091 -0.0664 -0.1968 -0.0760 1069 GLU   B O   
8244  C  CB  . GLU   B 765 ? 1.0014 1.1171 1.3866 -0.0676 -0.2048 -0.0851 1069 GLU   B CB  
8245  C  CG  . GLU   B 765 ? 1.1204 1.2419 1.5178 -0.0657 -0.2113 -0.0903 1069 GLU   B CG  
8246  C  CD  . GLU   B 765 ? 1.2053 1.3249 1.6233 -0.0669 -0.2213 -0.0969 1069 GLU   B CD  
8247  O  OE1 . GLU   B 765 ? 1.2540 1.3693 1.6807 -0.0710 -0.2208 -0.0968 1069 GLU   B OE1 
8248  O  OE2 . GLU   B 765 ? 1.2421 1.3641 1.6673 -0.0637 -0.2298 -0.1023 1069 GLU   B OE2 
8249  N  N   . HIS   B 766 ? 1.0112 1.1042 1.3826 -0.0682 -0.2101 -0.0842 1070 HIS   B N   
8250  C  CA  . HIS   B 766 ? 1.0455 1.1334 1.4118 -0.0716 -0.2033 -0.0796 1070 HIS   B CA  
8251  C  C   . HIS   B 766 ? 1.0621 1.1569 1.4313 -0.0768 -0.1895 -0.0732 1070 HIS   B C   
8252  O  O   . HIS   B 766 ? 1.0752 1.1672 1.4290 -0.0767 -0.1826 -0.0679 1070 HIS   B O   
8253  C  CB  . HIS   B 766 ? 1.0846 1.1669 1.4676 -0.0754 -0.2082 -0.0831 1070 HIS   B CB  
8254  C  CG  . HIS   B 766 ? 1.0848 1.1620 1.4655 -0.0796 -0.2004 -0.0784 1070 HIS   B CG  
8255  N  ND1 . HIS   B 766 ? 1.1228 1.2041 1.5193 -0.0869 -0.1905 -0.0751 1070 HIS   B ND1 
8256  C  CD2 . HIS   B 766 ? 1.0218 1.0896 1.3855 -0.0773 -0.2008 -0.0762 1070 HIS   B CD2 
8257  C  CE1 . HIS   B 766 ? 1.1355 1.2099 1.5245 -0.0889 -0.1853 -0.0711 1070 HIS   B CE1 
8258  N  NE2 . HIS   B 766 ? 1.0525 1.1189 1.4219 -0.0832 -0.1916 -0.0718 1070 HIS   B NE2 
8259  N  N   . SER   B 767 ? 1.0757 1.1793 1.4638 -0.0811 -0.1854 -0.0737 1071 SER   B N   
8260  C  CA  . SER   B 767 ? 1.0766 1.1855 1.4678 -0.0861 -0.1721 -0.0677 1071 SER   B CA  
8261  C  C   . SER   B 767 ? 1.0714 1.1839 1.4431 -0.0828 -0.1666 -0.0634 1071 SER   B C   
8262  O  O   . SER   B 767 ? 1.0740 1.1862 1.4365 -0.0847 -0.1570 -0.0576 1071 SER   B O   
8263  C  CB  . SER   B 767 ? 1.0981 1.2151 1.5152 -0.0913 -0.1690 -0.0695 1071 SER   B CB  
8264  O  OG  . SER   B 767 ? 1.2718 1.3856 1.7081 -0.0946 -0.1743 -0.0736 1071 SER   B OG  
8265  N  N   . PHE   B 768 ? 1.0070 1.1228 1.3723 -0.0778 -0.1725 -0.0662 1072 PHE   B N   
8266  C  CA  . PHE   B 768 ? 0.9162 1.0341 1.2616 -0.0742 -0.1684 -0.0624 1072 PHE   B CA  
8267  C  C   . PHE   B 768 ? 0.9588 1.0693 1.2841 -0.0718 -0.1670 -0.0588 1072 PHE   B C   
8268  O  O   . PHE   B 768 ? 0.9497 1.0612 1.2646 -0.0730 -0.1584 -0.0533 1072 PHE   B O   
8269  C  CB  . PHE   B 768 ? 0.9123 1.0323 1.2522 -0.0684 -0.1764 -0.0664 1072 PHE   B CB  
8270  C  CG  . PHE   B 768 ? 0.9475 1.0699 1.2683 -0.0648 -0.1724 -0.0627 1072 PHE   B CG  
8271  C  CD1 . PHE   B 768 ? 0.8205 0.9509 1.1442 -0.0668 -0.1652 -0.0602 1072 PHE   B CD1 
8272  C  CD2 . PHE   B 768 ? 1.0201 1.1365 1.3203 -0.0593 -0.1758 -0.0619 1072 PHE   B CD2 
8273  C  CE1 . PHE   B 768 ? 0.8815 1.0137 1.1882 -0.0637 -0.1618 -0.0570 1072 PHE   B CE1 
8274  C  CE2 . PHE   B 768 ? 0.9821 1.1010 1.2660 -0.0563 -0.1719 -0.0584 1072 PHE   B CE2 
8275  C  CZ  . PHE   B 768 ? 0.8782 1.0048 1.1656 -0.0586 -0.1652 -0.0561 1072 PHE   B CZ  
8276  N  N   . TRP   B 769 ? 1.0037 1.1064 1.3236 -0.0684 -0.1756 -0.0620 1073 TRP   B N   
8277  C  CA  . TRP   B 769 ? 0.9929 1.0884 1.2926 -0.0648 -0.1757 -0.0592 1073 TRP   B CA  
8278  C  C   . TRP   B 769 ? 0.9637 1.0565 1.2625 -0.0693 -0.1671 -0.0542 1073 TRP   B C   
8279  O  O   . TRP   B 769 ? 0.9574 1.0483 1.2396 -0.0675 -0.1625 -0.0497 1073 TRP   B O   
8280  C  CB  . TRP   B 769 ? 0.9587 1.0456 1.2547 -0.0604 -0.1869 -0.0641 1073 TRP   B CB  
8281  C  CG  . TRP   B 769 ? 0.9456 1.0234 1.2272 -0.0583 -0.1873 -0.0620 1073 TRP   B CG  
8282  C  CD1 . TRP   B 769 ? 0.9461 1.0161 1.2330 -0.0598 -0.1912 -0.0639 1073 TRP   B CD1 
8283  C  CD2 . TRP   B 769 ? 0.9376 1.0131 1.1978 -0.0544 -0.1838 -0.0577 1073 TRP   B CD2 
8284  N  NE1 . TRP   B 769 ? 0.9425 1.0053 1.2120 -0.0568 -0.1902 -0.0610 1073 TRP   B NE1 
8285  C  CE2 . TRP   B 769 ? 0.9631 1.0294 1.2165 -0.0534 -0.1857 -0.0572 1073 TRP   B CE2 
8286  C  CE3 . TRP   B 769 ? 0.9670 1.0474 1.2141 -0.0516 -0.1792 -0.0542 1073 TRP   B CE3 
8287  C  CZ2 . TRP   B 769 ? 0.9784 1.0406 1.2123 -0.0495 -0.1832 -0.0534 1073 TRP   B CZ2 
8288  C  CZ3 . TRP   B 769 ? 0.9536 1.0300 1.1820 -0.0480 -0.1768 -0.0504 1073 TRP   B CZ3 
8289  C  CH2 . TRP   B 769 ? 0.9367 1.0044 1.1589 -0.0469 -0.1788 -0.0501 1073 TRP   B CH2 
8290  N  N   . ARG   B 770 ? 0.9412 1.0335 1.2577 -0.0750 -0.1649 -0.0549 1074 ARG   B N   
8291  C  CA  . ARG   B 770 ? 1.0082 1.0964 1.3236 -0.0791 -0.1570 -0.0503 1074 ARG   B CA  
8292  C  C   . ARG   B 770 ? 1.0179 1.1124 1.3349 -0.0829 -0.1454 -0.0452 1074 ARG   B C   
8293  O  O   . ARG   B 770 ? 1.0094 1.1004 1.3191 -0.0848 -0.1381 -0.0403 1074 ARG   B O   
8294  C  CB  . ARG   B 770 ? 1.0362 1.1198 1.3694 -0.0835 -0.1592 -0.0529 1074 ARG   B CB  
8295  C  CG  . ARG   B 770 ? 0.9734 1.0477 1.3011 -0.0801 -0.1689 -0.0565 1074 ARG   B CG  
8296  C  CD  . ARG   B 770 ? 0.9018 0.9705 1.2054 -0.0754 -0.1682 -0.0531 1074 ARG   B CD  
8297  N  NE  . ARG   B 770 ? 0.9639 1.0227 1.2620 -0.0722 -0.1767 -0.0562 1074 ARG   B NE  
8298  C  CZ  . ARG   B 770 ? 1.0078 1.0602 1.2861 -0.0674 -0.1782 -0.0544 1074 ARG   B CZ  
8299  N  NH1 . ARG   B 770 ? 1.0603 1.1153 1.3227 -0.0650 -0.1722 -0.0496 1074 ARG   B NH1 
8300  N  NH2 . ARG   B 770 ? 0.9841 1.0270 1.2587 -0.0647 -0.1860 -0.0576 1074 ARG   B NH2 
8301  N  N   . SER   B 771 ? 1.0890 1.1919 1.4145 -0.0836 -0.1440 -0.0462 1075 SER   B N   
8302  C  CA  . SER   B 771 ? 1.1286 1.2374 1.4547 -0.0866 -0.1336 -0.0417 1075 SER   B CA  
8303  C  C   . SER   B 771 ? 1.1322 1.2388 1.4368 -0.0843 -0.1284 -0.0364 1075 SER   B C   
8304  O  O   . SER   B 771 ? 1.1452 1.2504 1.4343 -0.0792 -0.1331 -0.0367 1075 SER   B O   
8305  C  CB  . SER   B 771 ? 1.1441 1.2617 1.4771 -0.0856 -0.1351 -0.0442 1075 SER   B CB  
8306  O  OG  . SER   B 771 ? 1.2261 1.3495 1.5629 -0.0888 -0.1254 -0.0406 1075 SER   B OG  
8307  N  N   . PHE   B 772 ? 1.1096 1.2154 1.4133 -0.0879 -0.1185 -0.0316 1076 PHE   B N   
8308  C  CA  . PHE   B 772 ? 1.0937 1.1972 1.3781 -0.0860 -0.1135 -0.0266 1076 PHE   B CA  
8309  C  C   . PHE   B 772 ? 1.1160 1.2260 1.3905 -0.0826 -0.1137 -0.0260 1076 PHE   B C   
8310  O  O   . PHE   B 772 ? 1.1084 1.2250 1.3914 -0.0841 -0.1113 -0.0267 1076 PHE   B O   
8311  C  CB  . PHE   B 772 ? 1.0926 1.1940 1.3794 -0.0905 -0.1029 -0.0219 1076 PHE   B CB  
8312  C  CG  . PHE   B 772 ? 1.0940 1.1933 1.3622 -0.0887 -0.0975 -0.0168 1076 PHE   B CG  
8313  C  CD1 . PHE   B 772 ? 1.1000 1.2050 1.3604 -0.0873 -0.0944 -0.0149 1076 PHE   B CD1 
8314  C  CD2 . PHE   B 772 ? 1.1146 1.2056 1.3732 -0.0886 -0.0956 -0.0140 1076 PHE   B CD2 
8315  C  CE1 . PHE   B 772 ? 1.1190 1.2218 1.3628 -0.0857 -0.0899 -0.0105 1076 PHE   B CE1 
8316  C  CE2 . PHE   B 772 ? 1.0934 1.1823 1.3352 -0.0868 -0.0910 -0.0094 1076 PHE   B CE2 
8317  C  CZ  . PHE   B 772 ? 1.1002 1.1951 1.3349 -0.0854 -0.0883 -0.0078 1076 PHE   B CZ  
8318  N  N   . HIS   B 773 ? 1.0910 1.1989 1.3477 -0.0781 -0.1163 -0.0246 1077 HIS   B N   
8319  C  CA  . HIS   B 773 ? 1.1320 1.2454 1.3794 -0.0744 -0.1182 -0.0247 1077 HIS   B CA  
8320  C  C   . HIS   B 773 ? 1.0980 1.2106 1.3280 -0.0724 -0.1139 -0.0201 1077 HIS   B C   
8321  O  O   . HIS   B 773 ? 1.0262 1.1342 1.2445 -0.0691 -0.1169 -0.0193 1077 HIS   B O   
8322  C  CB  . HIS   B 773 ? 1.1455 1.2579 1.3903 -0.0697 -0.1280 -0.0291 1077 HIS   B CB  
8323  C  CG  . HIS   B 773 ? 1.1592 1.2771 1.3970 -0.0661 -0.1298 -0.0298 1077 HIS   B CG  
8324  N  ND1 . HIS   B 773 ? 1.1759 1.3007 1.4215 -0.0679 -0.1272 -0.0303 1077 HIS   B ND1 
8325  C  CD2 . HIS   B 773 ? 1.1485 1.2657 1.3721 -0.0610 -0.1335 -0.0297 1077 HIS   B CD2 
8326  C  CE1 . HIS   B 773 ? 1.2151 1.3430 1.4515 -0.0641 -0.1294 -0.0306 1077 HIS   B CE1 
8327  N  NE2 . HIS   B 773 ? 1.2210 1.3445 1.4442 -0.0599 -0.1330 -0.0302 1077 HIS   B NE2 
8328  N  N   . THR   B 774 ? 1.1958 1.3128 1.4241 -0.0741 -0.1073 -0.0172 1078 THR   B N   
8329  C  CA  . THR   B 774 ? 1.2077 1.3257 1.4207 -0.0720 -0.1042 -0.0135 1078 THR   B CA  
8330  C  C   . THR   B 774 ? 1.3134 1.4374 1.5220 -0.0688 -0.1076 -0.0150 1078 THR   B C   
8331  O  O   . THR   B 774 ? 1.2314 1.3584 1.4480 -0.0680 -0.1121 -0.0188 1078 THR   B O   
8332  C  CB  . THR   B 774 ? 1.2509 1.3696 1.4632 -0.0753 -0.0955 -0.0095 1078 THR   B CB  
8333  O  OG1 . THR   B 774 ? 1.3150 1.4404 1.5319 -0.0761 -0.0935 -0.0102 1078 THR   B OG1 
8334  C  CG2 . THR   B 774 ? 1.2335 1.3478 1.4561 -0.0796 -0.0910 -0.0088 1078 THR   B CG2 
8335  N  N   . GLU   B 775 ? 1.4683 1.5935 1.6639 -0.0668 -0.1055 -0.0119 1079 GLU   B N   
8336  C  CA  . GLU   B 775 ? 1.4746 1.6051 1.6652 -0.0640 -0.1075 -0.0126 1079 GLU   B CA  
8337  C  C   . GLU   B 775 ? 1.4682 1.6043 1.6682 -0.0664 -0.1051 -0.0139 1079 GLU   B C   
8338  O  O   . GLU   B 775 ? 1.4515 1.5913 1.6529 -0.0644 -0.1087 -0.0164 1079 GLU   B O   
8339  C  CB  . GLU   B 775 ? 1.4661 1.5971 1.6429 -0.0623 -0.1049 -0.0088 1079 GLU   B CB  
8340  N  N   . ARG   B 776 ? 1.3905 1.5266 1.5968 -0.0705 -0.0988 -0.0121 1080 ARG   B N   
8341  C  CA  . ARG   B 776 ? 1.3260 1.4673 1.5403 -0.0726 -0.0956 -0.0128 1080 ARG   B CA  
8342  C  C   . ARG   B 776 ? 1.3021 1.4431 1.5322 -0.0766 -0.0927 -0.0141 1080 ARG   B C   
8343  O  O   . ARG   B 776 ? 1.2594 1.4042 1.4965 -0.0787 -0.0885 -0.0140 1080 ARG   B O   
8344  C  CB  . ARG   B 776 ? 1.3408 1.4835 1.5460 -0.0733 -0.0896 -0.0091 1080 ARG   B CB  
8345  N  N   . LYS   B 777 ? 1.2916 1.4281 1.5280 -0.0777 -0.0947 -0.0152 1081 LYS   B N   
8346  C  CA  . LYS   B 777 ? 1.2468 1.3827 1.4993 -0.0818 -0.0917 -0.0162 1081 LYS   B CA  
8347  C  C   . LYS   B 777 ? 1.2330 1.3666 1.4949 -0.0814 -0.0989 -0.0203 1081 LYS   B C   
8348  O  O   . LYS   B 777 ? 1.2256 1.3556 1.4788 -0.0782 -0.1046 -0.0211 1081 LYS   B O   
8349  C  CB  . LYS   B 777 ? 1.1650 1.2958 1.4154 -0.0849 -0.0837 -0.0120 1081 LYS   B CB  
8350  N  N   . THR   B 778 ? 1.1628 1.2984 1.4429 -0.0845 -0.0987 -0.0229 1082 THR   B N   
8351  C  CA  . THR   B 778 ? 1.1731 1.3062 1.4643 -0.0846 -0.1056 -0.0271 1082 THR   B CA  
8352  C  C   . THR   B 778 ? 1.2298 1.3640 1.5409 -0.0897 -0.1013 -0.0278 1082 THR   B C   
8353  O  O   . THR   B 778 ? 1.2097 1.3501 1.5328 -0.0910 -0.1000 -0.0295 1082 THR   B O   
8354  C  CB  . THR   B 778 ? 1.1759 1.3122 1.4686 -0.0808 -0.1149 -0.0320 1082 THR   B CB  
8355  O  OG1 . THR   B 778 ? 1.2897 1.4256 1.5640 -0.0762 -0.1173 -0.0307 1082 THR   B OG1 
8356  C  CG2 . THR   B 778 ? 1.1842 1.3161 1.4848 -0.0802 -0.1231 -0.0363 1082 THR   B CG2 
8357  N  N   . GLU   B 779 ? 1.2765 1.4045 1.5914 -0.0925 -0.0989 -0.0265 1083 GLU   B N   
8358  C  CA  . GLU   B 779 ? 1.2780 1.4052 1.6112 -0.0976 -0.0938 -0.0264 1083 GLU   B CA  
8359  C  C   . GLU   B 779 ? 1.2636 1.3860 1.6066 -0.0985 -0.1006 -0.0300 1083 GLU   B C   
8360  O  O   . GLU   B 779 ? 1.2590 1.3759 1.5901 -0.0956 -0.1062 -0.0305 1083 GLU   B O   
8361  C  CB  . GLU   B 779 ? 1.2833 1.4060 1.6102 -0.1004 -0.0829 -0.0206 1083 GLU   B CB  
8362  N  N   . PRO   B 780 ? 1.2129 1.3373 1.5779 -0.1024 -0.1003 -0.0326 1084 PRO   B N   
8363  C  CA  . PRO   B 780 ? 1.1868 1.3072 1.5625 -0.1030 -0.1086 -0.0370 1084 PRO   B CA  
8364  C  C   . PRO   B 780 ? 1.1711 1.2823 1.5432 -0.1053 -0.1051 -0.0341 1084 PRO   B C   
8365  O  O   . PRO   B 780 ? 1.1004 1.2093 1.4732 -0.1088 -0.0949 -0.0296 1084 PRO   B O   
8366  C  CB  . PRO   B 780 ? 1.1466 1.2731 1.5486 -0.1068 -0.1085 -0.0404 1084 PRO   B CB  
8367  C  CG  . PRO   B 780 ? 1.1656 1.2999 1.5684 -0.1069 -0.1019 -0.0385 1084 PRO   B CG  
8368  C  CD  . PRO   B 780 ? 1.2326 1.3636 1.6146 -0.1061 -0.0937 -0.0324 1084 PRO   B CD  
8369  N  N   . ALA   B 781 ? 1.1767 1.2820 1.5443 -0.1030 -0.1138 -0.0369 1085 ALA   B N   
8370  C  CA  . ALA   B 781 ? 1.0686 1.1644 1.4312 -0.1045 -0.1120 -0.0347 1085 ALA   B CA  
8371  C  C   . ALA   B 781 ? 1.0982 1.1925 1.4799 -0.1110 -0.1045 -0.0334 1085 ALA   B C   
8372  O  O   . ALA   B 781 ? 1.0994 1.2001 1.5010 -0.1141 -0.1029 -0.0355 1085 ALA   B O   
8373  C  CB  . ALA   B 781 ? 1.0243 1.1145 1.3841 -0.1014 -0.1236 -0.0392 1085 ALA   B CB  
8374  N  N   . THR   B 782 ? 1.1046 1.1901 1.4802 -0.1128 -0.0996 -0.0298 1086 THR   B N   
8375  C  CA  . THR   B 782 ? 1.0965 1.1790 1.4880 -0.1189 -0.0910 -0.0277 1086 THR   B CA  
8376  C  C   . THR   B 782 ? 1.1456 1.2165 1.5288 -0.1197 -0.0898 -0.0254 1086 THR   B C   
8377  O  O   . THR   B 782 ? 1.1233 1.1892 1.4846 -0.1159 -0.0899 -0.0225 1086 THR   B O   
8378  C  CB  . THR   B 782 ? 1.0594 1.1453 1.4494 -0.1209 -0.0784 -0.0225 1086 THR   B CB  
8379  O  OG1 . THR   B 782 ? 1.2275 1.3124 1.6377 -0.1269 -0.0706 -0.0214 1086 THR   B OG1 
8380  C  CG2 . THR   B 782 ? 0.9801 1.0593 1.3458 -0.1186 -0.0724 -0.0168 1086 THR   B CG2 
8381  N  N   . GLY   B 783 ? 1.1289 1.1958 1.5305 -0.1246 -0.0885 -0.0266 1087 GLY   B N   
8382  C  CA  . GLY   B 783 ? 1.1640 1.2193 1.5596 -0.1261 -0.0860 -0.0241 1087 GLY   B CA  
8383  C  C   . GLY   B 783 ? 1.1275 1.1763 1.5084 -0.1215 -0.0965 -0.0265 1087 GLY   B C   
8384  O  O   . GLY   B 783 ? 1.1868 1.2259 1.5554 -0.1211 -0.0941 -0.0235 1087 GLY   B O   
8385  N  N   . PHE   B 784 ? 1.1001 1.1535 1.4811 -0.1177 -0.1078 -0.0318 1088 PHE   B N   
8386  C  CA  . PHE   B 784 ? 1.0674 1.1146 1.4355 -0.1130 -0.1184 -0.0347 1088 PHE   B CA  
8387  C  C   . PHE   B 784 ? 1.1122 1.1612 1.4971 -0.1130 -0.1298 -0.0419 1088 PHE   B C   
8388  O  O   . PHE   B 784 ? 1.1828 1.2409 1.5817 -0.1138 -0.1320 -0.0450 1088 PHE   B O   
8389  C  CB  . PHE   B 784 ? 1.0789 1.1290 1.4241 -0.1063 -0.1212 -0.0335 1088 PHE   B CB  
8390  C  CG  . PHE   B 784 ? 1.0975 1.1423 1.4215 -0.1045 -0.1140 -0.0274 1088 PHE   B CG  
8391  C  CD1 . PHE   B 784 ? 1.0977 1.1332 1.4069 -0.1014 -0.1177 -0.0267 1088 PHE   B CD1 
8392  C  CD2 . PHE   B 784 ? 1.1262 1.1754 1.4445 -0.1054 -0.1042 -0.0225 1088 PHE   B CD2 
8393  C  CE1 . PHE   B 784 ? 1.1160 1.1468 1.4059 -0.0994 -0.1116 -0.0213 1088 PHE   B CE1 
8394  C  CE2 . PHE   B 784 ? 1.0969 1.1411 1.3954 -0.1034 -0.0984 -0.0172 1088 PHE   B CE2 
8395  C  CZ  . PHE   B 784 ? 1.0536 1.0888 1.3383 -0.1004 -0.1022 -0.0166 1088 PHE   B CZ  
8396  N  N   . ILE   B 785 ? 1.0848 1.1249 1.4679 -0.1120 -0.1375 -0.0447 1089 ILE   B N   
8397  C  CA  . ILE   B 785 ? 1.1138 1.1537 1.5091 -0.1109 -0.1500 -0.0520 1089 ILE   B CA  
8398  C  C   . ILE   B 785 ? 1.0993 1.1351 1.4730 -0.1032 -0.1596 -0.0541 1089 ILE   B C   
8399  O  O   . ILE   B 785 ? 1.0629 1.0909 1.4181 -0.1005 -0.1583 -0.0510 1089 ILE   B O   
8400  C  CB  . ILE   B 785 ? 1.1264 1.1582 1.5377 -0.1157 -0.1521 -0.0542 1089 ILE   B CB  
8401  C  CG1 . ILE   B 785 ? 1.2033 1.2369 1.6328 -0.1233 -0.1400 -0.0505 1089 ILE   B CG1 
8402  C  CG2 . ILE   B 785 ? 1.0769 1.1095 1.5037 -0.1150 -0.1652 -0.0621 1089 ILE   B CG2 
8403  C  CD1 . ILE   B 785 ? 1.2330 1.2783 1.6847 -0.1266 -0.1383 -0.0526 1089 ILE   B CD1 
8404  N  N   . ASP   B 786 ? 1.0780 1.1187 1.4538 -0.0994 -0.1689 -0.0592 1090 ASP   B N   
8405  C  CA  . ASP   B 786 ? 1.0816 1.1180 1.4372 -0.0918 -0.1779 -0.0613 1090 ASP   B CA  
8406  C  C   . ASP   B 786 ? 1.1054 1.1316 1.4644 -0.0908 -0.1884 -0.0664 1090 ASP   B C   
8407  O  O   . ASP   B 786 ? 1.0965 1.1231 1.4669 -0.0898 -0.1984 -0.0727 1090 ASP   B O   
8408  C  CB  . ASP   B 786 ? 1.0848 1.1295 1.4383 -0.0875 -0.1829 -0.0642 1090 ASP   B CB  
8409  C  CG  . ASP   B 786 ? 1.1087 1.1493 1.4381 -0.0793 -0.1892 -0.0648 1090 ASP   B CG  
8410  O  OD1 . ASP   B 786 ? 1.1520 1.1824 1.4703 -0.0765 -0.1938 -0.0654 1090 ASP   B OD1 
8411  O  OD2 . ASP   B 786 ? 1.0562 1.1034 1.3775 -0.0757 -0.1892 -0.0644 1090 ASP   B OD2 
8412  N  N   . GLY   B 787 ? 1.1098 1.1261 1.4583 -0.0908 -0.1861 -0.0636 1091 GLY   B N   
8413  C  CA  . GLY   B 787 ? 1.1108 1.1162 1.4607 -0.0898 -0.1955 -0.0679 1091 GLY   B CA  
8414  C  C   . GLY   B 787 ? 1.1462 1.1484 1.4849 -0.0823 -0.2082 -0.0733 1091 GLY   B C   
8415  O  O   . GLY   B 787 ? 1.1335 1.1292 1.4799 -0.0816 -0.2185 -0.0790 1091 GLY   B O   
8416  N  N   . ASP   B 788 ? 1.1343 1.1403 1.4544 -0.0763 -0.2077 -0.0714 1092 ASP   B N   
8417  C  CA  . ASP   B 788 ? 1.0887 1.0916 1.3973 -0.0687 -0.2190 -0.0762 1092 ASP   B CA  
8418  C  C   . ASP   B 788 ? 1.1779 1.1847 1.5056 -0.0696 -0.2278 -0.0830 1092 ASP   B C   
8419  O  O   . ASP   B 788 ? 1.2348 1.2342 1.5618 -0.0659 -0.2395 -0.0888 1092 ASP   B O   
8420  C  CB  . ASP   B 788 ? 1.1373 1.1455 1.4261 -0.0630 -0.2154 -0.0728 1092 ASP   B CB  
8421  C  CG  . ASP   B 788 ? 1.1461 1.1475 1.4118 -0.0588 -0.2119 -0.0682 1092 ASP   B CG  
8422  O  OD1 . ASP   B 788 ? 1.1425 1.1351 1.4066 -0.0605 -0.2113 -0.0672 1092 ASP   B OD1 
8423  O  OD2 . ASP   B 788 ? 1.1276 1.1323 1.3766 -0.0537 -0.2098 -0.0657 1092 ASP   B OD2 
8424  N  N   . LEU   B 789 ? 1.1642 1.1822 1.5092 -0.0745 -0.2225 -0.0824 1093 LEU   B N   
8425  C  CA  . LEU   B 789 ? 1.1971 1.2195 1.5622 -0.0757 -0.2307 -0.0888 1093 LEU   B CA  
8426  C  C   . LEU   B 789 ? 1.1642 1.1815 1.5505 -0.0812 -0.2348 -0.0925 1093 LEU   B C   
8427  O  O   . LEU   B 789 ? 1.2005 1.2133 1.5946 -0.0793 -0.2470 -0.0993 1093 LEU   B O   
8428  C  CB  . LEU   B 789 ? 1.1764 1.2123 1.5545 -0.0791 -0.2237 -0.0872 1093 LEU   B CB  
8429  C  CG  . LEU   B 789 ? 1.1822 1.2217 1.5723 -0.0767 -0.2348 -0.0943 1093 LEU   B CG  
8430  C  CD1 . LEU   B 789 ? 1.2059 1.2408 1.5727 -0.0672 -0.2432 -0.0966 1093 LEU   B CD1 
8431  C  CD2 . LEU   B 789 ? 1.1613 1.2140 1.5687 -0.0807 -0.2289 -0.0936 1093 LEU   B CD2 
8432  N  N   . ILE   B 790 ? 1.1505 1.1680 1.5465 -0.0882 -0.2247 -0.0881 1094 ILE   B N   
8433  C  CA  . ILE   B 790 ? 1.1834 1.1953 1.5994 -0.0940 -0.2273 -0.0908 1094 ILE   B CA  
8434  C  C   . ILE   B 790 ? 1.2561 1.2551 1.6633 -0.0894 -0.2400 -0.0959 1094 ILE   B C   
8435  O  O   . ILE   B 790 ? 1.2702 1.2664 1.6939 -0.0905 -0.2503 -0.1025 1094 ILE   B O   
8436  C  CB  . ILE   B 790 ? 1.1623 1.1726 1.5809 -0.1003 -0.2139 -0.0841 1094 ILE   B CB  
8437  C  CG1 . ILE   B 790 ? 1.1399 1.1624 1.5708 -0.1053 -0.2019 -0.0799 1094 ILE   B CG1 
8438  C  CG2 . ILE   B 790 ? 1.1752 1.1776 1.6115 -0.1058 -0.2167 -0.0867 1094 ILE   B CG2 
8439  C  CD1 . ILE   B 790 ? 1.1636 1.1932 1.6258 -0.1111 -0.2037 -0.0841 1094 ILE   B CD1 
8440  N  N   . GLU   B 791 ? 1.2656 1.2563 1.6465 -0.0839 -0.2398 -0.0931 1095 GLU   B N   
8441  C  CA  . GLU   B 791 ? 1.2421 1.2194 1.6131 -0.0794 -0.2511 -0.0975 1095 GLU   B CA  
8442  C  C   . GLU   B 791 ? 1.2591 1.2352 1.6273 -0.0728 -0.2649 -0.1046 1095 GLU   B C   
8443  O  O   . GLU   B 791 ? 1.2681 1.2333 1.6333 -0.0695 -0.2762 -0.1098 1095 GLU   B O   
8444  C  CB  . GLU   B 791 ? 1.2558 1.2247 1.5987 -0.0744 -0.2473 -0.0926 1095 GLU   B CB  
8445  C  CG  . GLU   B 791 ? 1.3124 1.2785 1.6559 -0.0802 -0.2355 -0.0862 1095 GLU   B CG  
8446  C  CD  . GLU   B 791 ? 1.2962 1.2526 1.6136 -0.0754 -0.2330 -0.0821 1095 GLU   B CD  
8447  O  OE1 . GLU   B 791 ? 1.2577 1.2073 1.5567 -0.0675 -0.2412 -0.0845 1095 GLU   B OE1 
8448  O  OE2 . GLU   B 791 ? 1.2002 1.1553 1.5159 -0.0794 -0.2225 -0.0763 1095 GLU   B OE2 
8449  N  N   . SER   B 792 ? 1.2620 1.2483 1.6303 -0.0705 -0.2645 -0.1049 1096 SER   B N   
8450  C  CA  . SER   B 792 ? 1.2824 1.2668 1.6477 -0.0640 -0.2777 -0.1118 1096 SER   B CA  
8451  C  C   . SER   B 792 ? 1.2976 1.2817 1.6891 -0.0677 -0.2876 -0.1191 1096 SER   B C   
8452  O  O   . SER   B 792 ? 1.3219 1.3015 1.7114 -0.0621 -0.3007 -0.1257 1096 SER   B O   
8453  C  CB  . SER   B 792 ? 1.3022 1.2975 1.6612 -0.0606 -0.2746 -0.1103 1096 SER   B CB  
8454  O  OG  . SER   B 792 ? 1.2637 1.2715 1.6463 -0.0669 -0.2695 -0.1102 1096 SER   B OG  
8455  N  N   . PHE   B 793 ? 1.3289 1.3171 1.7448 -0.0767 -0.2818 -0.1180 1097 PHE   B N   
8456  C  CA  . PHE   B 793 ? 1.3297 1.3179 1.7729 -0.0809 -0.2909 -0.1249 1097 PHE   B CA  
8457  C  C   . PHE   B 793 ? 1.3824 1.3557 1.8200 -0.0771 -0.3047 -0.1309 1097 PHE   B C   
8458  O  O   . PHE   B 793 ? 1.4445 1.4159 1.8940 -0.0754 -0.3178 -0.1386 1097 PHE   B O   
8459  C  CB  . PHE   B 793 ? 1.3250 1.3192 1.7937 -0.0913 -0.2803 -0.1216 1097 PHE   B CB  
8460  C  CG  . PHE   B 793 ? 1.4361 1.4294 1.9346 -0.0966 -0.2887 -0.1281 1097 PHE   B CG  
8461  C  CD1 . PHE   B 793 ? 1.4858 1.4835 1.9989 -0.0946 -0.3005 -0.1356 1097 PHE   B CD1 
8462  C  CD2 . PHE   B 793 ? 1.4915 1.4789 2.0036 -0.1036 -0.2849 -0.1269 1097 PHE   B CD2 
8463  C  CE1 . PHE   B 793 ? 1.5079 1.5049 2.0499 -0.0994 -0.3089 -0.1420 1097 PHE   B CE1 
8464  C  CE2 . PHE   B 793 ? 1.4874 1.4741 2.0288 -0.1089 -0.2926 -0.1330 1097 PHE   B CE2 
8465  C  CZ  . PHE   B 793 ? 1.4952 1.4870 2.0520 -0.1068 -0.3048 -0.1406 1097 PHE   B CZ  
8466  N  N   . LEU   B 794 ? 1.3428 1.3051 1.7619 -0.0754 -0.3024 -0.1277 1098 LEU   B N   
8467  C  CA  . LEU   B 794 ? 1.3125 1.2599 1.7259 -0.0717 -0.3154 -0.1335 1098 LEU   B CA  
8468  C  C   . LEU   B 794 ? 1.3845 1.3257 1.7774 -0.0611 -0.3277 -0.1383 1098 LEU   B C   
8469  O  O   . LEU   B 794 ? 1.4489 1.3783 1.8396 -0.0574 -0.3409 -0.1447 1098 LEU   B O   
8470  C  CB  . LEU   B 794 ? 1.2620 1.1984 1.6599 -0.0721 -0.3101 -0.1289 1098 LEU   B CB  
8471  C  CG  . LEU   B 794 ? 1.2781 1.2186 1.6864 -0.0808 -0.2952 -0.1219 1098 LEU   B CG  
8472  C  CD1 . LEU   B 794 ? 1.3871 1.3355 1.7781 -0.0789 -0.2824 -0.1142 1098 LEU   B CD1 
8473  C  CD2 . LEU   B 794 ? 1.3368 1.2634 1.7393 -0.0824 -0.2952 -0.1208 1098 LEU   B CD2 
8474  N  N   . ASP   B 795 ? 1.4164 1.3646 1.7940 -0.0560 -0.3239 -0.1356 1099 ASP   B N   
8475  C  CA  . ASP   B 795 ? 1.4510 1.3928 1.8075 -0.0455 -0.3344 -0.1397 1099 ASP   B CA  
8476  C  C   . ASP   B 795 ? 1.4813 1.4300 1.8511 -0.0437 -0.3431 -0.1457 1099 ASP   B C   
8477  O  O   . ASP   B 795 ? 1.5396 1.4835 1.8920 -0.0349 -0.3513 -0.1490 1099 ASP   B O   
8478  C  CB  . ASP   B 795 ? 1.4972 1.4402 1.8254 -0.0397 -0.3256 -0.1331 1099 ASP   B CB  
8479  C  CG  . ASP   B 795 ? 1.6034 1.5368 1.9135 -0.0387 -0.3200 -0.1282 1099 ASP   B CG  
8480  O  OD1 . ASP   B 795 ? 1.5564 1.4945 1.8733 -0.0456 -0.3083 -0.1223 1099 ASP   B OD1 
8481  O  OD2 . ASP   B 795 ? 1.7213 1.6422 2.0097 -0.0307 -0.3273 -0.1302 1099 ASP   B OD2 
8482  N  N   . ILE   B 796 ? 1.4729 1.4324 1.8727 -0.0516 -0.3414 -0.1473 1100 ILE   B N   
8483  C  CA  . ILE   B 796 ? 1.4610 1.4275 1.8751 -0.0501 -0.3497 -0.1531 1100 ILE   B CA  
8484  C  C   . ILE   B 796 ? 1.5238 1.4830 1.9561 -0.0508 -0.3651 -0.1621 1100 ILE   B C   
8485  O  O   . ILE   B 796 ? 1.4314 1.3810 1.8674 -0.0535 -0.3682 -0.1635 1100 ILE   B O   
8486  C  CB  . ILE   B 796 ? 1.3498 1.3336 1.7860 -0.0575 -0.3388 -0.1497 1100 ILE   B CB  
8487  C  CG1 . ILE   B 796 ? 1.4507 1.4381 1.9122 -0.0682 -0.3310 -0.1474 1100 ILE   B CG1 
8488  C  CG2 . ILE   B 796 ? 1.3799 1.3708 1.7972 -0.0553 -0.3263 -0.1423 1100 ILE   B CG2 
8489  C  CD1 . ILE   B 796 ? 1.4656 1.4679 1.9566 -0.0752 -0.3260 -0.1476 1100 ILE   B CD1 
8490  N  N   . SER   B 797 ? 1.6521 1.6160 2.0967 -0.0485 -0.3748 -0.1684 1101 SER   B N   
8491  C  CA  . SER   B 797 ? 1.6984 1.6549 2.1580 -0.0474 -0.3917 -0.1779 1101 SER   B CA  
8492  C  C   . SER   B 797 ? 1.6736 1.6367 2.1700 -0.0585 -0.3899 -0.1794 1101 SER   B C   
8493  O  O   . SER   B 797 ? 1.6580 1.6352 2.1736 -0.0658 -0.3782 -0.1752 1101 SER   B O   
8494  C  CB  . SER   B 797 ? 1.7028 1.6620 2.1620 -0.0406 -0.4028 -0.1841 1101 SER   B CB  
8495  O  OG  . SER   B 797 ? 1.6640 1.6331 2.1108 -0.0380 -0.3930 -0.1788 1101 SER   B OG  
8496  N  N   . ARG   B 798 ? 1.6317 1.5838 2.1377 -0.0597 -0.4011 -0.1853 1102 ARG   B N   
8497  C  CA  . ARG   B 798 ? 1.6185 1.5761 2.1606 -0.0702 -0.4001 -0.1872 1102 ARG   B CA  
8498  C  C   . ARG   B 798 ? 1.6652 1.6369 2.2371 -0.0735 -0.4033 -0.1914 1102 ARG   B C   
8499  O  O   . ARG   B 798 ? 1.6750 1.6568 2.2765 -0.0833 -0.3951 -0.1895 1102 ARG   B O   
8500  C  CB  . ARG   B 798 ? 1.5829 1.5253 2.1294 -0.0701 -0.4135 -0.1937 1102 ARG   B CB  
8501  C  CG  . ARG   B 798 ? 1.5905 1.5373 2.1757 -0.0811 -0.4135 -0.1962 1102 ARG   B CG  
8502  C  CD  . ARG   B 798 ? 1.5993 1.5517 2.1928 -0.0905 -0.3947 -0.1872 1102 ARG   B CD  
8503  N  NE  . ARG   B 798 ? 1.6571 1.6170 2.2901 -0.1011 -0.3925 -0.1890 1102 ARG   B NE  
8504  C  CZ  . ARG   B 798 ? 1.6827 1.6350 2.3299 -0.1076 -0.3927 -0.1896 1102 ARG   B CZ  
8505  N  NH1 . ARG   B 798 ? 1.6549 1.5916 2.2799 -0.1046 -0.3953 -0.1888 1102 ARG   B NH1 
8506  N  NH2 . ARG   B 798 ? 1.6490 1.6096 2.3338 -0.1173 -0.3899 -0.1910 1102 ARG   B NH2 
8507  N  N   . PRO   B 799 ? 1.6682 1.6412 2.2346 -0.0659 -0.4143 -0.1969 1103 PRO   B N   
8508  C  CA  . PRO   B 799 ? 1.6797 1.6687 2.2713 -0.0690 -0.4133 -0.1988 1103 PRO   B CA  
8509  C  C   . PRO   B 799 ? 1.6800 1.6832 2.2719 -0.0736 -0.3939 -0.1896 1103 PRO   B C   
8510  O  O   . PRO   B 799 ? 1.6919 1.7075 2.3130 -0.0821 -0.3858 -0.1879 1103 PRO   B O   
8511  C  CB  . PRO   B 799 ? 1.6490 1.6336 2.2244 -0.0580 -0.4276 -0.2051 1103 PRO   B CB  
8512  C  CG  . PRO   B 799 ? 1.6992 1.6692 2.2345 -0.0493 -0.4288 -0.2027 1103 PRO   B CG  
8513  C  CD  . PRO   B 799 ? 1.6689 1.6288 2.2050 -0.0540 -0.4272 -0.2013 1103 PRO   B CD  
8514  N  N   . LYS   B 800 ? 1.6903 1.6913 2.2499 -0.0679 -0.3862 -0.1835 1104 LYS   B N   
8515  C  CA  . LYS   B 800 ? 1.6592 1.6729 2.2167 -0.0716 -0.3684 -0.1749 1104 LYS   B CA  
8516  C  C   . LYS   B 800 ? 1.6825 1.6987 2.2520 -0.0813 -0.3541 -0.1683 1104 LYS   B C   
8517  O  O   . LYS   B 800 ? 1.7145 1.7435 2.2999 -0.0878 -0.3414 -0.1636 1104 LYS   B O   
8518  C  CB  . LYS   B 800 ? 1.5273 1.5369 2.0476 -0.0632 -0.3645 -0.1703 1104 LYS   B CB  
8519  N  N   . MET   B 801 ? 1.6044 1.6082 2.1655 -0.0821 -0.3558 -0.1679 1105 MET   B N   
8520  C  CA  . MET   B 801 ? 1.6160 1.6206 2.1887 -0.0912 -0.3430 -0.1621 1105 MET   B CA  
8521  C  C   . MET   B 801 ? 1.6472 1.6633 2.2591 -0.1006 -0.3393 -0.1635 1105 MET   B C   
8522  O  O   . MET   B 801 ? 1.6249 1.6501 2.2470 -0.1073 -0.3238 -0.1568 1105 MET   B O   
8523  C  CB  . MET   B 801 ? 1.5962 1.5848 2.1603 -0.0907 -0.3495 -0.1639 1105 MET   B CB  
8524  C  CG  . MET   B 801 ? 1.5421 1.5183 2.0674 -0.0812 -0.3530 -0.1625 1105 MET   B CG  
8525  S  SD  . MET   B 801 ? 1.6106 1.5681 2.1260 -0.0812 -0.3586 -0.1638 1105 MET   B SD  
8526  C  CE  . MET   B 801 ? 1.4659 1.4273 1.9937 -0.0920 -0.3402 -0.1552 1105 MET   B CE  
8527  N  N   . GLN   B 802 ? 1.7186 1.7341 2.3530 -0.1010 -0.3535 -0.1722 1106 GLN   B N   
8528  C  CA  . GLN   B 802 ? 1.7376 1.7640 2.4114 -0.1099 -0.3508 -0.1740 1106 GLN   B CA  
8529  C  C   . GLN   B 802 ? 1.7483 1.7911 2.4313 -0.1112 -0.3409 -0.1706 1106 GLN   B C   
8530  O  O   . GLN   B 802 ? 1.7551 1.8081 2.4632 -0.1196 -0.3294 -0.1672 1106 GLN   B O   
8531  C  CB  . GLN   B 802 ? 1.7529 1.7757 2.4480 -0.1089 -0.3696 -0.1847 1106 GLN   B CB  
8532  C  CG  . GLN   B 802 ? 1.7774 1.7852 2.4736 -0.1106 -0.3780 -0.1881 1106 GLN   B CG  
8533  C  CD  . GLN   B 802 ? 1.7941 1.7925 2.4896 -0.1038 -0.4000 -0.1987 1106 GLN   B CD  
8534  O  OE1 . GLN   B 802 ? 1.8030 1.8046 2.4920 -0.0968 -0.4089 -0.2030 1106 GLN   B OE1 
8535  N  NE2 . GLN   B 802 ? 1.7320 1.7180 2.4333 -0.1057 -0.4090 -0.2029 1106 GLN   B NE2 
8536  N  N   . GLU   B 803 ? 1.8617 1.9069 2.5243 -0.1030 -0.3448 -0.1714 1107 GLU   B N   
8537  C  CA  . GLU   B 803 ? 1.8517 1.9120 2.5226 -0.1038 -0.3364 -0.1687 1107 GLU   B CA  
8538  C  C   . GLU   B 803 ? 1.8109 1.8771 2.4752 -0.1088 -0.3161 -0.1585 1107 GLU   B C   
8539  O  O   . GLU   B 803 ? 1.8036 1.8824 2.4878 -0.1142 -0.3058 -0.1555 1107 GLU   B O   
8540  C  CB  . GLU   B 803 ? 1.8409 1.9011 2.4887 -0.0937 -0.3444 -0.1713 1107 GLU   B CB  
8541  C  CG  . GLU   B 803 ? 1.9031 1.9524 2.5437 -0.0860 -0.3648 -0.1805 1107 GLU   B CG  
8542  C  CD  . GLU   B 803 ? 1.9543 2.0046 2.6288 -0.0896 -0.3776 -0.1892 1107 GLU   B CD  
8543  O  OE1 . GLU   B 803 ? 1.9646 2.0082 2.6356 -0.0828 -0.3948 -0.1973 1107 GLU   B OE1 
8544  O  OE2 . GLU   B 803 ? 1.9529 2.0105 2.6579 -0.0992 -0.3705 -0.1879 1107 GLU   B OE2 
8545  N  N   . VAL   B 804 ? 1.6616 1.7186 2.2983 -0.1069 -0.3102 -0.1530 1108 VAL   B N   
8546  C  CA  . VAL   B 804 ? 1.5794 1.6407 2.2080 -0.1111 -0.2916 -0.1434 1108 VAL   B CA  
8547  C  C   . VAL   B 804 ? 1.5516 1.6133 2.2033 -0.1210 -0.2820 -0.1403 1108 VAL   B C   
8548  O  O   . VAL   B 804 ? 1.5229 1.5899 2.1747 -0.1256 -0.2660 -0.1328 1108 VAL   B O   
8549  C  CB  . VAL   B 804 ? 1.5046 1.5563 2.0957 -0.1053 -0.2887 -0.1386 1108 VAL   B CB  
8550  C  CG1 . VAL   B 804 ? 1.5087 1.5552 2.0780 -0.0952 -0.3020 -0.1434 1108 VAL   B CG1 
8551  C  CG2 . VAL   B 804 ? 1.5749 1.6141 2.1617 -0.1081 -0.2884 -0.1373 1108 VAL   B CG2 
8552  N  N   . VAL   B 805 ? 1.5735 1.6289 2.2440 -0.1242 -0.2912 -0.1458 1109 VAL   B N   
8553  C  CA  . VAL   B 805 ? 1.5944 1.6499 2.2889 -0.1338 -0.2822 -0.1432 1109 VAL   B CA  
8554  C  C   . VAL   B 805 ? 1.6414 1.7088 2.3749 -0.1400 -0.2822 -0.1467 1109 VAL   B C   
8555  O  O   . VAL   B 805 ? 1.6749 1.7445 2.4317 -0.1486 -0.2728 -0.1440 1109 VAL   B O   
8556  C  CB  . VAL   B 805 ? 1.6018 1.6424 2.2940 -0.1345 -0.2908 -0.1463 1109 VAL   B CB  
8557  C  CG1 . VAL   B 805 ? 1.5428 1.5722 2.1982 -0.1296 -0.2874 -0.1413 1109 VAL   B CG1 
8558  C  CG2 . VAL   B 805 ? 1.6664 1.7025 2.3652 -0.1299 -0.3111 -0.1565 1109 VAL   B CG2 
8559  N  N   . ALA   B 806 ? 1.6039 1.6793 2.3448 -0.1358 -0.2915 -0.1523 1110 ALA   B N   
8560  C  CA  . ALA   B 806 ? 1.6540 1.7408 2.4329 -0.1406 -0.2945 -0.1571 1110 ALA   B CA  
8561  C  C   . ALA   B 806 ? 1.7059 1.8039 2.5042 -0.1485 -0.2757 -0.1502 1110 ALA   B C   
8562  O  O   . ALA   B 806 ? 1.6765 1.7807 2.4601 -0.1469 -0.2642 -0.1441 1110 ALA   B O   
8563  C  CB  . ALA   B 806 ? 1.6247 1.7180 2.4010 -0.1333 -0.3060 -0.1629 1110 ALA   B CB  
8564  N  N   . ASN   B 807 ? 1.7504 1.8508 2.5823 -0.1569 -0.2728 -0.1514 1111 ASN   B N   
8565  C  CA  . ASN   B 807 ? 1.7514 1.8625 2.6061 -0.1646 -0.2556 -0.1457 1111 ASN   B CA  
8566  C  C   . ASN   B 807 ? 1.7489 1.8558 2.5817 -0.1667 -0.2375 -0.1353 1111 ASN   B C   
8567  O  O   . ASN   B 807 ? 1.7366 1.8483 2.5499 -0.1634 -0.2286 -0.1301 1111 ASN   B O   
8568  C  CB  . ASN   B 807 ? 1.7257 1.8518 2.5914 -0.1625 -0.2544 -0.1469 1111 ASN   B CB  
8569  C  CG  . ASN   B 807 ? 1.7089 1.8424 2.6103 -0.1640 -0.2673 -0.1559 1111 ASN   B CG  
8570  O  OD1 . ASN   B 807 ? 1.7479 1.8905 2.6833 -0.1712 -0.2602 -0.1557 1111 ASN   B OD1 
8571  N  ND2 . ASN   B 807 ? 1.6713 1.8008 2.5651 -0.1571 -0.2862 -0.1640 1111 ASN   B ND2 
8572  N  N   . LEU   B 808 ? 1.7629 1.8604 2.5990 -0.1721 -0.2321 -0.1325 1112 LEU   B N   
8573  C  CA  . LEU   B 808 ? 1.7688 1.8616 2.5878 -0.1749 -0.2146 -0.1228 1112 LEU   B CA  
8574  C  C   . LEU   B 808 ? 1.8526 1.9331 2.6771 -0.1802 -0.2136 -0.1221 1112 LEU   B C   
8575  O  O   . LEU   B 808 ? 1.8801 1.9502 2.6952 -0.1772 -0.2272 -0.1270 1112 LEU   B O   
8576  C  CB  . LEU   B 808 ? 1.7486 1.8369 2.5260 -0.1671 -0.2137 -0.1189 1112 LEU   B CB  
8577  C  CG  . LEU   B 808 ? 1.8230 1.9113 2.5829 -0.1687 -0.1948 -0.1088 1112 LEU   B CG  
8578  C  CD1 . LEU   B 808 ? 1.8277 1.9046 2.5854 -0.1739 -0.1862 -0.1040 1112 LEU   B CD1 
8579  C  CD2 . LEU   B 808 ? 1.7685 1.8703 2.5493 -0.1727 -0.1828 -0.1059 1112 LEU   B CD2 
8580  N  N   . GLN   B 809 ? 1.8836 1.9645 2.7225 -0.1879 -0.1975 -0.1159 1113 GLN   B N   
8581  C  CA  . GLN   B 809 ? 1.8930 1.9621 2.7393 -0.1936 -0.1950 -0.1146 1113 GLN   B CA  
8582  C  C   . GLN   B 809 ? 1.8658 1.9250 2.6841 -0.1937 -0.1810 -0.1056 1113 GLN   B C   
8583  O  O   . GLN   B 809 ? 1.8496 1.9067 2.6349 -0.1873 -0.1797 -0.1022 1113 GLN   B O   
8584  C  CB  . GLN   B 809 ? 1.8368 1.9119 2.7249 -0.2030 -0.1881 -0.1151 1113 GLN   B CB  
8585  C  CG  . GLN   B 809 ? 1.7941 1.8588 2.6988 -0.2078 -0.1960 -0.1194 1113 GLN   B CG  
8586  C  CD  . GLN   B 809 ? 1.7952 1.8597 2.7092 -0.2039 -0.2188 -0.1304 1113 GLN   B CD  
8587  O  OE1 . GLN   B 809 ? 1.7673 1.8439 2.7038 -0.2036 -0.2257 -0.1359 1113 GLN   B OE1 
8588  N  NE2 . GLN   B 809 ? 1.7944 1.8453 2.6877 -0.1999 -0.2305 -0.1335 1113 GLN   B NE2 
8589  N  N   . GLU   B 819 ? 1.7841 1.8743 2.7178 -0.1895 -0.2574 -0.1510 1123 GLU   B N   
8590  C  CA  . GLU   B 819 ? 1.8052 1.8881 2.6953 -0.1819 -0.2563 -0.1469 1123 GLU   B CA  
8591  C  C   . GLU   B 819 ? 1.8428 1.9080 2.7133 -0.1810 -0.2622 -0.1472 1123 GLU   B C   
8592  O  O   . GLU   B 819 ? 1.7891 1.8481 2.6807 -0.1855 -0.2699 -0.1520 1123 GLU   B O   
8593  C  CB  . GLU   B 819 ? 1.7300 1.8169 2.6054 -0.1727 -0.2703 -0.1525 1123 GLU   B CB  
8594  N  N   . ALA   B 820 ? 1.8341 1.8911 2.6655 -0.1752 -0.2589 -0.1423 1124 ALA   B N   
8595  C  CA  . ALA   B 820 ? 1.8185 1.8592 2.6290 -0.1734 -0.2639 -0.1422 1124 ALA   B CA  
8596  C  C   . ALA   B 820 ? 1.7842 1.8183 2.5725 -0.1637 -0.2825 -0.1491 1124 ALA   B C   
8597  O  O   . ALA   B 820 ? 1.7237 1.7645 2.4985 -0.1572 -0.2860 -0.1501 1124 ALA   B O   
8598  C  CB  . ALA   B 820 ? 1.8016 1.8369 2.5850 -0.1735 -0.2478 -0.1323 1124 ALA   B CB  
8599  N  N   . THR   B 821 ? 1.7957 1.8165 2.5816 -0.1629 -0.2947 -0.1540 1125 THR   B N   
8600  C  CA  . THR   B 821 ? 1.7565 1.7699 2.5241 -0.1539 -0.3133 -0.1613 1125 THR   B CA  
8601  C  C   . THR   B 821 ? 1.7185 1.7249 2.4429 -0.1458 -0.3103 -0.1564 1125 THR   B C   
8602  O  O   . THR   B 821 ? 1.7030 1.7102 2.4126 -0.1474 -0.2947 -0.1478 1125 THR   B O   
8603  C  CB  . THR   B 821 ? 1.7178 1.7180 2.4950 -0.1553 -0.3270 -0.1680 1125 THR   B CB  
8604  O  OG1 . THR   B 821 ? 1.7517 1.7577 2.5705 -0.1648 -0.3259 -0.1707 1125 THR   B OG1 
8605  C  CG2 . THR   B 821 ? 1.6417 1.6361 2.4078 -0.1463 -0.3483 -0.1774 1125 THR   B CG2 
8606  N  N   . ALA   B 822 ? 1.7200 1.7190 2.4240 -0.1368 -0.3256 -0.1621 1126 ALA   B N   
8607  C  CA  . ALA   B 822 ? 1.6790 1.6689 2.3429 -0.1292 -0.3242 -0.1581 1126 ALA   B CA  
8608  C  C   . ALA   B 822 ? 1.6564 1.6326 2.3104 -0.1319 -0.3204 -0.1548 1126 ALA   B C   
8609  O  O   . ALA   B 822 ? 1.6384 1.6128 2.2741 -0.1326 -0.3068 -0.1466 1126 ALA   B O   
8610  C  CB  . ALA   B 822 ? 1.6478 1.6317 2.2932 -0.1189 -0.3417 -0.1652 1126 ALA   B CB  
8611  N  N   . ASP   B 823 ? 1.6932 1.6593 2.3601 -0.1337 -0.3324 -0.1612 1127 ASP   B N   
8612  C  CA  . ASP   B 823 ? 1.7194 1.6695 2.3712 -0.1337 -0.3330 -0.1598 1127 ASP   B CA  
8613  C  C   . ASP   B 823 ? 1.7342 1.6842 2.3846 -0.1404 -0.3142 -0.1503 1127 ASP   B C   
8614  O  O   . ASP   B 823 ? 1.7316 1.6696 2.3592 -0.1383 -0.3113 -0.1467 1127 ASP   B O   
8615  C  CB  . ASP   B 823 ? 1.7145 1.6560 2.3888 -0.1370 -0.3471 -0.1680 1127 ASP   B CB  
8616  C  CG  . ASP   B 823 ? 1.7322 1.6720 2.4067 -0.1299 -0.3668 -0.1778 1127 ASP   B CG  
8617  O  OD1 . ASP   B 823 ? 1.7519 1.6801 2.3968 -0.1208 -0.3764 -0.1801 1127 ASP   B OD1 
8618  O  OD2 . ASP   B 823 ? 1.7301 1.6802 2.4337 -0.1329 -0.3724 -0.1830 1127 ASP   B OD2 
8619  N  N   . ASP   B 824 ? 1.8500 1.8124 2.5243 -0.1481 -0.3013 -0.1463 1128 ASP   B N   
8620  C  CA  . ASP   B 824 ? 1.8673 1.8288 2.5380 -0.1537 -0.2831 -0.1370 1128 ASP   B CA  
8621  C  C   . ASP   B 824 ? 1.8373 1.8035 2.4789 -0.1488 -0.2718 -0.1295 1128 ASP   B C   
8622  O  O   . ASP   B 824 ? 1.8488 1.8097 2.4747 -0.1501 -0.2598 -0.1222 1128 ASP   B O   
8623  C  CB  . ASP   B 824 ? 1.9107 1.8818 2.6183 -0.1641 -0.2729 -0.1354 1128 ASP   B CB  
8624  C  CG  . ASP   B 824 ? 1.9086 1.8954 2.6385 -0.1645 -0.2764 -0.1395 1128 ASP   B CG  
8625  O  OD1 . ASP   B 824 ? 1.9494 1.9373 2.6710 -0.1573 -0.2906 -0.1457 1128 ASP   B OD1 
8626  O  OD2 . ASP   B 824 ? 1.8757 1.8732 2.6305 -0.1716 -0.2648 -0.1363 1128 ASP   B OD2 
8627  N  N   . LEU   B 825 ? 1.6370 1.6128 2.2715 -0.1432 -0.2757 -0.1313 1129 LEU   B N   
8628  C  CA  . LEU   B 825 ? 1.5417 1.5217 2.1479 -0.1378 -0.2669 -0.1249 1129 LEU   B CA  
8629  C  C   . LEU   B 825 ? 1.5000 1.4682 2.0714 -0.1289 -0.2744 -0.1253 1129 LEU   B C   
8630  O  O   . LEU   B 825 ? 1.4695 1.4365 2.0156 -0.1257 -0.2653 -0.1187 1129 LEU   B O   
8631  C  CB  . LEU   B 825 ? 1.5032 1.4976 2.1151 -0.1351 -0.2681 -0.1266 1129 LEU   B CB  
8632  C  CG  . LEU   B 825 ? 1.4507 1.4584 2.0817 -0.1419 -0.2529 -0.1214 1129 LEU   B CG  
8633  C  CD1 . LEU   B 825 ? 1.3765 1.3978 2.0155 -0.1392 -0.2559 -0.1242 1129 LEU   B CD1 
8634  C  CD2 . LEU   B 825 ? 1.4381 1.4442 2.0465 -0.1419 -0.2372 -0.1119 1129 LEU   B CD2 
8635  N  N   . ILE   B 826 ? 1.5265 1.4860 2.0963 -0.1245 -0.2910 -0.1331 1130 ILE   B N   
8636  C  CA  . ILE   B 826 ? 1.4245 1.3712 1.9618 -0.1160 -0.2981 -0.1336 1130 ILE   B CA  
8637  C  C   . ILE   B 826 ? 1.4233 1.3595 1.9483 -0.1185 -0.2893 -0.1277 1130 ILE   B C   
8638  O  O   . ILE   B 826 ? 1.4231 1.3528 1.9181 -0.1125 -0.2869 -0.1239 1130 ILE   B O   
8639  C  CB  . ILE   B 826 ? 1.3474 1.2851 1.8864 -0.1112 -0.3176 -0.1432 1130 ILE   B CB  
8640  C  CG1 . ILE   B 826 ? 1.4083 1.3540 1.9460 -0.1051 -0.3265 -0.1481 1130 ILE   B CG1 
8641  C  CG2 . ILE   B 826 ? 1.2806 1.2031 1.7892 -0.1039 -0.3233 -0.1432 1130 ILE   B CG2 
8642  C  CD1 . ILE   B 826 ? 1.4741 1.4325 2.0474 -0.1113 -0.3280 -0.1520 1130 ILE   B CD1 
8643  N  N   . LYS   B 827 ? 1.4278 1.3619 1.9758 -0.1274 -0.2840 -0.1268 1131 LYS   B N   
8644  C  CA  . LYS   B 827 ? 1.4378 1.3621 1.9750 -0.1302 -0.2743 -0.1207 1131 LYS   B CA  
8645  C  C   . LYS   B 827 ? 1.4326 1.3637 1.9544 -0.1303 -0.2576 -0.1114 1131 LYS   B C   
8646  O  O   . LYS   B 827 ? 1.4091 1.3332 1.9028 -0.1255 -0.2537 -0.1068 1131 LYS   B O   
8647  C  CB  . LYS   B 827 ? 1.3717 1.2929 1.9388 -0.1401 -0.2716 -0.1216 1131 LYS   B CB  
8648  N  N   . VAL   B 828 ? 1.3687 1.3136 1.9082 -0.1352 -0.2480 -0.1087 1132 VAL   B N   
8649  C  CA  . VAL   B 828 ? 1.3949 1.3456 1.9227 -0.1363 -0.2316 -0.0998 1132 VAL   B CA  
8650  C  C   . VAL   B 828 ? 1.4017 1.3521 1.8959 -0.1273 -0.2322 -0.0972 1132 VAL   B C   
8651  O  O   . VAL   B 828 ? 1.4102 1.3562 1.8837 -0.1258 -0.2230 -0.0906 1132 VAL   B O   
8652  C  CB  . VAL   B 828 ? 1.4016 1.3677 1.9533 -0.1418 -0.2232 -0.0984 1132 VAL   B CB  
8653  C  CG1 . VAL   B 828 ? 1.4859 1.4531 2.0736 -0.1499 -0.2258 -0.1028 1132 VAL   B CG1 
8654  C  CG2 . VAL   B 828 ? 1.3975 1.3744 1.9445 -0.1361 -0.2293 -0.1014 1132 VAL   B CG2 
8655  N  N   . VAL   B 829 ? 1.3864 1.3410 1.8745 -0.1209 -0.2432 -0.1023 1133 VAL   B N   
8656  C  CA  . VAL   B 829 ? 1.3596 1.3141 1.8168 -0.1122 -0.2437 -0.0999 1133 VAL   B CA  
8657  C  C   . VAL   B 829 ? 1.4185 1.3582 1.8517 -0.1076 -0.2471 -0.0989 1133 VAL   B C   
8658  O  O   . VAL   B 829 ? 1.4112 1.3493 1.8204 -0.1036 -0.2402 -0.0932 1133 VAL   B O   
8659  C  CB  . VAL   B 829 ? 1.3804 1.3405 1.8358 -0.1061 -0.2555 -0.1060 1133 VAL   B CB  
8660  C  CG1 . VAL   B 829 ? 1.3564 1.3079 1.7807 -0.0966 -0.2621 -0.1064 1133 VAL   B CG1 
8661  C  CG2 . VAL   B 829 ? 1.3259 1.3013 1.7866 -0.1069 -0.2478 -0.1032 1133 VAL   B CG2 
8662  N  N   . GLU   B 830 ? 1.4291 1.3577 1.8684 -0.1076 -0.2582 -0.1047 1134 GLU   B N   
8663  C  CA  . GLU   B 830 ? 1.4014 1.3151 1.8184 -0.1028 -0.2623 -0.1043 1134 GLU   B CA  
8664  C  C   . GLU   B 830 ? 1.3837 1.2937 1.7897 -0.1056 -0.2482 -0.0960 1134 GLU   B C   
8665  O  O   . GLU   B 830 ? 1.4123 1.3172 1.7914 -0.0996 -0.2461 -0.0923 1134 GLU   B O   
8666  C  CB  . GLU   B 830 ? 1.4506 1.3530 1.8809 -0.1046 -0.2747 -0.1114 1134 GLU   B CB  
8667  N  N   . GLU   B 831 ? 1.3420 1.2550 1.7683 -0.1145 -0.2381 -0.0927 1135 GLU   B N   
8668  C  CA  . GLU   B 831 ? 1.3620 1.2718 1.7776 -0.1170 -0.2240 -0.0846 1135 GLU   B CA  
8669  C  C   . GLU   B 831 ? 1.3806 1.2973 1.7727 -0.1115 -0.2169 -0.0791 1135 GLU   B C   
8670  O  O   . GLU   B 831 ? 1.3963 1.3064 1.7664 -0.1082 -0.2117 -0.0741 1135 GLU   B O   
8671  C  CB  . GLU   B 831 ? 1.3343 1.2492 1.7758 -0.1269 -0.2128 -0.0816 1135 GLU   B CB  
8672  N  N   . LEU   B 832 ? 1.3778 1.3076 1.7745 -0.1101 -0.2170 -0.0800 1136 LEU   B N   
8673  C  CA  . LEU   B 832 ? 1.3168 1.2543 1.6942 -0.1057 -0.2097 -0.0748 1136 LEU   B CA  
8674  C  C   . LEU   B 832 ? 1.3208 1.2526 1.6703 -0.0962 -0.2171 -0.0757 1136 LEU   B C   
8675  O  O   . LEU   B 832 ? 1.3375 1.2689 1.6661 -0.0926 -0.2103 -0.0701 1136 LEU   B O   
8676  C  CB  . LEU   B 832 ? 1.2694 1.2219 1.6601 -0.1070 -0.2085 -0.0760 1136 LEU   B CB  
8677  C  CG  . LEU   B 832 ? 1.2592 1.2181 1.6799 -0.1160 -0.2024 -0.0761 1136 LEU   B CG  
8678  C  CD1 . LEU   B 832 ? 1.2034 1.1771 1.6327 -0.1160 -0.2001 -0.0764 1136 LEU   B CD1 
8679  C  CD2 . LEU   B 832 ? 1.2485 1.2038 1.6697 -0.1215 -0.1884 -0.0691 1136 LEU   B CD2 
8680  N  N   . THR   B 833 ? 1.3059 1.2335 1.6549 -0.0917 -0.2309 -0.0826 1137 THR   B N   
8681  C  CA  . THR   B 833 ? 1.3148 1.2357 1.6375 -0.0823 -0.2379 -0.0836 1137 THR   B CA  
8682  C  C   . THR   B 833 ? 1.3377 1.2467 1.6426 -0.0807 -0.2340 -0.0795 1137 THR   B C   
8683  O  O   . THR   B 833 ? 1.3422 1.2487 1.6229 -0.0737 -0.2334 -0.0768 1137 THR   B O   
8684  C  CB  . THR   B 833 ? 1.3490 1.2643 1.6749 -0.0782 -0.2537 -0.0921 1137 THR   B CB  
8685  O  OG1 . THR   B 833 ? 1.3784 1.2808 1.7111 -0.0806 -0.2597 -0.0953 1137 THR   B OG1 
8686  C  CG2 . THR   B 833 ? 1.3396 1.2659 1.6884 -0.0814 -0.2575 -0.0965 1137 THR   B CG2 
8687  N  N   . ARG   B 834 ? 1.3353 1.2375 1.6525 -0.0872 -0.2305 -0.0785 1138 ARG   B N   
8688  C  CA  . ARG   B 834 ? 1.3594 1.2493 1.6613 -0.0861 -0.2272 -0.0749 1138 ARG   B CA  
8689  C  C   . ARG   B 834 ? 1.3451 1.2387 1.6311 -0.0852 -0.2143 -0.0668 1138 ARG   B C   
8690  O  O   . ARG   B 834 ? 1.3889 1.2734 1.6550 -0.0810 -0.2130 -0.0638 1138 ARG   B O   
8691  C  CB  . ARG   B 834 ? 1.3469 1.2286 1.6679 -0.0938 -0.2264 -0.0760 1138 ARG   B CB  
8692  N  N   . ILE   B 835 ? 1.3169 1.2231 1.6109 -0.0888 -0.2051 -0.0631 1139 ILE   B N   
8693  C  CA  . ILE   B 835 ? 1.3357 1.2452 1.6149 -0.0880 -0.1933 -0.0556 1139 ILE   B CA  
8694  C  C   . ILE   B 835 ? 1.3375 1.2468 1.5904 -0.0788 -0.1960 -0.0542 1139 ILE   B C   
8695  O  O   . ILE   B 835 ? 1.2661 1.1738 1.5026 -0.0767 -0.1886 -0.0485 1139 ILE   B O   
8696  C  CB  . ILE   B 835 ? 1.3021 1.2252 1.5949 -0.0931 -0.1840 -0.0527 1139 ILE   B CB  
8697  C  CG1 . ILE   B 835 ? 1.3813 1.3060 1.6619 -0.0937 -0.1710 -0.0448 1139 ILE   B CG1 
8698  C  CG2 . ILE   B 835 ? 1.1856 1.1200 1.4773 -0.0889 -0.1892 -0.0556 1139 ILE   B CG2 
8699  C  CD1 . ILE   B 835 ? 1.3035 1.2150 1.5758 -0.0951 -0.1660 -0.0410 1139 ILE   B CD1 
8700  N  N   . HIS   B 836 ? 1.3086 1.2193 1.5570 -0.0732 -0.2063 -0.0593 1140 HIS   B N   
8701  C  CA  . HIS   B 836 ? 1.3113 1.2210 1.5355 -0.0642 -0.2092 -0.0583 1140 HIS   B CA  
8702  C  C   . HIS   B 836 ? 1.3049 1.2046 1.5224 -0.0585 -0.2222 -0.0644 1140 HIS   B C   
8703  O  O   . HIS   B 836 ? 1.3410 1.2341 1.5376 -0.0512 -0.2249 -0.0637 1140 HIS   B O   
8704  C  CB  . HIS   B 836 ? 1.3169 1.2405 1.5388 -0.0619 -0.2067 -0.0572 1140 HIS   B CB  
8705  C  CG  . HIS   B 836 ? 1.2456 1.1751 1.4821 -0.0625 -0.2146 -0.0632 1140 HIS   B CG  
8706  N  ND1 . HIS   B 836 ? 1.2182 1.1482 1.4446 -0.0553 -0.2232 -0.0670 1140 HIS   B ND1 
8707  C  CD2 . HIS   B 836 ? 1.2286 1.1633 1.4892 -0.0691 -0.2152 -0.0662 1140 HIS   B CD2 
8708  C  CE1 . HIS   B 836 ? 1.2089 1.1439 1.4518 -0.0573 -0.2293 -0.0722 1140 HIS   B CE1 
8709  N  NE2 . HIS   B 836 ? 1.2201 1.1584 1.4845 -0.0657 -0.2247 -0.0718 1140 HIS   B NE2 
8710  N  N   . SER   C 3   ? 1.6947 1.3469 1.1089 0.0806  -0.1294 0.0060  868  SER   C N   
8711  C  CA  . SER   C 3   ? 1.7219 1.3883 1.1556 0.0741  -0.1148 0.0092  868  SER   C CA  
8712  C  C   . SER   C 3   ? 1.7151 1.3759 1.1437 0.0756  -0.0973 0.0154  868  SER   C C   
8713  O  O   . SER   C 3   ? 1.6678 1.3463 1.1200 0.0693  -0.0902 0.0181  868  SER   C O   
8714  C  CB  . SER   C 3   ? 1.7116 1.3716 1.1375 0.0750  -0.1124 0.0076  868  SER   C CB  
8715  O  OG  . SER   C 3   ? 1.5548 1.2164 0.9847 0.0734  -0.0944 0.0122  868  SER   C OG  
8716  N  N   . LEU   C 4   ? 1.7643 1.3999 1.1619 0.0842  -0.0902 0.0177  869  LEU   C N   
8717  C  CA  . LEU   C 4   ? 1.7055 1.3315 1.0937 0.0872  -0.0741 0.0237  869  LEU   C CA  
8718  C  C   . LEU   C 4   ? 1.6943 1.3183 1.0798 0.0890  -0.0775 0.0251  869  LEU   C C   
8719  O  O   . LEU   C 4   ? 1.7015 1.3139 1.0750 0.0925  -0.0654 0.0299  869  LEU   C O   
8720  C  CB  . LEU   C 4   ? 1.7763 1.3742 1.1300 0.0966  -0.0663 0.0255  869  LEU   C CB  
8721  C  CG  . LEU   C 4   ? 1.7529 1.3484 1.1057 0.0962  -0.0526 0.0276  869  LEU   C CG  
8722  C  CD1 . LEU   C 4   ? 1.5542 1.1184 0.8685 0.1072  -0.0453 0.0300  869  LEU   C CD1 
8723  C  CD2 . LEU   C 4   ? 1.6939 1.3078 1.0737 0.0888  -0.0371 0.0321  869  LEU   C CD2 
8724  N  N   . THR   C 5   ? 1.7209 1.3557 1.1174 0.0866  -0.0935 0.0211  870  THR   C N   
8725  C  CA  . THR   C 5   ? 1.6894 1.3230 1.0839 0.0885  -0.0988 0.0219  870  THR   C CA  
8726  C  C   . THR   C 5   ? 1.6663 1.3274 1.0946 0.0797  -0.1062 0.0201  870  THR   C C   
8727  O  O   . THR   C 5   ? 1.6862 1.3488 1.1153 0.0809  -0.1147 0.0193  870  THR   C O   
8728  C  CB  . THR   C 5   ? 1.7031 1.3158 1.0690 0.0976  -0.1128 0.0184  870  THR   C CB  
8729  O  OG1 . THR   C 5   ? 1.7549 1.3804 1.1348 0.0942  -0.1304 0.0125  870  THR   C OG1 
8730  C  CG2 . THR   C 5   ? 1.7259 1.3135 1.0605 0.1056  -0.1082 0.0188  870  THR   C CG2 
8731  N  N   . THR   C 6   ? 1.5965 1.2786 1.0517 0.0714  -0.1033 0.0194  871  THR   C N   
8732  C  CA  . THR   C 6   ? 1.5649 1.2729 1.0523 0.0630  -0.1076 0.0185  871  THR   C CA  
8733  C  C   . THR   C 6   ? 1.5469 1.2658 1.0512 0.0579  -0.0918 0.0234  871  THR   C C   
8734  O  O   . THR   C 6   ? 1.5348 1.2488 1.0353 0.0579  -0.0787 0.0262  871  THR   C O   
8735  C  CB  . THR   C 6   ? 1.5839 1.3086 1.0911 0.0571  -0.1169 0.0140  871  THR   C CB  
8736  O  OG1 . THR   C 6   ? 1.6460 1.3791 1.1655 0.0523  -0.1054 0.0157  871  THR   C OG1 
8737  C  CG2 . THR   C 6   ? 1.5609 1.2707 1.0478 0.0627  -0.1296 0.0095  871  THR   C CG2 
8738  N  N   . CYS   C 7   ? 1.5272 1.2601 1.0494 0.0538  -0.0929 0.0244  872  CYS   C N   
8739  C  CA  . CYS   C 7   ? 1.4899 1.2342 1.0299 0.0486  -0.0793 0.0286  872  CYS   C CA  
8740  C  C   . CYS   C 7   ? 1.4720 1.2389 1.0406 0.0401  -0.0781 0.0272  872  CYS   C C   
8741  O  O   . CYS   C 7   ? 1.4493 1.2311 1.0342 0.0361  -0.0896 0.0235  872  CYS   C O   
8742  C  CB  . CYS   C 7   ? 1.4351 1.1852 0.9828 0.0477  -0.0812 0.0302  872  CYS   C CB  
8743  S  SG  . CYS   C 7   ? 1.4467 1.2127 1.0194 0.0405  -0.0661 0.0348  872  CYS   C SG  
8744  N  N   . GLU   C 8   ? 1.5372 1.3065 1.1124 0.0376  -0.0641 0.0302  873  GLU   C N   
8745  C  CA  . GLU   C 8   ? 1.5533 1.3436 1.1554 0.0298  -0.0619 0.0291  873  GLU   C CA  
8746  C  C   . GLU   C 8   ? 1.5532 1.3648 1.1823 0.0232  -0.0650 0.0289  873  GLU   C C   
8747  O  O   . GLU   C 8   ? 1.5592 1.3889 1.2104 0.0170  -0.0677 0.0269  873  GLU   C O   
8748  C  CB  . GLU   C 8   ? 1.6075 1.3955 1.2112 0.0289  -0.0457 0.0326  873  GLU   C CB  
8749  C  CG  . GLU   C 8   ? 1.7084 1.4774 1.2882 0.0348  -0.0414 0.0327  873  GLU   C CG  
8750  C  CD  . GLU   C 8   ? 1.7964 1.5746 1.3876 0.0312  -0.0399 0.0307  873  GLU   C CD  
8751  O  OE1 . GLU   C 8   ? 1.7953 1.5936 1.4132 0.0241  -0.0373 0.0307  873  GLU   C OE1 
8752  O  OE2 . GLU   C 8   ? 1.8140 1.5789 1.3869 0.0357  -0.0416 0.0292  873  GLU   C OE2 
8753  N  N   . VAL   C 9   ? 1.4570 1.2664 1.0844 0.0244  -0.0645 0.0311  874  VAL   C N   
8754  C  CA  . VAL   C 9   ? 1.3506 1.1787 1.0027 0.0184  -0.0640 0.0319  874  VAL   C CA  
8755  C  C   . VAL   C 9   ? 1.3349 1.1720 0.9944 0.0176  -0.0786 0.0287  874  VAL   C C   
8756  O  O   . VAL   C 9   ? 1.3533 1.2098 1.0364 0.0116  -0.0827 0.0271  874  VAL   C O   
8757  C  CB  . VAL   C 9   ? 1.3098 1.1309 0.9579 0.0197  -0.0525 0.0366  874  VAL   C CB  
8758  C  CG1 . VAL   C 9   ? 1.3316 1.1712 1.0044 0.0137  -0.0525 0.0372  874  VAL   C CG1 
8759  C  CG2 . VAL   C 9   ? 1.3079 1.1222 0.9522 0.0199  -0.0378 0.0396  874  VAL   C CG2 
8760  N  N   . CYS   C 10  ? 1.3390 1.1621 0.9787 0.0237  -0.0864 0.0278  875  CYS   C N   
8761  C  CA  . CYS   C 10  ? 1.2965 1.1271 0.9424 0.0236  -0.1004 0.0249  875  CYS   C CA  
8762  C  C   . CYS   C 10  ? 1.3356 1.1609 0.9718 0.0264  -0.1131 0.0205  875  CYS   C C   
8763  O  O   . CYS   C 10  ? 1.3350 1.1694 0.9806 0.0253  -0.1253 0.0174  875  CYS   C O   
8764  C  CB  . CYS   C 10  ? 1.2992 1.1191 0.9321 0.0284  -0.1013 0.0269  875  CYS   C CB  
8765  S  SG  . CYS   C 10  ? 1.3288 1.1177 0.9222 0.0391  -0.1018 0.0277  875  CYS   C SG  
8766  N  N   . GLY   C 11  ? 1.3457 1.1559 0.9629 0.0303  -0.1105 0.0201  876  GLY   C N   
8767  C  CA  . GLY   C 11  ? 1.3777 1.1817 0.9849 0.0330  -0.1224 0.0158  876  GLY   C CA  
8768  C  C   . GLY   C 11  ? 1.4165 1.2020 0.9990 0.0410  -0.1316 0.0144  876  GLY   C C   
8769  O  O   . GLY   C 11  ? 1.4209 1.2055 1.0007 0.0425  -0.1452 0.0101  876  GLY   C O   
8770  N  N   . ALA   C 12  ? 1.4419 1.2121 1.0061 0.0464  -0.1249 0.0179  877  ALA   C N   
8771  C  CA  . ALA   C 12  ? 1.4041 1.1555 0.9433 0.0546  -0.1336 0.0167  877  ALA   C CA  
8772  C  C   . ALA   C 12  ? 1.4756 1.2056 0.9875 0.0611  -0.1343 0.0154  877  ALA   C C   
8773  O  O   . ALA   C 12  ? 1.5176 1.2441 1.0264 0.0602  -0.1240 0.0170  877  ALA   C O   
8774  C  CB  . ALA   C 12  ? 1.4197 1.1619 0.9487 0.0581  -0.1257 0.0211  877  ALA   C CB  
8775  N  N   . CYS   C 13  ? 1.4735 1.1892 0.9658 0.0679  -0.1469 0.0123  878  CYS   C N   
8776  C  CA  . CYS   C 13  ? 1.5710 1.2649 1.0355 0.0748  -0.1489 0.0107  878  CYS   C CA  
8777  C  C   . CYS   C 13  ? 1.5978 1.2669 1.0306 0.0849  -0.1523 0.0114  878  CYS   C C   
8778  O  O   . CYS   C 13  ? 1.5682 1.2363 0.9986 0.0877  -0.1663 0.0082  878  CYS   C O   
8779  C  CB  . CYS   C 13  ? 1.5200 1.2197 0.9909 0.0731  -0.1633 0.0049  878  CYS   C CB  
8780  S  SG  . CYS   C 13  ? 1.6494 1.3343 1.1023 0.0758  -0.1577 0.0042  878  CYS   C SG  
8781  N  N   . PHE   C 14  ? 1.6045 1.2530 1.0127 0.0906  -0.1397 0.0152  879  PHE   C N   
8782  C  CA  . PHE   C 14  ? 1.6405 1.2623 1.0148 0.1010  -0.1405 0.0165  879  PHE   C CA  
8783  C  C   . PHE   C 14  ? 1.6512 1.2509 0.9969 0.1087  -0.1463 0.0136  879  PHE   C C   
8784  O  O   . PHE   C 14  ? 1.6529 1.2544 1.0011 0.1065  -0.1440 0.0123  879  PHE   C O   
8785  C  CB  . PHE   C 14  ? 1.6060 1.2176 0.9703 0.1029  -0.1219 0.0231  879  PHE   C CB  
8786  C  CG  . PHE   C 14  ? 1.6358 1.2666 1.0258 0.0959  -0.1157 0.0260  879  PHE   C CG  
8787  C  CD1 . PHE   C 14  ? 1.6427 1.2847 1.0451 0.0945  -0.1270 0.0241  879  PHE   C CD1 
8788  C  CD2 . PHE   C 14  ? 1.6465 1.2844 1.0488 0.0909  -0.0983 0.0307  879  PHE   C CD2 
8789  C  CE1 . PHE   C 14  ? 1.5740 1.2334 0.9998 0.0882  -0.1213 0.0267  879  PHE   C CE1 
8790  C  CE2 . PHE   C 14  ? 1.5999 1.2553 1.0261 0.0845  -0.0929 0.0333  879  PHE   C CE2 
8791  C  CZ  . PHE   C 14  ? 1.5500 1.2160 0.9876 0.0832  -0.1044 0.0313  879  PHE   C CZ  
8792  N  N   . GLU   C 15  ? 1.6343 1.2117 0.9511 0.1183  -0.1537 0.0127  880  GLU   C N   
8793  C  CA  . GLU   C 15  ? 1.7253 1.2784 1.0110 0.1268  -0.1586 0.0102  880  GLU   C CA  
8794  C  C   . GLU   C 15  ? 1.7767 1.3125 1.0423 0.1305  -0.1403 0.0151  880  GLU   C C   
8795  O  O   . GLU   C 15  ? 1.8121 1.3319 1.0573 0.1355  -0.1411 0.0135  880  GLU   C O   
8796  C  CB  . GLU   C 15  ? 1.6611 1.1945 0.9207 0.1366  -0.1722 0.0077  880  GLU   C CB  
8797  N  N   . THR   C 16  ? 1.7408 1.2810 1.0142 0.1276  -0.1236 0.0211  881  THR   C N   
8798  C  CA  . THR   C 16  ? 1.7444 1.2649 0.9955 0.1327  -0.1058 0.0264  881  THR   C CA  
8799  C  C   . THR   C 16  ? 1.6912 1.2293 0.9676 0.1241  -0.0883 0.0311  881  THR   C C   
8800  O  O   . THR   C 16  ? 1.6332 1.1934 0.9381 0.1163  -0.0874 0.0320  881  THR   C O   
8801  C  CB  . THR   C 16  ? 1.7827 1.2815 1.0074 0.1412  -0.1028 0.0297  881  THR   C CB  
8802  O  OG1 . THR   C 16  ? 1.8550 1.3378 1.0631 0.1448  -0.0830 0.0358  881  THR   C OG1 
8803  C  CG2 . THR   C 16  ? 1.6998 1.2163 0.9470 0.1360  -0.1055 0.0308  881  THR   C CG2 
8804  N  N   . ARG   C 17  ? 1.7376 1.2650 1.0028 0.1261  -0.0743 0.0340  882  ARG   C N   
8805  C  CA  . ARG   C 17  ? 1.7336 1.2759 1.0213 0.1187  -0.0570 0.0384  882  ARG   C CA  
8806  C  C   . ARG   C 17  ? 1.6595 1.1952 0.9434 0.1199  -0.0422 0.0447  882  ARG   C C   
8807  O  O   . ARG   C 17  ? 1.6439 1.1916 0.9472 0.1138  -0.0277 0.0486  882  ARG   C O   
8808  C  CB  . ARG   C 17  ? 1.7395 1.2744 1.0192 0.1199  -0.0474 0.0391  882  ARG   C CB  
8809  N  N   . LYS   C 18  ? 1.6665 1.1835 0.9267 0.1274  -0.0455 0.0459  883  LYS   C N   
8810  C  CA  . LYS   C 18  ? 1.6871 1.2032 0.9505 0.1267  -0.0340 0.0512  883  LYS   C CA  
8811  C  C   . LYS   C 18  ? 1.6389 1.1783 0.9302 0.1195  -0.0435 0.0495  883  LYS   C C   
8812  O  O   . LYS   C 18  ? 1.6260 1.1817 0.9415 0.1123  -0.0339 0.0526  883  LYS   C O   
8813  C  CB  . LYS   C 18  ? 1.6956 1.1807 0.9208 0.1381  -0.0318 0.0538  883  LYS   C CB  
8814  C  CG  . LYS   C 18  ? 1.6513 1.1358 0.8800 0.1373  -0.0229 0.0588  883  LYS   C CG  
8815  C  CD  . LYS   C 18  ? 1.6650 1.1337 0.8810 0.1400  -0.0005 0.0657  883  LYS   C CD  
8816  C  CE  . LYS   C 18  ? 1.6389 1.1101 0.8638 0.1374  0.0098  0.0708  883  LYS   C CE  
8817  N  NZ  . LYS   C 18  ? 1.6971 1.1476 0.8950 0.1460  0.0043  0.0716  883  LYS   C NZ  
8818  N  N   . GLY   C 19  ? 1.6163 1.1571 0.9044 0.1217  -0.0623 0.0443  884  GLY   C N   
8819  C  CA  . GLY   C 19  ? 1.6067 1.1709 0.9224 0.1149  -0.0730 0.0418  884  GLY   C CA  
8820  C  C   . GLY   C 19  ? 1.6096 1.2018 0.9624 0.1035  -0.0660 0.0426  884  GLY   C C   
8821  O  O   . GLY   C 19  ? 1.6395 1.2478 1.0142 0.0977  -0.0639 0.0442  884  GLY   C O   
8822  N  N   . LEU   C 20  ? 1.5839 1.1807 0.9427 0.1006  -0.0615 0.0417  885  LEU   C N   
8823  C  CA  . LEU   C 20  ? 1.6101 1.2336 1.0038 0.0901  -0.0565 0.0418  885  LEU   C CA  
8824  C  C   . LEU   C 20  ? 1.5865 1.2136 0.9909 0.0865  -0.0382 0.0477  885  LEU   C C   
8825  O  O   . LEU   C 20  ? 1.5588 1.2086 0.9934 0.0780  -0.0357 0.0482  885  LEU   C O   
8826  C  CB  . LEU   C 20  ? 1.6091 1.2358 1.0056 0.0884  -0.0568 0.0393  885  LEU   C CB  
8827  C  CG  . LEU   C 20  ? 1.5656 1.2162 0.9888 0.0811  -0.0698 0.0342  885  LEU   C CG  
8828  C  CD1 . LEU   C 20  ? 1.6937 1.3486 1.1222 0.0785  -0.0672 0.0325  885  LEU   C CD1 
8829  C  CD2 . LEU   C 20  ? 1.5042 1.1796 0.9599 0.0723  -0.0684 0.0351  885  LEU   C CD2 
8830  N  N   . SER   C 21  ? 1.5236 1.1286 0.9041 0.0928  -0.0250 0.0522  886  SER   C N   
8831  C  CA  . SER   C 21  ? 1.5500 1.1582 0.9416 0.0892  -0.0074 0.0578  886  SER   C CA  
8832  C  C   . SER   C 21  ? 1.6101 1.2219 1.0080 0.0880  -0.0085 0.0597  886  SER   C C   
8833  O  O   . SER   C 21  ? 1.5789 1.2085 1.0032 0.0805  -0.0022 0.0616  886  SER   C O   
8834  C  CB  . SER   C 21  ? 1.5620 1.1454 0.9269 0.0962  0.0077  0.0623  886  SER   C CB  
8835  O  OG  . SER   C 21  ? 1.6722 1.2311 1.0056 0.1055  0.0056  0.0637  886  SER   C OG  
8836  N  N   . SER   C 22  ? 1.5609 1.1559 0.9349 0.0955  -0.0170 0.0591  887  SER   C N   
8837  C  CA  . SER   C 22  ? 1.5823 1.1806 0.9618 0.0947  -0.0192 0.0606  887  SER   C CA  
8838  C  C   . SER   C 22  ? 1.6045 1.2313 1.0170 0.0861  -0.0298 0.0571  887  SER   C C   
8839  O  O   . SER   C 22  ? 1.6992 1.3351 1.1256 0.0827  -0.0283 0.0589  887  SER   C O   
8840  C  CB  . SER   C 22  ? 1.5925 1.1684 0.9406 0.1047  -0.0288 0.0597  887  SER   C CB  
8841  O  OG  . SER   C 22  ? 1.5871 1.1662 0.9323 0.1065  -0.0468 0.0537  887  SER   C OG  
8842  N  N   . HIS   C 23  ? 1.5497 1.1901 0.9746 0.0828  -0.0403 0.0523  888  HIS   C N   
8843  C  CA  . HIS   C 23  ? 1.5662 1.2346 1.0244 0.0740  -0.0479 0.0495  888  HIS   C CA  
8844  C  C   . HIS   C 23  ? 1.6139 1.2992 1.0983 0.0656  -0.0347 0.0521  888  HIS   C C   
8845  O  O   . HIS   C 23  ? 1.6612 1.3647 1.1700 0.0592  -0.0346 0.0525  888  HIS   C O   
8846  C  CB  . HIS   C 23  ? 1.5309 1.2075 0.9935 0.0733  -0.0632 0.0436  888  HIS   C CB  
8847  C  CG  . HIS   C 23  ? 1.5083 1.2132 1.0048 0.0642  -0.0701 0.0408  888  HIS   C CG  
8848  N  ND1 . HIS   C 23  ? 1.5882 1.3070 1.1019 0.0607  -0.0745 0.0408  888  HIS   C ND1 
8849  C  CD2 . HIS   C 23  ? 1.4969 1.2183 1.0124 0.0584  -0.0733 0.0378  888  HIS   C CD2 
8850  C  CE1 . HIS   C 23  ? 1.5385 1.2807 1.0801 0.0531  -0.0798 0.0381  888  HIS   C CE1 
8851  N  NE2 . HIS   C 23  ? 1.4620 1.2061 1.0052 0.0516  -0.0792 0.0362  888  HIS   C NE2 
8852  N  N   . ALA   C 24  ? 1.5944 1.2733 1.0737 0.0659  -0.0234 0.0539  889  ALA   C N   
8853  C  CA  . ALA   C 24  ? 1.5488 1.2443 1.0538 0.0581  -0.0117 0.0559  889  ALA   C CA  
8854  C  C   . ALA   C 24  ? 1.6346 1.3326 1.1496 0.0553  -0.0008 0.0604  889  ALA   C C   
8855  O  O   . ALA   C 24  ? 1.7091 1.4269 1.2522 0.0475  0.0031  0.0608  889  ALA   C O   
8856  C  CB  . ALA   C 24  ? 1.5268 1.2124 1.0218 0.0601  -0.0008 0.0574  889  ALA   C CB  
8857  N  N   . ARG   C 25  ? 1.6312 1.3088 1.1233 0.0617  0.0043  0.0638  890  ARG   C N   
8858  C  CA  . ARG   C 25  ? 1.6155 1.2955 1.1171 0.0591  0.0124  0.0677  890  ARG   C CA  
8859  C  C   . ARG   C 25  ? 1.6612 1.3637 1.1885 0.0527  0.0020  0.0650  890  ARG   C C   
8860  O  O   . ARG   C 25  ? 1.6952 1.4153 1.2489 0.0453  0.0076  0.0659  890  ARG   C O   
8861  C  CB  . ARG   C 25  ? 1.7257 1.3804 1.1971 0.0676  0.0151  0.0708  890  ARG   C CB  
8862  N  N   . SER   C 26  ? 1.7136 1.4162 1.2340 0.0557  -0.0135 0.0614  891  SER   C N   
8863  C  CA  . SER   C 26  ? 1.7246 1.4458 1.2660 0.0510  -0.0233 0.0593  891  SER   C CA  
8864  C  C   . SER   C 26  ? 1.7261 1.4738 1.2997 0.0421  -0.0261 0.0565  891  SER   C C   
8865  O  O   . SER   C 26  ? 1.7036 1.4678 1.2951 0.0382  -0.0353 0.0542  891  SER   C O   
8866  C  CB  . SER   C 26  ? 1.7080 1.4232 1.2348 0.0566  -0.0396 0.0557  891  SER   C CB  
8867  O  OG  . SER   C 26  ? 1.7424 1.4700 1.2788 0.0544  -0.0514 0.0508  891  SER   C OG  
8868  N  N   . HIS   C 27  ? 1.6182 1.3700 1.1990 0.0391  -0.0183 0.0568  892  HIS   C N   
8869  C  CA  . HIS   C 27  ? 1.5594 1.3349 1.1709 0.0305  -0.0174 0.0553  892  HIS   C CA  
8870  C  C   . HIS   C 27  ? 1.6160 1.3958 1.2417 0.0261  -0.0023 0.0592  892  HIS   C C   
8871  O  O   . HIS   C 27  ? 1.7077 1.5065 1.3593 0.0193  -0.0025 0.0586  892  HIS   C O   
8872  C  CB  . HIS   C 27  ? 1.5627 1.3427 1.1764 0.0295  -0.0201 0.0523  892  HIS   C CB  
8873  C  CG  . HIS   C 27  ? 1.4921 1.2769 1.1040 0.0306  -0.0364 0.0474  892  HIS   C CG  
8874  N  ND1 . HIS   C 27  ? 1.4421 1.2456 1.0742 0.0261  -0.0469 0.0446  892  HIS   C ND1 
8875  C  CD2 . HIS   C 27  ? 1.4505 1.2238 1.0435 0.0357  -0.0438 0.0449  892  HIS   C CD2 
8876  C  CE1 . HIS   C 27  ? 1.3630 1.1667 0.9895 0.0281  -0.0599 0.0406  892  HIS   C CE1 
8877  N  NE2 . HIS   C 27  ? 1.3641 1.1496 0.9670 0.0339  -0.0587 0.0405  892  HIS   C NE2 
8878  N  N   . LEU   C 28  ? 1.5622 1.3244 1.1717 0.0298  0.0106  0.0633  893  LEU   C N   
8879  C  CA  . LEU   C 28  ? 1.6596 1.4244 1.2823 0.0258  0.0256  0.0673  893  LEU   C CA  
8880  C  C   . LEU   C 28  ? 1.6931 1.4540 1.3160 0.0258  0.0288  0.0703  893  LEU   C C   
8881  O  O   . LEU   C 28  ? 1.5682 1.3101 1.1674 0.0323  0.0292  0.0724  893  LEU   C O   
8882  C  CB  . LEU   C 28  ? 1.6880 1.4360 1.2945 0.0296  0.0393  0.0706  893  LEU   C CB  
8883  C  CG  . LEU   C 28  ? 1.7080 1.4632 1.3230 0.0273  0.0427  0.0690  893  LEU   C CG  
8884  C  CD1 . LEU   C 28  ? 1.6439 1.3925 1.2414 0.0320  0.0319  0.0653  893  LEU   C CD1 
8885  C  CD2 . LEU   C 28  ? 1.6145 1.3600 1.2266 0.0280  0.0606  0.0734  893  LEU   C CD2 
8886  N  N   . HIS   D 4   ? 1.6498 1.5262 1.6431 -0.1241 -0.0214 0.0122  73   HIS   D N   
8887  C  CA  . HIS   D 4   ? 1.7451 1.6360 1.7565 -0.1281 -0.0223 0.0133  73   HIS   D CA  
8888  C  C   . HIS   D 4   ? 1.9006 1.8036 1.9118 -0.1262 -0.0300 0.0099  73   HIS   D C   
8889  O  O   . HIS   D 4   ? 1.9479 1.8480 1.9467 -0.1228 -0.0351 0.0065  73   HIS   D O   
8890  C  CB  . HIS   D 4   ? 1.6718 1.5657 1.6866 -0.1254 -0.0134 0.0180  73   HIS   D CB  
8891  C  CG  . HIS   D 4   ? 1.5716 1.4524 1.5833 -0.1256 -0.0045 0.0218  73   HIS   D CG  
8892  N  ND1 . HIS   D 4   ? 1.5405 1.4162 1.5423 -0.1192 0.0036  0.0252  73   HIS   D ND1 
8893  C  CD2 . HIS   D 4   ? 1.6377 1.5086 1.6546 -0.1314 -0.0023 0.0228  73   HIS   D CD2 
8894  C  CE1 . HIS   D 4   ? 1.6341 1.4971 1.6345 -0.1208 0.0109  0.0282  73   HIS   D CE1 
8895  N  NE2 . HIS   D 4   ? 1.7096 1.5697 1.7196 -0.1284 0.0076  0.0269  73   HIS   D NE2 
8896  N  N   . ASP   D 5   ? 1.9957 1.9123 2.0209 -0.1283 -0.0307 0.0110  74   ASP   D N   
8897  C  CA  . ASP   D 5   ? 2.0620 1.9906 2.0885 -0.1268 -0.0374 0.0082  74   ASP   D CA  
8898  C  C   . ASP   D 5   ? 2.0750 2.0100 2.0957 -0.1199 -0.0337 0.0098  74   ASP   D C   
8899  O  O   . ASP   D 5   ? 2.0609 1.9914 2.0776 -0.1166 -0.0262 0.0131  74   ASP   D O   
8900  C  CB  . ASP   D 5   ? 2.0663 2.0053 2.1119 -0.1336 -0.0418 0.0079  74   ASP   D CB  
8901  C  CG  . ASP   D 5   ? 2.1134 2.0484 2.1610 -0.1387 -0.0498 0.0041  74   ASP   D CG  
8902  O  OD1 . ASP   D 5   ? 2.0695 2.0014 2.1044 -0.1357 -0.0552 0.0006  74   ASP   D OD1 
8903  O  OD2 . ASP   D 5   ? 2.0760 2.0102 2.1376 -0.1455 -0.0507 0.0047  74   ASP   D OD2 
8904  N  N   . ASP   D 6   ? 2.3470 2.2921 2.3670 -0.1176 -0.0391 0.0075  75   ASP   D N   
8905  C  CA  . ASP   D 6   ? 2.3598 2.3099 2.3723 -0.1105 -0.0368 0.0081  75   ASP   D CA  
8906  C  C   . ASP   D 6   ? 2.3530 2.3091 2.3745 -0.1102 -0.0305 0.0121  75   ASP   D C   
8907  O  O   . ASP   D 6   ? 2.3391 2.2905 2.3525 -0.1049 -0.0245 0.0144  75   ASP   D O   
8908  C  CB  . ASP   D 6   ? 2.3657 2.3255 2.3771 -0.1089 -0.0437 0.0048  75   ASP   D CB  
8909  C  CG  . ASP   D 6   ? 2.3336 2.2960 2.3347 -0.1012 -0.0423 0.0046  75   ASP   D CG  
8910  O  OD1 . ASP   D 6   ? 2.3521 2.3052 2.3409 -0.0965 -0.0388 0.0049  75   ASP   D OD1 
8911  O  OD2 . ASP   D 6   ? 2.3259 2.2993 2.3313 -0.0999 -0.0447 0.0040  75   ASP   D OD2 
8912  N  N   . ASP   D 7   ? 2.0638 2.0298 2.1016 -0.1153 -0.0319 0.0131  76   ASP   D N   
8913  C  CA  . ASP   D 7   ? 1.8952 1.8671 1.9433 -0.1155 -0.0258 0.0170  76   ASP   D CA  
8914  C  C   . ASP   D 7   ? 1.8309 1.7990 1.8914 -0.1217 -0.0213 0.0198  76   ASP   D C   
8915  O  O   . ASP   D 7   ? 1.8415 1.8182 1.9176 -0.1253 -0.0200 0.0218  76   ASP   D O   
8916  C  CB  . ASP   D 7   ? 1.9245 1.9113 1.9831 -0.1165 -0.0301 0.0163  76   ASP   D CB  
8917  C  CG  . ASP   D 7   ? 1.8871 1.8810 1.9536 -0.1149 -0.0241 0.0201  76   ASP   D CG  
8918  O  OD1 . ASP   D 7   ? 1.8364 1.8259 1.9086 -0.1164 -0.0167 0.0239  76   ASP   D OD1 
8919  O  OD2 . ASP   D 7   ? 1.8532 1.8569 1.9209 -0.1123 -0.0268 0.0193  76   ASP   D OD2 
8920  N  N   . SER   D 8   ? 1.8711 1.8265 1.9259 -0.1231 -0.0191 0.0200  77   SER   D N   
8921  C  CA  . SER   D 8   ? 1.8174 1.7689 1.8852 -0.1297 -0.0152 0.0224  77   SER   D CA  
8922  C  C   . SER   D 8   ? 1.7601 1.7091 1.8304 -0.1277 -0.0046 0.0276  77   SER   D C   
8923  O  O   . SER   D 8   ? 1.6401 1.5845 1.6968 -0.1207 0.0002  0.0292  77   SER   D O   
8924  C  CB  . SER   D 8   ? 1.8010 1.7390 1.8616 -0.1320 -0.0164 0.0209  77   SER   D CB  
8925  O  OG  . SER   D 8   ? 1.7560 1.6908 1.8309 -0.1389 -0.0131 0.0230  77   SER   D OG  
8926  N  N   . CYS   D 9   ? 1.8965 1.8486 1.9848 -0.1338 -0.0010 0.0303  78   CYS   D N   
8927  C  CA  . CYS   D 9   ? 1.8665 1.8143 1.9586 -0.1330 0.0101  0.0356  78   CYS   D CA  
8928  C  C   . CYS   D 9   ? 1.8331 1.7676 1.9257 -0.1371 0.0143  0.0369  78   CYS   D C   
8929  O  O   . CYS   D 9   ? 1.8525 1.7884 1.9594 -0.1447 0.0106  0.0357  78   CYS   D O   
8930  C  CB  . CYS   D 9   ? 1.8598 1.8203 1.9727 -0.1368 0.0123  0.0381  78   CYS   D CB  
8931  S  SG  . CYS   D 9   ? 1.9768 1.9549 2.0948 -0.1351 0.0040  0.0353  78   CYS   D SG  
8932  N  N   . GLN   D 10  ? 1.5962 1.5174 1.6734 -0.1321 0.0217  0.0393  79   GLN   D N   
8933  C  CA  . GLN   D 10  ? 1.6034 1.5100 1.6775 -0.1350 0.0259  0.0405  79   GLN   D CA  
8934  C  C   . GLN   D 10  ? 1.5479 1.4457 1.6201 -0.1326 0.0387  0.0463  79   GLN   D C   
8935  O  O   . GLN   D 10  ? 1.5114 1.4110 1.5765 -0.1261 0.0437  0.0487  79   GLN   D O   
8936  C  CB  . GLN   D 10  ? 1.6196 1.5153 1.6727 -0.1308 0.0214  0.0371  79   GLN   D CB  
8937  C  CG  . GLN   D 10  ? 1.6204 1.5241 1.6712 -0.1309 0.0095  0.0315  79   GLN   D CG  
8938  C  CD  . GLN   D 10  ? 1.6781 1.5859 1.7445 -0.1397 0.0024  0.0289  79   GLN   D CD  
8939  O  OE1 . GLN   D 10  ? 1.7500 1.6701 1.8341 -0.1441 0.0000  0.0290  79   GLN   D OE1 
8940  N  NE2 . GLN   D 10  ? 1.6281 1.5253 1.6878 -0.1418 -0.0012 0.0263  79   GLN   D NE2 
8941  N  N   . VAL   D 11  ? 1.5137 1.4015 1.5920 -0.1377 0.0441  0.0486  80   VAL   D N   
8942  C  CA  . VAL   D 11  ? 1.4771 1.3541 1.5526 -0.1356 0.0571  0.0543  80   VAL   D CA  
8943  C  C   . VAL   D 11  ? 1.4940 1.3526 1.5504 -0.1328 0.0593  0.0540  80   VAL   D C   
8944  O  O   . VAL   D 11  ? 1.5878 1.4392 1.6494 -0.1389 0.0582  0.0532  80   VAL   D O   
8945  C  CB  . VAL   D 11  ? 1.5040 1.3844 1.6039 -0.1439 0.0631  0.0578  80   VAL   D CB  
8946  C  CG1 . VAL   D 11  ? 1.5297 1.3985 1.6257 -0.1411 0.0776  0.0642  80   VAL   D CG1 
8947  C  CG2 . VAL   D 11  ? 1.4292 1.3286 1.5488 -0.1470 0.0591  0.0573  80   VAL   D CG2 
8948  N  N   . ILE   D 12  ? 1.5049 1.3557 1.5393 -0.1236 0.0620  0.0545  81   ILE   D N   
8949  C  CA  . ILE   D 12  ? 1.5475 1.3817 1.5611 -0.1194 0.0624  0.0534  81   ILE   D CA  
8950  C  C   . ILE   D 12  ? 1.5569 1.3768 1.5590 -0.1141 0.0750  0.0589  81   ILE   D C   
8951  O  O   . ILE   D 12  ? 1.5838 1.4070 1.5828 -0.1086 0.0802  0.0616  81   ILE   D O   
8952  C  CB  . ILE   D 12  ? 1.5900 1.4263 1.5860 -0.1124 0.0536  0.0487  81   ILE   D CB  
8953  C  CG1 . ILE   D 12  ? 1.5869 1.4371 1.5936 -0.1173 0.0416  0.0435  81   ILE   D CG1 
8954  C  CG2 . ILE   D 12  ? 1.5580 1.3768 1.5326 -0.1077 0.0543  0.0476  81   ILE   D CG2 
8955  C  CD1 . ILE   D 12  ? 1.6209 1.4656 1.6322 -0.1243 0.0361  0.0406  81   ILE   D CD1 
8956  N  N   . PRO   D 13  ? 1.5516 1.3550 1.5466 -0.1152 0.0804  0.0606  82   PRO   D N   
8957  C  CA  . PRO   D 13  ? 1.5743 1.3625 1.5564 -0.1096 0.0927  0.0659  82   PRO   D CA  
8958  C  C   . PRO   D 13  ? 1.5075 1.2887 1.4637 -0.0981 0.0917  0.0647  82   PRO   D C   
8959  O  O   . PRO   D 13  ? 1.4833 1.2647 1.4281 -0.0951 0.0827  0.0599  82   PRO   D O   
8960  C  CB  . PRO   D 13  ? 1.5889 1.3614 1.5698 -0.1143 0.0966  0.0670  82   PRO   D CB  
8961  C  CG  . PRO   D 13  ? 1.5334 1.3090 1.5138 -0.1177 0.0843  0.0609  82   PRO   D CG  
8962  C  CD  . PRO   D 13  ? 1.5689 1.3655 1.5656 -0.1212 0.0752  0.0577  82   PRO   D CD  
8963  N  N   . VAL   D 14  ? 1.5849 1.3593 1.5317 -0.0915 0.1013  0.0692  83   VAL   D N   
8964  C  CA  . VAL   D 14  ? 1.5648 1.3331 1.4880 -0.0801 0.1005  0.0683  83   VAL   D CA  
8965  C  C   . VAL   D 14  ? 1.5693 1.3154 1.4715 -0.0748 0.1069  0.0703  83   VAL   D C   
8966  O  O   . VAL   D 14  ? 1.6207 1.3553 1.5249 -0.0770 0.1176  0.0752  83   VAL   D O   
8967  C  CB  . VAL   D 14  ? 1.5738 1.3476 1.4973 -0.0748 0.1062  0.0716  83   VAL   D CB  
8968  C  CG1 . VAL   D 14  ? 1.4850 1.2579 1.3881 -0.0641 0.1012  0.0688  83   VAL   D CG1 
8969  C  CG2 . VAL   D 14  ? 1.6313 1.4250 1.5799 -0.0821 0.1035  0.0715  83   VAL   D CG2 
8970  N  N   . LEU   D 15  ? 1.5594 1.2992 1.4415 -0.0674 0.1007  0.0666  84   LEU   D N   
8971  C  CA  . LEU   D 15  ? 1.6648 1.3831 1.5243 -0.0605 0.1068  0.0685  84   LEU   D CA  
8972  C  C   . LEU   D 15  ? 1.7395 1.4499 1.5890 -0.0530 0.1172  0.0736  84   LEU   D C   
8973  O  O   . LEU   D 15  ? 1.7489 1.4686 1.5963 -0.0477 0.1147  0.0729  84   LEU   D O   
8974  C  CB  . LEU   D 15  ? 1.6151 1.3294 1.4554 -0.0533 0.0976  0.0633  84   LEU   D CB  
8975  N  N   . PRO   D 16  ? 1.8617 1.5548 1.7047 -0.0524 0.1290  0.0790  85   PRO   D N   
8976  C  CA  . PRO   D 16  ? 1.9082 1.5946 1.7457 -0.0469 0.1405  0.0847  85   PRO   D CA  
8977  C  C   . PRO   D 16  ? 1.9186 1.6030 1.7361 -0.0347 0.1384  0.0836  85   PRO   D C   
8978  O  O   . PRO   D 16  ? 1.9216 1.6183 1.7465 -0.0334 0.1380  0.0841  85   PRO   D O   
8979  C  CB  . PRO   D 16  ? 1.9089 1.5728 1.7357 -0.0465 0.1518  0.0894  85   PRO   D CB  
8980  C  CG  . PRO   D 16  ? 1.9168 1.5830 1.7587 -0.0572 0.1481  0.0874  85   PRO   D CG  
8981  C  CD  . PRO   D 16  ? 1.8514 1.5311 1.6948 -0.0580 0.1329  0.0802  85   PRO   D CD  
8982  N  N   . GLN   D 17  ? 1.9037 1.5724 1.6962 -0.0257 0.1371  0.0822  86   GLN   D N   
8983  C  CA  . GLN   D 17  ? 1.8697 1.5343 1.6422 -0.0135 0.1353  0.0813  86   GLN   D CA  
8984  C  C   . GLN   D 17  ? 1.9871 1.6630 1.7559 -0.0105 0.1207  0.0742  86   GLN   D C   
8985  O  O   . GLN   D 17  ? 1.9775 1.6433 1.7263 -0.0024 0.1163  0.0713  86   GLN   D O   
8986  C  CB  . GLN   D 17  ? 1.8526 1.4919 1.5990 -0.0044 0.1435  0.0845  86   GLN   D CB  
8987  N  N   . VAL   D 18  ? 2.0595 1.7571 1.8487 -0.0170 0.1135  0.0713  87   VAL   D N   
8988  C  CA  . VAL   D 18  ? 2.0486 1.7591 1.8375 -0.0149 0.1003  0.0649  87   VAL   D CA  
8989  C  C   . VAL   D 18  ? 2.0507 1.7655 1.8308 -0.0058 0.0981  0.0642  87   VAL   D C   
8990  O  O   . VAL   D 18  ? 2.0834 1.8020 1.8697 -0.0057 0.1042  0.0677  87   VAL   D O   
8991  C  CB  . VAL   D 18  ? 2.0326 1.7635 1.8465 -0.0258 0.0934  0.0622  87   VAL   D CB  
8992  C  CG1 . VAL   D 18  ? 2.0422 1.7687 1.8652 -0.0349 0.0950  0.0627  87   VAL   D CG1 
8993  C  CG2 . VAL   D 18  ? 2.0175 1.7623 1.8491 -0.0297 0.0969  0.0649  87   VAL   D CG2 
8994  N  N   . MET   D 19  ? 1.9413 1.6557 1.7077 0.0017  0.0893  0.0593  88   MET   D N   
8995  C  CA  . MET   D 19  ? 1.9317 1.6510 1.6905 0.0102  0.0855  0.0578  88   MET   D CA  
8996  C  C   . MET   D 19  ? 1.8675 1.5949 1.6223 0.0139  0.0728  0.0511  88   MET   D C   
8997  O  O   . MET   D 19  ? 1.9035 1.6248 1.6417 0.0241  0.0693  0.0491  88   MET   D O   
8998  C  CB  . MET   D 19  ? 1.9920 1.6914 1.7280 0.0208  0.0931  0.0612  88   MET   D CB  
8999  N  N   . MET   D 20  ? 1.7509 1.4919 1.5209 0.0060  0.0658  0.0477  89   MET   D N   
9000  C  CA  . MET   D 20  ? 1.6833 1.4304 1.4495 0.0090  0.0548  0.0416  89   MET   D CA  
9001  C  C   . MET   D 20  ? 1.6176 1.3868 1.4033 0.0027  0.0472  0.0384  89   MET   D C   
9002  O  O   . MET   D 20  ? 1.6235 1.4029 1.4269 -0.0058 0.0496  0.0405  89   MET   D O   
9003  C  CB  . MET   D 20  ? 1.7011 1.4385 1.4612 0.0071  0.0535  0.0400  89   MET   D CB  
9004  C  CG  . MET   D 20  ? 1.6957 1.4453 1.4631 0.0040  0.0429  0.0344  89   MET   D CG  
9005  S  SD  . MET   D 20  ? 1.8754 1.6113 1.6328 0.0032  0.0417  0.0325  89   MET   D SD  
9006  C  CE  . MET   D 20  ? 1.7694 1.5003 1.5076 0.0156  0.0340  0.0276  89   MET   D CE  
9007  N  N   . ILE   D 21  ? 1.5293 1.3056 1.3114 0.0074  0.0379  0.0334  90   ILE   D N   
9008  C  CA  . ILE   D 21  ? 1.4529 1.2481 1.2510 0.0017  0.0297  0.0296  90   ILE   D CA  
9009  C  C   . ILE   D 21  ? 1.3990 1.1918 1.1966 -0.0017 0.0257  0.0267  90   ILE   D C   
9010  O  O   . ILE   D 21  ? 1.4040 1.1902 1.1888 0.0046  0.0215  0.0236  90   ILE   D O   
9011  C  CB  . ILE   D 21  ? 1.4235 1.2279 1.2192 0.0085  0.0223  0.0258  90   ILE   D CB  
9012  C  CG1 . ILE   D 21  ? 1.3301 1.1419 1.1321 0.0090  0.0250  0.0283  90   ILE   D CG1 
9013  C  CG2 . ILE   D 21  ? 1.3505 1.1696 1.1569 0.0046  0.0132  0.0209  90   ILE   D CG2 
9014  C  CD1 . ILE   D 21  ? 1.4164 1.2139 1.2076 0.0134  0.0344  0.0332  90   ILE   D CD1 
9015  N  N   . LEU   D 22  ? 1.3640 1.1613 1.1751 -0.0114 0.0268  0.0276  91   LEU   D N   
9016  C  CA  . LEU   D 22  ? 1.3626 1.1569 1.1731 -0.0150 0.0233  0.0250  91   LEU   D CA  
9017  C  C   . LEU   D 22  ? 1.3084 1.1199 1.1319 -0.0193 0.0146  0.0208  91   LEU   D C   
9018  O  O   . LEU   D 22  ? 1.3117 1.1355 1.1515 -0.0265 0.0141  0.0216  91   LEU   D O   
9019  C  CB  . LEU   D 22  ? 1.3330 1.1193 1.1490 -0.0226 0.0299  0.0286  91   LEU   D CB  
9020  C  CG  . LEU   D 22  ? 1.2965 1.0829 1.1156 -0.0279 0.0250  0.0256  91   LEU   D CG  
9021  C  CD1 . LEU   D 22  ? 1.2949 1.0687 1.0950 -0.0200 0.0227  0.0231  91   LEU   D CD1 
9022  C  CD2 . LEU   D 22  ? 1.2731 1.0542 1.1014 -0.0367 0.0304  0.0288  91   LEU   D CD2 
9023  N  N   . ILE   D 23  ? 1.2608 1.0730 1.0769 -0.0148 0.0080  0.0164  92   ILE   D N   
9024  C  CA  . ILE   D 23  ? 1.2995 1.1271 1.1270 -0.0186 0.0005  0.0126  92   ILE   D CA  
9025  C  C   . ILE   D 23  ? 1.3289 1.1540 1.1604 -0.0255 -0.0010 0.0115  92   ILE   D C   
9026  O  O   . ILE   D 23  ? 1.2367 1.0475 1.0575 -0.0242 0.0014  0.0120  92   ILE   D O   
9027  C  CB  . ILE   D 23  ? 1.2628 1.0943 1.0829 -0.0106 -0.0060 0.0084  92   ILE   D CB  
9028  C  CG1 . ILE   D 23  ? 1.2446 1.0741 1.0572 -0.0027 -0.0044 0.0094  92   ILE   D CG1 
9029  C  CG2 . ILE   D 23  ? 1.2090 1.0580 1.0424 -0.0144 -0.0128 0.0050  92   ILE   D CG2 
9030  C  CD1 . ILE   D 23  ? 1.2176 1.0517 1.0246 0.0052  -0.0112 0.0050  92   ILE   D CD1 
9031  N  N   . PRO   D 24  ? 1.3063 1.1442 1.1524 -0.0328 -0.0050 0.0101  93   PRO   D N   
9032  C  CA  . PRO   D 24  ? 1.2116 1.0465 1.0608 -0.0391 -0.0069 0.0088  93   PRO   D CA  
9033  C  C   . PRO   D 24  ? 1.2601 1.0877 1.0962 -0.0339 -0.0108 0.0053  93   PRO   D C   
9034  O  O   . PRO   D 24  ? 1.2697 1.1035 1.1025 -0.0283 -0.0153 0.0022  93   PRO   D O   
9035  C  CB  . PRO   D 24  ? 1.1274 0.9787 0.9927 -0.0456 -0.0118 0.0072  93   PRO   D CB  
9036  C  CG  . PRO   D 24  ? 1.1730 1.0343 1.0454 -0.0443 -0.0104 0.0090  93   PRO   D CG  
9037  C  CD  . PRO   D 24  ? 1.2244 1.0795 1.0835 -0.0349 -0.0086 0.0092  93   PRO   D CD  
9038  N  N   . GLY   D 25  ? 1.2861 1.1004 1.1156 -0.0359 -0.0088 0.0057  94   GLY   D N   
9039  C  CA  . GLY   D 25  ? 1.2611 1.0666 1.0777 -0.0314 -0.0118 0.0026  94   GLY   D CA  
9040  C  C   . GLY   D 25  ? 1.2749 1.0656 1.0746 -0.0232 -0.0079 0.0038  94   GLY   D C   
9041  O  O   . GLY   D 25  ? 1.2712 1.0491 1.0597 -0.0213 -0.0076 0.0029  94   GLY   D O   
9042  N  N   . GLN   D 26  ? 1.2973 1.0891 1.0939 -0.0177 -0.0054 0.0055  95   GLN   D N   
9043  C  CA  . GLN   D 26  ? 1.2659 1.0422 1.0466 -0.0104 -0.0006 0.0074  95   GLN   D CA  
9044  C  C   . GLN   D 26  ? 1.2997 1.0615 1.0771 -0.0151 0.0055  0.0106  95   GLN   D C   
9045  O  O   . GLN   D 26  ? 1.2691 1.0351 1.0595 -0.0242 0.0070  0.0122  95   GLN   D O   
9046  C  CB  . GLN   D 26  ? 1.3330 1.1121 1.1135 -0.0061 0.0026  0.0099  95   GLN   D CB  
9047  C  CG  . GLN   D 26  ? 1.3687 1.1522 1.1420 0.0034  -0.0021 0.0070  95   GLN   D CG  
9048  C  CD  . GLN   D 26  ? 1.3694 1.1513 1.1391 0.0083  0.0018  0.0098  95   GLN   D CD  
9049  O  OE1 . GLN   D 26  ? 1.3668 1.1491 1.1434 0.0036  0.0076  0.0138  95   GLN   D OE1 
9050  N  NE2 . GLN   D 26  ? 1.3066 1.0865 1.0657 0.0180  -0.0014 0.0076  95   GLN   D NE2 
9051  N  N   . THR   D 27  ? 1.3654 1.1100 1.1261 -0.0092 0.0090  0.0116  96   THR   D N   
9052  C  CA  . THR   D 27  ? 1.3785 1.1080 1.1352 -0.0134 0.0151  0.0147  96   THR   D CA  
9053  C  C   . THR   D 27  ? 1.3469 1.0638 1.0943 -0.0092 0.0235  0.0193  96   THR   D C   
9054  O  O   . THR   D 27  ? 1.3570 1.0662 1.0891 0.0005  0.0238  0.0190  96   THR   D O   
9055  C  CB  . THR   D 27  ? 1.4444 1.1623 1.1890 -0.0111 0.0124  0.0120  96   THR   D CB  
9056  O  OG1 . THR   D 27  ? 1.4720 1.2025 1.2237 -0.0129 0.0044  0.0075  96   THR   D OG1 
9057  C  CG2 . THR   D 27  ? 1.4053 1.1105 1.1505 -0.0181 0.0176  0.0147  96   THR   D CG2 
9058  N  N   . LEU   D 28  ? 1.3409 1.0559 1.0977 -0.0164 0.0301  0.0235  97   LEU   D N   
9059  C  CA  . LEU   D 28  ? 1.3640 1.0679 1.1142 -0.0136 0.0393  0.0286  97   LEU   D CA  
9060  C  C   . LEU   D 28  ? 1.4249 1.1085 1.1637 -0.0140 0.0453  0.0309  97   LEU   D C   
9061  O  O   . LEU   D 28  ? 1.4042 1.0859 1.1530 -0.0229 0.0477  0.0323  97   LEU   D O   
9062  C  CB  . LEU   D 28  ? 1.3481 1.0625 1.1167 -0.0212 0.0437  0.0320  97   LEU   D CB  
9063  C  CG  . LEU   D 28  ? 1.4000 1.1029 1.1647 -0.0202 0.0547  0.0380  97   LEU   D CG  
9064  C  CD1 . LEU   D 28  ? 1.4532 1.1514 1.2022 -0.0089 0.0558  0.0384  97   LEU   D CD1 
9065  C  CD2 . LEU   D 28  ? 1.3978 1.1127 1.1837 -0.0290 0.0583  0.0410  97   LEU   D CD2 
9066  N  N   . PRO   D 29  ? 1.4652 1.1331 1.1831 -0.0045 0.0470  0.0310  98   PRO   D N   
9067  C  CA  . PRO   D 29  ? 1.3633 1.0103 1.0693 -0.0045 0.0538  0.0338  98   PRO   D CA  
9068  C  C   . PRO   D 29  ? 1.4221 1.0589 1.1260 -0.0045 0.0650  0.0400  98   PRO   D C   
9069  O  O   . PRO   D 29  ? 1.4669 1.1051 1.1661 0.0016  0.0674  0.0416  98   PRO   D O   
9070  C  CB  . PRO   D 29  ? 1.3850 1.0205 1.0689 0.0067  0.0501  0.0309  98   PRO   D CB  
9071  C  CG  . PRO   D 29  ? 1.4389 1.0913 1.1265 0.0109  0.0404  0.0259  98   PRO   D CG  
9072  C  CD  . PRO   D 29  ? 1.4794 1.1480 1.1837 0.0065  0.0414  0.0276  98   PRO   D CD  
9073  N  N   . LEU   D 30  ? 1.4952 1.1213 1.2026 -0.0114 0.0719  0.0435  99   LEU   D N   
9074  C  CA  . LEU   D 30  ? 1.5488 1.1637 1.2551 -0.0122 0.0838  0.0498  99   LEU   D CA  
9075  C  C   . LEU   D 30  ? 1.6142 1.2057 1.3057 -0.0111 0.0905  0.0524  99   LEU   D C   
9076  O  O   . LEU   D 30  ? 1.5718 1.1591 1.2637 -0.0153 0.0870  0.0500  99   LEU   D O   
9077  C  CB  . LEU   D 30  ? 1.4875 1.1152 1.2191 -0.0238 0.0873  0.0525  99   LEU   D CB  
9078  C  CG  . LEU   D 30  ? 1.4232 1.0748 1.1727 -0.0271 0.0807  0.0501  99   LEU   D CG  
9079  C  CD1 . LEU   D 30  ? 1.4550 1.1155 1.2268 -0.0371 0.0864  0.0538  99   LEU   D CD1 
9080  C  CD2 . LEU   D 30  ? 1.4625 1.1182 1.2021 -0.0172 0.0794  0.0496  99   LEU   D CD2 
9081  N  N   . GLN   D 31  ? 1.7165 1.2919 1.3937 -0.0049 0.1003  0.0572  100  GLN   D N   
9082  C  CA  . GLN   D 31  ? 1.7425 1.2951 1.4082 -0.0051 0.1097  0.0613  100  GLN   D CA  
9083  C  C   . GLN   D 31  ? 1.7585 1.3099 1.4366 -0.0111 0.1214  0.0677  100  GLN   D C   
9084  O  O   . GLN   D 31  ? 1.8071 1.3521 1.4761 -0.0046 0.1287  0.0715  100  GLN   D O   
9085  C  CB  . GLN   D 31  ? 1.6938 1.2266 1.3304 0.0080  0.1117  0.0616  100  GLN   D CB  
9086  N  N   . LEU   D 32  ? 1.7681 1.3263 1.4677 -0.0232 0.1229  0.0687  101  LEU   D N   
9087  C  CA  . LEU   D 32  ? 1.7770 1.3353 1.4914 -0.0299 0.1338  0.0746  101  LEU   D CA  
9088  C  C   . LEU   D 32  ? 1.8980 1.4314 1.5982 -0.0277 0.1460  0.0800  101  LEU   D C   
9089  O  O   . LEU   D 32  ? 2.0166 1.5352 1.7041 -0.0266 0.1450  0.0787  101  LEU   D O   
9090  C  CB  . LEU   D 32  ? 1.8141 1.3876 1.5569 -0.0436 0.1307  0.0735  101  LEU   D CB  
9091  C  CG  . LEU   D 32  ? 1.7667 1.3658 1.5294 -0.0477 0.1229  0.0706  101  LEU   D CG  
9092  C  CD1 . LEU   D 32  ? 1.7175 1.3246 1.4682 -0.0396 0.1116  0.0649  101  LEU   D CD1 
9093  C  CD2 . LEU   D 32  ? 1.7562 1.3676 1.5437 -0.0607 0.1181  0.0687  101  LEU   D CD2 
9094  N  N   . PHE   D 33  ? 1.9795 1.5075 1.6810 -0.0268 0.1578  0.0860  102  PHE   D N   
9095  C  CA  . PHE   D 33  ? 2.0308 1.5350 1.7201 -0.0253 0.1710  0.0920  102  PHE   D CA  
9096  C  C   . PHE   D 33  ? 2.0885 1.5941 1.7984 -0.0344 0.1830  0.0981  102  PHE   D C   
9097  O  O   . PHE   D 33  ? 2.1587 1.6469 1.8658 -0.0372 0.1932  0.1025  102  PHE   D O   
9098  C  CB  . PHE   D 33  ? 2.0459 1.5342 1.7068 -0.0110 0.1760  0.0942  102  PHE   D CB  
9099  C  CG  . PHE   D 33  ? 2.1323 1.6229 1.7967 -0.0086 0.1856  0.0993  102  PHE   D CG  
9100  C  CD1 . PHE   D 33  ? 2.1862 1.6629 1.8523 -0.0111 0.2010  0.1066  102  PHE   D CD1 
9101  C  CD2 . PHE   D 33  ? 2.1155 1.6225 1.7823 -0.0039 0.1794  0.0970  102  PHE   D CD2 
9102  C  CE1 . PHE   D 33  ? 2.2252 1.7039 1.8941 -0.0084 0.2103  0.1116  102  PHE   D CE1 
9103  C  CE2 . PHE   D 33  ? 2.0870 1.5960 1.7566 -0.0013 0.1882  0.1017  102  PHE   D CE2 
9104  C  CZ  . PHE   D 33  ? 2.1410 1.6360 1.8114 -0.0034 0.2036  0.1090  102  PHE   D CZ  
9105  N  N   . HIS   D 34  ? 2.0974 1.6229 1.8280 -0.0388 0.1824  0.0986  103  HIS   D N   
9106  C  CA  . HIS   D 34  ? 2.1569 1.6839 1.9055 -0.0453 0.1948  0.1049  103  HIS   D CA  
9107  C  C   . HIS   D 34  ? 2.1881 1.7280 1.9668 -0.0600 0.1921  0.1039  103  HIS   D C   
9108  O  O   . HIS   D 34  ? 2.1206 1.6782 1.9114 -0.0644 0.1793  0.0981  103  HIS   D O   
9109  C  CB  . HIS   D 34  ? 2.1524 1.6932 1.9055 -0.0410 0.1958  0.1061  103  HIS   D CB  
9110  C  CG  . HIS   D 34  ? 2.2123 1.7573 1.9855 -0.0474 0.2080  0.1123  103  HIS   D CG  
9111  N  ND1 . HIS   D 34  ? 2.2133 1.7646 2.0131 -0.0604 0.2111  0.1140  103  HIS   D ND1 
9112  C  CD2 . HIS   D 34  ? 2.2287 1.7729 1.9997 -0.0423 0.2176  0.1172  103  HIS   D CD2 
9113  C  CE1 . HIS   D 34  ? 2.2027 1.7572 2.0166 -0.0631 0.2224  0.1196  103  HIS   D CE1 
9114  N  NE2 . HIS   D 34  ? 2.2413 1.7915 2.0377 -0.0522 0.2268  0.1218  103  HIS   D NE2 
9115  N  N   . PRO   D 35  ? 2.4180 1.9491 2.2092 -0.0675 0.2039  0.1094  104  PRO   D N   
9116  C  CA  . PRO   D 35  ? 2.4152 1.9571 2.2352 -0.0815 0.2010  0.1082  104  PRO   D CA  
9117  C  C   . PRO   D 35  ? 2.3836 1.9521 2.2313 -0.0886 0.1947  0.1061  104  PRO   D C   
9118  O  O   . PRO   D 35  ? 2.3720 1.9539 2.2341 -0.0958 0.1829  0.1008  104  PRO   D O   
9119  C  CB  . PRO   D 35  ? 2.4302 1.9565 2.2565 -0.0862 0.2169  0.1153  104  PRO   D CB  
9120  C  CG  . PRO   D 35  ? 2.4860 1.9873 2.2794 -0.0745 0.2249  0.1184  104  PRO   D CG  
9121  C  CD  . PRO   D 35  ? 2.4470 1.9548 2.2225 -0.0626 0.2189  0.1160  104  PRO   D CD  
9122  N  N   . GLN   D 36  ? 2.1837 1.7599 2.0389 -0.0867 0.2020  0.1101  105  GLN   D N   
9123  C  CA  . GLN   D 36  ? 2.0835 1.6848 1.9649 -0.0930 0.1965  0.1085  105  GLN   D CA  
9124  C  C   . GLN   D 36  ? 2.0610 1.6777 1.9410 -0.0921 0.1795  0.1007  105  GLN   D C   
9125  O  O   . GLN   D 36  ? 2.0091 1.6438 1.9117 -0.1006 0.1711  0.0973  105  GLN   D O   
9126  C  CB  . GLN   D 36  ? 2.0207 1.6264 1.9017 -0.0872 0.2053  0.1130  105  GLN   D CB  
9127  N  N   . GLU   D 37  ? 2.0729 1.6818 1.9261 -0.0814 0.1746  0.0979  106  GLU   D N   
9128  C  CA  . GLU   D 37  ? 1.9900 1.6117 1.8397 -0.0795 0.1591  0.0907  106  GLU   D CA  
9129  C  C   . GLU   D 37  ? 1.9468 1.5668 1.8012 -0.0866 0.1509  0.0864  106  GLU   D C   
9130  O  O   . GLU   D 37  ? 1.8980 1.5346 1.7714 -0.0943 0.1415  0.0824  106  GLU   D O   
9131  C  CB  . GLU   D 37  ? 1.9519 1.5649 1.7723 -0.0660 0.1568  0.0891  106  GLU   D CB  
9132  N  N   . VAL   D 38  ? 1.9733 1.5725 1.8099 -0.0838 0.1543  0.0871  107  VAL   D N   
9133  C  CA  . VAL   D 38  ? 1.9327 1.5277 1.7712 -0.0897 0.1469  0.0831  107  VAL   D CA  
9134  C  C   . VAL   D 38  ? 1.8930 1.4981 1.7612 -0.1033 0.1460  0.0832  107  VAL   D C   
9135  O  O   . VAL   D 38  ? 1.8583 1.4695 1.7345 -0.1093 0.1357  0.0782  107  VAL   D O   
9136  C  CB  . VAL   D 38  ? 1.8883 1.4573 1.7049 -0.0853 0.1537  0.0854  107  VAL   D CB  
9137  C  CG1 . VAL   D 38  ? 2.0471 1.6027 1.8644 -0.0857 0.1699  0.0931  107  VAL   D CG1 
9138  C  CG2 . VAL   D 38  ? 1.8194 1.3832 1.6413 -0.0931 0.1479  0.0821  107  VAL   D CG2 
9139  N  N   . SER   D 39  ? 1.9118 1.5190 1.7969 -0.1083 0.1567  0.0887  108  SER   D N   
9140  C  CA  . SER   D 39  ? 1.8704 1.4893 1.7861 -0.1211 0.1553  0.0886  108  SER   D CA  
9141  C  C   . SER   D 39  ? 1.8527 1.4952 1.7829 -0.1242 0.1420  0.0831  108  SER   D C   
9142  O  O   . SER   D 39  ? 1.8209 1.4709 1.7661 -0.1325 0.1331  0.0791  108  SER   D O   
9143  C  CB  . SER   D 39  ? 1.9479 1.5669 1.8796 -0.1246 0.1693  0.0956  108  SER   D CB  
9144  O  OG  . SER   D 39  ? 1.9531 1.5512 1.8653 -0.1177 0.1826  0.1012  108  SER   D OG  
9145  N  N   . MET   D 40  ? 1.9533 1.6072 1.8788 -0.1173 0.1405  0.0829  109  MET   D N   
9146  C  CA  . MET   D 40  ? 1.9508 1.6264 1.8879 -0.1192 0.1282  0.0778  109  MET   D CA  
9147  C  C   . MET   D 40  ? 1.9293 1.6048 1.8543 -0.1175 0.1152  0.0711  109  MET   D C   
9148  O  O   . MET   D 40  ? 1.8908 1.5791 1.8298 -0.1239 0.1048  0.0666  109  MET   D O   
9149  C  CB  . MET   D 40  ? 1.9659 1.6512 1.8974 -0.1112 0.1299  0.0791  109  MET   D CB  
9150  C  CG  . MET   D 40  ? 2.0012 1.7097 1.9470 -0.1137 0.1189  0.0747  109  MET   D CG  
9151  S  SD  . MET   D 40  ? 2.0901 1.8077 2.0211 -0.1022 0.1162  0.0737  109  MET   D SD  
9152  C  CE  . MET   D 40  ? 1.9389 1.6421 1.8388 -0.0924 0.1105  0.0699  109  MET   D CE  
9153  N  N   . VAL   D 41  ? 1.8876 1.5480 1.7860 -0.1086 0.1158  0.0705  110  VAL   D N   
9154  C  CA  . VAL   D 41  ? 1.8011 1.4603 1.6861 -0.1056 0.1043  0.0644  110  VAL   D CA  
9155  C  C   . VAL   D 41  ? 1.7932 1.4489 1.6886 -0.1150 0.0993  0.0618  110  VAL   D C   
9156  O  O   . VAL   D 41  ? 1.7366 1.4041 1.6404 -0.1190 0.0880  0.0566  110  VAL   D O   
9157  C  CB  . VAL   D 41  ? 1.7947 1.4362 1.6500 -0.0944 0.1074  0.0649  110  VAL   D CB  
9158  C  CG1 . VAL   D 41  ? 1.7372 1.3810 1.5790 -0.0897 0.0954  0.0585  110  VAL   D CG1 
9159  C  CG2 . VAL   D 41  ? 1.7798 1.4211 1.6255 -0.0857 0.1148  0.0686  110  VAL   D CG2 
9160  N  N   . ARG   D 42  ? 1.8377 1.4763 1.7318 -0.1183 0.1076  0.0653  111  ARG   D N   
9161  C  CA  . ARG   D 42  ? 1.7838 1.4178 1.6890 -0.1278 0.1036  0.0632  111  ARG   D CA  
9162  C  C   . ARG   D 42  ? 1.7401 1.3937 1.6729 -0.1374 0.0965  0.0608  111  ARG   D C   
9163  O  O   . ARG   D 42  ? 1.7316 1.3928 1.6677 -0.1403 0.0846  0.0552  111  ARG   D O   
9164  C  CB  . ARG   D 42  ? 1.6453 1.2607 1.5514 -0.1314 0.1159  0.0686  111  ARG   D CB  
9165  N  N   . ASN   D 43  ? 1.7311 1.3936 1.6834 -0.1418 0.1036  0.0650  112  ASN   D N   
9166  C  CA  . ASN   D 43  ? 1.7133 1.3952 1.6925 -0.1503 0.0972  0.0630  112  ASN   D CA  
9167  C  C   . ASN   D 43  ? 1.7288 1.4260 1.7051 -0.1475 0.0837  0.0570  112  ASN   D C   
9168  O  O   . ASN   D 43  ? 1.7343 1.4422 1.7261 -0.1546 0.0742  0.0530  112  ASN   D O   
9169  C  CB  . ASN   D 43  ? 1.7038 1.3947 1.6993 -0.1518 0.1068  0.0684  112  ASN   D CB  
9170  C  CG  . ASN   D 43  ? 1.7136 1.4239 1.7389 -0.1611 0.1011  0.0668  112  ASN   D CG  
9171  O  OD1 . ASN   D 43  ? 1.7192 1.4394 1.7499 -0.1643 0.0884  0.0611  112  ASN   D OD1 
9172  N  ND2 . ASN   D 43  ? 1.7184 1.4337 1.7628 -0.1653 0.1106  0.0718  112  ASN   D ND2 
9173  N  N   . LEU   D 44  ? 1.7398 1.4376 1.6960 -0.1372 0.0828  0.0562  113  LEU   D N   
9174  C  CA  . LEU   D 44  ? 1.7089 1.4222 1.6632 -0.1341 0.0716  0.0512  113  LEU   D CA  
9175  C  C   . LEU   D 44  ? 1.7405 1.4501 1.6856 -0.1345 0.0606  0.0453  113  LEU   D C   
9176  O  O   . LEU   D 44  ? 1.7310 1.4537 1.6859 -0.1381 0.0503  0.0409  113  LEU   D O   
9177  C  CB  . LEU   D 44  ? 1.6805 1.3952 1.6172 -0.1229 0.0743  0.0523  113  LEU   D CB  
9178  C  CG  . LEU   D 44  ? 1.5913 1.3240 1.5394 -0.1217 0.0747  0.0535  113  LEU   D CG  
9179  C  CD1 . LEU   D 44  ? 1.5416 1.2742 1.4700 -0.1103 0.0756  0.0536  113  LEU   D CD1 
9180  C  CD2 . LEU   D 44  ? 1.5782 1.3293 1.5435 -0.1278 0.0635  0.0490  113  LEU   D CD2 
9181  N  N   . ILE   D 45  ? 1.7040 1.3955 1.6296 -0.1305 0.0625  0.0451  114  ILE   D N   
9182  C  CA  . ILE   D 45  ? 1.6673 1.3541 1.5831 -0.1304 0.0526  0.0396  114  ILE   D CA  
9183  C  C   . ILE   D 45  ? 1.6612 1.3534 1.5968 -0.1412 0.0457  0.0368  114  ILE   D C   
9184  O  O   . ILE   D 45  ? 1.6520 1.3497 1.5866 -0.1422 0.0348  0.0315  114  ILE   D O   
9185  C  CB  . ILE   D 45  ? 1.5952 1.2599 1.4891 -0.1255 0.0571  0.0405  114  ILE   D CB  
9186  C  CG1 . ILE   D 45  ? 1.6095 1.2711 1.4802 -0.1135 0.0575  0.0399  114  ILE   D CG1 
9187  C  CG2 . ILE   D 45  ? 1.6239 1.2820 1.5141 -0.1290 0.0485  0.0357  114  ILE   D CG2 
9188  C  CD1 . ILE   D 45  ? 1.5448 1.2115 1.4053 -0.1095 0.0460  0.0337  114  ILE   D CD1 
9189  N  N   . GLN   D 46  ? 1.7112 1.4017 1.6652 -0.1493 0.0518  0.0403  115  GLN   D N   
9190  C  CA  . GLN   D 46  ? 1.6843 1.3798 1.6597 -0.1601 0.0457  0.0381  115  GLN   D CA  
9191  C  C   . GLN   D 46  ? 1.7802 1.4973 1.7729 -0.1632 0.0377  0.0354  115  GLN   D C   
9192  O  O   . GLN   D 46  ? 1.7462 1.4688 1.7553 -0.1713 0.0303  0.0325  115  GLN   D O   
9193  C  CB  . GLN   D 46  ? 1.6942 1.3826 1.6857 -0.1674 0.0556  0.0430  115  GLN   D CB  
9194  N  N   . LYS   D 47  ? 1.8468 1.5758 1.8357 -0.1569 0.0386  0.0362  116  LYS   D N   
9195  C  CA  . LYS   D 47  ? 1.8422 1.5913 1.8454 -0.1589 0.0310  0.0337  116  LYS   D CA  
9196  C  C   . LYS   D 47  ? 1.8495 1.6051 1.8361 -0.1507 0.0238  0.0299  116  LYS   D C   
9197  O  O   . LYS   D 47  ? 1.8862 1.6339 1.8570 -0.1476 0.0180  0.0262  116  LYS   D O   
9198  C  CB  . LYS   D 47  ? 1.8242 1.5840 1.8445 -0.1608 0.0388  0.0385  116  LYS   D CB  
9199  N  N   . ASP   D 48  ? 1.8776 1.6480 1.8687 -0.1474 0.0243  0.0309  117  ASP   D N   
9200  C  CA  . ASP   D 48  ? 1.8447 1.6232 1.8234 -0.1405 0.0173  0.0273  117  ASP   D CA  
9201  C  C   . ASP   D 48  ? 1.9047 1.6724 1.8589 -0.1305 0.0212  0.0278  117  ASP   D C   
9202  O  O   . ASP   D 48  ? 1.9062 1.6778 1.8483 -0.1247 0.0149  0.0243  117  ASP   D O   
9203  C  CB  . ASP   D 48  ? 1.8044 1.6012 1.7950 -0.1398 0.0167  0.0281  117  ASP   D CB  
9204  C  CG  . ASP   D 48  ? 1.8988 1.6950 1.8888 -0.1358 0.0278  0.0336  117  ASP   D CG  
9205  O  OD1 . ASP   D 48  ? 1.9680 1.7537 1.9389 -0.1280 0.0329  0.0351  117  ASP   D OD1 
9206  O  OD2 . ASP   D 48  ? 1.9712 1.7767 1.9797 -0.1403 0.0316  0.0365  117  ASP   D OD2 
9207  N  N   . ARG   D 49  ? 1.8126 1.5669 1.7595 -0.1282 0.0314  0.0323  118  ARG   D N   
9208  C  CA  . ARG   D 49  ? 1.6673 1.4094 1.5905 -0.1184 0.0358  0.0332  118  ARG   D CA  
9209  C  C   . ARG   D 49  ? 1.6180 1.3701 1.5346 -0.1103 0.0364  0.0337  118  ARG   D C   
9210  O  O   . ARG   D 49  ? 1.5839 1.3325 1.4825 -0.1021 0.0338  0.0315  118  ARG   D O   
9211  C  CB  . ARG   D 49  ? 1.6000 1.3320 1.5068 -0.1157 0.0292  0.0288  118  ARG   D CB  
9212  N  N   . THR   D 50  ? 1.6187 1.3833 1.5501 -0.1123 0.0397  0.0364  119  THR   D N   
9213  C  CA  . THR   D 50  ? 1.5120 1.2874 1.4393 -0.1054 0.0394  0.0365  119  THR   D CA  
9214  C  C   . THR   D 50  ? 1.5190 1.2945 1.4515 -0.1042 0.0498  0.0422  119  THR   D C   
9215  O  O   . THR   D 50  ? 1.5555 1.3355 1.5065 -0.1114 0.0538  0.0450  119  THR   D O   
9216  C  CB  . THR   D 50  ? 1.4931 1.2877 1.4337 -0.1085 0.0301  0.0329  119  THR   D CB  
9217  O  OG1 . THR   D 50  ? 1.5301 1.3244 1.4664 -0.1099 0.0207  0.0278  119  THR   D OG1 
9218  C  CG2 . THR   D 50  ? 1.3617 1.1664 1.2965 -0.1010 0.0293  0.0327  119  THR   D CG2 
9219  N  N   . PHE   D 51  ? 1.4363 1.2070 1.3526 -0.0948 0.0541  0.0438  120  PHE   D N   
9220  C  CA  . PHE   D 51  ? 1.4039 1.1764 1.3232 -0.0920 0.0628  0.0486  120  PHE   D CA  
9221  C  C   . PHE   D 51  ? 1.3871 1.1727 1.3030 -0.0857 0.0582  0.0467  120  PHE   D C   
9222  O  O   . PHE   D 51  ? 1.3575 1.1523 1.2725 -0.0849 0.0485  0.0419  120  PHE   D O   
9223  C  CB  . PHE   D 51  ? 1.3977 1.1508 1.3000 -0.0863 0.0730  0.0527  120  PHE   D CB  
9224  C  CG  . PHE   D 51  ? 1.3672 1.1096 1.2457 -0.0773 0.0698  0.0500  120  PHE   D CG  
9225  C  CD1 . PHE   D 51  ? 1.4022 1.1490 1.2687 -0.0683 0.0670  0.0486  120  PHE   D CD1 
9226  C  CD2 . PHE   D 51  ? 1.3478 1.0761 1.2162 -0.0780 0.0689  0.0487  120  PHE   D CD2 
9227  C  CE1 . PHE   D 51  ? 1.4165 1.1539 1.2621 -0.0599 0.0636  0.0458  120  PHE   D CE1 
9228  C  CE2 . PHE   D 51  ? 1.2999 1.0186 1.1466 -0.0695 0.0657  0.0461  120  PHE   D CE2 
9229  C  CZ  . PHE   D 51  ? 1.3141 1.0376 1.1498 -0.0605 0.0630  0.0447  120  PHE   D CZ  
9230  N  N   . ALA   D 52  ? 1.4492 1.2348 1.3629 -0.0810 0.0655  0.0506  121  ALA   D N   
9231  C  CA  . ALA   D 52  ? 1.3928 1.1897 1.3035 -0.0749 0.0621  0.0493  121  ALA   D CA  
9232  C  C   . ALA   D 52  ? 1.4332 1.2177 1.3218 -0.0639 0.0669  0.0509  121  ALA   D C   
9233  O  O   . ALA   D 52  ? 1.4599 1.2307 1.3416 -0.0618 0.0768  0.0555  121  ALA   D O   
9234  C  CB  . ALA   D 52  ? 1.2674 1.0780 1.1973 -0.0792 0.0652  0.0520  121  ALA   D CB  
9235  N  N   . VAL   D 53  ? 1.3858 1.1746 1.2633 -0.0569 0.0598  0.0471  122  VAL   D N   
9236  C  CA  . VAL   D 53  ? 1.4902 1.2695 1.3476 -0.0459 0.0625  0.0478  122  VAL   D CA  
9237  C  C   . VAL   D 53  ? 1.5175 1.3096 1.3800 -0.0427 0.0615  0.0481  122  VAL   D C   
9238  O  O   . VAL   D 53  ? 1.3954 1.2037 1.2686 -0.0452 0.0537  0.0448  122  VAL   D O   
9239  C  CB  . VAL   D 53  ? 1.4944 1.2681 1.3350 -0.0395 0.0553  0.0432  122  VAL   D CB  
9240  C  CG1 . VAL   D 53  ? 1.5169 1.2777 1.3360 -0.0280 0.0589  0.0444  122  VAL   D CG1 
9241  C  CG2 . VAL   D 53  ? 1.3900 1.1539 1.2284 -0.0439 0.0546  0.0421  122  VAL   D CG2 
9242  N  N   . LEU   D 54  ? 1.6187 1.4028 1.4727 -0.0368 0.0695  0.0521  123  LEU   D N   
9243  C  CA  . LEU   D 54  ? 1.5723 1.3669 1.4316 -0.0342 0.0703  0.0533  123  LEU   D CA  
9244  C  C   . LEU   D 54  ? 1.6346 1.4237 1.4742 -0.0227 0.0678  0.0516  123  LEU   D C   
9245  O  O   . LEU   D 54  ? 1.6449 1.4170 1.4654 -0.0156 0.0716  0.0527  123  LEU   D O   
9246  C  CB  . LEU   D 54  ? 1.5443 1.3349 1.4110 -0.0369 0.0819  0.0595  123  LEU   D CB  
9247  C  CG  . LEU   D 54  ? 1.4865 1.2881 1.3778 -0.0486 0.0828  0.0607  123  LEU   D CG  
9248  C  CD1 . LEU   D 54  ? 1.4589 1.2564 1.3582 -0.0509 0.0948  0.0670  123  LEU   D CD1 
9249  C  CD2 . LEU   D 54  ? 1.4406 1.2629 1.3469 -0.0522 0.0737  0.0571  123  LEU   D CD2 
9250  N  N   . ALA   D 55  ? 1.6285 1.4320 1.4731 -0.0207 0.0610  0.0487  124  ALA   D N   
9251  C  CA  . ALA   D 55  ? 1.6962 1.4971 1.5258 -0.0103 0.0586  0.0474  124  ALA   D CA  
9252  C  C   . ALA   D 55  ? 1.7975 1.6003 1.6301 -0.0083 0.0653  0.0515  124  ALA   D C   
9253  O  O   . ALA   D 55  ? 1.8420 1.6559 1.6928 -0.0156 0.0678  0.0535  124  ALA   D O   
9254  C  CB  . ALA   D 55  ? 1.5276 1.3429 1.3610 -0.0094 0.0469  0.0416  124  ALA   D CB  
9255  N  N   . TYR   D 56  ? 1.8066 1.5981 1.6211 0.0018  0.0681  0.0526  125  TYR   D N   
9256  C  CA  . TYR   D 56  ? 1.9593 1.7526 1.7751 0.0048  0.0737  0.0560  125  TYR   D CA  
9257  C  C   . TYR   D 56  ? 1.9785 1.7760 1.7852 0.0134  0.0668  0.0527  125  TYR   D C   
9258  O  O   . TYR   D 56  ? 2.0315 1.8347 1.8421 0.0151  0.0688  0.0544  125  TYR   D O   
9259  C  CB  . TYR   D 56  ? 2.0110 1.7855 1.8142 0.0090  0.0860  0.0618  125  TYR   D CB  
9260  C  CG  . TYR   D 56  ? 2.0520 1.8194 1.8410 0.0190  0.0894  0.0637  125  TYR   D CG  
9261  C  CD1 . TYR   D 56  ? 2.0580 1.8099 1.8226 0.0301  0.0880  0.0623  125  TYR   D CD1 
9262  C  CD2 . TYR   D 56  ? 2.0508 1.8265 1.8502 0.0176  0.0940  0.0667  125  TYR   D CD2 
9263  C  CE1 . TYR   D 56  ? 2.0172 1.7615 1.7675 0.0397  0.0907  0.0638  125  TYR   D CE1 
9264  C  CE2 . TYR   D 56  ? 2.0779 1.8462 1.8632 0.0271  0.0972  0.0684  125  TYR   D CE2 
9265  C  CZ  . TYR   D 56  ? 2.0664 1.8186 1.8268 0.0382  0.0954  0.0668  125  TYR   D CZ  
9266  O  OH  . TYR   D 56  ? 2.0769 1.8205 1.8219 0.0481  0.0979  0.0682  125  TYR   D OH  
9267  N  N   . ALA   D 64  ? 2.0909 1.9084 1.9429 -0.0052 0.0843  0.0634  133  ALA   D N   
9268  C  CA  . ALA   D 64  ? 2.1116 1.9490 1.9809 -0.0116 0.0746  0.0593  133  ALA   D CA  
9269  C  C   . ALA   D 64  ? 2.0944 1.9394 1.9830 -0.0232 0.0745  0.0595  133  ALA   D C   
9270  O  O   . ALA   D 64  ? 2.0788 1.9141 1.9686 -0.0267 0.0821  0.0630  133  ALA   D O   
9271  C  CB  . ALA   D 64  ? 2.1125 1.9521 1.9717 -0.0068 0.0635  0.0533  133  ALA   D CB  
9272  N  N   . GLN   D 65  ? 1.8971 1.7589 1.8004 -0.0290 0.0656  0.0557  134  GLN   D N   
9273  C  CA  . GLN   D 65  ? 1.6548 1.5267 1.5789 -0.0399 0.0649  0.0560  134  GLN   D CA  
9274  C  C   . GLN   D 65  ? 1.5772 1.4568 1.5053 -0.0440 0.0542  0.0505  134  GLN   D C   
9275  O  O   . GLN   D 65  ? 1.5366 1.4308 1.4812 -0.0506 0.0490  0.0488  134  GLN   D O   
9276  C  CB  . GLN   D 65  ? 1.6214 1.5076 1.5634 -0.0440 0.0664  0.0579  134  GLN   D CB  
9277  C  CG  . GLN   D 65  ? 1.6675 1.5668 1.6107 -0.0408 0.0584  0.0545  134  GLN   D CG  
9278  C  CD  . GLN   D 65  ? 1.7271 1.6210 1.6572 -0.0314 0.0622  0.0563  134  GLN   D CD  
9279  O  OE1 . GLN   D 65  ? 1.7889 1.6697 1.6995 -0.0234 0.0631  0.0559  134  GLN   D OE1 
9280  N  NE2 . GLN   D 65  ? 1.6565 1.5603 1.5969 -0.0321 0.0640  0.0582  134  GLN   D NE2 
9281  N  N   . PHE   D 66  ? 1.5738 1.4435 1.4867 -0.0399 0.0509  0.0479  135  PHE   D N   
9282  C  CA  . PHE   D 66  ? 1.4776 1.3521 1.3939 -0.0443 0.0425  0.0434  135  PHE   D CA  
9283  C  C   . PHE   D 66  ? 1.4693 1.3277 1.3728 -0.0430 0.0448  0.0434  135  PHE   D C   
9284  O  O   . PHE   D 66  ? 1.5441 1.3880 1.4361 -0.0387 0.0527  0.0469  135  PHE   D O   
9285  C  CB  . PHE   D 66  ? 1.4242 1.3075 1.3361 -0.0400 0.0329  0.0384  135  PHE   D CB  
9286  C  CG  . PHE   D 66  ? 1.5190 1.4179 1.4427 -0.0411 0.0299  0.0380  135  PHE   D CG  
9287  C  CD1 . PHE   D 66  ? 1.4876 1.4008 1.4287 -0.0490 0.0250  0.0364  135  PHE   D CD1 
9288  C  CD2 . PHE   D 66  ? 1.5204 1.4192 1.4371 -0.0339 0.0317  0.0390  135  PHE   D CD2 
9289  C  CE1 . PHE   D 66  ? 1.3829 1.3100 1.3341 -0.0497 0.0222  0.0360  135  PHE   D CE1 
9290  C  CE2 . PHE   D 66  ? 1.4463 1.3589 1.3733 -0.0348 0.0289  0.0386  135  PHE   D CE2 
9291  C  CZ  . PHE   D 66  ? 1.4110 1.3378 1.3554 -0.0428 0.0243  0.0371  135  PHE   D CZ  
9292  N  N   . GLY   D 67  ? 1.4335 1.2936 1.3379 -0.0463 0.0379  0.0395  136  GLY   D N   
9293  C  CA  . GLY   D 67  ? 1.4378 1.2830 1.3304 -0.0453 0.0395  0.0392  136  GLY   D CA  
9294  C  C   . GLY   D 67  ? 1.3291 1.1789 1.2273 -0.0510 0.0319  0.0352  136  GLY   D C   
9295  O  O   . GLY   D 67  ? 1.2305 1.0949 1.1404 -0.0549 0.0252  0.0325  136  GLY   D O   
9296  N  N   . THR   D 68  ? 1.2998 1.1362 1.1886 -0.0510 0.0332  0.0349  137  THR   D N   
9297  C  CA  . THR   D 68  ? 1.2513 1.0890 1.1426 -0.0556 0.0266  0.0312  137  THR   D CA  
9298  C  C   . THR   D 68  ? 1.2938 1.1200 1.1873 -0.0615 0.0315  0.0334  137  THR   D C   
9299  O  O   . THR   D 68  ? 1.3378 1.1502 1.2225 -0.0588 0.0395  0.0370  137  THR   D O   
9300  C  CB  . THR   D 68  ? 1.2291 1.0616 1.1040 -0.0484 0.0211  0.0272  137  THR   D CB  
9301  O  OG1 . THR   D 68  ? 1.2971 1.1381 1.1687 -0.0419 0.0176  0.0255  137  THR   D OG1 
9302  C  CG2 . THR   D 68  ? 1.2223 1.0590 1.1015 -0.0531 0.0137  0.0231  137  THR   D CG2 
9303  N  N   . THR   D 69  ? 1.3092 1.1408 1.2142 -0.0693 0.0266  0.0313  138  THR   D N   
9304  C  CA  . THR   D 69  ? 1.2418 1.0621 1.1483 -0.0750 0.0297  0.0325  138  THR   D CA  
9305  C  C   . THR   D 69  ? 1.2163 1.0232 1.1045 -0.0701 0.0276  0.0301  138  THR   D C   
9306  O  O   . THR   D 69  ? 1.1630 0.9734 1.0428 -0.0652 0.0210  0.0262  138  THR   D O   
9307  C  CB  . THR   D 69  ? 1.2363 1.0656 1.1604 -0.0848 0.0244  0.0307  138  THR   D CB  
9308  O  OG1 . THR   D 69  ? 1.2165 1.0539 1.1387 -0.0840 0.0147  0.0256  138  THR   D OG1 
9309  C  CG2 . THR   D 69  ? 1.2517 1.0935 1.1953 -0.0902 0.0270  0.0334  138  THR   D CG2 
9310  N  N   . ALA   D 70  ? 1.2842 1.0754 1.1667 -0.0716 0.0334  0.0325  139  ALA   D N   
9311  C  CA  . ALA   D 70  ? 1.2869 1.0640 1.1526 -0.0677 0.0319  0.0304  139  ALA   D CA  
9312  C  C   . ALA   D 70  ? 1.2989 1.0677 1.1701 -0.0756 0.0325  0.0306  139  ALA   D C   
9313  O  O   . ALA   D 70  ? 1.3306 1.0941 1.2101 -0.0808 0.0395  0.0346  139  ALA   D O   
9314  C  CB  . ALA   D 70  ? 1.2817 1.0438 1.1288 -0.0590 0.0389  0.0331  139  ALA   D CB  
9315  N  N   . GLU   D 71  ? 1.2903 1.0572 1.1563 -0.0762 0.0252  0.0263  140  GLU   D N   
9316  C  CA  . GLU   D 71  ? 1.3498 1.1082 1.2193 -0.0832 0.0241  0.0255  140  GLU   D CA  
9317  C  C   . GLU   D 71  ? 1.3088 1.0471 1.1599 -0.0787 0.0282  0.0263  140  GLU   D C   
9318  O  O   . GLU   D 71  ? 1.3334 1.0668 1.1679 -0.0708 0.0254  0.0239  140  GLU   D O   
9319  C  CB  . GLU   D 71  ? 1.3187 1.0857 1.1925 -0.0863 0.0137  0.0202  140  GLU   D CB  
9320  C  CG  . GLU   D 71  ? 1.3066 1.0668 1.1864 -0.0944 0.0112  0.0190  140  GLU   D CG  
9321  C  CD  . GLU   D 71  ? 1.3001 1.0677 1.1811 -0.0960 0.0009  0.0137  140  GLU   D CD  
9322  O  OE1 . GLU   D 71  ? 1.1026 0.8816 0.9817 -0.0914 -0.0033 0.0115  140  GLU   D OE1 
9323  O  OE2 . GLU   D 71  ? 1.4240 1.1855 1.3073 -0.1015 -0.0027 0.0117  140  GLU   D OE2 
9324  N  N   . ILE   D 72  ? 1.3607 1.0874 1.2153 -0.0838 0.0349  0.0297  141  ILE   D N   
9325  C  CA  . ILE   D 72  ? 1.3470 1.0538 1.1847 -0.0805 0.0384  0.0302  141  ILE   D CA  
9326  C  C   . ILE   D 72  ? 1.3476 1.0520 1.1803 -0.0819 0.0297  0.0252  141  ILE   D C   
9327  O  O   . ILE   D 72  ? 1.3965 1.1081 1.2430 -0.0897 0.0243  0.0230  141  ILE   D O   
9328  C  CB  . ILE   D 72  ? 1.3341 1.0288 1.1776 -0.0864 0.0476  0.0350  141  ILE   D CB  
9329  C  CG1 . ILE   D 72  ? 1.3000 0.9988 1.1512 -0.0859 0.0563  0.0401  141  ILE   D CG1 
9330  C  CG2 . ILE   D 72  ? 1.3839 1.0575 1.2075 -0.0813 0.0522  0.0361  141  ILE   D CG2 
9331  C  CD1 . ILE   D 72  ? 1.3930 1.1072 1.2700 -0.0955 0.0555  0.0411  141  ILE   D CD1 
9332  N  N   . TYR   D 73  ? 1.2967 0.9910 1.1096 -0.0738 0.0282  0.0232  142  TYR   D N   
9333  C  CA  . TYR   D 73  ? 1.3603 1.0500 1.1662 -0.0741 0.0210  0.0187  142  TYR   D CA  
9334  C  C   . TYR   D 73  ? 1.3404 1.0093 1.1271 -0.0693 0.0245  0.0192  142  TYR   D C   
9335  O  O   . TYR   D 73  ? 1.4129 1.0757 1.1919 -0.0690 0.0192  0.0157  142  TYR   D O   
9336  C  CB  . TYR   D 73  ? 1.3690 1.0715 1.1713 -0.0687 0.0128  0.0142  142  TYR   D CB  
9337  C  CG  . TYR   D 73  ? 1.4122 1.1104 1.1968 -0.0574 0.0137  0.0137  142  TYR   D CG  
9338  C  CD1 . TYR   D 73  ? 1.3744 1.0795 1.1592 -0.0524 0.0169  0.0158  142  TYR   D CD1 
9339  C  CD2 . TYR   D 73  ? 1.4800 1.1667 1.2475 -0.0514 0.0111  0.0110  142  TYR   D CD2 
9340  C  CE1 . TYR   D 73  ? 1.4220 1.1228 1.1909 -0.0420 0.0172  0.0151  142  TYR   D CE1 
9341  C  CE2 . TYR   D 73  ? 1.5385 1.2212 1.2903 -0.0408 0.0116  0.0103  142  TYR   D CE2 
9342  C  CZ  . TYR   D 73  ? 1.4214 1.1114 1.1743 -0.0362 0.0144  0.0124  142  TYR   D CZ  
9343  O  OH  . TYR   D 73  ? 1.4775 1.1640 1.2159 -0.0257 0.0143  0.0116  142  TYR   D OH  
9344  N  N   . ALA   D 74  ? 1.3460 1.0034 1.1240 -0.0653 0.0333  0.0235  143  ALA   D N   
9345  C  CA  . ALA   D 74  ? 1.4319 1.0679 1.1923 -0.0614 0.0379  0.0248  143  ALA   D CA  
9346  C  C   . ALA   D 74  ? 1.4764 1.1018 1.2387 -0.0637 0.0490  0.0308  143  ALA   D C   
9347  O  O   . ALA   D 74  ? 1.4257 1.0584 1.1942 -0.0626 0.0537  0.0339  143  ALA   D O   
9348  C  CB  . ALA   D 74  ? 1.3931 1.0235 1.1322 -0.0493 0.0361  0.0228  143  ALA   D CB  
9349  N  N   . TYR   D 75  ? 1.5377 1.1456 1.2947 -0.0667 0.0534  0.0325  144  TYR   D N   
9350  C  CA  . TYR   D 75  ? 1.4446 1.0410 1.2039 -0.0695 0.0646  0.0384  144  TYR   D CA  
9351  C  C   . TYR   D 75  ? 1.4599 1.0328 1.2015 -0.0670 0.0686  0.0393  144  TYR   D C   
9352  O  O   . TYR   D 75  ? 1.5126 1.0805 1.2515 -0.0696 0.0628  0.0359  144  TYR   D O   
9353  C  CB  . TYR   D 75  ? 1.4422 1.0476 1.2269 -0.0818 0.0659  0.0400  144  TYR   D CB  
9354  C  CG  . TYR   D 75  ? 1.5238 1.1178 1.3139 -0.0860 0.0778  0.0462  144  TYR   D CG  
9355  C  CD1 . TYR   D 75  ? 1.5240 1.0997 1.3101 -0.0899 0.0821  0.0477  144  TYR   D CD1 
9356  C  CD2 . TYR   D 75  ? 1.5910 1.1925 1.3907 -0.0861 0.0851  0.0506  144  TYR   D CD2 
9357  C  CE1 . TYR   D 75  ? 1.5440 1.1092 1.3359 -0.0940 0.0938  0.0536  144  TYR   D CE1 
9358  C  CE2 . TYR   D 75  ? 1.6466 1.2376 1.4518 -0.0898 0.0968  0.0565  144  TYR   D CE2 
9359  C  CZ  . TYR   D 75  ? 1.5913 1.1644 1.3929 -0.0938 0.1013  0.0580  144  TYR   D CZ  
9360  O  OH  . TYR   D 75  ? 1.6624 1.2254 1.4704 -0.0976 0.1136  0.0642  144  TYR   D OH  
9361  N  N   . ARG   D 76  ? 1.5910 1.1490 1.3193 -0.0613 0.0784  0.0439  145  ARG   D N   
9362  C  CA  . ARG   D 76  ? 1.6091 1.1434 1.3202 -0.0588 0.0836  0.0456  145  ARG   D CA  
9363  C  C   . ARG   D 76  ? 1.6775 1.1986 1.3845 -0.0574 0.0968  0.0523  145  ARG   D C   
9364  O  O   . ARG   D 76  ? 1.6731 1.1955 1.3722 -0.0498 0.1008  0.0545  145  ARG   D O   
9365  C  CB  . ARG   D 76  ? 1.5587 1.0842 1.2452 -0.0474 0.0786  0.0421  145  ARG   D CB  
9366  N  N   . GLU   D 77  ? 1.7113 1.2187 1.4228 -0.0645 0.1035  0.0554  146  GLU   D N   
9367  C  CA  . GLU   D 77  ? 1.7762 1.2666 1.4804 -0.0626 0.1169  0.0620  146  GLU   D CA  
9368  C  C   . GLU   D 77  ? 1.8789 1.3463 1.5541 -0.0529 0.1195  0.0622  146  GLU   D C   
9369  O  O   . GLU   D 77  ? 1.8378 1.2985 1.5041 -0.0522 0.1128  0.0582  146  GLU   D O   
9370  C  CB  . GLU   D 77  ? 1.7584 1.2443 1.4817 -0.0750 0.1234  0.0654  146  GLU   D CB  
9371  C  CG  . GLU   D 77  ? 1.6713 1.1788 1.4233 -0.0860 0.1169  0.0630  146  GLU   D CG  
9372  C  CD  . GLU   D 77  ? 1.7058 1.2144 1.4796 -0.0955 0.1266  0.0684  146  GLU   D CD  
9373  O  OE1 . GLU   D 77  ? 1.8715 1.3640 1.6376 -0.0934 0.1390  0.0741  146  GLU   D OE1 
9374  O  OE2 . GLU   D 77  ? 1.6241 1.1494 1.4228 -0.1050 0.1220  0.0669  146  GLU   D OE2 
9375  N  N   . GLU   D 78  ? 1.9942 1.4491 1.6541 -0.0448 0.1291  0.0669  147  GLU   D N   
9376  C  CA  . GLU   D 78  ? 2.1343 1.5670 1.7655 -0.0345 0.1314  0.0672  147  GLU   D CA  
9377  C  C   . GLU   D 78  ? 2.2780 1.6935 1.8959 -0.0286 0.1451  0.0739  147  GLU   D C   
9378  O  O   . GLU   D 78  ? 2.3163 1.7314 1.9201 -0.0182 0.1461  0.0746  147  GLU   D O   
9379  C  CB  . GLU   D 78  ? 2.0611 1.5011 1.6777 -0.0240 0.1207  0.0616  147  GLU   D CB  
9380  C  CG  . GLU   D 78  ? 2.1598 1.5793 1.7459 -0.0109 0.1227  0.0618  147  GLU   D CG  
9381  C  CD  . GLU   D 78  ? 2.2126 1.6409 1.7878 0.0005  0.1176  0.0595  147  GLU   D CD  
9382  O  OE1 . GLU   D 78  ? 2.2351 1.6491 1.7908 0.0104  0.1238  0.0625  147  GLU   D OE1 
9383  O  OE2 . GLU   D 78  ? 2.1573 1.6064 1.7433 -0.0003 0.1074  0.0546  147  GLU   D OE2 
9384  N  N   . GLN   D 79  ? 2.5007 1.9010 2.1223 -0.0350 0.1557  0.0789  148  GLN   D N   
9385  C  CA  . GLN   D 79  ? 2.5765 1.9600 2.1875 -0.0307 0.1701  0.0860  148  GLN   D CA  
9386  C  C   . GLN   D 79  ? 2.6722 2.0356 2.2497 -0.0161 0.1720  0.0864  148  GLN   D C   
9387  O  O   . GLN   D 79  ? 2.6641 2.0069 2.2254 -0.0138 0.1743  0.0868  148  GLN   D O   
9388  C  CB  . GLN   D 79  ? 2.5284 1.8982 2.1498 -0.0408 0.1803  0.0907  148  GLN   D CB  
9389  N  N   . ASP   D 80  ? 2.6141 1.9827 2.1810 -0.0060 0.1713  0.0864  149  ASP   D N   
9390  C  CA  . ASP   D 80  ? 2.6344 1.9856 2.1698 0.0088  0.1717  0.0862  149  ASP   D CA  
9391  C  C   . ASP   D 80  ? 2.6726 1.9992 2.1920 0.0133  0.1871  0.0936  149  ASP   D C   
9392  O  O   . ASP   D 80  ? 2.6445 1.9734 2.1714 0.0120  0.1963  0.0986  149  ASP   D O   
9393  C  CB  . ASP   D 80  ? 2.5998 1.9662 2.1308 0.0178  0.1641  0.0830  149  ASP   D CB  
9394  N  N   . PHE   D 81  ? 2.7877 2.0900 2.2837 0.0192  0.1898  0.0943  150  PHE   D N   
9395  C  CA  . PHE   D 81  ? 2.8157 2.0914 2.2951 0.0229  0.2048  0.1013  150  PHE   D CA  
9396  C  C   . PHE   D 81  ? 2.8016 2.0773 2.3043 0.0093  0.2160  0.1068  150  PHE   D C   
9397  O  O   . PHE   D 81  ? 2.7828 2.0529 2.2942 0.0003  0.2165  0.1066  150  PHE   D O   
9398  C  CB  . PHE   D 81  ? 2.7733 2.0424 2.2344 0.0352  0.2104  0.1044  150  PHE   D CB  
9399  N  N   . GLY   D 82  ? 2.7440 2.0256 2.2570 0.0079  0.2250  0.1118  151  GLY   D N   
9400  C  CA  . GLY   D 82  ? 2.6835 1.9699 2.2229 -0.0053 0.2347  0.1166  151  GLY   D CA  
9401  C  C   . GLY   D 82  ? 2.6033 1.9187 2.1703 -0.0120 0.2302  0.1152  151  GLY   D C   
9402  O  O   . GLY   D 82  ? 2.5607 1.8844 2.1533 -0.0233 0.2367  0.1185  151  GLY   D O   
9403  N  N   . ILE   D 83  ? 2.5864 1.9172 2.1487 -0.0050 0.2191  0.1102  152  ILE   D N   
9404  C  CA  . ILE   D 83  ? 2.4920 1.8497 2.0776 -0.0097 0.2143  0.1087  152  ILE   D CA  
9405  C  C   . ILE   D 83  ? 2.5215 1.8999 2.1271 -0.0187 0.2002  0.1019  152  ILE   D C   
9406  O  O   . ILE   D 83  ? 2.5383 1.9178 2.1321 -0.0138 0.1888  0.0961  152  ILE   D O   
9407  C  CB  . ILE   D 83  ? 2.3582 1.7208 1.9280 0.0029  0.2108  0.1074  152  ILE   D CB  
9408  N  N   . GLU   D 84  ? 2.5096 1.9037 2.1456 -0.0317 0.2011  0.1028  153  GLU   D N   
9409  C  CA  . GLU   D 84  ? 2.4853 1.9002 2.1418 -0.0405 0.1879  0.0966  153  GLU   D CA  
9410  C  C   . GLU   D 84  ? 2.4590 1.8962 2.1191 -0.0360 0.1773  0.0921  153  GLU   D C   
9411  O  O   . GLU   D 84  ? 2.4508 1.8992 2.1205 -0.0357 0.1813  0.0946  153  GLU   D O   
9412  C  CB  . GLU   D 84  ? 2.4981 1.9226 2.1858 -0.0552 0.1922  0.0990  153  GLU   D CB  
9413  C  CG  . GLU   D 84  ? 2.4921 1.9429 2.2035 -0.0633 0.1791  0.0932  153  GLU   D CG  
9414  C  CD  . GLU   D 84  ? 2.5082 1.9737 2.2517 -0.0755 0.1832  0.0959  153  GLU   D CD  
9415  O  OE1 . GLU   D 84  ? 2.4503 1.9276 2.2026 -0.0742 0.1872  0.0985  153  GLU   D OE1 
9416  O  OE2 . GLU   D 84  ? 2.5553 2.0207 2.3155 -0.0863 0.1820  0.0952  153  GLU   D OE2 
9417  N  N   . ILE   D 85  ? 2.3244 1.7683 1.9777 -0.0329 0.1641  0.0854  154  ILE   D N   
9418  C  CA  . ILE   D 85  ? 2.1456 1.6098 1.8011 -0.0283 0.1534  0.0806  154  ILE   D CA  
9419  C  C   . ILE   D 85  ? 2.0274 1.5112 1.7043 -0.0379 0.1419  0.0752  154  ILE   D C   
9420  O  O   . ILE   D 85  ? 2.0209 1.4989 1.7001 -0.0436 0.1386  0.0731  154  ILE   D O   
9421  C  CB  . ILE   D 85  ? 2.1788 1.6344 1.8065 -0.0145 0.1475  0.0772  154  ILE   D CB  
9422  C  CG1 . ILE   D 85  ? 2.3465 1.7747 1.9486 -0.0059 0.1581  0.0819  154  ILE   D CG1 
9423  C  CG2 . ILE   D 85  ? 2.0915 1.5641 1.7194 -0.0079 0.1413  0.0748  154  ILE   D CG2 
9424  C  CD1 . ILE   D 85  ? 2.4268 1.8495 2.0291 -0.0042 0.1710  0.0887  154  ILE   D CD1 
9425  N  N   . VAL   D 86  ? 1.8845 1.3908 1.5762 -0.0395 0.1358  0.0730  155  VAL   D N   
9426  C  CA  . VAL   D 86  ? 1.8060 1.3319 1.5147 -0.0463 0.1237  0.0673  155  VAL   D CA  
9427  C  C   . VAL   D 86  ? 1.8009 1.3381 1.4998 -0.0373 0.1139  0.0625  155  VAL   D C   
9428  O  O   . VAL   D 86  ? 1.7826 1.3235 1.4757 -0.0302 0.1163  0.0641  155  VAL   D O   
9429  C  CB  . VAL   D 86  ? 1.7836 1.3274 1.5218 -0.0574 0.1249  0.0689  155  VAL   D CB  
9430  C  CG1 . VAL   D 86  ? 1.7630 1.3289 1.5153 -0.0614 0.1116  0.0628  155  VAL   D CG1 
9431  C  CG2 . VAL   D 86  ? 1.7351 1.2699 1.4863 -0.0679 0.1315  0.0720  155  VAL   D CG2 
9432  N  N   . LYS   D 87  ? 1.7082 1.2505 1.4051 -0.0374 0.1031  0.0567  156  LYS   D N   
9433  C  CA  . LYS   D 87  ? 1.6403 1.1950 1.3309 -0.0299 0.0932  0.0518  156  LYS   D CA  
9434  C  C   . LYS   D 87  ? 1.5502 1.1263 1.2621 -0.0383 0.0838  0.0476  156  LYS   D C   
9435  O  O   . LYS   D 87  ? 1.5381 1.1133 1.2532 -0.0434 0.0782  0.0444  156  LYS   D O   
9436  C  CB  . LYS   D 87  ? 1.6989 1.2396 1.3655 -0.0206 0.0891  0.0486  156  LYS   D CB  
9437  C  CG  . LYS   D 87  ? 1.8067 1.3340 1.4503 -0.0078 0.0939  0.0508  156  LYS   D CG  
9438  C  CD  . LYS   D 87  ? 1.9119 1.4216 1.5317 0.0006  0.0912  0.0483  156  LYS   D CD  
9439  C  CE  . LYS   D 87  ? 1.8785 1.3775 1.4754 0.0144  0.0930  0.0490  156  LYS   D CE  
9440  N  NZ  . LYS   D 87  ? 1.9010 1.4152 1.4962 0.0213  0.0824  0.0437  156  LYS   D NZ  
9441  N  N   . VAL   D 88  ? 1.5895 1.1839 1.3150 -0.0396 0.0820  0.0476  157  VAL   D N   
9442  C  CA  . VAL   D 88  ? 1.5162 1.1318 1.2612 -0.0466 0.0732  0.0438  157  VAL   D CA  
9443  C  C   . VAL   D 88  ? 1.4388 1.0668 1.1777 -0.0387 0.0646  0.0394  157  VAL   D C   
9444  O  O   . VAL   D 88  ? 1.4349 1.0590 1.1598 -0.0291 0.0665  0.0402  157  VAL   D O   
9445  C  CB  . VAL   D 88  ? 1.4565 1.0844 1.2243 -0.0549 0.0777  0.0472  157  VAL   D CB  
9446  C  CG1 . VAL   D 88  ? 1.5341 1.1671 1.2985 -0.0482 0.0819  0.0498  157  VAL   D CG1 
9447  C  CG2 . VAL   D 88  ? 1.3810 1.0288 1.1686 -0.0626 0.0687  0.0434  157  VAL   D CG2 
9448  N  N   . LYS   D 89  ? 1.4361 1.0785 1.1852 -0.0427 0.0551  0.0347  158  LYS   D N   
9449  C  CA  . LYS   D 89  ? 1.3789 1.0366 1.1278 -0.0375 0.0470  0.0307  158  LYS   D CA  
9450  C  C   . LYS   D 89  ? 1.3213 0.9990 1.0929 -0.0462 0.0421  0.0292  158  LYS   D C   
9451  O  O   . LYS   D 89  ? 1.3446 1.0231 1.1282 -0.0553 0.0412  0.0290  158  LYS   D O   
9452  C  CB  . LYS   D 89  ? 1.2999 0.9533 1.0344 -0.0313 0.0396  0.0257  158  LYS   D CB  
9453  N  N   . ALA   D 90  ? 1.3347 1.0280 1.1123 -0.0435 0.0391  0.0283  159  ALA   D N   
9454  C  CA  . ALA   D 90  ? 1.2614 0.9737 1.0595 -0.0510 0.0345  0.0269  159  ALA   D CA  
9455  C  C   . ALA   D 90  ? 1.2879 1.0141 1.0846 -0.0454 0.0270  0.0231  159  ALA   D C   
9456  O  O   . ALA   D 90  ? 1.3593 1.0816 1.1415 -0.0360 0.0266  0.0222  159  ALA   D O   
9457  C  CB  . ALA   D 90  ? 1.2257 0.9435 1.0385 -0.0562 0.0413  0.0316  159  ALA   D CB  
9458  N  N   . ILE   D 91  ? 1.2061 0.9485 1.0181 -0.0512 0.0209  0.0206  160  ILE   D N   
9459  C  CA  . ILE   D 91  ? 1.2170 0.9731 1.0294 -0.0469 0.0136  0.0168  160  ILE   D CA  
9460  C  C   . ILE   D 91  ? 1.3074 1.0808 1.1371 -0.0512 0.0130  0.0178  160  ILE   D C   
9461  O  O   . ILE   D 91  ? 1.2466 1.0236 1.0908 -0.0594 0.0153  0.0200  160  ILE   D O   
9462  C  CB  . ILE   D 91  ? 1.1836 0.9417 0.9949 -0.0485 0.0059  0.0121  160  ILE   D CB  
9463  C  CG1 . ILE   D 91  ? 1.2359 1.0061 1.0453 -0.0428 -0.0007 0.0083  160  ILE   D CG1 
9464  C  CG2 . ILE   D 91  ? 1.1561 0.9208 0.9835 -0.0590 0.0033  0.0117  160  ILE   D CG2 
9465  C  CD1 . ILE   D 91  ? 1.1449 0.9188 0.9556 -0.0452 -0.0077 0.0041  160  ILE   D CD1 
9466  N  N   . GLY   D 92  ? 1.3567 1.1405 1.1851 -0.0454 0.0098  0.0163  161  GLY   D N   
9467  C  CA  . GLY   D 92  ? 1.3406 1.1405 1.1840 -0.0486 0.0089  0.0171  161  GLY   D CA  
9468  C  C   . GLY   D 92  ? 1.3407 1.1534 1.1983 -0.0559 0.0023  0.0142  161  GLY   D C   
9469  O  O   . GLY   D 92  ? 1.3454 1.1591 1.1989 -0.0551 -0.0038 0.0103  161  GLY   D O   
9470  N  N   . ARG   D 93  ? 1.2393 1.0616 1.1133 -0.0628 0.0035  0.0162  162  ARG   D N   
9471  C  CA  . ARG   D 93  ? 1.2066 1.0389 1.0940 -0.0703 -0.0025 0.0138  162  ARG   D CA  
9472  C  C   . ARG   D 93  ? 1.2120 1.0618 1.1124 -0.0718 -0.0052 0.0136  162  ARG   D C   
9473  O  O   . ARG   D 93  ? 1.2409 1.0997 1.1404 -0.0693 -0.0113 0.0103  162  ARG   D O   
9474  C  CB  . ARG   D 93  ? 1.2714 1.0976 1.1682 -0.0789 0.0004  0.0159  162  ARG   D CB  
9475  C  CG  . ARG   D 93  ? 1.1658 0.9770 1.0522 -0.0794 0.0000  0.0146  162  ARG   D CG  
9476  C  CD  . ARG   D 93  ? 1.1537 0.9680 1.0349 -0.0782 -0.0084 0.0096  162  ARG   D CD  
9477  N  NE  . ARG   D 93  ? 1.3107 1.1123 1.1864 -0.0812 -0.0097 0.0082  162  ARG   D NE  
9478  C  CZ  . ARG   D 93  ? 1.2468 1.0395 1.1075 -0.0763 -0.0123 0.0055  162  ARG   D CZ  
9479  N  NH1 . ARG   D 93  ? 1.1988 0.9944 1.0492 -0.0682 -0.0143 0.0035  162  ARG   D NH1 
9480  N  NH2 . ARG   D 93  ? 1.2243 1.0047 1.0806 -0.0796 -0.0129 0.0046  162  ARG   D NH2 
9481  N  N   . GLN   D 94  ? 1.2486 1.1031 1.1610 -0.0757 -0.0006 0.0171  163  GLN   D N   
9482  C  CA  . GLN   D 94  ? 1.1952 1.0658 1.1202 -0.0773 -0.0029 0.0172  163  GLN   D CA  
9483  C  C   . GLN   D 94  ? 1.2538 1.1254 1.1771 -0.0724 0.0033  0.0206  163  GLN   D C   
9484  O  O   . GLN   D 94  ? 1.1943 1.0552 1.1132 -0.0712 0.0108  0.0243  163  GLN   D O   
9485  C  CB  . GLN   D 94  ? 1.2135 1.0914 1.1568 -0.0868 -0.0043 0.0178  163  GLN   D CB  
9486  C  CG  . GLN   D 94  ? 1.2544 1.1321 1.1996 -0.0915 -0.0114 0.0140  163  GLN   D CG  
9487  C  CD  . GLN   D 94  ? 1.4258 1.3052 1.3869 -0.1009 -0.0118 0.0150  163  GLN   D CD  
9488  O  OE1 . GLN   D 94  ? 1.4486 1.3387 1.4210 -0.1054 -0.0177 0.0130  163  GLN   D OE1 
9489  N  NE2 . GLN   D 94  ? 1.4103 1.2788 1.3726 -0.1037 -0.0055 0.0180  163  GLN   D NE2 
9490  N  N   . ARG   D 95  ? 1.2786 1.1626 1.2050 -0.0694 0.0000  0.0194  164  ARG   D N   
9491  C  CA  . ARG   D 95  ? 1.1995 1.0866 1.1260 -0.0652 0.0046  0.0223  164  ARG   D CA  
9492  C  C   . ARG   D 95  ? 1.1839 1.0808 1.1283 -0.0717 0.0071  0.0250  164  ARG   D C   
9493  O  O   . ARG   D 95  ? 1.2021 1.1074 1.1593 -0.0786 0.0027  0.0235  164  ARG   D O   
9494  C  CB  . ARG   D 95  ? 1.1783 1.0738 1.0997 -0.0588 -0.0004 0.0194  164  ARG   D CB  
9495  C  CG  . ARG   D 95  ? 1.1883 1.0762 1.0937 -0.0520 -0.0036 0.0163  164  ARG   D CG  
9496  C  CD  . ARG   D 95  ? 1.1199 1.0198 1.0274 -0.0499 -0.0109 0.0124  164  ARG   D CD  
9497  N  NE  . ARG   D 95  ? 1.1911 1.1035 1.1144 -0.0574 -0.0141 0.0119  164  ARG   D NE  
9498  C  CZ  . ARG   D 95  ? 1.1852 1.1105 1.1148 -0.0575 -0.0195 0.0095  164  ARG   D CZ  
9499  N  NH1 . ARG   D 95  ? 1.2139 1.1420 1.1365 -0.0510 -0.0225 0.0072  164  ARG   D NH1 
9500  N  NH2 . ARG   D 95  ? 1.2480 1.1832 1.1914 -0.0643 -0.0219 0.0095  164  ARG   D NH2 
9501  N  N   . PHE   D 96  ? 1.2603 1.1554 1.2051 -0.0693 0.0141  0.0290  165  PHE   D N   
9502  C  CA  . PHE   D 96  ? 1.3209 1.2239 1.2830 -0.0754 0.0176  0.0320  165  PHE   D CA  
9503  C  C   . PHE   D 96  ? 1.3795 1.2844 1.3401 -0.0703 0.0233  0.0353  165  PHE   D C   
9504  O  O   . PHE   D 96  ? 1.3997 1.2959 1.3448 -0.0624 0.0262  0.0359  165  PHE   D O   
9505  C  CB  . PHE   D 96  ? 1.3409 1.2354 1.3097 -0.0819 0.0230  0.0348  165  PHE   D CB  
9506  C  CG  . PHE   D 96  ? 1.2713 1.1490 1.2269 -0.0775 0.0317  0.0382  165  PHE   D CG  
9507  C  CD1 . PHE   D 96  ? 1.2985 1.1734 1.2529 -0.0740 0.0401  0.0426  165  PHE   D CD1 
9508  C  CD2 . PHE   D 96  ? 1.2532 1.1174 1.1972 -0.0768 0.0317  0.0371  165  PHE   D CD2 
9509  C  CE1 . PHE   D 96  ? 1.2979 1.1565 1.2391 -0.0696 0.0484  0.0459  165  PHE   D CE1 
9510  C  CE2 . PHE   D 96  ? 1.3323 1.1804 1.2634 -0.0725 0.0399  0.0404  165  PHE   D CE2 
9511  C  CZ  . PHE   D 96  ? 1.2966 1.1418 1.2262 -0.0688 0.0483  0.0448  165  PHE   D CZ  
9512  N  N   . LYS   D 97  ? 1.3426 1.2587 1.3193 -0.0747 0.0246  0.0372  166  LYS   D N   
9513  C  CA  . LYS   D 97  ? 1.3644 1.2814 1.3424 -0.0713 0.0316  0.0412  166  LYS   D CA  
9514  C  C   . LYS   D 97  ? 1.3601 1.2734 1.3499 -0.0771 0.0399  0.0457  166  LYS   D C   
9515  O  O   . LYS   D 97  ? 1.3906 1.3090 1.3951 -0.0853 0.0376  0.0451  166  LYS   D O   
9516  C  CB  . LYS   D 97  ? 1.3875 1.3205 1.3752 -0.0713 0.0272  0.0400  166  LYS   D CB  
9517  N  N   . VAL   D 98  ? 1.4142 1.3184 1.3976 -0.0728 0.0495  0.0502  167  VAL   D N   
9518  C  CA  . VAL   D 98  ? 1.4208 1.3206 1.4154 -0.0780 0.0586  0.0549  167  VAL   D CA  
9519  C  C   . VAL   D 98  ? 1.4101 1.3231 1.4225 -0.0811 0.0611  0.0574  167  VAL   D C   
9520  O  O   . VAL   D 98  ? 1.3040 1.2227 1.3130 -0.0758 0.0610  0.0577  167  VAL   D O   
9521  C  CB  . VAL   D 98  ? 1.3360 1.2180 1.3149 -0.0721 0.0688  0.0590  167  VAL   D CB  
9522  C  CG1 . VAL   D 98  ? 1.4060 1.2760 1.3650 -0.0670 0.0653  0.0561  167  VAL   D CG1 
9523  C  CG2 . VAL   D 98  ? 1.4552 1.3372 1.4274 -0.0647 0.0742  0.0618  167  VAL   D CG2 
9524  N  N   . LEU   D 99  ? 1.3938 1.3114 1.4255 -0.0897 0.0634  0.0591  168  LEU   D N   
9525  C  CA  . LEU   D 99  ? 1.3630 1.2933 1.4142 -0.0936 0.0658  0.0614  168  LEU   D CA  
9526  C  C   . LEU   D 99  ? 1.3802 1.3031 1.4364 -0.0939 0.0788  0.0676  168  LEU   D C   
9527  O  O   . LEU   D 99  ? 1.4548 1.3799 1.5104 -0.0894 0.0846  0.0707  168  LEU   D O   
9528  C  CB  . LEU   D 99  ? 1.3122 1.2544 1.3838 -0.1032 0.0582  0.0587  168  LEU   D CB  
9529  C  CG  . LEU   D 99  ? 1.2416 1.1949 1.3135 -0.1040 0.0456  0.0530  168  LEU   D CG  
9530  C  CD1 . LEU   D 99  ? 1.4360 1.3972 1.5022 -0.0976 0.0438  0.0525  168  LEU   D CD1 
9531  C  CD2 . LEU   D 99  ? 1.3429 1.2882 1.4003 -0.1028 0.0394  0.0490  168  LEU   D CD2 
9532  N  N   . GLU   D 100 ? 1.3203 1.2343 1.3817 -0.0991 0.0837  0.0695  169  GLU   D N   
9533  C  CA  . GLU   D 100 ? 1.4344 1.3384 1.4985 -0.0992 0.0970  0.0756  169  GLU   D CA  
9534  C  C   . GLU   D 100 ? 1.5039 1.3886 1.5495 -0.0962 0.1013  0.0763  169  GLU   D C   
9535  O  O   . GLU   D 100 ? 1.4967 1.3773 1.5314 -0.0956 0.0936  0.0721  169  GLU   D O   
9536  C  CB  . GLU   D 100 ? 1.3947 1.3066 1.4861 -0.1093 0.0997  0.0775  169  GLU   D CB  
9537  N  N   . LEU   D 101 ? 1.5782 1.4505 1.6194 -0.0937 0.1140  0.0819  170  LEU   D N   
9538  C  CA  . LEU   D 101 ? 1.6493 1.5017 1.6715 -0.0900 0.1193  0.0833  170  LEU   D CA  
9539  C  C   . LEU   D 101 ? 1.8323 1.6744 1.8612 -0.0924 0.1337  0.0898  170  LEU   D C   
9540  O  O   . LEU   D 101 ? 1.8977 1.7255 1.9106 -0.0853 0.1436  0.0939  170  LEU   D O   
9541  C  CB  . LEU   D 101 ? 1.4536 1.2970 1.4487 -0.0784 0.1186  0.0824  170  LEU   D CB  
9542  N  N   . ARG   D 102 ? 2.0179 1.8670 2.0714 -0.1025 0.1351  0.0909  171  ARG   D N   
9543  C  CA  . ARG   D 102 ? 2.0566 1.8965 2.1193 -0.1058 0.1488  0.0971  171  ARG   D CA  
9544  C  C   . ARG   D 102 ? 2.1025 1.9209 2.1465 -0.1032 0.1544  0.0986  171  ARG   D C   
9545  O  O   . ARG   D 102 ? 2.1080 1.9227 2.1479 -0.1063 0.1467  0.0946  171  ARG   D O   
9546  C  CB  . ARG   D 102 ? 2.0106 1.8628 2.1044 -0.1178 0.1471  0.0969  171  ARG   D CB  
9547  N  N   . THR   D 103 ? 2.0118 1.8155 2.0436 -0.0973 0.1678  0.1043  172  THR   D N   
9548  C  CA  . THR   D 103 ? 2.0332 1.8154 2.0489 -0.0953 0.1749  0.1066  172  THR   D CA  
9549  C  C   . THR   D 103 ? 2.0320 1.8110 2.0686 -0.1053 0.1829  0.1102  172  THR   D C   
9550  O  O   . THR   D 103 ? 2.0079 1.7974 2.0684 -0.1111 0.1881  0.1132  172  THR   D O   
9551  C  CB  . THR   D 103 ? 2.0179 1.7837 2.0093 -0.0840 0.1861  0.1113  172  THR   D CB  
9552  O  OG1 . THR   D 103 ? 2.0045 1.7677 1.9717 -0.0746 0.1776  0.1072  172  THR   D OG1 
9553  C  CG2 . THR   D 103 ? 1.9678 1.7113 1.9487 -0.0836 0.1977  0.1158  172  THR   D CG2 
9554  N  N   . GLN   D 104 ? 2.1154 1.8799 2.1437 -0.1073 0.1833  0.1097  173  GLN   D N   
9555  C  CA  . GLN   D 104 ? 2.2308 1.9891 2.2763 -0.1161 0.1918  0.1133  173  GLN   D CA  
9556  C  C   . GLN   D 104 ? 2.3607 2.0994 2.3931 -0.1106 0.2089  0.1206  173  GLN   D C   
9557  O  O   . GLN   D 104 ? 2.3647 2.0904 2.3696 -0.0998 0.2122  0.1217  173  GLN   D O   
9558  C  CB  . GLN   D 104 ? 2.2415 1.9938 2.2858 -0.1218 0.1835  0.1090  173  GLN   D CB  
9559  N  N   . SER   D 105 ? 2.4967 2.2333 2.5496 -0.1180 0.2198  0.1255  174  SER   D N   
9560  C  CA  . SER   D 105 ? 2.5184 2.2342 2.5594 -0.1139 0.2367  0.1326  174  SER   D CA  
9561  C  C   . SER   D 105 ? 2.5890 2.2838 2.6046 -0.1101 0.2360  0.1314  174  SER   D C   
9562  O  O   . SER   D 105 ? 2.6375 2.3133 2.6286 -0.1011 0.2458  0.1354  174  SER   D O   
9563  C  CB  . SER   D 105 ? 2.4771 2.1952 2.5474 -0.1239 0.2477  0.1376  174  SER   D CB  
9564  O  OG  . SER   D 105 ? 2.5374 2.2600 2.6258 -0.1349 0.2396  0.1339  174  SER   D OG  
9565  N  N   . ASP   D 106 ? 2.6616 2.3591 2.6820 -0.1166 0.2244  0.1260  175  ASP   D N   
9566  C  CA  . ASP   D 106 ? 2.6415 2.3206 2.6376 -0.1127 0.2218  0.1239  175  ASP   D CA  
9567  C  C   . ASP   D 106 ? 2.6570 2.3298 2.6215 -0.0997 0.2173  0.1217  175  ASP   D C   
9568  O  O   . ASP   D 106 ? 2.6653 2.3175 2.6039 -0.0919 0.2234  0.1238  175  ASP   D O   
9569  C  CB  . ASP   D 106 ? 2.5503 2.2363 2.5579 -0.1216 0.2083  0.1177  175  ASP   D CB  
9570  N  N   . GLY   D 107 ? 2.5208 2.2111 2.4871 -0.0972 0.2065  0.1173  176  GLY   D N   
9571  C  CA  . GLY   D 107 ? 2.4056 2.0927 2.3452 -0.0854 0.2011  0.1147  176  GLY   D CA  
9572  C  C   . GLY   D 107 ? 2.3612 2.0640 2.3025 -0.0863 0.1838  0.1070  176  GLY   D C   
9573  O  O   . GLY   D 107 ? 2.2854 1.9991 2.2221 -0.0808 0.1779  0.1047  176  GLY   D O   
9574  N  N   . ILE   D 108 ? 2.4966 2.2003 2.4444 -0.0934 0.1756  0.1030  177  ILE   D N   
9575  C  CA  . ILE   D 108 ? 2.4634 2.1801 2.4119 -0.0946 0.1596  0.0957  177  ILE   D CA  
9576  C  C   . ILE   D 108 ? 2.4189 2.1588 2.3870 -0.0978 0.1535  0.0938  177  ILE   D C   
9577  O  O   . ILE   D 108 ? 2.4392 2.1909 2.4334 -0.1074 0.1533  0.0943  177  ILE   D O   
9578  C  CB  . ILE   D 108 ? 2.4773 2.1919 2.4348 -0.1034 0.1534  0.0924  177  ILE   D CB  
9579  C  CG1 . ILE   D 108 ? 2.4513 2.1429 2.3859 -0.0991 0.1573  0.0932  177  ILE   D CG1 
9580  C  CG2 . ILE   D 108 ? 2.3780 2.1087 2.3410 -0.1060 0.1374  0.0853  177  ILE   D CG2 
9581  C  CD1 . ILE   D 108 ? 2.4236 2.1015 2.3665 -0.1052 0.1692  0.0984  177  ILE   D CD1 
9582  N  N   . GLN   D 109 ? 2.1209 1.8676 2.0769 -0.0897 0.1480  0.0915  178  GLN   D N   
9583  C  CA  . GLN   D 109 ? 1.9619 1.7295 1.9343 -0.0918 0.1426  0.0899  178  GLN   D CA  
9584  C  C   . GLN   D 109 ? 1.8603 1.6429 1.8475 -0.0994 0.1290  0.0839  178  GLN   D C   
9585  O  O   . GLN   D 109 ? 1.8333 1.6113 1.8098 -0.0989 0.1208  0.0795  178  GLN   D O   
9586  C  CB  . GLN   D 109 ? 1.8757 1.6452 1.8300 -0.0809 0.1402  0.0889  178  GLN   D CB  
9587  C  CG  . GLN   D 109 ? 1.8654 1.6435 1.8285 -0.0788 0.1470  0.0928  178  GLN   D CG  
9588  C  CD  . GLN   D 109 ? 1.7753 1.5469 1.7149 -0.0664 0.1486  0.0933  178  GLN   D CD  
9589  O  OE1 . GLN   D 109 ? 1.7087 1.4726 1.6274 -0.0597 0.1426  0.0899  178  GLN   D OE1 
9590  N  NE2 . GLN   D 109 ? 1.7586 1.5328 1.7013 -0.0632 0.1566  0.0976  178  GLN   D NE2 
9591  N  N   . GLN   D 110 ? 1.8448 1.6448 1.8563 -0.1062 0.1267  0.0838  179  GLN   D N   
9592  C  CA  . GLN   D 110 ? 1.8201 1.6362 1.8447 -0.1120 0.1133  0.0781  179  GLN   D CA  
9593  C  C   . GLN   D 110 ? 1.7569 1.5883 1.7815 -0.1074 0.1075  0.0761  179  GLN   D C   
9594  O  O   . GLN   D 110 ? 1.7582 1.5912 1.7815 -0.1026 0.1146  0.0797  179  GLN   D O   
9595  C  CB  . GLN   D 110 ? 1.8154 1.6402 1.8686 -0.1236 0.1133  0.0788  179  GLN   D CB  
9596  C  CG  . GLN   D 110 ? 1.8229 1.6349 1.8780 -0.1296 0.1148  0.0788  179  GLN   D CG  
9597  C  CD  . GLN   D 110 ? 1.9291 1.7523 2.0079 -0.1405 0.1062  0.0754  179  GLN   D CD  
9598  O  OE1 . GLN   D 110 ? 1.9733 1.8042 2.0759 -0.1475 0.1102  0.0779  179  GLN   D OE1 
9599  N  NE2 . GLN   D 110 ? 1.8406 1.6646 1.9129 -0.1416 0.0943  0.0696  179  GLN   D NE2 
9600  N  N   . ALA   D 111 ? 1.6254 1.4675 1.6511 -0.1087 0.0946  0.0703  180  ALA   D N   
9601  C  CA  . ALA   D 111 ? 1.5855 1.4408 1.6088 -0.1039 0.0883  0.0678  180  ALA   D CA  
9602  C  C   . ALA   D 111 ? 1.4959 1.3686 1.5370 -0.1108 0.0772  0.0635  180  ALA   D C   
9603  O  O   . ALA   D 111 ? 1.4637 1.3361 1.5051 -0.1147 0.0691  0.0594  180  ALA   D O   
9604  C  CB  . ALA   D 111 ? 1.5586 1.4064 1.5563 -0.0945 0.0840  0.0649  180  ALA   D CB  
9605  N  N   . LYS   D 112 ? 1.4616 1.3488 1.5169 -0.1119 0.0771  0.0644  181  LYS   D N   
9606  C  CA  . LYS   D 112 ? 1.4287 1.3327 1.4969 -0.1161 0.0660  0.0601  181  LYS   D CA  
9607  C  C   . LYS   D 112 ? 1.4251 1.3317 1.4759 -0.1088 0.0583  0.0561  181  LYS   D C   
9608  O  O   . LYS   D 112 ? 1.3710 1.2787 1.4126 -0.1017 0.0612  0.0575  181  LYS   D O   
9609  C  CB  . LYS   D 112 ? 1.3481 1.2663 1.4371 -0.1196 0.0685  0.0625  181  LYS   D CB  
9610  N  N   . VAL   D 113 ? 1.4423 1.3491 1.4885 -0.1105 0.0489  0.0512  182  VAL   D N   
9611  C  CA  . VAL   D 113 ? 1.3761 1.2822 1.4044 -0.1037 0.0422  0.0474  182  VAL   D CA  
9612  C  C   . VAL   D 113 ? 1.4062 1.3272 1.4437 -0.1070 0.0313  0.0429  182  VAL   D C   
9613  O  O   . VAL   D 113 ? 1.4648 1.3903 1.5158 -0.1145 0.0266  0.0412  182  VAL   D O   
9614  C  CB  . VAL   D 113 ? 1.4178 1.3086 1.4296 -0.1017 0.0416  0.0458  182  VAL   D CB  
9615  C  CG1 . VAL   D 113 ? 1.3804 1.2741 1.3812 -0.0984 0.0316  0.0404  182  VAL   D CG1 
9616  C  CG2 . VAL   D 113 ? 1.4342 1.3104 1.4297 -0.0945 0.0512  0.0495  182  VAL   D CG2 
9617  N  N   . GLN   D 114 ? 1.4319 1.3601 1.4622 -0.1012 0.0273  0.0410  183  GLN   D N   
9618  C  CA  . GLN   D 114 ? 1.4265 1.3676 1.4620 -0.1029 0.0172  0.0367  183  GLN   D CA  
9619  C  C   . GLN   D 114 ? 1.3828 1.3182 1.4004 -0.0977 0.0118  0.0328  183  GLN   D C   
9620  O  O   . GLN   D 114 ? 1.3713 1.3040 1.3754 -0.0901 0.0130  0.0328  183  GLN   D O   
9621  C  CB  . GLN   D 114 ? 1.3950 1.3487 1.4366 -0.1003 0.0172  0.0376  183  GLN   D CB  
9622  C  CG  . GLN   D 114 ? 1.5197 1.4870 1.5675 -0.1021 0.0074  0.0336  183  GLN   D CG  
9623  C  CD  . GLN   D 114 ? 1.6093 1.5875 1.6783 -0.1100 0.0050  0.0339  183  GLN   D CD  
9624  O  OE1 . GLN   D 114 ? 1.6086 1.5876 1.6842 -0.1157 -0.0007 0.0314  183  GLN   D OE1 
9625  N  NE2 . GLN   D 114 ? 1.6304 1.6167 1.7100 -0.1099 0.0090  0.0369  183  GLN   D NE2 
9626  N  N   . ILE   D 115 ? 1.4299 1.3628 1.4475 -0.1018 0.0058  0.0296  184  ILE   D N   
9627  C  CA  . ILE   D 115 ? 1.4349 1.3625 1.4364 -0.0971 0.0007  0.0258  184  ILE   D CA  
9628  C  C   . ILE   D 115 ? 1.4133 1.3523 1.4128 -0.0931 -0.0050 0.0232  184  ILE   D C   
9629  O  O   . ILE   D 115 ? 1.5356 1.4865 1.5469 -0.0970 -0.0101 0.0217  184  ILE   D O   
9630  C  CB  . ILE   D 115 ? 1.5032 1.4267 1.5060 -0.1025 -0.0048 0.0228  184  ILE   D CB  
9631  C  CG1 . ILE   D 115 ? 1.4273 1.3387 1.4321 -0.1065 0.0009  0.0254  184  ILE   D CG1 
9632  C  CG2 . ILE   D 115 ? 1.4821 1.4004 1.4683 -0.0972 -0.0097 0.0190  184  ILE   D CG2 
9633  C  CD1 . ILE   D 115 ? 1.3068 1.2028 1.2931 -0.1009 0.0050  0.0259  184  ILE   D CD1 
9634  N  N   . LEU   D 116 ? 1.3695 1.3049 1.3545 -0.0851 -0.0042 0.0226  185  LEU   D N   
9635  C  CA  . LEU   D 116 ? 1.3627 1.3085 1.3462 -0.0812 -0.0093 0.0202  185  LEU   D CA  
9636  C  C   . LEU   D 116 ? 1.4353 1.3855 1.4191 -0.0835 -0.0176 0.0158  185  LEU   D C   
9637  O  O   . LEU   D 116 ? 1.5110 1.4538 1.4916 -0.0862 -0.0193 0.0143  185  LEU   D O   
9638  C  CB  . LEU   D 116 ? 1.3170 1.2571 1.2850 -0.0722 -0.0074 0.0200  185  LEU   D CB  
9639  C  CG  . LEU   D 116 ? 1.2832 1.2176 1.2476 -0.0682 0.0007  0.0242  185  LEU   D CG  
9640  C  CD1 . LEU   D 116 ? 1.2970 1.2307 1.2490 -0.0593 -0.0003 0.0231  185  LEU   D CD1 
9641  C  CD2 . LEU   D 116 ? 1.3048 1.2484 1.2851 -0.0728 0.0038  0.0273  185  LEU   D CD2 
9642  N  N   . PRO   D 117 ? 1.4483 1.4100 1.4356 -0.0824 -0.0226 0.0137  186  PRO   D N   
9643  C  CA  . PRO   D 117 ? 1.5043 1.4706 1.4926 -0.0848 -0.0300 0.0098  186  PRO   D CA  
9644  C  C   . PRO   D 117 ? 1.4715 1.4307 1.4451 -0.0797 -0.0323 0.0069  186  PRO   D C   
9645  O  O   . PRO   D 117 ? 1.4344 1.3899 1.3980 -0.0730 -0.0301 0.0070  186  PRO   D O   
9646  C  CB  . PRO   D 117 ? 1.4827 1.4630 1.4787 -0.0844 -0.0333 0.0091  186  PRO   D CB  
9647  C  CG  . PRO   D 117 ? 1.4065 1.3874 1.3990 -0.0788 -0.0286 0.0114  186  PRO   D CG  
9648  C  CD  . PRO   D 117 ? 1.3950 1.3658 1.3859 -0.0792 -0.0214 0.0150  186  PRO   D CD  
9649  N  N   . GLU   D 118 ? 1.5266 1.4837 1.4990 -0.0827 -0.0371 0.0041  187  GLU   D N   
9650  C  CA  . GLU   D 118 ? 1.4572 1.4105 1.4178 -0.0783 -0.0405 0.0007  187  GLU   D CA  
9651  C  C   . GLU   D 118 ? 1.3882 1.3498 1.3537 -0.0812 -0.0470 -0.0022 187  GLU   D C   
9652  O  O   . GLU   D 118 ? 1.3902 1.3475 1.3547 -0.0847 -0.0502 -0.0040 187  GLU   D O   
9653  C  CB  . GLU   D 118 ? 1.3961 1.3352 1.3464 -0.0778 -0.0390 0.0002  187  GLU   D CB  
9654  C  CG  . GLU   D 118 ? 1.3807 1.3116 1.3175 -0.0700 -0.0356 0.0006  187  GLU   D CG  
9655  C  CD  . GLU   D 118 ? 1.3617 1.2955 1.2905 -0.0640 -0.0395 -0.0028 187  GLU   D CD  
9656  O  OE1 . GLU   D 118 ? 1.3276 1.2636 1.2522 -0.0579 -0.0384 -0.0027 187  GLU   D OE1 
9657  O  OE2 . GLU   D 118 ? 1.3987 1.3322 1.3254 -0.0653 -0.0437 -0.0057 187  GLU   D OE2 
9658  N  N   . CYS   D 119 ? 1.2878 1.2605 1.2576 -0.0792 -0.0488 -0.0027 188  CYS   D N   
9659  C  CA  . CYS   D 119 ? 1.2808 1.2618 1.2551 -0.0813 -0.0542 -0.0051 188  CYS   D CA  
9660  C  C   . CYS   D 119 ? 1.2779 1.2547 1.2417 -0.0779 -0.0571 -0.0084 188  CYS   D C   
9661  O  O   . CYS   D 119 ? 1.2541 1.2294 1.2102 -0.0718 -0.0559 -0.0092 188  CYS   D O   
9662  C  CB  . CYS   D 119 ? 1.1853 1.1784 1.1662 -0.0796 -0.0547 -0.0046 188  CYS   D CB  
9663  S  SG  . CYS   D 119 ? 1.3378 1.3360 1.3299 -0.0821 -0.0504 -0.0006 188  CYS   D SG  
9664  N  N   . VAL   D 120 ? 1.2684 1.2428 1.2317 -0.0815 -0.0611 -0.0104 189  VAL   D N   
9665  C  CA  . VAL   D 120 ? 1.1296 1.1002 1.0834 -0.0786 -0.0639 -0.0135 189  VAL   D CA  
9666  C  C   . VAL   D 120 ? 1.0830 1.0633 1.0416 -0.0796 -0.0679 -0.0150 189  VAL   D C   
9667  O  O   . VAL   D 120 ? 1.1459 1.1302 1.1126 -0.0846 -0.0703 -0.0146 189  VAL   D O   
9668  C  CB  . VAL   D 120 ? 1.1210 1.0800 1.0689 -0.0813 -0.0652 -0.0146 189  VAL   D CB  
9669  C  CG1 . VAL   D 120 ? 1.1282 1.0810 1.0638 -0.0764 -0.0661 -0.0172 189  VAL   D CG1 
9670  C  CG2 . VAL   D 120 ? 1.1887 1.1393 1.1367 -0.0831 -0.0611 -0.0122 189  VAL   D CG2 
9671  N  N   . LEU   D 121 ? 1.0835 1.0673 1.0374 -0.0746 -0.0684 -0.0167 190  LEU   D N   
9672  C  CA  . LEU   D 121 ? 1.0644 1.0574 1.0225 -0.0749 -0.0713 -0.0178 190  LEU   D CA  
9673  C  C   . LEU   D 121 ? 1.1100 1.0993 1.0598 -0.0728 -0.0735 -0.0206 190  LEU   D C   
9674  O  O   . LEU   D 121 ? 1.1291 1.1129 1.0705 -0.0683 -0.0721 -0.0218 190  LEU   D O   
9675  C  CB  . LEU   D 121 ? 1.0536 1.0561 1.0158 -0.0711 -0.0696 -0.0172 190  LEU   D CB  
9676  C  CG  . LEU   D 121 ? 1.0251 1.0333 0.9958 -0.0725 -0.0675 -0.0144 190  LEU   D CG  
9677  C  CD1 . LEU   D 121 ? 1.0937 1.1099 1.0664 -0.0680 -0.0667 -0.0146 190  LEU   D CD1 
9678  C  CD2 . LEU   D 121 ? 1.0623 1.0755 1.0420 -0.0784 -0.0699 -0.0136 190  LEU   D CD2 
9679  N  N   . PRO   D 122 ? 1.0775 1.0695 1.0291 -0.0755 -0.0770 -0.0217 191  PRO   D N   
9680  C  CA  . PRO   D 122 ? 1.1112 1.0994 1.0544 -0.0731 -0.0786 -0.0242 191  PRO   D CA  
9681  C  C   . PRO   D 122 ? 1.1076 1.1013 1.0493 -0.0675 -0.0765 -0.0249 191  PRO   D C   
9682  O  O   . PRO   D 122 ? 1.1565 1.1577 1.1041 -0.0657 -0.0746 -0.0237 191  PRO   D O   
9683  C  CB  . PRO   D 122 ? 1.2434 1.2347 1.1900 -0.0771 -0.0826 -0.0247 191  PRO   D CB  
9684  C  CG  . PRO   D 122 ? 1.2594 1.2608 1.2180 -0.0797 -0.0823 -0.0225 191  PRO   D CG  
9685  C  CD  . PRO   D 122 ? 1.1499 1.1494 1.1114 -0.0801 -0.0792 -0.0206 191  PRO   D CD  
9686  N  N   . SER   D 123 ? 1.1331 1.1230 1.0669 -0.0645 -0.0769 -0.0270 192  SER   D N   
9687  C  CA  . SER   D 123 ? 1.1399 1.1361 1.0742 -0.0597 -0.0751 -0.0278 192  SER   D CA  
9688  C  C   . SER   D 123 ? 1.1726 1.1797 1.1159 -0.0613 -0.0758 -0.0268 192  SER   D C   
9689  O  O   . SER   D 123 ? 1.2071 1.2151 1.1524 -0.0652 -0.0783 -0.0266 192  SER   D O   
9690  C  CB  . SER   D 123 ? 1.2105 1.2011 1.1358 -0.0567 -0.0752 -0.0299 192  SER   D CB  
9691  O  OG  . SER   D 123 ? 1.1782 1.1766 1.1066 -0.0535 -0.0737 -0.0304 192  SER   D OG  
9692  N  N   . THR   D 124 ? 1.1948 1.2099 1.1434 -0.0581 -0.0738 -0.0265 193  THR   D N   
9693  C  CA  . THR   D 124 ? 1.2044 1.2296 1.1615 -0.0594 -0.0743 -0.0256 193  THR   D CA  
9694  C  C   . THR   D 124 ? 1.2174 1.2428 1.1720 -0.0602 -0.0755 -0.0265 193  THR   D C   
9695  O  O   . THR   D 124 ? 1.2250 1.2555 1.1845 -0.0631 -0.0771 -0.0257 193  THR   D O   
9696  C  CB  . THR   D 124 ? 1.1987 1.2316 1.1610 -0.0553 -0.0723 -0.0256 193  THR   D CB  
9697  O  OG1 . THR   D 124 ? 1.2610 1.2907 1.2181 -0.0504 -0.0707 -0.0274 193  THR   D OG1 
9698  C  CG2 . THR   D 124 ? 1.1692 1.2038 1.1358 -0.0555 -0.0716 -0.0240 193  THR   D CG2 
9699  N  N   . MET   D 125 ? 1.2133 1.2328 1.1597 -0.0573 -0.0747 -0.0282 194  MET   D N   
9700  C  CA  . MET   D 125 ? 1.2209 1.2396 1.1636 -0.0573 -0.0753 -0.0290 194  MET   D CA  
9701  C  C   . MET   D 125 ? 1.2229 1.2345 1.1604 -0.0614 -0.0789 -0.0292 194  MET   D C   
9702  O  O   . MET   D 125 ? 1.2296 1.2407 1.1643 -0.0619 -0.0800 -0.0296 194  MET   D O   
9703  C  CB  . MET   D 125 ? 1.1860 1.2007 1.1217 -0.0524 -0.0727 -0.0306 194  MET   D CB  
9704  C  CG  . MET   D 125 ? 1.2254 1.2477 1.1673 -0.0481 -0.0696 -0.0308 194  MET   D CG  
9705  S  SD  . MET   D 125 ? 1.1549 1.1895 1.1072 -0.0479 -0.0681 -0.0300 194  MET   D SD  
9706  C  CE  . MET   D 125 ? 1.0844 1.1253 1.0456 -0.0520 -0.0705 -0.0281 194  MET   D CE  
9707  N  N   . SER   D 126 ? 1.2245 1.2305 1.1608 -0.0641 -0.0807 -0.0290 195  SER   D N   
9708  C  CA  . SER   D 126 ? 1.2379 1.2369 1.1702 -0.0682 -0.0847 -0.0295 195  SER   D CA  
9709  C  C   . SER   D 126 ? 1.2483 1.2529 1.1854 -0.0709 -0.0873 -0.0289 195  SER   D C   
9710  O  O   . SER   D 126 ? 1.3188 1.3182 1.2494 -0.0715 -0.0899 -0.0301 195  SER   D O   
9711  C  CB  . SER   D 126 ? 1.2612 1.2566 1.1965 -0.0717 -0.0859 -0.0287 195  SER   D CB  
9712  O  OG  . SER   D 126 ? 1.2644 1.2687 1.2109 -0.0742 -0.0855 -0.0267 195  SER   D OG  
9713  N  N   . ALA   D 127 ? 1.2266 1.2414 1.1743 -0.0722 -0.0865 -0.0272 196  ALA   D N   
9714  C  CA  . ALA   D 127 ? 1.2404 1.2605 1.1933 -0.0750 -0.0893 -0.0265 196  ALA   D CA  
9715  C  C   . ALA   D 127 ? 1.2675 1.2897 1.2167 -0.0723 -0.0883 -0.0270 196  ALA   D C   
9716  O  O   . ALA   D 127 ? 1.2460 1.2670 1.1932 -0.0739 -0.0912 -0.0272 196  ALA   D O   
9717  C  CB  . ALA   D 127 ? 1.1645 1.1945 1.1294 -0.0769 -0.0885 -0.0244 196  ALA   D CB  
9718  N  N   . VAL   D 128 ? 1.2926 1.3178 1.2413 -0.0681 -0.0841 -0.0271 197  VAL   D N   
9719  C  CA  . VAL   D 128 ? 1.3060 1.3334 1.2524 -0.0655 -0.0823 -0.0273 197  VAL   D CA  
9720  C  C   . VAL   D 128 ? 1.3649 1.3836 1.2999 -0.0620 -0.0805 -0.0289 197  VAL   D C   
9721  O  O   . VAL   D 128 ? 1.3365 1.3569 1.2698 -0.0587 -0.0772 -0.0290 197  VAL   D O   
9722  C  CB  . VAL   D 128 ? 1.2726 1.3107 1.2283 -0.0636 -0.0789 -0.0262 197  VAL   D CB  
9723  C  CG1 . VAL   D 128 ? 1.2484 1.2938 1.2143 -0.0666 -0.0804 -0.0247 197  VAL   D CG1 
9724  C  CG2 . VAL   D 128 ? 1.2797 1.3180 1.2349 -0.0594 -0.0751 -0.0270 197  VAL   D CG2 
9725  N  N   . GLN   D 129 ? 1.3623 1.3713 1.2894 -0.0625 -0.0824 -0.0301 198  GLN   D N   
9726  C  CA  . GLN   D 129 ? 1.3551 1.3551 1.2705 -0.0589 -0.0808 -0.0317 198  GLN   D CA  
9727  C  C   . GLN   D 129 ? 1.3965 1.3917 1.3042 -0.0587 -0.0824 -0.0321 198  GLN   D C   
9728  O  O   . GLN   D 129 ? 1.4155 1.4092 1.3231 -0.0622 -0.0869 -0.0320 198  GLN   D O   
9729  C  CB  . GLN   D 129 ? 1.3738 1.3638 1.2821 -0.0595 -0.0828 -0.0329 198  GLN   D CB  
9730  C  CG  . GLN   D 129 ? 1.3989 1.3873 1.3050 -0.0554 -0.0789 -0.0336 198  GLN   D CG  
9731  C  CD  . GLN   D 129 ? 1.3799 1.3691 1.2824 -0.0503 -0.0745 -0.0341 198  GLN   D CD  
9732  O  OE1 . GLN   D 129 ? 1.3842 1.3676 1.2782 -0.0491 -0.0745 -0.0347 198  GLN   D OE1 
9733  N  NE2 . GLN   D 129 ? 1.3636 1.3598 1.2727 -0.0472 -0.0707 -0.0338 198  GLN   D NE2 
9734  N  N   . LEU   D 130 ? 1.4009 1.3938 1.3023 -0.0544 -0.0784 -0.0325 199  LEU   D N   
9735  C  CA  . LEU   D 130 ? 1.4034 1.3894 1.2945 -0.0531 -0.0790 -0.0329 199  LEU   D CA  
9736  C  C   . LEU   D 130 ? 1.4425 1.4145 1.3196 -0.0523 -0.0817 -0.0348 199  LEU   D C   
9737  O  O   . LEU   D 130 ? 1.4060 1.3731 1.2777 -0.0492 -0.0789 -0.0358 199  LEU   D O   
9738  C  CB  . LEU   D 130 ? 1.3337 1.3227 1.2242 -0.0487 -0.0728 -0.0323 199  LEU   D CB  
9739  C  CG  . LEU   D 130 ? 1.2573 1.2578 1.1588 -0.0494 -0.0706 -0.0305 199  LEU   D CG  
9740  C  CD1 . LEU   D 130 ? 1.2237 1.2226 1.1203 -0.0454 -0.0653 -0.0301 199  LEU   D CD1 
9741  C  CD2 . LEU   D 130 ? 1.2439 1.2460 1.1478 -0.0537 -0.0758 -0.0299 199  LEU   D CD2 
9742  N  N   . GLU   D 131 ? 1.4997 1.4651 1.3709 -0.0549 -0.0873 -0.0356 200  GLU   D N   
9743  C  CA  . GLU   D 131 ? 1.5186 1.4700 1.3763 -0.0545 -0.0909 -0.0376 200  GLU   D CA  
9744  C  C   . GLU   D 131 ? 1.5259 1.4690 1.3713 -0.0488 -0.0863 -0.0385 200  GLU   D C   
9745  O  O   . GLU   D 131 ? 1.5899 1.5249 1.4285 -0.0477 -0.0867 -0.0399 200  GLU   D O   
9746  C  CB  . GLU   D 131 ? 1.5671 1.5128 1.4190 -0.0566 -0.0970 -0.0383 200  GLU   D CB  
9747  C  CG  . GLU   D 131 ? 1.5907 1.5435 1.4547 -0.0623 -0.1023 -0.0377 200  GLU   D CG  
9748  C  CD  . GLU   D 131 ? 1.5883 1.5556 1.4660 -0.0634 -0.0993 -0.0354 200  GLU   D CD  
9749  O  OE1 . GLU   D 131 ? 1.5893 1.5644 1.4792 -0.0675 -0.1015 -0.0345 200  GLU   D OE1 
9750  O  OE2 . GLU   D 131 ? 1.5452 1.5158 1.4215 -0.0600 -0.0945 -0.0344 200  GLU   D OE2 
9751  N  N   . SER   D 132 ? 1.3914 1.3362 1.2340 -0.0452 -0.0815 -0.0376 201  SER   D N   
9752  C  CA  . SER   D 132 ? 1.4017 1.3386 1.2328 -0.0395 -0.0765 -0.0383 201  SER   D CA  
9753  C  C   . SER   D 132 ? 1.4500 1.3904 1.2861 -0.0375 -0.0724 -0.0384 201  SER   D C   
9754  O  O   . SER   D 132 ? 1.4689 1.4003 1.2947 -0.0338 -0.0705 -0.0397 201  SER   D O   
9755  C  CB  . SER   D 132 ? 1.3197 1.2594 1.1496 -0.0361 -0.0710 -0.0368 201  SER   D CB  
9756  O  OG  . SER   D 132 ? 1.3175 1.2704 1.1615 -0.0355 -0.0656 -0.0353 201  SER   D OG  
9757  N  N   . LEU   D 133 ? 1.4611 1.4140 1.3124 -0.0395 -0.0713 -0.0373 202  LEU   D N   
9758  C  CA  . LEU   D 133 ? 1.4376 1.3948 1.2946 -0.0374 -0.0678 -0.0375 202  LEU   D CA  
9759  C  C   . LEU   D 133 ? 1.4376 1.3893 1.2927 -0.0396 -0.0717 -0.0386 202  LEU   D C   
9760  O  O   . LEU   D 133 ? 1.4735 1.4256 1.3300 -0.0372 -0.0693 -0.0391 202  LEU   D O   
9761  C  CB  . LEU   D 133 ? 1.3994 1.3715 1.2726 -0.0382 -0.0652 -0.0360 202  LEU   D CB  
9762  C  CG  . LEU   D 133 ? 1.3534 1.3314 1.2304 -0.0341 -0.0588 -0.0352 202  LEU   D CG  
9763  C  CD1 . LEU   D 133 ? 1.3133 1.2841 1.1795 -0.0323 -0.0572 -0.0350 202  LEU   D CD1 
9764  C  CD2 . LEU   D 133 ? 1.3539 1.3459 1.2465 -0.0361 -0.0579 -0.0337 202  LEU   D CD2 
9765  N  N   . ASN   D 134 ? 1.4601 1.4068 1.3127 -0.0440 -0.0778 -0.0391 203  ASN   D N   
9766  C  CA  . ASN   D 134 ? 1.4674 1.4094 1.3198 -0.0467 -0.0812 -0.0399 203  ASN   D CA  
9767  C  C   . ASN   D 134 ? 1.5026 1.4335 1.3432 -0.0429 -0.0797 -0.0415 203  ASN   D C   
9768  O  O   . ASN   D 134 ? 1.5219 1.4515 1.3642 -0.0431 -0.0796 -0.0418 203  ASN   D O   
9769  C  CB  . ASN   D 134 ? 1.4671 1.4046 1.3185 -0.0520 -0.0880 -0.0403 203  ASN   D CB  
9770  C  CG  . ASN   D 134 ? 1.4579 1.4074 1.3238 -0.0565 -0.0897 -0.0386 203  ASN   D CG  
9771  O  OD1 . ASN   D 134 ? 1.5499 1.5070 1.4206 -0.0561 -0.0882 -0.0374 203  ASN   D OD1 
9772  N  ND2 . ASN   D 134 ? 1.4170 1.3677 1.2897 -0.0607 -0.0925 -0.0383 203  ASN   D ND2 
9773  N  N   . LYS   D 135 ? 1.5268 1.4493 1.3550 -0.0390 -0.0782 -0.0425 204  LYS   D N   
9774  C  CA  . LYS   D 135 ? 1.5142 1.4252 1.3299 -0.0349 -0.0767 -0.0441 204  LYS   D CA  
9775  C  C   . LYS   D 135 ? 1.5543 1.4710 1.3754 -0.0309 -0.0713 -0.0438 204  LYS   D C   
9776  O  O   . LYS   D 135 ? 1.6139 1.5235 1.4292 -0.0292 -0.0712 -0.0450 204  LYS   D O   
9777  C  CB  . LYS   D 135 ? 1.4455 1.3472 1.2472 -0.0309 -0.0753 -0.0449 204  LYS   D CB  
9778  N  N   . CYS   D 136 ? 1.5782 1.5073 1.4102 -0.0294 -0.0669 -0.0424 205  CYS   D N   
9779  C  CA  . CYS   D 136 ? 1.6217 1.5570 1.4598 -0.0252 -0.0620 -0.0424 205  CYS   D CA  
9780  C  C   . CYS   D 136 ? 1.6760 1.6180 1.5245 -0.0275 -0.0635 -0.0419 205  CYS   D C   
9781  O  O   . CYS   D 136 ? 1.6855 1.6345 1.5412 -0.0243 -0.0602 -0.0419 205  CYS   D O   
9782  C  CB  . CYS   D 136 ? 1.6494 1.5950 1.4955 -0.0226 -0.0569 -0.0412 205  CYS   D CB  
9783  S  SG  . CYS   D 136 ? 1.6258 1.5641 1.4601 -0.0201 -0.0544 -0.0411 205  CYS   D SG  
9784  N  N   . GLN   D 137 ? 1.6667 1.6066 1.5164 -0.0327 -0.0683 -0.0417 206  GLN   D N   
9785  C  CA  . GLN   D 137 ? 1.6758 1.6215 1.5349 -0.0349 -0.0693 -0.0409 206  GLN   D CA  
9786  C  C   . GLN   D 137 ? 1.7865 1.7233 1.6389 -0.0334 -0.0697 -0.0420 206  GLN   D C   
9787  O  O   . GLN   D 137 ? 1.8182 1.7581 1.6767 -0.0345 -0.0700 -0.0413 206  GLN   D O   
9788  C  CB  . GLN   D 137 ? 1.6197 1.5682 1.4846 -0.0413 -0.0736 -0.0398 206  GLN   D CB  
9789  C  CG  . GLN   D 137 ? 1.6058 1.5651 1.4798 -0.0428 -0.0731 -0.0385 206  GLN   D CG  
9790  C  CD  . GLN   D 137 ? 1.6459 1.6162 1.5292 -0.0393 -0.0687 -0.0378 206  GLN   D CD  
9791  O  OE1 . GLN   D 137 ? 1.6462 1.6192 1.5290 -0.0360 -0.0654 -0.0379 206  GLN   D OE1 
9792  N  NE2 . GLN   D 137 ? 1.5693 1.5457 1.4611 -0.0398 -0.0686 -0.0371 206  GLN   D NE2 
9793  N  N   . ILE   D 138 ? 1.7642 1.6895 1.6038 -0.0306 -0.0694 -0.0435 207  ILE   D N   
9794  C  CA  . ILE   D 138 ? 1.8122 1.7289 1.6450 -0.0281 -0.0691 -0.0446 207  ILE   D CA  
9795  C  C   . ILE   D 138 ? 1.8426 1.7625 1.6753 -0.0213 -0.0642 -0.0452 207  ILE   D C   
9796  O  O   . ILE   D 138 ? 1.8191 1.7361 1.6455 -0.0178 -0.0619 -0.0460 207  ILE   D O   
9797  C  CB  . ILE   D 138 ? 1.8174 1.7187 1.6360 -0.0292 -0.0722 -0.0460 207  ILE   D CB  
9798  C  CG1 . ILE   D 138 ? 1.8551 1.7541 1.6760 -0.0362 -0.0775 -0.0455 207  ILE   D CG1 
9799  C  CG2 . ILE   D 138 ? 1.7813 1.6738 1.5925 -0.0259 -0.0712 -0.0471 207  ILE   D CG2 
9800  C  CD1 . ILE   D 138 ? 1.7826 1.6779 1.6056 -0.0391 -0.0791 -0.0451 207  ILE   D CD1 
9801  N  N   . PHE   D 139 ? 1.9608 1.8865 1.8005 -0.0192 -0.0627 -0.0450 208  PHE   D N   
9802  C  CA  . PHE   D 139 ? 1.9967 1.9269 1.8388 -0.0128 -0.0585 -0.0457 208  PHE   D CA  
9803  C  C   . PHE   D 139 ? 2.0039 1.9234 1.8355 -0.0085 -0.0578 -0.0473 208  PHE   D C   
9804  O  O   . PHE   D 139 ? 2.0273 1.9393 1.8542 -0.0103 -0.0603 -0.0474 208  PHE   D O   
9805  C  CB  . PHE   D 139 ? 1.9888 1.9319 1.8448 -0.0122 -0.0576 -0.0449 208  PHE   D CB  
9806  C  CG  . PHE   D 139 ? 1.9783 1.9311 1.8447 -0.0171 -0.0591 -0.0433 208  PHE   D CG  
9807  C  CD1 . PHE   D 139 ? 1.9646 1.9224 1.8338 -0.0182 -0.0579 -0.0427 208  PHE   D CD1 
9808  C  CD2 . PHE   D 139 ? 1.9506 1.9071 1.8234 -0.0204 -0.0613 -0.0422 208  PHE   D CD2 
9809  C  CE1 . PHE   D 139 ? 1.9051 1.8716 1.7836 -0.0226 -0.0593 -0.0412 208  PHE   D CE1 
9810  C  CE2 . PHE   D 139 ? 1.9460 1.9114 1.8283 -0.0247 -0.0625 -0.0406 208  PHE   D CE2 
9811  C  CZ  . PHE   D 139 ? 1.9205 1.8911 1.8058 -0.0258 -0.0617 -0.0402 208  PHE   D CZ  
9812  N  N   . PRO   D 140 ? 1.8463 1.7644 1.6739 -0.0026 -0.0543 -0.0484 209  PRO   D N   
9813  C  CA  . PRO   D 140 ? 1.8497 1.7575 1.6672 0.0020  -0.0536 -0.0500 209  PRO   D CA  
9814  C  C   . PRO   D 140 ? 1.9184 1.8290 1.7411 0.0033  -0.0544 -0.0500 209  PRO   D C   
9815  O  O   . PRO   D 140 ? 1.8986 1.8210 1.7338 0.0031  -0.0541 -0.0492 209  PRO   D O   
9816  C  CB  . PRO   D 140 ? 1.7894 1.6994 1.6063 0.0084  -0.0489 -0.0509 209  PRO   D CB  
9817  C  CG  . PRO   D 140 ? 1.6750 1.5907 1.4957 0.0061  -0.0476 -0.0498 209  PRO   D CG  
9818  C  CD  . PRO   D 140 ? 1.7361 1.6606 1.5674 0.0000  -0.0506 -0.0483 209  PRO   D CD  
9819  N  N   . SER   D 141 ? 1.9676 1.8664 1.7799 0.0047  -0.0556 -0.0508 210  SER   D N   
9820  C  CA  . SER   D 141 ? 2.0006 1.8993 1.8152 0.0059  -0.0566 -0.0507 210  SER   D CA  
9821  C  C   . SER   D 141 ? 1.9850 1.8944 1.8091 0.0117  -0.0543 -0.0514 210  SER   D C   
9822  O  O   . SER   D 141 ? 1.9769 1.8895 1.8022 0.0164  -0.0515 -0.0525 210  SER   D O   
9823  C  CB  . SER   D 141 ? 1.9791 1.8626 1.7798 0.0079  -0.0574 -0.0518 210  SER   D CB  
9824  O  OG  . SER   D 141 ? 1.9662 1.8388 1.7575 0.0031  -0.0597 -0.0516 210  SER   D OG  
9825  N  N   . LYS   D 142 ? 1.8812 1.7956 1.7122 0.0115  -0.0556 -0.0508 211  LYS   D N   
9826  C  CA  . LYS   D 142 ? 1.8395 1.7636 1.6799 0.0169  -0.0546 -0.0516 211  LYS   D CA  
9827  C  C   . LYS   D 142 ? 2.0220 1.9387 1.8548 0.0239  -0.0539 -0.0535 211  LYS   D C   
9828  O  O   . LYS   D 142 ? 2.0546 1.9624 1.8799 0.0244  -0.0555 -0.0534 211  LYS   D O   
9829  C  CB  . LYS   D 142 ? 1.7073 1.6383 1.5564 0.0147  -0.0565 -0.0504 211  LYS   D CB  
9830  C  CG  . LYS   D 142 ? 1.6981 1.6226 1.5428 0.0083  -0.0585 -0.0486 211  LYS   D CG  
9831  C  CD  . LYS   D 142 ? 1.6707 1.6026 1.5242 0.0068  -0.0598 -0.0472 211  LYS   D CD  
9832  C  CE  . LYS   D 142 ? 1.6566 1.5848 1.5090 -0.0004 -0.0611 -0.0450 211  LYS   D CE  
9833  N  NZ  . LYS   D 142 ? 1.6084 1.5454 1.4706 -0.0024 -0.0619 -0.0434 211  LYS   D NZ  
9834  N  N   . PRO   D 143 ? 2.0834 2.0031 1.9179 0.0295  -0.0514 -0.0551 212  PRO   D N   
9835  C  CA  . PRO   D 143 ? 2.0725 1.9867 1.9016 0.0368  -0.0510 -0.0570 212  PRO   D CA  
9836  C  C   . PRO   D 143 ? 2.0714 1.9920 1.9084 0.0399  -0.0530 -0.0575 212  PRO   D C   
9837  O  O   . PRO   D 143 ? 2.0987 2.0324 1.9495 0.0400  -0.0531 -0.0575 212  PRO   D O   
9838  C  CB  . PRO   D 143 ? 2.0733 1.9925 1.9061 0.0414  -0.0474 -0.0582 212  PRO   D CB  
9839  C  CG  . PRO   D 143 ? 2.0795 2.0003 1.9126 0.0362  -0.0459 -0.0569 212  PRO   D CG  
9840  C  CD  . PRO   D 143 ? 2.0387 1.9653 1.8786 0.0295  -0.0485 -0.0551 212  PRO   D CD  
9841  N  N   . VAL   D 144 ? 2.0447 1.9553 1.8722 0.0428  -0.0545 -0.0580 213  VAL   D N   
9842  C  CA  . VAL   D 144 ? 2.0042 1.9183 1.8364 0.0461  -0.0568 -0.0584 213  VAL   D CA  
9843  C  C   . VAL   D 144 ? 1.9428 1.8659 1.7843 0.0536  -0.0567 -0.0609 213  VAL   D C   
9844  O  O   . VAL   D 144 ? 1.8937 1.8252 1.7449 0.0556  -0.0587 -0.0614 213  VAL   D O   
9845  C  CB  . VAL   D 144 ? 1.9570 1.8566 1.7755 0.0476  -0.0582 -0.0582 213  VAL   D CB  
9846  C  CG1 . VAL   D 144 ? 1.9078 1.8007 1.7208 0.0397  -0.0586 -0.0557 213  VAL   D CG1 
9847  C  CG2 . VAL   D 144 ? 2.0174 1.9062 1.8241 0.0525  -0.0569 -0.0599 213  VAL   D CG2 
9848  N  N   . SER   D 151 ? 1.5947 1.5761 1.4997 0.0428  -0.0601 -0.0588 220  SER   D N   
9849  C  CA  . SER   D 151 ? 1.7404 1.7350 1.6608 0.0447  -0.0587 -0.0601 220  SER   D CA  
9850  C  C   . SER   D 151 ? 1.7312 1.7352 1.6614 0.0383  -0.0581 -0.0582 220  SER   D C   
9851  O  O   . SER   D 151 ? 1.6580 1.6581 1.5822 0.0325  -0.0567 -0.0560 220  SER   D O   
9852  C  CB  . SER   D 151 ? 1.6920 1.6845 1.6100 0.0474  -0.0547 -0.0609 220  SER   D CB  
9853  O  OG  . SER   D 151 ? 1.6464 1.6511 1.5793 0.0485  -0.0523 -0.0617 220  SER   D OG  
9854  N  N   . TYR   D 152 ? 1.8025 1.8185 1.7476 0.0394  -0.0596 -0.0591 221  TYR   D N   
9855  C  CA  . TYR   D 152 ? 1.7883 1.8132 1.7428 0.0337  -0.0593 -0.0574 221  TYR   D CA  
9856  C  C   . TYR   D 152 ? 1.7645 1.7903 1.7188 0.0296  -0.0550 -0.0559 221  TYR   D C   
9857  O  O   . TYR   D 152 ? 1.7218 1.7490 1.6761 0.0237  -0.0546 -0.0537 221  TYR   D O   
9858  C  CB  . TYR   D 152 ? 1.7977 1.8353 1.7691 0.0363  -0.0612 -0.0591 221  TYR   D CB  
9859  N  N   . LYS   D 153 ? 1.6569 1.6819 1.6108 0.0330  -0.0515 -0.0569 222  LYS   D N   
9860  C  CA  . LYS   D 153 ? 1.5252 1.5506 1.4784 0.0301  -0.0470 -0.0555 222  LYS   D CA  
9861  C  C   . LYS   D 153 ? 1.5212 1.5367 1.4606 0.0246  -0.0471 -0.0534 222  LYS   D C   
9862  O  O   . LYS   D 153 ? 1.5125 1.5301 1.4529 0.0200  -0.0454 -0.0516 222  LYS   D O   
9863  C  CB  . LYS   D 153 ? 1.5144 1.5376 1.4662 0.0354  -0.0431 -0.0569 222  LYS   D CB  
9864  N  N   . TRP   D 154 ? 1.5455 1.5499 1.4719 0.0252  -0.0493 -0.0535 223  TRP   D N   
9865  C  CA  . TRP   D 154 ? 1.4764 1.4716 1.3911 0.0196  -0.0501 -0.0517 223  TRP   D CA  
9866  C  C   . TRP   D 154 ? 1.4818 1.4826 1.4024 0.0140  -0.0524 -0.0499 223  TRP   D C   
9867  O  O   . TRP   D 154 ? 1.4577 1.4603 1.3791 0.0090  -0.0516 -0.0483 223  TRP   D O   
9868  C  CB  . TRP   D 154 ? 1.3819 1.3642 1.2828 0.0213  -0.0519 -0.0522 223  TRP   D CB  
9869  C  CG  . TRP   D 154 ? 1.3662 1.3381 1.2551 0.0162  -0.0522 -0.0507 223  TRP   D CG  
9870  C  CD1 . TRP   D 154 ? 1.4445 1.4084 1.3237 0.0159  -0.0503 -0.0508 223  TRP   D CD1 
9871  C  CD2 . TRP   D 154 ? 1.3909 1.3593 1.2766 0.0106  -0.0549 -0.0490 223  TRP   D CD2 
9872  N  NE1 . TRP   D 154 ? 1.5097 1.4653 1.3801 0.0104  -0.0521 -0.0495 223  TRP   D NE1 
9873  C  CE2 . TRP   D 154 ? 1.4434 1.4019 1.3182 0.0070  -0.0548 -0.0483 223  TRP   D CE2 
9874  C  CE3 . TRP   D 154 ? 1.3554 1.3276 1.2463 0.0085  -0.0572 -0.0480 223  TRP   D CE3 
9875  C  CZ2 . TRP   D 154 ? 1.4099 1.3630 1.2804 0.0011  -0.0571 -0.0467 223  TRP   D CZ2 
9876  C  CZ3 . TRP   D 154 ? 1.4030 1.3697 1.2891 0.0028  -0.0588 -0.0462 223  TRP   D CZ3 
9877  C  CH2 . TRP   D 154 ? 1.3907 1.3483 1.2675 -0.0010 -0.0588 -0.0456 223  TRP   D CH2 
9878  N  N   . TRP   D 155 ? 1.4524 1.4557 1.3769 0.0149  -0.0554 -0.0501 224  TRP   D N   
9879  C  CA  . TRP   D 155 ? 1.3933 1.4006 1.3220 0.0098  -0.0575 -0.0483 224  TRP   D CA  
9880  C  C   . TRP   D 155 ? 1.4009 1.4203 1.3425 0.0073  -0.0565 -0.0477 224  TRP   D C   
9881  O  O   . TRP   D 155 ? 1.4015 1.4243 1.3464 0.0025  -0.0578 -0.0460 224  TRP   D O   
9882  C  CB  . TRP   D 155 ? 1.3461 1.3531 1.2756 0.0122  -0.0605 -0.0487 224  TRP   D CB  
9883  C  CG  . TRP   D 155 ? 1.2859 1.2801 1.2020 0.0126  -0.0614 -0.0484 224  TRP   D CG  
9884  C  CD1 . TRP   D 155 ? 1.2718 1.2584 1.1804 0.0181  -0.0617 -0.0501 224  TRP   D CD1 
9885  C  CD2 . TRP   D 155 ? 1.2577 1.2448 1.1666 0.0073  -0.0621 -0.0462 224  TRP   D CD2 
9886  N  NE1 . TRP   D 155 ? 1.2949 1.2698 1.1916 0.0165  -0.0623 -0.0490 224  TRP   D NE1 
9887  C  CE2 . TRP   D 155 ? 1.2874 1.2625 1.1845 0.0098  -0.0625 -0.0466 224  TRP   D CE2 
9888  C  CE3 . TRP   D 155 ? 1.2532 1.2429 1.1649 0.0007  -0.0625 -0.0440 224  TRP   D CE3 
9889  C  CZ2 . TRP   D 155 ? 1.2880 1.2538 1.1769 0.0057  -0.0628 -0.0447 224  TRP   D CZ2 
9890  C  CZ3 . TRP   D 155 ? 1.2382 1.2192 1.1422 -0.0032 -0.0631 -0.0423 224  TRP   D CZ3 
9891  C  CH2 . TRP   D 155 ? 1.2388 1.2080 1.1318 -0.0009 -0.0631 -0.0426 224  TRP   D CH2 
9892  N  N   . GLN   D 156 ? 1.4339 1.4599 1.3833 0.0105  -0.0541 -0.0489 225  GLN   D N   
9893  C  CA  . GLN   D 156 ? 1.4041 1.4401 1.3646 0.0079  -0.0523 -0.0481 225  GLN   D CA  
9894  C  C   . GLN   D 156 ? 1.3598 1.3915 1.3137 0.0044  -0.0494 -0.0466 225  GLN   D C   
9895  O  O   . GLN   D 156 ? 1.3227 1.3574 1.2788 -0.0005 -0.0494 -0.0449 225  GLN   D O   
9896  C  CB  . GLN   D 156 ? 1.4373 1.4825 1.4106 0.0126  -0.0507 -0.0499 225  GLN   D CB  
9897  C  CG  . GLN   D 156 ? 1.5260 1.5760 1.5068 0.0162  -0.0545 -0.0517 225  GLN   D CG  
9898  C  CD  . GLN   D 156 ? 1.5437 1.6000 1.5314 0.0125  -0.0574 -0.0506 225  GLN   D CD  
9899  O  OE1 . GLN   D 156 ? 1.4921 1.5585 1.4927 0.0117  -0.0568 -0.0507 225  GLN   D OE1 
9900  N  NE2 . GLN   D 156 ? 1.4753 1.5255 1.4547 0.0105  -0.0601 -0.0495 225  GLN   D NE2 
9901  N  N   . LYS   D 157 ? 1.3685 1.3923 1.3131 0.0071  -0.0470 -0.0473 226  LYS   D N   
9902  C  CA  . LYS   D 157 ? 1.3318 1.3491 1.2671 0.0040  -0.0450 -0.0461 226  LYS   D CA  
9903  C  C   . LYS   D 157 ? 1.2812 1.2917 1.2081 -0.0014 -0.0484 -0.0447 226  LYS   D C   
9904  O  O   . LYS   D 157 ? 1.2436 1.2522 1.1671 -0.0055 -0.0482 -0.0433 226  LYS   D O   
9905  C  CB  . LYS   D 157 ? 1.3535 1.3621 1.2790 0.0084  -0.0422 -0.0472 226  LYS   D CB  
9906  N  N   . TYR   D 158 ? 1.3079 1.3146 1.2317 -0.0013 -0.0515 -0.0450 227  TYR   D N   
9907  C  CA  . TYR   D 158 ? 1.3085 1.3095 1.2262 -0.0065 -0.0544 -0.0435 227  TYR   D CA  
9908  C  C   . TYR   D 158 ? 1.2270 1.2367 1.1538 -0.0112 -0.0555 -0.0419 227  TYR   D C   
9909  O  O   . TYR   D 158 ? 1.2197 1.2271 1.1433 -0.0160 -0.0563 -0.0405 227  TYR   D O   
9910  C  CB  . TYR   D 158 ? 1.2837 1.2794 1.1973 -0.0050 -0.0566 -0.0439 227  TYR   D CB  
9911  C  CG  . TYR   D 158 ? 1.2293 1.2217 1.1405 -0.0103 -0.0592 -0.0422 227  TYR   D CG  
9912  C  CD1 . TYR   D 158 ? 1.1877 1.1881 1.1080 -0.0123 -0.0606 -0.0411 227  TYR   D CD1 
9913  C  CD2 . TYR   D 158 ? 1.2273 1.2084 1.1276 -0.0131 -0.0602 -0.0417 227  TYR   D CD2 
9914  C  CE1 . TYR   D 158 ? 1.1503 1.1479 1.0692 -0.0170 -0.0624 -0.0393 227  TYR   D CE1 
9915  C  CE2 . TYR   D 158 ? 1.2301 1.2086 1.1297 -0.0181 -0.0623 -0.0401 227  TYR   D CE2 
9916  C  CZ  . TYR   D 158 ? 1.1629 1.1498 1.0719 -0.0199 -0.0631 -0.0388 227  TYR   D CZ  
9917  O  OH  . TYR   D 158 ? 1.1620 1.1467 1.0711 -0.0247 -0.0646 -0.0370 227  TYR   D OH  
9918  N  N   . GLN   D 159 ? 1.2062 1.2262 1.1448 -0.0097 -0.0557 -0.0421 228  GLN   D N   
9919  C  CA  . GLN   D 159 ? 1.1787 1.2070 1.1261 -0.0138 -0.0567 -0.0405 228  GLN   D CA  
9920  C  C   . GLN   D 159 ? 1.1766 1.2084 1.1264 -0.0160 -0.0545 -0.0397 228  GLN   D C   
9921  O  O   . GLN   D 159 ? 1.1687 1.2023 1.1197 -0.0206 -0.0556 -0.0382 228  GLN   D O   
9922  C  CB  . GLN   D 159 ? 1.1924 1.2300 1.1511 -0.0109 -0.0576 -0.0413 228  GLN   D CB  
9923  C  CG  . GLN   D 159 ? 1.1292 1.1760 1.0979 -0.0143 -0.0586 -0.0400 228  GLN   D CG  
9924  C  CD  . GLN   D 159 ? 1.1057 1.1607 1.0851 -0.0108 -0.0596 -0.0412 228  GLN   D CD  
9925  O  OE1 . GLN   D 159 ? 1.0341 1.0893 1.0142 -0.0104 -0.0622 -0.0412 228  GLN   D OE1 
9926  N  NE2 . GLN   D 159 ? 1.1644 1.2260 1.1521 -0.0081 -0.0576 -0.0425 228  GLN   D NE2 
9927  N  N   . LYS   D 160 ? 1.1854 1.2179 1.1356 -0.0124 -0.0511 -0.0407 229  LYS   D N   
9928  C  CA  . LYS   D 160 ? 1.2014 1.2362 1.1529 -0.0140 -0.0482 -0.0398 229  LYS   D CA  
9929  C  C   . LYS   D 160 ? 1.1806 1.2058 1.1198 -0.0175 -0.0491 -0.0388 229  LYS   D C   
9930  O  O   . LYS   D 160 ? 1.2567 1.2838 1.1968 -0.0209 -0.0491 -0.0375 229  LYS   D O   
9931  C  CB  . LYS   D 160 ? 1.2340 1.2705 1.1881 -0.0091 -0.0437 -0.0409 229  LYS   D CB  
9932  C  CG  . LYS   D 160 ? 1.3704 1.4193 1.3403 -0.0077 -0.0417 -0.0411 229  LYS   D CG  
9933  C  CD  . LYS   D 160 ? 1.4543 1.5074 1.4282 -0.0104 -0.0387 -0.0394 229  LYS   D CD  
9934  C  CE  . LYS   D 160 ? 1.5365 1.6014 1.5268 -0.0087 -0.0361 -0.0397 229  LYS   D CE  
9935  N  NZ  . LYS   D 160 ? 1.4252 1.4969 1.4231 -0.0126 -0.0357 -0.0380 229  LYS   D NZ  
9936  N  N   . ARG   D 161 ? 1.1870 1.2016 1.1146 -0.0166 -0.0502 -0.0396 230  ARG   D N   
9937  C  CA  . ARG   D 161 ? 1.1928 1.1977 1.1087 -0.0199 -0.0517 -0.0391 230  ARG   D CA  
9938  C  C   . ARG   D 161 ? 1.2298 1.2345 1.1465 -0.0254 -0.0560 -0.0379 230  ARG   D C   
9939  O  O   . ARG   D 161 ? 1.3377 1.3420 1.2531 -0.0292 -0.0574 -0.0369 230  ARG   D O   
9940  C  CB  . ARG   D 161 ? 1.1881 1.1811 1.0911 -0.0170 -0.0513 -0.0404 230  ARG   D CB  
9941  N  N   . LYS   D 162 ? 1.2570 1.2622 1.1762 -0.0257 -0.0580 -0.0380 231  LYS   D N   
9942  C  CA  . LYS   D 162 ? 1.2123 1.2154 1.1310 -0.0307 -0.0616 -0.0368 231  LYS   D CA  
9943  C  C   . LYS   D 162 ? 1.1405 1.1532 1.0691 -0.0343 -0.0626 -0.0352 231  LYS   D C   
9944  O  O   . LYS   D 162 ? 1.1249 1.1360 1.0529 -0.0390 -0.0652 -0.0341 231  LYS   D O   
9945  C  CB  . LYS   D 162 ? 1.1413 1.1418 1.0596 -0.0295 -0.0626 -0.0370 231  LYS   D CB  
9946  C  CG  . LYS   D 162 ? 1.1653 1.1609 1.0813 -0.0345 -0.0655 -0.0358 231  LYS   D CG  
9947  C  CD  . LYS   D 162 ? 1.2232 1.2142 1.1368 -0.0329 -0.0658 -0.0359 231  LYS   D CD  
9948  C  CE  . LYS   D 162 ? 1.2855 1.2674 1.1934 -0.0373 -0.0678 -0.0350 231  LYS   D CE  
9949  N  NZ  . LYS   D 162 ? 1.3000 1.2694 1.1961 -0.0356 -0.0678 -0.0363 231  LYS   D NZ  
9950  N  N   . PHE   D 163 ? 1.1540 1.1767 1.0924 -0.0322 -0.0607 -0.0351 232  PHE   D N   
9951  C  CA  . PHE   D 163 ? 1.1226 1.1547 1.0710 -0.0351 -0.0615 -0.0337 232  PHE   D CA  
9952  C  C   . PHE   D 163 ? 1.1480 1.1852 1.1000 -0.0349 -0.0592 -0.0334 232  PHE   D C   
9953  O  O   . PHE   D 163 ? 1.1129 1.1593 1.0747 -0.0357 -0.0589 -0.0326 232  PHE   D O   
9954  C  CB  . PHE   D 163 ? 1.0650 1.1041 1.0221 -0.0331 -0.0617 -0.0339 232  PHE   D CB  
9955  C  CG  . PHE   D 163 ? 1.0646 1.0980 1.0174 -0.0328 -0.0634 -0.0340 232  PHE   D CG  
9956  C  CD1 . PHE   D 163 ? 1.0615 1.0916 1.0123 -0.0372 -0.0656 -0.0325 232  PHE   D CD1 
9957  C  CD2 . PHE   D 163 ? 1.0880 1.1194 1.0394 -0.0279 -0.0627 -0.0354 232  PHE   D CD2 
9958  C  CE1 . PHE   D 163 ? 1.0432 1.0677 0.9903 -0.0368 -0.0664 -0.0323 232  PHE   D CE1 
9959  C  CE2 . PHE   D 163 ? 1.0382 1.0637 0.9849 -0.0273 -0.0639 -0.0353 232  PHE   D CE2 
9960  C  CZ  . PHE   D 163 ? 1.0277 1.0495 0.9721 -0.0319 -0.0655 -0.0337 232  PHE   D CZ  
9961  N  N   . HIS   D 164 ? 1.1766 1.2073 1.1202 -0.0337 -0.0575 -0.0339 233  HIS   D N   
9962  C  CA  . HIS   D 164 ? 1.1360 1.1698 1.0813 -0.0331 -0.0545 -0.0335 233  HIS   D CA  
9963  C  C   . HIS   D 164 ? 1.1009 1.1385 1.0495 -0.0375 -0.0564 -0.0318 233  HIS   D C   
9964  O  O   . HIS   D 164 ? 1.0814 1.1268 1.0381 -0.0375 -0.0545 -0.0310 233  HIS   D O   
9965  C  CB  . HIS   D 164 ? 1.0716 1.0955 1.0047 -0.0309 -0.0526 -0.0342 233  HIS   D CB  
9966  C  CG  . HIS   D 164 ? 1.1361 1.1597 1.0670 -0.0309 -0.0500 -0.0334 233  HIS   D CG  
9967  N  ND1 . HIS   D 164 ? 1.0871 1.1159 1.0237 -0.0277 -0.0449 -0.0333 233  HIS   D ND1 
9968  C  CD2 . HIS   D 164 ? 1.1553 1.1734 1.0786 -0.0335 -0.0516 -0.0326 233  HIS   D CD2 
9969  C  CE1 . HIS   D 164 ? 1.1482 1.1743 1.0801 -0.0282 -0.0430 -0.0322 233  HIS   D CE1 
9970  N  NE2 . HIS   D 164 ? 1.1440 1.1635 1.0673 -0.0316 -0.0473 -0.0319 233  HIS   D NE2 
9971  N  N   . CYS   D 165 ? 1.1122 1.1443 1.0549 -0.0412 -0.0603 -0.0314 234  CYS   D N   
9972  C  CA  . CYS   D 165 ? 1.0551 1.0903 1.0008 -0.0455 -0.0628 -0.0300 234  CYS   D CA  
9973  C  C   . CYS   D 165 ? 1.0214 1.0664 0.9789 -0.0473 -0.0640 -0.0290 234  CYS   D C   
9974  O  O   . CYS   D 165 ? 0.9942 1.0423 0.9550 -0.0508 -0.0662 -0.0278 234  CYS   D O   
9975  C  CB  . CYS   D 165 ? 1.1329 1.1596 1.0703 -0.0489 -0.0671 -0.0301 234  CYS   D CB  
9976  S  SG  . CYS   D 165 ? 1.1670 1.1814 1.0893 -0.0472 -0.0667 -0.0312 234  CYS   D SG  
9977  N  N   . ALA   D 166 ? 1.0137 1.0631 0.9772 -0.0448 -0.0628 -0.0295 235  ALA   D N   
9978  C  CA  . ALA   D 166 ? 0.9736 1.0324 0.9480 -0.0458 -0.0635 -0.0286 235  ALA   D CA  
9979  C  C   . ALA   D 166 ? 1.0237 1.0897 1.0047 -0.0456 -0.0614 -0.0280 235  ALA   D C   
9980  O  O   . ALA   D 166 ? 0.9776 1.0512 0.9674 -0.0469 -0.0622 -0.0271 235  ALA   D O   
9981  C  CB  . ALA   D 166 ? 1.0191 1.0802 0.9975 -0.0424 -0.0629 -0.0296 235  ALA   D CB  
9982  N  N   . ASN   D 167 ? 1.0509 1.1137 1.0272 -0.0439 -0.0586 -0.0283 236  ASN   D N   
9983  C  CA  . ASN   D 167 ? 1.0042 1.0721 0.9854 -0.0437 -0.0559 -0.0275 236  ASN   D CA  
9984  C  C   . ASN   D 167 ? 0.9840 1.0522 0.9641 -0.0476 -0.0582 -0.0260 236  ASN   D C   
9985  O  O   . ASN   D 167 ? 1.0556 1.1297 1.0420 -0.0482 -0.0568 -0.0250 236  ASN   D O   
9986  C  CB  . ASN   D 167 ? 1.0232 1.0862 0.9984 -0.0406 -0.0517 -0.0281 236  ASN   D CB  
9987  C  CG  . ASN   D 167 ? 1.1262 1.1948 1.1096 -0.0366 -0.0481 -0.0291 236  ASN   D CG  
9988  O  OD1 . ASN   D 167 ? 1.1502 1.2262 1.1431 -0.0362 -0.0455 -0.0286 236  ASN   D OD1 
9989  N  ND2 . ASN   D 167 ? 1.1312 1.1963 1.1117 -0.0338 -0.0480 -0.0307 236  ASN   D ND2 
9990  N  N   . LEU   D 168 ? 0.9465 1.0085 0.9193 -0.0503 -0.0618 -0.0258 237  LEU   D N   
9991  C  CA  . LEU   D 168 ? 0.9677 1.0304 0.9406 -0.0540 -0.0648 -0.0246 237  LEU   D CA  
9992  C  C   . LEU   D 168 ? 0.9268 0.9970 0.9092 -0.0565 -0.0673 -0.0236 237  LEU   D C   
9993  O  O   . LEU   D 168 ? 0.9458 1.0175 0.9296 -0.0596 -0.0699 -0.0225 237  LEU   D O   
9994  C  CB  . LEU   D 168 ? 1.0106 1.0636 0.9726 -0.0558 -0.0681 -0.0250 237  LEU   D CB  
9995  C  CG  . LEU   D 168 ? 0.9774 1.0211 0.9281 -0.0529 -0.0660 -0.0262 237  LEU   D CG  
9996  C  CD1 . LEU   D 168 ? 1.0841 1.1189 1.0265 -0.0543 -0.0696 -0.0272 237  LEU   D CD1 
9997  C  CD2 . LEU   D 168 ? 1.0029 1.0434 0.9477 -0.0526 -0.0650 -0.0255 237  LEU   D CD2 
9998  N  N   . THR   D 169 ? 0.8875 0.9619 0.8760 -0.0550 -0.0666 -0.0241 238  THR   D N   
9999  C  CA  . THR   D 169 ? 0.9554 1.0354 0.9514 -0.0568 -0.0688 -0.0232 238  THR   D CA  
10000 C  C   . THR   D 169 ? 0.9405 1.0292 0.9463 -0.0548 -0.0671 -0.0231 238  THR   D C   
10001 O  O   . THR   D 169 ? 0.9293 1.0200 0.9372 -0.0521 -0.0642 -0.0239 238  THR   D O   
10002 C  CB  . THR   D 169 ? 0.9645 1.0401 0.9577 -0.0568 -0.0702 -0.0237 238  THR   D CB  
10003 O  OG1 . THR   D 169 ? 0.9155 0.9924 0.9106 -0.0529 -0.0682 -0.0249 238  THR   D OG1 
10004 C  CG2 . THR   D 169 ? 0.9340 0.9999 0.9170 -0.0580 -0.0715 -0.0243 238  THR   D CG2 
10005 N  N   . SER   D 170 ? 0.8926 0.9862 0.9047 -0.0560 -0.0688 -0.0223 239  SER   D N   
10006 C  CA  . SER   D 170 ? 0.9040 1.0055 0.9253 -0.0544 -0.0681 -0.0223 239  SER   D CA  
10007 C  C   . SER   D 170 ? 0.8839 0.9861 0.9075 -0.0506 -0.0675 -0.0238 239  SER   D C   
10008 O  O   . SER   D 170 ? 0.9579 1.0662 0.9892 -0.0489 -0.0675 -0.0242 239  SER   D O   
10009 C  CB  . SER   D 170 ? 0.9493 1.0553 0.9756 -0.0569 -0.0702 -0.0207 239  SER   D CB  
10010 O  OG  . SER   D 170 ? 1.0150 1.1169 1.0376 -0.0587 -0.0720 -0.0201 239  SER   D OG  
10011 N  N   . TRP   D 171 ? 0.9212 1.0170 0.9382 -0.0491 -0.0673 -0.0248 240  TRP   D N   
10012 C  CA  . TRP   D 171 ? 0.8887 0.9841 0.9065 -0.0452 -0.0670 -0.0263 240  TRP   D CA  
10013 C  C   . TRP   D 171 ? 0.9049 0.9959 0.9180 -0.0424 -0.0650 -0.0279 240  TRP   D C   
10014 O  O   . TRP   D 171 ? 0.9108 0.9970 0.9175 -0.0437 -0.0640 -0.0277 240  TRP   D O   
10015 C  CB  . TRP   D 171 ? 0.8949 0.9858 0.9086 -0.0456 -0.0688 -0.0258 240  TRP   D CB  
10016 C  CG  . TRP   D 171 ? 0.8916 0.9858 0.9090 -0.0482 -0.0703 -0.0240 240  TRP   D CG  
10017 C  CD1 . TRP   D 171 ? 0.8683 0.9600 0.8833 -0.0522 -0.0713 -0.0224 240  TRP   D CD1 
10018 C  CD2 . TRP   D 171 ? 1.0133 1.1137 1.0379 -0.0468 -0.0711 -0.0238 240  TRP   D CD2 
10019 N  NE1 . TRP   D 171 ? 0.9366 1.0330 0.9570 -0.0533 -0.0723 -0.0209 240  TRP   D NE1 
10020 C  CE2 . TRP   D 171 ? 1.0211 1.1224 1.0468 -0.0500 -0.0721 -0.0218 240  TRP   D CE2 
10021 C  CE3 . TRP   D 171 ? 0.9569 1.0621 0.9874 -0.0431 -0.0712 -0.0253 240  TRP   D CE3 
10022 C  CZ2 . TRP   D 171 ? 1.0444 1.1508 1.0758 -0.0493 -0.0730 -0.0211 240  TRP   D CZ2 
10023 C  CZ3 . TRP   D 171 ? 0.9849 1.0949 1.0210 -0.0426 -0.0725 -0.0248 240  TRP   D CZ3 
10024 C  CH2 . TRP   D 171 ? 1.0316 1.1419 1.0676 -0.0455 -0.0732 -0.0226 240  TRP   D CH2 
10025 N  N   . PRO   D 172 ? 0.9093 1.0016 0.9252 -0.0381 -0.0645 -0.0297 241  PRO   D N   
10026 C  CA  . PRO   D 172 ? 0.9741 1.0631 0.9869 -0.0349 -0.0622 -0.0313 241  PRO   D CA  
10027 C  C   . PRO   D 172 ? 0.9582 1.0386 0.9615 -0.0332 -0.0628 -0.0321 241  PRO   D C   
10028 O  O   . PRO   D 172 ? 0.9286 1.0055 0.9283 -0.0340 -0.0648 -0.0316 241  PRO   D O   
10029 C  CB  . PRO   D 172 ? 0.9589 1.0552 0.9819 -0.0312 -0.0618 -0.0329 241  PRO   D CB  
10030 C  CG  . PRO   D 172 ? 0.9346 1.0332 0.9607 -0.0309 -0.0649 -0.0328 241  PRO   D CG  
10031 C  CD  . PRO   D 172 ? 0.8996 0.9966 0.9222 -0.0356 -0.0662 -0.0305 241  PRO   D CD  
10032 N  N   . ARG   D 173 ? 0.9395 1.0163 0.9390 -0.0304 -0.0606 -0.0335 242  ARG   D N   
10033 C  CA  . ARG   D 173 ? 0.9737 1.0418 0.9637 -0.0284 -0.0609 -0.0344 242  ARG   D CA  
10034 C  C   . ARG   D 173 ? 0.9944 1.0618 0.9850 -0.0258 -0.0630 -0.0351 242  ARG   D C   
10035 O  O   . ARG   D 173 ? 0.9969 1.0573 0.9800 -0.0268 -0.0643 -0.0346 242  ARG   D O   
10036 C  CB  . ARG   D 173 ? 1.0045 1.0706 0.9926 -0.0246 -0.0580 -0.0360 242  ARG   D CB  
10037 C  CG  . ARG   D 173 ? 1.0735 1.1340 1.0539 -0.0265 -0.0560 -0.0353 242  ARG   D CG  
10038 C  CD  . ARG   D 173 ? 1.2123 1.2700 1.1899 -0.0222 -0.0526 -0.0368 242  ARG   D CD  
10039 N  NE  . ARG   D 173 ? 1.3480 1.4061 1.3250 -0.0230 -0.0494 -0.0360 242  ARG   D NE  
10040 C  CZ  . ARG   D 173 ? 1.4439 1.5094 1.4303 -0.0216 -0.0462 -0.0360 242  ARG   D CZ  
10041 N  NH1 . ARG   D 173 ? 1.4001 1.4734 1.3978 -0.0187 -0.0461 -0.0372 242  ARG   D NH1 
10042 N  NH2 . ARG   D 173 ? 1.4289 1.4937 1.4134 -0.0229 -0.0432 -0.0348 242  ARG   D NH2 
10043 N  N   . TRP   D 174 ? 0.9717 1.0458 0.9710 -0.0223 -0.0634 -0.0365 243  TRP   D N   
10044 C  CA  . TRP   D 174 ? 0.9187 0.9909 0.9171 -0.0187 -0.0656 -0.0376 243  TRP   D CA  
10045 C  C   . TRP   D 174 ? 0.9300 1.0006 0.9263 -0.0212 -0.0676 -0.0358 243  TRP   D C   
10046 O  O   . TRP   D 174 ? 0.9681 1.0334 0.9591 -0.0189 -0.0688 -0.0361 243  TRP   D O   
10047 C  CB  . TRP   D 174 ? 0.9910 1.0710 0.9999 -0.0145 -0.0663 -0.0396 243  TRP   D CB  
10048 C  CG  . TRP   D 174 ? 1.0019 1.0916 1.0223 -0.0164 -0.0667 -0.0391 243  TRP   D CG  
10049 C  CD1 . TRP   D 174 ? 0.9923 1.0884 1.0208 -0.0173 -0.0644 -0.0392 243  TRP   D CD1 
10050 C  CD2 . TRP   D 174 ? 0.9336 1.0273 0.9586 -0.0172 -0.0693 -0.0385 243  TRP   D CD2 
10051 N  NE1 . TRP   D 174 ? 0.9916 1.0953 1.0294 -0.0189 -0.0655 -0.0388 243  TRP   D NE1 
10052 C  CE2 . TRP   D 174 ? 0.9838 1.0863 1.0196 -0.0188 -0.0687 -0.0384 243  TRP   D CE2 
10053 C  CE3 . TRP   D 174 ? 0.9405 1.0306 0.9610 -0.0167 -0.0717 -0.0379 243  TRP   D CE3 
10054 C  CZ2 . TRP   D 174 ? 0.9842 1.0918 1.0263 -0.0197 -0.0709 -0.0379 243  TRP   D CZ2 
10055 C  CZ3 . TRP   D 174 ? 0.9453 1.0406 0.9719 -0.0174 -0.0736 -0.0373 243  TRP   D CZ3 
10056 C  CH2 . TRP   D 174 ? 1.0195 1.1235 1.0567 -0.0189 -0.0735 -0.0374 243  TRP   D CH2 
10057 N  N   . LEU   D 175 ? 0.9649 1.0400 0.9654 -0.0256 -0.0677 -0.0340 244  LEU   D N   
10058 C  CA  . LEU   D 175 ? 0.9676 1.0409 0.9660 -0.0284 -0.0690 -0.0321 244  LEU   D CA  
10059 C  C   . LEU   D 175 ? 0.9775 1.0414 0.9659 -0.0306 -0.0686 -0.0311 244  LEU   D C   
10060 O  O   . LEU   D 175 ? 1.0075 1.0655 0.9906 -0.0292 -0.0690 -0.0308 244  LEU   D O   
10061 C  CB  . LEU   D 175 ? 0.9466 1.0265 0.9515 -0.0327 -0.0692 -0.0303 244  LEU   D CB  
10062 C  CG  . LEU   D 175 ? 0.9663 1.0472 0.9726 -0.0337 -0.0706 -0.0288 244  LEU   D CG  
10063 C  CD1 . LEU   D 175 ? 1.0126 1.0879 1.0133 -0.0377 -0.0704 -0.0267 244  LEU   D CD1 
10064 C  CD2 . LEU   D 175 ? 0.9580 1.0366 0.9628 -0.0285 -0.0717 -0.0302 244  LEU   D CD2 
10065 N  N   . TYR   D 176 ? 0.9907 1.0522 0.9759 -0.0338 -0.0677 -0.0306 245  TYR   D N   
10066 C  CA  . TYR   D 176 ? 1.0181 1.0704 0.9943 -0.0363 -0.0678 -0.0298 245  TYR   D CA  
10067 C  C   . TYR   D 176 ? 0.9891 1.0335 0.9578 -0.0323 -0.0674 -0.0311 245  TYR   D C   
10068 O  O   . TYR   D 176 ? 1.0302 1.0669 0.9924 -0.0337 -0.0675 -0.0303 245  TYR   D O   
10069 C  CB  . TYR   D 176 ? 1.0145 1.0648 0.9876 -0.0394 -0.0674 -0.0297 245  TYR   D CB  
10070 C  CG  . TYR   D 176 ? 0.9954 1.0518 0.9743 -0.0436 -0.0682 -0.0282 245  TYR   D CG  
10071 C  CD1 . TYR   D 176 ? 0.9795 1.0344 0.9584 -0.0480 -0.0697 -0.0265 245  TYR   D CD1 
10072 C  CD2 . TYR   D 176 ? 0.9567 1.0203 0.9417 -0.0431 -0.0673 -0.0285 245  TYR   D CD2 
10073 C  CE1 . TYR   D 176 ? 0.9775 1.0381 0.9618 -0.0516 -0.0706 -0.0252 245  TYR   D CE1 
10074 C  CE2 . TYR   D 176 ? 0.8979 0.9665 0.8875 -0.0466 -0.0680 -0.0271 245  TYR   D CE2 
10075 C  CZ  . TYR   D 176 ? 0.9244 0.9916 0.9135 -0.0508 -0.0699 -0.0255 245  TYR   D CZ  
10076 O  OH  . TYR   D 176 ? 0.8908 0.9630 0.8846 -0.0540 -0.0708 -0.0242 245  TYR   D OH  
10077 N  N   . SER   D 177 ? 0.9485 0.9947 0.9185 -0.0273 -0.0668 -0.0332 246  SER   D N   
10078 C  CA  . SER   D 177 ? 0.9989 1.0377 0.9618 -0.0229 -0.0668 -0.0345 246  SER   D CA  
10079 C  C   . SER   D 177 ? 1.0135 1.0496 0.9747 -0.0217 -0.0678 -0.0336 246  SER   D C   
10080 O  O   . SER   D 177 ? 1.0195 1.0463 0.9722 -0.0214 -0.0675 -0.0331 246  SER   D O   
10081 C  CB  . SER   D 177 ? 0.9857 1.0284 0.9523 -0.0174 -0.0664 -0.0369 246  SER   D CB  
10082 O  OG  . SER   D 177 ? 1.0256 1.0683 0.9914 -0.0178 -0.0646 -0.0376 246  SER   D OG  
10083 N  N   . LEU   D 178 ? 0.9780 1.0213 0.9467 -0.0210 -0.0688 -0.0333 247  LEU   D N   
10084 C  CA  . LEU   D 178 ? 1.0140 1.0542 0.9804 -0.0193 -0.0695 -0.0324 247  LEU   D CA  
10085 C  C   . LEU   D 178 ? 0.9934 1.0266 0.9541 -0.0237 -0.0684 -0.0298 247  LEU   D C   
10086 O  O   . LEU   D 178 ? 1.0139 1.0413 0.9697 -0.0219 -0.0680 -0.0289 247  LEU   D O   
10087 C  CB  . LEU   D 178 ? 1.0168 1.0660 0.9923 -0.0185 -0.0709 -0.0323 247  LEU   D CB  
10088 C  CG  . LEU   D 178 ? 0.9637 1.0202 0.9466 -0.0145 -0.0721 -0.0349 247  LEU   D CG  
10089 C  CD1 . LEU   D 178 ? 0.8971 0.9615 0.8885 -0.0141 -0.0738 -0.0348 247  LEU   D CD1 
10090 C  CD2 . LEU   D 178 ? 1.0228 1.0743 1.0009 -0.0082 -0.0731 -0.0373 247  LEU   D CD2 
10091 N  N   . TYR   D 179 ? 0.9621 0.9953 0.9232 -0.0291 -0.0679 -0.0287 248  TYR   D N   
10092 C  CA  . TYR   D 179 ? 0.9745 1.0019 0.9321 -0.0336 -0.0671 -0.0265 248  TYR   D CA  
10093 C  C   . TYR   D 179 ? 1.0481 1.0667 0.9980 -0.0355 -0.0667 -0.0269 248  TYR   D C   
10094 O  O   . TYR   D 179 ? 1.0802 1.0949 1.0289 -0.0403 -0.0666 -0.0253 248  TYR   D O   
10095 C  CB  . TYR   D 179 ? 0.9913 1.0255 0.9565 -0.0389 -0.0675 -0.0246 248  TYR   D CB  
10096 C  CG  . TYR   D 179 ? 1.0101 1.0512 0.9819 -0.0378 -0.0677 -0.0236 248  TYR   D CG  
10097 C  CD1 . TYR   D 179 ? 1.0126 1.0621 0.9907 -0.0352 -0.0688 -0.0249 248  TYR   D CD1 
10098 C  CD2 . TYR   D 179 ? 1.0177 1.0568 0.9897 -0.0393 -0.0667 -0.0213 248  TYR   D CD2 
10099 C  CE1 . TYR   D 179 ? 1.0970 1.1523 1.0808 -0.0341 -0.0693 -0.0242 248  TYR   D CE1 
10100 C  CE2 . TYR   D 179 ? 0.9989 1.0437 0.9761 -0.0379 -0.0668 -0.0203 248  TYR   D CE2 
10101 C  CZ  . TYR   D 179 ? 1.0498 1.1024 1.0325 -0.0353 -0.0684 -0.0219 248  TYR   D CZ  
10102 O  OH  . TYR   D 179 ? 1.0963 1.1538 1.0836 -0.0339 -0.0688 -0.0211 248  TYR   D OH  
10103 N  N   . ASP   D 180 ? 1.0736 1.0889 1.0185 -0.0317 -0.0667 -0.0291 249  ASP   D N   
10104 C  CA  . ASP   D 180 ? 1.0854 1.0925 1.0226 -0.0331 -0.0665 -0.0298 249  ASP   D CA  
10105 C  C   . ASP   D 180 ? 1.0877 1.0838 1.0154 -0.0302 -0.0656 -0.0300 249  ASP   D C   
10106 O  O   . ASP   D 180 ? 1.1108 1.1054 1.0355 -0.0245 -0.0654 -0.0317 249  ASP   D O   
10107 C  CB  . ASP   D 180 ? 1.0784 1.0883 1.0157 -0.0307 -0.0664 -0.0319 249  ASP   D CB  
10108 C  CG  . ASP   D 180 ? 1.1135 1.1136 1.0411 -0.0307 -0.0661 -0.0329 249  ASP   D CG  
10109 O  OD1 . ASP   D 180 ? 1.1542 1.1483 1.0780 -0.0353 -0.0668 -0.0319 249  ASP   D OD1 
10110 O  OD2 . ASP   D 180 ? 1.1348 1.1331 1.0589 -0.0260 -0.0654 -0.0348 249  ASP   D OD2 
10111 N  N   . ALA   D 181 ? 1.0243 1.0126 0.9477 -0.0342 -0.0652 -0.0285 250  ALA   D N   
10112 C  CA  . ALA   D 181 ? 1.0662 1.0430 0.9803 -0.0323 -0.0641 -0.0284 250  ALA   D CA  
10113 C  C   . ALA   D 181 ? 1.1183 1.0901 1.0249 -0.0263 -0.0640 -0.0308 250  ALA   D C   
10114 O  O   . ALA   D 181 ? 1.0839 1.0542 0.9880 -0.0209 -0.0636 -0.0314 250  ALA   D O   
10115 C  CB  . ALA   D 181 ? 1.1328 1.1016 1.0433 -0.0379 -0.0641 -0.0272 250  ALA   D CB  
10116 N  N   . GLU   D 182 ? 1.1469 1.1158 1.0497 -0.0270 -0.0645 -0.0323 251  GLU   D N   
10117 C  CA  . GLU   D 182 ? 1.1567 1.1201 1.0520 -0.0215 -0.0642 -0.0345 251  GLU   D CA  
10118 C  C   . GLU   D 182 ? 1.1200 1.0903 1.0195 -0.0151 -0.0642 -0.0360 251  GLU   D C   
10119 O  O   . GLU   D 182 ? 1.0383 1.0031 0.9318 -0.0096 -0.0640 -0.0373 251  GLU   D O   
10120 C  CB  . GLU   D 182 ? 1.0951 1.0571 0.9877 -0.0231 -0.0646 -0.0358 251  GLU   D CB  
10121 N  N   . THR   D 183 ? 1.1374 1.1198 1.0475 -0.0158 -0.0648 -0.0360 252  THR   D N   
10122 C  CA  . THR   D 183 ? 1.0976 1.0876 1.0137 -0.0103 -0.0653 -0.0374 252  THR   D CA  
10123 C  C   . THR   D 183 ? 1.0676 1.0556 0.9826 -0.0074 -0.0659 -0.0368 252  THR   D C   
10124 O  O   . THR   D 183 ? 1.0308 1.0181 0.9443 -0.0012 -0.0667 -0.0386 252  THR   D O   
10125 C  CB  . THR   D 183 ? 1.0117 1.0143 0.9395 -0.0126 -0.0657 -0.0373 252  THR   D CB  
10126 O  OG1 . THR   D 183 ? 1.1106 1.1144 1.0385 -0.0143 -0.0648 -0.0379 252  THR   D OG1 
10127 C  CG2 . THR   D 183 ? 1.0484 1.0593 0.9839 -0.0074 -0.0666 -0.0390 252  THR   D CG2 
10128 N  N   . LEU   D 184 ? 1.0603 1.0470 0.9757 -0.0114 -0.0655 -0.0343 253  LEU   D N   
10129 C  CA  . LEU   D 184 ? 1.0564 1.0400 0.9693 -0.0082 -0.0655 -0.0335 253  LEU   D CA  
10130 C  C   . LEU   D 184 ? 1.0685 1.0395 0.9695 -0.0041 -0.0648 -0.0340 253  LEU   D C   
10131 O  O   . LEU   D 184 ? 1.0636 1.0324 0.9613 0.0021  -0.0657 -0.0352 253  LEU   D O   
10132 C  CB  . LEU   D 184 ? 1.0887 1.0732 1.0046 -0.0134 -0.0645 -0.0305 253  LEU   D CB  
10133 C  CG  . LEU   D 184 ? 1.0089 1.0059 0.9365 -0.0167 -0.0654 -0.0299 253  LEU   D CG  
10134 C  CD1 . LEU   D 184 ? 1.0031 1.0008 0.9336 -0.0213 -0.0642 -0.0269 253  LEU   D CD1 
10135 C  CD2 . LEU   D 184 ? 1.0491 1.0544 0.9827 -0.0115 -0.0673 -0.0320 253  LEU   D CD2 
10136 N  N   . MET   D 185 ? 1.1185 1.0807 1.0125 -0.0073 -0.0634 -0.0333 254  MET   D N   
10137 C  CA  . MET   D 185 ? 1.0647 1.0139 0.9466 -0.0036 -0.0626 -0.0337 254  MET   D CA  
10138 C  C   . MET   D 185 ? 1.0775 1.0269 0.9568 0.0037  -0.0640 -0.0368 254  MET   D C   
10139 O  O   . MET   D 185 ? 1.0910 1.0333 0.9629 0.0094  -0.0642 -0.0375 254  MET   D O   
10140 C  CB  . MET   D 185 ? 1.0464 0.9869 0.9222 -0.0085 -0.0614 -0.0330 254  MET   D CB  
10141 C  CG  . MET   D 185 ? 1.1053 1.0484 0.9868 -0.0162 -0.0608 -0.0306 254  MET   D CG  
10142 S  SD  . MET   D 185 ? 1.1655 1.0944 1.0386 -0.0210 -0.0591 -0.0289 254  MET   D SD  
10143 C  CE  . MET   D 185 ? 1.2385 1.1644 1.1073 -0.0220 -0.0608 -0.0313 254  MET   D CE  
10144 N  N   . ASP   D 186 ? 1.0588 1.0160 0.9441 0.0038  -0.0648 -0.0387 255  ASP   D N   
10145 C  CA  . ASP   D 186 ? 1.1156 1.0735 0.9998 0.0108  -0.0659 -0.0417 255  ASP   D CA  
10146 C  C   . ASP   D 186 ? 1.1403 1.1038 1.0293 0.0163  -0.0679 -0.0428 255  ASP   D C   
10147 O  O   . ASP   D 186 ? 1.1694 1.1275 1.0526 0.0230  -0.0690 -0.0446 255  ASP   D O   
10148 C  CB  . ASP   D 186 ? 1.1373 1.1025 1.0276 0.0098  -0.0656 -0.0432 255  ASP   D CB  
10149 C  CG  . ASP   D 186 ? 1.2236 1.1873 1.1113 0.0167  -0.0659 -0.0461 255  ASP   D CG  
10150 O  OD1 . ASP   D 186 ? 1.2465 1.1997 1.1237 0.0181  -0.0650 -0.0465 255  ASP   D OD1 
10151 O  OD2 . ASP   D 186 ? 1.2398 1.2129 1.1365 0.0207  -0.0671 -0.0479 255  ASP   D OD2 
10152 N  N   . ARG   D 187 ? 1.0967 1.0704 0.9959 0.0140  -0.0687 -0.0421 256  ARG   D N   
10153 C  CA  . ARG   D 187 ? 1.1371 1.1155 1.0407 0.0190  -0.0711 -0.0432 256  ARG   D CA  
10154 C  C   . ARG   D 187 ? 1.1145 1.0818 1.0071 0.0229  -0.0713 -0.0424 256  ARG   D C   
10155 O  O   . ARG   D 187 ? 1.0869 1.0527 0.9774 0.0299  -0.0737 -0.0444 256  ARG   D O   
10156 C  CB  . ARG   D 187 ? 1.1107 1.1003 1.0257 0.0150  -0.0717 -0.0421 256  ARG   D CB  
10157 C  CG  . ARG   D 187 ? 1.0719 1.0726 0.9979 0.0122  -0.0716 -0.0429 256  ARG   D CG  
10158 C  CD  . ARG   D 187 ? 1.0850 1.0971 1.0228 0.0115  -0.0732 -0.0430 256  ARG   D CD  
10159 N  NE  . ARG   D 187 ? 1.1056 1.1175 1.0432 0.0069  -0.0726 -0.0401 256  ARG   D NE  
10160 C  CZ  . ARG   D 187 ? 1.1973 1.2158 1.1418 0.0069  -0.0741 -0.0397 256  ARG   D CZ  
10161 N  NH1 . ARG   D 187 ? 1.2219 1.2477 1.1741 0.0111  -0.0767 -0.0421 256  ARG   D NH1 
10162 N  NH2 . ARG   D 187 ? 1.2116 1.2294 1.1556 0.0027  -0.0729 -0.0369 256  ARG   D NH2 
10163 N  N   . ILE   D 188 ? 1.0389 0.9978 0.9244 0.0187  -0.0688 -0.0395 257  ILE   D N   
10164 C  CA  . ILE   D 188 ? 1.0832 1.0307 0.9579 0.0222  -0.0680 -0.0383 257  ILE   D CA  
10165 C  C   . ILE   D 188 ? 1.1365 1.0729 0.9997 0.0277  -0.0681 -0.0399 257  ILE   D C   
10166 O  O   . ILE   D 188 ? 1.1485 1.0777 1.0038 0.0342  -0.0692 -0.0406 257  ILE   D O   
10167 C  CB  . ILE   D 188 ? 1.0723 1.0147 0.9443 0.0156  -0.0647 -0.0345 257  ILE   D CB  
10168 C  CG1 . ILE   D 188 ? 0.9216 0.8744 0.8040 0.0120  -0.0649 -0.0330 257  ILE   D CG1 
10169 C  CG2 . ILE   D 188 ? 1.0756 1.0035 0.9344 0.0190  -0.0627 -0.0330 257  ILE   D CG2 
10170 C  CD1 . ILE   D 188 ? 0.9920 0.9400 0.8724 0.0071  -0.0618 -0.0294 257  ILE   D CD1 
10171 N  N   . LYS   D 189 ? 1.1019 1.0359 0.9631 0.0254  -0.0671 -0.0405 258  LYS   D N   
10172 C  CA  . LYS   D 189 ? 1.0842 1.0088 0.9354 0.0309  -0.0674 -0.0424 258  LYS   D CA  
10173 C  C   . LYS   D 189 ? 1.0810 1.0109 0.9357 0.0388  -0.0708 -0.0459 258  LYS   D C   
10174 O  O   . LYS   D 189 ? 1.1282 1.0499 0.9742 0.0457  -0.0721 -0.0471 258  LYS   D O   
10175 C  CB  . LYS   D 189 ? 1.1585 1.0813 1.0085 0.0272  -0.0660 -0.0428 258  LYS   D CB  
10176 C  CG  . LYS   D 189 ? 1.1605 1.0711 1.0008 0.0226  -0.0633 -0.0404 258  LYS   D CG  
10177 C  CD  . LYS   D 189 ? 1.2516 1.1630 1.0934 0.0173  -0.0626 -0.0406 258  LYS   D CD  
10178 C  CE  . LYS   D 189 ? 1.2735 1.1899 1.1176 0.0216  -0.0638 -0.0437 258  LYS   D CE  
10179 N  NZ  . LYS   D 189 ? 1.3638 1.2697 1.1980 0.0217  -0.0628 -0.0444 258  LYS   D NZ  
10180 N  N   . LYS   D 190 ? 1.1245 1.0680 0.9923 0.0381  -0.0723 -0.0475 259  LYS   D N   
10181 C  CA  . LYS   D 190 ? 1.1534 1.1030 1.0268 0.0452  -0.0756 -0.0510 259  LYS   D CA  
10182 C  C   . LYS   D 190 ? 1.1685 1.1142 1.0376 0.0515  -0.0785 -0.0517 259  LYS   D C   
10183 O  O   . LYS   D 190 ? 1.1887 1.1286 1.0516 0.0589  -0.0807 -0.0540 259  LYS   D O   
10184 C  CB  . LYS   D 190 ? 1.1739 1.1393 1.0636 0.0426  -0.0765 -0.0520 259  LYS   D CB  
10185 C  CG  . LYS   D 190 ? 1.2169 1.1860 1.1102 0.0398  -0.0743 -0.0526 259  LYS   D CG  
10186 C  CD  . LYS   D 190 ? 1.4021 1.3853 1.3106 0.0411  -0.0755 -0.0547 259  LYS   D CD  
10187 C  CE  . LYS   D 190 ? 1.5860 1.5720 1.4972 0.0387  -0.0726 -0.0551 259  LYS   D CE  
10188 N  NZ  . LYS   D 190 ? 1.6548 1.6544 1.5814 0.0401  -0.0730 -0.0570 259  LYS   D NZ  
10189 N  N   . GLN   D 191 ? 1.1354 1.0836 1.0071 0.0489  -0.0786 -0.0497 260  GLN   D N   
10190 C  CA  . GLN   D 191 ? 1.1107 1.0543 0.9772 0.0549  -0.0812 -0.0502 260  GLN   D CA  
10191 C  C   . GLN   D 191 ? 1.1796 1.1064 1.0288 0.0589  -0.0799 -0.0493 260  GLN   D C   
10192 O  O   . GLN   D 191 ? 1.2287 1.1496 1.0711 0.0670  -0.0829 -0.0513 260  GLN   D O   
10193 C  CB  . GLN   D 191 ? 1.1471 1.0952 1.0182 0.0507  -0.0806 -0.0478 260  GLN   D CB  
10194 C  CG  . GLN   D 191 ? 1.2049 1.1691 1.0927 0.0475  -0.0824 -0.0488 260  GLN   D CG  
10195 C  CD  . GLN   D 191 ? 1.2171 1.1852 1.1086 0.0477  -0.0840 -0.0479 260  GLN   D CD  
10196 O  OE1 . GLN   D 191 ? 1.2321 1.1950 1.1178 0.0543  -0.0869 -0.0491 260  GLN   D OE1 
10197 N  NE2 . GLN   D 191 ? 1.2140 1.1909 1.1148 0.0407  -0.0824 -0.0459 260  GLN   D NE2 
10198 N  N   . LEU   D 192 ? 1.1616 1.0801 1.0033 0.0535  -0.0754 -0.0462 261  LEU   D N   
10199 C  CA  . LEU   D 192 ? 1.1806 1.0825 1.0059 0.0570  -0.0736 -0.0452 261  LEU   D CA  
10200 C  C   . LEU   D 192 ? 1.2041 1.1010 1.0235 0.0639  -0.0758 -0.0484 261  LEU   D C   
10201 O  O   . LEU   D 192 ? 1.2395 1.1238 1.0458 0.0702  -0.0763 -0.0487 261  LEU   D O   
10202 C  CB  . LEU   D 192 ? 1.1089 1.0037 0.9294 0.0493  -0.0687 -0.0417 261  LEU   D CB  
10203 C  CG  . LEU   D 192 ? 1.1478 1.0457 0.9731 0.0424  -0.0660 -0.0381 261  LEU   D CG  
10204 C  CD1 . LEU   D 192 ? 1.1387 1.0306 0.9612 0.0348  -0.0619 -0.0354 261  LEU   D CD1 
10205 C  CD2 . LEU   D 192 ? 1.0335 0.9241 0.8512 0.0467  -0.0654 -0.0365 261  LEU   D CD2 
10206 N  N   . ARG   D 193 ? 1.2064 1.1121 1.0346 0.0630  -0.0768 -0.0507 262  ARG   D N   
10207 C  CA  . ARG   D 193 ? 1.2352 1.1375 1.0594 0.0699  -0.0789 -0.0539 262  ARG   D CA  
10208 C  C   . ARG   D 193 ? 1.2555 1.1606 1.0817 0.0788  -0.0840 -0.0571 262  ARG   D C   
10209 O  O   . ARG   D 193 ? 1.3000 1.1983 1.1189 0.0862  -0.0861 -0.0595 262  ARG   D O   
10210 C  CB  . ARG   D 193 ? 1.1260 1.0377 0.9599 0.0670  -0.0782 -0.0554 262  ARG   D CB  
10211 N  N   . GLU   D 194 ? 1.2051 1.1197 1.0409 0.0782  -0.0863 -0.0573 263  GLU   D N   
10212 C  CA  . GLU   D 194 ? 1.2713 1.1871 1.1080 0.0866  -0.0917 -0.0602 263  GLU   D CA  
10213 C  C   . GLU   D 194 ? 1.2739 1.1728 1.0923 0.0928  -0.0921 -0.0595 263  GLU   D C   
10214 O  O   . GLU   D 194 ? 1.2032 1.0979 1.0169 0.1017  -0.0965 -0.0626 263  GLU   D O   
10215 C  CB  . GLU   D 194 ? 1.2491 1.1768 1.0983 0.0839  -0.0937 -0.0601 263  GLU   D CB  
10216 C  CG  . GLU   D 194 ? 1.2508 1.1951 1.1185 0.0817  -0.0954 -0.0624 263  GLU   D CG  
10217 C  CD  . GLU   D 194 ? 1.4905 1.4400 1.3650 0.0900  -0.1015 -0.0670 263  GLU   D CD  
10218 O  OE1 . GLU   D 194 ? 1.5590 1.5100 1.4352 0.0934  -0.1057 -0.0681 263  GLU   D OE1 
10219 O  OE2 . GLU   D 194 ? 1.5310 1.4827 1.4088 0.0934  -0.1024 -0.0696 263  GLU   D OE2 
10220 N  N   . TRP   D 195 ? 1.2860 1.1752 1.0944 0.0884  -0.0875 -0.0554 264  TRP   D N   
10221 C  CA  . TRP   D 195 ? 1.2805 1.1524 1.0707 0.0931  -0.0863 -0.0538 264  TRP   D CA  
10222 C  C   . TRP   D 195 ? 1.3561 1.2146 1.1331 0.0950  -0.0838 -0.0535 264  TRP   D C   
10223 O  O   . TRP   D 195 ? 1.4023 1.2451 1.1631 0.0989  -0.0821 -0.0519 264  TRP   D O   
10224 C  CB  . TRP   D 195 ? 1.2697 1.1376 1.0565 0.0869  -0.0816 -0.0492 264  TRP   D CB  
10225 C  CG  . TRP   D 195 ? 1.2406 1.1195 1.0380 0.0855  -0.0836 -0.0491 264  TRP   D CG  
10226 C  CD1 . TRP   D 195 ? 1.2082 1.0972 1.0150 0.0903  -0.0896 -0.0528 264  TRP   D CD1 
10227 C  CD2 . TRP   D 195 ? 1.1580 1.0389 0.9582 0.0789  -0.0799 -0.0453 264  TRP   D CD2 
10228 N  NE1 . TRP   D 195 ? 1.2237 1.1204 1.0383 0.0871  -0.0898 -0.0515 264  TRP   D NE1 
10229 C  CE2 . TRP   D 195 ? 1.1902 1.0822 1.0007 0.0802  -0.0838 -0.0469 264  TRP   D CE2 
10230 C  CE3 . TRP   D 195 ? 1.1318 1.0063 0.9274 0.0721  -0.0737 -0.0409 264  TRP   D CE3 
10231 C  CZ2 . TRP   D 195 ? 1.2612 1.1577 1.0766 0.0752  -0.0816 -0.0440 264  TRP   D CZ2 
10232 C  CZ3 . TRP   D 195 ? 1.1422 1.0218 0.9436 0.0670  -0.0715 -0.0380 264  TRP   D CZ3 
10233 C  CH2 . TRP   D 195 ? 1.2054 1.0959 1.0163 0.0687  -0.0754 -0.0396 264  TRP   D CH2 
10234 N  N   . ASP   D 196 ? 1.3595 1.2230 1.1422 0.0922  -0.0831 -0.0547 265  ASP   D N   
10235 C  CA  . ASP   D 196 ? 1.4277 1.2776 1.1972 0.0929  -0.0802 -0.0539 265  ASP   D CA  
10236 C  C   . ASP   D 196 ? 1.5339 1.3910 1.3111 0.0901  -0.0798 -0.0556 265  ASP   D C   
10237 O  O   . ASP   D 196 ? 1.4940 1.3618 1.2828 0.0824  -0.0781 -0.0546 265  ASP   D O   
10238 C  CB  . ASP   D 196 ? 1.4394 1.2786 1.2000 0.0864  -0.0745 -0.0492 265  ASP   D CB  
10239 C  CG  . ASP   D 196 ? 1.4321 1.2572 1.1798 0.0861  -0.0713 -0.0482 265  ASP   D CG  
10240 O  OD1 . ASP   D 196 ? 1.4925 1.3144 1.2359 0.0922  -0.0737 -0.0512 265  ASP   D OD1 
10241 O  OD2 . ASP   D 196 ? 1.4532 1.2704 1.1957 0.0796  -0.0665 -0.0446 265  ASP   D OD2 
10242 N  N   . GLU   D 197 ? 1.6134 1.4640 1.3835 0.0965  -0.0812 -0.0581 266  GLU   D N   
10243 C  CA  . GLU   D 197 ? 1.6455 1.4992 1.4192 0.0945  -0.0800 -0.0593 266  GLU   D CA  
10244 C  C   . GLU   D 197 ? 1.6389 1.4794 1.4006 0.0890  -0.0751 -0.0562 266  GLU   D C   
10245 O  O   . GLU   D 197 ? 1.5650 1.3912 1.3125 0.0930  -0.0742 -0.0563 266  GLU   D O   
10246 C  CB  . GLU   D 197 ? 1.7039 1.5569 1.4761 0.1039  -0.0837 -0.0634 266  GLU   D CB  
10247 C  CG  . GLU   D 197 ? 1.7325 1.6010 1.5203 0.1081  -0.0887 -0.0667 266  GLU   D CG  
10248 C  CD  . GLU   D 197 ? 1.8209 1.7059 1.6264 0.1031  -0.0878 -0.0676 266  GLU   D CD  
10249 O  OE1 . GLU   D 197 ? 1.9357 1.8322 1.7537 0.1075  -0.0914 -0.0710 266  GLU   D OE1 
10250 O  OE2 . GLU   D 197 ? 1.7699 1.6560 1.5766 0.0948  -0.0836 -0.0650 266  GLU   D OE2 
10251 N  N   . ASN   D 198 ? 1.6927 1.5381 1.4608 0.0795  -0.0721 -0.0534 267  ASN   D N   
10252 C  CA  . ASN   D 198 ? 1.6900 1.5253 1.4505 0.0724  -0.0677 -0.0501 267  ASN   D CA  
10253 C  C   . ASN   D 198 ? 1.7244 1.5656 1.4914 0.0663  -0.0664 -0.0505 267  ASN   D C   
10254 O  O   . ASN   D 198 ? 1.7606 1.6143 1.5385 0.0672  -0.0682 -0.0528 267  ASN   D O   
10255 C  CB  . ASN   D 198 ? 1.6624 1.4986 1.4254 0.0665  -0.0656 -0.0466 267  ASN   D CB  
10256 N  N   . LEU   D 199 ? 1.6514 1.4832 1.4116 0.0601  -0.0632 -0.0481 268  LEU   D N   
10257 C  CA  . LEU   D 199 ? 1.6240 1.4585 1.3877 0.0544  -0.0621 -0.0483 268  LEU   D CA  
10258 C  C   . LEU   D 199 ? 1.6507 1.4961 1.4265 0.0457  -0.0613 -0.0464 268  LEU   D C   
10259 O  O   . LEU   D 199 ? 1.6250 1.4695 1.4019 0.0419  -0.0601 -0.0437 268  LEU   D O   
10260 C  CB  . LEU   D 199 ? 1.5728 1.3907 1.3228 0.0524  -0.0598 -0.0471 268  LEU   D CB  
10261 N  N   . LYS   D 200 ? 1.6500 1.5056 1.4348 0.0428  -0.0619 -0.0476 269  LYS   D N   
10262 C  CA  . LYS   D 200 ? 1.5419 1.4067 1.3370 0.0345  -0.0612 -0.0459 269  LYS   D CA  
10263 C  C   . LYS   D 200 ? 1.5831 1.4385 1.3722 0.0275  -0.0595 -0.0442 269  LYS   D C   
10264 O  O   . LYS   D 200 ? 1.5844 1.4463 1.3811 0.0205  -0.0593 -0.0431 269  LYS   D O   
10265 C  CB  . LYS   D 200 ? 1.4291 1.3082 1.2358 0.0347  -0.0624 -0.0480 269  LYS   D CB  
10266 N  N   . ASP   D 201 ? 1.6001 1.4403 1.3759 0.0294  -0.0584 -0.0441 270  ASP   D N   
10267 C  CA  . ASP   D 201 ? 1.6854 1.5145 1.4543 0.0234  -0.0571 -0.0427 270  ASP   D CA  
10268 C  C   . ASP   D 201 ? 1.7186 1.5426 1.4875 0.0180  -0.0552 -0.0394 270  ASP   D C   
10269 O  O   . ASP   D 201 ? 1.6262 1.4588 1.4033 0.0170  -0.0550 -0.0380 270  ASP   D O   
10270 C  CB  . ASP   D 201 ? 1.7088 1.5238 1.4636 0.0286  -0.0568 -0.0443 270  ASP   D CB  
10271 C  CG  . ASP   D 201 ? 1.7939 1.5965 1.5410 0.0229  -0.0559 -0.0435 270  ASP   D CG  
10272 O  OD1 . ASP   D 201 ? 1.8165 1.6189 1.5625 0.0215  -0.0568 -0.0451 270  ASP   D OD1 
10273 O  OD2 . ASP   D 201 ? 1.8678 1.6600 1.6094 0.0201  -0.0542 -0.0412 270  ASP   D OD2 
10274 N  N   . ASP   D 202 ? 1.9801 1.7899 1.7399 0.0146  -0.0536 -0.0381 271  ASP   D N   
10275 C  CA  . ASP   D 202 ? 1.9977 1.8005 1.7568 0.0091  -0.0510 -0.0347 271  ASP   D CA  
10276 C  C   . ASP   D 202 ? 1.9800 1.7877 1.7430 0.0116  -0.0497 -0.0329 271  ASP   D C   
10277 O  O   . ASP   D 202 ? 1.9621 1.7718 1.7312 0.0061  -0.0478 -0.0301 271  ASP   D O   
10278 C  CB  . ASP   D 202 ? 2.0377 1.8216 1.7824 0.0102  -0.0491 -0.0342 271  ASP   D CB  
10279 N  N   . SER   D 203 ? 1.6617 1.4707 1.4209 0.0202  -0.0508 -0.0347 272  SER   D N   
10280 C  CA  . SER   D 203 ? 1.5268 1.3410 1.2888 0.0243  -0.0507 -0.0338 272  SER   D CA  
10281 C  C   . SER   D 203 ? 1.5200 1.3447 1.2944 0.0176  -0.0498 -0.0315 272  SER   D C   
10282 O  O   . SER   D 203 ? 1.5198 1.3396 1.2929 0.0157  -0.0469 -0.0285 272  SER   D O   
10283 C  CB  . SER   D 203 ? 1.5223 1.3455 1.2869 0.0321  -0.0540 -0.0372 272  SER   D CB  
10284 O  OG  . SER   D 203 ? 1.5798 1.4114 1.3508 0.0304  -0.0560 -0.0395 272  SER   D OG  
10285 N  N   . LEU   D 204 ? 1.4737 1.3122 1.2600 0.0137  -0.0519 -0.0326 273  LEU   D N   
10286 C  CA  . LEU   D 204 ? 1.3177 1.1674 1.1163 0.0080  -0.0516 -0.0307 273  LEU   D CA  
10287 C  C   . LEU   D 204 ? 1.2727 1.1245 1.0775 -0.0011 -0.0515 -0.0297 273  LEU   D C   
10288 O  O   . LEU   D 204 ? 1.2564 1.1093 1.0611 -0.0021 -0.0534 -0.0318 273  LEU   D O   
10289 C  CB  . LEU   D 204 ? 1.3342 1.1993 1.1427 0.0112  -0.0544 -0.0326 273  LEU   D CB  
10290 C  CG  . LEU   D 204 ? 1.2473 1.1143 1.0545 0.0185  -0.0552 -0.0331 273  LEU   D CG  
10291 C  CD1 . LEU   D 204 ? 1.1906 1.0539 0.9969 0.0168  -0.0524 -0.0298 273  LEU   D CD1 
10292 C  CD2 . LEU   D 204 ? 1.3249 1.1815 1.1200 0.0264  -0.0558 -0.0352 273  LEU   D CD2 
10293 N  N   . PRO   D 205 ? 1.2263 1.0788 1.0367 -0.0074 -0.0495 -0.0267 274  PRO   D N   
10294 C  CA  . PRO   D 205 ? 1.2288 1.0839 1.0463 -0.0160 -0.0500 -0.0260 274  PRO   D CA  
10295 C  C   . PRO   D 205 ? 1.2476 1.1160 1.0739 -0.0175 -0.0533 -0.0281 274  PRO   D C   
10296 O  O   . PRO   D 205 ? 1.2776 1.1560 1.1084 -0.0132 -0.0546 -0.0294 274  PRO   D O   
10297 C  CB  . PRO   D 205 ? 1.1591 1.0166 0.9840 -0.0210 -0.0474 -0.0225 274  PRO   D CB  
10298 C  CG  . PRO   D 205 ? 1.1909 1.0404 1.0079 -0.0156 -0.0444 -0.0210 274  PRO   D CG  
10299 C  CD  . PRO   D 205 ? 1.2764 1.1269 1.0870 -0.0067 -0.0465 -0.0238 274  PRO   D CD  
10300 N  N   . SER   D 206 ? 1.3185 1.1863 1.1473 -0.0236 -0.0547 -0.0284 275  SER   D N   
10301 C  CA  . SER   D 206 ? 1.3230 1.2014 1.1585 -0.0251 -0.0575 -0.0302 275  SER   D CA  
10302 C  C   . SER   D 206 ? 1.2499 1.1389 1.0980 -0.0315 -0.0581 -0.0285 275  SER   D C   
10303 O  O   . SER   D 206 ? 1.2593 1.1604 1.1151 -0.0309 -0.0594 -0.0292 275  SER   D O   
10304 C  CB  . SER   D 206 ? 1.3267 1.1975 1.1555 -0.0267 -0.0592 -0.0321 275  SER   D CB  
10305 O  OG  . SER   D 206 ? 1.4201 1.2859 1.2508 -0.0342 -0.0598 -0.0308 275  SER   D OG  
10306 N  N   . ASN   D 207 ? 1.2161 1.1005 1.0667 -0.0376 -0.0571 -0.0262 276  ASN   D N   
10307 C  CA  . ASN   D 207 ? 1.1800 1.0741 1.0429 -0.0434 -0.0574 -0.0244 276  ASN   D CA  
10308 C  C   . ASN   D 207 ? 1.2284 1.1310 1.0965 -0.0400 -0.0557 -0.0230 276  ASN   D C   
10309 O  O   . ASN   D 207 ? 1.2482 1.1448 1.1106 -0.0359 -0.0530 -0.0219 276  ASN   D O   
10310 C  CB  . ASN   D 207 ? 1.2510 1.1379 1.1161 -0.0499 -0.0561 -0.0221 276  ASN   D CB  
10311 C  CG  . ASN   D 207 ? 1.2428 1.1398 1.1211 -0.0553 -0.0559 -0.0200 276  ASN   D CG  
10312 O  OD1 . ASN   D 207 ? 1.2682 1.1725 1.1512 -0.0531 -0.0541 -0.0185 276  ASN   D OD1 
10313 N  ND2 . ASN   D 207 ? 1.3464 1.2436 1.2307 -0.0622 -0.0582 -0.0199 276  ASN   D ND2 
10314 N  N   . PRO   D 208 ? 1.2127 1.1286 1.0908 -0.0412 -0.0572 -0.0231 277  PRO   D N   
10315 C  CA  . PRO   D 208 ? 1.2062 1.1299 1.0886 -0.0375 -0.0559 -0.0222 277  PRO   D CA  
10316 C  C   . PRO   D 208 ? 1.1933 1.1149 1.0787 -0.0398 -0.0528 -0.0189 277  PRO   D C   
10317 O  O   . PRO   D 208 ? 1.1699 1.0926 1.0540 -0.0352 -0.0511 -0.0180 277  PRO   D O   
10318 C  CB  . PRO   D 208 ? 1.1814 1.1190 1.0738 -0.0392 -0.0584 -0.0231 277  PRO   D CB  
10319 C  CG  . PRO   D 208 ? 1.1804 1.1164 1.0713 -0.0421 -0.0608 -0.0248 277  PRO   D CG  
10320 C  CD  . PRO   D 208 ? 1.1932 1.1172 1.0787 -0.0459 -0.0601 -0.0239 277  PRO   D CD  
10321 N  N   . ILE   D 209 ? 1.1727 1.0912 1.0621 -0.0466 -0.0520 -0.0170 278  ILE   D N   
10322 C  CA  . ILE   D 209 ? 1.1642 1.0785 1.0554 -0.0484 -0.0479 -0.0137 278  ILE   D CA  
10323 C  C   . ILE   D 209 ? 1.2138 1.1157 1.0926 -0.0428 -0.0448 -0.0132 278  ILE   D C   
10324 O  O   . ILE   D 209 ? 1.2566 1.1584 1.1332 -0.0382 -0.0424 -0.0118 278  ILE   D O   
10325 C  CB  . ILE   D 209 ? 1.1291 1.0406 1.0266 -0.0566 -0.0476 -0.0121 278  ILE   D CB  
10326 C  CG1 . ILE   D 209 ? 1.2446 1.1686 1.1544 -0.0618 -0.0508 -0.0124 278  ILE   D CG1 
10327 C  CG2 . ILE   D 209 ? 1.1417 1.0487 1.0414 -0.0582 -0.0426 -0.0084 278  ILE   D CG2 
10328 C  CD1 . ILE   D 209 ? 1.2703 1.1963 1.1787 -0.0629 -0.0557 -0.0157 278  ILE   D CD1 
10329 N  N   . ASP   D 210 ? 1.2102 1.1011 1.0801 -0.0424 -0.0451 -0.0144 279  ASP   D N   
10330 C  CA  . ASP   D 210 ? 1.2096 1.0872 1.0672 -0.0374 -0.0419 -0.0137 279  ASP   D CA  
10331 C  C   . ASP   D 210 ? 1.1991 1.0782 1.0500 -0.0285 -0.0428 -0.0154 279  ASP   D C   
10332 O  O   . ASP   D 210 ? 1.2080 1.0794 1.0509 -0.0235 -0.0399 -0.0142 279  ASP   D O   
10333 C  CB  . ASP   D 210 ? 1.2048 1.0704 1.0542 -0.0389 -0.0425 -0.0149 279  ASP   D CB  
10334 C  CG  . ASP   D 210 ? 1.2740 1.1377 1.1306 -0.0478 -0.0424 -0.0135 279  ASP   D CG  
10335 O  OD1 . ASP   D 210 ? 1.2850 1.1499 1.1489 -0.0517 -0.0392 -0.0104 279  ASP   D OD1 
10336 O  OD2 . ASP   D 210 ? 1.3552 1.2160 1.2102 -0.0506 -0.0455 -0.0157 279  ASP   D OD2 
10337 N  N   . PHE   D 211 ? 1.2014 1.0899 1.0553 -0.0263 -0.0467 -0.0184 280  PHE   D N   
10338 C  CA  . PHE   D 211 ? 1.1718 1.0632 1.0216 -0.0182 -0.0480 -0.0203 280  PHE   D CA  
10339 C  C   . PHE   D 211 ? 1.1862 1.0840 1.0407 -0.0161 -0.0469 -0.0186 280  PHE   D C   
10340 O  O   . PHE   D 211 ? 1.2016 1.0950 1.0490 -0.0092 -0.0462 -0.0188 280  PHE   D O   
10341 C  CB  . PHE   D 211 ? 1.1552 1.0559 1.0090 -0.0170 -0.0519 -0.0236 280  PHE   D CB  
10342 C  CG  . PHE   D 211 ? 1.1676 1.0721 1.0191 -0.0089 -0.0538 -0.0260 280  PHE   D CG  
10343 C  CD1 . PHE   D 211 ? 1.1494 1.0639 1.0080 -0.0066 -0.0546 -0.0258 280  PHE   D CD1 
10344 C  CD2 . PHE   D 211 ? 1.1276 1.0263 0.9709 -0.0037 -0.0550 -0.0286 280  PHE   D CD2 
10345 C  CE1 . PHE   D 211 ? 1.1118 1.0302 0.9696 0.0007  -0.0568 -0.0284 280  PHE   D CE1 
10346 C  CE2 . PHE   D 211 ? 1.1540 1.0571 0.9968 0.0038  -0.0570 -0.0311 280  PHE   D CE2 
10347 C  CZ  . PHE   D 211 ? 1.1365 1.0496 0.9870 0.0059  -0.0581 -0.0310 280  PHE   D CZ  
10348 N  N   . SER   D 212 ? 1.1358 1.0433 1.0017 -0.0216 -0.0467 -0.0170 281  SER   D N   
10349 C  CA  . SER   D 212 ? 1.1385 1.0514 1.0085 -0.0196 -0.0454 -0.0153 281  SER   D CA  
10350 C  C   . SER   D 212 ? 1.1651 1.0658 1.0262 -0.0169 -0.0409 -0.0125 281  SER   D C   
10351 O  O   . SER   D 212 ? 1.1326 1.0317 0.9888 -0.0106 -0.0404 -0.0124 281  SER   D O   
10352 C  CB  . SER   D 212 ? 1.1329 1.0567 1.0161 -0.0263 -0.0454 -0.0136 281  SER   D CB  
10353 O  OG  . SER   D 212 ? 1.1623 1.0803 1.0473 -0.0326 -0.0423 -0.0109 281  SER   D OG  
10354 N  N   . TYR   D 213 ? 1.1736 1.0649 1.0323 -0.0216 -0.0376 -0.0103 282  TYR   D N   
10355 C  CA  . TYR   D 213 ? 1.1608 1.0400 1.0114 -0.0195 -0.0324 -0.0072 282  TYR   D CA  
10356 C  C   . TYR   D 213 ? 1.1387 1.0054 0.9740 -0.0118 -0.0321 -0.0086 282  TYR   D C   
10357 O  O   . TYR   D 213 ? 1.1225 0.9805 0.9492 -0.0069 -0.0288 -0.0067 282  TYR   D O   
10358 C  CB  . TYR   D 213 ? 1.1707 1.0437 1.0247 -0.0271 -0.0285 -0.0043 282  TYR   D CB  
10359 C  CG  . TYR   D 213 ? 1.1483 1.0324 1.0174 -0.0343 -0.0280 -0.0023 282  TYR   D CG  
10360 C  CD1 . TYR   D 213 ? 1.1416 1.0305 1.0150 -0.0332 -0.0252 0.0001  282  TYR   D CD1 
10361 C  CD2 . TYR   D 213 ? 1.1763 1.0654 1.0547 -0.0419 -0.0303 -0.0030 282  TYR   D CD2 
10362 C  CE1 . TYR   D 213 ? 1.1522 1.0512 1.0395 -0.0395 -0.0247 0.0019  282  TYR   D CE1 
10363 C  CE2 . TYR   D 213 ? 1.1739 1.0729 1.0660 -0.0482 -0.0302 -0.0014 282  TYR   D CE2 
10364 C  CZ  . TYR   D 213 ? 1.1837 1.0879 1.0806 -0.0470 -0.0273 0.0011  282  TYR   D CZ  
10365 O  OH  . TYR   D 213 ? 1.2649 1.1791 1.1757 -0.0531 -0.0271 0.0027  282  TYR   D OH  
10366 N  N   . ARG   D 214 ? 1.1546 1.0199 0.9858 -0.0102 -0.0356 -0.0118 283  ARG   D N   
10367 C  CA  . ARG   D 214 ? 1.2063 1.0607 1.0234 -0.0022 -0.0360 -0.0134 283  ARG   D CA  
10368 C  C   . ARG   D 214 ? 1.2053 1.0645 1.0203 0.0059  -0.0384 -0.0150 283  ARG   D C   
10369 O  O   . ARG   D 214 ? 1.2054 1.0543 1.0089 0.0127  -0.0369 -0.0146 283  ARG   D O   
10370 C  CB  . ARG   D 214 ? 1.2129 1.0659 1.0272 -0.0023 -0.0393 -0.0166 283  ARG   D CB  
10371 C  CG  . ARG   D 214 ? 1.2564 1.1002 1.0575 0.0065  -0.0405 -0.0189 283  ARG   D CG  
10372 C  CD  . ARG   D 214 ? 1.3253 1.1515 1.1136 0.0078  -0.0361 -0.0165 283  ARG   D CD  
10373 N  NE  . ARG   D 214 ? 1.3502 1.1698 1.1373 0.0020  -0.0353 -0.0164 283  ARG   D NE  
10374 C  CZ  . ARG   D 214 ? 1.4009 1.2168 1.1822 0.0041  -0.0379 -0.0193 283  ARG   D CZ  
10375 N  NH1 . ARG   D 214 ? 1.3993 1.2175 1.1762 0.0119  -0.0412 -0.0224 283  ARG   D NH1 
10376 N  NH2 . ARG   D 214 ? 1.3533 1.1630 1.1338 -0.0015 -0.0374 -0.0192 283  ARG   D NH2 
10377 N  N   . VAL   D 215 ? 1.2039 1.0782 1.0300 0.0052  -0.0421 -0.0169 284  VAL   D N   
10378 C  CA  . VAL   D 215 ? 1.1122 0.9924 0.9384 0.0123  -0.0451 -0.0188 284  VAL   D CA  
10379 C  C   . VAL   D 215 ? 1.1024 0.9795 0.9263 0.0141  -0.0420 -0.0158 284  VAL   D C   
10380 O  O   . VAL   D 215 ? 1.1392 1.0122 0.9555 0.0219  -0.0431 -0.0167 284  VAL   D O   
10381 C  CB  . VAL   D 215 ? 1.1157 1.0126 0.9554 0.0099  -0.0493 -0.0211 284  VAL   D CB  
10382 C  CG1 . VAL   D 215 ? 1.0774 0.9810 0.9185 0.0172  -0.0531 -0.0237 284  VAL   D CG1 
10383 C  CG2 . VAL   D 215 ? 1.1588 1.0571 0.9998 0.0075  -0.0512 -0.0235 284  VAL   D CG2 
10384 N  N   . ALA   D 216 ? 1.0626 0.9417 0.8932 0.0073  -0.0383 -0.0124 285  ALA   D N   
10385 C  CA  . ALA   D 216 ? 1.0954 0.9698 0.9225 0.0094  -0.0343 -0.0092 285  ALA   D CA  
10386 C  C   . ALA   D 216 ? 1.2060 1.0628 1.0163 0.0157  -0.0311 -0.0080 285  ALA   D C   
10387 O  O   . ALA   D 216 ? 1.2273 1.0789 1.0297 0.0224  -0.0303 -0.0074 285  ALA   D O   
10388 C  CB  . ALA   D 216 ? 1.1207 0.9979 0.9571 0.0008  -0.0298 -0.0053 285  ALA   D CB  
10389 N  N   . ALA   D 217 ? 1.2575 1.1044 1.0615 0.0139  -0.0295 -0.0079 286  ALA   D N   
10390 C  CA  . ALA   D 217 ? 1.1713 1.0003 0.9591 0.0190  -0.0258 -0.0065 286  ALA   D CA  
10391 C  C   . ALA   D 217 ? 1.1412 0.9645 0.9170 0.0290  -0.0299 -0.0100 286  ALA   D C   
10392 O  O   . ALA   D 217 ? 1.2808 1.0896 1.0421 0.0353  -0.0273 -0.0088 286  ALA   D O   
10393 C  CB  . ALA   D 217 ? 1.1814 1.0020 0.9677 0.0130  -0.0226 -0.0051 286  ALA   D CB  
10394 N  N   . CYS   D 218 ? 1.1661 1.0001 0.9478 0.0308  -0.0361 -0.0141 287  CYS   D N   
10395 C  CA  . CYS   D 218 ? 1.1828 1.0125 0.9550 0.0401  -0.0404 -0.0177 287  CYS   D CA  
10396 C  C   . CYS   D 218 ? 1.2206 1.0573 0.9945 0.0468  -0.0446 -0.0198 287  CYS   D C   
10397 O  O   . CYS   D 218 ? 1.2985 1.1285 1.0622 0.0557  -0.0476 -0.0221 287  CYS   D O   
10398 C  CB  . CYS   D 218 ? 1.2585 1.0937 1.0350 0.0387  -0.0442 -0.0212 287  CYS   D CB  
10399 S  SG  . CYS   D 218 ? 1.7494 1.5726 1.5203 0.0323  -0.0400 -0.0193 287  CYS   D SG  
10400 N  N   . LEU   D 219 ? 1.1897 1.0388 0.9756 0.0431  -0.0452 -0.0190 288  LEU   D N   
10401 C  CA  . LEU   D 219 ? 1.1502 1.0063 0.9386 0.0489  -0.0494 -0.0210 288  LEU   D CA  
10402 C  C   . LEU   D 219 ? 1.1983 1.0412 0.9725 0.0560  -0.0472 -0.0192 288  LEU   D C   
10403 O  O   . LEU   D 219 ? 1.2238 1.0577 0.9925 0.0534  -0.0408 -0.0149 288  LEU   D O   
10404 C  CB  . LEU   D 219 ? 1.1286 1.0005 0.9331 0.0425  -0.0500 -0.0203 288  LEU   D CB  
10405 C  CG  . LEU   D 219 ? 1.1253 1.0123 0.9431 0.0399  -0.0550 -0.0238 288  LEU   D CG  
10406 C  CD1 . LEU   D 219 ? 1.1047 0.9872 0.9189 0.0392  -0.0553 -0.0254 288  LEU   D CD1 
10407 C  CD2 . LEU   D 219 ? 1.1158 1.0173 0.9495 0.0314  -0.0545 -0.0226 288  LEU   D CD2 
10408 N  N   . PRO   D 220 ? 1.1590 1.0005 0.9273 0.0652  -0.0523 -0.0223 289  PRO   D N   
10409 C  CA  . PRO   D 220 ? 1.1605 0.9896 0.9148 0.0728  -0.0509 -0.0208 289  PRO   D CA  
10410 C  C   . PRO   D 220 ? 1.2088 1.0450 0.9700 0.0706  -0.0496 -0.0187 289  PRO   D C   
10411 O  O   . PRO   D 220 ? 1.1219 0.9608 0.8822 0.0768  -0.0542 -0.0209 289  PRO   D O   
10412 C  CB  . PRO   D 220 ? 1.1437 0.9710 0.8918 0.0829  -0.0583 -0.0257 289  PRO   D CB  
10413 C  CG  . PRO   D 220 ? 1.1695 1.0152 0.9352 0.0794  -0.0639 -0.0294 289  PRO   D CG  
10414 C  CD  . PRO   D 220 ? 1.1452 0.9972 0.9208 0.0689  -0.0598 -0.0274 289  PRO   D CD  
10415 N  N   . ILE   D 221 ? 1.2046 1.0438 0.9730 0.0619  -0.0436 -0.0146 290  ILE   D N   
10416 C  CA  . ILE   D 221 ? 1.1591 1.0053 0.9348 0.0590  -0.0415 -0.0122 290  ILE   D CA  
10417 C  C   . ILE   D 221 ? 1.1747 1.0061 0.9383 0.0604  -0.0337 -0.0073 290  ILE   D C   
10418 O  O   . ILE   D 221 ? 1.1375 0.9557 0.8911 0.0604  -0.0289 -0.0052 290  ILE   D O   
10419 C  CB  . ILE   D 221 ? 1.1612 1.0229 0.9555 0.0482  -0.0405 -0.0111 290  ILE   D CB  
10420 C  CG1 . ILE   D 221 ? 1.2383 1.0948 1.0330 0.0410  -0.0349 -0.0083 290  ILE   D CG1 
10421 C  CG2 . ILE   D 221 ? 1.1333 1.0096 0.9397 0.0468  -0.0474 -0.0156 290  ILE   D CG2 
10422 C  CD1 . ILE   D 221 ? 1.2364 1.1075 1.0480 0.0316  -0.0361 -0.0088 290  ILE   D CD1 
10423 N  N   . ASP   D 222 ? 1.2164 1.0499 0.9810 0.0618  -0.0323 -0.0055 291  ASP   D N   
10424 C  CA  . ASP   D 222 ? 1.2554 1.0763 1.0099 0.0633  -0.0245 -0.0006 291  ASP   D CA  
10425 C  C   . ASP   D 222 ? 1.2514 1.0778 1.0181 0.0525  -0.0177 0.0036  291  ASP   D C   
10426 O  O   . ASP   D 222 ? 1.2516 1.0918 1.0339 0.0446  -0.0199 0.0025  291  ASP   D O   
10427 C  CB  . ASP   D 222 ? 1.2415 1.0622 0.9917 0.0697  -0.0262 -0.0008 291  ASP   D CB  
10428 C  CG  . ASP   D 222 ? 1.3130 1.1512 1.0810 0.0633  -0.0275 -0.0006 291  ASP   D CG  
10429 O  OD1 . ASP   D 222 ? 1.2856 1.1388 1.0686 0.0577  -0.0323 -0.0033 291  ASP   D OD1 
10430 O  OD2 . ASP   D 222 ? 1.3563 1.1930 1.1232 0.0640  -0.0234 0.0025  291  ASP   D OD2 
10431 N  N   . ASP   D 223 ? 1.2547 1.0704 1.0147 0.0523  -0.0093 0.0086  292  ASP   D N   
10432 C  CA  . ASP   D 223 ? 1.2488 1.0680 1.0202 0.0422  -0.0026 0.0126  292  ASP   D CA  
10433 C  C   . ASP   D 223 ? 1.1993 1.0370 0.9897 0.0353  -0.0045 0.0126  292  ASP   D C   
10434 O  O   . ASP   D 223 ? 1.1521 0.9993 0.9567 0.0261  -0.0041 0.0130  292  ASP   D O   
10435 C  CB  . ASP   D 223 ? 1.3181 1.1216 1.0789 0.0437  0.0073  0.0181  292  ASP   D CB  
10436 C  CG  . ASP   D 223 ? 1.3905 1.1771 1.1377 0.0457  0.0110  0.0191  292  ASP   D CG  
10437 O  OD1 . ASP   D 223 ? 1.3680 1.1580 1.1197 0.0417  0.0074  0.0166  292  ASP   D OD1 
10438 O  OD2 . ASP   D 223 ? 1.3804 1.1500 1.1119 0.0513  0.0175  0.0223  292  ASP   D OD2 
10439 N  N   . VAL   D 224 ? 1.2492 1.0922 1.0401 0.0397  -0.0070 0.0118  293  VAL   D N   
10440 C  CA  . VAL   D 224 ? 1.2607 1.1206 1.0691 0.0333  -0.0085 0.0121  293  VAL   D CA  
10441 C  C   . VAL   D 224 ? 1.1852 1.0598 1.0072 0.0277  -0.0154 0.0081  293  VAL   D C   
10442 O  O   . VAL   D 224 ? 1.1376 1.0240 0.9748 0.0193  -0.0149 0.0091  293  VAL   D O   
10443 C  CB  . VAL   D 224 ? 1.1236 0.9858 0.9289 0.0397  -0.0107 0.0115  293  VAL   D CB  
10444 C  CG1 . VAL   D 224 ? 1.0496 0.8955 0.8392 0.0462  -0.0039 0.0152  293  VAL   D CG1 
10445 C  CG2 . VAL   D 224 ? 1.1683 1.0344 0.9706 0.0460  -0.0202 0.0059  293  VAL   D CG2 
10446 N  N   . LEU   D 225 ? 1.1808 1.0549 0.9975 0.0326  -0.0219 0.0037  294  LEU   D N   
10447 C  CA  . LEU   D 225 ? 1.2070 1.0939 1.0357 0.0277  -0.0276 0.0002  294  LEU   D CA  
10448 C  C   . LEU   D 225 ? 1.1925 1.0774 1.0248 0.0204  -0.0246 0.0015  294  LEU   D C   
10449 O  O   . LEU   D 225 ? 1.1003 0.9968 0.9457 0.0133  -0.0269 0.0004  294  LEU   D O   
10450 C  CB  . LEU   D 225 ? 1.1966 1.0832 1.0192 0.0351  -0.0349 -0.0047 294  LEU   D CB  
10451 C  CG  . LEU   D 225 ? 1.1177 1.0194 0.9515 0.0354  -0.0415 -0.0081 294  LEU   D CG  
10452 C  CD1 . LEU   D 225 ? 1.0859 0.9918 0.9234 0.0354  -0.0399 -0.0059 294  LEU   D CD1 
10453 C  CD2 . LEU   D 225 ? 1.1457 1.0452 0.9727 0.0440  -0.0482 -0.0128 294  LEU   D CD2 
10454 N  N   . ARG   D 226 ? 1.1497 1.0191 0.9697 0.0223  -0.0195 0.0037  295  ARG   D N   
10455 C  CA  . ARG   D 226 ? 1.1395 1.0053 0.9625 0.0152  -0.0160 0.0054  295  ARG   D CA  
10456 C  C   . ARG   D 226 ? 1.1548 1.0285 0.9921 0.0061  -0.0118 0.0088  295  ARG   D C   
10457 O  O   . ARG   D 226 ? 1.1290 1.0103 0.9774 -0.0016 -0.0133 0.0082  295  ARG   D O   
10458 C  CB  . ARG   D 226 ? 1.1502 0.9969 0.9570 0.0194  -0.0107 0.0076  295  ARG   D CB  
10459 C  CG  . ARG   D 226 ? 1.1478 0.9883 0.9451 0.0240  -0.0150 0.0040  295  ARG   D CG  
10460 C  CD  . ARG   D 226 ? 1.2225 1.0434 1.0027 0.0286  -0.0100 0.0060  295  ARG   D CD  
10461 N  NE  . ARG   D 226 ? 1.2762 1.0927 1.0481 0.0333  -0.0151 0.0020  295  ARG   D NE  
10462 C  CZ  . ARG   D 226 ? 1.2617 1.0638 1.0219 0.0350  -0.0126 0.0025  295  ARG   D CZ  
10463 N  NH1 . ARG   D 226 ? 1.2561 1.0458 1.0106 0.0326  -0.0048 0.0069  295  ARG   D NH1 
10464 N  NH2 . ARG   D 226 ? 1.2799 1.0801 1.0344 0.0392  -0.0178 -0.0014 295  ARG   D NH2 
10465 N  N   . ILE   D 227 ? 1.1486 1.0201 0.9855 0.0070  -0.0067 0.0124  296  ILE   D N   
10466 C  CA  . ILE   D 227 ? 1.1828 1.0623 1.0342 -0.0013 -0.0028 0.0156  296  ILE   D CA  
10467 C  C   . ILE   D 227 ? 1.1420 1.0395 1.0086 -0.0060 -0.0088 0.0130  296  ILE   D C   
10468 O  O   . ILE   D 227 ? 1.1792 1.0846 1.0587 -0.0143 -0.0089 0.0136  296  ILE   D O   
10469 C  CB  . ILE   D 227 ? 1.1578 1.0321 1.0059 0.0014  0.0040  0.0198  296  ILE   D CB  
10470 C  CG1 . ILE   D 227 ? 1.1516 1.0078 0.9868 0.0038  0.0114  0.0232  296  ILE   D CG1 
10471 C  CG2 . ILE   D 227 ? 1.0931 0.9800 0.9587 -0.0063 0.0060  0.0222  296  ILE   D CG2 
10472 C  CD1 . ILE   D 227 ? 1.2307 1.0756 1.0517 0.0124  0.0159  0.0255  296  ILE   D CD1 
10473 N  N   . GLN   D 228 ? 1.0894 0.9934 0.9550 -0.0007 -0.0141 0.0102  297  GLN   D N   
10474 C  CA  . GLN   D 228 ? 1.1217 1.0422 1.0013 -0.0049 -0.0194 0.0079  297  GLN   D CA  
10475 C  C   . GLN   D 228 ? 1.1112 1.0365 0.9973 -0.0108 -0.0229 0.0056  297  GLN   D C   
10476 O  O   . GLN   D 228 ? 1.0967 1.0310 0.9954 -0.0184 -0.0231 0.0063  297  GLN   D O   
10477 C  CB  . GLN   D 228 ? 1.1565 1.0819 1.0331 0.0020  -0.0251 0.0046  297  GLN   D CB  
10478 C  CG  . GLN   D 228 ? 1.2310 1.1572 1.1068 0.0055  -0.0230 0.0066  297  GLN   D CG  
10479 C  CD  . GLN   D 228 ? 1.2913 1.2242 1.1670 0.0112  -0.0295 0.0030  297  GLN   D CD  
10480 O  OE1 . GLN   D 228 ? 1.2253 1.1506 1.0899 0.0192  -0.0299 0.0026  297  GLN   D OE1 
10481 N  NE2 . GLN   D 228 ? 1.3152 1.2621 1.2033 0.0071  -0.0347 0.0004  297  GLN   D NE2 
10482 N  N   . LEU   D 229 ? 1.1123 1.0311 0.9893 -0.0070 -0.0256 0.0028  298  LEU   D N   
10483 C  CA  . LEU   D 229 ? 1.1002 1.0223 0.9818 -0.0120 -0.0285 0.0007  298  LEU   D CA  
10484 C  C   . LEU   D 229 ? 1.1470 1.0665 1.0343 -0.0201 -0.0244 0.0036  298  LEU   D C   
10485 O  O   . LEU   D 229 ? 1.1622 1.0891 1.0590 -0.0264 -0.0269 0.0025  298  LEU   D O   
10486 C  CB  . LEU   D 229 ? 1.0516 0.9645 0.9210 -0.0063 -0.0307 -0.0021 298  LEU   D CB  
10487 C  CG  . LEU   D 229 ? 1.0189 0.9363 0.8854 0.0009  -0.0361 -0.0057 298  LEU   D CG  
10488 C  CD1 . LEU   D 229 ? 1.0861 0.9933 0.9403 0.0068  -0.0378 -0.0081 298  LEU   D CD1 
10489 C  CD2 . LEU   D 229 ? 1.0489 0.9813 0.9281 -0.0030 -0.0409 -0.0083 298  LEU   D CD2 
10490 N  N   . LEU   D 230 ? 1.0955 1.0045 0.9777 -0.0198 -0.0179 0.0073  299  LEU   D N   
10491 C  CA  . LEU   D 230 ? 1.0666 0.9731 0.9556 -0.0276 -0.0138 0.0101  299  LEU   D CA  
10492 C  C   . LEU   D 230 ? 1.0908 1.0100 0.9959 -0.0342 -0.0135 0.0118  299  LEU   D C   
10493 O  O   . LEU   D 230 ? 1.1586 1.0807 1.0733 -0.0418 -0.0133 0.0124  299  LEU   D O   
10494 C  CB  . LEU   D 230 ? 1.0894 0.9807 0.9685 -0.0253 -0.0063 0.0138  299  LEU   D CB  
10495 C  CG  . LEU   D 230 ? 1.2096 1.0878 1.0779 -0.0243 -0.0059 0.0129  299  LEU   D CG  
10496 C  CD1 . LEU   D 230 ? 1.1732 1.0528 1.0345 -0.0191 -0.0125 0.0082  299  LEU   D CD1 
10497 C  CD2 . LEU   D 230 ? 1.2767 1.1381 1.1315 -0.0196 0.0011  0.0161  299  LEU   D CD2 
10498 N  N   . LYS   D 231 ? 1.1175 1.0444 1.0259 -0.0315 -0.0140 0.0122  300  LYS   D N   
10499 C  CA  . LYS   D 231 ? 1.0876 1.0263 1.0112 -0.0376 -0.0137 0.0138  300  LYS   D CA  
10500 C  C   . LYS   D 231 ? 1.0456 0.9978 0.9785 -0.0407 -0.0207 0.0104  300  LYS   D C   
10501 O  O   . LYS   D 231 ? 1.0004 0.9619 0.9461 -0.0468 -0.0213 0.0113  300  LYS   D O   
10502 C  CB  . LYS   D 231 ? 1.0554 0.9958 0.9789 -0.0337 -0.0102 0.0163  300  LYS   D CB  
10503 C  CG  . LYS   D 231 ? 1.1139 1.0401 1.0218 -0.0261 -0.0058 0.0178  300  LYS   D CG  
10504 C  CD  . LYS   D 231 ? 1.2002 1.1255 1.1080 -0.0234 -0.0005 0.0213  300  LYS   D CD  
10505 C  CE  . LYS   D 231 ? 1.2878 1.2148 1.2073 -0.0307 0.0056  0.0255  300  LYS   D CE  
10506 N  NZ  . LYS   D 231 ? 1.4177 1.3444 1.3373 -0.0276 0.0110  0.0290  300  LYS   D NZ  
10507 N  N   . ILE   D 232 ? 1.0436 0.9967 0.9704 -0.0366 -0.0257 0.0067  301  ILE   D N   
10508 C  CA  . ILE   D 232 ? 1.0266 0.9912 0.9614 -0.0395 -0.0316 0.0036  301  ILE   D CA  
10509 C  C   . ILE   D 232 ? 1.1349 1.1003 1.0767 -0.0474 -0.0323 0.0037  301  ILE   D C   
10510 O  O   . ILE   D 232 ? 1.1422 1.0977 1.0796 -0.0492 -0.0297 0.0047  301  ILE   D O   
10511 C  CB  . ILE   D 232 ? 1.0760 1.0398 1.0029 -0.0338 -0.0360 -0.0002 301  ILE   D CB  
10512 C  CG1 . ILE   D 232 ? 1.0669 1.0336 0.9906 -0.0269 -0.0372 -0.0010 301  ILE   D CG1 
10513 C  CG2 . ILE   D 232 ? 1.1046 1.0773 1.0383 -0.0375 -0.0410 -0.0031 301  ILE   D CG2 
10514 C  CD1 . ILE   D 232 ? 1.1066 1.0777 1.0281 -0.0223 -0.0427 -0.0052 301  ILE   D CD1 
10515 N  N   . GLY   D 233 ? 1.1420 1.1189 1.0946 -0.0519 -0.0360 0.0026  302  GLY   D N   
10516 C  CA  . GLY   D 233 ? 1.1637 1.1430 1.1248 -0.0595 -0.0372 0.0028  302  GLY   D CA  
10517 C  C   . GLY   D 233 ? 1.1791 1.1578 1.1378 -0.0612 -0.0419 -0.0005 302  GLY   D C   
10518 O  O   . GLY   D 233 ? 1.2144 1.1935 1.1788 -0.0672 -0.0434 -0.0006 302  GLY   D O   
10519 N  N   . SER   D 234 ? 1.1407 1.1182 1.0912 -0.0558 -0.0443 -0.0032 303  SER   D N   
10520 C  CA  . SER   D 234 ? 1.0962 1.0728 1.0438 -0.0568 -0.0482 -0.0063 303  SER   D CA  
10521 C  C   . SER   D 234 ? 1.1035 1.0736 1.0395 -0.0501 -0.0486 -0.0084 303  SER   D C   
10522 O  O   . SER   D 234 ? 1.0807 1.0527 1.0137 -0.0443 -0.0484 -0.0089 303  SER   D O   
10523 C  CB  . SER   D 234 ? 1.0770 1.0655 1.0323 -0.0586 -0.0523 -0.0080 303  SER   D CB  
10524 O  OG  . SER   D 234 ? 1.1091 1.1034 1.0636 -0.0532 -0.0530 -0.0090 303  SER   D OG  
10525 N  N   . ALA   D 235 ? 1.0837 1.0461 1.0133 -0.0508 -0.0496 -0.0100 304  ALA   D N   
10526 C  CA  . ALA   D 235 ? 1.0642 1.0205 0.9832 -0.0445 -0.0502 -0.0123 304  ALA   D CA  
10527 C  C   . ALA   D 235 ? 1.0571 1.0229 0.9782 -0.0403 -0.0533 -0.0148 304  ALA   D C   
10528 O  O   . ALA   D 235 ? 1.1104 1.0738 1.0251 -0.0338 -0.0535 -0.0162 304  ALA   D O   
10529 C  CB  . ALA   D 235 ? 1.1589 1.1063 1.0714 -0.0463 -0.0512 -0.0137 304  ALA   D CB  
10530 N  N   . ILE   D 236 ? 1.0673 1.0437 0.9974 -0.0438 -0.0558 -0.0154 305  ILE   D N   
10531 C  CA  . ILE   D 236 ? 1.0313 1.0167 0.9644 -0.0400 -0.0582 -0.0176 305  ILE   D CA  
10532 C  C   . ILE   D 236 ? 1.0472 1.0362 0.9818 -0.0357 -0.0572 -0.0167 305  ILE   D C   
10533 O  O   . ILE   D 236 ? 1.0577 1.0470 0.9888 -0.0296 -0.0583 -0.0186 305  ILE   D O   
10534 C  CB  . ILE   D 236 ? 1.0368 1.0320 0.9787 -0.0446 -0.0606 -0.0181 305  ILE   D CB  
10535 C  CG1 . ILE   D 236 ? 1.0265 1.0181 0.9649 -0.0469 -0.0623 -0.0199 305  ILE   D CG1 
10536 C  CG2 . ILE   D 236 ? 1.0662 1.0711 1.0126 -0.0409 -0.0622 -0.0197 305  ILE   D CG2 
10537 C  CD1 . ILE   D 236 ? 0.9986 0.9929 0.9345 -0.0425 -0.0639 -0.0228 305  ILE   D CD1 
10538 N  N   . GLN   D 237 ? 1.0370 1.0289 0.9772 -0.0387 -0.0555 -0.0140 306  GLN   D N   
10539 C  CA  . GLN   D 237 ? 1.0537 1.0482 0.9945 -0.0344 -0.0546 -0.0131 306  GLN   D CA  
10540 C  C   . GLN   D 237 ? 1.1027 1.0863 1.0324 -0.0284 -0.0526 -0.0130 306  GLN   D C   
10541 O  O   . GLN   D 237 ? 1.1413 1.1256 1.0683 -0.0225 -0.0535 -0.0139 306  GLN   D O   
10542 C  CB  . GLN   D 237 ? 1.0468 1.0457 0.9953 -0.0387 -0.0525 -0.0100 306  GLN   D CB  
10543 C  CG  . GLN   D 237 ? 1.0655 1.0761 1.0248 -0.0433 -0.0550 -0.0103 306  GLN   D CG  
10544 C  CD  . GLN   D 237 ? 1.0535 1.0676 1.0208 -0.0486 -0.0532 -0.0074 306  GLN   D CD  
10545 O  OE1 . GLN   D 237 ? 1.0208 1.0288 0.9876 -0.0519 -0.0505 -0.0053 306  GLN   D OE1 
10546 N  NE2 . GLN   D 237 ? 1.1389 1.1632 1.1144 -0.0496 -0.0546 -0.0071 306  GLN   D NE2 
10547 N  N   . ARG   D 238 ? 1.0444 1.0172 0.9671 -0.0298 -0.0502 -0.0120 307  ARG   D N   
10548 C  CA  . ARG   D 238 ? 1.0754 1.0364 0.9865 -0.0241 -0.0480 -0.0116 307  ARG   D CA  
10549 C  C   . ARG   D 238 ? 1.0767 1.0360 0.9812 -0.0176 -0.0510 -0.0151 307  ARG   D C   
10550 O  O   . ARG   D 238 ? 1.0536 1.0093 0.9518 -0.0108 -0.0514 -0.0158 307  ARG   D O   
10551 C  CB  . ARG   D 238 ? 1.1105 1.0605 1.0166 -0.0276 -0.0444 -0.0095 307  ARG   D CB  
10552 C  CG  . ARG   D 238 ? 1.1315 1.0684 1.0261 -0.0227 -0.0406 -0.0078 307  ARG   D CG  
10553 C  CD  . ARG   D 238 ? 1.1162 1.0429 1.0080 -0.0274 -0.0366 -0.0053 307  ARG   D CD  
10554 N  NE  . ARG   D 238 ? 1.0872 1.0201 0.9907 -0.0350 -0.0349 -0.0029 307  ARG   D NE  
10555 C  CZ  . ARG   D 238 ? 1.1294 1.0649 1.0397 -0.0418 -0.0364 -0.0032 307  ARG   D CZ  
10556 N  NH1 . ARG   D 238 ? 1.1688 1.0995 1.0740 -0.0423 -0.0388 -0.0056 307  ARG   D NH1 
10557 N  NH2 . ARG   D 238 ? 1.1492 1.0920 1.0713 -0.0481 -0.0358 -0.0013 307  ARG   D NH2 
10558 N  N   . LEU   D 239 ? 1.0632 1.0250 0.9692 -0.0194 -0.0534 -0.0174 308  LEU   D N   
10559 C  CA  . LEU   D 239 ? 1.0264 0.9886 0.9286 -0.0137 -0.0563 -0.0208 308  LEU   D CA  
10560 C  C   . LEU   D 239 ? 1.0532 1.0251 0.9613 -0.0096 -0.0590 -0.0224 308  LEU   D C   
10561 O  O   . LEU   D 239 ? 1.0448 1.0141 0.9478 -0.0027 -0.0605 -0.0242 308  LEU   D O   
10562 C  CB  . LEU   D 239 ? 1.0247 0.9895 0.9292 -0.0170 -0.0580 -0.0227 308  LEU   D CB  
10563 C  CG  . LEU   D 239 ? 1.0366 0.9914 0.9347 -0.0204 -0.0565 -0.0221 308  LEU   D CG  
10564 C  CD1 . LEU   D 239 ? 1.0943 1.0499 0.9911 -0.0202 -0.0586 -0.0249 308  LEU   D CD1 
10565 C  CD2 . LEU   D 239 ? 1.1482 1.0896 1.0347 -0.0164 -0.0541 -0.0212 308  LEU   D CD2 
10566 N  N   . ARG   D 240 ? 1.1119 1.0951 1.0308 -0.0137 -0.0600 -0.0219 309  ARG   D N   
10567 C  CA  . ARG   D 240 ? 1.0516 1.0441 0.9769 -0.0104 -0.0625 -0.0234 309  ARG   D CA  
10568 C  C   . ARG   D 240 ? 1.0717 1.0597 0.9919 -0.0051 -0.0621 -0.0226 309  ARG   D C   
10569 O  O   . ARG   D 240 ? 1.0682 1.0573 0.9871 0.0012  -0.0648 -0.0250 309  ARG   D O   
10570 C  CB  . ARG   D 240 ? 1.0467 1.0504 0.9834 -0.0162 -0.0630 -0.0224 309  ARG   D CB  
10571 C  CG  . ARG   D 240 ? 0.9965 1.0071 0.9390 -0.0186 -0.0648 -0.0243 309  ARG   D CG  
10572 C  CD  . ARG   D 240 ? 1.0242 1.0432 0.9759 -0.0249 -0.0648 -0.0228 309  ARG   D CD  
10573 N  NE  . ARG   D 240 ? 0.9815 1.0073 0.9392 -0.0240 -0.0653 -0.0220 309  ARG   D NE  
10574 C  CZ  . ARG   D 240 ? 1.0915 1.1260 1.0558 -0.0220 -0.0676 -0.0237 309  ARG   D CZ  
10575 N  NH1 . ARG   D 240 ? 1.0454 1.0835 1.0121 -0.0211 -0.0690 -0.0262 309  ARG   D NH1 
10576 N  NH2 . ARG   D 240 ? 1.2158 1.2551 1.1845 -0.0208 -0.0683 -0.0230 309  ARG   D NH2 
10577 N  N   . CYS   D 241 ? 1.0869 1.0691 1.0038 -0.0072 -0.0586 -0.0193 310  CYS   D N   
10578 C  CA  . CYS   D 241 ? 1.0885 1.0643 0.9985 -0.0018 -0.0574 -0.0182 310  CYS   D CA  
10579 C  C   . CYS   D 241 ? 1.0533 1.0184 0.9511 0.0054  -0.0582 -0.0201 310  CYS   D C   
10580 O  O   . CYS   D 241 ? 1.0556 1.0196 0.9497 0.0123  -0.0607 -0.0218 310  CYS   D O   
10581 C  CB  . CYS   D 241 ? 1.0679 1.0383 0.9762 -0.0056 -0.0524 -0.0140 310  CYS   D CB  
10582 S  SG  . CYS   D 241 ? 1.1901 1.1546 1.0911 0.0010  -0.0509 -0.0126 310  CYS   D SG  
10583 N  N   . GLU   D 242 ? 1.0241 0.9805 0.9152 0.0041  -0.0562 -0.0197 311  GLU   D N   
10584 C  CA  . GLU   D 242 ? 1.0452 0.9916 0.9248 0.0109  -0.0572 -0.0216 311  GLU   D CA  
10585 C  C   . GLU   D 242 ? 1.0367 0.9901 0.9199 0.0160  -0.0624 -0.0258 311  GLU   D C   
10586 O  O   . GLU   D 242 ? 1.0343 0.9843 0.9119 0.0235  -0.0648 -0.0275 311  GLU   D O   
10587 C  CB  . GLU   D 242 ? 1.0640 1.0023 0.9382 0.0079  -0.0551 -0.0212 311  GLU   D CB  
10588 C  CG  . GLU   D 242 ? 1.0631 0.9897 0.9297 0.0060  -0.0500 -0.0176 311  GLU   D CG  
10589 C  CD  . GLU   D 242 ? 1.1195 1.0427 0.9868 -0.0006 -0.0479 -0.0165 311  GLU   D CD  
10590 O  OE1 . GLU   D 242 ? 1.0962 1.0224 0.9654 -0.0017 -0.0505 -0.0190 311  GLU   D OE1 
10591 O  OE2 . GLU   D 242 ? 1.1487 1.0659 1.0150 -0.0048 -0.0436 -0.0131 311  GLU   D OE2 
10592 N  N   . LEU   D 243 ? 1.0623 1.0256 0.9551 0.0122  -0.0642 -0.0274 312  LEU   D N   
10593 C  CA  . LEU   D 243 ? 1.0304 1.0016 0.9287 0.0164  -0.0685 -0.0312 312  LEU   D CA  
10594 C  C   . LEU   D 243 ? 1.0875 1.0636 0.9893 0.0207  -0.0713 -0.0320 312  LEU   D C   
10595 O  O   . LEU   D 243 ? 1.1440 1.1208 1.0452 0.0273  -0.0751 -0.0352 312  LEU   D O   
10596 C  CB  . LEU   D 243 ? 0.9946 0.9765 0.9039 0.0107  -0.0690 -0.0319 312  LEU   D CB  
10597 C  CG  . LEU   D 243 ? 1.0356 1.0219 0.9481 0.0144  -0.0719 -0.0356 312  LEU   D CG  
10598 C  CD1 . LEU   D 243 ? 1.0642 1.0401 0.9657 0.0216  -0.0728 -0.0374 312  LEU   D CD1 
10599 C  CD2 . LEU   D 243 ? 1.0002 0.9906 0.9173 0.0087  -0.0706 -0.0356 312  LEU   D CD2 
10600 N  N   . ASP   D 244 ? 1.1043 1.0833 1.0095 0.0174  -0.0696 -0.0294 313  ASP   D N   
10601 C  CA  . ASP   D 244 ? 1.0912 1.0746 0.9995 0.0214  -0.0724 -0.0302 313  ASP   D CA  
10602 C  C   . ASP   D 244 ? 1.0801 1.0517 0.9755 0.0293  -0.0730 -0.0305 313  ASP   D C   
10603 O  O   . ASP   D 244 ? 1.0602 1.0333 0.9557 0.0354  -0.0772 -0.0330 313  ASP   D O   
10604 C  CB  . ASP   D 244 ? 1.0771 1.0665 0.9922 0.0159  -0.0703 -0.0273 313  ASP   D CB  
10605 C  CG  . ASP   D 244 ? 1.0922 1.0935 1.0182 0.0164  -0.0741 -0.0291 313  ASP   D CG  
10606 O  OD1 . ASP   D 244 ? 1.0688 1.0759 1.0003 0.0186  -0.0777 -0.0325 313  ASP   D OD1 
10607 O  OD2 . ASP   D 244 ? 1.1061 1.1108 1.0355 0.0148  -0.0733 -0.0272 313  ASP   D OD2 
10608 N  N   . ILE   D 245 ? 1.0924 1.0518 0.9765 0.0293  -0.0688 -0.0278 314  ILE   D N   
10609 C  CA  . ILE   D 245 ? 1.0992 1.0457 0.9692 0.0371  -0.0688 -0.0279 314  ILE   D CA  
10610 C  C   . ILE   D 245 ? 1.1116 1.0553 0.9773 0.0440  -0.0734 -0.0321 314  ILE   D C   
10611 O  O   . ILE   D 245 ? 1.1264 1.0668 0.9871 0.0517  -0.0773 -0.0343 314  ILE   D O   
10612 C  CB  . ILE   D 245 ? 1.0759 1.0096 0.9353 0.0351  -0.0626 -0.0240 314  ILE   D CB  
10613 C  CG1 . ILE   D 245 ? 1.0247 0.9628 0.8910 0.0276  -0.0582 -0.0200 314  ILE   D CG1 
10614 C  CG2 . ILE   D 245 ? 1.1184 1.0379 0.9622 0.0434  -0.0622 -0.0236 314  ILE   D CG2 
10615 C  CD1 . ILE   D 245 ? 1.0874 1.0151 0.9471 0.0238  -0.0519 -0.0162 314  ILE   D CD1 
10616 N  N   . MET   D 246 ? 1.0962 1.0412 0.9640 0.0417  -0.0733 -0.0333 315  MET   D N   
10617 C  CA  . MET   D 246 ? 1.0975 1.0398 0.9616 0.0483  -0.0773 -0.0371 315  MET   D CA  
10618 C  C   . MET   D 246 ? 1.1544 1.1084 1.0295 0.0516  -0.0832 -0.0411 315  MET   D C   
10619 O  O   . MET   D 246 ? 1.1905 1.1423 1.0628 0.0588  -0.0874 -0.0446 315  MET   D O   
10620 C  CB  . MET   D 246 ? 1.0837 1.0252 0.9480 0.0447  -0.0754 -0.0374 315  MET   D CB  
10621 C  CG  . MET   D 246 ? 1.1286 1.0608 0.9855 0.0394  -0.0696 -0.0335 315  MET   D CG  
10622 S  SD  . MET   D 246 ? 1.2300 1.1596 1.0855 0.0360  -0.0683 -0.0343 315  MET   D SD  
10623 C  CE  . MET   D 246 ? 1.1245 1.0543 0.9780 0.0454  -0.0735 -0.0393 315  MET   D CE  
10624 N  N   . ASN   D 247 ? 1.1292 1.0955 1.0172 0.0466  -0.0836 -0.0407 316  ASN   D N   
10625 C  CA  . ASN   D 247 ? 1.0994 1.0768 0.9988 0.0494  -0.0890 -0.0443 316  ASN   D CA  
10626 C  C   . ASN   D 247 ? 1.1249 1.1021 1.0234 0.0535  -0.0920 -0.0446 316  ASN   D C   
10627 O  O   . ASN   D 247 ? 1.0931 1.0739 0.9958 0.0591  -0.0976 -0.0484 316  ASN   D O   
10628 C  CB  . ASN   D 247 ? 1.1117 1.1031 1.0264 0.0419  -0.0881 -0.0440 316  ASN   D CB  
10629 C  CG  . ASN   D 247 ? 1.1056 1.0983 1.0223 0.0394  -0.0865 -0.0448 316  ASN   D CG  
10630 O  OD1 . ASN   D 247 ? 1.1028 1.0925 1.0166 0.0446  -0.0886 -0.0476 316  ASN   D OD1 
10631 N  ND2 . ASN   D 247 ? 1.1425 1.1396 1.0641 0.0316  -0.0829 -0.0425 316  ASN   D ND2 
10632 N  N   . LYS   D 248 ? 1.1383 1.1109 1.0315 0.0510  -0.0884 -0.0410 317  LYS   D N   
10633 C  CA  . LYS   D 248 ? 1.0597 1.0324 0.9521 0.0541  -0.0905 -0.0408 317  LYS   D CA  
10634 C  C   . LYS   D 248 ? 1.1325 1.0899 1.0078 0.0617  -0.0905 -0.0402 317  LYS   D C   
10635 O  O   . LYS   D 248 ? 1.1445 1.1006 1.0175 0.0673  -0.0945 -0.0417 317  LYS   D O   
10636 C  CB  . LYS   D 248 ? 1.0804 1.0588 0.9790 0.0467  -0.0865 -0.0370 317  LYS   D CB  
10637 C  CG  . LYS   D 248 ? 1.1024 1.0966 1.0181 0.0409  -0.0881 -0.0381 317  LYS   D CG  
10638 C  CD  . LYS   D 248 ? 1.1353 1.1344 1.0559 0.0355  -0.0853 -0.0348 317  LYS   D CD  
10639 C  CE  . LYS   D 248 ? 1.1192 1.1322 1.0551 0.0282  -0.0852 -0.0348 317  LYS   D CE  
10640 N  NZ  . LYS   D 248 ? 1.1584 1.1736 1.0967 0.0213  -0.0806 -0.0307 317  LYS   D NZ  
10641 N  N   . CYS   D 249 ? 1.1893 1.1344 1.0520 0.0622  -0.0860 -0.0378 318  CYS   D N   
10642 C  CA  . CYS   D 249 ? 1.1580 1.0871 1.0030 0.0692  -0.0847 -0.0365 318  CYS   D CA  
10643 C  C   . CYS   D 249 ? 1.1355 1.0560 0.9710 0.0774  -0.0887 -0.0400 318  CYS   D C   
10644 O  O   . CYS   D 249 ? 1.1539 1.0622 0.9771 0.0791  -0.0854 -0.0386 318  CYS   D O   
10645 C  CB  . CYS   D 249 ? 1.1530 1.0730 0.9900 0.0646  -0.0766 -0.0314 318  CYS   D CB  
10646 S  SG  . CYS   D 249 ? 1.2464 1.1746 1.0929 0.0565  -0.0720 -0.0272 318  CYS   D SG  
10647 N  N   . THR   D 250 ? 1.1210 1.0479 0.9626 0.0825  -0.0961 -0.0446 319  THR   D N   
10648 C  CA  . THR   D 250 ? 1.1944 1.1172 1.0318 0.0895  -0.1009 -0.0487 319  THR   D CA  
10649 C  C   . THR   D 250 ? 1.2034 1.1111 1.0236 0.1000  -0.1041 -0.0499 319  THR   D C   
10650 O  O   . THR   D 250 ? 1.2066 1.1103 1.0225 0.1072  -0.1092 -0.0537 319  THR   D O   
10651 C  CB  . THR   D 250 ? 1.1662 1.1043 1.0210 0.0893  -0.1072 -0.0531 319  THR   D CB  
10652 O  OG1 . THR   D 250 ? 1.2104 1.1524 1.0692 0.0926  -0.1121 -0.0549 319  THR   D OG1 
10653 C  CG2 . THR   D 250 ? 1.1321 1.0835 1.0020 0.0792  -0.1034 -0.0514 319  THR   D CG2 
10654 N  N   . SER   D 251 ? 1.2228 1.1219 1.0327 0.1014  -0.1011 -0.0468 320  SER   D N   
10655 C  CA  . SER   D 251 ? 1.2444 1.1276 1.0359 0.1116  -0.1034 -0.0475 320  SER   D CA  
10656 C  C   . SER   D 251 ? 1.2028 1.0708 0.9781 0.1108  -0.0949 -0.0421 320  SER   D C   
10657 O  O   . SER   D 251 ? 1.1824 1.0535 0.9617 0.1037  -0.0886 -0.0378 320  SER   D O   
10658 C  CB  . SER   D 251 ? 1.1807 1.0672 0.9747 0.1156  -0.1088 -0.0494 320  SER   D CB  
10659 O  OG  . SER   D 251 ? 1.2284 1.1079 1.0144 0.1264  -0.1169 -0.0540 320  SER   D OG  
10660 N  N   . LEU   D 252 ? 1.1871 1.0388 0.9446 0.1183  -0.0945 -0.0422 321  LEU   D N   
10661 C  CA  . LEU   D 252 ? 1.2449 1.0801 0.9855 0.1186  -0.0863 -0.0372 321  LEU   D CA  
10662 C  C   . LEU   D 252 ? 1.2602 1.0799 0.9823 0.1287  -0.0875 -0.0369 321  LEU   D C   
10663 O  O   . LEU   D 252 ? 1.2260 1.0369 0.9372 0.1385  -0.0937 -0.0406 321  LEU   D O   
10664 C  CB  . LEU   D 252 ? 1.2294 1.0559 0.9622 0.1190  -0.0837 -0.0369 321  LEU   D CB  
10665 C  CG  . LEU   D 252 ? 1.1388 0.9763 0.8855 0.1090  -0.0807 -0.0362 321  LEU   D CG  
10666 C  CD1 . LEU   D 252 ? 1.1364 0.9641 0.8738 0.1115  -0.0799 -0.0369 321  LEU   D CD1 
10667 C  CD2 . LEU   D 252 ? 1.1497 0.9899 0.9018 0.0991  -0.0723 -0.0308 321  LEU   D CD2 
10668 N  N   . CYS   D 253 ? 1.2237 1.0394 0.9416 0.1266  -0.0815 -0.0325 322  CYS   D N   
10669 C  CA  . CYS   D 253 ? 1.3082 1.1095 1.0087 0.1358  -0.0820 -0.0319 322  CYS   D CA  
10670 C  C   . CYS   D 253 ? 1.3036 1.0869 0.9865 0.1367  -0.0718 -0.0261 322  CYS   D C   
10671 O  O   . CYS   D 253 ? 1.3158 1.0997 1.0026 0.1288  -0.0641 -0.0222 322  CYS   D O   
10672 C  CB  . CYS   D 253 ? 1.3692 1.1800 1.0786 0.1342  -0.0838 -0.0318 322  CYS   D CB  
10673 S  SG  . CYS   D 253 ? 1.3462 1.1807 1.0806 0.1299  -0.0932 -0.0372 322  CYS   D SG  
10674 N  N   . CYS   D 254 ? 1.3698 1.1365 1.0329 0.1468  -0.0720 -0.0256 323  CYS   D N   
10675 C  CA  . CYS   D 254 ? 1.3413 1.0890 0.9858 0.1490  -0.0622 -0.0200 323  CYS   D CA  
10676 C  C   . CYS   D 254 ? 1.3831 1.1364 1.0360 0.1405  -0.0533 -0.0145 323  CYS   D C   
10677 O  O   . CYS   D 254 ? 1.4603 1.2209 1.1191 0.1405  -0.0553 -0.0148 323  CYS   D O   
10678 C  CB  . CYS   D 254 ? 1.2872 1.0161 0.9083 0.1626  -0.0653 -0.0212 323  CYS   D CB  
10679 S  SG  . CYS   D 254 ? 1.3102 1.0161 0.9085 0.1662  -0.0526 -0.0139 323  CYS   D SG  
10680 N  N   . LYS   D 255 ? 1.3613 1.1111 1.0150 0.1334  -0.0435 -0.0095 324  LYS   D N   
10681 C  CA  . LYS   D 255 ? 1.3508 1.1078 1.0154 0.1244  -0.0352 -0.0045 324  LYS   D CA  
10682 C  C   . LYS   D 255 ? 1.4337 1.1784 1.0845 0.1302  -0.0298 -0.0008 324  LYS   D C   
10683 O  O   . LYS   D 255 ? 1.3802 1.1332 1.0412 0.1245  -0.0254 0.0023  324  LYS   D O   
10684 C  CB  . LYS   D 255 ? 1.3578 1.1131 1.0266 0.1157  -0.0265 -0.0003 324  LYS   D CB  
10685 C  CG  . LYS   D 255 ? 1.3753 1.1388 1.0574 0.1058  -0.0181 0.0048  324  LYS   D CG  
10686 C  CD  . LYS   D 255 ? 1.4259 1.1877 1.1129 0.0972  -0.0106 0.0083  324  LYS   D CD  
10687 C  CE  . LYS   D 255 ? 1.4676 1.2151 1.1453 0.0965  0.0014  0.0149  324  LYS   D CE  
10688 N  NZ  . LYS   D 255 ? 1.3582 1.1009 1.0379 0.0897  0.0078  0.0177  324  LYS   D NZ  
10689 N  N   . GLN   D 256 ? 1.4825 1.2073 1.1099 0.1417  -0.0301 -0.0010 325  GLN   D N   
10690 C  CA  . GLN   D 256 ? 1.4719 1.1809 1.0822 0.1482  -0.0236 0.0030  325  GLN   D CA  
10691 C  C   . GLN   D 256 ? 1.4756 1.1873 1.0835 0.1550  -0.0307 0.0001  325  GLN   D C   
10692 O  O   . GLN   D 256 ? 1.4232 1.1332 1.0295 0.1549  -0.0250 0.0037  325  GLN   D O   
10693 C  CB  . GLN   D 256 ? 1.4671 1.1518 1.0516 0.1577  -0.0201 0.0044  325  GLN   D CB  
10694 C  CG  . GLN   D 256 ? 1.5586 1.2363 1.1425 0.1510  -0.0086 0.0100  325  GLN   D CG  
10695 C  CD  . GLN   D 256 ? 1.6638 1.3460 1.2572 0.1430  0.0023  0.0162  325  GLN   D CD  
10696 O  OE1 . GLN   D 256 ? 1.6671 1.3454 1.2547 0.1471  0.0048  0.0182  325  GLN   D OE1 
10697 N  NE2 . GLN   D 256 ? 1.7137 1.4040 1.3222 0.1316  0.0085  0.0191  325  GLN   D NE2 
10698 N  N   . CYS   D 257 ? 1.4775 1.1926 1.0848 0.1612  -0.0428 -0.0065 326  CYS   D N   
10699 C  CA  . CYS   D 257 ? 1.4203 1.1388 1.0269 0.1673  -0.0509 -0.0101 326  CYS   D CA  
10700 C  C   . CYS   D 257 ? 1.5203 1.2630 1.1522 0.1599  -0.0589 -0.0142 326  CYS   D C   
10701 O  O   . CYS   D 257 ? 1.5634 1.3113 1.1981 0.1637  -0.0661 -0.0174 326  CYS   D O   
10702 C  CB  . CYS   D 257 ? 1.3949 1.0976 0.9809 0.1812  -0.0595 -0.0146 326  CYS   D CB  
10703 S  SG  . CYS   D 257 ? 1.3763 1.0862 0.9696 0.1821  -0.0702 -0.0213 326  CYS   D SG  
10704 N  N   . GLN   D 258 ? 1.5411 1.2981 1.1910 0.1498  -0.0579 -0.0143 327  GLN   D N   
10705 C  CA  . GLN   D 258 ? 1.5285 1.3087 1.2035 0.1410  -0.0627 -0.0168 327  GLN   D CA  
10706 C  C   . GLN   D 258 ? 1.5549 1.3438 1.2366 0.1455  -0.0757 -0.0240 327  GLN   D C   
10707 O  O   . GLN   D 258 ? 1.6181 1.4220 1.3170 0.1392  -0.0795 -0.0267 327  GLN   D O   
10708 C  CB  . GLN   D 258 ? 1.5151 1.3034 1.1989 0.1362  -0.0587 -0.0138 327  GLN   D CB  
10709 C  CG  . GLN   D 258 ? 1.5613 1.3726 1.2698 0.1278  -0.0643 -0.0166 327  GLN   D CG  
10710 C  CD  . GLN   D 258 ? 1.5832 1.4052 1.3049 0.1187  -0.0574 -0.0122 327  GLN   D CD  
10711 O  OE1 . GLN   D 258 ? 1.6168 1.4309 1.3325 0.1166  -0.0476 -0.0067 327  GLN   D OE1 
10712 N  NE2 . GLN   D 258 ? 1.6349 1.4749 1.3753 0.1132  -0.0626 -0.0147 327  GLN   D NE2 
10713 N  N   . GLU   D 259 ? 1.4942 1.2745 1.1637 0.1560  -0.0827 -0.0273 328  GLU   D N   
10714 C  CA  . GLU   D 259 ? 1.5379 1.3268 1.2153 0.1602  -0.0954 -0.0344 328  GLU   D CA  
10715 C  C   . GLU   D 259 ? 1.5596 1.3335 1.2200 0.1707  -0.1008 -0.0378 328  GLU   D C   
10716 O  O   . GLU   D 259 ? 1.5576 1.3159 1.1989 0.1816  -0.1041 -0.0390 328  GLU   D O   
10717 C  CB  . GLU   D 259 ? 1.7385 1.5309 1.4179 0.1642  -0.1018 -0.0369 328  GLU   D CB  
10718 C  CG  . GLU   D 259 ? 1.8084 1.6107 1.4984 0.1680  -0.1156 -0.0446 328  GLU   D CG  
10719 C  CD  . GLU   D 259 ? 1.8183 1.6445 1.5363 0.1574  -0.1182 -0.0466 328  GLU   D CD  
10720 O  OE1 . GLU   D 259 ? 1.7665 1.5996 1.4934 0.1500  -0.1136 -0.0450 328  GLU   D OE1 
10721 O  OE2 . GLU   D 259 ? 1.7988 1.6363 1.5293 0.1566  -0.1249 -0.0498 328  GLU   D OE2 
10722 N  N   . THR   D 260 ? 1.6368 1.4159 1.3043 0.1676  -0.1020 -0.0395 329  THR   D N   
10723 C  CA  . THR   D 260 ? 1.6603 1.4286 1.3156 0.1765  -0.1079 -0.0433 329  THR   D CA  
10724 C  C   . THR   D 260 ? 1.5961 1.3758 1.2657 0.1697  -0.1080 -0.0447 329  THR   D C   
10725 O  O   . THR   D 260 ? 1.6021 1.3757 1.2666 0.1660  -0.1001 -0.0409 329  THR   D O   
10726 C  CB  . THR   D 260 ? 1.6707 1.4147 1.2990 0.1840  -0.1014 -0.0396 329  THR   D CB  
10727 O  OG1 . THR   D 260 ? 1.6740 1.4063 1.2873 0.1919  -0.1022 -0.0389 329  THR   D OG1 
10728 C  CG2 . THR   D 260 ? 1.6258 1.3594 1.2425 0.1925  -0.1073 -0.0435 329  THR   D CG2 
10729 N  N   . GLU   D 261 ? 1.4991 1.2951 1.1870 0.1681  -0.1168 -0.0499 330  GLU   D N   
10730 C  CA  . GLU   D 261 ? 1.4521 1.2593 1.1539 0.1624  -0.1175 -0.0517 330  GLU   D CA  
10731 C  C   . GLU   D 261 ? 1.4284 1.2207 1.1142 0.1686  -0.1168 -0.0521 330  GLU   D C   
10732 O  O   . GLU   D 261 ? 1.4261 1.2090 1.1008 0.1793  -0.1244 -0.0563 330  GLU   D O   
10733 C  CB  . GLU   D 261 ? 1.4588 1.2830 1.1801 0.1624  -0.1278 -0.0579 330  GLU   D CB  
10734 C  CG  . GLU   D 261 ? 1.4909 1.3256 1.2254 0.1578  -0.1286 -0.0598 330  GLU   D CG  
10735 C  CD  . GLU   D 261 ? 1.5250 1.3782 1.2814 0.1562  -0.1371 -0.0652 330  GLU   D CD  
10736 O  OE1 . GLU   D 261 ? 1.5066 1.3739 1.2789 0.1488  -0.1362 -0.0644 330  GLU   D OE1 
10737 O  OE2 . GLU   D 261 ? 1.6119 1.4653 1.3697 0.1624  -0.1444 -0.0702 330  GLU   D OE2 
10738 N  N   . ILE   D 262 ? 1.3690 1.1594 1.0542 0.1618  -0.1080 -0.0479 331  ILE   D N   
10739 C  CA  . ILE   D 262 ? 1.3147 1.0926 0.9869 0.1661  -0.1068 -0.0481 331  ILE   D CA  
10740 C  C   . ILE   D 262 ? 1.2830 1.0739 0.9704 0.1641  -0.1125 -0.0526 331  ILE   D C   
10741 O  O   . ILE   D 262 ? 1.3182 1.1028 0.9984 0.1724  -0.1188 -0.0566 331  ILE   D O   
10742 C  CB  . ILE   D 262 ? 1.3424 1.1109 1.0064 0.1600  -0.0948 -0.0415 331  ILE   D CB  
10743 C  CG1 . ILE   D 262 ? 1.3148 1.0672 0.9607 0.1641  -0.0889 -0.0372 331  ILE   D CG1 
10744 C  CG2 . ILE   D 262 ? 1.3528 1.1113 1.0072 0.1625  -0.0935 -0.0419 331  ILE   D CG2 
10745 C  CD1 . ILE   D 262 ? 1.3942 1.1296 1.0192 0.1779  -0.0947 -0.0399 331  ILE   D CD1 
10746 N  N   . THR   D 263 ? 1.2957 1.1047 1.0040 0.1534  -0.1105 -0.0520 332  THR   D N   
10747 C  CA  . THR   D 263 ? 1.3124 1.1320 1.0336 0.1507  -0.1135 -0.0552 332  THR   D CA  
10748 C  C   . THR   D 263 ? 1.3137 1.1544 1.0587 0.1398  -0.1126 -0.0550 332  THR   D C   
10749 O  O   . THR   D 263 ? 1.2983 1.1445 1.0489 0.1346  -0.1095 -0.0523 332  THR   D O   
10750 C  CB  . THR   D 263 ? 1.2049 1.0130 0.9147 0.1497  -0.1073 -0.0526 332  THR   D CB  
10751 O  OG1 . THR   D 263 ? 1.1676 0.9814 0.8842 0.1514  -0.1120 -0.0567 332  THR   D OG1 
10752 C  CG2 . THR   D 263 ? 1.1521 0.9644 0.8681 0.1381  -0.0977 -0.0472 332  THR   D CG2 
10753 N  N   . THR   D 264 ? 1.3381 1.1903 1.0968 0.1368  -0.1150 -0.0578 333  THR   D N   
10754 C  CA  . THR   D 264 ? 1.2600 1.1321 1.0413 0.1277  -0.1150 -0.0582 333  THR   D CA  
10755 C  C   . THR   D 264 ? 1.2863 1.1629 1.0737 0.1216  -0.1110 -0.0575 333  THR   D C   
10756 O  O   . THR   D 264 ? 1.3077 1.1742 1.0844 0.1256  -0.1104 -0.0580 333  THR   D O   
10757 C  CB  . THR   D 264 ? 1.2434 1.1285 1.0395 0.1311  -0.1242 -0.0638 333  THR   D CB  
10758 O  OG1 . THR   D 264 ? 1.3357 1.2211 1.1334 0.1360  -0.1286 -0.0678 333  THR   D OG1 
10759 C  CG2 . THR   D 264 ? 1.3008 1.1796 1.0892 0.1392  -0.1300 -0.0657 333  THR   D CG2 
10760 N  N   . LYS   D 265 ? 1.2930 1.1848 1.0975 0.1122  -0.1086 -0.0565 334  LYS   D N   
10761 C  CA  . LYS   D 265 ? 1.2982 1.1934 1.1074 0.1055  -0.1039 -0.0551 334  LYS   D CA  
10762 C  C   . LYS   D 265 ? 1.3397 1.2361 1.1510 0.1106  -0.1083 -0.0593 334  LYS   D C   
10763 O  O   . LYS   D 265 ? 1.3727 1.2605 1.1750 0.1112  -0.1054 -0.0586 334  LYS   D O   
10764 C  CB  . LYS   D 265 ? 1.3497 1.2610 1.1768 0.0954  -0.1015 -0.0536 334  LYS   D CB  
10765 C  CG  . LYS   D 265 ? 1.4192 1.3416 1.2593 0.0911  -0.1016 -0.0555 334  LYS   D CG  
10766 C  CD  . LYS   D 265 ? 1.3591 1.2947 1.2137 0.0809  -0.0982 -0.0532 334  LYS   D CD  
10767 C  CE  . LYS   D 265 ? 1.3632 1.3096 1.2304 0.0773  -0.0983 -0.0551 334  LYS   D CE  
10768 N  NZ  . LYS   D 265 ? 1.2192 1.1755 1.0972 0.0674  -0.0942 -0.0524 334  LYS   D NZ  
10769 N  N   . ASN   D 266 ? 1.4616 1.3687 1.2850 0.1145  -0.1154 -0.0639 335  ASN   D N   
10770 C  CA  . ASN   D 266 ? 1.5155 1.4267 1.3448 0.1182  -0.1192 -0.0680 335  ASN   D CA  
10771 C  C   . ASN   D 266 ? 1.5178 1.4132 1.3295 0.1280  -0.1217 -0.0696 335  ASN   D C   
10772 O  O   . ASN   D 266 ? 1.5177 1.4142 1.3317 0.1323  -0.1248 -0.0729 335  ASN   D O   
10773 C  CB  . ASN   D 266 ? 1.4950 1.4215 1.3427 0.1199  -0.1261 -0.0724 335  ASN   D CB  
10774 C  CG  . ASN   D 266 ? 1.5284 1.4507 1.3716 0.1276  -0.1327 -0.0748 335  ASN   D CG  
10775 O  OD1 . ASN   D 266 ? 1.5434 1.4502 1.3679 0.1330  -0.1325 -0.0735 335  ASN   D OD1 
10776 N  ND2 . ASN   D 266 ? 1.5901 1.5254 1.4497 0.1284  -0.1388 -0.0784 335  ASN   D ND2 
10777 N  N   . GLU   D 267 ? 1.4198 1.3000 1.2136 0.1317  -0.1201 -0.0673 336  GLU   D N   
10778 C  CA  . GLU   D 267 ? 1.3433 1.2060 1.1176 0.1404  -0.1212 -0.0679 336  GLU   D CA  
10779 C  C   . GLU   D 267 ? 1.3227 1.1740 1.0848 0.1364  -0.1131 -0.0638 336  GLU   D C   
10780 O  O   . GLU   D 267 ? 1.3413 1.1782 1.0877 0.1430  -0.1133 -0.0642 336  GLU   D O   
10781 C  CB  . GLU   D 267 ? 1.3440 1.1949 1.1042 0.1477  -0.1239 -0.0677 336  GLU   D CB  
10782 C  CG  . GLU   D 267 ? 1.3713 1.2130 1.1213 0.1601  -0.1319 -0.0723 336  GLU   D CG  
10783 C  CD  . GLU   D 267 ? 1.3730 1.2293 1.1405 0.1637  -0.1412 -0.0782 336  GLU   D CD  
10784 O  OE1 . GLU   D 267 ? 1.4454 1.3126 1.2252 0.1604  -0.1434 -0.0787 336  GLU   D OE1 
10785 O  OE2 . GLU   D 267 ? 1.3980 1.2547 1.1673 0.1698  -0.1463 -0.0824 336  GLU   D OE2 
10786 N  N   . ILE   D 268 ? 1.3141 1.1714 1.0832 0.1259  -0.1064 -0.0599 337  ILE   D N   
10787 C  CA  . ILE   D 268 ? 1.3104 1.1564 1.0683 0.1217  -0.0990 -0.0559 337  ILE   D CA  
10788 C  C   . ILE   D 268 ? 1.3211 1.1666 1.0792 0.1231  -0.0997 -0.0582 337  ILE   D C   
10789 O  O   . ILE   D 268 ? 1.3333 1.1928 1.1067 0.1217  -0.1029 -0.0613 337  ILE   D O   
10790 C  CB  . ILE   D 268 ? 1.2485 1.1017 1.0151 0.1101  -0.0925 -0.0516 337  ILE   D CB  
10791 C  CG1 . ILE   D 268 ? 1.2287 1.0800 0.9927 0.1092  -0.0909 -0.0488 337  ILE   D CG1 
10792 C  CG2 . ILE   D 268 ? 1.2665 1.1093 1.0239 0.1055  -0.0857 -0.0482 337  ILE   D CG2 
10793 C  CD1 . ILE   D 268 ? 1.1679 1.0212 0.9357 0.0989  -0.0835 -0.0439 337  ILE   D CD1 
10794 N  N   . PHE   D 269 ? 1.3453 1.1744 1.0865 0.1257  -0.0963 -0.0565 338  PHE   D N   
10795 C  CA  . PHE   D 269 ? 1.3049 1.1319 1.0445 0.1271  -0.0964 -0.0583 338  PHE   D CA  
10796 C  C   . PHE   D 269 ? 1.3053 1.1164 1.0296 0.1242  -0.0895 -0.0544 338  PHE   D C   
10797 O  O   . PHE   D 269 ? 1.3056 1.1050 1.0182 0.1236  -0.0852 -0.0507 338  PHE   D O   
10798 C  CB  . PHE   D 269 ? 1.3466 1.1705 1.0819 0.1386  -0.1038 -0.0634 338  PHE   D CB  
10799 C  CG  . PHE   D 269 ? 1.3644 1.1672 1.0768 0.1471  -0.1035 -0.0629 338  PHE   D CG  
10800 C  CD1 . PHE   D 269 ? 1.3792 1.1749 1.0843 0.1535  -0.1057 -0.0655 338  PHE   D CD1 
10801 C  CD2 . PHE   D 269 ? 1.3929 1.1826 1.0908 0.1493  -0.1011 -0.0598 338  PHE   D CD2 
10802 C  CE1 . PHE   D 269 ? 1.3590 1.1347 1.0423 0.1616  -0.1055 -0.0651 338  PHE   D CE1 
10803 C  CE2 . PHE   D 269 ? 1.4337 1.2031 1.1096 0.1575  -0.1005 -0.0592 338  PHE   D CE2 
10804 C  CZ  . PHE   D 269 ? 1.3997 1.1620 1.0682 0.1636  -0.1029 -0.0619 338  PHE   D CZ  
10805 N  N   . SER   D 270 ? 1.3923 1.2031 1.1173 0.1223  -0.0881 -0.0552 339  SER   D N   
10806 C  CA  . SER   D 270 ? 1.4359 1.2322 1.1477 0.1193  -0.0820 -0.0520 339  SER   D CA  
10807 C  C   . SER   D 270 ? 1.4964 1.2797 1.1939 0.1289  -0.0847 -0.0545 339  SER   D C   
10808 O  O   . SER   D 270 ? 1.4810 1.2708 1.1846 0.1324  -0.0886 -0.0583 339  SER   D O   
10809 C  CB  . SER   D 270 ? 1.4556 1.2601 1.1778 0.1095  -0.0785 -0.0508 339  SER   D CB  
10810 O  OG  . SER   D 270 ? 1.4565 1.2619 1.1819 0.1002  -0.0732 -0.0465 339  SER   D OG  
10811 N  N   . LEU   D 271 ? 1.5744 1.3394 1.2531 0.1337  -0.0823 -0.0523 340  LEU   D N   
10812 C  CA  . LEU   D 271 ? 1.6845 1.4348 1.3471 0.1432  -0.0844 -0.0543 340  LEU   D CA  
10813 C  C   . LEU   D 271 ? 1.7979 1.5379 1.4525 0.1386  -0.0787 -0.0520 340  LEU   D C   
10814 O  O   . LEU   D 271 ? 1.7520 1.4944 1.4091 0.1396  -0.0804 -0.0545 340  LEU   D O   
10815 C  CB  . LEU   D 271 ? 1.6069 1.3414 1.2518 0.1514  -0.0849 -0.0532 340  LEU   D CB  
10816 C  CG  . LEU   D 271 ? 1.5587 1.2746 1.1838 0.1610  -0.0860 -0.0544 340  LEU   D CG  
10817 C  CD1 . LEU   D 271 ? 1.5012 1.2125 1.1184 0.1729  -0.0929 -0.0577 340  LEU   D CD1 
10818 C  CD2 . LEU   D 271 ? 1.6351 1.3318 1.2430 0.1580  -0.0777 -0.0493 340  LEU   D CD2 
10819 N  N   . SER   D 272 ? 2.2573 1.9859 1.9030 0.1332  -0.0719 -0.0471 341  SER   D N   
10820 C  CA  . SER   D 272 ? 2.2933 2.0127 1.9331 0.1274  -0.0663 -0.0446 341  SER   D CA  
10821 C  C   . SER   D 272 ? 2.2790 2.0143 1.9365 0.1177  -0.0658 -0.0451 341  SER   D C   
10822 O  O   . SER   D 272 ? 2.2497 2.0026 1.9238 0.1143  -0.0683 -0.0463 341  SER   D O   
10823 C  CB  . SER   D 272 ? 2.3158 2.0210 1.9448 0.1232  -0.0590 -0.0392 341  SER   D CB  
10824 O  OG  . SER   D 272 ? 2.3905 2.0882 2.0164 0.1162  -0.0538 -0.0368 341  SER   D OG  
10825 N  N   . LEU   D 273 ? 1.9656 1.6939 1.6187 0.1136  -0.0625 -0.0441 342  LEU   D N   
10826 C  CA  . LEU   D 273 ? 1.8442 1.5844 1.5113 0.1041  -0.0612 -0.0440 342  LEU   D CA  
10827 C  C   . LEU   D 273 ? 1.8455 1.5873 1.5182 0.0937  -0.0561 -0.0396 342  LEU   D C   
10828 O  O   . LEU   D 273 ? 1.8229 1.5722 1.5054 0.0852  -0.0547 -0.0390 342  LEU   D O   
10829 C  CB  . LEU   D 273 ? 1.7594 1.4908 1.4191 0.1040  -0.0602 -0.0449 342  LEU   D CB  
10830 C  CG  . LEU   D 273 ? 1.7285 1.4543 1.3793 0.1148  -0.0643 -0.0488 342  LEU   D CG  
10831 C  CD1 . LEU   D 273 ? 1.4998 1.2258 1.1516 0.1129  -0.0642 -0.0505 342  LEU   D CD1 
10832 C  CD2 . LEU   D 273 ? 1.7420 1.4812 1.4024 0.1216  -0.0705 -0.0525 342  LEU   D CD2 
10833 N  N   . CYS   D 274 ? 1.8654 1.6002 1.5320 0.0944  -0.0533 -0.0366 343  CYS   D N   
10834 C  CA  . CYS   D 274 ? 1.8154 1.5518 1.4878 0.0852  -0.0482 -0.0323 343  CYS   D CA  
10835 C  C   . CYS   D 274 ? 1.7357 1.4898 1.4241 0.0819  -0.0502 -0.0325 343  CYS   D C   
10836 O  O   . CYS   D 274 ? 1.7111 1.4684 1.4061 0.0742  -0.0463 -0.0291 343  CYS   D O   
10837 C  CB  . CYS   D 274 ? 1.9071 1.6256 1.5643 0.0875  -0.0430 -0.0285 343  CYS   D CB  
10838 S  SG  . CYS   D 274 ? 2.0906 1.7857 1.7277 0.0905  -0.0393 -0.0273 343  CYS   D SG  
10839 N  N   . GLY   D 275 ? 1.6987 1.4640 1.3936 0.0877  -0.0561 -0.0362 344  GLY   D N   
10840 C  CA  . GLY   D 275 ? 1.5572 1.3388 1.2670 0.0848  -0.0581 -0.0364 344  GLY   D CA  
10841 C  C   . GLY   D 275 ? 1.4627 1.2434 1.1683 0.0931  -0.0613 -0.0374 344  GLY   D C   
10842 O  O   . GLY   D 275 ? 1.5390 1.3069 1.2300 0.1021  -0.0627 -0.0385 344  GLY   D O   
10843 N  N   . PRO   D 276 ? 1.4089 1.2028 1.1268 0.0905  -0.0628 -0.0373 345  PRO   D N   
10844 C  CA  . PRO   D 276 ? 1.3776 1.1713 1.0922 0.0982  -0.0663 -0.0385 345  PRO   D CA  
10845 C  C   . PRO   D 276 ? 1.3225 1.1048 1.0268 0.0981  -0.0613 -0.0342 345  PRO   D C   
10846 O  O   . PRO   D 276 ? 1.2997 1.0750 0.9944 0.1061  -0.0633 -0.0347 345  PRO   D O   
10847 C  CB  . PRO   D 276 ? 1.3531 1.1673 1.0871 0.0947  -0.0703 -0.0406 345  PRO   D CB  
10848 C  CG  . PRO   D 276 ? 1.3305 1.1517 1.0748 0.0832  -0.0655 -0.0376 345  PRO   D CG  
10849 C  CD  . PRO   D 276 ? 1.4153 1.2256 1.1510 0.0809  -0.0620 -0.0365 345  PRO   D CD  
10850 N  N   . MET   D 277 ? 1.3588 1.1388 1.0650 0.0892  -0.0546 -0.0299 346  MET   D N   
10851 C  CA  . MET   D 277 ? 1.2525 1.0215 0.9500 0.0881  -0.0485 -0.0252 346  MET   D CA  
10852 C  C   . MET   D 277 ? 1.3171 1.0735 1.0075 0.0826  -0.0415 -0.0215 346  MET   D C   
10853 O  O   . MET   D 277 ? 1.1777 0.9358 0.8745 0.0740  -0.0361 -0.0178 346  MET   D O   
10854 C  CB  . MET   D 277 ? 1.1861 0.9684 0.8976 0.0819  -0.0474 -0.0234 346  MET   D CB  
10855 C  CG  . MET   D 277 ? 1.2326 1.0072 0.9356 0.0861  -0.0448 -0.0208 346  MET   D CG  
10856 S  SD  . MET   D 277 ? 1.2962 1.0856 1.0168 0.0759  -0.0415 -0.0176 346  MET   D SD  
10857 C  CE  . MET   D 277 ? 1.2524 1.0373 0.9760 0.0651  -0.0339 -0.0135 346  MET   D CE  
10858 N  N   . ALA   D 278 ? 1.3627 1.1059 1.0397 0.0877  -0.0417 -0.0226 347  ALA   D N   
10859 C  CA  . ALA   D 278 ? 1.3716 1.1019 1.0415 0.0825  -0.0350 -0.0190 347  ALA   D CA  
10860 C  C   . ALA   D 278 ? 1.2727 0.9878 0.9300 0.0846  -0.0284 -0.0145 347  ALA   D C   
10861 O  O   . ALA   D 278 ? 1.3000 1.0113 0.9497 0.0922  -0.0296 -0.0146 347  ALA   D O   
10862 C  CB  . ALA   D 278 ? 1.4788 1.1990 1.1382 0.0868  -0.0367 -0.0214 347  ALA   D CB  
10863 N  N   . ALA   D 279 ? 1.2415 0.9478 0.8971 0.0777  -0.0212 -0.0103 348  ALA   D N   
10864 C  CA  . ALA   D 279 ? 1.2736 0.9642 0.9173 0.0791  -0.0135 -0.0055 348  ALA   D CA  
10865 C  C   . ALA   D 279 ? 1.3671 1.0361 0.9897 0.0862  -0.0114 -0.0051 348  ALA   D C   
10866 O  O   . ALA   D 279 ? 1.4620 1.1254 1.0824 0.0832  -0.0106 -0.0055 348  ALA   D O   
10867 C  CB  . ALA   D 279 ? 1.2428 0.9355 0.8972 0.0675  -0.0065 -0.0010 348  ALA   D CB  
10868 N  N   . TYR   D 280 ? 1.3096 0.9658 0.9160 0.0959  -0.0104 -0.0043 349  TYR   D N   
10869 C  CA  . TYR   D 280 ? 1.3016 0.9357 0.8863 0.1034  -0.0077 -0.0034 349  TYR   D CA  
10870 C  C   . TYR   D 280 ? 1.3880 1.0065 0.9628 0.1023  0.0023  0.0027  349  TYR   D C   
10871 O  O   . TYR   D 280 ? 1.3518 0.9765 0.9344 0.0986  0.0060  0.0056  349  TYR   D O   
10872 C  CB  . TYR   D 280 ? 1.3851 1.0149 0.9570 0.1165  -0.0150 -0.0076 349  TYR   D CB  
10873 C  CG  . TYR   D 280 ? 1.4178 1.0659 1.0030 0.1171  -0.0246 -0.0135 349  TYR   D CG  
10874 C  CD1 . TYR   D 280 ? 1.4193 1.0866 1.0205 0.1152  -0.0293 -0.0155 349  TYR   D CD1 
10875 C  CD2 . TYR   D 280 ? 1.4267 1.0728 1.0090 0.1193  -0.0285 -0.0169 349  TYR   D CD2 
10876 C  CE1 . TYR   D 280 ? 1.4388 1.1228 1.0530 0.1154  -0.0374 -0.0206 349  TYR   D CE1 
10877 C  CE2 . TYR   D 280 ? 1.4257 1.0887 1.0210 0.1197  -0.0365 -0.0220 349  TYR   D CE2 
10878 C  CZ  . TYR   D 280 ? 1.4540 1.1356 1.0652 0.1177  -0.0407 -0.0237 349  TYR   D CZ  
10879 O  OH  . TYR   D 280 ? 1.6031 1.3009 1.2273 0.1181  -0.0480 -0.0286 349  TYR   D OH  
10880 N  N   . VAL   D 281 ? 1.4692 1.0672 1.0272 0.1051  0.0074  0.0048  350  VAL   D N   
10881 C  CA  . VAL   D 281 ? 1.4509 1.0323 0.9988 0.1041  0.0179  0.0109  350  VAL   D CA  
10882 C  C   . VAL   D 281 ? 1.4946 1.0546 1.0166 0.1173  0.0188  0.0112  350  VAL   D C   
10883 O  O   . VAL   D 281 ? 1.5195 1.0680 1.0284 0.1228  0.0163  0.0091  350  VAL   D O   
10884 C  CB  . VAL   D 281 ? 1.4326 1.0075 0.9849 0.0941  0.0250  0.0143  350  VAL   D CB  
10885 C  CG1 . VAL   D 281 ? 1.5733 1.1315 1.1093 0.0987  0.0244  0.0129  350  VAL   D CG1 
10886 C  CG2 . VAL   D 281 ? 1.4095 0.9737 0.9591 0.0906  0.0363  0.0209  350  VAL   D CG2 
10887 N  N   . ASN   D 282 ? 1.5333 1.0879 1.0473 0.1228  0.0218  0.0137  351  ASN   D N   
10888 C  CA  . ASN   D 282 ? 1.5343 1.0667 1.0221 0.1356  0.0235  0.0145  351  ASN   D CA  
10889 C  C   . ASN   D 282 ? 1.5675 1.0783 1.0421 0.1336  0.0339  0.0196  351  ASN   D C   
10890 O  O   . ASN   D 282 ? 1.5247 1.0395 1.0125 0.1220  0.0396  0.0225  351  ASN   D O   
10891 C  CB  . ASN   D 282 ? 1.4570 0.9880 0.9391 0.1416  0.0249  0.0162  351  ASN   D CB  
10892 C  CG  . ASN   D 282 ? 1.5080 1.0290 0.9880 0.1367  0.0378  0.0235  351  ASN   D CG  
10893 O  OD1 . ASN   D 282 ? 1.5300 1.0503 1.0189 0.1266  0.0451  0.0271  351  ASN   D OD1 
10894 N  ND2 . ASN   D 282 ? 1.5195 1.0327 0.9880 0.1441  0.0405  0.0256  351  ASN   D ND2 
10895 N  N   . PRO   D 283 ? 1.6026 1.0900 1.0514 0.1445  0.0365  0.0208  352  PRO   D N   
10896 C  CA  . PRO   D 283 ? 1.5775 1.0430 1.0127 0.1431  0.0466  0.0257  352  PRO   D CA  
10897 C  C   . PRO   D 283 ? 1.5410 0.9987 0.9768 0.1380  0.0593  0.0328  352  PRO   D C   
10898 O  O   . PRO   D 283 ? 1.5788 1.0145 0.9984 0.1401  0.0686  0.0374  352  PRO   D O   
10899 C  CB  . PRO   D 283 ? 1.5569 1.0008 0.9637 0.1580  0.0440  0.0240  352  PRO   D CB  
10900 C  CG  . PRO   D 283 ? 1.5907 1.0456 0.9972 0.1671  0.0328  0.0186  352  PRO   D CG  
10901 C  CD  . PRO   D 283 ? 1.6236 1.1028 1.0544 0.1588  0.0309  0.0182  352  PRO   D CD  
10902 N  N   . HIS   D 284 ? 1.5062 0.9814 0.9606 0.1314  0.0602  0.0340  353  HIS   D N   
10903 C  CA  . HIS   D 284 ? 1.5253 0.9955 0.9837 0.1254  0.0725  0.0408  353  HIS   D CA  
10904 C  C   . HIS   D 284 ? 1.5211 1.0133 1.0087 0.1109  0.0734  0.0416  353  HIS   D C   
10905 O  O   . HIS   D 284 ? 1.5444 1.0397 1.0407 0.1060  0.0812  0.0462  353  HIS   D O   
10906 C  CB  . HIS   D 284 ? 1.5919 1.0564 1.0388 0.1342  0.0749  0.0428  353  HIS   D CB  
10907 C  CG  . HIS   D 284 ? 1.6783 1.1155 1.0943 0.1473  0.0786  0.0445  353  HIS   D CG  
10908 N  ND1 . HIS   D 284 ? 1.7230 1.1397 1.1254 0.1486  0.0919  0.0514  353  HIS   D ND1 
10909 C  CD2 . HIS   D 284 ? 1.6766 1.1034 1.0725 0.1601  0.0707  0.0403  353  HIS   D CD2 
10910 C  CE1 . HIS   D 284 ? 1.7381 1.1322 1.1122 0.1618  0.0921  0.0513  353  HIS   D CE1 
10911 N  NE2 . HIS   D 284 ? 1.7080 1.1079 1.0778 0.1690  0.0790  0.0445  353  HIS   D NE2 
10912 N  N   . GLY   D 285 ? 1.5665 1.0740 1.0692 0.1045  0.0655  0.0371  354  GLY   D N   
10913 C  CA  . GLY   D 285 ? 1.5710 1.0995 1.1007 0.0913  0.0649  0.0371  354  GLY   D CA  
10914 C  C   . GLY   D 285 ? 1.5293 1.0798 1.0744 0.0903  0.0587  0.0347  354  GLY   D C   
10915 O  O   . GLY   D 285 ? 1.5183 1.0885 1.0854 0.0807  0.0550  0.0329  354  GLY   D O   
10916 N  N   . TYR   D 286 ? 1.4951 1.0425 1.0291 0.1000  0.0576  0.0346  355  TYR   D N   
10917 C  CA  . TYR   D 286 ? 1.3679 0.9354 0.9149 0.1002  0.0504  0.0314  355  TYR   D CA  
10918 C  C   . TYR   D 286 ? 1.3779 0.9622 0.9364 0.0983  0.0388  0.0250  355  TYR   D C   
10919 O  O   . TYR   D 286 ? 1.3847 0.9617 0.9320 0.1041  0.0336  0.0215  355  TYR   D O   
10920 C  CB  . TYR   D 286 ? 1.4090 0.9669 0.9375 0.1132  0.0489  0.0311  355  TYR   D CB  
10921 C  CG  . TYR   D 286 ? 1.4693 1.0125 0.9876 0.1153  0.0606  0.0376  355  TYR   D CG  
10922 C  CD1 . TYR   D 286 ? 1.4355 0.9905 0.9691 0.1089  0.0653  0.0407  355  TYR   D CD1 
10923 C  CD2 . TYR   D 286 ? 1.5103 1.0276 1.0031 0.1241  0.0670  0.0406  355  TYR   D CD2 
10924 C  CE1 . TYR   D 286 ? 1.3613 0.9033 0.8860 0.1110  0.0763  0.0467  355  TYR   D CE1 
10925 C  CE2 . TYR   D 286 ? 1.4584 0.9618 0.9414 0.1264  0.0783  0.0467  355  TYR   D CE2 
10926 C  CZ  . TYR   D 286 ? 1.4255 0.9419 0.9252 0.1197  0.0829  0.0498  355  TYR   D CZ  
10927 O  OH  . TYR   D 286 ? 1.5909 1.0946 1.0823 0.1216  0.0945  0.0560  355  TYR   D OH  
10928 N  N   . VAL   D 287 ? 1.3452 0.9519 0.9264 0.0900  0.0350  0.0234  356  VAL   D N   
10929 C  CA  . VAL   D 287 ? 1.3654 0.9891 0.9591 0.0876  0.0247  0.0177  356  VAL   D CA  
10930 C  C   . VAL   D 287 ? 1.3642 1.0027 0.9637 0.0924  0.0169  0.0140  356  VAL   D C   
10931 O  O   . VAL   D 287 ? 1.3744 1.0202 0.9814 0.0903  0.0194  0.0162  356  VAL   D O   
10932 C  CB  . VAL   D 287 ? 1.2846 0.9224 0.8999 0.0740  0.0258  0.0183  356  VAL   D CB  
10933 C  CG1 . VAL   D 287 ? 1.2328 0.8820 0.8556 0.0726  0.0165  0.0126  356  VAL   D CG1 
10934 C  CG2 . VAL   D 287 ? 1.3564 0.9799 0.9684 0.0682  0.0354  0.0232  356  VAL   D CG2 
10935 N  N   . HIS   D 288 ? 1.3094 0.9529 0.9066 0.0984  0.0073  0.0084  357  HIS   D N   
10936 C  CA  . HIS   D 288 ? 1.2851 0.9436 0.8896 0.1025  -0.0012 0.0042  357  HIS   D CA  
10937 C  C   . HIS   D 288 ? 1.3078 0.9844 0.9288 0.0975  -0.0088 -0.0005 357  HIS   D C   
10938 O  O   . HIS   D 288 ? 1.2587 0.9317 0.8740 0.1013  -0.0134 -0.0039 357  HIS   D O   
10939 C  CB  . HIS   D 288 ? 1.3089 0.9557 0.8942 0.1164  -0.0061 0.0015  357  HIS   D CB  
10940 C  CG  . HIS   D 288 ? 1.4133 1.0406 0.9796 0.1230  0.0011  0.0058  357  HIS   D CG  
10941 N  ND1 . HIS   D 288 ? 1.3612 0.9903 0.9264 0.1264  0.0018  0.0072  357  HIS   D ND1 
10942 C  CD2 . HIS   D 288 ? 1.3574 0.9621 0.9039 0.1273  0.0079  0.0091  357  HIS   D CD2 
10943 C  CE1 . HIS   D 288 ? 1.4144 1.0228 0.9599 0.1325  0.0091  0.0112  357  HIS   D CE1 
10944 N  NE2 . HIS   D 288 ? 1.3288 0.9221 0.8627 0.1332  0.0130  0.0126  357  HIS   D NE2 
10945 N  N   . GLU   D 289 ? 1.3632 1.0591 1.0045 0.0894  -0.0102 -0.0007 358  GLU   D N   
10946 C  CA  . GLU   D 289 ? 1.2976 1.0117 0.9533 0.0875  -0.0188 -0.0057 358  GLU   D CA  
10947 C  C   . GLU   D 289 ? 1.2819 0.9975 0.9313 0.0983  -0.0266 -0.0100 358  GLU   D C   
10948 O  O   . GLU   D 289 ? 1.2545 0.9734 0.9045 0.1013  -0.0273 -0.0095 358  GLU   D O   
10949 C  CB  . GLU   D 289 ? 1.2252 0.9587 0.9026 0.0773  -0.0187 -0.0049 358  GLU   D CB  
10950 C  CG  . GLU   D 289 ? 1.2355 0.9695 0.9218 0.0660  -0.0115 -0.0007 358  GLU   D CG  
10951 C  CD  . GLU   D 289 ? 1.2669 1.0027 0.9586 0.0620  -0.0053 0.0039  358  GLU   D CD  
10952 O  OE1 . GLU   D 289 ? 1.2714 0.9936 0.9491 0.0683  -0.0008 0.0066  358  GLU   D OE1 
10953 O  OE2 . GLU   D 289 ? 1.2073 0.9575 0.9167 0.0529  -0.0047 0.0048  358  GLU   D OE2 
10954 N  N   . THR   D 290 ? 1.2722 0.9850 0.9154 0.1046  -0.0325 -0.0142 359  THR   D N   
10955 C  CA  . THR   D 290 ? 1.2647 0.9766 0.9005 0.1158  -0.0402 -0.0185 359  THR   D CA  
10956 C  C   . THR   D 290 ? 1.2422 0.9731 0.8943 0.1149  -0.0487 -0.0239 359  THR   D C   
10957 O  O   . THR   D 290 ? 1.2995 1.0316 0.9531 0.1145  -0.0511 -0.0264 359  THR   D O   
10958 C  CB  . THR   D 290 ? 1.2854 0.9769 0.8993 0.1255  -0.0403 -0.0192 359  THR   D CB  
10959 O  OG1 . THR   D 290 ? 1.3155 0.9890 0.9149 0.1255  -0.0312 -0.0137 359  THR   D OG1 
10960 C  CG2 . THR   D 290 ? 1.2489 0.9382 0.8543 0.1378  -0.0485 -0.0235 359  THR   D CG2 
10961 N  N   . LEU   D 291 ? 1.2029 0.9479 0.8666 0.1148  -0.0530 -0.0255 360  LEU   D N   
10962 C  CA  . LEU   D 291 ? 1.2505 1.0123 0.9285 0.1156  -0.0613 -0.0308 360  LEU   D CA  
10963 C  C   . LEU   D 291 ? 1.2237 0.9778 0.8904 0.1274  -0.0681 -0.0352 360  LEU   D C   
10964 O  O   . LEU   D 291 ? 1.2699 1.0111 0.9212 0.1361  -0.0690 -0.0350 360  LEU   D O   
10965 C  CB  . LEU   D 291 ? 1.1922 0.9694 0.8844 0.1131  -0.0640 -0.0313 360  LEU   D CB  
10966 C  CG  . LEU   D 291 ? 1.2178 1.0137 0.9271 0.1129  -0.0720 -0.0363 360  LEU   D CG  
10967 C  CD1 . LEU   D 291 ? 1.1587 0.9651 0.8810 0.1044  -0.0707 -0.0367 360  LEU   D CD1 
10968 C  CD2 . LEU   D 291 ? 1.2337 1.0425 0.9550 0.1107  -0.0741 -0.0364 360  LEU   D CD2 
10969 N  N   . THR   D 292 ? 1.2175 0.9790 0.8912 0.1282  -0.0729 -0.0392 361  THR   D N   
10970 C  CA  . THR   D 292 ? 1.2796 1.0371 0.9463 0.1391  -0.0804 -0.0440 361  THR   D CA  
10971 C  C   . THR   D 292 ? 1.3137 1.0894 0.9972 0.1407  -0.0885 -0.0486 361  THR   D C   
10972 O  O   . THR   D 292 ? 1.2957 1.0886 0.9979 0.1334  -0.0892 -0.0495 361  THR   D O   
10973 C  CB  . THR   D 292 ? 1.3137 1.0666 0.9767 0.1398  -0.0804 -0.0455 361  THR   D CB  
10974 O  OG1 . THR   D 292 ? 1.3326 1.0990 1.0117 0.1294  -0.0779 -0.0450 361  THR   D OG1 
10975 C  CG2 . THR   D 292 ? 1.3195 1.0505 0.9618 0.1416  -0.0738 -0.0417 361  THR   D CG2 
10976 N  N   . VAL   D 293 ? 1.3004 1.0720 0.9772 0.1501  -0.0943 -0.0511 362  VAL   D N   
10977 C  CA  . VAL   D 293 ? 1.3618 1.1497 1.0545 0.1522  -0.1026 -0.0558 362  VAL   D CA  
10978 C  C   . VAL   D 293 ? 1.3543 1.1368 1.0402 0.1638  -0.1108 -0.0610 362  VAL   D C   
10979 O  O   . VAL   D 293 ? 1.3718 1.1361 1.0377 0.1717  -0.1105 -0.0607 362  VAL   D O   
10980 C  CB  . VAL   D 293 ? 1.2407 1.0325 0.9363 0.1520  -0.1036 -0.0548 362  VAL   D CB  
10981 C  CG1 . VAL   D 293 ? 1.2228 1.0165 0.9218 0.1416  -0.0949 -0.0491 362  VAL   D CG1 
10982 C  CG2 . VAL   D 293 ? 1.2817 1.0563 0.9572 0.1631  -0.1063 -0.0553 362  VAL   D CG2 
10983 N  N   . TYR   D 294 ? 1.3612 1.1599 1.0645 0.1649  -0.1180 -0.0659 363  TYR   D N   
10984 C  CA  . TYR   D 294 ? 1.3714 1.1671 1.0712 0.1760  -0.1268 -0.0714 363  TYR   D CA  
10985 C  C   . TYR   D 294 ? 1.3256 1.1131 1.0151 0.1853  -0.1330 -0.0733 363  TYR   D C   
10986 O  O   . TYR   D 294 ? 1.2831 1.0561 0.9561 0.1959  -0.1371 -0.0755 363  TYR   D O   
10987 C  CB  . TYR   D 294 ? 1.3448 1.1607 1.0679 0.1738  -0.1321 -0.0759 363  TYR   D CB  
10988 N  N   . LYS   D 295 ? 1.3294 1.1253 1.0275 0.1818  -0.1336 -0.0726 364  LYS   D N   
10989 C  CA  . LYS   D 295 ? 1.3573 1.1468 1.0472 0.1901  -0.1398 -0.0745 364  LYS   D CA  
10990 C  C   . LYS   D 295 ? 1.3343 1.1188 1.0175 0.1855  -0.1332 -0.0693 364  LYS   D C   
10991 O  O   . LYS   D 295 ? 1.3660 1.1628 1.0632 0.1748  -0.1279 -0.0664 364  LYS   D O   
10992 C  CB  . LYS   D 295 ? 1.2085 1.0152 0.9184 0.1922  -0.1500 -0.0804 364  LYS   D CB  
10993 N  N   . ALA   D 296 ? 1.3614 1.1272 1.0227 0.1937  -0.1332 -0.0681 365  ALA   D N   
10994 C  CA  . ALA   D 296 ? 1.3660 1.1256 1.0194 0.1915  -0.1276 -0.0635 365  ALA   D CA  
10995 C  C   . ALA   D 296 ? 1.4320 1.1832 1.0745 0.2024  -0.1355 -0.0667 365  ALA   D C   
10996 O  O   . ALA   D 296 ? 1.4331 1.1750 1.0651 0.2132  -0.1431 -0.0709 365  ALA   D O   
10997 C  CB  . ALA   D 296 ? 1.3426 1.0840 0.9765 0.1900  -0.1169 -0.0573 365  ALA   D CB  
10998 N  N   . CYS   D 297 ? 1.3963 1.1499 1.0405 0.1999  -0.1338 -0.0645 366  CYS   D N   
10999 C  CA  . CYS   D 297 ? 1.4414 1.1895 1.0781 0.2092  -0.1418 -0.0677 366  CYS   D CA  
11000 C  C   . CYS   D 297 ? 1.4556 1.1882 1.0736 0.2110  -0.1348 -0.0625 366  CYS   D C   
11001 O  O   . CYS   D 297 ? 1.3947 1.1247 1.0105 0.2034  -0.1237 -0.0564 366  CYS   D O   
11002 C  CB  . CYS   D 297 ? 1.4834 1.2528 1.1443 0.2053  -0.1492 -0.0718 366  CYS   D CB  
11003 S  SG  . CYS   D 297 ? 1.8200 1.6026 1.4979 0.2095  -0.1617 -0.0799 366  CYS   D SG  
11004 N  N   . ASN   D 298 ? 1.4890 1.2107 1.0934 0.2215  -0.1414 -0.0651 367  ASN   D N   
11005 C  CA  . ASN   D 298 ? 1.4315 1.1378 1.0172 0.2248  -0.1355 -0.0606 367  ASN   D CA  
11006 C  C   . ASN   D 298 ? 1.3916 1.0790 0.9568 0.2253  -0.1242 -0.0546 367  ASN   D C   
11007 O  O   . ASN   D 298 ? 1.3971 1.0785 0.9559 0.2213  -0.1143 -0.0487 367  ASN   D O   
11008 C  CB  . ASN   D 298 ? 1.4096 1.1298 1.0107 0.2150  -0.1308 -0.0575 367  ASN   D CB  
11009 C  CG  . ASN   D 298 ? 1.4398 1.1800 1.0633 0.2128  -0.1407 -0.0629 367  ASN   D CG  
11010 O  OD1 . ASN   D 298 ? 1.4956 1.2369 1.1207 0.2204  -0.1519 -0.0691 367  ASN   D OD1 
11011 N  ND2 . ASN   D 298 ? 1.5105 1.2665 1.1518 0.2024  -0.1368 -0.0605 367  ASN   D ND2 
11012 N  N   . LEU   D 299 ? 1.4207 1.0988 0.9764 0.2297  -0.1250 -0.0558 368  LEU   D N   
11013 C  CA  . LEU   D 299 ? 1.4431 1.1016 0.9782 0.2308  -0.1145 -0.0503 368  LEU   D CA  
11014 C  C   . LEU   D 299 ? 1.4623 1.0967 0.9691 0.2459  -0.1189 -0.0521 368  LEU   D C   
11015 O  O   . LEU   D 299 ? 1.5400 1.1741 1.0454 0.2545  -0.1303 -0.0584 368  LEU   D O   
11016 C  CB  . LEU   D 299 ? 1.4299 1.0941 0.9738 0.2233  -0.1100 -0.0491 368  LEU   D CB  
11017 C  CG  . LEU   D 299 ? 1.4295 1.1153 0.9991 0.2082  -0.1046 -0.0466 368  LEU   D CG  
11018 C  CD1 . LEU   D 299 ? 1.3202 1.0031 0.8895 0.2012  -0.0958 -0.0428 368  LEU   D CD1 
11019 C  CD2 . LEU   D 299 ? 1.3565 1.0460 0.9300 0.2026  -0.0985 -0.0423 368  LEU   D CD2 
11020 N  N   . ASN   D 300 ? 1.4352 1.0494 0.9197 0.2495  -0.1100 -0.0467 369  ASN   D N   
11021 C  CA  . ASN   D 300 ? 1.4670 1.0557 0.9221 0.2635  -0.1121 -0.0475 369  ASN   D CA  
11022 C  C   . ASN   D 300 ? 1.4936 1.0709 0.9388 0.2615  -0.1035 -0.0438 369  ASN   D C   
11023 O  O   . ASN   D 300 ? 1.5290 1.1075 0.9785 0.2516  -0.0915 -0.0376 369  ASN   D O   
11024 C  CB  . ASN   D 300 ? 1.5483 1.1192 0.9822 0.2703  -0.1076 -0.0439 369  ASN   D CB  
11025 C  CG  . ASN   D 300 ? 1.6081 1.1828 1.0430 0.2778  -0.1194 -0.0493 369  ASN   D CG  
11026 O  OD1 . ASN   D 300 ? 1.6330 1.2180 1.0785 0.2814  -0.1322 -0.0563 369  ASN   D OD1 
11027 N  ND2 . ASN   D 300 ? 1.5811 1.1469 1.0048 0.2803  -0.1150 -0.0460 369  ASN   D ND2 
11028 N  N   . LEU   D 301 ? 1.5400 1.1073 0.9735 0.2706  -0.1102 -0.0477 370  LEU   D N   
11029 C  CA  . LEU   D 301 ? 1.5077 1.0610 0.9283 0.2705  -0.1028 -0.0445 370  LEU   D CA  
11030 C  C   . LEU   D 301 ? 1.5178 1.0421 0.9066 0.2793  -0.0949 -0.0397 370  LEU   D C   
11031 O  O   . LEU   D 301 ? 1.6096 1.1198 0.9798 0.2917  -0.1011 -0.0421 370  LEU   D O   
11032 C  CB  . LEU   D 301 ? 1.5170 1.0706 0.9373 0.2773  -0.1129 -0.0507 370  LEU   D CB  
11033 C  CG  . LEU   D 301 ? 1.5026 1.0812 0.9500 0.2737  -0.1240 -0.0574 370  LEU   D CG  
11034 C  CD1 . LEU   D 301 ? 1.4508 1.0222 0.8897 0.2842  -0.1334 -0.0630 370  LEU   D CD1 
11035 C  CD2 . LEU   D 301 ? 1.4774 1.0770 0.9505 0.2582  -0.1178 -0.0551 370  LEU   D CD2 
11036 N  N   . ILE   D 302 ? 1.5494 1.0643 0.9318 0.2729  -0.0814 -0.0328 371  ILE   D N   
11037 C  CA  . ILE   D 302 ? 1.5110 0.9977 0.8637 0.2801  -0.0719 -0.0274 371  ILE   D CA  
11038 C  C   . ILE   D 302 ? 1.6344 1.1058 0.9722 0.2847  -0.0708 -0.0276 371  ILE   D C   
11039 O  O   . ILE   D 302 ? 1.6352 1.1187 0.9886 0.2766  -0.0705 -0.0284 371  ILE   D O   
11040 C  CB  . ILE   D 302 ? 1.4577 0.9441 0.8143 0.2696  -0.0567 -0.0193 371  ILE   D CB  
11041 C  CG1 . ILE   D 302 ? 1.5755 1.0718 0.9408 0.2675  -0.0570 -0.0186 371  ILE   D CG1 
11042 C  CG2 . ILE   D 302 ? 1.5656 1.0236 0.8939 0.2754  -0.0455 -0.0133 371  ILE   D CG2 
11043 C  CD1 . ILE   D 302 ? 1.6478 1.1384 1.0012 0.2805  -0.0687 -0.0239 371  ILE   D CD1 
11044 N  N   . GLY   D 303 ? 1.6525 1.0966 0.9591 0.2980  -0.0702 -0.0268 372  GLY   D N   
11045 C  CA  . GLY   D 303 ? 1.6644 1.0911 0.9536 0.3036  -0.0688 -0.0267 372  GLY   D CA  
11046 C  C   . GLY   D 303 ? 1.6979 1.1342 0.9950 0.3086  -0.0830 -0.0347 372  GLY   D C   
11047 O  O   . GLY   D 303 ? 1.6991 1.1510 1.0098 0.3111  -0.0951 -0.0408 372  GLY   D O   
11048 N  N   . ARG   D 304 ? 1.6857 1.1124 0.9745 0.3100  -0.0812 -0.0345 373  ARG   D N   
11049 C  CA  . ARG   D 304 ? 1.6636 1.0995 0.9609 0.3136  -0.0928 -0.0414 373  ARG   D CA  
11050 C  C   . ARG   D 304 ? 1.6576 1.1037 0.9704 0.3017  -0.0866 -0.0394 373  ARG   D C   
11051 O  O   . ARG   D 304 ? 1.6861 1.1258 0.9963 0.2935  -0.0735 -0.0327 373  ARG   D O   
11052 C  CB  . ARG   D 304 ? 1.7322 1.1433 1.0000 0.3303  -0.0990 -0.0443 373  ARG   D CB  
11053 N  N   . PRO   D 305 ? 1.6944 1.1567 1.0242 0.3005  -0.0957 -0.0452 374  PRO   D N   
11054 C  CA  . PRO   D 305 ? 1.6781 1.1545 1.0270 0.2877  -0.0904 -0.0436 374  PRO   D CA  
11055 C  C   . PRO   D 305 ? 1.6268 1.0831 0.9583 0.2862  -0.0793 -0.0383 374  PRO   D C   
11056 O  O   . PRO   D 305 ? 1.6318 1.0628 0.9355 0.2967  -0.0771 -0.0366 374  PRO   D O   
11057 C  CB  . PRO   D 305 ? 1.6336 1.1247 0.9964 0.2913  -0.1031 -0.0513 374  PRO   D CB  
11058 C  CG  . PRO   D 305 ? 1.5990 1.0928 0.9604 0.3017  -0.1151 -0.0568 374  PRO   D CG  
11059 C  CD  . PRO   D 305 ? 1.6688 1.1364 1.0004 0.3113  -0.1111 -0.0533 374  PRO   D CD  
11060 N  N   . SER   D 306 ? 1.6073 1.0745 0.9550 0.2733  -0.0726 -0.0356 375  SER   D N   
11061 C  CA  . SER   D 306 ? 1.6372 1.0876 0.9719 0.2702  -0.0622 -0.0307 375  SER   D CA  
11062 C  C   . SER   D 306 ? 1.6438 1.1112 1.0001 0.2584  -0.0609 -0.0313 375  SER   D C   
11063 O  O   . SER   D 306 ? 1.6259 1.1181 1.0078 0.2506  -0.0654 -0.0340 375  SER   D O   
11064 C  CB  . SER   D 306 ? 1.6412 1.0783 0.9658 0.2653  -0.0487 -0.0228 375  SER   D CB  
11065 O  OG  . SER   D 306 ? 1.6675 1.0930 0.9863 0.2588  -0.0377 -0.0177 375  SER   D OG  
11066 N  N   . THR   D 307 ? 1.7090 1.1615 1.0536 0.2573  -0.0546 -0.0286 376  THR   D N   
11067 C  CA  . THR   D 307 ? 1.6349 1.0992 0.9961 0.2464  -0.0520 -0.0285 376  THR   D CA  
11068 C  C   . THR   D 307 ? 1.6502 1.1056 1.0096 0.2356  -0.0385 -0.0214 376  THR   D C   
11069 O  O   . THR   D 307 ? 1.6177 1.0843 0.9929 0.2250  -0.0360 -0.0209 376  THR   D O   
11070 C  CB  . THR   D 307 ? 1.5305 0.9884 0.8834 0.2539  -0.0584 -0.0329 376  THR   D CB  
11071 O  OG1 . THR   D 307 ? 1.6205 1.0497 0.9441 0.2631  -0.0540 -0.0303 376  THR   D OG1 
11072 C  CG2 . THR   D 307 ? 1.5312 1.0010 0.8906 0.2632  -0.0721 -0.0403 376  THR   D CG2 
11073 N  N   . GLU   D 308 ? 1.7687 1.2051 1.1106 0.2378  -0.0296 -0.0158 377  GLU   D N   
11074 C  CA  . GLU   D 308 ? 1.7908 1.2183 1.1317 0.2277  -0.0165 -0.0090 377  GLU   D CA  
11075 C  C   . GLU   D 308 ? 1.7455 1.1970 1.1154 0.2123  -0.0137 -0.0076 377  GLU   D C   
11076 O  O   . GLU   D 308 ? 1.7437 1.2078 1.1249 0.2095  -0.0143 -0.0071 377  GLU   D O   
11077 C  CB  . GLU   D 308 ? 1.7984 1.2037 1.1179 0.2327  -0.0074 -0.0033 377  GLU   D CB  
11078 N  N   . HIS   D 309 ? 1.7319 1.1893 1.1133 0.2026  -0.0111 -0.0071 378  HIS   D N   
11079 C  CA  . HIS   D 309 ? 1.7751 1.2530 1.1824 0.1878  -0.0082 -0.0057 378  HIS   D CA  
11080 C  C   . HIS   D 309 ? 1.7305 1.2354 1.1603 0.1854  -0.0181 -0.0110 378  HIS   D C   
11081 O  O   . HIS   D 309 ? 1.7285 1.2513 1.1796 0.1742  -0.0162 -0.0098 378  HIS   D O   
11082 C  CB  . HIS   D 309 ? 1.7658 1.2407 1.1757 0.1807  0.0024  0.0008  378  HIS   D CB  
11083 C  CG  . HIS   D 309 ? 1.8145 1.2956 1.2400 0.1660  0.0101  0.0046  378  HIS   D CG  
11084 N  ND1 . HIS   D 309 ? 1.7637 1.2689 1.2151 0.1554  0.0067  0.0026  378  HIS   D ND1 
11085 C  CD2 . HIS   D 309 ? 1.8343 1.3002 1.2534 0.1604  0.0208  0.0101  378  HIS   D CD2 
11086 C  CE1 . HIS   D 309 ? 1.7267 1.2312 1.1865 0.1441  0.0144  0.0065  378  HIS   D CE1 
11087 N  NE2 . HIS   D 309 ? 1.8040 1.2852 1.2453 0.1467  0.0230  0.0111  378  HIS   D NE2 
11088 N  N   . SER   D 310 ? 1.5693 1.0778 0.9958 0.1954  -0.0285 -0.0168 379  SER   D N   
11089 C  CA  . SER   D 310 ? 1.5858 1.1193 1.0338 0.1936  -0.0378 -0.0220 379  SER   D CA  
11090 C  C   . SER   D 310 ? 1.6040 1.1556 1.0745 0.1805  -0.0366 -0.0221 379  SER   D C   
11091 O  O   . SER   D 310 ? 1.6215 1.1694 1.0907 0.1785  -0.0361 -0.0229 379  SER   D O   
11092 C  CB  . SER   D 310 ? 1.5631 1.0964 1.0048 0.2056  -0.0488 -0.0284 379  SER   D CB  
11093 O  OG  . SER   D 310 ? 1.6012 1.1592 1.0653 0.2033  -0.0573 -0.0334 379  SER   D OG  
11094 N  N   . TRP   D 311 ? 1.5549 1.1253 1.0455 0.1719  -0.0362 -0.0213 380  TRP   D N   
11095 C  CA  . TRP   D 311 ? 1.5366 1.1242 1.0483 0.1599  -0.0356 -0.0216 380  TRP   D CA  
11096 C  C   . TRP   D 311 ? 1.4982 1.1002 1.0207 0.1621  -0.0447 -0.0277 380  TRP   D C   
11097 O  O   . TRP   D 311 ? 1.5257 1.1392 1.0626 0.1535  -0.0445 -0.0284 380  TRP   D O   
11098 C  CB  . TRP   D 311 ? 1.5024 1.1061 1.0320 0.1508  -0.0332 -0.0194 380  TRP   D CB  
11099 C  CG  . TRP   D 311 ? 1.4792 1.0709 1.0015 0.1469  -0.0232 -0.0131 380  TRP   D CG  
11100 C  CD1 . TRP   D 311 ? 1.5268 1.1007 1.0374 0.1441  -0.0146 -0.0087 380  TRP   D CD1 
11101 C  CD2 . TRP   D 311 ? 1.4776 1.0737 1.0041 0.1455  -0.0204 -0.0105 380  TRP   D CD2 
11102 N  NE1 . TRP   D 311 ? 1.5276 1.0954 1.0359 0.1408  -0.0063 -0.0033 380  TRP   D NE1 
11103 C  CE2 . TRP   D 311 ? 1.4861 1.0671 1.0036 0.1418  -0.0097 -0.0043 380  TRP   D CE2 
11104 C  CE3 . TRP   D 311 ? 1.4269 1.0382 0.9641 0.1470  -0.0260 -0.0127 380  TRP   D CE3 
11105 C  CZ2 . TRP   D 311 ? 1.4596 1.0406 0.9785 0.1399  -0.0041 -0.0002 380  TRP   D CZ2 
11106 C  CZ3 . TRP   D 311 ? 1.3833 0.9941 0.9211 0.1452  -0.0209 -0.0089 380  TRP   D CZ3 
11107 C  CH2 . TRP   D 311 ? 1.4299 1.0258 0.9586 0.1418  -0.0099 -0.0027 380  TRP   D CH2 
11108 N  N   . PHE   D 312 ? 1.4935 1.0947 1.0096 0.1735  -0.0528 -0.0322 381  PHE   D N   
11109 C  CA  . PHE   D 312 ? 1.5390 1.1545 1.0666 0.1764  -0.0616 -0.0382 381  PHE   D CA  
11110 C  C   . PHE   D 312 ? 1.6136 1.2130 1.1223 0.1884  -0.0656 -0.0410 381  PHE   D C   
11111 O  O   . PHE   D 312 ? 1.5511 1.1464 1.0513 0.1995  -0.0720 -0.0441 381  PHE   D O   
11112 C  CB  . PHE   D 312 ? 1.5306 1.1641 1.0728 0.1783  -0.0688 -0.0415 381  PHE   D CB  
11113 C  CG  . PHE   D 312 ? 1.5332 1.1803 1.0912 0.1678  -0.0648 -0.0385 381  PHE   D CG  
11114 C  CD1 . PHE   D 312 ? 1.5147 1.1522 1.0643 0.1664  -0.0584 -0.0337 381  PHE   D CD1 
11115 C  CD2 . PHE   D 312 ? 1.5310 1.2004 1.1122 0.1597  -0.0674 -0.0404 381  PHE   D CD2 
11116 C  CE1 . PHE   D 312 ? 1.4916 1.1417 1.0560 0.1571  -0.0549 -0.0310 381  PHE   D CE1 
11117 C  CE2 . PHE   D 312 ? 1.5040 1.1859 1.0997 0.1504  -0.0641 -0.0377 381  PHE   D CE2 
11118 C  CZ  . PHE   D 312 ? 1.5159 1.1885 1.1035 0.1490  -0.0580 -0.0331 381  PHE   D CZ  
11119 N  N   . PRO   D 313 ? 1.6751 1.2646 1.1765 0.1867  -0.0622 -0.0402 382  PRO   D N   
11120 C  CA  . PRO   D 313 ? 1.6502 1.2222 1.1317 0.1983  -0.0651 -0.0424 382  PRO   D CA  
11121 C  C   . PRO   D 313 ? 1.6686 1.2513 1.1562 0.2075  -0.0761 -0.0490 382  PRO   D C   
11122 O  O   . PRO   D 313 ? 1.6593 1.2623 1.1673 0.2033  -0.0804 -0.0523 382  PRO   D O   
11123 C  CB  . PRO   D 313 ? 1.6461 1.2117 1.1253 0.1925  -0.0603 -0.0409 382  PRO   D CB  
11124 C  CG  . PRO   D 313 ? 1.6954 1.2832 1.1995 0.1799  -0.0595 -0.0410 382  PRO   D CG  
11125 C  CD  . PRO   D 313 ? 1.6544 1.2501 1.1669 0.1749  -0.0571 -0.0382 382  PRO   D CD  
11126 N  N   . GLY   D 314 ? 1.6663 1.2348 1.1361 0.2204  -0.0806 -0.0510 383  GLY   D N   
11127 C  CA  . GLY   D 314 ? 1.6920 1.2692 1.1666 0.2304  -0.0916 -0.0573 383  GLY   D CA  
11128 C  C   . GLY   D 314 ? 1.6999 1.2806 1.1752 0.2353  -0.0962 -0.0584 383  GLY   D C   
11129 O  O   . GLY   D 314 ? 1.7028 1.2848 1.1763 0.2459  -0.1055 -0.0634 383  GLY   D O   
11130 N  N   . TYR   D 315 ? 1.6935 1.2754 1.1712 0.2281  -0.0900 -0.0538 384  TYR   D N   
11131 C  CA  . TYR   D 315 ? 1.6073 1.1937 1.0871 0.2313  -0.0937 -0.0545 384  TYR   D CA  
11132 C  C   . TYR   D 315 ? 1.5936 1.1576 1.0501 0.2352  -0.0872 -0.0496 384  TYR   D C   
11133 O  O   . TYR   D 315 ? 1.6275 1.1786 1.0741 0.2300  -0.0773 -0.0442 384  TYR   D O   
11134 C  CB  . TYR   D 315 ? 1.5736 1.1831 1.0786 0.2195  -0.0923 -0.0536 384  TYR   D CB  
11135 C  CG  . TYR   D 315 ? 1.5554 1.1877 1.0839 0.2164  -0.0990 -0.0585 384  TYR   D CG  
11136 C  CD1 . TYR   D 315 ? 1.5505 1.1895 1.0885 0.2090  -0.0958 -0.0582 384  TYR   D CD1 
11137 C  CD2 . TYR   D 315 ? 1.5297 1.1762 1.0707 0.2213  -0.1085 -0.0635 384  TYR   D CD2 
11138 C  CE1 . TYR   D 315 ? 1.5037 1.1628 1.0624 0.2067  -0.1013 -0.0625 384  TYR   D CE1 
11139 C  CE2 . TYR   D 315 ? 1.5490 1.2162 1.1121 0.2186  -0.1140 -0.0678 384  TYR   D CE2 
11140 C  CZ  . TYR   D 315 ? 1.5335 1.2068 1.1051 0.2114  -0.1101 -0.0672 384  TYR   D CZ  
11141 O  OH  . TYR   D 315 ? 1.5849 1.2780 1.1777 0.2090  -0.1148 -0.0712 384  TYR   D OH  
11142 N  N   . ALA   D 316 ? 1.5999 1.1592 1.0480 0.2445  -0.0927 -0.0515 385  ALA   D N   
11143 C  CA  . ALA   D 316 ? 1.5654 1.1062 0.9937 0.2482  -0.0869 -0.0470 385  ALA   D CA  
11144 C  C   . ALA   D 316 ? 1.6034 1.1581 1.0463 0.2407  -0.0847 -0.0448 385  ALA   D C   
11145 O  O   . ALA   D 316 ? 1.5688 1.1454 1.0335 0.2372  -0.0912 -0.0485 385  ALA   D O   
11146 C  CB  . ALA   D 316 ? 1.5716 1.0962 0.9787 0.2643  -0.0947 -0.0504 385  ALA   D CB  
11147 N  N   . TRP   D 317 ? 1.6020 1.1434 1.0327 0.2384  -0.0752 -0.0388 386  TRP   D N   
11148 C  CA  . TRP   D 317 ? 1.5640 1.1158 1.0057 0.2320  -0.0720 -0.0361 386  TRP   D CA  
11149 C  C   . TRP   D 317 ? 1.5825 1.1176 1.0036 0.2426  -0.0725 -0.0351 386  TRP   D C   
11150 O  O   . TRP   D 317 ? 1.5726 1.0836 0.9680 0.2513  -0.0694 -0.0332 386  TRP   D O   
11151 C  CB  . TRP   D 317 ? 1.4916 1.0447 0.9403 0.2187  -0.0595 -0.0295 386  TRP   D CB  
11152 C  CG  . TRP   D 317 ? 1.4926 1.0212 0.9191 0.2207  -0.0500 -0.0244 386  TRP   D CG  
11153 C  CD1 . TRP   D 317 ? 1.5740 1.0934 0.9942 0.2193  -0.0467 -0.0236 386  TRP   D CD1 
11154 C  CD2 . TRP   D 317 ? 1.5538 1.0625 0.9603 0.2251  -0.0422 -0.0193 386  TRP   D CD2 
11155 N  NE1 . TRP   D 317 ? 1.6340 1.1292 1.0321 0.2221  -0.0373 -0.0183 386  TRP   D NE1 
11156 C  CE2 . TRP   D 317 ? 1.6468 1.1349 1.0361 0.2258  -0.0341 -0.0155 386  TRP   D CE2 
11157 C  CE3 . TRP   D 317 ? 1.5789 1.0847 0.9801 0.2286  -0.0410 -0.0176 386  TRP   D CE3 
11158 C  CZ2 . TRP   D 317 ? 1.6193 1.0843 0.9867 0.2298  -0.0245 -0.0098 386  TRP   D CZ2 
11159 C  CZ3 . TRP   D 317 ? 1.6133 1.0959 0.9922 0.2328  -0.0314 -0.0119 386  TRP   D CZ3 
11160 C  CH2 . TRP   D 317 ? 1.5046 0.9673 0.8672 0.2332  -0.0231 -0.0080 386  TRP   D CH2 
11161 N  N   . THR   D 318 ? 1.5384 1.0860 0.9703 0.2418  -0.0763 -0.0363 387  THR   D N   
11162 C  CA  . THR   D 318 ? 1.5626 1.0968 0.9773 0.2508  -0.0768 -0.0353 387  THR   D CA  
11163 C  C   . THR   D 318 ? 1.5169 1.0647 0.9471 0.2411  -0.0717 -0.0319 387  THR   D C   
11164 O  O   . THR   D 318 ? 1.5541 1.1250 1.0081 0.2350  -0.0774 -0.0351 387  THR   D O   
11165 C  CB  . THR   D 318 ? 1.5748 1.1100 0.9856 0.2633  -0.0910 -0.0426 387  THR   D CB  
11166 O  OG1 . THR   D 318 ? 1.6065 1.1383 1.0132 0.2693  -0.0975 -0.0470 387  THR   D OG1 
11167 C  CG2 . THR   D 318 ? 1.5756 1.0888 0.9601 0.2753  -0.0910 -0.0414 387  THR   D CG2 
11168 N  N   . VAL   D 319 ? 1.5292 1.0631 0.9469 0.2395  -0.0606 -0.0254 388  VAL   D N   
11169 C  CA  . VAL   D 319 ? 1.4779 1.0252 0.9116 0.2293  -0.0546 -0.0217 388  VAL   D CA  
11170 C  C   . VAL   D 319 ? 1.4924 1.0535 0.9362 0.2326  -0.0644 -0.0261 388  VAL   D C   
11171 O  O   . VAL   D 319 ? 1.5342 1.0849 0.9627 0.2451  -0.0720 -0.0296 388  VAL   D O   
11172 C  CB  . VAL   D 319 ? 1.4765 1.0048 0.8930 0.2295  -0.0418 -0.0143 388  VAL   D CB  
11173 C  CG1 . VAL   D 319 ? 1.4390 0.9813 0.8710 0.2215  -0.0378 -0.0115 388  VAL   D CG1 
11174 C  CG2 . VAL   D 319 ? 1.4470 0.9654 0.8594 0.2228  -0.0308 -0.0092 388  VAL   D CG2 
11175 N  N   . ALA   D 320 ? 1.5196 1.1036 0.9887 0.2217  -0.0643 -0.0261 389  ALA   D N   
11176 C  CA  . ALA   D 320 ? 1.4613 1.0599 0.9423 0.2236  -0.0735 -0.0303 389  ALA   D CA  
11177 C  C   . ALA   D 320 ? 1.4011 1.0074 0.8914 0.2158  -0.0664 -0.0258 389  ALA   D C   
11178 O  O   . ALA   D 320 ? 1.3058 0.9222 0.8109 0.2036  -0.0585 -0.0218 389  ALA   D O   
11179 C  CB  . ALA   D 320 ? 1.3711 0.9929 0.8762 0.2192  -0.0832 -0.0362 389  ALA   D CB  
11180 N  N   . GLN   D 321 ? 1.4205 1.0220 0.9024 0.2230  -0.0698 -0.0266 390  GLN   D N   
11181 C  CA  . GLN   D 321 ? 1.3993 1.0056 0.8870 0.2175  -0.0632 -0.0223 390  GLN   D CA  
11182 C  C   . GLN   D 321 ? 1.3778 0.9975 0.8762 0.2201  -0.0734 -0.0270 390  GLN   D C   
11183 O  O   . GLN   D 321 ? 1.3947 1.0136 0.8890 0.2293  -0.0850 -0.0331 390  GLN   D O   
11184 C  CB  . GLN   D 321 ? 1.4260 1.0078 0.8880 0.2239  -0.0536 -0.0166 390  GLN   D CB  
11185 C  CG  . GLN   D 321 ? 1.4675 1.0285 0.9031 0.2401  -0.0604 -0.0198 390  GLN   D CG  
11186 C  CD  . GLN   D 321 ? 1.6122 1.1499 1.0226 0.2470  -0.0511 -0.0143 390  GLN   D CD  
11187 O  OE1 . GLN   D 321 ? 1.6100 1.1380 1.0058 0.2575  -0.0563 -0.0162 390  GLN   D OE1 
11188 N  NE2 . GLN   D 321 ? 1.5355 1.0634 0.9405 0.2413  -0.0372 -0.0073 390  GLN   D NE2 
11189 N  N   . CYS   D 322 ? 1.3778 1.0093 0.8897 0.2121  -0.0687 -0.0240 391  CYS   D N   
11190 C  CA  . CYS   D 322 ? 1.3978 1.0444 0.9232 0.2122  -0.0773 -0.0280 391  CYS   D CA  
11191 C  C   . CYS   D 322 ? 1.4110 1.0420 0.9156 0.2262  -0.0838 -0.0306 391  CYS   D C   
11192 O  O   . CYS   D 322 ? 1.4506 1.0621 0.9337 0.2322  -0.0768 -0.0264 391  CYS   D O   
11193 C  CB  . CYS   D 322 ? 1.3573 1.0165 0.8981 0.2014  -0.0695 -0.0234 391  CYS   D CB  
11194 S  SG  . CYS   D 322 ? 1.2952 0.9690 0.8485 0.2024  -0.0783 -0.0272 391  CYS   D SG  
11195 N  N   . LYS   D 323 ? 1.4362 1.0758 0.9477 0.2315  -0.0971 -0.0376 392  LYS   D N   
11196 C  CA  . LYS   D 323 ? 1.3986 1.0242 0.8915 0.2453  -0.1056 -0.0412 392  LYS   D CA  
11197 C  C   . LYS   D 323 ? 1.3787 1.0043 0.8701 0.2454  -0.1033 -0.0391 392  LYS   D C   
11198 O  O   . LYS   D 323 ? 1.4840 1.1022 0.9646 0.2555  -0.1117 -0.0428 392  LYS   D O   
11199 C  CB  . LYS   D 323 ? 1.4221 1.0586 0.9258 0.2501  -0.1210 -0.0497 392  LYS   D CB  
11200 C  CG  . LYS   D 323 ? 1.4123 1.0729 0.9425 0.2428  -0.1270 -0.0527 392  LYS   D CG  
11201 C  CD  . LYS   D 323 ? 1.4227 1.0922 0.9625 0.2489  -0.1427 -0.0613 392  LYS   D CD  
11202 C  CE  . LYS   D 323 ? 1.3098 1.0028 0.8762 0.2420  -0.1490 -0.0646 392  LYS   D CE  
11203 N  NZ  . LYS   D 323 ? 1.2551 0.9570 0.8327 0.2469  -0.1629 -0.0725 392  LYS   D NZ  
11204 N  N   . ILE   D 324 ? 1.3755 1.0088 0.8772 0.2348  -0.0923 -0.0331 393  ILE   D N   
11205 C  CA  . ILE   D 324 ? 1.3849 1.0195 0.8867 0.2344  -0.0898 -0.0309 393  ILE   D CA  
11206 C  C   . ILE   D 324 ? 1.4469 1.0661 0.9335 0.2333  -0.0748 -0.0227 393  ILE   D C   
11207 O  O   . ILE   D 324 ? 1.4501 1.0518 0.9157 0.2425  -0.0728 -0.0210 393  ILE   D O   
11208 C  CB  . ILE   D 324 ? 1.4013 1.0631 0.9337 0.2223  -0.0919 -0.0320 393  ILE   D CB  
11209 C  CG1 . ILE   D 324 ? 1.3986 1.0750 0.9461 0.2237  -0.1064 -0.0400 393  ILE   D CG1 
11210 C  CG2 . ILE   D 324 ? 1.3929 1.0558 0.9253 0.2217  -0.0888 -0.0294 393  ILE   D CG2 
11211 C  CD1 . ILE   D 324 ? 1.3489 1.0237 0.8923 0.2326  -0.1175 -0.0451 393  ILE   D CD1 
11212 N  N   . CYS   D 325 ? 1.4712 1.0962 0.9683 0.2224  -0.0644 -0.0178 394  CYS   D N   
11213 C  CA  . CYS   D 325 ? 1.4350 1.0479 0.9221 0.2194  -0.0493 -0.0098 394  CYS   D CA  
11214 C  C   . CYS   D 325 ? 1.3334 0.9297 0.8055 0.2214  -0.0427 -0.0071 394  CYS   D C   
11215 O  O   . CYS   D 325 ? 1.3399 0.9283 0.8077 0.2168  -0.0296 -0.0004 394  CYS   D O   
11216 C  CB  . CYS   D 325 ? 1.4089 1.0419 0.9215 0.2045  -0.0420 -0.0060 394  CYS   D CB  
11217 S  SG  . CYS   D 325 ? 1.4286 1.0824 0.9668 0.1918  -0.0441 -0.0080 394  CYS   D SG  
11218 N  N   . ALA   D 326 ? 1.3973 0.9890 0.8626 0.2278  -0.0515 -0.0122 395  ALA   D N   
11219 C  CA  . ALA   D 326 ? 1.4720 1.0475 0.9221 0.2308  -0.0470 -0.0105 395  ALA   D CA  
11220 C  C   . ALA   D 326 ? 1.4242 1.0057 0.8870 0.2179  -0.0353 -0.0050 395  ALA   D C   
11221 O  O   . ALA   D 326 ? 1.4484 1.0138 0.8969 0.2194  -0.0281 -0.0017 395  ALA   D O   
11222 C  CB  . ALA   D 326 ? 1.4844 1.0304 0.9013 0.2438  -0.0422 -0.0076 395  ALA   D CB  
11223 N  N   . SER   D 327 ? 1.4289 1.0329 0.9180 0.2053  -0.0337 -0.0041 396  SER   D N   
11224 C  CA  . SER   D 327 ? 1.4013 1.0136 0.9053 0.1926  -0.0248 0.0000  396  SER   D CA  
11225 C  C   . SER   D 327 ? 1.3743 0.9884 0.8812 0.1912  -0.0292 -0.0032 396  SER   D C   
11226 O  O   . SER   D 327 ? 1.3482 0.9683 0.8577 0.1960  -0.0409 -0.0096 396  SER   D O   
11227 C  CB  . SER   D 327 ? 1.3549 0.9918 0.8865 0.1806  -0.0247 0.0004  396  SER   D CB  
11228 O  OG  . SER   D 327 ? 1.3870 1.0207 0.9165 0.1793  -0.0164 0.0054  396  SER   D OG  
11229 N  N   . HIS   D 328 ? 1.3351 0.9440 0.8421 0.1846  -0.0199 0.0011  397  HIS   D N   
11230 C  CA  . HIS   D 328 ? 1.3097 0.9194 0.8188 0.1833  -0.0236 -0.0017 397  HIS   D CA  
11231 C  C   . HIS   D 328 ? 1.3145 0.9501 0.8510 0.1736  -0.0301 -0.0055 397  HIS   D C   
11232 O  O   . HIS   D 328 ? 1.3168 0.9667 0.8720 0.1623  -0.0253 -0.0028 397  HIS   D O   
11233 C  CB  . HIS   D 328 ? 1.3864 0.9835 0.8887 0.1786  -0.0121 0.0038  397  HIS   D CB  
11234 C  CG  . HIS   D 328 ? 1.3927 0.9896 0.8961 0.1773  -0.0155 0.0010  397  HIS   D CG  
11235 N  ND1 . HIS   D 328 ? 1.3840 0.9897 0.9025 0.1656  -0.0107 0.0030  397  HIS   D ND1 
11236 C  CD2 . HIS   D 328 ? 1.3984 0.9880 0.8902 0.1865  -0.0239 -0.0039 397  HIS   D CD2 
11237 C  CE1 . HIS   D 328 ? 1.3742 0.9773 0.8893 0.1678  -0.0155 -0.0004 397  HIS   D CE1 
11238 N  NE2 . HIS   D 328 ? 1.3378 0.9314 0.8372 0.1804  -0.0234 -0.0045 397  HIS   D NE2 
11239 N  N   . ILE   D 329 ? 1.3363 0.9778 0.8754 0.1782  -0.0411 -0.0119 398  ILE   D N   
11240 C  CA  . ILE   D 329 ? 1.2952 0.9598 0.8589 0.1698  -0.0472 -0.0156 398  ILE   D CA  
11241 C  C   . ILE   D 329 ? 1.3318 0.9956 0.8973 0.1666  -0.0468 -0.0165 398  ILE   D C   
11242 O  O   . ILE   D 329 ? 1.3639 1.0444 0.9493 0.1565  -0.0470 -0.0171 398  ILE   D O   
11243 C  CB  . ILE   D 329 ? 1.2375 0.9136 0.8082 0.1759  -0.0601 -0.0223 398  ILE   D CB  
11244 C  CG1 . ILE   D 329 ? 1.2376 0.9186 0.8116 0.1763  -0.0603 -0.0213 398  ILE   D CG1 
11245 C  CG2 . ILE   D 329 ? 1.2142 0.9118 0.8080 0.1687  -0.0661 -0.0263 398  ILE   D CG2 
11246 C  CD1 . ILE   D 329 ? 1.2651 0.9590 0.8562 0.1637  -0.0522 -0.0166 398  ILE   D CD1 
11247 N  N   . GLY   D 330 ? 1.3916 1.0356 0.9361 0.1748  -0.0459 -0.0165 399  GLY   D N   
11248 C  CA  . GLY   D 330 ? 1.3605 1.0029 0.9051 0.1736  -0.0473 -0.0183 399  GLY   D CA  
11249 C  C   . GLY   D 330 ? 1.3910 1.0154 0.9138 0.1865  -0.0522 -0.0213 399  GLY   D C   
11250 O  O   . GLY   D 330 ? 1.4118 1.0153 0.9120 0.1947  -0.0483 -0.0188 399  GLY   D O   
11251 N  N   . TRP   D 331 ? 1.3695 1.0016 0.8990 0.1882  -0.0602 -0.0266 400  TRP   D N   
11252 C  CA  . TRP   D 331 ? 1.4171 1.0332 0.9276 0.1997  -0.0650 -0.0296 400  TRP   D CA  
11253 C  C   . TRP   D 331 ? 1.3752 1.0056 0.8977 0.2038  -0.0775 -0.0369 400  TRP   D C   
11254 O  O   . TRP   D 331 ? 1.2815 0.9334 0.8272 0.1958  -0.0806 -0.0391 400  TRP   D O   
11255 C  CB  . TRP   D 331 ? 1.4203 1.0237 0.9216 0.1969  -0.0577 -0.0266 400  TRP   D CB  
11256 C  CG  . TRP   D 331 ? 1.3416 0.9335 0.8357 0.1908  -0.0449 -0.0192 400  TRP   D CG  
11257 C  CD1 . TRP   D 331 ? 1.4191 0.9872 0.8892 0.1974  -0.0380 -0.0151 400  TRP   D CD1 
11258 C  CD2 . TRP   D 331 ? 1.3074 0.9113 0.8190 0.1770  -0.0373 -0.0151 400  TRP   D CD2 
11259 N  NE1 . TRP   D 331 ? 1.3908 0.9558 0.8635 0.1883  -0.0263 -0.0087 400  TRP   D NE1 
11260 C  CE2 . TRP   D 331 ? 1.3336 0.9205 0.8319 0.1757  -0.0260 -0.0087 400  TRP   D CE2 
11261 C  CE3 . TRP   D 331 ? 1.3129 0.9400 0.8502 0.1659  -0.0390 -0.0163 400  TRP   D CE3 
11262 C  CZ2 . TRP   D 331 ? 1.3726 0.9656 0.8835 0.1635  -0.0167 -0.0036 400  TRP   D CZ2 
11263 C  CZ3 . TRP   D 331 ? 1.3549 0.9873 0.9034 0.1541  -0.0302 -0.0114 400  TRP   D CZ3 
11264 C  CH2 . TRP   D 331 ? 1.3294 0.9452 0.8653 0.1529  -0.0193 -0.0051 400  TRP   D CH2 
11265 N  N   . LYS   D 332 ? 1.4369 1.0548 0.9431 0.2167  -0.0847 -0.0408 401  LYS   D N   
11266 C  CA  . LYS   D 332 ? 1.4394 1.0684 0.9553 0.2217  -0.0963 -0.0478 401  LYS   D CA  
11267 C  C   . LYS   D 332 ? 1.4640 1.0830 0.9705 0.2247  -0.0958 -0.0487 401  LYS   D C   
11268 O  O   . LYS   D 332 ? 1.5112 1.1077 0.9939 0.2315  -0.0919 -0.0463 401  LYS   D O   
11269 C  CB  . LYS   D 332 ? 1.4613 1.0849 0.9677 0.2344  -0.1064 -0.0524 401  LYS   D CB  
11270 C  CG  . LYS   D 332 ? 1.4599 1.0999 0.9828 0.2377  -0.1187 -0.0598 401  LYS   D CG  
11271 C  CD  . LYS   D 332 ? 1.4379 1.0692 0.9486 0.2517  -0.1294 -0.0647 401  LYS   D CD  
11272 C  CE  . LYS   D 332 ? 1.4436 1.0913 0.9720 0.2550  -0.1416 -0.0722 401  LYS   D CE  
11273 N  NZ  . LYS   D 332 ? 1.4646 1.1025 0.9807 0.2697  -0.1533 -0.0779 401  LYS   D NZ  
11274 N  N   . PHE   D 333 ? 1.4885 1.1237 1.0132 0.2197  -0.0994 -0.0519 402  PHE   D N   
11275 C  CA  . PHE   D 333 ? 1.5043 1.1325 1.0231 0.2209  -0.0984 -0.0526 402  PHE   D CA  
11276 C  C   . PHE   D 333 ? 1.5442 1.1769 1.0656 0.2305  -0.1100 -0.0596 402  PHE   D C   
11277 O  O   . PHE   D 333 ? 1.5014 1.1548 1.0445 0.2279  -0.1166 -0.0638 402  PHE   D O   
11278 C  CB  . PHE   D 333 ? 1.4768 1.1183 1.0131 0.2074  -0.0922 -0.0502 402  PHE   D CB  
11279 C  CG  . PHE   D 333 ? 1.4974 1.1294 1.0270 0.1992  -0.0803 -0.0432 402  PHE   D CG  
11280 C  CD1 . PHE   D 333 ? 1.5119 1.1255 1.0249 0.1998  -0.0737 -0.0401 402  PHE   D CD1 
11281 C  CD2 . PHE   D 333 ? 1.4190 1.0602 0.9594 0.1909  -0.0757 -0.0398 402  PHE   D CD2 
11282 C  CE1 . PHE   D 333 ? 1.5050 1.1099 1.0132 0.1920  -0.0627 -0.0337 402  PHE   D CE1 
11283 C  CE2 . PHE   D 333 ? 1.3549 0.9879 0.8907 0.1834  -0.0648 -0.0334 402  PHE   D CE2 
11284 C  CZ  . PHE   D 333 ? 1.4687 1.0836 0.9887 0.1838  -0.0582 -0.0304 402  PHE   D CZ  
11285 N  N   . THR   D 334 ? 1.5423 1.1554 1.0419 0.2414  -0.1121 -0.0608 403  THR   D N   
11286 C  CA  . THR   D 334 ? 1.5646 1.1775 1.0621 0.2528  -0.1233 -0.0674 403  THR   D CA  
11287 C  C   . THR   D 334 ? 1.5961 1.2008 1.0863 0.2548  -0.1219 -0.0680 403  THR   D C   
11288 O  O   . THR   D 334 ? 1.6302 1.2169 1.1026 0.2541  -0.1136 -0.0635 403  THR   D O   
11289 C  CB  . THR   D 334 ? 1.6082 1.2029 1.0835 0.2663  -0.1284 -0.0688 403  THR   D CB  
11290 O  OG1 . THR   D 334 ? 1.6776 1.2467 1.1256 0.2734  -0.1240 -0.0663 403  THR   D OG1 
11291 C  CG2 . THR   D 334 ? 1.4574 1.0511 0.9308 0.2628  -0.1240 -0.0649 403  THR   D CG2 
11292 N  N   . ALA   D 335 ? 1.6225 1.2401 1.1263 0.2577  -0.1300 -0.0737 404  ALA   D N   
11293 C  CA  . ALA   D 335 ? 1.6324 1.2451 1.1323 0.2591  -0.1290 -0.0747 404  ALA   D CA  
11294 C  C   . ALA   D 335 ? 1.7254 1.3126 1.1969 0.2719  -0.1306 -0.0751 404  ALA   D C   
11295 O  O   . ALA   D 335 ? 1.7732 1.3538 1.2354 0.2836  -0.1391 -0.0789 404  ALA   D O   
11296 C  CB  . ALA   D 335 ? 1.6320 1.2651 1.1540 0.2599  -0.1375 -0.0808 404  ALA   D CB  
11297 N  N   . THR   D 336 ? 1.7516 1.3241 1.2092 0.2699  -0.1229 -0.0715 405  THR   D N   
11298 C  CA  . THR   D 336 ? 1.7115 1.2602 1.1430 0.2818  -0.1242 -0.0722 405  THR   D CA  
11299 C  C   . THR   D 336 ? 1.7985 1.3521 1.2349 0.2882  -0.1317 -0.0778 405  THR   D C   
11300 O  O   . THR   D 336 ? 1.9398 1.4742 1.3552 0.2981  -0.1332 -0.0786 405  THR   D O   
11301 C  CB  . THR   D 336 ? 1.7436 1.2724 1.1564 0.2774  -0.1122 -0.0656 405  THR   D CB  
11302 O  OG1 . THR   D 336 ? 1.7218 1.2543 1.1412 0.2713  -0.1087 -0.0653 405  THR   D OG1 
11303 C  CG2 . THR   D 336 ? 1.7469 1.2782 1.1642 0.2665  -0.1031 -0.0597 405  THR   D CG2 
11304 N  N   . LYS   D 337 ? 1.8980 1.4757 1.3609 0.2828  -0.1359 -0.0813 406  LYS   D N   
11305 C  CA  . LYS   D 337 ? 1.8722 1.4565 1.3422 0.2894  -0.1436 -0.0871 406  LYS   D CA  
11306 C  C   . LYS   D 337 ? 1.8918 1.4964 1.3829 0.2927  -0.1543 -0.0929 406  LYS   D C   
11307 O  O   . LYS   D 337 ? 1.9186 1.5276 1.4134 0.2920  -0.1564 -0.0927 406  LYS   D O   
11308 C  CB  . LYS   D 337 ? 1.8138 1.4072 1.2958 0.2803  -0.1380 -0.0859 406  LYS   D CB  
11309 N  N   . LYS   D 338 ? 1.8763 1.4938 1.3822 0.2958  -0.1607 -0.0980 407  LYS   D N   
11310 C  CA  . LYS   D 338 ? 1.7945 1.4337 1.3244 0.2973  -0.1701 -0.1035 407  LYS   D CA  
11311 C  C   . LYS   D 338 ? 1.7868 1.4502 1.3449 0.2869  -0.1679 -0.1042 407  LYS   D C   
11312 O  O   . LYS   D 338 ? 1.7583 1.4414 1.3386 0.2838  -0.1725 -0.1069 407  LYS   D O   
11313 C  CB  . LYS   D 338 ? 1.6856 1.3206 1.2111 0.3121  -0.1818 -0.1101 407  LYS   D CB  
11314 N  N   . ASP   D 339 ? 1.8123 1.4743 1.3697 0.2819  -0.1612 -0.1021 408  ASP   D N   
11315 C  CA  . ASP   D 339 ? 1.7535 1.4375 1.3364 0.2723  -0.1588 -0.1026 408  ASP   D CA  
11316 C  C   . ASP   D 339 ? 1.7818 1.4758 1.3754 0.2589  -0.1518 -0.0981 408  ASP   D C   
11317 O  O   . ASP   D 339 ? 1.7559 1.4713 1.3738 0.2519  -0.1523 -0.0993 408  ASP   D O   
11318 C  CB  . ASP   D 339 ? 1.6964 1.3748 1.2740 0.2713  -0.1539 -0.1018 408  ASP   D CB  
11319 N  N   . MET   D 340 ? 1.8608 1.5398 1.4372 0.2556  -0.1455 -0.0929 409  MET   D N   
11320 C  CA  . MET   D 340 ? 1.8178 1.5038 1.4022 0.2421  -0.1371 -0.0878 409  MET   D CA  
11321 C  C   . MET   D 340 ? 1.7910 1.4986 1.3987 0.2370  -0.1406 -0.0894 409  MET   D C   
11322 O  O   . MET   D 340 ? 1.8032 1.5122 1.4116 0.2434  -0.1476 -0.0922 409  MET   D O   
11323 C  CB  . MET   D 340 ? 1.7727 1.4391 1.3354 0.2408  -0.1304 -0.0824 409  MET   D CB  
11324 C  CG  . MET   D 340 ? 1.8388 1.4801 1.3741 0.2508  -0.1303 -0.0818 409  MET   D CG  
11325 S  SD  . MET   D 340 ? 1.9237 1.5481 1.4424 0.2421  -0.1176 -0.0737 409  MET   D SD  
11326 C  CE  . MET   D 340 ? 1.8348 1.4643 1.3618 0.2318  -0.1107 -0.0718 409  MET   D CE  
11327 N  N   . SER   D 341 ? 1.6575 1.3811 1.2834 0.2254  -0.1357 -0.0876 410  SER   D N   
11328 C  CA  . SER   D 341 ? 1.5649 1.3084 1.2126 0.2188  -0.1373 -0.0882 410  SER   D CA  
11329 C  C   . SER   D 341 ? 1.4887 1.2329 1.1370 0.2067  -0.1285 -0.0823 410  SER   D C   
11330 O  O   . SER   D 341 ? 1.4521 1.1928 1.0976 0.1998  -0.1213 -0.0791 410  SER   D O   
11331 C  CB  . SER   D 341 ? 1.5011 1.2654 1.1729 0.2165  -0.1403 -0.0920 410  SER   D CB  
11332 O  OG  . SER   D 341 ? 1.5685 1.3515 1.2612 0.2130  -0.1441 -0.0938 410  SER   D OG  
11333 N  N   . PRO   D 342 ? 1.5401 1.2880 1.1917 0.2041  -0.1288 -0.0808 411  PRO   D N   
11334 C  CA  . PRO   D 342 ? 1.5370 1.2872 1.1901 0.2119  -0.1370 -0.0843 411  PRO   D CA  
11335 C  C   . PRO   D 342 ? 1.5512 1.2786 1.1784 0.2228  -0.1390 -0.0842 411  PRO   D C   
11336 O  O   . PRO   D 342 ? 1.4887 1.1985 1.0968 0.2224  -0.1323 -0.0802 411  PRO   D O   
11337 C  CB  . PRO   D 342 ? 1.4474 1.2073 1.1106 0.2031  -0.1339 -0.0813 411  PRO   D CB  
11338 C  CG  . PRO   D 342 ? 1.4366 1.1879 1.0910 0.1941  -0.1233 -0.0751 411  PRO   D CG  
11339 C  CD  . PRO   D 342 ? 1.4978 1.2483 1.1525 0.1924  -0.1207 -0.0755 411  PRO   D CD  
11340 N  N   . GLN   D 343 ? 1.5674 1.2943 1.1934 0.2329  -0.1485 -0.0887 412  GLN   D N   
11341 C  CA  . GLN   D 343 ? 1.6420 1.3467 1.2424 0.2445  -0.1513 -0.0891 412  GLN   D CA  
11342 C  C   . GLN   D 343 ? 1.6639 1.3565 1.2497 0.2427  -0.1461 -0.0842 412  GLN   D C   
11343 O  O   . GLN   D 343 ? 1.6161 1.2866 1.1770 0.2492  -0.1436 -0.0820 412  GLN   D O   
11344 C  CB  . GLN   D 343 ? 1.6358 1.3439 1.2400 0.2561  -0.1639 -0.0959 412  GLN   D CB  
11345 C  CG  . GLN   D 343 ? 1.6682 1.3817 1.2800 0.2615  -0.1693 -0.1007 412  GLN   D CG  
11346 C  CD  . GLN   D 343 ? 1.6832 1.3753 1.2709 0.2685  -0.1668 -0.0996 412  GLN   D CD  
11347 O  OE1 . GLN   D 343 ? 1.7366 1.4310 1.3280 0.2685  -0.1659 -0.1008 412  GLN   D OE1 
11348 N  NE2 . GLN   D 343 ? 1.7121 1.3825 1.2743 0.2746  -0.1654 -0.0971 412  GLN   D NE2 
11349 N  N   . LYS   D 344 ? 1.7207 1.4269 1.3213 0.2343  -0.1442 -0.0825 413  LYS   D N   
11350 C  CA  . LYS   D 344 ? 1.6734 1.3704 1.2628 0.2321  -0.1391 -0.0780 413  LYS   D CA  
11351 C  C   . LYS   D 344 ? 1.6079 1.3214 1.2162 0.2183  -0.1328 -0.0745 413  LYS   D C   
11352 O  O   . LYS   D 344 ? 1.5766 1.3107 1.2080 0.2129  -0.1359 -0.0771 413  LYS   D O   
11353 C  CB  . LYS   D 344 ? 1.7348 1.4281 1.3186 0.2419  -0.1479 -0.0814 413  LYS   D CB  
11354 N  N   . PHE   D 345 ? 1.5570 1.2613 1.1553 0.2126  -0.1237 -0.0685 414  PHE   D N   
11355 C  CA  . PHE   D 345 ? 1.4707 1.1892 1.0852 0.2002  -0.1179 -0.0650 414  PHE   D CA  
11356 C  C   . PHE   D 345 ? 1.4247 1.1290 1.0239 0.1984  -0.1100 -0.0592 414  PHE   D C   
11357 O  O   . PHE   D 345 ? 1.5003 1.1835 1.0767 0.2049  -0.1069 -0.0571 414  PHE   D O   
11358 C  CB  . PHE   D 345 ? 1.4327 1.1613 1.0603 0.1896  -0.1124 -0.0633 414  PHE   D CB  
11359 C  CG  . PHE   D 345 ? 1.4526 1.1642 1.0636 0.1880  -0.1044 -0.0592 414  PHE   D CG  
11360 C  CD1 . PHE   D 345 ? 1.4367 1.1370 1.0357 0.1954  -0.1066 -0.0614 414  PHE   D CD1 
11361 C  CD2 . PHE   D 345 ? 1.4421 1.1486 1.0497 0.1793  -0.0947 -0.0532 414  PHE   D CD2 
11362 C  CE1 . PHE   D 345 ? 1.4857 1.1698 1.0693 0.1939  -0.0992 -0.0577 414  PHE   D CE1 
11363 C  CE2 . PHE   D 345 ? 1.4336 1.1240 1.0266 0.1776  -0.0873 -0.0495 414  PHE   D CE2 
11364 C  CZ  . PHE   D 345 ? 1.4464 1.1255 1.0272 0.1848  -0.0895 -0.0517 414  PHE   D CZ  
11365 N  N   . TRP   D 346 ? 1.3643 1.0800 0.9763 0.1894  -0.1062 -0.0564 415  TRP   D N   
11366 C  CA  . TRP   D 346 ? 1.3636 1.0688 0.9647 0.1867  -0.0983 -0.0508 415  TRP   D CA  
11367 C  C   . TRP   D 346 ? 1.3427 1.0520 0.9514 0.1739  -0.0882 -0.0455 415  TRP   D C   
11368 O  O   . TRP   D 346 ? 1.3475 1.0751 0.9768 0.1648  -0.0883 -0.0461 415  TRP   D O   
11369 C  CB  . TRP   D 346 ? 1.3844 1.0987 0.9934 0.1870  -0.1019 -0.0515 415  TRP   D CB  
11370 C  CG  . TRP   D 346 ? 1.3811 1.0927 0.9846 0.1987  -0.1123 -0.0569 415  TRP   D CG  
11371 C  CD1 . TRP   D 346 ? 1.3612 1.0877 0.9802 0.2014  -0.1223 -0.0629 415  TRP   D CD1 
11372 C  CD2 . TRP   D 346 ? 1.3931 1.0855 0.9740 0.2098  -0.1141 -0.0567 415  TRP   D CD2 
11373 N  NE1 . TRP   D 346 ? 1.3599 1.0780 0.9681 0.2133  -0.1309 -0.0668 415  TRP   D NE1 
11374 C  CE2 . TRP   D 346 ? 1.3950 1.0919 0.9790 0.2188  -0.1261 -0.0632 415  TRP   D CE2 
11375 C  CE3 . TRP   D 346 ? 1.4065 1.0780 0.9647 0.2130  -0.1066 -0.0517 415  TRP   D CE3 
11376 C  CZ2 . TRP   D 346 ? 1.4688 1.1495 1.0332 0.2311  -0.1314 -0.0650 415  TRP   D CZ2 
11377 C  CZ3 . TRP   D 346 ? 1.4202 1.0755 0.9585 0.2254  -0.1111 -0.0532 415  TRP   D CZ3 
11378 C  CH2 . TRP   D 346 ? 1.4686 1.1283 1.0096 0.2344  -0.1237 -0.0599 415  TRP   D CH2 
11379 N  N   . GLY   D 347 ? 1.3352 1.0268 0.9272 0.1733  -0.0796 -0.0404 416  GLY   D N   
11380 C  CA  . GLY   D 347 ? 1.2715 0.9658 0.8703 0.1614  -0.0699 -0.0350 416  GLY   D CA  
11381 C  C   . GLY   D 347 ? 1.2995 0.9935 0.8982 0.1588  -0.0652 -0.0311 416  GLY   D C   
11382 O  O   . GLY   D 347 ? 1.3578 1.0348 0.9379 0.1658  -0.0624 -0.0288 416  GLY   D O   
11383 N  N   . LEU   D 348 ? 1.3081 1.0202 0.9268 0.1491  -0.0642 -0.0301 417  LEU   D N   
11384 C  CA  . LEU   D 348 ? 1.2413 0.9553 0.8621 0.1464  -0.0601 -0.0267 417  LEU   D CA  
11385 C  C   . LEU   D 348 ? 1.2302 0.9461 0.8582 0.1346  -0.0502 -0.0211 417  LEU   D C   
11386 O  O   . LEU   D 348 ? 1.2907 1.0208 0.9357 0.1254  -0.0501 -0.0216 417  LEU   D O   
11387 C  CB  . LEU   D 348 ? 1.2613 0.9947 0.8996 0.1453  -0.0675 -0.0303 417  LEU   D CB  
11388 C  CG  . LEU   D 348 ? 1.2615 1.0010 0.9031 0.1529  -0.0786 -0.0371 417  LEU   D CG  
11389 C  CD1 . LEU   D 348 ? 1.1557 0.9163 0.8180 0.1502  -0.0856 -0.0407 417  LEU   D CD1 
11390 C  CD2 . LEU   D 348 ? 1.2889 1.0096 0.9080 0.1666  -0.0826 -0.0389 417  LEU   D CD2 
11391 N  N   . THR   D 349 ? 1.2160 0.9174 0.8313 0.1350  -0.0418 -0.0159 418  THR   D N   
11392 C  CA  . THR   D 349 ? 1.2650 0.9668 0.8870 0.1242  -0.0321 -0.0106 418  THR   D CA  
11393 C  C   . THR   D 349 ? 1.2511 0.9710 0.8925 0.1158  -0.0313 -0.0093 418  THR   D C   
11394 O  O   . THR   D 349 ? 1.3154 1.0390 0.9572 0.1197  -0.0340 -0.0100 418  THR   D O   
11395 C  CB  . THR   D 349 ? 1.3108 0.9904 0.9131 0.1274  -0.0227 -0.0052 418  THR   D CB  
11396 O  OG1 . THR   D 349 ? 1.2657 0.9473 0.8772 0.1165  -0.0132 0.0002  418  THR   D OG1 
11397 C  CG2 . THR   D 349 ? 1.3020 0.9716 0.8900 0.1372  -0.0229 -0.0045 418  THR   D CG2 
11398 N  N   . ARG   D 350 ? 1.1774 0.9083 0.8348 0.1044  -0.0281 -0.0077 419  ARG   D N   
11399 C  CA  . ARG   D 350 ? 1.1447 0.8934 0.8217 0.0954  -0.0273 -0.0066 419  ARG   D CA  
11400 C  C   . ARG   D 350 ? 1.2812 1.0262 0.9549 0.0963  -0.0221 -0.0026 419  ARG   D C   
11401 O  O   . ARG   D 350 ? 1.3016 1.0577 0.9834 0.0970  -0.0259 -0.0040 419  ARG   D O   
11402 C  CB  . ARG   D 350 ? 1.1758 0.9297 0.8646 0.0838  -0.0222 -0.0040 419  ARG   D CB  
11403 C  CG  . ARG   D 350 ? 1.1561 0.9304 0.8654 0.0761  -0.0269 -0.0066 419  ARG   D CG  
11404 C  CD  . ARG   D 350 ? 1.1585 0.9363 0.8782 0.0649  -0.0208 -0.0031 419  ARG   D CD  
11405 N  NE  . ARG   D 350 ? 1.1830 0.9651 0.9099 0.0605  -0.0157 0.0008  419  ARG   D NE  
11406 C  CZ  . ARG   D 350 ? 1.1871 0.9596 0.9105 0.0569  -0.0070 0.0059  419  ARG   D CZ  
11407 N  NH1 . ARG   D 350 ? 1.2495 1.0059 0.9608 0.0579  -0.0022 0.0079  419  ARG   D NH1 
11408 N  NH2 . ARG   D 350 ? 1.1890 0.9683 0.9220 0.0521  -0.0029 0.0092  419  ARG   D NH2 
11409 N  N   . SER   D 351 ? 1.2196 0.9493 0.8825 0.0957  -0.0128 0.0025  420  SER   D N   
11410 C  CA  . SER   D 351 ? 1.2953 1.0214 0.9562 0.0955  -0.0060 0.0071  420  SER   D CA  
11411 C  C   . SER   D 351 ? 1.2708 0.9945 0.9224 0.1056  -0.0108 0.0051  420  SER   D C   
11412 O  O   . SER   D 351 ? 1.2126 0.9388 0.8668 0.1049  -0.0074 0.0077  420  SER   D O   
11413 C  CB  . SER   D 351 ? 1.3428 1.0493 0.9897 0.0957  0.0047  0.0126  420  SER   D CB  
11414 O  OG  . SER   D 351 ? 1.3579 1.0479 0.9867 0.1029  0.0038  0.0113  420  SER   D OG  
11415 N  N   . ALA   D 352 ? 1.1976 0.9169 0.8390 0.1149  -0.0190 0.0002  421  ALA   D N   
11416 C  CA  . ALA   D 352 ? 1.2672 0.9820 0.8980 0.1254  -0.0244 -0.0022 421  ALA   D CA  
11417 C  C   . ALA   D 352 ? 1.3261 1.0605 0.9731 0.1244  -0.0340 -0.0070 421  ALA   D C   
11418 O  O   . ALA   D 352 ? 1.3354 1.0679 0.9759 0.1325  -0.0393 -0.0093 421  ALA   D O   
11419 C  CB  . ALA   D 352 ? 1.3116 1.0090 0.9212 0.1370  -0.0284 -0.0048 421  ALA   D CB  
11420 N  N   . LEU   D 353 ? 1.2760 1.0285 0.9435 0.1150  -0.0363 -0.0085 422  LEU   D N   
11421 C  CA  . LEU   D 353 ? 1.2140 0.9846 0.8968 0.1143  -0.0456 -0.0136 422  LEU   D CA  
11422 C  C   . LEU   D 353 ? 1.2623 1.0494 0.9638 0.1050  -0.0435 -0.0116 422  LEU   D C   
11423 O  O   . LEU   D 353 ? 1.2965 1.0836 1.0023 0.0975  -0.0352 -0.0068 422  LEU   D O   
11424 C  CB  . LEU   D 353 ? 1.2512 1.0297 0.9422 0.1122  -0.0511 -0.0176 422  LEU   D CB  
11425 C  CG  . LEU   D 353 ? 1.2453 1.0129 0.9225 0.1220  -0.0566 -0.0216 422  LEU   D CG  
11426 C  CD1 . LEU   D 353 ? 1.1712 0.9452 0.8568 0.1173  -0.0583 -0.0237 422  LEU   D CD1 
11427 C  CD2 . LEU   D 353 ? 1.2796 1.0517 0.9571 0.1303  -0.0666 -0.0268 422  LEU   D CD2 
11428 N  N   . LEU   D 354 ? 1.2769 1.0784 0.9901 0.1055  -0.0513 -0.0156 423  LEU   D N   
11429 C  CA  . LEU   D 354 ? 1.2558 1.0736 0.9864 0.0982  -0.0510 -0.0147 423  LEU   D CA  
11430 C  C   . LEU   D 354 ? 1.2573 1.0930 1.0048 0.0959  -0.0597 -0.0198 423  LEU   D C   
11431 O  O   . LEU   D 354 ? 1.2243 1.0617 0.9703 0.1030  -0.0675 -0.0241 423  LEU   D O   
11432 C  CB  . LEU   D 354 ? 1.2780 1.0906 1.0012 0.1034  -0.0501 -0.0131 423  LEU   D CB  
11433 C  CG  . LEU   D 354 ? 1.1855 1.0149 0.9258 0.0975  -0.0515 -0.0130 423  LEU   D CG  
11434 C  CD1 . LEU   D 354 ? 1.1590 1.0009 0.9164 0.0851  -0.0465 -0.0103 423  LEU   D CD1 
11435 C  CD2 . LEU   D 354 ? 1.2185 1.0403 0.9497 0.1018  -0.0479 -0.0101 423  LEU   D CD2 
11436 N  N   . PRO   D 355 ? 1.2166 1.0654 0.9801 0.0862  -0.0585 -0.0195 424  PRO   D N   
11437 C  CA  . PRO   D 355 ? 1.2036 1.0699 0.9839 0.0832  -0.0655 -0.0238 424  PRO   D CA  
11438 C  C   . PRO   D 355 ? 1.1952 1.0711 0.9836 0.0837  -0.0689 -0.0247 424  PRO   D C   
11439 O  O   . PRO   D 355 ? 1.1958 1.0723 0.9857 0.0802  -0.0640 -0.0209 424  PRO   D O   
11440 C  CB  . PRO   D 355 ? 1.2018 1.0777 0.9953 0.0722  -0.0613 -0.0217 424  PRO   D CB  
11441 C  CG  . PRO   D 355 ? 1.2300 1.0921 1.0125 0.0703  -0.0533 -0.0173 424  PRO   D CG  
11442 C  CD  . PRO   D 355 ? 1.2065 1.0552 0.9742 0.0771  -0.0503 -0.0149 424  PRO   D CD  
11443 N  N   . THR   D 356 ? 1.1753 1.0591 0.9700 0.0879  -0.0773 -0.0297 425  THR   D N   
11444 C  CA  . THR   D 356 ? 1.2612 1.1538 1.0637 0.0887  -0.0814 -0.0310 425  THR   D CA  
11445 C  C   . THR   D 356 ? 1.2606 1.1694 1.0802 0.0866  -0.0885 -0.0356 425  THR   D C   
11446 O  O   . THR   D 356 ? 1.1490 1.0600 0.9713 0.0877  -0.0917 -0.0387 425  THR   D O   
11447 C  CB  . THR   D 356 ? 1.1581 1.0383 0.9452 0.0994  -0.0849 -0.0323 425  THR   D CB  
11448 O  OG1 . THR   D 356 ? 1.1728 1.0529 0.9588 0.1068  -0.0937 -0.0379 425  THR   D OG1 
11449 C  CG2 . THR   D 356 ? 1.2632 1.1243 1.0303 0.1037  -0.0782 -0.0284 425  THR   D CG2 
11450 N  N   . ILE   D 357 ? 1.2202 1.1401 1.0511 0.0839  -0.0907 -0.0361 426  ILE   D N   
11451 C  CA  . ILE   D 357 ? 1.1355 1.0715 0.9841 0.0810  -0.0965 -0.0398 426  ILE   D CA  
11452 C  C   . ILE   D 357 ? 1.1037 1.0403 0.9522 0.0887  -0.1047 -0.0441 426  ILE   D C   
11453 O  O   . ILE   D 357 ? 1.1671 1.1044 1.0156 0.0892  -0.1050 -0.0430 426  ILE   D O   
11454 C  CB  . ILE   D 357 ? 1.1518 1.1010 1.0151 0.0711  -0.0929 -0.0372 426  ILE   D CB  
11455 C  CG1 . ILE   D 357 ? 1.1716 1.1236 1.0393 0.0631  -0.0872 -0.0346 426  ILE   D CG1 
11456 C  CG2 . ILE   D 357 ? 1.1845 1.1485 1.0640 0.0697  -0.0990 -0.0408 426  ILE   D CG2 
11457 C  CD1 . ILE   D 357 ? 1.1810 1.1438 1.0609 0.0538  -0.0833 -0.0316 426  ILE   D CD1 
11458 N  N   . PRO   D 358 ? 1.0985 1.0352 0.9478 0.0946  -0.1116 -0.0490 427  PRO   D N   
11459 C  CA  . PRO   D 358 ? 1.1144 1.0521 0.9652 0.1022  -0.1206 -0.0538 427  PRO   D CA  
11460 C  C   . PRO   D 358 ? 1.2290 1.1795 1.0944 0.0985  -0.1236 -0.0547 427  PRO   D C   
11461 O  O   . PRO   D 358 ? 1.2731 1.2229 1.1384 0.1046  -0.1307 -0.0582 427  PRO   D O   
11462 C  CB  . PRO   D 358 ? 1.1203 1.0628 0.9783 0.1046  -0.1260 -0.0584 427  PRO   D CB  
11463 C  CG  . PRO   D 358 ? 1.0887 1.0236 0.9378 0.1031  -0.1201 -0.0559 427  PRO   D CG  
11464 C  CD  . PRO   D 358 ? 1.1215 1.0574 0.9708 0.0944  -0.1112 -0.0502 427  PRO   D CD  
11465 N  N   . VAL   D 369 ? 1.6904 1.6960 1.6145 0.0484  -0.0967 -0.0354 438  VAL   D N   
11466 C  CA  . VAL   D 369 ? 1.6685 1.6746 1.5938 0.0438  -0.0930 -0.0343 438  VAL   D CA  
11467 C  C   . VAL   D 369 ? 1.6475 1.6445 1.5628 0.0415  -0.0857 -0.0296 438  VAL   D C   
11468 O  O   . VAL   D 369 ? 1.6826 1.6686 1.5855 0.0464  -0.0839 -0.0279 438  VAL   D O   
11469 C  CB  . VAL   D 369 ? 1.6577 1.6597 1.5791 0.0492  -0.0969 -0.0380 438  VAL   D CB  
11470 C  CG1 . VAL   D 369 ? 1.5887 1.5878 1.5075 0.0454  -0.0924 -0.0364 438  VAL   D CG1 
11471 C  CG2 . VAL   D 369 ? 1.6926 1.7059 1.6278 0.0493  -0.1029 -0.0423 438  VAL   D CG2 
11472 N  N   . ILE   D 370 ? 1.4430 1.4443 1.3640 0.0341  -0.0816 -0.0275 439  ILE   D N   
11473 C  CA  . ILE   D 370 ? 1.3787 1.3738 1.2941 0.0302  -0.0747 -0.0229 439  ILE   D CA  
11474 C  C   . ILE   D 370 ? 1.3192 1.3157 1.2377 0.0248  -0.0724 -0.0225 439  ILE   D C   
11475 O  O   . ILE   D 370 ? 1.3019 1.3074 1.2298 0.0220  -0.0753 -0.0249 439  ILE   D O   
11476 C  CB  . ILE   D 370 ? 1.2686 1.2701 1.1910 0.0253  -0.0719 -0.0198 439  ILE   D CB  
11477 C  CG1 . ILE   D 370 ? 1.3455 1.3415 1.2643 0.0210  -0.0647 -0.0151 439  ILE   D CG1 
11478 C  CG2 . ILE   D 370 ? 1.3167 1.3328 1.2546 0.0191  -0.0742 -0.0210 439  ILE   D CG2 
11479 C  CD1 . ILE   D 370 ? 1.3514 1.3557 1.2796 0.0155  -0.0624 -0.0124 439  ILE   D CD1 
11480 N  N   . LEU   D 371 ? 1.2414 1.2285 1.1517 0.0234  -0.0672 -0.0195 440  LEU   D N   
11481 C  CA  . LEU   D 371 ? 1.2267 1.2137 1.1386 0.0186  -0.0654 -0.0193 440  LEU   D CA  
11482 C  C   . LEU   D 371 ? 1.2240 1.2216 1.1484 0.0097  -0.0636 -0.0176 440  LEU   D C   
11483 O  O   . LEU   D 371 ? 1.2286 1.2271 1.1555 0.0060  -0.0600 -0.0143 440  LEU   D O   
11484 C  CB  . LEU   D 371 ? 1.1775 1.1506 1.0769 0.0198  -0.0606 -0.0169 440  LEU   D CB  
11485 C  CG  . LEU   D 371 ? 1.1341 1.0969 1.0214 0.0280  -0.0630 -0.0194 440  LEU   D CG  
11486 C  CD1 . LEU   D 371 ? 1.0883 1.0365 0.9627 0.0290  -0.0577 -0.0166 440  LEU   D CD1 
11487 C  CD2 . LEU   D 371 ? 1.1016 1.0705 0.9942 0.0285  -0.0678 -0.0235 440  LEU   D CD2 
11488 N  N   . CYS   D 372 ? 1.1587 1.1640 1.0907 0.0066  -0.0662 -0.0199 441  CYS   D N   
11489 C  CA  . CYS   D 372 ? 1.1704 1.1858 1.1138 -0.0010 -0.0656 -0.0190 441  CYS   D CA  
11490 C  C   . CYS   D 372 ? 1.2122 1.2239 1.1540 -0.0057 -0.0631 -0.0181 441  CYS   D C   
11491 O  O   . CYS   D 372 ? 1.2082 1.2140 1.1438 -0.0031 -0.0638 -0.0198 441  CYS   D O   
11492 C  CB  . CYS   D 372 ? 1.1826 1.2087 1.1353 -0.0005 -0.0702 -0.0223 441  CYS   D CB  
11493 S  SG  . CYS   D 372 ? 1.2752 1.3140 1.2413 -0.0085 -0.0703 -0.0218 441  CYS   D SG  
11494 N  N   . LEU   D 373 ? 1.2109 1.2252 1.1578 -0.0125 -0.0603 -0.0153 442  LEU   D N   
11495 C  CA  . LEU   D 373 ? 1.2525 1.2633 1.1983 -0.0172 -0.0587 -0.0148 442  LEU   D CA  
11496 C  C   . LEU   D 373 ? 1.2893 1.3100 1.2448 -0.0227 -0.0607 -0.0159 442  LEU   D C   
11497 O  O   . LEU   D 373 ? 1.2491 1.2705 1.2079 -0.0287 -0.0594 -0.0144 442  LEU   D O   
11498 C  CB  . LEU   D 373 ? 1.1904 1.1945 1.1337 -0.0207 -0.0540 -0.0111 442  LEU   D CB  
11499 C  CG  . LEU   D 373 ? 1.1699 1.1812 1.1229 -0.0268 -0.0525 -0.0084 442  LEU   D CG  
11500 C  CD1 . LEU   D 373 ? 1.1697 1.1735 1.1205 -0.0299 -0.0476 -0.0050 442  LEU   D CD1 
11501 C  CD2 . LEU   D 373 ? 1.2161 1.2340 1.1733 -0.0242 -0.0535 -0.0082 442  LEU   D CD2 
11502 O  OXT . LEU   D 373 ? 1.2442 1.2723 1.2045 -0.0210 -0.0638 -0.0183 442  LEU   D OXT 
11503 N  N   . SER   E 2   ? 1.1040 1.2617 1.2519 -0.0988 -0.0709 0.0158  2    SER   E N   
11504 C  CA  . SER   E 2   ? 1.1666 1.3302 1.3185 -0.1002 -0.0768 0.0144  2    SER   E CA  
11505 C  C   . SER   E 2   ? 1.1884 1.3500 1.3418 -0.1044 -0.0827 0.0120  2    SER   E C   
11506 O  O   . SER   E 2   ? 1.1701 1.3260 1.3219 -0.1065 -0.0823 0.0113  2    SER   E O   
11507 C  CB  . SER   E 2   ? 1.1102 1.2745 1.2527 -0.0964 -0.0784 0.0130  2    SER   E CB  
11508 O  OG  . SER   E 2   ? 0.9641 1.1230 1.0965 -0.0963 -0.0811 0.0104  2    SER   E OG  
11509 N  N   . TYR   E 3   ? 1.1485 1.3145 1.3043 -0.1052 -0.0883 0.0106  3    TYR   E N   
11510 C  CA  . TYR   E 3   ? 1.1249 1.2892 1.2817 -0.1086 -0.0948 0.0082  3    TYR   E CA  
11511 C  C   . TYR   E 3   ? 1.0756 1.2389 1.2226 -0.1067 -0.0992 0.0060  3    TYR   E C   
11512 O  O   . TYR   E 3   ? 1.1031 1.2705 1.2487 -0.1040 -0.0988 0.0066  3    TYR   E O   
11513 C  CB  . TYR   E 3   ? 1.1399 1.3101 1.3110 -0.1117 -0.0978 0.0088  3    TYR   E CB  
11514 C  CG  . TYR   E 3   ? 1.1659 1.3396 1.3486 -0.1127 -0.0921 0.0118  3    TYR   E CG  
11515 C  CD1 . TYR   E 3   ? 1.1925 1.3616 1.3783 -0.1152 -0.0890 0.0125  3    TYR   E CD1 
11516 C  CD2 . TYR   E 3   ? 1.1997 1.3806 1.3899 -0.1109 -0.0895 0.0142  3    TYR   E CD2 
11517 C  CE1 . TYR   E 3   ? 1.2149 1.3866 1.4113 -0.1160 -0.0831 0.0156  3    TYR   E CE1 
11518 C  CE2 . TYR   E 3   ? 1.2429 1.4266 1.4436 -0.1114 -0.0837 0.0171  3    TYR   E CE2 
11519 C  CZ  . TYR   E 3   ? 1.2315 1.4106 1.4353 -0.1140 -0.0803 0.0179  3    TYR   E CZ  
11520 O  OH  . TYR   E 3   ? 1.1742 1.3557 1.3884 -0.1144 -0.0738 0.0212  3    TYR   E OH  
11521 N  N   . ASN   E 4   ? 1.0895 1.2469 1.2295 -0.1081 -0.1033 0.0034  4    ASN   E N   
11522 C  CA  . ASN   E 4   ? 1.0610 1.2157 1.1895 -0.1057 -0.1056 0.0016  4    ASN   E CA  
11523 C  C   . ASN   E 4   ? 1.1007 1.2514 1.2258 -0.1077 -0.1123 -0.0009 4    ASN   E C   
11524 O  O   . ASN   E 4   ? 1.1096 1.2580 1.2396 -0.1110 -0.1152 -0.0018 4    ASN   E O   
11525 C  CB  . ASN   E 4   ? 1.0463 1.1958 1.1644 -0.1031 -0.1013 0.0013  4    ASN   E CB  
11526 C  CG  . ASN   E 4   ? 1.0455 1.1987 1.1646 -0.1000 -0.0959 0.0034  4    ASN   E CG  
11527 O  OD1 . ASN   E 4   ? 1.1156 1.2733 1.2350 -0.0979 -0.0960 0.0039  4    ASN   E OD1 
11528 N  ND2 . ASN   E 4   ? 1.0417 1.1925 1.1609 -0.0994 -0.0912 0.0046  4    ASN   E ND2 
11529 N  N   . TYR   E 5   ? 1.0804 1.2297 1.1969 -0.1055 -0.1147 -0.0022 5    TYR   E N   
11530 C  CA  . TYR   E 5   ? 1.0509 1.1966 1.1628 -0.1064 -0.1213 -0.0045 5    TYR   E CA  
11531 C  C   . TYR   E 5   ? 1.0602 1.1995 1.1577 -0.1037 -0.1206 -0.0059 5    TYR   E C   
11532 O  O   . TYR   E 5   ? 1.0858 1.2273 1.1795 -0.1008 -0.1170 -0.0050 5    TYR   E O   
11533 C  CB  . TYR   E 5   ? 1.0599 1.2119 1.1782 -0.1060 -0.1248 -0.0039 5    TYR   E CB  
11534 C  CG  . TYR   E 5   ? 1.0449 1.1933 1.1571 -0.1057 -0.1316 -0.0060 5    TYR   E CG  
11535 C  CD1 . TYR   E 5   ? 1.0149 1.1598 1.1151 -0.1027 -0.1315 -0.0066 5    TYR   E CD1 
11536 C  CD2 . TYR   E 5   ? 1.0289 1.1773 1.1476 -0.1083 -0.1382 -0.0074 5    TYR   E CD2 
11537 C  CE1 . TYR   E 5   ? 1.0428 1.1833 1.1360 -0.1019 -0.1374 -0.0084 5    TYR   E CE1 
11538 C  CE2 . TYR   E 5   ? 1.0308 1.1750 1.1427 -0.1075 -0.1450 -0.0095 5    TYR   E CE2 
11539 C  CZ  . TYR   E 5   ? 1.0674 1.2072 1.1659 -0.1042 -0.1444 -0.0099 5    TYR   E CZ  
11540 O  OH  . TYR   E 5   ? 1.0487 1.1832 1.1390 -0.1029 -0.1507 -0.0119 5    TYR   E OH  
11541 N  N   . VAL   E 6   ? 1.0246 1.1560 1.1142 -0.1045 -0.1237 -0.0081 6    VAL   E N   
11542 C  CA  . VAL   E 6   ? 0.9743 1.0990 1.0501 -0.1019 -0.1225 -0.0094 6    VAL   E CA  
11543 C  C   . VAL   E 6   ? 0.9915 1.1110 1.0599 -0.1016 -0.1285 -0.0113 6    VAL   E C   
11544 O  O   . VAL   E 6   ? 1.0659 1.1832 1.1374 -0.1040 -0.1342 -0.0126 6    VAL   E O   
11545 C  CB  . VAL   E 6   ? 0.9645 1.0827 1.0348 -0.1022 -0.1200 -0.0103 6    VAL   E CB  
11546 C  CG1 . VAL   E 6   ? 1.0161 1.1382 1.0932 -0.1024 -0.1145 -0.0084 6    VAL   E CG1 
11547 C  CG2 . VAL   E 6   ? 0.9954 1.1075 1.0654 -0.1052 -0.1252 -0.0121 6    VAL   E CG2 
11548 N  N   . VAL   E 7   ? 0.9438 1.0609 1.0025 -0.0985 -0.1274 -0.0115 7    VAL   E N   
11549 C  CA  . VAL   E 7   ? 1.0211 1.1317 1.0705 -0.0975 -0.1326 -0.0133 7    VAL   E CA  
11550 C  C   . VAL   E 7   ? 1.0189 1.1230 1.0546 -0.0943 -0.1292 -0.0138 7    VAL   E C   
11551 O  O   . VAL   E 7   ? 0.9361 1.0432 0.9715 -0.0925 -0.1234 -0.0126 7    VAL   E O   
11552 C  CB  . VAL   E 7   ? 1.0129 1.1282 1.0663 -0.0970 -0.1362 -0.0127 7    VAL   E CB  
11553 C  CG1 . VAL   E 7   ? 1.0321 1.1530 1.0864 -0.0947 -0.1311 -0.0107 7    VAL   E CG1 
11554 C  CG2 . VAL   E 7   ? 1.0297 1.1367 1.0723 -0.0958 -0.1424 -0.0147 7    VAL   E CG2 
11555 N  N   . THR   E 8   ? 1.0015 1.0961 1.0260 -0.0935 -0.1330 -0.0158 8    THR   E N   
11556 C  CA  . THR   E 8   ? 1.0278 1.1154 1.0392 -0.0904 -0.1295 -0.0163 8    THR   E CA  
11557 C  C   . THR   E 8   ? 1.0426 1.1307 1.0492 -0.0877 -0.1284 -0.0154 8    THR   E C   
11558 O  O   . THR   E 8   ? 1.0994 1.1847 1.1025 -0.0872 -0.1336 -0.0160 8    THR   E O   
11559 C  CB  . THR   E 8   ? 1.0208 1.0969 1.0205 -0.0900 -0.1335 -0.0188 8    THR   E CB  
11560 O  OG1 . THR   E 8   ? 1.0604 1.1355 1.0644 -0.0926 -0.1338 -0.0196 8    THR   E OG1 
11561 C  CG2 . THR   E 8   ? 0.9932 1.0621 0.9792 -0.0863 -0.1291 -0.0190 8    THR   E CG2 
11562 N  N   . ALA   E 9   ? 0.9647 1.0564 0.9716 -0.0858 -0.1220 -0.0139 9    ALA   E N   
11563 C  CA  . ALA   E 9   ? 1.0279 1.1188 1.0293 -0.0831 -0.1200 -0.0130 9    ALA   E CA  
11564 C  C   . ALA   E 9   ? 1.0020 1.0824 0.9884 -0.0803 -0.1184 -0.0139 9    ALA   E C   
11565 O  O   . ALA   E 9   ? 1.0830 1.1580 1.0607 -0.0783 -0.1198 -0.0139 9    ALA   E O   
11566 C  CB  . ALA   E 9   ? 1.0528 1.1521 1.0618 -0.0825 -0.1139 -0.0111 9    ALA   E CB  
11567 N  N   . GLN   E 10  ? 1.0377 1.1145 1.0205 -0.0799 -0.1153 -0.0147 10   GLN   E N   
11568 C  CA  . GLN   E 10  ? 1.0451 1.1115 1.0138 -0.0771 -0.1132 -0.0157 10   GLN   E CA  
11569 C  C   . GLN   E 10  ? 1.0737 1.1340 1.0384 -0.0781 -0.1157 -0.0176 10   GLN   E C   
11570 O  O   . GLN   E 10  ? 1.0564 1.1206 1.0277 -0.0795 -0.1134 -0.0177 10   GLN   E O   
11571 C  CB  . GLN   E 10  ? 1.0219 1.0904 0.9902 -0.0748 -0.1052 -0.0145 10   GLN   E CB  
11572 C  CG  . GLN   E 10  ? 1.0489 1.1075 1.0041 -0.0718 -0.1019 -0.0153 10   GLN   E CG  
11573 C  CD  . GLN   E 10  ? 1.1573 1.2049 1.0982 -0.0698 -0.1055 -0.0161 10   GLN   E CD  
11574 O  OE1 . GLN   E 10  ? 1.2344 1.2792 1.1737 -0.0712 -0.1126 -0.0172 10   GLN   E OE1 
11575 N  NE2 . GLN   E 10  ? 1.1915 1.2322 1.1218 -0.0663 -0.1005 -0.0155 10   GLN   E NE2 
11576 N  N   . LYS   E 11  ? 1.1075 1.1575 1.0607 -0.0773 -0.1206 -0.0193 11   LYS   E N   
11577 C  CA  . LYS   E 11  ? 1.0371 1.0796 0.9847 -0.0779 -0.1232 -0.0214 11   LYS   E CA  
11578 C  C   . LYS   E 11  ? 1.0392 1.0780 0.9805 -0.0755 -0.1164 -0.0214 11   LYS   E C   
11579 O  O   . LYS   E 11  ? 1.0381 1.0771 0.9757 -0.0726 -0.1107 -0.0201 11   LYS   E O   
11580 C  CB  . LYS   E 11  ? 0.9741 1.0053 0.9093 -0.0768 -0.1301 -0.0234 11   LYS   E CB  
11581 N  N   . PRO   E 12  ? 1.0282 1.0639 0.9689 -0.0765 -0.1168 -0.0227 12   PRO   E N   
11582 C  CA  . PRO   E 12  ? 1.0160 1.0482 0.9511 -0.0740 -0.1107 -0.0228 12   PRO   E CA  
11583 C  C   . PRO   E 12  ? 0.9987 1.0205 0.9181 -0.0697 -0.1083 -0.0232 12   PRO   E C   
11584 O  O   . PRO   E 12  ? 0.9860 0.9980 0.8942 -0.0688 -0.1130 -0.0245 12   PRO   E O   
11585 C  CB  . PRO   E 12  ? 1.0542 1.0821 0.9889 -0.0759 -0.1137 -0.0245 12   PRO   E CB  
11586 C  CG  . PRO   E 12  ? 1.1058 1.1301 1.0401 -0.0785 -0.1223 -0.0259 12   PRO   E CG  
11587 C  CD  . PRO   E 12  ? 1.0525 1.0868 0.9974 -0.0799 -0.1231 -0.0242 12   PRO   E CD  
11588 N  N   . THR   E 13  ? 0.9980 1.0214 0.9165 -0.0670 -0.1007 -0.0221 13   THR   E N   
11589 C  CA  . THR   E 13  ? 1.0033 1.0182 0.9086 -0.0628 -0.0967 -0.0218 13   THR   E CA  
11590 C  C   . THR   E 13  ? 1.0070 1.0135 0.9024 -0.0599 -0.0931 -0.0229 13   THR   E C   
11591 O  O   . THR   E 13  ? 1.0134 1.0095 0.8946 -0.0563 -0.0914 -0.0231 13   THR   E O   
11592 C  CB  . THR   E 13  ? 1.0471 1.0697 0.9588 -0.0615 -0.0902 -0.0195 13   THR   E CB  
11593 O  OG1 . THR   E 13  ? 1.0431 1.0700 0.9600 -0.0602 -0.0835 -0.0191 13   THR   E OG1 
11594 C  CG2 . THR   E 13  ? 1.0353 1.0691 0.9608 -0.0647 -0.0928 -0.0184 13   THR   E CG2 
11595 N  N   . ALA   E 14  ? 1.0631 1.0731 0.9648 -0.0610 -0.0917 -0.0235 14   ALA   E N   
11596 C  CA  . ALA   E 14  ? 1.0643 1.0664 0.9571 -0.0583 -0.0887 -0.0247 14   ALA   E CA  
11597 C  C   . ALA   E 14  ? 1.0479 1.0374 0.9277 -0.0583 -0.0949 -0.0269 14   ALA   E C   
11598 O  O   . ALA   E 14  ? 1.0601 1.0496 0.9426 -0.0616 -0.1021 -0.0278 14   ALA   E O   
11599 C  CB  . ALA   E 14  ? 1.0575 1.0667 0.9606 -0.0596 -0.0864 -0.0249 14   ALA   E CB  
11600 N  N   . VAL   E 15  ? 1.0622 1.0408 0.9281 -0.0544 -0.0922 -0.0278 15   VAL   E N   
11601 C  CA  . VAL   E 15  ? 1.1245 1.0897 0.9766 -0.0538 -0.0979 -0.0302 15   VAL   E CA  
11602 C  C   . VAL   E 15  ? 1.0957 1.0587 0.9480 -0.0540 -0.0970 -0.0315 15   VAL   E C   
11603 O  O   . VAL   E 15  ? 1.1162 1.0813 0.9695 -0.0514 -0.0901 -0.0308 15   VAL   E O   
11604 C  CB  . VAL   E 15  ? 1.1501 1.1021 0.9837 -0.0488 -0.0961 -0.0304 15   VAL   E CB  
11605 C  CG1 . VAL   E 15  ? 1.1329 1.0882 0.9671 -0.0479 -0.0944 -0.0285 15   VAL   E CG1 
11606 C  CG2 . VAL   E 15  ? 1.1462 1.0940 0.9732 -0.0445 -0.0881 -0.0301 15   VAL   E CG2 
11607 N  N   . ASN   E 16  ? 1.1191 1.0779 0.9709 -0.0571 -0.1041 -0.0334 16   ASN   E N   
11608 C  CA  . ASN   E 16  ? 1.1898 1.1444 1.0401 -0.0573 -0.1040 -0.0348 16   ASN   E CA  
11609 C  C   . ASN   E 16  ? 1.1709 1.1093 1.0037 -0.0552 -0.1080 -0.0373 16   ASN   E C   
11610 O  O   . ASN   E 16  ? 1.2703 1.2035 1.0996 -0.0547 -0.1075 -0.0385 16   ASN   E O   
11611 C  CB  . ASN   E 16  ? 1.1555 1.1180 1.0201 -0.0627 -0.1080 -0.0349 16   ASN   E CB  
11612 C  CG  . ASN   E 16  ? 1.1463 1.1086 1.0140 -0.0665 -0.1162 -0.0357 16   ASN   E CG  
11613 O  OD1 . ASN   E 16  ? 1.2262 1.1890 1.0919 -0.0659 -0.1179 -0.0352 16   ASN   E OD1 
11614 N  ND2 . ASN   E 16  ? 1.1291 1.0907 1.0023 -0.0705 -0.1212 -0.0369 16   ASN   E ND2 
11615 N  N   . GLY   E 17  ? 1.2011 1.1305 1.0222 -0.0536 -0.1121 -0.0381 17   GLY   E N   
11616 C  CA  . GLY   E 17  ? 1.2740 1.1869 1.0769 -0.0507 -0.1154 -0.0405 17   GLY   E CA  
11617 C  C   . GLY   E 17  ? 1.2867 1.1892 1.0749 -0.0477 -0.1189 -0.0411 17   GLY   E C   
11618 O  O   . GLY   E 17  ? 1.3069 1.2144 1.1003 -0.0495 -0.1224 -0.0405 17   GLY   E O   
11619 N  N   . CYS   E 18  ? 1.2625 1.1497 1.0314 -0.0428 -0.1183 -0.0425 18   CYS   E N   
11620 C  CA  . CYS   E 18  ? 1.2224 1.0987 0.9751 -0.0386 -0.1198 -0.0428 18   CYS   E CA  
11621 C  C   . CYS   E 18  ? 1.2944 1.1518 1.0262 -0.0347 -0.1233 -0.0455 18   CYS   E C   
11622 O  O   . CYS   E 18  ? 1.3587 1.2110 1.0835 -0.0314 -0.1173 -0.0455 18   CYS   E O   
11623 C  CB  . CYS   E 18  ? 1.1962 1.0768 0.9480 -0.0347 -0.1096 -0.0397 18   CYS   E CB  
11624 S  SG  . CYS   E 18  ? 1.3659 1.2487 1.1176 -0.0305 -0.0967 -0.0379 18   CYS   E SG  
11625 N  N   . VAL   E 19  ? 1.2811 1.1281 1.0033 -0.0350 -0.1331 -0.0480 19   VAL   E N   
11626 C  CA  . VAL   E 19  ? 1.3014 1.1290 1.0022 -0.0310 -0.1374 -0.0508 19   VAL   E CA  
11627 C  C   . VAL   E 19  ? 1.3069 1.1223 0.9902 -0.0265 -0.1410 -0.0514 19   VAL   E C   
11628 O  O   . VAL   E 19  ? 1.3042 1.1255 0.9936 -0.0282 -0.1443 -0.0507 19   VAL   E O   
11629 C  CB  . VAL   E 19  ? 1.3287 1.1524 1.0328 -0.0355 -0.1477 -0.0542 19   VAL   E CB  
11630 C  CG1 . VAL   E 19  ? 1.3033 1.1338 1.0185 -0.0383 -0.1434 -0.0539 19   VAL   E CG1 
11631 C  CG2 . VAL   E 19  ? 1.2826 1.1147 1.0006 -0.0410 -0.1564 -0.0548 19   VAL   E CG2 
11632 N  N   . THR   E 20  ? 1.3541 1.1517 1.0148 -0.0204 -0.1401 -0.0527 20   THR   E N   
11633 C  CA  . THR   E 20  ? 1.3662 1.1481 1.0064 -0.0155 -0.1452 -0.0541 20   THR   E CA  
11634 C  C   . THR   E 20  ? 1.4255 1.1945 1.0569 -0.0167 -0.1582 -0.0586 20   THR   E C   
11635 O  O   . THR   E 20  ? 1.4192 1.1883 1.0560 -0.0199 -0.1611 -0.0605 20   THR   E O   
11636 C  CB  . THR   E 20  ? 1.3838 1.1525 1.0028 -0.0073 -0.1359 -0.0527 20   THR   E CB  
11637 O  OG1 . THR   E 20  ? 1.5665 1.3212 1.1714 -0.0046 -0.1373 -0.0552 20   THR   E OG1 
11638 C  CG2 . THR   E 20  ? 1.3192 1.1011 0.9498 -0.0069 -0.1225 -0.0487 20   THR   E CG2 
11639 N  N   . GLY   E 21  ? 1.4399 1.1971 1.0573 -0.0140 -0.1664 -0.0605 21   GLY   E N   
11640 C  CA  . GLY   E 21  ? 1.4778 1.2225 1.0872 -0.0150 -0.1797 -0.0651 21   GLY   E CA  
11641 C  C   . GLY   E 21  ? 1.5455 1.2807 1.1431 -0.0123 -0.1887 -0.0668 21   GLY   E C   
11642 O  O   . GLY   E 21  ? 1.5161 1.2503 1.1061 -0.0081 -0.1835 -0.0644 21   GLY   E O   
11643 N  N   . HIS   E 22  ? 1.5405 1.2684 1.1370 -0.0148 -0.2024 -0.0711 22   HIS   E N   
11644 C  CA  . HIS   E 22  ? 1.5719 1.2904 1.1584 -0.0127 -0.2136 -0.0737 22   HIS   E CA  
11645 C  C   . HIS   E 22  ? 1.5964 1.3257 1.2048 -0.0207 -0.2253 -0.0762 22   HIS   E C   
11646 O  O   . HIS   E 22  ? 1.6464 1.3667 1.2522 -0.0224 -0.2364 -0.0805 22   HIS   E O   
11647 C  CB  . HIS   E 22  ? 1.5940 1.2871 1.1508 -0.0055 -0.2193 -0.0771 22   HIS   E CB  
11648 C  CG  . HIS   E 22  ? 1.5854 1.2688 1.1252 0.0004  -0.2078 -0.0753 22   HIS   E CG  
11649 N  ND1 . HIS   E 22  ? 1.5667 1.2440 1.0906 0.0074  -0.1974 -0.0721 22   HIS   E ND1 
11650 C  CD2 . HIS   E 22  ? 1.6083 1.2871 1.1451 0.0003  -0.2046 -0.0762 22   HIS   E CD2 
11651 C  CE1 . HIS   E 22  ? 1.6071 1.2767 1.1193 0.0115  -0.1883 -0.0711 22   HIS   E CE1 
11652 N  NE2 . HIS   E 22  ? 1.6463 1.3166 1.1657 0.0074  -0.1926 -0.0736 22   HIS   E NE2 
11653 N  N   . PHE   E 23  ? 1.5811 1.3300 1.2116 -0.0254 -0.2225 -0.0734 23   PHE   E N   
11654 C  CA  . PHE   E 23  ? 1.5994 1.3625 1.2544 -0.0333 -0.2307 -0.0746 23   PHE   E CA  
11655 C  C   . PHE   E 23  ? 1.6511 1.4119 1.3049 -0.0325 -0.2416 -0.0765 23   PHE   E C   
11656 O  O   . PHE   E 23  ? 1.6553 1.4166 1.3188 -0.0368 -0.2538 -0.0801 23   PHE   E O   
11657 C  CB  . PHE   E 23  ? 1.5648 1.3504 1.2438 -0.0383 -0.2203 -0.0702 23   PHE   E CB  
11658 C  CG  . PHE   E 23  ? 1.5413 1.3421 1.2468 -0.0467 -0.2260 -0.0709 23   PHE   E CG  
11659 C  CD1 . PHE   E 23  ? 1.5573 1.3536 1.2673 -0.0506 -0.2335 -0.0743 23   PHE   E CD1 
11660 C  CD2 . PHE   E 23  ? 1.4773 1.2962 1.2030 -0.0506 -0.2238 -0.0683 23   PHE   E CD2 
11661 C  CE1 . PHE   E 23  ? 1.5013 1.3110 1.2357 -0.0583 -0.2382 -0.0747 23   PHE   E CE1 
11662 C  CE2 . PHE   E 23  ? 1.4775 1.3096 1.2269 -0.0579 -0.2286 -0.0688 23   PHE   E CE2 
11663 C  CZ  . PHE   E 23  ? 1.5055 1.3331 1.2596 -0.0618 -0.2356 -0.0719 23   PHE   E CZ  
11664 N  N   . THR   E 24  ? 1.6855 1.4437 1.3278 -0.0271 -0.2372 -0.0743 24   THR   E N   
11665 C  CA  . THR   E 24  ? 1.7344 1.4891 1.3724 -0.0251 -0.2465 -0.0757 24   THR   E CA  
11666 C  C   . THR   E 24  ? 1.7845 1.5156 1.3973 -0.0194 -0.2582 -0.0805 24   THR   E C   
11667 O  O   . THR   E 24  ? 1.8012 1.5300 1.4184 -0.0213 -0.2719 -0.0843 24   THR   E O   
11668 C  CB  . THR   E 24  ? 1.7588 1.5180 1.3923 -0.0211 -0.2368 -0.0713 24   THR   E CB  
11669 O  OG1 . THR   E 24  ? 1.7642 1.5048 1.3688 -0.0124 -0.2316 -0.0707 24   THR   E OG1 
11670 C  CG2 . THR   E 24  ? 1.6946 1.4738 1.3483 -0.0254 -0.2236 -0.0666 24   THR   E CG2 
11671 N  N   . SER   E 25  ? 1.7354 1.4487 1.3221 -0.0122 -0.2530 -0.0805 25   SER   E N   
11672 C  CA  . SER   E 25  ? 1.6924 1.3815 1.2527 -0.0062 -0.2628 -0.0849 25   SER   E CA  
11673 C  C   . SER   E 25  ? 1.7055 1.3822 1.2481 -0.0019 -0.2542 -0.0844 25   SER   E C   
11674 O  O   . SER   E 25  ? 1.6326 1.3173 1.1786 -0.0016 -0.2398 -0.0801 25   SER   E O   
11675 C  CB  . SER   E 25  ? 1.7370 1.4129 1.2761 0.0014  -0.2664 -0.0852 25   SER   E CB  
11676 O  OG  . SER   E 25  ? 1.7574 1.4095 1.2639 0.0104  -0.2645 -0.0861 25   SER   E OG  
11677 N  N   . ALA   E 26  ? 1.7225 1.3795 1.2465 0.0013  -0.2634 -0.0890 26   ALA   E N   
11678 C  CA  . ALA   E 26  ? 1.6968 1.3391 1.2001 0.0067  -0.2557 -0.0887 26   ALA   E CA  
11679 C  C   . ALA   E 26  ? 1.7284 1.3598 1.2081 0.0158  -0.2449 -0.0853 26   ALA   E C   
11680 O  O   . ALA   E 26  ? 1.6941 1.3194 1.1620 0.0198  -0.2336 -0.0831 26   ALA   E O   
11681 C  CB  . ALA   E 26  ? 1.5602 1.1823 1.0473 0.0087  -0.2688 -0.0945 26   ALA   E CB  
11682 N  N   . GLU   E 27  ? 1.7412 1.3714 1.2155 0.0189  -0.2473 -0.0844 27   GLU   E N   
11683 C  CA  . GLU   E 27  ? 1.7144 1.3331 1.1659 0.0275  -0.2377 -0.0812 27   GLU   E CA  
11684 C  C   . GLU   E 27  ? 1.7392 1.3771 1.2069 0.0254  -0.2231 -0.0752 27   GLU   E C   
11685 O  O   . GLU   E 27  ? 1.7642 1.3945 1.2157 0.0320  -0.2136 -0.0719 27   GLU   E O   
11686 C  CB  . GLU   E 27  ? 1.6827 1.2852 1.1147 0.0332  -0.2493 -0.0840 27   GLU   E CB  
11687 N  N   . ASP   E 28  ? 1.7329 1.3945 1.2316 0.0166  -0.2209 -0.0736 28   ASP   E N   
11688 C  CA  . ASP   E 28  ? 1.6964 1.3774 1.2129 0.0138  -0.2079 -0.0683 28   ASP   E CA  
11689 C  C   . ASP   E 28  ? 1.6723 1.3642 1.2014 0.0106  -0.1964 -0.0659 28   ASP   E C   
11690 O  O   . ASP   E 28  ? 1.7017 1.3959 1.2393 0.0064  -0.2007 -0.0684 28   ASP   E O   
11691 C  CB  . ASP   E 28  ? 1.6780 1.3788 1.2212 0.0064  -0.2140 -0.0681 28   ASP   E CB  
11692 C  CG  . ASP   E 28  ? 1.7638 1.4571 1.2973 0.0096  -0.2235 -0.0695 28   ASP   E CG  
11693 O  OD1 . ASP   E 28  ? 1.8592 1.5343 1.3662 0.0179  -0.2217 -0.0692 28   ASP   E OD1 
11694 O  OD2 . ASP   E 28  ? 1.7804 1.4859 1.3328 0.0041  -0.2324 -0.0709 28   ASP   E OD2 
11695 N  N   . LEU   E 29  ? 1.6163 1.3151 1.1472 0.0126  -0.1818 -0.0612 29   LEU   E N   
11696 C  CA  . LEU   E 29  ? 1.5860 1.2985 1.1325 0.0093  -0.1703 -0.0585 29   LEU   E CA  
11697 C  C   . LEU   E 29  ? 1.5575 1.2948 1.1344 0.0016  -0.1685 -0.0562 29   LEU   E C   
11698 O  O   . LEU   E 29  ? 1.5379 1.2829 1.1197 0.0021  -0.1629 -0.0530 29   LEU   E O   
11699 C  CB  . LEU   E 29  ? 1.5336 1.2399 1.0664 0.0158  -0.1554 -0.0548 29   LEU   E CB  
11700 C  CG  . LEU   E 29  ? 1.4786 1.1970 1.0264 0.0126  -0.1462 -0.0532 29   LEU   E CG  
11701 C  CD1 . LEU   E 29  ? 1.4673 1.1853 1.0213 0.0081  -0.1558 -0.0572 29   LEU   E CD1 
11702 C  CD2 . LEU   E 29  ? 1.4017 1.1092 0.9321 0.0199  -0.1334 -0.0508 29   LEU   E CD2 
11703 N  N   . ASN   E 30  ? 1.5012 1.2504 1.0977 -0.0054 -0.1729 -0.0577 30   ASN   E N   
11704 C  CA  . ASN   E 30  ? 1.4775 1.2493 1.1024 -0.0128 -0.1720 -0.0559 30   ASN   E CA  
11705 C  C   . ASN   E 30  ? 1.4653 1.2506 1.1043 -0.0150 -0.1596 -0.0527 30   ASN   E C   
11706 O  O   . ASN   E 30  ? 1.4612 1.2413 1.0949 -0.0137 -0.1558 -0.0533 30   ASN   E O   
11707 C  CB  . ASN   E 30  ? 1.4673 1.2445 1.1068 -0.0194 -0.1845 -0.0593 30   ASN   E CB  
11708 C  CG  . ASN   E 30  ? 1.5440 1.3123 1.1756 -0.0184 -0.1975 -0.0624 30   ASN   E CG  
11709 O  OD1 . ASN   E 30  ? 1.5688 1.3376 1.1971 -0.0161 -0.1975 -0.0610 30   ASN   E OD1 
11710 N  ND2 . ASN   E 30  ? 1.5288 1.2888 1.1579 -0.0203 -0.2090 -0.0667 30   ASN   E ND2 
11711 N  N   . LEU   E 31  ? 1.4428 1.2453 1.0997 -0.0181 -0.1538 -0.0494 31   LEU   E N   
11712 C  CA  . LEU   E 31  ? 1.3648 1.1833 1.0401 -0.0215 -0.1444 -0.0468 31   LEU   E CA  
11713 C  C   . LEU   E 31  ? 1.3374 1.1731 1.0373 -0.0292 -0.1499 -0.0471 31   LEU   E C   
11714 O  O   . LEU   E 31  ? 1.3125 1.1567 1.0215 -0.0311 -0.1521 -0.0459 31   LEU   E O   
11715 C  CB  . LEU   E 31  ? 1.3188 1.1425 0.9942 -0.0183 -0.1321 -0.0427 31   LEU   E CB  
11716 C  CG  . LEU   E 31  ? 1.3152 1.1560 1.0108 -0.0219 -0.1233 -0.0404 31   LEU   E CG  
11717 C  CD1 . LEU   E 31  ? 1.2572 1.0956 0.9534 -0.0231 -0.1241 -0.0424 31   LEU   E CD1 
11718 C  CD2 . LEU   E 31  ? 1.3395 1.1816 1.0317 -0.0176 -0.1104 -0.0368 31   LEU   E CD2 
11719 N  N   . LEU   E 32  ? 1.3319 1.1717 1.0418 -0.0334 -0.1523 -0.0487 32   LEU   E N   
11720 C  CA  . LEU   E 32  ? 1.2560 1.1118 0.9896 -0.0407 -0.1562 -0.0487 32   LEU   E CA  
11721 C  C   . LEU   E 32  ? 1.2711 1.1421 1.0205 -0.0427 -0.1457 -0.0456 32   LEU   E C   
11722 O  O   . LEU   E 32  ? 1.2574 1.1262 1.0041 -0.0415 -0.1402 -0.0455 32   LEU   E O   
11723 C  CB  . LEU   E 32  ? 1.2023 1.0532 0.9378 -0.0442 -0.1649 -0.0521 32   LEU   E CB  
11724 C  CG  . LEU   E 32  ? 1.3076 1.1467 1.0330 -0.0436 -0.1774 -0.0555 32   LEU   E CG  
11725 C  CD1 . LEU   E 32  ? 1.2907 1.1312 1.0274 -0.0495 -0.1868 -0.0585 32   LEU   E CD1 
11726 C  CD2 . LEU   E 32  ? 1.3276 1.1728 1.0572 -0.0435 -0.1796 -0.0542 32   LEU   E CD2 
11727 N  N   . ILE   E 33  ? 1.2899 1.1759 1.0554 -0.0456 -0.1433 -0.0431 33   ILE   E N   
11728 C  CA  . ILE   E 33  ? 1.2010 1.1020 0.9824 -0.0475 -0.1343 -0.0403 33   ILE   E CA  
11729 C  C   . ILE   E 33  ? 1.1923 1.1068 0.9946 -0.0542 -0.1384 -0.0405 33   ILE   E C   
11730 O  O   . ILE   E 33  ? 1.1591 1.0768 0.9681 -0.0572 -0.1461 -0.0413 33   ILE   E O   
11731 C  CB  . ILE   E 33  ? 1.1773 1.0844 0.9602 -0.0452 -0.1271 -0.0372 33   ILE   E CB  
11732 C  CG1 . ILE   E 33  ? 1.2464 1.1431 1.0127 -0.0389 -0.1189 -0.0363 33   ILE   E CG1 
11733 C  CG2 . ILE   E 33  ? 1.1377 1.0627 0.9414 -0.0488 -0.1214 -0.0348 33   ILE   E CG2 
11734 C  CD1 . ILE   E 33  ? 1.2767 1.1777 1.0433 -0.0364 -0.1117 -0.0332 33   ILE   E CD1 
11735 N  N   . ALA   E 34  ? 1.1637 1.0858 0.9762 -0.0561 -0.1333 -0.0397 34   ALA   E N   
11736 C  CA  . ALA   E 34  ? 1.1323 1.0664 0.9638 -0.0619 -0.1355 -0.0395 34   ALA   E CA  
11737 C  C   . ALA   E 34  ? 1.1530 1.1021 0.9988 -0.0627 -0.1275 -0.0364 34   ALA   E C   
11738 O  O   . ALA   E 34  ? 1.1263 1.0761 0.9697 -0.0598 -0.1195 -0.0352 34   ALA   E O   
11739 C  CB  . ALA   E 34  ? 1.0360 0.9651 0.8668 -0.0635 -0.1370 -0.0413 34   ALA   E CB  
11740 N  N   . LYS   E 35  ? 1.1292 1.0900 0.9902 -0.0666 -0.1299 -0.0353 35   LYS   E N   
11741 C  CA  . LYS   E 35  ? 1.0437 1.0187 0.9188 -0.0676 -0.1235 -0.0326 35   LYS   E CA  
11742 C  C   . LYS   E 35  ? 1.1049 1.0899 0.9970 -0.0729 -0.1265 -0.0324 35   LYS   E C   
11743 O  O   . LYS   E 35  ? 1.1485 1.1416 1.0510 -0.0755 -0.1295 -0.0316 35   LYS   E O   
11744 C  CB  . LYS   E 35  ? 1.0915 1.0700 0.9663 -0.0660 -0.1222 -0.0309 35   LYS   E CB  
11745 C  CG  . LYS   E 35  ? 0.9946 0.9664 0.8559 -0.0606 -0.1157 -0.0300 35   LYS   E CG  
11746 C  CD  . LYS   E 35  ? 1.0305 1.0002 0.8865 -0.0589 -0.1177 -0.0292 35   LYS   E CD  
11747 C  CE  . LYS   E 35  ? 1.1083 1.0728 0.9532 -0.0539 -0.1100 -0.0276 35   LYS   E CE  
11748 N  NZ  . LYS   E 35  ? 0.9606 0.9216 0.7987 -0.0519 -0.1116 -0.0267 35   LYS   E NZ  
11749 N  N   . ASN   E 36  ? 1.1178 1.1014 1.0119 -0.0742 -0.1256 -0.0332 36   ASN   E N   
11750 C  CA  . ASN   E 36  ? 1.1390 1.1307 1.0480 -0.0788 -0.1272 -0.0328 36   ASN   E CA  
11751 C  C   . ASN   E 36  ? 1.1267 1.1170 1.0403 -0.0828 -0.1359 -0.0342 36   ASN   E C   
11752 O  O   . ASN   E 36  ? 1.1305 1.1127 1.0402 -0.0843 -0.1405 -0.0363 36   ASN   E O   
11753 C  CB  . ASN   E 36  ? 1.1039 1.1098 1.0270 -0.0797 -0.1221 -0.0302 36   ASN   E CB  
11754 C  CG  . ASN   E 36  ? 1.0894 1.1019 1.0253 -0.0833 -0.1215 -0.0296 36   ASN   E CG  
11755 O  OD1 . ASN   E 36  ? 1.1053 1.1121 1.0402 -0.0854 -0.1245 -0.0310 36   ASN   E OD1 
11756 N  ND2 . ASN   E 36  ? 1.0536 1.0776 1.0011 -0.0839 -0.1174 -0.0274 36   ASN   E ND2 
11757 N  N   . THR   E 37  ? 1.1244 1.1231 1.0476 -0.0846 -0.1383 -0.0331 37   THR   E N   
11758 C  CA  . THR   E 37  ? 1.0977 1.0968 1.0277 -0.0884 -0.1466 -0.0344 37   THR   E CA  
11759 C  C   . THR   E 37  ? 1.1508 1.1427 1.0705 -0.0863 -0.1526 -0.0359 37   THR   E C   
11760 O  O   . THR   E 37  ? 1.1864 1.1783 1.1112 -0.0890 -0.1604 -0.0372 37   THR   E O   
11761 C  CB  . THR   E 37  ? 1.0991 1.1124 1.0474 -0.0918 -0.1458 -0.0322 37   THR   E CB  
11762 O  OG1 . THR   E 37  ? 1.1834 1.2017 1.1319 -0.0899 -0.1452 -0.0309 37   THR   E OG1 
11763 C  CG2 . THR   E 37  ? 1.1298 1.1507 1.0863 -0.0923 -0.1382 -0.0302 37   THR   E CG2 
11764 N  N   . ARG   E 38  ? 1.1548 1.1405 1.0603 -0.0815 -0.1492 -0.0357 38   ARG   E N   
11765 C  CA  . ARG   E 38  ? 1.1772 1.1554 1.0712 -0.0787 -0.1539 -0.0367 38   ARG   E CA  
11766 C  C   . ARG   E 38  ? 1.1911 1.1531 1.0651 -0.0749 -0.1553 -0.0389 38   ARG   E C   
11767 O  O   . ARG   E 38  ? 1.1895 1.1478 1.0570 -0.0727 -0.1492 -0.0386 38   ARG   E O   
11768 C  CB  . ARG   E 38  ? 1.1083 1.0925 1.0021 -0.0759 -0.1483 -0.0341 38   ARG   E CB  
11769 C  CG  . ARG   E 38  ? 1.1083 1.1083 1.0209 -0.0792 -0.1453 -0.0317 38   ARG   E CG  
11770 C  CD  . ARG   E 38  ? 1.1303 1.1352 1.0544 -0.0832 -0.1533 -0.0326 38   ARG   E CD  
11771 N  NE  . ARG   E 38  ? 1.1671 1.1661 1.0830 -0.0812 -0.1597 -0.0337 38   ARG   E NE  
11772 C  CZ  . ARG   E 38  ? 1.1952 1.1984 1.1199 -0.0836 -0.1668 -0.0344 38   ARG   E CZ  
11773 N  NH1 . ARG   E 38  ? 1.1535 1.1670 1.0960 -0.0883 -0.1683 -0.0339 38   ARG   E NH1 
11774 N  NH2 . ARG   E 38  ? 1.1566 1.1534 1.0719 -0.0811 -0.1725 -0.0355 38   ARG   E NH2 
11775 N  N   . LEU   E 39  ? 1.2091 1.1613 1.0734 -0.0738 -0.1637 -0.0413 39   LEU   E N   
11776 C  CA  . LEU   E 39  ? 1.1876 1.1229 1.0309 -0.0695 -0.1659 -0.0435 39   LEU   E CA  
11777 C  C   . LEU   E 39  ? 1.2228 1.1518 1.0529 -0.0648 -0.1664 -0.0431 39   LEU   E C   
11778 O  O   . LEU   E 39  ? 1.2265 1.1581 1.0606 -0.0658 -0.1727 -0.0436 39   LEU   E O   
11779 C  CB  . LEU   E 39  ? 1.1372 1.0640 0.9788 -0.0720 -0.1762 -0.0471 39   LEU   E CB  
11780 C  CG  . LEU   E 39  ? 1.2604 1.1684 1.0789 -0.0672 -0.1799 -0.0498 39   LEU   E CG  
11781 C  CD1 . LEU   E 39  ? 1.2703 1.1729 1.0774 -0.0633 -0.1704 -0.0487 39   LEU   E CD1 
11782 C  CD2 . LEU   E 39  ? 1.1875 1.0872 1.0053 -0.0699 -0.1900 -0.0536 39   LEU   E CD2 
11783 N  N   . GLU   E 40  ? 1.1809 1.1019 0.9956 -0.0596 -0.1596 -0.0422 40   GLU   E N   
11784 C  CA  . GLU   E 40  ? 1.2685 1.1816 1.0685 -0.0546 -0.1592 -0.0417 40   GLU   E CA  
11785 C  C   . GLU   E 40  ? 1.2871 1.1807 1.0643 -0.0500 -0.1634 -0.0444 40   GLU   E C   
11786 O  O   . GLU   E 40  ? 1.2918 1.1784 1.0609 -0.0484 -0.1597 -0.0450 40   GLU   E O   
11787 C  CB  . GLU   E 40  ? 1.2088 1.1272 1.0085 -0.0518 -0.1476 -0.0381 40   GLU   E CB  
11788 C  CG  . GLU   E 40  ? 1.2114 1.1476 1.0319 -0.0558 -0.1446 -0.0357 40   GLU   E CG  
11789 C  CD  . GLU   E 40  ? 1.2514 1.1936 1.0734 -0.0534 -0.1340 -0.0324 40   GLU   E CD  
11790 O  OE1 . GLU   E 40  ? 1.2398 1.1737 1.0489 -0.0491 -0.1274 -0.0319 40   GLU   E OE1 
11791 O  OE2 . GLU   E 40  ? 1.1829 1.1380 1.0194 -0.0559 -0.1323 -0.0305 40   GLU   E OE2 
11792 N  N   . ILE   E 41  ? 1.3052 1.1898 1.0718 -0.0477 -0.1712 -0.0460 41   ILE   E N   
11793 C  CA  . ILE   E 41  ? 1.3509 1.2156 1.0941 -0.0428 -0.1763 -0.0488 41   ILE   E CA  
11794 C  C   . ILE   E 41  ? 1.3991 1.2550 1.1252 -0.0365 -0.1725 -0.0472 41   ILE   E C   
11795 O  O   . ILE   E 41  ? 1.3912 1.2504 1.1199 -0.0364 -0.1761 -0.0466 41   ILE   E O   
11796 C  CB  . ILE   E 41  ? 1.3250 1.1841 1.0685 -0.0451 -0.1904 -0.0528 41   ILE   E CB  
11797 C  CG1 . ILE   E 41  ? 1.2598 1.1266 1.0202 -0.0514 -0.1936 -0.0542 41   ILE   E CG1 
11798 C  CG2 . ILE   E 41  ? 1.3622 1.1994 1.0792 -0.0390 -0.1957 -0.0556 41   ILE   E CG2 
11799 C  CD1 . ILE   E 41  ? 1.2718 1.1399 1.0416 -0.0554 -0.2063 -0.0573 41   ILE   E CD1 
11800 N  N   . TYR   E 42  ? 1.3784 1.2223 1.0863 -0.0310 -0.1654 -0.0465 42   TYR   E N   
11801 C  CA  . TYR   E 42  ? 1.3914 1.2245 1.0805 -0.0243 -0.1604 -0.0449 42   TYR   E CA  
11802 C  C   . TYR   E 42  ? 1.4422 1.2529 1.1049 -0.0184 -0.1651 -0.0477 42   TYR   E C   
11803 O  O   . TYR   E 42  ? 1.3957 1.1998 1.0544 -0.0191 -0.1689 -0.0504 42   TYR   E O   
11804 C  CB  . TYR   E 42  ? 1.3942 1.2332 1.0855 -0.0225 -0.1457 -0.0409 42   TYR   E CB  
11805 C  CG  . TYR   E 42  ? 1.3866 1.2464 1.1019 -0.0274 -0.1404 -0.0379 42   TYR   E CG  
11806 C  CD1 . TYR   E 42  ? 1.4411 1.3075 1.1627 -0.0283 -0.1422 -0.0365 42   TYR   E CD1 
11807 C  CD2 . TYR   E 42  ? 1.3601 1.2322 1.0910 -0.0308 -0.1336 -0.0367 42   TYR   E CD2 
11808 C  CE1 . TYR   E 42  ? 1.4169 1.3018 1.1599 -0.0326 -0.1375 -0.0339 42   TYR   E CE1 
11809 C  CE2 . TYR   E 42  ? 1.3900 1.2805 1.1422 -0.0350 -0.1291 -0.0342 42   TYR   E CE2 
11810 C  CZ  . TYR   E 42  ? 1.3709 1.2675 1.1289 -0.0358 -0.1310 -0.0328 42   TYR   E CZ  
11811 O  OH  . TYR   E 42  ? 1.3229 1.2367 1.1008 -0.0397 -0.1269 -0.0304 42   TYR   E OH  
11812 N  N   . VAL   E 43  ? 1.5310 1.3294 1.1750 -0.0124 -0.1644 -0.0470 43   VAL   E N   
11813 C  CA  . VAL   E 43  ? 1.5362 1.3118 1.1518 -0.0052 -0.1661 -0.0488 43   VAL   E CA  
11814 C  C   . VAL   E 43  ? 1.5695 1.3395 1.1724 0.0006  -0.1519 -0.0451 43   VAL   E C   
11815 O  O   . VAL   E 43  ? 1.5519 1.3276 1.1578 0.0017  -0.1451 -0.0417 43   VAL   E O   
11816 C  CB  . VAL   E 43  ? 1.4771 1.2402 1.0781 -0.0019 -0.1776 -0.0513 43   VAL   E CB  
11817 C  CG1 . VAL   E 43  ? 1.4947 1.2334 1.0643 0.0067  -0.1770 -0.0525 43   VAL   E CG1 
11818 C  CG2 . VAL   E 43  ? 1.4564 1.2234 1.0693 -0.0073 -0.1920 -0.0555 43   VAL   E CG2 
11819 N  N   . VAL   E 44  ? 1.5423 1.3006 1.1310 0.0045  -0.1473 -0.0457 44   VAL   E N   
11820 C  CA  . VAL   E 44  ? 1.6048 1.3584 1.1834 0.0097  -0.1330 -0.0422 44   VAL   E CA  
11821 C  C   . VAL   E 44  ? 1.7132 1.4474 1.2651 0.0177  -0.1325 -0.0417 44   VAL   E C   
11822 O  O   . VAL   E 44  ? 1.7487 1.4632 1.2776 0.0228  -0.1381 -0.0445 44   VAL   E O   
11823 C  CB  . VAL   E 44  ? 1.4883 1.2369 1.0622 0.0110  -0.1283 -0.0431 44   VAL   E CB  
11824 C  CG1 . VAL   E 44  ? 1.5313 1.2671 1.0858 0.0187  -0.1163 -0.0406 44   VAL   E CG1 
11825 C  CG2 . VAL   E 44  ? 1.4577 1.2270 1.0581 0.0044  -0.1233 -0.0418 44   VAL   E CG2 
11826 N  N   . THR   E 45  ? 1.7628 1.5016 1.3169 0.0189  -0.1258 -0.0382 45   THR   E N   
11827 C  CA  . THR   E 45  ? 1.7917 1.5121 1.3202 0.0269  -0.1230 -0.0369 45   THR   E CA  
11828 C  C   . THR   E 45  ? 1.8480 1.5611 1.3650 0.0325  -0.1075 -0.0335 45   THR   E C   
11829 O  O   . THR   E 45  ? 1.8647 1.5889 1.3958 0.0298  -0.0990 -0.0320 45   THR   E O   
11830 C  CB  . THR   E 45  ? 1.7947 1.5225 1.3303 0.0258  -0.1232 -0.0346 45   THR   E CB  
11831 O  OG1 . THR   E 45  ? 1.8462 1.5801 1.3863 0.0271  -0.1080 -0.0297 45   THR   E OG1 
11832 C  CG2 . THR   E 45  ? 1.7552 1.5037 1.3185 0.0171  -0.1314 -0.0359 45   THR   E CG2 
11833 N  N   . ALA   E 46  ? 1.8717 1.5651 1.3624 0.0406  -0.1039 -0.0323 46   ALA   E N   
11834 C  CA  . ALA   E 46  ? 1.8306 1.5170 1.3107 0.0462  -0.0882 -0.0286 46   ALA   E CA  
11835 C  C   . ALA   E 46  ? 1.8796 1.5836 1.3801 0.0430  -0.0760 -0.0239 46   ALA   E C   
11836 O  O   . ALA   E 46  ? 1.9309 1.6406 1.4385 0.0433  -0.0635 -0.0213 46   ALA   E O   
11837 C  CB  . ALA   E 46  ? 1.8234 1.4838 1.2698 0.0559  -0.0868 -0.0282 46   ALA   E CB  
11838 N  N   . GLU   E 47  ? 1.8348 1.5478 1.3456 0.0398  -0.0796 -0.0229 47   GLU   E N   
11839 C  CA  . GLU   E 47  ? 1.7997 1.5287 1.3294 0.0368  -0.0687 -0.0186 47   GLU   E CA  
11840 C  C   . GLU   E 47  ? 1.7828 1.5364 1.3443 0.0282  -0.0687 -0.0188 47   GLU   E C   
11841 O  O   . GLU   E 47  ? 1.7005 1.4666 1.2775 0.0263  -0.0573 -0.0156 47   GLU   E O   
11842 C  CB  . GLU   E 47  ? 1.7521 1.4801 1.2792 0.0372  -0.0723 -0.0173 47   GLU   E CB  
11843 N  N   . GLY   E 48  ? 1.7882 1.5486 1.3596 0.0231  -0.0812 -0.0225 48   GLY   E N   
11844 C  CA  . GLY   E 48  ? 1.7111 1.4932 1.3107 0.0154  -0.0818 -0.0229 48   GLY   E CA  
11845 C  C   . GLY   E 48  ? 1.6458 1.4314 1.2520 0.0107  -0.0962 -0.0271 48   GLY   E C   
11846 O  O   . GLY   E 48  ? 1.6582 1.4309 1.2501 0.0130  -0.1024 -0.0303 48   GLY   E O   
11847 N  N   . LEU   E 49  ? 1.6071 1.4096 1.2349 0.0042  -0.1016 -0.0273 49   LEU   E N   
11848 C  CA  . LEU   E 49  ? 1.6189 1.4265 1.2560 -0.0008 -0.1145 -0.0310 49   LEU   E CA  
11849 C  C   . LEU   E 49  ? 1.6271 1.4355 1.2653 -0.0020 -0.1243 -0.0318 49   LEU   E C   
11850 O  O   . LEU   E 49  ? 1.6222 1.4346 1.2627 -0.0012 -0.1199 -0.0291 49   LEU   E O   
11851 C  CB  . LEU   E 49  ? 1.5234 1.3513 1.1872 -0.0078 -0.1124 -0.0306 49   LEU   E CB  
11852 C  CG  . LEU   E 49  ? 1.4213 1.2482 1.0844 -0.0066 -0.1044 -0.0304 49   LEU   E CG  
11853 C  CD1 . LEU   E 49  ? 1.3335 1.1803 1.0212 -0.0116 -0.0975 -0.0284 49   LEU   E CD1 
11854 C  CD2 . LEU   E 49  ? 1.3993 1.2175 1.0551 -0.0071 -0.1133 -0.0343 49   LEU   E CD2 
11855 N  N   . ARG   E 50  ? 1.6548 1.4587 1.2907 -0.0036 -0.1376 -0.0358 50   ARG   E N   
11856 C  CA  . ARG   E 50  ? 1.6064 1.4119 1.2452 -0.0050 -0.1481 -0.0371 50   ARG   E CA  
11857 C  C   . ARG   E 50  ? 1.5792 1.4004 1.2416 -0.0128 -0.1564 -0.0392 50   ARG   E C   
11858 O  O   . ARG   E 50  ? 1.5745 1.3919 1.2364 -0.0145 -0.1630 -0.0424 50   ARG   E O   
11859 C  CB  . ARG   E 50  ? 1.6157 1.4000 1.2292 0.0008  -0.1576 -0.0401 50   ARG   E CB  
11860 N  N   . PRO   E 51  ? 1.5076 1.3459 1.1904 -0.0174 -0.1562 -0.0375 51   PRO   E N   
11861 C  CA  . PRO   E 51  ? 1.4481 1.3014 1.1537 -0.0246 -0.1633 -0.0391 51   PRO   E CA  
11862 C  C   . PRO   E 51  ? 1.4955 1.3419 1.1974 -0.0253 -0.1782 -0.0433 51   PRO   E C   
11863 O  O   . PRO   E 51  ? 1.5857 1.4253 1.2783 -0.0223 -0.1842 -0.0440 51   PRO   E O   
11864 C  CB  . PRO   E 51  ? 1.4508 1.3212 1.1749 -0.0279 -0.1591 -0.0360 51   PRO   E CB  
11865 C  CG  . PRO   E 51  ? 1.5118 1.3788 1.2266 -0.0235 -0.1466 -0.0324 51   PRO   E CG  
11866 C  CD  . PRO   E 51  ? 1.4836 1.3289 1.1706 -0.0164 -0.1469 -0.0334 51   PRO   E CD  
11867 N  N   . VAL   E 52  ? 1.4486 1.2967 1.1583 -0.0293 -0.1841 -0.0461 52   VAL   E N   
11868 C  CA  . VAL   E 52  ? 1.4469 1.2885 1.1547 -0.0304 -0.1985 -0.0505 52   VAL   E CA  
11869 C  C   . VAL   E 52  ? 1.4195 1.2789 1.1543 -0.0380 -0.2044 -0.0511 52   VAL   E C   
11870 O  O   . VAL   E 52  ? 1.4320 1.2938 1.1719 -0.0388 -0.2132 -0.0524 52   VAL   E O   
11871 C  CB  . VAL   E 52  ? 1.4465 1.2738 1.1407 -0.0288 -0.2019 -0.0536 52   VAL   E CB  
11872 C  CG1 . VAL   E 52  ? 1.4993 1.3178 1.1895 -0.0293 -0.2171 -0.0583 52   VAL   E CG1 
11873 C  CG2 . VAL   E 52  ? 1.4593 1.2699 1.1278 -0.0213 -0.1943 -0.0525 52   VAL   E CG2 
11874 N  N   . LYS   E 53  ? 1.3554 1.2267 1.1073 -0.0432 -0.2000 -0.0503 53   LYS   E N   
11875 C  CA  . LYS   E 53  ? 1.3467 1.2358 1.1246 -0.0501 -0.2030 -0.0499 53   LYS   E CA  
11876 C  C   . LYS   E 53  ? 1.3661 1.2681 1.1590 -0.0539 -0.1931 -0.0474 53   LYS   E C   
11877 O  O   . LYS   E 53  ? 1.3682 1.2640 1.1523 -0.0522 -0.1870 -0.0472 53   LYS   E O   
11878 C  CB  . LYS   E 53  ? 1.2632 1.1503 1.0479 -0.0537 -0.2161 -0.0541 53   LYS   E CB  
11879 N  N   . GLU   E 54  ? 1.2816 1.2009 1.0964 -0.0587 -0.1916 -0.0455 54   GLU   E N   
11880 C  CA  . GLU   E 54  ? 1.2649 1.1972 1.0955 -0.0626 -0.1833 -0.0432 54   GLU   E CA  
11881 C  C   . GLU   E 54  ? 1.2418 1.1859 1.0939 -0.0690 -0.1891 -0.0441 54   GLU   E C   
11882 O  O   . GLU   E 54  ? 1.2580 1.2089 1.1198 -0.0706 -0.1943 -0.0441 54   GLU   E O   
11883 C  CB  . GLU   E 54  ? 1.2297 1.1718 1.0651 -0.0614 -0.1729 -0.0393 54   GLU   E CB  
11884 C  CG  . GLU   E 54  ? 1.2266 1.1796 1.0742 -0.0638 -0.1634 -0.0370 54   GLU   E CG  
11885 C  CD  . GLU   E 54  ? 1.2261 1.1967 1.0964 -0.0687 -0.1627 -0.0352 54   GLU   E CD  
11886 O  OE1 . GLU   E 54  ? 1.1911 1.1654 1.0703 -0.0715 -0.1708 -0.0364 54   GLU   E OE1 
11887 O  OE2 . GLU   E 54  ? 1.1801 1.1603 1.0594 -0.0696 -0.1542 -0.0327 54   GLU   E OE2 
11888 N  N   . VAL   E 55  ? 1.2263 1.1721 1.0854 -0.0724 -0.1883 -0.0449 55   VAL   E N   
11889 C  CA  . VAL   E 55  ? 1.2043 1.1587 1.0822 -0.0783 -0.1941 -0.0459 55   VAL   E CA  
11890 C  C   . VAL   E 55  ? 1.1920 1.1592 1.0853 -0.0817 -0.1855 -0.0433 55   VAL   E C   
11891 O  O   . VAL   E 55  ? 1.1928 1.1600 1.0807 -0.0796 -0.1766 -0.0414 55   VAL   E O   
11892 C  CB  . VAL   E 55  ? 1.2204 1.1631 1.0923 -0.0794 -0.2028 -0.0499 55   VAL   E CB  
11893 C  CG1 . VAL   E 55  ? 1.1939 1.1297 1.0571 -0.0785 -0.1969 -0.0500 55   VAL   E CG1 
11894 C  CG2 . VAL   E 55  ? 1.2489 1.2002 1.1408 -0.0855 -0.2093 -0.0510 55   VAL   E CG2 
11895 N  N   . GLY   E 56  ? 1.2041 1.1820 1.1167 -0.0870 -0.1884 -0.0431 56   GLY   E N   
11896 C  CA  . GLY   E 56  ? 1.1516 1.1404 1.0788 -0.0904 -0.1814 -0.0408 56   GLY   E CA  
11897 C  C   . GLY   E 56  ? 1.2004 1.1876 1.1356 -0.0948 -0.1857 -0.0427 56   GLY   E C   
11898 O  O   . GLY   E 56  ? 1.2063 1.1893 1.1437 -0.0968 -0.1950 -0.0454 56   GLY   E O   
11899 N  N   . MET   E 57  ? 1.1688 1.1590 1.1086 -0.0963 -0.1789 -0.0414 57   MET   E N   
11900 C  CA  . MET   E 57  ? 1.1648 1.1532 1.1119 -0.1005 -0.1813 -0.0426 57   MET   E CA  
11901 C  C   . MET   E 57  ? 1.1410 1.1427 1.1065 -0.1043 -0.1755 -0.0399 57   MET   E C   
11902 O  O   . MET   E 57  ? 1.1955 1.2050 1.1635 -0.1026 -0.1678 -0.0371 57   MET   E O   
11903 C  CB  . MET   E 57  ? 1.1640 1.1411 1.0969 -0.0984 -0.1784 -0.0438 57   MET   E CB  
11904 C  CG  . MET   E 57  ? 1.2361 1.1985 1.1487 -0.0941 -0.1828 -0.0464 57   MET   E CG  
11905 S  SD  . MET   E 57  ? 1.3648 1.3142 1.2708 -0.0958 -0.1871 -0.0496 57   MET   E SD  
11906 C  CE  . MET   E 57  ? 1.3005 1.2581 1.2291 -0.1031 -0.1941 -0.0503 57   MET   E CE  
11907 N  N   . TYR   E 58  ? 1.1343 1.1378 1.1124 -0.1091 -0.1791 -0.0406 58   TYR   E N   
11908 C  CA  . TYR   E 58  ? 1.0640 1.0776 1.0576 -0.1125 -0.1731 -0.0380 58   TYR   E CA  
11909 C  C   . TYR   E 58  ? 1.0734 1.0810 1.0604 -0.1120 -0.1676 -0.0378 58   TYR   E C   
11910 O  O   . TYR   E 58  ? 1.1001 1.1051 1.0932 -0.1156 -0.1685 -0.0384 58   TYR   E O   
11911 C  CB  . TYR   E 58  ? 1.0942 1.1129 1.1055 -0.1179 -0.1785 -0.0385 58   TYR   E CB  
11912 C  CG  . TYR   E 58  ? 1.1232 1.1508 1.1449 -0.1187 -0.1827 -0.0380 58   TYR   E CG  
11913 C  CD1 . TYR   E 58  ? 1.0697 1.1041 1.0895 -0.1154 -0.1787 -0.0359 58   TYR   E CD1 
11914 C  CD2 . TYR   E 58  ? 1.1621 1.1912 1.1960 -0.1226 -0.1908 -0.0397 58   TYR   E CD2 
11915 C  CE1 . TYR   E 58  ? 1.0495 1.0916 1.0784 -0.1159 -0.1826 -0.0355 58   TYR   E CE1 
11916 C  CE2 . TYR   E 58  ? 1.1816 1.2189 1.2254 -0.1230 -0.1948 -0.0394 58   TYR   E CE2 
11917 C  CZ  . TYR   E 58  ? 1.1091 1.1528 1.1498 -0.1195 -0.1907 -0.0372 58   TYR   E CZ  
11918 O  OH  . TYR   E 58  ? 1.1526 1.2041 1.2026 -0.1197 -0.1947 -0.0369 58   TYR   E OH  
11919 N  N   . GLY   E 59  ? 1.0186 1.0233 0.9928 -0.1074 -0.1618 -0.0371 59   GLY   E N   
11920 C  CA  . GLY   E 59  ? 1.0474 1.0467 1.0148 -0.1062 -0.1564 -0.0370 59   GLY   E CA  
11921 C  C   . GLY   E 59  ? 1.0612 1.0555 1.0128 -0.1007 -0.1516 -0.0369 59   GLY   E C   
11922 O  O   . GLY   E 59  ? 1.0852 1.0754 1.0268 -0.0976 -0.1541 -0.0378 59   GLY   E O   
11923 N  N   . LYS   E 60  ? 1.0942 1.0883 1.0434 -0.0991 -0.1447 -0.0358 60   LYS   E N   
11924 C  CA  . LYS   E 60  ? 1.0854 1.0755 1.0214 -0.0939 -0.1394 -0.0357 60   LYS   E CA  
11925 C  C   . LYS   E 60  ? 1.0791 1.0543 0.9990 -0.0919 -0.1429 -0.0385 60   LYS   E C   
11926 O  O   . LYS   E 60  ? 1.0598 1.0286 0.9782 -0.0935 -0.1439 -0.0397 60   LYS   E O   
11927 C  CB  . LYS   E 60  ? 1.0347 1.0305 0.9751 -0.0928 -0.1314 -0.0337 60   LYS   E CB  
11928 C  CG  . LYS   E 60  ? 0.9654 0.9751 0.9202 -0.0941 -0.1281 -0.0310 60   LYS   E CG  
11929 C  CD  . LYS   E 60  ? 0.8930 0.9081 0.8529 -0.0932 -0.1212 -0.0293 60   LYS   E CD  
11930 C  CE  . LYS   E 60  ? 0.9160 0.9278 0.8655 -0.0884 -0.1161 -0.0295 60   LYS   E CE  
11931 N  NZ  . LYS   E 60  ? 0.9784 0.9977 0.9295 -0.0857 -0.1127 -0.0281 60   LYS   E NZ  
11932 N  N   . ILE   E 61  ? 1.0507 1.0197 0.9583 -0.0884 -0.1448 -0.0396 61   ILE   E N   
11933 C  CA  . ILE   E 61  ? 1.0640 1.0181 0.9544 -0.0857 -0.1477 -0.0422 61   ILE   E CA  
11934 C  C   . ILE   E 61  ? 1.1112 1.0611 0.9946 -0.0829 -0.1411 -0.0419 61   ILE   E C   
11935 O  O   . ILE   E 61  ? 1.1734 1.1251 1.0516 -0.0788 -0.1346 -0.0406 61   ILE   E O   
11936 C  CB  . ILE   E 61  ? 1.1195 1.0683 0.9973 -0.0815 -0.1491 -0.0427 61   ILE   E CB  
11937 C  CG1 . ILE   E 61  ? 1.0973 1.0504 0.9826 -0.0842 -0.1563 -0.0430 61   ILE   E CG1 
11938 C  CG2 . ILE   E 61  ? 1.1146 1.0470 0.9728 -0.0778 -0.1512 -0.0452 61   ILE   E CG2 
11939 C  CD1 . ILE   E 61  ? 1.0756 1.0233 0.9489 -0.0802 -0.1584 -0.0435 61   ILE   E CD1 
11940 N  N   . ALA   E 62  ? 1.1492 1.0933 1.0326 -0.0851 -0.1428 -0.0432 62   ALA   E N   
11941 C  CA  . ALA   E 62  ? 1.1632 1.1029 1.0399 -0.0823 -0.1369 -0.0431 62   ALA   E CA  
11942 C  C   . ALA   E 62  ? 1.1849 1.1088 1.0425 -0.0786 -0.1389 -0.0457 62   ALA   E C   
11943 O  O   . ALA   E 62  ? 1.1869 1.1070 1.0358 -0.0744 -0.1331 -0.0455 62   ALA   E O   
11944 C  CB  . ALA   E 62  ? 1.1157 1.0578 1.0027 -0.0863 -0.1364 -0.0427 62   ALA   E CB  
11945 N  N   . VAL   E 63  ? 1.1264 1.0409 0.9775 -0.0798 -0.1472 -0.0482 63   VAL   E N   
11946 C  CA  . VAL   E 63  ? 1.1746 1.0732 1.0061 -0.0758 -0.1499 -0.0507 63   VAL   E CA  
11947 C  C   . VAL   E 63  ? 1.2040 1.0977 1.0289 -0.0750 -0.1569 -0.0522 63   VAL   E C   
11948 O  O   . VAL   E 63  ? 1.2325 1.1317 1.0686 -0.0793 -0.1630 -0.0525 63   VAL   E O   
11949 C  CB  . VAL   E 63  ? 1.2089 1.0969 1.0367 -0.0780 -0.1541 -0.0531 63   VAL   E CB  
11950 C  CG1 . VAL   E 63  ? 1.1809 1.0512 0.9878 -0.0740 -0.1584 -0.0561 63   VAL   E CG1 
11951 C  CG2 . VAL   E 63  ? 1.1602 1.0513 0.9917 -0.0776 -0.1467 -0.0517 63   VAL   E CG2 
11952 N  N   . MET   E 64  ? 1.1454 1.0285 0.9520 -0.0694 -0.1560 -0.0530 64   MET   E N   
11953 C  CA  . MET   E 64  ? 1.1419 1.0186 0.9395 -0.0676 -0.1623 -0.0544 64   MET   E CA  
11954 C  C   . MET   E 64  ? 1.2356 1.0941 1.0096 -0.0619 -0.1635 -0.0567 64   MET   E C   
11955 O  O   . MET   E 64  ? 1.2188 1.0745 0.9824 -0.0567 -0.1557 -0.0553 64   MET   E O   
11956 C  CB  . MET   E 64  ? 1.1862 1.0734 0.9884 -0.0659 -0.1576 -0.0517 64   MET   E CB  
11957 C  CG  . MET   E 64  ? 1.2149 1.0961 1.0081 -0.0638 -0.1638 -0.0528 64   MET   E CG  
11958 S  SD  . MET   E 64  ? 1.2571 1.1451 1.0480 -0.0596 -0.1560 -0.0495 64   MET   E SD  
11959 C  CE  . MET   E 64  ? 1.1510 1.0318 0.9270 -0.0532 -0.1452 -0.0483 64   MET   E CE  
11960 N  N   . GLU   E 65  ? 1.2470 1.0930 1.0127 -0.0627 -0.1734 -0.0601 65   GLU   E N   
11961 C  CA  . GLU   E 65  ? 1.2704 1.0977 1.0130 -0.0573 -0.1752 -0.0626 65   GLU   E CA  
11962 C  C   . GLU   E 65  ? 1.3036 1.1192 1.0353 -0.0564 -0.1862 -0.0657 65   GLU   E C   
11963 O  O   . GLU   E 65  ? 1.2884 1.1083 1.0319 -0.0613 -0.1948 -0.0671 65   GLU   E O   
11964 C  CB  . GLU   E 65  ? 1.2706 1.0904 1.0105 -0.0585 -0.1756 -0.0643 65   GLU   E CB  
11965 C  CG  . GLU   E 65  ? 1.3179 1.1426 1.0584 -0.0561 -0.1642 -0.0618 65   GLU   E CG  
11966 C  CD  . GLU   E 65  ? 1.4314 1.2517 1.1569 -0.0488 -0.1566 -0.0604 65   GLU   E CD  
11967 O  OE1 . GLU   E 65  ? 1.4698 1.2753 1.1763 -0.0444 -0.1604 -0.0623 65   GLU   E OE1 
11968 O  OE2 . GLU   E 65  ? 1.4479 1.2790 1.1805 -0.0474 -0.1469 -0.0573 65   GLU   E OE2 
11969 N  N   . LEU   E 66  ? 1.3531 1.1534 1.0618 -0.0496 -0.1859 -0.0669 66   LEU   E N   
11970 C  CA  . LEU   E 66  ? 1.4580 1.2431 1.1514 -0.0473 -0.1965 -0.0704 66   LEU   E CA  
11971 C  C   . LEU   E 66  ? 1.4237 1.1911 1.1023 -0.0459 -0.2022 -0.0741 66   LEU   E C   
11972 O  O   . LEU   E 66  ? 1.4174 1.1822 1.0932 -0.0452 -0.1964 -0.0737 66   LEU   E O   
11973 C  CB  . LEU   E 66  ? 1.4372 1.2154 1.1131 -0.0402 -0.1929 -0.0692 66   LEU   E CB  
11974 C  CG  . LEU   E 66  ? 1.3624 1.1542 1.0498 -0.0413 -0.1912 -0.0665 66   LEU   E CG  
11975 C  CD1 . LEU   E 66  ? 1.3840 1.1648 1.0509 -0.0340 -0.1895 -0.0660 66   LEU   E CD1 
11976 C  CD2 . LEU   E 66  ? 1.3450 1.1446 1.0493 -0.0477 -0.2019 -0.0682 66   LEU   E CD2 
11977 N  N   . PHE   E 67  ? 1.4550 1.2096 1.1238 -0.0454 -0.2143 -0.0780 67   PHE   E N   
11978 C  CA  . PHE   E 67  ? 1.5183 1.2547 1.1723 -0.0441 -0.2217 -0.0821 67   PHE   E CA  
11979 C  C   . PHE   E 67  ? 1.5440 1.2696 1.1912 -0.0441 -0.2360 -0.0863 67   PHE   E C   
11980 O  O   . PHE   E 67  ? 1.5367 1.2727 1.1989 -0.0481 -0.2416 -0.0862 67   PHE   E O   
11981 C  CB  . PHE   E 67  ? 1.5061 1.2480 1.1754 -0.0504 -0.2217 -0.0826 67   PHE   E CB  
11982 C  CG  . PHE   E 67  ? 1.4764 1.2303 1.1697 -0.0587 -0.2293 -0.0834 67   PHE   E CG  
11983 C  CD1 . PHE   E 67  ? 1.4467 1.2210 1.1621 -0.0630 -0.2241 -0.0798 67   PHE   E CD1 
11984 C  CD2 . PHE   E 67  ? 1.5227 1.2673 1.2168 -0.0622 -0.2416 -0.0877 67   PHE   E CD2 
11985 C  CE1 . PHE   E 67  ? 1.4241 1.2093 1.1616 -0.0705 -0.2306 -0.0804 67   PHE   E CE1 
11986 C  CE2 . PHE   E 67  ? 1.4946 1.2505 1.2120 -0.0699 -0.2482 -0.0883 67   PHE   E CE2 
11987 C  CZ  . PHE   E 67  ? 1.4255 1.2016 1.1643 -0.0739 -0.2424 -0.0846 67   PHE   E CZ  
11988 N  N   . ARG   E 68  ? 1.6221 1.3264 1.2460 -0.0392 -0.2422 -0.0899 68   ARG   E N   
11989 C  CA  . ARG   E 68  ? 1.7393 1.4307 1.3547 -0.0388 -0.2572 -0.0946 68   ARG   E CA  
11990 C  C   . ARG   E 68  ? 1.7311 1.4112 1.3449 -0.0417 -0.2655 -0.0988 68   ARG   E C   
11991 O  O   . ARG   E 68  ? 1.7428 1.4056 1.3349 -0.0365 -0.2645 -0.1005 68   ARG   E O   
11992 C  CB  . ARG   E 68  ? 1.7108 1.3843 1.2972 -0.0294 -0.2584 -0.0957 68   ARG   E CB  
11993 N  N   . PRO   E 69  ? 1.7262 1.4151 1.3621 -0.0499 -0.2733 -0.1005 69   PRO   E N   
11994 C  CA  . PRO   E 69  ? 1.8069 1.4840 1.4412 -0.0530 -0.2818 -0.1047 69   PRO   E CA  
11995 C  C   . PRO   E 69  ? 1.9247 1.5790 1.5348 -0.0474 -0.2941 -0.1098 69   PRO   E C   
11996 O  O   . PRO   E 69  ? 1.9775 1.6289 1.5808 -0.0442 -0.2999 -0.1108 69   PRO   E O   
11997 C  CB  . PRO   E 69  ? 1.7359 1.4285 1.4006 -0.0628 -0.2880 -0.1051 69   PRO   E CB  
11998 C  CG  . PRO   E 69  ? 1.6965 1.4099 1.3785 -0.0647 -0.2802 -0.1006 69   PRO   E CG  
11999 C  CD  . PRO   E 69  ? 1.7452 1.4530 1.4071 -0.0565 -0.2763 -0.0992 69   PRO   E CD  
12000 N  N   . LYS   E 70  ? 2.0042 1.6415 1.6000 -0.0459 -0.2978 -0.1131 70   LYS   E N   
12001 C  CA  . LYS   E 70  ? 2.0515 1.6654 1.6230 -0.0404 -0.3100 -0.1183 70   LYS   E CA  
12002 C  C   . LYS   E 70  ? 2.0451 1.6609 1.6287 -0.0446 -0.3253 -0.1220 70   LYS   E C   
12003 O  O   . LYS   E 70  ? 2.0119 1.6309 1.6134 -0.0520 -0.3338 -0.1248 70   LYS   E O   
12004 C  CB  . LYS   E 70  ? 2.0462 1.6432 1.6054 -0.0399 -0.3131 -0.1216 70   LYS   E CB  
12005 N  N   . GLY   E 71  ? 2.0065 1.6209 1.5815 -0.0400 -0.3285 -0.1221 71   GLY   E N   
12006 C  CA  . GLY   E 71  ? 1.9454 1.5619 1.5316 -0.0432 -0.3430 -0.1256 71   GLY   E CA  
12007 C  C   . GLY   E 71  ? 1.9524 1.5875 1.5538 -0.0445 -0.3393 -0.1220 71   GLY   E C   
12008 O  O   . GLY   E 71  ? 1.9403 1.5844 1.5607 -0.0496 -0.3491 -0.1239 71   GLY   E O   
12009 N  N   . GLU   E 72  ? 1.9005 1.5414 1.4945 -0.0400 -0.3253 -0.1170 72   GLU   E N   
12010 C  CA  . GLU   E 72  ? 1.8752 1.5312 1.4791 -0.0398 -0.3211 -0.1135 72   GLU   E CA  
12011 C  C   . GLU   E 72  ? 1.8860 1.5289 1.4611 -0.0296 -0.3163 -0.1122 72   GLU   E C   
12012 O  O   . GLU   E 72  ? 1.9251 1.5548 1.4785 -0.0236 -0.3091 -0.1115 72   GLU   E O   
12013 C  CB  . GLU   E 72  ? 1.8878 1.5674 1.5154 -0.0452 -0.3070 -0.1078 72   GLU   E CB  
12014 C  CG  . GLU   E 72  ? 1.8954 1.5857 1.5468 -0.0541 -0.3068 -0.1079 72   GLU   E CG  
12015 C  CD  . GLU   E 72  ? 1.9480 1.6450 1.6213 -0.0613 -0.3201 -0.1112 72   GLU   E CD  
12016 O  OE1 . GLU   E 72  ? 1.8953 1.6102 1.5899 -0.0655 -0.3195 -0.1090 72   GLU   E OE1 
12017 O  OE2 . GLU   E 72  ? 2.0082 1.6922 1.6775 -0.0628 -0.3312 -0.1160 72   GLU   E OE2 
12018 N  N   . SER   E 73  ? 1.7510 1.3973 1.3261 -0.0275 -0.3201 -0.1119 73   SER   E N   
12019 C  CA  . SER   E 73  ? 1.7359 1.3721 1.2861 -0.0182 -0.3138 -0.1097 73   SER   E CA  
12020 C  C   . SER   E 73  ? 1.7870 1.4396 1.3456 -0.0183 -0.2962 -0.1032 73   SER   E C   
12021 O  O   . SER   E 73  ? 1.7919 1.4362 1.3312 -0.0117 -0.2854 -0.1006 73   SER   E O   
12022 C  CB  . SER   E 73  ? 1.6969 1.3285 1.2418 -0.0153 -0.3251 -0.1120 73   SER   E CB  
12023 O  OG  . SER   E 73  ? 1.7000 1.3538 1.2738 -0.0221 -0.3264 -0.1103 73   SER   E OG  
12024 N  N   . LYS   E 74  ? 1.7871 1.4627 1.3747 -0.0256 -0.2933 -0.1005 74   LYS   E N   
12025 C  CA  . LYS   E 74  ? 1.6512 1.3434 1.2493 -0.0263 -0.2778 -0.0946 74   LYS   E CA  
12026 C  C   . LYS   E 74  ? 1.6604 1.3642 1.2756 -0.0323 -0.2700 -0.0928 74   LYS   E C   
12027 O  O   . LYS   E 74  ? 1.6775 1.3823 1.3046 -0.0380 -0.2773 -0.0956 74   LYS   E O   
12028 C  CB  . LYS   E 74  ? 1.5947 1.3046 1.2125 -0.0299 -0.2787 -0.0925 74   LYS   E CB  
12029 C  CG  . LYS   E 74  ? 1.6254 1.3252 1.2281 -0.0244 -0.2866 -0.0941 74   LYS   E CG  
12030 C  CD  . LYS   E 74  ? 1.6558 1.3739 1.2826 -0.0297 -0.2908 -0.0932 74   LYS   E CD  
12031 C  CE  . LYS   E 74  ? 1.6552 1.3881 1.3110 -0.0393 -0.2958 -0.0945 74   LYS   E CE  
12032 N  NZ  . LYS   E 74  ? 1.5933 1.3382 1.2694 -0.0438 -0.3052 -0.0956 74   LYS   E NZ  
12033 N  N   . ASP   E 75  ? 1.6574 1.3695 1.2736 -0.0307 -0.2551 -0.0881 75   ASP   E N   
12034 C  CA  . ASP   E 75  ? 1.5942 1.3205 1.2292 -0.0363 -0.2468 -0.0857 75   ASP   E CA  
12035 C  C   . ASP   E 75  ? 1.5466 1.2930 1.2121 -0.0450 -0.2501 -0.0849 75   ASP   E C   
12036 O  O   . ASP   E 75  ? 1.5319 1.2862 1.2060 -0.0462 -0.2544 -0.0845 75   ASP   E O   
12037 C  CB  . ASP   E 75  ? 1.5129 1.2459 1.1450 -0.0328 -0.2308 -0.0807 75   ASP   E CB  
12038 C  CG  . ASP   E 75  ? 1.5708 1.2854 1.1757 -0.0249 -0.2252 -0.0810 75   ASP   E CG  
12039 O  OD1 . ASP   E 75  ? 1.6337 1.3326 1.2256 -0.0235 -0.2320 -0.0848 75   ASP   E OD1 
12040 O  OD2 . ASP   E 75  ? 1.5598 1.2761 1.1573 -0.0201 -0.2138 -0.0775 75   ASP   E OD2 
12041 N  N   . LEU   E 76  ? 1.5050 1.2598 1.1866 -0.0509 -0.2477 -0.0845 76   LEU   E N   
12042 C  CA  . LEU   E 76  ? 1.4641 1.2387 1.1751 -0.0591 -0.2480 -0.0830 76   LEU   E CA  
12043 C  C   . LEU   E 76  ? 1.4408 1.2303 1.1636 -0.0607 -0.2339 -0.0783 76   LEU   E C   
12044 O  O   . LEU   E 76  ? 1.4499 1.2337 1.1610 -0.0570 -0.2256 -0.0771 76   LEU   E O   
12045 C  CB  . LEU   E 76  ? 1.4995 1.2715 1.2213 -0.0652 -0.2574 -0.0866 76   LEU   E CB  
12046 C  CG  . LEU   E 76  ? 1.5346 1.2951 1.2498 -0.0645 -0.2725 -0.0913 76   LEU   E CG  
12047 C  CD1 . LEU   E 76  ? 1.5976 1.3656 1.3359 -0.0729 -0.2810 -0.0934 76   LEU   E CD1 
12048 C  CD2 . LEU   E 76  ? 1.5359 1.3003 1.2483 -0.0612 -0.2741 -0.0902 76   LEU   E CD2 
12049 N  N   . LEU   E 77  ? 1.4304 1.2388 1.1767 -0.0660 -0.2317 -0.0758 77   LEU   E N   
12050 C  CA  . LEU   E 77  ? 1.3712 1.1949 1.1301 -0.0676 -0.2192 -0.0713 77   LEU   E CA  
12051 C  C   . LEU   E 77  ? 1.3361 1.1689 1.1146 -0.0745 -0.2188 -0.0711 77   LEU   E C   
12052 O  O   . LEU   E 77  ? 1.3286 1.1673 1.1233 -0.0801 -0.2264 -0.0724 77   LEU   E O   
12053 C  CB  . LEU   E 77  ? 1.3314 1.1698 1.1018 -0.0680 -0.2159 -0.0683 77   LEU   E CB  
12054 C  CG  . LEU   E 77  ? 1.2029 1.0552 0.9828 -0.0683 -0.2029 -0.0639 77   LEU   E CG  
12055 C  CD1 . LEU   E 77  ? 1.2866 1.1292 1.0483 -0.0625 -0.1947 -0.0632 77   LEU   E CD1 
12056 C  CD2 . LEU   E 77  ? 1.1785 1.0413 0.9643 -0.0673 -0.2001 -0.0613 77   LEU   E CD2 
12057 N  N   . PHE   E 78  ? 1.3173 1.1510 1.0947 -0.0739 -0.2098 -0.0694 78   PHE   E N   
12058 C  CA  . PHE   E 78  ? 1.3079 1.1515 1.1039 -0.0800 -0.2070 -0.0682 78   PHE   E CA  
12059 C  C   . PHE   E 78  ? 1.2461 1.1067 1.0554 -0.0807 -0.1961 -0.0638 78   PHE   E C   
12060 O  O   . PHE   E 78  ? 1.1978 1.0589 0.9980 -0.0758 -0.1877 -0.0617 78   PHE   E O   
12061 C  CB  . PHE   E 78  ? 1.2622 1.0948 1.0494 -0.0795 -0.2056 -0.0697 78   PHE   E CB  
12062 C  CG  . PHE   E 78  ? 1.1987 1.0410 1.0044 -0.0854 -0.2022 -0.0682 78   PHE   E CG  
12063 C  CD1 . PHE   E 78  ? 1.2170 1.0612 1.0374 -0.0919 -0.2098 -0.0699 78   PHE   E CD1 
12064 C  CD2 . PHE   E 78  ? 1.1606 1.0103 0.9695 -0.0843 -0.1913 -0.0651 78   PHE   E CD2 
12065 C  CE1 . PHE   E 78  ? 1.1958 1.0482 1.0325 -0.0971 -0.2061 -0.0683 78   PHE   E CE1 
12066 C  CE2 . PHE   E 78  ? 1.1781 1.0356 1.0027 -0.0893 -0.1882 -0.0637 78   PHE   E CE2 
12067 C  CZ  . PHE   E 78  ? 1.1402 0.9988 0.9783 -0.0956 -0.1952 -0.0651 78   PHE   E CZ  
12068 N  N   . ILE   E 79  ? 1.1834 1.0575 1.0144 -0.0867 -0.1963 -0.0624 79   ILE   E N   
12069 C  CA  . ILE   E 79  ? 1.1731 1.0632 1.0180 -0.0878 -0.1871 -0.0584 79   ILE   E CA  
12070 C  C   . ILE   E 79  ? 1.2065 1.1029 1.0672 -0.0934 -0.1854 -0.0576 79   ILE   E C   
12071 O  O   . ILE   E 79  ? 1.1557 1.0517 1.0264 -0.0984 -0.1926 -0.0593 79   ILE   E O   
12072 C  CB  . ILE   E 79  ? 1.1991 1.1010 1.0548 -0.0889 -0.1886 -0.0568 79   ILE   E CB  
12073 C  CG1 . ILE   E 79  ? 1.1951 1.0950 1.0369 -0.0827 -0.1843 -0.0557 79   ILE   E CG1 
12074 C  CG2 . ILE   E 79  ? 1.1663 1.0853 1.0433 -0.0932 -0.1830 -0.0536 79   ILE   E CG2 
12075 C  CD1 . ILE   E 79  ? 1.2424 1.1482 1.0889 -0.0828 -0.1884 -0.0552 79   ILE   E CD1 
12076 N  N   . LEU   E 80  ? 1.2002 1.1017 1.0627 -0.0922 -0.1760 -0.0551 80   LEU   E N   
12077 C  CA  . LEU   E 80  ? 1.1363 1.0466 1.0149 -0.0968 -0.1722 -0.0533 80   LEU   E CA  
12078 C  C   . LEU   E 80  ? 1.1761 1.1016 1.0653 -0.0962 -0.1643 -0.0496 80   LEU   E C   
12079 O  O   . LEU   E 80  ? 1.1578 1.0843 1.0385 -0.0914 -0.1583 -0.0484 80   LEU   E O   
12080 C  CB  . LEU   E 80  ? 1.1384 1.0400 1.0088 -0.0956 -0.1684 -0.0538 80   LEU   E CB  
12081 C  CG  . LEU   E 80  ? 1.1457 1.0550 1.0317 -0.1001 -0.1646 -0.0519 80   LEU   E CG  
12082 C  CD1 . LEU   E 80  ? 1.1444 1.0556 1.0447 -0.1066 -0.1718 -0.0529 80   LEU   E CD1 
12083 C  CD2 . LEU   E 80  ? 1.1939 1.0935 1.0701 -0.0983 -0.1611 -0.0526 80   LEU   E CD2 
12084 N  N   . THR   E 81  ? 1.1936 1.1307 1.1014 -0.1010 -0.1644 -0.0479 81   THR   E N   
12085 C  CA  . THR   E 81  ? 1.1351 1.0867 1.0541 -0.1009 -0.1574 -0.0445 81   THR   E CA  
12086 C  C   . THR   E 81  ? 1.1110 1.0663 1.0365 -0.1020 -0.1506 -0.0426 81   THR   E C   
12087 O  O   . THR   E 81  ? 1.0941 1.0440 1.0221 -0.1051 -0.1523 -0.0435 81   THR   E O   
12088 C  CB  . THR   E 81  ? 1.1082 1.0706 1.0434 -0.1048 -0.1611 -0.0435 81   THR   E CB  
12089 O  OG1 . THR   E 81  ? 1.1495 1.1128 1.0974 -0.1104 -0.1645 -0.0439 81   THR   E OG1 
12090 C  CG2 . THR   E 81  ? 1.1000 1.0588 1.0291 -0.1035 -0.1684 -0.0454 81   THR   E CG2 
12091 N  N   . ALA   E 82  ? 1.1277 1.0921 1.0563 -0.0995 -0.1431 -0.0400 82   ALA   E N   
12092 C  CA  . ALA   E 82  ? 1.0683 1.0369 1.0026 -0.0998 -0.1363 -0.0381 82   ALA   E CA  
12093 C  C   . ALA   E 82  ? 1.0810 1.0521 1.0288 -0.1053 -0.1377 -0.0373 82   ALA   E C   
12094 O  O   . ALA   E 82  ? 1.1030 1.0716 1.0514 -0.1057 -0.1339 -0.0367 82   ALA   E O   
12095 C  CB  . ALA   E 82  ? 1.0960 1.0764 1.0359 -0.0973 -0.1298 -0.0354 82   ALA   E CB  
12096 N  N   . LYS   E 83  ? 1.1208 1.0972 1.0801 -0.1093 -0.1426 -0.0373 83   LYS   E N   
12097 C  CA  . LYS   E 83  ? 1.0866 1.0653 1.0597 -0.1147 -0.1436 -0.0365 83   LYS   E CA  
12098 C  C   . LYS   E 83  ? 1.1572 1.1241 1.1266 -0.1176 -0.1498 -0.0393 83   LYS   E C   
12099 O  O   . LYS   E 83  ? 1.1722 1.1403 1.1540 -0.1226 -0.1519 -0.0390 83   LYS   E O   
12100 C  CB  . LYS   E 83  ? 1.0721 1.0623 1.0611 -0.1179 -0.1458 -0.0351 83   LYS   E CB  
12101 C  CG  . LYS   E 83  ? 1.0931 1.0954 1.0902 -0.1166 -0.1385 -0.0317 83   LYS   E CG  
12102 C  CD  . LYS   E 83  ? 1.0848 1.0977 1.0990 -0.1203 -0.1402 -0.0301 83   LYS   E CD  
12103 C  CE  . LYS   E 83  ? 1.0820 1.1060 1.1030 -0.1186 -0.1331 -0.0268 83   LYS   E CE  
12104 N  NZ  . LYS   E 83  ? 1.1157 1.1488 1.1543 -0.1226 -0.1327 -0.0247 83   LYS   E NZ  
12105 N  N   . TYR   E 84  ? 1.1904 1.1459 1.1431 -0.1143 -0.1526 -0.0419 84   TYR   E N   
12106 C  CA  . TYR   E 84  ? 1.2313 1.1732 1.1764 -0.1159 -0.1585 -0.0450 84   TYR   E CA  
12107 C  C   . TYR   E 84  ? 1.2233 1.1630 1.1723 -0.1189 -0.1684 -0.0475 84   TYR   E C   
12108 O  O   . TYR   E 84  ? 1.2077 1.1380 1.1559 -0.1219 -0.1746 -0.0501 84   TYR   E O   
12109 C  CB  . TYR   E 84  ? 1.2190 1.1576 1.1700 -0.1193 -0.1557 -0.0443 84   TYR   E CB  
12110 C  CG  . TYR   E 84  ? 1.1850 1.1227 1.1279 -0.1150 -0.1471 -0.0426 84   TYR   E CG  
12111 C  CD1 . TYR   E 84  ? 1.1781 1.1077 1.1035 -0.1096 -0.1460 -0.0440 84   TYR   E CD1 
12112 C  CD2 . TYR   E 84  ? 1.2054 1.1505 1.1580 -0.1160 -0.1401 -0.0395 84   TYR   E CD2 
12113 C  CE1 . TYR   E 84  ? 1.1824 1.1116 1.1011 -0.1055 -0.1385 -0.0427 84   TYR   E CE1 
12114 C  CE2 . TYR   E 84  ? 1.1816 1.1256 1.1263 -0.1117 -0.1329 -0.0382 84   TYR   E CE2 
12115 C  CZ  . TYR   E 84  ? 1.1552 1.0917 1.0836 -0.1065 -0.1323 -0.0400 84   TYR   E CZ  
12116 O  OH  . TYR   E 84  ? 1.1471 1.0828 1.0683 -0.1019 -0.1256 -0.0390 84   TYR   E OH  
12117 N  N   . ASN   E 85  ? 1.1854 1.1331 1.1382 -0.1180 -0.1705 -0.0470 85   ASN   E N   
12118 C  CA  . ASN   E 85  ? 1.2079 1.1527 1.1622 -0.1198 -0.1804 -0.0497 85   ASN   E CA  
12119 C  C   . ASN   E 85  ? 1.1885 1.1193 1.1218 -0.1153 -0.1851 -0.0529 85   ASN   E C   
12120 O  O   . ASN   E 85  ? 1.1787 1.1084 1.0992 -0.1099 -0.1810 -0.0523 85   ASN   E O   
12121 C  CB  . ASN   E 85  ? 1.1550 1.1125 1.1192 -0.1198 -0.1809 -0.0481 85   ASN   E CB  
12122 C  CG  . ASN   E 85  ? 1.1507 1.1223 1.1334 -0.1229 -0.1745 -0.0444 85   ASN   E CG  
12123 O  OD1 . ASN   E 85  ? 1.1410 1.1229 1.1275 -0.1209 -0.1699 -0.0420 85   ASN   E OD1 
12124 N  ND2 . ASN   E 85  ? 1.1467 1.1182 1.1407 -0.1276 -0.1741 -0.0441 85   ASN   E ND2 
12125 N  N   . ALA   E 86  ? 1.2302 1.1497 1.1597 -0.1174 -0.1933 -0.0564 86   ALA   E N   
12126 C  CA  . ALA   E 86  ? 1.1932 1.0974 1.1017 -0.1131 -0.1983 -0.0596 86   ALA   E CA  
12127 C  C   . ALA   E 86  ? 1.1902 1.0910 1.0992 -0.1141 -0.2095 -0.0627 86   ALA   E C   
12128 O  O   . ALA   E 86  ? 1.2425 1.1476 1.1676 -0.1195 -0.2154 -0.0635 86   ALA   E O   
12129 C  CB  . ALA   E 86  ? 1.2718 1.1630 1.1722 -0.1138 -0.1991 -0.0616 86   ALA   E CB  
12130 N  N   . CYS   E 87  ? 1.2415 1.1343 1.1329 -0.1086 -0.2123 -0.0643 87   CYS   E N   
12131 C  CA  . CYS   E 87  ? 1.3115 1.1995 1.2008 -0.1087 -0.2235 -0.0674 87   CYS   E CA  
12132 C  C   . CYS   E 87  ? 1.2698 1.1419 1.1334 -0.1020 -0.2266 -0.0699 87   CYS   E C   
12133 O  O   . CYS   E 87  ? 1.2593 1.1277 1.1087 -0.0970 -0.2187 -0.0684 87   CYS   E O   
12134 C  CB  . CYS   E 87  ? 1.2531 1.1552 1.1551 -0.1094 -0.2237 -0.0654 87   CYS   E CB  
12135 S  SG  . CYS   E 87  ? 1.3053 1.2137 1.1975 -0.1033 -0.2124 -0.0616 87   CYS   E SG  
12136 N  N   . ILE   E 88  ? 1.3161 1.1788 1.1743 -0.1019 -0.2382 -0.0738 88   ILE   E N   
12137 C  CA  . ILE   E 88  ? 1.3603 1.2080 1.1942 -0.0953 -0.2424 -0.0762 88   ILE   E CA  
12138 C  C   . ILE   E 88  ? 1.3304 1.1819 1.1668 -0.0942 -0.2492 -0.0770 88   ILE   E C   
12139 O  O   . ILE   E 88  ? 1.3000 1.1575 1.1531 -0.0991 -0.2572 -0.0784 88   ILE   E O   
12140 C  CB  . ILE   E 88  ? 1.3527 1.1821 1.1736 -0.0949 -0.2512 -0.0809 88   ILE   E CB  
12141 C  CG1 . ILE   E 88  ? 1.3228 1.1441 1.1315 -0.0926 -0.2435 -0.0802 88   ILE   E CG1 
12142 C  CG2 . ILE   E 88  ? 1.3919 1.2074 1.1929 -0.0893 -0.2598 -0.0841 88   ILE   E CG2 
12143 C  CD1 . ILE   E 88  ? 1.3116 1.1206 1.1183 -0.0955 -0.2507 -0.0838 88   ILE   E CD1 
12144 N  N   . LEU   E 89  ? 1.3091 1.1568 1.1291 -0.0878 -0.2459 -0.0760 89   LEU   E N   
12145 C  CA  . LEU   E 89  ? 1.3834 1.2352 1.2044 -0.0860 -0.2506 -0.0760 89   LEU   E CA  
12146 C  C   . LEU   E 89  ? 1.4165 1.2499 1.2111 -0.0790 -0.2565 -0.0789 89   LEU   E C   
12147 O  O   . LEU   E 89  ? 1.4255 1.2464 1.2003 -0.0742 -0.2521 -0.0791 89   LEU   E O   
12148 C  CB  . LEU   E 89  ? 1.3469 1.2137 1.1755 -0.0851 -0.2395 -0.0711 89   LEU   E CB  
12149 C  CG  . LEU   E 89  ? 1.3381 1.2212 1.1884 -0.0907 -0.2314 -0.0678 89   LEU   E CG  
12150 C  CD1 . LEU   E 89  ? 1.3494 1.2435 1.2011 -0.0880 -0.2202 -0.0634 89   LEU   E CD1 
12151 C  CD2 . LEU   E 89  ? 1.3031 1.1974 1.1774 -0.0974 -0.2380 -0.0684 89   LEU   E CD2 
12152 N  N   . GLU   E 90  ? 1.4620 1.2934 1.2562 -0.0781 -0.2665 -0.0811 90   GLU   E N   
12153 C  CA  . GLU   E 90  ? 1.6020 1.4166 1.3708 -0.0708 -0.2719 -0.0834 90   GLU   E CA  
12154 C  C   . GLU   E 90  ? 1.6210 1.4427 1.3914 -0.0683 -0.2723 -0.0817 90   GLU   E C   
12155 O  O   . GLU   E 90  ? 1.5364 1.3748 1.3287 -0.0730 -0.2721 -0.0799 90   GLU   E O   
12156 C  CB  . GLU   E 90  ? 1.6127 1.4118 1.3735 -0.0707 -0.2870 -0.0892 90   GLU   E CB  
12157 N  N   . TYR   E 91  ? 1.8008 1.6088 1.5468 -0.0608 -0.2727 -0.0823 91   TYR   E N   
12158 C  CA  . TYR   E 91  ? 1.8224 1.6336 1.5650 -0.0572 -0.2729 -0.0807 91   TYR   E CA  
12159 C  C   . TYR   E 91  ? 1.8714 1.6740 1.6104 -0.0562 -0.2886 -0.0853 91   TYR   E C   
12160 O  O   . TYR   E 91  ? 1.8859 1.6701 1.6064 -0.0526 -0.2970 -0.0894 91   TYR   E O   
12161 C  CB  . TYR   E 91  ? 1.8237 1.6244 1.5418 -0.0493 -0.2635 -0.0784 91   TYR   E CB  
12162 C  CG  . TYR   E 91  ? 1.8530 1.6579 1.5675 -0.0456 -0.2601 -0.0757 91   TYR   E CG  
12163 C  CD1 . TYR   E 91  ? 1.8760 1.6942 1.6087 -0.0491 -0.2652 -0.0753 91   TYR   E CD1 
12164 C  CD2 . TYR   E 91  ? 1.9275 1.7232 1.6207 -0.0386 -0.2512 -0.0733 91   TYR   E CD2 
12165 C  CE1 . TYR   E 91  ? 1.9258 1.7473 1.6549 -0.0457 -0.2621 -0.0728 91   TYR   E CE1 
12166 C  CE2 . TYR   E 91  ? 1.9791 1.7778 1.6688 -0.0352 -0.2478 -0.0707 91   TYR   E CE2 
12167 C  CZ  . TYR   E 91  ? 1.9565 1.7680 1.6637 -0.0388 -0.2534 -0.0705 91   TYR   E CZ  
12168 O  OH  . TYR   E 91  ? 1.9398 1.7539 1.6429 -0.0353 -0.2498 -0.0679 91   TYR   E OH  
12169 N  N   . LYS   E 92  ? 1.7945 1.6104 1.5517 -0.0594 -0.2930 -0.0848 92   LYS   E N   
12170 C  CA  . LYS   E 92  ? 1.8534 1.6637 1.6106 -0.0587 -0.3083 -0.0890 92   LYS   E CA  
12171 C  C   . LYS   E 92  ? 1.8964 1.7129 1.6531 -0.0554 -0.3072 -0.0868 92   LYS   E C   
12172 O  O   . LYS   E 92  ? 1.7978 1.6327 1.5772 -0.0600 -0.3045 -0.0843 92   LYS   E O   
12173 C  CB  . LYS   E 92  ? 1.7655 1.5866 1.5497 -0.0669 -0.3170 -0.0915 92   LYS   E CB  
12174 N  N   . GLN   E 93  ? 2.0444 1.8446 1.7747 -0.0474 -0.3093 -0.0877 93   GLN   E N   
12175 C  CA  . GLN   E 93  ? 2.0715 1.8737 1.7968 -0.0432 -0.3089 -0.0859 93   GLN   E CA  
12176 C  C   . GLN   E 93  ? 2.1303 1.9248 1.8537 -0.0418 -0.3260 -0.0909 93   GLN   E C   
12177 O  O   . GLN   E 93  ? 2.1605 1.9356 1.8635 -0.0373 -0.3351 -0.0952 93   GLN   E O   
12178 C  CB  . GLN   E 93  ? 2.0669 1.8556 1.7640 -0.0351 -0.2994 -0.0834 93   GLN   E CB  
12179 C  CG  . GLN   E 93  ? 2.0636 1.8564 1.7571 -0.0313 -0.2950 -0.0802 93   GLN   E CG  
12180 C  CD  . GLN   E 93  ? 2.2313 2.0089 1.9063 -0.0249 -0.3069 -0.0834 93   GLN   E CD  
12181 O  OE1 . GLN   E 93  ? 2.3040 2.0746 1.9795 -0.0255 -0.3215 -0.0885 93   GLN   E OE1 
12182 N  NE2 . GLN   E 93  ? 2.2747 2.0469 1.9338 -0.0187 -0.3010 -0.0806 93   GLN   E NE2 
12183 N  N   . SER   E 94  ? 2.1285 1.9379 1.8730 -0.0453 -0.3307 -0.0906 94   SER   E N   
12184 C  CA  . SER   E 94  ? 2.0819 1.8861 1.8266 -0.0437 -0.3467 -0.0951 94   SER   E CA  
12185 C  C   . SER   E 94  ? 2.2004 2.0069 1.9390 -0.0389 -0.3450 -0.0927 94   SER   E C   
12186 O  O   . SER   E 94  ? 2.1490 1.9713 1.9086 -0.0423 -0.3471 -0.0917 94   SER   E O   
12187 C  CB  . SER   E 94  ? 2.0066 1.8264 1.7832 -0.0522 -0.3549 -0.0973 94   SER   E CB  
12188 O  OG  . SER   E 94  ? 1.9432 1.7631 1.7250 -0.0509 -0.3685 -0.1005 94   SER   E OG  
12189 N  N   . GLY   E 95  ? 2.2208 2.0106 1.9296 -0.0306 -0.3409 -0.0918 95   GLY   E N   
12190 C  CA  . GLY   E 95  ? 2.1983 1.9881 1.8983 -0.0254 -0.3377 -0.0891 95   GLY   E CA  
12191 C  C   . GLY   E 95  ? 2.1737 1.9779 1.8819 -0.0273 -0.3205 -0.0827 95   GLY   E C   
12192 O  O   . GLY   E 95  ? 2.1754 1.9815 1.8831 -0.0290 -0.3093 -0.0802 95   GLY   E O   
12193 N  N   . GLU   E 96  ? 2.1243 1.9384 1.8401 -0.0266 -0.3186 -0.0801 96   GLU   E N   
12194 C  CA  . GLU   E 96  ? 2.0656 1.8950 1.7926 -0.0290 -0.3034 -0.0743 96   GLU   E CA  
12195 C  C   . GLU   E 96  ? 2.0778 1.9250 1.8310 -0.0376 -0.2977 -0.0729 96   GLU   E C   
12196 O  O   . GLU   E 96  ? 2.0056 1.8613 1.7635 -0.0393 -0.2840 -0.0686 96   GLU   E O   
12197 C  CB  . GLU   E 96  ? 1.9357 1.7750 1.6716 -0.0283 -0.3047 -0.0725 96   GLU   E CB  
12198 N  N   . SER   E 97  ? 2.2703 2.1228 2.0408 -0.0429 -0.3080 -0.0765 97   SER   E N   
12199 C  CA  . SER   E 97  ? 2.2271 2.0959 2.0229 -0.0510 -0.3033 -0.0753 97   SER   E CA  
12200 C  C   . SER   E 97  ? 2.1975 2.0579 1.9839 -0.0516 -0.2980 -0.0756 97   SER   E C   
12201 O  O   . SER   E 97  ? 2.1907 2.0341 1.9602 -0.0486 -0.3056 -0.0795 97   SER   E O   
12202 C  CB  . SER   E 97  ? 2.2326 2.1096 2.0508 -0.0564 -0.3161 -0.0789 97   SER   E CB  
12203 O  OG  . SER   E 97  ? 2.2044 2.0864 2.0368 -0.0627 -0.3153 -0.0798 97   SER   E OG  
12204 N  N   . ILE   E 98  ? 1.9160 1.7879 1.7132 -0.0553 -0.2852 -0.0717 98   ILE   E N   
12205 C  CA  . ILE   E 98  ? 1.7969 1.6638 1.5891 -0.0566 -0.2793 -0.0717 98   ILE   E CA  
12206 C  C   . ILE   E 98  ? 1.6991 1.5826 1.5190 -0.0648 -0.2775 -0.0710 98   ILE   E C   
12207 O  O   . ILE   E 98  ? 1.7225 1.6232 1.5627 -0.0686 -0.2738 -0.0683 98   ILE   E O   
12208 C  CB  . ILE   E 98  ? 1.7021 1.5659 1.4796 -0.0525 -0.2649 -0.0677 98   ILE   E CB  
12209 C  CG1 . ILE   E 98  ? 1.7028 1.5810 1.4906 -0.0528 -0.2564 -0.0632 98   ILE   E CG1 
12210 C  CG2 . ILE   E 98  ? 1.7646 1.6075 1.5116 -0.0444 -0.2665 -0.0691 98   ILE   E CG2 
12211 C  CD1 . ILE   E 98  ? 1.6901 1.5893 1.5062 -0.0601 -0.2513 -0.0608 98   ILE   E CD1 
12212 N  N   . ASP   E 99  ? 1.6434 1.5212 1.4635 -0.0675 -0.2800 -0.0734 99   ASP   E N   
12213 C  CA  . ASP   E 99  ? 1.5507 1.4428 1.3956 -0.0751 -0.2774 -0.0725 99   ASP   E CA  
12214 C  C   . ASP   E 99  ? 1.5482 1.4308 1.3855 -0.0761 -0.2756 -0.0739 99   ASP   E C   
12215 O  O   . ASP   E 99  ? 1.5609 1.4266 1.3812 -0.0731 -0.2835 -0.0778 99   ASP   E O   
12216 C  CB  . ASP   E 99  ? 1.4363 1.3367 1.3025 -0.0801 -0.2889 -0.0751 99   ASP   E CB  
12217 N  N   . ILE   E 100 ? 1.4994 1.3920 1.3481 -0.0799 -0.2652 -0.0709 100  ILE   E N   
12218 C  CA  . ILE   E 100 ? 1.4444 1.3293 1.2867 -0.0807 -0.2620 -0.0717 100  ILE   E CA  
12219 C  C   . ILE   E 100 ? 1.4312 1.3213 1.2934 -0.0878 -0.2684 -0.0738 100  ILE   E C   
12220 O  O   . ILE   E 100 ? 1.4260 1.3319 1.3106 -0.0932 -0.2641 -0.0714 100  ILE   E O   
12221 C  CB  . ILE   E 100 ? 1.3881 1.2801 1.2308 -0.0804 -0.2471 -0.0673 100  ILE   E CB  
12222 C  CG1 . ILE   E 100 ? 1.3930 1.2760 1.2129 -0.0730 -0.2404 -0.0657 100  ILE   E CG1 
12223 C  CG2 . ILE   E 100 ? 1.4367 1.3247 1.2803 -0.0831 -0.2448 -0.0682 100  ILE   E CG2 
12224 C  CD1 . ILE   E 100 ? 1.5099 1.3745 1.3068 -0.0687 -0.2404 -0.0679 100  ILE   E CD1 
12225 N  N   . ILE   E 101 ? 1.4357 1.3117 1.2892 -0.0878 -0.2780 -0.0783 101  ILE   E N   
12226 C  CA  . ILE   E 101 ? 1.4289 1.3078 1.3004 -0.0944 -0.2853 -0.0808 101  ILE   E CA  
12227 C  C   . ILE   E 101 ? 1.4201 1.2972 1.2924 -0.0971 -0.2781 -0.0798 101  ILE   E C   
12228 O  O   . ILE   E 101 ? 1.4067 1.2734 1.2595 -0.0927 -0.2721 -0.0794 101  ILE   E O   
12229 C  CB  . ILE   E 101 ? 1.5288 1.3933 1.3917 -0.0931 -0.3009 -0.0865 101  ILE   E CB  
12230 C  CG1 . ILE   E 101 ? 1.5594 1.4029 1.3901 -0.0854 -0.3025 -0.0887 101  ILE   E CG1 
12231 C  CG2 . ILE   E 101 ? 1.5297 1.4011 1.4017 -0.0928 -0.3089 -0.0874 101  ILE   E CG2 
12232 C  CD1 . ILE   E 101 ? 1.5507 1.3849 1.3695 -0.0848 -0.2955 -0.0884 101  ILE   E CD1 
12233 N  N   . THR   E 102 ? 1.4502 1.3376 1.3456 -0.1043 -0.2781 -0.0794 102  THR   E N   
12234 C  CA  . THR   E 102 ? 1.4076 1.2939 1.3057 -0.1073 -0.2714 -0.0784 102  THR   E CA  
12235 C  C   . THR   E 102 ? 1.4169 1.2903 1.3131 -0.1098 -0.2824 -0.0833 102  THR   E C   
12236 O  O   . THR   E 102 ? 1.4215 1.3000 1.3368 -0.1155 -0.2900 -0.0851 102  THR   E O   
12237 C  CB  . THR   E 102 ? 1.3862 1.2910 1.3091 -0.1130 -0.2630 -0.0744 102  THR   E CB  
12238 O  OG1 . THR   E 102 ? 1.4739 1.3826 1.4171 -0.1199 -0.2694 -0.0761 102  THR   E OG1 
12239 C  CG2 . THR   E 102 ? 1.4136 1.3329 1.3457 -0.1121 -0.2591 -0.0712 102  THR   E CG2 
12240 N  N   . ARG   E 103 ? 1.4441 1.3000 1.3165 -0.1052 -0.2834 -0.0855 103  ARG   E N   
12241 C  CA  . ARG   E 103 ? 1.4194 1.2614 1.2876 -0.1071 -0.2933 -0.0902 103  ARG   E CA  
12242 C  C   . ARG   E 103 ? 1.4610 1.3093 1.3476 -0.1142 -0.2893 -0.0891 103  ARG   E C   
12243 O  O   . ARG   E 103 ? 1.4682 1.3188 1.3723 -0.1201 -0.2972 -0.0913 103  ARG   E O   
12244 C  CB  . ARG   E 103 ? 1.3175 1.1395 1.1553 -0.1002 -0.2937 -0.0923 103  ARG   E CB  
12245 N  N   . ALA   E 104 ? 1.4335 1.2853 1.3176 -0.1137 -0.2767 -0.0854 104  ALA   E N   
12246 C  CA  . ALA   E 104 ? 1.3850 1.2435 1.2861 -0.1198 -0.2712 -0.0836 104  ALA   E CA  
12247 C  C   . ALA   E 104 ? 1.4147 1.2916 1.3306 -0.1213 -0.2592 -0.0782 104  ALA   E C   
12248 O  O   . ALA   E 104 ? 1.3810 1.2643 1.2921 -0.1173 -0.2544 -0.0758 104  ALA   E O   
12249 C  CB  . ALA   E 104 ? 1.3962 1.2409 1.2811 -0.1180 -0.2676 -0.0845 104  ALA   E CB  
12250 N  N   . HIS   E 105 ? 1.3904 1.2752 1.3245 -0.1272 -0.2546 -0.0762 105  HIS   E N   
12251 C  CA  . HIS   E 105 ? 1.3257 1.2255 1.2715 -0.1283 -0.2425 -0.0712 105  HIS   E CA  
12252 C  C   . HIS   E 105 ? 1.3060 1.2082 1.2661 -0.1341 -0.2385 -0.0699 105  HIS   E C   
12253 O  O   . HIS   E 105 ? 1.3525 1.2512 1.3233 -0.1392 -0.2459 -0.0724 105  HIS   E O   
12254 C  CB  . HIS   E 105 ? 1.3218 1.2375 1.2835 -0.1295 -0.2424 -0.0690 105  HIS   E CB  
12255 C  CG  . HIS   E 105 ? 1.3282 1.2506 1.3125 -0.1358 -0.2502 -0.0704 105  HIS   E CG  
12256 N  ND1 . HIS   E 105 ? 1.2563 1.1929 1.2639 -0.1411 -0.2448 -0.0672 105  HIS   E ND1 
12257 C  CD2 . HIS   E 105 ? 1.4113 1.3285 1.3988 -0.1374 -0.2630 -0.0745 105  HIS   E CD2 
12258 C  CE1 . HIS   E 105 ? 1.3438 1.2840 1.3688 -0.1459 -0.2535 -0.0692 105  HIS   E CE1 
12259 N  NE2 . HIS   E 105 ? 1.4050 1.3338 1.4187 -0.1439 -0.2649 -0.0738 105  HIS   E NE2 
12260 N  N   . GLY   E 106 ? 1.2764 1.1839 1.2362 -0.1331 -0.2269 -0.0662 106  GLY   E N   
12261 C  CA  . GLY   E 106 ? 1.2387 1.1492 1.2114 -0.1379 -0.2214 -0.0643 106  GLY   E CA  
12262 C  C   . GLY   E 106 ? 1.2672 1.1831 1.2353 -0.1348 -0.2088 -0.0602 106  GLY   E C   
12263 O  O   . GLY   E 106 ? 1.2939 1.2080 1.2462 -0.1289 -0.2051 -0.0597 106  GLY   E O   
12264 N  N   . ASN   E 107 ? 1.2256 1.1479 1.2077 -0.1388 -0.2023 -0.0575 107  ASN   E N   
12265 C  CA  . ASN   E 107 ? 1.2235 1.1504 1.2024 -0.1362 -0.1908 -0.0538 107  ASN   E CA  
12266 C  C   . ASN   E 107 ? 1.2971 1.2123 1.2666 -0.1360 -0.1877 -0.0544 107  ASN   E C   
12267 O  O   . ASN   E 107 ? 1.3551 1.2640 1.3309 -0.1407 -0.1915 -0.0558 107  ASN   E O   
12268 C  CB  . ASN   E 107 ? 1.1767 1.1183 1.1757 -0.1397 -0.1845 -0.0499 107  ASN   E CB  
12269 C  CG  . ASN   E 107 ? 1.2171 1.1633 1.2116 -0.1362 -0.1737 -0.0465 107  ASN   E CG  
12270 O  OD1 . ASN   E 107 ? 1.2670 1.2176 1.2538 -0.1315 -0.1706 -0.0455 107  ASN   E OD1 
12271 N  ND2 . ASN   E 107 ? 1.2771 1.2213 1.2754 -0.1381 -0.1679 -0.0448 107  ASN   E ND2 
12272 N  N   . VAL   E 108 ? 1.3095 1.2221 1.2647 -0.1307 -0.1806 -0.0531 108  VAL   E N   
12273 C  CA  . VAL   E 108 ? 1.2804 1.1804 1.2230 -0.1293 -0.1784 -0.0542 108  VAL   E CA  
12274 C  C   . VAL   E 108 ? 1.3429 1.2482 1.2882 -0.1282 -0.1676 -0.0505 108  VAL   E C   
12275 O  O   . VAL   E 108 ? 1.3468 1.2449 1.2782 -0.1240 -0.1632 -0.0506 108  VAL   E O   
12276 C  CB  . VAL   E 108 ? 1.2607 1.1493 1.1806 -0.1231 -0.1808 -0.0568 108  VAL   E CB  
12277 C  CG1 . VAL   E 108 ? 1.1918 1.0720 1.1071 -0.1241 -0.1923 -0.0608 108  VAL   E CG1 
12278 C  CG2 . VAL   E 108 ? 1.3618 1.2585 1.2757 -0.1176 -0.1750 -0.0548 108  VAL   E CG2 
12279 N  N   . GLN   E 109 ? 1.4709 1.3884 1.4337 -0.1316 -0.1635 -0.0474 109  GLN   E N   
12280 C  CA  . GLN   E 109 ? 1.5094 1.4306 1.4744 -0.1305 -0.1538 -0.0441 109  GLN   E CA  
12281 C  C   . GLN   E 109 ? 1.5109 1.4220 1.4763 -0.1337 -0.1531 -0.0445 109  GLN   E C   
12282 O  O   . GLN   E 109 ? 1.5107 1.4177 1.4845 -0.1390 -0.1588 -0.0460 109  GLN   E O   
12283 C  CB  . GLN   E 109 ? 1.4918 1.4282 1.4742 -0.1327 -0.1494 -0.0406 109  GLN   E CB  
12284 C  CG  . GLN   E 109 ? 1.4851 1.4274 1.4661 -0.1290 -0.1396 -0.0373 109  GLN   E CG  
12285 C  CD  . GLN   E 109 ? 1.5425 1.4999 1.5368 -0.1295 -0.1364 -0.0344 109  GLN   E CD  
12286 O  OE1 . GLN   E 109 ? 1.5729 1.5366 1.5801 -0.1333 -0.1406 -0.0344 109  GLN   E OE1 
12287 N  NE2 . GLN   E 109 ? 1.5679 1.5311 1.5593 -0.1253 -0.1290 -0.0320 109  GLN   E NE2 
12288 N  N   . ASP   E 110 ? 1.4413 1.3475 1.3971 -0.1303 -0.1463 -0.0432 110  ASP   E N   
12289 C  CA  . ASP   E 110 ? 1.4174 1.3151 1.3744 -0.1331 -0.1439 -0.0428 110  ASP   E CA  
12290 C  C   . ASP   E 110 ? 1.4427 1.3495 1.4117 -0.1343 -0.1355 -0.0386 110  ASP   E C   
12291 O  O   . ASP   E 110 ? 1.4905 1.4046 1.4567 -0.1298 -0.1296 -0.0365 110  ASP   E O   
12292 C  CB  . ASP   E 110 ? 1.3999 1.2846 1.3375 -0.1284 -0.1421 -0.0443 110  ASP   E CB  
12293 C  CG  . ASP   E 110 ? 1.3863 1.2584 1.3123 -0.1283 -0.1506 -0.0486 110  ASP   E CG  
12294 O  OD1 . ASP   E 110 ? 1.3651 1.2346 1.2996 -0.1336 -0.1577 -0.0504 110  ASP   E OD1 
12295 O  OD2 . ASP   E 110 ? 1.3278 1.1925 1.2364 -0.1227 -0.1501 -0.0502 110  ASP   E OD2 
12296 N  N   . ARG   E 111 ? 1.4781 1.3844 1.4608 -0.1402 -0.1351 -0.0373 111  ARG   E N   
12297 C  CA  . ARG   E 111 ? 1.3931 1.3068 1.3870 -0.1414 -0.1269 -0.0331 111  ARG   E CA  
12298 C  C   . ARG   E 111 ? 1.3625 1.2723 1.3437 -0.1358 -0.1191 -0.0315 111  ARG   E C   
12299 O  O   . ARG   E 111 ? 1.3736 1.2921 1.3549 -0.1320 -0.1136 -0.0292 111  ARG   E O   
12300 C  CB  . ARG   E 111 ? 1.2676 1.1778 1.2755 -0.1483 -0.1270 -0.0322 111  ARG   E CB  
12301 N  N   . ILE   E 112 ? 1.3599 1.2561 1.3299 -0.1351 -0.1191 -0.0329 112  ILE   E N   
12302 C  CA  . ILE   E 112 ? 1.4299 1.3207 1.3858 -0.1292 -0.1130 -0.0321 112  ILE   E CA  
12303 C  C   . ILE   E 112 ? 1.5133 1.4017 1.4537 -0.1235 -0.1160 -0.0349 112  ILE   E C   
12304 O  O   . ILE   E 112 ? 1.5342 1.4155 1.4685 -0.1244 -0.1229 -0.0381 112  ILE   E O   
12305 C  CB  . ILE   E 112 ? 1.4160 1.2928 1.3670 -0.1310 -0.1112 -0.0322 112  ILE   E CB  
12306 N  N   . GLY   E 113 ? 1.4429 1.3367 1.3768 -0.1175 -0.1109 -0.0337 113  GLY   E N   
12307 C  CA  . GLY   E 113 ? 1.4437 1.3339 1.3625 -0.1118 -0.1124 -0.0361 113  GLY   E CA  
12308 C  C   . GLY   E 113 ? 1.4779 1.3775 1.3939 -0.1059 -0.1077 -0.0348 113  GLY   E C   
12309 O  O   . GLY   E 113 ? 1.4530 1.3648 1.3789 -0.1065 -0.1069 -0.0332 113  GLY   E O   
12310 N  N   . ARG   E 114 ? 1.5224 1.4162 1.4251 -0.1001 -0.1046 -0.0355 114  ARG   E N   
12311 C  CA  . ARG   E 114 ? 1.4827 1.3845 1.3821 -0.0941 -0.1007 -0.0348 114  ARG   E CA  
12312 C  C   . ARG   E 114 ? 1.5050 1.4089 1.3989 -0.0919 -0.1043 -0.0370 114  ARG   E C   
12313 O  O   . ARG   E 114 ? 1.5226 1.4162 1.4049 -0.0906 -0.1075 -0.0395 114  ARG   E O   
12314 C  CB  . ARG   E 114 ? 1.4890 1.3839 1.3774 -0.0887 -0.0961 -0.0349 114  ARG   E CB  
12315 N  N   . PRO   E 115 ? 1.4404 1.3566 1.3416 -0.0914 -0.1040 -0.0360 115  PRO   E N   
12316 C  CA  . PRO   E 115 ? 1.3730 1.2907 1.2683 -0.0891 -0.1068 -0.0377 115  PRO   E CA  
12317 C  C   . PRO   E 115 ? 1.3490 1.2636 1.2323 -0.0823 -0.1033 -0.0386 115  PRO   E C   
12318 O  O   . PRO   E 115 ? 1.3676 1.2867 1.2521 -0.0789 -0.0981 -0.0373 115  PRO   E O   
12319 C  CB  . PRO   E 115 ? 1.3731 1.3052 1.2807 -0.0903 -0.1062 -0.0358 115  PRO   E CB  
12320 C  CG  . PRO   E 115 ? 1.3608 1.2970 1.2809 -0.0949 -0.1052 -0.0336 115  PRO   E CG  
12321 C  CD  . PRO   E 115 ? 1.4288 1.3569 1.3441 -0.0938 -0.1016 -0.0332 115  PRO   E CD  
12322 N  N   . SER   E 116 ? 1.3156 1.2227 1.1876 -0.0801 -0.1061 -0.0409 116  SER   E N   
12323 C  CA  . SER   E 116 ? 1.3864 1.2887 1.2463 -0.0738 -0.1027 -0.0420 116  SER   E CA  
12324 C  C   . SER   E 116 ? 1.3987 1.3125 1.2623 -0.0695 -0.0981 -0.0408 116  SER   E C   
12325 O  O   . SER   E 116 ? 1.4590 1.3820 1.3296 -0.0707 -0.0989 -0.0399 116  SER   E O   
12326 C  CB  . SER   E 116 ? 1.4138 1.3051 1.2603 -0.0722 -0.1065 -0.0446 116  SER   E CB  
12327 O  OG  . SER   E 116 ? 1.4400 1.3285 1.2762 -0.0656 -0.1024 -0.0453 116  SER   E OG  
12328 N  N   . GLU   E 117 ? 1.4382 1.3508 1.2966 -0.0643 -0.0935 -0.0408 117  GLU   E N   
12329 C  CA  . GLU   E 117 ? 1.4343 1.3573 1.2966 -0.0599 -0.0890 -0.0399 117  GLU   E CA  
12330 C  C   . GLU   E 117 ? 1.4214 1.3468 1.2806 -0.0583 -0.0896 -0.0406 117  GLU   E C   
12331 O  O   . GLU   E 117 ? 1.4568 1.3933 1.3245 -0.0585 -0.0884 -0.0393 117  GLU   E O   
12332 C  CB  . GLU   E 117 ? 1.4048 1.3244 1.2609 -0.0543 -0.0848 -0.0405 117  GLU   E CB  
12333 N  N   . THR   E 118 ? 1.4122 1.3268 1.2587 -0.0565 -0.0914 -0.0425 118  THR   E N   
12334 C  CA  . THR   E 118 ? 1.4251 1.3401 1.2667 -0.0547 -0.0918 -0.0430 118  THR   E CA  
12335 C  C   . THR   E 118 ? 1.3760 1.2921 1.2211 -0.0596 -0.0974 -0.0430 118  THR   E C   
12336 O  O   . THR   E 118 ? 1.3834 1.2971 1.2223 -0.0584 -0.0989 -0.0437 118  THR   E O   
12337 C  CB  . THR   E 118 ? 1.4563 1.3583 1.2816 -0.0502 -0.0914 -0.0451 118  THR   E CB  
12338 O  OG1 . THR   E 118 ? 1.4729 1.3622 1.2901 -0.0530 -0.0967 -0.0468 118  THR   E OG1 
12339 C  CG2 . THR   E 118 ? 1.4049 1.3064 1.2271 -0.0446 -0.0858 -0.0452 118  THR   E CG2 
12340 N  N   . GLY   E 119 ? 1.3740 1.2935 1.2289 -0.0651 -0.1005 -0.0422 119  GLY   E N   
12341 C  CA  . GLY   E 119 ? 1.3416 1.2649 1.2028 -0.0696 -0.1054 -0.0419 119  GLY   E CA  
12342 C  C   . GLY   E 119 ? 1.2963 1.2075 1.1477 -0.0712 -0.1118 -0.0442 119  GLY   E C   
12343 O  O   . GLY   E 119 ? 1.2791 1.1780 1.1176 -0.0689 -0.1127 -0.0461 119  GLY   E O   
12344 N  N   . ILE   E 120 ? 1.2532 1.1679 1.1108 -0.0752 -0.1168 -0.0442 120  ILE   E N   
12345 C  CA  . ILE   E 120 ? 1.2079 1.1121 1.0587 -0.0776 -0.1243 -0.0465 120  ILE   E CA  
12346 C  C   . ILE   E 120 ? 1.2727 1.1668 1.1063 -0.0723 -0.1246 -0.0483 120  ILE   E C   
12347 O  O   . ILE   E 120 ? 1.2223 1.1210 1.0538 -0.0693 -0.1223 -0.0475 120  ILE   E O   
12348 C  CB  . ILE   E 120 ? 1.1334 1.0446 0.9951 -0.0822 -0.1295 -0.0461 120  ILE   E CB  
12349 C  CG1 . ILE   E 120 ? 1.1107 1.0305 0.9891 -0.0875 -0.1293 -0.0444 120  ILE   E CG1 
12350 C  CG2 . ILE   E 120 ? 1.1704 1.0703 1.0238 -0.0837 -0.1377 -0.0489 120  ILE   E CG2 
12351 C  CD1 . ILE   E 120 ? 1.3296 1.2611 1.2168 -0.0861 -0.1219 -0.0416 120  ILE   E CD1 
12352 N  N   . ILE   E 121 ? 1.2981 1.1779 1.1188 -0.0710 -0.1270 -0.0506 121  ILE   E N   
12353 C  CA  . ILE   E 121 ? 1.2206 1.0879 1.0237 -0.0668 -0.1293 -0.0528 121  ILE   E CA  
12354 C  C   . ILE   E 121 ? 1.2154 1.0746 1.0161 -0.0707 -0.1390 -0.0552 121  ILE   E C   
12355 O  O   . ILE   E 121 ? 1.2667 1.1245 1.0751 -0.0758 -0.1433 -0.0558 121  ILE   E O   
12356 C  CB  . ILE   E 121 ? 1.2003 1.0561 0.9893 -0.0622 -0.1261 -0.0540 121  ILE   E CB  
12357 C  CG1 . ILE   E 121 ? 1.2562 1.1199 1.0474 -0.0577 -0.1169 -0.0520 121  ILE   E CG1 
12358 C  CG2 . ILE   E 121 ? 1.2053 1.0471 0.9753 -0.0577 -0.1287 -0.0563 121  ILE   E CG2 
12359 C  CD1 . ILE   E 121 ? 1.2751 1.1275 1.0494 -0.0511 -0.1132 -0.0533 121  ILE   E CD1 
12360 N  N   . GLY   E 122 ? 1.2186 1.0722 1.0091 -0.0681 -0.1424 -0.0564 122  GLY   E N   
12361 C  CA  . GLY   E 122 ? 1.1864 1.0305 0.9724 -0.0709 -0.1523 -0.0591 122  GLY   E CA  
12362 C  C   . GLY   E 122 ? 1.2843 1.1140 1.0490 -0.0651 -0.1541 -0.0613 122  GLY   E C   
12363 O  O   . GLY   E 122 ? 1.3541 1.1863 1.1129 -0.0605 -0.1496 -0.0600 122  GLY   E O   
12364 N  N   . ILE   E 123 ? 1.2815 1.0955 1.0342 -0.0650 -0.1604 -0.0644 123  ILE   E N   
12365 C  CA  . ILE   E 123 ? 1.3255 1.1234 1.0556 -0.0589 -0.1622 -0.0667 123  ILE   E CA  
12366 C  C   . ILE   E 123 ? 1.4173 1.2028 1.1410 -0.0613 -0.1741 -0.0704 123  ILE   E C   
12367 O  O   . ILE   E 123 ? 1.4038 1.1928 1.1410 -0.0678 -0.1805 -0.0713 123  ILE   E O   
12368 C  CB  . ILE   E 123 ? 1.3602 1.1489 1.0783 -0.0546 -0.1566 -0.0670 123  ILE   E CB  
12369 C  CG1 . ILE   E 123 ? 1.4118 1.1967 1.1358 -0.0593 -0.1599 -0.0684 123  ILE   E CG1 
12370 C  CG2 . ILE   E 123 ? 1.3094 1.1103 1.0338 -0.0516 -0.1453 -0.0637 123  ILE   E CG2 
12371 C  CD1 . ILE   E 123 ? 1.4130 1.1876 1.1241 -0.0549 -0.1552 -0.0690 123  ILE   E CD1 
12372 N  N   . ILE   E 124 ? 1.4394 1.2099 1.1423 -0.0558 -0.1773 -0.0726 124  ILE   E N   
12373 C  CA  . ILE   E 124 ? 1.4628 1.2197 1.1572 -0.0571 -0.1894 -0.0765 124  ILE   E CA  
12374 C  C   . ILE   E 124 ? 1.4928 1.2289 1.1622 -0.0511 -0.1909 -0.0793 124  ILE   E C   
12375 O  O   . ILE   E 124 ? 1.5091 1.2395 1.1626 -0.0440 -0.1849 -0.0784 124  ILE   E O   
12376 C  CB  . ILE   E 124 ? 1.4595 1.2193 1.1548 -0.0570 -0.1950 -0.0768 124  ILE   E CB  
12377 C  CG1 . ILE   E 124 ? 1.3395 1.1167 1.0602 -0.0645 -0.1973 -0.0754 124  ILE   E CG1 
12378 C  CG2 . ILE   E 124 ? 1.5061 1.2475 1.1850 -0.0554 -0.2067 -0.0813 124  ILE   E CG2 
12379 C  CD1 . ILE   E 124 ? 1.4130 1.1907 1.1360 -0.0659 -0.2065 -0.0769 124  ILE   E CD1 
12380 N  N   . ASP   E 125 ? 1.6040 1.3285 1.2701 -0.0538 -0.1989 -0.0826 125  ASP   E N   
12381 C  CA  . ASP   E 125 ? 1.6289 1.3325 1.2712 -0.0484 -0.2017 -0.0857 125  ASP   E CA  
12382 C  C   . ASP   E 125 ? 1.6437 1.3361 1.2665 -0.0421 -0.2050 -0.0871 125  ASP   E C   
12383 O  O   . ASP   E 125 ? 1.6373 1.3333 1.2653 -0.0442 -0.2118 -0.0878 125  ASP   E O   
12384 C  CB  . ASP   E 125 ? 1.6660 1.3596 1.3106 -0.0536 -0.2119 -0.0894 125  ASP   E CB  
12385 C  CG  . ASP   E 125 ? 1.7386 1.4088 1.3584 -0.0488 -0.2195 -0.0937 125  ASP   E CG  
12386 O  OD1 . ASP   E 125 ? 1.7556 1.4149 1.3565 -0.0420 -0.2136 -0.0937 125  ASP   E OD1 
12387 O  OD2 . ASP   E 125 ? 1.7833 1.4458 1.4028 -0.0518 -0.2317 -0.0973 125  ASP   E OD2 
12388 N  N   . PRO   E 126 ? 1.6449 1.3242 1.2452 -0.0341 -0.1999 -0.0873 126  PRO   E N   
12389 C  CA  . PRO   E 126 ? 1.6505 1.3184 1.2307 -0.0273 -0.2019 -0.0882 126  PRO   E CA  
12390 C  C   . PRO   E 126 ? 1.6797 1.3330 1.2505 -0.0282 -0.2164 -0.0928 126  PRO   E C   
12391 O  O   . PRO   E 126 ? 1.7251 1.3710 1.2825 -0.0237 -0.2197 -0.0936 126  PRO   E O   
12392 C  CB  . PRO   E 126 ? 1.5800 1.2346 1.1382 -0.0190 -0.1938 -0.0879 126  PRO   E CB  
12393 C  CG  . PRO   E 126 ? 1.6231 1.2887 1.1941 -0.0211 -0.1847 -0.0854 126  PRO   E CG  
12394 C  CD  . PRO   E 126 ? 1.6232 1.2987 1.2163 -0.0304 -0.1909 -0.0862 126  PRO   E CD  
12395 N  N   . GLU   E 127 ? 1.7042 1.3524 1.2809 -0.0336 -0.2252 -0.0960 127  GLU   E N   
12396 C  CA  . GLU   E 127 ? 1.6936 1.3288 1.2641 -0.0352 -0.2401 -0.1008 127  GLU   E CA  
12397 C  C   . GLU   E 127 ? 1.7227 1.3725 1.3181 -0.0436 -0.2476 -0.1011 127  GLU   E C   
12398 O  O   . GLU   E 127 ? 1.7592 1.4005 1.3539 -0.0460 -0.2606 -0.1052 127  GLU   E O   
12399 C  CB  . GLU   E 127 ? 1.7369 1.3555 1.2977 -0.0358 -0.2459 -0.1046 127  GLU   E CB  
12400 N  N   . CYS   E 128 ? 1.7286 1.4000 1.3460 -0.0478 -0.2399 -0.0969 128  CYS   E N   
12401 C  CA  . CYS   E 128 ? 1.7019 1.3887 1.3448 -0.0559 -0.2456 -0.0967 128  CYS   E CA  
12402 C  C   . CYS   E 128 ? 1.7222 1.4069 1.3781 -0.0633 -0.2535 -0.0994 128  CYS   E C   
12403 O  O   . CYS   E 128 ? 1.6179 1.3107 1.2922 -0.0698 -0.2613 -0.1005 128  CYS   E O   
12404 C  CB  . CYS   E 128 ? 1.7074 1.3924 1.3470 -0.0545 -0.2545 -0.0984 128  CYS   E CB  
12405 S  SG  . CYS   E 128 ? 1.7475 1.4394 1.3787 -0.0479 -0.2450 -0.0944 128  CYS   E SG  
12406 N  N   . ARG   E 129 ? 1.9136 1.5880 1.5610 -0.0625 -0.2511 -0.1004 129  ARG   E N   
12407 C  CA  . ARG   E 129 ? 1.8994 1.5707 1.5584 -0.0695 -0.2577 -0.1028 129  ARG   E CA  
12408 C  C   . ARG   E 129 ? 1.8888 1.5804 1.5761 -0.0772 -0.2518 -0.0993 129  ARG   E C   
12409 O  O   . ARG   E 129 ? 1.8855 1.5791 1.5889 -0.0845 -0.2583 -0.1008 129  ARG   E O   
12410 C  CB  . ARG   E 129 ? 1.8726 1.5264 1.5133 -0.0660 -0.2564 -0.1047 129  ARG   E CB  
12411 N  N   . MET   E 130 ? 1.7433 1.4498 1.4374 -0.0757 -0.2397 -0.0946 130  MET   E N   
12412 C  CA  . MET   E 130 ? 1.6786 1.4053 1.3994 -0.0825 -0.2349 -0.0911 130  MET   E CA  
12413 C  C   . MET   E 130 ? 1.6169 1.3579 1.3404 -0.0790 -0.2227 -0.0865 130  MET   E C   
12414 O  O   . MET   E 130 ? 1.5909 1.3263 1.2968 -0.0718 -0.2171 -0.0857 130  MET   E O   
12415 C  CB  . MET   E 130 ? 1.6317 1.3578 1.3627 -0.0878 -0.2333 -0.0910 130  MET   E CB  
12416 C  CG  . MET   E 130 ? 1.6392 1.3676 1.3660 -0.0847 -0.2210 -0.0879 130  MET   E CG  
12417 S  SD  . MET   E 130 ? 1.7960 1.5047 1.4916 -0.0753 -0.2181 -0.0897 130  MET   E SD  
12418 C  CE  . MET   E 130 ? 1.6066 1.3188 1.3063 -0.0756 -0.2072 -0.0869 130  MET   E CE  
12419 N  N   . ILE   E 131 ? 1.5619 1.3214 1.3083 -0.0842 -0.2188 -0.0833 131  ILE   E N   
12420 C  CA  . ILE   E 131 ? 1.4573 1.2323 1.2109 -0.0824 -0.2074 -0.0788 131  ILE   E CA  
12421 C  C   . ILE   E 131 ? 1.4331 1.2129 1.1945 -0.0844 -0.1993 -0.0766 131  ILE   E C   
12422 O  O   . ILE   E 131 ? 1.4374 1.2171 1.2103 -0.0902 -0.2024 -0.0772 131  ILE   E O   
12423 C  CB  . ILE   E 131 ? 1.3920 1.1837 1.1652 -0.0867 -0.2089 -0.0770 131  ILE   E CB  
12424 C  CG1 . ILE   E 131 ? 1.4368 1.2263 1.1997 -0.0823 -0.2125 -0.0778 131  ILE   E CG1 
12425 C  CG2 . ILE   E 131 ? 1.3061 1.1151 1.0942 -0.0880 -0.1982 -0.0725 131  ILE   E CG2 
12426 C  CD1 . ILE   E 131 ? 1.3614 1.1636 1.1418 -0.0867 -0.2175 -0.0772 131  ILE   E CD1 
12427 N  N   . GLY   E 132 ? 1.3890 1.1727 1.1445 -0.0794 -0.1890 -0.0739 132  GLY   E N   
12428 C  CA  . GLY   E 132 ? 1.3564 1.1456 1.1189 -0.0804 -0.1808 -0.0716 132  GLY   E CA  
12429 C  C   . GLY   E 132 ? 1.3072 1.1158 1.0863 -0.0817 -0.1731 -0.0676 132  GLY   E C   
12430 O  O   . GLY   E 132 ? 1.3760 1.1912 1.1532 -0.0782 -0.1700 -0.0661 132  GLY   E O   
12431 N  N   . LEU   E 133 ? 1.2708 1.0876 1.0655 -0.0864 -0.1700 -0.0657 133  LEU   E N   
12432 C  CA  . LEU   E 133 ? 1.3088 1.1437 1.1203 -0.0880 -0.1633 -0.0619 133  LEU   E CA  
12433 C  C   . LEU   E 133 ? 1.2853 1.1228 1.1002 -0.0877 -0.1555 -0.0599 133  LEU   E C   
12434 O  O   . LEU   E 133 ? 1.3377 1.1715 1.1584 -0.0919 -0.1571 -0.0603 133  LEU   E O   
12435 C  CB  . LEU   E 133 ? 1.2905 1.1348 1.1210 -0.0950 -0.1684 -0.0614 133  LEU   E CB  
12436 C  CG  . LEU   E 133 ? 1.2768 1.1295 1.1128 -0.0953 -0.1718 -0.0611 133  LEU   E CG  
12437 C  CD1 . LEU   E 133 ? 1.2931 1.1340 1.1106 -0.0907 -0.1769 -0.0639 133  LEU   E CD1 
12438 C  CD2 . LEU   E 133 ? 1.2502 1.1087 1.1040 -0.1025 -0.1784 -0.0615 133  LEU   E CD2 
12439 N  N   . ARG   E 134 ? 1.2266 1.0705 1.0386 -0.0827 -0.1472 -0.0578 134  ARG   E N   
12440 C  CA  . ARG   E 134 ? 1.3243 1.1726 1.1412 -0.0821 -0.1399 -0.0557 134  ARG   E CA  
12441 C  C   . ARG   E 134 ? 1.3325 1.1980 1.1673 -0.0847 -0.1359 -0.0525 134  ARG   E C   
12442 O  O   . ARG   E 134 ? 1.2585 1.1335 1.0950 -0.0813 -0.1310 -0.0508 134  ARG   E O   
12443 C  CB  . ARG   E 134 ? 1.2940 1.1385 1.0976 -0.0749 -0.1335 -0.0556 134  ARG   E CB  
12444 C  CG  . ARG   E 134 ? 1.2904 1.1350 1.0960 -0.0740 -0.1277 -0.0544 134  ARG   E CG  
12445 C  CD  . ARG   E 134 ? 1.3218 1.1820 1.1438 -0.0759 -0.1226 -0.0512 134  ARG   E CD  
12446 N  NE  . ARG   E 134 ? 1.3713 1.2416 1.1942 -0.0714 -0.1175 -0.0498 134  ARG   E NE  
12447 C  CZ  . ARG   E 134 ? 1.4110 1.2807 1.2268 -0.0655 -0.1117 -0.0495 134  ARG   E CZ  
12448 N  NH1 . ARG   E 134 ? 1.3496 1.2098 1.1567 -0.0630 -0.1099 -0.0505 134  ARG   E NH1 
12449 N  NH2 . ARG   E 134 ? 1.3765 1.2557 1.1945 -0.0620 -0.1075 -0.0483 134  ARG   E NH2 
12450 N  N   . LEU   E 135 ? 1.3137 1.1828 1.1619 -0.0905 -0.1374 -0.0516 135  LEU   E N   
12451 C  CA  . LEU   E 135 ? 1.2557 1.1398 1.1209 -0.0933 -0.1339 -0.0486 135  LEU   E CA  
12452 C  C   . LEU   E 135 ? 1.3384 1.2254 1.2071 -0.0922 -0.1268 -0.0465 135  LEU   E C   
12453 O  O   . LEU   E 135 ? 1.3827 1.2813 1.2587 -0.0907 -0.1215 -0.0440 135  LEU   E O   
12454 C  CB  . LEU   E 135 ? 1.2622 1.1490 1.1411 -0.1003 -0.1395 -0.0486 135  LEU   E CB  
12455 C  CG  . LEU   E 135 ? 1.2857 1.1782 1.1695 -0.1019 -0.1451 -0.0493 135  LEU   E CG  
12456 C  CD1 . LEU   E 135 ? 1.2907 1.1730 1.1573 -0.0977 -0.1492 -0.0521 135  LEU   E CD1 
12457 C  CD2 . LEU   E 135 ? 1.2721 1.1653 1.1693 -0.1089 -0.1513 -0.0499 135  LEU   E CD2 
12458 N  N   . TYR   E 136 ? 1.4460 1.3222 1.3093 -0.0930 -0.1269 -0.0474 136  TYR   E N   
12459 C  CA  . TYR   E 136 ? 1.4534 1.3309 1.3208 -0.0929 -0.1211 -0.0453 136  TYR   E CA  
12460 C  C   . TYR   E 136 ? 1.4692 1.3345 1.3213 -0.0883 -0.1189 -0.0468 136  TYR   E C   
12461 O  O   . TYR   E 136 ? 1.4445 1.2978 1.2846 -0.0874 -0.1232 -0.0495 136  TYR   E O   
12462 C  CB  . TYR   E 136 ? 1.4240 1.3011 1.3038 -0.0998 -0.1230 -0.0444 136  TYR   E CB  
12463 C  CG  . TYR   E 136 ? 1.3649 1.2534 1.2609 -0.1048 -0.1257 -0.0431 136  TYR   E CG  
12464 C  CD1 . TYR   E 136 ? 1.3993 1.3010 1.3072 -0.1051 -0.1207 -0.0400 136  TYR   E CD1 
12465 C  CD2 . TYR   E 136 ? 1.3207 1.2064 1.2199 -0.1090 -0.1334 -0.0451 136  TYR   E CD2 
12466 C  CE1 . TYR   E 136 ? 1.3998 1.3118 1.3224 -0.1094 -0.1229 -0.0388 136  TYR   E CE1 
12467 C  CE2 . TYR   E 136 ? 1.2849 1.1811 1.1993 -0.1133 -0.1360 -0.0440 136  TYR   E CE2 
12468 C  CZ  . TYR   E 136 ? 1.3151 1.2246 1.2412 -0.1135 -0.1305 -0.0408 136  TYR   E CZ  
12469 O  OH  . TYR   E 136 ? 1.2754 1.1955 1.2167 -0.1176 -0.1328 -0.0396 136  TYR   E OH  
12470 N  N   . ASP   E 137 ? 1.4867 1.3550 1.3389 -0.0851 -0.1125 -0.0450 137  ASP   E N   
12471 C  CA  . ASP   E 137 ? 1.5043 1.3626 1.3429 -0.0800 -0.1097 -0.0461 137  ASP   E CA  
12472 C  C   . ASP   E 137 ? 1.5454 1.3898 1.3792 -0.0831 -0.1123 -0.0473 137  ASP   E C   
12473 O  O   . ASP   E 137 ? 1.4908 1.3359 1.3343 -0.0879 -0.1119 -0.0458 137  ASP   E O   
12474 C  CB  . ASP   E 137 ? 1.5175 1.3830 1.3586 -0.0758 -0.1027 -0.0441 137  ASP   E CB  
12475 C  CG  . ASP   E 137 ? 1.5537 1.4248 1.3895 -0.0695 -0.0998 -0.0445 137  ASP   E CG  
12476 O  OD1 . ASP   E 137 ? 1.6328 1.4959 1.4569 -0.0667 -0.1018 -0.0466 137  ASP   E OD1 
12477 O  OD2 . ASP   E 137 ? 1.4968 1.3794 1.3399 -0.0672 -0.0957 -0.0427 137  ASP   E OD2 
12478 N  N   . GLY   E 138 ? 1.5763 1.4077 1.3953 -0.0804 -0.1149 -0.0500 138  GLY   E N   
12479 C  CA  . GLY   E 138 ? 1.5045 1.3212 1.3171 -0.0829 -0.1179 -0.0516 138  GLY   E CA  
12480 C  C   . GLY   E 138 ? 1.5541 1.3637 1.3671 -0.0881 -0.1261 -0.0539 138  GLY   E C   
12481 O  O   . GLY   E 138 ? 1.5734 1.3694 1.3797 -0.0899 -0.1294 -0.0557 138  GLY   E O   
12482 N  N   . LEU   E 139 ? 1.5621 1.3802 1.3824 -0.0903 -0.1298 -0.0540 139  LEU   E N   
12483 C  CA  . LEU   E 139 ? 1.5225 1.3349 1.3448 -0.0953 -0.1382 -0.0563 139  LEU   E CA  
12484 C  C   . LEU   E 139 ? 1.4608 1.2722 1.2739 -0.0920 -0.1424 -0.0584 139  LEU   E C   
12485 O  O   . LEU   E 139 ? 1.4801 1.2982 1.2891 -0.0869 -0.1381 -0.0575 139  LEU   E O   
12486 C  CB  . LEU   E 139 ? 1.4922 1.3152 1.3344 -0.1023 -0.1399 -0.0545 139  LEU   E CB  
12487 C  CG  . LEU   E 139 ? 1.4770 1.2935 1.3268 -0.1084 -0.1413 -0.0543 139  LEU   E CG  
12488 C  CD1 . LEU   E 139 ? 1.4792 1.2878 1.3208 -0.1055 -0.1353 -0.0534 139  LEU   E CD1 
12489 C  CD2 . LEU   E 139 ? 1.4355 1.2652 1.3061 -0.1140 -0.1400 -0.0515 139  LEU   E CD2 
12490 N  N   . PHE   E 140 ? 1.3566 1.1593 1.1668 -0.0951 -0.1508 -0.0613 140  PHE   E N   
12491 C  CA  . PHE   E 140 ? 1.3613 1.1615 1.1627 -0.0925 -0.1559 -0.0634 140  PHE   E CA  
12492 C  C   . PHE   E 140 ? 1.3847 1.1837 1.1946 -0.0986 -0.1653 -0.0653 140  PHE   E C   
12493 O  O   . PHE   E 140 ? 1.4236 1.2103 1.2305 -0.1017 -0.1713 -0.0678 140  PHE   E O   
12494 C  CB  . PHE   E 140 ? 1.4000 1.1846 1.1796 -0.0865 -0.1568 -0.0660 140  PHE   E CB  
12495 C  CG  . PHE   E 140 ? 1.3927 1.1748 1.1607 -0.0821 -0.1597 -0.0676 140  PHE   E CG  
12496 C  CD1 . PHE   E 140 ? 1.4211 1.2156 1.1922 -0.0789 -0.1548 -0.0655 140  PHE   E CD1 
12497 C  CD2 . PHE   E 140 ? 1.3153 1.0817 1.0688 -0.0810 -0.1674 -0.0713 140  PHE   E CD2 
12498 C  CE1 . PHE   E 140 ? 1.4046 1.1960 1.1645 -0.0747 -0.1568 -0.0666 140  PHE   E CE1 
12499 C  CE2 . PHE   E 140 ? 1.3874 1.1504 1.1290 -0.0765 -0.1697 -0.0726 140  PHE   E CE2 
12500 C  CZ  . PHE   E 140 ? 1.4229 1.1982 1.1675 -0.0733 -0.1642 -0.0702 140  PHE   E CZ  
12501 N  N   . LYS   E 141 ? 1.3711 1.1824 1.1919 -0.1003 -0.1669 -0.0643 141  LYS   E N   
12502 C  CA  . LYS   E 141 ? 1.3678 1.1792 1.1976 -0.1057 -0.1762 -0.0661 141  LYS   E CA  
12503 C  C   . LYS   E 141 ? 1.3965 1.1963 1.2102 -0.1023 -0.1838 -0.0698 141  LYS   E C   
12504 O  O   . LYS   E 141 ? 1.3678 1.1668 1.1685 -0.0961 -0.1811 -0.0697 141  LYS   E O   
12505 C  CB  . LYS   E 141 ? 1.2590 1.0878 1.1069 -0.1088 -0.1751 -0.0636 141  LYS   E CB  
12506 N  N   . VAL   E 142 ? 1.4339 1.2247 1.2488 -0.1065 -0.1934 -0.0730 142  VAL   E N   
12507 C  CA  . VAL   E 142 ? 1.4593 1.2365 1.2584 -0.1037 -0.2022 -0.0770 142  VAL   E CA  
12508 C  C   . VAL   E 142 ? 1.4486 1.2304 1.2613 -0.1090 -0.2116 -0.0786 142  VAL   E C   
12509 O  O   . VAL   E 142 ? 1.4583 1.2404 1.2854 -0.1157 -0.2161 -0.0794 142  VAL   E O   
12510 C  CB  . VAL   E 142 ? 1.4319 1.1902 1.2163 -0.1028 -0.2057 -0.0801 142  VAL   E CB  
12511 C  CG1 . VAL   E 142 ? 1.4616 1.2047 1.2238 -0.0971 -0.2123 -0.0838 142  VAL   E CG1 
12512 C  CG2 . VAL   E 142 ? 1.3944 1.1517 1.1730 -0.0996 -0.1956 -0.0778 142  VAL   E CG2 
12513 N  N   . ILE   E 143 ? 1.3846 1.1709 1.1942 -0.1062 -0.2141 -0.0788 143  ILE   E N   
12514 C  CA  . ILE   E 143 ? 1.4416 1.2311 1.2621 -0.1103 -0.2240 -0.0808 143  ILE   E CA  
12515 C  C   . ILE   E 143 ? 1.5218 1.2936 1.3240 -0.1073 -0.2346 -0.0856 143  ILE   E C   
12516 O  O   . ILE   E 143 ? 1.5372 1.3059 1.3256 -0.1016 -0.2360 -0.0863 143  ILE   E O   
12517 C  CB  . ILE   E 143 ? 1.4559 1.2608 1.2847 -0.1092 -0.2213 -0.0782 143  ILE   E CB  
12518 C  CG1 . ILE   E 143 ? 1.3744 1.1958 1.2179 -0.1107 -0.2101 -0.0733 143  ILE   E CG1 
12519 C  CG2 . ILE   E 143 ? 1.4532 1.2621 1.2956 -0.1139 -0.2316 -0.0802 143  ILE   E CG2 
12520 C  CD1 . ILE   E 143 ? 1.3544 1.1859 1.1947 -0.1058 -0.2035 -0.0706 143  ILE   E CD1 
12521 N  N   . PRO   E 144 ? 1.5188 1.2782 1.3201 -0.1107 -0.2422 -0.0890 144  PRO   E N   
12522 C  CA  . PRO   E 144 ? 1.5713 1.3131 1.3550 -0.1078 -0.2534 -0.0940 144  PRO   E CA  
12523 C  C   . PRO   E 144 ? 1.6500 1.3960 1.4359 -0.1070 -0.2610 -0.0954 144  PRO   E C   
12524 O  O   . PRO   E 144 ? 1.5681 1.3284 1.3755 -0.1122 -0.2629 -0.0942 144  PRO   E O   
12525 C  CB  . PRO   E 144 ? 1.5180 1.2512 1.3102 -0.1142 -0.2610 -0.0971 144  PRO   E CB  
12526 C  CG  . PRO   E 144 ? 1.5377 1.2877 1.3570 -0.1216 -0.2559 -0.0936 144  PRO   E CG  
12527 C  CD  . PRO   E 144 ? 1.5179 1.2799 1.3370 -0.1182 -0.2423 -0.0886 144  PRO   E CD  
12528 N  N   . LEU   E 145 ? 1.7007 1.4339 1.4635 -0.1000 -0.2650 -0.0979 145  LEU   E N   
12529 C  CA  . LEU   E 145 ? 1.7153 1.4497 1.4747 -0.0974 -0.2717 -0.0992 145  LEU   E CA  
12530 C  C   . LEU   E 145 ? 1.8470 1.5666 1.6006 -0.0985 -0.2872 -0.1049 145  LEU   E C   
12531 O  O   . LEU   E 145 ? 1.8851 1.5875 1.6148 -0.0923 -0.2925 -0.1081 145  LEU   E O   
12532 C  CB  . LEU   E 145 ? 1.6914 1.4212 1.4283 -0.0883 -0.2650 -0.0977 145  LEU   E CB  
12533 C  CG  . LEU   E 145 ? 1.6724 1.4197 1.4176 -0.0871 -0.2519 -0.0922 145  LEU   E CG  
12534 C  CD1 . LEU   E 145 ? 1.6347 1.3763 1.3579 -0.0783 -0.2458 -0.0910 145  LEU   E CD1 
12535 C  CD2 . LEU   E 145 ? 1.6151 1.3804 1.3832 -0.0921 -0.2537 -0.0905 145  LEU   E CD2 
12536 N  N   . ASP   E 146 ? 1.9887 1.7148 1.7648 -0.1064 -0.2945 -0.1063 146  ASP   E N   
12537 C  CA  . ASP   E 146 ? 2.0181 1.7327 1.7938 -0.1085 -0.3101 -0.1119 146  ASP   E CA  
12538 C  C   . ASP   E 146 ? 2.0601 1.7866 1.8517 -0.1109 -0.3170 -0.1123 146  ASP   E C   
12539 O  O   . ASP   E 146 ? 2.0410 1.7867 1.8525 -0.1143 -0.3103 -0.1083 146  ASP   E O   
12540 C  CB  . ASP   E 146 ? 1.9781 1.6889 1.7677 -0.1159 -0.3145 -0.1139 146  ASP   E CB  
12541 C  CG  . ASP   E 146 ? 2.0284 1.7215 1.7978 -0.1128 -0.3124 -0.1155 146  ASP   E CG  
12542 O  OD1 . ASP   E 146 ? 2.0228 1.7075 1.7683 -0.1049 -0.3065 -0.1147 146  ASP   E OD1 
12543 O  OD2 . ASP   E 146 ? 2.1717 1.8589 1.9492 -0.1182 -0.3165 -0.1175 146  ASP   E OD2 
12544 N  N   . ARG   E 147 ? 2.0801 1.7944 1.8619 -0.1087 -0.3308 -0.1174 147  ARG   E N   
12545 C  CA  . ARG   E 147 ? 2.0595 1.7832 1.8523 -0.1094 -0.3378 -0.1181 147  ARG   E CA  
12546 C  C   . ARG   E 147 ? 2.0609 1.8026 1.8880 -0.1187 -0.3390 -0.1168 147  ARG   E C   
12547 O  O   . ARG   E 147 ? 1.9874 1.7435 1.8287 -0.1199 -0.3395 -0.1152 147  ARG   E O   
12548 C  CB  . ARG   E 147 ? 2.0883 1.7942 1.8653 -0.1057 -0.3538 -0.1243 147  ARG   E CB  
12549 N  N   . ASP   E 148 ? 2.1782 1.9192 2.0188 -0.1253 -0.3392 -0.1174 148  ASP   E N   
12550 C  CA  . ASP   E 148 ? 2.1682 1.9258 2.0417 -0.1342 -0.3395 -0.1159 148  ASP   E CA  
12551 C  C   . ASP   E 148 ? 2.1594 1.9357 2.0469 -0.1363 -0.3238 -0.1093 148  ASP   E C   
12552 O  O   . ASP   E 148 ? 2.1781 1.9711 2.0915 -0.1419 -0.3228 -0.1072 148  ASP   E O   
12553 C  CB  . ASP   E 148 ? 2.1271 1.8764 2.0105 -0.1408 -0.3457 -0.1191 148  ASP   E CB  
12554 N  N   . ASN   E 149 ? 1.9620 1.7362 1.8334 -0.1316 -0.3118 -0.1060 149  ASN   E N   
12555 C  CA  . ASN   E 149 ? 1.7847 1.5758 1.6694 -0.1335 -0.2975 -0.1000 149  ASN   E CA  
12556 C  C   . ASN   E 149 ? 1.7329 1.5388 1.6231 -0.1311 -0.2944 -0.0973 149  ASN   E C   
12557 O  O   . ASN   E 149 ? 1.6932 1.4982 1.5664 -0.1245 -0.2883 -0.0954 149  ASN   E O   
12558 C  CB  . ASN   E 149 ? 1.6899 1.4747 1.5566 -0.1290 -0.2861 -0.0976 149  ASN   E CB  
12559 C  CG  . ASN   E 149 ? 1.5144 1.3127 1.3979 -0.1332 -0.2738 -0.0926 149  ASN   E CG  
12560 O  OD1 . ASN   E 149 ? 1.5247 1.3379 1.4321 -0.1388 -0.2726 -0.0905 149  ASN   E OD1 
12561 N  ND2 . ASN   E 149 ? 1.4562 1.2488 1.3269 -0.1303 -0.2648 -0.0908 149  ASN   E ND2 
12562 N  N   . LYS   E 150 ? 1.6396 1.4587 1.5542 -0.1366 -0.2987 -0.0970 150  LYS   E N   
12563 C  CA  . LYS   E 150 ? 1.5681 1.4025 1.4908 -0.1352 -0.2953 -0.0940 150  LYS   E CA  
12564 C  C   . LYS   E 150 ? 1.5107 1.3623 1.4502 -0.1382 -0.2819 -0.0883 150  LYS   E C   
12565 O  O   . LYS   E 150 ? 1.4961 1.3581 1.4348 -0.1350 -0.2748 -0.0849 150  LYS   E O   
12566 C  CB  . LYS   E 150 ? 1.5705 1.4100 1.5094 -0.1385 -0.3075 -0.0969 150  LYS   E CB  
12567 N  N   . GLU   E 151 ? 1.4814 1.3353 1.4355 -0.1442 -0.2784 -0.0872 151  GLU   E N   
12568 C  CA  . GLU   E 151 ? 1.3843 1.2525 1.3527 -0.1468 -0.2657 -0.0819 151  GLU   E CA  
12569 C  C   . GLU   E 151 ? 1.4186 1.2816 1.3700 -0.1425 -0.2547 -0.0794 151  GLU   E C   
12570 O  O   . GLU   E 151 ? 1.4761 1.3487 1.4369 -0.1441 -0.2441 -0.0752 151  GLU   E O   
12571 C  CB  . GLU   E 151 ? 1.3641 1.2373 1.3571 -0.1551 -0.2666 -0.0815 151  GLU   E CB  
12572 N  N   . LEU   E 152 ? 1.4498 1.2975 1.3762 -0.1368 -0.2570 -0.0819 152  LEU   E N   
12573 C  CA  . LEU   E 152 ? 1.4230 1.2655 1.3318 -0.1318 -0.2469 -0.0798 152  LEU   E CA  
12574 C  C   . LEU   E 152 ? 1.3640 1.2050 1.2794 -0.1356 -0.2406 -0.0783 152  LEU   E C   
12575 O  O   . LEU   E 152 ? 1.3161 1.1613 1.2283 -0.1334 -0.2296 -0.0748 152  LEU   E O   
12576 C  CB  . LEU   E 152 ? 1.4119 1.2671 1.3197 -0.1277 -0.2373 -0.0757 152  LEU   E CB  
12577 C  CG  . LEU   E 152 ? 1.4566 1.3119 1.3547 -0.1230 -0.2420 -0.0769 152  LEU   E CG  
12578 C  CD1 . LEU   E 152 ? 1.3806 1.2527 1.2876 -0.1217 -0.2340 -0.0726 152  LEU   E CD1 
12579 C  CD2 . LEU   E 152 ? 1.3801 1.2193 1.2502 -0.1157 -0.2425 -0.0789 152  LEU   E CD2 
12580 N  N   . LYS   E 153 ? 1.4126 1.2469 1.3369 -0.1412 -0.2477 -0.0809 153  LYS   E N   
12581 C  CA  . LYS   E 153 ? 1.3772 1.2073 1.3061 -0.1448 -0.2427 -0.0799 153  LYS   E CA  
12582 C  C   . LYS   E 153 ? 1.4260 1.2432 1.3309 -0.1390 -0.2377 -0.0801 153  LYS   E C   
12583 O  O   . LYS   E 153 ? 1.4497 1.2542 1.3344 -0.1340 -0.2431 -0.0834 153  LYS   E O   
12584 C  CB  . LYS   E 153 ? 1.2612 1.0837 1.2010 -0.1513 -0.2530 -0.0836 153  LYS   E CB  
12585 N  N   . ALA   E 154 ? 1.3372 1.1573 1.2441 -0.1393 -0.2272 -0.0768 154  ALA   E N   
12586 C  CA  . ALA   E 154 ? 1.4187 1.2293 1.3046 -0.1333 -0.2208 -0.0763 154  ALA   E CA  
12587 C  C   . ALA   E 154 ? 1.4729 1.2778 1.3616 -0.1363 -0.2158 -0.0753 154  ALA   E C   
12588 O  O   . ALA   E 154 ? 1.5303 1.3400 1.4378 -0.1430 -0.2158 -0.0742 154  ALA   E O   
12589 C  CB  . ALA   E 154 ? 1.4922 1.3139 1.3738 -0.1279 -0.2108 -0.0726 154  ALA   E CB  
12590 N  N   . PHE   E 155 ? 1.4847 1.2790 1.3543 -0.1311 -0.2113 -0.0755 155  PHE   E N   
12591 C  CA  . PHE   E 155 ? 1.5091 1.2967 1.3777 -0.1326 -0.2059 -0.0744 155  PHE   E CA  
12592 C  C   . PHE   E 155 ? 1.4894 1.2777 1.3442 -0.1258 -0.1955 -0.0719 155  PHE   E C   
12593 O  O   . PHE   E 155 ? 1.4908 1.2773 1.3305 -0.1194 -0.1949 -0.0726 155  PHE   E O   
12594 C  CB  . PHE   E 155 ? 1.5399 1.3086 1.3986 -0.1342 -0.2141 -0.0788 155  PHE   E CB  
12595 C  CG  . PHE   E 155 ? 1.5264 1.2801 1.3587 -0.1269 -0.2172 -0.0819 155  PHE   E CG  
12596 C  CD1 . PHE   E 155 ? 1.5447 1.2944 1.3605 -0.1203 -0.2087 -0.0804 155  PHE   E CD1 
12597 C  CD2 . PHE   E 155 ? 1.5365 1.2796 1.3607 -0.1267 -0.2288 -0.0865 155  PHE   E CD2 
12598 C  CE1 . PHE   E 155 ? 1.5798 1.3155 1.3720 -0.1137 -0.2112 -0.0832 155  PHE   E CE1 
12599 C  CE2 . PHE   E 155 ? 1.5916 1.3198 1.3910 -0.1199 -0.2316 -0.0894 155  PHE   E CE2 
12600 C  CZ  . PHE   E 155 ? 1.5990 1.3236 1.3825 -0.1134 -0.2225 -0.0876 155  PHE   E CZ  
12601 N  N   . ASN   E 156 ? 1.4494 1.2403 1.3099 -0.1271 -0.1873 -0.0690 156  ASN   E N   
12602 C  CA  . ASN   E 156 ? 1.4675 1.2580 1.3159 -0.1209 -0.1780 -0.0669 156  ASN   E CA  
12603 C  C   . ASN   E 156 ? 1.5179 1.2905 1.3499 -0.1188 -0.1786 -0.0690 156  ASN   E C   
12604 O  O   . ASN   E 156 ? 1.6079 1.3691 1.4395 -0.1227 -0.1857 -0.0719 156  ASN   E O   
12605 C  CB  . ASN   E 156 ? 1.4696 1.2735 1.3328 -0.1227 -0.1688 -0.0623 156  ASN   E CB  
12606 C  CG  . ASN   E 156 ? 1.4323 1.2515 1.2998 -0.1196 -0.1643 -0.0599 156  ASN   E CG  
12607 O  OD1 . ASN   E 156 ? 1.4906 1.3090 1.3446 -0.1133 -0.1625 -0.0604 156  ASN   E OD1 
12608 N  ND2 . ASN   E 156 ? 1.5255 1.3586 1.4120 -0.1238 -0.1620 -0.0571 156  ASN   E ND2 
12609 N  N   . ILE   E 157 ? 1.4669 1.2368 1.2847 -0.1121 -0.1716 -0.0680 157  ILE   E N   
12610 C  CA  . ILE   E 157 ? 1.6274 1.3824 1.4313 -0.1097 -0.1696 -0.0691 157  ILE   E CA  
12611 C  C   . ILE   E 157 ? 1.5890 1.3488 1.3868 -0.1036 -0.1593 -0.0663 157  ILE   E C   
12612 O  O   . ILE   E 157 ? 1.5816 1.3519 1.3786 -0.0993 -0.1552 -0.0648 157  ILE   E O   
12613 C  CB  . ILE   E 157 ? 1.7011 1.4392 1.4859 -0.1065 -0.1771 -0.0736 157  ILE   E CB  
12614 C  CG1 . ILE   E 157 ? 1.5261 1.2627 1.2932 -0.0979 -0.1741 -0.0740 157  ILE   E CG1 
12615 C  CG2 . ILE   E 157 ? 1.6509 1.3882 1.4405 -0.1103 -0.1878 -0.0765 157  ILE   E CG2 
12616 C  CD1 . ILE   E 157 ? 1.7285 1.4484 1.4767 -0.0948 -0.1826 -0.0785 157  ILE   E CD1 
12617 N  N   . ARG   E 158 ? 1.6225 1.3744 1.4163 -0.1033 -0.1551 -0.0656 158  ARG   E N   
12618 C  CA  . ARG   E 158 ? 1.6028 1.3598 1.3938 -0.0984 -0.1457 -0.0628 158  ARG   E CA  
12619 C  C   . ARG   E 158 ? 1.6494 1.4030 1.4229 -0.0900 -0.1437 -0.0641 158  ARG   E C   
12620 O  O   . ARG   E 158 ? 1.6669 1.4078 1.4258 -0.0876 -0.1486 -0.0672 158  ARG   E O   
12621 C  CB  . ARG   E 158 ? 1.6795 1.4267 1.4687 -0.0998 -0.1426 -0.0622 158  ARG   E CB  
12622 N  N   . LEU   E 159 ? 1.6543 1.4193 1.4298 -0.0855 -0.1363 -0.0615 159  LEU   E N   
12623 C  CA  . LEU   E 159 ? 1.6760 1.4404 1.4378 -0.0774 -0.1326 -0.0621 159  LEU   E CA  
12624 C  C   . LEU   E 159 ? 1.6768 1.4426 1.4365 -0.0732 -0.1247 -0.0601 159  LEU   E C   
12625 O  O   . LEU   E 159 ? 1.5912 1.3702 1.3619 -0.0730 -0.1195 -0.0574 159  LEU   E O   
12626 C  CB  . LEU   E 159 ? 1.5079 1.2860 1.2752 -0.0759 -0.1318 -0.0611 159  LEU   E CB  
12627 N  N   . GLU   E 160 ? 1.7007 1.4522 1.4456 -0.0694 -0.1241 -0.0618 160  GLU   E N   
12628 C  CA  . GLU   E 160 ? 1.6654 1.4160 1.4072 -0.0653 -0.1174 -0.0603 160  GLU   E CA  
12629 C  C   . GLU   E 160 ? 1.6472 1.4108 1.3909 -0.0593 -0.1113 -0.0587 160  GLU   E C   
12630 O  O   . GLU   E 160 ? 1.6349 1.4057 1.3849 -0.0578 -0.1060 -0.0565 160  GLU   E O   
12631 C  CB  . GLU   E 160 ? 1.6687 1.4013 1.3927 -0.0616 -0.1184 -0.0627 160  GLU   E CB  
12632 N  N   . GLU   E 161 ? 1.6638 1.4302 1.4021 -0.0556 -0.1119 -0.0598 161  GLU   E N   
12633 C  CA  . GLU   E 161 ? 1.6411 1.4212 1.3836 -0.0508 -0.1064 -0.0582 161  GLU   E CA  
12634 C  C   . GLU   E 161 ? 1.6410 1.4370 1.4015 -0.0555 -0.1060 -0.0558 161  GLU   E C   
12635 O  O   . GLU   E 161 ? 1.6683 1.4678 1.4343 -0.0598 -0.1104 -0.0560 161  GLU   E O   
12636 C  CB  . GLU   E 161 ? 1.6009 1.3788 1.3330 -0.0461 -0.1070 -0.0598 161  GLU   E CB  
12637 N  N   . LEU   E 162 ? 1.6184 1.4237 1.3876 -0.0545 -0.1009 -0.0535 162  LEU   E N   
12638 C  CA  . LEU   E 162 ? 1.5949 1.4139 1.3807 -0.0591 -0.1003 -0.0511 162  LEU   E CA  
12639 C  C   . LEU   E 162 ? 1.5807 1.4145 1.3733 -0.0561 -0.0972 -0.0499 162  LEU   E C   
12640 O  O   . LEU   E 162 ? 1.5787 1.4245 1.3847 -0.0592 -0.0963 -0.0478 162  LEU   E O   
12641 C  CB  . LEU   E 162 ? 1.5990 1.4186 1.3905 -0.0601 -0.0969 -0.0492 162  LEU   E CB  
12642 C  CG  . LEU   E 162 ? 1.5385 1.3518 1.3353 -0.0672 -0.0998 -0.0486 162  LEU   E CG  
12643 C  CD1 . LEU   E 162 ? 1.6090 1.4309 1.4184 -0.0734 -0.1036 -0.0479 162  LEU   E CD1 
12644 C  CD2 . LEU   E 162 ? 1.5972 1.3933 1.3814 -0.0678 -0.1035 -0.0511 162  LEU   E CD2 
12645 N  N   . HIS   E 163 ? 1.5716 1.4048 1.3555 -0.0501 -0.0952 -0.0510 163  HIS   E N   
12646 C  CA  . HIS   E 163 ? 1.5735 1.4201 1.3636 -0.0468 -0.0916 -0.0499 163  HIS   E CA  
12647 C  C   . HIS   E 163 ? 1.5537 1.3965 1.3339 -0.0435 -0.0924 -0.0515 163  HIS   E C   
12648 O  O   . HIS   E 163 ? 1.5285 1.3680 1.3000 -0.0373 -0.0889 -0.0524 163  HIS   E O   
12649 C  CB  . HIS   E 163 ? 1.5742 1.4263 1.3663 -0.0415 -0.0859 -0.0491 163  HIS   E CB  
12650 C  CG  . HIS   E 163 ? 1.6529 1.5049 1.4504 -0.0435 -0.0849 -0.0477 163  HIS   E CG  
12651 N  ND1 . HIS   E 163 ? 1.7166 1.5771 1.5270 -0.0486 -0.0855 -0.0457 163  HIS   E ND1 
12652 C  CD2 . HIS   E 163 ? 1.6856 1.5296 1.4768 -0.0406 -0.0829 -0.0480 163  HIS   E CD2 
12653 C  CE1 . HIS   E 163 ? 1.6896 1.5469 1.5010 -0.0488 -0.0837 -0.0447 163  HIS   E CE1 
12654 N  NE2 . HIS   E 163 ? 1.6923 1.5396 1.4921 -0.0440 -0.0822 -0.0461 163  HIS   E NE2 
12655 N  N   . VAL   E 164 ? 1.4947 1.3378 1.2764 -0.0474 -0.0969 -0.0519 164  VAL   E N   
12656 C  CA  . VAL   E 164 ? 1.4511 1.2890 1.2224 -0.0447 -0.0983 -0.0533 164  VAL   E CA  
12657 C  C   . VAL   E 164 ? 1.3939 1.2452 1.1728 -0.0430 -0.0951 -0.0518 164  VAL   E C   
12658 O  O   . VAL   E 164 ? 1.3834 1.2455 1.1751 -0.0473 -0.0964 -0.0503 164  VAL   E O   
12659 C  CB  . VAL   E 164 ? 1.4387 1.2677 1.2060 -0.0496 -0.1059 -0.0549 164  VAL   E CB  
12660 C  CG1 . VAL   E 164 ? 1.3830 1.2009 1.1341 -0.0454 -0.1073 -0.0570 164  VAL   E CG1 
12661 C  CG2 . VAL   E 164 ? 1.5166 1.3366 1.2836 -0.0536 -0.1091 -0.0557 164  VAL   E CG2 
12662 N  N   . ILE   E 165 ? 1.3663 1.2166 1.1375 -0.0368 -0.0908 -0.0522 165  ILE   E N   
12663 C  CA  . ILE   E 165 ? 1.3831 1.2445 1.1601 -0.0350 -0.0874 -0.0508 165  ILE   E CA  
12664 C  C   . ILE   E 165 ? 1.3863 1.2447 1.1594 -0.0374 -0.0920 -0.0513 165  ILE   E C   
12665 O  O   . ILE   E 165 ? 1.4273 1.2957 1.2113 -0.0412 -0.0935 -0.0500 165  ILE   E O   
12666 C  CB  . ILE   E 165 ? 1.4025 1.2635 1.1731 -0.0275 -0.0809 -0.0510 165  ILE   E CB  
12667 C  CG1 . ILE   E 165 ? 1.4144 1.2755 1.1862 -0.0243 -0.0773 -0.0511 165  ILE   E CG1 
12668 C  CG2 . ILE   E 165 ? 1.3484 1.2225 1.1280 -0.0260 -0.0766 -0.0492 165  ILE   E CG2 
12669 C  CD1 . ILE   E 165 ? 1.4417 1.3113 1.2266 -0.0280 -0.0779 -0.0499 165  ILE   E CD1 
12670 N  N   . ASP   E 166 ? 1.3244 1.1683 1.0814 -0.0352 -0.0947 -0.0533 166  ASP   E N   
12671 C  CA  . ASP   E 166 ? 1.3490 1.1886 1.0996 -0.0361 -0.0988 -0.0540 166  ASP   E CA  
12672 C  C   . ASP   E 166 ? 1.3480 1.1694 1.0818 -0.0356 -0.1045 -0.0568 166  ASP   E C   
12673 O  O   . ASP   E 166 ? 1.3410 1.1519 1.0620 -0.0308 -0.1021 -0.0580 166  ASP   E O   
12674 C  CB  . ASP   E 166 ? 1.4111 1.2548 1.1584 -0.0307 -0.0928 -0.0529 166  ASP   E CB  
12675 C  CG  . ASP   E 166 ? 1.3894 1.2267 1.1274 -0.0305 -0.0965 -0.0535 166  ASP   E CG  
12676 O  OD1 . ASP   E 166 ? 1.3299 1.1650 1.0695 -0.0354 -0.1039 -0.0544 166  ASP   E OD1 
12677 O  OD2 . ASP   E 166 ? 1.4065 1.2410 1.1356 -0.0250 -0.0917 -0.0531 166  ASP   E OD2 
12678 N  N   . VAL   E 167 ? 1.3693 1.1867 1.1030 -0.0402 -0.1121 -0.0579 167  VAL   E N   
12679 C  CA  . VAL   E 167 ? 1.3542 1.1545 1.0733 -0.0405 -0.1190 -0.0608 167  VAL   E CA  
12680 C  C   . VAL   E 167 ? 1.3912 1.1860 1.1009 -0.0391 -0.1230 -0.0618 167  VAL   E C   
12681 O  O   . VAL   E 167 ? 1.4252 1.2303 1.1421 -0.0394 -0.1213 -0.0601 167  VAL   E O   
12682 C  CB  . VAL   E 167 ? 1.3095 1.1086 1.0375 -0.0476 -0.1256 -0.0617 167  VAL   E CB  
12683 C  CG1 . VAL   E 167 ? 1.1567 0.9703 0.9026 -0.0532 -0.1276 -0.0600 167  VAL   E CG1 
12684 C  CG2 . VAL   E 167 ? 1.3844 1.1661 1.0989 -0.0486 -0.1341 -0.0651 167  VAL   E CG2 
12685 N  N   . LYS   E 168 ? 1.4228 1.2004 1.1155 -0.0372 -0.1283 -0.0646 168  LYS   E N   
12686 C  CA  . LYS   E 168 ? 1.4144 1.1847 1.0961 -0.0354 -0.1328 -0.0658 168  LYS   E CA  
12687 C  C   . LYS   E 168 ? 1.4621 1.2118 1.1247 -0.0335 -0.1394 -0.0694 168  LYS   E C   
12688 O  O   . LYS   E 168 ? 1.4916 1.2321 1.1439 -0.0298 -0.1363 -0.0702 168  LYS   E O   
12689 C  CB  . LYS   E 168 ? 1.3475 1.1214 1.0232 -0.0291 -0.1248 -0.0639 168  LYS   E CB  
12690 N  N   . PHE   E 169 ? 1.4908 1.2330 1.1491 -0.0361 -0.1488 -0.0716 169  PHE   E N   
12691 C  CA  . PHE   E 169 ? 1.4834 1.2051 1.1228 -0.0342 -0.1563 -0.0754 169  PHE   E CA  
12692 C  C   . PHE   E 169 ? 1.5083 1.2172 1.1250 -0.0252 -0.1516 -0.0758 169  PHE   E C   
12693 O  O   . PHE   E 169 ? 1.4704 1.1844 1.0846 -0.0211 -0.1458 -0.0738 169  PHE   E O   
12694 C  CB  . PHE   E 169 ? 1.4782 1.1958 1.1183 -0.0382 -0.1676 -0.0777 169  PHE   E CB  
12695 C  CG  . PHE   E 169 ? 1.4796 1.2017 1.1363 -0.0467 -0.1747 -0.0788 169  PHE   E CG  
12696 C  CD1 . PHE   E 169 ? 1.5709 1.2801 1.2220 -0.0486 -0.1803 -0.0817 169  PHE   E CD1 
12697 C  CD2 . PHE   E 169 ? 1.5164 1.2552 1.1943 -0.0526 -0.1759 -0.0769 169  PHE   E CD2 
12698 C  CE1 . PHE   E 169 ? 1.5772 1.2902 1.2442 -0.0565 -0.1865 -0.0825 169  PHE   E CE1 
12699 C  CE2 . PHE   E 169 ? 1.5127 1.2555 1.2064 -0.0603 -0.1819 -0.0778 169  PHE   E CE2 
12700 C  CZ  . PHE   E 169 ? 1.5791 1.3090 1.2676 -0.0623 -0.1871 -0.0805 169  PHE   E CZ  
12701 N  N   . LEU   E 170 ? 1.5752 1.2663 1.1746 -0.0221 -0.1544 -0.0786 170  LEU   E N   
12702 C  CA  . LEU   E 170 ? 1.5438 1.2215 1.1209 -0.0132 -0.1494 -0.0790 170  LEU   E CA  
12703 C  C   . LEU   E 170 ? 1.5186 1.1793 1.0763 -0.0102 -0.1576 -0.0819 170  LEU   E C   
12704 O  O   . LEU   E 170 ? 1.5061 1.1606 1.0646 -0.0149 -0.1688 -0.0847 170  LEU   E O   
12705 C  CB  . LEU   E 170 ? 1.5950 1.2627 1.1629 -0.0102 -0.1465 -0.0800 170  LEU   E CB  
12706 C  CG  . LEU   E 170 ? 1.6058 1.2850 1.1796 -0.0061 -0.1338 -0.0767 170  LEU   E CG  
12707 C  CD1 . LEU   E 170 ? 1.5250 1.1957 1.0910 -0.0030 -0.1304 -0.0776 170  LEU   E CD1 
12708 C  CD2 . LEU   E 170 ? 1.6561 1.3336 1.2184 0.0010  -0.1272 -0.0751 170  LEU   E CD2 
12709 N  N   . TYR   E 171 ? 1.5673 1.2204 1.1079 -0.0023 -0.1519 -0.0811 171  TYR   E N   
12710 C  CA  . TYR   E 171 ? 1.6472 1.2829 1.1667 0.0019  -0.1586 -0.0836 171  TYR   E CA  
12711 C  C   . TYR   E 171 ? 1.7638 1.3769 1.2602 0.0068  -0.1620 -0.0869 171  TYR   E C   
12712 O  O   . TYR   E 171 ? 1.7934 1.4042 1.2870 0.0092  -0.1560 -0.0865 171  TYR   E O   
12713 C  CB  . TYR   E 171 ? 1.6747 1.3124 1.1862 0.0083  -0.1502 -0.0808 171  TYR   E CB  
12714 C  CG  . TYR   E 171 ? 1.6389 1.2909 1.1644 0.0047  -0.1514 -0.0788 171  TYR   E CG  
12715 C  CD1 . TYR   E 171 ? 1.6605 1.3067 1.1831 0.0020  -0.1629 -0.0813 171  TYR   E CD1 
12716 C  CD2 . TYR   E 171 ? 1.6254 1.2960 1.1663 0.0044  -0.1411 -0.0747 171  TYR   E CD2 
12717 C  CE1 . TYR   E 171 ? 1.7227 1.3817 1.2575 -0.0009 -0.1638 -0.0795 171  TYR   E CE1 
12718 C  CE2 . TYR   E 171 ? 1.6036 1.2865 1.1564 0.0014  -0.1419 -0.0728 171  TYR   E CE2 
12719 C  CZ  . TYR   E 171 ? 1.6109 1.2880 1.1604 -0.0011 -0.1531 -0.0751 171  TYR   E CZ  
12720 O  OH  . TYR   E 171 ? 1.3128 1.0020 0.8739 -0.0039 -0.1538 -0.0733 171  TYR   E OH  
12721 N  N   . GLY   E 172 ? 1.6821 1.2781 1.1618 0.0083  -0.1724 -0.0905 172  GLY   E N   
12722 C  CA  . GLY   E 172 ? 1.8749 1.4472 1.3298 0.0137  -0.1765 -0.0940 172  GLY   E CA  
12723 C  C   . GLY   E 172 ? 1.9990 1.5667 1.4563 0.0110  -0.1782 -0.0957 172  GLY   E C   
12724 O  O   . GLY   E 172 ? 2.0166 1.5754 1.4606 0.0169  -0.1715 -0.0955 172  GLY   E O   
12725 N  N   . CYS   E 173 ? 2.0057 1.5787 1.4794 0.0022  -0.1871 -0.0975 173  CYS   E N   
12726 C  CA  . CYS   E 173 ? 1.9773 1.5464 1.4551 -0.0014 -0.1891 -0.0990 173  CYS   E CA  
12727 C  C   . CYS   E 173 ? 1.9617 1.5196 1.4391 -0.0070 -0.2041 -0.1036 173  CYS   E C   
12728 O  O   . CYS   E 173 ? 1.9582 1.5210 1.4443 -0.0113 -0.2119 -0.1045 173  CYS   E O   
12729 C  CB  . CYS   E 173 ? 1.9252 1.5165 1.4294 -0.0073 -0.1819 -0.0955 173  CYS   E CB  
12730 S  SG  . CYS   E 173 ? 1.9913 1.5908 1.4946 -0.0007 -0.1653 -0.0915 173  CYS   E SG  
12731 N  N   . GLN   E 174 ? 1.9329 1.4756 1.4003 -0.0068 -0.2082 -0.1065 174  GLN   E N   
12732 C  CA  . GLN   E 174 ? 1.9095 1.4404 1.3766 -0.0122 -0.2224 -0.1111 174  GLN   E CA  
12733 C  C   . GLN   E 174 ? 1.8911 1.4389 1.3861 -0.0225 -0.2282 -0.1106 174  GLN   E C   
12734 O  O   . GLN   E 174 ? 1.8523 1.3990 1.3497 -0.0250 -0.2379 -0.1128 174  GLN   E O   
12735 C  CB  . GLN   E 174 ? 1.8785 1.3964 1.3385 -0.0125 -0.2234 -0.1132 174  GLN   E CB  
12736 C  CG  . GLN   E 174 ? 1.9286 1.4617 1.4048 -0.0149 -0.2123 -0.1094 174  GLN   E CG  
12737 C  CD  . GLN   E 174 ? 1.8492 1.3696 1.3192 -0.0154 -0.2133 -0.1113 174  GLN   E CD  
12738 O  OE1 . GLN   E 174 ? 1.9245 1.4248 1.3706 -0.0090 -0.2149 -0.1139 174  GLN   E OE1 
12739 N  NE2 . GLN   E 174 ? 1.7658 1.2974 1.2565 -0.0229 -0.2120 -0.1099 174  GLN   E NE2 
12740 N  N   . ALA   E 175 ? 1.8745 1.4374 1.3904 -0.0283 -0.2225 -0.1080 175  ALA   E N   
12741 C  CA  . ALA   E 175 ? 1.7948 1.3752 1.3382 -0.0377 -0.2258 -0.1068 175  ALA   E CA  
12742 C  C   . ALA   E 175 ? 1.8098 1.4124 1.3685 -0.0378 -0.2153 -0.1018 175  ALA   E C   
12743 O  O   . ALA   E 175 ? 1.8136 1.4184 1.3632 -0.0311 -0.2052 -0.0993 175  ALA   E O   
12744 C  CB  . ALA   E 175 ? 1.7648 1.3457 1.3211 -0.0445 -0.2271 -0.1072 175  ALA   E CB  
12745 N  N   . PRO   E 176 ? 1.7563 1.3758 1.3388 -0.0453 -0.2175 -0.1003 176  PRO   E N   
12746 C  CA  . PRO   E 176 ? 1.7063 1.3471 1.3045 -0.0458 -0.2077 -0.0957 176  PRO   E CA  
12747 C  C   . PRO   E 176 ? 1.6881 1.3364 1.2918 -0.0449 -0.1965 -0.0926 176  PRO   E C   
12748 O  O   . PRO   E 176 ? 1.6896 1.3367 1.3010 -0.0494 -0.1973 -0.0930 176  PRO   E O   
12749 C  CB  . PRO   E 176 ? 1.6900 1.3444 1.3122 -0.0547 -0.2139 -0.0954 176  PRO   E CB  
12750 C  CG  . PRO   E 176 ? 1.7153 1.3548 1.3297 -0.0564 -0.2276 -0.1002 176  PRO   E CG  
12751 C  CD  . PRO   E 176 ? 1.7677 1.3870 1.3630 -0.0530 -0.2296 -0.1031 176  PRO   E CD  
12752 N  N   . THR   E 177 ? 1.6441 1.3002 1.2444 -0.0392 -0.1861 -0.0895 177  THR   E N   
12753 C  CA  . THR   E 177 ? 1.6594 1.3215 1.2623 -0.0367 -0.1754 -0.0869 177  THR   E CA  
12754 C  C   . THR   E 177 ? 1.6439 1.3262 1.2608 -0.0360 -0.1660 -0.0826 177  THR   E C   
12755 O  O   . THR   E 177 ? 1.5865 1.2721 1.1989 -0.0323 -0.1638 -0.0816 177  THR   E O   
12756 C  CB  . THR   E 177 ? 1.6500 1.2957 1.2287 -0.0281 -0.1715 -0.0881 177  THR   E CB  
12757 O  OG1 . THR   E 177 ? 1.7925 1.4177 1.3541 -0.0272 -0.1815 -0.0924 177  THR   E OG1 
12758 C  CG2 . THR   E 177 ? 1.7033 1.3502 1.2844 -0.0271 -0.1645 -0.0869 177  THR   E CG2 
12759 N  N   . ILE   E 178 ? 1.6189 1.3138 1.2518 -0.0392 -0.1603 -0.0802 178  ILE   E N   
12760 C  CA  . ILE   E 178 ? 1.5720 1.2857 1.2187 -0.0387 -0.1517 -0.0764 178  ILE   E CA  
12761 C  C   . ILE   E 178 ? 1.5793 1.2929 1.2189 -0.0321 -0.1417 -0.0749 178  ILE   E C   
12762 O  O   . ILE   E 178 ? 1.5588 1.2596 1.1861 -0.0291 -0.1413 -0.0765 178  ILE   E O   
12763 C  CB  . ILE   E 178 ? 1.5343 1.2636 1.2050 -0.0467 -0.1524 -0.0746 178  ILE   E CB  
12764 C  CG1 . ILE   E 178 ? 1.4800 1.2048 1.1542 -0.0497 -0.1526 -0.0751 178  ILE   E CG1 
12765 C  CG2 . ILE   E 178 ? 1.5019 1.2316 1.1796 -0.0525 -0.1620 -0.0761 178  ILE   E CG2 
12766 C  CD1 . ILE   E 178 ? 1.5331 1.2584 1.2029 -0.0446 -0.1435 -0.0736 178  ILE   E CD1 
12767 N  N   . CYS   E 179 ? 1.5598 1.2878 1.2074 -0.0297 -0.1338 -0.0720 179  CYS   E N   
12768 C  CA  . CYS   E 179 ? 1.4992 1.2297 1.1430 -0.0233 -0.1240 -0.0704 179  CYS   E CA  
12769 C  C   . CYS   E 179 ? 1.4623 1.2135 1.1267 -0.0257 -0.1180 -0.0671 179  CYS   E C   
12770 O  O   . CYS   E 179 ? 1.4378 1.1998 1.1106 -0.0271 -0.1175 -0.0656 179  CYS   E O   
12771 C  CB  . CYS   E 179 ? 1.5077 1.2306 1.1346 -0.0157 -0.1202 -0.0706 179  CYS   E CB  
12772 S  SG  . CYS   E 179 ? 1.4835 1.2105 1.1076 -0.0078 -0.1078 -0.0686 179  CYS   E SG  
12773 N  N   . PHE   E 180 ? 1.4539 1.2101 1.1259 -0.0262 -0.1141 -0.0662 180  PHE   E N   
12774 C  CA  . PHE   E 180 ? 1.3988 1.1736 1.0901 -0.0286 -0.1093 -0.0633 180  PHE   E CA  
12775 C  C   . PHE   E 180 ? 1.4166 1.1954 1.1081 -0.0231 -0.1010 -0.0622 180  PHE   E C   
12776 O  O   . PHE   E 180 ? 1.4929 1.2600 1.1721 -0.0192 -0.0998 -0.0636 180  PHE   E O   
12777 C  CB  . PHE   E 180 ? 1.3853 1.1649 1.0905 -0.0362 -0.1140 -0.0631 180  PHE   E CB  
12778 C  CG  . PHE   E 180 ? 1.4395 1.2094 1.1403 -0.0368 -0.1149 -0.0643 180  PHE   E CG  
12779 C  CD1 . PHE   E 180 ? 1.4775 1.2525 1.1826 -0.0342 -0.1085 -0.0629 180  PHE   E CD1 
12780 C  CD2 . PHE   E 180 ? 1.4787 1.2339 1.1710 -0.0398 -0.1223 -0.0668 180  PHE   E CD2 
12781 C  CE1 . PHE   E 180 ? 1.5203 1.2858 1.2208 -0.0345 -0.1091 -0.0638 180  PHE   E CE1 
12782 C  CE2 . PHE   E 180 ? 1.5981 1.3439 1.2864 -0.0404 -0.1228 -0.0678 180  PHE   E CE2 
12783 C  CZ  . PHE   E 180 ? 1.6499 1.4007 1.3419 -0.0377 -0.1160 -0.0662 180  PHE   E CZ  
12784 N  N   . VAL   E 181 ? 1.3940 1.1892 1.0995 -0.0227 -0.0954 -0.0598 181  VAL   E N   
12785 C  CA  . VAL   E 181 ? 1.3879 1.1903 1.0986 -0.0186 -0.0882 -0.0586 181  VAL   E CA  
12786 C  C   . VAL   E 181 ? 1.4043 1.2155 1.1297 -0.0234 -0.0890 -0.0574 181  VAL   E C   
12787 O  O   . VAL   E 181 ? 1.4533 1.2733 1.1908 -0.0291 -0.0920 -0.0563 181  VAL   E O   
12788 C  CB  . VAL   E 181 ? 1.3379 1.1524 1.0548 -0.0147 -0.0815 -0.0567 181  VAL   E CB  
12789 C  CG1 . VAL   E 181 ? 1.3150 1.1418 1.0444 -0.0128 -0.0759 -0.0553 181  VAL   E CG1 
12790 C  CG2 . VAL   E 181 ? 1.3699 1.1745 1.0708 -0.0081 -0.0782 -0.0576 181  VAL   E CG2 
12791 N  N   . TYR   E 182 ? 1.4262 1.2348 1.1503 -0.0209 -0.0863 -0.0577 182  TYR   E N   
12792 C  CA  . TYR   E 182 ? 1.4424 1.2577 1.1785 -0.0247 -0.0866 -0.0565 182  TYR   E CA  
12793 C  C   . TYR   E 182 ? 1.4777 1.2980 1.2164 -0.0193 -0.0805 -0.0559 182  TYR   E C   
12794 O  O   . TYR   E 182 ? 1.4760 1.2908 1.2051 -0.0130 -0.0769 -0.0569 182  TYR   E O   
12795 C  CB  . TYR   E 182 ? 1.4924 1.2953 1.2234 -0.0290 -0.0919 -0.0578 182  TYR   E CB  
12796 C  CG  . TYR   E 182 ? 1.5297 1.3166 1.2441 -0.0245 -0.0918 -0.0599 182  TYR   E CG  
12797 C  CD1 . TYR   E 182 ? 1.5199 1.2963 1.2193 -0.0203 -0.0923 -0.0616 182  TYR   E CD1 
12798 C  CD2 . TYR   E 182 ? 1.5415 1.3229 1.2545 -0.0242 -0.0910 -0.0600 182  TYR   E CD2 
12799 C  CE1 . TYR   E 182 ? 1.5328 1.2942 1.2166 -0.0160 -0.0921 -0.0635 182  TYR   E CE1 
12800 C  CE2 . TYR   E 182 ? 1.5931 1.3597 1.2908 -0.0201 -0.0909 -0.0619 182  TYR   E CE2 
12801 C  CZ  . TYR   E 182 ? 1.5622 1.3190 1.2455 -0.0160 -0.0915 -0.0637 182  TYR   E CZ  
12802 O  OH  . TYR   E 182 ? 1.7329 1.4745 1.4006 -0.0116 -0.0913 -0.0655 182  TYR   E OH  
12803 N  N   . GLN   E 183 ? 1.5312 1.3615 1.2830 -0.0217 -0.0794 -0.0544 183  GLN   E N   
12804 C  CA  . GLN   E 183 ? 1.5237 1.3587 1.2788 -0.0169 -0.0747 -0.0539 183  GLN   E CA  
12805 C  C   . GLN   E 183 ? 1.5520 1.3805 1.3063 -0.0193 -0.0766 -0.0539 183  GLN   E C   
12806 O  O   . GLN   E 183 ? 1.5550 1.3843 1.3156 -0.0256 -0.0799 -0.0530 183  GLN   E O   
12807 C  CB  . GLN   E 183 ? 1.5249 1.3774 1.2955 -0.0167 -0.0716 -0.0521 183  GLN   E CB  
12808 C  CG  . GLN   E 183 ? 1.5660 1.4243 1.3409 -0.0113 -0.0672 -0.0519 183  GLN   E CG  
12809 C  CD  . GLN   E 183 ? 1.6269 1.5007 1.4141 -0.0091 -0.0636 -0.0509 183  GLN   E CD  
12810 O  OE1 . GLN   E 183 ? 1.5911 1.4667 1.3761 -0.0052 -0.0605 -0.0513 183  GLN   E OE1 
12811 N  NE2 . GLN   E 183 ? 1.7200 1.6048 1.5202 -0.0116 -0.0638 -0.0494 183  GLN   E NE2 
12812 N  N   . ASP   E 184 ? 1.5610 1.3819 1.3071 -0.0142 -0.0743 -0.0549 184  ASP   E N   
12813 C  CA  . ASP   E 184 ? 1.6268 1.4423 1.3722 -0.0149 -0.0746 -0.0546 184  ASP   E CA  
12814 C  C   . ASP   E 184 ? 1.6949 1.5145 1.4407 -0.0077 -0.0700 -0.0548 184  ASP   E C   
12815 O  O   . ASP   E 184 ? 1.6952 1.5203 1.4412 -0.0026 -0.0668 -0.0553 184  ASP   E O   
12816 C  CB  . ASP   E 184 ? 1.5719 1.3695 1.3035 -0.0164 -0.0780 -0.0562 184  ASP   E CB  
12817 C  CG  . ASP   E 184 ? 1.6773 1.4645 1.3941 -0.0099 -0.0765 -0.0583 184  ASP   E CG  
12818 O  OD1 . ASP   E 184 ? 1.6878 1.4818 1.4056 -0.0038 -0.0722 -0.0583 184  ASP   E OD1 
12819 O  OD2 . ASP   E 184 ? 1.7804 1.5525 1.4847 -0.0108 -0.0797 -0.0599 184  ASP   E OD2 
12820 N  N   . PRO   E 185 ? 1.7181 1.5350 1.4643 -0.0069 -0.0694 -0.0543 185  PRO   E N   
12821 C  CA  . PRO   E 185 ? 1.6838 1.5044 1.4307 0.0002  -0.0656 -0.0546 185  PRO   E CA  
12822 C  C   . PRO   E 185 ? 1.7773 1.5954 1.5166 0.0073  -0.0629 -0.0564 185  PRO   E C   
12823 O  O   . PRO   E 185 ? 1.7252 1.5537 1.4715 0.0123  -0.0596 -0.0564 185  PRO   E O   
12824 C  CB  . PRO   E 185 ? 1.6247 1.4338 1.3647 0.0002  -0.0665 -0.0546 185  PRO   E CB  
12825 C  CG  . PRO   E 185 ? 1.5920 1.4004 1.3372 -0.0082 -0.0695 -0.0531 185  PRO   E CG  
12826 C  CD  . PRO   E 185 ? 1.6643 1.4745 1.4107 -0.0126 -0.0720 -0.0534 185  PRO   E CD  
12827 N  N   . GLN   E 186 ? 1.8883 1.6927 1.6137 0.0079  -0.0642 -0.0578 186  GLN   E N   
12828 C  CA  . GLN   E 186 ? 1.8879 1.6875 1.6039 0.0151  -0.0612 -0.0594 186  GLN   E CA  
12829 C  C   . GLN   E 186 ? 1.8678 1.6787 1.5904 0.0171  -0.0583 -0.0591 186  GLN   E C   
12830 O  O   . GLN   E 186 ? 1.8505 1.6651 1.5734 0.0238  -0.0541 -0.0597 186  GLN   E O   
12831 C  CB  . GLN   E 186 ? 1.8992 1.6809 1.5983 0.0146  -0.0637 -0.0610 186  GLN   E CB  
12832 C  CG  . GLN   E 186 ? 1.9695 1.7377 1.6598 0.0139  -0.0659 -0.0616 186  GLN   E CG  
12833 C  CD  . GLN   E 186 ? 2.0576 1.8080 1.7307 0.0143  -0.0683 -0.0635 186  GLN   E CD  
12834 O  OE1 . GLN   E 186 ? 2.0391 1.7870 1.7060 0.0160  -0.0681 -0.0644 186  GLN   E OE1 
12835 N  NE2 . GLN   E 186 ? 2.1255 1.8626 1.7903 0.0129  -0.0706 -0.0641 186  GLN   E NE2 
12836 N  N   . GLY   E 187 ? 1.7763 1.5921 1.5040 0.0115  -0.0603 -0.0582 187  GLY   E N   
12837 C  CA  . GLY   E 187 ? 1.6994 1.5249 1.4327 0.0131  -0.0574 -0.0577 187  GLY   E CA  
12838 C  C   . GLY   E 187 ? 1.6119 1.4364 1.3445 0.0070  -0.0609 -0.0571 187  GLY   E C   
12839 O  O   . GLY   E 187 ? 1.5682 1.3906 1.3029 0.0006  -0.0654 -0.0567 187  GLY   E O   
12840 N  N   . ARG   E 188 ? 1.5630 1.3890 1.2931 0.0093  -0.0585 -0.0571 188  ARG   E N   
12841 C  CA  . ARG   E 188 ? 1.5723 1.3957 1.2991 0.0049  -0.0616 -0.0569 188  ARG   E CA  
12842 C  C   . ARG   E 188 ? 1.6386 1.4452 1.3464 0.0079  -0.0625 -0.0587 188  ARG   E C   
12843 O  O   . ARG   E 188 ? 1.6963 1.4995 1.3969 0.0146  -0.0578 -0.0593 188  ARG   E O   
12844 C  CB  . ARG   E 188 ? 1.5689 1.4060 1.3063 0.0053  -0.0582 -0.0554 188  ARG   E CB  
12845 N  N   . HIS   E 189 ? 1.6051 1.4013 1.3051 0.0031  -0.0687 -0.0596 189  HIS   E N   
12846 C  CA  . HIS   E 189 ? 1.6502 1.4290 1.3312 0.0055  -0.0708 -0.0616 189  HIS   E CA  
12847 C  C   . HIS   E 189 ? 1.5769 1.3520 1.2548 0.0005  -0.0764 -0.0619 189  HIS   E C   
12848 O  O   . HIS   E 189 ? 1.5144 1.3006 1.2053 -0.0048 -0.0784 -0.0605 189  HIS   E O   
12849 C  CB  . HIS   E 189 ? 1.6645 1.4296 1.3358 0.0055  -0.0737 -0.0632 189  HIS   E CB  
12850 C  CG  . HIS   E 189 ? 1.6287 1.4006 1.3091 0.0065  -0.0711 -0.0624 189  HIS   E CG  
12851 N  ND1 . HIS   E 189 ? 1.6945 1.4717 1.3767 0.0133  -0.0649 -0.0622 189  HIS   E ND1 
12852 C  CD2 . HIS   E 189 ? 1.6006 1.3746 1.2888 0.0017  -0.0737 -0.0618 189  HIS   E CD2 
12853 C  CE1 . HIS   E 189 ? 1.7261 1.5081 1.4161 0.0129  -0.0644 -0.0616 189  HIS   E CE1 
12854 N  NE2 . HIS   E 189 ? 1.7270 1.5068 1.4203 0.0060  -0.0694 -0.0613 189  HIS   E NE2 
12855 N  N   . VAL   E 190 ? 1.5793 1.3382 1.2396 0.0025  -0.0792 -0.0638 190  VAL   E N   
12856 C  CA  . VAL   E 190 ? 1.5262 1.2784 1.1808 -0.0016 -0.0857 -0.0648 190  VAL   E CA  
12857 C  C   . VAL   E 190 ? 1.5723 1.3072 1.2146 -0.0038 -0.0926 -0.0673 190  VAL   E C   
12858 O  O   . VAL   E 190 ? 1.6059 1.3291 1.2357 0.0008  -0.0910 -0.0687 190  VAL   E O   
12859 C  CB  . VAL   E 190 ? 1.5181 1.2664 1.1620 0.0034  -0.0830 -0.0648 190  VAL   E CB  
12860 C  CG1 . VAL   E 190 ? 1.6008 1.3365 1.2277 0.0115  -0.0786 -0.0660 190  VAL   E CG1 
12861 C  CG2 . VAL   E 190 ? 1.5106 1.2506 1.1471 -0.0004 -0.0906 -0.0661 190  VAL   E CG2 
12862 N  N   . LYS   E 191 ? 1.5896 1.3230 1.2362 -0.0110 -0.1002 -0.0679 191  LYS   E N   
12863 C  CA  . LYS   E 191 ? 1.5717 1.2890 1.2085 -0.0143 -0.1077 -0.0705 191  LYS   E CA  
12864 C  C   . LYS   E 191 ? 1.6051 1.3187 1.2406 -0.0188 -0.1156 -0.0717 191  LYS   E C   
12865 O  O   . LYS   E 191 ? 1.5768 1.3029 1.2238 -0.0217 -0.1158 -0.0702 191  LYS   E O   
12866 C  CB  . LYS   E 191 ? 1.3915 1.1111 1.0390 -0.0196 -0.1093 -0.0701 191  LYS   E CB  
12867 N  N   . THR   E 192 ? 1.6303 1.3261 1.2511 -0.0192 -0.1224 -0.0747 192  THR   E N   
12868 C  CA  . THR   E 192 ? 1.5823 1.2721 1.2004 -0.0233 -0.1312 -0.0766 192  THR   E CA  
12869 C  C   . THR   E 192 ? 1.6291 1.3088 1.2479 -0.0294 -0.1393 -0.0788 192  THR   E C   
12870 O  O   . THR   E 192 ? 1.7148 1.3838 1.3256 -0.0279 -0.1388 -0.0799 192  THR   E O   
12871 C  CB  . THR   E 192 ? 1.6102 1.2857 1.2072 -0.0171 -0.1327 -0.0786 192  THR   E CB  
12872 O  OG1 . THR   E 192 ? 1.6687 1.3245 1.2493 -0.0156 -0.1373 -0.0816 192  THR   E OG1 
12873 C  CG2 . THR   E 192 ? 1.6764 1.3563 1.2676 -0.0090 -0.1226 -0.0767 192  THR   E CG2 
12874 N  N   . TYR   E 193 ? 1.6228 1.3060 1.2517 -0.0363 -0.1466 -0.0794 193  TYR   E N   
12875 C  CA  . TYR   E 193 ? 1.6577 1.3320 1.2895 -0.0429 -0.1551 -0.0816 193  TYR   E CA  
12876 C  C   . TYR   E 193 ? 1.6888 1.3555 1.3151 -0.0449 -0.1648 -0.0843 193  TYR   E C   
12877 O  O   . TYR   E 193 ? 1.6961 1.3688 1.3219 -0.0429 -0.1646 -0.0837 193  TYR   E O   
12878 C  CB  . TYR   E 193 ? 1.6236 1.3122 1.2784 -0.0506 -0.1544 -0.0793 193  TYR   E CB  
12879 C  CG  . TYR   E 193 ? 1.6078 1.3002 1.2671 -0.0495 -0.1469 -0.0772 193  TYR   E CG  
12880 C  CD1 . TYR   E 193 ? 1.6686 1.3481 1.3122 -0.0440 -0.1441 -0.0784 193  TYR   E CD1 
12881 C  CD2 . TYR   E 193 ? 1.6190 1.3275 1.2977 -0.0536 -0.1427 -0.0741 193  TYR   E CD2 
12882 C  CE1 . TYR   E 193 ? 1.6952 1.3777 1.3424 -0.0426 -0.1376 -0.0767 193  TYR   E CE1 
12883 C  CE2 . TYR   E 193 ? 1.6061 1.3172 1.2879 -0.0522 -0.1363 -0.0724 193  TYR   E CE2 
12884 C  CZ  . TYR   E 193 ? 1.6428 1.3408 1.3087 -0.0467 -0.1338 -0.0737 193  TYR   E CZ  
12885 O  OH  . TYR   E 193 ? 1.6185 1.3184 1.2865 -0.0447 -0.1277 -0.0721 193  TYR   E OH  
12886 N  N   . GLU   E 194 ? 1.8307 1.4836 1.4528 -0.0488 -0.1735 -0.0874 194  GLU   E N   
12887 C  CA  . GLU   E 194 ? 1.8682 1.5125 1.4855 -0.0511 -0.1842 -0.0906 194  GLU   E CA  
12888 C  C   . GLU   E 194 ? 1.8527 1.5058 1.4916 -0.0607 -0.1905 -0.0906 194  GLU   E C   
12889 O  O   . GLU   E 194 ? 1.8192 1.4784 1.4721 -0.0657 -0.1879 -0.0890 194  GLU   E O   
12890 C  CB  . GLU   E 194 ? 1.9058 1.5266 1.5016 -0.0480 -0.1906 -0.0947 194  GLU   E CB  
12891 C  CG  . GLU   E 194 ? 1.9219 1.5316 1.4940 -0.0384 -0.1881 -0.0957 194  GLU   E CG  
12892 C  CD  . GLU   E 194 ? 2.0088 1.5944 1.5592 -0.0357 -0.1965 -0.1003 194  GLU   E CD  
12893 O  OE1 . GLU   E 194 ? 2.0715 1.6456 1.6004 -0.0275 -0.1947 -0.1013 194  GLU   E OE1 
12894 O  OE2 . GLU   E 194 ? 2.0599 1.6378 1.6148 -0.0418 -0.2048 -0.1029 194  GLU   E OE2 
12895 N  N   . VAL   E 195 ? 1.7505 1.4038 1.3918 -0.0632 -0.1987 -0.0923 195  VAL   E N   
12896 C  CA  . VAL   E 195 ? 1.7403 1.4053 1.4042 -0.0718 -0.2039 -0.0918 195  VAL   E CA  
12897 C  C   . VAL   E 195 ? 1.7485 1.3996 1.4092 -0.0757 -0.2170 -0.0964 195  VAL   E C   
12898 O  O   . VAL   E 195 ? 1.7265 1.3677 1.3729 -0.0720 -0.2236 -0.0992 195  VAL   E O   
12899 C  CB  . VAL   E 195 ? 1.6812 1.3631 1.3557 -0.0717 -0.2015 -0.0894 195  VAL   E CB  
12900 C  CG1 . VAL   E 195 ? 1.6621 1.3487 1.3517 -0.0788 -0.2111 -0.0908 195  VAL   E CG1 
12901 C  CG2 . VAL   E 195 ? 1.6211 1.3207 1.3096 -0.0721 -0.1903 -0.0847 195  VAL   E CG2 
12902 N  N   . SER   E 196 ? 1.7276 1.3778 1.4018 -0.0831 -0.2207 -0.0970 196  SER   E N   
12903 C  CA  . SER   E 196 ? 1.8019 1.4397 1.4765 -0.0879 -0.2333 -0.1014 196  SER   E CA  
12904 C  C   . SER   E 196 ? 1.7541 1.4063 1.4549 -0.0965 -0.2377 -0.1006 196  SER   E C   
12905 O  O   . SER   E 196 ? 1.7416 1.4026 1.4606 -0.1026 -0.2338 -0.0982 196  SER   E O   
12906 C  CB  . SER   E 196 ? 1.8792 1.5020 1.5475 -0.0895 -0.2346 -0.1032 196  SER   E CB  
12907 O  OG  . SER   E 196 ? 1.9165 1.5284 1.5883 -0.0950 -0.2470 -0.1074 196  SER   E OG  
12908 N  N   . LEU   E 197 ? 1.6903 1.3441 1.3924 -0.0968 -0.2459 -0.1026 197  LEU   E N   
12909 C  CA  . LEU   E 197 ? 1.7007 1.3653 1.4264 -0.1049 -0.2525 -0.1029 197  LEU   E CA  
12910 C  C   . LEU   E 197 ? 1.7949 1.4485 1.5276 -0.1117 -0.2623 -0.1065 197  LEU   E C   
12911 O  O   . LEU   E 197 ? 1.7765 1.4395 1.5316 -0.1192 -0.2670 -0.1065 197  LEU   E O   
12912 C  CB  . LEU   E 197 ? 1.6854 1.3533 1.4086 -0.1026 -0.2591 -0.1044 197  LEU   E CB  
12913 C  CG  . LEU   E 197 ? 1.7418 1.4130 1.4496 -0.0941 -0.2517 -0.1022 197  LEU   E CG  
12914 C  CD1 . LEU   E 197 ? 1.7306 1.4075 1.4403 -0.0932 -0.2577 -0.1030 197  LEU   E CD1 
12915 C  CD2 . LEU   E 197 ? 1.7070 1.3942 1.4240 -0.0935 -0.2377 -0.0968 197  LEU   E CD2 
12916 N  N   . ARG   E 198 ? 1.8597 1.4938 1.5743 -0.1091 -0.2654 -0.1096 198  ARG   E N   
12917 C  CA  . ARG   E 198 ? 1.7792 1.4021 1.5004 -0.1156 -0.2742 -0.1130 198  ARG   E CA  
12918 C  C   . ARG   E 198 ? 1.7989 1.4265 1.5339 -0.1208 -0.2660 -0.1098 198  ARG   E C   
12919 O  O   . ARG   E 198 ? 1.7538 1.3896 1.5123 -0.1291 -0.2679 -0.1091 198  ARG   E O   
12920 C  CB  . ARG   E 198 ? 1.8296 1.4282 1.5245 -0.1105 -0.2819 -0.1180 198  ARG   E CB  
12921 N  N   . GLU   E 199 ? 2.0123 1.6348 1.7333 -0.1158 -0.2566 -0.1079 199  GLU   E N   
12922 C  CA  . GLU   E 199 ? 2.0583 1.6864 1.7910 -0.1195 -0.2474 -0.1042 199  GLU   E CA  
12923 C  C   . GLU   E 199 ? 2.0105 1.6607 1.7590 -0.1200 -0.2368 -0.0988 199  GLU   E C   
12924 O  O   . GLU   E 199 ? 1.9939 1.6497 1.7504 -0.1218 -0.2278 -0.0953 199  GLU   E O   
12925 C  CB  . GLU   E 199 ? 2.1187 1.7324 1.8302 -0.1136 -0.2418 -0.1044 199  GLU   E CB  
12926 C  CG  . GLU   E 199 ? 2.1284 1.7483 1.8267 -0.1049 -0.2312 -0.1013 199  GLU   E CG  
12927 C  CD  . GLU   E 199 ? 2.1573 1.7649 1.8381 -0.0996 -0.2248 -0.1010 199  GLU   E CD  
12928 O  OE1 . GLU   E 199 ? 2.1290 1.7417 1.8185 -0.1018 -0.2169 -0.0979 199  GLU   E OE1 
12929 O  OE2 . GLU   E 199 ? 2.1920 1.7841 1.8497 -0.0931 -0.2278 -0.1040 199  GLU   E OE2 
12930 N  N   . LYS   E 200 ? 1.8987 1.5606 1.6508 -0.1182 -0.2379 -0.0982 200  LYS   E N   
12931 C  CA  . LYS   E 200 ? 1.7727 1.4553 1.5387 -0.1183 -0.2288 -0.0934 200  LYS   E CA  
12932 C  C   . LYS   E 200 ? 1.7691 1.4552 1.5314 -0.1149 -0.2163 -0.0895 200  LYS   E C   
12933 O  O   . LYS   E 200 ? 1.7406 1.4400 1.5200 -0.1186 -0.2093 -0.0857 200  LYS   E O   
12934 C  CB  . LYS   E 200 ? 1.5963 1.2923 1.3901 -0.1271 -0.2313 -0.0920 200  LYS   E CB  
12935 N  N   . GLU   E 201 ? 1.7328 1.4069 1.4727 -0.1076 -0.2133 -0.0905 201  GLU   E N   
12936 C  CA  . GLU   E 201 ? 1.7738 1.4504 1.5083 -0.1033 -0.2019 -0.0873 201  GLU   E CA  
12937 C  C   . GLU   E 201 ? 1.7840 1.4513 1.4940 -0.0938 -0.1995 -0.0886 201  GLU   E C   
12938 O  O   . GLU   E 201 ? 1.8000 1.4578 1.4966 -0.0908 -0.2065 -0.0918 201  GLU   E O   
12939 C  CB  . GLU   E 201 ? 1.8573 1.5256 1.5953 -0.1074 -0.2001 -0.0870 201  GLU   E CB  
12940 C  CG  . GLU   E 201 ? 1.9094 1.5887 1.6562 -0.1071 -0.1885 -0.0823 201  GLU   E CG  
12941 C  CD  . GLU   E 201 ? 1.8341 1.5326 1.6055 -0.1130 -0.1853 -0.0788 201  GLU   E CD  
12942 O  OE1 . GLU   E 201 ? 1.7787 1.4844 1.5610 -0.1167 -0.1914 -0.0796 201  GLU   E OE1 
12943 O  OE2 . GLU   E 201 ? 1.8255 1.5314 1.6048 -0.1135 -0.1767 -0.0752 201  GLU   E OE2 
12944 N  N   . PHE   E 202 ? 1.7636 1.4335 1.4678 -0.0889 -0.1894 -0.0859 202  PHE   E N   
12945 C  CA  . PHE   E 202 ? 1.7637 1.4290 1.4483 -0.0796 -0.1845 -0.0861 202  PHE   E CA  
12946 C  C   . PHE   E 202 ? 1.8278 1.4721 1.4914 -0.0755 -0.1864 -0.0890 202  PHE   E C   
12947 O  O   . PHE   E 202 ? 1.9042 1.5391 1.5689 -0.0792 -0.1885 -0.0900 202  PHE   E O   
12948 C  CB  . PHE   E 202 ? 1.7284 1.4079 1.4188 -0.0762 -0.1729 -0.0819 202  PHE   E CB  
12949 C  CG  . PHE   E 202 ? 1.7696 1.4660 1.4687 -0.0750 -0.1699 -0.0797 202  PHE   E CG  
12950 C  CD1 . PHE   E 202 ? 1.7899 1.4955 1.4861 -0.0687 -0.1603 -0.0770 202  PHE   E CD1 
12951 C  CD2 . PHE   E 202 ? 1.8591 1.5617 1.5688 -0.0799 -0.1769 -0.0804 202  PHE   E CD2 
12952 C  CE1 . PHE   E 202 ? 1.6485 1.3682 1.3509 -0.0669 -0.1572 -0.0751 202  PHE   E CE1 
12953 C  CE2 . PHE   E 202 ? 1.6507 1.3687 1.3685 -0.0789 -0.1741 -0.0782 202  PHE   E CE2 
12954 C  CZ  . PHE   E 202 ? 1.6291 1.3551 1.3429 -0.0726 -0.1645 -0.0757 202  PHE   E CZ  
12955 N  N   . ASN   E 203 ? 1.8530 1.4895 1.4969 -0.0674 -0.1855 -0.0904 203  ASN   E N   
12956 C  CA  . ASN   E 203 ? 1.8223 1.4398 1.4442 -0.0617 -0.1856 -0.0928 203  ASN   E CA  
12957 C  C   . ASN   E 203 ? 1.8227 1.4428 1.4321 -0.0524 -0.1763 -0.0911 203  ASN   E C   
12958 O  O   . ASN   E 203 ? 1.8250 1.4589 1.4399 -0.0502 -0.1719 -0.0889 203  ASN   E O   
12959 C  CB  . ASN   E 203 ? 1.7970 1.3966 1.4041 -0.0613 -0.1967 -0.0975 203  ASN   E CB  
12960 C  CG  . ASN   E 203 ? 1.8251 1.4213 1.4451 -0.0705 -0.2067 -0.0997 203  ASN   E CG  
12961 O  OD1 . ASN   E 203 ? 1.8293 1.4272 1.4617 -0.0762 -0.2054 -0.0986 203  ASN   E OD1 
12962 N  ND2 . ASN   E 203 ? 1.8408 1.4316 1.4579 -0.0719 -0.2167 -0.1028 203  ASN   E ND2 
12963 N  N   . LYS   E 204 ? 1.8509 1.4575 1.4437 -0.0469 -0.1734 -0.0922 204  LYS   E N   
12964 C  CA  . LYS   E 204 ? 1.7981 1.4074 1.3806 -0.0381 -0.1639 -0.0904 204  LYS   E CA  
12965 C  C   . LYS   E 204 ? 1.8028 1.4107 1.3734 -0.0323 -0.1643 -0.0912 204  LYS   E C   
12966 O  O   . LYS   E 204 ? 1.8137 1.4066 1.3698 -0.0310 -0.1718 -0.0945 204  LYS   E O   
12967 C  CB  . LYS   E 204 ? 1.7093 1.3025 1.2751 -0.0330 -0.1616 -0.0918 204  LYS   E CB  
12968 N  N   . GLY   E 205 ? 1.7557 1.3785 1.3317 -0.0284 -0.1559 -0.0881 205  GLY   E N   
12969 C  CA  . GLY   E 205 ? 1.7230 1.3463 1.2899 -0.0233 -0.1549 -0.0882 205  GLY   E CA  
12970 C  C   . GLY   E 205 ? 1.7269 1.3369 1.2712 -0.0136 -0.1503 -0.0891 205  GLY   E C   
12971 O  O   . GLY   E 205 ? 1.7910 1.3941 1.3283 -0.0102 -0.1464 -0.0894 205  GLY   E O   
12972 N  N   . PRO   E 206 ? 1.7478 1.3539 1.2802 -0.0086 -0.1503 -0.0896 206  PRO   E N   
12973 C  CA  . PRO   E 206 ? 1.7586 1.3496 1.2675 0.0009  -0.1463 -0.0908 206  PRO   E CA  
12974 C  C   . PRO   E 206 ? 1.8057 1.4041 1.3151 0.0072  -0.1343 -0.0881 206  PRO   E C   
12975 O  O   . PRO   E 206 ? 1.8103 1.3946 1.3020 0.0140  -0.1316 -0.0894 206  PRO   E O   
12976 C  CB  . PRO   E 206 ? 1.7293 1.3172 1.2285 0.0041  -0.1484 -0.0912 206  PRO   E CB  
12977 C  CG  . PRO   E 206 ? 1.7206 1.3238 1.2394 -0.0034 -0.1525 -0.0901 206  PRO   E CG  
12978 C  CD  . PRO   E 206 ? 1.7267 1.3358 1.2627 -0.0119 -0.1568 -0.0903 206  PRO   E CD  
12979 N  N   . TRP   E 207 ? 1.7840 1.4033 1.3126 0.0058  -0.1272 -0.0847 207  TRP   E N   
12980 C  CA  . TRP   E 207 ? 1.7999 1.4262 1.3293 0.0122  -0.1163 -0.0824 207  TRP   E CA  
12981 C  C   . TRP   E 207 ? 1.7532 1.4014 1.3067 0.0081  -0.1113 -0.0794 207  TRP   E C   
12982 O  O   . TRP   E 207 ? 1.7467 1.4048 1.3160 0.0004  -0.1157 -0.0787 207  TRP   E O   
12983 C  CB  . TRP   E 207 ? 1.8474 1.4723 1.3653 0.0201  -0.1099 -0.0815 207  TRP   E CB  
12984 C  CG  . TRP   E 207 ? 1.8228 1.4545 1.3448 0.0182  -0.1118 -0.0806 207  TRP   E CG  
12985 C  CD1 . TRP   E 207 ? 1.7998 1.4181 1.3070 0.0190  -0.1184 -0.0827 207  TRP   E CD1 
12986 C  CD2 . TRP   E 207 ? 1.8230 1.4755 1.3642 0.0157  -0.1071 -0.0775 207  TRP   E CD2 
12987 N  NE1 . TRP   E 207 ? 1.8328 1.4624 1.3487 0.0171  -0.1180 -0.0809 207  TRP   E NE1 
12988 C  CE2 . TRP   E 207 ? 1.8013 1.4520 1.3383 0.0149  -0.1110 -0.0777 207  TRP   E CE2 
12989 C  CE3 . TRP   E 207 ? 1.7549 1.4267 1.3160 0.0142  -0.1003 -0.0746 207  TRP   E CE3 
12990 C  CZ2 . TRP   E 207 ? 1.7142 1.3818 1.2662 0.0125  -0.1081 -0.0751 207  TRP   E CZ2 
12991 C  CZ3 . TRP   E 207 ? 1.7025 1.3910 1.2785 0.0118  -0.0976 -0.0721 207  TRP   E CZ3 
12992 C  CH2 . TRP   E 207 ? 1.6909 1.3772 1.2624 0.0109  -0.1014 -0.0723 207  TRP   E CH2 
12993 N  N   . LYS   E 208 ? 1.7560 1.4113 1.3121 0.0136  -0.1022 -0.0776 208  LYS   E N   
12994 C  CA  . LYS   E 208 ? 1.7436 1.4188 1.3207 0.0114  -0.0967 -0.0748 208  LYS   E CA  
12995 C  C   . LYS   E 208 ? 1.7469 1.4276 1.3226 0.0195  -0.0867 -0.0733 208  LYS   E C   
12996 O  O   . LYS   E 208 ? 1.7396 1.4083 1.2984 0.0266  -0.0837 -0.0744 208  LYS   E O   
12997 C  CB  . LYS   E 208 ? 1.6817 1.3573 1.2672 0.0063  -0.0997 -0.0751 208  LYS   E CB  
12998 C  CG  . LYS   E 208 ? 1.6905 1.3479 1.2598 0.0095  -0.1013 -0.0774 208  LYS   E CG  
12999 C  CD  . LYS   E 208 ? 1.6827 1.3437 1.2614 0.0068  -0.1003 -0.0767 208  LYS   E CD  
13000 C  CE  . LYS   E 208 ? 1.7139 1.3794 1.2921 0.0142  -0.0918 -0.0756 208  LYS   E CE  
13001 N  NZ  . LYS   E 208 ? 1.7155 1.3845 1.3025 0.0121  -0.0909 -0.0748 208  LYS   E NZ  
13002 N  N   . GLN   E 209 ? 1.6886 1.3879 1.2828 0.0186  -0.0814 -0.0709 209  GLN   E N   
13003 C  CA  . GLN   E 209 ? 1.7603 1.4674 1.3573 0.0257  -0.0721 -0.0695 209  GLN   E CA  
13004 C  C   . GLN   E 209 ? 1.7587 1.4806 1.3739 0.0235  -0.0698 -0.0680 209  GLN   E C   
13005 O  O   . GLN   E 209 ? 1.7100 1.4470 1.3419 0.0187  -0.0701 -0.0663 209  GLN   E O   
13006 C  CB  . GLN   E 209 ? 1.7228 1.4382 1.3223 0.0286  -0.0671 -0.0678 209  GLN   E CB  
13007 N  N   . GLU   E 210 ? 1.8108 1.5279 1.4221 0.0273  -0.0675 -0.0687 210  GLU   E N   
13008 C  CA  . GLU   E 210 ? 1.7856 1.5119 1.4105 0.0246  -0.0673 -0.0679 210  GLU   E CA  
13009 C  C   . GLU   E 210 ? 1.8461 1.5925 1.4892 0.0259  -0.0616 -0.0657 210  GLU   E C   
13010 O  O   . GLU   E 210 ? 1.8736 1.6292 1.5294 0.0230  -0.0621 -0.0648 210  GLU   E O   
13011 C  CB  . GLU   E 210 ? 1.8149 1.5296 1.4292 0.0292  -0.0664 -0.0693 210  GLU   E CB  
13012 N  N   . ASN   E 211 ? 1.9205 1.6737 1.5654 0.0301  -0.0562 -0.0648 211  ASN   E N   
13013 C  CA  . ASN   E 211 ? 1.8828 1.6553 1.5464 0.0307  -0.0514 -0.0629 211  ASN   E CA  
13014 C  C   . ASN   E 211 ? 1.9120 1.6915 1.5784 0.0324  -0.0472 -0.0616 211  ASN   E C   
13015 O  O   . ASN   E 211 ? 2.0180 1.7884 1.6715 0.0377  -0.0439 -0.0621 211  ASN   E O   
13016 C  CB  . ASN   E 211 ? 1.9268 1.7027 1.5934 0.0371  -0.0462 -0.0631 211  ASN   E CB  
13017 C  CG  . ASN   E 211 ? 1.9730 1.7541 1.6491 0.0342  -0.0488 -0.0630 211  ASN   E CG  
13018 O  OD1 . ASN   E 211 ? 1.9907 1.7871 1.6831 0.0336  -0.0469 -0.0617 211  ASN   E OD1 
13019 N  ND2 . ASN   E 211 ? 1.9903 1.7581 1.6562 0.0322  -0.0534 -0.0642 211  ASN   E ND2 
13020 N  N   . VAL   E 212 ? 1.7785 1.5737 1.4616 0.0282  -0.0469 -0.0599 212  VAL   E N   
13021 C  CA  . VAL   E 212 ? 1.7735 1.5764 1.4611 0.0291  -0.0430 -0.0584 212  VAL   E CA  
13022 C  C   . VAL   E 212 ? 1.7040 1.5268 1.4130 0.0276  -0.0399 -0.0566 212  VAL   E C   
13023 O  O   . VAL   E 212 ? 1.6811 1.5106 1.4000 0.0264  -0.0411 -0.0567 212  VAL   E O   
13024 C  CB  . VAL   E 212 ? 1.7547 1.5509 1.4350 0.0241  -0.0484 -0.0584 212  VAL   E CB  
13025 C  CG1 . VAL   E 212 ? 1.6695 1.4752 1.3633 0.0160  -0.0540 -0.0577 212  VAL   E CG1 
13026 C  CG2 . VAL   E 212 ? 1.6938 1.4907 1.3702 0.0272  -0.0438 -0.0573 212  VAL   E CG2 
13027 N  N   . GLU   E 213 ? 1.6492 1.4810 1.3652 0.0280  -0.0360 -0.0550 213  GLU   E N   
13028 C  CA  . GLU   E 213 ? 1.6668 1.5172 1.4032 0.0270  -0.0328 -0.0535 213  GLU   E CA  
13029 C  C   . GLU   E 213 ? 1.6037 1.4617 1.3513 0.0203  -0.0387 -0.0532 213  GLU   E C   
13030 O  O   . GLU   E 213 ? 1.6032 1.4585 1.3489 0.0145  -0.0440 -0.0530 213  GLU   E O   
13031 C  CB  . GLU   E 213 ? 1.6322 1.4892 1.3731 0.0269  -0.0289 -0.0518 213  GLU   E CB  
13032 N  N   . ALA   E 214 ? 1.5761 1.4435 1.3357 0.0214  -0.0376 -0.0532 214  ALA   E N   
13033 C  CA  . ALA   E 214 ? 1.6203 1.4950 1.3907 0.0160  -0.0422 -0.0528 214  ALA   E CA  
13034 C  C   . ALA   E 214 ? 1.5997 1.4855 1.3815 0.0108  -0.0433 -0.0511 214  ALA   E C   
13035 O  O   . ALA   E 214 ? 1.5969 1.4874 1.3860 0.0054  -0.0475 -0.0505 214  ALA   E O   
13036 C  CB  . ALA   E 214 ? 1.6200 1.5031 1.4008 0.0193  -0.0402 -0.0531 214  ALA   E CB  
13037 N  N   . GLU   E 215 ? 1.6045 1.4943 1.3878 0.0125  -0.0392 -0.0502 215  GLU   E N   
13038 C  CA  . GLU   E 215 ? 1.5900 1.4889 1.3822 0.0081  -0.0398 -0.0485 215  GLU   E CA  
13039 C  C   . GLU   E 215 ? 1.5530 1.4414 1.3322 0.0059  -0.0423 -0.0485 215  GLU   E C   
13040 O  O   . GLU   E 215 ? 1.5760 1.4685 1.3575 0.0054  -0.0402 -0.0472 215  GLU   E O   
13041 C  CB  . GLU   E 215 ? 1.6107 1.5219 1.4149 0.0114  -0.0333 -0.0474 215  GLU   E CB  
13042 C  CG  . GLU   E 215 ? 1.6120 1.5378 1.4341 0.0112  -0.0328 -0.0471 215  GLU   E CG  
13043 C  CD  . GLU   E 215 ? 1.6167 1.5448 1.4434 0.0057  -0.0390 -0.0471 215  GLU   E CD  
13044 O  OE1 . GLU   E 215 ? 1.6097 1.5359 1.4343 0.0003  -0.0430 -0.0463 215  GLU   E OE1 
13045 O  OE2 . GLU   E 215 ? 1.6375 1.5690 1.4699 0.0070  -0.0398 -0.0478 215  GLU   E OE2 
13046 N  N   . ALA   E 216 ? 1.5225 1.3971 1.2881 0.0047  -0.0471 -0.0499 216  ALA   E N   
13047 C  CA  . ALA   E 216 ? 1.5119 1.3750 1.2638 0.0032  -0.0502 -0.0503 216  ALA   E CA  
13048 C  C   . ALA   E 216 ? 1.4535 1.3196 1.2110 -0.0042 -0.0570 -0.0499 216  ALA   E C   
13049 O  O   . ALA   E 216 ? 1.3682 1.2353 1.1307 -0.0081 -0.0611 -0.0503 216  ALA   E O   
13050 C  CB  . ALA   E 216 ? 1.4840 1.3296 1.2175 0.0062  -0.0520 -0.0523 216  ALA   E CB  
13051 N  N   . SER   E 217 ? 1.3901 1.2576 1.1470 -0.0060 -0.0578 -0.0490 217  SER   E N   
13052 C  CA  . SER   E 217 ? 1.3660 1.2379 1.1299 -0.0128 -0.0638 -0.0485 217  SER   E CA  
13053 C  C   . SER   E 217 ? 1.3443 1.2071 1.0972 -0.0144 -0.0682 -0.0490 217  SER   E C   
13054 O  O   . SER   E 217 ? 1.4321 1.2972 1.1901 -0.0200 -0.0741 -0.0489 217  SER   E O   
13055 C  CB  . SER   E 217 ? 1.3831 1.2728 1.1655 -0.0149 -0.0612 -0.0464 217  SER   E CB  
13056 O  OG  . SER   E 217 ? 1.4056 1.3014 1.1915 -0.0098 -0.0537 -0.0455 217  SER   E OG  
13057 N  N   . MET   E 218 ? 1.3289 1.1813 1.0670 -0.0095 -0.0656 -0.0495 218  MET   E N   
13058 C  CA  . MET   E 218 ? 1.4036 1.2464 1.1300 -0.0104 -0.0701 -0.0501 218  MET   E CA  
13059 C  C   . MET   E 218 ? 1.4691 1.2927 1.1755 -0.0079 -0.0739 -0.0526 218  MET   E C   
13060 O  O   . MET   E 218 ? 1.3640 1.1796 1.0596 -0.0020 -0.0692 -0.0532 218  MET   E O   
13061 C  CB  . MET   E 218 ? 1.4594 1.3046 1.1834 -0.0066 -0.0642 -0.0485 218  MET   E CB  
13062 C  CG  . MET   E 218 ? 1.4574 1.3195 1.1991 -0.0097 -0.0621 -0.0462 218  MET   E CG  
13063 S  SD  . MET   E 218 ? 1.5039 1.3629 1.2382 -0.0088 -0.0618 -0.0450 218  MET   E SD  
13064 C  CE  . MET   E 218 ? 1.3844 1.2255 1.0956 -0.0007 -0.0570 -0.0459 218  MET   E CE  
13065 N  N   . VAL   E 219 ? 1.5223 1.3384 1.2238 -0.0123 -0.0826 -0.0542 219  VAL   E N   
13066 C  CA  . VAL   E 219 ? 1.5482 1.3453 1.2302 -0.0106 -0.0878 -0.0568 219  VAL   E CA  
13067 C  C   . VAL   E 219 ? 1.5424 1.3325 1.2137 -0.0094 -0.0905 -0.0570 219  VAL   E C   
13068 O  O   . VAL   E 219 ? 1.5273 1.3224 1.2057 -0.0143 -0.0960 -0.0568 219  VAL   E O   
13069 C  CB  . VAL   E 219 ? 1.5426 1.3351 1.2270 -0.0165 -0.0964 -0.0587 219  VAL   E CB  
13070 C  CG1 . VAL   E 219 ? 1.5591 1.3340 1.2262 -0.0165 -0.1045 -0.0614 219  VAL   E CG1 
13071 C  CG2 . VAL   E 219 ? 1.5491 1.3399 1.2344 -0.0154 -0.0939 -0.0592 219  VAL   E CG2 
13072 N  N   . ILE   E 220 ? 1.4723 1.2502 1.1258 -0.0026 -0.0867 -0.0574 220  ILE   E N   
13073 C  CA  . ILE   E 220 ? 1.4829 1.2515 1.1228 -0.0003 -0.0890 -0.0578 220  ILE   E CA  
13074 C  C   . ILE   E 220 ? 1.5764 1.3238 1.1946 0.0023  -0.0951 -0.0609 220  ILE   E C   
13075 O  O   . ILE   E 220 ? 1.6425 1.3801 1.2486 0.0076  -0.0910 -0.0617 220  ILE   E O   
13076 C  CB  . ILE   E 220 ? 1.5005 1.2714 1.1365 0.0059  -0.0789 -0.0553 220  ILE   E CB  
13077 C  CG1 . ILE   E 220 ? 1.4594 1.2508 1.1169 0.0031  -0.0735 -0.0524 220  ILE   E CG1 
13078 C  CG2 . ILE   E 220 ? 1.5474 1.3054 1.1658 0.0090  -0.0813 -0.0558 220  ILE   E CG2 
13079 C  CD1 . ILE   E 220 ? 1.3882 1.1817 1.0428 0.0090  -0.0632 -0.0500 220  ILE   E CD1 
13080 N  N   . ALA   E 221 ? 1.5874 1.3273 1.2003 -0.0011 -0.1050 -0.0629 221  ALA   E N   
13081 C  CA  . ALA   E 221 ? 1.5040 1.2231 1.0961 0.0011  -0.1122 -0.0663 221  ALA   E CA  
13082 C  C   . ALA   E 221 ? 1.5630 1.2687 1.1341 0.0083  -0.1099 -0.0663 221  ALA   E C   
13083 O  O   . ALA   E 221 ? 1.6574 1.3637 1.2273 0.0076  -0.1130 -0.0659 221  ALA   E O   
13084 C  CB  . ALA   E 221 ? 1.4346 1.1519 1.0319 -0.0060 -0.1245 -0.0687 221  ALA   E CB  
13085 N  N   . VAL   E 222 ? 1.6190 1.3120 1.1729 0.0155  -0.1044 -0.0668 222  VAL   E N   
13086 C  CA  . VAL   E 222 ? 1.6633 1.3414 1.1949 0.0230  -0.1017 -0.0667 222  VAL   E CA  
13087 C  C   . VAL   E 222 ? 1.7026 1.3629 1.2172 0.0226  -0.1139 -0.0704 222  VAL   E C   
13088 O  O   . VAL   E 222 ? 1.7070 1.3592 1.2189 0.0197  -0.1221 -0.0734 222  VAL   E O   
13089 C  CB  . VAL   E 222 ? 1.6862 1.3549 1.2038 0.0310  -0.0925 -0.0663 222  VAL   E CB  
13090 C  CG1 . VAL   E 222 ? 1.7270 1.3764 1.2181 0.0391  -0.0909 -0.0667 222  VAL   E CG1 
13091 C  CG2 . VAL   E 222 ? 1.5995 1.2861 1.1340 0.0322  -0.0802 -0.0626 222  VAL   E CG2 
13092 N  N   . PRO   E 223 ? 1.7682 1.4214 1.2713 0.0253  -0.1159 -0.0702 223  PRO   E N   
13093 C  CA  . PRO   E 223 ? 1.8208 1.4581 1.3094 0.0246  -0.1288 -0.0739 223  PRO   E CA  
13094 C  C   . PRO   E 223 ? 1.9356 1.5488 1.3967 0.0317  -0.1307 -0.0767 223  PRO   E C   
13095 O  O   . PRO   E 223 ? 1.8730 1.4810 1.3244 0.0379  -0.1212 -0.0755 223  PRO   E O   
13096 C  CB  . PRO   E 223 ? 1.7798 1.4189 1.2656 0.0261  -0.1286 -0.0723 223  PRO   E CB  
13097 C  CG  . PRO   E 223 ? 1.8150 1.4606 1.3010 0.0315  -0.1141 -0.0683 223  PRO   E CG  
13098 C  CD  . PRO   E 223 ? 1.7654 1.4263 1.2704 0.0287  -0.1069 -0.0666 223  PRO   E CD  
13099 N  N   . GLU   E 224 ? 2.1247 1.7226 1.5729 0.0308  -0.1435 -0.0807 224  GLU   E N   
13100 C  CA  . GLU   E 224 ? 2.1799 1.7546 1.6046 0.0353  -0.1490 -0.0845 224  GLU   E CA  
13101 C  C   . GLU   E 224 ? 2.2028 1.7641 1.6055 0.0455  -0.1386 -0.0833 224  GLU   E C   
13102 O  O   . GLU   E 224 ? 2.1919 1.7442 1.5866 0.0478  -0.1375 -0.0848 224  GLU   E O   
13103 C  CB  . GLU   E 224 ? 2.2118 1.7704 1.6214 0.0355  -0.1628 -0.0883 224  GLU   E CB  
13104 C  CG  . GLU   E 224 ? 2.2354 1.8023 1.6639 0.0257  -0.1752 -0.0908 224  GLU   E CG  
13105 C  CD  . GLU   E 224 ? 2.2991 1.8798 1.7425 0.0212  -0.1787 -0.0894 224  GLU   E CD  
13106 O  OE1 . GLU   E 224 ? 2.3109 1.8975 1.7689 0.0136  -0.1893 -0.0916 224  GLU   E OE1 
13107 O  OE2 . GLU   E 224 ? 2.2881 1.8737 1.7288 0.0253  -0.1705 -0.0862 224  GLU   E OE2 
13108 N  N   . PRO   E 225 ? 2.1030 1.6620 1.4954 0.0518  -0.1306 -0.0806 225  PRO   E N   
13109 C  CA  . PRO   E 225 ? 2.0986 1.6442 1.4700 0.0618  -0.1200 -0.0794 225  PRO   E CA  
13110 C  C   . PRO   E 225 ? 2.0479 1.5987 1.4263 0.0624  -0.1123 -0.0786 225  PRO   E C   
13111 O  O   . PRO   E 225 ? 1.9780 1.5130 1.3412 0.0654  -0.1156 -0.0814 225  PRO   E O   
13112 C  CB  . PRO   E 225 ? 2.1076 1.6620 1.4818 0.0652  -0.1090 -0.0749 225  PRO   E CB  
13113 C  CG  . PRO   E 225 ? 2.0713 1.6322 1.4542 0.0596  -0.1182 -0.0754 225  PRO   E CG  
13114 C  CD  . PRO   E 225 ? 2.0302 1.5992 1.4305 0.0502  -0.1300 -0.0783 225  PRO   E CD  
13115 N  N   . PHE   E 226 ? 2.0382 1.6109 1.4397 0.0596  -0.1024 -0.0749 226  PHE   E N   
13116 C  CA  . PHE   E 226 ? 1.9038 1.4832 1.3136 0.0606  -0.0944 -0.0739 226  PHE   E CA  
13117 C  C   . PHE   E 226 ? 1.8933 1.4832 1.3223 0.0520  -0.1014 -0.0756 226  PHE   E C   
13118 O  O   . PHE   E 226 ? 1.8894 1.4789 1.3197 0.0532  -0.0980 -0.0760 226  PHE   E O   
13119 C  CB  . PHE   E 226 ? 1.8412 1.4386 1.2663 0.0624  -0.0801 -0.0692 226  PHE   E CB  
13120 N  N   . GLY   E 227 ? 1.9353 1.5351 1.3797 0.0437  -0.1104 -0.0763 227  GLY   E N   
13121 C  CA  . GLY   E 227 ? 1.8569 1.4664 1.3196 0.0356  -0.1166 -0.0777 227  GLY   E CA  
13122 C  C   . GLY   E 227 ? 1.7436 1.3710 1.2263 0.0336  -0.1077 -0.0751 227  GLY   E C   
13123 O  O   . GLY   E 227 ? 1.7013 1.3343 1.1848 0.0389  -0.0962 -0.0723 227  GLY   E O   
13124 N  N   . GLY   E 228 ? 1.7622 1.3981 1.2611 0.0264  -0.1129 -0.0760 228  GLY   E N   
13125 C  CA  . GLY   E 228 ? 1.7924 1.4436 1.3084 0.0252  -0.1051 -0.0738 228  GLY   E CA  
13126 C  C   . GLY   E 228 ? 1.7627 1.4367 1.3029 0.0202  -0.1016 -0.0707 228  GLY   E C   
13127 O  O   . GLY   E 228 ? 1.7371 1.4158 1.2828 0.0163  -0.1065 -0.0704 228  GLY   E O   
13128 N  N   . ALA   E 229 ? 1.6825 1.3705 1.2370 0.0207  -0.0930 -0.0684 229  ALA   E N   
13129 C  CA  . ALA   E 229 ? 1.6187 1.3289 1.1978 0.0155  -0.0900 -0.0657 229  ALA   E CA  
13130 C  C   . ALA   E 229 ? 1.6632 1.3845 1.2494 0.0205  -0.0777 -0.0628 229  ALA   E C   
13131 O  O   . ALA   E 229 ? 1.5695 1.2855 1.1485 0.0261  -0.0719 -0.0630 229  ALA   E O   
13132 C  CB  . ALA   E 229 ? 1.5683 1.2859 1.1625 0.0088  -0.0948 -0.0665 229  ALA   E CB  
13133 N  N   . ILE   E 230 ? 1.6423 1.3788 1.2428 0.0186  -0.0741 -0.0602 230  ILE   E N   
13134 C  CA  . ILE   E 230 ? 1.5731 1.3230 1.1847 0.0219  -0.0631 -0.0573 230  ILE   E CA  
13135 C  C   . ILE   E 230 ? 1.5387 1.3077 1.1744 0.0162  -0.0631 -0.0562 230  ILE   E C   
13136 O  O   . ILE   E 230 ? 1.5101 1.2878 1.1576 0.0098  -0.0684 -0.0558 230  ILE   E O   
13137 C  CB  . ILE   E 230 ? 1.5643 1.3173 1.1746 0.0241  -0.0586 -0.0551 230  ILE   E CB  
13138 C  CG1 . ILE   E 230 ? 1.6120 1.3453 1.1969 0.0310  -0.0571 -0.0559 230  ILE   E CG1 
13139 C  CG2 . ILE   E 230 ? 1.5425 1.3119 1.1689 0.0260  -0.0480 -0.0522 230  ILE   E CG2 
13140 C  CD1 . ILE   E 230 ? 1.6368 1.3686 1.2163 0.0390  -0.0450 -0.0541 230  ILE   E CD1 
13141 N  N   . ILE   E 231 ? 1.5739 1.3490 1.2168 0.0188  -0.0571 -0.0557 231  ILE   E N   
13142 C  CA  . ILE   E 231 ? 1.5129 1.3047 1.1770 0.0146  -0.0566 -0.0547 231  ILE   E CA  
13143 C  C   . ILE   E 231 ? 1.5306 1.3370 1.2077 0.0176  -0.0472 -0.0523 231  ILE   E C   
13144 O  O   . ILE   E 231 ? 1.4914 1.2951 1.1635 0.0241  -0.0397 -0.0519 231  ILE   E O   
13145 C  CB  . ILE   E 231 ? 1.4650 1.2522 1.1276 0.0150  -0.0581 -0.0564 231  ILE   E CB  
13146 C  CG1 . ILE   E 231 ? 1.4951 1.2662 1.1437 0.0123  -0.0671 -0.0590 231  ILE   E CG1 
13147 C  CG2 . ILE   E 231 ? 1.3703 1.1736 1.0534 0.0107  -0.0581 -0.0554 231  ILE   E CG2 
13148 C  CD1 . ILE   E 231 ? 1.4055 1.1822 1.0648 0.0040  -0.0752 -0.0592 231  ILE   E CD1 
13149 N  N   . ILE   E 232 ? 1.5250 1.3468 1.2196 0.0128  -0.0476 -0.0506 232  ILE   E N   
13150 C  CA  . ILE   E 232 ? 1.4957 1.3323 1.2047 0.0145  -0.0398 -0.0482 232  ILE   E CA  
13151 C  C   . ILE   E 232 ? 1.4259 1.2780 1.1547 0.0116  -0.0396 -0.0478 232  ILE   E C   
13152 O  O   . ILE   E 232 ? 1.3969 1.2547 1.1345 0.0055  -0.0457 -0.0479 232  ILE   E O   
13153 C  CB  . ILE   E 232 ? 1.4346 1.2756 1.1463 0.0120  -0.0401 -0.0466 232  ILE   E CB  
13154 C  CG1 . ILE   E 232 ? 1.4309 1.2575 1.1232 0.0173  -0.0371 -0.0465 232  ILE   E CG1 
13155 C  CG2 . ILE   E 232 ? 1.4163 1.2759 1.1483 0.0111  -0.0344 -0.0443 232  ILE   E CG2 
13156 C  CD1 . ILE   E 232 ? 1.4510 1.2732 1.1369 0.0145  -0.0420 -0.0462 232  ILE   E CD1 
13157 N  N   . GLY   E 233 ? 1.4674 1.3255 1.2027 0.0162  -0.0327 -0.0474 233  GLY   E N   
13158 C  CA  . GLY   E 233 ? 1.5108 1.3832 1.2641 0.0147  -0.0319 -0.0471 233  GLY   E CA  
13159 C  C   . GLY   E 233 ? 1.5234 1.4099 1.2915 0.0167  -0.0247 -0.0453 233  GLY   E C   
13160 O  O   . GLY   E 233 ? 1.5479 1.4337 1.3130 0.0182  -0.0207 -0.0439 233  GLY   E O   
13161 N  N   . GLN   E 234 ? 1.5405 1.4396 1.3246 0.0169  -0.0230 -0.0452 234  GLN   E N   
13162 C  CA  . GLN   E 234 ? 1.5167 1.4305 1.3173 0.0175  -0.0176 -0.0435 234  GLN   E CA  
13163 C  C   . GLN   E 234 ? 1.5565 1.4685 1.3542 0.0240  -0.0088 -0.0429 234  GLN   E C   
13164 O  O   . GLN   E 234 ? 1.5826 1.5009 1.3869 0.0243  -0.0038 -0.0411 234  GLN   E O   
13165 C  CB  . GLN   E 234 ? 1.5398 1.4669 1.3578 0.0163  -0.0188 -0.0439 234  GLN   E CB  
13166 C  CG  . GLN   E 234 ? 1.5594 1.4918 1.3842 0.0095  -0.0257 -0.0436 234  GLN   E CG  
13167 C  CD  . GLN   E 234 ? 1.5842 1.5333 1.4292 0.0080  -0.0250 -0.0429 234  GLN   E CD  
13168 O  OE1 . GLN   E 234 ? 1.5378 1.4938 1.3906 0.0030  -0.0282 -0.0419 234  GLN   E OE1 
13169 N  NE2 . GLN   E 234 ? 1.5848 1.5401 1.4384 0.0125  -0.0210 -0.0436 234  GLN   E NE2 
13170 N  N   . GLU   E 235 ? 1.5889 1.4918 1.3765 0.0293  -0.0064 -0.0442 235  GLU   E N   
13171 C  CA  . GLU   E 235 ? 1.5922 1.4930 1.3771 0.0359  0.0026  -0.0435 235  GLU   E CA  
13172 C  C   . GLU   E 235 ? 1.6218 1.5040 1.3834 0.0398  0.0038  -0.0440 235  GLU   E C   
13173 O  O   . GLU   E 235 ? 1.6260 1.5046 1.3829 0.0455  0.0118  -0.0431 235  GLU   E O   
13174 C  CB  . GLU   E 235 ? 1.4981 1.4064 1.2940 0.0403  0.0062  -0.0445 235  GLU   E CB  
13175 N  N   . SER   E 236 ? 1.5992 1.4692 1.3462 0.0370  -0.0038 -0.0453 236  SER   E N   
13176 C  CA  . SER   E 236 ? 1.6053 1.4566 1.3297 0.0411  -0.0039 -0.0465 236  SER   E CA  
13177 C  C   . SER   E 236 ? 1.5903 1.4306 1.3007 0.0370  -0.0108 -0.0469 236  SER   E C   
13178 O  O   . SER   E 236 ? 1.5932 1.4361 1.3081 0.0308  -0.0186 -0.0475 236  SER   E O   
13179 C  CB  . SER   E 236 ? 1.6810 1.5265 1.4006 0.0427  -0.0071 -0.0487 236  SER   E CB  
13180 O  OG  . SER   E 236 ? 1.7114 1.5619 1.4387 0.0362  -0.0152 -0.0495 236  SER   E OG  
13181 N  N   . ILE   E 237 ? 1.6305 1.4579 1.3239 0.0409  -0.0079 -0.0465 237  ILE   E N   
13182 C  CA  . ILE   E 237 ? 1.6702 1.4833 1.3462 0.0386  -0.0148 -0.0474 237  ILE   E CA  
13183 C  C   . ILE   E 237 ? 1.6695 1.4638 1.3241 0.0435  -0.0159 -0.0495 237  ILE   E C   
13184 O  O   . ILE   E 237 ? 1.6483 1.4355 1.2932 0.0505  -0.0084 -0.0491 237  ILE   E O   
13185 C  CB  . ILE   E 237 ? 1.6816 1.4927 1.3524 0.0396  -0.0113 -0.0455 237  ILE   E CB  
13186 C  CG1 . ILE   E 237 ? 1.6217 1.4482 1.3103 0.0333  -0.0135 -0.0439 237  ILE   E CG1 
13187 C  CG2 . ILE   E 237 ? 1.6720 1.4637 1.3192 0.0404  -0.0169 -0.0468 237  ILE   E CG2 
13188 C  CD1 . ILE   E 237 ? 1.6449 1.4685 1.3275 0.0343  -0.0103 -0.0420 237  ILE   E CD1 
13189 N  N   . THR   E 238 ? 1.6918 1.4778 1.3394 0.0398  -0.0250 -0.0518 238  THR   E N   
13190 C  CA  . THR   E 238 ? 1.7457 1.5132 1.3729 0.0439  -0.0271 -0.0541 238  THR   E CA  
13191 C  C   . THR   E 238 ? 1.7349 1.4872 1.3453 0.0412  -0.0359 -0.0557 238  THR   E C   
13192 O  O   . THR   E 238 ? 1.7087 1.4659 1.3267 0.0343  -0.0433 -0.0560 238  THR   E O   
13193 C  CB  . THR   E 238 ? 1.7706 1.5395 1.4029 0.0431  -0.0297 -0.0557 238  THR   E CB  
13194 O  OG1 . THR   E 238 ? 1.7774 1.5425 1.4091 0.0364  -0.0399 -0.0573 238  THR   E OG1 
13195 C  CG2 . THR   E 238 ? 1.7857 1.5744 1.4410 0.0424  -0.0248 -0.0542 238  THR   E CG2 
13196 N  N   . TYR   E 239 ? 1.7747 1.5085 1.3625 0.0470  -0.0350 -0.0568 239  TYR   E N   
13197 C  CA  . TYR   E 239 ? 1.7529 1.4692 1.3222 0.0455  -0.0442 -0.0592 239  TYR   E CA  
13198 C  C   . TYR   E 239 ? 1.7629 1.4671 1.3223 0.0460  -0.0492 -0.0621 239  TYR   E C   
13199 O  O   . TYR   E 239 ? 1.7397 1.4422 1.2968 0.0511  -0.0434 -0.0621 239  TYR   E O   
13200 C  CB  . TYR   E 239 ? 1.6564 1.3583 1.2052 0.0519  -0.0406 -0.0588 239  TYR   E CB  
13201 C  CG  . TYR   E 239 ? 1.7060 1.3866 1.2316 0.0524  -0.0497 -0.0617 239  TYR   E CG  
13202 C  CD1 . TYR   E 239 ? 1.7679 1.4464 1.2958 0.0452  -0.0616 -0.0640 239  TYR   E CD1 
13203 C  CD2 . TYR   E 239 ? 1.6777 1.3398 1.1790 0.0604  -0.0463 -0.0621 239  TYR   E CD2 
13204 C  CE1 . TYR   E 239 ? 1.7159 1.3750 1.2236 0.0457  -0.0703 -0.0668 239  TYR   E CE1 
13205 C  CE2 . TYR   E 239 ? 1.6233 1.2646 1.1022 0.0614  -0.0552 -0.0650 239  TYR   E CE2 
13206 C  CZ  . TYR   E 239 ? 1.6501 1.2905 1.1331 0.0537  -0.0676 -0.0675 239  TYR   E CZ  
13207 O  OH  . TYR   E 239 ? 1.7767 1.3984 1.2410 0.0535  -0.0779 -0.0708 239  TYR   E OH  
13208 N  N   . HIS   E 240 ? 1.7274 1.4245 1.2831 0.0402  -0.0601 -0.0643 240  HIS   E N   
13209 C  CA  . HIS   E 240 ? 1.7271 1.4117 1.2738 0.0392  -0.0666 -0.0672 240  HIS   E CA  
13210 C  C   . HIS   E 240 ? 1.7603 1.4264 1.2883 0.0381  -0.0761 -0.0699 240  HIS   E C   
13211 O  O   . HIS   E 240 ? 1.7631 1.4323 1.2960 0.0328  -0.0825 -0.0700 240  HIS   E O   
13212 C  CB  . HIS   E 240 ? 1.7171 1.4139 1.2829 0.0317  -0.0710 -0.0673 240  HIS   E CB  
13213 C  CG  . HIS   E 240 ? 1.6918 1.4069 1.2764 0.0324  -0.0631 -0.0649 240  HIS   E CG  
13214 N  ND1 . HIS   E 240 ? 1.7669 1.4828 1.3540 0.0349  -0.0598 -0.0653 240  HIS   E ND1 
13215 C  CD2 . HIS   E 240 ? 1.6805 1.4130 1.2815 0.0316  -0.0576 -0.0623 240  HIS   E CD2 
13216 C  CE1 . HIS   E 240 ? 1.7717 1.5051 1.3765 0.0355  -0.0532 -0.0631 240  HIS   E CE1 
13217 N  NE2 . HIS   E 240 ? 1.7774 1.5211 1.3910 0.0334  -0.0517 -0.0613 240  HIS   E NE2 
13218 N  N   . ASN   E 241 ? 1.8372 1.4838 1.3442 0.0433  -0.0776 -0.0723 241  ASN   E N   
13219 C  CA  . ASN   E 241 ? 1.8576 1.4849 1.3462 0.0423  -0.0879 -0.0755 241  ASN   E CA  
13220 C  C   . ASN   E 241 ? 1.9678 1.5771 1.4389 0.0466  -0.0893 -0.0781 241  ASN   E C   
13221 O  O   . ASN   E 241 ? 2.0573 1.6521 1.5081 0.0547  -0.0853 -0.0786 241  ASN   E O   
13222 C  CB  . ASN   E 241 ? 1.8014 1.4199 1.2750 0.0466  -0.0874 -0.0752 241  ASN   E CB  
13223 C  CG  . ASN   E 241 ? 1.7943 1.3976 1.2549 0.0435  -0.1001 -0.0785 241  ASN   E CG  
13224 O  OD1 . ASN   E 241 ? 1.7833 1.3816 1.2455 0.0383  -0.1091 -0.0811 241  ASN   E OD1 
13225 N  ND2 . ASN   E 241 ? 1.7918 1.3877 1.2399 0.0468  -0.1008 -0.0784 241  ASN   E ND2 
13226 N  N   . GLY   E 242 ? 2.0385 1.6480 1.5169 0.0412  -0.0952 -0.0797 242  GLY   E N   
13227 C  CA  . GLY   E 242 ? 2.0664 1.6582 1.5286 0.0443  -0.0977 -0.0824 242  GLY   E CA  
13228 C  C   . GLY   E 242 ? 2.1502 1.7415 1.6067 0.0528  -0.0867 -0.0810 242  GLY   E C   
13229 O  O   . GLY   E 242 ? 2.1222 1.7297 1.5957 0.0525  -0.0798 -0.0788 242  GLY   E O   
13230 N  N   . ASP   E 243 ? 2.1245 1.6969 1.5568 0.0608  -0.0849 -0.0824 243  ASP   E N   
13231 C  CA  . ASP   E 243 ? 2.1592 1.7301 1.5851 0.0696  -0.0741 -0.0812 243  ASP   E CA  
13232 C  C   . ASP   E 243 ? 2.1731 1.7610 1.6113 0.0727  -0.0633 -0.0775 243  ASP   E C   
13233 O  O   . ASP   E 243 ? 2.1990 1.7952 1.6441 0.0772  -0.0540 -0.0758 243  ASP   E O   
13234 C  CB  . ASP   E 243 ? 2.1704 1.7164 1.5667 0.0777  -0.0747 -0.0835 243  ASP   E CB  
13235 N  N   . LYS   E 244 ? 2.1634 1.7568 1.6054 0.0701  -0.0644 -0.0762 244  LYS   E N   
13236 C  CA  . LYS   E 244 ? 2.0662 1.6738 1.5183 0.0731  -0.0542 -0.0727 244  LYS   E CA  
13237 C  C   . LYS   E 244 ? 1.9932 1.6257 1.4745 0.0671  -0.0515 -0.0705 244  LYS   E C   
13238 O  O   . LYS   E 244 ? 1.9079 1.5478 1.4020 0.0590  -0.0592 -0.0712 244  LYS   E O   
13239 C  CB  . LYS   E 244 ? 1.8562 1.4588 1.2996 0.0730  -0.0565 -0.0723 244  LYS   E CB  
13240 N  N   . TYR   E 245 ? 1.9583 1.6036 1.4502 0.0714  -0.0404 -0.0678 245  TYR   E N   
13241 C  CA  . TYR   E 245 ? 1.9223 1.5915 1.4415 0.0668  -0.0370 -0.0655 245  TYR   E CA  
13242 C  C   . TYR   E 245 ? 1.9355 1.6142 1.4609 0.0729  -0.0246 -0.0626 245  TYR   E C   
13243 O  O   . TYR   E 245 ? 1.9773 1.6540 1.4995 0.0796  -0.0173 -0.0624 245  TYR   E O   
13244 C  CB  . TYR   E 245 ? 1.9185 1.5932 1.4481 0.0646  -0.0388 -0.0665 245  TYR   E CB  
13245 C  CG  . TYR   E 245 ? 1.9097 1.6053 1.4620 0.0650  -0.0312 -0.0643 245  TYR   E CG  
13246 C  CD1 . TYR   E 245 ? 1.8954 1.6096 1.4697 0.0581  -0.0330 -0.0628 245  TYR   E CD1 
13247 C  CD2 . TYR   E 245 ? 1.9795 1.6759 1.5311 0.0725  -0.0225 -0.0638 245  TYR   E CD2 
13248 C  CE1 . TYR   E 245 ? 1.9040 1.6366 1.4986 0.0587  -0.0267 -0.0611 245  TYR   E CE1 
13249 C  CE2 . TYR   E 245 ? 2.0246 1.7399 1.5974 0.0730  -0.0163 -0.0621 245  TYR   E CE2 
13250 C  CZ  . TYR   E 245 ? 1.9923 1.7254 1.5863 0.0661  -0.0186 -0.0608 245  TYR   E CZ  
13251 O  OH  . TYR   E 245 ? 1.9379 1.6892 1.5526 0.0669  -0.0130 -0.0594 245  TYR   E OH  
13252 N  N   . LEU   E 246 ? 1.9127 1.6010 1.4466 0.0707  -0.0223 -0.0604 246  LEU   E N   
13253 C  CA  . LEU   E 246 ? 1.8181 1.5178 1.3617 0.0750  -0.0108 -0.0574 246  LEU   E CA  
13254 C  C   . LEU   E 246 ? 1.7511 1.4740 1.3222 0.0686  -0.0104 -0.0556 246  LEU   E C   
13255 O  O   . LEU   E 246 ? 1.7644 1.4921 1.3421 0.0614  -0.0181 -0.0559 246  LEU   E O   
13256 C  CB  . LEU   E 246 ? 1.7774 1.4670 1.3058 0.0787  -0.0075 -0.0561 246  LEU   E CB  
13257 C  CG  . LEU   E 246 ? 1.8587 1.5535 1.3902 0.0855  0.0061  -0.0531 246  LEU   E CG  
13258 C  CD1 . LEU   E 246 ? 1.8477 1.5359 1.3720 0.0934  0.0132  -0.0536 246  LEU   E CD1 
13259 C  CD2 . LEU   E 246 ? 1.8082 1.4913 1.3230 0.0888  0.0086  -0.0518 246  LEU   E CD2 
13260 N  N   . ALA   E 247 ? 1.7746 1.5119 1.3618 0.0714  -0.0016 -0.0538 247  ALA   E N   
13261 C  CA  . ALA   E 247 ? 1.7800 1.5393 1.3936 0.0661  -0.0009 -0.0523 247  ALA   E CA  
13262 C  C   . ALA   E 247 ? 1.7502 1.5210 1.3755 0.0701  0.0103  -0.0495 247  ALA   E C   
13263 O  O   . ALA   E 247 ? 1.7533 1.5211 1.3748 0.0772  0.0186  -0.0491 247  ALA   E O   
13264 C  CB  . ALA   E 247 ? 1.7314 1.4987 1.3573 0.0641  -0.0039 -0.0537 247  ALA   E CB  
13265 N  N   . ILE   E 248 ? 1.7608 1.5447 1.4006 0.0654  0.0107  -0.0476 248  ILE   E N   
13266 C  CA  . ILE   E 248 ? 1.7265 1.5228 1.3802 0.0679  0.0208  -0.0449 248  ILE   E CA  
13267 C  C   . ILE   E 248 ? 1.7149 1.5327 1.3955 0.0627  0.0197  -0.0443 248  ILE   E C   
13268 O  O   . ILE   E 248 ? 1.6844 1.5071 1.3715 0.0560  0.0111  -0.0453 248  ILE   E O   
13269 C  CB  . ILE   E 248 ? 1.6725 1.4632 1.3172 0.0679  0.0231  -0.0429 248  ILE   E CB  
13270 C  CG1 . ILE   E 248 ? 1.7070 1.5130 1.3699 0.0685  0.0326  -0.0399 248  ILE   E CG1 
13271 C  CG2 . ILE   E 248 ? 1.6646 1.4526 1.3055 0.0608  0.0123  -0.0438 248  ILE   E CG2 
13272 C  CD1 . ILE   E 248 ? 1.6771 1.4760 1.3294 0.0697  0.0364  -0.0377 248  ILE   E CD1 
13273 N  N   . ALA   E 249 ? 1.6919 1.5221 1.3884 0.0661  0.0284  -0.0430 249  ALA   E N   
13274 C  CA  . ALA   E 249 ? 1.6894 1.5402 1.4120 0.0620  0.0284  -0.0424 249  ALA   E CA  
13275 C  C   . ALA   E 249 ? 1.7891 1.6495 1.5233 0.0631  0.0372  -0.0395 249  ALA   E C   
13276 O  O   . ALA   E 249 ? 1.7824 1.6511 1.5286 0.0674  0.0455  -0.0387 249  ALA   E O   
13277 C  CB  . ALA   E 249 ? 1.6876 1.5455 1.4210 0.0649  0.0296  -0.0438 249  ALA   E CB  
13278 N  N   . PRO   E 250 ? 1.8685 1.7274 1.5991 0.0595  0.0357  -0.0380 250  PRO   E N   
13279 C  CA  . PRO   E 250 ? 1.8293 1.6967 1.5706 0.0602  0.0441  -0.0352 250  PRO   E CA  
13280 C  C   . PRO   E 250 ? 1.8119 1.7003 1.5808 0.0563  0.0444  -0.0348 250  PRO   E C   
13281 O  O   . PRO   E 250 ? 1.8076 1.7034 1.5855 0.0512  0.0361  -0.0363 250  PRO   E O   
13282 C  CB  . PRO   E 250 ? 1.8505 1.7098 1.5795 0.0566  0.0401  -0.0342 250  PRO   E CB  
13283 C  CG  . PRO   E 250 ? 1.8945 1.7388 1.6038 0.0555  0.0308  -0.0366 250  PRO   E CG  
13284 C  CD  . PRO   E 250 ? 1.8943 1.7435 1.6112 0.0546  0.0263  -0.0389 250  PRO   E CD  
13285 N  N   . PRO   E 251 ? 1.6783 1.5763 1.4612 0.0585  0.0534  -0.0328 251  PRO   E N   
13286 C  CA  . PRO   E 251 ? 1.6608 1.5788 1.4705 0.0551  0.0535  -0.0326 251  PRO   E CA  
13287 C  C   . PRO   E 251 ? 1.6462 1.5713 1.4635 0.0488  0.0504  -0.0311 251  PRO   E C   
13288 O  O   . PRO   E 251 ? 1.6330 1.5716 1.4676 0.0440  0.0455  -0.0317 251  PRO   E O   
13289 C  CB  . PRO   E 251 ? 1.6077 1.5316 1.4286 0.0608  0.0653  -0.0312 251  PRO   E CB  
13290 C  CG  . PRO   E 251 ? 1.6077 1.5161 1.4084 0.0651  0.0724  -0.0292 251  PRO   E CG  
13291 C  CD  . PRO   E 251 ? 1.6302 1.5210 1.4054 0.0651  0.0648  -0.0308 251  PRO   E CD  
13292 N  N   . ILE   E 252 ? 1.5752 1.4902 1.3785 0.0492  0.0532  -0.0292 252  ILE   E N   
13293 C  CA  . ILE   E 252 ? 1.5073 1.4279 1.3164 0.0438  0.0511  -0.0275 252  ILE   E CA  
13294 C  C   . ILE   E 252 ? 1.5793 1.5036 1.3907 0.0372  0.0391  -0.0293 252  ILE   E C   
13295 O  O   . ILE   E 252 ? 1.6611 1.5975 1.4877 0.0322  0.0363  -0.0287 252  ILE   E O   
13296 C  CB  . ILE   E 252 ? 1.5630 1.4690 1.3522 0.0460  0.0549  -0.0255 252  ILE   E CB  
13297 C  CG1 . ILE   E 252 ? 1.5166 1.4291 1.3134 0.0414  0.0548  -0.0234 252  ILE   E CG1 
13298 C  CG2 . ILE   E 252 ? 1.6191 1.5079 1.3840 0.0461  0.0469  -0.0274 252  ILE   E CG2 
13299 C  CD1 . ILE   E 252 ? 1.5240 1.4524 1.3444 0.0410  0.0628  -0.0214 252  ILE   E CD1 
13300 N  N   . ILE   E 253 ? 1.6366 1.5500 1.4331 0.0372  0.0321  -0.0315 253  ILE   E N   
13301 C  CA  . ILE   E 253 ? 1.6278 1.5437 1.4259 0.0310  0.0212  -0.0330 253  ILE   E CA  
13302 C  C   . ILE   E 253 ? 1.6270 1.5568 1.4439 0.0289  0.0183  -0.0343 253  ILE   E C   
13303 O  O   . ILE   E 253 ? 1.6702 1.6034 1.4906 0.0239  0.0100  -0.0354 253  ILE   E O   
13304 C  CB  . ILE   E 253 ? 1.6525 1.5517 1.4288 0.0314  0.0145  -0.0349 253  ILE   E CB  
13305 C  CG1 . ILE   E 253 ? 1.6558 1.5529 1.4311 0.0341  0.0133  -0.0371 253  ILE   E CG1 
13306 C  CG2 . ILE   E 253 ? 1.6459 1.5291 1.4014 0.0360  0.0190  -0.0340 253  ILE   E CG2 
13307 C  CD1 . ILE   E 253 ? 1.6245 1.5066 1.3811 0.0332  0.0055  -0.0392 253  ILE   E CD1 
13308 N  N   . LYS   E 254 ? 1.6416 1.5794 1.4708 0.0329  0.0249  -0.0343 254  LYS   E N   
13309 C  CA  . LYS   E 254 ? 1.6948 1.6435 1.5392 0.0324  0.0220  -0.0360 254  LYS   E CA  
13310 C  C   . LYS   E 254 ? 1.6805 1.6462 1.5469 0.0282  0.0209  -0.0353 254  LYS   E C   
13311 O  O   . LYS   E 254 ? 1.6745 1.6508 1.5561 0.0288  0.0203  -0.0365 254  LYS   E O   
13312 C  CB  . LYS   E 254 ? 1.6652 1.6142 1.5125 0.0391  0.0289  -0.0367 254  LYS   E CB  
13313 N  N   . GLN   E 255 ? 1.7421 1.7103 1.6103 0.0241  0.0203  -0.0335 255  GLN   E N   
13314 C  CA  . GLN   E 255 ? 1.7219 1.7056 1.6104 0.0202  0.0196  -0.0328 255  GLN   E CA  
13315 C  C   . GLN   E 255 ? 1.6929 1.6789 1.5821 0.0139  0.0105  -0.0331 255  GLN   E C   
13316 O  O   . GLN   E 255 ? 1.6727 1.6715 1.5786 0.0108  0.0085  -0.0330 255  GLN   E O   
13317 C  CB  . GLN   E 255 ? 1.7128 1.6993 1.6058 0.0204  0.0269  -0.0302 255  GLN   E CB  
13318 C  CG  . GLN   E 255 ? 1.7637 1.7431 1.6497 0.0265  0.0365  -0.0291 255  GLN   E CG  
13319 C  CD  . GLN   E 255 ? 1.8269 1.8174 1.7311 0.0301  0.0426  -0.0296 255  GLN   E CD  
13320 O  OE1 . GLN   E 255 ? 1.8082 1.8119 1.7308 0.0279  0.0394  -0.0307 255  GLN   E OE1 
13321 N  NE2 . GLN   E 255 ? 1.8170 1.8019 1.7164 0.0359  0.0514  -0.0288 255  GLN   E NE2 
13322 N  N   . SER   E 256 ? 1.5836 1.5576 1.4555 0.0121  0.0052  -0.0335 256  SER   E N   
13323 C  CA  . SER   E 256 ? 1.4702 1.4452 1.3415 0.0062  -0.0031 -0.0337 256  SER   E CA  
13324 C  C   . SER   E 256 ? 1.3905 1.3502 1.2417 0.0060  -0.0081 -0.0348 256  SER   E C   
13325 O  O   . SER   E 256 ? 1.3851 1.3330 1.2216 0.0101  -0.0047 -0.0349 256  SER   E O   
13326 C  CB  . SER   E 256 ? 1.3684 1.3484 1.2448 0.0028  -0.0024 -0.0316 256  SER   E CB  
13327 O  OG  . SER   E 256 ? 1.2675 1.2494 1.1448 -0.0028 -0.0103 -0.0317 256  SER   E OG  
13328 N  N   . THR   E 257 ? 1.3124 1.2721 1.1633 0.0011  -0.0161 -0.0356 257  THR   E N   
13329 C  CA  . THR   E 257 ? 1.3053 1.2517 1.1401 0.0002  -0.0220 -0.0370 257  THR   E CA  
13330 C  C   . THR   E 257 ? 1.2750 1.2120 1.0968 -0.0017 -0.0247 -0.0364 257  THR   E C   
13331 O  O   . THR   E 257 ? 1.3264 1.2696 1.1545 -0.0051 -0.0259 -0.0350 257  THR   E O   
13332 C  CB  . THR   E 257 ? 1.2196 1.1704 1.0611 -0.0042 -0.0290 -0.0381 257  THR   E CB  
13333 O  OG1 . THR   E 257 ? 1.2036 1.1611 1.0547 -0.0017 -0.0269 -0.0389 257  THR   E OG1 
13334 C  CG2 . THR   E 257 ? 1.3170 1.2542 1.1431 -0.0058 -0.0351 -0.0395 257  THR   E CG2 
13335 N  N   . ILE   E 258 ? 1.2512 1.1730 1.0545 0.0007  -0.0260 -0.0375 258  ILE   E N   
13336 C  CA  . ILE   E 258 ? 1.2370 1.1485 1.0267 -0.0008 -0.0296 -0.0373 258  ILE   E CA  
13337 C  C   . ILE   E 258 ? 1.2228 1.1335 1.0130 -0.0067 -0.0392 -0.0385 258  ILE   E C   
13338 O  O   . ILE   E 258 ? 1.2760 1.1814 1.0622 -0.0075 -0.0434 -0.0402 258  ILE   E O   
13339 C  CB  . ILE   E 258 ? 1.2781 1.1727 1.0470 0.0045  -0.0275 -0.0382 258  ILE   E CB  
13340 C  CG1 . ILE   E 258 ? 1.2881 1.1842 1.0582 0.0107  -0.0173 -0.0371 258  ILE   E CG1 
13341 C  CG2 . ILE   E 258 ? 1.3579 1.2428 1.1135 0.0040  -0.0300 -0.0377 258  ILE   E CG2 
13342 C  CD1 . ILE   E 258 ? 1.3174 1.2205 1.0946 0.0115  -0.0107 -0.0346 258  ILE   E CD1 
13343 N  N   . VAL   E 259 ? 1.2644 1.1805 1.0603 -0.0110 -0.0425 -0.0374 259  VAL   E N   
13344 C  CA  . VAL   E 259 ? 1.2840 1.2019 1.0839 -0.0169 -0.0510 -0.0381 259  VAL   E CA  
13345 C  C   . VAL   E 259 ? 1.2916 1.1991 1.0790 -0.0187 -0.0570 -0.0387 259  VAL   E C   
13346 O  O   . VAL   E 259 ? 1.3114 1.2174 1.0996 -0.0233 -0.0646 -0.0398 259  VAL   E O   
13347 C  CB  . VAL   E 259 ? 1.2641 1.1985 1.0836 -0.0210 -0.0512 -0.0367 259  VAL   E CB  
13348 C  CG1 . VAL   E 259 ? 1.2606 1.2042 1.0921 -0.0196 -0.0475 -0.0367 259  VAL   E CG1 
13349 C  CG2 . VAL   E 259 ? 1.2555 1.1957 1.0791 -0.0204 -0.0471 -0.0347 259  VAL   E CG2 
13350 N  N   . CYS   E 260 ? 1.2337 1.1336 1.0095 -0.0152 -0.0540 -0.0380 260  CYS   E N   
13351 C  CA  . CYS   E 260 ? 1.2991 1.1872 1.0611 -0.0163 -0.0606 -0.0391 260  CYS   E CA  
13352 C  C   . CYS   E 260 ? 1.3658 1.2390 1.1080 -0.0101 -0.0569 -0.0393 260  CYS   E C   
13353 O  O   . CYS   E 260 ? 1.3383 1.2129 1.0799 -0.0055 -0.0481 -0.0378 260  CYS   E O   
13354 C  CB  . CYS   E 260 ? 1.3317 1.2273 1.1013 -0.0201 -0.0638 -0.0378 260  CYS   E CB  
13355 S  SG  . CYS   E 260 ? 1.3378 1.2445 1.1170 -0.0178 -0.0542 -0.0346 260  CYS   E SG  
13356 N  N   . HIS   E 261 ? 1.4051 1.2637 1.1311 -0.0100 -0.0638 -0.0413 261  HIS   E N   
13357 C  CA  . HIS   E 261 ? 1.3840 1.2254 1.0881 -0.0040 -0.0619 -0.0421 261  HIS   E CA  
13358 C  C   . HIS   E 261 ? 1.3957 1.2271 1.0879 -0.0050 -0.0696 -0.0431 261  HIS   E C   
13359 O  O   . HIS   E 261 ? 1.3430 1.1804 1.0441 -0.0106 -0.0770 -0.0436 261  HIS   E O   
13360 C  CB  . HIS   E 261 ? 1.4022 1.2326 1.0959 -0.0017 -0.0633 -0.0444 261  HIS   E CB  
13361 C  CG  . HIS   E 261 ? 1.4095 1.2339 1.1006 -0.0063 -0.0742 -0.0471 261  HIS   E CG  
13362 N  ND1 . HIS   E 261 ? 1.3594 1.1664 1.0313 -0.0048 -0.0809 -0.0495 261  HIS   E ND1 
13363 C  CD2 . HIS   E 261 ? 1.4052 1.2385 1.1107 -0.0125 -0.0796 -0.0478 261  HIS   E CD2 
13364 C  CE1 . HIS   E 261 ? 1.3628 1.1687 1.0386 -0.0101 -0.0900 -0.0515 261  HIS   E CE1 
13365 N  NE2 . HIS   E 261 ? 1.3994 1.2211 1.0954 -0.0148 -0.0890 -0.0504 261  HIS   E NE2 
13366 N  N   . ASN   E 262 ? 1.4170 1.2329 1.0887 0.0007  -0.0677 -0.0434 262  ASN   E N   
13367 C  CA  . ASN   E 262 ? 1.3843 1.1880 1.0417 0.0006  -0.0759 -0.0449 262  ASN   E CA  
13368 C  C   . ASN   E 262 ? 1.4658 1.2494 1.0978 0.0080  -0.0736 -0.0459 262  ASN   E C   
13369 O  O   . ASN   E 262 ? 1.4508 1.2327 1.0781 0.0134  -0.0634 -0.0441 262  ASN   E O   
13370 C  CB  . ASN   E 262 ? 1.3866 1.1977 1.0502 -0.0009 -0.0754 -0.0428 262  ASN   E CB  
13371 C  CG  . ASN   E 262 ? 1.4330 1.2325 1.0835 -0.0013 -0.0851 -0.0446 262  ASN   E CG  
13372 O  OD1 . ASN   E 262 ? 1.4002 1.1916 1.0379 0.0027  -0.0832 -0.0436 262  ASN   E OD1 
13373 N  ND2 . ASN   E 262 ? 1.4495 1.2473 1.1026 -0.0060 -0.0957 -0.0474 262  ASN   E ND2 
13374 N  N   . ARG   E 263 ? 1.5409 1.3094 1.1571 0.0082  -0.0833 -0.0487 263  ARG   E N   
13375 C  CA  . ARG   E 263 ? 1.5777 1.3250 1.1675 0.0154  -0.0826 -0.0500 263  ARG   E CA  
13376 C  C   . ARG   E 263 ? 1.5720 1.3122 1.1495 0.0191  -0.0812 -0.0486 263  ARG   E C   
13377 O  O   . ARG   E 263 ? 1.5053 1.2447 1.0827 0.0161  -0.0899 -0.0496 263  ARG   E O   
13378 C  CB  . ARG   E 263 ? 1.6143 1.3477 1.1924 0.0141  -0.0941 -0.0542 263  ARG   E CB  
13379 C  CG  . ARG   E 263 ? 1.7519 1.4618 1.3011 0.0209  -0.0969 -0.0560 263  ARG   E CG  
13380 C  CD  . ARG   E 263 ? 1.6927 1.3880 1.2296 0.0211  -0.1053 -0.0600 263  ARG   E CD  
13381 N  NE  . ARG   E 263 ? 1.6250 1.3283 1.1775 0.0128  -0.1158 -0.0621 263  ARG   E NE  
13382 C  CZ  . ARG   E 263 ? 1.6010 1.3019 1.1537 0.0092  -0.1268 -0.0641 263  ARG   E CZ  
13383 N  NH1 . ARG   E 263 ? 1.6264 1.3169 1.1638 0.0131  -0.1294 -0.0643 263  ARG   E NH1 
13384 N  NH2 . ARG   E 263 ? 1.5697 1.2788 1.1385 0.0016  -0.1353 -0.0658 263  ARG   E NH2 
13385 N  N   . VAL   E 264 ? 1.6222 1.3574 1.1899 0.0258  -0.0701 -0.0462 264  VAL   E N   
13386 C  CA  . VAL   E 264 ? 1.6538 1.3787 1.2058 0.0306  -0.0677 -0.0447 264  VAL   E CA  
13387 C  C   . VAL   E 264 ? 1.8914 1.5941 1.4180 0.0340  -0.0775 -0.0481 264  VAL   E C   
13388 O  O   . VAL   E 264 ? 1.9251 1.6250 1.4497 0.0311  -0.0880 -0.0499 264  VAL   E O   
13389 C  CB  . VAL   E 264 ? 1.6356 1.3581 1.1813 0.0375  -0.0529 -0.0414 264  VAL   E CB  
13390 C  CG1 . VAL   E 264 ? 1.6302 1.3494 1.1688 0.0403  -0.0490 -0.0388 264  VAL   E CG1 
13391 C  CG2 . VAL   E 264 ? 1.5881 1.3301 1.1576 0.0348  -0.0441 -0.0392 264  VAL   E CG2 
13392 N  N   . ASP   E 265 ? 2.2367 1.9233 1.7440 0.0403  -0.0744 -0.0492 265  ASP   E N   
13393 C  CA  . ASP   E 265 ? 2.2801 1.9436 1.7610 0.0445  -0.0834 -0.0526 265  ASP   E CA  
13394 C  C   . ASP   E 265 ? 2.2643 1.9259 1.7487 0.0395  -0.0954 -0.0568 265  ASP   E C   
13395 O  O   . ASP   E 265 ? 2.2443 1.9157 1.7426 0.0363  -0.0931 -0.0569 265  ASP   E O   
13396 C  CB  . ASP   E 265 ? 2.3171 1.9626 1.7739 0.0541  -0.0745 -0.0519 265  ASP   E CB  
13397 C  CG  . ASP   E 265 ? 2.3297 1.9837 1.7968 0.0551  -0.0640 -0.0504 265  ASP   E CG  
13398 O  OD1 . ASP   E 265 ? 2.3141 1.9738 1.7917 0.0506  -0.0692 -0.0526 265  ASP   E OD1 
13399 O  OD2 . ASP   E 265 ? 2.3538 2.0094 1.8197 0.0601  -0.0507 -0.0470 265  ASP   E OD2 
13400 N  N   . PRO   E 266 ? 2.0920 1.7408 1.5641 0.0387  -0.1085 -0.0603 266  PRO   E N   
13401 C  CA  . PRO   E 266 ? 2.0348 1.6807 1.5102 0.0339  -0.1201 -0.0644 266  PRO   E CA  
13402 C  C   . PRO   E 266 ? 1.9485 1.5798 1.4084 0.0384  -0.1185 -0.0664 266  PRO   E C   
13403 O  O   . PRO   E 266 ? 1.8579 1.4865 1.3206 0.0344  -0.1274 -0.0697 266  PRO   E O   
13404 C  CB  . PRO   E 266 ? 1.9464 1.5805 1.4105 0.0332  -0.1338 -0.0676 266  PRO   E CB  
13405 C  CG  . PRO   E 266 ? 1.9481 1.5891 1.4154 0.0340  -0.1302 -0.0647 266  PRO   E CG  
13406 C  CD  . PRO   E 266 ? 2.0443 1.6856 1.5058 0.0403  -0.1142 -0.0606 266  PRO   E CD  
13407 N  N   . ASN   E 267 ? 1.9923 1.6144 1.4365 0.0465  -0.1074 -0.0645 267  ASN   E N   
13408 C  CA  . ASN   E 267 ? 1.9969 1.6056 1.4267 0.0512  -0.1051 -0.0661 267  ASN   E CA  
13409 C  C   . ASN   E 267 ? 1.9203 1.5436 1.3668 0.0502  -0.0943 -0.0638 267  ASN   E C   
13410 O  O   . ASN   E 267 ? 1.8957 1.5110 1.3350 0.0523  -0.0940 -0.0655 267  ASN   E O   
13411 C  CB  . ASN   E 267 ? 2.0655 1.6513 1.4641 0.0617  -0.1003 -0.0660 267  ASN   E CB  
13412 C  CG  . ASN   E 267 ? 2.1195 1.7102 1.5174 0.0660  -0.0883 -0.0614 267  ASN   E CG  
13413 O  OD1 . ASN   E 267 ? 2.1018 1.7133 1.5231 0.0613  -0.0829 -0.0584 267  ASN   E OD1 
13414 N  ND2 . ASN   E 267 ? 2.1015 1.6721 1.4722 0.0752  -0.0839 -0.0609 267  ASN   E ND2 
13415 N  N   . GLY   E 268 ? 1.9431 1.5870 1.4112 0.0473  -0.0859 -0.0601 268  GLY   E N   
13416 C  CA  . GLY   E 268 ? 1.8586 1.5184 1.3459 0.0452  -0.0777 -0.0583 268  GLY   E CA  
13417 C  C   . GLY   E 268 ? 1.8226 1.4857 1.3092 0.0515  -0.0624 -0.0548 268  GLY   E C   
13418 O  O   . GLY   E 268 ? 1.7741 1.4517 1.2783 0.0499  -0.0557 -0.0533 268  GLY   E O   
13419 N  N   . SER   E 269 ? 1.8556 1.5057 1.3230 0.0588  -0.0565 -0.0533 269  SER   E N   
13420 C  CA  . SER   E 269 ? 1.8214 1.4736 1.2880 0.0651  -0.0413 -0.0499 269  SER   E CA  
13421 C  C   . SER   E 269 ? 1.7920 1.4684 1.2863 0.0609  -0.0334 -0.0463 269  SER   E C   
13422 O  O   . SER   E 269 ? 1.7679 1.4534 1.2726 0.0630  -0.0229 -0.0443 269  SER   E O   
13423 C  CB  . SER   E 269 ? 1.8544 1.4881 1.2955 0.0735  -0.0364 -0.0486 269  SER   E CB  
13424 O  OG  . SER   E 269 ? 1.9556 1.5983 1.4049 0.0722  -0.0322 -0.0455 269  SER   E OG  
13425 N  N   . ARG   E 270 ? 1.8462 1.5331 1.3527 0.0551  -0.0384 -0.0456 270  ARG   E N   
13426 C  CA  . ARG   E 270 ? 1.7482 1.4562 1.2786 0.0515  -0.0311 -0.0422 270  ARG   E CA  
13427 C  C   . ARG   E 270 ? 1.6600 1.3851 1.2132 0.0421  -0.0400 -0.0433 270  ARG   E C   
13428 O  O   . ARG   E 270 ? 1.6718 1.3921 1.2209 0.0383  -0.0517 -0.0457 270  ARG   E O   
13429 C  CB  . ARG   E 270 ? 1.7218 1.4257 1.2442 0.0546  -0.0263 -0.0395 270  ARG   E CB  
13430 N  N   . TYR   E 271 ? 1.6068 1.3515 1.1840 0.0387  -0.0345 -0.0416 271  TYR   E N   
13431 C  CA  . TYR   E 271 ? 1.5633 1.3257 1.1636 0.0302  -0.0408 -0.0420 271  TYR   E CA  
13432 C  C   . TYR   E 271 ? 1.4992 1.2803 1.1202 0.0284  -0.0325 -0.0386 271  TYR   E C   
13433 O  O   . TYR   E 271 ? 1.5328 1.3157 1.1547 0.0331  -0.0213 -0.0363 271  TYR   E O   
13434 C  CB  . TYR   E 271 ? 1.5567 1.3241 1.1663 0.0272  -0.0444 -0.0441 271  TYR   E CB  
13435 C  CG  . TYR   E 271 ? 1.5662 1.3193 1.1619 0.0259  -0.0557 -0.0478 271  TYR   E CG  
13436 C  CD1 . TYR   E 271 ? 1.5160 1.2728 1.1190 0.0189  -0.0668 -0.0495 271  TYR   E CD1 
13437 C  CD2 . TYR   E 271 ? 1.6200 1.3556 1.1956 0.0315  -0.0553 -0.0497 271  TYR   E CD2 
13438 C  CE1 . TYR   E 271 ? 1.5665 1.3104 1.1581 0.0174  -0.0773 -0.0529 271  TYR   E CE1 
13439 C  CE2 . TYR   E 271 ? 1.6052 1.3272 1.1683 0.0301  -0.0660 -0.0532 271  TYR   E CE2 
13440 C  CZ  . TYR   E 271 ? 1.6421 1.3685 1.2137 0.0229  -0.0770 -0.0549 271  TYR   E CZ  
13441 O  OH  . TYR   E 271 ? 1.6511 1.3643 1.2118 0.0212  -0.0878 -0.0585 271  TYR   E OH  
13442 N  N   . LEU   E 272 ? 1.4696 1.2644 1.1076 0.0216  -0.0380 -0.0383 272  LEU   E N   
13443 C  CA  . LEU   E 272 ? 1.4313 1.2444 1.0904 0.0191  -0.0314 -0.0354 272  LEU   E CA  
13444 C  C   . LEU   E 272 ? 1.4100 1.2395 1.0909 0.0139  -0.0334 -0.0360 272  LEU   E C   
13445 O  O   . LEU   E 272 ? 1.4233 1.2541 1.1078 0.0090  -0.0429 -0.0381 272  LEU   E O   
13446 C  CB  . LEU   E 272 ? 1.3997 1.2160 1.0611 0.0161  -0.0352 -0.0342 272  LEU   E CB  
13447 C  CG  . LEU   E 272 ? 1.3744 1.1864 1.0281 0.0208  -0.0263 -0.0313 272  LEU   E CG  
13448 C  CD1 . LEU   E 272 ? 1.4744 1.2669 1.1036 0.0288  -0.0214 -0.0315 272  LEU   E CD1 
13449 C  CD2 . LEU   E 272 ? 1.3522 1.1632 1.0033 0.0183  -0.0322 -0.0309 272  LEU   E CD2 
13450 N  N   . LEU   E 273 ? 1.3707 1.2121 1.0660 0.0151  -0.0245 -0.0343 273  LEU   E N   
13451 C  CA  . LEU   E 273 ? 1.3611 1.2177 1.0765 0.0111  -0.0255 -0.0348 273  LEU   E CA  
13452 C  C   . LEU   E 273 ? 1.3401 1.2144 1.0764 0.0079  -0.0218 -0.0324 273  LEU   E C   
13453 O  O   . LEU   E 273 ? 1.3392 1.2154 1.0767 0.0108  -0.0138 -0.0301 273  LEU   E O   
13454 C  CB  . LEU   E 273 ? 1.3414 1.1971 1.0569 0.0156  -0.0192 -0.0353 273  LEU   E CB  
13455 C  CG  . LEU   E 273 ? 1.4231 1.2596 1.1158 0.0203  -0.0208 -0.0372 273  LEU   E CG  
13456 C  CD1 . LEU   E 273 ? 1.4578 1.2935 1.1500 0.0260  -0.0122 -0.0370 273  LEU   E CD1 
13457 C  CD2 . LEU   E 273 ? 1.3914 1.2230 1.0805 0.0159  -0.0319 -0.0401 273  LEU   E CD2 
13458 N  N   . GLY   E 274 ? 1.2693 1.1559 1.0216 0.0022  -0.0273 -0.0330 274  GLY   E N   
13459 C  CA  . GLY   E 274 ? 1.2816 1.1853 1.0544 -0.0010 -0.0246 -0.0311 274  GLY   E CA  
13460 C  C   . GLY   E 274 ? 1.2631 1.1794 1.0529 -0.0033 -0.0251 -0.0319 274  GLY   E C   
13461 O  O   . GLY   E 274 ? 1.2547 1.1690 1.0437 -0.0058 -0.0317 -0.0338 274  GLY   E O   
13462 N  N   . ASP   E 275 ? 1.2238 1.1528 1.0295 -0.0025 -0.0183 -0.0304 275  ASP   E N   
13463 C  CA  . ASP   E 275 ? 1.2220 1.1636 1.0446 -0.0039 -0.0181 -0.0310 275  ASP   E CA  
13464 C  C   . ASP   E 275 ? 1.2126 1.1684 1.0524 -0.0092 -0.0212 -0.0301 275  ASP   E C   
13465 O  O   . ASP   E 275 ? 1.2393 1.1957 1.0786 -0.0116 -0.0228 -0.0288 275  ASP   E O   
13466 C  CB  . ASP   E 275 ? 1.2533 1.1991 1.0823 0.0012  -0.0088 -0.0304 275  ASP   E CB  
13467 C  CG  . ASP   E 275 ? 1.2672 1.2225 1.1080 0.0014  -0.0021 -0.0280 275  ASP   E CG  
13468 O  OD1 . ASP   E 275 ? 1.2914 1.2473 1.1316 -0.0015 -0.0040 -0.0267 275  ASP   E OD1 
13469 O  OD2 . ASP   E 275 ? 1.2301 1.1922 1.0813 0.0045  0.0051  -0.0275 275  ASP   E OD2 
13470 N  N   . MET   E 276 ? 1.1524 1.1193 1.0072 -0.0106 -0.0221 -0.0307 276  MET   E N   
13471 C  CA  . MET   E 276 ? 1.1854 1.1650 1.0557 -0.0154 -0.0256 -0.0301 276  MET   E CA  
13472 C  C   . MET   E 276 ? 1.2042 1.1946 1.0879 -0.0151 -0.0197 -0.0283 276  MET   E C   
13473 O  O   . MET   E 276 ? 1.1653 1.1672 1.0633 -0.0183 -0.0218 -0.0279 276  MET   E O   
13474 C  CB  . MET   E 276 ? 1.1764 1.1623 1.0560 -0.0167 -0.0289 -0.0316 276  MET   E CB  
13475 C  CG  . MET   E 276 ? 1.2370 1.2120 1.1041 -0.0162 -0.0330 -0.0334 276  MET   E CG  
13476 S  SD  . MET   E 276 ? 1.2286 1.2102 1.1060 -0.0170 -0.0360 -0.0348 276  MET   E SD  
13477 C  CE  . MET   E 276 ? 1.1410 1.1340 1.0329 -0.0127 -0.0286 -0.0345 276  MET   E CE  
13478 N  N   . GLU   E 277 ? 1.2014 1.1881 1.0808 -0.0111 -0.0123 -0.0271 277  GLU   E N   
13479 C  CA  . GLU   E 277 ? 1.1393 1.1357 1.0318 -0.0108 -0.0061 -0.0253 277  GLU   E CA  
13480 C  C   . GLU   E 277 ? 1.2425 1.2318 1.1252 -0.0096 -0.0020 -0.0232 277  GLU   E C   
13481 O  O   . GLU   E 277 ? 1.2607 1.2561 1.1526 -0.0089 0.0045  -0.0214 277  GLU   E O   
13482 C  CB  . GLU   E 277 ? 1.1331 1.1354 1.0358 -0.0067 0.0008  -0.0256 277  GLU   E CB  
13483 C  CG  . GLU   E 277 ? 1.1760 1.1871 1.0909 -0.0075 -0.0030 -0.0276 277  GLU   E CG  
13484 C  CD  . GLU   E 277 ? 1.3277 1.3429 1.2508 -0.0027 0.0031  -0.0284 277  GLU   E CD  
13485 O  OE1 . GLU   E 277 ? 1.3948 1.4064 1.3148 0.0010  0.0108  -0.0273 277  GLU   E OE1 
13486 O  OE2 . GLU   E 277 ? 1.3713 1.3931 1.3038 -0.0025 0.0004  -0.0301 277  GLU   E OE2 
13487 N  N   . GLY   E 278 ? 1.2311 1.2071 1.0952 -0.0094 -0.0056 -0.0234 278  GLY   E N   
13488 C  CA  . GLY   E 278 ? 1.2219 1.1898 1.0749 -0.0081 -0.0024 -0.0216 278  GLY   E CA  
13489 C  C   . GLY   E 278 ? 1.2705 1.2248 1.1068 -0.0022 0.0040  -0.0212 278  GLY   E C   
13490 O  O   . GLY   E 278 ? 1.2853 1.2307 1.1095 -0.0004 0.0066  -0.0196 278  GLY   E O   
13491 N  N   . ARG   E 279 ? 1.2909 1.2429 1.1258 0.0012  0.0068  -0.0224 279  ARG   E N   
13492 C  CA  . ARG   E 279 ? 1.2787 1.2171 1.0968 0.0072  0.0129  -0.0221 279  ARG   E CA  
13493 C  C   . ARG   E 279 ? 1.2761 1.1980 1.0715 0.0076  0.0065  -0.0232 279  ARG   E C   
13494 O  O   . ARG   E 279 ? 1.2406 1.1607 1.0331 0.0045  -0.0026 -0.0253 279  ARG   E O   
13495 C  CB  . ARG   E 279 ? 1.2539 1.1935 1.0754 0.0106  0.0162  -0.0235 279  ARG   E CB  
13496 C  CG  . ARG   E 279 ? 1.1973 1.1456 1.0328 0.0139  0.0267  -0.0221 279  ARG   E CG  
13497 C  CD  . ARG   E 279 ? 1.2480 1.2111 1.1038 0.0120  0.0246  -0.0235 279  ARG   E CD  
13498 N  NE  . ARG   E 279 ? 1.3220 1.2963 1.1955 0.0141  0.0331  -0.0225 279  ARG   E NE  
13499 C  CZ  . ARG   E 279 ? 1.3866 1.3738 1.2785 0.0134  0.0323  -0.0238 279  ARG   E CZ  
13500 N  NH1 . ARG   E 279 ? 1.4118 1.4022 1.3064 0.0107  0.0238  -0.0260 279  ARG   E NH1 
13501 N  NH2 . ARG   E 279 ? 1.3855 1.3823 1.2937 0.0155  0.0400  -0.0229 279  ARG   E NH2 
13502 N  N   . LEU   E 280 ? 1.2988 1.2083 1.0781 0.0117  0.0112  -0.0218 280  LEU   E N   
13503 C  CA  . LEU   E 280 ? 1.3668 1.2585 1.1222 0.0135  0.0059  -0.0230 280  LEU   E CA  
13504 C  C   . LEU   E 280 ? 1.4160 1.2948 1.1562 0.0205  0.0126  -0.0232 280  LEU   E C   
13505 O  O   . LEU   E 280 ? 1.4190 1.2928 1.1534 0.0250  0.0220  -0.0209 280  LEU   E O   
13506 C  CB  . LEU   E 280 ? 1.3201 1.2059 1.0666 0.0130  0.0049  -0.0214 280  LEU   E CB  
13507 C  CG  . LEU   E 280 ? 1.3236 1.1910 1.0457 0.0149  -0.0020 -0.0230 280  LEU   E CG  
13508 C  CD1 . LEU   E 280 ? 1.2486 1.1170 0.9724 0.0102  -0.0138 -0.0261 280  LEU   E CD1 
13509 C  CD2 . LEU   E 280 ? 1.3021 1.1626 1.0140 0.0152  -0.0028 -0.0215 280  LEU   E CD2 
13510 N  N   . PHE   E 281 ? 1.3825 1.2555 1.1160 0.0214  0.0083  -0.0258 281  PHE   E N   
13511 C  CA  . PHE   E 281 ? 1.4063 1.2656 1.1234 0.0281  0.0136  -0.0262 281  PHE   E CA  
13512 C  C   . PHE   E 281 ? 1.4487 1.2878 1.1394 0.0305  0.0079  -0.0276 281  PHE   E C   
13513 O  O   . PHE   E 281 ? 1.4361 1.2720 1.1221 0.0264  -0.0020 -0.0290 281  PHE   E O   
13514 C  CB  . PHE   E 281 ? 1.4163 1.2793 1.1395 0.0285  0.0125  -0.0283 281  PHE   E CB  
13515 C  CG  . PHE   E 281 ? 1.3775 1.2598 1.1261 0.0258  0.0153  -0.0278 281  PHE   E CG  
13516 C  CD1 . PHE   E 281 ? 1.3191 1.2136 1.0827 0.0193  0.0078  -0.0286 281  PHE   E CD1 
13517 C  CD2 . PHE   E 281 ? 1.4213 1.3092 1.1788 0.0301  0.0252  -0.0267 281  PHE   E CD2 
13518 C  CE1 . PHE   E 281 ? 1.3477 1.2590 1.1336 0.0172  0.0099  -0.0283 281  PHE   E CE1 
13519 C  CE2 . PHE   E 281 ? 1.4195 1.3249 1.2004 0.0279  0.0270  -0.0266 281  PHE   E CE2 
13520 C  CZ  . PHE   E 281 ? 1.4019 1.3186 1.1964 0.0216  0.0192  -0.0275 281  PHE   E CZ  
13521 N  N   . MET   E 282 ? 1.5243 1.3492 1.1977 0.0374  0.0142  -0.0274 282  MET   E N   
13522 C  CA  . MET   E 282 ? 1.5596 1.3633 1.2059 0.0410  0.0094  -0.0291 282  MET   E CA  
13523 C  C   . MET   E 282 ? 1.5898 1.3849 1.2269 0.0447  0.0091  -0.0314 282  MET   E C   
13524 O  O   . MET   E 282 ? 1.6145 1.4087 1.2512 0.0501  0.0190  -0.0302 282  MET   E O   
13525 C  CB  . MET   E 282 ? 1.6471 1.4381 1.2765 0.0471  0.0173  -0.0267 282  MET   E CB  
13526 C  CG  . MET   E 282 ? 1.6917 1.4595 1.2916 0.0514  0.0118  -0.0286 282  MET   E CG  
13527 S  SD  . MET   E 282 ? 1.6562 1.4204 1.2509 0.0452  -0.0038 -0.0309 282  MET   E SD  
13528 C  CE  . MET   E 282 ? 1.5978 1.3467 1.1714 0.0508  0.0008  -0.0286 282  MET   E CE  
13529 N  N   . LEU   E 283 ? 1.5594 1.3480 1.1893 0.0418  -0.0019 -0.0345 283  LEU   E N   
13530 C  CA  . LEU   E 283 ? 1.6043 1.3814 1.2216 0.0454  -0.0033 -0.0369 283  LEU   E CA  
13531 C  C   . LEU   E 283 ? 1.6731 1.4270 1.2611 0.0513  -0.0043 -0.0377 283  LEU   E C   
13532 O  O   . LEU   E 283 ? 1.6444 1.3898 1.2214 0.0495  -0.0121 -0.0386 283  LEU   E O   
13533 C  CB  . LEU   E 283 ? 1.5523 1.3334 1.1767 0.0394  -0.0144 -0.0398 283  LEU   E CB  
13534 C  CG  . LEU   E 283 ? 1.5773 1.3491 1.1924 0.0426  -0.0151 -0.0421 283  LEU   E CG  
13535 C  CD1 . LEU   E 283 ? 1.5614 1.3407 1.1855 0.0473  -0.0038 -0.0406 283  LEU   E CD1 
13536 C  CD2 . LEU   E 283 ? 1.5724 1.3480 1.1951 0.0364  -0.0255 -0.0447 283  LEU   E CD2 
13537 N  N   . LEU   E 284 ? 1.6685 1.4117 1.2434 0.0587  0.0035  -0.0374 284  LEU   E N   
13538 C  CA  . LEU   E 284 ? 1.6930 1.4128 1.2385 0.0653  0.0034  -0.0383 284  LEU   E CA  
13539 C  C   . LEU   E 284 ? 1.6843 1.3923 1.2173 0.0679  -0.0006 -0.0413 284  LEU   E C   
13540 O  O   . LEU   E 284 ? 1.6921 1.4076 1.2355 0.0690  0.0043  -0.0413 284  LEU   E O   
13541 C  CB  . LEU   E 284 ? 1.6747 1.3893 1.2122 0.0729  0.0173  -0.0349 284  LEU   E CB  
13542 C  CG  . LEU   E 284 ? 1.7129 1.4378 1.2616 0.0709  0.0225  -0.0316 284  LEU   E CG  
13543 C  CD1 . LEU   E 284 ? 1.7249 1.4620 1.2894 0.0738  0.0369  -0.0283 284  LEU   E CD1 
13544 C  CD2 . LEU   E 284 ? 1.7677 1.4739 1.2916 0.0752  0.0220  -0.0308 284  LEU   E CD2 
13545 N  N   . LEU   E 285 ? 1.7073 1.3966 1.2183 0.0690  -0.0099 -0.0441 285  LEU   E N   
13546 C  CA  . LEU   E 285 ? 1.7330 1.4069 1.2272 0.0727  -0.0134 -0.0470 285  LEU   E CA  
13547 C  C   . LEU   E 285 ? 1.8880 1.5410 1.3549 0.0824  -0.0066 -0.0463 285  LEU   E C   
13548 O  O   . LEU   E 285 ? 1.9171 1.5549 1.3646 0.0844  -0.0114 -0.0470 285  LEU   E O   
13549 C  CB  . LEU   E 285 ? 1.7089 1.3760 1.1980 0.0671  -0.0288 -0.0509 285  LEU   E CB  
13550 C  CG  . LEU   E 285 ? 1.7236 1.4072 1.2358 0.0590  -0.0347 -0.0521 285  LEU   E CG  
13551 C  CD1 . LEU   E 285 ? 1.7053 1.4126 1.2446 0.0546  -0.0289 -0.0491 285  LEU   E CD1 
13552 C  CD2 . LEU   E 285 ? 1.6664 1.3456 1.1768 0.0525  -0.0494 -0.0552 285  LEU   E CD2 
13553 N  N   . GLU   E 286 ? 1.9601 1.6123 1.4257 0.0887  0.0048  -0.0448 286  GLU   E N   
13554 C  CA  . GLU   E 286 ? 1.9987 1.6315 1.4391 0.0986  0.0131  -0.0438 286  GLU   E CA  
13555 C  C   . GLU   E 286 ? 2.0118 1.6224 1.4268 0.1023  0.0051  -0.0476 286  GLU   E C   
13556 O  O   . GLU   E 286 ? 2.0084 1.6199 1.4267 0.1021  0.0034  -0.0495 286  GLU   E O   
13557 C  CB  . GLU   E 286 ? 1.9990 1.6404 1.4495 0.1038  0.0285  -0.0407 286  GLU   E CB  
13558 N  N   . LYS   E 287 ? 1.9100 1.5003 1.2995 0.1058  -0.0002 -0.0488 287  LYS   E N   
13559 C  CA  . LYS   E 287 ? 1.9633 1.5316 1.3282 0.1083  -0.0103 -0.0529 287  LYS   E CA  
13560 C  C   . LYS   E 287 ? 2.0980 1.6445 1.4350 0.1196  -0.0020 -0.0525 287  LYS   E C   
13561 O  O   . LYS   E 287 ? 2.0909 1.6355 1.4227 0.1257  0.0103  -0.0489 287  LYS   E O   
13562 C  CB  . LYS   E 287 ? 1.9486 1.5077 1.3030 0.1048  -0.0235 -0.0552 287  LYS   E CB  
13563 N  N   . GLU   E 288 ? 2.1839 1.7126 1.5018 0.1225  -0.0091 -0.0562 288  GLU   E N   
13564 C  CA  . GLU   E 288 ? 2.1562 1.6632 1.4469 0.1333  -0.0023 -0.0564 288  GLU   E CA  
13565 C  C   . GLU   E 288 ? 2.2449 1.7244 1.5037 0.1369  -0.0138 -0.0602 288  GLU   E C   
13566 O  O   . GLU   E 288 ? 2.2517 1.7220 1.5031 0.1354  -0.0239 -0.0643 288  GLU   E O   
13567 C  CB  . GLU   E 288 ? 2.0552 1.5669 1.3537 0.1344  0.0016  -0.0572 288  GLU   E CB  
13568 N  N   . GLU   E 289 ? 2.2647 1.7307 1.5042 0.1421  -0.0120 -0.0590 289  GLU   E N   
13569 C  CA  . GLU   E 289 ? 2.2342 1.6729 1.4415 0.1466  -0.0226 -0.0625 289  GLU   E CA  
13570 C  C   . GLU   E 289 ? 2.2650 1.6811 1.4452 0.1569  -0.0177 -0.0636 289  GLU   E C   
13571 O  O   . GLU   E 289 ? 2.2862 1.6907 1.4490 0.1664  -0.0056 -0.0607 289  GLU   E O   
13572 C  CB  . GLU   E 289 ? 2.1357 1.5671 1.3307 0.1498  -0.0207 -0.0604 289  GLU   E CB  
13573 N  N   . GLN   E 290 ? 2.2886 1.6973 1.4641 0.1552  -0.0272 -0.0678 290  GLN   E N   
13574 C  CA  . GLN   E 290 ? 2.3196 1.7077 1.4709 0.1643  -0.0235 -0.0693 290  GLN   E CA  
13575 C  C   . GLN   E 290 ? 2.3336 1.6903 1.4476 0.1711  -0.0327 -0.0728 290  GLN   E C   
13576 O  O   . GLN   E 290 ? 2.3434 1.6947 1.4516 0.1681  -0.0435 -0.0745 290  GLN   E O   
13577 C  CB  . GLN   E 290 ? 2.3027 1.6982 1.4674 0.1593  -0.0288 -0.0720 290  GLN   E CB  
13578 C  CG  . GLN   E 290 ? 2.2452 1.6698 1.4444 0.1540  -0.0194 -0.0687 290  GLN   E CG  
13579 C  CD  . GLN   E 290 ? 2.2538 1.6850 1.4654 0.1493  -0.0245 -0.0714 290  GLN   E CD  
13580 O  OE1 . GLN   E 290 ? 2.2645 1.6923 1.4767 0.1429  -0.0389 -0.0753 290  GLN   E OE1 
13581 N  NE2 . GLN   E 290 ? 2.2074 1.6480 1.4293 0.1526  -0.0128 -0.0692 290  GLN   E NE2 
13582 N  N   . MET   E 291 ? 2.3295 1.6645 1.4173 0.1809  -0.0285 -0.0738 291  MET   E N   
13583 C  CA  . MET   E 291 ? 2.3065 1.6101 1.3570 0.1884  -0.0368 -0.0771 291  MET   E CA  
13584 C  C   . MET   E 291 ? 2.2848 1.5772 1.3284 0.1835  -0.0557 -0.0834 291  MET   E C   
13585 O  O   . MET   E 291 ? 2.2483 1.5171 1.2649 0.1875  -0.0662 -0.0869 291  MET   E O   
13586 C  CB  . MET   E 291 ? 2.1793 1.4617 1.2014 0.2018  -0.0243 -0.0756 291  MET   E CB  
13587 C  CG  . MET   E 291 ? 2.1748 1.4580 1.1920 0.2093  -0.0069 -0.0698 291  MET   E CG  
13588 S  SD  . MET   E 291 ? 2.4296 1.7510 1.4906 0.2006  0.0045  -0.0643 291  MET   E SD  
13589 C  CE  . MET   E 291 ? 2.3074 1.6242 1.3583 0.2126  0.0285  -0.0580 291  MET   E CE  
13590 N  N   . ASP   E 292 ? 2.3380 1.6458 1.4046 0.1753  -0.0604 -0.0850 292  ASP   E N   
13591 C  CA  . ASP   E 292 ? 2.3389 1.6393 1.4040 0.1689  -0.0785 -0.0908 292  ASP   E CA  
13592 C  C   . ASP   E 292 ? 2.3998 1.7180 1.4887 0.1574  -0.0892 -0.0915 292  ASP   E C   
13593 O  O   . ASP   E 292 ? 2.3850 1.7117 1.4905 0.1482  -0.1003 -0.0945 292  ASP   E O   
13594 C  CB  . ASP   E 292 ? 2.3214 1.6281 1.3983 0.1659  -0.0782 -0.0921 292  ASP   E CB  
13595 C  CG  . ASP   E 292 ? 2.3598 1.6990 1.4760 0.1559  -0.0741 -0.0894 292  ASP   E CG  
13596 O  OD1 . ASP   E 292 ? 2.3798 1.7367 1.5124 0.1542  -0.0655 -0.0852 292  ASP   E OD1 
13597 O  OD2 . ASP   E 292 ? 2.3547 1.7009 1.4846 0.1498  -0.0795 -0.0915 292  ASP   E OD2 
13598 N  N   . GLY   E 293 ? 2.4279 1.7525 1.5198 0.1577  -0.0853 -0.0885 293  GLY   E N   
13599 C  CA  . GLY   E 293 ? 2.4062 1.7492 1.5215 0.1475  -0.0936 -0.0885 293  GLY   E CA  
13600 C  C   . GLY   E 293 ? 2.3892 1.7640 1.5431 0.1378  -0.0886 -0.0858 293  GLY   E C   
13601 O  O   . GLY   E 293 ? 2.3684 1.7616 1.5421 0.1325  -0.0868 -0.0832 293  GLY   E O   
13602 N  N   . THR   E 294 ? 2.3116 1.6923 1.4757 0.1358  -0.0866 -0.0865 294  THR   E N   
13603 C  CA  . THR   E 294 ? 2.3573 1.7665 1.5565 0.1268  -0.0832 -0.0844 294  THR   E CA  
13604 C  C   . THR   E 294 ? 2.3780 1.8068 1.5944 0.1271  -0.0695 -0.0789 294  THR   E C   
13605 O  O   . THR   E 294 ? 2.3543 1.7758 1.5566 0.1358  -0.0576 -0.0760 294  THR   E O   
13606 C  CB  . THR   E 294 ? 2.3590 1.7694 1.5620 0.1279  -0.0787 -0.0849 294  THR   E CB  
13607 O  OG1 . THR   E 294 ? 2.4368 1.8280 1.6235 0.1276  -0.0915 -0.0901 294  THR   E OG1 
13608 C  CG2 . THR   E 294 ? 2.2398 1.6789 1.4787 0.1188  -0.0759 -0.0830 294  THR   E CG2 
13609 N  N   . VAL   E 295 ? 2.3858 1.8395 1.6329 0.1173  -0.0713 -0.0776 295  VAL   E N   
13610 C  CA  . VAL   E 295 ? 2.3069 1.7829 1.5759 0.1159  -0.0590 -0.0726 295  VAL   E CA  
13611 C  C   . VAL   E 295 ? 2.2635 1.7616 1.5613 0.1092  -0.0565 -0.0719 295  VAL   E C   
13612 O  O   . VAL   E 295 ? 2.2462 1.7498 1.5558 0.1013  -0.0674 -0.0746 295  VAL   E O   
13613 C  CB  . VAL   E 295 ? 2.3081 1.7928 1.5859 0.1109  -0.0636 -0.0716 295  VAL   E CB  
13614 C  CG1 . VAL   E 295 ? 2.3115 1.8212 1.6156 0.1080  -0.0519 -0.0668 295  VAL   E CG1 
13615 C  CG2 . VAL   E 295 ? 2.3106 1.7726 1.5584 0.1188  -0.0646 -0.0719 295  VAL   E CG2 
13616 N  N   . THR   E 296 ? 2.2789 1.7889 1.5875 0.1127  -0.0422 -0.0683 296  THR   E N   
13617 C  CA  . THR   E 296 ? 2.3261 1.8553 1.6596 0.1079  -0.0390 -0.0676 296  THR   E CA  
13618 C  C   . THR   E 296 ? 2.3137 1.8675 1.6733 0.1051  -0.0289 -0.0633 296  THR   E C   
13619 O  O   . THR   E 296 ? 2.2971 1.8508 1.6526 0.1092  -0.0207 -0.0603 296  THR   E O   
13620 C  CB  . THR   E 296 ? 2.3306 1.8500 1.6528 0.1152  -0.0322 -0.0681 296  THR   E CB  
13621 O  OG1 . THR   E 296 ? 2.3258 1.8301 1.6259 0.1256  -0.0224 -0.0664 296  THR   E OG1 
13622 C  CG2 . THR   E 296 ? 2.3038 1.8065 1.6115 0.1141  -0.0442 -0.0729 296  THR   E CG2 
13623 N  N   . LEU   E 297 ? 2.1092 1.6834 1.4953 0.0982  -0.0296 -0.0630 297  LEU   E N   
13624 C  CA  . LEU   E 297 ? 1.9624 1.5611 1.3755 0.0948  -0.0212 -0.0593 297  LEU   E CA  
13625 C  C   . LEU   E 297 ? 1.9106 1.5134 1.3266 0.1019  -0.0070 -0.0569 297  LEU   E C   
13626 O  O   . LEU   E 297 ? 1.8130 1.4210 1.2373 0.1019  -0.0056 -0.0578 297  LEU   E O   
13627 C  CB  . LEU   E 297 ? 1.8840 1.5017 1.3230 0.0849  -0.0283 -0.0601 297  LEU   E CB  
13628 C  CG  . LEU   E 297 ? 1.7600 1.4034 1.2280 0.0802  -0.0222 -0.0569 297  LEU   E CG  
13629 C  CD1 . LEU   E 297 ? 1.7539 1.4097 1.2365 0.0828  -0.0122 -0.0553 297  LEU   E CD1 
13630 C  CD2 . LEU   E 297 ? 1.7995 1.4444 1.2653 0.0825  -0.0159 -0.0539 297  LEU   E CD2 
13631 N  N   . LYS   E 298 ? 1.8783 1.4787 1.2880 0.1080  0.0038  -0.0538 298  LYS   E N   
13632 C  CA  . LYS   E 298 ? 1.8912 1.4960 1.3049 0.1149  0.0182  -0.0512 298  LYS   E CA  
13633 C  C   . LYS   E 298 ? 1.8968 1.5288 1.3437 0.1098  0.0234  -0.0491 298  LYS   E C   
13634 O  O   . LYS   E 298 ? 1.8517 1.4915 1.3096 0.1108  0.0269  -0.0495 298  LYS   E O   
13635 C  CB  . LYS   E 298 ? 1.8861 1.4799 1.2834 0.1227  0.0285  -0.0484 298  LYS   E CB  
13636 N  N   . ASP   E 299 ? 1.8601 1.5065 1.3232 0.1043  0.0234  -0.0471 299  ASP   E N   
13637 C  CA  . ASP   E 299 ? 1.8273 1.4990 1.3214 0.0995  0.0280  -0.0451 299  ASP   E CA  
13638 C  C   . ASP   E 299 ? 1.8020 1.4863 1.3110 0.0907  0.0205  -0.0448 299  ASP   E C   
13639 O  O   . ASP   E 299 ? 1.7836 1.4574 1.2795 0.0882  0.0116  -0.0461 299  ASP   E O   
13640 C  CB  . ASP   E 299 ? 1.8462 1.5244 1.3472 0.1056  0.0436  -0.0414 299  ASP   E CB  
13641 C  CG  . ASP   E 299 ? 1.8719 1.5744 1.4038 0.1024  0.0486  -0.0402 299  ASP   E CG  
13642 O  OD1 . ASP   E 299 ? 1.8624 1.5694 1.4016 0.1017  0.0457  -0.0421 299  ASP   E OD1 
13643 O  OD2 . ASP   E 299 ? 1.8417 1.5582 1.3903 0.1007  0.0552  -0.0372 299  ASP   E OD2 
13644 N  N   . LEU   E 300 ? 1.7971 1.5041 1.3340 0.0861  0.0239  -0.0431 300  LEU   E N   
13645 C  CA  . LEU   E 300 ? 1.7266 1.4491 1.2820 0.0779  0.0187  -0.0423 300  LEU   E CA  
13646 C  C   . LEU   E 300 ? 1.7321 1.4717 1.3075 0.0782  0.0297  -0.0387 300  LEU   E C   
13647 O  O   . LEU   E 300 ? 1.7710 1.5219 1.3615 0.0800  0.0367  -0.0380 300  LEU   E O   
13648 C  CB  . LEU   E 300 ? 1.6694 1.4034 1.2409 0.0706  0.0095  -0.0445 300  LEU   E CB  
13649 C  CG  . LEU   E 300 ? 1.6501 1.3731 1.2102 0.0663  -0.0040 -0.0478 300  LEU   E CG  
13650 C  CD1 . LEU   E 300 ? 1.6101 1.3460 1.1885 0.0600  -0.0101 -0.0493 300  LEU   E CD1 
13651 C  CD2 . LEU   E 300 ? 1.6870 1.4070 1.2423 0.0623  -0.0106 -0.0476 300  LEU   E CD2 
13652 N  N   . ARG   E 301 ? 1.6778 1.4195 1.2542 0.0764  0.0308  -0.0366 301  ARG   E N   
13653 C  CA  . ARG   E 301 ? 1.6786 1.4367 1.2749 0.0757  0.0403  -0.0332 301  ARG   E CA  
13654 C  C   . ARG   E 301 ? 1.6478 1.4207 1.2617 0.0672  0.0335  -0.0329 301  ARG   E C   
13655 O  O   . ARG   E 301 ? 1.6437 1.4094 1.2475 0.0640  0.0249  -0.0338 301  ARG   E O   
13656 C  CB  . ARG   E 301 ? 1.6290 1.3763 1.2110 0.0821  0.0506  -0.0303 301  ARG   E CB  
13657 N  N   . VAL   E 302 ? 1.6828 1.4763 1.3231 0.0638  0.0372  -0.0316 302  VAL   E N   
13658 C  CA  . VAL   E 302 ? 1.6869 1.4955 1.3454 0.0565  0.0329  -0.0308 302  VAL   E CA  
13659 C  C   . VAL   E 302 ? 1.7113 1.5280 1.3799 0.0581  0.0436  -0.0272 302  VAL   E C   
13660 O  O   . VAL   E 302 ? 1.6998 1.5245 1.3803 0.0614  0.0534  -0.0258 302  VAL   E O   
13661 C  CB  . VAL   E 302 ? 1.5964 1.4223 1.2775 0.0509  0.0279  -0.0322 302  VAL   E CB  
13662 C  CG1 . VAL   E 302 ? 1.5900 1.4315 1.2898 0.0444  0.0255  -0.0308 302  VAL   E CG1 
13663 C  CG2 . VAL   E 302 ? 1.5735 1.3916 1.2453 0.0484  0.0169  -0.0354 302  VAL   E CG2 
13664 N  N   . GLU   E 303 ? 1.8814 1.6959 1.5458 0.0557  0.0418  -0.0258 303  GLU   E N   
13665 C  CA  . GLU   E 303 ? 1.8941 1.7152 1.5673 0.0567  0.0515  -0.0223 303  GLU   E CA  
13666 C  C   . GLU   E 303 ? 1.8726 1.7094 1.5648 0.0491  0.0462  -0.0217 303  GLU   E C   
13667 O  O   . GLU   E 303 ? 1.8741 1.7091 1.5622 0.0443  0.0353  -0.0234 303  GLU   E O   
13668 C  CB  . GLU   E 303 ? 1.9322 1.7346 1.5810 0.0620  0.0560  -0.0205 303  GLU   E CB  
13669 C  CG  . GLU   E 303 ? 2.0061 1.7950 1.6391 0.0707  0.0657  -0.0199 303  GLU   E CG  
13670 C  CD  . GLU   E 303 ? 2.0288 1.8290 1.6791 0.0737  0.0797  -0.0169 303  GLU   E CD  
13671 O  OE1 . GLU   E 303 ? 2.0089 1.8184 1.6720 0.0716  0.0851  -0.0142 303  GLU   E OE1 
13672 O  OE2 . GLU   E 303 ? 1.9850 1.7849 1.6367 0.0781  0.0852  -0.0175 303  GLU   E OE2 
13673 N  N   . LEU   E 304 ? 1.6845 1.5367 1.3979 0.0479  0.0540  -0.0194 304  LEU   E N   
13674 C  CA  . LEU   E 304 ? 1.5750 1.4425 1.3073 0.0412  0.0501  -0.0187 304  LEU   E CA  
13675 C  C   . LEU   E 304 ? 1.5131 1.3754 1.2382 0.0416  0.0539  -0.0159 304  LEU   E C   
13676 O  O   . LEU   E 304 ? 1.4884 1.3456 1.2089 0.0466  0.0650  -0.0133 304  LEU   E O   
13677 C  CB  . LEU   E 304 ? 1.4957 1.3828 1.2555 0.0395  0.0555  -0.0180 304  LEU   E CB  
13678 C  CG  . LEU   E 304 ? 1.4050 1.3073 1.1845 0.0339  0.0547  -0.0165 304  LEU   E CG  
13679 C  CD1 . LEU   E 304 ? 1.3352 1.2558 1.1402 0.0313  0.0548  -0.0175 304  LEU   E CD1 
13680 C  CD2 . LEU   E 304 ? 1.4721 1.3725 1.2511 0.0363  0.0652  -0.0130 304  LEU   E CD2 
13681 N  N   . LEU   E 305 ? 1.4685 1.3322 1.1932 0.0364  0.0450  -0.0164 305  LEU   E N   
13682 C  CA  . LEU   E 305 ? 1.5430 1.4004 1.2589 0.0369  0.0474  -0.0139 305  LEU   E CA  
13683 C  C   . LEU   E 305 ? 1.5312 1.4054 1.2700 0.0330  0.0519  -0.0116 305  LEU   E C   
13684 O  O   . LEU   E 305 ? 1.5844 1.4568 1.3227 0.0358  0.0618  -0.0085 305  LEU   E O   
13685 C  CB  . LEU   E 305 ? 1.4707 1.3181 1.1709 0.0343  0.0352  -0.0158 305  LEU   E CB  
13686 C  CG  . LEU   E 305 ? 1.4956 1.3247 1.1719 0.0383  0.0303  -0.0183 305  LEU   E CG  
13687 C  CD1 . LEU   E 305 ? 1.5120 1.3337 1.1771 0.0348  0.0168  -0.0208 305  LEU   E CD1 
13688 C  CD2 . LEU   E 305 ? 1.5861 1.3981 1.2412 0.0463  0.0397  -0.0165 305  LEU   E CD2 
13689 N  N   . GLY   E 306 ? 1.4897 1.3799 1.2483 0.0267  0.0450  -0.0129 306  GLY   E N   
13690 C  CA  . GLY   E 306 ? 1.4932 1.3991 1.2732 0.0226  0.0477  -0.0110 306  GLY   E CA  
13691 C  C   . GLY   E 306 ? 1.4336 1.3537 1.2302 0.0158  0.0376  -0.0130 306  GLY   E C   
13692 O  O   . GLY   E 306 ? 1.4299 1.3504 1.2260 0.0147  0.0308  -0.0157 306  GLY   E O   
13693 N  N   . GLU   E 307 ? 1.3781 1.3090 1.1887 0.0116  0.0370  -0.0116 307  GLU   E N   
13694 C  CA  . GLU   E 307 ? 1.3079 1.2520 1.1340 0.0054  0.0281  -0.0131 307  GLU   E CA  
13695 C  C   . GLU   E 307 ? 1.2680 1.2076 1.0852 0.0020  0.0197  -0.0132 307  GLU   E C   
13696 O  O   . GLU   E 307 ? 1.2674 1.2002 1.0757 0.0033  0.0228  -0.0111 307  GLU   E O   
13697 C  CB  . GLU   E 307 ? 1.3454 1.3067 1.1964 0.0029  0.0328  -0.0118 307  GLU   E CB  
13698 C  CG  . GLU   E 307 ? 1.4240 1.3952 1.2904 0.0042  0.0365  -0.0130 307  GLU   E CG  
13699 C  CD  . GLU   E 307 ? 1.4720 1.4606 1.3614 -0.0007 0.0321  -0.0139 307  GLU   E CD  
13700 O  OE1 . GLU   E 307 ? 1.3831 1.3779 1.2801 -0.0044 0.0303  -0.0127 307  GLU   E OE1 
13701 O  OE2 . GLU   E 307 ? 1.4472 1.4425 1.3461 -0.0005 0.0303  -0.0159 307  GLU   E OE2 
13702 N  N   . THR   E 308 ? 1.2574 1.2004 1.0770 -0.0021 0.0093  -0.0155 308  THR   E N   
13703 C  CA  . THR   E 308 ? 1.2460 1.1882 1.0624 -0.0061 0.0009  -0.0156 308  THR   E CA  
13704 C  C   . THR   E 308 ? 1.1896 1.1474 1.0256 -0.0118 -0.0050 -0.0166 308  THR   E C   
13705 O  O   . THR   E 308 ? 1.1917 1.1605 1.0432 -0.0123 -0.0019 -0.0169 308  THR   E O   
13706 C  CB  . THR   E 308 ? 1.2831 1.2101 1.0785 -0.0052 -0.0069 -0.0176 308  THR   E CB  
13707 O  OG1 . THR   E 308 ? 1.1915 1.1215 0.9909 -0.0079 -0.0142 -0.0202 308  THR   E OG1 
13708 C  CG2 . THR   E 308 ? 1.2642 1.1746 1.0390 0.0013  -0.0011 -0.0172 308  THR   E CG2 
13709 N  N   . SER   E 309 ? 1.1611 1.1203 0.9969 -0.0159 -0.0135 -0.0171 309  SER   E N   
13710 C  CA  . SER   E 309 ? 1.2101 1.1826 1.0627 -0.0209 -0.0193 -0.0181 309  SER   E CA  
13711 C  C   . SER   E 309 ? 1.1959 1.1672 1.0477 -0.0211 -0.0232 -0.0206 309  SER   E C   
13712 O  O   . SER   E 309 ? 1.2091 1.1679 1.0451 -0.0186 -0.0249 -0.0218 309  SER   E O   
13713 C  CB  . SER   E 309 ? 1.1521 1.1255 1.0041 -0.0251 -0.0276 -0.0182 309  SER   E CB  
13714 O  OG  . SER   E 309 ? 1.0962 1.0710 0.9493 -0.0252 -0.0249 -0.0160 309  SER   E OG  
13715 N  N   . ILE   E 310 ? 1.1414 1.1252 1.0098 -0.0239 -0.0248 -0.0212 310  ILE   E N   
13716 C  CA  . ILE   E 310 ? 1.0836 1.0671 0.9524 -0.0246 -0.0291 -0.0234 310  ILE   E CA  
13717 C  C   . ILE   E 310 ? 1.1400 1.1127 0.9948 -0.0262 -0.0371 -0.0248 310  ILE   E C   
13718 O  O   . ILE   E 310 ? 1.0954 1.0719 0.9546 -0.0305 -0.0437 -0.0250 310  ILE   E O   
13719 C  CB  . ILE   E 310 ? 1.1600 1.1578 1.0474 -0.0281 -0.0316 -0.0237 310  ILE   E CB  
13720 C  CG1 . ILE   E 310 ? 1.1317 1.1398 1.0334 -0.0262 -0.0244 -0.0229 310  ILE   E CG1 
13721 C  CG2 . ILE   E 310 ? 1.1009 1.0967 0.9867 -0.0296 -0.0374 -0.0258 310  ILE   E CG2 
13722 C  CD1 . ILE   E 310 ? 1.1942 1.2003 1.0952 -0.0223 -0.0203 -0.0241 310  ILE   E CD1 
13723 N  N   . ALA   E 311 ? 1.1616 1.1208 0.9999 -0.0227 -0.0366 -0.0259 311  ALA   E N   
13724 C  CA  . ALA   E 311 ? 1.0599 1.0068 0.8831 -0.0235 -0.0440 -0.0275 311  ALA   E CA  
13725 C  C   . ALA   E 311 ? 1.0836 1.0324 0.9111 -0.0272 -0.0512 -0.0294 311  ALA   E C   
13726 O  O   . ALA   E 311 ? 1.1273 1.0784 0.9591 -0.0264 -0.0495 -0.0303 311  ALA   E O   
13727 C  CB  . ALA   E 311 ? 1.1366 1.0680 0.9404 -0.0181 -0.0408 -0.0281 311  ALA   E CB  
13728 N  N   . GLU   E 312 ? 1.0608 1.0087 0.8878 -0.0313 -0.0591 -0.0300 312  GLU   E N   
13729 C  CA  . GLU   E 312 ? 1.1064 1.0531 0.9349 -0.0349 -0.0664 -0.0319 312  GLU   E CA  
13730 C  C   . GLU   E 312 ? 1.2114 1.1419 1.0216 -0.0335 -0.0714 -0.0339 312  GLU   E C   
13731 O  O   . GLU   E 312 ? 1.3144 1.2390 1.1200 -0.0331 -0.0731 -0.0356 312  GLU   E O   
13732 C  CB  . GLU   E 312 ? 1.0870 1.0432 0.9278 -0.0404 -0.0722 -0.0314 312  GLU   E CB  
13733 C  CG  . GLU   E 312 ? 1.1052 1.0598 0.9479 -0.0443 -0.0794 -0.0330 312  GLU   E CG  
13734 C  CD  . GLU   E 312 ? 1.2316 1.1910 1.0820 -0.0444 -0.0769 -0.0334 312  GLU   E CD  
13735 O  OE1 . GLU   E 312 ? 1.2081 1.1701 1.0600 -0.0408 -0.0701 -0.0328 312  GLU   E OE1 
13736 O  OE2 . GLU   E 312 ? 1.2967 1.2572 1.1520 -0.0481 -0.0817 -0.0342 312  GLU   E OE2 
13737 N  N   . CYS   E 313 ? 1.2452 1.1678 1.0445 -0.0325 -0.0738 -0.0338 313  CYS   E N   
13738 C  CA  . CYS   E 313 ? 1.2677 1.1738 1.0481 -0.0304 -0.0788 -0.0358 313  CYS   E CA  
13739 C  C   . CYS   E 313 ? 1.2779 1.1746 1.0435 -0.0250 -0.0738 -0.0348 313  CYS   E C   
13740 O  O   . CYS   E 313 ? 1.2729 1.1763 1.0441 -0.0245 -0.0693 -0.0325 313  CYS   E O   
13741 C  CB  . CYS   E 313 ? 1.2783 1.1831 1.0599 -0.0352 -0.0891 -0.0372 313  CYS   E CB  
13742 S  SG  . CYS   E 313 ? 1.3995 1.3069 1.1814 -0.0359 -0.0913 -0.0357 313  CYS   E SG  
13743 N  N   . LEU   E 314 ? 1.3128 1.1933 1.0591 -0.0207 -0.0744 -0.0363 314  LEU   E N   
13744 C  CA  . LEU   E 314 ? 1.2660 1.1348 0.9953 -0.0148 -0.0694 -0.0354 314  LEU   E CA  
13745 C  C   . LEU   E 314 ? 1.3277 1.1789 1.0366 -0.0130 -0.0773 -0.0378 314  LEU   E C   
13746 O  O   . LEU   E 314 ? 1.3882 1.2326 1.0923 -0.0145 -0.0841 -0.0404 314  LEU   E O   
13747 C  CB  . LEU   E 314 ? 1.2559 1.1212 0.9799 -0.0094 -0.0596 -0.0347 314  LEU   E CB  
13748 C  CG  . LEU   E 314 ? 1.2850 1.1638 1.0237 -0.0085 -0.0494 -0.0318 314  LEU   E CG  
13749 C  CD1 . LEU   E 314 ? 1.2887 1.1600 1.0174 -0.0019 -0.0395 -0.0309 314  LEU   E CD1 
13750 C  CD2 . LEU   E 314 ? 1.2076 1.0930 0.9524 -0.0102 -0.0487 -0.0296 314  LEU   E CD2 
13751 N  N   . THR   E 315 ? 1.3277 1.1706 1.0240 -0.0095 -0.0762 -0.0368 315  THR   E N   
13752 C  CA  . THR   E 315 ? 1.3161 1.1419 0.9925 -0.0075 -0.0844 -0.0391 315  THR   E CA  
13753 C  C   . THR   E 315 ? 1.3284 1.1425 0.9869 -0.0009 -0.0784 -0.0375 315  THR   E C   
13754 O  O   . THR   E 315 ? 1.3516 1.1724 1.0157 -0.0009 -0.0742 -0.0349 315  THR   E O   
13755 C  CB  . THR   E 315 ? 1.3159 1.1470 1.0010 -0.0133 -0.0955 -0.0405 315  THR   E CB  
13756 O  OG1 . THR   E 315 ? 1.4426 1.2587 1.1126 -0.0128 -0.1057 -0.0438 315  THR   E OG1 
13757 C  CG2 . THR   E 315 ? 1.4297 1.2657 1.1176 -0.0134 -0.0946 -0.0383 315  THR   E CG2 
13758 N  N   . TYR   E 316 ? 1.4126 1.2090 1.0495 0.0051  -0.0770 -0.0387 316  TYR   E N   
13759 C  CA  . TYR   E 316 ? 1.4504 1.2331 1.0675 0.0119  -0.0716 -0.0372 316  TYR   E CA  
13760 C  C   . TYR   E 316 ? 1.4515 1.2233 1.0555 0.0121  -0.0819 -0.0389 316  TYR   E C   
13761 O  O   . TYR   E 316 ? 1.4564 1.2218 1.0559 0.0099  -0.0932 -0.0424 316  TYR   E O   
13762 C  CB  . TYR   E 316 ? 1.4257 1.1925 1.0235 0.0187  -0.0661 -0.0378 316  TYR   E CB  
13763 C  CG  . TYR   E 316 ? 1.5844 1.3333 1.1576 0.0265  -0.0615 -0.0366 316  TYR   E CG  
13764 C  CD1 . TYR   E 316 ? 1.6594 1.3918 1.2127 0.0288  -0.0709 -0.0388 316  TYR   E CD1 
13765 C  CD2 . TYR   E 316 ? 1.6617 1.4096 1.2315 0.0318  -0.0475 -0.0333 316  TYR   E CD2 
13766 C  CE1 . TYR   E 316 ? 1.6871 1.4014 1.2159 0.0365  -0.0667 -0.0377 316  TYR   E CE1 
13767 C  CE2 . TYR   E 316 ? 1.7022 1.4322 1.2481 0.0394  -0.0425 -0.0319 316  TYR   E CE2 
13768 C  CZ  . TYR   E 316 ? 1.7004 1.4135 1.2253 0.0418  -0.0522 -0.0342 316  TYR   E CZ  
13769 O  OH  . TYR   E 316 ? 1.7264 1.4207 1.2264 0.0496  -0.0477 -0.0329 316  TYR   E OH  
13770 N  N   . LEU   E 317 ? 1.4723 1.2418 1.0706 0.0148  -0.0782 -0.0366 317  LEU   E N   
13771 C  CA  . LEU   E 317 ? 1.5118 1.2718 1.0984 0.0153  -0.0880 -0.0381 317  LEU   E CA  
13772 C  C   . LEU   E 317 ? 1.6434 1.3797 1.1995 0.0238  -0.0868 -0.0385 317  LEU   E C   
13773 O  O   . LEU   E 317 ? 1.5945 1.3154 1.1340 0.0258  -0.0960 -0.0421 317  LEU   E O   
13774 C  CB  . LEU   E 317 ? 1.4898 1.2627 1.0901 0.0123  -0.0864 -0.0354 317  LEU   E CB  
13775 C  CG  . LEU   E 317 ? 1.4875 1.2833 1.1171 0.0042  -0.0880 -0.0350 317  LEU   E CG  
13776 C  CD1 . LEU   E 317 ? 1.4542 1.2622 1.0964 0.0024  -0.0833 -0.0317 317  LEU   E CD1 
13777 C  CD2 . LEU   E 317 ? 1.3806 1.1780 1.0161 -0.0011 -0.1019 -0.0385 317  LEU   E CD2 
13778 N  N   . ASP   E 318 ? 1.7131 1.4454 1.2611 0.0290  -0.0754 -0.0350 318  ASP   E N   
13779 C  CA  . ASP   E 318 ? 1.7220 1.4313 1.2402 0.0377  -0.0728 -0.0350 318  ASP   E CA  
13780 C  C   . ASP   E 318 ? 1.7011 1.4111 1.2172 0.0420  -0.0581 -0.0302 318  ASP   E C   
13781 O  O   . ASP   E 318 ? 1.6846 1.4117 1.2210 0.0380  -0.0528 -0.0274 318  ASP   E O   
13782 C  CB  . ASP   E 318 ? 1.7273 1.4226 1.2286 0.0392  -0.0855 -0.0377 318  ASP   E CB  
13783 C  CG  . ASP   E 318 ? 1.8059 1.4748 1.2742 0.0482  -0.0859 -0.0390 318  ASP   E CG  
13784 O  OD1 . ASP   E 318 ? 1.8820 1.5423 1.3414 0.0506  -0.0854 -0.0408 318  ASP   E OD1 
13785 O  OD2 . ASP   E 318 ? 1.8495 1.5055 1.3001 0.0531  -0.0867 -0.0382 318  ASP   E OD2 
13786 N  N   . ASN   E 319 ? 1.7284 1.4189 1.2195 0.0504  -0.0516 -0.0294 319  ASN   E N   
13787 C  CA  . ASN   E 319 ? 1.7447 1.4331 1.2314 0.0553  -0.0368 -0.0248 319  ASN   E CA  
13788 C  C   . ASN   E 319 ? 1.6620 1.3723 1.1763 0.0510  -0.0260 -0.0219 319  ASN   E C   
13789 O  O   . ASN   E 319 ? 1.6771 1.3948 1.2000 0.0511  -0.0164 -0.0181 319  ASN   E O   
13790 C  CB  . ASN   E 319 ? 1.7541 1.4379 1.2335 0.0565  -0.0390 -0.0232 319  ASN   E CB  
13791 C  CG  . ASN   E 319 ? 1.8064 1.4746 1.2665 0.0580  -0.0542 -0.0272 319  ASN   E CG  
13792 O  OD1 . ASN   E 319 ? 1.7980 1.4749 1.2693 0.0525  -0.0651 -0.0290 319  ASN   E OD1 
13793 N  ND2 . ASN   E 319 ? 1.8900 1.5348 1.3212 0.0657  -0.0551 -0.0287 319  ASN   E ND2 
13794 N  N   . GLY   E 320 ? 1.6998 1.4203 1.2284 0.0471  -0.0280 -0.0238 320  GLY   E N   
13795 C  CA  . GLY   E 320 ? 1.7184 1.4580 1.2714 0.0439  -0.0183 -0.0216 320  GLY   E CA  
13796 C  C   . GLY   E 320 ? 1.5962 1.3582 1.1771 0.0359  -0.0208 -0.0207 320  GLY   E C   
13797 O  O   . GLY   E 320 ? 1.5333 1.3108 1.1342 0.0337  -0.0121 -0.0185 320  GLY   E O   
13798 N  N   . VAL   E 321 ? 1.5524 1.3166 1.1356 0.0317  -0.0322 -0.0224 321  VAL   E N   
13799 C  CA  . VAL   E 321 ? 1.5379 1.3232 1.1474 0.0240  -0.0355 -0.0219 321  VAL   E CA  
13800 C  C   . VAL   E 321 ? 1.5132 1.3074 1.1355 0.0186  -0.0439 -0.0251 321  VAL   E C   
13801 O  O   . VAL   E 321 ? 1.5093 1.2933 1.1201 0.0185  -0.0542 -0.0285 321  VAL   E O   
13802 C  CB  . VAL   E 321 ? 1.4966 1.2809 1.1036 0.0222  -0.0430 -0.0219 321  VAL   E CB  
13803 C  CG1 . VAL   E 321 ? 1.5084 1.2864 1.1062 0.0269  -0.0334 -0.0182 321  VAL   E CG1 
13804 C  CG2 . VAL   E 321 ? 1.5518 1.3201 1.1394 0.0238  -0.0558 -0.0256 321  VAL   E CG2 
13805 N  N   . VAL   E 322 ? 1.3980 1.2105 1.0438 0.0143  -0.0394 -0.0241 322  VAL   E N   
13806 C  CA  . VAL   E 322 ? 1.3501 1.1727 1.0103 0.0090  -0.0460 -0.0265 322  VAL   E CA  
13807 C  C   . VAL   E 322 ? 1.3579 1.1985 1.0403 0.0021  -0.0502 -0.0259 322  VAL   E C   
13808 O  O   . VAL   E 322 ? 1.4259 1.2786 1.1225 0.0010  -0.0428 -0.0232 322  VAL   E O   
13809 C  CB  . VAL   E 322 ? 1.3239 1.1524 0.9924 0.0102  -0.0377 -0.0261 322  VAL   E CB  
13810 C  CG1 . VAL   E 322 ? 1.2501 1.0938 0.9390 0.0039  -0.0428 -0.0276 322  VAL   E CG1 
13811 C  CG2 . VAL   E 322 ? 1.4784 1.2890 1.1253 0.0160  -0.0370 -0.0278 322  VAL   E CG2 
13812 N  N   . PHE   E 323 ? 1.3146 1.1567 1.0001 -0.0024 -0.0619 -0.0285 323  PHE   E N   
13813 C  CA  . PHE   E 323 ? 1.2903 1.1502 0.9982 -0.0090 -0.0658 -0.0281 323  PHE   E CA  
13814 C  C   . PHE   E 323 ? 1.2858 1.1589 1.0115 -0.0121 -0.0627 -0.0282 323  PHE   E C   
13815 O  O   . PHE   E 323 ? 1.3102 1.1793 1.0330 -0.0127 -0.0666 -0.0305 323  PHE   E O   
13816 C  CB  . PHE   E 323 ? 1.2918 1.1496 0.9987 -0.0129 -0.0789 -0.0307 323  PHE   E CB  
13817 C  CG  . PHE   E 323 ? 1.3136 1.1894 1.0436 -0.0197 -0.0826 -0.0303 323  PHE   E CG  
13818 C  CD1 . PHE   E 323 ? 1.2322 1.1185 0.9730 -0.0211 -0.0794 -0.0278 323  PHE   E CD1 
13819 C  CD2 . PHE   E 323 ? 1.2654 1.1475 1.0064 -0.0244 -0.0887 -0.0323 323  PHE   E CD2 
13820 C  CE1 . PHE   E 323 ? 1.1721 1.0741 0.9330 -0.0268 -0.0826 -0.0274 323  PHE   E CE1 
13821 C  CE2 . PHE   E 323 ? 1.2291 1.1272 0.9906 -0.0301 -0.0915 -0.0318 323  PHE   E CE2 
13822 C  CZ  . PHE   E 323 ? 1.2209 1.1290 0.9922 -0.0312 -0.0884 -0.0293 323  PHE   E CZ  
13823 N  N   . VAL   E 324 ? 1.2540 1.1423 0.9976 -0.0141 -0.0560 -0.0258 324  VAL   E N   
13824 C  CA  . VAL   E 324 ? 1.1711 1.0726 0.9323 -0.0167 -0.0531 -0.0259 324  VAL   E CA  
13825 C  C   . VAL   E 324 ? 1.1886 1.1041 0.9678 -0.0232 -0.0596 -0.0262 324  VAL   E C   
13826 O  O   . VAL   E 324 ? 1.2129 1.1379 1.0026 -0.0251 -0.0580 -0.0243 324  VAL   E O   
13827 C  CB  . VAL   E 324 ? 1.1587 1.0673 0.9280 -0.0141 -0.0413 -0.0233 324  VAL   E CB  
13828 C  CG1 . VAL   E 324 ? 1.1326 1.0523 0.9172 -0.0157 -0.0388 -0.0239 324  VAL   E CG1 
13829 C  CG2 . VAL   E 324 ? 1.2191 1.1130 0.9698 -0.0074 -0.0342 -0.0225 324  VAL   E CG2 
13830 N  N   . GLY   E 325 ? 1.2025 1.1191 0.9853 -0.0265 -0.0667 -0.0284 325  GLY   E N   
13831 C  CA  . GLY   E 325 ? 1.1742 1.1036 0.9740 -0.0325 -0.0725 -0.0286 325  GLY   E CA  
13832 C  C   . GLY   E 325 ? 1.0720 1.0154 0.8895 -0.0343 -0.0676 -0.0278 325  GLY   E C   
13833 O  O   . GLY   E 325 ? 1.0257 0.9674 0.8423 -0.0326 -0.0646 -0.0286 325  GLY   E O   
13834 N  N   . SER   E 326 ? 1.1393 1.0962 0.9726 -0.0374 -0.0670 -0.0262 326  SER   E N   
13835 C  CA  . SER   E 326 ? 1.0820 1.0525 0.9323 -0.0385 -0.0620 -0.0252 326  SER   E CA  
13836 C  C   . SER   E 326 ? 1.0618 1.0433 0.9268 -0.0438 -0.0676 -0.0254 326  SER   E C   
13837 O  O   . SER   E 326 ? 1.0450 1.0277 0.9113 -0.0465 -0.0730 -0.0252 326  SER   E O   
13838 C  CB  . SER   E 326 ? 1.0413 1.0178 0.8971 -0.0365 -0.0542 -0.0228 326  SER   E CB  
13839 O  OG  . SER   E 326 ? 1.1101 1.0964 0.9789 -0.0360 -0.0485 -0.0223 326  SER   E OG  
13840 N  N   . ARG   E 327 ? 1.0664 1.0553 0.9419 -0.0448 -0.0662 -0.0258 327  ARG   E N   
13841 C  CA  . ARG   E 327 ? 1.0545 1.0543 0.9446 -0.0491 -0.0698 -0.0257 327  ARG   E CA  
13842 C  C   . ARG   E 327 ? 1.0221 1.0347 0.9268 -0.0492 -0.0649 -0.0241 327  ARG   E C   
13843 O  O   . ARG   E 327 ? 0.9873 1.0093 0.9039 -0.0525 -0.0674 -0.0235 327  ARG   E O   
13844 C  CB  . ARG   E 327 ? 1.0389 1.0369 0.9296 -0.0500 -0.0720 -0.0273 327  ARG   E CB  
13845 C  CG  . ARG   E 327 ? 1.0246 1.0178 0.9124 -0.0536 -0.0797 -0.0286 327  ARG   E CG  
13846 C  CD  . ARG   E 327 ? 1.1228 1.1264 1.0242 -0.0580 -0.0833 -0.0276 327  ARG   E CD  
13847 N  NE  . ARG   E 327 ? 1.2368 1.2461 1.1477 -0.0600 -0.0836 -0.0278 327  ARG   E NE  
13848 C  CZ  . ARG   E 327 ? 1.3629 1.3672 1.2717 -0.0622 -0.0879 -0.0290 327  ARG   E CZ  
13849 N  NH1 . ARG   E 327 ? 1.3773 1.3718 1.2764 -0.0632 -0.0930 -0.0304 327  ARG   E NH1 
13850 N  NH2 . ARG   E 327 ? 1.4011 1.4096 1.3172 -0.0632 -0.0870 -0.0290 327  ARG   E NH2 
13851 N  N   . LEU   E 328 ? 1.0044 1.0173 0.9085 -0.0455 -0.0578 -0.0234 328  LEU   E N   
13852 C  CA  . LEU   E 328 ? 1.0384 1.0625 0.9563 -0.0451 -0.0527 -0.0223 328  LEU   E CA  
13853 C  C   . LEU   E 328 ? 1.0821 1.1079 1.0008 -0.0440 -0.0484 -0.0205 328  LEU   E C   
13854 O  O   . LEU   E 328 ? 1.0831 1.1191 1.0146 -0.0452 -0.0468 -0.0194 328  LEU   E O   
13855 C  CB  . LEU   E 328 ? 1.0475 1.0718 0.9669 -0.0417 -0.0476 -0.0231 328  LEU   E CB  
13856 C  CG  . LEU   E 328 ? 1.0403 1.0689 0.9666 -0.0428 -0.0502 -0.0245 328  LEU   E CG  
13857 C  CD1 . LEU   E 328 ? 0.9698 0.9916 0.8885 -0.0454 -0.0569 -0.0255 328  LEU   E CD1 
13858 C  CD2 . LEU   E 328 ? 0.9864 1.0136 0.9121 -0.0387 -0.0453 -0.0254 328  LEU   E CD2 
13859 N  N   . GLY   E 329 ? 1.1005 1.1159 1.0055 -0.0414 -0.0464 -0.0201 329  GLY   E N   
13860 C  CA  . GLY   E 329 ? 1.1091 1.1246 1.0134 -0.0404 -0.0423 -0.0181 329  GLY   E CA  
13861 C  C   . GLY   E 329 ? 1.0757 1.0827 0.9677 -0.0410 -0.0470 -0.0178 329  GLY   E C   
13862 O  O   . GLY   E 329 ? 1.0099 1.0140 0.8981 -0.0434 -0.0545 -0.0191 329  GLY   E O   
13863 N  N   . ASP   E 330 ? 1.0634 1.0661 0.9494 -0.0389 -0.0427 -0.0161 330  ASP   E N   
13864 C  CA  . ASP   E 330 ? 1.0925 1.0855 0.9648 -0.0386 -0.0472 -0.0160 330  ASP   E CA  
13865 C  C   . ASP   E 330 ? 1.1174 1.0955 0.9713 -0.0353 -0.0483 -0.0175 330  ASP   E C   
13866 O  O   . ASP   E 330 ? 1.0953 1.0695 0.9451 -0.0320 -0.0423 -0.0176 330  ASP   E O   
13867 C  CB  . ASP   E 330 ? 1.1299 1.1220 1.0004 -0.0370 -0.0421 -0.0136 330  ASP   E CB  
13868 C  CG  . ASP   E 330 ? 1.1419 1.1482 1.0305 -0.0402 -0.0413 -0.0122 330  ASP   E CG  
13869 O  OD1 . ASP   E 330 ? 1.1189 1.1331 1.0170 -0.0440 -0.0476 -0.0132 330  ASP   E OD1 
13870 O  OD2 . ASP   E 330 ? 1.1774 1.1870 1.0710 -0.0390 -0.0342 -0.0103 330  ASP   E OD2 
13871 N  N   . SER   E 331 ? 1.0993 1.0697 0.9431 -0.0363 -0.0563 -0.0189 331  SER   E N   
13872 C  CA  . SER   E 331 ? 1.1129 1.0673 0.9370 -0.0328 -0.0578 -0.0202 331  SER   E CA  
13873 C  C   . SER   E 331 ? 1.1328 1.0777 0.9436 -0.0285 -0.0527 -0.0185 331  SER   E C   
13874 O  O   . SER   E 331 ? 1.1311 1.0810 0.9471 -0.0292 -0.0507 -0.0165 331  SER   E O   
13875 C  CB  . SER   E 331 ? 1.1377 1.0868 0.9560 -0.0353 -0.0686 -0.0225 331  SER   E CB  
13876 O  OG  . SER   E 331 ? 1.1868 1.1446 1.0179 -0.0393 -0.0725 -0.0238 331  SER   E OG  
13877 N  N   . GLN   E 332 ? 1.2325 1.1631 1.0254 -0.0238 -0.0504 -0.0191 332  GLN   E N   
13878 C  CA  . GLN   E 332 ? 1.1626 1.0836 0.9427 -0.0190 -0.0434 -0.0170 332  GLN   E CA  
13879 C  C   . GLN   E 332 ? 1.2466 1.1486 1.0028 -0.0142 -0.0452 -0.0185 332  GLN   E C   
13880 O  O   . GLN   E 332 ? 1.2452 1.1426 0.9967 -0.0140 -0.0486 -0.0208 332  GLN   E O   
13881 C  CB  . GLN   E 332 ? 1.0945 1.0226 0.8844 -0.0172 -0.0318 -0.0149 332  GLN   E CB  
13882 C  CG  . GLN   E 332 ? 1.1567 1.0868 0.9505 -0.0167 -0.0299 -0.0164 332  GLN   E CG  
13883 C  CD  . GLN   E 332 ? 1.2050 1.1420 1.0091 -0.0146 -0.0190 -0.0146 332  GLN   E CD  
13884 O  OE1 . GLN   E 332 ? 1.2311 1.1710 1.0400 -0.0138 -0.0166 -0.0156 332  GLN   E OE1 
13885 N  NE2 . GLN   E 332 ? 1.1586 1.0983 0.9664 -0.0137 -0.0123 -0.0119 332  GLN   E NE2 
13886 N  N   . LEU   E 333 ? 1.3261 1.2164 1.0665 -0.0102 -0.0430 -0.0172 333  LEU   E N   
13887 C  CA  . LEU   E 333 ? 1.3046 1.1755 1.0206 -0.0041 -0.0414 -0.0178 333  LEU   E CA  
13888 C  C   . LEU   E 333 ? 1.3583 1.2270 1.0720 0.0006  -0.0279 -0.0151 333  LEU   E C   
13889 O  O   . LEU   E 333 ? 1.3865 1.2601 1.1063 0.0010  -0.0205 -0.0122 333  LEU   E O   
13890 C  CB  . LEU   E 333 ? 1.3148 1.1730 1.0136 -0.0017 -0.0467 -0.0177 333  LEU   E CB  
13891 C  CG  . LEU   E 333 ? 1.3444 1.2009 1.0411 -0.0050 -0.0606 -0.0206 333  LEU   E CG  
13892 C  CD1 . LEU   E 333 ? 1.3074 1.1499 0.9853 -0.0013 -0.0644 -0.0204 333  LEU   E CD1 
13893 C  CD2 . LEU   E 333 ? 1.3653 1.2151 1.0556 -0.0053 -0.0675 -0.0241 333  LEU   E CD2 
13894 N  N   . VAL   E 334 ? 1.3601 1.2212 1.0652 0.0041  -0.0244 -0.0161 334  VAL   E N   
13895 C  CA  . VAL   E 334 ? 1.3844 1.2421 1.0863 0.0091  -0.0114 -0.0137 334  VAL   E CA  
13896 C  C   . VAL   E 334 ? 1.4085 1.2441 1.0822 0.0161  -0.0097 -0.0139 334  VAL   E C   
13897 O  O   . VAL   E 334 ? 1.4172 1.2409 1.0754 0.0170  -0.0189 -0.0167 334  VAL   E O   
13898 C  CB  . VAL   E 334 ? 1.4121 1.2800 1.1286 0.0081  -0.0070 -0.0143 334  VAL   E CB  
13899 C  CG1 . VAL   E 334 ? 1.3466 1.2353 1.0897 0.0018  -0.0084 -0.0140 334  VAL   E CG1 
13900 C  CG2 . VAL   E 334 ? 1.3207 1.1812 1.0279 0.0084  -0.0143 -0.0177 334  VAL   E CG2 
13901 N  N   . LYS   E 335 ? 1.4508 1.2803 1.1176 0.0211  0.0021  -0.0109 335  LYS   E N   
13902 C  CA  . LYS   E 335 ? 1.4976 1.3056 1.1370 0.0287  0.0058  -0.0105 335  LYS   E CA  
13903 C  C   . LYS   E 335 ? 1.5201 1.3268 1.1599 0.0327  0.0165  -0.0097 335  LYS   E C   
13904 O  O   . LYS   E 335 ? 1.5239 1.3411 1.1789 0.0326  0.0273  -0.0070 335  LYS   E O   
13905 C  CB  . LYS   E 335 ? 1.4580 1.2569 1.0857 0.0322  0.0115  -0.0074 335  LYS   E CB  
13906 N  N   . LEU   E 336 ? 1.5895 1.3839 1.2136 0.0360  0.0132  -0.0122 336  LEU   E N   
13907 C  CA  . LEU   E 336 ? 1.6413 1.4315 1.2618 0.0411  0.0234  -0.0114 336  LEU   E CA  
13908 C  C   . LEU   E 336 ? 1.6760 1.4502 1.2769 0.0486  0.0343  -0.0083 336  LEU   E C   
13909 O  O   . LEU   E 336 ? 1.6720 1.4303 1.2514 0.0518  0.0304  -0.0083 336  LEU   E O   
13910 C  CB  . LEU   E 336 ? 1.6023 1.3837 1.2116 0.0423  0.0159  -0.0151 336  LEU   E CB  
13911 C  CG  . LEU   E 336 ? 1.5139 1.3122 1.1446 0.0347  0.0067  -0.0177 336  LEU   E CG  
13912 C  CD1 . LEU   E 336 ? 1.4648 1.2582 1.0903 0.0353  0.0019  -0.0209 336  LEU   E CD1 
13913 C  CD2 . LEU   E 336 ? 1.5066 1.3253 1.1642 0.0313  0.0146  -0.0154 336  LEU   E CD2 
13914 N  N   . ASN   E 337 ? 1.7138 1.4927 1.3232 0.0515  0.0480  -0.0055 337  ASN   E N   
13915 C  CA  . ASN   E 337 ? 1.7900 1.5552 1.3837 0.0587  0.0608  -0.0020 337  ASN   E CA  
13916 C  C   . ASN   E 337 ? 1.8971 1.6532 1.4808 0.0650  0.0686  -0.0021 337  ASN   E C   
13917 O  O   . ASN   E 337 ? 1.9246 1.6892 1.5194 0.0631  0.0663  -0.0043 337  ASN   E O   
13918 C  CB  . ASN   E 337 ? 1.7823 1.5608 1.3957 0.0569  0.0721  0.0021  337  ASN   E CB  
13919 C  CG  . ASN   E 337 ? 1.6881 1.4688 1.3030 0.0534  0.0672  0.0031  337  ASN   E CG  
13920 O  OD1 . ASN   E 337 ? 1.6195 1.3850 1.2126 0.0555  0.0601  0.0022  337  ASN   E OD1 
13921 N  ND2 . ASN   E 337 ? 1.5755 1.3750 1.2162 0.0479  0.0705  0.0049  337  ASN   E ND2 
13922 N  N   . VAL   E 338 ? 1.9472 1.6857 1.5095 0.0728  0.0784  0.0004  338  VAL   E N   
13923 C  CA  . VAL   E 338 ? 1.9675 1.6963 1.5194 0.0796  0.0877  0.0009  338  VAL   E CA  
13924 C  C   . VAL   E 338 ? 1.9919 1.7310 1.5614 0.0812  0.1043  0.0049  338  VAL   E C   
13925 O  O   . VAL   E 338 ? 1.9892 1.7234 1.5546 0.0866  0.1133  0.0055  338  VAL   E O   
13926 C  CB  . VAL   E 338 ? 1.9732 1.6741 1.4884 0.0882  0.0884  0.0010  338  VAL   E CB  
13927 C  CG1 . VAL   E 338 ? 1.9083 1.6005 1.4145 0.0929  0.1010  0.0057  338  VAL   E CG1 
13928 C  CG2 . VAL   E 338 ? 2.0076 1.6978 1.5100 0.0942  0.0920  -0.0005 338  VAL   E CG2 
13929 N  N   . ASP   E 339 ? 2.0600 1.8132 1.6493 0.0768  0.1085  0.0075  339  ASP   E N   
13930 C  CA  . ASP   E 339 ? 2.0796 1.8449 1.6896 0.0772  0.1233  0.0110  339  ASP   E CA  
13931 C  C   . ASP   E 339 ? 2.0833 1.8740 1.7267 0.0684  0.1192  0.0103  339  ASP   E C   
13932 O  O   . ASP   E 339 ? 2.0701 1.8668 1.7179 0.0627  0.1075  0.0086  339  ASP   E O   
13933 C  CB  . ASP   E 339 ? 2.1228 1.8767 1.7213 0.0818  0.1356  0.0157  339  ASP   E CB  
13934 N  N   . SER   E 340 ? 2.0718 1.8775 1.7389 0.0677  0.1285  0.0116  340  SER   E N   
13935 C  CA  . SER   E 340 ? 2.0905 1.9200 1.7892 0.0599  0.1243  0.0106  340  SER   E CA  
13936 C  C   . SER   E 340 ? 2.0677 1.9054 1.7801 0.0564  0.1293  0.0138  340  SER   E C   
13937 O  O   . SER   E 340 ? 2.0272 1.8541 1.7284 0.0604  0.1391  0.0174  340  SER   E O   
13938 C  CB  . SER   E 340 ? 2.1197 1.9625 1.8394 0.0604  0.1310  0.0101  340  SER   E CB  
13939 O  OG  . SER   E 340 ? 2.1559 2.0015 1.8859 0.0635  0.1466  0.0139  340  SER   E OG  
13940 N  N   . ASN   E 341 ? 2.1518 2.0085 1.8883 0.0491  0.1224  0.0124  341  ASN   E N   
13941 C  CA  . ASN   E 341 ? 2.1427 2.0108 1.8977 0.0450  0.1269  0.0150  341  ASN   E CA  
13942 C  C   . ASN   E 341 ? 2.2797 2.1630 2.0613 0.0446  0.1376  0.0163  341  ASN   E C   
13943 O  O   . ASN   E 341 ? 2.2680 2.1510 2.0509 0.0484  0.1425  0.0156  341  ASN   E O   
13944 C  CB  . ASN   E 341 ? 1.9606 1.8403 1.7266 0.0376  0.1136  0.0128  341  ASN   E CB  
13945 N  N   . GLU   E 342 ? 2.4980 2.3948 2.3015 0.0402  0.1410  0.0181  342  GLU   E N   
13946 C  CA  . GLU   E 342 ? 2.5348 2.4475 2.3662 0.0392  0.1500  0.0190  342  GLU   E CA  
13947 C  C   . GLU   E 342 ? 2.5412 2.4672 2.3879 0.0369  0.1420  0.0149  342  GLU   E C   
13948 O  O   . GLU   E 342 ? 2.5915 2.5215 2.4471 0.0399  0.1485  0.0146  342  GLU   E O   
13949 C  CB  . GLU   E 342 ? 2.5308 2.4559 2.3832 0.0341  0.1526  0.0210  342  GLU   E CB  
13950 N  N   . GLN   E 343 ? 2.3444 2.2769 2.1936 0.0317  0.1281  0.0119  343  GLN   E N   
13951 C  CA  . GLN   E 343 ? 2.3031 2.2465 2.1642 0.0296  0.1200  0.0081  343  GLN   E CA  
13952 C  C   . GLN   E 343 ? 2.3161 2.2469 2.1570 0.0344  0.1176  0.0062  343  GLN   E C   
13953 O  O   . GLN   E 343 ? 2.2450 2.1823 2.0919 0.0329  0.1098  0.0029  343  GLN   E O   
13954 C  CB  . GLN   E 343 ? 2.1695 2.1225 2.0384 0.0229  0.1065  0.0058  343  GLN   E CB  
13955 N  N   . GLY   E 344 ? 2.5083 2.4207 2.3251 0.0402  0.1240  0.0081  344  GLY   E N   
13956 C  CA  . GLY   E 344 ? 2.4961 2.3944 2.2916 0.0454  0.1224  0.0064  344  GLY   E CA  
13957 C  C   . GLY   E 344 ? 2.4637 2.3530 2.2405 0.0436  0.1084  0.0035  344  GLY   E C   
13958 O  O   . GLY   E 344 ? 2.4565 2.3331 2.2144 0.0476  0.1059  0.0018  344  GLY   E O   
13959 N  N   . SER   E 345 ? 2.1306 2.0262 1.9127 0.0377  0.0992  0.0029  345  SER   E N   
13960 C  CA  . SER   E 345 ? 1.9196 1.8079 1.6865 0.0355  0.0857  0.0001  345  SER   E CA  
13961 C  C   . SER   E 345 ? 1.8854 1.7518 1.6219 0.0403  0.0858  0.0010  345  SER   E C   
13962 O  O   . SER   E 345 ? 1.9334 1.7913 1.6612 0.0440  0.0953  0.0042  345  SER   E O   
13963 C  CB  . SER   E 345 ? 1.8405 1.7411 1.6211 0.0283  0.0766  -0.0006 345  SER   E CB  
13964 O  OG  . SER   E 345 ? 1.7110 1.6024 1.4750 0.0267  0.0647  -0.0027 345  SER   E OG  
13965 N  N   . TYR   E 346 ? 1.7546 1.6113 1.4746 0.0403  0.0750  -0.0020 346  TYR   E N   
13966 C  CA  . TYR   E 346 ? 1.7446 1.5815 1.4364 0.0436  0.0711  -0.0021 346  TYR   E CA  
13967 C  C   . TYR   E 346 ? 1.6811 1.5203 1.3724 0.0380  0.0580  -0.0038 346  TYR   E C   
13968 O  O   . TYR   E 346 ? 1.6789 1.5035 1.3496 0.0400  0.0540  -0.0036 346  TYR   E O   
13969 C  CB  . TYR   E 346 ? 1.8627 1.6838 1.5332 0.0488  0.0689  -0.0044 346  TYR   E CB  
13970 C  CG  . TYR   E 346 ? 1.9646 1.7822 1.6339 0.0550  0.0818  -0.0028 346  TYR   E CG  
13971 C  CD1 . TYR   E 346 ? 2.0509 1.8771 1.7355 0.0562  0.0950  0.0007  346  TYR   E CD1 
13972 C  CD2 . TYR   E 346 ? 1.8952 1.7008 1.5487 0.0598  0.0810  -0.0049 346  TYR   E CD2 
13973 C  CE1 . TYR   E 346 ? 2.0463 1.8700 1.7313 0.0619  0.1072  0.0021  346  TYR   E CE1 
13974 C  CE2 . TYR   E 346 ? 2.0031 1.8058 1.6560 0.0658  0.0931  -0.0034 346  TYR   E CE2 
13975 C  CZ  . TYR   E 346 ? 2.0224 1.8345 1.6915 0.0668  0.1063  0.0001  346  TYR   E CZ  
13976 O  OH  . TYR   E 346 ? 2.0686 1.8788 1.7389 0.0726  0.1188  0.0017  346  TYR   E OH  
13977 N  N   . VAL   E 347 ? 1.6296 1.4864 1.3429 0.0313  0.0512  -0.0053 347  VAL   E N   
13978 C  CA  . VAL   E 347 ? 1.5865 1.4477 1.3027 0.0256  0.0396  -0.0067 347  VAL   E CA  
13979 C  C   . VAL   E 347 ? 1.5452 1.4144 1.2725 0.0233  0.0440  -0.0037 347  VAL   E C   
13980 O  O   . VAL   E 347 ? 1.5550 1.4357 1.3002 0.0227  0.0529  -0.0016 347  VAL   E O   
13981 C  CB  . VAL   E 347 ? 1.4458 1.3215 1.1797 0.0199  0.0308  -0.0095 347  VAL   E CB  
13982 C  CG1 . VAL   E 347 ? 1.3699 1.2453 1.1006 0.0152  0.0177  -0.0115 347  VAL   E CG1 
13983 C  CG2 . VAL   E 347 ? 1.4384 1.3094 1.1668 0.0228  0.0309  -0.0117 347  VAL   E CG2 
13984 N  N   . VAL   E 348 ? 1.4546 1.3172 1.1712 0.0221  0.0375  -0.0036 348  VAL   E N   
13985 C  CA  . VAL   E 348 ? 1.4390 1.3088 1.1655 0.0195  0.0401  -0.0010 348  VAL   E CA  
13986 C  C   . VAL   E 348 ? 1.4464 1.3179 1.1717 0.0149  0.0271  -0.0028 348  VAL   E C   
13987 O  O   . VAL   E 348 ? 1.4675 1.3245 1.1721 0.0170  0.0201  -0.0042 348  VAL   E O   
13988 C  CB  . VAL   E 348 ? 1.3978 1.2537 1.1083 0.0252  0.0504  0.0025  348  VAL   E CB  
13989 C  CG1 . VAL   E 348 ? 1.4537 1.2909 1.1373 0.0282  0.0435  0.0017  348  VAL   E CG1 
13990 C  CG2 . VAL   E 348 ? 1.4806 1.3477 1.2081 0.0224  0.0568  0.0055  348  VAL   E CG2 
13991 N  N   . ALA   E 349 ? 1.4003 1.2892 1.1478 0.0088  0.0234  -0.0030 349  ALA   E N   
13992 C  CA  . ALA   E 349 ? 1.3862 1.2783 1.1349 0.0042  0.0111  -0.0048 349  ALA   E CA  
13993 C  C   . ALA   E 349 ? 1.4980 1.3799 1.2326 0.0060  0.0103  -0.0031 349  ALA   E C   
13994 O  O   . ALA   E 349 ? 1.5119 1.3949 1.2498 0.0071  0.0189  0.0001  349  ALA   E O   
13995 C  CB  . ALA   E 349 ? 1.3151 1.2278 1.0904 -0.0021 0.0084  -0.0050 349  ALA   E CB  
13996 N  N   . MET   E 350 ? 1.5063 1.3777 1.2251 0.0063  0.0000  -0.0052 350  MET   E N   
13997 C  CA  . MET   E 350 ? 1.4642 1.3252 1.1685 0.0082  -0.0026 -0.0041 350  MET   E CA  
13998 C  C   . MET   E 350 ? 1.4335 1.3031 1.1468 0.0027  -0.0140 -0.0055 350  MET   E C   
13999 O  O   . MET   E 350 ? 1.5054 1.3673 1.2077 0.0040  -0.0176 -0.0049 350  MET   E O   
14000 C  CB  . MET   E 350 ? 1.5274 1.3664 1.2028 0.0143  -0.0051 -0.0053 350  MET   E CB  
14001 C  CG  . MET   E 350 ? 1.5141 1.3498 1.1843 0.0128  -0.0168 -0.0094 350  MET   E CG  
14002 S  SD  . MET   E 350 ? 1.6401 1.4483 1.2750 0.0205  -0.0202 -0.0110 350  MET   E SD  
14003 C  CE  . MET   E 350 ? 1.5424 1.3455 1.1690 0.0192  -0.0321 -0.0120 350  MET   E CE  
14004 N  N   . GLU   E 351 ? 1.3664 1.2510 1.0986 -0.0028 -0.0197 -0.0073 351  GLU   E N   
14005 C  CA  . GLU   E 351 ? 1.3196 1.2142 1.0632 -0.0082 -0.0293 -0.0084 351  GLU   E CA  
14006 C  C   . GLU   E 351 ? 1.2678 1.1801 1.0345 -0.0135 -0.0306 -0.0094 351  GLU   E C   
14007 O  O   . GLU   E 351 ? 1.3001 1.2145 1.0708 -0.0126 -0.0259 -0.0099 351  GLU   E O   
14008 C  CB  . GLU   E 351 ? 1.3482 1.2318 1.0766 -0.0078 -0.0413 -0.0112 351  GLU   E CB  
14009 C  CG  . GLU   E 351 ? 1.3813 1.2714 1.1167 -0.0117 -0.0500 -0.0116 351  GLU   E CG  
14010 C  CD  . GLU   E 351 ? 1.5142 1.3888 1.2292 -0.0090 -0.0593 -0.0134 351  GLU   E CD  
14011 O  OE1 . GLU   E 351 ? 1.5494 1.4282 1.2689 -0.0117 -0.0670 -0.0139 351  GLU   E OE1 
14012 O  OE2 . GLU   E 351 ? 1.5493 1.4074 1.2438 -0.0040 -0.0590 -0.0144 351  GLU   E OE2 
14013 N  N   . THR   E 352 ? 1.1929 1.1174 0.9743 -0.0185 -0.0368 -0.0097 352  THR   E N   
14014 C  CA  . THR   E 352 ? 1.1452 1.0856 0.9473 -0.0234 -0.0390 -0.0108 352  THR   E CA  
14015 C  C   . THR   E 352 ? 1.1487 1.0955 0.9579 -0.0280 -0.0494 -0.0121 352  THR   E C   
14016 O  O   . THR   E 352 ? 1.2811 1.2261 1.0869 -0.0281 -0.0518 -0.0111 352  THR   E O   
14017 C  CB  . THR   E 352 ? 1.0561 1.0094 0.8761 -0.0246 -0.0300 -0.0086 352  THR   E CB  
14018 O  OG1 . THR   E 352 ? 1.3036 1.2585 1.1253 -0.0248 -0.0277 -0.0062 352  THR   E OG1 
14019 C  CG2 . THR   E 352 ? 1.0903 1.0392 0.9066 -0.0204 -0.0195 -0.0075 352  THR   E CG2 
14020 N  N   . PHE   E 353 ? 1.1094 1.0635 0.9284 -0.0317 -0.0553 -0.0142 353  PHE   E N   
14021 C  CA  . PHE   E 353 ? 1.1158 1.0756 0.9418 -0.0360 -0.0653 -0.0155 353  PHE   E CA  
14022 C  C   . PHE   E 353 ? 1.0873 1.0640 0.9351 -0.0404 -0.0647 -0.0152 353  PHE   E C   
14023 O  O   . PHE   E 353 ? 1.1347 1.1152 0.9884 -0.0407 -0.0619 -0.0160 353  PHE   E O   
14024 C  CB  . PHE   E 353 ? 1.2044 1.1548 1.0196 -0.0361 -0.0738 -0.0184 353  PHE   E CB  
14025 C  CG  . PHE   E 353 ? 1.2178 1.1503 1.0100 -0.0312 -0.0749 -0.0190 353  PHE   E CG  
14026 C  CD1 . PHE   E 353 ? 1.1893 1.1111 0.9685 -0.0268 -0.0692 -0.0192 353  PHE   E CD1 
14027 C  CD2 . PHE   E 353 ? 1.2581 1.1840 1.0413 -0.0307 -0.0816 -0.0194 353  PHE   E CD2 
14028 C  CE1 . PHE   E 353 ? 1.2374 1.1416 0.9940 -0.0217 -0.0699 -0.0196 353  PHE   E CE1 
14029 C  CE2 . PHE   E 353 ? 1.2543 1.1626 1.0150 -0.0256 -0.0829 -0.0201 353  PHE   E CE2 
14030 C  CZ  . PHE   E 353 ? 1.2607 1.1579 1.0077 -0.0211 -0.0769 -0.0201 353  PHE   E CZ  
14031 N  N   . THR   E 354 ? 0.9957 0.9822 0.8551 -0.0434 -0.0668 -0.0142 354  THR   E N   
14032 C  CA  . THR   E 354 ? 1.0398 1.0411 0.9184 -0.0464 -0.0642 -0.0135 354  THR   E CA  
14033 C  C   . THR   E 354 ? 1.0324 1.0383 0.9180 -0.0496 -0.0702 -0.0156 354  THR   E C   
14034 O  O   . THR   E 354 ? 1.0082 1.0111 0.8904 -0.0514 -0.0781 -0.0170 354  THR   E O   
14035 C  CB  . THR   E 354 ? 1.0614 1.0721 0.9509 -0.0484 -0.0640 -0.0117 354  THR   E CB  
14036 O  OG1 . THR   E 354 ? 1.1859 1.1994 1.0785 -0.0515 -0.0726 -0.0126 354  THR   E OG1 
14037 C  CG2 . THR   E 354 ? 1.0390 1.0427 0.9190 -0.0453 -0.0591 -0.0098 354  THR   E CG2 
14038 N  N   . ASN   E 355 ? 0.9514 0.9641 0.8465 -0.0500 -0.0663 -0.0158 355  ASN   E N   
14039 C  CA  . ASN   E 355 ? 0.9663 0.9853 0.8707 -0.0531 -0.0704 -0.0173 355  ASN   E CA  
14040 C  C   . ASN   E 355 ? 0.9879 1.0206 0.9096 -0.0548 -0.0670 -0.0162 355  ASN   E C   
14041 O  O   . ASN   E 355 ? 0.9408 0.9766 0.8667 -0.0528 -0.0603 -0.0156 355  ASN   E O   
14042 C  CB  . ASN   E 355 ? 1.0852 1.0966 0.9816 -0.0512 -0.0696 -0.0190 355  ASN   E CB  
14043 C  CG  . ASN   E 355 ? 1.0131 1.0315 0.9200 -0.0538 -0.0716 -0.0201 355  ASN   E CG  
14044 O  OD1 . ASN   E 355 ? 0.9803 1.0044 0.8953 -0.0574 -0.0769 -0.0204 355  ASN   E OD1 
14045 N  ND2 . ASN   E 355 ? 1.0300 1.0474 0.9364 -0.0515 -0.0669 -0.0207 355  ASN   E ND2 
14046 N  N   . LEU   E 356 ? 0.9448 0.9855 0.8766 -0.0582 -0.0718 -0.0161 356  LEU   E N   
14047 C  CA  . LEU   E 356 ? 0.9218 0.9749 0.8692 -0.0599 -0.0697 -0.0152 356  LEU   E CA  
14048 C  C   . LEU   E 356 ? 1.0448 1.1016 0.9984 -0.0601 -0.0688 -0.0164 356  LEU   E C   
14049 O  O   . LEU   E 356 ? 1.0189 1.0842 0.9835 -0.0599 -0.0654 -0.0159 356  LEU   E O   
14050 C  CB  . LEU   E 356 ? 0.9472 1.0065 0.9020 -0.0632 -0.0752 -0.0147 356  LEU   E CB  
14051 C  CG  . LEU   E 356 ? 0.9791 1.0353 0.9285 -0.0630 -0.0771 -0.0136 356  LEU   E CG  
14052 C  CD1 . LEU   E 356 ? 0.8776 0.9405 0.8351 -0.0661 -0.0826 -0.0132 356  LEU   E CD1 
14053 C  CD2 . LEU   E 356 ? 1.0038 1.0610 0.9536 -0.0606 -0.0702 -0.0120 356  LEU   E CD2 
14054 N  N   . GLY   E 357 ? 1.0119 1.0623 0.9588 -0.0604 -0.0721 -0.0179 357  GLY   E N   
14055 C  CA  . GLY   E 357 ? 0.9343 0.9875 0.8864 -0.0609 -0.0721 -0.0190 357  GLY   E CA  
14056 C  C   . GLY   E 357 ? 0.9812 1.0310 0.9295 -0.0574 -0.0667 -0.0197 357  GLY   E C   
14057 O  O   . GLY   E 357 ? 0.9485 0.9919 0.8881 -0.0546 -0.0631 -0.0194 357  GLY   E O   
14058 N  N   . PRO   E 358 ? 0.9844 1.0385 0.9394 -0.0573 -0.0658 -0.0204 358  PRO   E N   
14059 C  CA  . PRO   E 358 ? 0.9610 1.0227 0.9265 -0.0600 -0.0689 -0.0203 358  PRO   E CA  
14060 C  C   . PRO   E 358 ? 0.9745 1.0463 0.9513 -0.0606 -0.0673 -0.0190 358  PRO   E C   
14061 O  O   . PRO   E 358 ? 0.9118 0.9865 0.8919 -0.0583 -0.0626 -0.0186 358  PRO   E O   
14062 C  CB  . PRO   E 358 ? 0.8932 0.9551 0.8604 -0.0582 -0.0669 -0.0215 358  PRO   E CB  
14063 C  CG  . PRO   E 358 ? 0.9469 1.0062 0.9104 -0.0544 -0.0614 -0.0218 358  PRO   E CG  
14064 C  CD  . PRO   E 358 ? 0.9560 1.0069 0.9079 -0.0540 -0.0616 -0.0214 358  PRO   E CD  
14065 N  N   . ILE   E 359 ? 0.9309 1.0077 0.9138 -0.0635 -0.0711 -0.0182 359  ILE   E N   
14066 C  CA  . ILE   E 359 ? 0.9230 1.0092 0.9168 -0.0641 -0.0701 -0.0170 359  ILE   E CA  
14067 C  C   . ILE   E 359 ? 0.9058 0.9979 0.9081 -0.0641 -0.0701 -0.0175 359  ILE   E C   
14068 O  O   . ILE   E 359 ? 0.9559 1.0481 0.9594 -0.0659 -0.0734 -0.0175 359  ILE   E O   
14069 C  CB  . ILE   E 359 ? 0.9266 1.0147 0.9217 -0.0669 -0.0741 -0.0159 359  ILE   E CB  
14070 C  CG1 . ILE   E 359 ? 0.8218 0.9058 0.8103 -0.0660 -0.0729 -0.0151 359  ILE   E CG1 
14071 C  CG2 . ILE   E 359 ? 0.9190 1.0168 0.9260 -0.0681 -0.0745 -0.0149 359  ILE   E CG2 
14072 C  CD1 . ILE   E 359 ? 0.8296 0.9108 0.8139 -0.0682 -0.0780 -0.0147 359  ILE   E CD1 
14073 N  N   . VAL   E 360 ? 0.8534 0.9500 0.8617 -0.0617 -0.0664 -0.0178 360  VAL   E N   
14074 C  CA  . VAL   E 360 ? 0.9123 1.0131 0.9271 -0.0607 -0.0664 -0.0186 360  VAL   E CA  
14075 C  C   . VAL   E 360 ? 0.9634 1.0728 0.9887 -0.0612 -0.0671 -0.0178 360  VAL   E C   
14076 O  O   . VAL   E 360 ? 0.9644 1.0767 0.9942 -0.0605 -0.0680 -0.0183 360  VAL   E O   
14077 C  CB  . VAL   E 360 ? 0.9169 1.0170 0.9319 -0.0572 -0.0626 -0.0199 360  VAL   E CB  
14078 C  CG1 . VAL   E 360 ? 0.8937 0.9846 0.8976 -0.0562 -0.0620 -0.0208 360  VAL   E CG1 
14079 C  CG2 . VAL   E 360 ? 0.8405 0.9454 0.8617 -0.0559 -0.0589 -0.0195 360  VAL   E CG2 
14080 N  N   . ASP   E 361 ? 0.9517 1.0645 0.9802 -0.0621 -0.0665 -0.0167 361  ASP   E N   
14081 C  CA  . ASP   E 361 ? 0.9118 1.0321 0.9496 -0.0626 -0.0673 -0.0160 361  ASP   E CA  
14082 C  C   . ASP   E 361 ? 0.9323 1.0535 0.9699 -0.0641 -0.0673 -0.0145 361  ASP   E C   
14083 O  O   . ASP   E 361 ? 0.9100 1.0266 0.9413 -0.0639 -0.0655 -0.0142 361  ASP   E O   
14084 C  CB  . ASP   E 361 ? 0.8521 0.9773 0.8977 -0.0600 -0.0649 -0.0170 361  ASP   E CB  
14085 C  CG  . ASP   E 361 ? 0.9075 1.0392 0.9615 -0.0601 -0.0669 -0.0168 361  ASP   E CG  
14086 O  OD1 . ASP   E 361 ? 0.8286 0.9612 0.8825 -0.0620 -0.0696 -0.0157 361  ASP   E OD1 
14087 O  OD2 . ASP   E 361 ? 0.9214 1.0572 0.9825 -0.0579 -0.0657 -0.0179 361  ASP   E OD2 
14088 N  N   . MET   E 362 ? 0.9077 1.0343 0.9514 -0.0654 -0.0692 -0.0135 362  MET   E N   
14089 C  CA  . MET   E 362 ? 0.9008 1.0283 0.9444 -0.0667 -0.0694 -0.0121 362  MET   E CA  
14090 C  C   . MET   E 362 ? 0.9365 1.0708 0.9885 -0.0673 -0.0708 -0.0113 362  MET   E C   
14091 O  O   . MET   E 362 ? 0.9971 1.1345 1.0535 -0.0671 -0.0723 -0.0117 362  MET   E O   
14092 C  CB  . MET   E 362 ? 0.8619 0.9839 0.8973 -0.0686 -0.0722 -0.0115 362  MET   E CB  
14093 C  CG  . MET   E 362 ? 0.8843 1.0075 0.9211 -0.0705 -0.0762 -0.0113 362  MET   E CG  
14094 S  SD  . MET   E 362 ? 1.0658 1.1835 1.0949 -0.0728 -0.0799 -0.0108 362  MET   E SD  
14095 C  CE  . MET   E 362 ? 0.8949 1.0142 0.9278 -0.0752 -0.0839 -0.0106 362  MET   E CE  
14096 N  N   . CYS   E 363 ? 1.0000 1.1360 1.0537 -0.0678 -0.0702 -0.0102 363  CYS   E N   
14097 C  CA  . CYS   E 363 ? 0.9482 1.0900 1.0088 -0.0685 -0.0717 -0.0093 363  CYS   E CA  
14098 C  C   . CYS   E 363 ? 0.9129 1.0536 0.9707 -0.0697 -0.0723 -0.0078 363  CYS   E C   
14099 O  O   . CYS   E 363 ? 0.9323 1.0684 0.9843 -0.0694 -0.0703 -0.0075 363  CYS   E O   
14100 C  CB  . CYS   E 363 ? 0.9398 1.0864 1.0087 -0.0668 -0.0697 -0.0100 363  CYS   E CB  
14101 S  SG  . CYS   E 363 ? 0.9900 1.1348 1.0590 -0.0657 -0.0647 -0.0102 363  CYS   E SG  
14102 N  N   . VAL   E 364 ? 0.9864 1.1309 1.0481 -0.0707 -0.0748 -0.0068 364  VAL   E N   
14103 C  CA  . VAL   E 364 ? 0.9761 1.1198 1.0355 -0.0716 -0.0758 -0.0053 364  VAL   E CA  
14104 C  C   . VAL   E 364 ? 1.0235 1.1710 1.0889 -0.0709 -0.0739 -0.0047 364  VAL   E C   
14105 O  O   . VAL   E 364 ? 1.0631 1.2156 1.1359 -0.0703 -0.0740 -0.0052 364  VAL   E O   
14106 C  CB  . VAL   E 364 ? 0.9591 1.1044 1.0190 -0.0731 -0.0800 -0.0046 364  VAL   E CB  
14107 C  CG1 . VAL   E 364 ? 1.0645 1.2085 1.1213 -0.0737 -0.0814 -0.0033 364  VAL   E CG1 
14108 C  CG2 . VAL   E 364 ? 1.0155 1.1571 1.0706 -0.0741 -0.0819 -0.0053 364  VAL   E CG2 
14109 N  N   . VAL   E 365 ? 1.0820 1.2268 1.1439 -0.0709 -0.0723 -0.0037 365  VAL   E N   
14110 C  CA  . VAL   E 365 ? 1.0243 1.1713 1.0913 -0.0703 -0.0695 -0.0032 365  VAL   E CA  
14111 C  C   . VAL   E 365 ? 1.2416 1.3850 1.3031 -0.0707 -0.0692 -0.0016 365  VAL   E C   
14112 O  O   . VAL   E 365 ? 1.2447 1.3818 1.2971 -0.0705 -0.0688 -0.0012 365  VAL   E O   
14113 C  CB  . VAL   E 365 ? 1.0220 1.1682 1.0913 -0.0692 -0.0649 -0.0042 365  VAL   E CB  
14114 C  CG1 . VAL   E 365 ? 1.1681 1.3154 1.2422 -0.0689 -0.0616 -0.0034 365  VAL   E CG1 
14115 C  CG2 . VAL   E 365 ? 1.0290 1.1793 1.1048 -0.0684 -0.0656 -0.0059 365  VAL   E CG2 
14116 N  N   . ASP   E 366 ? 1.3954 1.5420 1.4617 -0.0708 -0.0696 -0.0006 366  ASP   E N   
14117 C  CA  . ASP   E 366 ? 1.4122 1.5552 1.4735 -0.0709 -0.0692 0.0010  366  ASP   E CA  
14118 C  C   . ASP   E 366 ? 1.3803 1.5212 1.4429 -0.0702 -0.0638 0.0016  366  ASP   E C   
14119 O  O   . ASP   E 366 ? 1.4022 1.5462 1.4714 -0.0703 -0.0626 0.0020  366  ASP   E O   
14120 C  CB  . ASP   E 366 ? 1.4277 1.5748 1.4928 -0.0713 -0.0727 0.0019  366  ASP   E CB  
14121 C  CG  . ASP   E 366 ? 1.4849 1.6277 1.5431 -0.0712 -0.0735 0.0035  366  ASP   E CG  
14122 O  OD1 . ASP   E 366 ? 1.5016 1.6377 1.5518 -0.0706 -0.0710 0.0040  366  ASP   E OD1 
14123 O  OD2 . ASP   E 366 ? 1.5195 1.6651 1.5799 -0.0714 -0.0767 0.0042  366  ASP   E OD2 
14124 N  N   . LEU   E 367 ? 1.3146 1.4499 1.3709 -0.0695 -0.0603 0.0015  367  LEU   E N   
14125 C  CA  . LEU   E 367 ? 1.2814 1.4152 1.3405 -0.0689 -0.0542 0.0019  367  LEU   E CA  
14126 C  C   . LEU   E 367 ? 1.3493 1.4802 1.4064 -0.0689 -0.0523 0.0039  367  LEU   E C   
14127 O  O   . LEU   E 367 ? 1.3154 1.4470 1.3785 -0.0688 -0.0477 0.0044  367  LEU   E O   
14128 C  CB  . LEU   E 367 ? 1.2161 1.3439 1.2679 -0.0678 -0.0506 0.0017  367  LEU   E CB  
14129 C  CG  . LEU   E 367 ? 1.1632 1.2944 1.2203 -0.0675 -0.0501 -0.0003 367  LEU   E CG  
14130 C  CD1 . LEU   E 367 ? 1.1344 1.2596 1.1854 -0.0660 -0.0451 -0.0003 367  LEU   E CD1 
14131 C  CD2 . LEU   E 367 ? 1.1262 1.2650 1.1973 -0.0677 -0.0491 -0.0012 367  LEU   E CD2 
14132 N  N   . GLU   E 368 ? 1.3920 1.5198 1.4414 -0.0689 -0.0559 0.0049  368  GLU   E N   
14133 C  CA  . GLU   E 368 ? 1.4544 1.5785 1.5003 -0.0685 -0.0544 0.0069  368  GLU   E CA  
14134 C  C   . GLU   E 368 ? 1.5155 1.6449 1.5670 -0.0693 -0.0587 0.0072  368  GLU   E C   
14135 O  O   . GLU   E 368 ? 1.5397 1.6659 1.5873 -0.0689 -0.0586 0.0088  368  GLU   E O   
14136 C  CB  . GLU   E 368 ? 1.3712 1.4862 1.4024 -0.0672 -0.0551 0.0079  368  GLU   E CB  
14137 C  CG  . GLU   E 368 ? 1.2521 1.3605 1.2764 -0.0660 -0.0502 0.0078  368  GLU   E CG  
14138 C  CD  . GLU   E 368 ? 1.3431 1.4417 1.3519 -0.0644 -0.0516 0.0085  368  GLU   E CD  
14139 O  OE1 . GLU   E 368 ? 1.3751 1.4722 1.3795 -0.0642 -0.0558 0.0093  368  GLU   E OE1 
14140 O  OE2 . GLU   E 368 ? 1.3575 1.4497 1.3581 -0.0630 -0.0490 0.0082  368  GLU   E OE2 
14141 N  N   . ARG   E 369 ? 1.5943 1.7310 1.6541 -0.0700 -0.0621 0.0058  369  ARG   E N   
14142 C  CA  . ARG   E 369 ? 1.6146 1.7564 1.6798 -0.0704 -0.0659 0.0061  369  ARG   E CA  
14143 C  C   . ARG   E 369 ? 1.6464 1.7846 1.7036 -0.0700 -0.0691 0.0075  369  ARG   E C   
14144 O  O   . ARG   E 369 ? 1.6724 1.8112 1.7309 -0.0698 -0.0698 0.0086  369  ARG   E O   
14145 C  CB  . ARG   E 369 ? 1.5624 1.7071 1.6364 -0.0706 -0.0631 0.0063  369  ARG   E CB  
14146 N  N   . GLN   E 370 ? 1.5950 1.7291 1.6435 -0.0697 -0.0714 0.0073  370  GLN   E N   
14147 C  CA  . GLN   E 370 ? 1.5891 1.7201 1.6303 -0.0692 -0.0756 0.0082  370  GLN   E CA  
14148 C  C   . GLN   E 370 ? 1.5891 1.7252 1.6336 -0.0699 -0.0813 0.0074  370  GLN   E C   
14149 O  O   . GLN   E 370 ? 1.5478 1.6818 1.5873 -0.0696 -0.0855 0.0077  370  GLN   E O   
14150 C  CB  . GLN   E 370 ? 1.5610 1.6826 1.5894 -0.0680 -0.0747 0.0085  370  GLN   E CB  
14151 C  CG  . GLN   E 370 ? 1.5983 1.7139 1.6228 -0.0671 -0.0678 0.0094  370  GLN   E CG  
14152 C  CD  . GLN   E 370 ? 1.6303 1.7425 1.6527 -0.0663 -0.0652 0.0113  370  GLN   E CD  
14153 O  OE1 . GLN   E 370 ? 1.6546 1.7721 1.6861 -0.0671 -0.0644 0.0117  370  GLN   E OE1 
14154 N  NE2 . GLN   E 370 ? 1.5728 1.6753 1.5825 -0.0645 -0.0638 0.0125  370  GLN   E NE2 
14155 N  N   . GLY   E 371 ? 1.5863 1.7288 1.6394 -0.0709 -0.0816 0.0063  371  GLY   E N   
14156 C  CA  . GLY   E 371 ? 1.5429 1.6902 1.5999 -0.0716 -0.0861 0.0057  371  GLY   E CA  
14157 C  C   . GLY   E 371 ? 1.5395 1.6834 1.5906 -0.0722 -0.0888 0.0049  371  GLY   E C   
14158 O  O   . GLY   E 371 ? 1.4680 1.6147 1.5213 -0.0729 -0.0931 0.0047  371  GLY   E O   
14159 N  N   . GLN   E 372 ? 1.5414 1.6793 1.5855 -0.0718 -0.0863 0.0043  372  GLN   E N   
14160 C  CA  . GLN   E 372 ? 1.4868 1.6197 1.5236 -0.0721 -0.0887 0.0034  372  GLN   E CA  
14161 C  C   . GLN   E 372 ? 1.4595 1.5945 1.4998 -0.0730 -0.0879 0.0020  372  GLN   E C   
14162 O  O   . GLN   E 372 ? 1.4301 1.5670 1.4724 -0.0742 -0.0915 0.0012  372  GLN   E O   
14163 C  CB  . GLN   E 372 ? 1.4717 1.5953 1.4969 -0.0706 -0.0863 0.0037  372  GLN   E CB  
14164 C  CG  . GLN   E 372 ? 1.5025 1.6191 1.5179 -0.0703 -0.0891 0.0026  372  GLN   E CG  
14165 C  CD  . GLN   E 372 ? 1.5206 1.6364 1.5335 -0.0705 -0.0959 0.0024  372  GLN   E CD  
14166 O  OE1 . GLN   E 372 ? 1.5000 1.6229 1.5214 -0.0716 -0.0989 0.0027  372  GLN   E OE1 
14167 N  NE2 . GLN   E 372 ? 1.4856 1.5926 1.4868 -0.0693 -0.0983 0.0018  372  GLN   E NE2 
14168 N  N   . GLY   E 373 ? 1.4205 1.5552 1.4621 -0.0725 -0.0831 0.0016  373  GLY   E N   
14169 C  CA  . GLY   E 373 ? 1.3355 1.4713 1.3792 -0.0729 -0.0823 0.0002  373  GLY   E CA  
14170 C  C   . GLY   E 373 ? 1.2970 1.4252 1.3313 -0.0723 -0.0808 -0.0006 373  GLY   E C   
14171 O  O   . GLY   E 373 ? 1.2940 1.4165 1.3199 -0.0722 -0.0836 -0.0007 373  GLY   E O   
14172 N  N   . GLN   E 374 ? 1.2030 1.3309 1.2387 -0.0716 -0.0764 -0.0012 374  GLN   E N   
14173 C  CA  . GLN   E 374 ? 1.1658 1.2868 1.1932 -0.0706 -0.0743 -0.0020 374  GLN   E CA  
14174 C  C   . GLN   E 374 ? 1.1395 1.2630 1.1710 -0.0708 -0.0737 -0.0035 374  GLN   E C   
14175 O  O   . GLN   E 374 ? 1.1089 1.2387 1.1496 -0.0709 -0.0724 -0.0038 374  GLN   E O   
14176 C  CB  . GLN   E 374 ? 1.1681 1.2850 1.1919 -0.0690 -0.0686 -0.0012 374  GLN   E CB  
14177 C  CG  . GLN   E 374 ? 1.2531 1.3653 1.2701 -0.0683 -0.0687 0.0003  374  GLN   E CG  
14178 C  CD  . GLN   E 374 ? 1.3443 1.4592 1.3674 -0.0680 -0.0642 0.0017  374  GLN   E CD  
14179 O  OE1 . GLN   E 374 ? 1.2553 1.3697 1.2807 -0.0671 -0.0586 0.0017  374  GLN   E OE1 
14180 N  NE2 . GLN   E 374 ? 1.3536 1.4719 1.3801 -0.0686 -0.0667 0.0027  374  GLN   E NE2 
14181 N  N   . LEU   E 375 ? 1.0820 1.2001 1.1063 -0.0708 -0.0750 -0.0046 375  LEU   E N   
14182 C  CA  . LEU   E 375 ? 1.0263 1.1455 1.0530 -0.0707 -0.0742 -0.0060 375  LEU   E CA  
14183 C  C   . LEU   E 375 ? 0.9850 1.1009 1.0091 -0.0687 -0.0688 -0.0064 375  LEU   E C   
14184 O  O   . LEU   E 375 ? 0.9849 1.0935 0.9996 -0.0675 -0.0669 -0.0061 375  LEU   E O   
14185 C  CB  . LEU   E 375 ? 1.0221 1.1371 1.0431 -0.0718 -0.0784 -0.0069 375  LEU   E CB  
14186 C  CG  . LEU   E 375 ? 0.9467 1.0647 0.9725 -0.0726 -0.0796 -0.0080 375  LEU   E CG  
14187 C  CD1 . LEU   E 375 ? 0.9418 1.0681 0.9787 -0.0727 -0.0789 -0.0076 375  LEU   E CD1 
14188 C  CD2 . LEU   E 375 ? 0.9331 1.0490 0.9565 -0.0746 -0.0848 -0.0083 375  LEU   E CD2 
14189 N  N   . VAL   E 376 ? 0.8954 1.0165 0.9278 -0.0681 -0.0662 -0.0071 376  VAL   E N   
14190 C  CA  . VAL   E 376 ? 0.9466 1.0657 0.9787 -0.0662 -0.0610 -0.0077 376  VAL   E CA  
14191 C  C   . VAL   E 376 ? 0.9990 1.1181 1.0316 -0.0656 -0.0616 -0.0094 376  VAL   E C   
14192 O  O   . VAL   E 376 ? 0.9622 1.0869 1.0022 -0.0660 -0.0635 -0.0100 376  VAL   E O   
14193 C  CB  . VAL   E 376 ? 0.9318 1.0566 0.9738 -0.0655 -0.0572 -0.0072 376  VAL   E CB  
14194 C  CG1 . VAL   E 376 ? 0.9148 1.0404 0.9607 -0.0637 -0.0530 -0.0084 376  VAL   E CG1 
14195 C  CG2 . VAL   E 376 ? 0.9644 1.0857 1.0025 -0.0653 -0.0544 -0.0055 376  VAL   E CG2 
14196 N  N   . THR   E 377 ? 0.9703 1.0825 0.9942 -0.0643 -0.0598 -0.0100 377  THR   E N   
14197 C  CA  . THR   E 377 ? 0.8891 0.9989 0.9101 -0.0639 -0.0611 -0.0115 377  THR   E CA  
14198 C  C   . THR   E 377 ? 0.9378 1.0463 0.9592 -0.0613 -0.0562 -0.0124 377  THR   E C   
14199 O  O   . THR   E 377 ? 0.9360 1.0407 0.9535 -0.0599 -0.0519 -0.0118 377  THR   E O   
14200 C  CB  . THR   E 377 ? 0.8798 0.9813 0.8890 -0.0646 -0.0642 -0.0117 377  THR   E CB  
14201 O  OG1 . THR   E 377 ? 0.8191 0.9131 0.8188 -0.0627 -0.0608 -0.0114 377  THR   E OG1 
14202 C  CG2 . THR   E 377 ? 0.9016 1.0042 0.9106 -0.0669 -0.0692 -0.0108 377  THR   E CG2 
14203 N  N   . CYS   E 378 ? 0.9546 1.0656 0.9804 -0.0605 -0.0566 -0.0139 378  CYS   E N   
14204 C  CA  . CYS   E 378 ? 0.9559 1.0641 0.9797 -0.0580 -0.0530 -0.0151 378  CYS   E CA  
14205 C  C   . CYS   E 378 ? 0.8908 0.9898 0.9018 -0.0578 -0.0544 -0.0156 378  CYS   E C   
14206 O  O   . CYS   E 378 ? 0.8687 0.9663 0.8772 -0.0592 -0.0587 -0.0162 378  CYS   E O   
14207 C  CB  . CYS   E 378 ? 0.9498 1.0633 0.9819 -0.0569 -0.0536 -0.0166 378  CYS   E CB  
14208 S  SG  . CYS   E 378 ? 0.9816 1.1053 1.0287 -0.0569 -0.0531 -0.0165 378  CYS   E SG  
14209 N  N   . SER   E 379 ? 0.8891 0.9816 0.8922 -0.0558 -0.0506 -0.0155 379  SER   E N   
14210 C  CA  . SER   E 379 ? 0.9020 0.9845 0.8913 -0.0557 -0.0524 -0.0158 379  SER   E CA  
14211 C  C   . SER   E 379 ? 0.9602 1.0364 0.9427 -0.0525 -0.0482 -0.0167 379  SER   E C   
14212 O  O   . SER   E 379 ? 0.9504 1.0282 0.9365 -0.0503 -0.0424 -0.0163 379  SER   E O   
14213 C  CB  . SER   E 379 ? 0.8779 0.9559 0.8600 -0.0565 -0.0533 -0.0144 379  SER   E CB  
14214 O  OG  . SER   E 379 ? 0.9453 1.0259 0.9294 -0.0595 -0.0591 -0.0141 379  SER   E OG  
14215 N  N   . GLY   E 380 ? 0.9253 0.9943 0.8983 -0.0524 -0.0510 -0.0178 380  GLY   E N   
14216 C  CA  . GLY   E 380 ? 0.9823 1.0446 0.9479 -0.0492 -0.0475 -0.0188 380  GLY   E CA  
14217 C  C   . GLY   E 380 ? 0.9908 1.0590 0.9657 -0.0475 -0.0452 -0.0199 380  GLY   E C   
14218 O  O   . GLY   E 380 ? 0.9874 1.0637 0.9730 -0.0489 -0.0473 -0.0202 380  GLY   E O   
14219 N  N   . ALA   E 381 ? 1.0188 1.0823 0.9889 -0.0442 -0.0408 -0.0206 381  ALA   E N   
14220 C  CA  . ALA   E 381 ? 0.9924 1.0607 0.9706 -0.0419 -0.0386 -0.0219 381  ALA   E CA  
14221 C  C   . ALA   E 381 ? 1.0152 1.0794 0.9897 -0.0380 -0.0319 -0.0219 381  ALA   E C   
14222 O  O   . ALA   E 381 ? 1.0555 1.1101 1.0171 -0.0368 -0.0302 -0.0214 381  ALA   E O   
14223 C  CB  . ALA   E 381 ? 0.9423 1.0076 0.9167 -0.0423 -0.0430 -0.0235 381  ALA   E CB  
14224 N  N   . PHE   E 382 ? 0.9550 1.0262 0.9409 -0.0359 -0.0282 -0.0225 382  PHE   E N   
14225 C  CA  . PHE   E 382 ? 1.0295 1.0981 1.0143 -0.0320 -0.0214 -0.0226 382  PHE   E CA  
14226 C  C   . PHE   E 382 ? 1.0861 1.1525 1.0686 -0.0317 -0.0161 -0.0205 382  PHE   E C   
14227 O  O   . PHE   E 382 ? 1.0994 1.1715 1.0893 -0.0341 -0.0166 -0.0192 382  PHE   E O   
14228 C  CB  . PHE   E 382 ? 1.0398 1.0979 1.0105 -0.0296 -0.0219 -0.0238 382  PHE   E CB  
14229 C  CG  . PHE   E 382 ? 1.0386 1.0970 1.0090 -0.0306 -0.0279 -0.0255 382  PHE   E CG  
14230 C  CD1 . PHE   E 382 ? 1.0344 1.1012 1.0172 -0.0300 -0.0290 -0.0267 382  PHE   E CD1 
14231 C  CD2 . PHE   E 382 ? 1.0317 1.0811 0.9891 -0.0321 -0.0326 -0.0259 382  PHE   E CD2 
14232 C  CE1 . PHE   E 382 ? 1.0487 1.1144 1.0296 -0.0306 -0.0340 -0.0281 382  PHE   E CE1 
14233 C  CE2 . PHE   E 382 ? 1.0729 1.1217 1.0296 -0.0332 -0.0375 -0.0272 382  PHE   E CE2 
14234 C  CZ  . PHE   E 382 ? 1.0142 1.0708 0.9822 -0.0323 -0.0379 -0.0282 382  PHE   E CZ  
14235 N  N   . LYS   E 383 ? 1.0751 1.1326 1.0468 -0.0286 -0.0109 -0.0199 383  LYS   E N   
14236 C  CA  . LYS   E 383 ? 1.1279 1.1825 1.0970 -0.0279 -0.0050 -0.0176 383  LYS   E CA  
14237 C  C   . LYS   E 383 ? 1.1608 1.2117 1.1221 -0.0309 -0.0093 -0.0164 383  LYS   E C   
14238 O  O   . LYS   E 383 ? 1.2014 1.2517 1.1627 -0.0310 -0.0054 -0.0144 383  LYS   E O   
14239 C  CB  . LYS   E 383 ? 1.2173 1.2615 1.1741 -0.0234 0.0014  -0.0172 383  LYS   E CB  
14240 C  CG  . LYS   E 383 ? 1.2043 1.2344 1.1399 -0.0226 -0.0020 -0.0176 383  LYS   E CG  
14241 C  CD  . LYS   E 383 ? 1.2012 1.2218 1.1258 -0.0176 0.0042  -0.0177 383  LYS   E CD  
14242 C  CE  . LYS   E 383 ? 1.2390 1.2441 1.1415 -0.0161 0.0029  -0.0173 383  LYS   E CE  
14243 N  NZ  . LYS   E 383 ? 1.2659 1.2662 1.1627 -0.0149 0.0086  -0.0147 383  LYS   E NZ  
14244 N  N   . GLU   E 384 ? 1.2287 1.2770 1.1837 -0.0333 -0.0170 -0.0174 384  GLU   E N   
14245 C  CA  . GLU   E 384 ? 1.2373 1.2830 1.1865 -0.0363 -0.0217 -0.0165 384  GLU   E CA  
14246 C  C   . GLU   E 384 ? 1.1766 1.2338 1.1402 -0.0398 -0.0250 -0.0161 384  GLU   E C   
14247 O  O   . GLU   E 384 ? 1.1878 1.2443 1.1485 -0.0424 -0.0292 -0.0153 384  GLU   E O   
14248 C  CB  . GLU   E 384 ? 1.2554 1.2925 1.1914 -0.0372 -0.0284 -0.0178 384  GLU   E CB  
14249 C  CG  . GLU   E 384 ? 1.2758 1.3003 1.1959 -0.0336 -0.0263 -0.0185 384  GLU   E CG  
14250 C  CD  . GLU   E 384 ? 1.3406 1.3577 1.2519 -0.0301 -0.0190 -0.0169 384  GLU   E CD  
14251 O  OE1 . GLU   E 384 ? 1.3958 1.4130 1.3067 -0.0309 -0.0177 -0.0151 384  GLU   E OE1 
14252 O  OE2 . GLU   E 384 ? 1.3706 1.3811 1.2748 -0.0262 -0.0142 -0.0173 384  GLU   E OE2 
14253 N  N   . GLY   E 385 ? 1.0273 1.0946 1.0061 -0.0398 -0.0234 -0.0167 385  GLY   E N   
14254 C  CA  . GLY   E 385 ? 1.0104 1.0880 1.0024 -0.0428 -0.0266 -0.0165 385  GLY   E CA  
14255 C  C   . GLY   E 385 ? 0.9899 1.0695 0.9846 -0.0442 -0.0248 -0.0144 385  GLY   E C   
14256 O  O   . GLY   E 385 ? 0.9978 1.0758 0.9929 -0.0425 -0.0183 -0.0131 385  GLY   E O   
14257 N  N   . SER   E 386 ? 0.9196 1.0025 0.9165 -0.0473 -0.0301 -0.0140 386  SER   E N   
14258 C  CA  . SER   E 386 ? 0.8936 0.9759 0.8894 -0.0484 -0.0288 -0.0120 386  SER   E CA  
14259 C  C   . SER   E 386 ? 0.9525 1.0422 0.9564 -0.0517 -0.0340 -0.0118 386  SER   E C   
14260 O  O   . SER   E 386 ? 0.9713 1.0622 0.9747 -0.0533 -0.0399 -0.0128 386  SER   E O   
14261 C  CB  . SER   E 386 ? 0.9496 1.0202 0.9281 -0.0477 -0.0296 -0.0112 386  SER   E CB  
14262 O  OG  . SER   E 386 ? 0.9402 1.0093 0.9138 -0.0501 -0.0373 -0.0120 386  SER   E OG  
14263 N  N   . LEU   E 387 ? 0.9662 1.0603 0.9773 -0.0525 -0.0317 -0.0103 387  LEU   E N   
14264 C  CA  . LEU   E 387 ? 0.9605 1.0589 0.9753 -0.0552 -0.0365 -0.0096 387  LEU   E CA  
14265 C  C   . LEU   E 387 ? 0.9433 1.0336 0.9450 -0.0557 -0.0384 -0.0084 387  LEU   E C   
14266 O  O   . LEU   E 387 ? 0.9154 0.9981 0.9080 -0.0538 -0.0341 -0.0073 387  LEU   E O   
14267 C  CB  . LEU   E 387 ? 0.8729 0.9793 0.9011 -0.0559 -0.0338 -0.0088 387  LEU   E CB  
14268 C  CG  . LEU   E 387 ? 0.8511 0.9657 0.8923 -0.0555 -0.0338 -0.0106 387  LEU   E CG  
14269 C  CD1 . LEU   E 387 ? 0.9423 1.0655 0.9967 -0.0569 -0.0350 -0.0104 387  LEU   E CD1 
14270 C  CD2 . LEU   E 387 ? 0.9303 1.0445 0.9683 -0.0556 -0.0390 -0.0123 387  LEU   E CD2 
14271 N  N   . ARG   E 388 ? 0.9260 1.0175 0.9265 -0.0579 -0.0450 -0.0086 388  ARG   E N   
14272 C  CA  . ARG   E 388 ? 0.9477 1.0328 0.9375 -0.0586 -0.0484 -0.0077 388  ARG   E CA  
14273 C  C   . ARG   E 388 ? 0.9854 1.0772 0.9829 -0.0609 -0.0517 -0.0068 388  ARG   E C   
14274 O  O   . ARG   E 388 ? 0.9899 1.0897 0.9976 -0.0625 -0.0544 -0.0074 388  ARG   E O   
14275 C  CB  . ARG   E 388 ? 0.9183 0.9978 0.8992 -0.0591 -0.0539 -0.0091 388  ARG   E CB  
14276 C  CG  . ARG   E 388 ? 0.9044 0.9767 0.8769 -0.0567 -0.0511 -0.0102 388  ARG   E CG  
14277 C  CD  . ARG   E 388 ? 0.8831 0.9440 0.8407 -0.0543 -0.0487 -0.0095 388  ARG   E CD  
14278 N  NE  . ARG   E 388 ? 0.9370 0.9917 0.8879 -0.0515 -0.0444 -0.0103 388  ARG   E NE  
14279 C  CZ  . ARG   E 388 ? 0.9919 1.0347 0.9270 -0.0492 -0.0443 -0.0106 388  ARG   E CZ  
14280 N  NH1 . ARG   E 388 ? 0.9830 1.0184 0.9071 -0.0493 -0.0486 -0.0103 388  ARG   E NH1 
14281 N  NH2 . ARG   E 388 ? 1.0064 1.0442 0.9364 -0.0464 -0.0400 -0.0113 388  ARG   E NH2 
14282 N  N   . ILE   E 389 ? 0.9742 1.0623 0.9663 -0.0607 -0.0512 -0.0052 389  ILE   E N   
14283 C  CA  . ILE   E 389 ? 0.9935 1.0870 0.9915 -0.0626 -0.0545 -0.0042 389  ILE   E CA  
14284 C  C   . ILE   E 389 ? 1.0377 1.1249 1.0250 -0.0630 -0.0598 -0.0040 389  ILE   E C   
14285 O  O   . ILE   E 389 ? 1.0556 1.1333 1.0305 -0.0611 -0.0584 -0.0034 389  ILE   E O   
14286 C  CB  . ILE   E 389 ? 0.9899 1.0856 0.9932 -0.0621 -0.0493 -0.0026 389  ILE   E CB  
14287 C  CG1 . ILE   E 389 ? 0.9704 1.0730 0.9860 -0.0618 -0.0447 -0.0032 389  ILE   E CG1 
14288 C  CG2 . ILE   E 389 ? 1.0203 1.1204 1.0279 -0.0638 -0.0531 -0.0016 389  ILE   E CG2 
14289 C  CD1 . ILE   E 389 ? 0.9638 1.0611 0.9753 -0.0594 -0.0380 -0.0031 389  ILE   E CD1 
14290 N  N   . ILE   E 390 ? 1.0173 1.1094 1.0094 -0.0652 -0.0658 -0.0044 390  ILE   E N   
14291 C  CA  . ILE   E 390 ? 1.0827 1.1701 1.0670 -0.0658 -0.0721 -0.0048 390  ILE   E CA  
14292 C  C   . ILE   E 390 ? 1.1387 1.2313 1.1286 -0.0671 -0.0752 -0.0036 390  ILE   E C   
14293 O  O   . ILE   E 390 ? 1.1370 1.2386 1.1385 -0.0688 -0.0763 -0.0035 390  ILE   E O   
14294 C  CB  . ILE   E 390 ? 1.0751 1.1632 1.0604 -0.0674 -0.0767 -0.0065 390  ILE   E CB  
14295 C  CG1 . ILE   E 390 ? 1.0245 1.1068 1.0034 -0.0658 -0.0738 -0.0077 390  ILE   E CG1 
14296 C  CG2 . ILE   E 390 ? 0.9737 1.0580 0.9533 -0.0685 -0.0839 -0.0070 390  ILE   E CG2 
14297 C  CD1 . ILE   E 390 ? 0.9808 1.0686 0.9679 -0.0670 -0.0741 -0.0089 390  ILE   E CD1 
14298 N  N   . ARG   E 391 ? 1.1668 1.2532 1.1477 -0.0660 -0.0766 -0.0028 391  ARG   E N   
14299 C  CA  . ARG   E 391 ? 1.1954 1.2854 1.1799 -0.0667 -0.0794 -0.0016 391  ARG   E CA  
14300 C  C   . ARG   E 391 ? 1.2093 1.2933 1.1848 -0.0665 -0.0861 -0.0021 391  ARG   E C   
14301 O  O   . ARG   E 391 ? 1.2502 1.3250 1.2139 -0.0650 -0.0872 -0.0030 391  ARG   E O   
14302 C  CB  . ARG   E 391 ? 1.1415 1.2295 1.1243 -0.0651 -0.0738 0.0003  391  ARG   E CB  
14303 N  N   . ASN   E 392 ? 1.2350 1.3244 1.2164 -0.0678 -0.0907 -0.0017 392  ASN   E N   
14304 C  CA  . ASN   E 392 ? 1.2724 1.3564 1.2461 -0.0672 -0.0970 -0.0021 392  ASN   E CA  
14305 C  C   . ASN   E 392 ? 1.2454 1.3243 1.2117 -0.0649 -0.0955 -0.0005 392  ASN   E C   
14306 O  O   . ASN   E 392 ? 1.2343 1.3044 1.1887 -0.0630 -0.0991 -0.0008 392  ASN   E O   
14307 C  CB  . ASN   E 392 ? 1.2735 1.3656 1.2575 -0.0696 -0.1032 -0.0026 392  ASN   E CB  
14308 C  CG  . ASN   E 392 ? 1.2288 1.3237 1.2180 -0.0718 -0.1054 -0.0042 392  ASN   E CG  
14309 O  OD1 . ASN   E 392 ? 1.2853 1.3749 1.2685 -0.0713 -0.1036 -0.0052 392  ASN   E OD1 
14310 N  ND2 . ASN   E 392 ? 1.1954 1.2984 1.1957 -0.0741 -0.1090 -0.0042 392  ASN   E ND2 
14311 N  N   . LEU   E 406 ? 1.1240 1.1715 1.0543 -0.0632 -0.1064 -0.0088 710  LEU   E N   
14312 C  CA  . LEU   E 406 ? 1.2252 1.2802 1.1642 -0.0634 -0.0988 -0.0068 710  LEU   E CA  
14313 C  C   . LEU   E 406 ? 1.1673 1.2152 1.0973 -0.0604 -0.0909 -0.0059 710  LEU   E C   
14314 O  O   . LEU   E 406 ? 1.2456 1.2833 1.1629 -0.0583 -0.0909 -0.0069 710  LEU   E O   
14315 C  CB  . LEU   E 406 ? 1.2717 1.3379 1.2260 -0.0665 -0.0980 -0.0071 710  LEU   E CB  
14316 C  CG  . LEU   E 406 ? 1.1805 1.2445 1.1338 -0.0677 -0.1004 -0.0091 710  LEU   E CG  
14317 C  CD1 . LEU   E 406 ? 1.2416 1.2991 1.1868 -0.0654 -0.0943 -0.0094 710  LEU   E CD1 
14318 C  CD2 . LEU   E 406 ? 1.0443 1.1189 1.0124 -0.0710 -0.1017 -0.0094 710  LEU   E CD2 
14319 N  N   . HIS   E 407 ? 1.2642 1.3174 1.2009 -0.0603 -0.0841 -0.0041 711  HIS   E N   
14320 C  CA  . HIS   E 407 ? 1.2883 1.3358 1.2186 -0.0576 -0.0758 -0.0030 711  HIS   E CA  
14321 C  C   . HIS   E 407 ? 1.2684 1.3218 1.2076 -0.0585 -0.0712 -0.0035 711  HIS   E C   
14322 O  O   . HIS   E 407 ? 1.2414 1.3056 1.1947 -0.0611 -0.0719 -0.0037 711  HIS   E O   
14323 C  CB  . HIS   E 407 ? 1.3517 1.4007 1.2842 -0.0567 -0.0712 -0.0006 711  HIS   E CB  
14324 C  CG  . HIS   E 407 ? 1.4163 1.4640 1.3493 -0.0551 -0.0616 0.0008  711  HIS   E CG  
14325 N  ND1 . HIS   E 407 ? 1.3689 1.4268 1.3168 -0.0568 -0.0571 0.0012  711  HIS   E ND1 
14326 C  CD2 . HIS   E 407 ? 1.4469 1.4840 1.3676 -0.0518 -0.0556 0.0020  711  HIS   E CD2 
14327 C  CE1 . HIS   E 407 ? 1.3815 1.4360 1.3276 -0.0549 -0.0490 0.0024  711  HIS   E CE1 
14328 N  NE2 . HIS   E 407 ? 1.4528 1.4947 1.3825 -0.0519 -0.0474 0.0031  711  HIS   E NE2 
14329 N  N   . ILE   E 408 ? 1.1404 1.1861 1.0707 -0.0561 -0.0666 -0.0038 712  ILE   E N   
14330 C  CA  . ILE   E 408 ? 1.1528 1.2030 1.0905 -0.0563 -0.0616 -0.0044 712  ILE   E CA  
14331 C  C   . ILE   E 408 ? 1.0917 1.1386 1.0271 -0.0537 -0.0526 -0.0027 712  ILE   E C   
14332 O  O   . ILE   E 408 ? 1.0997 1.1353 1.0207 -0.0507 -0.0498 -0.0021 712  ILE   E O   
14333 C  CB  . ILE   E 408 ? 1.1597 1.2046 1.0907 -0.0558 -0.0641 -0.0065 712  ILE   E CB  
14334 C  CG1 . ILE   E 408 ? 1.0195 1.0717 0.9596 -0.0591 -0.0707 -0.0080 712  ILE   E CG1 
14335 C  CG2 . ILE   E 408 ? 1.0463 1.0912 0.9792 -0.0542 -0.0569 -0.0066 712  ILE   E CG2 
14336 C  CD1 . ILE   E 408 ? 1.0753 1.1256 1.0120 -0.0606 -0.0787 -0.0086 712  ILE   E CD1 
14337 N  N   . ARG   E 409 ? 1.0354 1.0917 0.9848 -0.0548 -0.0479 -0.0022 713  ARG   E N   
14338 C  CA  . ARG   E 409 ? 1.0302 1.0855 0.9814 -0.0528 -0.0389 -0.0009 713  ARG   E CA  
14339 C  C   . ARG   E 409 ? 1.0277 1.0881 0.9870 -0.0529 -0.0368 -0.0024 713  ARG   E C   
14340 O  O   . ARG   E 409 ? 1.0013 1.0709 0.9720 -0.0552 -0.0405 -0.0037 713  ARG   E O   
14341 C  CB  . ARG   E 409 ? 1.1160 1.1782 1.0782 -0.0539 -0.0356 0.0008  713  ARG   E CB  
14342 C  CG  . ARG   E 409 ? 1.1464 1.2084 1.1129 -0.0523 -0.0262 0.0022  713  ARG   E CG  
14343 C  CD  . ARG   E 409 ? 1.1535 1.2278 1.1388 -0.0546 -0.0246 0.0022  713  ARG   E CD  
14344 N  NE  . ARG   E 409 ? 1.3006 1.3747 1.2909 -0.0536 -0.0163 0.0041  713  ARG   E NE  
14345 C  CZ  . ARG   E 409 ? 1.3004 1.3798 1.3002 -0.0552 -0.0151 0.0053  713  ARG   E CZ  
14346 N  NH1 . ARG   E 409 ? 1.2387 1.3240 1.2435 -0.0575 -0.0217 0.0049  713  ARG   E NH1 
14347 N  NH2 . ARG   E 409 ? 1.3229 1.4017 1.3278 -0.0545 -0.0070 0.0070  713  ARG   E NH2 
14348 N  N   . THR   E 410 ? 0.9806 1.0347 0.9335 -0.0501 -0.0309 -0.0024 714  THR   E N   
14349 C  CA  . THR   E 410 ? 0.9947 1.0528 0.9540 -0.0498 -0.0294 -0.0040 714  THR   E CA  
14350 C  C   . THR   E 410 ? 1.0008 1.0633 0.9702 -0.0485 -0.0208 -0.0031 714  THR   E C   
14351 O  O   . THR   E 410 ? 0.9887 1.0451 0.9525 -0.0463 -0.0142 -0.0013 714  THR   E O   
14352 C  CB  . THR   E 410 ? 1.0211 1.0689 0.9659 -0.0476 -0.0307 -0.0053 714  THR   E CB  
14353 O  OG1 . THR   E 410 ? 1.0532 1.0963 0.9945 -0.0443 -0.0227 -0.0048 714  THR   E OG1 
14354 C  CG2 . THR   E 410 ? 0.9575 0.9947 0.8859 -0.0470 -0.0355 -0.0051 714  THR   E CG2 
14355 N  N   . VAL   E 411 ? 0.9795 1.0523 0.9639 -0.0498 -0.0210 -0.0043 715  VAL   E N   
14356 C  CA  . VAL   E 411 ? 0.9495 1.0281 0.9462 -0.0488 -0.0140 -0.0040 715  VAL   E CA  
14357 C  C   . VAL   E 411 ? 1.0075 1.0864 1.0056 -0.0470 -0.0125 -0.0058 715  VAL   E C   
14358 O  O   . VAL   E 411 ? 0.9441 1.0310 0.9525 -0.0481 -0.0161 -0.0076 715  VAL   E O   
14359 C  CB  . VAL   E 411 ? 0.9628 1.0533 0.9770 -0.0514 -0.0156 -0.0042 715  VAL   E CB  
14360 C  CG1 . VAL   E 411 ? 0.9631 1.0587 0.9902 -0.0504 -0.0083 -0.0038 715  VAL   E CG1 
14361 C  CG2 . VAL   E 411 ? 0.9770 1.0677 0.9899 -0.0533 -0.0185 -0.0026 715  VAL   E CG2 
14362 N  N   . PRO   E 412 ? 0.9628 1.0327 0.9501 -0.0438 -0.0073 -0.0054 716  PRO   E N   
14363 C  CA  . PRO   E 412 ? 0.9235 0.9933 0.9118 -0.0416 -0.0052 -0.0070 716  PRO   E CA  
14364 C  C   . PRO   E 412 ? 0.9803 1.0612 0.9874 -0.0416 -0.0023 -0.0080 716  PRO   E C   
14365 O  O   . PRO   E 412 ? 1.0164 1.1004 1.0323 -0.0410 0.0042  -0.0067 716  PRO   E O   
14366 C  CB  . PRO   E 412 ? 1.0083 1.0670 0.9837 -0.0379 0.0022  -0.0056 716  PRO   E CB  
14367 C  CG  . PRO   E 412 ? 1.1066 1.1613 1.0777 -0.0383 0.0051  -0.0030 716  PRO   E CG  
14368 C  CD  . PRO   E 412 ? 0.9771 1.0357 0.9496 -0.0418 -0.0032 -0.0033 716  PRO   E CD  
14369 N  N   . LEU   E 413 ? 0.9963 1.0824 1.0091 -0.0420 -0.0069 -0.0102 717  LEU   E N   
14370 C  CA  . LEU   E 413 ? 0.9119 1.0076 0.9413 -0.0413 -0.0048 -0.0116 717  LEU   E CA  
14371 C  C   . LEU   E 413 ? 1.0056 1.0984 1.0333 -0.0377 -0.0002 -0.0126 717  LEU   E C   
14372 O  O   . LEU   E 413 ? 1.0158 1.1157 1.0575 -0.0365 0.0034  -0.0134 717  LEU   E O   
14373 C  CB  . LEU   E 413 ? 0.8863 0.9895 0.9236 -0.0433 -0.0124 -0.0135 717  LEU   E CB  
14374 C  CG  . LEU   E 413 ? 0.9834 1.0900 1.0234 -0.0465 -0.0162 -0.0124 717  LEU   E CG  
14375 C  CD1 . LEU   E 413 ? 0.9039 1.0155 0.9476 -0.0484 -0.0239 -0.0139 717  LEU   E CD1 
14376 C  CD2 . LEU   E 413 ? 0.9431 1.0565 0.9973 -0.0469 -0.0115 -0.0115 717  LEU   E CD2 
14377 N  N   . TYR   E 414 ? 0.9974 1.0798 1.0086 -0.0359 -0.0005 -0.0127 718  TYR   E N   
14378 C  CA  . TYR   E 414 ? 1.0308 1.1094 1.0383 -0.0324 0.0029  -0.0139 718  TYR   E CA  
14379 C  C   . TYR   E 414 ? 1.0347 1.1210 1.0528 -0.0321 -0.0009 -0.0165 718  TYR   E C   
14380 O  O   . TYR   E 414 ? 1.1125 1.1991 1.1335 -0.0289 0.0027  -0.0176 718  TYR   E O   
14381 C  CB  . TYR   E 414 ? 1.0408 1.1184 1.0520 -0.0295 0.0128  -0.0124 718  TYR   E CB  
14382 C  CG  . TYR   E 414 ? 1.0371 1.1059 1.0365 -0.0293 0.0170  -0.0097 718  TYR   E CG  
14383 C  CD1 . TYR   E 414 ? 1.1088 1.1645 1.0877 -0.0275 0.0164  -0.0093 718  TYR   E CD1 
14384 C  CD2 . TYR   E 414 ? 1.0593 1.1322 1.0674 -0.0307 0.0210  -0.0077 718  TYR   E CD2 
14385 C  CE1 . TYR   E 414 ? 1.0649 1.1117 1.0317 -0.0268 0.0197  -0.0069 718  TYR   E CE1 
14386 C  CE2 . TYR   E 414 ? 1.1110 1.1749 1.1071 -0.0302 0.0248  -0.0052 718  TYR   E CE2 
14387 C  CZ  . TYR   E 414 ? 1.1301 1.1808 1.1052 -0.0281 0.0241  -0.0048 718  TYR   E CZ  
14388 O  OH  . TYR   E 414 ? 1.2518 1.2924 1.2132 -0.0270 0.0274  -0.0024 718  TYR   E OH  
14389 N  N   . GLU   E 415 ? 0.9477 1.0400 0.9714 -0.0349 -0.0081 -0.0175 719  GLU   E N   
14390 C  CA  . GLU   E 415 ? 0.9384 1.0360 0.9689 -0.0346 -0.0126 -0.0199 719  GLU   E CA  
14391 C  C   . GLU   E 415 ? 0.9556 1.0544 0.9839 -0.0379 -0.0204 -0.0201 719  GLU   E C   
14392 O  O   . GLU   E 415 ? 0.9319 1.0277 0.9539 -0.0403 -0.0221 -0.0186 719  GLU   E O   
14393 C  CB  . GLU   E 415 ? 0.8975 1.0054 0.9465 -0.0333 -0.0102 -0.0209 719  GLU   E CB  
14394 C  CG  . GLU   E 415 ? 0.9984 1.1144 1.0593 -0.0362 -0.0120 -0.0204 719  GLU   E CG  
14395 C  CD  . GLU   E 415 ? 1.0252 1.1508 1.1047 -0.0349 -0.0094 -0.0215 719  GLU   E CD  
14396 O  OE1 . GLU   E 415 ? 1.0124 1.1378 1.0957 -0.0323 -0.0031 -0.0215 719  GLU   E OE1 
14397 O  OE2 . GLU   E 415 ? 1.0362 1.1695 1.1266 -0.0365 -0.0138 -0.0225 719  GLU   E OE2 
14398 N  N   . SER   E 416 ? 0.9309 1.0338 0.9641 -0.0379 -0.0251 -0.0220 720  SER   E N   
14399 C  CA  . SER   E 416 ? 0.9341 1.0353 0.9614 -0.0406 -0.0317 -0.0220 720  SER   E CA  
14400 C  C   . SER   E 416 ? 1.0144 1.1239 1.0523 -0.0431 -0.0353 -0.0217 720  SER   E C   
14401 O  O   . SER   E 416 ? 0.9973 1.1133 1.0453 -0.0423 -0.0371 -0.0232 720  SER   E O   
14402 C  CB  . SER   E 416 ? 0.9121 1.0102 0.9348 -0.0391 -0.0347 -0.0239 720  SER   E CB  
14403 O  OG  . SER   E 416 ? 0.9532 1.0439 0.9670 -0.0363 -0.0311 -0.0243 720  SER   E OG  
14404 N  N   . PRO   E 417 ? 0.9671 1.0763 1.0027 -0.0460 -0.0367 -0.0200 721  PRO   E N   
14405 C  CA  . PRO   E 417 ? 0.9068 1.0229 0.9508 -0.0483 -0.0407 -0.0198 721  PRO   E CA  
14406 C  C   . PRO   E 417 ? 0.8727 0.9885 0.9143 -0.0490 -0.0461 -0.0208 721  PRO   E C   
14407 O  O   . PRO   E 417 ? 0.9622 1.0713 0.9932 -0.0496 -0.0481 -0.0208 721  PRO   E O   
14408 C  CB  . PRO   E 417 ? 0.9031 1.0168 0.9418 -0.0508 -0.0410 -0.0177 721  PRO   E CB  
14409 C  CG  . PRO   E 417 ? 0.8993 1.0031 0.9238 -0.0501 -0.0394 -0.0172 721  PRO   E CG  
14410 C  CD  . PRO   E 417 ? 0.9279 1.0301 0.9529 -0.0468 -0.0347 -0.0183 721  PRO   E CD  
14411 N  N   . ARG   E 418 ? 0.9079 1.0305 0.9593 -0.0487 -0.0486 -0.0217 722  ARG   E N   
14412 C  CA  . ARG   E 418 ? 0.9139 1.0360 0.9632 -0.0491 -0.0532 -0.0225 722  ARG   E CA  
14413 C  C   . ARG   E 418 ? 0.8451 0.9717 0.8989 -0.0514 -0.0567 -0.0215 722  ARG   E C   
14414 O  O   . ARG   E 418 ? 0.9495 1.0732 0.9975 -0.0535 -0.0596 -0.0206 722  ARG   E O   
14415 C  CB  . ARG   E 418 ? 0.9900 1.1142 1.0443 -0.0459 -0.0534 -0.0246 722  ARG   E CB  
14416 C  CG  . ARG   E 418 ? 0.9361 1.0558 0.9860 -0.0433 -0.0500 -0.0256 722  ARG   E CG  
14417 C  CD  . ARG   E 418 ? 0.9305 1.0416 0.9671 -0.0441 -0.0511 -0.0252 722  ARG   E CD  
14418 N  NE  . ARG   E 418 ? 1.0132 1.1230 1.0476 -0.0444 -0.0552 -0.0259 722  ARG   E NE  
14419 C  CZ  . ARG   E 418 ? 1.0411 1.1444 1.0659 -0.0462 -0.0574 -0.0254 722  ARG   E CZ  
14420 N  NH1 . ARG   E 418 ? 1.0013 1.0987 1.0175 -0.0478 -0.0567 -0.0245 722  ARG   E NH1 
14421 N  NH2 . ARG   E 418 ? 0.9476 1.0497 0.9712 -0.0462 -0.0603 -0.0258 722  ARG   E NH2 
14422 N  N   . LYS   E 419 ? 0.8639 0.9972 0.9281 -0.0511 -0.0565 -0.0216 723  LYS   E N   
14423 C  CA  . LYS   E 419 ? 0.9124 1.0497 0.9804 -0.0530 -0.0595 -0.0207 723  LYS   E CA  
14424 C  C   . LYS   E 419 ? 0.9178 1.0587 0.9914 -0.0543 -0.0575 -0.0195 723  LYS   E C   
14425 O  O   . LYS   E 419 ? 0.8818 1.0231 0.9583 -0.0534 -0.0535 -0.0196 723  LYS   E O   
14426 C  CB  . LYS   E 419 ? 0.8714 1.0126 0.9457 -0.0512 -0.0623 -0.0221 723  LYS   E CB  
14427 C  CG  . LYS   E 419 ? 0.9137 1.0506 0.9818 -0.0497 -0.0641 -0.0231 723  LYS   E CG  
14428 C  CD  . LYS   E 419 ? 0.9541 1.0872 1.0147 -0.0524 -0.0663 -0.0215 723  LYS   E CD  
14429 C  CE  . LYS   E 419 ? 0.9939 1.1211 1.0471 -0.0514 -0.0671 -0.0222 723  LYS   E CE  
14430 N  NZ  . LYS   E 419 ? 1.1726 1.3008 1.2275 -0.0501 -0.0695 -0.0225 723  LYS   E NZ  
14431 N  N   . ILE   E 420 ? 0.9236 1.0669 0.9987 -0.0563 -0.0600 -0.0183 724  ILE   E N   
14432 C  CA  . ILE   E 420 ? 0.9822 1.1280 1.0613 -0.0577 -0.0584 -0.0169 724  ILE   E CA  
14433 C  C   . ILE   E 420 ? 0.9522 1.1022 1.0358 -0.0589 -0.0617 -0.0163 724  ILE   E C   
14434 O  O   . ILE   E 420 ? 0.9333 1.0822 1.0128 -0.0599 -0.0649 -0.0157 724  ILE   E O   
14435 C  CB  . ILE   E 420 ? 0.9644 1.1047 1.0343 -0.0593 -0.0567 -0.0152 724  ILE   E CB  
14436 C  CG1 . ILE   E 420 ? 0.9126 1.0550 0.9856 -0.0607 -0.0557 -0.0136 724  ILE   E CG1 
14437 C  CG2 . ILE   E 420 ? 0.9880 1.1246 1.0496 -0.0609 -0.0604 -0.0146 724  ILE   E CG2 
14438 C  CD1 . ILE   E 420 ? 0.9322 1.0686 0.9966 -0.0612 -0.0528 -0.0122 724  ILE   E CD1 
14439 N  N   . CYS   E 421 ? 1.0011 1.1557 1.0932 -0.0588 -0.0608 -0.0163 725  CYS   E N   
14440 C  CA  . CYS   E 421 ? 1.0756 1.2336 1.1714 -0.0599 -0.0635 -0.0154 725  CYS   E CA  
14441 C  C   . CYS   E 421 ? 1.0126 1.1726 1.1138 -0.0608 -0.0610 -0.0145 725  CYS   E C   
14442 O  O   . CYS   E 421 ? 0.9821 1.1425 1.0875 -0.0601 -0.0573 -0.0150 725  CYS   E O   
14443 C  CB  . CYS   E 421 ? 1.0045 1.1660 1.1061 -0.0581 -0.0667 -0.0170 725  CYS   E CB  
14444 S  SG  . CYS   E 421 ? 1.1393 1.3049 1.2523 -0.0556 -0.0654 -0.0195 725  CYS   E SG  
14445 N  N   . TYR   E 422 ? 1.0627 1.2240 1.1639 -0.0623 -0.0628 -0.0131 726  TYR   E N   
14446 C  CA  . TYR   E 422 ? 1.0633 1.2256 1.1683 -0.0634 -0.0607 -0.0119 726  TYR   E CA  
14447 C  C   . TYR   E 422 ? 1.0081 1.1757 1.1235 -0.0627 -0.0624 -0.0129 726  TYR   E C   
14448 O  O   . TYR   E 422 ? 0.9785 1.1481 1.0953 -0.0618 -0.0662 -0.0138 726  TYR   E O   
14449 C  CB  . TYR   E 422 ? 1.0250 1.1848 1.1227 -0.0652 -0.0618 -0.0097 726  TYR   E CB  
14450 C  CG  . TYR   E 422 ? 1.0470 1.2070 1.1471 -0.0661 -0.0598 -0.0083 726  TYR   E CG  
14451 C  CD1 . TYR   E 422 ? 1.0539 1.2126 1.1566 -0.0660 -0.0549 -0.0080 726  TYR   E CD1 
14452 C  CD2 . TYR   E 422 ? 1.0560 1.2172 1.1559 -0.0671 -0.0624 -0.0070 726  TYR   E CD2 
14453 C  CE1 . TYR   E 422 ? 1.1382 1.2965 1.2430 -0.0669 -0.0526 -0.0065 726  TYR   E CE1 
14454 C  CE2 . TYR   E 422 ? 1.0397 1.2006 1.1413 -0.0679 -0.0606 -0.0057 726  TYR   E CE2 
14455 C  CZ  . TYR   E 422 ? 1.0830 1.2423 1.1870 -0.0678 -0.0557 -0.0054 726  TYR   E CZ  
14456 O  OH  . TYR   E 422 ? 1.0382 1.1964 1.1437 -0.0686 -0.0534 -0.0039 726  TYR   E OH  
14457 N  N   . GLN   E 423 ? 1.0267 1.1960 1.1495 -0.0630 -0.0594 -0.0129 727  GLN   E N   
14458 C  CA  . GLN   E 423 ? 1.0988 1.2727 1.2323 -0.0625 -0.0612 -0.0142 727  GLN   E CA  
14459 C  C   . GLN   E 423 ? 1.0846 1.2583 1.2199 -0.0643 -0.0594 -0.0124 727  GLN   E C   
14460 O  O   . GLN   E 423 ? 1.0680 1.2420 1.2092 -0.0648 -0.0554 -0.0122 727  GLN   E O   
14461 C  CB  . GLN   E 423 ? 1.0809 1.2577 1.2245 -0.0609 -0.0598 -0.0166 727  GLN   E CB  
14462 C  CG  . GLN   E 423 ? 1.0045 1.1858 1.1598 -0.0604 -0.0623 -0.0183 727  GLN   E CG  
14463 C  CD  . GLN   E 423 ? 1.0620 1.2465 1.2256 -0.0579 -0.0643 -0.0215 727  GLN   E CD  
14464 O  OE1 . GLN   E 423 ? 1.0920 1.2792 1.2664 -0.0577 -0.0622 -0.0228 727  GLN   E OE1 
14465 N  NE2 . GLN   E 423 ? 1.0058 1.1896 1.1645 -0.0559 -0.0684 -0.0227 727  GLN   E NE2 
14466 N  N   . GLU   E 424 ? 1.0797 1.2528 1.2102 -0.0651 -0.0622 -0.0110 728  GLU   E N   
14467 C  CA  . GLU   E 424 ? 1.1058 1.2777 1.2359 -0.0666 -0.0607 -0.0090 728  GLU   E CA  
14468 C  C   . GLU   E 424 ? 1.0995 1.2743 1.2410 -0.0667 -0.0596 -0.0098 728  GLU   E C   
14469 O  O   . GLU   E 424 ? 1.0491 1.2223 1.1923 -0.0680 -0.0556 -0.0084 728  GLU   E O   
14470 C  CB  . GLU   E 424 ? 1.1161 1.2879 1.2408 -0.0669 -0.0647 -0.0078 728  GLU   E CB  
14471 C  CG  . GLU   E 424 ? 1.1281 1.2986 1.2517 -0.0681 -0.0639 -0.0058 728  GLU   E CG  
14472 C  CD  . GLU   E 424 ? 1.2861 1.4572 1.4056 -0.0681 -0.0681 -0.0049 728  GLU   E CD  
14473 O  OE1 . GLU   E 424 ? 1.3112 1.4810 1.4237 -0.0681 -0.0697 -0.0044 728  GLU   E OE1 
14474 O  OE2 . GLU   E 424 ? 1.3641 1.5370 1.4879 -0.0679 -0.0698 -0.0048 728  GLU   E OE2 
14475 N  N   . VAL   E 425 ? 1.0995 1.2782 1.2489 -0.0654 -0.0631 -0.0122 729  VAL   E N   
14476 C  CA  . VAL   E 425 ? 1.0589 1.2404 1.2200 -0.0656 -0.0630 -0.0134 729  VAL   E CA  
14477 C  C   . VAL   E 425 ? 1.0877 1.2694 1.2559 -0.0663 -0.0575 -0.0136 729  VAL   E C   
14478 O  O   . VAL   E 425 ? 1.1814 1.3637 1.3572 -0.0676 -0.0550 -0.0131 729  VAL   E O   
14479 C  CB  . VAL   E 425 ? 1.0925 1.2773 1.2599 -0.0635 -0.0683 -0.0163 729  VAL   E CB  
14480 C  CG1 . VAL   E 425 ? 1.1169 1.3051 1.2985 -0.0631 -0.0677 -0.0187 729  VAL   E CG1 
14481 C  CG2 . VAL   E 425 ? 1.1115 1.2963 1.2765 -0.0631 -0.0725 -0.0158 729  VAL   E CG2 
14482 N  N   . SER   E 426 ? 1.0410 1.2221 1.2069 -0.0655 -0.0552 -0.0141 730  SER   E N   
14483 C  CA  . SER   E 426 ? 1.0273 1.2088 1.2003 -0.0657 -0.0496 -0.0143 730  SER   E CA  
14484 C  C   . SER   E 426 ? 1.1066 1.2827 1.2698 -0.0666 -0.0439 -0.0115 730  SER   E C   
14485 O  O   . SER   E 426 ? 1.1471 1.3226 1.3141 -0.0665 -0.0384 -0.0113 730  SER   E O   
14486 C  CB  . SER   E 426 ? 1.1358 1.3202 1.3142 -0.0637 -0.0508 -0.0171 730  SER   E CB  
14487 O  OG  . SER   E 426 ? 1.1819 1.3706 1.3688 -0.0623 -0.0565 -0.0199 730  SER   E OG  
14488 N  N   . GLN   E 427 ? 1.1376 1.3097 1.2882 -0.0672 -0.0452 -0.0095 731  GLN   E N   
14489 C  CA  . GLN   E 427 ? 1.1634 1.3293 1.3025 -0.0677 -0.0409 -0.0071 731  GLN   E CA  
14490 C  C   . GLN   E 427 ? 1.1455 1.3097 1.2825 -0.0664 -0.0373 -0.0077 731  GLN   E C   
14491 O  O   . GLN   E 427 ? 1.1210 1.2824 1.2585 -0.0663 -0.0310 -0.0066 731  GLN   E O   
14492 C  CB  . GLN   E 427 ? 1.1736 1.3366 1.3137 -0.0690 -0.0362 -0.0048 731  GLN   E CB  
14493 C  CG  . GLN   E 427 ? 1.1847 1.3464 1.3201 -0.0700 -0.0393 -0.0033 731  GLN   E CG  
14494 C  CD  . GLN   E 427 ? 1.3002 1.4590 1.4378 -0.0711 -0.0344 -0.0013 731  GLN   E CD  
14495 O  OE1 . GLN   E 427 ? 1.3220 1.4745 1.4488 -0.0712 -0.0318 0.0012  731  GLN   E OE1 
14496 N  NE2 . GLN   E 427 ? 1.3049 1.4678 1.4564 -0.0719 -0.0332 -0.0023 731  GLN   E NE2 
14497 N  N   . CYS   E 428 ? 1.1267 1.2919 1.2606 -0.0652 -0.0411 -0.0094 732  CYS   E N   
14498 C  CA  . CYS   E 428 ? 1.1173 1.2811 1.2495 -0.0637 -0.0384 -0.0103 732  CYS   E CA  
14499 C  C   . CYS   E 428 ? 1.0808 1.2441 1.2058 -0.0628 -0.0433 -0.0115 732  CYS   E C   
14500 O  O   . CYS   E 428 ? 1.0325 1.1978 1.1568 -0.0632 -0.0485 -0.0119 732  CYS   E O   
14501 C  CB  . CYS   E 428 ? 1.1319 1.3010 1.2787 -0.0628 -0.0364 -0.0124 732  CYS   E CB  
14502 S  SG  . CYS   E 428 ? 1.1971 1.3728 1.3533 -0.0620 -0.0439 -0.0153 732  CYS   E SG  
14503 N  N   . PHE   E 429 ? 1.0470 1.2071 1.1665 -0.0616 -0.0411 -0.0119 733  PHE   E N   
14504 C  CA  . PHE   E 429 ? 1.0015 1.1600 1.1138 -0.0607 -0.0448 -0.0130 733  PHE   E CA  
14505 C  C   . PHE   E 429 ? 1.0099 1.1715 1.1292 -0.0585 -0.0447 -0.0155 733  PHE   E C   
14506 O  O   . PHE   E 429 ? 1.0196 1.1820 1.1450 -0.0576 -0.0402 -0.0160 733  PHE   E O   
14507 C  CB  . PHE   E 429 ? 0.9987 1.1499 1.0972 -0.0608 -0.0430 -0.0116 733  PHE   E CB  
14508 C  CG  . PHE   E 429 ? 0.9388 1.0867 1.0287 -0.0626 -0.0452 -0.0097 733  PHE   E CG  
14509 C  CD1 . PHE   E 429 ? 0.9209 1.0692 1.0068 -0.0633 -0.0506 -0.0099 733  PHE   E CD1 
14510 C  CD2 . PHE   E 429 ? 1.0105 1.1545 1.0962 -0.0632 -0.0416 -0.0076 733  PHE   E CD2 
14511 C  CE1 . PHE   E 429 ? 0.9893 1.1350 1.0683 -0.0648 -0.0529 -0.0083 733  PHE   E CE1 
14512 C  CE2 . PHE   E 429 ? 1.0326 1.1733 1.1101 -0.0645 -0.0442 -0.0060 733  PHE   E CE2 
14513 C  CZ  . PHE   E 429 ? 1.0653 1.2073 1.1400 -0.0653 -0.0500 -0.0064 733  PHE   E CZ  
14514 N  N   . GLY   E 430 ? 0.9905 1.1533 1.1086 -0.0576 -0.0496 -0.0170 734  GLY   E N   
14515 C  CA  . GLY   E 430 ? 0.9975 1.1616 1.1190 -0.0552 -0.0501 -0.0194 734  GLY   E CA  
14516 C  C   . GLY   E 430 ? 0.9874 1.1458 1.0970 -0.0546 -0.0498 -0.0192 734  GLY   E C   
14517 O  O   . GLY   E 430 ? 0.9296 1.0848 1.0303 -0.0557 -0.0527 -0.0182 734  GLY   E O   
14518 N  N   . VAL   E 431 ? 0.9855 1.1424 1.0956 -0.0527 -0.0464 -0.0201 735  VAL   E N   
14519 C  CA  . VAL   E 431 ? 0.9143 1.0651 1.0131 -0.0519 -0.0458 -0.0201 735  VAL   E CA  
14520 C  C   . VAL   E 431 ? 0.9228 1.0750 1.0260 -0.0489 -0.0454 -0.0225 735  VAL   E C   
14521 O  O   . VAL   E 431 ? 0.8903 1.0456 1.0025 -0.0475 -0.0417 -0.0233 735  VAL   E O   
14522 C  CB  . VAL   E 431 ? 0.9489 1.0939 1.0393 -0.0526 -0.0410 -0.0182 735  VAL   E CB  
14523 C  CG1 . VAL   E 431 ? 0.9514 1.0905 1.0332 -0.0507 -0.0389 -0.0188 735  VAL   E CG1 
14524 C  CG2 . VAL   E 431 ? 0.9478 1.0894 1.0293 -0.0552 -0.0434 -0.0162 735  VAL   E CG2 
14525 N  N   . LEU   E 432 ? 0.9090 1.0590 1.0066 -0.0478 -0.0490 -0.0236 736  LEU   E N   
14526 C  CA  . LEU   E 432 ? 0.9544 1.1035 1.0524 -0.0447 -0.0487 -0.0257 736  LEU   E CA  
14527 C  C   . LEU   E 432 ? 0.9322 1.0747 1.0204 -0.0442 -0.0446 -0.0249 736  LEU   E C   
14528 O  O   . LEU   E 432 ? 0.9017 1.0383 0.9784 -0.0459 -0.0454 -0.0235 736  LEU   E O   
14529 C  CB  . LEU   E 432 ? 0.9188 1.0665 1.0126 -0.0437 -0.0537 -0.0268 736  LEU   E CB  
14530 C  CG  . LEU   E 432 ? 0.8945 1.0473 0.9959 -0.0433 -0.0580 -0.0278 736  LEU   E CG  
14531 C  CD1 . LEU   E 432 ? 0.8276 0.9774 0.9233 -0.0414 -0.0618 -0.0289 736  LEU   E CD1 
14532 C  CD2 . LEU   E 432 ? 0.9278 1.0868 1.0429 -0.0413 -0.0570 -0.0296 736  LEU   E CD2 
14533 N  N   . SER   E 433 ? 0.9277 1.0710 1.0206 -0.0418 -0.0405 -0.0259 737  SER   E N   
14534 C  CA  . SER   E 433 ? 0.9600 1.0966 1.0433 -0.0408 -0.0362 -0.0252 737  SER   E CA  
14535 C  C   . SER   E 433 ? 1.0042 1.1398 1.0879 -0.0372 -0.0357 -0.0274 737  SER   E C   
14536 O  O   . SER   E 433 ? 1.0022 1.1434 1.0961 -0.0352 -0.0377 -0.0294 737  SER   E O   
14537 C  CB  . SER   E 433 ? 0.9516 1.0882 1.0381 -0.0410 -0.0297 -0.0236 737  SER   E CB  
14538 O  OG  . SER   E 433 ? 0.9397 1.0817 1.0389 -0.0386 -0.0261 -0.0250 737  SER   E OG  
14539 N  N   . SER   E 434 ? 0.9933 1.1213 1.0653 -0.0361 -0.0334 -0.0270 738  SER   E N   
14540 C  CA  . SER   E 434 ? 0.9878 1.1138 1.0589 -0.0325 -0.0318 -0.0287 738  SER   E CA  
14541 C  C   . SER   E 434 ? 1.0126 1.1343 1.0796 -0.0310 -0.0249 -0.0277 738  SER   E C   
14542 O  O   . SER   E 434 ? 1.0287 1.1454 1.0875 -0.0328 -0.0226 -0.0256 738  SER   E O   
14543 C  CB  . SER   E 434 ? 1.0010 1.1206 1.0604 -0.0321 -0.0359 -0.0295 738  SER   E CB  
14544 O  OG  . SER   E 434 ? 1.1403 1.2547 1.1937 -0.0289 -0.0331 -0.0304 738  SER   E OG  
14545 N  N   . ARG   E 435 ? 1.0096 1.1329 1.0823 -0.0274 -0.0218 -0.0292 739  ARG   E N   
14546 C  CA  . ARG   E 435 ? 1.0248 1.1442 1.0945 -0.0252 -0.0145 -0.0283 739  ARG   E CA  
14547 C  C   . ARG   E 435 ? 1.1088 1.2256 1.1760 -0.0211 -0.0140 -0.0303 739  ARG   E C   
14548 O  O   . ARG   E 435 ? 1.1686 1.2918 1.2470 -0.0191 -0.0162 -0.0325 739  ARG   E O   
14549 C  CB  . ARG   E 435 ? 1.0222 1.1489 1.1071 -0.0251 -0.0091 -0.0277 739  ARG   E CB  
14550 C  CG  . ARG   E 435 ? 1.1219 1.2478 1.2101 -0.0213 -0.0016 -0.0278 739  ARG   E CG  
14551 C  CD  . ARG   E 435 ? 1.1517 1.2844 1.2554 -0.0216 0.0046  -0.0268 739  ARG   E CD  
14552 N  NE  . ARG   E 435 ? 1.0817 1.2246 1.2050 -0.0198 0.0041  -0.0291 739  ARG   E NE  
14553 C  CZ  . ARG   E 435 ? 1.0816 1.2330 1.2183 -0.0216 -0.0008 -0.0304 739  ARG   E CZ  
14554 N  NH1 . ARG   E 435 ? 1.0778 1.2289 1.2102 -0.0251 -0.0058 -0.0296 739  ARG   E NH1 
14555 N  NH2 . ARG   E 435 ? 1.1226 1.2827 1.2774 -0.0197 -0.0009 -0.0327 739  ARG   E NH2 
14556 N  N   . ILE   E 436 ? 1.1054 1.2126 1.1579 -0.0197 -0.0118 -0.0298 740  ILE   E N   
14557 C  CA  . ILE   E 436 ? 1.1498 1.2542 1.1997 -0.0156 -0.0108 -0.0316 740  ILE   E CA  
14558 C  C   . ILE   E 436 ? 1.2061 1.3143 1.2662 -0.0123 -0.0035 -0.0317 740  ILE   E C   
14559 O  O   . ILE   E 436 ? 1.2142 1.3205 1.2732 -0.0126 0.0027  -0.0296 740  ILE   E O   
14560 C  CB  . ILE   E 436 ? 1.1673 1.2592 1.1972 -0.0151 -0.0113 -0.0312 740  ILE   E CB  
14561 C  CG1 . ILE   E 436 ? 1.2049 1.2936 1.2265 -0.0187 -0.0185 -0.0310 740  ILE   E CG1 
14562 C  CG2 . ILE   E 436 ? 1.1418 1.2305 1.1689 -0.0105 -0.0103 -0.0331 740  ILE   E CG2 
14563 C  CD1 . ILE   E 436 ? 1.2580 1.3529 1.2879 -0.0189 -0.0242 -0.0328 740  ILE   E CD1 
14564 N  N   . GLU   E 437 ? 1.2483 1.3619 1.3187 -0.0089 -0.0040 -0.0340 741  GLU   E N   
14565 C  CA  . GLU   E 437 ? 1.2878 1.4046 1.3679 -0.0050 0.0029  -0.0345 741  GLU   E CA  
14566 C  C   . GLU   E 437 ? 1.3174 1.4294 1.3907 -0.0005 0.0026  -0.0364 741  GLU   E C   
14567 O  O   . GLU   E 437 ? 1.3025 1.4091 1.3649 -0.0005 -0.0031 -0.0374 741  GLU   E O   
14568 C  CB  . GLU   E 437 ? 1.3313 1.4611 1.4344 -0.0049 0.0027  -0.0358 741  GLU   E CB  
14569 C  CG  . GLU   E 437 ? 1.3682 1.5023 1.4802 -0.0078 0.0077  -0.0335 741  GLU   E CG  
14570 C  CD  . GLU   E 437 ? 1.4209 1.5675 1.5557 -0.0085 0.0063  -0.0350 741  GLU   E CD  
14571 O  OE1 . GLU   E 437 ? 1.5045 1.6571 1.6519 -0.0051 0.0061  -0.0374 741  GLU   E OE1 
14572 O  OE2 . GLU   E 437 ? 1.4686 1.6188 1.6087 -0.0123 0.0051  -0.0338 741  GLU   E OE2 
14573 N  N   . VAL   E 438 ? 1.4153 1.5288 1.4951 0.0034  0.0092  -0.0366 742  VAL   E N   
14574 C  CA  . VAL   E 438 ? 1.4966 1.6053 1.5703 0.0083  0.0104  -0.0382 742  VAL   E CA  
14575 C  C   . VAL   E 438 ? 1.6049 1.7242 1.6987 0.0119  0.0112  -0.0406 742  VAL   E C   
14576 O  O   . VAL   E 438 ? 1.6531 1.7797 1.7622 0.0122  0.0169  -0.0400 742  VAL   E O   
14577 C  CB  . VAL   E 438 ? 1.4693 1.5681 1.5296 0.0106  0.0181  -0.0363 742  VAL   E CB  
14578 C  CG1 . VAL   E 438 ? 1.5821 1.6799 1.6441 0.0164  0.0218  -0.0379 742  VAL   E CG1 
14579 C  CG2 . VAL   E 438 ? 1.4185 1.5046 1.4560 0.0085  0.0150  -0.0352 742  VAL   E CG2 
14580 N  N   . GLN   E 439 ? 1.6377 1.7576 1.7317 0.0146  0.0053  -0.0434 743  GLN   E N   
14581 C  CA  . GLN   E 439 ? 1.7267 1.8551 1.8375 0.0190  0.0053  -0.0461 743  GLN   E CA  
14582 C  C   . GLN   E 439 ? 1.8520 1.9802 1.9670 0.0228  0.0145  -0.0454 743  GLN   E C   
14583 O  O   . GLN   E 439 ? 1.8531 1.9719 1.9534 0.0258  0.0175  -0.0451 743  GLN   E O   
14584 C  CB  . GLN   E 439 ? 1.7583 1.8830 1.8618 0.0220  -0.0017 -0.0488 743  GLN   E CB  
14585 C  CG  . GLN   E 439 ? 1.8562 1.9850 1.9698 0.0280  -0.0006 -0.0515 743  GLN   E CG  
14586 C  CD  . GLN   E 439 ? 1.8810 2.0226 2.0170 0.0289  -0.0046 -0.0540 743  GLN   E CD  
14587 O  OE1 . GLN   E 439 ? 1.8295 1.9774 1.9748 0.0249  -0.0066 -0.0535 743  GLN   E OE1 
14588 N  NE2 . GLN   E 439 ? 1.8527 1.9979 1.9972 0.0343  -0.0062 -0.0570 743  GLN   E NE2 
14589 N  N   . ASP   E 440 ? 2.2577 2.3961 2.3929 0.0229  0.0195  -0.0452 744  ASP   E N   
14590 C  CA  . ASP   E 440 ? 2.2699 2.4085 2.4104 0.0262  0.0296  -0.0440 744  ASP   E CA  
14591 C  C   . ASP   E 440 ? 2.2857 2.4311 2.4407 0.0318  0.0295  -0.0471 744  ASP   E C   
14592 O  O   . ASP   E 440 ? 2.2824 2.4289 2.4373 0.0337  0.0216  -0.0501 744  ASP   E O   
14593 C  CB  . ASP   E 440 ? 2.2284 2.3732 2.3822 0.0230  0.0361  -0.0416 744  ASP   E CB  
14594 C  CG  . ASP   E 440 ? 2.2057 2.3644 2.3840 0.0212  0.0321  -0.0435 744  ASP   E CG  
14595 O  OD1 . ASP   E 440 ? 2.1978 2.3639 2.3903 0.0246  0.0290  -0.0467 744  ASP   E OD1 
14596 O  OD2 . ASP   E 440 ? 2.2019 2.3637 2.3851 0.0164  0.0318  -0.0420 744  ASP   E OD2 
14597 N  N   . THR   E 441 ? 2.0981 2.2479 2.2657 0.0346  0.0384  -0.0464 745  THR   E N   
14598 C  CA  . THR   E 441 ? 2.0316 2.1874 2.2126 0.0403  0.0393  -0.0492 745  THR   E CA  
14599 C  C   . THR   E 441 ? 1.9711 2.1422 2.1804 0.0401  0.0358  -0.0518 745  THR   E C   
14600 O  O   . THR   E 441 ? 1.9259 2.1021 2.1446 0.0441  0.0308  -0.0553 745  THR   E O   
14601 C  CB  . THR   E 441 ? 1.9947 2.1468 2.1743 0.0441  0.0511  -0.0471 745  THR   E CB  
14602 O  OG1 . THR   E 441 ? 1.9848 2.1458 2.1835 0.0493  0.0531  -0.0496 745  THR   E OG1 
14603 C  CG2 . THR   E 441 ? 1.9559 2.1090 2.1403 0.0406  0.0601  -0.0433 745  THR   E CG2 
14604 N  N   . SER   E 442 ? 1.9629 2.1409 2.1854 0.0355  0.0377  -0.0503 746  SER   E N   
14605 C  CA  . SER   E 442 ? 1.9313 2.1233 2.1807 0.0348  0.0338  -0.0530 746  SER   E CA  
14606 C  C   . SER   E 442 ? 1.8340 2.0278 2.0821 0.0336  0.0210  -0.0560 746  SER   E C   
14607 O  O   . SER   E 442 ? 1.7800 1.9826 2.0442 0.0309  0.0165  -0.0573 746  SER   E O   
14608 C  CB  . SER   E 442 ? 1.8907 2.0884 2.1535 0.0298  0.0395  -0.0504 746  SER   E CB  
14609 O  OG  . SER   E 442 ? 1.8675 2.0655 2.1366 0.0313  0.0518  -0.0478 746  SER   E OG  
14610 N  N   . GLY   E 443 ? 1.8452 2.0304 2.0742 0.0358  0.0153  -0.0572 747  GLY   E N   
14611 C  CA  . GLY   E 443 ? 1.7922 1.9772 2.0168 0.0346  0.0040  -0.0594 747  GLY   E CA  
14612 C  C   . GLY   E 443 ? 1.7937 1.9777 2.0132 0.0283  0.0012  -0.0575 747  GLY   E C   
14613 O  O   . GLY   E 443 ? 1.7016 1.8884 1.9238 0.0271  -0.0076 -0.0595 747  GLY   E O   
14614 N  N   . GLY   E 444 ? 1.8088 1.9883 2.0203 0.0246  0.0082  -0.0536 748  GLY   E N   
14615 C  CA  . GLY   E 444 ? 1.7327 1.9116 1.9403 0.0188  0.0059  -0.0517 748  GLY   E CA  
14616 C  C   . GLY   E 444 ? 1.7502 1.9168 1.9327 0.0161  0.0072  -0.0486 748  GLY   E C   
14617 O  O   . GLY   E 444 ? 1.7869 1.9448 1.9526 0.0185  0.0059  -0.0489 748  GLY   E O   
14618 N  N   . THR   E 445 ? 1.7223 1.8881 1.9024 0.0112  0.0094  -0.0458 749  THR   E N   
14619 C  CA  . THR   E 445 ? 1.6335 1.7881 1.7912 0.0085  0.0105  -0.0430 749  THR   E CA  
14620 C  C   . THR   E 445 ? 1.5697 1.7236 1.7286 0.0057  0.0188  -0.0395 749  THR   E C   
14621 O  O   . THR   E 445 ? 1.5769 1.7377 1.7487 0.0025  0.0189  -0.0389 749  THR   E O   
14622 C  CB  . THR   E 445 ? 1.5430 1.6958 1.6923 0.0050  0.0016  -0.0433 749  THR   E CB  
14623 O  OG1 . THR   E 445 ? 1.5624 1.7253 1.7293 0.0028  -0.0023 -0.0445 749  THR   E OG1 
14624 C  CG2 . THR   E 445 ? 1.5039 1.6519 1.6429 0.0078  -0.0052 -0.0457 749  THR   E CG2 
14625 N  N   . THR   E 446 ? 1.5807 1.7254 1.7253 0.0072  0.0256  -0.0373 750  THR   E N   
14626 C  CA  . THR   E 446 ? 1.5318 1.6728 1.6729 0.0052  0.0338  -0.0338 750  THR   E CA  
14627 C  C   . THR   E 446 ? 1.4877 1.6195 1.6088 0.0015  0.0305  -0.0318 750  THR   E C   
14628 O  O   . THR   E 446 ? 1.4900 1.6145 1.5952 0.0017  0.0250  -0.0326 750  THR   E O   
14629 C  CB  . THR   E 446 ? 1.5658 1.7011 1.7016 0.0096  0.0434  -0.0325 750  THR   E CB  
14630 O  OG1 . THR   E 446 ? 1.5368 1.6629 1.6584 0.0081  0.0497  -0.0290 750  THR   E OG1 
14631 C  CG2 . THR   E 446 ? 1.6236 1.7515 1.7452 0.0135  0.0404  -0.0343 750  THR   E CG2 
14632 N  N   . ALA   E 447 ? 1.4909 1.6229 1.6134 -0.0020 0.0338  -0.0292 751  ALA   E N   
14633 C  CA  . ALA   E 447 ? 1.4758 1.5998 1.5810 -0.0056 0.0306  -0.0273 751  ALA   E CA  
14634 C  C   . ALA   E 447 ? 1.5027 1.6132 1.5863 -0.0036 0.0353  -0.0254 751  ALA   E C   
14635 O  O   . ALA   E 447 ? 1.5244 1.6317 1.6069 0.0002  0.0429  -0.0248 751  ALA   E O   
14636 C  CB  . ALA   E 447 ? 1.4279 1.5565 1.5417 -0.0096 0.0324  -0.0253 751  ALA   E CB  
14637 N  N   . LEU   E 448 ? 1.3796 1.4819 1.4458 -0.0062 0.0306  -0.0245 752  LEU   E N   
14638 C  CA  . LEU   E 448 ? 1.3672 1.4556 1.4113 -0.0045 0.0334  -0.0230 752  LEU   E CA  
14639 C  C   . LEU   E 448 ? 1.3524 1.4354 1.3899 -0.0058 0.0393  -0.0198 752  LEU   E C   
14640 O  O   . LEU   E 448 ? 1.3390 1.4136 1.3668 -0.0026 0.0469  -0.0181 752  LEU   E O   
14641 C  CB  . LEU   E 448 ? 1.3389 1.4204 1.3672 -0.0063 0.0245  -0.0241 752  LEU   E CB  
14642 C  CG  . LEU   E 448 ? 1.2739 1.3556 1.3007 -0.0046 0.0187  -0.0270 752  LEU   E CG  
14643 C  CD1 . LEU   E 448 ? 1.2289 1.3042 1.2488 0.0006  0.0235  -0.0277 752  LEU   E CD1 
14644 C  CD2 . LEU   E 448 ? 1.3360 1.4306 1.3827 -0.0051 0.0152  -0.0289 752  LEU   E CD2 
14645 N  N   . ARG   E 449 ? 1.3440 1.4312 1.3863 -0.0101 0.0361  -0.0188 753  ARG   E N   
14646 C  CA  . ARG   E 449 ? 1.2237 1.3060 1.2598 -0.0117 0.0407  -0.0158 753  ARG   E CA  
14647 C  C   . ARG   E 449 ? 1.1965 1.2897 1.2499 -0.0156 0.0391  -0.0153 753  ARG   E C   
14648 O  O   . ARG   E 449 ? 1.1864 1.2876 1.2491 -0.0179 0.0315  -0.0174 753  ARG   E O   
14649 C  CB  . ARG   E 449 ? 1.2288 1.2993 1.2427 -0.0130 0.0358  -0.0150 753  ARG   E CB  
14650 C  CG  . ARG   E 449 ? 1.2954 1.3709 1.3119 -0.0177 0.0262  -0.0159 753  ARG   E CG  
14651 C  CD  . ARG   E 449 ? 1.2889 1.3546 1.2863 -0.0187 0.0192  -0.0164 753  ARG   E CD  
14652 N  NE  . ARG   E 449 ? 1.2732 1.3363 1.2656 -0.0166 0.0160  -0.0187 753  ARG   E NE  
14653 C  CZ  . ARG   E 449 ? 1.3118 1.3639 1.2891 -0.0132 0.0186  -0.0189 753  ARG   E CZ  
14654 N  NH1 . ARG   E 449 ? 1.2843 1.3270 1.2497 -0.0111 0.0247  -0.0168 753  ARG   E NH1 
14655 N  NH2 . ARG   E 449 ? 1.3878 1.4377 1.3609 -0.0116 0.0150  -0.0210 753  ARG   E NH2 
14656 N  N   . PRO   E 450 ? 1.2207 1.3137 1.2781 -0.0162 0.0461  -0.0127 754  PRO   E N   
14657 C  CA  . PRO   E 450 ? 1.1692 1.2712 1.2412 -0.0202 0.0443  -0.0122 754  PRO   E CA  
14658 C  C   . PRO   E 450 ? 1.1069 1.2068 1.1692 -0.0237 0.0351  -0.0124 754  PRO   E C   
14659 O  O   . PRO   E 450 ? 1.1498 1.2394 1.1936 -0.0239 0.0342  -0.0110 754  PRO   E O   
14660 C  CB  . PRO   E 450 ? 1.2253 1.3232 1.2968 -0.0197 0.0542  -0.0088 754  PRO   E CB  
14661 C  CG  . PRO   E 450 ? 1.2057 1.2889 1.2535 -0.0168 0.0573  -0.0073 754  PRO   E CG  
14662 C  CD  . PRO   E 450 ? 1.2422 1.3238 1.2852 -0.0138 0.0546  -0.0098 754  PRO   E CD  
14663 N  N   . SER   E 451 ? 1.0642 1.1736 1.1386 -0.0262 0.0280  -0.0144 755  SER   E N   
14664 C  CA  . SER   E 451 ? 1.0701 1.1790 1.1376 -0.0293 0.0190  -0.0149 755  SER   E CA  
14665 C  C   . SER   E 451 ? 1.0478 1.1661 1.1307 -0.0326 0.0170  -0.0147 755  SER   E C   
14666 O  O   . SER   E 451 ? 1.0889 1.2134 1.1868 -0.0324 0.0223  -0.0143 755  SER   E O   
14667 C  CB  . SER   E 451 ? 1.1054 1.2152 1.1702 -0.0286 0.0119  -0.0177 755  SER   E CB  
14668 O  OG  . SER   E 451 ? 1.1316 1.2516 1.2142 -0.0275 0.0109  -0.0199 755  SER   E OG  
14669 N  N   . ALA   E 452 ? 0.9934 1.1128 1.0729 -0.0355 0.0093  -0.0151 756  ALA   E N   
14670 C  CA  . ALA   E 452 ? 1.0177 1.1446 1.1094 -0.0386 0.0073  -0.0147 756  ALA   E CA  
14671 C  C   . ALA   E 452 ? 1.0643 1.2020 1.1772 -0.0380 0.0081  -0.0165 756  ALA   E C   
14672 O  O   . ALA   E 452 ? 1.1706 1.3122 1.2953 -0.0385 0.0135  -0.0154 756  ALA   E O   
14673 C  CB  . ALA   E 452 ? 0.9988 1.1264 1.0855 -0.0412 -0.0017 -0.0153 756  ALA   E CB  
14674 N  N   . SER   E 453 ? 1.0116 1.1538 1.1295 -0.0368 0.0028  -0.0193 757  SER   E N   
14675 C  CA  . SER   E 453 ? 1.0546 1.2070 1.1924 -0.0360 0.0020  -0.0216 757  SER   E CA  
14676 C  C   . SER   E 453 ? 1.1453 1.3000 1.2942 -0.0340 0.0108  -0.0211 757  SER   E C   
14677 O  O   . SER   E 453 ? 1.1357 1.2977 1.3016 -0.0351 0.0130  -0.0212 757  SER   E O   
14678 C  CB  . SER   E 453 ? 1.0620 1.2163 1.1996 -0.0340 -0.0044 -0.0246 757  SER   E CB  
14679 O  OG  . SER   E 453 ? 1.1072 1.2532 1.2294 -0.0319 -0.0033 -0.0244 757  SER   E OG  
14680 N  N   . THR   E 454 ? 1.1727 1.3211 1.3126 -0.0311 0.0161  -0.0205 758  THR   E N   
14681 C  CA  . THR   E 454 ? 1.1676 1.3185 1.3187 -0.0287 0.0247  -0.0202 758  THR   E CA  
14682 C  C   . THR   E 454 ? 1.1696 1.3218 1.3287 -0.0307 0.0318  -0.0175 758  THR   E C   
14683 O  O   . THR   E 454 ? 1.1992 1.3590 1.3775 -0.0304 0.0361  -0.0179 758  THR   E O   
14684 C  CB  . THR   E 454 ? 1.1394 1.2814 1.2760 -0.0251 0.0297  -0.0194 758  THR   E CB  
14685 O  OG1 . THR   E 454 ? 1.1414 1.2730 1.2610 -0.0258 0.0342  -0.0162 758  THR   E OG1 
14686 C  CG2 . THR   E 454 ? 1.1452 1.2843 1.2713 -0.0236 0.0223  -0.0218 758  THR   E CG2 
14687 N  N   . GLN   E 455 ? 1.1671 1.3120 1.3126 -0.0328 0.0328  -0.0147 759  GLN   E N   
14688 C  CA  . GLN   E 455 ? 1.1573 1.3013 1.3076 -0.0343 0.0403  -0.0118 759  GLN   E CA  
14689 C  C   . GLN   E 455 ? 1.1580 1.3058 1.3129 -0.0383 0.0350  -0.0114 759  GLN   E C   
14690 O  O   . GLN   E 455 ? 1.1755 1.3170 1.3202 -0.0400 0.0370  -0.0088 759  GLN   E O   
14691 C  CB  . GLN   E 455 ? 1.1555 1.2868 1.2857 -0.0327 0.0469  -0.0087 759  GLN   E CB  
14692 C  CG  . GLN   E 455 ? 1.1857 1.3127 1.3119 -0.0284 0.0537  -0.0086 759  GLN   E CG  
14693 C  CD  . GLN   E 455 ? 1.3707 1.4837 1.4750 -0.0264 0.0598  -0.0056 759  GLN   E CD  
14694 O  OE1 . GLN   E 455 ? 1.3817 1.4874 1.4700 -0.0280 0.0559  -0.0044 759  GLN   E OE1 
14695 N  NE2 . GLN   E 455 ? 1.3928 1.5017 1.4961 -0.0228 0.0692  -0.0044 759  GLN   E NE2 
14696 N  N   . ALA   E 456 ? 1.1797 1.3371 1.3492 -0.0396 0.0282  -0.0142 760  ALA   E N   
14697 C  CA  . ALA   E 456 ? 1.1169 1.2781 1.2915 -0.0431 0.0230  -0.0141 760  ALA   E CA  
14698 C  C   . ALA   E 456 ? 1.1407 1.3087 1.3354 -0.0446 0.0279  -0.0136 760  ALA   E C   
14699 O  O   . ALA   E 456 ? 1.2201 1.3923 1.4284 -0.0430 0.0335  -0.0143 760  ALA   E O   
14700 C  CB  . ALA   E 456 ? 1.1542 1.3210 1.3320 -0.0435 0.0125  -0.0173 760  ALA   E CB  
14701 N  N   . LEU   E 457 ? 1.1800 1.3490 1.3770 -0.0478 0.0256  -0.0126 761  LEU   E N   
14702 C  CA  . LEU   E 457 ? 1.1808 1.3552 1.3959 -0.0498 0.0302  -0.0119 761  LEU   E CA  
14703 C  C   . LEU   E 457 ? 1.1174 1.3030 1.3548 -0.0498 0.0256  -0.0156 761  LEU   E C   
14704 O  O   . LEU   E 457 ? 1.1177 1.3085 1.3719 -0.0490 0.0311  -0.0162 761  LEU   E O   
14705 C  CB  . LEU   E 457 ? 1.1494 1.3208 1.3591 -0.0530 0.0286  -0.0098 761  LEU   E CB  
14706 C  CG  . LEU   E 457 ? 1.1969 1.3578 1.3915 -0.0529 0.0369  -0.0056 761  LEU   E CG  
14707 C  CD1 . LEU   E 457 ? 1.2537 1.4134 1.4504 -0.0559 0.0383  -0.0033 761  LEU   E CD1 
14708 C  CD2 . LEU   E 457 ? 1.2187 1.3779 1.4179 -0.0505 0.0476  -0.0042 761  LEU   E CD2 
14709 N  N   . SER   E 458 ? 1.0951 1.2845 1.3334 -0.0505 0.0156  -0.0181 762  SER   E N   
14710 C  CA  . SER   E 458 ? 1.1593 1.3578 1.4149 -0.0494 0.0099  -0.0222 762  SER   E CA  
14711 C  C   . SER   E 458 ? 1.1178 1.3153 1.3640 -0.0463 0.0046  -0.0245 762  SER   E C   
14712 O  O   . SER   E 458 ? 1.1281 1.3188 1.3551 -0.0460 0.0021  -0.0234 762  SER   E O   
14713 C  CB  . SER   E 458 ? 1.2029 1.4061 1.4664 -0.0517 0.0021  -0.0238 762  SER   E CB  
14714 O  OG  . SER   E 458 ? 1.2186 1.4174 1.4749 -0.0547 0.0040  -0.0207 762  SER   E OG  
14715 N  N   . SER   E 459 ? 1.0932 1.2970 1.3532 -0.0438 0.0029  -0.0276 763  SER   E N   
14716 C  CA  . SER   E 459 ? 1.0761 1.2793 1.3287 -0.0407 -0.0028 -0.0302 763  SER   E CA  
14717 C  C   . SER   E 459 ? 1.0998 1.3113 1.3688 -0.0393 -0.0104 -0.0345 763  SER   E C   
14718 O  O   . SER   E 459 ? 1.2035 1.4221 1.4926 -0.0397 -0.0091 -0.0358 763  SER   E O   
14719 C  CB  . SER   E 459 ? 1.0707 1.2710 1.3192 -0.0376 0.0037  -0.0297 763  SER   E CB  
14720 O  OG  . SER   E 459 ? 1.2036 1.4041 1.4601 -0.0383 0.0137  -0.0273 763  SER   E OG  
14721 N  N   . SER   E 460 ? 1.1357 1.3458 1.3956 -0.0374 -0.0184 -0.0366 764  SER   E N   
14722 C  CA  . SER   E 460 ? 1.0854 1.3016 1.3573 -0.0350 -0.0263 -0.0409 764  SER   E CA  
14723 C  C   . SER   E 460 ? 1.1498 1.3624 1.4096 -0.0313 -0.0301 -0.0425 764  SER   E C   
14724 O  O   . SER   E 460 ? 1.1468 1.3520 1.3878 -0.0315 -0.0288 -0.0404 764  SER   E O   
14725 C  CB  . SER   E 460 ? 1.0748 1.2927 1.3485 -0.0369 -0.0337 -0.0419 764  SER   E CB  
14726 O  OG  . SER   E 460 ? 1.0785 1.2895 1.3323 -0.0380 -0.0364 -0.0400 764  SER   E OG  
14727 N  N   . VAL   E 461 ? 1.2009 1.4183 1.4716 -0.0279 -0.0350 -0.0464 765  VAL   E N   
14728 C  CA  . VAL   E 461 ? 1.1530 1.3671 1.4134 -0.0239 -0.0394 -0.0484 765  VAL   E CA  
14729 C  C   . VAL   E 461 ? 1.1759 1.3925 1.4405 -0.0219 -0.0495 -0.0520 765  VAL   E C   
14730 O  O   . VAL   E 461 ? 1.2261 1.4495 1.5084 -0.0217 -0.0526 -0.0545 765  VAL   E O   
14731 C  CB  . VAL   E 461 ? 1.1172 1.3333 1.3845 -0.0205 -0.0349 -0.0496 765  VAL   E CB  
14732 C  CG1 . VAL   E 461 ? 1.1210 1.3313 1.3769 -0.0215 -0.0257 -0.0459 765  VAL   E CG1 
14733 C  CG2 . VAL   E 461 ? 1.1556 1.3811 1.4478 -0.0202 -0.0336 -0.0517 765  VAL   E CG2 
14734 N  N   . SER   E 462 ? 1.1998 1.4105 1.4480 -0.0203 -0.0546 -0.0523 766  SER   E N   
14735 C  CA  . SER   E 462 ? 1.2261 1.4376 1.4756 -0.0180 -0.0639 -0.0554 766  SER   E CA  
14736 C  C   . SER   E 462 ? 1.3051 1.5210 1.5670 -0.0132 -0.0674 -0.0596 766  SER   E C   
14737 O  O   . SER   E 462 ? 1.2239 1.4394 1.4855 -0.0108 -0.0635 -0.0599 766  SER   E O   
14738 C  CB  . SER   E 462 ? 1.1650 1.3684 1.3937 -0.0173 -0.0674 -0.0543 766  SER   E CB  
14739 O  OG  . SER   E 462 ? 1.1910 1.3939 1.4176 -0.0180 -0.0736 -0.0549 766  SER   E OG  
14740 N  N   . SER   E 463 ? 1.4755 1.6955 1.7485 -0.0114 -0.0747 -0.0631 767  SER   E N   
14741 C  CA  . SER   E 463 ? 1.5420 1.7658 1.8264 -0.0064 -0.0796 -0.0676 767  SER   E CA  
14742 C  C   . SER   E 463 ? 1.5987 1.8209 1.8808 -0.0035 -0.0900 -0.0707 767  SER   E C   
14743 O  O   . SER   E 463 ? 1.5943 1.8212 1.8897 -0.0041 -0.0944 -0.0729 767  SER   E O   
14744 C  CB  . SER   E 463 ? 1.5797 1.8129 1.8885 -0.0070 -0.0768 -0.0692 767  SER   E CB  
14745 O  OG  . SER   E 463 ? 1.6207 1.8584 1.9428 -0.0069 -0.0839 -0.0723 767  SER   E OG  
14746 N  N   . SER   E 464 ? 1.5500 1.7648 1.8146 -0.0003 -0.0936 -0.0710 768  SER   E N   
14747 C  CA  . SER   E 464 ? 1.5602 1.7716 1.8195 0.0032  -0.1029 -0.0737 768  SER   E CA  
14748 C  C   . SER   E 464 ? 1.5959 1.8063 1.8563 0.0098  -0.1086 -0.0779 768  SER   E C   
14749 O  O   . SER   E 464 ? 1.5506 1.7619 1.8171 0.0134  -0.1168 -0.0817 768  SER   E O   
14750 C  CB  . SER   E 464 ? 1.5268 1.7295 1.7641 0.0019  -0.1029 -0.0706 768  SER   E CB  
14751 O  OG  . SER   E 464 ? 1.5550 1.7531 1.7851 0.0061  -0.1112 -0.0731 768  SER   E OG  
14752 N  N   . LYS   E 465 ? 1.5939 1.8020 1.8484 0.0117  -0.1045 -0.0773 769  LYS   E N   
14753 C  CA  . LYS   E 465 ? 1.6425 1.8487 1.8962 0.0182  -0.1095 -0.0810 769  LYS   E CA  
14754 C  C   . LYS   E 465 ? 1.6867 1.8845 1.9246 0.0222  -0.1172 -0.0823 769  LYS   E C   
14755 O  O   . LYS   E 465 ? 1.6597 1.8563 1.8994 0.0282  -0.1241 -0.0864 769  LYS   E O   
14756 C  CB  . LYS   E 465 ? 1.6084 1.8239 1.8859 0.0209  -0.1132 -0.0855 769  LYS   E CB  
14757 N  N   . LEU   E 466 ? 1.7258 1.9174 1.9479 0.0192  -0.1159 -0.0789 770  LEU   E N   
14758 C  CA  . LEU   E 466 ? 1.7183 1.9012 1.9243 0.0227  -0.1220 -0.0795 770  LEU   E CA  
14759 C  C   . LEU   E 466 ? 1.6900 1.8650 1.8810 0.0269  -0.1217 -0.0795 770  LEU   E C   
14760 O  O   . LEU   E 466 ? 1.6433 1.8107 1.8220 0.0314  -0.1271 -0.0808 770  LEU   E O   
14761 C  CB  . LEU   E 466 ? 1.6358 1.8146 1.8300 0.0180  -0.1197 -0.0755 770  LEU   E CB  
14762 N  N   . PHE   E 467 ? 1.6929 1.8690 1.8841 0.0257  -0.1154 -0.0781 771  PHE   E N   
14763 C  CA  . PHE   E 467 ? 1.6791 1.8476 1.8564 0.0294  -0.1145 -0.0780 771  PHE   E CA  
14764 C  C   . PHE   E 467 ? 1.6756 1.8491 1.8639 0.0319  -0.1121 -0.0800 771  PHE   E C   
14765 O  O   . PHE   E 467 ? 1.6288 1.8115 1.8365 0.0318  -0.1127 -0.0823 771  PHE   E O   
14766 C  CB  . PHE   E 467 ? 1.5911 1.7532 1.7518 0.0249  -0.1081 -0.0732 771  PHE   E CB  
14767 C  CG  . PHE   E 467 ? 1.5917 1.7511 1.7449 0.0212  -0.1088 -0.0706 771  PHE   E CG  
14768 C  CD1 . PHE   E 467 ? 1.5508 1.7031 1.6926 0.0244  -0.1142 -0.0712 771  PHE   E CD1 
14769 C  CD2 . PHE   E 467 ? 1.5935 1.7571 1.7505 0.0147  -0.1037 -0.0674 771  PHE   E CD2 
14770 C  CE1 . PHE   E 467 ? 1.5371 1.6871 1.6724 0.0212  -0.1143 -0.0688 771  PHE   E CE1 
14771 C  CE2 . PHE   E 467 ? 1.5441 1.7054 1.6945 0.0115  -0.1042 -0.0650 771  PHE   E CE2 
14772 C  CZ  . PHE   E 467 ? 1.5215 1.6763 1.6614 0.0147  -0.1094 -0.0657 771  PHE   E CZ  
14773 N  N   . THR   E 476 ? 2.0208 2.1476 2.1336 0.0500  -0.0400 -0.0687 780  THR   E N   
14774 C  CA  . THR   E 476 ? 2.0618 2.1857 2.1666 0.0446  -0.0438 -0.0670 780  THR   E CA  
14775 C  C   . THR   E 476 ? 2.1283 2.2465 2.2213 0.0389  -0.0383 -0.0631 780  THR   E C   
14776 O  O   . THR   E 476 ? 2.1031 2.2144 2.1825 0.0352  -0.0408 -0.0614 780  THR   E O   
14777 C  CB  . THR   E 476 ? 1.9754 2.1104 2.0981 0.0428  -0.0479 -0.0682 780  THR   E CB  
14778 O  OG1 . THR   E 476 ? 1.9992 2.1446 2.1410 0.0428  -0.0429 -0.0684 780  THR   E OG1 
14779 C  CG2 . THR   E 476 ? 1.8566 1.9932 1.9836 0.0477  -0.0561 -0.0718 780  THR   E CG2 
14780 N  N   . SER   E 477 ? 2.2089 2.3298 2.3074 0.0385  -0.0309 -0.0618 781  SER   E N   
14781 C  CA  . SER   E 477 ? 2.1807 2.2946 2.2664 0.0346  -0.0253 -0.0584 781  SER   E CA  
14782 C  C   . SER   E 477 ? 2.1452 2.2609 2.2365 0.0372  -0.0170 -0.0579 781  SER   E C   
14783 O  O   . SER   E 477 ? 2.1527 2.2782 2.2625 0.0399  -0.0151 -0.0594 781  SER   E O   
14784 C  CB  . SER   E 477 ? 2.1552 2.2723 2.2431 0.0281  -0.0256 -0.0561 781  SER   E CB  
14785 O  OG  . SER   E 477 ? 2.1586 2.2872 2.2663 0.0272  -0.0231 -0.0562 781  SER   E OG  
14786 N  N   . PHE   E 478 ? 1.9144 2.0203 1.9898 0.0364  -0.0121 -0.0557 782  PHE   E N   
14787 C  CA  . PHE   E 478 ? 1.8051 1.9105 1.8827 0.0395  -0.0037 -0.0549 782  PHE   E CA  
14788 C  C   . PHE   E 478 ? 1.7154 1.8118 1.7775 0.0360  0.0012  -0.0517 782  PHE   E C   
14789 O  O   . PHE   E 478 ? 1.7007 1.7852 1.7435 0.0363  0.0005  -0.0511 782  PHE   E O   
14790 C  CB  . PHE   E 478 ? 1.7459 1.8464 1.8181 0.0459  -0.0035 -0.0570 782  PHE   E CB  
14791 N  N   . GLY   E 479 ? 1.6988 1.8004 1.7693 0.0328  0.0059  -0.0495 783  GLY   E N   
14792 C  CA  . GLY   E 479 ? 1.6638 1.7573 1.7204 0.0295  0.0103  -0.0465 783  GLY   E CA  
14793 C  C   . GLY   E 479 ? 1.6602 1.7479 1.7039 0.0241  0.0045  -0.0453 783  GLY   E C   
14794 O  O   . GLY   E 479 ? 1.5377 1.6179 1.5688 0.0216  0.0073  -0.0430 783  GLY   E O   
14795 N  N   . GLU   E 480 ? 1.6338 1.7249 1.6806 0.0224  -0.0033 -0.0468 784  GLU   E N   
14796 C  CA  . GLU   E 480 ? 1.5138 1.5992 1.5484 0.0178  -0.0091 -0.0459 784  GLU   E CA  
14797 C  C   . GLU   E 480 ? 1.4547 1.5457 1.4958 0.0125  -0.0090 -0.0439 784  GLU   E C   
14798 O  O   . GLU   E 480 ? 1.4905 1.5908 1.5473 0.0123  -0.0057 -0.0436 784  GLU   E O   
14799 C  CB  . GLU   E 480 ? 1.5032 1.5898 1.5388 0.0186  -0.0167 -0.0481 784  GLU   E CB  
14800 N  N   . GLU   E 481 ? 1.3861 1.4711 1.4152 0.0081  -0.0128 -0.0425 785  GLU   E N   
14801 C  CA  . GLU   E 481 ? 1.2722 1.3616 1.3059 0.0032  -0.0134 -0.0407 785  GLU   E CA  
14802 C  C   . GLU   E 481 ? 1.2978 1.3967 1.3446 0.0017  -0.0190 -0.0419 785  GLU   E C   
14803 O  O   . GLU   E 481 ? 1.2488 1.3470 1.2942 0.0031  -0.0242 -0.0436 785  GLU   E O   
14804 C  CB  . GLU   E 481 ? 1.2116 1.2914 1.2283 -0.0007 -0.0156 -0.0389 785  GLU   E CB  
14805 C  CG  . GLU   E 481 ? 1.3251 1.3946 1.3277 0.0006  -0.0106 -0.0377 785  GLU   E CG  
14806 C  CD  . GLU   E 481 ? 1.3767 1.4376 1.3643 -0.0036 -0.0130 -0.0360 785  GLU   E CD  
14807 O  OE1 . GLU   E 481 ? 1.3404 1.4010 1.3257 -0.0069 -0.0192 -0.0362 785  GLU   E OE1 
14808 O  OE2 . GLU   E 481 ? 1.3191 1.3732 1.2974 -0.0032 -0.0086 -0.0346 785  GLU   E OE2 
14809 N  N   . VAL   E 482 ? 1.3184 1.4253 1.3772 -0.0010 -0.0178 -0.0408 786  VAL   E N   
14810 C  CA  . VAL   E 482 ? 1.2312 1.3473 1.3033 -0.0024 -0.0226 -0.0419 786  VAL   E CA  
14811 C  C   . VAL   E 482 ? 1.1779 1.2959 1.2506 -0.0075 -0.0232 -0.0397 786  VAL   E C   
14812 O  O   . VAL   E 482 ? 1.1982 1.3131 1.2660 -0.0094 -0.0186 -0.0375 786  VAL   E O   
14813 C  CB  . VAL   E 482 ? 1.2454 1.3717 1.3370 0.0008  -0.0205 -0.0438 786  VAL   E CB  
14814 C  CG1 . VAL   E 482 ? 1.2542 1.3896 1.3596 -0.0007 -0.0256 -0.0450 786  VAL   E CG1 
14815 C  CG2 . VAL   E 482 ? 1.2177 1.3423 1.3090 0.0063  -0.0208 -0.0462 786  VAL   E CG2 
14816 N  N   . GLU   E 483 ? 1.1643 1.2868 1.2422 -0.0095 -0.0289 -0.0403 787  GLU   E N   
14817 C  CA  . GLU   E 483 ? 1.1155 1.2404 1.1947 -0.0142 -0.0301 -0.0384 787  GLU   E CA  
14818 C  C   . GLU   E 483 ? 1.1169 1.2526 1.2144 -0.0145 -0.0306 -0.0392 787  GLU   E C   
14819 O  O   . GLU   E 483 ? 1.0920 1.2326 1.1983 -0.0122 -0.0347 -0.0416 787  GLU   E O   
14820 C  CB  . GLU   E 483 ? 1.1339 1.2552 1.2042 -0.0166 -0.0363 -0.0381 787  GLU   E CB  
14821 C  CG  . GLU   E 483 ? 1.2439 1.3548 1.2968 -0.0178 -0.0364 -0.0369 787  GLU   E CG  
14822 C  CD  . GLU   E 483 ? 1.2946 1.4027 1.3407 -0.0209 -0.0418 -0.0362 787  GLU   E CD  
14823 O  OE1 . GLU   E 483 ? 1.3360 1.4474 1.3867 -0.0200 -0.0461 -0.0375 787  GLU   E OE1 
14824 O  OE2 . GLU   E 483 ? 1.3989 1.5012 1.4346 -0.0239 -0.0417 -0.0345 787  GLU   E OE2 
14825 N  N   . VAL   E 484 ? 1.1615 1.2999 1.2637 -0.0173 -0.0269 -0.0372 788  VAL   E N   
14826 C  CA  . VAL   E 484 ? 1.0580 1.2057 1.1766 -0.0187 -0.0276 -0.0376 788  VAL   E CA  
14827 C  C   . VAL   E 484 ? 1.0119 1.1590 1.1259 -0.0230 -0.0310 -0.0358 788  VAL   E C   
14828 O  O   . VAL   E 484 ? 1.0176 1.1594 1.1214 -0.0256 -0.0286 -0.0334 788  VAL   E O   
14829 C  CB  . VAL   E 484 ? 1.0881 1.2395 1.2168 -0.0186 -0.0200 -0.0365 788  VAL   E CB  
14830 C  CG1 . VAL   E 484 ? 1.1185 1.2801 1.2665 -0.0196 -0.0210 -0.0374 788  VAL   E CG1 
14831 C  CG2 . VAL   E 484 ? 1.1115 1.2615 1.2412 -0.0142 -0.0155 -0.0376 788  VAL   E CG2 
14832 N  N   . HIS   E 485 ? 1.0306 1.1826 1.1513 -0.0234 -0.0368 -0.0372 789  HIS   E N   
14833 C  CA  . HIS   E 485 ? 1.0297 1.1819 1.1476 -0.0271 -0.0401 -0.0357 789  HIS   E CA  
14834 C  C   . HIS   E 485 ? 1.0051 1.1651 1.1377 -0.0288 -0.0390 -0.0354 789  HIS   E C   
14835 O  O   . HIS   E 485 ? 0.9811 1.1476 1.1279 -0.0268 -0.0399 -0.0376 789  HIS   E O   
14836 C  CB  . HIS   E 485 ? 0.9757 1.1271 1.0898 -0.0265 -0.0470 -0.0370 789  HIS   E CB  
14837 C  CG  . HIS   E 485 ? 1.0882 1.2311 1.1865 -0.0263 -0.0482 -0.0364 789  HIS   E CG  
14838 N  ND1 . HIS   E 485 ? 1.1140 1.2536 1.2041 -0.0281 -0.0524 -0.0356 789  HIS   E ND1 
14839 C  CD2 . HIS   E 485 ? 1.0943 1.2311 1.1837 -0.0245 -0.0457 -0.0366 789  HIS   E CD2 
14840 C  CE1 . HIS   E 485 ? 1.1198 1.2519 1.1974 -0.0277 -0.0525 -0.0353 789  HIS   E CE1 
14841 N  NE2 . HIS   E 485 ? 1.0879 1.2179 1.1644 -0.0255 -0.0486 -0.0359 789  HIS   E NE2 
14842 N  N   . ASN   E 486 ? 0.9592 1.1180 1.0884 -0.0324 -0.0372 -0.0328 790  ASN   E N   
14843 C  CA  . ASN   E 486 ? 0.9855 1.1506 1.1272 -0.0344 -0.0360 -0.0323 790  ASN   E CA  
14844 C  C   . ASN   E 486 ? 0.9968 1.1610 1.1335 -0.0377 -0.0396 -0.0307 790  ASN   E C   
14845 O  O   . ASN   E 486 ? 0.9527 1.1110 1.0757 -0.0391 -0.0409 -0.0292 790  ASN   E O   
14846 C  CB  . ASN   E 486 ? 0.9634 1.1281 1.1083 -0.0350 -0.0280 -0.0304 790  ASN   E CB  
14847 C  CG  . ASN   E 486 ? 1.0527 1.2173 1.2011 -0.0315 -0.0236 -0.0317 790  ASN   E CG  
14848 O  OD1 . ASN   E 486 ? 1.0692 1.2281 1.2064 -0.0296 -0.0237 -0.0320 790  ASN   E OD1 
14849 N  ND2 . ASN   E 486 ? 1.1040 1.2749 1.2684 -0.0307 -0.0194 -0.0323 790  ASN   E ND2 
14850 N  N   . LEU   E 487 ? 0.9913 1.1618 1.1399 -0.0387 -0.0416 -0.0313 791  LEU   E N   
14851 C  CA  . LEU   E 487 ? 0.9704 1.1411 1.1170 -0.0419 -0.0434 -0.0295 791  LEU   E CA  
14852 C  C   . LEU   E 487 ? 0.9906 1.1614 1.1405 -0.0439 -0.0371 -0.0273 791  LEU   E C   
14853 O  O   . LEU   E 487 ? 1.0174 1.1930 1.1806 -0.0433 -0.0338 -0.0280 791  LEU   E O   
14854 C  CB  . LEU   E 487 ? 0.9501 1.1265 1.1070 -0.0416 -0.0489 -0.0313 791  LEU   E CB  
14855 C  CG  . LEU   E 487 ? 0.9187 1.0963 1.0764 -0.0446 -0.0505 -0.0297 791  LEU   E CG  
14856 C  CD1 . LEU   E 487 ? 0.9210 1.0929 1.0636 -0.0466 -0.0511 -0.0273 791  LEU   E CD1 
14857 C  CD2 . LEU   E 487 ? 0.9225 1.1044 1.0878 -0.0434 -0.0567 -0.0319 791  LEU   E CD2 
14858 N  N   . LEU   E 488 ? 0.9471 1.1122 1.0848 -0.0460 -0.0350 -0.0246 792  LEU   E N   
14859 C  CA  . LEU   E 488 ? 0.9776 1.1413 1.1159 -0.0477 -0.0291 -0.0222 792  LEU   E CA  
14860 C  C   . LEU   E 488 ? 0.9823 1.1483 1.1237 -0.0505 -0.0314 -0.0210 792  LEU   E C   
14861 O  O   . LEU   E 488 ? 1.0019 1.1682 1.1393 -0.0514 -0.0371 -0.0212 792  LEU   E O   
14862 C  CB  . LEU   E 488 ? 1.0131 1.1682 1.1354 -0.0479 -0.0256 -0.0201 792  LEU   E CB  
14863 C  CG  . LEU   E 488 ? 0.9551 1.1050 1.0692 -0.0453 -0.0233 -0.0207 792  LEU   E CG  
14864 C  CD1 . LEU   E 488 ? 0.8823 1.0230 0.9791 -0.0461 -0.0219 -0.0186 792  LEU   E CD1 
14865 C  CD2 . LEU   E 488 ? 0.9622 1.1143 1.0856 -0.0430 -0.0168 -0.0213 792  LEU   E CD2 
14866 N  N   . ILE   E 489 ? 0.9832 1.1507 1.1318 -0.0517 -0.0266 -0.0196 793  ILE   E N   
14867 C  CA  . ILE   E 489 ? 1.0550 1.2241 1.2066 -0.0543 -0.0280 -0.0183 793  ILE   E CA  
14868 C  C   . ILE   E 489 ? 1.0554 1.2184 1.1981 -0.0556 -0.0222 -0.0151 793  ILE   E C   
14869 O  O   . ILE   E 489 ? 1.0891 1.2514 1.2365 -0.0552 -0.0154 -0.0141 793  ILE   E O   
14870 C  CB  . ILE   E 489 ? 1.0751 1.2518 1.2451 -0.0545 -0.0282 -0.0198 793  ILE   E CB  
14871 C  CG1 . ILE   E 489 ? 0.9895 1.1709 1.1653 -0.0533 -0.0358 -0.0229 793  ILE   E CG1 
14872 C  CG2 . ILE   E 489 ? 1.0929 1.2697 1.2658 -0.0571 -0.0266 -0.0178 793  ILE   E CG2 
14873 C  CD1 . ILE   E 489 ? 0.9465 1.1260 1.1126 -0.0543 -0.0416 -0.0223 793  ILE   E CD1 
14874 N  N   . ILE   E 490 ? 1.0364 1.1945 1.1660 -0.0569 -0.0248 -0.0135 794  ILE   E N   
14875 C  CA  . ILE   E 490 ? 1.0455 1.1964 1.1639 -0.0576 -0.0204 -0.0107 794  ILE   E CA  
14876 C  C   . ILE   E 490 ? 1.0791 1.2308 1.1994 -0.0598 -0.0212 -0.0090 794  ILE   E C   
14877 O  O   . ILE   E 490 ? 1.0483 1.2040 1.1720 -0.0610 -0.0270 -0.0098 794  ILE   E O   
14878 C  CB  . ILE   E 490 ? 1.0195 1.1633 1.1209 -0.0571 -0.0229 -0.0102 794  ILE   E CB  
14879 C  CG1 . ILE   E 490 ? 1.0150 1.1570 1.1139 -0.0547 -0.0212 -0.0116 794  ILE   E CG1 
14880 C  CG2 . ILE   E 490 ? 1.0014 1.1371 1.0901 -0.0577 -0.0198 -0.0075 794  ILE   E CG2 
14881 C  CD1 . ILE   E 490 ? 1.0190 1.1627 1.1160 -0.0543 -0.0275 -0.0138 794  ILE   E CD1 
14882 N  N   . ASP   E 491 ? 1.0570 1.2044 1.1749 -0.0602 -0.0151 -0.0067 795  ASP   E N   
14883 C  CA  . ASP   E 491 ? 1.0445 1.1918 1.1639 -0.0621 -0.0149 -0.0049 795  ASP   E CA  
14884 C  C   . ASP   E 491 ? 1.0570 1.1980 1.1606 -0.0627 -0.0182 -0.0033 795  ASP   E C   
14885 O  O   . ASP   E 491 ? 1.0671 1.2003 1.1576 -0.0616 -0.0155 -0.0019 795  ASP   E O   
14886 C  CB  . ASP   E 491 ? 1.0963 1.2412 1.2201 -0.0621 -0.0065 -0.0029 795  ASP   E CB  
14887 C  CG  . ASP   E 491 ? 1.1560 1.3024 1.2856 -0.0641 -0.0064 -0.0016 795  ASP   E CG  
14888 O  OD1 . ASP   E 491 ? 1.0807 1.2346 1.2257 -0.0652 -0.0083 -0.0032 795  ASP   E OD1 
14889 O  OD2 . ASP   E 491 ? 1.1180 1.2577 1.2364 -0.0646 -0.0050 0.0009  795  ASP   E OD2 
14890 N  N   . GLN   E 492 ? 1.0980 1.2422 1.2029 -0.0641 -0.0242 -0.0035 796  GLN   E N   
14891 C  CA  . GLN   E 492 ? 1.0998 1.2391 1.1913 -0.0646 -0.0281 -0.0023 796  GLN   E CA  
14892 C  C   . GLN   E 492 ? 1.0666 1.1976 1.1475 -0.0644 -0.0235 0.0003  796  GLN   E C   
14893 O  O   . GLN   E 492 ? 1.0042 1.1292 1.0717 -0.0640 -0.0258 0.0011  796  GLN   E O   
14894 C  CB  . GLN   E 492 ? 1.1071 1.2515 1.2034 -0.0661 -0.0341 -0.0027 796  GLN   E CB  
14895 C  CG  . GLN   E 492 ? 1.0871 1.2318 1.1872 -0.0672 -0.0326 -0.0011 796  GLN   E CG  
14896 C  CD  . GLN   E 492 ? 1.1131 1.2613 1.2143 -0.0683 -0.0389 -0.0012 796  GLN   E CD  
14897 O  OE1 . GLN   E 492 ? 1.1320 1.2864 1.2424 -0.0684 -0.0424 -0.0029 796  GLN   E OE1 
14898 N  NE2 . GLN   E 492 ? 1.0976 1.2412 1.1887 -0.0687 -0.0406 0.0006  796  GLN   E NE2 
14899 N  N   . HIS   E 493 ? 1.1305 1.2606 1.2169 -0.0644 -0.0170 0.0017  797  HIS   E N   
14900 C  CA  . HIS   E 493 ? 1.1263 1.2478 1.2021 -0.0638 -0.0122 0.0045  797  HIS   E CA  
14901 C  C   . HIS   E 493 ? 1.1424 1.2567 1.2096 -0.0616 -0.0061 0.0051  797  HIS   E C   
14902 O  O   . HIS   E 493 ? 1.1246 1.2306 1.1760 -0.0602 -0.0068 0.0059  797  HIS   E O   
14903 C  CB  . HIS   E 493 ? 1.1578 1.2810 1.2433 -0.0650 -0.0079 0.0059  797  HIS   E CB  
14904 C  CG  . HIS   E 493 ? 1.1529 1.2821 1.2457 -0.0669 -0.0137 0.0054  797  HIS   E CG  
14905 N  ND1 . HIS   E 493 ? 1.1435 1.2698 1.2269 -0.0673 -0.0185 0.0064  797  HIS   E ND1 
14906 C  CD2 . HIS   E 493 ? 1.1327 1.2701 1.2411 -0.0682 -0.0153 0.0039  797  HIS   E CD2 
14907 C  CE1 . HIS   E 493 ? 1.1730 1.3055 1.2657 -0.0687 -0.0225 0.0057  797  HIS   E CE1 
14908 N  NE2 . HIS   E 493 ? 1.1688 1.3078 1.2764 -0.0693 -0.0208 0.0041  797  HIS   E NE2 
14909 N  N   . THR   E 494 ? 1.1522 1.2694 1.2300 -0.0610 0.0000  0.0048  798  THR   E N   
14910 C  CA  . THR   E 494 ? 1.1791 1.2900 1.2504 -0.0586 0.0069  0.0056  798  THR   E CA  
14911 C  C   . THR   E 494 ? 1.1473 1.2577 1.2127 -0.0572 0.0033  0.0035  798  THR   E C   
14912 O  O   . THR   E 494 ? 1.1541 1.2562 1.2067 -0.0550 0.0065  0.0041  798  THR   E O   
14913 C  CB  . THR   E 494 ? 1.1819 1.2971 1.2687 -0.0586 0.0145  0.0058  798  THR   E CB  
14914 O  OG1 . THR   E 494 ? 1.2248 1.3377 1.3095 -0.0562 0.0192  0.0053  798  THR   E OG1 
14915 C  CG2 . THR   E 494 ? 1.1576 1.2848 1.2635 -0.0606 0.0101  0.0034  798  THR   E CG2 
14916 N  N   . PHE   E 495 ? 1.1310 1.2495 1.2047 -0.0583 -0.0033 0.0010  799  PHE   E N   
14917 C  CA  . PHE   E 495 ? 1.0772 1.1958 1.1469 -0.0571 -0.0064 -0.0011 799  PHE   E CA  
14918 C  C   . PHE   E 495 ? 1.0800 1.1987 1.1548 -0.0550 0.0001  -0.0017 799  PHE   E C   
14919 O  O   . PHE   E 495 ? 1.2080 1.3211 1.2728 -0.0529 0.0013  -0.0020 799  PHE   E O   
14920 C  CB  . PHE   E 495 ? 1.0355 1.1450 1.0864 -0.0563 -0.0096 -0.0006 799  PHE   E CB  
14921 C  CG  . PHE   E 495 ? 1.0812 1.1926 1.1292 -0.0583 -0.0178 -0.0010 799  PHE   E CG  
14922 C  CD1 . PHE   E 495 ? 1.1066 1.2253 1.1621 -0.0593 -0.0236 -0.0032 799  PHE   E CD1 
14923 C  CD2 . PHE   E 495 ? 1.0733 1.1790 1.1109 -0.0588 -0.0196 0.0007  799  PHE   E CD2 
14924 C  CE1 . PHE   E 495 ? 1.0445 1.1651 1.0979 -0.0610 -0.0306 -0.0034 799  PHE   E CE1 
14925 C  CE2 . PHE   E 495 ? 1.0198 1.1279 1.0558 -0.0605 -0.0271 0.0002  799  PHE   E CE2 
14926 C  CZ  . PHE   E 495 ? 0.9920 1.1077 1.0362 -0.0616 -0.0323 -0.0018 799  PHE   E CZ  
14927 N  N   . GLU   E 496 ? 1.0491 1.1743 1.1399 -0.0554 0.0044  -0.0018 800  GLU   E N   
14928 C  CA  . GLU   E 496 ? 1.0695 1.1969 1.1688 -0.0535 0.0101  -0.0027 800  GLU   E CA  
14929 C  C   . GLU   E 496 ? 1.1187 1.2568 1.2345 -0.0540 0.0055  -0.0057 800  GLU   E C   
14930 O  O   . GLU   E 496 ? 1.0828 1.2264 1.2049 -0.0559 -0.0004 -0.0066 800  GLU   E O   
14931 C  CB  . GLU   E 496 ? 1.1648 1.2906 1.2704 -0.0532 0.0197  -0.0004 800  GLU   E CB  
14932 C  CG  . GLU   E 496 ? 1.2852 1.4186 1.4071 -0.0559 0.0192  -0.0003 800  GLU   E CG  
14933 C  CD  . GLU   E 496 ? 1.3785 1.5094 1.5061 -0.0560 0.0288  0.0024  800  GLU   E CD  
14934 O  OE1 . GLU   E 496 ? 1.4398 1.5650 1.5624 -0.0537 0.0367  0.0038  800  GLU   E OE1 
14935 O  OE2 . GLU   E 496 ? 1.3661 1.5002 1.5028 -0.0584 0.0288  0.0031  800  GLU   E OE2 
14936 N  N   . VAL   E 497 ? 1.1495 1.2901 1.2715 -0.0519 0.0081  -0.0073 801  VAL   E N   
14937 C  CA  . VAL   E 497 ? 1.1288 1.2780 1.2631 -0.0515 0.0028  -0.0105 801  VAL   E CA  
14938 C  C   . VAL   E 497 ? 1.0811 1.2387 1.2360 -0.0525 0.0050  -0.0112 801  VAL   E C   
14939 O  O   . VAL   E 497 ? 1.0589 1.2184 1.2237 -0.0514 0.0116  -0.0111 801  VAL   E O   
14940 C  CB  . VAL   E 497 ? 1.1628 1.3105 1.2937 -0.0486 0.0037  -0.0121 801  VAL   E CB  
14941 C  CG1 . VAL   E 497 ? 1.1026 1.2405 1.2125 -0.0478 0.0026  -0.0110 801  VAL   E CG1 
14942 C  CG2 . VAL   E 497 ? 1.2228 1.3712 1.3623 -0.0466 0.0125  -0.0117 801  VAL   E CG2 
14943 N  N   . LEU   E 498 ? 1.1157 1.2782 1.2774 -0.0547 -0.0007 -0.0119 802  LEU   E N   
14944 C  CA  . LEU   E 498 ? 1.0710 1.2408 1.2518 -0.0560 0.0004  -0.0127 802  LEU   E CA  
14945 C  C   . LEU   E 498 ? 1.1117 1.2891 1.3074 -0.0542 -0.0016 -0.0161 802  LEU   E C   
14946 O  O   . LEU   E 498 ? 1.1332 1.3151 1.3444 -0.0540 0.0033  -0.0166 802  LEU   E O   
14947 C  CB  . LEU   E 498 ? 1.0606 1.2327 1.2428 -0.0584 -0.0057 -0.0128 802  LEU   E CB  
14948 C  CG  . LEU   E 498 ? 1.0686 1.2338 1.2376 -0.0601 -0.0043 -0.0095 802  LEU   E CG  
14949 C  CD1 . LEU   E 498 ? 1.1015 1.2694 1.2724 -0.0622 -0.0107 -0.0098 802  LEU   E CD1 
14950 C  CD2 . LEU   E 498 ? 1.0676 1.2293 1.2390 -0.0606 0.0050  -0.0068 802  LEU   E CD2 
14951 N  N   . HIS   E 499 ? 1.1073 1.2861 1.2989 -0.0528 -0.0087 -0.0185 803  HIS   E N   
14952 C  CA  . HIS   E 499 ? 1.1199 1.3049 1.3234 -0.0505 -0.0118 -0.0220 803  HIS   E CA  
14953 C  C   . HIS   E 499 ? 1.0985 1.2798 1.2892 -0.0481 -0.0147 -0.0230 803  HIS   E C   
14954 O  O   . HIS   E 499 ? 1.0906 1.2661 1.2653 -0.0487 -0.0174 -0.0218 803  HIS   E O   
14955 C  CB  . HIS   E 499 ? 1.1514 1.3430 1.3662 -0.0512 -0.0195 -0.0245 803  HIS   E CB  
14956 C  CG  . HIS   E 499 ? 1.1506 1.3489 1.3805 -0.0488 -0.0223 -0.0282 803  HIS   E CG  
14957 N  ND1 . HIS   E 499 ? 1.1600 1.3633 1.4068 -0.0484 -0.0173 -0.0290 803  HIS   E ND1 
14958 C  CD2 . HIS   E 499 ? 1.1602 1.3608 1.3905 -0.0464 -0.0295 -0.0313 803  HIS   E CD2 
14959 C  CE1 . HIS   E 499 ? 1.1567 1.3655 1.4144 -0.0458 -0.0218 -0.0326 803  HIS   E CE1 
14960 N  NE2 . HIS   E 499 ? 1.1536 1.3604 1.4008 -0.0445 -0.0293 -0.0341 803  HIS   E NE2 
14961 N  N   . ALA   E 500 ? 1.1336 1.3181 1.3320 -0.0453 -0.0142 -0.0253 804  ALA   E N   
14962 C  CA  . ALA   E 500 ? 1.0630 1.2443 1.2511 -0.0427 -0.0171 -0.0267 804  ALA   E CA  
14963 C  C   . ALA   E 500 ? 1.0511 1.2392 1.2525 -0.0401 -0.0218 -0.0305 804  ALA   E C   
14964 O  O   . ALA   E 500 ? 1.0235 1.2159 1.2379 -0.0383 -0.0181 -0.0318 804  ALA   E O   
14965 C  CB  . ALA   E 500 ? 1.0815 1.2570 1.2610 -0.0410 -0.0099 -0.0252 804  ALA   E CB  
14966 N  N   . HIS   E 501 ? 1.0518 1.2404 1.2498 -0.0396 -0.0298 -0.0324 805  HIS   E N   
14967 C  CA  . HIS   E 501 ? 1.0990 1.2924 1.3063 -0.0366 -0.0354 -0.0361 805  HIS   E CA  
14968 C  C   . HIS   E 501 ? 1.0479 1.2365 1.2432 -0.0336 -0.0368 -0.0370 805  HIS   E C   
14969 O  O   . HIS   E 501 ? 1.0089 1.1918 1.1889 -0.0342 -0.0394 -0.0359 805  HIS   E O   
14970 C  CB  . HIS   E 501 ? 1.0565 1.2525 1.2666 -0.0372 -0.0432 -0.0376 805  HIS   E CB  
14971 C  CG  . HIS   E 501 ? 1.0550 1.2540 1.2711 -0.0335 -0.0496 -0.0414 805  HIS   E CG  
14972 N  ND1 . HIS   E 501 ? 1.0866 1.2926 1.3210 -0.0319 -0.0513 -0.0444 805  HIS   E ND1 
14973 C  CD2 . HIS   E 501 ? 1.0790 1.2744 1.2849 -0.0309 -0.0548 -0.0428 805  HIS   E CD2 
14974 C  CE1 . HIS   E 501 ? 1.1420 1.3485 1.3767 -0.0282 -0.0577 -0.0476 805  HIS   E CE1 
14975 N  NE2 . HIS   E 501 ? 1.1239 1.3237 1.3410 -0.0275 -0.0596 -0.0466 805  HIS   E NE2 
14976 N  N   . GLN   E 502 ? 1.0451 1.2363 1.2482 -0.0303 -0.0351 -0.0391 806  GLN   E N   
14977 C  CA  . GLN   E 502 ? 1.0616 1.2485 1.2548 -0.0271 -0.0364 -0.0403 806  GLN   E CA  
14978 C  C   . GLN   E 502 ? 1.1026 1.2917 1.2989 -0.0242 -0.0445 -0.0437 806  GLN   E C   
14979 O  O   . GLN   E 502 ? 1.1505 1.3464 1.3627 -0.0226 -0.0472 -0.0464 806  GLN   E O   
14980 C  CB  . GLN   E 502 ? 1.0470 1.2349 1.2463 -0.0246 -0.0300 -0.0406 806  GLN   E CB  
14981 C  CG  . GLN   E 502 ? 0.9902 1.1763 1.1856 -0.0202 -0.0326 -0.0431 806  GLN   E CG  
14982 C  CD  . GLN   E 502 ? 1.0504 1.2382 1.2532 -0.0174 -0.0260 -0.0435 806  GLN   E CD  
14983 O  OE1 . GLN   E 502 ? 1.0495 1.2350 1.2501 -0.0188 -0.0183 -0.0409 806  GLN   E OE1 
14984 N  NE2 . GLN   E 502 ? 1.0963 1.2877 1.3075 -0.0133 -0.0290 -0.0468 806  GLN   E NE2 
14985 N  N   . PHE   E 503 ? 1.0659 1.2489 1.2470 -0.0234 -0.0485 -0.0436 807  PHE   E N   
14986 C  CA  . PHE   E 503 ? 1.0886 1.2720 1.2700 -0.0203 -0.0559 -0.0465 807  PHE   E CA  
14987 C  C   . PHE   E 503 ? 1.0536 1.2382 1.2400 -0.0156 -0.0564 -0.0494 807  PHE   E C   
14988 O  O   . PHE   E 503 ? 1.0091 1.1949 1.2002 -0.0147 -0.0508 -0.0492 807  PHE   E O   
14989 C  CB  . PHE   E 503 ? 1.0791 1.2554 1.2431 -0.0211 -0.0592 -0.0451 807  PHE   E CB  
14990 C  CG  . PHE   E 503 ? 1.0120 1.1876 1.1719 -0.0252 -0.0599 -0.0427 807  PHE   E CG  
14991 C  CD1 . PHE   E 503 ? 0.9909 1.1691 1.1550 -0.0252 -0.0655 -0.0438 807  PHE   E CD1 
14992 C  CD2 . PHE   E 503 ? 0.9623 1.1342 1.1133 -0.0287 -0.0554 -0.0395 807  PHE   E CD2 
14993 C  CE1 . PHE   E 503 ? 0.9866 1.1641 1.1466 -0.0287 -0.0661 -0.0415 807  PHE   E CE1 
14994 C  CE2 . PHE   E 503 ? 1.0162 1.1874 1.1632 -0.0322 -0.0564 -0.0373 807  PHE   E CE2 
14995 C  CZ  . PHE   E 503 ? 1.0373 1.2116 1.1892 -0.0323 -0.0616 -0.0382 807  PHE   E CZ  
14996 N  N   . LEU   E 504 ? 1.0609 1.2443 1.2450 -0.0121 -0.0631 -0.0520 808  LEU   E N   
14997 C  CA  . LEU   E 504 ? 1.0974 1.2819 1.2864 -0.0070 -0.0650 -0.0552 808  LEU   E CA  
14998 C  C   . LEU   E 504 ? 1.0878 1.2655 1.2635 -0.0055 -0.0613 -0.0542 808  LEU   E C   
14999 O  O   . LEU   E 504 ? 1.1022 1.2728 1.2621 -0.0077 -0.0599 -0.0516 808  LEU   E O   
15000 C  CB  . LEU   E 504 ? 1.0814 1.2648 1.2692 -0.0035 -0.0735 -0.0581 808  LEU   E CB  
15001 C  CG  . LEU   E 504 ? 1.1482 1.3393 1.3537 -0.0019 -0.0785 -0.0614 808  LEU   E CG  
15002 C  CD1 . LEU   E 504 ? 1.1574 1.3545 1.3785 0.0014  -0.0772 -0.0642 808  LEU   E CD1 
15003 C  CD2 . LEU   E 504 ? 1.1848 1.3804 1.3984 -0.0068 -0.0769 -0.0596 808  LEU   E CD2 
15004 N  N   . GLN   E 505 ? 1.0350 1.2147 1.2176 -0.0016 -0.0600 -0.0563 809  GLN   E N   
15005 C  CA  . GLN   E 505 ? 1.1413 1.3143 1.3115 0.0004  -0.0567 -0.0557 809  GLN   E CA  
15006 C  C   . GLN   E 505 ? 1.1752 1.3399 1.3286 0.0018  -0.0616 -0.0558 809  GLN   E C   
15007 O  O   . GLN   E 505 ? 1.1918 1.3568 1.3462 0.0041  -0.0681 -0.0579 809  GLN   E O   
15008 C  CB  . GLN   E 505 ? 1.1323 1.3094 1.3138 0.0052  -0.0554 -0.0584 809  GLN   E CB  
15009 N  N   . ASN   E 506 ? 1.1874 1.3442 1.3250 0.0004  -0.0584 -0.0535 810  ASN   E N   
15010 C  CA  . ASN   E 506 ? 1.2151 1.3632 1.3363 0.0010  -0.0619 -0.0530 810  ASN   E CA  
15011 C  C   . ASN   E 506 ? 1.2028 1.3503 1.3201 -0.0024 -0.0655 -0.0516 810  ASN   E C   
15012 O  O   . ASN   E 506 ? 1.2187 1.3602 1.3250 -0.0016 -0.0690 -0.0515 810  ASN   E O   
15013 C  CB  . ASN   E 506 ? 1.2479 1.3941 1.3684 0.0068  -0.0665 -0.0563 810  ASN   E CB  
15014 C  CG  . ASN   E 506 ? 1.3040 1.4502 1.4272 0.0106  -0.0632 -0.0577 810  ASN   E CG  
15015 O  OD1 . ASN   E 506 ? 1.3882 1.5327 1.5083 0.0090  -0.0572 -0.0559 810  ASN   E OD1 
15016 N  ND2 . ASN   E 506 ? 1.3667 1.5142 1.4950 0.0160  -0.0673 -0.0610 810  ASN   E ND2 
15017 N  N   . GLU   E 507 ? 1.1584 1.3118 1.2847 -0.0059 -0.0645 -0.0505 811  GLU   E N   
15018 C  CA  . GLU   E 507 ? 1.1273 1.2804 1.2505 -0.0087 -0.0679 -0.0492 811  GLU   E CA  
15019 C  C   . GLU   E 507 ? 1.0802 1.2288 1.1925 -0.0136 -0.0643 -0.0457 811  GLU   E C   
15020 O  O   . GLU   E 507 ? 1.0936 1.2438 1.2083 -0.0160 -0.0594 -0.0441 811  GLU   E O   
15021 C  CB  . GLU   E 507 ? 1.0936 1.2552 1.2323 -0.0096 -0.0696 -0.0502 811  GLU   E CB  
15022 C  CG  . GLU   E 507 ? 1.1155 1.2767 1.2509 -0.0123 -0.0729 -0.0489 811  GLU   E CG  
15023 C  CD  . GLU   E 507 ? 1.1442 1.3128 1.2942 -0.0120 -0.0763 -0.0507 811  GLU   E CD  
15024 O  OE1 . GLU   E 507 ? 1.1250 1.2998 1.2874 -0.0138 -0.0732 -0.0506 811  GLU   E OE1 
15025 O  OE2 . GLU   E 507 ? 1.1918 1.3592 1.3403 -0.0098 -0.0820 -0.0521 811  GLU   E OE2 
15026 N  N   . TYR   E 508 ? 1.0373 1.1797 1.1373 -0.0146 -0.0667 -0.0444 812  TYR   E N   
15027 C  CA  . TYR   E 508 ? 1.0107 1.1488 1.1008 -0.0191 -0.0645 -0.0413 812  TYR   E CA  
15028 C  C   . TYR   E 508 ? 1.0451 1.1869 1.1389 -0.0222 -0.0666 -0.0400 812  TYR   E C   
15029 O  O   . TYR   E 508 ? 1.0653 1.2074 1.1595 -0.0208 -0.0708 -0.0408 812  TYR   E O   
15030 C  CB  . TYR   E 508 ? 1.0666 1.1959 1.1421 -0.0188 -0.0657 -0.0406 812  TYR   E CB  
15031 C  CG  . TYR   E 508 ? 1.0446 1.1685 1.1106 -0.0220 -0.0621 -0.0385 812  TYR   E CG  
15032 C  CD1 . TYR   E 508 ? 1.0384 1.1614 1.1003 -0.0265 -0.0619 -0.0360 812  TYR   E CD1 
15033 C  CD2 . TYR   E 508 ? 1.0534 1.1732 1.1147 -0.0202 -0.0591 -0.0391 812  TYR   E CD2 
15034 C  CE1 . TYR   E 508 ? 1.0480 1.1658 1.1011 -0.0292 -0.0594 -0.0343 812  TYR   E CE1 
15035 C  CE2 . TYR   E 508 ? 1.1030 1.2171 1.1548 -0.0228 -0.0562 -0.0373 812  TYR   E CE2 
15036 C  CZ  . TYR   E 508 ? 1.1199 1.2330 1.1677 -0.0274 -0.0566 -0.0350 812  TYR   E CZ  
15037 O  OH  . TYR   E 508 ? 1.2519 1.3589 1.2901 -0.0298 -0.0545 -0.0335 812  TYR   E OH  
15038 N  N   . ALA   E 509 ? 1.0218 1.1658 1.1176 -0.0260 -0.0635 -0.0379 813  ALA   E N   
15039 C  CA  . ALA   E 509 ? 0.9799 1.1271 1.0787 -0.0291 -0.0652 -0.0365 813  ALA   E CA  
15040 C  C   . ALA   E 509 ? 0.9403 1.0820 1.0273 -0.0323 -0.0655 -0.0340 813  ALA   E C   
15041 O  O   . ALA   E 509 ? 0.9953 1.1333 1.0756 -0.0344 -0.0625 -0.0324 813  ALA   E O   
15042 C  CB  . ALA   E 509 ? 0.9311 1.0838 1.0395 -0.0312 -0.0618 -0.0357 813  ALA   E CB  
15043 N  N   . LEU   E 510 ? 0.8613 1.0024 0.9459 -0.0325 -0.0691 -0.0336 814  LEU   E N   
15044 C  CA  . LEU   E 510 ? 0.8984 1.0343 0.9728 -0.0351 -0.0697 -0.0314 814  LEU   E CA  
15045 C  C   . LEU   E 510 ? 0.9527 1.0915 1.0290 -0.0384 -0.0706 -0.0295 814  LEU   E C   
15046 O  O   . LEU   E 510 ? 1.0036 1.1397 1.0740 -0.0417 -0.0698 -0.0274 814  LEU   E O   
15047 C  CB  . LEU   E 510 ? 0.9959 1.1271 1.0640 -0.0325 -0.0723 -0.0322 814  LEU   E CB  
15048 C  CG  . LEU   E 510 ? 1.0504 1.1783 1.1163 -0.0284 -0.0723 -0.0344 814  LEU   E CG  
15049 C  CD1 . LEU   E 510 ? 1.0597 1.1821 1.1183 -0.0260 -0.0748 -0.0347 814  LEU   E CD1 
15050 C  CD2 . LEU   E 510 ? 0.9974 1.1212 1.0574 -0.0296 -0.0690 -0.0340 814  LEU   E CD2 
15051 N  N   . SER   E 511 ? 0.9656 1.1094 1.0498 -0.0374 -0.0727 -0.0302 815  SER   E N   
15052 C  CA  . SER   E 511 ? 0.9424 1.0884 1.0277 -0.0401 -0.0739 -0.0283 815  SER   E CA  
15053 C  C   . SER   E 511 ? 0.9456 1.0977 1.0407 -0.0411 -0.0730 -0.0284 815  SER   E C   
15054 O  O   . SER   E 511 ? 0.9653 1.1207 1.0684 -0.0391 -0.0726 -0.0304 815  SER   E O   
15055 C  CB  . SER   E 511 ? 0.9891 1.1342 1.0733 -0.0379 -0.0773 -0.0287 815  SER   E CB  
15056 O  OG  . SER   E 511 ? 1.0071 1.1521 1.0938 -0.0334 -0.0791 -0.0315 815  SER   E OG  
15057 N  N   . LEU   E 512 ? 0.9922 1.1457 1.0873 -0.0444 -0.0726 -0.0263 816  LEU   E N   
15058 C  CA  . LEU   E 512 ? 0.9527 1.1113 1.0564 -0.0457 -0.0716 -0.0261 816  LEU   E CA  
15059 C  C   . LEU   E 512 ? 0.9054 1.0654 1.0090 -0.0476 -0.0734 -0.0243 816  LEU   E C   
15060 O  O   . LEU   E 512 ? 0.9807 1.1380 1.0772 -0.0497 -0.0736 -0.0224 816  LEU   E O   
15061 C  CB  . LEU   E 512 ? 0.9057 1.0636 1.0086 -0.0477 -0.0673 -0.0250 816  LEU   E CB  
15062 C  CG  . LEU   E 512 ? 0.9301 1.0921 1.0414 -0.0489 -0.0649 -0.0246 816  LEU   E CG  
15063 C  CD1 . LEU   E 512 ? 0.9088 1.0757 1.0320 -0.0464 -0.0654 -0.0272 816  LEU   E CD1 
15064 C  CD2 . LEU   E 512 ? 0.9351 1.0939 1.0416 -0.0503 -0.0603 -0.0233 816  LEU   E CD2 
15065 N  N   . VAL   E 513 ? 0.9746 1.1389 1.0864 -0.0469 -0.0750 -0.0252 817  VAL   E N   
15066 C  CA  . VAL   E 513 ? 1.0792 1.2450 1.1914 -0.0484 -0.0767 -0.0236 817  VAL   E CA  
15067 C  C   . VAL   E 513 ? 1.0408 1.2112 1.1629 -0.0489 -0.0765 -0.0242 817  VAL   E C   
15068 O  O   . VAL   E 513 ? 1.0017 1.1747 1.1318 -0.0469 -0.0769 -0.0265 817  VAL   E O   
15069 C  CB  . VAL   E 513 ? 0.9666 1.1309 1.0756 -0.0462 -0.0802 -0.0240 817  VAL   E CB  
15070 C  CG1 . VAL   E 513 ? 0.9482 1.1145 1.0638 -0.0425 -0.0831 -0.0268 817  VAL   E CG1 
15071 C  CG2 . VAL   E 513 ? 0.9492 1.1143 1.0566 -0.0481 -0.0811 -0.0218 817  VAL   E CG2 
15072 N  N   . SER   E 514 ? 1.0377 1.2091 1.1596 -0.0515 -0.0758 -0.0222 818  SER   E N   
15073 C  CA  . SER   E 514 ? 1.0749 1.2501 1.2054 -0.0521 -0.0761 -0.0224 818  SER   E CA  
15074 C  C   . SER   E 514 ? 1.0573 1.2328 1.1865 -0.0516 -0.0795 -0.0218 818  SER   E C   
15075 O  O   . SER   E 514 ? 1.0535 1.2270 1.1755 -0.0529 -0.0797 -0.0197 818  SER   E O   
15076 C  CB  . SER   E 514 ? 1.0643 1.2395 1.1951 -0.0551 -0.0721 -0.0204 818  SER   E CB  
15077 O  OG  . SER   E 514 ? 1.0703 1.2480 1.2067 -0.0561 -0.0727 -0.0198 818  SER   E OG  
15078 N  N   . CYS   E 515 ? 1.0680 1.2458 1.2042 -0.0496 -0.0823 -0.0237 819  CYS   E N   
15079 C  CA  . CYS   E 515 ? 1.1913 1.3692 1.3264 -0.0491 -0.0853 -0.0231 819  CYS   E CA  
15080 C  C   . CYS   E 515 ? 1.1555 1.3358 1.2998 -0.0471 -0.0883 -0.0256 819  CYS   E C   
15081 O  O   . CYS   E 515 ? 1.1494 1.3318 1.3018 -0.0465 -0.0881 -0.0277 819  CYS   E O   
15082 C  CB  . CYS   E 515 ? 1.1856 1.3601 1.3123 -0.0470 -0.0873 -0.0227 819  CYS   E CB  
15083 S  SG  . CYS   E 515 ? 1.0158 1.1886 1.1427 -0.0427 -0.0896 -0.0259 819  CYS   E SG  
15084 N  N   . LYS   E 516 ? 1.1565 1.3363 1.2997 -0.0461 -0.0912 -0.0253 820  LYS   E N   
15085 C  CA  . LYS   E 516 ? 1.2316 1.4124 1.3814 -0.0436 -0.0952 -0.0278 820  LYS   E CA  
15086 C  C   . LYS   E 516 ? 1.2421 1.4193 1.3848 -0.0396 -0.0989 -0.0287 820  LYS   E C   
15087 O  O   . LYS   E 516 ? 1.2705 1.4453 1.4048 -0.0398 -0.0982 -0.0263 820  LYS   E O   
15088 C  CB  . LYS   E 516 ? 1.1177 1.3001 1.2717 -0.0457 -0.0953 -0.0267 820  LYS   E CB  
15089 N  N   . LEU   E 517 ? 1.2846 1.4610 1.4304 -0.0359 -0.1028 -0.0320 821  LEU   E N   
15090 C  CA  . LEU   E 517 ? 1.2737 1.4454 1.4118 -0.0313 -0.1063 -0.0330 821  LEU   E CA  
15091 C  C   . LEU   E 517 ? 1.2583 1.4291 1.4000 -0.0282 -0.1115 -0.0355 821  LEU   E C   
15092 O  O   . LEU   E 517 ? 1.2821 1.4563 1.4344 -0.0289 -0.1132 -0.0376 821  LEU   E O   
15093 C  CB  . LEU   E 517 ? 1.2258 1.3956 1.3619 -0.0284 -0.1071 -0.0351 821  LEU   E CB  
15094 C  CG  . LEU   E 517 ? 1.1775 1.3471 1.3093 -0.0309 -0.1025 -0.0332 821  LEU   E CG  
15095 C  CD1 . LEU   E 517 ? 1.2417 1.4102 1.3662 -0.0337 -0.0994 -0.0293 821  LEU   E CD1 
15096 C  CD2 . LEU   E 517 ? 1.1680 1.3421 1.3089 -0.0339 -0.0998 -0.0337 821  LEU   E CD2 
15097 N  N   . GLY   E 518 ? 1.2554 1.4213 1.3882 -0.0245 -0.1139 -0.0353 822  GLY   E N   
15098 C  CA  . GLY   E 518 ? 1.2809 1.4446 1.4152 -0.0209 -0.1192 -0.0377 822  GLY   E CA  
15099 C  C   . GLY   E 518 ? 1.2907 1.4576 1.4315 -0.0239 -0.1191 -0.0368 822  GLY   E C   
15100 O  O   . GLY   E 518 ? 1.3077 1.4777 1.4498 -0.0284 -0.1148 -0.0339 822  GLY   E O   
15101 N  N   . LYS   E 519 ? 1.2894 1.4547 1.4337 -0.0211 -0.1244 -0.0396 823  LYS   E N   
15102 C  CA  . LYS   E 519 ? 1.2256 1.3934 1.3769 -0.0237 -0.1248 -0.0393 823  LYS   E CA  
15103 C  C   . LYS   E 519 ? 1.2608 1.4345 1.4260 -0.0278 -0.1233 -0.0404 823  LYS   E C   
15104 O  O   . LYS   E 519 ? 1.2373 1.4131 1.4092 -0.0305 -0.1229 -0.0400 823  LYS   E O   
15105 C  CB  . LYS   E 519 ? 1.0402 1.2037 1.1904 -0.0192 -0.1312 -0.0421 823  LYS   E CB  
15106 N  N   . ASP   E 520 ? 1.2688 1.4448 1.4382 -0.0282 -0.1219 -0.0416 824  ASP   E N   
15107 C  CA  . ASP   E 520 ? 1.2341 1.4156 1.4158 -0.0322 -0.1189 -0.0419 824  ASP   E CA  
15108 C  C   . ASP   E 520 ? 1.2453 1.4287 1.4253 -0.0371 -0.1128 -0.0377 824  ASP   E C   
15109 O  O   . ASP   E 520 ? 1.2616 1.4430 1.4310 -0.0376 -0.1102 -0.0347 824  ASP   E O   
15110 C  CB  . ASP   E 520 ? 1.1972 1.3801 1.3809 -0.0314 -0.1176 -0.0433 824  ASP   E CB  
15111 C  CG  . ASP   E 520 ? 1.1779 1.3662 1.3762 -0.0341 -0.1156 -0.0446 824  ASP   E CG  
15112 O  OD1 . ASP   E 520 ? 1.2083 1.3991 1.4116 -0.0383 -0.1115 -0.0425 824  ASP   E OD1 
15113 O  OD2 . ASP   E 520 ? 1.1334 1.3230 1.3379 -0.0318 -0.1178 -0.0477 824  ASP   E OD2 
15114 N  N   . PRO   E 521 ? 1.2482 1.4350 1.4384 -0.0407 -0.1105 -0.0374 825  PRO   E N   
15115 C  CA  . PRO   E 521 ? 1.2258 1.4134 1.4131 -0.0449 -0.1051 -0.0335 825  PRO   E CA  
15116 C  C   . PRO   E 521 ? 1.2625 1.4523 1.4518 -0.0479 -0.0992 -0.0320 825  PRO   E C   
15117 O  O   . PRO   E 521 ? 1.3222 1.5114 1.5054 -0.0505 -0.0950 -0.0286 825  PRO   E O   
15118 C  CB  . PRO   E 521 ? 1.2296 1.4182 1.4256 -0.0466 -0.1061 -0.0340 825  PRO   E CB  
15119 C  CG  . PRO   E 521 ? 1.2613 1.4524 1.4703 -0.0454 -0.1091 -0.0380 825  PRO   E CG  
15120 C  CD  . PRO   E 521 ? 1.2668 1.4559 1.4707 -0.0407 -0.1135 -0.0406 825  PRO   E CD  
15121 N  N   . ASN   E 522 ? 1.2151 1.4073 1.4127 -0.0473 -0.0990 -0.0344 826  ASN   E N   
15122 C  CA  . ASN   E 522 ? 1.2815 1.4756 1.4813 -0.0500 -0.0929 -0.0328 826  ASN   E CA  
15123 C  C   . ASN   E 522 ? 1.2343 1.4259 1.4217 -0.0495 -0.0910 -0.0310 826  ASN   E C   
15124 O  O   . ASN   E 522 ? 1.2111 1.4002 1.3901 -0.0469 -0.0942 -0.0313 826  ASN   E O   
15125 C  CB  . ASN   E 522 ? 1.2090 1.4066 1.4222 -0.0494 -0.0928 -0.0358 826  ASN   E CB  
15126 C  CG  . ASN   E 522 ? 1.1909 1.3898 1.4135 -0.0466 -0.0994 -0.0399 826  ASN   E CG  
15127 O  OD1 . ASN   E 522 ? 1.1903 1.3908 1.4190 -0.0441 -0.1020 -0.0430 826  ASN   E OD1 
15128 N  ND2 . ASN   E 522 ? 1.2294 1.4273 1.4533 -0.0469 -0.1025 -0.0400 826  ASN   E ND2 
15129 N  N   . THR   E 523 ? 1.1800 1.3718 1.3658 -0.0519 -0.0855 -0.0291 827  THR   E N   
15130 C  CA  . THR   E 523 ? 1.1662 1.3556 1.3415 -0.0516 -0.0836 -0.0277 827  THR   E CA  
15131 C  C   . THR   E 523 ? 1.1640 1.3546 1.3436 -0.0505 -0.0818 -0.0295 827  THR   E C   
15132 O  O   . THR   E 523 ? 1.1495 1.3427 1.3389 -0.0517 -0.0788 -0.0301 827  THR   E O   
15133 C  CB  . THR   E 523 ? 1.1203 1.3077 1.2877 -0.0547 -0.0793 -0.0241 827  THR   E CB  
15134 O  OG1 . THR   E 523 ? 1.2037 1.3912 1.3715 -0.0562 -0.0801 -0.0226 827  THR   E OG1 
15135 C  CG2 . THR   E 523 ? 1.1516 1.3360 1.3070 -0.0541 -0.0800 -0.0228 827  THR   E CG2 
15136 N  N   . TYR   E 524 ? 1.1244 1.3129 1.2971 -0.0481 -0.0834 -0.0303 828  TYR   E N   
15137 C  CA  . TYR   E 524 ? 1.0901 1.2795 1.2663 -0.0464 -0.0824 -0.0322 828  TYR   E CA  
15138 C  C   . TYR   E 524 ? 1.1153 1.3013 1.2806 -0.0471 -0.0791 -0.0304 828  TYR   E C   
15139 O  O   . TYR   E 524 ? 1.1233 1.3061 1.2780 -0.0478 -0.0796 -0.0284 828  TYR   E O   
15140 C  CB  . TYR   E 524 ? 1.0702 1.2595 1.2486 -0.0422 -0.0880 -0.0356 828  TYR   E CB  
15141 C  CG  . TYR   E 524 ? 1.1505 1.3419 1.3375 -0.0410 -0.0927 -0.0378 828  TYR   E CG  
15142 C  CD1 . TYR   E 524 ? 1.1674 1.3568 1.3491 -0.0410 -0.0955 -0.0368 828  TYR   E CD1 
15143 C  CD2 . TYR   E 524 ? 1.1843 1.3795 1.3851 -0.0397 -0.0945 -0.0411 828  TYR   E CD2 
15144 C  CE1 . TYR   E 524 ? 1.1854 1.3760 1.3744 -0.0396 -0.1001 -0.0390 828  TYR   E CE1 
15145 C  CE2 . TYR   E 524 ? 1.1812 1.3779 1.3903 -0.0386 -0.0994 -0.0434 828  TYR   E CE2 
15146 C  CZ  . TYR   E 524 ? 1.2085 1.4025 1.4110 -0.0385 -0.1023 -0.0424 828  TYR   E CZ  
15147 O  OH  . TYR   E 524 ? 1.2477 1.4425 1.4577 -0.0371 -0.1074 -0.0448 828  TYR   E OH  
15148 N  N   . PHE   E 525 ? 1.0799 1.2664 1.2482 -0.0468 -0.0758 -0.0311 829  PHE   E N   
15149 C  CA  . PHE   E 525 ? 1.0081 1.1910 1.1666 -0.0464 -0.0736 -0.0302 829  PHE   E CA  
15150 C  C   . PHE   E 525 ? 0.9945 1.1765 1.1522 -0.0425 -0.0774 -0.0329 829  PHE   E C   
15151 O  O   . PHE   E 525 ? 0.9977 1.1826 1.1646 -0.0404 -0.0781 -0.0356 829  PHE   E O   
15152 C  CB  . PHE   E 525 ? 0.9751 1.1583 1.1362 -0.0476 -0.0679 -0.0295 829  PHE   E CB  
15153 C  CG  . PHE   E 525 ? 1.0197 1.2016 1.1777 -0.0511 -0.0636 -0.0265 829  PHE   E CG  
15154 C  CD1 . PHE   E 525 ? 1.0754 1.2534 1.2216 -0.0528 -0.0637 -0.0240 829  PHE   E CD1 
15155 C  CD2 . PHE   E 525 ? 0.9771 1.1614 1.1441 -0.0524 -0.0593 -0.0261 829  PHE   E CD2 
15156 C  CE1 . PHE   E 525 ? 1.0459 1.2222 1.1886 -0.0555 -0.0602 -0.0214 829  PHE   E CE1 
15157 C  CE2 . PHE   E 525 ? 0.9740 1.1561 1.1370 -0.0551 -0.0552 -0.0232 829  PHE   E CE2 
15158 C  CZ  . PHE   E 525 ? 0.9634 1.1413 1.1138 -0.0565 -0.0559 -0.0210 829  PHE   E CZ  
15159 N  N   . ILE   E 526 ? 0.9589 1.1369 1.1060 -0.0415 -0.0799 -0.0323 830  ILE   E N   
15160 C  CA  . ILE   E 526 ? 1.0163 1.1919 1.1601 -0.0375 -0.0831 -0.0345 830  ILE   E CA  
15161 C  C   . ILE   E 526 ? 0.9797 1.1515 1.1152 -0.0375 -0.0802 -0.0338 830  ILE   E C   
15162 O  O   . ILE   E 526 ? 0.9735 1.1422 1.1003 -0.0401 -0.0779 -0.0312 830  ILE   E O   
15163 C  CB  . ILE   E 526 ? 0.9906 1.1635 1.1278 -0.0359 -0.0873 -0.0343 830  ILE   E CB  
15164 C  CG1 . ILE   E 526 ? 1.0206 1.1966 1.1645 -0.0364 -0.0897 -0.0346 830  ILE   E CG1 
15165 C  CG2 . ILE   E 526 ? 0.9645 1.1345 1.0990 -0.0310 -0.0910 -0.0370 830  ILE   E CG2 
15166 C  CD1 . ILE   E 526 ? 1.0132 1.1865 1.1491 -0.0369 -0.0912 -0.0325 830  ILE   E CD1 
15167 N  N   . VAL   E 527 ? 0.9250 1.0967 1.0631 -0.0344 -0.0806 -0.0362 831  VAL   E N   
15168 C  CA  . VAL   E 527 ? 0.9709 1.1389 1.1019 -0.0341 -0.0778 -0.0358 831  VAL   E CA  
15169 C  C   . VAL   E 527 ? 1.0033 1.1673 1.1283 -0.0301 -0.0812 -0.0376 831  VAL   E C   
15170 O  O   . VAL   E 527 ? 0.9646 1.1302 1.0953 -0.0264 -0.0849 -0.0404 831  VAL   E O   
15171 C  CB  . VAL   E 527 ? 1.0199 1.1910 1.1590 -0.0341 -0.0739 -0.0367 831  VAL   E CB  
15172 C  CG1 . VAL   E 527 ? 1.0174 1.1844 1.1496 -0.0323 -0.0720 -0.0372 831  VAL   E CG1 
15173 C  CG2 . VAL   E 527 ? 0.9864 1.1590 1.1272 -0.0382 -0.0694 -0.0342 831  VAL   E CG2 
15174 N  N   . GLY   E 528 ? 1.0311 1.1894 1.1443 -0.0306 -0.0801 -0.0361 832  GLY   E N   
15175 C  CA  . GLY   E 528 ? 1.0796 1.2328 1.1856 -0.0269 -0.0822 -0.0374 832  GLY   E CA  
15176 C  C   . GLY   E 528 ? 1.0173 1.1683 1.1209 -0.0259 -0.0795 -0.0381 832  GLY   E C   
15177 O  O   . GLY   E 528 ? 0.9954 1.1454 1.0960 -0.0289 -0.0756 -0.0364 832  GLY   E O   
15178 N  N   . THR   E 529 ? 1.0254 1.1750 1.1297 -0.0214 -0.0817 -0.0408 833  THR   E N   
15179 C  CA  . THR   E 529 ? 1.0412 1.1892 1.1445 -0.0197 -0.0793 -0.0419 833  THR   E CA  
15180 C  C   . THR   E 529 ? 1.0821 1.2236 1.1764 -0.0156 -0.0817 -0.0432 833  THR   E C   
15181 O  O   . THR   E 529 ? 1.0845 1.2227 1.1738 -0.0137 -0.0850 -0.0434 833  THR   E O   
15182 C  CB  . THR   E 529 ? 1.0533 1.2079 1.1704 -0.0178 -0.0791 -0.0444 833  THR   E CB  
15183 O  OG1 . THR   E 529 ? 1.0968 1.2532 1.2196 -0.0136 -0.0844 -0.0474 833  THR   E OG1 
15184 C  CG2 . THR   E 529 ? 1.0647 1.2250 1.1905 -0.0217 -0.0764 -0.0430 833  THR   E CG2 
15185 N  N   . ALA   E 530 ? 1.1271 1.2661 1.2188 -0.0140 -0.0795 -0.0441 834  ALA   E N   
15186 C  CA  . ALA   E 530 ? 1.0942 1.2272 1.1785 -0.0095 -0.0815 -0.0457 834  ALA   E CA  
15187 C  C   . ALA   E 530 ? 1.0615 1.1965 1.1514 -0.0066 -0.0800 -0.0480 834  ALA   E C   
15188 O  O   . ALA   E 530 ? 1.0261 1.1634 1.1191 -0.0090 -0.0758 -0.0471 834  ALA   E O   
15189 C  CB  . ALA   E 530 ? 1.0640 1.1886 1.1338 -0.0113 -0.0800 -0.0434 834  ALA   E CB  
15190 N  N   . MET   E 531 ? 1.0686 1.2025 1.1598 -0.0012 -0.0836 -0.0509 835  MET   E N   
15191 C  CA  . MET   E 531 ? 1.1366 1.2716 1.2322 0.0024  -0.0826 -0.0532 835  MET   E CA  
15192 C  C   . MET   E 531 ? 1.1247 1.2506 1.2059 0.0033  -0.0807 -0.0523 835  MET   E C   
15193 O  O   . MET   E 531 ? 1.1566 1.2755 1.2266 0.0041  -0.0827 -0.0516 835  MET   E O   
15194 C  CB  . MET   E 531 ? 1.1673 1.3051 1.2711 0.0081  -0.0879 -0.0571 835  MET   E CB  
15195 C  CG  . MET   E 531 ? 1.2274 1.3743 1.3469 0.0073  -0.0901 -0.0585 835  MET   E CG  
15196 S  SD  . MET   E 531 ? 1.1934 1.3489 1.3265 0.0028  -0.0839 -0.0572 835  MET   E SD  
15197 C  CE  . MET   E 531 ? 1.1535 1.3121 1.2959 0.0076  -0.0829 -0.0604 835  MET   E CE  
15198 N  N   . VAL   E 532 ? 1.0907 1.2163 1.1718 0.0031  -0.0765 -0.0522 836  VAL   E N   
15199 C  CA  . VAL   E 532 ? 1.1561 1.2726 1.2230 0.0033  -0.0745 -0.0511 836  VAL   E CA  
15200 C  C   . VAL   E 532 ? 1.2585 1.3746 1.3274 0.0075  -0.0728 -0.0532 836  VAL   E C   
15201 O  O   . VAL   E 532 ? 1.2286 1.3510 1.3081 0.0074  -0.0698 -0.0538 836  VAL   E O   
15202 C  CB  . VAL   E 532 ? 1.1477 1.2614 1.2076 -0.0025 -0.0705 -0.0478 836  VAL   E CB  
15203 C  CG1 . VAL   E 532 ? 1.0894 1.2062 1.1515 -0.0067 -0.0718 -0.0458 836  VAL   E CG1 
15204 C  CG2 . VAL   E 532 ? 1.1783 1.2954 1.2436 -0.0037 -0.0657 -0.0475 836  VAL   E CG2 
15205 N  N   . TYR   E 533 ? 1.2499 1.3581 1.3084 0.0113  -0.0743 -0.0542 837  TYR   E N   
15206 C  CA  . TYR   E 533 ? 1.2426 1.3494 1.3015 0.0159  -0.0730 -0.0563 837  TYR   E CA  
15207 C  C   . TYR   E 533 ? 1.2640 1.3594 1.3062 0.0162  -0.0716 -0.0552 837  TYR   E C   
15208 O  O   . TYR   E 533 ? 1.3134 1.4019 1.3452 0.0160  -0.0741 -0.0544 837  TYR   E O   
15209 C  CB  . TYR   E 533 ? 1.2863 1.3960 1.3527 0.0221  -0.0779 -0.0599 837  TYR   E CB  
15210 C  CG  . TYR   E 533 ? 1.2259 1.3454 1.3077 0.0220  -0.0809 -0.0613 837  TYR   E CG  
15211 C  CD1 . TYR   E 533 ? 1.2397 1.3688 1.3369 0.0205  -0.0781 -0.0618 837  TYR   E CD1 
15212 C  CD2 . TYR   E 533 ? 1.2189 1.3374 1.2995 0.0235  -0.0864 -0.0622 837  TYR   E CD2 
15213 C  CE1 . TYR   E 533 ? 1.2923 1.4300 1.4040 0.0201  -0.0811 -0.0631 837  TYR   E CE1 
15214 C  CE2 . TYR   E 533 ? 1.2516 1.3783 1.3457 0.0235  -0.0896 -0.0637 837  TYR   E CE2 
15215 C  CZ  . TYR   E 533 ? 1.2940 1.4305 1.4041 0.0216  -0.0871 -0.0642 837  TYR   E CZ  
15216 O  OH  . TYR   E 533 ? 1.2669 1.4112 1.3908 0.0214  -0.0905 -0.0658 837  TYR   E OH  
15217 N  N   . PRO   E 534 ? 1.2799 1.3728 1.3191 0.0170  -0.0677 -0.0552 838  PRO   E N   
15218 C  CA  . PRO   E 534 ? 1.3197 1.4013 1.3427 0.0166  -0.0663 -0.0540 838  PRO   E CA  
15219 C  C   . PRO   E 534 ? 1.3462 1.4202 1.3601 0.0205  -0.0701 -0.0551 838  PRO   E C   
15220 O  O   . PRO   E 534 ? 1.3349 1.4004 1.3364 0.0183  -0.0704 -0.0534 838  PRO   E O   
15221 C  CB  . PRO   E 534 ? 1.3340 1.4153 1.3579 0.0192  -0.0623 -0.0550 838  PRO   E CB  
15222 C  CG  . PRO   E 534 ? 1.3162 1.4084 1.3555 0.0181  -0.0599 -0.0552 838  PRO   E CG  
15223 C  CD  . PRO   E 534 ? 1.2651 1.3648 1.3156 0.0189  -0.0645 -0.0566 838  PRO   E CD  
15224 N  N   . GLU   E 535 ? 1.3103 1.3874 1.3307 0.0264  -0.0732 -0.0581 839  GLU   E N   
15225 C  CA  . GLU   E 535 ? 1.3144 1.3838 1.3258 0.0312  -0.0771 -0.0595 839  GLU   E CA  
15226 C  C   . GLU   E 535 ? 1.2886 1.3547 1.2942 0.0286  -0.0796 -0.0577 839  GLU   E C   
15227 O  O   . GLU   E 535 ? 1.3042 1.3600 1.2961 0.0284  -0.0795 -0.0563 839  GLU   E O   
15228 C  CB  . GLU   E 535 ? 1.3326 1.4075 1.3544 0.0378  -0.0808 -0.0632 839  GLU   E CB  
15229 N  N   . GLU   E 536 ? 1.2450 1.3192 1.2607 0.0266  -0.0813 -0.0575 840  GLU   E N   
15230 C  CA  . GLU   E 536 ? 1.2144 1.2860 1.2256 0.0250  -0.0838 -0.0561 840  GLU   E CA  
15231 C  C   . GLU   E 536 ? 1.1621 1.2308 1.1670 0.0180  -0.0804 -0.0523 840  GLU   E C   
15232 O  O   . GLU   E 536 ? 1.1858 1.2605 1.1971 0.0135  -0.0777 -0.0511 840  GLU   E O   
15233 C  CB  . GLU   E 536 ? 1.1682 1.2491 1.1924 0.0258  -0.0872 -0.0575 840  GLU   E CB  
15234 N  N   . ALA   E 537 ? 1.1721 1.2315 1.1646 0.0174  -0.0805 -0.0506 841  ALA   E N   
15235 C  CA  . ALA   E 537 ? 1.0398 1.0954 1.0260 0.0110  -0.0775 -0.0473 841  ALA   E CA  
15236 C  C   . ALA   E 537 ? 1.0419 1.1029 1.0335 0.0066  -0.0779 -0.0453 841  ALA   E C   
15237 O  O   . ALA   E 537 ? 1.0492 1.1145 1.0445 0.0013  -0.0758 -0.0436 841  ALA   E O   
15238 C  CB  . ALA   E 537 ? 1.1108 1.1540 1.0825 0.0118  -0.0769 -0.0461 841  ALA   E CB  
15239 N  N   . GLU   E 538 ? 1.1311 1.1916 1.1224 0.0092  -0.0807 -0.0455 842  GLU   E N   
15240 C  CA  . GLU   E 538 ? 1.1337 1.1991 1.1299 0.0064  -0.0816 -0.0440 842  GLU   E CA  
15241 C  C   . GLU   E 538 ? 1.1403 1.2159 1.1497 0.0083  -0.0843 -0.0463 842  GLU   E C   
15242 O  O   . GLU   E 538 ? 1.1581 1.2350 1.1712 0.0136  -0.0868 -0.0493 842  GLU   E O   
15243 C  CB  . GLU   E 538 ? 1.1691 1.2272 1.1568 0.0089  -0.0831 -0.0431 842  GLU   E CB  
15244 C  CG  . GLU   E 538 ? 1.2867 1.3390 1.2668 0.0039  -0.0801 -0.0395 842  GLU   E CG  
15245 C  CD  . GLU   E 538 ? 1.4899 1.5303 1.4571 0.0073  -0.0798 -0.0388 842  GLU   E CD  
15246 O  OE1 . GLU   E 538 ? 1.4469 1.4844 1.4112 0.0133  -0.0825 -0.0404 842  GLU   E OE1 
15247 O  OE2 . GLU   E 538 ? 1.5373 1.5708 1.4971 0.0041  -0.0769 -0.0367 842  GLU   E OE2 
15248 N  N   . PRO   E 539 ? 1.2037 1.2862 1.2205 0.0041  -0.0839 -0.0448 843  PRO   E N   
15249 C  CA  . PRO   E 539 ? 1.1574 1.2497 1.1875 0.0050  -0.0861 -0.0467 843  PRO   E CA  
15250 C  C   . PRO   E 539 ? 1.1649 1.2563 1.1951 0.0096  -0.0907 -0.0483 843  PRO   E C   
15251 O  O   . PRO   E 539 ? 1.1151 1.2042 1.1412 0.0084  -0.0912 -0.0464 843  PRO   E O   
15252 C  CB  . PRO   E 539 ? 1.0853 1.1832 1.1204 -0.0015 -0.0838 -0.0441 843  PRO   E CB  
15253 C  CG  . PRO   E 539 ? 1.0767 1.1679 1.1015 -0.0056 -0.0807 -0.0412 843  PRO   E CG  
15254 C  CD  . PRO   E 539 ? 1.1416 1.2230 1.1550 -0.0019 -0.0816 -0.0414 843  PRO   E CD  
15255 N  N   . LYS   E 540 ? 1.2074 1.3007 1.2428 0.0151  -0.0941 -0.0518 844  LYS   E N   
15256 C  CA  . LYS   E 540 ? 1.2515 1.3431 1.2863 0.0203  -0.0992 -0.0538 844  LYS   E CA  
15257 C  C   . LYS   E 540 ? 1.2086 1.3099 1.2578 0.0204  -0.1024 -0.0557 844  LYS   E C   
15258 O  O   . LYS   E 540 ? 1.1995 1.2993 1.2482 0.0242  -0.1070 -0.0572 844  LYS   E O   
15259 C  CB  . LYS   E 540 ? 1.2652 1.3506 1.2944 0.0274  -0.1020 -0.0567 844  LYS   E CB  
15260 C  CG  . LYS   E 540 ? 1.2813 1.3544 1.2937 0.0299  -0.1018 -0.0551 844  LYS   E CG  
15261 C  CD  . LYS   E 540 ? 1.4093 1.4802 1.4186 0.0313  -0.1045 -0.0545 844  LYS   E CD  
15262 C  CE  . LYS   E 540 ? 1.4907 1.5486 1.4835 0.0357  -0.1048 -0.0535 844  LYS   E CE  
15263 N  NZ  . LYS   E 540 ? 1.2776 1.3319 1.2668 0.0409  -0.1093 -0.0548 844  LYS   E NZ  
15264 N  N   . GLN   E 541 ? 1.2264 1.3367 1.2876 0.0162  -0.1001 -0.0555 845  GLN   E N   
15265 C  CA  . GLN   E 541 ? 1.1970 1.3158 1.2717 0.0159  -0.1030 -0.0571 845  GLN   E CA  
15266 C  C   . GLN   E 541 ? 1.1354 1.2622 1.2197 0.0096  -0.0987 -0.0552 845  GLN   E C   
15267 O  O   . GLN   E 541 ? 1.1401 1.2689 1.2274 0.0082  -0.0950 -0.0551 845  GLN   E O   
15268 C  CB  . GLN   E 541 ? 1.2298 1.3520 1.3139 0.0216  -0.1076 -0.0615 845  GLN   E CB  
15269 C  CG  . GLN   E 541 ? 1.2796 1.4068 1.3721 0.0210  -0.1044 -0.0625 845  GLN   E CG  
15270 C  CD  . GLN   E 541 ? 1.3967 1.5286 1.5011 0.0263  -0.1089 -0.0670 845  GLN   E CD  
15271 O  OE1 . GLN   E 541 ? 1.4575 1.5891 1.5641 0.0304  -0.1150 -0.0696 845  GLN   E OE1 
15272 N  NE2 . GLN   E 541 ? 1.4250 1.5614 1.5374 0.0265  -0.1059 -0.0680 845  GLN   E NE2 
15273 N  N   . GLY   E 542 ? 1.1368 1.2673 1.2253 0.0062  -0.0990 -0.0538 846  GLY   E N   
15274 C  CA  . GLY   E 542 ? 1.1313 1.2693 1.2295 0.0009  -0.0955 -0.0523 846  GLY   E CA  
15275 C  C   . GLY   E 542 ? 1.1359 1.2799 1.2445 0.0006  -0.0989 -0.0534 846  GLY   E C   
15276 O  O   . GLY   E 542 ? 1.1492 1.2916 1.2577 0.0050  -0.1042 -0.0557 846  GLY   E O   
15277 N  N   . ARG   E 543 ? 1.1416 1.2918 1.2584 -0.0042 -0.0962 -0.0518 847  ARG   E N   
15278 C  CA  . ARG   E 543 ? 1.0756 1.2309 1.2021 -0.0045 -0.0995 -0.0529 847  ARG   E CA  
15279 C  C   . ARG   E 543 ? 1.0581 1.2151 1.1835 -0.0101 -0.0965 -0.0494 847  ARG   E C   
15280 O  O   . ARG   E 543 ? 1.0620 1.2184 1.1833 -0.0140 -0.0916 -0.0467 847  ARG   E O   
15281 C  CB  . ARG   E 543 ? 1.0696 1.2329 1.2132 -0.0035 -0.1005 -0.0559 847  ARG   E CB  
15282 C  CG  . ARG   E 543 ? 1.0559 1.2241 1.2072 -0.0070 -0.0944 -0.0547 847  ARG   E CG  
15283 C  CD  . ARG   E 543 ? 1.0843 1.2598 1.2531 -0.0049 -0.0956 -0.0581 847  ARG   E CD  
15284 N  NE  . ARG   E 543 ? 1.1516 1.3341 1.3334 -0.0090 -0.0925 -0.0571 847  ARG   E NE  
15285 C  CZ  . ARG   E 543 ? 1.1587 1.3447 1.3470 -0.0115 -0.0863 -0.0559 847  ARG   E CZ  
15286 N  NH1 . ARG   E 543 ? 1.1423 1.3263 1.3270 -0.0100 -0.0828 -0.0559 847  ARG   E NH1 
15287 N  NH2 . ARG   E 543 ? 1.0773 1.2684 1.2756 -0.0154 -0.0833 -0.0546 847  ARG   E NH2 
15288 N  N   . ILE   E 544 ? 1.0582 1.2167 1.1866 -0.0100 -0.0999 -0.0497 848  ILE   E N   
15289 C  CA  . ILE   E 544 ? 1.0178 1.1797 1.1492 -0.0149 -0.0977 -0.0471 848  ILE   E CA  
15290 C  C   . ILE   E 544 ? 1.0107 1.1802 1.1581 -0.0157 -0.0983 -0.0490 848  ILE   E C   
15291 O  O   . ILE   E 544 ? 1.0301 1.2016 1.1854 -0.0120 -0.1030 -0.0524 848  ILE   E O   
15292 C  CB  . ILE   E 544 ? 0.9742 1.1326 1.0985 -0.0144 -0.1006 -0.0460 848  ILE   E CB  
15293 C  CG1 . ILE   E 544 ? 1.0199 1.1708 1.1293 -0.0136 -0.0994 -0.0440 848  ILE   E CG1 
15294 C  CG2 . ILE   E 544 ? 0.9614 1.1237 1.0897 -0.0191 -0.0987 -0.0436 848  ILE   E CG2 
15295 C  CD1 . ILE   E 544 ? 1.0019 1.1487 1.1035 -0.0128 -0.1012 -0.0425 848  ILE   E CD1 
15296 N  N   . VAL   E 545 ? 1.0048 1.1781 1.1573 -0.0203 -0.0935 -0.0469 849  VAL   E N   
15297 C  CA  . VAL   E 545 ? 0.9835 1.1638 1.1515 -0.0216 -0.0930 -0.0482 849  VAL   E CA  
15298 C  C   . VAL   E 545 ? 0.9859 1.1680 1.1551 -0.0258 -0.0916 -0.0457 849  VAL   E C   
15299 O  O   . VAL   E 545 ? 0.9851 1.1643 1.1448 -0.0288 -0.0884 -0.0425 849  VAL   E O   
15300 C  CB  . VAL   E 545 ? 1.0330 1.2163 1.2076 -0.0227 -0.0877 -0.0482 849  VAL   E CB  
15301 C  CG1 . VAL   E 545 ? 1.0371 1.2273 1.2278 -0.0248 -0.0862 -0.0489 849  VAL   E CG1 
15302 C  CG2 . VAL   E 545 ? 1.0511 1.2334 1.2264 -0.0181 -0.0896 -0.0511 849  VAL   E CG2 
15303 N  N   . VAL   E 546 ? 1.0768 1.2633 1.2578 -0.0259 -0.0942 -0.0474 850  VAL   E N   
15304 C  CA  . VAL   E 546 ? 1.0800 1.2685 1.2638 -0.0296 -0.0930 -0.0454 850  VAL   E CA  
15305 C  C   . VAL   E 546 ? 1.0513 1.2455 1.2491 -0.0323 -0.0891 -0.0454 850  VAL   E C   
15306 O  O   . VAL   E 546 ? 1.0623 1.2606 1.2733 -0.0305 -0.0911 -0.0485 850  VAL   E O   
15307 C  CB  . VAL   E 546 ? 1.0353 1.2235 1.2208 -0.0277 -0.0992 -0.0470 850  VAL   E CB  
15308 C  CG1 . VAL   E 546 ? 0.9875 1.1776 1.1759 -0.0317 -0.0975 -0.0447 850  VAL   E CG1 
15309 C  CG2 . VAL   E 546 ? 1.0487 1.2305 1.2200 -0.0246 -0.1026 -0.0468 850  VAL   E CG2 
15310 N  N   . PHE   E 547 ? 1.0779 1.2720 1.2730 -0.0364 -0.0835 -0.0420 851  PHE   E N   
15311 C  CA  . PHE   E 547 ? 1.0882 1.2866 1.2951 -0.0392 -0.0788 -0.0414 851  PHE   E CA  
15312 C  C   . PHE   E 547 ? 1.1171 1.3161 1.3255 -0.0423 -0.0787 -0.0396 851  PHE   E C   
15313 O  O   . PHE   E 547 ? 1.0810 1.2770 1.2801 -0.0427 -0.0813 -0.0382 851  PHE   E O   
15314 C  CB  . PHE   E 547 ? 1.0404 1.2371 1.2425 -0.0410 -0.0717 -0.0390 851  PHE   E CB  
15315 C  CG  . PHE   E 547 ? 1.0729 1.2685 1.2727 -0.0380 -0.0711 -0.0405 851  PHE   E CG  
15316 C  CD1 . PHE   E 547 ? 1.0586 1.2488 1.2437 -0.0367 -0.0723 -0.0398 851  PHE   E CD1 
15317 C  CD2 . PHE   E 547 ? 1.1035 1.3033 1.3161 -0.0365 -0.0692 -0.0426 851  PHE   E CD2 
15318 C  CE1 . PHE   E 547 ? 1.0460 1.2346 1.2284 -0.0339 -0.0717 -0.0412 851  PHE   E CE1 
15319 C  CE2 . PHE   E 547 ? 1.0722 1.2709 1.2825 -0.0335 -0.0685 -0.0440 851  PHE   E CE2 
15320 C  CZ  . PHE   E 547 ? 1.0525 1.2453 1.2472 -0.0321 -0.0699 -0.0433 851  PHE   E CZ  
15321 N  N   . GLN   E 548 ? 1.1964 1.3992 1.4172 -0.0445 -0.0753 -0.0394 852  GLN   E N   
15322 C  CA  . GLN   E 548 ? 1.2001 1.4031 1.4224 -0.0479 -0.0735 -0.0372 852  GLN   E CA  
15323 C  C   . GLN   E 548 ? 1.1960 1.4004 1.4246 -0.0506 -0.0658 -0.0352 852  GLN   E C   
15324 O  O   . GLN   E 548 ? 1.1584 1.3663 1.3985 -0.0498 -0.0634 -0.0368 852  GLN   E O   
15325 C  CB  . GLN   E 548 ? 1.2043 1.4102 1.4374 -0.0473 -0.0790 -0.0396 852  GLN   E CB  
15326 C  CG  . GLN   E 548 ? 1.2675 1.4718 1.4967 -0.0498 -0.0794 -0.0374 852  GLN   E CG  
15327 C  CD  . GLN   E 548 ? 1.2538 1.4613 1.4972 -0.0503 -0.0823 -0.0395 852  GLN   E CD  
15328 O  OE1 . GLN   E 548 ? 1.2249 1.4365 1.4825 -0.0493 -0.0833 -0.0424 852  GLN   E OE1 
15329 N  NE2 . GLN   E 548 ? 1.2426 1.4485 1.4829 -0.0519 -0.0838 -0.0381 852  GLN   E NE2 
15330 N  N   . TYR   E 549 ? 1.2319 1.4331 1.4523 -0.0535 -0.0619 -0.0317 853  TYR   E N   
15331 C  CA  . TYR   E 549 ? 1.3500 1.5511 1.5742 -0.0559 -0.0542 -0.0294 853  TYR   E CA  
15332 C  C   . TYR   E 549 ? 1.3792 1.5809 1.6089 -0.0586 -0.0536 -0.0281 853  TYR   E C   
15333 O  O   . TYR   E 549 ? 1.3433 1.5423 1.5638 -0.0595 -0.0560 -0.0265 853  TYR   E O   
15334 C  CB  . TYR   E 549 ? 1.2411 1.4368 1.4500 -0.0566 -0.0496 -0.0263 853  TYR   E CB  
15335 C  CG  . TYR   E 549 ? 1.2083 1.4024 1.4189 -0.0585 -0.0415 -0.0238 853  TYR   E CG  
15336 C  CD1 . TYR   E 549 ? 1.2755 1.4717 1.4953 -0.0576 -0.0365 -0.0246 853  TYR   E CD1 
15337 C  CD2 . TYR   E 549 ? 1.1988 1.3890 1.4019 -0.0609 -0.0387 -0.0206 853  TYR   E CD2 
15338 C  CE1 . TYR   E 549 ? 1.3061 1.5000 1.5268 -0.0590 -0.0283 -0.0220 853  TYR   E CE1 
15339 C  CE2 . TYR   E 549 ? 1.2197 1.4073 1.4230 -0.0622 -0.0310 -0.0182 853  TYR   E CE2 
15340 C  CZ  . TYR   E 549 ? 1.2420 1.4313 1.4540 -0.0613 -0.0255 -0.0187 853  TYR   E CZ  
15341 O  OH  . TYR   E 549 ? 1.1809 1.3668 1.3925 -0.0623 -0.0171 -0.0160 853  TYR   E OH  
15342 N  N   . SER   E 550 ? 1.5403 1.7456 1.7854 -0.0597 -0.0503 -0.0287 854  SER   E N   
15343 C  CA  . SER   E 550 ? 1.6116 1.8176 1.8635 -0.0621 -0.0504 -0.0279 854  SER   E CA  
15344 C  C   . SER   E 550 ? 1.6570 1.8653 1.9236 -0.0641 -0.0438 -0.0273 854  SER   E C   
15345 O  O   . SER   E 550 ? 1.6756 1.8855 1.9521 -0.0659 -0.0446 -0.0276 854  SER   E O   
15346 C  CB  . SER   E 550 ? 1.5927 1.8014 1.8508 -0.0607 -0.0591 -0.0313 854  SER   E CB  
15347 O  OG  . SER   E 550 ? 1.5332 1.7456 1.7993 -0.0578 -0.0627 -0.0349 854  SER   E OG  
15348 N  N   . ASP   E 551 ? 1.5807 1.7889 1.8488 -0.0639 -0.0369 -0.0263 855  ASP   E N   
15349 C  CA  . ASP   E 551 ? 1.6249 1.8366 1.9104 -0.0652 -0.0310 -0.0264 855  ASP   E CA  
15350 C  C   . ASP   E 551 ? 1.5553 1.7660 1.8395 -0.0642 -0.0232 -0.0251 855  ASP   E C   
15351 O  O   . ASP   E 551 ? 1.6083 1.8235 1.9083 -0.0639 -0.0194 -0.0263 855  ASP   E O   
15352 C  CB  . ASP   E 551 ? 1.6974 1.9161 2.0014 -0.0641 -0.0371 -0.0309 855  ASP   E CB  
15353 C  CG  . ASP   E 551 ? 1.6914 1.9120 1.9925 -0.0604 -0.0431 -0.0341 855  ASP   E CG  
15354 O  OD1 . ASP   E 551 ? 1.7302 1.9554 2.0432 -0.0588 -0.0497 -0.0381 855  ASP   E OD1 
15355 O  OD2 . ASP   E 551 ? 1.7073 1.9242 1.9935 -0.0590 -0.0414 -0.0327 855  ASP   E OD2 
15356 N  N   . GLY   E 552 ? 1.4695 1.6742 1.7349 -0.0634 -0.0211 -0.0227 856  GLY   E N   
15357 C  CA  . GLY   E 552 ? 1.5524 1.7548 1.8131 -0.0619 -0.0145 -0.0215 856  GLY   E CA  
15358 C  C   . GLY   E 552 ? 1.5688 1.7747 1.8326 -0.0588 -0.0179 -0.0247 856  GLY   E C   
15359 O  O   . GLY   E 552 ? 1.4435 1.6469 1.7015 -0.0572 -0.0130 -0.0239 856  GLY   E O   
15360 N  N   . LYS   E 553 ? 1.7515 1.9624 2.0237 -0.0576 -0.0261 -0.0284 857  LYS   E N   
15361 C  CA  . LYS   E 553 ? 1.7138 1.9276 1.9885 -0.0543 -0.0299 -0.0316 857  LYS   E CA  
15362 C  C   . LYS   E 553 ? 1.7018 1.9145 1.9670 -0.0528 -0.0392 -0.0334 857  LYS   E C   
15363 O  O   . LYS   E 553 ? 1.6682 1.8805 1.9316 -0.0542 -0.0437 -0.0333 857  LYS   E O   
15364 C  CB  . LYS   E 553 ? 1.7065 1.9281 2.0041 -0.0534 -0.0302 -0.0348 857  LYS   E CB  
15365 N  N   . LEU   E 554 ? 1.4782 1.6898 1.7364 -0.0498 -0.0417 -0.0349 858  LEU   E N   
15366 C  CA  . LEU   E 554 ? 1.3948 1.6052 1.6449 -0.0477 -0.0500 -0.0369 858  LEU   E CA  
15367 C  C   . LEU   E 554 ? 1.3553 1.5714 1.6206 -0.0454 -0.0564 -0.0413 858  LEU   E C   
15368 O  O   . LEU   E 554 ? 1.3868 1.6072 1.6648 -0.0437 -0.0549 -0.0434 858  LEU   E O   
15369 C  CB  . LEU   E 554 ? 1.2255 1.4316 1.4618 -0.0455 -0.0493 -0.0366 858  LEU   E CB  
15370 C  CG  . LEU   E 554 ? 1.1854 1.3858 1.4033 -0.0454 -0.0529 -0.0353 858  LEU   E CG  
15371 C  CD1 . LEU   E 554 ? 1.1979 1.3953 1.4080 -0.0488 -0.0513 -0.0321 858  LEU   E CD1 
15372 C  CD2 . LEU   E 554 ? 1.1667 1.3628 1.3736 -0.0439 -0.0495 -0.0345 858  LEU   E CD2 
15373 N  N   . GLN   E 555 ? 1.2481 1.4641 1.5121 -0.0450 -0.0637 -0.0427 859  GLN   E N   
15374 C  CA  . GLN   E 555 ? 1.2520 1.4718 1.5271 -0.0420 -0.0711 -0.0472 859  GLN   E CA  
15375 C  C   . GLN   E 555 ? 1.1614 1.3772 1.4227 -0.0385 -0.0773 -0.0485 859  GLN   E C   
15376 O  O   . GLN   E 555 ? 1.1387 1.3499 1.3861 -0.0392 -0.0790 -0.0466 859  GLN   E O   
15377 C  CB  . GLN   E 555 ? 1.2494 1.4717 1.5347 -0.0436 -0.0751 -0.0483 859  GLN   E CB  
15378 N  N   . THR   E 556 ? 1.1237 1.3409 1.3888 -0.0346 -0.0803 -0.0517 860  THR   E N   
15379 C  CA  . THR   E 556 ? 1.1427 1.3557 1.3959 -0.0307 -0.0866 -0.0534 860  THR   E CA  
15380 C  C   . THR   E 556 ? 1.0805 1.2935 1.3369 -0.0292 -0.0946 -0.0559 860  THR   E C   
15381 O  O   . THR   E 556 ? 1.0439 1.2615 1.3156 -0.0278 -0.0987 -0.0594 860  THR   E O   
15382 C  CB  . THR   E 556 ? 1.1320 1.3460 1.3883 -0.0266 -0.0877 -0.0561 860  THR   E CB  
15383 O  OG1 . THR   E 556 ? 1.1385 1.3523 1.3927 -0.0280 -0.0798 -0.0538 860  THR   E OG1 
15384 C  CG2 . THR   E 556 ? 1.0970 1.3050 1.3382 -0.0226 -0.0933 -0.0573 860  THR   E CG2 
15385 N  N   . VAL   E 557 ? 1.0923 1.3004 1.3347 -0.0295 -0.0969 -0.0541 861  VAL   E N   
15386 C  CA  . VAL   E 557 ? 1.0852 1.2922 1.3285 -0.0278 -0.1041 -0.0562 861  VAL   E CA  
15387 C  C   . VAL   E 557 ? 1.1254 1.3285 1.3613 -0.0222 -0.1109 -0.0592 861  VAL   E C   
15388 O  O   . VAL   E 557 ? 1.1749 1.3779 1.4155 -0.0192 -0.1180 -0.0624 861  VAL   E O   
15389 C  CB  . VAL   E 557 ? 1.0155 1.2193 1.2484 -0.0307 -0.1029 -0.0527 861  VAL   E CB  
15390 C  CG1 . VAL   E 557 ? 1.0473 1.2488 1.2785 -0.0282 -0.1103 -0.0547 861  VAL   E CG1 
15391 C  CG2 . VAL   E 557 ? 1.0512 1.2583 1.2920 -0.0358 -0.0971 -0.0502 861  VAL   E CG2 
15392 N  N   . ALA   E 558 ? 1.1064 1.3057 1.3304 -0.0203 -0.1092 -0.0582 862  ALA   E N   
15393 C  CA  . ALA   E 558 ? 1.1098 1.3040 1.3245 -0.0149 -0.1152 -0.0606 862  ALA   E CA  
15394 C  C   . ALA   E 558 ? 1.0891 1.2797 1.2929 -0.0138 -0.1116 -0.0592 862  ALA   E C   
15395 O  O   . ALA   E 558 ? 1.0726 1.2627 1.2707 -0.0175 -0.1052 -0.0557 862  ALA   E O   
15396 C  CB  . ALA   E 558 ? 1.0795 1.2683 1.2824 -0.0141 -0.1187 -0.0594 862  ALA   E CB  
15397 N  N   . GLU   E 559 ? 1.1184 1.3061 1.3190 -0.0086 -0.1160 -0.0621 863  GLU   E N   
15398 C  CA  . GLU   E 559 ? 1.1316 1.3146 1.3200 -0.0071 -0.1132 -0.0609 863  GLU   E CA  
15399 C  C   . GLU   E 559 ? 1.1245 1.3005 1.3017 -0.0013 -0.1191 -0.0629 863  GLU   E C   
15400 O  O   . GLU   E 559 ? 1.1913 1.3679 1.3750 0.0033  -0.1251 -0.0670 863  GLU   E O   
15401 C  CB  . GLU   E 559 ? 1.1491 1.3363 1.3468 -0.0068 -0.1099 -0.0621 863  GLU   E CB  
15402 C  CG  . GLU   E 559 ? 1.2348 1.4261 1.4465 -0.0026 -0.1152 -0.0669 863  GLU   E CG  
15403 C  CD  . GLU   E 559 ? 1.3816 1.5774 1.6029 -0.0024 -0.1111 -0.0678 863  GLU   E CD  
15404 O  OE1 . GLU   E 559 ? 1.3264 1.5182 1.5381 -0.0003 -0.1092 -0.0674 863  GLU   E OE1 
15405 O  OE2 . GLU   E 559 ? 1.4727 1.6760 1.7114 -0.0044 -0.1093 -0.0687 863  GLU   E OE2 
15406 N  N   . LYS   E 560 ? 1.0727 1.2418 1.2333 -0.0014 -0.1173 -0.0600 864  LYS   E N   
15407 C  CA  . LYS   E 560 ? 1.0861 1.2471 1.2336 0.0039  -0.1215 -0.0611 864  LYS   E CA  
15408 C  C   . LYS   E 560 ? 1.0914 1.2480 1.2297 0.0052  -0.1184 -0.0603 864  LYS   E C   
15409 O  O   . LYS   E 560 ? 1.1249 1.2796 1.2554 0.0014  -0.1129 -0.0567 864  LYS   E O   
15410 C  CB  . LYS   E 560 ? 1.0652 1.2211 1.2012 0.0030  -0.1216 -0.0583 864  LYS   E CB  
15411 C  CG  . LYS   E 560 ? 1.0835 1.2300 1.2050 0.0087  -0.1253 -0.0590 864  LYS   E CG  
15412 C  CD  . LYS   E 560 ? 1.0528 1.1960 1.1704 0.0111  -0.1298 -0.0594 864  LYS   E CD  
15413 C  CE  . LYS   E 560 ? 1.1381 1.2732 1.2470 0.0190  -0.1360 -0.0626 864  LYS   E CE  
15414 N  NZ  . LYS   E 560 ? 1.1110 1.2402 1.2121 0.0226  -0.1402 -0.0629 864  LYS   E NZ  
15415 N  N   . GLU   E 561 ? 1.0861 1.2408 1.2251 0.0107  -0.1223 -0.0637 865  GLU   E N   
15416 C  CA  . GLU   E 561 ? 1.1314 1.2811 1.2612 0.0127  -0.1199 -0.0633 865  GLU   E CA  
15417 C  C   . GLU   E 561 ? 1.1917 1.3314 1.3030 0.0146  -0.1200 -0.0613 865  GLU   E C   
15418 O  O   . GLU   E 561 ? 1.2158 1.3506 1.3215 0.0188  -0.1250 -0.0626 865  GLU   E O   
15419 C  CB  . GLU   E 561 ? 1.1848 1.3356 1.3214 0.0184  -0.1244 -0.0679 865  GLU   E CB  
15420 C  CG  . GLU   E 561 ? 1.3001 1.4425 1.4234 0.0231  -0.1248 -0.0684 865  GLU   E CG  
15421 C  CD  . GLU   E 561 ? 1.4279 1.5714 1.5583 0.0293  -0.1301 -0.0732 865  GLU   E CD  
15422 O  OE1 . GLU   E 561 ? 1.4445 1.5923 1.5863 0.0318  -0.1360 -0.0767 865  GLU   E OE1 
15423 O  OE2 . GLU   E 561 ? 1.4668 1.6068 1.5917 0.0319  -0.1286 -0.0736 865  GLU   E OE2 
15424 N  N   . VAL   E 562 ? 1.2159 1.3521 1.3179 0.0116  -0.1144 -0.0580 866  VAL   E N   
15425 C  CA  . VAL   E 562 ? 1.1443 1.2710 1.2296 0.0129  -0.1134 -0.0557 866  VAL   E CA  
15426 C  C   . VAL   E 562 ? 1.1275 1.2485 1.2053 0.0161  -0.1125 -0.0565 866  VAL   E C   
15427 O  O   . VAL   E 562 ? 1.0806 1.2054 1.1649 0.0157  -0.1109 -0.0577 866  VAL   E O   
15428 C  CB  . VAL   E 562 ? 1.1055 1.2320 1.1857 0.0067  -0.1080 -0.0511 866  VAL   E CB  
15429 C  CG1 . VAL   E 562 ? 1.1420 1.2712 1.2255 0.0049  -0.1096 -0.0501 866  VAL   E CG1 
15430 C  CG2 . VAL   E 562 ? 1.1250 1.2569 1.2115 0.0015  -0.1031 -0.0497 866  VAL   E CG2 
15431 N  N   . LYS   E 563 ? 1.1190 1.2304 1.1824 0.0196  -0.1133 -0.0557 867  LYS   E N   
15432 C  CA  . LYS   E 563 ? 1.1056 1.2098 1.1597 0.0231  -0.1126 -0.0563 867  LYS   E CA  
15433 C  C   . LYS   E 563 ? 1.1105 1.2110 1.1562 0.0183  -0.1064 -0.0525 867  LYS   E C   
15434 O  O   . LYS   E 563 ? 1.2187 1.3101 1.2516 0.0204  -0.1052 -0.0514 867  LYS   E O   
15435 C  CB  . LYS   E 563 ? 1.1361 1.2307 1.1787 0.0300  -0.1169 -0.0577 867  LYS   E CB  
15436 N  N   . GLY   E 564 ? 1.1210 1.2281 1.1736 0.0120  -0.1025 -0.0505 868  GLY   E N   
15437 C  CA  . GLY   E 564 ? 1.1135 1.2172 1.1587 0.0073  -0.0973 -0.0471 868  GLY   E CA  
15438 C  C   . GLY   E 564 ? 1.1106 1.2220 1.1647 0.0014  -0.0939 -0.0458 868  GLY   E C   
15439 O  O   . GLY   E 564 ? 1.1048 1.2231 1.1700 0.0018  -0.0946 -0.0479 868  GLY   E O   
15440 N  N   . ALA   E 565 ? 1.1093 1.2193 1.1587 -0.0039 -0.0902 -0.0424 869  ALA   E N   
15441 C  CA  . ALA   E 565 ? 1.0423 1.1580 1.0977 -0.0093 -0.0869 -0.0410 869  ALA   E CA  
15442 C  C   . ALA   E 565 ? 1.0966 1.2152 1.1538 -0.0135 -0.0864 -0.0384 869  ALA   E C   
15443 O  O   . ALA   E 565 ? 1.0839 1.1979 1.1333 -0.0153 -0.0854 -0.0360 869  ALA   E O   
15444 C  CB  . ALA   E 565 ? 1.0036 1.1142 1.0513 -0.0116 -0.0834 -0.0395 869  ALA   E CB  
15445 N  N   . VAL   E 566 ? 1.0089 1.1353 1.0768 -0.0152 -0.0868 -0.0389 870  VAL   E N   
15446 C  CA  . VAL   E 566 ? 1.0309 1.1604 1.1007 -0.0194 -0.0861 -0.0365 870  VAL   E CA  
15447 C  C   . VAL   E 566 ? 1.0485 1.1764 1.1137 -0.0243 -0.0823 -0.0338 870  VAL   E C   
15448 O  O   . VAL   E 566 ? 1.0823 1.2131 1.1513 -0.0265 -0.0800 -0.0338 870  VAL   E O   
15449 C  CB  . VAL   E 566 ? 1.0572 1.1947 1.1393 -0.0202 -0.0871 -0.0376 870  VAL   E CB  
15450 C  CG1 . VAL   E 566 ? 1.0424 1.1821 1.1254 -0.0231 -0.0874 -0.0354 870  VAL   E CG1 
15451 C  CG2 . VAL   E 566 ? 1.0791 1.2185 1.1676 -0.0151 -0.0911 -0.0411 870  VAL   E CG2 
15452 N  N   . TYR   E 567 ? 1.0180 1.1410 1.0751 -0.0260 -0.0816 -0.0315 871  TYR   E N   
15453 C  CA  . TYR   E 567 ? 1.0164 1.1380 1.0698 -0.0308 -0.0788 -0.0291 871  TYR   E CA  
15454 C  C   . TYR   E 567 ? 1.0018 1.1279 1.0593 -0.0349 -0.0784 -0.0270 871  TYR   E C   
15455 O  O   . TYR   E 567 ? 1.0999 1.2266 1.1568 -0.0388 -0.0766 -0.0257 871  TYR   E O   
15456 C  CB  . TYR   E 567 ? 1.0808 1.1946 1.1242 -0.0312 -0.0780 -0.0277 871  TYR   E CB  
15457 C  CG  . TYR   E 567 ? 1.0930 1.2008 1.1304 -0.0279 -0.0778 -0.0293 871  TYR   E CG  
15458 C  CD1 . TYR   E 567 ? 1.0525 1.1595 1.0891 -0.0285 -0.0762 -0.0302 871  TYR   E CD1 
15459 C  CD2 . TYR   E 567 ? 1.1113 1.2135 1.1429 -0.0238 -0.0790 -0.0299 871  TYR   E CD2 
15460 C  CE1 . TYR   E 567 ? 1.0826 1.1840 1.1135 -0.0253 -0.0760 -0.0317 871  TYR   E CE1 
15461 C  CE2 . TYR   E 567 ? 1.1077 1.2039 1.1332 -0.0206 -0.0789 -0.0314 871  TYR   E CE2 
15462 C  CZ  . TYR   E 567 ? 1.1191 1.2152 1.1446 -0.0214 -0.0775 -0.0323 871  TYR   E CZ  
15463 O  OH  . TYR   E 567 ? 1.1086 1.1984 1.1276 -0.0179 -0.0774 -0.0338 871  TYR   E OH  
15464 N  N   . SER   E 568 ? 1.0183 1.1471 1.0790 -0.0340 -0.0802 -0.0267 872  SER   E N   
15465 C  CA  . SER   E 568 ? 1.0534 1.1862 1.1175 -0.0377 -0.0799 -0.0246 872  SER   E CA  
15466 C  C   . SER   E 568 ? 1.0549 1.1919 1.1253 -0.0355 -0.0822 -0.0256 872  SER   E C   
15467 O  O   . SER   E 568 ? 1.1043 1.2391 1.1732 -0.0313 -0.0844 -0.0270 872  SER   E O   
15468 C  CB  . SER   E 568 ? 1.0507 1.1798 1.1089 -0.0400 -0.0791 -0.0220 872  SER   E CB  
15469 O  OG  . SER   E 568 ? 1.0897 1.2164 1.1443 -0.0436 -0.0773 -0.0208 872  SER   E OG  
15470 N  N   . MET   E 569 ? 1.0246 1.1671 1.1014 -0.0381 -0.0820 -0.0249 873  MET   E N   
15471 C  CA  . MET   E 569 ? 1.0393 1.1855 1.1218 -0.0367 -0.0843 -0.0254 873  MET   E CA  
15472 C  C   . MET   E 569 ? 1.0169 1.1655 1.1001 -0.0403 -0.0835 -0.0228 873  MET   E C   
15473 O  O   . MET   E 569 ? 1.0653 1.2156 1.1495 -0.0440 -0.0817 -0.0214 873  MET   E O   
15474 C  CB  . MET   E 569 ? 0.9371 1.0881 1.0288 -0.0356 -0.0851 -0.0278 873  MET   E CB  
15475 C  CG  . MET   E 569 ? 0.9293 1.0789 1.0223 -0.0308 -0.0875 -0.0310 873  MET   E CG  
15476 S  SD  . MET   E 569 ? 0.9957 1.1505 1.0994 -0.0305 -0.0866 -0.0335 873  MET   E SD  
15477 C  CE  . MET   E 569 ? 1.0253 1.1851 1.1348 -0.0356 -0.0839 -0.0312 873  MET   E CE  
15478 N  N   . VAL   E 570 ? 0.9965 1.1446 1.0787 -0.0389 -0.0851 -0.0220 874  VAL   E N   
15479 C  CA  . VAL   E 570 ? 1.0490 1.1996 1.1325 -0.0417 -0.0846 -0.0196 874  VAL   E CA  
15480 C  C   . VAL   E 570 ? 1.1242 1.2773 1.2121 -0.0394 -0.0871 -0.0205 874  VAL   E C   
15481 O  O   . VAL   E 570 ? 1.0968 1.2471 1.1823 -0.0353 -0.0891 -0.0217 874  VAL   E O   
15482 C  CB  . VAL   E 570 ? 1.0084 1.1554 1.0855 -0.0427 -0.0834 -0.0171 874  VAL   E CB  
15483 C  CG1 . VAL   E 570 ? 0.9780 1.1280 1.0572 -0.0453 -0.0830 -0.0147 874  VAL   E CG1 
15484 C  CG2 . VAL   E 570 ? 1.0462 1.1902 1.1191 -0.0450 -0.0814 -0.0166 874  VAL   E CG2 
15485 N  N   . GLU   E 571 ? 1.0466 1.2043 1.1404 -0.0418 -0.0871 -0.0200 875  GLU   E N   
15486 C  CA  . GLU   E 571 ? 1.0746 1.2342 1.1720 -0.0401 -0.0894 -0.0204 875  GLU   E CA  
15487 C  C   . GLU   E 571 ? 1.1159 1.2734 1.2081 -0.0396 -0.0892 -0.0181 875  GLU   E C   
15488 O  O   . GLU   E 571 ? 1.1540 1.3117 1.2441 -0.0428 -0.0871 -0.0155 875  GLU   E O   
15489 C  CB  . GLU   E 571 ? 1.1268 1.2913 1.2314 -0.0430 -0.0889 -0.0201 875  GLU   E CB  
15490 C  CG  . GLU   E 571 ? 1.1715 1.3378 1.2798 -0.0417 -0.0913 -0.0204 875  GLU   E CG  
15491 C  CD  . GLU   E 571 ? 1.2575 1.4241 1.3629 -0.0435 -0.0905 -0.0174 875  GLU   E CD  
15492 O  OE1 . GLU   E 571 ? 1.2683 1.4339 1.3694 -0.0457 -0.0884 -0.0153 875  GLU   E OE1 
15493 O  OE2 . GLU   E 571 ? 1.2736 1.4414 1.3814 -0.0425 -0.0922 -0.0174 875  GLU   E OE2 
15494 N  N   . PHE   E 572 ? 1.1417 1.2965 1.2316 -0.0355 -0.0913 -0.0190 876  PHE   E N   
15495 C  CA  . PHE   E 572 ? 1.1992 1.3504 1.2827 -0.0340 -0.0905 -0.0168 876  PHE   E CA  
15496 C  C   . PHE   E 572 ? 1.2765 1.4277 1.3608 -0.0311 -0.0928 -0.0172 876  PHE   E C   
15497 O  O   . PHE   E 572 ? 1.2534 1.4012 1.3355 -0.0264 -0.0955 -0.0194 876  PHE   E O   
15498 C  CB  . PHE   E 572 ? 1.1792 1.3244 1.2555 -0.0308 -0.0900 -0.0174 876  PHE   E CB  
15499 C  CG  . PHE   E 572 ? 1.1209 1.2618 1.1906 -0.0295 -0.0880 -0.0148 876  PHE   E CG  
15500 C  CD1 . PHE   E 572 ? 1.1227 1.2642 1.1916 -0.0334 -0.0848 -0.0119 876  PHE   E CD1 
15501 C  CD2 . PHE   E 572 ? 1.1204 1.2563 1.1847 -0.0242 -0.0893 -0.0154 876  PHE   E CD2 
15502 C  CE1 . PHE   E 572 ? 1.2036 1.3415 1.2678 -0.0324 -0.0824 -0.0094 876  PHE   E CE1 
15503 C  CE2 . PHE   E 572 ? 1.2258 1.3573 1.2839 -0.0229 -0.0867 -0.0127 876  PHE   E CE2 
15504 C  CZ  . PHE   E 572 ? 1.2624 1.3952 1.3210 -0.0271 -0.0829 -0.0096 876  PHE   E CZ  
15505 N  N   . ASN   E 573 ? 1.4157 1.5701 1.5026 -0.0335 -0.0921 -0.0152 877  ASN   E N   
15506 C  CA  . ASN   E 573 ? 1.4030 1.5574 1.4905 -0.0310 -0.0941 -0.0153 877  ASN   E CA  
15507 C  C   . ASN   E 573 ? 1.3791 1.5341 1.4711 -0.0286 -0.0980 -0.0188 877  ASN   E C   
15508 O  O   . ASN   E 573 ? 1.4045 1.5557 1.4935 -0.0239 -0.1009 -0.0204 877  ASN   E O   
15509 C  CB  . ASN   E 573 ? 1.3920 1.5409 1.4716 -0.0270 -0.0934 -0.0140 877  ASN   E CB  
15510 C  CG  . ASN   E 573 ? 1.4471 1.5957 1.5238 -0.0295 -0.0894 -0.0105 877  ASN   E CG  
15511 O  OD1 . ASN   E 573 ? 1.4897 1.6425 1.5704 -0.0343 -0.0878 -0.0090 877  ASN   E OD1 
15512 N  ND2 . ASN   E 573 ? 1.4291 1.5723 1.4988 -0.0263 -0.0877 -0.0091 877  ASN   E ND2 
15513 N  N   . GLY   E 574 ? 1.2376 1.3969 1.3368 -0.0316 -0.0981 -0.0200 878  GLY   E N   
15514 C  CA  . GLY   E 574 ? 1.1736 1.3344 1.2794 -0.0301 -0.1014 -0.0232 878  GLY   E CA  
15515 C  C   . GLY   E 574 ? 1.2097 1.3682 1.3152 -0.0270 -0.1033 -0.0262 878  GLY   E C   
15516 O  O   . GLY   E 574 ? 1.1816 1.3426 1.2946 -0.0267 -0.1055 -0.0290 878  GLY   E O   
15517 N  N   . LYS   E 575 ? 1.2326 1.3863 1.3297 -0.0246 -0.1025 -0.0257 879  LYS   E N   
15518 C  CA  . LYS   E 575 ? 1.1666 1.3174 1.2620 -0.0215 -0.1039 -0.0282 879  LYS   E CA  
15519 C  C   . LYS   E 575 ? 1.1241 1.2764 1.2199 -0.0250 -0.1004 -0.0273 879  LYS   E C   
15520 O  O   . LYS   E 575 ? 1.1659 1.3209 1.2623 -0.0294 -0.0971 -0.0247 879  LYS   E O   
15521 C  CB  . LYS   E 575 ? 1.1176 1.2609 1.2024 -0.0165 -0.1048 -0.0281 879  LYS   E CB  
15522 C  CG  . LYS   E 575 ? 1.1060 1.2463 1.1882 -0.0125 -0.1082 -0.0288 879  LYS   E CG  
15523 C  CD  . LYS   E 575 ? 1.0872 1.2204 1.1576 -0.0090 -0.1064 -0.0266 879  LYS   E CD  
15524 C  CE  . LYS   E 575 ? 1.0445 1.1714 1.1090 -0.0023 -0.1108 -0.0287 879  LYS   E CE  
15525 N  NZ  . LYS   E 575 ? 1.1769 1.2949 1.2300 0.0031  -0.1109 -0.0292 879  LYS   E NZ  
15526 N  N   . LEU   E 576 ? 1.0794 1.2299 1.1747 -0.0226 -0.1014 -0.0297 880  LEU   E N   
15527 C  CA  . LEU   E 576 ? 1.1280 1.2791 1.2229 -0.0252 -0.0983 -0.0291 880  LEU   E CA  
15528 C  C   . LEU   E 576 ? 1.1158 1.2604 1.2007 -0.0227 -0.0973 -0.0285 880  LEU   E C   
15529 O  O   . LEU   E 576 ? 1.0480 1.1885 1.1296 -0.0179 -0.1001 -0.0308 880  LEU   E O   
15530 C  CB  . LEU   E 576 ? 1.0515 1.2063 1.1551 -0.0251 -0.0994 -0.0320 880  LEU   E CB  
15531 C  CG  . LEU   E 576 ? 1.0039 1.1579 1.1062 -0.0258 -0.0970 -0.0325 880  LEU   E CG  
15532 C  CD1 . LEU   E 576 ? 0.9489 1.1085 1.0606 -0.0288 -0.0950 -0.0332 880  LEU   E CD1 
15533 C  CD2 . LEU   E 576 ? 1.0107 1.1604 1.1095 -0.0205 -0.0998 -0.0352 880  LEU   E CD2 
15534 N  N   . LEU   E 577 ? 1.0659 1.2092 1.1459 -0.0260 -0.0936 -0.0255 881  LEU   E N   
15535 C  CA  . LEU   E 577 ? 1.0807 1.2179 1.1520 -0.0248 -0.0919 -0.0247 881  LEU   E CA  
15536 C  C   . LEU   E 577 ? 1.0517 1.1891 1.1241 -0.0258 -0.0909 -0.0260 881  LEU   E C   
15537 O  O   . LEU   E 577 ? 1.0470 1.1888 1.1245 -0.0297 -0.0893 -0.0257 881  LEU   E O   
15538 C  CB  . LEU   E 577 ? 1.0582 1.1942 1.1253 -0.0281 -0.0886 -0.0210 881  LEU   E CB  
15539 C  CG  . LEU   E 577 ? 1.0445 1.1731 1.1023 -0.0259 -0.0869 -0.0196 881  LEU   E CG  
15540 C  CD1 . LEU   E 577 ? 1.0887 1.2123 1.1419 -0.0195 -0.0897 -0.0218 881  LEU   E CD1 
15541 C  CD2 . LEU   E 577 ? 1.0042 1.1324 1.0600 -0.0279 -0.0844 -0.0162 881  LEU   E CD2 
15542 N  N   . ALA   E 578 ? 1.0381 1.1702 1.1049 -0.0219 -0.0917 -0.0276 882  ALA   E N   
15543 C  CA  . ALA   E 578 ? 1.0911 1.2229 1.1585 -0.0220 -0.0910 -0.0292 882  ALA   E CA  
15544 C  C   . ALA   E 578 ? 1.0771 1.2010 1.1344 -0.0195 -0.0900 -0.0288 882  ALA   E C   
15545 O  O   . ALA   E 578 ? 1.1059 1.2245 1.1572 -0.0152 -0.0915 -0.0292 882  ALA   E O   
15546 C  CB  . ALA   E 578 ? 1.0158 1.1508 1.0906 -0.0188 -0.0942 -0.0329 882  ALA   E CB  
15547 N  N   . SER   E 579 ? 1.0666 1.1891 1.1216 -0.0220 -0.0874 -0.0282 883  SER   E N   
15548 C  CA  . SER   E 579 ? 1.1297 1.2444 1.1754 -0.0198 -0.0864 -0.0280 883  SER   E CA  
15549 C  C   . SER   E 579 ? 1.1075 1.2215 1.1542 -0.0166 -0.0878 -0.0312 883  SER   E C   
15550 O  O   . SER   E 579 ? 1.1183 1.2374 1.1717 -0.0186 -0.0874 -0.0323 883  SER   E O   
15551 C  CB  . SER   E 579 ? 1.0474 1.1599 1.0891 -0.0246 -0.0828 -0.0252 883  SER   E CB  
15552 O  OG  . SER   E 579 ? 1.0946 1.2114 1.1410 -0.0286 -0.0816 -0.0253 883  SER   E OG  
15553 N  N   . ILE   E 580 ? 1.0655 1.1733 1.1057 -0.0112 -0.0896 -0.0327 884  ILE   E N   
15554 C  CA  . ILE   E 580 ? 1.0862 1.1922 1.1260 -0.0076 -0.0910 -0.0356 884  ILE   E CA  
15555 C  C   . ILE   E 580 ? 1.1099 1.2064 1.1379 -0.0059 -0.0892 -0.0346 884  ILE   E C   
15556 O  O   . ILE   E 580 ? 1.1502 1.2400 1.1702 -0.0020 -0.0901 -0.0343 884  ILE   E O   
15557 C  CB  . ILE   E 580 ? 1.0945 1.2016 1.1381 -0.0018 -0.0958 -0.0391 884  ILE   E CB  
15558 C  CG1 . ILE   E 580 ? 1.1154 1.2310 1.1704 -0.0036 -0.0977 -0.0398 884  ILE   E CG1 
15559 C  CG2 . ILE   E 580 ? 1.0484 1.1555 1.0943 0.0011  -0.0970 -0.0421 884  ILE   E CG2 
15560 C  CD1 . ILE   E 580 ? 1.0883 1.2022 1.1406 -0.0022 -0.0995 -0.0388 884  ILE   E CD1 
15561 N  N   . ASN   E 581 ? 1.1222 1.2176 1.1485 -0.0087 -0.0866 -0.0340 885  ASN   E N   
15562 C  CA  . ASN   E 581 ? 1.0488 1.1352 1.0645 -0.0080 -0.0845 -0.0330 885  ASN   E CA  
15563 C  C   . ASN   E 581 ? 1.0648 1.1463 1.0740 -0.0097 -0.0824 -0.0298 885  ASN   E C   
15564 O  O   . ASN   E 581 ? 1.0602 1.1443 1.0717 -0.0152 -0.0801 -0.0273 885  ASN   E O   
15565 C  CB  . ASN   E 581 ? 1.0220 1.1032 1.0330 -0.0013 -0.0870 -0.0359 885  ASN   E CB  
15566 C  CG  . ASN   E 581 ? 1.0334 1.1191 1.0509 -0.0002 -0.0880 -0.0388 885  ASN   E CG  
15567 O  OD1 . ASN   E 581 ? 1.0752 1.1672 1.0998 -0.0044 -0.0864 -0.0385 885  ASN   E OD1 
15568 N  ND2 . ASN   E 581 ? 1.0713 1.1536 1.0863 0.0058  -0.0907 -0.0417 885  ASN   E ND2 
15569 N  N   . SER   E 582 ? 1.1070 1.1813 1.1083 -0.0049 -0.0831 -0.0296 886  SER   E N   
15570 C  CA  . SER   E 582 ? 1.1011 1.1702 1.0964 -0.0063 -0.0803 -0.0263 886  SER   E CA  
15571 C  C   . SER   E 582 ? 1.1677 1.2397 1.1656 -0.0049 -0.0816 -0.0256 886  SER   E C   
15572 O  O   . SER   E 582 ? 1.1687 1.2375 1.1629 -0.0061 -0.0789 -0.0227 886  SER   E O   
15573 C  CB  . SER   E 582 ? 1.1090 1.1664 1.0920 -0.0020 -0.0790 -0.0259 886  SER   E CB  
15574 O  OG  . SER   E 582 ? 1.1273 1.1804 1.1051 0.0044  -0.0812 -0.0268 886  SER   E OG  
15575 N  N   . THR   E 583 ? 1.1167 1.1947 1.1213 -0.0025 -0.0855 -0.0283 887  THR   E N   
15576 C  CA  . THR   E 583 ? 1.1178 1.1973 1.1239 0.0001  -0.0877 -0.0285 887  THR   E CA  
15577 C  C   . THR   E 583 ? 1.1250 1.2144 1.1418 -0.0050 -0.0877 -0.0276 887  THR   E C   
15578 O  O   . THR   E 583 ? 1.1349 1.2313 1.1603 -0.0074 -0.0889 -0.0292 887  THR   E O   
15579 C  CB  . THR   E 583 ? 1.2221 1.3008 1.2286 0.0066  -0.0929 -0.0324 887  THR   E CB  
15580 O  OG1 . THR   E 583 ? 1.2969 1.3656 1.2923 0.0121  -0.0933 -0.0334 887  THR   E OG1 
15581 C  CG2 . THR   E 583 ? 1.1643 1.2443 1.1722 0.0093  -0.0957 -0.0328 887  THR   E CG2 
15582 N  N   . VAL   E 584 ? 1.1274 1.2168 1.1434 -0.0062 -0.0863 -0.0250 888  VAL   E N   
15583 C  CA  . VAL   E 584 ? 1.1632 1.2611 1.1883 -0.0098 -0.0868 -0.0243 888  VAL   E CA  
15584 C  C   . VAL   E 584 ? 1.1521 1.2507 1.1786 -0.0050 -0.0909 -0.0264 888  VAL   E C   
15585 O  O   . VAL   E 584 ? 1.2003 1.2920 1.2187 -0.0003 -0.0915 -0.0261 888  VAL   E O   
15586 C  CB  . VAL   E 584 ? 1.1425 1.2406 1.1668 -0.0140 -0.0830 -0.0203 888  VAL   E CB  
15587 C  CG1 . VAL   E 584 ? 1.0918 1.1981 1.1248 -0.0170 -0.0839 -0.0198 888  VAL   E CG1 
15588 C  CG2 . VAL   E 584 ? 1.1007 1.1979 1.1242 -0.0187 -0.0798 -0.0187 888  VAL   E CG2 
15589 N  N   . ARG   E 585 ? 1.1072 1.2136 1.1437 -0.0063 -0.0937 -0.0284 889  ARG   E N   
15590 C  CA  . ARG   E 585 ? 1.1229 1.2302 1.1622 -0.0018 -0.0985 -0.0312 889  ARG   E CA  
15591 C  C   . ARG   E 585 ? 1.1551 1.2703 1.2037 -0.0053 -0.0992 -0.0307 889  ARG   E C   
15592 O  O   . ARG   E 585 ? 1.1183 1.2404 1.1753 -0.0101 -0.0980 -0.0305 889  ARG   E O   
15593 C  CB  . ARG   E 585 ? 1.0770 1.1854 1.1203 0.0013  -0.1022 -0.0353 889  ARG   E CB  
15594 C  CG  . ARG   E 585 ? 1.0459 1.1595 1.0984 0.0032  -0.1071 -0.0384 889  ARG   E CG  
15595 C  CD  . ARG   E 585 ? 1.0319 1.1457 1.0878 0.0069  -0.1107 -0.0424 889  ARG   E CD  
15596 N  NE  . ARG   E 585 ? 1.0616 1.1657 1.1054 0.0127  -0.1118 -0.0431 889  ARG   E NE  
15597 C  CZ  . ARG   E 585 ? 1.0828 1.1844 1.1252 0.0159  -0.1134 -0.0456 889  ARG   E CZ  
15598 N  NH1 . ARG   E 585 ? 1.0507 1.1592 1.1038 0.0142  -0.1140 -0.0477 889  ARG   E NH1 
15599 N  NH2 . ARG   E 585 ? 1.1121 1.2037 1.1419 0.0211  -0.1139 -0.0457 889  ARG   E NH2 
15600 N  N   . LEU   E 586 ? 1.1364 1.2497 1.1827 -0.0024 -0.1011 -0.0306 890  LEU   E N   
15601 C  CA  . LEU   E 586 ? 1.0895 1.2092 1.1439 -0.0048 -0.1024 -0.0304 890  LEU   E CA  
15602 C  C   . LEU   E 586 ? 1.0828 1.2049 1.1440 -0.0016 -0.1080 -0.0346 890  LEU   E C   
15603 O  O   . LEU   E 586 ? 1.1428 1.2592 1.1988 0.0045  -0.1118 -0.0370 890  LEU   E O   
15604 C  CB  . LEU   E 586 ? 1.0522 1.1683 1.1005 -0.0035 -0.1013 -0.0279 890  LEU   E CB  
15605 C  CG  . LEU   E 586 ? 1.0688 1.1919 1.1253 -0.0072 -0.1014 -0.0269 890  LEU   E CG  
15606 C  CD1 . LEU   E 586 ? 1.0838 1.2147 1.1496 -0.0134 -0.0996 -0.0266 890  LEU   E CD1 
15607 C  CD2 . LEU   E 586 ? 1.1014 1.2223 1.1527 -0.0080 -0.0981 -0.0231 890  LEU   E CD2 
15608 N  N   . TYR   E 587 ? 1.0933 1.2235 1.1661 -0.0054 -0.1085 -0.0355 891  TYR   E N   
15609 C  CA  . TYR   E 587 ? 1.1055 1.2392 1.1873 -0.0032 -0.1135 -0.0394 891  TYR   E CA  
15610 C  C   . TYR   E 587 ? 1.1063 1.2438 1.1939 -0.0050 -0.1148 -0.0389 891  TYR   E C   
15611 O  O   . TYR   E 587 ? 1.0545 1.1942 1.1416 -0.0090 -0.1113 -0.0356 891  TYR   E O   
15612 C  CB  . TYR   E 587 ? 1.0945 1.2342 1.1862 -0.0060 -0.1127 -0.0410 891  TYR   E CB  
15613 C  CG  . TYR   E 587 ? 1.0426 1.1792 1.1318 -0.0027 -0.1137 -0.0432 891  TYR   E CG  
15614 C  CD1 . TYR   E 587 ? 1.0723 1.2056 1.1611 0.0034  -0.1192 -0.0470 891  TYR   E CD1 
15615 C  CD2 . TYR   E 587 ? 1.0552 1.1922 1.1428 -0.0055 -0.1094 -0.0418 891  TYR   E CD2 
15616 C  CE1 . TYR   E 587 ? 1.0979 1.2285 1.1847 0.0067  -0.1203 -0.0493 891  TYR   E CE1 
15617 C  CE2 . TYR   E 587 ? 1.0138 1.1480 1.0992 -0.0023 -0.1103 -0.0439 891  TYR   E CE2 
15618 C  CZ  . TYR   E 587 ? 1.0661 1.1973 1.1513 0.0038  -0.1156 -0.0476 891  TYR   E CZ  
15619 O  OH  . TYR   E 587 ? 1.0640 1.1924 1.1469 0.0071  -0.1165 -0.0497 891  TYR   E OH  
15620 N  N   . GLU   E 588 ? 1.1623 1.3008 1.2561 -0.0019 -0.1203 -0.0425 892  GLU   E N   
15621 C  CA  . GLU   E 588 ? 1.1307 1.2724 1.2307 -0.0029 -0.1225 -0.0428 892  GLU   E CA  
15622 C  C   . GLU   E 588 ? 1.1112 1.2593 1.2257 -0.0041 -0.1256 -0.0461 892  GLU   E C   
15623 O  O   . GLU   E 588 ? 1.1063 1.2545 1.2249 -0.0012 -0.1288 -0.0496 892  GLU   E O   
15624 C  CB  . GLU   E 588 ? 1.1183 1.2531 1.2103 0.0029  -0.1269 -0.0441 892  GLU   E CB  
15625 C  CG  . GLU   E 588 ? 1.1773 1.3084 1.2598 0.0026  -0.1237 -0.0402 892  GLU   E CG  
15626 C  CD  . GLU   E 588 ? 1.3347 1.4564 1.4054 0.0096  -0.1270 -0.0413 892  GLU   E CD  
15627 O  OE1 . GLU   E 588 ? 1.4950 1.6123 1.5562 0.0104  -0.1238 -0.0380 892  GLU   E OE1 
15628 O  OE2 . GLU   E 588 ? 1.4657 1.5843 1.5367 0.0146  -0.1328 -0.0453 892  GLU   E OE2 
15629 N  N   . TRP   E 589 ? 1.1284 1.2817 1.2508 -0.0083 -0.1246 -0.0451 893  TRP   E N   
15630 C  CA  . TRP   E 589 ? 1.2166 1.3762 1.3539 -0.0102 -0.1266 -0.0477 893  TRP   E CA  
15631 C  C   . TRP   E 589 ? 1.2610 1.4185 1.4010 -0.0063 -0.1333 -0.0509 893  TRP   E C   
15632 O  O   . TRP   E 589 ? 1.2246 1.3807 1.3617 -0.0067 -0.1339 -0.0495 893  TRP   E O   
15633 C  CB  . TRP   E 589 ? 1.1726 1.3380 1.3162 -0.0166 -0.1216 -0.0447 893  TRP   E CB  
15634 C  CG  . TRP   E 589 ? 1.1637 1.3358 1.3224 -0.0196 -0.1209 -0.0465 893  TRP   E CG  
15635 C  CD1 . TRP   E 589 ? 1.1869 1.3635 1.3550 -0.0234 -0.1197 -0.0459 893  TRP   E CD1 
15636 C  CD2 . TRP   E 589 ? 1.1597 1.3344 1.3257 -0.0188 -0.1210 -0.0490 893  TRP   E CD2 
15637 N  NE1 . TRP   E 589 ? 1.1300 1.3117 1.3110 -0.0251 -0.1186 -0.0476 893  TRP   E NE1 
15638 C  CE2 . TRP   E 589 ? 1.1513 1.3323 1.3316 -0.0224 -0.1194 -0.0496 893  TRP   E CE2 
15639 C  CE3 . TRP   E 589 ? 1.1939 1.3661 1.3557 -0.0153 -0.1220 -0.0506 893  TRP   E CE3 
15640 C  CZ2 . TRP   E 589 ? 1.1746 1.3598 1.3657 -0.0225 -0.1185 -0.0517 893  TRP   E CZ2 
15641 C  CZ3 . TRP   E 589 ? 1.2053 1.3817 1.3775 -0.0154 -0.1216 -0.0529 893  TRP   E CZ3 
15642 C  CH2 . TRP   E 589 ? 1.1650 1.3480 1.3520 -0.0190 -0.1197 -0.0534 893  TRP   E CH2 
15643 N  N   . THR   E 590 ? 1.2627 1.4199 1.4085 -0.0024 -0.1388 -0.0553 894  THR   E N   
15644 C  CA  . THR   E 590 ? 1.3257 1.4801 1.4742 0.0018  -0.1463 -0.0591 894  THR   E CA  
15645 C  C   . THR   E 590 ? 1.4179 1.5790 1.5820 -0.0021 -0.1474 -0.0603 894  THR   E C   
15646 O  O   . THR   E 590 ? 1.3477 1.5156 1.5219 -0.0074 -0.1426 -0.0589 894  THR   E O   
15647 C  CB  . THR   E 590 ? 1.3677 1.5193 1.5170 0.0077  -0.1524 -0.0637 894  THR   E CB  
15648 O  OG1 . THR   E 590 ? 1.3610 1.5200 1.5259 0.0053  -0.1522 -0.0660 894  THR   E OG1 
15649 C  CG2 . THR   E 590 ? 1.2339 1.3784 1.3676 0.0116  -0.1509 -0.0625 894  THR   E CG2 
15650 N  N   . THR   E 591 ? 1.4476 1.6057 1.6129 0.0009  -0.1537 -0.0629 895  THR   E N   
15651 C  CA  . THR   E 591 ? 1.4590 1.6224 1.6394 -0.0022 -0.1557 -0.0646 895  THR   E CA  
15652 C  C   . THR   E 591 ? 1.4296 1.5988 1.6266 -0.0027 -0.1581 -0.0684 895  THR   E C   
15653 O  O   . THR   E 591 ? 1.4467 1.6221 1.6584 -0.0070 -0.1570 -0.0689 895  THR   E O   
15654 C  CB  . THR   E 591 ? 1.5048 1.6629 1.6824 0.0014  -0.1625 -0.0669 895  THR   E CB  
15655 O  OG1 . THR   E 591 ? 1.6141 1.7635 1.7732 0.0062  -0.1633 -0.0655 895  THR   E OG1 
15656 C  CG2 . THR   E 591 ? 1.4588 1.6202 1.6426 -0.0035 -0.1600 -0.0648 895  THR   E CG2 
15657 N  N   . GLU   E 592 ? 1.3773 1.5446 1.5722 0.0017  -0.1611 -0.0711 896  GLU   E N   
15658 C  CA  . GLU   E 592 ? 1.3533 1.5267 1.5638 0.0013  -0.1625 -0.0744 896  GLU   E CA  
15659 C  C   . GLU   E 592 ? 1.3969 1.5752 1.6091 -0.0027 -0.1541 -0.0713 896  GLU   E C   
15660 O  O   . GLU   E 592 ? 1.3987 1.5803 1.6191 -0.0016 -0.1546 -0.0736 896  GLU   E O   
15661 C  CB  . GLU   E 592 ? 1.3120 1.4806 1.5198 0.0086  -0.1707 -0.0793 896  GLU   E CB  
15662 N  N   . LYS   E 593 ? 1.3525 1.5308 1.5568 -0.0070 -0.1469 -0.0663 897  LYS   E N   
15663 C  CA  . LYS   E 593 ? 1.2671 1.4496 1.4727 -0.0114 -0.1388 -0.0631 897  LYS   E CA  
15664 C  C   . LYS   E 593 ? 1.3461 1.5271 1.5470 -0.0083 -0.1384 -0.0641 897  LYS   E C   
15665 O  O   . LYS   E 593 ? 1.3458 1.5317 1.5565 -0.0095 -0.1359 -0.0650 897  LYS   E O   
15666 C  CB  . LYS   E 593 ? 1.1472 1.3376 1.3706 -0.0163 -0.1356 -0.0632 897  LYS   E CB  
15667 N  N   . GLU   E 594 ? 1.4026 1.5762 1.5877 -0.0041 -0.1404 -0.0637 898  GLU   E N   
15668 C  CA  . GLU   E 594 ? 1.3768 1.5473 1.5540 -0.0012 -0.1393 -0.0639 898  GLU   E CA  
15669 C  C   . GLU   E 594 ? 1.3663 1.5303 1.5254 -0.0011 -0.1358 -0.0599 898  GLU   E C   
15670 O  O   . GLU   E 594 ? 1.3703 1.5327 1.5240 -0.0029 -0.1345 -0.0573 898  GLU   E O   
15671 C  CB  . GLU   E 594 ? 1.3786 1.5460 1.5570 0.0056  -0.1471 -0.0689 898  GLU   E CB  
15672 C  CG  . GLU   E 594 ? 1.4553 1.6134 1.6190 0.0112  -0.1524 -0.0697 898  GLU   E CG  
15673 C  CD  . GLU   E 594 ? 1.5508 1.7060 1.7178 0.0179  -0.1618 -0.0753 898  GLU   E CD  
15674 O  OE1 . GLU   E 594 ? 1.5247 1.6758 1.6891 0.0207  -0.1673 -0.0770 898  GLU   E OE1 
15675 O  OE2 . GLU   E 594 ? 1.6310 1.7874 1.8026 0.0206  -0.1637 -0.0781 898  GLU   E OE2 
15676 N  N   . LEU   E 595 ? 1.2641 1.4243 1.4142 0.0010  -0.1341 -0.0594 899  LEU   E N   
15677 C  CA  . LEU   E 595 ? 1.2074 1.3614 1.3414 0.0011  -0.1305 -0.0558 899  LEU   E CA  
15678 C  C   . LEU   E 595 ? 1.1852 1.3304 1.3071 0.0080  -0.1352 -0.0576 899  LEU   E C   
15679 O  O   . LEU   E 595 ? 1.1500 1.2933 1.2724 0.0122  -0.1385 -0.0607 899  LEU   E O   
15680 C  CB  . LEU   E 595 ? 1.2062 1.3615 1.3378 -0.0022 -0.1243 -0.0533 899  LEU   E CB  
15681 C  CG  . LEU   E 595 ? 1.1119 1.2726 1.2480 -0.0090 -0.1181 -0.0499 899  LEU   E CG  
15682 C  CD1 . LEU   E 595 ? 1.0602 1.2223 1.1967 -0.0109 -0.1136 -0.0492 899  LEU   E CD1 
15683 C  CD2 . LEU   E 595 ? 1.0815 1.2391 1.2074 -0.0114 -0.1152 -0.0459 899  LEU   E CD2 
15684 N  N   . ARG   E 596 ? 1.1727 1.3120 1.2836 0.0095  -0.1355 -0.0556 900  ARG   E N   
15685 C  CA  . ARG   E 596 ? 1.1752 1.3048 1.2726 0.0163  -0.1392 -0.0567 900  ARG   E CA  
15686 C  C   . ARG   E 596 ? 1.1688 1.2926 1.2518 0.0156  -0.1335 -0.0523 900  ARG   E C   
15687 O  O   . ARG   E 596 ? 1.1669 1.2927 1.2489 0.0112  -0.1292 -0.0487 900  ARG   E O   
15688 C  CB  . ARG   E 596 ? 1.1282 1.2546 1.2245 0.0199  -0.1449 -0.0586 900  ARG   E CB  
15689 N  N   . THR   E 597 ? 1.1145 1.2309 1.1868 0.0200  -0.1336 -0.0527 901  THR   E N   
15690 C  CA  . THR   E 597 ? 1.0987 1.2093 1.1582 0.0192  -0.1280 -0.0485 901  THR   E CA  
15691 C  C   . THR   E 597 ? 1.0876 1.1919 1.1369 0.0217  -0.1278 -0.0464 901  THR   E C   
15692 O  O   . THR   E 597 ? 1.2000 1.2978 1.2433 0.0280  -0.1328 -0.0488 901  THR   E O   
15693 C  CB  . THR   E 597 ? 1.1030 1.2065 1.1533 0.0237  -0.1282 -0.0496 901  THR   E CB  
15694 O  OG1 . THR   E 597 ? 1.1139 1.2230 1.1744 0.0230  -0.1300 -0.0526 901  THR   E OG1 
15695 C  CG2 . THR   E 597 ? 1.0914 1.1910 1.1321 0.0209  -0.1213 -0.0451 901  THR   E CG2 
15696 N  N   . GLU   E 598 ? 1.0891 1.1950 1.1364 0.0169  -0.1220 -0.0420 902  GLU   E N   
15697 C  CA  . GLU   E 598 ? 1.1677 1.2680 1.2058 0.0190  -0.1206 -0.0395 902  GLU   E CA  
15698 C  C   . GLU   E 598 ? 1.2071 1.2974 1.2304 0.0225  -0.1172 -0.0372 902  GLU   E C   
15699 O  O   . GLU   E 598 ? 1.2524 1.3335 1.2651 0.0294  -0.1199 -0.0384 902  GLU   E O   
15700 C  CB  . GLU   E 598 ? 1.1548 1.2619 1.1989 0.0126  -0.1165 -0.0360 902  GLU   E CB  
15701 N  N   . CYS   E 599 ? 1.2175 1.3089 1.2396 0.0179  -0.1111 -0.0338 903  CYS   E N   
15702 C  CA  . CYS   E 599 ? 1.2194 1.3014 1.2286 0.0208  -0.1076 -0.0318 903  CYS   E CA  
15703 C  C   . CYS   E 599 ? 1.2110 1.2948 1.2223 0.0174  -0.1050 -0.0316 903  CYS   E C   
15704 O  O   . CYS   E 599 ? 1.1619 1.2543 1.1841 0.0126  -0.1053 -0.0326 903  CYS   E O   
15705 C  CB  . CYS   E 599 ? 1.2799 1.3591 1.2833 0.0192  -0.1019 -0.0271 903  CYS   E CB  
15706 S  SG  . CYS   E 599 ? 1.2039 1.2949 1.2201 0.0106  -0.0990 -0.0245 903  CYS   E SG  
15707 N  N   . ASN   E 600 ? 1.2738 1.3487 1.2738 0.0201  -0.1022 -0.0302 904  ASN   E N   
15708 C  CA  . ASN   E 600 ? 1.1919 1.2665 1.1916 0.0176  -0.0995 -0.0298 904  ASN   E CA  
15709 C  C   . ASN   E 600 ? 1.2009 1.2690 1.1917 0.0162  -0.0932 -0.0256 904  ASN   E C   
15710 O  O   . ASN   E 600 ? 1.2833 1.3427 1.2637 0.0206  -0.0917 -0.0240 904  ASN   E O   
15711 C  CB  . ASN   E 600 ? 1.1930 1.2621 1.1880 0.0235  -0.1036 -0.0336 904  ASN   E CB  
15712 C  CG  . ASN   E 600 ? 1.1806 1.2583 1.1875 0.0212  -0.1068 -0.0369 904  ASN   E CG  
15713 O  OD1 . ASN   E 600 ? 1.1956 1.2829 1.2141 0.0162  -0.1067 -0.0368 904  ASN   E OD1 
15714 N  ND2 . ASN   E 600 ? 1.1689 1.2429 1.1729 0.0253  -0.1094 -0.0397 904  ASN   E ND2 
15715 N  N   . HIS   E 601 ? 1.1947 1.2665 1.1897 0.0101  -0.0894 -0.0237 905  HIS   E N   
15716 C  CA  . HIS   E 601 ? 1.2194 1.2852 1.2074 0.0082  -0.0836 -0.0201 905  HIS   E CA  
15717 C  C   . HIS   E 601 ? 1.2250 1.2890 1.2118 0.0069  -0.0829 -0.0211 905  HIS   E C   
15718 O  O   . HIS   E 601 ? 1.1931 1.2647 1.1886 0.0023  -0.0837 -0.0222 905  HIS   E O   
15719 C  CB  . HIS   E 601 ? 1.1024 1.1740 1.0967 0.0016  -0.0795 -0.0165 905  HIS   E CB  
15720 C  CG  . HIS   E 601 ? 1.1694 1.2344 1.1570 0.0004  -0.0737 -0.0126 905  HIS   E CG  
15721 N  ND1 . HIS   E 601 ? 1.2256 1.2845 1.2078 0.0000  -0.0713 -0.0122 905  HIS   E ND1 
15722 C  CD2 . HIS   E 601 ? 1.1982 1.2610 1.1838 -0.0001 -0.0696 -0.0091 905  HIS   E CD2 
15723 C  CE1 . HIS   E 601 ? 1.2559 1.3095 1.2336 -0.0012 -0.0659 -0.0085 905  HIS   E CE1 
15724 N  NE2 . HIS   E 601 ? 1.2955 1.3516 1.2755 -0.0013 -0.0646 -0.0065 905  HIS   E NE2 
15725 N  N   . TYR   E 602 ? 1.2350 1.2884 1.2103 0.0110  -0.0813 -0.0207 906  TYR   E N   
15726 C  CA  . TYR   E 602 ? 1.2258 1.2759 1.1982 0.0108  -0.0809 -0.0218 906  TYR   E CA  
15727 C  C   . TYR   E 602 ? 1.1838 1.2305 1.1536 0.0059  -0.0750 -0.0181 906  TYR   E C   
15728 O  O   . TYR   E 602 ? 1.2258 1.2660 1.1890 0.0067  -0.0710 -0.0150 906  TYR   E O   
15729 C  CB  . TYR   E 602 ? 1.2413 1.2813 1.2026 0.0189  -0.0835 -0.0241 906  TYR   E CB  
15730 C  CG  . TYR   E 602 ? 1.2816 1.3247 1.2463 0.0239  -0.0901 -0.0283 906  TYR   E CG  
15731 C  CD1 . TYR   E 602 ? 1.2711 1.3140 1.2350 0.0271  -0.0924 -0.0285 906  TYR   E CD1 
15732 C  CD2 . TYR   E 602 ? 1.3396 1.3858 1.3087 0.0255  -0.0943 -0.0321 906  TYR   E CD2 
15733 C  CE1 . TYR   E 602 ? 1.2574 1.3029 1.2249 0.0317  -0.0990 -0.0326 906  TYR   E CE1 
15734 C  CE2 . TYR   E 602 ? 1.3080 1.3573 1.2816 0.0300  -0.1006 -0.0361 906  TYR   E CE2 
15735 C  CZ  . TYR   E 602 ? 1.3072 1.3561 1.2801 0.0329  -0.1032 -0.0365 906  TYR   E CZ  
15736 O  OH  . TYR   E 602 ? 1.2971 1.3489 1.2751 0.0372  -0.1100 -0.0407 906  TYR   E OH  
15737 N  N   . ASN   E 603 ? 1.1471 1.1979 1.1220 0.0010  -0.0743 -0.0184 907  ASN   E N   
15738 C  CA  . ASN   E 603 ? 1.1786 1.2281 1.1538 -0.0049 -0.0695 -0.0152 907  ASN   E CA  
15739 C  C   . ASN   E 603 ? 1.2425 1.2841 1.2103 -0.0041 -0.0681 -0.0156 907  ASN   E C   
15740 O  O   . ASN   E 603 ? 1.2819 1.3221 1.2474 -0.0006 -0.0712 -0.0187 907  ASN   E O   
15741 C  CB  . ASN   E 603 ? 1.1712 1.2316 1.1581 -0.0119 -0.0699 -0.0149 907  ASN   E CB  
15742 C  CG  . ASN   E 603 ? 1.1984 1.2668 1.1927 -0.0123 -0.0718 -0.0148 907  ASN   E CG  
15743 O  OD1 . ASN   E 603 ? 1.1649 1.2397 1.1653 -0.0117 -0.0755 -0.0175 907  ASN   E OD1 
15744 N  ND2 . ASN   E 603 ? 1.1365 1.2041 1.1304 -0.0133 -0.0689 -0.0118 907  ASN   E ND2 
15745 N  N   . ASN   E 604 ? 1.2315 1.2675 1.1957 -0.0073 -0.0634 -0.0124 908  ASN   E N   
15746 C  CA  . ASN   E 604 ? 1.2023 1.2305 1.1599 -0.0075 -0.0616 -0.0124 908  ASN   E CA  
15747 C  C   . ASN   E 604 ? 1.1947 1.2283 1.1592 -0.0141 -0.0617 -0.0127 908  ASN   E C   
15748 O  O   . ASN   E 604 ? 1.2200 1.2474 1.1796 -0.0153 -0.0601 -0.0125 908  ASN   E O   
15749 C  CB  . ASN   E 604 ? 1.1895 1.2074 1.1390 -0.0073 -0.0562 -0.0088 908  ASN   E CB  
15750 C  CG  . ASN   E 604 ? 1.2488 1.2706 1.2058 -0.0144 -0.0524 -0.0054 908  ASN   E CG  
15751 O  OD1 . ASN   E 604 ? 1.2873 1.3192 1.2543 -0.0185 -0.0539 -0.0053 908  ASN   E OD1 
15752 N  ND2 . ASN   E 604 ? 1.2993 1.3128 1.2514 -0.0159 -0.0475 -0.0025 908  ASN   E ND2 
15753 N  N   . ILE   E 605 ? 1.1663 1.2106 1.1411 -0.0182 -0.0635 -0.0131 909  ILE   E N   
15754 C  CA  . ILE   E 605 ? 1.1213 1.1712 1.1021 -0.0230 -0.0647 -0.0143 909  ILE   E CA  
15755 C  C   . ILE   E 605 ? 1.1594 1.2172 1.1459 -0.0209 -0.0687 -0.0173 909  ILE   E C   
15756 O  O   . ILE   E 605 ? 1.1964 1.2567 1.1844 -0.0172 -0.0706 -0.0181 909  ILE   E O   
15757 C  CB  . ILE   E 605 ? 1.1126 1.1676 1.1007 -0.0301 -0.0631 -0.0118 909  ILE   E CB  
15758 C  CG1 . ILE   E 605 ? 1.0861 1.1505 1.0825 -0.0311 -0.0646 -0.0115 909  ILE   E CG1 
15759 C  CG2 . ILE   E 605 ? 1.1704 1.2187 1.1550 -0.0318 -0.0590 -0.0085 909  ILE   E CG2 
15760 C  CD1 . ILE   E 605 ? 1.0506 1.1201 1.0542 -0.0375 -0.0632 -0.0090 909  ILE   E CD1 
15761 N  N   . MET   E 606 ? 1.1685 1.2295 1.1580 -0.0230 -0.0699 -0.0191 910  MET   E N   
15762 C  CA  . MET   E 606 ? 1.0236 1.0922 1.0196 -0.0216 -0.0729 -0.0218 910  MET   E CA  
15763 C  C   . MET   E 606 ? 1.0504 1.1277 1.0554 -0.0268 -0.0729 -0.0205 910  MET   E C   
15764 O  O   . MET   E 606 ? 1.0992 1.1766 1.1050 -0.0319 -0.0713 -0.0188 910  MET   E O   
15765 C  CB  . MET   E 606 ? 1.0896 1.1566 1.0839 -0.0206 -0.0736 -0.0241 910  MET   E CB  
15766 C  CG  . MET   E 606 ? 1.1215 1.1968 1.1240 -0.0229 -0.0747 -0.0257 910  MET   E CG  
15767 S  SD  . MET   E 606 ? 1.2891 1.3604 1.2875 -0.0235 -0.0738 -0.0271 910  MET   E SD  
15768 C  CE  . MET   E 606 ? 1.1471 1.2280 1.1549 -0.0272 -0.0739 -0.0277 910  MET   E CE  
15769 N  N   . ALA   E 607 ? 1.1309 1.2148 1.1420 -0.0255 -0.0749 -0.0213 911  ALA   E N   
15770 C  CA  . ALA   E 607 ? 1.0748 1.1661 1.0935 -0.0298 -0.0748 -0.0197 911  ALA   E CA  
15771 C  C   . ALA   E 607 ? 1.0505 1.1481 1.0754 -0.0328 -0.0755 -0.0209 911  ALA   E C   
15772 O  O   . ALA   E 607 ? 1.0658 1.1687 1.0963 -0.0311 -0.0773 -0.0228 911  ALA   E O   
15773 C  CB  . ALA   E 607 ? 1.0380 1.1325 1.0596 -0.0268 -0.0765 -0.0199 911  ALA   E CB  
15774 N  N   . LEU   E 608 ? 1.0606 1.1570 1.0844 -0.0373 -0.0741 -0.0198 912  LEU   E N   
15775 C  CA  . LEU   E 608 ? 1.0920 1.1930 1.1200 -0.0400 -0.0743 -0.0207 912  LEU   E CA  
15776 C  C   . LEU   E 608 ? 1.0960 1.2037 1.1305 -0.0437 -0.0746 -0.0192 912  LEU   E C   
15777 O  O   . LEU   E 608 ? 1.1061 1.2192 1.1458 -0.0442 -0.0752 -0.0202 912  LEU   E O   
15778 C  CB  . LEU   E 608 ? 1.0683 1.1642 1.0911 -0.0427 -0.0731 -0.0204 912  LEU   E CB  
15779 C  CG  . LEU   E 608 ? 1.1073 1.2005 1.1271 -0.0391 -0.0732 -0.0230 912  LEU   E CG  
15780 C  CD1 . LEU   E 608 ? 1.1409 1.2273 1.1543 -0.0352 -0.0731 -0.0233 912  LEU   E CD1 
15781 C  CD2 . LEU   E 608 ? 1.1001 1.1905 1.1166 -0.0414 -0.0723 -0.0234 912  LEU   E CD2 
15782 N  N   . TYR   E 609 ? 1.0499 1.1572 1.0844 -0.0461 -0.0741 -0.0168 913  TYR   E N   
15783 C  CA  . TYR   E 609 ? 1.0543 1.1674 1.0945 -0.0497 -0.0744 -0.0152 913  TYR   E CA  
15784 C  C   . TYR   E 609 ? 1.0911 1.2072 1.1345 -0.0476 -0.0749 -0.0145 913  TYR   E C   
15785 O  O   . TYR   E 609 ? 1.0846 1.1966 1.1244 -0.0454 -0.0741 -0.0136 913  TYR   E O   
15786 C  CB  . TYR   E 609 ? 1.0070 1.1177 1.0459 -0.0542 -0.0736 -0.0132 913  TYR   E CB  
15787 C  CG  . TYR   E 609 ? 0.9960 1.1027 1.0308 -0.0560 -0.0736 -0.0142 913  TYR   E CG  
15788 C  CD1 . TYR   E 609 ? 1.0123 1.1217 1.0482 -0.0566 -0.0742 -0.0156 913  TYR   E CD1 
15789 C  CD2 . TYR   E 609 ? 1.0187 1.1185 1.0480 -0.0570 -0.0728 -0.0138 913  TYR   E CD2 
15790 C  CE1 . TYR   E 609 ? 0.9836 1.0886 1.0147 -0.0578 -0.0741 -0.0165 913  TYR   E CE1 
15791 C  CE2 . TYR   E 609 ? 1.0225 1.1180 1.0474 -0.0585 -0.0730 -0.0149 913  TYR   E CE2 
15792 C  CZ  . TYR   E 609 ? 1.0015 1.0996 1.0270 -0.0587 -0.0737 -0.0163 913  TYR   E CZ  
15793 O  OH  . TYR   E 609 ? 1.0042 1.0973 1.0243 -0.0597 -0.0738 -0.0173 913  TYR   E OH  
15794 N  N   . LEU   E 610 ? 1.0293 1.1518 1.0787 -0.0479 -0.0761 -0.0148 914  LEU   E N   
15795 C  CA  . LEU   E 610 ? 0.9994 1.1248 1.0518 -0.0458 -0.0769 -0.0142 914  LEU   E CA  
15796 C  C   . LEU   E 610 ? 1.0110 1.1421 1.0690 -0.0494 -0.0772 -0.0127 914  LEU   E C   
15797 O  O   . LEU   E 610 ? 1.0145 1.1494 1.0760 -0.0510 -0.0778 -0.0135 914  LEU   E O   
15798 C  CB  . LEU   E 610 ? 1.0236 1.1503 1.0777 -0.0414 -0.0787 -0.0168 914  LEU   E CB  
15799 C  CG  . LEU   E 610 ? 1.0061 1.1310 1.0586 -0.0371 -0.0797 -0.0169 914  LEU   E CG  
15800 C  CD1 . LEU   E 610 ? 1.0097 1.1270 1.0542 -0.0353 -0.0781 -0.0158 914  LEU   E CD1 
15801 C  CD2 . LEU   E 610 ? 1.0599 1.1862 1.1149 -0.0329 -0.0823 -0.0200 914  LEU   E CD2 
15802 N  N   . LYS   E 611 ? 0.9849 1.1164 1.0435 -0.0506 -0.0764 -0.0104 915  LYS   E N   
15803 C  CA  . LYS   E 611 ? 1.0041 1.1409 1.0679 -0.0536 -0.0769 -0.0089 915  LYS   E CA  
15804 C  C   . LYS   E 611 ? 1.0638 1.2017 1.1288 -0.0517 -0.0766 -0.0074 915  LYS   E C   
15805 O  O   . LYS   E 611 ? 1.0257 1.1594 1.0872 -0.0500 -0.0750 -0.0063 915  LYS   E O   
15806 C  CB  . LYS   E 611 ? 0.9410 1.0773 1.0049 -0.0582 -0.0763 -0.0073 915  LYS   E CB  
15807 C  CG  . LYS   E 611 ? 0.9640 1.0983 1.0253 -0.0601 -0.0767 -0.0087 915  LYS   E CG  
15808 C  CD  . LYS   E 611 ? 0.9508 1.0889 1.0147 -0.0603 -0.0776 -0.0100 915  LYS   E CD  
15809 C  CE  . LYS   E 611 ? 0.9313 1.0672 0.9924 -0.0626 -0.0777 -0.0107 915  LYS   E CE  
15810 N  NZ  . LYS   E 611 ? 0.9885 1.1259 1.0506 -0.0665 -0.0787 -0.0094 915  LYS   E NZ  
15811 N  N   . THR   E 612 ? 1.0610 1.2041 1.1308 -0.0518 -0.0779 -0.0073 916  THR   E N   
15812 C  CA  . THR   E 612 ? 1.0110 1.1551 1.0819 -0.0494 -0.0778 -0.0061 916  THR   E CA  
15813 C  C   . THR   E 612 ? 0.9663 1.1153 1.0421 -0.0525 -0.0779 -0.0042 916  THR   E C   
15814 O  O   . THR   E 612 ? 0.9621 1.1147 1.0411 -0.0553 -0.0790 -0.0045 916  THR   E O   
15815 C  CB  . THR   E 612 ? 0.9996 1.1443 1.0710 -0.0454 -0.0798 -0.0084 916  THR   E CB  
15816 O  OG1 . THR   E 612 ? 1.1057 1.2557 1.1826 -0.0472 -0.0813 -0.0090 916  THR   E OG1 
15817 C  CG2 . THR   E 612 ? 1.0164 1.1574 1.0845 -0.0429 -0.0805 -0.0109 916  THR   E CG2 
15818 N  N   . LYS   E 613 ? 0.9587 1.1075 1.0346 -0.0516 -0.0766 -0.0021 917  LYS   E N   
15819 C  CA  . LYS   E 613 ? 0.9143 1.0678 0.9951 -0.0535 -0.0767 -0.0001 917  LYS   E CA  
15820 C  C   . LYS   E 613 ? 1.1802 1.3328 1.2597 -0.0493 -0.0762 0.0005  917  LYS   E C   
15821 O  O   . LYS   E 613 ? 1.1819 1.3314 1.2591 -0.0478 -0.0737 0.0023  917  LYS   E O   
15822 C  CB  . LYS   E 613 ? 0.9394 1.0935 1.0224 -0.0571 -0.0752 0.0021  917  LYS   E CB  
15823 C  CG  . LYS   E 613 ? 0.9011 1.0606 0.9898 -0.0598 -0.0761 0.0036  917  LYS   E CG  
15824 C  CD  . LYS   E 613 ? 1.1391 1.3010 1.2290 -0.0625 -0.0785 0.0022  917  LYS   E CD  
15825 C  CE  . LYS   E 613 ? 1.1080 1.2664 1.1948 -0.0645 -0.0786 0.0010  917  LYS   E CE  
15826 N  NZ  . LYS   E 613 ? 1.0759 1.2337 1.1605 -0.0642 -0.0798 -0.0013 917  LYS   E NZ  
15827 N  N   . GLY   E 614 ? 1.2192 1.3739 1.3000 -0.0473 -0.0784 -0.0009 918  GLY   E N   
15828 C  CA  . GLY   E 614 ? 1.2377 1.3909 1.3166 -0.0429 -0.0787 -0.0008 918  GLY   E CA  
15829 C  C   . GLY   E 614 ? 1.2705 1.4174 1.3430 -0.0383 -0.0785 -0.0022 918  GLY   E C   
15830 O  O   . GLY   E 614 ? 1.2667 1.4124 1.3381 -0.0369 -0.0806 -0.0049 918  GLY   E O   
15831 N  N   . ASP   E 615 ? 1.3579 1.5005 1.4260 -0.0357 -0.0759 -0.0003 919  ASP   E N   
15832 C  CA  . ASP   E 615 ? 1.3618 1.4971 1.4221 -0.0309 -0.0754 -0.0012 919  ASP   E CA  
15833 C  C   . ASP   E 615 ? 1.3389 1.4702 1.3960 -0.0323 -0.0730 -0.0006 919  ASP   E C   
15834 O  O   . ASP   E 615 ? 1.3383 1.4634 1.3887 -0.0285 -0.0730 -0.0018 919  ASP   E O   
15835 C  CB  . ASP   E 615 ? 1.4517 1.5829 1.5073 -0.0266 -0.0734 0.0007  919  ASP   E CB  
15836 C  CG  . ASP   E 615 ? 1.5208 1.6528 1.5784 -0.0291 -0.0688 0.0046  919  ASP   E CG  
15837 O  OD1 . ASP   E 615 ? 1.4693 1.6068 1.5337 -0.0346 -0.0684 0.0055  919  ASP   E OD1 
15838 O  OD2 . ASP   E 615 ? 1.5901 1.7168 1.6424 -0.0255 -0.0655 0.0066  919  ASP   E OD2 
15839 N  N   . PHE   E 616 ? 1.2936 1.4281 1.3551 -0.0375 -0.0711 0.0012  920  PHE   E N   
15840 C  CA  . PHE   E 616 ? 1.1912 1.3220 1.2503 -0.0394 -0.0689 0.0018  920  PHE   E CA  
15841 C  C   . PHE   E 616 ? 1.1853 1.3163 1.2440 -0.0406 -0.0714 -0.0011 920  PHE   E C   
15842 O  O   . PHE   E 616 ? 1.1321 1.2682 1.1954 -0.0427 -0.0740 -0.0025 920  PHE   E O   
15843 C  CB  . PHE   E 616 ? 1.1622 1.2965 1.2271 -0.0446 -0.0668 0.0044  920  PHE   E CB  
15844 C  CG  . PHE   E 616 ? 1.2727 1.4056 1.3379 -0.0435 -0.0629 0.0076  920  PHE   E CG  
15845 C  CD1 . PHE   E 616 ? 1.2632 1.3898 1.3213 -0.0381 -0.0608 0.0082  920  PHE   E CD1 
15846 C  CD2 . PHE   E 616 ? 1.2844 1.4220 1.3569 -0.0478 -0.0614 0.0100  920  PHE   E CD2 
15847 C  CE1 . PHE   E 616 ? 1.2613 1.3861 1.3194 -0.0368 -0.0565 0.0114  920  PHE   E CE1 
15848 C  CE2 . PHE   E 616 ? 1.2426 1.3793 1.3166 -0.0468 -0.0574 0.0131  920  PHE   E CE2 
15849 C  CZ  . PHE   E 616 ? 1.2977 1.4279 1.3643 -0.0413 -0.0546 0.0140  920  PHE   E CZ  
15850 N  N   . ILE   E 617 ? 1.1532 1.2779 1.2060 -0.0391 -0.0703 -0.0017 921  ILE   E N   
15851 C  CA  . ILE   E 617 ? 1.0827 1.2067 1.1344 -0.0396 -0.0722 -0.0044 921  ILE   E CA  
15852 C  C   . ILE   E 617 ? 1.0519 1.1721 1.1013 -0.0425 -0.0699 -0.0034 921  ILE   E C   
15853 O  O   . ILE   E 617 ? 1.1037 1.2182 1.1487 -0.0413 -0.0670 -0.0016 921  ILE   E O   
15854 C  CB  . ILE   E 617 ? 1.0940 1.2136 1.1403 -0.0339 -0.0741 -0.0070 921  ILE   E CB  
15855 C  CG1 . ILE   E 617 ? 1.1219 1.2445 1.1705 -0.0309 -0.0766 -0.0080 921  ILE   E CG1 
15856 C  CG2 . ILE   E 617 ? 1.0758 1.1962 1.1228 -0.0344 -0.0761 -0.0098 921  ILE   E CG2 
15857 C  CD1 . ILE   E 617 ? 1.1379 1.2547 1.1801 -0.0244 -0.0784 -0.0100 921  ILE   E CD1 
15858 N  N   . LEU   E 618 ? 1.0341 1.1567 1.0860 -0.0462 -0.0711 -0.0045 922  LEU   E N   
15859 C  CA  . LEU   E 618 ? 1.0484 1.1671 1.0980 -0.0492 -0.0697 -0.0040 922  LEU   E CA  
15860 C  C   . LEU   E 618 ? 0.9671 1.0819 1.0119 -0.0472 -0.0707 -0.0066 922  LEU   E C   
15861 O  O   . LEU   E 618 ? 1.0194 1.1378 1.0664 -0.0471 -0.0729 -0.0087 922  LEU   E O   
15862 C  CB  . LEU   E 618 ? 0.9820 1.1054 1.0373 -0.0548 -0.0704 -0.0031 922  LEU   E CB  
15863 C  CG  . LEU   E 618 ? 1.0316 1.1508 1.0853 -0.0582 -0.0691 -0.0023 922  LEU   E CG  
15864 C  CD1 . LEU   E 618 ? 1.0507 1.1648 1.1020 -0.0570 -0.0657 -0.0002 922  LEU   E CD1 
15865 C  CD2 . LEU   E 618 ? 1.0313 1.1550 1.0909 -0.0633 -0.0704 -0.0015 922  LEU   E CD2 
15866 N  N   . VAL   E 619 ? 0.9725 1.0801 1.0109 -0.0456 -0.0689 -0.0064 923  VAL   E N   
15867 C  CA  . VAL   E 619 ? 1.0473 1.1506 1.0807 -0.0434 -0.0698 -0.0088 923  VAL   E CA  
15868 C  C   . VAL   E 619 ? 1.0512 1.1497 1.0816 -0.0467 -0.0683 -0.0082 923  VAL   E C   
15869 O  O   . VAL   E 619 ? 1.0823 1.1773 1.1117 -0.0485 -0.0658 -0.0059 923  VAL   E O   
15870 C  CB  . VAL   E 619 ? 1.0575 1.1548 1.0841 -0.0372 -0.0696 -0.0097 923  VAL   E CB  
15871 C  CG1 . VAL   E 619 ? 0.9845 1.0785 1.0070 -0.0346 -0.0711 -0.0126 923  VAL   E CG1 
15872 C  CG2 . VAL   E 619 ? 1.0825 1.1837 1.1118 -0.0339 -0.0714 -0.0103 923  VAL   E CG2 
15873 N  N   . GLY   E 620 ? 1.0390 1.1370 1.0681 -0.0474 -0.0696 -0.0103 924  GLY   E N   
15874 C  CA  . GLY   E 620 ? 1.0434 1.1367 1.0694 -0.0505 -0.0687 -0.0100 924  GLY   E CA  
15875 C  C   . GLY   E 620 ? 1.0362 1.1254 1.0569 -0.0480 -0.0695 -0.0126 924  GLY   E C   
15876 O  O   . GLY   E 620 ? 1.0462 1.1383 1.0679 -0.0449 -0.0710 -0.0147 924  GLY   E O   
15877 N  N   . ASP   E 621 ? 1.0515 1.1339 1.0670 -0.0495 -0.0683 -0.0123 925  ASP   E N   
15878 C  CA  . ASP   E 621 ? 1.0341 1.1119 1.0439 -0.0473 -0.0688 -0.0146 925  ASP   E CA  
15879 C  C   . ASP   E 621 ? 1.0181 1.0934 1.0266 -0.0517 -0.0690 -0.0146 925  ASP   E C   
15880 O  O   . ASP   E 621 ? 1.0142 1.0914 1.0265 -0.0564 -0.0692 -0.0131 925  ASP   E O   
15881 C  CB  . ASP   E 621 ? 1.0273 1.0968 1.0294 -0.0430 -0.0674 -0.0148 925  ASP   E CB  
15882 C  CG  . ASP   E 621 ? 1.0459 1.1086 1.0445 -0.0455 -0.0649 -0.0124 925  ASP   E CG  
15883 O  OD1 . ASP   E 621 ? 1.0657 1.1299 1.0683 -0.0508 -0.0646 -0.0110 925  ASP   E OD1 
15884 O  OD2 . ASP   E 621 ? 1.0668 1.1222 1.0588 -0.0420 -0.0632 -0.0120 925  ASP   E OD2 
15885 N  N   . LEU   E 622 ? 1.0245 1.0950 1.0274 -0.0500 -0.0692 -0.0165 926  LEU   E N   
15886 C  CA  . LEU   E 622 ? 0.9931 1.0605 0.9936 -0.0535 -0.0697 -0.0169 926  LEU   E CA  
15887 C  C   . LEU   E 622 ? 1.0165 1.0778 1.0149 -0.0573 -0.0689 -0.0152 926  LEU   E C   
15888 O  O   . LEU   E 622 ? 1.0522 1.1115 1.0498 -0.0610 -0.0700 -0.0154 926  LEU   E O   
15889 C  CB  . LEU   E 622 ? 0.9596 1.0228 0.9541 -0.0503 -0.0697 -0.0193 926  LEU   E CB  
15890 C  CG  . LEU   E 622 ? 0.9324 0.9963 0.9263 -0.0525 -0.0707 -0.0205 926  LEU   E CG  
15891 C  CD1 . LEU   E 622 ? 0.9119 0.9840 0.9131 -0.0553 -0.0718 -0.0197 926  LEU   E CD1 
15892 C  CD2 . LEU   E 622 ? 1.0039 1.0671 0.9949 -0.0481 -0.0703 -0.0228 926  LEU   E CD2 
15893 N  N   . MET   E 623 ? 0.9897 1.0478 0.9872 -0.0564 -0.0669 -0.0135 927  MET   E N   
15894 C  CA  . MET   E 623 ? 0.9369 0.9883 0.9325 -0.0597 -0.0655 -0.0118 927  MET   E CA  
15895 C  C   . MET   E 623 ? 1.0043 1.0598 1.0076 -0.0634 -0.0646 -0.0091 927  MET   E C   
15896 O  O   . MET   E 623 ? 0.9702 1.0207 0.9733 -0.0652 -0.0623 -0.0072 927  MET   E O   
15897 C  CB  . MET   E 623 ? 1.1016 1.1444 1.0895 -0.0558 -0.0631 -0.0116 927  MET   E CB  
15898 C  CG  . MET   E 623 ? 1.1289 1.1672 1.1093 -0.0519 -0.0639 -0.0143 927  MET   E CG  
15899 S  SD  . MET   E 623 ? 1.0853 1.1115 1.0573 -0.0536 -0.0630 -0.0146 927  MET   E SD  
15900 C  CE  . MET   E 623 ? 1.1017 1.1264 1.0673 -0.0486 -0.0645 -0.0179 927  MET   E CE  
15901 N  N   . ARG   E 624 ? 1.0349 1.0993 1.0453 -0.0647 -0.0661 -0.0089 928  ARG   E N   
15902 C  CA  . ARG   E 624 ? 1.0080 1.0770 1.0263 -0.0680 -0.0654 -0.0064 928  ARG   E CA  
15903 C  C   . ARG   E 624 ? 1.0358 1.1034 1.0537 -0.0650 -0.0621 -0.0044 928  ARG   E C   
15904 O  O   . ARG   E 624 ? 1.0131 1.0814 1.0360 -0.0675 -0.0601 -0.0019 928  ARG   E O   
15905 C  CB  . ARG   E 624 ? 1.0305 1.0965 1.0515 -0.0736 -0.0660 -0.0055 928  ARG   E CB  
15906 C  CG  . ARG   E 624 ? 1.0249 1.0979 1.0560 -0.0784 -0.0677 -0.0042 928  ARG   E CG  
15907 C  CD  . ARG   E 624 ? 1.1617 1.2360 1.1986 -0.0790 -0.0642 -0.0012 928  ARG   E CD  
15908 N  NE  . ARG   E 624 ? 1.1821 1.2596 1.2285 -0.0841 -0.0647 0.0005  928  ARG   E NE  
15909 C  CZ  . ARG   E 624 ? 1.3279 1.4044 1.3790 -0.0852 -0.0609 0.0033  928  ARG   E CZ  
15910 N  NH1 . ARG   E 624 ? 1.3096 1.3804 1.3553 -0.0817 -0.0565 0.0046  928  ARG   E NH1 
15911 N  NH2 . ARG   E 624 ? 1.3945 1.4756 1.4561 -0.0897 -0.0616 0.0047  928  ARG   E NH2 
15912 N  N   . SER   E 625 ? 1.0471 1.1120 1.0589 -0.0594 -0.0613 -0.0055 929  SER   E N   
15913 C  CA  . SER   E 625 ? 1.0343 1.0983 1.0451 -0.0557 -0.0587 -0.0038 929  SER   E CA  
15914 C  C   . SER   E 625 ? 1.0982 1.1716 1.1159 -0.0556 -0.0602 -0.0035 929  SER   E C   
15915 O  O   . SER   E 625 ? 1.0780 1.1563 1.0968 -0.0541 -0.0629 -0.0057 929  SER   E O   
15916 C  CB  . SER   E 625 ? 1.0721 1.1298 1.0737 -0.0495 -0.0582 -0.0053 929  SER   E CB  
15917 O  OG  . SER   E 625 ? 1.1392 1.1890 1.1343 -0.0498 -0.0578 -0.0062 929  SER   E OG  
15918 N  N   . VAL   E 626 ? 1.1439 1.2200 1.1670 -0.0574 -0.0582 -0.0009 930  VAL   E N   
15919 C  CA  . VAL   E 626 ? 1.1027 1.1872 1.1322 -0.0572 -0.0593 -0.0004 930  VAL   E CA  
15920 C  C   . VAL   E 626 ? 1.1157 1.1982 1.1431 -0.0530 -0.0565 0.0014  930  VAL   E C   
15921 O  O   . VAL   E 626 ? 1.1449 1.2215 1.1699 -0.0528 -0.0526 0.0037  930  VAL   E O   
15922 C  CB  . VAL   E 626 ? 1.0584 1.1492 1.0971 -0.0630 -0.0603 0.0009  930  VAL   E CB  
15923 C  CG1 . VAL   E 626 ? 1.0994 1.1969 1.1440 -0.0622 -0.0599 0.0025  930  VAL   E CG1 
15924 C  CG2 . VAL   E 626 ? 0.9896 1.0836 1.0295 -0.0655 -0.0641 -0.0014 930  VAL   E CG2 
15925 N  N   . LEU   E 627 ? 1.1688 1.2558 1.1969 -0.0497 -0.0582 0.0004  931  LEU   E N   
15926 C  CA  . LEU   E 627 ? 1.1678 1.2521 1.1918 -0.0443 -0.0566 0.0013  931  LEU   E CA  
15927 C  C   . LEU   E 627 ? 1.1391 1.2316 1.1695 -0.0443 -0.0582 0.0015  931  LEU   E C   
15928 O  O   . LEU   E 627 ? 1.1318 1.2304 1.1660 -0.0451 -0.0617 -0.0005 931  LEU   E O   
15929 C  CB  . LEU   E 627 ? 1.0865 1.1656 1.1020 -0.0387 -0.0583 -0.0014 931  LEU   E CB  
15930 C  CG  . LEU   E 627 ? 1.0737 1.1499 1.0842 -0.0325 -0.0580 -0.0014 931  LEU   E CG  
15931 C  CD1 . LEU   E 627 ? 1.1762 1.2483 1.1855 -0.0326 -0.0530 0.0024  931  LEU   E CD1 
15932 C  CD2 . LEU   E 627 ? 1.1530 1.2217 1.1543 -0.0271 -0.0592 -0.0037 931  LEU   E CD2 
15933 N  N   . LEU   E 628 ? 1.1631 1.2556 1.1948 -0.0433 -0.0553 0.0042  932  LEU   E N   
15934 C  CA  . LEU   E 628 ? 1.1438 1.2436 1.1812 -0.0431 -0.0567 0.0046  932  LEU   E CA  
15935 C  C   . LEU   E 628 ? 1.1631 1.2593 1.1944 -0.0366 -0.0564 0.0044  932  LEU   E C   
15936 O  O   . LEU   E 628 ? 1.1542 1.2440 1.1804 -0.0337 -0.0525 0.0066  932  LEU   E O   
15937 C  CB  . LEU   E 628 ? 1.0990 1.2030 1.1444 -0.0475 -0.0542 0.0077  932  LEU   E CB  
15938 C  CG  . LEU   E 628 ? 1.1862 1.2981 1.2376 -0.0475 -0.0561 0.0079  932  LEU   E CG  
15939 C  CD1 . LEU   E 628 ? 1.1527 1.2699 1.2064 -0.0486 -0.0610 0.0049  932  LEU   E CD1 
15940 C  CD2 . LEU   E 628 ? 1.1892 1.3062 1.2496 -0.0519 -0.0542 0.0107  932  LEU   E CD2 
15941 N  N   . LEU   E 629 ? 1.1643 1.2641 1.1960 -0.0341 -0.0605 0.0018  933  LEU   E N   
15942 C  CA  . LEU   E 629 ? 1.1897 1.2865 1.2159 -0.0277 -0.0618 0.0007  933  LEU   E CA  
15943 C  C   . LEU   E 629 ? 1.1876 1.2905 1.2192 -0.0277 -0.0628 0.0014  933  LEU   E C   
15944 O  O   . LEU   E 629 ? 1.2104 1.3212 1.2504 -0.0323 -0.0641 0.0016  933  LEU   E O   
15945 C  CB  . LEU   E 629 ? 1.1502 1.2464 1.1738 -0.0247 -0.0662 -0.0033 933  LEU   E CB  
15946 C  CG  . LEU   E 629 ? 1.1351 1.2219 1.1486 -0.0194 -0.0661 -0.0046 933  LEU   E CG  
15947 C  CD1 . LEU   E 629 ? 1.1137 1.1958 1.1243 -0.0221 -0.0631 -0.0035 933  LEU   E CD1 
15948 C  CD2 . LEU   E 629 ? 1.1337 1.2221 1.1474 -0.0164 -0.0712 -0.0087 933  LEU   E CD2 
15949 N  N   . ALA   E 630 ? 1.2654 1.3641 1.2915 -0.0223 -0.0623 0.0019  934  ALA   E N   
15950 C  CA  . ALA   E 630 ? 1.2383 1.3417 1.2680 -0.0211 -0.0636 0.0022  934  ALA   E CA  
15951 C  C   . ALA   E 630 ? 1.2912 1.3912 1.3152 -0.0149 -0.0676 -0.0007 934  ALA   E C   
15952 O  O   . ALA   E 630 ? 1.3275 1.4187 1.3419 -0.0095 -0.0671 -0.0013 934  ALA   E O   
15953 C  CB  . ALA   E 630 ? 1.1604 1.2620 1.1895 -0.0206 -0.0587 0.0061  934  ALA   E CB  
15954 N  N   . TYR   E 631 ? 1.3083 1.4147 1.3381 -0.0154 -0.0716 -0.0026 935  TYR   E N   
15955 C  CA  . TYR   E 631 ? 1.2878 1.3917 1.3140 -0.0098 -0.0759 -0.0054 935  TYR   E CA  
15956 C  C   . TYR   E 631 ? 1.2801 1.3799 1.3011 -0.0055 -0.0743 -0.0036 935  TYR   E C   
15957 O  O   . TYR   E 631 ? 1.2290 1.3338 1.2552 -0.0081 -0.0726 -0.0013 935  TYR   E O   
15958 C  CB  . TYR   E 631 ? 1.2834 1.3954 1.3185 -0.0122 -0.0804 -0.0081 935  TYR   E CB  
15959 C  CG  . TYR   E 631 ? 1.3786 1.4886 1.4117 -0.0069 -0.0856 -0.0115 935  TYR   E CG  
15960 C  CD1 . TYR   E 631 ? 1.3645 1.4700 1.3935 -0.0030 -0.0887 -0.0147 935  TYR   E CD1 
15961 C  CD2 . TYR   E 631 ? 1.3282 1.4409 1.3641 -0.0058 -0.0877 -0.0117 935  TYR   E CD2 
15962 C  CE1 . TYR   E 631 ? 1.3943 1.4981 1.4226 0.0019  -0.0941 -0.0182 935  TYR   E CE1 
15963 C  CE2 . TYR   E 631 ? 1.2406 1.3511 1.2752 -0.0010 -0.0929 -0.0151 935  TYR   E CE2 
15964 C  CZ  . TYR   E 631 ? 1.2831 1.3893 1.3141 0.0027  -0.0963 -0.0185 935  TYR   E CZ  
15965 O  OH  . TYR   E 631 ? 1.2355 1.3395 1.2660 0.0075  -0.1022 -0.0222 935  TYR   E OH  
15966 N  N   . LYS   E 632 ? 1.3090 1.3995 1.3194 0.0013  -0.0748 -0.0044 936  LYS   E N   
15967 C  CA  . LYS   E 632 ? 1.3384 1.4232 1.3417 0.0064  -0.0732 -0.0028 936  LYS   E CA  
15968 C  C   . LYS   E 632 ? 1.3760 1.4626 1.3806 0.0095  -0.0792 -0.0059 936  LYS   E C   
15969 O  O   . LYS   E 632 ? 1.4055 1.4858 1.4033 0.0152  -0.0834 -0.0090 936  LYS   E O   
15970 C  CB  . LYS   E 632 ? 1.3822 1.4546 1.3719 0.0127  -0.0707 -0.0021 936  LYS   E CB  
15971 N  N   . PRO   E 633 ? 1.3827 1.4773 1.3961 0.0059  -0.0800 -0.0053 937  PRO   E N   
15972 C  CA  . PRO   E 633 ? 1.3134 1.4109 1.3303 0.0075  -0.0862 -0.0088 937  PRO   E CA  
15973 C  C   . PRO   E 633 ? 1.3349 1.4236 1.3417 0.0155  -0.0891 -0.0103 937  PRO   E C   
15974 O  O   . PRO   E 633 ? 1.3051 1.3927 1.3120 0.0184  -0.0953 -0.0144 937  PRO   E O   
15975 C  CB  . PRO   E 633 ? 1.1582 1.2648 1.1849 0.0022  -0.0850 -0.0068 937  PRO   E CB  
15976 C  CG  . PRO   E 633 ? 1.1974 1.3027 1.2218 0.0011  -0.0786 -0.0023 937  PRO   E CG  
15977 C  CD  . PRO   E 633 ? 1.3001 1.4003 1.3194 0.0013  -0.0753 -0.0014 937  PRO   E CD  
15978 N  N   . MET   E 634 ? 1.2952 1.3770 1.2931 0.0193  -0.0848 -0.0073 938  MET   E N   
15979 C  CA  . MET   E 634 ? 1.3673 1.4390 1.3534 0.0276  -0.0873 -0.0087 938  MET   E CA  
15980 C  C   . MET   E 634 ? 1.3840 1.4461 1.3598 0.0332  -0.0897 -0.0112 938  MET   E C   
15981 O  O   . MET   E 634 ? 1.3755 1.4310 1.3444 0.0396  -0.0952 -0.0145 938  MET   E O   
15982 C  CB  . MET   E 634 ? 1.3411 1.4078 1.3203 0.0303  -0.0812 -0.0044 938  MET   E CB  
15983 N  N   . GLU   E 635 ? 1.3851 1.4458 1.3595 0.0313  -0.0860 -0.0099 939  GLU   E N   
15984 C  CA  . GLU   E 635 ? 1.4373 1.4886 1.4015 0.0367  -0.0881 -0.0122 939  GLU   E CA  
15985 C  C   . GLU   E 635 ? 1.4569 1.5138 1.4289 0.0341  -0.0934 -0.0162 939  GLU   E C   
15986 O  O   . GLU   E 635 ? 1.4642 1.5142 1.4290 0.0383  -0.0958 -0.0185 939  GLU   E O   
15987 C  CB  . GLU   E 635 ? 1.4903 1.5348 1.4466 0.0370  -0.0806 -0.0083 939  GLU   E CB  
15988 N  N   . GLY   E 636 ? 1.6041 1.6728 1.5901 0.0275  -0.0951 -0.0170 940  GLY   E N   
15989 C  CA  . GLY   E 636 ? 1.6157 1.6907 1.6106 0.0245  -0.0993 -0.0204 940  GLY   E CA  
15990 C  C   . GLY   E 636 ? 1.6475 1.7197 1.6393 0.0238  -0.0972 -0.0204 940  GLY   E C   
15991 O  O   . GLY   E 636 ? 1.6482 1.7199 1.6411 0.0257  -0.1017 -0.0240 940  GLY   E O   
15992 N  N   . ASN   E 637 ? 1.5748 1.6451 1.5634 0.0212  -0.0905 -0.0163 941  ASN   E N   
15993 C  CA  . ASN   E 637 ? 1.5371 1.6047 1.5231 0.0200  -0.0882 -0.0161 941  ASN   E CA  
15994 C  C   . ASN   E 637 ? 1.5582 1.6313 1.5503 0.0126  -0.0821 -0.0122 941  ASN   E C   
15995 O  O   . ASN   E 637 ? 1.5436 1.6210 1.5400 0.0095  -0.0793 -0.0094 941  ASN   E O   
15996 C  CB  . ASN   E 637 ? 1.5330 1.5873 1.5037 0.0271  -0.0866 -0.0156 941  ASN   E CB  
15997 C  CG  . ASN   E 637 ? 1.6012 1.6519 1.5688 0.0285  -0.0884 -0.0180 941  ASN   E CG  
15998 O  OD1 . ASN   E 637 ? 1.5738 1.6306 1.5492 0.0271  -0.0932 -0.0215 941  ASN   E OD1 
15999 N  ND2 . ASN   E 637 ? 1.6320 1.6730 1.5886 0.0311  -0.0841 -0.0159 941  ASN   E ND2 
16000 N  N   . PHE   E 638 ? 1.4997 1.5726 1.4923 0.0099  -0.0806 -0.0123 942  PHE   E N   
16001 C  CA  . PHE   E 638 ? 1.3752 1.4519 1.3726 0.0032  -0.0754 -0.0090 942  PHE   E CA  
16002 C  C   . PHE   E 638 ? 1.4270 1.4946 1.4151 0.0051  -0.0694 -0.0055 942  PHE   E C   
16003 O  O   . PHE   E 638 ? 1.4243 1.4817 1.4010 0.0112  -0.0693 -0.0061 942  PHE   E O   
16004 C  CB  . PHE   E 638 ? 1.2969 1.3768 1.2986 -0.0006 -0.0764 -0.0107 942  PHE   E CB  
16005 C  CG  . PHE   E 638 ? 1.1548 1.2429 1.1656 -0.0024 -0.0814 -0.0141 942  PHE   E CG  
16006 C  CD1 . PHE   E 638 ? 1.0887 1.1863 1.1099 -0.0083 -0.0813 -0.0133 942  PHE   E CD1 
16007 C  CD2 . PHE   E 638 ? 1.1812 1.2672 1.1901 0.0019  -0.0860 -0.0180 942  PHE   E CD2 
16008 C  CE1 . PHE   E 638 ? 1.1187 1.2232 1.1480 -0.0099 -0.0851 -0.0162 942  PHE   E CE1 
16009 C  CE2 . PHE   E 638 ? 1.1212 1.2149 1.1395 0.0001  -0.0900 -0.0209 942  PHE   E CE2 
16010 C  CZ  . PHE   E 638 ? 1.0989 1.2016 1.1272 -0.0058 -0.0893 -0.0199 942  PHE   E CZ  
16011 N  N   . GLU   E 639 ? 1.4105 1.4817 1.4037 -0.0003 -0.0645 -0.0018 943  GLU   E N   
16012 C  CA  . GLU   E 639 ? 1.4239 1.4877 1.4110 0.0002  -0.0580 0.0020  943  GLU   E CA  
16013 C  C   . GLU   E 639 ? 1.4218 1.4894 1.4157 -0.0070 -0.0548 0.0038  943  GLU   E C   
16014 O  O   . GLU   E 639 ? 1.4365 1.5135 1.4412 -0.0128 -0.0550 0.0046  943  GLU   E O   
16015 C  CB  . GLU   E 639 ? 1.4482 1.5120 1.4353 0.0015  -0.0545 0.0051  943  GLU   E CB  
16016 C  CG  . GLU   E 639 ? 1.5426 1.5962 1.5207 0.0045  -0.0477 0.0088  943  GLU   E CG  
16017 C  CD  . GLU   E 639 ? 1.6590 1.7002 1.6228 0.0114  -0.0483 0.0072  943  GLU   E CD  
16018 O  OE1 . GLU   E 639 ? 1.6851 1.7255 1.6481 0.0104  -0.0508 0.0049  943  GLU   E OE1 
16019 O  OE2 . GLU   E 639 ? 1.7053 1.7371 1.6580 0.0182  -0.0463 0.0083  943  GLU   E OE2 
16020 N  N   . GLU   E 640 ? 1.4103 1.4701 1.3976 -0.0064 -0.0519 0.0046  944  GLU   E N   
16021 C  CA  . GLU   E 640 ? 1.2982 1.3607 1.2916 -0.0130 -0.0494 0.0059  944  GLU   E CA  
16022 C  C   . GLU   E 640 ? 1.2690 1.3332 1.2678 -0.0169 -0.0437 0.0102  944  GLU   E C   
16023 O  O   . GLU   E 640 ? 1.2960 1.3530 1.2886 -0.0136 -0.0388 0.0130  944  GLU   E O   
16024 C  CB  . GLU   E 640 ? 1.3214 1.3747 1.3061 -0.0112 -0.0481 0.0054  944  GLU   E CB  
16025 C  CG  . GLU   E 640 ? 1.3525 1.4089 1.3436 -0.0181 -0.0472 0.0057  944  GLU   E CG  
16026 C  CD  . GLU   E 640 ? 1.4320 1.4787 1.4166 -0.0183 -0.0420 0.0081  944  GLU   E CD  
16027 O  OE1 . GLU   E 640 ? 1.4926 1.5310 1.4674 -0.0140 -0.0427 0.0064  944  GLU   E OE1 
16028 O  OE2 . GLU   E 640 ? 1.3330 1.3804 1.3229 -0.0226 -0.0372 0.0115  944  GLU   E OE2 
16029 N  N   . ILE   E 641 ? 1.2352 1.3087 1.2456 -0.0238 -0.0444 0.0107  945  ILE   E N   
16030 C  CA  . ILE   E 641 ? 1.2175 1.2953 1.2359 -0.0277 -0.0403 0.0143  945  ILE   E CA  
16031 C  C   . ILE   E 641 ? 1.2763 1.3525 1.2987 -0.0330 -0.0366 0.0164  945  ILE   E C   
16032 O  O   . ILE   E 641 ? 1.2856 1.3580 1.3083 -0.0333 -0.0307 0.0199  945  ILE   E O   
16033 C  CB  . ILE   E 641 ? 1.1915 1.2808 1.2204 -0.0314 -0.0440 0.0135  945  ILE   E CB  
16034 C  CG1 . ILE   E 641 ? 1.2434 1.3338 1.2688 -0.0262 -0.0475 0.0115  945  ILE   E CG1 
16035 C  CG2 . ILE   E 641 ? 1.1261 1.2201 1.1639 -0.0352 -0.0402 0.0170  945  ILE   E CG2 
16036 C  CD1 . ILE   E 641 ? 1.2636 1.3443 1.2778 -0.0189 -0.0450 0.0124  945  ILE   E CD1 
16037 N  N   . ALA   E 642 ? 1.2746 1.3537 1.3004 -0.0374 -0.0398 0.0143  946  ALA   E N   
16038 C  CA  . ALA   E 642 ? 1.2495 1.3269 1.2791 -0.0426 -0.0373 0.0157  946  ALA   E CA  
16039 C  C   . ALA   E 642 ? 1.2451 1.3208 1.2715 -0.0439 -0.0411 0.0126  946  ALA   E C   
16040 O  O   . ALA   E 642 ? 1.2143 1.2923 1.2381 -0.0416 -0.0456 0.0095  946  ALA   E O   
16041 C  CB  . ALA   E 642 ? 1.2267 1.3131 1.2695 -0.0490 -0.0373 0.0173  946  ALA   E CB  
16042 N  N   . ARG   E 643 ? 1.3113 1.3831 1.3384 -0.0477 -0.0391 0.0134  947  ARG   E N   
16043 C  CA  . ARG   E 643 ? 1.2470 1.3174 1.2718 -0.0496 -0.0424 0.0107  947  ARG   E CA  
16044 C  C   . ARG   E 643 ? 1.2060 1.2740 1.2351 -0.0553 -0.0403 0.0121  947  ARG   E C   
16045 O  O   . ARG   E 643 ? 1.2207 1.2863 1.2530 -0.0569 -0.0356 0.0153  947  ARG   E O   
16046 C  CB  . ARG   E 643 ? 1.2199 1.2818 1.2326 -0.0437 -0.0428 0.0088  947  ARG   E CB  
16047 C  CG  . ARG   E 643 ? 1.2017 1.2527 1.2070 -0.0417 -0.0375 0.0111  947  ARG   E CG  
16048 C  CD  . ARG   E 643 ? 1.2457 1.2890 1.2388 -0.0340 -0.0377 0.0098  947  ARG   E CD  
16049 N  NE  . ARG   E 643 ? 1.3142 1.3590 1.3045 -0.0325 -0.0430 0.0058  947  ARG   E NE  
16050 C  CZ  . ARG   E 643 ? 1.4292 1.4688 1.4103 -0.0260 -0.0450 0.0036  947  ARG   E CZ  
16051 N  NH1 . ARG   E 643 ? 1.5040 1.5364 1.4766 -0.0200 -0.0427 0.0047  947  ARG   E NH1 
16052 N  NH2 . ARG   E 643 ? 1.3765 1.4180 1.3568 -0.0253 -0.0495 0.0001  947  ARG   E NH2 
16053 N  N   . ASP   E 644 ? 1.2270 1.2955 1.2563 -0.0583 -0.0439 0.0098  948  ASP   E N   
16054 C  CA  . ASP   E 644 ? 1.2267 1.2916 1.2586 -0.0634 -0.0429 0.0104  948  ASP   E CA  
16055 C  C   . ASP   E 644 ? 1.2237 1.2841 1.2482 -0.0626 -0.0460 0.0073  948  ASP   E C   
16056 O  O   . ASP   E 644 ? 1.2179 1.2827 1.2414 -0.0614 -0.0501 0.0047  948  ASP   E O   
16057 C  CB  . ASP   E 644 ? 1.2331 1.3063 1.2772 -0.0697 -0.0451 0.0109  948  ASP   E CB  
16058 C  CG  . ASP   E 644 ? 1.3016 1.3710 1.3496 -0.0753 -0.0444 0.0115  948  ASP   E CG  
16059 O  OD1 . ASP   E 644 ? 1.3961 1.4569 1.4398 -0.0747 -0.0402 0.0131  948  ASP   E OD1 
16060 O  OD2 . ASP   E 644 ? 1.2788 1.3532 1.3336 -0.0801 -0.0484 0.0104  948  ASP   E OD2 
16061 N  N   . PHE   E 645 ? 1.1980 1.2492 1.2170 -0.0631 -0.0436 0.0078  949  PHE   E N   
16062 C  CA  . PHE   E 645 ? 1.1956 1.2420 1.2080 -0.0628 -0.0462 0.0050  949  PHE   E CA  
16063 C  C   . PHE   E 645 ? 1.1528 1.1963 1.1692 -0.0690 -0.0463 0.0055  949  PHE   E C   
16064 O  O   . PHE   E 645 ? 1.2212 1.2598 1.2394 -0.0710 -0.0422 0.0080  949  PHE   E O   
16065 C  CB  . PHE   E 645 ? 1.2239 1.2606 1.2242 -0.0568 -0.0440 0.0046  949  PHE   E CB  
16066 C  CG  . PHE   E 645 ? 1.2588 1.2976 1.2548 -0.0504 -0.0449 0.0036  949  PHE   E CG  
16067 C  CD1 . PHE   E 645 ? 1.2475 1.2965 1.2497 -0.0504 -0.0485 0.0023  949  PHE   E CD1 
16068 C  CD2 . PHE   E 645 ? 1.1926 1.2228 1.1783 -0.0442 -0.0425 0.0039  949  PHE   E CD2 
16069 C  CE1 . PHE   E 645 ? 1.2242 1.2752 1.2232 -0.0447 -0.0498 0.0011  949  PHE   E CE1 
16070 C  CE2 . PHE   E 645 ? 1.3245 1.3563 1.3063 -0.0381 -0.0441 0.0026  949  PHE   E CE2 
16071 C  CZ  . PHE   E 645 ? 1.2974 1.3398 1.2864 -0.0385 -0.0479 0.0012  949  PHE   E CZ  
16072 N  N   . ASN   E 646 ? 1.1008 1.1474 1.1189 -0.0719 -0.0508 0.0030  950  ASN   E N   
16073 C  CA  . ASN   E 646 ? 1.1166 1.1598 1.1374 -0.0774 -0.0521 0.0028  950  ASN   E CA  
16074 C  C   . ASN   E 646 ? 1.0942 1.1353 1.1083 -0.0766 -0.0561 -0.0006 950  ASN   E C   
16075 O  O   . ASN   E 646 ? 1.0937 1.1409 1.1109 -0.0782 -0.0601 -0.0023 950  ASN   E O   
16076 C  CB  . ASN   E 646 ? 1.1452 1.1961 1.1785 -0.0831 -0.0538 0.0039  950  ASN   E CB  
16077 C  CG  . ASN   E 646 ? 1.2166 1.2632 1.2536 -0.0889 -0.0551 0.0037  950  ASN   E CG  
16078 O  OD1 . ASN   E 646 ? 1.2801 1.3182 1.3095 -0.0887 -0.0553 0.0024  950  ASN   E OD1 
16079 N  ND2 . ASN   E 646 ? 1.2892 1.3415 1.3379 -0.0938 -0.0562 0.0049  950  ASN   E ND2 
16080 N  N   . PRO   E 647 ? 1.0703 1.1021 1.0746 -0.0739 -0.0548 -0.0015 951  PRO   E N   
16081 C  CA  . PRO   E 647 ? 1.0893 1.1192 1.0862 -0.0714 -0.0578 -0.0046 951  PRO   E CA  
16082 C  C   . PRO   E 647 ? 1.0690 1.1007 1.0687 -0.0760 -0.0620 -0.0063 951  PRO   E C   
16083 O  O   . PRO   E 647 ? 1.0817 1.1096 1.0839 -0.0806 -0.0624 -0.0058 951  PRO   E O   
16084 C  CB  . PRO   E 647 ? 1.0835 1.1018 1.0703 -0.0686 -0.0553 -0.0048 951  PRO   E CB  
16085 C  CG  . PRO   E 647 ? 1.0814 1.0962 1.0695 -0.0685 -0.0506 -0.0016 951  PRO   E CG  
16086 C  CD  . PRO   E 647 ? 1.0621 1.0842 1.0623 -0.0738 -0.0505 0.0004  951  PRO   E CD  
16087 N  N   . ASN   E 648 ? 1.0498 1.0874 1.0494 -0.0745 -0.0649 -0.0083 952  ASN   E N   
16088 C  CA  . ASN   E 648 ? 0.9999 1.0392 1.0003 -0.0776 -0.0689 -0.0101 952  ASN   E CA  
16089 C  C   . ASN   E 648 ? 1.0393 1.0848 1.0386 -0.0741 -0.0703 -0.0118 952  ASN   E C   
16090 O  O   . ASN   E 648 ? 1.0648 1.1157 1.0666 -0.0710 -0.0690 -0.0112 952  ASN   E O   
16091 C  CB  . ASN   E 648 ? 1.0010 1.0452 1.0111 -0.0832 -0.0708 -0.0089 952  ASN   E CB  
16092 C  CG  . ASN   E 648 ? 1.0362 1.0802 1.0455 -0.0860 -0.0754 -0.0110 952  ASN   E CG  
16093 O  OD1 . ASN   E 648 ? 1.0396 1.0787 1.0407 -0.0842 -0.0766 -0.0131 952  ASN   E OD1 
16094 N  ND2 . ASN   E 648 ? 1.0925 1.1415 1.1100 -0.0902 -0.0780 -0.0103 952  ASN   E ND2 
16095 N  N   . TRP   E 649 ? 1.0282 1.0724 1.0237 -0.0745 -0.0729 -0.0139 953  TRP   E N   
16096 C  CA  . TRP   E 649 ? 1.0097 1.0597 1.0048 -0.0716 -0.0738 -0.0154 953  TRP   E CA  
16097 C  C   . TRP   E 649 ? 1.0081 1.0674 1.0117 -0.0737 -0.0752 -0.0144 953  TRP   E C   
16098 O  O   . TRP   E 649 ? 0.9950 1.0552 1.0021 -0.0779 -0.0775 -0.0140 953  TRP   E O   
16099 C  CB  . TRP   E 649 ? 1.0332 1.0784 1.0213 -0.0713 -0.0756 -0.0177 953  TRP   E CB  
16100 C  CG  . TRP   E 649 ? 1.0879 1.1232 1.0669 -0.0693 -0.0746 -0.0189 953  TRP   E CG  
16101 C  CD1 . TRP   E 649 ? 1.1422 1.1692 1.1152 -0.0714 -0.0762 -0.0199 953  TRP   E CD1 
16102 C  CD2 . TRP   E 649 ? 1.1106 1.1429 1.0851 -0.0645 -0.0721 -0.0193 953  TRP   E CD2 
16103 N  NE1 . TRP   E 649 ? 1.0675 1.0867 1.0325 -0.0683 -0.0745 -0.0209 953  TRP   E NE1 
16104 C  CE2 . TRP   E 649 ? 1.0832 1.1055 1.0491 -0.0640 -0.0721 -0.0205 953  TRP   E CE2 
16105 C  CE3 . TRP   E 649 ? 1.0856 1.1222 1.0623 -0.0603 -0.0703 -0.0190 953  TRP   E CE3 
16106 C  CZ2 . TRP   E 649 ? 1.1301 1.1469 1.0895 -0.0594 -0.0701 -0.0212 953  TRP   E CZ2 
16107 C  CZ3 . TRP   E 649 ? 1.0436 1.0748 1.0139 -0.0558 -0.0688 -0.0199 953  TRP   E CZ3 
16108 C  CH2 . TRP   E 649 ? 1.1329 1.1543 1.0947 -0.0553 -0.0686 -0.0209 953  TRP   E CH2 
16109 N  N   . MET   E 650 ? 1.0238 1.0898 1.0307 -0.0706 -0.0741 -0.0141 954  MET   E N   
16110 C  CA  . MET   E 650 ? 0.9971 1.0719 1.0117 -0.0719 -0.0750 -0.0131 954  MET   E CA  
16111 C  C   . MET   E 650 ? 0.9329 1.0125 0.9474 -0.0695 -0.0756 -0.0146 954  MET   E C   
16112 O  O   . MET   E 650 ? 0.9186 0.9987 0.9313 -0.0653 -0.0743 -0.0156 954  MET   E O   
16113 C  CB  . MET   E 650 ? 1.0120 1.0908 1.0316 -0.0705 -0.0730 -0.0112 954  MET   E CB  
16114 C  CG  . MET   E 650 ? 0.9461 1.0337 0.9735 -0.0720 -0.0742 -0.0102 954  MET   E CG  
16115 S  SD  . MET   E 650 ? 0.9600 1.0518 0.9933 -0.0708 -0.0719 -0.0077 954  MET   E SD  
16116 C  CE  . MET   E 650 ? 1.0484 1.1386 1.0764 -0.0645 -0.0705 -0.0092 954  MET   E CE  
16117 N  N   . SER   E 651 ? 0.9378 1.0210 0.9549 -0.0720 -0.0776 -0.0146 955  SER   E N   
16118 C  CA  . SER   E 651 ? 0.9004 0.9862 0.9162 -0.0703 -0.0779 -0.0159 955  SER   E CA  
16119 C  C   . SER   E 651 ? 0.9259 1.0202 0.9485 -0.0694 -0.0776 -0.0152 955  SER   E C   
16120 O  O   . SER   E 651 ? 0.8934 0.9902 0.9160 -0.0667 -0.0767 -0.0162 955  SER   E O   
16121 C  CB  . SER   E 651 ? 0.8736 0.9562 0.8860 -0.0732 -0.0803 -0.0164 955  SER   E CB  
16122 O  OG  . SER   E 651 ? 0.9996 1.0844 1.0105 -0.0715 -0.0800 -0.0173 955  SER   E OG  
16123 N  N   . ALA   E 652 ? 0.9111 1.0097 0.9397 -0.0715 -0.0784 -0.0134 956  ALA   E N   
16124 C  CA  . ALA   E 652 ? 0.9328 1.0391 0.9678 -0.0711 -0.0785 -0.0126 956  ALA   E CA  
16125 C  C   . ALA   E 652 ? 0.9805 1.0897 1.0210 -0.0725 -0.0784 -0.0105 956  ALA   E C   
16126 O  O   . ALA   E 652 ? 0.9330 1.0388 0.9735 -0.0750 -0.0787 -0.0096 956  ALA   E O   
16127 C  CB  . ALA   E 652 ? 0.8871 0.9955 0.9224 -0.0730 -0.0802 -0.0127 956  ALA   E CB  
16128 N  N   . VAL   E 653 ? 1.0290 1.1442 1.0745 -0.0710 -0.0779 -0.0098 957  VAL   E N   
16129 C  CA  . VAL   E 653 ? 1.0124 1.1303 1.0628 -0.0715 -0.0772 -0.0077 957  VAL   E CA  
16130 C  C   . VAL   E 653 ? 0.9762 1.1012 1.0321 -0.0709 -0.0778 -0.0071 957  VAL   E C   
16131 O  O   . VAL   E 653 ? 1.0107 1.1382 1.0666 -0.0690 -0.0780 -0.0083 957  VAL   E O   
16132 C  CB  . VAL   E 653 ? 0.9313 1.0457 0.9790 -0.0682 -0.0749 -0.0076 957  VAL   E CB  
16133 C  CG1 . VAL   E 653 ? 0.9416 1.0591 0.9898 -0.0640 -0.0746 -0.0087 957  VAL   E CG1 
16134 C  CG2 . VAL   E 653 ? 0.9246 1.0389 0.9756 -0.0694 -0.0734 -0.0053 957  VAL   E CG2 
16135 N  N   . GLU   E 654 ? 1.0287 1.1570 1.0898 -0.0723 -0.0777 -0.0051 958  GLU   E N   
16136 C  CA  . GLU   E 654 ? 1.0204 1.1551 1.0865 -0.0723 -0.0787 -0.0044 958  GLU   E CA  
16137 C  C   . GLU   E 654 ? 1.0372 1.1747 1.1085 -0.0729 -0.0778 -0.0021 958  GLU   E C   
16138 O  O   . GLU   E 654 ? 1.0699 1.2057 1.1430 -0.0754 -0.0774 -0.0009 958  GLU   E O   
16139 C  CB  . GLU   E 654 ? 1.0487 1.1848 1.1153 -0.0752 -0.0811 -0.0048 958  GLU   E CB  
16140 C  CG  . GLU   E 654 ? 1.0689 1.2110 1.1402 -0.0754 -0.0822 -0.0040 958  GLU   E CG  
16141 C  CD  . GLU   E 654 ? 1.1027 1.2470 1.1736 -0.0724 -0.0815 -0.0050 958  GLU   E CD  
16142 O  OE1 . GLU   E 654 ? 1.1829 1.3305 1.2572 -0.0704 -0.0808 -0.0043 958  GLU   E OE1 
16143 O  OE2 . GLU   E 654 ? 1.1124 1.2550 1.1799 -0.0720 -0.0815 -0.0065 958  GLU   E OE2 
16144 N  N   . ILE   E 655 ? 1.0150 1.1569 1.0894 -0.0708 -0.0775 -0.0015 959  ILE   E N   
16145 C  CA  . ILE   E 655 ? 1.0435 1.1881 1.1226 -0.0708 -0.0763 0.0008  959  ILE   E CA  
16146 C  C   . ILE   E 655 ? 1.0557 1.2050 1.1403 -0.0741 -0.0783 0.0018  959  ILE   E C   
16147 O  O   . ILE   E 655 ? 1.0091 1.1615 1.0943 -0.0741 -0.0803 0.0010  959  ILE   E O   
16148 C  CB  . ILE   E 655 ? 1.0532 1.1995 1.1321 -0.0666 -0.0753 0.0009  959  ILE   E CB  
16149 C  CG1 . ILE   E 655 ? 0.9972 1.1382 1.0702 -0.0630 -0.0738 -0.0002 959  ILE   E CG1 
16150 C  CG2 . ILE   E 655 ? 1.0447 1.1937 1.1281 -0.0664 -0.0737 0.0034  959  ILE   E CG2 
16151 C  CD1 . ILE   E 655 ? 0.9297 1.0719 1.0015 -0.0590 -0.0746 -0.0017 959  ILE   E CD1 
16152 N  N   . LEU   E 656 ? 1.0436 1.1934 1.1327 -0.0767 -0.0780 0.0034  960  LEU   E N   
16153 C  CA  . LEU   E 656 ? 1.0395 1.1937 1.1343 -0.0797 -0.0805 0.0041  960  LEU   E CA  
16154 C  C   . LEU   E 656 ? 1.1267 1.2863 1.2266 -0.0782 -0.0798 0.0058  960  LEU   E C   
16155 O  O   . LEU   E 656 ? 1.1751 1.3385 1.2765 -0.0782 -0.0819 0.0056  960  LEU   E O   
16156 C  CB  . LEU   E 656 ? 1.0205 1.1734 1.1194 -0.0834 -0.0809 0.0050  960  LEU   E CB  
16157 C  CG  . LEU   E 656 ? 1.0265 1.1750 1.1213 -0.0859 -0.0836 0.0031  960  LEU   E CG  
16158 C  CD1 . LEU   E 656 ? 1.0867 1.2349 1.1874 -0.0899 -0.0852 0.0037  960  LEU   E CD1 
16159 C  CD2 . LEU   E 656 ? 0.9460 1.0961 1.0380 -0.0856 -0.0867 0.0016  960  LEU   E CD2 
16160 N  N   . ASP   E 657 ? 1.1413 1.3007 1.2437 -0.0770 -0.0766 0.0077  961  ASP   E N   
16161 C  CA  . ASP   E 657 ? 1.1345 1.2978 1.2404 -0.0746 -0.0750 0.0094  961  ASP   E CA  
16162 C  C   . ASP   E 657 ? 1.2164 1.3756 1.3179 -0.0709 -0.0713 0.0100  961  ASP   E C   
16163 O  O   . ASP   E 657 ? 1.2415 1.3956 1.3367 -0.0696 -0.0708 0.0086  961  ASP   E O   
16164 C  CB  . ASP   E 657 ? 1.2011 1.3691 1.3160 -0.0772 -0.0751 0.0115  961  ASP   E CB  
16165 C  CG  . ASP   E 657 ? 1.2827 1.4485 1.4013 -0.0783 -0.0715 0.0135  961  ASP   E CG  
16166 O  OD1 . ASP   E 657 ? 1.2984 1.4592 1.4119 -0.0759 -0.0680 0.0138  961  ASP   E OD1 
16167 O  OD2 . ASP   E 657 ? 1.2699 1.4390 1.3969 -0.0814 -0.0720 0.0147  961  ASP   E OD2 
16168 N  N   . ASP   E 658 ? 1.2762 1.4368 1.3802 -0.0687 -0.0686 0.0121  962  ASP   E N   
16169 C  CA  . ASP   E 658 ? 1.3126 1.4683 1.4112 -0.0644 -0.0650 0.0128  962  ASP   E CA  
16170 C  C   . ASP   E 658 ? 1.3294 1.4799 1.4269 -0.0655 -0.0617 0.0140  962  ASP   E C   
16171 O  O   . ASP   E 658 ? 1.3353 1.4797 1.4259 -0.0620 -0.0592 0.0139  962  ASP   E O   
16172 C  CB  . ASP   E 658 ? 1.3411 1.4992 1.4421 -0.0615 -0.0629 0.0149  962  ASP   E CB  
16173 C  CG  . ASP   E 658 ? 1.4037 1.5606 1.4989 -0.0568 -0.0640 0.0135  962  ASP   E CG  
16174 O  OD1 . ASP   E 658 ? 1.4038 1.5597 1.4951 -0.0565 -0.0668 0.0109  962  ASP   E OD1 
16175 O  OD2 . ASP   E 658 ? 1.3998 1.5567 1.4945 -0.0534 -0.0621 0.0150  962  ASP   E OD2 
16176 N  N   . ASP   E 659 ? 1.4337 1.5859 1.5378 -0.0700 -0.0617 0.0150  963  ASP   E N   
16177 C  CA  . ASP   E 659 ? 1.4520 1.5996 1.5568 -0.0714 -0.0581 0.0165  963  ASP   E CA  
16178 C  C   . ASP   E 659 ? 1.4205 1.5655 1.5248 -0.0754 -0.0603 0.0149  963  ASP   E C   
16179 O  O   . ASP   E 659 ? 1.4504 1.5903 1.5539 -0.0764 -0.0575 0.0157  963  ASP   E O   
16180 C  CB  . ASP   E 659 ? 1.5038 1.6554 1.6188 -0.0735 -0.0553 0.0195  963  ASP   E CB  
16181 C  CG  . ASP   E 659 ? 1.5604 1.7138 1.6756 -0.0694 -0.0523 0.0215  963  ASP   E CG  
16182 O  OD1 . ASP   E 659 ? 1.5095 1.6571 1.6165 -0.0648 -0.0491 0.0219  963  ASP   E OD1 
16183 O  OD2 . ASP   E 659 ? 1.5871 1.7473 1.7101 -0.0705 -0.0534 0.0224  963  ASP   E OD2 
16184 N  N   . ASN   E 660 ? 1.3090 1.4569 1.4137 -0.0775 -0.0652 0.0127  964  ASN   E N   
16185 C  CA  . ASN   E 660 ? 1.2409 1.3861 1.3450 -0.0813 -0.0677 0.0111  964  ASN   E CA  
16186 C  C   . ASN   E 660 ? 1.2303 1.3729 1.3259 -0.0796 -0.0702 0.0083  964  ASN   E C   
16187 O  O   . ASN   E 660 ? 1.2100 1.3560 1.3043 -0.0778 -0.0721 0.0073  964  ASN   E O   
16188 C  CB  . ASN   E 660 ? 1.1650 1.3156 1.2779 -0.0856 -0.0712 0.0112  964  ASN   E CB  
16189 C  CG  . ASN   E 660 ? 1.1878 1.3415 1.3108 -0.0874 -0.0685 0.0140  964  ASN   E CG  
16190 O  OD1 . ASN   E 660 ? 1.1592 1.3096 1.2852 -0.0899 -0.0666 0.0149  964  ASN   E OD1 
16191 N  ND2 . ASN   E 660 ? 1.2703 1.4300 1.3987 -0.0863 -0.0682 0.0154  964  ASN   E ND2 
16192 N  N   . PHE   E 661 ? 1.2496 1.3860 1.3397 -0.0800 -0.0699 0.0071  965  PHE   E N   
16193 C  CA  . PHE   E 661 ? 1.2323 1.3658 1.3147 -0.0784 -0.0718 0.0045  965  PHE   E CA  
16194 C  C   . PHE   E 661 ? 1.2027 1.3334 1.2842 -0.0822 -0.0745 0.0031  965  PHE   E C   
16195 O  O   . PHE   E 661 ? 1.2472 1.3756 1.3318 -0.0852 -0.0741 0.0039  965  PHE   E O   
16196 C  CB  . PHE   E 661 ? 1.2409 1.3685 1.3162 -0.0745 -0.0688 0.0042  965  PHE   E CB  
16197 C  CG  . PHE   E 661 ? 1.2764 1.4049 1.3522 -0.0710 -0.0658 0.0060  965  PHE   E CG  
16198 C  CD1 . PHE   E 661 ? 1.2662 1.3987 1.3419 -0.0679 -0.0669 0.0054  965  PHE   E CD1 
16199 C  CD2 . PHE   E 661 ? 1.2764 1.4015 1.3530 -0.0707 -0.0618 0.0083  965  PHE   E CD2 
16200 C  CE1 . PHE   E 661 ? 1.3003 1.4331 1.3758 -0.0644 -0.0645 0.0069  965  PHE   E CE1 
16201 C  CE2 . PHE   E 661 ? 1.3389 1.4641 1.4151 -0.0670 -0.0588 0.0101  965  PHE   E CE2 
16202 C  CZ  . PHE   E 661 ? 1.3568 1.4857 1.4320 -0.0637 -0.0604 0.0093  965  PHE   E CZ  
16203 N  N   . LEU   E 662 ? 1.0400 1.1710 1.1176 -0.0820 -0.0774 0.0009  966  LEU   E N   
16204 C  CA  . LEU   E 662 ? 0.9710 1.0987 1.0463 -0.0850 -0.0803 -0.0006 966  LEU   E CA  
16205 C  C   . LEU   E 662 ? 1.0270 1.1491 1.0935 -0.0828 -0.0799 -0.0026 966  LEU   E C   
16206 O  O   . LEU   E 662 ? 0.9953 1.1185 1.0585 -0.0795 -0.0791 -0.0035 966  LEU   E O   
16207 C  CB  . LEU   E 662 ? 0.9834 1.1153 1.0610 -0.0866 -0.0840 -0.0012 966  LEU   E CB  
16208 C  CG  . LEU   E 662 ? 1.0570 1.1849 1.1301 -0.0888 -0.0875 -0.0031 966  LEU   E CG  
16209 C  CD1 . LEU   E 662 ? 1.0381 1.1656 1.1167 -0.0930 -0.0903 -0.0027 966  LEU   E CD1 
16210 C  CD2 . LEU   E 662 ? 0.9367 1.0670 1.0071 -0.0877 -0.0895 -0.0041 966  LEU   E CD2 
16211 N  N   . GLY   E 663 ? 1.0499 1.1658 1.1129 -0.0847 -0.0804 -0.0034 967  GLY   E N   
16212 C  CA  . GLY   E 663 ? 1.0080 1.1179 1.0625 -0.0826 -0.0798 -0.0053 967  GLY   E CA  
16213 C  C   . GLY   E 663 ? 1.0106 1.1156 1.0610 -0.0852 -0.0826 -0.0069 967  GLY   E C   
16214 O  O   . GLY   E 663 ? 1.0156 1.1208 1.0700 -0.0889 -0.0852 -0.0065 967  GLY   E O   
16215 N  N   . ALA   E 664 ? 0.9731 1.0735 1.0157 -0.0830 -0.0824 -0.0087 968  ALA   E N   
16216 C  CA  . ALA   E 664 ? 0.9961 1.0904 1.0326 -0.0845 -0.0847 -0.0105 968  ALA   E CA  
16217 C  C   . ALA   E 664 ? 1.0072 1.0937 1.0372 -0.0833 -0.0830 -0.0113 968  ALA   E C   
16218 O  O   . ALA   E 664 ? 0.9605 1.0464 0.9873 -0.0795 -0.0804 -0.0117 968  ALA   E O   
16219 C  CB  . ALA   E 664 ? 0.9186 1.0140 0.9508 -0.0827 -0.0857 -0.0119 968  ALA   E CB  
16220 N  N   . GLU   E 665 ? 1.0201 1.1005 1.0482 -0.0863 -0.0847 -0.0117 969  GLU   E N   
16221 C  CA  . GLU   E 665 ? 1.0557 1.1281 1.0777 -0.0853 -0.0829 -0.0123 969  GLU   E CA  
16222 C  C   . GLU   E 665 ? 1.0626 1.1273 1.0792 -0.0878 -0.0860 -0.0140 969  GLU   E C   
16223 O  O   . GLU   E 665 ? 1.0717 1.1371 1.0898 -0.0905 -0.0897 -0.0145 969  GLU   E O   
16224 C  CB  . GLU   E 665 ? 1.0668 1.1384 1.0933 -0.0862 -0.0802 -0.0103 969  GLU   E CB  
16225 C  CG  . GLU   E 665 ? 1.0620 1.1349 1.0967 -0.0913 -0.0819 -0.0089 969  GLU   E CG  
16226 C  CD  . GLU   E 665 ? 1.1322 1.2032 1.1708 -0.0920 -0.0782 -0.0067 969  GLU   E CD  
16227 O  OE1 . GLU   E 665 ? 1.2511 1.3141 1.2841 -0.0916 -0.0766 -0.0070 969  GLU   E OE1 
16228 O  OE2 . GLU   E 665 ? 1.1302 1.2072 1.1768 -0.0925 -0.0764 -0.0045 969  GLU   E OE2 
16229 N  N   . ASN   E 666 ? 1.0684 1.1251 1.0782 -0.0867 -0.0846 -0.0147 970  ASN   E N   
16230 C  CA  . ASN   E 666 ? 1.0905 1.1384 1.0933 -0.0883 -0.0872 -0.0166 970  ASN   E CA  
16231 C  C   . ASN   E 666 ? 1.0747 1.1201 1.0830 -0.0936 -0.0898 -0.0160 970  ASN   E C   
16232 O  O   . ASN   E 666 ? 1.0851 1.1326 1.1007 -0.0953 -0.0878 -0.0140 970  ASN   E O   
16233 C  CB  . ASN   E 666 ? 1.0265 1.0666 1.0203 -0.0852 -0.0847 -0.0176 970  ASN   E CB  
16234 C  CG  . ASN   E 666 ? 1.0742 1.1040 1.0602 -0.0868 -0.0874 -0.0194 970  ASN   E CG  
16235 O  OD1 . ASN   E 666 ? 1.2277 1.2524 1.2153 -0.0901 -0.0882 -0.0190 970  ASN   E OD1 
16236 N  ND2 . ASN   E 666 ? 1.0997 1.1261 1.0773 -0.0843 -0.0884 -0.0214 970  ASN   E ND2 
16237 N  N   . ALA   E 667 ? 1.0774 1.1181 1.0824 -0.0959 -0.0943 -0.0178 971  ALA   E N   
16238 C  CA  . ALA   E 667 ? 1.0841 1.1226 1.0805 -0.0935 -0.0964 -0.0198 971  ALA   E CA  
16239 C  C   . ALA   E 667 ? 1.0527 1.0969 1.0536 -0.0952 -0.1001 -0.0198 971  ALA   E C   
16240 O  O   . ALA   E 667 ? 1.0456 1.0880 1.0500 -0.0991 -0.1045 -0.0203 971  ALA   E O   
16241 C  CB  . ALA   E 667 ? 0.9454 0.9727 0.9320 -0.0939 -0.0988 -0.0220 971  ALA   E CB  
16242 N  N   . PHE   E 668 ? 0.9746 1.0253 0.9757 -0.0925 -0.0986 -0.0194 972  PHE   E N   
16243 C  CA  . PHE   E 668 ? 0.9830 1.0389 0.9877 -0.0936 -0.1018 -0.0193 972  PHE   E CA  
16244 C  C   . PHE   E 668 ? 0.9296 0.9921 0.9468 -0.0973 -0.1033 -0.0176 972  PHE   E C   
16245 O  O   . PHE   E 668 ? 0.9426 1.0051 0.9630 -0.1003 -0.1081 -0.0181 972  PHE   E O   
16246 C  CB  . PHE   E 668 ? 0.9827 1.0311 0.9790 -0.0943 -0.1067 -0.0214 972  PHE   E CB  
16247 C  CG  . PHE   E 668 ? 0.9792 1.0190 0.9628 -0.0910 -0.1053 -0.0232 972  PHE   E CG  
16248 C  CD1 . PHE   E 668 ? 0.9671 1.0082 0.9450 -0.0869 -0.1023 -0.0233 972  PHE   E CD1 
16249 C  CD2 . PHE   E 668 ? 0.9027 0.9330 0.8805 -0.0921 -0.1068 -0.0246 972  PHE   E CD2 
16250 C  CE1 . PHE   E 668 ? 1.0106 1.0439 0.9774 -0.0838 -0.1005 -0.0248 972  PHE   E CE1 
16251 C  CE2 . PHE   E 668 ? 0.9687 0.9910 0.9346 -0.0888 -0.1053 -0.0261 972  PHE   E CE2 
16252 C  CZ  . PHE   E 668 ? 0.9722 0.9962 0.9327 -0.0845 -0.1021 -0.0262 972  PHE   E CZ  
16253 N  N   . ASN   E 669 ? 0.9208 0.9886 0.9448 -0.0969 -0.0992 -0.0156 973  ASN   E N   
16254 C  CA  . ASN   E 669 ? 0.9479 1.0219 0.9838 -0.0999 -0.0994 -0.0136 973  ASN   E CA  
16255 C  C   . ASN   E 669 ? 1.0104 1.0934 1.0514 -0.0976 -0.0963 -0.0118 973  ASN   E C   
16256 O  O   . ASN   E 669 ? 1.0109 1.0949 1.0472 -0.0938 -0.0933 -0.0120 973  ASN   E O   
16257 C  CB  . ASN   E 669 ? 0.9888 1.0591 1.0281 -0.1018 -0.0970 -0.0126 973  ASN   E CB  
16258 C  CG  . ASN   E 669 ? 1.0912 1.1525 1.1269 -0.1048 -0.1007 -0.0144 973  ASN   E CG  
16259 O  OD1 . ASN   E 669 ? 1.0938 1.1543 1.1305 -0.1072 -0.1060 -0.0157 973  ASN   E OD1 
16260 N  ND2 . ASN   E 669 ? 1.0760 1.1301 1.1070 -0.1045 -0.0981 -0.0145 973  ASN   E ND2 
16261 N  N   . LEU   E 670 ? 0.9573 1.0470 1.0084 -0.0998 -0.0974 -0.0103 974  LEU   E N   
16262 C  CA  . LEU   E 670 ? 0.9117 1.0094 0.9689 -0.0980 -0.0941 -0.0083 974  LEU   E CA  
16263 C  C   . LEU   E 670 ? 0.9637 1.0627 1.0289 -0.0997 -0.0912 -0.0061 974  LEU   E C   
16264 O  O   . LEU   E 670 ? 1.0467 1.1429 1.1162 -0.1033 -0.0927 -0.0060 974  LEU   E O   
16265 C  CB  . LEU   E 670 ? 0.9686 1.0732 1.0310 -0.0987 -0.0970 -0.0079 974  LEU   E CB  
16266 C  CG  . LEU   E 670 ? 0.9524 1.0575 1.0079 -0.0960 -0.0980 -0.0092 974  LEU   E CG  
16267 C  CD1 . LEU   E 670 ? 0.9880 1.0848 1.0329 -0.0951 -0.0989 -0.0113 974  LEU   E CD1 
16268 C  CD2 . LEU   E 670 ? 0.9462 1.0552 1.0059 -0.0978 -0.1024 -0.0092 974  LEU   E CD2 
16269 N  N   . PHE   E 671 ? 1.0251 1.1281 1.0924 -0.0970 -0.0870 -0.0044 975  PHE   E N   
16270 C  CA  . PHE   E 671 ? 1.0199 1.1250 1.0950 -0.0980 -0.0836 -0.0019 975  PHE   E CA  
16271 C  C   . PHE   E 671 ? 1.0317 1.1445 1.1113 -0.0957 -0.0817 -0.0002 975  PHE   E C   
16272 O  O   . PHE   E 671 ? 1.0173 1.1327 1.0928 -0.0927 -0.0822 -0.0011 975  PHE   E O   
16273 C  CB  . PHE   E 671 ? 0.9537 1.0521 1.0236 -0.0964 -0.0794 -0.0014 975  PHE   E CB  
16274 C  CG  . PHE   E 671 ? 1.0262 1.1241 1.0887 -0.0913 -0.0768 -0.0018 975  PHE   E CG  
16275 C  CD1 . PHE   E 671 ? 1.0730 1.1747 1.1379 -0.0884 -0.0734 0.0001  975  PHE   E CD1 
16276 C  CD2 . PHE   E 671 ? 1.0747 1.1684 1.1279 -0.0891 -0.0781 -0.0041 975  PHE   E CD2 
16277 C  CE1 . PHE   E 671 ? 1.1041 1.2053 1.1626 -0.0835 -0.0718 -0.0007 975  PHE   E CE1 
16278 C  CE2 . PHE   E 671 ? 1.0797 1.1736 1.1275 -0.0843 -0.0760 -0.0047 975  PHE   E CE2 
16279 C  CZ  . PHE   E 671 ? 1.0853 1.1829 1.1359 -0.0816 -0.0732 -0.0031 975  PHE   E CZ  
16280 N  N   . VAL   E 672 ? 1.0700 1.1861 1.1583 -0.0969 -0.0793 0.0022  976  VAL   E N   
16281 C  CA  . VAL   E 672 ? 1.0695 1.1920 1.1622 -0.0945 -0.0767 0.0041  976  VAL   E CA  
16282 C  C   . VAL   E 672 ? 1.1014 1.2219 1.1968 -0.0938 -0.0713 0.0067  976  VAL   E C   
16283 O  O   . VAL   E 672 ? 1.1420 1.2603 1.2430 -0.0971 -0.0702 0.0078  976  VAL   E O   
16284 C  CB  . VAL   E 672 ? 0.9949 1.1251 1.0968 -0.0968 -0.0799 0.0047  976  VAL   E CB  
16285 C  CG1 . VAL   E 672 ? 1.0234 1.1596 1.1314 -0.0949 -0.0765 0.0072  976  VAL   E CG1 
16286 C  CG2 . VAL   E 672 ? 1.0050 1.1368 1.1023 -0.0964 -0.0845 0.0024  976  VAL   E CG2 
16287 N  N   . CYS   E 673 ? 1.0755 1.1959 1.1667 -0.0893 -0.0678 0.0076  977  CYS   E N   
16288 C  CA  . CYS   E 673 ? 1.1573 1.2752 1.2496 -0.0877 -0.0622 0.0103  977  CYS   E CA  
16289 C  C   . CYS   E 673 ? 1.1821 1.3057 1.2775 -0.0846 -0.0603 0.0120  977  CYS   E C   
16290 O  O   . CYS   E 673 ? 1.2209 1.3492 1.3152 -0.0829 -0.0630 0.0107  977  CYS   E O   
16291 C  CB  . CYS   E 673 ? 1.1621 1.2716 1.2437 -0.0842 -0.0595 0.0096  977  CYS   E CB  
16292 S  SG  . CYS   E 673 ? 1.2779 1.3885 1.3507 -0.0793 -0.0619 0.0070  977  CYS   E SG  
16293 N  N   . GLN   E 674 ? 1.1804 1.3032 1.2795 -0.0839 -0.0553 0.0149  978  GLN   E N   
16294 C  CA  . GLN   E 674 ? 1.2527 1.3814 1.3570 -0.0819 -0.0534 0.0169  978  GLN   E CA  
16295 C  C   . GLN   E 674 ? 1.3325 1.4561 1.4319 -0.0775 -0.0473 0.0192  978  GLN   E C   
16296 O  O   . GLN   E 674 ? 1.3190 1.4358 1.4159 -0.0777 -0.0433 0.0205  978  GLN   E O   
16297 C  CB  . GLN   E 674 ? 1.2389 1.3739 1.3565 -0.0865 -0.0539 0.0185  978  GLN   E CB  
16298 C  CG  . GLN   E 674 ? 1.3113 1.4493 1.4350 -0.0848 -0.0489 0.0218  978  GLN   E CG  
16299 C  CD  . GLN   E 674 ? 1.2846 1.4276 1.4226 -0.0896 -0.0485 0.0236  978  GLN   E CD  
16300 O  OE1 . GLN   E 674 ? 1.2279 1.3747 1.3720 -0.0937 -0.0537 0.0219  978  GLN   E OE1 
16301 N  NE2 . GLN   E 674 ? 1.3778 1.5204 1.5213 -0.0888 -0.0422 0.0270  978  GLN   E NE2 
16302 N  N   . LYS   E 675 ? 1.3999 1.5265 1.4978 -0.0734 -0.0465 0.0199  979  LYS   E N   
16303 C  CA  . LYS   E 675 ? 1.4712 1.5932 1.5644 -0.0687 -0.0408 0.0222  979  LYS   E CA  
16304 C  C   . LYS   E 675 ? 1.5545 1.6786 1.6575 -0.0707 -0.0359 0.0259  979  LYS   E C   
16305 O  O   . LYS   E 675 ? 1.5714 1.7036 1.6841 -0.0727 -0.0372 0.0266  979  LYS   E O   
16306 C  CB  . LYS   E 675 ? 1.4543 1.5786 1.5426 -0.0636 -0.0423 0.0214  979  LYS   E CB  
16307 N  N   . ASP   E 676 ? 1.7629 1.8798 1.8636 -0.0700 -0.0300 0.0282  980  ASP   E N   
16308 C  CA  . ASP   E 676 ? 1.8338 1.9522 1.9442 -0.0717 -0.0242 0.0319  980  ASP   E CA  
16309 C  C   . ASP   E 676 ? 1.8463 1.9674 1.9564 -0.0671 -0.0214 0.0339  980  ASP   E C   
16310 O  O   . ASP   E 676 ? 1.8442 1.9591 1.9427 -0.0610 -0.0192 0.0341  980  ASP   E O   
16311 C  CB  . ASP   E 676 ? 1.9059 2.0145 2.0124 -0.0714 -0.0178 0.0342  980  ASP   E CB  
16312 C  CG  . ASP   E 676 ? 1.8922 1.9975 1.9999 -0.0764 -0.0202 0.0325  980  ASP   E CG  
16313 O  OD1 . ASP   E 676 ? 1.8207 1.9284 1.9263 -0.0781 -0.0269 0.0290  980  ASP   E OD1 
16314 O  OD2 . ASP   E 676 ? 1.8600 1.9599 1.9703 -0.0785 -0.0152 0.0347  980  ASP   E OD2 
16315 N  N   . SER   E 677 ? 1.8329 1.9629 1.9554 -0.0696 -0.0218 0.0352  981  SER   E N   
16316 C  CA  . SER   E 677 ? 1.8967 2.0298 2.0195 -0.0653 -0.0193 0.0370  981  SER   E CA  
16317 C  C   . SER   E 677 ? 1.8526 1.9768 1.9668 -0.0597 -0.0115 0.0400  981  SER   E C   
16318 O  O   . SER   E 677 ? 1.7766 1.9000 1.8854 -0.0544 -0.0098 0.0409  981  SER   E O   
16319 C  CB  . SER   E 677 ? 1.8981 2.0409 2.0371 -0.0691 -0.0190 0.0389  981  SER   E CB  
16320 O  OG  . SER   E 677 ? 1.8454 1.9929 1.9941 -0.0756 -0.0236 0.0373  981  SER   E OG  
16321 N  N   . ALA   E 679 ? 1.6772 1.7877 1.7943 -0.0616 0.0038  0.0464  983  ALA   E N   
16322 C  CA  . ALA   E 679 ? 1.7580 1.8578 1.8579 -0.0541 0.0072  0.0468  983  ALA   E CA  
16323 C  C   . ALA   E 679 ? 1.8409 1.9312 1.9380 -0.0520 0.0173  0.0511  983  ALA   E C   
16324 O  O   . ALA   E 679 ? 1.8354 1.9165 1.9189 -0.0451 0.0216  0.0525  983  ALA   E O   
16325 C  CB  . ALA   E 679 ? 1.6595 1.7624 1.7549 -0.0487 0.0057  0.0466  983  ALA   E CB  
16326 N  N   . THR   E 680 ? 1.8412 1.9333 1.9510 -0.0581 0.0207  0.0531  984  THR   E N   
16327 C  CA  . THR   E 680 ? 1.8306 1.9146 1.9409 -0.0575 0.0308  0.0575  984  THR   E CA  
16328 C  C   . THR   E 680 ? 1.8891 1.9584 1.9793 -0.0507 0.0346  0.0579  984  THR   E C   
16329 O  O   . THR   E 680 ? 1.8766 1.9392 1.9582 -0.0444 0.0413  0.0608  984  THR   E O   
16330 C  CB  . THR   E 680 ? 1.7906 1.8758 1.9136 -0.0654 0.0315  0.0579  984  THR   E CB  
16331 O  OG1 . THR   E 680 ? 1.7569 1.8555 1.8985 -0.0717 0.0268  0.0570  984  THR   E OG1 
16332 C  CG2 . THR   E 680 ? 1.7727 1.8504 1.8984 -0.0652 0.0426  0.0628  984  THR   E CG2 
16333 N  N   . THR   E 681 ? 1.9996 2.0634 2.0816 -0.0517 0.0304  0.0550  985  THR   E N   
16334 C  CA  . THR   E 681 ? 2.0373 2.0869 2.1003 -0.0456 0.0331  0.0549  985  THR   E CA  
16335 C  C   . THR   E 681 ? 2.0157 2.0653 2.0672 -0.0423 0.0241  0.0500  985  THR   E C   
16336 O  O   . THR   E 681 ? 1.9978 2.0572 2.0567 -0.0464 0.0162  0.0467  985  THR   E O   
16337 C  CB  . THR   E 681 ? 2.0320 2.0738 2.0954 -0.0493 0.0371  0.0561  985  THR   E CB  
16338 O  OG1 . THR   E 681 ? 2.0447 2.0754 2.0905 -0.0450 0.0350  0.0539  985  THR   E OG1 
16339 C  CG2 . THR   E 681 ? 1.9643 2.0159 2.0443 -0.0585 0.0319  0.0543  985  THR   E CG2 
16340 N  N   . ASP   E 682 ? 1.9732 2.0115 2.0067 -0.0347 0.0253  0.0496  986  ASP   E N   
16341 C  CA  . ASP   E 682 ? 1.9669 2.0043 1.9898 -0.0315 0.0170  0.0449  986  ASP   E CA  
16342 C  C   . ASP   E 682 ? 1.9291 1.9682 1.9551 -0.0369 0.0117  0.0418  986  ASP   E C   
16343 O  O   . ASP   E 682 ? 1.8896 1.9350 1.9163 -0.0380 0.0037  0.0379  986  ASP   E O   
16344 C  CB  . ASP   E 682 ? 1.9820 2.0052 1.9852 -0.0225 0.0196  0.0450  986  ASP   E CB  
16345 C  CG  . ASP   E 682 ? 2.0395 2.0627 2.0360 -0.0158 0.0189  0.0450  986  ASP   E CG  
16346 O  OD1 . ASP   E 682 ? 2.0525 2.0857 2.0598 -0.0179 0.0184  0.0458  986  ASP   E OD1 
16347 O  OD2 . ASP   E 682 ? 2.1079 2.1205 2.0879 -0.0081 0.0185  0.0439  986  ASP   E OD2 
16348 N  N   . GLU   E 683 ? 1.9404 1.9732 1.9675 -0.0401 0.0164  0.0437  987  GLU   E N   
16349 C  CA  . GLU   E 683 ? 1.8209 1.8550 1.8513 -0.0456 0.0117  0.0410  987  GLU   E CA  
16350 C  C   . GLU   E 683 ? 1.8335 1.8817 1.8789 -0.0522 0.0052  0.0389  987  GLU   E C   
16351 O  O   . GLU   E 683 ? 1.7563 1.8078 1.8005 -0.0538 -0.0020 0.0350  987  GLU   E O   
16352 C  CB  . GLU   E 683 ? 1.7444 1.7708 1.7772 -0.0491 0.0184  0.0440  987  GLU   E CB  
16353 N  N   . GLU   E 684 ? 1.9491 2.0055 2.0084 -0.0557 0.0077  0.0414  988  GLU   E N   
16354 C  CA  . GLU   E 684 ? 1.9456 2.0145 2.0194 -0.0620 0.0017  0.0396  988  GLU   E CA  
16355 C  C   . GLU   E 684 ? 1.9185 1.9945 1.9895 -0.0596 -0.0056 0.0363  988  GLU   E C   
16356 O  O   . GLU   E 684 ? 1.8920 1.9730 1.9654 -0.0629 -0.0125 0.0329  988  GLU   E O   
16357 C  CB  . GLU   E 684 ? 1.9521 2.0279 2.0414 -0.0656 0.0063  0.0431  988  GLU   E CB  
16358 N  N   . ARG   E 685 ? 1.8061 1.8820 1.8716 -0.0538 -0.0040 0.0371  989  ARG   E N   
16359 C  CA  . ARG   E 685 ? 1.7674 1.8498 1.8311 -0.0516 -0.0106 0.0342  989  ARG   E CA  
16360 C  C   . ARG   E 685 ? 1.6633 1.7413 1.7154 -0.0489 -0.0158 0.0303  989  ARG   E C   
16361 O  O   . ARG   E 685 ? 1.6183 1.7029 1.6724 -0.0500 -0.0224 0.0271  989  ARG   E O   
16362 C  CB  . ARG   E 685 ? 1.7718 1.8543 1.8322 -0.0460 -0.0075 0.0361  989  ARG   E CB  
16363 C  CG  . ARG   E 685 ? 1.8637 1.9338 1.9115 -0.0395 -0.0006 0.0386  989  ARG   E CG  
16364 C  CD  . ARG   E 685 ? 1.9304 2.0009 1.9776 -0.0348 0.0037  0.0413  989  ARG   E CD  
16365 N  NE  . ARG   E 685 ? 2.0261 2.0846 2.0567 -0.0265 0.0071  0.0421  989  ARG   E NE  
16366 C  CZ  . ARG   E 685 ? 2.0437 2.1006 2.0683 -0.0205 0.0082  0.0428  989  ARG   E CZ  
16367 N  NH1 . ARG   E 685 ? 2.0443 2.1111 2.0782 -0.0218 0.0065  0.0431  989  ARG   E NH1 
16368 N  NH2 . ARG   E 685 ? 1.9642 2.0088 1.9725 -0.0126 0.0108  0.0432  989  ARG   E NH2 
16369 N  N   . GLN   E 686 ? 1.6293 1.6960 1.6696 -0.0452 -0.0130 0.0304  990  GLN   E N   
16370 C  CA  . GLN   E 686 ? 1.5286 1.5909 1.5587 -0.0425 -0.0178 0.0267  990  GLN   E CA  
16371 C  C   . GLN   E 686 ? 1.5112 1.5753 1.5455 -0.0483 -0.0213 0.0246  990  GLN   E C   
16372 O  O   . GLN   E 686 ? 1.4127 1.4734 1.4393 -0.0465 -0.0251 0.0216  990  GLN   E O   
16373 C  CB  . GLN   E 686 ? 1.4878 1.5368 1.5029 -0.0359 -0.0137 0.0275  990  GLN   E CB  
16374 N  N   . HIS   E 687 ? 1.4922 1.5611 1.5384 -0.0550 -0.0203 0.0261  991  HIS   E N   
16375 C  CA  . HIS   E 687 ? 1.4097 1.4803 1.4601 -0.0606 -0.0242 0.0240  991  HIS   E CA  
16376 C  C   . HIS   E 687 ? 1.3514 1.4337 1.4139 -0.0656 -0.0291 0.0228  991  HIS   E C   
16377 O  O   . HIS   E 687 ? 1.3745 1.4630 1.4468 -0.0676 -0.0273 0.0251  991  HIS   E O   
16378 C  CB  . HIS   E 687 ? 1.4351 1.4997 1.4887 -0.0646 -0.0196 0.0262  991  HIS   E CB  
16379 C  CG  . HIS   E 687 ? 1.3707 1.4372 1.4293 -0.0706 -0.0241 0.0240  991  HIS   E CG  
16380 N  ND1 . HIS   E 687 ? 1.3363 1.4083 1.4084 -0.0773 -0.0246 0.0250  991  HIS   E ND1 
16381 C  CD2 . HIS   E 687 ? 1.3171 1.3805 1.3688 -0.0706 -0.0285 0.0208  991  HIS   E CD2 
16382 C  CE1 . HIS   E 687 ? 1.3201 1.3917 1.3925 -0.0810 -0.0294 0.0223  991  HIS   E CE1 
16383 N  NE2 . HIS   E 687 ? 1.3517 1.4181 1.4118 -0.0771 -0.0315 0.0199  991  HIS   E NE2 
16384 N  N   . LEU   E 688 ? 1.2928 1.3776 1.3541 -0.0673 -0.0351 0.0194  992  LEU   E N   
16385 C  CA  . LEU   E 688 ? 1.2609 1.3554 1.3315 -0.0717 -0.0402 0.0180  992  LEU   E CA  
16386 C  C   . LEU   E 688 ? 1.2585 1.3530 1.3369 -0.0782 -0.0409 0.0182  992  LEU   E C   
16387 O  O   . LEU   E 688 ? 1.3130 1.4021 1.3866 -0.0796 -0.0424 0.0166  992  LEU   E O   
16388 C  CB  . LEU   E 688 ? 1.2164 1.3124 1.2808 -0.0698 -0.0456 0.0144  992  LEU   E CB  
16389 C  CG  . LEU   E 688 ? 1.2529 1.3505 1.3122 -0.0640 -0.0460 0.0137  992  LEU   E CG  
16390 C  CD1 . LEU   E 688 ? 1.2065 1.3029 1.2586 -0.0616 -0.0501 0.0102  992  LEU   E CD1 
16391 C  CD2 . LEU   E 688 ? 1.2774 1.3846 1.3457 -0.0653 -0.0476 0.0145  992  LEU   E CD2 
16392 N  N   . GLN   E 689 ? 1.2455 1.3461 1.3361 -0.0820 -0.0401 0.0202  993  GLN   E N   
16393 C  CA  . GLN   E 689 ? 1.2357 1.3366 1.3355 -0.0882 -0.0407 0.0206  993  GLN   E CA  
16394 C  C   . GLN   E 689 ? 1.2511 1.3569 1.3538 -0.0918 -0.0481 0.0175  993  GLN   E C   
16395 O  O   . GLN   E 689 ? 1.1919 1.3041 1.2948 -0.0905 -0.0518 0.0162  993  GLN   E O   
16396 C  CB  . GLN   E 689 ? 1.2415 1.3471 1.3542 -0.0906 -0.0368 0.0240  993  GLN   E CB  
16397 C  CG  . GLN   E 689 ? 1.3493 1.4517 1.4703 -0.0957 -0.0342 0.0256  993  GLN   E CG  
16398 C  CD  . GLN   E 689 ? 1.4573 1.5479 1.5680 -0.0943 -0.0303 0.0259  993  GLN   E CD  
16399 O  OE1 . GLN   E 689 ? 1.3970 1.4828 1.5003 -0.0949 -0.0340 0.0231  993  GLN   E OE1 
16400 N  NE2 . GLN   E 689 ? 1.3847 1.4700 1.4945 -0.0921 -0.0225 0.0294  993  GLN   E NE2 
16401 N  N   . GLU   E 690 ? 1.2903 1.3923 1.3946 -0.0961 -0.0503 0.0163  994  GLU   E N   
16402 C  CA  . GLU   E 690 ? 1.2549 1.3598 1.3608 -0.0994 -0.0573 0.0134  994  GLU   E CA  
16403 C  C   . GLU   E 690 ? 1.2288 1.3414 1.3491 -0.1039 -0.0598 0.0141  994  GLU   E C   
16404 O  O   . GLU   E 690 ? 1.2475 1.3596 1.3772 -0.1075 -0.0574 0.0159  994  GLU   E O   
16405 C  CB  . GLU   E 690 ? 1.2942 1.3908 1.3945 -0.1016 -0.0589 0.0115  994  GLU   E CB  
16406 C  CG  . GLU   E 690 ? 1.3855 1.4748 1.4717 -0.0971 -0.0576 0.0102  994  GLU   E CG  
16407 C  CD  . GLU   E 690 ? 1.5130 1.5933 1.5938 -0.0993 -0.0586 0.0087  994  GLU   E CD  
16408 O  OE1 . GLU   E 690 ? 1.4107 1.4913 1.4980 -0.1043 -0.0621 0.0078  994  GLU   E OE1 
16409 O  OE2 . GLU   E 690 ? 1.4815 1.5543 1.5517 -0.0957 -0.0560 0.0083  994  GLU   E OE2 
16410 N  N   . VAL   E 691 ? 1.2399 1.3595 1.3621 -0.1038 -0.0646 0.0127  995  VAL   E N   
16411 C  CA  . VAL   E 691 ? 1.2638 1.3912 1.3993 -0.1073 -0.0673 0.0133  995  VAL   E CA  
16412 C  C   . VAL   E 691 ? 1.2153 1.3441 1.3500 -0.1097 -0.0751 0.0101  995  VAL   E C   
16413 O  O   . VAL   E 691 ? 1.2161 1.3517 1.3595 -0.1116 -0.0788 0.0100  995  VAL   E O   
16414 C  CB  . VAL   E 691 ? 1.2437 1.3785 1.3834 -0.1043 -0.0650 0.0153  995  VAL   E CB  
16415 C  CG1 . VAL   E 691 ? 1.2437 1.3750 1.3792 -0.1004 -0.0575 0.0180  995  VAL   E CG1 
16416 C  CG2 . VAL   E 691 ? 1.1971 1.3356 1.3304 -0.1016 -0.0691 0.0133  995  VAL   E CG2 
16417 N  N   . GLY   E 692 ? 1.0575 1.1796 1.1817 -0.1094 -0.0775 0.0076  996  GLY   E N   
16418 C  CA  . GLY   E 692 ? 1.0503 1.1724 1.1720 -0.1111 -0.0845 0.0047  996  GLY   E CA  
16419 C  C   . GLY   E 692 ? 1.0460 1.1598 1.1552 -0.1103 -0.0865 0.0021  996  GLY   E C   
16420 O  O   . GLY   E 692 ? 0.9766 1.0881 1.0758 -0.1063 -0.0844 0.0015  996  GLY   E O   
16421 N  N   . LEU   E 693 ? 1.0621 1.1715 1.1721 -0.1139 -0.0909 0.0002  997  LEU   E N   
16422 C  CA  . LEU   E 693 ? 0.9950 1.0964 1.0932 -0.1133 -0.0935 -0.0025 997  LEU   E CA  
16423 C  C   . LEU   E 693 ? 0.9691 1.0707 1.0661 -0.1149 -0.1008 -0.0050 997  LEU   E C   
16424 O  O   . LEU   E 693 ? 0.9958 1.1025 1.1026 -0.1176 -0.1044 -0.0049 997  LEU   E O   
16425 C  CB  . LEU   E 693 ? 1.0138 1.1070 1.1111 -0.1158 -0.0922 -0.0026 997  LEU   E CB  
16426 C  CG  . LEU   E 693 ? 1.0336 1.1250 1.1317 -0.1144 -0.0849 0.0000  997  LEU   E CG  
16427 C  CD1 . LEU   E 693 ? 1.1043 1.1852 1.1956 -0.1152 -0.0836 -0.0007 997  LEU   E CD1 
16428 C  CD2 . LEU   E 693 ? 1.0388 1.1329 1.1304 -0.1090 -0.0810 0.0010  997  LEU   E CD2 
16429 N  N   . PHE   E 694 ? 0.8895 0.9852 0.9741 -0.1129 -0.1028 -0.0073 998  PHE   E N   
16430 C  CA  . PHE   E 694 ? 0.9611 1.0551 1.0416 -0.1136 -0.1093 -0.0098 998  PHE   E CA  
16431 C  C   . PHE   E 694 ? 1.0020 1.0876 1.0676 -0.1111 -0.1101 -0.0121 998  PHE   E C   
16432 O  O   . PHE   E 694 ? 0.9547 1.0400 1.0131 -0.1073 -0.1061 -0.0118 998  PHE   E O   
16433 C  CB  . PHE   E 694 ? 0.9483 1.0505 1.0323 -0.1122 -0.1107 -0.0092 998  PHE   E CB  
16434 C  CG  . PHE   E 694 ? 0.9334 1.0341 1.0137 -0.1126 -0.1175 -0.0114 998  PHE   E CG  
16435 C  CD1 . PHE   E 694 ? 0.9579 1.0602 1.0468 -0.1161 -0.1231 -0.0121 998  PHE   E CD1 
16436 C  CD2 . PHE   E 694 ? 0.9831 1.0811 1.0517 -0.1093 -0.1180 -0.0127 998  PHE   E CD2 
16437 C  CE1 . PHE   E 694 ? 0.9801 1.0803 1.0645 -0.1159 -0.1296 -0.0142 998  PHE   E CE1 
16438 C  CE2 . PHE   E 694 ? 0.9768 1.0726 1.0408 -0.1091 -0.1238 -0.0145 998  PHE   E CE2 
16439 C  CZ  . PHE   E 694 ? 0.9992 1.0958 1.0705 -0.1123 -0.1298 -0.0153 998  PHE   E CZ  
16440 N  N   . HIS   E 695 ? 0.9706 1.0490 1.0320 -0.1131 -0.1152 -0.0144 999  HIS   E N   
16441 C  CA  . HIS   E 695 ? 0.9385 1.0085 0.9856 -0.1108 -0.1167 -0.0168 999  HIS   E CA  
16442 C  C   . HIS   E 695 ? 0.9974 1.0696 1.0397 -0.1086 -0.1196 -0.0177 999  HIS   E C   
16443 O  O   . HIS   E 695 ? 0.9931 1.0643 1.0362 -0.1102 -0.1257 -0.0190 999  HIS   E O   
16444 C  CB  . HIS   E 695 ? 1.0064 1.0671 1.0508 -0.1137 -0.1213 -0.0189 999  HIS   E CB  
16445 C  CG  . HIS   E 695 ? 1.0037 1.0545 1.0328 -0.1111 -0.1220 -0.0212 999  HIS   E CG  
16446 N  ND1 . HIS   E 695 ? 1.0198 1.0661 1.0418 -0.1087 -0.1170 -0.0210 999  HIS   E ND1 
16447 C  CD2 . HIS   E 695 ? 1.0217 1.0656 1.0407 -0.1102 -0.1270 -0.0237 999  HIS   E CD2 
16448 C  CE1 . HIS   E 695 ? 1.0293 1.0671 1.0382 -0.1065 -0.1187 -0.0232 999  HIS   E CE1 
16449 N  NE2 . HIS   E 695 ? 0.9959 1.0318 1.0024 -0.1073 -0.1246 -0.0248 999  HIS   E NE2 
16450 N  N   . LEU   E 696 ? 0.9641 1.0395 1.0016 -0.1047 -0.1154 -0.0168 1000 LEU   E N   
16451 C  CA  . LEU   E 696 ? 0.9199 0.9960 0.9512 -0.1022 -0.1172 -0.0176 1000 LEU   E CA  
16452 C  C   . LEU   E 696 ? 0.9264 0.9922 0.9450 -0.1013 -0.1208 -0.0202 1000 LEU   E C   
16453 O  O   . LEU   E 696 ? 1.0322 1.0953 1.0485 -0.1022 -0.1264 -0.0215 1000 LEU   E O   
16454 C  CB  . LEU   E 696 ? 0.9431 1.0235 0.9718 -0.0984 -0.1116 -0.0164 1000 LEU   E CB  
16455 C  CG  . LEU   E 696 ? 0.9611 1.0438 0.9860 -0.0962 -0.1125 -0.0165 1000 LEU   E CG  
16456 C  CD1 . LEU   E 696 ? 0.9242 1.0139 0.9589 -0.0984 -0.1158 -0.0155 1000 LEU   E CD1 
16457 C  CD2 . LEU   E 696 ? 0.8590 0.9455 0.8819 -0.0926 -0.1069 -0.0156 1000 LEU   E CD2 
16458 N  N   . GLY   E 697 ? 0.9090 0.9686 0.9188 -0.0992 -0.1176 -0.0209 1001 GLY   E N   
16459 C  CA  . GLY   E 697 ? 0.8944 0.9436 0.8909 -0.0976 -0.1200 -0.0232 1001 GLY   E CA  
16460 C  C   . GLY   E 697 ? 0.9364 0.9845 0.9235 -0.0930 -0.1160 -0.0233 1001 GLY   E C   
16461 O  O   . GLY   E 697 ? 0.9143 0.9536 0.8893 -0.0910 -0.1173 -0.0250 1001 GLY   E O   
16462 N  N   . GLU   E 698 ? 0.9305 0.9869 0.9228 -0.0913 -0.1111 -0.0215 1002 GLU   E N   
16463 C  CA  . GLU   E 698 ? 0.8999 0.9563 0.8859 -0.0871 -0.1063 -0.0214 1002 GLU   E CA  
16464 C  C   . GLU   E 698 ? 0.9596 1.0209 0.9512 -0.0860 -0.1013 -0.0203 1002 GLU   E C   
16465 O  O   . GLU   E 698 ? 0.9292 0.9938 0.9288 -0.0883 -0.1012 -0.0193 1002 GLU   E O   
16466 C  CB  . GLU   E 698 ? 0.9114 0.9729 0.8982 -0.0856 -0.1058 -0.0205 1002 GLU   E CB  
16467 C  CG  . GLU   E 698 ? 0.8847 0.9438 0.8693 -0.0871 -0.1114 -0.0211 1002 GLU   E CG  
16468 C  CD  . GLU   E 698 ? 0.9504 0.9985 0.9206 -0.0850 -0.1132 -0.0230 1002 GLU   E CD  
16469 O  OE1 . GLU   E 698 ? 0.9991 1.0437 0.9623 -0.0819 -0.1087 -0.0233 1002 GLU   E OE1 
16470 O  OE2 . GLU   E 698 ? 0.9653 1.0081 0.9313 -0.0861 -0.1190 -0.0242 1002 GLU   E OE2 
16471 N  N   . PHE   E 699 ? 0.9828 1.0445 0.9704 -0.0823 -0.0970 -0.0204 1003 PHE   E N   
16472 C  CA  . PHE   E 699 ? 0.9414 1.0065 0.9327 -0.0805 -0.0927 -0.0198 1003 PHE   E CA  
16473 C  C   . PHE   E 699 ? 0.9212 0.9953 0.9190 -0.0789 -0.0900 -0.0185 1003 PHE   E C   
16474 O  O   . PHE   E 699 ? 0.9487 1.0232 0.9430 -0.0766 -0.0884 -0.0188 1003 PHE   E O   
16475 C  CB  . PHE   E 699 ? 0.9651 1.0232 0.9474 -0.0775 -0.0902 -0.0213 1003 PHE   E CB  
16476 C  CG  . PHE   E 699 ? 0.9739 1.0351 0.9593 -0.0749 -0.0862 -0.0210 1003 PHE   E CG  
16477 C  CD1 . PHE   E 699 ? 0.9289 0.9954 0.9165 -0.0717 -0.0828 -0.0209 1003 PHE   E CD1 
16478 C  CD2 . PHE   E 699 ? 0.9510 1.0095 0.9371 -0.0757 -0.0860 -0.0210 1003 PHE   E CD2 
16479 C  CE1 . PHE   E 699 ? 0.9132 0.9822 0.9037 -0.0691 -0.0799 -0.0209 1003 PHE   E CE1 
16480 C  CE2 . PHE   E 699 ? 0.9231 0.9837 0.9112 -0.0729 -0.0827 -0.0208 1003 PHE   E CE2 
16481 C  CZ  . PHE   E 699 ? 0.8709 0.9368 0.8611 -0.0695 -0.0800 -0.0209 1003 PHE   E CZ  
16482 N  N   . VAL   E 700 ? 0.8821 0.9631 0.8890 -0.0799 -0.0894 -0.0171 1004 VAL   E N   
16483 C  CA  . VAL   E 700 ? 0.9236 1.0129 0.9371 -0.0788 -0.0878 -0.0159 1004 VAL   E CA  
16484 C  C   . VAL   E 700 ? 0.8621 0.9542 0.8768 -0.0753 -0.0839 -0.0162 1004 VAL   E C   
16485 O  O   . VAL   E 700 ? 0.8936 0.9858 0.9103 -0.0745 -0.0826 -0.0160 1004 VAL   E O   
16486 C  CB  . VAL   E 700 ? 0.9243 1.0197 0.9470 -0.0814 -0.0894 -0.0142 1004 VAL   E CB  
16487 C  CG1 . VAL   E 700 ? 0.9117 1.0152 0.9405 -0.0799 -0.0877 -0.0131 1004 VAL   E CG1 
16488 C  CG2 . VAL   E 700 ? 0.8902 0.9839 0.9129 -0.0846 -0.0937 -0.0142 1004 VAL   E CG2 
16489 N  N   . ASN   E 701 ? 0.8490 0.9431 0.8628 -0.0730 -0.0820 -0.0165 1005 ASN   E N   
16490 C  CA  . ASN   E 701 ? 0.8689 0.9664 0.8853 -0.0697 -0.0786 -0.0169 1005 ASN   E CA  
16491 C  C   . ASN   E 701 ? 0.8668 0.9728 0.8921 -0.0693 -0.0781 -0.0158 1005 ASN   E C   
16492 O  O   . ASN   E 701 ? 0.8451 0.9541 0.8739 -0.0667 -0.0762 -0.0163 1005 ASN   E O   
16493 C  CB  . ASN   E 701 ? 0.8958 0.9911 0.9076 -0.0674 -0.0764 -0.0179 1005 ASN   E CB  
16494 C  CG  . ASN   E 701 ? 0.9476 1.0359 0.9520 -0.0656 -0.0752 -0.0194 1005 ASN   E CG  
16495 O  OD1 . ASN   E 701 ? 0.9808 1.0677 0.9853 -0.0648 -0.0750 -0.0199 1005 ASN   E OD1 
16496 N  ND2 . ASN   E 701 ? 0.8978 0.9809 0.8949 -0.0647 -0.0742 -0.0200 1005 ASN   E ND2 
16497 N  N   . VAL   E 702 ? 0.8228 0.9323 0.8516 -0.0716 -0.0799 -0.0145 1006 VAL   E N   
16498 C  CA  . VAL   E 702 ? 0.8234 0.9402 0.8595 -0.0709 -0.0792 -0.0136 1006 VAL   E CA  
16499 C  C   . VAL   E 702 ? 0.8669 0.9867 0.9067 -0.0737 -0.0818 -0.0121 1006 VAL   E C   
16500 O  O   . VAL   E 702 ? 0.8860 1.0035 0.9227 -0.0756 -0.0838 -0.0119 1006 VAL   E O   
16501 C  CB  . VAL   E 702 ? 0.9083 1.0266 0.9443 -0.0692 -0.0772 -0.0140 1006 VAL   E CB  
16502 C  CG1 . VAL   E 702 ? 0.8959 1.0095 0.9251 -0.0705 -0.0780 -0.0140 1006 VAL   E CG1 
16503 C  CG2 . VAL   E 702 ? 0.9117 1.0372 0.9553 -0.0690 -0.0769 -0.0130 1006 VAL   E CG2 
16504 N  N   . PHE   E 703 ? 0.8168 0.9413 0.8630 -0.0738 -0.0819 -0.0110 1007 PHE   E N   
16505 C  CA  . PHE   E 703 ? 0.9146 1.0434 0.9657 -0.0758 -0.0837 -0.0095 1007 PHE   E CA  
16506 C  C   . PHE   E 703 ? 0.9699 1.1042 1.0251 -0.0742 -0.0827 -0.0090 1007 PHE   E C   
16507 O  O   . PHE   E 703 ? 1.0101 1.1452 1.0657 -0.0718 -0.0806 -0.0100 1007 PHE   E O   
16508 C  CB  . PHE   E 703 ? 0.9215 1.0519 0.9770 -0.0768 -0.0841 -0.0082 1007 PHE   E CB  
16509 C  CG  . PHE   E 703 ? 0.9599 1.0855 1.0130 -0.0792 -0.0855 -0.0083 1007 PHE   E CG  
16510 C  CD1 . PHE   E 703 ? 0.9858 1.1102 1.0387 -0.0822 -0.0885 -0.0081 1007 PHE   E CD1 
16511 C  CD2 . PHE   E 703 ? 0.9479 1.0695 0.9987 -0.0784 -0.0839 -0.0087 1007 PHE   E CD2 
16512 C  CE1 . PHE   E 703 ? 0.9203 1.0400 0.9717 -0.0846 -0.0903 -0.0085 1007 PHE   E CE1 
16513 C  CE2 . PHE   E 703 ? 0.9104 1.0271 0.9593 -0.0808 -0.0851 -0.0088 1007 PHE   E CE2 
16514 C  CZ  . PHE   E 703 ? 0.9618 1.0776 1.0114 -0.0841 -0.0884 -0.0087 1007 PHE   E CZ  
16515 N  N   . CYS   E 704 ? 0.9557 1.0938 1.0149 -0.0756 -0.0843 -0.0077 1008 CYS   E N   
16516 C  CA  . CYS   E 704 ? 0.9903 1.1330 1.0531 -0.0743 -0.0834 -0.0073 1008 CYS   E CA  
16517 C  C   . CYS   E 704 ? 0.9688 1.1151 1.0352 -0.0759 -0.0855 -0.0058 1008 CYS   E C   
16518 O  O   . CYS   E 704 ? 0.9796 1.1239 1.0435 -0.0778 -0.0877 -0.0055 1008 CYS   E O   
16519 C  CB  . CYS   E 704 ? 1.0082 1.1488 1.0673 -0.0732 -0.0818 -0.0083 1008 CYS   E CB  
16520 S  SG  . CYS   E 704 ? 1.0115 1.1546 1.0719 -0.0735 -0.0820 -0.0073 1008 CYS   E SG  
16521 N  N   . HIS   E 705 ? 0.9955 1.1466 1.0674 -0.0748 -0.0850 -0.0049 1009 HIS   E N   
16522 C  CA  . HIS   E 705 ? 0.9467 1.1016 1.0225 -0.0760 -0.0868 -0.0034 1009 HIS   E CA  
16523 C  C   . HIS   E 705 ? 0.9781 1.1334 1.0525 -0.0759 -0.0871 -0.0033 1009 HIS   E C   
16524 O  O   . HIS   E 705 ? 0.9585 1.1141 1.0327 -0.0743 -0.0851 -0.0039 1009 HIS   E O   
16525 C  CB  . HIS   E 705 ? 0.9334 1.0925 1.0147 -0.0745 -0.0859 -0.0024 1009 HIS   E CB  
16526 C  CG  . HIS   E 705 ? 0.9514 1.1102 1.0345 -0.0751 -0.0858 -0.0017 1009 HIS   E CG  
16527 N  ND1 . HIS   E 705 ? 0.9665 1.1264 1.0523 -0.0774 -0.0875 -0.0004 1009 HIS   E ND1 
16528 C  CD2 . HIS   E 705 ? 0.9436 1.1006 1.0260 -0.0736 -0.0841 -0.0019 1009 HIS   E CD2 
16529 C  CE1 . HIS   E 705 ? 1.0609 1.2199 1.1484 -0.0776 -0.0863 0.0003  1009 HIS   E CE1 
16530 N  NE2 . HIS   E 705 ? 1.1109 1.2678 1.1957 -0.0752 -0.0842 -0.0006 1009 HIS   E NE2 
16531 N  N   . GLY   E 706 ? 0.9614 1.1164 1.0349 -0.0776 -0.0896 -0.0025 1010 GLY   E N   
16532 C  CA  . GLY   E 706 ? 0.9473 1.1015 1.0180 -0.0773 -0.0899 -0.0023 1010 GLY   E CA  
16533 C  C   . GLY   E 706 ? 0.9841 1.1358 1.0515 -0.0791 -0.0934 -0.0020 1010 GLY   E C   
16534 O  O   . GLY   E 706 ? 0.9752 1.1264 1.0437 -0.0807 -0.0957 -0.0021 1010 GLY   E O   
16535 N  N   . SER   E 707 ? 0.9722 1.1220 1.0357 -0.0786 -0.0938 -0.0017 1011 SER   E N   
16536 C  CA  . SER   E 707 ? 0.9876 1.1339 1.0464 -0.0795 -0.0975 -0.0017 1011 SER   E CA  
16537 C  C   . SER   E 707 ? 1.0586 1.1999 1.1096 -0.0781 -0.0959 -0.0018 1011 SER   E C   
16538 O  O   . SER   E 707 ? 1.1158 1.2583 1.1678 -0.0768 -0.0922 -0.0014 1011 SER   E O   
16539 C  CB  . SER   E 707 ? 0.9855 1.1366 1.0501 -0.0803 -0.1006 -0.0006 1011 SER   E CB  
16540 O  OG  . SER   E 707 ? 1.0637 1.2112 1.1236 -0.0808 -0.1047 -0.0008 1011 SER   E OG  
16541 N  N   . LEU   E 708 ? 1.0292 1.1643 1.0722 -0.0783 -0.0987 -0.0023 1012 LEU   E N   
16542 C  CA  . LEU   E 708 ? 1.1351 1.2642 1.1692 -0.0766 -0.0971 -0.0022 1012 LEU   E CA  
16543 C  C   . LEU   E 708 ? 1.2192 1.3472 1.2508 -0.0762 -0.1005 -0.0013 1012 LEU   E C   
16544 O  O   . LEU   E 708 ? 1.1921 1.3143 1.2154 -0.0746 -0.0992 -0.0010 1012 LEU   E O   
16545 C  CB  . LEU   E 708 ? 1.1973 1.3180 1.2214 -0.0762 -0.0972 -0.0035 1012 LEU   E CB  
16546 C  CG  . LEU   E 708 ? 1.1113 1.2301 1.1342 -0.0759 -0.0936 -0.0046 1012 LEU   E CG  
16547 C  CD1 . LEU   E 708 ? 1.0307 1.1397 1.0411 -0.0744 -0.0929 -0.0054 1012 LEU   E CD1 
16548 C  CD2 . LEU   E 708 ? 1.0090 1.1330 1.0386 -0.0750 -0.0883 -0.0042 1012 LEU   E CD2 
16549 N  N   . VAL   E 709 ? 1.1860 1.3194 1.2246 -0.0775 -0.1044 -0.0010 1013 VAL   E N   
16550 C  CA  . VAL   E 709 ? 1.2191 1.3529 1.2573 -0.0770 -0.1082 -0.0002 1013 VAL   E CA  
16551 C  C   . VAL   E 709 ? 1.2941 1.4344 1.3394 -0.0764 -0.1058 0.0014  1013 VAL   E C   
16552 O  O   . VAL   E 709 ? 1.3318 1.4755 1.3817 -0.0763 -0.1015 0.0016  1013 VAL   E O   
16553 C  CB  . VAL   E 709 ? 1.1368 1.2729 1.1795 -0.0787 -0.1142 -0.0008 1013 VAL   E CB  
16554 C  CG1 . VAL   E 709 ? 1.0899 1.2187 1.1249 -0.0792 -0.1172 -0.0026 1013 VAL   E CG1 
16555 C  CG2 . VAL   E 709 ? 1.1245 1.2686 1.1790 -0.0804 -0.1133 -0.0004 1013 VAL   E CG2 
16556 N  N   . MET   E 710 ? 1.3023 1.4440 1.3485 -0.0758 -0.1088 0.0022  1014 MET   E N   
16557 C  CA  . MET   E 710 ? 1.3754 1.5218 1.4267 -0.0749 -0.1065 0.0037  1014 MET   E CA  
16558 C  C   . MET   E 710 ? 1.3501 1.5046 1.4119 -0.0756 -0.1087 0.0044  1014 MET   E C   
16559 O  O   . MET   E 710 ? 1.3056 1.4649 1.3734 -0.0751 -0.1061 0.0053  1014 MET   E O   
16560 C  CB  . MET   E 710 ? 1.4408 1.5821 1.4843 -0.0731 -0.1069 0.0045  1014 MET   E CB  
16561 C  CG  . MET   E 710 ? 1.5208 1.6639 1.5666 -0.0720 -0.1026 0.0058  1014 MET   E CG  
16562 S  SD  . MET   E 710 ? 1.6038 1.7383 1.6383 -0.0698 -0.1010 0.0069  1014 MET   E SD  
16563 C  CE  . MET   E 710 ? 1.5200 1.6482 1.5480 -0.0696 -0.0951 0.0063  1014 MET   E CE  
16564 N  N   . PRO   E 719 ? 1.3396 1.5433 1.5015 -0.0925 -0.1228 0.0084  1023 PRO   E N   
16565 C  CA  . PRO   E 719 ? 1.3645 1.5645 1.5268 -0.0956 -0.1273 0.0063  1023 PRO   E CA  
16566 C  C   . PRO   E 719 ? 1.3575 1.5519 1.5135 -0.0967 -0.1239 0.0057  1023 PRO   E C   
16567 O  O   . PRO   E 719 ? 1.2781 1.4718 1.4395 -0.0994 -0.1236 0.0055  1023 PRO   E O   
16568 C  CB  . PRO   E 719 ? 1.3084 1.5039 1.4612 -0.0945 -0.1332 0.0044  1023 PRO   E CB  
16569 C  CG  . PRO   E 719 ? 1.3668 1.5608 1.5101 -0.0913 -0.1295 0.0052  1023 PRO   E CG  
16570 C  CD  . PRO   E 719 ? 1.3193 1.5199 1.4705 -0.0900 -0.1243 0.0077  1023 PRO   E CD  
16571 N  N   . THR   E 720 ? 1.3330 1.5234 1.4776 -0.0945 -0.1212 0.0055  1024 THR   E N   
16572 C  CA  . THR   E 720 ? 1.3102 1.4947 1.4468 -0.0947 -0.1181 0.0047  1024 THR   E CA  
16573 C  C   . THR   E 720 ? 1.3169 1.5026 1.4505 -0.0920 -0.1122 0.0061  1024 THR   E C   
16574 O  O   . THR   E 720 ? 1.4196 1.6062 1.5493 -0.0896 -0.1119 0.0064  1024 THR   E O   
16575 C  CB  . THR   E 720 ? 1.3155 1.4928 1.4402 -0.0945 -0.1217 0.0024  1024 THR   E CB  
16576 O  OG1 . THR   E 720 ? 1.3001 1.4722 1.4166 -0.0940 -0.1180 0.0018  1024 THR   E OG1 
16577 C  CG2 . THR   E 720 ? 1.3474 1.5248 1.4665 -0.0919 -0.1231 0.0025  1024 THR   E CG2 
16578 N  N   . GLN   E 721 ? 1.3572 1.5426 1.4927 -0.0922 -0.1077 0.0069  1025 GLN   E N   
16579 C  CA  . GLN   E 721 ? 1.3464 1.5323 1.4793 -0.0894 -0.1025 0.0080  1025 GLN   E CA  
16580 C  C   . GLN   E 721 ? 1.3680 1.5479 1.4911 -0.0887 -0.1008 0.0066  1025 GLN   E C   
16581 O  O   . GLN   E 721 ? 1.3842 1.5607 1.5065 -0.0900 -0.0995 0.0061  1025 GLN   E O   
16582 C  CB  . GLN   E 721 ? 1.3701 1.5591 1.5108 -0.0894 -0.0983 0.0101  1025 GLN   E CB  
16583 C  CG  . GLN   E 721 ? 1.4793 1.6745 1.6315 -0.0904 -0.0993 0.0117  1025 GLN   E CG  
16584 C  CD  . GLN   E 721 ? 1.5164 1.7133 1.6773 -0.0916 -0.0954 0.0135  1025 GLN   E CD  
16585 O  OE1 . GLN   E 721 ? 1.4363 1.6291 1.5939 -0.0915 -0.0918 0.0137  1025 GLN   E OE1 
16586 N  NE2 . GLN   E 721 ? 1.5777 1.7804 1.7499 -0.0926 -0.0961 0.0150  1025 GLN   E NE2 
16587 N  N   . GLY   E 722 ? 1.2587 1.4372 1.3750 -0.0866 -0.1005 0.0059  1026 GLY   E N   
16588 C  CA  . GLY   E 722 ? 1.1791 1.3531 1.2877 -0.0853 -0.0981 0.0047  1026 GLY   E CA  
16589 C  C   . GLY   E 722 ? 1.0583 1.2269 1.1592 -0.0862 -0.1005 0.0028  1026 GLY   E C   
16590 O  O   . GLY   E 722 ? 1.0935 1.2611 1.1938 -0.0877 -0.1044 0.0022  1026 GLY   E O   
16591 N  N   . SER   E 723 ? 0.9526 1.1173 1.0472 -0.0850 -0.0981 0.0017  1027 SER   E N   
16592 C  CA  . SER   E 723 ? 0.9198 1.0791 1.0065 -0.0853 -0.0996 0.0000  1027 SER   E CA  
16593 C  C   . SER   E 723 ? 1.0116 1.1672 1.0927 -0.0838 -0.0965 -0.0011 1027 SER   E C   
16594 O  O   . SER   E 723 ? 0.9905 1.1473 1.0706 -0.0816 -0.0941 -0.0011 1027 SER   E O   
16595 C  CB  . SER   E 723 ? 0.8796 1.0392 0.9635 -0.0845 -0.1014 0.0001  1027 SER   E CB  
16596 O  OG  . SER   E 723 ? 0.9287 1.0827 1.0040 -0.0839 -0.1013 -0.0012 1027 SER   E OG  
16597 N  N   . VAL   E 724 ? 1.0068 1.1578 1.0848 -0.0850 -0.0967 -0.0021 1028 VAL   E N   
16598 C  CA  . VAL   E 724 ? 0.9555 1.1023 1.0279 -0.0835 -0.0940 -0.0033 1028 VAL   E CA  
16599 C  C   . VAL   E 724 ? 0.9657 1.1063 1.0302 -0.0842 -0.0957 -0.0048 1028 VAL   E C   
16600 O  O   . VAL   E 724 ? 1.0166 1.1543 1.0800 -0.0863 -0.0989 -0.0053 1028 VAL   E O   
16601 C  CB  . VAL   E 724 ? 0.9410 1.0868 1.0153 -0.0838 -0.0922 -0.0032 1028 VAL   E CB  
16602 C  CG1 . VAL   E 724 ? 0.9594 1.1031 1.0298 -0.0811 -0.0891 -0.0042 1028 VAL   E CG1 
16603 C  CG2 . VAL   E 724 ? 0.9113 1.0621 0.9934 -0.0840 -0.0914 -0.0014 1028 VAL   E CG2 
16604 N  N   . LEU   E 725 ? 0.9658 1.1041 1.0249 -0.0822 -0.0936 -0.0057 1029 LEU   E N   
16605 C  CA  . LEU   E 725 ? 0.9744 1.1060 1.0248 -0.0820 -0.0942 -0.0070 1029 LEU   E CA  
16606 C  C   . LEU   E 725 ? 0.9764 1.1040 1.0233 -0.0812 -0.0920 -0.0082 1029 LEU   E C   
16607 O  O   . LEU   E 725 ? 0.9832 1.1134 1.0334 -0.0798 -0.0893 -0.0081 1029 LEU   E O   
16608 C  CB  . LEU   E 725 ? 0.9627 1.0939 1.0095 -0.0801 -0.0924 -0.0070 1029 LEU   E CB  
16609 C  CG  . LEU   E 725 ? 0.9447 1.0780 0.9926 -0.0806 -0.0948 -0.0060 1029 LEU   E CG  
16610 C  CD1 . LEU   E 725 ? 0.9151 1.0479 0.9599 -0.0787 -0.0921 -0.0056 1029 LEU   E CD1 
16611 C  CD2 . LEU   E 725 ? 0.9147 1.0430 0.9575 -0.0822 -0.0993 -0.0066 1029 LEU   E CD2 
16612 N  N   . PHE   E 726 ? 0.9432 1.0639 0.9828 -0.0819 -0.0936 -0.0094 1030 PHE   E N   
16613 C  CA  . PHE   E 726 ? 0.8847 1.0010 0.9200 -0.0808 -0.0914 -0.0106 1030 PHE   E CA  
16614 C  C   . PHE   E 726 ? 0.8834 0.9924 0.9086 -0.0795 -0.0911 -0.0119 1030 PHE   E C   
16615 O  O   . PHE   E 726 ? 0.8889 0.9938 0.9090 -0.0804 -0.0941 -0.0122 1030 PHE   E O   
16616 C  CB  . PHE   E 726 ? 0.8732 0.9875 0.9102 -0.0827 -0.0929 -0.0108 1030 PHE   E CB  
16617 C  CG  . PHE   E 726 ? 0.8762 0.9874 0.9123 -0.0856 -0.0974 -0.0111 1030 PHE   E CG  
16618 C  CD1 . PHE   E 726 ? 0.8829 0.9860 0.9102 -0.0859 -0.0995 -0.0127 1030 PHE   E CD1 
16619 C  CD2 . PHE   E 726 ? 0.8679 0.9839 0.9123 -0.0880 -0.0998 -0.0099 1030 PHE   E CD2 
16620 C  CE1 . PHE   E 726 ? 0.8712 0.9710 0.8979 -0.0886 -0.1046 -0.0133 1030 PHE   E CE1 
16621 C  CE2 . PHE   E 726 ? 0.8818 0.9952 0.9267 -0.0908 -0.1045 -0.0104 1030 PHE   E CE2 
16622 C  CZ  . PHE   E 726 ? 0.8646 0.9698 0.9007 -0.0911 -0.1071 -0.0122 1030 PHE   E CZ  
16623 N  N   . GLY   E 727 ? 0.8779 0.9852 0.9003 -0.0772 -0.0874 -0.0127 1031 GLY   E N   
16624 C  CA  . GLY   E 727 ? 0.8853 0.9854 0.8983 -0.0755 -0.0861 -0.0139 1031 GLY   E CA  
16625 C  C   . GLY   E 727 ? 0.9292 1.0234 0.9374 -0.0755 -0.0863 -0.0152 1031 GLY   E C   
16626 O  O   . GLY   E 727 ? 0.8904 0.9867 0.9030 -0.0756 -0.0856 -0.0153 1031 GLY   E O   
16627 N  N   . THR   E 728 ? 0.9608 1.0468 0.9592 -0.0750 -0.0872 -0.0163 1032 THR   E N   
16628 C  CA  . THR   E 728 ? 0.9157 0.9948 0.9085 -0.0752 -0.0882 -0.0177 1032 THR   E CA  
16629 C  C   . THR   E 728 ? 0.9999 1.0724 0.9832 -0.0721 -0.0852 -0.0188 1032 THR   E C   
16630 O  O   . THR   E 728 ? 0.9708 1.0438 0.9520 -0.0700 -0.0823 -0.0184 1032 THR   E O   
16631 C  CB  . THR   E 728 ? 0.8785 0.9528 0.8682 -0.0781 -0.0936 -0.0182 1032 THR   E CB  
16632 O  OG1 . THR   E 728 ? 0.8621 0.9313 0.8438 -0.0774 -0.0954 -0.0186 1032 THR   E OG1 
16633 C  CG2 . THR   E 728 ? 0.8659 0.9473 0.8660 -0.0811 -0.0961 -0.0169 1032 THR   E CG2 
16634 N  N   . VAL   E 729 ? 0.9743 1.0402 0.9520 -0.0718 -0.0857 -0.0201 1033 VAL   E N   
16635 C  CA  . VAL   E 729 ? 0.9536 1.0132 0.9226 -0.0686 -0.0824 -0.0212 1033 VAL   E CA  
16636 C  C   . VAL   E 729 ? 0.9565 1.0074 0.9139 -0.0678 -0.0839 -0.0218 1033 VAL   E C   
16637 O  O   . VAL   E 729 ? 0.9845 1.0306 0.9346 -0.0646 -0.0803 -0.0223 1033 VAL   E O   
16638 C  CB  . VAL   E 729 ? 0.9396 0.9950 0.9063 -0.0682 -0.0823 -0.0224 1033 VAL   E CB  
16639 C  CG1 . VAL   E 729 ? 0.9824 1.0285 0.9375 -0.0653 -0.0805 -0.0238 1033 VAL   E CG1 
16640 C  CG2 . VAL   E 729 ? 1.0124 1.0752 0.9880 -0.0670 -0.0793 -0.0219 1033 VAL   E CG2 
16641 N  N   . ASN   E 730 ? 0.9328 0.9813 0.8883 -0.0703 -0.0890 -0.0218 1034 ASN   E N   
16642 C  CA  . ASN   E 730 ? 0.9605 1.0002 0.9043 -0.0692 -0.0911 -0.0225 1034 ASN   E CA  
16643 C  C   . ASN   E 730 ? 1.0148 1.0580 0.9597 -0.0687 -0.0904 -0.0211 1034 ASN   E C   
16644 O  O   . ASN   E 730 ? 0.9905 1.0265 0.9257 -0.0678 -0.0927 -0.0215 1034 ASN   E O   
16645 C  CB  . ASN   E 730 ? 0.9936 1.0270 0.9334 -0.0720 -0.0979 -0.0238 1034 ASN   E CB  
16646 C  CG  . ASN   E 730 ? 1.0597 1.0879 0.9969 -0.0724 -0.0985 -0.0252 1034 ASN   E CG  
16647 O  OD1 . ASN   E 730 ? 1.0606 1.0824 0.9892 -0.0694 -0.0954 -0.0261 1034 ASN   E OD1 
16648 N  ND2 . ASN   E 730 ? 1.0445 1.0756 0.9895 -0.0761 -0.1019 -0.0252 1034 ASN   E ND2 
16649 N  N   . GLY   E 731 ? 0.9851 1.0386 0.9411 -0.0690 -0.0875 -0.0196 1035 GLY   E N   
16650 C  CA  . GLY   E 731 ? 0.9773 1.0339 0.9345 -0.0686 -0.0868 -0.0182 1035 GLY   E CA  
16651 C  C   . GLY   E 731 ? 0.9906 1.0488 0.9504 -0.0715 -0.0929 -0.0180 1035 GLY   E C   
16652 O  O   . GLY   E 731 ? 1.0213 1.0796 0.9793 -0.0709 -0.0934 -0.0171 1035 GLY   E O   
16653 N  N   . MET   E 732 ? 0.9790 1.0381 0.9432 -0.0744 -0.0974 -0.0187 1036 MET   E N   
16654 C  CA  . MET   E 732 ? 0.9482 1.0118 0.9193 -0.0774 -0.1025 -0.0182 1036 MET   E CA  
16655 C  C   . MET   E 732 ? 0.9374 1.0124 0.9211 -0.0781 -0.0998 -0.0164 1036 MET   E C   
16656 O  O   . MET   E 732 ? 0.9495 1.0289 0.9384 -0.0774 -0.0957 -0.0160 1036 MET   E O   
16657 C  CB  . MET   E 732 ? 0.9446 1.0057 0.9176 -0.0803 -0.1072 -0.0194 1036 MET   E CB  
16658 C  CG  . MET   E 732 ? 0.9038 0.9683 0.8840 -0.0836 -0.1132 -0.0193 1036 MET   E CG  
16659 S  SD  . MET   E 732 ? 1.0139 1.0914 1.0109 -0.0858 -0.1109 -0.0173 1036 MET   E SD  
16660 C  CE  . MET   E 732 ? 0.9465 1.0262 0.9515 -0.0898 -0.1182 -0.0175 1036 MET   E CE  
16661 N  N   . ILE   E 733 ? 0.9354 1.0147 0.9234 -0.0791 -0.1024 -0.0154 1037 ILE   E N   
16662 C  CA  . ILE   E 733 ? 0.9227 1.0123 0.9223 -0.0799 -0.1005 -0.0137 1037 ILE   E CA  
16663 C  C   . ILE   E 733 ? 0.9153 1.0091 0.9225 -0.0829 -0.1056 -0.0134 1037 ILE   E C   
16664 O  O   . ILE   E 733 ? 0.9778 1.0680 0.9813 -0.0836 -0.1105 -0.0139 1037 ILE   E O   
16665 C  CB  . ILE   E 733 ? 0.8885 0.9803 0.8871 -0.0778 -0.0976 -0.0125 1037 ILE   E CB  
16666 C  CG1 . ILE   E 733 ? 0.9306 1.0185 0.9229 -0.0749 -0.0921 -0.0128 1037 ILE   E CG1 
16667 C  CG2 . ILE   E 733 ? 0.7857 0.8875 0.7959 -0.0785 -0.0961 -0.0111 1037 ILE   E CG2 
16668 C  CD1 . ILE   E 733 ? 0.8588 0.9413 0.8422 -0.0727 -0.0905 -0.0123 1037 ILE   E CD1 
16669 N  N   . GLY   E 734 ? 0.8520 0.9531 0.8698 -0.0843 -0.1044 -0.0124 1038 GLY   E N   
16670 C  CA  . GLY   E 734 ? 0.9185 1.0236 0.9446 -0.0872 -0.1084 -0.0120 1038 GLY   E CA  
16671 C  C   . GLY   E 734 ? 0.9321 1.0467 0.9686 -0.0874 -0.1067 -0.0101 1038 GLY   E C   
16672 O  O   . GLY   E 734 ? 0.9130 1.0313 0.9512 -0.0855 -0.1023 -0.0093 1038 GLY   E O   
16673 N  N   . LEU   E 735 ? 0.9120 1.0305 0.9558 -0.0896 -0.1103 -0.0095 1039 LEU   E N   
16674 C  CA  . LEU   E 735 ? 0.9308 1.0579 0.9844 -0.0897 -0.1091 -0.0077 1039 LEU   E CA  
16675 C  C   . LEU   E 735 ? 0.9329 1.0635 0.9959 -0.0924 -0.1102 -0.0070 1039 LEU   E C   
16676 O  O   . LEU   E 735 ? 0.9957 1.1237 1.0599 -0.0947 -0.1144 -0.0079 1039 LEU   E O   
16677 C  CB  . LEU   E 735 ? 0.9947 1.1239 1.0484 -0.0892 -0.1118 -0.0071 1039 LEU   E CB  
16678 C  CG  . LEU   E 735 ? 0.9121 1.0497 0.9746 -0.0888 -0.1102 -0.0052 1039 LEU   E CG  
16679 C  CD1 . LEU   E 735 ? 0.8772 1.0149 0.9351 -0.0862 -0.1078 -0.0048 1039 LEU   E CD1 
16680 C  CD2 . LEU   E 735 ? 0.9976 1.1391 1.0672 -0.0905 -0.1147 -0.0047 1039 LEU   E CD2 
16681 N  N   . VAL   E 736 ? 0.9708 1.1066 1.0403 -0.0918 -0.1063 -0.0056 1040 VAL   E N   
16682 C  CA  . VAL   E 736 ? 1.0091 1.1490 1.0883 -0.0938 -0.1062 -0.0043 1040 VAL   E CA  
16683 C  C   . VAL   E 736 ? 1.0880 1.2356 1.1748 -0.0930 -0.1051 -0.0025 1040 VAL   E C   
16684 O  O   . VAL   E 736 ? 1.0116 1.1614 1.0967 -0.0904 -0.1022 -0.0019 1040 VAL   E O   
16685 C  CB  . VAL   E 736 ? 0.9359 1.0740 1.0151 -0.0935 -0.1021 -0.0041 1040 VAL   E CB  
16686 C  CG1 . VAL   E 736 ? 0.9845 1.1264 1.0736 -0.0954 -0.1012 -0.0024 1040 VAL   E CG1 
16687 C  CG2 . VAL   E 736 ? 1.0388 1.1690 1.1103 -0.0942 -0.1031 -0.0059 1040 VAL   E CG2 
16688 N  N   . THR   E 737 ? 1.1411 1.2927 1.2365 -0.0950 -0.1076 -0.0016 1041 THR   E N   
16689 C  CA  . THR   E 737 ? 1.1634 1.3223 1.2671 -0.0944 -0.1064 0.0004  1041 THR   E CA  
16690 C  C   . THR   E 737 ? 1.2001 1.3623 1.3144 -0.0967 -0.1060 0.0017  1041 THR   E C   
16691 O  O   . THR   E 737 ? 1.2029 1.3621 1.3191 -0.0995 -0.1083 0.0008  1041 THR   E O   
16692 C  CB  . THR   E 737 ? 1.1445 1.3061 1.2488 -0.0940 -0.1101 0.0003  1041 THR   E CB  
16693 O  OG1 . THR   E 737 ? 1.1896 1.3579 1.3004 -0.0925 -0.1080 0.0023  1041 THR   E OG1 
16694 C  CG2 . THR   E 737 ? 1.2110 1.3726 1.3203 -0.0968 -0.1155 -0.0004 1041 THR   E CG2 
16695 N  N   . SER   E 738 ? 1.2078 1.3760 1.3293 -0.0956 -0.1032 0.0038  1042 SER   E N   
16696 C  CA  . SER   E 738 ? 1.1504 1.3218 1.2821 -0.0973 -0.1012 0.0055  1042 SER   E CA  
16697 C  C   . SER   E 738 ? 1.1941 1.3710 1.3359 -0.0992 -0.1050 0.0061  1042 SER   E C   
16698 O  O   . SER   E 738 ? 1.2689 1.4481 1.4097 -0.0982 -0.1083 0.0056  1042 SER   E O   
16699 C  CB  . SER   E 738 ? 1.1623 1.3362 1.2954 -0.0945 -0.0955 0.0076  1042 SER   E CB  
16700 O  OG  . SER   E 738 ? 1.1931 1.3618 1.3197 -0.0934 -0.0920 0.0072  1042 SER   E OG  
16701 N  N   . LEU   E 739 ? 1.1851 1.3639 1.3369 -0.1017 -0.1042 0.0071  1043 LEU   E N   
16702 C  CA  . LEU   E 739 ? 1.2069 1.3912 1.3705 -0.1039 -0.1078 0.0075  1043 LEU   E CA  
16703 C  C   . LEU   E 739 ? 1.2836 1.4732 1.4585 -0.1039 -0.1027 0.0104  1043 LEU   E C   
16704 O  O   . LEU   E 739 ? 1.2493 1.4366 1.4227 -0.1032 -0.0970 0.0118  1043 LEU   E O   
16705 C  CB  . LEU   E 739 ? 1.2321 1.4132 1.3987 -0.1077 -0.1131 0.0055  1043 LEU   E CB  
16706 C  CG  . LEU   E 739 ? 1.1754 1.3492 1.3298 -0.1078 -0.1178 0.0026  1043 LEU   E CG  
16707 C  CD1 . LEU   E 739 ? 1.1671 1.3353 1.3220 -0.1111 -0.1194 0.0012  1043 LEU   E CD1 
16708 C  CD2 . LEU   E 739 ? 1.1774 1.3527 1.3321 -0.1078 -0.1247 0.0011  1043 LEU   E CD2 
16709 N  N   . SER   E 740 ? 1.4864 1.6829 1.6722 -0.1044 -0.1046 0.0114  1044 SER   E N   
16710 C  CA  . SER   E 740 ? 1.5003 1.7020 1.6990 -0.1050 -0.1000 0.0142  1044 SER   E CA  
16711 C  C   . SER   E 740 ? 1.5042 1.7050 1.7126 -0.1095 -0.1011 0.0138  1044 SER   E C   
16712 O  O   . SER   E 740 ? 1.5099 1.7085 1.7183 -0.1122 -0.1075 0.0113  1044 SER   E O   
16713 C  CB  . SER   E 740 ? 1.5346 1.7443 1.7424 -0.1039 -0.1018 0.0152  1044 SER   E CB  
16714 O  OG  . SER   E 740 ? 1.5320 1.7446 1.7504 -0.1073 -0.1078 0.0140  1044 SER   E OG  
16715 N  N   . GLU   E 741 ? 1.3856 1.5878 1.6024 -0.1101 -0.0947 0.0165  1045 GLU   E N   
16716 C  CA  . GLU   E 741 ? 1.3296 1.5316 1.5579 -0.1146 -0.0950 0.0166  1045 GLU   E CA  
16717 C  C   . GLU   E 741 ? 1.2967 1.5036 1.5363 -0.1176 -0.1028 0.0148  1045 GLU   E C   
16718 O  O   . GLU   E 741 ? 1.2979 1.5017 1.5398 -0.1212 -0.1078 0.0125  1045 GLU   E O   
16719 C  CB  . GLU   E 741 ? 1.2847 1.4895 1.5232 -0.1145 -0.0867 0.0202  1045 GLU   E CB  
16720 C  CG  . GLU   E 741 ? 1.3374 1.5424 1.5897 -0.1194 -0.0863 0.0206  1045 GLU   E CG  
16721 C  CD  . GLU   E 741 ? 1.3740 1.5760 1.6288 -0.1193 -0.0768 0.0239  1045 GLU   E CD  
16722 O  OE1 . GLU   E 741 ? 1.3965 1.6031 1.6578 -0.1170 -0.0707 0.0271  1045 GLU   E OE1 
16723 O  OE2 . GLU   E 741 ? 1.3332 1.5278 1.5831 -0.1212 -0.0753 0.0234  1045 GLU   E OE2 
16724 N  N   . SER   E 742 ? 1.3191 1.5336 1.5657 -0.1160 -0.1044 0.0156  1046 SER   E N   
16725 C  CA  . SER   E 742 ? 1.3275 1.5464 1.5827 -0.1178 -0.1127 0.0136  1046 SER   E CA  
16726 C  C   . SER   E 742 ? 1.3174 1.5297 1.5618 -0.1190 -0.1206 0.0098  1046 SER   E C   
16727 O  O   . SER   E 742 ? 1.2902 1.5010 1.5410 -0.1226 -0.1260 0.0077  1046 SER   E O   
16728 C  CB  . SER   E 742 ? 1.3891 1.6145 1.6454 -0.1143 -0.1139 0.0144  1046 SER   E CB  
16729 O  OG  . SER   E 742 ? 1.3301 1.5553 1.5836 -0.1145 -0.1231 0.0114  1046 SER   E OG  
16730 N  N   . TRP   E 743 ? 1.3127 1.5208 1.5409 -0.1157 -0.1214 0.0088  1047 TRP   E N   
16731 C  CA  . TRP   E 743 ? 1.3038 1.5055 1.5209 -0.1161 -0.1287 0.0054  1047 TRP   E CA  
16732 C  C   . TRP   E 743 ? 1.2852 1.4792 1.4979 -0.1189 -0.1290 0.0038  1047 TRP   E C   
16733 O  O   . TRP   E 743 ? 1.2377 1.4276 1.4489 -0.1210 -0.1361 0.0009  1047 TRP   E O   
16734 C  CB  . TRP   E 743 ? 1.3390 1.5378 1.5403 -0.1120 -0.1280 0.0051  1047 TRP   E CB  
16735 C  CG  . TRP   E 743 ? 1.4040 1.6084 1.6073 -0.1094 -0.1307 0.0055  1047 TRP   E CG  
16736 C  CD1 . TRP   E 743 ? 1.4480 1.6588 1.6564 -0.1070 -0.1261 0.0081  1047 TRP   E CD1 
16737 C  CD2 . TRP   E 743 ? 1.3674 1.5705 1.5664 -0.1087 -0.1386 0.0032  1047 TRP   E CD2 
16738 N  NE1 . TRP   E 743 ? 1.3862 1.6001 1.5943 -0.1050 -0.1307 0.0076  1047 TRP   E NE1 
16739 C  CE2 . TRP   E 743 ? 1.3619 1.5712 1.5642 -0.1059 -0.1383 0.0046  1047 TRP   E CE2 
16740 C  CE3 . TRP   E 743 ? 1.3595 1.5562 1.5514 -0.1097 -0.1459 0.0001  1047 TRP   E CE3 
16741 C  CZ2 . TRP   E 743 ? 1.3501 1.5593 1.5488 -0.1042 -0.1449 0.0031  1047 TRP   E CZ2 
16742 C  CZ3 . TRP   E 743 ? 1.3775 1.5738 1.5654 -0.1078 -0.1525 -0.0014 1047 TRP   E CZ3 
16743 C  CH2 . TRP   E 743 ? 1.3528 1.5553 1.5442 -0.1052 -0.1519 0.0001  1047 TRP   E CH2 
16744 N  N   . TYR   E 744 ? 1.3104 1.5018 1.5206 -0.1189 -0.1216 0.0056  1048 TYR   E N   
16745 C  CA  . TYR   E 744 ? 1.2803 1.4636 1.4851 -0.1213 -0.1217 0.0041  1048 TYR   E CA  
16746 C  C   . TYR   E 744 ? 1.2390 1.4229 1.4570 -0.1260 -0.1263 0.0029  1048 TYR   E C   
16747 O  O   . TYR   E 744 ? 1.2340 1.4110 1.4466 -0.1280 -0.1314 0.0001  1048 TYR   E O   
16748 C  CB  . TYR   E 744 ? 1.2005 1.3814 1.4022 -0.1203 -0.1129 0.0065  1048 TYR   E CB  
16749 C  CG  . TYR   E 744 ? 1.2132 1.3864 1.4118 -0.1230 -0.1123 0.0054  1048 TYR   E CG  
16750 C  CD1 . TYR   E 744 ? 1.1856 1.3505 1.3688 -0.1219 -0.1141 0.0032  1048 TYR   E CD1 
16751 C  CD2 . TYR   E 744 ? 1.2170 1.3908 1.4281 -0.1265 -0.1095 0.0068  1048 TYR   E CD2 
16752 C  CE1 . TYR   E 744 ? 1.2307 1.3881 1.4104 -0.1241 -0.1134 0.0022  1048 TYR   E CE1 
16753 C  CE2 . TYR   E 744 ? 1.1381 1.3043 1.3460 -0.1290 -0.1087 0.0059  1048 TYR   E CE2 
16754 C  CZ  . TYR   E 744 ? 1.2274 1.3854 1.4193 -0.1277 -0.1109 0.0036  1048 TYR   E CZ  
16755 O  OH  . TYR   E 744 ? 1.2909 1.4408 1.4791 -0.1299 -0.1102 0.0027  1048 TYR   E OH  
16756 N  N   . ASN   E 745 ? 1.2150 1.4066 1.4504 -0.1278 -0.1247 0.0048  1049 ASN   E N   
16757 C  CA  . ASN   E 745 ? 1.2585 1.4512 1.5086 -0.1326 -0.1289 0.0037  1049 ASN   E CA  
16758 C  C   . ASN   E 745 ? 1.2416 1.4358 1.4950 -0.1335 -0.1397 0.0005  1049 ASN   E C   
16759 O  O   . ASN   E 745 ? 1.2569 1.4476 1.5148 -0.1370 -0.1458 -0.0021 1049 ASN   E O   
16760 C  CB  . ASN   E 745 ? 1.2082 1.4087 1.4768 -0.1342 -0.1226 0.0071  1049 ASN   E CB  
16761 C  CG  . ASN   E 745 ? 1.2685 1.4654 1.5334 -0.1336 -0.1124 0.0101  1049 ASN   E CG  
16762 O  OD1 . ASN   E 745 ? 1.2979 1.4864 1.5534 -0.1346 -0.1114 0.0091  1049 ASN   E OD1 
16763 N  ND2 . ASN   E 745 ? 1.2848 1.4874 1.5560 -0.1316 -0.1048 0.0137  1049 ASN   E ND2 
16764 N  N   . LEU   E 746 ? 1.2576 1.4563 1.5082 -0.1303 -0.1424 0.0004  1050 LEU   E N   
16765 C  CA  . LEU   E 746 ? 1.2243 1.4226 1.4745 -0.1303 -0.1529 -0.0029 1050 LEU   E CA  
16766 C  C   . LEU   E 746 ? 1.2515 1.4387 1.4845 -0.1301 -0.1580 -0.0062 1050 LEU   E C   
16767 O  O   . LEU   E 746 ? 1.2559 1.4394 1.4910 -0.1323 -0.1663 -0.0093 1050 LEU   E O   
16768 C  CB  . LEU   E 746 ? 1.1568 1.3604 1.4043 -0.1262 -0.1540 -0.0022 1050 LEU   E CB  
16769 C  CG  . LEU   E 746 ? 1.1864 1.3902 1.4333 -0.1253 -0.1645 -0.0051 1050 LEU   E CG  
16770 C  CD1 . LEU   E 746 ? 1.1651 1.3748 1.4107 -0.1213 -0.1634 -0.0035 1050 LEU   E CD1 
16771 C  CD2 . LEU   E 746 ? 1.2499 1.4428 1.4790 -0.1245 -0.1711 -0.0087 1050 LEU   E CD2 
16772 N  N   . LEU   E 747 ? 1.2724 1.4541 1.4881 -0.1270 -0.1534 -0.0056 1051 LEU   E N   
16773 C  CA  . LEU   E 747 ? 1.2897 1.4609 1.4879 -0.1261 -0.1574 -0.0085 1051 LEU   E CA  
16774 C  C   . LEU   E 747 ? 1.3043 1.4687 1.5020 -0.1294 -0.1568 -0.0096 1051 LEU   E C   
16775 O  O   . LEU   E 747 ? 1.3006 1.4564 1.4887 -0.1299 -0.1628 -0.0127 1051 LEU   E O   
16776 C  CB  . LEU   E 747 ? 1.2256 1.3938 1.4073 -0.1218 -0.1522 -0.0074 1051 LEU   E CB  
16777 C  CG  . LEU   E 747 ? 1.1761 1.3474 1.3523 -0.1180 -0.1534 -0.0070 1051 LEU   E CG  
16778 C  CD1 . LEU   E 747 ? 1.1528 1.3211 1.3263 -0.1178 -0.1632 -0.0100 1051 LEU   E CD1 
16779 C  CD2 . LEU   E 747 ? 1.2597 1.4415 1.4495 -0.1176 -0.1495 -0.0041 1051 LEU   E CD2 
16780 N  N   . LEU   E 748 ? 1.3067 1.4736 1.5129 -0.1313 -0.1495 -0.0070 1052 LEU   E N   
16781 C  CA  . LEU   E 748 ? 1.3055 1.4668 1.5148 -0.1351 -0.1493 -0.0079 1052 LEU   E CA  
16782 C  C   . LEU   E 748 ? 1.3511 1.5130 1.5727 -0.1389 -0.1583 -0.0105 1052 LEU   E C   
16783 O  O   . LEU   E 748 ? 1.3738 1.5274 1.5884 -0.1402 -0.1647 -0.0138 1052 LEU   E O   
16784 C  CB  . LEU   E 748 ? 1.2592 1.4241 1.4777 -0.1363 -0.1397 -0.0043 1052 LEU   E CB  
16785 C  CG  . LEU   E 748 ? 1.2712 1.4301 1.4926 -0.1400 -0.1371 -0.0043 1052 LEU   E CG  
16786 C  CD1 . LEU   E 748 ? 1.3074 1.4549 1.5126 -0.1398 -0.1409 -0.0074 1052 LEU   E CD1 
16787 C  CD2 . LEU   E 748 ? 1.2357 1.3959 1.4578 -0.1388 -0.1262 -0.0005 1052 LEU   E CD2 
16788 N  N   . ASP   E 749 ? 1.4147 1.5864 1.6549 -0.1406 -0.1590 -0.0093 1053 ASP   E N   
16789 C  CA  . ASP   E 749 ? 1.4434 1.6169 1.6966 -0.1438 -0.1685 -0.0120 1053 ASP   E CA  
16790 C  C   . ASP   E 749 ? 1.4558 1.6221 1.6947 -0.1417 -0.1785 -0.0160 1053 ASP   E C   
16791 O  O   . ASP   E 749 ? 1.4850 1.6440 1.7218 -0.1440 -0.1855 -0.0193 1053 ASP   E O   
16792 C  CB  . ASP   E 749 ? 1.4632 1.6490 1.7355 -0.1441 -0.1684 -0.0102 1053 ASP   E CB  
16793 C  CG  . ASP   E 749 ? 1.5390 1.7289 1.8325 -0.1490 -0.1742 -0.0117 1053 ASP   E CG  
16794 O  OD1 . ASP   E 749 ? 1.5927 1.7848 1.8996 -0.1526 -0.1685 -0.0097 1053 ASP   E OD1 
16795 O  OD2 . ASP   E 749 ? 1.5866 1.7774 1.8838 -0.1491 -0.1846 -0.0148 1053 ASP   E OD2 
16796 N  N   . MET   E 750 ? 1.3626 1.5303 1.5909 -0.1372 -0.1791 -0.0158 1054 MET   E N   
16797 C  CA  . MET   E 750 ? 1.3360 1.4958 1.5480 -0.1344 -0.1872 -0.0191 1054 MET   E CA  
16798 C  C   . MET   E 750 ? 1.3423 1.4895 1.5392 -0.1350 -0.1890 -0.0216 1054 MET   E C   
16799 O  O   . MET   E 750 ? 1.3606 1.5013 1.5555 -0.1362 -0.1982 -0.0252 1054 MET   E O   
16800 C  CB  . MET   E 750 ? 1.3220 1.4833 1.5215 -0.1293 -0.1835 -0.0174 1054 MET   E CB  
16801 C  CG  . MET   E 750 ? 1.3250 1.4925 1.5299 -0.1273 -0.1891 -0.0179 1054 MET   E CG  
16802 S  SD  . MET   E 750 ? 1.5302 1.6890 1.7285 -0.1271 -0.2032 -0.0230 1054 MET   E SD  
16803 C  CE  . MET   E 750 ? 1.4975 1.6585 1.6881 -0.1219 -0.2071 -0.0230 1054 MET   E CE  
16804 N  N   . GLN   E 751 ? 1.3279 1.4713 1.5144 -0.1339 -0.1806 -0.0197 1055 GLN   E N   
16805 C  CA  . GLN   E 751 ? 1.3009 1.4323 1.4719 -0.1338 -0.1814 -0.0218 1055 GLN   E CA  
16806 C  C   . GLN   E 751 ? 1.3313 1.4576 1.5093 -0.1381 -0.1884 -0.0248 1055 GLN   E C   
16807 O  O   . GLN   E 751 ? 1.2999 1.4161 1.4658 -0.1374 -0.1954 -0.0282 1055 GLN   E O   
16808 C  CB  . GLN   E 751 ? 1.3152 1.4453 1.4808 -0.1333 -0.1710 -0.0192 1055 GLN   E CB  
16809 C  CG  . GLN   E 751 ? 1.2861 1.4156 1.4369 -0.1285 -0.1652 -0.0176 1055 GLN   E CG  
16810 C  CD  . GLN   E 751 ? 1.2563 1.3834 1.4017 -0.1280 -0.1562 -0.0156 1055 GLN   E CD  
16811 O  OE1 . GLN   E 751 ? 1.1951 1.3180 1.3430 -0.1308 -0.1549 -0.0160 1055 GLN   E OE1 
16812 N  NE2 . GLN   E 751 ? 1.2356 1.3651 1.3736 -0.1244 -0.1500 -0.0137 1055 GLN   E NE2 
16813 N  N   . ASN   E 752 ? 1.3672 1.4996 1.5644 -0.1425 -0.1862 -0.0234 1056 ASN   E N   
16814 C  CA  . ASN   E 752 ? 1.3636 1.4915 1.5697 -0.1472 -0.1924 -0.0260 1056 ASN   E CA  
16815 C  C   . ASN   E 752 ? 1.3564 1.4816 1.5628 -0.1471 -0.2050 -0.0301 1056 ASN   E C   
16816 O  O   . ASN   E 752 ? 1.3446 1.4597 1.5435 -0.1481 -0.2122 -0.0337 1056 ASN   E O   
16817 C  CB  . ASN   E 752 ? 1.3678 1.5045 1.5974 -0.1518 -0.1879 -0.0236 1056 ASN   E CB  
16818 C  CG  . ASN   E 752 ? 1.4889 1.6258 1.7172 -0.1521 -0.1758 -0.0198 1056 ASN   E CG  
16819 O  OD1 . ASN   E 752 ? 1.5244 1.6560 1.7550 -0.1553 -0.1736 -0.0198 1056 ASN   E OD1 
16820 N  ND2 . ASN   E 752 ? 1.4294 1.5722 1.6539 -0.1485 -0.1681 -0.0165 1056 ASN   E ND2 
16821 N  N   . ARG   E 753 ? 1.3632 1.4972 1.5784 -0.1457 -0.2082 -0.0297 1057 ARG   E N   
16822 C  CA  . ARG   E 753 ? 1.3367 1.4688 1.5531 -0.1452 -0.2207 -0.0336 1057 ARG   E CA  
16823 C  C   . ARG   E 753 ? 1.3397 1.4586 1.5310 -0.1411 -0.2260 -0.0366 1057 ARG   E C   
16824 O  O   . ARG   E 753 ? 1.2770 1.3870 1.4638 -0.1420 -0.2354 -0.0407 1057 ARG   E O   
16825 C  CB  . ARG   E 753 ? 1.2545 1.3978 1.4815 -0.1433 -0.2219 -0.0323 1057 ARG   E CB  
16826 N  N   . LEU   E 754 ? 1.3123 1.4295 1.4868 -0.1365 -0.2198 -0.0347 1058 LEU   E N   
16827 C  CA  . LEU   E 754 ? 1.2840 1.3885 1.4344 -0.1324 -0.2234 -0.0371 1058 LEU   E CA  
16828 C  C   . LEU   E 754 ? 1.3314 1.4244 1.4731 -0.1343 -0.2246 -0.0393 1058 LEU   E C   
16829 O  O   . LEU   E 754 ? 1.3691 1.4513 1.4997 -0.1332 -0.2333 -0.0431 1058 LEU   E O   
16830 C  CB  . LEU   E 754 ? 1.2635 1.3684 1.3995 -0.1279 -0.2149 -0.0343 1058 LEU   E CB  
16831 C  CG  . LEU   E 754 ? 1.3105 1.4257 1.4528 -0.1256 -0.2133 -0.0320 1058 LEU   E CG  
16832 C  CD1 . LEU   E 754 ? 1.3312 1.4566 1.4850 -0.1271 -0.2025 -0.0278 1058 LEU   E CD1 
16833 C  CD2 . LEU   E 754 ? 1.3397 1.4487 1.4615 -0.1201 -0.2129 -0.0321 1058 LEU   E CD2 
16834 N  N   . ASN   E 755 ? 1.3316 1.4262 1.4778 -0.1368 -0.2159 -0.0369 1059 ASN   E N   
16835 C  CA  . ASN   E 755 ? 1.2843 1.3675 1.4207 -0.1381 -0.2162 -0.0388 1059 ASN   E CA  
16836 C  C   . ASN   E 755 ? 1.2876 1.3648 1.4299 -0.1414 -0.2273 -0.0429 1059 ASN   E C   
16837 O  O   . ASN   E 755 ? 1.3281 1.3926 1.4563 -0.1408 -0.2313 -0.0458 1059 ASN   E O   
16838 C  CB  . ASN   E 755 ? 1.2188 1.3053 1.3623 -0.1409 -0.2060 -0.0357 1059 ASN   E CB  
16839 C  CG  . ASN   E 755 ? 1.2712 1.3528 1.3968 -0.1371 -0.1978 -0.0340 1059 ASN   E CG  
16840 O  OD1 . ASN   E 755 ? 1.2322 1.3057 1.3392 -0.1330 -0.2001 -0.0356 1059 ASN   E OD1 
16841 N  ND2 . ASN   E 755 ? 1.2860 1.3723 1.4168 -0.1382 -0.1880 -0.0307 1059 ASN   E ND2 
16842 N  N   . LYS   E 756 ? 1.3092 1.3950 1.4722 -0.1447 -0.2327 -0.0435 1060 LYS   E N   
16843 C  CA  . LYS   E 756 ? 1.3084 1.3885 1.4778 -0.1476 -0.2445 -0.0479 1060 LYS   E CA  
16844 C  C   . LYS   E 756 ? 1.3225 1.3927 1.4742 -0.1431 -0.2550 -0.0519 1060 LYS   E C   
16845 O  O   . LYS   E 756 ? 1.3979 1.4577 1.5448 -0.1441 -0.2644 -0.0561 1060 LYS   E O   
16846 C  CB  . LYS   E 756 ? 1.1993 1.2919 1.3966 -0.1521 -0.2477 -0.0476 1060 LYS   E CB  
16847 N  N   . VAL   E 757 ? 1.3009 1.3729 1.4413 -0.1380 -0.2533 -0.0506 1061 VAL   E N   
16848 C  CA  . VAL   E 757 ? 1.2979 1.3615 1.4230 -0.1334 -0.2630 -0.0539 1061 VAL   E CA  
16849 C  C   . VAL   E 757 ? 1.3515 1.4023 1.4483 -0.1281 -0.2598 -0.0541 1061 VAL   E C   
16850 O  O   . VAL   E 757 ? 1.4423 1.4811 1.5229 -0.1247 -0.2683 -0.0576 1061 VAL   E O   
16851 C  CB  . VAL   E 757 ? 1.3145 1.3884 1.4472 -0.1311 -0.2647 -0.0526 1061 VAL   E CB  
16852 C  CG1 . VAL   E 757 ? 1.3279 1.4165 1.4899 -0.1361 -0.2647 -0.0513 1061 VAL   E CG1 
16853 C  CG2 . VAL   E 757 ? 1.3529 1.4300 1.4738 -0.1268 -0.2543 -0.0487 1061 VAL   E CG2 
16854 N  N   . ILE   E 758 ? 1.3461 1.3991 1.4366 -0.1271 -0.2478 -0.0505 1062 ILE   E N   
16855 C  CA  . ILE   E 758 ? 1.3658 1.4075 1.4311 -0.1221 -0.2440 -0.0505 1062 ILE   E CA  
16856 C  C   . ILE   E 758 ? 1.3848 1.4137 1.4402 -0.1233 -0.2465 -0.0532 1062 ILE   E C   
16857 O  O   . ILE   E 758 ? 1.4099 1.4408 1.4781 -0.1282 -0.2456 -0.0533 1062 ILE   E O   
16858 C  CB  . ILE   E 758 ? 1.3999 1.4481 1.4621 -0.1204 -0.2309 -0.0460 1062 ILE   E CB  
16859 C  CG1 . ILE   E 758 ? 1.3942 1.4576 1.4722 -0.1209 -0.2271 -0.0428 1062 ILE   E CG1 
16860 C  CG2 . ILE   E 758 ? 1.3698 1.4073 1.4067 -0.1146 -0.2281 -0.0461 1062 ILE   E CG2 
16861 C  CD1 . ILE   E 758 ? 1.2992 1.3637 1.3740 -0.1174 -0.2335 -0.0437 1062 ILE   E CD1 
16862 N  N   . LYS   E 759 ? 1.3839 1.3989 1.4159 -0.1185 -0.2491 -0.0552 1063 LYS   E N   
16863 C  CA  . LYS   E 759 ? 1.3861 1.3872 1.4054 -0.1186 -0.2516 -0.0580 1063 LYS   E CA  
16864 C  C   . LYS   E 759 ? 1.4909 1.4895 1.4986 -0.1167 -0.2398 -0.0552 1063 LYS   E C   
16865 O  O   . LYS   E 759 ? 1.5485 1.5475 1.5446 -0.1123 -0.2336 -0.0531 1063 LYS   E O   
16866 C  CB  . LYS   E 759 ? 1.3339 1.3200 1.3337 -0.1141 -0.2618 -0.0621 1063 LYS   E CB  
16867 N  N   . SER   E 760 ? 1.4858 1.4822 1.4977 -0.1202 -0.2368 -0.0553 1064 SER   E N   
16868 C  CA  . SER   E 760 ? 1.4300 1.4223 1.4305 -0.1184 -0.2270 -0.0534 1064 SER   E CA  
16869 C  C   . SER   E 760 ? 1.4464 1.4214 1.4234 -0.1144 -0.2309 -0.0565 1064 SER   E C   
16870 O  O   . SER   E 760 ? 1.5062 1.4717 1.4805 -0.1156 -0.2405 -0.0603 1064 SER   E O   
16871 C  CB  . SER   E 760 ? 1.3935 1.3903 1.4083 -0.1237 -0.2224 -0.0521 1064 SER   E CB  
16872 O  OG  . SER   E 760 ? 1.3759 1.3673 1.3790 -0.1219 -0.2142 -0.0508 1064 SER   E OG  
16873 N  N   . VAL   E 761 ? 1.3123 1.2828 1.2725 -0.1096 -0.2233 -0.0549 1065 VAL   E N   
16874 C  CA  . VAL   E 761 ? 1.3334 1.2872 1.2704 -0.1052 -0.2256 -0.0574 1065 VAL   E CA  
16875 C  C   . VAL   E 761 ? 1.3833 1.3303 1.3180 -0.1073 -0.2232 -0.0583 1065 VAL   E C   
16876 O  O   . VAL   E 761 ? 1.4497 1.3891 1.3690 -0.1037 -0.2173 -0.0578 1065 VAL   E O   
16877 C  CB  . VAL   E 761 ? 1.2975 1.2489 1.2177 -0.0990 -0.2183 -0.0554 1065 VAL   E CB  
16878 C  CG1 . VAL   E 761 ? 1.2332 1.1680 1.1299 -0.0943 -0.2175 -0.0572 1065 VAL   E CG1 
16879 C  CG2 . VAL   E 761 ? 1.3422 1.2949 1.2599 -0.0964 -0.2233 -0.0557 1065 VAL   E CG2 
16880 N  N   . GLY   E 762 ? 1.2965 1.2458 1.2464 -0.1129 -0.2278 -0.0595 1066 GLY   E N   
16881 C  CA  . GLY   E 762 ? 1.2684 1.2098 1.2154 -0.1149 -0.2266 -0.0607 1066 GLY   E CA  
16882 C  C   . GLY   E 762 ? 1.3393 1.2883 1.3090 -0.1219 -0.2292 -0.0607 1066 GLY   E C   
16883 O  O   . GLY   E 762 ? 1.3737 1.3195 1.3470 -0.1250 -0.2270 -0.0608 1066 GLY   E O   
16884 N  N   . LYS   E 763 ? 1.3006 1.2599 1.2862 -0.1244 -0.2336 -0.0604 1067 LYS   E N   
16885 C  CA  . LYS   E 763 ? 1.2768 1.2454 1.2865 -0.1310 -0.2354 -0.0599 1067 LYS   E CA  
16886 C  C   . LYS   E 763 ? 1.2630 1.2410 1.2834 -0.1334 -0.2236 -0.0557 1067 LYS   E C   
16887 O  O   . LYS   E 763 ? 1.2343 1.2147 1.2691 -0.1386 -0.2229 -0.0553 1067 LYS   E O   
16888 C  CB  . LYS   E 763 ? 1.1722 1.1302 1.1837 -0.1346 -0.2451 -0.0641 1067 LYS   E CB  
16889 N  N   . ILE   E 764 ? 1.2379 1.2209 1.2510 -0.1295 -0.2143 -0.0525 1068 ILE   E N   
16890 C  CA  . ILE   E 764 ? 1.1913 1.1840 1.2140 -0.1309 -0.2033 -0.0484 1068 ILE   E CA  
16891 C  C   . ILE   E 764 ? 1.1927 1.2006 1.2362 -0.1338 -0.2022 -0.0459 1068 ILE   E C   
16892 O  O   . ILE   E 764 ? 1.2248 1.2384 1.2687 -0.1316 -0.2042 -0.0456 1068 ILE   E O   
16893 C  CB  . ILE   E 764 ? 1.1785 1.1707 1.1863 -0.1255 -0.1946 -0.0463 1068 ILE   E CB  
16894 C  CG1 . ILE   E 764 ? 1.1234 1.1023 1.1137 -0.1230 -0.1930 -0.0478 1068 ILE   E CG1 
16895 C  CG2 . ILE   E 764 ? 1.1783 1.1826 1.1978 -0.1265 -0.1845 -0.0421 1068 ILE   E CG2 
16896 C  CD1 . ILE   E 764 ? 1.1224 1.0980 1.0948 -0.1167 -0.1880 -0.0471 1068 ILE   E CD1 
16897 N  N   . GLU   E 765 ? 1.2235 1.2377 1.2838 -0.1385 -0.1984 -0.0441 1069 GLU   E N   
16898 C  CA  . GLU   E 765 ? 1.2304 1.2586 1.3110 -0.1413 -0.1970 -0.0417 1069 GLU   E CA  
16899 C  C   . GLU   E 765 ? 1.2049 1.2422 1.2846 -0.1382 -0.1872 -0.0377 1069 GLU   E C   
16900 O  O   . GLU   E 765 ? 1.2011 1.2368 1.2747 -0.1369 -0.1791 -0.0358 1069 GLU   E O   
16901 C  CB  . GLU   E 765 ? 1.2590 1.2901 1.3581 -0.1473 -0.1961 -0.0409 1069 GLU   E CB  
16902 C  CG  . GLU   E 765 ? 1.3506 1.3927 1.4713 -0.1510 -0.2000 -0.0405 1069 GLU   E CG  
16903 C  CD  . GLU   E 765 ? 1.5443 1.5930 1.6843 -0.1560 -0.1939 -0.0377 1069 GLU   E CD  
16904 O  OE1 . GLU   E 765 ? 1.6046 1.6652 1.7628 -0.1581 -0.1927 -0.0356 1069 GLU   E OE1 
16905 O  OE2 . GLU   E 765 ? 1.6091 1.6506 1.7453 -0.1575 -0.1900 -0.0374 1069 GLU   E OE2 
16906 N  N   . HIS   E 766 ? 1.2079 1.2546 1.2935 -0.1368 -0.1882 -0.0367 1070 HIS   E N   
16907 C  CA  . HIS   E 766 ? 1.1315 1.1863 1.2152 -0.1335 -0.1798 -0.0333 1070 HIS   E CA  
16908 C  C   . HIS   E 766 ? 1.1076 1.1680 1.2008 -0.1354 -0.1705 -0.0299 1070 HIS   E C   
16909 O  O   . HIS   E 766 ? 1.1080 1.1681 1.1924 -0.1323 -0.1629 -0.0281 1070 HIS   E O   
16910 C  CB  . HIS   E 766 ? 1.1956 1.2602 1.2879 -0.1328 -0.1827 -0.0326 1070 HIS   E CB  
16911 C  CG  . HIS   E 766 ? 1.1557 1.2285 1.2467 -0.1295 -0.1749 -0.0293 1070 HIS   E CG  
16912 N  ND1 . HIS   E 766 ? 1.0905 1.1743 1.1963 -0.1311 -0.1687 -0.0259 1070 HIS   E ND1 
16913 C  CD2 . HIS   E 766 ? 1.1069 1.1783 1.1839 -0.1247 -0.1723 -0.0288 1070 HIS   E CD2 
16914 C  CE1 . HIS   E 766 ? 1.0912 1.1798 1.1918 -0.1274 -0.1632 -0.0238 1070 HIS   E CE1 
16915 N  NE2 . HIS   E 766 ? 1.0354 1.1170 1.1193 -0.1237 -0.1652 -0.0255 1070 HIS   E NE2 
16916 N  N   . SER   E 767 ? 1.1274 1.1928 1.2385 -0.1402 -0.1709 -0.0291 1071 SER   E N   
16917 C  CA  . SER   E 767 ? 1.1180 1.1868 1.2375 -0.1421 -0.1622 -0.0259 1071 SER   E CA  
16918 C  C   . SER   E 767 ? 1.0850 1.1443 1.1900 -0.1402 -0.1572 -0.0260 1071 SER   E C   
16919 O  O   . SER   E 767 ? 1.0621 1.1240 1.1632 -0.1376 -0.1490 -0.0234 1071 SER   E O   
16920 C  CB  . SER   E 767 ? 1.2621 1.3332 1.4004 -0.1480 -0.1646 -0.0260 1071 SER   E CB  
16921 O  OG  . SER   E 767 ? 1.3535 1.4329 1.5052 -0.1495 -0.1704 -0.0265 1071 SER   E OG  
16922 N  N   . PHE   E 768 ? 1.0922 1.1402 1.1888 -0.1413 -0.1624 -0.0291 1072 PHE   E N   
16923 C  CA  . PHE   E 768 ? 1.1090 1.1472 1.1917 -0.1396 -0.1582 -0.0294 1072 PHE   E CA  
16924 C  C   . PHE   E 768 ? 1.1000 1.1380 1.1674 -0.1337 -0.1535 -0.0286 1072 PHE   E C   
16925 O  O   . PHE   E 768 ? 1.0758 1.1126 1.1378 -0.1317 -0.1461 -0.0269 1072 PHE   E O   
16926 C  CB  . PHE   E 768 ? 1.1506 1.1762 1.2250 -0.1410 -0.1659 -0.0333 1072 PHE   E CB  
16927 C  CG  . PHE   E 768 ? 1.0703 1.0850 1.1288 -0.1386 -0.1622 -0.0339 1072 PHE   E CG  
16928 C  CD1 . PHE   E 768 ? 1.0602 1.0713 1.1228 -0.1412 -0.1578 -0.0328 1072 PHE   E CD1 
16929 C  CD2 . PHE   E 768 ? 1.1199 1.1280 1.1596 -0.1336 -0.1629 -0.0355 1072 PHE   E CD2 
16930 C  CE1 . PHE   E 768 ? 1.1170 1.1180 1.1650 -0.1388 -0.1545 -0.0334 1072 PHE   E CE1 
16931 C  CE2 . PHE   E 768 ? 1.1085 1.1070 1.1343 -0.1312 -0.1593 -0.0361 1072 PHE   E CE2 
16932 C  CZ  . PHE   E 768 ? 1.1294 1.1244 1.1593 -0.1337 -0.1554 -0.0351 1072 PHE   E CZ  
16933 N  N   . TRP   E 769 ? 1.1436 1.1823 1.2039 -0.1308 -0.1578 -0.0300 1073 TRP   E N   
16934 C  CA  . TRP   E 769 ? 1.1135 1.1511 1.1592 -0.1254 -0.1538 -0.0296 1073 TRP   E CA  
16935 C  C   . TRP   E 769 ? 1.0375 1.0856 1.0892 -0.1237 -0.1457 -0.0260 1073 TRP   E C   
16936 O  O   . TRP   E 769 ? 1.0366 1.0831 1.0806 -0.1208 -0.1393 -0.0249 1073 TRP   E O   
16937 C  CB  . TRP   E 769 ? 1.0739 1.1095 1.1117 -0.1231 -0.1603 -0.0316 1073 TRP   E CB  
16938 C  CG  . TRP   E 769 ? 0.9992 1.0390 1.0295 -0.1185 -0.1565 -0.0303 1073 TRP   E CG  
16939 C  CD1 . TRP   E 769 ? 1.0316 1.0794 1.0674 -0.1178 -0.1579 -0.0294 1073 TRP   E CD1 
16940 C  CD2 . TRP   E 769 ? 1.0169 1.0527 1.0332 -0.1140 -0.1510 -0.0300 1073 TRP   E CD2 
16941 N  NE1 . TRP   E 769 ? 1.0307 1.0798 1.0569 -0.1133 -0.1534 -0.0283 1073 TRP   E NE1 
16942 C  CE2 . TRP   E 769 ? 1.0395 1.0815 1.0541 -0.1110 -0.1491 -0.0287 1073 TRP   E CE2 
16943 C  CE3 . TRP   E 769 ? 1.0411 1.0688 1.0467 -0.1123 -0.1473 -0.0306 1073 TRP   E CE3 
16944 C  CZ2 . TRP   E 769 ? 1.0318 1.0725 1.0354 -0.1065 -0.1436 -0.0280 1073 TRP   E CZ2 
16945 C  CZ3 . TRP   E 769 ? 0.9906 1.0173 0.9851 -0.1075 -0.1420 -0.0299 1073 TRP   E CZ3 
16946 C  CH2 . TRP   E 769 ? 1.0149 1.0482 1.0090 -0.1049 -0.1401 -0.0287 1073 TRP   E CH2 
16947 N  N   . ARG   E 770 ? 1.0212 1.0797 1.0866 -0.1253 -0.1460 -0.0243 1074 ARG   E N   
16948 C  CA  . ARG   E 770 ? 1.0344 1.1025 1.1053 -0.1235 -0.1389 -0.0211 1074 ARG   E CA  
16949 C  C   . ARG   E 770 ? 1.0874 1.1574 1.1663 -0.1254 -0.1324 -0.0187 1074 ARG   E C   
16950 O  O   . ARG   E 770 ? 1.0306 1.1079 1.1140 -0.1237 -0.1264 -0.0160 1074 ARG   E O   
16951 C  CB  . ARG   E 770 ? 1.0124 1.0905 1.0943 -0.1243 -0.1415 -0.0201 1074 ARG   E CB  
16952 C  CG  . ARG   E 770 ? 0.9908 1.0680 1.0638 -0.1214 -0.1463 -0.0218 1074 ARG   E CG  
16953 C  CD  . ARG   E 770 ? 0.9695 1.0444 1.0285 -0.1166 -0.1414 -0.0213 1074 ARG   E CD  
16954 N  NE  . ARG   E 770 ? 1.0434 1.1195 1.0961 -0.1137 -0.1442 -0.0219 1074 ARG   E NE  
16955 C  CZ  . ARG   E 770 ? 1.0641 1.1378 1.1048 -0.1096 -0.1410 -0.0219 1074 ARG   E CZ  
16956 N  NH1 . ARG   E 770 ? 1.0494 1.1197 1.0830 -0.1077 -0.1354 -0.0215 1074 ARG   E NH1 
16957 N  NH2 . ARG   E 770 ? 1.0632 1.1377 1.0989 -0.1073 -0.1434 -0.0222 1074 ARG   E NH2 
16958 N  N   . SER   E 771 ? 1.1056 1.1686 1.1858 -0.1284 -0.1334 -0.0196 1075 SER   E N   
16959 C  CA  . SER   E 771 ? 1.1011 1.1640 1.1868 -0.1297 -0.1267 -0.0173 1075 SER   E CA  
16960 C  C   . SER   E 771 ? 1.0892 1.1488 1.1623 -0.1252 -0.1205 -0.0165 1075 SER   E C   
16961 O  O   . SER   E 771 ? 1.0672 1.1199 1.1264 -0.1225 -0.1220 -0.0186 1075 SER   E O   
16962 C  CB  . SER   E 771 ? 1.1466 1.2017 1.2359 -0.1341 -0.1294 -0.0186 1075 SER   E CB  
16963 O  OG  . SER   E 771 ? 1.2085 1.2680 1.3131 -0.1387 -0.1344 -0.0189 1075 SER   E OG  
16964 N  N   . PHE   E 772 ? 1.1173 1.1815 1.1951 -0.1242 -0.1134 -0.0136 1076 PHE   E N   
16965 C  CA  . PHE   E 772 ? 1.1540 1.2155 1.2214 -0.1198 -0.1076 -0.0128 1076 PHE   E CA  
16966 C  C   . PHE   E 772 ? 1.1915 1.2416 1.2492 -0.1198 -0.1074 -0.0144 1076 PHE   E C   
16967 O  O   . PHE   E 772 ? 1.2050 1.2509 1.2678 -0.1232 -0.1066 -0.0138 1076 PHE   E O   
16968 C  CB  . PHE   E 772 ? 1.1821 1.2493 1.2570 -0.1190 -0.1007 -0.0094 1076 PHE   E CB  
16969 C  CG  . PHE   E 772 ? 1.1395 1.2044 1.2046 -0.1142 -0.0951 -0.0087 1076 PHE   E CG  
16970 C  CD1 . PHE   E 772 ? 1.1566 1.2126 1.2145 -0.1135 -0.0924 -0.0089 1076 PHE   E CD1 
16971 C  CD2 . PHE   E 772 ? 1.1429 1.2143 1.2063 -0.1103 -0.0929 -0.0079 1076 PHE   E CD2 
16972 C  CE1 . PHE   E 772 ? 1.1337 1.1876 1.1828 -0.1088 -0.0877 -0.0085 1076 PHE   E CE1 
16973 C  CE2 . PHE   E 772 ? 1.1820 1.2516 1.2374 -0.1058 -0.0883 -0.0074 1076 PHE   E CE2 
16974 C  CZ  . PHE   E 772 ? 1.1441 1.2049 1.1923 -0.1050 -0.0859 -0.0078 1076 PHE   E CZ  
16975 N  N   . HIS   E 773 ? 1.1840 1.2289 1.2278 -0.1160 -0.1076 -0.0161 1077 HIS   E N   
16976 C  CA  . HIS   E 773 ? 1.2615 1.2951 1.2944 -0.1155 -0.1083 -0.0181 1077 HIS   E CA  
16977 C  C   . HIS   E 773 ? 1.3032 1.3342 1.3262 -0.1106 -0.1027 -0.0176 1077 HIS   E C   
16978 O  O   . HIS   E 773 ? 1.2451 1.2801 1.2631 -0.1067 -0.1015 -0.0178 1077 HIS   E O   
16979 C  CB  . HIS   E 773 ? 1.3298 1.3580 1.3544 -0.1155 -0.1149 -0.0212 1077 HIS   E CB  
16980 C  CG  . HIS   E 773 ? 1.3695 1.3857 1.3807 -0.1139 -0.1154 -0.0233 1077 HIS   E CG  
16981 N  ND1 . HIS   E 773 ? 1.3956 1.4037 1.4071 -0.1167 -0.1157 -0.0238 1077 HIS   E ND1 
16982 C  CD2 . HIS   E 773 ? 1.3415 1.3525 1.3390 -0.1098 -0.1155 -0.0251 1077 HIS   E CD2 
16983 C  CE1 . HIS   E 773 ? 1.4861 1.4843 1.4839 -0.1142 -0.1162 -0.0258 1077 HIS   E CE1 
16984 N  NE2 . HIS   E 773 ? 1.4321 1.4320 1.4213 -0.1099 -0.1160 -0.0266 1077 HIS   E NE2 
16985 N  N   . THR   E 774 ? 1.4474 1.4718 1.4681 -0.1108 -0.0993 -0.0170 1078 THR   E N   
16986 C  CA  . THR   E 774 ? 1.4481 1.4668 1.4577 -0.1064 -0.0952 -0.0173 1078 THR   E CA  
16987 C  C   . THR   E 774 ? 1.5487 1.5552 1.5493 -0.1073 -0.0975 -0.0194 1078 THR   E C   
16988 O  O   . THR   E 774 ? 1.5037 1.5061 1.5079 -0.1118 -0.1018 -0.0204 1078 THR   E O   
16989 C  CB  . THR   E 774 ? 1.3922 1.4126 1.4054 -0.1050 -0.0889 -0.0145 1078 THR   E CB  
16990 O  OG1 . THR   E 774 ? 1.4738 1.4948 1.4980 -0.1097 -0.0882 -0.0126 1078 THR   E OG1 
16991 C  CG2 . THR   E 774 ? 1.2464 1.2765 1.2625 -0.1016 -0.0863 -0.0131 1078 THR   E CG2 
16992 N  N   . GLU   E 775 ? 1.6589 1.6596 1.6479 -0.1029 -0.0949 -0.0203 1079 GLU   E N   
16993 C  CA  . GLU   E 775 ? 1.7363 1.7249 1.7150 -0.1029 -0.0970 -0.0225 1079 GLU   E CA  
16994 C  C   . GLU   E 775 ? 1.7273 1.7093 1.7107 -0.1077 -0.0974 -0.0220 1079 GLU   E C   
16995 O  O   . GLU   E 775 ? 1.7264 1.6996 1.7052 -0.1099 -0.1015 -0.0241 1079 GLU   E O   
16996 C  CB  . GLU   E 775 ? 1.7574 1.7414 1.7246 -0.0972 -0.0931 -0.0231 1079 GLU   E CB  
16997 C  CG  . GLU   E 775 ? 1.7741 1.7622 1.7352 -0.0927 -0.0932 -0.0243 1079 GLU   E CG  
16998 C  CD  . GLU   E 775 ? 1.8122 1.7904 1.7598 -0.0899 -0.0946 -0.0269 1079 GLU   E CD  
16999 O  OE1 . GLU   E 775 ? 1.8457 1.8249 1.7886 -0.0881 -0.0967 -0.0284 1079 GLU   E OE1 
17000 O  OE2 . GLU   E 775 ? 1.8111 1.7802 1.7524 -0.0893 -0.0934 -0.0274 1079 GLU   E OE2 
17001 N  N   . ARG   E 776 ? 1.6572 1.6429 1.6498 -0.1093 -0.0932 -0.0191 1080 ARG   E N   
17002 C  CA  . ARG   E 776 ? 1.6656 1.6452 1.6638 -0.1139 -0.0925 -0.0182 1080 ARG   E CA  
17003 C  C   . ARG   E 776 ? 1.6241 1.6123 1.6377 -0.1172 -0.0901 -0.0152 1080 ARG   E C   
17004 O  O   . ARG   E 776 ? 1.7148 1.7003 1.7325 -0.1185 -0.0852 -0.0128 1080 ARG   E O   
17005 C  CB  . ARG   E 776 ? 1.7370 1.7068 1.7260 -0.1112 -0.0878 -0.0176 1080 ARG   E CB  
17006 N  N   . LYS   E 777 ? 1.5961 1.5944 1.6183 -0.1186 -0.0930 -0.0151 1081 LYS   E N   
17007 C  CA  . LYS   E 777 ? 1.5592 1.5657 1.5971 -0.1222 -0.0917 -0.0126 1081 LYS   E CA  
17008 C  C   . LYS   E 777 ? 1.4994 1.5147 1.5440 -0.1237 -0.0973 -0.0137 1081 LYS   E C   
17009 O  O   . LYS   E 777 ? 1.4870 1.5050 1.5242 -0.1202 -0.0992 -0.0151 1081 LYS   E O   
17010 C  CB  . LYS   E 777 ? 1.5537 1.5653 1.5936 -0.1190 -0.0843 -0.0093 1081 LYS   E CB  
17011 N  N   . THR   E 778 ? 1.3855 1.4046 1.4441 -0.1290 -0.1000 -0.0132 1082 THR   E N   
17012 C  CA  . THR   E 778 ? 1.3081 1.3356 1.3745 -0.1306 -0.1055 -0.0141 1082 THR   E CA  
17013 C  C   . THR   E 778 ? 1.3423 1.3788 1.4262 -0.1339 -0.1031 -0.0112 1082 THR   E C   
17014 O  O   . THR   E 778 ? 1.2741 1.3081 1.3657 -0.1369 -0.0994 -0.0094 1082 THR   E O   
17015 C  CB  . THR   E 778 ? 1.2849 1.3070 1.3499 -0.1336 -0.1140 -0.0176 1082 THR   E CB  
17016 O  OG1 . THR   E 778 ? 1.5169 1.5302 1.5843 -0.1376 -0.1146 -0.0181 1082 THR   E OG1 
17017 C  CG2 . THR   E 778 ? 1.3568 1.3733 1.4048 -0.1293 -0.1170 -0.0203 1082 THR   E CG2 
17018 N  N   . GLU   E 779 ? 1.4124 1.4590 1.5020 -0.1329 -0.1046 -0.0107 1083 GLU   E N   
17019 C  CA  . GLU   E 779 ? 1.3919 1.4483 1.4964 -0.1345 -0.1014 -0.0077 1083 GLU   E CA  
17020 C  C   . GLU   E 779 ? 1.3586 1.4237 1.4695 -0.1351 -0.1071 -0.0088 1083 GLU   E C   
17021 O  O   . GLU   E 779 ? 1.3394 1.4042 1.4403 -0.1322 -0.1110 -0.0109 1083 GLU   E O   
17022 C  CB  . GLU   E 779 ? 1.4003 1.4601 1.5015 -0.1301 -0.0933 -0.0047 1083 GLU   E CB  
17023 C  CG  . GLU   E 779 ? 1.4726 1.5417 1.5882 -0.1312 -0.0892 -0.0014 1083 GLU   E CG  
17024 C  CD  . GLU   E 779 ? 1.5592 1.6279 1.6715 -0.1275 -0.0804 0.0018  1083 GLU   E CD  
17025 O  OE1 . GLU   E 779 ? 1.5765 1.6362 1.6796 -0.1260 -0.0769 0.0019  1083 GLU   E OE1 
17026 O  OE2 . GLU   E 779 ? 1.5496 1.6264 1.6681 -0.1259 -0.0772 0.0041  1083 GLU   E OE2 
17027 N  N   . PRO   E 780 ? 1.2540 1.3268 1.3813 -0.1384 -0.1076 -0.0072 1084 PRO   E N   
17028 C  CA  . PRO   E 780 ? 1.2194 1.2999 1.3535 -0.1392 -0.1140 -0.0085 1084 PRO   E CA  
17029 C  C   . PRO   E 780 ? 1.2170 1.3061 1.3499 -0.1351 -0.1108 -0.0067 1084 PRO   E C   
17030 O  O   . PRO   E 780 ? 1.2093 1.3022 1.3453 -0.1334 -0.1036 -0.0036 1084 PRO   E O   
17031 C  CB  . PRO   E 780 ? 1.1891 1.2739 1.3425 -0.1447 -0.1151 -0.0075 1084 PRO   E CB  
17032 C  CG  . PRO   E 780 ? 1.2397 1.3237 1.3976 -0.1450 -0.1059 -0.0039 1084 PRO   E CG  
17033 C  CD  . PRO   E 780 ? 1.2411 1.3150 1.3819 -0.1420 -0.1025 -0.0045 1084 PRO   E CD  
17034 N  N   . ALA   E 781 ? 1.1550 1.2464 1.2825 -0.1333 -0.1163 -0.0087 1085 ALA   E N   
17035 C  CA  . ALA   E 781 ? 1.1032 1.2019 1.2281 -0.1293 -0.1139 -0.0074 1085 ALA   E CA  
17036 C  C   . ALA   E 781 ? 1.1188 1.2276 1.2591 -0.1304 -0.1112 -0.0046 1085 ALA   E C   
17037 O  O   . ALA   E 781 ? 1.1415 1.2533 1.2957 -0.1345 -0.1135 -0.0043 1085 ALA   E O   
17038 C  CB  . ALA   E 781 ? 1.0601 1.1587 1.1774 -0.1276 -0.1205 -0.0100 1085 ALA   E CB  
17039 N  N   . THR   E 782 ? 1.0895 1.2036 1.2276 -0.1266 -0.1064 -0.0025 1086 THR   E N   
17040 C  CA  . THR   E 782 ? 1.1459 1.2684 1.2973 -0.1271 -0.1023 0.0005  1086 THR   E CA  
17041 C  C   . THR   E 782 ? 1.1292 1.2579 1.2767 -0.1227 -0.1002 0.0016  1086 THR   E C   
17042 O  O   . THR   E 782 ? 1.1352 1.2608 1.2710 -0.1189 -0.0970 0.0016  1086 THR   E O   
17043 C  CB  . THR   E 782 ? 1.1163 1.2359 1.2711 -0.1278 -0.0948 0.0032  1086 THR   E CB  
17044 O  OG1 . THR   E 782 ? 1.1824 1.3100 1.3503 -0.1282 -0.0906 0.0063  1086 THR   E OG1 
17045 C  CG2 . THR   E 782 ? 1.0718 1.1863 1.2121 -0.1232 -0.0898 0.0036  1086 THR   E CG2 
17046 N  N   . GLY   E 783 ? 1.1480 1.2851 1.3056 -0.1232 -0.1020 0.0025  1087 GLY   E N   
17047 C  CA  . GLY   E 783 ? 1.1279 1.2707 1.2825 -0.1192 -0.1000 0.0037  1087 GLY   E CA  
17048 C  C   . GLY   E 783 ? 1.0922 1.2330 1.2345 -0.1166 -0.1040 0.0013  1087 GLY   E C   
17049 O  O   . GLY   E 783 ? 1.1143 1.2572 1.2506 -0.1128 -0.1013 0.0020  1087 GLY   E O   
17050 N  N   . PHE   E 784 ? 1.0771 1.2131 1.2150 -0.1184 -0.1103 -0.0015 1088 PHE   E N   
17051 C  CA  . PHE   E 784 ? 1.0786 1.2127 1.2059 -0.1162 -0.1146 -0.0037 1088 PHE   E CA  
17052 C  C   . PHE   E 784 ? 1.1252 1.2600 1.2572 -0.1187 -0.1225 -0.0056 1088 PHE   E C   
17053 O  O   . PHE   E 784 ? 1.2157 1.3493 1.3559 -0.1224 -0.1255 -0.0063 1088 PHE   E O   
17054 C  CB  . PHE   E 784 ? 1.0739 1.1991 1.1868 -0.1146 -0.1141 -0.0055 1088 PHE   E CB  
17055 C  CG  . PHE   E 784 ? 1.0459 1.1709 1.1517 -0.1108 -0.1078 -0.0043 1088 PHE   E CG  
17056 C  CD1 . PHE   E 784 ? 0.9751 1.0987 1.0824 -0.1105 -0.1022 -0.0026 1088 PHE   E CD1 
17057 C  CD2 . PHE   E 784 ? 1.0350 1.1608 1.1324 -0.1073 -0.1077 -0.0049 1088 PHE   E CD2 
17058 C  CE1 . PHE   E 784 ? 0.9921 1.1151 1.0925 -0.1067 -0.0972 -0.0019 1088 PHE   E CE1 
17059 C  CE2 . PHE   E 784 ? 1.0135 1.1394 1.1054 -0.1038 -0.1026 -0.0041 1088 PHE   E CE2 
17060 C  CZ  . PHE   E 784 ? 0.9685 1.0930 1.0618 -0.1034 -0.0977 -0.0027 1088 PHE   E CZ  
17061 N  N   . ILE   E 785 ? 1.0915 1.2276 1.2179 -0.1165 -0.1261 -0.0066 1089 ILE   E N   
17062 C  CA  . ILE   E 785 ? 1.0827 1.2179 1.2106 -0.1179 -0.1343 -0.0088 1089 ILE   E CA  
17063 C  C   . ILE   E 785 ? 1.0993 1.2270 1.2110 -0.1153 -0.1375 -0.0111 1089 ILE   E C   
17064 O  O   . ILE   E 785 ? 1.1284 1.2568 1.2321 -0.1119 -0.1345 -0.0105 1089 ILE   E O   
17065 C  CB  . ILE   E 785 ? 1.0983 1.2427 1.2367 -0.1177 -0.1362 -0.0076 1089 ILE   E CB  
17066 C  CG1 . ILE   E 785 ? 1.1421 1.2926 1.2977 -0.1210 -0.1346 -0.0059 1089 ILE   E CG1 
17067 C  CG2 . ILE   E 785 ? 1.0541 1.1965 1.1894 -0.1175 -0.1448 -0.0101 1089 ILE   E CG2 
17068 C  CD1 . ILE   E 785 ? 1.2263 1.3848 1.3937 -0.1216 -0.1384 -0.0054 1089 ILE   E CD1 
17069 N  N   . ASP   E 786 ? 1.0878 1.2081 1.1950 -0.1169 -0.1435 -0.0139 1090 ASP   E N   
17070 C  CA  . ASP   E 786 ? 1.0871 1.1985 1.1780 -0.1145 -0.1466 -0.0162 1090 ASP   E CA  
17071 C  C   . ASP   E 786 ? 1.1231 1.2362 1.2113 -0.1125 -0.1513 -0.0168 1090 ASP   E C   
17072 O  O   . ASP   E 786 ? 1.1209 1.2305 1.2083 -0.1133 -0.1590 -0.0190 1090 ASP   E O   
17073 C  CB  . ASP   E 786 ? 1.0914 1.1937 1.1786 -0.1169 -0.1516 -0.0189 1090 ASP   E CB  
17074 C  CG  . ASP   E 786 ? 1.0677 1.1596 1.1372 -0.1140 -0.1544 -0.0213 1090 ASP   E CG  
17075 O  OD1 . ASP   E 786 ? 1.0697 1.1612 1.1296 -0.1104 -0.1507 -0.0205 1090 ASP   E OD1 
17076 O  OD2 . ASP   E 786 ? 1.0835 1.1673 1.1487 -0.1155 -0.1603 -0.0239 1090 ASP   E OD2 
17077 N  N   . GLY   E 787 ? 1.0613 1.1794 1.1477 -0.1096 -0.1468 -0.0149 1091 GLY   E N   
17078 C  CA  . GLY   E 787 ? 1.0673 1.1868 1.1499 -0.1072 -0.1500 -0.0150 1091 GLY   E CA  
17079 C  C   . GLY   E 787 ? 1.0935 1.2034 1.1634 -0.1059 -0.1565 -0.0178 1091 GLY   E C   
17080 O  O   . GLY   E 787 ? 1.1103 1.2206 1.1822 -0.1059 -0.1631 -0.0189 1091 GLY   E O   
17081 N  N   . ASP   E 788 ? 1.1266 1.2274 1.1831 -0.1044 -0.1549 -0.0190 1092 ASP   E N   
17082 C  CA  . ASP   E 788 ? 1.1468 1.2369 1.1902 -0.1030 -0.1610 -0.0218 1092 ASP   E CA  
17083 C  C   . ASP   E 788 ? 1.1708 1.2598 1.2216 -0.1060 -0.1698 -0.0239 1092 ASP   E C   
17084 O  O   . ASP   E 788 ? 1.2288 1.3141 1.2748 -0.1046 -0.1767 -0.0256 1092 ASP   E O   
17085 C  CB  . ASP   E 788 ? 1.1282 1.2090 1.1594 -0.1021 -0.1580 -0.0229 1092 ASP   E CB  
17086 C  CG  . ASP   E 788 ? 1.1630 1.2445 1.1869 -0.0989 -0.1500 -0.0211 1092 ASP   E CG  
17087 O  OD1 . ASP   E 788 ? 1.2002 1.2860 1.2237 -0.0968 -0.1478 -0.0196 1092 ASP   E OD1 
17088 O  OD2 . ASP   E 788 ? 1.1818 1.2592 1.2006 -0.0985 -0.1458 -0.0213 1092 ASP   E OD2 
17089 N  N   . LEU   E 789 ? 1.1014 1.1934 1.1642 -0.1099 -0.1699 -0.0239 1093 LEU   E N   
17090 C  CA  . LEU   E 789 ? 1.1109 1.2025 1.1828 -0.1131 -0.1783 -0.0261 1093 LEU   E CA  
17091 C  C   . LEU   E 789 ? 1.1537 1.2535 1.2359 -0.1131 -0.1824 -0.0255 1093 LEU   E C   
17092 O  O   . LEU   E 789 ? 1.2031 1.2987 1.2810 -0.1119 -0.1905 -0.0278 1093 LEU   E O   
17093 C  CB  . LEU   E 789 ? 1.1531 1.2479 1.2383 -0.1176 -0.1763 -0.0256 1093 LEU   E CB  
17094 C  CG  . LEU   E 789 ? 1.1844 1.2791 1.2805 -0.1210 -0.1855 -0.0279 1093 LEU   E CG  
17095 C  CD1 . LEU   E 789 ? 1.2101 1.2918 1.2918 -0.1199 -0.1936 -0.0318 1093 LEU   E CD1 
17096 C  CD2 . LEU   E 789 ? 1.1601 1.2592 1.2726 -0.1260 -0.1833 -0.0270 1093 LEU   E CD2 
17097 N  N   . ILE   E 790 ? 1.1201 1.2311 1.2155 -0.1140 -0.1770 -0.0226 1094 ILE   E N   
17098 C  CA  . ILE   E 790 ? 1.1022 1.2219 1.2074 -0.1135 -0.1794 -0.0216 1094 ILE   E CA  
17099 C  C   . ILE   E 790 ? 1.1824 1.2971 1.2746 -0.1095 -0.1841 -0.0228 1094 ILE   E C   
17100 O  O   . ILE   E 790 ? 1.2632 1.3790 1.3598 -0.1095 -0.1918 -0.0243 1094 ILE   E O   
17101 C  CB  . ILE   E 790 ? 1.1177 1.2473 1.2310 -0.1131 -0.1706 -0.0179 1094 ILE   E CB  
17102 C  CG1 . ILE   E 790 ? 1.1282 1.2638 1.2578 -0.1172 -0.1676 -0.0166 1094 ILE   E CG1 
17103 C  CG2 . ILE   E 790 ? 1.1943 1.3310 1.3121 -0.1111 -0.1721 -0.0168 1094 ILE   E CG2 
17104 C  CD1 . ILE   E 790 ? 1.1925 1.3368 1.3397 -0.1193 -0.1717 -0.0163 1094 ILE   E CD1 
17105 N  N   . GLU   E 791 ? 1.1706 1.2795 1.2466 -0.1060 -0.1796 -0.0223 1095 GLU   E N   
17106 C  CA  . GLU   E 791 ? 1.1816 1.2856 1.2447 -0.1019 -0.1823 -0.0229 1095 GLU   E CA  
17107 C  C   . GLU   E 791 ? 1.2346 1.3281 1.2880 -0.1010 -0.1919 -0.0264 1095 GLU   E C   
17108 O  O   . GLU   E 791 ? 1.2568 1.3481 1.3051 -0.0984 -0.1972 -0.0272 1095 GLU   E O   
17109 C  CB  . GLU   E 791 ? 1.1560 1.2557 1.2048 -0.0986 -0.1747 -0.0215 1095 GLU   E CB  
17110 C  CG  . GLU   E 791 ? 1.1824 1.2918 1.2386 -0.0983 -0.1661 -0.0181 1095 GLU   E CG  
17111 C  CD  . GLU   E 791 ? 1.2211 1.3271 1.2643 -0.0946 -0.1601 -0.0169 1095 GLU   E CD  
17112 O  OE1 . GLU   E 791 ? 1.1852 1.2811 1.2130 -0.0920 -0.1613 -0.0182 1095 GLU   E OE1 
17113 O  OE2 . GLU   E 791 ? 1.2354 1.3490 1.2845 -0.0941 -0.1539 -0.0145 1095 GLU   E OE2 
17114 N  N   . SER   E 792 ? 1.2755 1.3617 1.3254 -0.1028 -0.1944 -0.0285 1096 SER   E N   
17115 C  CA  . SER   E 792 ? 1.2852 1.3608 1.3262 -0.1020 -0.2042 -0.0322 1096 SER   E CA  
17116 C  C   . SER   E 792 ? 1.3612 1.4420 1.4162 -0.1040 -0.2134 -0.0338 1096 SER   E C   
17117 O  O   . SER   E 792 ? 1.4118 1.4845 1.4591 -0.1023 -0.2226 -0.0369 1096 SER   E O   
17118 C  CB  . SER   E 792 ? 1.2725 1.3401 1.3090 -0.1040 -0.2047 -0.0341 1096 SER   E CB  
17119 O  OG  . SER   E 792 ? 1.3034 1.3796 1.3581 -0.1088 -0.2024 -0.0331 1096 SER   E OG  
17120 N  N   . PHE   E 793 ? 1.4083 1.5021 1.4838 -0.1073 -0.2113 -0.0319 1097 PHE   E N   
17121 C  CA  . PHE   E 793 ? 1.4264 1.5264 1.5160 -0.1087 -0.2194 -0.0332 1097 PHE   E CA  
17122 C  C   . PHE   E 793 ? 1.4644 1.5614 1.5438 -0.1040 -0.2242 -0.0338 1097 PHE   E C   
17123 O  O   . PHE   E 793 ? 1.5359 1.6298 1.6164 -0.1035 -0.2345 -0.0367 1097 PHE   E O   
17124 C  CB  . PHE   E 793 ? 1.4364 1.5513 1.5477 -0.1117 -0.2142 -0.0302 1097 PHE   E CB  
17125 C  CG  . PHE   E 793 ? 1.5349 1.6580 1.6588 -0.1114 -0.2201 -0.0303 1097 PHE   E CG  
17126 C  CD1 . PHE   E 793 ? 1.5187 1.6433 1.6555 -0.1141 -0.2296 -0.0331 1097 PHE   E CD1 
17127 C  CD2 . PHE   E 793 ? 1.5029 1.6321 1.6262 -0.1084 -0.2162 -0.0278 1097 PHE   E CD2 
17128 C  CE1 . PHE   E 793 ? 1.5214 1.6539 1.6706 -0.1135 -0.2352 -0.0333 1097 PHE   E CE1 
17129 C  CE2 . PHE   E 793 ? 1.5200 1.6567 1.6548 -0.1078 -0.2216 -0.0279 1097 PHE   E CE2 
17130 C  CZ  . PHE   E 793 ? 1.5300 1.6685 1.6779 -0.1103 -0.2311 -0.0307 1097 PHE   E CZ  
17131 N  N   . LEU   E 794 ? 1.4661 1.5637 1.5359 -0.1006 -0.2171 -0.0312 1098 LEU   E N   
17132 C  CA  . LEU   E 794 ? 1.4345 1.5286 1.4936 -0.0960 -0.2205 -0.0314 1098 LEU   E CA  
17133 C  C   . LEU   E 794 ? 1.4540 1.5329 1.4944 -0.0929 -0.2287 -0.0349 1098 LEU   E C   
17134 O  O   . LEU   E 794 ? 1.4973 1.5728 1.5330 -0.0900 -0.2363 -0.0365 1098 LEU   E O   
17135 C  CB  . LEU   E 794 ? 1.4012 1.4970 1.4520 -0.0933 -0.2106 -0.0280 1098 LEU   E CB  
17136 C  CG  . LEU   E 794 ? 1.4381 1.5387 1.4890 -0.0902 -0.2101 -0.0262 1098 LEU   E CG  
17137 C  CD1 . LEU   E 794 ? 1.4022 1.5057 1.4485 -0.0887 -0.1991 -0.0228 1098 LEU   E CD1 
17138 C  CD2 . LEU   E 794 ? 1.5077 1.5973 1.5426 -0.0858 -0.2178 -0.0284 1098 LEU   E CD2 
17139 N  N   . ASP   E 795 ? 1.4702 1.5394 1.4997 -0.0933 -0.2278 -0.0364 1099 ASP   E N   
17140 C  CA  . ASP   E 795 ? 1.5534 1.6069 1.5636 -0.0900 -0.2350 -0.0397 1099 ASP   E CA  
17141 C  C   . ASP   E 795 ? 1.5931 1.6432 1.6102 -0.0929 -0.2455 -0.0436 1099 ASP   E C   
17142 O  O   . ASP   E 795 ? 1.6374 1.6759 1.6425 -0.0925 -0.2478 -0.0459 1099 ASP   E O   
17143 C  CB  . ASP   E 795 ? 1.6193 1.6637 1.6122 -0.0880 -0.2269 -0.0387 1099 ASP   E CB  
17144 C  CG  . ASP   E 795 ? 1.7697 1.7963 1.7397 -0.0841 -0.2321 -0.0417 1099 ASP   E CG  
17145 O  OD1 . ASP   E 795 ? 1.8215 1.8405 1.7850 -0.0818 -0.2428 -0.0448 1099 ASP   E OD1 
17146 O  OD2 . ASP   E 795 ? 1.8138 1.8340 1.7722 -0.0830 -0.2253 -0.0410 1099 ASP   E OD2 
17147 N  N   . ILE   E 796 ? 1.5789 1.6382 1.6152 -0.0958 -0.2520 -0.0445 1100 ILE   E N   
17148 C  CA  . ILE   E 796 ? 1.5984 1.6526 1.6395 -0.0979 -0.2635 -0.0488 1100 ILE   E CA  
17149 C  C   . ILE   E 796 ? 1.7178 1.7723 1.7616 -0.0955 -0.2745 -0.0511 1100 ILE   E C   
17150 O  O   . ILE   E 796 ? 1.7703 1.8284 1.8112 -0.0922 -0.2726 -0.0492 1100 ILE   E O   
17151 C  CB  . ILE   E 796 ? 1.5687 1.6328 1.6327 -0.1045 -0.2622 -0.0486 1100 ILE   E CB  
17152 C  CG1 . ILE   E 796 ? 1.6154 1.6964 1.7024 -0.1070 -0.2599 -0.0460 1100 ILE   E CG1 
17153 C  CG2 . ILE   E 796 ? 1.4918 1.5541 1.5511 -0.1063 -0.2519 -0.0466 1100 ILE   E CG2 
17154 C  CD1 . ILE   E 796 ? 1.5996 1.6899 1.7097 -0.1133 -0.2586 -0.0457 1100 ILE   E CD1 
17155 N  N   . SER   E 797 ? 1.7966 1.8464 1.8450 -0.0969 -0.2863 -0.0554 1101 SER   E N   
17156 C  CA  . SER   E 797 ? 1.8039 1.8530 1.8547 -0.0944 -0.2982 -0.0582 1101 SER   E CA  
17157 C  C   . SER   E 797 ? 1.7826 1.8494 1.8610 -0.0980 -0.2986 -0.0567 1101 SER   E C   
17158 O  O   . SER   E 797 ? 1.7770 1.8540 1.8758 -0.1037 -0.2950 -0.0557 1101 SER   E O   
17159 C  CB  . SER   E 797 ? 1.8126 1.8501 1.8590 -0.0946 -0.3114 -0.0637 1101 SER   E CB  
17160 O  OG  . SER   E 797 ? 1.8073 1.8536 1.8783 -0.1010 -0.3153 -0.0651 1101 SER   E OG  
17161 N  N   . ARG   E 798 ? 1.7546 1.8244 1.8331 -0.0943 -0.3029 -0.0567 1102 ARG   E N   
17162 C  CA  . ARG   E 798 ? 1.7173 1.8041 1.8209 -0.0969 -0.3024 -0.0549 1102 ARG   E CA  
17163 C  C   . ARG   E 798 ? 1.7308 1.8253 1.8594 -0.1025 -0.3098 -0.0574 1102 ARG   E C   
17164 O  O   . ARG   E 798 ? 1.7149 1.8246 1.8666 -0.1064 -0.3046 -0.0548 1102 ARG   E O   
17165 C  CB  . ARG   E 798 ? 1.6615 1.7484 1.7598 -0.0916 -0.3079 -0.0552 1102 ARG   E CB  
17166 C  CG  . ARG   E 798 ? 1.6919 1.7811 1.7795 -0.0881 -0.2970 -0.0507 1102 ARG   E CG  
17167 C  CD  . ARG   E 798 ? 1.7354 1.8341 1.8329 -0.0857 -0.2995 -0.0496 1102 ARG   E CD  
17168 N  NE  . ARG   E 798 ? 1.7314 1.8477 1.8572 -0.0905 -0.2960 -0.0475 1102 ARG   E NE  
17169 C  CZ  . ARG   E 798 ? 1.6927 1.8202 1.8274 -0.0898 -0.2893 -0.0439 1102 ARG   E CZ  
17170 N  NH1 . ARG   E 798 ? 1.6113 1.7348 1.7299 -0.0849 -0.2853 -0.0418 1102 ARG   E NH1 
17171 N  NH2 . ARG   E 798 ? 1.6635 1.8061 1.8237 -0.0941 -0.2863 -0.0422 1102 ARG   E NH2 
17172 N  N   . PRO   E 799 ? 1.7266 1.8116 1.8527 -0.1031 -0.3213 -0.0623 1103 PRO   E N   
17173 C  CA  . PRO   E 799 ? 1.7182 1.8108 1.8694 -0.1095 -0.3260 -0.0642 1103 PRO   E CA  
17174 C  C   . PRO   E 799 ? 1.7004 1.7988 1.8609 -0.1149 -0.3140 -0.0609 1103 PRO   E C   
17175 O  O   . PRO   E 799 ? 1.6617 1.7738 1.8476 -0.1199 -0.3106 -0.0592 1103 PRO   E O   
17176 C  CB  . PRO   E 799 ? 1.7208 1.7984 1.8608 -0.1084 -0.3395 -0.0700 1103 PRO   E CB  
17177 C  CG  . PRO   E 799 ? 1.7421 1.8035 1.8492 -0.1025 -0.3370 -0.0699 1103 PRO   E CG  
17178 C  CD  . PRO   E 799 ? 1.7011 1.7677 1.8017 -0.0982 -0.3301 -0.0662 1103 PRO   E CD  
17179 N  N   . LYS   E 800 ? 1.6964 1.7846 1.8366 -0.1136 -0.3071 -0.0599 1104 LYS   E N   
17180 C  CA  . LYS   E 800 ? 1.6724 1.7645 1.8188 -0.1181 -0.2960 -0.0569 1104 LYS   E CA  
17181 C  C   . LYS   E 800 ? 1.6313 1.7389 1.7926 -0.1196 -0.2845 -0.0518 1104 LYS   E C   
17182 O  O   . LYS   E 800 ? 1.6289 1.7460 1.8098 -0.1247 -0.2792 -0.0500 1104 LYS   E O   
17183 C  CB  . LYS   E 800 ? 1.6993 1.7777 1.8194 -0.1152 -0.2905 -0.0566 1104 LYS   E CB  
17184 N  N   . MET   E 801 ? 1.6675 1.7772 1.8192 -0.1150 -0.2803 -0.0494 1105 MET   E N   
17185 C  CA  . MET   E 801 ? 1.6464 1.7702 1.8115 -0.1159 -0.2702 -0.0448 1105 MET   E CA  
17186 C  C   . MET   E 801 ? 1.6694 1.8068 1.8628 -0.1196 -0.2738 -0.0448 1105 MET   E C   
17187 O  O   . MET   E 801 ? 1.6229 1.7720 1.8327 -0.1225 -0.2651 -0.0412 1105 MET   E O   
17188 C  CB  . MET   E 801 ? 1.6226 1.7459 1.7738 -0.1102 -0.2675 -0.0429 1105 MET   E CB  
17189 C  CG  . MET   E 801 ? 1.6285 1.7364 1.7513 -0.1054 -0.2687 -0.0443 1105 MET   E CG  
17190 S  SD  . MET   E 801 ? 1.6503 1.7596 1.7591 -0.1004 -0.2591 -0.0402 1105 MET   E SD  
17191 C  CE  . MET   E 801 ? 1.6103 1.7003 1.6875 -0.0947 -0.2633 -0.0427 1105 MET   E CE  
17192 N  N   . GLN   E 802 ? 1.6679 1.8037 1.8673 -0.1192 -0.2867 -0.0488 1106 GLN   E N   
17193 C  CA  . GLN   E 802 ? 1.6741 1.8225 1.9019 -0.1231 -0.2911 -0.0493 1106 GLN   E CA  
17194 C  C   . GLN   E 802 ? 1.6406 1.7926 1.8849 -0.1296 -0.2870 -0.0488 1106 GLN   E C   
17195 O  O   . GLN   E 802 ? 1.6488 1.8133 1.9134 -0.1330 -0.2794 -0.0455 1106 GLN   E O   
17196 C  CB  . GLN   E 802 ? 1.7031 1.8472 1.9326 -0.1213 -0.3069 -0.0544 1106 GLN   E CB  
17197 C  CG  . GLN   E 802 ? 1.6559 1.7959 1.8692 -0.1145 -0.3114 -0.0550 1106 GLN   E CG  
17198 C  CD  . GLN   E 802 ? 1.6455 1.7999 1.8731 -0.1134 -0.3065 -0.0515 1106 GLN   E CD  
17199 O  OE1 . GLN   E 802 ? 1.6389 1.7941 1.8548 -0.1101 -0.2980 -0.0480 1106 GLN   E OE1 
17200 N  NE2 . GLN   E 802 ? 1.6814 1.8474 1.9351 -0.1162 -0.3120 -0.0525 1106 GLN   E NE2 
17201 N  N   . GLU   E 803 ? 1.6306 1.7709 1.8654 -0.1313 -0.2914 -0.0519 1107 GLU   E N   
17202 C  CA  . GLU   E 803 ? 1.6598 1.8020 1.9088 -0.1375 -0.2877 -0.0515 1107 GLU   E CA  
17203 C  C   . GLU   E 803 ? 1.6550 1.8028 1.9048 -0.1388 -0.2721 -0.0462 1107 GLU   E C   
17204 O  O   . GLU   E 803 ? 1.6725 1.8304 1.9435 -0.1433 -0.2660 -0.0437 1107 GLU   E O   
17205 C  CB  . GLU   E 803 ? 1.6967 1.8235 1.9309 -0.1381 -0.2945 -0.0556 1107 GLU   E CB  
17206 C  CG  . GLU   E 803 ? 1.7368 1.8644 1.9869 -0.1447 -0.2932 -0.0561 1107 GLU   E CG  
17207 C  CD  . GLU   E 803 ? 1.8340 1.9462 2.0708 -0.1452 -0.3022 -0.0608 1107 GLU   E CD  
17208 O  OE1 . GLU   E 803 ? 1.8443 1.9452 2.0599 -0.1402 -0.3099 -0.0638 1107 GLU   E OE1 
17209 O  OE2 . GLU   E 803 ? 1.9051 2.0156 2.1518 -0.1505 -0.3014 -0.0615 1107 GLU   E OE2 
17210 N  N   . VAL   E 804 ? 1.6518 1.7931 1.8789 -0.1348 -0.2653 -0.0444 1108 VAL   E N   
17211 C  CA  . VAL   E 804 ? 1.5998 1.7456 1.8263 -0.1356 -0.2512 -0.0397 1108 VAL   E CA  
17212 C  C   . VAL   E 804 ? 1.6637 1.8242 1.9068 -0.1357 -0.2443 -0.0357 1108 VAL   E C   
17213 O  O   . VAL   E 804 ? 1.6697 1.8354 1.9173 -0.1370 -0.2331 -0.0319 1108 VAL   E O   
17214 C  CB  . VAL   E 804 ? 1.5800 1.7160 1.7792 -0.1310 -0.2460 -0.0388 1108 VAL   E CB  
17215 C  CG1 . VAL   E 804 ? 1.5236 1.6443 1.7045 -0.1296 -0.2541 -0.0430 1108 VAL   E CG1 
17216 C  CG2 . VAL   E 804 ? 1.6620 1.8015 1.8536 -0.1259 -0.2451 -0.0373 1108 VAL   E CG2 
17217 N  N   . VAL   E 805 ? 1.7386 1.9058 1.9909 -0.1339 -0.2508 -0.0366 1109 VAL   E N   
17218 C  CA  . VAL   E 805 ? 1.7547 1.9357 2.0227 -0.1337 -0.2444 -0.0328 1109 VAL   E CA  
17219 C  C   . VAL   E 805 ? 1.7279 1.9197 2.0249 -0.1382 -0.2476 -0.0332 1109 VAL   E C   
17220 O  O   . VAL   E 805 ? 1.7133 1.9170 2.0261 -0.1388 -0.2407 -0.0296 1109 VAL   E O   
17221 C  CB  . VAL   E 805 ? 1.7646 1.9466 2.0223 -0.1280 -0.2473 -0.0327 1109 VAL   E CB  
17222 C  CG1 . VAL   E 805 ? 1.7278 1.9006 1.9593 -0.1239 -0.2417 -0.0315 1109 VAL   E CG1 
17223 C  CG2 . VAL   E 805 ? 1.7473 1.9254 2.0049 -0.1264 -0.2618 -0.0373 1109 VAL   E CG2 
17224 N  N   . ALA   E 806 ? 1.6431 1.8310 1.9479 -0.1414 -0.2575 -0.0372 1110 ALA   E N   
17225 C  CA  . ALA   E 806 ? 1.5847 1.7827 1.9182 -0.1456 -0.2620 -0.0380 1110 ALA   E CA  
17226 C  C   . ALA   E 806 ? 1.5640 1.7714 1.9160 -0.1499 -0.2499 -0.0336 1110 ALA   E C   
17227 O  O   . ALA   E 806 ? 1.5908 1.7928 1.9388 -0.1528 -0.2438 -0.0327 1110 ALA   E O   
17228 C  CB  . ALA   E 806 ? 1.5006 1.6909 1.8374 -0.1486 -0.2743 -0.0433 1110 ALA   E CB  
17229 N  N   . ASN   E 807 ? 1.5228 1.7436 1.8944 -0.1499 -0.2463 -0.0309 1111 ASN   E N   
17230 C  CA  . ASN   E 807 ? 1.5150 1.7451 1.9065 -0.1538 -0.2353 -0.0268 1111 ASN   E CA  
17231 C  C   . ASN   E 807 ? 1.5104 1.7388 1.8880 -0.1520 -0.2212 -0.0222 1111 ASN   E C   
17232 O  O   . ASN   E 807 ? 1.5072 1.7338 1.8881 -0.1554 -0.2135 -0.0202 1111 ASN   E O   
17233 C  CB  . ASN   E 807 ? 1.4674 1.6951 1.8733 -0.1602 -0.2374 -0.0285 1111 ASN   E CB  
17234 C  CG  . ASN   E 807 ? 1.4956 1.7250 1.9172 -0.1624 -0.2518 -0.0334 1111 ASN   E CG  
17235 O  OD1 . ASN   E 807 ? 1.4937 1.7138 1.9011 -0.1605 -0.2632 -0.0379 1111 ASN   E OD1 
17236 N  ND2 . ASN   E 807 ? 1.4414 1.6823 1.8928 -0.1664 -0.2514 -0.0325 1111 ASN   E ND2 
17237 N  N   . LEU   E 808 ? 1.5235 1.7523 1.8860 -0.1467 -0.2181 -0.0205 1112 LEU   E N   
17238 C  CA  . LEU   E 808 ? 1.4546 1.6811 1.8029 -0.1446 -0.2060 -0.0166 1112 LEU   E CA  
17239 C  C   . LEU   E 808 ? 1.4500 1.6876 1.8079 -0.1424 -0.1974 -0.0123 1112 LEU   E C   
17240 O  O   . LEU   E 808 ? 1.5399 1.7815 1.8957 -0.1386 -0.2006 -0.0124 1112 LEU   E O   
17241 C  CB  . LEU   E 808 ? 1.4799 1.6960 1.8003 -0.1402 -0.2084 -0.0182 1112 LEU   E CB  
17242 C  CG  . LEU   E 808 ? 1.4400 1.6518 1.7451 -0.1387 -0.1971 -0.0150 1112 LEU   E CG  
17243 C  CD1 . LEU   E 808 ? 1.4234 1.6335 1.7367 -0.1434 -0.1918 -0.0141 1112 LEU   E CD1 
17244 C  CD2 . LEU   E 808 ? 1.3745 1.5747 1.6537 -0.1354 -0.2002 -0.0172 1112 LEU   E CD2 
17245 N  N   . GLU   E 819 ? 1.7514 2.0024 2.1448 -0.1429 -0.2256 -0.0199 1123 GLU   E N   
17246 C  CA  . GLU   E 819 ? 1.7506 1.9941 2.1302 -0.1400 -0.2385 -0.0245 1123 GLU   E CA  
17247 C  C   . GLU   E 819 ? 1.8074 2.0482 2.1660 -0.1339 -0.2365 -0.0233 1123 GLU   E C   
17248 O  O   . GLU   E 819 ? 1.8273 2.0725 2.1883 -0.1305 -0.2421 -0.0241 1123 GLU   E O   
17249 C  CB  . GLU   E 819 ? 1.6980 1.9487 2.0984 -0.1410 -0.2500 -0.0277 1123 GLU   E CB  
17250 N  N   . ALA   E 820 ? 1.7349 1.9683 2.0733 -0.1324 -0.2284 -0.0213 1124 ALA   E N   
17251 C  CA  . ALA   E 820 ? 1.7032 1.9327 2.0207 -0.1268 -0.2265 -0.0203 1124 ALA   E CA  
17252 C  C   . ALA   E 820 ? 1.7766 1.9956 2.0767 -0.1240 -0.2379 -0.0247 1124 ALA   E C   
17253 O  O   . ALA   E 820 ? 1.8207 2.0309 2.1150 -0.1260 -0.2439 -0.0279 1124 ALA   E O   
17254 C  CB  . ALA   E 820 ? 1.5972 1.8218 1.8993 -0.1263 -0.2151 -0.0173 1124 ALA   E CB  
17255 N  N   . THR   E 821 ? 1.7986 2.0177 2.0898 -0.1191 -0.2410 -0.0247 1125 THR   E N   
17256 C  CA  . THR   E 821 ? 1.8177 2.0266 2.0925 -0.1158 -0.2521 -0.0287 1125 THR   E CA  
17257 C  C   . THR   E 821 ? 1.8230 2.0182 2.0723 -0.1145 -0.2497 -0.0293 1125 THR   E C   
17258 O  O   . THR   E 821 ? 1.8047 1.9992 2.0458 -0.1143 -0.2390 -0.0262 1125 THR   E O   
17259 C  CB  . THR   E 821 ? 1.8029 2.0144 2.0728 -0.1104 -0.2550 -0.0283 1125 THR   E CB  
17260 O  OG1 . THR   E 821 ? 1.8214 2.0199 2.0680 -0.1064 -0.2623 -0.0311 1125 THR   E OG1 
17261 C  CG2 . THR   E 821 ? 1.7586 1.9753 2.0246 -0.1083 -0.2432 -0.0236 1125 THR   E CG2 
17262 N  N   . ALA   E 822 ? 1.7988 1.9827 2.0351 -0.1133 -0.2596 -0.0335 1126 ALA   E N   
17263 C  CA  . ALA   E 822 ? 1.7475 1.9181 1.9573 -0.1106 -0.2572 -0.0338 1126 ALA   E CA  
17264 C  C   . ALA   E 822 ? 1.7467 1.9181 1.9438 -0.1062 -0.2493 -0.0305 1126 ALA   E C   
17265 O  O   . ALA   E 822 ? 1.7172 1.8887 1.9083 -0.1066 -0.2388 -0.0275 1126 ALA   E O   
17266 C  CB  . ALA   E 822 ? 1.6764 1.8346 1.8723 -0.1081 -0.2696 -0.0386 1126 ALA   E CB  
17267 N  N   . ASP   E 823 ? 1.7211 1.8941 1.9162 -0.1022 -0.2543 -0.0308 1127 ASP   E N   
17268 C  CA  . ASP   E 823 ? 1.7247 1.8960 1.9051 -0.0977 -0.2486 -0.0283 1127 ASP   E CA  
17269 C  C   . ASP   E 823 ? 1.7211 1.9014 1.9082 -0.0988 -0.2359 -0.0237 1127 ASP   E C   
17270 O  O   . ASP   E 823 ? 1.6790 1.8559 1.8516 -0.0958 -0.2297 -0.0217 1127 ASP   E O   
17271 C  CB  . ASP   E 823 ? 1.7676 1.9410 1.9494 -0.0937 -0.2562 -0.0293 1127 ASP   E CB  
17272 C  CG  . ASP   E 823 ? 1.8086 1.9680 1.9656 -0.0886 -0.2618 -0.0313 1127 ASP   E CG  
17273 O  OD1 . ASP   E 823 ? 1.8352 1.9832 1.9776 -0.0888 -0.2629 -0.0331 1127 ASP   E OD1 
17274 O  OD2 . ASP   E 823 ? 1.8535 2.0127 2.0050 -0.0842 -0.2644 -0.0309 1127 ASP   E OD2 
17275 N  N   . ASP   E 824 ? 1.7970 1.9887 2.0056 -0.1026 -0.2320 -0.0220 1128 ASP   E N   
17276 C  CA  . ASP   E 824 ? 1.7996 1.9974 2.0109 -0.1031 -0.2197 -0.0179 1128 ASP   E CA  
17277 C  C   . ASP   E 824 ? 1.7828 1.9745 1.9851 -0.1054 -0.2129 -0.0172 1128 ASP   E C   
17278 O  O   . ASP   E 824 ? 1.7530 1.9488 1.9570 -0.1059 -0.2030 -0.0141 1128 ASP   E O   
17279 C  CB  . ASP   E 824 ? 1.8285 2.0401 2.0644 -0.1056 -0.2164 -0.0157 1128 ASP   E CB  
17280 C  CG  . ASP   E 824 ? 1.8426 2.0571 2.0946 -0.1109 -0.2175 -0.0167 1128 ASP   E CG  
17281 O  OD1 . ASP   E 824 ? 1.8888 2.0970 2.1339 -0.1132 -0.2142 -0.0170 1128 ASP   E OD1 
17282 O  OD2 . ASP   E 824 ? 1.8255 2.0487 2.0981 -0.1128 -0.2213 -0.0171 1128 ASP   E OD2 
17283 N  N   . LEU   E 825 ? 1.7103 1.8920 1.9028 -0.1064 -0.2181 -0.0203 1129 LEU   E N   
17284 C  CA  . LEU   E 825 ? 1.6232 1.7984 1.8062 -0.1081 -0.2121 -0.0199 1129 LEU   E CA  
17285 C  C   . LEU   E 825 ? 1.5447 1.7075 1.7032 -0.1047 -0.2124 -0.0210 1129 LEU   E C   
17286 O  O   . LEU   E 825 ? 1.5221 1.6813 1.6714 -0.1047 -0.2048 -0.0196 1129 LEU   E O   
17287 C  CB  . LEU   E 825 ? 1.6027 1.7764 1.7956 -0.1127 -0.2163 -0.0221 1129 LEU   E CB  
17288 C  CG  . LEU   E 825 ? 1.5756 1.7601 1.7884 -0.1164 -0.2090 -0.0193 1129 LEU   E CG  
17289 C  CD1 . LEU   E 825 ? 1.5428 1.7269 1.7687 -0.1217 -0.2121 -0.0211 1129 LEU   E CD1 
17290 C  CD2 . LEU   E 825 ? 1.5177 1.7018 1.7217 -0.1154 -0.1975 -0.0160 1129 LEU   E CD2 
17291 N  N   . ILE   E 826 ? 1.5849 1.7409 1.7328 -0.1015 -0.2208 -0.0235 1130 ILE   E N   
17292 C  CA  . ILE   E 826 ? 1.5514 1.6963 1.6759 -0.0974 -0.2194 -0.0237 1130 ILE   E CA  
17293 C  C   . ILE   E 826 ? 1.5357 1.6852 1.6569 -0.0954 -0.2097 -0.0200 1130 ILE   E C   
17294 O  O   . ILE   E 826 ? 1.5008 1.6447 1.6088 -0.0942 -0.2031 -0.0189 1130 ILE   E O   
17295 C  CB  . ILE   E 826 ? 1.4818 1.6189 1.5953 -0.0935 -0.2293 -0.0264 1130 ILE   E CB  
17296 C  CG1 . ILE   E 826 ? 1.4984 1.6302 1.6145 -0.0952 -0.2400 -0.0305 1130 ILE   E CG1 
17297 C  CG2 . ILE   E 826 ? 1.4212 1.5453 1.5102 -0.0897 -0.2275 -0.0267 1130 ILE   E CG2 
17298 C  CD1 . ILE   E 826 ? 1.5554 1.6957 1.6893 -0.0957 -0.2485 -0.0318 1130 ILE   E CD1 
17299 N  N   . LYS   E 827 ? 1.4996 1.6594 1.6335 -0.0949 -0.2086 -0.0181 1131 LYS   E N   
17300 C  CA  . LYS   E 827 ? 1.5113 1.6755 1.6428 -0.0929 -0.2001 -0.0147 1131 LYS   E CA  
17301 C  C   . LYS   E 827 ? 1.5115 1.6793 1.6469 -0.0953 -0.1904 -0.0125 1131 LYS   E C   
17302 O  O   . LYS   E 827 ? 1.4899 1.6547 1.6146 -0.0936 -0.1836 -0.0109 1131 LYS   E O   
17303 C  CB  . LYS   E 827 ? 1.5833 1.7579 1.7283 -0.0918 -0.2014 -0.0133 1131 LYS   E CB  
17304 C  CG  . LYS   E 827 ? 1.6710 1.8562 1.8387 -0.0955 -0.2024 -0.0131 1131 LYS   E CG  
17305 C  CD  . LYS   E 827 ? 1.6909 1.8861 1.8696 -0.0963 -0.1929 -0.0094 1131 LYS   E CD  
17306 C  CE  . LYS   E 827 ? 1.7107 1.9161 1.9123 -0.0997 -0.1938 -0.0090 1131 LYS   E CE  
17307 N  NZ  . LYS   E 827 ? 1.6789 1.8947 1.8926 -0.0993 -0.1865 -0.0055 1131 LYS   E NZ  
17308 N  N   . VAL   E 828 ? 1.5544 1.7284 1.7055 -0.0992 -0.1897 -0.0124 1132 VAL   E N   
17309 C  CA  . VAL   E 828 ? 1.5136 1.6900 1.6678 -0.1013 -0.1808 -0.0103 1132 VAL   E CA  
17310 C  C   . VAL   E 828 ? 1.4774 1.6436 1.6144 -0.1006 -0.1781 -0.0112 1132 VAL   E C   
17311 O  O   . VAL   E 828 ? 1.4371 1.6024 1.5664 -0.0990 -0.1708 -0.0094 1132 VAL   E O   
17312 C  CB  . VAL   E 828 ? 1.4992 1.6811 1.6708 -0.1057 -0.1813 -0.0105 1132 VAL   E CB  
17313 C  CG1 . VAL   E 828 ? 1.4207 1.6005 1.5903 -0.1077 -0.1738 -0.0094 1132 VAL   E CG1 
17314 C  CG2 . VAL   E 828 ? 1.5005 1.6942 1.6901 -0.1062 -0.1796 -0.0083 1132 VAL   E CG2 
17315 N  N   . VAL   E 829 ? 1.4732 1.6312 1.6038 -0.1016 -0.1842 -0.0141 1133 VAL   E N   
17316 C  CA  . VAL   E 829 ? 1.4299 1.5777 1.5445 -0.1010 -0.1818 -0.0151 1133 VAL   E CA  
17317 C  C   . VAL   E 829 ? 1.4283 1.5705 1.5263 -0.0967 -0.1792 -0.0145 1133 VAL   E C   
17318 O  O   . VAL   E 829 ? 1.3605 1.4994 1.4495 -0.0958 -0.1725 -0.0134 1133 VAL   E O   
17319 C  CB  . VAL   E 829 ? 1.3871 1.5267 1.4978 -0.1024 -0.1899 -0.0186 1133 VAL   E CB  
17320 C  CG1 . VAL   E 829 ? 1.3692 1.4961 1.4586 -0.0995 -0.1907 -0.0201 1133 VAL   E CG1 
17321 C  CG2 . VAL   E 829 ? 1.2871 1.4289 1.4087 -0.1068 -0.1880 -0.0187 1133 VAL   E CG2 
17322 N  N   . GLU   E 830 ? 1.4847 1.6259 1.5789 -0.0940 -0.1843 -0.0150 1134 GLU   E N   
17323 C  CA  . GLU   E 830 ? 1.4322 1.5686 1.5119 -0.0900 -0.1812 -0.0139 1134 GLU   E CA  
17324 C  C   . GLU   E 830 ? 1.4115 1.5552 1.4955 -0.0896 -0.1721 -0.0108 1134 GLU   E C   
17325 O  O   . GLU   E 830 ? 1.4084 1.5477 1.4809 -0.0874 -0.1670 -0.0098 1134 GLU   E O   
17326 C  CB  . GLU   E 830 ? 1.4413 1.5762 1.5179 -0.0872 -0.1881 -0.0147 1134 GLU   E CB  
17327 C  CG  . GLU   E 830 ? 1.4841 1.6063 1.5449 -0.0849 -0.1952 -0.0176 1134 GLU   E CG  
17328 C  CD  . GLU   E 830 ? 1.5329 1.6552 1.5972 -0.0836 -0.2054 -0.0195 1134 GLU   E CD  
17329 O  OE1 . GLU   E 830 ? 1.5666 1.6988 1.6489 -0.0860 -0.2086 -0.0196 1134 GLU   E OE1 
17330 O  OE2 . GLU   E 830 ? 1.5219 1.6341 1.5709 -0.0799 -0.2102 -0.0210 1134 GLU   E OE2 
17331 N  N   . GLU   E 831 ? 1.3418 1.4962 1.4421 -0.0916 -0.1700 -0.0091 1135 GLU   E N   
17332 C  CA  . GLU   E 831 ? 1.3512 1.5117 1.4555 -0.0913 -0.1616 -0.0064 1135 GLU   E CA  
17333 C  C   . GLU   E 831 ? 1.3650 1.5221 1.4643 -0.0924 -0.1556 -0.0062 1135 GLU   E C   
17334 O  O   . GLU   E 831 ? 1.3325 1.4894 1.4263 -0.0908 -0.1493 -0.0048 1135 GLU   E O   
17335 C  CB  . GLU   E 831 ? 1.3765 1.5481 1.4988 -0.0930 -0.1606 -0.0048 1135 GLU   E CB  
17336 C  CG  . GLU   E 831 ? 1.4033 1.5809 1.5303 -0.0928 -0.1521 -0.0021 1135 GLU   E CG  
17337 C  CD  . GLU   E 831 ? 1.4835 1.6616 1.6042 -0.0894 -0.1492 -0.0006 1135 GLU   E CD  
17338 O  OE1 . GLU   E 831 ? 1.5068 1.6804 1.6192 -0.0874 -0.1535 -0.0015 1135 GLU   E OE1 
17339 O  OE2 . GLU   E 831 ? 1.4507 1.6330 1.5742 -0.0888 -0.1429 0.0014  1135 GLU   E OE2 
17340 N  N   . LEU   E 832 ? 1.3694 1.5239 1.4710 -0.0951 -0.1576 -0.0077 1136 LEU   E N   
17341 C  CA  . LEU   E 832 ? 1.2894 1.4404 1.3863 -0.0960 -0.1522 -0.0077 1136 LEU   E CA  
17342 C  C   . LEU   E 832 ? 1.2681 1.4093 1.3477 -0.0935 -0.1514 -0.0088 1136 LEU   E C   
17343 O  O   . LEU   E 832 ? 1.3014 1.4412 1.3758 -0.0927 -0.1451 -0.0079 1136 LEU   E O   
17344 C  CB  . LEU   E 832 ? 1.2365 1.3869 1.3405 -0.0995 -0.1546 -0.0089 1136 LEU   E CB  
17345 C  CG  . LEU   E 832 ? 1.1937 1.3535 1.3156 -0.1023 -0.1530 -0.0074 1136 LEU   E CG  
17346 C  CD1 . LEU   E 832 ? 1.3163 1.4803 1.4487 -0.1034 -0.1602 -0.0083 1136 LEU   E CD1 
17347 C  CD2 . LEU   E 832 ? 1.1471 1.3051 1.2726 -0.1052 -0.1508 -0.0078 1136 LEU   E CD2 
17348 N  N   . THR   E 833 ? 1.2542 1.3884 1.3245 -0.0920 -0.1574 -0.0105 1137 THR   E N   
17349 C  CA  . THR   E 833 ? 1.2478 1.3721 1.3011 -0.0893 -0.1559 -0.0112 1137 THR   E CA  
17350 C  C   . THR   E 833 ? 1.2937 1.4198 1.3427 -0.0867 -0.1495 -0.0091 1137 THR   E C   
17351 O  O   . THR   E 833 ? 1.2915 1.4106 1.3281 -0.0846 -0.1461 -0.0092 1137 THR   E O   
17352 C  CB  . THR   E 833 ? 1.3165 1.4325 1.3603 -0.0877 -0.1639 -0.0135 1137 THR   E CB  
17353 O  OG1 . THR   E 833 ? 1.4417 1.5465 1.4684 -0.0854 -0.1625 -0.0144 1137 THR   E OG1 
17354 C  CG2 . THR   E 833 ? 1.3412 1.4597 1.3854 -0.0854 -0.1669 -0.0127 1137 THR   E CG2 
17355 N  N   . ARG   E 834 ? 1.2716 1.4068 1.3308 -0.0868 -0.1474 -0.0071 1138 ARG   E N   
17356 C  CA  . ARG   E 834 ? 1.2300 1.3669 1.2860 -0.0845 -0.1419 -0.0053 1138 ARG   E CA  
17357 C  C   . ARG   E 834 ? 1.2086 1.3482 1.2668 -0.0849 -0.1345 -0.0042 1138 ARG   E C   
17358 O  O   . ARG   E 834 ? 1.1906 1.3306 1.2455 -0.0831 -0.1298 -0.0029 1138 ARG   E O   
17359 C  CB  . ARG   E 834 ? 1.2242 1.3691 1.2896 -0.0840 -0.1430 -0.0037 1138 ARG   E CB  
17360 C  CG  . ARG   E 834 ? 1.3041 1.4489 1.3716 -0.0837 -0.1509 -0.0048 1138 ARG   E CG  
17361 C  CD  . ARG   E 834 ? 1.3354 1.4713 1.3887 -0.0806 -0.1542 -0.0055 1138 ARG   E CD  
17362 N  NE  . ARG   E 834 ? 1.3173 1.4530 1.3730 -0.0803 -0.1625 -0.0069 1138 ARG   E NE  
17363 C  CZ  . ARG   E 834 ? 1.3681 1.4945 1.4116 -0.0780 -0.1681 -0.0085 1138 ARG   E CZ  
17364 N  NH1 . ARG   E 834 ? 1.3476 1.4637 1.3751 -0.0759 -0.1656 -0.0089 1138 ARG   E NH1 
17365 N  NH2 . ARG   E 834 ? 1.3973 1.5244 1.4449 -0.0778 -0.1763 -0.0100 1138 ARG   E NH2 
17366 N  N   . ILE   E 835 ? 1.1816 1.3229 1.2453 -0.0872 -0.1333 -0.0046 1139 ILE   E N   
17367 C  CA  . ILE   E 835 ? 1.1930 1.3366 1.2584 -0.0872 -0.1267 -0.0037 1139 ILE   E CA  
17368 C  C   . ILE   E 835 ? 1.1686 1.3044 1.2225 -0.0860 -0.1238 -0.0047 1139 ILE   E C   
17369 O  O   . ILE   E 835 ? 1.0978 1.2350 1.1520 -0.0854 -0.1183 -0.0042 1139 ILE   E O   
17370 C  CB  . ILE   E 835 ? 1.1306 1.2790 1.2064 -0.0897 -0.1258 -0.0035 1139 ILE   E CB  
17371 C  CG1 . ILE   E 835 ? 1.1575 1.3008 1.2314 -0.0918 -0.1295 -0.0053 1139 ILE   E CG1 
17372 C  CG2 . ILE   E 835 ? 1.1661 1.3227 1.2541 -0.0906 -0.1275 -0.0022 1139 ILE   E CG2 
17373 C  CD1 . ILE   E 835 ? 1.1394 1.2876 1.2247 -0.0944 -0.1288 -0.0048 1139 ILE   E CD1 
17374 N  N   . HIS   E 836 ? 1.1304 1.2580 1.1741 -0.0854 -0.1272 -0.0062 1140 HIS   E N   
17375 C  CA  . HIS   E 836 ? 1.1151 1.2349 1.1468 -0.0835 -0.1240 -0.0069 1140 HIS   E CA  
17376 C  C   . HIS   E 836 ? 1.1348 1.2472 1.1554 -0.0814 -0.1274 -0.0074 1140 HIS   E C   
17377 O  O   . HIS   E 836 ? 1.2166 1.3223 1.2264 -0.0791 -0.1242 -0.0074 1140 HIS   E O   
17378 C  CB  . HIS   E 836 ? 1.1937 1.3087 1.2222 -0.0847 -0.1241 -0.0085 1140 HIS   E CB  
17379 C  CG  . HIS   E 836 ? 1.1331 1.2419 1.1573 -0.0857 -0.1310 -0.0104 1140 HIS   E CG  
17380 N  ND1 . HIS   E 836 ? 1.1184 1.2166 1.1287 -0.0840 -0.1327 -0.0119 1140 HIS   E ND1 
17381 C  CD2 . HIS   E 836 ? 1.1134 1.2251 1.1455 -0.0882 -0.1367 -0.0111 1140 HIS   E CD2 
17382 C  CE1 . HIS   E 836 ? 1.1947 1.2891 1.2041 -0.0853 -0.1397 -0.0137 1140 HIS   E CE1 
17383 N  NE2 . HIS   E 836 ? 1.1463 1.2491 1.1696 -0.0880 -0.1423 -0.0133 1140 HIS   E NE2 
17384 N  N   . SER   F 3   ? 1.8899 1.1274 1.0430 0.2813  0.0695  0.0419  868  SER   F N   
17385 C  CA  . SER   F 3   ? 2.0122 1.2428 1.1701 0.2708  0.0868  0.0503  868  SER   F CA  
17386 C  C   . SER   F 3   ? 2.0265 1.2717 1.2028 0.2623  0.0940  0.0544  868  SER   F C   
17387 O  O   . SER   F 3   ? 1.9109 1.1833 1.1179 0.2497  0.0909  0.0528  868  SER   F O   
17388 C  CB  . SER   F 3   ? 2.0374 1.2322 1.1611 0.2810  0.0979  0.0559  868  SER   F CB  
17389 O  OG  . SER   F 3   ? 2.0636 1.2420 1.1607 0.2971  0.0937  0.0545  868  SER   F OG  
17390 N  N   . LEU   F 4   ? 2.0950 1.3213 1.2519 0.2694  0.1037  0.0597  869  LEU   F N   
17391 C  CA  . LEU   F 4   ? 2.0631 1.2997 1.2340 0.2629  0.1118  0.0641  869  LEU   F CA  
17392 C  C   . LEU   F 4   ? 2.0268 1.2807 1.2052 0.2672  0.0997  0.0588  869  LEU   F C   
17393 O  O   . LEU   F 4   ? 1.9683 1.2276 1.1528 0.2652  0.1053  0.0620  869  LEU   F O   
17394 C  CB  . LEU   F 4   ? 2.0935 1.3019 1.2397 0.2694  0.1277  0.0722  869  LEU   F CB  
17395 C  CG  . LEU   F 4   ? 2.1583 1.3605 1.3129 0.2578  0.1445  0.0800  869  LEU   F CG  
17396 C  CD1 . LEU   F 4   ? 2.1275 1.3127 1.2698 0.2604  0.1609  0.0883  869  LEU   F CD1 
17397 C  CD2 . LEU   F 4   ? 2.1092 1.3425 1.3028 0.2400  0.1425  0.0788  869  LEU   F CD2 
17398 N  N   . THR   F 5   ? 1.9988 1.2608 1.1765 0.2735  0.0835  0.0507  870  THR   F N   
17399 C  CA  . THR   F 5   ? 1.9165 1.1943 1.1010 0.2782  0.0705  0.0448  870  THR   F CA  
17400 C  C   . THR   F 5   ? 1.8497 1.1597 1.0665 0.2678  0.0589  0.0387  870  THR   F C   
17401 O  O   . THR   F 5   ? 1.8188 1.1452 1.0459 0.2696  0.0481  0.0337  870  THR   F O   
17402 C  CB  . THR   F 5   ? 1.8718 1.1296 1.0256 0.2967  0.0607  0.0402  870  THR   F CB  
17403 O  OG1 . THR   F 5   ? 1.9275 1.2033 1.0912 0.3006  0.0451  0.0328  870  THR   F OG1 
17404 C  CG2 . THR   F 5   ? 1.9318 1.1780 1.0736 0.3010  0.0566  0.0376  870  THR   F CG2 
17405 N  N   . THR   F 6   ? 1.8150 1.1338 1.0477 0.2568  0.0611  0.0391  871  THR   F N   
17406 C  CA  . THR   F 6   ? 1.7801 1.1278 1.0423 0.2468  0.0511  0.0337  871  THR   F CA  
17407 C  C   . THR   F 6   ? 1.7722 1.1411 1.0637 0.2308  0.0582  0.0373  871  THR   F C   
17408 O  O   . THR   F 6   ? 1.7820 1.1437 1.0756 0.2232  0.0716  0.0439  871  THR   F O   
17409 C  CB  . THR   F 6   ? 1.8153 1.1601 1.0771 0.2448  0.0484  0.0314  871  THR   F CB  
17410 O  OG1 . THR   F 6   ? 1.9483 1.2838 1.2114 0.2359  0.0625  0.0382  871  THR   F OG1 
17411 C  CG2 . THR   F 6   ? 1.7619 1.0845 0.9940 0.2611  0.0416  0.0280  871  THR   F CG2 
17412 N  N   . CYS   F 7   ? 1.7580 1.1533 1.0728 0.2256  0.0488  0.0328  872  CYS   F N   
17413 C  CA  . CYS   F 7   ? 1.6794 1.0974 1.0234 0.2109  0.0530  0.0350  872  CYS   F CA  
17414 C  C   . CYS   F 7   ? 1.6715 1.1011 1.0345 0.1986  0.0537  0.0347  872  CYS   F C   
17415 O  O   . CYS   F 7   ? 1.6534 1.0873 1.0176 0.2003  0.0445  0.0294  872  CYS   F O   
17416 C  CB  . CYS   F 7   ? 1.6084 1.0489 0.9683 0.2110  0.0417  0.0298  872  CYS   F CB  
17417 S  SG  . CYS   F 7   ? 1.5180 0.9911 0.9167 0.1931  0.0422  0.0301  872  CYS   F SG  
17418 N  N   . GLU   F 8   ? 1.6442 1.0787 1.0222 0.1864  0.0647  0.0402  873  GLU   F N   
17419 C  CA  . GLU   F 8   ? 1.6356 1.0791 1.0304 0.1746  0.0660  0.0402  873  GLU   F CA  
17420 C  C   . GLU   F 8   ? 1.5975 1.0710 1.0216 0.1648  0.0571  0.0357  873  GLU   F C   
17421 O  O   . GLU   F 8   ? 1.6118 1.0937 1.0488 0.1566  0.0553  0.0342  873  GLU   F O   
17422 C  CB  . GLU   F 8   ? 1.6657 1.1009 1.0646 0.1655  0.0813  0.0479  873  GLU   F CB  
17423 C  CG  . GLU   F 8   ? 1.8263 1.2348 1.1995 0.1744  0.0924  0.0537  873  GLU   F CG  
17424 C  CD  . GLU   F 8   ? 1.8639 1.2550 1.2313 0.1694  0.1053  0.0597  873  GLU   F CD  
17425 O  OE1 . GLU   F 8   ? 1.9136 1.2811 1.2560 0.1784  0.1075  0.0605  873  GLU   F OE1 
17426 O  OE2 . GLU   F 8   ? 1.8906 1.2917 1.2788 0.1565  0.1130  0.0635  873  GLU   F OE2 
17427 N  N   . VAL   F 9   ? 1.5034 0.9927 0.9380 0.1654  0.0515  0.0335  874  VAL   F N   
17428 C  CA  . VAL   F 9   ? 1.4942 1.0113 0.9562 0.1560  0.0435  0.0294  874  VAL   F CA  
17429 C  C   . VAL   F 9   ? 1.5389 1.0640 1.0008 0.1619  0.0295  0.0218  874  VAL   F C   
17430 O  O   . VAL   F 9   ? 1.5215 1.0602 0.9987 0.1549  0.0246  0.0187  874  VAL   F O   
17431 C  CB  . VAL   F 9   ? 1.4065 0.9380 0.8818 0.1529  0.0443  0.0307  874  VAL   F CB  
17432 C  CG1 . VAL   F 9   ? 1.3479 0.9051 0.8445 0.1486  0.0326  0.0248  874  VAL   F CG1 
17433 C  CG2 . VAL   F 9   ? 1.3911 0.9247 0.8789 0.1418  0.0567  0.0373  874  VAL   F CG2 
17434 N  N   . CYS   F 10  ? 1.5272 1.0442 0.9724 0.1748  0.0226  0.0185  875  CYS   F N   
17435 C  CA  . CYS   F 10  ? 1.4564 0.9840 0.9050 0.1804  0.0087  0.0110  875  CYS   F CA  
17436 C  C   . CYS   F 10  ? 1.5850 1.0933 1.0096 0.1929  0.0042  0.0082  875  CYS   F C   
17437 O  O   . CYS   F 10  ? 1.5763 1.0926 1.0032 0.1985  -0.0076 0.0018  875  CYS   F O   
17438 C  CB  . CYS   F 10  ? 1.4697 1.0091 0.9237 0.1847  0.0014  0.0080  875  CYS   F CB  
17439 S  SG  . CYS   F 10  ? 1.4095 0.9246 0.8330 0.2006  0.0027  0.0095  875  CYS   F SG  
17440 N  N   . GLY   F 11  ? 1.6236 1.1067 1.0254 0.1980  0.0130  0.0127  876  GLY   F N   
17441 C  CA  . GLY   F 11  ? 1.6158 1.0781 0.9924 0.2105  0.0095  0.0106  876  GLY   F CA  
17442 C  C   . GLY   F 11  ? 1.6327 1.0815 0.9877 0.2256  0.0042  0.0085  876  GLY   F C   
17443 O  O   . GLY   F 11  ? 1.6546 1.0877 0.9895 0.2369  -0.0009 0.0056  876  GLY   F O   
17444 N  N   . ALA   F 12  ? 1.6336 1.0874 0.9914 0.2264  0.0049  0.0097  877  ALA   F N   
17445 C  CA  . ALA   F 12  ? 1.6399 1.0799 0.9763 0.2408  -0.0002 0.0078  877  ALA   F CA  
17446 C  C   . ALA   F 12  ? 1.6564 1.0643 0.9602 0.2512  0.0073  0.0117  877  ALA   F C   
17447 O  O   . ALA   F 12  ? 1.7342 1.1305 1.0330 0.2460  0.0207  0.0184  877  ALA   F O   
17448 C  CB  . ALA   F 12  ? 1.5999 1.0484 0.9441 0.2385  0.0025  0.0100  877  ALA   F CB  
17449 N  N   . CYS   F 13  ? 1.6141 1.0071 0.8957 0.2662  -0.0013 0.0075  878  CYS   F N   
17450 C  CA  . CYS   F 13  ? 1.7591 1.1202 1.0070 0.2780  0.0053  0.0111  878  CYS   F CA  
17451 C  C   . CYS   F 13  ? 1.7842 1.1342 1.0132 0.2914  0.0001  0.0094  878  CYS   F C   
17452 O  O   . CYS   F 13  ? 1.7678 1.1194 0.9917 0.3013  -0.0139 0.0024  878  CYS   F O   
17453 C  CB  . CYS   F 13  ? 1.7440 1.0901 0.9756 0.2852  0.0014  0.0085  878  CYS   F CB  
17454 S  SG  . CYS   F 13  ? 1.9411 1.2466 1.1317 0.2974  0.0133  0.0149  878  CYS   F SG  
17455 N  N   . PHE   F 14  ? 1.7528 1.0893 0.9696 0.2927  0.0115  0.0157  879  PHE   F N   
17456 C  CA  . PHE   F 14  ? 1.8455 1.1678 1.0409 0.3059  0.0082  0.0149  879  PHE   F CA  
17457 C  C   . PHE   F 14  ? 1.9260 1.2144 1.0839 0.3207  0.0112  0.0166  879  PHE   F C   
17458 O  O   . PHE   F 14  ? 1.9059 1.1826 1.0545 0.3216  0.0139  0.0174  879  PHE   F O   
17459 C  CB  . PHE   F 14  ? 1.8024 1.1281 1.0038 0.3004  0.0186  0.0207  879  PHE   F CB  
17460 C  CG  . PHE   F 14  ? 1.7585 1.1157 0.9945 0.2869  0.0155  0.0191  879  PHE   F CG  
17461 C  CD1 . PHE   F 14  ? 1.6634 1.0381 0.9113 0.2894  0.0015  0.0124  879  PHE   F CD1 
17462 C  CD2 . PHE   F 14  ? 1.7569 1.1268 1.0145 0.2715  0.0259  0.0239  879  PHE   F CD2 
17463 C  CE1 . PHE   F 14  ? 1.6404 1.0440 0.9201 0.2770  -0.0012 0.0109  879  PHE   F CE1 
17464 C  CE2 . PHE   F 14  ? 1.7170 1.1163 1.0067 0.2591  0.0226  0.0222  879  PHE   F CE2 
17465 C  CZ  . PHE   F 14  ? 1.6819 1.0979 0.9823 0.2618  0.0093  0.0159  879  PHE   F CZ  
17466 N  N   . GLU   F 15  ? 1.9700 1.2413 1.1051 0.3326  0.0113  0.0174  880  GLU   F N   
17467 C  CA  . GLU   F 15  ? 1.9567 1.1940 1.0542 0.3472  0.0153  0.0196  880  GLU   F CA  
17468 C  C   . GLU   F 15  ? 2.0158 1.2341 1.0976 0.3474  0.0329  0.0287  880  GLU   F C   
17469 O  O   . GLU   F 15  ? 2.1461 1.3358 1.1998 0.3552  0.0417  0.0331  880  GLU   F O   
17470 C  CB  . GLU   F 15  ? 2.0909 1.3193 1.1695 0.3637  0.0000  0.0126  880  GLU   F CB  
17471 C  CG  . GLU   F 15  ? 2.1874 1.4292 1.2762 0.3666  -0.0175 0.0035  880  GLU   F CG  
17472 C  CD  . GLU   F 15  ? 2.3276 1.5551 1.3931 0.3846  -0.0321 -0.0032 880  GLU   F CD  
17473 O  OE1 . GLU   F 15  ? 2.3998 1.6334 1.4689 0.3894  -0.0461 -0.0104 880  GLU   F OE1 
17474 O  OE2 . GLU   F 15  ? 2.4193 1.6293 1.4630 0.3942  -0.0297 -0.0011 880  GLU   F OE2 
17475 N  N   . THR   F 16  ? 2.1083 1.3412 1.2075 0.3389  0.0387  0.0319  881  THR   F N   
17476 C  CA  . THR   F 16  ? 2.0873 1.3039 1.1744 0.3382  0.0563  0.0408  881  THR   F CA  
17477 C  C   . THR   F 16  ? 2.0248 1.2627 1.1436 0.3196  0.0671  0.0458  881  THR   F C   
17478 O  O   . THR   F 16  ? 1.9924 1.2598 1.1420 0.3089  0.0595  0.0419  881  THR   F O   
17479 C  CB  . THR   F 16  ? 2.0717 1.2818 1.1461 0.3472  0.0550  0.0409  881  THR   F CB  
17480 O  OG1 . THR   F 16  ? 2.0694 1.2691 1.1394 0.3431  0.0736  0.0502  881  THR   F OG1 
17481 C  CG2 . THR   F 16  ? 1.9898 1.2317 1.0940 0.3401  0.0426  0.0349  881  THR   F CG2 
17482 N  N   . ARG   F 17  ? 1.9294 1.1516 1.0400 0.3162  0.0851  0.0545  882  ARG   F N   
17483 C  CA  . ARG   F 17  ? 1.8603 1.1006 0.9995 0.2993  0.0966  0.0599  882  ARG   F CA  
17484 C  C   . ARG   F 17  ? 1.8008 1.0643 0.9613 0.2942  0.0925  0.0584  882  ARG   F C   
17485 O  O   . ARG   F 17  ? 1.7687 1.0581 0.9613 0.2795  0.0931  0.0585  882  ARG   F O   
17486 C  CB  . ARG   F 17  ? 1.8506 1.0681 0.9752 0.2987  0.1168  0.0697  882  ARG   F CB  
17487 C  CG  . ARG   F 17  ? 1.9067 1.0983 1.0082 0.3040  0.1229  0.0722  882  ARG   F CG  
17488 C  CD  . ARG   F 17  ? 2.1637 1.3195 1.2238 0.3213  0.1294  0.0757  882  ARG   F CD  
17489 N  NE  . ARG   F 17  ? 2.1408 1.2931 1.1845 0.3354  0.1159  0.0698  882  ARG   F NE  
17490 C  CZ  . ARG   F 17  ? 2.0912 1.2263 1.1086 0.3501  0.1051  0.0647  882  ARG   F CZ  
17491 N  NH1 . ARG   F 17  ? 2.1565 1.2746 1.1584 0.3538  0.1064  0.0650  882  ARG   F NH1 
17492 N  NH2 . ARG   F 17  ? 2.0205 1.1554 1.0272 0.3614  0.0922  0.0590  882  ARG   F NH2 
17493 N  N   . LYS   F 18  ? 1.7755 1.0292 0.9178 0.3063  0.0885  0.0570  883  LYS   F N   
17494 C  CA  . LYS   F 18  ? 1.7886 1.0637 0.9496 0.3025  0.0832  0.0549  883  LYS   F CA  
17495 C  C   . LYS   F 18  ? 1.7982 1.1008 0.9831 0.2977  0.0656  0.0461  883  LYS   F C   
17496 O  O   . LYS   F 18  ? 1.7391 1.0673 0.9514 0.2878  0.0627  0.0448  883  LYS   F O   
17497 C  CB  . LYS   F 18  ? 1.7891 1.0457 0.9231 0.3177  0.0818  0.0548  883  LYS   F CB  
17498 C  CG  . LYS   F 18  ? 1.6906 0.9669 0.8409 0.3154  0.0755  0.0522  883  LYS   F CG  
17499 C  CD  . LYS   F 18  ? 1.7266 0.9966 0.8745 0.3135  0.0912  0.0602  883  LYS   F CD  
17500 C  CE  . LYS   F 18  ? 1.6910 0.9882 0.8664 0.3048  0.0874  0.0586  883  LYS   F CE  
17501 N  NZ  . LYS   F 18  ? 1.6810 0.9691 0.8479 0.3077  0.0993  0.0648  883  LYS   F NZ  
17502 N  N   . GLY   F 19  ? 1.7854 1.0829 0.9606 0.3048  0.0540  0.0402  884  GLY   F N   
17503 C  CA  . GLY   F 19  ? 1.7991 1.1229 0.9990 0.2988  0.0391  0.0325  884  GLY   F CA  
17504 C  C   . GLY   F 19  ? 1.7296 1.0778 0.9630 0.2805  0.0447  0.0349  884  GLY   F C   
17505 O  O   . GLY   F 19  ? 1.7147 1.0888 0.9743 0.2720  0.0388  0.0321  884  GLY   F O   
17506 N  N   . LEU   F 20  ? 1.7184 1.0576 0.9504 0.2744  0.0561  0.0400  885  LEU   F N   
17507 C  CA  . LEU   F 20  ? 1.6408 1.0005 0.9028 0.2572  0.0623  0.0427  885  LEU   F CA  
17508 C  C   . LEU   F 20  ? 1.6409 1.0127 0.9191 0.2491  0.0707  0.0473  885  LEU   F C   
17509 O  O   . LEU   F 20  ? 1.6324 1.0308 0.9400 0.2375  0.0673  0.0456  885  LEU   F O   
17510 C  CB  . LEU   F 20  ? 1.6220 0.9659 0.8762 0.2535  0.0743  0.0481  885  LEU   F CB  
17511 C  CG  . LEU   F 20  ? 1.7053 1.0615 0.9757 0.2449  0.0691  0.0448  885  LEU   F CG  
17512 C  CD1 . LEU   F 20  ? 1.8682 1.2094 1.1335 0.2393  0.0834  0.0514  885  LEU   F CD1 
17513 C  CD2 . LEU   F 20  ? 1.6084 0.9974 0.9141 0.2314  0.0631  0.0418  885  LEU   F CD2 
17514 N  N   . SER   F 21  ? 1.6454 0.9975 0.9044 0.2554  0.0822  0.0533  886  SER   F N   
17515 C  CA  . SER   F 21  ? 1.6544 1.0157 0.9277 0.2478  0.0923  0.0587  886  SER   F CA  
17516 C  C   . SER   F 21  ? 1.6713 1.0593 0.9670 0.2436  0.0814  0.0537  886  SER   F C   
17517 O  O   . SER   F 21  ? 1.5993 1.0081 0.9220 0.2307  0.0853  0.0558  886  SER   F O   
17518 C  CB  . SER   F 21  ? 1.7060 1.0408 0.9510 0.2590  0.1032  0.0644  886  SER   F CB  
17519 O  OG  . SER   F 21  ? 1.8412 1.1784 1.0981 0.2499  0.1190  0.0721  886  SER   F OG  
17520 N  N   . SER   F 22  ? 1.6522 1.0397 0.9373 0.2544  0.0675  0.0472  887  SER   F N   
17521 C  CA  . SER   F 22  ? 1.6189 1.0314 0.9253 0.2505  0.0566  0.0422  887  SER   F CA  
17522 C  C   . SER   F 22  ? 1.6037 1.0426 0.9395 0.2384  0.0485  0.0377  887  SER   F C   
17523 O  O   . SER   F 22  ? 1.6662 1.1282 1.0289 0.2269  0.0487  0.0380  887  SER   F O   
17524 C  CB  . SER   F 22  ? 1.6781 1.0827 0.9658 0.2652  0.0434  0.0360  887  SER   F CB  
17525 O  OG  . SER   F 22  ? 1.7516 1.1663 1.0460 0.2664  0.0287  0.0284  887  SER   F OG  
17526 N  N   . HIS   F 23  ? 1.6383 1.0735 0.9689 0.2412  0.0412  0.0336  888  HIS   F N   
17527 C  CA  . HIS   F 23  ? 1.6301 1.0885 0.9864 0.2308  0.0333  0.0292  888  HIS   F CA  
17528 C  C   . HIS   F 23  ? 1.6291 1.1026 1.0103 0.2147  0.0433  0.0340  888  HIS   F C   
17529 O  O   . HIS   F 23  ? 1.6313 1.1296 1.0391 0.2044  0.0376  0.0310  888  HIS   F O   
17530 C  CB  . HIS   F 23  ? 1.5733 1.0204 0.9173 0.2357  0.0287  0.0262  888  HIS   F CB  
17531 C  CG  . HIS   F 23  ? 1.5036 0.9724 0.8720 0.2256  0.0218  0.0221  888  HIS   F CG  
17532 N  ND1 . HIS   F 23  ? 1.5673 1.0545 0.9492 0.2264  0.0073  0.0147  888  HIS   F ND1 
17533 C  CD2 . HIS   F 23  ? 1.4853 0.9601 0.8671 0.2147  0.0273  0.0243  888  HIS   F CD2 
17534 C  CE1 . HIS   F 23  ? 1.5503 1.0535 0.9520 0.2167  0.0046  0.0127  888  HIS   F CE1 
17535 N  NE2 . HIS   F 23  ? 1.5224 1.0182 0.9240 0.2096  0.0163  0.0183  888  HIS   F NE2 
17536 N  N   . ALA   F 24  ? 1.5962 1.0543 0.9687 0.2124  0.0582  0.0413  889  ALA   F N   
17537 C  CA  . ALA   F 24  ? 1.5617 1.0317 0.9564 0.1978  0.0688  0.0465  889  ALA   F CA  
17538 C  C   . ALA   F 24  ? 1.6692 1.1647 1.0894 0.1897  0.0652  0.0453  889  ALA   F C   
17539 O  O   . ALA   F 24  ? 1.7510 1.2680 1.1971 0.1777  0.0625  0.0438  889  ALA   F O   
17540 C  CB  . ALA   F 24  ? 1.6205 1.0689 0.9998 0.1996  0.0854  0.0548  889  ALA   F CB  
17541 N  N   . ARG   F 25  ? 1.6784 1.1715 1.0910 0.1966  0.0648  0.0457  890  ARG   F N   
17542 C  CA  . ARG   F 25  ? 1.6323 1.1480 1.0677 0.1894  0.0624  0.0450  890  ARG   F CA  
17543 C  C   . ARG   F 25  ? 1.6615 1.2009 1.1170 0.1847  0.0478  0.0377  890  ARG   F C   
17544 O  O   . ARG   F 25  ? 1.7598 1.3216 1.2415 0.1732  0.0470  0.0375  890  ARG   F O   
17545 C  CB  . ARG   F 25  ? 1.8107 1.3171 1.2305 0.1997  0.0627  0.0458  890  ARG   F CB  
17546 N  N   . SER   F 26  ? 1.6874 1.2222 1.1311 0.1938  0.0361  0.0316  891  SER   F N   
17547 C  CA  . SER   F 26  ? 1.7153 1.2712 1.1776 0.1897  0.0227  0.0246  891  SER   F CA  
17548 C  C   . SER   F 26  ? 1.7141 1.2874 1.2011 0.1751  0.0253  0.0254  891  SER   F C   
17549 O  O   . SER   F 26  ? 1.7014 1.2974 1.2109 0.1678  0.0178  0.0217  891  SER   F O   
17550 C  CB  . SER   F 26  ? 1.7049 1.2491 1.1492 0.2011  0.0125  0.0190  891  SER   F CB  
17551 O  OG  . SER   F 26  ? 1.6947 1.2540 1.1550 0.1954  0.0044  0.0142  891  SER   F OG  
17552 N  N   . HIS   F 27  ? 1.6444 1.2065 1.1271 0.1708  0.0354  0.0301  892  HIS   F N   
17553 C  CA  . HIS   F 27  ? 1.6455 1.2216 1.1497 0.1575  0.0376  0.0308  892  HIS   F CA  
17554 C  C   . HIS   F 27  ? 1.7719 1.3606 1.2961 0.1458  0.0464  0.0357  892  HIS   F C   
17555 O  O   . HIS   F 27  ? 1.8876 1.4967 1.4357 0.1349  0.0435  0.0342  892  HIS   F O   
17556 C  CB  . HIS   F 27  ? 1.5921 1.1506 1.0835 0.1578  0.0441  0.0334  892  HIS   F CB  
17557 C  CG  . HIS   F 27  ? 1.5033 1.0567 0.9843 0.1646  0.0343  0.0278  892  HIS   F CG  
17558 N  ND1 . HIS   F 27  ? 1.5069 1.0793 1.0042 0.1611  0.0229  0.0217  892  HIS   F ND1 
17559 C  CD2 . HIS   F 27  ? 1.4198 0.9511 0.8760 0.1750  0.0344  0.0274  892  HIS   F CD2 
17560 C  CE1 . HIS   F 27  ? 1.4217 0.9845 0.9053 0.1690  0.0164  0.0177  892  HIS   F CE1 
17561 N  NE2 . HIS   F 27  ? 1.3760 0.9139 0.8345 0.1775  0.0228  0.0210  892  HIS   F NE2 
17562 N  N   . LEU   F 28  ? 1.7571 1.3337 1.2719 0.1482  0.0571  0.0416  893  LEU   F N   
17563 C  CA  . LEU   F 28  ? 1.8159 1.4032 1.3494 0.1375  0.0663  0.0466  893  LEU   F CA  
17564 C  C   . LEU   F 28  ? 1.9541 1.5633 1.5057 0.1342  0.0593  0.0437  893  LEU   F C   
17565 O  O   . LEU   F 28  ? 2.0337 1.6638 1.6079 0.1247  0.0537  0.0409  893  LEU   F O   
17566 C  CB  . LEU   F 28  ? 1.8321 1.3996 1.3499 0.1418  0.0803  0.0538  893  LEU   F CB  
17567 C  CG  . LEU   F 28  ? 1.8772 1.4190 1.3729 0.1470  0.0889  0.0575  893  LEU   F CG  
17568 C  CD1 . LEU   F 28  ? 1.8189 1.3428 1.3002 0.1517  0.1028  0.0646  893  LEU   F CD1 
17569 C  CD2 . LEU   F 28  ? 1.8583 1.4029 1.3665 0.1363  0.0927  0.0588  893  LEU   F CD2 
17570 N  N   . ARG   F 29  ? 1.9677 1.5715 1.5084 0.1424  0.0596  0.0444  894  ARG   F N   
17571 C  CA  . ARG   F 29  ? 1.9733 1.5958 1.5296 0.1397  0.0543  0.0424  894  ARG   F CA  
17572 C  C   . ARG   F 29  ? 1.9470 1.5904 1.5204 0.1355  0.0407  0.0355  894  ARG   F C   
17573 O  O   . ARG   F 29  ? 1.9420 1.5818 1.5064 0.1417  0.0317  0.0305  894  ARG   F O   
17574 C  CB  . ARG   F 29  ? 1.9949 1.6053 1.5315 0.1522  0.0531  0.0422  894  ARG   F CB  
17575 ZN ZN  . ZN    G .   ? 1.3914 1.1501 0.9731 0.0515  -0.0707 0.0570  501  ZN    A ZN  
17576 S  S   . SO4   H .   ? 1.3931 1.4975 1.3995 -0.0219 -0.1181 0.0346  502  SO4   A S   
17577 O  O1  . SO4   H .   ? 1.2210 1.3216 1.2282 -0.0259 -0.1122 0.0345  502  SO4   A O1  
17578 O  O2  . SO4   H .   ? 1.2886 1.4008 1.2999 -0.0228 -0.1215 0.0333  502  SO4   A O2  
17579 O  O3  . SO4   H .   ? 1.2943 1.4041 1.3075 -0.0198 -0.1195 0.0347  502  SO4   A O3  
17580 O  O4  . SO4   H .   ? 1.3586 1.4521 1.3516 -0.0188 -0.1193 0.0359  502  SO4   A O4  
17581 C  C1  . A1A5H I .   ? 1.4603 1.2743 1.0819 0.0253  -0.1092 0.0145  503  A1A5H A C1  
17582 C  C2  . A1A5H I .   ? 1.4894 1.3011 1.1063 0.0268  -0.1234 0.0099  503  A1A5H A C2  
17583 C  C3  . A1A5H I .   ? 1.4395 1.2664 1.0744 0.0231  -0.1350 0.0072  503  A1A5H A C3  
17584 C  C11 . A1A5H I .   ? 1.5496 1.3486 1.1512 0.0287  -0.1185 0.0082  503  A1A5H A C11 
17585 C  C13 . A1A5H I .   ? 1.6732 1.4485 1.2453 0.0359  -0.1128 0.0092  503  A1A5H A C13 
17586 C  C14 . A1A5H I .   ? 1.5694 1.3289 1.1202 0.0420  -0.1267 0.0052  503  A1A5H A C14 
17587 C  C15 . A1A5H I .   ? 1.6179 1.3901 1.1844 0.0373  -0.1393 0.0003  503  A1A5H A C15 
17588 C  C17 . A1A5H I .   ? 1.5459 1.3551 1.1599 0.0247  -0.1288 0.0037  503  A1A5H A C17 
17589 C  C18 . A1A5H I .   ? 1.6672 1.4315 1.2274 0.0391  -0.0968 0.0141  503  A1A5H A C18 
17590 C  C19 . A1A5H I .   ? 1.7358 1.5107 1.3090 0.0345  -0.1005 0.0109  503  A1A5H A C19 
17591 C  C20 . A1A5H I .   ? 1.6673 1.4752 1.2793 0.0253  -0.1540 -0.0045 503  A1A5H A C20 
17592 C  C21 . A1A5H I .   ? 1.6837 1.4864 1.2900 0.0251  -0.1528 -0.0063 503  A1A5H A C21 
17593 C  C22 . A1A5H I .   ? 1.3243 1.2143 1.0388 0.0061  -0.1367 0.0104  503  A1A5H A C22 
17594 C  C23 . A1A5H I .   ? 1.2829 1.1697 0.9919 0.0097  -0.1490 0.0084  503  A1A5H A C23 
17595 C  C24 . A1A5H I .   ? 1.2930 1.1996 1.0267 0.0049  -0.1532 0.0081  503  A1A5H A C24 
17596 C  C25 . A1A5H I .   ? 1.3362 1.2600 1.0921 -0.0016 -0.1553 0.0060  503  A1A5H A C25 
17597 C  C27 . A1A5H I .   ? 1.3860 1.2948 1.1243 -0.0008 -0.1386 0.0084  503  A1A5H A C27 
17598 C  C4  . A1A5H I .   ? 1.3517 1.1955 1.0083 0.0181  -0.1321 0.0090  503  A1A5H A C4  
17599 C  C5  . A1A5H I .   ? 1.3198 1.1655 0.9805 0.0166  -0.1184 0.0133  503  A1A5H A C5  
17600 C  C6  . A1A5H I .   ? 1.3191 1.1501 0.9629 0.0201  -0.1069 0.0161  503  A1A5H A C6  
17601 C  C7  . A1A5H I .   ? 1.3472 1.2084 1.0249 0.0140  -0.1419 0.0070  503  A1A5H A C7  
17602 C  C9  . A1A5H I .   ? 1.3789 1.2431 1.0630 0.0115  -0.1190 0.0142  503  A1A5H A C9  
17603 N  N16 . A1A5H I .   ? 1.6336 1.4298 1.2303 0.0298  -0.1426 0.0000  503  A1A5H A N16 
17604 N  N26 . A1A5H I .   ? 1.3799 1.3033 1.1360 -0.0039 -0.1477 0.0064  503  A1A5H A N26 
17605 N  N8  . A1A5H I .   ? 1.3666 1.2389 1.0592 0.0103  -0.1324 0.0106  503  A1A5H A N8  
17606 O  O10 . A1A5H I .   ? 1.3626 1.2338 1.0572 0.0087  -0.1096 0.0173  503  A1A5H A O10 
17607 O  O12 . A1A5H I .   ? 1.4810 1.2768 1.0775 0.0315  -0.1269 0.0077  503  A1A5H A O12 
17608 O  O28 . A1A5H I .   ? 1.3438 1.2544 1.0853 -0.0033 -0.1318 0.0088  503  A1A5H A O28 
17609 O  O29 . A1A5H I .   ? 1.3081 1.2454 1.0808 -0.0045 -0.1633 0.0040  503  A1A5H A O29 
17637 ZN ZN  . ZN    J .   ? 1.4492 1.2248 1.0328 0.0396  -0.0760 0.0349  900  ZN    C ZN  
17638 ZN ZN  . ZN    K .   ? 1.5528 1.2376 1.1219 0.1866  -0.0619 -0.0179 501  ZN    D ZN  
17639 S  S   . SO4   L .   ? 1.6421 1.6543 1.5810 0.0305  -0.0832 -0.0485 502  SO4   D S   
17640 O  O1  . SO4   L .   ? 1.6222 1.6439 1.5723 0.0325  -0.0847 -0.0515 502  SO4   D O1  
17641 O  O2  . SO4   L .   ? 1.5813 1.5950 1.5217 0.0334  -0.0862 -0.0487 502  SO4   D O2  
17642 O  O3  . SO4   L .   ? 1.5226 1.5363 1.4624 0.0222  -0.0795 -0.0452 502  SO4   D O3  
17643 O  O4  . SO4   L .   ? 1.5343 1.5333 1.4590 0.0342  -0.0823 -0.0485 502  SO4   D O4  
17644 C  C1  . A1A5H M .   ? 1.7162 1.1491 1.0864 0.1921  0.0385  0.0243  503  A1A5H D C1  
17645 C  C2  . A1A5H M .   ? 1.7298 1.1486 1.0817 0.2017  0.0329  0.0209  503  A1A5H D C2  
17646 C  C3  . A1A5H M .   ? 1.7012 1.1342 1.0619 0.2035  0.0203  0.0138  503  A1A5H D C3  
17647 C  C11 . A1A5H M .   ? 1.8487 1.2266 1.1709 0.2025  0.0532  0.0309  503  A1A5H D C11 
17648 C  C13 . A1A5H M .   ? 1.9317 1.2859 1.2308 0.2102  0.0638  0.0369  503  A1A5H D C13 
17649 C  C14 . A1A5H M .   ? 1.7909 1.1213 1.0584 0.2267  0.0594  0.0346  503  A1A5H D C14 
17650 C  C15 . A1A5H M .   ? 1.7594 1.0783 1.0189 0.2264  0.0598  0.0340  503  A1A5H D C15 
17651 C  C17 . A1A5H M .   ? 1.7583 1.1227 1.0703 0.2032  0.0538  0.0303  503  A1A5H D C17 
17652 C  C18 . A1A5H M .   ? 1.9441 1.2894 1.2456 0.2016  0.0796  0.0450  503  A1A5H D C18 
17653 C  C19 . A1A5H M .   ? 1.8284 1.1889 1.1355 0.2067  0.0705  0.0410  503  A1A5H D C19 
17654 C  C20 . A1A5H M .   ? 1.8549 1.2079 1.1374 0.2280  0.0350  0.0208  503  A1A5H D C20 
17655 C  C21 . A1A5H M .   ? 1.8731 1.2120 1.1369 0.2385  0.0282  0.0167  503  A1A5H D C21 
17656 C  C22 . A1A5H M .   ? 1.5316 1.0613 0.9833 0.1794  -0.0095 -0.0023 503  A1A5H D C22 
17657 C  C23 . A1A5H M .   ? 1.5362 1.0712 0.9847 0.1904  -0.0219 -0.0088 503  A1A5H D C23 
17658 C  C24 . A1A5H M .   ? 1.5099 1.0698 0.9823 0.1848  -0.0307 -0.0141 503  A1A5H D C24 
17659 C  C25 . A1A5H M .   ? 1.5413 1.1023 1.0186 0.1791  -0.0297 -0.0147 503  A1A5H D C25 
17660 C  C27 . A1A5H M .   ? 1.5692 1.1017 1.0281 0.1725  -0.0091 -0.0032 503  A1A5H D C27 
17661 C  C4  . A1A5H M .   ? 1.6440 1.1050 1.0317 0.1954  0.0135  0.0104  503  A1A5H D C4  
17662 C  C5  . A1A5H M .   ? 1.5713 1.0456 0.9764 0.1857  0.0191  0.0138  503  A1A5H D C5  
17663 C  C6  . A1A5H M .   ? 1.5660 1.0266 0.9625 0.1842  0.0313  0.0206  503  A1A5H D C6  
17664 C  C7  . A1A5H M .   ? 1.6317 1.1119 1.0334 0.1962  0.0004  0.0030  503  A1A5H D C7  
17665 C  C9  . A1A5H M .   ? 1.5224 1.0248 0.9545 0.1777  0.0107  0.0093  503  A1A5H D C9  
17666 N  N16 . A1A5H M .   ? 1.7704 1.1123 1.0527 0.2188  0.0501  0.0284  503  A1A5H D N16 
17667 N  N26 . A1A5H M .   ? 1.5446 1.0919 1.0146 0.1734  -0.0192 -0.0093 503  A1A5H D N26 
17668 N  N8  . A1A5H M .   ? 1.5576 1.0629 0.9872 0.1840  0.0002  0.0032  503  A1A5H D N8  
17669 O  O10 . A1A5H M .   ? 1.4735 0.9935 0.9268 0.1672  0.0128  0.0107  503  A1A5H D O10 
17670 O  O12 . A1A5H M .   ? 1.7704 1.1610 1.0948 0.2102  0.0393  0.0240  503  A1A5H D O12 
17671 O  O28 . A1A5H M .   ? 1.6135 1.1360 1.0694 0.1662  0.0001  0.0015  503  A1A5H D O28 
17672 O  O29 . A1A5H M .   ? 1.4599 1.0325 0.9468 0.1796  -0.0375 -0.0197 503  A1A5H D O29 
17700 ZN ZN  . ZN    N .   ? 1.6433 1.1484 1.0637 0.1947  0.0219  0.0202  900  ZN    F ZN  
17701 O  O   . HOH   O .   ? 1.1351 1.2521 1.1354 -0.0307 -0.1815 0.0103  601  HOH   A O   
17702 O  O   . HOH   O .   ? 0.9107 0.9320 0.8147 -0.0199 -0.1029 0.0377  602  HOH   A O   
17703 O  O   . HOH   O .   ? 0.8610 0.9102 0.9523 -0.0762 -0.0235 0.0361  603  HOH   A O   
17704 O  O   . HOH   O .   ? 0.9564 1.0298 0.9631 -0.0355 -0.0902 0.0366  604  HOH   A O   
17705 O  O   . HOH   O .   ? 1.0948 1.1024 0.9615 -0.0345 -0.1568 -0.0016 605  HOH   A O   
17706 O  O   . HOH   O .   ? 0.9465 1.0936 1.0433 -0.0716 -0.0570 0.0087  606  HOH   A O   
17707 O  O   . HOH   P .   ? 1.0183 1.0904 1.4160 -0.1045 -0.1508 -0.0547 1201 HOH   B O   
17708 O  O   . HOH   P .   ? 0.9438 0.8813 0.9387 0.0560  -0.2296 -0.0563 1202 HOH   B O   
17709 O  O   . HOH   P .   ? 0.9910 1.0527 1.1150 -0.0240 -0.1581 -0.0248 1203 HOH   B O   
17710 O  O   . HOH   P .   ? 0.9322 0.9620 1.2063 -0.0286 -0.2623 -0.1003 1204 HOH   B O   
17711 O  O   . HOH   P .   ? 0.9238 0.9910 0.8985 0.0075  -0.1251 0.0429  1205 HOH   B O   
17712 O  O   . HOH   P .   ? 1.2556 1.2524 1.1680 0.1159  -0.1358 0.0424  1206 HOH   B O   
17713 O  O   . HOH   P .   ? 0.9694 1.0985 1.2049 -0.0137 -0.2053 -0.0790 1207 HOH   B O   
17714 O  O   . HOH   P .   ? 0.8760 0.9697 0.8886 -0.0055 -0.1178 0.0374  1208 HOH   B O   
17715 O  O   . HOH   P .   ? 1.2550 1.1926 1.1375 0.1194  -0.1918 -0.0423 1209 HOH   B O   
17716 O  O   . HOH   P .   ? 1.1647 1.2257 1.1366 0.0861  -0.1114 0.0248  1210 HOH   B O   
17717 O  O   . HOH   P .   ? 1.4255 1.1982 1.1719 0.1927  -0.2761 -0.0843 1211 HOH   B O   
17718 O  O   . HOH   P .   ? 1.0902 0.9336 0.8769 0.0334  -0.0836 0.0735  1212 HOH   B O   
17719 O  O   . HOH   P .   ? 0.8429 0.8879 0.8986 0.0256  -0.1833 -0.0391 1213 HOH   B O   
17720 O  O   . HOH   P .   ? 1.2279 1.2369 1.1358 0.0938  -0.1050 -0.0048 1214 HOH   B O   
17721 O  O   . HOH   P .   ? 1.2844 1.0864 1.1261 0.0441  -0.1199 0.0496  1215 HOH   B O   
17722 O  O   . HOH   P .   ? 1.0459 1.0141 1.0039 0.0619  -0.1697 -0.0096 1216 HOH   B O   
17723 O  O   . HOH   Q .   ? 1.6306 1.1903 0.9279 0.1250  -0.1341 0.0232  1001 HOH   C O   
17724 O  O   . HOH   R .   ? 1.3628 1.1773 1.1262 0.0301  -0.0436 -0.0247 601  HOH   D O   
17725 O  O   . HOH   R .   ? 1.4246 1.1451 1.1563 0.0111  0.0268  0.0220  602  HOH   D O   
17726 O  O   . HOH   R .   ? 1.5564 1.4086 1.3296 0.0128  -0.0587 -0.0537 603  HOH   D O   
17727 O  O   . HOH   R .   ? 1.0903 0.9881 0.9058 0.0720  -0.0773 -0.0362 604  HOH   D O   
17728 O  O   . HOH   R .   ? 1.4029 0.9787 0.8403 0.2922  -0.1437 -0.0646 605  HOH   D O   
17729 O  O   . HOH   R .   ? 1.2456 0.8923 0.8459 0.1014  0.0255  0.0218  606  HOH   D O   
17730 O  O   . HOH   R .   ? 1.3578 1.3333 1.2592 -0.0691 -0.0960 -0.0344 607  HOH   D O   
17731 O  O   . HOH   S .   ? 1.3882 1.2203 1.0500 -0.0011 -0.0856 -0.0205 1201 HOH   E O   
17732 O  O   . HOH   S .   ? 1.0642 0.9993 0.8661 -0.0414 -0.1040 -0.0262 1202 HOH   E O   
17733 O  O   . HOH   S .   ? 0.9184 0.9368 0.8276 -0.0360 -0.0251 -0.0128 1203 HOH   E O   
17734 O  O   . HOH   S .   ? 1.5094 1.2202 1.1022 -0.0194 -0.2012 -0.0770 1204 HOH   E O   
17735 O  O   . HOH   S .   ? 1.0396 1.0765 0.9986 0.0057  0.0105  -0.0318 1205 HOH   E O   
17736 O  O   . HOH   S .   ? 1.3506 1.0168 0.9211 -0.0152 -0.3193 -0.1043 1206 HOH   E O   
17737 O  O   . HOH   S .   ? 0.8242 0.9386 0.9047 0.0316  -0.1455 -0.0637 1207 HOH   E O   
17738 O  O   . HOH   S .   ? 1.1873 1.0570 0.9298 -0.0251 -0.0868 -0.0418 1208 HOH   E O   
17739 O  O   . HOH   S .   ? 1.5357 1.2841 1.1397 -0.0074 -0.2357 -0.0669 1209 HOH   E O   
17740 O  O   . HOH   S .   ? 1.0201 1.0301 1.0050 -0.1070 -0.2042 -0.0442 1210 HOH   E O   
17741 O  O   . HOH   S .   ? 1.0875 1.2227 1.1815 -0.0094 -0.0520 -0.0452 1211 HOH   E O   
17742 O  O   . HOH   T .   ? 1.6054 0.9640 0.8174 0.3278  -0.0451 -0.0112 1001 HOH   F O   
# 
