data_9MUM
# 
_entry.id   9MUM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9MUM         pdb_00009mum 10.2210/pdb9mum/pdb 
WWPDB D_1000291880 ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-03-12 ? 
# 
_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                        9MUM 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-14 
_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_contact_author.id                 2 
_pdbx_contact_author.email              pshaffe4@its.jnj.com 
_pdbx_contact_author.name_first         Paul 
_pdbx_contact_author.name_last          Shaffer 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2249-8068 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Shaffer, P.L.' 1 0000-0003-2249-8068 
'Duda, D.M.'    2 ?                   
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                4672 
_citation.page_last                 4693 
_citation.title                     
'Design, Synthesis, and Characterization of GluN2A Negative Allosteric Modulators Suitable for In Vivo Exploration.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02751 
_citation.pdbx_database_id_PubMed   39960408 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Bischoff, F.P.'       1  ? 
primary 'Van Brandt, S.'       2  ? 
primary 'Viellevoye, M.'       3  ? 
primary 'De Cleyn, M.'         4  ? 
primary 'Surkyn, M.'           5  ? 
primary 'Carbajo, R.J.'        6  ? 
primary 'Dominguez Blanco, M.' 7  ? 
primary 'Wroblowski, B.'       8  ? 
primary 'Karpowich, N.K.'      9  ? 
primary 'Steele, R.A.'         10 ? 
primary 'Schalk-Hihi, C.'      11 ? 
primary 'Miller, R.'           12 ? 
primary 'Duda, D.'             13 ? 
primary 'Shaffer, P.'          14 ? 
primary 'Ballentine, S.'       15 ? 
primary 'Simavorian, S.'       16 ? 
primary 'Lord, B.'             17 ? 
primary 'Neff, R.A.'           18 ? 
primary 'Bonaventure, P.'      19 ? 
primary 'Gijsen, H.J.M.'       20 ? 
# 
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 'Glutamate receptor ionotropic, NMDA 1'                                                           35163.988 1   
? ? ? ? 
2 polymer     man 'Glutamate receptor ionotropic, NMDA 2A'                                                          33551.281 1   
? ? ? ? 
3 non-polymer syn GLYCINE                                                                                           75.067    1   
? ? ? ? 
4 non-polymer nat 'GLUTAMIC ACID'                                                                                   147.129   1   
? ? ? ? 
5 non-polymer syn '5-[2-(3-chlorophenyl)-2,2-difluoroethoxy]-N-[1-(pyrazin-2-yl)cyclopropyl]pyrazine-2-carboxamide' 431.823   1   
? ? ? ? 
6 water       nat water                                                                                             18.015    244 
? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'GluN1,Glutamate [NMDA] receptor subunit zeta-1,N-methyl-D-aspartate receptor subunit NR1,NMD-R1,hNR1'           
2 'GluN2A,Glutamate [NMDA] receptor subunit epsilon-1,N-methyl D-aspartate receptor subtype 2A,NMDAR2A,NR2A,hNR2A' 
# 
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 
;MHHHHHHENLYFQGSMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHTVPQCCYGF
CIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGL
TILVKKGTRITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSA
VLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDS
;
;MHHHHHHENLYFQGSMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHTVPQCCYGF
CIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGL
TILVKKGTRITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSA
VLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDS
;
A ? 
2 'polypeptide(L)' no no 
;MHHHHHHENLYFQGPDDNHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNSTNEGMNVKKCCKGFCIDILKK
LSRTVKFTYDLYLVTNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRGTQVTGL
SDKKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPYMHQYMTKFNQKGVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGC
KLVTIGSGYIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGICHN
;
;MHHHHHHENLYFQGPDDNHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNSTNEGMNVKKCCKGFCIDILKK
LSRTVKFTYDLYLVTNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRGTQVTGL
SDKKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPYMHQYMTKFNQKGVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGC
KLVTIGSGYIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGICHN
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 GLYCINE                                                                                           GLY   
4 'GLUTAMIC ACID'                                                                                   GLU   
5 '5-[2-(3-chlorophenyl)-2,2-difluoroethoxy]-N-[1-(pyrazin-2-yl)cyclopropyl]pyrazine-2-carboxamide' A1BRB 
6 water                                                                                             HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   GLU n 
1 9   ASN n 
1 10  LEU n 
1 11  TYR n 
1 12  PHE n 
1 13  GLN n 
1 14  GLY n 
1 15  SER n 
1 16  MET n 
1 17  SER n 
1 18  THR n 
1 19  ARG n 
1 20  LEU n 
1 21  LYS n 
1 22  ILE n 
1 23  VAL n 
1 24  THR n 
1 25  ILE n 
1 26  HIS n 
1 27  GLN n 
1 28  GLU n 
1 29  PRO n 
1 30  PHE n 
1 31  VAL n 
1 32  TYR n 
1 33  VAL n 
1 34  LYS n 
1 35  PRO n 
1 36  THR n 
1 37  LEU n 
1 38  SER n 
1 39  ASP n 
1 40  GLY n 
1 41  THR n 
1 42  CYS n 
1 43  LYS n 
1 44  GLU n 
1 45  GLU n 
1 46  PHE n 
1 47  THR n 
1 48  VAL n 
1 49  ASN n 
1 50  GLY n 
1 51  ASP n 
1 52  PRO n 
1 53  VAL n 
1 54  LYS n 
1 55  LYS n 
1 56  VAL n 
1 57  ILE n 
1 58  CYS n 
1 59  THR n 
1 60  GLY n 
1 61  PRO n 
1 62  ASN n 
1 63  ASP n 
1 64  THR n 
1 65  SER n 
1 66  PRO n 
1 67  GLY n 
1 68  SER n 
1 69  PRO n 
1 70  ARG n 
1 71  HIS n 
1 72  THR n 
1 73  VAL n 
1 74  PRO n 
1 75  GLN n 
1 76  CYS n 
1 77  CYS n 
1 78  TYR n 
1 79  GLY n 
1 80  PHE n 
1 81  CYS n 
1 82  ILE n 
1 83  ASP n 
1 84  LEU n 
1 85  LEU n 
1 86  ILE n 
1 87  LYS n 
1 88  LEU n 
1 89  ALA n 
1 90  ARG n 
1 91  THR n 
1 92  MET n 
1 93  ASN n 
1 94  PHE n 
1 95  THR n 
1 96  TYR n 
1 97  GLU n 
1 98  VAL n 
1 99  HIS n 
1 100 LEU n 
1 101 VAL n 
1 102 ALA n 
1 103 ASP n 
1 104 GLY n 
1 105 LYS n 
1 106 PHE n 
1 107 GLY n 
1 108 THR n 
1 109 GLN n 
1 110 GLU n 
1 111 ARG n 
1 112 VAL n 
1 113 ASN n 
1 114 ASN n 
1 115 SER n 
1 116 ASN n 
1 117 LYS n 
1 118 LYS n 
1 119 GLU n 
1 120 TRP n 
1 121 ASN n 
1 122 GLY n 
1 123 MET n 
1 124 MET n 
1 125 GLY n 
1 126 GLU n 
1 127 LEU n 
1 128 LEU n 
1 129 SER n 
1 130 GLY n 
1 131 GLN n 
1 132 ALA n 
1 133 ASP n 
1 134 MET n 
1 135 ILE n 
1 136 VAL n 
1 137 ALA n 
1 138 PRO n 
1 139 LEU n 
1 140 THR n 
1 141 ILE n 
1 142 ASN n 
1 143 ASN n 
1 144 GLU n 
1 145 ARG n 
1 146 ALA n 
1 147 GLN n 
1 148 TYR n 
1 149 ILE n 
1 150 GLU n 
1 151 PHE n 
1 152 SER n 
1 153 LYS n 
1 154 PRO n 
1 155 PHE n 
1 156 LYS n 
1 157 TYR n 
1 158 GLN n 
1 159 GLY n 
1 160 LEU n 
1 161 THR n 
1 162 ILE n 
1 163 LEU n 
1 164 VAL n 
1 165 LYS n 
1 166 LYS n 
1 167 GLY n 
1 168 THR n 
1 169 ARG n 
1 170 ILE n 
1 171 THR n 
1 172 GLY n 
1 173 ILE n 
1 174 ASN n 
1 175 ASP n 
1 176 PRO n 
1 177 ARG n 
1 178 LEU n 
1 179 ARG n 
1 180 ASN n 
1 181 PRO n 
1 182 SER n 
1 183 ASP n 
1 184 LYS n 
1 185 PHE n 
1 186 ILE n 
1 187 TYR n 
1 188 ALA n 
1 189 THR n 
1 190 VAL n 
1 191 LYS n 
1 192 GLN n 
1 193 SER n 
1 194 SER n 
1 195 VAL n 
1 196 ASP n 
1 197 ILE n 
1 198 TYR n 
1 199 PHE n 
1 200 ARG n 
1 201 ARG n 
1 202 GLN n 
1 203 VAL n 
1 204 GLU n 
1 205 LEU n 
1 206 SER n 
1 207 THR n 
1 208 MET n 
1 209 TYR n 
1 210 ARG n 
1 211 HIS n 
1 212 MET n 
1 213 GLU n 
1 214 LYS n 
1 215 HIS n 
1 216 ASN n 
1 217 TYR n 
1 218 GLU n 
1 219 SER n 
1 220 ALA n 
1 221 ALA n 
1 222 GLU n 
1 223 ALA n 
1 224 ILE n 
1 225 GLN n 
1 226 ALA n 
1 227 VAL n 
1 228 ARG n 
1 229 ASP n 
1 230 ASN n 
1 231 LYS n 
1 232 LEU n 
1 233 HIS n 
1 234 ALA n 
1 235 PHE n 
1 236 ILE n 
1 237 TRP n 
1 238 ASP n 
1 239 SER n 
1 240 ALA n 
1 241 VAL n 
1 242 LEU n 
1 243 GLU n 
1 244 PHE n 
1 245 GLU n 
1 246 ALA n 
1 247 SER n 
1 248 GLN n 
1 249 LYS n 
1 250 CYS n 
1 251 ASP n 
1 252 LEU n 
1 253 VAL n 
1 254 THR n 
1 255 THR n 
1 256 GLY n 
1 257 GLU n 
1 258 LEU n 
1 259 PHE n 
1 260 PHE n 
1 261 ARG n 
1 262 SER n 
1 263 GLY n 
1 264 PHE n 
1 265 GLY n 
1 266 ILE n 
1 267 GLY n 
1 268 MET n 
1 269 ARG n 
1 270 LYS n 
1 271 ASP n 
1 272 SER n 
1 273 PRO n 
1 274 TRP n 
1 275 LYS n 
1 276 GLN n 
1 277 ASN n 
1 278 VAL n 
1 279 SER n 
1 280 LEU n 
1 281 SER n 
1 282 ILE n 
1 283 LEU n 
1 284 LYS n 
1 285 SER n 
1 286 HIS n 
1 287 GLU n 
1 288 ASN n 
1 289 GLY n 
1 290 PHE n 
1 291 MET n 
1 292 GLU n 
1 293 ASP n 
1 294 LEU n 
1 295 ASP n 
1 296 LYS n 
1 297 THR n 
1 298 TRP n 
1 299 VAL n 
1 300 ARG n 
1 301 TYR n 
1 302 GLN n 
1 303 GLU n 
1 304 CYS n 
1 305 ASP n 
1 306 SER n 
2 1   MET n 
2 2   HIS n 
2 3   HIS n 
2 4   HIS n 
2 5   HIS n 
2 6   HIS n 
2 7   HIS n 
2 8   GLU n 
2 9   ASN n 
2 10  LEU n 
2 11  TYR n 
2 12  PHE n 
2 13  GLN n 
2 14  GLY n 
2 15  PRO n 
2 16  ASP n 
2 17  ASP n 
2 18  ASN n 
2 19  HIS n 
2 20  LEU n 
2 21  SER n 
2 22  ILE n 
2 23  VAL n 
2 24  THR n 
2 25  LEU n 
2 26  GLU n 
2 27  GLU n 
2 28  ALA n 
2 29  PRO n 
2 30  PHE n 
2 31  VAL n 
2 32  ILE n 
2 33  VAL n 
2 34  GLU n 
2 35  ASP n 
2 36  ILE n 
2 37  ASP n 
2 38  PRO n 
2 39  LEU n 
2 40  THR n 
2 41  GLU n 
2 42  THR n 
2 43  CYS n 
2 44  VAL n 
2 45  ARG n 
2 46  ASN n 
2 47  THR n 
2 48  VAL n 
2 49  PRO n 
2 50  CYS n 
2 51  ARG n 
2 52  LYS n 
2 53  PHE n 
2 54  VAL n 
2 55  LYS n 
2 56  ILE n 
2 57  ASN n 
2 58  ASN n 
2 59  SER n 
2 60  THR n 
2 61  ASN n 
2 62  GLU n 
2 63  GLY n 
2 64  MET n 
2 65  ASN n 
2 66  VAL n 
2 67  LYS n 
2 68  LYS n 
2 69  CYS n 
2 70  CYS n 
2 71  LYS n 
2 72  GLY n 
2 73  PHE n 
2 74  CYS n 
2 75  ILE n 
2 76  ASP n 
2 77  ILE n 
2 78  LEU n 
2 79  LYS n 
2 80  LYS n 
2 81  LEU n 
2 82  SER n 
2 83  ARG n 
2 84  THR n 
2 85  VAL n 
2 86  LYS n 
2 87  PHE n 
2 88  THR n 
2 89  TYR n 
2 90  ASP n 
2 91  LEU n 
2 92  TYR n 
2 93  LEU n 
2 94  VAL n 
2 95  THR n 
2 96  ASN n 
2 97  GLY n 
2 98  LYS n 
2 99  HIS n 
2 100 GLY n 
2 101 LYS n 
2 102 LYS n 
2 103 VAL n 
2 104 ASN n 
2 105 ASN n 
2 106 VAL n 
2 107 TRP n 
2 108 ASN n 
2 109 GLY n 
2 110 MET n 
2 111 ILE n 
2 112 GLY n 
2 113 GLU n 
2 114 VAL n 
2 115 VAL n 
2 116 TYR n 
2 117 GLN n 
2 118 ARG n 
2 119 ALA n 
2 120 VAL n 
2 121 MET n 
2 122 ALA n 
2 123 VAL n 
2 124 GLY n 
2 125 SER n 
2 126 LEU n 
2 127 THR n 
2 128 ILE n 
2 129 ASN n 
2 130 GLU n 
2 131 GLU n 
2 132 ARG n 
2 133 SER n 
2 134 GLU n 
2 135 VAL n 
2 136 VAL n 
2 137 ASP n 
2 138 PHE n 
2 139 SER n 
2 140 VAL n 
2 141 PRO n 
2 142 PHE n 
2 143 VAL n 
2 144 GLU n 
2 145 THR n 
2 146 GLY n 
2 147 ILE n 
2 148 SER n 
2 149 VAL n 
2 150 MET n 
2 151 VAL n 
2 152 SER n 
2 153 ARG n 
2 154 GLY n 
2 155 THR n 
2 156 GLN n 
2 157 VAL n 
2 158 THR n 
2 159 GLY n 
2 160 LEU n 
2 161 SER n 
2 162 ASP n 
2 163 LYS n 
2 164 LYS n 
2 165 PHE n 
2 166 GLN n 
2 167 ARG n 
2 168 PRO n 
2 169 HIS n 
2 170 ASP n 
2 171 TYR n 
2 172 SER n 
2 173 PRO n 
2 174 PRO n 
2 175 PHE n 
2 176 ARG n 
2 177 PHE n 
2 178 GLY n 
2 179 THR n 
2 180 VAL n 
2 181 PRO n 
2 182 ASN n 
2 183 GLY n 
2 184 SER n 
2 185 THR n 
2 186 GLU n 
2 187 ARG n 
2 188 ASN n 
2 189 ILE n 
2 190 ARG n 
2 191 ASN n 
2 192 ASN n 
2 193 TYR n 
2 194 PRO n 
2 195 TYR n 
2 196 MET n 
2 197 HIS n 
2 198 GLN n 
2 199 TYR n 
2 200 MET n 
2 201 THR n 
2 202 LYS n 
2 203 PHE n 
2 204 ASN n 
2 205 GLN n 
2 206 LYS n 
2 207 GLY n 
2 208 VAL n 
2 209 GLU n 
2 210 ASP n 
2 211 ALA n 
2 212 LEU n 
2 213 VAL n 
2 214 SER n 
2 215 LEU n 
2 216 LYS n 
2 217 THR n 
2 218 GLY n 
2 219 LYS n 
2 220 LEU n 
2 221 ASP n 
2 222 ALA n 
2 223 PHE n 
2 224 ILE n 
2 225 TYR n 
2 226 ASP n 
2 227 ALA n 
2 228 ALA n 
2 229 VAL n 
2 230 LEU n 
2 231 ASN n 
2 232 TYR n 
2 233 LYS n 
2 234 ALA n 
2 235 GLY n 
2 236 ARG n 
2 237 ASP n 
2 238 GLU n 
2 239 GLY n 
2 240 CYS n 
2 241 LYS n 
2 242 LEU n 
2 243 VAL n 
2 244 THR n 
2 245 ILE n 
2 246 GLY n 
2 247 SER n 
2 248 GLY n 
2 249 TYR n 
2 250 ILE n 
2 251 PHE n 
2 252 ALA n 
2 253 THR n 
2 254 THR n 
2 255 GLY n 
2 256 TYR n 
2 257 GLY n 
2 258 ILE n 
2 259 ALA n 
2 260 LEU n 
2 261 GLN n 
2 262 LYS n 
2 263 GLY n 
2 264 SER n 
2 265 PRO n 
2 266 TRP n 
2 267 LYS n 
2 268 ARG n 
2 269 GLN n 
2 270 ILE n 
2 271 ASP n 
2 272 LEU n 
2 273 ALA n 
2 274 LEU n 
2 275 LEU n 
2 276 GLN n 
2 277 PHE n 
2 278 VAL n 
2 279 GLY n 
2 280 ASP n 
2 281 GLY n 
2 282 GLU n 
2 283 MET n 
2 284 GLU n 
2 285 GLU n 
2 286 LEU n 
2 287 GLU n 
2 288 THR n 
2 289 LEU n 
2 290 TRP n 
2 291 LEU n 
2 292 THR n 
2 293 GLY n 
2 294 ILE n 
2 295 CYS n 
2 296 HIS n 
2 297 ASN 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   166 human ? 'GRIN1, NMDAR1'   ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? 'Origami2 (DE3)' ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 167 306 human ? 'GRIN1, NMDAR1'   ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? 'Origami2 (DE3)' ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1   155 human ? 'GRIN2A, NMDAR2A' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? 'Origami2 (DE3)' ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 2 sample 'Biological sequence' 156 297 human ? 'GRIN2A, NMDAR2A' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? 'Origami2 (DE3)' ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1BRB non-polymer         . '5-[2-(3-chlorophenyl)-2,2-difluoroethoxy]-N-[1-(pyrazin-2-yl)cyclopropyl]pyrazine-2-carboxamide' ? 
'C20 H16 Cl F2 N5 O2' 431.823 
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 
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 
# 
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   MET 1   379 ?   ?   ?   A . n 
A 1 2   HIS 2   380 ?   ?   ?   A . n 
A 1 3   HIS 3   381 ?   ?   ?   A . n 
A 1 4   HIS 4   382 ?   ?   ?   A . n 
A 1 5   HIS 5   383 ?   ?   ?   A . n 
A 1 6   HIS 6   384 ?   ?   ?   A . n 
A 1 7   HIS 7   385 ?   ?   ?   A . n 
A 1 8   GLU 8   386 ?   ?   ?   A . n 
A 1 9   ASN 9   387 ?   ?   ?   A . n 
A 1 10  LEU 10  388 ?   ?   ?   A . n 
A 1 11  TYR 11  389 ?   ?   ?   A . n 
A 1 12  PHE 12  390 ?   ?   ?   A . n 
A 1 13  GLN 13  391 ?   ?   ?   A . n 
A 1 14  GLY 14  392 ?   ?   ?   A . n 
A 1 15  SER 15  393 ?   ?   ?   A . n 
A 1 16  MET 16  394 ?   ?   ?   A . n 
A 1 17  SER 17  395 ?   ?   ?   A . n 
A 1 18  THR 18  396 ?   ?   ?   A . n 
A 1 19  ARG 19  397 397 ARG ARG A . n 
A 1 20  LEU 20  398 398 LEU LEU A . n 
A 1 21  LYS 21  399 399 LYS LYS A . n 
A 1 22  ILE 22  400 400 ILE ILE A . n 
A 1 23  VAL 23  401 401 VAL VAL A . n 
A 1 24  THR 24  402 402 THR THR A . n 
A 1 25  ILE 25  403 403 ILE ILE A . n 
A 1 26  HIS 26  404 404 HIS HIS A . n 
A 1 27  GLN 27  405 405 GLN GLN A . n 
A 1 28  GLU 28  406 406 GLU GLU A . n 
A 1 29  PRO 29  407 407 PRO PRO A . n 
A 1 30  PHE 30  408 408 PHE PHE A . n 
A 1 31  VAL 31  409 409 VAL VAL A . n 
A 1 32  TYR 32  410 410 TYR TYR A . n 
A 1 33  VAL 33  411 411 VAL VAL A . n 
A 1 34  LYS 34  412 412 LYS LYS A . n 
A 1 35  PRO 35  413 413 PRO PRO A . n 
A 1 36  THR 36  414 414 THR THR A . n 
A 1 37  LEU 37  415 415 LEU LEU A . n 
A 1 38  SER 38  416 416 SER SER A . n 
A 1 39  ASP 39  417 417 ASP ASP A . n 
A 1 40  GLY 40  418 418 GLY GLY A . n 
A 1 41  THR 41  419 419 THR THR A . n 
A 1 42  CYS 42  420 420 CYS CYS A . n 
A 1 43  LYS 43  421 421 LYS LYS A . n 
A 1 44  GLU 44  422 422 GLU GLU A . n 
A 1 45  GLU 45  423 423 GLU GLU A . n 
A 1 46  PHE 46  424 424 PHE PHE A . n 
A 1 47  THR 47  425 425 THR THR A . n 
A 1 48  VAL 48  426 426 VAL VAL A . n 
A 1 49  ASN 49  427 427 ASN ASN A . n 
A 1 50  GLY 50  428 428 GLY GLY A . n 
A 1 51  ASP 51  429 429 ASP ASP A . n 
A 1 52  PRO 52  430 430 PRO PRO A . n 
A 1 53  VAL 53  431 431 VAL VAL A . n 
A 1 54  LYS 54  432 432 LYS LYS A . n 
A 1 55  LYS 55  433 433 LYS LYS A . n 
A 1 56  VAL 56  434 434 VAL VAL A . n 
A 1 57  ILE 57  435 435 ILE ILE A . n 
A 1 58  CYS 58  436 436 CYS CYS A . n 
A 1 59  THR 59  437 437 THR THR A . n 
A 1 60  GLY 60  438 438 GLY GLY A . n 
A 1 61  PRO 61  439 439 PRO PRO A . n 
A 1 62  ASN 62  440 440 ASN ASN A . n 
A 1 63  ASP 63  441 ?   ?   ?   A . n 
A 1 64  THR 64  442 ?   ?   ?   A . n 
A 1 65  SER 65  443 ?   ?   ?   A . n 
A 1 66  PRO 66  444 ?   ?   ?   A . n 
A 1 67  GLY 67  445 ?   ?   ?   A . n 
A 1 68  SER 68  446 446 SER SER A . n 
A 1 69  PRO 69  447 447 PRO PRO A . n 
A 1 70  ARG 70  448 448 ARG ARG A . n 
A 1 71  HIS 71  449 449 HIS HIS A . n 
A 1 72  THR 72  450 450 THR THR A . n 
A 1 73  VAL 73  451 451 VAL VAL A . n 
A 1 74  PRO 74  452 452 PRO PRO A . n 
A 1 75  GLN 75  453 453 GLN GLN A . n 
A 1 76  CYS 76  454 454 CYS CYS A . n 
A 1 77  CYS 77  455 455 CYS CYS A . n 
A 1 78  TYR 78  456 456 TYR TYR A . n 
A 1 79  GLY 79  457 457 GLY GLY A . n 
A 1 80  PHE 80  458 458 PHE PHE A . n 
A 1 81  CYS 81  459 459 CYS CYS A . n 
A 1 82  ILE 82  460 460 ILE ILE A . n 
A 1 83  ASP 83  461 461 ASP ASP A . n 
A 1 84  LEU 84  462 462 LEU LEU A . n 
A 1 85  LEU 85  463 463 LEU LEU A . n 
A 1 86  ILE 86  464 464 ILE ILE A . n 
A 1 87  LYS 87  465 465 LYS LYS A . n 
A 1 88  LEU 88  466 466 LEU LEU A . n 
A 1 89  ALA 89  467 467 ALA ALA A . n 
A 1 90  ARG 90  468 468 ARG ARG A . n 
A 1 91  THR 91  469 469 THR THR A . n 
A 1 92  MET 92  470 470 MET MET A . n 
A 1 93  ASN 93  471 471 ASN ASN A . n 
A 1 94  PHE 94  472 472 PHE PHE A . n 
A 1 95  THR 95  473 473 THR THR A . n 
A 1 96  TYR 96  474 474 TYR TYR A . n 
A 1 97  GLU 97  475 475 GLU GLU A . n 
A 1 98  VAL 98  476 476 VAL VAL A . n 
A 1 99  HIS 99  477 477 HIS HIS A . n 
A 1 100 LEU 100 478 478 LEU LEU A . n 
A 1 101 VAL 101 479 479 VAL VAL A . n 
A 1 102 ALA 102 480 480 ALA ALA A . n 
A 1 103 ASP 103 481 481 ASP ASP A . n 
A 1 104 GLY 104 482 482 GLY GLY A . n 
A 1 105 LYS 105 483 483 LYS LYS A . n 
A 1 106 PHE 106 484 484 PHE PHE A . n 
A 1 107 GLY 107 485 485 GLY GLY A . n 
A 1 108 THR 108 486 486 THR THR A . n 
A 1 109 GLN 109 487 487 GLN GLN A . n 
A 1 110 GLU 110 488 488 GLU GLU A . n 
A 1 111 ARG 111 489 ?   ?   ?   A . n 
A 1 112 VAL 112 490 ?   ?   ?   A . n 
A 1 113 ASN 113 491 ?   ?   ?   A . n 
A 1 114 ASN 114 492 ?   ?   ?   A . n 
A 1 115 SER 115 493 ?   ?   ?   A . n 
A 1 116 ASN 116 494 494 ASN ASN A . n 
A 1 117 LYS 117 495 495 LYS LYS A . n 
A 1 118 LYS 118 496 496 LYS LYS A . n 
A 1 119 GLU 119 497 497 GLU GLU A . n 
A 1 120 TRP 120 498 498 TRP TRP A . n 
A 1 121 ASN 121 499 499 ASN ASN A . n 
A 1 122 GLY 122 500 500 GLY GLY A . n 
A 1 123 MET 123 501 501 MET MET A . n 
A 1 124 MET 124 502 502 MET MET A . n 
A 1 125 GLY 125 503 503 GLY GLY A . n 
A 1 126 GLU 126 504 504 GLU GLU A . n 
A 1 127 LEU 127 505 505 LEU LEU A . n 
A 1 128 LEU 128 506 506 LEU LEU A . n 
A 1 129 SER 129 507 507 SER SER A . n 
A 1 130 GLY 130 508 508 GLY GLY A . n 
A 1 131 GLN 131 509 509 GLN GLN A . n 
A 1 132 ALA 132 510 510 ALA ALA A . n 
A 1 133 ASP 133 511 511 ASP ASP A . n 
A 1 134 MET 134 512 512 MET MET A . n 
A 1 135 ILE 135 513 513 ILE ILE A . n 
A 1 136 VAL 136 514 514 VAL VAL A . n 
A 1 137 ALA 137 515 515 ALA ALA A . n 
A 1 138 PRO 138 516 516 PRO PRO A . n 
A 1 139 LEU 139 517 517 LEU LEU A . n 
A 1 140 THR 140 518 518 THR THR A . n 
A 1 141 ILE 141 519 519 ILE ILE A . n 
A 1 142 ASN 142 520 520 ASN ASN A . n 
A 1 143 ASN 143 521 521 ASN ASN A . n 
A 1 144 GLU 144 522 522 GLU GLU A . n 
A 1 145 ARG 145 523 523 ARG ARG A . n 
A 1 146 ALA 146 524 524 ALA ALA A . n 
A 1 147 GLN 147 525 525 GLN GLN A . n 
A 1 148 TYR 148 526 526 TYR TYR A . n 
A 1 149 ILE 149 527 527 ILE ILE A . n 
A 1 150 GLU 150 528 528 GLU GLU A . n 
A 1 151 PHE 151 529 529 PHE PHE A . n 
A 1 152 SER 152 530 530 SER SER A . n 
A 1 153 LYS 153 531 531 LYS LYS A . n 
A 1 154 PRO 154 532 532 PRO PRO A . n 
A 1 155 PHE 155 533 533 PHE PHE A . n 
A 1 156 LYS 156 534 534 LYS LYS A . n 
A 1 157 TYR 157 535 535 TYR TYR A . n 
A 1 158 GLN 158 536 536 GLN GLN A . n 
A 1 159 GLY 159 537 537 GLY GLY A . n 
A 1 160 LEU 160 538 538 LEU LEU A . n 
A 1 161 THR 161 539 539 THR THR A . n 
A 1 162 ILE 162 540 540 ILE ILE A . n 
A 1 163 LEU 163 541 541 LEU LEU A . n 
A 1 164 VAL 164 542 542 VAL VAL A . n 
A 1 165 LYS 165 543 543 LYS LYS A . n 
A 1 166 LYS 166 544 544 LYS LYS A . n 
A 1 167 GLY 167 545 545 GLY GLY A . n 
A 1 168 THR 168 546 546 THR THR A . n 
A 1 169 ARG 169 663 663 ARG ARG A . n 
A 1 170 ILE 170 664 664 ILE ILE A . n 
A 1 171 THR 171 665 665 THR THR A . n 
A 1 172 GLY 172 666 666 GLY GLY A . n 
A 1 173 ILE 173 667 667 ILE ILE A . n 
A 1 174 ASN 174 668 668 ASN ASN A . n 
A 1 175 ASP 175 669 669 ASP ASP A . n 
A 1 176 PRO 176 670 670 PRO PRO A . n 
A 1 177 ARG 177 671 671 ARG ARG A . n 
A 1 178 LEU 178 672 672 LEU LEU A . n 
A 1 179 ARG 179 673 673 ARG ARG A . n 
A 1 180 ASN 180 674 674 ASN ASN A . n 
A 1 181 PRO 181 675 675 PRO PRO A . n 
A 1 182 SER 182 676 676 SER SER A . n 
A 1 183 ASP 183 677 677 ASP ASP A . n 
A 1 184 LYS 184 678 678 LYS LYS A . n 
A 1 185 PHE 185 679 679 PHE PHE A . n 
A 1 186 ILE 186 680 680 ILE ILE A . n 
A 1 187 TYR 187 681 681 TYR TYR A . n 
A 1 188 ALA 188 682 682 ALA ALA A . n 
A 1 189 THR 189 683 683 THR THR A . n 
A 1 190 VAL 190 684 684 VAL VAL A . n 
A 1 191 LYS 191 685 685 LYS LYS A . n 
A 1 192 GLN 192 686 686 GLN GLN A . n 
A 1 193 SER 193 687 687 SER SER A . n 
A 1 194 SER 194 688 688 SER SER A . n 
A 1 195 VAL 195 689 689 VAL VAL A . n 
A 1 196 ASP 196 690 690 ASP ASP A . n 
A 1 197 ILE 197 691 691 ILE ILE A . n 
A 1 198 TYR 198 692 692 TYR TYR A . n 
A 1 199 PHE 199 693 693 PHE PHE A . n 
A 1 200 ARG 200 694 694 ARG ARG A . n 
A 1 201 ARG 201 695 695 ARG ARG A . n 
A 1 202 GLN 202 696 696 GLN GLN A . n 
A 1 203 VAL 203 697 697 VAL VAL A . n 
A 1 204 GLU 204 698 698 GLU GLU A . n 
A 1 205 LEU 205 699 699 LEU LEU A . n 
A 1 206 SER 206 700 700 SER SER A . n 
A 1 207 THR 207 701 701 THR THR A . n 
A 1 208 MET 208 702 702 MET MET A . n 
A 1 209 TYR 209 703 703 TYR TYR A . n 
A 1 210 ARG 210 704 704 ARG ARG A . n 
A 1 211 HIS 211 705 705 HIS HIS A . n 
A 1 212 MET 212 706 706 MET MET A . n 
A 1 213 GLU 213 707 707 GLU GLU A . n 
A 1 214 LYS 214 708 708 LYS LYS A . n 
A 1 215 HIS 215 709 709 HIS HIS A . n 
A 1 216 ASN 216 710 710 ASN ASN A . n 
A 1 217 TYR 217 711 711 TYR TYR A . n 
A 1 218 GLU 218 712 712 GLU GLU A . n 
A 1 219 SER 219 713 713 SER SER A . n 
A 1 220 ALA 220 714 714 ALA ALA A . n 
A 1 221 ALA 221 715 715 ALA ALA A . n 
A 1 222 GLU 222 716 716 GLU GLU A . n 
A 1 223 ALA 223 717 717 ALA ALA A . n 
A 1 224 ILE 224 718 718 ILE ILE A . n 
A 1 225 GLN 225 719 719 GLN GLN A . n 
A 1 226 ALA 226 720 720 ALA ALA A . n 
A 1 227 VAL 227 721 721 VAL VAL A . n 
A 1 228 ARG 228 722 722 ARG ARG A . n 
A 1 229 ASP 229 723 723 ASP ASP A . n 
A 1 230 ASN 230 724 724 ASN ASN A . n 
A 1 231 LYS 231 725 725 LYS LYS A . n 
A 1 232 LEU 232 726 726 LEU LEU A . n 
A 1 233 HIS 233 727 727 HIS HIS A . n 
A 1 234 ALA 234 728 728 ALA ALA A . n 
A 1 235 PHE 235 729 729 PHE PHE A . n 
A 1 236 ILE 236 730 730 ILE ILE A . n 
A 1 237 TRP 237 731 731 TRP TRP A . n 
A 1 238 ASP 238 732 732 ASP ASP A . n 
A 1 239 SER 239 733 733 SER SER A . n 
A 1 240 ALA 240 734 734 ALA ALA A . n 
A 1 241 VAL 241 735 735 VAL VAL A . n 
A 1 242 LEU 242 736 736 LEU LEU A . n 
A 1 243 GLU 243 737 737 GLU GLU A . n 
A 1 244 PHE 244 738 738 PHE PHE A . n 
A 1 245 GLU 245 739 739 GLU GLU A . n 
A 1 246 ALA 246 740 740 ALA ALA A . n 
A 1 247 SER 247 741 741 SER SER A . n 
A 1 248 GLN 248 742 742 GLN GLN A . n 
A 1 249 LYS 249 743 743 LYS LYS A . n 
A 1 250 CYS 250 744 744 CYS CYS A . n 
A 1 251 ASP 251 745 745 ASP ASP A . n 
A 1 252 LEU 252 746 746 LEU LEU A . n 
A 1 253 VAL 253 747 747 VAL VAL A . n 
A 1 254 THR 254 748 748 THR THR A . n 
A 1 255 THR 255 749 749 THR THR A . n 
A 1 256 GLY 256 750 750 GLY GLY A . n 
A 1 257 GLU 257 751 751 GLU GLU A . n 
A 1 258 LEU 258 752 752 LEU LEU A . n 
A 1 259 PHE 259 753 753 PHE PHE A . n 
A 1 260 PHE 260 754 754 PHE PHE A . n 
A 1 261 ARG 261 755 755 ARG ARG A . n 
A 1 262 SER 262 756 756 SER SER A . n 
A 1 263 GLY 263 757 757 GLY GLY A . n 
A 1 264 PHE 264 758 758 PHE PHE A . n 
A 1 265 GLY 265 759 759 GLY GLY A . n 
A 1 266 ILE 266 760 760 ILE ILE A . n 
A 1 267 GLY 267 761 761 GLY GLY A . n 
A 1 268 MET 268 762 762 MET MET A . n 
A 1 269 ARG 269 763 763 ARG ARG A . n 
A 1 270 LYS 270 764 764 LYS LYS A . n 
A 1 271 ASP 271 765 765 ASP ASP A . n 
A 1 272 SER 272 766 766 SER SER A . n 
A 1 273 PRO 273 767 767 PRO PRO A . n 
A 1 274 TRP 274 768 768 TRP TRP A . n 
A 1 275 LYS 275 769 769 LYS LYS A . n 
A 1 276 GLN 276 770 770 GLN GLN A . n 
A 1 277 ASN 277 771 771 ASN ASN A . n 
A 1 278 VAL 278 772 772 VAL VAL A . n 
A 1 279 SER 279 773 773 SER SER A . n 
A 1 280 LEU 280 774 774 LEU LEU A . n 
A 1 281 SER 281 775 775 SER SER A . n 
A 1 282 ILE 282 776 776 ILE ILE A . n 
A 1 283 LEU 283 777 777 LEU LEU A . n 
A 1 284 LYS 284 778 778 LYS LYS A . n 
A 1 285 SER 285 779 779 SER SER A . n 
A 1 286 HIS 286 780 780 HIS HIS A . n 
A 1 287 GLU 287 781 781 GLU GLU A . n 
A 1 288 ASN 288 782 782 ASN ASN A . n 
A 1 289 GLY 289 783 783 GLY GLY A . n 
A 1 290 PHE 290 784 784 PHE PHE A . n 
A 1 291 MET 291 785 785 MET MET A . n 
A 1 292 GLU 292 786 786 GLU GLU A . n 
A 1 293 ASP 293 787 787 ASP ASP A . n 
A 1 294 LEU 294 788 788 LEU LEU A . n 
A 1 295 ASP 295 789 789 ASP ASP A . n 
A 1 296 LYS 296 790 790 LYS LYS A . n 
A 1 297 THR 297 791 791 THR THR A . n 
A 1 298 TRP 298 792 792 TRP TRP A . n 
A 1 299 VAL 299 793 793 VAL VAL A . n 
A 1 300 ARG 300 794 794 ARG ARG A . n 
A 1 301 TYR 301 795 795 TYR TYR A . n 
A 1 302 GLN 302 796 ?   ?   ?   A . n 
A 1 303 GLU 303 797 ?   ?   ?   A . n 
A 1 304 CYS 304 798 ?   ?   ?   A . n 
A 1 305 ASP 305 799 ?   ?   ?   A . n 
A 1 306 SER 306 800 ?   ?   ?   A . n 
B 2 1   MET 1   387 ?   ?   ?   B . n 
B 2 2   HIS 2   388 ?   ?   ?   B . n 
B 2 3   HIS 3   389 ?   ?   ?   B . n 
B 2 4   HIS 4   390 ?   ?   ?   B . n 
B 2 5   HIS 5   391 ?   ?   ?   B . n 
B 2 6   HIS 6   392 ?   ?   ?   B . n 
B 2 7   HIS 7   393 ?   ?   ?   B . n 
B 2 8   GLU 8   394 ?   ?   ?   B . n 
B 2 9   ASN 9   395 ?   ?   ?   B . n 
B 2 10  LEU 10  396 ?   ?   ?   B . n 
B 2 11  TYR 11  397 ?   ?   ?   B . n 
B 2 12  PHE 12  398 ?   ?   ?   B . n 
B 2 13  GLN 13  399 ?   ?   ?   B . n 
B 2 14  GLY 14  400 ?   ?   ?   B . n 
B 2 15  PRO 15  401 ?   ?   ?   B . n 
B 2 16  ASP 16  402 ?   ?   ?   B . n 
B 2 17  ASP 17  403 403 ASP ASP B . n 
B 2 18  ASN 18  404 404 ASN ASN B . n 
B 2 19  HIS 19  405 405 HIS HIS B . n 
B 2 20  LEU 20  406 406 LEU LEU B . n 
B 2 21  SER 21  407 407 SER SER B . n 
B 2 22  ILE 22  408 408 ILE ILE B . n 
B 2 23  VAL 23  409 409 VAL VAL B . n 
B 2 24  THR 24  410 410 THR THR B . n 
B 2 25  LEU 25  411 411 LEU LEU B . n 
B 2 26  GLU 26  412 412 GLU GLU B . n 
B 2 27  GLU 27  413 413 GLU GLU B . n 
B 2 28  ALA 28  414 414 ALA ALA B . n 
B 2 29  PRO 29  415 415 PRO PRO B . n 
B 2 30  PHE 30  416 416 PHE PHE B . n 
B 2 31  VAL 31  417 417 VAL VAL B . n 
B 2 32  ILE 32  418 418 ILE ILE B . n 
B 2 33  VAL 33  419 419 VAL VAL B . n 
B 2 34  GLU 34  420 420 GLU GLU B . n 
B 2 35  ASP 35  421 421 ASP ASP B . n 
B 2 36  ILE 36  422 422 ILE ILE B . n 
B 2 37  ASP 37  423 ?   ?   ?   B . n 
B 2 38  PRO 38  424 ?   ?   ?   B . n 
B 2 39  LEU 39  425 ?   ?   ?   B . n 
B 2 40  THR 40  426 ?   ?   ?   B . n 
B 2 41  GLU 41  427 427 GLU GLU B . n 
B 2 42  THR 42  428 428 THR THR B . n 
B 2 43  CYS 43  429 429 CYS CYS B . n 
B 2 44  VAL 44  430 430 VAL VAL B . n 
B 2 45  ARG 45  431 431 ARG ARG B . n 
B 2 46  ASN 46  432 432 ASN ASN B . n 
B 2 47  THR 47  433 433 THR THR B . n 
B 2 48  VAL 48  434 434 VAL VAL B . n 
B 2 49  PRO 49  435 435 PRO PRO B . n 
B 2 50  CYS 50  436 436 CYS CYS B . n 
B 2 51  ARG 51  437 437 ARG ARG B . n 
B 2 52  LYS 52  438 438 LYS LYS B . n 
B 2 53  PHE 53  439 439 PHE PHE B . n 
B 2 54  VAL 54  440 440 VAL VAL B . n 
B 2 55  LYS 55  441 441 LYS LYS B . n 
B 2 56  ILE 56  442 442 ILE ILE B . n 
B 2 57  ASN 57  443 443 ASN ASN B . n 
B 2 58  ASN 58  444 444 ASN ASN B . n 
B 2 59  SER 59  445 445 SER SER B . n 
B 2 60  THR 60  446 446 THR THR B . n 
B 2 61  ASN 61  447 447 ASN ASN B . n 
B 2 62  GLU 62  448 448 GLU GLU B . n 
B 2 63  GLY 63  449 449 GLY GLY B . n 
B 2 64  MET 64  450 450 MET MET B . n 
B 2 65  ASN 65  451 451 ASN ASN B . n 
B 2 66  VAL 66  452 452 VAL VAL B . n 
B 2 67  LYS 67  453 453 LYS LYS B . n 
B 2 68  LYS 68  454 454 LYS LYS B . n 
B 2 69  CYS 69  455 455 CYS CYS B . n 
B 2 70  CYS 70  456 456 CYS CYS B . n 
B 2 71  LYS 71  457 457 LYS LYS B . n 
B 2 72  GLY 72  458 458 GLY GLY B . n 
B 2 73  PHE 73  459 459 PHE PHE B . n 
B 2 74  CYS 74  460 460 CYS CYS B . n 
B 2 75  ILE 75  461 461 ILE ILE B . n 
B 2 76  ASP 76  462 462 ASP ASP B . n 
B 2 77  ILE 77  463 463 ILE ILE B . n 
B 2 78  LEU 78  464 464 LEU LEU B . n 
B 2 79  LYS 79  465 465 LYS LYS B . n 
B 2 80  LYS 80  466 466 LYS LYS B . n 
B 2 81  LEU 81  467 467 LEU LEU B . n 
B 2 82  SER 82  468 468 SER SER B . n 
B 2 83  ARG 83  469 469 ARG ARG B . n 
B 2 84  THR 84  470 470 THR THR B . n 
B 2 85  VAL 85  471 471 VAL VAL B . n 
B 2 86  LYS 86  472 472 LYS LYS B . n 
B 2 87  PHE 87  473 473 PHE PHE B . n 
B 2 88  THR 88  474 474 THR THR B . n 
B 2 89  TYR 89  475 475 TYR TYR B . n 
B 2 90  ASP 90  476 476 ASP ASP B . n 
B 2 91  LEU 91  477 477 LEU LEU B . n 
B 2 92  TYR 92  478 478 TYR TYR B . n 
B 2 93  LEU 93  479 479 LEU LEU B . n 
B 2 94  VAL 94  480 480 VAL VAL B . n 
B 2 95  THR 95  481 481 THR THR B . n 
B 2 96  ASN 96  482 482 ASN ASN B . n 
B 2 97  GLY 97  483 483 GLY GLY B . n 
B 2 98  LYS 98  484 484 LYS LYS B . n 
B 2 99  HIS 99  485 485 HIS HIS B . n 
B 2 100 GLY 100 486 486 GLY GLY B . n 
B 2 101 LYS 101 487 487 LYS LYS B . n 
B 2 102 LYS 102 488 488 LYS LYS B . n 
B 2 103 VAL 103 489 489 VAL VAL B . n 
B 2 104 ASN 104 490 490 ASN ASN B . n 
B 2 105 ASN 105 491 491 ASN ASN B . n 
B 2 106 VAL 106 492 492 VAL VAL B . n 
B 2 107 TRP 107 493 493 TRP TRP B . n 
B 2 108 ASN 108 494 494 ASN ASN B . n 
B 2 109 GLY 109 495 495 GLY GLY B . n 
B 2 110 MET 110 496 496 MET MET B . n 
B 2 111 ILE 111 497 497 ILE ILE B . n 
B 2 112 GLY 112 498 498 GLY GLY B . n 
B 2 113 GLU 113 499 499 GLU GLU B . n 
B 2 114 VAL 114 500 500 VAL VAL B . n 
B 2 115 VAL 115 501 501 VAL VAL B . n 
B 2 116 TYR 116 502 502 TYR TYR B . n 
B 2 117 GLN 117 503 503 GLN GLN B . n 
B 2 118 ARG 118 504 504 ARG ARG B . n 
B 2 119 ALA 119 505 505 ALA ALA B . n 
B 2 120 VAL 120 506 506 VAL VAL B . n 
B 2 121 MET 121 507 507 MET MET B . n 
B 2 122 ALA 122 508 508 ALA ALA B . n 
B 2 123 VAL 123 509 509 VAL VAL B . n 
B 2 124 GLY 124 510 510 GLY GLY B . n 
B 2 125 SER 125 511 511 SER SER B . n 
B 2 126 LEU 126 512 512 LEU LEU B . n 
B 2 127 THR 127 513 513 THR THR B . n 
B 2 128 ILE 128 514 514 ILE ILE B . n 
B 2 129 ASN 129 515 515 ASN ASN B . n 
B 2 130 GLU 130 516 516 GLU GLU B . n 
B 2 131 GLU 131 517 517 GLU GLU B . n 
B 2 132 ARG 132 518 518 ARG ARG B . n 
B 2 133 SER 133 519 519 SER SER B . n 
B 2 134 GLU 134 520 520 GLU GLU B . n 
B 2 135 VAL 135 521 521 VAL VAL B . n 
B 2 136 VAL 136 522 522 VAL VAL B . n 
B 2 137 ASP 137 523 523 ASP ASP B . n 
B 2 138 PHE 138 524 524 PHE PHE B . n 
B 2 139 SER 139 525 525 SER SER B . n 
B 2 140 VAL 140 526 526 VAL VAL B . n 
B 2 141 PRO 141 527 527 PRO PRO B . n 
B 2 142 PHE 142 528 528 PHE PHE B . n 
B 2 143 VAL 143 529 529 VAL VAL B . n 
B 2 144 GLU 144 530 530 GLU GLU B . n 
B 2 145 THR 145 531 531 THR THR B . n 
B 2 146 GLY 146 532 532 GLY GLY B . n 
B 2 147 ILE 147 533 533 ILE ILE B . n 
B 2 148 SER 148 534 534 SER SER B . n 
B 2 149 VAL 149 535 535 VAL VAL B . n 
B 2 150 MET 150 536 536 MET MET B . n 
B 2 151 VAL 151 537 537 VAL VAL B . n 
B 2 152 SER 152 538 538 SER SER B . n 
B 2 153 ARG 153 539 539 ARG ARG B . n 
B 2 154 GLY 154 540 540 GLY GLY B . n 
B 2 155 THR 155 541 541 THR THR B . n 
B 2 156 GLN 156 542 542 GLN GLN B . n 
B 2 157 VAL 157 662 662 VAL VAL B . n 
B 2 158 THR 158 663 663 THR THR B . n 
B 2 159 GLY 159 664 664 GLY GLY B . n 
B 2 160 LEU 160 665 665 LEU LEU B . n 
B 2 161 SER 161 666 666 SER SER B . n 
B 2 162 ASP 162 667 667 ASP ASP B . n 
B 2 163 LYS 163 668 668 LYS LYS B . n 
B 2 164 LYS 164 669 669 LYS LYS B . n 
B 2 165 PHE 165 670 670 PHE PHE B . n 
B 2 166 GLN 166 671 671 GLN GLN B . n 
B 2 167 ARG 167 672 672 ARG ARG B . n 
B 2 168 PRO 168 673 673 PRO PRO B . n 
B 2 169 HIS 169 674 674 HIS HIS B . n 
B 2 170 ASP 170 675 675 ASP ASP B . n 
B 2 171 TYR 171 676 676 TYR TYR B . n 
B 2 172 SER 172 677 677 SER SER B . n 
B 2 173 PRO 173 678 678 PRO PRO B . n 
B 2 174 PRO 174 679 679 PRO PRO B . n 
B 2 175 PHE 175 680 680 PHE PHE B . n 
B 2 176 ARG 176 681 681 ARG ARG B . n 
B 2 177 PHE 177 682 682 PHE PHE B . n 
B 2 178 GLY 178 683 683 GLY GLY B . n 
B 2 179 THR 179 684 684 THR THR B . n 
B 2 180 VAL 180 685 685 VAL VAL B . n 
B 2 181 PRO 181 686 686 PRO PRO B . n 
B 2 182 ASN 182 687 687 ASN ASN B . n 
B 2 183 GLY 183 688 688 GLY GLY B . n 
B 2 184 SER 184 689 689 SER SER B . n 
B 2 185 THR 185 690 690 THR THR B . n 
B 2 186 GLU 186 691 691 GLU GLU B . n 
B 2 187 ARG 187 692 692 ARG ARG B . n 
B 2 188 ASN 188 693 693 ASN ASN B . n 
B 2 189 ILE 189 694 694 ILE ILE B . n 
B 2 190 ARG 190 695 695 ARG ARG B . n 
B 2 191 ASN 191 696 696 ASN ASN B . n 
B 2 192 ASN 192 697 697 ASN ASN B . n 
B 2 193 TYR 193 698 698 TYR TYR B . n 
B 2 194 PRO 194 699 699 PRO PRO B . n 
B 2 195 TYR 195 700 700 TYR TYR B . n 
B 2 196 MET 196 701 701 MET MET B . n 
B 2 197 HIS 197 702 702 HIS HIS B . n 
B 2 198 GLN 198 703 703 GLN GLN B . n 
B 2 199 TYR 199 704 704 TYR TYR B . n 
B 2 200 MET 200 705 705 MET MET B . n 
B 2 201 THR 201 706 706 THR THR B . n 
B 2 202 LYS 202 707 707 LYS LYS B . n 
B 2 203 PHE 203 708 708 PHE PHE B . n 
B 2 204 ASN 204 709 709 ASN ASN B . n 
B 2 205 GLN 205 710 710 GLN GLN B . n 
B 2 206 LYS 206 711 711 LYS LYS B . n 
B 2 207 GLY 207 712 712 GLY GLY B . n 
B 2 208 VAL 208 713 713 VAL VAL B . n 
B 2 209 GLU 209 714 714 GLU GLU B . n 
B 2 210 ASP 210 715 715 ASP ASP B . n 
B 2 211 ALA 211 716 716 ALA ALA B . n 
B 2 212 LEU 212 717 717 LEU LEU B . n 
B 2 213 VAL 213 718 718 VAL VAL B . n 
B 2 214 SER 214 719 719 SER SER B . n 
B 2 215 LEU 215 720 720 LEU LEU B . n 
B 2 216 LYS 216 721 721 LYS LYS B . n 
B 2 217 THR 217 722 722 THR THR B . n 
B 2 218 GLY 218 723 723 GLY GLY B . n 
B 2 219 LYS 219 724 724 LYS LYS B . n 
B 2 220 LEU 220 725 725 LEU LEU B . n 
B 2 221 ASP 221 726 726 ASP ASP B . n 
B 2 222 ALA 222 727 727 ALA ALA B . n 
B 2 223 PHE 223 728 728 PHE PHE B . n 
B 2 224 ILE 224 729 729 ILE ILE B . n 
B 2 225 TYR 225 730 730 TYR TYR B . n 
B 2 226 ASP 226 731 731 ASP ASP B . n 
B 2 227 ALA 227 732 732 ALA ALA B . n 
B 2 228 ALA 228 733 733 ALA ALA B . n 
B 2 229 VAL 229 734 734 VAL VAL B . n 
B 2 230 LEU 230 735 735 LEU LEU B . n 
B 2 231 ASN 231 736 736 ASN ASN B . n 
B 2 232 TYR 232 737 737 TYR TYR B . n 
B 2 233 LYS 233 738 738 LYS LYS B . n 
B 2 234 ALA 234 739 739 ALA ALA B . n 
B 2 235 GLY 235 740 740 GLY GLY B . n 
B 2 236 ARG 236 741 741 ARG ARG B . n 
B 2 237 ASP 237 742 742 ASP ASP B . n 
B 2 238 GLU 238 743 743 GLU GLU B . n 
B 2 239 GLY 239 744 744 GLY GLY B . n 
B 2 240 CYS 240 745 745 CYS CYS B . n 
B 2 241 LYS 241 746 746 LYS LYS B . n 
B 2 242 LEU 242 747 747 LEU LEU B . n 
B 2 243 VAL 243 748 748 VAL VAL B . n 
B 2 244 THR 244 749 749 THR THR B . n 
B 2 245 ILE 245 750 750 ILE ILE B . n 
B 2 246 GLY 246 751 751 GLY GLY B . n 
B 2 247 SER 247 752 752 SER SER B . n 
B 2 248 GLY 248 753 753 GLY GLY B . n 
B 2 249 TYR 249 754 754 TYR TYR B . n 
B 2 250 ILE 250 755 755 ILE ILE B . n 
B 2 251 PHE 251 756 756 PHE PHE B . n 
B 2 252 ALA 252 757 757 ALA ALA B . n 
B 2 253 THR 253 758 758 THR THR B . n 
B 2 254 THR 254 759 759 THR THR B . n 
B 2 255 GLY 255 760 760 GLY GLY B . n 
B 2 256 TYR 256 761 761 TYR TYR B . n 
B 2 257 GLY 257 762 762 GLY GLY B . n 
B 2 258 ILE 258 763 763 ILE ILE B . n 
B 2 259 ALA 259 764 764 ALA ALA B . n 
B 2 260 LEU 260 765 765 LEU LEU B . n 
B 2 261 GLN 261 766 766 GLN GLN B . n 
B 2 262 LYS 262 767 767 LYS LYS B . n 
B 2 263 GLY 263 768 768 GLY GLY B . n 
B 2 264 SER 264 769 769 SER SER B . n 
B 2 265 PRO 265 770 770 PRO PRO B . n 
B 2 266 TRP 266 771 771 TRP TRP B . n 
B 2 267 LYS 267 772 772 LYS LYS B . n 
B 2 268 ARG 268 773 773 ARG ARG B . n 
B 2 269 GLN 269 774 774 GLN GLN B . n 
B 2 270 ILE 270 775 775 ILE ILE B . n 
B 2 271 ASP 271 776 776 ASP ASP B . n 
B 2 272 LEU 272 777 777 LEU LEU B . n 
B 2 273 ALA 273 778 778 ALA ALA B . n 
B 2 274 LEU 274 779 779 LEU LEU B . n 
B 2 275 LEU 275 780 780 LEU LEU B . n 
B 2 276 GLN 276 781 781 GLN GLN B . n 
B 2 277 PHE 277 782 782 PHE PHE B . n 
B 2 278 VAL 278 783 783 VAL VAL B . n 
B 2 279 GLY 279 784 784 GLY GLY B . n 
B 2 280 ASP 280 785 785 ASP ASP B . n 
B 2 281 GLY 281 786 786 GLY GLY B . n 
B 2 282 GLU 282 787 787 GLU GLU B . n 
B 2 283 MET 283 788 788 MET MET B . n 
B 2 284 GLU 284 789 789 GLU GLU B . n 
B 2 285 GLU 285 790 790 GLU GLU B . n 
B 2 286 LEU 286 791 791 LEU LEU B . n 
B 2 287 GLU 287 792 792 GLU GLU B . n 
B 2 288 THR 288 793 793 THR THR B . n 
B 2 289 LEU 289 794 794 LEU LEU B . n 
B 2 290 TRP 290 795 795 TRP TRP B . n 
B 2 291 LEU 291 796 796 LEU LEU B . n 
B 2 292 THR 292 797 797 THR THR B . n 
B 2 293 GLY 293 798 798 GLY GLY B . n 
B 2 294 ILE 294 799 799 ILE ILE B . n 
B 2 295 CYS 295 800 800 CYS CYS B . n 
B 2 296 HIS 296 801 ?   ?   ?   B . n 
B 2 297 ASN 297 802 ?   ?   ?   B . n 
# 
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 
C 3 GLY   1   1001 1001 GLY   GLY A . 
D 4 GLU   1   1001 1001 GLU   GLU B . 
E 5 A1BRB 1   1002 1    A1BRB UNL B . 
F 6 HOH   1   1101 169  HOH   HOH A . 
F 6 HOH   2   1102 178  HOH   HOH A . 
F 6 HOH   3   1103 15   HOH   HOH A . 
F 6 HOH   4   1104 147  HOH   HOH A . 
F 6 HOH   5   1105 206  HOH   HOH A . 
F 6 HOH   6   1106 172  HOH   HOH A . 
F 6 HOH   7   1107 142  HOH   HOH A . 
F 6 HOH   8   1108 182  HOH   HOH A . 
F 6 HOH   9   1109 239  HOH   HOH A . 
F 6 HOH   10  1110 154  HOH   HOH A . 
F 6 HOH   11  1111 223  HOH   HOH A . 
F 6 HOH   12  1112 71   HOH   HOH A . 
F 6 HOH   13  1113 177  HOH   HOH A . 
F 6 HOH   14  1114 204  HOH   HOH A . 
F 6 HOH   15  1115 151  HOH   HOH A . 
F 6 HOH   16  1116 46   HOH   HOH A . 
F 6 HOH   17  1117 10   HOH   HOH A . 
F 6 HOH   18  1118 139  HOH   HOH A . 
F 6 HOH   19  1119 120  HOH   HOH A . 
F 6 HOH   20  1120 153  HOH   HOH A . 
F 6 HOH   21  1121 133  HOH   HOH A . 
F 6 HOH   22  1122 103  HOH   HOH A . 
F 6 HOH   23  1123 145  HOH   HOH A . 
F 6 HOH   24  1124 225  HOH   HOH A . 
F 6 HOH   25  1125 44   HOH   HOH A . 
F 6 HOH   26  1126 55   HOH   HOH A . 
F 6 HOH   27  1127 26   HOH   HOH A . 
F 6 HOH   28  1128 83   HOH   HOH A . 
F 6 HOH   29  1129 41   HOH   HOH A . 
F 6 HOH   30  1130 4    HOH   HOH A . 
F 6 HOH   31  1131 38   HOH   HOH A . 
F 6 HOH   32  1132 100  HOH   HOH A . 
F 6 HOH   33  1133 129  HOH   HOH A . 
F 6 HOH   34  1134 87   HOH   HOH A . 
F 6 HOH   35  1135 152  HOH   HOH A . 
F 6 HOH   36  1136 64   HOH   HOH A . 
F 6 HOH   37  1137 173  HOH   HOH A . 
F 6 HOH   38  1138 210  HOH   HOH A . 
F 6 HOH   39  1139 110  HOH   HOH A . 
F 6 HOH   40  1140 170  HOH   HOH A . 
F 6 HOH   41  1141 81   HOH   HOH A . 
F 6 HOH   42  1142 69   HOH   HOH A . 
F 6 HOH   43  1143 196  HOH   HOH A . 
F 6 HOH   44  1144 24   HOH   HOH A . 
F 6 HOH   45  1145 22   HOH   HOH A . 
F 6 HOH   46  1146 104  HOH   HOH A . 
F 6 HOH   47  1147 181  HOH   HOH A . 
F 6 HOH   48  1148 184  HOH   HOH A . 
F 6 HOH   49  1149 82   HOH   HOH A . 
F 6 HOH   50  1150 66   HOH   HOH A . 
F 6 HOH   51  1151 13   HOH   HOH A . 
F 6 HOH   52  1152 148  HOH   HOH A . 
F 6 HOH   53  1153 195  HOH   HOH A . 
F 6 HOH   54  1154 62   HOH   HOH A . 
F 6 HOH   55  1155 227  HOH   HOH A . 
F 6 HOH   56  1156 53   HOH   HOH A . 
F 6 HOH   57  1157 11   HOH   HOH A . 
F 6 HOH   58  1158 21   HOH   HOH A . 
F 6 HOH   59  1159 97   HOH   HOH A . 
F 6 HOH   60  1160 84   HOH   HOH A . 
F 6 HOH   61  1161 159  HOH   HOH A . 
F 6 HOH   62  1162 114  HOH   HOH A . 
F 6 HOH   63  1163 161  HOH   HOH A . 
F 6 HOH   64  1164 34   HOH   HOH A . 
F 6 HOH   65  1165 134  HOH   HOH A . 
F 6 HOH   66  1166 176  HOH   HOH A . 
F 6 HOH   67  1167 213  HOH   HOH A . 
F 6 HOH   68  1168 127  HOH   HOH A . 
F 6 HOH   69  1169 167  HOH   HOH A . 
F 6 HOH   70  1170 79   HOH   HOH A . 
F 6 HOH   71  1171 220  HOH   HOH A . 
F 6 HOH   72  1172 28   HOH   HOH A . 
F 6 HOH   73  1173 70   HOH   HOH A . 
F 6 HOH   74  1174 212  HOH   HOH A . 
F 6 HOH   75  1175 49   HOH   HOH A . 
F 6 HOH   76  1176 187  HOH   HOH A . 
F 6 HOH   77  1177 113  HOH   HOH A . 
F 6 HOH   78  1178 207  HOH   HOH A . 
F 6 HOH   79  1179 141  HOH   HOH A . 
F 6 HOH   80  1180 156  HOH   HOH A . 
F 6 HOH   81  1181 29   HOH   HOH A . 
F 6 HOH   82  1182 76   HOH   HOH A . 
F 6 HOH   83  1183 35   HOH   HOH A . 
F 6 HOH   84  1184 180  HOH   HOH A . 
F 6 HOH   85  1185 189  HOH   HOH A . 
F 6 HOH   86  1186 5    HOH   HOH A . 
F 6 HOH   87  1187 85   HOH   HOH A . 
F 6 HOH   88  1188 130  HOH   HOH A . 
F 6 HOH   89  1189 234  HOH   HOH A . 
F 6 HOH   90  1190 116  HOH   HOH A . 
F 6 HOH   91  1191 140  HOH   HOH A . 
F 6 HOH   92  1192 2    HOH   HOH A . 
F 6 HOH   93  1193 160  HOH   HOH A . 
F 6 HOH   94  1194 117  HOH   HOH A . 
F 6 HOH   95  1195 175  HOH   HOH A . 
F 6 HOH   96  1196 168  HOH   HOH A . 
F 6 HOH   97  1197 166  HOH   HOH A . 
F 6 HOH   98  1198 146  HOH   HOH A . 
F 6 HOH   99  1199 112  HOH   HOH A . 
F 6 HOH   100 1200 150  HOH   HOH A . 
F 6 HOH   101 1201 205  HOH   HOH A . 
F 6 HOH   102 1202 209  HOH   HOH A . 
F 6 HOH   103 1203 202  HOH   HOH A . 
F 6 HOH   104 1204 215  HOH   HOH A . 
F 6 HOH   105 1205 208  HOH   HOH A . 
F 6 HOH   106 1206 235  HOH   HOH A . 
F 6 HOH   107 1207 237  HOH   HOH A . 
F 6 HOH   108 1208 185  HOH   HOH A . 
F 6 HOH   109 1209 224  HOH   HOH A . 
F 6 HOH   110 1210 200  HOH   HOH A . 
F 6 HOH   111 1211 149  HOH   HOH A . 
F 6 HOH   112 1212 118  HOH   HOH A . 
F 6 HOH   113 1213 91   HOH   HOH A . 
F 6 HOH   114 1214 92   HOH   HOH A . 
F 6 HOH   115 1215 191  HOH   HOH A . 
F 6 HOH   116 1216 242  HOH   HOH A . 
G 6 HOH   1   1101 194  HOH   HOH B . 
G 6 HOH   2   1102 143  HOH   HOH B . 
G 6 HOH   3   1103 37   HOH   HOH B . 
G 6 HOH   4   1104 123  HOH   HOH B . 
G 6 HOH   5   1105 67   HOH   HOH B . 
G 6 HOH   6   1106 164  HOH   HOH B . 
G 6 HOH   7   1107 174  HOH   HOH B . 
G 6 HOH   8   1108 119  HOH   HOH B . 
G 6 HOH   9   1109 211  HOH   HOH B . 
G 6 HOH   10  1110 80   HOH   HOH B . 
G 6 HOH   11  1111 65   HOH   HOH B . 
G 6 HOH   12  1112 126  HOH   HOH B . 
G 6 HOH   13  1113 86   HOH   HOH B . 
G 6 HOH   14  1114 201  HOH   HOH B . 
G 6 HOH   15  1115 43   HOH   HOH B . 
G 6 HOH   16  1116 214  HOH   HOH B . 
G 6 HOH   17  1117 93   HOH   HOH B . 
G 6 HOH   18  1118 63   HOH   HOH B . 
G 6 HOH   19  1119 132  HOH   HOH B . 
G 6 HOH   20  1120 18   HOH   HOH B . 
G 6 HOH   21  1121 108  HOH   HOH B . 
G 6 HOH   22  1122 158  HOH   HOH B . 
G 6 HOH   23  1123 20   HOH   HOH B . 
G 6 HOH   24  1124 236  HOH   HOH B . 
G 6 HOH   25  1125 61   HOH   HOH B . 
G 6 HOH   26  1126 101  HOH   HOH B . 
G 6 HOH   27  1127 45   HOH   HOH B . 
G 6 HOH   28  1128 90   HOH   HOH B . 
G 6 HOH   29  1129 58   HOH   HOH B . 
G 6 HOH   30  1130 27   HOH   HOH B . 
G 6 HOH   31  1131 39   HOH   HOH B . 
G 6 HOH   32  1132 135  HOH   HOH B . 
G 6 HOH   33  1133 25   HOH   HOH B . 
G 6 HOH   34  1134 218  HOH   HOH B . 
G 6 HOH   35  1135 48   HOH   HOH B . 
G 6 HOH   36  1136 128  HOH   HOH B . 
G 6 HOH   37  1137 12   HOH   HOH B . 
G 6 HOH   38  1138 136  HOH   HOH B . 
G 6 HOH   39  1139 111  HOH   HOH B . 
G 6 HOH   40  1140 102  HOH   HOH B . 
G 6 HOH   41  1141 23   HOH   HOH B . 
G 6 HOH   42  1142 198  HOH   HOH B . 
G 6 HOH   43  1143 42   HOH   HOH B . 
G 6 HOH   44  1144 31   HOH   HOH B . 
G 6 HOH   45  1145 59   HOH   HOH B . 
G 6 HOH   46  1146 203  HOH   HOH B . 
G 6 HOH   47  1147 125  HOH   HOH B . 
G 6 HOH   48  1148 138  HOH   HOH B . 
G 6 HOH   49  1149 72   HOH   HOH B . 
G 6 HOH   50  1150 19   HOH   HOH B . 
G 6 HOH   51  1151 98   HOH   HOH B . 
G 6 HOH   52  1152 8    HOH   HOH B . 
G 6 HOH   53  1153 241  HOH   HOH B . 
G 6 HOH   54  1154 193  HOH   HOH B . 
G 6 HOH   55  1155 217  HOH   HOH B . 
G 6 HOH   56  1156 216  HOH   HOH B . 
G 6 HOH   57  1157 179  HOH   HOH B . 
G 6 HOH   58  1158 6    HOH   HOH B . 
G 6 HOH   59  1159 36   HOH   HOH B . 
G 6 HOH   60  1160 89   HOH   HOH B . 
G 6 HOH   61  1161 73   HOH   HOH B . 
G 6 HOH   62  1162 3    HOH   HOH B . 
G 6 HOH   63  1163 68   HOH   HOH B . 
G 6 HOH   64  1164 228  HOH   HOH B . 
G 6 HOH   65  1165 9    HOH   HOH B . 
G 6 HOH   66  1166 77   HOH   HOH B . 
G 6 HOH   67  1167 32   HOH   HOH B . 
G 6 HOH   68  1168 171  HOH   HOH B . 
G 6 HOH   69  1169 107  HOH   HOH B . 
G 6 HOH   70  1170 60   HOH   HOH B . 
G 6 HOH   71  1171 95   HOH   HOH B . 
G 6 HOH   72  1172 75   HOH   HOH B . 
G 6 HOH   73  1173 105  HOH   HOH B . 
G 6 HOH   74  1174 88   HOH   HOH B . 
G 6 HOH   75  1175 144  HOH   HOH B . 
G 6 HOH   76  1176 50   HOH   HOH B . 
G 6 HOH   77  1177 78   HOH   HOH B . 
G 6 HOH   78  1178 51   HOH   HOH B . 
G 6 HOH   79  1179 96   HOH   HOH B . 
G 6 HOH   80  1180 7    HOH   HOH B . 
G 6 HOH   81  1181 121  HOH   HOH B . 
G 6 HOH   82  1182 57   HOH   HOH B . 
G 6 HOH   83  1183 233  HOH   HOH B . 
G 6 HOH   84  1184 238  HOH   HOH B . 
G 6 HOH   85  1185 197  HOH   HOH B . 
G 6 HOH   86  1186 183  HOH   HOH B . 
G 6 HOH   87  1187 99   HOH   HOH B . 
G 6 HOH   88  1188 122  HOH   HOH B . 
G 6 HOH   89  1189 137  HOH   HOH B . 
G 6 HOH   90  1190 109  HOH   HOH B . 
G 6 HOH   91  1191 115  HOH   HOH B . 
G 6 HOH   92  1192 74   HOH   HOH B . 
G 6 HOH   93  1193 33   HOH   HOH B . 
G 6 HOH   94  1194 47   HOH   HOH B . 
G 6 HOH   95  1195 40   HOH   HOH B . 
G 6 HOH   96  1196 188  HOH   HOH B . 
G 6 HOH   97  1197 14   HOH   HOH B . 
G 6 HOH   98  1198 106  HOH   HOH B . 
G 6 HOH   99  1199 52   HOH   HOH B . 
G 6 HOH   100 1200 56   HOH   HOH B . 
G 6 HOH   101 1201 16   HOH   HOH B . 
G 6 HOH   102 1202 30   HOH   HOH B . 
G 6 HOH   103 1203 231  HOH   HOH B . 
G 6 HOH   104 1204 163  HOH   HOH B . 
G 6 HOH   105 1205 17   HOH   HOH B . 
G 6 HOH   106 1206 190  HOH   HOH B . 
G 6 HOH   107 1207 131  HOH   HOH B . 
G 6 HOH   108 1208 221  HOH   HOH B . 
G 6 HOH   109 1209 1    HOH   HOH B . 
G 6 HOH   110 1210 155  HOH   HOH B . 
G 6 HOH   111 1211 124  HOH   HOH B . 
G 6 HOH   112 1212 226  HOH   HOH B . 
G 6 HOH   113 1213 230  HOH   HOH B . 
G 6 HOH   114 1214 192  HOH   HOH B . 
G 6 HOH   115 1215 232  HOH   HOH B . 
G 6 HOH   116 1216 186  HOH   HOH B . 
G 6 HOH   117 1217 165  HOH   HOH B . 
G 6 HOH   118 1218 54   HOH   HOH B . 
G 6 HOH   119 1219 243  HOH   HOH B . 
G 6 HOH   120 1220 94   HOH   HOH B . 
G 6 HOH   121 1221 162  HOH   HOH B . 
G 6 HOH   122 1222 219  HOH   HOH B . 
G 6 HOH   123 1223 229  HOH   HOH B . 
G 6 HOH   124 1224 222  HOH   HOH B . 
G 6 HOH   125 1225 199  HOH   HOH B . 
G 6 HOH   126 1226 244  HOH   HOH B . 
G 6 HOH   127 1227 240  HOH   HOH B . 
G 6 HOH   128 1228 157  HOH   HOH B . 
# 
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 SER 416 ? OG  ? A SER 38  OG  
2  1 Y 1 A HIS 449 ? CG  ? A HIS 71  CG  
3  1 Y 1 A HIS 449 ? ND1 ? A HIS 71  ND1 
4  1 Y 1 A HIS 449 ? CD2 ? A HIS 71  CD2 
5  1 Y 1 A HIS 449 ? CE1 ? A HIS 71  CE1 
6  1 Y 1 A HIS 449 ? NE2 ? A HIS 71  NE2 
7  1 Y 1 A LYS 495 ? CG  ? A LYS 117 CG  
8  1 Y 1 A LYS 495 ? CD  ? A LYS 117 CD  
9  1 Y 1 A LYS 495 ? CE  ? A LYS 117 CE  
10 1 Y 1 A LYS 495 ? NZ  ? A LYS 117 NZ  
11 1 Y 1 A LYS 496 ? CG  ? A LYS 118 CG  
12 1 Y 1 A LYS 496 ? CD  ? A LYS 118 CD  
13 1 Y 1 A LYS 496 ? CE  ? A LYS 118 CE  
14 1 Y 1 A LYS 496 ? NZ  ? A LYS 118 NZ  
15 1 Y 1 A ARG 663 ? CG  ? A ARG 169 CG  
16 1 Y 1 A ARG 663 ? CD  ? A ARG 169 CD  
17 1 Y 1 A ARG 663 ? NE  ? A ARG 169 NE  
18 1 Y 1 A ARG 663 ? CZ  ? A ARG 169 CZ  
19 1 Y 1 A ARG 663 ? NH1 ? A ARG 169 NH1 
20 1 Y 1 A ARG 663 ? NH2 ? A ARG 169 NH2 
21 1 Y 1 A ARG 695 ? CG  ? A ARG 201 CG  
22 1 Y 1 A ARG 695 ? CD  ? A ARG 201 CD  
23 1 Y 1 A ARG 695 ? NE  ? A ARG 201 NE  
24 1 Y 1 A ARG 695 ? CZ  ? A ARG 201 CZ  
25 1 Y 1 A ARG 695 ? NH1 ? A ARG 201 NH1 
26 1 Y 1 A ARG 695 ? NH2 ? A ARG 201 NH2 
27 1 Y 1 A GLU 698 ? CG  ? A GLU 204 CG  
28 1 Y 1 A GLU 698 ? CD  ? A GLU 204 CD  
29 1 Y 1 A GLU 698 ? OE1 ? A GLU 204 OE1 
30 1 Y 1 A GLU 698 ? OE2 ? A GLU 204 OE2 
31 1 Y 1 A GLU 707 ? CG  ? A GLU 213 CG  
32 1 Y 1 A GLU 707 ? CD  ? A GLU 213 CD  
33 1 Y 1 A GLU 707 ? OE1 ? A GLU 213 OE1 
34 1 Y 1 A GLU 707 ? OE2 ? A GLU 213 OE2 
35 1 Y 1 A LYS 708 ? CG  ? A LYS 214 CG  
36 1 Y 1 A LYS 708 ? CD  ? A LYS 214 CD  
37 1 Y 1 A LYS 708 ? CE  ? A LYS 214 CE  
38 1 Y 1 A LYS 708 ? NZ  ? A LYS 214 NZ  
39 1 Y 1 A LYS 725 ? CG  ? A LYS 231 CG  
40 1 Y 1 A LYS 725 ? CD  ? A LYS 231 CD  
41 1 Y 1 A LYS 725 ? CE  ? A LYS 231 CE  
42 1 Y 1 A LYS 725 ? NZ  ? A LYS 231 NZ  
43 1 Y 1 A GLU 751 ? CG  ? A GLU 257 CG  
44 1 Y 1 A GLU 751 ? CD  ? A GLU 257 CD  
45 1 Y 1 A GLU 751 ? OE1 ? A GLU 257 OE1 
46 1 Y 1 A GLU 751 ? OE2 ? A GLU 257 OE2 
47 1 Y 1 B GLU 427 ? CG  ? B GLU 41  CG  
48 1 Y 1 B GLU 427 ? CD  ? B GLU 41  CD  
49 1 Y 1 B GLU 427 ? OE1 ? B GLU 41  OE1 
50 1 Y 1 B GLU 427 ? OE2 ? B GLU 41  OE2 
51 1 Y 1 B LYS 453 ? CG  ? B LYS 67  CG  
52 1 Y 1 B LYS 453 ? CD  ? B LYS 67  CD  
53 1 Y 1 B LYS 453 ? CE  ? B LYS 67  CE  
54 1 Y 1 B LYS 453 ? NZ  ? B LYS 67  NZ  
55 1 Y 1 B GLN 542 ? CG  ? B GLN 156 CG  
56 1 Y 1 B GLN 542 ? CD  ? B GLN 156 CD  
57 1 Y 1 B GLN 542 ? OE1 ? B GLN 156 OE1 
58 1 Y 1 B GLN 542 ? NE2 ? B GLN 156 NE2 
59 1 Y 1 B GLU 743 ? CG  ? B GLU 238 CG  
60 1 Y 1 B GLU 743 ? CD  ? B GLU 238 CD  
61 1 Y 1 B GLU 743 ? OE1 ? B GLU 238 OE1 
62 1 Y 1 B GLU 743 ? OE2 ? B GLU 238 OE2 
63 1 Y 1 B LYS 746 ? CG  ? B LYS 241 CG  
64 1 Y 1 B LYS 746 ? CD  ? B LYS 241 CD  
65 1 Y 1 B LYS 746 ? CE  ? B LYS 241 CE  
66 1 Y 1 B LYS 746 ? NZ  ? B LYS 241 NZ  
67 1 Y 1 B GLU 789 ? CG  ? B GLU 284 CG  
68 1 Y 1 B GLU 789 ? CD  ? B GLU 284 CD  
69 1 Y 1 B GLU 789 ? OE1 ? B GLU 284 OE1 
70 1 Y 1 B GLU 789 ? OE2 ? B GLU 284 OE2 
# 
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 ? ? ? 1.20.1_4487                     1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? 'Mar 15, 2019 (BUILT 20191211)' 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? 'Mar 15, 2019 (BUILT 20191211)' 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487                     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                     9MUM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     54.500 
_cell.length_a_esd                 ? 
_cell.length_b                     90.000 
_cell.length_b_esd                 ? 
_cell.length_c                     124.940 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9MUM 
_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                   9MUM 
_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             2.23 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.83 
_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              7.0 
_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    '0.1M Hepes pH 7.0, 0.2M ammonium acetate, 20% PEG-3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 X 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         2020-03-14 
_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 
_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 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MUM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.97 
_reflns.d_resolution_low                               37.8 
_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                                     40128 
_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                           90.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.9 
_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                                0.057 
_reflns.pdbx_Rpim_I_all                                0.022 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.053 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_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                                    1.97 
_reflns_shell.d_res_low                                     2.01 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2182 
_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                               6.8 
_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                               .963 
_reflns_shell.pdbx_Rpim_I_all                               0.367 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  .735 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.890 
_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                                 9MUM 
_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                            1.97 
_refine.ls_d_res_low                             37.80 
_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                     40117 
_refine.ls_number_reflns_R_free                  2051 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    90.87 
_refine.ls_percent_reflns_R_free                 5.11 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1944 
_refine.ls_R_factor_R_free                       0.2408 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1919 
_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                          1.34 
_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               THROUGHOUT 
_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                 24.30 
_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                            0.22 
_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                       1.97 
_refine_hist.d_res_low                        37.80 
_refine_hist.number_atoms_solvent             244 
_refine_hist.number_atoms_total               4583 
_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        4294 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         45 
_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' ? 0.007 ? 4428 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.842 ? 5990 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.731 ? 594  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.058 ? 666  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007 ? 773  ? 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' 1.97 2.02  . . 161 2775 100.00 . . . . 0.2397 . . . . . . . . . . . 0.2963 
'X-RAY DIFFRACTION' 2.02 2.07  . . 150 2726 100.00 . . . . 0.2257 . . . . . . . . . . . 0.2655 
'X-RAY DIFFRACTION' 2.07 2.12  . . 139 2727 100.00 . . . . 0.2164 . . . . . . . . . . . 0.2731 
'X-RAY DIFFRACTION' 2.12 2.19  . . 143 2793 100.00 . . . . 0.2133 . . . . . . . . . . . 0.2911 
'X-RAY DIFFRACTION' 2.19 2.24  . . 100 2063 98.00  . . . . 0.2146 . . . . . . . . . . . 0.3088 
'X-RAY DIFFRACTION' 2.27 2.34  . . 126 2466 100.00 . . . . 0.2002 . . . . . . . . . . . 0.2480 
'X-RAY DIFFRACTION' 2.34 2.43  . . 146 2761 100.00 . . . . 0.2003 . . . . . . . . . . . 0.2486 
'X-RAY DIFFRACTION' 2.43 2.54  . . 161 2750 100.00 . . . . 0.2092 . . . . . . . . . . . 0.2849 
'X-RAY DIFFRACTION' 2.54 2.61  . . 74  1531 99.00  . . . . 0.2246 . . . . . . . . . . . 0.2847 
'X-RAY DIFFRACTION' 2.70 2.84  . . 110 2373 100.00 . . . . 0.2272 . . . . . . . . . . . 0.2690 
'X-RAY DIFFRACTION' 2.84 3.06  . . 138 2792 100.00 . . . . 0.2287 . . . . . . . . . . . 0.2613 
'X-RAY DIFFRACTION' 3.06 3.37  . . 182 2775 100.00 . . . . 0.2038 . . . . . . . . . . . 0.2624 
'X-RAY DIFFRACTION' 3.37 3.86  . . 114 1948 70.00  . . . . 0.1797 . . . . . . . . . . . 0.2436 
'X-RAY DIFFRACTION' 3.86 4.86  . . 143 2601 91.00  . . . . 0.1507 . . . . . . . . . . . 0.1953 
'X-RAY DIFFRACTION' 4.86 37.80 . . 164 2985 100.00 . . . . 0.1806 . . . . . . . . . . . 0.2111 
# 
_struct.entry_id                     9MUM 
_struct.title                        
'Crystal structure of GluN1/GluN2A ligand-binding domain in complex with Compound 11, Glycine and Glutamate' 
_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        9MUM 
_struct_keywords.text            'NMDARS, LBD, ION CHANNELS, METAL TRANSPORT, NEGATIVE MODULATOR, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
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 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 6 ? 
# 
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 NMDZ1_HUMAN Q05586 ? 1 
;MSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFT
YEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKK
;
394 
2 UNP NMDZ1_HUMAN Q05586 ? 1 
;RITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQ
KCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDS
;
663 
3 UNP NMDE1_HUMAN Q12879 ? 2 
;PDDNHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNSTNEGMNVKKCCKGFCIDILKKLSRTVKFTYDLYLV
TNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSR
;
401 
4 UNP NMDE1_HUMAN Q12879 ? 2 
;QVTGLSDKKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPYMHQYMTKFNQKGVEDALVSLKTGKLDAFIYDAAVLNYKAG
RDEGCKLVTIGSGYIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGICHN
;
661 
# 
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 9MUM A 16  ? 166 ? Q05586 394 ? 544 ? 394 544 
2 2 9MUM A 169 ? 306 ? Q05586 663 ? 800 ? 663 800 
3 3 9MUM B 15  ? 153 ? Q12879 401 ? 539 ? 401 539 
4 4 9MUM B 156 ? 297 ? Q12879 661 ? 802 ? 542 802 
# 
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 
1 9MUM MET A 1   ? UNP Q05586 ? ? 'initiating methionine' 379 1  
1 9MUM HIS A 2   ? UNP Q05586 ? ? 'expression tag'        380 2  
1 9MUM HIS A 3   ? UNP Q05586 ? ? 'expression tag'        381 3  
1 9MUM HIS A 4   ? UNP Q05586 ? ? 'expression tag'        382 4  
1 9MUM HIS A 5   ? UNP Q05586 ? ? 'expression tag'        383 5  
1 9MUM HIS A 6   ? UNP Q05586 ? ? 'expression tag'        384 6  
1 9MUM HIS A 7   ? UNP Q05586 ? ? 'expression tag'        385 7  
1 9MUM GLU A 8   ? UNP Q05586 ? ? 'expression tag'        386 8  
1 9MUM ASN A 9   ? UNP Q05586 ? ? 'expression tag'        387 9  
1 9MUM LEU A 10  ? UNP Q05586 ? ? 'expression tag'        388 10 
1 9MUM TYR A 11  ? UNP Q05586 ? ? 'expression tag'        389 11 
1 9MUM PHE A 12  ? UNP Q05586 ? ? 'expression tag'        390 12 
1 9MUM GLN A 13  ? UNP Q05586 ? ? 'expression tag'        391 13 
1 9MUM GLY A 14  ? UNP Q05586 ? ? 'expression tag'        392 14 
1 9MUM SER A 15  ? UNP Q05586 ? ? 'expression tag'        393 15 
1 9MUM GLY A 167 ? UNP Q05586 ? ? linker                  545 16 
1 9MUM THR A 168 ? UNP Q05586 ? ? linker                  546 17 
3 9MUM MET B 1   ? UNP Q12879 ? ? 'initiating methionine' 387 18 
3 9MUM HIS B 2   ? UNP Q12879 ? ? 'expression tag'        388 19 
3 9MUM HIS B 3   ? UNP Q12879 ? ? 'expression tag'        389 20 
3 9MUM HIS B 4   ? UNP Q12879 ? ? 'expression tag'        390 21 
3 9MUM HIS B 5   ? UNP Q12879 ? ? 'expression tag'        391 22 
3 9MUM HIS B 6   ? UNP Q12879 ? ? 'expression tag'        392 23 
3 9MUM HIS B 7   ? UNP Q12879 ? ? 'expression tag'        393 24 
3 9MUM GLU B 8   ? UNP Q12879 ? ? 'expression tag'        394 25 
3 9MUM ASN B 9   ? UNP Q12879 ? ? 'expression tag'        395 26 
3 9MUM LEU B 10  ? UNP Q12879 ? ? 'expression tag'        396 27 
3 9MUM TYR B 11  ? UNP Q12879 ? ? 'expression tag'        397 28 
3 9MUM PHE B 12  ? UNP Q12879 ? ? 'expression tag'        398 29 
3 9MUM GLN B 13  ? UNP Q12879 ? ? 'expression tag'        399 30 
3 9MUM GLY B 14  ? UNP Q12879 ? ? 'expression tag'        400 31 
3 9MUM GLY B 154 ? UNP Q12879 ? ? linker                  540 32 
3 9MUM THR B 155 ? UNP Q12879 ? ? linker                  541 33 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 3160  ? 
1 MORE         -6    ? 
1 'SSA (A^2)'  24110 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 GLY A 79  ? ASN A 93  ? GLY A 457 ASN A 471 1 ? 15 
HELX_P HELX_P2  AA2 ASN A 121 ? SER A 129 ? ASN A 499 SER A 507 1 ? 9  
HELX_P HELX_P3  AA3 ASN A 142 ? GLN A 147 ? ASN A 520 GLN A 525 1 ? 6  
HELX_P HELX_P4  AA4 ASP A 175 ? ASN A 180 ? ASP A 669 ASN A 674 1 ? 6  
HELX_P HELX_P5  AA5 SER A 193 ? GLN A 202 ? SER A 687 GLN A 696 1 ? 10 
HELX_P HELX_P6  AA6 LEU A 205 ? GLU A 213 ? LEU A 699 GLU A 707 1 ? 9  
HELX_P HELX_P7  AA7 SER A 219 ? ASP A 229 ? SER A 713 ASP A 723 1 ? 11 
HELX_P HELX_P8  AA8 SER A 239 ? LYS A 249 ? SER A 733 LYS A 743 1 ? 11 
HELX_P HELX_P9  AA9 TRP A 274 ? ASN A 288 ? TRP A 768 ASN A 782 1 ? 15 
HELX_P HELX_P10 AB1 GLY A 289 ? VAL A 299 ? GLY A 783 VAL A 793 1 ? 11 
HELX_P HELX_P11 AB2 GLY B 72  ? LYS B 86  ? GLY B 458 LYS B 472 1 ? 15 
HELX_P HELX_P12 AB3 ASN B 108 ? TYR B 116 ? ASN B 494 TYR B 502 1 ? 9  
HELX_P HELX_P13 AB4 ASN B 129 ? GLU B 134 ? ASN B 515 GLU B 520 1 ? 6  
HELX_P HELX_P14 AB5 ASP B 162 ? ARG B 167 ? ASP B 667 ARG B 672 1 ? 6  
HELX_P HELX_P15 AB6 PRO B 168 ? TYR B 171 ? PRO B 673 TYR B 676 5 ? 4  
HELX_P HELX_P16 AB7 GLY B 183 ? TYR B 193 ? GLY B 688 TYR B 698 1 ? 11 
HELX_P HELX_P17 AB8 TYR B 193 ? THR B 201 ? TYR B 698 THR B 706 1 ? 9  
HELX_P HELX_P18 AB9 LYS B 202 ? ASN B 204 ? LYS B 707 ASN B 709 5 ? 3  
HELX_P HELX_P19 AC1 GLY B 207 ? THR B 217 ? GLY B 712 THR B 722 1 ? 11 
HELX_P HELX_P20 AC2 ALA B 227 ? ARG B 236 ? ALA B 732 ARG B 741 1 ? 10 
HELX_P HELX_P21 AC3 ASP B 237 ? CYS B 240 ? ASP B 742 CYS B 745 5 ? 4  
HELX_P HELX_P22 AC4 ILE B 245 ? TYR B 249 ? ILE B 750 TYR B 754 1 ? 5  
HELX_P HELX_P23 AC5 TRP B 266 ? ASP B 280 ? TRP B 771 ASP B 785 1 ? 15 
HELX_P HELX_P24 AC6 GLY B 281 ? THR B 292 ? GLY B 786 THR B 797 1 ? 12 
# 
_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 ? ? A CYS 42  SG ? ? ? 1_555 A CYS 76  SG ? ? A CYS 420 A CYS 454 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
disulf2 disulf ? ? A CYS 58  SG ? ? ? 1_555 A CYS 77  SG ? ? A CYS 436 A CYS 455 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
disulf3 disulf ? ? B CYS 43  SG ? ? ? 1_555 B CYS 69  SG ? ? B CYS 429 B CYS 455 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
disulf4 disulf ? ? B CYS 50  SG ? ? ? 1_555 B CYS 70  SG ? ? B CYS 436 B CYS 456 1_555 ? ? ? ? ? ? ? 2.059 ? ? 
disulf5 disulf ? ? B CYS 240 SG ? ? ? 1_555 B CYS 295 SG ? ? B CYS 745 B CYS 800 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 A 42  ? CYS A 76  ? CYS A 420 ? 1_555 CYS A 454 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 58  ? CYS A 77  ? CYS A 436 ? 1_555 CYS A 455 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS B 43  ? CYS B 69  ? CYS B 429 ? 1_555 CYS B 455 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS B 50  ? CYS B 70  ? CYS B 436 ? 1_555 CYS B 456 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5 CYS B 240 ? CYS B 295 ? CYS B 745 ? 1_555 CYS B 800 ? 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 GLU 28  A . ? GLU 406 A PRO 29  A ? PRO 407 A 1 4.28  
2 ALA 28  B . ? ALA 414 B PRO 29  B ? PRO 415 B 1 3.13  
3 SER 172 B . ? SER 677 B PRO 173 B ? PRO 678 B 1 -5.88 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 8 ? 
AA6 ? 2 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
# 
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 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA5 6 7 ? anti-parallel 
AA5 7 8 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? 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 TYR A 32  ? PRO A 35  ? TYR A 410 PRO A 413 
AA1 2 THR A 72  ? TYR A 78  ? THR A 450 TYR A 456 
AA1 3 VAL A 56  ? PRO A 61  ? VAL A 434 PRO A 439 
AA1 4 TYR A 96  ? LEU A 100 ? TYR A 474 LEU A 478 
AA1 5 LEU A 20  ? THR A 24  ? LEU A 398 THR A 402 
AA1 6 MET A 134 ? ILE A 135 ? MET A 512 ILE A 513 
AA1 7 GLY A 267 ? MET A 268 ? GLY A 761 MET A 762 
AA1 8 GLU A 150 ? PHE A 151 ? GLU A 528 PHE A 529 
AA2 1 GLN A 109 ? GLU A 110 ? GLN A 487 GLU A 488 
AA2 2 GLU A 119 ? TRP A 120 ? GLU A 497 TRP A 498 
AA3 1 TYR A 187 ? ALA A 188 ? TYR A 681 ALA A 682 
AA3 2 ALA A 234 ? ASP A 238 ? ALA A 728 ASP A 732 
AA3 3 LYS A 156 ? LYS A 165 ? LYS A 534 LYS A 543 
AA3 4 LEU A 252 ? THR A 254 ? LEU A 746 THR A 748 
AA4 1 TYR A 187 ? ALA A 188 ? TYR A 681 ALA A 682 
AA4 2 ALA A 234 ? ASP A 238 ? ALA A 728 ASP A 732 
AA4 3 LYS A 156 ? LYS A 165 ? LYS A 534 LYS A 543 
AA4 4 PHE A 260 ? PHE A 264 ? PHE A 754 PHE A 758 
AA5 1 ILE B 32  ? GLU B 34  ? ILE B 418 GLU B 420 
AA5 2 GLY B 63  ? LYS B 71  ? GLY B 449 LYS B 457 
AA5 3 VAL B 48  ? LYS B 55  ? VAL B 434 LYS B 441 
AA5 4 THR B 88  ? LEU B 93  ? THR B 474 LEU B 479 
AA5 5 HIS B 19  ? THR B 24  ? HIS B 405 THR B 410 
AA5 6 MET B 121 ? ALA B 122 ? MET B 507 ALA B 508 
AA5 7 ALA B 259 ? GLN B 261 ? ALA B 764 GLN B 766 
AA5 8 VAL B 136 ? PHE B 138 ? VAL B 522 PHE B 524 
AA6 1 LYS B 102 ? VAL B 103 ? LYS B 488 VAL B 489 
AA6 2 VAL B 106 ? TRP B 107 ? VAL B 492 TRP B 493 
AA7 1 PHE B 177 ? GLY B 178 ? PHE B 682 GLY B 683 
AA7 2 ALA B 222 ? ASP B 226 ? ALA B 727 ASP B 731 
AA7 3 VAL B 143 ? SER B 152 ? VAL B 529 SER B 538 
AA7 4 LEU B 242 ? THR B 244 ? LEU B 747 THR B 749 
AA8 1 PHE B 177 ? GLY B 178 ? PHE B 682 GLY B 683 
AA8 2 ALA B 222 ? ASP B 226 ? ALA B 727 ASP B 731 
AA8 3 VAL B 143 ? SER B 152 ? VAL B 529 SER B 538 
AA8 4 PHE B 251 ? TYR B 256 ? PHE B 756 TYR B 761 
# 
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 TYR A 32  ? N TYR A 410 O TYR A 78  ? O TYR A 456 
AA1 2 3 O GLN A 75  ? O GLN A 453 N CYS A 58  ? N CYS A 436 
AA1 3 4 N THR A 59  ? N THR A 437 O LEU A 100 ? O LEU A 478 
AA1 4 5 O GLU A 97  ? O GLU A 475 N ILE A 22  ? N ILE A 400 
AA1 5 6 N VAL A 23  ? N VAL A 401 O MET A 134 ? O MET A 512 
AA1 6 7 N ILE A 135 ? N ILE A 513 O GLY A 267 ? O GLY A 761 
AA1 7 8 O MET A 268 ? O MET A 762 N GLU A 150 ? N GLU A 528 
AA2 1 2 N GLU A 110 ? N GLU A 488 O GLU A 119 ? O GLU A 497 
AA3 1 2 N ALA A 188 ? N ALA A 682 O ILE A 236 ? O ILE A 730 
AA3 2 3 O PHE A 235 ? O PHE A 729 N LEU A 163 ? N LEU A 541 
AA3 3 4 N VAL A 164 ? N VAL A 542 O VAL A 253 ? O VAL A 747 
AA4 1 2 N ALA A 188 ? N ALA A 682 O ILE A 236 ? O ILE A 730 
AA4 2 3 O PHE A 235 ? O PHE A 729 N LEU A 163 ? N LEU A 541 
AA4 3 4 N GLN A 158 ? N GLN A 536 O SER A 262 ? O SER A 756 
AA5 1 2 N ILE B 32  ? N ILE B 418 O LYS B 71  ? O LYS B 457 
AA5 2 3 O VAL B 66  ? O VAL B 452 N LYS B 52  ? N LYS B 438 
AA5 3 4 N ARG B 51  ? N ARG B 437 O LEU B 93  ? O LEU B 479 
AA5 4 5 O THR B 88  ? O THR B 474 N LEU B 20  ? N LEU B 406 
AA5 5 6 N VAL B 23  ? N VAL B 409 O MET B 121 ? O MET B 507 
AA5 6 7 N ALA B 122 ? N ALA B 508 O ALA B 259 ? O ALA B 764 
AA5 7 8 O LEU B 260 ? O LEU B 765 N ASP B 137 ? N ASP B 523 
AA6 1 2 N VAL B 103 ? N VAL B 489 O VAL B 106 ? O VAL B 492 
AA7 1 2 N GLY B 178 ? N GLY B 683 O ILE B 224 ? O ILE B 729 
AA7 2 3 O PHE B 223 ? O PHE B 728 N MET B 150 ? N MET B 536 
AA7 3 4 N VAL B 151 ? N VAL B 537 O VAL B 243 ? O VAL B 748 
AA8 1 2 N GLY B 178 ? N GLY B 683 O ILE B 224 ? O ILE B 729 
AA8 2 3 O PHE B 223 ? O PHE B 728 N MET B 150 ? N MET B 536 
AA8 3 4 N ILE B 147 ? N ILE B 533 O PHE B 251 ? O PHE B 756 
# 
_pdbx_entry_details.entry_id                   9MUM 
_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 
# 
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 GLN A 405 ? ? -171.59 88.06   
2 1 GLN A 536 ? ? -160.60 -142.89 
3 1 GLU A 751 ? ? -106.94 -164.73 
4 1 GLU B 413 ? ? -165.14 97.71   
5 1 ARG B 431 ? ? 56.17   -133.64 
6 1 LYS B 472 ? ? 71.05   68.75   
7 1 LYS B 484 ? ? -123.81 -113.99 
8 1 THR B 759 ? ? -155.52 -158.20 
# 
_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         -13.8920 
_pdbx_refine_tls.origin_y         -14.6113 
_pdbx_refine_tls.origin_z         25.5595 
_pdbx_refine_tls.T[1][1]          0.2378 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0062 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0091 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2234 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0052 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2797 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.7493 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0379 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.4291 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.5303 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0412 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.2597 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0379 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.1045 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0758 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0498 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0248 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0915 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0810 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0817 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0207 
_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_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1215 ? 6.06 . 
2 1 O ? A HOH 1216 ? 6.57 . 
3 1 O ? B HOH 1228 ? 5.82 . 
# 
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 MET 379 ? A MET 1   
2  1 Y 1 A HIS 380 ? A HIS 2   
3  1 Y 1 A HIS 381 ? A HIS 3   
4  1 Y 1 A HIS 382 ? A HIS 4   
5  1 Y 1 A HIS 383 ? A HIS 5   
6  1 Y 1 A HIS 384 ? A HIS 6   
7  1 Y 1 A HIS 385 ? A HIS 7   
8  1 Y 1 A GLU 386 ? A GLU 8   
9  1 Y 1 A ASN 387 ? A ASN 9   
10 1 Y 1 A LEU 388 ? A LEU 10  
11 1 Y 1 A TYR 389 ? A TYR 11  
12 1 Y 1 A PHE 390 ? A PHE 12  
13 1 Y 1 A GLN 391 ? A GLN 13  
14 1 Y 1 A GLY 392 ? A GLY 14  
15 1 Y 1 A SER 393 ? A SER 15  
16 1 Y 1 A MET 394 ? A MET 16  
17 1 Y 1 A SER 395 ? A SER 17  
18 1 Y 1 A THR 396 ? A THR 18  
19 1 Y 1 A ASP 441 ? A ASP 63  
20 1 Y 1 A THR 442 ? A THR 64  
21 1 Y 1 A SER 443 ? A SER 65  
22 1 Y 1 A PRO 444 ? A PRO 66  
23 1 Y 1 A GLY 445 ? A GLY 67  
24 1 Y 1 A ARG 489 ? A ARG 111 
25 1 Y 1 A VAL 490 ? A VAL 112 
26 1 Y 1 A ASN 491 ? A ASN 113 
27 1 Y 1 A ASN 492 ? A ASN 114 
28 1 Y 1 A SER 493 ? A SER 115 
29 1 Y 1 A GLN 796 ? A GLN 302 
30 1 Y 1 A GLU 797 ? A GLU 303 
31 1 Y 1 A CYS 798 ? A CYS 304 
32 1 Y 1 A ASP 799 ? A ASP 305 
33 1 Y 1 A SER 800 ? A SER 306 
34 1 Y 1 B MET 387 ? B MET 1   
35 1 Y 1 B HIS 388 ? B HIS 2   
36 1 Y 1 B HIS 389 ? B HIS 3   
37 1 Y 1 B HIS 390 ? B HIS 4   
38 1 Y 1 B HIS 391 ? B HIS 5   
39 1 Y 1 B HIS 392 ? B HIS 6   
40 1 Y 1 B HIS 393 ? B HIS 7   
41 1 Y 1 B GLU 394 ? B GLU 8   
42 1 Y 1 B ASN 395 ? B ASN 9   
43 1 Y 1 B LEU 396 ? B LEU 10  
44 1 Y 1 B TYR 397 ? B TYR 11  
45 1 Y 1 B PHE 398 ? B PHE 12  
46 1 Y 1 B GLN 399 ? B GLN 13  
47 1 Y 1 B GLY 400 ? B GLY 14  
48 1 Y 1 B PRO 401 ? B PRO 15  
49 1 Y 1 B ASP 402 ? B ASP 16  
50 1 Y 1 B ASP 423 ? B ASP 37  
51 1 Y 1 B PRO 424 ? B PRO 38  
52 1 Y 1 B LEU 425 ? B LEU 39  
53 1 Y 1 B THR 426 ? B THR 40  
54 1 Y 1 B HIS 801 ? B HIS 296 
55 1 Y 1 B ASN 802 ? B ASN 297 
# 
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 
A1BRB C10  C  Y N 1   
A1BRB C11  C  Y N 2   
A1BRB C13  C  Y N 3   
A1BRB C14  C  Y N 4   
A1BRB C16  C  Y N 5   
A1BRB C17  C  Y N 6   
A1BRB C2   C  N N 7   
A1BRB C20  C  N N 8   
A1BRB C21  C  N N 9   
A1BRB C24  C  Y N 10  
A1BRB C25  C  Y N 11  
A1BRB C26  C  Y N 12  
A1BRB C27  C  Y N 13  
A1BRB C28  C  Y N 14  
A1BRB C30  C  Y N 15  
A1BRB C4   C  N N 16  
A1BRB C5   C  N N 17  
A1BRB C6   C  N N 18  
A1BRB C7   C  Y N 19  
A1BRB C8   C  Y N 20  
A1BRB F22  F  N N 21  
A1BRB F23  F  N N 22  
A1BRB N12  N  Y N 23  
A1BRB N15  N  Y N 24  
A1BRB N18  N  Y N 25  
A1BRB N3   N  N N 26  
A1BRB N9   N  Y N 27  
A1BRB O1   O  N N 28  
A1BRB O19  O  N N 29  
A1BRB CL29 CL N N 30  
A1BRB H1   H  N N 31  
A1BRB H2   H  N N 32  
A1BRB H3   H  N N 33  
A1BRB H4   H  N N 34  
A1BRB H5   H  N N 35  
A1BRB H6   H  N N 36  
A1BRB H7   H  N N 37  
A1BRB H8   H  N N 38  
A1BRB H9   H  N N 39  
A1BRB H10  H  N N 40  
A1BRB H11  H  N N 41  
A1BRB H12  H  N N 42  
A1BRB H13  H  N N 43  
A1BRB H14  H  N N 44  
A1BRB H15  H  N N 45  
A1BRB H16  H  N N 46  
ALA   N    N  N N 47  
ALA   CA   C  N S 48  
ALA   C    C  N N 49  
ALA   O    O  N N 50  
ALA   CB   C  N N 51  
ALA   OXT  O  N N 52  
ALA   H    H  N N 53  
ALA   H2   H  N N 54  
ALA   HA   H  N N 55  
ALA   HB1  H  N N 56  
ALA   HB2  H  N N 57  
ALA   HB3  H  N N 58  
ALA   HXT  H  N N 59  
ARG   N    N  N N 60  
ARG   CA   C  N S 61  
ARG   C    C  N N 62  
ARG   O    O  N N 63  
ARG   CB   C  N N 64  
ARG   CG   C  N N 65  
ARG   CD   C  N N 66  
ARG   NE   N  N N 67  
ARG   CZ   C  N N 68  
ARG   NH1  N  N N 69  
ARG   NH2  N  N N 70  
ARG   OXT  O  N N 71  
ARG   H    H  N N 72  
ARG   H2   H  N N 73  
ARG   HA   H  N N 74  
ARG   HB2  H  N N 75  
ARG   HB3  H  N N 76  
ARG   HG2  H  N N 77  
ARG   HG3  H  N N 78  
ARG   HD2  H  N N 79  
ARG   HD3  H  N N 80  
ARG   HE   H  N N 81  
ARG   HH11 H  N N 82  
ARG   HH12 H  N N 83  
ARG   HH21 H  N N 84  
ARG   HH22 H  N N 85  
ARG   HXT  H  N N 86  
ASN   N    N  N N 87  
ASN   CA   C  N S 88  
ASN   C    C  N N 89  
ASN   O    O  N N 90  
ASN   CB   C  N N 91  
ASN   CG   C  N N 92  
ASN   OD1  O  N N 93  
ASN   ND2  N  N N 94  
ASN   OXT  O  N N 95  
ASN   H    H  N N 96  
ASN   H2   H  N N 97  
ASN   HA   H  N N 98  
ASN   HB2  H  N N 99  
ASN   HB3  H  N N 100 
ASN   HD21 H  N N 101 
ASN   HD22 H  N N 102 
ASN   HXT  H  N N 103 
ASP   N    N  N N 104 
ASP   CA   C  N S 105 
ASP   C    C  N N 106 
ASP   O    O  N N 107 
ASP   CB   C  N N 108 
ASP   CG   C  N N 109 
ASP   OD1  O  N N 110 
ASP   OD2  O  N N 111 
ASP   OXT  O  N N 112 
ASP   H    H  N N 113 
ASP   H2   H  N N 114 
ASP   HA   H  N N 115 
ASP   HB2  H  N N 116 
ASP   HB3  H  N N 117 
ASP   HD2  H  N N 118 
ASP   HXT  H  N N 119 
CYS   N    N  N N 120 
CYS   CA   C  N R 121 
CYS   C    C  N N 122 
CYS   O    O  N N 123 
CYS   CB   C  N N 124 
CYS   SG   S  N N 125 
CYS   OXT  O  N N 126 
CYS   H    H  N N 127 
CYS   H2   H  N N 128 
CYS   HA   H  N N 129 
CYS   HB2  H  N N 130 
CYS   HB3  H  N N 131 
CYS   HG   H  N N 132 
CYS   HXT  H  N N 133 
GLN   N    N  N N 134 
GLN   CA   C  N S 135 
GLN   C    C  N N 136 
GLN   O    O  N N 137 
GLN   CB   C  N N 138 
GLN   CG   C  N N 139 
GLN   CD   C  N N 140 
GLN   OE1  O  N N 141 
GLN   NE2  N  N N 142 
GLN   OXT  O  N N 143 
GLN   H    H  N N 144 
GLN   H2   H  N N 145 
GLN   HA   H  N N 146 
GLN   HB2  H  N N 147 
GLN   HB3  H  N N 148 
GLN   HG2  H  N N 149 
GLN   HG3  H  N N 150 
GLN   HE21 H  N N 151 
GLN   HE22 H  N N 152 
GLN   HXT  H  N N 153 
GLU   N    N  N N 154 
GLU   CA   C  N S 155 
GLU   C    C  N N 156 
GLU   O    O  N N 157 
GLU   CB   C  N N 158 
GLU   CG   C  N N 159 
GLU   CD   C  N N 160 
GLU   OE1  O  N N 161 
GLU   OE2  O  N N 162 
GLU   OXT  O  N N 163 
GLU   H    H  N N 164 
GLU   H2   H  N N 165 
GLU   HA   H  N N 166 
GLU   HB2  H  N N 167 
GLU   HB3  H  N N 168 
GLU   HG2  H  N N 169 
GLU   HG3  H  N N 170 
GLU   HE2  H  N N 171 
GLU   HXT  H  N N 172 
GLY   N    N  N N 173 
GLY   CA   C  N N 174 
GLY   C    C  N N 175 
GLY   O    O  N N 176 
GLY   OXT  O  N N 177 
GLY   H    H  N N 178 
GLY   H2   H  N N 179 
GLY   HA2  H  N N 180 
GLY   HA3  H  N N 181 
GLY   HXT  H  N N 182 
HIS   N    N  N N 183 
HIS   CA   C  N S 184 
HIS   C    C  N N 185 
HIS   O    O  N N 186 
HIS   CB   C  N N 187 
HIS   CG   C  Y N 188 
HIS   ND1  N  Y N 189 
HIS   CD2  C  Y N 190 
HIS   CE1  C  Y N 191 
HIS   NE2  N  Y N 192 
HIS   OXT  O  N N 193 
HIS   H    H  N N 194 
HIS   H2   H  N N 195 
HIS   HA   H  N N 196 
HIS   HB2  H  N N 197 
HIS   HB3  H  N N 198 
HIS   HD1  H  N N 199 
HIS   HD2  H  N N 200 
HIS   HE1  H  N N 201 
HIS   HE2  H  N N 202 
HIS   HXT  H  N N 203 
HOH   O    O  N N 204 
HOH   H1   H  N N 205 
HOH   H2   H  N N 206 
ILE   N    N  N N 207 
ILE   CA   C  N S 208 
ILE   C    C  N N 209 
ILE   O    O  N N 210 
ILE   CB   C  N S 211 
ILE   CG1  C  N N 212 
ILE   CG2  C  N N 213 
ILE   CD1  C  N N 214 
ILE   OXT  O  N N 215 
ILE   H    H  N N 216 
ILE   H2   H  N N 217 
ILE   HA   H  N N 218 
ILE   HB   H  N N 219 
ILE   HG12 H  N N 220 
ILE   HG13 H  N N 221 
ILE   HG21 H  N N 222 
ILE   HG22 H  N N 223 
ILE   HG23 H  N N 224 
ILE   HD11 H  N N 225 
ILE   HD12 H  N N 226 
ILE   HD13 H  N N 227 
ILE   HXT  H  N N 228 
LEU   N    N  N N 229 
LEU   CA   C  N S 230 
LEU   C    C  N N 231 
LEU   O    O  N N 232 
LEU   CB   C  N N 233 
LEU   CG   C  N N 234 
LEU   CD1  C  N N 235 
LEU   CD2  C  N N 236 
LEU   OXT  O  N N 237 
LEU   H    H  N N 238 
LEU   H2   H  N N 239 
LEU   HA   H  N N 240 
LEU   HB2  H  N N 241 
LEU   HB3  H  N N 242 
LEU   HG   H  N N 243 
LEU   HD11 H  N N 244 
LEU   HD12 H  N N 245 
LEU   HD13 H  N N 246 
LEU   HD21 H  N N 247 
LEU   HD22 H  N N 248 
LEU   HD23 H  N N 249 
LEU   HXT  H  N N 250 
LYS   N    N  N N 251 
LYS   CA   C  N S 252 
LYS   C    C  N N 253 
LYS   O    O  N N 254 
LYS   CB   C  N N 255 
LYS   CG   C  N N 256 
LYS   CD   C  N N 257 
LYS   CE   C  N N 258 
LYS   NZ   N  N N 259 
LYS   OXT  O  N N 260 
LYS   H    H  N N 261 
LYS   H2   H  N N 262 
LYS   HA   H  N N 263 
LYS   HB2  H  N N 264 
LYS   HB3  H  N N 265 
LYS   HG2  H  N N 266 
LYS   HG3  H  N N 267 
LYS   HD2  H  N N 268 
LYS   HD3  H  N N 269 
LYS   HE2  H  N N 270 
LYS   HE3  H  N N 271 
LYS   HZ1  H  N N 272 
LYS   HZ2  H  N N 273 
LYS   HZ3  H  N N 274 
LYS   HXT  H  N N 275 
MET   N    N  N N 276 
MET   CA   C  N S 277 
MET   C    C  N N 278 
MET   O    O  N N 279 
MET   CB   C  N N 280 
MET   CG   C  N N 281 
MET   SD   S  N N 282 
MET   CE   C  N N 283 
MET   OXT  O  N N 284 
MET   H    H  N N 285 
MET   H2   H  N N 286 
MET   HA   H  N N 287 
MET   HB2  H  N N 288 
MET   HB3  H  N N 289 
MET   HG2  H  N N 290 
MET   HG3  H  N N 291 
MET   HE1  H  N N 292 
MET   HE2  H  N N 293 
MET   HE3  H  N N 294 
MET   HXT  H  N N 295 
PHE   N    N  N N 296 
PHE   CA   C  N S 297 
PHE   C    C  N N 298 
PHE   O    O  N N 299 
PHE   CB   C  N N 300 
PHE   CG   C  Y N 301 
PHE   CD1  C  Y N 302 
PHE   CD2  C  Y N 303 
PHE   CE1  C  Y N 304 
PHE   CE2  C  Y N 305 
PHE   CZ   C  Y N 306 
PHE   OXT  O  N N 307 
PHE   H    H  N N 308 
PHE   H2   H  N N 309 
PHE   HA   H  N N 310 
PHE   HB2  H  N N 311 
PHE   HB3  H  N N 312 
PHE   HD1  H  N N 313 
PHE   HD2  H  N N 314 
PHE   HE1  H  N N 315 
PHE   HE2  H  N N 316 
PHE   HZ   H  N N 317 
PHE   HXT  H  N N 318 
PRO   N    N  N N 319 
PRO   CA   C  N S 320 
PRO   C    C  N N 321 
PRO   O    O  N N 322 
PRO   CB   C  N N 323 
PRO   CG   C  N N 324 
PRO   CD   C  N N 325 
PRO   OXT  O  N N 326 
PRO   H    H  N N 327 
PRO   HA   H  N N 328 
PRO   HB2  H  N N 329 
PRO   HB3  H  N N 330 
PRO   HG2  H  N N 331 
PRO   HG3  H  N N 332 
PRO   HD2  H  N N 333 
PRO   HD3  H  N N 334 
PRO   HXT  H  N N 335 
SER   N    N  N N 336 
SER   CA   C  N S 337 
SER   C    C  N N 338 
SER   O    O  N N 339 
SER   CB   C  N N 340 
SER   OG   O  N N 341 
SER   OXT  O  N N 342 
SER   H    H  N N 343 
SER   H2   H  N N 344 
SER   HA   H  N N 345 
SER   HB2  H  N N 346 
SER   HB3  H  N N 347 
SER   HG   H  N N 348 
SER   HXT  H  N N 349 
THR   N    N  N N 350 
THR   CA   C  N S 351 
THR   C    C  N N 352 
THR   O    O  N N 353 
THR   CB   C  N R 354 
THR   OG1  O  N N 355 
THR   CG2  C  N N 356 
THR   OXT  O  N N 357 
THR   H    H  N N 358 
THR   H2   H  N N 359 
THR   HA   H  N N 360 
THR   HB   H  N N 361 
THR   HG1  H  N N 362 
THR   HG21 H  N N 363 
THR   HG22 H  N N 364 
THR   HG23 H  N N 365 
THR   HXT  H  N N 366 
TRP   N    N  N N 367 
TRP   CA   C  N S 368 
TRP   C    C  N N 369 
TRP   O    O  N N 370 
TRP   CB   C  N N 371 
TRP   CG   C  Y N 372 
TRP   CD1  C  Y N 373 
TRP   CD2  C  Y N 374 
TRP   NE1  N  Y N 375 
TRP   CE2  C  Y N 376 
TRP   CE3  C  Y N 377 
TRP   CZ2  C  Y N 378 
TRP   CZ3  C  Y N 379 
TRP   CH2  C  Y N 380 
TRP   OXT  O  N N 381 
TRP   H    H  N N 382 
TRP   H2   H  N N 383 
TRP   HA   H  N N 384 
TRP   HB2  H  N N 385 
TRP   HB3  H  N N 386 
TRP   HD1  H  N N 387 
TRP   HE1  H  N N 388 
TRP   HE3  H  N N 389 
TRP   HZ2  H  N N 390 
TRP   HZ3  H  N N 391 
TRP   HH2  H  N N 392 
TRP   HXT  H  N N 393 
TYR   N    N  N N 394 
TYR   CA   C  N S 395 
TYR   C    C  N N 396 
TYR   O    O  N N 397 
TYR   CB   C  N N 398 
TYR   CG   C  Y N 399 
TYR   CD1  C  Y N 400 
TYR   CD2  C  Y N 401 
TYR   CE1  C  Y N 402 
TYR   CE2  C  Y N 403 
TYR   CZ   C  Y N 404 
TYR   OH   O  N N 405 
TYR   OXT  O  N N 406 
TYR   H    H  N N 407 
TYR   H2   H  N N 408 
TYR   HA   H  N N 409 
TYR   HB2  H  N N 410 
TYR   HB3  H  N N 411 
TYR   HD1  H  N N 412 
TYR   HD2  H  N N 413 
TYR   HE1  H  N N 414 
TYR   HE2  H  N N 415 
TYR   HH   H  N N 416 
TYR   HXT  H  N N 417 
VAL   N    N  N N 418 
VAL   CA   C  N S 419 
VAL   C    C  N N 420 
VAL   O    O  N N 421 
VAL   CB   C  N N 422 
VAL   CG1  C  N N 423 
VAL   CG2  C  N N 424 
VAL   OXT  O  N N 425 
VAL   H    H  N N 426 
VAL   H2   H  N N 427 
VAL   HA   H  N N 428 
VAL   HB   H  N N 429 
VAL   HG11 H  N N 430 
VAL   HG12 H  N N 431 
VAL   HG13 H  N N 432 
VAL   HG21 H  N N 433 
VAL   HG22 H  N N 434 
VAL   HG23 H  N N 435 
VAL   HXT  H  N N 436 
# 
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 
A1BRB CL29 C28  sing N N 1   
A1BRB N9   C10  doub Y N 2   
A1BRB N9   C8   sing Y N 3   
A1BRB C10  C11  sing Y N 4   
A1BRB C8   C7   doub Y N 5   
A1BRB C11  N12  doub Y N 6   
A1BRB F22  C21  sing N N 7   
A1BRB C6   C4   sing N N 8   
A1BRB C6   C5   sing N N 9   
A1BRB C30  C28  doub Y N 10  
A1BRB C30  C24  sing Y N 11  
A1BRB C28  C27  sing Y N 12  
A1BRB C7   N12  sing Y N 13  
A1BRB C7   C4   sing N N 14  
A1BRB C17  N18  doub Y N 15  
A1BRB C17  C16  sing Y N 16  
A1BRB N18  C13  sing Y N 17  
A1BRB N3   C4   sing N N 18  
A1BRB N3   C2   sing N N 19  
A1BRB C4   C5   sing N N 20  
A1BRB O19  C16  sing N N 21  
A1BRB O19  C20  sing N N 22  
A1BRB C21  C24  sing N N 23  
A1BRB C21  F23  sing N N 24  
A1BRB C21  C20  sing N N 25  
A1BRB C24  C25  doub Y N 26  
A1BRB C27  C26  doub Y N 27  
A1BRB C16  N15  doub Y N 28  
A1BRB C13  C2   sing N N 29  
A1BRB C13  C14  doub Y N 30  
A1BRB C2   O1   doub N N 31  
A1BRB C25  C26  sing Y N 32  
A1BRB N15  C14  sing Y N 33  
A1BRB C10  H1   sing N N 34  
A1BRB C11  H2   sing N N 35  
A1BRB C14  H3   sing N N 36  
A1BRB C17  H4   sing N N 37  
A1BRB C20  H5   sing N N 38  
A1BRB C20  H6   sing N N 39  
A1BRB C25  H7   sing N N 40  
A1BRB C26  H8   sing N N 41  
A1BRB C27  H9   sing N N 42  
A1BRB C30  H10  sing N N 43  
A1BRB C5   H11  sing N N 44  
A1BRB C5   H12  sing N N 45  
A1BRB C6   H13  sing N N 46  
A1BRB C6   H14  sing N N 47  
A1BRB C8   H15  sing N N 48  
A1BRB N3   H16  sing N N 49  
ALA   N    CA   sing N N 50  
ALA   N    H    sing N N 51  
ALA   N    H2   sing N N 52  
ALA   CA   C    sing N N 53  
ALA   CA   CB   sing N N 54  
ALA   CA   HA   sing N N 55  
ALA   C    O    doub N N 56  
ALA   C    OXT  sing N N 57  
ALA   CB   HB1  sing N N 58  
ALA   CB   HB2  sing N N 59  
ALA   CB   HB3  sing N N 60  
ALA   OXT  HXT  sing N N 61  
ARG   N    CA   sing N N 62  
ARG   N    H    sing N N 63  
ARG   N    H2   sing N N 64  
ARG   CA   C    sing N N 65  
ARG   CA   CB   sing N N 66  
ARG   CA   HA   sing N N 67  
ARG   C    O    doub N N 68  
ARG   C    OXT  sing N N 69  
ARG   CB   CG   sing N N 70  
ARG   CB   HB2  sing N N 71  
ARG   CB   HB3  sing N N 72  
ARG   CG   CD   sing N N 73  
ARG   CG   HG2  sing N N 74  
ARG   CG   HG3  sing N N 75  
ARG   CD   NE   sing N N 76  
ARG   CD   HD2  sing N N 77  
ARG   CD   HD3  sing N N 78  
ARG   NE   CZ   sing N N 79  
ARG   NE   HE   sing N N 80  
ARG   CZ   NH1  sing N N 81  
ARG   CZ   NH2  doub N N 82  
ARG   NH1  HH11 sing N N 83  
ARG   NH1  HH12 sing N N 84  
ARG   NH2  HH21 sing N N 85  
ARG   NH2  HH22 sing N N 86  
ARG   OXT  HXT  sing N N 87  
ASN   N    CA   sing N N 88  
ASN   N    H    sing N N 89  
ASN   N    H2   sing N N 90  
ASN   CA   C    sing N N 91  
ASN   CA   CB   sing N N 92  
ASN   CA   HA   sing N N 93  
ASN   C    O    doub N N 94  
ASN   C    OXT  sing N N 95  
ASN   CB   CG   sing N N 96  
ASN   CB   HB2  sing N N 97  
ASN   CB   HB3  sing N N 98  
ASN   CG   OD1  doub N N 99  
ASN   CG   ND2  sing N N 100 
ASN   ND2  HD21 sing N N 101 
ASN   ND2  HD22 sing N N 102 
ASN   OXT  HXT  sing N N 103 
ASP   N    CA   sing N N 104 
ASP   N    H    sing N N 105 
ASP   N    H2   sing N N 106 
ASP   CA   C    sing N N 107 
ASP   CA   CB   sing N N 108 
ASP   CA   HA   sing N N 109 
ASP   C    O    doub N N 110 
ASP   C    OXT  sing N N 111 
ASP   CB   CG   sing N N 112 
ASP   CB   HB2  sing N N 113 
ASP   CB   HB3  sing N N 114 
ASP   CG   OD1  doub N N 115 
ASP   CG   OD2  sing N N 116 
ASP   OD2  HD2  sing N N 117 
ASP   OXT  HXT  sing N N 118 
CYS   N    CA   sing N N 119 
CYS   N    H    sing N N 120 
CYS   N    H2   sing N N 121 
CYS   CA   C    sing N N 122 
CYS   CA   CB   sing N N 123 
CYS   CA   HA   sing N N 124 
CYS   C    O    doub N N 125 
CYS   C    OXT  sing N N 126 
CYS   CB   SG   sing N N 127 
CYS   CB   HB2  sing N N 128 
CYS   CB   HB3  sing N N 129 
CYS   SG   HG   sing N N 130 
CYS   OXT  HXT  sing N N 131 
GLN   N    CA   sing N N 132 
GLN   N    H    sing N N 133 
GLN   N    H2   sing N N 134 
GLN   CA   C    sing N N 135 
GLN   CA   CB   sing N N 136 
GLN   CA   HA   sing N N 137 
GLN   C    O    doub N N 138 
GLN   C    OXT  sing N N 139 
GLN   CB   CG   sing N N 140 
GLN   CB   HB2  sing N N 141 
GLN   CB   HB3  sing N N 142 
GLN   CG   CD   sing N N 143 
GLN   CG   HG2  sing N N 144 
GLN   CG   HG3  sing N N 145 
GLN   CD   OE1  doub N N 146 
GLN   CD   NE2  sing N N 147 
GLN   NE2  HE21 sing N N 148 
GLN   NE2  HE22 sing N N 149 
GLN   OXT  HXT  sing N N 150 
GLU   N    CA   sing N N 151 
GLU   N    H    sing N N 152 
GLU   N    H2   sing N N 153 
GLU   CA   C    sing N N 154 
GLU   CA   CB   sing N N 155 
GLU   CA   HA   sing N N 156 
GLU   C    O    doub N N 157 
GLU   C    OXT  sing N N 158 
GLU   CB   CG   sing N N 159 
GLU   CB   HB2  sing N N 160 
GLU   CB   HB3  sing N N 161 
GLU   CG   CD   sing N N 162 
GLU   CG   HG2  sing N N 163 
GLU   CG   HG3  sing N N 164 
GLU   CD   OE1  doub N N 165 
GLU   CD   OE2  sing N N 166 
GLU   OE2  HE2  sing N N 167 
GLU   OXT  HXT  sing N N 168 
GLY   N    CA   sing N N 169 
GLY   N    H    sing N N 170 
GLY   N    H2   sing N N 171 
GLY   CA   C    sing N N 172 
GLY   CA   HA2  sing N N 173 
GLY   CA   HA3  sing N N 174 
GLY   C    O    doub N N 175 
GLY   C    OXT  sing N N 176 
GLY   OXT  HXT  sing N N 177 
HIS   N    CA   sing N N 178 
HIS   N    H    sing N N 179 
HIS   N    H2   sing N N 180 
HIS   CA   C    sing N N 181 
HIS   CA   CB   sing N N 182 
HIS   CA   HA   sing N N 183 
HIS   C    O    doub N N 184 
HIS   C    OXT  sing N N 185 
HIS   CB   CG   sing N N 186 
HIS   CB   HB2  sing N N 187 
HIS   CB   HB3  sing N N 188 
HIS   CG   ND1  sing Y N 189 
HIS   CG   CD2  doub Y N 190 
HIS   ND1  CE1  doub Y N 191 
HIS   ND1  HD1  sing N N 192 
HIS   CD2  NE2  sing Y N 193 
HIS   CD2  HD2  sing N N 194 
HIS   CE1  NE2  sing Y N 195 
HIS   CE1  HE1  sing N N 196 
HIS   NE2  HE2  sing N N 197 
HIS   OXT  HXT  sing N N 198 
HOH   O    H1   sing N N 199 
HOH   O    H2   sing N N 200 
ILE   N    CA   sing N N 201 
ILE   N    H    sing N N 202 
ILE   N    H2   sing N N 203 
ILE   CA   C    sing N N 204 
ILE   CA   CB   sing N N 205 
ILE   CA   HA   sing N N 206 
ILE   C    O    doub N N 207 
ILE   C    OXT  sing N N 208 
ILE   CB   CG1  sing N N 209 
ILE   CB   CG2  sing N N 210 
ILE   CB   HB   sing N N 211 
ILE   CG1  CD1  sing N N 212 
ILE   CG1  HG12 sing N N 213 
ILE   CG1  HG13 sing N N 214 
ILE   CG2  HG21 sing N N 215 
ILE   CG2  HG22 sing N N 216 
ILE   CG2  HG23 sing N N 217 
ILE   CD1  HD11 sing N N 218 
ILE   CD1  HD12 sing N N 219 
ILE   CD1  HD13 sing N N 220 
ILE   OXT  HXT  sing N N 221 
LEU   N    CA   sing N N 222 
LEU   N    H    sing N N 223 
LEU   N    H2   sing N N 224 
LEU   CA   C    sing N N 225 
LEU   CA   CB   sing N N 226 
LEU   CA   HA   sing N N 227 
LEU   C    O    doub N N 228 
LEU   C    OXT  sing N N 229 
LEU   CB   CG   sing N N 230 
LEU   CB   HB2  sing N N 231 
LEU   CB   HB3  sing N N 232 
LEU   CG   CD1  sing N N 233 
LEU   CG   CD2  sing N N 234 
LEU   CG   HG   sing N N 235 
LEU   CD1  HD11 sing N N 236 
LEU   CD1  HD12 sing N N 237 
LEU   CD1  HD13 sing N N 238 
LEU   CD2  HD21 sing N N 239 
LEU   CD2  HD22 sing N N 240 
LEU   CD2  HD23 sing N N 241 
LEU   OXT  HXT  sing N N 242 
LYS   N    CA   sing N N 243 
LYS   N    H    sing N N 244 
LYS   N    H2   sing N N 245 
LYS   CA   C    sing N N 246 
LYS   CA   CB   sing N N 247 
LYS   CA   HA   sing N N 248 
LYS   C    O    doub N N 249 
LYS   C    OXT  sing N N 250 
LYS   CB   CG   sing N N 251 
LYS   CB   HB2  sing N N 252 
LYS   CB   HB3  sing N N 253 
LYS   CG   CD   sing N N 254 
LYS   CG   HG2  sing N N 255 
LYS   CG   HG3  sing N N 256 
LYS   CD   CE   sing N N 257 
LYS   CD   HD2  sing N N 258 
LYS   CD   HD3  sing N N 259 
LYS   CE   NZ   sing N N 260 
LYS   CE   HE2  sing N N 261 
LYS   CE   HE3  sing N N 262 
LYS   NZ   HZ1  sing N N 263 
LYS   NZ   HZ2  sing N N 264 
LYS   NZ   HZ3  sing N N 265 
LYS   OXT  HXT  sing N N 266 
MET   N    CA   sing N N 267 
MET   N    H    sing N N 268 
MET   N    H2   sing N N 269 
MET   CA   C    sing N N 270 
MET   CA   CB   sing N N 271 
MET   CA   HA   sing N N 272 
MET   C    O    doub N N 273 
MET   C    OXT  sing N N 274 
MET   CB   CG   sing N N 275 
MET   CB   HB2  sing N N 276 
MET   CB   HB3  sing N N 277 
MET   CG   SD   sing N N 278 
MET   CG   HG2  sing N N 279 
MET   CG   HG3  sing N N 280 
MET   SD   CE   sing N N 281 
MET   CE   HE1  sing N N 282 
MET   CE   HE2  sing N N 283 
MET   CE   HE3  sing N N 284 
MET   OXT  HXT  sing N N 285 
PHE   N    CA   sing N N 286 
PHE   N    H    sing N N 287 
PHE   N    H2   sing N N 288 
PHE   CA   C    sing N N 289 
PHE   CA   CB   sing N N 290 
PHE   CA   HA   sing N N 291 
PHE   C    O    doub N N 292 
PHE   C    OXT  sing N N 293 
PHE   CB   CG   sing N N 294 
PHE   CB   HB2  sing N N 295 
PHE   CB   HB3  sing N N 296 
PHE   CG   CD1  doub Y N 297 
PHE   CG   CD2  sing Y N 298 
PHE   CD1  CE1  sing Y N 299 
PHE   CD1  HD1  sing N N 300 
PHE   CD2  CE2  doub Y N 301 
PHE   CD2  HD2  sing N N 302 
PHE   CE1  CZ   doub Y N 303 
PHE   CE1  HE1  sing N N 304 
PHE   CE2  CZ   sing Y N 305 
PHE   CE2  HE2  sing N N 306 
PHE   CZ   HZ   sing N N 307 
PHE   OXT  HXT  sing N N 308 
PRO   N    CA   sing N N 309 
PRO   N    CD   sing N N 310 
PRO   N    H    sing N N 311 
PRO   CA   C    sing N N 312 
PRO   CA   CB   sing N N 313 
PRO   CA   HA   sing N N 314 
PRO   C    O    doub N N 315 
PRO   C    OXT  sing N N 316 
PRO   CB   CG   sing N N 317 
PRO   CB   HB2  sing N N 318 
PRO   CB   HB3  sing N N 319 
PRO   CG   CD   sing N N 320 
PRO   CG   HG2  sing N N 321 
PRO   CG   HG3  sing N N 322 
PRO   CD   HD2  sing N N 323 
PRO   CD   HD3  sing N N 324 
PRO   OXT  HXT  sing N N 325 
SER   N    CA   sing N N 326 
SER   N    H    sing N N 327 
SER   N    H2   sing N N 328 
SER   CA   C    sing N N 329 
SER   CA   CB   sing N N 330 
SER   CA   HA   sing N N 331 
SER   C    O    doub N N 332 
SER   C    OXT  sing N N 333 
SER   CB   OG   sing N N 334 
SER   CB   HB2  sing N N 335 
SER   CB   HB3  sing N N 336 
SER   OG   HG   sing N N 337 
SER   OXT  HXT  sing N N 338 
THR   N    CA   sing N N 339 
THR   N    H    sing N N 340 
THR   N    H2   sing N N 341 
THR   CA   C    sing N N 342 
THR   CA   CB   sing N N 343 
THR   CA   HA   sing N N 344 
THR   C    O    doub N N 345 
THR   C    OXT  sing N N 346 
THR   CB   OG1  sing N N 347 
THR   CB   CG2  sing N N 348 
THR   CB   HB   sing N N 349 
THR   OG1  HG1  sing N N 350 
THR   CG2  HG21 sing N N 351 
THR   CG2  HG22 sing N N 352 
THR   CG2  HG23 sing N N 353 
THR   OXT  HXT  sing N N 354 
TRP   N    CA   sing N N 355 
TRP   N    H    sing N N 356 
TRP   N    H2   sing N N 357 
TRP   CA   C    sing N N 358 
TRP   CA   CB   sing N N 359 
TRP   CA   HA   sing N N 360 
TRP   C    O    doub N N 361 
TRP   C    OXT  sing N N 362 
TRP   CB   CG   sing N N 363 
TRP   CB   HB2  sing N N 364 
TRP   CB   HB3  sing N N 365 
TRP   CG   CD1  doub Y N 366 
TRP   CG   CD2  sing Y N 367 
TRP   CD1  NE1  sing Y N 368 
TRP   CD1  HD1  sing N N 369 
TRP   CD2  CE2  doub Y N 370 
TRP   CD2  CE3  sing Y N 371 
TRP   NE1  CE2  sing Y N 372 
TRP   NE1  HE1  sing N N 373 
TRP   CE2  CZ2  sing Y N 374 
TRP   CE3  CZ3  doub Y N 375 
TRP   CE3  HE3  sing N N 376 
TRP   CZ2  CH2  doub Y N 377 
TRP   CZ2  HZ2  sing N N 378 
TRP   CZ3  CH2  sing Y N 379 
TRP   CZ3  HZ3  sing N N 380 
TRP   CH2  HH2  sing N N 381 
TRP   OXT  HXT  sing N N 382 
TYR   N    CA   sing N N 383 
TYR   N    H    sing N N 384 
TYR   N    H2   sing N N 385 
TYR   CA   C    sing N N 386 
TYR   CA   CB   sing N N 387 
TYR   CA   HA   sing N N 388 
TYR   C    O    doub N N 389 
TYR   C    OXT  sing N N 390 
TYR   CB   CG   sing N N 391 
TYR   CB   HB2  sing N N 392 
TYR   CB   HB3  sing N N 393 
TYR   CG   CD1  doub Y N 394 
TYR   CG   CD2  sing Y N 395 
TYR   CD1  CE1  sing Y N 396 
TYR   CD1  HD1  sing N N 397 
TYR   CD2  CE2  doub Y N 398 
TYR   CD2  HD2  sing N N 399 
TYR   CE1  CZ   doub Y N 400 
TYR   CE1  HE1  sing N N 401 
TYR   CE2  CZ   sing Y N 402 
TYR   CE2  HE2  sing N N 403 
TYR   CZ   OH   sing N N 404 
TYR   OH   HH   sing N N 405 
TYR   OXT  HXT  sing N N 406 
VAL   N    CA   sing N N 407 
VAL   N    H    sing N N 408 
VAL   N    H2   sing N N 409 
VAL   CA   C    sing N N 410 
VAL   CA   CB   sing N N 411 
VAL   CA   HA   sing N N 412 
VAL   C    O    doub N N 413 
VAL   C    OXT  sing N N 414 
VAL   CB   CG1  sing N N 415 
VAL   CB   CG2  sing N N 416 
VAL   CB   HB   sing N N 417 
VAL   CG1  HG11 sing N N 418 
VAL   CG1  HG12 sing N N 419 
VAL   CG1  HG13 sing N N 420 
VAL   CG2  HG21 sing N N 421 
VAL   CG2  HG22 sing N N 422 
VAL   CG2  HG23 sing N N 423 
VAL   OXT  HXT  sing N N 424 
# 
_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   5U8C 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9MUM 
_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]   0.018349 
_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]   0.011111 
_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]   0.008004 
_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 
C  
CL 
F  
N  
O  
S  
# 
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    . ARG   A 1 19  ? 14.559  -6.916  25.867  1.00 61.39  ? 397  ARG   A N    1 
ATOM   2    C  CA   . ARG   A 1 19  ? 14.339  -7.727  27.064  1.00 56.34  ? 397  ARG   A CA   1 
ATOM   3    C  C    . ARG   A 1 19  ? 13.185  -7.173  27.897  1.00 50.64  ? 397  ARG   A C    1 
ATOM   4    O  O    . ARG   A 1 19  ? 13.274  -6.064  28.426  1.00 53.84  ? 397  ARG   A O    1 
ATOM   5    C  CB   . ARG   A 1 19  ? 15.611  -7.798  27.913  1.00 54.55  ? 397  ARG   A CB   1 
ATOM   6    C  CG   . ARG   A 1 19  ? 15.512  -8.761  29.094  1.00 52.22  ? 397  ARG   A CG   1 
ATOM   7    C  CD   . ARG   A 1 19  ? 16.781  -9.593  29.229  1.00 58.82  ? 397  ARG   A CD   1 
ATOM   8    N  NE   . ARG   A 1 19  ? 17.107  -9.900  30.618  1.00 59.37  ? 397  ARG   A NE   1 
ATOM   9    C  CZ   . ARG   A 1 19  ? 17.221  -11.129 31.107  1.00 62.00  ? 397  ARG   A CZ   1 
ATOM   10   N  NH1  . ARG   A 1 19  ? 17.047  -12.197 30.345  1.00 60.70  ? 397  ARG   A NH1  1 
ATOM   11   N  NH2  . ARG   A 1 19  ? 17.530  -11.289 32.391  1.00 64.82  ? 397  ARG   A NH2  1 
ATOM   12   N  N    . LEU   A 1 20  ? 12.110  -7.952  28.027  1.00 47.51  ? 398  LEU   A N    1 
ATOM   13   C  CA   . LEU   A 1 20  ? 10.862  -7.444  28.591  1.00 47.72  ? 398  LEU   A CA   1 
ATOM   14   C  C    . LEU   A 1 20  ? 10.781  -7.730  30.085  1.00 45.60  ? 398  LEU   A C    1 
ATOM   15   O  O    . LEU   A 1 20  ? 11.071  -8.844  30.532  1.00 48.08  ? 398  LEU   A O    1 
ATOM   16   C  CB   . LEU   A 1 20  ? 9.653   -8.057  27.883  1.00 45.68  ? 398  LEU   A CB   1 
ATOM   17   C  CG   . LEU   A 1 20  ? 9.528   -7.761  26.393  1.00 48.44  ? 398  LEU   A CG   1 
ATOM   18   C  CD1  . LEU   A 1 20  ? 8.091   -7.988  25.922  1.00 48.93  ? 398  LEU   A CD1  1 
ATOM   19   C  CD2  . LEU   A 1 20  ? 10.039  -6.368  26.029  1.00 49.98  ? 398  LEU   A CD2  1 
ATOM   20   N  N    . LYS   A 1 21  ? 10.386  -6.718  30.850  1.00 39.83  ? 399  LYS   A N    1 
ATOM   21   C  CA   . LYS   A 1 21  ? 10.115  -6.863  32.275  1.00 41.81  ? 399  LYS   A CA   1 
ATOM   22   C  C    . LYS   A 1 21  ? 8.664   -7.310  32.429  1.00 41.02  ? 399  LYS   A C    1 
ATOM   23   O  O    . LYS   A 1 21  ? 7.736   -6.563  32.090  1.00 38.50  ? 399  LYS   A O    1 
ATOM   24   C  CB   . LYS   A 1 21  ? 10.385  -5.551  33.013  1.00 44.65  ? 399  LYS   A CB   1 
ATOM   25   C  CG   . LYS   A 1 21  ? 11.867  -5.133  33.027  1.00 48.57  ? 399  LYS   A CG   1 
ATOM   26   C  CD   . LYS   A 1 21  ? 12.069  -3.746  33.652  1.00 43.01  ? 399  LYS   A CD   1 
ATOM   27   C  CE   . LYS   A 1 21  ? 13.506  -3.229  33.437  1.00 55.88  ? 399  LYS   A CE   1 
ATOM   28   N  NZ   . LYS   A 1 21  ? 13.771  -2.600  32.103  1.00 60.80  ? 399  LYS   A NZ   1 
ATOM   29   N  N    . ILE   A 1 22  ? 8.469   -8.539  32.901  1.00 36.61  ? 400  ILE   A N    1 
ATOM   30   C  CA   . ILE   A 1 22  ? 7.136   -9.114  33.076  1.00 36.50  ? 400  ILE   A CA   1 
ATOM   31   C  C    . ILE   A 1 22  ? 6.746   -8.948  34.533  1.00 38.77  ? 400  ILE   A C    1 
ATOM   32   O  O    . ILE   A 1 22  ? 7.540   -9.246  35.433  1.00 40.12  ? 400  ILE   A O    1 
ATOM   33   C  CB   . ILE   A 1 22  ? 7.100   -10.601 32.679  1.00 35.98  ? 400  ILE   A CB   1 
ATOM   34   C  CG1  . ILE   A 1 22  ? 7.750   -10.810 31.314  1.00 40.20  ? 400  ILE   A CG1  1 
ATOM   35   C  CG2  . ILE   A 1 22  ? 5.631   -11.087 32.601  1.00 35.65  ? 400  ILE   A CG2  1 
ATOM   36   C  CD1  . ILE   A 1 22  ? 6.946   -10.221 30.180  1.00 41.84  ? 400  ILE   A CD1  1 
ATOM   37   N  N    . VAL   A 1 23  ? 5.541   -8.463  34.780  1.00 35.49  ? 401  VAL   A N    1 
ATOM   38   C  CA   . VAL   A 1 23  ? 5.020   -8.429  36.134  1.00 35.76  ? 401  VAL   A CA   1 
ATOM   39   C  C    . VAL   A 1 23  ? 3.903   -9.449  36.184  1.00 35.09  ? 401  VAL   A C    1 
ATOM   40   O  O    . VAL   A 1 23  ? 3.141   -9.607  35.222  1.00 34.34  ? 401  VAL   A O    1 
ATOM   41   C  CB   . VAL   A 1 23  ? 4.536   -7.033  36.585  1.00 37.43  ? 401  VAL   A CB   1 
ATOM   42   C  CG1  . VAL   A 1 23  ? 3.356   -6.539  35.745  1.00 36.22  ? 401  VAL   A CG1  1 
ATOM   43   C  CG2  . VAL   A 1 23  ? 4.186   -7.046  38.079  1.00 38.42  ? 401  VAL   A CG2  1 
ATOM   44   N  N    . THR   A 1 24  ? 3.844   -10.183 37.281  1.00 36.27  ? 402  THR   A N    1 
ATOM   45   C  CA   . THR   A 1 24  ? 2.752   -11.095 37.507  1.00 33.34  ? 402  THR   A CA   1 
ATOM   46   C  C    . THR   A 1 24  ? 2.411   -11.055 38.988  1.00 32.54  ? 402  THR   A C    1 
ATOM   47   O  O    . THR   A 1 24  ? 2.874   -10.185 39.727  1.00 32.54  ? 402  THR   A O    1 
ATOM   48   C  CB   . THR   A 1 24  ? 3.096   -12.500 37.001  1.00 32.86  ? 402  THR   A CB   1 
ATOM   49   O  OG1  . THR   A 1 24  ? 1.915   -13.300 37.064  1.00 34.20  ? 402  THR   A OG1  1 
ATOM   50   C  CG2  . THR   A 1 24  ? 4.213   -13.126 37.816  1.00 37.11  ? 402  THR   A CG2  1 
ATOM   51   N  N    . ILE   A 1 25  ? 1.550   -11.978 39.408  1.00 33.01  ? 403  ILE   A N    1 
ATOM   52   C  CA   . ILE   A 1 25  ? 1.003   -11.974 40.754  1.00 30.94  ? 403  ILE   A CA   1 
ATOM   53   C  C    . ILE   A 1 25  ? 0.739   -13.419 41.149  1.00 34.25  ? 403  ILE   A C    1 
ATOM   54   O  O    . ILE   A 1 25  ? 0.423   -14.258 40.303  1.00 34.04  ? 403  ILE   A O    1 
ATOM   55   C  CB   . ILE   A 1 25  ? -0.286  -11.111 40.793  1.00 31.01  ? 403  ILE   A CB   1 
ATOM   56   C  CG1  . ILE   A 1 25  ? -0.761  -10.880 42.215  1.00 30.34  ? 403  ILE   A CG1  1 
ATOM   57   C  CG2  . ILE   A 1 25  ? -1.381  -11.752 39.952  1.00 29.32  ? 403  ILE   A CG2  1 
ATOM   58   C  CD1  . ILE   A 1 25  ? -1.965  -9.952  42.269  1.00 31.30  ? 403  ILE   A CD1  1 
ATOM   59   N  N    . HIS   A 1 26  ? 0.871   -13.712 42.442  1.00 30.88  ? 404  HIS   A N    1 
ATOM   60   C  CA   . HIS   A 1 26  ? 0.512   -15.033 42.943  1.00 31.96  ? 404  HIS   A CA   1 
ATOM   61   C  C    . HIS   A 1 26  ? -0.991  -15.285 42.750  1.00 36.79  ? 404  HIS   A C    1 
ATOM   62   O  O    . HIS   A 1 26  ? -1.831  -14.489 43.195  1.00 35.87  ? 404  HIS   A O    1 
ATOM   63   C  CB   . HIS   A 1 26  ? 0.917   -15.156 44.411  1.00 38.85  ? 404  HIS   A CB   1 
ATOM   64   C  CG   . HIS   A 1 26  ? 0.651   -16.507 45.002  1.00 44.18  ? 404  HIS   A CG   1 
ATOM   65   N  ND1  . HIS   A 1 26  ? 0.037   -16.680 46.224  1.00 47.15  ? 404  HIS   A ND1  1 
ATOM   66   C  CD2  . HIS   A 1 26  ? 0.896   -17.752 44.525  1.00 41.50  ? 404  HIS   A CD2  1 
ATOM   67   C  CE1  . HIS   A 1 26  ? -0.069  -17.974 46.483  1.00 49.70  ? 404  HIS   A CE1  1 
ATOM   68   N  NE2  . HIS   A 1 26  ? 0.444   -18.646 45.468  1.00 44.10  ? 404  HIS   A NE2  1 
ATOM   69   N  N    . GLN   A 1 27  ? -1.336  -16.389 42.078  1.00 32.80  ? 405  GLN   A N    1 
ATOM   70   C  CA   . GLN   A 1 27  ? -2.751  -16.715 41.871  1.00 34.85  ? 405  GLN   A CA   1 
ATOM   71   C  C    . GLN   A 1 27  ? -2.904  -18.105 41.270  1.00 33.62  ? 405  GLN   A C    1 
ATOM   72   O  O    . GLN   A 1 27  ? -2.938  -18.260 40.045  1.00 30.65  ? 405  GLN   A O    1 
ATOM   73   C  CB   . GLN   A 1 27  ? -3.435  -15.658 40.982  1.00 30.46  ? 405  GLN   A CB   1 
ATOM   74   C  CG   . GLN   A 1 27  ? -4.966  -15.671 40.975  1.00 31.79  ? 405  GLN   A CG   1 
ATOM   75   C  CD   . GLN   A 1 27  ? -5.619  -14.979 42.173  1.00 36.99  ? 405  GLN   A CD   1 
ATOM   76   O  OE1  . GLN   A 1 27  ? -6.841  -15.052 42.331  1.00 39.79  ? 405  GLN   A OE1  1 
ATOM   77   N  NE2  . GLN   A 1 27  ? -4.820  -14.304 43.012  1.00 31.90  ? 405  GLN   A NE2  1 
ATOM   78   N  N    . GLU   A 1 28  ? -2.976  -19.119 42.129  1.00 35.07  ? 406  GLU   A N    1 
ATOM   79   C  CA   . GLU   A 1 28  ? -3.126  -20.487 41.656  1.00 32.15  ? 406  GLU   A CA   1 
ATOM   80   C  C    . GLU   A 1 28  ? -4.494  -20.653 40.995  1.00 33.54  ? 406  GLU   A C    1 
ATOM   81   O  O    . GLU   A 1 28  ? -5.474  -20.087 41.471  1.00 32.90  ? 406  GLU   A O    1 
ATOM   82   C  CB   . GLU   A 1 28  ? -2.958  -21.471 42.825  1.00 33.82  ? 406  GLU   A CB   1 
ATOM   83   C  CG   . GLU   A 1 28  ? -1.603  -21.338 43.525  1.00 39.59  ? 406  GLU   A CG   1 
ATOM   84   C  CD   . GLU   A 1 28  ? -1.395  -22.341 44.653  1.00 43.54  ? 406  GLU   A CD   1 
ATOM   85   O  OE1  . GLU   A 1 28  ? -2.280  -23.192 44.888  1.00 44.11  ? 406  GLU   A OE1  1 
ATOM   86   O  OE2  . GLU   A 1 28  ? -0.331  -22.280 45.294  1.00 48.59  ? 406  GLU   A OE2  1 
ATOM   87   N  N    . PRO   A 1 29  ? -4.594  -21.410 39.877  1.00 32.26  ? 407  PRO   A N    1 
ATOM   88   C  CA   . PRO   A 1 29  ? -3.549  -22.200 39.218  1.00 34.32  ? 407  PRO   A CA   1 
ATOM   89   C  C    . PRO   A 1 29  ? -2.833  -21.451 38.105  1.00 35.03  ? 407  PRO   A C    1 
ATOM   90   O  O    . PRO   A 1 29  ? -2.090  -22.048 37.321  1.00 32.37  ? 407  PRO   A O    1 
ATOM   91   C  CB   . PRO   A 1 29  ? -4.339  -23.399 38.675  1.00 36.18  ? 407  PRO   A CB   1 
ATOM   92   C  CG   . PRO   A 1 29  ? -5.697  -22.779 38.287  1.00 31.86  ? 407  PRO   A CG   1 
ATOM   93   C  CD   . PRO   A 1 29  ? -5.916  -21.617 39.238  1.00 31.97  ? 407  PRO   A CD   1 
ATOM   94   N  N    . PHE   A 1 30  ? -3.042  -20.138 37.998  1.00 32.52  ? 408  PHE   A N    1 
ATOM   95   C  CA   . PHE   A 1 30  ? -2.403  -19.418 36.915  1.00 30.26  ? 408  PHE   A CA   1 
ATOM   96   C  C    . PHE   A 1 30  ? -0.942  -19.109 37.233  1.00 35.12  ? 408  PHE   A C    1 
ATOM   97   O  O    . PHE   A 1 30  ? -0.091  -19.177 36.341  1.00 34.62  ? 408  PHE   A O    1 
ATOM   98   C  CB   . PHE   A 1 30  ? -3.194  -18.144 36.610  1.00 28.04  ? 408  PHE   A CB   1 
ATOM   99   C  CG   . PHE   A 1 30  ? -4.575  -18.435 36.121  1.00 32.31  ? 408  PHE   A CG   1 
ATOM   100  C  CD1  . PHE   A 1 30  ? -4.818  -18.643 34.782  1.00 31.98  ? 408  PHE   A CD1  1 
ATOM   101  C  CD2  . PHE   A 1 30  ? -5.626  -18.567 37.025  1.00 31.11  ? 408  PHE   A CD2  1 
ATOM   102  C  CE1  . PHE   A 1 30  ? -6.094  -18.952 34.335  1.00 34.77  ? 408  PHE   A CE1  1 
ATOM   103  C  CE2  . PHE   A 1 30  ? -6.885  -18.872 36.587  1.00 33.08  ? 408  PHE   A CE2  1 
ATOM   104  C  CZ   . PHE   A 1 30  ? -7.123  -19.063 35.236  1.00 34.15  ? 408  PHE   A CZ   1 
ATOM   105  N  N    . VAL   A 1 31  ? -0.625  -18.753 38.482  1.00 29.60  ? 409  VAL   A N    1 
ATOM   106  C  CA   . VAL   A 1 31  ? 0.756   -18.469 38.860  1.00 30.40  ? 409  VAL   A CA   1 
ATOM   107  C  C    . VAL   A 1 31  ? 0.980   -19.053 40.246  1.00 34.58  ? 409  VAL   A C    1 
ATOM   108  O  O    . VAL   A 1 31  ? 0.420   -18.548 41.229  1.00 34.33  ? 409  VAL   A O    1 
ATOM   109  C  CB   . VAL   A 1 31  ? 1.070   -16.959 38.856  1.00 33.54  ? 409  VAL   A CB   1 
ATOM   110  C  CG1  . VAL   A 1 31  ? 2.515   -16.706 39.316  1.00 36.46  ? 409  VAL   A CG1  1 
ATOM   111  C  CG2  . VAL   A 1 31  ? 0.793   -16.346 37.482  1.00 31.94  ? 409  VAL   A CG2  1 
ATOM   112  N  N    . TYR   A 1 32  ? 1.775   -20.128 40.322  1.00 30.93  ? 410  TYR   A N    1 
ATOM   113  C  CA   . TYR   A 1 32  ? 2.304   -20.661 41.570  1.00 33.15  ? 410  TYR   A CA   1 
ATOM   114  C  C    . TYR   A 1 32  ? 3.597   -19.932 41.929  1.00 33.91  ? 410  TYR   A C    1 
ATOM   115  O  O    . TYR   A 1 32  ? 4.372   -19.577 41.043  1.00 32.69  ? 410  TYR   A O    1 
ATOM   116  C  CB   . TYR   A 1 32  ? 2.585   -22.159 41.427  1.00 32.40  ? 410  TYR   A CB   1 
ATOM   117  C  CG   . TYR   A 1 32  ? 1.348   -23.019 41.273  1.00 34.77  ? 410  TYR   A CG   1 
ATOM   118  C  CD1  . TYR   A 1 32  ? 0.687   -23.119 40.053  1.00 28.82  ? 410  TYR   A CD1  1 
ATOM   119  C  CD2  . TYR   A 1 32  ? 0.854   -23.756 42.354  1.00 33.69  ? 410  TYR   A CD2  1 
ATOM   120  C  CE1  . TYR   A 1 32  ? -0.449  -23.904 39.930  1.00 33.69  ? 410  TYR   A CE1  1 
ATOM   121  C  CE2  . TYR   A 1 32  ? -0.276  -24.548 42.228  1.00 35.34  ? 410  TYR   A CE2  1 
ATOM   122  C  CZ   . TYR   A 1 32  ? -0.924  -24.615 41.017  1.00 35.00  ? 410  TYR   A CZ   1 
ATOM   123  O  OH   . TYR   A 1 32  ? -2.055  -25.405 40.882  1.00 34.48  ? 410  TYR   A OH   1 
ATOM   124  N  N    . VAL   A 1 33  ? 3.827   -19.715 43.230  1.00 31.18  ? 411  VAL   A N    1 
ATOM   125  C  CA   . VAL   A 1 33  ? 5.044   -19.079 43.736  1.00 39.00  ? 411  VAL   A CA   1 
ATOM   126  C  C    . VAL   A 1 33  ? 5.577   -19.947 44.871  1.00 43.97  ? 411  VAL   A C    1 
ATOM   127  O  O    . VAL   A 1 33  ? 4.859   -20.217 45.843  1.00 41.29  ? 411  VAL   A O    1 
ATOM   128  C  CB   . VAL   A 1 33  ? 4.806   -17.636 44.219  1.00 42.68  ? 411  VAL   A CB   1 
ATOM   129  C  CG1  . VAL   A 1 33  ? 6.113   -17.016 44.714  1.00 41.81  ? 411  VAL   A CG1  1 
ATOM   130  C  CG2  . VAL   A 1 33  ? 4.202   -16.797 43.108  1.00 36.30  ? 411  VAL   A CG2  1 
ATOM   131  N  N    . LYS   A 1 34  ? 6.808   -20.418 44.720  1.00 36.04  ? 412  LYS   A N    1 
ATOM   132  C  CA   . LYS   A 1 34  ? 7.442   -21.319 45.666  1.00 39.38  ? 412  LYS   A CA   1 
ATOM   133  C  C    . LYS   A 1 34  ? 8.846   -20.820 45.950  1.00 41.61  ? 412  LYS   A C    1 
ATOM   134  O  O    . LYS   A 1 34  ? 9.464   -20.196 45.086  1.00 40.38  ? 412  LYS   A O    1 
ATOM   135  C  CB   . LYS   A 1 34  ? 7.508   -22.751 45.113  1.00 36.71  ? 412  LYS   A CB   1 
ATOM   136  C  CG   . LYS   A 1 34  ? 6.129   -23.401 44.863  1.00 37.63  ? 412  LYS   A CG   1 
ATOM   137  C  CD   . LYS   A 1 34  ? 5.293   -23.437 46.137  1.00 39.81  ? 412  LYS   A CD   1 
ATOM   138  C  CE   . LYS   A 1 34  ? 3.909   -24.027 45.862  1.00 43.27  ? 412  LYS   A CE   1 
ATOM   139  N  NZ   . LYS   A 1 34  ? 3.052   -24.070 47.086  1.00 49.41  ? 412  LYS   A NZ   1 
ATOM   140  N  N    . PRO   A 1 35  ? 9.375   -21.088 47.144  1.00 45.53  ? 413  PRO   A N    1 
ATOM   141  C  CA   . PRO   A 1 35  ? 10.766  -20.724 47.439  1.00 40.97  ? 413  PRO   A CA   1 
ATOM   142  C  C    . PRO   A 1 35  ? 11.744  -21.494 46.565  1.00 44.93  ? 413  PRO   A C    1 
ATOM   143  O  O    . PRO   A 1 35  ? 11.497  -22.637 46.179  1.00 41.08  ? 413  PRO   A O    1 
ATOM   144  C  CB   . PRO   A 1 35  ? 10.932  -21.117 48.915  1.00 44.28  ? 413  PRO   A CB   1 
ATOM   145  C  CG   . PRO   A 1 35  ? 9.529   -21.195 49.461  1.00 46.22  ? 413  PRO   A CG   1 
ATOM   146  C  CD   . PRO   A 1 35  ? 8.691   -21.680 48.308  1.00 42.79  ? 413  PRO   A CD   1 
ATOM   147  N  N    . THR   A 1 36  ? 12.880  -20.863 46.266  1.00 45.82  ? 414  THR   A N    1 
ATOM   148  C  CA   . THR   A 1 36  ? 13.944  -21.583 45.576  1.00 45.52  ? 414  THR   A CA   1 
ATOM   149  C  C    . THR   A 1 36  ? 14.562  -22.624 46.502  1.00 47.21  ? 414  THR   A C    1 
ATOM   150  O  O    . THR   A 1 36  ? 14.424  -22.570 47.724  1.00 48.99  ? 414  THR   A O    1 
ATOM   151  C  CB   . THR   A 1 36  ? 15.074  -20.653 45.128  1.00 48.21  ? 414  THR   A CB   1 
ATOM   152  O  OG1  . THR   A 1 36  ? 15.707  -20.099 46.285  1.00 42.03  ? 414  THR   A OG1  1 
ATOM   153  C  CG2  . THR   A 1 36  ? 14.525  -19.513 44.276  1.00 48.72  ? 414  THR   A CG2  1 
ATOM   154  N  N    . LEU   A 1 37  ? 15.285  -23.558 45.903  1.00 48.17  ? 415  LEU   A N    1 
ATOM   155  C  CA   . LEU   A 1 37  ? 16.113  -24.458 46.688  1.00 53.92  ? 415  LEU   A CA   1 
ATOM   156  C  C    . LEU   A 1 37  ? 17.293  -23.686 47.288  1.00 57.79  ? 415  LEU   A C    1 
ATOM   157  O  O    . LEU   A 1 37  ? 17.527  -22.519 46.965  1.00 56.59  ? 415  LEU   A O    1 
ATOM   158  C  CB   . LEU   A 1 37  ? 16.600  -25.605 45.810  1.00 54.60  ? 415  LEU   A CB   1 
ATOM   159  C  CG   . LEU   A 1 37  ? 15.529  -26.687 45.621  1.00 58.31  ? 415  LEU   A CG   1 
ATOM   160  C  CD1  . LEU   A 1 37  ? 16.115  -27.858 44.848  1.00 58.01  ? 415  LEU   A CD1  1 
ATOM   161  C  CD2  . LEU   A 1 37  ? 14.941  -27.124 46.960  1.00 61.31  ? 415  LEU   A CD2  1 
ATOM   162  N  N    . SER   A 1 38  ? 18.058  -24.355 48.168  1.00 55.26  ? 416  SER   A N    1 
ATOM   163  C  CA   . SER   A 1 38  ? 19.179  -23.689 48.832  1.00 57.44  ? 416  SER   A CA   1 
ATOM   164  C  C    . SER   A 1 38  ? 20.225  -23.191 47.848  1.00 60.13  ? 416  SER   A C    1 
ATOM   165  O  O    . SER   A 1 38  ? 21.016  -22.309 48.193  1.00 62.94  ? 416  SER   A O    1 
ATOM   166  C  CB   . SER   A 1 38  ? 19.862  -24.626 49.839  1.00 54.90  ? 416  SER   A CB   1 
ATOM   167  N  N    . ASP   A 1 39  ? 20.274  -23.747 46.643  1.00 56.89  ? 417  ASP   A N    1 
ATOM   168  C  CA   . ASP   A 1 39  ? 21.267  -23.340 45.662  1.00 58.52  ? 417  ASP   A CA   1 
ATOM   169  C  C    . ASP   A 1 39  ? 20.706  -22.363 44.635  1.00 57.95  ? 417  ASP   A C    1 
ATOM   170  O  O    . ASP   A 1 39  ? 21.326  -22.145 43.589  1.00 53.82  ? 417  ASP   A O    1 
ATOM   171  C  CB   . ASP   A 1 39  ? 21.836  -24.576 44.975  1.00 59.74  ? 417  ASP   A CB   1 
ATOM   172  C  CG   . ASP   A 1 39  ? 20.785  -25.342 44.226  1.00 59.38  ? 417  ASP   A CG   1 
ATOM   173  O  OD1  . ASP   A 1 39  ? 19.586  -25.134 44.527  1.00 59.70  ? 417  ASP   A OD1  1 
ATOM   174  O  OD2  . ASP   A 1 39  ? 21.153  -26.175 43.370  1.00 61.52  ? 417  ASP   A OD2  1 
ATOM   175  N  N    . GLY   A 1 40  ? 19.538  -21.788 44.899  1.00 53.72  ? 418  GLY   A N    1 
ATOM   176  C  CA   . GLY   A 1 40  ? 18.987  -20.795 44.014  1.00 52.64  ? 418  GLY   A CA   1 
ATOM   177  C  C    . GLY   A 1 40  ? 18.199  -21.336 42.849  1.00 52.80  ? 418  GLY   A C    1 
ATOM   178  O  O    . GLY   A 1 40  ? 17.597  -20.542 42.115  1.00 50.20  ? 418  GLY   A O    1 
ATOM   179  N  N    . THR   A 1 41  ? 18.159  -22.651 42.657  1.00 51.43  ? 419  THR   A N    1 
ATOM   180  C  CA   . THR   A 1 41  ? 17.415  -23.233 41.550  1.00 46.40  ? 419  THR   A CA   1 
ATOM   181  C  C    . THR   A 1 41  ? 16.039  -23.701 42.020  1.00 49.87  ? 419  THR   A C    1 
ATOM   182  O  O    . THR   A 1 41  ? 15.743  -23.762 43.222  1.00 49.42  ? 419  THR   A O    1 
ATOM   183  C  CB   . THR   A 1 41  ? 18.182  -24.403 40.927  1.00 51.68  ? 419  THR   A CB   1 
ATOM   184  O  OG1  . THR   A 1 41  ? 18.253  -25.486 41.866  1.00 52.53  ? 419  THR   A OG1  1 
ATOM   185  C  CG2  . THR   A 1 41  ? 19.601  -23.960 40.594  1.00 56.90  ? 419  THR   A CG2  1 
ATOM   186  N  N    . CYS   A 1 42  ? 15.198  -24.043 41.041  1.00 44.80  ? 420  CYS   A N    1 
ATOM   187  C  CA   . CYS   A 1 42  ? 13.825  -24.474 41.271  1.00 43.01  ? 420  CYS   A CA   1 
ATOM   188  C  C    . CYS   A 1 42  ? 13.716  -25.987 41.131  1.00 47.09  ? 420  CYS   A C    1 
ATOM   189  O  O    . CYS   A 1 42  ? 14.226  -26.564 40.172  1.00 47.58  ? 420  CYS   A O    1 
ATOM   190  C  CB   . CYS   A 1 42  ? 12.881  -23.806 40.282  1.00 44.38  ? 420  CYS   A CB   1 
ATOM   191  S  SG   . CYS   A 1 42  ? 12.831  -22.039 40.415  1.00 50.20  ? 420  CYS   A SG   1 
ATOM   192  N  N    . LYS   A 1 43  ? 13.019  -26.614 42.078  1.00 45.44  ? 421  LYS   A N    1 
ATOM   193  C  CA   . LYS   A 1 43  ? 12.961  -28.068 42.134  1.00 49.87  ? 421  LYS   A CA   1 
ATOM   194  C  C    . LYS   A 1 43  ? 12.314  -28.638 40.877  1.00 48.64  ? 421  LYS   A C    1 
ATOM   195  O  O    . LYS   A 1 43  ? 11.356  -28.079 40.344  1.00 47.74  ? 421  LYS   A O    1 
ATOM   196  C  CB   . LYS   A 1 43  ? 12.186  -28.511 43.373  1.00 53.34  ? 421  LYS   A CB   1 
ATOM   197  C  CG   . LYS   A 1 43  ? 12.666  -29.848 43.969  1.00 57.65  ? 421  LYS   A CG   1 
ATOM   198  C  CD   . LYS   A 1 43  ? 11.608  -30.924 43.832  1.00 60.58  ? 421  LYS   A CD   1 
ATOM   199  C  CE   . LYS   A 1 43  ? 10.549  -30.778 44.917  1.00 67.23  ? 421  LYS   A CE   1 
ATOM   200  N  NZ   . LYS   A 1 43  ? 9.657   -31.971 45.027  1.00 72.58  ? 421  LYS   A NZ   1 
ATOM   201  N  N    . GLU   A 1 44  ? 12.858  -29.755 40.399  1.00 50.36  ? 422  GLU   A N    1 
ATOM   202  C  CA   . GLU   A 1 44  ? 12.346  -30.419 39.203  1.00 52.49  ? 422  GLU   A CA   1 
ATOM   203  C  C    . GLU   A 1 44  ? 11.045  -31.141 39.538  1.00 52.17  ? 422  GLU   A C    1 
ATOM   204  O  O    . GLU   A 1 44  ? 11.033  -32.022 40.402  1.00 52.89  ? 422  GLU   A O    1 
ATOM   205  C  CB   . GLU   A 1 44  ? 13.380  -31.408 38.668  1.00 58.62  ? 422  GLU   A CB   1 
ATOM   206  C  CG   . GLU   A 1 44  ? 13.081  -31.938 37.269  1.00 65.75  ? 422  GLU   A CG   1 
ATOM   207  C  CD   . GLU   A 1 44  ? 14.014  -33.072 36.851  1.00 74.61  ? 422  GLU   A CD   1 
ATOM   208  O  OE1  . GLU   A 1 44  ? 15.027  -33.311 37.550  1.00 77.20  ? 422  GLU   A OE1  1 
ATOM   209  O  OE2  . GLU   A 1 44  ? 13.736  -33.719 35.817  1.00 77.95  ? 422  GLU   A OE2  1 
ATOM   210  N  N    . GLU   A 1 45  ? 9.954   -30.768 38.865  1.00 51.61  ? 423  GLU   A N    1 
ATOM   211  C  CA   . GLU   A 1 45  ? 8.641   -31.365 39.072  1.00 48.04  ? 423  GLU   A CA   1 
ATOM   212  C  C    . GLU   A 1 45  ? 8.007   -31.681 37.722  1.00 49.67  ? 423  GLU   A C    1 
ATOM   213  O  O    . GLU   A 1 45  ? 8.435   -31.174 36.682  1.00 46.99  ? 423  GLU   A O    1 
ATOM   214  C  CB   . GLU   A 1 45  ? 7.720   -30.435 39.877  1.00 51.96  ? 423  GLU   A CB   1 
ATOM   215  C  CG   . GLU   A 1 45  ? 8.081   -30.305 41.344  1.00 55.18  ? 423  GLU   A CG   1 
ATOM   216  C  CD   . GLU   A 1 45  ? 7.088   -29.463 42.118  1.00 56.55  ? 423  GLU   A CD   1 
ATOM   217  O  OE1  . GLU   A 1 45  ? 6.665   -28.402 41.610  1.00 52.52  ? 423  GLU   A OE1  1 
ATOM   218  O  OE2  . GLU   A 1 45  ? 6.727   -29.867 43.243  1.00 61.83  ? 423  GLU   A OE2  1 
ATOM   219  N  N    . PHE   A 1 46  ? 6.936   -32.489 37.756  1.00 48.58  ? 424  PHE   A N    1 
ATOM   220  C  CA   . PHE   A 1 46  ? 6.261   -33.005 36.566  1.00 47.81  ? 424  PHE   A CA   1 
ATOM   221  C  C    . PHE   A 1 46  ? 4.760   -32.780 36.648  1.00 52.05  ? 424  PHE   A C    1 
ATOM   222  O  O    . PHE   A 1 46  ? 4.167   -32.925 37.718  1.00 54.33  ? 424  PHE   A O    1 
ATOM   223  C  CB   . PHE   A 1 46  ? 6.541   -34.489 36.383  1.00 50.26  ? 424  PHE   A CB   1 
ATOM   224  C  CG   . PHE   A 1 46  ? 7.972   -34.782 36.237  1.00 43.49  ? 424  PHE   A CG   1 
ATOM   225  C  CD1  . PHE   A 1 46  ? 8.577   -34.689 34.998  1.00 49.19  ? 424  PHE   A CD1  1 
ATOM   226  C  CD2  . PHE   A 1 46  ? 8.743   -35.072 37.342  1.00 52.94  ? 424  PHE   A CD2  1 
ATOM   227  C  CE1  . PHE   A 1 46  ? 9.935   -34.931 34.854  1.00 54.02  ? 424  PHE   A CE1  1 
ATOM   228  C  CE2  . PHE   A 1 46  ? 10.101  -35.314 37.210  1.00 53.90  ? 424  PHE   A CE2  1 
ATOM   229  C  CZ   . PHE   A 1 46  ? 10.697  -35.240 35.964  1.00 53.04  ? 424  PHE   A CZ   1 
ATOM   230  N  N    . THR   A 1 47  ? 4.148   -32.436 35.509  1.00 47.52  ? 425  THR   A N    1 
ATOM   231  C  CA   . THR   A 1 47  ? 2.724   -32.124 35.473  1.00 52.38  ? 425  THR   A CA   1 
ATOM   232  C  C    . THR   A 1 47  ? 1.897   -33.393 35.686  1.00 57.10  ? 425  THR   A C    1 
ATOM   233  O  O    . THR   A 1 47  ? 2.422   -34.491 35.896  1.00 54.20  ? 425  THR   A O    1 
ATOM   234  C  CB   . THR   A 1 47  ? 2.328   -31.459 34.149  1.00 52.30  ? 425  THR   A CB   1 
ATOM   235  O  OG1  . THR   A 1 47  ? 2.344   -32.422 33.082  1.00 53.01  ? 425  THR   A OG1  1 
ATOM   236  C  CG2  . THR   A 1 47  ? 3.263   -30.305 33.798  1.00 49.54  ? 425  THR   A CG2  1 
ATOM   237  N  N    . VAL   A 1 48  ? 0.571   -33.229 35.639  1.00 59.89  ? 426  VAL   A N    1 
ATOM   238  C  CA   . VAL   A 1 48  ? -0.318  -34.375 35.758  1.00 64.80  ? 426  VAL   A CA   1 
ATOM   239  C  C    . VAL   A 1 48  ? -0.195  -35.303 34.555  1.00 61.23  ? 426  VAL   A C    1 
ATOM   240  O  O    . VAL   A 1 48  ? -0.534  -36.485 34.652  1.00 63.27  ? 426  VAL   A O    1 
ATOM   241  C  CB   . VAL   A 1 48  ? -1.775  -33.905 35.948  1.00 64.88  ? 426  VAL   A CB   1 
ATOM   242  C  CG1  . VAL   A 1 48  ? -2.027  -33.556 37.408  1.00 69.06  ? 426  VAL   A CG1  1 
ATOM   243  C  CG2  . VAL   A 1 48  ? -2.072  -32.719 35.047  1.00 61.49  ? 426  VAL   A CG2  1 
ATOM   244  N  N    . ASN   A 1 49  ? 0.298   -34.798 33.427  1.00 57.41  ? 427  ASN   A N    1 
ATOM   245  C  CA   . ASN   A 1 49  ? 0.457   -35.576 32.207  1.00 54.92  ? 427  ASN   A CA   1 
ATOM   246  C  C    . ASN   A 1 49  ? 1.809   -36.285 32.129  1.00 53.21  ? 427  ASN   A C    1 
ATOM   247  O  O    . ASN   A 1 49  ? 2.049   -37.030 31.173  1.00 48.52  ? 427  ASN   A O    1 
ATOM   248  C  CB   . ASN   A 1 49  ? 0.290   -34.658 30.985  1.00 58.93  ? 427  ASN   A CB   1 
ATOM   249  C  CG   . ASN   A 1 49  ? -1.114  -34.029 30.891  1.00 65.38  ? 427  ASN   A CG   1 
ATOM   250  O  OD1  . ASN   A 1 49  ? -2.103  -34.589 31.374  1.00 64.72  ? 427  ASN   A OD1  1 
ATOM   251  N  ND2  . ASN   A 1 49  ? -1.190  -32.846 30.272  1.00 58.86  ? 427  ASN   A ND2  1 
ATOM   252  N  N    . GLY   A 1 50  ? 2.702   -36.065 33.101  1.00 54.66  ? 428  GLY   A N    1 
ATOM   253  C  CA   . GLY   A 1 50  ? 4.019   -36.667 33.107  1.00 48.71  ? 428  GLY   A CA   1 
ATOM   254  C  C    . GLY   A 1 50  ? 5.138   -35.807 32.545  1.00 46.02  ? 428  GLY   A C    1 
ATOM   255  O  O    . GLY   A 1 50  ? 6.304   -36.205 32.646  1.00 41.78  ? 428  GLY   A O    1 
ATOM   256  N  N    . ASP   A 1 51  ? 4.822   -34.651 31.940  1.00 46.00  ? 429  ASP   A N    1 
ATOM   257  C  CA   . ASP   A 1 51  ? 5.801   -33.755 31.336  1.00 46.14  ? 429  ASP   A CA   1 
ATOM   258  C  C    . ASP   A 1 51  ? 6.447   -32.869 32.405  1.00 45.53  ? 429  ASP   A C    1 
ATOM   259  O  O    . ASP   A 1 51  ? 5.843   -32.606 33.446  1.00 45.49  ? 429  ASP   A O    1 
ATOM   260  C  CB   . ASP   A 1 51  ? 5.132   -32.878 30.280  1.00 50.82  ? 429  ASP   A CB   1 
ATOM   261  C  CG   . ASP   A 1 51  ? 4.320   -33.686 29.272  1.00 51.67  ? 429  ASP   A CG   1 
ATOM   262  O  OD1  . ASP   A 1 51  ? 4.894   -34.582 28.626  1.00 50.10  ? 429  ASP   A OD1  1 
ATOM   263  O  OD2  . ASP   A 1 51  ? 3.103   -33.437 29.144  1.00 56.57  ? 429  ASP   A OD2  1 
ATOM   264  N  N    . PRO   A 1 52  ? 7.677   -32.409 32.187  1.00 45.87  ? 430  PRO   A N    1 
ATOM   265  C  CA   . PRO   A 1 52  ? 8.315   -31.561 33.203  1.00 43.91  ? 430  PRO   A CA   1 
ATOM   266  C  C    . PRO   A 1 52  ? 7.603   -30.217 33.314  1.00 46.11  ? 430  PRO   A C    1 
ATOM   267  O  O    . PRO   A 1 52  ? 7.062   -29.692 32.339  1.00 42.68  ? 430  PRO   A O    1 
ATOM   268  C  CB   . PRO   A 1 52  ? 9.761   -31.410 32.699  1.00 49.31  ? 430  PRO   A CB   1 
ATOM   269  C  CG   . PRO   A 1 52  ? 9.718   -31.781 31.233  1.00 50.04  ? 430  PRO   A CG   1 
ATOM   270  C  CD   . PRO   A 1 52  ? 8.610   -32.796 31.109  1.00 46.02  ? 430  PRO   A CD   1 
ATOM   271  N  N    . VAL   A 1 53  ? 7.576   -29.684 34.534  1.00 45.52  ? 431  VAL   A N    1 
ATOM   272  C  CA   . VAL   A 1 53  ? 6.987   -28.372 34.786  1.00 43.29  ? 431  VAL   A CA   1 
ATOM   273  C  C    . VAL   A 1 53  ? 8.019   -27.305 34.444  1.00 41.23  ? 431  VAL   A C    1 
ATOM   274  O  O    . VAL   A 1 53  ? 9.109   -27.271 35.026  1.00 44.02  ? 431  VAL   A O    1 
ATOM   275  C  CB   . VAL   A 1 53  ? 6.519   -28.228 36.241  1.00 42.01  ? 431  VAL   A CB   1 
ATOM   276  C  CG1  . VAL   A 1 53  ? 6.089   -26.774 36.508  1.00 40.70  ? 431  VAL   A CG1  1 
ATOM   277  C  CG2  . VAL   A 1 53  ? 5.389   -29.177 36.550  1.00 43.19  ? 431  VAL   A CG2  1 
ATOM   278  N  N    . LYS   A 1 54  ? 7.684   -26.441 33.496  1.00 36.21  ? 432  LYS   A N    1 
ATOM   279  C  CA   . LYS   A 1 54  ? 8.569   -25.345 33.135  1.00 41.02  ? 432  LYS   A CA   1 
ATOM   280  C  C    . LYS   A 1 54  ? 8.475   -24.252 34.200  1.00 40.12  ? 432  LYS   A C    1 
ATOM   281  O  O    . LYS   A 1 54  ? 7.398   -23.693 34.428  1.00 43.21  ? 432  LYS   A O    1 
ATOM   282  C  CB   . LYS   A 1 54  ? 8.208   -24.793 31.757  1.00 40.07  ? 432  LYS   A CB   1 
ATOM   283  C  CG   . LYS   A 1 54  ? 8.577   -25.715 30.593  1.00 46.34  ? 432  LYS   A CG   1 
ATOM   284  C  CD   . LYS   A 1 54  ? 7.922   -25.272 29.294  1.00 50.06  ? 432  LYS   A CD   1 
ATOM   285  C  CE   . LYS   A 1 54  ? 6.419   -25.341 29.351  1.00 48.94  ? 432  LYS   A CE   1 
ATOM   286  N  NZ   . LYS   A 1 54  ? 5.916   -26.387 30.295  1.00 57.86  ? 432  LYS   A NZ   1 
ATOM   287  N  N    . LYS   A 1 55  ? 9.597   -23.946 34.842  1.00 39.69  ? 433  LYS   A N    1 
ATOM   288  C  CA   . LYS   A 1 55  ? 9.656   -22.943 35.892  1.00 36.04  ? 433  LYS   A CA   1 
ATOM   289  C  C    . LYS   A 1 55  ? 10.597  -21.818 35.502  1.00 42.44  ? 433  LYS   A C    1 
ATOM   290  O  O    . LYS   A 1 55  ? 11.563  -22.016 34.758  1.00 42.91  ? 433  LYS   A O    1 
ATOM   291  C  CB   . LYS   A 1 55  ? 10.091  -23.565 37.223  1.00 38.06  ? 433  LYS   A CB   1 
ATOM   292  C  CG   . LYS   A 1 55  ? 9.180   -24.717 37.687  1.00 39.27  ? 433  LYS   A CG   1 
ATOM   293  C  CD   . LYS   A 1 55  ? 9.587   -25.247 39.054  1.00 41.17  ? 433  LYS   A CD   1 
ATOM   294  C  CE   . LYS   A 1 55  ? 8.638   -26.329 39.546  1.00 43.92  ? 433  LYS   A CE   1 
ATOM   295  N  NZ   . LYS   A 1 55  ? 9.031   -26.771 40.910  1.00 46.38  ? 433  LYS   A NZ   1 
ATOM   296  N  N    . VAL   A 1 56  ? 10.295  -20.622 36.002  1.00 39.03  ? 434  VAL   A N    1 
ATOM   297  C  CA   . VAL   A 1 56  ? 11.149  -19.468 35.785  1.00 39.29  ? 434  VAL   A CA   1 
ATOM   298  C  C    . VAL   A 1 56  ? 11.455  -18.869 37.143  1.00 43.50  ? 434  VAL   A C    1 
ATOM   299  O  O    . VAL   A 1 56  ? 10.651  -18.957 38.076  1.00 39.95  ? 434  VAL   A O    1 
ATOM   300  C  CB   . VAL   A 1 56  ? 10.496  -18.425 34.860  1.00 42.26  ? 434  VAL   A CB   1 
ATOM   301  C  CG1  . VAL   A 1 56  ? 10.141  -19.065 33.532  1.00 41.32  ? 434  VAL   A CG1  1 
ATOM   302  C  CG2  . VAL   A 1 56  ? 9.276   -17.832 35.515  1.00 44.06  ? 434  VAL   A CG2  1 
ATOM   303  N  N    . ILE   A 1 57  ? 12.641  -18.286 37.260  1.00 37.87  ? 435  ILE   A N    1 
ATOM   304  C  CA   . ILE   A 1 57  ? 12.985  -17.515 38.443  1.00 41.77  ? 435  ILE   A CA   1 
ATOM   305  C  C    . ILE   A 1 57  ? 12.209  -16.204 38.401  1.00 43.95  ? 435  ILE   A C    1 
ATOM   306  O  O    . ILE   A 1 57  ? 12.222  -15.494 37.390  1.00 46.43  ? 435  ILE   A O    1 
ATOM   307  C  CB   . ILE   A 1 57  ? 14.502  -17.261 38.503  1.00 44.14  ? 435  ILE   A CB   1 
ATOM   308  C  CG1  . ILE   A 1 57  ? 15.236  -18.563 38.783  1.00 46.85  ? 435  ILE   A CG1  1 
ATOM   309  C  CG2  . ILE   A 1 57  ? 14.826  -16.239 39.584  1.00 48.55  ? 435  ILE   A CG2  1 
ATOM   310  C  CD1  . ILE   A 1 57  ? 14.946  -19.114 40.146  1.00 52.17  ? 435  ILE   A CD1  1 
ATOM   311  N  N    . CYS   A 1 58  ? 11.509  -15.885 39.482  1.00 39.96  ? 436  CYS   A N    1 
ATOM   312  C  CA   . CYS   A 1 58  ? 10.812  -14.608 39.572  1.00 41.35  ? 436  CYS   A CA   1 
ATOM   313  C  C    . CYS   A 1 58  ? 11.196  -13.940 40.879  1.00 47.23  ? 436  CYS   A C    1 
ATOM   314  O  O    . CYS   A 1 58  ? 11.192  -14.590 41.932  1.00 47.46  ? 436  CYS   A O    1 
ATOM   315  C  CB   . CYS   A 1 58  ? 9.294   -14.782 39.489  1.00 42.26  ? 436  CYS   A CB   1 
ATOM   316  S  SG   . CYS   A 1 58  ? 8.635   -16.039 40.616  1.00 51.26  ? 436  CYS   A SG   1 
ATOM   317  N  N    . THR   A 1 59  ? 11.546  -12.656 40.810  1.00 43.34  ? 437  THR   A N    1 
ATOM   318  C  CA   . THR   A 1 59  ? 11.895  -11.909 42.004  1.00 42.13  ? 437  THR   A CA   1 
ATOM   319  C  C    . THR   A 1 59  ? 10.645  -11.275 42.602  1.00 44.87  ? 437  THR   A C    1 
ATOM   320  O  O    . THR   A 1 59  ? 9.707   -10.912 41.888  1.00 43.29  ? 437  THR   A O    1 
ATOM   321  C  CB   . THR   A 1 59  ? 12.939  -10.830 41.701  1.00 45.25  ? 437  THR   A CB   1 
ATOM   322  O  OG1  . THR   A 1 59  ? 12.477  -9.977  40.648  1.00 41.73  ? 437  THR   A OG1  1 
ATOM   323  C  CG2  . THR   A 1 59  ? 14.259  -11.463 41.273  1.00 46.86  ? 437  THR   A CG2  1 
ATOM   324  N  N    . GLY   A 1 60  ? 10.635  -11.153 43.927  1.00 49.49  ? 438  GLY   A N    1 
ATOM   325  C  CA   . GLY   A 1 60  ? 9.562   -10.467 44.603  1.00 49.23  ? 438  GLY   A CA   1 
ATOM   326  C  C    . GLY   A 1 60  ? 9.731   -10.441 46.103  1.00 55.05  ? 438  GLY   A C    1 
ATOM   327  O  O    . GLY   A 1 60  ? 10.638  -11.066 46.672  1.00 49.70  ? 438  GLY   A O    1 
ATOM   328  N  N    . PRO   A 1 61  ? 8.860   -9.700  46.780  1.00 56.38  ? 439  PRO   A N    1 
ATOM   329  C  CA   . PRO   A 1 61  ? 8.916   -9.641  48.241  1.00 62.66  ? 439  PRO   A CA   1 
ATOM   330  C  C    . PRO   A 1 61  ? 8.353   -10.913 48.863  1.00 64.58  ? 439  PRO   A C    1 
ATOM   331  O  O    . PRO   A 1 61  ? 7.707   -11.736 48.207  1.00 61.64  ? 439  PRO   A O    1 
ATOM   332  C  CB   . PRO   A 1 61  ? 8.047   -8.425  48.576  1.00 60.38  ? 439  PRO   A CB   1 
ATOM   333  C  CG   . PRO   A 1 61  ? 7.057   -8.376  47.451  1.00 56.80  ? 439  PRO   A CG   1 
ATOM   334  C  CD   . PRO   A 1 61  ? 7.807   -8.827  46.230  1.00 52.66  ? 439  PRO   A CD   1 
ATOM   335  N  N    . ASN   A 1 62  ? 8.606   -11.047 50.160  1.00 78.19  ? 440  ASN   A N    1 
ATOM   336  C  CA   . ASN   A 1 62  ? 8.079   -12.143 50.963  1.00 78.03  ? 440  ASN   A CA   1 
ATOM   337  C  C    . ASN   A 1 62  ? 6.703   -11.794 51.528  1.00 78.31  ? 440  ASN   A C    1 
ATOM   338  O  O    . ASN   A 1 62  ? 6.538   -10.790 52.228  1.00 78.28  ? 440  ASN   A O    1 
ATOM   339  C  CB   . ASN   A 1 62  ? 9.044   -12.477 52.104  1.00 78.86  ? 440  ASN   A CB   1 
ATOM   340  C  CG   . ASN   A 1 62  ? 10.450  -12.777 51.611  1.00 81.06  ? 440  ASN   A CG   1 
ATOM   341  O  OD1  . ASN   A 1 62  ? 10.695  -13.821 51.006  1.00 76.15  ? 440  ASN   A OD1  1 
ATOM   342  N  ND2  . ASN   A 1 62  ? 11.388  -11.867 51.888  1.00 77.40  ? 440  ASN   A ND2  1 
ATOM   343  N  N    . SER   A 1 68  ? 5.127   -2.527  55.948  1.00 65.67  ? 446  SER   A N    1 
ATOM   344  C  CA   . SER   A 1 68  ? 6.270   -3.420  56.118  1.00 67.54  ? 446  SER   A CA   1 
ATOM   345  C  C    . SER   A 1 68  ? 7.238   -3.335  54.913  1.00 69.70  ? 446  SER   A C    1 
ATOM   346  O  O    . SER   A 1 68  ? 6.775   -3.179  53.781  1.00 61.46  ? 446  SER   A O    1 
ATOM   347  C  CB   . SER   A 1 68  ? 5.784   -4.867  56.346  1.00 64.74  ? 446  SER   A CB   1 
ATOM   348  O  OG   . SER   A 1 68  ? 4.594   -5.156  55.627  1.00 72.38  ? 446  SER   A OG   1 
ATOM   349  N  N    . PRO   A 1 69  ? 8.554   -3.346  55.174  1.00 65.48  ? 447  PRO   A N    1 
ATOM   350  C  CA   . PRO   A 1 69  ? 9.527   -3.372  54.075  1.00 63.44  ? 447  PRO   A CA   1 
ATOM   351  C  C    . PRO   A 1 69  ? 9.227   -4.489  53.084  1.00 67.33  ? 447  PRO   A C    1 
ATOM   352  O  O    . PRO   A 1 69  ? 8.696   -5.539  53.445  1.00 67.40  ? 447  PRO   A O    1 
ATOM   353  C  CB   . PRO   A 1 69  ? 10.862  -3.652  54.794  1.00 63.50  ? 447  PRO   A CB   1 
ATOM   354  C  CG   . PRO   A 1 69  ? 10.539  -3.448  56.300  1.00 62.02  ? 447  PRO   A CG   1 
ATOM   355  C  CD   . PRO   A 1 69  ? 9.219   -2.742  56.328  1.00 64.29  ? 447  PRO   A CD   1 
ATOM   356  N  N    . ARG   A 1 70  ? 9.613   -4.270  51.829  1.00 78.68  ? 448  ARG   A N    1 
ATOM   357  C  CA   . ARG   A 1 70  ? 9.531   -5.276  50.775  1.00 75.08  ? 448  ARG   A CA   1 
ATOM   358  C  C    . ARG   A 1 70  ? 10.949  -5.712  50.410  1.00 77.96  ? 448  ARG   A C    1 
ATOM   359  O  O    . ARG   A 1 70  ? 11.576  -5.140  49.519  1.00 70.58  ? 448  ARG   A O    1 
ATOM   360  C  CB   . ARG   A 1 70  ? 8.773   -4.724  49.571  1.00 69.45  ? 448  ARG   A CB   1 
ATOM   361  C  CG   . ARG   A 1 70  ? 7.324   -4.359  49.868  1.00 64.95  ? 448  ARG   A CG   1 
ATOM   362  C  CD   . ARG   A 1 70  ? 6.696   -3.549  48.756  1.00 60.52  ? 448  ARG   A CD   1 
ATOM   363  N  NE   . ARG   A 1 70  ? 5.370   -3.071  49.133  1.00 66.38  ? 448  ARG   A NE   1 
ATOM   364  C  CZ   . ARG   A 1 70  ? 4.657   -2.188  48.443  1.00 64.30  ? 448  ARG   A CZ   1 
ATOM   365  N  NH1  . ARG   A 1 70  ? 5.108   -1.656  47.317  1.00 60.65  ? 448  ARG   A NH1  1 
ATOM   366  N  NH2  . ARG   A 1 70  ? 3.464   -1.818  48.903  1.00 59.49  ? 448  ARG   A NH2  1 
ATOM   367  N  N    . HIS   A 1 71  ? 11.447  -6.735  51.107  1.00 77.10  ? 449  HIS   A N    1 
ATOM   368  C  CA   . HIS   A 1 71  ? 12.738  -7.344  50.790  1.00 71.91  ? 449  HIS   A CA   1 
ATOM   369  C  C    . HIS   A 1 71  ? 12.548  -8.293  49.612  1.00 67.66  ? 449  HIS   A C    1 
ATOM   370  O  O    . HIS   A 1 71  ? 11.888  -9.331  49.739  1.00 65.47  ? 449  HIS   A O    1 
ATOM   371  C  CB   . HIS   A 1 71  ? 13.309  -8.079  52.001  1.00 65.60  ? 449  HIS   A CB   1 
ATOM   372  N  N    . THR   A 1 72  ? 13.113  -7.931  48.464  1.00 58.37  ? 450  THR   A N    1 
ATOM   373  C  CA   . THR   A 1 72  ? 12.941  -8.713  47.248  1.00 59.84  ? 450  THR   A CA   1 
ATOM   374  C  C    . THR   A 1 72  ? 13.938  -9.872  47.206  1.00 57.86  ? 450  THR   A C    1 
ATOM   375  O  O    . THR   A 1 72  ? 15.131  -9.683  47.462  1.00 58.78  ? 450  THR   A O    1 
ATOM   376  C  CB   . THR   A 1 72  ? 13.105  -7.801  46.033  1.00 59.08  ? 450  THR   A CB   1 
ATOM   377  O  OG1  . THR   A 1 72  ? 13.492  -8.572  44.892  1.00 59.67  ? 450  THR   A OG1  1 
ATOM   378  C  CG2  . THR   A 1 72  ? 14.150  -6.729  46.313  1.00 67.37  ? 450  THR   A CG2  1 
ATOM   379  N  N    . VAL   A 1 73  ? 13.446  -11.074 46.914  1.00 50.81  ? 451  VAL   A N    1 
ATOM   380  C  CA   . VAL   A 1 73  ? 14.310  -12.257 46.810  1.00 54.27  ? 451  VAL   A CA   1 
ATOM   381  C  C    . VAL   A 1 73  ? 13.866  -13.102 45.633  1.00 50.81  ? 451  VAL   A C    1 
ATOM   382  O  O    . VAL   A 1 73  ? 12.692  -13.083 45.225  1.00 49.12  ? 451  VAL   A O    1 
ATOM   383  C  CB   . VAL   A 1 73  ? 14.286  -13.114 48.099  1.00 54.15  ? 451  VAL   A CB   1 
ATOM   384  C  CG1  . VAL   A 1 73  ? 14.918  -12.373 49.262  1.00 55.71  ? 451  VAL   A CG1  1 
ATOM   385  C  CG2  . VAL   A 1 73  ? 12.862  -13.545 48.436  1.00 52.30  ? 451  VAL   A CG2  1 
ATOM   386  N  N    . PRO   A 1 74  ? 14.798  -13.851 45.038  1.00 43.91  ? 452  PRO   A N    1 
ATOM   387  C  CA   . PRO   A 1 74  ? 14.418  -14.755 43.946  1.00 49.19  ? 452  PRO   A CA   1 
ATOM   388  C  C    . PRO   A 1 74  ? 13.550  -15.915 44.430  1.00 46.26  ? 452  PRO   A C    1 
ATOM   389  O  O    . PRO   A 1 74  ? 13.762  -16.480 45.507  1.00 45.50  ? 452  PRO   A O    1 
ATOM   390  C  CB   . PRO   A 1 74  ? 15.769  -15.225 43.384  1.00 47.33  ? 452  PRO   A CB   1 
ATOM   391  C  CG   . PRO   A 1 74  ? 16.757  -14.981 44.484  1.00 52.32  ? 452  PRO   A CG   1 
ATOM   392  C  CD   . PRO   A 1 74  ? 16.265  -13.789 45.228  1.00 49.03  ? 452  PRO   A CD   1 
ATOM   393  N  N    . GLN   A 1 75  ? 12.546  -16.246 43.618  1.00 44.98  ? 453  GLN   A N    1 
ATOM   394  C  CA   . GLN   A 1 75  ? 11.595  -17.321 43.897  1.00 42.85  ? 453  GLN   A CA   1 
ATOM   395  C  C    . GLN   A 1 75  ? 11.279  -18.052 42.593  1.00 41.60  ? 453  GLN   A C    1 
ATOM   396  O  O    . GLN   A 1 75  ? 11.749  -17.675 41.518  1.00 39.50  ? 453  GLN   A O    1 
ATOM   397  C  CB   . GLN   A 1 75  ? 10.317  -16.773 44.554  1.00 42.19  ? 453  GLN   A CB   1 
ATOM   398  C  CG   . GLN   A 1 75  ? 10.547  -15.964 45.836  1.00 46.14  ? 453  GLN   A CG   1 
ATOM   399  C  CD   . GLN   A 1 75  ? 9.340   -15.139 46.229  1.00 49.33  ? 453  GLN   A CD   1 
ATOM   400  O  OE1  . GLN   A 1 75  ? 8.284   -15.687 46.523  1.00 44.72  ? 453  GLN   A OE1  1 
ATOM   401  N  NE2  . GLN   A 1 75  ? 9.496   -13.817 46.255  1.00 53.99  ? 453  GLN   A NE2  1 
ATOM   402  N  N    . CYS   A 1 76  ? 10.450  -19.090 42.683  1.00 38.44  ? 454  CYS   A N    1 
ATOM   403  C  CA   . CYS   A 1 76  ? 10.097  -19.936 41.548  1.00 38.17  ? 454  CYS   A CA   1 
ATOM   404  C  C    . CYS   A 1 76  ? 8.650   -19.709 41.136  1.00 38.58  ? 454  CYS   A C    1 
ATOM   405  O  O    . CYS   A 1 76  ? 7.747   -19.785 41.975  1.00 39.18  ? 454  CYS   A O    1 
ATOM   406  C  CB   . CYS   A 1 76  ? 10.303  -21.410 41.896  1.00 41.80  ? 454  CYS   A CB   1 
ATOM   407  S  SG   . CYS   A 1 76  ? 12.018  -21.774 42.269  1.00 48.60  ? 454  CYS   A SG   1 
ATOM   408  N  N    . CYS   A 1 77  ? 8.432   -19.459 39.841  1.00 36.31  ? 455  CYS   A N    1 
ATOM   409  C  CA   . CYS   A 1 77  ? 7.105   -19.213 39.282  1.00 34.50  ? 455  CYS   A CA   1 
ATOM   410  C  C    . CYS   A 1 77  ? 6.782   -20.242 38.209  1.00 36.59  ? 455  CYS   A C    1 
ATOM   411  O  O    . CYS   A 1 77  ? 7.623   -20.542 37.359  1.00 38.23  ? 455  CYS   A O    1 
ATOM   412  C  CB   . CYS   A 1 77  ? 7.011   -17.803 38.654  1.00 36.52  ? 455  CYS   A CB   1 
ATOM   413  S  SG   . CYS   A 1 77  ? 6.791   -16.466 39.845  1.00 54.23  ? 455  CYS   A SG   1 
ATOM   414  N  N    . TYR   A 1 78  ? 5.543   -20.729 38.210  1.00 33.07  ? 456  TYR   A N    1 
ATOM   415  C  CA   . TYR   A 1 78  ? 5.082   -21.643 37.175  1.00 33.66  ? 456  TYR   A CA   1 
ATOM   416  C  C    . TYR   A 1 78  ? 3.557   -21.624 37.170  1.00 35.06  ? 456  TYR   A C    1 
ATOM   417  O  O    . TYR   A 1 78  ? 2.921   -21.080 38.077  1.00 34.41  ? 456  TYR   A O    1 
ATOM   418  C  CB   . TYR   A 1 78  ? 5.622   -23.066 37.390  1.00 33.75  ? 456  TYR   A CB   1 
ATOM   419  C  CG   . TYR   A 1 78  ? 5.331   -23.662 38.761  1.00 34.51  ? 456  TYR   A CG   1 
ATOM   420  C  CD1  . TYR   A 1 78  ? 6.184   -23.422 39.839  1.00 37.36  ? 456  TYR   A CD1  1 
ATOM   421  C  CD2  . TYR   A 1 78  ? 4.198   -24.456 38.979  1.00 35.68  ? 456  TYR   A CD2  1 
ATOM   422  C  CE1  . TYR   A 1 78  ? 5.939   -23.967 41.089  1.00 38.71  ? 456  TYR   A CE1  1 
ATOM   423  C  CE2  . TYR   A 1 78  ? 3.946   -25.018 40.231  1.00 36.41  ? 456  TYR   A CE2  1 
ATOM   424  C  CZ   . TYR   A 1 78  ? 4.812   -24.762 41.281  1.00 40.57  ? 456  TYR   A CZ   1 
ATOM   425  O  OH   . TYR   A 1 78  ? 4.576   -25.295 42.532  1.00 41.37  ? 456  TYR   A OH   1 
ATOM   426  N  N    . GLY   A 1 79  ? 2.979   -22.240 36.148  1.00 31.73  ? 457  GLY   A N    1 
ATOM   427  C  CA   . GLY   A 1 79  ? 1.540   -22.389 36.033  1.00 33.77  ? 457  GLY   A CA   1 
ATOM   428  C  C    . GLY   A 1 79  ? 1.074   -21.935 34.675  1.00 31.34  ? 457  GLY   A C    1 
ATOM   429  O  O    . GLY   A 1 79  ? 1.878   -21.666 33.778  1.00 33.02  ? 457  GLY   A O    1 
ATOM   430  N  N    . PHE   A 1 80  ? -0.255  -21.868 34.528  1.00 30.94  ? 458  PHE   A N    1 
ATOM   431  C  CA   . PHE   A 1 80  ? -0.905  -21.527 33.261  1.00 32.36  ? 458  PHE   A CA   1 
ATOM   432  C  C    . PHE   A 1 80  ? -0.338  -20.249 32.659  1.00 32.05  ? 458  PHE   A C    1 
ATOM   433  O  O    . PHE   A 1 80  ? -0.003  -20.205 31.470  1.00 30.58  ? 458  PHE   A O    1 
ATOM   434  C  CB   . PHE   A 1 80  ? -2.409  -21.398 33.530  1.00 34.02  ? 458  PHE   A CB   1 
ATOM   435  C  CG   . PHE   A 1 80  ? -3.280  -21.234 32.319  1.00 35.19  ? 458  PHE   A CG   1 
ATOM   436  C  CD1  . PHE   A 1 80  ? -3.281  -20.050 31.603  1.00 32.82  ? 458  PHE   A CD1  1 
ATOM   437  C  CD2  . PHE   A 1 80  ? -4.244  -22.193 32.020  1.00 37.87  ? 458  PHE   A CD2  1 
ATOM   438  C  CE1  . PHE   A 1 80  ? -4.154  -19.876 30.541  1.00 38.40  ? 458  PHE   A CE1  1 
ATOM   439  C  CE2  . PHE   A 1 80  ? -5.124  -22.016 30.977  1.00 38.65  ? 458  PHE   A CE2  1 
ATOM   440  C  CZ   . PHE   A 1 80  ? -5.082  -20.867 30.249  1.00 37.38  ? 458  PHE   A CZ   1 
ATOM   441  N  N    . CYS   A 1 81  ? -0.216  -19.189 33.465  1.00 32.96  ? 459  CYS   A N    1 
ATOM   442  C  CA   . CYS   A 1 81  ? 0.266   -17.930 32.904  1.00 31.80  ? 459  CYS   A CA   1 
ATOM   443  C  C    . CYS   A 1 81  ? 1.764   -17.991 32.575  1.00 31.98  ? 459  CYS   A C    1 
ATOM   444  O  O    . CYS   A 1 81  ? 2.213   -17.341 31.625  1.00 30.60  ? 459  CYS   A O    1 
ATOM   445  C  CB   . CYS   A 1 81  ? -0.075  -16.774 33.857  1.00 33.68  ? 459  CYS   A CB   1 
ATOM   446  S  SG   . CYS   A 1 81  ? -1.840  -16.191 33.665  1.00 41.70  ? 459  CYS   A SG   1 
ATOM   447  N  N    . ILE   A 1 82  ? 2.549   -18.785 33.304  1.00 31.46  ? 460  ILE   A N    1 
ATOM   448  C  CA   . ILE   A 1 82  ? 3.970   -18.876 32.972  1.00 31.92  ? 460  ILE   A CA   1 
ATOM   449  C  C    . ILE   A 1 82  ? 4.168   -19.691 31.695  1.00 35.59  ? 460  ILE   A C    1 
ATOM   450  O  O    . ILE   A 1 82  ? 4.987   -19.336 30.835  1.00 30.19  ? 460  ILE   A O    1 
ATOM   451  C  CB   . ILE   A 1 82  ? 4.766   -19.448 34.151  1.00 31.12  ? 460  ILE   A CB   1 
ATOM   452  C  CG1  . ILE   A 1 82  ? 4.606   -18.553 35.379  1.00 35.36  ? 460  ILE   A CG1  1 
ATOM   453  C  CG2  . ILE   A 1 82  ? 6.253   -19.561 33.794  1.00 37.20  ? 460  ILE   A CG2  1 
ATOM   454  C  CD1  . ILE   A 1 82  ? 5.169   -17.147 35.193  1.00 34.78  ? 460  ILE   A CD1  1 
ATOM   455  N  N    . ASP   A 1 83  ? 3.410   -20.780 31.540  1.00 34.84  ? 461  ASP   A N    1 
ATOM   456  C  CA   . ASP   A 1 83  ? 3.411   -21.507 30.271  1.00 36.51  ? 461  ASP   A CA   1 
ATOM   457  C  C    . ASP   A 1 83  ? 3.016   -20.596 29.111  1.00 32.20  ? 461  ASP   A C    1 
ATOM   458  O  O    . ASP   A 1 83  ? 3.613   -20.667 28.028  1.00 33.07  ? 461  ASP   A O    1 
ATOM   459  C  CB   . ASP   A 1 83  ? 2.449   -22.690 30.340  1.00 35.24  ? 461  ASP   A CB   1 
ATOM   460  C  CG   . ASP   A 1 83  ? 3.053   -23.926 30.986  1.00 38.55  ? 461  ASP   A CG   1 
ATOM   461  O  OD1  . ASP   A 1 83  ? 4.213   -23.865 31.422  1.00 38.70  ? 461  ASP   A OD1  1 
ATOM   462  O  OD2  . ASP   A 1 83  ? 2.346   -24.969 31.064  1.00 37.05  ? 461  ASP   A OD2  1 
ATOM   463  N  N    . LEU   A 1 84  ? 1.993   -19.748 29.308  1.00 32.17  ? 462  LEU   A N    1 
ATOM   464  C  CA   . LEU   A 1 84  ? 1.602   -18.825 28.244  1.00 32.85  ? 462  LEU   A CA   1 
ATOM   465  C  C    . LEU   A 1 84  ? 2.734   -17.856 27.914  1.00 33.82  ? 462  LEU   A C    1 
ATOM   466  O  O    . LEU   A 1 84  ? 3.025   -17.618 26.735  1.00 34.26  ? 462  LEU   A O    1 
ATOM   467  C  CB   . LEU   A 1 84  ? 0.324   -18.060 28.616  1.00 28.81  ? 462  LEU   A CB   1 
ATOM   468  C  CG   . LEU   A 1 84  ? -0.225  -17.132 27.524  1.00 31.40  ? 462  LEU   A CG   1 
ATOM   469  C  CD1  . LEU   A 1 84  ? -0.478  -17.916 26.248  1.00 35.28  ? 462  LEU   A CD1  1 
ATOM   470  C  CD2  . LEU   A 1 84  ? -1.547  -16.415 27.938  1.00 29.90  ? 462  LEU   A CD2  1 
ATOM   471  N  N    . LEU   A 1 85  ? 3.387   -17.295 28.937  1.00 34.89  ? 463  LEU   A N    1 
ATOM   472  C  CA   . LEU   A 1 85  ? 4.516   -16.392 28.701  1.00 32.41  ? 463  LEU   A CA   1 
ATOM   473  C  C    . LEU   A 1 85  ? 5.613   -17.090 27.904  1.00 37.84  ? 463  LEU   A C    1 
ATOM   474  O  O    . LEU   A 1 85  ? 6.160   -16.524 26.951  1.00 35.21  ? 463  LEU   A O    1 
ATOM   475  C  CB   . LEU   A 1 85  ? 5.064   -15.878 30.030  1.00 31.65  ? 463  LEU   A CB   1 
ATOM   476  C  CG   . LEU   A 1 85  ? 6.421   -15.144 29.955  1.00 34.18  ? 463  LEU   A CG   1 
ATOM   477  C  CD1  . LEU   A 1 85  ? 6.233   -13.818 29.236  1.00 35.41  ? 463  LEU   A CD1  1 
ATOM   478  C  CD2  . LEU   A 1 85  ? 7.036   -14.947 31.325  1.00 29.66  ? 463  LEU   A CD2  1 
ATOM   479  N  N    . ILE   A 1 86  ? 5.929   -18.339 28.266  1.00 34.51  ? 464  ILE   A N    1 
ATOM   480  C  CA   . ILE   A 1 86  ? 6.997   -19.055 27.575  1.00 39.27  ? 464  ILE   A CA   1 
ATOM   481  C  C    . ILE   A 1 86  ? 6.636   -19.234 26.106  1.00 40.69  ? 464  ILE   A C    1 
ATOM   482  O  O    . ILE   A 1 86  ? 7.467   -19.016 25.209  1.00 39.12  ? 464  ILE   A O    1 
ATOM   483  C  CB   . ILE   A 1 86  ? 7.278   -20.399 28.280  1.00 35.96  ? 464  ILE   A CB   1 
ATOM   484  C  CG1  . ILE   A 1 86  ? 7.919   -20.146 29.651  1.00 39.27  ? 464  ILE   A CG1  1 
ATOM   485  C  CG2  . ILE   A 1 86  ? 8.161   -21.284 27.406  1.00 45.60  ? 464  ILE   A CG2  1 
ATOM   486  C  CD1  . ILE   A 1 86  ? 7.978   -21.374 30.579  1.00 37.83  ? 464  ILE   A CD1  1 
ATOM   487  N  N    . LYS   A 1 87  ? 5.376   -19.588 25.842  1.00 37.78  ? 465  LYS   A N    1 
ATOM   488  C  CA   . LYS   A 1 87  ? 4.879   -19.721 24.478  1.00 39.10  ? 465  LYS   A CA   1 
ATOM   489  C  C    . LYS   A 1 87  ? 5.013   -18.413 23.711  1.00 41.42  ? 465  LYS   A C    1 
ATOM   490  O  O    . LYS   A 1 87  ? 5.541   -18.392 22.594  1.00 46.63  ? 465  LYS   A O    1 
ATOM   491  C  CB   . LYS   A 1 87  ? 3.416   -20.167 24.499  1.00 39.56  ? 465  LYS   A CB   1 
ATOM   492  C  CG   . LYS   A 1 87  ? 2.818   -20.461 23.130  1.00 38.54  ? 465  LYS   A CG   1 
ATOM   493  C  CD   . LYS   A 1 87  ? 3.628   -21.560 22.448  1.00 47.09  ? 465  LYS   A CD   1 
ATOM   494  C  CE   . LYS   A 1 87  ? 2.922   -22.154 21.233  1.00 45.71  ? 465  LYS   A CE   1 
ATOM   495  N  NZ   . LYS   A 1 87  ? 3.657   -23.375 20.768  1.00 51.68  ? 465  LYS   A NZ   1 
ATOM   496  N  N    . LEU   A 1 88  ? 4.523   -17.311 24.293  1.00 40.30  ? 466  LEU   A N    1 
ATOM   497  C  CA   . LEU   A 1 88  ? 4.642   -16.007 23.646  1.00 40.08  ? 466  LEU   A CA   1 
ATOM   498  C  C    . LEU   A 1 88  ? 6.097   -15.642 23.384  1.00 44.99  ? 466  LEU   A C    1 
ATOM   499  O  O    . LEU   A 1 88  ? 6.432   -15.136 22.307  1.00 44.94  ? 466  LEU   A O    1 
ATOM   500  C  CB   . LEU   A 1 88  ? 3.992   -14.934 24.505  1.00 37.02  ? 466  LEU   A CB   1 
ATOM   501  C  CG   . LEU   A 1 88  ? 2.479   -14.999 24.693  1.00 40.15  ? 466  LEU   A CG   1 
ATOM   502  C  CD1  . LEU   A 1 88  ? 2.056   -13.927 25.684  1.00 36.47  ? 466  LEU   A CD1  1 
ATOM   503  C  CD2  . LEU   A 1 88  ? 1.796   -14.800 23.357  1.00 38.63  ? 466  LEU   A CD2  1 
ATOM   504  N  N    . ALA   A 1 89  ? 6.974   -15.864 24.369  1.00 42.00  ? 467  ALA   A N    1 
ATOM   505  C  CA   . ALA   A 1 89  ? 8.381   -15.512 24.202  1.00 44.25  ? 467  ALA   A CA   1 
ATOM   506  C  C    . ALA   A 1 89  ? 9.026   -16.333 23.095  1.00 48.79  ? 467  ALA   A C    1 
ATOM   507  O  O    . ALA   A 1 89  ? 9.777   -15.795 22.271  1.00 48.01  ? 467  ALA   A O    1 
ATOM   508  C  CB   . ALA   A 1 89  ? 9.141   -15.709 25.516  1.00 44.83  ? 467  ALA   A CB   1 
ATOM   509  N  N    . ARG   A 1 90  ? 8.751   -17.638 23.065  1.00 44.29  ? 468  ARG   A N    1 
ATOM   510  C  CA   . ARG   A 1 90  ? 9.323   -18.495 22.032  1.00 47.65  ? 468  ARG   A CA   1 
ATOM   511  C  C    . ARG   A 1 90  ? 8.780   -18.126 20.658  1.00 50.55  ? 468  ARG   A C    1 
ATOM   512  O  O    . ARG   A 1 90  ? 9.529   -18.107 19.677  1.00 54.63  ? 468  ARG   A O    1 
ATOM   513  C  CB   . ARG   A 1 90  ? 9.037   -19.968 22.347  1.00 50.97  ? 468  ARG   A CB   1 
ATOM   514  C  CG   . ARG   A 1 90  ? 9.114   -20.925 21.154  1.00 55.45  ? 468  ARG   A CG   1 
ATOM   515  C  CD   . ARG   A 1 90  ? 8.875   -22.385 21.578  1.00 60.70  ? 468  ARG   A CD   1 
ATOM   516  N  NE   . ARG   A 1 90  ? 7.708   -22.512 22.450  1.00 66.63  ? 468  ARG   A NE   1 
ATOM   517  C  CZ   . ARG   A 1 90  ? 7.634   -23.299 23.519  1.00 68.48  ? 468  ARG   A CZ   1 
ATOM   518  N  NH1  . ARG   A 1 90  ? 8.658   -24.055 23.892  1.00 70.53  ? 468  ARG   A NH1  1 
ATOM   519  N  NH2  . ARG   A 1 90  ? 6.501   -23.331 24.230  1.00 50.42  ? 468  ARG   A NH2  1 
ATOM   520  N  N    . THR   A 1 91  ? 7.487   -17.795 20.570  1.00 47.19  ? 469  THR   A N    1 
ATOM   521  C  CA   . THR   A 1 91  ? 6.869   -17.579 19.269  1.00 51.21  ? 469  THR   A CA   1 
ATOM   522  C  C    . THR   A 1 91  ? 7.102   -16.172 18.721  1.00 55.31  ? 469  THR   A C    1 
ATOM   523  O  O    . THR   A 1 91  ? 7.080   -15.990 17.500  1.00 60.52  ? 469  THR   A O    1 
ATOM   524  C  CB   . THR   A 1 91  ? 5.366   -17.887 19.341  1.00 50.48  ? 469  THR   A CB   1 
ATOM   525  O  OG1  . THR   A 1 91  ? 4.851   -18.036 18.015  1.00 67.33  ? 469  THR   A OG1  1 
ATOM   526  C  CG2  . THR   A 1 91  ? 4.605   -16.773 20.027  1.00 52.50  ? 469  THR   A CG2  1 
ATOM   527  N  N    . MET   A 1 92  ? 7.342   -15.178 19.577  1.00 49.87  ? 470  MET   A N    1 
ATOM   528  C  CA   . MET   A 1 92  ? 7.593   -13.819 19.128  1.00 50.75  ? 470  MET   A CA   1 
ATOM   529  C  C    . MET   A 1 92  ? 9.047   -13.402 19.277  1.00 52.16  ? 470  MET   A C    1 
ATOM   530  O  O    . MET   A 1 92  ? 9.390   -12.274 18.912  1.00 55.06  ? 470  MET   A O    1 
ATOM   531  C  CB   . MET   A 1 92  ? 6.698   -12.845 19.891  1.00 52.02  ? 470  MET   A CB   1 
ATOM   532  C  CG   . MET   A 1 92  ? 5.221   -13.094 19.637  1.00 52.38  ? 470  MET   A CG   1 
ATOM   533  S  SD   . MET   A 1 92  ? 4.236   -12.158 20.805  1.00 56.13  ? 470  MET   A SD   1 
ATOM   534  C  CE   . MET   A 1 92  ? 4.876   -10.536 20.431  1.00 49.32  ? 470  MET   A CE   1 
ATOM   535  N  N    . ASN   A 1 93  ? 9.897   -14.269 19.827  1.00 51.13  ? 471  ASN   A N    1 
ATOM   536  C  CA   . ASN   A 1 93  ? 11.333  -14.031 19.914  1.00 55.55  ? 471  ASN   A CA   1 
ATOM   537  C  C    . ASN   A 1 93  ? 11.693  -12.851 20.806  1.00 54.37  ? 471  ASN   A C    1 
ATOM   538  O  O    . ASN   A 1 93  ? 12.361  -11.915 20.351  1.00 56.79  ? 471  ASN   A O    1 
ATOM   539  C  CB   . ASN   A 1 93  ? 11.921  -13.815 18.513  1.00 58.90  ? 471  ASN   A CB   1 
ATOM   540  C  CG   . ASN   A 1 93  ? 13.296  -14.411 18.365  1.00 68.16  ? 471  ASN   A CG   1 
ATOM   541  O  OD1  . ASN   A 1 93  ? 14.050  -14.506 19.334  1.00 71.68  ? 471  ASN   A OD1  1 
ATOM   542  N  ND2  . ASN   A 1 93  ? 13.640  -14.811 17.145  1.00 78.75  ? 471  ASN   A ND2  1 
ATOM   543  N  N    . PHE   A 1 94  ? 11.290  -12.891 22.077  1.00 47.59  ? 472  PHE   A N    1 
ATOM   544  C  CA   . PHE   A 1 94  ? 11.744  -11.905 23.046  1.00 50.25  ? 472  PHE   A CA   1 
ATOM   545  C  C    . PHE   A 1 94  ? 12.219  -12.603 24.310  1.00 47.23  ? 472  PHE   A C    1 
ATOM   546  O  O    . PHE   A 1 94  ? 11.789  -13.713 24.623  1.00 53.16  ? 472  PHE   A O    1 
ATOM   547  C  CB   . PHE   A 1 94  ? 10.656  -10.860 23.363  1.00 50.77  ? 472  PHE   A CB   1 
ATOM   548  C  CG   . PHE   A 1 94  ? 9.442   -11.408 24.071  1.00 47.26  ? 472  PHE   A CG   1 
ATOM   549  C  CD1  . PHE   A 1 94  ? 9.420   -11.558 25.447  1.00 47.48  ? 472  PHE   A CD1  1 
ATOM   550  C  CD2  . PHE   A 1 94  ? 8.299   -11.699 23.359  1.00 46.74  ? 472  PHE   A CD2  1 
ATOM   551  C  CE1  . PHE   A 1 94  ? 8.292   -12.040 26.098  1.00 45.41  ? 472  PHE   A CE1  1 
ATOM   552  C  CE2  . PHE   A 1 94  ? 7.159   -12.164 23.996  1.00 49.03  ? 472  PHE   A CE2  1 
ATOM   553  C  CZ   . PHE   A 1 94  ? 7.152   -12.336 25.370  1.00 45.87  ? 472  PHE   A CZ   1 
ATOM   554  N  N    . THR   A 1 95  ? 13.143  -11.962 25.012  1.00 49.41  ? 473  THR   A N    1 
ATOM   555  C  CA   . THR   A 1 95  ? 13.596  -12.444 26.306  1.00 48.24  ? 473  THR   A CA   1 
ATOM   556  C  C    . THR   A 1 95  ? 12.923  -11.644 27.412  1.00 48.31  ? 473  THR   A C    1 
ATOM   557  O  O    . THR   A 1 95  ? 12.362  -10.565 27.178  1.00 51.05  ? 473  THR   A O    1 
ATOM   558  C  CB   . THR   A 1 95  ? 15.121  -12.343 26.432  1.00 50.94  ? 473  THR   A CB   1 
ATOM   559  O  OG1  . THR   A 1 95  ? 15.522  -10.972 26.347  1.00 54.10  ? 473  THR   A OG1  1 
ATOM   560  C  CG2  . THR   A 1 95  ? 15.777  -13.116 25.297  1.00 50.46  ? 473  THR   A CG2  1 
ATOM   561  N  N    . TYR   A 1 96  ? 12.990  -12.174 28.634  1.00 46.30  ? 474  TYR   A N    1 
ATOM   562  C  CA   . TYR   A 1 96  ? 12.169  -11.613 29.697  1.00 47.72  ? 474  TYR   A CA   1 
ATOM   563  C  C    . TYR   A 1 96  ? 12.806  -11.852 31.056  1.00 47.55  ? 474  TYR   A C    1 
ATOM   564  O  O    . TYR   A 1 96  ? 13.605  -12.773 31.246  1.00 47.37  ? 474  TYR   A O    1 
ATOM   565  C  CB   . TYR   A 1 96  ? 10.748  -12.206 29.684  1.00 41.14  ? 474  TYR   A CB   1 
ATOM   566  C  CG   . TYR   A 1 96  ? 10.741  -13.714 29.753  1.00 44.92  ? 474  TYR   A CG   1 
ATOM   567  C  CD1  . TYR   A 1 96  ? 10.708  -14.371 30.975  1.00 47.48  ? 474  TYR   A CD1  1 
ATOM   568  C  CD2  . TYR   A 1 96  ? 10.773  -14.482 28.601  1.00 44.62  ? 474  TYR   A CD2  1 
ATOM   569  C  CE1  . TYR   A 1 96  ? 10.719  -15.750 31.049  1.00 47.33  ? 474  TYR   A CE1  1 
ATOM   570  C  CE2  . TYR   A 1 96  ? 10.776  -15.869 28.666  1.00 42.50  ? 474  TYR   A CE2  1 
ATOM   571  C  CZ   . TYR   A 1 96  ? 10.758  -16.491 29.893  1.00 46.48  ? 474  TYR   A CZ   1 
ATOM   572  O  OH   . TYR   A 1 96  ? 10.755  -17.863 29.968  1.00 49.66  ? 474  TYR   A OH   1 
ATOM   573  N  N    . GLU   A 1 97  ? 12.430  -10.991 32.000  1.00 45.38  ? 475  GLU   A N    1 
ATOM   574  C  CA   . GLU   A 1 97  ? 12.670  -11.164 33.429  1.00 47.03  ? 475  GLU   A CA   1 
ATOM   575  C  C    . GLU   A 1 97  ? 11.334  -10.993 34.131  1.00 42.15  ? 475  GLU   A C    1 
ATOM   576  O  O    . GLU   A 1 97  ? 10.623  -10.019 33.871  1.00 41.60  ? 475  GLU   A O    1 
ATOM   577  C  CB   . GLU   A 1 97  ? 13.671  -10.139 33.980  1.00 45.68  ? 475  GLU   A CB   1 
ATOM   578  C  CG   . GLU   A 1 97  ? 14.781  -9.801  33.041  1.00 57.55  ? 475  GLU   A CG   1 
ATOM   579  C  CD   . GLU   A 1 97  ? 15.524  -8.521  33.418  1.00 67.04  ? 475  GLU   A CD   1 
ATOM   580  O  OE1  . GLU   A 1 97  ? 15.248  -7.945  34.499  1.00 63.27  ? 475  GLU   A OE1  1 
ATOM   581  O  OE2  . GLU   A 1 97  ? 16.415  -8.114  32.636  1.00 69.74  ? 475  GLU   A OE2  1 
ATOM   582  N  N    . VAL   A 1 98  ? 10.992  -11.925 35.016  1.00 41.94  ? 476  VAL   A N    1 
ATOM   583  C  CA   . VAL   A 1 98  ? 9.698   -11.922 35.692  1.00 42.51  ? 476  VAL   A CA   1 
ATOM   584  C  C    . VAL   A 1 98  ? 9.860   -11.435 37.120  1.00 41.95  ? 476  VAL   A C    1 
ATOM   585  O  O    . VAL   A 1 98  ? 10.773  -11.871 37.829  1.00 36.81  ? 476  VAL   A O    1 
ATOM   586  C  CB   . VAL   A 1 98  ? 9.074   -13.328 35.678  1.00 40.08  ? 476  VAL   A CB   1 
ATOM   587  C  CG1  . VAL   A 1 98  ? 7.694   -13.291 36.303  1.00 39.03  ? 476  VAL   A CG1  1 
ATOM   588  C  CG2  . VAL   A 1 98  ? 9.022   -13.853 34.256  1.00 41.18  ? 476  VAL   A CG2  1 
ATOM   589  N  N    . HIS   A 1 99  ? 8.957   -10.555 37.561  1.00 36.30  ? 477  HIS   A N    1 
ATOM   590  C  CA   . HIS   A 1 99  ? 8.880   -10.218 38.971  1.00 36.22  ? 477  HIS   A CA   1 
ATOM   591  C  C    . HIS   A 1 99  ? 7.432   -10.180 39.424  1.00 35.66  ? 477  HIS   A C    1 
ATOM   592  O  O    . HIS   A 1 99  ? 6.510   -10.019 38.620  1.00 37.08  ? 477  HIS   A O    1 
ATOM   593  C  CB   . HIS   A 1 99  ? 9.581   -8.904  39.273  1.00 39.46  ? 477  HIS   A CB   1 
ATOM   594  C  CG   . HIS   A 1 99  ? 8.834   -7.693  38.822  1.00 40.26  ? 477  HIS   A CG   1 
ATOM   595  N  ND1  . HIS   A 1 99  ? 9.037   -7.126  37.583  1.00 43.05  ? 477  HIS   A ND1  1 
ATOM   596  C  CD2  . HIS   A 1 99  ? 7.925   -6.911  39.451  1.00 42.37  ? 477  HIS   A CD2  1 
ATOM   597  C  CE1  . HIS   A 1 99  ? 8.273   -6.054  37.461  1.00 44.64  ? 477  HIS   A CE1  1 
ATOM   598  N  NE2  . HIS   A 1 99  ? 7.593   -5.898  38.583  1.00 44.22  ? 477  HIS   A NE2  1 
ATOM   599  N  N    . LEU   A 1 100 ? 7.254   -10.340 40.737  1.00 38.26  ? 478  LEU   A N    1 
ATOM   600  C  CA   . LEU   A 1 100 ? 5.951   -10.278 41.385  1.00 37.73  ? 478  LEU   A CA   1 
ATOM   601  C  C    . LEU   A 1 100 ? 5.613   -8.834  41.740  1.00 36.41  ? 478  LEU   A C    1 
ATOM   602  O  O    . LEU   A 1 100 ? 6.455   -8.105  42.272  1.00 37.19  ? 478  LEU   A O    1 
ATOM   603  C  CB   . LEU   A 1 100 ? 5.931   -11.133 42.662  1.00 37.63  ? 478  LEU   A CB   1 
ATOM   604  C  CG   . LEU   A 1 100 ? 6.006   -12.673 42.653  1.00 34.27  ? 478  LEU   A CG   1 
ATOM   605  C  CD1  . LEU   A 1 100 ? 4.944   -13.281 41.708  1.00 40.42  ? 478  LEU   A CD1  1 
ATOM   606  C  CD2  . LEU   A 1 100 ? 7.375   -13.180 42.317  1.00 46.16  ? 478  LEU   A CD2  1 
ATOM   607  N  N    . VAL   A 1 101 ? 4.356   -8.441  41.483  1.00 37.95  ? 479  VAL   A N    1 
ATOM   608  C  CA   . VAL   A 1 101 ? 3.944   -7.061  41.717  1.00 32.12  ? 479  VAL   A CA   1 
ATOM   609  C  C    . VAL   A 1 101 ? 4.256   -6.674  43.152  1.00 39.17  ? 479  VAL   A C    1 
ATOM   610  O  O    . VAL   A 1 101 ? 3.902   -7.385  44.103  1.00 38.76  ? 479  VAL   A O    1 
ATOM   611  C  CB   . VAL   A 1 101 ? 2.455   -6.879  41.385  1.00 35.28  ? 479  VAL   A CB   1 
ATOM   612  C  CG1  . VAL   A 1 101 ? 1.594   -7.935  42.099  1.00 31.39  ? 479  VAL   A CG1  1 
ATOM   613  C  CG2  . VAL   A 1 101 ? 1.999   -5.436  41.691  1.00 34.85  ? 479  VAL   A CG2  1 
ATOM   614  N  N    . ALA   A 1 102 ? 4.949   -5.543  43.309  1.00 37.08  ? 480  ALA   A N    1 
ATOM   615  C  CA   . ALA   A 1 102 ? 5.497   -5.169  44.611  1.00 40.50  ? 480  ALA   A CA   1 
ATOM   616  C  C    . ALA   A 1 102 ? 4.416   -5.045  45.687  1.00 41.82  ? 480  ALA   A C    1 
ATOM   617  O  O    . ALA   A 1 102 ? 4.646   -5.420  46.844  1.00 40.02  ? 480  ALA   A O    1 
ATOM   618  C  CB   . ALA   A 1 102 ? 6.288   -3.862  44.489  1.00 45.40  ? 480  ALA   A CB   1 
ATOM   619  N  N    . ASP   A 1 103 ? 3.238   -4.511  45.347  1.00 43.11  ? 481  ASP   A N    1 
ATOM   620  C  CA   . ASP   A 1 103 ? 2.239   -4.262  46.383  1.00 40.40  ? 481  ASP   A CA   1 
ATOM   621  C  C    . ASP   A 1 103 ? 1.218   -5.380  46.479  1.00 39.39  ? 481  ASP   A C    1 
ATOM   622  O  O    . ASP   A 1 103 ? 0.265   -5.267  47.259  1.00 36.69  ? 481  ASP   A O    1 
ATOM   623  C  CB   . ASP   A 1 103 ? 1.528   -2.898  46.174  1.00 41.45  ? 481  ASP   A CB   1 
ATOM   624  C  CG   . ASP   A 1 103 ? 0.619   -2.858  44.941  1.00 38.57  ? 481  ASP   A CG   1 
ATOM   625  O  OD1  . ASP   A 1 103 ? 0.502   -3.887  44.221  1.00 37.30  ? 481  ASP   A OD1  1 
ATOM   626  O  OD2  . ASP   A 1 103 ? 0.013   -1.774  44.681  1.00 37.66  ? 481  ASP   A OD2  1 
ATOM   627  N  N    . GLY   A 1 104 ? 1.403   -6.451  45.708  1.00 37.38  ? 482  GLY   A N    1 
ATOM   628  C  CA   . GLY   A 1 104 ? 0.535   -7.607  45.762  1.00 37.07  ? 482  GLY   A CA   1 
ATOM   629  C  C    . GLY   A 1 104 ? -0.853  -7.441  45.173  1.00 36.94  ? 482  GLY   A C    1 
ATOM   630  O  O    . GLY   A 1 104 ? -1.675  -8.345  45.338  1.00 35.04  ? 482  GLY   A O    1 
ATOM   631  N  N    . LYS   A 1 105 ? -1.136  -6.343  44.467  1.00 31.36  ? 483  LYS   A N    1 
ATOM   632  C  CA   . LYS   A 1 105 ? -2.487  -6.048  44.015  1.00 32.08  ? 483  LYS   A CA   1 
ATOM   633  C  C    . LYS   A 1 105 ? -2.600  -6.145  42.495  1.00 34.11  ? 483  LYS   A C    1 
ATOM   634  O  O    . LYS   A 1 105 ? -1.616  -6.024  41.762  1.00 31.97  ? 483  LYS   A O    1 
ATOM   635  C  CB   . LYS   A 1 105 ? -2.914  -4.652  44.495  1.00 38.34  ? 483  LYS   A CB   1 
ATOM   636  C  CG   . LYS   A 1 105 ? -2.879  -4.461  46.014  1.00 36.75  ? 483  LYS   A CG   1 
ATOM   637  C  CD   . LYS   A 1 105 ? -3.794  -5.464  46.728  1.00 42.75  ? 483  LYS   A CD   1 
ATOM   638  C  CE   . LYS   A 1 105 ? -3.964  -5.142  48.228  1.00 41.04  ? 483  LYS   A CE   1 
ATOM   639  N  NZ   . LYS   A 1 105 ? -2.715  -5.203  49.030  1.00 41.75  ? 483  LYS   A NZ   1 
ATOM   640  N  N    . PHE   A 1 106 ? -3.831  -6.381  42.027  1.00 32.81  ? 484  PHE   A N    1 
ATOM   641  C  CA   . PHE   A 1 106 ? -4.079  -6.465  40.592  1.00 31.37  ? 484  PHE   A CA   1 
ATOM   642  C  C    . PHE   A 1 106 ? -4.042  -5.083  39.944  1.00 32.83  ? 484  PHE   A C    1 
ATOM   643  O  O    . PHE   A 1 106 ? -3.354  -4.875  38.940  1.00 32.35  ? 484  PHE   A O    1 
ATOM   644  C  CB   . PHE   A 1 106 ? -5.427  -7.151  40.338  1.00 32.97  ? 484  PHE   A CB   1 
ATOM   645  C  CG   . PHE   A 1 106 ? -5.374  -8.664  40.368  1.00 31.72  ? 484  PHE   A CG   1 
ATOM   646  C  CD1  . PHE   A 1 106 ? -5.138  -9.391  39.212  1.00 28.66  ? 484  PHE   A CD1  1 
ATOM   647  C  CD2  . PHE   A 1 106 ? -5.603  -9.352  41.549  1.00 30.38  ? 484  PHE   A CD2  1 
ATOM   648  C  CE1  . PHE   A 1 106 ? -5.101  -10.786 39.243  1.00 30.48  ? 484  PHE   A CE1  1 
ATOM   649  C  CE2  . PHE   A 1 106 ? -5.582  -10.736 41.587  1.00 31.60  ? 484  PHE   A CE2  1 
ATOM   650  C  CZ   . PHE   A 1 106 ? -5.336  -11.458 40.429  1.00 31.43  ? 484  PHE   A CZ   1 
ATOM   651  N  N    . GLY   A 1 107 ? -4.809  -4.129  40.472  1.00 35.15  ? 485  GLY   A N    1 
ATOM   652  C  CA   . GLY   A 1 107 ? -4.698  -2.791  39.948  1.00 32.20  ? 485  GLY   A CA   1 
ATOM   653  C  C    . GLY   A 1 107 ? -6.015  -2.073  39.771  1.00 36.54  ? 485  GLY   A C    1 
ATOM   654  O  O    . GLY   A 1 107 ? -6.835  -2.460  38.933  1.00 35.61  ? 485  GLY   A O    1 
ATOM   655  N  N    . THR   A 1 108 ? -6.229  -1.038  40.576  1.00 35.90  ? 486  THR   A N    1 
ATOM   656  C  CA   . THR   A 1 108 ? -7.355  -0.128  40.423  1.00 37.06  ? 486  THR   A CA   1 
ATOM   657  C  C    . THR   A 1 108 ? -6.843  1.304   40.472  1.00 39.93  ? 486  THR   A C    1 
ATOM   658  O  O    . THR   A 1 108 ? -5.720  1.571   40.917  1.00 37.96  ? 486  THR   A O    1 
ATOM   659  C  CB   . THR   A 1 108 ? -8.406  -0.357  41.510  1.00 39.41  ? 486  THR   A CB   1 
ATOM   660  O  OG1  . THR   A 1 108 ? -7.851  -0.059  42.794  1.00 37.43  ? 486  THR   A OG1  1 
ATOM   661  C  CG2  . THR   A 1 108 ? -8.866  -1.801  41.492  1.00 37.15  ? 486  THR   A CG2  1 
ATOM   662  N  N    . GLN   A 1 109 ? -7.685  2.231   40.007  1.00 38.70  ? 487  GLN   A N    1 
ATOM   663  C  CA   . GLN   A 1 109 ? -7.365  3.648   40.027  1.00 40.25  ? 487  GLN   A CA   1 
ATOM   664  C  C    . GLN   A 1 109 ? -8.066  4.274   41.223  1.00 43.85  ? 487  GLN   A C    1 
ATOM   665  O  O    . GLN   A 1 109 ? -9.297  4.307   41.267  1.00 43.28  ? 487  GLN   A O    1 
ATOM   666  C  CB   . GLN   A 1 109 ? -7.800  4.325   38.723  1.00 40.92  ? 487  GLN   A CB   1 
ATOM   667  C  CG   . GLN   A 1 109 ? -7.249  5.753   38.583  1.00 45.78  ? 487  GLN   A CG   1 
ATOM   668  C  CD   . GLN   A 1 109 ? -7.554  6.391   37.238  1.00 48.19  ? 487  GLN   A CD   1 
ATOM   669  O  OE1  . GLN   A 1 109 ? -8.594  6.127   36.635  1.00 42.88  ? 487  GLN   A OE1  1 
ATOM   670  N  NE2  . GLN   A 1 109 ? -6.657  7.262   36.777  1.00 45.30  ? 487  GLN   A NE2  1 
ATOM   671  N  N    . GLU   A 1 110 ? -7.291  4.754   42.192  1.00 43.76  ? 488  GLU   A N    1 
ATOM   672  C  CA   . GLU   A 1 110 ? -7.864  5.342   43.408  1.00 46.61  ? 488  GLU   A CA   1 
ATOM   673  C  C    . GLU   A 1 110 ? -7.696  6.865   43.446  1.00 45.97  ? 488  GLU   A C    1 
ATOM   674  O  O    . GLU   A 1 110 ? -6.595  7.378   43.256  1.00 44.31  ? 488  GLU   A O    1 
ATOM   675  C  CB   . GLU   A 1 110 ? -7.233  4.712   44.661  1.00 48.40  ? 488  GLU   A CB   1 
ATOM   676  C  CG   . GLU   A 1 110 ? -7.410  3.190   44.777  1.00 47.27  ? 488  GLU   A CG   1 
ATOM   677  C  CD   . GLU   A 1 110 ? -8.877  2.772   44.779  1.00 54.25  ? 488  GLU   A CD   1 
ATOM   678  O  OE1  . GLU   A 1 110 ? -9.697  3.522   45.347  1.00 53.37  ? 488  GLU   A OE1  1 
ATOM   679  O  OE2  . GLU   A 1 110 ? -9.210  1.702   44.210  1.00 53.68  ? 488  GLU   A OE2  1 
ATOM   680  N  N    . ASN   A 1 116 ? -8.583  14.716  44.684  1.00 75.22  ? 494  ASN   A N    1 
ATOM   681  C  CA   . ASN   A 1 116 ? -8.330  15.416  43.426  1.00 74.55  ? 494  ASN   A CA   1 
ATOM   682  C  C    . ASN   A 1 116 ? -7.673  14.534  42.357  1.00 77.58  ? 494  ASN   A C    1 
ATOM   683  O  O    . ASN   A 1 116 ? -8.312  14.154  41.373  1.00 77.83  ? 494  ASN   A O    1 
ATOM   684  C  CB   . ASN   A 1 116 ? -7.467  16.643  43.686  1.00 78.46  ? 494  ASN   A CB   1 
ATOM   685  C  CG   . ASN   A 1 116 ? -7.228  17.461  42.432  1.00 81.98  ? 494  ASN   A CG   1 
ATOM   686  O  OD1  . ASN   A 1 116 ? -7.902  17.278  41.418  1.00 82.27  ? 494  ASN   A OD1  1 
ATOM   687  N  ND2  . ASN   A 1 116 ? -6.304  18.413  42.515  1.00 83.49  ? 494  ASN   A ND2  1 
ATOM   688  N  N    . LYS   A 1 117 ? -6.390  14.239  42.541  1.00 72.31  ? 495  LYS   A N    1 
ATOM   689  C  CA   . LYS   A 1 117 ? -5.665  13.382  41.618  1.00 70.51  ? 495  LYS   A CA   1 
ATOM   690  C  C    . LYS   A 1 117 ? -6.043  11.913  41.838  1.00 63.42  ? 495  LYS   A C    1 
ATOM   691  O  O    . LYS   A 1 117 ? -6.518  11.519  42.907  1.00 60.27  ? 495  LYS   A O    1 
ATOM   692  C  CB   . LYS   A 1 117 ? -4.158  13.585  41.786  1.00 65.62  ? 495  LYS   A CB   1 
ATOM   693  N  N    . LYS   A 1 118 ? -5.838  11.105  40.798  1.00 60.96  ? 496  LYS   A N    1 
ATOM   694  C  CA   . LYS   A 1 118 ? -6.053  9.666   40.852  1.00 54.35  ? 496  LYS   A CA   1 
ATOM   695  C  C    . LYS   A 1 118 ? -4.778  8.943   40.424  1.00 58.06  ? 496  LYS   A C    1 
ATOM   696  O  O    . LYS   A 1 118 ? -3.985  9.464   39.633  1.00 60.26  ? 496  LYS   A O    1 
ATOM   697  C  CB   . LYS   A 1 118 ? -7.223  9.241   39.961  1.00 52.07  ? 496  LYS   A CB   1 
ATOM   698  N  N    . GLU   A 1 119 ? -4.587  7.736   40.961  1.00 49.27  ? 497  GLU   A N    1 
ATOM   699  C  CA   . GLU   A 1 119 ? -3.383  6.945   40.743  1.00 49.30  ? 497  GLU   A CA   1 
ATOM   700  C  C    . GLU   A 1 119 ? -3.736  5.473   40.596  1.00 42.68  ? 497  GLU   A C    1 
ATOM   701  O  O    . GLU   A 1 119 ? -4.659  4.973   41.243  1.00 43.02  ? 497  GLU   A O    1 
ATOM   702  C  CB   . GLU   A 1 119 ? -2.403  7.094   41.910  1.00 55.52  ? 497  GLU   A CB   1 
ATOM   703  C  CG   . GLU   A 1 119 ? -2.622  6.036   42.980  1.00 53.73  ? 497  GLU   A CG   1 
ATOM   704  C  CD   . GLU   A 1 119 ? -1.698  6.206   44.139  1.00 63.62  ? 497  GLU   A CD   1 
ATOM   705  O  OE1  . GLU   A 1 119 ? -1.280  7.360   44.314  1.00 66.32  ? 497  GLU   A OE1  1 
ATOM   706  O  OE2  . GLU   A 1 119 ? -1.427  5.227   44.876  1.00 63.72  ? 497  GLU   A OE2  1 
ATOM   707  N  N    . TRP   A 1 120 ? -2.950  4.769   39.780  1.00 42.04  ? 498  TRP   A N    1 
ATOM   708  C  CA   . TRP   A 1 120 ? -3.073  3.321   39.620  1.00 41.23  ? 498  TRP   A CA   1 
ATOM   709  C  C    . TRP   A 1 120 ? -2.115  2.611   40.574  1.00 43.11  ? 498  TRP   A C    1 
ATOM   710  O  O    . TRP   A 1 120 ? -0.946  2.996   40.700  1.00 43.51  ? 498  TRP   A O    1 
ATOM   711  C  CB   . TRP   A 1 120 ? -2.765  2.904   38.182  1.00 39.53  ? 498  TRP   A CB   1 
ATOM   712  C  CG   . TRP   A 1 120 ? -3.855  3.209   37.205  1.00 41.32  ? 498  TRP   A CG   1 
ATOM   713  C  CD1  . TRP   A 1 120 ? -3.950  4.318   36.406  1.00 41.82  ? 498  TRP   A CD1  1 
ATOM   714  C  CD2  . TRP   A 1 120 ? -5.008  2.412   36.924  1.00 37.81  ? 498  TRP   A CD2  1 
ATOM   715  N  NE1  . TRP   A 1 120 ? -5.084  4.250   35.640  1.00 41.95  ? 498  TRP   A NE1  1 
ATOM   716  C  CE2  . TRP   A 1 120 ? -5.754  3.090   35.939  1.00 36.99  ? 498  TRP   A CE2  1 
ATOM   717  C  CE3  . TRP   A 1 120 ? -5.483  1.190   37.412  1.00 36.25  ? 498  TRP   A CE3  1 
ATOM   718  C  CZ2  . TRP   A 1 120 ? -6.948  2.587   35.427  1.00 40.01  ? 498  TRP   A CZ2  1 
ATOM   719  C  CZ3  . TRP   A 1 120 ? -6.667  0.688   36.906  1.00 35.89  ? 498  TRP   A CZ3  1 
ATOM   720  C  CH2  . TRP   A 1 120 ? -7.394  1.388   35.929  1.00 40.14  ? 498  TRP   A CH2  1 
ATOM   721  N  N    . ASN   A 1 121 ? -2.609  1.588   41.241  1.00 41.14  ? 499  ASN   A N    1 
ATOM   722  C  CA   . ASN   A 1 121 ? -1.815  0.707   42.079  1.00 40.30  ? 499  ASN   A CA   1 
ATOM   723  C  C    . ASN   A 1 121 ? -1.565  -0.605  41.332  1.00 35.50  ? 499  ASN   A C    1 
ATOM   724  O  O    . ASN   A 1 121 ? -1.912  -0.747  40.150  1.00 35.21  ? 499  ASN   A O    1 
ATOM   725  C  CB   . ASN   A 1 121 ? -2.551  0.489   43.400  1.00 43.00  ? 499  ASN   A CB   1 
ATOM   726  C  CG   . ASN   A 1 121 ? -3.984  0.041   43.189  1.00 39.39  ? 499  ASN   A CG   1 
ATOM   727  O  OD1  . ASN   A 1 121 ? -4.240  -0.897  42.437  1.00 41.31  ? 499  ASN   A OD1  1 
ATOM   728  N  ND2  . ASN   A 1 121 ? -4.929  0.709   43.854  1.00 39.64  ? 499  ASN   A ND2  1 
ATOM   729  N  N    . GLY   A 1 122 ? -0.985  -1.577  42.032  1.00 36.98  ? 500  GLY   A N    1 
ATOM   730  C  CA   . GLY   A 1 122 ? -0.902  -2.951  41.540  1.00 32.89  ? 500  GLY   A CA   1 
ATOM   731  C  C    . GLY   A 1 122 ? -0.123  -3.079  40.241  1.00 32.66  ? 500  GLY   A C    1 
ATOM   732  O  O    . GLY   A 1 122 ? 0.741   -2.260  39.909  1.00 36.07  ? 500  GLY   A O    1 
ATOM   733  N  N    . MET   A 1 123 ? -0.452  -4.129  39.480  1.00 36.09  ? 501  MET   A N    1 
ATOM   734  C  CA   . MET   A 1 123 ? 0.258   -4.385  38.236  1.00 33.03  ? 501  MET   A CA   1 
ATOM   735  C  C    . MET   A 1 123 ? -0.002  -3.279  37.242  1.00 36.24  ? 501  MET   A C    1 
ATOM   736  O  O    . MET   A 1 123 ? 0.844   -2.987  36.393  1.00 35.84  ? 501  MET   A O    1 
ATOM   737  C  CB   . MET   A 1 123 ? -0.203  -5.711  37.656  1.00 30.82  ? 501  MET   A CB   1 
ATOM   738  C  CG   . MET   A 1 123 ? -0.135  -6.835  38.678  1.00 33.86  ? 501  MET   A CG   1 
ATOM   739  S  SD   . MET   A 1 123 ? -0.115  -8.433  37.878  1.00 34.10  ? 501  MET   A SD   1 
ATOM   740  C  CE   . MET   A 1 123 ? -1.898  -8.646  38.015  1.00 28.67  ? 501  MET   A CE   1 
ATOM   741  N  N    . MET   A 1 124 ? -1.177  -2.659  37.335  1.00 32.25  ? 502  MET   A N    1 
ATOM   742  C  CA   . MET   A 1 124 ? -1.504  -1.569  36.428  1.00 35.75  ? 502  MET   A CA   1 
ATOM   743  C  C    . MET   A 1 124 ? -0.547  -0.407  36.641  1.00 32.90  ? 502  MET   A C    1 
ATOM   744  O  O    . MET   A 1 124 ? -0.023  0.168   35.680  1.00 37.88  ? 502  MET   A O    1 
ATOM   745  C  CB   . MET   A 1 124 ? -2.941  -1.107  36.653  1.00 30.19  ? 502  MET   A CB   1 
ATOM   746  C  CG   . MET   A 1 124 ? -3.968  -2.072  36.093  1.00 36.19  ? 502  MET   A CG   1 
ATOM   747  S  SD   . MET   A 1 124 ? -4.050  -2.006  34.304  1.00 36.73  ? 502  MET   A SD   1 
ATOM   748  C  CE   . MET   A 1 124 ? -4.501  -0.291  34.033  1.00 37.42  ? 502  MET   A CE   1 
ATOM   749  N  N    . GLY   A 1 125 ? -0.304  -0.055  37.906  1.00 34.77  ? 503  GLY   A N    1 
ATOM   750  C  CA   . GLY   A 1 125 ? 0.614   1.037   38.208  1.00 39.77  ? 503  GLY   A CA   1 
ATOM   751  C  C    . GLY   A 1 125 ? 2.035   0.744   37.759  1.00 39.45  ? 503  GLY   A C    1 
ATOM   752  O  O    . GLY   A 1 125 ? 2.709   1.616   37.208  1.00 39.49  ? 503  GLY   A O    1 
ATOM   753  N  N    . GLU   A 1 126 ? 2.489   -0.499  37.956  1.00 35.74  ? 504  GLU   A N    1 
ATOM   754  C  CA   . GLU   A 1 126 ? 3.822   -0.905  37.507  1.00 40.37  ? 504  GLU   A CA   1 
ATOM   755  C  C    . GLU   A 1 126 ? 3.944   -0.859  35.985  1.00 39.84  ? 504  GLU   A C    1 
ATOM   756  O  O    . GLU   A 1 126 ? 4.960   -0.397  35.463  1.00 40.96  ? 504  GLU   A O    1 
ATOM   757  C  CB   . GLU   A 1 126 ? 4.155   -2.306  38.026  1.00 39.80  ? 504  GLU   A CB   1 
ATOM   758  C  CG   . GLU   A 1 126 ? 4.255   -2.383  39.544  1.00 43.05  ? 504  GLU   A CG   1 
ATOM   759  C  CD   . GLU   A 1 126 ? 5.229   -3.442  40.052  1.00 46.65  ? 504  GLU   A CD   1 
ATOM   760  O  OE1  . GLU   A 1 126 ? 5.865   -4.121  39.225  1.00 44.15  ? 504  GLU   A OE1  1 
ATOM   761  O  OE2  . GLU   A 1 126 ? 5.351   -3.599  41.285  1.00 42.14  ? 504  GLU   A OE2  1 
ATOM   762  N  N    . LEU   A 1 127 ? 2.914   -1.306  35.247  1.00 39.06  ? 505  LEU   A N    1 
ATOM   763  C  CA   . LEU   A 1 127 ? 3.005   -1.232  33.787  1.00 34.54  ? 505  LEU   A CA   1 
ATOM   764  C  C    . LEU   A 1 127 ? 3.018   0.224   33.311  1.00 40.05  ? 505  LEU   A C    1 
ATOM   765  O  O    . LEU   A 1 127 ? 3.765   0.586   32.384  1.00 36.68  ? 505  LEU   A O    1 
ATOM   766  C  CB   . LEU   A 1 127 ? 1.851   -2.007  33.140  1.00 39.15  ? 505  LEU   A CB   1 
ATOM   767  C  CG   . LEU   A 1 127 ? 1.819   -2.038  31.601  1.00 37.07  ? 505  LEU   A CG   1 
ATOM   768  C  CD1  . LEU   A 1 127 ? 3.021   -2.788  31.055  1.00 39.78  ? 505  LEU   A CD1  1 
ATOM   769  C  CD2  . LEU   A 1 127 ? 0.531   -2.643  31.048  1.00 36.27  ? 505  LEU   A CD2  1 
ATOM   770  N  N    . LEU   A 1 128 ? 2.221   1.081   33.952  1.00 33.52  ? 506  LEU   A N    1 
ATOM   771  C  CA   . LEU   A 1 128 ? 2.141   2.473   33.523  1.00 39.26  ? 506  LEU   A CA   1 
ATOM   772  C  C    . LEU   A 1 128 ? 3.375   3.262   33.913  1.00 42.14  ? 506  LEU   A C    1 
ATOM   773  O  O    . LEU   A 1 128 ? 3.730   4.220   33.217  1.00 46.06  ? 506  LEU   A O    1 
ATOM   774  C  CB   . LEU   A 1 128 ? 0.900   3.152   34.106  1.00 37.65  ? 506  LEU   A CB   1 
ATOM   775  C  CG   . LEU   A 1 128 ? -0.413  2.674   33.457  1.00 38.58  ? 506  LEU   A CG   1 
ATOM   776  C  CD1  . LEU   A 1 128 ? -1.624  3.239   34.176  1.00 35.90  ? 506  LEU   A CD1  1 
ATOM   777  C  CD2  . LEU   A 1 128 ? -0.427  3.039   31.982  1.00 40.17  ? 506  LEU   A CD2  1 
ATOM   778  N  N    . SER   A 1 129 ? 4.034   2.891   35.008  1.00 41.35  ? 507  SER   A N    1 
ATOM   779  C  CA   . SER   A 1 129 ? 5.238   3.598   35.417  1.00 46.04  ? 507  SER   A CA   1 
ATOM   780  C  C    . SER   A 1 129 ? 6.494   3.085   34.720  1.00 45.60  ? 507  SER   A C    1 
ATOM   781  O  O    . SER   A 1 129 ? 7.556   3.691   34.872  1.00 44.80  ? 507  SER   A O    1 
ATOM   782  C  CB   . SER   A 1 129 ? 5.429   3.485   36.927  1.00 46.28  ? 507  SER   A CB   1 
ATOM   783  O  OG   . SER   A 1 129 ? 5.726   2.145   37.266  1.00 47.27  ? 507  SER   A OG   1 
ATOM   784  N  N    . GLY   A 1 130 ? 6.404   1.997   33.957  1.00 45.51  ? 508  GLY   A N    1 
ATOM   785  C  CA   . GLY   A 1 130 ? 7.582   1.414   33.348  1.00 45.07  ? 508  GLY   A CA   1 
ATOM   786  C  C    . GLY   A 1 130 ? 8.311   0.395   34.203  1.00 45.91  ? 508  GLY   A C    1 
ATOM   787  O  O    . GLY   A 1 130 ? 9.315   -0.170  33.743  1.00 44.63  ? 508  GLY   A O    1 
ATOM   788  N  N    . GLN   A 1 131 ? 7.846   0.142   35.432  1.00 44.00  ? 509  GLN   A N    1 
ATOM   789  C  CA   . GLN   A 1 131 ? 8.416   -0.943  36.223  1.00 44.76  ? 509  GLN   A CA   1 
ATOM   790  C  C    . GLN   A 1 131 ? 8.183   -2.297  35.569  1.00 44.49  ? 509  GLN   A C    1 
ATOM   791  O  O    . GLN   A 1 131 ? 8.883   -3.261  35.892  1.00 42.88  ? 509  GLN   A O    1 
ATOM   792  C  CB   . GLN   A 1 131 ? 7.813   -0.964  37.621  1.00 46.18  ? 509  GLN   A CB   1 
ATOM   793  C  CG   . GLN   A 1 131 ? 8.404   0.026   38.580  1.00 52.81  ? 509  GLN   A CG   1 
ATOM   794  C  CD   . GLN   A 1 131 ? 7.461   0.300   39.731  1.00 54.89  ? 509  GLN   A CD   1 
ATOM   795  O  OE1  . GLN   A 1 131 ? 6.668   1.230   39.682  1.00 57.08  ? 509  GLN   A OE1  1 
ATOM   796  N  NE2  . GLN   A 1 131 ? 7.563   -0.500  40.791  1.00 55.41  ? 509  GLN   A NE2  1 
ATOM   797  N  N    . ALA   A 1 132 ? 7.190   -2.394  34.687  1.00 39.33  ? 510  ALA   A N    1 
ATOM   798  C  CA   . ALA   A 1 132 ? 6.959   -3.570  33.860  1.00 39.57  ? 510  ALA   A CA   1 
ATOM   799  C  C    . ALA   A 1 132 ? 6.670   -3.130  32.436  1.00 40.77  ? 510  ALA   A C    1 
ATOM   800  O  O    . ALA   A 1 132 ? 6.210   -2.007  32.196  1.00 40.26  ? 510  ALA   A O    1 
ATOM   801  C  CB   . ALA   A 1 132 ? 5.790   -4.415  34.360  1.00 37.77  ? 510  ALA   A CB   1 
ATOM   802  N  N    . ASP   A 1 133 ? 6.952   -4.028  31.490  1.00 38.56  ? 511  ASP   A N    1 
ATOM   803  C  CA   . ASP   A 1 133 ? 6.611   -3.827  30.089  1.00 38.57  ? 511  ASP   A CA   1 
ATOM   804  C  C    . ASP   A 1 133 ? 5.411   -4.647  29.652  1.00 38.31  ? 511  ASP   A C    1 
ATOM   805  O  O    . ASP   A 1 133 ? 4.788   -4.321  28.633  1.00 37.91  ? 511  ASP   A O    1 
ATOM   806  C  CB   . ASP   A 1 133 ? 7.794   -4.205  29.194  1.00 42.85  ? 511  ASP   A CB   1 
ATOM   807  C  CG   . ASP   A 1 133 ? 9.047   -3.429  29.527  1.00 46.54  ? 511  ASP   A CG   1 
ATOM   808  O  OD1  . ASP   A 1 133 ? 8.961   -2.183  29.693  1.00 45.31  ? 511  ASP   A OD1  1 
ATOM   809  O  OD2  . ASP   A 1 133 ? 10.109  -4.080  29.660  1.00 43.07  ? 511  ASP   A OD2  1 
ATOM   810  N  N    . MET   A 1 134 ? 5.088   -5.707  30.384  1.00 37.58  ? 512  MET   A N    1 
ATOM   811  C  CA   . MET   A 1 134 ? 3.967   -6.562  30.037  1.00 34.46  ? 512  MET   A CA   1 
ATOM   812  C  C    . MET   A 1 134 ? 3.431   -7.171  31.319  1.00 36.46  ? 512  MET   A C    1 
ATOM   813  O  O    . MET   A 1 134 ? 4.210   -7.540  32.204  1.00 34.00  ? 512  MET   A O    1 
ATOM   814  C  CB   . MET   A 1 134 ? 4.394   -7.663  29.068  1.00 36.21  ? 512  MET   A CB   1 
ATOM   815  C  CG   . MET   A 1 134 ? 3.264   -8.614  28.658  1.00 38.19  ? 512  MET   A CG   1 
ATOM   816  S  SD   . MET   A 1 134 ? 3.920   -9.878  27.541  1.00 41.85  ? 512  MET   A SD   1 
ATOM   817  C  CE   . MET   A 1 134 ? 4.175   -8.871  26.084  1.00 47.97  ? 512  MET   A CE   1 
ATOM   818  N  N    . ILE   A 1 135 ? 2.106   -7.276  31.408  1.00 31.23  ? 513  ILE   A N    1 
ATOM   819  C  CA   . ILE   A 1 135 ? 1.431   -7.961  32.506  1.00 29.97  ? 513  ILE   A CA   1 
ATOM   820  C  C    . ILE   A 1 135 ? 0.994   -9.324  32.001  1.00 30.42  ? 513  ILE   A C    1 
ATOM   821  O  O    . ILE   A 1 135 ? 0.170   -9.412  31.083  1.00 29.25  ? 513  ILE   A O    1 
ATOM   822  C  CB   . ILE   A 1 135 ? 0.202   -7.179  33.004  1.00 29.38  ? 513  ILE   A CB   1 
ATOM   823  C  CG1  . ILE   A 1 135 ? 0.555   -5.748  33.415  1.00 32.09  ? 513  ILE   A CG1  1 
ATOM   824  C  CG2  . ILE   A 1 135 ? -0.501  -7.957  34.144  1.00 32.90  ? 513  ILE   A CG2  1 
ATOM   825  C  CD1  . ILE   A 1 135 ? -0.666  -4.948  33.858  1.00 28.47  ? 513  ILE   A CD1  1 
ATOM   826  N  N    . VAL   A 1 136 ? 1.516   -10.384 32.603  1.00 33.06  ? 514  VAL   A N    1 
ATOM   827  C  CA   . VAL   A 1 136 ? 1.101   -11.750 32.274  1.00 33.26  ? 514  VAL   A CA   1 
ATOM   828  C  C    . VAL   A 1 136 ? 0.551   -12.335 33.566  1.00 34.07  ? 514  VAL   A C    1 
ATOM   829  O  O    . VAL   A 1 136 ? 1.317   -12.741 34.455  1.00 33.24  ? 514  VAL   A O    1 
ATOM   830  C  CB   . VAL   A 1 136 ? 2.254   -12.591 31.711  1.00 28.29  ? 514  VAL   A CB   1 
ATOM   831  C  CG1  . VAL   A 1 136 ? 1.766   -13.982 31.344  1.00 34.42  ? 514  VAL   A CG1  1 
ATOM   832  C  CG2  . VAL   A 1 136 ? 2.860   -11.900 30.474  1.00 31.56  ? 514  VAL   A CG2  1 
ATOM   833  N  N    . ALA   A 1 137 ? -0.780  -12.344 33.691  1.00 31.64  ? 515  ALA   A N    1 
ATOM   834  C  CA   . ALA   A 1 137 ? -1.492  -12.693 34.914  1.00 30.76  ? 515  ALA   A CA   1 
ATOM   835  C  C    . ALA   A 1 137 ? -2.968  -12.909 34.602  1.00 30.28  ? 515  ALA   A C    1 
ATOM   836  O  O    . ALA   A 1 137 ? -3.417  -12.563 33.502  1.00 31.29  ? 515  ALA   A O    1 
ATOM   837  C  CB   . ALA   A 1 137 ? -1.341  -11.581 35.953  1.00 31.86  ? 515  ALA   A CB   1 
ATOM   838  N  N    . PRO   A 1 138 ? -3.771  -13.439 35.543  1.00 31.06  ? 516  PRO   A N    1 
ATOM   839  C  CA   . PRO   A 1 138 ? -5.227  -13.463 35.322  1.00 29.75  ? 516  PRO   A CA   1 
ATOM   840  C  C    . PRO   A 1 138 ? -5.838  -12.073 35.471  1.00 31.25  ? 516  PRO   A C    1 
ATOM   841  O  O    . PRO   A 1 138 ? -6.573  -11.801 36.427  1.00 31.48  ? 516  PRO   A O    1 
ATOM   842  C  CB   . PRO   A 1 138 ? -5.740  -14.433 36.396  1.00 32.85  ? 516  PRO   A CB   1 
ATOM   843  C  CG   . PRO   A 1 138 ? -4.700  -14.406 37.473  1.00 30.15  ? 516  PRO   A CG   1 
ATOM   844  C  CD   . PRO   A 1 138 ? -3.377  -14.200 36.741  1.00 30.21  ? 516  PRO   A CD   1 
ATOM   845  N  N    . LEU   A 1 139 ? -5.543  -11.199 34.511  1.00 32.81  ? 517  LEU   A N    1 
ATOM   846  C  CA   . LEU   A 1 139 ? -5.857  -9.772  34.589  1.00 31.58  ? 517  LEU   A CA   1 
ATOM   847  C  C    . LEU   A 1 139 ? -7.149  -9.490  33.830  1.00 31.28  ? 517  LEU   A C    1 
ATOM   848  O  O    . LEU   A 1 139 ? -7.179  -9.562  32.595  1.00 30.60  ? 517  LEU   A O    1 
ATOM   849  C  CB   . LEU   A 1 139 ? -4.711  -8.943  34.012  1.00 30.91  ? 517  LEU   A CB   1 
ATOM   850  C  CG   . LEU   A 1 139 ? -4.920  -7.416  34.017  1.00 32.58  ? 517  LEU   A CG   1 
ATOM   851  C  CD1  . LEU   A 1 139 ? -4.818  -6.858  35.429  1.00 31.49  ? 517  LEU   A CD1  1 
ATOM   852  C  CD2  . LEU   A 1 139 ? -3.918  -6.745  33.098  1.00 33.63  ? 517  LEU   A CD2  1 
ATOM   853  N  N    . THR   A 1 140 ? -8.196  -9.134  34.565  1.00 24.94  ? 518  THR   A N    1 
ATOM   854  C  CA   . THR   A 1 140 ? -9.509  -8.920  33.964  1.00 30.39  ? 518  THR   A CA   1 
ATOM   855  C  C    . THR   A 1 140 ? -9.549  -7.671  33.085  1.00 32.50  ? 518  THR   A C    1 
ATOM   856  O  O    . THR   A 1 140 ? -9.083  -6.593  33.472  1.00 32.48  ? 518  THR   A O    1 
ATOM   857  C  CB   . THR   A 1 140 ? -10.568 -8.805  35.059  1.00 29.32  ? 518  THR   A CB   1 
ATOM   858  O  OG1  . THR   A 1 140 ? -10.679 -10.060 35.744  1.00 30.86  ? 518  THR   A OG1  1 
ATOM   859  C  CG2  . THR   A 1 140 ? -11.912 -8.408  34.455  1.00 29.24  ? 518  THR   A CG2  1 
ATOM   860  N  N    . ILE   A 1 141 ? -10.149 -7.825  31.909  1.00 32.92  ? 519  ILE   A N    1 
ATOM   861  C  CA   . ILE   A 1 141 ? -10.385 -6.727  30.976  1.00 29.47  ? 519  ILE   A CA   1 
ATOM   862  C  C    . ILE   A 1 141 ? -11.622 -5.940  31.420  1.00 33.61  ? 519  ILE   A C    1 
ATOM   863  O  O    . ILE   A 1 141 ? -12.736 -6.478  31.458  1.00 33.00  ? 519  ILE   A O    1 
ATOM   864  C  CB   . ILE   A 1 141 ? -10.564 -7.283  29.553  1.00 32.29  ? 519  ILE   A CB   1 
ATOM   865  C  CG1  . ILE   A 1 141 ? -9.338  -8.129  29.143  1.00 30.59  ? 519  ILE   A CG1  1 
ATOM   866  C  CG2  . ILE   A 1 141 ? -10.809 -6.145  28.572  1.00 35.93  ? 519  ILE   A CG2  1 
ATOM   867  C  CD1  . ILE   A 1 141 ? -9.572  -9.033  27.853  1.00 29.63  ? 519  ILE   A CD1  1 
ATOM   868  N  N    . ASN   A 1 142 ? -11.446 -4.649  31.716  1.00 33.51  ? 520  ASN   A N    1 
ATOM   869  C  CA   . ASN   A 1 142 ? -12.589 -3.793  32.014  1.00 29.58  ? 520  ASN   A CA   1 
ATOM   870  C  C    . ASN   A 1 142 ? -12.345 -2.417  31.420  1.00 30.77  ? 520  ASN   A C    1 
ATOM   871  O  O    . ASN   A 1 142 ? -11.252 -2.111  30.921  1.00 33.51  ? 520  ASN   A O    1 
ATOM   872  C  CB   . ASN   A 1 142 ? -12.868 -3.689  33.523  1.00 33.80  ? 520  ASN   A CB   1 
ATOM   873  C  CG   . ASN   A 1 142 ? -11.709 -3.069  34.306  1.00 34.82  ? 520  ASN   A CG   1 
ATOM   874  O  OD1  . ASN   A 1 142 ? -10.773 -2.484  33.738  1.00 33.86  ? 520  ASN   A OD1  1 
ATOM   875  N  ND2  . ASN   A 1 142 ? -11.768 -3.204  35.622  1.00 33.18  ? 520  ASN   A ND2  1 
ATOM   876  N  N    . ASN   A 1 143 ? -13.389 -1.583  31.460  1.00 37.15  ? 521  ASN   A N    1 
ATOM   877  C  CA   . ASN   A 1 143 ? -13.297 -0.280  30.810  1.00 36.68  ? 521  ASN   A CA   1 
ATOM   878  C  C    . ASN   A 1 143 ? -12.254 0.598   31.488  1.00 35.40  ? 521  ASN   A C    1 
ATOM   879  O  O    . ASN   A 1 143 ? -11.485 1.307   30.817  1.00 36.19  ? 521  ASN   A O    1 
ATOM   880  C  CB   . ASN   A 1 143 ? -14.664 0.405   30.823  1.00 35.28  ? 521  ASN   A CB   1 
ATOM   881  C  CG   . ASN   A 1 143 ? -14.590 1.849   30.344  1.00 39.23  ? 521  ASN   A CG   1 
ATOM   882  O  OD1  . ASN   A 1 143 ? -14.263 2.741   31.106  1.00 40.09  ? 521  ASN   A OD1  1 
ATOM   883  N  ND2  . ASN   A 1 143 ? -14.848 2.065   29.050  1.00 38.33  ? 521  ASN   A ND2  1 
ATOM   884  N  N    . GLU   A 1 144 ? -12.230 0.568   32.821  1.00 35.68  ? 522  GLU   A N    1 
ATOM   885  C  CA   . GLU   A 1 144 ? -11.304 1.388   33.592  1.00 34.55  ? 522  GLU   A CA   1 
ATOM   886  C  C    . GLU   A 1 144 ? -9.867  1.175   33.132  1.00 37.24  ? 522  GLU   A C    1 
ATOM   887  O  O    . GLU   A 1 144 ? -9.149  2.135   32.827  1.00 35.34  ? 522  GLU   A O    1 
ATOM   888  C  CB   . GLU   A 1 144 ? -11.460 1.057   35.082  1.00 38.88  ? 522  GLU   A CB   1 
ATOM   889  C  CG   . GLU   A 1 144 ? -12.816 1.473   35.690  1.00 41.98  ? 522  GLU   A CG   1 
ATOM   890  C  CD   . GLU   A 1 144 ? -13.971 0.484   35.441  1.00 44.14  ? 522  GLU   A CD   1 
ATOM   891  O  OE1  . GLU   A 1 144 ? -13.868 -0.433  34.579  1.00 35.66  ? 522  GLU   A OE1  1 
ATOM   892  O  OE2  . GLU   A 1 144 ? -15.003 0.641   36.135  1.00 47.03  ? 522  GLU   A OE2  1 
ATOM   893  N  N    . ARG   A 1 145 ? -9.433  -0.085  33.063  1.00 33.56  ? 523  ARG   A N    1 
ATOM   894  C  CA   . ARG   A 1 145 ? -8.053  -0.370  32.681  1.00 35.28  ? 523  ARG   A CA   1 
ATOM   895  C  C    . ARG   A 1 145 ? -7.805  -0.102  31.200  1.00 35.36  ? 523  ARG   A C    1 
ATOM   896  O  O    . ARG   A 1 145 ? -6.724  0.378   30.819  1.00 35.49  ? 523  ARG   A O    1 
ATOM   897  C  CB   . ARG   A 1 145 ? -7.710  -1.819  33.036  1.00 30.47  ? 523  ARG   A CB   1 
ATOM   898  C  CG   . ARG   A 1 145 ? -7.669  -2.050  34.541  1.00 32.47  ? 523  ARG   A CG   1 
ATOM   899  C  CD   . ARG   A 1 145 ? -7.821  -3.514  34.887  1.00 38.51  ? 523  ARG   A CD   1 
ATOM   900  N  NE   . ARG   A 1 145 ? -7.603  -3.770  36.310  1.00 35.16  ? 523  ARG   A NE   1 
ATOM   901  C  CZ   . ARG   A 1 145 ? -7.694  -4.967  36.872  1.00 34.55  ? 523  ARG   A CZ   1 
ATOM   902  N  NH1  . ARG   A 1 145 ? -7.987  -6.046  36.155  1.00 29.60  ? 523  ARG   A NH1  1 
ATOM   903  N  NH2  . ARG   A 1 145 ? -7.478  -5.087  38.186  1.00 33.36  ? 523  ARG   A NH2  1 
ATOM   904  N  N    . ALA   A 1 146 ? -8.784  -0.424  30.352  1.00 37.19  ? 524  ALA   A N    1 
ATOM   905  C  CA   . ALA   A 1 146 ? -8.626  -0.281  28.909  1.00 35.43  ? 524  ALA   A CA   1 
ATOM   906  C  C    . ALA   A 1 146 ? -8.468  1.169   28.488  1.00 37.34  ? 524  ALA   A C    1 
ATOM   907  O  O    . ALA   A 1 146 ? -7.891  1.429   27.424  1.00 38.07  ? 524  ALA   A O    1 
ATOM   908  C  CB   . ALA   A 1 146 ? -9.819  -0.897  28.180  1.00 36.65  ? 524  ALA   A CB   1 
ATOM   909  N  N    . GLN   A 1 147 ? -8.960  2.112   29.301  1.00 35.41  ? 525  GLN   A N    1 
ATOM   910  C  CA   . GLN   A 1 147 ? -8.701  3.525   29.050  1.00 38.91  ? 525  GLN   A CA   1 
ATOM   911  C  C    . GLN   A 1 147 ? -7.210  3.833   29.054  1.00 44.10  ? 525  GLN   A C    1 
ATOM   912  O  O    . GLN   A 1 147 ? -6.763  4.750   28.355  1.00 42.39  ? 525  GLN   A O    1 
ATOM   913  C  CB   . GLN   A 1 147 ? -9.396  4.385   30.103  1.00 42.15  ? 525  GLN   A CB   1 
ATOM   914  C  CG   . GLN   A 1 147 ? -10.833 4.718   29.733  1.00 52.16  ? 525  GLN   A CG   1 
ATOM   915  C  CD   . GLN   A 1 147 ? -11.548 5.508   30.801  1.00 60.37  ? 525  GLN   A CD   1 
ATOM   916  O  OE1  . GLN   A 1 147 ? -12.651 5.151   31.225  1.00 61.72  ? 525  GLN   A OE1  1 
ATOM   917  N  NE2  . GLN   A 1 147 ? -10.937 6.613   31.221  1.00 55.13  ? 525  GLN   A NE2  1 
ATOM   918  N  N    . TYR   A 1 148 ? -6.427  3.085   29.828  1.00 37.03  ? 526  TYR   A N    1 
ATOM   919  C  CA   . TYR   A 1 148 ? -5.036  3.434   30.079  1.00 37.29  ? 526  TYR   A CA   1 
ATOM   920  C  C    . TYR   A 1 148 ? -4.033  2.477   29.472  1.00 42.15  ? 526  TYR   A C    1 
ATOM   921  O  O    . TYR   A 1 148 ? -2.900  2.894   29.231  1.00 37.13  ? 526  TYR   A O    1 
ATOM   922  C  CB   . TYR   A 1 148 ? -4.769  3.528   31.582  1.00 38.69  ? 526  TYR   A CB   1 
ATOM   923  C  CG   . TYR   A 1 148 ? -5.349  4.788   32.173  1.00 40.04  ? 526  TYR   A CG   1 
ATOM   924  C  CD1  . TYR   A 1 148 ? -6.687  4.841   32.557  1.00 41.55  ? 526  TYR   A CD1  1 
ATOM   925  C  CD2  . TYR   A 1 148 ? -4.561  5.926   32.346  1.00 40.68  ? 526  TYR   A CD2  1 
ATOM   926  C  CE1  . TYR   A 1 148 ? -7.237  5.998   33.090  1.00 41.80  ? 526  TYR   A CE1  1 
ATOM   927  C  CE2  . TYR   A 1 148 ? -5.087  7.076   32.893  1.00 46.16  ? 526  TYR   A CE2  1 
ATOM   928  C  CZ   . TYR   A 1 148 ? -6.434  7.107   33.260  1.00 44.80  ? 526  TYR   A CZ   1 
ATOM   929  O  OH   . TYR   A 1 148 ? -6.964  8.252   33.792  1.00 46.18  ? 526  TYR   A OH   1 
ATOM   930  N  N    . ILE   A 1 149 ? -4.411  1.214   29.220  1.00 37.02  ? 527  ILE   A N    1 
ATOM   931  C  CA   . ILE   A 1 149 ? -3.488  0.224   28.683  1.00 41.63  ? 527  ILE   A CA   1 
ATOM   932  C  C    . ILE   A 1 149 ? -4.170  -0.523  27.548  1.00 41.20  ? 527  ILE   A C    1 
ATOM   933  O  O    . ILE   A 1 149 ? -5.371  -0.402  27.319  1.00 37.61  ? 527  ILE   A O    1 
ATOM   934  C  CB   . ILE   A 1 149 ? -2.982  -0.784  29.742  1.00 38.59  ? 527  ILE   A CB   1 
ATOM   935  C  CG1  . ILE   A 1 149 ? -4.116  -1.681  30.244  1.00 32.95  ? 527  ILE   A CG1  1 
ATOM   936  C  CG2  . ILE   A 1 149 ? -2.326  -0.087  30.897  1.00 37.12  ? 527  ILE   A CG2  1 
ATOM   937  C  CD1  . ILE   A 1 149 ? -3.584  -2.958  30.895  1.00 33.29  ? 527  ILE   A CD1  1 
ATOM   938  N  N    . GLU   A 1 150 ? -3.371  -1.312  26.845  1.00 39.90  ? 528  GLU   A N    1 
ATOM   939  C  CA   . GLU   A 1 150 ? -3.849  -2.150  25.761  1.00 38.01  ? 528  GLU   A CA   1 
ATOM   940  C  C    . GLU   A 1 150 ? -3.971  -3.580  26.272  1.00 41.29  ? 528  GLU   A C    1 
ATOM   941  O  O    . GLU   A 1 150 ? -3.023  -4.115  26.858  1.00 38.14  ? 528  GLU   A O    1 
ATOM   942  C  CB   . GLU   A 1 150 ? -2.893  -2.093  24.571  1.00 46.96  ? 528  GLU   A CB   1 
ATOM   943  C  CG   . GLU   A 1 150 ? -3.193  -3.139  23.515  1.00 51.64  ? 528  GLU   A CG   1 
ATOM   944  C  CD   . GLU   A 1 150 ? -4.132  -2.621  22.445  1.00 58.09  ? 528  GLU   A CD   1 
ATOM   945  O  OE1  . GLU   A 1 150 ? -4.480  -3.412  21.538  1.00 62.87  ? 528  GLU   A OE1  1 
ATOM   946  O  OE2  . GLU   A 1 150 ? -4.496  -1.417  22.497  1.00 63.22  ? 528  GLU   A OE2  1 
ATOM   947  N  N    . PHE   A 1 151 ? -5.139  -4.179  26.073  1.00 36.71  ? 529  PHE   A N    1 
ATOM   948  C  CA   . PHE   A 1 151 ? -5.353  -5.590  26.362  1.00 34.64  ? 529  PHE   A CA   1 
ATOM   949  C  C    . PHE   A 1 151 ? -5.274  -6.396  25.075  1.00 36.97  ? 529  PHE   A C    1 
ATOM   950  O  O    . PHE   A 1 151 ? -5.771  -5.963  24.029  1.00 35.42  ? 529  PHE   A O    1 
ATOM   951  C  CB   . PHE   A 1 151 ? -6.722  -5.825  26.997  1.00 34.47  ? 529  PHE   A CB   1 
ATOM   952  C  CG   . PHE   A 1 151 ? -6.807  -5.437  28.442  1.00 33.26  ? 529  PHE   A CG   1 
ATOM   953  C  CD1  . PHE   A 1 151 ? -6.310  -6.256  29.436  1.00 31.66  ? 529  PHE   A CD1  1 
ATOM   954  C  CD2  . PHE   A 1 151 ? -7.413  -4.245  28.803  1.00 34.96  ? 529  PHE   A CD2  1 
ATOM   955  C  CE1  . PHE   A 1 151 ? -6.421  -5.890  30.772  1.00 34.61  ? 529  PHE   A CE1  1 
ATOM   956  C  CE2  . PHE   A 1 151 ? -7.532  -3.869  30.130  1.00 34.45  ? 529  PHE   A CE2  1 
ATOM   957  C  CZ   . PHE   A 1 151 ? -7.032  -4.687  31.119  1.00 35.13  ? 529  PHE   A CZ   1 
ATOM   958  N  N    . SER   A 1 152 ? -4.654  -7.572  25.161  1.00 34.46  ? 530  SER   A N    1 
ATOM   959  C  CA   . SER   A 1 152 ? -4.820  -8.584  24.129  1.00 33.21  ? 530  SER   A CA   1 
ATOM   960  C  C    . SER   A 1 152 ? -6.280  -9.039  24.055  1.00 32.10  ? 530  SER   A C    1 
ATOM   961  O  O    . SER   A 1 152 ? -7.084  -8.802  24.961  1.00 32.13  ? 530  SER   A O    1 
ATOM   962  C  CB   . SER   A 1 152 ? -3.943  -9.797  24.431  1.00 31.44  ? 530  SER   A CB   1 
ATOM   963  O  OG   . SER   A 1 152 ? -4.551  -10.635 25.419  1.00 30.30  ? 530  SER   A OG   1 
ATOM   964  N  N    . LYS   A 1 153 ? -6.623  -9.721  22.956  1.00 33.71  ? 531  LYS   A N    1 
ATOM   965  C  CA   . LYS   A 1 153 ? -7.831  -10.536 22.956  1.00 28.38  ? 531  LYS   A CA   1 
ATOM   966  C  C    . LYS   A 1 153 ? -7.755  -11.505 24.130  1.00 30.52  ? 531  LYS   A C    1 
ATOM   967  O  O    . LYS   A 1 153 ? -6.660  -11.893 24.535  1.00 31.96  ? 531  LYS   A O    1 
ATOM   968  C  CB   . LYS   A 1 153 ? -7.971  -11.313 21.646  1.00 31.47  ? 531  LYS   A CB   1 
ATOM   969  C  CG   . LYS   A 1 153 ? -8.323  -10.447 20.442  1.00 32.15  ? 531  LYS   A CG   1 
ATOM   970  C  CD   . LYS   A 1 153 ? -9.787  -10.046 20.486  1.00 34.53  ? 531  LYS   A CD   1 
ATOM   971  C  CE   . LYS   A 1 153 ? -10.138 -9.144  19.288  1.00 35.57  ? 531  LYS   A CE   1 
ATOM   972  N  NZ   . LYS   A 1 153 ? -9.532  -7.788  19.411  1.00 31.94  ? 531  LYS   A NZ   1 
ATOM   973  N  N    . PRO   A 1 154 ? -8.894  -11.913 24.693  1.00 30.47  ? 532  PRO   A N    1 
ATOM   974  C  CA   . PRO   A 1 154 ? -8.854  -12.675 25.946  1.00 31.16  ? 532  PRO   A CA   1 
ATOM   975  C  C    . PRO   A 1 154 ? -8.163  -14.019 25.767  1.00 34.57  ? 532  PRO   A C    1 
ATOM   976  O  O    . PRO   A 1 154 ? -8.437  -14.755 24.816  1.00 32.62  ? 532  PRO   A O    1 
ATOM   977  C  CB   . PRO   A 1 154 ? -10.336 -12.845 26.311  1.00 28.92  ? 532  PRO   A CB   1 
ATOM   978  C  CG   . PRO   A 1 154 ? -11.060 -11.747 25.544  1.00 32.05  ? 532  PRO   A CG   1 
ATOM   979  C  CD   . PRO   A 1 154 ? -10.276 -11.588 24.279  1.00 29.80  ? 532  PRO   A CD   1 
ATOM   980  N  N    . PHE   A 1 155 ? -7.233  -14.322 26.675  1.00 31.27  ? 533  PHE   A N    1 
ATOM   981  C  CA   . PHE   A 1 155 ? -6.652  -15.656 26.675  1.00 30.80  ? 533  PHE   A CA   1 
ATOM   982  C  C    . PHE   A 1 155 ? -7.451  -16.632 27.513  1.00 31.27  ? 533  PHE   A C    1 
ATOM   983  O  O    . PHE   A 1 155 ? -7.212  -17.836 27.409  1.00 31.84  ? 533  PHE   A O    1 
ATOM   984  C  CB   . PHE   A 1 155 ? -5.166  -15.653 27.118  1.00 32.27  ? 533  PHE   A CB   1 
ATOM   985  C  CG   . PHE   A 1 155 ? -4.915  -15.303 28.579  1.00 33.55  ? 533  PHE   A CG   1 
ATOM   986  C  CD1  . PHE   A 1 155 ? -5.104  -16.236 29.594  1.00 31.63  ? 533  PHE   A CD1  1 
ATOM   987  C  CD2  . PHE   A 1 155 ? -4.380  -14.073 28.918  1.00 32.29  ? 533  PHE   A CD2  1 
ATOM   988  C  CE1  . PHE   A 1 155 ? -4.829  -15.935 30.927  1.00 31.31  ? 533  PHE   A CE1  1 
ATOM   989  C  CE2  . PHE   A 1 155 ? -4.112  -13.745 30.269  1.00 33.50  ? 533  PHE   A CE2  1 
ATOM   990  C  CZ   . PHE   A 1 155 ? -4.340  -14.683 31.267  1.00 32.68  ? 533  PHE   A CZ   1 
ATOM   991  N  N    . LYS   A 1 156 ? -8.429  -16.151 28.289  1.00 30.31  ? 534  LYS   A N    1 
ATOM   992  C  CA   . LYS   A 1 156 ? -9.278  -17.037 29.072  1.00 31.15  ? 534  LYS   A CA   1 
ATOM   993  C  C    . LYS   A 1 156 ? -10.628 -16.367 29.268  1.00 33.85  ? 534  LYS   A C    1 
ATOM   994  O  O    . LYS   A 1 156 ? -10.677 -15.199 29.671  1.00 31.87  ? 534  LYS   A O    1 
ATOM   995  C  CB   . LYS   A 1 156 ? -8.631  -17.350 30.423  1.00 31.45  ? 534  LYS   A CB   1 
ATOM   996  C  CG   . LYS   A 1 156 ? -9.508  -18.156 31.369  1.00 32.43  ? 534  LYS   A CG   1 
ATOM   997  C  CD   . LYS   A 1 156 ? -9.754  -19.582 30.860  1.00 37.08  ? 534  LYS   A CD   1 
ATOM   998  C  CE   . LYS   A 1 156 ? -10.656 -20.338 31.850  1.00 42.24  ? 534  LYS   A CE   1 
ATOM   999  N  NZ   . LYS   A 1 156 ? -11.077 -21.698 31.440  1.00 38.63  ? 534  LYS   A NZ   1 
ATOM   1000 N  N    . TYR   A 1 157 ? -11.705 -17.089 28.946  1.00 30.60  ? 535  TYR   A N    1 
ATOM   1001 C  CA   . TYR   A 1 157 ? -13.082 -16.637 29.162  1.00 33.98  ? 535  TYR   A CA   1 
ATOM   1002 C  C    . TYR   A 1 157 ? -13.618 -17.353 30.394  1.00 33.45  ? 535  TYR   A C    1 
ATOM   1003 O  O    . TYR   A 1 157 ? -13.486 -18.575 30.504  1.00 30.74  ? 535  TYR   A O    1 
ATOM   1004 C  CB   . TYR   A 1 157 ? -13.990 -16.939 27.962  1.00 33.12  ? 535  TYR   A CB   1 
ATOM   1005 C  CG   . TYR   A 1 157 ? -13.628 -16.186 26.701  1.00 33.21  ? 535  TYR   A CG   1 
ATOM   1006 C  CD1  . TYR   A 1 157 ? -12.628 -16.653 25.868  1.00 31.29  ? 535  TYR   A CD1  1 
ATOM   1007 C  CD2  . TYR   A 1 157 ? -14.288 -15.012 26.344  1.00 34.38  ? 535  TYR   A CD2  1 
ATOM   1008 C  CE1  . TYR   A 1 157 ? -12.291 -15.979 24.706  1.00 36.31  ? 535  TYR   A CE1  1 
ATOM   1009 C  CE2  . TYR   A 1 157 ? -13.963 -14.332 25.189  1.00 30.26  ? 535  TYR   A CE2  1 
ATOM   1010 C  CZ   . TYR   A 1 157 ? -12.948 -14.806 24.385  1.00 32.46  ? 535  TYR   A CZ   1 
ATOM   1011 O  OH   . TYR   A 1 157 ? -12.625 -14.125 23.231  1.00 30.07  ? 535  TYR   A OH   1 
ATOM   1012 N  N    . GLN   A 1 158 ? -14.198 -16.586 31.321  1.00 29.25  ? 536  GLN   A N    1 
ATOM   1013 C  CA   . GLN   A 1 158 ? -14.690 -17.091 32.600  1.00 32.11  ? 536  GLN   A CA   1 
ATOM   1014 C  C    . GLN   A 1 158 ? -15.696 -16.101 33.194  1.00 33.72  ? 536  GLN   A C    1 
ATOM   1015 O  O    . GLN   A 1 158 ? -16.490 -15.514 32.450  1.00 32.99  ? 536  GLN   A O    1 
ATOM   1016 C  CB   . GLN   A 1 158 ? -13.499 -17.387 33.536  1.00 31.14  ? 536  GLN   A CB   1 
ATOM   1017 C  CG   . GLN   A 1 158 ? -12.592 -16.181 33.848  1.00 30.76  ? 536  GLN   A CG   1 
ATOM   1018 C  CD   . GLN   A 1 158 ? -12.614 -15.735 35.301  1.00 31.82  ? 536  GLN   A CD   1 
ATOM   1019 O  OE1  . GLN   A 1 158 ? -12.338 -16.521 36.219  1.00 36.38  ? 536  GLN   A OE1  1 
ATOM   1020 N  NE2  . GLN   A 1 158 ? -12.833 -14.440 35.511  1.00 30.74  ? 536  GLN   A NE2  1 
ATOM   1021 N  N    . GLY   A 1 159 ? -15.711 -15.909 34.506  1.00 31.22  ? 537  GLY   A N    1 
ATOM   1022 C  CA   . GLY   A 1 159 ? -16.695 -15.000 35.075  1.00 32.87  ? 537  GLY   A CA   1 
ATOM   1023 C  C    . GLY   A 1 159 ? -16.563 -14.927 36.581  1.00 35.72  ? 537  GLY   A C    1 
ATOM   1024 O  O    . GLY   A 1 159 ? -15.570 -15.370 37.151  1.00 36.26  ? 537  GLY   A O    1 
ATOM   1025 N  N    . LEU   A 1 160 ? -17.572 -14.352 37.232  1.00 31.18  ? 538  LEU   A N    1 
ATOM   1026 C  CA   . LEU   A 1 160 ? -17.552 -14.237 38.680  1.00 35.94  ? 538  LEU   A CA   1 
ATOM   1027 C  C    . LEU   A 1 160 ? -18.537 -15.230 39.279  1.00 34.59  ? 538  LEU   A C    1 
ATOM   1028 O  O    . LEU   A 1 160 ? -19.639 -15.424 38.755  1.00 33.89  ? 538  LEU   A O    1 
ATOM   1029 C  CB   . LEU   A 1 160 ? -17.908 -12.821 39.139  1.00 32.03  ? 538  LEU   A CB   1 
ATOM   1030 C  CG   . LEU   A 1 160 ? -17.037 -11.681 38.590  1.00 37.95  ? 538  LEU   A CG   1 
ATOM   1031 C  CD1  . LEU   A 1 160 ? -17.489 -10.406 39.247  1.00 32.79  ? 538  LEU   A CD1  1 
ATOM   1032 C  CD2  . LEU   A 1 160 ? -15.535 -11.910 38.809  1.00 31.41  ? 538  LEU   A CD2  1 
ATOM   1033 N  N    . THR   A 1 161 ? -18.134 -15.849 40.383  1.00 36.74  ? 539  THR   A N    1 
ATOM   1034 C  CA   . THR   A 1 161 ? -18.984 -16.776 41.112  1.00 34.94  ? 539  THR   A CA   1 
ATOM   1035 C  C    . THR   A 1 161 ? -18.705 -16.575 42.596  1.00 38.65  ? 539  THR   A C    1 
ATOM   1036 O  O    . THR   A 1 161 ? -17.954 -15.670 42.985  1.00 33.96  ? 539  THR   A O    1 
ATOM   1037 C  CB   . THR   A 1 161 ? -18.744 -18.215 40.632  1.00 38.23  ? 539  THR   A CB   1 
ATOM   1038 O  OG1  . THR   A 1 161 ? -19.737 -19.089 41.181  1.00 45.00  ? 539  THR   A OG1  1 
ATOM   1039 C  CG2  . THR   A 1 161 ? -17.363 -18.701 41.046  1.00 35.00  ? 539  THR   A CG2  1 
ATOM   1040 N  N    . ILE   A 1 162 ? -19.323 -17.400 43.439  1.00 36.14  ? 540  ILE   A N    1 
ATOM   1041 C  CA   . ILE   A 1 162 ? -19.223 -17.250 44.889  1.00 40.53  ? 540  ILE   A CA   1 
ATOM   1042 C  C    . ILE   A 1 162 ? -18.741 -18.559 45.486  1.00 41.85  ? 540  ILE   A C    1 
ATOM   1043 O  O    . ILE   A 1 162 ? -19.252 -19.630 45.134  1.00 40.88  ? 540  ILE   A O    1 
ATOM   1044 C  CB   . ILE   A 1 162 ? -20.559 -16.822 45.530  1.00 39.27  ? 540  ILE   A CB   1 
ATOM   1045 C  CG1  . ILE   A 1 162 ? -21.030 -15.473 44.984  1.00 45.06  ? 540  ILE   A CG1  1 
ATOM   1046 C  CG2  . ILE   A 1 162 ? -20.459 -16.759 47.033  1.00 43.83  ? 540  ILE   A CG2  1 
ATOM   1047 C  CD1  . ILE   A 1 162 ? -22.473 -15.460 44.510  1.00 47.25  ? 540  ILE   A CD1  1 
ATOM   1048 N  N    . LEU   A 1 163 ? -17.765 -18.471 46.387  1.00 38.21  ? 541  LEU   A N    1 
ATOM   1049 C  CA   . LEU   A 1 163 ? -17.205 -19.633 47.064  1.00 40.65  ? 541  LEU   A CA   1 
ATOM   1050 C  C    . LEU   A 1 163 ? -17.657 -19.601 48.514  1.00 42.54  ? 541  LEU   A C    1 
ATOM   1051 O  O    . LEU   A 1 163 ? -17.558 -18.561 49.175  1.00 37.87  ? 541  LEU   A O    1 
ATOM   1052 C  CB   . LEU   A 1 163 ? -15.677 -19.636 46.981  1.00 42.51  ? 541  LEU   A CB   1 
ATOM   1053 C  CG   . LEU   A 1 163 ? -14.899 -20.760 47.675  1.00 42.89  ? 541  LEU   A CG   1 
ATOM   1054 C  CD1  . LEU   A 1 163 ? -14.626 -21.823 46.651  1.00 39.37  ? 541  LEU   A CD1  1 
ATOM   1055 C  CD2  . LEU   A 1 163 ? -13.586 -20.261 48.256  1.00 43.62  ? 541  LEU   A CD2  1 
ATOM   1056 N  N    . VAL   A 1 164 ? -18.176 -20.726 49.003  1.00 42.54  ? 542  VAL   A N    1 
ATOM   1057 C  CA   . VAL   A 1 164 ? -18.600 -20.856 50.390  1.00 40.29  ? 542  VAL   A CA   1 
ATOM   1058 C  C    . VAL   A 1 164 ? -18.063 -22.175 50.932  1.00 44.34  ? 542  VAL   A C    1 
ATOM   1059 O  O    . VAL   A 1 164 ? -17.558 -23.017 50.190  1.00 43.82  ? 542  VAL   A O    1 
ATOM   1060 C  CB   . VAL   A 1 164 ? -20.136 -20.792 50.543  1.00 44.95  ? 542  VAL   A CB   1 
ATOM   1061 C  CG1  . VAL   A 1 164 ? -20.681 -19.496 49.957  1.00 41.52  ? 542  VAL   A CG1  1 
ATOM   1062 C  CG2  . VAL   A 1 164 ? -20.781 -21.990 49.855  1.00 42.59  ? 542  VAL   A CG2  1 
ATOM   1063 N  N    . LYS   A 1 165 ? -18.160 -22.333 52.252  1.00 45.82  ? 543  LYS   A N    1 
ATOM   1064 C  CA   . LYS   A 1 165 ? -17.830 -23.595 52.903  1.00 49.59  ? 543  LYS   A CA   1 
ATOM   1065 C  C    . LYS   A 1 165 ? -18.962 -24.592 52.689  1.00 53.99  ? 543  LYS   A C    1 
ATOM   1066 O  O    . LYS   A 1 165 ? -20.141 -24.221 52.704  1.00 52.30  ? 543  LYS   A O    1 
ATOM   1067 C  CB   . LYS   A 1 165 ? -17.585 -23.380 54.397  1.00 47.61  ? 543  LYS   A CB   1 
ATOM   1068 C  CG   . LYS   A 1 165 ? -17.830 -24.613 55.251  1.00 53.41  ? 543  LYS   A CG   1 
ATOM   1069 C  CD   . LYS   A 1 165 ? -16.559 -25.416 55.493  1.00 56.74  ? 543  LYS   A CD   1 
ATOM   1070 C  CE   . LYS   A 1 165 ? -15.722 -24.853 56.636  1.00 59.87  ? 543  LYS   A CE   1 
ATOM   1071 N  NZ   . LYS   A 1 165 ? -14.267 -25.254 56.556  1.00 54.72  ? 543  LYS   A NZ   1 
ATOM   1072 N  N    . LYS   A 1 166 ? -18.598 -25.856 52.469  1.00 53.06  ? 544  LYS   A N    1 
ATOM   1073 C  CA   . LYS   A 1 166 ? -19.597 -26.893 52.246  1.00 56.33  ? 544  LYS   A CA   1 
ATOM   1074 C  C    . LYS   A 1 166 ? -20.578 -26.915 53.408  1.00 54.35  ? 544  LYS   A C    1 
ATOM   1075 O  O    . LYS   A 1 166 ? -20.175 -26.916 54.573  1.00 52.18  ? 544  LYS   A O    1 
ATOM   1076 C  CB   . LYS   A 1 166 ? -18.924 -28.256 52.085  1.00 55.22  ? 544  LYS   A CB   1 
ATOM   1077 C  CG   . LYS   A 1 166 ? -19.753 -29.290 51.340  1.00 57.22  ? 544  LYS   A CG   1 
ATOM   1078 C  CD   . LYS   A 1 166 ? -18.977 -30.599 51.168  1.00 61.93  ? 544  LYS   A CD   1 
ATOM   1079 C  CE   . LYS   A 1 166 ? -19.793 -31.643 50.413  1.00 69.40  ? 544  LYS   A CE   1 
ATOM   1080 N  NZ   . LYS   A 1 166 ? -19.109 -32.967 50.344  1.00 74.37  ? 544  LYS   A NZ   1 
ATOM   1081 N  N    . GLY   A 1 167 ? -21.874 -26.884 53.084  1.00 61.15  ? 545  GLY   A N    1 
ATOM   1082 C  CA   . GLY   A 1 167 ? -22.938 -26.790 54.062  1.00 69.46  ? 545  GLY   A CA   1 
ATOM   1083 C  C    . GLY   A 1 167 ? -23.631 -25.440 54.080  1.00 71.14  ? 545  GLY   A C    1 
ATOM   1084 O  O    . GLY   A 1 167 ? -24.797 -25.358 54.481  1.00 76.93  ? 545  GLY   A O    1 
ATOM   1085 N  N    . THR   A 1 168 ? -22.936 -24.386 53.667  1.00 63.44  ? 546  THR   A N    1 
ATOM   1086 C  CA   . THR   A 1 168 ? -23.539 -23.062 53.596  1.00 60.57  ? 546  THR   A CA   1 
ATOM   1087 C  C    . THR   A 1 168 ? -24.520 -23.009 52.431  1.00 59.75  ? 546  THR   A C    1 
ATOM   1088 O  O    . THR   A 1 168 ? -24.191 -23.414 51.312  1.00 63.35  ? 546  THR   A O    1 
ATOM   1089 C  CB   . THR   A 1 168 ? -22.439 -22.004 53.450  1.00 54.74  ? 546  THR   A CB   1 
ATOM   1090 O  OG1  . THR   A 1 168 ? -21.652 -21.981 54.645  1.00 52.40  ? 546  THR   A OG1  1 
ATOM   1091 C  CG2  . THR   A 1 168 ? -23.003 -20.611 53.187  1.00 54.30  ? 546  THR   A CG2  1 
ATOM   1092 N  N    . ARG   A 1 169 ? -25.733 -22.534 52.692  1.00 54.67  ? 663  ARG   A N    1 
ATOM   1093 C  CA   . ARG   A 1 169 ? -26.802 -22.541 51.698  1.00 57.80  ? 663  ARG   A CA   1 
ATOM   1094 C  C    . ARG   A 1 169 ? -27.114 -21.104 51.289  1.00 58.17  ? 663  ARG   A C    1 
ATOM   1095 O  O    . ARG   A 1 169 ? -27.810 -20.380 52.009  1.00 57.15  ? 663  ARG   A O    1 
ATOM   1096 C  CB   . ARG   A 1 169 ? -28.046 -23.243 52.239  1.00 56.24  ? 663  ARG   A CB   1 
ATOM   1097 N  N    . ILE   A 1 170 ? -26.593 -20.694 50.134  1.00 54.22  ? 664  ILE   A N    1 
ATOM   1098 C  CA   . ILE   A 1 170 ? -27.016 -19.465 49.472  1.00 53.39  ? 664  ILE   A CA   1 
ATOM   1099 C  C    . ILE   A 1 170 ? -27.290 -19.781 48.008  1.00 54.70  ? 664  ILE   A C    1 
ATOM   1100 O  O    . ILE   A 1 170 ? -26.595 -20.606 47.402  1.00 53.89  ? 664  ILE   A O    1 
ATOM   1101 C  CB   . ILE   A 1 170 ? -25.977 -18.330 49.597  1.00 54.75  ? 664  ILE   A CB   1 
ATOM   1102 C  CG1  . ILE   A 1 170 ? -24.715 -18.654 48.816  1.00 55.94  ? 664  ILE   A CG1  1 
ATOM   1103 C  CG2  . ILE   A 1 170 ? -25.630 -18.067 51.054  1.00 56.83  ? 664  ILE   A CG2  1 
ATOM   1104 C  CD1  . ILE   A 1 170 ? -23.746 -17.523 48.793  1.00 56.27  ? 664  ILE   A CD1  1 
ATOM   1105 N  N    . THR   A 1 171 ? -28.302 -19.115 47.433  1.00 49.84  ? 665  THR   A N    1 
ATOM   1106 C  CA   . THR   A 1 171 ? -28.683 -19.396 46.053  1.00 52.64  ? 665  THR   A CA   1 
ATOM   1107 C  C    . THR   A 1 171 ? -27.703 -18.780 45.060  1.00 54.95  ? 665  THR   A C    1 
ATOM   1108 O  O    . THR   A 1 171 ? -27.483 -19.333 43.977  1.00 50.03  ? 665  THR   A O    1 
ATOM   1109 C  CB   . THR   A 1 171 ? -30.080 -18.854 45.765  1.00 52.13  ? 665  THR   A CB   1 
ATOM   1110 O  OG1  . THR   A 1 171 ? -30.030 -17.423 45.767  1.00 45.97  ? 665  THR   A OG1  1 
ATOM   1111 C  CG2  . THR   A 1 171 ? -31.055 -19.306 46.844  1.00 50.68  ? 665  THR   A CG2  1 
ATOM   1112 N  N    . GLY   A 1 172 ? -27.131 -17.629 45.392  1.00 51.22  ? 666  GLY   A N    1 
ATOM   1113 C  CA   . GLY   A 1 172 ? -26.267 -16.923 44.451  1.00 51.06  ? 666  GLY   A CA   1 
ATOM   1114 C  C    . GLY   A 1 172 ? -26.247 -15.432 44.750  1.00 41.62  ? 666  GLY   A C    1 
ATOM   1115 O  O    . GLY   A 1 172 ? -26.483 -15.014 45.881  1.00 43.09  ? 666  GLY   A O    1 
ATOM   1116 N  N    . ILE   A 1 173 ? -25.975 -14.648 43.703  1.00 41.99  ? 667  ILE   A N    1 
ATOM   1117 C  CA   . ILE   A 1 173 ? -25.857 -13.201 43.866  1.00 43.47  ? 667  ILE   A CA   1 
ATOM   1118 C  C    . ILE   A 1 173 ? -27.146 -12.558 44.357  1.00 45.62  ? 667  ILE   A C    1 
ATOM   1119 O  O    . ILE   A 1 173 ? -27.106 -11.469 44.939  1.00 45.80  ? 667  ILE   A O    1 
ATOM   1120 C  CB   . ILE   A 1 173 ? -25.364 -12.539 42.553  1.00 40.79  ? 667  ILE   A CB   1 
ATOM   1121 C  CG1  . ILE   A 1 173 ? -24.796 -11.146 42.855  1.00 42.69  ? 667  ILE   A CG1  1 
ATOM   1122 C  CG2  . ILE   A 1 173 ? -26.477 -12.482 41.487  1.00 42.62  ? 667  ILE   A CG2  1 
ATOM   1123 C  CD1  . ILE   A 1 173 ? -23.308 -11.139 43.198  1.00 41.98  ? 667  ILE   A CD1  1 
ATOM   1124 N  N    . ASN   A 1 174 ? -28.288 -13.213 44.182  1.00 45.07  ? 668  ASN   A N    1 
ATOM   1125 C  CA   . ASN   A 1 174 ? -29.564 -12.636 44.588  1.00 45.15  ? 668  ASN   A CA   1 
ATOM   1126 C  C    . ASN   A 1 174 ? -30.067 -13.173 45.919  1.00 49.34  ? 668  ASN   A C    1 
ATOM   1127 O  O    . ASN   A 1 174 ? -31.212 -12.902 46.294  1.00 49.60  ? 668  ASN   A O    1 
ATOM   1128 C  CB   . ASN   A 1 174 ? -30.587 -12.858 43.483  1.00 43.66  ? 668  ASN   A CB   1 
ATOM   1129 C  CG   . ASN   A 1 174 ? -30.148 -12.225 42.193  1.00 48.66  ? 668  ASN   A CG   1 
ATOM   1130 O  OD1  . ASN   A 1 174 ? -29.623 -11.109 42.201  1.00 49.35  ? 668  ASN   A OD1  1 
ATOM   1131 N  ND2  . ASN   A 1 174 ? -30.295 -12.944 41.086  1.00 49.27  ? 668  ASN   A ND2  1 
ATOM   1132 N  N    . ASP   A 1 175 ? -29.230 -13.896 46.650  1.00 47.15  ? 669  ASP   A N    1 
ATOM   1133 C  CA   . ASP   A 1 175 ? -29.630 -14.420 47.942  1.00 46.09  ? 669  ASP   A CA   1 
ATOM   1134 C  C    . ASP   A 1 175 ? -29.864 -13.274 48.928  1.00 51.25  ? 669  ASP   A C    1 
ATOM   1135 O  O    . ASP   A 1 175 ? -29.098 -12.304 48.946  1.00 47.08  ? 669  ASP   A O    1 
ATOM   1136 C  CB   . ASP   A 1 175 ? -28.546 -15.361 48.465  1.00 49.91  ? 669  ASP   A CB   1 
ATOM   1137 C  CG   . ASP   A 1 175 ? -29.008 -16.191 49.635  1.00 51.47  ? 669  ASP   A CG   1 
ATOM   1138 O  OD1  . ASP   A 1 175 ? -29.014 -15.685 50.780  1.00 49.47  ? 669  ASP   A OD1  1 
ATOM   1139 O  OD2  . ASP   A 1 175 ? -29.378 -17.358 49.382  1.00 50.67  ? 669  ASP   A OD2  1 
ATOM   1140 N  N    . PRO   A 1 176 ? -30.922 -13.346 49.749  1.00 52.31  ? 670  PRO   A N    1 
ATOM   1141 C  CA   . PRO   A 1 176 ? -31.156 -12.280 50.746  1.00 48.96  ? 670  PRO   A CA   1 
ATOM   1142 C  C    . PRO   A 1 176 ? -29.998 -11.998 51.694  1.00 51.82  ? 670  PRO   A C    1 
ATOM   1143 O  O    . PRO   A 1 176 ? -29.860 -10.852 52.146  1.00 48.83  ? 670  PRO   A O    1 
ATOM   1144 C  CB   . PRO   A 1 176 ? -32.392 -12.786 51.507  1.00 52.94  ? 670  PRO   A CB   1 
ATOM   1145 C  CG   . PRO   A 1 176 ? -33.106 -13.624 50.509  1.00 50.61  ? 670  PRO   A CG   1 
ATOM   1146 C  CD   . PRO   A 1 176 ? -32.044 -14.300 49.687  1.00 40.61  ? 670  PRO   A CD   1 
ATOM   1147 N  N    . ARG   A 1 177 ? -29.161 -12.985 52.021  1.00 48.18  ? 671  ARG   A N    1 
ATOM   1148 C  CA   . ARG   A 1 177 ? -28.044 -12.701 52.912  1.00 49.03  ? 671  ARG   A CA   1 
ATOM   1149 C  C    . ARG   A 1 177 ? -26.957 -11.883 52.222  1.00 50.63  ? 671  ARG   A C    1 
ATOM   1150 O  O    . ARG   A 1 177 ? -26.045 -11.391 52.892  1.00 49.41  ? 671  ARG   A O    1 
ATOM   1151 C  CB   . ARG   A 1 177 ? -27.485 -14.017 53.452  1.00 50.32  ? 671  ARG   A CB   1 
ATOM   1152 C  CG   . ARG   A 1 177 ? -28.489 -14.762 54.334  1.00 54.88  ? 671  ARG   A CG   1 
ATOM   1153 C  CD   . ARG   A 1 177 ? -28.186 -16.242 54.295  1.00 57.22  ? 671  ARG   A CD   1 
ATOM   1154 N  NE   . ARG   A 1 177 ? -27.321 -16.674 55.378  1.00 59.05  ? 671  ARG   A NE   1 
ATOM   1155 C  CZ   . ARG   A 1 177 ? -26.874 -17.914 55.508  1.00 59.13  ? 671  ARG   A CZ   1 
ATOM   1156 N  NH1  . ARG   A 1 177 ? -27.124 -18.832 54.589  1.00 54.41  ? 671  ARG   A NH1  1 
ATOM   1157 N  NH2  . ARG   A 1 177 ? -26.143 -18.232 56.573  1.00 60.52  ? 671  ARG   A NH2  1 
ATOM   1158 N  N    . LEU   A 1 178 ? -27.042 -11.712 50.906  1.00 48.71  ? 672  LEU   A N    1 
ATOM   1159 C  CA   . LEU   A 1 178 ? -26.150 -10.823 50.177  1.00 48.19  ? 672  LEU   A CA   1 
ATOM   1160 C  C    . LEU   A 1 178 ? -26.805 -9.488  49.846  1.00 50.19  ? 672  LEU   A C    1 
ATOM   1161 O  O    . LEU   A 1 178 ? -26.183 -8.439  50.022  1.00 48.34  ? 672  LEU   A O    1 
ATOM   1162 C  CB   . LEU   A 1 178 ? -25.673 -11.509 48.893  1.00 45.69  ? 672  LEU   A CB   1 
ATOM   1163 C  CG   . LEU   A 1 178 ? -24.424 -12.401 49.005  1.00 48.41  ? 672  LEU   A CG   1 
ATOM   1164 C  CD1  . LEU   A 1 178 ? -24.636 -13.528 49.985  1.00 47.37  ? 672  LEU   A CD1  1 
ATOM   1165 C  CD2  . LEU   A 1 178 ? -24.062 -12.968 47.626  1.00 46.56  ? 672  LEU   A CD2  1 
ATOM   1166 N  N    . ARG   A 1 179 ? -28.065 -9.504  49.406  1.00 50.75  ? 673  ARG   A N    1 
ATOM   1167 C  CA   . ARG   A 1 179 ? -28.739 -8.277  48.992  1.00 50.42  ? 673  ARG   A CA   1 
ATOM   1168 C  C    . ARG   A 1 179 ? -29.297 -7.480  50.167  1.00 50.41  ? 673  ARG   A C    1 
ATOM   1169 O  O    . ARG   A 1 179 ? -29.451 -6.259  50.057  1.00 54.87  ? 673  ARG   A O    1 
ATOM   1170 C  CB   . ARG   A 1 179 ? -29.842 -8.622  47.995  1.00 48.69  ? 673  ARG   A CB   1 
ATOM   1171 C  CG   . ARG   A 1 179 ? -29.302 -9.262  46.731  1.00 45.41  ? 673  ARG   A CG   1 
ATOM   1172 C  CD   . ARG   A 1 179 ? -28.731 -8.224  45.787  1.00 48.55  ? 673  ARG   A CD   1 
ATOM   1173 N  NE   . ARG   A 1 179 ? -28.448 -8.819  44.486  1.00 50.17  ? 673  ARG   A NE   1 
ATOM   1174 C  CZ   . ARG   A 1 179 ? -28.125 -8.138  43.395  1.00 49.77  ? 673  ARG   A CZ   1 
ATOM   1175 N  NH1  . ARG   A 1 179 ? -28.015 -6.821  43.408  1.00 52.62  ? 673  ARG   A NH1  1 
ATOM   1176 N  NH2  . ARG   A 1 179 ? -27.957 -8.790  42.249  1.00 51.70  ? 673  ARG   A NH2  1 
ATOM   1177 N  N    . ASN   A 1 180 ? -29.602 -8.124  51.294  1.00 50.04  ? 674  ASN   A N    1 
ATOM   1178 C  CA   . ASN   A 1 180 ? -30.005 -7.432  52.518  1.00 52.65  ? 674  ASN   A CA   1 
ATOM   1179 C  C    . ASN   A 1 180 ? -29.080 -7.881  53.644  1.00 52.78  ? 674  ASN   A C    1 
ATOM   1180 O  O    . ASN   A 1 180 ? -29.484 -8.637  54.535  1.00 54.56  ? 674  ASN   A O    1 
ATOM   1181 C  CB   . ASN   A 1 180 ? -31.477 -7.689  52.852  1.00 51.66  ? 674  ASN   A CB   1 
ATOM   1182 C  CG   . ASN   A 1 180 ? -31.986 -6.824  53.996  1.00 57.39  ? 674  ASN   A CG   1 
ATOM   1183 O  OD1  . ASN   A 1 180 ? -31.444 -5.757  54.276  1.00 59.63  ? 674  ASN   A OD1  1 
ATOM   1184 N  ND2  . ASN   A 1 180 ? -33.045 -7.282  54.655  1.00 50.68  ? 674  ASN   A ND2  1 
ATOM   1185 N  N    . PRO   A 1 181 ? -27.838 -7.410  53.646  1.00 51.97  ? 675  PRO   A N    1 
ATOM   1186 C  CA   . PRO   A 1 181 ? -26.806 -8.034  54.478  1.00 53.90  ? 675  PRO   A CA   1 
ATOM   1187 C  C    . PRO   A 1 181 ? -26.846 -7.578  55.925  1.00 57.49  ? 675  PRO   A C    1 
ATOM   1188 O  O    . PRO   A 1 181 ? -27.419 -6.546  56.277  1.00 55.82  ? 675  PRO   A O    1 
ATOM   1189 C  CB   . PRO   A 1 181 ? -25.503 -7.577  53.819  1.00 53.36  ? 675  PRO   A CB   1 
ATOM   1190 C  CG   . PRO   A 1 181 ? -25.840 -6.223  53.285  1.00 52.94  ? 675  PRO   A CG   1 
ATOM   1191 C  CD   . PRO   A 1 181 ? -27.295 -6.305  52.834  1.00 51.25  ? 675  PRO   A CD   1 
ATOM   1192 N  N    . SER   A 1 182 ? -26.182 -8.373  56.756  1.00 53.77  ? 676  SER   A N    1 
ATOM   1193 C  CA   . SER   A 1 182 ? -25.978 -8.062  58.157  1.00 63.26  ? 676  SER   A CA   1 
ATOM   1194 C  C    . SER   A 1 182 ? -24.611 -8.600  58.556  1.00 63.39  ? 676  SER   A C    1 
ATOM   1195 O  O    . SER   A 1 182 ? -23.897 -9.195  57.747  1.00 60.12  ? 676  SER   A O    1 
ATOM   1196 C  CB   . SER   A 1 182 ? -27.080 -8.663  59.024  1.00 59.26  ? 676  SER   A CB   1 
ATOM   1197 O  OG   . SER   A 1 182 ? -26.959 -8.206  60.354  1.00 68.82  ? 676  SER   A OG   1 
ATOM   1198 N  N    . ASP   A 1 183 ? -24.245 -8.387  59.815  1.00 64.77  ? 677  ASP   A N    1 
ATOM   1199 C  CA   . ASP   A 1 183 ? -22.993 -8.933  60.321  1.00 69.87  ? 677  ASP   A CA   1 
ATOM   1200 C  C    . ASP   A 1 183 ? -23.073 -10.427 60.615  1.00 65.33  ? 677  ASP   A C    1 
ATOM   1201 O  O    . ASP   A 1 183 ? -22.040 -11.041 60.902  1.00 62.71  ? 677  ASP   A O    1 
ATOM   1202 C  CB   . ASP   A 1 183 ? -22.558 -8.158  61.571  1.00 72.75  ? 677  ASP   A CB   1 
ATOM   1203 C  CG   . ASP   A 1 183 ? -23.728 -7.787  62.473  1.00 79.74  ? 677  ASP   A CG   1 
ATOM   1204 O  OD1  . ASP   A 1 183 ? -23.933 -6.575  62.695  1.00 87.74  ? 677  ASP   A OD1  1 
ATOM   1205 O  OD2  . ASP   A 1 183 ? -24.429 -8.692  62.981  1.00 79.67  ? 677  ASP   A OD2  1 
ATOM   1206 N  N    . LYS   A 1 184 ? -24.264 -11.027 60.534  1.00 64.46  ? 678  LYS   A N    1 
ATOM   1207 C  CA   . LYS   A 1 184 ? -24.387 -12.463 60.754  1.00 61.32  ? 678  LYS   A CA   1 
ATOM   1208 C  C    . LYS   A 1 184 ? -23.747 -13.254 59.624  1.00 60.69  ? 678  LYS   A C    1 
ATOM   1209 O  O    . LYS   A 1 184 ? -23.284 -14.378 59.843  1.00 60.72  ? 678  LYS   A O    1 
ATOM   1210 C  CB   . LYS   A 1 184 ? -25.859 -12.855 60.886  1.00 65.65  ? 678  LYS   A CB   1 
ATOM   1211 C  CG   . LYS   A 1 184 ? -26.618 -12.133 61.985  1.00 66.53  ? 678  LYS   A CG   1 
ATOM   1212 C  CD   . LYS   A 1 184 ? -28.106 -12.490 61.953  1.00 69.95  ? 678  LYS   A CD   1 
ATOM   1213 C  CE   . LYS   A 1 184 ? -28.850 -11.703 60.863  1.00 67.02  ? 678  LYS   A CE   1 
ATOM   1214 N  NZ   . LYS   A 1 184 ? -29.894 -10.796 61.408  1.00 75.44  ? 678  LYS   A NZ   1 
ATOM   1215 N  N    . PHE   A 1 185 ? -23.709 -12.686 58.417  1.00 57.56  ? 679  PHE   A N    1 
ATOM   1216 C  CA   . PHE   A 1 185 ? -23.175 -13.352 57.234  1.00 54.21  ? 679  PHE   A CA   1 
ATOM   1217 C  C    . PHE   A 1 185 ? -22.255 -12.385 56.502  1.00 53.59  ? 679  PHE   A C    1 
ATOM   1218 O  O    . PHE   A 1 185 ? -22.720 -11.412 55.901  1.00 53.46  ? 679  PHE   A O    1 
ATOM   1219 C  CB   . PHE   A 1 185 ? -24.308 -13.821 56.329  1.00 53.18  ? 679  PHE   A CB   1 
ATOM   1220 C  CG   . PHE   A 1 185 ? -23.881 -14.764 55.259  1.00 50.96  ? 679  PHE   A CG   1 
ATOM   1221 C  CD1  . PHE   A 1 185 ? -23.477 -14.286 54.027  1.00 48.56  ? 679  PHE   A CD1  1 
ATOM   1222 C  CD2  . PHE   A 1 185 ? -23.890 -16.132 55.478  1.00 50.10  ? 679  PHE   A CD2  1 
ATOM   1223 C  CE1  . PHE   A 1 185 ? -23.084 -15.159 53.024  1.00 46.70  ? 679  PHE   A CE1  1 
ATOM   1224 C  CE2  . PHE   A 1 185 ? -23.493 -17.010 54.485  1.00 50.10  ? 679  PHE   A CE2  1 
ATOM   1225 C  CZ   . PHE   A 1 185 ? -23.094 -16.527 53.258  1.00 44.61  ? 679  PHE   A CZ   1 
ATOM   1226 N  N    . ILE   A 1 186 ? -20.960 -12.670 56.530  1.00 51.08  ? 680  ILE   A N    1 
ATOM   1227 C  CA   . ILE   A 1 186 ? -19.928 -11.776 56.022  1.00 47.75  ? 680  ILE   A CA   1 
ATOM   1228 C  C    . ILE   A 1 186 ? -19.443 -12.274 54.668  1.00 48.13  ? 680  ILE   A C    1 
ATOM   1229 O  O    . ILE   A 1 186 ? -19.155 -13.466 54.499  1.00 46.90  ? 680  ILE   A O    1 
ATOM   1230 C  CB   . ILE   A 1 186 ? -18.761 -11.677 57.018  1.00 51.83  ? 680  ILE   A CB   1 
ATOM   1231 C  CG1  . ILE   A 1 186 ? -19.284 -11.272 58.404  1.00 52.76  ? 680  ILE   A CG1  1 
ATOM   1232 C  CG2  . ILE   A 1 186 ? -17.665 -10.758 56.487  1.00 50.60  ? 680  ILE   A CG2  1 
ATOM   1233 C  CD1  . ILE   A 1 186 ? -18.193 -10.819 59.353  1.00 56.17  ? 680  ILE   A CD1  1 
ATOM   1234 N  N    . TYR   A 1 187 ? -19.340 -11.364 53.701  1.00 46.12  ? 681  TYR   A N    1 
ATOM   1235 C  CA   . TYR   A 1 187 ? -18.802 -11.716 52.397  1.00 42.83  ? 681  TYR   A CA   1 
ATOM   1236 C  C    . TYR   A 1 187 ? -17.884 -10.599 51.914  1.00 40.17  ? 681  TYR   A C    1 
ATOM   1237 O  O    . TYR   A 1 187 ? -17.949 -9.460  52.392  1.00 41.11  ? 681  TYR   A O    1 
ATOM   1238 C  CB   . TYR   A 1 187 ? -19.913 -11.997 51.368  1.00 39.54  ? 681  TYR   A CB   1 
ATOM   1239 C  CG   . TYR   A 1 187 ? -20.936 -10.892 51.239  1.00 43.44  ? 681  TYR   A CG   1 
ATOM   1240 C  CD1  . TYR   A 1 187 ? -22.068 -10.857 52.046  1.00 45.25  ? 681  TYR   A CD1  1 
ATOM   1241 C  CD2  . TYR   A 1 187 ? -20.764 -9.879  50.308  1.00 44.41  ? 681  TYR   A CD2  1 
ATOM   1242 C  CE1  . TYR   A 1 187 ? -23.008 -9.840  51.922  1.00 47.35  ? 681  TYR   A CE1  1 
ATOM   1243 C  CE2  . TYR   A 1 187 ? -21.696 -8.855  50.174  1.00 46.21  ? 681  TYR   A CE2  1 
ATOM   1244 C  CZ   . TYR   A 1 187 ? -22.816 -8.843  50.982  1.00 49.77  ? 681  TYR   A CZ   1 
ATOM   1245 O  OH   . TYR   A 1 187 ? -23.729 -7.823  50.838  1.00 47.17  ? 681  TYR   A OH   1 
ATOM   1246 N  N    . ALA   A 1 188 ? -17.017 -10.936 50.960  1.00 40.71  ? 682  ALA   A N    1 
ATOM   1247 C  CA   . ALA   A 1 188 ? -15.936 -10.028 50.597  1.00 38.36  ? 682  ALA   A CA   1 
ATOM   1248 C  C    . ALA   A 1 188 ? -15.299 -10.471 49.286  1.00 38.85  ? 682  ALA   A C    1 
ATOM   1249 O  O    . ALA   A 1 188 ? -15.583 -11.549 48.756  1.00 36.68  ? 682  ALA   A O    1 
ATOM   1250 C  CB   . ALA   A 1 188 ? -14.886 -9.944  51.715  1.00 39.38  ? 682  ALA   A CB   1 
ATOM   1251 N  N    . THR   A 1 189 ? -14.445 -9.597  48.761  1.00 34.24  ? 683  THR   A N    1 
ATOM   1252 C  CA   . THR   A 1 189 ? -13.649 -9.874  47.569  1.00 37.95  ? 683  THR   A CA   1 
ATOM   1253 C  C    . THR   A 1 189 ? -12.236 -9.399  47.911  1.00 32.85  ? 683  THR   A C    1 
ATOM   1254 O  O    . THR   A 1 189 ? -11.893 -9.172  49.073  1.00 33.23  ? 683  THR   A O    1 
ATOM   1255 C  CB   . THR   A 1 189 ? -14.262 -9.191  46.338  1.00 32.96  ? 683  THR   A CB   1 
ATOM   1256 O  OG1  . THR   A 1 189 ? -13.622 -9.650  45.142  1.00 33.60  ? 683  THR   A OG1  1 
ATOM   1257 C  CG2  . THR   A 1 189 ? -14.116 -7.667  46.420  1.00 38.71  ? 683  THR   A CG2  1 
ATOM   1258 N  N    . VAL   A 1 190 ? -11.390 -9.218  46.903  1.00 38.32  ? 684  VAL   A N    1 
ATOM   1259 C  CA   . VAL   A 1 190 ? -9.999  -8.815  47.107  1.00 35.42  ? 684  VAL   A CA   1 
ATOM   1260 C  C    . VAL   A 1 190 ? -9.894  -7.314  46.869  1.00 36.04  ? 684  VAL   A C    1 
ATOM   1261 O  O    . VAL   A 1 190 ? -10.433 -6.799  45.879  1.00 35.90  ? 684  VAL   A O    1 
ATOM   1262 C  CB   . VAL   A 1 190 ? -9.064  -9.590  46.164  1.00 33.14  ? 684  VAL   A CB   1 
ATOM   1263 C  CG1  . VAL   A 1 190 ? -7.612  -9.206  46.408  1.00 34.41  ? 684  VAL   A CG1  1 
ATOM   1264 C  CG2  . VAL   A 1 190 ? -9.299  -11.109 46.308  1.00 34.75  ? 684  VAL   A CG2  1 
ATOM   1265 N  N    . LYS   A 1 191 ? -9.221  -6.607  47.777  1.00 34.87  ? 685  LYS   A N    1 
ATOM   1266 C  CA   . LYS   A 1 191 ? -9.052  -5.165  47.609  1.00 37.05  ? 685  LYS   A CA   1 
ATOM   1267 C  C    . LYS   A 1 191 ? -8.297  -4.861  46.316  1.00 38.92  ? 685  LYS   A C    1 
ATOM   1268 O  O    . LYS   A 1 191 ? -7.448  -5.643  45.866  1.00 37.30  ? 685  LYS   A O    1 
ATOM   1269 C  CB   . LYS   A 1 191 ? -8.286  -4.564  48.794  1.00 42.41  ? 685  LYS   A CB   1 
ATOM   1270 C  CG   . LYS   A 1 191 ? -8.726  -5.087  50.149  1.00 43.68  ? 685  LYS   A CG   1 
ATOM   1271 C  CD   . LYS   A 1 191 ? -8.661  -4.044  51.239  1.00 46.01  ? 685  LYS   A CD   1 
ATOM   1272 C  CE   . LYS   A 1 191 ? -7.247  -3.694  51.614  1.00 46.92  ? 685  LYS   A CE   1 
ATOM   1273 N  NZ   . LYS   A 1 191 ? -7.192  -3.127  53.016  1.00 53.67  ? 685  LYS   A NZ   1 
ATOM   1274 N  N    . GLN   A 1 192 ? -8.616  -3.712  45.714  1.00 36.28  ? 686  GLN   A N    1 
ATOM   1275 C  CA   . GLN   A 1 192 ? -7.879  -3.202  44.549  1.00 37.89  ? 686  GLN   A CA   1 
ATOM   1276 C  C    . GLN   A 1 192 ? -7.784  -4.246  43.440  1.00 38.26  ? 686  GLN   A C    1 
ATOM   1277 O  O    . GLN   A 1 192 ? -6.750  -4.408  42.779  1.00 36.80  ? 686  GLN   A O    1 
ATOM   1278 C  CB   . GLN   A 1 192 ? -6.501  -2.706  44.971  1.00 39.46  ? 686  GLN   A CB   1 
ATOM   1279 C  CG   . GLN   A 1 192 ? -6.583  -1.498  45.889  1.00 40.68  ? 686  GLN   A CG   1 
ATOM   1280 C  CD   . GLN   A 1 192 ? -5.386  -1.388  46.784  1.00 50.73  ? 686  GLN   A CD   1 
ATOM   1281 O  OE1  . GLN   A 1 192 ? -4.330  -0.904  46.375  1.00 57.88  ? 686  GLN   A OE1  1 
ATOM   1282 N  NE2  . GLN   A 1 192 ? -5.535  -1.848  48.026  1.00 50.07  ? 686  GLN   A NE2  1 
ATOM   1283 N  N    . SER   A 1 193 ? -8.882  -4.971  43.243  1.00 33.26  ? 687  SER   A N    1 
ATOM   1284 C  CA   . SER   A 1 193 ? -9.053  -5.911  42.143  1.00 34.19  ? 687  SER   A CA   1 
ATOM   1285 C  C    . SER   A 1 193 ? -10.179 -5.431  41.236  1.00 36.76  ? 687  SER   A C    1 
ATOM   1286 O  O    . SER   A 1 193 ? -10.940 -4.511  41.579  1.00 33.18  ? 687  SER   A O    1 
ATOM   1287 C  CB   . SER   A 1 193 ? -9.388  -7.314  42.668  1.00 33.73  ? 687  SER   A CB   1 
ATOM   1288 O  OG   . SER   A 1 193 ? -10.724 -7.289  43.165  1.00 34.33  ? 687  SER   A OG   1 
ATOM   1289 N  N    . SER   A 1 194 ? -10.311 -6.099  40.083  1.00 35.66  ? 688  SER   A N    1 
ATOM   1290 C  CA   . SER   A 1 194 ? -11.400 -5.770  39.172  1.00 35.09  ? 688  SER   A CA   1 
ATOM   1291 C  C    . SER   A 1 194 ? -12.759 -6.025  39.811  1.00 32.58  ? 688  SER   A C    1 
ATOM   1292 O  O    . SER   A 1 194 ? -13.723 -5.335  39.495  1.00 33.56  ? 688  SER   A O    1 
ATOM   1293 C  CB   . SER   A 1 194 ? -11.279 -6.569  37.879  1.00 34.35  ? 688  SER   A CB   1 
ATOM   1294 O  OG   . SER   A 1 194 ? -11.392 -7.966  38.123  1.00 32.98  ? 688  SER   A OG   1 
ATOM   1295 N  N    . VAL   A 1 195 ? -12.844 -7.010  40.704  1.00 35.81  ? 689  VAL   A N    1 
ATOM   1296 C  CA   . VAL   A 1 195 ? -14.114 -7.369  41.311  1.00 31.50  ? 689  VAL   A CA   1 
ATOM   1297 C  C    . VAL   A 1 195 ? -14.565 -6.292  42.282  1.00 37.47  ? 689  VAL   A C    1 
ATOM   1298 O  O    . VAL   A 1 195 ? -15.749 -5.945  42.334  1.00 37.87  ? 689  VAL   A O    1 
ATOM   1299 C  CB   . VAL   A 1 195 ? -13.995 -8.737  41.997  1.00 34.38  ? 689  VAL   A CB   1 
ATOM   1300 C  CG1  . VAL   A 1 195 ? -15.373 -9.219  42.438  1.00 36.47  ? 689  VAL   A CG1  1 
ATOM   1301 C  CG2  . VAL   A 1 195 ? -13.357 -9.744  41.042  1.00 34.65  ? 689  VAL   A CG2  1 
ATOM   1302 N  N    . ASP   A 1 196 ? -13.638 -5.783  43.095  1.00 31.44  ? 690  ASP   A N    1 
ATOM   1303 C  CA   . ASP   A 1 196 ? -13.903 -4.621  43.939  1.00 34.74  ? 690  ASP   A CA   1 
ATOM   1304 C  C    . ASP   A 1 196 ? -14.517 -3.472  43.137  1.00 39.44  ? 690  ASP   A C    1 
ATOM   1305 O  O    . ASP   A 1 196 ? -15.516 -2.865  43.558  1.00 36.21  ? 690  ASP   A O    1 
ATOM   1306 C  CB   . ASP   A 1 196 ? -12.587 -4.207  44.593  1.00 36.12  ? 690  ASP   A CB   1 
ATOM   1307 C  CG   . ASP   A 1 196 ? -12.742 -3.147  45.684  1.00 46.61  ? 690  ASP   A CG   1 
ATOM   1308 O  OD1  . ASP   A 1 196 ? -13.877 -2.844  46.118  1.00 41.24  ? 690  ASP   A OD1  1 
ATOM   1309 O  OD2  . ASP   A 1 196 ? -11.683 -2.636  46.122  1.00 47.72  ? 690  ASP   A OD2  1 
ATOM   1310 N  N    . ILE   A 1 197 ? -13.932 -3.166  41.973  1.00 34.34  ? 691  ILE   A N    1 
ATOM   1311 C  CA   . ILE   A 1 197 ? -14.424 -2.063  41.158  1.00 40.59  ? 691  ILE   A CA   1 
ATOM   1312 C  C    . ILE   A 1 197 ? -15.754 -2.396  40.532  1.00 38.98  ? 691  ILE   A C    1 
ATOM   1313 O  O    . ILE   A 1 197 ? -16.591 -1.505  40.325  1.00 40.24  ? 691  ILE   A O    1 
ATOM   1314 C  CB   . ILE   A 1 197 ? -13.393 -1.695  40.083  1.00 41.26  ? 691  ILE   A CB   1 
ATOM   1315 C  CG1  . ILE   A 1 197 ? -12.203 -1.123  40.801  1.00 44.12  ? 691  ILE   A CG1  1 
ATOM   1316 C  CG2  . ILE   A 1 197 ? -13.970 -0.706  39.061  1.00 41.40  ? 691  ILE   A CG2  1 
ATOM   1317 C  CD1  . ILE   A 1 197 ? -11.507 -0.210  39.980  1.00 51.59  ? 691  ILE   A CD1  1 
ATOM   1318 N  N    . TYR   A 1 198 ? -15.961 -3.668  40.185  1.00 36.04  ? 692  TYR   A N    1 
ATOM   1319 C  CA   . TYR   A 1 198 ? -17.253 -4.074  39.654  1.00 40.38  ? 692  TYR   A CA   1 
ATOM   1320 C  C    . TYR   A 1 198 ? -18.369 -3.693  40.615  1.00 41.50  ? 692  TYR   A C    1 
ATOM   1321 O  O    . TYR   A 1 198 ? -19.398 -3.148  40.200  1.00 38.17  ? 692  TYR   A O    1 
ATOM   1322 C  CB   . TYR   A 1 198 ? -17.247 -5.575  39.392  1.00 36.51  ? 692  TYR   A CB   1 
ATOM   1323 C  CG   . TYR   A 1 198 ? -18.589 -6.195  39.039  1.00 38.91  ? 692  TYR   A CG   1 
ATOM   1324 C  CD1  . TYR   A 1 198 ? -19.015 -6.274  37.723  1.00 40.15  ? 692  TYR   A CD1  1 
ATOM   1325 C  CD2  . TYR   A 1 198 ? -19.408 -6.733  40.020  1.00 44.09  ? 692  TYR   A CD2  1 
ATOM   1326 C  CE1  . TYR   A 1 198 ? -20.242 -6.864  37.393  1.00 46.47  ? 692  TYR   A CE1  1 
ATOM   1327 C  CE2  . TYR   A 1 198 ? -20.629 -7.312  39.706  1.00 41.25  ? 692  TYR   A CE2  1 
ATOM   1328 C  CZ   . TYR   A 1 198 ? -21.039 -7.381  38.397  1.00 44.43  ? 692  TYR   A CZ   1 
ATOM   1329 O  OH   . TYR   A 1 198 ? -22.251 -7.969  38.095  1.00 46.97  ? 692  TYR   A OH   1 
ATOM   1330 N  N    . PHE   A 1 199 ? -18.165 -3.932  41.912  1.00 39.45  ? 693  PHE   A N    1 
ATOM   1331 C  CA   . PHE   A 1 199 ? -19.187 -3.589  42.896  1.00 42.04  ? 693  PHE   A CA   1 
ATOM   1332 C  C    . PHE   A 1 199 ? -19.210 -2.092  43.209  1.00 44.17  ? 693  PHE   A C    1 
ATOM   1333 O  O    . PHE   A 1 199 ? -20.276 -1.545  43.510  1.00 43.08  ? 693  PHE   A O    1 
ATOM   1334 C  CB   . PHE   A 1 199 ? -18.969 -4.416  44.168  1.00 40.18  ? 693  PHE   A CB   1 
ATOM   1335 C  CG   . PHE   A 1 199 ? -19.455 -5.834  44.040  1.00 40.97  ? 693  PHE   A CG   1 
ATOM   1336 C  CD1  . PHE   A 1 199 ? -18.631 -6.815  43.502  1.00 39.00  ? 693  PHE   A CD1  1 
ATOM   1337 C  CD2  . PHE   A 1 199 ? -20.737 -6.185  44.430  1.00 43.14  ? 693  PHE   A CD2  1 
ATOM   1338 C  CE1  . PHE   A 1 199 ? -19.082 -8.114  43.364  1.00 39.44  ? 693  PHE   A CE1  1 
ATOM   1339 C  CE2  . PHE   A 1 199 ? -21.191 -7.488  44.293  1.00 42.21  ? 693  PHE   A CE2  1 
ATOM   1340 C  CZ   . PHE   A 1 199 ? -20.365 -8.449  43.764  1.00 40.56  ? 693  PHE   A CZ   1 
ATOM   1341 N  N    . ARG   A 1 200 ? -18.067 -1.408  43.127  1.00 42.31  ? 694  ARG   A N    1 
ATOM   1342 C  CA   . ARG   A 1 200 ? -18.057 0.033   43.388  1.00 45.00  ? 694  ARG   A CA   1 
ATOM   1343 C  C    . ARG   A 1 200 ? -18.828 0.807   42.322  1.00 44.66  ? 694  ARG   A C    1 
ATOM   1344 O  O    . ARG   A 1 200 ? -19.491 1.805   42.628  1.00 49.15  ? 694  ARG   A O    1 
ATOM   1345 C  CB   . ARG   A 1 200 ? -16.623 0.547   43.453  1.00 48.21  ? 694  ARG   A CB   1 
ATOM   1346 C  CG   . ARG   A 1 200 ? -16.519 2.076   43.536  1.00 56.91  ? 694  ARG   A CG   1 
ATOM   1347 C  CD   . ARG   A 1 200 ? -15.227 2.570   42.895  1.00 59.81  ? 694  ARG   A CD   1 
ATOM   1348 N  NE   . ARG   A 1 200 ? -14.058 2.209   43.685  1.00 62.46  ? 694  ARG   A NE   1 
ATOM   1349 C  CZ   . ARG   A 1 200 ? -13.752 2.726   44.868  1.00 70.37  ? 694  ARG   A CZ   1 
ATOM   1350 N  NH1  . ARG   A 1 200 ? -14.492 3.674   45.425  1.00 68.65  ? 694  ARG   A NH1  1 
ATOM   1351 N  NH2  . ARG   A 1 200 ? -12.671 2.284   45.505  1.00 69.45  ? 694  ARG   A NH2  1 
ATOM   1352 N  N    . ARG   A 1 201 ? -18.771 0.351   41.069  1.00 43.50  ? 695  ARG   A N    1 
ATOM   1353 C  CA   . ARG   A 1 201 ? -19.231 1.155   39.941  1.00 50.56  ? 695  ARG   A CA   1 
ATOM   1354 C  C    . ARG   A 1 201 ? -20.743 1.084   39.731  1.00 50.57  ? 695  ARG   A C    1 
ATOM   1355 O  O    . ARG   A 1 201 ? -21.336 2.061   39.262  1.00 53.16  ? 695  ARG   A O    1 
ATOM   1356 C  CB   . ARG   A 1 201 ? -18.511 0.718   38.661  1.00 48.50  ? 695  ARG   A CB   1 
ATOM   1357 N  N    . GLN   A 1 202 ? -21.385 -0.043  40.054  1.00 46.15  ? 696  GLN   A N    1 
ATOM   1358 C  CA   . GLN   A 1 202 ? -22.813 -0.220  39.785  1.00 49.61  ? 696  GLN   A CA   1 
ATOM   1359 C  C    . GLN   A 1 202 ? -23.634 0.164   41.016  1.00 51.07  ? 696  GLN   A C    1 
ATOM   1360 O  O    . GLN   A 1 202 ? -23.494 -0.445  42.086  1.00 49.13  ? 696  GLN   A O    1 
ATOM   1361 C  CB   . GLN   A 1 202 ? -23.107 -1.662  39.369  1.00 45.95  ? 696  GLN   A CB   1 
ATOM   1362 C  CG   . GLN   A 1 202 ? -21.978 -2.290  38.593  1.00 51.78  ? 696  GLN   A CG   1 
ATOM   1363 C  CD   . GLN   A 1 202 ? -22.413 -3.254  37.504  1.00 52.91  ? 696  GLN   A CD   1 
ATOM   1364 O  OE1  . GLN   A 1 202 ? -23.580 -3.342  37.140  1.00 51.98  ? 696  GLN   A OE1  1 
ATOM   1365 N  NE2  . GLN   A 1 202 ? -21.445 -3.983  36.968  1.00 57.71  ? 696  GLN   A NE2  1 
ATOM   1366 N  N    . VAL   A 1 203 ? -24.500 1.167   40.857  1.00 48.22  ? 697  VAL   A N    1 
ATOM   1367 C  CA   . VAL   A 1 203 ? -25.338 1.613   41.964  1.00 50.10  ? 697  VAL   A CA   1 
ATOM   1368 C  C    . VAL   A 1 203 ? -26.294 0.512   42.395  1.00 47.62  ? 697  VAL   A C    1 
ATOM   1369 O  O    . VAL   A 1 203 ? -26.679 0.441   43.570  1.00 50.42  ? 697  VAL   A O    1 
ATOM   1370 C  CB   . VAL   A 1 203 ? -26.100 2.890   41.564  1.00 55.98  ? 697  VAL   A CB   1 
ATOM   1371 C  CG1  . VAL   A 1 203 ? -25.143 4.082   41.516  1.00 54.64  ? 697  VAL   A CG1  1 
ATOM   1372 C  CG2  . VAL   A 1 203 ? -26.791 2.684   40.229  1.00 53.46  ? 697  VAL   A CG2  1 
ATOM   1373 N  N    . GLU   A 1 204 ? -26.695 -0.361  41.464  1.00 45.02  ? 698  GLU   A N    1 
ATOM   1374 C  CA   . GLU   A 1 204 ? -27.556 -1.490  41.804  1.00 51.47  ? 698  GLU   A CA   1 
ATOM   1375 C  C    . GLU   A 1 204 ? -26.901 -2.437  42.805  1.00 53.67  ? 698  GLU   A C    1 
ATOM   1376 O  O    . GLU   A 1 204 ? -27.600 -3.232  43.442  1.00 47.83  ? 698  GLU   A O    1 
ATOM   1377 C  CB   . GLU   A 1 204 ? -27.933 -2.268  40.542  1.00 47.82  ? 698  GLU   A CB   1 
ATOM   1378 N  N    . LEU   A 1 205 ? -25.577 -2.388  42.955  1.00 46.50  ? 699  LEU   A N    1 
ATOM   1379 C  CA   . LEU   A 1 205 ? -24.901 -3.246  43.917  1.00 48.54  ? 699  LEU   A CA   1 
ATOM   1380 C  C    . LEU   A 1 205 ? -24.349 -2.465  45.106  1.00 48.85  ? 699  LEU   A C    1 
ATOM   1381 O  O    . LEU   A 1 205 ? -23.532 -2.997  45.860  1.00 45.62  ? 699  LEU   A O    1 
ATOM   1382 C  CB   . LEU   A 1 205 ? -23.788 -4.054  43.240  1.00 46.33  ? 699  LEU   A CB   1 
ATOM   1383 C  CG   . LEU   A 1 205 ? -24.075 -4.706  41.881  1.00 45.97  ? 699  LEU   A CG   1 
ATOM   1384 C  CD1  . LEU   A 1 205 ? -22.809 -4.812  41.005  1.00 49.00  ? 699  LEU   A CD1  1 
ATOM   1385 C  CD2  . LEU   A 1 205 ? -24.724 -6.071  42.047  1.00 53.05  ? 699  LEU   A CD2  1 
ATOM   1386 N  N    . SER   A 1 206 ? -24.808 -1.225  45.314  1.00 47.03  ? 700  SER   A N    1 
ATOM   1387 C  CA   . SER   A 1 206 ? -24.209 -0.386  46.345  1.00 49.32  ? 700  SER   A CA   1 
ATOM   1388 C  C    . SER   A 1 206 ? -24.374 -0.996  47.731  1.00 50.20  ? 700  SER   A C    1 
ATOM   1389 O  O    . SER   A 1 206 ? -23.487 -0.861  48.578  1.00 49.18  ? 700  SER   A O    1 
ATOM   1390 C  CB   . SER   A 1 206 ? -24.821 1.015   46.325  1.00 49.21  ? 700  SER   A CB   1 
ATOM   1391 O  OG   . SER   A 1 206 ? -26.159 0.972   46.782  1.00 53.56  ? 700  SER   A OG   1 
ATOM   1392 N  N    . THR   A 1 207 ? -25.517 -1.643  47.994  1.00 48.30  ? 701  THR   A N    1 
ATOM   1393 C  CA   . THR   A 1 207 ? -25.716 -2.256  49.307  1.00 48.03  ? 701  THR   A CA   1 
ATOM   1394 C  C    . THR   A 1 207 ? -24.666 -3.327  49.576  1.00 45.62  ? 701  THR   A C    1 
ATOM   1395 O  O    . THR   A 1 207 ? -24.172 -3.463  50.702  1.00 44.41  ? 701  THR   A O    1 
ATOM   1396 C  CB   . THR   A 1 207 ? -27.116 -2.856  49.416  1.00 47.15  ? 701  THR   A CB   1 
ATOM   1397 O  OG1  . THR   A 1 207 ? -28.098 -1.919  48.940  1.00 53.76  ? 701  THR   A OG1  1 
ATOM   1398 C  CG2  . THR   A 1 207 ? -27.410 -3.209  50.865  1.00 53.17  ? 701  THR   A CG2  1 
ATOM   1399 N  N    . MET   A 1 208 ? -24.326 -4.104  48.553  1.00 43.98  ? 702  MET   A N    1 
ATOM   1400 C  CA   . MET   A 1 208 ? -23.271 -5.101  48.695  1.00 44.28  ? 702  MET   A CA   1 
ATOM   1401 C  C    . MET   A 1 208 ? -21.894 -4.452  48.832  1.00 45.91  ? 702  MET   A C    1 
ATOM   1402 O  O    . MET   A 1 208 ? -21.117 -4.816  49.717  1.00 46.40  ? 702  MET   A O    1 
ATOM   1403 C  CB   . MET   A 1 208 ? -23.324 -6.057  47.505  1.00 43.76  ? 702  MET   A CB   1 
ATOM   1404 C  CG   . MET   A 1 208 ? -24.547 -6.970  47.533  1.00 45.02  ? 702  MET   A CG   1 
ATOM   1405 S  SD   . MET   A 1 208 ? -24.589 -8.096  46.120  1.00 46.61  ? 702  MET   A SD   1 
ATOM   1406 C  CE   . MET   A 1 208 ? -23.644 -9.452  46.835  1.00 45.69  ? 702  MET   A CE   1 
ATOM   1407 N  N    . TYR   A 1 209 ? -21.581 -3.475  47.982  1.00 45.90  ? 703  TYR   A N    1 
ATOM   1408 C  CA   . TYR   A 1 209 ? -20.260 -2.858  48.023  1.00 46.89  ? 703  TYR   A CA   1 
ATOM   1409 C  C    . TYR   A 1 209 ? -19.959 -2.268  49.399  1.00 49.09  ? 703  TYR   A C    1 
ATOM   1410 O  O    . TYR   A 1 209 ? -18.825 -2.350  49.883  1.00 50.02  ? 703  TYR   A O    1 
ATOM   1411 C  CB   . TYR   A 1 209 ? -20.159 -1.783  46.938  1.00 50.04  ? 703  TYR   A CB   1 
ATOM   1412 C  CG   . TYR   A 1 209 ? -18.905 -0.946  47.030  1.00 50.65  ? 703  TYR   A CG   1 
ATOM   1413 C  CD1  . TYR   A 1 209 ? -17.674 -1.460  46.615  1.00 44.97  ? 703  TYR   A CD1  1 
ATOM   1414 C  CD2  . TYR   A 1 209 ? -18.945 0.341   47.540  1.00 47.95  ? 703  TYR   A CD2  1 
ATOM   1415 C  CE1  . TYR   A 1 209 ? -16.522 -0.704  46.707  1.00 49.77  ? 703  TYR   A CE1  1 
ATOM   1416 C  CE2  . TYR   A 1 209 ? -17.807 1.101   47.632  1.00 51.67  ? 703  TYR   A CE2  1 
ATOM   1417 C  CZ   . TYR   A 1 209 ? -16.598 0.575   47.215  1.00 51.30  ? 703  TYR   A CZ   1 
ATOM   1418 O  OH   . TYR   A 1 209 ? -15.470 1.341   47.303  1.00 51.55  ? 703  TYR   A OH   1 
ATOM   1419 N  N    . ARG   A 1 210 ? -20.968 -1.687  50.054  1.00 46.50  ? 704  ARG   A N    1 
ATOM   1420 C  CA   . ARG   A 1 210 ? -20.744 -1.083  51.365  1.00 50.47  ? 704  ARG   A CA   1 
ATOM   1421 C  C    . ARG   A 1 210 ? -20.540 -2.135  52.450  1.00 50.21  ? 704  ARG   A C    1 
ATOM   1422 O  O    . ARG   A 1 210 ? -19.840 -1.879  53.438  1.00 50.72  ? 704  ARG   A O    1 
ATOM   1423 C  CB   . ARG   A 1 210 ? -21.911 -0.159  51.714  1.00 50.62  ? 704  ARG   A CB   1 
ATOM   1424 C  CG   . ARG   A 1 210 ? -21.969 1.100   50.849  1.00 52.86  ? 704  ARG   A CG   1 
ATOM   1425 C  CD   . ARG   A 1 210 ? -20.644 1.860   50.895  1.00 56.94  ? 704  ARG   A CD   1 
ATOM   1426 N  NE   . ARG   A 1 210 ? -20.508 2.833   49.813  1.00 59.01  ? 704  ARG   A NE   1 
ATOM   1427 C  CZ   . ARG   A 1 210 ? -19.650 3.846   49.819  1.00 61.71  ? 704  ARG   A CZ   1 
ATOM   1428 N  NH1  . ARG   A 1 210 ? -18.800 4.029   50.819  1.00 63.01  ? 704  ARG   A NH1  1 
ATOM   1429 N  NH2  . ARG   A 1 210 ? -19.631 4.688   48.789  1.00 64.32  ? 704  ARG   A NH2  1 
ATOM   1430 N  N    . HIS   A 1 211 ? -21.137 -3.319  52.288  1.00 50.04  ? 705  HIS   A N    1 
ATOM   1431 C  CA   . HIS   A 1 211 ? -20.818 -4.426  53.186  1.00 48.47  ? 705  HIS   A CA   1 
ATOM   1432 C  C    . HIS   A 1 211 ? -19.394 -4.919  52.944  1.00 44.95  ? 705  HIS   A C    1 
ATOM   1433 O  O    . HIS   A 1 211 ? -18.603 -5.052  53.882  1.00 48.96  ? 705  HIS   A O    1 
ATOM   1434 C  CB   . HIS   A 1 211 ? -21.829 -5.561  52.997  1.00 48.78  ? 705  HIS   A CB   1 
ATOM   1435 C  CG   . HIS   A 1 211 ? -21.520 -6.791  53.799  1.00 50.67  ? 705  HIS   A CG   1 
ATOM   1436 N  ND1  . HIS   A 1 211 ? -22.110 -7.055  55.015  1.00 51.69  ? 705  HIS   A ND1  1 
ATOM   1437 C  CD2  . HIS   A 1 211 ? -20.682 -7.829  53.554  1.00 50.60  ? 705  HIS   A CD2  1 
ATOM   1438 C  CE1  . HIS   A 1 211 ? -21.645 -8.196  55.490  1.00 52.25  ? 705  HIS   A CE1  1 
ATOM   1439 N  NE2  . HIS   A 1 211 ? -20.780 -8.689  54.623  1.00 51.23  ? 705  HIS   A NE2  1 
ATOM   1440 N  N    . MET   A 1 212 ? -19.042 -5.155  51.679  1.00 44.38  ? 706  MET   A N    1 
ATOM   1441 C  CA   . MET   A 1 212 ? -17.756 -5.770  51.365  1.00 47.30  ? 706  MET   A CA   1 
ATOM   1442 C  C    . MET   A 1 212 ? -16.588 -4.843  51.682  1.00 48.55  ? 706  MET   A C    1 
ATOM   1443 O  O    . MET   A 1 212 ? -15.494 -5.322  52.007  1.00 47.76  ? 706  MET   A O    1 
ATOM   1444 C  CB   . MET   A 1 212 ? -17.721 -6.178  49.891  1.00 43.57  ? 706  MET   A CB   1 
ATOM   1445 C  CG   . MET   A 1 212 ? -18.698 -7.272  49.535  1.00 43.96  ? 706  MET   A CG   1 
ATOM   1446 S  SD   . MET   A 1 212 ? -19.109 -7.229  47.771  1.00 51.48  ? 706  MET   A SD   1 
ATOM   1447 C  CE   . MET   A 1 212 ? -17.566 -7.845  47.143  1.00 39.01  ? 706  MET   A CE   1 
ATOM   1448 N  N    . GLU   A 1 213 ? -16.804 -3.522  51.604  1.00 46.09  ? 707  GLU   A N    1 
ATOM   1449 C  CA   . GLU   A 1 213 ? -15.744 -2.557  51.895  1.00 47.05  ? 707  GLU   A CA   1 
ATOM   1450 C  C    . GLU   A 1 213 ? -15.176 -2.751  53.293  1.00 50.05  ? 707  GLU   A C    1 
ATOM   1451 O  O    . GLU   A 1 213 ? -13.996 -2.476  53.533  1.00 51.38  ? 707  GLU   A O    1 
ATOM   1452 C  CB   . GLU   A 1 213 ? -16.276 -1.125  51.740  1.00 49.72  ? 707  GLU   A CB   1 
ATOM   1453 N  N    . LYS   A 1 214 ? -15.993 -3.216  54.225  1.00 50.18  ? 708  LYS   A N    1 
ATOM   1454 C  CA   . LYS   A 1 214 ? -15.521 -3.437  55.580  1.00 50.10  ? 708  LYS   A CA   1 
ATOM   1455 C  C    . LYS   A 1 214 ? -14.776 -4.755  55.740  1.00 49.42  ? 708  LYS   A C    1 
ATOM   1456 O  O    . LYS   A 1 214 ? -14.171 -4.974  56.792  1.00 52.04  ? 708  LYS   A O    1 
ATOM   1457 C  CB   . LYS   A 1 214 ? -16.707 -3.382  56.554  1.00 52.00  ? 708  LYS   A CB   1 
ATOM   1458 N  N    . HIS   A 1 215 ? -14.800 -5.647  54.744  1.00 47.65  ? 709  HIS   A N    1 
ATOM   1459 C  CA   . HIS   A 1 215 ? -14.253 -6.981  54.943  1.00 48.88  ? 709  HIS   A CA   1 
ATOM   1460 C  C    . HIS   A 1 215 ? -13.344 -7.489  53.831  1.00 45.75  ? 709  HIS   A C    1 
ATOM   1461 O  O    . HIS   A 1 215 ? -12.868 -8.620  53.929  1.00 44.45  ? 709  HIS   A O    1 
ATOM   1462 C  CB   . HIS   A 1 215 ? -15.383 -8.001  55.156  1.00 49.69  ? 709  HIS   A CB   1 
ATOM   1463 C  CG   . HIS   A 1 215 ? -16.371 -7.593  56.203  1.00 52.49  ? 709  HIS   A CG   1 
ATOM   1464 N  ND1  . HIS   A 1 215 ? -17.593 -7.032  55.899  1.00 52.50  ? 709  HIS   A ND1  1 
ATOM   1465 C  CD2  . HIS   A 1 215 ? -16.300 -7.630  57.555  1.00 53.29  ? 709  HIS   A CD2  1 
ATOM   1466 C  CE1  . HIS   A 1 215 ? -18.241 -6.764  57.018  1.00 50.93  ? 709  HIS   A CE1  1 
ATOM   1467 N  NE2  . HIS   A 1 215 ? -17.476 -7.108  58.037  1.00 53.20  ? 709  HIS   A NE2  1 
ATOM   1468 N  N    . ASN   A 1 216 ? -13.083 -6.697  52.796  1.00 42.20  ? 710  ASN   A N    1 
ATOM   1469 C  CA   . ASN   A 1 216 ? -12.260 -7.152  51.683  1.00 45.69  ? 710  ASN   A CA   1 
ATOM   1470 C  C    . ASN   A 1 216 ? -10.858 -7.544  52.162  1.00 42.52  ? 710  ASN   A C    1 
ATOM   1471 O  O    . ASN   A 1 216 ? -10.317 -6.970  53.105  1.00 41.43  ? 710  ASN   A O    1 
ATOM   1472 C  CB   . ASN   A 1 216 ? -12.167 -6.052  50.625  1.00 39.97  ? 710  ASN   A CB   1 
ATOM   1473 C  CG   . ASN   A 1 216 ? -13.419 -5.930  49.805  1.00 43.30  ? 710  ASN   A CG   1 
ATOM   1474 O  OD1  . ASN   A 1 216 ? -14.180 -6.887  49.680  1.00 41.38  ? 710  ASN   A OD1  1 
ATOM   1475 N  ND2  . ASN   A 1 216 ? -13.648 -4.744  49.234  1.00 43.76  ? 710  ASN   A ND2  1 
ATOM   1476 N  N    . TYR   A 1 217 ? -10.272 -8.538  51.499  1.00 40.96  ? 711  TYR   A N    1 
ATOM   1477 C  CA   . TYR   A 1 217 ? -9.001  -9.145  51.878  1.00 42.01  ? 711  TYR   A CA   1 
ATOM   1478 C  C    . TYR   A 1 217 ? -7.858  -8.663  50.983  1.00 41.41  ? 711  TYR   A C    1 
ATOM   1479 O  O    . TYR   A 1 217 ? -8.074  -8.157  49.876  1.00 39.07  ? 711  TYR   A O    1 
ATOM   1480 C  CB   . TYR   A 1 217 ? -9.122  -10.680 51.826  1.00 41.88  ? 711  TYR   A CB   1 
ATOM   1481 C  CG   . TYR   A 1 217 ? -9.833  -11.258 53.041  1.00 43.28  ? 711  TYR   A CG   1 
ATOM   1482 C  CD1  . TYR   A 1 217 ? -11.205 -11.107 53.212  1.00 42.29  ? 711  TYR   A CD1  1 
ATOM   1483 C  CD2  . TYR   A 1 217 ? -9.123  -11.957 54.013  1.00 46.06  ? 711  TYR   A CD2  1 
ATOM   1484 C  CE1  . TYR   A 1 217 ? -11.850 -11.625 54.325  1.00 45.88  ? 711  TYR   A CE1  1 
ATOM   1485 C  CE2  . TYR   A 1 217 ? -9.755  -12.481 55.135  1.00 46.08  ? 711  TYR   A CE2  1 
ATOM   1486 C  CZ   . TYR   A 1 217 ? -11.120 -12.314 55.283  1.00 50.22  ? 711  TYR   A CZ   1 
ATOM   1487 O  OH   . TYR   A 1 217 ? -11.756 -12.836 56.387  1.00 49.91  ? 711  TYR   A OH   1 
ATOM   1488 N  N    . GLU   A 1 218 ? -6.622  -8.842  51.461  1.00 39.18  ? 712  GLU   A N    1 
ATOM   1489 C  CA   . GLU   A 1 218 ? -5.473  -8.346  50.700  1.00 40.93  ? 712  GLU   A CA   1 
ATOM   1490 C  C    . GLU   A 1 218 ? -5.147  -9.243  49.508  1.00 38.46  ? 712  GLU   A C    1 
ATOM   1491 O  O    . GLU   A 1 218 ? -4.625  -8.766  48.487  1.00 37.99  ? 712  GLU   A O    1 
ATOM   1492 C  CB   . GLU   A 1 218 ? -4.251  -8.194  51.617  1.00 41.26  ? 712  GLU   A CB   1 
ATOM   1493 C  CG   . GLU   A 1 218 ? -4.494  -7.331  52.875  1.00 41.07  ? 712  GLU   A CG   1 
ATOM   1494 C  CD   . GLU   A 1 218 ? -4.639  -5.839  52.563  1.00 47.36  ? 712  GLU   A CD   1 
ATOM   1495 O  OE1  . GLU   A 1 218 ? -4.221  -5.404  51.462  1.00 45.98  ? 712  GLU   A OE1  1 
ATOM   1496 O  OE2  . GLU   A 1 218 ? -5.150  -5.095  53.431  1.00 49.93  ? 712  GLU   A OE2  1 
ATOM   1497 N  N    . SER   A 1 219 ? -5.466  -10.526 49.596  1.00 35.15  ? 713  SER   A N    1 
ATOM   1498 C  CA   . SER   A 1 219 ? -5.194  -11.443 48.501  1.00 35.63  ? 713  SER   A CA   1 
ATOM   1499 C  C    . SER   A 1 219 ? -6.259  -12.524 48.492  1.00 36.78  ? 713  SER   A C    1 
ATOM   1500 O  O    . SER   A 1 219 ? -6.928  -12.770 49.498  1.00 37.07  ? 713  SER   A O    1 
ATOM   1501 C  CB   . SER   A 1 219 ? -3.808  -12.087 48.621  1.00 41.00  ? 713  SER   A CB   1 
ATOM   1502 O  OG   . SER   A 1 219 ? -3.759  -12.947 49.753  1.00 39.16  ? 713  SER   A OG   1 
ATOM   1503 N  N    . ALA   A 1 220 ? -6.399  -13.167 47.329  1.00 33.35  ? 714  ALA   A N    1 
ATOM   1504 C  CA   . ALA   A 1 220 ? -7.376  -14.234 47.169  1.00 35.27  ? 714  ALA   A CA   1 
ATOM   1505 C  C    . ALA   A 1 220 ? -7.069  -15.413 48.088  1.00 40.04  ? 714  ALA   A C    1 
ATOM   1506 O  O    . ALA   A 1 220 ? -7.986  -16.040 48.628  1.00 36.43  ? 714  ALA   A O    1 
ATOM   1507 C  CB   . ALA   A 1 220 ? -7.415  -14.678 45.705  1.00 32.31  ? 714  ALA   A CB   1 
ATOM   1508 N  N    . ALA   A 1 221 ? -5.783  -15.732 48.280  1.00 39.49  ? 715  ALA   A N    1 
ATOM   1509 C  CA   . ALA   A 1 221 ? -5.431  -16.880 49.117  1.00 39.40  ? 715  ALA   A CA   1 
ATOM   1510 C  C    . ALA   A 1 221 ? -5.853  -16.655 50.566  1.00 39.95  ? 715  ALA   A C    1 
ATOM   1511 O  O    . ALA   A 1 221 ? -6.307  -17.586 51.242  1.00 41.82  ? 715  ALA   A O    1 
ATOM   1512 C  CB   . ALA   A 1 221 ? -3.926  -17.156 49.035  1.00 40.29  ? 715  ALA   A CB   1 
ATOM   1513 N  N    . GLU   A 1 222 ? -5.698  -15.425 51.063  1.00 38.99  ? 716  GLU   A N    1 
ATOM   1514 C  CA   . GLU   A 1 222 ? -6.138  -15.108 52.421  1.00 42.43  ? 716  GLU   A CA   1 
ATOM   1515 C  C    . GLU   A 1 222 ? -7.656  -15.197 52.550  1.00 41.80  ? 716  GLU   A C    1 
ATOM   1516 O  O    . GLU   A 1 222 ? -8.181  -15.545 53.616  1.00 40.41  ? 716  GLU   A O    1 
ATOM   1517 C  CB   . GLU   A 1 222 ? -5.681  -13.708 52.812  1.00 37.94  ? 716  GLU   A CB   1 
ATOM   1518 C  CG   . GLU   A 1 222 ? -4.199  -13.615 53.171  1.00 43.15  ? 716  GLU   A CG   1 
ATOM   1519 C  CD   . GLU   A 1 222 ? -3.724  -12.174 53.238  1.00 44.37  ? 716  GLU   A CD   1 
ATOM   1520 O  OE1  . GLU   A 1 222 ? -3.261  -11.638 52.210  1.00 51.44  ? 716  GLU   A OE1  1 
ATOM   1521 O  OE2  . GLU   A 1 222 ? -3.770  -11.589 54.340  1.00 54.52  ? 716  GLU   A OE2  1 
ATOM   1522 N  N    . ALA   A 1 223 ? -8.375  -14.817 51.495  1.00 37.46  ? 717  ALA   A N    1 
ATOM   1523 C  CA   . ALA   A 1 223 ? -9.825  -14.906 51.537  1.00 43.93  ? 717  ALA   A CA   1 
ATOM   1524 C  C    . ALA   A 1 223 ? -10.279 -16.359 51.493  1.00 42.27  ? 717  ALA   A C    1 
ATOM   1525 O  O    . ALA   A 1 223 ? -11.188 -16.753 52.230  1.00 42.93  ? 717  ALA   A O    1 
ATOM   1526 C  CB   . ALA   A 1 223 ? -10.427 -14.110 50.377  1.00 39.71  ? 717  ALA   A CB   1 
ATOM   1527 N  N    . ILE   A 1 224 ? -9.655  -17.165 50.630  1.00 43.26  ? 718  ILE   A N    1 
ATOM   1528 C  CA   . ILE   A 1 224 ? -9.990  -18.585 50.539  1.00 40.67  ? 718  ILE   A CA   1 
ATOM   1529 C  C    . ILE   A 1 224 ? -9.754  -19.270 51.877  1.00 45.86  ? 718  ILE   A C    1 
ATOM   1530 O  O    . ILE   A 1 224 ? -10.626 -19.979 52.393  1.00 47.99  ? 718  ILE   A O    1 
ATOM   1531 C  CB   . ILE   A 1 224 ? -9.183  -19.249 49.411  1.00 43.99  ? 718  ILE   A CB   1 
ATOM   1532 C  CG1  . ILE   A 1 224 ? -9.628  -18.682 48.054  1.00 45.15  ? 718  ILE   A CG1  1 
ATOM   1533 C  CG2  . ILE   A 1 224 ? -9.332  -20.765 49.468  1.00 44.69  ? 718  ILE   A CG2  1 
ATOM   1534 C  CD1  . ILE   A 1 224 ? -8.616  -18.879 46.936  1.00 43.84  ? 718  ILE   A CD1  1 
ATOM   1535 N  N    . GLN   A 1 225 ? -8.570  -19.063 52.459  1.00 45.40  ? 719  GLN   A N    1 
ATOM   1536 C  CA   . GLN   A 1 225 ? -8.275  -19.615 53.779  1.00 47.27  ? 719  GLN   A CA   1 
ATOM   1537 C  C    . GLN   A 1 225 ? -9.289  -19.144 54.819  1.00 51.27  ? 719  GLN   A C    1 
ATOM   1538 O  O    . GLN   A 1 225 ? -9.708  -19.920 55.685  1.00 48.00  ? 719  GLN   A O    1 
ATOM   1539 C  CB   . GLN   A 1 225 ? -6.857  -19.225 54.208  1.00 47.15  ? 719  GLN   A CB   1 
ATOM   1540 C  CG   . GLN   A 1 225 ? -6.376  -19.951 55.466  1.00 53.01  ? 719  GLN   A CG   1 
ATOM   1541 C  CD   . GLN   A 1 225 ? -6.310  -21.456 55.269  1.00 56.27  ? 719  GLN   A CD   1 
ATOM   1542 O  OE1  . GLN   A 1 225 ? -5.481  -21.959 54.511  1.00 58.03  ? 719  GLN   A OE1  1 
ATOM   1543 N  NE2  . GLN   A 1 225 ? -7.209  -22.178 55.922  1.00 53.57  ? 719  GLN   A NE2  1 
ATOM   1544 N  N    . ALA   A 1 226 ? -9.685  -17.868 54.758  1.00 47.87  ? 720  ALA   A N    1 
ATOM   1545 C  CA   . ALA   A 1 226 ? -10.670 -17.369 55.709  1.00 47.54  ? 720  ALA   A CA   1 
ATOM   1546 C  C    . ALA   A 1 226 ? -12.009 -18.071 55.537  1.00 48.88  ? 720  ALA   A C    1 
ATOM   1547 O  O    . ALA   A 1 226 ? -12.727 -18.277 56.523  1.00 52.08  ? 720  ALA   A O    1 
ATOM   1548 C  CB   . ALA   A 1 226 ? -10.839 -15.852 55.570  1.00 45.22  ? 720  ALA   A CB   1 
ATOM   1549 N  N    . VAL   A 1 227 ? -12.370 -18.446 54.306  1.00 43.53  ? 721  VAL   A N    1 
ATOM   1550 C  CA   . VAL   A 1 227 ? -13.597 -19.219 54.126  1.00 50.61  ? 721  VAL   A CA   1 
ATOM   1551 C  C    . VAL   A 1 227 ? -13.439 -20.612 54.730  1.00 55.22  ? 721  VAL   A C    1 
ATOM   1552 O  O    . VAL   A 1 227 ? -14.358 -21.135 55.375  1.00 53.60  ? 721  VAL   A O    1 
ATOM   1553 C  CB   . VAL   A 1 227 ? -13.992 -19.285 52.642  1.00 47.35  ? 721  VAL   A CB   1 
ATOM   1554 C  CG1  . VAL   A 1 227 ? -15.162 -20.240 52.453  1.00 43.70  ? 721  VAL   A CG1  1 
ATOM   1555 C  CG2  . VAL   A 1 227 ? -14.355 -17.889 52.129  1.00 42.66  ? 721  VAL   A CG2  1 
ATOM   1556 N  N    . ARG   A 1 228 ? -12.260 -21.214 54.556  1.00 53.42  ? 722  ARG   A N    1 
ATOM   1557 C  CA   . ARG   A 1 228 ? -11.988 -22.543 55.098  1.00 56.45  ? 722  ARG   A CA   1 
ATOM   1558 C  C    . ARG   A 1 228 ? -12.062 -22.550 56.619  1.00 53.11  ? 722  ARG   A C    1 
ATOM   1559 O  O    . ARG   A 1 228 ? -12.496 -23.539 57.219  1.00 58.55  ? 722  ARG   A O    1 
ATOM   1560 C  CB   . ARG   A 1 228 ? -10.602 -23.011 54.642  1.00 53.21  ? 722  ARG   A CB   1 
ATOM   1561 C  CG   . ARG   A 1 228 ? -10.574 -23.600 53.238  1.00 57.68  ? 722  ARG   A CG   1 
ATOM   1562 C  CD   . ARG   A 1 228 ? -10.327 -25.099 53.274  1.00 60.01  ? 722  ARG   A CD   1 
ATOM   1563 N  NE   . ARG   A 1 228 ? -8.928  -25.435 53.464  1.00 60.20  ? 722  ARG   A NE   1 
ATOM   1564 C  CZ   . ARG   A 1 228 ? -8.360  -26.538 53.001  1.00 53.49  ? 722  ARG   A CZ   1 
ATOM   1565 N  NH1  . ARG   A 1 228 ? -9.065  -27.471 52.388  1.00 51.95  ? 722  ARG   A NH1  1 
ATOM   1566 N  NH2  . ARG   A 1 228 ? -7.053  -26.708 53.162  1.00 63.67  ? 722  ARG   A NH2  1 
ATOM   1567 N  N    . ASP   A 1 229 ? -11.644 -21.461 57.255  1.00 50.69  ? 723  ASP   A N    1 
ATOM   1568 C  CA   . ASP   A 1 229 ? -11.611 -21.338 58.704  1.00 56.84  ? 723  ASP   A CA   1 
ATOM   1569 C  C    . ASP   A 1 229 ? -12.889 -20.760 59.282  1.00 60.12  ? 723  ASP   A C    1 
ATOM   1570 O  O    . ASP   A 1 229 ? -12.905 -20.390 60.460  1.00 60.67  ? 723  ASP   A O    1 
ATOM   1571 C  CB   . ASP   A 1 229 ? -10.430 -20.469 59.125  1.00 57.00  ? 723  ASP   A CB   1 
ATOM   1572 C  CG   . ASP   A 1 229 ? -9.112  -21.080 58.746  1.00 59.50  ? 723  ASP   A CG   1 
ATOM   1573 O  OD1  . ASP   A 1 229 ? -8.130  -20.319 58.588  1.00 55.19  ? 723  ASP   A OD1  1 
ATOM   1574 O  OD2  . ASP   A 1 229 ? -9.079  -22.321 58.577  1.00 57.95  ? 723  ASP   A OD2  1 
ATOM   1575 N  N    . ASN   A 1 230 ? -13.939 -20.650 58.473  1.00 60.17  ? 724  ASN   A N    1 
ATOM   1576 C  CA   . ASN   A 1 230 ? -15.236 -20.124 58.889  1.00 63.62  ? 724  ASN   A CA   1 
ATOM   1577 C  C    . ASN   A 1 230 ? -15.147 -18.700 59.443  1.00 64.45  ? 724  ASN   A C    1 
ATOM   1578 O  O    . ASN   A 1 230 ? -15.964 -18.299 60.275  1.00 70.39  ? 724  ASN   A O    1 
ATOM   1579 C  CB   . ASN   A 1 230 ? -15.910 -21.054 59.901  1.00 70.84  ? 724  ASN   A CB   1 
ATOM   1580 C  CG   . ASN   A 1 230 ? -17.411 -21.120 59.705  1.00 82.26  ? 724  ASN   A CG   1 
ATOM   1581 O  OD1  . ASN   A 1 230 ? -18.185 -20.606 60.517  1.00 93.32  ? 724  ASN   A OD1  1 
ATOM   1582 N  ND2  . ASN   A 1 230 ? -17.832 -21.737 58.603  1.00 76.68  ? 724  ASN   A ND2  1 
ATOM   1583 N  N    . LYS   A 1 231 ? -14.167 -17.916 58.983  1.00 59.04  ? 725  LYS   A N    1 
ATOM   1584 C  CA   . LYS   A 1 231 ? -14.093 -16.498 59.322  1.00 53.05  ? 725  LYS   A CA   1 
ATOM   1585 C  C    . LYS   A 1 231 ? -14.653 -15.596 58.226  1.00 54.60  ? 725  LYS   A C    1 
ATOM   1586 O  O    . LYS   A 1 231 ? -14.988 -14.437 58.502  1.00 50.89  ? 725  LYS   A O    1 
ATOM   1587 C  CB   . LYS   A 1 231 ? -12.642 -16.095 59.629  1.00 54.63  ? 725  LYS   A CB   1 
ATOM   1588 N  N    . LEU   A 1 232 ? -14.750 -16.095 56.997  1.00 52.54  ? 726  LEU   A N    1 
ATOM   1589 C  CA   . LEU   A 1 232 ? -15.450 -15.438 55.903  1.00 47.19  ? 726  LEU   A CA   1 
ATOM   1590 C  C    . LEU   A 1 232 ? -16.495 -16.401 55.372  1.00 46.95  ? 726  LEU   A C    1 
ATOM   1591 O  O    . LEU   A 1 232 ? -16.187 -17.566 55.111  1.00 51.91  ? 726  LEU   A O    1 
ATOM   1592 C  CB   . LEU   A 1 232 ? -14.484 -15.038 54.783  1.00 48.66  ? 726  LEU   A CB   1 
ATOM   1593 C  CG   . LEU   A 1 232 ? -15.097 -14.444 53.514  1.00 44.39  ? 726  LEU   A CG   1 
ATOM   1594 C  CD1  . LEU   A 1 232 ? -15.852 -13.156 53.814  1.00 44.11  ? 726  LEU   A CD1  1 
ATOM   1595 C  CD2  . LEU   A 1 232 ? -13.989 -14.201 52.516  1.00 41.07  ? 726  LEU   A CD2  1 
ATOM   1596 N  N    . HIS   A 1 233 ? -17.719 -15.924 55.194  1.00 46.48  ? 727  HIS   A N    1 
ATOM   1597 C  CA   . HIS   A 1 233 ? -18.771 -16.855 54.822  1.00 41.62  ? 727  HIS   A CA   1 
ATOM   1598 C  C    . HIS   A 1 233 ? -18.946 -17.006 53.318  1.00 45.76  ? 727  HIS   A C    1 
ATOM   1599 O  O    . HIS   A 1 233 ? -19.339 -18.087 52.860  1.00 45.97  ? 727  HIS   A O    1 
ATOM   1600 C  CB   . HIS   A 1 233 ? -20.079 -16.437 55.492  1.00 46.70  ? 727  HIS   A CB   1 
ATOM   1601 C  CG   . HIS   A 1 233 ? -19.947 -16.276 56.972  1.00 49.50  ? 727  HIS   A CG   1 
ATOM   1602 N  ND1  . HIS   A 1 233 ? -19.506 -17.298 57.786  1.00 57.45  ? 727  HIS   A ND1  1 
ATOM   1603 C  CD2  . HIS   A 1 233 ? -20.205 -15.229 57.789  1.00 48.24  ? 727  HIS   A CD2  1 
ATOM   1604 C  CE1  . HIS   A 1 233 ? -19.480 -16.882 59.040  1.00 54.99  ? 727  HIS   A CE1  1 
ATOM   1605 N  NE2  . HIS   A 1 233 ? -19.909 -15.632 59.070  1.00 55.43  ? 727  HIS   A NE2  1 
ATOM   1606 N  N    . ALA   A 1 234 ? -18.657 -15.967 52.534  1.00 43.08  ? 728  ALA   A N    1 
ATOM   1607 C  CA   . ALA   A 1 234 ? -18.721 -16.072 51.084  1.00 41.08  ? 728  ALA   A CA   1 
ATOM   1608 C  C    . ALA   A 1 234 ? -17.654 -15.180 50.467  1.00 40.39  ? 728  ALA   A C    1 
ATOM   1609 O  O    . ALA   A 1 234 ? -17.454 -14.043 50.907  1.00 38.17  ? 728  ALA   A O    1 
ATOM   1610 C  CB   . ALA   A 1 234 ? -20.108 -15.693 50.557  1.00 39.56  ? 728  ALA   A CB   1 
ATOM   1611 N  N    . PHE   A 1 235 ? -16.957 -15.719 49.468  1.00 36.63  ? 729  PHE   A N    1 
ATOM   1612 C  CA   . PHE   A 1 235 ? -15.884 -15.035 48.756  1.00 36.18  ? 729  PHE   A CA   1 
ATOM   1613 C  C    . PHE   A 1 235 ? -16.299 -14.892 47.302  1.00 37.04  ? 729  PHE   A C    1 
ATOM   1614 O  O    . PHE   A 1 235 ? -16.482 -15.896 46.601  1.00 37.71  ? 729  PHE   A O    1 
ATOM   1615 C  CB   . PHE   A 1 235 ? -14.576 -15.817 48.891  1.00 39.76  ? 729  PHE   A CB   1 
ATOM   1616 C  CG   . PHE   A 1 235 ? -13.420 -15.222 48.143  1.00 36.91  ? 729  PHE   A CG   1 
ATOM   1617 C  CD1  . PHE   A 1 235 ? -13.222 -13.853 48.114  1.00 36.44  ? 729  PHE   A CD1  1 
ATOM   1618 C  CD2  . PHE   A 1 235 ? -12.497 -16.046 47.504  1.00 36.76  ? 729  PHE   A CD2  1 
ATOM   1619 C  CE1  . PHE   A 1 235 ? -12.137 -13.305 47.439  1.00 38.70  ? 729  PHE   A CE1  1 
ATOM   1620 C  CE2  . PHE   A 1 235 ? -11.419 -15.509 46.812  1.00 36.13  ? 729  PHE   A CE2  1 
ATOM   1621 C  CZ   . PHE   A 1 235 ? -11.237 -14.136 46.783  1.00 38.28  ? 729  PHE   A CZ   1 
ATOM   1622 N  N    . ILE   A 1 236 ? -16.453 -13.657 46.843  1.00 34.23  ? 730  ILE   A N    1 
ATOM   1623 C  CA   . ILE   A 1 236 ? -16.865 -13.402 45.465  1.00 35.10  ? 730  ILE   A CA   1 
ATOM   1624 C  C    . ILE   A 1 236 ? -15.602 -13.174 44.636  1.00 34.71  ? 730  ILE   A C    1 
ATOM   1625 O  O    . ILE   A 1 236 ? -14.820 -12.260 44.928  1.00 34.98  ? 730  ILE   A O    1 
ATOM   1626 C  CB   . ILE   A 1 236 ? -17.824 -12.203 45.389  1.00 33.13  ? 730  ILE   A CB   1 
ATOM   1627 C  CG1  . ILE   A 1 236 ? -18.987 -12.408 46.360  1.00 36.64  ? 730  ILE   A CG1  1 
ATOM   1628 C  CG2  . ILE   A 1 236 ? -18.365 -11.999 43.969  1.00 32.43  ? 730  ILE   A CG2  1 
ATOM   1629 C  CD1  . ILE   A 1 236 ? -20.000 -11.284 46.363  1.00 37.41  ? 730  ILE   A CD1  1 
ATOM   1630 N  N    . TRP   A 1 237 ? -15.383 -14.004 43.612  1.00 33.22  ? 731  TRP   A N    1 
ATOM   1631 C  CA   . TRP   A 1 237 ? -14.103 -13.954 42.910  1.00 35.66  ? 731  TRP   A CA   1 
ATOM   1632 C  C    . TRP   A 1 237 ? -14.215 -14.629 41.548  1.00 35.04  ? 731  TRP   A C    1 
ATOM   1633 O  O    . TRP   A 1 237 ? -15.286 -15.100 41.149  1.00 36.82  ? 731  TRP   A O    1 
ATOM   1634 C  CB   . TRP   A 1 237 ? -13.011 -14.586 43.784  1.00 32.41  ? 731  TRP   A CB   1 
ATOM   1635 C  CG   . TRP   A 1 237 ? -11.593 -14.313 43.362  1.00 34.45  ? 731  TRP   A CG   1 
ATOM   1636 C  CD1  . TRP   A 1 237 ? -10.631 -15.247 43.095  1.00 32.40  ? 731  TRP   A CD1  1 
ATOM   1637 C  CD2  . TRP   A 1 237 ? -10.968 -13.029 43.181  1.00 36.03  ? 731  TRP   A CD2  1 
ATOM   1638 N  NE1  . TRP   A 1 237 ? -9.452  -14.629 42.735  1.00 34.56  ? 731  TRP   A NE1  1 
ATOM   1639 C  CE2  . TRP   A 1 237 ? -9.629  -13.269 42.792  1.00 35.70  ? 731  TRP   A CE2  1 
ATOM   1640 C  CE3  . TRP   A 1 237 ? -11.412 -11.700 43.303  1.00 34.82  ? 731  TRP   A CE3  1 
ATOM   1641 C  CZ2  . TRP   A 1 237 ? -8.733  -12.237 42.518  1.00 33.68  ? 731  TRP   A CZ2  1 
ATOM   1642 C  CZ3  . TRP   A 1 237 ? -10.517 -10.670 43.036  1.00 35.01  ? 731  TRP   A CZ3  1 
ATOM   1643 C  CH2  . TRP   A 1 237 ? -9.185  -10.947 42.652  1.00 29.57  ? 731  TRP   A CH2  1 
ATOM   1644 N  N    . ASP   A 1 238 ? -13.078 -14.658 40.833  1.00 32.11  ? 732  ASP   A N    1 
ATOM   1645 C  CA   . ASP   A 1 238 ? -12.967 -15.248 39.501  1.00 30.03  ? 732  ASP   A CA   1 
ATOM   1646 C  C    . ASP   A 1 238 ? -13.264 -16.742 39.521  1.00 33.19  ? 732  ASP   A C    1 
ATOM   1647 O  O    . ASP   A 1 238 ? -12.653 -17.504 40.282  1.00 31.15  ? 732  ASP   A O    1 
ATOM   1648 C  CB   . ASP   A 1 238 ? -11.550 -15.028 38.940  1.00 31.92  ? 732  ASP   A CB   1 
ATOM   1649 C  CG   . ASP   A 1 238 ? -11.262 -13.571 38.605  1.00 34.66  ? 732  ASP   A CG   1 
ATOM   1650 O  OD1  . ASP   A 1 238 ? -12.131 -12.917 37.985  1.00 36.30  ? 732  ASP   A OD1  1 
ATOM   1651 O  OD2  . ASP   A 1 238 ? -10.164 -13.073 38.960  1.00 34.88  ? 732  ASP   A OD2  1 
ATOM   1652 N  N    . SER   A 1 239 ? -14.165 -17.176 38.631  1.00 34.83  ? 733  SER   A N    1 
ATOM   1653 C  CA   . SER   A 1 239 ? -14.586 -18.572 38.629  1.00 31.89  ? 733  SER   A CA   1 
ATOM   1654 C  C    . SER   A 1 239 ? -13.450 -19.519 38.252  1.00 31.87  ? 733  SER   A C    1 
ATOM   1655 O  O    . SER   A 1 239 ? -13.398 -20.645 38.761  1.00 33.42  ? 733  SER   A O    1 
ATOM   1656 C  CB   . SER   A 1 239 ? -15.771 -18.761 37.675  1.00 37.50  ? 733  SER   A CB   1 
ATOM   1657 O  OG   . SER   A 1 239 ? -15.424 -18.408 36.335  1.00 33.45  ? 733  SER   A OG   1 
ATOM   1658 N  N    . ALA   A 1 240 ? -12.553 -19.107 37.348  1.00 33.18  ? 734  ALA   A N    1 
ATOM   1659 C  CA   . ALA   A 1 240 ? -11.427 -19.973 36.996  1.00 36.56  ? 734  ALA   A CA   1 
ATOM   1660 C  C    . ALA   A 1 240 ? -10.581 -20.312 38.212  1.00 36.19  ? 734  ALA   A C    1 
ATOM   1661 O  O    . ALA   A 1 240 ? -10.018 -21.412 38.288  1.00 34.18  ? 734  ALA   A O    1 
ATOM   1662 C  CB   . ALA   A 1 240 ? -10.560 -19.325 35.918  1.00 34.01  ? 734  ALA   A CB   1 
ATOM   1663 N  N    . VAL   A 1 241 ? -10.486 -19.390 39.171  1.00 31.83  ? 735  VAL   A N    1 
ATOM   1664 C  CA   . VAL   A 1 241 ? -9.761  -19.659 40.413  1.00 32.82  ? 735  VAL   A CA   1 
ATOM   1665 C  C    . VAL   A 1 241 ? -10.632 -20.442 41.396  1.00 37.35  ? 735  VAL   A C    1 
ATOM   1666 O  O    . VAL   A 1 241 ? -10.225 -21.495 41.904  1.00 35.93  ? 735  VAL   A O    1 
ATOM   1667 C  CB   . VAL   A 1 241 ? -9.268  -18.339 41.042  1.00 36.56  ? 735  VAL   A CB   1 
ATOM   1668 C  CG1  . VAL   A 1 241 ? -8.644  -18.601 42.432  1.00 33.79  ? 735  VAL   A CG1  1 
ATOM   1669 C  CG2  . VAL   A 1 241 ? -8.275  -17.624 40.123  1.00 34.83  ? 735  VAL   A CG2  1 
ATOM   1670 N  N    . LEU   A 1 242 ? -11.838 -19.933 41.685  1.00 34.40  ? 736  LEU   A N    1 
ATOM   1671 C  CA   . LEU   A 1 242 ? -12.705 -20.554 42.692  1.00 34.56  ? 736  LEU   A CA   1 
ATOM   1672 C  C    . LEU   A 1 242 ? -13.025 -22.002 42.348  1.00 36.55  ? 736  LEU   A C    1 
ATOM   1673 O  O    . LEU   A 1 242 ? -12.991 -22.882 43.218  1.00 35.88  ? 736  LEU   A O    1 
ATOM   1674 C  CB   . LEU   A 1 242 ? -14.008 -19.754 42.846  1.00 32.29  ? 736  LEU   A CB   1 
ATOM   1675 C  CG   . LEU   A 1 242 ? -13.859 -18.346 43.432  1.00 33.05  ? 736  LEU   A CG   1 
ATOM   1676 C  CD1  . LEU   A 1 242 ? -15.192 -17.583 43.690  1.00 34.52  ? 736  LEU   A CD1  1 
ATOM   1677 C  CD2  . LEU   A 1 242 ? -13.039 -18.442 44.696  1.00 38.64  ? 736  LEU   A CD2  1 
ATOM   1678 N  N    . GLU   A 1 243 ? -13.353 -22.267 41.085  1.00 34.99  ? 737  GLU   A N    1 
ATOM   1679 C  CA   . GLU   A 1 243 ? -13.681 -23.632 40.687  1.00 38.29  ? 737  GLU   A CA   1 
ATOM   1680 C  C    . GLU   A 1 243 ? -12.471 -24.549 40.820  1.00 43.62  ? 737  GLU   A C    1 
ATOM   1681 O  O    . GLU   A 1 243 ? -12.617 -25.728 41.161  1.00 42.79  ? 737  GLU   A O    1 
ATOM   1682 C  CB   . GLU   A 1 243 ? -14.218 -23.622 39.257  1.00 37.85  ? 737  GLU   A CB   1 
ATOM   1683 C  CG   . GLU   A 1 243 ? -15.706 -23.259 39.174  1.00 41.61  ? 737  GLU   A CG   1 
ATOM   1684 C  CD   . GLU   A 1 243 ? -16.132 -22.930 37.768  1.00 46.73  ? 737  GLU   A CD   1 
ATOM   1685 O  OE1  . GLU   A 1 243 ? -17.213 -22.324 37.593  1.00 52.30  ? 737  GLU   A OE1  1 
ATOM   1686 O  OE2  . GLU   A 1 243 ? -15.366 -23.238 36.830  1.00 50.19  ? 737  GLU   A OE2  1 
ATOM   1687 N  N    . PHE   A 1 244 ? -11.266 -24.028 40.579  1.00 40.81  ? 738  PHE   A N    1 
ATOM   1688 C  CA   . PHE   A 1 244 ? -10.079 -24.845 40.800  1.00 39.98  ? 738  PHE   A CA   1 
ATOM   1689 C  C    . PHE   A 1 244 ? -9.888  -25.127 42.284  1.00 42.82  ? 738  PHE   A C    1 
ATOM   1690 O  O    . PHE   A 1 244 ? -9.607  -26.267 42.677  1.00 39.10  ? 738  PHE   A O    1 
ATOM   1691 C  CB   . PHE   A 1 244 ? -8.840  -24.158 40.221  1.00 42.40  ? 738  PHE   A CB   1 
ATOM   1692 C  CG   . PHE   A 1 244 ? -7.570  -24.849 40.574  1.00 42.94  ? 738  PHE   A CG   1 
ATOM   1693 C  CD1  . PHE   A 1 244 ? -7.165  -25.973 39.863  1.00 45.86  ? 738  PHE   A CD1  1 
ATOM   1694 C  CD2  . PHE   A 1 244 ? -6.808  -24.425 41.644  1.00 40.02  ? 738  PHE   A CD2  1 
ATOM   1695 C  CE1  . PHE   A 1 244 ? -5.995  -26.626 40.202  1.00 48.27  ? 738  PHE   A CE1  1 
ATOM   1696 C  CE2  . PHE   A 1 244 ? -5.648  -25.080 41.987  1.00 43.08  ? 738  PHE   A CE2  1 
ATOM   1697 C  CZ   . PHE   A 1 244 ? -5.241  -26.173 41.270  1.00 43.94  ? 738  PHE   A CZ   1 
ATOM   1698 N  N    . GLU   A 1 245 ? -10.052 -24.104 43.129  1.00 38.95  ? 739  GLU   A N    1 
ATOM   1699 C  CA   . GLU   A 1 245 ? -9.954  -24.326 44.568  1.00 39.81  ? 739  GLU   A CA   1 
ATOM   1700 C  C    . GLU   A 1 245 ? -10.952 -25.389 45.033  1.00 45.77  ? 739  GLU   A C    1 
ATOM   1701 O  O    . GLU   A 1 245 ? -10.599 -26.290 45.811  1.00 46.21  ? 739  GLU   A O    1 
ATOM   1702 C  CB   . GLU   A 1 245 ? -10.169 -23.002 45.308  1.00 40.00  ? 739  GLU   A CB   1 
ATOM   1703 C  CG   . GLU   A 1 245 ? -9.022  -22.014 45.125  1.00 39.26  ? 739  GLU   A CG   1 
ATOM   1704 C  CD   . GLU   A 1 245 ? -7.775  -22.443 45.884  1.00 48.04  ? 739  GLU   A CD   1 
ATOM   1705 O  OE1  . GLU   A 1 245 ? -7.870  -23.387 46.703  1.00 50.26  ? 739  GLU   A OE1  1 
ATOM   1706 O  OE2  . GLU   A 1 245 ? -6.698  -21.845 45.667  1.00 43.00  ? 739  GLU   A OE2  1 
ATOM   1707 N  N    . ALA   A 1 246 ? -12.192 -25.329 44.537  1.00 41.39  ? 740  ALA   A N    1 
ATOM   1708 C  CA   . ALA   A 1 246 ? -13.201 -26.299 44.960  1.00 44.72  ? 740  ALA   A CA   1 
ATOM   1709 C  C    . ALA   A 1 246 ? -12.886 -27.704 44.457  1.00 47.92  ? 740  ALA   A C    1 
ATOM   1710 O  O    . ALA   A 1 246 ? -13.215 -28.689 45.129  1.00 50.96  ? 740  ALA   A O    1 
ATOM   1711 C  CB   . ALA   A 1 246 ? -14.587 -25.866 44.487  1.00 46.28  ? 740  ALA   A CB   1 
ATOM   1712 N  N    . SER   A 1 247 ? -12.251 -27.813 43.287  1.00 47.28  ? 741  SER   A N    1 
ATOM   1713 C  CA   . SER   A 1 247 ? -11.878 -29.117 42.749  1.00 46.36  ? 741  SER   A CA   1 
ATOM   1714 C  C    . SER   A 1 247 ? -10.772 -29.771 43.564  1.00 50.90  ? 741  SER   A C    1 
ATOM   1715 O  O    . SER   A 1 247 ? -10.655 -31.005 43.571  1.00 52.03  ? 741  SER   A O    1 
ATOM   1716 C  CB   . SER   A 1 247 ? -11.463 -28.970 41.284  1.00 43.74  ? 741  SER   A CB   1 
ATOM   1717 O  OG   . SER   A 1 247 ? -10.165 -28.395 41.170  1.00 47.74  ? 741  SER   A OG   1 
ATOM   1718 N  N    . GLN   A 1 248 ? -9.975  -28.973 44.273  1.00 48.33  ? 742  GLN   A N    1 
ATOM   1719 C  CA   . GLN   A 1 248 ? -8.866  -29.482 45.067  1.00 51.75  ? 742  GLN   A CA   1 
ATOM   1720 C  C    . GLN   A 1 248 ? -9.231  -29.643 46.542  1.00 54.39  ? 742  GLN   A C    1 
ATOM   1721 O  O    . GLN   A 1 248 ? -8.787  -30.597 47.188  1.00 50.16  ? 742  GLN   A O    1 
ATOM   1722 C  CB   . GLN   A 1 248 ? -7.659  -28.549 44.913  1.00 55.50  ? 742  GLN   A CB   1 
ATOM   1723 C  CG   . GLN   A 1 248 ? -6.346  -29.091 45.453  1.00 65.98  ? 742  GLN   A CG   1 
ATOM   1724 C  CD   . GLN   A 1 248 ? -5.470  -27.982 46.013  1.00 67.96  ? 742  GLN   A CD   1 
ATOM   1725 O  OE1  . GLN   A 1 248 ? -4.984  -28.067 47.147  1.00 66.48  ? 742  GLN   A OE1  1 
ATOM   1726 N  NE2  . GLN   A 1 248 ? -5.294  -26.917 45.233  1.00 62.35  ? 742  GLN   A NE2  1 
ATOM   1727 N  N    . LYS   A 1 249 ? -10.044 -28.740 47.090  1.00 51.79  ? 743  LYS   A N    1 
ATOM   1728 C  CA   . LYS   A 1 249 ? -10.382 -28.727 48.511  1.00 52.08  ? 743  LYS   A CA   1 
ATOM   1729 C  C    . LYS   A 1 249 ? -11.859 -29.083 48.673  1.00 55.04  ? 743  LYS   A C    1 
ATOM   1730 O  O    . LYS   A 1 249 ? -12.739 -28.295 48.315  1.00 51.77  ? 743  LYS   A O    1 
ATOM   1731 C  CB   . LYS   A 1 249 ? -10.059 -27.364 49.117  1.00 51.67  ? 743  LYS   A CB   1 
ATOM   1732 C  CG   . LYS   A 1 249 ? -8.568  -27.059 49.108  1.00 55.07  ? 743  LYS   A CG   1 
ATOM   1733 C  CD   . LYS   A 1 249 ? -8.260  -25.568 49.181  1.00 52.84  ? 743  LYS   A CD   1 
ATOM   1734 C  CE   . LYS   A 1 249 ? -6.770  -25.331 48.991  1.00 51.67  ? 743  LYS   A CE   1 
ATOM   1735 N  NZ   . LYS   A 1 249 ? -6.421  -23.891 48.874  1.00 47.39  ? 743  LYS   A NZ   1 
ATOM   1736 N  N    . CYS   A 1 250 ? -12.130 -30.262 49.222  1.00 51.64  ? 744  CYS   A N    1 
ATOM   1737 C  CA   . CYS   A 1 250 ? -13.485 -30.794 49.179  1.00 56.54  ? 744  CYS   A CA   1 
ATOM   1738 C  C    . CYS   A 1 250 ? -14.429 -30.154 50.192  1.00 53.23  ? 744  CYS   A C    1 
ATOM   1739 O  O    . CYS   A 1 250 ? -15.641 -30.399 50.116  1.00 59.85  ? 744  CYS   A O    1 
ATOM   1740 C  CB   . CYS   A 1 250 ? -13.446 -32.313 49.364  1.00 61.31  ? 744  CYS   A CB   1 
ATOM   1741 S  SG   . CYS   A 1 250 ? -12.633 -33.167 47.983  1.00 66.42  ? 744  CYS   A SG   1 
ATOM   1742 N  N    . ASP   A 1 251 ? -13.924 -29.339 51.117  1.00 47.25  ? 745  ASP   A N    1 
ATOM   1743 C  CA   . ASP   A 1 251 ? -14.777 -28.581 52.023  1.00 50.81  ? 745  ASP   A CA   1 
ATOM   1744 C  C    . ASP   A 1 251 ? -15.144 -27.200 51.480  1.00 51.04  ? 745  ASP   A C    1 
ATOM   1745 O  O    . ASP   A 1 251 ? -15.775 -26.412 52.193  1.00 45.94  ? 745  ASP   A O    1 
ATOM   1746 C  CB   . ASP   A 1 251 ? -14.103 -28.433 53.381  1.00 51.16  ? 745  ASP   A CB   1 
ATOM   1747 C  CG   . ASP   A 1 251 ? -12.799 -27.674 53.301  1.00 57.52  ? 745  ASP   A CG   1 
ATOM   1748 O  OD1  . ASP   A 1 251 ? -11.996 -27.944 52.376  1.00 57.67  ? 745  ASP   A OD1  1 
ATOM   1749 O  OD2  . ASP   A 1 251 ? -12.587 -26.802 54.171  1.00 56.37  ? 745  ASP   A OD2  1 
ATOM   1750 N  N    . LEU   A 1 252 ? -14.767 -26.897 50.243  1.00 47.27  ? 746  LEU   A N    1 
ATOM   1751 C  CA   . LEU   A 1 252 ? -15.122 -25.653 49.576  1.00 49.83  ? 746  LEU   A CA   1 
ATOM   1752 C  C    . LEU   A 1 252 ? -16.005 -25.949 48.374  1.00 48.79  ? 746  LEU   A C    1 
ATOM   1753 O  O    . LEU   A 1 252 ? -15.801 -26.949 47.680  1.00 49.72  ? 746  LEU   A O    1 
ATOM   1754 C  CB   . LEU   A 1 252 ? -13.872 -24.890 49.126  1.00 43.36  ? 746  LEU   A CB   1 
ATOM   1755 C  CG   . LEU   A 1 252 ? -12.995 -24.402 50.272  1.00 48.07  ? 746  LEU   A CG   1 
ATOM   1756 C  CD1  . LEU   A 1 252 ? -11.715 -23.768 49.736  1.00 48.34  ? 746  LEU   A CD1  1 
ATOM   1757 C  CD2  . LEU   A 1 252 ? -13.761 -23.419 51.121  1.00 47.12  ? 746  LEU   A CD2  1 
ATOM   1758 N  N    . VAL   A 1 253 ? -16.977 -25.068 48.122  1.00 45.47  ? 747  VAL   A N    1 
ATOM   1759 C  CA   . VAL   A 1 253 ? -17.902 -25.227 47.007  1.00 43.90  ? 747  VAL   A CA   1 
ATOM   1760 C  C    . VAL   A 1 253 ? -18.236 -23.857 46.417  1.00 44.10  ? 747  VAL   A C    1 
ATOM   1761 O  O    . VAL   A 1 253 ? -18.231 -22.836 47.113  1.00 42.03  ? 747  VAL   A O    1 
ATOM   1762 C  CB   . VAL   A 1 253 ? -19.177 -25.987 47.457  1.00 49.05  ? 747  VAL   A CB   1 
ATOM   1763 C  CG1  . VAL   A 1 253 ? -20.217 -25.042 48.053  1.00 45.20  ? 747  VAL   A CG1  1 
ATOM   1764 C  CG2  . VAL   A 1 253 ? -19.764 -26.773 46.314  1.00 51.67  ? 747  VAL   A CG2  1 
ATOM   1765 N  N    . THR   A 1 254 ? -18.471 -23.832 45.112  1.00 42.42  ? 748  THR   A N    1 
ATOM   1766 C  CA   . THR   A 1 254 ? -18.997 -22.641 44.466  1.00 45.24  ? 748  THR   A CA   1 
ATOM   1767 C  C    . THR   A 1 254 ? -20.515 -22.696 44.448  1.00 50.23  ? 748  THR   A C    1 
ATOM   1768 O  O    . THR   A 1 254 ? -21.126 -23.761 44.532  1.00 45.78  ? 748  THR   A O    1 
ATOM   1769 C  CB   . THR   A 1 254 ? -18.486 -22.490 43.034  1.00 46.11  ? 748  THR   A CB   1 
ATOM   1770 O  OG1  . THR   A 1 254 ? -19.089 -23.490 42.213  1.00 49.57  ? 748  THR   A OG1  1 
ATOM   1771 C  CG2  . THR   A 1 254 ? -16.958 -22.631 42.969  1.00 42.39  ? 748  THR   A CG2  1 
ATOM   1772 N  N    . THR   A 1 255 ? -21.119 -21.531 44.302  1.00 47.31  ? 749  THR   A N    1 
ATOM   1773 C  CA   . THR   A 1 255 ? -22.562 -21.413 44.381  1.00 54.95  ? 749  THR   A CA   1 
ATOM   1774 C  C    . THR   A 1 255 ? -23.244 -21.756 43.067  1.00 59.13  ? 749  THR   A C    1 
ATOM   1775 O  O    . THR   A 1 255 ? -24.449 -21.532 42.924  1.00 68.89  ? 749  THR   A O    1 
ATOM   1776 C  CB   . THR   A 1 255 ? -22.928 -19.999 44.818  1.00 55.35  ? 749  THR   A CB   1 
ATOM   1777 O  OG1  . THR   A 1 255 ? -24.318 -19.948 45.151  1.00 68.63  ? 749  THR   A OG1  1 
ATOM   1778 C  CG2  . THR   A 1 255 ? -22.638 -19.042 43.687  1.00 49.12  ? 749  THR   A CG2  1 
ATOM   1779 N  N    . GLY   A 1 256 ? -22.506 -22.296 42.106  1.00 66.77  ? 750  GLY   A N    1 
ATOM   1780 C  CA   . GLY   A 1 256 ? -23.120 -22.699 40.862  1.00 73.43  ? 750  GLY   A CA   1 
ATOM   1781 C  C    . GLY   A 1 256 ? -22.492 -22.037 39.659  1.00 65.58  ? 750  GLY   A C    1 
ATOM   1782 O  O    . GLY   A 1 256 ? -21.352 -22.340 39.301  1.00 73.39  ? 750  GLY   A O    1 
ATOM   1783 N  N    . GLU   A 1 257 ? -23.209 -21.121 39.037  1.00 60.19  ? 751  GLU   A N    1 
ATOM   1784 C  CA   . GLU   A 1 257 ? -22.766 -20.614 37.757  1.00 55.06  ? 751  GLU   A CA   1 
ATOM   1785 C  C    . GLU   A 1 257 ? -22.229 -19.191 37.909  1.00 50.31  ? 751  GLU   A C    1 
ATOM   1786 O  O    . GLU   A 1 257 ? -21.934 -18.726 39.020  1.00 46.39  ? 751  GLU   A O    1 
ATOM   1787 C  CB   . GLU   A 1 257 ? -23.918 -20.705 36.747  1.00 57.49  ? 751  GLU   A CB   1 
ATOM   1788 N  N    . LEU   A 1 258 ? -22.085 -18.500 36.789  1.00 47.58  ? 752  LEU   A N    1 
ATOM   1789 C  CA   . LEU   A 1 258 ? -21.535 -17.158 36.762  1.00 42.91  ? 752  LEU   A CA   1 
ATOM   1790 C  C    . LEU   A 1 258 ? -22.669 -16.158 36.710  1.00 43.33  ? 752  LEU   A C    1 
ATOM   1791 O  O    . LEU   A 1 258 ? -23.596 -16.311 35.909  1.00 44.77  ? 752  LEU   A O    1 
ATOM   1792 C  CB   . LEU   A 1 258 ? -20.622 -16.963 35.554  1.00 44.04  ? 752  LEU   A CB   1 
ATOM   1793 C  CG   . LEU   A 1 258 ? -19.780 -18.153 35.122  1.00 44.10  ? 752  LEU   A CG   1 
ATOM   1794 C  CD1  . LEU   A 1 258 ? -18.942 -17.772 33.902  1.00 40.96  ? 752  LEU   A CD1  1 
ATOM   1795 C  CD2  . LEU   A 1 258 ? -18.902 -18.581 36.271  1.00 38.22  ? 752  LEU   A CD2  1 
ATOM   1796 N  N    . PHE   A 1 259 ? -22.598 -15.144 37.564  1.00 39.78  ? 753  PHE   A N    1 
ATOM   1797 C  CA   . PHE   A 1 259 ? -23.524 -14.032 37.481  1.00 41.91  ? 753  PHE   A CA   1 
ATOM   1798 C  C    . PHE   A 1 259 ? -23.001 -12.907 36.601  1.00 41.88  ? 753  PHE   A C    1 
ATOM   1799 O  O    . PHE   A 1 259 ? -23.732 -11.941 36.366  1.00 42.66  ? 753  PHE   A O    1 
ATOM   1800 C  CB   . PHE   A 1 259 ? -23.867 -13.516 38.887  1.00 42.02  ? 753  PHE   A CB   1 
ATOM   1801 C  CG   . PHE   A 1 259 ? -22.677 -13.004 39.686  1.00 41.37  ? 753  PHE   A CG   1 
ATOM   1802 C  CD1  . PHE   A 1 259 ? -22.267 -11.674 39.588  1.00 41.01  ? 753  PHE   A CD1  1 
ATOM   1803 C  CD2  . PHE   A 1 259 ? -22.024 -13.831 40.582  1.00 36.73  ? 753  PHE   A CD2  1 
ATOM   1804 C  CE1  . PHE   A 1 259 ? -21.211 -11.196 40.339  1.00 42.09  ? 753  PHE   A CE1  1 
ATOM   1805 C  CE2  . PHE   A 1 259 ? -20.968 -13.355 41.352  1.00 37.22  ? 753  PHE   A CE2  1 
ATOM   1806 C  CZ   . PHE   A 1 259 ? -20.552 -12.041 41.222  1.00 37.65  ? 753  PHE   A CZ   1 
ATOM   1807 N  N    . PHE   A 1 260 ? -21.785 -13.043 36.063  1.00 37.96  ? 754  PHE   A N    1 
ATOM   1808 C  CA   . PHE   A 1 260 ? -21.154 -12.008 35.256  1.00 36.09  ? 754  PHE   A CA   1 
ATOM   1809 C  C    . PHE   A 1 260 ? -20.033 -12.655 34.460  1.00 37.73  ? 754  PHE   A C    1 
ATOM   1810 O  O    . PHE   A 1 260 ? -19.218 -13.378 35.031  1.00 37.13  ? 754  PHE   A O    1 
ATOM   1811 C  CB   . PHE   A 1 260 ? -20.607 -10.885 36.152  1.00 39.06  ? 754  PHE   A CB   1 
ATOM   1812 C  CG   . PHE   A 1 260 ? -19.972 -9.747  35.403  1.00 39.54  ? 754  PHE   A CG   1 
ATOM   1813 C  CD1  . PHE   A 1 260 ? -20.742 -8.912  34.613  1.00 41.20  ? 754  PHE   A CD1  1 
ATOM   1814 C  CD2  . PHE   A 1 260 ? -18.609 -9.482  35.533  1.00 39.30  ? 754  PHE   A CD2  1 
ATOM   1815 C  CE1  . PHE   A 1 260 ? -20.167 -7.850  33.936  1.00 43.87  ? 754  PHE   A CE1  1 
ATOM   1816 C  CE2  . PHE   A 1 260 ? -18.019 -8.415  34.862  1.00 36.87  ? 754  PHE   A CE2  1 
ATOM   1817 C  CZ   . PHE   A 1 260 ? -18.799 -7.600  34.058  1.00 39.15  ? 754  PHE   A CZ   1 
ATOM   1818 N  N    . ARG   A 1 261 ? -19.983 -12.403 33.158  1.00 33.02  ? 755  ARG   A N    1 
ATOM   1819 C  CA   . ARG   A 1 261 ? -18.897 -12.947 32.340  1.00 34.79  ? 755  ARG   A CA   1 
ATOM   1820 C  C    . ARG   A 1 261 ? -17.730 -11.973 32.318  1.00 34.60  ? 755  ARG   A C    1 
ATOM   1821 O  O    . ARG   A 1 261 ? -17.928 -10.759 32.188  1.00 35.25  ? 755  ARG   A O    1 
ATOM   1822 C  CB   . ARG   A 1 261 ? -19.362 -13.210 30.905  1.00 32.49  ? 755  ARG   A CB   1 
ATOM   1823 C  CG   . ARG   A 1 261 ? -20.405 -14.325 30.785  1.00 41.68  ? 755  ARG   A CG   1 
ATOM   1824 C  CD   . ARG   A 1 261 ? -20.684 -14.668 29.315  1.00 37.85  ? 755  ARG   A CD   1 
ATOM   1825 N  NE   . ARG   A 1 261 ? -21.782 -15.618 29.177  1.00 44.26  ? 755  ARG   A NE   1 
ATOM   1826 C  CZ   . ARG   A 1 261 ? -23.064 -15.288 29.249  1.00 42.15  ? 755  ARG   A CZ   1 
ATOM   1827 N  NH1  . ARG   A 1 261 ? -23.444 -14.061 29.565  1.00 42.14  ? 755  ARG   A NH1  1 
ATOM   1828 N  NH2  . ARG   A 1 261 ? -23.986 -16.215 29.007  1.00 45.80  ? 755  ARG   A NH2  1 
ATOM   1829 N  N    . SER   A 1 262 ? -16.513 -12.509 32.430  1.00 30.27  ? 756  SER   A N    1 
ATOM   1830 C  CA   . SER   A 1 262 ? -15.319 -11.674 32.313  1.00 35.12  ? 756  SER   A CA   1 
ATOM   1831 C  C    . SER   A 1 262 ? -14.186 -12.514 31.751  1.00 31.48  ? 756  SER   A C    1 
ATOM   1832 O  O    . SER   A 1 262 ? -14.274 -13.744 31.689  1.00 33.45  ? 756  SER   A O    1 
ATOM   1833 C  CB   . SER   A 1 262 ? -14.920 -11.056 33.657  1.00 32.67  ? 756  SER   A CB   1 
ATOM   1834 O  OG   . SER   A 1 262 ? -14.496 -12.069 34.546  1.00 34.96  ? 756  SER   A OG   1 
ATOM   1835 N  N    . GLY   A 1 263 ? -13.124 -11.840 31.326  1.00 33.79  ? 757  GLY   A N    1 
ATOM   1836 C  CA   . GLY   A 1 263 ? -12.018 -12.518 30.676  1.00 27.91  ? 757  GLY   A CA   1 
ATOM   1837 C  C    . GLY   A 1 263 ? -10.693 -11.882 31.041  1.00 33.17  ? 757  GLY   A C    1 
ATOM   1838 O  O    . GLY   A 1 263 ? -10.623 -10.712 31.417  1.00 29.80  ? 757  GLY   A O    1 
ATOM   1839 N  N    . PHE   A 1 264 ? -9.635  -12.672 30.920  1.00 29.71  ? 758  PHE   A N    1 
ATOM   1840 C  CA   . PHE   A 1 264 ? -8.281  -12.224 31.202  1.00 28.17  ? 758  PHE   A CA   1 
ATOM   1841 C  C    . PHE   A 1 264 ? -7.585  -11.916 29.887  1.00 30.48  ? 758  PHE   A C    1 
ATOM   1842 O  O    . PHE   A 1 264 ? -7.741  -12.660 28.910  1.00 31.09  ? 758  PHE   A O    1 
ATOM   1843 C  CB   . PHE   A 1 264 ? -7.492  -13.295 31.955  1.00 31.75  ? 758  PHE   A CB   1 
ATOM   1844 C  CG   . PHE   A 1 264 ? -8.166  -13.798 33.191  1.00 30.84  ? 758  PHE   A CG   1 
ATOM   1845 C  CD1  . PHE   A 1 264 ? -8.941  -12.950 33.983  1.00 30.05  ? 758  PHE   A CD1  1 
ATOM   1846 C  CD2  . PHE   A 1 264 ? -8.016  -15.124 33.572  1.00 30.78  ? 758  PHE   A CD2  1 
ATOM   1847 C  CE1  . PHE   A 1 264 ? -9.561  -13.437 35.134  1.00 28.10  ? 758  PHE   A CE1  1 
ATOM   1848 C  CE2  . PHE   A 1 264 ? -8.624  -15.613 34.719  1.00 27.82  ? 758  PHE   A CE2  1 
ATOM   1849 C  CZ   . PHE   A 1 264 ? -9.395  -14.785 35.495  1.00 27.48  ? 758  PHE   A CZ   1 
ATOM   1850 N  N    . GLY   A 1 265 ? -6.832  -10.810 29.858  1.00 30.34  ? 759  GLY   A N    1 
ATOM   1851 C  CA   . GLY   A 1 265 ? -5.961  -10.524 28.738  1.00 29.97  ? 759  GLY   A CA   1 
ATOM   1852 C  C    . GLY   A 1 265 ? -4.574  -10.125 29.206  1.00 31.56  ? 759  GLY   A C    1 
ATOM   1853 O  O    . GLY   A 1 265 ? -4.377  -9.715  30.345  1.00 30.55  ? 759  GLY   A O    1 
ATOM   1854 N  N    . ILE   A 1 266 ? -3.605  -10.280 28.294  1.00 32.69  ? 760  ILE   A N    1 
ATOM   1855 C  CA   . ILE   A 1 266 ? -2.256  -9.749  28.475  1.00 28.81  ? 760  ILE   A CA   1 
ATOM   1856 C  C    . ILE   A 1 266 ? -2.311  -8.223  28.406  1.00 33.25  ? 760  ILE   A C    1 
ATOM   1857 O  O    . ILE   A 1 266 ? -2.988  -7.657  27.542  1.00 33.69  ? 760  ILE   A O    1 
ATOM   1858 C  CB   . ILE   A 1 266 ? -1.319  -10.304 27.382  1.00 32.57  ? 760  ILE   A CB   1 
ATOM   1859 C  CG1  . ILE   A 1 266 ? -1.297  -11.832 27.339  1.00 31.88  ? 760  ILE   A CG1  1 
ATOM   1860 C  CG2  . ILE   A 1 266 ? 0.102   -9.772  27.564  1.00 31.17  ? 760  ILE   A CG2  1 
ATOM   1861 C  CD1  . ILE   A 1 266 ? -0.476  -12.454 28.471  1.00 34.01  ? 760  ILE   A CD1  1 
ATOM   1862 N  N    . GLY   A 1 267 ? -1.590  -7.549  29.301  1.00 31.64  ? 761  GLY   A N    1 
ATOM   1863 C  CA   . GLY   A 1 267 ? -1.588  -6.090  29.375  1.00 32.81  ? 761  GLY   A CA   1 
ATOM   1864 C  C    . GLY   A 1 267 ? -0.255  -5.497  28.939  1.00 34.47  ? 761  GLY   A C    1 
ATOM   1865 O  O    . GLY   A 1 267 ? 0.807   -5.957  29.358  1.00 32.14  ? 761  GLY   A O    1 
ATOM   1866 N  N    . MET   A 1 268 ? -0.338  -4.466  28.100  1.00 34.35  ? 762  MET   A N    1 
ATOM   1867 C  CA   . MET   A 1 268 ? 0.826   -3.748  27.595  1.00 38.49  ? 762  MET   A CA   1 
ATOM   1868 C  C    . MET   A 1 268 ? 0.473   -2.273  27.476  1.00 40.92  ? 762  MET   A C    1 
ATOM   1869 O  O    . MET   A 1 268 ? -0.700  -1.898  27.418  1.00 39.17  ? 762  MET   A O    1 
ATOM   1870 C  CB   . MET   A 1 268 ? 1.289   -4.266  26.222  1.00 41.28  ? 762  MET   A CB   1 
ATOM   1871 C  CG   . MET   A 1 268 ? 1.575   -5.762  26.138  1.00 43.07  ? 762  MET   A CG   1 
ATOM   1872 S  SD   . MET   A 1 268 ? 1.002   -6.420  24.563  1.00 54.35  ? 762  MET   A SD   1 
ATOM   1873 C  CE   . MET   A 1 268 ? -0.786  -6.561  24.852  1.00 39.56  ? 762  MET   A CE   1 
ATOM   1874 N  N    . ARG   A 1 269 ? 1.506   -1.434  27.442  1.00 39.91  ? 763  ARG   A N    1 
ATOM   1875 C  CA   . ARG   A 1 269 ? 1.273   -0.020  27.197  1.00 44.04  ? 763  ARG   A CA   1 
ATOM   1876 C  C    . ARG   A 1 269 ? 0.738   0.190   25.779  1.00 41.77  ? 763  ARG   A C    1 
ATOM   1877 O  O    . ARG   A 1 269 ? 0.963   -0.616  24.875  1.00 44.43  ? 763  ARG   A O    1 
ATOM   1878 C  CB   . ARG   A 1 269 ? 2.561   0.777   27.419  1.00 43.00  ? 763  ARG   A CB   1 
ATOM   1879 C  CG   . ARG   A 1 269 ? 2.928   0.910   28.893  1.00 40.27  ? 763  ARG   A CG   1 
ATOM   1880 C  CD   . ARG   A 1 269 ? 4.144   1.802   29.139  1.00 44.53  ? 763  ARG   A CD   1 
ATOM   1881 N  NE   . ARG   A 1 269 ? 5.377   1.199   28.645  1.00 49.04  ? 763  ARG   A NE   1 
ATOM   1882 C  CZ   . ARG   A 1 269 ? 6.096   0.299   29.305  1.00 45.69  ? 763  ARG   A CZ   1 
ATOM   1883 N  NH1  . ARG   A 1 269 ? 5.728   -0.140  30.498  1.00 43.54  ? 763  ARG   A NH1  1 
ATOM   1884 N  NH2  . ARG   A 1 269 ? 7.209   -0.178  28.749  1.00 42.91  ? 763  ARG   A NH2  1 
ATOM   1885 N  N    . LYS   A 1 270 ? 0.041   1.309   25.581  1.00 48.89  ? 764  LYS   A N    1 
ATOM   1886 C  CA   . LYS   A 1 270 ? -0.620  1.529   24.297  1.00 52.15  ? 764  LYS   A CA   1 
ATOM   1887 C  C    . LYS   A 1 270 ? 0.368   1.628   23.135  1.00 53.92  ? 764  LYS   A C    1 
ATOM   1888 O  O    . LYS   A 1 270 ? 0.004   1.323   21.998  1.00 55.21  ? 764  LYS   A O    1 
ATOM   1889 C  CB   . LYS   A 1 270 ? -1.493  2.777   24.377  1.00 53.50  ? 764  LYS   A CB   1 
ATOM   1890 C  CG   . LYS   A 1 270 ? -2.880  2.504   24.926  1.00 52.59  ? 764  LYS   A CG   1 
ATOM   1891 C  CD   . LYS   A 1 270 ? -3.366  3.633   25.823  1.00 58.65  ? 764  LYS   A CD   1 
ATOM   1892 C  CE   . LYS   A 1 270 ? -4.142  4.694   25.060  1.00 63.95  ? 764  LYS   A CE   1 
ATOM   1893 N  NZ   . LYS   A 1 270 ? -4.947  5.556   25.979  1.00 60.34  ? 764  LYS   A NZ   1 
ATOM   1894 N  N    . ASP   A 1 271 ? 1.610   2.016   23.393  1.00 50.26  ? 765  ASP   A N    1 
ATOM   1895 C  CA   . ASP   A 1 271 ? 2.610   2.168   22.344  1.00 58.19  ? 765  ASP   A CA   1 
ATOM   1896 C  C    . ASP   A 1 271 ? 3.516   0.949   22.202  1.00 58.54  ? 765  ASP   A C    1 
ATOM   1897 O  O    . ASP   A 1 271 ? 4.554   1.032   21.533  1.00 57.04  ? 765  ASP   A O    1 
ATOM   1898 C  CB   . ASP   A 1 271 ? 3.438   3.437   22.587  1.00 64.13  ? 765  ASP   A CB   1 
ATOM   1899 C  CG   . ASP   A 1 271 ? 4.455   3.291   23.719  1.00 64.30  ? 765  ASP   A CG   1 
ATOM   1900 O  OD1  . ASP   A 1 271 ? 4.467   2.258   24.432  1.00 62.61  ? 765  ASP   A OD1  1 
ATOM   1901 O  OD2  . ASP   A 1 271 ? 5.258   4.232   23.898  1.00 66.55  ? 765  ASP   A OD2  1 
ATOM   1902 N  N    . SER   A 1 272 ? 3.154   -0.167  22.823  1.00 56.17  ? 766  SER   A N    1 
ATOM   1903 C  CA   . SER   A 1 272 ? 3.980   -1.358  22.748  1.00 53.29  ? 766  SER   A CA   1 
ATOM   1904 C  C    . SER   A 1 272 ? 4.071   -1.831  21.301  1.00 51.27  ? 766  SER   A C    1 
ATOM   1905 O  O    . SER   A 1 272 ? 3.043   -1.924  20.619  1.00 48.86  ? 766  SER   A O    1 
ATOM   1906 C  CB   . SER   A 1 272 ? 3.399   -2.465  23.630  1.00 52.25  ? 766  SER   A CB   1 
ATOM   1907 O  OG   . SER   A 1 272 ? 4.130   -3.672  23.476  1.00 53.48  ? 766  SER   A OG   1 
ATOM   1908 N  N    . PRO   A 1 273 ? 5.272   -2.120  20.787  1.00 53.07  ? 767  PRO   A N    1 
ATOM   1909 C  CA   . PRO   A 1 273 ? 5.366   -2.716  19.450  1.00 51.91  ? 767  PRO   A CA   1 
ATOM   1910 C  C    . PRO   A 1 273 ? 4.954   -4.175  19.420  1.00 48.53  ? 767  PRO   A C    1 
ATOM   1911 O  O    . PRO   A 1 273 ? 4.756   -4.717  18.328  1.00 47.28  ? 767  PRO   A O    1 
ATOM   1912 C  CB   . PRO   A 1 273 ? 6.850   -2.567  19.106  1.00 57.21  ? 767  PRO   A CB   1 
ATOM   1913 C  CG   . PRO   A 1 273 ? 7.524   -2.640  20.431  1.00 59.96  ? 767  PRO   A CG   1 
ATOM   1914 C  CD   . PRO   A 1 273 ? 6.594   -1.976  21.422  1.00 53.09  ? 767  PRO   A CD   1 
ATOM   1915 N  N    . TRP   A 1 274 ? 4.830   -4.823  20.579  1.00 46.36  ? 768  TRP   A N    1 
ATOM   1916 C  CA   . TRP   A 1 274 ? 4.500   -6.237  20.649  1.00 48.34  ? 768  TRP   A CA   1 
ATOM   1917 C  C    . TRP   A 1 274 ? 3.005   -6.519  20.635  1.00 47.19  ? 768  TRP   A C    1 
ATOM   1918 O  O    . TRP   A 1 274 ? 2.623   -7.691  20.531  1.00 43.10  ? 768  TRP   A O    1 
ATOM   1919 C  CB   . TRP   A 1 274 ? 5.090   -6.867  21.919  1.00 52.61  ? 768  TRP   A CB   1 
ATOM   1920 C  CG   . TRP   A 1 274 ? 6.530   -6.610  22.102  1.00 51.82  ? 768  TRP   A CG   1 
ATOM   1921 C  CD1  . TRP   A 1 274 ? 7.093   -5.621  22.854  1.00 53.45  ? 768  TRP   A CD1  1 
ATOM   1922 C  CD2  . TRP   A 1 274 ? 7.614   -7.344  21.524  1.00 57.14  ? 768  TRP   A CD2  1 
ATOM   1923 N  NE1  . TRP   A 1 274 ? 8.459   -5.688  22.772  1.00 57.42  ? 768  TRP   A NE1  1 
ATOM   1924 C  CE2  . TRP   A 1 274 ? 8.807   -6.740  21.966  1.00 55.66  ? 768  TRP   A CE2  1 
ATOM   1925 C  CE3  . TRP   A 1 274 ? 7.692   -8.453  20.671  1.00 56.81  ? 768  TRP   A CE3  1 
ATOM   1926 C  CZ2  . TRP   A 1 274 ? 10.068  -7.203  21.587  1.00 63.76  ? 768  TRP   A CZ2  1 
ATOM   1927 C  CZ3  . TRP   A 1 274 ? 8.949   -8.912  20.294  1.00 59.29  ? 768  TRP   A CZ3  1 
ATOM   1928 C  CH2  . TRP   A 1 274 ? 10.117  -8.290  20.757  1.00 60.89  ? 768  TRP   A CH2  1 
ATOM   1929 N  N    . LYS   A 1 275 ? 2.145   -5.493  20.719  1.00 47.10  ? 769  LYS   A N    1 
ATOM   1930 C  CA   . LYS   A 1 275 ? 0.760   -5.773  21.098  1.00 44.25  ? 769  LYS   A CA   1 
ATOM   1931 C  C    . LYS   A 1 275 ? 0.021   -6.586  20.042  1.00 43.76  ? 769  LYS   A C    1 
ATOM   1932 O  O    . LYS   A 1 275 ? -0.732  -7.502  20.390  1.00 37.30  ? 769  LYS   A O    1 
ATOM   1933 C  CB   . LYS   A 1 275 ? -0.006  -4.491  21.416  1.00 45.64  ? 769  LYS   A CB   1 
ATOM   1934 C  CG   . LYS   A 1 275 ? 0.018   -3.420  20.358  1.00 52.67  ? 769  LYS   A CG   1 
ATOM   1935 C  CD   . LYS   A 1 275 ? -0.508  -2.097  20.937  1.00 56.12  ? 769  LYS   A CD   1 
ATOM   1936 C  CE   . LYS   A 1 275 ? -0.972  -1.141  19.838  1.00 59.64  ? 769  LYS   A CE   1 
ATOM   1937 N  NZ   . LYS   A 1 275 ? -0.485  -1.549  18.484  1.00 63.73  ? 769  LYS   A NZ   1 
ATOM   1938 N  N    . GLN   A 1 276 ? 0.199   -6.276  18.753  1.00 40.55  ? 770  GLN   A N    1 
ATOM   1939 C  CA   . GLN   A 1 276 ? -0.611  -6.975  17.753  1.00 45.03  ? 770  GLN   A CA   1 
ATOM   1940 C  C    . GLN   A 1 276 ? -0.188  -8.430  17.607  1.00 42.04  ? 770  GLN   A C    1 
ATOM   1941 O  O    . GLN   A 1 276 ? -1.041  -9.316  17.469  1.00 38.53  ? 770  GLN   A O    1 
ATOM   1942 C  CB   . GLN   A 1 276 ? -0.553  -6.253  16.406  1.00 50.52  ? 770  GLN   A CB   1 
ATOM   1943 C  CG   . GLN   A 1 276 ? -1.306  -6.937  15.220  1.00 53.63  ? 770  GLN   A CG   1 
ATOM   1944 C  CD   . GLN   A 1 276 ? -2.832  -7.228  15.400  1.00 61.97  ? 770  GLN   A CD   1 
ATOM   1945 O  OE1  . GLN   A 1 276 ? -3.329  -7.582  16.487  1.00 57.98  ? 770  GLN   A OE1  1 
ATOM   1946 N  NE2  . GLN   A 1 276 ? -3.568  -7.100  14.292  1.00 50.87  ? 770  GLN   A NE2  1 
ATOM   1947 N  N    . ASN   A 1 277 ? 1.117   -8.704  17.643  1.00 37.71  ? 771  ASN   A N    1 
ATOM   1948 C  CA   . ASN   A 1 277 ? 1.540   -10.097 17.566  1.00 42.04  ? 771  ASN   A CA   1 
ATOM   1949 C  C    . ASN   A 1 277 ? 1.179   -10.872 18.825  1.00 40.11  ? 771  ASN   A C    1 
ATOM   1950 O  O    . ASN   A 1 277 ? 0.910   -12.078 18.747  1.00 37.63  ? 771  ASN   A O    1 
ATOM   1951 C  CB   . ASN   A 1 277 ? 3.033   -10.183 17.273  1.00 39.56  ? 771  ASN   A CB   1 
ATOM   1952 C  CG   . ASN   A 1 277 ? 3.337   -9.912  15.815  1.00 47.43  ? 771  ASN   A CG   1 
ATOM   1953 O  OD1  . ASN   A 1 277 ? 2.453   -10.013 14.960  1.00 46.74  ? 771  ASN   A OD1  1 
ATOM   1954 N  ND2  . ASN   A 1 277 ? 4.584   -9.567  15.518  1.00 43.05  ? 771  ASN   A ND2  1 
ATOM   1955 N  N    . VAL   A 1 278 ? 1.170   -10.219 19.989  1.00 39.48  ? 772  VAL   A N    1 
ATOM   1956 C  CA   . VAL   A 1 278 ? 0.694   -10.899 21.190  1.00 40.45  ? 772  VAL   A CA   1 
ATOM   1957 C  C    . VAL   A 1 278 ? -0.744  -11.367 20.986  1.00 36.12  ? 772  VAL   A C    1 
ATOM   1958 O  O    . VAL   A 1 278 ? -1.084  -12.528 21.246  1.00 37.86  ? 772  VAL   A O    1 
ATOM   1959 C  CB   . VAL   A 1 278 ? 0.818   -9.987  22.424  1.00 42.52  ? 772  VAL   A CB   1 
ATOM   1960 C  CG1  . VAL   A 1 278 ? -0.018  -10.540 23.561  1.00 39.00  ? 772  VAL   A CG1  1 
ATOM   1961 C  CG2  . VAL   A 1 278 ? 2.276   -9.842  22.853  1.00 43.12  ? 772  VAL   A CG2  1 
ATOM   1962 N  N    . SER   A 1 279 ? -1.609  -10.469 20.505  1.00 36.66  ? 773  SER   A N    1 
ATOM   1963 C  CA   . SER   A 1 279 ? -3.018  -10.807 20.341  1.00 36.26  ? 773  SER   A CA   1 
ATOM   1964 C  C    . SER   A 1 279 ? -3.227  -11.886 19.281  1.00 36.67  ? 773  SER   A C    1 
ATOM   1965 O  O    . SER   A 1 279 ? -4.034  -12.805 19.472  1.00 33.35  ? 773  SER   A O    1 
ATOM   1966 C  CB   . SER   A 1 279 ? -3.809  -9.549  19.989  1.00 37.78  ? 773  SER   A CB   1 
ATOM   1967 O  OG   . SER   A 1 279 ? -5.109  -9.651  20.496  1.00 40.79  ? 773  SER   A OG   1 
ATOM   1968 N  N    . LEU   A 1 280 ? -2.545  -11.768 18.138  1.00 36.25  ? 774  LEU   A N    1 
ATOM   1969 C  CA   . LEU   A 1 280 ? -2.579  -12.823 17.126  1.00 37.08  ? 774  LEU   A CA   1 
ATOM   1970 C  C    . LEU   A 1 280 ? -2.165  -14.167 17.707  1.00 37.95  ? 774  LEU   A C    1 
ATOM   1971 O  O    . LEU   A 1 280 ? -2.793  -15.194 17.426  1.00 34.25  ? 774  LEU   A O    1 
ATOM   1972 C  CB   . LEU   A 1 280 ? -1.659  -12.439 15.969  1.00 37.22  ? 774  LEU   A CB   1 
ATOM   1973 C  CG   . LEU   A 1 280 ? -2.140  -11.272 15.102  1.00 38.00  ? 774  LEU   A CG   1 
ATOM   1974 C  CD1  . LEU   A 1 280 ? -1.336  -11.253 13.808  1.00 44.33  ? 774  LEU   A CD1  1 
ATOM   1975 C  CD2  . LEU   A 1 280 ? -3.594  -11.516 14.754  1.00 37.97  ? 774  LEU   A CD2  1 
ATOM   1976 N  N    . SER   A 1 281 ? -1.111  -14.183 18.525  1.00 35.78  ? 775  SER   A N    1 
ATOM   1977 C  CA   . SER   A 1 281 ? -0.662  -15.442 19.106  1.00 35.94  ? 775  SER   A CA   1 
ATOM   1978 C  C    . SER   A 1 281 ? -1.705  -16.024 20.053  1.00 33.42  ? 775  SER   A C    1 
ATOM   1979 O  O    . SER   A 1 281 ? -1.887  -17.247 20.113  1.00 32.53  ? 775  SER   A O    1 
ATOM   1980 C  CB   . SER   A 1 281 ? 0.667   -15.244 19.835  1.00 40.98  ? 775  SER   A CB   1 
ATOM   1981 O  OG   . SER   A 1 281 ? 1.051   -16.453 20.464  1.00 46.32  ? 775  SER   A OG   1 
ATOM   1982 N  N    . ILE   A 1 282 ? -2.394  -15.172 20.807  1.00 36.14  ? 776  ILE   A N    1 
ATOM   1983 C  CA   . ILE   A 1 282 ? -3.454  -15.676 21.676  1.00 32.01  ? 776  ILE   A CA   1 
ATOM   1984 C  C    . ILE   A 1 282 ? -4.529  -16.352 20.842  1.00 32.92  ? 776  ILE   A C    1 
ATOM   1985 O  O    . ILE   A 1 282 ? -4.989  -17.452 21.167  1.00 31.98  ? 776  ILE   A O    1 
ATOM   1986 C  CB   . ILE   A 1 282 ? -4.053  -14.542 22.526  1.00 30.50  ? 776  ILE   A CB   1 
ATOM   1987 C  CG1  . ILE   A 1 282 ? -2.999  -13.942 23.465  1.00 33.48  ? 776  ILE   A CG1  1 
ATOM   1988 C  CG2  . ILE   A 1 282 ? -5.313  -15.058 23.271  1.00 27.07  ? 776  ILE   A CG2  1 
ATOM   1989 C  CD1  . ILE   A 1 282 ? -2.391  -14.894 24.422  1.00 36.70  ? 776  ILE   A CD1  1 
ATOM   1990 N  N    . LEU   A 1 283 ? -4.959  -15.694 19.756  1.00 31.74  ? 777  LEU   A N    1 
ATOM   1991 C  CA   . LEU   A 1 283 ? -5.993  -16.283 18.903  1.00 32.84  ? 777  LEU   A CA   1 
ATOM   1992 C  C    . LEU   A 1 283 ? -5.518  -17.602 18.311  1.00 29.95  ? 777  LEU   A C    1 
ATOM   1993 O  O    . LEU   A 1 283 ? -6.264  -18.588 18.286  1.00 30.24  ? 777  LEU   A O    1 
ATOM   1994 C  CB   . LEU   A 1 283 ? -6.373  -15.313 17.783  1.00 31.48  ? 777  LEU   A CB   1 
ATOM   1995 C  CG   . LEU   A 1 283 ? -6.937  -13.976 18.244  1.00 30.33  ? 777  LEU   A CG   1 
ATOM   1996 C  CD1  . LEU   A 1 283 ? -7.214  -13.078 17.036  1.00 36.61  ? 777  LEU   A CD1  1 
ATOM   1997 C  CD2  . LEU   A 1 283 ? -8.203  -14.205 19.062  1.00 32.77  ? 777  LEU   A CD2  1 
ATOM   1998 N  N    . LYS   A 1 284 ? -4.281  -17.633 17.801  1.00 34.58  ? 778  LYS   A N    1 
ATOM   1999 C  CA   . LYS   A 1 284 ? -3.750  -18.879 17.248  1.00 33.73  ? 778  LYS   A CA   1 
ATOM   2000 C  C    . LYS   A 1 284 ? -3.782  -19.982 18.292  1.00 31.32  ? 778  LYS   A C    1 
ATOM   2001 O  O    . LYS   A 1 284 ? -4.078  -21.146 17.978  1.00 32.64  ? 778  LYS   A O    1 
ATOM   2002 C  CB   . LYS   A 1 284 ? -2.319  -18.664 16.746  1.00 31.79  ? 778  LYS   A CB   1 
ATOM   2003 C  CG   . LYS   A 1 284 ? -1.641  -19.899 16.153  1.00 35.39  ? 778  LYS   A CG   1 
ATOM   2004 C  CD   . LYS   A 1 284 ? -0.163  -19.609 15.820  1.00 42.89  ? 778  LYS   A CD   1 
ATOM   2005 C  CE   . LYS   A 1 284 ? 0.477   -20.827 15.198  1.00 44.94  ? 778  LYS   A CE   1 
ATOM   2006 N  NZ   . LYS   A 1 284 ? -0.239  -21.141 13.935  1.00 51.77  ? 778  LYS   A NZ   1 
ATOM   2007 N  N    . SER   A 1 285 ? -3.524  -19.624 19.555  1.00 31.71  ? 779  SER   A N    1 
ATOM   2008 C  CA   . SER   A 1 285 ? -3.436  -20.625 20.617  1.00 34.24  ? 779  SER   A CA   1 
ATOM   2009 C  C    . SER   A 1 285 ? -4.808  -21.157 21.001  1.00 32.18  ? 779  SER   A C    1 
ATOM   2010 O  O    . SER   A 1 285 ? -4.955  -22.342 21.321  1.00 33.46  ? 779  SER   A O    1 
ATOM   2011 C  CB   . SER   A 1 285 ? -2.732  -20.026 21.834  1.00 34.73  ? 779  SER   A CB   1 
ATOM   2012 O  OG   . SER   A 1 285 ? -1.372  -19.822 21.542  1.00 33.35  ? 779  SER   A OG   1 
ATOM   2013 N  N    . HIS   A 1 286 ? -5.829  -20.299 20.996  1.00 32.81  ? 780  HIS   A N    1 
ATOM   2014 C  CA   . HIS   A 1 286 ? -7.184  -20.808 21.148  1.00 30.13  ? 780  HIS   A CA   1 
ATOM   2015 C  C    . HIS   A 1 286 ? -7.505  -21.757 20.003  1.00 31.51  ? 780  HIS   A C    1 
ATOM   2016 O  O    . HIS   A 1 286 ? -8.015  -22.867 20.206  1.00 29.56  ? 780  HIS   A O    1 
ATOM   2017 C  CB   . HIS   A 1 286 ? -8.180  -19.642 21.160  1.00 28.90  ? 780  HIS   A CB   1 
ATOM   2018 C  CG   . HIS   A 1 286 ? -8.282  -18.941 22.479  1.00 32.02  ? 780  HIS   A CG   1 
ATOM   2019 N  ND1  . HIS   A 1 286 ? -8.657  -19.578 23.643  1.00 30.50  ? 780  HIS   A ND1  1 
ATOM   2020 C  CD2  . HIS   A 1 286 ? -8.051  -17.643 22.817  1.00 29.54  ? 780  HIS   A CD2  1 
ATOM   2021 C  CE1  . HIS   A 1 286 ? -8.669  -18.706 24.638  1.00 30.21  ? 780  HIS   A CE1  1 
ATOM   2022 N  NE2  . HIS   A 1 286 ? -8.311  -17.524 24.163  1.00 31.52  ? 780  HIS   A NE2  1 
ATOM   2023 N  N    . GLU   A 1 287 ? -7.183  -21.334 18.783  1.00 28.68  ? 781  GLU   A N    1 
ATOM   2024 C  CA   . GLU   A 1 287 ? -7.660  -22.037 17.597  1.00 34.62  ? 781  GLU   A CA   1 
ATOM   2025 C  C    . GLU   A 1 287 ? -6.979  -23.384 17.383  1.00 29.81  ? 781  GLU   A C    1 
ATOM   2026 O  O    . GLU   A 1 287 ? -7.618  -24.305 16.854  1.00 31.23  ? 781  GLU   A O    1 
ATOM   2027 C  CB   . GLU   A 1 287 ? -7.500  -21.143 16.358  1.00 29.26  ? 781  GLU   A CB   1 
ATOM   2028 C  CG   . GLU   A 1 287 ? -8.463  -19.928 16.419  1.00 30.81  ? 781  GLU   A CG   1 
ATOM   2029 C  CD   . GLU   A 1 287 ? -8.117  -18.855 15.420  1.00 34.74  ? 781  GLU   A CD   1 
ATOM   2030 O  OE1  . GLU   A 1 287 ? -7.666  -19.196 14.295  1.00 33.37  ? 781  GLU   A OE1  1 
ATOM   2031 O  OE2  . GLU   A 1 287 ? -8.318  -17.670 15.752  1.00 34.92  ? 781  GLU   A OE2  1 
ATOM   2032 N  N    . ASN   A 1 288 ? -5.700  -23.534 17.756  1.00 32.69  ? 782  ASN   A N    1 
ATOM   2033 C  CA   . ASN   A 1 288 ? -4.998  -24.790 17.508  1.00 34.57  ? 782  ASN   A CA   1 
ATOM   2034 C  C    . ASN   A 1 288 ? -4.987  -25.718 18.721  1.00 35.44  ? 782  ASN   A C    1 
ATOM   2035 O  O    . ASN   A 1 288 ? -4.296  -26.742 18.695  1.00 36.56  ? 782  ASN   A O    1 
ATOM   2036 C  CB   . ASN   A 1 288 ? -3.559  -24.538 17.031  1.00 36.06  ? 782  ASN   A CB   1 
ATOM   2037 C  CG   . ASN   A 1 288 ? -2.678  -23.896 18.090  1.00 38.00  ? 782  ASN   A CG   1 
ATOM   2038 O  OD1  . ASN   A 1 288 ? -2.995  -23.900 19.297  1.00 32.23  ? 782  ASN   A OD1  1 
ATOM   2039 N  ND2  . ASN   A 1 288 ? -1.531  -23.364 17.647  1.00 38.28  ? 782  ASN   A ND2  1 
ATOM   2040 N  N    . GLY   A 1 289 ? -5.726  -25.387 19.775  1.00 31.79  ? 783  GLY   A N    1 
ATOM   2041 C  CA   . GLY   A 1 289 ? -5.842  -26.258 20.928  1.00 35.95  ? 783  GLY   A CA   1 
ATOM   2042 C  C    . GLY   A 1 289 ? -4.814  -26.033 22.020  1.00 38.44  ? 783  GLY   A C    1 
ATOM   2043 O  O    . GLY   A 1 289 ? -4.859  -26.728 23.046  1.00 35.96  ? 783  GLY   A O    1 
ATOM   2044 N  N    . PHE   A 1 290 ? -3.894  -25.085 21.847  1.00 35.45  ? 784  PHE   A N    1 
ATOM   2045 C  CA   . PHE   A 1 290 ? -2.867  -24.873 22.866  1.00 36.41  ? 784  PHE   A CA   1 
ATOM   2046 C  C    . PHE   A 1 290 ? -3.477  -24.413 24.187  1.00 36.18  ? 784  PHE   A C    1 
ATOM   2047 O  O    . PHE   A 1 290 ? -3.121  -24.943 25.247  1.00 33.08  ? 784  PHE   A O    1 
ATOM   2048 C  CB   . PHE   A 1 290 ? -1.820  -23.867 22.378  1.00 36.14  ? 784  PHE   A CB   1 
ATOM   2049 C  CG   . PHE   A 1 290 ? -0.712  -23.611 23.389  1.00 38.45  ? 784  PHE   A CG   1 
ATOM   2050 C  CD1  . PHE   A 1 290 ? 0.323   -24.519 23.545  1.00 42.91  ? 784  PHE   A CD1  1 
ATOM   2051 C  CD2  . PHE   A 1 290 ? -0.739  -22.486 24.206  1.00 38.71  ? 784  PHE   A CD2  1 
ATOM   2052 C  CE1  . PHE   A 1 290 ? 1.331   -24.305 24.480  1.00 39.70  ? 784  PHE   A CE1  1 
ATOM   2053 C  CE2  . PHE   A 1 290 ? 0.268   -22.264 25.142  1.00 37.94  ? 784  PHE   A CE2  1 
ATOM   2054 C  CZ   . PHE   A 1 290 ? 1.295   -23.190 25.278  1.00 36.21  ? 784  PHE   A CZ   1 
ATOM   2055 N  N    . MET   A 1 291 ? -4.402  -23.428 24.147  1.00 30.94  ? 785  MET   A N    1 
ATOM   2056 C  CA   . MET   A 1 291 ? -5.077  -22.990 25.368  1.00 33.68  ? 785  MET   A CA   1 
ATOM   2057 C  C    . MET   A 1 291 ? -5.859  -24.118 26.012  1.00 35.15  ? 785  MET   A C    1 
ATOM   2058 O  O    . MET   A 1 291 ? -5.909  -24.217 27.239  1.00 37.64  ? 785  MET   A O    1 
ATOM   2059 C  CB   . MET   A 1 291 ? -6.015  -21.795 25.099  1.00 34.71  ? 785  MET   A CB   1 
ATOM   2060 C  CG   . MET   A 1 291 ? -5.254  -20.628 24.516  1.00 37.62  ? 785  MET   A CG   1 
ATOM   2061 S  SD   . MET   A 1 291 ? -4.107  -19.799 25.654  1.00 37.30  ? 785  MET   A SD   1 
ATOM   2062 C  CE   . MET   A 1 291 ? -4.666  -20.259 27.240  1.00 40.11  ? 785  MET   A CE   1 
ATOM   2063 N  N    . GLU   A 1 292 ? -6.490  -24.975 25.212  1.00 31.85  ? 786  GLU   A N    1 
ATOM   2064 C  CA   . GLU   A 1 292 ? -7.182  -26.106 25.813  1.00 35.91  ? 786  GLU   A CA   1 
ATOM   2065 C  C    . GLU   A 1 292 ? -6.195  -27.028 26.527  1.00 37.02  ? 786  GLU   A C    1 
ATOM   2066 O  O    . GLU   A 1 292 ? -6.471  -27.504 27.633  1.00 39.88  ? 786  GLU   A O    1 
ATOM   2067 C  CB   . GLU   A 1 292 ? -7.984  -26.868 24.751  1.00 45.49  ? 786  GLU   A CB   1 
ATOM   2068 C  CG   . GLU   A 1 292 ? -8.939  -27.892 25.345  1.00 48.84  ? 786  GLU   A CG   1 
ATOM   2069 C  CD   . GLU   A 1 292 ? -9.765  -28.630 24.296  1.00 57.52  ? 786  GLU   A CD   1 
ATOM   2070 O  OE1  . GLU   A 1 292 ? -9.294  -29.653 23.756  1.00 63.93  ? 786  GLU   A OE1  1 
ATOM   2071 O  OE2  . GLU   A 1 292 ? -10.874 -28.153 23.986  1.00 59.49  ? 786  GLU   A OE2  1 
ATOM   2072 N  N    . ASP   A 1 293 ? -5.033  -27.286 25.917  1.00 37.92  ? 787  ASP   A N    1 
ATOM   2073 C  CA   . ASP   A 1 293 ? -4.004  -28.082 26.587  1.00 34.88  ? 787  ASP   A CA   1 
ATOM   2074 C  C    . ASP   A 1 293 ? -3.611  -27.460 27.931  1.00 39.65  ? 787  ASP   A C    1 
ATOM   2075 O  O    . ASP   A 1 293 ? -3.527  -28.156 28.952  1.00 36.08  ? 787  ASP   A O    1 
ATOM   2076 C  CB   . ASP   A 1 293 ? -2.780  -28.211 25.687  1.00 41.29  ? 787  ASP   A CB   1 
ATOM   2077 C  CG   . ASP   A 1 293 ? -3.033  -29.091 24.474  1.00 50.89  ? 787  ASP   A CG   1 
ATOM   2078 O  OD1  . ASP   A 1 293 ? -3.917  -29.976 24.545  1.00 54.84  ? 787  ASP   A OD1  1 
ATOM   2079 O  OD2  . ASP   A 1 293 ? -2.352  -28.880 23.441  1.00 52.64  ? 787  ASP   A OD2  1 
ATOM   2080 N  N    . LEU   A 1 294 ? -3.354  -26.142 27.953  1.00 36.33  ? 788  LEU   A N    1 
ATOM   2081 C  CA   . LEU   A 1 294 ? -3.062  -25.497 29.232  1.00 36.69  ? 788  LEU   A CA   1 
ATOM   2082 C  C    . LEU   A 1 294 ? -4.203  -25.703 30.212  1.00 38.81  ? 788  LEU   A C    1 
ATOM   2083 O  O    . LEU   A 1 294 ? -3.979  -25.938 31.410  1.00 37.82  ? 788  LEU   A O    1 
ATOM   2084 C  CB   . LEU   A 1 294 ? -2.805  -24.001 29.033  1.00 32.19  ? 788  LEU   A CB   1 
ATOM   2085 C  CG   . LEU   A 1 294 ? -1.547  -23.646 28.248  1.00 34.57  ? 788  LEU   A CG   1 
ATOM   2086 C  CD1  . LEU   A 1 294 ? -1.347  -22.143 28.271  1.00 37.25  ? 788  LEU   A CD1  1 
ATOM   2087 C  CD2  . LEU   A 1 294 ? -0.332  -24.359 28.846  1.00 35.64  ? 788  LEU   A CD2  1 
ATOM   2088 N  N    . ASP   A 1 295 ? -5.440  -25.626 29.715  1.00 36.47  ? 789  ASP   A N    1 
ATOM   2089 C  CA   . ASP   A 1 295 ? -6.590  -25.750 30.597  1.00 42.65  ? 789  ASP   A CA   1 
ATOM   2090 C  C    . ASP   A 1 295 ? -6.622  -27.135 31.222  1.00 43.83  ? 789  ASP   A C    1 
ATOM   2091 O  O    . ASP   A 1 295 ? -6.864  -27.283 32.423  1.00 50.46  ? 789  ASP   A O    1 
ATOM   2092 C  CB   . ASP   A 1 295 ? -7.875  -25.491 29.820  1.00 45.15  ? 789  ASP   A CB   1 
ATOM   2093 C  CG   . ASP   A 1 295 ? -8.985  -25.000 30.709  1.00 53.84  ? 789  ASP   A CG   1 
ATOM   2094 O  OD1  . ASP   A 1 295 ? -8.904  -23.807 31.104  1.00 53.72  ? 789  ASP   A OD1  1 
ATOM   2095 O  OD2  . ASP   A 1 295 ? -9.875  -25.799 31.061  1.00 55.63  ? 789  ASP   A OD2  1 
ATOM   2096 N  N    . LYS   A 1 296 ? -6.352  -28.163 30.425  1.00 42.11  ? 790  LYS   A N    1 
ATOM   2097 C  CA   . LYS   A 1 296 ? -6.296  -29.517 30.965  1.00 48.66  ? 790  LYS   A CA   1 
ATOM   2098 C  C    . LYS   A 1 296 ? -5.106  -29.696 31.901  1.00 47.91  ? 790  LYS   A C    1 
ATOM   2099 O  O    . LYS   A 1 296 ? -5.217  -30.402 32.910  1.00 49.21  ? 790  LYS   A O    1 
ATOM   2100 C  CB   . LYS   A 1 296 ? -6.247  -30.523 29.815  1.00 51.54  ? 790  LYS   A CB   1 
ATOM   2101 C  CG   . LYS   A 1 296 ? -7.488  -30.444 28.912  1.00 58.63  ? 790  LYS   A CG   1 
ATOM   2102 C  CD   . LYS   A 1 296 ? -7.439  -31.454 27.771  1.00 63.17  ? 790  LYS   A CD   1 
ATOM   2103 C  CE   . LYS   A 1 296 ? -8.705  -31.397 26.917  1.00 63.57  ? 790  LYS   A CE   1 
ATOM   2104 N  NZ   . LYS   A 1 296 ? -8.609  -32.345 25.769  1.00 65.97  ? 790  LYS   A NZ   1 
ATOM   2105 N  N    . THR   A 1 297 ? -3.976  -29.046 31.606  1.00 39.37  ? 791  THR   A N    1 
ATOM   2106 C  CA   . THR   A 1 297 ? -2.773  -29.253 32.412  1.00 41.74  ? 791  THR   A CA   1 
ATOM   2107 C  C    . THR   A 1 297 ? -2.912  -28.610 33.786  1.00 39.95  ? 791  THR   A C    1 
ATOM   2108 O  O    . THR   A 1 297 ? -2.581  -29.227 34.804  1.00 44.34  ? 791  THR   A O    1 
ATOM   2109 C  CB   . THR   A 1 297 ? -1.549  -28.687 31.690  1.00 36.31  ? 791  THR   A CB   1 
ATOM   2110 O  OG1  . THR   A 1 297 ? -1.376  -29.366 30.445  1.00 40.05  ? 791  THR   A OG1  1 
ATOM   2111 C  CG2  . THR   A 1 297 ? -0.270  -28.868 32.545  1.00 38.54  ? 791  THR   A CG2  1 
ATOM   2112 N  N    . TRP   A 1 298 ? -3.435  -27.391 33.831  1.00 37.09  ? 792  TRP   A N    1 
ATOM   2113 C  CA   . TRP   A 1 298 ? -3.425  -26.557 35.023  1.00 41.47  ? 792  TRP   A CA   1 
ATOM   2114 C  C    . TRP   A 1 298 ? -4.776  -26.380 35.694  1.00 44.59  ? 792  TRP   A C    1 
ATOM   2115 O  O    . TRP   A 1 298 ? -4.812  -26.173 36.910  1.00 42.34  ? 792  TRP   A O    1 
ATOM   2116 C  CB   . TRP   A 1 298 ? -2.877  -25.168 34.678  1.00 38.54  ? 792  TRP   A CB   1 
ATOM   2117 C  CG   . TRP   A 1 298 ? -1.472  -25.231 34.241  1.00 34.84  ? 792  TRP   A CG   1 
ATOM   2118 C  CD1  . TRP   A 1 298 ? -1.004  -25.089 32.970  1.00 35.92  ? 792  TRP   A CD1  1 
ATOM   2119 C  CD2  . TRP   A 1 298 ? -0.339  -25.504 35.066  1.00 36.86  ? 792  TRP   A CD2  1 
ATOM   2120 N  NE1  . TRP   A 1 298 ? 0.361   -25.232 32.954  1.00 34.42  ? 792  TRP   A NE1  1 
ATOM   2121 C  CE2  . TRP   A 1 298 ? 0.796   -25.488 34.231  1.00 37.15  ? 792  TRP   A CE2  1 
ATOM   2122 C  CE3  . TRP   A 1 298 ? -0.168  -25.749 36.437  1.00 35.02  ? 792  TRP   A CE3  1 
ATOM   2123 C  CZ2  . TRP   A 1 298 ? 2.085   -25.717 34.717  1.00 34.38  ? 792  TRP   A CZ2  1 
ATOM   2124 C  CZ3  . TRP   A 1 298 ? 1.121   -25.974 36.919  1.00 34.62  ? 792  TRP   A CZ3  1 
ATOM   2125 C  CH2  . TRP   A 1 298 ? 2.227   -25.952 36.058  1.00 33.65  ? 792  TRP   A CH2  1 
ATOM   2126 N  N    . VAL   A 1 299 ? -5.877  -26.425 34.950  1.00 47.48  ? 793  VAL   A N    1 
ATOM   2127 C  CA   . VAL   A 1 299 ? -7.171  -25.959 35.459  1.00 53.50  ? 793  VAL   A CA   1 
ATOM   2128 C  C    . VAL   A 1 299 ? -8.113  -27.108 35.798  1.00 61.84  ? 793  VAL   A C    1 
ATOM   2129 O  O    . VAL   A 1 299 ? -8.694  -27.133 36.883  1.00 65.59  ? 793  VAL   A O    1 
ATOM   2130 C  CB   . VAL   A 1 299 ? -7.822  -24.971 34.466  1.00 56.53  ? 793  VAL   A CB   1 
ATOM   2131 C  CG1  . VAL   A 1 299 ? -9.062  -24.347 35.082  1.00 54.82  ? 793  VAL   A CG1  1 
ATOM   2132 C  CG2  . VAL   A 1 299 ? -6.832  -23.876 34.093  1.00 49.95  ? 793  VAL   A CG2  1 
ATOM   2133 N  N    . ARG   A 1 300 ? -8.289  -28.071 34.892  1.00 69.36  ? 794  ARG   A N    1 
ATOM   2134 C  CA   . ARG   A 1 300 ? -9.292  -29.125 35.057  1.00 75.82  ? 794  ARG   A CA   1 
ATOM   2135 C  C    . ARG   A 1 300 ? -8.617  -30.487 35.218  1.00 76.27  ? 794  ARG   A C    1 
ATOM   2136 O  O    . ARG   A 1 300 ? -8.130  -31.062 34.240  1.00 79.02  ? 794  ARG   A O    1 
ATOM   2137 C  CB   . ARG   A 1 300 ? -10.277 -29.137 33.882  1.00 79.59  ? 794  ARG   A CB   1 
ATOM   2138 C  CG   . ARG   A 1 300 ? -9.660  -28.969 32.487  1.00 79.68  ? 794  ARG   A CG   1 
ATOM   2139 C  CD   . ARG   A 1 300 ? -10.091 -30.077 31.511  1.00 82.14  ? 794  ARG   A CD   1 
ATOM   2140 N  NE   . ARG   A 1 300 ? -9.553  -31.382 31.895  1.00 91.71  ? 794  ARG   A NE   1 
ATOM   2141 C  CZ   . ARG   A 1 300 ? -9.695  -32.501 31.193  1.00 94.27  ? 794  ARG   A CZ   1 
ATOM   2142 N  NH1  . ARG   A 1 300 ? -10.345 -32.519 30.040  1.00 89.84  ? 794  ARG   A NH1  1 
ATOM   2143 N  NH2  . ARG   A 1 300 ? -9.163  -33.630 31.657  1.00 88.67  ? 794  ARG   A NH2  1 
ATOM   2144 N  N    . TYR   A 1 301 ? -8.611  -31.006 36.447  1.00 85.14  ? 795  TYR   A N    1 
ATOM   2145 C  CA   . TYR   A 1 301 ? -8.144  -32.366 36.746  1.00 83.16  ? 795  TYR   A CA   1 
ATOM   2146 C  C    . TYR   A 1 301 ? -8.438  -32.730 38.202  1.00 80.79  ? 795  TYR   A C    1 
ATOM   2147 O  O    . TYR   A 1 301 ? -9.575  -33.023 38.567  1.00 82.94  ? 795  TYR   A O    1 
ATOM   2148 C  CB   . TYR   A 1 301 ? -6.639  -32.521 36.469  1.00 84.50  ? 795  TYR   A CB   1 
ATOM   2149 C  CG   . TYR   A 1 301 ? -5.744  -31.609 37.291  1.00 84.60  ? 795  TYR   A CG   1 
ATOM   2150 C  CD1  . TYR   A 1 301 ? -5.413  -30.335 36.842  1.00 70.91  ? 795  TYR   A CD1  1 
ATOM   2151 C  CD2  . TYR   A 1 301 ? -5.223  -32.027 38.512  1.00 84.59  ? 795  TYR   A CD2  1 
ATOM   2152 C  CE1  . TYR   A 1 301 ? -4.599  -29.501 37.589  1.00 71.12  ? 795  TYR   A CE1  1 
ATOM   2153 C  CE2  . TYR   A 1 301 ? -4.408  -31.200 39.263  1.00 83.07  ? 795  TYR   A CE2  1 
ATOM   2154 C  CZ   . TYR   A 1 301 ? -4.099  -29.938 38.797  1.00 74.11  ? 795  TYR   A CZ   1 
ATOM   2155 O  OH   . TYR   A 1 301 ? -3.289  -29.111 39.540  1.00 72.24  ? 795  TYR   A OH   1 
ATOM   2156 N  N    . ASP   B 2 17  ? -18.057 11.335  6.551   1.00 95.17  ? 403  ASP   B N    1 
ATOM   2157 C  CA   . ASP   B 2 17  ? -17.580 12.046  7.731   1.00 97.78  ? 403  ASP   B CA   1 
ATOM   2158 C  C    . ASP   B 2 17  ? -17.955 11.276  8.999   1.00 91.16  ? 403  ASP   B C    1 
ATOM   2159 O  O    . ASP   B 2 17  ? -17.230 10.382  9.446   1.00 84.67  ? 403  ASP   B O    1 
ATOM   2160 C  CB   . ASP   B 2 17  ? -18.163 13.465  7.766   1.00 99.28  ? 403  ASP   B CB   1 
ATOM   2161 C  CG   . ASP   B 2 17  ? -17.496 14.352  8.803   1.00 104.22 ? 403  ASP   B CG   1 
ATOM   2162 O  OD1  . ASP   B 2 17  ? -16.460 13.936  9.372   1.00 103.66 ? 403  ASP   B OD1  1 
ATOM   2163 O  OD2  . ASP   B 2 17  ? -18.007 15.470  9.042   1.00 103.96 ? 403  ASP   B OD2  1 
ATOM   2164 N  N    . ASN   B 2 18  ? -19.101 11.641  9.568   1.00 85.32  ? 404  ASN   B N    1 
ATOM   2165 C  CA   . ASN   B 2 18  ? -19.662 10.982  10.738  1.00 72.61  ? 404  ASN   B CA   1 
ATOM   2166 C  C    . ASN   B 2 18  ? -20.786 10.024  10.372  1.00 63.97  ? 404  ASN   B C    1 
ATOM   2167 O  O    . ASN   B 2 18  ? -21.466 9.494   11.262  1.00 51.55  ? 404  ASN   B O    1 
ATOM   2168 C  CB   . ASN   B 2 18  ? -20.164 12.033  11.720  1.00 75.99  ? 404  ASN   B CB   1 
ATOM   2169 C  CG   . ASN   B 2 18  ? -19.846 11.677  13.133  1.00 73.94  ? 404  ASN   B CG   1 
ATOM   2170 O  OD1  . ASN   B 2 18  ? -18.814 11.061  13.404  1.00 73.26  ? 404  ASN   B OD1  1 
ATOM   2171 N  ND2  . ASN   B 2 18  ? -20.719 12.068  14.057  1.00 77.38  ? 404  ASN   B ND2  1 
ATOM   2172 N  N    . HIS   B 2 19  ? -20.994 9.800   9.080   1.00 62.82  ? 405  HIS   B N    1 
ATOM   2173 C  CA   . HIS   B 2 19  ? -22.052 8.945   8.557   1.00 58.99  ? 405  HIS   B CA   1 
ATOM   2174 C  C    . HIS   B 2 19  ? -21.415 7.732   7.885   1.00 59.74  ? 405  HIS   B C    1 
ATOM   2175 O  O    . HIS   B 2 19  ? -20.799 7.861   6.822   1.00 71.05  ? 405  HIS   B O    1 
ATOM   2176 C  CB   . HIS   B 2 19  ? -22.912 9.728   7.579   1.00 55.22  ? 405  HIS   B CB   1 
ATOM   2177 C  CG   . HIS   B 2 19  ? -24.096 8.968   7.104   1.00 56.40  ? 405  HIS   B CG   1 
ATOM   2178 N  ND1  . HIS   B 2 19  ? -25.174 8.700   7.915   1.00 58.89  ? 405  HIS   B ND1  1 
ATOM   2179 C  CD2  . HIS   B 2 19  ? -24.363 8.393   5.909   1.00 55.96  ? 405  HIS   B CD2  1 
ATOM   2180 C  CE1  . HIS   B 2 19  ? -26.065 8.000   7.235   1.00 57.71  ? 405  HIS   B CE1  1 
ATOM   2181 N  NE2  . HIS   B 2 19  ? -25.598 7.804   6.015   1.00 59.42  ? 405  HIS   B NE2  1 
ATOM   2182 N  N    . LEU   B 2 20  ? -21.593 6.553   8.480   1.00 52.85  ? 406  LEU   B N    1 
ATOM   2183 C  CA   . LEU   B 2 20  ? -20.752 5.399   8.192   1.00 48.12  ? 406  LEU   B CA   1 
ATOM   2184 C  C    . LEU   B 2 20  ? -21.497 4.300   7.438   1.00 45.04  ? 406  LEU   B C    1 
ATOM   2185 O  O    . LEU   B 2 20  ? -22.651 3.981   7.741   1.00 42.43  ? 406  LEU   B O    1 
ATOM   2186 C  CB   . LEU   B 2 20  ? -20.183 4.830   9.493   1.00 46.49  ? 406  LEU   B CB   1 
ATOM   2187 C  CG   . LEU   B 2 20  ? -19.550 5.839   10.446  1.00 48.54  ? 406  LEU   B CG   1 
ATOM   2188 C  CD1  . LEU   B 2 20  ? -19.031 5.154   11.706  1.00 48.11  ? 406  LEU   B CD1  1 
ATOM   2189 C  CD2  . LEU   B 2 20  ? -18.413 6.572   9.748   1.00 53.93  ? 406  LEU   B CD2  1 
ATOM   2190 N  N    . SER   B 2 21  ? -20.816 3.700   6.472   1.00 43.33  ? 407  SER   B N    1 
ATOM   2191 C  CA   . SER   B 2 21  ? -21.345 2.526   5.792   1.00 42.19  ? 407  SER   B CA   1 
ATOM   2192 C  C    . SER   B 2 21  ? -21.065 1.285   6.638   1.00 38.13  ? 407  SER   B C    1 
ATOM   2193 O  O    . SER   B 2 21  ? -19.906 0.983   6.948   1.00 36.04  ? 407  SER   B O    1 
ATOM   2194 C  CB   . SER   B 2 21  ? -20.725 2.396   4.402   1.00 45.24  ? 407  SER   B CB   1 
ATOM   2195 O  OG   . SER   B 2 21  ? -20.976 1.106   3.867   1.00 43.64  ? 407  SER   B OG   1 
ATOM   2196 N  N    . ILE   B 2 22  ? -22.119 0.564   7.014   1.00 38.51  ? 408  ILE   B N    1 
ATOM   2197 C  CA   . ILE   B 2 22  ? -22.002 -0.575  7.924   1.00 35.28  ? 408  ILE   B CA   1 
ATOM   2198 C  C    . ILE   B 2 22  ? -22.672 -1.788  7.289   1.00 34.07  ? 408  ILE   B C    1 
ATOM   2199 O  O    . ILE   B 2 22  ? -23.801 -1.687  6.795   1.00 37.27  ? 408  ILE   B O    1 
ATOM   2200 C  CB   . ILE   B 2 22  ? -22.635 -0.244  9.290   1.00 37.01  ? 408  ILE   B CB   1 
ATOM   2201 C  CG1  . ILE   B 2 22  ? -21.933 0.989   9.907   1.00 36.99  ? 408  ILE   B CG1  1 
ATOM   2202 C  CG2  . ILE   B 2 22  ? -22.603 -1.447  10.213  1.00 34.93  ? 408  ILE   B CG2  1 
ATOM   2203 C  CD1  . ILE   B 2 22  ? -22.392 1.329   11.301  1.00 34.81  ? 408  ILE   B CD1  1 
ATOM   2204 N  N    . VAL   B 2 23  ? -21.985 -2.934  7.302   1.00 31.63  ? 409  VAL   B N    1 
ATOM   2205 C  CA   . VAL   B 2 23  ? -22.497 -4.154  6.687   1.00 29.90  ? 409  VAL   B CA   1 
ATOM   2206 C  C    . VAL   B 2 23  ? -22.888 -5.124  7.788   1.00 34.39  ? 409  VAL   B C    1 
ATOM   2207 O  O    . VAL   B 2 23  ? -22.274 -5.160  8.863   1.00 32.43  ? 409  VAL   B O    1 
ATOM   2208 C  CB   . VAL   B 2 23  ? -21.486 -4.795  5.700   1.00 34.02  ? 409  VAL   B CB   1 
ATOM   2209 C  CG1  . VAL   B 2 23  ? -20.202 -5.317  6.413   1.00 30.57  ? 409  VAL   B CG1  1 
ATOM   2210 C  CG2  . VAL   B 2 23  ? -22.140 -5.927  4.893   1.00 31.85  ? 409  VAL   B CG2  1 
ATOM   2211 N  N    . THR   B 2 24  ? -23.927 -5.914  7.513   1.00 34.30  ? 410  THR   B N    1 
ATOM   2212 C  CA   . THR   B 2 24  ? -24.384 -6.968  8.408   1.00 30.41  ? 410  THR   B CA   1 
ATOM   2213 C  C    . THR   B 2 24  ? -24.846 -8.167  7.567   1.00 33.73  ? 410  THR   B C    1 
ATOM   2214 O  O    . THR   B 2 24  ? -24.680 -8.212  6.340   1.00 32.72  ? 410  THR   B O    1 
ATOM   2215 C  CB   . THR   B 2 24  ? -25.490 -6.439  9.339   1.00 31.63  ? 410  THR   B CB   1 
ATOM   2216 O  OG1  . THR   B 2 24  ? -25.812 -7.430  10.322  1.00 35.91  ? 410  THR   B OG1  1 
ATOM   2217 C  CG2  . THR   B 2 24  ? -26.759 -6.122  8.549   1.00 33.25  ? 410  THR   B CG2  1 
ATOM   2218 N  N    . LEU   B 2 25  ? -25.433 -9.149  8.241   1.00 30.06  ? 411  LEU   B N    1 
ATOM   2219 C  CA   . LEU   B 2 25  ? -25.874 -10.392 7.619   1.00 29.73  ? 411  LEU   B CA   1 
ATOM   2220 C  C    . LEU   B 2 25  ? -26.898 -11.032 8.542   1.00 31.71  ? 411  LEU   B C    1 
ATOM   2221 O  O    . LEU   B 2 25  ? -26.735 -10.987 9.762   1.00 30.43  ? 411  LEU   B O    1 
ATOM   2222 C  CB   . LEU   B 2 25  ? -24.685 -11.327 7.384   1.00 32.92  ? 411  LEU   B CB   1 
ATOM   2223 C  CG   . LEU   B 2 25  ? -24.962 -12.802 7.063   1.00 29.68  ? 411  LEU   B CG   1 
ATOM   2224 C  CD1  . LEU   B 2 25  ? -25.388 -12.908 5.619   1.00 32.38  ? 411  LEU   B CD1  1 
ATOM   2225 C  CD2  . LEU   B 2 25  ? -23.689 -13.611 7.300   1.00 34.43  ? 411  LEU   B CD2  1 
ATOM   2226 N  N    . GLU   B 2 26  ? -27.951 -11.615 7.965   1.00 30.51  ? 412  GLU   B N    1 
ATOM   2227 C  CA   . GLU   B 2 26  ? -29.006 -12.198 8.782   1.00 30.83  ? 412  GLU   B CA   1 
ATOM   2228 C  C    . GLU   B 2 26  ? -28.542 -13.506 9.416   1.00 34.29  ? 412  GLU   B C    1 
ATOM   2229 O  O    . GLU   B 2 26  ? -28.039 -14.399 8.729   1.00 28.61  ? 412  GLU   B O    1 
ATOM   2230 C  CB   . GLU   B 2 26  ? -30.263 -12.458 7.953   1.00 31.83  ? 412  GLU   B CB   1 
ATOM   2231 C  CG   . GLU   B 2 26  ? -31.396 -13.089 8.778   1.00 33.16  ? 412  GLU   B CG   1 
ATOM   2232 C  CD   . GLU   B 2 26  ? -32.715 -13.094 8.040   1.00 36.21  ? 412  GLU   B CD   1 
ATOM   2233 O  OE1  . GLU   B 2 26  ? -32.706 -13.227 6.795   1.00 38.22  ? 412  GLU   B OE1  1 
ATOM   2234 O  OE2  . GLU   B 2 26  ? -33.753 -12.911 8.702   1.00 38.87  ? 412  GLU   B OE2  1 
ATOM   2235 N  N    . GLU   B 2 27  ? -28.742 -13.621 10.730  1.00 28.98  ? 413  GLU   B N    1 
ATOM   2236 C  CA   . GLU   B 2 27  ? -28.508 -14.850 11.471  1.00 31.33  ? 413  GLU   B CA   1 
ATOM   2237 C  C    . GLU   B 2 27  ? -29.187 -14.698 12.819  1.00 33.14  ? 413  GLU   B C    1 
ATOM   2238 O  O    . GLU   B 2 27  ? -28.627 -14.065 13.723  1.00 33.96  ? 413  GLU   B O    1 
ATOM   2239 C  CB   . GLU   B 2 27  ? -27.018 -15.144 11.658  1.00 32.90  ? 413  GLU   B CB   1 
ATOM   2240 C  CG   . GLU   B 2 27  ? -26.796 -16.417 12.479  1.00 32.67  ? 413  GLU   B CG   1 
ATOM   2241 C  CD   . GLU   B 2 27  ? -25.537 -17.144 12.107  1.00 34.05  ? 413  GLU   B CD   1 
ATOM   2242 O  OE1  . GLU   B 2 27  ? -24.460 -16.505 12.070  1.00 35.84  ? 413  GLU   B OE1  1 
ATOM   2243 O  OE2  . GLU   B 2 27  ? -25.641 -18.363 11.831  1.00 32.67  ? 413  GLU   B OE2  1 
ATOM   2244 N  N    . ALA   B 2 28  ? -30.398 -15.238 12.960  1.00 30.31  ? 414  ALA   B N    1 
ATOM   2245 C  CA   . ALA   B 2 28  ? -31.143 -15.033 14.186  1.00 30.26  ? 414  ALA   B CA   1 
ATOM   2246 C  C    . ALA   B 2 28  ? -30.407 -15.711 15.339  1.00 32.18  ? 414  ALA   B C    1 
ATOM   2247 O  O    . ALA   B 2 28  ? -29.807 -16.774 15.157  1.00 31.48  ? 414  ALA   B O    1 
ATOM   2248 C  CB   . ALA   B 2 28  ? -32.563 -15.605 14.062  1.00 31.26  ? 414  ALA   B CB   1 
ATOM   2249 N  N    . PRO   B 2 29  ? -30.474 -15.148 16.549  1.00 31.90  ? 415  PRO   B N    1 
ATOM   2250 C  CA   . PRO   B 2 29  ? -31.232 -13.957 16.961  1.00 35.50  ? 415  PRO   B CA   1 
ATOM   2251 C  C    . PRO   B 2 29  ? -30.367 -12.722 16.942  1.00 34.45  ? 415  PRO   B C    1 
ATOM   2252 O  O    . PRO   B 2 29  ? -30.736 -11.699 17.518  1.00 35.79  ? 415  PRO   B O    1 
ATOM   2253 C  CB   . PRO   B 2 29  ? -31.643 -14.300 18.391  1.00 36.82  ? 415  PRO   B CB   1 
ATOM   2254 C  CG   . PRO   B 2 29  ? -30.426 -15.028 18.910  1.00 33.00  ? 415  PRO   B CG   1 
ATOM   2255 C  CD   . PRO   B 2 29  ? -29.862 -15.812 17.712  1.00 32.59  ? 415  PRO   B CD   1 
ATOM   2256 N  N    . PHE   B 2 30  ? -29.202 -12.799 16.295  1.00 29.03  ? 416  PHE   B N    1 
ATOM   2257 C  CA   . PHE   B 2 30  ? -28.270 -11.678 16.345  1.00 31.18  ? 416  PHE   B CA   1 
ATOM   2258 C  C    . PHE   B 2 30  ? -28.619 -10.618 15.323  1.00 29.17  ? 416  PHE   B C    1 
ATOM   2259 O  O    . PHE   B 2 30  ? -28.493 -9.425  15.603  1.00 32.58  ? 416  PHE   B O    1 
ATOM   2260 C  CB   . PHE   B 2 30  ? -26.847 -12.198 16.171  1.00 29.80  ? 416  PHE   B CB   1 
ATOM   2261 C  CG   . PHE   B 2 30  ? -26.477 -13.183 17.231  1.00 31.04  ? 416  PHE   B CG   1 
ATOM   2262 C  CD1  . PHE   B 2 30  ? -26.229 -12.738 18.520  1.00 31.57  ? 416  PHE   B CD1  1 
ATOM   2263 C  CD2  . PHE   B 2 30  ? -26.471 -14.539 16.977  1.00 30.20  ? 416  PHE   B CD2  1 
ATOM   2264 C  CE1  . PHE   B 2 30  ? -25.947 -13.625 19.530  1.00 31.85  ? 416  PHE   B CE1  1 
ATOM   2265 C  CE2  . PHE   B 2 30  ? -26.174 -15.440 17.986  1.00 33.32  ? 416  PHE   B CE2  1 
ATOM   2266 C  CZ   . PHE   B 2 30  ? -25.907 -14.970 19.264  1.00 30.92  ? 416  PHE   B CZ   1 
ATOM   2267 N  N    . VAL   B 2 31  ? -29.078 -11.030 14.145  1.00 31.56  ? 417  VAL   B N    1 
ATOM   2268 C  CA   . VAL   B 2 31  ? -29.563 -10.117 13.119  1.00 32.59  ? 417  VAL   B CA   1 
ATOM   2269 C  C    . VAL   B 2 31  ? -30.752 -10.791 12.449  1.00 32.97  ? 417  VAL   B C    1 
ATOM   2270 O  O    . VAL   B 2 31  ? -30.617 -11.897 11.910  1.00 34.29  ? 417  VAL   B O    1 
ATOM   2271 C  CB   . VAL   B 2 31  ? -28.483 -9.770  12.076  1.00 35.34  ? 417  VAL   B CB   1 
ATOM   2272 C  CG1  . VAL   B 2 31  ? -29.046 -8.820  11.025  1.00 33.13  ? 417  VAL   B CG1  1 
ATOM   2273 C  CG2  . VAL   B 2 31  ? -27.210 -9.175  12.734  1.00 31.48  ? 417  VAL   B CG2  1 
ATOM   2274 N  N    . ILE   B 2 32  ? -31.916 -10.140 12.503  1.00 31.68  ? 418  ILE   B N    1 
ATOM   2275 C  CA   . ILE   B 2 32  ? -33.164 -10.657 11.963  1.00 31.87  ? 418  ILE   B CA   1 
ATOM   2276 C  C    . ILE   B 2 32  ? -33.700 -9.646  10.955  1.00 37.88  ? 418  ILE   B C    1 
ATOM   2277 O  O    . ILE   B 2 32  ? -33.792 -8.454  11.261  1.00 36.80  ? 418  ILE   B O    1 
ATOM   2278 C  CB   . ILE   B 2 32  ? -34.189 -10.909 13.088  1.00 34.70  ? 418  ILE   B CB   1 
ATOM   2279 C  CG1  . ILE   B 2 32  ? -33.645 -11.986 14.067  1.00 34.84  ? 418  ILE   B CG1  1 
ATOM   2280 C  CG2  . ILE   B 2 32  ? -35.535 -11.299 12.503  1.00 36.88  ? 418  ILE   B CG2  1 
ATOM   2281 C  CD1  . ILE   B 2 32  ? -34.384 -12.064 15.413  1.00 34.70  ? 418  ILE   B CD1  1 
ATOM   2282 N  N    . VAL   B 2 33  ? -34.063 -10.114 9.764   1.00 35.63  ? 419  VAL   B N    1 
ATOM   2283 C  CA   . VAL   B 2 33  ? -34.492 -9.240  8.674   1.00 35.12  ? 419  VAL   B CA   1 
ATOM   2284 C  C    . VAL   B 2 33  ? -35.995 -9.392  8.493   1.00 37.85  ? 419  VAL   B C    1 
ATOM   2285 O  O    . VAL   B 2 33  ? -36.512 -10.514 8.470   1.00 38.42  ? 419  VAL   B O    1 
ATOM   2286 C  CB   . VAL   B 2 33  ? -33.734 -9.555  7.373   1.00 36.44  ? 419  VAL   B CB   1 
ATOM   2287 C  CG1  . VAL   B 2 33  ? -34.275 -8.732  6.211   1.00 41.30  ? 419  VAL   B CG1  1 
ATOM   2288 C  CG2  . VAL   B 2 33  ? -32.258 -9.250  7.557   1.00 34.47  ? 419  VAL   B CG2  1 
ATOM   2289 N  N    . GLU   B 2 34  ? -36.696 -8.266  8.392   1.00 39.94  ? 420  GLU   B N    1 
ATOM   2290 C  CA   . GLU   B 2 34  ? -38.121 -8.263  8.080   1.00 41.49  ? 420  GLU   B CA   1 
ATOM   2291 C  C    . GLU   B 2 34  ? -38.398 -7.311  6.926   1.00 43.79  ? 420  GLU   B C    1 
ATOM   2292 O  O    . GLU   B 2 34  ? -37.580 -6.450  6.598   1.00 40.22  ? 420  GLU   B O    1 
ATOM   2293 C  CB   . GLU   B 2 34  ? -38.954 -7.846  9.284   1.00 42.16  ? 420  GLU   B CB   1 
ATOM   2294 C  CG   . GLU   B 2 34  ? -38.649 -8.663  10.519  1.00 51.81  ? 420  GLU   B CG   1 
ATOM   2295 C  CD   . GLU   B 2 34  ? -39.452 -8.205  11.710  1.00 50.73  ? 420  GLU   B CD   1 
ATOM   2296 O  OE1  . GLU   B 2 34  ? -39.619 -6.974  11.862  1.00 50.42  ? 420  GLU   B OE1  1 
ATOM   2297 O  OE2  . GLU   B 2 34  ? -39.892 -9.075  12.493  1.00 57.28  ? 420  GLU   B OE2  1 
ATOM   2298 N  N    . ASP   B 2 35  ? -39.570 -7.480  6.312   1.00 44.73  ? 421  ASP   B N    1 
ATOM   2299 C  CA   . ASP   B 2 35  ? -40.057 -6.539  5.312   1.00 49.50  ? 421  ASP   B CA   1 
ATOM   2300 C  C    . ASP   B 2 35  ? -40.581 -5.272  5.980   1.00 51.54  ? 421  ASP   B C    1 
ATOM   2301 O  O    . ASP   B 2 35  ? -40.849 -5.232  7.184   1.00 51.01  ? 421  ASP   B O    1 
ATOM   2302 C  CB   . ASP   B 2 35  ? -41.172 -7.161  4.470   1.00 51.19  ? 421  ASP   B CB   1 
ATOM   2303 C  CG   . ASP   B 2 35  ? -40.711 -8.378  3.703   1.00 55.18  ? 421  ASP   B CG   1 
ATOM   2304 O  OD1  . ASP   B 2 35  ? -39.546 -8.381  3.254   1.00 56.59  ? 421  ASP   B OD1  1 
ATOM   2305 O  OD2  . ASP   B 2 35  ? -41.513 -9.323  3.540   1.00 63.23  ? 421  ASP   B OD2  1 
ATOM   2306 N  N    . ILE   B 2 36  ? -40.739 -4.223  5.185   1.00 45.22  ? 422  ILE   B N    1 
ATOM   2307 C  CA   . ILE   B 2 36  ? -41.465 -3.072  5.683   1.00 58.17  ? 422  ILE   B CA   1 
ATOM   2308 C  C    . ILE   B 2 36  ? -42.737 -2.894  4.845   1.00 56.10  ? 422  ILE   B C    1 
ATOM   2309 O  O    . ILE   B 2 36  ? -43.802 -2.541  5.364   1.00 70.38  ? 422  ILE   B O    1 
ATOM   2310 C  CB   . ILE   B 2 36  ? -40.593 -1.813  5.673   1.00 57.52  ? 422  ILE   B CB   1 
ATOM   2311 C  CG1  . ILE   B 2 36  ? -41.421 -0.606  6.101   1.00 65.71  ? 422  ILE   B CG1  1 
ATOM   2312 C  CG2  . ILE   B 2 36  ? -40.005 -1.586  4.296   1.00 52.15  ? 422  ILE   B CG2  1 
ATOM   2313 C  CD1  . ILE   B 2 36  ? -42.223 -0.851  7.364   1.00 64.39  ? 422  ILE   B CD1  1 
ATOM   2314 N  N    . GLU   B 2 41  ? -43.962 2.352   4.655   1.00 70.86  ? 427  GLU   B N    1 
ATOM   2315 C  CA   . GLU   B 2 41  ? -42.565 2.201   4.254   1.00 69.25  ? 427  GLU   B CA   1 
ATOM   2316 C  C    . GLU   B 2 41  ? -41.638 2.864   5.258   1.00 70.18  ? 427  GLU   B C    1 
ATOM   2317 O  O    . GLU   B 2 41  ? -40.714 3.580   4.884   1.00 74.42  ? 427  GLU   B O    1 
ATOM   2318 C  CB   . GLU   B 2 41  ? -42.326 2.793   2.863   1.00 67.98  ? 427  GLU   B CB   1 
ATOM   2319 N  N    . THR   B 2 42  ? -41.906 2.643   6.541   1.00 69.40  ? 428  THR   B N    1 
ATOM   2320 C  CA   . THR   B 2 42  ? -41.072 3.153   7.623   1.00 65.65  ? 428  THR   B CA   1 
ATOM   2321 C  C    . THR   B 2 42  ? -40.861 2.036   8.633   1.00 67.06  ? 428  THR   B C    1 
ATOM   2322 O  O    . THR   B 2 42  ? -41.831 1.488   9.162   1.00 71.52  ? 428  THR   B O    1 
ATOM   2323 C  CB   . THR   B 2 42  ? -41.710 4.371   8.303   1.00 70.80  ? 428  THR   B CB   1 
ATOM   2324 O  OG1  . THR   B 2 42  ? -42.619 3.931   9.322   1.00 70.68  ? 428  THR   B OG1  1 
ATOM   2325 C  CG2  . THR   B 2 42  ? -42.456 5.236   7.300   1.00 70.44  ? 428  THR   B CG2  1 
ATOM   2326 N  N    . CYS   B 2 43  ? -39.600 1.698   8.893   1.00 63.56  ? 429  CYS   B N    1 
ATOM   2327 C  CA   . CYS   B 2 43  ? -39.288 0.695   9.901   1.00 56.73  ? 429  CYS   B CA   1 
ATOM   2328 C  C    . CYS   B 2 43  ? -39.743 1.177   11.272  1.00 59.14  ? 429  CYS   B C    1 
ATOM   2329 O  O    . CYS   B 2 43  ? -39.522 2.334   11.639  1.00 61.49  ? 429  CYS   B O    1 
ATOM   2330 C  CB   . CYS   B 2 43  ? -37.789 0.420   9.913   1.00 51.05  ? 429  CYS   B CB   1 
ATOM   2331 S  SG   . CYS   B 2 43  ? -37.171 -0.315  8.384   1.00 48.27  ? 429  CYS   B SG   1 
ATOM   2332 N  N    . VAL   B 2 44  ? -40.369 0.284   12.037  1.00 57.50  ? 430  VAL   B N    1 
ATOM   2333 C  CA   . VAL   B 2 44  ? -40.969 0.655   13.316  1.00 63.08  ? 430  VAL   B CA   1 
ATOM   2334 C  C    . VAL   B 2 44  ? -40.404 -0.191  14.448  1.00 58.39  ? 430  VAL   B C    1 
ATOM   2335 O  O    . VAL   B 2 44  ? -39.499 -1.008  14.239  1.00 57.28  ? 430  VAL   B O    1 
ATOM   2336 C  CB   . VAL   B 2 44  ? -42.506 0.536   13.264  1.00 61.27  ? 430  VAL   B CB   1 
ATOM   2337 C  CG1  . VAL   B 2 44  ? -43.065 1.302   12.079  1.00 66.57  ? 430  VAL   B CG1  1 
ATOM   2338 C  CG2  . VAL   B 2 44  ? -42.920 -0.929  13.171  1.00 64.54  ? 430  VAL   B CG2  1 
ATOM   2339 N  N    . ARG   B 2 45  ? -40.922 0.025   15.655  1.00 60.20  ? 431  ARG   B N    1 
ATOM   2340 C  CA   . ARG   B 2 45  ? -40.656 -0.804  16.843  1.00 63.24  ? 431  ARG   B CA   1 
ATOM   2341 C  C    . ARG   B 2 45  ? -39.148 -0.858  17.082  1.00 59.09  ? 431  ARG   B C    1 
ATOM   2342 O  O    . ARG   B 2 45  ? -38.483 0.189   17.054  1.00 56.41  ? 431  ARG   B O    1 
ATOM   2343 C  CB   . ARG   B 2 45  ? -41.345 -2.156  16.672  1.00 66.49  ? 431  ARG   B CB   1 
ATOM   2344 C  CG   . ARG   B 2 45  ? -42.862 -2.119  16.891  1.00 69.84  ? 431  ARG   B CG   1 
ATOM   2345 C  CD   . ARG   B 2 45  ? -43.359 -3.380  17.602  1.00 73.67  ? 431  ARG   B CD   1 
ATOM   2346 N  NE   . ARG   B 2 45  ? -44.411 -4.082  16.871  1.00 77.98  ? 431  ARG   B NE   1 
ATOM   2347 C  CZ   . ARG   B 2 45  ? -45.139 -5.074  17.374  1.00 74.94  ? 431  ARG   B CZ   1 
ATOM   2348 N  NH1  . ARG   B 2 45  ? -44.960 -5.505  18.614  1.00 71.51  ? 431  ARG   B NH1  1 
ATOM   2349 N  NH2  . ARG   B 2 45  ? -46.076 -5.643  16.620  1.00 74.01  ? 431  ARG   B NH2  1 
ATOM   2350 N  N    . ASN   B 2 46  ? -38.563 -2.027  17.337  1.00 63.34  ? 432  ASN   B N    1 
ATOM   2351 C  CA   . ASN   B 2 46  ? -37.143 -2.122  17.640  1.00 61.07  ? 432  ASN   B CA   1 
ATOM   2352 C  C    . ASN   B 2 46  ? -36.296 -2.366  16.397  1.00 58.14  ? 432  ASN   B C    1 
ATOM   2353 O  O    . ASN   B 2 46  ? -35.166 -2.854  16.523  1.00 54.86  ? 432  ASN   B O    1 
ATOM   2354 C  CB   . ASN   B 2 46  ? -36.892 -3.227  18.675  1.00 64.72  ? 432  ASN   B CB   1 
ATOM   2355 C  CG   . ASN   B 2 46  ? -37.654 -4.516  18.370  1.00 68.03  ? 432  ASN   B CG   1 
ATOM   2356 O  OD1  . ASN   B 2 46  ? -38.543 -4.545  17.515  1.00 71.75  ? 432  ASN   B OD1  1 
ATOM   2357 N  ND2  . ASN   B 2 46  ? -37.320 -5.585  19.091  1.00 60.82  ? 432  ASN   B ND2  1 
ATOM   2358 N  N    . THR   B 2 47  ? -36.811 -2.038  15.209  1.00 53.57  ? 433  THR   B N    1 
ATOM   2359 C  CA   . THR   B 2 47  ? -36.110 -2.272  13.953  1.00 47.99  ? 433  THR   B CA   1 
ATOM   2360 C  C    . THR   B 2 47  ? -35.400 -1.008  13.473  1.00 47.98  ? 433  THR   B C    1 
ATOM   2361 O  O    . THR   B 2 47  ? -35.739 0.115   13.850  1.00 46.93  ? 433  THR   B O    1 
ATOM   2362 C  CB   . THR   B 2 47  ? -37.061 -2.768  12.856  1.00 44.02  ? 433  THR   B CB   1 
ATOM   2363 O  OG1  . THR   B 2 47  ? -37.831 -1.675  12.345  1.00 55.44  ? 433  THR   B OG1  1 
ATOM   2364 C  CG2  . THR   B 2 47  ? -38.008 -3.853  13.376  1.00 45.21  ? 433  THR   B CG2  1 
ATOM   2365 N  N    . VAL   B 2 48  ? -34.385 -1.212  12.639  1.00 42.79  ? 434  VAL   B N    1 
ATOM   2366 C  CA   . VAL   B 2 48  ? -33.641 -0.117  12.019  1.00 40.79  ? 434  VAL   B CA   1 
ATOM   2367 C  C    . VAL   B 2 48  ? -33.583 -0.394  10.523  1.00 41.33  ? 434  VAL   B C    1 
ATOM   2368 O  O    . VAL   B 2 48  ? -33.554 -1.568  10.118  1.00 40.17  ? 434  VAL   B O    1 
ATOM   2369 C  CB   . VAL   B 2 48  ? -32.235 0.025   12.623  1.00 42.62  ? 434  VAL   B CB   1 
ATOM   2370 C  CG1  . VAL   B 2 48  ? -32.328 0.171   14.121  1.00 44.52  ? 434  VAL   B CG1  1 
ATOM   2371 C  CG2  . VAL   B 2 48  ? -31.322 -1.149  12.221  1.00 39.57  ? 434  VAL   B CG2  1 
ATOM   2372 N  N    . PRO   B 2 49  ? -33.590 0.629   9.673   1.00 40.95  ? 435  PRO   B N    1 
ATOM   2373 C  CA   . PRO   B 2 49  ? -33.573 0.374   8.230   1.00 39.58  ? 435  PRO   B CA   1 
ATOM   2374 C  C    . PRO   B 2 49  ? -32.265 -0.267  7.787   1.00 42.81  ? 435  PRO   B C    1 
ATOM   2375 O  O    . PRO   B 2 49  ? -31.179 0.053   8.278   1.00 40.73  ? 435  PRO   B O    1 
ATOM   2376 C  CB   . PRO   B 2 49  ? -33.771 1.769   7.613   1.00 46.64  ? 435  PRO   B CB   1 
ATOM   2377 C  CG   . PRO   B 2 49  ? -33.423 2.727   8.703   1.00 44.59  ? 435  PRO   B CG   1 
ATOM   2378 C  CD   . PRO   B 2 49  ? -33.779 2.058   9.986   1.00 41.21  ? 435  PRO   B CD   1 
ATOM   2379 N  N    . CYS   B 2 50  ? -32.393 -1.234  6.891   1.00 39.42  ? 436  CYS   B N    1 
ATOM   2380 C  CA   . CYS   B 2 50  ? -31.254 -1.891  6.278   1.00 38.68  ? 436  CYS   B CA   1 
ATOM   2381 C  C    . CYS   B 2 50  ? -31.632 -2.207  4.845   1.00 40.77  ? 436  CYS   B C    1 
ATOM   2382 O  O    . CYS   B 2 50  ? -32.771 -2.587  4.571   1.00 42.80  ? 436  CYS   B O    1 
ATOM   2383 C  CB   . CYS   B 2 50  ? -30.858 -3.163  7.042   1.00 38.14  ? 436  CYS   B CB   1 
ATOM   2384 S  SG   . CYS   B 2 50  ? -32.207 -4.359  7.415   1.00 44.95  ? 436  CYS   B SG   1 
ATOM   2385 N  N    . ARG   B 2 51  ? -30.693 -2.035  3.930   1.00 39.69  ? 437  ARG   B N    1 
ATOM   2386 C  CA   . ARG   B 2 51  ? -30.966 -2.270  2.521   1.00 39.49  ? 437  ARG   B CA   1 
ATOM   2387 C  C    . ARG   B 2 51  ? -30.295 -3.560  2.070   1.00 37.53  ? 437  ARG   B C    1 
ATOM   2388 O  O    . ARG   B 2 51  ? -29.309 -4.005  2.659   1.00 38.07  ? 437  ARG   B O    1 
ATOM   2389 C  CB   . ARG   B 2 51  ? -30.509 -1.085  1.656   1.00 42.76  ? 437  ARG   B CB   1 
ATOM   2390 C  CG   . ARG   B 2 51  ? -29.102 -0.587  1.943   1.00 46.46  ? 437  ARG   B CG   1 
ATOM   2391 C  CD   . ARG   B 2 51  ? -28.755 0.697   1.172   1.00 51.11  ? 437  ARG   B CD   1 
ATOM   2392 N  NE   . ARG   B 2 51  ? -27.444 1.214   1.562   1.00 50.68  ? 437  ARG   B NE   1 
ATOM   2393 C  CZ   . ARG   B 2 51  ? -26.296 0.862   0.999   1.00 52.09  ? 437  ARG   B CZ   1 
ATOM   2394 N  NH1  . ARG   B 2 51  ? -26.249 -0.018  0.010   1.00 46.72  ? 437  ARG   B NH1  1 
ATOM   2395 N  NH2  . ARG   B 2 51  ? -25.162 1.387   1.457   1.00 50.43  ? 437  ARG   B NH2  1 
ATOM   2396 N  N    . LYS   B 2 52  ? -30.875 -4.174  1.043   1.00 36.33  ? 438  LYS   B N    1 
ATOM   2397 C  CA   . LYS   B 2 52  ? -30.365 -5.398  0.438   1.00 34.26  ? 438  LYS   B CA   1 
ATOM   2398 C  C    . LYS   B 2 52  ? -30.415 -5.222  -1.071  1.00 38.37  ? 438  LYS   B C    1 
ATOM   2399 O  O    . LYS   B 2 52  ? -31.470 -4.898  -1.631  1.00 37.48  ? 438  LYS   B O    1 
ATOM   2400 C  CB   . LYS   B 2 52  ? -31.170 -6.633  0.872   1.00 36.57  ? 438  LYS   B CB   1 
ATOM   2401 C  CG   . LYS   B 2 52  ? -30.770 -7.915  0.138   1.00 39.93  ? 438  LYS   B CG   1 
ATOM   2402 C  CD   . LYS   B 2 52  ? -31.176 -9.201  0.879   1.00 47.04  ? 438  LYS   B CD   1 
ATOM   2403 C  CE   . LYS   B 2 52  ? -32.688 -9.386  0.966   1.00 55.85  ? 438  LYS   B CE   1 
ATOM   2404 N  NZ   . LYS   B 2 52  ? -33.057 -10.680 1.667   1.00 54.43  ? 438  LYS   B NZ   1 
ATOM   2405 N  N    . PHE   B 2 53  ? -29.261 -5.362  -1.703  1.00 34.36  ? 439  PHE   B N    1 
ATOM   2406 C  CA   . PHE   B 2 53  ? -29.133 -5.274  -3.148  1.00 36.56  ? 439  PHE   B CA   1 
ATOM   2407 C  C    . PHE   B 2 53  ? -29.656 -6.563  -3.759  1.00 35.36  ? 439  PHE   B C    1 
ATOM   2408 O  O    . PHE   B 2 53  ? -29.132 -7.643  -3.468  1.00 33.79  ? 439  PHE   B O    1 
ATOM   2409 C  CB   . PHE   B 2 53  ? -27.666 -5.047  -3.510  1.00 40.70  ? 439  PHE   B CB   1 
ATOM   2410 C  CG   . PHE   B 2 53  ? -27.424 -4.832  -4.970  1.00 43.77  ? 439  PHE   B CG   1 
ATOM   2411 C  CD1  . PHE   B 2 53  ? -27.624 -3.592  -5.538  1.00 41.65  ? 439  PHE   B CD1  1 
ATOM   2412 C  CD2  . PHE   B 2 53  ? -26.975 -5.875  -5.771  1.00 44.81  ? 439  PHE   B CD2  1 
ATOM   2413 C  CE1  . PHE   B 2 53  ? -27.404 -3.390  -6.885  1.00 47.26  ? 439  PHE   B CE1  1 
ATOM   2414 C  CE2  . PHE   B 2 53  ? -26.742 -5.677  -7.113  1.00 45.21  ? 439  PHE   B CE2  1 
ATOM   2415 C  CZ   . PHE   B 2 53  ? -26.948 -4.433  -7.667  1.00 45.46  ? 439  PHE   B CZ   1 
ATOM   2416 N  N    . VAL   B 2 54  ? -30.695 -6.460  -4.581  1.00 36.12  ? 440  VAL   B N    1 
ATOM   2417 C  CA   . VAL   B 2 54  ? -31.337 -7.620  -5.188  1.00 34.49  ? 440  VAL   B CA   1 
ATOM   2418 C  C    . VAL   B 2 54  ? -31.188 -7.514  -6.706  1.00 36.18  ? 440  VAL   B C    1 
ATOM   2419 O  O    . VAL   B 2 54  ? -31.530 -6.482  -7.298  1.00 31.89  ? 440  VAL   B O    1 
ATOM   2420 C  CB   . VAL   B 2 54  ? -32.818 -7.718  -4.767  1.00 31.56  ? 440  VAL   B CB   1 
ATOM   2421 C  CG1  . VAL   B 2 54  ? -33.450 -8.954  -5.376  1.00 33.10  ? 440  VAL   B CG1  1 
ATOM   2422 C  CG2  . VAL   B 2 54  ? -32.929 -7.784  -3.242  1.00 35.99  ? 440  VAL   B CG2  1 
ATOM   2423 N  N    . LYS   B 2 55  ? -30.669 -8.571  -7.329  1.00 34.23  ? 441  LYS   B N    1 
ATOM   2424 C  CA   . LYS   B 2 55  ? -30.390 -8.531  -8.763  1.00 33.63  ? 441  LYS   B CA   1 
ATOM   2425 C  C    . LYS   B 2 55  ? -31.674 -8.597  -9.574  1.00 36.59  ? 441  LYS   B C    1 
ATOM   2426 O  O    . LYS   B 2 55  ? -32.662 -9.215  -9.169  1.00 30.27  ? 441  LYS   B O    1 
ATOM   2427 C  CB   . LYS   B 2 55  ? -29.465 -9.684  -9.169  1.00 39.77  ? 441  LYS   B CB   1 
ATOM   2428 C  CG   . LYS   B 2 55  ? -27.988 -9.414  -8.844  1.00 45.22  ? 441  LYS   B CG   1 
ATOM   2429 C  CD   . LYS   B 2 55  ? -27.433 -10.417 -7.852  1.00 53.59  ? 441  LYS   B CD   1 
ATOM   2430 C  CE   . LYS   B 2 55  ? -26.049 -9.993  -7.332  1.00 61.04  ? 441  LYS   B CE   1 
ATOM   2431 N  NZ   . LYS   B 2 55  ? -25.881 -10.322 -5.881  1.00 54.36  ? 441  LYS   B NZ   1 
ATOM   2432 N  N    . ILE   B 2 56  ? -31.657 -7.945  -10.739 1.00 32.31  ? 442  ILE   B N    1 
ATOM   2433 C  CA   . ILE   B 2 56  ? -32.821 -8.000  -11.612 1.00 38.01  ? 442  ILE   B CA   1 
ATOM   2434 C  C    . ILE   B 2 56  ? -32.900 -9.362  -12.295 1.00 38.80  ? 442  ILE   B C    1 
ATOM   2435 O  O    . ILE   B 2 56  ? -33.977 -9.966  -12.400 1.00 34.62  ? 442  ILE   B O    1 
ATOM   2436 C  CB   . ILE   B 2 56  ? -32.778 -6.858  -12.641 1.00 38.85  ? 442  ILE   B CB   1 
ATOM   2437 C  CG1  . ILE   B 2 56  ? -32.793 -5.502  -11.929 1.00 42.73  ? 442  ILE   B CG1  1 
ATOM   2438 C  CG2  . ILE   B 2 56  ? -33.965 -6.959  -13.573 1.00 40.93  ? 442  ILE   B CG2  1 
ATOM   2439 C  CD1  . ILE   B 2 56  ? -33.974 -5.328  -10.998 1.00 38.99  ? 442  ILE   B CD1  1 
ATOM   2440 N  N    . ASN   B 2 57  ? -31.768 -9.843  -12.801 1.00 37.85  ? 443  ASN   B N    1 
ATOM   2441 C  CA   . ASN   B 2 57  ? -31.685 -11.155 -13.433 1.00 38.75  ? 443  ASN   B CA   1 
ATOM   2442 C  C    . ASN   B 2 57  ? -30.223 -11.597 -13.424 1.00 49.86  ? 443  ASN   B C    1 
ATOM   2443 O  O    . ASN   B 2 57  ? -29.338 -10.884 -12.936 1.00 47.33  ? 443  ASN   B O    1 
ATOM   2444 C  CB   . ASN   B 2 57  ? -32.288 -11.141 -14.844 1.00 43.71  ? 443  ASN   B CB   1 
ATOM   2445 C  CG   . ASN   B 2 57  ? -31.565 -10.204 -15.789 1.00 51.11  ? 443  ASN   B CG   1 
ATOM   2446 O  OD1  . ASN   B 2 57  ? -30.430 -10.468 -16.180 1.00 57.16  ? 443  ASN   B OD1  1 
ATOM   2447 N  ND2  . ASN   B 2 57  ? -32.253 -9.158  -16.240 1.00 50.85  ? 443  ASN   B ND2  1 
ATOM   2448 N  N    . ASN   B 2 58  ? -29.975 -12.794 -13.951 1.00 52.53  ? 444  ASN   B N    1 
ATOM   2449 C  CA   . ASN   B 2 58  ? -28.647 -13.393 -13.914 1.00 47.57  ? 444  ASN   B CA   1 
ATOM   2450 C  C    . ASN   B 2 58  ? -27.861 -13.176 -15.191 1.00 49.53  ? 444  ASN   B C    1 
ATOM   2451 O  O    . ASN   B 2 58  ? -26.706 -13.600 -15.279 1.00 53.48  ? 444  ASN   B O    1 
ATOM   2452 C  CB   . ASN   B 2 58  ? -28.766 -14.877 -13.616 1.00 47.59  ? 444  ASN   B CB   1 
ATOM   2453 C  CG   . ASN   B 2 58  ? -29.353 -15.122 -12.260 1.00 49.64  ? 444  ASN   B CG   1 
ATOM   2454 O  OD1  . ASN   B 2 58  ? -29.068 -14.379 -11.318 1.00 49.37  ? 444  ASN   B OD1  1 
ATOM   2455 N  ND2  . ASN   B 2 58  ? -30.199 -16.144 -12.145 1.00 45.76  ? 444  ASN   B ND2  1 
ATOM   2456 N  N    . SER   B 2 59  ? -28.452 -12.516 -16.173 1.00 51.17  ? 445  SER   B N    1 
ATOM   2457 C  CA   . SER   B 2 59  ? -27.732 -12.079 -17.352 1.00 57.04  ? 445  SER   B CA   1 
ATOM   2458 C  C    . SER   B 2 59  ? -27.364 -10.604 -17.271 1.00 60.74  ? 445  SER   B C    1 
ATOM   2459 O  O    . SER   B 2 59  ? -27.086 -9.983  -18.303 1.00 62.72  ? 445  SER   B O    1 
ATOM   2460 C  CB   . SER   B 2 59  ? -28.566 -12.369 -18.601 1.00 59.74  ? 445  SER   B CB   1 
ATOM   2461 O  OG   . SER   B 2 59  ? -29.813 -11.701 -18.543 1.00 62.15  ? 445  SER   B OG   1 
ATOM   2462 N  N    . THR   B 2 60  ? -27.362 -10.028 -16.064 1.00 56.91  ? 446  THR   B N    1 
ATOM   2463 C  CA   . THR   B 2 60  ? -27.077 -8.611  -15.913 1.00 53.15  ? 446  THR   B CA   1 
ATOM   2464 C  C    . THR   B 2 60  ? -26.382 -8.355  -14.584 1.00 52.27  ? 446  THR   B C    1 
ATOM   2465 O  O    . THR   B 2 60  ? -26.416 -9.178  -13.667 1.00 48.19  ? 446  THR   B O    1 
ATOM   2466 C  CB   . THR   B 2 60  ? -28.353 -7.754  -16.042 1.00 57.26  ? 446  THR   B CB   1 
ATOM   2467 O  OG1  . THR   B 2 60  ? -27.998 -6.369  -16.140 1.00 58.91  ? 446  THR   B OG1  1 
ATOM   2468 C  CG2  . THR   B 2 60  ? -29.251 -7.922  -14.823 1.00 52.79  ? 446  THR   B CG2  1 
ATOM   2469 N  N    . ASN   B 2 61  ? -25.716 -7.203  -14.505 1.00 53.97  ? 447  ASN   B N    1 
ATOM   2470 C  CA   . ASN   B 2 61  ? -25.178 -6.691  -13.250 1.00 50.74  ? 447  ASN   B CA   1 
ATOM   2471 C  C    . ASN   B 2 61  ? -26.139 -5.737  -12.566 1.00 48.62  ? 447  ASN   B C    1 
ATOM   2472 O  O    . ASN   B 2 61  ? -25.864 -5.282  -11.447 1.00 51.05  ? 447  ASN   B O    1 
ATOM   2473 C  CB   . ASN   B 2 61  ? -23.848 -5.977  -13.491 1.00 47.79  ? 447  ASN   B CB   1 
ATOM   2474 C  CG   . ASN   B 2 61  ? -22.778 -6.905  -14.007 1.00 52.24  ? 447  ASN   B CG   1 
ATOM   2475 O  OD1  . ASN   B 2 61  ? -22.593 -8.002  -13.480 1.00 48.39  ? 447  ASN   B OD1  1 
ATOM   2476 N  ND2  . ASN   B 2 61  ? -22.071 -6.477  -15.055 1.00 46.21  ? 447  ASN   B ND2  1 
ATOM   2477 N  N    . GLU   B 2 62  ? -27.245 -5.425  -13.225 1.00 44.14  ? 448  GLU   B N    1 
ATOM   2478 C  CA   . GLU   B 2 62  ? -28.202 -4.465  -12.713 1.00 47.48  ? 448  GLU   B CA   1 
ATOM   2479 C  C    . GLU   B 2 62  ? -28.914 -5.051  -11.498 1.00 43.56  ? 448  GLU   B C    1 
ATOM   2480 O  O    . GLU   B 2 62  ? -29.236 -6.240  -11.459 1.00 41.58  ? 448  GLU   B O    1 
ATOM   2481 C  CB   . GLU   B 2 62  ? -29.176 -4.087  -13.837 1.00 46.86  ? 448  GLU   B CB   1 
ATOM   2482 C  CG   . GLU   B 2 62  ? -30.439 -3.342  -13.429 1.00 52.94  ? 448  GLU   B CG   1 
ATOM   2483 C  CD   . GLU   B 2 62  ? -31.304 -2.900  -14.621 1.00 59.17  ? 448  GLU   B CD   1 
ATOM   2484 O  OE1  . GLU   B 2 62  ? -32.011 -1.876  -14.488 1.00 60.17  ? 448  GLU   B OE1  1 
ATOM   2485 O  OE2  . GLU   B 2 62  ? -31.280 -3.555  -15.690 1.00 65.04  ? 448  GLU   B OE2  1 
ATOM   2486 N  N    . GLY   B 2 63  ? -29.101 -4.222  -10.474 1.00 43.17  ? 449  GLY   B N    1 
ATOM   2487 C  CA   . GLY   B 2 63  ? -29.822 -4.626  -9.284  1.00 40.57  ? 449  GLY   B CA   1 
ATOM   2488 C  C    . GLY   B 2 63  ? -30.567 -3.432  -8.728  1.00 42.83  ? 449  GLY   B C    1 
ATOM   2489 O  O    . GLY   B 2 63  ? -30.483 -2.326  -9.268  1.00 41.22  ? 449  GLY   B O    1 
ATOM   2490 N  N    . MET   B 2 64  ? -31.319 -3.666  -7.651  1.00 39.55  ? 450  MET   B N    1 
ATOM   2491 C  CA   . MET   B 2 64  ? -32.071 -2.612  -6.974  1.00 41.58  ? 450  MET   B CA   1 
ATOM   2492 C  C    . MET   B 2 64  ? -31.917 -2.782  -5.474  1.00 42.24  ? 450  MET   B C    1 
ATOM   2493 O  O    . MET   B 2 64  ? -31.895 -3.910  -4.977  1.00 39.76  ? 450  MET   B O    1 
ATOM   2494 C  CB   . MET   B 2 64  ? -33.542 -2.655  -7.375  1.00 44.78  ? 450  MET   B CB   1 
ATOM   2495 C  CG   . MET   B 2 64  ? -33.766 -2.028  -8.752  1.00 51.04  ? 450  MET   B CG   1 
ATOM   2496 S  SD   . MET   B 2 64  ? -35.191 -0.982  -8.813  1.00 64.19  ? 450  MET   B SD   1 
ATOM   2497 C  CE   . MET   B 2 64  ? -34.768 0.080   -7.446  1.00 59.55  ? 450  MET   B CE   1 
ATOM   2498 N  N    . ASN   B 2 65  ? -31.762 -1.669  -4.754  1.00 41.71  ? 451  ASN   B N    1 
ATOM   2499 C  CA   . ASN   B 2 65  ? -31.654 -1.724  -3.295  1.00 43.84  ? 451  ASN   B CA   1 
ATOM   2500 C  C    . ASN   B 2 65  ? -33.046 -1.824  -2.698  1.00 48.00  ? 451  ASN   B C    1 
ATOM   2501 O  O    . ASN   B 2 65  ? -33.821 -0.865  -2.749  1.00 54.07  ? 451  ASN   B O    1 
ATOM   2502 C  CB   . ASN   B 2 65  ? -30.928 -0.504  -2.737  1.00 50.10  ? 451  ASN   B CB   1 
ATOM   2503 C  CG   . ASN   B 2 65  ? -29.453 -0.526  -3.021  1.00 48.13  ? 451  ASN   B CG   1 
ATOM   2504 O  OD1  . ASN   B 2 65  ? -28.793 -1.556  -2.866  1.00 47.32  ? 451  ASN   B OD1  1 
ATOM   2505 N  ND2  . ASN   B 2 65  ? -28.924 0.602   -3.469  1.00 55.97  ? 451  ASN   B ND2  1 
ATOM   2506 N  N    . VAL   B 2 66  ? -33.360 -2.969  -2.117  1.00 41.35  ? 452  VAL   B N    1 
ATOM   2507 C  CA   . VAL   B 2 66  ? -34.637 -3.144  -1.445  1.00 40.94  ? 452  VAL   B CA   1 
ATOM   2508 C  C    . VAL   B 2 66  ? -34.532 -2.640  -0.016  1.00 45.00  ? 452  VAL   B C    1 
ATOM   2509 O  O    . VAL   B 2 66  ? -33.579 -2.967  0.704   1.00 40.31  ? 452  VAL   B O    1 
ATOM   2510 C  CB   . VAL   B 2 66  ? -35.073 -4.611  -1.485  1.00 41.37  ? 452  VAL   B CB   1 
ATOM   2511 C  CG1  . VAL   B 2 66  ? -36.367 -4.787  -0.704  1.00 41.64  ? 452  VAL   B CG1  1 
ATOM   2512 C  CG2  . VAL   B 2 66  ? -35.272 -5.031  -2.929  1.00 43.21  ? 452  VAL   B CG2  1 
ATOM   2513 N  N    . LYS   B 2 67  ? -35.522 -1.859  0.406   1.00 39.81  ? 453  LYS   B N    1 
ATOM   2514 C  CA   . LYS   B 2 67  ? -35.539 -1.341  1.764   1.00 41.91  ? 453  LYS   B CA   1 
ATOM   2515 C  C    . LYS   B 2 67  ? -36.183 -2.379  2.671   1.00 45.73  ? 453  LYS   B C    1 
ATOM   2516 O  O    . LYS   B 2 67  ? -37.335 -2.776  2.454   1.00 46.08  ? 453  LYS   B O    1 
ATOM   2517 C  CB   . LYS   B 2 67  ? -36.288 -0.010  1.826   1.00 38.37  ? 453  LYS   B CB   1 
ATOM   2518 N  N    . LYS   B 2 68  ? -35.431 -2.838  3.673   1.00 39.07  ? 454  LYS   B N    1 
ATOM   2519 C  CA   . LYS   B 2 68  ? -35.982 -3.743  4.669   1.00 40.05  ? 454  LYS   B CA   1 
ATOM   2520 C  C    . LYS   B 2 68  ? -35.682 -3.201  6.059   1.00 42.37  ? 454  LYS   B C    1 
ATOM   2521 O  O    . LYS   B 2 68  ? -35.167 -2.085  6.197   1.00 40.17  ? 454  LYS   B O    1 
ATOM   2522 C  CB   . LYS   B 2 68  ? -35.418 -5.164  4.503   1.00 43.69  ? 454  LYS   B CB   1 
ATOM   2523 C  CG   . LYS   B 2 68  ? -35.180 -5.568  3.045   1.00 45.77  ? 454  LYS   B CG   1 
ATOM   2524 C  CD   . LYS   B 2 68  ? -34.959 -7.057  2.884   1.00 49.27  ? 454  LYS   B CD   1 
ATOM   2525 C  CE   . LYS   B 2 68  ? -36.261 -7.833  3.079   1.00 49.85  ? 454  LYS   B CE   1 
ATOM   2526 N  NZ   . LYS   B 2 68  ? -37.303 -7.487  2.076   1.00 51.91  ? 454  LYS   B NZ   1 
ATOM   2527 N  N    . CYS   B 2 69  ? -35.990 -3.991  7.087   1.00 38.96  ? 455  CYS   B N    1 
ATOM   2528 C  CA   . CYS   B 2 69  ? -35.823 -3.601  8.477   1.00 38.20  ? 455  CYS   B CA   1 
ATOM   2529 C  C    . CYS   B 2 69  ? -35.108 -4.716  9.225   1.00 37.96  ? 455  CYS   B C    1 
ATOM   2530 O  O    . CYS   B 2 69  ? -35.386 -5.898  9.009   1.00 38.45  ? 455  CYS   B O    1 
ATOM   2531 C  CB   . CYS   B 2 69  ? -37.183 -3.278  9.126   1.00 41.95  ? 455  CYS   B CB   1 
ATOM   2532 S  SG   . CYS   B 2 69  ? -38.214 -2.071  8.192   1.00 49.00  ? 455  CYS   B SG   1 
ATOM   2533 N  N    . CYS   B 2 70  ? -34.172 -4.328  10.088  1.00 34.67  ? 456  CYS   B N    1 
ATOM   2534 C  CA   . CYS   B 2 70  ? -33.300 -5.237  10.807  1.00 37.58  ? 456  CYS   B CA   1 
ATOM   2535 C  C    . CYS   B 2 70  ? -33.495 -5.064  12.304  1.00 39.55  ? 456  CYS   B C    1 
ATOM   2536 O  O    . CYS   B 2 70  ? -33.601 -3.937  12.798  1.00 40.21  ? 456  CYS   B O    1 
ATOM   2537 C  CB   . CYS   B 2 70  ? -31.828 -4.975  10.439  1.00 35.38  ? 456  CYS   B CB   1 
ATOM   2538 S  SG   . CYS   B 2 70  ? -31.371 -5.620  8.812   1.00 44.08  ? 456  CYS   B SG   1 
ATOM   2539 N  N    . LYS   B 2 71  ? -33.505 -6.181  13.028  1.00 37.58  ? 457  LYS   B N    1 
ATOM   2540 C  CA   . LYS   B 2 71  ? -33.532 -6.161  14.485  1.00 38.78  ? 457  LYS   B CA   1 
ATOM   2541 C  C    . LYS   B 2 71  ? -32.710 -7.338  14.999  1.00 39.05  ? 457  LYS   B C    1 
ATOM   2542 O  O    . LYS   B 2 71  ? -32.272 -8.196  14.233  1.00 35.06  ? 457  LYS   B O    1 
ATOM   2543 C  CB   . LYS   B 2 71  ? -34.968 -6.229  15.020  1.00 39.90  ? 457  LYS   B CB   1 
ATOM   2544 C  CG   . LYS   B 2 71  ? -35.629 -7.578  14.776  1.00 39.24  ? 457  LYS   B CG   1 
ATOM   2545 C  CD   . LYS   B 2 71  ? -37.115 -7.571  15.148  1.00 43.74  ? 457  LYS   B CD   1 
ATOM   2546 C  CE   . LYS   B 2 71  ? -37.742 -8.944  14.942  1.00 46.49  ? 457  LYS   B CE   1 
ATOM   2547 N  NZ   . LYS   B 2 71  ? -39.213 -8.972  15.308  1.00 44.18  ? 457  LYS   B NZ   1 
ATOM   2548 N  N    . GLY   B 2 72  ? -32.494 -7.368  16.309  1.00 38.37  ? 458  GLY   B N    1 
ATOM   2549 C  CA   . GLY   B 2 72  ? -31.817 -8.461  16.962  1.00 36.22  ? 458  GLY   B CA   1 
ATOM   2550 C  C    . GLY   B 2 72  ? -30.736 -7.978  17.905  1.00 38.70  ? 458  GLY   B C    1 
ATOM   2551 O  O    . GLY   B 2 72  ? -30.467 -6.786  18.035  1.00 33.40  ? 458  GLY   B O    1 
ATOM   2552 N  N    . PHE   B 2 73  ? -30.103 -8.949  18.572  1.00 35.80  ? 459  PHE   B N    1 
ATOM   2553 C  CA   . PHE   B 2 73  ? -29.099 -8.641  19.591  1.00 32.73  ? 459  PHE   B CA   1 
ATOM   2554 C  C    . PHE   B 2 73  ? -28.012 -7.717  19.045  1.00 35.25  ? 459  PHE   B C    1 
ATOM   2555 O  O    . PHE   B 2 73  ? -27.682 -6.698  19.663  1.00 32.51  ? 459  PHE   B O    1 
ATOM   2556 C  CB   . PHE   B 2 73  ? -28.483 -9.945  20.124  1.00 34.21  ? 459  PHE   B CB   1 
ATOM   2557 C  CG   . PHE   B 2 73  ? -27.436 -9.744  21.194  1.00 33.96  ? 459  PHE   B CG   1 
ATOM   2558 C  CD1  . PHE   B 2 73  ? -26.130 -9.446  20.850  1.00 33.15  ? 459  PHE   B CD1  1 
ATOM   2559 C  CD2  . PHE   B 2 73  ? -27.743 -9.929  22.529  1.00 34.02  ? 459  PHE   B CD2  1 
ATOM   2560 C  CE1  . PHE   B 2 73  ? -25.156 -9.250  21.824  1.00 37.04  ? 459  PHE   B CE1  1 
ATOM   2561 C  CE2  . PHE   B 2 73  ? -26.767 -9.768  23.518  1.00 37.16  ? 459  PHE   B CE2  1 
ATOM   2562 C  CZ   . PHE   B 2 73  ? -25.474 -9.433  23.160  1.00 35.31  ? 459  PHE   B CZ   1 
ATOM   2563 N  N    . CYS   B 2 74  ? -27.447 -8.046  17.873  1.00 30.17  ? 460  CYS   B N    1 
ATOM   2564 C  CA   . CYS   B 2 74  ? -26.354 -7.219  17.376  1.00 34.17  ? 460  CYS   B CA   1 
ATOM   2565 C  C    . CYS   B 2 74  ? -26.852 -5.886  16.856  1.00 33.93  ? 460  CYS   B C    1 
ATOM   2566 O  O    . CYS   B 2 74  ? -26.082 -4.925  16.816  1.00 35.63  ? 460  CYS   B O    1 
ATOM   2567 C  CB   . CYS   B 2 74  ? -25.561 -7.949  16.288  1.00 36.43  ? 460  CYS   B CB   1 
ATOM   2568 S  SG   . CYS   B 2 74  ? -24.636 -9.346  16.932  1.00 38.91  ? 460  CYS   B SG   1 
ATOM   2569 N  N    . ILE   B 2 75  ? -28.124 -5.804  16.461  1.00 34.34  ? 461  ILE   B N    1 
ATOM   2570 C  CA   . ILE   B 2 75  ? -28.679 -4.519  16.054  1.00 36.86  ? 461  ILE   B CA   1 
ATOM   2571 C  C    . ILE   B 2 75  ? -28.858 -3.618  17.267  1.00 36.04  ? 461  ILE   B C    1 
ATOM   2572 O  O    . ILE   B 2 75  ? -28.613 -2.409  17.190  1.00 37.15  ? 461  ILE   B O    1 
ATOM   2573 C  CB   . ILE   B 2 75  ? -30.003 -4.707  15.292  1.00 40.63  ? 461  ILE   B CB   1 
ATOM   2574 C  CG1  . ILE   B 2 75  ? -29.785 -5.467  13.970  1.00 36.41  ? 461  ILE   B CG1  1 
ATOM   2575 C  CG2  . ILE   B 2 75  ? -30.667 -3.370  15.025  1.00 33.71  ? 461  ILE   B CG2  1 
ATOM   2576 C  CD1  . ILE   B 2 75  ? -28.735 -4.869  13.063  1.00 38.40  ? 461  ILE   B CD1  1 
ATOM   2577 N  N    . ASP   B 2 76  ? -29.287 -4.190  18.407  1.00 34.71  ? 462  ASP   B N    1 
ATOM   2578 C  CA   . ASP   B 2 76  ? -29.370 -3.406  19.641  1.00 38.67  ? 462  ASP   B CA   1 
ATOM   2579 C  C    . ASP   B 2 76  ? -27.996 -2.934  20.113  1.00 37.60  ? 462  ASP   B C    1 
ATOM   2580 O  O    . ASP   B 2 76  ? -27.888 -1.859  20.713  1.00 36.13  ? 462  ASP   B O    1 
ATOM   2581 C  CB   . ASP   B 2 76  ? -30.082 -4.209  20.728  1.00 40.72  ? 462  ASP   B CB   1 
ATOM   2582 C  CG   . ASP   B 2 76  ? -31.607 -4.209  20.549  1.00 43.84  ? 462  ASP   B CG   1 
ATOM   2583 O  OD1  . ASP   B 2 76  ? -32.084 -3.465  19.667  1.00 42.42  ? 462  ASP   B OD1  1 
ATOM   2584 O  OD2  . ASP   B 2 76  ? -32.326 -4.938  21.276  1.00 43.76  ? 462  ASP   B OD2  1 
ATOM   2585 N  N    . ILE   B 2 77  ? -26.940 -3.701  19.839  1.00 34.55  ? 463  ILE   B N    1 
ATOM   2586 C  CA   . ILE   B 2 77  ? -25.580 -3.259  20.163  1.00 32.79  ? 463  ILE   B CA   1 
ATOM   2587 C  C    . ILE   B 2 77  ? -25.176 -2.097  19.265  1.00 36.78  ? 463  ILE   B C    1 
ATOM   2588 O  O    . ILE   B 2 77  ? -24.577 -1.113  19.721  1.00 36.96  ? 463  ILE   B O    1 
ATOM   2589 C  CB   . ILE   B 2 77  ? -24.588 -4.430  20.022  1.00 36.47  ? 463  ILE   B CB   1 
ATOM   2590 C  CG1  . ILE   B 2 77  ? -24.728 -5.438  21.161  1.00 35.54  ? 463  ILE   B CG1  1 
ATOM   2591 C  CG2  . ILE   B 2 77  ? -23.149 -3.885  19.897  1.00 36.48  ? 463  ILE   B CG2  1 
ATOM   2592 C  CD1  . ILE   B 2 77  ? -24.095 -5.009  22.469  1.00 39.88  ? 463  ILE   B CD1  1 
ATOM   2593 N  N    . LEU   B 2 78  ? -25.481 -2.201  17.966  1.00 36.59  ? 464  LEU   B N    1 
ATOM   2594 C  CA   . LEU   B 2 78  ? -25.203 -1.102  17.041  1.00 37.55  ? 464  LEU   B CA   1 
ATOM   2595 C  C    . LEU   B 2 78  ? -25.959 0.162   17.431  1.00 36.76  ? 464  LEU   B C    1 
ATOM   2596 O  O    . LEU   B 2 78  ? -25.401 1.262   17.386  1.00 35.37  ? 464  LEU   B O    1 
ATOM   2597 C  CB   . LEU   B 2 78  ? -25.552 -1.509  15.608  1.00 34.03  ? 464  LEU   B CB   1 
ATOM   2598 C  CG   . LEU   B 2 78  ? -25.471 -0.388  14.558  1.00 40.33  ? 464  LEU   B CG   1 
ATOM   2599 C  CD1  . LEU   B 2 78  ? -24.082 0.204   14.467  1.00 38.70  ? 464  LEU   B CD1  1 
ATOM   2600 C  CD2  . LEU   B 2 78  ? -25.915 -0.908  13.193  1.00 42.46  ? 464  LEU   B CD2  1 
ATOM   2601 N  N    . LYS   B 2 79  ? -27.235 0.029   17.803  1.00 35.43  ? 465  LYS   B N    1 
ATOM   2602 C  CA   . LYS   B 2 79  ? -27.970 1.196   18.290  1.00 42.28  ? 465  LYS   B CA   1 
ATOM   2603 C  C    . LYS   B 2 79  ? -27.246 1.853   19.458  1.00 39.50  ? 465  LYS   B C    1 
ATOM   2604 O  O    . LYS   B 2 79  ? -27.038 3.068   19.464  1.00 40.18  ? 465  LYS   B O    1 
ATOM   2605 C  CB   . LYS   B 2 79  ? -29.391 0.800   18.691  1.00 40.45  ? 465  LYS   B CB   1 
ATOM   2606 C  CG   . LYS   B 2 79  ? -30.314 0.599   17.489  1.00 45.19  ? 465  LYS   B CG   1 
ATOM   2607 C  CD   . LYS   B 2 79  ? -31.464 -0.379  17.762  1.00 47.12  ? 465  LYS   B CD   1 
ATOM   2608 C  CE   . LYS   B 2 79  ? -32.409 0.092   18.838  1.00 53.21  ? 465  LYS   B CE   1 
ATOM   2609 N  NZ   . LYS   B 2 79  ? -33.499 -0.923  19.067  1.00 56.56  ? 465  LYS   B NZ   1 
ATOM   2610 N  N    . LYS   B 2 80  ? -26.824 1.057   20.440  1.00 39.82  ? 466  LYS   B N    1 
ATOM   2611 C  CA   . LYS   B 2 80  ? -26.143 1.609   21.607  1.00 40.49  ? 466  LYS   B CA   1 
ATOM   2612 C  C    . LYS   B 2 80  ? -24.851 2.308   21.211  1.00 42.82  ? 466  LYS   B C    1 
ATOM   2613 O  O    . LYS   B 2 80  ? -24.578 3.432   21.649  1.00 37.09  ? 466  LYS   B O    1 
ATOM   2614 C  CB   . LYS   B 2 80  ? -25.873 0.490   22.612  1.00 41.17  ? 466  LYS   B CB   1 
ATOM   2615 C  CG   . LYS   B 2 80  ? -27.081 0.100   23.428  1.00 40.35  ? 466  LYS   B CG   1 
ATOM   2616 C  CD   . LYS   B 2 80  ? -26.765 -1.069  24.350  1.00 47.73  ? 466  LYS   B CD   1 
ATOM   2617 C  CE   . LYS   B 2 80  ? -27.771 -1.173  25.486  1.00 59.55  ? 466  LYS   B CE   1 
ATOM   2618 N  NZ   . LYS   B 2 80  ? -27.671 0.010   26.405  1.00 60.85  ? 466  LYS   B NZ   1 
ATOM   2619 N  N    . LEU   B 2 81  ? -24.029 1.644   20.390  1.00 38.86  ? 467  LEU   B N    1 
ATOM   2620 C  CA   . LEU   B 2 81  ? -22.797 2.259   19.901  1.00 39.38  ? 467  LEU   B CA   1 
ATOM   2621 C  C    . LEU   B 2 81  ? -23.089 3.549   19.134  1.00 41.57  ? 467  LEU   B C    1 
ATOM   2622 O  O    . LEU   B 2 81  ? -22.402 4.557   19.317  1.00 41.40  ? 467  LEU   B O    1 
ATOM   2623 C  CB   . LEU   B 2 81  ? -22.047 1.262   19.009  1.00 40.44  ? 467  LEU   B CB   1 
ATOM   2624 C  CG   . LEU   B 2 81  ? -21.491 0.031   19.728  1.00 37.90  ? 467  LEU   B CG   1 
ATOM   2625 C  CD1  . LEU   B 2 81  ? -20.837 -0.919  18.721  1.00 36.65  ? 467  LEU   B CD1  1 
ATOM   2626 C  CD2  . LEU   B 2 81  ? -20.489 0.471   20.777  1.00 37.35  ? 467  LEU   B CD2  1 
ATOM   2627 N  N    . SER   B 2 82  ? -24.100 3.533   18.265  1.00 38.76  ? 468  SER   B N    1 
ATOM   2628 C  CA   . SER   B 2 82  ? -24.465 4.742   17.525  1.00 42.20  ? 468  SER   B CA   1 
ATOM   2629 C  C    . SER   B 2 82  ? -24.786 5.896   18.471  1.00 42.60  ? 468  SER   B C    1 
ATOM   2630 O  O    . SER   B 2 82  ? -24.297 7.018   18.286  1.00 44.09  ? 468  SER   B O    1 
ATOM   2631 C  CB   . SER   B 2 82  ? -25.656 4.458   16.607  1.00 39.89  ? 468  SER   B CB   1 
ATOM   2632 O  OG   . SER   B 2 82  ? -26.097 5.643   15.958  1.00 44.88  ? 468  SER   B OG   1 
ATOM   2633 N  N    . ARG   B 2 83  ? -25.590 5.631   19.502  1.00 42.57  ? 469  ARG   B N    1 
ATOM   2634 C  CA   . ARG   B 2 83  ? -25.933 6.661   20.474  1.00 46.66  ? 469  ARG   B CA   1 
ATOM   2635 C  C    . ARG   B 2 83  ? -24.711 7.092   21.283  1.00 47.83  ? 469  ARG   B C    1 
ATOM   2636 O  O    . ARG   B 2 83  ? -24.500 8.286   21.499  1.00 47.90  ? 469  ARG   B O    1 
ATOM   2637 C  CB   . ARG   B 2 83  ? -27.043 6.143   21.390  1.00 52.74  ? 469  ARG   B CB   1 
ATOM   2638 C  CG   . ARG   B 2 83  ? -26.970 6.597   22.850  1.00 54.87  ? 469  ARG   B CG   1 
ATOM   2639 C  CD   . ARG   B 2 83  ? -28.311 6.406   23.558  1.00 61.20  ? 469  ARG   B CD   1 
ATOM   2640 N  NE   . ARG   B 2 83  ? -29.330 7.338   23.085  1.00 76.69  ? 469  ARG   B NE   1 
ATOM   2641 C  CZ   . ARG   B 2 83  ? -30.607 7.031   22.895  1.00 78.36  ? 469  ARG   B CZ   1 
ATOM   2642 N  NH1  . ARG   B 2 83  ? -31.077 5.822   23.161  1.00 78.85  ? 469  ARG   B NH1  1 
ATOM   2643 N  NH2  . ARG   B 2 83  ? -31.435 7.962   22.427  1.00 73.74  ? 469  ARG   B NH2  1 
ATOM   2644 N  N    . THR   B 2 84  ? -23.880 6.138   21.711  1.00 44.55  ? 470  THR   B N    1 
ATOM   2645 C  CA   . THR   B 2 84  ? -22.815 6.434   22.667  1.00 42.11  ? 470  THR   B CA   1 
ATOM   2646 C  C    . THR   B 2 84  ? -21.575 7.003   21.987  1.00 45.19  ? 470  THR   B C    1 
ATOM   2647 O  O    . THR   B 2 84  ? -21.053 8.041   22.405  1.00 50.11  ? 470  THR   B O    1 
ATOM   2648 C  CB   . THR   B 2 84  ? -22.484 5.174   23.466  1.00 44.94  ? 470  THR   B CB   1 
ATOM   2649 O  OG1  . THR   B 2 84  ? -23.645 4.771   24.209  1.00 47.55  ? 470  THR   B OG1  1 
ATOM   2650 C  CG2  . THR   B 2 84  ? -21.301 5.395   24.405  1.00 45.84  ? 470  THR   B CG2  1 
ATOM   2651 N  N    . VAL   B 2 85  ? -21.093 6.349   20.932  1.00 42.77  ? 471  VAL   B N    1 
ATOM   2652 C  CA   . VAL   B 2 85  ? -19.942 6.853   20.191  1.00 47.00  ? 471  VAL   B CA   1 
ATOM   2653 C  C    . VAL   B 2 85  ? -20.302 8.035   19.307  1.00 49.44  ? 471  VAL   B C    1 
ATOM   2654 O  O    . VAL   B 2 85  ? -19.406 8.752   18.847  1.00 55.47  ? 471  VAL   B O    1 
ATOM   2655 C  CB   . VAL   B 2 85  ? -19.333 5.688   19.386  1.00 44.62  ? 471  VAL   B CB   1 
ATOM   2656 C  CG1  . VAL   B 2 85  ? -18.005 6.072   18.743  1.00 49.25  ? 471  VAL   B CG1  1 
ATOM   2657 C  CG2  . VAL   B 2 85  ? -19.118 4.496   20.309  1.00 44.22  ? 471  VAL   B CG2  1 
ATOM   2658 N  N    . LYS   B 2 86  ? -21.596 8.252   19.069  1.00 46.69  ? 472  LYS   B N    1 
ATOM   2659 C  CA   . LYS   B 2 86  ? -22.118 9.410   18.343  1.00 51.88  ? 472  LYS   B CA   1 
ATOM   2660 C  C    . LYS   B 2 86  ? -21.800 9.350   16.853  1.00 53.12  ? 472  LYS   B C    1 
ATOM   2661 O  O    . LYS   B 2 86  ? -20.999 10.144  16.344  1.00 51.36  ? 472  LYS   B O    1 
ATOM   2662 C  CB   . LYS   B 2 86  ? -21.598 10.712  18.956  1.00 52.50  ? 472  LYS   B CB   1 
ATOM   2663 C  CG   . LYS   B 2 86  ? -22.090 10.956  20.371  1.00 58.32  ? 472  LYS   B CG   1 
ATOM   2664 C  CD   . LYS   B 2 86  ? -21.763 12.364  20.830  1.00 64.44  ? 472  LYS   B CD   1 
ATOM   2665 C  CE   . LYS   B 2 86  ? -22.741 12.844  21.891  1.00 73.26  ? 472  LYS   B CE   1 
ATOM   2666 N  NZ   . LYS   B 2 86  ? -23.568 11.725  22.426  1.00 70.51  ? 472  LYS   B NZ   1 
ATOM   2667 N  N    . PHE   B 2 87  ? -22.426 8.405   16.147  1.00 46.82  ? 473  PHE   B N    1 
ATOM   2668 C  CA   . PHE   B 2 87  ? -22.333 8.346   14.699  1.00 45.41  ? 473  PHE   B CA   1 
ATOM   2669 C  C    . PHE   B 2 87  ? -23.685 7.957   14.133  1.00 47.79  ? 473  PHE   B C    1 
ATOM   2670 O  O    . PHE   B 2 87  ? -24.564 7.463   14.843  1.00 47.20  ? 473  PHE   B O    1 
ATOM   2671 C  CB   . PHE   B 2 87  ? -21.238 7.369   14.214  1.00 46.85  ? 473  PHE   B CB   1 
ATOM   2672 C  CG   . PHE   B 2 87  ? -21.463 5.933   14.617  1.00 41.04  ? 473  PHE   B CG   1 
ATOM   2673 C  CD1  . PHE   B 2 87  ? -22.330 5.112   13.911  1.00 40.49  ? 473  PHE   B CD1  1 
ATOM   2674 C  CD2  . PHE   B 2 87  ? -20.774 5.393   15.686  1.00 42.85  ? 473  PHE   B CD2  1 
ATOM   2675 C  CE1  . PHE   B 2 87  ? -22.511 3.773   14.293  1.00 41.18  ? 473  PHE   B CE1  1 
ATOM   2676 C  CE2  . PHE   B 2 87  ? -20.954 4.076   16.064  1.00 40.81  ? 473  PHE   B CE2  1 
ATOM   2677 C  CZ   . PHE   B 2 87  ? -21.830 3.273   15.371  1.00 37.76  ? 473  PHE   B CZ   1 
ATOM   2678 N  N    . THR   B 2 88  ? -23.841 8.205   12.838  1.00 49.50  ? 474  THR   B N    1 
ATOM   2679 C  CA   . THR   B 2 88  ? -24.976 7.736   12.071  1.00 43.72  ? 474  THR   B CA   1 
ATOM   2680 C  C    . THR   B 2 88  ? -24.487 6.745   11.026  1.00 45.55  ? 474  THR   B C    1 
ATOM   2681 O  O    . THR   B 2 88  ? -23.287 6.627   10.760  1.00 44.15  ? 474  THR   B O    1 
ATOM   2682 C  CB   . THR   B 2 88  ? -25.721 8.902   11.417  1.00 47.47  ? 474  THR   B CB   1 
ATOM   2683 O  OG1  . THR   B 2 88  ? -24.835 9.615   10.544  1.00 49.68  ? 474  THR   B OG1  1 
ATOM   2684 C  CG2  . THR   B 2 88  ? -26.258 9.846   12.486  1.00 47.61  ? 474  THR   B CG2  1 
ATOM   2685 N  N    . TYR   B 2 89  ? -25.428 6.019   10.429  1.00 42.56  ? 475  TYR   B N    1 
ATOM   2686 C  CA   . TYR   B 2 89  ? -25.016 4.894   9.606   1.00 42.80  ? 475  TYR   B CA   1 
ATOM   2687 C  C    . TYR   B 2 89  ? -26.081 4.570   8.568   1.00 46.38  ? 475  TYR   B C    1 
ATOM   2688 O  O    . TYR   B 2 89  ? -27.261 4.901   8.727   1.00 43.54  ? 475  TYR   B O    1 
ATOM   2689 C  CB   . TYR   B 2 89  ? -24.720 3.668   10.480  1.00 40.87  ? 475  TYR   B CB   1 
ATOM   2690 C  CG   . TYR   B 2 89  ? -25.877 3.205   11.356  1.00 40.08  ? 475  TYR   B CG   1 
ATOM   2691 C  CD1  . TYR   B 2 89  ? -26.876 2.395   10.834  1.00 40.66  ? 475  TYR   B CD1  1 
ATOM   2692 C  CD2  . TYR   B 2 89  ? -25.946 3.541   12.706  1.00 41.41  ? 475  TYR   B CD2  1 
ATOM   2693 C  CE1  . TYR   B 2 89  ? -27.917 1.960   11.606  1.00 41.67  ? 475  TYR   B CE1  1 
ATOM   2694 C  CE2  . TYR   B 2 89  ? -27.003 3.120   13.496  1.00 38.97  ? 475  TYR   B CE2  1 
ATOM   2695 C  CZ   . TYR   B 2 89  ? -27.988 2.319   12.936  1.00 45.38  ? 475  TYR   B CZ   1 
ATOM   2696 O  OH   . TYR   B 2 89  ? -29.055 1.861   13.689  1.00 41.53  ? 475  TYR   B OH   1 
ATOM   2697 N  N    . ASP   B 2 90  ? -25.634 3.921   7.491   1.00 44.04  ? 476  ASP   B N    1 
ATOM   2698 C  CA   . ASP   B 2 90  ? -26.494 3.319   6.474   1.00 45.07  ? 476  ASP   B CA   1 
ATOM   2699 C  C    . ASP   B 2 90  ? -26.153 1.837   6.468   1.00 42.23  ? 476  ASP   B C    1 
ATOM   2700 O  O    . ASP   B 2 90  ? -25.088 1.441   5.984   1.00 39.85  ? 476  ASP   B O    1 
ATOM   2701 C  CB   . ASP   B 2 90  ? -26.291 3.943   5.098   1.00 49.13  ? 476  ASP   B CB   1 
ATOM   2702 C  CG   . ASP   B 2 90  ? -26.916 5.327   4.987   1.00 62.36  ? 476  ASP   B CG   1 
ATOM   2703 O  OD1  . ASP   B 2 90  ? -26.475 6.120   4.121   1.00 66.17  ? 476  ASP   B OD1  1 
ATOM   2704 O  OD2  . ASP   B 2 90  ? -27.866 5.621   5.751   1.00 62.24  ? 476  ASP   B OD2  1 
ATOM   2705 N  N    . LEU   B 2 91  ? -27.050 1.044   7.031   1.00 39.09  ? 477  LEU   B N    1 
ATOM   2706 C  CA   . LEU   B 2 91  ? -26.840 -0.377  7.221   1.00 37.28  ? 477  LEU   B CA   1 
ATOM   2707 C  C    . LEU   B 2 91  ? -27.256 -1.140  5.970   1.00 38.69  ? 477  LEU   B C    1 
ATOM   2708 O  O    . LEU   B 2 91  ? -28.296 -0.858  5.385   1.00 37.13  ? 477  LEU   B O    1 
ATOM   2709 C  CB   . LEU   B 2 91  ? -27.654 -0.848  8.420   1.00 37.06  ? 477  LEU   B CB   1 
ATOM   2710 C  CG   . LEU   B 2 91  ? -27.437 -2.286  8.868   1.00 40.66  ? 477  LEU   B CG   1 
ATOM   2711 C  CD1  . LEU   B 2 91  ? -26.004 -2.525  9.384   1.00 33.95  ? 477  LEU   B CD1  1 
ATOM   2712 C  CD2  . LEU   B 2 91  ? -28.458 -2.600  9.940   1.00 39.73  ? 477  LEU   B CD2  1 
ATOM   2713 N  N    . TYR   B 2 92  ? -26.451 -2.118  5.567   1.00 36.58  ? 478  TYR   B N    1 
ATOM   2714 C  CA   . TYR   B 2 92  ? -26.795 -2.915  4.398   1.00 37.16  ? 478  TYR   B CA   1 
ATOM   2715 C  C    . TYR   B 2 92  ? -26.376 -4.361  4.621   1.00 34.51  ? 478  TYR   B C    1 
ATOM   2716 O  O    . TYR   B 2 92  ? -25.469 -4.656  5.400   1.00 33.88  ? 478  TYR   B O    1 
ATOM   2717 C  CB   . TYR   B 2 92  ? -26.160 -2.351  3.104   1.00 32.10  ? 478  TYR   B CB   1 
ATOM   2718 C  CG   . TYR   B 2 92  ? -24.670 -2.563  2.956   1.00 34.11  ? 478  TYR   B CG   1 
ATOM   2719 C  CD1  . TYR   B 2 92  ? -23.761 -1.693  3.560   1.00 36.39  ? 478  TYR   B CD1  1 
ATOM   2720 C  CD2  . TYR   B 2 92  ? -24.165 -3.607  2.185   1.00 35.36  ? 478  TYR   B CD2  1 
ATOM   2721 C  CE1  . TYR   B 2 92  ? -22.400 -1.859  3.415   1.00 32.97  ? 478  TYR   B CE1  1 
ATOM   2722 C  CE2  . TYR   B 2 92  ? -22.775 -3.803  2.045   1.00 31.97  ? 478  TYR   B CE2  1 
ATOM   2723 C  CZ   . TYR   B 2 92  ? -21.903 -2.923  2.667   1.00 37.43  ? 478  TYR   B CZ   1 
ATOM   2724 O  OH   . TYR   B 2 92  ? -20.534 -3.086  2.523   1.00 39.49  ? 478  TYR   B OH   1 
ATOM   2725 N  N    . LEU   B 2 93  ? -27.032 -5.258  3.898   1.00 32.94  ? 479  LEU   B N    1 
ATOM   2726 C  CA   . LEU   B 2 93  ? -26.822 -6.698  4.022   1.00 34.85  ? 479  LEU   B CA   1 
ATOM   2727 C  C    . LEU   B 2 93  ? -25.835 -7.150  2.960   1.00 31.68  ? 479  LEU   B C    1 
ATOM   2728 O  O    . LEU   B 2 93  ? -25.982 -6.793  1.785   1.00 30.55  ? 479  LEU   B O    1 
ATOM   2729 C  CB   . LEU   B 2 93  ? -28.143 -7.455  3.843   1.00 32.66  ? 479  LEU   B CB   1 
ATOM   2730 C  CG   . LEU   B 2 93  ? -29.145 -7.559  5.007   1.00 40.32  ? 479  LEU   B CG   1 
ATOM   2731 C  CD1  . LEU   B 2 93  ? -28.611 -8.421  6.119   1.00 37.22  ? 479  LEU   B CD1  1 
ATOM   2732 C  CD2  . LEU   B 2 93  ? -29.519 -6.205  5.538   1.00 46.33  ? 479  LEU   B CD2  1 
ATOM   2733 N  N    . VAL   B 2 94  ? -24.831 -7.930  3.366   1.00 29.37  ? 480  VAL   B N    1 
ATOM   2734 C  CA   . VAL   B 2 94  ? -23.829 -8.382  2.410   1.00 33.85  ? 480  VAL   B CA   1 
ATOM   2735 C  C    . VAL   B 2 94  ? -24.490 -9.287  1.377   1.00 34.05  ? 480  VAL   B C    1 
ATOM   2736 O  O    . VAL   B 2 94  ? -25.389 -10.076 1.701   1.00 33.59  ? 480  VAL   B O    1 
ATOM   2737 C  CB   . VAL   B 2 94  ? -22.674 -9.099  3.128   1.00 29.43  ? 480  VAL   B CB   1 
ATOM   2738 C  CG1  . VAL   B 2 94  ? -23.166 -10.359 3.846   1.00 29.62  ? 480  VAL   B CG1  1 
ATOM   2739 C  CG2  . VAL   B 2 94  ? -21.570 -9.446  2.138   1.00 31.31  ? 480  VAL   B CG2  1 
ATOM   2740 N  N    . THR   B 2 95  ? -24.071 -9.155  0.112   1.00 32.90  ? 481  THR   B N    1 
ATOM   2741 C  CA   . THR   B 2 95  ? -24.544 -10.053 -0.940  1.00 34.58  ? 481  THR   B CA   1 
ATOM   2742 C  C    . THR   B 2 95  ? -23.434 -10.871 -1.594  1.00 39.79  ? 481  THR   B C    1 
ATOM   2743 O  O    . THR   B 2 95  ? -23.728 -11.764 -2.397  1.00 37.20  ? 481  THR   B O    1 
ATOM   2744 C  CB   . THR   B 2 95  ? -25.280 -9.260  -2.022  1.00 35.95  ? 481  THR   B CB   1 
ATOM   2745 O  OG1  . THR   B 2 95  ? -24.464 -8.164  -2.436  1.00 38.94  ? 481  THR   B OG1  1 
ATOM   2746 C  CG2  . THR   B 2 95  ? -26.622 -8.722  -1.478  1.00 35.91  ? 481  THR   B CG2  1 
ATOM   2747 N  N    . ASN   B 2 96  ? -22.177 -10.585 -1.288  1.00 32.06  ? 482  ASN   B N    1 
ATOM   2748 C  CA   . ASN   B 2 96  ? -21.030 -11.293 -1.840  1.00 35.64  ? 482  ASN   B CA   1 
ATOM   2749 C  C    . ASN   B 2 96  ? -20.522 -12.246 -0.763  1.00 35.90  ? 482  ASN   B C    1 
ATOM   2750 O  O    . ASN   B 2 96  ? -19.605 -11.936 -0.015  1.00 36.79  ? 482  ASN   B O    1 
ATOM   2751 C  CB   . ASN   B 2 96  ? -19.946 -10.292 -2.271  1.00 34.43  ? 482  ASN   B CB   1 
ATOM   2752 C  CG   . ASN   B 2 96  ? -18.671 -10.974 -2.730  1.00 38.95  ? 482  ASN   B CG   1 
ATOM   2753 O  OD1  . ASN   B 2 96  ? -18.717 -11.924 -3.511  1.00 40.48  ? 482  ASN   B OD1  1 
ATOM   2754 N  ND2  . ASN   B 2 96  ? -17.521 -10.504 -2.225  1.00 37.79  ? 482  ASN   B ND2  1 
ATOM   2755 N  N    . GLY   B 2 97  ? -21.147 -13.413 -0.674  1.00 32.61  ? 483  GLY   B N    1 
ATOM   2756 C  CA   . GLY   B 2 97  ? -20.781 -14.367 0.360   1.00 35.70  ? 483  GLY   B CA   1 
ATOM   2757 C  C    . GLY   B 2 97  ? -21.496 -14.079 1.667   1.00 34.82  ? 483  GLY   B C    1 
ATOM   2758 O  O    . GLY   B 2 97  ? -22.523 -13.396 1.711   1.00 36.72  ? 483  GLY   B O    1 
ATOM   2759 N  N    . LYS   B 2 98  ? -20.926 -14.599 2.755   1.00 32.57  ? 484  LYS   B N    1 
ATOM   2760 C  CA   . LYS   B 2 98  ? -21.595 -14.556 4.056   1.00 30.76  ? 484  LYS   B CA   1 
ATOM   2761 C  C    . LYS   B 2 98  ? -20.725 -13.876 5.106   1.00 32.30  ? 484  LYS   B C    1 
ATOM   2762 O  O    . LYS   B 2 98  ? -20.480 -12.669 5.005   1.00 30.08  ? 484  LYS   B O    1 
ATOM   2763 C  CB   . LYS   B 2 98  ? -21.988 -15.969 4.503   1.00 34.36  ? 484  LYS   B CB   1 
ATOM   2764 C  CG   . LYS   B 2 98  ? -23.096 -16.608 3.631   1.00 40.00  ? 484  LYS   B CG   1 
ATOM   2765 C  CD   . LYS   B 2 98  ? -23.341 -18.063 4.013   1.00 43.00  ? 484  LYS   B CD   1 
ATOM   2766 C  CE   . LYS   B 2 98  ? -24.023 -18.199 5.377   1.00 46.99  ? 484  LYS   B CE   1 
ATOM   2767 N  NZ   . LYS   B 2 98  ? -24.358 -19.628 5.688   1.00 45.52  ? 484  LYS   B NZ   1 
ATOM   2768 N  N    . HIS   B 2 99  ? -20.273 -14.623 6.126   1.00 30.63  ? 485  HIS   B N    1 
ATOM   2769 C  CA   . HIS   B 2 99  ? -19.471 -14.007 7.188   1.00 31.03  ? 485  HIS   B CA   1 
ATOM   2770 C  C    . HIS   B 2 99  ? -18.097 -13.600 6.666   1.00 31.21  ? 485  HIS   B C    1 
ATOM   2771 O  O    . HIS   B 2 99  ? -17.648 -12.462 6.869   1.00 30.67  ? 485  HIS   B O    1 
ATOM   2772 C  CB   . HIS   B 2 99  ? -19.331 -14.969 8.371   1.00 30.66  ? 485  HIS   B CB   1 
ATOM   2773 C  CG   . HIS   B 2 99  ? -20.640 -15.458 8.911   1.00 28.98  ? 485  HIS   B CG   1 
ATOM   2774 N  ND1  . HIS   B 2 99  ? -21.375 -16.438 8.284   1.00 31.29  ? 485  HIS   B ND1  1 
ATOM   2775 C  CD2  . HIS   B 2 99  ? -21.355 -15.090 10.001  1.00 31.48  ? 485  HIS   B CD2  1 
ATOM   2776 C  CE1  . HIS   B 2 99  ? -22.489 -16.657 8.965   1.00 32.17  ? 485  HIS   B CE1  1 
ATOM   2777 N  NE2  . HIS   B 2 99  ? -22.502 -15.850 10.011  1.00 32.00  ? 485  HIS   B NE2  1 
ATOM   2778 N  N    . GLY   B 2 100 ? -17.411 -14.521 5.992   1.00 29.65  ? 486  GLY   B N    1 
ATOM   2779 C  CA   . GLY   B 2 100 ? -16.132 -14.207 5.391   1.00 27.73  ? 486  GLY   B CA   1 
ATOM   2780 C  C    . GLY   B 2 100 ? -15.284 -15.423 5.071   1.00 31.40  ? 486  GLY   B C    1 
ATOM   2781 O  O    . GLY   B 2 100 ? -15.085 -16.308 5.910   1.00 29.49  ? 486  GLY   B O    1 
ATOM   2782 N  N    . LYS   B 2 101 ? -14.779 -15.488 3.849   1.00 28.21  ? 487  LYS   B N    1 
ATOM   2783 C  CA   . LYS   B 2 101 ? -13.854 -16.548 3.482   1.00 29.35  ? 487  LYS   B CA   1 
ATOM   2784 C  C    . LYS   B 2 101 ? -12.857 -15.994 2.482   1.00 32.89  ? 487  LYS   B C    1 
ATOM   2785 O  O    . LYS   B 2 101 ? -13.229 -15.240 1.574   1.00 30.69  ? 487  LYS   B O    1 
ATOM   2786 C  CB   . LYS   B 2 101 ? -14.572 -17.760 2.884   1.00 29.92  ? 487  LYS   B CB   1 
ATOM   2787 C  CG   . LYS   B 2 101 ? -13.620 -18.929 2.562   1.00 31.74  ? 487  LYS   B CG   1 
ATOM   2788 C  CD   . LYS   B 2 101 ? -14.320 -19.984 1.760   1.00 30.77  ? 487  LYS   B CD   1 
ATOM   2789 C  CE   . LYS   B 2 101 ? -13.358 -21.145 1.426   1.00 32.18  ? 487  LYS   B CE   1 
ATOM   2790 N  NZ   . LYS   B 2 101 ? -14.078 -22.237 0.691   1.00 32.86  ? 487  LYS   B NZ   1 
ATOM   2791 N  N    . LYS   B 2 102 ? -11.593 -16.379 2.651   1.00 32.85  ? 488  LYS   B N    1 
ATOM   2792 C  CA   . LYS   B 2 102 ? -10.557 -16.007 1.698   1.00 33.17  ? 488  LYS   B CA   1 
ATOM   2793 C  C    . LYS   B 2 102 ? -10.556 -17.002 0.541   1.00 32.41  ? 488  LYS   B C    1 
ATOM   2794 O  O    . LYS   B 2 102 ? -10.329 -18.201 0.743   1.00 31.42  ? 488  LYS   B O    1 
ATOM   2795 C  CB   . LYS   B 2 102 ? -9.194  -15.960 2.384   1.00 34.78  ? 488  LYS   B CB   1 
ATOM   2796 C  CG   . LYS   B 2 102 ? -8.178  -15.110 1.631   1.00 37.25  ? 488  LYS   B CG   1 
ATOM   2797 C  CD   . LYS   B 2 102 ? -6.841  -14.954 2.390   1.00 36.45  ? 488  LYS   B CD   1 
ATOM   2798 C  CE   . LYS   B 2 102 ? -6.066  -16.277 2.388   1.00 42.05  ? 488  LYS   B CE   1 
ATOM   2799 N  NZ   . LYS   B 2 102 ? -4.694  -16.107 2.936   1.00 56.27  ? 488  LYS   B NZ   1 
ATOM   2800 N  N    . VAL   B 2 103 ? -10.807 -16.507 -0.671  1.00 34.58  ? 489  VAL   B N    1 
ATOM   2801 C  CA   . VAL   B 2 103 ? -10.897 -17.331 -1.873  1.00 36.19  ? 489  VAL   B CA   1 
ATOM   2802 C  C    . VAL   B 2 103 ? -9.864  -16.817 -2.870  1.00 36.69  ? 489  VAL   B C    1 
ATOM   2803 O  O    . VAL   B 2 103 ? -9.920  -15.648 -3.286  1.00 34.82  ? 489  VAL   B O    1 
ATOM   2804 C  CB   . VAL   B 2 103 ? -12.306 -17.301 -2.488  1.00 34.52  ? 489  VAL   B CB   1 
ATOM   2805 C  CG1  . VAL   B 2 103 ? -12.356 -18.193 -3.724  1.00 37.36  ? 489  VAL   B CG1  1 
ATOM   2806 C  CG2  . VAL   B 2 103 ? -13.339 -17.721 -1.473  1.00 34.80  ? 489  VAL   B CG2  1 
ATOM   2807 N  N    . ASN   B 2 104 ? -8.912  -17.682 -3.236  1.00 38.59  ? 490  ASN   B N    1 
ATOM   2808 C  CA   . ASN   B 2 104 ? -7.822  -17.292 -4.123  1.00 37.86  ? 490  ASN   B CA   1 
ATOM   2809 C  C    . ASN   B 2 104 ? -7.172  -16.003 -3.623  1.00 37.40  ? 490  ASN   B C    1 
ATOM   2810 O  O    . ASN   B 2 104 ? -6.855  -15.102 -4.398  1.00 36.84  ? 490  ASN   B O    1 
ATOM   2811 C  CB   . ASN   B 2 104 ? -8.312  -17.125 -5.564  1.00 37.28  ? 490  ASN   B CB   1 
ATOM   2812 C  CG   . ASN   B 2 104 ? -8.785  -18.432 -6.169  1.00 42.10  ? 490  ASN   B CG   1 
ATOM   2813 O  OD1  . ASN   B 2 104 ? -8.108  -19.462 -6.074  1.00 42.97  ? 490  ASN   B OD1  1 
ATOM   2814 N  ND2  . ASN   B 2 104 ? -9.960  -18.403 -6.777  1.00 40.14  ? 490  ASN   B ND2  1 
ATOM   2815 N  N    . ASN   B 2 105 ? -7.016  -15.915 -2.298  1.00 36.79  ? 491  ASN   B N    1 
ATOM   2816 C  CA   . ASN   B 2 105 ? -6.335  -14.818 -1.607  1.00 36.81  ? 491  ASN   B CA   1 
ATOM   2817 C  C    . ASN   B 2 105 ? -7.134  -13.518 -1.607  1.00 37.64  ? 491  ASN   B C    1 
ATOM   2818 O  O    . ASN   B 2 105 ? -6.562  -12.443 -1.414  1.00 42.77  ? 491  ASN   B O    1 
ATOM   2819 C  CB   . ASN   B 2 105 ? -4.927  -14.569 -2.161  1.00 40.34  ? 491  ASN   B CB   1 
ATOM   2820 C  CG   . ASN   B 2 105 ? -3.998  -13.998 -1.108  1.00 46.13  ? 491  ASN   B CG   1 
ATOM   2821 O  OD1  . ASN   B 2 105 ? -4.167  -14.247 0.089   1.00 44.60  ? 491  ASN   B OD1  1 
ATOM   2822 N  ND2  . ASN   B 2 105 ? -3.015  -13.232 -1.544  1.00 43.32  ? 491  ASN   B ND2  1 
ATOM   2823 N  N    . VAL   B 2 106 ? -8.452  -13.604 -1.773  1.00 33.30  ? 492  VAL   B N    1 
ATOM   2824 C  CA   . VAL   B 2 106 ? -9.340  -12.442 -1.784  1.00 37.81  ? 492  VAL   B CA   1 
ATOM   2825 C  C    . VAL   B 2 106 ? -10.472 -12.704 -0.795  1.00 35.61  ? 492  VAL   B C    1 
ATOM   2826 O  O    . VAL   B 2 106 ? -11.174 -13.714 -0.916  1.00 31.19  ? 492  VAL   B O    1 
ATOM   2827 C  CB   . VAL   B 2 106 ? -9.924  -12.177 -3.186  1.00 36.99  ? 492  VAL   B CB   1 
ATOM   2828 C  CG1  . VAL   B 2 106 ? -10.911 -10.997 -3.143  1.00 37.88  ? 492  VAL   B CG1  1 
ATOM   2829 C  CG2  . VAL   B 2 106 ? -8.793  -11.952 -4.226  1.00 40.88  ? 492  VAL   B CG2  1 
ATOM   2830 N  N    . TRP   B 2 107 ? -10.665 -11.792 0.165   1.00 33.97  ? 493  TRP   B N    1 
ATOM   2831 C  CA   . TRP   B 2 107 ? -11.694 -11.975 1.184   1.00 33.39  ? 493  TRP   B CA   1 
ATOM   2832 C  C    . TRP   B 2 107 ? -13.078 -11.616 0.650   1.00 34.04  ? 493  TRP   B C    1 
ATOM   2833 O  O    . TRP   B 2 107 ? -13.261 -10.553 0.053   1.00 36.47  ? 493  TRP   B O    1 
ATOM   2834 C  CB   . TRP   B 2 107 ? -11.381 -11.124 2.406   1.00 34.28  ? 493  TRP   B CB   1 
ATOM   2835 C  CG   . TRP   B 2 107 ? -10.384 -11.774 3.280   1.00 35.06  ? 493  TRP   B CG   1 
ATOM   2836 C  CD1  . TRP   B 2 107 ? -9.026  -11.555 3.303   1.00 35.07  ? 493  TRP   B CD1  1 
ATOM   2837 C  CD2  . TRP   B 2 107 ? -10.652 -12.758 4.278   1.00 30.85  ? 493  TRP   B CD2  1 
ATOM   2838 N  NE1  . TRP   B 2 107 ? -8.437  -12.370 4.246   1.00 35.81  ? 493  TRP   B NE1  1 
ATOM   2839 C  CE2  . TRP   B 2 107 ? -9.418  -13.108 4.864   1.00 34.89  ? 493  TRP   B CE2  1 
ATOM   2840 C  CE3  . TRP   B 2 107 ? -11.816 -13.395 4.720   1.00 32.41  ? 493  TRP   B CE3  1 
ATOM   2841 C  CZ2  . TRP   B 2 107 ? -9.321  -14.059 5.872   1.00 35.12  ? 493  TRP   B CZ2  1 
ATOM   2842 C  CZ3  . TRP   B 2 107 ? -11.720 -14.329 5.732   1.00 32.02  ? 493  TRP   B CZ3  1 
ATOM   2843 C  CH2  . TRP   B 2 107 ? -10.482 -14.654 6.298   1.00 35.59  ? 493  TRP   B CH2  1 
ATOM   2844 N  N    . ASN   B 2 108 ? -14.054 -12.489 0.877   1.00 32.17  ? 494  ASN   B N    1 
ATOM   2845 C  CA   . ASN   B 2 108 ? -15.433 -12.171 0.536   1.00 32.68  ? 494  ASN   B CA   1 
ATOM   2846 C  C    . ASN   B 2 108 ? -16.237 -11.956 1.819   1.00 28.93  ? 494  ASN   B C    1 
ATOM   2847 O  O    . ASN   B 2 108 ? -15.689 -11.924 2.925   1.00 31.25  ? 494  ASN   B O    1 
ATOM   2848 C  CB   . ASN   B 2 108 ? -16.048 -13.265 -0.360  1.00 30.48  ? 494  ASN   B CB   1 
ATOM   2849 C  CG   . ASN   B 2 108 ? -16.230 -14.628 0.348   1.00 35.14  ? 494  ASN   B CG   1 
ATOM   2850 O  OD1  . ASN   B 2 108 ? -16.425 -14.711 1.567   1.00 31.02  ? 494  ASN   B OD1  1 
ATOM   2851 N  ND2  . ASN   B 2 108 ? -16.257 -15.699 -0.451  1.00 34.07  ? 494  ASN   B ND2  1 
ATOM   2852 N  N    . GLY   B 2 109 ? -17.551 -11.823 1.675   1.00 33.63  ? 495  GLY   B N    1 
ATOM   2853 C  CA   . GLY   B 2 109 ? -18.382 -11.761 2.863   1.00 31.76  ? 495  GLY   B CA   1 
ATOM   2854 C  C    . GLY   B 2 109 ? -18.262 -10.416 3.569   1.00 30.11  ? 495  GLY   B C    1 
ATOM   2855 O  O    . GLY   B 2 109 ? -17.795 -9.425  3.011   1.00 32.11  ? 495  GLY   B O    1 
ATOM   2856 N  N    . MET   B 2 110 ? -18.710 -10.396 4.834   1.00 31.02  ? 496  MET   B N    1 
ATOM   2857 C  CA   . MET   B 2 110 ? -18.599 -9.175  5.626   1.00 32.55  ? 496  MET   B CA   1 
ATOM   2858 C  C    . MET   B 2 110 ? -17.143 -8.761  5.809   1.00 30.86  ? 496  MET   B C    1 
ATOM   2859 O  O    . MET   B 2 110 ? -16.830 -7.565  5.848   1.00 31.33  ? 496  MET   B O    1 
ATOM   2860 C  CB   . MET   B 2 110 ? -19.258 -9.346  7.002   1.00 30.36  ? 496  MET   B CB   1 
ATOM   2861 C  CG   . MET   B 2 110 ? -20.782 -9.397  6.991   1.00 33.67  ? 496  MET   B CG   1 
ATOM   2862 S  SD   . MET   B 2 110 ? -21.468 -9.287  8.669   1.00 34.27  ? 496  MET   B SD   1 
ATOM   2863 C  CE   . MET   B 2 110 ? -21.285 -10.950 9.254   1.00 30.86  ? 496  MET   B CE   1 
ATOM   2864 N  N    . ILE   B 2 111 ? -16.241 -9.729  5.973   1.00 28.67  ? 497  ILE   B N    1 
ATOM   2865 C  CA   . ILE   B 2 111 ? -14.827 -9.373  6.083   1.00 30.37  ? 497  ILE   B CA   1 
ATOM   2866 C  C    . ILE   B 2 111 ? -14.374 -8.672  4.809   1.00 31.68  ? 497  ILE   B C    1 
ATOM   2867 O  O    . ILE   B 2 111 ? -13.683 -7.648  4.855   1.00 33.99  ? 497  ILE   B O    1 
ATOM   2868 C  CB   . ILE   B 2 111 ? -13.974 -10.618 6.365   1.00 28.75  ? 497  ILE   B CB   1 
ATOM   2869 C  CG1  . ILE   B 2 111 ? -14.399 -11.290 7.678   1.00 30.02  ? 497  ILE   B CG1  1 
ATOM   2870 C  CG2  . ILE   B 2 111 ? -12.472 -10.248 6.381   1.00 29.95  ? 497  ILE   B CG2  1 
ATOM   2871 C  CD1  . ILE   B 2 111 ? -14.080 -10.513 8.939   1.00 32.82  ? 497  ILE   B CD1  1 
ATOM   2872 N  N    . GLY   B 2 112 ? -14.779 -9.202  3.652   1.00 32.34  ? 498  GLY   B N    1 
ATOM   2873 C  CA   . GLY   B 2 112 ? -14.384 -8.589  2.392   1.00 32.30  ? 498  GLY   B CA   1 
ATOM   2874 C  C    . GLY   B 2 112 ? -14.864 -7.156  2.253   1.00 34.30  ? 498  GLY   B C    1 
ATOM   2875 O  O    . GLY   B 2 112 ? -14.119 -6.288  1.786   1.00 33.55  ? 498  GLY   B O    1 
ATOM   2876 N  N    . GLU   B 2 113 ? -16.122 -6.893  2.641   1.00 30.38  ? 499  GLU   B N    1 
ATOM   2877 C  CA   . GLU   B 2 113 ? -16.671 -5.545  2.547   1.00 32.83  ? 499  GLU   B CA   1 
ATOM   2878 C  C    . GLU   B 2 113 ? -15.826 -4.569  3.347   1.00 33.29  ? 499  GLU   B C    1 
ATOM   2879 O  O    . GLU   B 2 113 ? -15.616 -3.428  2.923   1.00 39.32  ? 499  GLU   B O    1 
ATOM   2880 C  CB   . GLU   B 2 113 ? -18.121 -5.519  3.055   1.00 35.43  ? 499  GLU   B CB   1 
ATOM   2881 C  CG   . GLU   B 2 113 ? -19.096 -6.376  2.246   1.00 33.59  ? 499  GLU   B CG   1 
ATOM   2882 C  CD   . GLU   B 2 113 ? -19.241 -5.885  0.812   1.00 39.39  ? 499  GLU   B CD   1 
ATOM   2883 O  OE1  . GLU   B 2 113 ? -19.728 -4.759  0.601   1.00 40.12  ? 499  GLU   B OE1  1 
ATOM   2884 O  OE2  . GLU   B 2 113 ? -18.831 -6.622  -0.098  1.00 42.06  ? 499  GLU   B OE2  1 
ATOM   2885 N  N    . VAL   B 2 114 ? -15.321 -5.006  4.503   1.00 33.88  ? 500  VAL   B N    1 
ATOM   2886 C  CA   . VAL   B 2 114 ? -14.455 -4.149  5.311   1.00 34.76  ? 500  VAL   B CA   1 
ATOM   2887 C  C    . VAL   B 2 114 ? -13.072 -4.034  4.675   1.00 36.60  ? 500  VAL   B C    1 
ATOM   2888 O  O    . VAL   B 2 114 ? -12.543 -2.931  4.505   1.00 39.25  ? 500  VAL   B O    1 
ATOM   2889 C  CB   . VAL   B 2 114 ? -14.375 -4.681  6.755   1.00 36.50  ? 500  VAL   B CB   1 
ATOM   2890 C  CG1  . VAL   B 2 114 ? -13.435 -3.830  7.590   1.00 33.25  ? 500  VAL   B CG1  1 
ATOM   2891 C  CG2  . VAL   B 2 114 ? -15.765 -4.691  7.396   1.00 34.55  ? 500  VAL   B CG2  1 
ATOM   2892 N  N    . VAL   B 2 115 ? -12.468 -5.168  4.305   1.00 37.03  ? 501  VAL   B N    1 
ATOM   2893 C  CA   . VAL   B 2 115 ? -11.124 -5.154  3.717   1.00 38.60  ? 501  VAL   B CA   1 
ATOM   2894 C  C    . VAL   B 2 115 ? -11.074 -4.210  2.520   1.00 38.94  ? 501  VAL   B C    1 
ATOM   2895 O  O    . VAL   B 2 115 ? -10.136 -3.419  2.363   1.00 39.33  ? 501  VAL   B O    1 
ATOM   2896 C  CB   . VAL   B 2 115 ? -10.698 -6.577  3.309   1.00 38.79  ? 501  VAL   B CB   1 
ATOM   2897 C  CG1  . VAL   B 2 115 ? -9.458  -6.539  2.402   1.00 42.82  ? 501  VAL   B CG1  1 
ATOM   2898 C  CG2  . VAL   B 2 115 ? -10.482 -7.448  4.530   1.00 35.30  ? 501  VAL   B CG2  1 
ATOM   2899 N  N    . TYR   B 2 116 ? -12.089 -4.271  1.665   1.00 38.05  ? 502  TYR   B N    1 
ATOM   2900 C  CA   . TYR   B 2 116 ? -12.102 -3.483  0.448   1.00 39.55  ? 502  TYR   B CA   1 
ATOM   2901 C  C    . TYR   B 2 116 ? -12.802 -2.133  0.638   1.00 42.81  ? 502  TYR   B C    1 
ATOM   2902 O  O    . TYR   B 2 116 ? -13.115 -1.456  -0.348  1.00 41.27  ? 502  TYR   B O    1 
ATOM   2903 C  CB   . TYR   B 2 116 ? -12.697 -4.322  -0.688  1.00 43.80  ? 502  TYR   B CB   1 
ATOM   2904 C  CG   . TYR   B 2 116 ? -11.751 -5.480  -1.006  1.00 43.33  ? 502  TYR   B CG   1 
ATOM   2905 C  CD1  . TYR   B 2 116 ? -10.556 -5.241  -1.674  1.00 56.98  ? 502  TYR   B CD1  1 
ATOM   2906 C  CD2  . TYR   B 2 116 ? -12.036 -6.792  -0.622  1.00 43.17  ? 502  TYR   B CD2  1 
ATOM   2907 C  CE1  . TYR   B 2 116 ? -9.655  -6.259  -1.949  1.00 52.33  ? 502  TYR   B CE1  1 
ATOM   2908 C  CE2  . TYR   B 2 116 ? -11.139 -7.832  -0.896  1.00 45.59  ? 502  TYR   B CE2  1 
ATOM   2909 C  CZ   . TYR   B 2 116 ? -9.943  -7.547  -1.571  1.00 52.70  ? 502  TYR   B CZ   1 
ATOM   2910 O  OH   . TYR   B 2 116 ? -9.017  -8.529  -1.871  1.00 54.72  ? 502  TYR   B OH   1 
ATOM   2911 N  N    . GLN   B 2 117 ? -13.003 -1.713  1.896   1.00 41.51  ? 503  GLN   B N    1 
ATOM   2912 C  CA   . GLN   B 2 117 ? -13.408 -0.340  2.236   1.00 41.02  ? 503  GLN   B CA   1 
ATOM   2913 C  C    . GLN   B 2 117 ? -14.767 0.040   1.658   1.00 43.18  ? 503  GLN   B C    1 
ATOM   2914 O  O    . GLN   B 2 117 ? -15.020 1.217   1.362   1.00 38.74  ? 503  GLN   B O    1 
ATOM   2915 C  CB   . GLN   B 2 117 ? -12.344 0.668   1.789   1.00 42.23  ? 503  GLN   B CB   1 
ATOM   2916 C  CG   . GLN   B 2 117 ? -10.940 0.214   2.085   1.00 44.59  ? 503  GLN   B CG   1 
ATOM   2917 C  CD   . GLN   B 2 117 ? -9.930  1.340   1.948   1.00 56.19  ? 503  GLN   B CD   1 
ATOM   2918 O  OE1  . GLN   B 2 117 ? -9.559  1.992   2.923   1.00 64.26  ? 503  GLN   B OE1  1 
ATOM   2919 N  NE2  . GLN   B 2 117 ? -9.480  1.567   0.720   1.00 58.51  ? 503  GLN   B NE2  1 
ATOM   2920 N  N    . ARG   B 2 118 ? -15.648 -0.947  1.474   1.00 36.17  ? 504  ARG   B N    1 
ATOM   2921 C  CA   . ARG   B 2 118 ? -17.031 -0.651  1.138   1.00 42.01  ? 504  ARG   B CA   1 
ATOM   2922 C  C    . ARG   B 2 118 ? -17.892 -0.459  2.375   1.00 40.21  ? 504  ARG   B C    1 
ATOM   2923 O  O    . ARG   B 2 118 ? -18.961 0.161   2.288   1.00 38.63  ? 504  ARG   B O    1 
ATOM   2924 C  CB   . ARG   B 2 118 ? -17.622 -1.759  0.265   1.00 43.12  ? 504  ARG   B CB   1 
ATOM   2925 C  CG   . ARG   B 2 118 ? -17.148 -1.689  -1.177  1.00 46.26  ? 504  ARG   B CG   1 
ATOM   2926 C  CD   . ARG   B 2 118 ? -17.812 -2.776  -1.991  1.00 50.85  ? 504  ARG   B CD   1 
ATOM   2927 N  NE   . ARG   B 2 118 ? -17.327 -4.099  -1.637  1.00 41.45  ? 504  ARG   B NE   1 
ATOM   2928 C  CZ   . ARG   B 2 118 ? -16.271 -4.679  -2.191  1.00 51.20  ? 504  ARG   B CZ   1 
ATOM   2929 N  NH1  . ARG   B 2 118 ? -15.572 -4.078  -3.145  1.00 54.15  ? 504  ARG   B NH1  1 
ATOM   2930 N  NH2  . ARG   B 2 118 ? -15.913 -5.897  -1.783  1.00 49.77  ? 504  ARG   B NH2  1 
ATOM   2931 N  N    . ALA   B 2 119 ? -17.437 -0.973  3.513   1.00 37.89  ? 505  ALA   B N    1 
ATOM   2932 C  CA   . ALA   B 2 119 ? -18.015 -0.715  4.819   1.00 39.09  ? 505  ALA   B CA   1 
ATOM   2933 C  C    . ALA   B 2 119 ? -16.933 -0.232  5.769   1.00 40.36  ? 505  ALA   B C    1 
ATOM   2934 O  O    . ALA   B 2 119 ? -15.767 -0.647  5.682   1.00 36.94  ? 505  ALA   B O    1 
ATOM   2935 C  CB   . ALA   B 2 119 ? -18.663 -1.959  5.428   1.00 33.56  ? 505  ALA   B CB   1 
ATOM   2936 N  N    . VAL   B 2 120 ? -17.354 0.624   6.700   1.00 36.95  ? 506  VAL   B N    1 
ATOM   2937 C  CA   . VAL   B 2 120 ? -16.477 1.114   7.752   1.00 39.58  ? 506  VAL   B CA   1 
ATOM   2938 C  C    . VAL   B 2 120 ? -16.424 0.108   8.894   1.00 37.40  ? 506  VAL   B C    1 
ATOM   2939 O  O    . VAL   B 2 120 ? -15.409 0.006   9.603   1.00 35.15  ? 506  VAL   B O    1 
ATOM   2940 C  CB   . VAL   B 2 120 ? -16.974 2.490   8.226   1.00 40.21  ? 506  VAL   B CB   1 
ATOM   2941 C  CG1  . VAL   B 2 120 ? -16.276 2.920   9.514   1.00 42.31  ? 506  VAL   B CG1  1 
ATOM   2942 C  CG2  . VAL   B 2 120 ? -16.831 3.530   7.121   1.00 45.86  ? 506  VAL   B CG2  1 
ATOM   2943 N  N    . MET   B 2 121 ? -17.498 -0.661  9.082   1.00 38.95  ? 507  MET   B N    1 
ATOM   2944 C  CA   . MET   B 2 121 ? -17.473 -1.736  10.055  1.00 35.83  ? 507  MET   B CA   1 
ATOM   2945 C  C    . MET   B 2 121 ? -18.503 -2.783  9.653   1.00 33.90  ? 507  MET   B C    1 
ATOM   2946 O  O    . MET   B 2 121 ? -19.420 -2.516  8.876   1.00 35.80  ? 507  MET   B O    1 
ATOM   2947 C  CB   . MET   B 2 121 ? -17.734 -1.231  11.485  1.00 42.78  ? 507  MET   B CB   1 
ATOM   2948 C  CG   . MET   B 2 121 ? -19.022 -0.489  11.726  1.00 42.24  ? 507  MET   B CG   1 
ATOM   2949 S  SD   . MET   B 2 121 ? -19.069 0.471   13.283  1.00 52.28  ? 507  MET   B SD   1 
ATOM   2950 C  CE   . MET   B 2 121 ? -17.371 0.942   13.422  1.00 51.52  ? 507  MET   B CE   1 
ATOM   2951 N  N    . ALA   B 2 122 ? -18.318 -3.984  10.187  1.00 32.22  ? 508  ALA   B N    1 
ATOM   2952 C  CA   . ALA   B 2 122 ? -19.214 -5.117  10.015  1.00 34.19  ? 508  ALA   B CA   1 
ATOM   2953 C  C    . ALA   B 2 122 ? -19.750 -5.497  11.383  1.00 34.28  ? 508  ALA   B C    1 
ATOM   2954 O  O    . ALA   B 2 122 ? -18.984 -5.589  12.347  1.00 33.11  ? 508  ALA   B O    1 
ATOM   2955 C  CB   . ALA   B 2 122 ? -18.498 -6.323  9.392   1.00 30.05  ? 508  ALA   B CB   1 
ATOM   2956 N  N    . VAL   B 2 123 ? -21.056 -5.716  11.462  1.00 34.73  ? 509  VAL   B N    1 
ATOM   2957 C  CA   . VAL   B 2 123 ? -21.757 -5.907  12.725  1.00 34.16  ? 509  VAL   B CA   1 
ATOM   2958 C  C    . VAL   B 2 123 ? -22.634 -7.139  12.573  1.00 32.16  ? 509  VAL   B C    1 
ATOM   2959 O  O    . VAL   B 2 123 ? -23.510 -7.178  11.700  1.00 35.19  ? 509  VAL   B O    1 
ATOM   2960 C  CB   . VAL   B 2 123 ? -22.616 -4.686  13.081  1.00 38.20  ? 509  VAL   B CB   1 
ATOM   2961 C  CG1  . VAL   B 2 123 ? -23.594 -5.019  14.201  1.00 40.17  ? 509  VAL   B CG1  1 
ATOM   2962 C  CG2  . VAL   B 2 123 ? -21.735 -3.478  13.375  1.00 38.90  ? 509  VAL   B CG2  1 
ATOM   2963 N  N    . GLY   B 2 124 ? -22.381 -8.153  13.374  1.00 30.25  ? 510  GLY   B N    1 
ATOM   2964 C  CA   . GLY   B 2 124 ? -23.275 -9.301  13.360  1.00 34.29  ? 510  GLY   B CA   1 
ATOM   2965 C  C    . GLY   B 2 124 ? -22.634 -10.469 14.079  1.00 34.23  ? 510  GLY   B C    1 
ATOM   2966 O  O    . GLY   B 2 124 ? -21.809 -10.283 14.974  1.00 35.21  ? 510  GLY   B O    1 
ATOM   2967 N  N    . SER   B 2 125 ? -23.026 -11.674 13.664  1.00 28.83  ? 511  SER   B N    1 
ATOM   2968 C  CA   . SER   B 2 125 ? -22.512 -12.900 14.280  1.00 31.42  ? 511  SER   B CA   1 
ATOM   2969 C  C    . SER   B 2 125 ? -21.176 -13.290 13.638  1.00 32.36  ? 511  SER   B C    1 
ATOM   2970 O  O    . SER   B 2 125 ? -21.000 -14.370 13.079  1.00 29.77  ? 511  SER   B O    1 
ATOM   2971 C  CB   . SER   B 2 125 ? -23.548 -14.014 14.174  1.00 31.16  ? 511  SER   B CB   1 
ATOM   2972 O  OG   . SER   B 2 125 ? -23.944 -14.170 12.828  1.00 27.83  ? 511  SER   B OG   1 
ATOM   2973 N  N    . LEU   B 2 126 ? -20.216 -12.374 13.755  1.00 27.59  ? 512  LEU   B N    1 
ATOM   2974 C  CA   . LEU   B 2 126 ? -18.945 -12.436 13.033  1.00 30.19  ? 512  LEU   B CA   1 
ATOM   2975 C  C    . LEU   B 2 126 ? -17.851 -12.903 13.985  1.00 30.45  ? 512  LEU   B C    1 
ATOM   2976 O  O    . LEU   B 2 126 ? -17.481 -12.176 14.910  1.00 30.37  ? 512  LEU   B O    1 
ATOM   2977 C  CB   . LEU   B 2 126 ? -18.607 -11.066 12.459  1.00 29.43  ? 512  LEU   B CB   1 
ATOM   2978 C  CG   . LEU   B 2 126 ? -17.405 -10.970 11.520  1.00 35.74  ? 512  LEU   B CG   1 
ATOM   2979 C  CD1  . LEU   B 2 126 ? -17.616 -11.843 10.266  1.00 32.21  ? 512  LEU   B CD1  1 
ATOM   2980 C  CD2  . LEU   B 2 126 ? -17.140 -9.503  11.134  1.00 32.13  ? 512  LEU   B CD2  1 
ATOM   2981 N  N    . THR   B 2 127 ? -17.322 -14.101 13.752  1.00 29.91  ? 513  THR   B N    1 
ATOM   2982 C  CA   . THR   B 2 127 ? -16.379 -14.711 14.690  1.00 32.68  ? 513  THR   B CA   1 
ATOM   2983 C  C    . THR   B 2 127 ? -14.968 -14.121 14.545  1.00 28.91  ? 513  THR   B C    1 
ATOM   2984 O  O    . THR   B 2 127 ? -14.450 -13.988 13.435  1.00 31.31  ? 513  THR   B O    1 
ATOM   2985 C  CB   . THR   B 2 127 ? -16.352 -16.226 14.483  1.00 30.70  ? 513  THR   B CB   1 
ATOM   2986 O  OG1  . THR   B 2 127 ? -17.603 -16.795 14.908  1.00 28.36  ? 513  THR   B OG1  1 
ATOM   2987 C  CG2  . THR   B 2 127 ? -15.213 -16.863 15.291  1.00 30.52  ? 513  THR   B CG2  1 
ATOM   2988 N  N    . ILE   B 2 128 ? -14.355 -13.764 15.672  1.00 28.51  ? 514  ILE   B N    1 
ATOM   2989 C  CA   . ILE   B 2 128 ? -12.968 -13.284 15.707  1.00 28.89  ? 514  ILE   B CA   1 
ATOM   2990 C  C    . ILE   B 2 128 ? -12.039 -14.478 15.530  1.00 28.80  ? 514  ILE   B C    1 
ATOM   2991 O  O    . ILE   B 2 128 ? -12.130 -15.453 16.287  1.00 29.61  ? 514  ILE   B O    1 
ATOM   2992 C  CB   . ILE   B 2 128 ? -12.679 -12.565 17.035  1.00 30.29  ? 514  ILE   B CB   1 
ATOM   2993 C  CG1  . ILE   B 2 128 ? -13.520 -11.289 17.176  1.00 32.67  ? 514  ILE   B CG1  1 
ATOM   2994 C  CG2  . ILE   B 2 128 ? -11.165 -12.321 17.243  1.00 28.27  ? 514  ILE   B CG2  1 
ATOM   2995 C  CD1  . ILE   B 2 128 ? -13.478 -10.708 18.595  1.00 33.31  ? 514  ILE   B CD1  1 
ATOM   2996 N  N    . ASN   B 2 129 ? -11.170 -14.439 14.516  1.00 32.05  ? 515  ASN   B N    1 
ATOM   2997 C  CA   . ASN   B 2 129 ? -10.114 -15.452 14.452  1.00 31.64  ? 515  ASN   B CA   1 
ATOM   2998 C  C    . ASN   B 2 129 ? -8.823  -14.838 13.917  1.00 35.13  ? 515  ASN   B C    1 
ATOM   2999 O  O    . ASN   B 2 129 ? -8.769  -13.666 13.522  1.00 31.56  ? 515  ASN   B O    1 
ATOM   3000 C  CB   . ASN   B 2 129 ? -10.531 -16.717 13.660  1.00 28.43  ? 515  ASN   B CB   1 
ATOM   3001 C  CG   . ASN   B 2 129 ? -10.767 -16.467 12.164  1.00 33.98  ? 515  ASN   B CG   1 
ATOM   3002 O  OD1  . ASN   B 2 129 ? -10.289 -15.489 11.601  1.00 30.14  ? 515  ASN   B OD1  1 
ATOM   3003 N  ND2  . ASN   B 2 129 ? -11.477 -17.399 11.511  1.00 31.94  ? 515  ASN   B ND2  1 
ATOM   3004 N  N    . GLU   B 2 130 ? -7.765  -15.649 13.916  1.00 30.09  ? 516  GLU   B N    1 
ATOM   3005 C  CA   . GLU   B 2 130 ? -6.441  -15.109 13.618  1.00 30.30  ? 516  GLU   B CA   1 
ATOM   3006 C  C    . GLU   B 2 130 ? -6.353  -14.598 12.182  1.00 31.57  ? 516  GLU   B C    1 
ATOM   3007 O  O    . GLU   B 2 130 ? -5.910  -13.470 11.948  1.00 32.38  ? 516  GLU   B O    1 
ATOM   3008 C  CB   . GLU   B 2 130 ? -5.366  -16.162 13.879  1.00 32.35  ? 516  GLU   B CB   1 
ATOM   3009 C  CG   . GLU   B 2 130 ? -3.963  -15.620 13.611  1.00 35.96  ? 516  GLU   B CG   1 
ATOM   3010 C  CD   . GLU   B 2 130 ? -2.884  -16.695 13.661  1.00 38.87  ? 516  GLU   B CD   1 
ATOM   3011 O  OE1  . GLU   B 2 130 ? -3.217  -17.898 13.553  1.00 39.90  ? 516  GLU   B OE1  1 
ATOM   3012 O  OE2  . GLU   B 2 130 ? -1.697  -16.324 13.774  1.00 40.63  ? 516  GLU   B OE2  1 
ATOM   3013 N  N    . GLU   B 2 131 ? -6.784  -15.405 11.203  1.00 33.08  ? 517  GLU   B N    1 
ATOM   3014 C  CA   . GLU   B 2 131 ? -6.571  -15.019 9.810   1.00 31.14  ? 517  GLU   B CA   1 
ATOM   3015 C  C    . GLU   B 2 131 ? -7.370  -13.775 9.451   1.00 33.61  ? 517  GLU   B C    1 
ATOM   3016 O  O    . GLU   B 2 131 ? -6.876  -12.916 8.719   1.00 34.37  ? 517  GLU   B O    1 
ATOM   3017 C  CB   . GLU   B 2 131 ? -6.885  -16.178 8.863   1.00 34.88  ? 517  GLU   B CB   1 
ATOM   3018 C  CG   . GLU   B 2 131 ? -8.348  -16.603 8.791   1.00 33.21  ? 517  GLU   B CG   1 
ATOM   3019 C  CD   . GLU   B 2 131 ? -8.606  -17.508 7.586   1.00 37.85  ? 517  GLU   B CD   1 
ATOM   3020 O  OE1  . GLU   B 2 131 ? -7.628  -17.895 6.901   1.00 38.82  ? 517  GLU   B OE1  1 
ATOM   3021 O  OE2  . GLU   B 2 131 ? -9.780  -17.839 7.327   1.00 34.82  ? 517  GLU   B OE2  1 
ATOM   3022 N  N    . ARG   B 2 132 ? -8.582  -13.630 9.996   1.00 33.39  ? 518  ARG   B N    1 
ATOM   3023 C  CA   . ARG   B 2 132 ? -9.346  -12.405 9.769   1.00 29.47  ? 518  ARG   B CA   1 
ATOM   3024 C  C    . ARG   B 2 132 ? -8.682  -11.203 10.438  1.00 35.97  ? 518  ARG   B C    1 
ATOM   3025 O  O    . ARG   B 2 132 ? -8.692  -10.084 9.894   1.00 35.55  ? 518  ARG   B O    1 
ATOM   3026 C  CB   . ARG   B 2 132 ? -10.775 -12.587 10.301  1.00 31.48  ? 518  ARG   B CB   1 
ATOM   3027 C  CG   . ARG   B 2 132 ? -11.608 -13.578 9.493   1.00 30.95  ? 518  ARG   B CG   1 
ATOM   3028 C  CD   . ARG   B 2 132 ? -12.903 -13.945 10.213  1.00 32.47  ? 518  ARG   B CD   1 
ATOM   3029 N  NE   . ARG   B 2 132 ? -13.726 -14.812 9.376   1.00 27.22  ? 518  ARG   B NE   1 
ATOM   3030 C  CZ   . ARG   B 2 132 ? -14.937 -15.240 9.704   1.00 27.72  ? 518  ARG   B CZ   1 
ATOM   3031 N  NH1  . ARG   B 2 132 ? -15.495 -14.920 10.865  1.00 28.33  ? 518  ARG   B NH1  1 
ATOM   3032 N  NH2  . ARG   B 2 132 ? -15.625 -15.965 8.827   1.00 26.68  ? 518  ARG   B NH2  1 
ATOM   3033 N  N    . SER   B 2 133 ? -8.123  -11.406 11.636  1.00 33.85  ? 519  SER   B N    1 
ATOM   3034 C  CA   . SER   B 2 133 ? -7.465  -10.307 12.329  1.00 35.21  ? 519  SER   B CA   1 
ATOM   3035 C  C    . SER   B 2 133 ? -6.235  -9.824  11.584  1.00 38.63  ? 519  SER   B C    1 
ATOM   3036 O  O    . SER   B 2 133 ? -5.740  -8.731  11.873  1.00 39.70  ? 519  SER   B O    1 
ATOM   3037 C  CB   . SER   B 2 133 ? -7.084  -10.736 13.743  1.00 35.23  ? 519  SER   B CB   1 
ATOM   3038 O  OG   . SER   B 2 133 ? -8.244  -11.083 14.472  1.00 33.60  ? 519  SER   B OG   1 
ATOM   3039 N  N    . GLU   B 2 134 ? -5.728  -10.617 10.636  1.00 37.28  ? 520  GLU   B N    1 
ATOM   3040 C  CA   . GLU   B 2 134 ? -4.595  -10.176 9.843   1.00 37.03  ? 520  GLU   B CA   1 
ATOM   3041 C  C    . GLU   B 2 134 ? -5.003  -9.133  8.818   1.00 40.98  ? 520  GLU   B C    1 
ATOM   3042 O  O    . GLU   B 2 134 ? -4.134  -8.405  8.339   1.00 40.43  ? 520  GLU   B O    1 
ATOM   3043 C  CB   . GLU   B 2 134 ? -3.927  -11.368 9.148   1.00 38.20  ? 520  GLU   B CB   1 
ATOM   3044 C  CG   . GLU   B 2 134 ? -3.257  -12.372 10.104  1.00 36.47  ? 520  GLU   B CG   1 
ATOM   3045 C  CD   . GLU   B 2 134 ? -2.595  -13.535 9.372   1.00 48.94  ? 520  GLU   B CD   1 
ATOM   3046 O  OE1  . GLU   B 2 134 ? -2.733  -13.625 8.132   1.00 51.98  ? 520  GLU   B OE1  1 
ATOM   3047 O  OE2  . GLU   B 2 134 ? -1.956  -14.374 10.043  1.00 52.68  ? 520  GLU   B OE2  1 
ATOM   3048 N  N    . VAL   B 2 135 ? -6.290  -9.041  8.476   1.00 38.24  ? 521  VAL   B N    1 
ATOM   3049 C  CA   . VAL   B 2 135 ? -6.752  -8.104  7.454   1.00 36.70  ? 521  VAL   B CA   1 
ATOM   3050 C  C    . VAL   B 2 135 ? -7.741  -7.065  7.981   1.00 37.82  ? 521  VAL   B C    1 
ATOM   3051 O  O    . VAL   B 2 135 ? -7.918  -6.025  7.336   1.00 36.37  ? 521  VAL   B O    1 
ATOM   3052 C  CB   . VAL   B 2 135 ? -7.368  -8.849  6.246   1.00 37.92  ? 521  VAL   B CB   1 
ATOM   3053 C  CG1  . VAL   B 2 135 ? -6.312  -9.749  5.566   1.00 39.48  ? 521  VAL   B CG1  1 
ATOM   3054 C  CG2  . VAL   B 2 135 ? -8.616  -9.676  6.647   1.00 37.51  ? 521  VAL   B CG2  1 
ATOM   3055 N  N    . VAL   B 2 136 ? -8.435  -7.304  9.091   1.00 36.81  ? 522  VAL   B N    1 
ATOM   3056 C  CA   . VAL   B 2 136 ? -9.280  -6.292  9.714   1.00 36.19  ? 522  VAL   B CA   1 
ATOM   3057 C  C    . VAL   B 2 136 ? -8.892  -6.197  11.180  1.00 41.81  ? 522  VAL   B C    1 
ATOM   3058 O  O    . VAL   B 2 136 ? -8.262  -7.098  11.735  1.00 40.32  ? 522  VAL   B O    1 
ATOM   3059 C  CB   . VAL   B 2 136 ? -10.789 -6.604  9.599   1.00 36.55  ? 522  VAL   B CB   1 
ATOM   3060 C  CG1  . VAL   B 2 136 ? -11.215 -6.713  8.159   1.00 35.27  ? 522  VAL   B CG1  1 
ATOM   3061 C  CG2  . VAL   B 2 136 ? -11.129 -7.900  10.357  1.00 34.24  ? 522  VAL   B CG2  1 
ATOM   3062 N  N    . ASP   B 2 137 ? -9.283  -5.087  11.807  1.00 35.99  ? 523  ASP   B N    1 
ATOM   3063 C  CA   . ASP   B 2 137 ? -9.247  -4.967  13.258  1.00 38.07  ? 523  ASP   B CA   1 
ATOM   3064 C  C    . ASP   B 2 137 ? -10.587 -5.418  13.824  1.00 37.88  ? 523  ASP   B C    1 
ATOM   3065 O  O    . ASP   B 2 137 ? -11.634 -5.210  13.208  1.00 39.19  ? 523  ASP   B O    1 
ATOM   3066 C  CB   . ASP   B 2 137 ? -8.970  -3.525  13.685  1.00 37.69  ? 523  ASP   B CB   1 
ATOM   3067 C  CG   . ASP   B 2 137 ? -7.506  -3.135  13.527  1.00 43.06  ? 523  ASP   B CG   1 
ATOM   3068 O  OD1  . ASP   B 2 137 ? -6.654  -4.020  13.279  1.00 38.99  ? 523  ASP   B OD1  1 
ATOM   3069 O  OD2  . ASP   B 2 137 ? -7.223  -1.932  13.649  1.00 44.70  ? 523  ASP   B OD2  1 
ATOM   3070 N  N    . PHE   B 2 138 ? -10.556 -6.033  15.000  1.00 34.62  ? 524  PHE   B N    1 
ATOM   3071 C  CA   . PHE   B 2 138 ? -11.775 -6.407  15.703  1.00 33.32  ? 524  PHE   B CA   1 
ATOM   3072 C  C    . PHE   B 2 138 ? -11.880 -5.632  17.010  1.00 35.31  ? 524  PHE   B C    1 
ATOM   3073 O  O    . PHE   B 2 138 ? -10.873 -5.390  17.679  1.00 34.48  ? 524  PHE   B O    1 
ATOM   3074 C  CB   . PHE   B 2 138 ? -11.786 -7.905  16.019  1.00 33.75  ? 524  PHE   B CB   1 
ATOM   3075 C  CG   . PHE   B 2 138 ? -12.210 -8.787  14.871  1.00 32.07  ? 524  PHE   B CG   1 
ATOM   3076 C  CD1  . PHE   B 2 138 ? -13.545 -8.917  14.519  1.00 32.13  ? 524  PHE   B CD1  1 
ATOM   3077 C  CD2  . PHE   B 2 138 ? -11.251 -9.514  14.156  1.00 31.73  ? 524  PHE   B CD2  1 
ATOM   3078 C  CE1  . PHE   B 2 138 ? -13.935 -9.770  13.462  1.00 29.43  ? 524  PHE   B CE1  1 
ATOM   3079 C  CE2  . PHE   B 2 138 ? -11.612 -10.348 13.101  1.00 31.60  ? 524  PHE   B CE2  1 
ATOM   3080 C  CZ   . PHE   B 2 138 ? -12.976 -10.488 12.755  1.00 31.10  ? 524  PHE   B CZ   1 
ATOM   3081 N  N    . SER   B 2 139 ? -13.105 -5.260  17.377  1.00 35.01  ? 525  SER   B N    1 
ATOM   3082 C  CA   . SER   B 2 139 ? -13.389 -4.807  18.728  1.00 34.65  ? 525  SER   B CA   1 
ATOM   3083 C  C    . SER   B 2 139 ? -13.119 -5.925  19.729  1.00 36.42  ? 525  SER   B C    1 
ATOM   3084 O  O    . SER   B 2 139 ? -12.862 -7.080  19.366  1.00 32.65  ? 525  SER   B O    1 
ATOM   3085 C  CB   . SER   B 2 139 ? -14.843 -4.389  18.853  1.00 34.71  ? 525  SER   B CB   1 
ATOM   3086 O  OG   . SER   B 2 139 ? -15.672 -5.539  18.779  1.00 35.76  ? 525  SER   B OG   1 
ATOM   3087 N  N    . VAL   B 2 140 ? -13.253 -5.601  21.011  1.00 37.33  ? 526  VAL   B N    1 
ATOM   3088 C  CA   . VAL   B 2 140 ? -13.303 -6.641  22.040  1.00 36.61  ? 526  VAL   B CA   1 
ATOM   3089 C  C    . VAL   B 2 140 ? -14.483 -7.546  21.716  1.00 33.41  ? 526  VAL   B C    1 
ATOM   3090 O  O    . VAL   B 2 140 ? -15.493 -7.064  21.189  1.00 32.48  ? 526  VAL   B O    1 
ATOM   3091 C  CB   . VAL   B 2 140 ? -13.461 -6.050  23.445  1.00 37.69  ? 526  VAL   B CB   1 
ATOM   3092 C  CG1  . VAL   B 2 140 ? -12.274 -5.151  23.783  1.00 39.59  ? 526  VAL   B CG1  1 
ATOM   3093 C  CG2  . VAL   B 2 140 ? -14.744 -5.261  23.516  1.00 37.52  ? 526  VAL   B CG2  1 
ATOM   3094 N  N    . PRO   B 2 141 ? -14.398 -8.850  21.976  1.00 32.04  ? 527  PRO   B N    1 
ATOM   3095 C  CA   . PRO   B 2 141 ? -15.570 -9.711  21.795  1.00 31.70  ? 527  PRO   B CA   1 
ATOM   3096 C  C    . PRO   B 2 141 ? -16.680 -9.310  22.750  1.00 34.54  ? 527  PRO   B C    1 
ATOM   3097 O  O    . PRO   B 2 141 ? -16.423 -8.864  23.867  1.00 31.68  ? 527  PRO   B O    1 
ATOM   3098 C  CB   . PRO   B 2 141 ? -15.036 -11.101 22.136  1.00 31.24  ? 527  PRO   B CB   1 
ATOM   3099 C  CG   . PRO   B 2 141 ? -13.869 -10.853 23.036  1.00 31.40  ? 527  PRO   B CG   1 
ATOM   3100 C  CD   . PRO   B 2 141 ? -13.256 -9.588  22.533  1.00 32.63  ? 527  PRO   B CD   1 
ATOM   3101 N  N    . PHE   B 2 142 ? -17.931 -9.500  22.314  1.00 29.36  ? 528  PHE   B N    1 
ATOM   3102 C  CA   . PHE   B 2 142 ? -19.071 -9.213  23.180  1.00 32.26  ? 528  PHE   B CA   1 
ATOM   3103 C  C    . PHE   B 2 142 ? -20.139 -10.306 23.184  1.00 33.59  ? 528  PHE   B C    1 
ATOM   3104 O  O    . PHE   B 2 142 ? -21.145 -10.156 23.885  1.00 37.47  ? 528  PHE   B O    1 
ATOM   3105 C  CB   . PHE   B 2 142 ? -19.706 -7.856  22.809  1.00 31.19  ? 528  PHE   B CB   1 
ATOM   3106 C  CG   . PHE   B 2 142 ? -20.100 -7.742  21.375  1.00 35.72  ? 528  PHE   B CG   1 
ATOM   3107 C  CD1  . PHE   B 2 142 ? -19.195 -7.288  20.429  1.00 37.67  ? 528  PHE   B CD1  1 
ATOM   3108 C  CD2  . PHE   B 2 142 ? -21.398 -8.056  20.976  1.00 37.37  ? 528  PHE   B CD2  1 
ATOM   3109 C  CE1  . PHE   B 2 142 ? -19.562 -7.182  19.090  1.00 38.30  ? 528  PHE   B CE1  1 
ATOM   3110 C  CE2  . PHE   B 2 142 ? -21.779 -7.957  19.651  1.00 39.51  ? 528  PHE   B CE2  1 
ATOM   3111 C  CZ   . PHE   B 2 142 ? -20.847 -7.511  18.701  1.00 40.81  ? 528  PHE   B CZ   1 
ATOM   3112 N  N    . VAL   B 2 143 ? -19.948 -11.397 22.439  1.00 33.91  ? 529  VAL   B N    1 
ATOM   3113 C  CA   . VAL   B 2 143 ? -20.724 -12.625 22.607  1.00 32.59  ? 529  VAL   B CA   1 
ATOM   3114 C  C    . VAL   B 2 143 ? -19.735 -13.782 22.561  1.00 33.41  ? 529  VAL   B C    1 
ATOM   3115 O  O    . VAL   B 2 143 ? -18.979 -13.915 21.592  1.00 30.90  ? 529  VAL   B O    1 
ATOM   3116 C  CB   . VAL   B 2 143 ? -21.811 -12.811 21.528  1.00 29.78  ? 529  VAL   B CB   1 
ATOM   3117 C  CG1  . VAL   B 2 143 ? -22.546 -14.131 21.716  1.00 35.03  ? 529  VAL   B CG1  1 
ATOM   3118 C  CG2  . VAL   B 2 143 ? -22.821 -11.661 21.549  1.00 32.02  ? 529  VAL   B CG2  1 
ATOM   3119 N  N    . GLU   B 2 144 ? -19.744 -14.622 23.598  1.00 30.84  ? 530  GLU   B N    1 
ATOM   3120 C  CA   . GLU   B 2 144 ? -18.837 -15.767 23.652  1.00 35.82  ? 530  GLU   B CA   1 
ATOM   3121 C  C    . GLU   B 2 144 ? -19.207 -16.772 22.577  1.00 34.55  ? 530  GLU   B C    1 
ATOM   3122 O  O    . GLU   B 2 144 ? -20.360 -17.194 22.481  1.00 30.68  ? 530  GLU   B O    1 
ATOM   3123 C  CB   . GLU   B 2 144 ? -18.912 -16.451 25.018  1.00 37.17  ? 530  GLU   B CB   1 
ATOM   3124 C  CG   . GLU   B 2 144 ? -18.183 -15.759 26.147  1.00 41.24  ? 530  GLU   B CG   1 
ATOM   3125 C  CD   . GLU   B 2 144 ? -18.228 -16.565 27.457  1.00 43.86  ? 530  GLU   B CD   1 
ATOM   3126 O  OE1  . GLU   B 2 144 ? -18.689 -17.723 27.443  1.00 47.95  ? 530  GLU   B OE1  1 
ATOM   3127 O  OE2  . GLU   B 2 144 ? -17.797 -16.039 28.501  1.00 43.49  ? 530  GLU   B OE2  1 
ATOM   3128 N  N    . THR   B 2 145 ? -18.239 -17.197 21.784  1.00 30.01  ? 531  THR   B N    1 
ATOM   3129 C  CA   . THR   B 2 145 ? -18.568 -18.262 20.859  1.00 27.61  ? 531  THR   B CA   1 
ATOM   3130 C  C    . THR   B 2 145 ? -17.344 -19.146 20.667  1.00 31.88  ? 531  THR   B C    1 
ATOM   3131 O  O    . THR   B 2 145 ? -16.379 -19.087 21.436  1.00 29.55  ? 531  THR   B O    1 
ATOM   3132 C  CB   . THR   B 2 145 ? -19.117 -17.695 19.543  1.00 28.58  ? 531  THR   B CB   1 
ATOM   3133 O  OG1  . THR   B 2 145 ? -19.730 -18.749 18.799  1.00 27.15  ? 531  THR   B OG1  1 
ATOM   3134 C  CG2  . THR   B 2 145 ? -18.022 -17.042 18.711  1.00 27.42  ? 531  THR   B CG2  1 
ATOM   3135 N  N    . GLY   B 2 146 ? -17.401 -19.976 19.649  1.00 31.33  ? 532  GLY   B N    1 
ATOM   3136 C  CA   . GLY   B 2 146 ? -16.388 -20.949 19.344  1.00 29.71  ? 532  GLY   B CA   1 
ATOM   3137 C  C    . GLY   B 2 146 ? -17.044 -22.079 18.564  1.00 26.93  ? 532  GLY   B C    1 
ATOM   3138 O  O    . GLY   B 2 146 ? -17.940 -21.829 17.761  1.00 29.63  ? 532  GLY   B O    1 
ATOM   3139 N  N    . ILE   B 2 147 ? -16.618 -23.301 18.827  1.00 27.35  ? 533  ILE   B N    1 
ATOM   3140 C  CA   . ILE   B 2 147 ? -17.122 -24.453 18.087  1.00 29.52  ? 533  ILE   B CA   1 
ATOM   3141 C  C    . ILE   B 2 147 ? -17.776 -25.385 19.081  1.00 34.46  ? 533  ILE   B C    1 
ATOM   3142 O  O    . ILE   B 2 147 ? -17.110 -25.841 20.019  1.00 33.97  ? 533  ILE   B O    1 
ATOM   3143 C  CB   . ILE   B 2 147 ? -16.012 -25.168 17.308  1.00 30.91  ? 533  ILE   B CB   1 
ATOM   3144 C  CG1  . ILE   B 2 147 ? -15.438 -24.244 16.248  1.00 29.77  ? 533  ILE   B CG1  1 
ATOM   3145 C  CG2  . ILE   B 2 147 ? -16.598 -26.377 16.614  1.00 32.73  ? 533  ILE   B CG2  1 
ATOM   3146 C  CD1  . ILE   B 2 147 ? -14.296 -24.879 15.455  1.00 30.35  ? 533  ILE   B CD1  1 
ATOM   3147 N  N    . SER   B 2 148 ? -19.091 -25.622 18.912  1.00 31.87  ? 534  SER   B N    1 
ATOM   3148 C  CA   . SER   B 2 148 ? -19.797 -26.631 19.684  1.00 29.25  ? 534  SER   B CA   1 
ATOM   3149 C  C    . SER   B 2 148 ? -20.331 -27.711 18.746  1.00 32.32  ? 534  SER   B C    1 
ATOM   3150 O  O    . SER   B 2 148 ? -20.283 -27.592 17.518  1.00 28.73  ? 534  SER   B O    1 
ATOM   3151 C  CB   . SER   B 2 148 ? -20.935 -26.004 20.503  1.00 34.38  ? 534  SER   B CB   1 
ATOM   3152 O  OG   . SER   B 2 148 ? -20.421 -25.114 21.491  1.00 33.32  ? 534  SER   B OG   1 
ATOM   3153 N  N    . VAL   B 2 149 ? -20.857 -28.774 19.343  1.00 33.08  ? 535  VAL   B N    1 
ATOM   3154 C  CA   . VAL   B 2 149 ? -21.394 -29.918 18.616  1.00 29.61  ? 535  VAL   B CA   1 
ATOM   3155 C  C    . VAL   B 2 149 ? -22.815 -30.132 19.095  1.00 36.31  ? 535  VAL   B C    1 
ATOM   3156 O  O    . VAL   B 2 149 ? -23.051 -30.296 20.301  1.00 33.93  ? 535  VAL   B O    1 
ATOM   3157 C  CB   . VAL   B 2 149 ? -20.565 -31.195 18.838  1.00 37.10  ? 535  VAL   B CB   1 
ATOM   3158 C  CG1  . VAL   B 2 149 ? -21.152 -32.349 18.023  1.00 37.33  ? 535  VAL   B CG1  1 
ATOM   3159 C  CG2  . VAL   B 2 149 ? -19.103 -30.961 18.503  1.00 38.10  ? 535  VAL   B CG2  1 
ATOM   3160 N  N    . MET   B 2 150 ? -23.761 -30.133 18.172  1.00 31.91  ? 536  MET   B N    1 
ATOM   3161 C  CA   . MET   B 2 150 ? -25.149 -30.349 18.537  1.00 32.99  ? 536  MET   B CA   1 
ATOM   3162 C  C    . MET   B 2 150 ? -25.551 -31.768 18.133  1.00 37.28  ? 536  MET   B C    1 
ATOM   3163 O  O    . MET   B 2 150 ? -25.276 -32.197 17.010  1.00 35.14  ? 536  MET   B O    1 
ATOM   3164 C  CB   . MET   B 2 150 ? -26.062 -29.313 17.878  1.00 32.68  ? 536  MET   B CB   1 
ATOM   3165 C  CG   . MET   B 2 150 ? -27.522 -29.646 18.061  1.00 38.19  ? 536  MET   B CG   1 
ATOM   3166 S  SD   . MET   B 2 150 ? -28.622 -28.316 17.569  1.00 40.36  ? 536  MET   B SD   1 
ATOM   3167 C  CE   . MET   B 2 150 ? -28.599 -27.223 18.993  1.00 37.86  ? 536  MET   B CE   1 
ATOM   3168 N  N    . VAL   B 2 151 ? -26.189 -32.497 19.053  1.00 33.39  ? 537  VAL   B N    1 
ATOM   3169 C  CA   . VAL   B 2 151 ? -26.613 -33.878 18.822  1.00 38.49  ? 537  VAL   B CA   1 
ATOM   3170 C  C    . VAL   B 2 151 ? -28.005 -34.087 19.411  1.00 43.33  ? 537  VAL   B C    1 
ATOM   3171 O  O    . VAL   B 2 151 ? -28.544 -33.233 20.113  1.00 38.69  ? 537  VAL   B O    1 
ATOM   3172 C  CB   . VAL   B 2 151 ? -25.640 -34.899 19.444  1.00 38.39  ? 537  VAL   B CB   1 
ATOM   3173 C  CG1  . VAL   B 2 151 ? -24.270 -34.810 18.793  1.00 36.84  ? 537  VAL   B CG1  1 
ATOM   3174 C  CG2  . VAL   B 2 151 ? -25.554 -34.675 20.936  1.00 39.91  ? 537  VAL   B CG2  1 
ATOM   3175 N  N    . SER   B 2 152 ? -28.592 -35.245 19.115  1.00 42.03  ? 538  SER   B N    1 
ATOM   3176 C  CA   . SER   B 2 152 ? -29.772 -35.666 19.853  1.00 47.09  ? 538  SER   B CA   1 
ATOM   3177 C  C    . SER   B 2 152 ? -29.376 -36.082 21.266  1.00 49.91  ? 538  SER   B C    1 
ATOM   3178 O  O    . SER   B 2 152 ? -28.302 -36.653 21.494  1.00 46.27  ? 538  SER   B O    1 
ATOM   3179 C  CB   . SER   B 2 152 ? -30.470 -36.826 19.151  1.00 46.99  ? 538  SER   B CB   1 
ATOM   3180 O  OG   . SER   B 2 152 ? -31.387 -37.434 20.030  1.00 60.33  ? 538  SER   B OG   1 
ATOM   3181 N  N    . ARG   B 2 153 ? -30.259 -35.796 22.221  1.00 51.74  ? 539  ARG   B N    1 
ATOM   3182 C  CA   . ARG   B 2 153 ? -29.948 -36.049 23.623  1.00 51.71  ? 539  ARG   B CA   1 
ATOM   3183 C  C    . ARG   B 2 153 ? -29.522 -37.501 23.821  1.00 51.36  ? 539  ARG   B C    1 
ATOM   3184 O  O    . ARG   B 2 153 ? -30.135 -38.421 23.276  1.00 50.16  ? 539  ARG   B O    1 
ATOM   3185 C  CB   . ARG   B 2 153 ? -31.162 -35.704 24.492  1.00 53.62  ? 539  ARG   B CB   1 
ATOM   3186 C  CG   . ARG   B 2 153 ? -30.843 -35.531 25.968  1.00 55.73  ? 539  ARG   B CG   1 
ATOM   3187 C  CD   . ARG   B 2 153 ? -32.038 -34.976 26.744  1.00 56.29  ? 539  ARG   B CD   1 
ATOM   3188 N  NE   . ARG   B 2 153 ? -31.607 -33.914 27.647  1.00 58.01  ? 539  ARG   B NE   1 
ATOM   3189 C  CZ   . ARG   B 2 153 ? -31.848 -32.624 27.460  1.00 56.35  ? 539  ARG   B CZ   1 
ATOM   3190 N  NH1  . ARG   B 2 153 ? -32.564 -32.197 26.436  1.00 59.52  ? 539  ARG   B NH1  1 
ATOM   3191 N  NH2  . ARG   B 2 153 ? -31.358 -31.740 28.324  1.00 61.83  ? 539  ARG   B NH2  1 
ATOM   3192 N  N    . GLY   B 2 154 ? -28.421 -37.696 24.551  1.00 54.59  ? 540  GLY   B N    1 
ATOM   3193 C  CA   . GLY   B 2 154 ? -27.902 -39.014 24.856  1.00 54.85  ? 540  GLY   B CA   1 
ATOM   3194 C  C    . GLY   B 2 154 ? -26.763 -39.489 23.971  1.00 58.99  ? 540  GLY   B C    1 
ATOM   3195 O  O    . GLY   B 2 154 ? -26.136 -40.507 24.297  1.00 52.87  ? 540  GLY   B O    1 
ATOM   3196 N  N    . THR   B 2 155 ? -26.477 -38.797 22.867  1.00 50.70  ? 541  THR   B N    1 
ATOM   3197 C  CA   . THR   B 2 155 ? -25.421 -39.247 21.968  1.00 52.99  ? 541  THR   B CA   1 
ATOM   3198 C  C    . THR   B 2 155 ? -24.073 -39.256 22.673  1.00 52.24  ? 541  THR   B C    1 
ATOM   3199 O  O    . THR   B 2 155 ? -23.662 -38.261 23.275  1.00 54.20  ? 541  THR   B O    1 
ATOM   3200 C  CB   . THR   B 2 155 ? -25.364 -38.357 20.732  1.00 54.04  ? 541  THR   B CB   1 
ATOM   3201 O  OG1  . THR   B 2 155 ? -26.634 -38.394 20.072  1.00 45.89  ? 541  THR   B OG1  1 
ATOM   3202 C  CG2  . THR   B 2 155 ? -24.248 -38.806 19.780  1.00 49.32  ? 541  THR   B CG2  1 
ATOM   3203 N  N    . GLN   B 2 156 ? -23.386 -40.390 22.595  1.00 50.20  ? 542  GLN   B N    1 
ATOM   3204 C  CA   . GLN   B 2 156 ? -22.121 -40.580 23.301  1.00 58.50  ? 542  GLN   B CA   1 
ATOM   3205 C  C    . GLN   B 2 156 ? -21.004 -40.041 22.416  1.00 58.52  ? 542  GLN   B C    1 
ATOM   3206 O  O    . GLN   B 2 156 ? -20.491 -40.728 21.534  1.00 61.92  ? 542  GLN   B O    1 
ATOM   3207 C  CB   . GLN   B 2 156 ? -21.912 -42.049 23.653  1.00 59.64  ? 542  GLN   B CB   1 
ATOM   3208 N  N    . VAL   B 2 157 ? -20.632 -38.787 22.651  1.00 58.30  ? 662  VAL   B N    1 
ATOM   3209 C  CA   . VAL   B 2 157 ? -19.519 -38.144 21.963  1.00 55.58  ? 662  VAL   B CA   1 
ATOM   3210 C  C    . VAL   B 2 157 ? -18.818 -37.239 22.960  1.00 52.51  ? 662  VAL   B C    1 
ATOM   3211 O  O    . VAL   B 2 157 ? -19.472 -36.477 23.678  1.00 56.20  ? 662  VAL   B O    1 
ATOM   3212 C  CB   . VAL   B 2 157 ? -19.993 -37.352 20.728  1.00 54.02  ? 662  VAL   B CB   1 
ATOM   3213 C  CG1  . VAL   B 2 157 ? -19.065 -36.191 20.442  1.00 54.87  ? 662  VAL   B CG1  1 
ATOM   3214 C  CG2  . VAL   B 2 157 ? -20.070 -38.282 19.536  1.00 52.27  ? 662  VAL   B CG2  1 
ATOM   3215 N  N    . THR   B 2 158 ? -17.489 -37.329 23.022  1.00 50.88  ? 663  THR   B N    1 
ATOM   3216 C  CA   . THR   B 2 158 ? -16.776 -36.539 24.018  1.00 50.84  ? 663  THR   B CA   1 
ATOM   3217 C  C    . THR   B 2 158 ? -16.602 -35.090 23.580  1.00 51.83  ? 663  THR   B C    1 
ATOM   3218 O  O    . THR   B 2 158 ? -16.674 -34.177 24.411  1.00 53.05  ? 663  THR   B O    1 
ATOM   3219 C  CB   . THR   B 2 158 ? -15.410 -37.165 24.320  1.00 50.42  ? 663  THR   B CB   1 
ATOM   3220 O  OG1  . THR   B 2 158 ? -14.547 -37.038 23.176  1.00 50.07  ? 663  THR   B OG1  1 
ATOM   3221 C  CG2  . THR   B 2 158 ? -15.564 -38.639 24.690  1.00 47.05  ? 663  THR   B CG2  1 
ATOM   3222 N  N    . GLY   B 2 159 ? -16.378 -34.858 22.293  1.00 46.80  ? 664  GLY   B N    1 
ATOM   3223 C  CA   . GLY   B 2 159 ? -15.880 -33.574 21.841  1.00 48.68  ? 664  GLY   B CA   1 
ATOM   3224 C  C    . GLY   B 2 159 ? -15.353 -33.698 20.427  1.00 50.54  ? 664  GLY   B C    1 
ATOM   3225 O  O    . GLY   B 2 159 ? -15.548 -34.721 19.766  1.00 48.21  ? 664  GLY   B O    1 
ATOM   3226 N  N    . LEU   B 2 160 ? -14.669 -32.643 19.976  1.00 46.26  ? 665  LEU   B N    1 
ATOM   3227 C  CA   . LEU   B 2 160 ? -14.079 -32.689 18.639  1.00 47.30  ? 665  LEU   B CA   1 
ATOM   3228 C  C    . LEU   B 2 160 ? -12.992 -33.739 18.555  1.00 47.84  ? 665  LEU   B C    1 
ATOM   3229 O  O    . LEU   B 2 160 ? -12.738 -34.290 17.477  1.00 49.90  ? 665  LEU   B O    1 
ATOM   3230 C  CB   . LEU   B 2 160 ? -13.503 -31.331 18.249  1.00 40.03  ? 665  LEU   B CB   1 
ATOM   3231 C  CG   . LEU   B 2 160 ? -14.475 -30.266 17.766  1.00 44.18  ? 665  LEU   B CG   1 
ATOM   3232 C  CD1  . LEU   B 2 160 ? -13.706 -29.006 17.374  1.00 42.57  ? 665  LEU   B CD1  1 
ATOM   3233 C  CD2  . LEU   B 2 160 ? -15.240 -30.822 16.589  1.00 47.56  ? 665  LEU   B CD2  1 
ATOM   3234 N  N    . SER   B 2 161 ? -12.340 -34.019 19.679  1.00 44.59  ? 666  SER   B N    1 
ATOM   3235 C  CA   . SER   B 2 161 ? -11.286 -35.012 19.769  1.00 47.26  ? 666  SER   B CA   1 
ATOM   3236 C  C    . SER   B 2 161 ? -11.810 -36.441 19.758  1.00 46.09  ? 666  SER   B C    1 
ATOM   3237 O  O    . SER   B 2 161 ? -11.002 -37.375 19.665  1.00 48.24  ? 666  SER   B O    1 
ATOM   3238 C  CB   . SER   B 2 161 ? -10.472 -34.775 21.047  1.00 55.59  ? 666  SER   B CB   1 
ATOM   3239 O  OG   . SER   B 2 161 ? -11.323 -34.703 22.186  1.00 58.53  ? 666  SER   B OG   1 
ATOM   3240 N  N    . ASP   B 2 162 ? -13.122 -36.640 19.870  1.00 46.21  ? 667  ASP   B N    1 
ATOM   3241 C  CA   . ASP   B 2 162 ? -13.657 -37.995 19.856  1.00 41.16  ? 667  ASP   B CA   1 
ATOM   3242 C  C    . ASP   B 2 162 ? -13.198 -38.739 18.606  1.00 42.04  ? 667  ASP   B C    1 
ATOM   3243 O  O    . ASP   B 2 162 ? -13.152 -38.181 17.503  1.00 35.75  ? 667  ASP   B O    1 
ATOM   3244 C  CB   . ASP   B 2 162 ? -15.185 -37.965 19.945  1.00 44.27  ? 667  ASP   B CB   1 
ATOM   3245 C  CG   . ASP   B 2 162 ? -15.760 -39.296 20.359  1.00 46.64  ? 667  ASP   B CG   1 
ATOM   3246 O  OD1  . ASP   B 2 162 ? -15.623 -40.267 19.578  1.00 46.56  ? 667  ASP   B OD1  1 
ATOM   3247 O  OD2  . ASP   B 2 162 ? -16.269 -39.391 21.499  1.00 46.62  ? 667  ASP   B OD2  1 
ATOM   3248 N  N    . LYS   B 2 163 ? -12.827 -40.009 18.790  1.00 38.30  ? 668  LYS   B N    1 
ATOM   3249 C  CA   . LYS   B 2 163 ? -12.362 -40.810 17.668  1.00 38.69  ? 668  LYS   B CA   1 
ATOM   3250 C  C    . LYS   B 2 163 ? -13.426 -40.937 16.589  1.00 42.15  ? 668  LYS   B C    1 
ATOM   3251 O  O    . LYS   B 2 163 ? -13.090 -41.144 15.415  1.00 39.75  ? 668  LYS   B O    1 
ATOM   3252 C  CB   . LYS   B 2 163 ? -11.916 -42.199 18.148  1.00 41.58  ? 668  LYS   B CB   1 
ATOM   3253 C  CG   . LYS   B 2 163 ? -11.328 -43.080 17.037  1.00 49.57  ? 668  LYS   B CG   1 
ATOM   3254 C  CD   . LYS   B 2 163 ? -10.430 -44.205 17.564  1.00 51.04  ? 668  LYS   B CD   1 
ATOM   3255 C  CE   . LYS   B 2 163 ? -11.241 -45.318 18.214  1.00 60.61  ? 668  LYS   B CE   1 
ATOM   3256 N  NZ   . LYS   B 2 163 ? -10.383 -46.255 18.995  1.00 66.26  ? 668  LYS   B NZ   1 
ATOM   3257 N  N    . LYS   B 2 164 ? -14.715 -40.843 16.957  1.00 39.34  ? 669  LYS   B N    1 
ATOM   3258 C  CA   . LYS   B 2 164 ? -15.757 -40.950 15.941  1.00 38.05  ? 669  LYS   B CA   1 
ATOM   3259 C  C    . LYS   B 2 164 ? -15.650 -39.823 14.927  1.00 38.40  ? 669  LYS   B C    1 
ATOM   3260 O  O    . LYS   B 2 164 ? -16.000 -40.014 13.758  1.00 39.45  ? 669  LYS   B O    1 
ATOM   3261 C  CB   . LYS   B 2 164 ? -17.156 -40.945 16.572  1.00 42.01  ? 669  LYS   B CB   1 
ATOM   3262 C  CG   . LYS   B 2 164 ? -17.504 -42.156 17.411  1.00 40.89  ? 669  LYS   B CG   1 
ATOM   3263 C  CD   . LYS   B 2 164 ? -18.884 -41.981 18.070  1.00 49.38  ? 669  LYS   B CD   1 
ATOM   3264 C  CE   . LYS   B 2 164 ? -19.156 -43.099 19.079  1.00 62.12  ? 669  LYS   B CE   1 
ATOM   3265 N  NZ   . LYS   B 2 164 ? -20.469 -42.933 19.771  1.00 64.44  ? 669  LYS   B NZ   1 
ATOM   3266 N  N    . PHE   B 2 165 ? -15.183 -38.647 15.366  1.00 34.43  ? 670  PHE   B N    1 
ATOM   3267 C  CA   . PHE   B 2 165 ? -14.936 -37.511 14.483  1.00 37.06  ? 670  PHE   B CA   1 
ATOM   3268 C  C    . PHE   B 2 165 ? -13.559 -37.604 13.850  1.00 40.64  ? 670  PHE   B C    1 
ATOM   3269 O  O    . PHE   B 2 165 ? -13.412 -37.377 12.645  1.00 34.71  ? 670  PHE   B O    1 
ATOM   3270 C  CB   . PHE   B 2 165 ? -15.026 -36.197 15.257  1.00 34.99  ? 670  PHE   B CB   1 
ATOM   3271 C  CG   . PHE   B 2 165 ? -16.402 -35.819 15.668  1.00 37.31  ? 670  PHE   B CG   1 
ATOM   3272 C  CD1  . PHE   B 2 165 ? -17.455 -35.949 14.795  1.00 38.39  ? 670  PHE   B CD1  1 
ATOM   3273 C  CD2  . PHE   B 2 165 ? -16.641 -35.304 16.930  1.00 43.79  ? 670  PHE   B CD2  1 
ATOM   3274 C  CE1  . PHE   B 2 165 ? -18.739 -35.603 15.177  1.00 43.20  ? 670  PHE   B CE1  1 
ATOM   3275 C  CE2  . PHE   B 2 165 ? -17.917 -34.950 17.314  1.00 44.57  ? 670  PHE   B CE2  1 
ATOM   3276 C  CZ   . PHE   B 2 165 ? -18.969 -35.103 16.438  1.00 40.64  ? 670  PHE   B CZ   1 
ATOM   3277 N  N    . GLN   B 2 166 ? -12.549 -37.938 14.665  1.00 36.48  ? 671  GLN   B N    1 
ATOM   3278 C  CA   . GLN   B 2 166 ? -11.168 -37.878 14.210  1.00 41.85  ? 671  GLN   B CA   1 
ATOM   3279 C  C    . GLN   B 2 166 ? -10.847 -38.995 13.235  1.00 39.59  ? 671  GLN   B C    1 
ATOM   3280 O  O    . GLN   B 2 166 ? -10.094 -38.787 12.277  1.00 37.30  ? 671  GLN   B O    1 
ATOM   3281 C  CB   . GLN   B 2 166 ? -10.222 -37.938 15.403  1.00 38.09  ? 671  GLN   B CB   1 
ATOM   3282 C  CG   . GLN   B 2 166 ? -10.430 -36.803 16.384  1.00 41.64  ? 671  GLN   B CG   1 
ATOM   3283 C  CD   . GLN   B 2 166 ? -9.582  -35.612 16.032  1.00 51.26  ? 671  GLN   B CD   1 
ATOM   3284 O  OE1  . GLN   B 2 166 ? -10.078 -34.658 15.422  1.00 49.13  ? 671  GLN   B OE1  1 
ATOM   3285 N  NE2  . GLN   B 2 166 ? -8.275  -35.697 16.314  1.00 50.08  ? 671  GLN   B NE2  1 
ATOM   3286 N  N    . ARG   B 2 167 ? -11.373 -40.196 13.476  1.00 37.40  ? 672  ARG   B N    1 
ATOM   3287 C  CA   . ARG   B 2 167 ? -11.100 -41.366 12.645  1.00 37.13  ? 672  ARG   B CA   1 
ATOM   3288 C  C    . ARG   B 2 167 ? -12.419 -42.025 12.263  1.00 40.72  ? 672  ARG   B C    1 
ATOM   3289 O  O    . ARG   B 2 167 ? -12.665 -43.190 12.593  1.00 38.40  ? 672  ARG   B O    1 
ATOM   3290 C  CB   . ARG   B 2 167 ? -10.164 -42.348 13.359  1.00 47.14  ? 672  ARG   B CB   1 
ATOM   3291 C  CG   . ARG   B 2 167 ? -8.779  -41.764 13.693  1.00 45.02  ? 672  ARG   B CG   1 
ATOM   3292 C  CD   . ARG   B 2 167 ? -7.888  -42.783 14.435  1.00 49.14  ? 672  ARG   B CD   1 
ATOM   3293 N  NE   . ARG   B 2 167 ? -7.834  -44.057 13.727  1.00 51.44  ? 672  ARG   B NE   1 
ATOM   3294 C  CZ   . ARG   B 2 167 ? -6.954  -44.384 12.791  1.00 57.46  ? 672  ARG   B CZ   1 
ATOM   3295 N  NH1  . ARG   B 2 167 ? -5.998  -43.550 12.419  1.00 58.01  ? 672  ARG   B NH1  1 
ATOM   3296 N  NH2  . ARG   B 2 167 ? -7.042  -45.576 12.208  1.00 54.72  ? 672  ARG   B NH2  1 
ATOM   3297 N  N    . PRO   B 2 168 ? -13.269 -41.315 11.511  1.00 38.19  ? 673  PRO   B N    1 
ATOM   3298 C  CA   . PRO   B 2 168 ? -14.659 -41.780 11.320  1.00 36.12  ? 673  PRO   B CA   1 
ATOM   3299 C  C    . PRO   B 2 168 ? -14.800 -43.139 10.677  1.00 42.35  ? 673  PRO   B C    1 
ATOM   3300 O  O    . PRO   B 2 168 ? -15.779 -43.848 10.967  1.00 45.58  ? 673  PRO   B O    1 
ATOM   3301 C  CB   . PRO   B 2 168 ? -15.292 -40.675 10.458  1.00 38.90  ? 673  PRO   B CB   1 
ATOM   3302 C  CG   . PRO   B 2 168 ? -14.169 -39.933 9.836   1.00 41.45  ? 673  PRO   B CG   1 
ATOM   3303 C  CD   . PRO   B 2 168 ? -12.928 -40.144 10.684  1.00 37.66  ? 673  PRO   B CD   1 
ATOM   3304 N  N    . HIS   B 2 169 ? -13.867 -43.552 9.826   1.00 40.06  ? 674  HIS   B N    1 
ATOM   3305 C  CA   . HIS   B 2 169 ? -13.992 -44.869 9.214   1.00 42.79  ? 674  HIS   B CA   1 
ATOM   3306 C  C    . HIS   B 2 169 ? -13.469 -45.992 10.096  1.00 43.97  ? 674  HIS   B C    1 
ATOM   3307 O  O    . HIS   B 2 169 ? -13.421 -47.144 9.650   1.00 48.75  ? 674  HIS   B O    1 
ATOM   3308 C  CB   . HIS   B 2 169 ? -13.298 -44.875 7.859   1.00 45.58  ? 674  HIS   B CB   1 
ATOM   3309 C  CG   . HIS   B 2 169 ? -14.145 -44.289 6.774   1.00 45.42  ? 674  HIS   B CG   1 
ATOM   3310 N  ND1  . HIS   B 2 169 ? -13.857 -43.082 6.177   1.00 47.46  ? 674  HIS   B ND1  1 
ATOM   3311 C  CD2  . HIS   B 2 169 ? -15.281 -44.736 6.193   1.00 46.10  ? 674  HIS   B CD2  1 
ATOM   3312 C  CE1  . HIS   B 2 169 ? -14.780 -42.809 5.271   1.00 44.84  ? 674  HIS   B CE1  1 
ATOM   3313 N  NE2  . HIS   B 2 169 ? -15.650 -43.803 5.254   1.00 49.94  ? 674  HIS   B NE2  1 
ATOM   3314 N  N    . ASP   B 2 170 ? -13.095 -45.697 11.332  1.00 43.53  ? 675  ASP   B N    1 
ATOM   3315 C  CA   . ASP   B 2 170 ? -12.870 -46.759 12.301  1.00 48.41  ? 675  ASP   B CA   1 
ATOM   3316 C  C    . ASP   B 2 170 ? -14.172 -47.372 12.803  1.00 51.62  ? 675  ASP   B C    1 
ATOM   3317 O  O    . ASP   B 2 170 ? -14.120 -48.349 13.555  1.00 50.33  ? 675  ASP   B O    1 
ATOM   3318 C  CB   . ASP   B 2 170 ? -12.067 -46.239 13.499  1.00 46.46  ? 675  ASP   B CB   1 
ATOM   3319 C  CG   . ASP   B 2 170 ? -10.581 -46.019 13.184  1.00 50.46  ? 675  ASP   B CG   1 
ATOM   3320 O  OD1  . ASP   B 2 170 ? -10.153 -46.191 12.022  1.00 49.03  ? 675  ASP   B OD1  1 
ATOM   3321 O  OD2  . ASP   B 2 170 ? -9.838  -45.666 14.124  1.00 48.92  ? 675  ASP   B OD2  1 
ATOM   3322 N  N    . TYR   B 2 171 ? -15.329 -46.818 12.431  1.00 45.57  ? 676  TYR   B N    1 
ATOM   3323 C  CA   . TYR   B 2 171 ? -16.614 -47.305 12.918  1.00 49.12  ? 676  TYR   B CA   1 
ATOM   3324 C  C    . TYR   B 2 171 ? -17.503 -47.707 11.751  1.00 49.73  ? 676  TYR   B C    1 
ATOM   3325 O  O    . TYR   B 2 171 ? -17.521 -47.037 10.715  1.00 46.89  ? 676  TYR   B O    1 
ATOM   3326 C  CB   . TYR   B 2 171 ? -17.360 -46.257 13.773  1.00 47.88  ? 676  TYR   B CB   1 
ATOM   3327 C  CG   . TYR   B 2 171 ? -16.564 -45.703 14.939  1.00 48.06  ? 676  TYR   B CG   1 
ATOM   3328 C  CD1  . TYR   B 2 171 ? -15.425 -44.939 14.740  1.00 47.07  ? 676  TYR   B CD1  1 
ATOM   3329 C  CD2  . TYR   B 2 171 ? -16.870 -46.083 16.238  1.00 47.54  ? 676  TYR   B CD2  1 
ATOM   3330 C  CE1  . TYR   B 2 171 ? -14.687 -44.475 15.798  1.00 46.50  ? 676  TYR   B CE1  1 
ATOM   3331 C  CE2  . TYR   B 2 171 ? -16.126 -45.638 17.307  1.00 47.45  ? 676  TYR   B CE2  1 
ATOM   3332 C  CZ   . TYR   B 2 171 ? -15.036 -44.838 17.081  1.00 48.69  ? 676  TYR   B CZ   1 
ATOM   3333 O  OH   . TYR   B 2 171 ? -14.298 -44.387 18.150  1.00 57.40  ? 676  TYR   B OH   1 
ATOM   3334 N  N    . SER   B 2 172 ? -18.245 -48.800 11.923  1.00 49.97  ? 677  SER   B N    1 
ATOM   3335 C  CA   . SER   B 2 172 ? -19.218 -49.254 10.924  1.00 51.66  ? 677  SER   B CA   1 
ATOM   3336 C  C    . SER   B 2 172 ? -20.609 -49.335 11.535  1.00 51.68  ? 677  SER   B C    1 
ATOM   3337 O  O    . SER   B 2 172 ? -20.818 -50.114 12.484  1.00 60.09  ? 677  SER   B O    1 
ATOM   3338 C  CB   . SER   B 2 172 ? -18.828 -50.610 10.338  1.00 58.02  ? 677  SER   B CB   1 
ATOM   3339 O  OG   . SER   B 2 172 ? -17.960 -50.446 9.234   1.00 65.93  ? 677  SER   B OG   1 
ATOM   3340 N  N    . PRO   B 2 173 ? -21.586 -48.550 11.059  1.00 50.89  ? 678  PRO   B N    1 
ATOM   3341 C  CA   . PRO   B 2 173 ? -21.482 -47.488 10.057  1.00 50.70  ? 678  PRO   B CA   1 
ATOM   3342 C  C    . PRO   B 2 173 ? -20.738 -46.300 10.647  1.00 43.48  ? 678  PRO   B C    1 
ATOM   3343 O  O    . PRO   B 2 173 ? -20.692 -46.126 11.862  1.00 43.75  ? 678  PRO   B O    1 
ATOM   3344 C  CB   . PRO   B 2 173 ? -22.951 -47.139 9.750   1.00 49.11  ? 678  PRO   B CB   1 
ATOM   3345 C  CG   . PRO   B 2 173 ? -23.755 -48.242 10.320  1.00 51.82  ? 678  PRO   B CG   1 
ATOM   3346 C  CD   . PRO   B 2 173 ? -22.977 -48.729 11.492  1.00 51.61  ? 678  PRO   B CD   1 
ATOM   3347 N  N    . PRO   B 2 174 ? -20.116 -45.481 9.810   1.00 44.15  ? 679  PRO   B N    1 
ATOM   3348 C  CA   . PRO   B 2 174 ? -19.411 -44.304 10.326  1.00 41.47  ? 679  PRO   B CA   1 
ATOM   3349 C  C    . PRO   B 2 174 ? -20.386 -43.240 10.799  1.00 43.84  ? 679  PRO   B C    1 
ATOM   3350 O  O    . PRO   B 2 174 ? -21.532 -43.162 10.353  1.00 40.84  ? 679  PRO   B O    1 
ATOM   3351 C  CB   . PRO   B 2 174 ? -18.604 -43.815 9.122   1.00 42.53  ? 679  PRO   B CB   1 
ATOM   3352 C  CG   . PRO   B 2 174 ? -19.363 -44.322 7.933   1.00 42.18  ? 679  PRO   B CG   1 
ATOM   3353 C  CD   . PRO   B 2 174 ? -19.940 -45.652 8.358   1.00 43.09  ? 679  PRO   B CD   1 
ATOM   3354 N  N    . PHE   B 2 175 ? -19.897 -42.413 11.724  1.00 40.99  ? 680  PHE   B N    1 
ATOM   3355 C  CA   . PHE   B 2 175 ? -20.652 -41.282 12.244  1.00 39.47  ? 680  PHE   B CA   1 
ATOM   3356 C  C    . PHE   B 2 175 ? -20.916 -40.261 11.143  1.00 41.68  ? 680  PHE   B C    1 
ATOM   3357 O  O    . PHE   B 2 175 ? -20.018 -39.916 10.373  1.00 39.51  ? 680  PHE   B O    1 
ATOM   3358 C  CB   . PHE   B 2 175 ? -19.869 -40.643 13.381  1.00 42.30  ? 680  PHE   B CB   1 
ATOM   3359 C  CG   . PHE   B 2 175 ? -20.707 -40.106 14.493  1.00 42.62  ? 680  PHE   B CG   1 
ATOM   3360 C  CD1  . PHE   B 2 175 ? -21.632 -40.906 15.136  1.00 44.27  ? 680  PHE   B CD1  1 
ATOM   3361 C  CD2  . PHE   B 2 175 ? -20.510 -38.809 14.951  1.00 41.15  ? 680  PHE   B CD2  1 
ATOM   3362 C  CE1  . PHE   B 2 175 ? -22.385 -40.408 16.170  1.00 43.68  ? 680  PHE   B CE1  1 
ATOM   3363 C  CE2  . PHE   B 2 175 ? -21.255 -38.312 15.997  1.00 46.07  ? 680  PHE   B CE2  1 
ATOM   3364 C  CZ   . PHE   B 2 175 ? -22.201 -39.116 16.603  1.00 43.61  ? 680  PHE   B CZ   1 
ATOM   3365 N  N    . ARG   B 2 176 ? -22.150 -39.779 11.060  1.00 38.89  ? 681  ARG   B N    1 
ATOM   3366 C  CA   . ARG   B 2 176 ? -22.521 -38.783 10.066  1.00 38.63  ? 681  ARG   B CA   1 
ATOM   3367 C  C    . ARG   B 2 176 ? -22.548 -37.421 10.746  1.00 34.38  ? 681  ARG   B C    1 
ATOM   3368 O  O    . ARG   B 2 176 ? -23.370 -37.185 11.640  1.00 34.54  ? 681  ARG   B O    1 
ATOM   3369 C  CB   . ARG   B 2 176 ? -23.873 -39.104 9.436   1.00 35.27  ? 681  ARG   B CB   1 
ATOM   3370 C  CG   . ARG   B 2 176 ? -23.954 -40.514 8.832   1.00 42.35  ? 681  ARG   B CG   1 
ATOM   3371 C  CD   . ARG   B 2 176 ? -25.405 -40.917 8.582   1.00 44.29  ? 681  ARG   B CD   1 
ATOM   3372 N  NE   . ARG   B 2 176 ? -26.128 -40.949 9.847   1.00 43.32  ? 681  ARG   B NE   1 
ATOM   3373 C  CZ   . ARG   B 2 176 ? -27.441 -41.049 9.967   1.00 43.09  ? 681  ARG   B CZ   1 
ATOM   3374 N  NH1  . ARG   B 2 176 ? -28.229 -41.130 8.906   1.00 49.03  ? 681  ARG   B NH1  1 
ATOM   3375 N  NH2  . ARG   B 2 176 ? -27.979 -41.046 11.183  1.00 46.45  ? 681  ARG   B NH2  1 
ATOM   3376 N  N    . PHE   B 2 177 ? -21.652 -36.536 10.328  1.00 29.99  ? 682  PHE   B N    1 
ATOM   3377 C  CA   . PHE   B 2 177 ? -21.579 -35.208 10.935  1.00 28.73  ? 682  PHE   B CA   1 
ATOM   3378 C  C    . PHE   B 2 177 ? -21.137 -34.197 9.891   1.00 30.61  ? 682  PHE   B C    1 
ATOM   3379 O  O    . PHE   B 2 177 ? -20.328 -34.508 9.015   1.00 30.52  ? 682  PHE   B O    1 
ATOM   3380 C  CB   . PHE   B 2 177 ? -20.631 -35.187 12.140  1.00 34.49  ? 682  PHE   B CB   1 
ATOM   3381 C  CG   . PHE   B 2 177 ? -19.227 -35.657 11.833  1.00 34.80  ? 682  PHE   B CG   1 
ATOM   3382 C  CD1  . PHE   B 2 177 ? -18.927 -37.015 11.811  1.00 36.34  ? 682  PHE   B CD1  1 
ATOM   3383 C  CD2  . PHE   B 2 177 ? -18.201 -34.748 11.620  1.00 36.51  ? 682  PHE   B CD2  1 
ATOM   3384 C  CE1  . PHE   B 2 177 ? -17.631 -37.455 11.560  1.00 35.16  ? 682  PHE   B CE1  1 
ATOM   3385 C  CE2  . PHE   B 2 177 ? -16.906 -35.187 11.355  1.00 36.26  ? 682  PHE   B CE2  1 
ATOM   3386 C  CZ   . PHE   B 2 177 ? -16.626 -36.542 11.325  1.00 35.45  ? 682  PHE   B CZ   1 
ATOM   3387 N  N    . GLY   B 2 178 ? -21.666 -32.967 10.007  1.00 30.73  ? 683  GLY   B N    1 
ATOM   3388 C  CA   . GLY   B 2 178 ? -21.346 -31.926 9.050   1.00 31.09  ? 683  GLY   B CA   1 
ATOM   3389 C  C    . GLY   B 2 178 ? -21.415 -30.549 9.678   1.00 32.19  ? 683  GLY   B C    1 
ATOM   3390 O  O    . GLY   B 2 178 ? -21.886 -30.382 10.804  1.00 29.84  ? 683  GLY   B O    1 
ATOM   3391 N  N    . THR   B 2 179 ? -20.961 -29.553 8.918   1.00 27.87  ? 684  THR   B N    1 
ATOM   3392 C  CA   . THR   B 2 179 ? -21.086 -28.149 9.300   1.00 31.35  ? 684  THR   B CA   1 
ATOM   3393 C  C    . THR   B 2 179 ? -21.746 -27.387 8.143   1.00 32.00  ? 684  THR   B C    1 
ATOM   3394 O  O    . THR   B 2 179 ? -22.043 -27.961 7.090   1.00 32.80  ? 684  THR   B O    1 
ATOM   3395 C  CB   . THR   B 2 179 ? -19.713 -27.548 9.653   1.00 29.28  ? 684  THR   B CB   1 
ATOM   3396 O  OG1  . THR   B 2 179 ? -19.893 -26.263 10.264  1.00 30.80  ? 684  THR   B OG1  1 
ATOM   3397 C  CG2  . THR   B 2 179 ? -18.847 -27.373 8.409   1.00 33.18  ? 684  THR   B CG2  1 
ATOM   3398 N  N    . VAL   B 2 180 ? -21.989 -26.091 8.331   1.00 30.01  ? 685  VAL   B N    1 
ATOM   3399 C  CA   . VAL   B 2 180 ? -22.288 -25.180 7.233   1.00 27.36  ? 685  VAL   B CA   1 
ATOM   3400 C  C    . VAL   B 2 180 ? -20.951 -24.631 6.721   1.00 32.87  ? 685  VAL   B C    1 
ATOM   3401 O  O    . VAL   B 2 180 ? -20.235 -23.977 7.496   1.00 30.28  ? 685  VAL   B O    1 
ATOM   3402 C  CB   . VAL   B 2 180 ? -23.210 -24.031 7.661   1.00 33.23  ? 685  VAL   B CB   1 
ATOM   3403 C  CG1  . VAL   B 2 180 ? -23.406 -23.048 6.491   1.00 29.51  ? 685  VAL   B CG1  1 
ATOM   3404 C  CG2  . VAL   B 2 180 ? -24.540 -24.575 8.158   1.00 33.58  ? 685  VAL   B CG2  1 
ATOM   3405 N  N    . PRO   B 2 181 ? -20.595 -24.862 5.462   1.00 32.12  ? 686  PRO   B N    1 
ATOM   3406 C  CA   . PRO   B 2 181 ? -19.228 -24.570 5.012   1.00 32.13  ? 686  PRO   B CA   1 
ATOM   3407 C  C    . PRO   B 2 181 ? -18.959 -23.072 4.885   1.00 33.04  ? 686  PRO   B C    1 
ATOM   3408 O  O    . PRO   B 2 181 ? -19.852 -22.227 4.953   1.00 26.41  ? 686  PRO   B O    1 
ATOM   3409 C  CB   . PRO   B 2 181 ? -19.159 -25.269 3.645   1.00 33.46  ? 686  PRO   B CB   1 
ATOM   3410 C  CG   . PRO   B 2 181 ? -20.576 -25.286 3.170   1.00 32.95  ? 686  PRO   B CG   1 
ATOM   3411 C  CD   . PRO   B 2 181 ? -21.433 -25.434 4.394   1.00 30.83  ? 686  PRO   B CD   1 
ATOM   3412 N  N    . ASN   B 2 182 ? -17.671 -22.760 4.739   1.00 28.16  ? 687  ASN   B N    1 
ATOM   3413 C  CA   . ASN   B 2 182 ? -17.102 -21.465 4.370   1.00 28.26  ? 687  ASN   B CA   1 
ATOM   3414 C  C    . ASN   B 2 182 ? -17.065 -20.412 5.473   1.00 31.06  ? 687  ASN   B C    1 
ATOM   3415 O  O    . ASN   B 2 182 ? -16.725 -19.258 5.180   1.00 30.65  ? 687  ASN   B O    1 
ATOM   3416 C  CB   . ASN   B 2 182 ? -17.820 -20.872 3.155   1.00 29.55  ? 687  ASN   B CB   1 
ATOM   3417 C  CG   . ASN   B 2 182 ? -17.767 -21.804 1.958   1.00 37.31  ? 687  ASN   B CG   1 
ATOM   3418 O  OD1  . ASN   B 2 182 ? -16.843 -22.619 1.843   1.00 34.05  ? 687  ASN   B OD1  1 
ATOM   3419 N  ND2  . ASN   B 2 182 ? -18.768 -21.708 1.071   1.00 37.34  ? 687  ASN   B ND2  1 
ATOM   3420 N  N    . GLY   B 2 183 ? -17.359 -20.756 6.725   1.00 28.37  ? 688  GLY   B N    1 
ATOM   3421 C  CA   . GLY   B 2 183 ? -17.183 -19.853 7.835   1.00 27.88  ? 688  GLY   B CA   1 
ATOM   3422 C  C    . GLY   B 2 183 ? -16.041 -20.265 8.752   1.00 29.77  ? 688  GLY   B C    1 
ATOM   3423 O  O    . GLY   B 2 183 ? -15.225 -21.138 8.439   1.00 29.05  ? 688  GLY   B O    1 
ATOM   3424 N  N    . SER   B 2 184 ? -16.011 -19.632 9.926   1.00 27.91  ? 689  SER   B N    1 
ATOM   3425 C  CA   . SER   B 2 184 ? -14.893 -19.826 10.843  1.00 30.12  ? 689  SER   B CA   1 
ATOM   3426 C  C    . SER   B 2 184 ? -14.799 -21.270 11.323  1.00 31.72  ? 689  SER   B C    1 
ATOM   3427 O  O    . SER   B 2 184 ? -13.692 -21.762 11.589  1.00 28.43  ? 689  SER   B O    1 
ATOM   3428 C  CB   . SER   B 2 184 ? -15.027 -18.873 12.035  1.00 31.25  ? 689  SER   B CB   1 
ATOM   3429 O  OG   . SER   B 2 184 ? -16.263 -19.131 12.697  1.00 29.16  ? 689  SER   B OG   1 
ATOM   3430 N  N    . THR   B 2 185 ? -15.940 -21.966 11.434  1.00 28.09  ? 690  THR   B N    1 
ATOM   3431 C  CA   . THR   B 2 185 ? -15.917 -23.344 11.920  1.00 29.60  ? 690  THR   B CA   1 
ATOM   3432 C  C    . THR   B 2 185 ? -15.245 -24.275 10.915  1.00 28.85  ? 690  THR   B C    1 
ATOM   3433 O  O    . THR   B 2 185 ? -14.378 -25.078 11.286  1.00 27.60  ? 690  THR   B O    1 
ATOM   3434 C  CB   . THR   B 2 185 ? -17.329 -23.822 12.252  1.00 30.52  ? 690  THR   B CB   1 
ATOM   3435 O  OG1  . THR   B 2 185 ? -17.832 -23.069 13.365  1.00 30.67  ? 690  THR   B OG1  1 
ATOM   3436 C  CG2  . THR   B 2 185 ? -17.321 -25.315 12.627  1.00 26.48  ? 690  THR   B CG2  1 
ATOM   3437 N  N    . GLU   B 2 186 ? -15.611 -24.176 9.631   1.00 29.06  ? 691  GLU   B N    1 
ATOM   3438 C  CA   . GLU   B 2 186 ? -14.970 -25.045 8.646   1.00 32.71  ? 691  GLU   B CA   1 
ATOM   3439 C  C    . GLU   B 2 186 ? -13.492 -24.722 8.509   1.00 31.94  ? 691  GLU   B C    1 
ATOM   3440 O  O    . GLU   B 2 186 ? -12.669 -25.631 8.360   1.00 30.52  ? 691  GLU   B O    1 
ATOM   3441 C  CB   . GLU   B 2 186 ? -15.633 -24.960 7.269   1.00 32.56  ? 691  GLU   B CB   1 
ATOM   3442 C  CG   . GLU   B 2 186 ? -14.960 -25.971 6.308   1.00 35.22  ? 691  GLU   B CG   1 
ATOM   3443 C  CD   . GLU   B 2 186 ? -15.426 -25.927 4.861   1.00 33.80  ? 691  GLU   B CD   1 
ATOM   3444 O  OE1  . GLU   B 2 186 ? -15.927 -24.875 4.412   1.00 35.28  ? 691  GLU   B OE1  1 
ATOM   3445 O  OE2  . GLU   B 2 186 ? -15.292 -26.969 4.168   1.00 35.18  ? 691  GLU   B OE2  1 
ATOM   3446 N  N    . ARG   B 2 187 ? -13.141 -23.439 8.535   1.00 27.89  ? 692  ARG   B N    1 
ATOM   3447 C  CA   . ARG   B 2 187 ? -11.727 -23.062 8.488   1.00 28.96  ? 692  ARG   B CA   1 
ATOM   3448 C  C    . ARG   B 2 187 ? -10.926 -23.744 9.588   1.00 31.84  ? 692  ARG   B C    1 
ATOM   3449 O  O    . ARG   B 2 187 ? -9.811  -24.231 9.355   1.00 32.12  ? 692  ARG   B O    1 
ATOM   3450 C  CB   . ARG   B 2 187 ? -11.580 -21.554 8.621   1.00 31.81  ? 692  ARG   B CB   1 
ATOM   3451 C  CG   . ARG   B 2 187 ? -10.162 -21.027 8.362   1.00 34.92  ? 692  ARG   B CG   1 
ATOM   3452 C  CD   . ARG   B 2 187 ? -9.862  -21.068 6.882   1.00 37.25  ? 692  ARG   B CD   1 
ATOM   3453 N  NE   . ARG   B 2 187 ? -8.440  -21.041 6.582   1.00 41.87  ? 692  ARG   B NE   1 
ATOM   3454 C  CZ   . ARG   B 2 187 ? -7.639  -22.096 6.571   1.00 50.62  ? 692  ARG   B CZ   1 
ATOM   3455 N  NH1  . ARG   B 2 187 ? -8.087  -23.311 6.851   1.00 48.72  ? 692  ARG   B NH1  1 
ATOM   3456 N  NH2  . ARG   B 2 187 ? -6.360  -21.932 6.242   1.00 52.89  ? 692  ARG   B NH2  1 
ATOM   3457 N  N    . ASN   B 2 188 ? -11.444 -23.703 10.815  1.00 30.39  ? 693  ASN   B N    1 
ATOM   3458 C  CA   . ASN   B 2 188 ? -10.729 -24.288 11.937  1.00 32.52  ? 693  ASN   B CA   1 
ATOM   3459 C  C    . ASN   B 2 188 ? -10.583 -25.796 11.775  1.00 30.60  ? 693  ASN   B C    1 
ATOM   3460 O  O    . ASN   B 2 188 ? -9.521  -26.356 12.054  1.00 34.17  ? 693  ASN   B O    1 
ATOM   3461 C  CB   . ASN   B 2 188 ? -11.464 -23.974 13.238  1.00 32.19  ? 693  ASN   B CB   1 
ATOM   3462 C  CG   . ASN   B 2 188 ? -10.720 -24.500 14.444  1.00 37.92  ? 693  ASN   B CG   1 
ATOM   3463 O  OD1  . ASN   B 2 188 ? -10.888 -25.664 14.826  1.00 39.43  ? 693  ASN   B OD1  1 
ATOM   3464 N  ND2  . ASN   B 2 188 ? -9.840  -23.675 15.008  1.00 35.70  ? 693  ASN   B ND2  1 
ATOM   3465 N  N    . ILE   B 2 189 ? -11.657 -26.475 11.388  1.00 29.34  ? 694  ILE   B N    1 
ATOM   3466 C  CA   . ILE   B 2 189 ? -11.588 -27.924 11.212  1.00 32.15  ? 694  ILE   B CA   1 
ATOM   3467 C  C    . ILE   B 2 189 ? -10.620 -28.276 10.089  1.00 29.75  ? 694  ILE   B C    1 
ATOM   3468 O  O    . ILE   B 2 189 ? -9.785  -29.182 10.222  1.00 29.43  ? 694  ILE   B O    1 
ATOM   3469 C  CB   . ILE   B 2 189 ? -12.997 -28.482 10.953  1.00 32.16  ? 694  ILE   B CB   1 
ATOM   3470 C  CG1  . ILE   B 2 189 ? -13.837 -28.325 12.228  1.00 35.23  ? 694  ILE   B CG1  1 
ATOM   3471 C  CG2  . ILE   B 2 189 ? -12.923 -29.949 10.543  1.00 31.89  ? 694  ILE   B CG2  1 
ATOM   3472 C  CD1  . ILE   B 2 189 ? -15.261 -28.816 12.087  1.00 38.06  ? 694  ILE   B CD1  1 
ATOM   3473 N  N    . ARG   B 2 190 ? -10.690 -27.545 8.974   1.00 29.23  ? 695  ARG   B N    1 
ATOM   3474 C  CA   . ARG   B 2 190 ? -9.781  -27.821 7.866   1.00 32.16  ? 695  ARG   B CA   1 
ATOM   3475 C  C    . ARG   B 2 190 ? -8.324  -27.661 8.300   1.00 33.40  ? 695  ARG   B C    1 
ATOM   3476 O  O    . ARG   B 2 190 ? -7.450  -28.410 7.855   1.00 35.87  ? 695  ARG   B O    1 
ATOM   3477 C  CB   . ARG   B 2 190 ? -10.101 -26.892 6.682   1.00 32.97  ? 695  ARG   B CB   1 
ATOM   3478 C  CG   . ARG   B 2 190 ? -9.191  -27.100 5.459   1.00 32.86  ? 695  ARG   B CG   1 
ATOM   3479 C  CD   . ARG   B 2 190 ? -9.307  -25.942 4.452   1.00 36.31  ? 695  ARG   B CD   1 
ATOM   3480 N  NE   . ARG   B 2 190 ? -10.616 -25.911 3.803   1.00 38.23  ? 695  ARG   B NE   1 
ATOM   3481 C  CZ   . ARG   B 2 190 ? -10.934 -26.620 2.723   1.00 41.13  ? 695  ARG   B CZ   1 
ATOM   3482 N  NH1  . ARG   B 2 190 ? -10.076 -27.471 2.177   1.00 42.40  ? 695  ARG   B NH1  1 
ATOM   3483 N  NH2  . ARG   B 2 190 ? -12.146 -26.477 2.179   1.00 40.89  ? 695  ARG   B NH2  1 
ATOM   3484 N  N    . ASN   B 2 191 ? -8.039  -26.687 9.167   1.00 33.00  ? 696  ASN   B N    1 
ATOM   3485 C  CA   . ASN   B 2 191 ? -6.660  -26.503 9.599   1.00 36.55  ? 696  ASN   B CA   1 
ATOM   3486 C  C    . ASN   B 2 191 ? -6.222  -27.553 10.616  1.00 36.69  ? 696  ASN   B C    1 
ATOM   3487 O  O    . ASN   B 2 191 ? -5.097  -28.049 10.540  1.00 37.29  ? 696  ASN   B O    1 
ATOM   3488 C  CB   . ASN   B 2 191 ? -6.450  -25.108 10.187  1.00 40.88  ? 696  ASN   B CB   1 
ATOM   3489 C  CG   . ASN   B 2 191 ? -6.242  -24.057 9.120   1.00 50.63  ? 696  ASN   B CG   1 
ATOM   3490 O  OD1  . ASN   B 2 191 ? -6.733  -22.930 9.236   1.00 52.23  ? 696  ASN   B OD1  1 
ATOM   3491 N  ND2  . ASN   B 2 191 ? -5.547  -24.439 8.036   1.00 52.93  ? 696  ASN   B ND2  1 
ATOM   3492 N  N    . ASN   B 2 192 ? -7.083  -27.907 11.574  1.00 32.56  ? 697  ASN   B N    1 
ATOM   3493 C  CA   . ASN   B 2 192 ? -6.642  -28.731 12.696  1.00 33.79  ? 697  ASN   B CA   1 
ATOM   3494 C  C    . ASN   B 2 192 ? -6.778  -30.231 12.437  1.00 35.81  ? 697  ASN   B C    1 
ATOM   3495 O  O    . ASN   B 2 192 ? -5.958  -31.011 12.934  1.00 36.19  ? 697  ASN   B O    1 
ATOM   3496 C  CB   . ASN   B 2 192 ? -7.433  -28.386 13.958  1.00 30.97  ? 697  ASN   B CB   1 
ATOM   3497 C  CG   . ASN   B 2 192 ? -7.098  -27.019 14.512  1.00 38.77  ? 697  ASN   B CG   1 
ATOM   3498 O  OD1  . ASN   B 2 192 ? -5.957  -26.537 14.414  1.00 40.86  ? 697  ASN   B OD1  1 
ATOM   3499 N  ND2  . ASN   B 2 192 ? -8.094  -26.397 15.147  1.00 40.20  ? 697  ASN   B ND2  1 
ATOM   3500 N  N    . TYR   B 2 193 ? -7.798  -30.664 11.687  1.00 32.60  ? 698  TYR   B N    1 
ATOM   3501 C  CA   . TYR   B 2 193 ? -8.129  -32.091 11.540  1.00 30.77  ? 698  TYR   B CA   1 
ATOM   3502 C  C    . TYR   B 2 193 ? -8.348  -32.438 10.075  1.00 31.31  ? 698  TYR   B C    1 
ATOM   3503 O  O    . TYR   B 2 193 ? -9.496  -32.569 9.620   1.00 32.83  ? 698  TYR   B O    1 
ATOM   3504 C  CB   . TYR   B 2 193 ? -9.365  -32.457 12.366  1.00 34.25  ? 698  TYR   B CB   1 
ATOM   3505 C  CG   . TYR   B 2 193 ? -9.409  -31.809 13.741  1.00 40.24  ? 698  TYR   B CG   1 
ATOM   3506 C  CD1  . TYR   B 2 193 ? -8.533  -32.203 14.743  1.00 39.36  ? 698  TYR   B CD1  1 
ATOM   3507 C  CD2  . TYR   B 2 193 ? -10.332 -30.805 14.035  1.00 37.88  ? 698  TYR   B CD2  1 
ATOM   3508 C  CE1  . TYR   B 2 193 ? -8.570  -31.608 16.006  1.00 43.31  ? 698  TYR   B CE1  1 
ATOM   3509 C  CE2  . TYR   B 2 193 ? -10.369 -30.203 15.280  1.00 40.47  ? 698  TYR   B CE2  1 
ATOM   3510 C  CZ   . TYR   B 2 193 ? -9.485  -30.609 16.266  1.00 46.60  ? 698  TYR   B CZ   1 
ATOM   3511 O  OH   . TYR   B 2 193 ? -9.515  -30.006 17.516  1.00 50.02  ? 698  TYR   B OH   1 
ATOM   3512 N  N    . PRO   B 2 194 ? -7.271  -32.616 9.309   1.00 30.85  ? 699  PRO   B N    1 
ATOM   3513 C  CA   . PRO   B 2 194 ? -7.441  -32.770 7.854   1.00 32.26  ? 699  PRO   B CA   1 
ATOM   3514 C  C    . PRO   B 2 194 ? -8.270  -33.970 7.451   1.00 31.48  ? 699  PRO   B C    1 
ATOM   3515 O  O    . PRO   B 2 194 ? -9.089  -33.846 6.533   1.00 31.56  ? 699  PRO   B O    1 
ATOM   3516 C  CB   . PRO   B 2 194 ? -5.995  -32.854 7.342   1.00 33.24  ? 699  PRO   B CB   1 
ATOM   3517 C  CG   . PRO   B 2 194 ? -5.211  -32.069 8.355   1.00 34.05  ? 699  PRO   B CG   1 
ATOM   3518 C  CD   . PRO   B 2 194 ? -5.862  -32.383 9.674   1.00 31.99  ? 699  PRO   B CD   1 
ATOM   3519 N  N    . TYR   B 2 195 ? -8.110  -35.122 8.114   1.00 30.60  ? 700  TYR   B N    1 
ATOM   3520 C  CA   . TYR   B 2 195 ? -8.902  -36.285 7.715   1.00 32.75  ? 700  TYR   B CA   1 
ATOM   3521 C  C    . TYR   B 2 195 ? -10.383 -36.094 8.045   1.00 32.91  ? 700  TYR   B C    1 
ATOM   3522 O  O    . TYR   B 2 195 ? -11.253 -36.361 7.207   1.00 31.78  ? 700  TYR   B O    1 
ATOM   3523 C  CB   . TYR   B 2 195 ? -8.366  -37.540 8.386   1.00 33.37  ? 700  TYR   B CB   1 
ATOM   3524 C  CG   . TYR   B 2 195 ? -9.003  -38.804 7.886   1.00 35.71  ? 700  TYR   B CG   1 
ATOM   3525 C  CD1  . TYR   B 2 195 ? -8.616  -39.373 6.676   1.00 35.94  ? 700  TYR   B CD1  1 
ATOM   3526 C  CD2  . TYR   B 2 195 ? -9.981  -39.448 8.627   1.00 40.74  ? 700  TYR   B CD2  1 
ATOM   3527 C  CE1  . TYR   B 2 195 ? -9.208  -40.549 6.217   1.00 42.25  ? 700  TYR   B CE1  1 
ATOM   3528 C  CE2  . TYR   B 2 195 ? -10.556 -40.625 8.180   1.00 43.13  ? 700  TYR   B CE2  1 
ATOM   3529 C  CZ   . TYR   B 2 195 ? -10.169 -41.161 6.973   1.00 44.21  ? 700  TYR   B CZ   1 
ATOM   3530 O  OH   . TYR   B 2 195 ? -10.741 -42.326 6.533   1.00 49.20  ? 700  TYR   B OH   1 
ATOM   3531 N  N    . MET   B 2 196 ? -10.686 -35.625 9.255   1.00 33.20  ? 701  MET   B N    1 
ATOM   3532 C  CA   . MET   B 2 196 ? -12.070 -35.290 9.602   1.00 34.42  ? 701  MET   B CA   1 
ATOM   3533 C  C    . MET   B 2 196 ? -12.684 -34.335 8.587   1.00 31.96  ? 701  MET   B C    1 
ATOM   3534 O  O    . MET   B 2 196 ? -13.818 -34.538 8.122   1.00 34.98  ? 701  MET   B O    1 
ATOM   3535 C  CB   . MET   B 2 196 ? -12.101 -34.681 11.009  1.00 28.91  ? 701  MET   B CB   1 
ATOM   3536 C  CG   . MET   B 2 196 ? -13.462 -34.214 11.534  1.00 36.56  ? 701  MET   B CG   1 
ATOM   3537 S  SD   . MET   B 2 196 ? -13.141 -33.306 13.068  1.00 41.18  ? 701  MET   B SD   1 
ATOM   3538 C  CE   . MET   B 2 196 ? -14.638 -32.379 13.233  1.00 39.57  ? 701  MET   B CE   1 
ATOM   3539 N  N    . HIS   B 2 197 ? -11.946 -33.291 8.220   1.00 31.63  ? 702  HIS   B N    1 
ATOM   3540 C  CA   . HIS   B 2 197 ? -12.501 -32.287 7.329   1.00 31.88  ? 702  HIS   B CA   1 
ATOM   3541 C  C    . HIS   B 2 197 ? -12.851 -32.866 5.961   1.00 34.72  ? 702  HIS   B C    1 
ATOM   3542 O  O    . HIS   B 2 197 ? -13.932 -32.598 5.422   1.00 33.81  ? 702  HIS   B O    1 
ATOM   3543 C  CB   . HIS   B 2 197 ? -11.531 -31.127 7.152   1.00 31.14  ? 702  HIS   B CB   1 
ATOM   3544 C  CG   . HIS   B 2 197 ? -12.011 -30.141 6.138   1.00 33.70  ? 702  HIS   B CG   1 
ATOM   3545 N  ND1  . HIS   B 2 197 ? -11.577 -30.138 4.830   1.00 36.28  ? 702  HIS   B ND1  1 
ATOM   3546 C  CD2  . HIS   B 2 197 ? -12.968 -29.190 6.223   1.00 33.02  ? 702  HIS   B CD2  1 
ATOM   3547 C  CE1  . HIS   B 2 197 ? -12.212 -29.186 4.166   1.00 40.89  ? 702  HIS   B CE1  1 
ATOM   3548 N  NE2  . HIS   B 2 197 ? -13.058 -28.592 4.990   1.00 35.39  ? 702  HIS   B NE2  1 
ATOM   3549 N  N    . GLN   B 2 198 ? -11.932 -33.625 5.355   1.00 34.50  ? 703  GLN   B N    1 
ATOM   3550 C  CA   . GLN   B 2 198 ? -12.241 -34.173 4.040   1.00 32.44  ? 703  GLN   B CA   1 
ATOM   3551 C  C    . GLN   B 2 198 ? -13.368 -35.198 4.121   1.00 39.21  ? 703  GLN   B C    1 
ATOM   3552 O  O    . GLN   B 2 198 ? -14.140 -35.344 3.163   1.00 36.00  ? 703  GLN   B O    1 
ATOM   3553 C  CB   . GLN   B 2 198 ? -10.984 -34.763 3.410   1.00 38.07  ? 703  GLN   B CB   1 
ATOM   3554 C  CG   . GLN   B 2 198 ? -10.401 -35.967 4.147   1.00 35.18  ? 703  GLN   B CG   1 
ATOM   3555 C  CD   . GLN   B 2 198 ? -11.013 -37.254 3.701   1.00 39.10  ? 703  GLN   B CD   1 
ATOM   3556 O  OE1  . GLN   B 2 198 ? -11.230 -37.456 2.500   1.00 39.02  ? 703  GLN   B OE1  1 
ATOM   3557 N  NE2  . GLN   B 2 198 ? -11.301 -38.152 4.659   1.00 35.56  ? 703  GLN   B NE2  1 
ATOM   3558 N  N    . TYR   B 2 199 ? -13.506 -35.891 5.261   1.00 32.42  ? 704  TYR   B N    1 
ATOM   3559 C  CA   . TYR   B 2 199 ? -14.633 -36.799 5.417   1.00 34.93  ? 704  TYR   B CA   1 
ATOM   3560 C  C    . TYR   B 2 199 ? -15.942 -36.027 5.503   1.00 35.19  ? 704  TYR   B C    1 
ATOM   3561 O  O    . TYR   B 2 199 ? -16.978 -36.480 5.003   1.00 34.11  ? 704  TYR   B O    1 
ATOM   3562 C  CB   . TYR   B 2 199 ? -14.446 -37.659 6.672   1.00 35.12  ? 704  TYR   B CB   1 
ATOM   3563 C  CG   . TYR   B 2 199 ? -15.667 -38.473 7.031   1.00 35.55  ? 704  TYR   B CG   1 
ATOM   3564 C  CD1  . TYR   B 2 199 ? -15.877 -39.718 6.473   1.00 37.29  ? 704  TYR   B CD1  1 
ATOM   3565 C  CD2  . TYR   B 2 199 ? -16.604 -37.995 7.945   1.00 39.79  ? 704  TYR   B CD2  1 
ATOM   3566 C  CE1  . TYR   B 2 199 ? -16.980 -40.463 6.794   1.00 40.10  ? 704  TYR   B CE1  1 
ATOM   3567 C  CE2  . TYR   B 2 199 ? -17.721 -38.741 8.274   1.00 35.66  ? 704  TYR   B CE2  1 
ATOM   3568 C  CZ   . TYR   B 2 199 ? -17.900 -39.972 7.703   1.00 40.74  ? 704  TYR   B CZ   1 
ATOM   3569 O  OH   . TYR   B 2 199 ? -19.018 -40.728 8.014   1.00 44.48  ? 704  TYR   B OH   1 
ATOM   3570 N  N    . MET   B 2 200 ? -15.890 -34.855 6.125   1.00 36.23  ? 705  MET   B N    1 
ATOM   3571 C  CA   . MET   B 2 200 ? -17.065 -34.093 6.535   1.00 37.07  ? 705  MET   B CA   1 
ATOM   3572 C  C    . MET   B 2 200 ? -17.784 -33.486 5.347   1.00 37.95  ? 705  MET   B C    1 
ATOM   3573 O  O    . MET   B 2 200 ? -19.001 -33.263 5.406   1.00 36.50  ? 705  MET   B O    1 
ATOM   3574 C  CB   . MET   B 2 200 ? -16.579 -32.970 7.440   1.00 41.45  ? 705  MET   B CB   1 
ATOM   3575 C  CG   . MET   B 2 200 ? -16.809 -33.180 8.852   1.00 42.29  ? 705  MET   B CG   1 
ATOM   3576 S  SD   . MET   B 2 200 ? -16.285 -31.680 9.628   1.00 35.79  ? 705  MET   B SD   1 
ATOM   3577 C  CE   . MET   B 2 200 ? -17.688 -30.635 9.262   1.00 42.80  ? 705  MET   B CE   1 
ATOM   3578 N  N    . THR   B 2 201 ? -17.037 -33.162 4.288   1.00 36.91  ? 706  THR   B N    1 
ATOM   3579 C  CA   . THR   B 2 201 ? -17.580 -32.293 3.248   1.00 37.82  ? 706  THR   B CA   1 
ATOM   3580 C  C    . THR   B 2 201 ? -18.819 -32.893 2.601   1.00 37.74  ? 706  THR   B C    1 
ATOM   3581 O  O    . THR   B 2 201 ? -19.730 -32.151 2.231   1.00 34.66  ? 706  THR   B O    1 
ATOM   3582 C  CB   . THR   B 2 201 ? -16.510 -31.979 2.199   1.00 40.14  ? 706  THR   B CB   1 
ATOM   3583 O  OG1  . THR   B 2 201 ? -15.924 -33.193 1.737   1.00 40.69  ? 706  THR   B OG1  1 
ATOM   3584 C  CG2  . THR   B 2 201 ? -15.422 -31.078 2.790   1.00 41.21  ? 706  THR   B CG2  1 
ATOM   3585 N  N    . LYS   B 2 202 ? -18.906 -34.226 2.508   1.00 35.48  ? 707  LYS   B N    1 
ATOM   3586 C  CA   . LYS   B 2 202 ? -20.123 -34.813 1.954   1.00 33.05  ? 707  LYS   B CA   1 
ATOM   3587 C  C    . LYS   B 2 202 ? -21.345 -34.546 2.821   1.00 36.71  ? 707  LYS   B C    1 
ATOM   3588 O  O    . LYS   B 2 202 ? -22.466 -34.697 2.332   1.00 35.05  ? 707  LYS   B O    1 
ATOM   3589 C  CB   . LYS   B 2 202 ? -19.960 -36.317 1.738   1.00 40.74  ? 707  LYS   B CB   1 
ATOM   3590 C  CG   . LYS   B 2 202 ? -19.545 -37.096 2.974   1.00 39.29  ? 707  LYS   B CG   1 
ATOM   3591 C  CD   . LYS   B 2 202 ? -19.450 -38.594 2.674   1.00 40.10  ? 707  LYS   B CD   1 
ATOM   3592 C  CE   . LYS   B 2 202 ? -18.334 -39.244 3.503   1.00 45.06  ? 707  LYS   B CE   1 
ATOM   3593 N  NZ   . LYS   B 2 202 ? -16.963 -38.795 3.123   1.00 41.46  ? 707  LYS   B NZ   1 
ATOM   3594 N  N    . PHE   B 2 203 ? -21.167 -34.121 4.076   1.00 31.31  ? 708  PHE   B N    1 
ATOM   3595 C  CA   . PHE   B 2 203 ? -22.302 -33.779 4.925   1.00 31.51  ? 708  PHE   B CA   1 
ATOM   3596 C  C    . PHE   B 2 203 ? -22.486 -32.270 5.073   1.00 33.18  ? 708  PHE   B C    1 
ATOM   3597 O  O    . PHE   B 2 203 ? -23.208 -31.828 5.978   1.00 34.99  ? 708  PHE   B O    1 
ATOM   3598 C  CB   . PHE   B 2 203 ? -22.168 -34.446 6.304   1.00 33.15  ? 708  PHE   B CB   1 
ATOM   3599 C  CG   . PHE   B 2 203 ? -22.117 -35.959 6.238   1.00 37.09  ? 708  PHE   B CG   1 
ATOM   3600 C  CD1  . PHE   B 2 203 ? -23.258 -36.700 5.930   1.00 38.54  ? 708  PHE   B CD1  1 
ATOM   3601 C  CD2  . PHE   B 2 203 ? -20.929 -36.641 6.489   1.00 36.57  ? 708  PHE   B CD2  1 
ATOM   3602 C  CE1  . PHE   B 2 203 ? -23.203 -38.107 5.846   1.00 38.39  ? 708  PHE   B CE1  1 
ATOM   3603 C  CE2  . PHE   B 2 203 ? -20.864 -38.018 6.425   1.00 39.39  ? 708  PHE   B CE2  1 
ATOM   3604 C  CZ   . PHE   B 2 203 ? -21.999 -38.760 6.107   1.00 41.53  ? 708  PHE   B CZ   1 
ATOM   3605 N  N    . ASN   B 2 204 ? -21.863 -31.472 4.198   1.00 32.54  ? 709  ASN   B N    1 
ATOM   3606 C  CA   . ASN   B 2 204 ? -22.061 -30.025 4.222   1.00 32.59  ? 709  ASN   B CA   1 
ATOM   3607 C  C    . ASN   B 2 204 ? -23.550 -29.696 4.216   1.00 34.75  ? 709  ASN   B C    1 
ATOM   3608 O  O    . ASN   B 2 204 ? -24.323 -30.274 3.455   1.00 32.61  ? 709  ASN   B O    1 
ATOM   3609 C  CB   . ASN   B 2 204 ? -21.391 -29.353 3.017   1.00 32.41  ? 709  ASN   B CB   1 
ATOM   3610 C  CG   . ASN   B 2 204 ? -19.923 -29.057 3.248   1.00 36.33  ? 709  ASN   B CG   1 
ATOM   3611 O  OD1  . ASN   B 2 204 ? -19.438 -29.097 4.383   1.00 35.19  ? 709  ASN   B OD1  1 
ATOM   3612 N  ND2  . ASN   B 2 204 ? -19.207 -28.719 2.169   1.00 34.05  ? 709  ASN   B ND2  1 
ATOM   3613 N  N    . GLN   B 2 205 ? -23.944 -28.763 5.079   1.00 30.29  ? 710  GLN   B N    1 
ATOM   3614 C  CA   . GLN   B 2 205 ? -25.323 -28.308 5.217   1.00 34.21  ? 710  GLN   B CA   1 
ATOM   3615 C  C    . GLN   B 2 205 ? -25.450 -26.891 4.676   1.00 34.97  ? 710  GLN   B C    1 
ATOM   3616 O  O    . GLN   B 2 205 ? -24.612 -26.029 4.964   1.00 31.69  ? 710  GLN   B O    1 
ATOM   3617 C  CB   . GLN   B 2 205 ? -25.763 -28.345 6.684   1.00 33.30  ? 710  GLN   B CB   1 
ATOM   3618 C  CG   . GLN   B 2 205 ? -25.620 -29.717 7.340   1.00 34.39  ? 710  GLN   B CG   1 
ATOM   3619 C  CD   . GLN   B 2 205 ? -26.607 -30.726 6.803   1.00 35.74  ? 710  GLN   B CD   1 
ATOM   3620 O  OE1  . GLN   B 2 205 ? -27.813 -30.471 6.762   1.00 42.87  ? 710  GLN   B OE1  1 
ATOM   3621 N  NE2  . GLN   B 2 205 ? -26.108 -31.869 6.372   1.00 37.25  ? 710  GLN   B NE2  1 
ATOM   3622 N  N    . LYS   B 2 206 ? -26.502 -26.650 3.895   1.00 35.42  ? 711  LYS   B N    1 
ATOM   3623 C  CA   . LYS   B 2 206 ? -26.657 -25.337 3.270   1.00 34.56  ? 711  LYS   B CA   1 
ATOM   3624 C  C    . LYS   B 2 206 ? -26.911 -24.242 4.288   1.00 34.11  ? 711  LYS   B C    1 
ATOM   3625 O  O    . LYS   B 2 206 ? -26.554 -23.084 4.055   1.00 33.34  ? 711  LYS   B O    1 
ATOM   3626 C  CB   . LYS   B 2 206 ? -27.780 -25.365 2.236   1.00 38.93  ? 711  LYS   B CB   1 
ATOM   3627 C  CG   . LYS   B 2 206 ? -27.374 -24.664 0.949   1.00 52.46  ? 711  LYS   B CG   1 
ATOM   3628 C  CD   . LYS   B 2 206 ? -28.553 -24.479 0.025   1.00 54.89  ? 711  LYS   B CD   1 
ATOM   3629 C  CE   . LYS   B 2 206 ? -29.095 -25.842 -0.358  1.00 58.97  ? 711  LYS   B CE   1 
ATOM   3630 N  NZ   . LYS   B 2 206 ? -28.242 -26.506 -1.386  1.00 68.78  ? 711  LYS   B NZ   1 
ATOM   3631 N  N    . GLY   B 2 207 ? -27.514 -24.575 5.414   1.00 30.14  ? 712  GLY   B N    1 
ATOM   3632 C  CA   . GLY   B 2 207 ? -27.695 -23.577 6.450   1.00 29.62  ? 712  GLY   B CA   1 
ATOM   3633 C  C    . GLY   B 2 207 ? -28.121 -24.252 7.733   1.00 34.38  ? 712  GLY   B C    1 
ATOM   3634 O  O    . GLY   B 2 207 ? -28.323 -25.471 7.786   1.00 31.90  ? 712  GLY   B O    1 
ATOM   3635 N  N    . VAL   B 2 208 ? -28.267 -23.436 8.776   1.00 31.73  ? 713  VAL   B N    1 
ATOM   3636 C  CA   . VAL   B 2 208 ? -28.563 -23.988 10.092  1.00 33.70  ? 713  VAL   B CA   1 
ATOM   3637 C  C    . VAL   B 2 208 ? -29.910 -24.702 10.085  1.00 37.32  ? 713  VAL   B C    1 
ATOM   3638 O  O    . VAL   B 2 208 ? -30.060 -25.776 10.681  1.00 35.59  ? 713  VAL   B O    1 
ATOM   3639 C  CB   . VAL   B 2 208 ? -28.502 -22.889 11.171  1.00 34.90  ? 713  VAL   B CB   1 
ATOM   3640 C  CG1  . VAL   B 2 208 ? -29.109 -23.375 12.444  1.00 32.19  ? 713  VAL   B CG1  1 
ATOM   3641 C  CG2  . VAL   B 2 208 ? -27.060 -22.493 11.436  1.00 32.95  ? 713  VAL   B CG2  1 
ATOM   3642 N  N    . GLU   B 2 209 ? -30.908 -24.130 9.408   1.00 36.83  ? 714  GLU   B N    1 
ATOM   3643 C  CA   . GLU   B 2 209 ? -32.236 -24.743 9.471   1.00 38.22  ? 714  GLU   B CA   1 
ATOM   3644 C  C    . GLU   B 2 209 ? -32.249 -26.123 8.820   1.00 34.55  ? 714  GLU   B C    1 
ATOM   3645 O  O    . GLU   B 2 209 ? -32.839 -27.063 9.369   1.00 37.58  ? 714  GLU   B O    1 
ATOM   3646 C  CB   . GLU   B 2 209 ? -33.285 -23.838 8.835   1.00 39.68  ? 714  GLU   B CB   1 
ATOM   3647 C  CG   . GLU   B 2 209 ? -33.579 -22.630 9.673   1.00 44.04  ? 714  GLU   B CG   1 
ATOM   3648 C  CD   . GLU   B 2 209 ? -33.997 -23.023 11.084  1.00 52.51  ? 714  GLU   B CD   1 
ATOM   3649 O  OE1  . GLU   B 2 209 ? -34.880 -23.903 11.244  1.00 57.09  ? 714  GLU   B OE1  1 
ATOM   3650 O  OE2  . GLU   B 2 209 ? -33.425 -22.443 12.036  1.00 59.01  ? 714  GLU   B OE2  1 
ATOM   3651 N  N    . ASP   B 2 210 ? -31.604 -26.268 7.656   1.00 35.11  ? 715  ASP   B N    1 
ATOM   3652 C  CA   . ASP   B 2 210 ? -31.461 -27.589 7.052   1.00 37.60  ? 715  ASP   B CA   1 
ATOM   3653 C  C    . ASP   B 2 210 ? -30.794 -28.562 8.011   1.00 34.37  ? 715  ASP   B C    1 
ATOM   3654 O  O    . ASP   B 2 210 ? -31.218 -29.715 8.119   1.00 35.19  ? 715  ASP   B O    1 
ATOM   3655 C  CB   . ASP   B 2 210 ? -30.649 -27.523 5.759   1.00 33.81  ? 715  ASP   B CB   1 
ATOM   3656 C  CG   . ASP   B 2 210 ? -31.381 -26.814 4.625   1.00 39.51  ? 715  ASP   B CG   1 
ATOM   3657 O  OD1  . ASP   B 2 210 ? -32.428 -26.180 4.878   1.00 36.50  ? 715  ASP   B OD1  1 
ATOM   3658 O  OD2  . ASP   B 2 210 ? -30.871 -26.881 3.486   1.00 40.31  ? 715  ASP   B OD2  1 
ATOM   3659 N  N    . ALA   B 2 211 ? -29.727 -28.122 8.694   1.00 33.02  ? 716  ALA   B N    1 
ATOM   3660 C  CA   . ALA   B 2 211 ? -28.977 -29.033 9.562   1.00 36.46  ? 716  ALA   B CA   1 
ATOM   3661 C  C    . ALA   B 2 211 ? -29.827 -29.513 10.733  1.00 34.84  ? 716  ALA   B C    1 
ATOM   3662 O  O    . ALA   B 2 211 ? -29.796 -30.696 11.087  1.00 40.77  ? 716  ALA   B O    1 
ATOM   3663 C  CB   . ALA   B 2 211 ? -27.707 -28.353 10.076  1.00 33.92  ? 716  ALA   B CB   1 
ATOM   3664 N  N    . LEU   B 2 212 ? -30.566 -28.605 11.367  1.00 35.89  ? 717  LEU   B N    1 
ATOM   3665 C  CA   . LEU   B 2 212 ? -31.481 -29.013 12.429  1.00 36.75  ? 717  LEU   B CA   1 
ATOM   3666 C  C    . LEU   B 2 212 ? -32.494 -30.026 11.915  1.00 37.93  ? 717  LEU   B C    1 
ATOM   3667 O  O    . LEU   B 2 212 ? -32.796 -31.008 12.598  1.00 38.44  ? 717  LEU   B O    1 
ATOM   3668 C  CB   . LEU   B 2 212 ? -32.200 -27.793 12.995  1.00 38.46  ? 717  LEU   B CB   1 
ATOM   3669 C  CG   . LEU   B 2 212 ? -31.293 -26.769 13.674  1.00 42.91  ? 717  LEU   B CG   1 
ATOM   3670 C  CD1  . LEU   B 2 212 ? -32.111 -25.603 14.196  1.00 46.45  ? 717  LEU   B CD1  1 
ATOM   3671 C  CD2  . LEU   B 2 212 ? -30.540 -27.429 14.806  1.00 45.38  ? 717  LEU   B CD2  1 
ATOM   3672 N  N    . VAL   B 2 213 ? -33.019 -29.819 10.703  1.00 36.57  ? 718  VAL   B N    1 
ATOM   3673 C  CA   . VAL   B 2 213 ? -33.961 -30.797 10.157  1.00 38.61  ? 718  VAL   B CA   1 
ATOM   3674 C  C    . VAL   B 2 213 ? -33.274 -32.149 9.956   1.00 40.59  ? 718  VAL   B C    1 
ATOM   3675 O  O    . VAL   B 2 213 ? -33.848 -33.203 10.279  1.00 41.14  ? 718  VAL   B O    1 
ATOM   3676 C  CB   . VAL   B 2 213 ? -34.601 -30.279 8.851   1.00 40.28  ? 718  VAL   B CB   1 
ATOM   3677 C  CG1  . VAL   B 2 213 ? -35.309 -31.419 8.099   1.00 42.32  ? 718  VAL   B CG1  1 
ATOM   3678 C  CG2  . VAL   B 2 213 ? -35.582 -29.155 9.145   1.00 31.70  ? 718  VAL   B CG2  1 
ATOM   3679 N  N    . SER   B 2 214 ? -32.045 -32.144 9.419   1.00 36.41  ? 719  SER   B N    1 
ATOM   3680 C  CA   . SER   B 2 214 ? -31.309 -33.395 9.246   1.00 39.87  ? 719  SER   B CA   1 
ATOM   3681 C  C    . SER   B 2 214 ? -31.115 -34.107 10.575  1.00 40.58  ? 719  SER   B C    1 
ATOM   3682 O  O    . SER   B 2 214 ? -31.270 -35.329 10.659  1.00 42.68  ? 719  SER   B O    1 
ATOM   3683 C  CB   . SER   B 2 214 ? -29.943 -33.145 8.606   1.00 40.78  ? 719  SER   B CB   1 
ATOM   3684 O  OG   . SER   B 2 214 ? -30.034 -32.591 7.319   1.00 45.29  ? 719  SER   B OG   1 
ATOM   3685 N  N    . LEU   B 2 215 ? -30.738 -33.362 11.616  1.00 39.55  ? 720  LEU   B N    1 
ATOM   3686 C  CA   . LEU   B 2 215 ? -30.587 -33.955 12.943  1.00 40.71  ? 720  LEU   B CA   1 
ATOM   3687 C  C    . LEU   B 2 215 ? -31.890 -34.588 13.406  1.00 42.11  ? 720  LEU   B C    1 
ATOM   3688 O  O    . LEU   B 2 215 ? -31.920 -35.752 13.821  1.00 47.08  ? 720  LEU   B O    1 
ATOM   3689 C  CB   . LEU   B 2 215 ? -30.150 -32.894 13.953  1.00 36.78  ? 720  LEU   B CB   1 
ATOM   3690 C  CG   . LEU   B 2 215 ? -28.712 -32.409 14.042  1.00 39.68  ? 720  LEU   B CG   1 
ATOM   3691 C  CD1  . LEU   B 2 215 ? -28.634 -31.328 15.114  1.00 35.76  ? 720  LEU   B CD1  1 
ATOM   3692 C  CD2  . LEU   B 2 215 ? -27.721 -33.530 14.334  1.00 39.53  ? 720  LEU   B CD2  1 
ATOM   3693 N  N    . LYS   B 2 216 ? -32.984 -33.830 13.351  1.00 43.75  ? 721  LYS   B N    1 
ATOM   3694 C  CA   . LYS   B 2 216 ? -34.228 -34.324 13.937  1.00 44.72  ? 721  LYS   B CA   1 
ATOM   3695 C  C    . LYS   B 2 216 ? -34.775 -35.530 13.186  1.00 47.83  ? 721  LYS   B C    1 
ATOM   3696 O  O    . LYS   B 2 216 ? -35.425 -36.388 13.795  1.00 52.11  ? 721  LYS   B O    1 
ATOM   3697 C  CB   . LYS   B 2 216 ? -35.274 -33.213 13.990  1.00 45.19  ? 721  LYS   B CB   1 
ATOM   3698 C  CG   . LYS   B 2 216 ? -35.182 -32.342 15.228  1.00 47.69  ? 721  LYS   B CG   1 
ATOM   3699 C  CD   . LYS   B 2 216 ? -35.863 -30.998 14.993  1.00 55.30  ? 721  LYS   B CD   1 
ATOM   3700 C  CE   . LYS   B 2 216 ? -36.543 -30.498 16.270  1.00 63.62  ? 721  LYS   B CE   1 
ATOM   3701 N  NZ   . LYS   B 2 216 ? -37.990 -30.155 16.050  1.00 70.36  ? 721  LYS   B NZ   1 
ATOM   3702 N  N    . THR   B 2 217 ? -34.529 -35.623 11.882  1.00 43.57  ? 722  THR   B N    1 
ATOM   3703 C  CA   . THR   B 2 217 ? -35.043 -36.746 11.115  1.00 47.22  ? 722  THR   B CA   1 
ATOM   3704 C  C    . THR   B 2 217 ? -34.040 -37.885 10.996  1.00 49.47  ? 722  THR   B C    1 
ATOM   3705 O  O    . THR   B 2 217 ? -34.301 -38.847 10.268  1.00 50.94  ? 722  THR   B O    1 
ATOM   3706 C  CB   . THR   B 2 217 ? -35.460 -36.295 9.716   1.00 48.81  ? 722  THR   B CB   1 
ATOM   3707 O  OG1  . THR   B 2 217 ? -34.306 -35.847 8.993   1.00 45.03  ? 722  THR   B OG1  1 
ATOM   3708 C  CG2  . THR   B 2 217 ? -36.468 -35.150 9.821   1.00 45.04  ? 722  THR   B CG2  1 
ATOM   3709 N  N    . GLY   B 2 218 ? -32.895 -37.795 11.667  1.00 46.39  ? 723  GLY   B N    1 
ATOM   3710 C  CA   . GLY   B 2 218 ? -31.985 -38.921 11.695  1.00 47.50  ? 723  GLY   B CA   1 
ATOM   3711 C  C    . GLY   B 2 218 ? -31.122 -39.071 10.471  1.00 46.51  ? 723  GLY   B C    1 
ATOM   3712 O  O    . GLY   B 2 218 ? -30.564 -40.150 10.249  1.00 44.96  ? 723  GLY   B O    1 
ATOM   3713 N  N    . LYS   B 2 219 ? -30.997 -38.026 9.659   1.00 43.43  ? 724  LYS   B N    1 
ATOM   3714 C  CA   . LYS   B 2 219 ? -30.107 -38.063 8.514   1.00 44.72  ? 724  LYS   B CA   1 
ATOM   3715 C  C    . LYS   B 2 219 ? -28.714 -37.560 8.858   1.00 45.29  ? 724  LYS   B C    1 
ATOM   3716 O  O    . LYS   B 2 219 ? -27.789 -37.723 8.056   1.00 42.79  ? 724  LYS   B O    1 
ATOM   3717 C  CB   . LYS   B 2 219 ? -30.699 -37.234 7.365   1.00 50.83  ? 724  LYS   B CB   1 
ATOM   3718 C  CG   . LYS   B 2 219 ? -30.065 -37.530 6.015   1.00 63.31  ? 724  LYS   B CG   1 
ATOM   3719 C  CD   . LYS   B 2 219 ? -31.097 -37.558 4.905   1.00 62.26  ? 724  LYS   B CD   1 
ATOM   3720 C  CE   . LYS   B 2 219 ? -31.739 -36.188 4.730   1.00 70.92  ? 724  LYS   B CE   1 
ATOM   3721 N  NZ   . LYS   B 2 219 ? -30.748 -35.120 4.358   1.00 67.70  ? 724  LYS   B NZ   1 
ATOM   3722 N  N    . LEU   B 2 220 ? -28.553 -36.953 10.028  1.00 39.88  ? 725  LEU   B N    1 
ATOM   3723 C  CA   . LEU   B 2 220 ? -27.270 -36.486 10.521  1.00 38.10  ? 725  LEU   B CA   1 
ATOM   3724 C  C    . LEU   B 2 220 ? -27.171 -36.897 11.981  1.00 40.12  ? 725  LEU   B C    1 
ATOM   3725 O  O    . LEU   B 2 220 ? -28.171 -36.860 12.701  1.00 40.38  ? 725  LEU   B O    1 
ATOM   3726 C  CB   . LEU   B 2 220 ? -27.166 -34.957 10.386  1.00 39.45  ? 725  LEU   B CB   1 
ATOM   3727 C  CG   . LEU   B 2 220 ? -25.814 -34.277 10.280  1.00 42.80  ? 725  LEU   B CG   1 
ATOM   3728 C  CD1  . LEU   B 2 220 ? -25.087 -34.804 9.049   1.00 38.87  ? 725  LEU   B CD1  1 
ATOM   3729 C  CD2  . LEU   B 2 220 ? -26.032 -32.777 10.204  1.00 38.45  ? 725  LEU   B CD2  1 
ATOM   3730 N  N    . ASP   B 2 221 ? -25.980 -37.316 12.408  1.00 38.53  ? 726  ASP   B N    1 
ATOM   3731 C  CA   . ASP   B 2 221 ? -25.721 -37.658 13.803  1.00 39.19  ? 726  ASP   B CA   1 
ATOM   3732 C  C    . ASP   B 2 221 ? -25.246 -36.473 14.637  1.00 37.34  ? 726  ASP   B C    1 
ATOM   3733 O  O    . ASP   B 2 221 ? -25.594 -36.378 15.820  1.00 40.33  ? 726  ASP   B O    1 
ATOM   3734 C  CB   . ASP   B 2 221 ? -24.688 -38.780 13.870  1.00 38.12  ? 726  ASP   B CB   1 
ATOM   3735 C  CG   . ASP   B 2 221 ? -25.170 -40.040 13.198  1.00 41.26  ? 726  ASP   B CG   1 
ATOM   3736 O  OD1  . ASP   B 2 221 ? -26.324 -40.442 13.470  1.00 45.78  ? 726  ASP   B OD1  1 
ATOM   3737 O  OD2  . ASP   B 2 221 ? -24.426 -40.615 12.377  1.00 42.32  ? 726  ASP   B OD2  1 
ATOM   3738 N  N    . ALA   B 2 222 ? -24.444 -35.577 14.059  1.00 33.86  ? 727  ALA   B N    1 
ATOM   3739 C  CA   . ALA   B 2 222 ? -23.927 -34.413 14.772  1.00 32.42  ? 727  ALA   B CA   1 
ATOM   3740 C  C    . ALA   B 2 222 ? -23.836 -33.223 13.830  1.00 33.95  ? 727  ALA   B C    1 
ATOM   3741 O  O    . ALA   B 2 222 ? -23.601 -33.381 12.631  1.00 35.06  ? 727  ALA   B O    1 
ATOM   3742 C  CB   . ALA   B 2 222 ? -22.533 -34.669 15.391  1.00 31.83  ? 727  ALA   B CB   1 
ATOM   3743 N  N    . PHE   B 2 223 ? -24.010 -32.025 14.391  1.00 31.61  ? 728  PHE   B N    1 
ATOM   3744 C  CA   . PHE   B 2 223 ? -23.909 -30.769 13.648  1.00 31.11  ? 728  PHE   B CA   1 
ATOM   3745 C  C    . PHE   B 2 223 ? -22.890 -29.911 14.371  1.00 31.38  ? 728  PHE   B C    1 
ATOM   3746 O  O    . PHE   B 2 223 ? -23.109 -29.547 15.533  1.00 32.71  ? 728  PHE   B O    1 
ATOM   3747 C  CB   . PHE   B 2 223 ? -25.261 -30.069 13.564  1.00 32.00  ? 728  PHE   B CB   1 
ATOM   3748 C  CG   . PHE   B 2 223 ? -25.224 -28.708 12.913  1.00 30.65  ? 728  PHE   B CG   1 
ATOM   3749 C  CD1  . PHE   B 2 223 ? -24.533 -28.498 11.740  1.00 31.18  ? 728  PHE   B CD1  1 
ATOM   3750 C  CD2  . PHE   B 2 223 ? -25.911 -27.645 13.476  1.00 33.33  ? 728  PHE   B CD2  1 
ATOM   3751 C  CE1  . PHE   B 2 223 ? -24.524 -27.249 11.131  1.00 31.80  ? 728  PHE   B CE1  1 
ATOM   3752 C  CE2  . PHE   B 2 223 ? -25.903 -26.386 12.873  1.00 31.02  ? 728  PHE   B CE2  1 
ATOM   3753 C  CZ   . PHE   B 2 223 ? -25.199 -26.198 11.709  1.00 31.54  ? 728  PHE   B CZ   1 
ATOM   3754 N  N    . ILE   B 2 224 ? -21.760 -29.643 13.709  1.00 29.04  ? 729  ILE   B N    1 
ATOM   3755 C  CA   . ILE   B 2 224 ? -20.652 -28.873 14.279  1.00 27.67  ? 729  ILE   B CA   1 
ATOM   3756 C  C    . ILE   B 2 224 ? -20.759 -27.436 13.776  1.00 28.09  ? 729  ILE   B C    1 
ATOM   3757 O  O    . ILE   B 2 224 ? -20.798 -27.204 12.564  1.00 30.11  ? 729  ILE   B O    1 
ATOM   3758 C  CB   . ILE   B 2 224 ? -19.299 -29.487 13.897  1.00 29.21  ? 729  ILE   B CB   1 
ATOM   3759 C  CG1  . ILE   B 2 224 ? -19.277 -30.975 14.292  1.00 27.03  ? 729  ILE   B CG1  1 
ATOM   3760 C  CG2  . ILE   B 2 224 ? -18.160 -28.701 14.570  1.00 30.93  ? 729  ILE   B CG2  1 
ATOM   3761 C  CD1  . ILE   B 2 224 ? -18.072 -31.706 13.801  1.00 35.30  ? 729  ILE   B CD1  1 
ATOM   3762 N  N    . TYR   B 2 225 ? -20.815 -26.466 14.685  1.00 28.39  ? 730  TYR   B N    1 
ATOM   3763 C  CA   . TYR   B 2 225 ? -21.151 -25.107 14.264  1.00 30.94  ? 730  TYR   B CA   1 
ATOM   3764 C  C    . TYR   B 2 225 ? -20.850 -24.118 15.383  1.00 30.39  ? 730  TYR   B C    1 
ATOM   3765 O  O    . TYR   B 2 225 ? -20.558 -24.498 16.520  1.00 32.93  ? 730  TYR   B O    1 
ATOM   3766 C  CB   . TYR   B 2 225 ? -22.631 -25.001 13.854  1.00 27.69  ? 730  TYR   B CB   1 
ATOM   3767 C  CG   . TYR   B 2 225 ? -22.996 -23.743 13.085  1.00 29.26  ? 730  TYR   B CG   1 
ATOM   3768 C  CD1  . TYR   B 2 225 ? -22.505 -23.510 11.807  1.00 32.84  ? 730  TYR   B CD1  1 
ATOM   3769 C  CD2  . TYR   B 2 225 ? -23.856 -22.802 13.634  1.00 28.22  ? 730  TYR   B CD2  1 
ATOM   3770 C  CE1  . TYR   B 2 225 ? -22.858 -22.366 11.102  1.00 33.44  ? 730  TYR   B CE1  1 
ATOM   3771 C  CE2  . TYR   B 2 225 ? -24.201 -21.654 12.945  1.00 29.24  ? 730  TYR   B CE2  1 
ATOM   3772 C  CZ   . TYR   B 2 225 ? -23.708 -21.449 11.669  1.00 31.97  ? 730  TYR   B CZ   1 
ATOM   3773 O  OH   . TYR   B 2 225 ? -24.042 -20.307 10.972  1.00 31.32  ? 730  TYR   B OH   1 
ATOM   3774 N  N    . ASP   B 2 226 ? -20.973 -22.835 15.029  1.00 29.15  ? 731  ASP   B N    1 
ATOM   3775 C  CA   . ASP   B 2 226 ? -20.781 -21.695 15.923  1.00 31.37  ? 731  ASP   B CA   1 
ATOM   3776 C  C    . ASP   B 2 226 ? -21.495 -21.900 17.250  1.00 30.39  ? 731  ASP   B C    1 
ATOM   3777 O  O    . ASP   B 2 226 ? -22.700 -22.166 17.286  1.00 29.67  ? 731  ASP   B O    1 
ATOM   3778 C  CB   . ASP   B 2 226 ? -21.320 -20.428 15.240  1.00 30.52  ? 731  ASP   B CB   1 
ATOM   3779 C  CG   . ASP   B 2 226 ? -21.307 -19.226 16.142  1.00 28.42  ? 731  ASP   B CG   1 
ATOM   3780 O  OD1  . ASP   B 2 226 ? -20.227 -18.621 16.287  1.00 32.82  ? 731  ASP   B OD1  1 
ATOM   3781 O  OD2  . ASP   B 2 226 ? -22.365 -18.886 16.725  1.00 33.65  ? 731  ASP   B OD2  1 
ATOM   3782 N  N    . ALA   B 2 227 ? -20.749 -21.742 18.344  1.00 31.22  ? 732  ALA   B N    1 
ATOM   3783 C  CA   . ALA   B 2 227 ? -21.265 -22.121 19.654  1.00 29.96  ? 732  ALA   B CA   1 
ATOM   3784 C  C    . ALA   B 2 227 ? -22.455 -21.268 20.065  1.00 30.54  ? 732  ALA   B C    1 
ATOM   3785 O  O    . ALA   B 2 227 ? -23.402 -21.775 20.675  1.00 32.49  ? 732  ALA   B O    1 
ATOM   3786 C  CB   . ALA   B 2 227 ? -20.157 -22.018 20.703  1.00 31.94  ? 732  ALA   B CB   1 
ATOM   3787 N  N    . ALA   B 2 228 ? -22.417 -19.959 19.791  1.00 28.23  ? 733  ALA   B N    1 
ATOM   3788 C  CA   . ALA   B 2 228 ? -23.505 -19.117 20.280  1.00 31.08  ? 733  ALA   B CA   1 
ATOM   3789 C  C    . ALA   B 2 228 ? -24.820 -19.432 19.567  1.00 29.59  ? 733  ALA   B C    1 
ATOM   3790 O  O    . ALA   B 2 228 ? -25.881 -19.414 20.186  1.00 30.47  ? 733  ALA   B O    1 
ATOM   3791 C  CB   . ALA   B 2 228 ? -23.150 -17.644 20.118  1.00 27.73  ? 733  ALA   B CB   1 
ATOM   3792 N  N    . VAL   B 2 229 ? -24.776 -19.683 18.258  1.00 31.57  ? 734  VAL   B N    1 
ATOM   3793 C  CA   . VAL   B 2 229 ? -26.000 -20.046 17.541  1.00 26.28  ? 734  VAL   B CA   1 
ATOM   3794 C  C    . VAL   B 2 229 ? -26.528 -21.398 18.025  1.00 33.11  ? 734  VAL   B C    1 
ATOM   3795 O  O    . VAL   B 2 229 ? -27.735 -21.559 18.269  1.00 32.87  ? 734  VAL   B O    1 
ATOM   3796 C  CB   . VAL   B 2 229 ? -25.743 -20.015 16.023  1.00 28.01  ? 734  VAL   B CB   1 
ATOM   3797 C  CG1  . VAL   B 2 229 ? -26.833 -20.714 15.279  1.00 27.66  ? 734  VAL   B CG1  1 
ATOM   3798 C  CG2  . VAL   B 2 229 ? -25.662 -18.541 15.548  1.00 30.70  ? 734  VAL   B CG2  1 
ATOM   3799 N  N    . LEU   B 2 230 ? -25.646 -22.389 18.197  1.00 29.29  ? 735  LEU   B N    1 
ATOM   3800 C  CA   . LEU   B 2 230 ? -26.120 -23.681 18.697  1.00 33.38  ? 735  LEU   B CA   1 
ATOM   3801 C  C    . LEU   B 2 230 ? -26.721 -23.539 20.087  1.00 33.77  ? 735  LEU   B C    1 
ATOM   3802 O  O    . LEU   B 2 230 ? -27.744 -24.155 20.391  1.00 33.23  ? 735  LEU   B O    1 
ATOM   3803 C  CB   . LEU   B 2 230 ? -24.985 -24.702 18.721  1.00 31.80  ? 735  LEU   B CB   1 
ATOM   3804 C  CG   . LEU   B 2 230 ? -24.512 -25.174 17.346  1.00 30.05  ? 735  LEU   B CG   1 
ATOM   3805 C  CD1  . LEU   B 2 230 ? -23.591 -26.385 17.497  1.00 28.28  ? 735  LEU   B CD1  1 
ATOM   3806 C  CD2  . LEU   B 2 230 ? -25.647 -25.472 16.382  1.00 29.54  ? 735  LEU   B CD2  1 
ATOM   3807 N  N    . ASN   B 2 231 ? -26.103 -22.717 20.941  1.00 32.95  ? 736  ASN   B N    1 
ATOM   3808 C  CA   . ASN   B 2 231 ? -26.663 -22.488 22.271  1.00 37.93  ? 736  ASN   B CA   1 
ATOM   3809 C  C    . ASN   B 2 231 ? -28.056 -21.896 22.167  1.00 35.62  ? 736  ASN   B C    1 
ATOM   3810 O  O    . ASN   B 2 231 ? -28.961 -22.301 22.900  1.00 36.94  ? 736  ASN   B O    1 
ATOM   3811 C  CB   . ASN   B 2 231 ? -25.727 -21.585 23.083  1.00 39.91  ? 736  ASN   B CB   1 
ATOM   3812 C  CG   . ASN   B 2 231 ? -26.295 -21.205 24.459  1.00 46.89  ? 736  ASN   B CG   1 
ATOM   3813 O  OD1  . ASN   B 2 231 ? -27.366 -20.593 24.570  1.00 50.84  ? 736  ASN   B OD1  1 
ATOM   3814 N  ND2  . ASN   B 2 231 ? -25.586 -21.599 25.515  1.00 57.65  ? 736  ASN   B ND2  1 
ATOM   3815 N  N    . TYR   B 2 232 ? -28.252 -20.948 21.246  1.00 34.36  ? 737  TYR   B N    1 
ATOM   3816 C  CA   . TYR   B 2 232 ? -29.572 -20.357 21.052  1.00 37.78  ? 737  TYR   B CA   1 
ATOM   3817 C  C    . TYR   B 2 232 ? -30.590 -21.396 20.594  1.00 40.70  ? 737  TYR   B C    1 
ATOM   3818 O  O    . TYR   B 2 232 ? -31.707 -21.458 21.115  1.00 39.59  ? 737  TYR   B O    1 
ATOM   3819 C  CB   . TYR   B 2 232 ? -29.494 -19.217 20.038  1.00 37.68  ? 737  TYR   B CB   1 
ATOM   3820 C  CG   . TYR   B 2 232 ? -30.844 -18.608 19.745  1.00 38.47  ? 737  TYR   B CG   1 
ATOM   3821 C  CD1  . TYR   B 2 232 ? -31.473 -18.807 18.521  1.00 42.11  ? 737  TYR   B CD1  1 
ATOM   3822 C  CD2  . TYR   B 2 232 ? -31.507 -17.864 20.709  1.00 43.62  ? 737  TYR   B CD2  1 
ATOM   3823 C  CE1  . TYR   B 2 232 ? -32.724 -18.244 18.256  1.00 45.27  ? 737  TYR   B CE1  1 
ATOM   3824 C  CE2  . TYR   B 2 232 ? -32.739 -17.308 20.456  1.00 48.93  ? 737  TYR   B CE2  1 
ATOM   3825 C  CZ   . TYR   B 2 232 ? -33.344 -17.499 19.230  1.00 47.16  ? 737  TYR   B CZ   1 
ATOM   3826 O  OH   . TYR   B 2 232 ? -34.587 -16.938 19.002  1.00 60.44  ? 737  TYR   B OH   1 
ATOM   3827 N  N    . LYS   B 2 233 ? -30.224 -22.204 19.596  1.00 38.92  ? 738  LYS   B N    1 
ATOM   3828 C  CA   . LYS   B 2 233 ? -31.155 -23.185 19.042  1.00 39.44  ? 738  LYS   B CA   1 
ATOM   3829 C  C    . LYS   B 2 233 ? -31.460 -24.296 20.041  1.00 41.90  ? 738  LYS   B C    1 
ATOM   3830 O  O    . LYS   B 2 233 ? -32.600 -24.773 20.124  1.00 44.36  ? 738  LYS   B O    1 
ATOM   3831 C  CB   . LYS   B 2 233 ? -30.569 -23.764 17.758  1.00 37.08  ? 738  LYS   B CB   1 
ATOM   3832 C  CG   . LYS   B 2 233 ? -30.461 -22.764 16.619  1.00 34.93  ? 738  LYS   B CG   1 
ATOM   3833 C  CD   . LYS   B 2 233 ? -31.833 -22.233 16.204  1.00 42.09  ? 738  LYS   B CD   1 
ATOM   3834 C  CE   . LYS   B 2 233 ? -31.700 -21.403 14.943  1.00 46.48  ? 738  LYS   B CE   1 
ATOM   3835 N  NZ   . LYS   B 2 233 ? -33.013 -21.038 14.335  1.00 51.73  ? 738  LYS   B NZ   1 
ATOM   3836 N  N    . ALA   B 2 234 ? -30.454 -24.737 20.796  1.00 37.93  ? 739  ALA   B N    1 
ATOM   3837 C  CA   . ALA   B 2 234 ? -30.705 -25.717 21.843  1.00 42.52  ? 739  ALA   B CA   1 
ATOM   3838 C  C    . ALA   B 2 234 ? -31.692 -25.175 22.872  1.00 46.70  ? 739  ALA   B C    1 
ATOM   3839 O  O    . ALA   B 2 234 ? -32.574 -25.903 23.345  1.00 48.93  ? 739  ALA   B O    1 
ATOM   3840 C  CB   . ALA   B 2 234 ? -29.387 -26.125 22.509  1.00 41.20  ? 739  ALA   B CB   1 
ATOM   3841 N  N    . GLY   B 2 235 ? -31.572 -23.891 23.216  1.00 44.76  ? 740  GLY   B N    1 
ATOM   3842 C  CA   . GLY   B 2 235 ? -32.458 -23.295 24.201  1.00 49.64  ? 740  GLY   B CA   1 
ATOM   3843 C  C    . GLY   B 2 235 ? -33.902 -23.179 23.752  1.00 51.73  ? 740  GLY   B C    1 
ATOM   3844 O  O    . GLY   B 2 235 ? -34.798 -23.088 24.598  1.00 54.92  ? 740  GLY   B O    1 
ATOM   3845 N  N    . ARG   B 2 236 ? -34.153 -23.181 22.444  1.00 48.69  ? 741  ARG   B N    1 
ATOM   3846 C  CA   . ARG   B 2 236 ? -35.504 -23.040 21.918  1.00 52.59  ? 741  ARG   B CA   1 
ATOM   3847 C  C    . ARG   B 2 236 ? -35.952 -24.269 21.128  1.00 57.11  ? 741  ARG   B C    1 
ATOM   3848 O  O    . ARG   B 2 236 ? -36.887 -24.189 20.328  1.00 62.86  ? 741  ARG   B O    1 
ATOM   3849 C  CB   . ARG   B 2 236 ? -35.622 -21.775 21.064  1.00 57.78  ? 741  ARG   B CB   1 
ATOM   3850 C  CG   . ARG   B 2 236 ? -36.022 -20.533 21.857  1.00 61.50  ? 741  ARG   B CG   1 
ATOM   3851 C  CD   . ARG   B 2 236 ? -34.844 -19.606 22.118  1.00 63.34  ? 741  ARG   B CD   1 
ATOM   3852 N  NE   . ARG   B 2 236 ? -35.222 -18.402 22.856  1.00 77.56  ? 741  ARG   B NE   1 
ATOM   3853 C  CZ   . ARG   B 2 236 ? -35.838 -17.354 22.321  1.00 69.93  ? 741  ARG   B CZ   1 
ATOM   3854 N  NH1  . ARG   B 2 236 ? -36.258 -17.367 21.066  1.00 74.90  ? 741  ARG   B NH1  1 
ATOM   3855 N  NH2  . ARG   B 2 236 ? -36.036 -16.265 23.062  1.00 63.31  ? 741  ARG   B NH2  1 
ATOM   3856 N  N    . ASP   B 2 237 ? -35.313 -25.419 21.344  1.00 49.25  ? 742  ASP   B N    1 
ATOM   3857 C  CA   . ASP   B 2 237 ? -35.688 -26.617 20.599  1.00 55.12  ? 742  ASP   B CA   1 
ATOM   3858 C  C    . ASP   B 2 237 ? -36.940 -27.265 21.182  1.00 54.35  ? 742  ASP   B C    1 
ATOM   3859 O  O    . ASP   B 2 237 ? -37.048 -27.446 22.399  1.00 55.18  ? 742  ASP   B O    1 
ATOM   3860 C  CB   . ASP   B 2 237 ? -34.547 -27.630 20.575  1.00 51.75  ? 742  ASP   B CB   1 
ATOM   3861 C  CG   . ASP   B 2 237 ? -34.877 -28.850 19.720  1.00 52.19  ? 742  ASP   B CG   1 
ATOM   3862 O  OD1  . ASP   B 2 237 ? -35.158 -28.664 18.521  1.00 50.39  ? 742  ASP   B OD1  1 
ATOM   3863 O  OD2  . ASP   B 2 237 ? -34.846 -29.985 20.251  1.00 48.53  ? 742  ASP   B OD2  1 
ATOM   3864 N  N    . GLU   B 2 238 ? -37.867 -27.642 20.301  1.00 50.78  ? 743  GLU   B N    1 
ATOM   3865 C  CA   . GLU   B 2 238 ? -39.135 -28.224 20.738  1.00 55.83  ? 743  GLU   B CA   1 
ATOM   3866 C  C    . GLU   B 2 238 ? -38.893 -29.559 21.422  1.00 57.22  ? 743  GLU   B C    1 
ATOM   3867 O  O    . GLU   B 2 238 ? -38.311 -30.473 20.831  1.00 59.81  ? 743  GLU   B O    1 
ATOM   3868 C  CB   . GLU   B 2 238 ? -40.077 -28.403 19.550  1.00 53.74  ? 743  GLU   B CB   1 
ATOM   3869 N  N    . GLY   B 2 239 ? -39.348 -29.667 22.667  1.00 59.69  ? 744  GLY   B N    1 
ATOM   3870 C  CA   . GLY   B 2 239 ? -39.113 -30.839 23.476  1.00 58.57  ? 744  GLY   B CA   1 
ATOM   3871 C  C    . GLY   B 2 239 ? -37.712 -30.942 24.022  1.00 58.87  ? 744  GLY   B C    1 
ATOM   3872 O  O    . GLY   B 2 239 ? -37.407 -31.920 24.710  1.00 57.75  ? 744  GLY   B O    1 
ATOM   3873 N  N    . CYS   B 2 240 ? -36.851 -29.966 23.725  1.00 55.49  ? 745  CYS   B N    1 
ATOM   3874 C  CA   . CYS   B 2 240 ? -35.460 -29.957 24.165  1.00 55.83  ? 745  CYS   B CA   1 
ATOM   3875 C  C    . CYS   B 2 240 ? -34.774 -31.285 23.836  1.00 52.23  ? 745  CYS   B C    1 
ATOM   3876 O  O    . CYS   B 2 240 ? -34.075 -31.879 24.658  1.00 49.58  ? 745  CYS   B O    1 
ATOM   3877 C  CB   . CYS   B 2 240 ? -35.365 -29.629 25.654  1.00 54.99  ? 745  CYS   B CB   1 
ATOM   3878 S  SG   . CYS   B 2 240 ? -36.290 -28.145 26.157  1.00 65.93  ? 745  CYS   B SG   1 
ATOM   3879 N  N    . LYS   B 2 241 ? -34.987 -31.754 22.606  1.00 49.56  ? 746  LYS   B N    1 
ATOM   3880 C  CA   . LYS   B 2 241 ? -34.360 -32.997 22.171  1.00 49.00  ? 746  LYS   B CA   1 
ATOM   3881 C  C    . LYS   B 2 241 ? -32.924 -32.785 21.698  1.00 50.69  ? 746  LYS   B C    1 
ATOM   3882 O  O    . LYS   B 2 241 ? -32.088 -33.680 21.862  1.00 46.92  ? 746  LYS   B O    1 
ATOM   3883 C  CB   . LYS   B 2 241 ? -35.185 -33.642 21.053  1.00 49.35  ? 746  LYS   B CB   1 
ATOM   3884 N  N    . LEU   B 2 242 ? -32.611 -31.622 21.134  1.00 47.18  ? 747  LEU   B N    1 
ATOM   3885 C  CA   . LEU   B 2 242 ? -31.296 -31.361 20.561  1.00 43.49  ? 747  LEU   B CA   1 
ATOM   3886 C  C    . LEU   B 2 242 ? -30.477 -30.544 21.551  1.00 42.40  ? 747  LEU   B C    1 
ATOM   3887 O  O    . LEU   B 2 242 ? -30.944 -29.519 22.056  1.00 43.71  ? 747  LEU   B O    1 
ATOM   3888 C  CB   . LEU   B 2 242 ? -31.420 -30.624 19.226  1.00 42.14  ? 747  LEU   B CB   1 
ATOM   3889 C  CG   . LEU   B 2 242 ? -32.222 -31.271 18.091  1.00 46.60  ? 747  LEU   B CG   1 
ATOM   3890 C  CD1  . LEU   B 2 242 ? -32.334 -30.292 16.928  1.00 46.85  ? 747  LEU   B CD1  1 
ATOM   3891 C  CD2  . LEU   B 2 242 ? -31.620 -32.588 17.625  1.00 41.59  ? 747  LEU   B CD2  1 
ATOM   3892 N  N    . VAL   B 2 243 ? -29.260 -31.003 21.829  1.00 38.54  ? 748  VAL   B N    1 
ATOM   3893 C  CA   . VAL   B 2 243 ? -28.422 -30.425 22.868  1.00 39.86  ? 748  VAL   B CA   1 
ATOM   3894 C  C    . VAL   B 2 243 ? -27.009 -30.241 22.333  1.00 40.21  ? 748  VAL   B C    1 
ATOM   3895 O  O    . VAL   B 2 243 ? -26.593 -30.885 21.365  1.00 40.28  ? 748  VAL   B O    1 
ATOM   3896 C  CB   . VAL   B 2 243 ? -28.401 -31.304 24.140  1.00 39.43  ? 748  VAL   B CB   1 
ATOM   3897 C  CG1  . VAL   B 2 243 ? -29.804 -31.554 24.653  1.00 46.54  ? 748  VAL   B CG1  1 
ATOM   3898 C  CG2  . VAL   B 2 243 ? -27.728 -32.629 23.847  1.00 44.46  ? 748  VAL   B CG2  1 
ATOM   3899 N  N    . THR   B 2 244 ? -26.263 -29.360 22.987  1.00 35.30  ? 749  THR   B N    1 
ATOM   3900 C  CA   . THR   B 2 244 ? -24.836 -29.259 22.747  1.00 38.81  ? 749  THR   B CA   1 
ATOM   3901 C  C    . THR   B 2 244 ? -24.129 -30.194 23.714  1.00 41.90  ? 749  THR   B C    1 
ATOM   3902 O  O    . THR   B 2 244 ? -24.578 -30.384 24.845  1.00 43.57  ? 749  THR   B O    1 
ATOM   3903 C  CB   . THR   B 2 244 ? -24.326 -27.833 22.953  1.00 43.14  ? 749  THR   B CB   1 
ATOM   3904 O  OG1  . THR   B 2 244 ? -24.773 -27.362 24.227  1.00 39.89  ? 749  THR   B OG1  1 
ATOM   3905 C  CG2  . THR   B 2 244 ? -24.831 -26.903 21.846  1.00 35.40  ? 749  THR   B CG2  1 
ATOM   3906 N  N    . ILE   B 2 245 ? -23.023 -30.772 23.270  1.00 45.53  ? 750  ILE   B N    1 
ATOM   3907 C  CA   . ILE   B 2 245 ? -22.343 -31.780 24.077  1.00 46.00  ? 750  ILE   B CA   1 
ATOM   3908 C  C    . ILE   B 2 245 ? -21.504 -31.112 25.160  1.00 49.20  ? 750  ILE   B C    1 
ATOM   3909 O  O    . ILE   B 2 245 ? -21.082 -29.953 25.043  1.00 49.07  ? 750  ILE   B O    1 
ATOM   3910 C  CB   . ILE   B 2 245 ? -21.489 -32.699 23.191  1.00 48.80  ? 750  ILE   B CB   1 
ATOM   3911 C  CG1  . ILE   B 2 245 ? -20.287 -31.937 22.661  1.00 47.56  ? 750  ILE   B CG1  1 
ATOM   3912 C  CG2  . ILE   B 2 245 ? -22.306 -33.250 22.047  1.00 44.43  ? 750  ILE   B CG2  1 
ATOM   3913 C  CD1  . ILE   B 2 245 ? -19.115 -32.815 22.445  1.00 51.90  ? 750  ILE   B CD1  1 
ATOM   3914 N  N    . GLY   B 2 246 ? -21.262 -31.864 26.233  1.00 55.35  ? 751  GLY   B N    1 
ATOM   3915 C  CA   . GLY   B 2 246 ? -20.484 -31.366 27.352  1.00 50.60  ? 751  GLY   B CA   1 
ATOM   3916 C  C    . GLY   B 2 246 ? -21.149 -30.241 28.110  1.00 58.60  ? 751  GLY   B C    1 
ATOM   3917 O  O    . GLY   B 2 246 ? -20.451 -29.386 28.671  1.00 62.90  ? 751  GLY   B O    1 
ATOM   3918 N  N    . SER   B 2 247 ? -22.485 -30.217 28.142  1.00 58.68  ? 752  SER   B N    1 
ATOM   3919 C  CA   . SER   B 2 247 ? -23.250 -29.129 28.758  1.00 69.16  ? 752  SER   B CA   1 
ATOM   3920 C  C    . SER   B 2 247 ? -22.861 -27.777 28.157  1.00 71.71  ? 752  SER   B C    1 
ATOM   3921 O  O    . SER   B 2 247 ? -22.581 -26.808 28.869  1.00 76.40  ? 752  SER   B O    1 
ATOM   3922 C  CB   . SER   B 2 247 ? -23.082 -29.122 30.280  1.00 74.57  ? 752  SER   B CB   1 
ATOM   3923 O  OG   . SER   B 2 247 ? -23.536 -30.335 30.851  1.00 78.01  ? 752  SER   B OG   1 
ATOM   3924 N  N    . GLY   B 2 248 ? -22.838 -27.719 26.828  1.00 59.02  ? 753  GLY   B N    1 
ATOM   3925 C  CA   . GLY   B 2 248 ? -22.448 -26.500 26.150  1.00 50.40  ? 753  GLY   B CA   1 
ATOM   3926 C  C    . GLY   B 2 248 ? -20.958 -26.236 26.128  1.00 53.03  ? 753  GLY   B C    1 
ATOM   3927 O  O    . GLY   B 2 248 ? -20.534 -25.093 26.329  1.00 52.55  ? 753  GLY   B O    1 
ATOM   3928 N  N    . TYR   B 2 249 ? -20.143 -27.259 25.891  1.00 49.15  ? 754  TYR   B N    1 
ATOM   3929 C  CA   . TYR   B 2 249 ? -18.710 -27.029 25.810  1.00 50.54  ? 754  TYR   B CA   1 
ATOM   3930 C  C    . TYR   B 2 249 ? -18.367 -26.322 24.504  1.00 44.83  ? 754  TYR   B C    1 
ATOM   3931 O  O    . TYR   B 2 249 ? -19.066 -26.458 23.500  1.00 41.02  ? 754  TYR   B O    1 
ATOM   3932 C  CB   . TYR   B 2 249 ? -17.945 -28.342 25.934  1.00 49.94  ? 754  TYR   B CB   1 
ATOM   3933 C  CG   . TYR   B 2 249 ? -16.448 -28.136 26.039  1.00 56.97  ? 754  TYR   B CG   1 
ATOM   3934 C  CD1  . TYR   B 2 249 ? -15.859 -27.755 27.247  1.00 56.32  ? 754  TYR   B CD1  1 
ATOM   3935 C  CD2  . TYR   B 2 249 ? -15.619 -28.331 24.935  1.00 53.14  ? 754  TYR   B CD2  1 
ATOM   3936 C  CE1  . TYR   B 2 249 ? -14.487 -27.562 27.349  1.00 57.27  ? 754  TYR   B CE1  1 
ATOM   3937 C  CE2  . TYR   B 2 249 ? -14.241 -28.143 25.030  1.00 56.06  ? 754  TYR   B CE2  1 
ATOM   3938 C  CZ   . TYR   B 2 249 ? -13.684 -27.761 26.238  1.00 57.54  ? 754  TYR   B CZ   1 
ATOM   3939 O  OH   . TYR   B 2 249 ? -12.323 -27.577 26.331  1.00 60.95  ? 754  TYR   B OH   1 
ATOM   3940 N  N    . ILE   B 2 250 ? -17.287 -25.543 24.535  1.00 42.65  ? 755  ILE   B N    1 
ATOM   3941 C  CA   . ILE   B 2 250 ? -16.839 -24.740 23.398  1.00 38.70  ? 755  ILE   B CA   1 
ATOM   3942 C  C    . ILE   B 2 250 ? -15.370 -25.044 23.150  1.00 42.18  ? 755  ILE   B C    1 
ATOM   3943 O  O    . ILE   B 2 250 ? -14.536 -24.866 24.044  1.00 42.65  ? 755  ILE   B O    1 
ATOM   3944 C  CB   . ILE   B 2 250 ? -17.046 -23.234 23.653  1.00 37.97  ? 755  ILE   B CB   1 
ATOM   3945 C  CG1  . ILE   B 2 250 ? -18.542 -22.926 23.828  1.00 37.31  ? 755  ILE   B CG1  1 
ATOM   3946 C  CG2  . ILE   B 2 250 ? -16.426 -22.403 22.542  1.00 35.67  ? 755  ILE   B CG2  1 
ATOM   3947 C  CD1  . ILE   B 2 250 ? -18.863 -21.441 24.099  1.00 39.03  ? 755  ILE   B CD1  1 
ATOM   3948 N  N    . PHE   B 2 251 ? -15.051 -25.523 21.955  1.00 37.90  ? 756  PHE   B N    1 
ATOM   3949 C  CA   . PHE   B 2 251 ? -13.661 -25.606 21.531  1.00 38.42  ? 756  PHE   B CA   1 
ATOM   3950 C  C    . PHE   B 2 251 ? -13.267 -24.295 20.859  1.00 37.92  ? 756  PHE   B C    1 
ATOM   3951 O  O    . PHE   B 2 251 ? -14.084 -23.658 20.185  1.00 31.20  ? 756  PHE   B O    1 
ATOM   3952 C  CB   . PHE   B 2 251 ? -13.436 -26.788 20.580  1.00 37.65  ? 756  PHE   B CB   1 
ATOM   3953 C  CG   . PHE   B 2 251 ? -12.009 -26.897 20.077  1.00 44.24  ? 756  PHE   B CG   1 
ATOM   3954 C  CD1  . PHE   B 2 251 ? -11.059 -27.606 20.799  1.00 46.78  ? 756  PHE   B CD1  1 
ATOM   3955 C  CD2  . PHE   B 2 251 ? -11.628 -26.329 18.867  1.00 46.10  ? 756  PHE   B CD2  1 
ATOM   3956 C  CE1  . PHE   B 2 251 ? -9.744  -27.719 20.346  1.00 49.19  ? 756  PHE   B CE1  1 
ATOM   3957 C  CE2  . PHE   B 2 251 ? -10.304 -26.439 18.405  1.00 43.81  ? 756  PHE   B CE2  1 
ATOM   3958 C  CZ   . PHE   B 2 251 ? -9.370  -27.131 19.153  1.00 42.79  ? 756  PHE   B CZ   1 
ATOM   3959 N  N    . ALA   B 2 252 ? -12.010 -23.893 21.060  1.00 33.34  ? 757  ALA   B N    1 
ATOM   3960 C  CA   . ALA   B 2 252 ? -11.451 -22.667 20.482  1.00 36.02  ? 757  ALA   B CA   1 
ATOM   3961 C  C    . ALA   B 2 252 ? -12.298 -21.448 20.851  1.00 34.37  ? 757  ALA   B C    1 
ATOM   3962 O  O    . ALA   B 2 252 ? -12.858 -20.754 19.983  1.00 29.94  ? 757  ALA   B O    1 
ATOM   3963 C  CB   . ALA   B 2 252 ? -11.304 -22.789 18.963  1.00 32.30  ? 757  ALA   B CB   1 
ATOM   3964 N  N    . THR   B 2 253 ? -12.383 -21.197 22.165  1.00 34.42  ? 758  THR   B N    1 
ATOM   3965 C  CA   . THR   B 2 253 ? -13.168 -20.077 22.662  1.00 33.34  ? 758  THR   B CA   1 
ATOM   3966 C  C    . THR   B 2 253 ? -12.714 -18.786 22.000  1.00 34.94  ? 758  THR   B C    1 
ATOM   3967 O  O    . THR   B 2 253 ? -11.511 -18.529 21.864  1.00 34.86  ? 758  THR   B O    1 
ATOM   3968 C  CB   . THR   B 2 253 ? -13.044 -19.940 24.183  1.00 40.14  ? 758  THR   B CB   1 
ATOM   3969 O  OG1  . THR   B 2 253 ? -11.653 -19.959 24.570  1.00 39.98  ? 758  THR   B OG1  1 
ATOM   3970 C  CG2  . THR   B 2 253 ? -13.796 -21.066 24.889  1.00 35.53  ? 758  THR   B CG2  1 
ATOM   3971 N  N    . THR   B 2 254 ? -13.690 -17.993 21.574  1.00 30.87  ? 759  THR   B N    1 
ATOM   3972 C  CA   . THR   B 2 254 ? -13.472 -16.686 20.983  1.00 30.11  ? 759  THR   B CA   1 
ATOM   3973 C  C    . THR   B 2 254 ? -14.761 -15.894 21.210  1.00 29.02  ? 759  THR   B C    1 
ATOM   3974 O  O    . THR   B 2 254 ? -15.539 -16.195 22.123  1.00 28.51  ? 759  THR   B O    1 
ATOM   3975 C  CB   . THR   B 2 254 ? -13.061 -16.820 19.502  1.00 27.89  ? 759  THR   B CB   1 
ATOM   3976 O  OG1  . THR   B 2 254 ? -12.765 -15.523 18.948  1.00 32.48  ? 759  THR   B OG1  1 
ATOM   3977 C  CG2  . THR   B 2 254 ? -14.182 -17.492 18.697  1.00 29.19  ? 759  THR   B CG2  1 
ATOM   3978 N  N    . GLY   B 2 255 ? -14.985 -14.865 20.404  1.00 31.36  ? 760  GLY   B N    1 
ATOM   3979 C  CA   . GLY   B 2 255 ? -16.223 -14.123 20.519  1.00 27.89  ? 760  GLY   B CA   1 
ATOM   3980 C  C    . GLY   B 2 255 ? -16.599 -13.547 19.174  1.00 29.54  ? 760  GLY   B C    1 
ATOM   3981 O  O    . GLY   B 2 255 ? -15.792 -13.540 18.246  1.00 28.86  ? 760  GLY   B O    1 
ATOM   3982 N  N    . TYR   B 2 256 ? -17.850 -13.096 19.064  1.00 26.41  ? 761  TYR   B N    1 
ATOM   3983 C  CA   . TYR   B 2 256 ? -18.193 -12.178 17.984  1.00 29.88  ? 761  TYR   B CA   1 
ATOM   3984 C  C    . TYR   B 2 256 ? -17.509 -10.835 18.228  1.00 31.90  ? 761  TYR   B C    1 
ATOM   3985 O  O    . TYR   B 2 256 ? -17.458 -10.354 19.361  1.00 33.40  ? 761  TYR   B O    1 
ATOM   3986 C  CB   . TYR   B 2 256 ? -19.696 -11.944 17.926  1.00 30.31  ? 761  TYR   B CB   1 
ATOM   3987 C  CG   . TYR   B 2 256 ? -20.537 -13.143 17.575  1.00 30.65  ? 761  TYR   B CG   1 
ATOM   3988 C  CD1  . TYR   B 2 256 ? -19.990 -14.271 16.982  1.00 29.17  ? 761  TYR   B CD1  1 
ATOM   3989 C  CD2  . TYR   B 2 256 ? -21.888 -13.160 17.907  1.00 30.37  ? 761  TYR   B CD2  1 
ATOM   3990 C  CE1  . TYR   B 2 256 ? -20.803 -15.381 16.677  1.00 28.61  ? 761  TYR   B CE1  1 
ATOM   3991 C  CE2  . TYR   B 2 256 ? -22.689 -14.243 17.624  1.00 32.51  ? 761  TYR   B CE2  1 
ATOM   3992 C  CZ   . TYR   B 2 256 ? -22.150 -15.351 17.014  1.00 29.11  ? 761  TYR   B CZ   1 
ATOM   3993 O  OH   . TYR   B 2 256 ? -22.978 -16.426 16.727  1.00 30.53  ? 761  TYR   B OH   1 
ATOM   3994 N  N    . GLY   B 2 257 ? -16.997 -10.218 17.162  1.00 30.63  ? 762  GLY   B N    1 
ATOM   3995 C  CA   . GLY   B 2 257 ? -16.475 -8.876  17.251  1.00 32.04  ? 762  GLY   B CA   1 
ATOM   3996 C  C    . GLY   B 2 257 ? -17.031 -7.993  16.149  1.00 33.85  ? 762  GLY   B C    1 
ATOM   3997 O  O    . GLY   B 2 257 ? -17.565 -8.462  15.143  1.00 32.68  ? 762  GLY   B O    1 
ATOM   3998 N  N    . ILE   B 2 258 ? -16.876 -6.692  16.354  1.00 35.35  ? 763  ILE   B N    1 
ATOM   3999 C  CA   . ILE   B 2 258 ? -17.140 -5.704  15.315  1.00 32.67  ? 763  ILE   B CA   1 
ATOM   4000 C  C    . ILE   B 2 258 ? -15.877 -5.621  14.474  1.00 33.16  ? 763  ILE   B C    1 
ATOM   4001 O  O    . ILE   B 2 258 ? -14.799 -5.376  15.017  1.00 34.18  ? 763  ILE   B O    1 
ATOM   4002 C  CB   . ILE   B 2 258 ? -17.461 -4.342  15.941  1.00 35.83  ? 763  ILE   B CB   1 
ATOM   4003 C  CG1  . ILE   B 2 258 ? -18.649 -4.500  16.885  1.00 38.77  ? 763  ILE   B CG1  1 
ATOM   4004 C  CG2  . ILE   B 2 258 ? -17.718 -3.289  14.850  1.00 38.58  ? 763  ILE   B CG2  1 
ATOM   4005 C  CD1  . ILE   B 2 258 ? -19.948 -4.388  16.252  1.00 40.61  ? 763  ILE   B CD1  1 
ATOM   4006 N  N    . ALA   B 2 259 ? -15.984 -5.864  13.163  1.00 32.37  ? 764  ALA   B N    1 
ATOM   4007 C  CA   . ALA   B 2 259 ? -14.816 -5.760  12.296  1.00 34.39  ? 764  ALA   B CA   1 
ATOM   4008 C  C    . ALA   B 2 259 ? -14.677 -4.332  11.783  1.00 32.24  ? 764  ALA   B C    1 
ATOM   4009 O  O    . ALA   B 2 259 ? -15.657 -3.739  11.326  1.00 37.95  ? 764  ALA   B O    1 
ATOM   4010 C  CB   . ALA   B 2 259 ? -14.893 -6.721  11.110  1.00 32.05  ? 764  ALA   B CB   1 
ATOM   4011 N  N    . LEU   B 2 260 ? -13.453 -3.800  11.830  1.00 33.60  ? 765  LEU   B N    1 
ATOM   4012 C  CA   . LEU   B 2 260 ? -13.174 -2.458  11.340  1.00 35.59  ? 765  LEU   B CA   1 
ATOM   4013 C  C    . LEU   B 2 260 ? -11.951 -2.481  10.440  1.00 38.01  ? 765  LEU   B C    1 
ATOM   4014 O  O    . LEU   B 2 260 ? -11.136 -3.405  10.495  1.00 33.82  ? 765  LEU   B O    1 
ATOM   4015 C  CB   . LEU   B 2 260 ? -12.932 -1.468  12.485  1.00 36.72  ? 765  LEU   B CB   1 
ATOM   4016 C  CG   . LEU   B 2 260 ? -14.044 -1.362  13.525  1.00 36.25  ? 765  LEU   B CG   1 
ATOM   4017 C  CD1  . LEU   B 2 260 ? -13.727 -2.216  14.747  1.00 40.17  ? 765  LEU   B CD1  1 
ATOM   4018 C  CD2  . LEU   B 2 260 ? -14.169 0.075   13.907  1.00 41.74  ? 765  LEU   B CD2  1 
ATOM   4019 N  N    . GLN   B 2 261 ? -11.806 -1.430  9.628   1.00 34.40  ? 766  GLN   B N    1 
ATOM   4020 C  CA   . GLN   B 2 261 ? -10.637 -1.371  8.764   1.00 39.26  ? 766  GLN   B CA   1 
ATOM   4021 C  C    . GLN   B 2 261 ? -9.370  -1.296  9.608   1.00 39.13  ? 766  GLN   B C    1 
ATOM   4022 O  O    . GLN   B 2 261 ? -9.367  -0.768  10.720  1.00 39.56  ? 766  GLN   B O    1 
ATOM   4023 C  CB   . GLN   B 2 261 ? -10.735 -0.185  7.809   1.00 41.93  ? 766  GLN   B CB   1 
ATOM   4024 C  CG   . GLN   B 2 261 ? -12.036 -0.229  7.022   1.00 44.37  ? 766  GLN   B CG   1 
ATOM   4025 C  CD   . GLN   B 2 261 ? -12.202 0.912   6.045   1.00 50.15  ? 766  GLN   B CD   1 
ATOM   4026 O  OE1  . GLN   B 2 261 ? -11.289 1.719   5.840   1.00 47.23  ? 766  GLN   B OE1  1 
ATOM   4027 N  NE2  . GLN   B 2 261 ? -13.382 0.980   5.419   1.00 45.80  ? 766  GLN   B NE2  1 
ATOM   4028 N  N    . LYS   B 2 262 ? -8.301  -1.892  9.097   1.00 40.52  ? 767  LYS   B N    1 
ATOM   4029 C  CA   . LYS   B 2 262 ? -7.023  -1.834  9.799   1.00 43.39  ? 767  LYS   B CA   1 
ATOM   4030 C  C    . LYS   B 2 262 ? -6.639  -0.385  10.044  1.00 47.29  ? 767  LYS   B C    1 
ATOM   4031 O  O    . LYS   B 2 262 ? -6.630  0.430   9.119   1.00 47.32  ? 767  LYS   B O    1 
ATOM   4032 C  CB   . LYS   B 2 262 ? -5.939  -2.553  8.997   1.00 42.04  ? 767  LYS   B CB   1 
ATOM   4033 C  CG   . LYS   B 2 262 ? -5.835  -4.017  9.343   1.00 46.12  ? 767  LYS   B CG   1 
ATOM   4034 C  CD   . LYS   B 2 262 ? -4.435  -4.540  9.091   1.00 52.05  ? 767  LYS   B CD   1 
ATOM   4035 C  CE   . LYS   B 2 262 ? -4.126  -5.688  10.046  1.00 51.48  ? 767  LYS   B CE   1 
ATOM   4036 N  NZ   . LYS   B 2 262 ? -2.696  -6.127  9.939   1.00 53.38  ? 767  LYS   B NZ   1 
ATOM   4037 N  N    . GLY   B 2 263 ? -6.369  -0.058  11.305  1.00 53.63  ? 768  GLY   B N    1 
ATOM   4038 C  CA   . GLY   B 2 263 ? -6.033  1.303   11.667  1.00 50.72  ? 768  GLY   B CA   1 
ATOM   4039 C  C    . GLY   B 2 263 ? -7.227  2.203   11.858  1.00 53.89  ? 768  GLY   B C    1 
ATOM   4040 O  O    . GLY   B 2 263 ? -7.067  3.428   11.864  1.00 60.14  ? 768  GLY   B O    1 
ATOM   4041 N  N    . SER   B 2 264 ? -8.419  1.630   12.023  1.00 43.64  ? 769  SER   B N    1 
ATOM   4042 C  CA   . SER   B 2 264 ? -9.630  2.432   12.120  1.00 47.13  ? 769  SER   B CA   1 
ATOM   4043 C  C    . SER   B 2 264 ? -9.549  3.424   13.279  1.00 51.06  ? 769  SER   B C    1 
ATOM   4044 O  O    . SER   B 2 264 ? -9.128  3.059   14.385  1.00 53.46  ? 769  SER   B O    1 
ATOM   4045 C  CB   . SER   B 2 264 ? -10.844 1.533   12.323  1.00 47.15  ? 769  SER   B CB   1 
ATOM   4046 O  OG   . SER   B 2 264 ? -11.968 2.314   12.670  1.00 46.52  ? 769  SER   B OG   1 
ATOM   4047 N  N    . PRO   B 2 265 ? -9.982  4.669   13.080  1.00 48.25  ? 770  PRO   B N    1 
ATOM   4048 C  CA   . PRO   B 2 265 ? -10.066 5.613   14.199  1.00 53.34  ? 770  PRO   B CA   1 
ATOM   4049 C  C    . PRO   B 2 265 ? -11.273 5.389   15.094  1.00 53.95  ? 770  PRO   B C    1 
ATOM   4050 O  O    . PRO   B 2 265 ? -11.425 6.099   16.094  1.00 55.63  ? 770  PRO   B O    1 
ATOM   4051 C  CB   . PRO   B 2 265 ? -10.154 6.973   13.490  1.00 50.79  ? 770  PRO   B CB   1 
ATOM   4052 C  CG   . PRO   B 2 265 ? -10.884 6.660   12.224  1.00 52.92  ? 770  PRO   B CG   1 
ATOM   4053 C  CD   . PRO   B 2 265 ? -10.455 5.265   11.816  1.00 49.22  ? 770  PRO   B CD   1 
ATOM   4054 N  N    . TRP   B 2 266 ? -12.144 4.440   14.759  1.00 48.08  ? 771  TRP   B N    1 
ATOM   4055 C  CA   . TRP   B 2 266 ? -13.318 4.168   15.575  1.00 48.02  ? 771  TRP   B CA   1 
ATOM   4056 C  C    . TRP   B 2 266 ? -13.080 3.051   16.579  1.00 46.69  ? 771  TRP   B C    1 
ATOM   4057 O  O    . TRP   B 2 266 ? -13.916 2.856   17.469  1.00 43.25  ? 771  TRP   B O    1 
ATOM   4058 C  CB   . TRP   B 2 266 ? -14.522 3.778   14.696  1.00 45.99  ? 771  TRP   B CB   1 
ATOM   4059 C  CG   . TRP   B 2 266 ? -15.016 4.839   13.750  1.00 48.03  ? 771  TRP   B CG   1 
ATOM   4060 C  CD1  . TRP   B 2 266 ? -14.826 4.886   12.399  1.00 45.24  ? 771  TRP   B CD1  1 
ATOM   4061 C  CD2  . TRP   B 2 266 ? -15.821 5.976   14.083  1.00 43.37  ? 771  TRP   B CD2  1 
ATOM   4062 N  NE1  . TRP   B 2 266 ? -15.455 5.993   11.876  1.00 43.28  ? 771  TRP   B NE1  1 
ATOM   4063 C  CE2  . TRP   B 2 266 ? -16.068 6.676   12.892  1.00 46.80  ? 771  TRP   B CE2  1 
ATOM   4064 C  CE3  . TRP   B 2 266 ? -16.345 6.473   15.278  1.00 44.21  ? 771  TRP   B CE3  1 
ATOM   4065 C  CZ2  . TRP   B 2 266 ? -16.812 7.858   12.862  1.00 53.15  ? 771  TRP   B CZ2  1 
ATOM   4066 C  CZ3  . TRP   B 2 266 ? -17.083 7.645   15.244  1.00 49.39  ? 771  TRP   B CZ3  1 
ATOM   4067 C  CH2  . TRP   B 2 266 ? -17.313 8.317   14.047  1.00 49.15  ? 771  TRP   B CH2  1 
ATOM   4068 N  N    . LYS   B 2 267 ? -11.972 2.311   16.454  1.00 42.10  ? 772  LYS   B N    1 
ATOM   4069 C  CA   . LYS   B 2 267 ? -11.823 1.084   17.224  1.00 44.31  ? 772  LYS   B CA   1 
ATOM   4070 C  C    . LYS   B 2 267 ? -11.780 1.373   18.718  1.00 40.95  ? 772  LYS   B C    1 
ATOM   4071 O  O    . LYS   B 2 267 ? -12.536 0.782   19.494  1.00 39.26  ? 772  LYS   B O    1 
ATOM   4072 C  CB   . LYS   B 2 267 ? -10.570 0.329   16.784  1.00 46.90  ? 772  LYS   B CB   1 
ATOM   4073 C  CG   . LYS   B 2 267 ? -10.252 -0.863  17.677  1.00 48.69  ? 772  LYS   B CG   1 
ATOM   4074 C  CD   . LYS   B 2 267 ? -8.906  -1.475  17.337  1.00 48.62  ? 772  LYS   B CD   1 
ATOM   4075 C  CE   . LYS   B 2 267 ? -8.445  -2.404  18.450  1.00 52.06  ? 772  LYS   B CE   1 
ATOM   4076 N  NZ   . LYS   B 2 267 ? -9.448  -3.500  18.736  1.00 53.26  ? 772  LYS   B NZ   1 
ATOM   4077 N  N    . ARG   B 2 268 ? -10.935 2.321   19.136  1.00 44.43  ? 773  ARG   B N    1 
ATOM   4078 C  CA   . ARG   B 2 268 ? -10.784 2.593   20.564  1.00 44.12  ? 773  ARG   B CA   1 
ATOM   4079 C  C    . ARG   B 2 268 ? -12.105 3.016   21.199  1.00 44.08  ? 773  ARG   B C    1 
ATOM   4080 O  O    . ARG   B 2 268 ? -12.436 2.573   22.301  1.00 41.28  ? 773  ARG   B O    1 
ATOM   4081 C  CB   . ARG   B 2 268 ? -9.700  3.655   20.797  1.00 45.96  ? 773  ARG   B CB   1 
ATOM   4082 C  CG   . ARG   B 2 268 ? -9.737  4.261   22.197  1.00 56.01  ? 773  ARG   B CG   1 
ATOM   4083 C  CD   . ARG   B 2 268 ? -8.377  4.775   22.697  1.00 61.33  ? 773  ARG   B CD   1 
ATOM   4084 N  NE   . ARG   B 2 268 ? -7.334  3.758   22.600  1.00 69.18  ? 773  ARG   B NE   1 
ATOM   4085 C  CZ   . ARG   B 2 268 ? -7.050  2.882   23.559  1.00 66.25  ? 773  ARG   B CZ   1 
ATOM   4086 N  NH1  . ARG   B 2 268 ? -7.704  2.882   24.716  1.00 50.91  ? 773  ARG   B NH1  1 
ATOM   4087 N  NH2  . ARG   B 2 268 ? -6.089  1.981   23.354  1.00 67.90  ? 773  ARG   B NH2  1 
ATOM   4088 N  N    . GLN   B 2 269 ? -12.874 3.876   20.524  1.00 43.69  ? 774  GLN   B N    1 
ATOM   4089 C  CA   . GLN   B 2 269 ? -14.135 4.333   21.104  1.00 41.86  ? 774  GLN   B CA   1 
ATOM   4090 C  C    . GLN   B 2 269 ? -15.163 3.203   21.158  1.00 39.44  ? 774  GLN   B C    1 
ATOM   4091 O  O    . GLN   B 2 269 ? -15.949 3.110   22.110  1.00 40.22  ? 774  GLN   B O    1 
ATOM   4092 C  CB   . GLN   B 2 269 ? -14.666 5.521   20.300  1.00 44.80  ? 774  GLN   B CB   1 
ATOM   4093 C  CG   . GLN   B 2 269 ? -14.033 6.865   20.649  1.00 50.45  ? 774  GLN   B CG   1 
ATOM   4094 C  CD   . GLN   B 2 269 ? -15.041 8.009   20.552  1.00 58.89  ? 774  GLN   B CD   1 
ATOM   4095 O  OE1  . GLN   B 2 269 ? -15.393 8.433   19.447  1.00 59.46  ? 774  GLN   B OE1  1 
ATOM   4096 N  NE2  . GLN   B 2 269 ? -15.509 8.509   21.699  1.00 60.33  ? 774  GLN   B NE2  1 
ATOM   4097 N  N    . ILE   B 2 270 ? -15.169 2.334   20.151  1.00 37.73  ? 775  ILE   B N    1 
ATOM   4098 C  CA   . ILE   B 2 270 ? -16.099 1.207   20.148  1.00 38.27  ? 775  ILE   B CA   1 
ATOM   4099 C  C    . ILE   B 2 270 ? -15.776 0.249   21.289  1.00 40.47  ? 775  ILE   B C    1 
ATOM   4100 O  O    . ILE   B 2 270 ? -16.673 -0.203  22.017  1.00 36.06  ? 775  ILE   B O    1 
ATOM   4101 C  CB   . ILE   B 2 270 ? -16.066 0.492   18.786  1.00 38.77  ? 775  ILE   B CB   1 
ATOM   4102 C  CG1  . ILE   B 2 270 ? -16.627 1.392   17.670  1.00 39.66  ? 775  ILE   B CG1  1 
ATOM   4103 C  CG2  . ILE   B 2 270 ? -16.819 -0.835  18.867  1.00 37.10  ? 775  ILE   B CG2  1 
ATOM   4104 C  CD1  . ILE   B 2 270 ? -18.087 1.688   17.801  1.00 44.77  ? 775  ILE   B CD1  1 
ATOM   4105 N  N    . ASP   B 2 271 ? -14.489 -0.088  21.440  1.00 38.26  ? 776  ASP   B N    1 
ATOM   4106 C  CA   . ASP   B 2 271 ? -14.022 -0.927  22.541  1.00 36.37  ? 776  ASP   B CA   1 
ATOM   4107 C  C    . ASP   B 2 271 ? -14.431 -0.364  23.892  1.00 36.97  ? 776  ASP   B C    1 
ATOM   4108 O  O    . ASP   B 2 271 ? -14.996 -1.075  24.727  1.00 35.88  ? 776  ASP   B O    1 
ATOM   4109 C  CB   . ASP   B 2 271 ? -12.495 -1.056  22.488  1.00 36.75  ? 776  ASP   B CB   1 
ATOM   4110 C  CG   . ASP   B 2 271 ? -12.026 -2.064  21.461  1.00 44.92  ? 776  ASP   B CG   1 
ATOM   4111 O  OD1  . ASP   B 2 271 ? -12.874 -2.817  20.951  1.00 41.86  ? 776  ASP   B OD1  1 
ATOM   4112 O  OD2  . ASP   B 2 271 ? -10.811 -2.093  21.154  1.00 43.17  ? 776  ASP   B OD2  1 
ATOM   4113 N  N    . LEU   B 2 272 ? -14.103 0.906   24.147  1.00 37.92  ? 777  LEU   B N    1 
ATOM   4114 C  CA   . LEU   B 2 272 ? -14.435 1.499   25.441  1.00 37.54  ? 777  LEU   B CA   1 
ATOM   4115 C  C    . LEU   B 2 272 ? -15.944 1.505   25.673  1.00 39.16  ? 777  LEU   B C    1 
ATOM   4116 O  O    . LEU   B 2 272 ? -16.411 1.266   26.794  1.00 42.20  ? 777  LEU   B O    1 
ATOM   4117 C  CB   . LEU   B 2 272 ? -13.854 2.913   25.530  1.00 39.84  ? 777  LEU   B CB   1 
ATOM   4118 C  CG   . LEU   B 2 272 ? -12.315 2.988   25.549  1.00 41.91  ? 777  LEU   B CG   1 
ATOM   4119 C  CD1  . LEU   B 2 272 ? -11.837 4.422   25.434  1.00 53.47  ? 777  LEU   B CD1  1 
ATOM   4120 C  CD2  . LEU   B 2 272 ? -11.768 2.366   26.825  1.00 42.54  ? 777  LEU   B CD2  1 
ATOM   4121 N  N    . ALA   B 2 273 ? -16.726 1.768   24.625  1.00 36.56  ? 778  ALA   B N    1 
ATOM   4122 C  CA   . ALA   B 2 273 ? -18.178 1.763   24.769  1.00 36.81  ? 778  ALA   B CA   1 
ATOM   4123 C  C    . ALA   B 2 273 ? -18.701 0.364   25.106  1.00 40.06  ? 778  ALA   B C    1 
ATOM   4124 O  O    . ALA   B 2 273 ? -19.530 0.201   26.013  1.00 36.44  ? 778  ALA   B O    1 
ATOM   4125 C  CB   . ALA   B 2 273 ? -18.825 2.304   23.488  1.00 37.44  ? 778  ALA   B CB   1 
ATOM   4126 N  N    . LEU   B 2 274 ? -18.220 -0.664  24.394  1.00 33.13  ? 779  LEU   B N    1 
ATOM   4127 C  CA   . LEU   B 2 274 ? -18.639 -2.031  24.704  1.00 36.78  ? 779  LEU   B CA   1 
ATOM   4128 C  C    . LEU   B 2 274 ? -18.304 -2.385  26.151  1.00 40.11  ? 779  LEU   B C    1 
ATOM   4129 O  O    . LEU   B 2 274 ? -19.139 -2.937  26.886  1.00 32.43  ? 779  LEU   B O    1 
ATOM   4130 C  CB   . LEU   B 2 274 ? -17.973 -3.015  23.741  1.00 35.37  ? 779  LEU   B CB   1 
ATOM   4131 C  CG   . LEU   B 2 274 ? -18.487 -2.961  22.299  1.00 32.85  ? 779  LEU   B CG   1 
ATOM   4132 C  CD1  . LEU   B 2 274 ? -17.695 -3.970  21.465  1.00 37.28  ? 779  LEU   B CD1  1 
ATOM   4133 C  CD2  . LEU   B 2 274 ? -19.986 -3.242  22.228  1.00 31.94  ? 779  LEU   B CD2  1 
ATOM   4134 N  N    . LEU   B 2 275 ? -17.077 -2.058  26.580  1.00 35.72  ? 780  LEU   B N    1 
ATOM   4135 C  CA   . LEU   B 2 275 ? -16.679 -2.341  27.951  1.00 38.29  ? 780  LEU   B CA   1 
ATOM   4136 C  C    . LEU   B 2 275 ? -17.492 -1.534  28.945  1.00 37.51  ? 780  LEU   B C    1 
ATOM   4137 O  O    . LEU   B 2 275 ? -17.744 -2.000  30.060  1.00 42.34  ? 780  LEU   B O    1 
ATOM   4138 C  CB   . LEU   B 2 275 ? -15.188 -2.072  28.133  1.00 32.70  ? 780  LEU   B CB   1 
ATOM   4139 C  CG   . LEU   B 2 275 ? -14.338 -3.029  27.289  1.00 32.42  ? 780  LEU   B CG   1 
ATOM   4140 C  CD1  . LEU   B 2 275 ? -12.870 -2.600  27.382  1.00 33.79  ? 780  LEU   B CD1  1 
ATOM   4141 C  CD2  . LEU   B 2 275 ? -14.504 -4.447  27.775  1.00 31.12  ? 780  LEU   B CD2  1 
ATOM   4142 N  N    . GLN   B 2 276 ? -17.908 -0.327  28.570  1.00 37.69  ? 781  GLN   B N    1 
ATOM   4143 C  CA   . GLN   B 2 276 ? -18.784 0.431   29.453  1.00 42.57  ? 781  GLN   B CA   1 
ATOM   4144 C  C    . GLN   B 2 276 ? -20.138 -0.247  29.584  1.00 41.23  ? 781  GLN   B C    1 
ATOM   4145 O  O    . GLN   B 2 276 ? -20.673 -0.365  30.693  1.00 43.93  ? 781  GLN   B O    1 
ATOM   4146 C  CB   . GLN   B 2 276 ? -18.943 1.858   28.941  1.00 41.65  ? 781  GLN   B CB   1 
ATOM   4147 C  CG   . GLN   B 2 276 ? -19.896 2.708   29.759  1.00 48.30  ? 781  GLN   B CG   1 
ATOM   4148 C  CD   . GLN   B 2 276 ? -20.585 3.767   28.917  1.00 58.31  ? 781  GLN   B CD   1 
ATOM   4149 O  OE1  . GLN   B 2 276 ? -19.929 4.626   28.320  1.00 58.27  ? 781  GLN   B OE1  1 
ATOM   4150 N  NE2  . GLN   B 2 276 ? -21.916 3.717   28.868  1.00 62.30  ? 781  GLN   B NE2  1 
ATOM   4151 N  N    . PHE   B 2 277 ? -20.717 -0.689  28.461  1.00 39.31  ? 782  PHE   B N    1 
ATOM   4152 C  CA   . PHE   B 2 277 ? -21.993 -1.402  28.509  1.00 40.99  ? 782  PHE   B CA   1 
ATOM   4153 C  C    . PHE   B 2 277 ? -21.901 -2.614  29.424  1.00 42.27  ? 782  PHE   B C    1 
ATOM   4154 O  O    . PHE   B 2 277 ? -22.820 -2.894  30.203  1.00 43.03  ? 782  PHE   B O    1 
ATOM   4155 C  CB   . PHE   B 2 277 ? -22.414 -1.858  27.107  1.00 39.46  ? 782  PHE   B CB   1 
ATOM   4156 C  CG   . PHE   B 2 277 ? -22.522 -0.744  26.091  1.00 41.50  ? 782  PHE   B CG   1 
ATOM   4157 C  CD1  . PHE   B 2 277 ? -22.653 0.576   26.486  1.00 44.72  ? 782  PHE   B CD1  1 
ATOM   4158 C  CD2  . PHE   B 2 277 ? -22.514 -1.036  24.733  1.00 37.64  ? 782  PHE   B CD2  1 
ATOM   4159 C  CE1  . PHE   B 2 277 ? -22.753 1.589   25.552  1.00 42.94  ? 782  PHE   B CE1  1 
ATOM   4160 C  CE2  . PHE   B 2 277 ? -22.615 -0.036  23.790  1.00 42.06  ? 782  PHE   B CE2  1 
ATOM   4161 C  CZ   . PHE   B 2 277 ? -22.744 1.289   24.201  1.00 39.09  ? 782  PHE   B CZ   1 
ATOM   4162 N  N    . VAL   B 2 278 ? -20.805 -3.363  29.317  1.00 36.27  ? 783  VAL   B N    1 
ATOM   4163 C  CA   . VAL   B 2 278 ? -20.581 -4.522  30.184  1.00 43.22  ? 783  VAL   B CA   1 
ATOM   4164 C  C    . VAL   B 2 278 ? -20.541 -4.100  31.646  1.00 44.61  ? 783  VAL   B C    1 
ATOM   4165 O  O    . VAL   B 2 278 ? -21.287 -4.622  32.486  1.00 41.78  ? 783  VAL   B O    1 
ATOM   4166 C  CB   . VAL   B 2 278 ? -19.281 -5.238  29.781  1.00 39.00  ? 783  VAL   B CB   1 
ATOM   4167 C  CG1  . VAL   B 2 278 ? -18.809 -6.165  30.901  1.00 41.78  ? 783  VAL   B CG1  1 
ATOM   4168 C  CG2  . VAL   B 2 278 ? -19.504 -6.022  28.513  1.00 39.45  ? 783  VAL   B CG2  1 
ATOM   4169 N  N    . GLY   B 2 279 ? -19.660 -3.150  31.968  1.00 46.05  ? 784  GLY   B N    1 
ATOM   4170 C  CA   . GLY   B 2 279 ? -19.432 -2.794  33.356  1.00 48.23  ? 784  GLY   B CA   1 
ATOM   4171 C  C    . GLY   B 2 279 ? -20.645 -2.201  34.041  1.00 51.73  ? 784  GLY   B C    1 
ATOM   4172 O  O    . GLY   B 2 279 ? -20.840 -2.410  35.239  1.00 54.26  ? 784  GLY   B O    1 
ATOM   4173 N  N    . ASP   B 2 280 ? -21.480 -1.475  33.303  1.00 51.38  ? 785  ASP   B N    1 
ATOM   4174 C  CA   . ASP   B 2 280 ? -22.653 -0.830  33.878  1.00 52.27  ? 785  ASP   B CA   1 
ATOM   4175 C  C    . ASP   B 2 280 ? -23.902 -1.700  33.842  1.00 55.65  ? 785  ASP   B C    1 
ATOM   4176 O  O    . ASP   B 2 280 ? -24.989 -1.200  34.137  1.00 55.12  ? 785  ASP   B O    1 
ATOM   4177 C  CB   . ASP   B 2 280 ? -22.940 0.487   33.161  1.00 57.89  ? 785  ASP   B CB   1 
ATOM   4178 C  CG   . ASP   B 2 280 ? -21.700 1.331   32.977  1.00 69.94  ? 785  ASP   B CG   1 
ATOM   4179 O  OD1  . ASP   B 2 280 ? -20.637 0.949   33.508  1.00 70.12  ? 785  ASP   B OD1  1 
ATOM   4180 O  OD2  . ASP   B 2 280 ? -21.789 2.368   32.288  1.00 75.62  ? 785  ASP   B OD2  1 
ATOM   4181 N  N    . GLY   B 2 281 ? -23.785 -2.972  33.477  1.00 52.19  ? 786  GLY   B N    1 
ATOM   4182 C  CA   . GLY   B 2 281 ? -24.942 -3.843  33.505  1.00 50.85  ? 786  GLY   B CA   1 
ATOM   4183 C  C    . GLY   B 2 281 ? -25.841 -3.792  32.289  1.00 54.78  ? 786  GLY   B C    1 
ATOM   4184 O  O    . GLY   B 2 281 ? -26.818 -4.547  32.230  1.00 53.90  ? 786  GLY   B O    1 
ATOM   4185 N  N    . GLU   B 2 282 ? -25.532 -2.957  31.299  1.00 52.95  ? 787  GLU   B N    1 
ATOM   4186 C  CA   . GLU   B 2 282 ? -26.420 -2.816  30.152  1.00 55.23  ? 787  GLU   B CA   1 
ATOM   4187 C  C    . GLU   B 2 282 ? -26.459 -4.064  29.275  1.00 54.90  ? 787  GLU   B C    1 
ATOM   4188 O  O    . GLU   B 2 282 ? -27.443 -4.269  28.559  1.00 53.93  ? 787  GLU   B O    1 
ATOM   4189 C  CB   . GLU   B 2 282 ? -25.994 -1.623  29.308  1.00 53.13  ? 787  GLU   B CB   1 
ATOM   4190 C  CG   . GLU   B 2 282 ? -26.271 -0.294  29.946  1.00 61.47  ? 787  GLU   B CG   1 
ATOM   4191 C  CD   . GLU   B 2 282 ? -25.774 0.860   29.094  1.00 61.84  ? 787  GLU   B CD   1 
ATOM   4192 O  OE1  . GLU   B 2 282 ? -24.962 1.658   29.613  1.00 62.02  ? 787  GLU   B OE1  1 
ATOM   4193 O  OE2  . GLU   B 2 282 ? -26.202 0.974   27.919  1.00 61.48  ? 787  GLU   B OE2  1 
ATOM   4194 N  N    . MET   B 2 283 ? -25.420 -4.900  29.300  1.00 47.23  ? 788  MET   B N    1 
ATOM   4195 C  CA   . MET   B 2 283 ? -25.424 -6.051  28.404  1.00 48.69  ? 788  MET   B CA   1 
ATOM   4196 C  C    . MET   B 2 283 ? -26.378 -7.131  28.886  1.00 52.90  ? 788  MET   B C    1 
ATOM   4197 O  O    . MET   B 2 283 ? -26.968 -7.842  28.059  1.00 49.50  ? 788  MET   B O    1 
ATOM   4198 C  CB   . MET   B 2 283 ? -24.012 -6.618  28.239  1.00 47.35  ? 788  MET   B CB   1 
ATOM   4199 C  CG   . MET   B 2 283 ? -23.076 -5.717  27.456  1.00 48.28  ? 788  MET   B CG   1 
ATOM   4200 S  SD   . MET   B 2 283 ? -23.083 -6.004  25.675  1.00 51.71  ? 788  MET   B SD   1 
ATOM   4201 C  CE   . MET   B 2 283 ? -21.402 -5.543  25.211  1.00 37.59  ? 788  MET   B CE   1 
ATOM   4202 N  N    . GLU   B 2 284 ? -26.558 -7.258  30.207  1.00 57.26  ? 789  GLU   B N    1 
ATOM   4203 C  CA   . GLU   B 2 284 ? -27.469 -8.266  30.743  1.00 58.33  ? 789  GLU   B CA   1 
ATOM   4204 C  C    . GLU   B 2 284 ? -28.861 -8.107  30.158  1.00 58.27  ? 789  GLU   B C    1 
ATOM   4205 O  O    . GLU   B 2 284 ? -29.522 -9.100  29.829  1.00 58.15  ? 789  GLU   B O    1 
ATOM   4206 C  CB   . GLU   B 2 284 ? -27.521 -8.180  32.271  1.00 59.12  ? 789  GLU   B CB   1 
ATOM   4207 N  N    . GLU   B 2 285 ? -29.315 -6.859  30.008  1.00 60.82  ? 790  GLU   B N    1 
ATOM   4208 C  CA   . GLU   B 2 285 ? -30.620 -6.596  29.416  1.00 59.18  ? 790  GLU   B CA   1 
ATOM   4209 C  C    . GLU   B 2 285 ? -30.719 -7.171  28.008  1.00 56.56  ? 790  GLU   B C    1 
ATOM   4210 O  O    . GLU   B 2 285 ? -31.726 -7.806  27.662  1.00 51.57  ? 790  GLU   B O    1 
ATOM   4211 C  CB   . GLU   B 2 285 ? -30.888 -5.090  29.401  1.00 66.50  ? 790  GLU   B CB   1 
ATOM   4212 C  CG   . GLU   B 2 285 ? -30.382 -4.336  30.637  1.00 76.43  ? 790  GLU   B CG   1 
ATOM   4213 C  CD   . GLU   B 2 285 ? -29.958 -2.900  30.328  1.00 87.29  ? 790  GLU   B CD   1 
ATOM   4214 O  OE1  . GLU   B 2 285 ? -29.977 -2.511  29.137  1.00 90.63  ? 790  GLU   B OE1  1 
ATOM   4215 O  OE2  . GLU   B 2 285 ? -29.619 -2.158  31.281  1.00 78.37  ? 790  GLU   B OE2  1 
ATOM   4216 N  N    . LEU   B 2 286 ? -29.693 -6.943  27.173  1.00 50.98  ? 791  LEU   B N    1 
ATOM   4217 C  CA   . LEU   B 2 286 ? -29.725 -7.458  25.807  1.00 49.98  ? 791  LEU   B CA   1 
ATOM   4218 C  C    . LEU   B 2 286 ? -29.701 -8.981  25.787  1.00 46.77  ? 791  LEU   B C    1 
ATOM   4219 O  O    . LEU   B 2 286 ? -30.442 -9.607  25.014  1.00 44.49  ? 791  LEU   B O    1 
ATOM   4220 C  CB   . LEU   B 2 286 ? -28.567 -6.884  24.983  1.00 40.92  ? 791  LEU   B CB   1 
ATOM   4221 C  CG   . LEU   B 2 286 ? -28.634 -5.370  24.750  1.00 47.18  ? 791  LEU   B CG   1 
ATOM   4222 C  CD1  . LEU   B 2 286 ? -27.586 -4.886  23.745  1.00 44.18  ? 791  LEU   B CD1  1 
ATOM   4223 C  CD2  . LEU   B 2 286 ? -30.021 -4.981  24.300  1.00 49.65  ? 791  LEU   B CD2  1 
ATOM   4224 N  N    . GLU   B 2 287 ? -28.870 -9.591  26.636  1.00 44.31  ? 792  GLU   B N    1 
ATOM   4225 C  CA   . GLU   B 2 287 ? -28.824 -11.047 26.718  1.00 44.01  ? 792  GLU   B CA   1 
ATOM   4226 C  C    . GLU   B 2 287 ? -30.181 -11.618 27.108  1.00 45.13  ? 792  GLU   B C    1 
ATOM   4227 O  O    . GLU   B 2 287 ? -30.668 -12.579 26.495  1.00 42.79  ? 792  GLU   B O    1 
ATOM   4228 C  CB   . GLU   B 2 287 ? -27.753 -11.483 27.716  1.00 42.58  ? 792  GLU   B CB   1 
ATOM   4229 C  CG   . GLU   B 2 287 ? -27.754 -12.974 27.978  1.00 40.02  ? 792  GLU   B CG   1 
ATOM   4230 C  CD   . GLU   B 2 287 ? -26.641 -13.411 28.907  1.00 45.49  ? 792  GLU   B CD   1 
ATOM   4231 O  OE1  . GLU   B 2 287 ? -25.987 -12.522 29.495  1.00 42.90  ? 792  GLU   B OE1  1 
ATOM   4232 O  OE2  . GLU   B 2 287 ? -26.438 -14.643 29.065  1.00 46.31  ? 792  GLU   B OE2  1 
ATOM   4233 N  N    . THR   B 2 288 ? -30.800 -11.045 28.139  1.00 48.30  ? 793  THR   B N    1 
ATOM   4234 C  CA   . THR   B 2 288 ? -32.107 -11.521 28.583  1.00 44.97  ? 793  THR   B CA   1 
ATOM   4235 C  C    . THR   B 2 288 ? -33.157 -11.337 27.488  1.00 48.41  ? 793  THR   B C    1 
ATOM   4236 O  O    . THR   B 2 288 ? -33.975 -12.232 27.230  1.00 45.78  ? 793  THR   B O    1 
ATOM   4237 C  CB   . THR   B 2 288 ? -32.499 -10.776 29.862  1.00 50.71  ? 793  THR   B CB   1 
ATOM   4238 O  OG1  . THR   B 2 288 ? -31.495 -10.997 30.866  1.00 43.67  ? 793  THR   B OG1  1 
ATOM   4239 C  CG2  . THR   B 2 288 ? -33.862 -11.242 30.384  1.00 50.59  ? 793  THR   B CG2  1 
ATOM   4240 N  N    . LEU   B 2 289 ? -33.132 -10.185 26.819  1.00 41.98  ? 794  LEU   B N    1 
ATOM   4241 C  CA   . LEU   B 2 289 ? -34.087 -9.908  25.763  1.00 42.26  ? 794  LEU   B CA   1 
ATOM   4242 C  C    . LEU   B 2 289 ? -33.989 -10.917 24.619  1.00 44.89  ? 794  LEU   B C    1 
ATOM   4243 O  O    . LEU   B 2 289 ? -35.015 -11.440 24.168  1.00 43.93  ? 794  LEU   B O    1 
ATOM   4244 C  CB   . LEU   B 2 289 ? -33.869 -8.484  25.266  1.00 43.21  ? 794  LEU   B CB   1 
ATOM   4245 C  CG   . LEU   B 2 289 ? -34.952 -7.884  24.394  1.00 51.16  ? 794  LEU   B CG   1 
ATOM   4246 C  CD1  . LEU   B 2 289 ? -36.256 -7.814  25.202  1.00 56.85  ? 794  LEU   B CD1  1 
ATOM   4247 C  CD2  . LEU   B 2 289 ? -34.504 -6.492  23.955  1.00 49.26  ? 794  LEU   B CD2  1 
ATOM   4248 N  N    . TRP   B 2 290 ? -32.773 -11.224 24.146  1.00 37.13  ? 795  TRP   B N    1 
ATOM   4249 C  CA   . TRP   B 2 290 ? -32.601 -11.944 22.883  1.00 39.18  ? 795  TRP   B CA   1 
ATOM   4250 C  C    . TRP   B 2 290 ? -32.104 -13.382 23.011  1.00 41.10  ? 795  TRP   B C    1 
ATOM   4251 O  O    . TRP   B 2 290 ? -32.366 -14.188 22.113  1.00 42.58  ? 795  TRP   B O    1 
ATOM   4252 C  CB   . TRP   B 2 290 ? -31.627 -11.183 21.961  1.00 39.95  ? 795  TRP   B CB   1 
ATOM   4253 C  CG   . TRP   B 2 290 ? -32.119 -9.816  21.510  1.00 41.50  ? 795  TRP   B CG   1 
ATOM   4254 C  CD1  . TRP   B 2 290 ? -31.683 -8.592  21.947  1.00 38.67  ? 795  TRP   B CD1  1 
ATOM   4255 C  CD2  . TRP   B 2 290 ? -33.133 -9.552  20.528  1.00 40.01  ? 795  TRP   B CD2  1 
ATOM   4256 N  NE1  . TRP   B 2 290 ? -32.372 -7.585  21.300  1.00 37.91  ? 795  TRP   B NE1  1 
ATOM   4257 C  CE2  . TRP   B 2 290 ? -33.264 -8.149  20.425  1.00 40.26  ? 795  TRP   B CE2  1 
ATOM   4258 C  CE3  . TRP   B 2 290 ? -33.927 -10.365 19.714  1.00 38.45  ? 795  TRP   B CE3  1 
ATOM   4259 C  CZ2  . TRP   B 2 290 ? -34.173 -7.542  19.548  1.00 43.94  ? 795  TRP   B CZ2  1 
ATOM   4260 C  CZ3  . TRP   B 2 290 ? -34.842 -9.761  18.853  1.00 41.57  ? 795  TRP   B CZ3  1 
ATOM   4261 C  CH2  . TRP   B 2 290 ? -34.949 -8.366  18.774  1.00 43.33  ? 795  TRP   B CH2  1 
ATOM   4262 N  N    . LEU   B 2 291 ? -31.392 -13.736 24.076  1.00 37.46  ? 796  LEU   B N    1 
ATOM   4263 C  CA   . LEU   B 2 291 ? -30.609 -14.964 24.086  1.00 42.05  ? 796  LEU   B CA   1 
ATOM   4264 C  C    . LEU   B 2 291 ? -31.126 -16.026 25.050  1.00 45.94  ? 796  LEU   B C    1 
ATOM   4265 O  O    . LEU   B 2 291 ? -30.547 -17.113 25.112  1.00 51.36  ? 796  LEU   B O    1 
ATOM   4266 C  CB   . LEU   B 2 291 ? -29.135 -14.643 24.400  1.00 39.89  ? 796  LEU   B CB   1 
ATOM   4267 C  CG   . LEU   B 2 291 ? -28.400 -13.707 23.434  1.00 36.47  ? 796  LEU   B CG   1 
ATOM   4268 C  CD1  . LEU   B 2 291 ? -26.901 -13.575 23.743  1.00 39.19  ? 796  LEU   B CD1  1 
ATOM   4269 C  CD2  . LEU   B 2 291 ? -28.611 -14.179 22.002  1.00 38.25  ? 796  LEU   B CD2  1 
ATOM   4270 N  N    . THR   B 2 292 ? -32.206 -15.762 25.777  1.00 46.44  ? 797  THR   B N    1 
ATOM   4271 C  CA   . THR   B 2 292 ? -32.738 -16.726 26.730  1.00 52.94  ? 797  THR   B CA   1 
ATOM   4272 C  C    . THR   B 2 292 ? -33.485 -17.843 26.004  1.00 55.85  ? 797  THR   B C    1 
ATOM   4273 O  O    . THR   B 2 292 ? -33.985 -17.664 24.892  1.00 57.83  ? 797  THR   B O    1 
ATOM   4274 C  CB   . THR   B 2 292 ? -33.665 -16.021 27.722  1.00 57.86  ? 797  THR   B CB   1 
ATOM   4275 O  OG1  . THR   B 2 292 ? -32.970 -14.908 28.294  1.00 58.00  ? 797  THR   B OG1  1 
ATOM   4276 C  CG2  . THR   B 2 292 ? -34.102 -16.961 28.855  1.00 64.44  ? 797  THR   B CG2  1 
ATOM   4277 N  N    . GLY   B 2 293 ? -33.536 -19.007 26.633  1.00 55.00  ? 798  GLY   B N    1 
ATOM   4278 C  CA   . GLY   B 2 293 ? -34.237 -20.142 26.065  1.00 53.15  ? 798  GLY   B CA   1 
ATOM   4279 C  C    . GLY   B 2 293 ? -34.878 -20.979 27.152  1.00 58.01  ? 798  GLY   B C    1 
ATOM   4280 O  O    . GLY   B 2 293 ? -34.392 -21.046 28.282  1.00 59.25  ? 798  GLY   B O    1 
ATOM   4281 N  N    . ILE   B 2 294 ? -35.981 -21.637 26.785  1.00 55.08  ? 799  ILE   B N    1 
ATOM   4282 C  CA   . ILE   B 2 294 ? -36.734 -22.440 27.745  1.00 58.99  ? 799  ILE   B CA   1 
ATOM   4283 C  C    . ILE   B 2 294 ? -35.929 -23.656 28.191  1.00 60.94  ? 799  ILE   B C    1 
ATOM   4284 O  O    . ILE   B 2 294 ? -36.054 -24.116 29.329  1.00 54.03  ? 799  ILE   B O    1 
ATOM   4285 C  CB   . ILE   B 2 294 ? -38.083 -22.848 27.136  1.00 55.61  ? 799  ILE   B CB   1 
ATOM   4286 C  CG1  . ILE   B 2 294 ? -38.925 -21.602 26.852  1.00 61.56  ? 799  ILE   B CG1  1 
ATOM   4287 C  CG2  . ILE   B 2 294 ? -38.829 -23.796 28.060  1.00 64.32  ? 799  ILE   B CG2  1 
ATOM   4288 C  CD1  . ILE   B 2 294 ? -39.972 -21.806 25.777  1.00 57.97  ? 799  ILE   B CD1  1 
ATOM   4289 N  N    . CYS   B 2 295 ? -35.097 -24.200 27.312  1.00 58.33  ? 800  CYS   B N    1 
ATOM   4290 C  CA   . CYS   B 2 295 ? -34.326 -25.377 27.683  1.00 57.50  ? 800  CYS   B CA   1 
ATOM   4291 C  C    . CYS   B 2 295 ? -33.067 -24.959 28.446  1.00 59.77  ? 800  CYS   B C    1 
ATOM   4292 O  O    . CYS   B 2 295 ? -32.742 -25.535 29.484  1.00 65.67  ? 800  CYS   B O    1 
ATOM   4293 C  CB   . CYS   B 2 295 ? -33.953 -26.193 26.447  1.00 56.83  ? 800  CYS   B CB   1 
ATOM   4294 S  SG   . CYS   B 2 295 ? -35.314 -26.548 25.317  1.00 52.73  ? 800  CYS   B SG   1 
HETATM 4295 N  N    . GLY   C 3 .   ? -9.008  -10.879 37.760  1.00 32.20  ? 1001 GLY   A N    1 
HETATM 4296 C  CA   . GLY   C 3 .   ? -8.919  -9.982  38.893  1.00 33.38  ? 1001 GLY   A CA   1 
HETATM 4297 C  C    . GLY   C 3 .   ? -8.343  -8.646  38.491  1.00 29.22  ? 1001 GLY   A C    1 
HETATM 4298 O  O    . GLY   C 3 .   ? -8.271  -7.704  39.280  1.00 30.15  ? 1001 GLY   A O    1 
HETATM 4299 O  OXT  . GLY   C 3 .   ? -7.958  -8.479  37.338  1.00 29.09  ? 1001 GLY   A OXT  1 
HETATM 4300 N  N    . GLU   D 4 .   ? -19.688 -17.089 13.027  1.00 28.80  ? 1001 GLU   B N    1 
HETATM 4301 C  CA   . GLU   D 4 .   ? -19.092 -17.816 11.913  1.00 29.60  ? 1001 GLU   B CA   1 
HETATM 4302 C  C    . GLU   D 4 .   ? -18.193 -16.901 11.121  1.00 29.24  ? 1001 GLU   B C    1 
HETATM 4303 O  O    . GLU   D 4 .   ? -18.047 -15.736 11.477  1.00 28.81  ? 1001 GLU   B O    1 
HETATM 4304 C  CB   . GLU   D 4 .   ? -20.159 -18.401 10.985  1.00 31.10  ? 1001 GLU   B CB   1 
HETATM 4305 C  CG   . GLU   D 4 .   ? -20.664 -19.754 11.374  1.00 32.78  ? 1001 GLU   B CG   1 
HETATM 4306 C  CD   . GLU   D 4 .   ? -19.565 -20.789 11.548  1.00 32.10  ? 1001 GLU   B CD   1 
HETATM 4307 O  OE1  . GLU   D 4 .   ? -18.818 -21.075 10.583  1.00 33.74  ? 1001 GLU   B OE1  1 
HETATM 4308 O  OE2  . GLU   D 4 .   ? -19.460 -21.346 12.660  1.00 35.59  ? 1001 GLU   B OE2  1 
HETATM 4309 O  OXT  . GLU   D 4 .   ? -17.632 -17.309 10.110  1.00 28.48  ? 1001 GLU   B OXT  1 
HETATM 4310 C  C10  . A1BRB E 5 .   ? -22.901 -14.902 25.758  1.00 36.01  ? 1002 A1BRB B C10  1 
HETATM 4311 C  C11  . A1BRB E 5 .   ? -24.037 -14.228 26.152  1.00 36.20  ? 1002 A1BRB B C11  1 
HETATM 4312 C  C13  . A1BRB E 5 .   ? -19.386 -9.541  27.767  1.00 35.62  ? 1002 A1BRB B C13  1 
HETATM 4313 C  C14  . A1BRB E 5 .   ? -18.462 -9.593  28.800  1.00 31.43  ? 1002 A1BRB B C14  1 
HETATM 4314 C  C16  . A1BRB E 5 .   ? -17.000 -8.346  27.528  1.00 33.99  ? 1002 A1BRB B C16  1 
HETATM 4315 C  C17  . A1BRB E 5 .   ? -17.930 -8.296  26.502  1.00 32.63  ? 1002 A1BRB B C17  1 
HETATM 4316 C  C2   . A1BRB E 5 .   ? -20.691 -10.204 27.906  1.00 35.95  ? 1002 A1BRB B C2   1 
HETATM 4317 C  C20  . A1BRB E 5 .   ? -14.786 -8.360  28.144  1.00 35.19  ? 1002 A1BRB B C20  1 
HETATM 4318 C  C21  . A1BRB E 5 .   ? -14.121 -9.520  27.425  1.00 37.35  ? 1002 A1BRB B C21  1 
HETATM 4319 C  C24  . A1BRB E 5 .   ? -15.047 -10.679 27.467  1.00 32.65  ? 1002 A1BRB B C24  1 
HETATM 4320 C  C25  . A1BRB E 5 .   ? -15.056 -11.552 28.556  1.00 31.32  ? 1002 A1BRB B C25  1 
HETATM 4321 C  C26  . A1BRB E 5 .   ? -15.948 -12.628 28.578  1.00 33.95  ? 1002 A1BRB B C26  1 
HETATM 4322 C  C27  . A1BRB E 5 .   ? -16.838 -12.843 27.516  1.00 30.75  ? 1002 A1BRB B C27  1 
HETATM 4323 C  C28  . A1BRB E 5 .   ? -16.806 -11.966 26.426  1.00 34.50  ? 1002 A1BRB B C28  1 
HETATM 4324 C  C30  . A1BRB E 5 .   ? -15.918 -10.891 26.400  1.00 30.47  ? 1002 A1BRB B C30  1 
HETATM 4325 C  C4   . A1BRB E 5 .   ? -22.759 -10.862 26.789  1.00 35.55  ? 1002 A1BRB B C4   1 
HETATM 4326 C  C5   . A1BRB E 5 .   ? -23.827 -10.411 27.779  1.00 34.12  ? 1002 A1BRB B C5   1 
HETATM 4327 C  C6   . A1BRB E 5 .   ? -23.971 -10.070 26.327  1.00 39.02  ? 1002 A1BRB B C6   1 
HETATM 4328 C  C7   . A1BRB E 5 .   ? -22.816 -12.311 26.431  1.00 37.63  ? 1002 A1BRB B C7   1 
HETATM 4329 C  C8   . A1BRB E 5 .   ? -21.682 -12.986 26.038  1.00 32.69  ? 1002 A1BRB B C8   1 
HETATM 4330 F  F22  . A1BRB E 5 .   ? -13.818 -9.124  26.154  1.00 36.21  ? 1002 A1BRB B F22  1 
HETATM 4331 F  F23  . A1BRB E 5 .   ? -12.946 -9.812  28.055  1.00 35.54  ? 1002 A1BRB B F23  1 
HETATM 4332 N  N12  . A1BRB E 5 .   ? -24.023 -12.922 26.488  1.00 36.30  ? 1002 A1BRB B N12  1 
HETATM 4333 N  N15  . A1BRB E 5 .   ? -17.257 -8.983  28.690  1.00 35.93  ? 1002 A1BRB B N15  1 
HETATM 4334 N  N18  . A1BRB E 5 .   ? -19.141 -8.896  26.610  1.00 31.57  ? 1002 A1BRB B N18  1 
HETATM 4335 N  N3   . A1BRB E 5 .   ? -21.467 -10.233 26.760  1.00 33.11  ? 1002 A1BRB B N3   1 
HETATM 4336 N  N9   . A1BRB E 5 .   ? -21.696 -14.296 25.695  1.00 36.70  ? 1002 A1BRB B N9   1 
HETATM 4337 O  O1   . A1BRB E 5 .   ? -21.014 -10.698 28.979  1.00 36.53  ? 1002 A1BRB B O1   1 
HETATM 4338 O  O19  . A1BRB E 5 .   ? -15.780 -7.719  27.339  1.00 41.04  ? 1002 A1BRB B O19  1 
HETATM 4339 CL CL29 . A1BRB E 5 .   ? -17.871 -12.167 25.083  1.00 32.44  ? 1002 A1BRB B CL29 1 
HETATM 4340 O  O    . HOH   F 6 .   ? 11.591  -19.216 28.363  1.00 44.33  ? 1101 HOH   A O    1 
HETATM 4341 O  O    . HOH   F 6 .   ? -29.345 -5.055  54.996  1.00 61.20  ? 1102 HOH   A O    1 
HETATM 4342 O  O    . HOH   F 6 .   ? 5.036   -26.200 32.466  1.00 40.42  ? 1103 HOH   A O    1 
HETATM 4343 O  O    . HOH   F 6 .   ? -10.682 5.604   45.829  1.00 54.70  ? 1104 HOH   A O    1 
HETATM 4344 O  O    . HOH   F 6 .   ? 13.845  -5.300  24.278  1.00 65.18  ? 1105 HOH   A O    1 
HETATM 4345 O  O    . HOH   F 6 .   ? 17.594  -26.609 48.822  1.00 58.67  ? 1106 HOH   A O    1 
HETATM 4346 O  O    . HOH   F 6 .   ? -24.943 -2.321  52.713  1.00 61.96  ? 1107 HOH   A O    1 
HETATM 4347 O  O    . HOH   F 6 .   ? -4.617  -23.102 46.167  1.00 48.87  ? 1108 HOH   A O    1 
HETATM 4348 O  O    . HOH   F 6 .   ? 18.562  -10.084 34.304  1.00 85.57  ? 1109 HOH   A O    1 
HETATM 4349 O  O    . HOH   F 6 .   ? 2.620   -21.761 47.929  1.00 45.85  ? 1110 HOH   A O    1 
HETATM 4350 O  O    . HOH   F 6 .   ? -16.763 -33.124 51.206  1.00 64.77  ? 1111 HOH   A O    1 
HETATM 4351 O  O    . HOH   F 6 .   ? -19.272 -20.261 54.111  1.00 46.39  ? 1112 HOH   A O    1 
HETATM 4352 O  O    . HOH   F 6 .   ? 6.225   -15.328 47.924  1.00 52.38  ? 1113 HOH   A O    1 
HETATM 4353 O  O    . HOH   F 6 .   ? -25.166 -20.382 57.524  1.00 59.75  ? 1114 HOH   A O    1 
HETATM 4354 O  O    . HOH   F 6 .   ? -1.534  -14.149 50.093  1.00 52.83  ? 1115 HOH   A O    1 
HETATM 4355 O  O    . HOH   F 6 .   ? -21.840 0.329   44.270  1.00 46.65  ? 1116 HOH   A O    1 
HETATM 4356 O  O    . HOH   F 6 .   ? 4.890   -23.248 34.158  1.00 33.07  ? 1117 HOH   A O    1 
HETATM 4357 O  O    . HOH   F 6 .   ? 3.427   -6.687  17.362  1.00 43.14  ? 1118 HOH   A O    1 
HETATM 4358 O  O    . HOH   F 6 .   ? -15.715 -29.134 46.312  1.00 49.89  ? 1119 HOH   A O    1 
HETATM 4359 O  O    . HOH   F 6 .   ? -5.762  -24.060 53.013  1.00 56.39  ? 1120 HOH   A O    1 
HETATM 4360 O  O    . HOH   F 6 .   ? -16.940 -19.980 55.704  1.00 52.24  ? 1121 HOH   A O    1 
HETATM 4361 O  O    . HOH   F 6 .   ? -8.310  -20.142 27.923  1.00 39.69  ? 1122 HOH   A O    1 
HETATM 4362 O  O    . HOH   F 6 .   ? -14.778 -27.016 40.468  1.00 45.09  ? 1123 HOH   A O    1 
HETATM 4363 O  O    . HOH   F 6 .   ? -5.324  -20.679 47.563  1.00 47.34  ? 1124 HOH   A O    1 
HETATM 4364 O  O    . HOH   F 6 .   ? -4.218  -8.915  45.709  1.00 34.02  ? 1125 HOH   A O    1 
HETATM 4365 O  O    . HOH   F 6 .   ? -26.144 -21.930 55.237  1.00 55.84  ? 1126 HOH   A O    1 
HETATM 4366 O  O    . HOH   F 6 .   ? -13.683 -8.932  31.128  1.00 27.41  ? 1127 HOH   A O    1 
HETATM 4367 O  O    . HOH   F 6 .   ? 2.085   -0.588  41.470  1.00 38.11  ? 1128 HOH   A O    1 
HETATM 4368 O  O    . HOH   F 6 .   ? -2.766  -26.661 38.535  1.00 34.04  ? 1129 HOH   A O    1 
HETATM 4369 O  O    . HOH   F 6 .   ? -13.096 -10.821 36.551  1.00 33.69  ? 1130 HOH   A O    1 
HETATM 4370 O  O    . HOH   F 6 .   ? -7.715  -18.224 11.814  1.00 36.17  ? 1131 HOH   A O    1 
HETATM 4371 O  O    . HOH   F 6 .   ? -5.614  -20.050 50.480  1.00 44.87  ? 1132 HOH   A O    1 
HETATM 4372 O  O    . HOH   F 6 .   ? 13.801  -8.858  24.173  1.00 60.97  ? 1133 HOH   A O    1 
HETATM 4373 O  O    . HOH   F 6 .   ? -5.897  -19.760 44.162  1.00 42.02  ? 1134 HOH   A O    1 
HETATM 4374 O  O    . HOH   F 6 .   ? -5.275  -28.068 51.653  1.00 58.99  ? 1135 HOH   A O    1 
HETATM 4375 O  O    . HOH   F 6 .   ? -7.864  -24.061 22.629  1.00 35.36  ? 1136 HOH   A O    1 
HETATM 4376 O  O    . HOH   F 6 .   ? 12.434  -14.271 34.979  1.00 46.30  ? 1137 HOH   A O    1 
HETATM 4377 O  O    . HOH   F 6 .   ? 2.118   -5.904  54.805  1.00 61.55  ? 1138 HOH   A O    1 
HETATM 4378 O  O    . HOH   F 6 .   ? 1.709   -31.588 30.568  1.00 53.44  ? 1139 HOH   A O    1 
HETATM 4379 O  O    . HOH   F 6 .   ? -14.916 -20.687 34.941  1.00 42.47  ? 1140 HOH   A O    1 
HETATM 4380 O  O    . HOH   F 6 .   ? -3.786  -24.501 48.557  1.00 55.43  ? 1141 HOH   A O    1 
HETATM 4381 O  O    . HOH   F 6 .   ? -25.031 -15.763 41.400  1.00 42.74  ? 1142 HOH   A O    1 
HETATM 4382 O  O    . HOH   F 6 .   ? 8.933   -7.157  42.912  1.00 49.08  ? 1143 HOH   A O    1 
HETATM 4383 O  O    . HOH   F 6 .   ? -13.990 -4.242  36.858  1.00 35.00  ? 1144 HOH   A O    1 
HETATM 4384 O  O    . HOH   F 6 .   ? -2.182  -12.789 45.326  1.00 33.04  ? 1145 HOH   A O    1 
HETATM 4385 O  O    . HOH   F 6 .   ? 10.398  -28.390 37.193  1.00 44.59  ? 1146 HOH   A O    1 
HETATM 4386 O  O    . HOH   F 6 .   ? 8.498   -18.123 47.807  1.00 48.90  ? 1147 HOH   A O    1 
HETATM 4387 O  O    . HOH   F 6 .   ? -14.855 2.599   38.078  1.00 49.80  ? 1148 HOH   A O    1 
HETATM 4388 O  O    . HOH   F 6 .   ? -29.223 -15.933 43.584  1.00 44.09  ? 1149 HOH   A O    1 
HETATM 4389 O  O    . HOH   F 6 .   ? 3.574   -2.380  43.022  1.00 40.67  ? 1150 HOH   A O    1 
HETATM 4390 O  O    . HOH   F 6 .   ? -10.030 -14.637 22.384  1.00 28.82  ? 1151 HOH   A O    1 
HETATM 4391 O  O    . HOH   F 6 .   ? -0.750  -14.782 48.114  1.00 50.05  ? 1152 HOH   A O    1 
HETATM 4392 O  O    . HOH   F 6 .   ? 11.961  -25.014 33.802  1.00 46.22  ? 1153 HOH   A O    1 
HETATM 4393 O  O    . HOH   F 6 .   ? 9.189   -24.903 42.983  1.00 43.88  ? 1154 HOH   A O    1 
HETATM 4394 O  O    . HOH   F 6 .   ? 6.290   -8.034  51.822  1.00 61.93  ? 1155 HOH   A O    1 
HETATM 4395 O  O    . HOH   F 6 .   ? 3.467   -10.004 44.987  1.00 37.36  ? 1156 HOH   A O    1 
HETATM 4396 O  O    . HOH   F 6 .   ? -5.767  -7.082  44.142  1.00 31.22  ? 1157 HOH   A O    1 
HETATM 4397 O  O    . HOH   F 6 .   ? -16.425 -8.498  31.478  1.00 33.30  ? 1158 HOH   A O    1 
HETATM 4398 O  O    . HOH   F 6 .   ? -0.251  2.519   28.364  1.00 44.10  ? 1159 HOH   A O    1 
HETATM 4399 O  O    . HOH   F 6 .   ? 4.687   -23.094 27.090  1.00 38.41  ? 1160 HOH   A O    1 
HETATM 4400 O  O    . HOH   F 6 .   ? -7.053  -22.430 51.205  1.00 49.90  ? 1161 HOH   A O    1 
HETATM 4401 O  O    . HOH   F 6 .   ? 1.980   -13.678 16.670  1.00 44.60  ? 1162 HOH   A O    1 
HETATM 4402 O  O    . HOH   F 6 .   ? -24.594 -19.521 40.920  1.00 64.39  ? 1163 HOH   A O    1 
HETATM 4403 O  O    . HOH   F 6 .   ? -10.184 -17.117 17.815  1.00 35.58  ? 1164 HOH   A O    1 
HETATM 4404 O  O    . HOH   F 6 .   ? -1.551  -0.985  46.974  1.00 47.00  ? 1165 HOH   A O    1 
HETATM 4405 O  O    . HOH   F 6 .   ? -3.723  -15.350 46.342  1.00 42.97  ? 1166 HOH   A O    1 
HETATM 4406 O  O    . HOH   F 6 .   ? -1.952  -27.696 42.582  1.00 47.09  ? 1167 HOH   A O    1 
HETATM 4407 O  O    . HOH   F 6 .   ? -9.312  -21.253 13.190  1.00 37.25  ? 1168 HOH   A O    1 
HETATM 4408 O  O    . HOH   F 6 .   ? -22.730 -17.195 41.313  1.00 45.81  ? 1169 HOH   A O    1 
HETATM 4409 O  O    . HOH   F 6 .   ? -0.679  -10.934 46.124  1.00 36.79  ? 1170 HOH   A O    1 
HETATM 4410 O  O    . HOH   F 6 .   ? 0.068   -21.409 19.594  1.00 37.33  ? 1171 HOH   A O    1 
HETATM 4411 O  O    . HOH   F 6 .   ? -3.206  -18.138 44.848  1.00 43.62  ? 1172 HOH   A O    1 
HETATM 4412 O  O    . HOH   F 6 .   ? -27.925 -1.461  46.071  1.00 51.59  ? 1173 HOH   A O    1 
HETATM 4413 O  O    . HOH   F 6 .   ? -0.251  -30.489 36.199  1.00 49.93  ? 1174 HOH   A O    1 
HETATM 4414 O  O    . HOH   F 6 .   ? -15.933 -2.128  36.230  1.00 43.84  ? 1175 HOH   A O    1 
HETATM 4415 O  O    . HOH   F 6 .   ? -18.204 -26.331 43.610  1.00 49.38  ? 1176 HOH   A O    1 
HETATM 4416 O  O    . HOH   F 6 .   ? -1.116  -10.170 50.862  1.00 48.75  ? 1177 HOH   A O    1 
HETATM 4417 O  O    . HOH   F 6 .   ? -12.310 -21.904 34.092  1.00 45.31  ? 1178 HOH   A O    1 
HETATM 4418 O  O    . HOH   F 6 .   ? 2.360   -27.103 43.233  1.00 49.94  ? 1179 HOH   A O    1 
HETATM 4419 O  O    . HOH   F 6 .   ? -15.467 -6.078  32.486  1.00 40.99  ? 1180 HOH   A O    1 
HETATM 4420 O  O    . HOH   F 6 .   ? 1.690   -11.842 44.570  1.00 35.50  ? 1181 HOH   A O    1 
HETATM 4421 O  O    . HOH   F 6 .   ? -4.236  -21.871 15.119  1.00 35.30  ? 1182 HOH   A O    1 
HETATM 4422 O  O    . HOH   F 6 .   ? -4.835  -11.856 45.179  1.00 35.48  ? 1183 HOH   A O    1 
HETATM 4423 O  O    . HOH   F 6 .   ? -27.165 -4.655  46.006  1.00 48.25  ? 1184 HOH   A O    1 
HETATM 4424 O  O    . HOH   F 6 .   ? -9.731  -7.676  24.158  1.00 36.36  ? 1185 HOH   A O    1 
HETATM 4425 O  O    . HOH   F 6 .   ? -10.062 1.457   38.357  1.00 33.04  ? 1186 HOH   A O    1 
HETATM 4426 O  O    . HOH   F 6 .   ? -9.878  -22.330 23.633  1.00 37.42  ? 1187 HOH   A O    1 
HETATM 4427 O  O    . HOH   F 6 .   ? 11.653  -24.961 44.255  1.00 48.26  ? 1188 HOH   A O    1 
HETATM 4428 O  O    . HOH   F 6 .   ? 11.575  -27.771 33.340  1.00 49.46  ? 1189 HOH   A O    1 
HETATM 4429 O  O    . HOH   F 6 .   ? -34.064 -10.041 53.916  1.00 60.83  ? 1190 HOH   A O    1 
HETATM 4430 O  O    . HOH   F 6 .   ? -23.511 -5.197  56.967  1.00 58.49  ? 1191 HOH   A O    1 
HETATM 4431 O  O    . HOH   F 6 .   ? -14.349 -8.188  37.407  1.00 25.14  ? 1192 HOH   A O    1 
HETATM 4432 O  O    . HOH   F 6 .   ? 12.487  -26.764 37.651  1.00 46.12  ? 1193 HOH   A O    1 
HETATM 4433 O  O    . HOH   F 6 .   ? 2.046   -2.642  55.585  1.00 59.80  ? 1194 HOH   A O    1 
HETATM 4434 O  O    . HOH   F 6 .   ? 3.681   1.493   40.495  1.00 44.76  ? 1195 HOH   A O    1 
HETATM 4435 O  O    . HOH   F 6 .   ? -11.943 2.876   40.457  1.00 49.54  ? 1196 HOH   A O    1 
HETATM 4436 O  O    . HOH   F 6 .   ? -7.619  -2.336  25.466  1.00 46.52  ? 1197 HOH   A O    1 
HETATM 4437 O  O    . HOH   F 6 .   ? -11.553 -25.851 37.647  1.00 48.83  ? 1198 HOH   A O    1 
HETATM 4438 O  O    . HOH   F 6 .   ? -9.718  -1.650  37.662  1.00 38.70  ? 1199 HOH   A O    1 
HETATM 4439 O  O    . HOH   F 6 .   ? -26.495 -16.406 34.425  1.00 65.91  ? 1200 HOH   A O    1 
HETATM 4440 O  O    . HOH   F 6 .   ? -12.762 -31.764 46.171  1.00 55.00  ? 1201 HOH   A O    1 
HETATM 4441 O  O    . HOH   F 6 .   ? 14.600  -3.588  25.827  1.00 60.16  ? 1202 HOH   A O    1 
HETATM 4442 O  O    . HOH   F 6 .   ? -16.899 -25.666 40.869  1.00 55.75  ? 1203 HOH   A O    1 
HETATM 4443 O  O    . HOH   F 6 .   ? 14.443  -7.661  22.186  1.00 66.83  ? 1204 HOH   A O    1 
HETATM 4444 O  O    . HOH   F 6 .   ? 0.294   -29.108 37.952  1.00 53.59  ? 1205 HOH   A O    1 
HETATM 4445 O  O    . HOH   F 6 .   ? 10.865  -17.322 49.195  1.00 50.18  ? 1206 HOH   A O    1 
HETATM 4446 O  O    . HOH   F 6 .   ? -21.645 2.649   45.918  1.00 58.38  ? 1207 HOH   A O    1 
HETATM 4447 O  O    . HOH   F 6 .   ? -1.201  -19.859 49.044  1.00 49.59  ? 1208 HOH   A O    1 
HETATM 4448 O  O    . HOH   F 6 .   ? 2.875   -8.580  54.038  1.00 69.38  ? 1209 HOH   A O    1 
HETATM 4449 O  O    . HOH   F 6 .   ? -23.554 -4.305  59.072  1.00 71.89  ? 1210 HOH   A O    1 
HETATM 4450 O  O    . HOH   F 6 .   ? 0.325   -10.816 48.395  1.00 46.05  ? 1211 HOH   A O    1 
HETATM 4451 O  O    . HOH   F 6 .   ? -3.162  -20.671 50.650  1.00 53.02  ? 1212 HOH   A O    1 
HETATM 4452 O  O    . HOH   F 6 .   ? -14.136 -33.563 45.248  1.00 58.68  ? 1213 HOH   A O    1 
HETATM 4453 O  O    . HOH   F 6 .   ? 1.482   4.621   28.710  1.00 48.58  ? 1214 HOH   A O    1 
HETATM 4454 O  O    . HOH   F 6 .   ? -15.125 -35.098 43.386  1.00 71.28  ? 1215 HOH   A O    1 
HETATM 4455 O  O    . HOH   F 6 .   ? -16.223 -36.624 45.714  1.00 73.86  ? 1216 HOH   A O    1 
HETATM 4456 O  O    . HOH   G 6 .   ? -29.503 -14.671 -9.135  1.00 45.47  ? 1101 HOH   B O    1 
HETATM 4457 O  O    . HOH   G 6 .   ? -39.312 -11.235 12.715  1.00 49.96  ? 1102 HOH   B O    1 
HETATM 4458 O  O    . HOH   G 6 .   ? -45.066 3.820   6.001   1.00 61.44  ? 1103 HOH   B O    1 
HETATM 4459 O  O    . HOH   G 6 .   ? -17.668 -17.209 30.472  1.00 35.56  ? 1104 HOH   B O    1 
HETATM 4460 O  O    . HOH   G 6 .   ? -27.651 -9.674  -4.423  1.00 51.56  ? 1105 HOH   B O    1 
HETATM 4461 O  O    . HOH   G 6 .   ? -46.177 1.891   5.406   1.00 68.77  ? 1106 HOH   B O    1 
HETATM 4462 O  O    . HOH   G 6 .   ? -31.601 -26.265 1.270   1.00 50.71  ? 1107 HOH   B O    1 
HETATM 4463 O  O    . HOH   G 6 .   ? -15.327 -40.636 3.154   1.00 48.42  ? 1108 HOH   B O    1 
HETATM 4464 O  O    . HOH   G 6 .   ? -27.613 -2.301  -0.813  1.00 48.28  ? 1109 HOH   B O    1 
HETATM 4465 O  O    . HOH   G 6 .   ? -29.560 1.938   8.071   1.00 39.03  ? 1110 HOH   B O    1 
HETATM 4466 O  O    . HOH   G 6 .   ? -4.954  -19.676 13.898  1.00 37.08  ? 1111 HOH   B O    1 
HETATM 4467 O  O    . HOH   G 6 .   ? -23.866 1.892   3.546   1.00 48.82  ? 1112 HOH   B O    1 
HETATM 4468 O  O    . HOH   G 6 .   ? -8.986  -9.702  0.354   1.00 42.13  ? 1113 HOH   B O    1 
HETATM 4469 O  O    . HOH   G 6 .   ? -7.421  -21.955 11.453  1.00 51.19  ? 1114 HOH   B O    1 
HETATM 4470 O  O    . HOH   G 6 .   ? -13.282 1.231   10.250  1.00 39.93  ? 1115 HOH   B O    1 
HETATM 4471 O  O    . HOH   G 6 .   ? -17.594 7.364   22.615  1.00 53.86  ? 1116 HOH   B O    1 
HETATM 4472 O  O    . HOH   G 6 .   ? -14.140 -24.022 2.806   1.00 41.00  ? 1117 HOH   B O    1 
HETATM 4473 O  O    . HOH   G 6 .   ? -38.852 -9.010  17.848  1.00 50.52  ? 1118 HOH   B O    1 
HETATM 4474 O  O    . HOH   G 6 .   ? -29.968 -29.823 29.313  1.00 57.83  ? 1119 HOH   B O    1 
HETATM 4475 O  O    . HOH   G 6 .   ? -19.635 -30.508 6.523   1.00 33.71  ? 1120 HOH   B O    1 
HETATM 4476 O  O    . HOH   G 6 .   ? -17.658 -19.201 15.813  1.00 36.82  ? 1121 HOH   B O    1 
HETATM 4477 O  O    . HOH   G 6 .   ? -19.979 -41.846 5.897   1.00 43.23  ? 1122 HOH   B O    1 
HETATM 4478 O  O    . HOH   G 6 .   ? -12.016 -17.215 8.495   1.00 33.40  ? 1123 HOH   B O    1 
HETATM 4479 O  O    . HOH   G 6 .   ? -23.729 -5.568  -9.987  1.00 52.30  ? 1124 HOH   B O    1 
HETATM 4480 O  O    . HOH   G 6 .   ? -6.999  -29.767 5.662   1.00 32.71  ? 1125 HOH   B O    1 
HETATM 4481 O  O    . HOH   G 6 .   ? -25.116 -13.055 1.550   1.00 43.22  ? 1126 HOH   B O    1 
HETATM 4482 O  O    . HOH   G 6 .   ? -16.594 -27.374 1.896   1.00 36.36  ? 1127 HOH   B O    1 
HETATM 4483 O  O    . HOH   G 6 .   ? -32.340 -28.557 24.096  1.00 48.29  ? 1128 HOH   B O    1 
HETATM 4484 O  O    . HOH   G 6 .   ? -33.171 -23.867 3.810   1.00 45.50  ? 1129 HOH   B O    1 
HETATM 4485 O  O    . HOH   G 6 .   ? -26.695 -5.082  -0.133  1.00 35.72  ? 1130 HOH   B O    1 
HETATM 4486 O  O    . HOH   G 6 .   ? -6.136  -6.631  13.477  1.00 44.34  ? 1131 HOH   B O    1 
HETATM 4487 O  O    . HOH   G 6 .   ? -22.211 -34.367 26.273  1.00 50.31  ? 1132 HOH   B O    1 
HETATM 4488 O  O    . HOH   G 6 .   ? -20.381 -28.610 22.596  1.00 41.23  ? 1133 HOH   B O    1 
HETATM 4489 O  O    . HOH   G 6 .   ? -39.014 -4.860  2.600   1.00 47.52  ? 1134 HOH   B O    1 
HETATM 4490 O  O    . HOH   G 6 .   ? -11.017 -18.192 4.974   1.00 34.21  ? 1135 HOH   B O    1 
HETATM 4491 O  O    . HOH   G 6 .   ? -40.124 -6.375  16.343  1.00 58.31  ? 1136 HOH   B O    1 
HETATM 4492 O  O    . HOH   G 6 .   ? -9.968  -19.763 2.902   1.00 33.47  ? 1137 HOH   B O    1 
HETATM 4493 O  O    . HOH   G 6 .   ? -8.889  -3.605  6.677   1.00 39.94  ? 1138 HOH   B O    1 
HETATM 4494 O  O    . HOH   G 6 .   ? -28.597 -18.376 23.655  1.00 42.97  ? 1139 HOH   B O    1 
HETATM 4495 O  O    . HOH   G 6 .   ? -8.085  -9.434  16.601  1.00 36.51  ? 1140 HOH   B O    1 
HETATM 4496 O  O    . HOH   G 6 .   ? -18.196 -16.964 5.152   1.00 29.63  ? 1141 HOH   B O    1 
HETATM 4497 O  O    . HOH   G 6 .   ? -29.410 3.851   15.480  1.00 42.65  ? 1142 HOH   B O    1 
HETATM 4498 O  O    . HOH   G 6 .   ? -20.335 -18.282 6.604   1.00 32.49  ? 1143 HOH   B O    1 
HETATM 4499 O  O    . HOH   G 6 .   ? -28.685 -28.451 3.213   1.00 38.89  ? 1144 HOH   B O    1 
HETATM 4500 O  O    . HOH   G 6 .   ? -27.902 -37.047 17.213  1.00 39.96  ? 1145 HOH   B O    1 
HETATM 4501 O  O    . HOH   G 6 .   ? -3.436  -16.067 7.179   1.00 54.65  ? 1146 HOH   B O    1 
HETATM 4502 O  O    . HOH   G 6 .   ? -4.976  -13.852 -5.906  1.00 42.52  ? 1147 HOH   B O    1 
HETATM 4503 O  O    . HOH   G 6 .   ? -12.238 -40.619 4.024   1.00 45.67  ? 1148 HOH   B O    1 
HETATM 4504 O  O    . HOH   G 6 .   ? -11.161 -43.728 9.958   1.00 43.63  ? 1149 HOH   B O    1 
HETATM 4505 O  O    . HOH   G 6 .   ? -13.558 -18.531 6.234   1.00 32.61  ? 1150 HOH   B O    1 
HETATM 4506 O  O    . HOH   G 6 .   ? -27.624 -11.052 2.903   1.00 41.45  ? 1151 HOH   B O    1 
HETATM 4507 O  O    . HOH   G 6 .   ? -9.178  -36.027 11.488  1.00 34.67  ? 1152 HOH   B O    1 
HETATM 4508 O  O    . HOH   G 6 .   ? -8.553  -2.465  4.370   1.00 45.32  ? 1153 HOH   B O    1 
HETATM 4509 O  O    . HOH   G 6 .   ? -15.620 -15.226 -3.066  1.00 41.17  ? 1154 HOH   B O    1 
HETATM 4510 O  O    . HOH   G 6 .   ? -28.204 -19.279 11.512  1.00 44.17  ? 1155 HOH   B O    1 
HETATM 4511 O  O    . HOH   G 6 .   ? -3.441  -27.531 14.916  1.00 44.56  ? 1156 HOH   B O    1 
HETATM 4512 O  O    . HOH   G 6 .   ? -28.512 -33.962 5.480   1.00 49.69  ? 1157 HOH   B O    1 
HETATM 4513 O  O    . HOH   G 6 .   ? -22.515 -17.618 13.676  1.00 28.37  ? 1158 HOH   B O    1 
HETATM 4514 O  O    . HOH   G 6 .   ? -18.558 -16.143 2.568   1.00 34.52  ? 1159 HOH   B O    1 
HETATM 4515 O  O    . HOH   G 6 .   ? -16.973 -25.111 0.659   1.00 36.80  ? 1160 HOH   B O    1 
HETATM 4516 O  O    . HOH   G 6 .   ? -22.404 -18.310 23.968  1.00 36.57  ? 1161 HOH   B O    1 
HETATM 4517 O  O    . HOH   G 6 .   ? -17.965 -22.937 8.689   1.00 28.06  ? 1162 HOH   B O    1 
HETATM 4518 O  O    . HOH   G 6 .   ? -24.446 -5.442  -1.914  1.00 43.62  ? 1163 HOH   B O    1 
HETATM 4519 O  O    . HOH   G 6 .   ? -23.120 -43.876 8.195   1.00 46.20  ? 1164 HOH   B O    1 
HETATM 4520 O  O    . HOH   G 6 .   ? -11.821 -20.055 12.732  1.00 32.57  ? 1165 HOH   B O    1 
HETATM 4521 O  O    . HOH   G 6 .   ? -33.224 -4.712  17.457  1.00 42.00  ? 1166 HOH   B O    1 
HETATM 4522 O  O    . HOH   G 6 .   ? -17.342 -8.946  0.271   1.00 35.87  ? 1167 HOH   B O    1 
HETATM 4523 O  O    . HOH   G 6 .   ? -8.829  -20.391 -2.582  1.00 38.03  ? 1168 HOH   B O    1 
HETATM 4524 O  O    . HOH   G 6 .   ? -17.418 -42.370 13.008  1.00 42.33  ? 1169 HOH   B O    1 
HETATM 4525 O  O    . HOH   G 6 .   ? -16.150 -21.125 14.651  1.00 35.17  ? 1170 HOH   B O    1 
HETATM 4526 O  O    . HOH   G 6 .   ? -16.160 5.441   23.645  1.00 43.01  ? 1171 HOH   B O    1 
HETATM 4527 O  O    . HOH   G 6 .   ? -15.853 -3.311  31.678  1.00 35.58  ? 1172 HOH   B O    1 
HETATM 4528 O  O    . HOH   G 6 .   ? -34.578 -14.273 20.370  1.00 47.27  ? 1173 HOH   B O    1 
HETATM 4529 O  O    . HOH   G 6 .   ? -15.894 -21.034 -1.102  1.00 41.75  ? 1174 HOH   B O    1 
HETATM 4530 O  O    . HOH   G 6 .   ? -7.658  0.639   14.729  1.00 55.99  ? 1175 HOH   B O    1 
HETATM 4531 O  O    . HOH   G 6 .   ? -27.610 -20.742 8.199   1.00 39.91  ? 1176 HOH   B O    1 
HETATM 4532 O  O    . HOH   G 6 .   ? -26.450 -17.319 22.010  1.00 36.56  ? 1177 HOH   B O    1 
HETATM 4533 O  O    . HOH   G 6 .   ? -23.227 -20.080 8.263   1.00 31.65  ? 1178 HOH   B O    1 
HETATM 4534 O  O    . HOH   G 6 .   ? -34.992 0.383   4.769   1.00 41.38  ? 1179 HOH   B O    1 
HETATM 4535 O  O    . HOH   G 6 .   ? -9.905  -16.591 20.509  1.00 27.73  ? 1180 HOH   B O    1 
HETATM 4536 O  O    . HOH   G 6 .   ? -31.439 -11.757 4.686   1.00 40.87  ? 1181 HOH   B O    1 
HETATM 4537 O  O    . HOH   G 6 .   ? -24.225 -11.879 11.064  1.00 36.64  ? 1182 HOH   B O    1 
HETATM 4538 O  O    . HOH   G 6 .   ? -29.370 -30.922 4.391   1.00 43.16  ? 1183 HOH   B O    1 
HETATM 4539 O  O    . HOH   G 6 .   ? -31.005 -15.386 5.934   1.00 44.71  ? 1184 HOH   B O    1 
HETATM 4540 O  O    . HOH   G 6 .   ? -17.204 -18.386 -0.015  1.00 40.79  ? 1185 HOH   B O    1 
HETATM 4541 O  O    . HOH   G 6 .   ? -5.789  -23.715 13.776  1.00 40.93  ? 1186 HOH   B O    1 
HETATM 4542 O  O    . HOH   G 6 .   ? -22.384 -6.966  -0.764  1.00 41.26  ? 1187 HOH   B O    1 
HETATM 4543 O  O    . HOH   G 6 .   ? -28.090 6.186   11.572  1.00 43.60  ? 1188 HOH   B O    1 
HETATM 4544 O  O    . HOH   G 6 .   ? -13.304 -13.608 -2.924  1.00 37.21  ? 1189 HOH   B O    1 
HETATM 4545 O  O    . HOH   G 6 .   ? -5.856  -13.400 6.015   1.00 39.55  ? 1190 HOH   B O    1 
HETATM 4546 O  O    . HOH   G 6 .   ? -18.332 -22.527 -1.712  1.00 44.56  ? 1191 HOH   B O    1 
HETATM 4547 O  O    . HOH   G 6 .   ? -31.827 -14.709 -15.180 1.00 46.57  ? 1192 HOH   B O    1 
HETATM 4548 O  O    . HOH   G 6 .   ? -11.189 -19.656 27.467  1.00 34.43  ? 1193 HOH   B O    1 
HETATM 4549 O  O    . HOH   G 6 .   ? -11.809 -19.743 17.408  1.00 32.41  ? 1194 HOH   B O    1 
HETATM 4550 O  O    . HOH   G 6 .   ? -7.107  -18.316 -0.558  1.00 40.70  ? 1195 HOH   B O    1 
HETATM 4551 O  O    . HOH   G 6 .   ? -30.441 -27.408 29.698  1.00 64.15  ? 1196 HOH   B O    1 
HETATM 4552 O  O    . HOH   G 6 .   ? -14.151 -21.168 5.662   1.00 29.32  ? 1197 HOH   B O    1 
HETATM 4553 O  O    . HOH   G 6 .   ? -35.208 0.923   16.694  1.00 52.56  ? 1198 HOH   B O    1 
HETATM 4554 O  O    . HOH   G 6 .   ? -21.140 -19.898 1.491   1.00 40.66  ? 1199 HOH   B O    1 
HETATM 4555 O  O    . HOH   G 6 .   ? -30.118 -11.124 -5.812  1.00 37.51  ? 1200 HOH   B O    1 
HETATM 4556 O  O    . HOH   G 6 .   ? -31.674 -16.607 10.585  1.00 35.88  ? 1201 HOH   B O    1 
HETATM 4557 O  O    . HOH   G 6 .   ? -28.596 -11.824 5.017   1.00 33.13  ? 1202 HOH   B O    1 
HETATM 4558 O  O    . HOH   G 6 .   ? -23.437 3.733   2.327   1.00 56.62  ? 1203 HOH   B O    1 
HETATM 4559 O  O    . HOH   G 6 .   ? -30.797 -23.823 5.919   1.00 34.87  ? 1204 HOH   B O    1 
HETATM 4560 O  O    . HOH   G 6 .   ? -20.590 -20.974 8.059   1.00 32.63  ? 1205 HOH   B O    1 
HETATM 4561 O  O    . HOH   G 6 .   ? -32.959 -33.604 5.898   1.00 46.29  ? 1206 HOH   B O    1 
HETATM 4562 O  O    . HOH   G 6 .   ? -24.557 -24.275 24.111  1.00 47.04  ? 1207 HOH   B O    1 
HETATM 4563 O  O    . HOH   G 6 .   ? -21.059 -27.979 -0.205  1.00 47.68  ? 1208 HOH   B O    1 
HETATM 4564 O  O    . HOH   G 6 .   ? -12.241 -23.335 4.888   1.00 21.77  ? 1209 HOH   B O    1 
HETATM 4565 O  O    . HOH   G 6 .   ? -14.647 -11.530 -3.456  1.00 41.02  ? 1210 HOH   B O    1 
HETATM 4566 O  O    . HOH   G 6 .   ? -6.290  -19.979 10.689  1.00 45.03  ? 1211 HOH   B O    1 
HETATM 4567 O  O    . HOH   G 6 .   ? -14.739 -25.151 -0.765  1.00 45.72  ? 1212 HOH   B O    1 
HETATM 4568 O  O    . HOH   G 6 .   ? -25.445 -14.316 32.348  1.00 58.48  ? 1213 HOH   B O    1 
HETATM 4569 O  O    . HOH   G 6 .   ? -26.429 -35.004 4.893   1.00 52.95  ? 1214 HOH   B O    1 
HETATM 4570 O  O    . HOH   G 6 .   ? -23.364 -27.035 1.720   1.00 40.01  ? 1215 HOH   B O    1 
HETATM 4571 O  O    . HOH   G 6 .   ? -30.531 -17.141 8.718   1.00 48.65  ? 1216 HOH   B O    1 
HETATM 4572 O  O    . HOH   G 6 .   ? -19.372 -18.046 0.742   1.00 38.37  ? 1217 HOH   B O    1 
HETATM 4573 O  O    . HOH   G 6 .   ? -47.113 0.558   3.311   1.00 59.92  ? 1218 HOH   B O    1 
HETATM 4574 O  O    . HOH   G 6 .   ? -22.612 -4.771  -3.381  1.00 61.80  ? 1219 HOH   B O    1 
HETATM 4575 O  O    . HOH   G 6 .   ? -19.090 -25.508 -0.350  1.00 47.16  ? 1220 HOH   B O    1 
HETATM 4576 O  O    . HOH   G 6 .   ? -46.757 -0.185  6.907   1.00 70.73  ? 1221 HOH   B O    1 
HETATM 4577 O  O    . HOH   G 6 .   ? -28.580 -26.003 29.240  1.00 55.44  ? 1222 HOH   B O    1 
HETATM 4578 O  O    . HOH   G 6 .   ? -16.082 -10.030 -6.427  1.00 63.40  ? 1223 HOH   B O    1 
HETATM 4579 O  O    . HOH   G 6 .   ? -29.245 -13.202 -6.875  1.00 48.70  ? 1224 HOH   B O    1 
HETATM 4580 O  O    . HOH   G 6 .   ? -31.749 -22.629 2.099   1.00 57.36  ? 1225 HOH   B O    1 
HETATM 4581 O  O    . HOH   G 6 .   ? -14.770 -12.035 -6.227  1.00 56.93  ? 1226 HOH   B O    1 
HETATM 4582 O  O    . HOH   G 6 .   ? -31.865 -11.771 -3.594  1.00 42.47  ? 1227 HOH   B O    1 
HETATM 4583 O  O    . HOH   G 6 .   ? -49.282 0.213   3.651   1.00 68.34  ? 1228 HOH   B 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    . ARG   A 19  ? 0.6354 0.8043 0.8927 -0.1065 -0.0349 0.0127  397  ARG   A N    
2    C  CA   . ARG   A 19  ? 0.5742 0.7391 0.8275 -0.0959 -0.0396 0.0070  397  ARG   A CA   
3    C  C    . ARG   A 19  ? 0.5176 0.6529 0.7536 -0.0946 -0.0450 0.0034  397  ARG   A C    
4    O  O    . ARG   A 19  ? 0.5627 0.6869 0.7960 -0.1036 -0.0520 0.0030  397  ARG   A O    
5    C  CB   . ARG   A 19  ? 0.5402 0.7249 0.8076 -0.0990 -0.0463 0.0059  397  ARG   A CB   
6    C  CG   . ARG   A 19  ? 0.5121 0.6958 0.7764 -0.0876 -0.0510 0.0008  397  ARG   A CG   
7    C  CD   . ARG   A 19  ? 0.5800 0.7933 0.8614 -0.0839 -0.0515 0.0009  397  ARG   A CD   
8    N  NE   . ARG   A 19  ? 0.5867 0.8006 0.8683 -0.0799 -0.0604 -0.0029 397  ARG   A NE   
9    C  CZ   . ARG   A 19  ? 0.6174 0.8383 0.8998 -0.0676 -0.0609 -0.0054 397  ARG   A CZ   
10   N  NH1  . ARG   A 19  ? 0.5985 0.8258 0.8818 -0.0576 -0.0533 -0.0048 397  ARG   A NH1  
11   N  NH2  . ARG   A 19  ? 0.6535 0.8742 0.9352 -0.0652 -0.0698 -0.0084 397  ARG   A NH2  
12   N  N    . LEU   A 20  ? 0.4859 0.6089 0.7102 -0.0834 -0.0419 0.0007  398  LEU   A N    
13   C  CA   . LEU   A 20  ? 0.5031 0.5995 0.7105 -0.0813 -0.0449 -0.0023 398  LEU   A CA   
14   C  C    . LEU   A 20  ? 0.4797 0.5709 0.6820 -0.0761 -0.0524 -0.0074 398  LEU   A C    
15   O  O    . LEU   A 20  ? 0.5062 0.6087 0.7121 -0.0682 -0.0522 -0.0088 398  LEU   A O    
16   C  CB   . LEU   A 20  ? 0.4841 0.5704 0.6810 -0.0730 -0.0375 -0.0020 398  LEU   A CB   
17   C  CG   . LEU   A 20  ? 0.5178 0.6061 0.7165 -0.0773 -0.0300 0.0027  398  LEU   A CG   
18   C  CD1  . LEU   A 20  ? 0.5343 0.6057 0.7190 -0.0707 -0.0253 0.0022  398  LEU   A CD1  
19   C  CD2  . LEU   A 20  ? 0.5371 0.6227 0.7394 -0.0907 -0.0330 0.0062  398  LEU   A CD2  
20   N  N    . LYS   A 21  ? 0.4155 0.4892 0.6086 -0.0804 -0.0592 -0.0101 399  LYS   A N    
21   C  CA   . LYS   A 21  ? 0.4460 0.5117 0.6308 -0.0754 -0.0662 -0.0153 399  LYS   A CA   
22   C  C    . LYS   A 21  ? 0.4464 0.4963 0.6158 -0.0658 -0.0626 -0.0176 399  LYS   A C    
23   O  O    . LYS   A 21  ? 0.4235 0.4564 0.5829 -0.0669 -0.0613 -0.0180 399  LYS   A O    
24   C  CB   . LYS   A 21  ? 0.4868 0.5412 0.6684 -0.0842 -0.0754 -0.0179 399  LYS   A CB   
25   C  CG   . LYS   A 21  ? 0.5255 0.5970 0.7230 -0.0947 -0.0803 -0.0158 399  LYS   A CG   
26   C  CD   . LYS   A 21  ? 0.4614 0.5183 0.6544 -0.1048 -0.0900 -0.0182 399  LYS   A CD   
27   C  CE   . LYS   A 21  ? 0.6131 0.6873 0.8227 -0.1176 -0.0941 -0.0148 399  LYS   A CE   
28   N  NZ   . LYS   A 21  ? 0.6721 0.7492 0.8887 -0.1276 -0.0892 -0.0084 399  LYS   A NZ   
29   N  N    . ILE   A 22  ? 0.3891 0.4450 0.5568 -0.0564 -0.0610 -0.0186 400  ILE   A N    
30   C  CA   . ILE   A 22  ? 0.3962 0.4402 0.5504 -0.0477 -0.0575 -0.0201 400  ILE   A CA   
31   C  C    . ILE   A 22  ? 0.4316 0.4663 0.5750 -0.0447 -0.0643 -0.0247 400  ILE   A C    
32   O  O    . ILE   A 22  ? 0.4446 0.4878 0.5920 -0.0443 -0.0700 -0.0262 400  ILE   A O    
33   C  CB   . ILE   A 22  ? 0.3850 0.4396 0.5425 -0.0398 -0.0517 -0.0179 400  ILE   A CB   
34   C  CG1  . ILE   A 22  ? 0.4302 0.4976 0.5998 -0.0425 -0.0456 -0.0140 400  ILE   A CG1  
35   C  CG2  . ILE   A 22  ? 0.3896 0.4313 0.5335 -0.0330 -0.0472 -0.0184 400  ILE   A CG2  
36   C  CD1  . ILE   A 22  ? 0.4557 0.5133 0.6206 -0.0453 -0.0397 -0.0119 400  ILE   A CD1  
37   N  N    . VAL   A 23  ? 0.4003 0.4185 0.5297 -0.0421 -0.0640 -0.0272 401  VAL   A N    
38   C  CA   . VAL   A 23  ? 0.4102 0.4207 0.5277 -0.0377 -0.0692 -0.0318 401  VAL   A CA   
39   C  C    . VAL   A 23  ? 0.4053 0.4139 0.5140 -0.0291 -0.0637 -0.0310 401  VAL   A C    
40   O  O    . VAL   A 23  ? 0.3976 0.4026 0.5047 -0.0275 -0.0570 -0.0288 401  VAL   A O    
41   C  CB   . VAL   A 23  ? 0.4402 0.4341 0.5477 -0.0408 -0.0743 -0.0363 401  VAL   A CB   
42   C  CG1  . VAL   A 23  ? 0.4316 0.4127 0.5317 -0.0392 -0.0689 -0.0358 401  VAL   A CG1  
43   C  CG2  . VAL   A 23  ? 0.4583 0.4473 0.5541 -0.0360 -0.0802 -0.0415 401  VAL   A CG2  
44   N  N    . THR   A 24  ? 0.4211 0.4327 0.5245 -0.0241 -0.0667 -0.0325 402  THR   A N    
45   C  CA   . THR   A 24  ? 0.3881 0.3971 0.4817 -0.0170 -0.0625 -0.0316 402  THR   A CA   
46   C  C    . THR   A 24  ? 0.3830 0.3885 0.4649 -0.0137 -0.0679 -0.0353 402  THR   A C    
47   O  O    . THR   A 24  ? 0.3847 0.3871 0.4647 -0.0166 -0.0746 -0.0393 402  THR   A O    
48   C  CB   . THR   A 24  ? 0.3761 0.3954 0.4769 -0.0138 -0.0585 -0.0271 402  THR   A CB   
49   O  OG1  . THR   A 24  ? 0.3979 0.4129 0.4888 -0.0084 -0.0542 -0.0257 402  THR   A OG1  
50   C  CG2  . THR   A 24  ? 0.4246 0.4543 0.5312 -0.0128 -0.0642 -0.0269 402  THR   A CG2  
51   N  N    . ILE   A 25  ? 0.3920 0.3973 0.4650 -0.0080 -0.0651 -0.0340 403  ILE   A N    
52   C  CA   . ILE   A 25  ? 0.3711 0.3735 0.4310 -0.0045 -0.0689 -0.0370 403  ILE   A CA   
53   C  C    . ILE   A 25  ? 0.4124 0.4204 0.4686 0.0000  -0.0670 -0.0329 403  ILE   A C    
54   O  O    . ILE   A 25  ? 0.4080 0.4177 0.4678 0.0012  -0.0614 -0.0287 403  ILE   A O    
55   C  CB   . ILE   A 25  ? 0.3792 0.3715 0.4276 -0.0026 -0.0664 -0.0405 403  ILE   A CB   
56   C  CG1  . ILE   A 25  ? 0.3760 0.3660 0.4106 0.0010  -0.0707 -0.0449 403  ILE   A CG1  
57   C  CG2  . ILE   A 25  ? 0.3584 0.3504 0.4050 0.0001  -0.0583 -0.0368 403  ILE   A CG2  
58   C  CD1  . ILE   A 25  ? 0.3948 0.3760 0.4187 0.0039  -0.0687 -0.0493 403  ILE   A CD1  
59   N  N    . HIS   A 26  ? 0.3716 0.3816 0.4200 0.0022  -0.0722 -0.0341 404  HIS   A N    
60   C  CA   . HIS   A 26  ? 0.3861 0.3995 0.4285 0.0060  -0.0711 -0.0298 404  HIS   A CA   
61   C  C    . HIS   A 26  ? 0.4521 0.4614 0.4845 0.0083  -0.0646 -0.0283 404  HIS   A C    
62   O  O    . HIS   A 26  ? 0.4449 0.4503 0.4678 0.0093  -0.0640 -0.0322 404  HIS   A O    
63   C  CB   . HIS   A 26  ? 0.4752 0.4911 0.5097 0.0075  -0.0783 -0.0314 404  HIS   A CB   
64   C  CG   . HIS   A 26  ? 0.5442 0.5628 0.5718 0.0108  -0.0782 -0.0262 404  HIS   A CG   
65   N  ND1  . HIS   A 26  ? 0.5868 0.6051 0.5996 0.0130  -0.0803 -0.0265 404  HIS   A ND1  
66   C  CD2  . HIS   A 26  ? 0.5078 0.5286 0.5405 0.0123  -0.0765 -0.0206 404  HIS   A CD2  
67   C  CE1  . HIS   A 26  ? 0.6198 0.6398 0.6290 0.0149  -0.0801 -0.0205 404  HIS   A CE1  
68   N  NE2  . HIS   A 26  ? 0.5447 0.5653 0.5657 0.0147  -0.0781 -0.0171 404  HIS   A NE2  
69   N  N    . GLN   A 27  ? 0.4004 0.4108 0.4351 0.0093  -0.0599 -0.0230 405  GLN   A N    
70   C  CA   . GLN   A 27  ? 0.4300 0.4380 0.4562 0.0106  -0.0540 -0.0210 405  GLN   A CA   
71   C  C    . GLN   A 27  ? 0.4134 0.4220 0.4419 0.0111  -0.0508 -0.0148 405  GLN   A C    
72   O  O    . GLN   A 27  ? 0.3738 0.3809 0.4099 0.0103  -0.0465 -0.0134 405  GLN   A O    
73   C  CB   . GLN   A 27  ? 0.3752 0.3791 0.4031 0.0096  -0.0495 -0.0241 405  GLN   A CB   
74   C  CG   . GLN   A 27  ? 0.3955 0.3986 0.4138 0.0115  -0.0444 -0.0236 405  GLN   A CG   
75   C  CD   . GLN   A 27  ? 0.4653 0.4689 0.4713 0.0140  -0.0464 -0.0279 405  GLN   A CD   
76   O  OE1  . GLN   A 27  ? 0.5026 0.5085 0.5006 0.0160  -0.0424 -0.0275 405  GLN   A OE1  
77   N  NE2  . GLN   A 27  ? 0.4017 0.4042 0.4061 0.0141  -0.0526 -0.0324 405  GLN   A NE2  
78   N  N    . GLU   A 28  ? 0.4338 0.4435 0.4550 0.0125  -0.0532 -0.0111 406  GLU   A N    
79   C  CA   . GLU   A 28  ? 0.3974 0.4052 0.4191 0.0130  -0.0513 -0.0052 406  GLU   A CA   
80   C  C    . GLU   A 28  ? 0.4172 0.4228 0.4344 0.0117  -0.0447 -0.0032 406  GLU   A C    
81   O  O    . GLU   A 28  ? 0.4112 0.4184 0.4203 0.0115  -0.0427 -0.0048 406  GLU   A O    
82   C  CB   . GLU   A 28  ? 0.4213 0.4294 0.4343 0.0143  -0.0562 -0.0012 406  GLU   A CB   
83   C  CG   . GLU   A 28  ? 0.4919 0.5032 0.5093 0.0158  -0.0634 -0.0031 406  GLU   A CG   
84   C  CD   . GLU   A 28  ? 0.5449 0.5559 0.5534 0.0174  -0.0688 0.0014  406  GLU   A CD   
85   O  OE1  . GLU   A 28  ? 0.5566 0.5641 0.5553 0.0168  -0.0669 0.0064  406  GLU   A OE1  
86   O  OE2  . GLU   A 28  ? 0.6069 0.6211 0.6182 0.0190  -0.0752 0.0001  406  GLU   A OE2  
87   N  N    . PRO   A 29  ? 0.4003 0.4027 0.4228 0.0113  -0.0414 -0.0001 407  PRO   A N    
88   C  CA   . PRO   A 29  ? 0.4240 0.4247 0.4554 0.0127  -0.0431 0.0016  407  PRO   A CA   
89   C  C    . PRO   A 29  ? 0.4281 0.4308 0.4721 0.0125  -0.0410 -0.0019 407  PRO   A C    
90   O  O    . PRO   A 29  ? 0.3917 0.3944 0.4438 0.0139  -0.0408 -0.0010 407  PRO   A O    
91   C  CB   . PRO   A 29  ? 0.4507 0.4460 0.4778 0.0121  -0.0402 0.0066  407  PRO   A CB   
92   C  CG   . PRO   A 29  ? 0.3973 0.3933 0.4200 0.0096  -0.0346 0.0058  407  PRO   A CG   
93   C  CD   . PRO   A 29  ? 0.3986 0.3993 0.4169 0.0096  -0.0356 0.0020  407  PRO   A CD   
94   N  N    . PHE   A 30  ? 0.3953 0.3996 0.4408 0.0107  -0.0395 -0.0060 408  PHE   A N    
95   C  CA   . PHE   A 30  ? 0.3624 0.3682 0.4191 0.0095  -0.0375 -0.0084 408  PHE   A CA   
96   C  C    . PHE   A 30  ? 0.4192 0.4304 0.4848 0.0094  -0.0425 -0.0104 408  PHE   A C    
97   O  O    . PHE   A 30  ? 0.4080 0.4229 0.4845 0.0092  -0.0414 -0.0103 408  PHE   A O    
98   C  CB   . PHE   A 30  ? 0.3358 0.3393 0.3902 0.0075  -0.0345 -0.0115 408  PHE   A CB   
99   C  CG   . PHE   A 30  ? 0.3932 0.3936 0.4410 0.0076  -0.0293 -0.0096 408  PHE   A CG   
100  C  CD1  . PHE   A 30  ? 0.3879 0.3867 0.4406 0.0068  -0.0247 -0.0081 408  PHE   A CD1  
101  C  CD2  . PHE   A 30  ? 0.3817 0.3821 0.4184 0.0084  -0.0293 -0.0090 408  PHE   A CD2  
102  C  CE1  . PHE   A 30  ? 0.4259 0.4226 0.4728 0.0067  -0.0205 -0.0062 408  PHE   A CE1  
103  C  CE2  . PHE   A 30  ? 0.4085 0.4082 0.4403 0.0081  -0.0247 -0.0069 408  PHE   A CE2  
104  C  CZ   . PHE   A 30  ? 0.4210 0.4185 0.4580 0.0071  -0.0205 -0.0056 408  PHE   A CZ   
105  N  N    . VAL   A 31  ? 0.3501 0.3629 0.4115 0.0096  -0.0480 -0.0122 409  VAL   A N    
106  C  CA   . VAL   A 31  ? 0.3554 0.3743 0.4254 0.0091  -0.0535 -0.0140 409  VAL   A CA   
107  C  C    . VAL   A 31  ? 0.4104 0.4305 0.4729 0.0115  -0.0596 -0.0131 409  VAL   A C    
108  O  O    . VAL   A 31  ? 0.4115 0.4293 0.4637 0.0111  -0.0617 -0.0150 409  VAL   A O    
109  C  CB   . VAL   A 31  ? 0.3938 0.4131 0.4674 0.0052  -0.0551 -0.0185 409  VAL   A CB   
110  C  CG1  . VAL   A 31  ? 0.4251 0.4521 0.5080 0.0039  -0.0615 -0.0201 409  VAL   A CG1  
111  C  CG2  . VAL   A 31  ? 0.3722 0.3894 0.4518 0.0026  -0.0493 -0.0187 409  VAL   A CG2  
112  N  N    . TYR   A 32  ? 0.3616 0.3850 0.4286 0.0145  -0.0625 -0.0102 410  TYR   A N    
113  C  CA   . TYR   A 32  ? 0.3906 0.4161 0.4529 0.0169  -0.0695 -0.0091 410  TYR   A CA   
114  C  C    . TYR   A 32  ? 0.3943 0.4280 0.4662 0.0157  -0.0753 -0.0125 410  TYR   A C    
115  O  O    . TYR   A 32  ? 0.3723 0.4120 0.4576 0.0142  -0.0739 -0.0138 410  TYR   A O    
116  C  CB   . TYR   A 32  ? 0.3814 0.4054 0.4441 0.0212  -0.0706 -0.0043 410  TYR   A CB   
117  C  CG   . TYR   A 32  ? 0.4181 0.4332 0.4698 0.0216  -0.0665 -0.0002 410  TYR   A CG   
118  C  CD1  . TYR   A 32  ? 0.3432 0.3546 0.3973 0.0206  -0.0597 0.0003  410  TYR   A CD1  
119  C  CD2  . TYR   A 32  ? 0.4103 0.4210 0.4489 0.0225  -0.0698 0.0035  410  TYR   A CD2  
120  C  CE1  . TYR   A 32  ? 0.4107 0.4145 0.4550 0.0201  -0.0566 0.0042  410  TYR   A CE1  
121  C  CE2  . TYR   A 32  ? 0.4369 0.4402 0.4658 0.0217  -0.0664 0.0079  410  TYR   A CE2  
122  C  CZ   . TYR   A 32  ? 0.4327 0.4326 0.4647 0.0204  -0.0600 0.0081  410  TYR   A CZ   
123  O  OH   . TYR   A 32  ? 0.4314 0.4245 0.4542 0.0187  -0.0570 0.0125  410  TYR   A OH   
124  N  N    . VAL   A 33  ? 0.3615 0.3965 0.4265 0.0158  -0.0818 -0.0138 411  VAL   A N    
125  C  CA   . VAL   A 33  ? 0.4552 0.4982 0.5282 0.0143  -0.0886 -0.0170 411  VAL   A CA   
126  C  C    . VAL   A 33  ? 0.5189 0.5647 0.5871 0.0182  -0.0958 -0.0146 411  VAL   A C    
127  O  O    . VAL   A 33  ? 0.4916 0.5321 0.5450 0.0194  -0.0975 -0.0134 411  VAL   A O    
128  C  CB   . VAL   A 33  ? 0.5042 0.5448 0.5727 0.0099  -0.0904 -0.0223 411  VAL   A CB   
129  C  CG1  . VAL   A 33  ? 0.4875 0.5362 0.5648 0.0074  -0.0982 -0.0254 411  VAL   A CG1  
130  C  CG2  . VAL   A 33  ? 0.4237 0.4597 0.4957 0.0065  -0.0837 -0.0241 411  VAL   A CG2  
131  N  N    . LYS   A 34  ? 0.4114 0.4661 0.4918 0.0205  -0.1000 -0.0137 412  LYS   A N    
132  C  CA   . LYS   A 34  ? 0.4536 0.5114 0.5311 0.0251  -0.1074 -0.0111 412  LYS   A CA   
133  C  C    . LYS   A 34  ? 0.4734 0.5440 0.5638 0.0242  -0.1144 -0.0139 412  LYS   A C    
134  O  O    . LYS   A 34  ? 0.4504 0.5288 0.5552 0.0211  -0.1122 -0.0162 412  LYS   A O    
135  C  CB   . LYS   A 34  ? 0.4200 0.4753 0.4995 0.0310  -0.1057 -0.0061 412  LYS   A CB   
136  C  CG   . LYS   A 34  ? 0.4403 0.4828 0.5068 0.0313  -0.0996 -0.0025 412  LYS   A CG   
137  C  CD   . LYS   A 34  ? 0.4760 0.5121 0.5245 0.0302  -0.1023 -0.0009 412  LYS   A CD   
138  C  CE   . LYS   A 34  ? 0.5272 0.5528 0.5640 0.0294  -0.0960 0.0030  412  LYS   A CE   
139  N  NZ   . LYS   A 34  ? 0.6122 0.6338 0.6314 0.0280  -0.0978 0.0050  412  LYS   A NZ   
140  N  N    . PRO   A 35  ? 0.5236 0.5973 0.6090 0.0264  -0.1229 -0.0135 413  PRO   A N    
141  C  CA   . PRO   A 35  ? 0.4568 0.5444 0.5554 0.0257  -0.1304 -0.0158 413  PRO   A CA   
142  C  C    . PRO   A 35  ? 0.4978 0.5962 0.6133 0.0303  -0.1299 -0.0137 413  PRO   A C    
143  O  O    . PRO   A 35  ? 0.4513 0.5449 0.5647 0.0364  -0.1272 -0.0099 413  PRO   A O    
144  C  CB   . PRO   A 35  ? 0.5031 0.5897 0.5896 0.0286  -0.1394 -0.0147 413  PRO   A CB   
145  C  CG   . PRO   A 35  ? 0.5391 0.6118 0.6054 0.0281  -0.1359 -0.0134 413  PRO   A CG   
146  C  CD   . PRO   A 35  ? 0.4978 0.5632 0.5648 0.0289  -0.1262 -0.0107 413  PRO   A CD   
147  N  N    . THR   A 36  ? 0.4984 0.6118 0.6306 0.0274  -0.1327 -0.0164 414  THR   A N    
148  C  CA   . THR   A 36  ? 0.4843 0.6118 0.6334 0.0327  -0.1331 -0.0149 414  THR   A CA   
149  C  C    . THR   A 36  ? 0.5055 0.6363 0.6521 0.0406  -0.1418 -0.0123 414  THR   A C    
150  O  O    . THR   A 36  ? 0.5335 0.6597 0.6682 0.0403  -0.1486 -0.0122 414  THR   A O    
151  C  CB   . THR   A 36  ? 0.5059 0.6516 0.6742 0.0271  -0.1347 -0.0179 414  THR   A CB   
152  O  OG1  . THR   A 36  ? 0.4257 0.5778 0.5935 0.0240  -0.1445 -0.0200 414  THR   A OG1  
153  C  CG2  . THR   A 36  ? 0.5131 0.6546 0.6832 0.0184  -0.1273 -0.0201 414  THR   A CG2  
154  N  N    . LEU   A 37  ? 0.5110 0.6505 0.6690 0.0482  -0.1417 -0.0105 415  LEU   A N    
155  C  CA   . LEU   A 37  ? 0.5812 0.7270 0.7405 0.0563  -0.1509 -0.0085 415  LEU   A CA   
156  C  C    . LEU   A 37  ? 0.6198 0.7846 0.7915 0.0528  -0.1590 -0.0114 415  LEU   A C    
157  O  O    . LEU   A 37  ? 0.5989 0.7719 0.7795 0.0440  -0.1571 -0.0147 415  LEU   A O    
158  C  CB   . LEU   A 37  ? 0.5851 0.7354 0.7540 0.0661  -0.1487 -0.0066 415  LEU   A CB   
159  C  CG   . LEU   A 37  ? 0.6444 0.7734 0.7975 0.0713  -0.1449 -0.0028 415  LEU   A CG   
160  C  CD1  . LEU   A 37  ? 0.6366 0.7691 0.7984 0.0822  -0.1445 -0.0017 415  LEU   A CD1  
161  C  CD2  . LEU   A 37  ? 0.6939 0.8084 0.8272 0.0720  -0.1515 0.0007  415  LEU   A CD2  
162  N  N    . SER   A 38  ? 0.5854 0.7567 0.7576 0.0594  -0.1687 -0.0098 416  SER   A N    
163  C  CA   . SER   A 38  ? 0.6031 0.7928 0.7865 0.0562  -0.1776 -0.0124 416  SER   A CA   
164  C  C    . SER   A 38  ? 0.6214 0.8341 0.8293 0.0537  -0.1751 -0.0148 416  SER   A C    
165  O  O    . SER   A 38  ? 0.6483 0.8763 0.8667 0.0470  -0.1805 -0.0174 416  SER   A O    
166  C  CB   . SER   A 38  ? 0.5704 0.7643 0.7511 0.0653  -0.1885 -0.0098 416  SER   A CB   
167  N  N    . ASP   A 39  ? 0.5760 0.7923 0.7933 0.0587  -0.1672 -0.0139 417  ASP   A N    
168  C  CA   . ASP   A 39  ? 0.5810 0.8211 0.8215 0.0567  -0.1640 -0.0158 417  ASP   A CA   
169  C  C    . ASP   A 39  ? 0.5738 0.8109 0.8171 0.0467  -0.1539 -0.0173 417  ASP   A C    
170  O  O    . ASP   A 39  ? 0.5101 0.7643 0.7707 0.0453  -0.1487 -0.0180 417  ASP   A O    
171  C  CB   . ASP   A 39  ? 0.5900 0.8394 0.8404 0.0697  -0.1624 -0.0144 417  ASP   A CB   
172  C  CG   . ASP   A 39  ? 0.5962 0.8252 0.8347 0.0749  -0.1539 -0.0127 417  ASP   A CG   
173  O  OD1  . ASP   A 39  ? 0.6138 0.8205 0.8341 0.0699  -0.1512 -0.0117 417  ASP   A OD1  
174  O  OD2  . ASP   A 39  ? 0.6184 0.8539 0.8654 0.0841  -0.1503 -0.0126 417  ASP   A OD2  
175  N  N    . GLY   A 40  ? 0.5329 0.7489 0.7592 0.0400  -0.1510 -0.0177 418  GLY   A N    
176  C  CA   . GLY   A 40  ? 0.5203 0.7320 0.7480 0.0306  -0.1426 -0.0190 418  GLY   A CA   
177  C  C    . GLY   A 40  ? 0.5267 0.7284 0.7511 0.0343  -0.1319 -0.0175 418  GLY   A C    
178  O  O    . GLY   A 40  ? 0.4961 0.6918 0.7194 0.0268  -0.1247 -0.0183 418  GLY   A O    
179  N  N    . THR   A 41  ? 0.5112 0.7099 0.7332 0.0456  -0.1310 -0.0155 419  THR   A N    
180  C  CA   . THR   A 41  ? 0.4520 0.6405 0.6703 0.0494  -0.1216 -0.0143 419  THR   A CA   
181  C  C    . THR   A 41  ? 0.5122 0.6746 0.7081 0.0508  -0.1203 -0.0124 419  THR   A C    
182  O  O    . THR   A 41  ? 0.5135 0.6671 0.6971 0.0506  -0.1269 -0.0115 419  THR   A O    
183  C  CB   . THR   A 41  ? 0.5116 0.7114 0.7405 0.0611  -0.1211 -0.0137 419  THR   A CB   
184  O  OG1  . THR   A 41  ? 0.5280 0.7201 0.7480 0.0706  -0.1289 -0.0118 419  THR   A OG1  
185  C  CG2  . THR   A 41  ? 0.5604 0.7895 0.8121 0.0601  -0.1229 -0.0155 419  THR   A CG2  
186  N  N    . CYS   A 42  ? 0.4533 0.6047 0.6443 0.0519  -0.1117 -0.0116 420  CYS   A N    
187  C  CA   . CYS   A 42  ? 0.4447 0.5732 0.6162 0.0522  -0.1091 -0.0094 420  CYS   A CA   
188  C  C    . CYS   A 42  ? 0.5011 0.6209 0.6671 0.0628  -0.1100 -0.0067 420  CYS   A C    
189  O  O    . CYS   A 42  ? 0.5016 0.6286 0.6776 0.0689  -0.1068 -0.0074 420  CYS   A O    
190  C  CB   . CYS   A 42  ? 0.4655 0.5863 0.6343 0.0457  -0.0995 -0.0102 420  CYS   A CB   
191  S  SG   . CYS   A 42  ? 0.5367 0.6621 0.7087 0.0334  -0.0988 -0.0132 420  CYS   A SG   
192  N  N    . LYS   A 43  ? 0.4911 0.5950 0.6403 0.0648  -0.1143 -0.0037 421  LYS   A N    
193  C  CA   . LYS   A 43  ? 0.5530 0.6465 0.6954 0.0743  -0.1172 -0.0005 421  LYS   A CA   
194  C  C    . LYS   A 43  ? 0.5411 0.6250 0.6819 0.0766  -0.1091 -0.0003 421  LYS   A C    
195  O  O    . LYS   A 43  ? 0.5337 0.6106 0.6695 0.0698  -0.1019 -0.0007 421  LYS   A O    
196  C  CB   . LYS   A 43  ? 0.6087 0.6861 0.7318 0.0736  -0.1225 0.0036  421  LYS   A CB   
197  C  CG   . LYS   A 43  ? 0.6669 0.7384 0.7850 0.0835  -0.1308 0.0071  421  LYS   A CG   
198  C  CD   . LYS   A 43  ? 0.7169 0.7661 0.8189 0.0856  -0.1291 0.0116  421  LYS   A CD   
199  C  CE   . LYS   A 43  ? 0.8116 0.8482 0.8948 0.0789  -0.1307 0.0155  421  LYS   A CE   
200  N  NZ   . LYS   A 43  ? 0.8917 0.9075 0.9586 0.0808  -0.1314 0.0213  421  LYS   A NZ   
201  N  N    . GLU   A 44  ? 0.5617 0.6453 0.7065 0.0867  -0.1108 0.0001  422  GLU   A N    
202  C  CA   . GLU   A 44  ? 0.5924 0.6665 0.7353 0.0902  -0.1042 -0.0003 422  GLU   A CA   
203  C  C    . GLU   A 44  ? 0.6033 0.6527 0.7261 0.0886  -0.1043 0.0040  422  GLU   A C    
204  O  O    . GLU   A 44  ? 0.6194 0.6580 0.7322 0.0931  -0.1117 0.0076  422  GLU   A O    
205  C  CB   . GLU   A 44  ? 0.6646 0.7456 0.8172 0.1026  -0.1069 -0.0019 422  GLU   A CB   
206  C  CG   . GLU   A 44  ? 0.7563 0.8320 0.9100 0.1067  -0.0997 -0.0039 422  GLU   A CG   
207  C  CD   . GLU   A 44  ? 0.8652 0.9444 1.0254 0.1208  -0.1033 -0.0058 422  GLU   A CD   
208  O  OE1  . GLU   A 44  ? 0.8919 0.9821 1.0592 0.1273  -0.1109 -0.0059 422  GLU   A OE1  
209  O  OE2  . GLU   A 44  ? 0.9109 0.9819 1.0688 0.1258  -0.0989 -0.0075 422  GLU   A OE2  
210  N  N    . GLU   A 45  ? 0.6011 0.6420 0.7180 0.0819  -0.0965 0.0040  423  GLU   A N    
211  C  CA   . GLU   A 45  ? 0.5688 0.5887 0.6679 0.0788  -0.0957 0.0081  423  GLU   A CA   
212  C  C    . GLU   A 45  ? 0.5921 0.6044 0.6906 0.0789  -0.0882 0.0068  423  GLU   A C    
213  O  O    . GLU   A 45  ? 0.5502 0.5741 0.6609 0.0794  -0.0825 0.0028  423  GLU   A O    
214  C  CB   . GLU   A 45  ? 0.6221 0.6398 0.7121 0.0689  -0.0943 0.0096  423  GLU   A CB   
215  C  CG   . GLU   A 45  ? 0.6638 0.6841 0.7488 0.0685  -0.1022 0.0116  423  GLU   A CG   
216  C  CD   . GLU   A 45  ? 0.6857 0.7029 0.7599 0.0597  -0.1005 0.0126  423  GLU   A CD   
217  O  OE1  . GLU   A 45  ? 0.6317 0.6540 0.7099 0.0538  -0.0941 0.0095  423  GLU   A OE1  
218  O  OE2  . GLU   A 45  ? 0.7594 0.7692 0.8205 0.0592  -0.1057 0.0166  423  GLU   A OE2  
219  N  N    . PHE   A 46  ? 0.5898 0.5827 0.6734 0.0776  -0.0882 0.0106  424  PHE   A N    
220  C  CA   . PHE   A 46  ? 0.5847 0.5670 0.6650 0.0780  -0.0827 0.0100  424  PHE   A CA   
221  C  C    . PHE   A 46  ? 0.6463 0.6173 0.7140 0.0686  -0.0786 0.0131  424  PHE   A C    
222  O  O    . PHE   A 46  ? 0.6815 0.6451 0.7378 0.0647  -0.0823 0.0176  424  PHE   A O    
223  C  CB   . PHE   A 46  ? 0.6222 0.5904 0.6972 0.0872  -0.0880 0.0113  424  PHE   A CB   
224  C  CG   . PHE   A 46  ? 0.5284 0.5083 0.6158 0.0977  -0.0919 0.0078  424  PHE   A CG   
225  C  CD1  . PHE   A 46  ? 0.5929 0.5835 0.6925 0.1029  -0.0867 0.0025  424  PHE   A CD1  
226  C  CD2  . PHE   A 46  ? 0.6469 0.6299 0.7348 0.1024  -0.1004 0.0097  424  PHE   A CD2  
227  C  CE1  . PHE   A 46  ? 0.6450 0.6499 0.7576 0.1131  -0.0898 -0.0009 424  PHE   A CE1  
228  C  CE2  . PHE   A 46  ? 0.6501 0.6466 0.7511 0.1127  -0.1041 0.0064  424  PHE   A CE2  
229  C  CZ   . PHE   A 46  ? 0.6311 0.6393 0.7448 0.1181  -0.0986 0.0010  424  PHE   A CZ   
230  N  N    . THR   A 47  ? 0.5884 0.5591 0.6580 0.0653  -0.0710 0.0109  425  THR   A N    
231  C  CA   . THR   A 47  ? 0.6559 0.6187 0.7154 0.0567  -0.0666 0.0134  425  THR   A CA   
232  C  C    . THR   A 47  ? 0.7271 0.6703 0.7720 0.0563  -0.0701 0.0184  425  THR   A C    
233  O  O    . THR   A 47  ? 0.6948 0.6284 0.7363 0.0628  -0.0763 0.0200  425  THR   A O    
234  C  CB   . THR   A 47  ? 0.6514 0.6189 0.7169 0.0537  -0.0582 0.0099  425  THR   A CB   
235  O  OG1  . THR   A 47  ? 0.6637 0.6223 0.7283 0.0587  -0.0572 0.0087  425  THR   A OG1  
236  C  CG2  . THR   A 47  ? 0.6053 0.5913 0.6858 0.0540  -0.0551 0.0054  425  THR   A CG2  
237  N  N    . VAL   A 48  ? 0.7677 0.7045 0.8035 0.0484  -0.0663 0.0210  426  VAL   A N    
238  C  CA   . VAL   A 48  ? 0.8404 0.7593 0.8625 0.0461  -0.0691 0.0262  426  VAL   A CA   
239  C  C    . VAL   A 48  ? 0.7988 0.7066 0.8213 0.0510  -0.0689 0.0242  426  VAL   A C    
240  O  O    . VAL   A 48  ? 0.8339 0.7243 0.8459 0.0517  -0.0737 0.0280  426  VAL   A O    
241  C  CB   . VAL   A 48  ? 0.8443 0.7626 0.8583 0.0361  -0.0646 0.0294  426  VAL   A CB   
242  C  CG1  . VAL   A 48  ? 0.8981 0.8206 0.9054 0.0322  -0.0675 0.0333  426  VAL   A CG1  
243  C  CG2  . VAL   A 48  ? 0.7945 0.7245 0.8172 0.0334  -0.0565 0.0246  426  VAL   A CG2  
244  N  N    . ASN   A 49  ? 0.7436 0.6606 0.7772 0.0545  -0.0637 0.0184  427  ASN   A N    
245  C  CA   . ASN   A 49  ? 0.7146 0.6231 0.7489 0.0599  -0.0628 0.0153  427  ASN   A CA   
246  C  C    . ASN   A 49  ? 0.6911 0.5995 0.7311 0.0715  -0.0679 0.0124  427  ASN   A C    
247  O  O    . ASN   A 49  ? 0.6344 0.5351 0.6741 0.0778  -0.0680 0.0092  427  ASN   A O    
248  C  CB   . ASN   A 49  ? 0.7588 0.6785 0.8015 0.0578  -0.0542 0.0106  427  ASN   A CB   
249  C  CG   . ASN   A 49  ? 0.8428 0.7617 0.8797 0.0475  -0.0492 0.0130  427  ASN   A CG   
250  O  OD1  . ASN   A 49  ? 0.8422 0.7492 0.8676 0.0422  -0.0516 0.0178  427  ASN   A OD1  
251  N  ND2  . ASN   A 49  ? 0.7530 0.6852 0.7981 0.0446  -0.0425 0.0099  427  ASN   A ND2  
252  N  N    . GLY   A 50  ? 0.7047 0.6222 0.7499 0.0750  -0.0723 0.0130  428  GLY   A N    
253  C  CA   . GLY   A 50  ? 0.6261 0.5465 0.6780 0.0865  -0.0774 0.0102  428  GLY   A CA   
254  C  C    . GLY   A 50  ? 0.5786 0.5220 0.6481 0.0911  -0.0731 0.0044  428  GLY   A C    
255  O  O    . GLY   A 50  ? 0.5201 0.4701 0.5971 0.1008  -0.0774 0.0021  428  GLY   A O    
256  N  N    . ASP   A 51  ? 0.5719 0.5279 0.6481 0.0844  -0.0651 0.0023  429  ASP   A N    
257  C  CA   . ASP   A 51  ? 0.5608 0.5389 0.6533 0.0866  -0.0605 -0.0024 429  ASP   A CA   
258  C  C    . ASP   A 51  ? 0.5456 0.5386 0.6458 0.0839  -0.0632 -0.0015 429  ASP   A C    
259  O  O    . ASP   A 51  ? 0.5495 0.5370 0.6418 0.0778  -0.0660 0.0022  429  ASP   A O    
260  C  CB   . ASP   A 51  ? 0.6178 0.6008 0.7126 0.0797  -0.0515 -0.0043 429  ASP   A CB   
261  C  CG   . ASP   A 51  ? 0.6368 0.6042 0.7223 0.0807  -0.0490 -0.0049 429  ASP   A CG   
262  O  OD1  . ASP   A 51  ? 0.6178 0.5816 0.7042 0.0899  -0.0504 -0.0080 429  ASP   A OD1  
263  O  OD2  . ASP   A 51  ? 0.7046 0.6632 0.7816 0.0726  -0.0460 -0.0026 429  ASP   A OD2  
264  N  N    . PRO   A 52  ? 0.5383 0.5509 0.6536 0.0882  -0.0627 -0.0050 430  PRO   A N    
265  C  CA   . PRO   A 52  ? 0.5064 0.5330 0.6290 0.0851  -0.0661 -0.0043 430  PRO   A CA   
266  C  C    . PRO   A 52  ? 0.5331 0.5637 0.6553 0.0736  -0.0612 -0.0037 430  PRO   A C    
267  O  O    . PRO   A 52  ? 0.4891 0.5202 0.6122 0.0692  -0.0540 -0.0050 430  PRO   A O    
268  C  CB   . PRO   A 52  ? 0.5619 0.6098 0.7020 0.0919  -0.0657 -0.0083 430  PRO   A CB   
269  C  CG   . PRO   A 52  ? 0.5702 0.6182 0.7127 0.0961  -0.0591 -0.0115 430  PRO   A CG   
270  C  CD   . PRO   A 52  ? 0.5333 0.5561 0.6591 0.0972  -0.0602 -0.0095 430  PRO   A CD   
271  N  N    . VAL   A 53  ? 0.5260 0.5582 0.6455 0.0692  -0.0657 -0.0018 431  VAL   A N    
272  C  CA   . VAL   A 53  ? 0.4967 0.5325 0.6155 0.0594  -0.0623 -0.0019 431  VAL   A CA   
273  C  C    . VAL   A 53  ? 0.4587 0.5143 0.5935 0.0573  -0.0605 -0.0051 431  VAL   A C    
274  O  O    . VAL   A 53  ? 0.4872 0.5546 0.6306 0.0604  -0.0658 -0.0059 431  VAL   A O    
275  C  CB   . VAL   A 53  ? 0.4863 0.5155 0.5944 0.0559  -0.0678 0.0009  431  VAL   A CB   
276  C  CG1  . VAL   A 53  ? 0.4678 0.5023 0.5764 0.0471  -0.0650 -0.0005 431  VAL   A CG1  
277  C  CG2  . VAL   A 53  ? 0.5128 0.5235 0.6048 0.0558  -0.0688 0.0049  431  VAL   A CG2  
278  N  N    . LYS   A 54  ? 0.3925 0.4519 0.5313 0.0518  -0.0534 -0.0066 432  LYS   A N    
279  C  CA   . LYS   A 54  ? 0.4427 0.5199 0.5958 0.0479  -0.0515 -0.0088 432  LYS   A CA   
280  C  C    . LYS   A 54  ? 0.4315 0.5099 0.5829 0.0406  -0.0552 -0.0088 432  LYS   A C    
281  O  O    . LYS   A 54  ? 0.4776 0.5453 0.6189 0.0351  -0.0534 -0.0081 432  LYS   A O    
282  C  CB   . LYS   A 54  ? 0.4290 0.5081 0.5854 0.0441  -0.0430 -0.0098 432  LYS   A CB   
283  C  CG   . LYS   A 54  ? 0.5058 0.5883 0.6665 0.0514  -0.0392 -0.0110 432  LYS   A CG   
284  C  CD   . LYS   A 54  ? 0.5541 0.6343 0.7135 0.0475  -0.0310 -0.0114 432  LYS   A CD   
285  C  CE   . LYS   A 54  ? 0.5513 0.6125 0.6957 0.0439  -0.0293 -0.0097 432  LYS   A CE   
286  N  NZ   . LYS   A 54  ? 0.6726 0.7198 0.8058 0.0479  -0.0349 -0.0080 432  LYS   A NZ   
287  N  N    . LYS   A 55  ? 0.4183 0.5102 0.5794 0.0409  -0.0607 -0.0097 433  LYS   A N    
288  C  CA   . LYS   A 55  ? 0.3721 0.4656 0.5318 0.0346  -0.0654 -0.0103 433  LYS   A CA   
289  C  C    . LYS   A 55  ? 0.4427 0.5528 0.6173 0.0287  -0.0647 -0.0122 433  LYS   A C    
290  O  O    . LYS   A 55  ? 0.4389 0.5642 0.6272 0.0312  -0.0629 -0.0127 433  LYS   A O    
291  C  CB   . LYS   A 55  ? 0.3990 0.4923 0.5549 0.0391  -0.0741 -0.0095 433  LYS   A CB   
292  C  CG   . LYS   A 55  ? 0.4252 0.5015 0.5654 0.0441  -0.0755 -0.0066 433  LYS   A CG   
293  C  CD   . LYS   A 55  ? 0.4512 0.5267 0.5863 0.0478  -0.0845 -0.0051 433  LYS   A CD   
294  C  CE   . LYS   A 55  ? 0.4973 0.5554 0.6159 0.0512  -0.0860 -0.0013 433  LYS   A CE   
295  N  NZ   . LYS   A 55  ? 0.5307 0.5880 0.6433 0.0542  -0.0950 0.0007  433  LYS   A NZ   
296  N  N    . VAL   A 56  ? 0.4016 0.5086 0.5730 0.0206  -0.0662 -0.0133 434  VAL   A N    
297  C  CA   . VAL   A 56  ? 0.3962 0.5165 0.5802 0.0133  -0.0670 -0.0146 434  VAL   A CA   
298  C  C    . VAL   A 56  ? 0.4503 0.5708 0.6317 0.0098  -0.0755 -0.0161 434  VAL   A C    
299  O  O    . VAL   A 56  ? 0.4145 0.5217 0.5816 0.0108  -0.0785 -0.0164 434  VAL   A O    
300  C  CB   . VAL   A 56  ? 0.4361 0.5507 0.6189 0.0057  -0.0605 -0.0148 434  VAL   A CB   
301  C  CG1  . VAL   A 56  ? 0.4240 0.5380 0.6079 0.0094  -0.0523 -0.0134 434  VAL   A CG1  
302  C  CG2  . VAL   A 56  ? 0.4700 0.5667 0.6372 0.0025  -0.0614 -0.0156 434  VAL   A CG2  
303  N  N    . ILE   A 57  ? 0.3690 0.5057 0.5642 0.0058  -0.0795 -0.0171 435  ILE   A N    
304  C  CA   . ILE   A 57  ? 0.4187 0.5560 0.6122 0.0008  -0.0879 -0.0191 435  ILE   A CA   
305  C  C    . ILE   A 57  ? 0.4533 0.5778 0.6390 -0.0079 -0.0864 -0.0207 435  ILE   A C    
306  O  O    . ILE   A 57  ? 0.4818 0.6083 0.6738 -0.0138 -0.0813 -0.0202 435  ILE   A O    
307  C  CB   . ILE   A 57  ? 0.4353 0.5948 0.6470 -0.0018 -0.0928 -0.0194 435  ILE   A CB   
308  C  CG1  . ILE   A 57  ? 0.4639 0.6347 0.6815 0.0084  -0.0960 -0.0184 435  ILE   A CG1  
309  C  CG2  . ILE   A 57  ? 0.4919 0.6509 0.7019 -0.0092 -0.1013 -0.0219 435  ILE   A CG2  
310  C  CD1  . ILE   A 57  ? 0.5388 0.7000 0.7436 0.0134  -0.1034 -0.0186 435  ILE   A CD1  
311  N  N    . CYS   A 58  ? 0.4119 0.5231 0.5832 -0.0084 -0.0908 -0.0227 436  CYS   A N    
312  C  CA   . CYS   A 58  ? 0.4364 0.5351 0.5996 -0.0155 -0.0906 -0.0251 436  CYS   A CA   
313  C  C    . CYS   A 58  ? 0.5126 0.6103 0.6716 -0.0187 -0.1002 -0.0285 436  CYS   A C    
314  O  O    . CYS   A 58  ? 0.5180 0.6153 0.6698 -0.0135 -0.1052 -0.0289 436  CYS   A O    
315  C  CB   . CYS   A 58  ? 0.4591 0.5405 0.6062 -0.0122 -0.0852 -0.0250 436  CYS   A CB   
316  S  SG   . CYS   A 58  ? 0.5800 0.6551 0.7127 -0.0033 -0.0876 -0.0240 436  CYS   A SG   
317  N  N    . THR   A 59  ? 0.4623 0.5592 0.6252 -0.0276 -0.1032 -0.0308 437  THR   A N    
318  C  CA   . THR   A 59  ? 0.4495 0.5438 0.6077 -0.0315 -0.1128 -0.0348 437  THR   A CA   
319  C  C    . THR   A 59  ? 0.4973 0.5714 0.6363 -0.0309 -0.1131 -0.0384 437  THR   A C    
320  O  O    . THR   A 59  ? 0.4828 0.5459 0.6162 -0.0313 -0.1066 -0.0382 437  THR   A O    
321  C  CB   . THR   A 59  ? 0.4817 0.5844 0.6533 -0.0420 -0.1171 -0.0356 437  THR   A CB   
322  O  OG1  . THR   A 59  ? 0.4397 0.5338 0.6119 -0.0480 -0.1114 -0.0349 437  THR   A OG1  
323  C  CG2  . THR   A 59  ? 0.4876 0.6139 0.6788 -0.0421 -0.1177 -0.0324 437  THR   A CG2  
324  N  N    . GLY   A 60  ? 0.5605 0.6308 0.6892 -0.0294 -0.1207 -0.0419 438  GLY   A N    
325  C  CA   . GLY   A 60  ? 0.5688 0.6221 0.6795 -0.0286 -0.1219 -0.0463 438  GLY   A CA   
326  C  C    . GLY   A 60  ? 0.6465 0.6987 0.7466 -0.0266 -0.1308 -0.0501 438  GLY   A C    
327  O  O    . GLY   A 60  ? 0.5726 0.6371 0.6788 -0.0252 -0.1363 -0.0488 438  GLY   A O    
328  N  N    . PRO   A 61  ? 0.6734 0.7114 0.7572 -0.0258 -0.1327 -0.0552 439  PRO   A N    
329  C  CA   . PRO   A 61  ? 0.7578 0.7940 0.8290 -0.0234 -0.1409 -0.0593 439  PRO   A CA   
330  C  C    . PRO   A 61  ? 0.7843 0.8237 0.8458 -0.0150 -0.1383 -0.0560 439  PRO   A C    
331  O  O    . PRO   A 61  ? 0.7469 0.7866 0.8088 -0.0110 -0.1300 -0.0514 439  PRO   A O    
332  C  CB   . PRO   A 61  ? 0.7395 0.7587 0.7960 -0.0245 -0.1421 -0.0660 439  PRO   A CB   
333  C  CG   . PRO   A 61  ? 0.6964 0.7086 0.7530 -0.0230 -0.1320 -0.0637 439  PRO   A CG   
334  C  CD   . PRO   A 61  ? 0.6341 0.6570 0.7099 -0.0268 -0.1277 -0.0577 439  PRO   A CD   
335  N  N    . ASN   A 62  ? 0.9593 1.0005 1.0112 -0.0128 -0.1460 -0.0584 440  ASN   A N    
336  C  CA   . ASN   A 62  ? 0.9607 1.0036 1.0005 -0.0057 -0.1451 -0.0554 440  ASN   A CA   
337  C  C    . ASN   A 62  ? 0.9747 1.0063 0.9945 -0.0021 -0.1417 -0.0589 440  ASN   A C    
338  O  O    . ASN   A 62  ? 0.9800 1.0045 0.9896 -0.0033 -0.1467 -0.0657 440  ASN   A O    
339  C  CB   . ASN   A 62  ? 0.9688 1.0202 1.0075 -0.0050 -0.1553 -0.0559 440  ASN   A CB   
340  C  CG   . ASN   A 62  ? 0.9852 1.0503 1.0445 -0.0081 -0.1592 -0.0530 440  ASN   A CG   
341  O  OD1  . ASN   A 62  ? 0.9172 0.9900 0.9861 -0.0048 -0.1552 -0.0470 440  ASN   A OD1  
342  N  ND2  . ASN   A 62  ? 0.9353 1.0041 1.0014 -0.0143 -0.1675 -0.0573 440  ASN   A ND2  
343  N  N    . SER   A 68  ? 0.8752 0.8146 0.8054 -0.0069 -0.1862 -0.1273 446  SER   A N    
344  C  CA   . SER   A 68  ? 0.8892 0.8447 0.8323 -0.0117 -0.1898 -0.1208 446  SER   A CA   
345  C  C    . SER   A 68  ? 0.9075 0.8666 0.8741 -0.0214 -0.1898 -0.1149 446  SER   A C    
346  O  O    . SER   A 68  ? 0.8021 0.7567 0.7762 -0.0224 -0.1821 -0.1118 446  SER   A O    
347  C  CB   . SER   A 68  ? 0.8496 0.8198 0.7905 -0.0050 -0.1819 -0.1133 446  SER   A CB   
348  O  OG   . SER   A 68  ? 0.9476 0.9159 0.8866 0.0000  -0.1703 -0.1102 446  SER   A OG   
349  N  N    . PRO   A 69  ? 0.8478 0.8151 0.8252 -0.0287 -0.1987 -0.1140 447  PRO   A N    
350  C  CA   . PRO   A 69  ? 0.8115 0.7866 0.8121 -0.0377 -0.1982 -0.1078 447  PRO   A CA   
351  C  C    . PRO   A 69  ? 0.8531 0.8397 0.8654 -0.0345 -0.1863 -0.0985 447  PRO   A C    
352  O  O    . PRO   A 69  ? 0.8536 0.8475 0.8598 -0.0267 -0.1811 -0.0951 447  PRO   A O    
353  C  CB   . PRO   A 69  ? 0.8051 0.7938 0.8136 -0.0426 -0.2085 -0.1073 447  PRO   A CB   
354  C  CG   . PRO   A 69  ? 0.7959 0.7783 0.7823 -0.0371 -0.2161 -0.1151 447  PRO   A CG   
355  C  CD   . PRO   A 69  ? 0.8368 0.8007 0.8054 -0.0314 -0.2116 -0.1213 447  PRO   A CD   
356  N  N    . ARG   A 70  ? 0.9906 0.9789 1.0199 -0.0410 -0.1824 -0.0941 448  ARG   A N    
357  C  CA   . ARG   A 70  ? 0.9367 0.9365 0.9793 -0.0392 -0.1721 -0.0855 448  ARG   A CA   
358  C  C    . ARG   A 70  ? 0.9603 0.9780 1.0238 -0.0455 -0.1755 -0.0804 448  ARG   A C    
359  O  O    . ARG   A 70  ? 0.8615 0.8810 0.9392 -0.0540 -0.1756 -0.0786 448  ARG   A O    
360  C  CB   . ARG   A 70  ? 0.8685 0.8573 0.9130 -0.0406 -0.1640 -0.0844 448  ARG   A CB   
361  C  CG   . ARG   A 70  ? 0.8231 0.7964 0.8483 -0.0331 -0.1599 -0.0892 448  ARG   A CG   
362  C  CD   . ARG   A 70  ? 0.7709 0.7312 0.7975 -0.0353 -0.1546 -0.0893 448  ARG   A CD   
363  N  NE   . ARG   A 70  ? 0.8560 0.8019 0.8641 -0.0278 -0.1522 -0.0950 448  ARG   A NE   
364  C  CZ   . ARG   A 70  ? 0.8359 0.7669 0.8401 -0.0278 -0.1495 -0.0973 448  ARG   A CZ   
365  N  NH1  . ARG   A 70  ? 0.7869 0.7138 0.8036 -0.0357 -0.1487 -0.0939 448  ARG   A NH1  
366  N  NH2  . ARG   A 70  ? 0.7843 0.7046 0.7715 -0.0195 -0.1477 -0.1030 448  ARG   A NH2  
367  N  N    . HIS   A 71  ? 0.9443 0.9760 1.0094 -0.0413 -0.1782 -0.0778 449  HIS   A N    
368  C  CA   . HIS   A 71  ? 0.8653 0.9167 0.9503 -0.0448 -0.1808 -0.0727 449  HIS   A CA   
369  C  C    . HIS   A 71  ? 0.8047 0.8645 0.9013 -0.0414 -0.1697 -0.0654 449  HIS   A C    
370  O  O    . HIS   A 71  ? 0.7792 0.8397 0.8688 -0.0328 -0.1641 -0.0623 449  HIS   A O    
371  C  CB   . HIS   A 71  ? 0.7831 0.8450 0.8643 -0.0405 -0.1885 -0.0729 449  HIS   A CB   
372  N  N    . THR   A 72  ? 0.6796 0.7452 0.7931 -0.0483 -0.1666 -0.0626 450  THR   A N    
373  C  CA   . THR   A 72  ? 0.6922 0.7651 0.8163 -0.0454 -0.1561 -0.0563 450  THR   A CA   
374  C  C    . THR   A 72  ? 0.6552 0.7492 0.7938 -0.0420 -0.1569 -0.0516 450  THR   A C    
375  O  O    . THR   A 72  ? 0.6582 0.7660 0.8091 -0.0470 -0.1644 -0.0518 450  THR   A O    
376  C  CB   . THR   A 72  ? 0.6799 0.7502 0.8146 -0.0542 -0.1524 -0.0553 450  THR   A CB   
377  O  OG1  . THR   A 72  ? 0.6774 0.7621 0.8279 -0.0532 -0.1446 -0.0491 450  THR   A OG1  
378  C  CG2  . THR   A 72  ? 0.7812 0.8546 0.9239 -0.0652 -0.1622 -0.0581 450  THR   A CG2  
379  N  N    . VAL   A 73  ? 0.5658 0.6622 0.7026 -0.0333 -0.1499 -0.0475 451  VAL   A N    
380  C  CA   . VAL   A 73  ? 0.5994 0.7137 0.7488 -0.0283 -0.1504 -0.0431 451  VAL   A CA   
381  C  C    . VAL   A 73  ? 0.5534 0.6692 0.7079 -0.0233 -0.1396 -0.0384 451  VAL   A C    
382  O  O    . VAL   A 73  ? 0.5402 0.6419 0.6840 -0.0214 -0.1324 -0.0382 451  VAL   A O    
383  C  CB   . VAL   A 73  ? 0.6014 0.7163 0.7397 -0.0207 -0.1565 -0.0431 451  VAL   A CB   
384  C  CG1  . VAL   A 73  ? 0.6217 0.7383 0.7566 -0.0253 -0.1681 -0.0477 451  VAL   A CG1  
385  C  CG2  . VAL   A 73  ? 0.5901 0.6887 0.7084 -0.0144 -0.1513 -0.0428 451  VAL   A CG2  
386  N  N    . PRO   A 74  ? 0.4546 0.5880 0.6258 -0.0210 -0.1384 -0.0349 452  PRO   A N    
387  C  CA   . PRO   A 74  ? 0.5198 0.6543 0.6949 -0.0153 -0.1287 -0.0309 452  PRO   A CA   
388  C  C    . PRO   A 74  ? 0.4910 0.6153 0.6515 -0.0056 -0.1268 -0.0290 452  PRO   A C    
389  O  O    . PRO   A 74  ? 0.4830 0.6085 0.6372 -0.0011 -0.1336 -0.0289 452  PRO   A O    
390  C  CB   . PRO   A 74  ? 0.4815 0.6390 0.6778 -0.0145 -0.1297 -0.0287 452  PRO   A CB   
391  C  CG   . PRO   A 74  ? 0.5397 0.7079 0.7403 -0.0166 -0.1409 -0.0306 452  PRO   A CG   
392  C  CD   . PRO   A 74  ? 0.5069 0.6608 0.6951 -0.0241 -0.1456 -0.0348 452  PRO   A CD   
393  N  N    . GLN   A 75  ? 0.4801 0.5943 0.6348 -0.0032 -0.1178 -0.0272 453  GLN   A N    
394  C  CA   . GLN   A 75  ? 0.4612 0.5647 0.6021 0.0044  -0.1149 -0.0247 453  GLN   A CA   
395  C  C    . GLN   A 75  ? 0.4436 0.5470 0.5899 0.0079  -0.1059 -0.0216 453  GLN   A C    
396  O  O    . GLN   A 75  ? 0.4100 0.5215 0.5695 0.0046  -0.1017 -0.0216 453  GLN   A O    
397  C  CB   . GLN   A 75  ? 0.4647 0.5516 0.5866 0.0028  -0.1141 -0.0268 453  GLN   A CB   
398  C  CG   . GLN   A 75  ? 0.5176 0.6032 0.6322 -0.0004 -0.1228 -0.0309 453  GLN   A CG   
399  C  CD   . GLN   A 75  ? 0.5685 0.6390 0.6668 -0.0026 -0.1209 -0.0342 453  GLN   A CD   
400  O  OE1  . GLN   A 75  ? 0.5175 0.5796 0.6022 0.0017  -0.1173 -0.0327 453  GLN   A OE1  
401  N  NE2  . GLN   A 75  ? 0.6282 0.6957 0.7276 -0.0092 -0.1236 -0.0389 453  GLN   A NE2  
402  N  N    . CYS   A 76  ? 0.4105 0.5043 0.5457 0.0141  -0.1031 -0.0188 454  CYS   A N    
403  C  CA   . CYS   A 76  ? 0.4069 0.4986 0.5449 0.0183  -0.0956 -0.0160 454  CYS   A CA   
404  C  C    . CYS   A 76  ? 0.4210 0.4979 0.5468 0.0163  -0.0886 -0.0157 454  CYS   A C    
405  O  O    . CYS   A 76  ? 0.4371 0.5036 0.5479 0.0167  -0.0898 -0.0154 454  CYS   A O    
406  C  CB   . CYS   A 76  ? 0.4540 0.5451 0.5891 0.0269  -0.0985 -0.0127 454  CYS   A CB   
407  S  SG   . CYS   A 76  ? 0.5285 0.6388 0.6794 0.0310  -0.1066 -0.0131 454  CYS   A SG   
408  N  N    . CYS   A 77  ? 0.3901 0.4672 0.5224 0.0142  -0.0812 -0.0156 455  CYS   A N    
409  C  CA   . CYS   A 77  ? 0.3745 0.4393 0.4972 0.0124  -0.0743 -0.0153 455  CYS   A CA   
410  C  C    . CYS   A 77  ? 0.4012 0.4638 0.5254 0.0167  -0.0681 -0.0125 455  CYS   A C    
411  O  O    . CYS   A 77  ? 0.4145 0.4869 0.5512 0.0185  -0.0663 -0.0122 455  CYS   A O    
412  C  CB   . CYS   A 77  ? 0.3985 0.4633 0.5257 0.0051  -0.0713 -0.0178 455  CYS   A CB   
413  S  SG   . CYS   A 77  ? 0.6276 0.6866 0.7463 -0.0001 -0.0774 -0.0220 455  CYS   A SG   
414  N  N    . TYR   A 78  ? 0.3648 0.4154 0.4764 0.0181  -0.0647 -0.0107 456  TYR   A N    
415  C  CA   . TYR   A 78  ? 0.3739 0.4201 0.4850 0.0214  -0.0591 -0.0085 456  TYR   A CA   
416  C  C    . TYR   A 78  ? 0.4002 0.4341 0.4978 0.0196  -0.0550 -0.0073 456  TYR   A C    
417  O  O    . TYR   A 78  ? 0.3964 0.4262 0.4847 0.0173  -0.0569 -0.0080 456  TYR   A O    
418  C  CB   . TYR   A 78  ? 0.3747 0.4213 0.4863 0.0285  -0.0626 -0.0060 456  TYR   A CB   
419  C  CG   . TYR   A 78  ? 0.3904 0.4306 0.4901 0.0306  -0.0687 -0.0039 456  TYR   A CG   
420  C  CD1  . TYR   A 78  ? 0.4235 0.4707 0.5254 0.0311  -0.0761 -0.0048 456  TYR   A CD1  
421  C  CD2  . TYR   A 78  ? 0.4140 0.4417 0.5000 0.0314  -0.0674 -0.0005 456  TYR   A CD2  
422  C  CE1  . TYR   A 78  ? 0.4463 0.4880 0.5364 0.0330  -0.0818 -0.0025 456  TYR   A CE1  
423  C  CE2  . TYR   A 78  ? 0.4288 0.4513 0.5033 0.0327  -0.0729 0.0023  456  TYR   A CE2  
424  C  CZ   . TYR   A 78  ? 0.4786 0.5079 0.5548 0.0337  -0.0799 0.0013  456  TYR   A CZ   
425  O  OH   . TYR   A 78  ? 0.4944 0.5189 0.5584 0.0349  -0.0855 0.0043  456  TYR   A OH   
426  N  N    . GLY   A 79  ? 0.3600 0.3890 0.4566 0.0210  -0.0496 -0.0056 457  GLY   A N    
427  C  CA   . GLY   A 79  ? 0.3932 0.4120 0.4781 0.0194  -0.0457 -0.0040 457  GLY   A CA   
428  C  C    . GLY   A 79  ? 0.3614 0.3793 0.4500 0.0172  -0.0388 -0.0048 457  GLY   A C    
429  O  O    . GLY   A 79  ? 0.3768 0.4015 0.4764 0.0171  -0.0368 -0.0061 457  GLY   A O    
430  N  N    . PHE   A 80  ? 0.3619 0.3724 0.4412 0.0153  -0.0352 -0.0038 458  PHE   A N    
431  C  CA   . PHE   A 80  ? 0.3802 0.3885 0.4608 0.0134  -0.0290 -0.0041 458  PHE   A CA   
432  C  C    . PHE   A 80  ? 0.3714 0.3854 0.4611 0.0103  -0.0273 -0.0067 458  PHE   A C    
433  O  O    . PHE   A 80  ? 0.3495 0.3663 0.4461 0.0099  -0.0234 -0.0068 458  PHE   A O    
434  C  CB   . PHE   A 80  ? 0.4072 0.4090 0.4765 0.0115  -0.0267 -0.0030 458  PHE   A CB   
435  C  CG   . PHE   A 80  ? 0.4232 0.4219 0.4918 0.0099  -0.0209 -0.0026 458  PHE   A CG   
436  C  CD1  . PHE   A 80  ? 0.3911 0.3917 0.4644 0.0075  -0.0180 -0.0048 458  PHE   A CD1  
437  C  CD2  . PHE   A 80  ? 0.4613 0.4545 0.5230 0.0102  -0.0189 0.0002  458  PHE   A CD2  
438  C  CE1  . PHE   A 80  ? 0.4632 0.4608 0.5349 0.0063  -0.0131 -0.0043 458  PHE   A CE1  
439  C  CE2  . PHE   A 80  ? 0.4724 0.4633 0.5329 0.0086  -0.0141 0.0004  458  PHE   A CE2  
440  C  CZ   . PHE   A 80  ? 0.4539 0.4472 0.5192 0.0070  -0.0112 -0.0018 458  PHE   A CZ   
441  N  N    . CYS   A 81  ? 0.3827 0.3979 0.4717 0.0077  -0.0303 -0.0089 459  CYS   A N    
442  C  CA   . CYS   A 81  ? 0.3645 0.3828 0.4608 0.0037  -0.0293 -0.0110 459  CYS   A CA   
443  C  C    . CYS   A 81  ? 0.3589 0.3877 0.4684 0.0033  -0.0310 -0.0112 459  CYS   A C    
444  O  O    . CYS   A 81  ? 0.3374 0.3704 0.4548 0.0001  -0.0281 -0.0114 459  CYS   A O    
445  C  CB   . CYS   A 81  ? 0.3915 0.4062 0.4821 0.0012  -0.0328 -0.0138 459  CYS   A CB   
446  S  SG   . CYS   A 81  ? 0.5001 0.5053 0.5790 0.0010  -0.0286 -0.0144 459  CYS   A SG   
447  N  N    . ILE   A 82  ? 0.3498 0.3837 0.4619 0.0067  -0.0354 -0.0109 460  ILE   A N    
448  C  CA   . ILE   A 82  ? 0.3469 0.3931 0.4726 0.0071  -0.0369 -0.0112 460  ILE   A CA   
449  C  C    . ILE   A 82  ? 0.3905 0.4403 0.5215 0.0103  -0.0316 -0.0098 460  ILE   A C    
450  O  O    . ILE   A 82  ? 0.3151 0.3750 0.4571 0.0086  -0.0291 -0.0101 460  ILE   A O    
451  C  CB   . ILE   A 82  ? 0.3348 0.3859 0.4617 0.0104  -0.0438 -0.0114 460  ILE   A CB   
452  C  CG1  . ILE   A 82  ? 0.3915 0.4395 0.5126 0.0070  -0.0491 -0.0133 460  ILE   A CG1  
453  C  CG2  . ILE   A 82  ? 0.4016 0.4680 0.5438 0.0113  -0.0454 -0.0117 460  ILE   A CG2  
454  C  CD1  . ILE   A 82  ? 0.3801 0.4327 0.5087 0.0003  -0.0502 -0.0155 460  ILE   A CD1  
455  N  N    . ASP   A 83  ? 0.3864 0.4281 0.5093 0.0148  -0.0299 -0.0084 461  ASP   A N    
456  C  CA   . ASP   A 83  ? 0.4064 0.4487 0.5319 0.0179  -0.0248 -0.0078 461  ASP   A CA   
457  C  C    . ASP   A 83  ? 0.3511 0.3938 0.4786 0.0131  -0.0188 -0.0079 461  ASP   A C    
458  O  O    . ASP   A 83  ? 0.3569 0.4074 0.4922 0.0138  -0.0149 -0.0081 461  ASP   A O    
459  C  CB   . ASP   A 83  ? 0.3981 0.4285 0.5124 0.0217  -0.0246 -0.0061 461  ASP   A CB   
460  C  CG   . ASP   A 83  ? 0.4402 0.4703 0.5542 0.0281  -0.0296 -0.0054 461  ASP   A CG   
461  O  OD1  . ASP   A 83  ? 0.4358 0.4760 0.5585 0.0301  -0.0334 -0.0064 461  ASP   A OD1  
462  O  OD2  . ASP   A 83  ? 0.4280 0.4472 0.5326 0.0308  -0.0303 -0.0036 461  ASP   A OD2  
463  N  N    . LEU   A 84  ? 0.3559 0.3905 0.4759 0.0088  -0.0179 -0.0078 462  LEU   A N    
464  C  CA   . LEU   A 84  ? 0.3644 0.3981 0.4855 0.0044  -0.0130 -0.0077 462  LEU   A CA   
465  C  C    . LEU   A 84  ? 0.3694 0.4136 0.5019 -0.0001 -0.0131 -0.0081 462  LEU   A C    
466  O  O    . LEU   A 84  ? 0.3715 0.4209 0.5093 -0.0019 -0.0085 -0.0072 462  LEU   A O    
467  C  CB   . LEU   A 84  ? 0.3202 0.3434 0.4312 0.0016  -0.0129 -0.0078 462  LEU   A CB   
468  C  CG   . LEU   A 84  ? 0.3542 0.3743 0.4646 -0.0023 -0.0083 -0.0073 462  LEU   A CG   
469  C  CD1  . LEU   A 84  ? 0.4031 0.4237 0.5135 -0.0001 -0.0030 -0.0060 462  LEU   A CD1  
470  C  CD2  . LEU   A 84  ? 0.3419 0.3519 0.4421 -0.0035 -0.0086 -0.0079 462  LEU   A CD2  
471  N  N    . LEU   A 85  ? 0.3806 0.4285 0.5166 -0.0023 -0.0186 -0.0092 463  LEU   A N    
472  C  CA   . LEU   A 85  ? 0.3418 0.4005 0.4893 -0.0077 -0.0196 -0.0093 463  LEU   A CA   
473  C  C    . LEU   A 85  ? 0.4017 0.4753 0.5608 -0.0050 -0.0169 -0.0085 463  LEU   A C    
474  O  O    . LEU   A 85  ? 0.3629 0.4452 0.5299 -0.0093 -0.0133 -0.0073 463  LEU   A O    
475  C  CB   . LEU   A 85  ? 0.3312 0.3914 0.4801 -0.0098 -0.0269 -0.0110 463  LEU   A CB   
476  C  CG   . LEU   A 85  ? 0.3542 0.4280 0.5166 -0.0155 -0.0294 -0.0109 463  LEU   A CG   
477  C  CD1  . LEU   A 85  ? 0.3709 0.4406 0.5339 -0.0236 -0.0272 -0.0100 463  LEU   A CD1  
478  C  CD2  . LEU   A 85  ? 0.2954 0.3720 0.4594 -0.0162 -0.0374 -0.0129 463  LEU   A CD2  
479  N  N    . ILE   A 86  ? 0.3581 0.4351 0.5179 0.0023  -0.0186 -0.0091 464  ILE   A N    
480  C  CA   . ILE   A 86  ? 0.4098 0.5016 0.5805 0.0065  -0.0164 -0.0091 464  ILE   A CA   
481  C  C    . ILE   A 86  ? 0.4281 0.5199 0.5979 0.0072  -0.0089 -0.0084 464  ILE   A C    
482  O  O    . ILE   A 86  ? 0.4002 0.5062 0.5801 0.0058  -0.0051 -0.0079 464  ILE   A O    
483  C  CB   . ILE   A 86  ? 0.3684 0.4601 0.5377 0.0153  -0.0204 -0.0100 464  ILE   A CB   
484  C  CG1  . ILE   A 86  ? 0.4079 0.5039 0.5804 0.0144  -0.0281 -0.0107 464  ILE   A CG1  
485  C  CG2  . ILE   A 86  ? 0.4832 0.5878 0.6615 0.0219  -0.0175 -0.0108 464  ILE   A CG2  
486  C  CD1  . ILE   A 86  ? 0.3926 0.4844 0.5603 0.0224  -0.0333 -0.0108 464  ILE   A CD1  
487  N  N    . LYS   A 87  ? 0.4003 0.4772 0.5580 0.0087  -0.0066 -0.0081 465  LYS   A N    
488  C  CA   . LYS   A 87  ? 0.4187 0.4936 0.5736 0.0090  0.0001  -0.0074 465  LYS   A CA   
489  C  C    . LYS   A 87  ? 0.4449 0.5246 0.6041 0.0010  0.0036  -0.0058 465  LYS   A C    
490  O  O    . LYS   A 87  ? 0.5056 0.5956 0.6707 0.0006  0.0086  -0.0051 465  LYS   A O    
491  C  CB   . LYS   A 87  ? 0.4348 0.4926 0.5758 0.0106  0.0008  -0.0072 465  LYS   A CB   
492  C  CG   . LYS   A 87  ? 0.4244 0.4789 0.5611 0.0115  0.0068  -0.0068 465  LYS   A CG   
493  C  CD   . LYS   A 87  ? 0.5282 0.5911 0.6698 0.0185  0.0088  -0.0084 465  LYS   A CD   
494  C  CE   . LYS   A 87  ? 0.5151 0.5719 0.6496 0.0210  0.0136  -0.0088 465  LYS   A CE   
495  N  NZ   . LYS   A 87  ? 0.5880 0.6503 0.7252 0.0295  0.0143  -0.0113 465  LYS   A NZ   
496  N  N    . LEU   A 88  ? 0.4346 0.5064 0.5901 -0.0052 0.0009  -0.0051 466  LEU   A N    
497  C  CA   . LEU   A 88  ? 0.4303 0.5038 0.5888 -0.0133 0.0031  -0.0032 466  LEU   A CA   
498  C  C    . LEU   A 88  ? 0.4816 0.5735 0.6543 -0.0171 0.0033  -0.0022 466  LEU   A C    
499  O  O    . LEU   A 88  ? 0.4770 0.5763 0.6542 -0.0215 0.0079  0.0001  466  LEU   A O    
500  C  CB   . LEU   A 88  ? 0.3978 0.4590 0.5500 -0.0182 -0.0014 -0.0035 466  LEU   A CB   
501  C  CG   . LEU   A 88  ? 0.4473 0.4922 0.5860 -0.0158 -0.0010 -0.0041 466  LEU   A CG   
502  C  CD1  . LEU   A 88  ? 0.4056 0.4409 0.5393 -0.0194 -0.0061 -0.0053 466  LEU   A CD1  
503  C  CD2  . LEU   A 88  ? 0.4307 0.4716 0.5653 -0.0170 0.0048  -0.0022 466  LEU   A CD2  
504  N  N    . ALA   A 89  ? 0.4385 0.5389 0.6185 -0.0158 -0.0019 -0.0036 467  ALA   A N    
505  C  CA   . ALA   A 89  ? 0.4555 0.5756 0.6502 -0.0198 -0.0023 -0.0027 467  ALA   A CA   
506  C  C    . ALA   A 89  ? 0.5053 0.6412 0.7073 -0.0148 0.0038  -0.0024 467  ALA   A C    
507  O  O    . ALA   A 89  ? 0.4875 0.6381 0.6986 -0.0202 0.0075  -0.0002 467  ALA   A O    
508  C  CB   . ALA   A 89  ? 0.4588 0.5851 0.6593 -0.0182 -0.0095 -0.0045 467  ALA   A CB   
509  N  N    . ARG   A 90  ? 0.4507 0.5838 0.6483 -0.0048 0.0048  -0.0046 468  ARG   A N    
510  C  CA   . ARG   A 90  ? 0.4869 0.6335 0.6900 0.0016  0.0103  -0.0054 468  ARG   A CA   
511  C  C    . ARG   A 90  ? 0.5261 0.6703 0.7244 -0.0017 0.0175  -0.0036 468  ARG   A C    
512  O  O    . ARG   A 90  ? 0.5695 0.7306 0.7757 -0.0021 0.0227  -0.0028 468  ARG   A O    
513  C  CB   . ARG   A 90  ? 0.5333 0.6728 0.7304 0.0131  0.0086  -0.0084 468  ARG   A CB   
514  C  CG   . ARG   A 90  ? 0.5887 0.7331 0.7850 0.0207  0.0144  -0.0101 468  ARG   A CG   
515  C  CD   . ARG   A 90  ? 0.6606 0.7954 0.8504 0.0319  0.0112  -0.0131 468  ARG   A CD   
516  N  NE   . ARG   A 90  ? 0.7472 0.8602 0.9243 0.0307  0.0069  -0.0124 468  ARG   A NE   
517  C  CZ   . ARG   A 90  ? 0.7745 0.8795 0.9478 0.0359  0.0008  -0.0132 468  ARG   A CZ   
518  N  NH1  . ARG   A 90  ? 0.7945 0.9098 0.9755 0.0433  -0.0025 -0.0150 468  ARG   A NH1  
519  N  NH2  . ARG   A 90  ? 0.5557 0.6426 0.7173 0.0336  -0.0022 -0.0121 468  ARG   A NH2  
520  N  N    . THR   A 91  ? 0.4942 0.6190 0.6798 -0.0042 0.0179  -0.0027 469  THR   A N    
521  C  CA   . THR   A 91  ? 0.5484 0.6695 0.7280 -0.0061 0.0243  -0.0011 469  THR   A CA   
522  C  C    . THR   A 91  ? 0.5976 0.7232 0.7809 -0.0169 0.0263  0.0029  469  THR   A C    
523  O  O    . THR   A 91  ? 0.6622 0.7928 0.8445 -0.0188 0.0323  0.0048  469  THR   A O    
524  C  CB   . THR   A 91  ? 0.5512 0.6509 0.7160 -0.0037 0.0237  -0.0018 469  THR   A CB   
525  O  OG1  . THR   A 91  ? 0.7672 0.8650 0.9262 -0.0030 0.0297  -0.0011 469  THR   A OG1  
526  C  CG2  . THR   A 91  ? 0.5831 0.6695 0.7423 -0.0105 0.0201  -0.0002 469  THR   A CG2  
527  N  N    . MET   A 92  ? 0.5281 0.6518 0.7149 -0.0241 0.0213  0.0042  470  MET   A N    
528  C  CA   . MET   A 92  ? 0.5375 0.6633 0.7273 -0.0350 0.0221  0.0082  470  MET   A CA   
529  C  C    . MET   A 92  ? 0.5435 0.6901 0.7485 -0.0407 0.0210  0.0098  470  MET   A C    
530  O  O    . MET   A 92  ? 0.5780 0.7276 0.7865 -0.0511 0.0212  0.0138  470  MET   A O    
531  C  CB   . MET   A 92  ? 0.5634 0.6688 0.7444 -0.0400 0.0168  0.0086  470  MET   A CB   
532  C  CG   . MET   A 92  ? 0.5789 0.6658 0.7456 -0.0356 0.0183  0.0077  470  MET   A CG   
533  S  SD   . MET   A 92  ? 0.6364 0.7024 0.7937 -0.0384 0.0115  0.0065  470  MET   A SD   
534  C  CE   . MET   A 92  ? 0.5482 0.6152 0.7105 -0.0507 0.0100  0.0106  470  MET   A CE   
535  N  N    . ASN   A 93  ? 0.5226 0.6834 0.7366 -0.0345 0.0192  0.0071  471  ASN   A N    
536  C  CA   . ASN   A 93  ? 0.5653 0.7501 0.7954 -0.0387 0.0185  0.0083  471  ASN   A CA   
537  C  C    . ASN   A 93  ? 0.5498 0.7319 0.7841 -0.0492 0.0117  0.0100  471  ASN   A C    
538  O  O    . ASN   A 93  ? 0.5743 0.7671 0.8163 -0.0597 0.0126  0.0141  471  ASN   A O    
539  C  CB   . ASN   A 93  ? 0.5995 0.8023 0.8360 -0.0426 0.0263  0.0118  471  ASN   A CB   
540  C  CG   . ASN   A 93  ? 0.7018 0.9339 0.9542 -0.0390 0.0283  0.0110  471  ASN   A CG   
541  O  OD1  . ASN   A 93  ? 0.7401 0.9815 1.0019 -0.0385 0.0227  0.0095  471  ASN   A OD1  
542  N  ND2  . ASN   A 93  ? 0.8297 1.0774 1.0850 -0.0361 0.0363  0.0117  471  ASN   A ND2  
543  N  N    . PHE   A 94  ? 0.4702 0.6386 0.6994 -0.0469 0.0046  0.0071  472  PHE   A N    
544  C  CA   . PHE   A 94  ? 0.5030 0.6699 0.7363 -0.0555 -0.0029 0.0075  472  PHE   A CA   
545  C  C    . PHE   A 94  ? 0.4617 0.6335 0.6992 -0.0492 -0.0093 0.0038  472  PHE   A C    
546  O  O    . PHE   A 94  ? 0.5402 0.7074 0.7723 -0.0385 -0.0090 0.0009  472  PHE   A O    
547  C  CB   . PHE   A 94  ? 0.5225 0.6638 0.7426 -0.0612 -0.0062 0.0079  472  PHE   A CB   
548  C  CG   . PHE   A 94  ? 0.4894 0.6109 0.6955 -0.0527 -0.0083 0.0042  472  PHE   A CG   
549  C  CD1  . PHE   A 94  ? 0.4947 0.6107 0.6986 -0.0498 -0.0154 0.0008  472  PHE   A CD1  
550  C  CD2  . PHE   A 94  ? 0.4907 0.5996 0.6858 -0.0484 -0.0032 0.0045  472  PHE   A CD2  
551  C  CE1  . PHE   A 94  ? 0.4784 0.5777 0.6694 -0.0427 -0.0168 -0.0020 472  PHE   A CE1  
552  C  CE2  . PHE   A 94  ? 0.5293 0.6216 0.7121 -0.0416 -0.0049 0.0016  472  PHE   A CE2  
553  C  CZ   . PHE   A 94  ? 0.4915 0.5793 0.6723 -0.0389 -0.0115 -0.0015 472  PHE   A CZ   
554  N  N    . THR   A 95  ? 0.4828 0.6645 0.7300 -0.0563 -0.0153 0.0042  473  THR   A N    
555  C  CA   . THR   A 95  ? 0.4657 0.6510 0.7162 -0.0516 -0.0226 0.0009  473  THR   A CA   
556  C  C    . THR   A 95  ? 0.4773 0.6413 0.7170 -0.0558 -0.0300 -0.0010 473  THR   A C    
557  O  O    . THR   A 95  ? 0.5191 0.6686 0.7519 -0.0638 -0.0303 0.0004  473  THR   A O    
558  C  CB   . THR   A 95  ? 0.4846 0.6972 0.7537 -0.0559 -0.0251 0.0020  473  THR   A CB   
559  O  OG1  . THR   A 95  ? 0.5227 0.7364 0.7964 -0.0703 -0.0278 0.0050  473  THR   A OG1  
560  C  CG2  . THR   A 95  ? 0.4675 0.7027 0.7471 -0.0508 -0.0172 0.0034  473  THR   A CG2  
561  N  N    . TYR   A 96  ? 0.4534 0.6152 0.6908 -0.0500 -0.0364 -0.0043 474  TYR   A N    
562  C  CA   . TYR   A 96  ? 0.4828 0.6233 0.7071 -0.0513 -0.0425 -0.0068 474  TYR   A CA   
563  C  C    . TYR   A 96  ? 0.4777 0.6238 0.7052 -0.0493 -0.0511 -0.0096 474  TYR   A C    
564  O  O    . TYR   A 96  ? 0.4668 0.6295 0.7035 -0.0434 -0.0520 -0.0098 474  TYR   A O    
565  C  CB   . TYR   A 96  ? 0.4111 0.5326 0.6195 -0.0432 -0.0391 -0.0082 474  TYR   A CB   
566  C  CG   . TYR   A 96  ? 0.4570 0.5844 0.6655 -0.0318 -0.0369 -0.0090 474  TYR   A CG   
567  C  CD1  . TYR   A 96  ? 0.4919 0.6163 0.6959 -0.0257 -0.0427 -0.0113 474  TYR   A CD1  
568  C  CD2  . TYR   A 96  ? 0.4493 0.5845 0.6615 -0.0271 -0.0295 -0.0074 474  TYR   A CD2  
569  C  CE1  . TYR   A 96  ? 0.4890 0.6169 0.6923 -0.0156 -0.0416 -0.0116 474  TYR   A CE1  
570  C  CE2  . TYR   A 96  ? 0.4217 0.5601 0.6330 -0.0165 -0.0283 -0.0085 474  TYR   A CE2  
571  C  CZ   . TYR   A 96  ? 0.4749 0.6091 0.6819 -0.0110 -0.0346 -0.0104 474  TYR   A CZ   
572  O  OH   . TYR   A 96  ? 0.5155 0.6507 0.7208 -0.0007 -0.0342 -0.0110 474  TYR   A OH   
573  N  N    . GLU   A 97  ? 0.4581 0.5894 0.6769 -0.0539 -0.0578 -0.0118 475  GLU   A N    
574  C  CA   . GLU   A 97  ? 0.4803 0.6104 0.6962 -0.0513 -0.0664 -0.0151 475  GLU   A CA   
575  C  C    . GLU   A 97  ? 0.4327 0.5392 0.6297 -0.0477 -0.0679 -0.0180 475  GLU   A C    
576  O  O    . GLU   A 97  ? 0.4334 0.5249 0.6225 -0.0528 -0.0671 -0.0184 475  GLU   A O    
577  C  CB   . GLU   A 97  ? 0.4579 0.5953 0.6824 -0.0616 -0.0744 -0.0158 475  GLU   A CB   
578  C  CG   . GLU   A 97  ? 0.5956 0.7535 0.8375 -0.0695 -0.0719 -0.0121 475  GLU   A CG   
579  C  CD   . GLU   A 97  ? 0.7131 0.8729 0.9611 -0.0827 -0.0794 -0.0121 475  GLU   A CD   
580  O  OE1  . GLU   A 97  ? 0.6735 0.8187 0.9119 -0.0848 -0.0874 -0.0157 475  GLU   A OE1  
581  O  OE2  . GLU   A 97  ? 0.7369 0.9137 0.9992 -0.0913 -0.0775 -0.0083 475  GLU   A OE2  
582  N  N    . VAL   A 98  ? 0.4334 0.5372 0.6231 -0.0390 -0.0701 -0.0197 476  VAL   A N    
583  C  CA   . VAL   A 98  ? 0.4529 0.5375 0.6249 -0.0348 -0.0706 -0.0220 476  VAL   A CA   
584  C  C    . VAL   A 98  ? 0.4494 0.5292 0.6152 -0.0362 -0.0799 -0.0258 476  VAL   A C    
585  O  O    . VAL   A 98  ? 0.3782 0.4698 0.5505 -0.0349 -0.0854 -0.0262 476  VAL   A O    
586  C  CB   . VAL   A 98  ? 0.4244 0.5078 0.5905 -0.0247 -0.0664 -0.0208 476  VAL   A CB   
587  C  CG1  . VAL   A 98  ? 0.4230 0.4887 0.5715 -0.0213 -0.0662 -0.0226 476  VAL   A CG1  
588  C  CG2  . VAL   A 98  ? 0.4345 0.5233 0.6070 -0.0230 -0.0579 -0.0177 476  VAL   A CG2  
589  N  N    . HIS   A 99  ? 0.3880 0.4506 0.5406 -0.0381 -0.0817 -0.0288 477  HIS   A N    
590  C  CA   . HIS   A 99  ? 0.3924 0.4485 0.5354 -0.0375 -0.0898 -0.0330 477  HIS   A CA   
591  C  C    . HIS   A 99  ? 0.3967 0.4364 0.5217 -0.0321 -0.0877 -0.0354 477  HIS   A C    
592  O  O    . HIS   A 99  ? 0.4191 0.4503 0.5396 -0.0313 -0.0812 -0.0343 477  HIS   A O    
593  C  CB   . HIS   A 99  ? 0.4329 0.4870 0.5795 -0.0469 -0.0971 -0.0357 477  HIS   A CB   
594  C  CG   . HIS   A 99  ? 0.4512 0.4883 0.5902 -0.0516 -0.0959 -0.0374 477  HIS   A CG   
595  N  ND1  . HIS   A 99  ? 0.4835 0.5211 0.6309 -0.0582 -0.0917 -0.0342 477  HIS   A ND1  
596  C  CD2  . HIS   A 99  ? 0.4891 0.5081 0.6127 -0.0505 -0.0989 -0.0421 477  HIS   A CD2  
597  C  CE1  . HIS   A 99  ? 0.5132 0.5325 0.6504 -0.0610 -0.0925 -0.0364 477  HIS   A CE1  
598  N  NE2  . HIS   A 99  ? 0.5164 0.5243 0.6394 -0.0560 -0.0969 -0.0416 477  HIS   A NE2  
599  N  N    . LEU   A 100 ? 0.4341 0.4707 0.5489 -0.0285 -0.0934 -0.0385 478  LEU   A N    
600  C  CA   . LEU   A 100 ? 0.4374 0.4612 0.5348 -0.0234 -0.0923 -0.0412 478  LEU   A CA   
601  C  C    . LEU   A 100 ? 0.4280 0.4383 0.5171 -0.0274 -0.0966 -0.0466 478  LEU   A C    
602  O  O    . LEU   A 100 ? 0.4367 0.4474 0.5288 -0.0326 -0.1044 -0.0496 478  LEU   A O    
603  C  CB   . LEU   A 100 ? 0.4377 0.4652 0.5269 -0.0177 -0.0964 -0.0418 478  LEU   A CB   
604  C  CG   . LEU   A 100 ? 0.3914 0.4277 0.4830 -0.0118 -0.0935 -0.0369 478  LEU   A CG   
605  C  CD1  . LEU   A 100 ? 0.4718 0.5035 0.5604 -0.0084 -0.0841 -0.0335 478  LEU   A CD1  
606  C  CD2  . LEU   A 100 ? 0.5318 0.5825 0.6396 -0.0132 -0.0959 -0.0343 478  LEU   A CD2  
607  N  N    . VAL   A 101 ? 0.4552 0.4534 0.5335 -0.0244 -0.0921 -0.0481 479  VAL   A N    
608  C  CA   . VAL   A 101 ? 0.3891 0.3726 0.4588 -0.0269 -0.0960 -0.0536 479  VAL   A CA   
609  C  C    . VAL   A 101 ? 0.4822 0.4631 0.5431 -0.0263 -0.1050 -0.0593 479  VAL   A C    
610  O  O    . VAL   A 101 ? 0.4786 0.4632 0.5308 -0.0203 -0.1057 -0.0602 479  VAL   A O    
611  C  CB   . VAL   A 101 ? 0.4363 0.4093 0.4947 -0.0214 -0.0898 -0.0546 479  VAL   A CB   
612  C  CG1  . VAL   A 101 ? 0.3889 0.3665 0.4374 -0.0133 -0.0865 -0.0541 479  VAL   A CG1  
613  C  CG2  . VAL   A 101 ? 0.4399 0.3963 0.4881 -0.0223 -0.0946 -0.0611 479  VAL   A CG2  
614  N  N    . ALA   A 102 ? 0.4571 0.4315 0.5202 -0.0331 -0.1124 -0.0629 480  ALA   A N    
615  C  CA   . ALA   A 102 ? 0.5029 0.4761 0.5597 -0.0340 -0.1222 -0.0683 480  ALA   A CA   
616  C  C    . ALA   A 102 ? 0.5291 0.4933 0.5664 -0.0260 -0.1233 -0.0741 480  ALA   A C    
617  O  O    . ALA   A 102 ? 0.5070 0.4761 0.5376 -0.0231 -0.1283 -0.0765 480  ALA   A O    
618  C  CB   . ALA   A 102 ? 0.5664 0.5311 0.6276 -0.0436 -0.1301 -0.0714 480  ALA   A CB   
619  N  N    . ASP   A 103 ? 0.5528 0.5047 0.5803 -0.0219 -0.1189 -0.0765 481  ASP   A N    
620  C  CA   . ASP   A 103 ? 0.5271 0.4717 0.5362 -0.0141 -0.1202 -0.0829 481  ASP   A CA   
621  C  C    . ASP   A 103 ? 0.5134 0.4664 0.5168 -0.0063 -0.1118 -0.0794 481  ASP   A C    
622  O  O    . ASP   A 103 ? 0.4854 0.4351 0.4737 0.0006  -0.1112 -0.0839 481  ASP   A O    
623  C  CB   . ASP   A 103 ? 0.5499 0.4755 0.5495 -0.0131 -0.1219 -0.0892 481  ASP   A CB   
624  C  CG   . ASP   A 103 ? 0.5138 0.4354 0.5162 -0.0112 -0.1131 -0.0856 481  ASP   A CG   
625  O  OD1  . ASP   A 103 ? 0.4908 0.4241 0.5021 -0.0108 -0.1054 -0.0784 481  ASP   A OD1  
626  O  OD2  . ASP   A 103 ? 0.5099 0.4158 0.5051 -0.0097 -0.1145 -0.0901 481  ASP   A OD2  
627  N  N    . GLY   A 104 ? 0.4804 0.4445 0.4952 -0.0073 -0.1055 -0.0717 482  GLY   A N    
628  C  CA   . GLY   A 104 ? 0.4754 0.4472 0.4858 -0.0013 -0.0983 -0.0675 482  GLY   A CA   
629  C  C    . GLY   A 104 ? 0.4777 0.4441 0.4818 0.0032  -0.0907 -0.0676 482  GLY   A C    
630  O  O    . GLY   A 104 ? 0.4533 0.4261 0.4521 0.0078  -0.0852 -0.0645 482  GLY   A O    
631  N  N    . LYS   A 105 ? 0.4106 0.3656 0.4152 0.0017  -0.0905 -0.0705 483  LYS   A N    
632  C  CA   . LYS   A 105 ? 0.4239 0.3735 0.4214 0.0070  -0.0845 -0.0717 483  LYS   A CA   
633  C  C    . LYS   A 105 ? 0.4462 0.3950 0.4549 0.0038  -0.0784 -0.0662 483  LYS   A C    
634  O  O    . LYS   A 105 ? 0.4151 0.3639 0.4358 -0.0029 -0.0798 -0.0632 483  LYS   A O    
635  C  CB   . LYS   A 105 ? 0.5118 0.4472 0.4979 0.0099  -0.0896 -0.0803 483  LYS   A CB   
636  C  CG   . LYS   A 105 ? 0.4961 0.4314 0.4690 0.0138  -0.0958 -0.0869 483  LYS   A CG   
637  C  CD   . LYS   A 105 ? 0.5709 0.5185 0.5349 0.0205  -0.0904 -0.0853 483  LYS   A CD   
638  C  CE   . LYS   A 105 ? 0.5547 0.5020 0.5028 0.0256  -0.0959 -0.0926 483  LYS   A CE   
639  N  NZ   . LYS   A 105 ? 0.5628 0.5113 0.5121 0.0211  -0.1042 -0.0938 483  LYS   A NZ   
640  N  N    . PHE   A 106 ? 0.4310 0.3803 0.4354 0.0087  -0.0715 -0.0648 484  PHE   A N    
641  C  CA   . PHE   A 106 ? 0.4102 0.3584 0.4233 0.0065  -0.0656 -0.0600 484  PHE   A CA   
642  C  C    . PHE   A 106 ? 0.4333 0.3671 0.4468 0.0041  -0.0684 -0.0631 484  PHE   A C    
643  O  O    . PHE   A 106 ? 0.4245 0.3562 0.4483 -0.0022 -0.0680 -0.0594 484  PHE   A O    
644  C  CB   . PHE   A 106 ? 0.4303 0.3841 0.4384 0.0122  -0.0580 -0.0576 484  PHE   A CB   
645  C  CG   . PHE   A 106 ? 0.4089 0.3754 0.4209 0.0119  -0.0539 -0.0514 484  PHE   A CG   
646  C  CD1  . PHE   A 106 ? 0.3655 0.3358 0.3879 0.0087  -0.0492 -0.0453 484  PHE   A CD1  
647  C  CD2  . PHE   A 106 ? 0.3922 0.3659 0.3962 0.0151  -0.0548 -0.0518 484  PHE   A CD2  
648  C  CE1  . PHE   A 106 ? 0.3845 0.3642 0.4094 0.0088  -0.0461 -0.0400 484  PHE   A CE1  
649  C  CE2  . PHE   A 106 ? 0.4038 0.3869 0.4101 0.0146  -0.0517 -0.0458 484  PHE   A CE2  
650  C  CZ   . PHE   A 106 ? 0.3974 0.3827 0.4142 0.0116  -0.0476 -0.0401 484  PHE   A CZ   
651  N  N    . GLY   A 107 ? 0.4701 0.3937 0.4717 0.0094  -0.0711 -0.0697 485  GLY   A N    
652  C  CA   . GLY   A 107 ? 0.4385 0.3457 0.4392 0.0071  -0.0753 -0.0728 485  GLY   A CA   
653  C  C    . GLY   A 107 ? 0.4998 0.3978 0.4906 0.0148  -0.0735 -0.0768 485  GLY   A C    
654  O  O    . GLY   A 107 ? 0.4859 0.3882 0.4789 0.0174  -0.0667 -0.0729 485  GLY   A O    
655  N  N    . THR   A 108 ? 0.4997 0.3854 0.4791 0.0191  -0.0799 -0.0849 486  THR   A N    
656  C  CA   . THR   A 108 ? 0.5214 0.3956 0.4910 0.0270  -0.0800 -0.0900 486  THR   A CA   
657  C  C    . THR   A 108 ? 0.5667 0.4190 0.5316 0.0245  -0.0892 -0.0955 486  THR   A C    
658  O  O    . THR   A 108 ? 0.5425 0.3902 0.5096 0.0174  -0.0959 -0.0968 486  THR   A O    
659  C  CB   . THR   A 108 ? 0.5526 0.4347 0.5099 0.0378  -0.0781 -0.0957 486  THR   A CB   
660  O  OG1  . THR   A 108 ? 0.5313 0.4105 0.4805 0.0385  -0.0851 -0.1023 486  THR   A OG1  
661  C  CG2  . THR   A 108 ? 0.5156 0.4187 0.4774 0.0387  -0.0696 -0.0894 486  THR   A CG2  
662  N  N    . GLN   A 109 ? 0.5580 0.3962 0.5162 0.0302  -0.0900 -0.0987 487  GLN   A N    
663  C  CA   . GLN   A 109 ? 0.5879 0.4019 0.5394 0.0289  -0.0993 -0.1043 487  GLN   A CA   
664  C  C    . GLN   A 109 ? 0.6414 0.4482 0.5767 0.0402  -0.1039 -0.1153 487  GLN   A C    
665  O  O    . GLN   A 109 ? 0.6355 0.4454 0.5637 0.0513  -0.0997 -0.1185 487  GLN   A O    
666  C  CB   . GLN   A 109 ? 0.6001 0.4009 0.5537 0.0283  -0.0982 -0.1007 487  GLN   A CB   
667  C  CG   . GLN   A 109 ? 0.6725 0.4463 0.6209 0.0237  -0.1085 -0.1042 487  GLN   A CG   
668  C  CD   . GLN   A 109 ? 0.7067 0.4669 0.6575 0.0216  -0.1078 -0.0992 487  GLN   A CD   
669  O  OE1  . GLN   A 109 ? 0.6377 0.4035 0.5880 0.0290  -0.1013 -0.0972 487  GLN   A OE1  
670  N  NE2  . GLN   A 109 ? 0.6755 0.4175 0.6282 0.0112  -0.1150 -0.0970 487  GLN   A NE2  
671  N  N    . GLU   A 110 ? 0.6450 0.4433 0.5744 0.0376  -0.1125 -0.1214 488  GLU   A N    
672  C  CA   . GLU   A 110 ? 0.6889 0.4804 0.6017 0.0484  -0.1174 -0.1328 488  GLU   A CA   
673  C  C    . GLU   A 110 ? 0.6939 0.4558 0.5968 0.0491  -0.1282 -0.1404 488  GLU   A C    
674  O  O    . GLU   A 110 ? 0.6759 0.4247 0.5831 0.0379  -0.1356 -0.1389 488  GLU   A O    
675  C  CB   . GLU   A 110 ? 0.7082 0.5122 0.6184 0.0467  -0.1196 -0.1354 488  GLU   A CB   
676  C  CG   . GLU   A 110 ? 0.6822 0.5138 0.6001 0.0466  -0.1100 -0.1283 488  GLU   A CG   
677  C  CD   . GLU   A 110 ? 0.7684 0.6121 0.6808 0.0582  -0.1014 -0.1290 488  GLU   A CD   
678  O  OE1  . GLU   A 110 ? 0.7643 0.6004 0.6630 0.0690  -0.1037 -0.1380 488  GLU   A OE1  
679  O  OE2  . GLU   A 110 ? 0.7524 0.6132 0.6739 0.0567  -0.0926 -0.1208 488  GLU   A OE2  
680  N  N    . ASN   A 116 ? 1.1493 0.7380 0.9708 0.0780  -0.1894 -0.1936 494  ASN   A N    
681  C  CA   . ASN   A 116 ? 1.1460 0.7136 0.9731 0.0691  -0.1928 -0.1858 494  ASN   A CA   
682  C  C    . ASN   A 116 ? 1.1714 0.7571 1.0191 0.0537  -0.1849 -0.1706 494  ASN   A C    
683  O  O    . ASN   A 116 ? 1.1689 0.7642 1.0242 0.0563  -0.1762 -0.1632 494  ASN   A O    
684  C  CB   . ASN   A 116 ? 1.2051 0.7490 1.0269 0.0598  -0.2042 -0.1862 494  ASN   A CB   
685  C  CG   . ASN   A 116 ? 1.2547 0.7789 1.0813 0.0503  -0.2071 -0.1767 494  ASN   A CG   
686  O  OD1  . ASN   A 116 ? 1.2562 0.7821 1.0874 0.0539  -0.2011 -0.1711 494  ASN   A OD1  
687  N  ND2  . ASN   A 116 ? 1.2807 0.7860 1.1055 0.0386  -0.2167 -0.1750 494  ASN   A ND2  
688  N  N    . LYS   A 117 ? 1.0999 0.6908 0.9567 0.0380  -0.1879 -0.1661 495  LYS   A N    
689  C  CA   . LYS   A 117 ? 1.0641 0.6744 0.9407 0.0238  -0.1804 -0.1524 495  LYS   A CA   
690  C  C    . LYS   A 117 ? 0.9593 0.6057 0.8448 0.0288  -0.1675 -0.1488 495  LYS   A C    
691  O  O    . LYS   A 117 ? 0.9181 0.5761 0.7957 0.0392  -0.1658 -0.1564 495  LYS   A O    
692  C  CB   . LYS   A 117 ? 1.0015 0.6068 0.8852 0.0060  -0.1885 -0.1493 495  LYS   A CB   
693  N  N    . LYS   A 118 ? 0.9170 0.5808 0.8185 0.0211  -0.1585 -0.1369 496  LYS   A N    
694  C  CA   . LYS   A 118 ? 0.8191 0.5153 0.7306 0.0232  -0.1468 -0.1318 496  LYS   A CA   
695  C  C    . LYS   A 118 ? 0.8555 0.5665 0.7840 0.0074  -0.1446 -0.1221 496  LYS   A C    
696  O  O    . LYS   A 118 ? 0.8848 0.5845 0.8202 -0.0048 -0.1486 -0.1163 496  LYS   A O    
697  C  CB   . LYS   A 118 ? 0.7863 0.4918 0.7003 0.0316  -0.1367 -0.1273 496  LYS   A CB   
698  N  N    . GLU   A 119 ? 0.7335 0.4702 0.6684 0.0079  -0.1384 -0.1202 497  GLU   A N    
699  C  CA   . GLU   A 119 ? 0.7231 0.4764 0.6736 -0.0048 -0.1366 -0.1123 497  GLU   A CA   
700  C  C    . GLU   A 119 ? 0.6272 0.4082 0.5863 -0.0012 -0.1250 -0.1066 497  GLU   A C    
701  O  O    . GLU   A 119 ? 0.6310 0.4212 0.5824 0.0100  -0.1207 -0.1106 497  GLU   A O    
702  C  CB   . GLU   A 119 ? 0.8031 0.5555 0.7510 -0.0098 -0.1454 -0.1177 497  GLU   A CB   
703  C  CG   . GLU   A 119 ? 0.7742 0.5477 0.7196 -0.0024 -0.1414 -0.1206 497  GLU   A CG   
704  C  CD   . GLU   A 119 ? 0.9011 0.6734 0.8428 -0.0067 -0.1506 -0.1261 497  GLU   A CD   
705  O  OE1  . GLU   A 119 ? 0.9447 0.6951 0.8801 -0.0111 -0.1609 -0.1312 497  GLU   A OE1  
706  O  OE2  . GLU   A 119 ? 0.8950 0.6868 0.8392 -0.0055 -0.1481 -0.1255 497  GLU   A OE2  
707  N  N    . TRP   A 120 ? 0.6094 0.4039 0.5842 -0.0110 -0.1204 -0.0971 498  TRP   A N    
708  C  CA   . TRP   A 120 ? 0.5878 0.4073 0.5716 -0.0092 -0.1106 -0.0912 498  TRP   A CA   
709  C  C    . TRP   A 120 ? 0.6053 0.4390 0.5936 -0.0131 -0.1133 -0.0917 498  TRP   A C    
710  O  O    . TRP   A 120 ? 0.6095 0.4401 0.6036 -0.0228 -0.1201 -0.0912 498  TRP   A O    
711  C  CB   . TRP   A 120 ? 0.5591 0.3858 0.5569 -0.0165 -0.1041 -0.0812 498  TRP   A CB   
712  C  CG   . TRP   A 120 ? 0.5856 0.4046 0.5799 -0.0112 -0.0991 -0.0793 498  TRP   A CG   
713  C  CD1  . TRP   A 120 ? 0.5992 0.3987 0.5910 -0.0144 -0.1027 -0.0784 498  TRP   A CD1  
714  C  CD2  . TRP   A 120 ? 0.5379 0.3682 0.5307 -0.0022 -0.0902 -0.0777 498  TRP   A CD2  
715  N  NE1  . TRP   A 120 ? 0.6022 0.4007 0.5911 -0.0072 -0.0965 -0.0765 498  TRP   A NE1  
716  C  CE2  . TRP   A 120 ? 0.5326 0.3505 0.5225 0.0002  -0.0888 -0.0761 498  TRP   A CE2  
717  C  CE3  . TRP   A 120 ? 0.5114 0.3610 0.5049 0.0037  -0.0837 -0.0771 498  TRP   A CE3  
718  C  CZ2  . TRP   A 120 ? 0.5689 0.3942 0.5572 0.0083  -0.0812 -0.0744 498  TRP   A CZ2  
719  C  CZ3  . TRP   A 120 ? 0.5051 0.3615 0.4969 0.0110  -0.0761 -0.0751 498  TRP   A CZ3  
720  C  CH2  . TRP   A 120 ? 0.5635 0.4085 0.5531 0.0134  -0.0749 -0.0740 498  TRP   A CH2  
721  N  N    . ASN   A 121 ? 0.5761 0.4256 0.5616 -0.0058 -0.1082 -0.0923 499  ASN   A N    
722  C  CA   . ASN   A 121 ? 0.5588 0.4238 0.5486 -0.0082 -0.1095 -0.0915 499  ASN   A CA   
723  C  C    . ASN   A 121 ? 0.4870 0.3712 0.4905 -0.0109 -0.1010 -0.0823 499  ASN   A C    
724  O  O    . ASN   A 121 ? 0.4810 0.3659 0.4909 -0.0120 -0.0947 -0.0769 499  ASN   A O    
725  C  CB   . ASN   A 121 ? 0.5967 0.4648 0.5721 0.0019  -0.1104 -0.0985 499  ASN   A CB   
726  C  CG   . ASN   A 121 ? 0.5513 0.4247 0.5206 0.0118  -0.1018 -0.0981 499  ASN   A CG   
727  O  OD1  . ASN   A 121 ? 0.5687 0.4544 0.5465 0.0113  -0.0936 -0.0908 499  ASN   A OD1  
728  N  ND2  . ASN   A 121 ? 0.5623 0.4272 0.5167 0.0212  -0.1036 -0.1061 499  ASN   A ND2  
729  N  N    . GLY   A 122 ? 0.4995 0.3987 0.5067 -0.0114 -0.1011 -0.0808 500  GLY   A N    
730  C  CA   . GLY   A 122 ? 0.4386 0.3554 0.4557 -0.0114 -0.0934 -0.0733 500  GLY   A CA   
731  C  C    . GLY   A 122 ? 0.4291 0.3499 0.4619 -0.0196 -0.0905 -0.0663 500  GLY   A C    
732  O  O    . GLY   A 122 ? 0.4724 0.3868 0.5111 -0.0276 -0.0957 -0.0663 500  GLY   A O    
733  N  N    . MET   A 123 ? 0.4668 0.3985 0.5058 -0.0177 -0.0822 -0.0603 501  MET   A N    
734  C  CA   . MET   A 123 ? 0.4213 0.3591 0.4746 -0.0243 -0.0785 -0.0538 501  MET   A CA   
735  C  C    . MET   A 123 ? 0.4664 0.3908 0.5197 -0.0280 -0.0782 -0.0533 501  MET   A C    
736  O  O    . MET   A 123 ? 0.4574 0.3832 0.5212 -0.0361 -0.0784 -0.0492 501  MET   A O    
737  C  CB   . MET   A 123 ? 0.3880 0.3378 0.4453 -0.0203 -0.0699 -0.0485 501  MET   A CB   
738  C  CG   . MET   A 123 ? 0.4237 0.3843 0.4785 -0.0158 -0.0703 -0.0486 501  MET   A CG   
739  S  SD   . MET   A 123 ? 0.4192 0.3936 0.4827 -0.0141 -0.0624 -0.0414 501  MET   A SD   
740  C  CE   . MET   A 123 ? 0.3567 0.3261 0.4066 -0.0064 -0.0570 -0.0425 501  MET   A CE   
741  N  N    . MET   A 124 ? 0.4241 0.3359 0.4653 -0.0220 -0.0778 -0.0571 502  MET   A N    
742  C  CA   . MET   A 124 ? 0.4739 0.3708 0.5135 -0.0246 -0.0782 -0.0568 502  MET   A CA   
743  C  C    . MET   A 124 ? 0.4415 0.3265 0.4821 -0.0329 -0.0873 -0.0591 502  MET   A C    
744  O  O    . MET   A 124 ? 0.5039 0.3839 0.5513 -0.0409 -0.0878 -0.0549 502  MET   A O    
745  C  CB   . MET   A 124 ? 0.4117 0.2979 0.4376 -0.0151 -0.0772 -0.0615 502  MET   A CB   
746  C  CG   . MET   A 124 ? 0.4843 0.3805 0.5103 -0.0089 -0.0680 -0.0579 502  MET   A CG   
747  S  SD   . MET   A 124 ? 0.4888 0.3834 0.5233 -0.0136 -0.0621 -0.0505 502  MET   A SD   
748  C  CE   . MET   A 124 ? 0.5087 0.3793 0.5340 -0.0133 -0.0681 -0.0544 502  MET   A CE   
749  N  N    . GLY   A 125 ? 0.4690 0.3497 0.5025 -0.0315 -0.0947 -0.0657 503  GLY   A N    
750  C  CA   . GLY   A 125 ? 0.5362 0.4049 0.5699 -0.0398 -0.1044 -0.0684 503  GLY   A CA   
751  C  C    . GLY   A 125 ? 0.5225 0.4039 0.5724 -0.0511 -0.1053 -0.0625 503  GLY   A C    
752  O  O    . GLY   A 125 ? 0.5242 0.3973 0.5790 -0.0609 -0.1096 -0.0603 503  GLY   A O    
753  N  N    . GLU   A 126 ? 0.4658 0.3678 0.5243 -0.0499 -0.1012 -0.0594 504  GLU   A N    
754  C  CA   . GLU   A 126 ? 0.5137 0.4313 0.5887 -0.0590 -0.1012 -0.0538 504  GLU   A CA   
755  C  C    . GLU   A 126 ? 0.5029 0.4232 0.5876 -0.0644 -0.0948 -0.0466 504  GLU   A C    
756  O  O    . GLU   A 126 ? 0.5126 0.4362 0.6076 -0.0750 -0.0973 -0.0429 504  GLU   A O    
757  C  CB   . GLU   A 126 ? 0.4978 0.4356 0.5786 -0.0543 -0.0981 -0.0523 504  GLU   A CB   
758  C  CG   . GLU   A 126 ? 0.5420 0.4794 0.6144 -0.0504 -0.1052 -0.0586 504  GLU   A CG   
759  C  CD   . GLU   A 126 ? 0.5777 0.5348 0.6600 -0.0509 -0.1062 -0.0563 504  GLU   A CD   
760  O  OE1  . GLU   A 126 ? 0.5366 0.5081 0.6328 -0.0538 -0.1015 -0.0503 504  GLU   A OE1  
761  O  OE2  . GLU   A 126 ? 0.5224 0.4806 0.5979 -0.0477 -0.1119 -0.0607 504  GLU   A OE2  
762  N  N    . LEU   A 127 ? 0.4945 0.4140 0.5756 -0.0579 -0.0865 -0.0443 505  LEU   A N    
763  C  CA   . LEU   A 127 ? 0.4340 0.3556 0.5229 -0.0629 -0.0806 -0.0376 505  LEU   A CA   
764  C  C    . LEU   A 127 ? 0.5115 0.4139 0.5963 -0.0702 -0.0856 -0.0374 505  LEU   A C    
765  O  O    . LEU   A 127 ? 0.4648 0.3701 0.5589 -0.0800 -0.0849 -0.0317 505  LEU   A O    
766  C  CB   . LEU   A 127 ? 0.4929 0.4169 0.5778 -0.0543 -0.0715 -0.0356 505  LEU   A CB   
767  C  CG   . LEU   A 127 ? 0.4636 0.3902 0.5549 -0.0581 -0.0647 -0.0289 505  LEU   A CG   
768  C  CD1  . LEU   A 127 ? 0.4860 0.4327 0.5928 -0.0639 -0.0614 -0.0237 505  LEU   A CD1  
769  C  CD2  . LEU   A 127 ? 0.4558 0.3815 0.5408 -0.0494 -0.0573 -0.0280 505  LEU   A CD2  
770  N  N    . LEU   A 128 ? 0.4401 0.3226 0.5108 -0.0657 -0.0910 -0.0435 506  LEU   A N    
771  C  CA   . LEU   A 128 ? 0.5220 0.3829 0.5869 -0.0716 -0.0965 -0.0437 506  LEU   A CA   
772  C  C    . LEU   A 128 ? 0.5581 0.4150 0.6279 -0.0835 -0.1058 -0.0441 506  LEU   A C    
773  O  O    . LEU   A 128 ? 0.6114 0.4562 0.6823 -0.0930 -0.1092 -0.0405 506  LEU   A O    
774  C  CB   . LEU   A 128 ? 0.5141 0.3546 0.5619 -0.0617 -0.0999 -0.0510 506  LEU   A CB   
775  C  CG   . LEU   A 128 ? 0.5272 0.3686 0.5700 -0.0517 -0.0913 -0.0496 506  LEU   A CG   
776  C  CD1  . LEU   A 128 ? 0.5039 0.3294 0.5306 -0.0406 -0.0944 -0.0575 506  LEU   A CD1  
777  C  CD2  . LEU   A 128 ? 0.5473 0.3842 0.5946 -0.0576 -0.0875 -0.0422 506  LEU   A CD2  
778  N  N    . SER   A 129 ? 0.5441 0.4104 0.6165 -0.0837 -0.1104 -0.0480 507  SER   A N    
779  C  CA   . SER   A 129 ? 0.6023 0.4666 0.6802 -0.0955 -0.1197 -0.0484 507  SER   A CA   
780  C  C    . SER   A 129 ? 0.5829 0.4699 0.6798 -0.1060 -0.1165 -0.0406 507  SER   A C    
781  O  O    . SER   A 129 ? 0.5702 0.4580 0.6740 -0.1177 -0.1236 -0.0394 507  SER   A O    
782  C  CB   . SER   A 129 ? 0.6072 0.4719 0.6791 -0.0914 -0.1270 -0.0563 507  SER   A CB   
783  O  OG   . SER   A 129 ? 0.6091 0.4979 0.6892 -0.0866 -0.1217 -0.0549 507  SER   A OG   
784  N  N    . GLY   A 130 ? 0.5727 0.4784 0.6783 -0.1020 -0.1061 -0.0353 508  GLY   A N    
785  C  CA   . GLY   A 130 ? 0.5532 0.4827 0.6767 -0.1099 -0.1026 -0.0288 508  GLY   A CA   
786  C  C    . GLY   A 130 ? 0.5539 0.5046 0.6859 -0.1068 -0.1035 -0.0306 508  GLY   A C    
787  O  O    . GLY   A 130 ? 0.5252 0.4979 0.6728 -0.1118 -0.1005 -0.0257 508  GLY   A O    
788  N  N    . GLN   A 131 ? 0.5349 0.4802 0.6568 -0.0983 -0.1075 -0.0375 509  GLN   A N    
789  C  CA   . GLN   A 131 ? 0.5358 0.5006 0.6642 -0.0938 -0.1078 -0.0387 509  GLN   A CA   
790  C  C    . GLN   A 131 ? 0.5246 0.5062 0.6595 -0.0863 -0.0974 -0.0345 509  GLN   A C    
791  O  O    . GLN   A 131 ? 0.4948 0.4954 0.6389 -0.0841 -0.0967 -0.0334 509  GLN   A O    
792  C  CB   . GLN   A 131 ? 0.5620 0.5166 0.6760 -0.0856 -0.1134 -0.0465 509  GLN   A CB   
793  C  CG   . GLN   A 131 ? 0.6506 0.5953 0.7607 -0.0922 -0.1253 -0.0517 509  GLN   A CG   
794  C  CD   . GLN   A 131 ? 0.6887 0.6169 0.7800 -0.0832 -0.1297 -0.0599 509  GLN   A CD   
795  O  OE1  . GLN   A 131 ? 0.7276 0.6345 0.8067 -0.0819 -0.1318 -0.0635 509  GLN   A OE1  
796  N  NE2  . GLN   A 131 ? 0.6927 0.6312 0.7815 -0.0768 -0.1315 -0.0630 509  GLN   A NE2  
797  N  N    . ALA   A 132 ? 0.4636 0.4377 0.5929 -0.0819 -0.0898 -0.0323 510  ALA   A N    
798  C  CA   . ALA   A 132 ? 0.4602 0.4481 0.5953 -0.0762 -0.0799 -0.0280 510  ALA   A CA   
799  C  C    . ALA   A 132 ? 0.4761 0.4597 0.6132 -0.0805 -0.0739 -0.0229 510  ALA   A C    
800  O  O    . ALA   A 132 ? 0.4783 0.4437 0.6077 -0.0844 -0.0766 -0.0235 510  ALA   A O    
801  C  CB   . ALA   A 132 ? 0.4425 0.4264 0.5663 -0.0640 -0.0762 -0.0309 510  ALA   A CB   
802  N  N    . ASP   A 133 ? 0.4396 0.4393 0.5863 -0.0793 -0.0660 -0.0181 511  ASP   A N    
803  C  CA   . ASP   A 133 ? 0.4399 0.4378 0.5878 -0.0818 -0.0591 -0.0131 511  ASP   A CA   
804  C  C    . ASP   A 133 ? 0.4403 0.4349 0.5803 -0.0717 -0.0517 -0.0132 511  ASP   A C    
805  O  O    . ASP   A 133 ? 0.4390 0.4262 0.5753 -0.0724 -0.0471 -0.0102 511  ASP   A O    
806  C  CB   . ASP   A 133 ? 0.4815 0.5010 0.6456 -0.0881 -0.0550 -0.0076 511  ASP   A CB   
807  C  CG   . ASP   A 133 ? 0.5227 0.5490 0.6967 -0.0995 -0.0619 -0.0066 511  ASP   A CG   
808  O  OD1  . ASP   A 133 ? 0.5147 0.5242 0.6829 -0.1071 -0.0680 -0.0072 511  ASP   A OD1  
809  O  OD2  . ASP   A 133 ? 0.4670 0.5151 0.6543 -0.1006 -0.0617 -0.0055 511  ASP   A OD2  
810  N  N    . MET   A 134 ? 0.4302 0.4301 0.5676 -0.0628 -0.0508 -0.0160 512  MET   A N    
811  C  CA   . MET   A 134 ? 0.3939 0.3914 0.5241 -0.0539 -0.0443 -0.0158 512  MET   A CA   
812  C  C    . MET   A 134 ? 0.4227 0.4179 0.5449 -0.0461 -0.0472 -0.0203 512  MET   A C    
813  O  O    . MET   A 134 ? 0.3873 0.3908 0.5139 -0.0460 -0.0516 -0.0219 512  MET   A O    
814  C  CB   . MET   A 134 ? 0.4074 0.4212 0.5471 -0.0521 -0.0371 -0.0118 512  MET   A CB   
815  C  CG   . MET   A 134 ? 0.4359 0.4470 0.5684 -0.0437 -0.0309 -0.0115 512  MET   A CG   
816  S  SD   . MET   A 134 ? 0.4725 0.5017 0.6158 -0.0416 -0.0235 -0.0077 512  MET   A SD   
817  C  CE   . MET   A 134 ? 0.5487 0.5777 0.6962 -0.0501 -0.0197 -0.0032 512  MET   A CE   
818  N  N    . ILE   A 135 ? 0.3638 0.3485 0.4743 -0.0397 -0.0448 -0.0219 513  ILE   A N    
819  C  CA   . ILE   A 135 ? 0.3510 0.3347 0.4529 -0.0322 -0.0460 -0.0252 513  ILE   A CA   
820  C  C    . ILE   A 135 ? 0.3537 0.3454 0.4566 -0.0267 -0.0393 -0.0222 513  ILE   A C    
821  O  O    . ILE   A 135 ? 0.3411 0.3290 0.4411 -0.0251 -0.0339 -0.0203 513  ILE   A O    
822  C  CB   . ILE   A 135 ? 0.3533 0.3218 0.4414 -0.0286 -0.0477 -0.0292 513  ILE   A CB   
823  C  CG1  . ILE   A 135 ? 0.3923 0.3493 0.4777 -0.0337 -0.0549 -0.0326 513  ILE   A CG1  
824  C  CG2  . ILE   A 135 ? 0.4002 0.3705 0.4795 -0.0211 -0.0483 -0.0319 513  ILE   A CG2  
825  C  CD1  . ILE   A 135 ? 0.3562 0.2978 0.4276 -0.0288 -0.0567 -0.0372 513  ILE   A CD1  
826  N  N    . VAL   A 136 ? 0.3828 0.3844 0.4891 -0.0237 -0.0403 -0.0219 514  VAL   A N    
827  C  CA   . VAL   A 136 ? 0.3836 0.3905 0.4894 -0.0182 -0.0353 -0.0195 514  VAL   A CA   
828  C  C    . VAL   A 136 ? 0.3978 0.4027 0.4942 -0.0131 -0.0382 -0.0215 514  VAL   A C    
829  O  O    . VAL   A 136 ? 0.3844 0.3953 0.4833 -0.0124 -0.0428 -0.0222 514  VAL   A O    
830  C  CB   . VAL   A 136 ? 0.3121 0.3325 0.4303 -0.0187 -0.0337 -0.0168 514  VAL   A CB   
831  C  CG1  . VAL   A 136 ? 0.3897 0.4123 0.5056 -0.0127 -0.0291 -0.0147 514  VAL   A CG1  
832  C  CG2  . VAL   A 136 ? 0.3493 0.3734 0.4766 -0.0247 -0.0307 -0.0146 514  VAL   A CG2  
833  N  N    . ALA   A 137 ? 0.3730 0.3704 0.4587 -0.0098 -0.0358 -0.0222 515  ALA   A N    
834  C  CA   . ALA   A 137 ? 0.3661 0.3615 0.4412 -0.0056 -0.0380 -0.0240 515  ALA   A CA   
835  C  C    . ALA   A 137 ? 0.3644 0.3552 0.4308 -0.0023 -0.0331 -0.0232 515  ALA   A C    
836  O  O    . ALA   A 137 ? 0.3778 0.3654 0.4458 -0.0034 -0.0289 -0.0221 515  ALA   A O    
837  C  CB   . ALA   A 137 ? 0.3835 0.3738 0.4534 -0.0067 -0.0442 -0.0288 515  ALA   A CB   
838  N  N    . PRO   A 138 ? 0.3774 0.3686 0.4341 0.0014  -0.0334 -0.0236 516  PRO   A N    
839  C  CA   . PRO   A 138 ? 0.3643 0.3529 0.4131 0.0040  -0.0291 -0.0233 516  PRO   A CA   
840  C  C    . PRO   A 138 ? 0.3875 0.3693 0.4308 0.0049  -0.0302 -0.0278 516  PRO   A C    
841  O  O    . PRO   A 138 ? 0.3936 0.3750 0.4275 0.0082  -0.0316 -0.0307 516  PRO   A O    
842  C  CB   . PRO   A 138 ? 0.4049 0.3976 0.4457 0.0068  -0.0297 -0.0220 516  PRO   A CB   
843  C  CG   . PRO   A 138 ? 0.3698 0.3646 0.4110 0.0064  -0.0358 -0.0237 516  PRO   A CG   
844  C  CD   . PRO   A 138 ? 0.3662 0.3619 0.4197 0.0031  -0.0374 -0.0234 516  PRO   A CD   
845  N  N    . LEU   A 139 ? 0.4071 0.3837 0.4558 0.0021  -0.0298 -0.0282 517  LEU   A N    
846  C  CA   . LEU   A 139 ? 0.3960 0.3634 0.4403 0.0025  -0.0324 -0.0325 517  LEU   A CA   
847  C  C    . LEU   A 139 ? 0.3948 0.3588 0.4349 0.0054  -0.0279 -0.0321 517  LEU   A C    
848  O  O    . LEU   A 139 ? 0.3847 0.3478 0.4300 0.0032  -0.0242 -0.0288 517  LEU   A O    
849  C  CB   . LEU   A 139 ? 0.3863 0.3492 0.4388 -0.0033 -0.0353 -0.0326 517  LEU   A CB   
850  C  CG   . LEU   A 139 ? 0.4132 0.3635 0.4611 -0.0039 -0.0391 -0.0367 517  LEU   A CG   
851  C  CD1  . LEU   A 139 ? 0.4033 0.3497 0.4435 -0.0017 -0.0455 -0.0425 517  LEU   A CD1  
852  C  CD2  . LEU   A 139 ? 0.4249 0.3713 0.4816 -0.0111 -0.0405 -0.0345 517  LEU   A CD2  
853  N  N    . THR   A 140 ? 0.3182 0.2810 0.3485 0.0106  -0.0282 -0.0356 518  THR   A N    
854  C  CA   . THR   A 140 ? 0.3888 0.3507 0.4151 0.0144  -0.0242 -0.0354 518  THR   A CA   
855  C  C    . THR   A 140 ? 0.4190 0.3696 0.4461 0.0137  -0.0254 -0.0368 518  THR   A C    
856  O  O    . THR   A 140 ? 0.4227 0.3639 0.4476 0.0132  -0.0306 -0.0409 518  THR   A O    
857  C  CB   . THR   A 140 ? 0.3775 0.3430 0.3934 0.0206  -0.0245 -0.0393 518  THR   A CB   
858  O  OG1  . THR   A 140 ? 0.3939 0.3702 0.4084 0.0205  -0.0227 -0.0365 518  THR   A OG1  
859  C  CG2  . THR   A 140 ? 0.3778 0.3432 0.3901 0.0252  -0.0210 -0.0398 518  THR   A CG2  
860  N  N    . ILE   A 141 ? 0.4235 0.3744 0.4531 0.0136  -0.0210 -0.0334 519  ILE   A N    
861  C  CA   . ILE   A 141 ? 0.3834 0.3238 0.4127 0.0135  -0.0216 -0.0337 519  ILE   A CA   
862  C  C    . ILE   A 141 ? 0.4402 0.3767 0.4603 0.0211  -0.0227 -0.0384 519  ILE   A C    
863  O  O    . ILE   A 141 ? 0.4306 0.3757 0.4477 0.0256  -0.0190 -0.0379 519  ILE   A O    
864  C  CB   . ILE   A 141 ? 0.4162 0.3597 0.4511 0.0108  -0.0165 -0.0280 519  ILE   A CB   
865  C  CG1  . ILE   A 141 ? 0.3898 0.3387 0.4336 0.0046  -0.0151 -0.0241 519  ILE   A CG1  
866  C  CG2  . ILE   A 141 ? 0.4664 0.3987 0.5002 0.0105  -0.0174 -0.0277 519  ILE   A CG2  
867  C  CD1  . ILE   A 141 ? 0.3744 0.3289 0.4226 0.0029  -0.0094 -0.0189 519  ILE   A CD1  
868  N  N    . ASN   A 142 ? 0.4447 0.3681 0.4602 0.0226  -0.0281 -0.0429 520  ASN   A N    
869  C  CA   . ASN   A 142 ? 0.3996 0.3178 0.4064 0.0310  -0.0296 -0.0479 520  ASN   A CA   
870  C  C    . ASN   A 142 ? 0.4215 0.3214 0.4262 0.0302  -0.0344 -0.0494 520  ASN   A C    
871  O  O    . ASN   A 142 ? 0.4570 0.3493 0.4670 0.0224  -0.0367 -0.0467 520  ASN   A O    
872  C  CB   . ASN   A 142 ? 0.4546 0.3761 0.4533 0.0368  -0.0323 -0.0543 520  ASN   A CB   
873  C  CG   . ASN   A 142 ? 0.4713 0.3830 0.4685 0.0333  -0.0390 -0.0582 520  ASN   A CG   
874  O  OD1  . ASN   A 142 ? 0.4613 0.3620 0.4630 0.0269  -0.0424 -0.0567 520  ASN   A OD1  
875  N  ND2  . ASN   A 142 ? 0.4510 0.3676 0.4419 0.0371  -0.0410 -0.0630 520  ASN   A ND2  
876  N  N    . ASN   A 143 ? 0.5070 0.4002 0.5041 0.0384  -0.0360 -0.0536 521  ASN   A N    
877  C  CA   . ASN   A 143 ? 0.5086 0.3825 0.5026 0.0384  -0.0408 -0.0545 521  ASN   A CA   
878  C  C    . ASN   A 143 ? 0.4983 0.3574 0.4894 0.0346  -0.0485 -0.0585 521  ASN   A C    
879  O  O    . ASN   A 143 ? 0.5121 0.3573 0.5055 0.0276  -0.0521 -0.0559 521  ASN   A O    
880  C  CB   . ASN   A 143 ? 0.4949 0.3649 0.4807 0.0496  -0.0415 -0.0589 521  ASN   A CB   
881  C  CG   . ASN   A 143 ? 0.5545 0.4013 0.5348 0.0509  -0.0482 -0.0608 521  ASN   A CG   
882  O  OD1  . ASN   A 143 ? 0.5723 0.4052 0.5459 0.0530  -0.0549 -0.0669 521  ASN   A OD1  
883  N  ND2  . ASN   A 143 ? 0.5440 0.3857 0.5268 0.0491  -0.0467 -0.0554 521  ASN   A ND2  
884  N  N    . GLU   A 144 ? 0.5027 0.3647 0.4883 0.0386  -0.0511 -0.0648 522  GLU   A N    
885  C  CA   . GLU   A 144 ? 0.4942 0.3425 0.4760 0.0355  -0.0590 -0.0696 522  GLU   A CA   
886  C  C    . GLU   A 144 ? 0.5253 0.3727 0.5170 0.0228  -0.0602 -0.0640 522  GLU   A C    
887  O  O    . GLU   A 144 ? 0.5067 0.3378 0.4983 0.0169  -0.0661 -0.0639 522  GLU   A O    
888  C  CB   . GLU   A 144 ? 0.5483 0.4052 0.5238 0.0412  -0.0602 -0.0761 522  GLU   A CB   
889  C  CG   . GLU   A 144 ? 0.5911 0.4486 0.5555 0.0544  -0.0600 -0.0832 522  GLU   A CG   
890  C  CD   . GLU   A 144 ? 0.6109 0.4885 0.5776 0.0597  -0.0514 -0.0800 522  GLU   A CD   
891  O  OE1  . GLU   A 144 ? 0.4970 0.3847 0.4731 0.0538  -0.0457 -0.0721 522  GLU   A OE1  
892  O  OE2  . GLU   A 144 ? 0.6483 0.5318 0.6069 0.0701  -0.0505 -0.0857 522  GLU   A OE2  
893  N  N    . ARG   A 145 ? 0.4699 0.3350 0.4704 0.0184  -0.0547 -0.0591 523  ARG   A N    
894  C  CA   . ARG   A 145 ? 0.4875 0.3550 0.4982 0.0075  -0.0554 -0.0541 523  ARG   A CA   
895  C  C    . ARG   A 145 ? 0.4880 0.3505 0.5049 0.0012  -0.0532 -0.0474 523  ARG   A C    
896  O  O    . ARG   A 145 ? 0.4899 0.3463 0.5122 -0.0079 -0.0566 -0.0447 523  ARG   A O    
897  C  CB   . ARG   A 145 ? 0.4177 0.3049 0.4351 0.0061  -0.0505 -0.0512 523  ARG   A CB   
898  C  CG   . ARG   A 145 ? 0.4435 0.3352 0.4550 0.0101  -0.0537 -0.0570 523  ARG   A CG   
899  C  CD   . ARG   A 145 ? 0.5128 0.4229 0.5275 0.0116  -0.0482 -0.0540 523  ARG   A CD   
900  N  NE   . ARG   A 145 ? 0.4706 0.3854 0.4800 0.0141  -0.0516 -0.0585 523  ARG   A NE   
901  C  CZ   . ARG   A 145 ? 0.4580 0.3868 0.4679 0.0155  -0.0484 -0.0564 523  ARG   A CZ   
902  N  NH1  . ARG   A 145 ? 0.3900 0.3289 0.4058 0.0146  -0.0419 -0.0504 523  ARG   A NH1  
903  N  NH2  . ARG   A 145 ? 0.4439 0.3758 0.4477 0.0176  -0.0522 -0.0605 523  ARG   A NH2  
904  N  N    . ALA   A 146 ? 0.5101 0.3763 0.5265 0.0055  -0.0476 -0.0445 524  ALA   A N    
905  C  CA   . ALA   A 146 ? 0.4872 0.3504 0.5087 0.0001  -0.0447 -0.0378 524  ALA   A CA   
906  C  C    . ALA   A 146 ? 0.5199 0.3620 0.5366 -0.0027 -0.0510 -0.0381 524  ALA   A C    
907  O  O    . ALA   A 146 ? 0.5289 0.3672 0.5504 -0.0105 -0.0503 -0.0321 524  ALA   A O    
908  C  CB   . ALA   A 146 ? 0.5002 0.3714 0.5208 0.0061  -0.0382 -0.0353 524  ALA   A CB   
909  N  N    . GLN   A 147 ? 0.5036 0.3316 0.5102 0.0036  -0.0573 -0.0451 525  GLN   A N    
910  C  CA   . GLN   A 147 ? 0.5575 0.3624 0.5584 0.0006  -0.0649 -0.0460 525  GLN   A CA   
911  C  C    . GLN   A 147 ? 0.6224 0.4232 0.6298 -0.0121 -0.0692 -0.0432 525  GLN   A C    
912  O  O    . GLN   A 147 ? 0.6062 0.3917 0.6129 -0.0193 -0.0733 -0.0396 525  GLN   A O    
913  C  CB   . GLN   A 147 ? 0.6073 0.3982 0.5958 0.0104  -0.0715 -0.0553 525  GLN   A CB   
914  C  CG   . GLN   A 147 ? 0.7383 0.5245 0.7191 0.0219  -0.0700 -0.0573 525  GLN   A CG   
915  C  CD   . GLN   A 147 ? 0.8501 0.6250 0.8187 0.0332  -0.0759 -0.0673 525  GLN   A CD   
916  O  OE1  . GLN   A 147 ? 0.8652 0.6504 0.8296 0.0443  -0.0724 -0.0714 525  GLN   A OE1  
917  N  NE2  . GLN   A 147 ? 0.7931 0.5463 0.7553 0.0303  -0.0851 -0.0713 525  GLN   A NE2  
918  N  N    . TYR   A 148 ? 0.5263 0.3409 0.5398 -0.0154 -0.0685 -0.0443 526  TYR   A N    
919  C  CA   . TYR   A 148 ? 0.5285 0.3405 0.5479 -0.0266 -0.0738 -0.0431 526  TYR   A CA   
920  C  C    . TYR   A 148 ? 0.5790 0.4101 0.6124 -0.0353 -0.0682 -0.0360 526  TYR   A C    
921  O  O    . TYR   A 148 ? 0.5139 0.3432 0.5538 -0.0461 -0.0716 -0.0327 526  TYR   A O    
922  C  CB   . TYR   A 148 ? 0.5481 0.3589 0.5628 -0.0237 -0.0798 -0.0510 526  TYR   A CB   
923  C  CG   . TYR   A 148 ? 0.5777 0.3652 0.5786 -0.0180 -0.0880 -0.0585 526  TYR   A CG   
924  C  CD1  . TYR   A 148 ? 0.6011 0.3859 0.5917 -0.0046 -0.0866 -0.0641 526  TYR   A CD1  
925  C  CD2  . TYR   A 148 ? 0.5930 0.3615 0.5911 -0.0259 -0.0975 -0.0600 526  TYR   A CD2  
926  C  CE1  . TYR   A 148 ? 0.6157 0.3793 0.5932 0.0021  -0.0941 -0.0716 526  TYR   A CE1  
927  C  CE2  . TYR   A 148 ? 0.6748 0.4200 0.6592 -0.0200 -0.1057 -0.0674 526  TYR   A CE2  
928  C  CZ   . TYR   A 148 ? 0.6618 0.4046 0.6357 -0.0053 -0.1039 -0.0735 526  TYR   A CZ   
929  O  OH   . TYR   A 148 ? 0.6916 0.4113 0.6516 0.0019  -0.1121 -0.0815 526  TYR   A OH   
930  N  N    . ILE   A 149 ? 0.5063 0.3559 0.5446 -0.0309 -0.0599 -0.0337 527  ILE   A N    
931  C  CA   . ILE   A 149 ? 0.5542 0.4222 0.6052 -0.0374 -0.0546 -0.0280 527  ILE   A CA   
932  C  C    . ILE   A 149 ? 0.5453 0.4218 0.5984 -0.0344 -0.0461 -0.0231 527  ILE   A C    
933  O  O    . ILE   A 149 ? 0.5044 0.3749 0.5498 -0.0270 -0.0444 -0.0243 527  ILE   A O    
934  C  CB   . ILE   A 149 ? 0.5091 0.3926 0.5647 -0.0356 -0.0543 -0.0307 527  ILE   A CB   
935  C  CG1  . ILE   A 149 ? 0.4371 0.3278 0.4870 -0.0250 -0.0499 -0.0336 527  ILE   A CG1  
936  C  CG2  . ILE   A 149 ? 0.4938 0.3698 0.5468 -0.0384 -0.0629 -0.0359 527  ILE   A CG2  
937  C  CD1  . ILE   A 149 ? 0.4336 0.3417 0.4896 -0.0242 -0.0476 -0.0334 527  ILE   A CD1  
938  N  N    . GLU   A 150 ? 0.5204 0.4116 0.5841 -0.0399 -0.0412 -0.0177 528  GLU   A N    
939  C  CA   . GLU   A 150 ? 0.4924 0.3931 0.5587 -0.0377 -0.0332 -0.0132 528  GLU   A CA   
940  C  C    . GLU   A 150 ? 0.5275 0.4441 0.5971 -0.0324 -0.0290 -0.0146 528  GLU   A C    
941  O  O    . GLU   A 150 ? 0.4820 0.4086 0.5584 -0.0349 -0.0300 -0.0152 528  GLU   A O    
942  C  CB   . GLU   A 150 ? 0.6010 0.5075 0.6759 -0.0469 -0.0303 -0.0065 528  GLU   A CB   
943  C  CG   . GLU   A 150 ? 0.6551 0.5738 0.7333 -0.0446 -0.0221 -0.0025 528  GLU   A CG   
944  C  CD   . GLU   A 150 ? 0.7423 0.6511 0.8136 -0.0432 -0.0200 0.0004  528  GLU   A CD   
945  O  OE1  . GLU   A 150 ? 0.7995 0.7169 0.8722 -0.0412 -0.0137 0.0034  528  GLU   A OE1  
946  O  OE2  . GLU   A 150 ? 0.8152 0.7071 0.8796 -0.0440 -0.0251 -0.0003 528  GLU   A OE2  
947  N  N    . PHE   A 151 ? 0.4706 0.3891 0.5350 -0.0251 -0.0247 -0.0151 529  PHE   A N    
948  C  CA   . PHE   A 151 ? 0.4391 0.3712 0.5058 -0.0208 -0.0204 -0.0152 529  PHE   A CA   
949  C  C    . PHE   A 151 ? 0.4641 0.4048 0.5360 -0.0224 -0.0139 -0.0102 529  PHE   A C    
950  O  O    . PHE   A 151 ? 0.4470 0.3824 0.5164 -0.0231 -0.0117 -0.0075 529  PHE   A O    
951  C  CB   . PHE   A 151 ? 0.4406 0.3709 0.4983 -0.0125 -0.0199 -0.0187 529  PHE   A CB   
952  C  CG   . PHE   A 151 ? 0.4283 0.3548 0.4806 -0.0092 -0.0252 -0.0244 529  PHE   A CG   
953  C  CD1  . PHE   A 151 ? 0.4043 0.3398 0.4587 -0.0086 -0.0261 -0.0259 529  PHE   A CD1  
954  C  CD2  . PHE   A 151 ? 0.4570 0.3702 0.5011 -0.0061 -0.0296 -0.0283 529  PHE   A CD2  
955  C  CE1  . PHE   A 151 ? 0.4448 0.3771 0.4930 -0.0054 -0.0310 -0.0311 529  PHE   A CE1  
956  C  CE2  . PHE   A 151 ? 0.4538 0.3634 0.4916 -0.0024 -0.0345 -0.0343 529  PHE   A CE2  
957  C  CZ   . PHE   A 151 ? 0.4585 0.3780 0.4982 -0.0023 -0.0351 -0.0356 529  PHE   A CZ   
958  N  N    . SER   A 152 ? 0.4259 0.3793 0.5043 -0.0225 -0.0112 -0.0092 530  SER   A N    
959  C  CA   . SER   A 152 ? 0.4065 0.3678 0.4875 -0.0215 -0.0051 -0.0059 530  SER   A CA   
960  C  C    . SER   A 152 ? 0.3958 0.3548 0.4689 -0.0155 -0.0027 -0.0066 530  SER   A C    
961  O  O    . SER   A 152 ? 0.3999 0.3545 0.4666 -0.0114 -0.0052 -0.0098 530  SER   A O    
962  C  CB   . SER   A 152 ? 0.3776 0.3513 0.4657 -0.0212 -0.0038 -0.0057 530  SER   A CB   
963  O  OG   . SER   A 152 ? 0.3641 0.3393 0.4478 -0.0158 -0.0046 -0.0081 530  SER   A OG   
964  N  N    . LYS   A 153 ? 0.4148 0.3777 0.4884 -0.0149 0.0022  -0.0037 531  LYS   A N    
965  C  CA   . LYS   A 153 ? 0.3486 0.3130 0.4167 -0.0100 0.0046  -0.0041 531  LYS   A CA   
966  C  C    . LYS   A 153 ? 0.3739 0.3438 0.4421 -0.0074 0.0033  -0.0062 531  LYS   A C    
967  O  O    . LYS   A 153 ? 0.3885 0.3632 0.4624 -0.0091 0.0021  -0.0063 531  LYS   A O    
968  C  CB   . LYS   A 153 ? 0.3860 0.3546 0.4552 -0.0105 0.0095  -0.0010 531  LYS   A CB   
969  C  CG   . LYS   A 153 ? 0.3972 0.3603 0.4641 -0.0123 0.0110  0.0014  531  LYS   A CG   
970  C  CD   . LYS   A 153 ? 0.4317 0.3892 0.4910 -0.0083 0.0103  0.0005  531  LYS   A CD   
971  C  CE   . LYS   A 153 ? 0.4480 0.3990 0.5043 -0.0098 0.0110  0.0033  531  LYS   A CE   
972  N  NZ   . LYS   A 153 ? 0.4049 0.3470 0.4616 -0.0131 0.0074  0.0036  531  LYS   A NZ   
973  N  N    . PRO   A 154 ? 0.3752 0.3453 0.4372 -0.0034 0.0034  -0.0073 532  PRO   A N    
974  C  CA   . PRO   A 154 ? 0.3830 0.3572 0.4436 -0.0014 0.0015  -0.0089 532  PRO   A CA   
975  C  C    . PRO   A 154 ? 0.4228 0.4029 0.4878 -0.0021 0.0030  -0.0069 532  PRO   A C    
976  O  O    . PRO   A 154 ? 0.3975 0.3791 0.4628 -0.0021 0.0064  -0.0048 532  PRO   A O    
977  C  CB   . PRO   A 154 ? 0.3570 0.3318 0.4101 0.0023  0.0023  -0.0095 532  PRO   A CB   
978  C  CG   . PRO   A 154 ? 0.3992 0.3686 0.4498 0.0032  0.0030  -0.0098 532  PRO   A CG   
979  C  CD   . PRO   A 154 ? 0.3697 0.3369 0.4256 -0.0006 0.0048  -0.0072 532  PRO   A CD   
980  N  N    . PHE   A 155 ? 0.3790 0.3620 0.4471 -0.0023 0.0001  -0.0079 533  PHE   A N    
981  C  CA   . PHE   A 155 ? 0.3704 0.3581 0.4416 -0.0016 0.0006  -0.0064 533  PHE   A CA   
982  C  C    . PHE   A 155 ? 0.3785 0.3666 0.4431 0.0007  -0.0002 -0.0058 533  PHE   A C    
983  O  O    . PHE   A 155 ? 0.3850 0.3745 0.4503 0.0016  0.0002  -0.0042 533  PHE   A O    
984  C  CB   . PHE   A 155 ? 0.3851 0.3772 0.4639 -0.0028 -0.0022 -0.0072 533  PHE   A CB   
985  C  CG   . PHE   A 155 ? 0.4020 0.3940 0.4788 -0.0023 -0.0072 -0.0094 533  PHE   A CG   
986  C  CD1  . PHE   A 155 ? 0.3787 0.3721 0.4511 0.0003  -0.0093 -0.0092 533  PHE   A CD1  
987  C  CD2  . PHE   A 155 ? 0.3859 0.3762 0.4650 -0.0048 -0.0103 -0.0116 533  PHE   A CD2  
988  C  CE1  . PHE   A 155 ? 0.3752 0.3692 0.4452 0.0008  -0.0140 -0.0112 533  PHE   A CE1  
989  C  CE2  . PHE   A 155 ? 0.4021 0.3921 0.4786 -0.0043 -0.0154 -0.0142 533  PHE   A CE2  
990  C  CZ   . PHE   A 155 ? 0.3925 0.3849 0.4644 -0.0012 -0.0170 -0.0141 533  PHE   A CZ   
991  N  N    . LYS   A 156 ? 0.3689 0.3557 0.4269 0.0019  -0.0012 -0.0071 534  LYS   A N    
992  C  CA   . LYS   A 156 ? 0.3812 0.3699 0.4326 0.0032  -0.0015 -0.0058 534  LYS   A CA   
993  C  C    . LYS   A 156 ? 0.4173 0.4065 0.4625 0.0045  -0.0003 -0.0068 534  LYS   A C    
994  O  O    . LYS   A 156 ? 0.3931 0.3806 0.4371 0.0058  -0.0018 -0.0099 534  LYS   A O    
995  C  CB   . LYS   A 156 ? 0.3847 0.3753 0.4349 0.0039  -0.0056 -0.0065 534  LYS   A CB   
996  C  CG   . LYS   A 156 ? 0.3991 0.3919 0.4413 0.0047  -0.0061 -0.0047 534  LYS   A CG   
997  C  CD   . LYS   A 156 ? 0.4586 0.4504 0.4999 0.0036  -0.0047 -0.0007 534  LYS   A CD   
998  C  CE   . LYS   A 156 ? 0.5259 0.5201 0.5588 0.0030  -0.0056 0.0020  534  LYS   A CE   
999  N  NZ   . LYS   A 156 ? 0.4819 0.4736 0.5123 0.0010  -0.0049 0.0062  534  LYS   A NZ   
1000 N  N    . TYR   A 157 ? 0.3766 0.3680 0.4181 0.0043  0.0022  -0.0044 535  TYR   A N    
1001 C  CA   . TYR   A 157 ? 0.4201 0.4150 0.4562 0.0059  0.0036  -0.0050 535  TYR   A CA   
1002 C  C    . TYR   A 157 ? 0.4134 0.4139 0.4436 0.0060  0.0026  -0.0037 535  TYR   A C    
1003 O  O    . TYR   A 157 ? 0.3793 0.3801 0.4087 0.0037  0.0023  -0.0003 535  TYR   A O    
1004 C  CB   . TYR   A 157 ? 0.4089 0.4044 0.4450 0.0049  0.0068  -0.0028 535  TYR   A CB   
1005 C  CG   . TYR   A 157 ? 0.4103 0.4009 0.4507 0.0048  0.0081  -0.0035 535  TYR   A CG   
1006 C  CD1  . TYR   A 157 ? 0.3854 0.3727 0.4307 0.0028  0.0088  -0.0023 535  TYR   A CD1  
1007 C  CD2  . TYR   A 157 ? 0.4259 0.4154 0.4651 0.0070  0.0086  -0.0053 535  TYR   A CD2  
1008 C  CE1  . TYR   A 157 ? 0.4491 0.4330 0.4977 0.0021  0.0103  -0.0024 535  TYR   A CE1  
1009 C  CE2  . TYR   A 157 ? 0.3745 0.3587 0.4167 0.0063  0.0095  -0.0052 535  TYR   A CE2  
1010 C  CZ   . TYR   A 157 ? 0.4016 0.3835 0.4484 0.0034  0.0105  -0.0035 535  TYR   A CZ   
1011 O  OH   . TYR   A 157 ? 0.3718 0.3496 0.4210 0.0023  0.0118  -0.0029 535  TYR   A OH   
1012 N  N    . GLN   A 158 ? 0.3604 0.3650 0.3860 0.0088  0.0019  -0.0065 536  GLN   A N    
1013 C  CA   . GLN   A 158 ? 0.3965 0.4079 0.4156 0.0091  0.0011  -0.0055 536  GLN   A CA   
1014 C  C    . GLN   A 158 ? 0.4164 0.4341 0.4306 0.0133  0.0019  -0.0091 536  GLN   A C    
1015 O  O    . GLN   A 158 ? 0.4064 0.4254 0.4217 0.0152  0.0040  -0.0101 536  GLN   A O    
1016 C  CB   . GLN   A 158 ? 0.3853 0.3939 0.4041 0.0087  -0.0027 -0.0059 536  GLN   A CB   
1017 C  CG   . GLN   A 158 ? 0.3813 0.3852 0.4022 0.0110  -0.0057 -0.0110 536  GLN   A CG   
1018 C  CD   . GLN   A 158 ? 0.3959 0.4031 0.4100 0.0135  -0.0086 -0.0141 536  GLN   A CD   
1019 O  OE1  . GLN   A 158 ? 0.4538 0.4640 0.4643 0.0125  -0.0104 -0.0120 536  GLN   A OE1  
1020 N  NE2  . GLN   A 158 ? 0.3835 0.3888 0.3955 0.0170  -0.0096 -0.0194 536  GLN   A NE2  
1021 N  N    . GLY   A 159 ? 0.3853 0.4073 0.3937 0.0154  0.0001  -0.0111 537  GLY   A N    
1022 C  CA   . GLY   A 159 ? 0.4057 0.4346 0.4088 0.0205  0.0010  -0.0151 537  GLY   A CA   
1023 C  C    . GLY   A 159 ? 0.4425 0.4762 0.4383 0.0226  -0.0011 -0.0173 537  GLY   A C    
1024 O  O    . GLY   A 159 ? 0.4508 0.4806 0.4462 0.0203  -0.0041 -0.0164 537  GLY   A O    
1025 N  N    . LEU   A 160 ? 0.3840 0.4270 0.3738 0.0274  0.0004  -0.0205 538  LEU   A N    
1026 C  CA   . LEU   A 160 ? 0.4450 0.4941 0.4265 0.0300  -0.0013 -0.0231 538  LEU   A CA   
1027 C  C    . LEU   A 160 ? 0.4245 0.4888 0.4010 0.0277  0.0021  -0.0179 538  LEU   A C    
1028 O  O    . LEU   A 160 ? 0.4120 0.4856 0.3902 0.0274  0.0060  -0.0156 538  LEU   A O    
1029 C  CB   . LEU   A 160 ? 0.3972 0.4460 0.3738 0.0381  -0.0025 -0.0313 538  LEU   A CB   
1030 C  CG   . LEU   A 160 ? 0.4763 0.5090 0.4565 0.0401  -0.0064 -0.0365 538  LEU   A CG   
1031 C  CD1  . LEU   A 160 ? 0.4135 0.4457 0.3866 0.0484  -0.0082 -0.0446 538  LEU   A CD1  
1032 C  CD2  . LEU   A 160 ? 0.3959 0.4186 0.3789 0.0356  -0.0108 -0.0358 538  LEU   A CD2  
1033 N  N    . THR   A 161 ? 0.4527 0.5200 0.4232 0.0256  0.0004  -0.0158 539  THR   A N    
1034 C  CA   . THR   A 161 ? 0.4271 0.5088 0.3915 0.0225  0.0031  -0.0104 539  THR   A CA   
1035 C  C    . THR   A 161 ? 0.4759 0.5623 0.4304 0.0253  0.0009  -0.0131 539  THR   A C    
1036 O  O    . THR   A 161 ? 0.4197 0.4983 0.3725 0.0299  -0.0028 -0.0197 539  THR   A O    
1037 C  CB   . THR   A 161 ? 0.4690 0.5470 0.4366 0.0142  0.0030  -0.0017 539  THR   A CB   
1038 O  OG1  . THR   A 161 ? 0.5519 0.6439 0.5140 0.0100  0.0059  0.0044  539  THR   A OG1  
1039 C  CG2  . THR   A 161 ? 0.4321 0.4986 0.3992 0.0120  -0.0019 -0.0004 539  THR   A CG2  
1040 N  N    . ILE   A 162 ? 0.4422 0.5416 0.3896 0.0221  0.0028  -0.0078 540  ILE   A N    
1041 C  CA   . ILE   A 162 ? 0.4989 0.6055 0.4354 0.0247  0.0014  -0.0098 540  ILE   A CA   
1042 C  C    . ILE   A 162 ? 0.5176 0.6230 0.4497 0.0174  -0.0007 -0.0015 540  ILE   A C    
1043 O  O    . ILE   A 162 ? 0.5036 0.6128 0.4371 0.0106  0.0015  0.0067  540  ILE   A O    
1044 C  CB   . ILE   A 162 ? 0.4786 0.6053 0.4083 0.0292  0.0062  -0.0121 540  ILE   A CB   
1045 C  CG1  . ILE   A 162 ? 0.5507 0.6773 0.4839 0.0379  0.0075  -0.0210 540  ILE   A CG1  
1046 C  CG2  . ILE   A 162 ? 0.5377 0.6726 0.4548 0.0316  0.0050  -0.0138 540  ILE   A CG2  
1047 C  CD1  . ILE   A 162 ? 0.5719 0.7154 0.5079 0.0392  0.0134  -0.0195 540  ILE   A CD1  
1048 N  N    . LEU   A 163 ? 0.4753 0.5748 0.4017 0.0188  -0.0055 -0.0035 541  LEU   A N    
1049 C  CA   . LEU   A 163 ? 0.5089 0.6059 0.4299 0.0130  -0.0086 0.0040  541  LEU   A CA   
1050 C  C    . LEU   A 163 ? 0.5327 0.6435 0.4401 0.0145  -0.0080 0.0041  541  LEU   A C    
1051 O  O    . LEU   A 163 ? 0.4744 0.5881 0.3765 0.0214  -0.0090 -0.0041 541  LEU   A O    
1052 C  CB   . LEU   A 163 ? 0.5365 0.6171 0.4616 0.0133  -0.0150 0.0022  541  LEU   A CB   
1053 C  CG   . LEU   A 163 ? 0.5445 0.6204 0.4647 0.0089  -0.0197 0.0091  541  LEU   A CG   
1054 C  CD1  . LEU   A 163 ? 0.5005 0.5667 0.4287 0.0035  -0.0201 0.0158  541  LEU   A CD1  
1055 C  CD2  . LEU   A 163 ? 0.5567 0.6243 0.4761 0.0123  -0.0261 0.0040  541  LEU   A CD2  
1056 N  N    . VAL   A 164 ? 0.5321 0.6512 0.4332 0.0080  -0.0065 0.0134  542  VAL   A N    
1057 C  CA   . VAL   A 164 ? 0.5034 0.6366 0.3907 0.0082  -0.0057 0.0152  542  VAL   A CA   
1058 C  C    . VAL   A 164 ? 0.5587 0.6862 0.4400 0.0007  -0.0096 0.0253  542  VAL   A C    
1059 O  O    . VAL   A 164 ? 0.5543 0.6685 0.4423 -0.0044 -0.0122 0.0308  542  VAL   A O    
1060 C  CB   . VAL   A 164 ? 0.5563 0.7115 0.4402 0.0078  0.0017  0.0169  542  VAL   A CB   
1061 C  CG1  . VAL   A 164 ? 0.5092 0.6691 0.3992 0.0162  0.0050  0.0069  542  VAL   A CG1  
1062 C  CG2  . VAL   A 164 ? 0.5241 0.6815 0.4125 -0.0020 0.0042  0.0276  542  VAL   A CG2  
1063 N  N    . LYS   A 165 ? 0.5787 0.7158 0.4464 0.0005  -0.0103 0.0274  543  LYS   A N    
1064 C  CA   . LYS   A 165 ? 0.6304 0.7640 0.4899 -0.0068 -0.0139 0.0380  543  LYS   A CA   
1065 C  C    . LYS   A 165 ? 0.6832 0.8268 0.5412 -0.0157 -0.0092 0.0485  543  LYS   A C    
1066 O  O    . LYS   A 165 ? 0.6559 0.8179 0.5132 -0.0154 -0.0026 0.0476  543  LYS   A O    
1067 C  CB   . LYS   A 165 ? 0.6077 0.7491 0.4522 -0.0040 -0.0162 0.0368  543  LYS   A CB   
1068 C  CG   . LYS   A 165 ? 0.6835 0.8297 0.5159 -0.0122 -0.0172 0.0491  543  LYS   A CG   
1069 C  CD   . LYS   A 165 ? 0.7327 0.8603 0.5630 -0.0146 -0.0257 0.0541  543  LYS   A CD   
1070 C  CE   . LYS   A 165 ? 0.7756 0.9030 0.5961 -0.0087 -0.0309 0.0486  543  LYS   A CE   
1071 N  NZ   . LYS   A 165 ? 0.7157 0.8236 0.5399 -0.0079 -0.0397 0.0493  543  LYS   A NZ   
1072 N  N    . LYS   A 166 ? 0.6757 0.8069 0.5336 -0.0236 -0.0130 0.0584  544  LYS   A N    
1073 C  CA   . LYS   A 166 ? 0.7155 0.8532 0.5716 -0.0336 -0.0098 0.0692  544  LYS   A CA   
1074 C  C    . LYS   A 166 ? 0.6871 0.8478 0.5303 -0.0364 -0.0054 0.0735  544  LYS   A C    
1075 O  O    . LYS   A 166 ? 0.6626 0.8262 0.4938 -0.0350 -0.0080 0.0744  544  LYS   A O    
1076 C  CB   . LYS   A 166 ? 0.7085 0.8269 0.5628 -0.0409 -0.0162 0.0791  544  LYS   A CB   
1077 C  CG   . LYS   A 166 ? 0.7333 0.8502 0.5905 -0.0511 -0.0143 0.0885  544  LYS   A CG   
1078 C  CD   . LYS   A 166 ? 0.8014 0.8955 0.6561 -0.0569 -0.0218 0.0971  544  LYS   A CD   
1079 C  CE   . LYS   A 166 ? 0.8967 0.9870 0.7533 -0.0674 -0.0209 0.1061  544  LYS   A CE   
1080 N  NZ   . LYS   A 166 ? 0.9690 1.0360 0.8208 -0.0729 -0.0287 0.1148  544  LYS   A NZ   
1081 N  N    . GLY   A 167 ? 0.7663 0.9450 0.6122 -0.0401 0.0015  0.0757  545  GLY   A N    
1082 C  CA   . GLY   A 167 ? 0.8661 1.0711 0.7019 -0.0422 0.0072  0.0788  545  GLY   A CA   
1083 C  C    . GLY   A 167 ? 0.8798 1.1043 0.7188 -0.0322 0.0135  0.0675  545  GLY   A C    
1084 O  O    . GLY   A 167 ? 0.9460 1.1956 0.7813 -0.0340 0.0200  0.0698  545  GLY   A O    
1085 N  N    . THR   A 168 ? 0.7838 0.9973 0.6293 -0.0217 0.0115  0.0556  546  THR   A N    
1086 C  CA   . THR   A 168 ? 0.7416 0.9695 0.5902 -0.0113 0.0163  0.0442  546  THR   A CA   
1087 C  C    . THR   A 168 ? 0.7245 0.9602 0.5856 -0.0131 0.0213  0.0447  546  THR   A C    
1088 O  O    . THR   A 168 ? 0.7721 0.9913 0.6436 -0.0170 0.0190  0.0469  546  THR   A O    
1089 C  CB   . THR   A 168 ? 0.6725 0.8831 0.5242 -0.0009 0.0116  0.0322  546  THR   A CB   
1090 O  OG1  . THR   A 168 ? 0.6482 0.8554 0.4874 0.0012  0.0071  0.0311  546  THR   A OG1  
1091 C  CG2  . THR   A 168 ? 0.6623 0.8826 0.5181 0.0101  0.0155  0.0200  546  THR   A CG2  
1092 N  N    . ARG   A 169 ? 0.6519 0.9137 0.5117 -0.0102 0.0282  0.0426  663  ARG   A N    
1093 C  CA   . ARG   A 169 ? 0.6839 0.9575 0.5549 -0.0125 0.0331  0.0440  663  ARG   A CA   
1094 C  C    . ARG   A 169 ? 0.6847 0.9637 0.5617 0.0010  0.0356  0.0308  663  ARG   A C    
1095 O  O    . ARG   A 169 ? 0.6667 0.9670 0.5379 0.0086  0.0400  0.0252  663  ARG   A O    
1096 C  CB   . ARG   A 169 ? 0.6563 0.9579 0.5226 -0.0209 0.0389  0.0536  663  ARG   A CB   
1097 N  N    . ILE   A 170 ? 0.6376 0.8969 0.5255 0.0041  0.0327  0.0259  664  ILE   A N    
1098 C  CA   . ILE   A 170 ? 0.6235 0.8861 0.5189 0.0150  0.0348  0.0153  664  ILE   A CA   
1099 C  C    . ILE   A 170 ? 0.6381 0.8932 0.5471 0.0102  0.0351  0.0186  664  ILE   A C    
1100 O  O    . ILE   A 170 ? 0.6329 0.8691 0.5457 0.0022  0.0313  0.0245  664  ILE   A O    
1101 C  CB   . ILE   A 170 ? 0.6476 0.8916 0.5412 0.0257  0.0302  0.0037  664  ILE   A CB   
1102 C  CG1  . ILE   A 170 ? 0.6701 0.8853 0.5700 0.0215  0.0241  0.0052  664  ILE   A CG1  
1103 C  CG2  . ILE   A 170 ? 0.6769 0.9265 0.5561 0.0300  0.0290  0.0004  664  ILE   A CG2  
1104 C  CD1  . ILE   A 170 ? 0.6800 0.8779 0.5800 0.0307  0.0195  -0.0055 664  ILE   A CD1  
1105 N  N    . THR   A 171 ? 0.5694 0.8393 0.4851 0.0158  0.0393  0.0143  665  THR   A N    
1106 C  CA   . THR   A 171 ? 0.6023 0.8676 0.5302 0.0114  0.0397  0.0173  665  THR   A CA   
1107 C  C    . THR   A 171 ? 0.6383 0.8766 0.5729 0.0162  0.0352  0.0110  665  THR   A C    
1108 O  O    . THR   A 171 ? 0.5776 0.8030 0.5201 0.0099  0.0335  0.0153  665  THR   A O    
1109 C  CB   . THR   A 171 ? 0.5855 0.8764 0.5186 0.0164  0.0453  0.0148  665  THR   A CB   
1110 O  OG1  . THR   A 171 ? 0.5083 0.7972 0.4413 0.0311  0.0451  0.0025  665  THR   A OG1  
1111 C  CG2  . THR   A 171 ? 0.5594 0.8806 0.4856 0.0129  0.0505  0.0200  665  THR   A CG2  
1112 N  N    . GLY   A 172 ? 0.5950 0.8249 0.5264 0.0270  0.0331  0.0009  666  GLY   A N    
1113 C  CA   . GLY   A 172 ? 0.5986 0.8048 0.5365 0.0315  0.0290  -0.0051 666  GLY   A CA   
1114 C  C    . GLY   A 172 ? 0.4805 0.6855 0.4153 0.0448  0.0282  -0.0170 666  GLY   A C    
1115 O  O    . GLY   A 172 ? 0.4982 0.7151 0.4238 0.0506  0.0293  -0.0213 666  GLY   A O    
1116 N  N    . ILE   A 173 ? 0.4877 0.6778 0.4299 0.0494  0.0261  -0.0221 667  ILE   A N    
1117 C  CA   . ILE   A 173 ? 0.5096 0.6934 0.4488 0.0616  0.0241  -0.0333 667  ILE   A CA   
1118 C  C    . ILE   A 173 ? 0.5303 0.7373 0.4658 0.0711  0.0284  -0.0384 667  ILE   A C    
1119 O  O    . ILE   A 173 ? 0.5354 0.7405 0.4643 0.0820  0.0268  -0.0480 667  ILE   A O    
1120 C  CB   . ILE   A 173 ? 0.4797 0.6428 0.4275 0.0635  0.0210  -0.0363 667  ILE   A CB   
1121 C  CG1  . ILE   A 173 ? 0.5102 0.6588 0.4531 0.0737  0.0166  -0.0471 667  ILE   A CG1  
1122 C  CG2  . ILE   A 173 ? 0.4967 0.6701 0.4527 0.0646  0.0245  -0.0345 667  ILE   A CG2  
1123 C  CD1  . ILE   A 173 ? 0.5087 0.6371 0.4491 0.0700  0.0110  -0.0481 667  ILE   A CD1  
1124 N  N    . ASN   A 174 ? 0.5146 0.7441 0.4538 0.0674  0.0337  -0.0323 668  ASN   A N    
1125 C  CA   . ASN   A 174 ? 0.5077 0.7627 0.4450 0.0767  0.0382  -0.0368 668  ASN   A CA   
1126 C  C    . ASN   A 174 ? 0.5558 0.8349 0.4840 0.0751  0.0423  -0.0341 668  ASN   A C    
1127 O  O    . ASN   A 174 ? 0.5507 0.8561 0.4778 0.0813  0.0472  -0.0362 668  ASN   A O    
1128 C  CB   . ASN   A 174 ? 0.4812 0.7483 0.4294 0.0747  0.0414  -0.0327 668  ASN   A CB   
1129 C  CG   . ASN   A 174 ? 0.5496 0.7940 0.5054 0.0775  0.0376  -0.0359 668  ASN   A CG   
1130 O  OD1  . ASN   A 174 ? 0.5648 0.7929 0.5175 0.0869  0.0338  -0.0447 668  ASN   A OD1  
1131 N  ND2  . ASN   A 174 ? 0.5552 0.7967 0.5202 0.0686  0.0379  -0.0286 668  ASN   A ND2  
1132 N  N    . ASP   A 175 ? 0.5328 0.8043 0.4543 0.0674  0.0403  -0.0294 669  ASP   A N    
1133 C  CA   . ASP   A 175 ? 0.5156 0.8087 0.4271 0.0652  0.0438  -0.0261 669  ASP   A CA   
1134 C  C    . ASP   A 175 ? 0.5811 0.8836 0.4826 0.0796  0.0445  -0.0377 669  ASP   A C    
1135 O  O    . ASP   A 175 ? 0.5363 0.8182 0.4345 0.0879  0.0395  -0.0471 669  ASP   A O    
1136 C  CB   . ASP   A 175 ? 0.5707 0.8493 0.4766 0.0547  0.0402  -0.0192 669  ASP   A CB   
1137 C  CG   . ASP   A 175 ? 0.5863 0.8869 0.4827 0.0488  0.0438  -0.0122 669  ASP   A CG   
1138 O  OD1  . ASP   A 175 ? 0.5615 0.8716 0.4465 0.0560  0.0445  -0.0179 669  ASP   A OD1  
1139 O  OD2  . ASP   A 175 ? 0.5724 0.8805 0.4724 0.0366  0.0458  -0.0007 669  ASP   A OD2  
1140 N  N    . PRO   A 176 ? 0.5861 0.9195 0.4821 0.0828  0.0504  -0.0374 670  PRO   A N    
1141 C  CA   . PRO   A 176 ? 0.5441 0.8872 0.4290 0.0974  0.0512  -0.0491 670  PRO   A CA   
1142 C  C    . PRO   A 176 ? 0.5906 0.9154 0.4629 0.0996  0.0459  -0.0542 670  PRO   A C    
1143 O  O    . PRO   A 176 ? 0.5571 0.8764 0.4219 0.1128  0.0436  -0.0665 670  PRO   A O    
1144 C  CB   . PRO   A 176 ? 0.5827 0.9647 0.4641 0.0963  0.0592  -0.0444 670  PRO   A CB   
1145 C  CG   . PRO   A 176 ? 0.5451 0.9379 0.4399 0.0858  0.0624  -0.0340 670  PRO   A CG   
1146 C  CD   . PRO   A 176 ? 0.4267 0.7888 0.3274 0.0741  0.0568  -0.0272 670  PRO   A CD   
1147 N  N    . ARG   A 177 ? 0.5489 0.8636 0.4181 0.0874  0.0435  -0.0455 671  ARG   A N    
1148 C  CA   . ARG   A 177 ? 0.5691 0.8671 0.4268 0.0896  0.0379  -0.0504 671  ARG   A CA   
1149 C  C    . ARG   A 177 ? 0.5987 0.8641 0.4609 0.0935  0.0304  -0.0579 671  ARG   A C    
1150 O  O    . ARG   A 177 ? 0.5912 0.8417 0.4446 0.0972  0.0250  -0.0642 671  ARG   A O    
1151 C  CB   . ARG   A 177 ? 0.5870 0.8843 0.4404 0.0758  0.0370  -0.0385 671  ARG   A CB   
1152 C  CG   . ARG   A 177 ? 0.6365 0.9660 0.4825 0.0716  0.0439  -0.0312 671  ARG   A CG   
1153 C  CD   . ARG   A 177 ? 0.6666 0.9935 0.5141 0.0552  0.0434  -0.0162 671  ARG   A CD   
1154 N  NE   . ARG   A 177 ? 0.6965 1.0162 0.5310 0.0515  0.0395  -0.0136 671  ARG   A NE   
1155 C  CZ   . ARG   A 177 ? 0.7000 1.0136 0.5330 0.0385  0.0375  -0.0013 671  ARG   A CZ   
1156 N  NH1  . ARG   A 177 ? 0.6376 0.9484 0.4813 0.0278  0.0385  0.0087  671  ARG   A NH1  
1157 N  NH2  . ARG   A 177 ? 0.7235 1.0324 0.5436 0.0365  0.0339  0.0006  671  ARG   A NH2  
1158 N  N    . LEU   A 178 ? 0.5736 0.8282 0.4490 0.0925  0.0299  -0.0570 672  LEU   A N    
1159 C  CA   . LEU   A 178 ? 0.5750 0.8010 0.4550 0.0967  0.0235  -0.0641 672  LEU   A CA   
1160 C  C    . LEU   A 178 ? 0.6001 0.8265 0.4805 0.1107  0.0237  -0.0753 672  LEU   A C    
1161 O  O    . LEU   A 178 ? 0.5846 0.7925 0.4598 0.1187  0.0181  -0.0853 672  LEU   A O    
1162 C  CB   . LEU   A 178 ? 0.5439 0.7548 0.4373 0.0861  0.0221  -0.0557 672  LEU   A CB   
1163 C  CG   . LEU   A 178 ? 0.5837 0.7785 0.4773 0.0751  0.0178  -0.0487 672  LEU   A CG   
1164 C  CD1  . LEU   A 178 ? 0.5674 0.7788 0.4534 0.0678  0.0206  -0.0404 672  LEU   A CD1  
1165 C  CD2  . LEU   A 178 ? 0.5603 0.7413 0.4673 0.0667  0.0170  -0.0419 672  LEU   A CD2  
1166 N  N    . ARG   A 179 ? 0.5983 0.8457 0.4843 0.1141  0.0295  -0.0740 673  ARG   A N    
1167 C  CA   . ARG   A 179 ? 0.5936 0.8414 0.4809 0.1281  0.0294  -0.0841 673  ARG   A CA   
1168 C  C    . ARG   A 179 ? 0.5927 0.8557 0.4670 0.1419  0.0308  -0.0946 673  ARG   A C    
1169 O  O    . ARG   A 179 ? 0.6533 0.9071 0.5245 0.1553  0.0278  -0.1059 673  ARG   A O    
1170 C  CB   . ARG   A 179 ? 0.5620 0.8266 0.4615 0.1264  0.0346  -0.0784 673  ARG   A CB   
1171 C  CG   . ARG   A 179 ? 0.5221 0.7695 0.4338 0.1145  0.0327  -0.0697 673  ARG   A CG   
1172 C  CD   . ARG   A 179 ? 0.5697 0.7895 0.4855 0.1202  0.0269  -0.0762 673  ARG   A CD   
1173 N  NE   . ARG   A 179 ? 0.5899 0.7984 0.5178 0.1100  0.0263  -0.0680 673  ARG   A NE   
1174 C  CZ   . ARG   A 179 ? 0.5896 0.7778 0.5236 0.1124  0.0226  -0.0706 673  ARG   A CZ   
1175 N  NH1  . ARG   A 179 ? 0.6316 0.8065 0.5612 0.1241  0.0185  -0.0808 673  ARG   A NH1  
1176 N  NH2  . ARG   A 179 ? 0.6129 0.7944 0.5571 0.1029  0.0229  -0.0627 673  ARG   A NH2  
1177 N  N    . ASN   A 180 ? 0.5835 0.8689 0.4490 0.1395  0.0351  -0.0915 674  ASN   A N    
1178 C  CA   . ASN   A 180 ? 0.6165 0.9163 0.4677 0.1523  0.0364  -0.1017 674  ASN   A CA   
1179 C  C    . ASN   A 180 ? 0.6241 0.9181 0.4631 0.1464  0.0336  -0.1002 674  ASN   A C    
1180 O  O    . ASN   A 180 ? 0.6410 0.9589 0.4732 0.1422  0.0386  -0.0946 674  ASN   A O    
1181 C  CB   . ASN   A 180 ? 0.5907 0.9297 0.4423 0.1568  0.0453  -0.0999 674  ASN   A CB   
1182 C  CG   . ASN   A 180 ? 0.6628 1.0175 0.5000 0.1728  0.0469  -0.1122 674  ASN   A CG   
1183 O  OD1  . ASN   A 180 ? 0.7010 1.0350 0.5296 0.1838  0.0409  -0.1244 674  ASN   A OD1  
1184 N  ND2  . ASN   A 180 ? 0.5664 0.9584 0.4007 0.1741  0.0551  -0.1091 674  ASN   A ND2  
1185 N  N    . PRO   A 181 ? 0.6252 0.8885 0.4609 0.1459  0.0254  -0.1049 675  PRO   A N    
1186 C  CA   . PRO   A 181 ? 0.6551 0.9102 0.4826 0.1373  0.0219  -0.1009 675  PRO   A CA   
1187 C  C    . PRO   A 181 ? 0.7033 0.9683 0.5127 0.1463  0.0214  -0.1095 675  PRO   A C    
1188 O  O    . PRO   A 181 ? 0.6828 0.9534 0.4848 0.1608  0.0218  -0.1215 675  PRO   A O    
1189 C  CB   . PRO   A 181 ? 0.6584 0.8780 0.4909 0.1343  0.0131  -0.1036 675  PRO   A CB   
1190 C  CG   . PRO   A 181 ? 0.6564 0.8651 0.4901 0.1473  0.0107  -0.1153 675  PRO   A CG   
1191 C  CD   . PRO   A 181 ? 0.6244 0.8587 0.4643 0.1524  0.0187  -0.1135 675  PRO   A CD   
1192 N  N    . SER   A 182 ? 0.6585 0.9244 0.4602 0.1375  0.0200  -0.1034 676  SER   A N    
1193 C  CA   . SER   A 182 ? 0.7827 1.0547 0.5662 0.1438  0.0183  -0.1105 676  SER   A CA   
1194 C  C    . SER   A 182 ? 0.7921 1.0446 0.5718 0.1337  0.0114  -0.1058 676  SER   A C    
1195 O  O    . SER   A 182 ? 0.7521 0.9885 0.5437 0.1229  0.0085  -0.0975 676  SER   A O    
1196 C  CB   . SER   A 182 ? 0.7226 1.0311 0.4979 0.1446  0.0272  -0.1060 676  SER   A CB   
1197 O  OG   . SER   A 182 ? 0.8477 1.1627 0.6043 0.1529  0.0258  -0.1146 676  SER   A OG   
1198 N  N    . ASP   A 183 ? 0.8144 1.0693 0.5774 0.1378  0.0085  -0.1114 677  ASP   A N    
1199 C  CA   . ASP   A 183 ? 0.8856 1.1253 0.6439 0.1288  0.0018  -0.1068 677  ASP   A CA   
1200 C  C    . ASP   A 183 ? 0.8229 1.0778 0.5815 0.1157  0.0059  -0.0910 677  ASP   A C    
1201 O  O    . ASP   A 183 ? 0.7946 1.0369 0.5514 0.1072  0.0004  -0.0852 677  ASP   A O    
1202 C  CB   . ASP   A 183 ? 0.9296 1.1655 0.6690 0.1378  -0.0036 -0.1186 677  ASP   A CB   
1203 C  CG   . ASP   A 183 ? 1.0136 1.2772 0.7390 0.1492  0.0032  -0.1253 677  ASP   A CG   
1204 O  OD1  . ASP   A 183 ? 1.1192 1.3775 0.8370 0.1631  0.0008  -0.1400 677  ASP   A OD1  
1205 O  OD2  . ASP   A 183 ? 1.0051 1.2956 0.7264 0.1445  0.0106  -0.1161 677  ASP   A OD2  
1206 N  N    . LYS   A 184 ? 0.8023 1.0837 0.5633 0.1136  0.0151  -0.0838 678  LYS   A N    
1207 C  CA   . LYS   A 184 ? 0.7580 1.0524 0.5193 0.1001  0.0186  -0.0681 678  LYS   A CA   
1208 C  C    . LYS   A 184 ? 0.7511 1.0266 0.5285 0.0882  0.0157  -0.0579 678  LYS   A C    
1209 O  O    . LYS   A 184 ? 0.7524 1.0259 0.5288 0.0769  0.0143  -0.0463 678  LYS   A O    
1210 C  CB   . LYS   A 184 ? 0.8018 1.1300 0.5627 0.1002  0.0290  -0.0629 678  LYS   A CB   
1211 C  CG   . LYS   A 184 ? 0.8104 1.1620 0.5557 0.1127  0.0333  -0.0726 678  LYS   A CG   
1212 C  CD   . LYS   A 184 ? 0.8409 1.2280 0.5890 0.1126  0.0440  -0.0673 678  LYS   A CD   
1213 C  CE   . LYS   A 184 ? 0.7985 1.1872 0.5606 0.1213  0.0467  -0.0743 678  LYS   A CE   
1214 N  NZ   . LYS   A 184 ? 0.8993 1.3132 0.6537 0.1369  0.0524  -0.0856 678  LYS   A NZ   
1215 N  N    . PHE   A 185 ? 0.7114 0.9727 0.5030 0.0908  0.0146  -0.0621 679  PHE   A N    
1216 C  CA   . PHE   A 185 ? 0.6695 0.9137 0.4767 0.0808  0.0125  -0.0536 679  PHE   A CA   
1217 C  C    . PHE   A 185 ? 0.6681 0.8851 0.4828 0.0855  0.0056  -0.0628 679  PHE   A C    
1218 O  O    . PHE   A 185 ? 0.6657 0.8803 0.4852 0.0940  0.0067  -0.0711 679  PHE   A O    
1219 C  CB   . PHE   A 185 ? 0.6474 0.9070 0.4661 0.0770  0.0199  -0.0467 679  PHE   A CB   
1220 C  CG   . PHE   A 185 ? 0.6194 0.8654 0.4515 0.0654  0.0185  -0.0362 679  PHE   A CG   
1221 C  CD1  . PHE   A 185 ? 0.5910 0.8177 0.4363 0.0666  0.0157  -0.0397 679  PHE   A CD1  
1222 C  CD2  . PHE   A 185 ? 0.6069 0.8589 0.4377 0.0532  0.0198  -0.0229 679  PHE   A CD2  
1223 C  CE1  . PHE   A 185 ? 0.5675 0.7823 0.4246 0.0565  0.0146  -0.0306 679  PHE   A CE1  
1224 C  CE2  . PHE   A 185 ? 0.6075 0.8459 0.4500 0.0433  0.0181  -0.0139 679  PHE   A CE2  
1225 C  CZ   . PHE   A 185 ? 0.5397 0.7601 0.3953 0.0452  0.0157  -0.0180 679  PHE   A CZ   
1226 N  N    . ILE   A 186 ? 0.6427 0.8395 0.4585 0.0798  -0.0015 -0.0606 680  ILE   A N    
1227 C  CA   . ILE   A 186 ? 0.6071 0.7788 0.4284 0.0830  -0.0089 -0.0688 680  ILE   A CA   
1228 C  C    . ILE   A 186 ? 0.6110 0.7682 0.4493 0.0749  -0.0098 -0.0618 680  ILE   A C    
1229 O  O    . ILE   A 186 ? 0.5939 0.7515 0.4364 0.0652  -0.0094 -0.0507 680  ILE   A O    
1230 C  CB   . ILE   A 186 ? 0.6658 0.8266 0.4768 0.0826  -0.0167 -0.0720 680  ILE   A CB   
1231 C  CG1  . ILE   A 186 ? 0.6785 0.8552 0.4710 0.0905  -0.0155 -0.0786 680  ILE   A CG1  
1232 C  CG2  . ILE   A 186 ? 0.6565 0.7921 0.4739 0.0846  -0.0247 -0.0799 680  ILE   A CG2  
1233 C  CD1  . ILE   A 186 ? 0.7296 0.8938 0.5109 0.0927  -0.0241 -0.0854 680  ILE   A CD1  
1234 N  N    . TYR   A 187 ? 0.5871 0.7308 0.4345 0.0792  -0.0114 -0.0682 681  TYR   A N    
1235 C  CA   . TYR   A 187 ? 0.5451 0.6744 0.4081 0.0722  -0.0126 -0.0627 681  TYR   A CA   
1236 C  C    . TYR   A 187 ? 0.5173 0.6244 0.3847 0.0757  -0.0192 -0.0714 681  TYR   A C    
1237 O  O    . TYR   A 187 ? 0.5331 0.6361 0.3927 0.0844  -0.0220 -0.0821 681  TYR   A O    
1238 C  CB   . TYR   A 187 ? 0.4969 0.6362 0.3693 0.0712  -0.0055 -0.0581 681  TYR   A CB   
1239 C  CG   . TYR   A 187 ? 0.5444 0.6913 0.4148 0.0820  -0.0024 -0.0670 681  TYR   A CG   
1240 C  CD1  . TYR   A 187 ? 0.5627 0.7327 0.4238 0.0877  0.0030  -0.0688 681  TYR   A CD1  
1241 C  CD2  . TYR   A 187 ? 0.5596 0.6906 0.4371 0.0868  -0.0050 -0.0736 681  TYR   A CD2  
1242 C  CE1  . TYR   A 187 ? 0.5874 0.7650 0.4469 0.0989  0.0057  -0.0775 681  TYR   A CE1  
1243 C  CE2  . TYR   A 187 ? 0.5814 0.7177 0.4567 0.0976  -0.0029 -0.0819 681  TYR   A CE2  
1244 C  CZ   . TYR   A 187 ? 0.6215 0.7813 0.4880 0.1041  0.0024  -0.0841 681  TYR   A CZ   
1245 O  OH   . TYR   A 187 ? 0.5874 0.7529 0.4520 0.1160  0.0043  -0.0928 681  TYR   A OH   
1246 N  N    . ALA   A 188 ? 0.5248 0.6174 0.4045 0.0687  -0.0219 -0.0666 682  ALA   A N    
1247 C  CA   . ALA   A 188 ? 0.5004 0.5726 0.3844 0.0695  -0.0288 -0.0730 682  ALA   A CA   
1248 C  C    . ALA   A 188 ? 0.5052 0.5664 0.4046 0.0621  -0.0291 -0.0666 682  ALA   A C    
1249 O  O    . ALA   A 188 ? 0.4733 0.5413 0.3791 0.0563  -0.0248 -0.0575 682  ALA   A O    
1250 C  CB   . ALA   A 188 ? 0.5181 0.5847 0.3935 0.0689  -0.0359 -0.0763 682  ALA   A CB   
1251 N  N    . THR   A 189 ? 0.4507 0.4948 0.3557 0.0622  -0.0344 -0.0717 683  THR   A N    
1252 C  CA   . THR   A 189 ? 0.4965 0.5298 0.4157 0.0554  -0.0355 -0.0667 683  THR   A CA   
1253 C  C    . THR   A 189 ? 0.4360 0.4562 0.3561 0.0530  -0.0436 -0.0705 683  THR   A C    
1254 O  O    . THR   A 189 ? 0.4438 0.4648 0.3539 0.0552  -0.0481 -0.0749 683  THR   A O    
1255 C  CB   . THR   A 189 ? 0.4327 0.4605 0.3591 0.0578  -0.0324 -0.0684 683  THR   A CB   
1256 O  OG1  . THR   A 189 ? 0.4389 0.4594 0.3785 0.0509  -0.0320 -0.0623 683  THR   A OG1  
1257 C  CG2  . THR   A 189 ? 0.5113 0.5259 0.4334 0.0639  -0.0374 -0.0786 683  THR   A CG2  
1258 N  N    . VAL   A 190 ? 0.5050 0.5138 0.4371 0.0482  -0.0458 -0.0688 684  VAL   A N    
1259 C  CA   . VAL   A 190 ? 0.4708 0.4689 0.4061 0.0445  -0.0535 -0.0714 684  VAL   A CA   
1260 C  C    . VAL   A 190 ? 0.4838 0.4679 0.4178 0.0476  -0.0577 -0.0800 684  VAL   A C    
1261 O  O    . VAL   A 190 ? 0.4822 0.4610 0.4207 0.0490  -0.0548 -0.0804 684  VAL   A O    
1262 C  CB   . VAL   A 190 ? 0.4378 0.4338 0.3875 0.0370  -0.0533 -0.0639 684  VAL   A CB   
1263 C  CG1  . VAL   A 190 ? 0.4550 0.4431 0.4092 0.0329  -0.0611 -0.0662 684  VAL   A CG1  
1264 C  CG2  . VAL   A 190 ? 0.4542 0.4618 0.4044 0.0345  -0.0491 -0.0553 684  VAL   A CG2  
1265 N  N    . LYS   A 191 ? 0.4736 0.4508 0.4005 0.0486  -0.0652 -0.0868 685  LYS   A N    
1266 C  CA   . LYS   A 191 ? 0.5074 0.4686 0.4318 0.0509  -0.0706 -0.0951 685  LYS   A CA   
1267 C  C    . LYS   A 191 ? 0.5298 0.4804 0.4685 0.0440  -0.0718 -0.0916 685  LYS   A C    
1268 O  O    . LYS   A 191 ? 0.5044 0.4588 0.4542 0.0369  -0.0714 -0.0847 685  LYS   A O    
1269 C  CB   . LYS   A 191 ? 0.5804 0.5354 0.4956 0.0515  -0.0794 -0.1024 685  LYS   A CB   
1270 C  CG   . LYS   A 191 ? 0.5968 0.5644 0.4984 0.0565  -0.0788 -0.1043 685  LYS   A CG   
1271 C  CD   . LYS   A 191 ? 0.6339 0.5935 0.5209 0.0622  -0.0859 -0.1154 685  LYS   A CD   
1272 C  CE   . LYS   A 191 ? 0.6480 0.5976 0.5372 0.0559  -0.0957 -0.1178 685  LYS   A CE   
1273 N  NZ   . LYS   A 191 ? 0.7398 0.6872 0.6121 0.0613  -0.1023 -0.1273 685  LYS   A NZ   
1274 N  N    . GLN   A 192 ? 0.5012 0.4383 0.4390 0.0464  -0.0733 -0.0963 686  GLN   A N    
1275 C  CA   . GLN   A 192 ? 0.5217 0.4469 0.4712 0.0395  -0.0754 -0.0937 686  GLN   A CA   
1276 C  C    . GLN   A 192 ? 0.5188 0.4531 0.4817 0.0342  -0.0686 -0.0838 686  GLN   A C    
1277 O  O    . GLN   A 192 ? 0.4973 0.4295 0.4716 0.0264  -0.0701 -0.0794 686  GLN   A O    
1278 C  CB   . GLN   A 192 ? 0.5437 0.4601 0.4954 0.0330  -0.0844 -0.0963 686  GLN   A CB   
1279 C  CG   . GLN   A 192 ? 0.5681 0.4712 0.5062 0.0378  -0.0921 -0.1069 686  GLN   A CG   
1280 C  CD   . GLN   A 192 ? 0.6966 0.5975 0.6335 0.0327  -0.1006 -0.1097 686  GLN   A CD   
1281 O  OE1  . GLN   A 192 ? 0.7873 0.6793 0.7324 0.0245  -0.1063 -0.1088 686  GLN   A OE1  
1282 N  NE2  . GLN   A 192 ? 0.6885 0.5987 0.6153 0.0372  -0.1016 -0.1127 686  GLN   A NE2  
1283 N  N    . SER   A 193 ? 0.4524 0.3976 0.4137 0.0385  -0.0611 -0.0805 687  SER   A N    
1284 C  CA   . SER   A 193 ? 0.4583 0.4108 0.4301 0.0348  -0.0543 -0.0721 687  SER   A CA   
1285 C  C    . SER   A 193 ? 0.4920 0.4415 0.4634 0.0391  -0.0498 -0.0723 687  SER   A C    
1286 O  O    . SER   A 193 ? 0.4514 0.3955 0.4137 0.0461  -0.0512 -0.0789 687  SER   A O    
1287 C  CB   . SER   A 193 ? 0.4476 0.4160 0.4181 0.0351  -0.0499 -0.0669 687  SER   A CB   
1288 O  OG   . SER   A 193 ? 0.4561 0.4317 0.4166 0.0423  -0.0460 -0.0694 687  SER   A OG   
1289 N  N    . SER   A 194 ? 0.4735 0.4270 0.4543 0.0354  -0.0444 -0.0653 688  SER   A N    
1290 C  CA   . SER   A 194 ? 0.4666 0.4190 0.4476 0.0392  -0.0400 -0.0648 688  SER   A CA   
1291 C  C    . SER   A 194 ? 0.4340 0.3977 0.4062 0.0469  -0.0360 -0.0668 688  SER   A C    
1292 O  O    . SER   A 194 ? 0.4483 0.4099 0.4168 0.0530  -0.0347 -0.0699 688  SER   A O    
1293 C  CB   . SER   A 194 ? 0.4525 0.4085 0.4443 0.0337  -0.0350 -0.0569 688  SER   A CB   
1294 O  OG   . SER   A 194 ? 0.4300 0.3993 0.4237 0.0319  -0.0310 -0.0516 688  SER   A OG   
1295 N  N    . VAL   A 195 ? 0.4718 0.4483 0.4407 0.0466  -0.0343 -0.0647 689  VAL   A N    
1296 C  CA   . VAL   A 195 ? 0.4151 0.4054 0.3764 0.0525  -0.0299 -0.0654 689  VAL   A CA   
1297 C  C    . VAL   A 195 ? 0.4954 0.4831 0.4450 0.0610  -0.0331 -0.0747 689  VAL   A C    
1298 O  O    . VAL   A 195 ? 0.5000 0.4942 0.4446 0.0684  -0.0300 -0.0777 689  VAL   A O    
1299 C  CB   . VAL   A 195 ? 0.4475 0.4510 0.4079 0.0487  -0.0276 -0.0597 689  VAL   A CB   
1300 C  CG1  . VAL   A 195 ? 0.4706 0.4904 0.4247 0.0530  -0.0220 -0.0586 689  VAL   A CG1  
1301 C  CG2  . VAL   A 195 ? 0.4473 0.4502 0.4189 0.0409  -0.0257 -0.0516 689  VAL   A CG2  
1302 N  N    . ASP   A 196 ? 0.4236 0.4026 0.3685 0.0605  -0.0397 -0.0796 690  ASP   A N    
1303 C  CA   . ASP   A 196 ? 0.4714 0.4436 0.4048 0.0685  -0.0442 -0.0897 690  ASP   A CA   
1304 C  C    . ASP   A 196 ? 0.5350 0.4955 0.4680 0.0742  -0.0449 -0.0941 690  ASP   A C    
1305 O  O    . ASP   A 196 ? 0.4961 0.4595 0.4202 0.0840  -0.0442 -0.1005 690  ASP   A O    
1306 C  CB   . ASP   A 196 ? 0.4935 0.4541 0.4248 0.0646  -0.0523 -0.0933 690  ASP   A CB   
1307 C  CG   . ASP   A 196 ? 0.6334 0.5870 0.5507 0.0724  -0.0579 -0.1042 690  ASP   A CG   
1308 O  OD1  . ASP   A 196 ? 0.5662 0.5266 0.4743 0.0819  -0.0551 -0.1091 690  ASP   A OD1  
1309 O  OD2  . ASP   A 196 ? 0.6519 0.5936 0.5675 0.0690  -0.0655 -0.1079 690  ASP   A OD2  
1310 N  N    . ILE   A 197 ? 0.4714 0.4193 0.4139 0.0684  -0.0464 -0.0907 691  ILE   A N    
1311 C  CA   . ILE   A 197 ? 0.5553 0.4899 0.4972 0.0730  -0.0479 -0.0941 691  ILE   A CA   
1312 C  C    . ILE   A 197 ? 0.5302 0.4769 0.4739 0.0782  -0.0409 -0.0913 691  ILE   A C    
1313 O  O    . ILE   A 197 ? 0.5496 0.4910 0.4883 0.0868  -0.0416 -0.0963 691  ILE   A O    
1314 C  CB   . ILE   A 197 ? 0.5659 0.4848 0.5172 0.0642  -0.0512 -0.0901 691  ILE   A CB   
1315 C  CG1  . ILE   A 197 ? 0.6071 0.5138 0.5554 0.0602  -0.0593 -0.0945 691  ILE   A CG1  
1316 C  CG2  . ILE   A 197 ? 0.5719 0.4778 0.5233 0.0680  -0.0520 -0.0914 691  ILE   A CG2  
1317 C  CD1  . ILE   A 197 ? 0.7067 0.5946 0.6591 0.0551  -0.0643 -0.0943 691  ILE   A CD1  
1318 N  N    . TYR   A 198 ? 0.4854 0.4477 0.4362 0.0732  -0.0345 -0.0832 692  TYR   A N    
1319 C  CA   . TYR   A 198 ? 0.5352 0.5112 0.4878 0.0773  -0.0280 -0.0802 692  TYR   A CA   
1320 C  C    . TYR   A 198 ? 0.5492 0.5361 0.4915 0.0883  -0.0267 -0.0870 692  TYR   A C    
1321 O  O    . TYR   A 198 ? 0.5068 0.4960 0.4477 0.0960  -0.0250 -0.0896 692  TYR   A O    
1322 C  CB   . TYR   A 198 ? 0.4789 0.4697 0.4387 0.0697  -0.0223 -0.0711 692  TYR   A CB   
1323 C  CG   . TYR   A 198 ? 0.5031 0.5111 0.4644 0.0725  -0.0156 -0.0675 692  TYR   A CG   
1324 C  CD1  . TYR   A 198 ? 0.5166 0.5235 0.4854 0.0708  -0.0129 -0.0631 692  TYR   A CD1  
1325 C  CD2  . TYR   A 198 ? 0.5645 0.5910 0.5198 0.0760  -0.0122 -0.0679 692  TYR   A CD2  
1326 C  CE1  . TYR   A 198 ? 0.5905 0.6140 0.5612 0.0726  -0.0073 -0.0597 692  TYR   A CE1  
1327 C  CE2  . TYR   A 198 ? 0.5221 0.5659 0.4795 0.0775  -0.0062 -0.0642 692  TYR   A CE2  
1328 C  CZ   . TYR   A 198 ? 0.5601 0.6024 0.5255 0.0757  -0.0040 -0.0601 692  TYR   A CZ   
1329 O  OH   . TYR   A 198 ? 0.5855 0.6458 0.5533 0.0765  0.0014  -0.0564 692  TYR   A OH   
1330 N  N    . PHE   A 199 ? 0.5236 0.5174 0.4580 0.0897  -0.0278 -0.0902 693  PHE   A N    
1331 C  CA   . PHE   A 199 ? 0.5558 0.5619 0.4796 0.1004  -0.0263 -0.0970 693  PHE   A CA   
1332 C  C    . PHE   A 199 ? 0.5913 0.5809 0.5060 0.1101  -0.0326 -0.1080 693  PHE   A C    
1333 O  O    . PHE   A 199 ? 0.5773 0.5741 0.4854 0.1213  -0.0311 -0.1141 693  PHE   A O    
1334 C  CB   . PHE   A 199 ? 0.5298 0.5496 0.4473 0.0981  -0.0251 -0.0960 693  PHE   A CB   
1335 C  CG   . PHE   A 199 ? 0.5313 0.5711 0.4543 0.0920  -0.0181 -0.0863 693  PHE   A CG   
1336 C  CD1  . PHE   A 199 ? 0.5043 0.5412 0.4362 0.0809  -0.0177 -0.0777 693  PHE   A CD1  
1337 C  CD2  . PHE   A 199 ? 0.5528 0.6144 0.4721 0.0972  -0.0121 -0.0859 693  PHE   A CD2  
1338 C  CE1  . PHE   A 199 ? 0.5034 0.5559 0.4394 0.0752  -0.0121 -0.0689 693  PHE   A CE1  
1339 C  CE2  . PHE   A 199 ? 0.5336 0.6124 0.4577 0.0904  -0.0062 -0.0765 693  PHE   A CE2  
1340 C  CZ   . PHE   A 199 ? 0.5121 0.5851 0.4441 0.0794  -0.0065 -0.0681 693  PHE   A CZ   
1341 N  N    . ARG   A 200 ? 0.5752 0.5427 0.4896 0.1061  -0.0400 -0.1107 694  ARG   A N    
1342 C  CA   . ARG   A 200 ? 0.6187 0.5672 0.5237 0.1146  -0.0470 -0.1211 694  ARG   A CA   
1343 C  C    . ARG   A 200 ? 0.6164 0.5566 0.5239 0.1208  -0.0468 -0.1222 694  ARG   A C    
1344 O  O    . ARG   A 200 ? 0.6785 0.6122 0.5767 0.1327  -0.0497 -0.1310 694  ARG   A O    
1345 C  CB   . ARG   A 200 ? 0.6666 0.5933 0.5719 0.1069  -0.0553 -0.1226 694  ARG   A CB   
1346 C  CG   . ARG   A 200 ? 0.7878 0.6902 0.6841 0.1137  -0.0638 -0.1325 694  ARG   A CG   
1347 C  CD   . ARG   A 200 ? 0.8302 0.7101 0.7323 0.1031  -0.0707 -0.1299 694  ARG   A CD   
1348 N  NE   . ARG   A 200 ? 0.8638 0.7435 0.7658 0.0950  -0.0746 -0.1297 694  ARG   A NE   
1349 C  CZ   . ARG   A 200 ? 0.9700 0.8435 0.8603 0.0990  -0.0809 -0.1385 694  ARG   A CZ   
1350 N  NH1  . ARG   A 200 ? 0.9552 0.8209 0.8322 0.1113  -0.0842 -0.1489 694  ARG   A NH1  
1351 N  NH2  . ARG   A 200 ? 0.9573 0.8325 0.8489 0.0908  -0.0842 -0.1371 694  ARG   A NH2  
1352 N  N    . ARG   A 201 ? 0.5978 0.5378 0.5170 0.1135  -0.0435 -0.1133 695  ARG   A N    
1353 C  CA   . ARG   A 201 ? 0.6906 0.6181 0.6125 0.1173  -0.0449 -0.1134 695  ARG   A CA   
1354 C  C    . ARG   A 201 ? 0.6853 0.6298 0.6065 0.1276  -0.0392 -0.1143 695  ARG   A C    
1355 O  O    . ARG   A 201 ? 0.7227 0.6566 0.6407 0.1364  -0.0420 -0.1187 695  ARG   A O    
1356 C  CB   . ARG   A 201 ? 0.6627 0.5834 0.5967 0.1051  -0.0438 -0.1037 695  ARG   A CB   
1357 N  N    . GLN   A 202 ? 0.6194 0.5901 0.5438 0.1267  -0.0317 -0.1099 696  GLN   A N    
1358 C  CA   . GLN   A 202 ? 0.6563 0.6464 0.5821 0.1349  -0.0260 -0.1095 696  GLN   A CA   
1359 C  C    . GLN   A 202 ? 0.6741 0.6774 0.5890 0.1477  -0.0253 -0.1186 696  GLN   A C    
1360 O  O    . GLN   A 202 ? 0.6465 0.6632 0.5569 0.1460  -0.0231 -0.1192 696  GLN   A O    
1361 C  CB   . GLN   A 202 ? 0.5997 0.6110 0.5353 0.1258  -0.0184 -0.0991 696  GLN   A CB   
1362 C  CG   . GLN   A 202 ? 0.6743 0.6747 0.6186 0.1120  -0.0190 -0.0909 696  GLN   A CG   
1363 C  CD   . GLN   A 202 ? 0.6813 0.6930 0.6361 0.1053  -0.0134 -0.0815 696  GLN   A CD   
1364 O  OE1  . GLN   A 202 ? 0.6642 0.6899 0.6209 0.1105  -0.0096 -0.0807 696  GLN   A OE1  
1365 N  NE2  . GLN   A 202 ? 0.7418 0.7474 0.7035 0.0938  -0.0132 -0.0746 696  GLN   A NE2  
1366 N  N    . VAL   A 203 ? 0.6405 0.6406 0.5508 0.1610  -0.0271 -0.1257 697  VAL   A N    
1367 C  CA   . VAL   A 203 ? 0.6635 0.6768 0.5631 0.1750  -0.0264 -0.1354 697  VAL   A CA   
1368 C  C    . VAL   A 203 ? 0.6192 0.6679 0.5222 0.1749  -0.0172 -0.1308 697  VAL   A C    
1369 O  O    . VAL   A 203 ? 0.6522 0.7169 0.5467 0.1814  -0.0150 -0.1362 697  VAL   A O    
1370 C  CB   . VAL   A 203 ? 0.7432 0.7455 0.6382 0.1899  -0.0304 -0.1435 697  VAL   A CB   
1371 C  CG1  . VAL   A 203 ? 0.7408 0.7070 0.6282 0.1911  -0.0407 -0.1500 697  VAL   A CG1  
1372 C  CG2  . VAL   A 203 ? 0.7057 0.7137 0.6118 0.1888  -0.0271 -0.1363 697  VAL   A CG2  
1373 N  N    . GLU   A 204 ? 0.5781 0.6396 0.4929 0.1671  -0.0118 -0.1208 698  GLU   A N    
1374 C  CA   . GLU   A 204 ? 0.6475 0.7418 0.5663 0.1645  -0.0035 -0.1150 698  GLU   A CA   
1375 C  C    . GLU   A 204 ? 0.6738 0.7763 0.5892 0.1553  -0.0015 -0.1115 698  GLU   A C    
1376 O  O    . GLU   A 204 ? 0.5910 0.7204 0.5058 0.1546  0.0047  -0.1084 698  GLU   A O    
1377 C  CB   . GLU   A 204 ? 0.5943 0.6962 0.5263 0.1560  0.0005  -0.1046 698  GLU   A CB   
1378 N  N    . LEU   A 205 ? 0.5910 0.6716 0.5043 0.1478  -0.0067 -0.1112 699  LEU   A N    
1379 C  CA   . LEU   A 205 ? 0.6159 0.7029 0.5256 0.1398  -0.0058 -0.1081 699  LEU   A CA   
1380 C  C    . LEU   A 205 ? 0.6277 0.7044 0.5241 0.1465  -0.0112 -0.1181 699  LEU   A C    
1381 O  O    . LEU   A 205 ? 0.5884 0.6641 0.4810 0.1396  -0.0126 -0.1163 699  LEU   A O    
1382 C  CB   . LEU   A 205 ? 0.5891 0.6636 0.5076 0.1249  -0.0070 -0.0988 699  LEU   A CB   
1383 C  CG   . LEU   A 205 ? 0.5795 0.6566 0.5107 0.1176  -0.0035 -0.0896 699  LEU   A CG   
1384 C  CD1  . LEU   A 205 ? 0.6229 0.6775 0.5612 0.1075  -0.0074 -0.0851 699  LEU   A CD1  
1385 C  CD2  . LEU   A 205 ? 0.6595 0.7616 0.5946 0.1110  0.0035  -0.0811 699  LEU   A CD2  
1386 N  N    . SER   A 206 ? 0.6097 0.6790 0.4982 0.1602  -0.0146 -0.1290 700  SER   A N    
1387 C  CA   . SER   A 206 ? 0.6479 0.7030 0.5232 0.1665  -0.0211 -0.1394 700  SER   A CA   
1388 C  C    . SER   A 206 ? 0.6550 0.7313 0.5210 0.1675  -0.0177 -0.1407 700  SER   A C    
1389 O  O    . SER   A 206 ? 0.6483 0.7143 0.5059 0.1655  -0.0225 -0.1445 700  SER   A O    
1390 C  CB   . SER   A 206 ? 0.6526 0.6969 0.5202 0.1824  -0.0253 -0.1512 700  SER   A CB   
1391 O  OG   . SER   A 206 ? 0.6999 0.7713 0.5639 0.1941  -0.0191 -0.1548 700  SER   A OG   
1392 N  N    . THR   A 207 ? 0.6206 0.7273 0.4875 0.1707  -0.0094 -0.1375 701  THR   A N    
1393 C  CA   . THR   A 207 ? 0.6130 0.7414 0.4705 0.1710  -0.0056 -0.1378 701  THR   A CA   
1394 C  C    . THR   A 207 ? 0.5828 0.7081 0.4426 0.1558  -0.0063 -0.1286 701  THR   A C    
1395 O  O    . THR   A 207 ? 0.5704 0.6974 0.4196 0.1553  -0.0083 -0.1313 701  THR   A O    
1396 C  CB   . THR   A 207 ? 0.5893 0.7524 0.4495 0.1746  0.0037  -0.1340 701  THR   A CB   
1397 O  OG1  . THR   A 207 ? 0.6717 0.8380 0.5328 0.1884  0.0043  -0.1413 701  THR   A OG1  
1398 C  CG2  . THR   A 207 ? 0.6624 0.8478 0.5101 0.1778  0.0072  -0.1365 701  THR   A CG2  
1399 N  N    . MET   A 208 ? 0.5591 0.6800 0.4321 0.1439  -0.0049 -0.1180 702  MET   A N    
1400 C  CA   . MET   A 208 ? 0.5636 0.6792 0.4396 0.1302  -0.0063 -0.1095 702  MET   A CA   
1401 C  C    . MET   A 208 ? 0.5945 0.6825 0.4675 0.1282  -0.0152 -0.1145 702  MET   A C    
1402 O  O    . MET   A 208 ? 0.6033 0.6898 0.4700 0.1239  -0.0181 -0.1141 702  MET   A O    
1403 C  CB   . MET   A 208 ? 0.5514 0.6692 0.4420 0.1194  -0.0026 -0.0978 702  MET   A CB   
1404 C  CG   . MET   A 208 ? 0.5568 0.7035 0.4502 0.1179  0.0058  -0.0909 702  MET   A CG   
1405 S  SD   . MET   A 208 ? 0.5715 0.7184 0.4809 0.1050  0.0091  -0.0778 702  MET   A SD   
1406 C  CE   . MET   A 208 ? 0.5606 0.7080 0.4675 0.0921  0.0085  -0.0688 702  MET   A CE   
1407 N  N    . TYR   A 209 ? 0.6002 0.6665 0.4773 0.1310  -0.0201 -0.1190 703  TYR   A N    
1408 C  CA   . TYR   A 209 ? 0.6219 0.6623 0.4974 0.1274  -0.0287 -0.1229 703  TYR   A CA   
1409 C  C    . TYR   A 209 ? 0.6558 0.6934 0.5159 0.1341  -0.0336 -0.1328 703  TYR   A C    
1410 O  O    . TYR   A 209 ? 0.6721 0.6986 0.5298 0.1278  -0.0393 -0.1330 703  TYR   A O    
1411 C  CB   . TYR   A 209 ? 0.6673 0.6859 0.5479 0.1304  -0.0330 -0.1267 703  TYR   A CB   
1412 C  CG   . TYR   A 209 ? 0.6850 0.6768 0.5627 0.1276  -0.0425 -0.1319 703  TYR   A CG   
1413 C  CD1  . TYR   A 209 ? 0.6134 0.5954 0.4999 0.1148  -0.0452 -0.1249 703  TYR   A CD1  
1414 C  CD2  . TYR   A 209 ? 0.6597 0.6365 0.5258 0.1377  -0.0490 -0.1438 703  TYR   A CD2  
1415 C  CE1  . TYR   A 209 ? 0.6823 0.6419 0.5670 0.1112  -0.0540 -0.1292 703  TYR   A CE1  
1416 C  CE2  . TYR   A 209 ? 0.7160 0.6680 0.5793 0.1340  -0.0582 -0.1483 703  TYR   A CE2  
1417 C  CZ   . TYR   A 209 ? 0.7106 0.6550 0.5837 0.1203  -0.0606 -0.1407 703  TYR   A CZ   
1418 O  OH   . TYR   A 209 ? 0.7219 0.6435 0.5932 0.1159  -0.0698 -0.1448 703  TYR   A OH   
1419 N  N    . ARG   A 210 ? 0.6230 0.6715 0.4724 0.1470  -0.0317 -0.1413 704  ARG   A N    
1420 C  CA   . ARG   A 210 ? 0.6795 0.7254 0.5128 0.1546  -0.0364 -0.1518 704  ARG   A CA   
1421 C  C    . ARG   A 210 ? 0.6720 0.7365 0.4994 0.1491  -0.0334 -0.1470 704  ARG   A C    
1422 O  O    . ARG   A 210 ? 0.6844 0.7419 0.5008 0.1498  -0.0391 -0.1526 704  ARG   A O    
1423 C  CB   . ARG   A 210 ? 0.6823 0.7354 0.5057 0.1712  -0.0348 -0.1627 704  ARG   A CB   
1424 C  CG   . ARG   A 210 ? 0.7181 0.7470 0.5433 0.1783  -0.0405 -0.1698 704  ARG   A CG   
1425 C  CD   . ARG   A 210 ? 0.7815 0.7787 0.6032 0.1738  -0.0514 -0.1746 704  ARG   A CD   
1426 N  NE   . ARG   A 210 ? 0.8144 0.7864 0.6412 0.1754  -0.0567 -0.1770 704  ARG   A NE   
1427 C  CZ   . ARG   A 210 ? 0.8601 0.8028 0.6816 0.1751  -0.0668 -0.1838 704  ARG   A CZ   
1428 N  NH1  . ARG   A 210 ? 0.8827 0.8169 0.6944 0.1730  -0.0732 -0.1893 704  ARG   A NH1  
1429 N  NH2  . ARG   A 210 ? 0.8990 0.8200 0.7250 0.1763  -0.0711 -0.1848 704  ARG   A NH2  
1430 N  N    . HIS   A 211 ? 0.6600 0.7473 0.4940 0.1433  -0.0251 -0.1363 705  HIS   A N    
1431 C  CA   . HIS   A 211 ? 0.6368 0.7385 0.4662 0.1358  -0.0230 -0.1295 705  HIS   A CA   
1432 C  C    . HIS   A 211 ? 0.5958 0.6803 0.4319 0.1235  -0.0288 -0.1234 705  HIS   A C    
1433 O  O    . HIS   A 211 ? 0.6505 0.7316 0.4782 0.1211  -0.0334 -0.1250 705  HIS   A O    
1434 C  CB   . HIS   A 211 ? 0.6298 0.7586 0.4649 0.1318  -0.0133 -0.1191 705  HIS   A CB   
1435 C  CG   . HIS   A 211 ? 0.6506 0.7926 0.4818 0.1227  -0.0113 -0.1102 705  HIS   A CG   
1436 N  ND1  . HIS   A 211 ? 0.6608 0.8243 0.4787 0.1268  -0.0076 -0.1115 705  HIS   A ND1  
1437 C  CD2  . HIS   A 211 ? 0.6494 0.7859 0.4875 0.1101  -0.0126 -0.0998 705  HIS   A CD2  
1438 C  CE1  . HIS   A 211 ? 0.6664 0.8360 0.4829 0.1165  -0.0071 -0.1018 705  HIS   A CE1  
1439 N  NE2  . HIS   A 211 ? 0.6548 0.8079 0.4836 0.1066  -0.0103 -0.0947 705  HIS   A NE2  
1440 N  N    . MET   A 212 ? 0.5871 0.6609 0.4382 0.1161  -0.0287 -0.1168 706  MET   A N    
1441 C  CA   . MET   A 212 ? 0.6255 0.6869 0.4847 0.1044  -0.0329 -0.1099 706  MET   A CA   
1442 C  C    . MET   A 212 ? 0.6501 0.6893 0.5052 0.1048  -0.0426 -0.1178 706  MET   A C    
1443 O  O    . MET   A 212 ? 0.6414 0.6753 0.4980 0.0971  -0.0470 -0.1143 706  MET   A O    
1444 C  CB   . MET   A 212 ? 0.5746 0.6308 0.4502 0.0975  -0.0301 -0.1018 706  MET   A CB   
1445 C  CG   . MET   A 212 ? 0.5710 0.6476 0.4518 0.0943  -0.0215 -0.0925 706  MET   A CG   
1446 S  SD   . MET   A 212 ? 0.6630 0.7337 0.5595 0.0918  -0.0182 -0.0878 706  MET   A SD   
1447 C  CE   . MET   A 212 ? 0.5071 0.5610 0.4140 0.0797  -0.0227 -0.0808 706  MET   A CE   
1448 N  N    . GLU   A 213 ? 0.6250 0.6512 0.4749 0.1136  -0.0465 -0.1284 707  GLU   A N    
1449 C  CA   . GLU   A 213 ? 0.6462 0.6499 0.4915 0.1135  -0.0565 -0.1364 707  GLU   A CA   
1450 C  C    . GLU   A 213 ? 0.6870 0.6948 0.5200 0.1135  -0.0608 -0.1399 707  GLU   A C    
1451 O  O    . GLU   A 213 ? 0.7088 0.7017 0.5416 0.1082  -0.0689 -0.1419 707  GLU   A O    
1452 C  CB   . GLU   A 213 ? 0.6869 0.6768 0.5255 0.1247  -0.0600 -0.1479 707  GLU   A CB   
1453 N  N    . LYS   A 214 ? 0.6853 0.7137 0.5076 0.1189  -0.0557 -0.1404 708  LYS   A N    
1454 C  CA   . LYS   A 214 ? 0.6869 0.7205 0.4959 0.1192  -0.0594 -0.1433 708  LYS   A CA   
1455 C  C    . LYS   A 214 ? 0.6738 0.7150 0.4888 0.1076  -0.0588 -0.1316 708  LYS   A C    
1456 O  O    . LYS   A 214 ? 0.7096 0.7526 0.5149 0.1063  -0.0632 -0.1330 708  LYS   A O    
1457 C  CB   . LYS   A 214 ? 0.7094 0.7633 0.5033 0.1299  -0.0539 -0.1486 708  LYS   A CB   
1458 N  N    . HIS   A 215 ? 0.6451 0.6903 0.4749 0.0997  -0.0538 -0.1204 709  HIS   A N    
1459 C  CA   . HIS   A 215 ? 0.6565 0.7101 0.4905 0.0902  -0.0527 -0.1093 709  HIS   A CA   
1460 C  C    . HIS   A 215 ? 0.6148 0.6576 0.4660 0.0804  -0.0543 -0.1013 709  HIS   A C    
1461 O  O    . HIS   A 215 ? 0.5951 0.6435 0.4502 0.0732  -0.0538 -0.0922 709  HIS   A O    
1462 C  CB   . HIS   A 215 ? 0.6599 0.7368 0.4913 0.0902  -0.0434 -0.1015 709  HIS   A CB   
1463 C  CG   . HIS   A 215 ? 0.6957 0.7876 0.5109 0.0999  -0.0403 -0.1084 709  HIS   A CG   
1464 N  ND1  . HIS   A 215 ? 0.6932 0.7941 0.5073 0.1083  -0.0345 -0.1131 709  HIS   A ND1  
1465 C  CD2  . HIS   A 215 ? 0.7085 0.8087 0.5077 0.1030  -0.0424 -0.1120 709  HIS   A CD2  
1466 C  CE1  . HIS   A 215 ? 0.6739 0.7890 0.4723 0.1165  -0.0327 -0.1192 709  HIS   A CE1  
1467 N  NE2  . HIS   A 215 ? 0.7060 0.8206 0.4947 0.1133  -0.0373 -0.1187 709  HIS   A NE2  
1468 N  N    . ASN   A 216 ? 0.5717 0.5991 0.4326 0.0802  -0.0564 -0.1044 710  ASN   A N    
1469 C  CA   . ASN   A 216 ? 0.6133 0.6322 0.4905 0.0713  -0.0572 -0.0970 710  ASN   A CA   
1470 C  C    . ASN   A 216 ? 0.5743 0.5878 0.4534 0.0646  -0.0643 -0.0948 710  ASN   A C    
1471 O  O    . ASN   A 216 ? 0.5653 0.5738 0.4350 0.0668  -0.0711 -0.1018 710  ASN   A O    
1472 C  CB   . ASN   A 216 ? 0.5438 0.5464 0.4285 0.0725  -0.0592 -0.1018 710  ASN   A CB   
1473 C  CG   . ASN   A 216 ? 0.5831 0.5912 0.4709 0.0770  -0.0519 -0.1008 710  ASN   A CG   
1474 O  OD1  . ASN   A 216 ? 0.5530 0.5767 0.4426 0.0761  -0.0448 -0.0939 710  ASN   A OD1  
1475 N  ND2  . ASN   A 216 ? 0.5933 0.5882 0.4814 0.0819  -0.0540 -0.1076 710  ASN   A ND2  
1476 N  N    . TYR   A 217 ? 0.5500 0.5649 0.4414 0.0569  -0.0629 -0.0853 711  TYR   A N    
1477 C  CA   . TYR   A 217 ? 0.5627 0.5758 0.4577 0.0508  -0.0687 -0.0815 711  TYR   A CA   
1478 C  C    . TYR   A 217 ? 0.5550 0.5548 0.4638 0.0455  -0.0736 -0.0821 711  TYR   A C    
1479 O  O    . TYR   A 217 ? 0.5249 0.5176 0.4422 0.0450  -0.0711 -0.0825 711  TYR   A O    
1480 C  CB   . TYR   A 217 ? 0.5562 0.5807 0.4545 0.0465  -0.0641 -0.0704 711  TYR   A CB   
1481 C  CG   . TYR   A 217 ? 0.5744 0.6123 0.4577 0.0495  -0.0620 -0.0688 711  TYR   A CG   
1482 C  CD1  . TYR   A 217 ? 0.5612 0.6093 0.4365 0.0546  -0.0553 -0.0704 711  TYR   A CD1  
1483 C  CD2  . TYR   A 217 ? 0.6104 0.6519 0.4877 0.0471  -0.0667 -0.0655 711  TYR   A CD2  
1484 C  CE1  . TYR   A 217 ? 0.6066 0.6688 0.4680 0.0568  -0.0530 -0.0685 711  TYR   A CE1  
1485 C  CE2  . TYR   A 217 ? 0.6115 0.6653 0.4741 0.0492  -0.0648 -0.0635 711  TYR   A CE2  
1486 C  CZ   . TYR   A 217 ? 0.6630 0.7276 0.5177 0.0538  -0.0576 -0.0649 711  TYR   A CZ   
1487 O  OH   . TYR   A 217 ? 0.6592 0.7379 0.4994 0.0553  -0.0553 -0.0623 711  TYR   A OH   
1488 N  N    . GLU   A 218 ? 0.5267 0.5240 0.4379 0.0413  -0.0807 -0.0816 712  GLU   A N    
1489 C  CA   . GLU   A 218 ? 0.5479 0.5349 0.4723 0.0358  -0.0857 -0.0822 712  GLU   A CA   
1490 C  C    . GLU   A 218 ? 0.5104 0.5002 0.4506 0.0305  -0.0812 -0.0731 712  GLU   A C    
1491 O  O    . GLU   A 218 ? 0.5030 0.4854 0.4550 0.0267  -0.0817 -0.0730 712  GLU   A O    
1492 C  CB   . GLU   A 218 ? 0.5535 0.5385 0.4758 0.0331  -0.0952 -0.0852 712  GLU   A CB   
1493 C  CG   . GLU   A 218 ? 0.5579 0.5395 0.4630 0.0384  -0.1007 -0.0948 712  GLU   A CG   
1494 C  CD   . GLU   A 218 ? 0.6433 0.6100 0.5461 0.0403  -0.1040 -0.1041 712  GLU   A CD   
1495 O  OE1  . GLU   A 218 ? 0.6244 0.5825 0.5400 0.0356  -0.1042 -0.1028 712  GLU   A OE1  
1496 O  OE2  . GLU   A 218 ? 0.6821 0.6452 0.5697 0.0466  -0.1067 -0.1127 712  GLU   A OE2  
1497 N  N    . SER   A 219 ? 0.4652 0.4651 0.4053 0.0302  -0.0767 -0.0655 713  SER   A N    
1498 C  CA   . SER   A 219 ? 0.4661 0.4681 0.4197 0.0261  -0.0726 -0.0574 713  SER   A CA   
1499 C  C    . SER   A 219 ? 0.4794 0.4899 0.4283 0.0275  -0.0656 -0.0510 713  SER   A C    
1500 O  O    . SER   A 219 ? 0.4852 0.5023 0.4212 0.0306  -0.0648 -0.0514 713  SER   A O    
1501 C  CB   . SER   A 219 ? 0.5307 0.5342 0.4928 0.0219  -0.0781 -0.0537 713  SER   A CB   
1502 O  OG   . SER   A 219 ? 0.5082 0.5187 0.4610 0.0232  -0.0804 -0.0508 713  SER   A OG   
1503 N  N    . ALA   A 220 ? 0.4324 0.4430 0.3917 0.0249  -0.0605 -0.0451 714  ALA   A N    
1504 C  CA   . ALA   A 220 ? 0.4554 0.4730 0.4116 0.0249  -0.0543 -0.0384 714  ALA   A CA   
1505 C  C    . ALA   A 220 ? 0.5160 0.5391 0.4663 0.0238  -0.0567 -0.0327 714  ALA   A C    
1506 O  O    . ALA   A 220 ? 0.4710 0.5012 0.4119 0.0245  -0.0533 -0.0290 714  ALA   A O    
1507 C  CB   . ALA   A 220 ? 0.4147 0.4295 0.3834 0.0221  -0.0497 -0.0338 714  ALA   A CB   
1508 N  N    . ALA   A 221 ? 0.5080 0.5287 0.4639 0.0218  -0.0627 -0.0315 715  ALA   A N    
1509 C  CA   . ALA   A 221 ? 0.5074 0.5320 0.4577 0.0211  -0.0658 -0.0257 715  ALA   A CA   
1510 C  C    . ALA   A 221 ? 0.5180 0.5479 0.4521 0.0236  -0.0682 -0.0282 715  ALA   A C    
1511 O  O    . ALA   A 221 ? 0.5430 0.5781 0.4677 0.0232  -0.0673 -0.0223 715  ALA   A O    
1512 C  CB   . ALA   A 221 ? 0.5162 0.5382 0.4765 0.0196  -0.0724 -0.0248 715  ALA   A CB   
1513 N  N    . GLU   A 222 ? 0.5078 0.5359 0.4377 0.0261  -0.0715 -0.0368 716  GLU   A N    
1514 C  CA   . GLU   A 222 ? 0.5553 0.5884 0.4686 0.0294  -0.0735 -0.0405 716  GLU   A CA   
1515 C  C    . GLU   A 222 ? 0.5479 0.5887 0.4516 0.0318  -0.0659 -0.0394 716  GLU   A C    
1516 O  O    . GLU   A 222 ? 0.5321 0.5811 0.4221 0.0332  -0.0654 -0.0379 716  GLU   A O    
1517 C  CB   . GLU   A 222 ? 0.5010 0.5286 0.4118 0.0319  -0.0790 -0.0510 716  GLU   A CB   
1518 C  CG   . GLU   A 222 ? 0.5665 0.5903 0.4825 0.0295  -0.0881 -0.0524 716  GLU   A CG   
1519 C  CD   . GLU   A 222 ? 0.5845 0.6003 0.5011 0.0302  -0.0934 -0.0625 716  GLU   A CD   
1520 O  OE1  . GLU   A 222 ? 0.6718 0.6809 0.6016 0.0275  -0.0935 -0.0639 716  GLU   A OE1  
1521 O  OE2  . GLU   A 222 ? 0.7174 0.7333 0.6208 0.0333  -0.0979 -0.0688 716  GLU   A OE2  
1522 N  N    . ALA   A 223 ? 0.4912 0.5304 0.4019 0.0322  -0.0599 -0.0405 717  ALA   A N    
1523 C  CA   . ALA   A 223 ? 0.5725 0.6208 0.4760 0.0344  -0.0526 -0.0393 717  ALA   A CA   
1524 C  C    . ALA   A 223 ? 0.5494 0.6046 0.4520 0.0301  -0.0488 -0.0284 717  ALA   A C    
1525 O  O    . ALA   A 223 ? 0.5579 0.6239 0.4493 0.0306  -0.0454 -0.0256 717  ALA   A O    
1526 C  CB   . ALA   A 223 ? 0.5174 0.5620 0.4292 0.0362  -0.0480 -0.0431 717  ALA   A CB   
1527 N  N    . ILE   A 224 ? 0.5604 0.6091 0.4743 0.0257  -0.0494 -0.0224 718  ILE   A N    
1528 C  CA   . ILE   A 224 ? 0.5268 0.5787 0.4398 0.0213  -0.0471 -0.0121 718  ILE   A CA   
1529 C  C    . ILE   A 224 ? 0.5953 0.6516 0.4956 0.0205  -0.0511 -0.0079 718  ILE   A C    
1530 O  O    . ILE   A 224 ? 0.6227 0.6872 0.5135 0.0184  -0.0478 -0.0019 718  ILE   A O    
1531 C  CB   . ILE   A 224 ? 0.5674 0.6098 0.4942 0.0181  -0.0483 -0.0079 718  ILE   A CB   
1532 C  CG1  . ILE   A 224 ? 0.5795 0.6190 0.5171 0.0183  -0.0433 -0.0106 718  ILE   A CG1  
1533 C  CG2  . ILE   A 224 ? 0.5772 0.6196 0.5013 0.0139  -0.0480 0.0024  718  ILE   A CG2  
1534 C  CD1  . ILE   A 224 ? 0.5611 0.5915 0.5130 0.0167  -0.0450 -0.0098 718  ILE   A CD1  
1535 N  N    . GLN   A 225 ? 0.5912 0.6427 0.4911 0.0218  -0.0585 -0.0108 719  GLN   A N    
1536 C  CA   . GLN   A 225 ? 0.6179 0.6733 0.5050 0.0216  -0.0632 -0.0074 719  GLN   A CA   
1537 C  C    . GLN   A 225 ? 0.6700 0.7367 0.5413 0.0242  -0.0602 -0.0103 719  GLN   A C    
1538 O  O    . GLN   A 225 ? 0.6303 0.7041 0.4895 0.0222  -0.0598 -0.0038 719  GLN   A O    
1539 C  CB   . GLN   A 225 ? 0.6173 0.6669 0.5073 0.0232  -0.0720 -0.0119 719  GLN   A CB   
1540 C  CG   . GLN   A 225 ? 0.6947 0.7468 0.5728 0.0228  -0.0781 -0.0072 719  GLN   A CG   
1541 C  CD   . GLN   A 225 ? 0.7366 0.7858 0.6155 0.0190  -0.0783 0.0042  719  GLN   A CD   
1542 O  OE1  . GLN   A 225 ? 0.7573 0.7990 0.6485 0.0181  -0.0810 0.0067  719  GLN   A OE1  
1543 N  NE2  . GLN   A 225 ? 0.7048 0.7601 0.5706 0.0167  -0.0754 0.0111  719  GLN   A NE2  
1544 N  N    . ALA   A 226 ? 0.6266 0.6951 0.4973 0.0287  -0.0582 -0.0200 720  ALA   A N    
1545 C  CA   . ALA   A 226 ? 0.6235 0.7037 0.4792 0.0326  -0.0550 -0.0239 720  ALA   A CA   
1546 C  C    . ALA   A 226 ? 0.6377 0.7295 0.4900 0.0301  -0.0467 -0.0167 720  ALA   A C    
1547 O  O    . ALA   A 226 ? 0.6786 0.7831 0.5170 0.0307  -0.0443 -0.0147 720  ALA   A O    
1548 C  CB   . ALA   A 226 ? 0.5947 0.6725 0.4510 0.0388  -0.0549 -0.0362 720  ALA   A CB   
1549 N  N    . VAL   A 227 ? 0.5669 0.6556 0.4315 0.0269  -0.0423 -0.0126 721  VAL   A N    
1550 C  CA   . VAL   A 227 ? 0.6537 0.7534 0.5158 0.0231  -0.0352 -0.0049 721  VAL   A CA   
1551 C  C    . VAL   A 227 ? 0.7140 0.8150 0.5690 0.0168  -0.0373 0.0065  721  VAL   A C    
1552 O  O    . VAL   A 227 ? 0.6927 0.8066 0.5372 0.0141  -0.0334 0.0123  721  VAL   A O    
1553 C  CB   . VAL   A 227 ? 0.6091 0.7044 0.4857 0.0211  -0.0308 -0.0035 721  VAL   A CB   
1554 C  CG1  . VAL   A 227 ? 0.5599 0.6659 0.4344 0.0157  -0.0247 0.0057  721  VAL   A CG1  
1555 C  CG2  . VAL   A 227 ? 0.5480 0.6434 0.4293 0.0276  -0.0284 -0.0140 721  VAL   A CG2  
1556 N  N    . ARG   A 228 ? 0.6939 0.7817 0.5541 0.0145  -0.0437 0.0099  722  ARG   A N    
1557 C  CA   . ARG   A 228 ? 0.7352 0.8209 0.5886 0.0091  -0.0470 0.0207  722  ARG   A CA   
1558 C  C    . ARG   A 228 ? 0.6958 0.7907 0.5316 0.0101  -0.0494 0.0216  722  ARG   A C    
1559 O  O    . ARG   A 228 ? 0.7664 0.8663 0.5921 0.0050  -0.0488 0.0313  722  ARG   A O    
1560 C  CB   . ARG   A 228 ? 0.6962 0.7663 0.5591 0.0087  -0.0542 0.0222  722  ARG   A CB   
1561 C  CG   . ARG   A 228 ? 0.7512 0.8122 0.6281 0.0056  -0.0521 0.0259  722  ARG   A CG   
1562 C  CD   . ARG   A 228 ? 0.7842 0.8376 0.6585 0.0006  -0.0554 0.0370  722  ARG   A CD   
1563 N  NE   . ARG   A 228 ? 0.7889 0.8320 0.6663 0.0027  -0.0636 0.0373  722  ARG   A NE   
1564 C  CZ   . ARG   A 228 ? 0.7063 0.7381 0.5881 0.0008  -0.0674 0.0438  722  ARG   A CZ   
1565 N  NH1  . ARG   A 228 ? 0.6881 0.7158 0.5700 -0.0042 -0.0642 0.0512  722  ARG   A NH1  
1566 N  NH2  . ARG   A 228 ? 0.8361 0.8608 0.7222 0.0041  -0.0748 0.0428  722  ARG   A NH2  
1567 N  N    . ASP   A 229 ? 0.6659 0.7627 0.4974 0.0162  -0.0523 0.0117  723  ASP   A N    
1568 C  CA   . ASP   A 229 ? 0.7467 0.8519 0.5610 0.0182  -0.0551 0.0109  723  ASP   A CA   
1569 C  C    . ASP   A 229 ? 0.7862 0.9088 0.5894 0.0209  -0.0480 0.0074  723  ASP   A C    
1570 O  O    . ASP   A 229 ? 0.7953 0.9260 0.5838 0.0243  -0.0498 0.0039  723  ASP   A O    
1571 C  CB   . ASP   A 229 ? 0.7511 0.8487 0.5658 0.0234  -0.0630 0.0014  723  ASP   A CB   
1572 C  CG   . ASP   A 229 ? 0.7841 0.8679 0.6087 0.0211  -0.0705 0.0051  723  ASP   A CG   
1573 O  OD1  . ASP   A 229 ? 0.7295 0.8059 0.5614 0.0243  -0.0759 -0.0027 723  ASP   A OD1  
1574 O  OD2  . ASP   A 229 ? 0.7655 0.8459 0.5906 0.0161  -0.0709 0.0159  723  ASP   A OD2  
1575 N  N    . ASN   A 230 ? 0.7823 0.9116 0.5922 0.0202  -0.0402 0.0077  724  ASN   A N    
1576 C  CA   . ASN   A 230 ? 0.8225 0.9706 0.6240 0.0233  -0.0327 0.0045  724  ASN   A CA   
1577 C  C    . ASN   A 230 ? 0.8342 0.9850 0.6296 0.0330  -0.0340 -0.0095 724  ASN   A C    
1578 O  O    . ASN   A 230 ? 0.9082 1.0753 0.6910 0.0371  -0.0300 -0.0129 724  ASN   A O    
1579 C  CB   . ASN   A 230 ? 0.9140 1.0771 0.7004 0.0181  -0.0300 0.0146  724  ASN   A CB   
1580 C  CG   . ASN   A 230 ? 1.0525 1.2350 0.8381 0.0164  -0.0204 0.0175  724  ASN   A CG   
1581 O  OD1  . ASN   A 230 ? 1.1902 1.3910 0.9645 0.0207  -0.0160 0.0135  724  ASN   A OD1  
1582 N  ND2  . ASN   A 230 ? 0.9788 1.1581 0.7767 0.0105  -0.0171 0.0240  724  ASN   A ND2  
1583 N  N    . LYS   A 231 ? 0.7680 0.9031 0.5721 0.0367  -0.0397 -0.0179 725  LYS   A N    
1584 C  CA   . LYS   A 231 ? 0.6939 0.8280 0.4937 0.0456  -0.0416 -0.0317 725  LYS   A CA   
1585 C  C    . LYS   A 231 ? 0.7107 0.8419 0.5218 0.0498  -0.0372 -0.0387 725  LYS   A C    
1586 O  O    . LYS   A 231 ? 0.6648 0.7981 0.4706 0.0579  -0.0369 -0.0498 725  LYS   A O    
1587 C  CB   . LYS   A 231 ? 0.7188 0.8374 0.5193 0.0466  -0.0516 -0.0370 725  LYS   A CB   
1588 N  N    . LEU   A 232 ? 0.6815 0.8074 0.5075 0.0449  -0.0344 -0.0328 726  LEU   A N    
1589 C  CA   . LEU   A 232 ? 0.6104 0.7358 0.4468 0.0479  -0.0294 -0.0370 726  LEU   A CA   
1590 C  C    . LEU   A 232 ? 0.6021 0.7394 0.4426 0.0425  -0.0219 -0.0271 726  LEU   A C    
1591 O  O    . LEU   A 232 ? 0.6648 0.7985 0.5092 0.0345  -0.0227 -0.0168 726  LEU   A O    
1592 C  CB   . LEU   A 232 ? 0.6304 0.7366 0.4820 0.0468  -0.0337 -0.0399 726  LEU   A CB   
1593 C  CG   . LEU   A 232 ? 0.5734 0.6767 0.4366 0.0489  -0.0292 -0.0429 726  LEU   A CG   
1594 C  CD1  . LEU   A 232 ? 0.5703 0.6787 0.4267 0.0584  -0.0273 -0.0539 726  LEU   A CD1  
1595 C  CD2  . LEU   A 232 ? 0.5328 0.6179 0.4097 0.0463  -0.0339 -0.0441 726  LEU   A CD2  
1596 N  N    . HIS   A 233 ? 0.5918 0.7428 0.4315 0.0468  -0.0152 -0.0302 727  HIS   A N    
1597 C  CA   . HIS   A 233 ? 0.5246 0.6897 0.3671 0.0408  -0.0083 -0.0204 727  HIS   A CA   
1598 C  C    . HIS   A 233 ? 0.5743 0.7315 0.4329 0.0377  -0.0061 -0.0178 727  HIS   A C    
1599 O  O    . HIS   A 233 ? 0.5743 0.7351 0.4372 0.0297  -0.0033 -0.0076 727  HIS   A O    
1600 C  CB   . HIS   A 233 ? 0.5843 0.7729 0.4173 0.0463  -0.0017 -0.0236 727  HIS   A CB   
1601 C  CG   . HIS   A 233 ? 0.6225 0.8199 0.4383 0.0499  -0.0034 -0.0265 727  HIS   A CG   
1602 N  ND1  . HIS   A 233 ? 0.7257 0.9245 0.5328 0.0428  -0.0060 -0.0175 727  HIS   A ND1  
1603 C  CD2  . HIS   A 233 ? 0.6076 0.8127 0.4126 0.0600  -0.0033 -0.0375 727  HIS   A CD2  
1604 C  CE1  . HIS   A 233 ? 0.6968 0.9043 0.4884 0.0480  -0.0072 -0.0226 727  HIS   A CE1  
1605 N  NE2  . HIS   A 233 ? 0.7015 0.9131 0.4913 0.0586  -0.0055 -0.0350 727  HIS   A NE2  
1606 N  N    . ALA   A 234 ? 0.5415 0.6871 0.4084 0.0433  -0.0077 -0.0265 728  ALA   A N    
1607 C  CA   . ALA   A 234 ? 0.5141 0.6511 0.3957 0.0404  -0.0061 -0.0241 728  ALA   A CA   
1608 C  C    . ALA   A 234 ? 0.5096 0.6266 0.3986 0.0437  -0.0116 -0.0316 728  ALA   A C    
1609 O  O    . ALA   A 234 ? 0.4843 0.5977 0.3684 0.0510  -0.0143 -0.0414 728  ALA   A O    
1610 C  CB   . ALA   A 234 ? 0.4890 0.6404 0.3736 0.0439  0.0008  -0.0257 728  ALA   A CB   
1611 N  N    . PHE   A 235 ? 0.4624 0.5666 0.3628 0.0379  -0.0134 -0.0267 729  PHE   A N    
1612 C  CA   . PHE   A 235 ? 0.4597 0.5461 0.3689 0.0390  -0.0182 -0.0318 729  PHE   A CA   
1613 C  C    . PHE   A 235 ? 0.4679 0.5503 0.3891 0.0381  -0.0147 -0.0308 729  PHE   A C    
1614 O  O    . PHE   A 235 ? 0.4741 0.5573 0.4014 0.0321  -0.0122 -0.0228 729  PHE   A O    
1615 C  CB   . PHE   A 235 ? 0.5075 0.5839 0.4195 0.0335  -0.0237 -0.0270 729  PHE   A CB   
1616 C  CG   . PHE   A 235 ? 0.4733 0.5339 0.3954 0.0335  -0.0284 -0.0311 729  PHE   A CG   
1617 C  CD1  . PHE   A 235 ? 0.4694 0.5236 0.3914 0.0388  -0.0309 -0.0406 729  PHE   A CD1  
1618 C  CD2  . PHE   A 235 ? 0.4710 0.5235 0.4024 0.0281  -0.0307 -0.0253 729  PHE   A CD2  
1619 C  CE1  . PHE   A 235 ? 0.4995 0.5399 0.4309 0.0375  -0.0353 -0.0435 729  PHE   A CE1  
1620 C  CE2  . PHE   A 235 ? 0.4637 0.5043 0.4050 0.0276  -0.0345 -0.0286 729  PHE   A CE2  
1621 C  CZ   . PHE   A 235 ? 0.4927 0.5276 0.4342 0.0317  -0.0368 -0.0374 729  PHE   A CZ   
1622 N  N    . ILE   A 236 ? 0.4333 0.5103 0.3570 0.0440  -0.0150 -0.0388 730  ILE   A N    
1623 C  CA   . ILE   A 236 ? 0.4423 0.5151 0.3763 0.0438  -0.0120 -0.0383 730  ILE   A CA   
1624 C  C    . ILE   A 236 ? 0.4400 0.4953 0.3835 0.0407  -0.0164 -0.0389 730  ILE   A C    
1625 O  O    . ILE   A 236 ? 0.4471 0.4925 0.3893 0.0434  -0.0214 -0.0454 730  ILE   A O    
1626 C  CB   . ILE   A 236 ? 0.4170 0.4940 0.3480 0.0523  -0.0098 -0.0461 730  ILE   A CB   
1627 C  CG1  . ILE   A 236 ? 0.4580 0.5552 0.3792 0.0559  -0.0055 -0.0461 730  ILE   A CG1  
1628 C  CG2  . ILE   A 236 ? 0.4056 0.4797 0.3467 0.0521  -0.0067 -0.0447 730  ILE   A CG2  
1629 C  CD1  . ILE   A 236 ? 0.4666 0.5704 0.3844 0.0658  -0.0032 -0.0540 730  ILE   A CD1  
1630 N  N    . TRP   A 237 ? 0.4192 0.4710 0.3721 0.0348  -0.0148 -0.0322 731  TRP   A N    
1631 C  CA   . TRP   A 237 ? 0.4517 0.4898 0.4136 0.0315  -0.0186 -0.0319 731  TRP   A CA   
1632 C  C    . TRP   A 237 ? 0.4414 0.4769 0.4131 0.0271  -0.0153 -0.0261 731  TRP   A C    
1633 O  O    . TRP   A 237 ? 0.4613 0.5048 0.4329 0.0264  -0.0106 -0.0225 731  TRP   A O    
1634 C  CB   . TRP   A 237 ? 0.4119 0.4480 0.3714 0.0286  -0.0234 -0.0298 731  TRP   A CB   
1635 C  CG   . TRP   A 237 ? 0.4389 0.4634 0.4066 0.0265  -0.0283 -0.0313 731  TRP   A CG   
1636 C  CD1  . TRP   A 237 ? 0.4119 0.4332 0.3860 0.0221  -0.0303 -0.0262 731  TRP   A CD1  
1637 C  CD2  . TRP   A 237 ? 0.4610 0.4764 0.4315 0.0284  -0.0320 -0.0382 731  TRP   A CD2  
1638 N  NE1  . TRP   A 237 ? 0.4395 0.4526 0.4212 0.0212  -0.0345 -0.0294 731  TRP   A NE1  
1639 C  CE2  . TRP   A 237 ? 0.4561 0.4650 0.4356 0.0243  -0.0357 -0.0365 731  TRP   A CE2  
1640 C  CE3  . TRP   A 237 ? 0.4485 0.4600 0.4146 0.0333  -0.0328 -0.0458 731  TRP   A CE3  
1641 C  CZ2  . TRP   A 237 ? 0.4318 0.4317 0.4164 0.0237  -0.0400 -0.0413 731  TRP   A CZ2  
1642 C  CZ3  . TRP   A 237 ? 0.4534 0.4532 0.4236 0.0329  -0.0377 -0.0507 731  TRP   A CZ3  
1643 C  CH2  . TRP   A 237 ? 0.3831 0.3778 0.3627 0.0274  -0.0412 -0.0481 731  TRP   A CH2  
1644 N  N    . ASP   A 238 ? 0.4049 0.4301 0.3852 0.0242  -0.0179 -0.0255 732  ASP   A N    
1645 C  CA   . ASP   A 238 ? 0.3766 0.3980 0.3662 0.0204  -0.0154 -0.0209 732  ASP   A CA   
1646 C  C    . ASP   A 238 ? 0.4154 0.4418 0.4040 0.0163  -0.0135 -0.0134 732  ASP   A C    
1647 O  O    . ASP   A 238 ? 0.3905 0.4170 0.3761 0.0145  -0.0164 -0.0106 732  ASP   A O    
1648 C  CB   . ASP   A 238 ? 0.4011 0.4126 0.3993 0.0183  -0.0189 -0.0218 732  ASP   A CB   
1649 C  CG   . ASP   A 238 ? 0.4374 0.4417 0.4379 0.0205  -0.0208 -0.0279 732  ASP   A CG   
1650 O  OD1  . ASP   A 238 ? 0.4585 0.4622 0.4587 0.0229  -0.0179 -0.0297 732  ASP   A OD1  
1651 O  OD2  . ASP   A 238 ? 0.4412 0.4403 0.4439 0.0197  -0.0256 -0.0309 732  ASP   A OD2  
1652 N  N    . SER   A 239 ? 0.4344 0.4637 0.4253 0.0146  -0.0091 -0.0100 733  SER   A N    
1653 C  CA   . SER   A 239 ? 0.3966 0.4296 0.3856 0.0101  -0.0076 -0.0028 733  SER   A CA   
1654 C  C    . SER   A 239 ? 0.3976 0.4217 0.3915 0.0070  -0.0105 0.0008  733  SER   A C    
1655 O  O    . SER   A 239 ? 0.4185 0.4430 0.4082 0.0040  -0.0119 0.0060  733  SER   A O    
1656 C  CB   . SER   A 239 ? 0.4654 0.5029 0.4565 0.0086  -0.0030 -0.0005 733  SER   A CB   
1657 O  OG   . SER   A 239 ? 0.4140 0.4437 0.4134 0.0087  -0.0022 -0.0019 733  SER   A OG   
1658 N  N    . ALA   A 240 ? 0.4140 0.4304 0.4163 0.0076  -0.0114 -0.0017 734  ALA   A N    
1659 C  CA   . ALA   A 240 ? 0.4573 0.4671 0.4648 0.0058  -0.0139 0.0010  734  ALA   A CA   
1660 C  C    . ALA   A 240 ? 0.4539 0.4636 0.4576 0.0064  -0.0188 0.0014  734  ALA   A C    
1661 O  O    . ALA   A 240 ? 0.4295 0.4357 0.4334 0.0050  -0.0212 0.0055  734  ALA   A O    
1662 C  CB   . ALA   A 240 ? 0.4236 0.4279 0.4408 0.0066  -0.0138 -0.0021 734  ALA   A CB   
1663 N  N    . VAL   A 241 ? 0.3990 0.4119 0.3986 0.0088  -0.0208 -0.0029 735  VAL   A N    
1664 C  CA   . VAL   A 241 ? 0.4129 0.4267 0.4075 0.0094  -0.0258 -0.0026 735  VAL   A CA   
1665 C  C    . VAL   A 241 ? 0.4719 0.4916 0.4555 0.0081  -0.0253 0.0020  735  VAL   A C    
1666 O  O    . VAL   A 241 ? 0.4557 0.4735 0.4360 0.0064  -0.0283 0.0068  735  VAL   A O    
1667 C  CB   . VAL   A 241 ? 0.4603 0.4745 0.4543 0.0123  -0.0288 -0.0095 735  VAL   A CB   
1668 C  CG1  . VAL   A 241 ? 0.4269 0.4430 0.4141 0.0130  -0.0342 -0.0094 735  VAL   A CG1  
1669 C  CG2  . VAL   A 241 ? 0.4366 0.4450 0.4417 0.0121  -0.0300 -0.0129 735  VAL   A CG2  
1670 N  N    . LEU   A 242 ? 0.4341 0.4613 0.4116 0.0089  -0.0216 0.0006  736  LEU   A N    
1671 C  CA   . LEU   A 242 ? 0.4370 0.4726 0.4037 0.0074  -0.0206 0.0048  736  LEU   A CA   
1672 C  C    . LEU   A 242 ? 0.4632 0.4967 0.4290 0.0021  -0.0198 0.0132  736  LEU   A C    
1673 O  O    . LEU   A 242 ? 0.4569 0.4914 0.4151 -0.0003 -0.0222 0.0185  736  LEU   A O    
1674 C  CB   . LEU   A 242 ? 0.4062 0.4522 0.3684 0.0096  -0.0159 0.0017  736  LEU   A CB   
1675 C  CG   . LEU   A 242 ? 0.4162 0.4638 0.3756 0.0154  -0.0173 -0.0068 736  LEU   A CG   
1676 C  CD1  . LEU   A 242 ? 0.4329 0.4920 0.3869 0.0192  -0.0128 -0.0104 736  LEU   A CD1  
1677 C  CD2  . LEU   A 242 ? 0.4895 0.5367 0.4419 0.0162  -0.0224 -0.0076 736  LEU   A CD2  
1678 N  N    . GLU   A 243 ? 0.4422 0.4721 0.4151 0.0003  -0.0169 0.0146  737  GLU   A N    
1679 C  CA   . GLU   A 243 ? 0.4857 0.5117 0.4573 -0.0049 -0.0167 0.0221  737  GLU   A CA   
1680 C  C    . GLU   A 243 ? 0.5565 0.5719 0.5290 -0.0052 -0.0221 0.0250  737  GLU   A C    
1681 O  O    . GLU   A 243 ? 0.5491 0.5609 0.5157 -0.0090 -0.0242 0.0317  737  GLU   A O    
1682 C  CB   . GLU   A 243 ? 0.4784 0.5022 0.4573 -0.0062 -0.0129 0.0218  737  GLU   A CB   
1683 C  CG   . GLU   A 243 ? 0.5230 0.5586 0.4993 -0.0076 -0.0080 0.0222  737  GLU   A CG   
1684 C  CD   . GLU   A 243 ? 0.5859 0.6198 0.5699 -0.0075 -0.0047 0.0203  737  GLU   A CD   
1685 O  OE1  . GLU   A 243 ? 0.6533 0.6969 0.6370 -0.0067 -0.0009 0.0188  737  GLU   A OE1  
1686 O  OE2  . GLU   A 243 ? 0.6313 0.6545 0.6214 -0.0076 -0.0060 0.0200  737  GLU   A OE2  
1687 N  N    . PHE   A 244 ? 0.5203 0.5306 0.4999 -0.0014 -0.0248 0.0203  738  PHE   A N    
1688 C  CA   . PHE   A 244 ? 0.5119 0.5143 0.4928 -0.0005 -0.0302 0.0225  738  PHE   A CA   
1689 C  C    . PHE   A 244 ? 0.5502 0.5553 0.5213 -0.0006 -0.0344 0.0251  738  PHE   A C    
1690 O  O    . PHE   A 244 ? 0.5066 0.5059 0.4729 -0.0022 -0.0382 0.0309  738  PHE   A O    
1691 C  CB   . PHE   A 244 ? 0.5399 0.5393 0.5317 0.0033  -0.0318 0.0169  738  PHE   A CB   
1692 C  CG   . PHE   A 244 ? 0.5477 0.5421 0.5416 0.0053  -0.0377 0.0184  738  PHE   A CG   
1693 C  CD1  . PHE   A 244 ? 0.5864 0.5726 0.5834 0.0054  -0.0390 0.0218  738  PHE   A CD1  
1694 C  CD2  . PHE   A 244 ? 0.5103 0.5079 0.5023 0.0074  -0.0423 0.0162  738  PHE   A CD2  
1695 C  CE1  . PHE   A 244 ? 0.6177 0.5998 0.6167 0.0084  -0.0448 0.0229  738  PHE   A CE1  
1696 C  CE2  . PHE   A 244 ? 0.5496 0.5436 0.5437 0.0097  -0.0481 0.0177  738  PHE   A CE2  
1697 C  CZ   . PHE   A 244 ? 0.5616 0.5482 0.5596 0.0105  -0.0493 0.0211  738  PHE   A CZ   
1698 N  N    . GLU   A 245 ? 0.4999 0.5131 0.4670 0.0014  -0.0341 0.0208  739  GLU   A N    
1699 C  CA   . GLU   A 245 ? 0.5130 0.5301 0.4694 0.0014  -0.0378 0.0231  739  GLU   A CA   
1700 C  C    . GLU   A 245 ? 0.5913 0.6105 0.5372 -0.0036 -0.0365 0.0313  739  GLU   A C    
1701 O  O    . GLU   A 245 ? 0.6005 0.6161 0.5391 -0.0052 -0.0411 0.0370  739  GLU   A O    
1702 C  CB   . GLU   A 245 ? 0.5139 0.5396 0.4665 0.0045  -0.0369 0.0163  739  GLU   A CB   
1703 C  CG   . GLU   A 245 ? 0.5027 0.5251 0.4637 0.0083  -0.0402 0.0090  739  GLU   A CG   
1704 C  CD   . GLU   A 245 ? 0.6154 0.6344 0.5755 0.0094  -0.0473 0.0101  739  GLU   A CD   
1705 O  OE1  . GLU   A 245 ? 0.6464 0.6656 0.5974 0.0079  -0.0499 0.0160  739  GLU   A OE1  
1706 O  OE2  . GLU   A 245 ? 0.5496 0.5662 0.5181 0.0116  -0.0507 0.0053  739  GLU   A OE2  
1707 N  N    . ALA   A 246 ? 0.5340 0.5590 0.4794 -0.0065 -0.0308 0.0326  740  ALA   A N    
1708 C  CA   . ALA   A 246 ? 0.5782 0.6069 0.5141 -0.0125 -0.0294 0.0409  740  ALA   A CA   
1709 C  C    . ALA   A 246 ? 0.6230 0.6385 0.5593 -0.0166 -0.0327 0.0480  740  ALA   A C    
1710 O  O    . ALA   A 246 ? 0.6653 0.6792 0.5919 -0.0215 -0.0349 0.0560  740  ALA   A O    
1711 C  CB   . ALA   A 246 ? 0.5939 0.6337 0.5307 -0.0147 -0.0225 0.0403  740  ALA   A CB   
1712 N  N    . SER   A 247 ? 0.6148 0.6202 0.5614 -0.0145 -0.0334 0.0454  741  SER   A N    
1713 C  CA   . SER   A 247 ? 0.6078 0.5992 0.5546 -0.0169 -0.0370 0.0509  741  SER   A CA   
1714 C  C    . SER   A 247 ? 0.6694 0.6526 0.6118 -0.0146 -0.0442 0.0536  741  SER   A C    
1715 O  O    . SER   A 247 ? 0.6892 0.6610 0.6267 -0.0172 -0.0483 0.0601  741  SER   A O    
1716 C  CB   . SER   A 247 ? 0.5729 0.5575 0.5316 -0.0142 -0.0354 0.0463  741  SER   A CB   
1717 O  OG   . SER   A 247 ? 0.6215 0.6042 0.5882 -0.0079 -0.0379 0.0404  741  SER   A OG   
1718 N  N    . GLN   A 248 ? 0.6347 0.6232 0.5784 -0.0097 -0.0464 0.0488  742  GLN   A N    
1719 C  CA   . GLN   A 248 ? 0.6811 0.6636 0.6216 -0.0068 -0.0536 0.0507  742  GLN   A CA   
1720 C  C    . GLN   A 248 ? 0.7173 0.7055 0.6438 -0.0093 -0.0559 0.0555  742  GLN   A C    
1721 O  O    . GLN   A 248 ? 0.6688 0.6493 0.5879 -0.0100 -0.0618 0.0616  742  GLN   A O    
1722 C  CB   . GLN   A 248 ? 0.7244 0.7091 0.6753 -0.0004 -0.0555 0.0427  742  GLN   A CB   
1723 C  CG   . GLN   A 248 ? 0.8589 0.8377 0.8103 0.0037  -0.0633 0.0438  742  GLN   A CG   
1724 C  CD   . GLN   A 248 ? 0.8798 0.8666 0.8357 0.0078  -0.0656 0.0370  742  GLN   A CD   
1725 O  OE1  . GLN   A 248 ? 0.8628 0.8514 0.8119 0.0091  -0.0710 0.0384  742  GLN   A OE1  
1726 N  NE2  . GLN   A 248 ? 0.8037 0.7950 0.7705 0.0094  -0.0618 0.0299  742  GLN   A NE2  
1727 N  N    . LYS   A 249 ? 0.6813 0.6830 0.6034 -0.0104 -0.0513 0.0529  743  LYS   A N    
1728 C  CA   . LYS   A 249 ? 0.6868 0.6966 0.5954 -0.0120 -0.0527 0.0562  743  LYS   A CA   
1729 C  C    . LYS   A 249 ? 0.7244 0.7422 0.6247 -0.0188 -0.0474 0.0622  743  LYS   A C    
1730 O  O    . LYS   A 249 ? 0.6783 0.7070 0.5817 -0.0190 -0.0409 0.0582  743  LYS   A O    
1731 C  CB   . LYS   A 249 ? 0.6780 0.6979 0.5873 -0.0068 -0.0522 0.0475  743  LYS   A CB   
1732 C  CG   . LYS   A 249 ? 0.7206 0.7342 0.6375 -0.0013 -0.0583 0.0424  743  LYS   A CG   
1733 C  CD   . LYS   A 249 ? 0.6883 0.7089 0.6104 0.0031  -0.0571 0.0323  743  LYS   A CD   
1734 C  CE   . LYS   A 249 ? 0.6721 0.6872 0.6041 0.0072  -0.0631 0.0280  743  LYS   A CE   
1735 N  NZ   . LYS   A 249 ? 0.6141 0.6337 0.5526 0.0104  -0.0624 0.0184  743  LYS   A NZ   
1736 N  N    . CYS   A 250 ? 0.6864 0.6994 0.5762 -0.0246 -0.0504 0.0722  744  CYS   A N    
1737 C  CA   . CYS   A 250 ? 0.7485 0.7677 0.6322 -0.0327 -0.0458 0.0793  744  CYS   A CA   
1738 C  C    . CYS   A 250 ? 0.7031 0.7421 0.5775 -0.0343 -0.0410 0.0793  744  CYS   A C    
1739 O  O    . CYS   A 250 ? 0.7847 0.8335 0.6558 -0.0407 -0.0360 0.0841  744  CYS   A O    
1740 C  CB   . CYS   A 250 ? 0.8163 0.8216 0.6916 -0.0392 -0.0512 0.0906  744  CYS   A CB   
1741 S  SG   . CYS   A 250 ? 0.8852 0.8676 0.7709 -0.0374 -0.0557 0.0904  744  CYS   A SG   
1742 N  N    . ASP   A 251 ? 0.6264 0.6725 0.4966 -0.0286 -0.0424 0.0739  745  ASP   A N    
1743 C  CA   . ASP   A 251 ? 0.6677 0.7334 0.5295 -0.0282 -0.0375 0.0718  745  ASP   A CA   
1744 C  C    . ASP   A 251 ? 0.6643 0.7398 0.5350 -0.0221 -0.0319 0.0607  745  ASP   A C    
1745 O  O    . ASP   A 251 ? 0.5966 0.6880 0.4610 -0.0196 -0.0280 0.0568  745  ASP   A O    
1746 C  CB   . ASP   A 251 ? 0.6752 0.7432 0.5255 -0.0251 -0.0424 0.0715  745  ASP   A CB   
1747 C  CG   . ASP   A 251 ? 0.7561 0.8159 0.6136 -0.0170 -0.0473 0.0622  745  ASP   A CG   
1748 O  OD1  . ASP   A 251 ? 0.7588 0.8047 0.6277 -0.0155 -0.0505 0.0610  745  ASP   A OD1  
1749 O  OD2  . ASP   A 251 ? 0.7405 0.8088 0.5923 -0.0122 -0.0481 0.0561  745  ASP   A OD2  
1750 N  N    . LEU   A 252 ? 0.6152 0.6814 0.4996 -0.0195 -0.0315 0.0556  746  LEU   A N    
1751 C  CA   . LEU   A 252 ? 0.6424 0.7153 0.5357 -0.0143 -0.0266 0.0461  746  LEU   A CA   
1752 C  C    . LEU   A 252 ? 0.6264 0.6998 0.5275 -0.0184 -0.0217 0.0485  746  LEU   A C    
1753 O  O    . LEU   A 252 ? 0.6409 0.7025 0.5456 -0.0230 -0.0238 0.0544  746  LEU   A O    
1754 C  CB   . LEU   A 252 ? 0.5609 0.6230 0.4637 -0.0078 -0.0305 0.0376  746  LEU   A CB   
1755 C  CG   . LEU   A 252 ? 0.6227 0.6851 0.5186 -0.0034 -0.0356 0.0336  746  LEU   A CG   
1756 C  CD1  . LEU   A 252 ? 0.6260 0.6779 0.5329 0.0014  -0.0399 0.0265  746  LEU   A CD1  
1757 C  CD2  . LEU   A 252 ? 0.6085 0.6860 0.4959 0.0000  -0.0320 0.0282  746  LEU   A CD2  
1758 N  N    . VAL   A 253 ? 0.5790 0.6658 0.4826 -0.0161 -0.0156 0.0437  747  VAL   A N    
1759 C  CA   . VAL   A 253 ? 0.5557 0.6455 0.4668 -0.0195 -0.0109 0.0454  747  VAL   A CA   
1760 C  C    . VAL   A 253 ? 0.5537 0.6497 0.4724 -0.0124 -0.0070 0.0355  747  VAL   A C    
1761 O  O    . VAL   A 253 ? 0.5262 0.6297 0.4409 -0.0061 -0.0063 0.0286  747  VAL   A O    
1762 C  CB   . VAL   A 253 ? 0.6187 0.7229 0.5222 -0.0272 -0.0072 0.0541  747  VAL   A CB   
1763 C  CG1  . VAL   A 253 ? 0.5637 0.6902 0.4633 -0.0234 -0.0014 0.0497  747  VAL   A CG1  
1764 C  CG2  . VAL   A 253 ? 0.6511 0.7508 0.5613 -0.0340 -0.0057 0.0595  747  VAL   A CG2  
1765 N  N    . THR   A 254 ? 0.5307 0.6216 0.4595 -0.0133 -0.0050 0.0347  748  THR   A N    
1766 C  CA   . THR   A 254 ? 0.5621 0.6592 0.4975 -0.0076 -0.0011 0.0270  748  THR   A CA   
1767 C  C    . THR   A 254 ? 0.6198 0.7353 0.5535 -0.0101 0.0047  0.0298  748  THR   A C    
1768 O  O    . THR   A 254 ? 0.5627 0.6832 0.4933 -0.0180 0.0057  0.0384  748  THR   A O    
1769 C  CB   . THR   A 254 ? 0.5738 0.6572 0.5208 -0.0067 -0.0018 0.0244  748  THR   A CB   
1770 O  OG1  . THR   A 254 ? 0.6171 0.6994 0.5671 -0.0136 -0.0002 0.0312  748  THR   A OG1  
1771 C  CG2  . THR   A 254 ? 0.5313 0.5982 0.4812 -0.0053 -0.0073 0.0229  748  THR   A CG2  
1772 N  N    . THR   A 255 ? 0.5787 0.7040 0.5148 -0.0033 0.0081  0.0225  749  THR   A N    
1773 C  CA   . THR   A 255 ? 0.6690 0.8151 0.6040 -0.0038 0.0137  0.0239  749  THR   A CA   
1774 C  C    . THR   A 255 ? 0.7187 0.8649 0.6629 -0.0080 0.0160  0.0269  749  THR   A C    
1775 O  O    . THR   A 255 ? 0.8360 0.9999 0.7818 -0.0077 0.0206  0.0271  749  THR   A O    
1776 C  CB   . THR   A 255 ? 0.6712 0.8276 0.6042 0.0066  0.0159  0.0141  749  THR   A CB   
1777 O  OG1  . THR   A 255 ? 0.8323 1.0126 0.7628 0.0068  0.0214  0.0156  749  THR   A OG1  
1778 C  CG2  . THR   A 255 ? 0.5930 0.7379 0.5354 0.0125  0.0152  0.0069  749  THR   A CG2  
1779 N  N    . GLY   A 256 ? 0.8195 0.9475 0.7698 -0.0115 0.0130  0.0290  750  GLY   A N    
1780 C  CA   . GLY   A 256 ? 0.9016 1.0288 0.8594 -0.0159 0.0147  0.0319  750  GLY   A CA   
1781 C  C    . GLY   A 256 ? 0.8041 0.9169 0.7707 -0.0112 0.0135  0.0260  750  GLY   A C    
1782 O  O    . GLY   A 256 ? 0.9081 1.0035 0.8768 -0.0118 0.0098  0.0259  750  GLY   A O    
1783 N  N    . GLU   A 257 ? 0.7317 0.8522 0.7032 -0.0062 0.0165  0.0213  751  GLU   A N    
1784 C  CA   . GLU   A 257 ? 0.6683 0.7759 0.6478 -0.0034 0.0157  0.0174  751  GLU   A CA   
1785 C  C    . GLU   A 257 ? 0.6095 0.7125 0.5897 0.0060  0.0148  0.0085  751  GLU   A C    
1786 O  O    . GLU   A 257 ? 0.5608 0.6667 0.5350 0.0100  0.0138  0.0052  751  GLU   A O    
1787 C  CB   . GLU   A 257 ? 0.6943 0.8108 0.6792 -0.0056 0.0187  0.0193  751  GLU   A CB   
1788 N  N    . LEU   A 258 ? 0.5754 0.6703 0.5622 0.0092  0.0148  0.0048  752  LEU   A N    
1789 C  CA   . LEU   A 258 ? 0.5184 0.6058 0.5062 0.0170  0.0132  -0.0030 752  LEU   A CA   
1790 C  C    . LEU   A 258 ? 0.5199 0.6192 0.5074 0.0238  0.0159  -0.0075 752  LEU   A C    
1791 O  O    . LEU   A 258 ? 0.5343 0.6410 0.5258 0.0227  0.0184  -0.0053 752  LEU   A O    
1792 C  CB   . LEU   A 258 ? 0.5360 0.6066 0.5306 0.0162  0.0113  -0.0040 752  LEU   A CB   
1793 C  CG   . LEU   A 258 ? 0.5391 0.5999 0.5364 0.0093  0.0097  0.0014  752  LEU   A CG   
1794 C  CD1  . LEU   A 258 ? 0.5017 0.5488 0.5059 0.0097  0.0086  -0.0005 752  LEU   A CD1  
1795 C  CD2  . LEU   A 258 ? 0.4673 0.5251 0.4598 0.0082  0.0068  0.0021  752  LEU   A CD2  
1796 N  N    . PHE   A 259 ? 0.4760 0.5769 0.4584 0.0313  0.0149  -0.0141 753  PHE   A N    
1797 C  CA   . PHE   A 259 ? 0.5005 0.6095 0.4824 0.0398  0.0165  -0.0199 753  PHE   A CA   
1798 C  C    . PHE   A 259 ? 0.5044 0.5969 0.4900 0.0447  0.0138  -0.0252 753  PHE   A C    
1799 O  O    . PHE   A 259 ? 0.5131 0.6091 0.4986 0.0523  0.0143  -0.0299 753  PHE   A O    
1800 C  CB   . PHE   A 259 ? 0.5009 0.6213 0.4741 0.0463  0.0168  -0.0247 753  PHE   A CB   
1801 C  CG   . PHE   A 259 ? 0.4990 0.6059 0.4669 0.0486  0.0124  -0.0296 753  PHE   A CG   
1802 C  CD1  . PHE   A 259 ? 0.4991 0.5934 0.4658 0.0562  0.0091  -0.0378 753  PHE   A CD1  
1803 C  CD2  . PHE   A 259 ? 0.4417 0.5488 0.4050 0.0434  0.0111  -0.0261 753  PHE   A CD2  
1804 C  CE1  . PHE   A 259 ? 0.5182 0.6009 0.4801 0.0577  0.0045  -0.0423 753  PHE   A CE1  
1805 C  CE2  . PHE   A 259 ? 0.4532 0.5495 0.4116 0.0456  0.0067  -0.0307 753  PHE   A CE2  
1806 C  CZ   . PHE   A 259 ? 0.4628 0.5471 0.4208 0.0524  0.0034  -0.0389 753  PHE   A CZ   
1807 N  N    . PHE   A 260 ? 0.4593 0.5345 0.4485 0.0403  0.0109  -0.0240 754  PHE   A N    
1808 C  CA   . PHE   A 260 ? 0.4398 0.4990 0.4324 0.0433  0.0081  -0.0280 754  PHE   A CA   
1809 C  C    . PHE   A 260 ? 0.4629 0.5096 0.4613 0.0359  0.0068  -0.0237 754  PHE   A C    
1810 O  O    . PHE   A 260 ? 0.4562 0.5007 0.4537 0.0316  0.0054  -0.0215 754  PHE   A O    
1811 C  CB   . PHE   A 260 ? 0.4820 0.5335 0.4687 0.0496  0.0043  -0.0355 754  PHE   A CB   
1812 C  CG   . PHE   A 260 ? 0.4931 0.5271 0.4823 0.0520  0.0008  -0.0395 754  PHE   A CG   
1813 C  CD1  . PHE   A 260 ? 0.5143 0.5465 0.5046 0.0574  0.0012  -0.0417 754  PHE   A CD1  
1814 C  CD2  . PHE   A 260 ? 0.4944 0.5141 0.4845 0.0488  -0.0034 -0.0408 754  PHE   A CD2  
1815 C  CE1  . PHE   A 260 ? 0.5534 0.5684 0.5450 0.0590  -0.0024 -0.0447 754  PHE   A CE1  
1816 C  CE2  . PHE   A 260 ? 0.4683 0.4721 0.4605 0.0499  -0.0068 -0.0438 754  PHE   A CE2  
1817 C  CZ   . PHE   A 260 ? 0.4982 0.4988 0.4906 0.0548  -0.0064 -0.0455 754  PHE   A CZ   
1818 N  N    . ARG   A 261 ? 0.4038 0.4430 0.4078 0.0349  0.0071  -0.0226 755  ARG   A N    
1819 C  CA   . ARG   A 261 ? 0.4280 0.4563 0.4375 0.0287  0.0063  -0.0191 755  ARG   A CA   
1820 C  C    . ARG   A 261 ? 0.4299 0.4442 0.4405 0.0299  0.0025  -0.0231 755  ARG   A C    
1821 O  O    . ARG   A 261 ? 0.4406 0.4493 0.4495 0.0348  0.0009  -0.0275 755  ARG   A O    
1822 C  CB   . ARG   A 261 ? 0.3975 0.4251 0.4119 0.0264  0.0086  -0.0157 755  ARG   A CB   
1823 C  CG   . ARG   A 261 ? 0.5097 0.5500 0.5240 0.0232  0.0117  -0.0110 755  ARG   A CG   
1824 C  CD   . ARG   A 261 ? 0.4606 0.4982 0.4794 0.0201  0.0132  -0.0077 755  ARG   A CD   
1825 N  NE   . ARG   A 261 ? 0.5378 0.5875 0.5564 0.0169  0.0155  -0.0035 755  ARG   A NE   
1826 C  CZ   . ARG   A 261 ? 0.5071 0.5697 0.5249 0.0201  0.0172  -0.0041 755  ARG   A CZ   
1827 N  NH1  . ARG   A 261 ? 0.5067 0.5715 0.5229 0.0278  0.0167  -0.0091 755  ARG   A NH1  
1828 N  NH2  . ARG   A 261 ? 0.5494 0.6230 0.5679 0.0156  0.0190  0.0003  755  ARG   A NH2  
1829 N  N    . SER   A 262 ? 0.3760 0.3847 0.3894 0.0252  0.0008  -0.0213 756  SER   A N    
1830 C  CA   . SER   A 262 ? 0.4405 0.4373 0.4565 0.0247  -0.0028 -0.0241 756  SER   A CA   
1831 C  C    . SER   A 262 ? 0.3934 0.3868 0.4159 0.0188  -0.0028 -0.0202 756  SER   A C    
1832 O  O    . SER   A 262 ? 0.4162 0.4149 0.4397 0.0160  -0.0009 -0.0160 756  SER   A O    
1833 C  CB   . SER   A 262 ? 0.4118 0.4071 0.4225 0.0276  -0.0067 -0.0291 756  SER   A CB   
1834 O  OG   . SER   A 262 ? 0.4393 0.4405 0.4485 0.0251  -0.0072 -0.0269 756  SER   A OG   
1835 N  N    . GLY   A 263 ? 0.4241 0.4086 0.4510 0.0170  -0.0051 -0.0215 757  GLY   A N    
1836 C  CA   . GLY   A 263 ? 0.3479 0.3306 0.3819 0.0122  -0.0048 -0.0182 757  GLY   A CA   
1837 C  C    . GLY   A 263 ? 0.4152 0.3925 0.4527 0.0103  -0.0089 -0.0204 757  GLY   A C    
1838 O  O    . GLY   A 263 ? 0.3753 0.3467 0.4103 0.0118  -0.0120 -0.0244 757  GLY   A O    
1839 N  N    . PHE   A 264 ? 0.3687 0.3481 0.4121 0.0071  -0.0093 -0.0180 758  PHE   A N    
1840 C  CA   . PHE   A 264 ? 0.3483 0.3253 0.3968 0.0045  -0.0131 -0.0195 758  PHE   A CA   
1841 C  C    . PHE   A 264 ? 0.3757 0.3503 0.4320 0.0008  -0.0114 -0.0174 758  PHE   A C    
1842 O  O    . PHE   A 264 ? 0.3817 0.3589 0.4408 0.0001  -0.0074 -0.0141 758  PHE   A O    
1843 C  CB   . PHE   A 264 ? 0.3909 0.3737 0.4416 0.0039  -0.0149 -0.0181 758  PHE   A CB   
1844 C  CG   . PHE   A 264 ? 0.3811 0.3672 0.4235 0.0068  -0.0160 -0.0189 758  PHE   A CG   
1845 C  CD1  . PHE   A 264 ? 0.3741 0.3588 0.4087 0.0098  -0.0175 -0.0227 758  PHE   A CD1  
1846 C  CD2  . PHE   A 264 ? 0.3790 0.3698 0.4209 0.0067  -0.0159 -0.0156 758  PHE   A CD2  
1847 C  CE1  . PHE   A 264 ? 0.3504 0.3403 0.3771 0.0123  -0.0180 -0.0230 758  PHE   A CE1  
1848 C  CE2  . PHE   A 264 ? 0.3429 0.3373 0.3767 0.0086  -0.0169 -0.0154 758  PHE   A CE2  
1849 C  CZ   . PHE   A 264 ? 0.3410 0.3359 0.3673 0.0111  -0.0177 -0.0189 758  PHE   A CZ   
1850 N  N    . GLY   A 265 ? 0.3748 0.3442 0.4340 -0.0020 -0.0146 -0.0192 759  GLY   A N    
1851 C  CA   . GLY   A 265 ? 0.3676 0.3365 0.4348 -0.0066 -0.0133 -0.0167 759  GLY   A CA   
1852 C  C    . GLY   A 265 ? 0.3850 0.3555 0.4587 -0.0107 -0.0176 -0.0177 759  GLY   A C    
1853 O  O    . GLY   A 265 ? 0.3739 0.3422 0.4446 -0.0101 -0.0225 -0.0211 759  GLY   A O    
1854 N  N    . ILE   A 266 ? 0.3946 0.3701 0.4774 -0.0150 -0.0157 -0.0147 760  ILE   A N    
1855 C  CA   . ILE   A 266 ? 0.3418 0.3203 0.4326 -0.0203 -0.0194 -0.0148 760  ILE   A CA   
1856 C  C    . ILE   A 266 ? 0.4027 0.3699 0.4906 -0.0243 -0.0230 -0.0162 760  ILE   A C    
1857 O  O    . ILE   A 266 ? 0.4119 0.3719 0.4963 -0.0246 -0.0206 -0.0147 760  ILE   A O    
1858 C  CB   . ILE   A 266 ? 0.3825 0.3711 0.4837 -0.0234 -0.0154 -0.0110 760  ILE   A CB   
1859 C  CG1  . ILE   A 266 ? 0.3702 0.3676 0.4733 -0.0187 -0.0123 -0.0100 760  ILE   A CG1  
1860 C  CG2  . ILE   A 266 ? 0.3595 0.3542 0.4704 -0.0295 -0.0191 -0.0108 760  ILE   A CG2  
1861 C  CD1  . ILE   A 266 ? 0.3937 0.3980 0.5004 -0.0172 -0.0165 -0.0116 760  ILE   A CD1  
1862 N  N    . GLY   A 267 ? 0.3827 0.3476 0.4718 -0.0273 -0.0292 -0.0189 761  GLY   A N    
1863 C  CA   . GLY   A 267 ? 0.4032 0.3550 0.4886 -0.0313 -0.0340 -0.0207 761  GLY   A CA   
1864 C  C    . GLY   A 267 ? 0.4198 0.3747 0.5151 -0.0405 -0.0365 -0.0181 761  GLY   A C    
1865 O  O    . GLY   A 267 ? 0.3838 0.3500 0.4875 -0.0431 -0.0382 -0.0178 761  GLY   A O    
1866 N  N    . MET   A 268 ? 0.4221 0.3670 0.5161 -0.0455 -0.0368 -0.0159 762  MET   A N    
1867 C  CA   . MET   A 268 ? 0.4712 0.4177 0.5736 -0.0557 -0.0391 -0.0125 762  MET   A CA   
1868 C  C    . MET   A 268 ? 0.5112 0.4378 0.6059 -0.0596 -0.0442 -0.0131 762  MET   A C    
1869 O  O    . MET   A 268 ? 0.4968 0.4104 0.5809 -0.0538 -0.0441 -0.0151 762  MET   A O    
1870 C  CB   . MET   A 268 ? 0.4994 0.4584 0.6107 -0.0593 -0.0320 -0.0063 762  MET   A CB   
1871 C  CG   . MET   A 268 ? 0.5138 0.4907 0.6319 -0.0544 -0.0266 -0.0057 762  MET   A CG   
1872 S  SD   . MET   A 268 ? 0.6552 0.6368 0.7731 -0.0519 -0.0173 -0.0011 762  MET   A SD   
1873 C  CE   . MET   A 268 ? 0.4772 0.4450 0.5808 -0.0427 -0.0165 -0.0043 762  MET   A CE   
1874 N  N    . ARG   A 269 ? 0.4973 0.4217 0.5974 -0.0696 -0.0492 -0.0114 763  ARG   A N    
1875 C  CA   . ARG   A 269 ? 0.5588 0.4627 0.6517 -0.0747 -0.0545 -0.0110 763  ARG   A CA   
1876 C  C    . ARG   A 269 ? 0.5322 0.4318 0.6231 -0.0758 -0.0490 -0.0053 763  ARG   A C    
1877 O  O    . ARG   A 269 ? 0.5584 0.4732 0.6564 -0.0765 -0.0416 -0.0006 763  ARG   A O    
1878 C  CB   . ARG   A 269 ? 0.5436 0.4469 0.6434 -0.0868 -0.0612 -0.0095 763  ARG   A CB   
1879 C  CG   . ARG   A 269 ? 0.5103 0.4114 0.6085 -0.0858 -0.0691 -0.0162 763  ARG   A CG   
1880 C  CD   . ARG   A 269 ? 0.5631 0.4617 0.6673 -0.0985 -0.0769 -0.0150 763  ARG   A CD   
1881 N  NE   . ARG   A 269 ? 0.6069 0.5292 0.7274 -0.1063 -0.0733 -0.0094 763  ARG   A NE   
1882 C  CZ   . ARG   A 269 ? 0.5549 0.4965 0.6845 -0.1045 -0.0730 -0.0111 763  ARG   A CZ   
1883 N  NH1  . ARG   A 269 ? 0.5302 0.4702 0.6539 -0.0960 -0.0761 -0.0176 763  ARG   A NH1  
1884 N  NH2  . ARG   A 269 ? 0.5073 0.4709 0.6521 -0.1111 -0.0696 -0.0060 763  ARG   A NH2  
1885 N  N    . LYS   A 270 ? 0.6331 0.5111 0.7136 -0.0758 -0.0532 -0.0058 764  LYS   A N    
1886 C  CA   . LYS   A 270 ? 0.6774 0.5498 0.7541 -0.0756 -0.0486 -0.0006 764  LYS   A CA   
1887 C  C    . LYS   A 270 ? 0.6938 0.5754 0.7797 -0.0870 -0.0452 0.0077  764  LYS   A C    
1888 O  O    . LYS   A 270 ? 0.7087 0.5947 0.7944 -0.0862 -0.0388 0.0125  764  LYS   A O    
1889 C  CB   . LYS   A 270 ? 0.7077 0.5540 0.7712 -0.0730 -0.0549 -0.0029 764  LYS   A CB   
1890 C  CG   . LYS   A 270 ? 0.7013 0.5421 0.7549 -0.0593 -0.0541 -0.0091 764  LYS   A CG   
1891 C  CD   . LYS   A 270 ? 0.7893 0.6077 0.8314 -0.0555 -0.0631 -0.0156 764  LYS   A CD   
1892 C  CE   . LYS   A 270 ? 0.8667 0.6640 0.8990 -0.0540 -0.0659 -0.0137 764  LYS   A CE   
1893 N  NZ   . LYS   A 270 ? 0.8319 0.6093 0.8516 -0.0454 -0.0734 -0.0218 764  LYS   A NZ   
1894 N  N    . ASP   A 271 ? 0.6431 0.5295 0.7372 -0.0975 -0.0492 0.0095  765  ASP   A N    
1895 C  CA   . ASP   A 271 ? 0.7367 0.6340 0.8401 -0.1092 -0.0461 0.0176  765  ASP   A CA   
1896 C  C    . ASP   A 271 ? 0.7268 0.6531 0.8443 -0.1098 -0.0395 0.0191  765  ASP   A C    
1897 O  O    . ASP   A 271 ? 0.7000 0.6399 0.8275 -0.1198 -0.0373 0.0250  765  ASP   A O    
1898 C  CB   . ASP   A 271 ? 0.8158 0.7009 0.9198 -0.1221 -0.0548 0.0197  765  ASP   A CB   
1899 C  CG   . ASP   A 271 ? 0.8116 0.7069 0.9244 -0.1261 -0.0600 0.0159  765  ASP   A CG   
1900 O  OD1  . ASP   A 271 ? 0.7842 0.6937 0.9012 -0.1180 -0.0576 0.0110  765  ASP   A OD1  
1901 O  OD2  . ASP   A 271 ? 0.8417 0.7300 0.9569 -0.1379 -0.0671 0.0180  765  ASP   A OD2  
1902 N  N    . SER   A 272 ? 0.6932 0.6293 0.8116 -0.0993 -0.0366 0.0140  766  SER   A N    
1903 C  CA   . SER   A 272 ? 0.6441 0.6057 0.7749 -0.0983 -0.0311 0.0147  766  SER   A CA   
1904 C  C    . SER   A 272 ? 0.6132 0.5870 0.7479 -0.0997 -0.0223 0.0208  766  SER   A C    
1905 O  O    . SER   A 272 ? 0.5883 0.5536 0.7144 -0.0943 -0.0185 0.0217  766  SER   A O    
1906 C  CB   . SER   A 272 ? 0.6303 0.5962 0.7587 -0.0862 -0.0299 0.0086  766  SER   A CB   
1907 O  OG   . SER   A 272 ? 0.6347 0.6234 0.7740 -0.0841 -0.0247 0.0094  766  SER   A OG   
1908 N  N    . PRO   A 273 ? 0.6247 0.6193 0.7722 -0.1065 -0.0190 0.0250  767  PRO   A N    
1909 C  CA   . PRO   A 273 ? 0.6043 0.6128 0.7551 -0.1062 -0.0100 0.0298  767  PRO   A CA   
1910 C  C    . PRO   A 273 ? 0.5577 0.5772 0.7090 -0.0942 -0.0040 0.0261  767  PRO   A C    
1911 O  O    . PRO   A 273 ? 0.5395 0.5666 0.6903 -0.0918 0.0031  0.0289  767  PRO   A O    
1912 C  CB   . PRO   A 273 ? 0.6598 0.6890 0.8248 -0.1169 -0.0089 0.0345  767  PRO   A CB   
1913 C  CG   . PRO   A 273 ? 0.6907 0.7246 0.8627 -0.1173 -0.0155 0.0299  767  PRO   A CG   
1914 C  CD   . PRO   A 273 ? 0.6165 0.6244 0.7761 -0.1141 -0.0231 0.0250  767  PRO   A CD   
1915 N  N    . TRP   A 274 ? 0.5300 0.5500 0.6816 -0.0870 -0.0071 0.0202  768  TRP   A N    
1916 C  CA   . TRP   A 274 ? 0.5517 0.5810 0.7038 -0.0763 -0.0025 0.0171  768  TRP   A CA   
1917 C  C    . TRP   A 274 ? 0.5467 0.5606 0.6857 -0.0679 -0.0013 0.0146  768  TRP   A C    
1918 O  O    . TRP   A 274 ? 0.4932 0.5131 0.6313 -0.0598 0.0028  0.0127  768  TRP   A O    
1919 C  CB   . TRP   A 274 ? 0.6011 0.6386 0.7593 -0.0726 -0.0067 0.0126  768  TRP   A CB   
1920 C  CG   . TRP   A 274 ? 0.5812 0.6348 0.7528 -0.0803 -0.0089 0.0143  768  TRP   A CG   
1921 C  CD1  . TRP   A 274 ? 0.6025 0.6516 0.7768 -0.0884 -0.0163 0.0141  768  TRP   A CD1  
1922 C  CD2  . TRP   A 274 ? 0.6363 0.7141 0.8208 -0.0808 -0.0041 0.0164  768  TRP   A CD2  
1923 N  NE1  . TRP   A 274 ? 0.6410 0.7109 0.8297 -0.0946 -0.0164 0.0164  768  TRP   A NE1  
1924 C  CE2  . TRP   A 274 ? 0.6102 0.6988 0.8057 -0.0897 -0.0087 0.0178  768  TRP   A CE2  
1925 C  CE3  . TRP   A 274 ? 0.6265 0.7180 0.8140 -0.0742 0.0034  0.0169  768  TRP   A CE3  
1926 C  CZ2  . TRP   A 274 ? 0.6992 0.8139 0.9096 -0.0920 -0.0056 0.0198  768  TRP   A CZ2  
1927 C  CZ3  . TRP   A 274 ? 0.6451 0.7612 0.8465 -0.0757 0.0065  0.0185  768  TRP   A CZ3  
1928 C  CH2  . TRP   A 274 ? 0.6573 0.7857 0.8705 -0.0845 0.0021  0.0200  768  TRP   A CH2  
1929 N  N    . LYS   A 275 ? 0.5553 0.5499 0.6844 -0.0694 -0.0049 0.0146  769  LYS   A N    
1930 C  CA   . LYS   A 275 ? 0.5270 0.5091 0.6451 -0.0606 -0.0052 0.0109  769  LYS   A CA   
1931 C  C    . LYS   A 275 ? 0.5209 0.5064 0.6353 -0.0554 0.0018  0.0126  769  LYS   A C    
1932 O  O    . LYS   A 275 ? 0.4404 0.4260 0.5508 -0.0475 0.0032  0.0095  769  LYS   A O    
1933 C  CB   . LYS   A 275 ? 0.5549 0.5163 0.6632 -0.0620 -0.0107 0.0100  769  LYS   A CB   
1934 C  CG   . LYS   A 275 ? 0.6476 0.6004 0.7534 -0.0693 -0.0106 0.0153  769  LYS   A CG   
1935 C  CD   . LYS   A 275 ? 0.7015 0.6324 0.7983 -0.0707 -0.0182 0.0134  769  LYS   A CD   
1936 C  CE   . LYS   A 275 ? 0.7529 0.6705 0.8429 -0.0747 -0.0180 0.0184  769  LYS   A CE   
1937 N  NZ   . LYS   A 275 ? 0.7984 0.7293 0.8937 -0.0794 -0.0110 0.0249  769  LYS   A NZ   
1938 N  N    . GLN   A 276 ? 0.4792 0.4672 0.5943 -0.0600 0.0059  0.0176  770  GLN   A N    
1939 C  CA   . GLN   A 276 ? 0.5373 0.5266 0.6472 -0.0549 0.0118  0.0187  770  GLN   A CA   
1940 C  C    . GLN   A 276 ? 0.4921 0.4973 0.6078 -0.0499 0.0165  0.0171  770  GLN   A C    
1941 O  O    . GLN   A 276 ? 0.4499 0.4537 0.5603 -0.0429 0.0189  0.0152  770  GLN   A O    
1942 C  CB   . GLN   A 276 ? 0.6081 0.5955 0.7158 -0.0610 0.0148  0.0246  770  GLN   A CB   
1943 C  CG   . GLN   A 276 ? 0.6486 0.6383 0.7507 -0.0565 0.0209  0.0261  770  GLN   A CG   
1944 C  CD   . GLN   A 276 ? 0.7615 0.7395 0.8534 -0.0485 0.0200  0.0231  770  GLN   A CD   
1945 O  OE1  . GLN   A 276 ? 0.7127 0.6870 0.8032 -0.0433 0.0170  0.0186  770  GLN   A OE1  
1946 N  NE2  . GLN   A 276 ? 0.6247 0.5984 0.7096 -0.0479 0.0229  0.0260  770  GLN   A NE2  
1947 N  N    . ASN   A 277 ? 0.4286 0.4491 0.5551 -0.0532 0.0175  0.0179  771  ASN   A N    
1948 C  CA   . ASN   A 277 ? 0.4771 0.5116 0.6088 -0.0471 0.0213  0.0157  771  ASN   A CA   
1949 C  C    . ASN   A 277 ? 0.4543 0.4855 0.5844 -0.0402 0.0176  0.0109  771  ASN   A C    
1950 O  O    . ASN   A 277 ? 0.4221 0.4568 0.5508 -0.0334 0.0201  0.0089  771  ASN   A O    
1951 C  CB   . ASN   A 277 ? 0.4350 0.4886 0.5793 -0.0515 0.0233  0.0176  771  ASN   A CB   
1952 C  CG   . ASN   A 277 ? 0.5319 0.5933 0.6770 -0.0560 0.0293  0.0223  771  ASN   A CG   
1953 O  OD1  . ASN   A 277 ? 0.5285 0.5827 0.6648 -0.0537 0.0326  0.0234  771  ASN   A OD1  
1954 N  ND2  . ASN   A 277 ? 0.4676 0.5448 0.6233 -0.0626 0.0307  0.0253  771  ASN   A ND2  
1955 N  N    . VAL   A 278 ? 0.4489 0.4728 0.5785 -0.0421 0.0115  0.0091  772  VAL   A N    
1956 C  CA   . VAL   A 278 ? 0.4637 0.4836 0.5898 -0.0358 0.0081  0.0050  772  VAL   A CA   
1957 C  C    . VAL   A 278 ? 0.4156 0.4256 0.5311 -0.0301 0.0101  0.0041  772  VAL   A C    
1958 O  O    . VAL   A 278 ? 0.4376 0.4497 0.5511 -0.0241 0.0111  0.0023  772  VAL   A O    
1959 C  CB   . VAL   A 278 ? 0.4926 0.5051 0.6180 -0.0387 0.0012  0.0029  772  VAL   A CB   
1960 C  CG1  . VAL   A 278 ? 0.4525 0.4584 0.5707 -0.0321 -0.0017 -0.0009 772  VAL   A CG1  
1961 C  CG2  . VAL   A 278 ? 0.4923 0.5170 0.6292 -0.0434 -0.0016 0.0032  772  VAL   A CG2  
1962 N  N    . SER   A 279 ? 0.4285 0.4275 0.5369 -0.0320 0.0102  0.0054  773  SER   A N    
1963 C  CA   . SER   A 279 ? 0.4293 0.4202 0.5282 -0.0269 0.0116  0.0046  773  SER   A CA   
1964 C  C    . SER   A 279 ? 0.4327 0.4295 0.5310 -0.0239 0.0171  0.0059  773  SER   A C    
1965 O  O    . SER   A 279 ? 0.3928 0.3880 0.4863 -0.0189 0.0178  0.0043  773  SER   A O    
1966 C  CB   . SER   A 279 ? 0.4550 0.4335 0.5471 -0.0291 0.0102  0.0059  773  SER   A CB   
1967 O  OG   . SER   A 279 ? 0.4983 0.4693 0.5822 -0.0238 0.0089  0.0036  773  SER   A OG   
1968 N  N    . LEU   A 280 ? 0.4238 0.4274 0.5262 -0.0273 0.0210  0.0087  774  LEU   A N    
1969 C  CA   . LEU   A 280 ? 0.4323 0.4424 0.5341 -0.0242 0.0261  0.0092  774  LEU   A CA   
1970 C  C    . LEU   A 280 ? 0.4400 0.4568 0.5453 -0.0189 0.0259  0.0062  774  LEU   A C    
1971 O  O    . LEU   A 280 ? 0.3952 0.4103 0.4957 -0.0142 0.0275  0.0050  774  LEU   A O    
1972 C  CB   . LEU   A 280 ? 0.4293 0.4485 0.5362 -0.0289 0.0301  0.0125  774  LEU   A CB   
1973 C  CG   . LEU   A 280 ? 0.4434 0.4551 0.5451 -0.0339 0.0309  0.0164  774  LEU   A CG   
1974 C  CD1  . LEU   A 280 ? 0.5188 0.5416 0.6239 -0.0375 0.0363  0.0198  774  LEU   A CD1  
1975 C  CD2  . LEU   A 280 ? 0.4500 0.4516 0.5413 -0.0296 0.0314  0.0157  774  LEU   A CD2  
1976 N  N    . SER   A 281 ? 0.4073 0.4314 0.5207 -0.0197 0.0233  0.0052  775  SER   A N    
1977 C  CA   . SER   A 281 ? 0.4064 0.4361 0.5229 -0.0143 0.0224  0.0027  775  SER   A CA   
1978 C  C    . SER   A 281 ? 0.3803 0.4003 0.4891 -0.0102 0.0193  0.0008  775  SER   A C    
1979 O  O    . SER   A 281 ? 0.3699 0.3897 0.4764 -0.0053 0.0196  -0.0005 775  SER   A O    
1980 C  CB   . SER   A 281 ? 0.4633 0.5033 0.5903 -0.0161 0.0197  0.0021  775  SER   A CB   
1981 O  OG   . SER   A 281 ? 0.5288 0.5731 0.6580 -0.0101 0.0180  -0.0002 775  SER   A OG   
1982 N  N    . ILE   A 282 ? 0.4190 0.4307 0.5234 -0.0123 0.0160  0.0006  776  ILE   A N    
1983 C  CA   . ILE   A 282 ? 0.3717 0.3760 0.4684 -0.0088 0.0137  -0.0008 776  ILE   A CA   
1984 C  C    . ILE   A 282 ? 0.3869 0.3870 0.4767 -0.0065 0.0169  -0.0001 776  ILE   A C    
1985 O  O    . ILE   A 282 ? 0.3770 0.3753 0.4629 -0.0032 0.0164  -0.0007 776  ILE   A O    
1986 C  CB   . ILE   A 282 ? 0.3564 0.3535 0.4491 -0.0107 0.0102  -0.0016 776  ILE   A CB   
1987 C  CG1  . ILE   A 282 ? 0.3911 0.3914 0.4898 -0.0132 0.0060  -0.0029 776  ILE   A CG1  
1988 C  CG2  . ILE   A 282 ? 0.3175 0.3092 0.4017 -0.0071 0.0089  -0.0027 776  ILE   A CG2  
1989 C  CD1  . ILE   A 282 ? 0.4290 0.4346 0.5306 -0.0102 0.0033  -0.0042 776  ILE   A CD1  
1990 N  N    . LEU   A 283 ? 0.3735 0.3715 0.4611 -0.0087 0.0199  0.0015  777  LEU   A N    
1991 C  CA   . LEU   A 283 ? 0.3909 0.3853 0.4718 -0.0069 0.0225  0.0022  777  LEU   A CA   
1992 C  C    . LEU   A 283 ? 0.3524 0.3511 0.4345 -0.0040 0.0248  0.0015  777  LEU   A C    
1993 O  O    . LEU   A 283 ? 0.3592 0.3540 0.4358 -0.0015 0.0246  0.0009  777  LEU   A O    
1994 C  CB   . LEU   A 283 ? 0.3752 0.3671 0.4537 -0.0098 0.0250  0.0043  777  LEU   A CB   
1995 C  CG   . LEU   A 283 ? 0.3637 0.3491 0.4397 -0.0118 0.0224  0.0047  777  LEU   A CG   
1996 C  CD1  . LEU   A 283 ? 0.4451 0.4273 0.5185 -0.0145 0.0245  0.0074  777  LEU   A CD1  
1997 C  CD2  . LEU   A 283 ? 0.3982 0.3790 0.4680 -0.0086 0.0201  0.0032  777  LEU   A CD2  
1998 N  N    . LYS   A 284 ? 0.4060 0.4128 0.4951 -0.0043 0.0268  0.0015  778  LYS   A N    
1999 C  CA   . LYS   A 284 ? 0.3935 0.4046 0.4836 -0.0002 0.0287  0.0000  778  LYS   A CA   
2000 C  C    . LYS   A 284 ? 0.3644 0.3723 0.4533 0.0038  0.0250  -0.0017 778  LYS   A C    
2001 O  O    . LYS   A 284 ? 0.3838 0.3880 0.4682 0.0074  0.0252  -0.0029 778  LYS   A O    
2002 C  CB   . LYS   A 284 ? 0.3617 0.3850 0.4611 -0.0007 0.0312  0.0001  778  LYS   A CB   
2003 C  CG   . LYS   A 284 ? 0.4048 0.4341 0.5059 0.0049  0.0334  -0.0022 778  LYS   A CG   
2004 C  CD   . LYS   A 284 ? 0.4910 0.5358 0.6029 0.0045  0.0358  -0.0022 778  LYS   A CD   
2005 C  CE   . LYS   A 284 ? 0.5143 0.5656 0.6275 0.0115  0.0381  -0.0052 778  LYS   A CE   
2006 N  NZ   . LYS   A 284 ? 0.6053 0.6520 0.7098 0.0126  0.0419  -0.0055 778  LYS   A NZ   
2007 N  N    . SER   A 285 ? 0.3682 0.3765 0.4602 0.0029  0.0212  -0.0018 779  SER   A N    
2008 C  CA   . SER   A 285 ? 0.4014 0.4072 0.4922 0.0064  0.0173  -0.0029 779  SER   A CA   
2009 C  C    . SER   A 285 ? 0.3818 0.3780 0.4629 0.0065  0.0158  -0.0022 779  SER   A C    
2010 O  O    . SER   A 285 ? 0.4006 0.3925 0.4781 0.0094  0.0138  -0.0024 779  SER   A O    
2011 C  CB   . SER   A 285 ? 0.4045 0.4143 0.5008 0.0052  0.0136  -0.0031 779  SER   A CB   
2012 O  OG   . SER   A 285 ? 0.3802 0.4006 0.4864 0.0053  0.0144  -0.0037 779  SER   A OG   
2013 N  N    . HIS   A 286 ? 0.3922 0.3851 0.4692 0.0034  0.0164  -0.0011 780  HIS   A N    
2014 C  CA   . HIS   A 286 ? 0.3632 0.3497 0.4318 0.0032  0.0158  -0.0002 780  HIS   A CA   
2015 C  C    . HIS   A 286 ? 0.3830 0.3664 0.4478 0.0044  0.0180  -0.0002 780  HIS   A C    
2016 O  O    . HIS   A 286 ? 0.3619 0.3399 0.4214 0.0054  0.0162  0.0001  780  HIS   A O    
2017 C  CB   . HIS   A 286 ? 0.3490 0.3342 0.4146 0.0006  0.0165  0.0005  780  HIS   A CB   
2018 C  CG   . HIS   A 286 ? 0.3885 0.3741 0.4541 0.0001  0.0135  0.0000  780  HIS   A CG   
2019 N  ND1  . HIS   A 286 ? 0.3707 0.3554 0.4327 0.0010  0.0107  0.0002  780  HIS   A ND1  
2020 C  CD2  . HIS   A 286 ? 0.3561 0.3424 0.4241 -0.0012 0.0126  -0.0008 780  HIS   A CD2  
2021 C  CE1  . HIS   A 286 ? 0.3667 0.3524 0.4286 0.0008  0.0085  -0.0008 780  HIS   A CE1  
2022 N  NE2  . HIS   A 286 ? 0.3820 0.3680 0.4475 -0.0005 0.0094  -0.0018 780  HIS   A NE2  
2023 N  N    . GLU   A 287 ? 0.3455 0.3318 0.4124 0.0041  0.0216  -0.0006 781  GLU   A N    
2024 C  CA   . GLU   A 287 ? 0.4235 0.4066 0.4853 0.0049  0.0237  -0.0009 781  GLU   A CA   
2025 C  C    . GLU   A 287 ? 0.3633 0.3446 0.4248 0.0091  0.0230  -0.0028 781  GLU   A C    
2026 O  O    . GLU   A 287 ? 0.3857 0.3604 0.4405 0.0099  0.0225  -0.0034 781  GLU   A O    
2027 C  CB   . GLU   A 287 ? 0.3538 0.3409 0.4170 0.0034  0.0278  -0.0004 781  GLU   A CB   
2028 C  CG   . GLU   A 287 ? 0.3748 0.3602 0.4358 0.0000  0.0278  0.0016  781  GLU   A CG   
2029 C  CD   . GLU   A 287 ? 0.4227 0.4115 0.4858 -0.0021 0.0310  0.0028  781  GLU   A CD   
2030 O  OE1  . GLU   A 287 ? 0.4046 0.3962 0.4673 -0.0014 0.0341  0.0026  781  GLU   A OE1  
2031 O  OE2  . GLU   A 287 ? 0.4250 0.4129 0.4891 -0.0045 0.0301  0.0042  781  GLU   A OE2  
2032 N  N    . ASN   A 288 ? 0.3956 0.3824 0.4640 0.0120  0.0224  -0.0041 782  ASN   A N    
2033 C  CA   . ASN   A 288 ? 0.4201 0.4053 0.4882 0.0174  0.0215  -0.0065 782  ASN   A CA   
2034 C  C    . ASN   A 288 ? 0.4340 0.4127 0.5000 0.0195  0.0163  -0.0063 782  ASN   A C    
2035 O  O    . ASN   A 288 ? 0.4488 0.4254 0.5150 0.0248  0.0144  -0.0083 782  ASN   A O    
2036 C  CB   . ASN   A 288 ? 0.4321 0.4289 0.5092 0.0205  0.0242  -0.0083 782  ASN   A CB   
2037 C  CG   . ASN   A 288 ? 0.4510 0.4556 0.5370 0.0197  0.0223  -0.0076 782  ASN   A CG   
2038 O  OD1  . ASN   A 288 ? 0.3799 0.3801 0.4647 0.0185  0.0183  -0.0064 782  ASN   A OD1  
2039 N  ND2  . ASN   A 288 ? 0.4474 0.4646 0.5425 0.0201  0.0251  -0.0082 782  ASN   A ND2  
2040 N  N    . GLY   A 289 ? 0.3895 0.3653 0.4531 0.0159  0.0137  -0.0039 783  GLY   A N    
2041 C  CA   . GLY   A 289 ? 0.4455 0.4149 0.5056 0.0169  0.0087  -0.0028 783  GLY   A CA   
2042 C  C    . GLY   A 289 ? 0.4729 0.4480 0.5396 0.0189  0.0060  -0.0029 783  GLY   A C    
2043 O  O    . GLY   A 289 ? 0.4444 0.4142 0.5076 0.0198  0.0016  -0.0016 783  GLY   A O    
2044 N  N    . PHE   A 290 ? 0.4287 0.4142 0.5043 0.0190  0.0082  -0.0041 784  PHE   A N    
2045 C  CA   . PHE   A 290 ? 0.4364 0.4282 0.5188 0.0205  0.0051  -0.0044 784  PHE   A CA   
2046 C  C    . PHE   A 290 ? 0.4356 0.4248 0.5144 0.0172  0.0019  -0.0025 784  PHE   A C    
2047 O  O    . PHE   A 290 ? 0.3970 0.3848 0.4751 0.0191  -0.0026 -0.0019 784  PHE   A O    
2048 C  CB   . PHE   A 290 ? 0.4254 0.4297 0.5183 0.0198  0.0080  -0.0056 784  PHE   A CB   
2049 C  CG   . PHE   A 290 ? 0.4494 0.4615 0.5502 0.0209  0.0044  -0.0061 784  PHE   A CG   
2050 C  CD1  . PHE   A 290 ? 0.5028 0.5192 0.6083 0.0269  0.0021  -0.0075 784  PHE   A CD1  
2051 C  CD2  . PHE   A 290 ? 0.4510 0.4659 0.5540 0.0163  0.0028  -0.0053 784  PHE   A CD2  
2052 C  CE1  . PHE   A 290 ? 0.4570 0.4815 0.5700 0.0279  -0.0017 -0.0078 784  PHE   A CE1  
2053 C  CE2  . PHE   A 290 ? 0.4366 0.4586 0.5464 0.0169  -0.0011 -0.0059 784  PHE   A CE2  
2054 C  CZ   . PHE   A 290 ? 0.4111 0.4384 0.5262 0.0226  -0.0033 -0.0069 784  PHE   A CZ   
2055 N  N    . MET   A 291 ? 0.3703 0.3591 0.4464 0.0126  0.0039  -0.0017 785  MET   A N    
2056 C  CA   . MET   A 291 ? 0.4070 0.3941 0.4787 0.0102  0.0012  -0.0005 785  MET   A CA   
2057 C  C    . MET   A 291 ? 0.4310 0.4106 0.4941 0.0105  -0.0015 0.0017  785  MET   A C    
2058 O  O    . MET   A 291 ? 0.4635 0.4428 0.5238 0.0103  -0.0050 0.0028  785  MET   A O    
2059 C  CB   . MET   A 291 ? 0.4206 0.4081 0.4903 0.0065  0.0039  -0.0004 785  MET   A CB   
2060 C  CG   . MET   A 291 ? 0.4531 0.4461 0.5303 0.0052  0.0059  -0.0018 785  MET   A CG   
2061 S  SD   . MET   A 291 ? 0.4448 0.4435 0.5288 0.0045  0.0021  -0.0032 785  MET   A SD   
2062 C  CE   . MET   A 291 ? 0.4840 0.4793 0.5608 0.0056  -0.0025 -0.0028 785  MET   A CE   
2063 N  N    . GLU   A 292 ? 0.3928 0.3664 0.4511 0.0105  -0.0002 0.0025  786  GLU   A N    
2064 C  CA   . GLU   A 292 ? 0.4496 0.4152 0.4995 0.0098  -0.0034 0.0052  786  GLU   A CA   
2065 C  C    . GLU   A 292 ? 0.4645 0.4270 0.5150 0.0137  -0.0081 0.0055  786  GLU   A C    
2066 O  O    . GLU   A 292 ? 0.5036 0.4627 0.5487 0.0127  -0.0119 0.0082  786  GLU   A O    
2067 C  CB   . GLU   A 292 ? 0.5751 0.5337 0.6196 0.0087  -0.0019 0.0058  786  GLU   A CB   
2068 C  CG   . GLU   A 292 ? 0.6233 0.5738 0.6587 0.0057  -0.0051 0.0094  786  GLU   A CG   
2069 C  CD   . GLU   A 292 ? 0.7375 0.6807 0.7674 0.0036  -0.0043 0.0099  786  GLU   A CD   
2070 O  OE1  . GLU   A 292 ? 0.8223 0.7568 0.8501 0.0065  -0.0063 0.0088  786  GLU   A OE1  
2071 O  OE2  . GLU   A 292 ? 0.7621 0.7083 0.7898 -0.0005 -0.0019 0.0109  786  GLU   A OE2  
2072 N  N    . ASP   A 293 ? 0.4731 0.4377 0.5301 0.0185  -0.0079 0.0029  787  ASP   A N    
2073 C  CA   . ASP   A 293 ? 0.4345 0.3976 0.4932 0.0234  -0.0127 0.0028  787  ASP   A CA   
2074 C  C    . ASP   A 293 ? 0.4922 0.4613 0.5532 0.0224  -0.0157 0.0037  787  ASP   A C    
2075 O  O    . ASP   A 293 ? 0.4501 0.4144 0.5065 0.0235  -0.0206 0.0060  787  ASP   A O    
2076 C  CB   . ASP   A 293 ? 0.5109 0.4796 0.5782 0.0290  -0.0111 -0.0007 787  ASP   A CB   
2077 C  CG   . ASP   A 293 ? 0.6364 0.5975 0.6997 0.0316  -0.0094 -0.0021 787  ASP   A CG   
2078 O  OD1  . ASP   A 293 ? 0.6939 0.6424 0.7474 0.0301  -0.0117 -0.0001 787  ASP   A OD1  
2079 O  OD2  . ASP   A 293 ? 0.6542 0.6221 0.7237 0.0347  -0.0058 -0.0052 787  ASP   A OD2  
2080 N  N    . LEU   A 294 ? 0.4446 0.4234 0.5122 0.0203  -0.0132 0.0020  788  LEU   A N    
2081 C  CA   . LEU   A 294 ? 0.4472 0.4308 0.5159 0.0191  -0.0164 0.0023  788  LEU   A CA   
2082 C  C    . LEU   A 294 ? 0.4795 0.4575 0.5376 0.0160  -0.0183 0.0053  788  LEU   A C    
2083 O  O    . LEU   A 294 ? 0.4681 0.4459 0.5230 0.0166  -0.0227 0.0067  788  LEU   A O    
2084 C  CB   . LEU   A 294 ? 0.3852 0.3773 0.4607 0.0163  -0.0138 0.0000  788  LEU   A CB   
2085 C  CG   . LEU   A 294 ? 0.4086 0.4093 0.4957 0.0181  -0.0122 -0.0023 788  LEU   A CG   
2086 C  CD1  . LEU   A 294 ? 0.4387 0.4457 0.5310 0.0140  -0.0109 -0.0037 788  LEU   A CD1  
2087 C  CD2  . LEU   A 294 ? 0.4191 0.4238 0.5112 0.0229  -0.0168 -0.0027 788  LEU   A CD2  
2088 N  N    . ASP   A 295 ? 0.4529 0.4274 0.5054 0.0126  -0.0149 0.0064  789  ASP   A N    
2089 C  CA   . ASP   A 295 ? 0.5350 0.5072 0.5782 0.0092  -0.0158 0.0094  789  ASP   A CA   
2090 C  C    . ASP   A 295 ? 0.5550 0.5193 0.5911 0.0098  -0.0203 0.0131  789  ASP   A C    
2091 O  O    . ASP   A 295 ? 0.6408 0.6054 0.6710 0.0085  -0.0233 0.0157  789  ASP   A O    
2092 C  CB   . ASP   A 295 ? 0.5681 0.5396 0.6079 0.0058  -0.0115 0.0100  789  ASP   A CB   
2093 C  CG   . ASP   A 295 ? 0.6791 0.6542 0.7125 0.0027  -0.0111 0.0115  789  ASP   A CG   
2094 O  OD1  . ASP   A 295 ? 0.6747 0.6558 0.7106 0.0031  -0.0102 0.0089  789  ASP   A OD1  
2095 O  OD2  . ASP   A 295 ? 0.7052 0.6774 0.7311 -0.0001 -0.0119 0.0152  789  ASP   A OD2  
2096 N  N    . LYS   A 296 ? 0.5357 0.4924 0.5717 0.0120  -0.0210 0.0135  790  LYS   A N    
2097 C  CA   . LYS   A 296 ? 0.6244 0.5710 0.6533 0.0129  -0.0262 0.0171  790  LYS   A CA   
2098 C  C    . LYS   A 296 ? 0.6135 0.5616 0.6451 0.0174  -0.0312 0.0170  790  LYS   A C    
2099 O  O    . LYS   A 296 ? 0.6344 0.5769 0.6584 0.0167  -0.0359 0.0209  790  LYS   A O    
2100 C  CB   . LYS   A 296 ? 0.6647 0.6013 0.6925 0.0150  -0.0262 0.0165  790  LYS   A CB   
2101 C  CG   . LYS   A 296 ? 0.7563 0.6908 0.7805 0.0101  -0.0221 0.0171  790  LYS   A CG   
2102 C  CD   . LYS   A 296 ? 0.8182 0.7419 0.8401 0.0122  -0.0226 0.0159  790  LYS   A CD   
2103 C  CE   . LYS   A 296 ? 0.8252 0.7471 0.8431 0.0068  -0.0192 0.0166  790  LYS   A CE   
2104 N  NZ   . LYS   A 296 ? 0.8602 0.7711 0.8753 0.0092  -0.0201 0.0147  790  LYS   A NZ   
2105 N  N    . THR   A 297 ? 0.4991 0.4555 0.5412 0.0214  -0.0304 0.0129  791  THR   A N    
2106 C  CA   . THR   A 297 ? 0.5270 0.4862 0.5728 0.0261  -0.0356 0.0125  791  THR   A CA   
2107 C  C    . THR   A 297 ? 0.5036 0.4680 0.5462 0.0233  -0.0380 0.0139  791  THR   A C    
2108 O  O    . THR   A 297 ? 0.5620 0.5232 0.5997 0.0250  -0.0436 0.0165  791  THR   A O    
2109 C  CB   . THR   A 297 ? 0.4505 0.4197 0.5095 0.0303  -0.0338 0.0079  791  THR   A CB   
2110 O  OG1  . THR   A 297 ? 0.4985 0.4634 0.5596 0.0338  -0.0316 0.0063  791  THR   A OG1  
2111 C  CG2  . THR   A 297 ? 0.4751 0.4496 0.5394 0.0352  -0.0395 0.0074  791  THR   A CG2  
2112 N  N    . TRP   A 298 ? 0.4645 0.4361 0.5085 0.0194  -0.0342 0.0121  792  TRP   A N    
2113 C  CA   . TRP   A 298 ? 0.5187 0.4965 0.5606 0.0177  -0.0362 0.0116  792  TRP   A CA   
2114 C  C    . TRP   A 298 ? 0.5621 0.5387 0.5933 0.0133  -0.0348 0.0142  792  TRP   A C    
2115 O  O    . TRP   A 298 ? 0.5345 0.5139 0.5603 0.0127  -0.0379 0.0151  792  TRP   A O    
2116 C  CB   . TRP   A 298 ? 0.4752 0.4622 0.5268 0.0173  -0.0338 0.0069  792  TRP   A CB   
2117 C  CG   . TRP   A 298 ? 0.4230 0.4149 0.4858 0.0211  -0.0355 0.0046  792  TRP   A CG   
2118 C  CD1  . TRP   A 298 ? 0.4327 0.4276 0.5044 0.0223  -0.0318 0.0025  792  TRP   A CD1  
2119 C  CD2  . TRP   A 298 ? 0.4461 0.4419 0.5124 0.0245  -0.0414 0.0045  792  TRP   A CD2  
2120 N  NE1  . TRP   A 298 ? 0.4083 0.4101 0.4896 0.0262  -0.0346 0.0009  792  TRP   A NE1  
2121 C  CE2  . TRP   A 298 ? 0.4434 0.4459 0.5221 0.0277  -0.0408 0.0020  792  TRP   A CE2  
2122 C  CE3  . TRP   A 298 ? 0.4250 0.4203 0.4853 0.0252  -0.0473 0.0062  792  TRP   A CE3  
2123 C  CZ2  . TRP   A 298 ? 0.4036 0.4130 0.4895 0.0318  -0.0459 0.0012  792  TRP   A CZ2  
2124 C  CZ3  . TRP   A 298 ? 0.4160 0.4168 0.4828 0.0292  -0.0527 0.0054  792  TRP   A CZ3  
2125 C  CH2  . TRP   A 298 ? 0.3968 0.4050 0.4768 0.0325  -0.0520 0.0029  792  TRP   A CH2  
2126 N  N    . VAL   A 299 ? 0.6005 0.5746 0.6288 0.0102  -0.0303 0.0152  793  VAL   A N    
2127 C  CA   . VAL   A 299 ? 0.6783 0.6556 0.6990 0.0063  -0.0278 0.0165  793  VAL   A CA   
2128 C  C    . VAL   A 299 ? 0.7892 0.7608 0.7997 0.0029  -0.0287 0.0224  793  VAL   A C    
2129 O  O    . VAL   A 299 ? 0.8383 0.8131 0.8407 0.0006  -0.0299 0.0251  793  VAL   A O    
2130 C  CB   . VAL   A 299 ? 0.7140 0.6950 0.7389 0.0049  -0.0221 0.0134  793  VAL   A CB   
2131 C  CG1  . VAL   A 299 ? 0.6928 0.6793 0.7109 0.0023  -0.0198 0.0138  793  VAL   A CG1  
2132 C  CG2  . VAL   A 299 ? 0.6260 0.6112 0.6606 0.0072  -0.0216 0.0084  793  VAL   A CG2  
2133 N  N    . ARG   A 300 ? 0.8874 0.8507 0.8975 0.0022  -0.0284 0.0245  794  ARG   A N    
2134 C  CA   . ARG   A 300 ? 0.9744 0.9314 0.9750 -0.0025 -0.0293 0.0303  794  ARG   A CA   
2135 C  C    . ARG   A 300 ? 0.9855 0.9301 0.9824 -0.0008 -0.0351 0.0337  794  ARG   A C    
2136 O  O    . ARG   A 300 ? 1.0217 0.9584 1.0224 0.0021  -0.0357 0.0322  794  ARG   A O    
2137 C  CB   . ARG   A 300 ? 1.0222 0.9783 1.0237 -0.0057 -0.0248 0.0301  794  ARG   A CB   
2138 C  CG   . ARG   A 300 ? 1.0215 0.9746 1.0315 -0.0021 -0.0226 0.0256  794  ARG   A CG   
2139 C  CD   . ARG   A 300 ? 1.0573 0.9997 1.0641 -0.0040 -0.0230 0.0276  794  ARG   A CD   
2140 N  NE   . ARG   A 300 ? 1.1843 1.1145 1.1858 -0.0027 -0.0289 0.0308  794  ARG   A NE   
2141 C  CZ   . ARG   A 300 ? 1.2223 1.1397 1.2198 -0.0033 -0.0312 0.0323  794  ARG   A CZ   
2142 N  NH1  . ARG   A 300 ? 1.1666 1.0822 1.1647 -0.0055 -0.0279 0.0308  794  ARG   A NH1  
2143 N  NH2  . ARG   A 300 ? 1.1573 1.0625 1.1493 -0.0015 -0.0373 0.0351  794  ARG   A NH2  
2144 N  N    . TYR   A 301 ? 1.1012 1.0438 1.0900 -0.0022 -0.0395 0.0383  795  TYR   A N    
2145 C  CA   . TYR   A 301 ? 1.0827 1.0117 1.0654 -0.0011 -0.0460 0.0429  795  TYR   A CA   
2146 C  C    . TYR   A 301 ? 1.0561 0.9854 1.0281 -0.0045 -0.0498 0.0490  795  TYR   A C    
2147 O  O    . TYR   A 301 ? 1.0860 1.0159 1.0495 -0.0114 -0.0486 0.0542  795  TYR   A O    
2148 C  CB   . TYR   A 301 ? 1.0982 1.0238 1.0887 0.0071  -0.0495 0.0389  795  TYR   A CB   
2149 C  CG   . TYR   A 301 ? 1.0940 1.0306 1.0899 0.0108  -0.0507 0.0358  795  TYR   A CG   
2150 C  CD1  . TYR   A 301 ? 0.9134 0.8615 0.9195 0.0124  -0.0463 0.0297  795  TYR   A CD1  
2151 C  CD2  . TYR   A 301 ? 1.0963 1.0311 1.0866 0.0123  -0.0569 0.0391  795  TYR   A CD2  
2152 C  CE1  . TYR   A 301 ? 0.9114 0.8686 0.9221 0.0150  -0.0481 0.0267  795  TYR   A CE1  
2153 C  CE2  . TYR   A 301 ? 1.0723 1.0171 1.0671 0.0154  -0.0586 0.0359  795  TYR   A CE2  
2154 C  CZ   . TYR   A 301 ? 0.9516 0.9074 0.9568 0.0165  -0.0543 0.0296  795  TYR   A CZ   
2155 O  OH   . TYR   A 301 ? 0.9235 0.8884 0.9329 0.0188  -0.0567 0.0265  795  TYR   A OH   
2156 N  N    . ASP   B 17  ? 1.3525 1.0045 1.2591 0.0084  -0.0737 0.0712  403  ASP   B N    
2157 C  CA   . ASP   B 17  ? 1.3912 1.0264 1.2975 0.0083  -0.0797 0.0655  403  ASP   B CA   
2158 C  C    . ASP   B 17  ? 1.2984 0.9514 1.2139 0.0174  -0.0761 0.0538  403  ASP   B C    
2159 O  O    . ASP   B 17  ? 1.2067 0.8783 1.1323 0.0106  -0.0691 0.0517  403  ASP   B O    
2160 C  CB   . ASP   B 17  ? 1.4255 1.0282 1.3186 0.0162  -0.0918 0.0657  403  ASP   B CB   
2161 C  CG   . ASP   B 17  ? 1.4964 1.0766 1.3867 0.0133  -0.0992 0.0615  403  ASP   B CG   
2162 O  OD1  . ASP   B 17  ? 1.4836 1.0729 1.3822 0.0030  -0.0952 0.0601  403  ASP   B OD1  
2163 O  OD2  . ASP   B 17  ? 1.5059 1.0588 1.3855 0.0217  -0.1097 0.0593  403  ASP   B OD2  
2164 N  N    . ASN   B 18  ? 1.2276 0.8751 1.1392 0.0330  -0.0811 0.0464  404  ASN   B N    
2165 C  CA   . ASN   B 18  ? 1.0584 0.7231 0.9772 0.0432  -0.0782 0.0356  404  ASN   B CA   
2166 C  C    . ASN   B 18  ? 0.9393 0.6287 0.8626 0.0520  -0.0723 0.0339  404  ASN   B C    
2167 O  O    . ASN   B 18  ? 0.7752 0.4800 0.7037 0.0616  -0.0701 0.0255  404  ASN   B O    
2168 C  CB   . ASN   B 18  ? 1.1107 0.7544 1.0222 0.0549  -0.0875 0.0276  404  ASN   B CB   
2169 C  CG   . ASN   B 18  ? 1.0799 0.7320 0.9975 0.0567  -0.0858 0.0182  404  ASN   B CG   
2170 O  OD1  . ASN   B 18  ? 1.0653 0.7276 0.9904 0.0451  -0.0807 0.0194  404  ASN   B OD1  
2171 N  ND2  . ASN   B 18  ? 1.1258 0.7743 1.0400 0.0716  -0.0902 0.0087  404  ASN   B ND2  
2172 N  N    . HIS   B 19  ? 0.9240 0.6177 0.8452 0.0486  -0.0701 0.0420  405  HIS   B N    
2173 C  CA   . HIS   B 19  ? 0.8671 0.5826 0.7916 0.0557  -0.0655 0.0415  405  HIS   B CA   
2174 C  C    . HIS   B 19  ? 0.8674 0.6036 0.7990 0.0441  -0.0561 0.0463  405  HIS   B C    
2175 O  O    . HIS   B 19  ? 1.0137 0.7444 0.9415 0.0344  -0.0550 0.0549  405  HIS   B O    
2176 C  CB   . HIS   B 19  ? 0.8271 0.5293 0.7417 0.0627  -0.0718 0.0464  405  HIS   B CB   
2177 C  CG   . HIS   B 19  ? 0.8338 0.5576 0.7516 0.0710  -0.0686 0.0453  405  HIS   B CG   
2178 N  ND1  . HIS   B 19  ? 0.8592 0.5967 0.7815 0.0843  -0.0688 0.0367  405  HIS   B ND1  
2179 C  CD2  . HIS   B 19  ? 0.8245 0.5598 0.7418 0.0675  -0.0650 0.0517  405  HIS   B CD2  
2180 C  CE1  . HIS   B 19  ? 0.8370 0.5936 0.7620 0.0881  -0.0658 0.0382  405  HIS   B CE1  
2181 N  NE2  . HIS   B 19  ? 0.8605 0.6152 0.7821 0.0783  -0.0637 0.0469  405  HIS   B NE2  
2182 N  N    . LEU   B 20  ? 0.7689 0.5290 0.7102 0.0456  -0.0493 0.0408  406  LEU   B N    
2183 C  CA   . LEU   B 20  ? 0.7007 0.4782 0.6494 0.0346  -0.0408 0.0433  406  LEU   B CA   
2184 C  C    . LEU   B 20  ? 0.6537 0.4523 0.6053 0.0365  -0.0354 0.0444  406  LEU   B C    
2185 O  O    . LEU   B 20  ? 0.6165 0.4259 0.5699 0.0465  -0.0359 0.0397  406  LEU   B O    
2186 C  CB   . LEU   B 20  ? 0.6742 0.4609 0.6314 0.0330  -0.0376 0.0365  406  LEU   B CB   
2187 C  CG   . LEU   B 20  ? 0.7074 0.4749 0.6621 0.0324  -0.0435 0.0335  406  LEU   B CG   
2188 C  CD1  . LEU   B 20  ? 0.6952 0.4744 0.6582 0.0310  -0.0400 0.0268  406  LEU   B CD1  
2189 C  CD2  . LEU   B 20  ? 0.7828 0.5332 0.7332 0.0204  -0.0457 0.0413  406  LEU   B CD2  
2190 N  N    . SER   B 21  ? 0.6296 0.4350 0.5818 0.0267  -0.0302 0.0503  407  SER   B N    
2191 C  CA   . SER   B 21  ? 0.6075 0.4328 0.5626 0.0269  -0.0247 0.0508  407  SER   B CA   
2192 C  C    . SER   B 21  ? 0.5467 0.3904 0.5117 0.0252  -0.0186 0.0451  407  SER   B C    
2193 O  O    . SER   B 21  ? 0.5183 0.3632 0.4877 0.0172  -0.0151 0.0453  407  SER   B O    
2194 C  CB   . SER   B 21  ? 0.6479 0.4725 0.5983 0.0179  -0.0218 0.0590  407  SER   B CB   
2195 O  OG   . SER   B 21  ? 0.6200 0.4642 0.5738 0.0165  -0.0158 0.0584  407  SER   B OG   
2196 N  N    . ILE   B 22  ? 0.5453 0.4038 0.5142 0.0323  -0.0175 0.0403  408  ILE   B N    
2197 C  CA   . ILE   B 22  ? 0.4961 0.3707 0.4736 0.0315  -0.0127 0.0350  408  ILE   B CA   
2198 C  C    . ILE   B 22  ? 0.4743 0.3664 0.4538 0.0313  -0.0088 0.0352  408  ILE   B C    
2199 O  O    . ILE   B 22  ? 0.5144 0.4104 0.4911 0.0373  -0.0113 0.0358  408  ILE   B O    
2200 C  CB   . ILE   B 22  ? 0.5170 0.3922 0.4970 0.0401  -0.0158 0.0281  408  ILE   B CB   
2201 C  CG1  . ILE   B 22  ? 0.5244 0.3799 0.5012 0.0401  -0.0205 0.0274  408  ILE   B CG1  
2202 C  CG2  . ILE   B 22  ? 0.4822 0.3746 0.4703 0.0391  -0.0110 0.0234  408  ILE   B CG2  
2203 C  CD1  . ILE   B 22  ? 0.4963 0.3516 0.4748 0.0484  -0.0234 0.0200  408  ILE   B CD1  
2204 N  N    . VAL   B 23  ? 0.4383 0.3408 0.4226 0.0247  -0.0031 0.0347  409  VAL   B N    
2205 C  CA   . VAL   B 23  ? 0.4111 0.3284 0.3967 0.0234  0.0003  0.0348  409  VAL   B CA   
2206 C  C    . VAL   B 23  ? 0.4612 0.3917 0.4539 0.0253  0.0023  0.0293  409  VAL   B C    
2207 O  O    . VAL   B 23  ? 0.4353 0.3648 0.4323 0.0245  0.0032  0.0263  409  VAL   B O    
2208 C  CB   . VAL   B 23  ? 0.4633 0.3818 0.4475 0.0150  0.0049  0.0384  409  VAL   B CB   
2209 C  CG1  . VAL   B 23  ? 0.4171 0.3373 0.4073 0.0094  0.0089  0.0365  409  VAL   B CG1  
2210 C  CG2  . VAL   B 23  ? 0.4321 0.3628 0.4152 0.0144  0.0071  0.0385  409  VAL   B CG2  
2211 N  N    . THR   B 24  ? 0.4556 0.3987 0.4490 0.0275  0.0027  0.0284  410  THR   B N    
2212 C  CA   . THR   B 24  ? 0.3997 0.3566 0.3991 0.0279  0.0046  0.0244  410  THR   B CA   
2213 C  C    . THR   B 24  ? 0.4384 0.4058 0.4373 0.0244  0.0066  0.0256  410  THR   B C    
2214 O  O    . THR   B 24  ? 0.4284 0.3924 0.4223 0.0216  0.0069  0.0289  410  THR   B O    
2215 C  CB   . THR   B 24  ? 0.4127 0.3750 0.4142 0.0362  0.0014  0.0211  410  THR   B CB   
2216 O  OG1  . THR   B 24  ? 0.4605 0.4361 0.4677 0.0356  0.0037  0.0178  410  THR   B OG1  
2217 C  CG2  . THR   B 24  ? 0.4324 0.3998 0.4311 0.0415  -0.0018 0.0227  410  THR   B CG2  
2218 N  N    . LEU   B 25  ? 0.3864 0.3661 0.3898 0.0241  0.0076  0.0228  411  LEU   B N    
2219 C  CA   . LEU   B 25  ? 0.3791 0.3681 0.3823 0.0200  0.0089  0.0233  411  LEU   B CA   
2220 C  C    . LEU   B 25  ? 0.3979 0.4009 0.4061 0.0215  0.0083  0.0208  411  LEU   B C    
2221 O  O    . LEU   B 25  ? 0.3796 0.3847 0.3919 0.0229  0.0090  0.0184  411  LEU   B O    
2222 C  CB   . LEU   B 25  ? 0.4209 0.4060 0.4237 0.0134  0.0126  0.0232  411  LEU   B CB   
2223 C  CG   . LEU   B 25  ? 0.3775 0.3701 0.3803 0.0089  0.0138  0.0224  411  LEU   B CG   
2224 C  CD1  . LEU   B 25  ? 0.4137 0.4062 0.4103 0.0078  0.0127  0.0246  411  LEU   B CD1  
2225 C  CD2  . LEU   B 25  ? 0.4388 0.4269 0.4426 0.0045  0.0172  0.0212  411  LEU   B CD2  
2226 N  N    . GLU   B 26  ? 0.3794 0.3927 0.3873 0.0208  0.0068  0.0216  412  GLU   B N    
2227 C  CA   . GLU   B 26  ? 0.3766 0.4053 0.3896 0.0214  0.0061  0.0201  412  GLU   B CA   
2228 C  C    . GLU   B 26  ? 0.4187 0.4500 0.4342 0.0147  0.0087  0.0191  412  GLU   B C    
2229 O  O    . GLU   B 26  ? 0.3492 0.3759 0.3617 0.0090  0.0097  0.0198  412  GLU   B O    
2230 C  CB   . GLU   B 26  ? 0.3857 0.4256 0.3982 0.0217  0.0033  0.0216  412  GLU   B CB   
2231 C  CG   . GLU   B 26  ? 0.3943 0.4528 0.4129 0.0212  0.0027  0.0206  412  GLU   B CG   
2232 C  CD   . GLU   B 26  ? 0.4284 0.4999 0.4476 0.0227  -0.0008 0.0220  412  GLU   B CD   
2233 O  OE1  . GLU   B 26  ? 0.4572 0.5236 0.4714 0.0205  -0.0024 0.0238  412  GLU   B OE1  
2234 O  OE2  . GLU   B 26  ? 0.4549 0.5425 0.4796 0.0265  -0.0019 0.0213  412  GLU   B OE2  
2235 N  N    . GLU   B 27  ? 0.3476 0.3861 0.3676 0.0159  0.0095  0.0173  413  GLU   B N    
2236 C  CA   . GLU   B 27  ? 0.3753 0.4176 0.3975 0.0099  0.0112  0.0169  413  GLU   B CA   
2237 C  C    . GLU   B 27  ? 0.3925 0.4472 0.4193 0.0128  0.0113  0.0156  413  GLU   B C    
2238 O  O    . GLU   B 27  ? 0.4040 0.4546 0.4317 0.0165  0.0123  0.0136  413  GLU   B O    
2239 C  CB   . GLU   B 27  ? 0.4001 0.4290 0.4208 0.0070  0.0135  0.0161  413  GLU   B CB   
2240 C  CG   . GLU   B 27  ? 0.3957 0.4275 0.4181 0.0016  0.0146  0.0158  413  GLU   B CG   
2241 C  CD   . GLU   B 27  ? 0.4179 0.4379 0.4379 -0.0024 0.0161  0.0156  413  GLU   B CD   
2242 O  OE1  . GLU   B 27  ? 0.4436 0.4546 0.4634 -0.0004 0.0175  0.0148  413  GLU   B OE1  
2243 O  OE2  . GLU   B 27  ? 0.4010 0.4211 0.4193 -0.0076 0.0156  0.0161  413  GLU   B OE2  
2244 N  N    . ALA   B 28  ? 0.3505 0.4212 0.3800 0.0111  0.0103  0.0166  414  ALA   B N    
2245 C  CA   . ALA   B 28  ? 0.3435 0.4290 0.3773 0.0144  0.0108  0.0155  414  ALA   B CA   
2246 C  C    . ALA   B 28  ? 0.3685 0.4514 0.4027 0.0104  0.0130  0.0150  414  ALA   B C    
2247 O  O    . ALA   B 28  ? 0.3625 0.4385 0.3950 0.0031  0.0134  0.0164  414  ALA   B O    
2248 C  CB   . ALA   B 28  ? 0.3483 0.4538 0.3857 0.0118  0.0094  0.0174  414  ALA   B CB   
2249 N  N    . PRO   B 29  ? 0.3624 0.4511 0.3984 0.0153  0.0141  0.0129  415  PRO   B N    
2250 C  CA   . PRO   B 29  ? 0.4043 0.5024 0.4421 0.0248  0.0134  0.0104  415  PRO   B CA   
2251 C  C    . PRO   B 29  ? 0.3975 0.4793 0.4323 0.0316  0.0127  0.0075  415  PRO   B C    
2252 O  O    . PRO   B 29  ? 0.4133 0.4984 0.4483 0.0402  0.0119  0.0045  415  PRO   B O    
2253 C  CB   . PRO   B 29  ? 0.4154 0.5281 0.4555 0.0247  0.0153  0.0096  415  PRO   B CB   
2254 C  CG   . PRO   B 29  ? 0.3720 0.4721 0.4098 0.0185  0.0166  0.0102  415  PRO   B CG   
2255 C  CD   . PRO   B 29  ? 0.3714 0.4593 0.4074 0.0115  0.0158  0.0128  415  PRO   B CD   
2256 N  N    . PHE   B 30  ? 0.3356 0.3998 0.3677 0.0279  0.0128  0.0084  416  PHE   B N    
2257 C  CA   . PHE   B 30  ? 0.3690 0.4174 0.3985 0.0326  0.0120  0.0063  416  PHE   B CA   
2258 C  C    . PHE   B 30  ? 0.3462 0.3886 0.3734 0.0380  0.0095  0.0067  416  PHE   B C    
2259 O  O    . PHE   B 30  ? 0.3926 0.4275 0.4180 0.0450  0.0077  0.0044  416  PHE   B O    
2260 C  CB   . PHE   B 30  ? 0.3565 0.3911 0.3847 0.0262  0.0135  0.0073  416  PHE   B CB   
2261 C  CG   . PHE   B 30  ? 0.3701 0.4092 0.4000 0.0217  0.0153  0.0069  416  PHE   B CG   
2262 C  CD1  . PHE   B 30  ? 0.3765 0.4165 0.4067 0.0252  0.0154  0.0041  416  PHE   B CD1  
2263 C  CD2  . PHE   B 30  ? 0.3583 0.4006 0.3885 0.0145  0.0163  0.0094  416  PHE   B CD2  
2264 C  CE1  . PHE   B 30  ? 0.3782 0.4228 0.4092 0.0213  0.0167  0.0042  416  PHE   B CE1  
2265 C  CE2  . PHE   B 30  ? 0.3965 0.4419 0.4275 0.0105  0.0173  0.0096  416  PHE   B CE2  
2266 C  CZ   . PHE   B 30  ? 0.3655 0.4125 0.3969 0.0139  0.0176  0.0072  416  PHE   B CZ   
2267 N  N    . VAL   B 31  ? 0.3759 0.4208 0.4024 0.0351  0.0088  0.0096  417  VAL   B N    
2268 C  CA   . VAL   B 31  ? 0.3911 0.4321 0.4150 0.0402  0.0060  0.0107  417  VAL   B CA   
2269 C  C    . VAL   B 31  ? 0.3903 0.4465 0.4160 0.0385  0.0051  0.0127  417  VAL   B C    
2270 O  O    . VAL   B 31  ? 0.4065 0.4642 0.4320 0.0306  0.0062  0.0147  417  VAL   B O    
2271 C  CB   . VAL   B 31  ? 0.4335 0.4563 0.4528 0.0372  0.0058  0.0129  417  VAL   B CB   
2272 C  CG1  . VAL   B 31  ? 0.4082 0.4267 0.4237 0.0423  0.0025  0.0146  417  VAL   B CG1  
2273 C  CG2  . VAL   B 31  ? 0.3898 0.3982 0.4080 0.0372  0.0066  0.0113  417  VAL   B CG2  
2274 N  N    . ILE   B 32  ? 0.3694 0.4371 0.3971 0.0461  0.0027  0.0118  418  ILE   B N    
2275 C  CA   . ILE   B 32  ? 0.3650 0.4501 0.3956 0.0453  0.0013  0.0135  418  ILE   B CA   
2276 C  C    . ILE   B 32  ? 0.4433 0.5250 0.4711 0.0524  -0.0026 0.0144  418  ILE   B C    
2277 O  O    . ILE   B 32  ? 0.4318 0.5083 0.4583 0.0617  -0.0046 0.0123  418  ILE   B O    
2278 C  CB   . ILE   B 32  ? 0.3915 0.4988 0.4283 0.0479  0.0022  0.0117  418  ILE   B CB   
2279 C  CG1  . ILE   B 32  ? 0.3919 0.5017 0.4303 0.0399  0.0057  0.0117  418  ILE   B CG1  
2280 C  CG2  . ILE   B 32  ? 0.4112 0.5383 0.4519 0.0475  0.0002  0.0136  418  ILE   B CG2  
2281 C  CD1  . ILE   B 32  ? 0.3819 0.5112 0.4252 0.0429  0.0074  0.0097  418  ILE   B CD1  
2282 N  N    . VAL   B 33  ? 0.4147 0.4983 0.4407 0.0482  -0.0043 0.0174  419  VAL   B N    
2283 C  CA   . VAL   B 33  ? 0.4110 0.4900 0.4332 0.0540  -0.0083 0.0191  419  VAL   B CA   
2284 C  C    . VAL   B 33  ? 0.4366 0.5379 0.4638 0.0574  -0.0111 0.0194  419  VAL   B C    
2285 O  O    . VAL   B 33  ? 0.4376 0.5535 0.4687 0.0502  -0.0102 0.0204  419  VAL   B O    
2286 C  CB   . VAL   B 33  ? 0.4349 0.4993 0.4503 0.0473  -0.0084 0.0223  419  VAL   B CB   
2287 C  CG1  . VAL   B 33  ? 0.4992 0.5602 0.5099 0.0527  -0.0129 0.0248  419  VAL   B CG1  
2288 C  CG2  . VAL   B 33  ? 0.4180 0.4624 0.4293 0.0449  -0.0057 0.0222  419  VAL   B CG2  
2289 N  N    . GLU   B 34  ? 0.4621 0.5661 0.4894 0.0685  -0.0147 0.0186  420  GLU   B N    
2290 C  CA   . GLU   B 34  ? 0.4728 0.5984 0.5050 0.0731  -0.0180 0.0190  420  GLU   B CA   
2291 C  C    . GLU   B 34  ? 0.5069 0.6233 0.5335 0.0800  -0.0232 0.0211  420  GLU   B C    
2292 O  O    . GLU   B 34  ? 0.4716 0.5657 0.4910 0.0830  -0.0243 0.0218  420  GLU   B O    
2293 C  CB   . GLU   B 34  ? 0.4729 0.6170 0.5122 0.0821  -0.0176 0.0153  420  GLU   B CB   
2294 C  CG   . GLU   B 34  ? 0.5909 0.7431 0.6345 0.0760  -0.0125 0.0135  420  GLU   B CG   
2295 C  CD   . GLU   B 34  ? 0.5688 0.7401 0.6186 0.0853  -0.0117 0.0096  420  GLU   B CD   
2296 O  OE1  . GLU   B 34  ? 0.5674 0.7332 0.6152 0.0979  -0.0143 0.0067  420  GLU   B OE1  
2297 O  OE2  . GLU   B 34  ? 0.6431 0.8342 0.6990 0.0800  -0.0086 0.0096  420  GLU   B OE2  
2298 N  N    . ASP   B 35  ? 0.5117 0.6460 0.5418 0.0820  -0.0268 0.0225  421  ASP   B N    
2299 C  CA   . ASP   B 35  ? 0.5754 0.7047 0.6009 0.0903  -0.0325 0.0244  421  ASP   B CA   
2300 C  C    . ASP   B 35  ? 0.5999 0.7311 0.6273 0.1054  -0.0353 0.0212  421  ASP   B C    
2301 O  O    . ASP   B 35  ? 0.5871 0.7303 0.6208 0.1097  -0.0328 0.0172  421  ASP   B O    
2302 C  CB   . ASP   B 35  ? 0.5888 0.7383 0.6179 0.0877  -0.0359 0.0267  421  ASP   B CB   
2303 C  CG   . ASP   B 35  ? 0.6418 0.7876 0.6674 0.0736  -0.0343 0.0293  421  ASP   B CG   
2304 O  OD1  . ASP   B 35  ? 0.6699 0.7931 0.6872 0.0686  -0.0324 0.0307  421  ASP   B OD1  
2305 O  OD2  . ASP   B 35  ? 0.7352 0.9008 0.7664 0.0675  -0.0351 0.0300  421  ASP   B OD2  
2306 N  N    . ILE   B 36  ? 0.5260 0.6450 0.5471 0.1139  -0.0408 0.0229  422  ILE   B N    
2307 C  CA   . ILE   B 36  ? 0.6881 0.8112 0.7111 0.1296  -0.0447 0.0197  422  ILE   B CA   
2308 C  C    . ILE   B 36  ? 0.6552 0.7954 0.6809 0.1364  -0.0506 0.0215  422  ILE   B C    
2309 O  O    . ILE   B 36  ? 0.8267 0.9877 0.8598 0.1474  -0.0526 0.0183  422  ILE   B O    
2310 C  CB   . ILE   B 36  ? 0.6934 0.7856 0.7065 0.1362  -0.0472 0.0195  422  ILE   B CB   
2311 C  CG1  . ILE   B 36  ? 0.7959 0.8908 0.8098 0.1537  -0.0525 0.0158  422  ILE   B CG1  
2312 C  CG2  . ILE   B 36  ? 0.6358 0.7069 0.6387 0.1310  -0.0502 0.0254  422  ILE   B CG2  
2313 C  CD1  . ILE   B 36  ? 0.7668 0.8885 0.7914 0.1602  -0.0497 0.0099  422  ILE   B CD1  
2314 N  N    . GLU   B 41  ? 0.8640 0.9576 0.8709 0.1965  -0.0751 0.0160  427  GLU   B N    
2315 C  CA   . GLU   B 41  ? 0.8560 0.9217 0.8537 0.1831  -0.0723 0.0202  427  GLU   B CA   
2316 C  C    . GLU   B 41  ? 0.8764 0.9203 0.8698 0.1855  -0.0706 0.0162  427  GLU   B C    
2317 O  O    . GLU   B 41  ? 0.9439 0.9571 0.9267 0.1834  -0.0731 0.0192  427  GLU   B O    
2318 C  CB   . GLU   B 41  ? 0.8510 0.8947 0.8372 0.1825  -0.0785 0.0271  427  GLU   B CB   
2319 N  N    . THR   B 42  ? 0.8584 0.9187 0.8598 0.1896  -0.0666 0.0096  428  THR   B N    
2320 C  CA   . THR   B 42  ? 0.8177 0.8607 0.8159 0.1915  -0.0647 0.0049  428  THR   B CA   
2321 C  C    . THR   B 42  ? 0.8261 0.8888 0.8331 0.1825  -0.0563 0.0018  428  THR   B C    
2322 O  O    . THR   B 42  ? 0.8691 0.9624 0.8859 0.1861  -0.0539 -0.0012 428  THR   B O    
2323 C  CB   . THR   B 42  ? 0.8847 0.9243 0.8812 0.2109  -0.0702 -0.0014 428  THR   B CB   
2324 O  OG1  . THR   B 42  ? 0.8686 0.9406 0.8761 0.2177  -0.0666 -0.0076 428  THR   B OG1  
2325 C  CG2  . THR   B 42  ? 0.8840 0.9170 0.8755 0.2223  -0.0790 0.0014  428  THR   B CG2  
2326 N  N    . CYS   B 43  ? 0.7886 0.8344 0.7920 0.1707  -0.0520 0.0029  429  CYS   B N    
2327 C  CA   . CYS   B 43  ? 0.6948 0.7556 0.7052 0.1624  -0.0446 0.0002  429  CYS   B CA   
2328 C  C    . CYS   B 43  ? 0.7208 0.7917 0.7346 0.1744  -0.0441 -0.0075 429  CYS   B C    
2329 O  O    . CYS   B 43  ? 0.7592 0.8108 0.7664 0.1849  -0.0484 -0.0112 429  CYS   B O    
2330 C  CB   . CYS   B 43  ? 0.6320 0.6703 0.6372 0.1495  -0.0412 0.0025  429  CYS   B CB   
2331 S  SG   . CYS   B 43  ? 0.6011 0.6306 0.6025 0.1347  -0.0402 0.0109  429  CYS   B SG   
2332 N  N    . VAL   B 44  ? 0.6869 0.7875 0.7102 0.1727  -0.0391 -0.0100 430  VAL   B N    
2333 C  CA   . VAL   B 44  ? 0.7512 0.8674 0.7783 0.1846  -0.0380 -0.0173 430  VAL   B CA   
2334 C  C    . VAL   B 44  ? 0.6880 0.8123 0.7184 0.1755  -0.0310 -0.0193 430  VAL   B C    
2335 O  O    . VAL   B 44  ? 0.6770 0.7927 0.7066 0.1608  -0.0275 -0.0153 430  VAL   B O    
2336 C  CB   . VAL   B 44  ? 0.7141 0.8638 0.7500 0.1941  -0.0391 -0.0186 430  VAL   B CB   
2337 C  CG1  . VAL   B 44  ? 0.7848 0.9270 0.8175 0.2026  -0.0465 -0.0160 430  VAL   B CG1  
2338 C  CG2  . VAL   B 44  ? 0.7429 0.9209 0.7885 0.1807  -0.0336 -0.0146 430  VAL   B CG2  
2339 N  N    . ARG   B 45  ? 0.7044 0.8451 0.7379 0.1850  -0.0292 -0.0258 431  ARG   B N    
2340 C  CA   . ARG   B 45  ? 0.7368 0.8919 0.7742 0.1782  -0.0225 -0.0279 431  ARG   B CA   
2341 C  C    . ARG   B 45  ? 0.6961 0.8226 0.7265 0.1684  -0.0212 -0.0272 431  ARG   B C    
2342 O  O    . ARG   B 45  ? 0.6741 0.7730 0.6963 0.1741  -0.0255 -0.0296 431  ARG   B O    
2343 C  CB   . ARG   B 45  ? 0.7645 0.9501 0.8116 0.1676  -0.0180 -0.0233 431  ARG   B CB   
2344 C  CG   . ARG   B 45  ? 0.7924 1.0129 0.8481 0.1779  -0.0181 -0.0255 431  ARG   B CG   
2345 C  CD   . ARG   B 45  ? 0.8273 1.0799 0.8919 0.1682  -0.0117 -0.0238 431  ARG   B CD   
2346 N  NE   . ARG   B 45  ? 0.8702 1.1492 0.9437 0.1637  -0.0121 -0.0191 431  ARG   B NE   
2347 C  CZ   . ARG   B 45  ? 0.8179 1.1292 0.9003 0.1567  -0.0077 -0.0172 431  ARG   B CZ   
2348 N  NH1  . ARG   B 45  ? 0.7705 1.0926 0.8539 0.1536  -0.0023 -0.0192 431  ARG   B NH1  
2349 N  NH2  . ARG   B 45  ? 0.7961 1.1297 0.8863 0.1523  -0.0090 -0.0129 431  ARG   B NH2  
2350 N  N    . ASN   B 46  ? 0.7473 0.8788 0.7806 0.1538  -0.0159 -0.0239 432  ASN   B N    
2351 C  CA   . ASN   B 46  ? 0.7283 0.8359 0.7562 0.1451  -0.0145 -0.0235 432  ASN   B CA   
2352 C  C    . ASN   B 46  ? 0.6991 0.7862 0.7238 0.1343  -0.0157 -0.0171 432  ASN   B C    
2353 O  O    . ASN   B 46  ? 0.6625 0.7367 0.6853 0.1238  -0.0132 -0.0153 432  ASN   B O    
2354 C  CB   . ASN   B 46  ? 0.7681 0.8909 0.8000 0.1362  -0.0083 -0.0237 432  ASN   B CB   
2355 C  CG   . ASN   B 46  ? 0.7985 0.9478 0.8385 0.1273  -0.0048 -0.0189 432  ASN   B CG   
2356 O  OD1  . ASN   B 46  ? 0.8405 1.0014 0.8841 0.1295  -0.0068 -0.0165 432  ASN   B OD1  
2357 N  ND2  . ASN   B 46  ? 0.7033 0.8618 0.7458 0.1172  0.0000  -0.0175 432  ASN   B ND2  
2358 N  N    . THR   B 47  ? 0.6422 0.7271 0.6662 0.1370  -0.0195 -0.0139 433  THR   B N    
2359 C  CA   . THR   B 47  ? 0.5783 0.6463 0.5987 0.1273  -0.0205 -0.0077 433  THR   B CA   
2360 C  C    . THR   B 47  ? 0.5912 0.6290 0.6027 0.1320  -0.0256 -0.0075 433  THR   B C    
2361 O  O    . THR   B 47  ? 0.5816 0.6120 0.5895 0.1445  -0.0299 -0.0118 433  THR   B O    
2362 C  CB   . THR   B 47  ? 0.5216 0.6052 0.5457 0.1257  -0.0217 -0.0034 433  THR   B CB   
2363 O  OG1  . THR   B 47  ? 0.6680 0.7489 0.6895 0.1385  -0.0276 -0.0043 433  THR   B OG1  
2364 C  CG2  . THR   B 47  ? 0.5228 0.6386 0.5562 0.1227  -0.0178 -0.0039 433  THR   B CG2  
2365 N  N    . VAL   B 48  ? 0.5328 0.5528 0.5402 0.1215  -0.0251 -0.0025 434  VAL   B N    
2366 C  CA   . VAL   B 48  ? 0.5199 0.5112 0.5186 0.1229  -0.0298 -0.0005 434  VAL   B CA   
2367 C  C    . VAL   B 48  ? 0.5290 0.5161 0.5251 0.1162  -0.0307 0.0064  434  VAL   B C    
2368 O  O    . VAL   B 48  ? 0.5088 0.5087 0.5090 0.1067  -0.0265 0.0093  434  VAL   B O    
2369 C  CB   . VAL   B 48  ? 0.5503 0.5229 0.5460 0.1160  -0.0281 -0.0014 434  VAL   B CB   
2370 C  CG1  . VAL   B 48  ? 0.5716 0.5505 0.5695 0.1221  -0.0270 -0.0085 434  VAL   B CG1  
2371 C  CG2  . VAL   B 48  ? 0.5103 0.4846 0.5085 0.1011  -0.0226 0.0029  434  VAL   B CG2  
2372 N  N    . PRO   B 49  ? 0.5327 0.5019 0.5214 0.1209  -0.0363 0.0093  435  PRO   B N    
2373 C  CA   . PRO   B 49  ? 0.5175 0.4836 0.5028 0.1148  -0.0372 0.0161  435  PRO   B CA   
2374 C  C    . PRO   B 49  ? 0.5624 0.5185 0.5457 0.1005  -0.0327 0.0201  435  PRO   B C    
2375 O  O    . PRO   B 49  ? 0.5419 0.4827 0.5231 0.0965  -0.0316 0.0195  435  PRO   B O    
2376 C  CB   . PRO   B 49  ? 0.6165 0.5625 0.5931 0.1238  -0.0447 0.0181  435  PRO   B CB   
2377 C  CG   . PRO   B 49  ? 0.5962 0.5275 0.5704 0.1310  -0.0472 0.0129  435  PRO   B CG   
2378 C  CD   . PRO   B 49  ? 0.5436 0.4959 0.5264 0.1332  -0.0427 0.0064  435  PRO   B CD   
2379 N  N    . CYS   B 50  ? 0.5155 0.4822 0.5000 0.0930  -0.0301 0.0238  436  CYS   B N    
2380 C  CA   . CYS   B 50  ? 0.5095 0.4688 0.4916 0.0805  -0.0259 0.0277  436  CYS   B CA   
2381 C  C    . CYS   B 50  ? 0.5363 0.4985 0.5142 0.0775  -0.0272 0.0328  436  CYS   B C    
2382 O  O    . CYS   B 50  ? 0.5555 0.5343 0.5364 0.0813  -0.0288 0.0323  436  CYS   B O    
2383 C  CB   . CYS   B 50  ? 0.4957 0.4682 0.4851 0.0731  -0.0197 0.0249  436  CYS   B CB   
2384 S  SG   . CYS   B 50  ? 0.5692 0.5715 0.5673 0.0742  -0.0180 0.0221  436  CYS   B SG   
2385 N  N    . ARG   B 51  ? 0.5299 0.4772 0.5008 0.0706  -0.0265 0.0377  437  ARG   B N    
2386 C  CA   . ARG   B 51  ? 0.5290 0.4775 0.4941 0.0676  -0.0277 0.0427  437  ARG   B CA   
2387 C  C    . ARG   B 51  ? 0.5016 0.4568 0.4676 0.0566  -0.0219 0.0435  437  ARG   B C    
2388 O  O    . ARG   B 51  ? 0.5082 0.4609 0.4773 0.0507  -0.0172 0.0419  437  ARG   B O    
2389 C  CB   . ARG   B 51  ? 0.5809 0.5081 0.5356 0.0684  -0.0318 0.0484  437  ARG   B CB   
2390 C  CG   . ARG   B 51  ? 0.6347 0.5439 0.5867 0.0623  -0.0296 0.0500  437  ARG   B CG   
2391 C  CD   . ARG   B 51  ? 0.7044 0.5917 0.6458 0.0632  -0.0346 0.0562  437  ARG   B CD   
2392 N  NE   . ARG   B 51  ? 0.7050 0.5760 0.6448 0.0569  -0.0330 0.0576  437  ARG   B NE   
2393 C  CZ   . ARG   B 51  ? 0.7247 0.5923 0.6622 0.0460  -0.0283 0.0617  437  ARG   B CZ   
2394 N  NH1  . ARG   B 51  ? 0.6539 0.5319 0.5894 0.0405  -0.0246 0.0643  437  ARG   B NH1  
2395 N  NH2  . ARG   B 51  ? 0.7081 0.5625 0.6454 0.0406  -0.0274 0.0627  437  ARG   B NH2  
2396 N  N    . LYS   B 52  ? 0.4843 0.4485 0.4475 0.0545  -0.0226 0.0457  438  LYS   B N    
2397 C  CA   . LYS   B 52  ? 0.4566 0.4264 0.4189 0.0452  -0.0180 0.0462  438  LYS   B CA   
2398 C  C    . LYS   B 52  ? 0.5136 0.4784 0.4658 0.0433  -0.0201 0.0514  438  LYS   B C    
2399 O  O    . LYS   B 52  ? 0.5016 0.4712 0.4513 0.0487  -0.0252 0.0530  438  LYS   B O    
2400 C  CB   . LYS   B 52  ? 0.4767 0.4661 0.4465 0.0438  -0.0168 0.0422  438  LYS   B CB   
2401 C  CG   . LYS   B 52  ? 0.5188 0.5123 0.4860 0.0350  -0.0134 0.0424  438  LYS   B CG   
2402 C  CD   . LYS   B 52  ? 0.6013 0.6096 0.5764 0.0314  -0.0113 0.0382  438  LYS   B CD   
2403 C  CE   . LYS   B 52  ? 0.7056 0.7309 0.6854 0.0354  -0.0154 0.0372  438  LYS   B CE   
2404 N  NZ   . LYS   B 52  ? 0.6807 0.7200 0.6676 0.0302  -0.0135 0.0341  438  LYS   B NZ   
2405 N  N    . PHE   B 53  ? 0.4680 0.4233 0.4143 0.0362  -0.0164 0.0542  439  PHE   B N    
2406 C  CA   . PHE   B 53  ? 0.5009 0.4517 0.4366 0.0332  -0.0173 0.0593  439  PHE   B CA   
2407 C  C    . PHE   B 53  ? 0.4811 0.4459 0.4164 0.0298  -0.0163 0.0572  439  PHE   B C    
2408 O  O    . PHE   B 53  ? 0.4584 0.4284 0.3973 0.0244  -0.0116 0.0537  439  PHE   B O    
2409 C  CB   . PHE   B 53  ? 0.5591 0.4977 0.4896 0.0264  -0.0128 0.0626  439  PHE   B CB   
2410 C  CG   . PHE   B 53  ? 0.6036 0.5371 0.5222 0.0232  -0.0132 0.0685  439  PHE   B CG   
2411 C  CD1  . PHE   B 53  ? 0.5834 0.5049 0.4940 0.0264  -0.0181 0.0745  439  PHE   B CD1  
2412 C  CD2  . PHE   B 53  ? 0.6160 0.5560 0.5305 0.0171  -0.0088 0.0679  439  PHE   B CD2  
2413 C  CE1  . PHE   B 53  ? 0.6601 0.5770 0.5587 0.0230  -0.0185 0.0805  439  PHE   B CE1  
2414 C  CE2  . PHE   B 53  ? 0.6264 0.5625 0.5290 0.0143  -0.0089 0.0732  439  PHE   B CE2  
2415 C  CZ   . PHE   B 53  ? 0.6359 0.5608 0.5305 0.0169  -0.0136 0.0798  439  PHE   B CZ   
2416 N  N    . VAL   B 54  ? 0.4905 0.4606 0.4212 0.0332  -0.0213 0.0591  440  VAL   B N    
2417 C  CA   . VAL   B 54  ? 0.4659 0.4489 0.3956 0.0301  -0.0219 0.0570  440  VAL   B CA   
2418 C  C    . VAL   B 54  ? 0.4934 0.4714 0.4101 0.0276  -0.0232 0.0616  440  VAL   B C    
2419 O  O    . VAL   B 54  ? 0.4434 0.4147 0.3536 0.0320  -0.0277 0.0665  440  VAL   B O    
2420 C  CB   . VAL   B 54  ? 0.4214 0.4193 0.3584 0.0357  -0.0270 0.0547  440  VAL   B CB   
2421 C  CG1  . VAL   B 54  ? 0.4369 0.4477 0.3731 0.0311  -0.0280 0.0527  440  VAL   B CG1  
2422 C  CG2  . VAL   B 54  ? 0.4715 0.4752 0.4207 0.0382  -0.0252 0.0504  440  VAL   B CG2  
2423 N  N    . LYS   B 55  ? 0.4694 0.4498 0.3815 0.0210  -0.0195 0.0600  441  LYS   B N    
2424 C  CA   . LYS   B 55  ? 0.4678 0.4437 0.3664 0.0183  -0.0198 0.0639  441  LYS   B CA   
2425 C  C    . LYS   B 55  ? 0.5042 0.4881 0.3982 0.0213  -0.0265 0.0649  441  LYS   B C    
2426 O  O    . LYS   B 55  ? 0.4175 0.4138 0.3188 0.0225  -0.0296 0.0612  441  LYS   B O    
2427 C  CB   . LYS   B 55  ? 0.5465 0.5233 0.4413 0.0114  -0.0139 0.0608  441  LYS   B CB   
2428 C  CG   . LYS   B 55  ? 0.6183 0.5862 0.5135 0.0082  -0.0072 0.0618  441  LYS   B CG   
2429 C  CD   . LYS   B 55  ? 0.7199 0.6917 0.6246 0.0054  -0.0025 0.0558  441  LYS   B CD   
2430 C  CE   . LYS   B 55  ? 0.8157 0.7801 0.7234 0.0031  0.0032  0.0569  441  LYS   B CE   
2431 N  NZ   . LYS   B 55  ? 0.7262 0.6927 0.6466 0.0036  0.0048  0.0525  441  LYS   B NZ   
2432 N  N    . ILE   B 56  ? 0.4562 0.4337 0.3378 0.0220  -0.0291 0.0706  442  ILE   B N    
2433 C  CA   . ILE   B 56  ? 0.5278 0.5128 0.4038 0.0247  -0.0359 0.0719  442  ILE   B CA   
2434 C  C    . ILE   B 56  ? 0.5366 0.5297 0.4079 0.0189  -0.0349 0.0677  442  ILE   B C    
2435 O  O    . ILE   B 56  ? 0.4787 0.4836 0.3529 0.0195  -0.0397 0.0650  442  ILE   B O    
2436 C  CB   . ILE   B 56  ? 0.5461 0.5206 0.4093 0.0274  -0.0395 0.0797  442  ILE   B CB   
2437 C  CG1  . ILE   B 56  ? 0.5972 0.5616 0.4646 0.0336  -0.0419 0.0834  442  ILE   B CG1  
2438 C  CG2  . ILE   B 56  ? 0.5717 0.5546 0.4287 0.0303  -0.0469 0.0810  442  ILE   B CG2  
2439 C  CD1  . ILE   B 56  ? 0.5425 0.5167 0.4222 0.0412  -0.0469 0.0800  442  ILE   B CD1  
2440 N  N    . ASN   B 57  ? 0.5291 0.5163 0.3927 0.0135  -0.0289 0.0672  443  ASN   B N    
2441 C  CA   . ASN   B 57  ? 0.5406 0.5330 0.3985 0.0084  -0.0275 0.0624  443  ASN   B CA   
2442 C  C    . ASN   B 57  ? 0.6846 0.6705 0.5395 0.0040  -0.0192 0.0606  443  ASN   B C    
2443 O  O    . ASN   B 57  ? 0.6538 0.6325 0.5118 0.0042  -0.0148 0.0634  443  ASN   B O    
2444 C  CB   . ASN   B 57  ? 0.6074 0.6018 0.4513 0.0086  -0.0327 0.0650  443  ASN   B CB   
2445 C  CG   . ASN   B 57  ? 0.7089 0.6934 0.5395 0.0088  -0.0309 0.0720  443  ASN   B CG   
2446 O  OD1  . ASN   B 57  ? 0.7894 0.7692 0.6131 0.0049  -0.0244 0.0718  443  ASN   B OD1  
2447 N  ND2  . ASN   B 57  ? 0.7079 0.6902 0.5338 0.0133  -0.0370 0.0782  443  ASN   B ND2  
2448 N  N    . ASN   B 58  ? 0.7194 0.7080 0.5685 0.0002  -0.0173 0.0555  444  ASN   B N    
2449 C  CA   . ASN   B 58  ? 0.6585 0.6431 0.5057 -0.0031 -0.0096 0.0524  444  ASN   B CA   
2450 C  C    . ASN   B 58  ? 0.6897 0.6708 0.5216 -0.0045 -0.0062 0.0555  444  ASN   B C    
2451 O  O    . ASN   B 58  ? 0.7411 0.7204 0.5706 -0.0067 0.0005  0.0533  444  ASN   B O    
2452 C  CB   . ASN   B 58  ? 0.6565 0.6450 0.5067 -0.0058 -0.0095 0.0443  444  ASN   B CB   
2453 C  CG   . ASN   B 58  ? 0.6760 0.6686 0.5416 -0.0054 -0.0114 0.0418  444  ASN   B CG   
2454 O  OD1  . ASN   B 58  ? 0.6700 0.6607 0.5451 -0.0035 -0.0093 0.0442  444  ASN   B OD1  
2455 N  ND2  . ASN   B 58  ? 0.6242 0.6224 0.4919 -0.0075 -0.0158 0.0371  444  ASN   B ND2  
2456 N  N    . SER   B 59  ? 0.7141 0.6948 0.5354 -0.0031 -0.0108 0.0608  445  SER   B N    
2457 C  CA   . SER   B 59  ? 0.7946 0.7719 0.6009 -0.0045 -0.0077 0.0655  445  SER   B CA   
2458 C  C    . SER   B 59  ? 0.8438 0.8140 0.6500 -0.0037 -0.0070 0.0746  445  SER   B C    
2459 O  O    . SER   B 59  ? 0.8744 0.8415 0.6673 -0.0047 -0.0067 0.0809  445  SER   B O    
2460 C  CB   . SER   B 59  ? 0.8324 0.8130 0.6245 -0.0041 -0.0134 0.0656  445  SER   B CB   
2461 O  OG   . SER   B 59  ? 0.8615 0.8435 0.6563 -0.0008 -0.0217 0.0694  445  SER   B OG   
2462 N  N    . THR   B 60  ? 0.7919 0.7588 0.6118 -0.0021 -0.0071 0.0755  446  THR   B N    
2463 C  CA   . THR   B 60  ? 0.7472 0.7051 0.5670 -0.0012 -0.0077 0.0837  446  THR   B CA   
2464 C  C    . THR   B 60  ? 0.7326 0.6870 0.5665 -0.0017 -0.0037 0.0823  446  THR   B C    
2465 O  O    . THR   B 60  ? 0.6755 0.6350 0.5206 -0.0014 -0.0021 0.0754  446  THR   B O    
2466 C  CB   . THR   B 60  ? 0.8005 0.7561 0.6191 0.0041  -0.0168 0.0881  446  THR   B CB   
2467 O  OG1  . THR   B 60  ? 0.8266 0.7706 0.6411 0.0046  -0.0178 0.0968  446  THR   B OG1  
2468 C  CG2  . THR   B 60  ? 0.7372 0.6973 0.5712 0.0084  -0.0206 0.0832  446  THR   B CG2  
2469 N  N    . ASN   B 61  ? 0.7576 0.7027 0.5902 -0.0030 -0.0024 0.0893  447  ASN   B N    
2470 C  CA   . ASN   B 61  ? 0.7143 0.6541 0.5594 -0.0030 -0.0004 0.0890  447  ASN   B CA   
2471 C  C    . ASN   B 61  ? 0.6878 0.6212 0.5385 0.0028  -0.0077 0.0911  447  ASN   B C    
2472 O  O    . ASN   B 61  ? 0.7168 0.6453 0.5776 0.0039  -0.0072 0.0901  447  ASN   B O    
2473 C  CB   . ASN   B 61  ? 0.6807 0.6136 0.5217 -0.0085 0.0049  0.0952  447  ASN   B CB   
2474 C  CG   . ASN   B 61  ? 0.7353 0.6766 0.5729 -0.0135 0.0130  0.0925  447  ASN   B CG   
2475 O  OD1  . ASN   B 61  ? 0.6816 0.6304 0.5267 -0.0131 0.0163  0.0846  447  ASN   B OD1  
2476 N  ND2  . ASN   B 61  ? 0.6633 0.6034 0.4890 -0.0179 0.0162  0.0991  447  ASN   B ND2  
2477 N  N    . GLU   B 62  ? 0.6333 0.5669 0.4771 0.0071  -0.0145 0.0936  448  GLU   B N    
2478 C  CA   . GLU   B 62  ? 0.6761 0.6040 0.5238 0.0140  -0.0220 0.0957  448  GLU   B CA   
2479 C  C    . GLU   B 62  ? 0.6184 0.5555 0.4810 0.0182  -0.0231 0.0879  448  GLU   B C    
2480 O  O    . GLU   B 62  ? 0.5881 0.5372 0.4544 0.0168  -0.0216 0.0820  448  GLU   B O    
2481 C  CB   . GLU   B 62  ? 0.6721 0.6000 0.5083 0.0176  -0.0290 0.1004  448  GLU   B CB   
2482 C  CG   . GLU   B 62  ? 0.7481 0.6747 0.5886 0.0266  -0.0377 0.1011  448  GLU   B CG   
2483 C  CD   . GLU   B 62  ? 0.8315 0.7572 0.6595 0.0301  -0.0450 0.1066  448  GLU   B CD   
2484 O  OE1  . GLU   B 62  ? 0.8467 0.7653 0.6743 0.0374  -0.0521 0.1102  448  GLU   B OE1  
2485 O  OE2  . GLU   B 62  ? 0.9072 0.8389 0.7253 0.0262  -0.0439 0.1072  448  GLU   B OE2  
2486 N  N    . GLY   B 63  ? 0.6129 0.5438 0.4836 0.0229  -0.0257 0.0880  449  GLY   B N    
2487 C  CA   . GLY   B 63  ? 0.5724 0.5124 0.4566 0.0274  -0.0270 0.0813  449  GLY   B CA   
2488 C  C    . GLY   B 63  ? 0.6023 0.5357 0.4894 0.0360  -0.0335 0.0832  449  GLY   B C    
2489 O  O    . GLY   B 63  ? 0.5892 0.5092 0.4676 0.0381  -0.0373 0.0896  449  GLY   B O    
2490 N  N    . MET   B 64  ? 0.5536 0.4964 0.4526 0.0412  -0.0350 0.0775  450  MET   B N    
2491 C  CA   . MET   B 64  ? 0.5793 0.5181 0.4823 0.0509  -0.0409 0.0776  450  MET   B CA   
2492 C  C    . MET   B 64  ? 0.5823 0.5248 0.4979 0.0525  -0.0379 0.0715  450  MET   B C    
2493 O  O    . MET   B 64  ? 0.5441 0.4995 0.4673 0.0486  -0.0336 0.0665  450  MET   B O    
2494 C  CB   . MET   B 64  ? 0.6155 0.5668 0.5191 0.0581  -0.0476 0.0771  450  MET   B CB   
2495 C  CG   . MET   B 64  ? 0.7022 0.6452 0.5921 0.0592  -0.0527 0.0842  450  MET   B CG   
2496 S  SD   . MET   B 64  ? 0.8683 0.8124 0.7581 0.0727  -0.0631 0.0860  450  MET   B SD   
2497 C  CE   . MET   B 64  ? 0.8123 0.7420 0.7082 0.0787  -0.0632 0.0840  450  MET   B CE   
2498 N  N    . ASN   B 65  ? 0.5794 0.5093 0.4962 0.0580  -0.0404 0.0720  451  ASN   B N    
2499 C  CA   . ASN   B 65  ? 0.6018 0.5347 0.5294 0.0605  -0.0382 0.0661  451  ASN   B CA   
2500 C  C    . ASN   B 65  ? 0.6463 0.5953 0.5821 0.0697  -0.0420 0.0616  451  ASN   B C    
2501 O  O    . ASN   B 65  ? 0.7252 0.6703 0.6590 0.0794  -0.0485 0.0627  451  ASN   B O    
2502 C  CB   . ASN   B 65  ? 0.6885 0.6012 0.6137 0.0626  -0.0397 0.0678  451  ASN   B CB   
2503 C  CG   . ASN   B 65  ? 0.6691 0.5698 0.5898 0.0523  -0.0346 0.0712  451  ASN   B CG   
2504 O  OD1  . ASN   B 65  ? 0.6546 0.5637 0.5796 0.0449  -0.0281 0.0688  451  ASN   B OD1  
2505 N  ND2  . ASN   B 65  ? 0.7779 0.6591 0.6897 0.0516  -0.0378 0.0772  451  ASN   B ND2  
2506 N  N    . VAL   B 66  ? 0.5530 0.5201 0.4980 0.0669  -0.0383 0.0566  452  VAL   B N    
2507 C  CA   . VAL   B 66  ? 0.5387 0.5241 0.4928 0.0745  -0.0410 0.0524  452  VAL   B CA   
2508 C  C    . VAL   B 66  ? 0.5883 0.5719 0.5494 0.0802  -0.0401 0.0479  452  VAL   B C    
2509 O  O    . VAL   B 66  ? 0.5298 0.5083 0.4936 0.0745  -0.0350 0.0458  452  VAL   B O    
2510 C  CB   . VAL   B 66  ? 0.5354 0.5411 0.4955 0.0680  -0.0380 0.0497  452  VAL   B CB   
2511 C  CG1  . VAL   B 66  ? 0.5284 0.5551 0.4989 0.0748  -0.0404 0.0458  452  VAL   B CG1  
2512 C  CG2  . VAL   B 66  ? 0.5609 0.5679 0.5129 0.0635  -0.0400 0.0536  452  VAL   B CG2  
2513 N  N    . LYS   B 67  ? 0.5201 0.5084 0.4841 0.0918  -0.0452 0.0460  453  LYS   B N    
2514 C  CA   . LYS   B 67  ? 0.5450 0.5326 0.5149 0.0987  -0.0448 0.0410  453  LYS   B CA   
2515 C  C    . LYS   B 67  ? 0.5811 0.5938 0.5625 0.0978  -0.0411 0.0359  453  LYS   B C    
2516 O  O    . LYS   B 67  ? 0.5772 0.6100 0.5634 0.1010  -0.0433 0.0354  453  LYS   B O    
2517 C  CB   . LYS   B 67  ? 0.5033 0.4841 0.4703 0.1127  -0.0521 0.0407  453  LYS   B CB   
2518 N  N    . LYS   B 68  ? 0.4957 0.5076 0.4813 0.0927  -0.0358 0.0327  454  LYS   B N    
2519 C  CA   . LYS   B 68  ? 0.4972 0.5313 0.4930 0.0917  -0.0323 0.0284  454  LYS   B CA   
2520 C  C    . LYS   B 68  ? 0.5268 0.5571 0.5258 0.0973  -0.0309 0.0236  454  LYS   B C    
2521 O  O    . LYS   B 68  ? 0.5074 0.5181 0.5008 0.1026  -0.0335 0.0234  454  LYS   B O    
2522 C  CB   . LYS   B 68  ? 0.5409 0.5806 0.5386 0.0785  -0.0270 0.0292  454  LYS   B CB   
2523 C  CG   . LYS   B 68  ? 0.5715 0.6054 0.5622 0.0716  -0.0278 0.0339  454  LYS   B CG   
2524 C  CD   . LYS   B 68  ? 0.6119 0.6550 0.6050 0.0605  -0.0237 0.0337  454  LYS   B CD   
2525 C  CE   . LYS   B 68  ? 0.6085 0.6762 0.6092 0.0607  -0.0251 0.0322  454  LYS   B CE   
2526 N  NZ   . LYS   B 68  ? 0.6328 0.7082 0.6313 0.0653  -0.0308 0.0346  454  LYS   B NZ   
2527 N  N    . CYS   B 69  ? 0.4749 0.5232 0.4821 0.0956  -0.0271 0.0199  455  CYS   B N    
2528 C  CA   . CYS   B 69  ? 0.4641 0.5128 0.4745 0.1009  -0.0255 0.0149  455  CYS   B CA   
2529 C  C    . CYS   B 69  ? 0.4582 0.5115 0.4725 0.0906  -0.0194 0.0138  455  CYS   B C    
2530 O  O    . CYS   B 69  ? 0.4583 0.5260 0.4766 0.0826  -0.0169 0.0153  455  CYS   B O    
2531 C  CB   . CYS   B 69  ? 0.5024 0.5724 0.5190 0.1125  -0.0276 0.0110  455  CYS   B CB   
2532 S  SG   . CYS   B 69  ? 0.5936 0.6617 0.6065 0.1262  -0.0356 0.0123  455  CYS   B SG   
2533 N  N    . CYS   B 70  ? 0.4216 0.4615 0.4342 0.0906  -0.0177 0.0113  456  CYS   B N    
2534 C  CA   . CYS   B 70  ? 0.4575 0.4977 0.4727 0.0815  -0.0126 0.0104  456  CYS   B CA   
2535 C  C    . CYS   B 70  ? 0.4783 0.5269 0.4973 0.0870  -0.0112 0.0052  456  CYS   B C    
2536 O  O    . CYS   B 70  ? 0.4901 0.5312 0.5065 0.0969  -0.0142 0.0018  456  CYS   B O    
2537 C  CB   . CYS   B 70  ? 0.4394 0.4558 0.4488 0.0752  -0.0118 0.0125  456  CYS   B CB   
2538 S  SG   . CYS   B 70  ? 0.5532 0.5634 0.5584 0.0656  -0.0111 0.0184  456  CYS   B SG   
2539 N  N    . LYS   B 71  ? 0.4470 0.5099 0.4710 0.0806  -0.0070 0.0045  457  LYS   B N    
2540 C  CA   . LYS   B 71  ? 0.4587 0.5295 0.4854 0.0840  -0.0049 0.0001  457  LYS   B CA   
2541 C  C    . LYS   B 71  ? 0.4612 0.5327 0.4898 0.0729  -0.0005 0.0012  457  LYS   B C    
2542 O  O    . LYS   B 71  ? 0.4120 0.4800 0.4402 0.0635  0.0008  0.0049  457  LYS   B O    
2543 C  CB   . LYS   B 71  ? 0.4623 0.5592 0.4947 0.0911  -0.0050 -0.0021 457  LYS   B CB   
2544 C  CG   . LYS   B 71  ? 0.4450 0.5628 0.4832 0.0823  -0.0025 0.0012  457  LYS   B CG   
2545 C  CD   . LYS   B 71  ? 0.4906 0.6364 0.5351 0.0890  -0.0030 -0.0002 457  LYS   B CD   
2546 C  CE   . LYS   B 71  ? 0.5167 0.6827 0.5669 0.0785  -0.0009 0.0037  457  LYS   B CE   
2547 N  NZ   . LYS   B 71  ? 0.4748 0.6715 0.5324 0.0840  -0.0011 0.0029  457  LYS   B NZ   
2548 N  N    . GLY   B 72  ? 0.4509 0.5264 0.4806 0.0745  0.0014  -0.0023 458  GLY   B N    
2549 C  CA   . GLY   B 72  ? 0.4224 0.5001 0.4537 0.0652  0.0051  -0.0015 458  GLY   B CA   
2550 C  C    . GLY   B 72  ? 0.4595 0.5232 0.4879 0.0664  0.0055  -0.0047 458  GLY   B C    
2551 O  O    . GLY   B 72  ? 0.3978 0.4487 0.4226 0.0737  0.0027  -0.0076 458  GLY   B O    
2552 N  N    . PHE   B 73  ? 0.4217 0.4873 0.4514 0.0587  0.0085  -0.0039 459  PHE   B N    
2553 C  CA   . PHE   B 73  ? 0.3869 0.4422 0.4144 0.0591  0.0088  -0.0070 459  PHE   B CA   
2554 C  C    . PHE   B 73  ? 0.4278 0.4599 0.4515 0.0597  0.0063  -0.0073 459  PHE   B C    
2555 O  O    . PHE   B 73  ? 0.3974 0.4199 0.4181 0.0657  0.0041  -0.0112 459  PHE   B O    
2556 C  CB   . PHE   B 73  ? 0.4039 0.4627 0.4331 0.0497  0.0118  -0.0049 459  PHE   B CB   
2557 C  CG   . PHE   B 73  ? 0.4045 0.4542 0.4316 0.0495  0.0120  -0.0077 459  PHE   B CG   
2558 C  CD1  . PHE   B 73  ? 0.4009 0.4320 0.4265 0.0463  0.0110  -0.0074 459  PHE   B CD1  
2559 C  CD2  . PHE   B 73  ? 0.4015 0.4627 0.4285 0.0517  0.0132  -0.0102 459  PHE   B CD2  
2560 C  CE1  . PHE   B 73  ? 0.4532 0.4766 0.4774 0.0459  0.0106  -0.0099 459  PHE   B CE1  
2561 C  CE2  . PHE   B 73  ? 0.4448 0.4978 0.4695 0.0514  0.0129  -0.0128 459  PHE   B CE2  
2562 C  CZ   . PHE   B 73  ? 0.4279 0.4619 0.4515 0.0484  0.0113  -0.0127 459  PHE   B CZ   
2563 N  N    . CYS   B 74  ? 0.3667 0.3896 0.3901 0.0532  0.0066  -0.0032 460  CYS   B N    
2564 C  CA   . CYS   B 74  ? 0.4252 0.4277 0.4453 0.0523  0.0047  -0.0028 460  CYS   B CA   
2565 C  C    . CYS   B 74  ? 0.4263 0.4202 0.4427 0.0604  0.0007  -0.0036 460  CYS   B C    
2566 O  O    . CYS   B 74  ? 0.4548 0.4314 0.4676 0.0615  -0.0020 -0.0043 460  CYS   B O    
2567 C  CB   . CYS   B 74  ? 0.4557 0.4523 0.4762 0.0434  0.0066  0.0017  460  CYS   B CB   
2568 S  SG   . CYS   B 74  ? 0.4847 0.4851 0.5085 0.0349  0.0102  0.0022  460  CYS   B SG   
2569 N  N    . ILE   B 75  ? 0.4274 0.4329 0.4444 0.0659  -0.0004 -0.0034 461  ILE   B N    
2570 C  CA   . ILE   B 75  ? 0.4632 0.4608 0.4764 0.0751  -0.0049 -0.0045 461  ILE   B CA   
2571 C  C    . ILE   B 75  ? 0.4542 0.4495 0.4655 0.0844  -0.0071 -0.0105 461  ILE   B C    
2572 O  O    . ILE   B 75  ? 0.4758 0.4539 0.4819 0.0901  -0.0115 -0.0122 461  ILE   B O    
2573 C  CB   . ILE   B 75  ? 0.5056 0.5178 0.5206 0.0789  -0.0056 -0.0027 461  ILE   B CB   
2574 C  CG1  . ILE   B 75  ? 0.4524 0.4637 0.4675 0.0702  -0.0043 0.0029  461  ILE   B CG1  
2575 C  CG2  . ILE   B 75  ? 0.4215 0.4267 0.4326 0.0903  -0.0108 -0.0045 461  ILE   B CG2  
2576 C  CD1  . ILE   B 75  ? 0.4866 0.4762 0.4963 0.0664  -0.0058 0.0061  461  ILE   B CD1  
2577 N  N    . ASP   B 76  ? 0.4308 0.4429 0.4453 0.0860  -0.0044 -0.0139 462  ASP   B N    
2578 C  CA   . ASP   B 76  ? 0.4823 0.4929 0.4942 0.0947  -0.0062 -0.0202 462  ASP   B CA   
2579 C  C    . ASP   B 76  ? 0.4769 0.4667 0.4850 0.0911  -0.0077 -0.0218 462  ASP   B C    
2580 O  O    . ASP   B 76  ? 0.4637 0.4421 0.4670 0.0987  -0.0116 -0.0267 462  ASP   B O    
2581 C  CB   . ASP   B 76  ? 0.4989 0.5335 0.5147 0.0960  -0.0024 -0.0226 462  ASP   B CB   
2582 C  CG   . ASP   B 76  ? 0.5303 0.5861 0.5493 0.1037  -0.0023 -0.0232 462  ASP   B CG   
2583 O  OD1  . ASP   B 76  ? 0.5148 0.5647 0.5323 0.1096  -0.0058 -0.0226 462  ASP   B OD1  
2584 O  OD2  . ASP   B 76  ? 0.5203 0.5990 0.5433 0.1036  0.0011  -0.0239 462  ASP   B OD2  
2585 N  N    . ILE   B 77  ? 0.4393 0.4242 0.4494 0.0798  -0.0052 -0.0180 463  ILE   B N    
2586 C  CA   . ILE   B 77  ? 0.4239 0.3904 0.4316 0.0754  -0.0069 -0.0188 463  ILE   B CA   
2587 C  C    . ILE   B 77  ? 0.4831 0.4283 0.4861 0.0766  -0.0114 -0.0171 463  ILE   B C    
2588 O  O    . ILE   B 77  ? 0.4923 0.4209 0.4910 0.0788  -0.0154 -0.0201 463  ILE   B O    
2589 C  CB   . ILE   B 77  ? 0.4683 0.4371 0.4801 0.0638  -0.0029 -0.0149 463  ILE   B CB   
2590 C  CG1  . ILE   B 77  ? 0.4504 0.4351 0.4651 0.0623  0.0004  -0.0168 463  ILE   B CG1  
2591 C  CG2  . ILE   B 77  ? 0.4755 0.4250 0.4857 0.0583  -0.0049 -0.0140 463  ILE   B CG2  
2592 C  CD1  . ILE   B 77  ? 0.5079 0.4873 0.5202 0.0644  -0.0012 -0.0216 463  ILE   B CD1  
2593 N  N    . LEU   B 78  ? 0.4807 0.4254 0.4840 0.0744  -0.0112 -0.0120 464  LEU   B N    
2594 C  CA   . LEU   B 78  ? 0.5013 0.4263 0.4993 0.0753  -0.0156 -0.0095 464  LEU   B CA   
2595 C  C    . LEU   B 78  ? 0.4958 0.4124 0.4884 0.0877  -0.0213 -0.0141 464  LEU   B C    
2596 O  O    . LEU   B 78  ? 0.4872 0.3824 0.4741 0.0889  -0.0263 -0.0147 464  LEU   B O    
2597 C  CB   . LEU   B 78  ? 0.4552 0.3839 0.4538 0.0717  -0.0143 -0.0034 464  LEU   B CB   
2598 C  CG   . LEU   B 78  ? 0.5434 0.4533 0.5356 0.0733  -0.0190 0.0002  464  LEU   B CG   
2599 C  CD1  . LEU   B 78  ? 0.5304 0.4204 0.5197 0.0660  -0.0206 0.0023  464  LEU   B CD1  
2600 C  CD2  . LEU   B 78  ? 0.5682 0.4847 0.5606 0.0702  -0.0174 0.0059  464  LEU   B CD2  
2601 N  N    . LYS   B 79  ? 0.4729 0.4062 0.4670 0.0969  -0.0209 -0.0175 465  LYS   B N    
2602 C  CA   . LYS   B 79  ? 0.5635 0.4905 0.5525 0.1104  -0.0262 -0.0231 465  LYS   B CA   
2603 C  C    . LYS   B 79  ? 0.5341 0.4477 0.5190 0.1125  -0.0288 -0.0289 465  LYS   B C    
2604 O  O    . LYS   B 79  ? 0.5523 0.4443 0.5302 0.1178  -0.0351 -0.0312 465  LYS   B O    
2605 C  CB   . LYS   B 79  ? 0.5306 0.4827 0.5235 0.1196  -0.0242 -0.0263 465  LYS   B CB   
2606 C  CG   . LYS   B 79  ? 0.5869 0.5484 0.5819 0.1211  -0.0243 -0.0217 465  LYS   B CG   
2607 C  CD   . LYS   B 79  ? 0.5986 0.5910 0.6009 0.1232  -0.0200 -0.0223 465  LYS   B CD   
2608 C  CE   . LYS   B 79  ? 0.6712 0.6768 0.6737 0.1365  -0.0209 -0.0295 465  LYS   B CE   
2609 N  NZ   . LYS   B 79  ? 0.7004 0.7381 0.7106 0.1366  -0.0163 -0.0290 465  LYS   B NZ   
2610 N  N    . LYS   B 80  ? 0.5332 0.4580 0.5217 0.1079  -0.0247 -0.0312 466  LYS   B N    
2611 C  CA   . LYS   B 80  ? 0.5467 0.4605 0.5312 0.1098  -0.0273 -0.0371 466  LYS   B CA   
2612 C  C    . LYS   B 80  ? 0.5861 0.4737 0.5669 0.1022  -0.0314 -0.0346 466  LYS   B C    
2613 O  O    . LYS   B 80  ? 0.5223 0.3907 0.4963 0.1072  -0.0375 -0.0389 466  LYS   B O    
2614 C  CB   . LYS   B 80  ? 0.5478 0.4793 0.5370 0.1047  -0.0219 -0.0385 466  LYS   B CB   
2615 C  CG   . LYS   B 80  ? 0.5291 0.4841 0.5199 0.1135  -0.0191 -0.0429 466  LYS   B CG   
2616 C  CD   . LYS   B 80  ? 0.6158 0.5872 0.6106 0.1069  -0.0139 -0.0428 466  LYS   B CD   
2617 C  CE   . LYS   B 80  ? 0.7591 0.7505 0.7531 0.1163  -0.0121 -0.0485 466  LYS   B CE   
2618 N  NZ   . LYS   B 80  ? 0.7823 0.7611 0.7684 0.1265  -0.0169 -0.0568 466  LYS   B NZ   
2619 N  N    . LEU   B 81  ? 0.5348 0.4217 0.5199 0.0899  -0.0282 -0.0276 467  LEU   B N    
2620 C  CA   . LEU   B 81  ? 0.5496 0.4147 0.5321 0.0815  -0.0315 -0.0241 467  LEU   B CA   
2621 C  C    . LEU   B 81  ? 0.5867 0.4310 0.5618 0.0866  -0.0380 -0.0228 467  LEU   B C    
2622 O  O    . LEU   B 81  ? 0.5937 0.4160 0.5633 0.0855  -0.0437 -0.0239 467  LEU   B O    
2623 C  CB   . LEU   B 81  ? 0.5587 0.4305 0.5473 0.0691  -0.0262 -0.0168 467  LEU   B CB   
2624 C  CG   . LEU   B 81  ? 0.5191 0.4066 0.5143 0.0628  -0.0208 -0.0175 467  LEU   B CG   
2625 C  CD1  . LEU   B 81  ? 0.4997 0.3929 0.5000 0.0522  -0.0160 -0.0107 467  LEU   B CD1  
2626 C  CD2  . LEU   B 81  ? 0.5161 0.3932 0.5099 0.0604  -0.0237 -0.0214 467  LEU   B CD2  
2627 N  N    . SER   B 82  ? 0.5491 0.3996 0.5238 0.0920  -0.0377 -0.0201 468  SER   B N    
2628 C  CA   . SER   B 82  ? 0.6018 0.4326 0.5689 0.0978  -0.0444 -0.0186 468  SER   B CA   
2629 C  C    . SER   B 82  ? 0.6142 0.4303 0.5740 0.1094  -0.0513 -0.0264 468  SER   B C    
2630 O  O    . SER   B 82  ? 0.6443 0.4343 0.5967 0.1092  -0.0582 -0.0259 468  SER   B O    
2631 C  CB   . SER   B 82  ? 0.5678 0.4116 0.5362 0.1036  -0.0431 -0.0156 468  SER   B CB   
2632 O  OG   . SER   B 82  ? 0.6399 0.4649 0.6004 0.1108  -0.0501 -0.0144 468  SER   B OG   
2633 N  N    . ARG   B 83  ? 0.6079 0.4403 0.5693 0.1193  -0.0497 -0.0338 469  ARG   B N    
2634 C  CA   . ARG   B 83  ? 0.6661 0.4866 0.6202 0.1316  -0.0558 -0.0425 469  ARG   B CA   
2635 C  C    . ARG   B 83  ? 0.6881 0.4906 0.6385 0.1253  -0.0590 -0.0455 469  ARG   B C    
2636 O  O    . ARG   B 83  ? 0.7002 0.4777 0.6418 0.1301  -0.0669 -0.0490 469  ARG   B O    
2637 C  CB   . ARG   B 83  ? 0.7333 0.5798 0.6907 0.1427  -0.0520 -0.0492 469  ARG   B CB   
2638 C  CG   . ARG   B 83  ? 0.7630 0.6064 0.7155 0.1505  -0.0544 -0.0590 469  ARG   B CG   
2639 C  CD   . ARG   B 83  ? 0.8346 0.7021 0.7884 0.1648  -0.0519 -0.0657 469  ARG   B CD   
2640 N  NE   . ARG   B 83  ? 1.0346 0.8958 0.9836 0.1791  -0.0573 -0.0681 469  ARG   B NE   
2641 C  CZ   . ARG   B 83  ? 1.0463 0.9311 0.9998 0.1886  -0.0545 -0.0689 469  ARG   B CZ   
2642 N  NH1  . ARG   B 83  ? 1.0391 0.9554 1.0016 0.1849  -0.0465 -0.0673 469  ARG   B NH1  
2643 N  NH2  . ARG   B 83  ? 0.9922 0.8687 0.9409 0.2019  -0.0604 -0.0710 469  ARG   B NH2  
2644 N  N    . THR   B 84  ? 0.6405 0.4546 0.5974 0.1145  -0.0535 -0.0440 470  THR   B N    
2645 C  CA   . THR   B 84  ? 0.6145 0.4165 0.5689 0.1095  -0.0562 -0.0479 470  THR   B CA   
2646 C  C    . THR   B 84  ? 0.6619 0.4405 0.6145 0.0974  -0.0602 -0.0420 470  THR   B C    
2647 O  O    . THR   B 84  ? 0.7344 0.4897 0.6797 0.0979  -0.0676 -0.0454 470  THR   B O    
2648 C  CB   . THR   B 84  ? 0.6403 0.4652 0.6022 0.1039  -0.0491 -0.0488 470  THR   B CB   
2649 O  OG1  . THR   B 84  ? 0.6662 0.5119 0.6287 0.1151  -0.0460 -0.0545 470  THR   B OG1  
2650 C  CG2  . THR   B 84  ? 0.6559 0.4697 0.6160 0.0977  -0.0520 -0.0522 470  THR   B CG2  
2651 N  N    . VAL   B 85  ? 0.6272 0.4117 0.5859 0.0863  -0.0557 -0.0332 471  VAL   B N    
2652 C  CA   . VAL   B 85  ? 0.6876 0.4532 0.6451 0.0742  -0.0586 -0.0266 471  VAL   B CA   
2653 C  C    . VAL   B 85  ? 0.7289 0.4715 0.6779 0.0778  -0.0655 -0.0235 471  VAL   B C    
2654 O  O    . VAL   B 85  ? 0.8135 0.5354 0.7589 0.0689  -0.0700 -0.0189 471  VAL   B O    
2655 C  CB   . VAL   B 85  ? 0.6489 0.4310 0.6156 0.0621  -0.0508 -0.0188 471  VAL   B CB   
2656 C  CG1  . VAL   B 85  ? 0.7123 0.4797 0.6794 0.0484  -0.0526 -0.0121 471  VAL   B CG1  
2657 C  CG2  . VAL   B 85  ? 0.6339 0.4379 0.6081 0.0603  -0.0447 -0.0222 471  VAL   B CG2  
2658 N  N    . LYS   B 86  ? 0.6941 0.4403 0.6397 0.0906  -0.0666 -0.0257 472  LYS   B N    
2659 C  CA   . LYS   B 86  ? 0.7702 0.4945 0.7066 0.0972  -0.0741 -0.0239 472  LYS   B CA   
2660 C  C    . LYS   B 86  ? 0.7873 0.5071 0.7241 0.0874  -0.0728 -0.0129 472  LYS   B C    
2661 O  O    . LYS   B 86  ? 0.7744 0.4712 0.7059 0.0793  -0.0778 -0.0078 472  LYS   B O    
2662 C  CB   . LYS   B 86  ? 0.7913 0.4852 0.7180 0.0988  -0.0838 -0.0283 472  LYS   B CB   
2663 C  CG   . LYS   B 86  ? 0.8655 0.5613 0.7890 0.1114  -0.0864 -0.0401 472  LYS   B CG   
2664 C  CD   . LYS   B 86  ? 0.9582 0.6205 0.8698 0.1152  -0.0975 -0.0448 472  LYS   B CD   
2665 C  CE   . LYS   B 86  ? 1.0721 0.7340 0.9773 0.1336  -0.1013 -0.0568 472  LYS   B CE   
2666 N  NZ   . LYS   B 86  ? 1.0227 0.7200 0.9362 0.1407  -0.0923 -0.0608 472  LYS   B NZ   
2667 N  N    . PHE   B 87  ? 0.6981 0.4400 0.6409 0.0878  -0.0662 -0.0092 473  PHE   B N    
2668 C  CA   . PHE   B 87  ? 0.6814 0.4207 0.6233 0.0809  -0.0650 0.0004  473  PHE   B CA   
2669 C  C    . PHE   B 87  ? 0.7059 0.4611 0.6488 0.0909  -0.0631 0.0006  473  PHE   B C    
2670 O  O    . PHE   B 87  ? 0.6909 0.4645 0.6379 0.1004  -0.0606 -0.0058 473  PHE   B O    
2671 C  CB   . PHE   B 87  ? 0.6932 0.4443 0.6426 0.0653  -0.0576 0.0067  473  PHE   B CB   
2672 C  CG   . PHE   B 87  ? 0.6066 0.3868 0.5659 0.0648  -0.0491 0.0041  473  PHE   B CG   
2673 C  CD1  . PHE   B 87  ? 0.5923 0.3911 0.5549 0.0677  -0.0445 0.0064  473  PHE   B CD1  
2674 C  CD2  . PHE   B 87  ? 0.6250 0.4132 0.5899 0.0609  -0.0462 -0.0003 473  PHE   B CD2  
2675 C  CE1  . PHE   B 87  ? 0.5899 0.4137 0.5610 0.0662  -0.0372 0.0043  473  PHE   B CE1  
2676 C  CE2  . PHE   B 87  ? 0.5882 0.4011 0.5613 0.0601  -0.0390 -0.0022 473  PHE   B CE2  
2677 C  CZ   . PHE   B 87  ? 0.5429 0.3729 0.5189 0.0626  -0.0346 0.0002  473  PHE   B CZ   
2678 N  N    . THR   B 88  ? 0.7311 0.4795 0.6702 0.0883  -0.0645 0.0084  474  THR   B N    
2679 C  CA   . THR   B 88  ? 0.6521 0.4165 0.5926 0.0948  -0.0624 0.0104  474  THR   B CA   
2680 C  C    . THR   B 88  ? 0.6693 0.4467 0.6144 0.0825  -0.0555 0.0181  474  THR   B C    
2681 O  O    . THR   B 88  ? 0.6535 0.4245 0.5993 0.0698  -0.0533 0.0227  474  THR   B O    
2682 C  CB   . THR   B 88  ? 0.7093 0.4546 0.6399 0.1044  -0.0709 0.0124  474  THR   B CB   
2683 O  OG1  . THR   B 88  ? 0.7476 0.4692 0.6709 0.0945  -0.0747 0.0207  474  THR   B OG1  
2684 C  CG2  . THR   B 88  ? 0.7167 0.4498 0.6426 0.1184  -0.0778 0.0035  474  THR   B CG2  
2685 N  N    . TYR   B 89  ? 0.6242 0.4207 0.5724 0.0863  -0.0523 0.0193  475  TYR   B N    
2686 C  CA   . TYR   B 89  ? 0.6206 0.4321 0.5736 0.0756  -0.0452 0.0248  475  TYR   B CA   
2687 C  C    . TYR   B 89  ? 0.6625 0.4853 0.6145 0.0800  -0.0451 0.0281  475  TYR   B C    
2688 O  O    . TYR   B 89  ? 0.6253 0.4525 0.5763 0.0921  -0.0488 0.0247  475  TYR   B O    
2689 C  CB   . TYR   B 89  ? 0.5859 0.4181 0.5487 0.0715  -0.0380 0.0202  475  TYR   B CB   
2690 C  CG   . TYR   B 89  ? 0.5681 0.4190 0.5359 0.0820  -0.0370 0.0132  475  TYR   B CG   
2691 C  CD1  . TYR   B 89  ? 0.5675 0.4384 0.5389 0.0848  -0.0342 0.0141  475  TYR   B CD1  
2692 C  CD2  . TYR   B 89  ? 0.5850 0.4347 0.5537 0.0885  -0.0387 0.0058  475  TYR   B CD2  
2693 C  CE1  . TYR   B 89  ? 0.5724 0.4622 0.5488 0.0931  -0.0331 0.0085  475  TYR   B CE1  
2694 C  CE2  . TYR   B 89  ? 0.5462 0.4151 0.5194 0.0977  -0.0372 -0.0001 475  TYR   B CE2  
2695 C  CZ   . TYR   B 89  ? 0.6191 0.5087 0.5965 0.0997  -0.0343 0.0015  475  TYR   B CZ   
2696 O  OH   . TYR   B 89  ? 0.5615 0.4725 0.5439 0.1078  -0.0325 -0.0037 475  TYR   B OH   
2697 N  N    . ASP   B 90  ? 0.6311 0.4592 0.5831 0.0703  -0.0409 0.0346  476  ASP   B N    
2698 C  CA   . ASP   B 90  ? 0.6395 0.4815 0.5913 0.0718  -0.0395 0.0377  476  ASP   B CA   
2699 C  C    . ASP   B 90  ? 0.5942 0.4566 0.5536 0.0637  -0.0314 0.0371  476  ASP   B C    
2700 O  O    . ASP   B 90  ? 0.5649 0.4250 0.5241 0.0530  -0.0274 0.0410  476  ASP   B O    
2701 C  CB   . ASP   B 90  ? 0.6989 0.5264 0.6413 0.0681  -0.0426 0.0461  476  ASP   B CB   
2702 C  CG   . ASP   B 90  ? 0.8758 0.6839 0.8097 0.0781  -0.0517 0.0470  476  ASP   B CG   
2703 O  OD1  . ASP   B 90  ? 0.9335 0.7225 0.8583 0.0740  -0.0555 0.0541  476  ASP   B OD1  
2704 O  OD2  . ASP   B 90  ? 0.8722 0.6844 0.8083 0.0903  -0.0551 0.0407  476  ASP   B OD2  
2705 N  N    . LEU   B 91  ? 0.5456 0.4279 0.5117 0.0689  -0.0293 0.0321  477  LEU   B N    
2706 C  CA   . LEU   B 91  ? 0.5142 0.4149 0.4875 0.0622  -0.0225 0.0306  477  LEU   B CA   
2707 C  C    . LEU   B 91  ? 0.5291 0.4400 0.5010 0.0586  -0.0207 0.0348  477  LEU   B C    
2708 O  O    . LEU   B 91  ? 0.5090 0.4235 0.4783 0.0649  -0.0243 0.0360  477  LEU   B O    
2709 C  CB   . LEU   B 91  ? 0.5035 0.4205 0.4839 0.0688  -0.0215 0.0239  477  LEU   B CB   
2710 C  CG   . LEU   B 91  ? 0.5410 0.4752 0.5287 0.0622  -0.0153 0.0220  477  LEU   B CG   
2711 C  CD1  . LEU   B 91  ? 0.4581 0.3845 0.4474 0.0540  -0.0119 0.0217  477  LEU   B CD1  
2712 C  CD2  . LEU   B 91  ? 0.5218 0.4727 0.5152 0.0694  -0.0152 0.0165  477  LEU   B CD2  
2713 N  N    . TYR   B 92  ? 0.5001 0.4159 0.4737 0.0489  -0.0153 0.0366  478  TYR   B N    
2714 C  CA   . TYR   B 92  ? 0.5052 0.4302 0.4766 0.0452  -0.0135 0.0398  478  TYR   B CA   
2715 C  C    . TYR   B 92  ? 0.4654 0.4034 0.4424 0.0384  -0.0076 0.0376  478  TYR   B C    
2716 O  O    . TYR   B 92  ? 0.4565 0.3930 0.4376 0.0344  -0.0044 0.0354  478  TYR   B O    
2717 C  CB   . TYR   B 92  ? 0.4485 0.3601 0.4109 0.0405  -0.0143 0.0465  478  TYR   B CB   
2718 C  CG   . TYR   B 92  ? 0.4762 0.3814 0.4383 0.0309  -0.0097 0.0488  478  TYR   B CG   
2719 C  CD1  . TYR   B 92  ? 0.5098 0.4010 0.4719 0.0291  -0.0107 0.0493  478  TYR   B CD1  
2720 C  CD2  . TYR   B 92  ? 0.4896 0.4029 0.4511 0.0239  -0.0046 0.0502  478  TYR   B CD2  
2721 C  CE1  . TYR   B 92  ? 0.4676 0.3550 0.4303 0.0202  -0.0065 0.0516  478  TYR   B CE1  
2722 C  CE2  . TYR   B 92  ? 0.4478 0.3574 0.4096 0.0158  -0.0001 0.0520  478  TYR   B CE2  
2723 C  CZ   . TYR   B 92  ? 0.5206 0.4182 0.4836 0.0138  -0.0010 0.0529  478  TYR   B CZ   
2724 O  OH   . TYR   B 92  ? 0.5467 0.4427 0.5110 0.0057  0.0034  0.0550  478  TYR   B OH   
2725 N  N    . LEU   B 93  ? 0.4417 0.3916 0.4183 0.0369  -0.0067 0.0381  479  LEU   B N    
2726 C  CA   . LEU   B 93  ? 0.4605 0.4220 0.4414 0.0310  -0.0022 0.0359  479  LEU   B CA   
2727 C  C    . LEU   B 93  ? 0.4238 0.3803 0.3995 0.0236  0.0011  0.0390  479  LEU   B C    
2728 O  O    . LEU   B 93  ? 0.4133 0.3657 0.3817 0.0233  -0.0004 0.0430  479  LEU   B O    
2729 C  CB   . LEU   B 93  ? 0.4268 0.4041 0.4099 0.0332  -0.0038 0.0345  479  LEU   B CB   
2730 C  CG   . LEU   B 93  ? 0.5173 0.5072 0.5076 0.0386  -0.0052 0.0306  479  LEU   B CG   
2731 C  CD1  . LEU   B 93  ? 0.4744 0.4692 0.4708 0.0346  -0.0012 0.0272  479  LEU   B CD1  
2732 C  CD2  . LEU   B 93  ? 0.5955 0.5794 0.5856 0.0475  -0.0090 0.0298  479  LEU   B CD2  
2733 N  N    . VAL   B 94  ? 0.3931 0.3505 0.3723 0.0182  0.0057  0.0372  480  VAL   B N    
2734 C  CA   . VAL   B 94  ? 0.4523 0.4067 0.4271 0.0120  0.0094  0.0395  480  VAL   B CA   
2735 C  C    . VAL   B 94  ? 0.4539 0.4159 0.4242 0.0107  0.0093  0.0397  480  VAL   B C    
2736 O  O    . VAL   B 94  ? 0.4436 0.4154 0.4172 0.0118  0.0081  0.0368  480  VAL   B O    
2737 C  CB   . VAL   B 94  ? 0.3943 0.3496 0.3745 0.0077  0.0139  0.0368  480  VAL   B CB   
2738 C  CG1  . VAL   B 94  ? 0.3914 0.3572 0.3770 0.0076  0.0147  0.0323  480  VAL   B CG1  
2739 C  CG2  . VAL   B 94  ? 0.4202 0.3733 0.3962 0.0023  0.0180  0.0390  480  VAL   B CG2  
2740 N  N    . THR   B 95  ? 0.4433 0.4012 0.4057 0.0079  0.0103  0.0433  481  THR   B N    
2741 C  CA   . THR   B 95  ? 0.4644 0.4285 0.4210 0.0062  0.0103  0.0431  481  THR   B CA   
2742 C  C    . THR   B 95  ? 0.5316 0.4955 0.4847 0.0010  0.0154  0.0425  481  THR   B C    
2743 O  O    . THR   B 95  ? 0.4990 0.4674 0.4470 -0.0005 0.0156  0.0411  481  THR   B O    
2744 C  CB   . THR   B 95  ? 0.4854 0.4468 0.4338 0.0087  0.0063  0.0476  481  THR   B CB   
2745 O  OG1  . THR   B 95  ? 0.5285 0.4789 0.4721 0.0076  0.0070  0.0525  481  THR   B OG1  
2746 C  CG2  . THR   B 95  ? 0.4823 0.4476 0.4345 0.0151  0.0008  0.0470  481  THR   B CG2  
2747 N  N    . ASN   B 96  ? 0.4345 0.3938 0.3899 -0.0015 0.0192  0.0433  482  ASN   B N    
2748 C  CA   . ASN   B 96  ? 0.4801 0.4409 0.4332 -0.0055 0.0244  0.0425  482  ASN   B CA   
2749 C  C    . ASN   B 96  ? 0.4793 0.4437 0.4409 -0.0062 0.0268  0.0374  482  ASN   B C    
2750 O  O    . ASN   B 96  ? 0.4894 0.4518 0.4568 -0.0073 0.0290  0.0373  482  ASN   B O    
2751 C  CB   . ASN   B 96  ? 0.4675 0.4225 0.4180 -0.0084 0.0270  0.0475  482  ASN   B CB   
2752 C  CG   . ASN   B 96  ? 0.5237 0.4829 0.4733 -0.0120 0.0330  0.0465  482  ASN   B CG   
2753 O  OD1  . ASN   B 96  ? 0.5432 0.5073 0.4875 -0.0122 0.0348  0.0441  482  ASN   B OD1  
2754 N  ND2  . ASN   B 96  ? 0.5077 0.4655 0.4628 -0.0148 0.0360  0.0479  482  ASN   B ND2  
2755 N  N    . GLY   B 97  ? 0.4359 0.4053 0.3977 -0.0058 0.0258  0.0333  483  GLY   B N    
2756 C  CA   . GLY   B 97  ? 0.4719 0.4437 0.4408 -0.0063 0.0272  0.0289  483  GLY   B CA   
2757 C  C    . GLY   B 97  ? 0.4579 0.4310 0.4342 -0.0042 0.0242  0.0280  483  GLY   B C    
2758 O  O    . GLY   B 97  ? 0.4818 0.4558 0.4577 -0.0017 0.0206  0.0297  483  GLY   B O    
2759 N  N    . LYS   B 98  ? 0.4268 0.4006 0.4099 -0.0048 0.0257  0.0252  484  LYS   B N    
2760 C  CA   . LYS   B 98  ? 0.4009 0.3776 0.3905 -0.0031 0.0234  0.0238  484  LYS   B CA   
2761 C  C    . LYS   B 98  ? 0.4194 0.3928 0.4150 -0.0024 0.0247  0.0237  484  LYS   B C    
2762 O  O    . LYS   B 98  ? 0.3930 0.3616 0.3881 -0.0013 0.0242  0.0262  484  LYS   B O    
2763 C  CB   . LYS   B 98  ? 0.4445 0.4255 0.4355 -0.0048 0.0227  0.0206  484  LYS   B CB   
2764 C  CG   . LYS   B 98  ? 0.5165 0.5012 0.5021 -0.0059 0.0201  0.0205  484  LYS   B CG   
2765 C  CD   . LYS   B 98  ? 0.5537 0.5404 0.5399 -0.0089 0.0191  0.0176  484  LYS   B CD   
2766 C  CE   . LYS   B 98  ? 0.5999 0.5924 0.5930 -0.0090 0.0173  0.0173  484  LYS   B CE   
2767 N  NZ   . LYS   B 98  ? 0.5811 0.5746 0.5737 -0.0131 0.0157  0.0155  484  LYS   B NZ   
2768 N  N    . HIS   B 99  ? 0.3959 0.3710 0.3968 -0.0033 0.0257  0.0209  485  HIS   B N    
2769 C  CA   . HIS   B 99  ? 0.4000 0.3725 0.4066 -0.0027 0.0263  0.0204  485  HIS   B CA   
2770 C  C    . HIS   B 99  ? 0.4036 0.3722 0.4102 -0.0048 0.0294  0.0219  485  HIS   B C    
2771 O  O    . HIS   B 99  ? 0.3977 0.3618 0.4056 -0.0049 0.0289  0.0238  485  HIS   B O    
2772 C  CB   . HIS   B 99  ? 0.3927 0.3683 0.4040 -0.0031 0.0264  0.0174  485  HIS   B CB   
2773 C  CG   . HIS   B 99  ? 0.3693 0.3507 0.3810 -0.0022 0.0238  0.0166  485  HIS   B CG   
2774 N  ND1  . HIS   B 99  ? 0.3987 0.3833 0.4069 -0.0040 0.0230  0.0163  485  HIS   B ND1  
2775 C  CD2  . HIS   B 99  ? 0.3986 0.3840 0.4135 0.0000  0.0220  0.0159  485  HIS   B CD2  
2776 C  CE1  . HIS   B 99  ? 0.4071 0.3983 0.4171 -0.0036 0.0207  0.0161  485  HIS   B CE1  
2777 N  NE2  . HIS   B 99  ? 0.4032 0.3956 0.4172 -0.0009 0.0204  0.0158  485  HIS   B NE2  
2778 N  N    . GLY   B 100 ? 0.3838 0.3541 0.3886 -0.0067 0.0322  0.0210  486  GLY   B N    
2779 C  CA   . GLY   B 100 ? 0.3596 0.3293 0.3646 -0.0087 0.0357  0.0225  486  GLY   B CA   
2780 C  C    . GLY   B 100 ? 0.4048 0.3782 0.4100 -0.0092 0.0389  0.0197  486  GLY   B C    
2781 O  O    . GLY   B 100 ? 0.3789 0.3534 0.3881 -0.0083 0.0385  0.0165  486  GLY   B O    
2782 N  N    . LYS   B 101 ? 0.3655 0.3406 0.3658 -0.0102 0.0419  0.0208  487  LYS   B N    
2783 C  CA   . LYS   B 101 ? 0.3786 0.3576 0.3789 -0.0095 0.0452  0.0178  487  LYS   B CA   
2784 C  C    . LYS   B 101 ? 0.4226 0.4057 0.4212 -0.0113 0.0496  0.0204  487  LYS   B C    
2785 O  O    . LYS   B 101 ? 0.3972 0.3791 0.3897 -0.0129 0.0497  0.0242  487  LYS   B O    
2786 C  CB   . LYS   B 101 ? 0.3884 0.3664 0.3818 -0.0079 0.0441  0.0145  487  LYS   B CB   
2787 C  CG   . LYS   B 101 ? 0.4110 0.3914 0.4037 -0.0059 0.0469  0.0103  487  LYS   B CG   
2788 C  CD   . LYS   B 101 ? 0.4027 0.3801 0.3864 -0.0046 0.0453  0.0072  487  LYS   B CD   
2789 C  CE   . LYS   B 101 ? 0.4208 0.3992 0.4028 -0.0014 0.0477  0.0022  487  LYS   B CE   
2790 N  NZ   . LYS   B 101 ? 0.4343 0.4075 0.4065 -0.0003 0.0452  -0.0015 487  LYS   B NZ   
2791 N  N    . LYS   B 102 ? 0.4185 0.4073 0.4223 -0.0111 0.0529  0.0188  488  LYS   B N    
2792 C  CA   . LYS   B 102 ? 0.4206 0.4165 0.4234 -0.0129 0.0578  0.0211  488  LYS   B CA   
2793 C  C    . LYS   B 102 ? 0.4126 0.4118 0.4071 -0.0101 0.0604  0.0180  488  LYS   B C    
2794 O  O    . LYS   B 102 ? 0.3995 0.3996 0.3946 -0.0063 0.0606  0.0126  488  LYS   B O    
2795 C  CB   . LYS   B 102 ? 0.4352 0.4382 0.4481 -0.0136 0.0603  0.0205  488  LYS   B CB   
2796 C  CG   . LYS   B 102 ? 0.4633 0.4744 0.4775 -0.0178 0.0647  0.0251  488  LYS   B CG   
2797 C  CD   . LYS   B 102 ? 0.4465 0.4660 0.4722 -0.0194 0.0666  0.0250  488  LYS   B CD   
2798 C  CE   . LYS   B 102 ? 0.5135 0.5419 0.5424 -0.0141 0.0694  0.0192  488  LYS   B CE   
2799 N  NZ   . LYS   B 102 ? 0.6860 0.7257 0.7263 -0.0154 0.0717  0.0195  488  LYS   B NZ   
2800 N  N    . VAL   B 103 ? 0.4425 0.4427 0.4286 -0.0119 0.0621  0.0213  489  VAL   B N    
2801 C  CA   . VAL   B 103 ? 0.4653 0.4681 0.4416 -0.0093 0.0643  0.0184  489  VAL   B CA   
2802 C  C    . VAL   B 103 ? 0.4691 0.4818 0.4432 -0.0114 0.0702  0.0216  489  VAL   B C    
2803 O  O    . VAL   B 103 ? 0.4462 0.4587 0.4182 -0.0159 0.0707  0.0282  489  VAL   B O    
2804 C  CB   . VAL   B 103 ? 0.4499 0.4454 0.4163 -0.0094 0.0603  0.0192  489  VAL   B CB   
2805 C  CG1  . VAL   B 103 ? 0.4888 0.4865 0.4442 -0.0068 0.0622  0.0156  489  VAL   B CG1  
2806 C  CG2  . VAL   B 103 ? 0.4548 0.4429 0.4243 -0.0083 0.0548  0.0169  489  VAL   B CG2  
2807 N  N    . ASN   B 104 ? 0.4901 0.5116 0.4645 -0.0079 0.0746  0.0172  490  ASN   B N    
2808 C  CA   . ASN   B 104 ? 0.4768 0.5113 0.4503 -0.0096 0.0811  0.0200  490  ASN   B CA   
2809 C  C    . ASN   B 104 ? 0.4668 0.5051 0.4493 -0.0160 0.0822  0.0269  490  ASN   B C    
2810 O  O    . ASN   B 104 ? 0.4592 0.5024 0.4382 -0.0210 0.0852  0.0331  490  ASN   B O    
2811 C  CB   . ASN   B 104 ? 0.4740 0.5089 0.4335 -0.0103 0.0827  0.0221  490  ASN   B CB   
2812 C  CG   . ASN   B 104 ? 0.5392 0.5713 0.4890 -0.0042 0.0818  0.0147  490  ASN   B CG   
2813 O  OD1  . ASN   B 104 ? 0.5480 0.5849 0.4998 0.0012  0.0840  0.0081  490  ASN   B OD1  
2814 N  ND2  . ASN   B 104 ? 0.5207 0.5444 0.4600 -0.0047 0.0781  0.0154  490  ASN   B ND2  
2815 N  N    . ASN   B 105 ? 0.4565 0.4914 0.4499 -0.0163 0.0792  0.0260  491  ASN   B N    
2816 C  CA   . ASN   B 105 ? 0.4527 0.4902 0.4558 -0.0221 0.0792  0.0312  491  ASN   B CA   
2817 C  C    . ASN   B 105 ? 0.4681 0.4945 0.4675 -0.0274 0.0754  0.0378  491  ASN   B C    
2818 O  O    . ASN   B 105 ? 0.5312 0.5587 0.5352 -0.0334 0.0757  0.0434  491  ASN   B O    
2819 C  CB   . ASN   B 105 ? 0.4903 0.5444 0.4979 -0.0250 0.0857  0.0337  491  ASN   B CB   
2820 C  CG   . ASN   B 105 ? 0.5575 0.6165 0.5786 -0.0290 0.0852  0.0357  491  ASN   B CG   
2821 O  OD1  . ASN   B 105 ? 0.5380 0.5907 0.5659 -0.0269 0.0811  0.0325  491  ASN   B OD1  
2822 N  ND2  . ASN   B 105 ? 0.5168 0.5874 0.5417 -0.0353 0.0893  0.0413  491  ASN   B ND2  
2823 N  N    . VAL   B 106 ? 0.4195 0.4349 0.4108 -0.0252 0.0713  0.0371  492  VAL   B N    
2824 C  CA   . VAL   B 106 ? 0.4818 0.4861 0.4689 -0.0284 0.0669  0.0426  492  VAL   B CA   
2825 C  C    . VAL   B 106 ? 0.4566 0.4510 0.4454 -0.0247 0.0611  0.0390  492  VAL   B C    
2826 O  O    . VAL   B 106 ? 0.4022 0.3957 0.3871 -0.0204 0.0600  0.0343  492  VAL   B O    
2827 C  CB   . VAL   B 106 ? 0.4761 0.4791 0.4503 -0.0293 0.0677  0.0463  492  VAL   B CB   
2828 C  CG1  . VAL   B 106 ? 0.4930 0.4834 0.4628 -0.0314 0.0623  0.0517  492  VAL   B CG1  
2829 C  CG2  . VAL   B 106 ? 0.5223 0.5371 0.4938 -0.0332 0.0742  0.0502  492  VAL   B CG2  
2830 N  N    . TRP   B 107 ? 0.4365 0.4236 0.4306 -0.0265 0.0573  0.0412  493  TRP   B N    
2831 C  CA   . TRP   B 107 ? 0.4309 0.4107 0.4272 -0.0229 0.0522  0.0379  493  TRP   B CA   
2832 C  C    . TRP   B 107 ? 0.4444 0.4170 0.4321 -0.0212 0.0485  0.0397  493  TRP   B C    
2833 O  O    . TRP   B 107 ? 0.4784 0.4461 0.4610 -0.0236 0.0473  0.0452  493  TRP   B O    
2834 C  CB   . TRP   B 107 ? 0.4411 0.4162 0.4453 -0.0247 0.0494  0.0389  493  TRP   B CB   
2835 C  CG   . TRP   B 107 ? 0.4455 0.4273 0.4592 -0.0245 0.0513  0.0352  493  TRP   B CG   
2836 C  CD1  . TRP   B 107 ? 0.4412 0.4303 0.4611 -0.0282 0.0546  0.0367  493  TRP   B CD1  
2837 C  CD2  . TRP   B 107 ? 0.3906 0.3730 0.4086 -0.0204 0.0497  0.0296  493  TRP   B CD2  
2838 N  NE1  . TRP   B 107 ? 0.4460 0.4404 0.4741 -0.0259 0.0549  0.0320  493  TRP   B NE1  
2839 C  CE2  . TRP   B 107 ? 0.4366 0.4261 0.4631 -0.0212 0.0519  0.0278  493  TRP   B CE2  
2840 C  CE3  . TRP   B 107 ? 0.4125 0.3910 0.4280 -0.0165 0.0466  0.0264  493  TRP   B CE3  
2841 C  CZ2  . TRP   B 107 ? 0.4373 0.4283 0.4689 -0.0178 0.0507  0.0230  493  TRP   B CZ2  
2842 C  CZ3  . TRP   B 107 ? 0.4053 0.3855 0.4259 -0.0140 0.0456  0.0220  493  TRP   B CZ3  
2843 C  CH2  . TRP   B 107 ? 0.4461 0.4317 0.4743 -0.0145 0.0475  0.0204  493  TRP   B CH2  
2844 N  N    . ASN   B 108 ? 0.4214 0.3935 0.4075 -0.0173 0.0462  0.0355  494  ASN   B N    
2845 C  CA   . ASN   B 108 ? 0.4316 0.3988 0.4114 -0.0153 0.0420  0.0368  494  ASN   B CA   
2846 C  C    . ASN   B 108 ? 0.3835 0.3470 0.3689 -0.0127 0.0376  0.0348  494  ASN   B C    
2847 O  O    . ASN   B 108 ? 0.4103 0.3737 0.4034 -0.0129 0.0377  0.0330  494  ASN   B O    
2848 C  CB   . ASN   B 108 ? 0.4050 0.3756 0.3775 -0.0136 0.0424  0.0341  494  ASN   B CB   
2849 C  CG   . ASN   B 108 ? 0.4619 0.4351 0.4383 -0.0115 0.0419  0.0279  494  ASN   B CG   
2850 O  OD1  . ASN   B 108 ? 0.4077 0.3799 0.3912 -0.0105 0.0399  0.0261  494  ASN   B OD1  
2851 N  ND2  . ASN   B 108 ? 0.4494 0.4252 0.4199 -0.0107 0.0432  0.0249  494  ASN   B ND2  
2852 N  N    . GLY   B 109 ? 0.4450 0.4065 0.4264 -0.0101 0.0337  0.0351  495  GLY   B N    
2853 C  CA   . GLY   B 109 ? 0.4197 0.3807 0.4063 -0.0071 0.0301  0.0327  495  GLY   B CA   
2854 C  C    . GLY   B 109 ? 0.4001 0.3543 0.3896 -0.0064 0.0278  0.0349  495  GLY   B C    
2855 O  O    . GLY   B 109 ? 0.4285 0.3769 0.4148 -0.0083 0.0278  0.0392  495  GLY   B O    
2856 N  N    . MET   B 110 ? 0.4096 0.3643 0.4047 -0.0036 0.0255  0.0319  496  MET   B N    
2857 C  CA   . MET   B 110 ? 0.4306 0.3781 0.4281 -0.0021 0.0228  0.0328  496  MET   B CA   
2858 C  C    . MET   B 110 ? 0.4094 0.3531 0.4100 -0.0066 0.0250  0.0342  496  MET   B C    
2859 O  O    . MET   B 110 ? 0.4187 0.3537 0.4181 -0.0076 0.0229  0.0371  496  MET   B O    
2860 C  CB   . MET   B 110 ? 0.4003 0.3506 0.4028 0.0018  0.0205  0.0287  496  MET   B CB   
2861 C  CG   . MET   B 110 ? 0.4414 0.3962 0.4419 0.0066  0.0175  0.0278  496  MET   B CG   
2862 S  SD   . MET   B 110 ? 0.4457 0.4046 0.4519 0.0114  0.0151  0.0235  496  MET   B SD   
2863 C  CE   . MET   B 110 ? 0.3977 0.3664 0.4083 0.0082  0.0181  0.0206  496  MET   B CE   
2864 N  N    . ILE   B 111 ? 0.3781 0.3282 0.3830 -0.0092 0.0288  0.0321  497  ILE   B N    
2865 C  CA   . ILE   B 111 ? 0.3987 0.3479 0.4075 -0.0136 0.0311  0.0336  497  ILE   B CA   
2866 C  C    . ILE   B 111 ? 0.4180 0.3643 0.4213 -0.0175 0.0326  0.0391  497  ILE   B C    
2867 O  O    . ILE   B 111 ? 0.4489 0.3895 0.4531 -0.0212 0.0318  0.0426  497  ILE   B O    
2868 C  CB   . ILE   B 111 ? 0.3734 0.3313 0.3876 -0.0147 0.0348  0.0304  497  ILE   B CB   
2869 C  CG1  . ILE   B 111 ? 0.3874 0.3472 0.4062 -0.0115 0.0330  0.0257  497  ILE   B CG1  
2870 C  CG2  . ILE   B 111 ? 0.3863 0.3461 0.4055 -0.0193 0.0374  0.0322  497  ILE   B CG2  
2871 C  CD1  . ILE   B 111 ? 0.4225 0.3782 0.4464 -0.0113 0.0303  0.0248  497  ILE   B CD1  
2872 N  N    . GLY   B 112 ? 0.4273 0.3772 0.4243 -0.0172 0.0345  0.0403  498  GLY   B N    
2873 C  CA   . GLY   B 112 ? 0.4295 0.3777 0.4201 -0.0209 0.0362  0.0459  498  GLY   B CA   
2874 C  C    . GLY   B 112 ? 0.4603 0.3968 0.4462 -0.0212 0.0317  0.0507  498  GLY   B C    
2875 O  O    . GLY   B 112 ? 0.4530 0.3850 0.4369 -0.0263 0.0323  0.0560  498  GLY   B O    
2876 N  N    . GLU   B 113 ? 0.4130 0.3445 0.3969 -0.0158 0.0270  0.0491  499  GLU   B N    
2877 C  CA   . GLU   B 113 ? 0.4497 0.3690 0.4287 -0.0144 0.0219  0.0529  499  GLU   B CA   
2878 C  C    . GLU   B 113 ? 0.4572 0.3675 0.4400 -0.0176 0.0200  0.0542  499  GLU   B C    
2879 O  O    . GLU   B 113 ? 0.5389 0.4381 0.5168 -0.0205 0.0173  0.0595  499  GLU   B O    
2880 C  CB   . GLU   B 113 ? 0.4832 0.4013 0.4615 -0.0068 0.0173  0.0496  499  GLU   B CB   
2881 C  CG   . GLU   B 113 ? 0.4586 0.3850 0.4328 -0.0041 0.0178  0.0488  499  GLU   B CG   
2882 C  CD   . GLU   B 113 ? 0.5367 0.4590 0.5011 -0.0058 0.0173  0.0547  499  GLU   B CD   
2883 O  OE1  . GLU   B 113 ? 0.5509 0.4631 0.5103 -0.0035 0.0126  0.0584  499  GLU   B OE1  
2884 O  OE2  . GLU   B 113 ? 0.5694 0.4982 0.5305 -0.0092 0.0213  0.0556  499  GLU   B OE2  
2885 N  N    . VAL   B 114 ? 0.4605 0.3750 0.4518 -0.0176 0.0210  0.0495  500  VAL   B N    
2886 C  CA   . VAL   B 114 ? 0.4728 0.3796 0.4682 -0.0211 0.0190  0.0501  500  VAL   B CA   
2887 C  C    . VAL   B 114 ? 0.4946 0.4045 0.4914 -0.0297 0.0229  0.0547  500  VAL   B C    
2888 O  O    . VAL   B 114 ? 0.5322 0.4322 0.5268 -0.0348 0.0206  0.0596  500  VAL   B O    
2889 C  CB   . VAL   B 114 ? 0.4907 0.4019 0.4941 -0.0181 0.0186  0.0435  500  VAL   B CB   
2890 C  CG1  . VAL   B 114 ? 0.4508 0.3543 0.4582 -0.0221 0.0161  0.0438  500  VAL   B CG1  
2891 C  CG2  . VAL   B 114 ? 0.4672 0.3766 0.4689 -0.0099 0.0149  0.0395  500  VAL   B CG2  
2892 N  N    . VAL   B 115 ? 0.4942 0.4181 0.4947 -0.0314 0.0288  0.0533  501  VAL   B N    
2893 C  CA   . VAL   B 115 ? 0.5110 0.4417 0.5140 -0.0389 0.0333  0.0572  501  VAL   B CA   
2894 C  C    . VAL   B 115 ? 0.5203 0.4444 0.5148 -0.0438 0.0329  0.0651  501  VAL   B C    
2895 O  O    . VAL   B 115 ? 0.5257 0.4472 0.5213 -0.0513 0.0331  0.0702  501  VAL   B O    
2896 C  CB   . VAL   B 115 ? 0.5071 0.4536 0.5131 -0.0378 0.0395  0.0540  501  VAL   B CB   
2897 C  CG1  . VAL   B 115 ? 0.5548 0.5106 0.5616 -0.0446 0.0448  0.0586  501  VAL   B CG1  
2898 C  CG2  . VAL   B 115 ? 0.4581 0.4104 0.4729 -0.0345 0.0397  0.0474  501  VAL   B CG2  
2899 N  N    . TYR   B 116 ? 0.5129 0.4343 0.4985 -0.0401 0.0321  0.0665  502  TYR   B N    
2900 C  CA   . TYR   B 116 ? 0.5370 0.4527 0.5131 -0.0443 0.0318  0.0743  502  TYR   B CA   
2901 C  C    . TYR   B 116 ? 0.5866 0.4833 0.5568 -0.0432 0.0243  0.0779  502  TYR   B C    
2902 O  O    . TYR   B 116 ? 0.5728 0.4619 0.5334 -0.0450 0.0225  0.0843  502  TYR   B O    
2903 C  CB   . TYR   B 116 ? 0.5904 0.5143 0.5594 -0.0412 0.0350  0.0741  502  TYR   B CB   
2904 C  CG   . TYR   B 116 ? 0.5773 0.5181 0.5509 -0.0432 0.0424  0.0715  502  TYR   B CG   
2905 C  CD1  . TYR   B 116 ? 0.7478 0.6956 0.7215 -0.0506 0.0471  0.0766  502  TYR   B CD1  
2906 C  CD2  . TYR   B 116 ? 0.5710 0.5206 0.5486 -0.0377 0.0444  0.0640  502  TYR   B CD2  
2907 C  CE1  . TYR   B 116 ? 0.6820 0.6463 0.6601 -0.0514 0.0538  0.0737  502  TYR   B CE1  
2908 C  CE2  . TYR   B 116 ? 0.5958 0.5593 0.5771 -0.0386 0.0505  0.0612  502  TYR   B CE2  
2909 C  CZ   . TYR   B 116 ? 0.6831 0.6544 0.6648 -0.0449 0.0554  0.0658  502  TYR   B CZ   
2910 O  OH   . TYR   B 116 ? 0.7024 0.6888 0.6878 -0.0448 0.0616  0.0628  502  TYR   B OH   
2911 N  N    . GLN   B 117 ? 0.5711 0.4595 0.5464 -0.0401 0.0197  0.0738  503  GLN   B N    
2912 C  CA   . GLN   B 117 ? 0.5731 0.4420 0.5435 -0.0394 0.0122  0.0765  503  GLN   B CA   
2913 C  C    . GLN   B 117 ? 0.6065 0.4669 0.5674 -0.0324 0.0078  0.0779  503  GLN   B C    
2914 O  O    . GLN   B 117 ? 0.5583 0.4020 0.5116 -0.0329 0.0021  0.0829  503  GLN   B O    
2915 C  CB   . GLN   B 117 ? 0.5922 0.4525 0.5600 -0.0498 0.0115  0.0845  503  GLN   B CB   
2916 C  CG   . GLN   B 117 ? 0.6146 0.4877 0.5920 -0.0576 0.0168  0.0843  503  GLN   B CG   
2917 C  CD   . GLN   B 117 ? 0.7649 0.6285 0.7414 -0.0684 0.0146  0.0916  503  GLN   B CD   
2918 O  OE1  . GLN   B 117 ? 0.8691 0.7229 0.8496 -0.0706 0.0100  0.0901  503  GLN   B OE1  
2919 N  NE2  . GLN   B 117 ? 0.7951 0.6619 0.7659 -0.0756 0.0178  0.0998  503  GLN   B NE2  
2920 N  N    . ARG   B 118 ? 0.5139 0.3853 0.4750 -0.0258 0.0098  0.0736  504  ARG   B N    
2921 C  CA   . ARG   B 118 ? 0.5921 0.4578 0.5464 -0.0180 0.0051  0.0736  504  ARG   B CA   
2922 C  C    . ARG   B 118 ? 0.5692 0.4311 0.5276 -0.0095 0.0004  0.0671  504  ARG   B C    
2923 O  O    . ARG   B 118 ? 0.5536 0.4075 0.5068 -0.0025 -0.0051 0.0673  504  ARG   B O    
2924 C  CB   . ARG   B 118 ? 0.6023 0.4820 0.5542 -0.0158 0.0088  0.0726  504  ARG   B CB   
2925 C  CG   . ARG   B 118 ? 0.6443 0.5252 0.5879 -0.0219 0.0118  0.0797  504  ARG   B CG   
2926 C  CD   . ARG   B 118 ? 0.6995 0.5929 0.6398 -0.0189 0.0146  0.0777  504  ARG   B CD   
2927 N  NE   . ARG   B 118 ? 0.5730 0.4809 0.5209 -0.0199 0.0204  0.0719  504  ARG   B NE   
2928 C  CZ   . ARG   B 118 ? 0.6935 0.6102 0.6418 -0.0255 0.0266  0.0730  504  ARG   B CZ   
2929 N  NH1  . ARG   B 118 ? 0.7339 0.6481 0.6757 -0.0316 0.0285  0.0801  504  ARG   B NH1  
2930 N  NH2  . ARG   B 118 ? 0.6693 0.5976 0.6243 -0.0249 0.0309  0.0670  504  ARG   B NH2  
2931 N  N    . ALA   B 119 ? 0.5347 0.4028 0.5022 -0.0096 0.0024  0.0614  505  ALA   B N    
2932 C  CA   . ALA   B 119 ? 0.5498 0.4143 0.5212 -0.0027 -0.0015 0.0552  505  ALA   B CA   
2933 C  C    . ALA   B 119 ? 0.5666 0.4242 0.5428 -0.0073 -0.0023 0.0540  505  ALA   B C    
2934 O  O    . ALA   B 119 ? 0.5198 0.3834 0.5005 -0.0151 0.0021  0.0555  505  ALA   B O    
2935 C  CB   . ALA   B 119 ? 0.4722 0.3529 0.4499 0.0023  0.0014  0.0487  505  ALA   B CB   
2936 N  N    . VAL   B 120 ? 0.5276 0.3734 0.5029 -0.0019 -0.0082 0.0507  506  VAL   B N    
2937 C  CA   . VAL   B 120 ? 0.5621 0.4004 0.5413 -0.0051 -0.0102 0.0483  506  VAL   B CA   
2938 C  C    . VAL   B 120 ? 0.5269 0.3793 0.5148 -0.0026 -0.0070 0.0412  506  VAL   B C    
2939 O  O    . VAL   B 120 ? 0.4962 0.3498 0.4897 -0.0076 -0.0059 0.0396  506  VAL   B O    
2940 C  CB   . VAL   B 120 ? 0.5790 0.3969 0.5519 0.0002  -0.0185 0.0474  506  VAL   B CB   
2941 C  CG1  . VAL   B 120 ? 0.6067 0.4174 0.5834 -0.0012 -0.0214 0.0429  506  VAL   B CG1  
2942 C  CG2  . VAL   B 120 ? 0.6591 0.4606 0.6229 -0.0040 -0.0223 0.0555  506  VAL   B CG2  
2943 N  N    . MET   B 121 ? 0.5424 0.4060 0.5314 0.0048  -0.0056 0.0372  507  MET   B N    
2944 C  CA   . MET   B 121 ? 0.4958 0.3734 0.4923 0.0063  -0.0022 0.0316  507  MET   B CA   
2945 C  C    . MET   B 121 ? 0.4665 0.3583 0.4634 0.0105  0.0007  0.0304  507  MET   B C    
2946 O  O    . MET   B 121 ? 0.4927 0.3831 0.4845 0.0143  -0.0010 0.0326  507  MET   B O    
2947 C  CB   . MET   B 121 ? 0.5850 0.4576 0.5827 0.0120  -0.0063 0.0256  507  MET   B CB   
2948 C  CG   . MET   B 121 ? 0.5819 0.4485 0.5745 0.0220  -0.0113 0.0230  507  MET   B CG   
2949 S  SD   . MET   B 121 ? 0.7132 0.5685 0.7046 0.0283  -0.0171 0.0162  507  MET   B SD   
2950 C  CE   . MET   B 121 ? 0.7069 0.5506 0.6999 0.0173  -0.0179 0.0189  507  MET   B CE   
2951 N  N    . ALA   B 122 ? 0.4387 0.3438 0.4417 0.0094  0.0048  0.0272  508  ALA   B N    
2952 C  CA   . ALA   B 122 ? 0.4587 0.3774 0.4629 0.0121  0.0073  0.0256  508  ALA   B CA   
2953 C  C    . ALA   B 122 ? 0.4562 0.3819 0.4645 0.0168  0.0066  0.0201  508  ALA   B C    
2954 O  O    . ALA   B 122 ? 0.4402 0.3654 0.4524 0.0150  0.0071  0.0176  508  ALA   B O    
2955 C  CB   . ALA   B 122 ? 0.4024 0.3300 0.4092 0.0060  0.0126  0.0270  508  ALA   B CB   
2956 N  N    . VAL   B 123 ? 0.4597 0.3929 0.4671 0.0227  0.0055  0.0185  509  VAL   B N    
2957 C  CA   . VAL   B 123 ? 0.4489 0.3899 0.4592 0.0280  0.0047  0.0137  509  VAL   B CA   
2958 C  C    . VAL   B 123 ? 0.4176 0.3741 0.4301 0.0279  0.0071  0.0134  509  VAL   B C    
2959 O  O    . VAL   B 123 ? 0.4556 0.4159 0.4657 0.0297  0.0063  0.0153  509  VAL   B O    
2960 C  CB   . VAL   B 123 ? 0.5032 0.4382 0.5100 0.0365  -0.0001 0.0116  509  VAL   B CB   
2961 C  CG1  . VAL   B 123 ? 0.5230 0.4708 0.5325 0.0427  -0.0002 0.0069  509  VAL   B CG1  
2962 C  CG2  . VAL   B 123 ? 0.5188 0.4364 0.5229 0.0361  -0.0035 0.0114  509  VAL   B CG2  
2963 N  N    . GLY   B 124 ? 0.3893 0.3541 0.4060 0.0252  0.0097  0.0114  510  GLY   B N    
2964 C  CA   . GLY   B 124 ? 0.4353 0.4139 0.4537 0.0246  0.0112  0.0112  510  GLY   B CA   
2965 C  C    . GLY   B 124 ? 0.4317 0.4151 0.4536 0.0198  0.0139  0.0101  510  GLY   B C    
2966 O  O    . GLY   B 124 ? 0.4450 0.4243 0.4687 0.0194  0.0140  0.0083  510  GLY   B O    
2967 N  N    . SER   B 125 ? 0.3606 0.3518 0.3830 0.0163  0.0155  0.0113  511  SER   B N    
2968 C  CA   . SER   B 125 ? 0.3915 0.3862 0.4162 0.0119  0.0174  0.0107  511  SER   B CA   
2969 C  C    . SER   B 125 ? 0.4061 0.3928 0.4307 0.0075  0.0194  0.0117  511  SER   B C    
2970 O  O    . SER   B 125 ? 0.3731 0.3611 0.3970 0.0039  0.0207  0.0124  511  SER   B O    
2971 C  CB   . SER   B 125 ? 0.3846 0.3900 0.4094 0.0097  0.0175  0.0114  511  SER   B CB   
2972 O  OG   . SER   B 125 ? 0.3435 0.3484 0.3655 0.0083  0.0172  0.0134  511  SER   B OG   
2973 N  N    . LEU   B 126 ? 0.3481 0.3267 0.3734 0.0081  0.0192  0.0114  512  LEU   B N    
2974 C  CA   . LEU   B 126 ? 0.3829 0.3555 0.4085 0.0044  0.0212  0.0128  512  LEU   B CA   
2975 C  C    . LEU   B 126 ? 0.3850 0.3573 0.4148 0.0026  0.0221  0.0111  512  LEU   B C    
2976 O  O    . LEU   B 126 ? 0.3843 0.3537 0.4160 0.0039  0.0205  0.0097  512  LEU   B O    
2977 C  CB   . LEU   B 126 ? 0.3768 0.3410 0.4005 0.0051  0.0201  0.0146  512  LEU   B CB   
2978 C  CG   . LEU   B 126 ? 0.4583 0.4180 0.4817 0.0009  0.0224  0.0170  512  LEU   B CG   
2979 C  CD1  . LEU   B 126 ? 0.4134 0.3767 0.4336 -0.0009 0.0247  0.0186  512  LEU   B CD1  
2980 C  CD2  . LEU   B 126 ? 0.4165 0.3668 0.4376 0.0008  0.0205  0.0195  512  LEU   B CD2  
2981 N  N    . THR   B 127 ? 0.3770 0.3517 0.4078 -0.0002 0.0240  0.0110  513  THR   B N    
2982 C  CA   . THR   B 127 ? 0.4105 0.3859 0.4452 -0.0012 0.0243  0.0094  513  THR   B CA   
2983 C  C    . THR   B 127 ? 0.3629 0.3346 0.4010 -0.0029 0.0253  0.0097  513  THR   B C    
2984 O  O    . THR   B 127 ? 0.3939 0.3643 0.4314 -0.0046 0.0274  0.0114  513  THR   B O    
2985 C  CB   . THR   B 127 ? 0.3848 0.3628 0.4188 -0.0028 0.0254  0.0091  513  THR   B CB   
2986 O  OG1  . THR   B 127 ? 0.3546 0.3367 0.3862 -0.0026 0.0239  0.0091  513  THR   B OG1  
2987 C  CG2  . THR   B 127 ? 0.3814 0.3591 0.4193 -0.0034 0.0255  0.0077  513  THR   B CG2  
2988 N  N    . ILE   B 128 ? 0.3569 0.3279 0.3986 -0.0026 0.0238  0.0082  514  ILE   B N    
2989 C  CA   . ILE   B 128 ? 0.3607 0.3300 0.4070 -0.0049 0.0242  0.0085  514  ILE   B CA   
2990 C  C    . ILE   B 128 ? 0.3570 0.3307 0.4065 -0.0061 0.0264  0.0080  514  ILE   B C    
2991 O  O    . ILE   B 128 ? 0.3664 0.3424 0.4164 -0.0048 0.0256  0.0065  514  ILE   B O    
2992 C  CB   . ILE   B 128 ? 0.3784 0.3454 0.4269 -0.0042 0.0212  0.0065  514  ILE   B CB   
2993 C  CG1  . ILE   B 128 ? 0.4118 0.3729 0.4565 -0.0020 0.0186  0.0063  514  ILE   B CG1  
2994 C  CG2  . ILE   B 128 ? 0.3507 0.3181 0.4052 -0.0073 0.0211  0.0066  514  ILE   B CG2  
2995 C  CD1  . ILE   B 128 ? 0.4205 0.3795 0.4656 0.0000  0.0152  0.0033  514  ILE   B CD1  
2996 N  N    . ASN   B 129 ? 0.3971 0.3722 0.4484 -0.0081 0.0291  0.0095  515  ASN   B N    
2997 C  CA   . ASN   B 129 ? 0.3888 0.3690 0.4442 -0.0081 0.0309  0.0084  515  ASN   B CA   
2998 C  C    . ASN   B 129 ? 0.4302 0.4140 0.4907 -0.0109 0.0330  0.0098  515  ASN   B C    
2999 O  O    . ASN   B 129 ? 0.3860 0.3671 0.4460 -0.0138 0.0330  0.0122  515  ASN   B O    
3000 C  CB   . ASN   B 129 ? 0.3493 0.3304 0.4004 -0.0064 0.0328  0.0076  515  ASN   B CB   
3001 C  CG   . ASN   B 129 ? 0.4210 0.4021 0.4678 -0.0074 0.0355  0.0094  515  ASN   B CG   
3002 O  OD1  . ASN   B 129 ? 0.3718 0.3535 0.4197 -0.0097 0.0370  0.0117  515  ASN   B OD1  
3003 N  ND2  . ASN   B 129 ? 0.3974 0.3775 0.4386 -0.0061 0.0360  0.0086  515  ASN   B ND2  
3004 N  N    . GLU   B 130 ? 0.3625 0.3527 0.4279 -0.0102 0.0346  0.0085  516  GLU   B N    
3005 C  CA   . GLU   B 130 ? 0.3608 0.3575 0.4329 -0.0131 0.0365  0.0099  516  GLU   B CA   
3006 C  C    . GLU   B 130 ? 0.3772 0.3758 0.4466 -0.0158 0.0402  0.0129  516  GLU   B C    
3007 O  O    . GLU   B 130 ? 0.3867 0.3854 0.4582 -0.0204 0.0403  0.0159  516  GLU   B O    
3008 C  CB   . GLU   B 130 ? 0.3819 0.3870 0.4602 -0.0106 0.0375  0.0075  516  GLU   B CB   
3009 C  CG   . GLU   B 130 ? 0.4216 0.4366 0.5083 -0.0138 0.0395  0.0090  516  GLU   B CG   
3010 C  CD   . GLU   B 130 ? 0.4529 0.4782 0.5458 -0.0100 0.0410  0.0065  516  GLU   B CD   
3011 O  OE1  . GLU   B 130 ? 0.4679 0.4911 0.5569 -0.0048 0.0412  0.0038  516  GLU   B OE1  
3012 O  OE2  . GLU   B 130 ? 0.4689 0.5043 0.5706 -0.0123 0.0417  0.0072  516  GLU   B OE2  
3013 N  N    . GLU   B 131 ? 0.3979 0.3973 0.4619 -0.0134 0.0429  0.0123  517  GLU   B N    
3014 C  CA   . GLU   B 131 ? 0.3731 0.3759 0.4341 -0.0157 0.0468  0.0150  517  GLU   B CA   
3015 C  C    . GLU   B 131 ? 0.4087 0.4037 0.4645 -0.0190 0.0454  0.0188  517  GLU   B C    
3016 O  O    . GLU   B 131 ? 0.4177 0.4146 0.4736 -0.0233 0.0473  0.0226  517  GLU   B O    
3017 C  CB   . GLU   B 131 ? 0.4219 0.4265 0.4771 -0.0119 0.0495  0.0129  517  GLU   B CB   
3018 C  CG   . GLU   B 131 ? 0.4063 0.4022 0.4532 -0.0098 0.0471  0.0119  517  GLU   B CG   
3019 C  CD   . GLU   B 131 ? 0.4670 0.4640 0.5069 -0.0075 0.0496  0.0103  517  GLU   B CD   
3020 O  OE1  . GLU   B 131 ? 0.4764 0.4809 0.5176 -0.0063 0.0534  0.0094  517  GLU   B OE1  
3021 O  OE2  . GLU   B 131 ? 0.4330 0.4240 0.4659 -0.0066 0.0478  0.0099  517  GLU   B OE2  
3022 N  N    . ARG   B 132 ? 0.4103 0.3968 0.4617 -0.0171 0.0418  0.0180  518  ARG   B N    
3023 C  CA   . ARG   B 132 ? 0.3648 0.3434 0.4116 -0.0190 0.0397  0.0211  518  ARG   B CA   
3024 C  C    . ARG   B 132 ? 0.4467 0.4220 0.4982 -0.0228 0.0373  0.0228  518  ARG   B C    
3025 O  O    . ARG   B 132 ? 0.4440 0.4140 0.4927 -0.0263 0.0366  0.0267  518  ARG   B O    
3026 C  CB   . ARG   B 132 ? 0.3938 0.3665 0.4360 -0.0152 0.0364  0.0192  518  ARG   B CB   
3027 C  CG   . ARG   B 132 ? 0.3885 0.3628 0.4248 -0.0128 0.0378  0.0183  518  ARG   B CG   
3028 C  CD   . ARG   B 132 ? 0.4093 0.3810 0.4432 -0.0097 0.0347  0.0163  518  ARG   B CD   
3029 N  NE   . ARG   B 132 ? 0.3444 0.3173 0.3726 -0.0085 0.0354  0.0158  518  ARG   B NE   
3030 C  CZ   . ARG   B 132 ? 0.3518 0.3243 0.3772 -0.0068 0.0331  0.0148  518  ARG   B CZ   
3031 N  NH1  . ARG   B 132 ? 0.3589 0.3309 0.3866 -0.0054 0.0304  0.0139  518  ARG   B NH1  
3032 N  NH2  . ARG   B 132 ? 0.3401 0.3135 0.3602 -0.0067 0.0333  0.0146  518  ARG   B NH2  
3033 N  N    . SER   B 133 ? 0.4170 0.3944 0.4749 -0.0223 0.0354  0.0201  519  SER   B N    
3034 C  CA   . SER   B 133 ? 0.4339 0.4079 0.4961 -0.0262 0.0325  0.0212  519  SER   B CA   
3035 C  C    . SER   B 133 ? 0.4737 0.4537 0.5404 -0.0323 0.0351  0.0250  519  SER   B C    
3036 O  O    . SER   B 133 ? 0.4880 0.4636 0.5569 -0.0373 0.0325  0.0273  519  SER   B O    
3037 C  CB   . SER   B 133 ? 0.4315 0.4077 0.4993 -0.0243 0.0299  0.0174  519  SER   B CB   
3038 O  OG   . SER   B 133 ? 0.4140 0.3853 0.4773 -0.0194 0.0275  0.0145  519  SER   B OG   
3039 N  N    . GLU   B 134 ? 0.4528 0.4430 0.5205 -0.0322 0.0402  0.0257  520  GLU   B N    
3040 C  CA   . GLU   B 134 ? 0.4455 0.4441 0.5173 -0.0381 0.0435  0.0297  520  GLU   B CA   
3041 C  C    . GLU   B 134 ? 0.5003 0.4918 0.5649 -0.0424 0.0438  0.0351  520  GLU   B C    
3042 O  O    . GLU   B 134 ? 0.4911 0.4866 0.5585 -0.0493 0.0452  0.0397  520  GLU   B O    
3043 C  CB   . GLU   B 134 ? 0.4547 0.4675 0.5293 -0.0354 0.0490  0.0281  520  GLU   B CB   
3044 C  CG   . GLU   B 134 ? 0.4275 0.4482 0.5101 -0.0314 0.0486  0.0233  520  GLU   B CG   
3045 C  CD   . GLU   B 134 ? 0.5803 0.6140 0.6650 -0.0276 0.0536  0.0212  520  GLU   B CD   
3046 O  OE1  . GLU   B 134 ? 0.6198 0.6564 0.6989 -0.0277 0.0577  0.0229  520  GLU   B OE1  
3047 O  OE2  . GLU   B 134 ? 0.6233 0.6637 0.7144 -0.0238 0.0532  0.0176  520  GLU   B OE2  
3048 N  N    . VAL   B 135 ? 0.4719 0.4535 0.5274 -0.0390 0.0423  0.0352  521  VAL   B N    
3049 C  CA   . VAL   B 135 ? 0.4575 0.4317 0.5052 -0.0422 0.0422  0.0405  521  VAL   B CA   
3050 C  C    . VAL   B 135 ? 0.4788 0.4369 0.5213 -0.0412 0.0361  0.0411  521  VAL   B C    
3051 O  O    . VAL   B 135 ? 0.4653 0.4147 0.5021 -0.0449 0.0345  0.0461  521  VAL   B O    
3052 C  CB   . VAL   B 135 ? 0.4742 0.4522 0.5145 -0.0390 0.0460  0.0408  521  VAL   B CB   
3053 C  CG1  . VAL   B 135 ? 0.4874 0.4812 0.5317 -0.0398 0.0522  0.0403  521  VAL   B CG1  
3054 C  CG2  . VAL   B 135 ? 0.4715 0.4456 0.5080 -0.0317 0.0440  0.0359  521  VAL   B CG2  
3055 N  N    . VAL   B 136 ? 0.4673 0.4208 0.5105 -0.0359 0.0326  0.0362  522  VAL   B N    
3056 C  CA   . VAL   B 136 ? 0.4656 0.4050 0.5045 -0.0339 0.0268  0.0358  522  VAL   B CA   
3057 C  C    . VAL   B 136 ? 0.5352 0.4733 0.5801 -0.0333 0.0235  0.0317  522  VAL   B C    
3058 O  O    . VAL   B 136 ? 0.5107 0.4589 0.5623 -0.0328 0.0255  0.0288  522  VAL   B O    
3059 C  CB   . VAL   B 136 ? 0.4735 0.4094 0.5058 -0.0269 0.0256  0.0338  522  VAL   B CB   
3060 C  CG1  . VAL   B 136 ? 0.4591 0.3962 0.4848 -0.0274 0.0282  0.0376  522  VAL   B CG1  
3061 C  CG2  . VAL   B 136 ? 0.4403 0.3846 0.4761 -0.0220 0.0269  0.0284  522  VAL   B CG2  
3062 N  N    . ASP   B 137 ? 0.4668 0.3919 0.5087 -0.0328 0.0179  0.0313  523  ASP   B N    
3063 C  CA   . ASP   B 137 ? 0.4932 0.4154 0.5381 -0.0303 0.0140  0.0264  523  ASP   B CA   
3064 C  C    . ASP   B 137 ? 0.4923 0.4138 0.5332 -0.0219 0.0129  0.0221  523  ASP   B C    
3065 O  O    . ASP   B 137 ? 0.5123 0.4297 0.5469 -0.0183 0.0125  0.0232  523  ASP   B O    
3066 C  CB   . ASP   B 137 ? 0.4939 0.4015 0.5367 -0.0337 0.0082  0.0274  523  ASP   B CB   
3067 C  CG   . ASP   B 137 ? 0.5589 0.4692 0.6079 -0.0432 0.0084  0.0310  523  ASP   B CG   
3068 O  OD1  . ASP   B 137 ? 0.5001 0.4253 0.5562 -0.0459 0.0133  0.0316  523  ASP   B OD1  
3069 O  OD2  . ASP   B 137 ? 0.5848 0.4822 0.6314 -0.0477 0.0036  0.0330  523  ASP   B OD2  
3070 N  N    . PHE   B 138 ? 0.4481 0.3747 0.4927 -0.0189 0.0122  0.0174  524  PHE   B N    
3071 C  CA   . PHE   B 138 ? 0.4325 0.3599 0.4737 -0.0117 0.0110  0.0135  524  PHE   B CA   
3072 C  C    . PHE   B 138 ? 0.4604 0.3805 0.5006 -0.0091 0.0059  0.0094  524  PHE   B C    
3073 O  O    . PHE   B 138 ? 0.4490 0.3680 0.4932 -0.0127 0.0041  0.0084  524  PHE   B O    
3074 C  CB   . PHE   B 138 ? 0.4325 0.3723 0.4774 -0.0101 0.0145  0.0115  524  PHE   B CB   
3075 C  CG   . PHE   B 138 ? 0.4098 0.3557 0.4531 -0.0099 0.0186  0.0137  524  PHE   B CG   
3076 C  CD1  . PHE   B 138 ? 0.4123 0.3580 0.4503 -0.0058 0.0185  0.0136  524  PHE   B CD1  
3077 C  CD2  . PHE   B 138 ? 0.4020 0.3546 0.4491 -0.0136 0.0225  0.0155  524  PHE   B CD2  
3078 C  CE1  . PHE   B 138 ? 0.3771 0.3281 0.4131 -0.0060 0.0217  0.0153  524  PHE   B CE1  
3079 C  CE2  . PHE   B 138 ? 0.3995 0.3569 0.4441 -0.0131 0.0259  0.0168  524  PHE   B CE2  
3080 C  CZ   . PHE   B 138 ? 0.3957 0.3517 0.4344 -0.0095 0.0253  0.0167  524  PHE   B CZ   
3081 N  N    . SER   B 139 ? 0.4598 0.3759 0.4945 -0.0025 0.0036  0.0069  525  SER   B N    
3082 C  CA   . SER   B 139 ? 0.4572 0.3695 0.4901 0.0019  -0.0004 0.0018  525  SER   B CA   
3083 C  C    . SER   B 139 ? 0.4743 0.3980 0.5115 0.0024  0.0014  -0.0010 525  SER   B C    
3084 O  O    . SER   B 139 ? 0.4220 0.3556 0.4630 0.0002  0.0055  0.0008  525  SER   B O    
3085 C  CB   . SER   B 139 ? 0.4607 0.3706 0.4875 0.0100  -0.0022 -0.0005 525  SER   B CB   
3086 O  OG   . SER   B 139 ? 0.4693 0.3924 0.4971 0.0128  0.0016  -0.0006 525  SER   B OG   
3087 N  N    . VAL   B 140 ? 0.4870 0.4088 0.5225 0.0059  -0.0019 -0.0056 526  VAL   B N    
3088 C  CA   . VAL   B 140 ? 0.4737 0.4062 0.5111 0.0076  -0.0006 -0.0082 526  VAL   B CA   
3089 C  C    . VAL   B 140 ? 0.4306 0.3726 0.4664 0.0111  0.0030  -0.0073 526  VAL   B C    
3090 O  O    . VAL   B 140 ? 0.4207 0.3606 0.4527 0.0149  0.0027  -0.0070 526  VAL   B O    
3091 C  CB   . VAL   B 140 ? 0.4897 0.4188 0.5235 0.0118  -0.0048 -0.0135 526  VAL   B CB   
3092 C  CG1  . VAL   B 140 ? 0.5167 0.4356 0.5518 0.0075  -0.0091 -0.0145 526  VAL   B CG1  
3093 C  CG2  . VAL   B 140 ? 0.4912 0.4159 0.5183 0.0191  -0.0066 -0.0161 526  VAL   B CG2  
3094 N  N    . PRO   B 141 ? 0.4088 0.3610 0.4475 0.0098  0.0058  -0.0066 527  PRO   B N    
3095 C  CA   . PRO   B 141 ? 0.4022 0.3631 0.4390 0.0123  0.0084  -0.0057 527  PRO   B CA   
3096 C  C    . PRO   B 141 ? 0.4385 0.4027 0.4710 0.0183  0.0067  -0.0091 527  PRO   B C    
3097 O  O    . PRO   B 141 ? 0.4035 0.3659 0.4345 0.0204  0.0042  -0.0126 527  PRO   B O    
3098 C  CB   . PRO   B 141 ? 0.3929 0.3612 0.4331 0.0091  0.0104  -0.0047 527  PRO   B CB   
3099 C  CG   . PRO   B 141 ? 0.3950 0.3604 0.4377 0.0076  0.0081  -0.0065 527  PRO   B CG   
3100 C  CD   . PRO   B 141 ? 0.4135 0.3693 0.4569 0.0061  0.0061  -0.0066 527  PRO   B CD   
3101 N  N    . PHE   B 142 ? 0.3715 0.3419 0.4020 0.0214  0.0082  -0.0083 528  PHE   B N    
3102 C  CA   . PHE   B 142 ? 0.4072 0.3843 0.4342 0.0276  0.0073  -0.0114 528  PHE   B CA   
3103 C  C    . PHE   B 142 ? 0.4192 0.4105 0.4466 0.0274  0.0102  -0.0095 528  PHE   B C    
3104 O  O    . PHE   B 142 ? 0.4661 0.4663 0.4913 0.0323  0.0101  -0.0116 528  PHE   B O    
3105 C  CB   . PHE   B 142 ? 0.3972 0.3673 0.4207 0.0336  0.0047  -0.0133 528  PHE   B CB   
3106 C  CG   . PHE   B 142 ? 0.4552 0.4228 0.4790 0.0327  0.0056  -0.0098 528  PHE   B CG   
3107 C  CD1  . PHE   B 142 ? 0.4836 0.4396 0.5081 0.0285  0.0049  -0.0072 528  PHE   B CD1  
3108 C  CD2  . PHE   B 142 ? 0.4728 0.4508 0.4961 0.0359  0.0069  -0.0088 528  PHE   B CD2  
3109 C  CE1  . PHE   B 142 ? 0.4925 0.4464 0.5162 0.0276  0.0057  -0.0036 528  PHE   B CE1  
3110 C  CE2  . PHE   B 142 ? 0.5007 0.4767 0.5237 0.0352  0.0073  -0.0056 528  PHE   B CE2  
3111 C  CZ   . PHE   B 142 ? 0.5215 0.4849 0.5443 0.0312  0.0067  -0.0029 528  PHE   B CZ   
3112 N  N    . VAL   B 143 ? 0.4216 0.4155 0.4515 0.0220  0.0125  -0.0057 529  VAL   B N    
3113 C  CA   . VAL   B 143 ? 0.4008 0.4064 0.4309 0.0198  0.0145  -0.0036 529  VAL   B CA   
3114 C  C    . VAL   B 143 ? 0.4114 0.4145 0.4436 0.0138  0.0154  -0.0014 529  VAL   B C    
3115 O  O    . VAL   B 143 ? 0.3813 0.3774 0.4152 0.0110  0.0160  0.0001  529  VAL   B O    
3116 C  CB   . VAL   B 143 ? 0.3634 0.3745 0.3935 0.0199  0.0155  -0.0013 529  VAL   B CB   
3117 C  CG1  . VAL   B 143 ? 0.4260 0.4485 0.4564 0.0160  0.0170  0.0012  529  VAL   B CG1  
3118 C  CG2  . VAL   B 143 ? 0.3913 0.4056 0.4197 0.0269  0.0142  -0.0036 529  VAL   B CG2  
3119 N  N    . GLU   B 144 ? 0.3771 0.3861 0.4086 0.0122  0.0155  -0.0011 530  GLU   B N    
3120 C  CA   . GLU   B 144 ? 0.4408 0.4467 0.4736 0.0075  0.0157  0.0009  530  GLU   B CA   
3121 C  C    . GLU   B 144 ? 0.4244 0.4309 0.4574 0.0037  0.0170  0.0040  530  GLU   B C    
3122 O  O    . GLU   B 144 ? 0.3733 0.3875 0.4047 0.0028  0.0176  0.0056  530  GLU   B O    
3123 C  CB   . GLU   B 144 ? 0.4566 0.4683 0.4873 0.0066  0.0150  0.0012  530  GLU   B CB   
3124 C  CG   . GLU   B 144 ? 0.5092 0.5186 0.5393 0.0093  0.0131  -0.0019 530  GLU   B CG   
3125 C  CD   . GLU   B 144 ? 0.5413 0.5566 0.5685 0.0080  0.0124  -0.0010 530  GLU   B CD   
3126 O  OE1  . GLU   B 144 ? 0.5921 0.6116 0.6181 0.0043  0.0131  0.0027  530  GLU   B OE1  
3127 O  OE2  . GLU   B 144 ? 0.5373 0.5524 0.5628 0.0105  0.0107  -0.0037 530  GLU   B OE2  
3128 N  N    . THR   B 145 ? 0.3688 0.3680 0.4035 0.0015  0.0175  0.0047  531  THR   B N    
3129 C  CA   . THR   B 145 ? 0.3389 0.3377 0.3725 -0.0019 0.0182  0.0070  531  THR   B CA   
3130 C  C    . THR   B 145 ? 0.3947 0.3869 0.4296 -0.0038 0.0181  0.0072  531  THR   B C    
3131 O  O    . THR   B 145 ? 0.3653 0.3554 0.4021 -0.0030 0.0172  0.0061  531  THR   B O    
3132 C  CB   . THR   B 145 ? 0.3514 0.3497 0.3846 -0.0011 0.0193  0.0073  531  THR   B CB   
3133 O  OG1  . THR   B 145 ? 0.3336 0.3332 0.3647 -0.0044 0.0194  0.0092  531  THR   B OG1  
3134 C  CG2  . THR   B 145 ? 0.3386 0.3294 0.3737 -0.0004 0.0202  0.0065  531  THR   B CG2  
3135 N  N    . GLY   B 146 ? 0.3893 0.3786 0.4227 -0.0059 0.0187  0.0083  532  GLY   B N    
3136 C  CA   . GLY   B 146 ? 0.3706 0.3539 0.4044 -0.0068 0.0184  0.0081  532  GLY   B CA   
3137 C  C    . GLY   B 146 ? 0.3376 0.3185 0.3671 -0.0096 0.0179  0.0093  532  GLY   B C    
3138 O  O    . GLY   B 146 ? 0.3715 0.3549 0.3993 -0.0104 0.0186  0.0099  532  GLY   B O    
3139 N  N    . ILE   B 147 ? 0.3453 0.3210 0.3729 -0.0108 0.0162  0.0097  533  ILE   B N    
3140 C  CA   . ILE   B 147 ? 0.3761 0.3468 0.3989 -0.0137 0.0148  0.0105  533  ILE   B CA   
3141 C  C    . ILE   B 147 ? 0.4398 0.4102 0.4593 -0.0175 0.0119  0.0133  533  ILE   B C    
3142 O  O    . ILE   B 147 ? 0.4345 0.4019 0.4542 -0.0169 0.0102  0.0137  533  ILE   B O    
3143 C  CB   . ILE   B 147 ? 0.3967 0.3591 0.4188 -0.0115 0.0148  0.0083  533  ILE   B CB   
3144 C  CG1  . ILE   B 147 ? 0.3806 0.3451 0.4055 -0.0087 0.0182  0.0063  533  ILE   B CG1  
3145 C  CG2  . ILE   B 147 ? 0.4241 0.3796 0.4398 -0.0144 0.0126  0.0086  533  ILE   B CG2  
3146 C  CD1  . ILE   B 147 ? 0.3897 0.3489 0.4143 -0.0058 0.0190  0.0038  533  ILE   B CD1  
3147 N  N    . SER   B 148 ? 0.4065 0.3813 0.4232 -0.0217 0.0111  0.0155  534  SER   B N    
3148 C  CA   . SER   B 148 ? 0.3746 0.3492 0.3875 -0.0270 0.0081  0.0189  534  SER   B CA   
3149 C  C    . SER   B 148 ? 0.4177 0.3851 0.4254 -0.0315 0.0056  0.0197  534  SER   B C    
3150 O  O    . SER   B 148 ? 0.3734 0.3378 0.3805 -0.0301 0.0065  0.0174  534  SER   B O    
3151 C  CB   . SER   B 148 ? 0.4345 0.4229 0.4488 -0.0290 0.0091  0.0213  534  SER   B CB   
3152 O  OG   . SER   B 148 ? 0.4185 0.4117 0.4360 -0.0249 0.0106  0.0201  534  SER   B OG   
3153 N  N    . VAL   B 149 ? 0.4298 0.3941 0.4332 -0.0374 0.0022  0.0232  535  VAL   B N    
3154 C  CA   . VAL   B 149 ? 0.3907 0.3463 0.3883 -0.0429 -0.0014 0.0243  535  VAL   B CA   
3155 C  C    . VAL   B 149 ? 0.4723 0.4381 0.4690 -0.0506 -0.0027 0.0290  535  VAL   B C    
3156 O  O    . VAL   B 149 ? 0.4406 0.4115 0.4373 -0.0536 -0.0033 0.0327  535  VAL   B O    
3157 C  CB   . VAL   B 149 ? 0.4930 0.4317 0.4851 -0.0433 -0.0055 0.0244  535  VAL   B CB   
3158 C  CG1  . VAL   B 149 ? 0.5019 0.4295 0.4869 -0.0490 -0.0099 0.0250  535  VAL   B CG1  
3159 C  CG2  . VAL   B 149 ? 0.5071 0.4390 0.5014 -0.0349 -0.0038 0.0198  535  VAL   B CG2  
3160 N  N    . MET   B 150 ? 0.4154 0.3855 0.4115 -0.0541 -0.0032 0.0291  536  MET   B N    
3161 C  CA   . MET   B 150 ? 0.4250 0.4072 0.4213 -0.0620 -0.0045 0.0337  536  MET   B CA   
3162 C  C    . MET   B 150 ? 0.4856 0.4558 0.4750 -0.0704 -0.0101 0.0361  536  MET   B C    
3163 O  O    . MET   B 150 ? 0.4639 0.4220 0.4493 -0.0697 -0.0121 0.0329  536  MET   B O    
3164 C  CB   . MET   B 150 ? 0.4143 0.4120 0.4154 -0.0603 -0.0019 0.0327  536  MET   B CB   
3165 C  CG   . MET   B 150 ? 0.4793 0.4907 0.4811 -0.0687 -0.0036 0.0372  536  MET   B CG   
3166 S  SD   . MET   B 150 ? 0.4973 0.5303 0.5060 -0.0651 -0.0005 0.0362  536  MET   B SD   
3167 C  CE   . MET   B 150 ? 0.4588 0.5069 0.4728 -0.0592 0.0039  0.0365  536  MET   B CE   
3168 N  N    . VAL   B 151 ? 0.4362 0.4092 0.4233 -0.0787 -0.0127 0.0417  537  VAL   B N    
3169 C  CA   . VAL   B 151 ? 0.5073 0.4678 0.4873 -0.0883 -0.0189 0.0449  537  VAL   B CA   
3170 C  C    . VAL   B 151 ? 0.5627 0.5395 0.5442 -0.0988 -0.0199 0.0515  537  VAL   B C    
3171 O  O    . VAL   B 151 ? 0.4950 0.4925 0.4827 -0.0977 -0.0157 0.0533  537  VAL   B O    
3172 C  CB   . VAL   B 151 ? 0.5150 0.4553 0.4883 -0.0885 -0.0227 0.0461  537  VAL   B CB   
3173 C  CG1  . VAL   B 151 ? 0.5008 0.4262 0.4729 -0.0782 -0.0220 0.0395  537  VAL   B CG1  
3174 C  CG2  . VAL   B 151 ? 0.5305 0.4799 0.5058 -0.0891 -0.0209 0.0504  537  VAL   B CG2  
3175 N  N    . SER   B 152 ? 0.5512 0.5189 0.5268 -0.1092 -0.0258 0.0549  538  SER   B N    
3176 C  CA   . SER   B 152 ? 0.6105 0.5921 0.5866 -0.1210 -0.0274 0.0624  538  SER   B CA   
3177 C  C    . SER   B 152 ? 0.6481 0.6269 0.6213 -0.1234 -0.0277 0.0675  538  SER   B C    
3178 O  O    . SER   B 152 ? 0.6109 0.5688 0.5782 -0.1200 -0.0302 0.0664  538  SER   B O    
3179 C  CB   . SER   B 152 ? 0.6148 0.5856 0.5848 -0.1326 -0.0344 0.0651  538  SER   B CB   
3180 O  OG   . SER   B 152 ? 0.7808 0.7614 0.7501 -0.1452 -0.0367 0.0735  538  SER   B OG   
3181 N  N    . ARG   B 153 ? 0.6625 0.6635 0.6397 -0.1289 -0.0251 0.0731  539  ARG   B N    
3182 C  CA   . ARG   B 153 ? 0.6628 0.6647 0.6371 -0.1308 -0.0247 0.0782  539  ARG   B CA   
3183 C  C    . ARG   B 153 ? 0.6705 0.6468 0.6344 -0.1386 -0.0320 0.0825  539  ARG   B C    
3184 O  O    . ARG   B 153 ? 0.6595 0.6273 0.6190 -0.1490 -0.0375 0.0856  539  ARG   B O    
3185 C  CB   . ARG   B 153 ? 0.6758 0.7066 0.6548 -0.1377 -0.0214 0.0843  539  ARG   B CB   
3186 C  CG   . ARG   B 153 ? 0.7006 0.7388 0.6782 -0.1363 -0.0186 0.0879  539  ARG   B CG   
3187 C  CD   . ARG   B 153 ? 0.6950 0.7657 0.6782 -0.1405 -0.0140 0.0923  539  ARG   B CD   
3188 N  NE   . ARG   B 153 ? 0.7117 0.7947 0.6978 -0.1299 -0.0082 0.0892  539  ARG   B NE   
3189 C  CZ   . ARG   B 153 ? 0.6822 0.7828 0.6761 -0.1201 -0.0028 0.0834  539  ARG   B CZ   
3190 N  NH1  . ARG   B 153 ? 0.7172 0.8272 0.7172 -0.1193 -0.0021 0.0806  539  ARG   B NH1  
3191 N  NH2  . ARG   B 153 ? 0.7489 0.8567 0.7438 -0.1108 0.0014  0.0803  539  ARG   B NH2  
3192 N  N    . GLY   B 154 ? 0.7174 0.6799 0.6770 -0.1331 -0.0326 0.0822  540  GLY   B N    
3193 C  CA   . GLY   B 154 ? 0.7327 0.6696 0.6819 -0.1386 -0.0398 0.0863  540  GLY   B CA   
3194 C  C    . GLY   B 154 ? 0.7958 0.7053 0.7404 -0.1307 -0.0437 0.0796  540  GLY   B C    
3195 O  O    . GLY   B 154 ? 0.7287 0.6154 0.6646 -0.1323 -0.0497 0.0819  540  GLY   B O    
3196 N  N    . THR   B 155 ? 0.6885 0.5995 0.6381 -0.1220 -0.0406 0.0716  541  THR   B N    
3197 C  CA   . THR   B 155 ? 0.7271 0.6142 0.6722 -0.1143 -0.0438 0.0650  541  THR   B CA   
3198 C  C    . THR   B 155 ? 0.7215 0.5981 0.6653 -0.1049 -0.0436 0.0632  541  THR   B C    
3199 O  O    . THR   B 155 ? 0.7393 0.6304 0.6898 -0.0980 -0.0379 0.0618  541  THR   B O    
3200 C  CB   . THR   B 155 ? 0.7359 0.6304 0.6871 -0.1067 -0.0395 0.0573  541  THR   B CB   
3201 O  OG1  . THR   B 155 ? 0.6290 0.5333 0.5812 -0.1154 -0.0404 0.0591  541  THR   B OG1  
3202 C  CG2  . THR   B 155 ? 0.6852 0.5572 0.6316 -0.0982 -0.0421 0.0502  541  THR   B CG2  
3203 N  N    . GLN   B 156 ? 0.7073 0.5580 0.6422 -0.1045 -0.0503 0.0631  542  GLN   B N    
3204 C  CA   . GLN   B 156 ? 0.8168 0.6561 0.7497 -0.0961 -0.0515 0.0620  542  GLN   B CA   
3205 C  C    . GLN   B 156 ? 0.8167 0.6525 0.7542 -0.0825 -0.0484 0.0526  542  GLN   B C    
3206 O  O    . GLN   B 156 ? 0.8679 0.6849 0.8001 -0.0786 -0.0523 0.0479  542  GLN   B O    
3207 C  CB   . GLN   B 156 ? 0.8440 0.6570 0.7650 -0.1014 -0.0607 0.0665  542  GLN   B CB   
3208 N  N    . VAL   B 157 ? 0.8047 0.6591 0.7515 -0.0754 -0.0413 0.0497  662  VAL   B N    
3209 C  CA   . VAL   B 157 ? 0.7684 0.6228 0.7207 -0.0632 -0.0376 0.0418  662  VAL   B CA   
3210 C  C    . VAL   B 157 ? 0.7230 0.5901 0.6821 -0.0571 -0.0334 0.0418  662  VAL   B C    
3211 O  O    . VAL   B 157 ? 0.7625 0.6471 0.7257 -0.0607 -0.0298 0.0452  662  VAL   B O    
3212 C  CB   . VAL   B 157 ? 0.7435 0.6084 0.7006 -0.0618 -0.0330 0.0371  662  VAL   B CB   
3213 C  CG1  . VAL   B 157 ? 0.7480 0.6232 0.7136 -0.0513 -0.0268 0.0314  662  VAL   B CG1  
3214 C  CG2  . VAL   B 157 ? 0.7296 0.5769 0.6794 -0.0629 -0.0376 0.0338  662  VAL   B CG2  
3215 N  N    . THR   B 158 ? 0.7048 0.5636 0.6650 -0.0477 -0.0341 0.0379  663  THR   B N    
3216 C  CA   . THR   B 158 ? 0.6986 0.5682 0.6647 -0.0425 -0.0312 0.0380  663  THR   B CA   
3217 C  C    . THR   B 158 ? 0.7021 0.5892 0.6780 -0.0373 -0.0240 0.0334  663  THR   B C    
3218 O  O    . THR   B 158 ? 0.7112 0.6125 0.6919 -0.0370 -0.0207 0.0346  663  THR   B O    
3219 C  CB   . THR   B 158 ? 0.6985 0.5544 0.6628 -0.0346 -0.0351 0.0360  663  THR   B CB   
3220 O  OG1  . THR   B 158 ? 0.6941 0.5462 0.6620 -0.0260 -0.0334 0.0287  663  THR   B OG1  
3221 C  CG2  . THR   B 158 ? 0.6664 0.5016 0.6197 -0.0393 -0.0431 0.0406  663  THR   B CG2  
3222 N  N    . GLY   B 159 ? 0.6381 0.5237 0.6164 -0.0334 -0.0218 0.0280  664  GLY   B N    
3223 C  CA   . GLY   B 159 ? 0.6547 0.5532 0.6417 -0.0273 -0.0158 0.0235  664  GLY   B CA   
3224 C  C    . GLY   B 159 ? 0.6803 0.5725 0.6675 -0.0222 -0.0148 0.0179  664  GLY   B C    
3225 O  O    . GLY   B 159 ? 0.6576 0.5364 0.6379 -0.0237 -0.0185 0.0172  664  GLY   B O    
3226 N  N    . LEU   B 160 ? 0.6204 0.5224 0.6150 -0.0164 -0.0098 0.0141  665  LEU   B N    
3227 C  CA   . LEU   B 160 ? 0.6346 0.5329 0.6295 -0.0113 -0.0080 0.0088  665  LEU   B CA   
3228 C  C    . LEU   B 160 ? 0.6469 0.5321 0.6388 -0.0052 -0.0116 0.0060  665  LEU   B C    
3229 O  O    . LEU   B 160 ? 0.6769 0.5541 0.6650 -0.0019 -0.0121 0.0020  665  LEU   B O    
3230 C  CB   . LEU   B 160 ? 0.5352 0.4470 0.5387 -0.0070 -0.0021 0.0062  665  LEU   B CB   
3231 C  CG   . LEU   B 160 ? 0.5835 0.5059 0.5891 -0.0107 0.0017  0.0071  665  LEU   B CG   
3232 C  CD1  . LEU   B 160 ? 0.5572 0.4897 0.5704 -0.0063 0.0067  0.0046  665  LEU   B CD1  
3233 C  CD2  . LEU   B 160 ? 0.6304 0.5469 0.6298 -0.0134 0.0008  0.0061  665  LEU   B CD2  
3234 N  N    . SER   B 161 ? 0.6060 0.4890 0.5992 -0.0031 -0.0143 0.0078  666  SER   B N    
3235 C  CA   . SER   B 161 ? 0.6447 0.5155 0.6354 0.0035  -0.0184 0.0055  666  SER   B CA   
3236 C  C    . SER   B 161 ? 0.6402 0.4915 0.6197 0.0003  -0.0252 0.0072  666  SER   B C    
3237 O  O    . SER   B 161 ? 0.6730 0.5112 0.6487 0.0066  -0.0294 0.0046  666  SER   B O    
3238 C  CB   . SER   B 161 ? 0.7469 0.6227 0.7426 0.0065  -0.0196 0.0074  666  SER   B CB   
3239 O  OG   . SER   B 161 ? 0.7844 0.6620 0.7776 -0.0008 -0.0214 0.0134  666  SER   B OG   
3240 N  N    . ASP   B 162 ? 0.6442 0.4932 0.6183 -0.0092 -0.0268 0.0116  667  ASP   B N    
3241 C  CA   . ASP   B 162 ? 0.5905 0.4199 0.5535 -0.0138 -0.0339 0.0138  667  ASP   B CA   
3242 C  C    . ASP   B 162 ? 0.6080 0.4235 0.5656 -0.0078 -0.0360 0.0075  667  ASP   B C    
3243 O  O    . ASP   B 162 ? 0.5249 0.3478 0.4855 -0.0049 -0.0313 0.0028  667  ASP   B O    
3244 C  CB   . ASP   B 162 ? 0.6299 0.4628 0.5894 -0.0256 -0.0344 0.0191  667  ASP   B CB   
3245 C  CG   . ASP   B 162 ? 0.6696 0.4840 0.6183 -0.0327 -0.0423 0.0238  667  ASP   B CG   
3246 O  OD1  . ASP   B 162 ? 0.6774 0.4734 0.6183 -0.0312 -0.0471 0.0206  667  ASP   B OD1  
3247 O  OD2  . ASP   B 162 ? 0.6690 0.4862 0.6164 -0.0396 -0.0440 0.0306  667  ASP   B OD2  
3248 N  N    . LYS   B 163 ? 0.5704 0.3653 0.5195 -0.0054 -0.0432 0.0072  668  LYS   B N    
3249 C  CA   . LYS   B 163 ? 0.5825 0.3624 0.5252 0.0014  -0.0460 0.0005  668  LYS   B CA   
3250 C  C    . LYS   B 163 ? 0.6295 0.4057 0.5663 -0.0052 -0.0460 -0.0009 668  LYS   B C    
3251 O  O    . LYS   B 163 ? 0.6018 0.3730 0.5354 0.0008  -0.0453 -0.0077 668  LYS   B O    
3252 C  CB   . LYS   B 163 ? 0.6304 0.3860 0.5635 0.0045  -0.0550 0.0010  668  LYS   B CB   
3253 C  CG   . LYS   B 163 ? 0.7398 0.4782 0.6653 0.0135  -0.0585 -0.0071 668  LYS   B CG   
3254 C  CD   . LYS   B 163 ? 0.7672 0.4854 0.6865 0.0217  -0.0663 -0.0083 668  LYS   B CD   
3255 C  CE   . LYS   B 163 ? 0.9005 0.5951 0.8074 0.0122  -0.0758 -0.0018 668  LYS   B CE   
3256 N  NZ   . LYS   B 163 ? 0.9797 0.6564 0.8815 0.0195  -0.0835 -0.0010 668  LYS   B NZ   
3257 N  N    . LYS   B 164 ? 0.5935 0.3728 0.5284 -0.0174 -0.0471 0.0055  669  LYS   B N    
3258 C  CA   . LYS   B 164 ? 0.5795 0.3567 0.5094 -0.0241 -0.0476 0.0044  669  LYS   B CA   
3259 C  C    . LYS   B 164 ? 0.5758 0.3706 0.5128 -0.0198 -0.0397 -0.0003 669  LYS   B C    
3260 O  O    . LYS   B 164 ? 0.5923 0.3825 0.5242 -0.0200 -0.0401 -0.0045 669  LYS   B O    
3261 C  CB   . LYS   B 164 ? 0.6285 0.4104 0.5572 -0.0380 -0.0495 0.0124  669  LYS   B CB   
3262 C  CG   . LYS   B 164 ? 0.6237 0.3868 0.5432 -0.0453 -0.0580 0.0182  669  LYS   B CG   
3263 C  CD   . LYS   B 164 ? 0.7274 0.5011 0.6477 -0.0594 -0.0583 0.0266  669  LYS   B CD   
3264 C  CE   . LYS   B 164 ? 0.8971 0.6543 0.8090 -0.0674 -0.0662 0.0339  669  LYS   B CE   
3265 N  NZ   . LYS   B 164 ? 0.9217 0.6919 0.8348 -0.0813 -0.0660 0.0425  669  LYS   B NZ   
3266 N  N    . PHE   B 165 ? 0.5154 0.3294 0.4635 -0.0162 -0.0330 0.0004  670  PHE   B N    
3267 C  CA   . PHE   B 165 ? 0.5410 0.3711 0.4960 -0.0118 -0.0256 -0.0034 670  PHE   B CA   
3268 C  C    . PHE   B 165 ? 0.5867 0.4145 0.5428 -0.0001 -0.0235 -0.0102 670  PHE   B C    
3269 O  O    . PHE   B 165 ? 0.5111 0.3416 0.4660 0.0036  -0.0204 -0.0151 670  PHE   B O    
3270 C  CB   . PHE   B 165 ? 0.5046 0.3548 0.4702 -0.0135 -0.0199 0.0004  670  PHE   B CB   
3271 C  CG   . PHE   B 165 ? 0.5311 0.3895 0.4972 -0.0235 -0.0199 0.0060  670  PHE   B CG   
3272 C  CD1  . PHE   B 165 ? 0.5465 0.4041 0.5081 -0.0292 -0.0209 0.0059  670  PHE   B CD1  
3273 C  CD2  . PHE   B 165 ? 0.6080 0.4763 0.5793 -0.0268 -0.0189 0.0110  670  PHE   B CD2  
3274 C  CE1  . PHE   B 165 ? 0.6037 0.4711 0.5667 -0.0382 -0.0209 0.0111  670  PHE   B CE1  
3275 C  CE2  . PHE   B 165 ? 0.6145 0.4924 0.5865 -0.0352 -0.0185 0.0159  670  PHE   B CE2  
3276 C  CZ   . PHE   B 165 ? 0.5659 0.4440 0.5343 -0.0409 -0.0195 0.0160  670  PHE   B CZ   
3277 N  N    . GLN   B 166 ? 0.5344 0.3585 0.4931 0.0059  -0.0252 -0.0104 671  GLN   B N    
3278 C  CA   . GLN   B 166 ? 0.6001 0.4272 0.5628 0.0175  -0.0225 -0.0164 671  GLN   B CA   
3279 C  C    . GLN   B 166 ? 0.5805 0.3905 0.5331 0.0237  -0.0264 -0.0228 671  GLN   B C    
3280 O  O    . GLN   B 166 ? 0.5491 0.3650 0.5033 0.0317  -0.0223 -0.0288 671  GLN   B O    
3281 C  CB   . GLN   B 166 ? 0.5500 0.3787 0.5184 0.0221  -0.0239 -0.0146 671  GLN   B CB   
3282 C  CG   . GLN   B 166 ? 0.5863 0.4316 0.5640 0.0171  -0.0201 -0.0093 671  GLN   B CG   
3283 C  CD   . GLN   B 166 ? 0.6983 0.5624 0.6869 0.0222  -0.0129 -0.0120 671  GLN   B CD   
3284 O  OE1  . GLN   B 166 ? 0.6666 0.5419 0.6583 0.0187  -0.0079 -0.0117 671  GLN   B OE1  
3285 N  NE2  . GLN   B 166 ? 0.6804 0.5478 0.6746 0.0307  -0.0127 -0.0146 671  GLN   B NE2  
3286 N  N    . ARG   B 167 ? 0.5634 0.3522 0.5053 0.0202  -0.0344 -0.0216 672  ARG   B N    
3287 C  CA   . ARG   B 167 ? 0.5705 0.3393 0.5012 0.0262  -0.0397 -0.0280 672  ARG   B CA   
3288 C  C    . ARG   B 167 ? 0.6247 0.3784 0.5442 0.0159  -0.0453 -0.0261 672  ARG   B C    
3289 O  O    . ARG   B 167 ? 0.6060 0.3373 0.5155 0.0136  -0.0539 -0.0251 672  ARG   B O    
3290 C  CB   . ARG   B 167 ? 0.7033 0.4568 0.6310 0.0343  -0.0458 -0.0293 672  ARG   B CB   
3291 C  CG   . ARG   B 167 ? 0.6672 0.4366 0.6065 0.0451  -0.0408 -0.0317 672  ARG   B CG   
3292 C  CD   . ARG   B 167 ? 0.7257 0.4797 0.6618 0.0535  -0.0477 -0.0327 672  ARG   B CD   
3293 N  NE   . ARG   B 167 ? 0.7674 0.4970 0.6901 0.0593  -0.0546 -0.0386 672  ARG   B NE   
3294 C  CZ   . ARG   B 167 ? 0.8447 0.5731 0.7656 0.0720  -0.0534 -0.0476 672  ARG   B CZ   
3295 N  NH1  . ARG   B 167 ? 0.8401 0.5915 0.7724 0.0801  -0.0453 -0.0513 672  ARG   B NH1  
3296 N  NH2  . ARG   B 167 ? 0.8229 0.5264 0.7298 0.0764  -0.0607 -0.0529 672  ARG   B NH2  
3297 N  N    . PRO   B 168 ? 0.5885 0.3535 0.5091 0.0097  -0.0412 -0.0257 673  PRO   B N    
3298 C  CA   . PRO   B 168 ? 0.5682 0.3235 0.4806 -0.0022 -0.0463 -0.0223 673  PRO   B CA   
3299 C  C    . PRO   B 168 ? 0.6608 0.3897 0.5585 -0.0015 -0.0548 -0.0270 673  PRO   B C    
3300 O  O    . PRO   B 168 ? 0.7087 0.4241 0.5991 -0.0120 -0.0617 -0.0226 673  PRO   B O    
3301 C  CB   . PRO   B 168 ? 0.5955 0.3697 0.5126 -0.0057 -0.0396 -0.0227 673  PRO   B CB   
3302 C  CG   . PRO   B 168 ? 0.6214 0.4086 0.5448 0.0055  -0.0322 -0.0282 673  PRO   B CG   
3303 C  CD   . PRO   B 168 ? 0.5723 0.3580 0.5006 0.0140  -0.0322 -0.0289 673  PRO   B CD   
3304 N  N    . HIS   B 169 ? 0.6360 0.3571 0.5289 0.0104  -0.0547 -0.0356 674  HIS   B N    
3305 C  CA   . HIS   B 169 ? 0.6848 0.3786 0.5624 0.0119  -0.0635 -0.0409 674  HIS   B CA   
3306 C  C    . HIS   B 169 ? 0.7093 0.3805 0.5809 0.0153  -0.0718 -0.0400 674  HIS   B C    
3307 O  O    . HIS   B 169 ? 0.7828 0.4284 0.6410 0.0183  -0.0799 -0.0449 674  HIS   B O    
3308 C  CB   . HIS   B 169 ? 0.7214 0.4159 0.5946 0.0235  -0.0602 -0.0512 674  HIS   B CB   
3309 C  CG   . HIS   B 169 ? 0.7166 0.4212 0.5879 0.0177  -0.0567 -0.0525 674  HIS   B CG   
3310 N  ND1  . HIS   B 169 ? 0.7312 0.4605 0.6114 0.0212  -0.0469 -0.0537 674  HIS   B ND1  
3311 C  CD2  . HIS   B 169 ? 0.7322 0.4258 0.5937 0.0082  -0.0622 -0.0523 674  HIS   B CD2  
3312 C  CE1  . HIS   B 169 ? 0.6984 0.4311 0.5740 0.0148  -0.0464 -0.0542 674  HIS   B CE1  
3313 N  NE2  . HIS   B 169 ? 0.7738 0.4856 0.6383 0.0070  -0.0556 -0.0537 674  HIS   B NE2  
3314 N  N    . ASP   B 170 ? 0.6983 0.3771 0.5786 0.0150  -0.0705 -0.0339 675  ASP   B N    
3315 C  CA   . ASP   B 170 ? 0.7697 0.4263 0.6434 0.0150  -0.0794 -0.0306 675  ASP   B CA   
3316 C  C    . ASP   B 170 ? 0.8178 0.4600 0.6834 -0.0011 -0.0870 -0.0227 675  ASP   B C    
3317 O  O    . ASP   B 170 ? 0.8113 0.4319 0.6692 -0.0031 -0.0955 -0.0192 675  ASP   B O    
3318 C  CB   . ASP   B 170 ? 0.7368 0.4068 0.6217 0.0193  -0.0760 -0.0262 675  ASP   B CB   
3319 C  CG   . ASP   B 170 ? 0.7827 0.4608 0.6738 0.0362  -0.0716 -0.0339 675  ASP   B CG   
3320 O  OD1  . ASP   B 170 ? 0.7667 0.4424 0.6539 0.0450  -0.0701 -0.0427 675  ASP   B OD1  
3321 O  OD2  . ASP   B 170 ? 0.7569 0.4450 0.6570 0.0405  -0.0696 -0.0310 675  ASP   B OD2  
3322 N  N    . TYR   B 171 ? 0.7365 0.3909 0.6041 -0.0128 -0.0841 -0.0194 676  TYR   B N    
3323 C  CA   . TYR   B 171 ? 0.7863 0.4319 0.6482 -0.0291 -0.0904 -0.0113 676  TYR   B CA   
3324 C  C    . TYR   B 171 ? 0.8003 0.4362 0.6529 -0.0355 -0.0943 -0.0149 676  TYR   B C    
3325 O  O    . TYR   B 171 ? 0.7589 0.4082 0.6145 -0.0315 -0.0884 -0.0206 676  TYR   B O    
3326 C  CB   . TYR   B 171 ? 0.7577 0.4297 0.6317 -0.0391 -0.0841 -0.0023 676  TYR   B CB   
3327 C  CG   . TYR   B 171 ? 0.7527 0.4371 0.6364 -0.0337 -0.0798 0.0014  676  TYR   B CG   
3328 C  CD1  . TYR   B 171 ? 0.7325 0.4307 0.6251 -0.0205 -0.0726 -0.0042 676  TYR   B CD1  
3329 C  CD2  . TYR   B 171 ? 0.7480 0.4278 0.6305 -0.0416 -0.0839 0.0102  676  TYR   B CD2  
3330 C  CE1  . TYR   B 171 ? 0.7191 0.4277 0.6200 -0.0159 -0.0695 -0.0012 676  TYR   B CE1  
3331 C  CE2  . TYR   B 171 ? 0.7411 0.4308 0.6311 -0.0364 -0.0808 0.0132  676  TYR   B CE2  
3332 C  CZ   . TYR   B 171 ? 0.7490 0.4528 0.6483 -0.0236 -0.0739 0.0073  676  TYR   B CZ   
3333 O  OH   . TYR   B 171 ? 0.8533 0.5672 0.7602 -0.0190 -0.0713 0.0102  676  TYR   B OH   
3334 N  N    . SER   B 172 ? 0.8152 0.4276 0.6560 -0.0460 -0.1046 -0.0113 677  SER   B N    
3335 C  CA   . SER   B 172 ? 0.8431 0.4453 0.6746 -0.0547 -0.1097 -0.0137 677  SER   B CA   
3336 C  C    . SER   B 172 ? 0.8414 0.4484 0.6737 -0.0739 -0.1132 -0.0031 677  SER   B C    
3337 O  O    . SER   B 172 ? 0.9548 0.5463 0.7819 -0.0817 -0.1203 0.0040  677  SER   B O    
3338 C  CB   . SER   B 172 ? 0.9412 0.5077 0.7557 -0.0496 -0.1204 -0.0208 677  SER   B CB   
3339 O  OG   . SER   B 172 ? 1.0420 0.6086 0.8544 -0.0342 -0.1166 -0.0324 677  SER   B OG   
3340 N  N    . PRO   B 173 ? 0.8219 0.4508 0.6607 -0.0820 -0.1084 -0.0013 678  PRO   B N    
3341 C  CA   . PRO   B 173 ? 0.8100 0.4603 0.6559 -0.0747 -0.0996 -0.0075 678  PRO   B CA   
3342 C  C    . PRO   B 173 ? 0.7056 0.3807 0.5659 -0.0658 -0.0889 -0.0063 678  PRO   B C    
3343 O  O    . PRO   B 173 ? 0.7046 0.3864 0.5711 -0.0689 -0.0876 0.0008  678  PRO   B O    
3344 C  CB   . PRO   B 173 ? 0.7842 0.4491 0.6327 -0.0894 -0.0999 -0.0026 678  PRO   B CB   
3345 C  CG   . PRO   B 173 ? 0.8276 0.4739 0.6677 -0.1040 -0.1103 0.0042  678  PRO   B CG   
3346 C  CD   . PRO   B 173 ? 0.8294 0.4632 0.6684 -0.1005 -0.1124 0.0081  678  PRO   B CD   
3347 N  N    . PRO   B 174 ? 0.7080 0.3964 0.5732 -0.0548 -0.0813 -0.0133 679  PRO   B N    
3348 C  CA   . PRO   B 174 ? 0.6617 0.3733 0.5405 -0.0471 -0.0715 -0.0122 679  PRO   B CA   
3349 C  C    . PRO   B 174 ? 0.6795 0.4168 0.5693 -0.0564 -0.0660 -0.0048 679  PRO   B C    
3350 O  O    . PRO   B 174 ? 0.6401 0.3829 0.5286 -0.0661 -0.0676 -0.0026 679  PRO   B O    
3351 C  CB   . PRO   B 174 ? 0.6732 0.3903 0.5523 -0.0346 -0.0658 -0.0214 679  PRO   B CB   
3352 C  CG   . PRO   B 174 ? 0.6759 0.3825 0.5443 -0.0392 -0.0706 -0.0256 679  PRO   B CG   
3353 C  CD   . PRO   B 174 ? 0.6995 0.3807 0.5568 -0.0484 -0.0818 -0.0226 679  PRO   B CD   
3354 N  N    . PHE   B 175 ? 0.6344 0.3878 0.5351 -0.0527 -0.0598 -0.0014 680  PHE   B N    
3355 C  CA   . PHE   B 175 ? 0.6031 0.3818 0.5147 -0.0587 -0.0539 0.0045  680  PHE   B CA   
3356 C  C    . PHE   B 175 ? 0.6241 0.4192 0.5402 -0.0559 -0.0478 0.0007  680  PHE   B C    
3357 O  O    . PHE   B 175 ? 0.5964 0.3921 0.5129 -0.0456 -0.0439 -0.0057 680  PHE   B O    
3358 C  CB   . PHE   B 175 ? 0.6323 0.4218 0.5531 -0.0532 -0.0490 0.0072  680  PHE   B CB   
3359 C  CG   . PHE   B 175 ? 0.6287 0.4344 0.5563 -0.0619 -0.0472 0.0154  680  PHE   B CG   
3360 C  CD1  . PHE   B 175 ? 0.6535 0.4525 0.5760 -0.0738 -0.0533 0.0220  680  PHE   B CD1  
3361 C  CD2  . PHE   B 175 ? 0.5991 0.4265 0.5378 -0.0580 -0.0395 0.0164  680  PHE   B CD2  
3362 C  CE1  . PHE   B 175 ? 0.6384 0.4544 0.5670 -0.0812 -0.0510 0.0294  680  PHE   B CE1  
3363 C  CE2  . PHE   B 175 ? 0.6545 0.4971 0.5988 -0.0648 -0.0377 0.0232  680  PHE   B CE2  
3364 C  CZ   . PHE   B 175 ? 0.6266 0.4645 0.5660 -0.0762 -0.0432 0.0296  680  PHE   B CZ   
3365 N  N    . ARG   B 176 ? 0.5830 0.3922 0.5025 -0.0650 -0.0471 0.0049  681  ARG   B N    
3366 C  CA   . ARG   B 176 ? 0.5732 0.3981 0.4966 -0.0630 -0.0421 0.0023  681  ARG   B CA   
3367 C  C    . ARG   B 176 ? 0.5074 0.3555 0.4433 -0.0610 -0.0345 0.0059  681  ARG   B C    
3368 O  O    . ARG   B 176 ? 0.5040 0.3633 0.4449 -0.0682 -0.0346 0.0122  681  ARG   B O    
3369 C  CB   . ARG   B 176 ? 0.5317 0.3576 0.4507 -0.0734 -0.0467 0.0041  681  ARG   B CB   
3370 C  CG   . ARG   B 176 ? 0.6343 0.4350 0.5398 -0.0770 -0.0556 0.0007  681  ARG   B CG   
3371 C  CD   . ARG   B 176 ? 0.6593 0.4619 0.5618 -0.0905 -0.0614 0.0047  681  ARG   B CD   
3372 N  NE   . ARG   B 176 ? 0.6418 0.4538 0.5502 -0.1004 -0.0623 0.0135  681  ARG   B NE   
3373 C  CZ   . ARG   B 176 ? 0.6351 0.4571 0.5452 -0.1128 -0.0654 0.0190  681  ARG   B CZ   
3374 N  NH1  . ARG   B 176 ? 0.7109 0.5345 0.6175 -0.1175 -0.0686 0.0169  681  ARG   B NH1  
3375 N  NH2  . ARG   B 176 ? 0.6723 0.5046 0.5880 -0.1207 -0.0653 0.0270  681  ARG   B NH2  
3376 N  N    . PHE   B 177 ? 0.4478 0.3032 0.3884 -0.0512 -0.0282 0.0019  682  PHE   B N    
3377 C  CA   . PHE   B 177 ? 0.4216 0.2966 0.3732 -0.0486 -0.0216 0.0047  682  PHE   B CA   
3378 C  C    . PHE   B 177 ? 0.4417 0.3253 0.3959 -0.0415 -0.0160 0.0006  682  PHE   B C    
3379 O  O    . PHE   B 177 ? 0.4452 0.3199 0.3945 -0.0354 -0.0155 -0.0048 682  PHE   B O    
3380 C  CB   . PHE   B 177 ? 0.4935 0.3672 0.4496 -0.0444 -0.0202 0.0061  682  PHE   B CB   
3381 C  CG   . PHE   B 177 ? 0.5027 0.3639 0.4558 -0.0353 -0.0201 0.0007  682  PHE   B CG   
3382 C  CD1  . PHE   B 177 ? 0.5318 0.3727 0.4760 -0.0354 -0.0264 -0.0011 682  PHE   B CD1  
3383 C  CD2  . PHE   B 177 ? 0.5193 0.3892 0.4788 -0.0268 -0.0140 -0.0023 682  PHE   B CD2  
3384 C  CE1  . PHE   B 177 ? 0.5212 0.3518 0.4630 -0.0258 -0.0264 -0.0065 682  PHE   B CE1  
3385 C  CE2  . PHE   B 177 ? 0.5196 0.3807 0.4774 -0.0182 -0.0137 -0.0072 682  PHE   B CE2  
3386 C  CZ   . PHE   B 177 ? 0.5187 0.3606 0.4677 -0.0171 -0.0198 -0.0096 682  PHE   B CZ   
3387 N  N    . GLY   B 178 ? 0.4348 0.3360 0.3967 -0.0422 -0.0116 0.0033  683  GLY   B N    
3388 C  CA   . GLY   B 178 ? 0.4360 0.3453 0.4000 -0.0366 -0.0066 0.0007  683  GLY   B CA   
3389 C  C    . GLY   B 178 ? 0.4414 0.3667 0.4151 -0.0348 -0.0017 0.0037  683  GLY   B C    
3390 O  O    . GLY   B 178 ? 0.4079 0.3396 0.3863 -0.0380 -0.0022 0.0075  683  GLY   B O    
3391 N  N    . THR   B 179 ? 0.3840 0.3152 0.3597 -0.0296 0.0027  0.0018  684  THR   B N    
3392 C  CA   . THR   B 179 ? 0.4211 0.3654 0.4046 -0.0277 0.0068  0.0043  684  THR   B CA   
3393 C  C    . THR   B 179 ? 0.4278 0.3785 0.4094 -0.0276 0.0079  0.0043  684  THR   B C    
3394 O  O    . THR   B 179 ? 0.4420 0.3876 0.4166 -0.0290 0.0057  0.0023  684  THR   B O    
3395 C  CB   . THR   B 179 ? 0.3932 0.3378 0.3816 -0.0216 0.0109  0.0029  684  THR   B CB   
3396 O  OG1  . THR   B 179 ? 0.4065 0.3618 0.4020 -0.0206 0.0136  0.0054  684  THR   B OG1  
3397 C  CG2  . THR   B 179 ? 0.4445 0.3863 0.4298 -0.0171 0.0138  -0.0006 684  THR   B CG2  
3398 N  N    . VAL   B 180 ? 0.3972 0.3584 0.3846 -0.0257 0.0107  0.0064  685  VAL   B N    
3399 C  CA   . VAL   B 180 ? 0.3627 0.3285 0.3484 -0.0238 0.0123  0.0065  685  VAL   B CA   
3400 C  C    . VAL   B 180 ? 0.4334 0.3962 0.4193 -0.0188 0.0166  0.0047  685  VAL   B C    
3401 O  O    . VAL   B 180 ? 0.3979 0.3629 0.3899 -0.0163 0.0191  0.0054  685  VAL   B O    
3402 C  CB   . VAL   B 180 ? 0.4313 0.4087 0.4225 -0.0237 0.0126  0.0097  685  VAL   B CB   
3403 C  CG1  . VAL   B 180 ? 0.3840 0.3644 0.3728 -0.0211 0.0139  0.0102  685  VAL   B CG1  
3404 C  CG2  . VAL   B 180 ? 0.4334 0.4170 0.4253 -0.0289 0.0088  0.0118  685  VAL   B CG2  
3405 N  N    . PRO   B 181 ? 0.4274 0.3862 0.4068 -0.0174 0.0174  0.0024  686  PRO   B N    
3406 C  CA   . PRO   B 181 ? 0.4282 0.3851 0.4076 -0.0131 0.0217  0.0006  686  PRO   B CA   
3407 C  C    . PRO   B 181 ? 0.4360 0.3996 0.4197 -0.0113 0.0252  0.0034  686  PRO   B C    
3408 O  O    . PRO   B 181 ? 0.3499 0.3183 0.3352 -0.0123 0.0242  0.0063  686  PRO   B O    
3409 C  CB   . PRO   B 181 ? 0.4499 0.4018 0.4197 -0.0124 0.0213  -0.0026 686  PRO   B CB   
3410 C  CG   . PRO   B 181 ? 0.4442 0.3979 0.4097 -0.0163 0.0174  -0.0011 686  PRO   B CG   
3411 C  CD   . PRO   B 181 ? 0.4145 0.3710 0.3858 -0.0199 0.0143  0.0013  686  PRO   B CD   
3412 N  N    . ASN   B 182 ? 0.3735 0.3372 0.3594 -0.0085 0.0292  0.0025  687  ASN   B N    
3413 C  CA   . ASN   B 182 ? 0.3725 0.3406 0.3609 -0.0073 0.0328  0.0051  687  ASN   B CA   
3414 C  C    . ASN   B 182 ? 0.4042 0.3752 0.4006 -0.0075 0.0328  0.0078  687  ASN   B C    
3415 O  O    . ASN   B 182 ? 0.3979 0.3708 0.3958 -0.0073 0.0348  0.0104  687  ASN   B O    
3416 C  CB   . ASN   B 182 ? 0.3905 0.3600 0.3722 -0.0081 0.0326  0.0070  687  ASN   B CB   
3417 C  CG   . ASN   B 182 ? 0.4927 0.4595 0.4653 -0.0076 0.0327  0.0040  687  ASN   B CG   
3418 O  OD1  . ASN   B 182 ? 0.4526 0.4171 0.4241 -0.0056 0.0345  0.0004  687  ASN   B OD1  
3419 N  ND2  . ASN   B 182 ? 0.4953 0.4623 0.4610 -0.0089 0.0305  0.0049  687  ASN   B ND2  
3420 N  N    . GLY   B 183 ? 0.3687 0.3394 0.3697 -0.0080 0.0306  0.0074  688  GLY   B N    
3421 C  CA   . GLY   B 183 ? 0.3596 0.3325 0.3675 -0.0076 0.0306  0.0090  688  GLY   B CA   
3422 C  C    . GLY   B 183 ? 0.3820 0.3541 0.3952 -0.0066 0.0316  0.0073  688  GLY   B C    
3423 O  O    . GLY   B 183 ? 0.3737 0.3440 0.3860 -0.0056 0.0328  0.0050  688  GLY   B O    
3424 N  N    . SER   B 184 ? 0.3560 0.3297 0.3748 -0.0065 0.0307  0.0082  689  SER   B N    
3425 C  CA   . SER   B 184 ? 0.3821 0.3558 0.4064 -0.0056 0.0312  0.0070  689  SER   B CA   
3426 C  C    . SER   B 184 ? 0.4037 0.3746 0.4269 -0.0053 0.0295  0.0050  689  SER   B C    
3427 O  O    . SER   B 184 ? 0.3613 0.3314 0.3873 -0.0037 0.0302  0.0033  689  SER   B O    
3428 C  CB   . SER   B 184 ? 0.3944 0.3697 0.4234 -0.0055 0.0299  0.0080  689  SER   B CB   
3429 O  OG   . SER   B 184 ? 0.3680 0.3445 0.3953 -0.0059 0.0273  0.0084  689  SER   B OG   
3430 N  N    . THR   B 185 ? 0.3597 0.3290 0.3787 -0.0071 0.0269  0.0053  690  THR   B N    
3431 C  CA   . THR   B 185 ? 0.3811 0.3456 0.3980 -0.0077 0.0244  0.0040  690  THR   B CA   
3432 C  C    . THR   B 185 ? 0.3748 0.3340 0.3874 -0.0060 0.0251  0.0013  690  THR   B C    
3433 O  O    . THR   B 185 ? 0.3600 0.3154 0.3735 -0.0038 0.0244  -0.0006 690  THR   B O    
3434 C  CB   . THR   B 185 ? 0.3938 0.3585 0.4072 -0.0113 0.0213  0.0057  690  THR   B CB   
3435 O  OG1  . THR   B 185 ? 0.3924 0.3631 0.4100 -0.0118 0.0208  0.0076  690  THR   B OG1  
3436 C  CG2  . THR   B 185 ? 0.3463 0.3038 0.3560 -0.0130 0.0181  0.0050  690  THR   B CG2  
3437 N  N    . GLU   B 186 ? 0.3792 0.3383 0.3868 -0.0062 0.0262  0.0008  691  GLU   B N    
3438 C  CA   . GLU   B 186 ? 0.4286 0.3830 0.4312 -0.0038 0.0270  -0.0026 691  GLU   B CA   
3439 C  C    . GLU   B 186 ? 0.4160 0.3741 0.4233 0.0001  0.0308  -0.0041 691  GLU   B C    
3440 O  O    . GLU   B 186 ? 0.3995 0.3544 0.4057 0.0036  0.0308  -0.0074 691  GLU   B O    
3441 C  CB   . GLU   B 186 ? 0.4292 0.3834 0.4246 -0.0048 0.0275  -0.0029 691  GLU   B CB   
3442 C  CG   . GLU   B 186 ? 0.4668 0.4155 0.4558 -0.0016 0.0280  -0.0073 691  GLU   B CG   
3443 C  CD   . GLU   B 186 ? 0.4516 0.4002 0.4324 -0.0019 0.0288  -0.0084 691  GLU   B CD   
3444 O  OE1  . GLU   B 186 ? 0.4684 0.4227 0.4495 -0.0037 0.0303  -0.0053 691  GLU   B OE1  
3445 O  OE2  . GLU   B 186 ? 0.4739 0.4157 0.4471 0.0000  0.0274  -0.0125 691  GLU   B OE2  
3446 N  N    . ARG   B 187 ? 0.3607 0.3258 0.3734 -0.0004 0.0337  -0.0017 692  ARG   B N    
3447 C  CA   . ARG   B 187 ? 0.3704 0.3409 0.3889 0.0021  0.0372  -0.0025 692  ARG   B CA   
3448 C  C    . ARG   B 187 ? 0.4055 0.3750 0.4292 0.0045  0.0356  -0.0042 692  ARG   B C    
3449 O  O    . ARG   B 187 ? 0.4076 0.3795 0.4334 0.0083  0.0373  -0.0068 692  ARG   B O    
3450 C  CB   . ARG   B 187 ? 0.4029 0.3792 0.4266 -0.0002 0.0392  0.0010  692  ARG   B CB   
3451 C  CG   . ARG   B 187 ? 0.4379 0.4214 0.4674 0.0008  0.0430  0.0011  692  ARG   B CG   
3452 C  CD   . ARG   B 187 ? 0.4681 0.4549 0.4926 0.0016  0.0468  0.0006  692  ARG   B CD   
3453 N  NE   . ARG   B 187 ? 0.5219 0.5174 0.5517 0.0034  0.0507  -0.0004 692  ARG   B NE   
3454 C  CZ   . ARG   B 187 ? 0.6316 0.6293 0.6625 0.0081  0.0515  -0.0044 692  ARG   B CZ   
3455 N  NH1  . ARG   B 187 ? 0.6118 0.6012 0.6382 0.0112  0.0481  -0.0078 692  ARG   B NH1  
3456 N  NH2  . ARG   B 187 ? 0.6548 0.6633 0.6913 0.0098  0.0555  -0.0049 692  ARG   B NH2  
3457 N  N    . ASN   B 188 ? 0.3871 0.3544 0.4132 0.0027  0.0324  -0.0026 693  ASN   B N    
3458 C  CA   . ASN   B 188 ? 0.4130 0.3791 0.4435 0.0047  0.0303  -0.0036 693  ASN   B CA   
3459 C  C    . ASN   B 188 ? 0.3930 0.3513 0.4183 0.0076  0.0279  -0.0066 693  ASN   B C    
3460 O  O    . ASN   B 188 ? 0.4371 0.3956 0.4655 0.0118  0.0276  -0.0088 693  ASN   B O    
3461 C  CB   . ASN   B 188 ? 0.4086 0.3738 0.4406 0.0019  0.0273  -0.0012 693  ASN   B CB   
3462 C  CG   . ASN   B 188 ? 0.4802 0.4445 0.5163 0.0037  0.0249  -0.0018 693  ASN   B CG   
3463 O  OD1  . ASN   B 188 ? 0.5029 0.4604 0.5351 0.0045  0.0218  -0.0024 693  ASN   B OD1  
3464 N  ND2  . ASN   B 188 ? 0.4475 0.4180 0.4909 0.0044  0.0260  -0.0015 693  ASN   B ND2  
3465 N  N    . ILE   B 189 ? 0.3821 0.3331 0.3995 0.0055  0.0255  -0.0067 694  ILE   B N    
3466 C  CA   . ILE   B 189 ? 0.4232 0.3640 0.4343 0.0078  0.0222  -0.0096 694  ILE   B CA   
3467 C  C    . ILE   B 189 ? 0.3931 0.3348 0.4025 0.0134  0.0250  -0.0139 694  ILE   B C    
3468 O  O    . ILE   B 189 ? 0.3907 0.3280 0.3997 0.0185  0.0236  -0.0171 694  ILE   B O    
3469 C  CB   . ILE   B 189 ? 0.4285 0.3618 0.4315 0.0031  0.0188  -0.0085 694  ILE   B CB   
3470 C  CG1  . ILE   B 189 ? 0.4665 0.4005 0.4716 -0.0018 0.0160  -0.0044 694  ILE   B CG1  
3471 C  CG2  . ILE   B 189 ? 0.4320 0.3526 0.4269 0.0051  0.0150  -0.0119 694  ILE   B CG2  
3472 C  CD1  . ILE   B 189 ? 0.5059 0.4356 0.5047 -0.0074 0.0126  -0.0025 694  ILE   B CD1  
3473 N  N    . ARG   B 190 ? 0.3848 0.3327 0.3929 0.0129  0.0291  -0.0140 695  ARG   B N    
3474 C  CA   . ARG   B 190 ? 0.4216 0.3726 0.4277 0.0181  0.0325  -0.0179 695  ARG   B CA   
3475 C  C    . ARG   B 190 ? 0.4315 0.3910 0.4466 0.0228  0.0350  -0.0191 695  ARG   B C    
3476 O  O    . ARG   B 190 ? 0.4630 0.4229 0.4770 0.0292  0.0359  -0.0235 695  ARG   B O    
3477 C  CB   . ARG   B 190 ? 0.4305 0.3882 0.4339 0.0159  0.0366  -0.0166 695  ARG   B CB   
3478 C  CG   . ARG   B 190 ? 0.4284 0.3915 0.4289 0.0210  0.0409  -0.0204 695  ARG   B CG   
3479 C  CD   . ARG   B 190 ? 0.4693 0.4414 0.4688 0.0180  0.0456  -0.0176 695  ARG   B CD   
3480 N  NE   . ARG   B 190 ? 0.4987 0.4645 0.4893 0.0144  0.0435  -0.0165 695  ARG   B NE   
3481 C  CZ   . ARG   B 190 ? 0.5405 0.5015 0.5207 0.0163  0.0430  -0.0200 695  ARG   B CZ   
3482 N  NH1  . ARG   B 190 ? 0.5579 0.5187 0.5346 0.0225  0.0445  -0.0254 695  ARG   B NH1  
3483 N  NH2  . ARG   B 190 ? 0.5412 0.4981 0.5143 0.0123  0.0407  -0.0185 695  ARG   B NH2  
3484 N  N    . ASN   B 191 ? 0.4210 0.3879 0.4451 0.0201  0.0360  -0.0156 696  ASN   B N    
3485 C  CA   . ASN   B 191 ? 0.4597 0.4360 0.4931 0.0238  0.0379  -0.0165 696  ASN   B CA   
3486 C  C    . ASN   B 191 ? 0.4630 0.4331 0.4979 0.0280  0.0335  -0.0185 696  ASN   B C    
3487 O  O    . ASN   B 191 ? 0.4678 0.4425 0.5064 0.0342  0.0343  -0.0216 696  ASN   B O    
3488 C  CB   . ASN   B 191 ? 0.5087 0.4939 0.5507 0.0191  0.0397  -0.0123 696  ASN   B CB   
3489 C  CG   . ASN   B 191 ? 0.6289 0.6232 0.6718 0.0167  0.0449  -0.0105 696  ASN   B CG   
3490 O  OD1  . ASN   B 191 ? 0.6482 0.6437 0.6925 0.0115  0.0454  -0.0067 696  ASN   B OD1  
3491 N  ND2  . ASN   B 191 ? 0.6567 0.6568 0.6978 0.0206  0.0486  -0.0133 696  ASN   B ND2  
3492 N  N    . ASN   B 192 ? 0.4149 0.3752 0.4469 0.0248  0.0286  -0.0164 697  ASN   B N    
3493 C  CA   . ASN   B 192 ? 0.4318 0.3866 0.4655 0.0279  0.0241  -0.0170 697  ASN   B CA   
3494 C  C    . ASN   B 192 ? 0.4649 0.4058 0.4898 0.0321  0.0200  -0.0204 697  ASN   B C    
3495 O  O    . ASN   B 192 ? 0.4702 0.4080 0.4967 0.0379  0.0172  -0.0225 697  ASN   B O    
3496 C  CB   . ASN   B 192 ? 0.3968 0.3485 0.4314 0.0223  0.0209  -0.0128 697  ASN   B CB   
3497 C  CG   . ASN   B 192 ? 0.4888 0.4519 0.5322 0.0195  0.0234  -0.0102 697  ASN   B CG   
3498 O  OD1  . ASN   B 192 ? 0.5094 0.4824 0.5606 0.0220  0.0260  -0.0112 697  ASN   B OD1  
3499 N  ND2  . ASN   B 192 ? 0.5077 0.4697 0.5500 0.0141  0.0222  -0.0069 697  ASN   B ND2  
3500 N  N    . TYR   B 193 ? 0.4305 0.3623 0.4458 0.0295  0.0189  -0.0210 698  TYR   B N    
3501 C  CA   . TYR   B 193 ? 0.4161 0.3314 0.4215 0.0318  0.0136  -0.0237 698  TYR   B CA   
3502 C  C    . TYR   B 193 ? 0.4267 0.3387 0.4241 0.0339  0.0153  -0.0279 698  TYR   B C    
3503 O  O    . TYR   B 193 ? 0.4508 0.3559 0.4406 0.0285  0.0136  -0.0269 698  TYR   B O    
3504 C  CB   . TYR   B 193 ? 0.4654 0.3703 0.4658 0.0245  0.0084  -0.0195 698  TYR   B CB   
3505 C  CG   . TYR   B 193 ? 0.5368 0.4479 0.5444 0.0209  0.0079  -0.0147 698  TYR   B CG   
3506 C  CD1  . TYR   B 193 ? 0.5247 0.4345 0.5363 0.0249  0.0053  -0.0146 698  TYR   B CD1  
3507 C  CD2  . TYR   B 193 ? 0.5036 0.4219 0.5136 0.0141  0.0097  -0.0106 698  TYR   B CD2  
3508 C  CE1  . TYR   B 193 ? 0.5709 0.4865 0.5882 0.0216  0.0046  -0.0106 698  TYR   B CE1  
3509 C  CE2  . TYR   B 193 ? 0.5327 0.4566 0.5483 0.0115  0.0092  -0.0071 698  TYR   B CE2  
3510 C  CZ   . TYR   B 193 ? 0.6097 0.5322 0.6288 0.0150  0.0067  -0.0071 698  TYR   B CZ   
3511 O  OH   . TYR   B 193 ? 0.6496 0.5777 0.6733 0.0125  0.0060  -0.0038 698  TYR   B OH   
3512 N  N    . PRO   B 194 ? 0.4188 0.3362 0.4172 0.0418  0.0184  -0.0328 699  PRO   B N    
3513 C  CA   . PRO   B 194 ? 0.4395 0.3563 0.4300 0.0439  0.0210  -0.0368 699  PRO   B CA   
3514 C  C    . PRO   B 194 ? 0.4403 0.3380 0.4176 0.0435  0.0151  -0.0398 699  PRO   B C    
3515 O  O    . PRO   B 194 ? 0.4445 0.3401 0.4146 0.0398  0.0158  -0.0402 699  PRO   B O    
3516 C  CB   . PRO   B 194 ? 0.4469 0.3743 0.4419 0.0535  0.0253  -0.0417 699  PRO   B CB   
3517 C  CG   . PRO   B 194 ? 0.4483 0.3888 0.4568 0.0529  0.0273  -0.0381 699  PRO   B CG   
3518 C  CD   . PRO   B 194 ? 0.4259 0.3551 0.4344 0.0483  0.0212  -0.0342 699  PRO   B CD   
3519 N  N    . TYR   B 195 ? 0.4354 0.3183 0.4089 0.0468  0.0088  -0.0415 700  TYR   B N    
3520 C  CA   . TYR   B 195 ? 0.4739 0.3365 0.4340 0.0456  0.0024  -0.0442 700  TYR   B CA   
3521 C  C    . TYR   B 195 ? 0.4787 0.3362 0.4356 0.0339  -0.0007 -0.0384 700  TYR   B C    
3522 O  O    . TYR   B 195 ? 0.4696 0.3203 0.4175 0.0301  -0.0024 -0.0398 700  TYR   B O    
3523 C  CB   . TYR   B 195 ? 0.4884 0.3348 0.4446 0.0516  -0.0042 -0.0467 700  TYR   B CB   
3524 C  CG   . TYR   B 195 ? 0.5306 0.3541 0.4721 0.0515  -0.0114 -0.0504 700  TYR   B CG   
3525 C  CD1  . TYR   B 195 ? 0.5382 0.3562 0.4710 0.0594  -0.0111 -0.0584 700  TYR   B CD1  
3526 C  CD2  . TYR   B 195 ? 0.6016 0.4089 0.5373 0.0431  -0.0187 -0.0460 700  TYR   B CD2  
3527 C  CE1  . TYR   B 195 ? 0.6308 0.4257 0.5490 0.0591  -0.0186 -0.0623 700  TYR   B CE1  
3528 C  CE2  . TYR   B 195 ? 0.6440 0.4290 0.5659 0.0420  -0.0261 -0.0492 700  TYR   B CE2  
3529 C  CZ   . TYR   B 195 ? 0.6629 0.4410 0.5759 0.0501  -0.0263 -0.0575 700  TYR   B CZ   
3530 O  OH   . TYR   B 195 ? 0.7389 0.4931 0.6373 0.0488  -0.0343 -0.0611 700  TYR   B OH   
3531 N  N    . MET   B 196 ? 0.4785 0.3405 0.4426 0.0283  -0.0013 -0.0322 701  MET   B N    
3532 C  CA   . MET   B 196 ? 0.4943 0.3561 0.4572 0.0176  -0.0031 -0.0266 701  MET   B CA   
3533 C  C    . MET   B 196 ? 0.4594 0.3323 0.4225 0.0143  0.0016  -0.0263 701  MET   B C    
3534 O  O    . MET   B 196 ? 0.5015 0.3695 0.4579 0.0081  -0.0011 -0.0253 701  MET   B O    
3535 C  CB   . MET   B 196 ? 0.4190 0.2886 0.3910 0.0139  -0.0027 -0.0207 701  MET   B CB   
3536 C  CG   . MET   B 196 ? 0.5143 0.3877 0.4869 0.0038  -0.0038 -0.0148 701  MET   B CG   
3537 S  SD   . MET   B 196 ? 0.5651 0.4506 0.5488 0.0027  -0.0017 -0.0097 701  MET   B SD   
3538 C  CE   . MET   B 196 ? 0.5408 0.4365 0.5262 -0.0064 -0.0002 -0.0047 701  MET   B CE   
3539 N  N    . HIS   B 197 ? 0.4478 0.3358 0.4182 0.0180  0.0083  -0.0268 702  HIS   B N    
3540 C  CA   . HIS   B 197 ? 0.4474 0.3457 0.4180 0.0148  0.0126  -0.0256 702  HIS   B CA   
3541 C  C    . HIS   B 197 ? 0.4894 0.3807 0.4489 0.0160  0.0116  -0.0301 702  HIS   B C    
3542 O  O    . HIS   B 197 ? 0.4793 0.3710 0.4344 0.0103  0.0107  -0.0283 702  HIS   B O    
3543 C  CB   . HIS   B 197 ? 0.4298 0.3440 0.4094 0.0184  0.0195  -0.0251 702  HIS   B CB   
3544 C  CG   . HIS   B 197 ? 0.4598 0.3827 0.4381 0.0156  0.0236  -0.0238 702  HIS   B CG   
3545 N  ND1  . HIS   B 197 ? 0.4931 0.4191 0.4663 0.0196  0.0270  -0.0275 702  HIS   B ND1  
3546 C  CD2  . HIS   B 197 ? 0.4486 0.3771 0.4289 0.0095  0.0242  -0.0191 702  HIS   B CD2  
3547 C  CE1  . HIS   B 197 ? 0.5495 0.4823 0.5217 0.0155  0.0295  -0.0246 702  HIS   B CE1  
3548 N  NE2  . HIS   B 197 ? 0.4779 0.4121 0.4546 0.0098  0.0277  -0.0196 702  HIS   B NE2  
3549 N  N    . GLN   B 198 ? 0.4901 0.3759 0.4448 0.0240  0.0117  -0.0362 703  GLN   B N    
3550 C  CA   . GLN   B 198 ? 0.4703 0.3491 0.4132 0.0257  0.0107  -0.0412 703  GLN   B CA   
3551 C  C    . GLN   B 198 ? 0.5651 0.4264 0.4982 0.0200  0.0027  -0.0414 703  GLN   B C    
3552 O  O    . GLN   B 198 ? 0.5286 0.3862 0.4530 0.0170  0.0010  -0.0431 703  GLN   B O    
3553 C  CB   . GLN   B 198 ? 0.5431 0.4208 0.4828 0.0364  0.0128  -0.0484 703  GLN   B CB   
3554 C  CG   . GLN   B 198 ? 0.5118 0.3753 0.4497 0.0420  0.0074  -0.0517 703  GLN   B CG   
3555 C  CD   . GLN   B 198 ? 0.5734 0.4153 0.4970 0.0420  -0.0001 -0.0562 703  GLN   B CD   
3556 O  OE1  . GLN   B 198 ? 0.5765 0.4157 0.4905 0.0438  0.0003  -0.0610 703  GLN   B OE1  
3557 N  NE2  . GLN   B 198 ? 0.5348 0.3604 0.4561 0.0396  -0.0074 -0.0547 703  GLN   B NE2  
3558 N  N    . TYR   B 199 ? 0.4823 0.3331 0.4166 0.0176  -0.0027 -0.0392 704  TYR   B N    
3559 C  CA   . TYR   B 199 ? 0.5221 0.3573 0.4478 0.0102  -0.0105 -0.0380 704  TYR   B CA   
3560 C  C    . TYR   B 199 ? 0.5212 0.3658 0.4499 0.0001  -0.0101 -0.0319 704  TYR   B C    
3561 O  O    . TYR   B 199 ? 0.5125 0.3499 0.4334 -0.0061 -0.0147 -0.0319 704  TYR   B O    
3562 C  CB   . TYR   B 199 ? 0.5285 0.3512 0.4548 0.0095  -0.0161 -0.0359 704  TYR   B CB   
3563 C  CG   . TYR   B 199 ? 0.5409 0.3496 0.4601 -0.0005 -0.0239 -0.0325 704  TYR   B CG   
3564 C  CD1  . TYR   B 199 ? 0.5743 0.3621 0.4805 -0.0004 -0.0310 -0.0370 704  TYR   B CD1  
3565 C  CD2  . TYR   B 199 ? 0.5900 0.4066 0.5152 -0.0101 -0.0244 -0.0249 704  TYR   B CD2  
3566 C  CE1  . TYR   B 199 ? 0.6163 0.3913 0.5160 -0.0107 -0.0386 -0.0334 704  TYR   B CE1  
3567 C  CE2  . TYR   B 199 ? 0.5432 0.3492 0.4625 -0.0200 -0.0313 -0.0212 704  TYR   B CE2  
3568 C  CZ   . TYR   B 199 ? 0.6187 0.4038 0.5255 -0.0208 -0.0385 -0.0252 704  TYR   B CZ   
3569 O  OH   . TYR   B 199 ? 0.6716 0.4460 0.5724 -0.0320 -0.0459 -0.0211 704  TYR   B OH   
3570 N  N    . MET   B 200 ? 0.5253 0.3861 0.4652 -0.0013 -0.0050 -0.0271 705  MET   B N    
3571 C  CA   . MET   B 200 ? 0.5310 0.4017 0.4756 -0.0097 -0.0048 -0.0209 705  MET   B CA   
3572 C  C    . MET   B 200 ? 0.5410 0.4187 0.4822 -0.0119 -0.0030 -0.0214 705  MET   B C    
3573 O  O    . MET   B 200 ? 0.5213 0.4029 0.4625 -0.0192 -0.0053 -0.0177 705  MET   B O    
3574 C  CB   . MET   B 200 ? 0.5778 0.4626 0.5344 -0.0082 0.0003  -0.0171 705  MET   B CB   
3575 C  CG   . MET   B 200 ? 0.5874 0.4709 0.5485 -0.0120 -0.0024 -0.0128 705  MET   B CG   
3576 S  SD   . MET   B 200 ? 0.4951 0.3958 0.4688 -0.0098 0.0039  -0.0096 705  MET   B SD   
3577 C  CE   . MET   B 200 ? 0.5795 0.4920 0.5548 -0.0160 0.0054  -0.0058 705  MET   B CE   
3578 N  N    . THR   B 201 ? 0.5276 0.4085 0.4662 -0.0055 0.0012  -0.0257 706  THR   B N    
3579 C  CA   . THR   B 201 ? 0.5365 0.4270 0.4734 -0.0069 0.0041  -0.0250 706  THR   B CA   
3580 C  C    . THR   B 201 ? 0.5409 0.4245 0.4686 -0.0130 -0.0016 -0.0255 706  THR   B C    
3581 O  O    . THR   B 201 ? 0.4984 0.3911 0.4272 -0.0173 -0.0012 -0.0223 706  THR   B O    
3582 C  CB   . THR   B 201 ? 0.5655 0.4601 0.4997 0.0007  0.0096  -0.0294 706  THR   B CB   
3583 O  OG1  . THR   B 201 ? 0.5797 0.4613 0.5049 0.0059  0.0069  -0.0360 706  THR   B OG1  
3584 C  CG2  . THR   B 201 ? 0.5716 0.4775 0.5168 0.0049  0.0157  -0.0274 706  THR   B CG2  
3585 N  N    . LYS   B 202 ? 0.5206 0.3878 0.4394 -0.0138 -0.0077 -0.0293 707  LYS   B N    
3586 C  CA   . LYS   B 202 ? 0.4950 0.3554 0.4054 -0.0210 -0.0140 -0.0294 707  LYS   B CA   
3587 C  C    . LYS   B 202 ? 0.5369 0.4042 0.4538 -0.0305 -0.0168 -0.0225 707  LYS   B C    
3588 O  O    . LYS   B 202 ? 0.5169 0.3850 0.4297 -0.0371 -0.0209 -0.0214 707  LYS   B O    
3589 C  CB   . LYS   B 202 ? 0.6033 0.4424 0.5022 -0.0204 -0.0208 -0.0349 707  LYS   B CB   
3590 C  CG   . LYS   B 202 ? 0.5876 0.4159 0.4891 -0.0207 -0.0241 -0.0335 707  LYS   B CG   
3591 C  CD   . LYS   B 202 ? 0.6102 0.4147 0.4987 -0.0201 -0.0319 -0.0390 707  LYS   B CD   
3592 C  CE   . LYS   B 202 ? 0.6762 0.4699 0.5658 -0.0133 -0.0327 -0.0408 707  LYS   B CE   
3593 N  NZ   . LYS   B 202 ? 0.6272 0.4282 0.5200 -0.0011 -0.0257 -0.0456 707  LYS   B NZ   
3594 N  N    . PHE   B 203 ? 0.4628 0.3369 0.3899 -0.0311 -0.0145 -0.0180 708  PHE   B N    
3595 C  CA   . PHE   B 203 ? 0.4600 0.3436 0.3937 -0.0392 -0.0162 -0.0115 708  PHE   B CA   
3596 C  C    . PHE   B 203 ? 0.4717 0.3741 0.4150 -0.0375 -0.0103 -0.0080 708  PHE   B C    
3597 O  O    . PHE   B 203 ? 0.4888 0.4012 0.4393 -0.0419 -0.0103 -0.0030 708  PHE   B O    
3598 C  CB   . PHE   B 203 ? 0.4819 0.3592 0.4186 -0.0422 -0.0189 -0.0085 708  PHE   B CB   
3599 C  CG   . PHE   B 203 ? 0.5420 0.3986 0.4686 -0.0449 -0.0261 -0.0112 708  PHE   B CG   
3600 C  CD1  . PHE   B 203 ? 0.5647 0.4151 0.4847 -0.0541 -0.0328 -0.0100 708  PHE   B CD1  
3601 C  CD2  . PHE   B 203 ? 0.5411 0.3839 0.4644 -0.0382 -0.0266 -0.0149 708  PHE   B CD2  
3602 C  CE1  . PHE   B 203 ? 0.5735 0.4021 0.4830 -0.0569 -0.0403 -0.0125 708  PHE   B CE1  
3603 C  CE2  . PHE   B 203 ? 0.5872 0.4090 0.5003 -0.0398 -0.0338 -0.0176 708  PHE   B CE2  
3604 C  CZ   . PHE   B 203 ? 0.6196 0.4330 0.5253 -0.0494 -0.0409 -0.0164 708  PHE   B CZ   
3605 N  N    . ASN   B 204 ? 0.4620 0.3694 0.4050 -0.0313 -0.0054 -0.0104 709  ASN   B N    
3606 C  CA   . ASN   B 204 ? 0.4550 0.3777 0.4056 -0.0298 -0.0006 -0.0070 709  ASN   B CA   
3607 C  C    . ASN   B 204 ? 0.4787 0.4106 0.4310 -0.0361 -0.0036 -0.0031 709  ASN   B C    
3608 O  O    . ASN   B 204 ? 0.4550 0.3836 0.4004 -0.0402 -0.0080 -0.0042 709  ASN   B O    
3609 C  CB   . ASN   B 204 ? 0.4530 0.3781 0.4002 -0.0241 0.0038  -0.0096 709  ASN   B CB   
3610 C  CG   . ASN   B 204 ? 0.5015 0.4263 0.4524 -0.0175 0.0090  -0.0114 709  ASN   B CG   
3611 O  OD1  . ASN   B 204 ? 0.4849 0.4096 0.4426 -0.0168 0.0097  -0.0101 709  ASN   B OD1  
3612 N  ND2  . ASN   B 204 ? 0.4736 0.3997 0.4204 -0.0129 0.0128  -0.0140 709  ASN   B ND2  
3613 N  N    . GLN   B 205 ? 0.4152 0.3592 0.3766 -0.0366 -0.0014 0.0011  710  GLN   B N    
3614 C  CA   . GLN   B 205 ? 0.4596 0.4156 0.4245 -0.0412 -0.0036 0.0049  710  GLN   B CA   
3615 C  C    . GLN   B 205 ? 0.4648 0.4311 0.4328 -0.0367 0.0000  0.0061  710  GLN   B C    
3616 O  O    . GLN   B 205 ? 0.4213 0.3891 0.3935 -0.0316 0.0045  0.0063  710  GLN   B O    
3617 C  CB   . GLN   B 205 ? 0.4434 0.4060 0.4158 -0.0446 -0.0041 0.0086  710  GLN   B CB   
3618 C  CG   . GLN   B 205 ? 0.4620 0.4135 0.4311 -0.0495 -0.0079 0.0085  710  GLN   B CG   
3619 C  CD   . GLN   B 205 ? 0.4826 0.4301 0.4455 -0.0574 -0.0141 0.0087  710  GLN   B CD   
3620 O  OE1  . GLN   B 205 ? 0.5679 0.5276 0.5336 -0.0622 -0.0160 0.0117  710  GLN   B OE1  
3621 N  NE2  . GLN   B 205 ? 0.5102 0.4407 0.4645 -0.0584 -0.0175 0.0053  710  GLN   B NE2  
3622 N  N    . LYS   B 206 ? 0.4690 0.4419 0.4348 -0.0390 -0.0026 0.0072  711  LYS   B N    
3623 C  CA   . LYS   B 206 ? 0.4550 0.4359 0.4222 -0.0346 -0.0001 0.0086  711  LYS   B CA   
3624 C  C    . LYS   B 206 ? 0.4427 0.4341 0.4193 -0.0320 0.0022  0.0117  711  LYS   B C    
3625 O  O    . LYS   B 206 ? 0.4316 0.4252 0.4099 -0.0269 0.0052  0.0126  711  LYS   B O    
3626 C  CB   . LYS   B 206 ? 0.5102 0.4962 0.4727 -0.0373 -0.0042 0.0091  711  LYS   B CB   
3627 C  CG   . LYS   B 206 ? 0.6844 0.6682 0.6406 -0.0328 -0.0023 0.0082  711  LYS   B CG   
3628 C  CD   . LYS   B 206 ? 0.7141 0.7050 0.6666 -0.0348 -0.0065 0.0094  711  LYS   B CD   
3629 C  CE   . LYS   B 206 ? 0.7695 0.7554 0.7158 -0.0413 -0.0119 0.0069  711  LYS   B CE   
3630 N  NZ   . LYS   B 206 ? 0.9020 0.8746 0.8369 -0.0400 -0.0116 0.0024  711  LYS   B NZ   
3631 N  N    . GLY   B 207 ? 0.3884 0.3859 0.3707 -0.0354 0.0007  0.0135  712  GLY   B N    
3632 C  CA   . GLY   B 207 ? 0.3759 0.3831 0.3664 -0.0322 0.0030  0.0157  712  GLY   B CA   
3633 C  C    . GLY   B 207 ? 0.4332 0.4451 0.4281 -0.0366 0.0017  0.0172  712  GLY   B C    
3634 O  O    . GLY   B 207 ? 0.4043 0.4116 0.3960 -0.0428 -0.0013 0.0172  712  GLY   B O    
3635 N  N    . VAL   B 208 ? 0.3943 0.4152 0.3960 -0.0335 0.0038  0.0186  713  VAL   B N    
3636 C  CA   . VAL   B 208 ? 0.4163 0.4425 0.4219 -0.0373 0.0034  0.0203  713  VAL   B CA   
3637 C  C    . VAL   B 208 ? 0.4584 0.4952 0.4646 -0.0444 -0.0005 0.0228  713  VAL   B C    
3638 O  O    . VAL   B 208 ? 0.4374 0.4724 0.4426 -0.0512 -0.0025 0.0244  713  VAL   B O    
3639 C  CB   . VAL   B 208 ? 0.4264 0.4611 0.4384 -0.0318 0.0064  0.0208  713  VAL   B CB   
3640 C  CG1  . VAL   B 208 ? 0.3877 0.4321 0.4032 -0.0358 0.0058  0.0231  713  VAL   B CG1  
3641 C  CG2  . VAL   B 208 ? 0.4058 0.4288 0.4174 -0.0272 0.0094  0.0187  713  VAL   B CG2  
3642 N  N    . GLU   B 209 ? 0.4478 0.4960 0.4556 -0.0435 -0.0019 0.0236  714  GLU   B N    
3643 C  CA   . GLU   B 209 ? 0.4603 0.5218 0.4702 -0.0506 -0.0055 0.0262  714  GLU   B CA   
3644 C  C    . GLU   B 209 ? 0.4197 0.4701 0.4227 -0.0591 -0.0098 0.0260  714  GLU   B C    
3645 O  O    . GLU   B 209 ? 0.4566 0.5110 0.4603 -0.0675 -0.0126 0.0286  714  GLU   B O    
3646 C  CB   . GLU   B 209 ? 0.4726 0.5493 0.4859 -0.0472 -0.0067 0.0269  714  GLU   B CB   
3647 C  CG   . GLU   B 209 ? 0.5210 0.6109 0.5413 -0.0397 -0.0036 0.0273  714  GLU   B CG   
3648 C  CD   . GLU   B 209 ? 0.6226 0.7244 0.6482 -0.0434 -0.0026 0.0294  714  GLU   B CD   
3649 O  OE1  . GLU   B 209 ? 0.6767 0.7887 0.7039 -0.0519 -0.0053 0.0322  714  GLU   B OE1  
3650 O  OE2  . GLU   B 209 ? 0.7044 0.8053 0.7322 -0.0382 0.0008  0.0285  714  GLU   B OE2  
3651 N  N    . ASP   B 210 ? 0.4340 0.4703 0.4298 -0.0572 -0.0105 0.0230  715  ASP   B N    
3652 C  CA   . ASP   B 210 ? 0.4727 0.4954 0.4606 -0.0639 -0.0147 0.0217  715  ASP   B CA   
3653 C  C    . ASP   B 210 ? 0.4360 0.4475 0.4224 -0.0676 -0.0149 0.0220  715  ASP   B C    
3654 O  O    . ASP   B 210 ? 0.4491 0.4558 0.4321 -0.0762 -0.0195 0.0233  715  ASP   B O    
3655 C  CB   . ASP   B 210 ? 0.4320 0.4407 0.4118 -0.0594 -0.0143 0.0176  715  ASP   B CB   
3656 C  CG   . ASP   B 210 ? 0.5018 0.5190 0.4804 -0.0574 -0.0156 0.0175  715  ASP   B CG   
3657 O  OD1  . ASP   B 210 ? 0.4558 0.4901 0.4410 -0.0576 -0.0163 0.0204  715  ASP   B OD1  
3658 O  OD2  . ASP   B 210 ? 0.5179 0.5250 0.4886 -0.0551 -0.0159 0.0146  715  ASP   B OD2  
3659 N  N    . ALA   B 211 ? 0.4199 0.4262 0.4084 -0.0615 -0.0105 0.0210  716  ALA   B N    
3660 C  CA   . ALA   B 211 ? 0.4682 0.4626 0.4546 -0.0639 -0.0110 0.0212  716  ALA   B CA   
3661 C  C    . ALA   B 211 ? 0.4430 0.4474 0.4334 -0.0714 -0.0128 0.0259  716  ALA   B C    
3662 O  O    . ALA   B 211 ? 0.5228 0.5173 0.5089 -0.0783 -0.0165 0.0274  716  ALA   B O    
3663 C  CB   . ALA   B 211 ? 0.4368 0.4265 0.4257 -0.0558 -0.0060 0.0194  716  ALA   B CB   
3664 N  N    . LEU   B 212 ? 0.4473 0.4709 0.4454 -0.0699 -0.0103 0.0285  717  LEU   B N    
3665 C  CA   . LEU   B 212 ? 0.4525 0.4893 0.4546 -0.0772 -0.0116 0.0332  717  LEU   B CA   
3666 C  C    . LEU   B 212 ? 0.4679 0.5064 0.4671 -0.0880 -0.0173 0.0357  717  LEU   B C    
3667 O  O    . LEU   B 212 ? 0.4754 0.5122 0.4730 -0.0969 -0.0202 0.0394  717  LEU   B O    
3668 C  CB   . LEU   B 212 ? 0.4639 0.5230 0.4745 -0.0725 -0.0080 0.0345  717  LEU   B CB   
3669 C  CG   . LEU   B 212 ? 0.5196 0.5777 0.5332 -0.0628 -0.0030 0.0324  717  LEU   B CG   
3670 C  CD1  . LEU   B 212 ? 0.5550 0.6342 0.5759 -0.0578 -0.0003 0.0331  717  LEU   B CD1  
3671 C  CD2  . LEU   B 212 ? 0.5543 0.6038 0.5661 -0.0651 -0.0025 0.0337  717  LEU   B CD2  
3672 N  N    . VAL   B 213 ? 0.4502 0.4913 0.4481 -0.0878 -0.0194 0.0339  718  VAL   B N    
3673 C  CA   . VAL   B 213 ? 0.4768 0.5187 0.4716 -0.0986 -0.0256 0.0359  718  VAL   B CA   
3674 C  C    . VAL   B 213 ? 0.5135 0.5305 0.4983 -0.1041 -0.0300 0.0346  718  VAL   B C    
3675 O  O    . VAL   B 213 ? 0.5220 0.5368 0.5044 -0.1152 -0.0350 0.0382  718  VAL   B O    
3676 C  CB   . VAL   B 213 ? 0.4957 0.5446 0.4902 -0.0965 -0.0273 0.0338  718  VAL   B CB   
3677 C  CG1  . VAL   B 213 ? 0.5252 0.5688 0.5139 -0.1075 -0.0347 0.0345  718  VAL   B CG1  
3678 C  CG2  . VAL   B 213 ? 0.3748 0.4502 0.3794 -0.0930 -0.0248 0.0360  718  VAL   B CG2  
3679 N  N    . SER   B 214 ? 0.4688 0.4670 0.4475 -0.0966 -0.0285 0.0296  719  SER   B N    
3680 C  CA   . SER   B 214 ? 0.5239 0.4979 0.4930 -0.0998 -0.0327 0.0276  719  SER   B CA   
3681 C  C    . SER   B 214 ? 0.5343 0.5036 0.5037 -0.1049 -0.0336 0.0317  719  SER   B C    
3682 O  O    . SER   B 214 ? 0.5677 0.5235 0.5305 -0.1136 -0.0396 0.0333  719  SER   B O    
3683 C  CB   . SER   B 214 ? 0.5422 0.5007 0.5064 -0.0892 -0.0296 0.0216  719  SER   B CB   
3684 O  OG   . SER   B 214 ? 0.5995 0.5600 0.5613 -0.0849 -0.0290 0.0180  719  SER   B OG   
3685 N  N    . LEU   B 215 ? 0.5158 0.4947 0.4920 -0.0997 -0.0282 0.0334  720  LEU   B N    
3686 C  CA   . LEU   B 215 ? 0.5312 0.5078 0.5077 -0.1044 -0.0288 0.0378  720  LEU   B CA   
3687 C  C    . LEU   B 215 ? 0.5447 0.5326 0.5225 -0.1174 -0.0329 0.0441  720  LEU   B C    
3688 O  O    . LEU   B 215 ? 0.6139 0.5890 0.5858 -0.1262 -0.0379 0.0474  720  LEU   B O    
3689 C  CB   . LEU   B 215 ? 0.4749 0.4638 0.4588 -0.0967 -0.0223 0.0384  720  LEU   B CB   
3690 C  CG   . LEU   B 215 ? 0.5154 0.4934 0.4990 -0.0858 -0.0184 0.0340  720  LEU   B CG   
3691 C  CD1  . LEU   B 215 ? 0.4580 0.4516 0.4493 -0.0806 -0.0130 0.0355  720  LEU   B CD1  
3692 C  CD2  . LEU   B 215 ? 0.5234 0.4789 0.4996 -0.0866 -0.0217 0.0333  720  LEU   B CD2  
3693 N  N    . LYS   B 216 ? 0.5548 0.5670 0.5404 -0.1189 -0.0309 0.0462  721  LYS   B N    
3694 C  CA   . LYS   B 216 ? 0.5607 0.5888 0.5495 -0.1312 -0.0338 0.0529  721  LYS   B CA   
3695 C  C    . LYS   B 216 ? 0.6065 0.6227 0.5882 -0.1429 -0.0418 0.0541  721  LYS   B C    
3696 O  O    . LYS   B 216 ? 0.6602 0.6788 0.6409 -0.1553 -0.0458 0.0602  721  LYS   B O    
3697 C  CB   . LYS   B 216 ? 0.5531 0.6116 0.5524 -0.1288 -0.0299 0.0542  721  LYS   B CB   
3698 C  CG   . LYS   B 216 ? 0.5769 0.6519 0.5832 -0.1227 -0.0236 0.0559  721  LYS   B CG   
3699 C  CD   . LYS   B 216 ? 0.6623 0.7613 0.6775 -0.1148 -0.0195 0.0541  721  LYS   B CD   
3700 C  CE   . LYS   B 216 ? 0.7567 0.8811 0.7796 -0.1150 -0.0154 0.0581  721  LYS   B CE   
3701 N  NZ   . LYS   B 216 ? 0.8299 0.9825 0.8608 -0.1185 -0.0159 0.0606  721  LYS   B NZ   
3702 N  N    . THR   B 217 ? 0.5587 0.5619 0.5350 -0.1398 -0.0445 0.0486  722  THR   B N    
3703 C  CA   . THR   B 217 ? 0.6117 0.6022 0.5804 -0.1505 -0.0527 0.0489  722  THR   B CA   
3704 C  C    . THR   B 217 ? 0.6551 0.6129 0.6115 -0.1513 -0.0574 0.0463  722  THR   B C    
3705 O  O    . THR   B 217 ? 0.6817 0.6239 0.6297 -0.1588 -0.0649 0.0451  722  THR   B O    
3706 C  CB   . THR   B 217 ? 0.6305 0.6255 0.5987 -0.1475 -0.0541 0.0444  722  THR   B CB   
3707 O  OG1  . THR   B 217 ? 0.5892 0.5692 0.5526 -0.1348 -0.0509 0.0373  722  THR   B OG1  
3708 C  CG2  . THR   B 217 ? 0.5679 0.5951 0.5481 -0.1457 -0.0499 0.0469  722  THR   B CG2  
3709 N  N    . GLY   B 218 ? 0.6202 0.5670 0.5754 -0.1432 -0.0537 0.0449  723  GLY   B N    
3710 C  CA   . GLY   B 218 ? 0.6478 0.5648 0.5921 -0.1437 -0.0586 0.0430  723  GLY   B CA   
3711 C  C    . GLY   B 218 ? 0.6445 0.5418 0.5807 -0.1349 -0.0598 0.0345  723  GLY   B C    
3712 O  O    . GLY   B 218 ? 0.6371 0.5086 0.5626 -0.1361 -0.0656 0.0320  723  GLY   B O    
3713 N  N    . LYS   B 219 ? 0.6005 0.5089 0.5407 -0.1259 -0.0547 0.0300  724  LYS   B N    
3714 C  CA   . LYS   B 219 ? 0.6247 0.5171 0.5574 -0.1167 -0.0546 0.0220  724  LYS   B CA   
3715 C  C    . LYS   B 219 ? 0.6331 0.5203 0.5676 -0.1041 -0.0485 0.0187  724  LYS   B C    
3716 O  O    . LYS   B 219 ? 0.6083 0.4812 0.5364 -0.0961 -0.0481 0.0122  724  LYS   B O    
3717 C  CB   . LYS   B 219 ? 0.6966 0.6031 0.6316 -0.1143 -0.0529 0.0194  724  LYS   B CB   
3718 C  CG   . LYS   B 219 ? 0.8639 0.7534 0.7884 -0.1082 -0.0548 0.0116  724  LYS   B CG   
3719 C  CD   . LYS   B 219 ? 0.8497 0.7449 0.7710 -0.1139 -0.0592 0.0106  724  LYS   B CD   
3720 C  CE   . LYS   B 219 ? 0.9471 0.8688 0.8787 -0.1108 -0.0539 0.0128  724  LYS   B CE   
3721 N  NZ   . LYS   B 219 ? 0.9047 0.8291 0.8383 -0.0975 -0.0462 0.0091  724  LYS   B NZ   
3722 N  N    . LEU   B 220 ? 0.5575 0.4571 0.5006 -0.1023 -0.0436 0.0228  725  LEU   B N    
3723 C  CA   . LEU   B 220 ? 0.5352 0.4314 0.4810 -0.0917 -0.0383 0.0204  725  LEU   B CA   
3724 C  C    . LEU   B 220 ? 0.5605 0.4556 0.5083 -0.0958 -0.0391 0.0259  725  LEU   B C    
3725 O  O    . LEU   B 220 ? 0.5579 0.4666 0.5099 -0.1043 -0.0398 0.0320  725  LEU   B O    
3726 C  CB   . LEU   B 220 ? 0.5427 0.4584 0.4977 -0.0838 -0.0306 0.0194  725  LEU   B CB   
3727 C  CG   . LEU   B 220 ? 0.5856 0.4981 0.5425 -0.0720 -0.0250 0.0151  725  LEU   B CG   
3728 C  CD1  . LEU   B 220 ? 0.5442 0.4403 0.4923 -0.0672 -0.0267 0.0087  725  LEU   B CD1  
3729 C  CD2  . LEU   B 220 ? 0.5211 0.4532 0.4867 -0.0671 -0.0189 0.0156  725  LEU   B CD2  
3730 N  N    . ASP   B 221 ? 0.5465 0.4263 0.4911 -0.0897 -0.0391 0.0238  726  ASP   B N    
3731 C  CA   . ASP   B 221 ? 0.5551 0.4330 0.5010 -0.0921 -0.0398 0.0288  726  ASP   B CA   
3732 C  C    . ASP   B 221 ? 0.5229 0.4174 0.4785 -0.0851 -0.0325 0.0296  726  ASP   B C    
3733 O  O    . ASP   B 221 ? 0.5566 0.4604 0.5156 -0.0893 -0.0318 0.0351  726  ASP   B O    
3734 C  CB   . ASP   B 221 ? 0.5531 0.4051 0.4901 -0.0890 -0.0446 0.0262  726  ASP   B CB   
3735 C  CG   . ASP   B 221 ? 0.6030 0.4355 0.5290 -0.0966 -0.0530 0.0256  726  ASP   B CG   
3736 O  OD1  . ASP   B 221 ? 0.6592 0.4960 0.5843 -0.1089 -0.0569 0.0314  726  ASP   B OD1  
3737 O  OD2  . ASP   B 221 ? 0.6253 0.4390 0.5436 -0.0904 -0.0558 0.0192  726  ASP   B OD2  
3738 N  N    . ALA   B 222 ? 0.4764 0.3745 0.4357 -0.0747 -0.0273 0.0243  727  ALA   B N    
3739 C  CA   . ALA   B 222 ? 0.4507 0.3626 0.4186 -0.0680 -0.0210 0.0245  727  ALA   B CA   
3740 C  C    . ALA   B 222 ? 0.4651 0.3874 0.4376 -0.0615 -0.0159 0.0206  727  ALA   B C    
3741 O  O    . ALA   B 222 ? 0.4830 0.3978 0.4513 -0.0588 -0.0165 0.0163  727  ALA   B O    
3742 C  CB   . ALA   B 222 ? 0.4471 0.3477 0.4144 -0.0610 -0.0206 0.0226  727  ALA   B CB   
3743 N  N    . PHE   B 223 ? 0.4271 0.3663 0.4077 -0.0587 -0.0111 0.0220  728  PHE   B N    
3744 C  CA   . PHE   B 223 ? 0.4160 0.3648 0.4011 -0.0525 -0.0064 0.0192  728  PHE   B CA   
3745 C  C    . PHE   B 223 ? 0.4165 0.3686 0.4072 -0.0454 -0.0022 0.0181  728  PHE   B C    
3746 O  O    . PHE   B 223 ? 0.4291 0.3898 0.4238 -0.0463 -0.0011 0.0210  728  PHE   B O    
3747 C  CB   . PHE   B 223 ? 0.4202 0.3862 0.4093 -0.0561 -0.0057 0.0219  728  PHE   B CB   
3748 C  CG   . PHE   B 223 ? 0.3987 0.3740 0.3921 -0.0497 -0.0015 0.0197  728  PHE   B CG   
3749 C  CD1  . PHE   B 223 ? 0.4088 0.3765 0.3993 -0.0449 -0.0002 0.0158  728  PHE   B CD1  
3750 C  CD2  . PHE   B 223 ? 0.4250 0.4167 0.4249 -0.0483 0.0010  0.0217  728  PHE   B CD2  
3751 C  CE1  . PHE   B 223 ? 0.4131 0.3884 0.4067 -0.0398 0.0032  0.0147  728  PHE   B CE1  
3752 C  CE2  . PHE   B 223 ? 0.3925 0.3907 0.3954 -0.0423 0.0041  0.0200  728  PHE   B CE2  
3753 C  CZ   . PHE   B 223 ? 0.4030 0.3925 0.4027 -0.0385 0.0050  0.0169  728  PHE   B CZ   
3754 N  N    . ILE   B 224 ? 0.3892 0.3346 0.3797 -0.0387 0.0001  0.0140  729  ILE   B N    
3755 C  CA   . ILE   B 224 ? 0.3693 0.3169 0.3652 -0.0324 0.0037  0.0127  729  ILE   B CA   
3756 C  C    . ILE   B 224 ? 0.3695 0.3277 0.3701 -0.0287 0.0079  0.0119  729  ILE   B C    
3757 O  O    . ILE   B 224 ? 0.3961 0.3533 0.3945 -0.0274 0.0089  0.0100  729  ILE   B O    
3758 C  CB   . ILE   B 224 ? 0.3937 0.3290 0.3871 -0.0275 0.0035  0.0090  729  ILE   B CB   
3759 C  CG1  . ILE   B 224 ? 0.3726 0.2946 0.3598 -0.0308 -0.0017 0.0098  729  ILE   B CG1  
3760 C  CG2  . ILE   B 224 ? 0.4119 0.3512 0.4119 -0.0219 0.0068  0.0081  729  ILE   B CG2  
3761 C  CD1  . ILE   B 224 ? 0.4827 0.3920 0.4664 -0.0253 -0.0026 0.0055  729  ILE   B CD1  
3762 N  N    . TYR   B 225 ? 0.3683 0.3358 0.3745 -0.0270 0.0100  0.0133  730  TYR   B N    
3763 C  CA   . TYR   B 225 ? 0.3964 0.3728 0.4062 -0.0241 0.0128  0.0130  730  TYR   B CA   
3764 C  C    . TYR   B 225 ? 0.3856 0.3683 0.4008 -0.0211 0.0147  0.0134  730  TYR   B C    
3765 O  O    . TYR   B 225 ? 0.4176 0.3998 0.4337 -0.0218 0.0138  0.0142  730  TYR   B O    
3766 C  CB   . TYR   B 225 ? 0.3529 0.3377 0.3616 -0.0277 0.0115  0.0149  730  TYR   B CB   
3767 C  CG   . TYR   B 225 ? 0.3700 0.3612 0.3805 -0.0242 0.0135  0.0144  730  TYR   B CG   
3768 C  CD1  . TYR   B 225 ? 0.4181 0.4038 0.4258 -0.0221 0.0146  0.0126  730  TYR   B CD1  
3769 C  CD2  . TYR   B 225 ? 0.3517 0.3544 0.3660 -0.0228 0.0140  0.0158  730  TYR   B CD2  
3770 C  CE1  . TYR   B 225 ? 0.4239 0.4144 0.4324 -0.0192 0.0159  0.0129  730  TYR   B CE1  
3771 C  CE2  . TYR   B 225 ? 0.3629 0.3698 0.3782 -0.0191 0.0151  0.0155  730  TYR   B CE2  
3772 C  CZ   . TYR   B 225 ? 0.4008 0.4010 0.4130 -0.0177 0.0158  0.0144  730  TYR   B CZ   
3773 O  OH   . TYR   B 225 ? 0.3914 0.3947 0.4038 -0.0143 0.0165  0.0147  730  TYR   B OH   
3774 N  N    . ASP   B 226 ? 0.3672 0.3551 0.3851 -0.0177 0.0168  0.0128  731  ASP   B N    
3775 C  CA   . ASP   B 226 ? 0.3923 0.3852 0.4145 -0.0143 0.0181  0.0125  731  ASP   B CA   
3776 C  C    . ASP   B 226 ? 0.3771 0.3774 0.4001 -0.0159 0.0169  0.0141  731  ASP   B C    
3777 O  O    . ASP   B 226 ? 0.3657 0.3738 0.3878 -0.0187 0.0159  0.0159  731  ASP   B O    
3778 C  CB   . ASP   B 226 ? 0.3798 0.3770 0.4029 -0.0113 0.0192  0.0123  731  ASP   B CB   
3779 C  CG   . ASP   B 226 ? 0.3507 0.3520 0.3770 -0.0075 0.0197  0.0116  731  ASP   B CG   
3780 O  OD1  . ASP   B 226 ? 0.4077 0.4036 0.4359 -0.0053 0.0207  0.0103  731  ASP   B OD1  
3781 O  OD2  . ASP   B 226 ? 0.4138 0.4239 0.4407 -0.0066 0.0190  0.0122  731  ASP   B OD2  
3782 N  N    . ALA   B 227 ? 0.3873 0.3866 0.4122 -0.0142 0.0171  0.0134  732  ALA   B N    
3783 C  CA   . ALA   B 227 ? 0.3694 0.3750 0.3939 -0.0161 0.0160  0.0151  732  ALA   B CA   
3784 C  C    . ALA   B 227 ? 0.3722 0.3904 0.3979 -0.0145 0.0167  0.0155  732  ALA   B C    
3785 O  O    . ALA   B 227 ? 0.3942 0.4214 0.4190 -0.0178 0.0161  0.0178  732  ALA   B O    
3786 C  CB   . ALA   B 227 ? 0.3953 0.3972 0.4211 -0.0140 0.0158  0.0140  732  ALA   B CB   
3787 N  N    . ALA   B 228 ? 0.3418 0.3613 0.3696 -0.0094 0.0179  0.0132  733  ALA   B N    
3788 C  CA   . ALA   B 228 ? 0.3736 0.4049 0.4024 -0.0062 0.0182  0.0128  733  ALA   B CA   
3789 C  C    . ALA   B 228 ? 0.3518 0.3922 0.3804 -0.0086 0.0179  0.0148  733  ALA   B C    
3790 O  O    . ALA   B 228 ? 0.3582 0.4120 0.3877 -0.0088 0.0180  0.0158  733  ALA   B O    
3791 C  CB   . ALA   B 228 ? 0.3319 0.3598 0.3621 0.0001  0.0187  0.0098  733  ALA   B CB   
3792 N  N    . VAL   B 229 ? 0.3792 0.4136 0.4067 -0.0104 0.0174  0.0153  734  VAL   B N    
3793 C  CA   . VAL   B 229 ? 0.3094 0.3523 0.3367 -0.0132 0.0164  0.0172  734  VAL   B CA   
3794 C  C    . VAL   B 229 ? 0.3949 0.4425 0.4208 -0.0206 0.0151  0.0202  734  VAL   B C    
3795 O  O    . VAL   B 229 ? 0.3866 0.4482 0.4140 -0.0231 0.0146  0.0222  734  VAL   B O    
3796 C  CB   . VAL   B 229 ? 0.3349 0.3692 0.3601 -0.0134 0.0160  0.0168  734  VAL   B CB   
3797 C  CG1  . VAL   B 229 ? 0.3287 0.3695 0.3527 -0.0180 0.0141  0.0188  734  VAL   B CG1  
3798 C  CG2  . VAL   B 229 ? 0.3690 0.4023 0.3953 -0.0066 0.0167  0.0151  734  VAL   B CG2  
3799 N  N    . LEU   B 230 ? 0.3511 0.3874 0.3744 -0.0244 0.0143  0.0208  735  LEU   B N    
3800 C  CA   . LEU   B 230 ? 0.4029 0.4413 0.4240 -0.0319 0.0124  0.0241  735  LEU   B CA   
3801 C  C    . LEU   B 230 ? 0.4028 0.4547 0.4256 -0.0325 0.0132  0.0260  735  LEU   B C    
3802 O  O    . LEU   B 230 ? 0.3924 0.4550 0.4150 -0.0383 0.0122  0.0295  735  LEU   B O    
3803 C  CB   . LEU   B 230 ? 0.3894 0.4118 0.4069 -0.0343 0.0109  0.0241  735  LEU   B CB   
3804 C  CG   . LEU   B 230 ? 0.3724 0.3824 0.3869 -0.0348 0.0098  0.0224  735  LEU   B CG   
3805 C  CD1  . LEU   B 230 ? 0.3562 0.3517 0.3666 -0.0373 0.0076  0.0225  735  LEU   B CD1  
3806 C  CD2  . LEU   B 230 ? 0.3648 0.3797 0.3779 -0.0390 0.0081  0.0236  735  LEU   B CD2  
3807 N  N    . ASN   B 231 ? 0.3918 0.4441 0.4160 -0.0267 0.0150  0.0238  736  ASN   B N    
3808 C  CA   . ASN   B 231 ? 0.4502 0.5160 0.4750 -0.0262 0.0160  0.0249  736  ASN   B CA   
3809 C  C    . ASN   B 231 ? 0.4137 0.4980 0.4416 -0.0247 0.0171  0.0253  736  ASN   B C    
3810 O  O    . ASN   B 231 ? 0.4254 0.5245 0.4536 -0.0286 0.0174  0.0283  736  ASN   B O    
3811 C  CB   . ASN   B 231 ? 0.4765 0.5382 0.5017 -0.0194 0.0172  0.0215  736  ASN   B CB   
3812 C  CG   . ASN   B 231 ? 0.5602 0.6363 0.5851 -0.0175 0.0185  0.0216  736  ASN   B CG   
3813 O  OD1  . ASN   B 231 ? 0.6045 0.6959 0.6315 -0.0147 0.0198  0.0211  736  ASN   B OD1  
3814 N  ND2  . ASN   B 231 ? 0.6986 0.7708 0.7209 -0.0186 0.0181  0.0223  736  ASN   B ND2  
3815 N  N    . TYR   B 232 ? 0.3971 0.4813 0.4272 -0.0192 0.0174  0.0225  737  TYR   B N    
3816 C  CA   . TYR   B 232 ? 0.4334 0.5352 0.4668 -0.0166 0.0179  0.0226  737  TYR   B CA   
3817 C  C    . TYR   B 232 ? 0.4670 0.5783 0.5010 -0.0251 0.0164  0.0268  737  TYR   B C    
3818 O  O    . TYR   B 232 ? 0.4455 0.5764 0.4823 -0.0268 0.0170  0.0289  737  TYR   B O    
3819 C  CB   . TYR   B 232 ? 0.4335 0.5302 0.4681 -0.0093 0.0177  0.0194  737  TYR   B CB   
3820 C  CG   . TYR   B 232 ? 0.4365 0.5507 0.4746 -0.0057 0.0176  0.0193  737  TYR   B CG   
3821 C  CD1  . TYR   B 232 ? 0.4816 0.5978 0.5205 -0.0081 0.0158  0.0207  737  TYR   B CD1  
3822 C  CD2  . TYR   B 232 ? 0.4958 0.6254 0.5361 0.0004  0.0190  0.0176  737  TYR   B CD2  
3823 C  CE1  . TYR   B 232 ? 0.5146 0.6481 0.5572 -0.0042 0.0153  0.0207  737  TYR   B CE1  
3824 C  CE2  . TYR   B 232 ? 0.5561 0.7031 0.6001 0.0048  0.0188  0.0172  737  TYR   B CE2  
3825 C  CZ   . TYR   B 232 ? 0.5324 0.6815 0.5779 0.0024  0.0168  0.0189  737  TYR   B CZ   
3826 O  OH   . TYR   B 232 ? 0.6929 0.8608 0.7426 0.0073  0.0163  0.0186  737  TYR   B OH   
3827 N  N    . LYS   B 233 ? 0.4497 0.5479 0.4812 -0.0305 0.0143  0.0280  738  LYS   B N    
3828 C  CA   . LYS   B 233 ? 0.4541 0.5588 0.4856 -0.0392 0.0119  0.0316  738  LYS   B CA   
3829 C  C    . LYS   B 233 ? 0.4839 0.5942 0.5140 -0.0480 0.0111  0.0362  738  LYS   B C    
3830 O  O    . LYS   B 233 ? 0.5091 0.6351 0.5413 -0.0544 0.0102  0.0398  738  LYS   B O    
3831 C  CB   . LYS   B 233 ? 0.4314 0.5183 0.4590 -0.0420 0.0095  0.0309  738  LYS   B CB   
3832 C  CG   . LYS   B 233 ? 0.4051 0.4885 0.4335 -0.0350 0.0099  0.0277  738  LYS   B CG   
3833 C  CD   . LYS   B 233 ? 0.4883 0.5901 0.5207 -0.0338 0.0092  0.0285  738  LYS   B CD   
3834 C  CE   . LYS   B 233 ? 0.5464 0.6419 0.5779 -0.0280 0.0087  0.0260  738  LYS   B CE   
3835 N  NZ   . LYS   B 233 ? 0.6063 0.7180 0.6411 -0.0272 0.0069  0.0270  738  LYS   B NZ   
3836 N  N    . ALA   B 234 ? 0.4389 0.5368 0.4654 -0.0488 0.0113  0.0364  739  ALA   B N    
3837 C  CA   . ALA   B 234 ? 0.4963 0.5987 0.5204 -0.0568 0.0105  0.0412  739  ALA   B CA   
3838 C  C    . ALA   B 234 ? 0.5397 0.6668 0.5676 -0.0556 0.0133  0.0428  739  ALA   B C    
3839 O  O    . ALA   B 234 ? 0.5636 0.7040 0.5917 -0.0641 0.0127  0.0479  739  ALA   B O    
3840 C  CB   . ALA   B 234 ? 0.4869 0.5720 0.5066 -0.0560 0.0101  0.0408  739  ALA   B CB   
3841 N  N    . GLY   B 235 ? 0.5122 0.6458 0.5428 -0.0452 0.0162  0.0384  740  GLY   B N    
3842 C  CA   . GLY   B 235 ? 0.5652 0.7222 0.5987 -0.0420 0.0191  0.0387  740  GLY   B CA   
3843 C  C    . GLY   B 235 ? 0.5824 0.7617 0.6214 -0.0439 0.0193  0.0404  740  GLY   B C    
3844 O  O    . GLY   B 235 ? 0.6144 0.8165 0.6559 -0.0446 0.0214  0.0424  740  GLY   B O    
3845 N  N    . ARG   B 236 ? 0.5449 0.7193 0.5857 -0.0446 0.0171  0.0397  741  ARG   B N    
3846 C  CA   . ARG   B 236 ? 0.5854 0.7810 0.6318 -0.0460 0.0166  0.0412  741  ARG   B CA   
3847 C  C    . ARG   B 236 ? 0.6438 0.8367 0.6895 -0.0584 0.0128  0.0459  741  ARG   B C    
3848 O  O    . ARG   B 236 ? 0.7111 0.9161 0.7609 -0.0598 0.0112  0.0465  741  ARG   B O    
3849 C  CB   . ARG   B 236 ? 0.6501 0.8458 0.6995 -0.0347 0.0168  0.0361  741  ARG   B CB   
3850 C  CG   . ARG   B 236 ? 0.6908 0.9025 0.7434 -0.0233 0.0198  0.0324  741  ARG   B CG   
3851 C  CD   . ARG   B 236 ? 0.7214 0.9147 0.7704 -0.0137 0.0209  0.0272  741  ARG   B CD   
3852 N  NE   . ARG   B 236 ? 0.8966 1.1028 0.9475 -0.0023 0.0230  0.0230  741  ARG   B NE   
3853 C  CZ   . ARG   B 236 ? 0.7965 1.0101 0.8506 0.0071  0.0225  0.0197  741  ARG   B CZ   
3854 N  NH1  . ARG   B 236 ? 0.8590 1.0714 0.9153 0.0059  0.0201  0.0207  741  ARG   B NH1  
3855 N  NH2  . ARG   B 236 ? 0.7099 0.9315 0.7642 0.0183  0.0240  0.0150  741  ARG   B NH2  
3856 N  N    . ASP   B 237 ? 0.5515 0.7283 0.5915 -0.0673 0.0108  0.0491  742  ASP   B N    
3857 C  CA   . ASP   B 237 ? 0.6285 0.7995 0.6664 -0.0792 0.0064  0.0531  742  ASP   B CA   
3858 C  C    . ASP   B 237 ? 0.6097 0.8043 0.6511 -0.0898 0.0059  0.0594  742  ASP   B C    
3859 O  O    . ASP   B 237 ? 0.6169 0.8218 0.6579 -0.0924 0.0082  0.0626  742  ASP   B O    
3860 C  CB   . ASP   B 237 ? 0.5975 0.7411 0.6276 -0.0843 0.0037  0.0539  742  ASP   B CB   
3861 C  CG   . ASP   B 237 ? 0.6076 0.7414 0.6341 -0.0957 -0.0017 0.0570  742  ASP   B CG   
3862 O  OD1  . ASP   B 237 ? 0.5851 0.7170 0.6126 -0.0945 -0.0035 0.0546  742  ASP   B OD1  
3863 O  OD2  . ASP   B 237 ? 0.5649 0.6920 0.5869 -0.1059 -0.0044 0.0619  742  ASP   B OD2  
3864 N  N    . GLU   B 238 ? 0.5606 0.7638 0.6048 -0.0964 0.0027  0.0614  743  GLU   B N    
3865 C  CA   . GLU   B 238 ? 0.6147 0.8430 0.6635 -0.1073 0.0019  0.0677  743  GLU   B CA   
3866 C  C    . GLU   B 238 ? 0.6379 0.8557 0.6803 -0.1207 -0.0006 0.0741  743  GLU   B C    
3867 O  O    . GLU   B 238 ? 0.6814 0.8741 0.7171 -0.1271 -0.0053 0.0747  743  GLU   B O    
3868 C  CB   . GLU   B 238 ? 0.5840 0.8210 0.6369 -0.1123 -0.0020 0.0684  743  GLU   B CB   
3869 N  N    . GLY   B 239 ? 0.6622 0.8992 0.7064 -0.1246 0.0024  0.0788  744  GLY   B N    
3870 C  CA   . GLY   B 239 ? 0.6533 0.8814 0.6909 -0.1368 0.0004  0.0855  744  GLY   B CA   
3871 C  C    . GLY   B 239 ? 0.6685 0.8705 0.6980 -0.1315 0.0009  0.0833  744  GLY   B C    
3872 O  O    . GLY   B 239 ? 0.6599 0.8514 0.6829 -0.1407 -0.0013 0.0889  744  GLY   B O    
3873 N  N    . CYS   B 240 ? 0.6291 0.8203 0.6590 -0.1173 0.0033  0.0757  745  CYS   B N    
3874 C  CA   . CYS   B 240 ? 0.6433 0.8110 0.6669 -0.1113 0.0037  0.0730  745  CYS   B CA   
3875 C  C    . CYS   B 240 ? 0.6099 0.7495 0.6251 -0.1202 -0.0020 0.0758  745  CYS   B C    
3876 O  O    . CYS   B 240 ? 0.5826 0.7096 0.5917 -0.1228 -0.0030 0.0786  745  CYS   B O    
3877 C  CB   . CYS   B 240 ? 0.6287 0.8091 0.6515 -0.1086 0.0078  0.0748  745  CYS   B CB   
3878 S  SG   . CYS   B 240 ? 0.7529 0.9677 0.7844 -0.0980 0.0142  0.0712  745  CYS   B SG   
3879 N  N    . LYS   B 241 ? 0.5796 0.7091 0.5942 -0.1245 -0.0062 0.0749  746  LYS   B N    
3880 C  CA   . LYS   B 241 ? 0.5847 0.6862 0.5908 -0.1318 -0.0122 0.0765  746  LYS   B CA   
3881 C  C    . LYS   B 241 ? 0.6159 0.6920 0.6180 -0.1213 -0.0122 0.0699  746  LYS   B C    
3882 O  O    . LYS   B 241 ? 0.5782 0.6315 0.5728 -0.1239 -0.0158 0.0709  746  LYS   B O    
3883 C  CB   . LYS   B 241 ? 0.5895 0.6901 0.5955 -0.1410 -0.0172 0.0778  746  LYS   B CB   
3884 N  N    . LEU   B 242 ? 0.5688 0.6485 0.5755 -0.1096 -0.0085 0.0634  747  LEU   B N    
3885 C  CA   . LEU   B 242 ? 0.5301 0.5884 0.5340 -0.1003 -0.0082 0.0573  747  LEU   B CA   
3886 C  C    . LEU   B 242 ? 0.5150 0.5754 0.5206 -0.0911 -0.0039 0.0552  747  LEU   B C    
3887 O  O    . LEU   B 242 ? 0.5233 0.6031 0.5345 -0.0861 0.0003  0.0544  747  LEU   B O    
3888 C  CB   . LEU   B 242 ? 0.5116 0.5709 0.5186 -0.0942 -0.0074 0.0521  747  LEU   B CB   
3889 C  CG   . LEU   B 242 ? 0.5690 0.6269 0.5744 -0.1018 -0.0119 0.0530  747  LEU   B CG   
3890 C  CD1  . LEU   B 242 ? 0.5697 0.6318 0.5785 -0.0939 -0.0102 0.0480  747  LEU   B CD1  
3891 C  CD2  . LEU   B 242 ? 0.5172 0.5494 0.5136 -0.1077 -0.0174 0.0532  747  LEU   B CD2  
3892 N  N    . VAL   B 243 ? 0.4744 0.5149 0.4751 -0.0887 -0.0052 0.0541  748  VAL   B N    
3893 C  CA   . VAL   B 243 ? 0.4908 0.5316 0.4921 -0.0818 -0.0023 0.0527  748  VAL   B CA   
3894 C  C    . VAL   B 243 ? 0.5020 0.5236 0.5020 -0.0735 -0.0023 0.0472  748  VAL   B C    
3895 O  O    . VAL   B 243 ? 0.5094 0.5150 0.5060 -0.0745 -0.0053 0.0455  748  VAL   B O    
3896 C  CB   . VAL   B 243 ? 0.4875 0.5269 0.4839 -0.0887 -0.0042 0.0588  748  VAL   B CB   
3897 C  CG1  . VAL   B 243 ? 0.5702 0.6302 0.5679 -0.0981 -0.0039 0.0649  748  VAL   B CG1  
3898 C  CG2  . VAL   B 243 ? 0.5618 0.5766 0.5507 -0.0937 -0.0098 0.0605  748  VAL   B CG2  
3899 N  N    . THR   B 244 ? 0.4382 0.4623 0.4408 -0.0655 0.0008  0.0444  749  THR   B N    
3900 C  CA   . THR   B 244 ? 0.4883 0.4962 0.4902 -0.0587 0.0007  0.0402  749  THR   B CA   
3901 C  C    . THR   B 244 ? 0.5328 0.5297 0.5296 -0.0612 -0.0023 0.0432  749  THR   B C    
3902 O  O    . THR   B 244 ? 0.5516 0.5570 0.5468 -0.0652 -0.0024 0.0475  749  THR   B O    
3903 C  CB   . THR   B 244 ? 0.5390 0.5539 0.5461 -0.0494 0.0047  0.0357  749  THR   B CB   
3904 O  OG1  . THR   B 244 ? 0.4928 0.5219 0.5009 -0.0492 0.0065  0.0376  749  THR   B OG1  
3905 C  CG2  . THR   B 244 ? 0.4375 0.4590 0.4487 -0.0459 0.0070  0.0326  749  THR   B CG2  
3906 N  N    . ILE   B 245 ? 0.5858 0.5644 0.5799 -0.0584 -0.0047 0.0408  750  ILE   B N    
3907 C  CA   . ILE   B 245 ? 0.5977 0.5636 0.5863 -0.0604 -0.0086 0.0437  750  ILE   B CA   
3908 C  C    . ILE   B 245 ? 0.6362 0.6061 0.6271 -0.0544 -0.0067 0.0426  750  ILE   B C    
3909 O  O    . ILE   B 245 ? 0.6303 0.6071 0.6270 -0.0474 -0.0030 0.0382  750  ILE   B O    
3910 C  CB   . ILE   B 245 ? 0.6415 0.5865 0.6261 -0.0587 -0.0123 0.0412  750  ILE   B CB   
3911 C  CG1  . ILE   B 245 ? 0.6251 0.5673 0.6146 -0.0487 -0.0095 0.0349  750  ILE   B CG1  
3912 C  CG2  . ILE   B 245 ? 0.5885 0.5293 0.5703 -0.0642 -0.0143 0.0413  750  ILE   B CG2  
3913 C  CD1  . ILE   B 245 ? 0.6873 0.6115 0.6733 -0.0449 -0.0130 0.0328  750  ILE   B CD1  
3914 N  N    . GLY   B 246 ? 0.7174 0.6822 0.7033 -0.0575 -0.0098 0.0469  751  GLY   B N    
3915 C  CA   . GLY   B 246 ? 0.6559 0.6240 0.6427 -0.0525 -0.0089 0.0463  751  GLY   B CA   
3916 C  C    . GLY   B 246 ? 0.7494 0.7375 0.7396 -0.0514 -0.0046 0.0462  751  GLY   B C    
3917 O  O    . GLY   B 246 ? 0.8017 0.7935 0.7947 -0.0450 -0.0029 0.0429  751  GLY   B O    
3918 N  N    . SER   B 247 ? 0.7462 0.7475 0.7360 -0.0574 -0.0031 0.0495  752  SER   B N    
3919 C  CA   . SER   B 247 ? 0.8709 0.8927 0.8640 -0.0555 0.0012  0.0488  752  SER   B CA   
3920 C  C    . SER   B 247 ? 0.9000 0.9251 0.8997 -0.0464 0.0045  0.0418  752  SER   B C    
3921 O  O    . SER   B 247 ? 0.9564 0.9886 0.9577 -0.0407 0.0066  0.0388  752  SER   B O    
3922 C  CB   . SER   B 247 ? 0.9388 0.9668 0.9278 -0.0556 0.0011  0.0516  752  SER   B CB   
3923 O  OG   . SER   B 247 ? 0.9853 1.0110 0.9676 -0.0649 -0.0020 0.0590  752  SER   B OG   
3924 N  N    . GLY   B 248 ? 0.7404 0.7592 0.7429 -0.0454 0.0046  0.0391  753  GLY   B N    
3925 C  CA   . GLY   B 248 ? 0.6290 0.6490 0.6369 -0.0379 0.0073  0.0333  753  GLY   B CA   
3926 C  C    . GLY   B 248 ? 0.6658 0.6740 0.6752 -0.0321 0.0067  0.0296  753  GLY   B C    
3927 O  O    . GLY   B 248 ? 0.6573 0.6692 0.6702 -0.0262 0.0087  0.0258  753  GLY   B O    
3928 N  N    . TYR   B 249 ? 0.6221 0.6162 0.6291 -0.0335 0.0038  0.0305  754  TYR   B N    
3929 C  CA   . TYR   B 249 ? 0.6419 0.6269 0.6514 -0.0278 0.0033  0.0270  754  TYR   B CA   
3930 C  C    . TYR   B 249 ? 0.5688 0.5518 0.5829 -0.0238 0.0056  0.0227  754  TYR   B C    
3931 O  O    . TYR   B 249 ? 0.5206 0.5038 0.5343 -0.0260 0.0063  0.0229  754  TYR   B O    
3932 C  CB   . TYR   B 249 ? 0.6403 0.6114 0.6458 -0.0292 -0.0008 0.0289  754  TYR   B CB   
3933 C  CG   . TYR   B 249 ? 0.7304 0.6952 0.7392 -0.0230 -0.0015 0.0255  754  TYR   B CG   
3934 C  CD1  . TYR   B 249 ? 0.7207 0.6891 0.7302 -0.0206 -0.0023 0.0255  754  TYR   B CD1  
3935 C  CD2  . TYR   B 249 ? 0.6837 0.6402 0.6950 -0.0196 -0.0014 0.0222  754  TYR   B CD2  
3936 C  CE1  . TYR   B 249 ? 0.7328 0.6970 0.7462 -0.0154 -0.0033 0.0225  754  TYR   B CE1  
3937 C  CE2  . TYR   B 249 ? 0.7203 0.6737 0.7359 -0.0140 -0.0018 0.0192  754  TYR   B CE2  
3938 C  CZ   . TYR   B 249 ? 0.7373 0.6947 0.7543 -0.0122 -0.0029 0.0195  754  TYR   B CZ   
3939 O  OH   . TYR   B 249 ? 0.7795 0.7351 0.8013 -0.0071 -0.0037 0.0168  754  TYR   B OH   
3940 N  N    . ILE   B 250 ? 0.5401 0.5217 0.5585 -0.0185 0.0067  0.0192  755  ILE   B N    
3941 C  CA   . ILE   B 250 ? 0.4890 0.4695 0.5118 -0.0150 0.0091  0.0157  755  ILE   B CA   
3942 C  C    . ILE   B 250 ? 0.5349 0.5075 0.5604 -0.0118 0.0082  0.0136  755  ILE   B C    
3943 O  O    . ILE   B 250 ? 0.5402 0.5130 0.5675 -0.0096 0.0071  0.0130  755  ILE   B O    
3944 C  CB   . ILE   B 250 ? 0.4759 0.4647 0.5022 -0.0120 0.0114  0.0136  755  ILE   B CB   
3945 C  CG1  . ILE   B 250 ? 0.4650 0.4635 0.4893 -0.0140 0.0123  0.0152  755  ILE   B CG1  
3946 C  CG2  . ILE   B 250 ? 0.4462 0.4325 0.4766 -0.0091 0.0134  0.0107  755  ILE   B CG2  
3947 C  CD1  . ILE   B 250 ? 0.4834 0.4893 0.5101 -0.0099 0.0140  0.0126  755  ILE   B CD1  
3948 N  N    . PHE   B 251 ? 0.4827 0.4492 0.5080 -0.0113 0.0087  0.0124  756  PHE   B N    
3949 C  CA   . PHE   B 251 ? 0.4896 0.4517 0.5186 -0.0072 0.0090  0.0097  756  PHE   B CA   
3950 C  C    . PHE   B 251 ? 0.4797 0.4471 0.5141 -0.0051 0.0125  0.0074  756  PHE   B C    
3951 O  O    . PHE   B 251 ? 0.3937 0.3642 0.4274 -0.0063 0.0145  0.0076  756  PHE   B O    
3952 C  CB   . PHE   B 251 ? 0.4840 0.4371 0.5095 -0.0069 0.0079  0.0090  756  PHE   B CB   
3953 C  CG   . PHE   B 251 ? 0.5668 0.5177 0.5964 -0.0018 0.0086  0.0058  756  PHE   B CG   
3954 C  CD1  . PHE   B 251 ? 0.6000 0.5469 0.6305 0.0011  0.0057  0.0055  756  PHE   B CD1  
3955 C  CD2  . PHE   B 251 ? 0.5884 0.5421 0.6209 0.0001  0.0122  0.0034  756  PHE   B CD2  
3956 C  CE1  . PHE   B 251 ? 0.6288 0.5761 0.6640 0.0063  0.0064  0.0025  756  PHE   B CE1  
3957 C  CE2  . PHE   B 251 ? 0.5578 0.5121 0.5946 0.0047  0.0134  0.0007  756  PHE   B CE2  
3958 C  CZ   . PHE   B 251 ? 0.5451 0.4969 0.5838 0.0080  0.0105  0.0001  756  PHE   B CZ   
3959 N  N    . ALA   B 252 ? 0.4195 0.3882 0.4593 -0.0021 0.0128  0.0056  757  ALA   B N    
3960 C  CA   . ALA   B 252 ? 0.4501 0.4231 0.4953 -0.0009 0.0156  0.0040  757  ALA   B CA   
3961 C  C    . ALA   B 252 ? 0.4280 0.4050 0.4729 -0.0022 0.0162  0.0045  757  ALA   B C    
3962 O  O    . ALA   B 252 ? 0.3718 0.3498 0.4161 -0.0028 0.0183  0.0046  757  ALA   B O    
3963 C  CB   . ALA   B 252 ? 0.4036 0.3753 0.4485 -0.0004 0.0183  0.0031  757  ALA   B CB   
3964 N  N    . THR   B 253 ? 0.4279 0.4071 0.4726 -0.0021 0.0141  0.0047  758  THR   B N    
3965 C  CA   . THR   B 253 ? 0.4133 0.3962 0.4571 -0.0021 0.0143  0.0044  758  THR   B CA   
3966 C  C    . THR   B 253 ? 0.4325 0.4151 0.4800 -0.0013 0.0158  0.0029  758  THR   B C    
3967 O  O    . THR   B 253 ? 0.4301 0.4120 0.4824 -0.0010 0.0158  0.0020  758  THR   B O    
3968 C  CB   . THR   B 253 ? 0.4990 0.4843 0.5420 -0.0014 0.0118  0.0039  758  THR   B CB   
3969 O  OG1  . THR   B 253 ? 0.4959 0.4798 0.5434 -0.0003 0.0102  0.0027  758  THR   B OG1  
3970 C  CG2  . THR   B 253 ? 0.4419 0.4282 0.4797 -0.0030 0.0104  0.0064  758  THR   B CG2  
3971 N  N    . THR   B 254 ? 0.3813 0.3649 0.4267 -0.0010 0.0168  0.0030  759  THR   B N    
3972 C  CA   . THR   B 254 ? 0.3718 0.3534 0.4190 -0.0005 0.0176  0.0023  759  THR   B CA   
3973 C  C    . THR   B 254 ? 0.3586 0.3418 0.4022 0.0013  0.0171  0.0019  759  THR   B C    
3974 O  O    . THR   B 254 ? 0.3516 0.3390 0.3925 0.0023  0.0161  0.0016  759  THR   B O    
3975 C  CB   . THR   B 254 ? 0.3438 0.3235 0.3923 -0.0018 0.0201  0.0034  759  THR   B CB   
3976 O  OG1  . THR   B 254 ? 0.4023 0.3795 0.4522 -0.0021 0.0205  0.0036  759  THR   B OG1  
3977 C  CG2  . THR   B 254 ? 0.3616 0.3420 0.4056 -0.0022 0.0212  0.0048  759  THR   B CG2  
3978 N  N    . GLY   B 255 ? 0.3894 0.3697 0.4326 0.0021  0.0176  0.0020  760  GLY   B N    
3979 C  CA   . GLY   B 255 ? 0.3460 0.3279 0.3858 0.0049  0.0169  0.0014  760  GLY   B CA   
3980 C  C    . GLY   B 255 ? 0.3684 0.3472 0.4070 0.0050  0.0179  0.0029  760  GLY   B C    
3981 O  O    . GLY   B 255 ? 0.3604 0.3354 0.4006 0.0026  0.0192  0.0043  760  GLY   B O    
3982 N  N    . TYR   B 256 ? 0.3287 0.3103 0.3644 0.0080  0.0173  0.0028  761  TYR   B N    
3983 C  CA   . TYR   B 256 ? 0.3747 0.3518 0.4086 0.0093  0.0171  0.0040  761  TYR   B CA   
3984 C  C    . TYR   B 256 ? 0.4033 0.3715 0.4373 0.0106  0.0150  0.0027  761  TYR   B C    
3985 O  O    . TYR   B 256 ? 0.4227 0.3899 0.4565 0.0131  0.0129  -0.0001 761  TYR   B O    
3986 C  CB   . TYR   B 256 ? 0.3791 0.3621 0.4103 0.0133  0.0163  0.0038  761  TYR   B CB   
3987 C  CG   . TYR   B 256 ? 0.3806 0.3725 0.4114 0.0112  0.0177  0.0054  761  TYR   B CG   
3988 C  CD1  . TYR   B 256 ? 0.3620 0.3531 0.3933 0.0065  0.0194  0.0070  761  TYR   B CD1  
3989 C  CD2  . TYR   B 256 ? 0.3742 0.3757 0.4041 0.0141  0.0171  0.0050  761  TYR   B CD2  
3990 C  CE1  . TYR   B 256 ? 0.3531 0.3507 0.3833 0.0041  0.0199  0.0084  761  TYR   B CE1  
3991 C  CE2  . TYR   B 256 ? 0.3985 0.4086 0.4283 0.0112  0.0179  0.0068  761  TYR   B CE2  
3992 C  CZ   . TYR   B 256 ? 0.3565 0.3636 0.3861 0.0059  0.0190  0.0085  761  TYR   B CZ   
3993 O  OH   . TYR   B 256 ? 0.3725 0.3864 0.4012 0.0025  0.0190  0.0103  761  TYR   B OH   
3994 N  N    . GLY   B 257 ? 0.3897 0.3508 0.4232 0.0086  0.0152  0.0050  762  GLY   B N    
3995 C  CA   . GLY   B 257 ? 0.4112 0.3622 0.4439 0.0089  0.0125  0.0046  762  GLY   B CA   
3996 C  C    . GLY   B 257 ? 0.4377 0.3822 0.4662 0.0103  0.0115  0.0071  762  GLY   B C    
3997 O  O    . GLY   B 257 ? 0.4221 0.3704 0.4491 0.0098  0.0134  0.0095  762  GLY   B O    
3998 N  N    . ILE   B 258 ? 0.4610 0.3948 0.4872 0.0118  0.0079  0.0065  763  ILE   B N    
3999 C  CA   . ILE   B 258 ? 0.4318 0.3561 0.4535 0.0122  0.0061  0.0096  763  ILE   B CA   
4000 C  C    . ILE   B 258 ? 0.4387 0.3588 0.4622 0.0047  0.0078  0.0137  763  ILE   B C    
4001 O  O    . ILE   B 258 ? 0.4516 0.3685 0.4784 0.0008  0.0071  0.0131  763  ILE   B O    
4002 C  CB   . ILE   B 258 ? 0.4771 0.3896 0.4948 0.0171  0.0007  0.0070  763  ILE   B CB   
4003 C  CG1  . ILE   B 258 ? 0.5122 0.4321 0.5289 0.0252  -0.0003 0.0023  763  ILE   B CG1  
4004 C  CG2  . ILE   B 258 ? 0.5178 0.4182 0.5299 0.0176  -0.0020 0.0108  763  ILE   B CG2  
4005 C  CD1  . ILE   B 258 ? 0.5353 0.4589 0.5488 0.0308  -0.0007 0.0031  763  ILE   B CD1  
4006 N  N    . ALA   B 259 ? 0.4289 0.3506 0.4504 0.0024  0.0102  0.0178  764  ALA   B N    
4007 C  CA   . ALA   B 259 ? 0.4548 0.3744 0.4774 -0.0047 0.0125  0.0220  764  ALA   B CA   
4008 C  C    . ALA   B 259 ? 0.4339 0.3394 0.4517 -0.0065 0.0088  0.0256  764  ALA   B C    
4009 O  O    . ALA   B 259 ? 0.5103 0.4096 0.5221 -0.0022 0.0062  0.0267  764  ALA   B O    
4010 C  CB   . ALA   B 259 ? 0.4227 0.3508 0.4445 -0.0066 0.0170  0.0246  764  ALA   B CB   
4011 N  N    . LEU   B 260 ? 0.4519 0.3525 0.4723 -0.0130 0.0084  0.0277  765  LEU   B N    
4012 C  CA   . LEU   B 260 ? 0.4835 0.3696 0.4992 -0.0165 0.0046  0.0320  765  LEU   B CA   
4013 C  C    . LEU   B 260 ? 0.5122 0.4016 0.5303 -0.0258 0.0081  0.0376  765  LEU   B C    
4014 O  O    . LEU   B 260 ? 0.4526 0.3548 0.4774 -0.0290 0.0127  0.0369  765  LEU   B O    
4015 C  CB   . LEU   B 260 ? 0.5020 0.3758 0.5176 -0.0159 -0.0013 0.0289  765  LEU   B CB   
4016 C  CG   . LEU   B 260 ? 0.4976 0.3690 0.5107 -0.0063 -0.0047 0.0227  765  LEU   B CG   
4017 C  CD1  . LEU   B 260 ? 0.5415 0.4236 0.5611 -0.0051 -0.0031 0.0173  765  LEU   B CD1  
4018 C  CD2  . LEU   B 260 ? 0.5754 0.4278 0.5827 -0.0045 -0.0118 0.0220  765  LEU   B CD2  
4019 N  N    . GLN   B 261 ? 0.4722 0.3501 0.4847 -0.0300 0.0058  0.0434  766  GLN   B N    
4020 C  CA   . GLN   B 261 ? 0.5316 0.4139 0.5461 -0.0396 0.0093  0.0493  766  GLN   B CA   
4021 C  C    . GLN   B 261 ? 0.5260 0.4116 0.5490 -0.0457 0.0090  0.0481  766  GLN   B C    
4022 O  O    . GLN   B 261 ? 0.5340 0.4109 0.5581 -0.0442 0.0040  0.0443  766  GLN   B O    
4023 C  CB   . GLN   B 261 ? 0.5730 0.4410 0.5791 -0.0437 0.0061  0.0565  766  GLN   B CB   
4024 C  CG   . GLN   B 261 ? 0.6079 0.4727 0.6055 -0.0369 0.0056  0.0575  766  GLN   B CG   
4025 C  CD   . GLN   B 261 ? 0.6892 0.5391 0.6772 -0.0403 0.0020  0.0649  766  GLN   B CD   
4026 O  OE1  . GLN   B 261 ? 0.6550 0.4971 0.6424 -0.0491 0.0004  0.0703  766  GLN   B OE1  
4027 N  NE2  . GLN   B 261 ? 0.6378 0.4839 0.6183 -0.0336 0.0004  0.0657  766  GLN   B NE2  
4028 N  N    . LYS   B 262 ? 0.5370 0.4365 0.5660 -0.0520 0.0145  0.0508  767  LYS   B N    
4029 C  CA   . LYS   B 262 ? 0.5684 0.4736 0.6065 -0.0583 0.0143  0.0502  767  LYS   B CA   
4030 C  C    . LYS   B 262 ? 0.6242 0.5128 0.6597 -0.0650 0.0079  0.0537  767  LYS   B C    
4031 O  O    . LYS   B 262 ? 0.6296 0.5095 0.6589 -0.0702 0.0069  0.0604  767  LYS   B O    
4032 C  CB   . LYS   B 262 ? 0.5432 0.4666 0.5876 -0.0641 0.0213  0.0535  767  LYS   B CB   
4033 C  CG   . LYS   B 262 ? 0.5873 0.5269 0.6380 -0.0584 0.0259  0.0480  767  LYS   B CG   
4034 C  CD   . LYS   B 262 ? 0.6534 0.6105 0.7135 -0.0640 0.0309  0.0495  767  LYS   B CD   
4035 C  CE   . LYS   B 262 ? 0.6400 0.6081 0.7081 -0.0587 0.0320  0.0430  767  LYS   B CE   
4036 N  NZ   . LYS   B 262 ? 0.6547 0.6404 0.7331 -0.0634 0.0360  0.0439  767  LYS   B NZ   
4037 N  N    . GLY   B 263 ? 0.7052 0.5882 0.7443 -0.0647 0.0031  0.0492  768  GLY   B N    
4038 C  CA   . GLY   B 263 ? 0.6753 0.5404 0.7114 -0.0707 -0.0042 0.0514  768  GLY   B CA   
4039 C  C    . GLY   B 263 ? 0.7262 0.5699 0.7514 -0.0640 -0.0107 0.0497  768  GLY   B C    
4040 O  O    . GLY   B 263 ? 0.8134 0.6385 0.8333 -0.0689 -0.0171 0.0528  768  GLY   B O    
4041 N  N    . SER   B 264 ? 0.5969 0.4426 0.6187 -0.0530 -0.0096 0.0450  769  SER   B N    
4042 C  CA   . SER   B 264 ? 0.6503 0.4782 0.6621 -0.0452 -0.0153 0.0433  769  SER   B CA   
4043 C  C    . SER   B 264 ? 0.7066 0.5174 0.7159 -0.0443 -0.0234 0.0389  769  SER   B C    
4044 O  O    . SER   B 264 ? 0.7330 0.5499 0.7482 -0.0436 -0.0239 0.0333  769  SER   B O    
4045 C  CB   . SER   B 264 ? 0.6478 0.4850 0.6587 -0.0339 -0.0125 0.0380  769  SER   B CB   
4046 O  OG   . SER   B 264 ? 0.6475 0.4697 0.6503 -0.0253 -0.0184 0.0350  769  SER   B OG   
4047 N  N    . PRO   B 265 ? 0.6817 0.4702 0.6815 -0.0435 -0.0304 0.0409  770  PRO   B N    
4048 C  CA   . PRO   B 265 ? 0.7535 0.5238 0.7492 -0.0405 -0.0388 0.0354  770  PRO   B CA   
4049 C  C    . PRO   B 265 ? 0.7623 0.5328 0.7548 -0.0263 -0.0403 0.0266  770  PRO   B C    
4050 O  O    . PRO   B 265 ? 0.7895 0.5462 0.7779 -0.0220 -0.0470 0.0208  770  PRO   B O    
4051 C  CB   . PRO   B 265 ? 0.7329 0.4785 0.7185 -0.0443 -0.0457 0.0413  770  PRO   B CB   
4052 C  CG   . PRO   B 265 ? 0.7594 0.5102 0.7412 -0.0414 -0.0413 0.0467  770  PRO   B CG   
4053 C  CD   . PRO   B 265 ? 0.7002 0.4783 0.6917 -0.0445 -0.0313 0.0480  770  PRO   B CD   
4054 N  N    . TRP   B 266 ? 0.6824 0.4683 0.6763 -0.0190 -0.0345 0.0255  771  TRP   B N    
4055 C  CA   . TRP   B 266 ? 0.6811 0.4706 0.6729 -0.0062 -0.0353 0.0179  771  TRP   B CA   
4056 C  C    . TRP   B 266 ? 0.6555 0.4635 0.6552 -0.0048 -0.0309 0.0125  771  TRP   B C    
4057 O  O    . TRP   B 266 ? 0.6111 0.4228 0.6094 0.0047  -0.0317 0.0058  771  TRP   B O    
4058 C  CB   . TRP   B 266 ? 0.6542 0.4503 0.6428 0.0010  -0.0322 0.0198  771  TRP   B CB   
4059 C  CG   . TRP   B 266 ? 0.6891 0.4673 0.6685 0.0024  -0.0370 0.0246  771  TRP   B CG   
4060 C  CD1  . TRP   B 266 ? 0.6548 0.4320 0.6321 -0.0038 -0.0349 0.0329  771  TRP   B CD1  
4061 C  CD2  . TRP   B 266 ? 0.6396 0.3984 0.6100 0.0113  -0.0449 0.0213  771  TRP   B CD2  
4062 N  NE1  . TRP   B 266 ? 0.6398 0.3975 0.6072 0.0002  -0.0413 0.0356  771  TRP   B NE1  
4063 C  CE2  . TRP   B 266 ? 0.6898 0.4355 0.6530 0.0098  -0.0477 0.0284  771  TRP   B CE2  
4064 C  CE3  . TRP   B 266 ? 0.6539 0.4049 0.6210 0.0209  -0.0501 0.0129  771  TRP   B CE3  
4065 C  CZ2  . TRP   B 266 ? 0.7808 0.5048 0.7338 0.0177  -0.0559 0.0274  771  TRP   B CZ2  
4066 C  CZ3  . TRP   B 266 ? 0.7297 0.4599 0.6869 0.0292  -0.0580 0.0114  771  TRP   B CZ3  
4067 C  CH2  . TRP   B 266 ? 0.7335 0.4500 0.6839 0.0277  -0.0610 0.0186  771  TRP   B CH2  
4068 N  N    . LYS   B 267 ? 0.5904 0.4108 0.5984 -0.0138 -0.0263 0.0152  772  LYS   B N    
4069 C  CA   . LYS   B 267 ? 0.6098 0.4487 0.6251 -0.0120 -0.0216 0.0111  772  LYS   B CA   
4070 C  C    . LYS   B 267 ? 0.5689 0.4035 0.5835 -0.0080 -0.0262 0.0038  772  LYS   B C    
4071 O  O    . LYS   B 267 ? 0.5447 0.3881 0.5590 -0.0001 -0.0249 -0.0014 772  LYS   B O    
4072 C  CB   . LYS   B 267 ? 0.6353 0.4871 0.6594 -0.0217 -0.0166 0.0154  772  LYS   B CB   
4073 C  CG   . LYS   B 267 ? 0.6502 0.5184 0.6814 -0.0203 -0.0131 0.0112  772  LYS   B CG   
4074 C  CD   . LYS   B 267 ? 0.6424 0.5222 0.6826 -0.0291 -0.0093 0.0147  772  LYS   B CD   
4075 C  CE   . LYS   B 267 ? 0.6798 0.5717 0.7264 -0.0277 -0.0082 0.0101  772  LYS   B CE   
4076 N  NZ   . LYS   B 267 ? 0.6922 0.5938 0.7376 -0.0196 -0.0047 0.0070  772  LYS   B NZ   
4077 N  N    . ARG   B 268 ? 0.6179 0.4388 0.6314 -0.0136 -0.0320 0.0035  773  ARG   B N    
4078 C  CA   . ARG   B 268 ? 0.6158 0.4324 0.6281 -0.0104 -0.0368 -0.0037 773  ARG   B CA   
4079 C  C    . ARG   B 268 ? 0.6205 0.4301 0.6243 0.0022  -0.0400 -0.0102 773  ARG   B C    
4080 O  O    . ARG   B 268 ? 0.5824 0.3999 0.5861 0.0083  -0.0397 -0.0164 773  ARG   B O    
4081 C  CB   . ARG   B 268 ? 0.6448 0.4453 0.6562 -0.0191 -0.0435 -0.0028 773  ARG   B CB   
4082 C  CG   . ARG   B 268 ? 0.7772 0.5671 0.7837 -0.0145 -0.0505 -0.0109 773  ARG   B CG   
4083 C  CD   . ARG   B 268 ? 0.8457 0.6288 0.8556 -0.0251 -0.0556 -0.0107 773  ARG   B CD   
4084 N  NE   . ARG   B 268 ? 0.9344 0.7378 0.9562 -0.0331 -0.0500 -0.0072 773  ARG   B NE   
4085 C  CZ   . ARG   B 268 ? 0.8907 0.7088 0.9177 -0.0310 -0.0481 -0.0115 773  ARG   B CZ   
4086 N  NH1  . ARG   B 268 ? 0.6990 0.5149 0.7203 -0.0219 -0.0508 -0.0192 773  ARG   B NH1  
4087 N  NH2  . ARG   B 268 ? 0.9022 0.7379 0.9399 -0.0378 -0.0433 -0.0079 773  ARG   B NH2  
4088 N  N    . GLN   B 269 ? 0.6228 0.4183 0.6190 0.0066  -0.0432 -0.0087 774  GLN   B N    
4089 C  CA   . GLN   B 269 ? 0.6041 0.3938 0.5925 0.0196  -0.0465 -0.0152 774  GLN   B CA   
4090 C  C    . GLN   B 269 ? 0.5654 0.3765 0.5568 0.0272  -0.0398 -0.0167 774  GLN   B C    
4091 O  O    . GLN   B 269 ? 0.5744 0.3908 0.5631 0.0366  -0.0404 -0.0234 774  GLN   B O    
4092 C  CB   . GLN   B 269 ? 0.6512 0.4202 0.6310 0.0226  -0.0519 -0.0127 774  GLN   B CB   
4093 C  CG   . GLN   B 269 ? 0.7336 0.4766 0.7066 0.0193  -0.0612 -0.0142 774  GLN   B CG   
4094 C  CD   . GLN   B 269 ? 0.8511 0.5737 0.8128 0.0300  -0.0682 -0.0172 774  GLN   B CD   
4095 O  OE1  . GLN   B 269 ? 0.8624 0.5762 0.8205 0.0297  -0.0691 -0.0113 774  GLN   B OE1  
4096 N  NE2  . GLN   B 269 ? 0.8740 0.5889 0.8295 0.0400  -0.0733 -0.0265 774  GLN   B NE2  
4097 N  N    . ILE   B 270 ? 0.5376 0.3615 0.5344 0.0228  -0.0335 -0.0107 775  ILE   B N    
4098 C  CA   . ILE   B 270 ? 0.5369 0.3806 0.5367 0.0283  -0.0276 -0.0116 775  ILE   B CA   
4099 C  C    . ILE   B 270 ? 0.5583 0.4164 0.5631 0.0279  -0.0247 -0.0155 775  ILE   B C    
4100 O  O    . ILE   B 270 ? 0.4991 0.3680 0.5029 0.0355  -0.0233 -0.0198 775  ILE   B O    
4101 C  CB   . ILE   B 270 ? 0.5391 0.3913 0.5428 0.0230  -0.0222 -0.0044 775  ILE   B CB   
4102 C  CG1  . ILE   B 270 ? 0.5567 0.3961 0.5542 0.0250  -0.0251 -0.0005 775  ILE   B CG1  
4103 C  CG2  . ILE   B 270 ? 0.5097 0.3826 0.5174 0.0263  -0.0163 -0.0052 775  ILE   B CG2  
4104 C  CD1  . ILE   B 270 ? 0.6228 0.4630 0.6153 0.0369  -0.0270 -0.0040 775  ILE   B CD1  
4105 N  N    . ASP   B 271 ? 0.5280 0.3875 0.5383 0.0189  -0.0239 -0.0136 776  ASP   B N    
4106 C  CA   . ASP   B 271 ? 0.4986 0.3699 0.5133 0.0180  -0.0222 -0.0170 776  ASP   B CA   
4107 C  C    . ASP   B 271 ? 0.5098 0.3762 0.5187 0.0253  -0.0267 -0.0245 776  ASP   B C    
4108 O  O    . ASP   B 271 ? 0.4918 0.3709 0.5006 0.0304  -0.0244 -0.0279 776  ASP   B O    
4109 C  CB   . ASP   B 271 ? 0.5016 0.3721 0.5225 0.0076  -0.0223 -0.0141 776  ASP   B CB   
4110 C  CG   . ASP   B 271 ? 0.5988 0.4811 0.6267 0.0016  -0.0162 -0.0081 776  ASP   B CG   
4111 O  OD1  . ASP   B 271 ? 0.5570 0.4486 0.5847 0.0051  -0.0118 -0.0068 776  ASP   B OD1  
4112 O  OD2  . ASP   B 271 ? 0.5747 0.4575 0.6081 -0.0067 -0.0158 -0.0049 776  ASP   B OD2  
4113 N  N    . LEU   B 272 ? 0.5298 0.3777 0.5333 0.0255  -0.0335 -0.0270 777  LEU   B N    
4114 C  CA   . LEU   B 272 ? 0.5292 0.3711 0.5261 0.0329  -0.0383 -0.0350 777  LEU   B CA   
4115 C  C    . LEU   B 272 ? 0.5494 0.3975 0.5411 0.0451  -0.0371 -0.0390 777  LEU   B C    
4116 O  O    . LEU   B 272 ? 0.5860 0.4423 0.5749 0.0517  -0.0369 -0.0449 777  LEU   B O    
4117 C  CB   . LEU   B 272 ? 0.5682 0.3862 0.5593 0.0308  -0.0466 -0.0369 777  LEU   B CB   
4118 C  CG   . LEU   B 272 ? 0.5941 0.4075 0.5907 0.0184  -0.0487 -0.0339 777  LEU   B CG   
4119 C  CD1  . LEU   B 272 ? 0.7509 0.5394 0.7414 0.0150  -0.0572 -0.0345 777  LEU   B CD1  
4120 C  CD2  . LEU   B 272 ? 0.5977 0.4216 0.5970 0.0177  -0.0487 -0.0384 777  LEU   B CD2  
4121 N  N    . ALA   B 273 ? 0.5178 0.3633 0.5080 0.0483  -0.0362 -0.0358 778  ALA   B N    
4122 C  CA   . ALA   B 273 ? 0.5195 0.3731 0.5059 0.0599  -0.0350 -0.0392 778  ALA   B CA   
4123 C  C    . ALA   B 273 ? 0.5506 0.4291 0.5425 0.0606  -0.0280 -0.0385 778  ALA   B C    
4124 O  O    . ALA   B 273 ? 0.5020 0.3912 0.4913 0.0687  -0.0272 -0.0437 778  ALA   B O    
4125 C  CB   . ALA   B 273 ? 0.5307 0.3766 0.5150 0.0624  -0.0359 -0.0350 778  ALA   B CB   
4126 N  N    . LEU   B 274 ? 0.4572 0.3452 0.4564 0.0519  -0.0230 -0.0322 779  LEU   B N    
4127 C  CA   . LEU   B 274 ? 0.4949 0.4040 0.4986 0.0514  -0.0170 -0.0312 779  LEU   B CA   
4128 C  C    . LEU   B 274 ? 0.5352 0.4506 0.5382 0.0522  -0.0174 -0.0358 779  LEU   B C    
4129 O  O    . LEU   B 274 ? 0.4335 0.3634 0.4354 0.0574  -0.0149 -0.0383 779  LEU   B O    
4130 C  CB   . LEU   B 274 ? 0.4730 0.3875 0.4835 0.0419  -0.0127 -0.0244 779  LEU   B CB   
4131 C  CG   . LEU   B 274 ? 0.4412 0.3545 0.4523 0.0412  -0.0111 -0.0194 779  LEU   B CG   
4132 C  CD1  . LEU   B 274 ? 0.4936 0.4123 0.5107 0.0321  -0.0068 -0.0138 779  LEU   B CD1  
4133 C  CD2  . LEU   B 274 ? 0.4262 0.3517 0.4358 0.0489  -0.0092 -0.0205 779  LEU   B CD2  
4134 N  N    . LEU   B 275 ? 0.4828 0.3880 0.4862 0.0468  -0.0206 -0.0368 780  LEU   B N    
4135 C  CA   . LEU   B 275 ? 0.5143 0.4243 0.5162 0.0474  -0.0217 -0.0412 780  LEU   B CA   
4136 C  C    . LEU   B 275 ? 0.5081 0.4156 0.5016 0.0578  -0.0251 -0.0488 780  LEU   B C    
4137 O  O    . LEU   B 275 ? 0.5663 0.4850 0.5576 0.0611  -0.0240 -0.0523 780  LEU   B O    
4138 C  CB   . LEU   B 275 ? 0.4462 0.3457 0.4507 0.0393  -0.0252 -0.0406 780  LEU   B CB   
4139 C  CG   . LEU   B 275 ? 0.4375 0.3435 0.4509 0.0299  -0.0211 -0.0338 780  LEU   B CG   
4140 C  CD1  . LEU   B 275 ? 0.4569 0.3533 0.4736 0.0220  -0.0249 -0.0331 780  LEU   B CD1  
4141 C  CD2  . LEU   B 275 ? 0.4141 0.3375 0.4308 0.0294  -0.0164 -0.0325 780  LEU   B CD2  
4142 N  N    . GLN   B 276 ? 0.5169 0.4099 0.5051 0.0634  -0.0294 -0.0514 781  GLN   B N    
4143 C  CA   . GLN   B 276 ? 0.5821 0.4734 0.5619 0.0751  -0.0325 -0.0593 781  GLN   B CA   
4144 C  C    . GLN   B 276 ? 0.5579 0.4704 0.5383 0.0824  -0.0271 -0.0596 781  GLN   B C    
4145 O  O    . GLN   B 276 ? 0.5899 0.5132 0.5662 0.0891  -0.0264 -0.0649 781  GLN   B O    
4146 C  CB   . GLN   B 276 ? 0.5799 0.4493 0.5535 0.0801  -0.0388 -0.0618 781  GLN   B CB   
4147 C  CG   . GLN   B 276 ? 0.6682 0.5346 0.6325 0.0939  -0.0424 -0.0706 781  GLN   B CG   
4148 C  CD   . GLN   B 276 ? 0.8013 0.6531 0.7612 0.1012  -0.0465 -0.0711 781  GLN   B CD   
4149 O  OE1  . GLN   B 276 ? 0.8091 0.6383 0.7665 0.0970  -0.0520 -0.0694 781  GLN   B OE1  
4150 N  NE2  . GLN   B 276 ? 0.8478 0.7128 0.8065 0.1121  -0.0440 -0.0733 781  GLN   B NE2  
4151 N  N    . PHE   B 277 ? 0.5296 0.4491 0.5149 0.0810  -0.0234 -0.0539 782  PHE   B N    
4152 C  CA   . PHE   B 277 ? 0.5431 0.4841 0.5302 0.0863  -0.0183 -0.0533 782  PHE   B CA   
4153 C  C    . PHE   B 277 ? 0.5525 0.5117 0.5420 0.0823  -0.0139 -0.0525 782  PHE   B C    
4154 O  O    . PHE   B 277 ? 0.5573 0.5329 0.5447 0.0886  -0.0115 -0.0555 782  PHE   B O    
4155 C  CB   . PHE   B 277 ? 0.5205 0.4658 0.5132 0.0826  -0.0153 -0.0464 782  PHE   B CB   
4156 C  CG   . PHE   B 277 ? 0.5530 0.4808 0.5430 0.0857  -0.0195 -0.0458 782  PHE   B CG   
4157 C  CD1  . PHE   B 277 ? 0.6015 0.5136 0.5840 0.0943  -0.0256 -0.0519 782  PHE   B CD1  
4158 C  CD2  . PHE   B 277 ? 0.5032 0.4297 0.4974 0.0802  -0.0178 -0.0390 782  PHE   B CD2  
4159 C  CE1  . PHE   B 277 ? 0.5860 0.4804 0.5652 0.0969  -0.0301 -0.0507 782  PHE   B CE1  
4160 C  CE2  . PHE   B 277 ? 0.5656 0.4760 0.5565 0.0826  -0.0218 -0.0376 782  PHE   B CE2  
4161 C  CZ   . PHE   B 277 ? 0.5360 0.4299 0.5194 0.0909  -0.0281 -0.0432 782  PHE   B CZ   
4162 N  N    . VAL   B 278 ? 0.4757 0.4328 0.4698 0.0720  -0.0127 -0.0482 783  VAL   B N    
4163 C  CA   . VAL   B 278 ? 0.5583 0.5298 0.5542 0.0677  -0.0094 -0.0469 783  VAL   B CA   
4164 C  C    . VAL   B 278 ? 0.5778 0.5503 0.5667 0.0734  -0.0119 -0.0538 783  VAL   B C    
4165 O  O    . VAL   B 278 ? 0.5372 0.5265 0.5237 0.0771  -0.0090 -0.0552 783  VAL   B O    
4166 C  CB   . VAL   B 278 ? 0.5047 0.4708 0.5063 0.0569  -0.0089 -0.0418 783  VAL   B CB   
4167 C  CG1  . VAL   B 278 ? 0.5369 0.5124 0.5383 0.0535  -0.0077 -0.0418 783  VAL   B CG1  
4168 C  CG2  . VAL   B 278 ? 0.5068 0.4778 0.5145 0.0517  -0.0050 -0.0351 783  VAL   B CG2  
4169 N  N    . GLY   B 279 ? 0.6032 0.5580 0.5884 0.0736  -0.0175 -0.0580 784  GLY   B N    
4170 C  CA   . GLY   B 279 ? 0.6334 0.5875 0.6115 0.0778  -0.0205 -0.0646 784  GLY   B CA   
4171 C  C    . GLY   B 279 ? 0.6778 0.6393 0.6483 0.0902  -0.0206 -0.0714 784  GLY   B C    
4172 O  O    . GLY   B 279 ? 0.7083 0.6800 0.6735 0.0939  -0.0200 -0.0755 784  GLY   B O    
4173 N  N    . ASP   B 280 ? 0.6750 0.6326 0.6447 0.0971  -0.0213 -0.0727 785  ASP   B N    
4174 C  CA   . ASP   B 280 ? 0.6860 0.6509 0.6490 0.1104  -0.0217 -0.0797 785  ASP   B CA   
4175 C  C    . ASP   B 280 ? 0.7188 0.7103 0.6854 0.1132  -0.0149 -0.0767 785  ASP   B C    
4176 O  O    . ASP   B 280 ? 0.7103 0.7111 0.6730 0.1246  -0.0144 -0.0818 785  ASP   B O    
4177 C  CB   . ASP   B 280 ? 0.7647 0.7108 0.7241 0.1178  -0.0269 -0.0832 785  ASP   B CB   
4178 C  CG   . ASP   B 280 ? 0.9273 0.8460 0.8840 0.1127  -0.0338 -0.0843 785  ASP   B CG   
4179 O  OD1  . ASP   B 280 ? 0.9303 0.8460 0.8879 0.1045  -0.0346 -0.0835 785  ASP   B OD1  
4180 O  OD2  . ASP   B 280 ? 1.0064 0.9067 0.9602 0.1165  -0.0386 -0.0857 785  ASP   B OD2  
4181 N  N    . GLY   B 281 ? 0.6684 0.6723 0.6424 0.1034  -0.0099 -0.0688 786  GLY   B N    
4182 C  CA   . GLY   B 281 ? 0.6418 0.6710 0.6192 0.1045  -0.0040 -0.0656 786  GLY   B CA   
4183 C  C    . GLY   B 281 ? 0.6882 0.7222 0.6709 0.1065  -0.0024 -0.0622 786  GLY   B C    
4184 O  O    . GLY   B 281 ? 0.6685 0.7243 0.6551 0.1064  0.0023  -0.0590 786  GLY   B O    
4185 N  N    . GLU   B 282 ? 0.6713 0.6859 0.6545 0.1076  -0.0063 -0.0622 787  GLU   B N    
4186 C  CA   . GLU   B 282 ? 0.6976 0.7162 0.6848 0.1105  -0.0055 -0.0593 787  GLU   B CA   
4187 C  C    . GLU   B 282 ? 0.6873 0.7160 0.6826 0.0998  -0.0010 -0.0505 787  GLU   B C    
4188 O  O    . GLU   B 282 ? 0.6699 0.7104 0.6689 0.1018  0.0009  -0.0479 787  GLU   B O    
4189 C  CB   . GLU   B 282 ? 0.6801 0.6737 0.6647 0.1133  -0.0112 -0.0607 787  GLU   B CB   
4190 C  CG   . GLU   B 282 ? 0.7921 0.7750 0.7684 0.1260  -0.0164 -0.0695 787  GLU   B CG   
4191 C  CD   . GLU   B 282 ? 0.8072 0.7624 0.7801 0.1273  -0.0228 -0.0699 787  GLU   B CD   
4192 O  OE1  . GLU   B 282 ? 0.8181 0.7536 0.7847 0.1280  -0.0280 -0.0745 787  GLU   B OE1  
4193 O  OE2  . GLU   B 282 ? 0.8023 0.7554 0.7783 0.1273  -0.0229 -0.0655 787  GLU   B OE2  
4194 N  N    . MET   B 283 ? 0.5908 0.6150 0.5886 0.0888  0.0002  -0.0463 788  MET   B N    
4195 C  CA   . MET   B 283 ? 0.6048 0.6359 0.6092 0.0794  0.0037  -0.0386 788  MET   B CA   
4196 C  C    . MET   B 283 ? 0.6492 0.7049 0.6559 0.0779  0.0083  -0.0361 788  MET   B C    
4197 O  O    . MET   B 283 ? 0.6014 0.6664 0.6129 0.0737  0.0107  -0.0311 788  MET   B O    
4198 C  CB   . MET   B 283 ? 0.5912 0.6100 0.5977 0.0691  0.0033  -0.0351 788  MET   B CB   
4199 C  CG   . MET   B 283 ? 0.6106 0.6072 0.6167 0.0678  -0.0005 -0.0353 788  MET   B CG   
4200 S  SD   . MET   B 283 ? 0.6539 0.6458 0.6649 0.0621  0.0007  -0.0287 788  MET   B SD   
4201 C  CE   . MET   B 283 ? 0.4821 0.4523 0.4938 0.0550  -0.0021 -0.0272 788  MET   B CE   
4202 N  N    . GLU   B 284 ? 0.7020 0.7685 0.7050 0.0809  0.0094  -0.0394 789  GLU   B N    
4203 C  CA   . GLU   B 284 ? 0.7069 0.7978 0.7116 0.0787  0.0138  -0.0365 789  GLU   B CA   
4204 C  C    . GLU   B 284 ? 0.6996 0.8067 0.7077 0.0840  0.0155  -0.0360 789  GLU   B C    
4205 O  O    . GLU   B 284 ? 0.6913 0.8142 0.7040 0.0780  0.0186  -0.0305 789  GLU   B O    
4206 C  CB   . GLU   B 284 ? 0.7158 0.8161 0.7145 0.0829  0.0145  -0.0409 789  GLU   B CB   
4207 N  N    . GLU   B 285 ? 0.7342 0.8369 0.7399 0.0954  0.0129  -0.0418 790  GLU   B N    
4208 C  CA   . GLU   B 285 ? 0.7072 0.8250 0.7164 0.1020  0.0137  -0.0418 790  GLU   B CA   
4209 C  C    . GLU   B 285 ? 0.6727 0.7881 0.6881 0.0943  0.0140  -0.0350 790  GLU   B C    
4210 O  O    . GLU   B 285 ? 0.6014 0.7366 0.6217 0.0924  0.0166  -0.0314 790  GLU   B O    
4211 C  CB   . GLU   B 285 ? 0.8048 0.9124 0.8095 0.1159  0.0096  -0.0493 790  GLU   B CB   
4212 C  CG   . GLU   B 285 ? 0.9360 1.0354 0.9326 0.1229  0.0075  -0.0569 790  GLU   B CG   
4213 C  CD   . GLU   B 285 ? 1.0838 1.1578 1.0749 0.1315  0.0012  -0.0628 790  GLU   B CD   
4214 O  OE1  . GLU   B 285 ? 1.1294 1.1914 1.1228 0.1313  -0.0013 -0.0601 790  GLU   B OE1  
4215 O  OE2  . GLU   B 285 ? 0.9762 1.0417 0.9599 0.1384  -0.0015 -0.0700 790  GLU   B OE2  
4216 N  N    . LEU   B 286 ? 0.6101 0.7019 0.6249 0.0897  0.0113  -0.0333 791  LEU   B N    
4217 C  CA   . LEU   B 286 ? 0.5970 0.6855 0.6164 0.0828  0.0115  -0.0273 791  LEU   B CA   
4218 C  C    . LEU   B 286 ? 0.5513 0.6511 0.5746 0.0712  0.0150  -0.0213 791  LEU   B C    
4219 O  O    . LEU   B 286 ? 0.5174 0.6282 0.5449 0.0674  0.0163  -0.0171 791  LEU   B O    
4220 C  CB   . LEU   B 286 ? 0.4917 0.5539 0.5093 0.0802  0.0082  -0.0267 791  LEU   B CB   
4221 C  CG   . LEU   B 286 ? 0.5772 0.6249 0.5905 0.0905  0.0037  -0.0315 791  LEU   B CG   
4222 C  CD1  . LEU   B 286 ? 0.5477 0.5712 0.5597 0.0860  0.0008  -0.0290 791  LEU   B CD1  
4223 C  CD2  . LEU   B 286 ? 0.6034 0.6647 0.6183 0.0991  0.0033  -0.0323 791  LEU   B CD2  
4224 N  N    . GLU   B 287 ? 0.5218 0.6185 0.5433 0.0655  0.0162  -0.0208 792  GLU   B N    
4225 C  CA   . GLU   B 287 ? 0.5142 0.6197 0.5382 0.0549  0.0188  -0.0151 792  GLU   B CA   
4226 C  C    . GLU   B 287 ? 0.5189 0.6504 0.5453 0.0548  0.0216  -0.0132 792  GLU   B C    
4227 O  O    . GLU   B 287 ? 0.4852 0.6252 0.5153 0.0474  0.0228  -0.0079 792  GLU   B O    
4228 C  CB   . GLU   B 287 ? 0.4996 0.5979 0.5205 0.0506  0.0190  -0.0154 792  GLU   B CB   
4229 C  CG   . GLU   B 287 ? 0.4639 0.5707 0.4860 0.0405  0.0212  -0.0096 792  GLU   B CG   
4230 C  CD   . GLU   B 287 ? 0.5370 0.6355 0.5558 0.0367  0.0207  -0.0096 792  GLU   B CD   
4231 O  OE1  . GLU   B 287 ? 0.5083 0.5977 0.5239 0.0421  0.0188  -0.0145 792  GLU   B OE1  
4232 O  OE2  . GLU   B 287 ? 0.5465 0.6474 0.5657 0.0283  0.0216  -0.0046 792  GLU   B OE2  
4233 N  N    . THR   B 288 ? 0.5553 0.7004 0.5795 0.0630  0.0226  -0.0175 793  THR   B N    
4234 C  CA   . THR   B 288 ? 0.5029 0.6759 0.5299 0.0633  0.0256  -0.0158 793  THR   B CA   
4235 C  C    . THR   B 288 ? 0.5413 0.7243 0.5737 0.0657  0.0252  -0.0144 793  THR   B C    
4236 O  O    . THR   B 288 ? 0.5005 0.7012 0.5375 0.0591  0.0270  -0.0093 793  THR   B O    
4237 C  CB   . THR   B 288 ? 0.5730 0.7580 0.5959 0.0734  0.0267  -0.0219 793  THR   B CB   
4238 O  OG1  . THR   B 288 ? 0.4888 0.6642 0.5061 0.0705  0.0267  -0.0229 793  THR   B OG1  
4239 C  CG2  . THR   B 288 ? 0.5597 0.7769 0.5857 0.0739  0.0305  -0.0200 793  THR   B CG2  
4240 N  N    . LEU   B 289 ? 0.4640 0.6351 0.4958 0.0748  0.0223  -0.0185 794  LEU   B N    
4241 C  CA   . LEU   B 289 ? 0.4633 0.6426 0.4997 0.0783  0.0211  -0.0174 794  LEU   B CA   
4242 C  C    . LEU   B 289 ? 0.4967 0.6723 0.5367 0.0667  0.0210  -0.0106 794  LEU   B C    
4243 O  O    . LEU   B 289 ? 0.4767 0.6707 0.5217 0.0638  0.0217  -0.0073 794  LEU   B O    
4244 C  CB   . LEU   B 289 ? 0.4822 0.6441 0.5155 0.0895  0.0172  -0.0225 794  LEU   B CB   
4245 C  CG   . LEU   B 289 ? 0.5787 0.7498 0.6154 0.0973  0.0153  -0.0231 794  LEU   B CG   
4246 C  CD1  . LEU   B 289 ? 0.6395 0.8411 0.6795 0.1050  0.0177  -0.0257 794  LEU   B CD1  
4247 C  CD2  . LEU   B 289 ? 0.5640 0.7120 0.5958 0.1073  0.0107  -0.0276 794  LEU   B CD2  
4248 N  N    . TRP   B 290 ? 0.4069 0.5597 0.4444 0.0598  0.0198  -0.0087 795  TRP   B N    
4249 C  CA   . TRP   B 290 ? 0.4345 0.5799 0.4741 0.0512  0.0190  -0.0038 795  TRP   B CA   
4250 C  C    . TRP   B 290 ? 0.4591 0.6034 0.4989 0.0386  0.0206  0.0011  795  TRP   B C    
4251 O  O    . TRP   B 290 ? 0.4768 0.6223 0.5186 0.0313  0.0201  0.0052  795  TRP   B O    
4252 C  CB   . TRP   B 290 ? 0.4536 0.5739 0.4903 0.0533  0.0163  -0.0050 795  TRP   B CB   
4253 C  CG   . TRP   B 290 ? 0.4746 0.5918 0.5104 0.0646  0.0136  -0.0085 795  TRP   B CG   
4254 C  CD1  . TRP   B 290 ? 0.4444 0.5490 0.4761 0.0736  0.0115  -0.0136 795  TRP   B CD1  
4255 C  CD2  . TRP   B 290 ? 0.4520 0.5778 0.4904 0.0682  0.0119  -0.0072 795  TRP   B CD2  
4256 N  NE1  . TRP   B 290 ? 0.4351 0.5389 0.4664 0.0828  0.0086  -0.0154 795  TRP   B NE1  
4257 C  CE2  . TRP   B 290 ? 0.4589 0.5762 0.4945 0.0799  0.0089  -0.0115 795  TRP   B CE2  
4258 C  CE3  . TRP   B 290 ? 0.4265 0.5654 0.4690 0.0625  0.0122  -0.0029 795  TRP   B CE3  
4259 C  CZ2  . TRP   B 290 ? 0.5034 0.6256 0.5403 0.0867  0.0061  -0.0113 795  TRP   B CZ2  
4260 C  CZ3  . TRP   B 290 ? 0.4634 0.6086 0.5075 0.0689  0.0096  -0.0028 795  TRP   B CZ3  
4261 C  CH2  . TRP   B 290 ? 0.4893 0.6262 0.5307 0.0811  0.0067  -0.0069 795  TRP   B CH2  
4262 N  N    . LEU   B 291 ? 0.4151 0.5559 0.4522 0.0360  0.0218  0.0006  796  LEU   B N    
4263 C  CA   . LEU   B 291 ? 0.4765 0.6088 0.5125 0.0252  0.0223  0.0047  796  LEU   B CA   
4264 C  C    . LEU   B 291 ? 0.5203 0.6689 0.5564 0.0186  0.0242  0.0082  796  LEU   B C    
4265 O  O    . LEU   B 291 ? 0.5919 0.7332 0.6265 0.0098  0.0240  0.0120  796  LEU   B O    
4266 C  CB   . LEU   B 291 ? 0.4572 0.5687 0.4897 0.0260  0.0214  0.0023  796  LEU   B CB   
4267 C  CG   . LEU   B 291 ? 0.4202 0.5133 0.4522 0.0301  0.0194  0.0000  796  LEU   B CG   
4268 C  CD1  . LEU   B 291 ? 0.4615 0.5364 0.4912 0.0288  0.0186  -0.0015 796  LEU   B CD1  
4269 C  CD2  . LEU   B 291 ? 0.4433 0.5331 0.4771 0.0255  0.0188  0.0034  796  LEU   B CD2  
4270 N  N    . THR   B 292 ? 0.5187 0.6894 0.5564 0.0226  0.0259  0.0074  797  THR   B N    
4271 C  CA   . THR   B 292 ? 0.5954 0.7834 0.6328 0.0158  0.0280  0.0115  797  THR   B CA   
4272 C  C    . THR   B 292 ? 0.6280 0.8251 0.6690 0.0054  0.0276  0.0177  797  THR   B C    
4273 O  O    . THR   B 292 ? 0.6515 0.8496 0.6960 0.0061  0.0262  0.0178  797  THR   B O    
4274 C  CB   . THR   B 292 ? 0.6498 0.8607 0.6879 0.0240  0.0305  0.0083  797  THR   B CB   
4275 O  OG1  . THR   B 292 ? 0.6566 0.8565 0.6906 0.0342  0.0300  0.0017  797  THR   B OG1  
4276 C  CG2  . THR   B 292 ? 0.7276 0.9567 0.7643 0.0168  0.0331  0.0128  797  THR   B CG2  
4277 N  N    . GLY   B 293 ? 0.6160 0.8184 0.6553 -0.0046 0.0283  0.0229  798  GLY   B N    
4278 C  CA   . GLY   B 293 ? 0.5892 0.7992 0.6309 -0.0158 0.0272  0.0291  798  GLY   B CA   
4279 C  C    . GLY   B 293 ? 0.6447 0.8738 0.6857 -0.0236 0.0290  0.0343  798  GLY   B C    
4280 O  O    . GLY   B 293 ? 0.6622 0.8905 0.6987 -0.0231 0.0305  0.0343  798  GLY   B O    
4281 N  N    . ILE   B 294 ? 0.6003 0.8468 0.6455 -0.0316 0.0287  0.0392  799  ILE   B N    
4282 C  CA   . ILE   B 294 ? 0.6429 0.9104 0.6880 -0.0405 0.0305  0.0453  799  ILE   B CA   
4283 C  C    . ILE   B 294 ? 0.6756 0.9258 0.7140 -0.0514 0.0286  0.0506  799  ILE   B C    
4284 O  O    . ILE   B 294 ? 0.5858 0.8461 0.6209 -0.0562 0.0303  0.0546  799  ILE   B O    
4285 C  CB   . ILE   B 294 ? 0.5904 0.8803 0.6423 -0.0473 0.0299  0.0495  799  ILE   B CB   
4286 C  CG1  . ILE   B 294 ? 0.6570 0.9666 0.7155 -0.0349 0.0318  0.0442  799  ILE   B CG1  
4287 C  CG2  . ILE   B 294 ? 0.6937 1.0047 0.7455 -0.0589 0.0314  0.0571  799  ILE   B CG2  
4288 C  CD1  . ILE   B 294 ? 0.6045 0.9278 0.6702 -0.0391 0.0297  0.0465  799  ILE   B CD1  
4289 N  N    . CYS   B 295 ? 0.6521 0.8762 0.6879 -0.0553 0.0249  0.0508  800  CYS   B N    
4290 C  CA   . CYS   B 295 ? 0.6498 0.8560 0.6790 -0.0647 0.0224  0.0555  800  CYS   B CA   
4291 C  C    . CYS   B 295 ? 0.6853 0.8761 0.7095 -0.0575 0.0232  0.0518  800  CYS   B C    
4292 O  O    . CYS   B 295 ? 0.7621 0.9518 0.7812 -0.0619 0.0232  0.0554  800  CYS   B O    
4293 C  CB   . CYS   B 295 ? 0.6487 0.8339 0.6768 -0.0712 0.0180  0.0569  800  CYS   B CB   
4294 S  SG   . CYS   B 295 ? 0.5900 0.7899 0.6238 -0.0786 0.0160  0.0598  800  CYS   B SG   
4295 N  N    . GLY   C .   ? 0.4099 0.3913 0.4223 0.0179  -0.0301 -0.0375 1001 GLY   A N    
4296 C  CA   . GLY   C .   ? 0.4286 0.4066 0.4332 0.0208  -0.0351 -0.0438 1001 GLY   A CA   
4297 C  C    . GLY   C .   ? 0.3790 0.3452 0.3862 0.0194  -0.0392 -0.0480 1001 GLY   A C    
4298 O  O    . GLY   C .   ? 0.3950 0.3551 0.3955 0.0218  -0.0441 -0.0542 1001 GLY   A O    
4299 O  OXT  . GLY   C .   ? 0.3758 0.3379 0.3915 0.0157  -0.0378 -0.0453 1001 GLY   A OXT  
4300 N  N    . GLU   D .   ? 0.3612 0.3476 0.3854 -0.0034 0.0233  0.0115  1001 GLU   B N    
4301 C  CA   . GLU   D .   ? 0.3735 0.3561 0.3950 -0.0054 0.0248  0.0115  1001 GLU   B CA   
4302 C  C    . GLU   D .   ? 0.3702 0.3489 0.3918 -0.0046 0.0267  0.0122  1001 GLU   B C    
4303 O  O    . GLU   D .   ? 0.3646 0.3420 0.3882 -0.0031 0.0264  0.0129  1001 GLU   B O    
4304 C  CB   . GLU   D .   ? 0.3934 0.3782 0.4102 -0.0069 0.0236  0.0122  1001 GLU   B CB   
4305 C  CG   . GLU   D .   ? 0.4145 0.4008 0.4301 -0.0098 0.0220  0.0117  1001 GLU   B CG   
4306 C  CD   . GLU   D .   ? 0.4080 0.3883 0.4234 -0.0108 0.0227  0.0101  1001 GLU   B CD   
4307 O  OE1  . GLU   D .   ? 0.4311 0.4070 0.4440 -0.0103 0.0242  0.0089  1001 GLU   B OE1  
4308 O  OE2  . GLU   D .   ? 0.4514 0.4319 0.4689 -0.0117 0.0215  0.0099  1001 GLU   B OE2  
4309 O  OXT  . GLU   D .   ? 0.3622 0.3389 0.3812 -0.0057 0.0285  0.0122  1001 GLU   B OXT  
4310 C  C10  . A1BRB E .   ? 0.4328 0.4768 0.4587 0.0178  0.0171  -0.0017 1002 A1BRB B C10  
4311 C  C11  . A1BRB E .   ? 0.4316 0.4872 0.4564 0.0233  0.0177  -0.0038 1002 A1BRB B C11  
4312 C  C13  . A1BRB E .   ? 0.4462 0.4422 0.4649 0.0360  0.0047  -0.0219 1002 A1BRB B C13  
4313 C  C14  . A1BRB E .   ? 0.3946 0.3877 0.4121 0.0346  0.0027  -0.0240 1002 A1BRB B C14  
4314 C  C16  . A1BRB E .   ? 0.4332 0.4039 0.4546 0.0309  -0.0009 -0.0238 1002 A1BRB B C16  
4315 C  C17  . A1BRB E .   ? 0.4150 0.3879 0.4367 0.0326  0.0012  -0.0216 1002 A1BRB B C17  
4316 C  C2   . A1BRB E .   ? 0.4456 0.4571 0.4634 0.0378  0.0077  -0.0205 1002 A1BRB B C2   
4317 C  C20  . A1BRB E .   ? 0.4499 0.4113 0.4757 0.0236  -0.0046 -0.0242 1002 A1BRB B C20  
4318 C  C21  . A1BRB E .   ? 0.4738 0.4394 0.5059 0.0176  -0.0016 -0.0192 1002 A1BRB B C21  
4319 C  C24  . A1BRB E .   ? 0.4109 0.3875 0.4420 0.0183  0.0019  -0.0169 1002 A1BRB B C24  
4320 C  C25  . A1BRB E .   ? 0.3922 0.3764 0.4216 0.0182  0.0019  -0.0170 1002 A1BRB B C25  
4321 C  C26  . A1BRB E .   ? 0.4227 0.4165 0.4507 0.0178  0.0048  -0.0142 1002 A1BRB B C26  
4322 C  C27  . A1BRB E .   ? 0.3810 0.3775 0.4098 0.0176  0.0075  -0.0117 1002 A1BRB B C27  
4323 C  C28  . A1BRB E .   ? 0.4303 0.4196 0.4608 0.0183  0.0075  -0.0120 1002 A1BRB B C28  
4324 C  C30  . A1BRB E .   ? 0.3824 0.3615 0.4138 0.0186  0.0048  -0.0143 1002 A1BRB B C30  
4325 C  C4   . A1BRB E .   ? 0.4335 0.4637 0.4536 0.0389  0.0118  -0.0161 1002 A1BRB B C4   
4326 C  C5   . A1BRB E .   ? 0.4121 0.4554 0.4289 0.0462  0.0122  -0.0198 1002 A1BRB B C5   
4327 C  C6   . A1BRB E .   ? 0.4757 0.5117 0.4952 0.0459  0.0117  -0.0178 1002 A1BRB B C6   
4328 C  C7   . A1BRB E .   ? 0.4567 0.4934 0.4795 0.0313  0.0142  -0.0108 1002 A1BRB B C7   
4329 C  C8   . A1BRB E .   ? 0.3966 0.4240 0.4215 0.0251  0.0141  -0.0082 1002 A1BRB B C8   
4330 F  F22  . A1BRB E .   ? 0.4604 0.4198 0.4956 0.0148  -0.0008 -0.0167 1002 A1BRB B F22  
4331 F  F23  . A1BRB E .   ? 0.4501 0.4152 0.4851 0.0143  -0.0035 -0.0196 1002 A1BRB B F23  
4332 N  N12  . A1BRB E .   ? 0.4346 0.4868 0.4577 0.0309  0.0163  -0.0086 1002 A1BRB B N12  
4333 N  N15  . A1BRB E .   ? 0.4552 0.4356 0.4743 0.0322  -0.0004 -0.0252 1002 A1BRB B N15  
4334 N  N18  . A1BRB E .   ? 0.3977 0.3835 0.4183 0.0353  0.0039  -0.0208 1002 A1BRB B N18  
4335 N  N3   . A1BRB E .   ? 0.4081 0.4222 0.4280 0.0380  0.0092  -0.0179 1002 A1BRB B N3   
4336 N  N9   . A1BRB E .   ? 0.4458 0.4766 0.4722 0.0188  0.0156  -0.0039 1002 A1BRB B N9   
4337 O  O1   . A1BRB E .   ? 0.4503 0.4721 0.4657 0.0385  0.0085  -0.0212 1002 A1BRB B O1   
4338 O  O19  . A1BRB E .   ? 0.5256 0.4844 0.5492 0.0273  -0.0038 -0.0242 1002 A1BRB B O19  
4339 CL CL29 . A1BRB E .   ? 0.4031 0.3956 0.4340 0.0184  0.0102  -0.0090 1002 A1BRB B CL29 
4340 O  O    . HOH   F .   ? 0.4375 0.5921 0.6546 0.0092  -0.0261 -0.0108 1101 HOH   A O    
4341 O  O    . HOH   F .   ? 0.7422 1.0274 0.5558 0.1831  0.0272  -0.1336 1102 HOH   A O    
4342 O  O    . HOH   F .   ? 0.4609 0.4954 0.5794 0.0431  -0.0430 -0.0045 1103 HOH   A O    
4343 O  O    . HOH   F .   ? 0.7990 0.6042 0.6751 0.0853  -0.1135 -0.1552 1104 HOH   A O    
4344 O  O    . HOH   F .   ? 0.6931 0.8426 0.9409 -0.1213 -0.0299 0.0204  1105 HOH   A O    
4345 O  O    . HOH   F .   ? 0.6419 0.7929 0.7946 0.0756  -0.1739 -0.0022 1106 HOH   A O    
4346 O  O    . HOH   F .   ? 0.7964 0.9388 0.6191 0.1771  -0.0090 -0.1502 1107 HOH   A O    
4347 O  O    . HOH   F .   ? 0.6241 0.6347 0.5979 0.0134  -0.0616 0.0097  1108 HOH   A O    
4348 O  O    . HOH   F .   ? 0.9139 1.1371 1.2003 -0.0775 -0.0879 -0.0116 1109 HOH   A O    
4349 O  O    . HOH   F .   ? 0.5671 0.5944 0.5806 0.0227  -0.0976 -0.0049 1110 HOH   A O    
4350 O  O    . HOH   F .   ? 0.8576 0.8994 0.7040 -0.0620 -0.0409 0.1115  1111 HOH   A O    
4351 O  O    . HOH   F .   ? 0.5816 0.7505 0.4304 0.0156  -0.0046 0.0114  1112 HOH   A O    
4352 O  O    . HOH   F .   ? 0.6314 0.6756 0.6832 0.0048  -0.1158 -0.0359 1113 HOH   A O    
4353 O  O    . HOH   F .   ? 0.7215 1.0196 0.5292 0.0162  0.0282  0.0217  1114 HOH   A O    
4354 O  O    . HOH   F .   ? 0.6755 0.6906 0.6413 0.0187  -0.0904 -0.0445 1115 HOH   A O    
4355 O  O    . HOH   F .   ? 0.6289 0.6244 0.5193 0.1472  -0.0340 -0.1324 1116 HOH   A O    
4356 O  O    . HOH   F .   ? 0.3641 0.4083 0.4841 0.0281  -0.0462 -0.0064 1117 HOH   A O    
4357 O  O    . HOH   F .   ? 0.4881 0.5205 0.6307 -0.0745 0.0139  0.0258  1118 HOH   A O    
4358 O  O    . HOH   F .   ? 0.6495 0.6875 0.5585 -0.0333 -0.0278 0.0670  1119 HOH   A O    
4359 O  O    . HOH   F .   ? 0.7366 0.7677 0.6382 0.0128  -0.0771 0.0215  1120 HOH   A O    
4360 O  O    . HOH   F .   ? 0.6671 0.8154 0.5025 0.0201  -0.0188 0.0056  1121 HOH   A O    
4361 O  O    . HOH   F .   ? 0.4884 0.4756 0.5439 0.0031  -0.0002 -0.0002 1122 HOH   A O    
4362 O  O    . HOH   F .   ? 0.5789 0.5948 0.5395 -0.0196 -0.0189 0.0417  1123 HOH   A O    
4363 O  O    . HOH   F .   ? 0.6053 0.6261 0.5674 0.0153  -0.0611 -0.0026 1124 HOH   A O    
4364 O  O    . HOH   F .   ? 0.4453 0.4224 0.4249 0.0188  -0.0743 -0.0643 1125 HOH   A O    
4365 O  O    . HOH   F .   ? 0.6646 0.9588 0.4982 -0.0025 0.0320  0.0388  1126 HOH   A O    
4366 O  O    . HOH   F .   ? 0.3507 0.3189 0.3717 0.0241  -0.0098 -0.0300 1127 HOH   A O    
4367 O  O    . HOH   F .   ? 0.5060 0.4041 0.5380 -0.0360 -0.1148 -0.0765 1128 HOH   A O    
4368 O  O    . HOH   F .   ? 0.4278 0.4097 0.4558 0.0187  -0.0494 0.0154  1129 HOH   A O    
4369 O  O    . HOH   F .   ? 0.4284 0.4214 0.4303 0.0281  -0.0163 -0.0360 1130 HOH   A O    
4370 O  O    . HOH   F .   ? 0.4405 0.4356 0.4984 -0.0044 0.0406  0.0055  1131 HOH   A O    
4371 O  O    . HOH   F .   ? 0.5799 0.6107 0.5144 0.0182  -0.0681 -0.0064 1132 HOH   A O    
4372 O  O    . HOH   F .   ? 0.6276 0.8073 0.8815 -0.0879 -0.0179 0.0132  1133 HOH   A O    
4373 O  O    . HOH   F .   ? 0.5316 0.5455 0.5193 0.0133  -0.0488 -0.0065 1134 HOH   A O    
4374 O  O    . HOH   F .   ? 0.7772 0.7806 0.6837 0.0071  -0.0825 0.0464  1135 HOH   A O    
4375 O  O    . HOH   F .   ? 0.4378 0.4115 0.4943 0.0068  0.0085  0.0016  1136 HOH   A O    
4376 O  O    . HOH   F .   ? 0.4725 0.6069 0.6796 -0.0253 -0.0693 -0.0174 1137 HOH   A O    
4377 O  O    . HOH   F .   ? 0.8137 0.7824 0.7425 0.0118  -0.1495 -0.1051 1138 HOH   A O    
4378 O  O    . HOH   F .   ? 0.6644 0.6293 0.7369 0.0553  -0.0433 0.0029  1139 HOH   A O    
4379 O  O    . HOH   F .   ? 0.5296 0.5493 0.5348 0.0006  -0.0022 0.0076  1140 HOH   A O    
4380 O  O    . HOH   F .   ? 0.7135 0.7240 0.6686 0.0148  -0.0740 0.0178  1141 HOH   A O    
4381 O  O    . HOH   F .   ? 0.5013 0.6625 0.4603 0.0355  0.0229  -0.0123 1142 HOH   A O    
4382 O  O    . HOH   F .   ? 0.5765 0.6010 0.6873 -0.0463 -0.1199 -0.0518 1143 HOH   A O    
4383 O  O    . HOH   F .   ? 0.4691 0.4119 0.4488 0.0507  -0.0333 -0.0659 1144 HOH   A O    
4384 O  O    . HOH   F .   ? 0.4173 0.4181 0.4200 0.0120  -0.0727 -0.0435 1145 HOH   A O    
4385 O  O    . HOH   F .   ? 0.4940 0.5642 0.6359 0.0705  -0.0827 -0.0035 1146 HOH   A O    
4386 O  O    . HOH   F .   ? 0.5723 0.6388 0.6468 0.0133  -0.1229 -0.0247 1147 HOH   A O    
4387 O  O    . HOH   F .   ? 0.6990 0.5575 0.6359 0.0823  -0.0644 -0.1042 1148 HOH   A O    
4388 O  O    . HOH   F .   ? 0.4919 0.7434 0.4400 0.0421  0.0393  -0.0092 1149 HOH   A O    
4389 O  O    . HOH   F .   ? 0.5248 0.4542 0.5661 -0.0363 -0.1188 -0.0747 1150 HOH   A O    
4390 O  O    . HOH   F .   ? 0.3521 0.3303 0.4126 -0.0024 0.0128  -0.0014 1151 HOH   A O    
4391 O  O    . HOH   F .   ? 0.6323 0.6468 0.6227 0.0146  -0.0860 -0.0381 1152 HOH   A O    
4392 O  O    . HOH   F .   ? 0.4817 0.6046 0.6697 0.0540  -0.0615 -0.0121 1153 HOH   A O    
4393 O  O    . HOH   F .   ? 0.4983 0.5638 0.6049 0.0442  -0.1034 -0.0023 1154 HOH   A O    
4394 O  O    . HOH   F .   ? 0.7816 0.7841 0.7874 -0.0112 -0.1511 -0.0792 1155 HOH   A O    
4395 O  O    . HOH   F .   ? 0.4569 0.4593 0.5035 -0.0093 -0.1004 -0.0530 1156 HOH   A O    
4396 O  O    . HOH   F .   ? 0.4159 0.3762 0.3940 0.0227  -0.0685 -0.0700 1157 HOH   A O    
4397 O  O    . HOH   F .   ? 0.4248 0.4051 0.4354 0.0362  -0.0062 -0.0337 1158 HOH   A O    
4398 O  O    . HOH   F .   ? 0.5864 0.4381 0.6511 -0.0694 -0.0705 -0.0215 1159 HOH   A O    
4399 O  O    . HOH   F .   ? 0.4203 0.4778 0.5613 0.0280  -0.0138 -0.0092 1160 HOH   A O    
4400 O  O    . HOH   F .   ? 0.6484 0.6831 0.5645 0.0132  -0.0641 0.0111  1161 HOH   A O    
4401 O  O    . HOH   F .   ? 0.4997 0.5592 0.6359 -0.0287 0.0313  0.0102  1162 HOH   A O    
4402 O  O    . HOH   F .   ? 0.7768 0.9314 0.7384 0.0059  0.0219  0.0131  1163 HOH   A O    
4403 O  O    . HOH   F .   ? 0.4374 0.4186 0.4959 -0.0039 0.0242  0.0037  1164 HOH   A O    
4404 O  O    . HOH   F .   ? 0.6440 0.5382 0.6037 0.0072  -0.1204 -0.1067 1165 HOH   A O    
4405 O  O    . HOH   F .   ? 0.5452 0.5570 0.5306 0.0168  -0.0662 -0.0320 1166 HOH   A O    
4406 O  O    . HOH   F .   ? 0.6011 0.5829 0.6054 0.0210  -0.0675 0.0236  1167 HOH   A O    
4407 O  O    . HOH   F .   ? 0.4618 0.4435 0.5100 0.0016  0.0336  0.0005  1168 HOH   A O    
4408 O  O    . HOH   F .   ? 0.5505 0.6800 0.5102 0.0228  0.0158  -0.0046 1169 HOH   A O    
4409 O  O    . HOH   F .   ? 0.4665 0.4604 0.4711 0.0080  -0.0856 -0.0537 1170 HOH   A O    
4410 O  O    . HOH   F .   ? 0.4238 0.4576 0.5371 0.0134  0.0207  -0.0060 1171 HOH   A O    
4411 O  O    . HOH   F .   ? 0.5478 0.5614 0.5481 0.0145  -0.0615 -0.0168 1172 HOH   A O    
4412 O  O    . HOH   F .   ? 0.6473 0.7806 0.5322 0.1818  0.0000  -0.1333 1173 HOH   A O    
4413 O  O    . HOH   F .   ? 0.6317 0.5921 0.6733 0.0365  -0.0573 0.0178  1174 HOH   A O    
4414 O  O    . HOH   F .   ? 0.5896 0.5179 0.5583 0.0673  -0.0353 -0.0751 1175 HOH   A O    
4415 O  O    . HOH   F .   ? 0.6249 0.6922 0.5592 -0.0269 -0.0091 0.0492  1176 HOH   A O    
4416 O  O    . HOH   F .   ? 0.6335 0.6289 0.5897 0.0184  -0.1031 -0.0693 1177 HOH   A O    
4417 O  O    . HOH   F .   ? 0.5684 0.5698 0.5835 -0.0001 -0.0077 0.0091  1178 HOH   A O    
4418 O  O    . HOH   F .   ? 0.6208 0.6219 0.6549 0.0338  -0.0838 0.0147  1179 HOH   A O    
4419 O  O    . HOH   F .   ? 0.5327 0.4895 0.5354 0.0418  -0.0164 -0.0447 1180 HOH   A O    
4420 O  O    . HOH   F .   ? 0.4354 0.4407 0.4728 -0.0003 -0.0872 -0.0453 1181 HOH   A O    
4421 O  O    . HOH   F .   ? 0.4191 0.4250 0.4970 0.0101  0.0332  -0.0043 1182 HOH   A O    
4422 O  O    . HOH   F .   ? 0.4557 0.4516 0.4409 0.0185  -0.0632 -0.0481 1183 HOH   A O    
4423 O  O    . HOH   F .   ? 0.5920 0.7497 0.4915 0.1471  0.0094  -0.1061 1184 HOH   A O    
4424 O  O    . HOH   F .   ? 0.4626 0.4041 0.5148 -0.0036 -0.0040 -0.0106 1185 HOH   A O    
4425 O  O    . HOH   F .   ? 0.4804 0.3336 0.4413 0.0423  -0.0737 -0.0915 1186 HOH   A O    
4426 O  O    . HOH   F .   ? 0.4645 0.4420 0.5155 0.0014  0.0093  0.0035  1187 HOH   A O    
4427 O  O    . HOH   F .   ? 0.5399 0.6302 0.6637 0.0500  -0.1193 -0.0040 1188 HOH   A O    
4428 O  O    . HOH   F .   ? 0.5340 0.6363 0.7089 0.0734  -0.0630 -0.0113 1189 HOH   A O    
4429 O  O    . HOH   F .   ? 0.6748 1.1072 0.5294 0.1411  0.0667  -0.0768 1190 HOH   A O    
4430 O  O    . HOH   F .   ? 0.7500 0.9352 0.5371 0.1562  -0.0061 -0.1366 1191 HOH   A O    
4431 O  O    . HOH   F .   ? 0.3277 0.3121 0.3152 0.0417  -0.0205 -0.0502 1192 HOH   A O    
4432 O  O    . HOH   F .   ? 0.4916 0.5998 0.6609 0.0663  -0.0874 -0.0077 1193 HOH   A O    
4433 O  O    . HOH   F .   ? 0.8111 0.7433 0.7179 0.0118  -0.1659 -0.1295 1194 HOH   A O    
4434 O  O    . HOH   F .   ? 0.5932 0.4710 0.6363 -0.0572 -0.1270 -0.0750 1195 HOH   A O    
4435 O  O    . HOH   F .   ? 0.7027 0.5465 0.6331 0.0679  -0.0800 -0.1125 1196 HOH   A O    
4436 O  O    . HOH   F .   ? 0.6109 0.5012 0.6555 -0.0149 -0.0277 -0.0179 1197 HOH   A O    
4437 O  O    . HOH   F .   ? 0.6237 0.6169 0.6145 -0.0062 -0.0214 0.0262  1198 HOH   A O    
4438 O  O    . HOH   F .   ? 0.5311 0.4261 0.5132 0.0328  -0.0580 -0.0748 1199 HOH   A O    
4439 O  O    . HOH   F .   ? 0.7888 0.9269 0.7887 0.0227  0.0251  -0.0012 1200 HOH   A O    
4440 O  O    . HOH   F .   ? 0.7313 0.7202 0.6383 -0.0314 -0.0474 0.0765  1201 HOH   A O    
4441 O  O    . HOH   F .   ? 0.6331 0.7697 0.8829 -0.1383 -0.0470 0.0190  1202 HOH   A O    
4442 O  O    . HOH   F .   ? 0.7059 0.7491 0.6632 -0.0201 -0.0099 0.0390  1203 HOH   A O    
4443 O  O    . HOH   F .   ? 0.6941 0.8888 0.9565 -0.1049 -0.0094 0.0230  1204 HOH   A O    
4444 O  O    . HOH   F .   ? 0.6727 0.6479 0.7157 0.0341  -0.0613 0.0166  1205 HOH   A O    
4445 O  O    . HOH   F .   ? 0.5775 0.6636 0.6655 0.0097  -0.1416 -0.0298 1206 HOH   A O    
4446 O  O    . HOH   F .   ? 0.7961 0.7628 0.6592 0.1681  -0.0478 -0.1571 1207 HOH   A O    
4447 O  O    . HOH   F .   ? 0.6284 0.6507 0.6051 0.0186  -0.0842 -0.0113 1208 HOH   A O    
4448 O  O    . HOH   F .   ? 0.8968 0.8908 0.8484 0.0093  -0.1414 -0.0853 1209 HOH   A O    
4449 O  O    . HOH   F .   ? 0.9269 1.1208 0.6839 0.1716  -0.0095 -0.1533 1210 HOH   A O    
4450 O  O    . HOH   F .   ? 0.5867 0.5844 0.5788 0.0091  -0.0991 -0.0592 1211 HOH   A O    
4451 O  O    . HOH   F .   ? 0.6806 0.7062 0.6277 0.0189  -0.0806 -0.0050 1212 HOH   A O    
4452 O  O    . HOH   F .   ? 0.7840 0.7602 0.6853 -0.0449 -0.0472 0.0892  1213 HOH   A O    
4453 O  O    . HOH   F .   ? 0.6503 0.4789 0.7166 -0.0907 -0.0870 -0.0204 1214 HOH   A O    
4454 O  O    . HOH   F .   ? 0.9492 0.9059 0.8532 -0.0552 -0.0474 0.0958  1215 HOH   A O    
4455 O  O    . HOH   F .   ? 0.9903 0.9500 0.8659 -0.0722 -0.0527 0.1174  1216 HOH   A O    
4456 O  O    . HOH   G .   ? 0.6115 0.6076 0.5087 -0.0028 -0.0094 0.0404  1101 HOH   B O    
4457 O  O    . HOH   G .   ? 0.5489 0.7431 0.6063 0.0580  -0.0039 0.0139  1102 HOH   B O    
4458 O  O    . HOH   G .   ? 0.7402 0.8430 0.7514 0.2252  -0.0804 0.0058  1103 HOH   B O    
4459 O  O    . HOH   G .   ? 0.4362 0.4590 0.4558 0.0083  0.0090  -0.0016 1104 HOH   B O    
4460 O  O    . HOH   G .   ? 0.6845 0.6572 0.6174 0.0118  -0.0027 0.0508  1105 HOH   B O    
4461 O  O    . HOH   G .   ? 0.8108 0.9640 0.8380 0.2108  -0.0755 0.0098  1106 HOH   B O    
4462 O  O    . HOH   G .   ? 0.6515 0.6621 0.6130 -0.0527 -0.0194 0.0132  1107 HOH   B O    
4463 O  O    . HOH   G .   ? 0.7289 0.5007 0.6100 0.0139  -0.0317 -0.0563 1108 HOH   B O    
4464 O  O    . HOH   G .   ? 0.6601 0.5737 0.6005 0.0401  -0.0202 0.0602  1109 HOH   B O    
4465 O  O    . HOH   G .   ? 0.5399 0.4351 0.5081 0.0945  -0.0375 0.0230  1110 HOH   B O    
4466 O  O    . HOH   G .   ? 0.4417 0.4495 0.5177 0.0016  0.0378  0.0004  1111 HOH   B O    
4467 O  O    . HOH   G .   ? 0.6886 0.5317 0.6347 0.0382  -0.0265 0.0560  1112 HOH   B O    
4468 O  O    . HOH   G .   ? 0.5373 0.5247 0.5389 -0.0378 0.0587  0.0513  1113 HOH   B O    
4469 O  O    . HOH   G .   ? 0.6344 0.6252 0.6853 0.0064  0.0396  -0.0028 1114 HOH   B O    
4470 O  O    . HOH   G .   ? 0.5607 0.3986 0.5578 -0.0214 -0.0097 0.0428  1115 HOH   B O    
4471 O  O    . HOH   G .   ? 0.7807 0.5284 0.7373 0.0623  -0.0656 -0.0365 1116 HOH   B O    
4472 O  O    . HOH   G .   ? 0.5384 0.5015 0.5180 0.0013  0.0390  -0.0065 1117 HOH   B O    
4473 O  O    . HOH   G .   ? 0.5510 0.7589 0.6096 0.0873  0.0052  -0.0029 1118 HOH   B O    
4474 O  O    . HOH   G .   ? 0.6966 0.8067 0.6940 -0.0890 0.0077  0.0698  1119 HOH   B O    
4475 O  O    . HOH   G .   ? 0.4684 0.3826 0.4299 -0.0218 0.0033  -0.0078 1120 HOH   B O    
4476 O  O    . HOH   G .   ? 0.4616 0.4453 0.4922 -0.0058 0.0226  0.0086  1121 HOH   B O    
4477 O  O    . HOH   G .   ? 0.6698 0.4228 0.5499 -0.0362 -0.0545 -0.0297 1122 HOH   B O    
4478 O  O    . HOH   G .   ? 0.4197 0.4002 0.4490 -0.0074 0.0409  0.0114  1123 HOH   B O    
4479 O  O    . HOH   G .   ? 0.7283 0.6551 0.6037 -0.0036 0.0040  0.0862  1124 HOH   B O    
4480 O  O    . HOH   G .   ? 0.4293 0.3849 0.4285 0.0389  0.0383  -0.0330 1125 HOH   B O    
4481 O  O    . HOH   G .   ? 0.5612 0.5449 0.5361 0.0031  0.0126  0.0307  1126 HOH   B O    
4482 O  O    . HOH   G .   ? 0.4962 0.4338 0.4515 -0.0021 0.0251  -0.0151 1127 HOH   B O    
4483 O  O    . HOH   G .   ? 0.5645 0.6879 0.5824 -0.0856 0.0067  0.0589  1128 HOH   B O    
4484 O  O    . HOH   G .   ? 0.5626 0.6144 0.5518 -0.0455 -0.0147 0.0216  1129 HOH   B O    
4485 O  O    . HOH   G .   ? 0.4886 0.4269 0.4416 0.0281  -0.0078 0.0522  1130 HOH   B O    
4486 O  O    . HOH   G .   ? 0.5551 0.5082 0.6213 -0.0401 0.0217  0.0266  1131 HOH   B O    
4487 O  O    . HOH   G .   ? 0.6648 0.6100 0.6370 -0.0742 -0.0192 0.0572  1132 HOH   B O    
4488 O  O    . HOH   G .   ? 0.5295 0.5029 0.5343 -0.0374 0.0016  0.0283  1133 HOH   B O    
4489 O  O    . HOH   G .   ? 0.5740 0.6555 0.5758 0.0941  -0.0410 0.0329  1134 HOH   B O    
4490 O  O    . HOH   G .   ? 0.4317 0.4201 0.4480 -0.0063 0.0498  0.0106  1135 HOH   B O    
4491 O  O    . HOH   G .   ? 0.6524 0.8543 0.7089 0.1159  -0.0050 -0.0077 1136 HOH   B O    
4492 O  O    . HOH   G .   ? 0.4230 0.4190 0.4297 -0.0014 0.0563  0.0053  1137 HOH   B O    
4493 O  O    . HOH   G .   ? 0.5246 0.4456 0.5473 -0.0488 0.0263  0.0547  1138 HOH   B O    
4494 O  O    . HOH   G .   ? 0.4986 0.6034 0.5307 -0.0011 0.0211  0.0152  1139 HOH   B O    
4495 O  O    . HOH   G .   ? 0.4540 0.4141 0.5192 -0.0204 0.0188  0.0115  1140 HOH   B O    
4496 O  O    . HOH   G .   ? 0.3846 0.3588 0.3825 -0.0073 0.0319  0.0165  1141 HOH   B O    
4497 O  O    . HOH   G .   ? 0.5853 0.4759 0.5594 0.1282  -0.0418 -0.0161 1142 HOH   B O    
4498 O  O    . HOH   G .   ? 0.4184 0.3975 0.4186 -0.0080 0.0257  0.0142  1143 HOH   B O    
4499 O  O    . HOH   G .   ? 0.5153 0.4891 0.4732 -0.0536 -0.0146 0.0077  1144 HOH   B O    
4500 O  O    . HOH   G .   ? 0.5444 0.4689 0.5049 -0.1119 -0.0362 0.0491  1145 HOH   B O    
4501 O  O    . HOH   G .   ? 0.6564 0.6945 0.7256 -0.0151 0.0613  0.0151  1146 HOH   B O    
4502 O  O    . HOH   G .   ? 0.5230 0.5912 0.5015 -0.0305 0.0964  0.0438  1147 HOH   B O    
4503 O  O    . HOH   G .   ? 0.6866 0.4675 0.5812 0.0388  -0.0234 -0.0626 1148 HOH   B O    
4504 O  O    . HOH   G .   ? 0.6780 0.4019 0.5778 0.0370  -0.0506 -0.0455 1149 HOH   B O    
4505 O  O    . HOH   G .   ? 0.4162 0.3939 0.4288 -0.0062 0.0413  0.0101  1150 HOH   B O    
4506 O  O    . HOH   G .   ? 0.5326 0.5264 0.5158 0.0161  0.0037  0.0319  1151 HOH   B O    
4507 O  O    . HOH   G .   ? 0.4935 0.3548 0.4691 0.0349  -0.0049 -0.0294 1152 HOH   B O    
4508 O  O    . HOH   G .   ? 0.5985 0.5144 0.6091 -0.0591 0.0287  0.0685  1153 HOH   B O    
4509 O  O    . HOH   G .   ? 0.5435 0.5233 0.4973 -0.0128 0.0486  0.0297  1154 HOH   B O    
4510 O  O    . HOH   G .   ? 0.5391 0.5810 0.5582 -0.0129 0.0112  0.0188  1155 HOH   B O    
4511 O  O    . HOH   G .   ? 0.5491 0.5321 0.6120 0.0339  0.0248  -0.0161 1156 HOH   B O    
4512 O  O    . HOH   G .   ? 0.6747 0.5970 0.6162 -0.0795 -0.0333 0.0073  1157 HOH   B O    
4513 O  O    . HOH   G .   ? 0.3507 0.3534 0.3737 -0.0038 0.0198  0.0128  1158 HOH   B O    
4514 O  O    . HOH   G .   ? 0.4514 0.4245 0.4357 -0.0079 0.0331  0.0209  1159 HOH   B O    
4515 O  O    . HOH   G .   ? 0.4967 0.4493 0.4524 -0.0037 0.0307  -0.0087 1160 HOH   B O    
4516 O  O    . HOH   G .   ? 0.4418 0.4781 0.4697 -0.0002 0.0179  0.0089  1161 HOH   B O    
4517 O  O    . HOH   G .   ? 0.3658 0.3316 0.3687 -0.0106 0.0248  0.0049  1162 HOH   B O    
4518 O  O    . HOH   G .   ? 0.5958 0.5245 0.5372 0.0134  0.0003  0.0595  1163 HOH   B O    
4519 O  O    . HOH   G .   ? 0.7170 0.4480 0.5903 -0.0772 -0.0762 -0.0084 1164 HOH   B O    
4520 O  O    . HOH   G .   ? 0.4071 0.3841 0.4464 -0.0028 0.0324  0.0042  1165 HOH   B O    
4521 O  O    . HOH   G .   ? 0.5009 0.5694 0.5254 0.1005  -0.0047 -0.0124 1166 HOH   B O    
4522 O  O    . HOH   G .   ? 0.4818 0.4286 0.4524 -0.0135 0.0311  0.0479  1167 HOH   B O    
4523 O  O    . HOH   G .   ? 0.4847 0.5015 0.4590 0.0034  0.0719  0.0025  1168 HOH   B O    
4524 O  O    . HOH   G .   ? 0.6504 0.3998 0.5581 -0.0329 -0.0562 -0.0043 1169 HOH   B O    
4525 O  O    . HOH   G .   ? 0.4443 0.4193 0.4727 -0.0071 0.0238  0.0071  1170 HOH   B O    
4526 O  O    . HOH   G .   ? 0.6276 0.4070 0.5995 0.0483  -0.0559 -0.0360 1171 HOH   B O    
4527 O  O    . HOH   G .   ? 0.4764 0.4037 0.4717 0.0499  -0.0243 -0.0520 1172 HOH   B O    
4528 O  O    . HOH   G .   ? 0.5250 0.6967 0.5744 0.0317  0.0179  0.0089  1173 HOH   B O    
4529 O  O    . HOH   G .   ? 0.5515 0.5249 0.5099 -0.0043 0.0430  0.0042  1174 HOH   B O    
4530 O  O    . HOH   G .   ? 0.7442 0.6035 0.7795 -0.0486 -0.0114 0.0314  1175 HOH   B O    
4531 O  O    . HOH   G .   ? 0.4966 0.5184 0.5011 -0.0200 0.0086  0.0181  1176 HOH   B O    
4532 O  O    . HOH   G .   ? 0.4297 0.4986 0.4610 0.0040  0.0194  0.0107  1177 HOH   B O    
4533 O  O    . HOH   G .   ? 0.4026 0.3945 0.4056 -0.0131 0.0180  0.0139  1178 HOH   B O    
4534 O  O    . HOH   G .   ? 0.5422 0.5124 0.5178 0.1148  -0.0453 0.0296  1179 HOH   B O    
4535 O  O    . HOH   G .   ? 0.3370 0.3185 0.3981 -0.0029 0.0182  0.0014  1180 HOH   B O    
4536 O  O    . HOH   G .   ? 0.5051 0.5425 0.5051 0.0241  -0.0037 0.0275  1181 HOH   B O    
4537 O  O    . HOH   G .   ? 0.4608 0.4544 0.4769 0.0150  0.0145  0.0161  1182 HOH   B O    
4538 O  O    . HOH   G .   ? 0.5749 0.5357 0.5293 -0.0690 -0.0240 0.0091  1183 HOH   B O    
4539 O  O    . HOH   G .   ? 0.5479 0.5966 0.5543 0.0049  0.0014  0.0237  1184 HOH   B O    
4540 O  O    . HOH   G .   ? 0.5356 0.5103 0.5038 -0.0082 0.0394  0.0149  1185 HOH   B O    
4541 O  O    . HOH   G .   ? 0.5013 0.4919 0.5621 0.0140  0.0333  -0.0069 1186 HOH   B O    
4542 O  O    . HOH   G .   ? 0.5594 0.4954 0.5127 0.0041  0.0111  0.0532  1187 HOH   B O    
4543 O  O    . HOH   G .   ? 0.6283 0.4487 0.5796 0.1156  -0.0562 0.0063  1188 HOH   B O    
4544 O  O    . HOH   G .   ? 0.4885 0.4741 0.4511 -0.0187 0.0561  0.0373  1189 HOH   B O    
4545 O  O    . HOH   G .   ? 0.4796 0.4929 0.5302 -0.0253 0.0576  0.0261  1190 HOH   B O    
4546 O  O    . HOH   G .   ? 0.5944 0.5590 0.5396 -0.0068 0.0329  0.0004  1191 HOH   B O    
4547 O  O    . HOH   G .   ? 0.6426 0.6448 0.4819 -0.0033 -0.0283 0.0475  1192 HOH   B O    
4548 O  O    . HOH   G .   ? 0.4252 0.4131 0.4698 0.0012  0.0043  0.0014  1193 HOH   B O    
4549 O  O    . HOH   G .   ? 0.4018 0.3797 0.4500 -0.0024 0.0238  0.0038  1194 HOH   B O    
4550 O  O    . HOH   G .   ? 0.5054 0.5340 0.5071 -0.0048 0.0742  0.0120  1195 HOH   B O    
4551 O  O    . HOH   G .   ? 0.7638 0.9033 0.7702 -0.0712 0.0159  0.0601  1196 HOH   B O    
4552 O  O    . HOH   G .   ? 0.3796 0.3518 0.3826 -0.0036 0.0390  0.0035  1197 HOH   B O    
4553 O  O    . HOH   G .   ? 0.6550 0.6816 0.6604 0.1564  -0.0283 -0.0258 1198 HOH   B O    
4554 O  O    . HOH   G .   ? 0.5335 0.5080 0.5033 -0.0110 0.0248  0.0124  1199 HOH   B O    
4555 O  O    . HOH   G .   ? 0.5014 0.4952 0.4285 0.0122  -0.0116 0.0483  1200 HOH   B O    
4556 O  O    . HOH   G .   ? 0.4200 0.4977 0.4457 0.0016  0.0059  0.0206  1201 HOH   B O    
4557 O  O    . HOH   G .   ? 0.4172 0.4282 0.4134 0.0178  0.0036  0.0268  1202 HOH   B O    
4558 O  O    . HOH   G .   ? 0.8033 0.6145 0.7336 0.0353  -0.0345 0.0670  1203 HOH   B O    
4559 O  O    . HOH   G .   ? 0.4326 0.4663 0.4260 -0.0403 -0.0054 0.0199  1204 HOH   B O    
4560 O  O    . HOH   G .   ? 0.4200 0.3979 0.4217 -0.0123 0.0225  0.0103  1205 HOH   B O    
4561 O  O    . HOH   G .   ? 0.6085 0.5840 0.5663 -0.1058 -0.0426 0.0217  1206 HOH   B O    
4562 O  O    . HOH   G .   ? 0.5753 0.6193 0.5929 -0.0320 0.0131  0.0281  1207 HOH   B O    
4563 O  O    . HOH   G .   ? 0.6485 0.5816 0.5815 -0.0173 0.0100  -0.0128 1208 HOH   B O    
4564 O  O    . HOH   G .   ? 0.2856 0.2564 0.2850 0.0033  0.0421  -0.0049 1209 HOH   B O    
4565 O  O    . HOH   G .   ? 0.5439 0.5168 0.4981 -0.0214 0.0496  0.0476  1210 HOH   B O    
4566 O  O    . HOH   G .   ? 0.5492 0.5533 0.6083 0.0016  0.0451  0.0012  1211 HOH   B O    
4567 O  O    . HOH   G .   ? 0.6092 0.5678 0.5601 0.0041  0.0398  -0.0134 1212 HOH   B O    
4568 O  O    . HOH   G .   ? 0.7031 0.8085 0.7102 0.0335  0.0207  -0.0107 1213 HOH   B O    
4569 O  O    . HOH   G .   ? 0.7310 0.6214 0.6596 -0.0691 -0.0331 -0.0019 1214 HOH   B O    
4570 O  O    . HOH   G .   ? 0.5407 0.4895 0.4900 -0.0269 0.0049  -0.0028 1215 HOH   B O    
4571 O  O    . HOH   G .   ? 0.5920 0.6483 0.6082 -0.0031 0.0056  0.0211  1216 HOH   B O    
4572 O  O    . HOH   G .   ? 0.5046 0.4785 0.4746 -0.0088 0.0318  0.0168  1217 HOH   B O    
4573 O  O    . HOH   G .   ? 0.6891 0.8675 0.7202 0.1961  -0.0792 0.0198  1218 HOH   B O    
4574 O  O    . HOH   G .   ? 0.8340 0.7504 0.7637 0.0031  0.0051  0.0687  1219 HOH   B O    
4575 O  O    . HOH   G .   ? 0.6329 0.5819 0.5769 -0.0091 0.0234  -0.0082 1220 HOH   B O    
4576 O  O    . HOH   G .   ? 0.8106 1.0178 0.8591 0.1959  -0.0625 0.0058  1221 HOH   B O    
4577 O  O    . HOH   G .   ? 0.6609 0.7767 0.6690 -0.0541 0.0163  0.0485  1222 HOH   B O    
4578 O  O    . HOH   G .   ? 0.8395 0.8047 0.7649 -0.0235 0.0458  0.0606  1223 HOH   B O    
4579 O  O    . HOH   G .   ? 0.6463 0.6405 0.5637 0.0026  -0.0069 0.0431  1224 HOH   B O    
4580 O  O    . HOH   G .   ? 0.7222 0.7567 0.7005 -0.0349 -0.0108 0.0191  1225 HOH   B O    
4581 O  O    . HOH   G .   ? 0.7504 0.7304 0.6821 -0.0222 0.0539  0.0504  1226 HOH   B O    
4582 O  O    . HOH   G .   ? 0.5496 0.5653 0.4988 0.0157  -0.0153 0.0421  1227 HOH   B O    
4583 O  O    . HOH   G .   ? 0.7697 1.0061 0.8206 0.2080  -0.0819 0.0163  1228 HOH   B O    
# 
