data_9MUL
# 
_entry.id   9MUL 
# 
_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   9MUL         pdb_00009mul 10.2210/pdb9mul/pdb 
WWPDB D_1000291694 ?            ?                   
# 
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                        9MUL 
_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-[(3-chlorobenzene-1-sulfonyl)methoxy]-6-methyl-N-[(pyridin-3-yl)methyl]pyrazine-2-carboxamide' 432.881   1   
? ? ? ? 
6 water       nat water                                                                                             18.015    252 
? ? ? ? 
# 
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-[(3-chlorobenzene-1-sulfonyl)methoxy]-6-methyl-N-[(pyridin-3-yl)methyl]pyrazine-2-carboxamide' A1BRA 
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 
A1BRA non-polymer         . '5-[(3-chlorobenzene-1-sulfonyl)methoxy]-6-methyl-N-[(pyridin-3-yl)methyl]pyrazine-2-carboxamide' ? 
'C19 H17 Cl N4 O4 S' 432.881 
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 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BRA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BRA 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 GLY   1   1001 1001 GLY   GLY A . 
D 4 GLU   1   1001 1001 GLU   GLU B . 
E 5 A1BRA 1   1002 1    A1BRA UNL B . 
F 6 HOH   1   1101 150  HOH   HOH A . 
F 6 HOH   2   1102 205  HOH   HOH A . 
F 6 HOH   3   1103 251  HOH   HOH A . 
F 6 HOH   4   1104 197  HOH   HOH A . 
F 6 HOH   5   1105 139  HOH   HOH A . 
F 6 HOH   6   1106 184  HOH   HOH A . 
F 6 HOH   7   1107 8    HOH   HOH A . 
F 6 HOH   8   1108 109  HOH   HOH A . 
F 6 HOH   9   1109 215  HOH   HOH A . 
F 6 HOH   10  1110 74   HOH   HOH A . 
F 6 HOH   11  1111 130  HOH   HOH A . 
F 6 HOH   12  1112 233  HOH   HOH A . 
F 6 HOH   13  1113 172  HOH   HOH A . 
F 6 HOH   14  1114 32   HOH   HOH A . 
F 6 HOH   15  1115 176  HOH   HOH A . 
F 6 HOH   16  1116 111  HOH   HOH A . 
F 6 HOH   17  1117 22   HOH   HOH A . 
F 6 HOH   18  1118 140  HOH   HOH A . 
F 6 HOH   19  1119 247  HOH   HOH A . 
F 6 HOH   20  1120 70   HOH   HOH A . 
F 6 HOH   21  1121 123  HOH   HOH A . 
F 6 HOH   22  1122 107  HOH   HOH A . 
F 6 HOH   23  1123 220  HOH   HOH A . 
F 6 HOH   24  1124 53   HOH   HOH A . 
F 6 HOH   25  1125 61   HOH   HOH A . 
F 6 HOH   26  1126 180  HOH   HOH A . 
F 6 HOH   27  1127 3    HOH   HOH A . 
F 6 HOH   28  1128 67   HOH   HOH A . 
F 6 HOH   29  1129 65   HOH   HOH A . 
F 6 HOH   30  1130 175  HOH   HOH A . 
F 6 HOH   31  1131 25   HOH   HOH A . 
F 6 HOH   32  1132 5    HOH   HOH A . 
F 6 HOH   33  1133 124  HOH   HOH A . 
F 6 HOH   34  1134 116  HOH   HOH A . 
F 6 HOH   35  1135 158  HOH   HOH A . 
F 6 HOH   36  1136 60   HOH   HOH A . 
F 6 HOH   37  1137 250  HOH   HOH A . 
F 6 HOH   38  1138 39   HOH   HOH A . 
F 6 HOH   39  1139 143  HOH   HOH A . 
F 6 HOH   40  1140 125  HOH   HOH A . 
F 6 HOH   41  1141 83   HOH   HOH A . 
F 6 HOH   42  1142 72   HOH   HOH A . 
F 6 HOH   43  1143 20   HOH   HOH A . 
F 6 HOH   44  1144 87   HOH   HOH A . 
F 6 HOH   45  1145 191  HOH   HOH A . 
F 6 HOH   46  1146 122  HOH   HOH A . 
F 6 HOH   47  1147 24   HOH   HOH A . 
F 6 HOH   48  1148 64   HOH   HOH A . 
F 6 HOH   49  1149 40   HOH   HOH A . 
F 6 HOH   50  1150 16   HOH   HOH A . 
F 6 HOH   51  1151 225  HOH   HOH A . 
F 6 HOH   52  1152 93   HOH   HOH A . 
F 6 HOH   53  1153 114  HOH   HOH A . 
F 6 HOH   54  1154 152  HOH   HOH A . 
F 6 HOH   55  1155 196  HOH   HOH A . 
F 6 HOH   56  1156 29   HOH   HOH A . 
F 6 HOH   57  1157 58   HOH   HOH A . 
F 6 HOH   58  1158 132  HOH   HOH A . 
F 6 HOH   59  1159 216  HOH   HOH A . 
F 6 HOH   60  1160 156  HOH   HOH A . 
F 6 HOH   61  1161 185  HOH   HOH A . 
F 6 HOH   62  1162 183  HOH   HOH A . 
F 6 HOH   63  1163 104  HOH   HOH A . 
F 6 HOH   64  1164 82   HOH   HOH A . 
F 6 HOH   65  1165 2    HOH   HOH A . 
F 6 HOH   66  1166 127  HOH   HOH A . 
F 6 HOH   67  1167 51   HOH   HOH A . 
F 6 HOH   68  1168 166  HOH   HOH A . 
F 6 HOH   69  1169 110  HOH   HOH A . 
F 6 HOH   70  1170 37   HOH   HOH A . 
F 6 HOH   71  1171 190  HOH   HOH A . 
F 6 HOH   72  1172 221  HOH   HOH A . 
F 6 HOH   73  1173 219  HOH   HOH A . 
F 6 HOH   74  1174 182  HOH   HOH A . 
F 6 HOH   75  1175 206  HOH   HOH A . 
F 6 HOH   76  1176 129  HOH   HOH A . 
F 6 HOH   77  1177 48   HOH   HOH A . 
F 6 HOH   78  1178 228  HOH   HOH A . 
F 6 HOH   79  1179 146  HOH   HOH A . 
F 6 HOH   80  1180 173  HOH   HOH A . 
F 6 HOH   81  1181 31   HOH   HOH A . 
F 6 HOH   82  1182 213  HOH   HOH A . 
F 6 HOH   83  1183 163  HOH   HOH A . 
F 6 HOH   84  1184 128  HOH   HOH A . 
F 6 HOH   85  1185 192  HOH   HOH A . 
F 6 HOH   86  1186 91   HOH   HOH A . 
F 6 HOH   87  1187 119  HOH   HOH A . 
F 6 HOH   88  1188 120  HOH   HOH A . 
F 6 HOH   89  1189 142  HOH   HOH A . 
F 6 HOH   90  1190 234  HOH   HOH A . 
F 6 HOH   91  1191 141  HOH   HOH A . 
F 6 HOH   92  1192 66   HOH   HOH A . 
F 6 HOH   93  1193 79   HOH   HOH A . 
F 6 HOH   94  1194 84   HOH   HOH A . 
F 6 HOH   95  1195 208  HOH   HOH A . 
F 6 HOH   96  1196 153  HOH   HOH A . 
F 6 HOH   97  1197 231  HOH   HOH A . 
F 6 HOH   98  1198 118  HOH   HOH A . 
F 6 HOH   99  1199 178  HOH   HOH A . 
F 6 HOH   100 1200 149  HOH   HOH A . 
F 6 HOH   101 1201 209  HOH   HOH A . 
F 6 HOH   102 1202 239  HOH   HOH A . 
F 6 HOH   103 1203 212  HOH   HOH A . 
F 6 HOH   104 1204 232  HOH   HOH A . 
F 6 HOH   105 1205 147  HOH   HOH A . 
F 6 HOH   106 1206 177  HOH   HOH A . 
F 6 HOH   107 1207 198  HOH   HOH A . 
F 6 HOH   108 1208 236  HOH   HOH A . 
F 6 HOH   109 1209 218  HOH   HOH A . 
F 6 HOH   110 1210 131  HOH   HOH A . 
F 6 HOH   111 1211 144  HOH   HOH A . 
F 6 HOH   112 1212 106  HOH   HOH A . 
F 6 HOH   113 1213 171  HOH   HOH A . 
F 6 HOH   114 1214 170  HOH   HOH A . 
F 6 HOH   115 1215 160  HOH   HOH A . 
F 6 HOH   116 1216 165  HOH   HOH A . 
F 6 HOH   117 1217 186  HOH   HOH A . 
F 6 HOH   118 1218 235  HOH   HOH A . 
F 6 HOH   119 1219 90   HOH   HOH A . 
F 6 HOH   120 1220 98   HOH   HOH A . 
G 6 HOH   1   1101 73   HOH   HOH B . 
G 6 HOH   2   1102 76   HOH   HOH B . 
G 6 HOH   3   1103 23   HOH   HOH B . 
G 6 HOH   4   1104 112  HOH   HOH B . 
G 6 HOH   5   1105 55   HOH   HOH B . 
G 6 HOH   6   1106 41   HOH   HOH B . 
G 6 HOH   7   1107 1    HOH   HOH B . 
G 6 HOH   8   1108 75   HOH   HOH B . 
G 6 HOH   9   1109 202  HOH   HOH B . 
G 6 HOH   10  1110 71   HOH   HOH B . 
G 6 HOH   11  1111 137  HOH   HOH B . 
G 6 HOH   12  1112 126  HOH   HOH B . 
G 6 HOH   13  1113 42   HOH   HOH B . 
G 6 HOH   14  1114 155  HOH   HOH B . 
G 6 HOH   15  1115 49   HOH   HOH B . 
G 6 HOH   16  1116 17   HOH   HOH B . 
G 6 HOH   17  1117 77   HOH   HOH B . 
G 6 HOH   18  1118 241  HOH   HOH B . 
G 6 HOH   19  1119 38   HOH   HOH B . 
G 6 HOH   20  1120 99   HOH   HOH B . 
G 6 HOH   21  1121 169  HOH   HOH B . 
G 6 HOH   22  1122 181  HOH   HOH B . 
G 6 HOH   23  1123 56   HOH   HOH B . 
G 6 HOH   24  1124 252  HOH   HOH B . 
G 6 HOH   25  1125 28   HOH   HOH B . 
G 6 HOH   26  1126 19   HOH   HOH B . 
G 6 HOH   27  1127 69   HOH   HOH B . 
G 6 HOH   28  1128 238  HOH   HOH B . 
G 6 HOH   29  1129 100  HOH   HOH B . 
G 6 HOH   30  1130 145  HOH   HOH B . 
G 6 HOH   31  1131 102  HOH   HOH B . 
G 6 HOH   32  1132 13   HOH   HOH B . 
G 6 HOH   33  1133 101  HOH   HOH B . 
G 6 HOH   34  1134 6    HOH   HOH B . 
G 6 HOH   35  1135 15   HOH   HOH B . 
G 6 HOH   36  1136 248  HOH   HOH B . 
G 6 HOH   37  1137 203  HOH   HOH B . 
G 6 HOH   38  1138 11   HOH   HOH B . 
G 6 HOH   39  1139 68   HOH   HOH B . 
G 6 HOH   40  1140 243  HOH   HOH B . 
G 6 HOH   41  1141 59   HOH   HOH B . 
G 6 HOH   42  1142 227  HOH   HOH B . 
G 6 HOH   43  1143 57   HOH   HOH B . 
G 6 HOH   44  1144 33   HOH   HOH B . 
G 6 HOH   45  1145 34   HOH   HOH B . 
G 6 HOH   46  1146 21   HOH   HOH B . 
G 6 HOH   47  1147 36   HOH   HOH B . 
G 6 HOH   48  1148 229  HOH   HOH B . 
G 6 HOH   49  1149 50   HOH   HOH B . 
G 6 HOH   50  1150 134  HOH   HOH B . 
G 6 HOH   51  1151 237  HOH   HOH B . 
G 6 HOH   52  1152 224  HOH   HOH B . 
G 6 HOH   53  1153 78   HOH   HOH B . 
G 6 HOH   54  1154 27   HOH   HOH B . 
G 6 HOH   55  1155 97   HOH   HOH B . 
G 6 HOH   56  1156 9    HOH   HOH B . 
G 6 HOH   57  1157 4    HOH   HOH B . 
G 6 HOH   58  1158 54   HOH   HOH B . 
G 6 HOH   59  1159 136  HOH   HOH B . 
G 6 HOH   60  1160 10   HOH   HOH B . 
G 6 HOH   61  1161 179  HOH   HOH B . 
G 6 HOH   62  1162 138  HOH   HOH B . 
G 6 HOH   63  1163 35   HOH   HOH B . 
G 6 HOH   64  1164 26   HOH   HOH B . 
G 6 HOH   65  1165 62   HOH   HOH B . 
G 6 HOH   66  1166 46   HOH   HOH B . 
G 6 HOH   67  1167 115  HOH   HOH B . 
G 6 HOH   68  1168 157  HOH   HOH B . 
G 6 HOH   69  1169 223  HOH   HOH B . 
G 6 HOH   70  1170 189  HOH   HOH B . 
G 6 HOH   71  1171 174  HOH   HOH B . 
G 6 HOH   72  1172 193  HOH   HOH B . 
G 6 HOH   73  1173 12   HOH   HOH B . 
G 6 HOH   74  1174 161  HOH   HOH B . 
G 6 HOH   75  1175 44   HOH   HOH B . 
G 6 HOH   76  1176 135  HOH   HOH B . 
G 6 HOH   77  1177 207  HOH   HOH B . 
G 6 HOH   78  1178 94   HOH   HOH B . 
G 6 HOH   79  1179 80   HOH   HOH B . 
G 6 HOH   80  1180 43   HOH   HOH B . 
G 6 HOH   81  1181 52   HOH   HOH B . 
G 6 HOH   82  1182 121  HOH   HOH B . 
G 6 HOH   83  1183 88   HOH   HOH B . 
G 6 HOH   84  1184 81   HOH   HOH B . 
G 6 HOH   85  1185 240  HOH   HOH B . 
G 6 HOH   86  1186 211  HOH   HOH B . 
G 6 HOH   87  1187 105  HOH   HOH B . 
G 6 HOH   88  1188 14   HOH   HOH B . 
G 6 HOH   89  1189 45   HOH   HOH B . 
G 6 HOH   90  1190 103  HOH   HOH B . 
G 6 HOH   91  1191 85   HOH   HOH B . 
G 6 HOH   92  1192 63   HOH   HOH B . 
G 6 HOH   93  1193 133  HOH   HOH B . 
G 6 HOH   94  1194 226  HOH   HOH B . 
G 6 HOH   95  1195 89   HOH   HOH B . 
G 6 HOH   96  1196 96   HOH   HOH B . 
G 6 HOH   97  1197 30   HOH   HOH B . 
G 6 HOH   98  1198 162  HOH   HOH B . 
G 6 HOH   99  1199 201  HOH   HOH B . 
G 6 HOH   100 1200 249  HOH   HOH B . 
G 6 HOH   101 1201 244  HOH   HOH B . 
G 6 HOH   102 1202 113  HOH   HOH B . 
G 6 HOH   103 1203 47   HOH   HOH B . 
G 6 HOH   104 1204 95   HOH   HOH B . 
G 6 HOH   105 1205 7    HOH   HOH B . 
G 6 HOH   106 1206 18   HOH   HOH B . 
G 6 HOH   107 1207 86   HOH   HOH B . 
G 6 HOH   108 1208 168  HOH   HOH B . 
G 6 HOH   109 1209 217  HOH   HOH B . 
G 6 HOH   110 1210 245  HOH   HOH B . 
G 6 HOH   111 1211 214  HOH   HOH B . 
G 6 HOH   112 1212 188  HOH   HOH B . 
G 6 HOH   113 1213 194  HOH   HOH B . 
G 6 HOH   114 1214 210  HOH   HOH B . 
G 6 HOH   115 1215 117  HOH   HOH B . 
G 6 HOH   116 1216 230  HOH   HOH B . 
G 6 HOH   117 1217 199  HOH   HOH B . 
G 6 HOH   118 1218 167  HOH   HOH B . 
G 6 HOH   119 1219 151  HOH   HOH B . 
G 6 HOH   120 1220 195  HOH   HOH B . 
G 6 HOH   121 1221 187  HOH   HOH B . 
G 6 HOH   122 1222 200  HOH   HOH B . 
G 6 HOH   123 1223 246  HOH   HOH B . 
G 6 HOH   124 1224 92   HOH   HOH B . 
G 6 HOH   125 1225 154  HOH   HOH B . 
G 6 HOH   126 1226 204  HOH   HOH B . 
G 6 HOH   127 1227 108  HOH   HOH B . 
G 6 HOH   128 1228 164  HOH   HOH B . 
G 6 HOH   129 1229 148  HOH   HOH B . 
G 6 HOH   130 1230 222  HOH   HOH B . 
G 6 HOH   131 1231 159  HOH   HOH B . 
G 6 HOH   132 1232 242  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 ARG 397 ? CG  ? A ARG 19  CG  
2  1 Y 1 A ARG 397 ? CD  ? A ARG 19  CD  
3  1 Y 1 A ARG 397 ? NE  ? A ARG 19  NE  
4  1 Y 1 A ARG 397 ? CZ  ? A ARG 19  CZ  
5  1 Y 1 A ARG 397 ? NH1 ? A ARG 19  NH1 
6  1 Y 1 A ARG 397 ? NH2 ? A ARG 19  NH2 
7  1 Y 1 A SER 416 ? OG  ? A SER 38  OG  
8  1 Y 1 A HIS 449 ? CG  ? A HIS 71  CG  
9  1 Y 1 A HIS 449 ? ND1 ? A HIS 71  ND1 
10 1 Y 1 A HIS 449 ? CD2 ? A HIS 71  CD2 
11 1 Y 1 A HIS 449 ? CE1 ? A HIS 71  CE1 
12 1 Y 1 A HIS 449 ? NE2 ? A HIS 71  NE2 
13 1 Y 1 A GLU 475 ? CG  ? A GLU 97  CG  
14 1 Y 1 A GLU 475 ? CD  ? A GLU 97  CD  
15 1 Y 1 A GLU 475 ? OE1 ? A GLU 97  OE1 
16 1 Y 1 A GLU 475 ? OE2 ? A GLU 97  OE2 
17 1 Y 1 A LYS 495 ? CG  ? A LYS 117 CG  
18 1 Y 1 A LYS 495 ? CD  ? A LYS 117 CD  
19 1 Y 1 A LYS 495 ? CE  ? A LYS 117 CE  
20 1 Y 1 A LYS 495 ? NZ  ? A LYS 117 NZ  
21 1 Y 1 A LYS 496 ? CG  ? A LYS 118 CG  
22 1 Y 1 A LYS 496 ? CD  ? A LYS 118 CD  
23 1 Y 1 A LYS 496 ? CE  ? A LYS 118 CE  
24 1 Y 1 A LYS 496 ? NZ  ? A LYS 118 NZ  
25 1 Y 1 A ARG 663 ? CG  ? A ARG 169 CG  
26 1 Y 1 A ARG 663 ? CD  ? A ARG 169 CD  
27 1 Y 1 A ARG 663 ? NE  ? A ARG 169 NE  
28 1 Y 1 A ARG 663 ? CZ  ? A ARG 169 CZ  
29 1 Y 1 A ARG 663 ? NH1 ? A ARG 169 NH1 
30 1 Y 1 A ARG 663 ? NH2 ? A ARG 169 NH2 
31 1 Y 1 A GLU 698 ? CG  ? A GLU 204 CG  
32 1 Y 1 A GLU 698 ? CD  ? A GLU 204 CD  
33 1 Y 1 A GLU 698 ? OE1 ? A GLU 204 OE1 
34 1 Y 1 A GLU 698 ? OE2 ? A GLU 204 OE2 
35 1 Y 1 A GLU 707 ? CG  ? A GLU 213 CG  
36 1 Y 1 A GLU 707 ? CD  ? A GLU 213 CD  
37 1 Y 1 A GLU 707 ? OE1 ? A GLU 213 OE1 
38 1 Y 1 A GLU 707 ? OE2 ? A GLU 213 OE2 
39 1 Y 1 A LYS 708 ? CG  ? A LYS 214 CG  
40 1 Y 1 A LYS 708 ? CD  ? A LYS 214 CD  
41 1 Y 1 A LYS 708 ? CE  ? A LYS 214 CE  
42 1 Y 1 A LYS 708 ? NZ  ? A LYS 214 NZ  
43 1 Y 1 A GLU 716 ? CG  ? A GLU 222 CG  
44 1 Y 1 A GLU 716 ? CD  ? A GLU 222 CD  
45 1 Y 1 A GLU 716 ? OE1 ? A GLU 222 OE1 
46 1 Y 1 A GLU 716 ? OE2 ? A GLU 222 OE2 
47 1 Y 1 A LYS 725 ? CG  ? A LYS 231 CG  
48 1 Y 1 A LYS 725 ? CD  ? A LYS 231 CD  
49 1 Y 1 A LYS 725 ? CE  ? A LYS 231 CE  
50 1 Y 1 A LYS 725 ? NZ  ? A LYS 231 NZ  
51 1 Y 1 A GLU 751 ? CG  ? A GLU 257 CG  
52 1 Y 1 A GLU 751 ? CD  ? A GLU 257 CD  
53 1 Y 1 A GLU 751 ? OE1 ? A GLU 257 OE1 
54 1 Y 1 A GLU 751 ? OE2 ? A GLU 257 OE2 
55 1 Y 1 B GLU 427 ? CG  ? B GLU 41  CG  
56 1 Y 1 B GLU 427 ? CD  ? B GLU 41  CD  
57 1 Y 1 B GLU 427 ? OE1 ? B GLU 41  OE1 
58 1 Y 1 B GLU 427 ? OE2 ? B GLU 41  OE2 
59 1 Y 1 B LYS 453 ? CG  ? B LYS 67  CG  
60 1 Y 1 B LYS 453 ? CD  ? B LYS 67  CD  
61 1 Y 1 B LYS 453 ? CE  ? B LYS 67  CE  
62 1 Y 1 B LYS 453 ? NZ  ? B LYS 67  NZ  
63 1 Y 1 B GLN 542 ? CG  ? B GLN 156 CG  
64 1 Y 1 B GLN 542 ? CD  ? B GLN 156 CD  
65 1 Y 1 B GLN 542 ? OE1 ? B GLN 156 OE1 
66 1 Y 1 B GLN 542 ? NE2 ? B GLN 156 NE2 
67 1 Y 1 B GLU 743 ? CG  ? B GLU 238 CG  
68 1 Y 1 B GLU 743 ? CD  ? B GLU 238 CD  
69 1 Y 1 B GLU 743 ? OE1 ? B GLU 238 OE1 
70 1 Y 1 B GLU 743 ? OE2 ? B GLU 238 OE2 
71 1 Y 1 B LYS 746 ? CG  ? B LYS 241 CG  
72 1 Y 1 B LYS 746 ? CD  ? B LYS 241 CD  
73 1 Y 1 B LYS 746 ? CE  ? B LYS 241 CE  
74 1 Y 1 B LYS 746 ? NZ  ? B LYS 241 NZ  
75 1 Y 1 B GLU 789 ? CG  ? B GLU 284 CG  
76 1 Y 1 B GLU 789 ? CD  ? B GLU 284 CD  
77 1 Y 1 B GLU 789 ? OE1 ? B GLU 284 OE1 
78 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 reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? 0.5.893     2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? 0.5.893     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                     9MUL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     54.928 
_cell.length_a_esd                 ? 
_cell.length_b                     90.013 
_cell.length_b_esd                 ? 
_cell.length_c                     124.006 
_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                         9MUL 
_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                   9MUL 
_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          44.86 
_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 PILATUS 200K' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-01-20 
_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   1.54 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU FR-E SUPERBRIGHT' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MUL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.40 
_reflns.d_resolution_low                               36.42 
_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                                     23262 
_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                           94.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.04 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.07948 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.986 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    2.40 
_reflns_shell.d_res_low                                     2.49 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.28 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2048 
_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                               3.4 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.3087 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.724 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          85.26 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9MUL 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.40 
_refine.ls_d_res_low                             36.42 
_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                     23256 
_refine.ls_number_reflns_R_free                  1143 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.24 
_refine.ls_percent_reflns_R_free                 4.91 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1993 
_refine.ls_R_factor_R_free                       0.2524 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1966 
_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                 23.80 
_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                            0.29 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.40 
_refine_hist.d_res_low                        36.42 
_refine_hist.number_atoms_solvent             252 
_refine_hist.number_atoms_total               4582 
_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        4286 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         44 
_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' ? 0.002 ? 4418 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.460 ? 5975 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 4.737 ? 593  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.042 ? 666  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.003 ? 771  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.40 2.51  . . 151 2452 86.00 . . . . 0.2601 . . . . . . . . . . . 0.3386 
'X-RAY DIFFRACTION' 2.51 2.64  . . 120 2606 90.00 . . . . 0.2481 . . . . . . . . . . . 0.3239 
'X-RAY DIFFRACTION' 2.64 2.81  . . 130 2719 94.00 . . . . 0.2383 . . . . . . . . . . . 0.2957 
'X-RAY DIFFRACTION' 2.81 3.03  . . 164 2807 97.00 . . . . 0.2322 . . . . . . . . . . . 0.2929 
'X-RAY DIFFRACTION' 3.03 3.33  . . 132 2849 98.00 . . . . 0.2021 . . . . . . . . . . . 0.2613 
'X-RAY DIFFRACTION' 3.33 3.81  . . 159 2847 98.00 . . . . 0.1784 . . . . . . . . . . . 0.2533 
'X-RAY DIFFRACTION' 3.81 4.80  . . 137 2894 97.00 . . . . 0.1545 . . . . . . . . . . . 0.1970 
'X-RAY DIFFRACTION' 4.80 36.42 . . 150 2939 95.00 . . . . 0.1805 . . . . . . . . . . . 0.2006 
# 
_struct.entry_id                     9MUL 
_struct.title                        
'Crystal structure of GluN1/GluN2A ligand-binding domain in complex with Compound 1, 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        9MUL 
_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 9MUL A 16  ? 166 ? Q05586 394 ? 544 ? 394 544 
2 2 9MUL A 169 ? 306 ? Q05586 663 ? 800 ? 663 800 
3 3 9MUL B 15  ? 153 ? Q12879 401 ? 539 ? 401 539 
4 4 9MUL 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 9MUL MET A 1   ? UNP Q05586 ? ? 'initiating methionine' 379 1  
1 9MUL HIS A 2   ? UNP Q05586 ? ? 'expression tag'        380 2  
1 9MUL HIS A 3   ? UNP Q05586 ? ? 'expression tag'        381 3  
1 9MUL HIS A 4   ? UNP Q05586 ? ? 'expression tag'        382 4  
1 9MUL HIS A 5   ? UNP Q05586 ? ? 'expression tag'        383 5  
1 9MUL HIS A 6   ? UNP Q05586 ? ? 'expression tag'        384 6  
1 9MUL HIS A 7   ? UNP Q05586 ? ? 'expression tag'        385 7  
1 9MUL GLU A 8   ? UNP Q05586 ? ? 'expression tag'        386 8  
1 9MUL ASN A 9   ? UNP Q05586 ? ? 'expression tag'        387 9  
1 9MUL LEU A 10  ? UNP Q05586 ? ? 'expression tag'        388 10 
1 9MUL TYR A 11  ? UNP Q05586 ? ? 'expression tag'        389 11 
1 9MUL PHE A 12  ? UNP Q05586 ? ? 'expression tag'        390 12 
1 9MUL GLN A 13  ? UNP Q05586 ? ? 'expression tag'        391 13 
1 9MUL GLY A 14  ? UNP Q05586 ? ? 'expression tag'        392 14 
1 9MUL SER A 15  ? UNP Q05586 ? ? 'expression tag'        393 15 
1 9MUL GLY A 167 ? UNP Q05586 ? ? linker                  545 16 
1 9MUL THR A 168 ? UNP Q05586 ? ? linker                  546 17 
3 9MUL MET B 1   ? UNP Q12879 ? ? 'initiating methionine' 387 18 
3 9MUL HIS B 2   ? UNP Q12879 ? ? 'expression tag'        388 19 
3 9MUL HIS B 3   ? UNP Q12879 ? ? 'expression tag'        389 20 
3 9MUL HIS B 4   ? UNP Q12879 ? ? 'expression tag'        390 21 
3 9MUL HIS B 5   ? UNP Q12879 ? ? 'expression tag'        391 22 
3 9MUL HIS B 6   ? UNP Q12879 ? ? 'expression tag'        392 23 
3 9MUL HIS B 7   ? UNP Q12879 ? ? 'expression tag'        393 24 
3 9MUL GLU B 8   ? UNP Q12879 ? ? 'expression tag'        394 25 
3 9MUL ASN B 9   ? UNP Q12879 ? ? 'expression tag'        395 26 
3 9MUL LEU B 10  ? UNP Q12879 ? ? 'expression tag'        396 27 
3 9MUL TYR B 11  ? UNP Q12879 ? ? 'expression tag'        397 28 
3 9MUL PHE B 12  ? UNP Q12879 ? ? 'expression tag'        398 29 
3 9MUL GLN B 13  ? UNP Q12879 ? ? 'expression tag'        399 30 
3 9MUL GLY B 14  ? UNP Q12879 ? ? 'expression tag'        400 31 
3 9MUL GLY B 154 ? UNP Q12879 ? ? linker                  540 32 
3 9MUL 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)' 2320  ? 
1 MORE         -7    ? 
1 'SSA (A^2)'  24160 ? 
# 
_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  ? VAL B 85  ? GLY B 458 VAL B 471 1 ? 14 
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 GLU B 282 ? LEU B 291 ? GLU B 787 LEU B 796 1 ? 10 
# 
_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 ? ? ? ? ? ? ? 2.030 ? ? 
disulf2 disulf ? ? A CYS 58  SG ? ? ? 1_555 A CYS 77  SG ? ? A CYS 436 A CYS 455 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf3 disulf ? ? B CYS 43  SG ? ? ? 1_555 B CYS 69  SG ? ? B CYS 429 B CYS 455 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf4 disulf ? ? B CYS 50  SG ? ? ? 1_555 B CYS 70  SG ? ? B CYS 436 B CYS 456 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf5 disulf ? ? B CYS 240 SG ? ? ? 1_555 B CYS 295 SG ? ? B CYS 745 B CYS 800 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
# 
_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 3.34  
2 ALA 28  B . ? ALA 414 B PRO 29  B ? PRO 415 B 1 1.87  
3 SER 172 B . ? SER 677 B PRO 173 B ? PRO 678 B 1 -1.29 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
AA4 ? 8 ? 
AA5 ? 2 ? 
AA6 ? 4 ? 
AA7 ? 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 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA4 6 7 ? anti-parallel 
AA4 7 8 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 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 ? PHE A 264 ? LEU A 746 PHE A 758 
AA4 1 ILE B 32  ? GLU B 34  ? ILE B 418 GLU B 420 
AA4 2 GLY B 63  ? LYS B 71  ? GLY B 449 LYS B 457 
AA4 3 VAL B 48  ? LYS B 55  ? VAL B 434 LYS B 441 
AA4 4 THR B 88  ? LEU B 93  ? THR B 474 LEU B 479 
AA4 5 HIS B 19  ? THR B 24  ? HIS B 405 THR B 410 
AA4 6 MET B 121 ? ALA B 122 ? MET B 507 ALA B 508 
AA4 7 ALA B 259 ? LEU B 260 ? ALA B 764 LEU B 765 
AA4 8 ASP B 137 ? PHE B 138 ? ASP B 523 PHE B 524 
AA5 1 LYS B 102 ? VAL B 103 ? LYS B 488 VAL B 489 
AA5 2 VAL B 106 ? TRP B 107 ? VAL B 492 TRP B 493 
AA6 1 PHE B 177 ? GLY B 178 ? PHE B 682 GLY B 683 
AA6 2 ALA B 222 ? ASP B 226 ? ALA B 727 ASP B 731 
AA6 3 VAL B 143 ? SER B 152 ? VAL B 529 SER B 538 
AA6 4 LEU B 242 ? THR B 244 ? LEU B 747 THR B 749 
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 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 ILE B 32  ? N ILE B 418 O LYS B 71  ? O LYS B 457 
AA4 2 3 O CYS B 70  ? O CYS B 456 N VAL B 48  ? N VAL B 434 
AA4 3 4 N ARG B 51  ? N ARG B 437 O LEU B 93  ? O LEU B 479 
AA4 4 5 O THR B 88  ? O THR B 474 N LEU B 20  ? N LEU B 406 
AA4 5 6 N VAL B 23  ? N VAL B 409 O MET B 121 ? O MET B 507 
AA4 6 7 N ALA B 122 ? N ALA B 508 O ALA B 259 ? O ALA B 764 
AA4 7 8 O LEU B 260 ? O LEU B 765 N ASP B 137 ? N ASP B 523 
AA5 1 2 N VAL B 103 ? N VAL B 489 O VAL B 106 ? O VAL B 492 
AA6 1 2 N GLY B 178 ? N GLY B 683 O ILE B 224 ? O ILE B 729 
AA6 2 3 O PHE B 223 ? O PHE B 728 N MET B 150 ? N MET B 536 
AA6 3 4 N VAL B 151 ? N VAL B 537 O VAL B 243 ? O VAL B 748 
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 THR B 145 ? N THR B 531 O THR B 254 ? O THR B 759 
# 
_pdbx_entry_details.entry_id                   9MUL 
_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 ? ? -165.76 88.60   
2  1 ASN A 471 ? ? 61.51   67.33   
3  1 PRO A 516 ? ? -66.54  71.69   
4  1 GLN A 536 ? ? -149.23 -141.29 
5  1 GLU A 751 ? ? -88.31  -131.82 
6  1 ARG B 431 ? ? 58.54   -132.25 
7  1 LYS B 472 ? ? 62.82   80.15   
8  1 LYS B 484 ? ? -121.70 -108.31 
9  1 ASN B 494 ? ? -108.82 -166.62 
10 1 ARG B 672 ? ? -119.90 72.61   
11 1 THR B 759 ? ? -150.43 -152.06 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 6.4114   -21.7092 39.2959 0.2599 ? 0.0551  ? -0.1384 ? 0.2272 ? -0.0554 ? 0.3702 ? 1.4749 ? 
-0.8276 ? -0.2310 ? 0.7234 ? -0.2064 ? 1.5424 ? 0.1359  ? -0.0059 ? -0.3720 ? 0.3201  ? 0.0643  ? -0.3798 ? 0.2627  ? 0.1094  ? 
-0.0910 ? 
2  'X-RAY DIFFRACTION' ? refined 9.1505   -16.8252 41.9245 0.2467 ? 0.0581  ? -0.1141 ? 0.2363 ? -0.0408 ? 0.4354 ? 0.8096 ? 
-0.0389 ? -0.7472 ? 1.6899 ? 0.0147  ? 0.9780 ? 0.1854  ? -0.2975 ? -0.2881 ? 0.1628  ? -0.0893 ? 0.0142  ? -0.1150 ? 0.0074  ? 
-0.0104 ? 
3  'X-RAY DIFFRACTION' ? refined 1.3388   -7.4669  34.0122 0.1571 ? -0.0186 ? -0.0792 ? 0.1889 ? -0.0258 ? 0.2479 ? 1.4558 ? 
0.0319  ? 0.8372  ? 1.2110 ? -0.8798 ? 1.2840 ? -0.1094 ? -0.0462 ? 0.1591  ? 0.1756  ? 0.0802  ? -0.4397 ? -0.1034 ? 0.1517  ? 
0.0196  ? 
4  'X-RAY DIFFRACTION' ? refined -11.2764 -9.5572  33.3350 0.2614 ? 0.0551  ? -0.0757 ? 0.1337 ? -0.0439 ? 0.2358 ? 1.7455 ? 
0.8391  ? 0.0808  ? 0.3898 ? 0.0812  ? 1.9189 ? 0.0042  ? -0.0450 ? -0.0174 ? 0.2934  ? -0.2281 ? 0.0132  ? -0.4088 ? 0.0873  ? 
0.1984  ? 
5  'X-RAY DIFFRACTION' ? refined -21.2569 -10.2587 48.2394 0.2483 ? 0.0354  ? 0.0269  ? 0.3087 ? -0.0532 ? 0.3454 ? 2.2886 ? 
-0.2904 ? 0.0375  ? 2.0498 ? -0.0488 ? 1.5615 ? 0.0416  ? -0.2238 ? -0.1523 ? 0.4264  ? -0.0164 ? 0.3506  ? -0.0754 ? -0.4379 ? 
-0.0238 ? 
6  'X-RAY DIFFRACTION' ? refined -14.4874 -13.9602 48.8257 0.2827 ? 0.0410  ? -0.0015 ? 0.2918 ? 0.0175  ? 0.1806 ? 3.0309 ? 
0.3800  ? 0.2381  ? 1.3258 ? -0.5113 ? 2.2939 ? -0.0893 ? -0.5963 ? -0.2736 ? 0.4634  ? 0.0139  ? 0.0877  ? 0.0560  ? -0.0683 ? 
0.0703  ? 
7  'X-RAY DIFFRACTION' ? refined -17.3944 -19.4908 40.4912 0.1738 ? 0.0505  ? -0.0017 ? 0.2480 ? -0.0039 ? 0.2217 ? 1.1047 ? 
0.2936  ? -0.0164 ? 2.1013 ? -0.9038 ? 3.2994 ? -0.0891 ? -0.1542 ? -0.4057 ? 0.2408  ? 0.0325  ? 0.3973  ? 0.2179  ? -0.6462 ? 
0.0713  ? 
8  'X-RAY DIFFRACTION' ? refined -1.0391  -9.4932  21.4578 0.1505 ? -0.0167 ? 0.0111  ? 0.2408 ? -0.0259 ? 0.2157 ? 1.2369 ? 
1.1443  ? 0.5396  ? 3.0629 ? 0.9540  ? 2.5311 ? 0.0082  ? 0.5077  ? -0.1119 ? -0.3267 ? 0.1265  ? -0.1661 ? -0.2054 ? 0.0967  ? 
-0.0687 ? 
9  'X-RAY DIFFRACTION' ? refined -5.4319  -26.1535 29.6855 0.2816 ? -0.0641 ? -0.0593 ? 0.2502 ? -0.0087 ? 0.2892 ? 1.5400 ? 
-1.2774 ? 0.5970  ? 1.3726 ? 0.5639  ? 6.3001 ? 0.4385  ? -0.1903 ? -0.4231 ? -0.2738 ? 0.0846  ? 0.1883  ? 1.0106  ? -0.4928 ? 
-0.4792 ? 
10 'X-RAY DIFFRACTION' ? refined -26.9855 -5.1573  10.5051 0.1756 ? 0.0945  ? -0.0944 ? 0.1785 ? -0.0115 ? 0.1663 ? 1.6431 ? 
-1.2156 ? -0.2957 ? 2.6445 ? -0.8579 ? 2.9236 ? -0.2518 ? -0.1436 ? 0.2607  ? -0.2740 ? 0.1364  ? 0.2411  ? -0.2146 ? -0.2523 ? 
0.0639  ? 
11 'X-RAY DIFFRACTION' ? refined -33.9623 -4.6157  0.3027  0.2646 ? 0.0055  ? -0.0514 ? 0.2339 ? 0.0807  ? 0.2126 ? 2.7412 ? 
-0.2135 ? 0.7627  ? 2.6967 ? 1.3264  ? 5.7381 ? 0.0165  ? 0.0220  ? 0.1895  ? -0.1840 ? 0.1330  ? -0.1457 ? -0.8865 ? -0.8472 ? 
0.0746  ? 
12 'X-RAY DIFFRACTION' ? refined -20.1958 -8.1805  10.4388 0.1678 ? -0.0084 ? -0.0101 ? 0.1447 ? -0.0117 ? 0.1359 ? 1.4346 ? 
-0.6220 ? 0.5425  ? 0.8864 ? -0.3786 ? 1.1550 ? -0.1281 ? 0.0531  ? 0.2427  ? -0.0232 ? 0.0917  ? -0.1237 ? -0.1887 ? -0.0474 ? 
0.0372  ? 
13 'X-RAY DIFFRACTION' ? refined -18.0580 -37.9521 14.1325 0.2618 ? -0.0035 ? 0.0055  ? 0.2627 ? 0.0605  ? 0.1534 ? 1.5470 ? 
-0.2756 ? -1.0143 ? 2.0957 ? -0.4119 ? 1.5913 ? 0.0402  ? -0.4414 ? -0.2883 ? -0.0329 ? -0.1645 ? 0.0391  ? 0.3784  ? 0.2893  ? 
0.1058  ? 
14 'X-RAY DIFFRACTION' ? refined -13.0160 -30.7331 7.9769  0.1960 ? 0.0065  ? -0.0147 ? 0.2087 ? -0.0242 ? 0.1640 ? 1.4132 ? 
-1.2030 ? 0.1081  ? 3.6802 ? 1.1929  ? 1.8190 ? 0.0639  ? 0.3214  ? 0.1087  ? -0.6817 ? 0.1588  ? -0.4342 ? 0.2174  ? 0.1535  ? 
-0.1571 ? 
15 'X-RAY DIFFRACTION' ? refined -28.8502 -28.3283 15.3876 0.1587 ? -0.0339 ? -0.0195 ? 0.1827 ? 0.0300  ? 0.1702 ? 2.3454 ? 
0.4839  ? -0.7142 ? 3.4654 ? 0.3883  ? 2.0179 ? -0.0760 ? -0.1002 ? 0.0285  ? 0.0693  ? 0.0233  ? 0.3692  ? 0.1012  ? -0.5152 ? 
0.0037  ? 
16 'X-RAY DIFFRACTION' ? refined -14.0794 -10.0753 16.8218 0.1899 ? -0.0407 ? -0.1273 ? 0.0923 ? -0.0089 ? 0.2523 ? 2.2005 ? 
-0.3063 ? -0.3835 ? 2.7353 ? 0.0088  ? 1.6703 ? 0.2023  ? 0.1205  ? 0.1271  ? 0.3214  ? -0.1357 ? -0.3626 ? -0.1836 ? 0.2659  ? 
-0.0689 ? 
17 'X-RAY DIFFRACTION' ? refined -24.2708 -6.6102  25.4051 0.2445 ? 0.1435  ? 0.0179  ? 0.3213 ? -0.0274 ? 0.1575 ? 2.0753 ? 
-0.0436 ? -0.0191 ? 1.8456 ? 0.1947  ? 1.8541 ? -0.2756 ? -0.5573 ? 0.4376  ? 0.6072  ? 0.1323  ? 0.1222  ? -0.3200 ? -0.3475 ? 
0.0202  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 397 through 428 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 429 through 457 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 458 through 520 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 521 through 543 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 544 through 696 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 697 through 742 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 743 through 758 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 759 through 781 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 782 through 1001 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 403 through 420 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 421 through 448 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 449 through 538 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 539 through 688 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 689 through 708 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 709 through 753 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 754 through 771 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 772 through 1001 )
;
# 
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 
A1BRA C1   C  N N 1   
A1BRA C13  C  Y N 2   
A1BRA C14  C  Y N 3   
A1BRA C15  C  Y N 4   
A1BRA C16  C  Y N 5   
A1BRA C17  C  Y N 6   
A1BRA C19  C  Y N 7   
A1BRA C2   C  Y N 8   
A1BRA C20  C  N N 9   
A1BRA C23  C  N N 10  
A1BRA C24  C  Y N 11  
A1BRA C25  C  Y N 12  
A1BRA C26  C  Y N 13  
A1BRA C27  C  Y N 14  
A1BRA C29  C  Y N 15  
A1BRA C4   C  Y N 16  
A1BRA C5   C  Y N 17  
A1BRA C7   C  Y N 18  
A1BRA C9   C  N N 19  
A1BRA N22  N  N N 20  
A1BRA N28  N  Y N 21  
A1BRA N3   N  Y N 22  
A1BRA N6   N  Y N 23  
A1BRA O11  O  N N 24  
A1BRA O12  O  N N 25  
A1BRA O21  O  N N 26  
A1BRA O8   O  N N 27  
A1BRA S10  S  N N 28  
A1BRA CL18 CL N N 29  
A1BRA H1   H  N N 30  
A1BRA H2   H  N N 31  
A1BRA H3   H  N N 32  
A1BRA H4   H  N N 33  
A1BRA H5   H  N N 34  
A1BRA H6   H  N N 35  
A1BRA H7   H  N N 36  
A1BRA H8   H  N N 37  
A1BRA H9   H  N N 38  
A1BRA H10  H  N N 39  
A1BRA H11  H  N N 40  
A1BRA H12  H  N N 41  
A1BRA H13  H  N N 42  
A1BRA H14  H  N N 43  
A1BRA H15  H  N N 44  
A1BRA H16  H  N N 45  
A1BRA H17  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 
A1BRA CL18 C17  sing N N 1   
A1BRA C27  C26  doub Y N 2   
A1BRA C27  N28  sing Y N 3   
A1BRA C26  C25  sing Y N 4   
A1BRA N28  C29  doub Y N 5   
A1BRA C1   C2   sing N N 6   
A1BRA C25  C24  doub Y N 7   
A1BRA C29  C24  sing Y N 8   
A1BRA O12  S10  doub N N 9   
A1BRA C24  C23  sing N N 10  
A1BRA C17  C19  doub Y N 11  
A1BRA C17  C16  sing Y N 12  
A1BRA C19  C13  sing Y N 13  
A1BRA C23  N22  sing N N 14  
A1BRA N22  C20  sing N N 15  
A1BRA C2   N3   doub Y N 16  
A1BRA C2   C7   sing Y N 17  
A1BRA N3   C4   sing Y N 18  
A1BRA C16  C15  doub Y N 19  
A1BRA C13  S10  sing N N 20  
A1BRA C13  C14  doub Y N 21  
A1BRA S10  O11  doub N N 22  
A1BRA S10  C9   sing N N 23  
A1BRA O8   C7   sing N N 24  
A1BRA O8   C9   sing N N 25  
A1BRA C7   N6   doub Y N 26  
A1BRA C4   C20  sing N N 27  
A1BRA C4   C5   doub Y N 28  
A1BRA C20  O21  doub N N 29  
A1BRA C15  C14  sing Y N 30  
A1BRA N6   C5   sing Y N 31  
A1BRA C1   H1   sing N N 32  
A1BRA C1   H2   sing N N 33  
A1BRA C1   H3   sing N N 34  
A1BRA C14  H4   sing N N 35  
A1BRA C15  H5   sing N N 36  
A1BRA C16  H6   sing N N 37  
A1BRA C19  H7   sing N N 38  
A1BRA C23  H8   sing N N 39  
A1BRA C23  H9   sing N N 40  
A1BRA C25  H10  sing N N 41  
A1BRA C26  H11  sing N N 42  
A1BRA C27  H12  sing N N 43  
A1BRA C29  H13  sing N N 44  
A1BRA C5   H14  sing N N 45  
A1BRA C9   H15  sing N N 46  
A1BRA C9   H16  sing N N 47  
A1BRA N22  H17  sing N N 48  
ALA   N    CA   sing N N 49  
ALA   N    H    sing N N 50  
ALA   N    H2   sing N N 51  
ALA   CA   C    sing N N 52  
ALA   CA   CB   sing N N 53  
ALA   CA   HA   sing N N 54  
ALA   C    O    doub N N 55  
ALA   C    OXT  sing N N 56  
ALA   CB   HB1  sing N N 57  
ALA   CB   HB2  sing N N 58  
ALA   CB   HB3  sing N N 59  
ALA   OXT  HXT  sing N N 60  
ARG   N    CA   sing N N 61  
ARG   N    H    sing N N 62  
ARG   N    H2   sing N N 63  
ARG   CA   C    sing N N 64  
ARG   CA   CB   sing N N 65  
ARG   CA   HA   sing N N 66  
ARG   C    O    doub N N 67  
ARG   C    OXT  sing N N 68  
ARG   CB   CG   sing N N 69  
ARG   CB   HB2  sing N N 70  
ARG   CB   HB3  sing N N 71  
ARG   CG   CD   sing N N 72  
ARG   CG   HG2  sing N N 73  
ARG   CG   HG3  sing N N 74  
ARG   CD   NE   sing N N 75  
ARG   CD   HD2  sing N N 76  
ARG   CD   HD3  sing N N 77  
ARG   NE   CZ   sing N N 78  
ARG   NE   HE   sing N N 79  
ARG   CZ   NH1  sing N N 80  
ARG   CZ   NH2  doub N N 81  
ARG   NH1  HH11 sing N N 82  
ARG   NH1  HH12 sing N N 83  
ARG   NH2  HH21 sing N N 84  
ARG   NH2  HH22 sing N N 85  
ARG   OXT  HXT  sing N N 86  
ASN   N    CA   sing N N 87  
ASN   N    H    sing N N 88  
ASN   N    H2   sing N N 89  
ASN   CA   C    sing N N 90  
ASN   CA   CB   sing N N 91  
ASN   CA   HA   sing N N 92  
ASN   C    O    doub N N 93  
ASN   C    OXT  sing N N 94  
ASN   CB   CG   sing N N 95  
ASN   CB   HB2  sing N N 96  
ASN   CB   HB3  sing N N 97  
ASN   CG   OD1  doub N N 98  
ASN   CG   ND2  sing N N 99  
ASN   ND2  HD21 sing N N 100 
ASN   ND2  HD22 sing N N 101 
ASN   OXT  HXT  sing N N 102 
ASP   N    CA   sing N N 103 
ASP   N    H    sing N N 104 
ASP   N    H2   sing N N 105 
ASP   CA   C    sing N N 106 
ASP   CA   CB   sing N N 107 
ASP   CA   HA   sing N N 108 
ASP   C    O    doub N N 109 
ASP   C    OXT  sing N N 110 
ASP   CB   CG   sing N N 111 
ASP   CB   HB2  sing N N 112 
ASP   CB   HB3  sing N N 113 
ASP   CG   OD1  doub N N 114 
ASP   CG   OD2  sing N N 115 
ASP   OD2  HD2  sing N N 116 
ASP   OXT  HXT  sing N N 117 
CYS   N    CA   sing N N 118 
CYS   N    H    sing N N 119 
CYS   N    H2   sing N N 120 
CYS   CA   C    sing N N 121 
CYS   CA   CB   sing N N 122 
CYS   CA   HA   sing N N 123 
CYS   C    O    doub N N 124 
CYS   C    OXT  sing N N 125 
CYS   CB   SG   sing N N 126 
CYS   CB   HB2  sing N N 127 
CYS   CB   HB3  sing N N 128 
CYS   SG   HG   sing N N 129 
CYS   OXT  HXT  sing N N 130 
GLN   N    CA   sing N N 131 
GLN   N    H    sing N N 132 
GLN   N    H2   sing N N 133 
GLN   CA   C    sing N N 134 
GLN   CA   CB   sing N N 135 
GLN   CA   HA   sing N N 136 
GLN   C    O    doub N N 137 
GLN   C    OXT  sing N N 138 
GLN   CB   CG   sing N N 139 
GLN   CB   HB2  sing N N 140 
GLN   CB   HB3  sing N N 141 
GLN   CG   CD   sing N N 142 
GLN   CG   HG2  sing N N 143 
GLN   CG   HG3  sing N N 144 
GLN   CD   OE1  doub N N 145 
GLN   CD   NE2  sing N N 146 
GLN   NE2  HE21 sing N N 147 
GLN   NE2  HE22 sing N N 148 
GLN   OXT  HXT  sing N N 149 
GLU   N    CA   sing N N 150 
GLU   N    H    sing N N 151 
GLU   N    H2   sing N N 152 
GLU   CA   C    sing N N 153 
GLU   CA   CB   sing N N 154 
GLU   CA   HA   sing N N 155 
GLU   C    O    doub N N 156 
GLU   C    OXT  sing N N 157 
GLU   CB   CG   sing N N 158 
GLU   CB   HB2  sing N N 159 
GLU   CB   HB3  sing N N 160 
GLU   CG   CD   sing N N 161 
GLU   CG   HG2  sing N N 162 
GLU   CG   HG3  sing N N 163 
GLU   CD   OE1  doub N N 164 
GLU   CD   OE2  sing N N 165 
GLU   OE2  HE2  sing N N 166 
GLU   OXT  HXT  sing N N 167 
GLY   N    CA   sing N N 168 
GLY   N    H    sing N N 169 
GLY   N    H2   sing N N 170 
GLY   CA   C    sing N N 171 
GLY   CA   HA2  sing N N 172 
GLY   CA   HA3  sing N N 173 
GLY   C    O    doub N N 174 
GLY   C    OXT  sing N N 175 
GLY   OXT  HXT  sing N N 176 
HIS   N    CA   sing N N 177 
HIS   N    H    sing N N 178 
HIS   N    H2   sing N N 179 
HIS   CA   C    sing N N 180 
HIS   CA   CB   sing N N 181 
HIS   CA   HA   sing N N 182 
HIS   C    O    doub N N 183 
HIS   C    OXT  sing N N 184 
HIS   CB   CG   sing N N 185 
HIS   CB   HB2  sing N N 186 
HIS   CB   HB3  sing N N 187 
HIS   CG   ND1  sing Y N 188 
HIS   CG   CD2  doub Y N 189 
HIS   ND1  CE1  doub Y N 190 
HIS   ND1  HD1  sing N N 191 
HIS   CD2  NE2  sing Y N 192 
HIS   CD2  HD2  sing N N 193 
HIS   CE1  NE2  sing Y N 194 
HIS   CE1  HE1  sing N N 195 
HIS   NE2  HE2  sing N N 196 
HIS   OXT  HXT  sing N N 197 
HOH   O    H1   sing N N 198 
HOH   O    H2   sing N N 199 
ILE   N    CA   sing N N 200 
ILE   N    H    sing N N 201 
ILE   N    H2   sing N N 202 
ILE   CA   C    sing N N 203 
ILE   CA   CB   sing N N 204 
ILE   CA   HA   sing N N 205 
ILE   C    O    doub N N 206 
ILE   C    OXT  sing N N 207 
ILE   CB   CG1  sing N N 208 
ILE   CB   CG2  sing N N 209 
ILE   CB   HB   sing N N 210 
ILE   CG1  CD1  sing N N 211 
ILE   CG1  HG12 sing N N 212 
ILE   CG1  HG13 sing N N 213 
ILE   CG2  HG21 sing N N 214 
ILE   CG2  HG22 sing N N 215 
ILE   CG2  HG23 sing N N 216 
ILE   CD1  HD11 sing N N 217 
ILE   CD1  HD12 sing N N 218 
ILE   CD1  HD13 sing N N 219 
ILE   OXT  HXT  sing N N 220 
LEU   N    CA   sing N N 221 
LEU   N    H    sing N N 222 
LEU   N    H2   sing N N 223 
LEU   CA   C    sing N N 224 
LEU   CA   CB   sing N N 225 
LEU   CA   HA   sing N N 226 
LEU   C    O    doub N N 227 
LEU   C    OXT  sing N N 228 
LEU   CB   CG   sing N N 229 
LEU   CB   HB2  sing N N 230 
LEU   CB   HB3  sing N N 231 
LEU   CG   CD1  sing N N 232 
LEU   CG   CD2  sing N N 233 
LEU   CG   HG   sing N N 234 
LEU   CD1  HD11 sing N N 235 
LEU   CD1  HD12 sing N N 236 
LEU   CD1  HD13 sing N N 237 
LEU   CD2  HD21 sing N N 238 
LEU   CD2  HD22 sing N N 239 
LEU   CD2  HD23 sing N N 240 
LEU   OXT  HXT  sing N N 241 
LYS   N    CA   sing N N 242 
LYS   N    H    sing N N 243 
LYS   N    H2   sing N N 244 
LYS   CA   C    sing N N 245 
LYS   CA   CB   sing N N 246 
LYS   CA   HA   sing N N 247 
LYS   C    O    doub N N 248 
LYS   C    OXT  sing N N 249 
LYS   CB   CG   sing N N 250 
LYS   CB   HB2  sing N N 251 
LYS   CB   HB3  sing N N 252 
LYS   CG   CD   sing N N 253 
LYS   CG   HG2  sing N N 254 
LYS   CG   HG3  sing N N 255 
LYS   CD   CE   sing N N 256 
LYS   CD   HD2  sing N N 257 
LYS   CD   HD3  sing N N 258 
LYS   CE   NZ   sing N N 259 
LYS   CE   HE2  sing N N 260 
LYS   CE   HE3  sing N N 261 
LYS   NZ   HZ1  sing N N 262 
LYS   NZ   HZ2  sing N N 263 
LYS   NZ   HZ3  sing N N 264 
LYS   OXT  HXT  sing N N 265 
MET   N    CA   sing N N 266 
MET   N    H    sing N N 267 
MET   N    H2   sing N N 268 
MET   CA   C    sing N N 269 
MET   CA   CB   sing N N 270 
MET   CA   HA   sing N N 271 
MET   C    O    doub N N 272 
MET   C    OXT  sing N N 273 
MET   CB   CG   sing N N 274 
MET   CB   HB2  sing N N 275 
MET   CB   HB3  sing N N 276 
MET   CG   SD   sing N N 277 
MET   CG   HG2  sing N N 278 
MET   CG   HG3  sing N N 279 
MET   SD   CE   sing N N 280 
MET   CE   HE1  sing N N 281 
MET   CE   HE2  sing N N 282 
MET   CE   HE3  sing N N 283 
MET   OXT  HXT  sing N N 284 
PHE   N    CA   sing N N 285 
PHE   N    H    sing N N 286 
PHE   N    H2   sing N N 287 
PHE   CA   C    sing N N 288 
PHE   CA   CB   sing N N 289 
PHE   CA   HA   sing N N 290 
PHE   C    O    doub N N 291 
PHE   C    OXT  sing N N 292 
PHE   CB   CG   sing N N 293 
PHE   CB   HB2  sing N N 294 
PHE   CB   HB3  sing N N 295 
PHE   CG   CD1  doub Y N 296 
PHE   CG   CD2  sing Y N 297 
PHE   CD1  CE1  sing Y N 298 
PHE   CD1  HD1  sing N N 299 
PHE   CD2  CE2  doub Y N 300 
PHE   CD2  HD2  sing N N 301 
PHE   CE1  CZ   doub Y N 302 
PHE   CE1  HE1  sing N N 303 
PHE   CE2  CZ   sing Y N 304 
PHE   CE2  HE2  sing N N 305 
PHE   CZ   HZ   sing N N 306 
PHE   OXT  HXT  sing N N 307 
PRO   N    CA   sing N N 308 
PRO   N    CD   sing N N 309 
PRO   N    H    sing N N 310 
PRO   CA   C    sing N N 311 
PRO   CA   CB   sing N N 312 
PRO   CA   HA   sing N N 313 
PRO   C    O    doub N N 314 
PRO   C    OXT  sing N N 315 
PRO   CB   CG   sing N N 316 
PRO   CB   HB2  sing N N 317 
PRO   CB   HB3  sing N N 318 
PRO   CG   CD   sing N N 319 
PRO   CG   HG2  sing N N 320 
PRO   CG   HG3  sing N N 321 
PRO   CD   HD2  sing N N 322 
PRO   CD   HD3  sing N N 323 
PRO   OXT  HXT  sing N N 324 
SER   N    CA   sing N N 325 
SER   N    H    sing N N 326 
SER   N    H2   sing N N 327 
SER   CA   C    sing N N 328 
SER   CA   CB   sing N N 329 
SER   CA   HA   sing N N 330 
SER   C    O    doub N N 331 
SER   C    OXT  sing N N 332 
SER   CB   OG   sing N N 333 
SER   CB   HB2  sing N N 334 
SER   CB   HB3  sing N N 335 
SER   OG   HG   sing N N 336 
SER   OXT  HXT  sing N N 337 
THR   N    CA   sing N N 338 
THR   N    H    sing N N 339 
THR   N    H2   sing N N 340 
THR   CA   C    sing N N 341 
THR   CA   CB   sing N N 342 
THR   CA   HA   sing N N 343 
THR   C    O    doub N N 344 
THR   C    OXT  sing N N 345 
THR   CB   OG1  sing N N 346 
THR   CB   CG2  sing N N 347 
THR   CB   HB   sing N N 348 
THR   OG1  HG1  sing N N 349 
THR   CG2  HG21 sing N N 350 
THR   CG2  HG22 sing N N 351 
THR   CG2  HG23 sing N N 352 
THR   OXT  HXT  sing N N 353 
TRP   N    CA   sing N N 354 
TRP   N    H    sing N N 355 
TRP   N    H2   sing N N 356 
TRP   CA   C    sing N N 357 
TRP   CA   CB   sing N N 358 
TRP   CA   HA   sing N N 359 
TRP   C    O    doub N N 360 
TRP   C    OXT  sing N N 361 
TRP   CB   CG   sing N N 362 
TRP   CB   HB2  sing N N 363 
TRP   CB   HB3  sing N N 364 
TRP   CG   CD1  doub Y N 365 
TRP   CG   CD2  sing Y N 366 
TRP   CD1  NE1  sing Y N 367 
TRP   CD1  HD1  sing N N 368 
TRP   CD2  CE2  doub Y N 369 
TRP   CD2  CE3  sing Y N 370 
TRP   NE1  CE2  sing Y N 371 
TRP   NE1  HE1  sing N N 372 
TRP   CE2  CZ2  sing Y N 373 
TRP   CE3  CZ3  doub Y N 374 
TRP   CE3  HE3  sing N N 375 
TRP   CZ2  CH2  doub Y N 376 
TRP   CZ2  HZ2  sing N N 377 
TRP   CZ3  CH2  sing Y N 378 
TRP   CZ3  HZ3  sing N N 379 
TRP   CH2  HH2  sing N N 380 
TRP   OXT  HXT  sing N N 381 
TYR   N    CA   sing N N 382 
TYR   N    H    sing N N 383 
TYR   N    H2   sing N N 384 
TYR   CA   C    sing N N 385 
TYR   CA   CB   sing N N 386 
TYR   CA   HA   sing N N 387 
TYR   C    O    doub N N 388 
TYR   C    OXT  sing N N 389 
TYR   CB   CG   sing N N 390 
TYR   CB   HB2  sing N N 391 
TYR   CB   HB3  sing N N 392 
TYR   CG   CD1  doub Y N 393 
TYR   CG   CD2  sing Y N 394 
TYR   CD1  CE1  sing Y N 395 
TYR   CD1  HD1  sing N N 396 
TYR   CD2  CE2  doub Y N 397 
TYR   CD2  HD2  sing N N 398 
TYR   CE1  CZ   doub Y N 399 
TYR   CE1  HE1  sing N N 400 
TYR   CE2  CZ   sing Y N 401 
TYR   CE2  HE2  sing N N 402 
TYR   CZ   OH   sing N N 403 
TYR   OH   HH   sing N N 404 
TYR   OXT  HXT  sing N N 405 
VAL   N    CA   sing N N 406 
VAL   N    H    sing N N 407 
VAL   N    H2   sing N N 408 
VAL   CA   C    sing N N 409 
VAL   CA   CB   sing N N 410 
VAL   CA   HA   sing N N 411 
VAL   C    O    doub N N 412 
VAL   C    OXT  sing N N 413 
VAL   CB   CG1  sing N N 414 
VAL   CB   CG2  sing N N 415 
VAL   CB   HB   sing N N 416 
VAL   CG1  HG11 sing N N 417 
VAL   CG1  HG12 sing N N 418 
VAL   CG1  HG13 sing N N 419 
VAL   CG2  HG21 sing N N 420 
VAL   CG2  HG22 sing N N 421 
VAL   CG2  HG23 sing N N 422 
VAL   OXT  HXT  sing N N 423 
# 
_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                    9MUL 
_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]   0.018206 
_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]   0.011110 
_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]   0.008064 
_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 
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  ? 14.835  -6.715  26.310  1.00 30.33 ? 397  ARG   A N    1 
ATOM   2    C  CA   . ARG   A 1 19  ? 14.277  -7.717  27.210  1.00 37.26 ? 397  ARG   A CA   1 
ATOM   3    C  C    . ARG   A 1 19  ? 13.058  -7.169  27.943  1.00 32.67 ? 397  ARG   A C    1 
ATOM   4    O  O    . ARG   A 1 19  ? 13.140  -6.146  28.623  1.00 31.11 ? 397  ARG   A O    1 
ATOM   5    C  CB   . ARG   A 1 19  ? 15.332  -8.186  28.212  1.00 25.55 ? 397  ARG   A CB   1 
ATOM   6    N  N    . LEU   A 1 20  ? 11.930  -7.860  27.806  1.00 27.96 ? 398  LEU   A N    1 
ATOM   7    C  CA   . LEU   A 1 20  ? 10.676  -7.389  28.376  1.00 31.88 ? 398  LEU   A CA   1 
ATOM   8    C  C    . LEU   A 1 20  ? 10.607  -7.686  29.868  1.00 30.20 ? 398  LEU   A C    1 
ATOM   9    O  O    . LEU   A 1 20  ? 10.970  -8.775  30.319  1.00 29.36 ? 398  LEU   A O    1 
ATOM   10   C  CB   . LEU   A 1 20  ? 9.488   -8.038  27.664  1.00 26.08 ? 398  LEU   A CB   1 
ATOM   11   C  CG   . LEU   A 1 20  ? 9.268   -7.660  26.199  1.00 33.32 ? 398  LEU   A CG   1 
ATOM   12   C  CD1  . LEU   A 1 20  ? 8.016   -8.329  25.653  1.00 37.31 ? 398  LEU   A CD1  1 
ATOM   13   C  CD2  . LEU   A 1 20  ? 9.185   -6.151  26.040  1.00 33.46 ? 398  LEU   A CD2  1 
ATOM   14   N  N    . LYS   A 1 21  ? 10.135  -6.705  30.632  1.00 27.59 ? 399  LYS   A N    1 
ATOM   15   C  CA   . LYS   A 1 21  ? 9.914   -6.866  32.065  1.00 24.47 ? 399  LYS   A CA   1 
ATOM   16   C  C    . LYS   A 1 21  ? 8.473   -7.314  32.278  1.00 29.19 ? 399  LYS   A C    1 
ATOM   17   O  O    . LYS   A 1 21  ? 7.534   -6.550  32.029  1.00 31.00 ? 399  LYS   A O    1 
ATOM   18   C  CB   . LYS   A 1 21  ? 10.207  -5.566  32.808  1.00 26.15 ? 399  LYS   A CB   1 
ATOM   19   C  CG   . LYS   A 1 21  ? 11.664  -5.392  33.207  1.00 33.68 ? 399  LYS   A CG   1 
ATOM   20   C  CD   . LYS   A 1 21  ? 11.909  -4.023  33.819  1.00 38.34 ? 399  LYS   A CD   1 
ATOM   21   C  CE   . LYS   A 1 21  ? 13.276  -3.482  33.432  1.00 49.78 ? 399  LYS   A CE   1 
ATOM   22   N  NZ   . LYS   A 1 21  ? 13.213  -2.634  32.209  1.00 59.13 ? 399  LYS   A NZ   1 
ATOM   23   N  N    . ILE   A 1 22  ? 8.298   -8.551  32.732  1.00 24.92 ? 400  ILE   A N    1 
ATOM   24   C  CA   . ILE   A 1 22  ? 6.982   -9.145  32.932  1.00 21.39 ? 400  ILE   A CA   1 
ATOM   25   C  C    . ILE   A 1 22  ? 6.598   -9.005  34.396  1.00 23.21 ? 400  ILE   A C    1 
ATOM   26   O  O    . ILE   A 1 22  ? 7.406   -9.290  35.289  1.00 23.42 ? 400  ILE   A O    1 
ATOM   27   C  CB   . ILE   A 1 22  ? 6.967   -10.623 32.504  1.00 27.34 ? 400  ILE   A CB   1 
ATOM   28   C  CG1  . ILE   A 1 22  ? 7.580   -10.787 31.112  1.00 25.03 ? 400  ILE   A CG1  1 
ATOM   29   C  CG2  . ILE   A 1 22  ? 5.550   -11.172 32.539  1.00 20.54 ? 400  ILE   A CG2  1 
ATOM   30   C  CD1  . ILE   A 1 22  ? 6.742   -10.192 30.005  1.00 27.46 ? 400  ILE   A CD1  1 
ATOM   31   N  N    . VAL   A 1 23  ? 5.366   -8.568  34.646  1.00 18.82 ? 401  VAL   A N    1 
ATOM   32   C  CA   . VAL   A 1 23  ? 4.795   -8.536  35.986  1.00 17.26 ? 401  VAL   A CA   1 
ATOM   33   C  C    . VAL   A 1 23  ? 3.685   -9.574  36.053  1.00 20.95 ? 401  VAL   A C    1 
ATOM   34   O  O    . VAL   A 1 23  ? 2.980   -9.816  35.064  1.00 19.88 ? 401  VAL   A O    1 
ATOM   35   C  CB   . VAL   A 1 23  ? 4.276   -7.132  36.362  1.00 21.84 ? 401  VAL   A CB   1 
ATOM   36   C  CG1  . VAL   A 1 23  ? 3.011   -6.783  35.587  1.00 20.29 ? 401  VAL   A CG1  1 
ATOM   37   C  CG2  . VAL   A 1 23  ? 4.034   -7.034  37.861  1.00 18.88 ? 401  VAL   A CG2  1 
ATOM   38   N  N    . THR   A 1 24  ? 3.553   -10.211 37.211  1.00 19.63 ? 402  THR   A N    1 
ATOM   39   C  CA   . THR   A 1 24  ? 2.509   -11.200 37.434  1.00 18.02 ? 402  THR   A CA   1 
ATOM   40   C  C    . THR   A 1 24  ? 2.165   -11.196 38.920  1.00 16.82 ? 402  THR   A C    1 
ATOM   41   O  O    . THR   A 1 24  ? 2.662   -10.365 39.686  1.00 20.18 ? 402  THR   A O    1 
ATOM   42   C  CB   . THR   A 1 24  ? 2.946   -12.584 36.933  1.00 16.85 ? 402  THR   A CB   1 
ATOM   43   O  OG1  . THR   A 1 24  ? 1.847   -13.499 37.032  1.00 20.34 ? 402  THR   A OG1  1 
ATOM   44   C  CG2  . THR   A 1 24  ? 4.112   -13.109 37.752  1.00 18.15 ? 402  THR   A CG2  1 
ATOM   45   N  N    . ILE   A 1 25  ? 1.307   -12.129 39.327  1.00 16.74 ? 403  ILE   A N    1 
ATOM   46   C  CA   . ILE   A 1 25  ? 0.783   -12.160 40.686  1.00 18.91 ? 403  ILE   A CA   1 
ATOM   47   C  C    . ILE   A 1 25  ? 0.503   -13.608 41.058  1.00 19.46 ? 403  ILE   A C    1 
ATOM   48   O  O    . ILE   A 1 25  ? 0.184   -14.437 40.201  1.00 18.75 ? 403  ILE   A O    1 
ATOM   49   C  CB   . ILE   A 1 25  ? -0.486  -11.282 40.815  1.00 17.65 ? 403  ILE   A CB   1 
ATOM   50   C  CG1  . ILE   A 1 25  ? -0.915  -11.134 42.278  1.00 16.83 ? 403  ILE   A CG1  1 
ATOM   51   C  CG2  . ILE   A 1 25  ? -1.622  -11.847 39.973  1.00 15.89 ? 403  ILE   A CG2  1 
ATOM   52   C  CD1  . ILE   A 1 25  ? -2.099  -10.206 42.470  1.00 23.16 ? 403  ILE   A CD1  1 
ATOM   53   N  N    . HIS   A 1 26  ? 0.638   -13.913 42.346  1.00 18.33 ? 404  HIS   A N    1 
ATOM   54   C  CA   . HIS   A 1 26  ? 0.340   -15.250 42.841  1.00 19.41 ? 404  HIS   A CA   1 
ATOM   55   C  C    . HIS   A 1 26  ? -1.152  -15.523 42.717  1.00 24.24 ? 404  HIS   A C    1 
ATOM   56   O  O    . HIS   A 1 26  ? -1.972  -14.811 43.308  1.00 25.27 ? 404  HIS   A O    1 
ATOM   57   C  CB   . HIS   A 1 26  ? 0.794   -15.394 44.291  1.00 20.23 ? 404  HIS   A CB   1 
ATOM   58   C  CG   . HIS   A 1 26  ? 0.488   -16.731 44.892  1.00 27.93 ? 404  HIS   A CG   1 
ATOM   59   N  ND1  . HIS   A 1 26  ? -0.120  -16.873 46.121  1.00 30.09 ? 404  HIS   A ND1  1 
ATOM   60   C  CD2  . HIS   A 1 26  ? 0.711   -17.986 44.436  1.00 26.95 ? 404  HIS   A CD2  1 
ATOM   61   C  CE1  . HIS   A 1 26  ? -0.263  -18.158 46.393  1.00 28.46 ? 404  HIS   A CE1  1 
ATOM   62   N  NE2  . HIS   A 1 26  ? 0.234   -18.855 45.388  1.00 27.73 ? 404  HIS   A NE2  1 
ATOM   63   N  N    . GLN   A 1 27  ? -1.501  -16.554 41.947  1.00 25.88 ? 405  GLN   A N    1 
ATOM   64   C  CA   . GLN   A 1 27  ? -2.910  -16.867 41.698  1.00 26.99 ? 405  GLN   A CA   1 
ATOM   65   C  C    . GLN   A 1 27  ? -2.968  -18.275 41.099  1.00 26.40 ? 405  GLN   A C    1 
ATOM   66   O  O    . GLN   A 1 27  ? -2.930  -18.442 39.879  1.00 24.44 ? 405  GLN   A O    1 
ATOM   67   C  CB   . GLN   A 1 27  ? -3.558  -15.835 40.789  1.00 21.66 ? 405  GLN   A CB   1 
ATOM   68   C  CG   . GLN   A 1 27  ? -5.082  -15.835 40.840  1.00 19.37 ? 405  GLN   A CG   1 
ATOM   69   C  CD   . GLN   A 1 27  ? -5.647  -15.050 42.010  1.00 20.91 ? 405  GLN   A CD   1 
ATOM   70   O  OE1  . GLN   A 1 27  ? -6.862  -14.935 42.154  1.00 19.25 ? 405  GLN   A OE1  1 
ATOM   71   N  NE2  . GLN   A 1 27  ? -4.770  -14.495 42.841  1.00 17.21 ? 405  GLN   A NE2  1 
ATOM   72   N  N    . GLU   A 1 28  ? -3.052  -19.271 41.975  1.00 25.15 ? 406  GLU   A N    1 
ATOM   73   C  CA   . GLU   A 1 28  ? -3.206  -20.640 41.523  1.00 25.56 ? 406  GLU   A CA   1 
ATOM   74   C  C    . GLU   A 1 28  ? -4.611  -20.845 40.958  1.00 24.43 ? 406  GLU   A C    1 
ATOM   75   O  O    . GLU   A 1 28  ? -5.577  -20.265 41.463  1.00 29.51 ? 406  GLU   A O    1 
ATOM   76   C  CB   . GLU   A 1 28  ? -2.947  -21.618 42.669  1.00 21.15 ? 406  GLU   A CB   1 
ATOM   77   C  CG   . GLU   A 1 28  ? -1.670  -21.330 43.449  1.00 24.75 ? 406  GLU   A CG   1 
ATOM   78   C  CD   . GLU   A 1 28  ? -1.387  -22.363 44.524  1.00 29.64 ? 406  GLU   A CD   1 
ATOM   79   O  OE1  . GLU   A 1 28  ? -2.198  -23.297 44.675  1.00 29.34 ? 406  GLU   A OE1  1 
ATOM   80   O  OE2  . GLU   A 1 28  ? -0.348  -22.247 45.208  1.00 35.23 ? 406  GLU   A OE2  1 
ATOM   81   N  N    . PRO   A 1 29  ? -4.763  -21.665 39.910  1.00 25.85 ? 407  PRO   A N    1 
ATOM   82   C  CA   . PRO   A 1 29  ? -3.741  -22.477 39.240  1.00 22.39 ? 407  PRO   A CA   1 
ATOM   83   C  C    . PRO   A 1 29  ? -3.033  -21.736 38.114  1.00 24.51 ? 407  PRO   A C    1 
ATOM   84   O  O    . PRO   A 1 29  ? -2.296  -22.341 37.340  1.00 22.16 ? 407  PRO   A O    1 
ATOM   85   C  CB   . PRO   A 1 29  ? -4.561  -23.654 38.712  1.00 23.19 ? 407  PRO   A CB   1 
ATOM   86   C  CG   . PRO   A 1 29  ? -5.859  -22.999 38.299  1.00 23.97 ? 407  PRO   A CG   1 
ATOM   87   C  CD   . PRO   A 1 29  ? -6.090  -21.871 39.297  1.00 26.73 ? 407  PRO   A CD   1 
ATOM   88   N  N    . PHE   A 1 30  ? -3.240  -20.425 37.991  1.00 24.74 ? 408  PHE   A N    1 
ATOM   89   C  CA   . PHE   A 1 30  ? -2.666  -19.696 36.866  1.00 21.21 ? 408  PHE   A CA   1 
ATOM   90   C  C    . PHE   A 1 30  ? -1.202  -19.348 37.106  1.00 24.02 ? 408  PHE   A C    1 
ATOM   91   O  O    . PHE   A 1 30  ? -0.388  -19.420 36.179  1.00 23.96 ? 408  PHE   A O    1 
ATOM   92   C  CB   . PHE   A 1 30  ? -3.487  -18.436 36.589  1.00 19.16 ? 408  PHE   A CB   1 
ATOM   93   C  CG   . PHE   A 1 30  ? -4.835  -18.716 35.985  1.00 18.26 ? 408  PHE   A CG   1 
ATOM   94   C  CD1  . PHE   A 1 30  ? -4.976  -18.887 34.617  1.00 17.06 ? 408  PHE   A CD1  1 
ATOM   95   C  CD2  . PHE   A 1 30  ? -5.958  -18.824 36.787  1.00 18.16 ? 408  PHE   A CD2  1 
ATOM   96   C  CE1  . PHE   A 1 30  ? -6.214  -19.151 34.060  1.00 20.37 ? 408  PHE   A CE1  1 
ATOM   97   C  CE2  . PHE   A 1 30  ? -7.199  -19.087 36.236  1.00 17.35 ? 408  PHE   A CE2  1 
ATOM   98   C  CZ   . PHE   A 1 30  ? -7.327  -19.252 34.872  1.00 17.29 ? 408  PHE   A CZ   1 
ATOM   99   N  N    . VAL   A 1 31  ? -0.846  -18.967 38.332  1.00 21.79 ? 409  VAL   A N    1 
ATOM   100  C  CA   . VAL   A 1 31  ? 0.530   -18.618 38.675  1.00 21.39 ? 409  VAL   A CA   1 
ATOM   101  C  C    . VAL   A 1 31  ? 0.839   -19.206 40.046  1.00 26.25 ? 409  VAL   A C    1 
ATOM   102  O  O    . VAL   A 1 31  ? 0.326   -18.722 41.061  1.00 22.78 ? 409  VAL   A O    1 
ATOM   103  C  CB   . VAL   A 1 31  ? 0.774   -17.101 38.680  1.00 23.78 ? 409  VAL   A CB   1 
ATOM   104  C  CG1  . VAL   A 1 31  ? 2.199   -16.797 39.113  1.00 24.95 ? 409  VAL   A CG1  1 
ATOM   105  C  CG2  . VAL   A 1 31  ? 0.497   -16.499 37.310  1.00 17.23 ? 409  VAL   A CG2  1 
ATOM   106  N  N    . TYR   A 1 32  ? 1.669   -20.244 40.079  1.00 22.22 ? 410  TYR   A N    1 
ATOM   107  C  CA   . TYR   A 1 32  ? 2.178   -20.785 41.329  1.00 21.37 ? 410  TYR   A CA   1 
ATOM   108  C  C    . TYR   A 1 32  ? 3.452   -20.052 41.727  1.00 28.05 ? 410  TYR   A C    1 
ATOM   109  O  O    . TYR   A 1 32  ? 4.203   -19.566 40.877  1.00 26.06 ? 410  TYR   A O    1 
ATOM   110  C  CB   . TYR   A 1 32  ? 2.462   -22.283 41.208  1.00 22.05 ? 410  TYR   A CB   1 
ATOM   111  C  CG   . TYR   A 1 32  ? 1.231   -23.162 41.134  1.00 25.59 ? 410  TYR   A CG   1 
ATOM   112  C  CD1  . TYR   A 1 32  ? 0.510   -23.286 39.954  1.00 21.83 ? 410  TYR   A CD1  1 
ATOM   113  C  CD2  . TYR   A 1 32  ? 0.799   -23.879 42.243  1.00 23.11 ? 410  TYR   A CD2  1 
ATOM   114  C  CE1  . TYR   A 1 32  ? -0.611  -24.091 39.882  1.00 22.21 ? 410  TYR   A CE1  1 
ATOM   115  C  CE2  . TYR   A 1 32  ? -0.321  -24.687 42.180  1.00 25.44 ? 410  TYR   A CE2  1 
ATOM   116  C  CZ   . TYR   A 1 32  ? -1.022  -24.789 40.998  1.00 26.39 ? 410  TYR   A CZ   1 
ATOM   117  O  OH   . TYR   A 1 32  ? -2.137  -25.593 40.930  1.00 27.86 ? 410  TYR   A OH   1 
ATOM   118  N  N    . VAL   A 1 33  ? 3.689   -19.974 43.034  1.00 28.73 ? 411  VAL   A N    1 
ATOM   119  C  CA   . VAL   A 1 33  ? 4.856   -19.287 43.579  1.00 28.10 ? 411  VAL   A CA   1 
ATOM   120  C  C    . VAL   A 1 33  ? 5.424   -20.154 44.695  1.00 26.83 ? 411  VAL   A C    1 
ATOM   121  O  O    . VAL   A 1 33  ? 4.763   -20.363 45.719  1.00 27.77 ? 411  VAL   A O    1 
ATOM   122  C  CB   . VAL   A 1 33  ? 4.522   -17.882 44.101  1.00 29.68 ? 411  VAL   A CB   1 
ATOM   123  C  CG1  . VAL   A 1 33  ? 5.665   -17.347 44.944  1.00 22.46 ? 411  VAL   A CG1  1 
ATOM   124  C  CG2  . VAL   A 1 33  ? 4.227   -16.940 42.942  1.00 20.65 ? 411  VAL   A CG2  1 
ATOM   125  N  N    . LYS   A 1 34  ? 6.638   -20.658 44.501  1.00 25.09 ? 412  LYS   A N    1 
ATOM   126  C  CA   . LYS   A 1 34  ? 7.319   -21.498 45.470  1.00 25.41 ? 412  LYS   A CA   1 
ATOM   127  C  C    . LYS   A 1 34  ? 8.734   -20.987 45.691  1.00 31.80 ? 412  LYS   A C    1 
ATOM   128  O  O    . LYS   A 1 34  ? 9.329   -20.385 44.790  1.00 28.89 ? 412  LYS   A O    1 
ATOM   129  C  CB   . LYS   A 1 34  ? 7.374   -22.961 45.002  1.00 29.73 ? 412  LYS   A CB   1 
ATOM   130  C  CG   . LYS   A 1 34  ? 6.016   -23.608 44.787  1.00 30.78 ? 412  LYS   A CG   1 
ATOM   131  C  CD   . LYS   A 1 34  ? 5.188   -23.610 46.061  1.00 26.03 ? 412  LYS   A CD   1 
ATOM   132  C  CE   . LYS   A 1 34  ? 3.883   -24.362 45.859  1.00 34.81 ? 412  LYS   A CE   1 
ATOM   133  N  NZ   . LYS   A 1 34  ? 2.968   -24.223 47.024  1.00 38.13 ? 412  LYS   A NZ   1 
ATOM   134  N  N    . PRO   A 1 35  ? 9.292   -21.199 46.880  1.00 32.53 ? 413  PRO   A N    1 
ATOM   135  C  CA   . PRO   A 1 35  ? 10.684  -20.803 47.115  1.00 35.78 ? 413  PRO   A CA   1 
ATOM   136  C  C    . PRO   A 1 35  ? 11.644  -21.642 46.288  1.00 31.82 ? 413  PRO   A C    1 
ATOM   137  O  O    . PRO   A 1 35  ? 11.345  -22.774 45.900  1.00 28.65 ? 413  PRO   A O    1 
ATOM   138  C  CB   . PRO   A 1 35  ? 10.881  -21.053 48.616  1.00 30.44 ? 413  PRO   A CB   1 
ATOM   139  C  CG   . PRO   A 1 35  ? 9.498   -21.119 49.187  1.00 35.22 ? 413  PRO   A CG   1 
ATOM   140  C  CD   . PRO   A 1 35  ? 8.647   -21.701 48.104  1.00 27.73 ? 413  PRO   A CD   1 
ATOM   141  N  N    . THR   A 1 36  ? 12.810  -21.064 46.012  1.00 32.14 ? 414  THR   A N    1 
ATOM   142  C  CA   . THR   A 1 36  ? 13.841  -21.781 45.283  1.00 31.63 ? 414  THR   A CA   1 
ATOM   143  C  C    . THR   A 1 36  ? 14.504  -22.818 46.187  1.00 32.31 ? 414  THR   A C    1 
ATOM   144  O  O    . THR   A 1 36  ? 14.292  -22.856 47.402  1.00 36.13 ? 414  THR   A O    1 
ATOM   145  C  CB   . THR   A 1 36  ? 14.896  -20.816 44.742  1.00 35.35 ? 414  THR   A CB   1 
ATOM   146  O  OG1  . THR   A 1 36  ? 15.634  -20.251 45.833  1.00 36.11 ? 414  THR   A OG1  1 
ATOM   147  C  CG2  . THR   A 1 36  ? 14.242  -19.696 43.954  1.00 36.80 ? 414  THR   A CG2  1 
ATOM   148  N  N    . LEU   A 1 37  ? 15.319  -23.672 45.574  1.00 31.75 ? 415  LEU   A N    1 
ATOM   149  C  CA   . LEU   A 1 37  ? 16.133  -24.600 46.340  1.00 40.99 ? 415  LEU   A CA   1 
ATOM   150  C  C    . LEU   A 1 37  ? 17.338  -23.863 46.922  1.00 41.31 ? 415  LEU   A C    1 
ATOM   151  O  O    . LEU   A 1 37  ? 17.546  -22.670 46.681  1.00 42.90 ? 415  LEU   A O    1 
ATOM   152  C  CB   . LEU   A 1 37  ? 16.560  -25.778 45.468  1.00 34.41 ? 415  LEU   A CB   1 
ATOM   153  C  CG   . LEU   A 1 37  ? 15.420  -26.652 44.937  1.00 39.33 ? 415  LEU   A CG   1 
ATOM   154  C  CD1  . LEU   A 1 37  ? 15.957  -27.785 44.075  1.00 38.10 ? 415  LEU   A CD1  1 
ATOM   155  C  CD2  . LEU   A 1 37  ? 14.580  -27.193 46.084  1.00 35.11 ? 415  LEU   A CD2  1 
ATOM   156  N  N    . SER   A 1 38  ? 18.145  -24.585 47.704  1.00 45.31 ? 416  SER   A N    1 
ATOM   157  C  CA   . SER   A 1 38  ? 19.295  -23.962 48.354  1.00 50.00 ? 416  SER   A CA   1 
ATOM   158  C  C    . SER   A 1 38  ? 20.262  -23.377 47.331  1.00 45.11 ? 416  SER   A C    1 
ATOM   159  O  O    . SER   A 1 38  ? 20.880  -22.334 47.576  1.00 44.07 ? 416  SER   A O    1 
ATOM   160  C  CB   . SER   A 1 38  ? 20.008  -24.977 49.246  1.00 50.85 ? 416  SER   A CB   1 
ATOM   161  N  N    . ASP   A 1 39  ? 20.395  -24.026 46.175  1.00 44.18 ? 417  ASP   A N    1 
ATOM   162  C  CA   . ASP   A 1 39  ? 21.289  -23.573 45.120  1.00 45.20 ? 417  ASP   A CA   1 
ATOM   163  C  C    . ASP   A 1 39  ? 20.640  -22.549 44.194  1.00 44.61 ? 417  ASP   A C    1 
ATOM   164  O  O    . ASP   A 1 39  ? 21.165  -22.290 43.105  1.00 47.42 ? 417  ASP   A O    1 
ATOM   165  C  CB   . ASP   A 1 39  ? 21.794  -24.770 44.311  1.00 44.71 ? 417  ASP   A CB   1 
ATOM   166  C  CG   . ASP   A 1 39  ? 20.673  -25.520 43.619  1.00 52.26 ? 417  ASP   A CG   1 
ATOM   167  O  OD1  . ASP   A 1 39  ? 19.503  -25.352 44.024  1.00 51.89 ? 417  ASP   A OD1  1 
ATOM   168  O  OD2  . ASP   A 1 39  ? 20.961  -26.284 42.674  1.00 56.60 ? 417  ASP   A OD2  1 
ATOM   169  N  N    . GLY   A 1 40  ? 19.515  -21.964 44.599  1.00 44.46 ? 418  GLY   A N    1 
ATOM   170  C  CA   . GLY   A 1 40  ? 18.868  -20.947 43.795  1.00 38.88 ? 418  GLY   A CA   1 
ATOM   171  C  C    . GLY   A 1 40  ? 18.123  -21.458 42.585  1.00 42.96 ? 418  GLY   A C    1 
ATOM   172  O  O    . GLY   A 1 40  ? 17.808  -20.669 41.689  1.00 38.39 ? 418  GLY   A O    1 
ATOM   173  N  N    . THR   A 1 41  ? 17.832  -22.753 42.524  1.00 39.30 ? 419  THR   A N    1 
ATOM   174  C  CA   . THR   A 1 41  ? 17.099  -23.344 41.416  1.00 40.20 ? 419  THR   A CA   1 
ATOM   175  C  C    . THR   A 1 41  ? 15.728  -23.815 41.884  1.00 37.95 ? 419  THR   A C    1 
ATOM   176  O  O    . THR   A 1 41  ? 15.404  -23.796 43.074  1.00 37.92 ? 419  THR   A O    1 
ATOM   177  C  CB   . THR   A 1 41  ? 17.880  -24.511 40.798  1.00 40.73 ? 419  THR   A CB   1 
ATOM   178  O  OG1  . THR   A 1 41  ? 17.745  -25.674 41.625  1.00 42.77 ? 419  THR   A OG1  1 
ATOM   179  C  CG2  . THR   A 1 41  ? 19.351  -24.155 40.660  1.00 47.61 ? 419  THR   A CG2  1 
ATOM   180  N  N    . CYS   A 1 42  ? 14.919  -24.243 40.919  1.00 37.20 ? 420  CYS   A N    1 
ATOM   181  C  CA   . CYS   A 1 42  ? 13.570  -24.726 41.169  1.00 34.85 ? 420  CYS   A CA   1 
ATOM   182  C  C    . CYS   A 1 42  ? 13.529  -26.243 41.043  1.00 38.84 ? 420  CYS   A C    1 
ATOM   183  O  O    . CYS   A 1 42  ? 14.205  -26.822 40.186  1.00 37.22 ? 420  CYS   A O    1 
ATOM   184  C  CB   . CYS   A 1 42  ? 12.577  -24.087 40.197  1.00 27.65 ? 420  CYS   A CB   1 
ATOM   185  S  SG   . CYS   A 1 42  ? 12.659  -22.287 40.180  1.00 30.74 ? 420  CYS   A SG   1 
ATOM   186  N  N    . LYS   A 1 43  ? 12.731  -26.878 41.900  1.00 33.79 ? 421  LYS   A N    1 
ATOM   187  C  CA   . LYS   A 1 43  ? 12.668  -28.334 41.932  1.00 41.33 ? 421  LYS   A CA   1 
ATOM   188  C  C    . LYS   A 1 43  ? 12.071  -28.872 40.636  1.00 39.66 ? 421  LYS   A C    1 
ATOM   189  O  O    . LYS   A 1 43  ? 11.053  -28.371 40.149  1.00 39.63 ? 421  LYS   A O    1 
ATOM   190  C  CB   . LYS   A 1 43  ? 11.844  -28.807 43.132  1.00 41.34 ? 421  LYS   A CB   1 
ATOM   191  C  CG   . LYS   A 1 43  ? 11.834  -30.324 43.352  1.00 40.17 ? 421  LYS   A CG   1 
ATOM   192  C  CD   . LYS   A 1 43  ? 13.164  -30.972 42.979  1.00 51.23 ? 421  LYS   A CD   1 
ATOM   193  C  CE   . LYS   A 1 43  ? 12.987  -32.443 42.635  1.00 48.43 ? 421  LYS   A CE   1 
ATOM   194  N  NZ   . LYS   A 1 43  ? 14.276  -33.106 42.292  1.00 48.54 ? 421  LYS   A NZ   1 
ATOM   195  N  N    . GLU   A 1 44  ? 12.726  -29.885 40.075  1.00 45.19 ? 422  GLU   A N    1 
ATOM   196  C  CA   . GLU   A 1 44  ? 12.208  -30.590 38.912  1.00 45.42 ? 422  GLU   A CA   1 
ATOM   197  C  C    . GLU   A 1 44  ? 10.907  -31.300 39.263  1.00 43.43 ? 422  GLU   A C    1 
ATOM   198  O  O    . GLU   A 1 44  ? 10.889  -32.200 40.108  1.00 49.49 ? 422  GLU   A O    1 
ATOM   199  C  CB   . GLU   A 1 44  ? 13.255  -31.590 38.423  1.00 45.48 ? 422  GLU   A CB   1 
ATOM   200  C  CG   . GLU   A 1 44  ? 12.845  -32.430 37.230  1.00 57.84 ? 422  GLU   A CG   1 
ATOM   201  C  CD   . GLU   A 1 44  ? 13.906  -33.451 36.865  1.00 75.45 ? 422  GLU   A CD   1 
ATOM   202  O  OE1  . GLU   A 1 44  ? 14.975  -33.448 37.511  1.00 72.11 ? 422  GLU   A OE1  1 
ATOM   203  O  OE2  . GLU   A 1 44  ? 13.676  -34.253 35.936  1.00 77.39 ? 422  GLU   A OE2  1 
ATOM   204  N  N    . GLU   A 1 45  ? 9.816   -30.891 38.619  1.00 37.94 ? 423  GLU   A N    1 
ATOM   205  C  CA   . GLU   A 1 45  ? 8.505   -31.487 38.831  1.00 38.71 ? 423  GLU   A CA   1 
ATOM   206  C  C    . GLU   A 1 45  ? 7.885   -31.824 37.481  1.00 36.48 ? 423  GLU   A C    1 
ATOM   207  O  O    . GLU   A 1 45  ? 8.366   -31.401 36.427  1.00 36.31 ? 423  GLU   A O    1 
ATOM   208  C  CB   . GLU   A 1 45  ? 7.589   -30.555 39.635  1.00 41.23 ? 423  GLU   A CB   1 
ATOM   209  C  CG   . GLU   A 1 45  ? 7.909   -30.511 41.122  1.00 44.45 ? 423  GLU   A CG   1 
ATOM   210  C  CD   . GLU   A 1 45  ? 6.869   -29.753 41.923  1.00 49.14 ? 423  GLU   A CD   1 
ATOM   211  O  OE1  . GLU   A 1 45  ? 6.647   -28.558 41.634  1.00 48.98 ? 423  GLU   A OE1  1 
ATOM   212  O  OE2  . GLU   A 1 45  ? 6.273   -30.353 42.841  1.00 53.38 ? 423  GLU   A OE2  1 
ATOM   213  N  N    . PHE   A 1 46  ? 6.802   -32.597 37.518  1.00 36.28 ? 424  PHE   A N    1 
ATOM   214  C  CA   . PHE   A 1 46  ? 6.195   -33.129 36.307  1.00 37.22 ? 424  PHE   A CA   1 
ATOM   215  C  C    . PHE   A 1 46  ? 4.688   -32.926 36.335  1.00 44.03 ? 424  PHE   A C    1 
ATOM   216  O  O    . PHE   A 1 46  ? 4.057   -33.020 37.392  1.00 45.74 ? 424  PHE   A O    1 
ATOM   217  C  CB   . PHE   A 1 46  ? 6.534   -34.615 36.136  1.00 33.63 ? 424  PHE   A CB   1 
ATOM   218  C  CG   . PHE   A 1 46  ? 8.004   -34.878 35.978  1.00 38.07 ? 424  PHE   A CG   1 
ATOM   219  C  CD1  . PHE   A 1 46  ? 8.812   -35.073 37.087  1.00 41.26 ? 424  PHE   A CD1  1 
ATOM   220  C  CD2  . PHE   A 1 46  ? 8.583   -34.912 34.720  1.00 43.85 ? 424  PHE   A CD2  1 
ATOM   221  C  CE1  . PHE   A 1 46  ? 10.167  -35.305 36.943  1.00 43.90 ? 424  PHE   A CE1  1 
ATOM   222  C  CE2  . PHE   A 1 46  ? 9.939   -35.145 34.570  1.00 45.88 ? 424  PHE   A CE2  1 
ATOM   223  C  CZ   . PHE   A 1 46  ? 10.731  -35.343 35.683  1.00 44.55 ? 424  PHE   A CZ   1 
ATOM   224  N  N    . THR   A 1 47  ? 4.119   -32.652 35.161  1.00 44.33 ? 425  THR   A N    1 
ATOM   225  C  CA   . THR   A 1 47  ? 2.701   -32.344 35.041  1.00 52.32 ? 425  THR   A CA   1 
ATOM   226  C  C    . THR   A 1 47  ? 1.853   -33.594 35.272  1.00 51.24 ? 425  THR   A C    1 
ATOM   227  O  O    . THR   A 1 47  ? 2.352   -34.680 35.581  1.00 40.68 ? 425  THR   A O    1 
ATOM   228  C  CB   . THR   A 1 47  ? 2.395   -31.747 33.667  1.00 50.78 ? 425  THR   A CB   1 
ATOM   229  O  OG1  . THR   A 1 47  ? 2.310   -32.797 32.694  1.00 42.02 ? 425  THR   A OG1  1 
ATOM   230  C  CG2  . THR   A 1 47  ? 3.470   -30.753 33.251  1.00 49.79 ? 425  THR   A CG2  1 
ATOM   231  N  N    . VAL   A 1 48  ? 0.539   -33.424 35.109  1.00 57.81 ? 426  VAL   A N    1 
ATOM   232  C  CA   . VAL   A 1 48  ? -0.390  -34.537 35.253  1.00 58.14 ? 426  VAL   A CA   1 
ATOM   233  C  C    . VAL   A 1 48  ? -0.223  -35.559 34.138  1.00 54.09 ? 426  VAL   A C    1 
ATOM   234  O  O    . VAL   A 1 48  ? -0.614  -36.721 34.304  1.00 55.32 ? 426  VAL   A O    1 
ATOM   235  C  CB   . VAL   A 1 48  ? -1.840  -34.018 35.295  1.00 59.47 ? 426  VAL   A CB   1 
ATOM   236  C  CG1  . VAL   A 1 48  ? -2.036  -33.090 36.483  1.00 64.13 ? 426  VAL   A CG1  1 
ATOM   237  C  CG2  . VAL   A 1 48  ? -2.188  -33.306 33.996  1.00 56.16 ? 426  VAL   A CG2  1 
ATOM   238  N  N    . ASN   A 1 49  ? 0.350   -35.160 33.004  1.00 49.50 ? 427  ASN   A N    1 
ATOM   239  C  CA   . ASN   A 1 49  ? 0.552   -36.048 31.868  1.00 45.84 ? 427  ASN   A CA   1 
ATOM   240  C  C    . ASN   A 1 49  ? 1.988   -36.545 31.758  1.00 46.65 ? 427  ASN   A C    1 
ATOM   241  O  O    . ASN   A 1 49  ? 2.374   -37.065 30.707  1.00 43.94 ? 427  ASN   A O    1 
ATOM   242  C  CB   . ASN   A 1 49  ? 0.140   -35.344 30.572  1.00 51.04 ? 427  ASN   A CB   1 
ATOM   243  C  CG   . ASN   A 1 49  ? -1.142  -34.544 30.726  1.00 67.82 ? 427  ASN   A CG   1 
ATOM   244  O  OD1  . ASN   A 1 49  ? -2.180  -35.079 31.113  1.00 64.60 ? 427  ASN   A OD1  1 
ATOM   245  N  ND2  . ASN   A 1 49  ? -1.073  -33.252 30.421  1.00 56.98 ? 427  ASN   A ND2  1 
ATOM   246  N  N    . GLY   A 1 50  ? 2.787   -36.393 32.813  1.00 45.47 ? 428  GLY   A N    1 
ATOM   247  C  CA   . GLY   A 1 50  ? 4.146   -36.891 32.827  1.00 43.49 ? 428  GLY   A CA   1 
ATOM   248  C  C    . GLY   A 1 50  ? 5.187   -35.969 32.232  1.00 35.46 ? 428  GLY   A C    1 
ATOM   249  O  O    . GLY   A 1 50  ? 6.379   -36.299 32.279  1.00 38.45 ? 428  GLY   A O    1 
ATOM   250  N  N    . ASP   A 1 51  ? 4.786   -34.830 31.680  1.00 39.87 ? 429  ASP   A N    1 
ATOM   251  C  CA   . ASP   A 1 51  ? 5.734   -33.912 31.070  1.00 39.57 ? 429  ASP   A CA   1 
ATOM   252  C  C    . ASP   A 1 51  ? 6.402   -33.041 32.133  1.00 39.24 ? 429  ASP   A C    1 
ATOM   253  O  O    . ASP   A 1 51  ? 5.841   -32.826 33.209  1.00 41.59 ? 429  ASP   A O    1 
ATOM   254  C  CB   . ASP   A 1 51  ? 5.027   -33.029 30.046  1.00 40.44 ? 429  ASP   A CB   1 
ATOM   255  C  CG   . ASP   A 1 51  ? 4.499   -33.817 28.867  1.00 34.18 ? 429  ASP   A CG   1 
ATOM   256  O  OD1  . ASP   A 1 51  ? 5.254   -34.646 28.318  1.00 31.31 ? 429  ASP   A OD1  1 
ATOM   257  O  OD2  . ASP   A 1 51  ? 3.327   -33.612 28.492  1.00 36.97 ? 429  ASP   A OD2  1 
ATOM   258  N  N    . PRO   A 1 52  ? 7.604   -32.533 31.861  1.00 36.51 ? 430  PRO   A N    1 
ATOM   259  C  CA   . PRO   A 1 52  ? 8.259   -31.648 32.833  1.00 36.69 ? 430  PRO   A CA   1 
ATOM   260  C  C    . PRO   A 1 52  ? 7.524   -30.323 32.961  1.00 34.18 ? 430  PRO   A C    1 
ATOM   261  O  O    . PRO   A 1 52  ? 7.051   -29.755 31.974  1.00 35.86 ? 430  PRO   A O    1 
ATOM   262  C  CB   . PRO   A 1 52  ? 9.665   -31.455 32.251  1.00 34.20 ? 430  PRO   A CB   1 
ATOM   263  C  CG   . PRO   A 1 52  ? 9.513   -31.744 30.794  1.00 34.93 ? 430  PRO   A CG   1 
ATOM   264  C  CD   . PRO   A 1 52  ? 8.467   -32.811 30.700  1.00 35.82 ? 430  PRO   A CD   1 
ATOM   265  N  N    . VAL   A 1 53  ? 7.428   -29.837 34.195  1.00 31.11 ? 431  VAL   A N    1 
ATOM   266  C  CA   . VAL   A 1 53  ? 6.801   -28.547 34.466  1.00 29.49 ? 431  VAL   A CA   1 
ATOM   267  C  C    . VAL   A 1 53  ? 7.813   -27.445 34.182  1.00 32.42 ? 431  VAL   A C    1 
ATOM   268  O  O    . VAL   A 1 53  ? 8.856   -27.360 34.839  1.00 27.50 ? 431  VAL   A O    1 
ATOM   269  C  CB   . VAL   A 1 53  ? 6.294   -28.467 35.912  1.00 30.33 ? 431  VAL   A CB   1 
ATOM   270  C  CG1  . VAL   A 1 53  ? 5.780   -27.069 36.214  1.00 27.20 ? 431  VAL   A CG1  1 
ATOM   271  C  CG2  . VAL   A 1 53  ? 5.207   -29.497 36.154  1.00 30.66 ? 431  VAL   A CG2  1 
ATOM   272  N  N    . LYS   A 1 54  ? 7.508   -26.601 33.201  1.00 26.04 ? 432  LYS   A N    1 
ATOM   273  C  CA   . LYS   A 1 54  ? 8.377   -25.475 32.891  1.00 24.52 ? 432  LYS   A CA   1 
ATOM   274  C  C    . LYS   A 1 54  ? 8.277   -24.424 33.988  1.00 27.19 ? 432  LYS   A C    1 
ATOM   275  O  O    . LYS   A 1 54  ? 7.183   -23.955 34.317  1.00 26.70 ? 432  LYS   A O    1 
ATOM   276  C  CB   . LYS   A 1 54  ? 8.003   -24.873 31.538  1.00 26.38 ? 432  LYS   A CB   1 
ATOM   277  C  CG   . LYS   A 1 54  ? 8.061   -25.855 30.384  1.00 27.08 ? 432  LYS   A CG   1 
ATOM   278  C  CD   . LYS   A 1 54  ? 6.935   -25.608 29.395  1.00 30.68 ? 432  LYS   A CD   1 
ATOM   279  C  CE   . LYS   A 1 54  ? 7.466   -25.057 28.082  1.00 40.64 ? 432  LYS   A CE   1 
ATOM   280  N  NZ   . LYS   A 1 54  ? 6.886   -25.762 26.907  1.00 51.11 ? 432  LYS   A NZ   1 
ATOM   281  N  N    . LYS   A 1 55  ? 9.421   -24.058 34.559  1.00 24.10 ? 433  LYS   A N    1 
ATOM   282  C  CA   . LYS   A 1 55  ? 9.487   -23.072 35.625  1.00 23.82 ? 433  LYS   A CA   1 
ATOM   283  C  C    . LYS   A 1 55  ? 10.454  -21.961 35.243  1.00 24.01 ? 433  LYS   A C    1 
ATOM   284  O  O    . LYS   A 1 55  ? 11.427  -22.184 34.515  1.00 25.07 ? 433  LYS   A O    1 
ATOM   285  C  CB   . LYS   A 1 55  ? 9.926   -23.712 36.949  1.00 27.16 ? 433  LYS   A CB   1 
ATOM   286  C  CG   . LYS   A 1 55  ? 9.024   -24.841 37.420  1.00 29.22 ? 433  LYS   A CG   1 
ATOM   287  C  CD   . LYS   A 1 55  ? 9.464   -25.376 38.772  1.00 25.43 ? 433  LYS   A CD   1 
ATOM   288  C  CE   . LYS   A 1 55  ? 8.506   -26.441 39.280  1.00 27.44 ? 433  LYS   A CE   1 
ATOM   289  N  NZ   . LYS   A 1 55  ? 8.898   -26.951 40.623  1.00 37.53 ? 433  LYS   A NZ   1 
ATOM   290  N  N    . VAL   A 1 56  ? 10.170  -20.756 35.731  1.00 23.10 ? 434  VAL   A N    1 
ATOM   291  C  CA   . VAL   A 1 56  ? 11.036  -19.604 35.525  1.00 26.28 ? 434  VAL   A CA   1 
ATOM   292  C  C    . VAL   A 1 56  ? 11.334  -18.973 36.877  1.00 31.73 ? 434  VAL   A C    1 
ATOM   293  O  O    . VAL   A 1 56  ? 10.557  -19.096 37.829  1.00 32.15 ? 434  VAL   A O    1 
ATOM   294  C  CB   . VAL   A 1 56  ? 10.415  -18.563 34.562  1.00 26.16 ? 434  VAL   A CB   1 
ATOM   295  C  CG1  . VAL   A 1 56  ? 9.895   -19.237 33.301  1.00 22.41 ? 434  VAL   A CG1  1 
ATOM   296  C  CG2  . VAL   A 1 56  ? 9.304   -17.785 35.251  1.00 26.28 ? 434  VAL   A CG2  1 
ATOM   297  N  N    . ILE   A 1 57  ? 12.480  -18.307 36.960  1.00 26.22 ? 435  ILE   A N    1 
ATOM   298  C  CA   . ILE   A 1 57  ? 12.846  -17.567 38.161  1.00 27.61 ? 435  ILE   A CA   1 
ATOM   299  C  C    . ILE   A 1 57  ? 12.101  -16.240 38.160  1.00 28.71 ? 435  ILE   A C    1 
ATOM   300  O  O    . ILE   A 1 57  ? 12.157  -15.483 37.183  1.00 33.56 ? 435  ILE   A O    1 
ATOM   301  C  CB   . ILE   A 1 57  ? 14.366  -17.352 38.229  1.00 31.28 ? 435  ILE   A CB   1 
ATOM   302  C  CG1  . ILE   A 1 57  ? 15.086  -18.672 38.521  1.00 34.95 ? 435  ILE   A CG1  1 
ATOM   303  C  CG2  . ILE   A 1 57  ? 14.711  -16.308 39.279  1.00 24.41 ? 435  ILE   A CG2  1 
ATOM   304  C  CD1  . ILE   A 1 57  ? 14.815  -19.230 39.904  1.00 32.58 ? 435  ILE   A CD1  1 
ATOM   305  N  N    . CYS   A 1 58  ? 11.388  -15.959 39.248  1.00 30.30 ? 436  CYS   A N    1 
ATOM   306  C  CA   . CYS   A 1 58  ? 10.656  -14.710 39.397  1.00 27.03 ? 436  CYS   A CA   1 
ATOM   307  C  C    . CYS   A 1 58  ? 11.013  -14.082 40.734  1.00 32.82 ? 436  CYS   A C    1 
ATOM   308  O  O    . CYS   A 1 58  ? 11.020  -14.765 41.763  1.00 30.87 ? 436  CYS   A O    1 
ATOM   309  C  CB   . CYS   A 1 58  ? 9.143   -14.932 39.292  1.00 25.77 ? 436  CYS   A CB   1 
ATOM   310  S  SG   . CYS   A 1 58  ? 8.464   -16.155 40.436  1.00 33.40 ? 436  CYS   A SG   1 
ATOM   311  N  N    . THR   A 1 59  ? 11.315  -12.789 40.714  1.00 32.33 ? 437  THR   A N    1 
ATOM   312  C  CA   . THR   A 1 59  ? 11.677  -12.058 41.918  1.00 30.73 ? 437  THR   A CA   1 
ATOM   313  C  C    . THR   A 1 59  ? 10.448  -11.390 42.522  1.00 33.89 ? 437  THR   A C    1 
ATOM   314  O  O    . THR   A 1 59  ? 9.478   -11.081 41.827  1.00 29.78 ? 437  THR   A O    1 
ATOM   315  C  CB   . THR   A 1 59  ? 12.743  -11.004 41.612  1.00 26.17 ? 437  THR   A CB   1 
ATOM   316  O  OG1  . THR   A 1 59  ? 12.266  -10.122 40.589  1.00 25.88 ? 437  THR   A OG1  1 
ATOM   317  C  CG2  . THR   A 1 59  ? 14.027  -11.666 41.141  1.00 28.36 ? 437  THR   A CG2  1 
ATOM   318  N  N    . GLY   A 1 60  ? 10.495  -11.172 43.832  1.00 38.38 ? 438  GLY   A N    1 
ATOM   319  C  CA   . GLY   A 1 60  ? 9.399   -10.545 44.527  1.00 31.23 ? 438  GLY   A CA   1 
ATOM   320  C  C    . GLY   A 1 60  ? 9.598   -10.529 46.027  1.00 35.48 ? 438  GLY   A C    1 
ATOM   321  O  O    . GLY   A 1 60  ? 10.492  -11.187 46.567  1.00 37.70 ? 438  GLY   A O    1 
ATOM   322  N  N    . PRO   A 1 61  ? 8.766   -9.767  46.730  1.00 40.53 ? 439  PRO   A N    1 
ATOM   323  C  CA   . PRO   A 1 61  ? 8.876   -9.709  48.190  1.00 45.22 ? 439  PRO   A CA   1 
ATOM   324  C  C    . PRO   A 1 61  ? 8.334   -10.972 48.840  1.00 48.61 ? 439  PRO   A C    1 
ATOM   325  O  O    . PRO   A 1 61  ? 7.596   -11.754 48.237  1.00 50.16 ? 439  PRO   A O    1 
ATOM   326  C  CB   . PRO   A 1 61  ? 8.029   -8.487  48.560  1.00 40.30 ? 439  PRO   A CB   1 
ATOM   327  C  CG   . PRO   A 1 61  ? 7.028   -8.388  47.457  1.00 34.85 ? 439  PRO   A CG   1 
ATOM   328  C  CD   . PRO   A 1 61  ? 7.724   -8.863  46.211  1.00 32.53 ? 439  PRO   A CD   1 
ATOM   329  N  N    . ASN   A 1 62  ? 8.720   -11.164 50.098  1.00 57.97 ? 440  ASN   A N    1 
ATOM   330  C  CA   . ASN   A 1 62  ? 8.229   -12.291 50.883  1.00 58.88 ? 440  ASN   A CA   1 
ATOM   331  C  C    . ASN   A 1 62  ? 6.968   -11.903 51.647  1.00 69.09 ? 440  ASN   A C    1 
ATOM   332  O  O    . ASN   A 1 62  ? 6.989   -10.995 52.479  1.00 76.70 ? 440  ASN   A O    1 
ATOM   333  C  CB   . ASN   A 1 62  ? 9.300   -12.785 51.857  1.00 60.11 ? 440  ASN   A CB   1 
ATOM   334  C  CG   . ASN   A 1 62  ? 10.365  -13.624 51.179  1.00 67.96 ? 440  ASN   A CG   1 
ATOM   335  O  OD1  . ASN   A 1 62  ? 11.559  -13.429 51.402  1.00 68.52 ? 440  ASN   A OD1  1 
ATOM   336  N  ND2  . ASN   A 1 62  ? 9.936   -14.562 50.342  1.00 63.49 ? 440  ASN   A ND2  1 
ATOM   337  N  N    . SER   A 1 68  ? 5.024   -2.149  55.290  1.00 33.80 ? 446  SER   A N    1 
ATOM   338  C  CA   . SER   A 1 68  ? 6.103   -3.121  55.425  1.00 38.29 ? 446  SER   A CA   1 
ATOM   339  C  C    . SER   A 1 68  ? 7.114   -2.991  54.289  1.00 39.63 ? 446  SER   A C    1 
ATOM   340  O  O    . SER   A 1 68  ? 6.733   -2.823  53.131  1.00 38.66 ? 446  SER   A O    1 
ATOM   341  C  CB   . SER   A 1 68  ? 5.542   -4.544  55.461  1.00 38.77 ? 446  SER   A CB   1 
ATOM   342  O  OG   . SER   A 1 68  ? 4.857   -4.796  56.677  1.00 47.60 ? 446  SER   A OG   1 
ATOM   343  N  N    . PRO   A 1 69  ? 8.403   -3.058  54.625  1.00 43.48 ? 447  PRO   A N    1 
ATOM   344  C  CA   . PRO   A 1 69  ? 9.434   -3.059  53.581  1.00 37.69 ? 447  PRO   A CA   1 
ATOM   345  C  C    . PRO   A 1 69  ? 9.317   -4.293  52.699  1.00 47.15 ? 447  PRO   A C    1 
ATOM   346  O  O    . PRO   A 1 69  ? 8.804   -5.335  53.112  1.00 41.76 ? 447  PRO   A O    1 
ATOM   347  C  CB   . PRO   A 1 69  ? 10.746  -3.057  54.374  1.00 35.41 ? 447  PRO   A CB   1 
ATOM   348  C  CG   . PRO   A 1 69  ? 10.378  -2.528  55.727  1.00 35.41 ? 447  PRO   A CG   1 
ATOM   349  C  CD   . PRO   A 1 69  ? 8.981   -3.008  55.977  1.00 41.31 ? 447  PRO   A CD   1 
ATOM   350  N  N    . ARG   A 1 70  ? 9.803   -4.165  51.467  1.00 51.83 ? 448  ARG   A N    1 
ATOM   351  C  CA   . ARG   A 1 70  ? 9.705   -5.220  50.461  1.00 51.17 ? 448  ARG   A CA   1 
ATOM   352  C  C    . ARG   A 1 70  ? 11.113  -5.619  50.028  1.00 56.11 ? 448  ARG   A C    1 
ATOM   353  O  O    . ARG   A 1 70  ? 11.676  -5.041  49.095  1.00 54.92 ? 448  ARG   A O    1 
ATOM   354  C  CB   . ARG   A 1 70  ? 8.861   -4.758  49.273  1.00 45.34 ? 448  ARG   A CB   1 
ATOM   355  C  CG   . ARG   A 1 70  ? 7.425   -4.417  49.632  1.00 47.46 ? 448  ARG   A CG   1 
ATOM   356  C  CD   . ARG   A 1 70  ? 6.735   -3.658  48.511  1.00 41.85 ? 448  ARG   A CD   1 
ATOM   357  N  NE   . ARG   A 1 70  ? 5.411   -3.192  48.907  1.00 45.98 ? 448  ARG   A NE   1 
ATOM   358  C  CZ   . ARG   A 1 70  ? 4.696   -2.302  48.233  1.00 45.29 ? 448  ARG   A CZ   1 
ATOM   359  N  NH1  . ARG   A 1 70  ? 5.146   -1.759  47.114  1.00 42.64 ? 448  ARG   A NH1  1 
ATOM   360  N  NH2  . ARG   A 1 70  ? 3.500   -1.947  48.694  1.00 42.42 ? 448  ARG   A NH2  1 
ATOM   361  N  N    . HIS   A 1 71  ? 11.677  -6.613  50.710  1.00 60.70 ? 449  HIS   A N    1 
ATOM   362  C  CA   . HIS   A 1 71  ? 12.969  -7.167  50.326  1.00 51.74 ? 449  HIS   A CA   1 
ATOM   363  C  C    . HIS   A 1 71  ? 12.759  -8.203  49.227  1.00 48.21 ? 449  HIS   A C    1 
ATOM   364  O  O    . HIS   A 1 71  ? 12.126  -9.239  49.456  1.00 51.94 ? 449  HIS   A O    1 
ATOM   365  C  CB   . HIS   A 1 71  ? 13.667  -7.786  51.535  1.00 46.04 ? 449  HIS   A CB   1 
ATOM   366  N  N    . THR   A 1 72  ? 13.285  -7.923  48.038  1.00 41.84 ? 450  THR   A N    1 
ATOM   367  C  CA   . THR   A 1 72  ? 13.062  -8.782  46.882  1.00 41.01 ? 450  THR   A CA   1 
ATOM   368  C  C    . THR   A 1 72  ? 13.992  -9.990  46.926  1.00 36.94 ? 450  THR   A C    1 
ATOM   369  O  O    . THR   A 1 72  ? 15.198  -9.851  47.154  1.00 45.08 ? 450  THR   A O    1 
ATOM   370  C  CB   . THR   A 1 72  ? 13.268  -7.988  45.591  1.00 34.40 ? 450  THR   A CB   1 
ATOM   371  O  OG1  . THR   A 1 72  ? 12.048  -7.323  45.242  1.00 42.01 ? 450  THR   A OG1  1 
ATOM   372  C  CG2  . THR   A 1 72  ? 13.682  -8.901  44.446  1.00 38.22 ? 450  THR   A CG2  1 
ATOM   373  N  N    . VAL   A 1 73  ? 13.425  -11.173 46.708  1.00 36.15 ? 451  VAL   A N    1 
ATOM   374  C  CA   . VAL   A 1 73  ? 14.175  -12.427 46.727  1.00 36.07 ? 451  VAL   A CA   1 
ATOM   375  C  C    . VAL   A 1 73  ? 13.769  -13.249 45.508  1.00 37.31 ? 451  VAL   A C    1 
ATOM   376  O  O    . VAL   A 1 73  ? 12.579  -13.291 45.162  1.00 32.64 ? 451  VAL   A O    1 
ATOM   377  C  CB   . VAL   A 1 73  ? 13.930  -13.197 48.036  1.00 42.22 ? 451  VAL   A CB   1 
ATOM   378  C  CG1  . VAL   A 1 73  ? 12.443  -13.239 48.351  1.00 44.73 ? 451  VAL   A CG1  1 
ATOM   379  C  CG2  . VAL   A 1 73  ? 14.503  -14.605 47.961  1.00 42.44 ? 451  VAL   A CG2  1 
ATOM   380  N  N    . PRO   A 1 74  ? 14.709  -13.893 44.816  1.00 35.47 ? 452  PRO   A N    1 
ATOM   381  C  CA   . PRO   A 1 74  ? 14.328  -14.752 43.688  1.00 34.19 ? 452  PRO   A CA   1 
ATOM   382  C  C    . PRO   A 1 74  ? 13.487  -15.935 44.146  1.00 30.59 ? 452  PRO   A C    1 
ATOM   383  O  O    . PRO   A 1 74  ? 13.799  -16.601 45.135  1.00 32.83 ? 452  PRO   A O    1 
ATOM   384  C  CB   . PRO   A 1 74  ? 15.676  -15.206 43.114  1.00 32.65 ? 452  PRO   A CB   1 
ATOM   385  C  CG   . PRO   A 1 74  ? 16.668  -14.972 44.212  1.00 31.78 ? 452  PRO   A CG   1 
ATOM   386  C  CD   . PRO   A 1 74  ? 16.170  -13.774 44.952  1.00 31.67 ? 452  PRO   A CD   1 
ATOM   387  N  N    . GLN   A 1 75  ? 12.402  -16.184 43.413  1.00 31.09 ? 453  GLN   A N    1 
ATOM   388  C  CA   . GLN   A 1 75  ? 11.505  -17.294 43.709  1.00 27.56 ? 453  GLN   A CA   1 
ATOM   389  C  C    . GLN   A 1 75  ? 11.207  -18.078 42.436  1.00 29.93 ? 453  GLN   A C    1 
ATOM   390  O  O    . GLN   A 1 75  ? 11.790  -17.803 41.382  1.00 29.71 ? 453  GLN   A O    1 
ATOM   391  C  CB   . GLN   A 1 75  ? 10.213  -16.785 44.353  1.00 31.04 ? 453  GLN   A CB   1 
ATOM   392  C  CG   . GLN   A 1 75  ? 10.444  -15.966 45.618  1.00 30.93 ? 453  GLN   A CG   1 
ATOM   393  C  CD   . GLN   A 1 75  ? 9.180   -15.314 46.139  1.00 37.99 ? 453  GLN   A CD   1 
ATOM   394  O  OE1  . GLN   A 1 75  ? 8.169   -15.977 46.357  1.00 36.41 ? 453  GLN   A OE1  1 
ATOM   395  N  NE2  . GLN   A 1 75  ? 9.234   -14.002 46.341  1.00 36.81 ? 453  GLN   A NE2  1 
ATOM   396  N  N    . CYS   A 1 76  ? 10.305  -19.052 42.520  1.00 31.67 ? 454  CYS   A N    1 
ATOM   397  C  CA   . CYS   A 1 76  ? 10.011  -19.954 41.414  1.00 26.34 ? 454  CYS   A CA   1 
ATOM   398  C  C    . CYS   A 1 76  ? 8.563   -19.787 40.978  1.00 25.70 ? 454  CYS   A C    1 
ATOM   399  O  O    . CYS   A 1 76  ? 7.647   -19.875 41.802  1.00 27.13 ? 454  CYS   A O    1 
ATOM   400  C  CB   . CYS   A 1 76  ? 10.285  -21.405 41.810  1.00 30.11 ? 454  CYS   A CB   1 
ATOM   401  S  SG   . CYS   A 1 76  ? 12.034  -21.768 42.040  1.00 34.38 ? 454  CYS   A SG   1 
ATOM   402  N  N    . CYS   A 1 77  ? 8.363   -19.561 39.681  1.00 24.62 ? 455  CYS   A N    1 
ATOM   403  C  CA   . CYS   A 1 77  ? 7.045   -19.323 39.110  1.00 25.12 ? 455  CYS   A CA   1 
ATOM   404  C  C    . CYS   A 1 77  ? 6.729   -20.376 38.056  1.00 25.33 ? 455  CYS   A C    1 
ATOM   405  O  O    . CYS   A 1 77  ? 7.600   -20.762 37.270  1.00 26.40 ? 455  CYS   A O    1 
ATOM   406  C  CB   . CYS   A 1 77  ? 6.959   -17.928 38.483  1.00 23.35 ? 455  CYS   A CB   1 
ATOM   407  S  SG   . CYS   A 1 77  ? 6.639   -16.594 39.660  1.00 36.73 ? 455  CYS   A SG   1 
ATOM   408  N  N    . TYR   A 1 78  ? 5.477   -20.828 38.044  1.00 24.19 ? 456  TYR   A N    1 
ATOM   409  C  CA   . TYR   A 1 78  ? 4.989   -21.754 37.031  1.00 24.36 ? 456  TYR   A CA   1 
ATOM   410  C  C    . TYR   A 1 78  ? 3.469   -21.752 37.074  1.00 26.80 ? 456  TYR   A C    1 
ATOM   411  O  O    . TYR   A 1 78  ? 2.859   -21.281 38.038  1.00 25.02 ? 456  TYR   A O    1 
ATOM   412  C  CB   . TYR   A 1 78  ? 5.541   -23.171 37.234  1.00 24.73 ? 456  TYR   A CB   1 
ATOM   413  C  CG   . TYR   A 1 78  ? 5.184   -23.809 38.561  1.00 26.94 ? 456  TYR   A CG   1 
ATOM   414  C  CD1  . TYR   A 1 78  ? 5.969   -23.600 39.688  1.00 25.61 ? 456  TYR   A CD1  1 
ATOM   415  C  CD2  . TYR   A 1 78  ? 4.074   -24.637 38.681  1.00 25.93 ? 456  TYR   A CD2  1 
ATOM   416  C  CE1  . TYR   A 1 78  ? 5.650   -24.187 40.901  1.00 26.05 ? 456  TYR   A CE1  1 
ATOM   417  C  CE2  . TYR   A 1 78  ? 3.749   -25.229 39.889  1.00 26.56 ? 456  TYR   A CE2  1 
ATOM   418  C  CZ   . TYR   A 1 78  ? 4.541   -25.000 40.996  1.00 26.68 ? 456  TYR   A CZ   1 
ATOM   419  O  OH   . TYR   A 1 78  ? 4.223   -25.583 42.202  1.00 33.69 ? 456  TYR   A OH   1 
ATOM   420  N  N    . GLY   A 1 79  ? 2.865   -22.272 36.014  1.00 25.01 ? 457  GLY   A N    1 
ATOM   421  C  CA   . GLY   A 1 79  ? 1.430   -22.423 35.958  1.00 25.60 ? 457  GLY   A CA   1 
ATOM   422  C  C    . GLY   A 1 79  ? 0.891   -22.100 34.582  1.00 25.64 ? 457  GLY   A C    1 
ATOM   423  O  O    . GLY   A 1 79  ? 1.628   -22.034 33.599  1.00 25.28 ? 457  GLY   A O    1 
ATOM   424  N  N    . PHE   A 1 80  ? -0.430  -21.906 34.537  1.00 23.27 ? 458  PHE   A N    1 
ATOM   425  C  CA   . PHE   A 1 80  ? -1.128  -21.589 33.294  1.00 20.89 ? 458  PHE   A CA   1 
ATOM   426  C  C    . PHE   A 1 80  ? -0.514  -20.378 32.602  1.00 17.75 ? 458  PHE   A C    1 
ATOM   427  O  O    . PHE   A 1 80  ? -0.129  -20.445 31.429  1.00 19.24 ? 458  PHE   A O    1 
ATOM   428  C  CB   . PHE   A 1 80  ? -2.609  -21.347 33.602  1.00 21.87 ? 458  PHE   A CB   1 
ATOM   429  C  CG   . PHE   A 1 80  ? -3.497  -21.265 32.387  1.00 20.61 ? 458  PHE   A CG   1 
ATOM   430  C  CD1  . PHE   A 1 80  ? -3.489  -20.145 31.570  1.00 20.38 ? 458  PHE   A CD1  1 
ATOM   431  C  CD2  . PHE   A 1 80  ? -4.370  -22.297 32.087  1.00 21.29 ? 458  PHE   A CD2  1 
ATOM   432  C  CE1  . PHE   A 1 80  ? -4.316  -20.069 30.466  1.00 24.15 ? 458  PHE   A CE1  1 
ATOM   433  C  CE2  . PHE   A 1 80  ? -5.200  -22.225 30.987  1.00 16.77 ? 458  PHE   A CE2  1 
ATOM   434  C  CZ   . PHE   A 1 80  ? -5.173  -21.111 30.176  1.00 18.36 ? 458  PHE   A CZ   1 
ATOM   435  N  N    . CYS   A 1 81  ? -0.419  -19.256 33.319  1.00 16.42 ? 459  CYS   A N    1 
ATOM   436  C  CA   . CYS   A 1 81  ? 0.056   -18.020 32.708  1.00 21.04 ? 459  CYS   A CA   1 
ATOM   437  C  C    . CYS   A 1 81  ? 1.545   -18.074 32.390  1.00 19.14 ? 459  CYS   A C    1 
ATOM   438  O  O    . CYS   A 1 81  ? 1.993   -17.445 31.424  1.00 19.24 ? 459  CYS   A O    1 
ATOM   439  C  CB   . CYS   A 1 81  ? -0.252  -16.835 33.622  1.00 15.60 ? 459  CYS   A CB   1 
ATOM   440  S  SG   . CYS   A 1 81  ? -2.000  -16.379 33.675  1.00 21.89 ? 459  CYS   A SG   1 
ATOM   441  N  N    . ILE   A 1 82  ? 2.327   -18.806 33.186  1.00 17.41 ? 460  ILE   A N    1 
ATOM   442  C  CA   . ILE   A 1 82  ? 3.747   -18.948 32.884  1.00 17.21 ? 460  ILE   A CA   1 
ATOM   443  C  C    . ILE   A 1 82  ? 3.941   -19.765 31.614  1.00 22.47 ? 460  ILE   A C    1 
ATOM   444  O  O    . ILE   A 1 82  ? 4.788   -19.439 30.773  1.00 22.66 ? 460  ILE   A O    1 
ATOM   445  C  CB   . ILE   A 1 82  ? 4.490   -19.567 34.081  1.00 22.19 ? 460  ILE   A CB   1 
ATOM   446  C  CG1  . ILE   A 1 82  ? 4.405   -18.640 35.296  1.00 20.11 ? 460  ILE   A CG1  1 
ATOM   447  C  CG2  . ILE   A 1 82  ? 5.941   -19.854 33.721  1.00 24.54 ? 460  ILE   A CG2  1 
ATOM   448  C  CD1  . ILE   A 1 82  ? 4.880   -17.230 35.025  1.00 18.58 ? 460  ILE   A CD1  1 
ATOM   449  N  N    . ASP   A 1 83  ? 3.160   -20.836 31.451  1.00 20.67 ? 461  ASP   A N    1 
ATOM   450  C  CA   . ASP   A 1 83  ? 3.191   -21.588 30.200  1.00 20.58 ? 461  ASP   A CA   1 
ATOM   451  C  C    . ASP   A 1 83  ? 2.788   -20.708 29.024  1.00 23.79 ? 461  ASP   A C    1 
ATOM   452  O  O    . ASP   A 1 83  ? 3.365   -20.811 27.935  1.00 24.57 ? 461  ASP   A O    1 
ATOM   453  C  CB   . ASP   A 1 83  ? 2.274   -22.807 30.294  1.00 22.01 ? 461  ASP   A CB   1 
ATOM   454  C  CG   . ASP   A 1 83  ? 2.963   -24.011 30.901  1.00 21.03 ? 461  ASP   A CG   1 
ATOM   455  O  OD1  . ASP   A 1 83  ? 4.141   -23.886 31.299  1.00 25.47 ? 461  ASP   A OD1  1 
ATOM   456  O  OD2  . ASP   A 1 83  ? 2.329   -25.085 30.976  1.00 25.17 ? 461  ASP   A OD2  1 
ATOM   457  N  N    . LEU   A 1 84  ? 1.799   -19.835 29.226  1.00 21.13 ? 462  LEU   A N    1 
ATOM   458  C  CA   . LEU   A 1 84  ? 1.386   -18.925 28.163  1.00 22.55 ? 462  LEU   A CA   1 
ATOM   459  C  C    . LEU   A 1 84  ? 2.465   -17.890 27.873  1.00 22.11 ? 462  LEU   A C    1 
ATOM   460  O  O    . LEU   A 1 84  ? 2.665   -17.500 26.717  1.00 23.15 ? 462  LEU   A O    1 
ATOM   461  C  CB   . LEU   A 1 84  ? 0.071   -18.242 28.541  1.00 18.34 ? 462  LEU   A CB   1 
ATOM   462  C  CG   . LEU   A 1 84  ? -0.544  -17.323 27.484  1.00 19.77 ? 462  LEU   A CG   1 
ATOM   463  C  CD1  . LEU   A 1 84  ? -0.830  -18.091 26.203  1.00 15.11 ? 462  LEU   A CD1  1 
ATOM   464  C  CD2  . LEU   A 1 84  ? -1.809  -16.667 28.012  1.00 17.48 ? 462  LEU   A CD2  1 
ATOM   465  N  N    . LEU   A 1 85  ? 3.170   -17.434 28.912  1.00 21.62 ? 463  LEU   A N    1 
ATOM   466  C  CA   . LEU   A 1 85  ? 4.265   -16.490 28.707  1.00 22.12 ? 463  LEU   A CA   1 
ATOM   467  C  C    . LEU   A 1 85  ? 5.384   -17.116 27.886  1.00 22.37 ? 463  LEU   A C    1 
ATOM   468  O  O    . LEU   A 1 85  ? 5.932   -16.477 26.979  1.00 19.81 ? 463  LEU   A O    1 
ATOM   469  C  CB   . LEU   A 1 85  ? 4.801   -16.007 30.055  1.00 17.50 ? 463  LEU   A CB   1 
ATOM   470  C  CG   . LEU   A 1 85  ? 6.156   -15.295 30.022  1.00 25.28 ? 463  LEU   A CG   1 
ATOM   471  C  CD1  . LEU   A 1 85  ? 6.046   -13.949 29.317  1.00 24.79 ? 463  LEU   A CD1  1 
ATOM   472  C  CD2  . LEU   A 1 85  ? 6.714   -15.130 31.427  1.00 28.09 ? 463  LEU   A CD2  1 
ATOM   473  N  N    . ILE   A 1 86  ? 5.736   -18.367 28.190  1.00 24.15 ? 464  ILE   A N    1 
ATOM   474  C  CA   . ILE   A 1 86  ? 6.807   -19.042 27.464  1.00 24.49 ? 464  ILE   A CA   1 
ATOM   475  C  C    . ILE   A 1 86  ? 6.427   -19.225 26.001  1.00 27.62 ? 464  ILE   A C    1 
ATOM   476  O  O    . ILE   A 1 86  ? 7.262   -19.066 25.101  1.00 28.77 ? 464  ILE   A O    1 
ATOM   477  C  CB   . ILE   A 1 86  ? 7.140   -20.385 28.140  1.00 30.29 ? 464  ILE   A CB   1 
ATOM   478  C  CG1  . ILE   A 1 86  ? 7.692   -20.148 29.548  1.00 26.84 ? 464  ILE   A CG1  1 
ATOM   479  C  CG2  . ILE   A 1 86  ? 8.130   -21.180 27.307  1.00 35.92 ? 464  ILE   A CG2  1 
ATOM   480  C  CD1  . ILE   A 1 86  ? 7.920   -21.418 30.333  1.00 23.78 ? 464  ILE   A CD1  1 
ATOM   481  N  N    . LYS   A 1 87  ? 5.160   -19.555 25.739  1.00 25.20 ? 465  LYS   A N    1 
ATOM   482  C  CA   . LYS   A 1 87  ? 4.700   -19.694 24.362  1.00 26.57 ? 465  LYS   A CA   1 
ATOM   483  C  C    . LYS   A 1 87  ? 4.820   -18.374 23.612  1.00 30.17 ? 465  LYS   A C    1 
ATOM   484  O  O    . LYS   A 1 87  ? 5.315   -18.333 22.480  1.00 31.03 ? 465  LYS   A O    1 
ATOM   485  C  CB   . LYS   A 1 87  ? 3.256   -20.197 24.339  1.00 27.42 ? 465  LYS   A CB   1 
ATOM   486  C  CG   . LYS   A 1 87  ? 2.785   -20.670 22.974  1.00 30.12 ? 465  LYS   A CG   1 
ATOM   487  C  CD   . LYS   A 1 87  ? 3.475   -21.964 22.576  1.00 37.25 ? 465  LYS   A CD   1 
ATOM   488  C  CE   . LYS   A 1 87  ? 2.940   -22.494 21.257  1.00 36.47 ? 465  LYS   A CE   1 
ATOM   489  N  NZ   . LYS   A 1 87  ? 3.552   -23.803 20.904  1.00 34.99 ? 465  LYS   A NZ   1 
ATOM   490  N  N    . LEU   A 1 88  ? 4.377   -17.280 24.236  1.00 28.12 ? 466  LEU   A N    1 
ATOM   491  C  CA   . LEU   A 1 88  ? 4.452   -15.974 23.589  1.00 25.92 ? 466  LEU   A CA   1 
ATOM   492  C  C    . LEU   A 1 88  ? 5.895   -15.580 23.306  1.00 29.92 ? 466  LEU   A C    1 
ATOM   493  O  O    . LEU   A 1 88  ? 6.185   -14.943 22.287  1.00 30.47 ? 466  LEU   A O    1 
ATOM   494  C  CB   . LEU   A 1 88  ? 3.769   -14.919 24.459  1.00 26.19 ? 466  LEU   A CB   1 
ATOM   495  C  CG   . LEU   A 1 88  ? 2.249   -15.025 24.594  1.00 27.64 ? 466  LEU   A CG   1 
ATOM   496  C  CD1  . LEU   A 1 88  ? 1.741   -14.118 25.705  1.00 18.75 ? 466  LEU   A CD1  1 
ATOM   497  C  CD2  . LEU   A 1 88  ? 1.568   -14.693 23.276  1.00 24.44 ? 466  LEU   A CD2  1 
ATOM   498  N  N    . ALA   A 1 89  ? 6.816   -15.955 24.196  1.00 28.28 ? 467  ALA   A N    1 
ATOM   499  C  CA   . ALA   A 1 89  ? 8.220   -15.612 23.999  1.00 32.61 ? 467  ALA   A CA   1 
ATOM   500  C  C    . ALA   A 1 89  ? 8.815   -16.381 22.827  1.00 37.81 ? 467  ALA   A C    1 
ATOM   501  O  O    . ALA   A 1 89  ? 9.490   -15.801 21.970  1.00 38.55 ? 467  ALA   A O    1 
ATOM   502  C  CB   . ALA   A 1 89  ? 9.011   -15.881 25.279  1.00 29.86 ? 467  ALA   A CB   1 
ATOM   503  N  N    . ARG   A 1 90  ? 8.582   -17.696 22.778  1.00 35.82 ? 468  ARG   A N    1 
ATOM   504  C  CA   . ARG   A 1 90  ? 9.086   -18.493 21.665  1.00 38.14 ? 468  ARG   A CA   1 
ATOM   505  C  C    . ARG   A 1 90  ? 8.408   -18.120 20.353  1.00 37.39 ? 468  ARG   A C    1 
ATOM   506  O  O    . ARG   A 1 90  ? 9.048   -18.152 19.296  1.00 43.07 ? 468  ARG   A O    1 
ATOM   507  C  CB   . ARG   A 1 90  ? 8.889   -19.984 21.943  1.00 41.64 ? 468  ARG   A CB   1 
ATOM   508  C  CG   . ARG   A 1 90  ? 10.107  -20.695 22.512  1.00 57.98 ? 468  ARG   A CG   1 
ATOM   509  C  CD   . ARG   A 1 90  ? 9.676   -21.910 23.322  1.00 64.37 ? 468  ARG   A CD   1 
ATOM   510  N  NE   . ARG   A 1 90  ? 10.334  -22.000 24.622  1.00 71.20 ? 468  ARG   A NE   1 
ATOM   511  C  CZ   . ARG   A 1 90  ? 10.275  -23.062 25.414  1.00 67.31 ? 468  ARG   A CZ   1 
ATOM   512  N  NH1  . ARG   A 1 90  ? 9.608   -24.148 25.065  1.00 71.19 ? 468  ARG   A NH1  1 
ATOM   513  N  NH2  . ARG   A 1 90  ? 10.902  -23.034 26.587  1.00 60.37 ? 468  ARG   A NH2  1 
ATOM   514  N  N    . THR   A 1 91  ? 7.121   -17.766 20.400  1.00 37.25 ? 469  THR   A N    1 
ATOM   515  C  CA   . THR   A 1 91  ? 6.390   -17.455 19.175  1.00 38.89 ? 469  THR   A CA   1 
ATOM   516  C  C    . THR   A 1 91  ? 6.838   -16.125 18.580  1.00 41.71 ? 469  THR   A C    1 
ATOM   517  O  O    . THR   A 1 91  ? 7.052   -16.024 17.366  1.00 45.02 ? 469  THR   A O    1 
ATOM   518  C  CB   . THR   A 1 91  ? 4.886   -17.435 19.455  1.00 36.09 ? 469  THR   A CB   1 
ATOM   519  O  OG1  . THR   A 1 91  ? 4.425   -18.770 19.695  1.00 38.19 ? 469  THR   A OG1  1 
ATOM   520  C  CG2  . THR   A 1 91  ? 4.120   -16.839 18.278  1.00 33.83 ? 469  THR   A CG2  1 
ATOM   521  N  N    . MET   A 1 92  ? 6.990   -15.099 19.413  1.00 36.43 ? 470  MET   A N    1 
ATOM   522  C  CA   . MET   A 1 92  ? 7.299   -13.754 18.949  1.00 37.03 ? 470  MET   A CA   1 
ATOM   523  C  C    . MET   A 1 92  ? 8.763   -13.376 19.131  1.00 35.53 ? 470  MET   A C    1 
ATOM   524  O  O    . MET   A 1 92  ? 9.144   -12.253 18.783  1.00 40.82 ? 470  MET   A O    1 
ATOM   525  C  CB   . MET   A 1 92  ? 6.400   -12.742 19.663  1.00 32.47 ? 470  MET   A CB   1 
ATOM   526  C  CG   . MET   A 1 92  ? 4.919   -13.059 19.523  1.00 39.89 ? 470  MET   A CG   1 
ATOM   527  S  SD   . MET   A 1 92  ? 3.867   -11.998 20.523  1.00 43.13 ? 470  MET   A SD   1 
ATOM   528  C  CE   . MET   A 1 92  ? 4.582   -10.395 20.172  1.00 35.61 ? 470  MET   A CE   1 
ATOM   529  N  N    . ASN   A 1 93  ? 9.585   -14.279 19.669  1.00 39.41 ? 471  ASN   A N    1 
ATOM   530  C  CA   . ASN   A 1 93  ? 11.038  -14.119 19.731  1.00 41.76 ? 471  ASN   A CA   1 
ATOM   531  C  C    . ASN   A 1 93  ? 11.428  -12.890 20.559  1.00 36.16 ? 471  ASN   A C    1 
ATOM   532  O  O    . ASN   A 1 93  ? 11.965  -11.902 20.055  1.00 44.54 ? 471  ASN   A O    1 
ATOM   533  C  CB   . ASN   A 1 93  ? 11.632  -14.047 18.317  1.00 37.35 ? 471  ASN   A CB   1 
ATOM   534  C  CG   . ASN   A 1 93  ? 13.140  -14.195 18.306  1.00 39.53 ? 471  ASN   A CG   1 
ATOM   535  O  OD1  . ASN   A 1 93  ? 13.723  -14.814 19.196  1.00 49.70 ? 471  ASN   A OD1  1 
ATOM   536  N  ND2  . ASN   A 1 93  ? 13.781  -13.626 17.292  1.00 37.65 ? 471  ASN   A ND2  1 
ATOM   537  N  N    . PHE   A 1 94  ? 11.149  -12.982 21.859  1.00 36.15 ? 472  PHE   A N    1 
ATOM   538  C  CA   . PHE   A 1 94  ? 11.588  -11.963 22.800  1.00 30.22 ? 472  PHE   A CA   1 
ATOM   539  C  C    . PHE   A 1 94  ? 12.055  -12.619 24.090  1.00 35.85 ? 472  PHE   A C    1 
ATOM   540  O  O    . PHE   A 1 94  ? 11.597  -13.704 24.458  1.00 33.14 ? 472  PHE   A O    1 
ATOM   541  C  CB   . PHE   A 1 94  ? 10.486  -10.924 23.095  1.00 33.84 ? 472  PHE   A CB   1 
ATOM   542  C  CG   . PHE   A 1 94  ? 9.287   -11.470 23.831  1.00 36.36 ? 472  PHE   A CG   1 
ATOM   543  C  CD1  . PHE   A 1 94  ? 9.292   -11.594 25.213  1.00 36.72 ? 472  PHE   A CD1  1 
ATOM   544  C  CD2  . PHE   A 1 94  ? 8.138   -11.817 23.140  1.00 37.00 ? 472  PHE   A CD2  1 
ATOM   545  C  CE1  . PHE   A 1 94  ? 8.186   -12.080 25.886  1.00 32.23 ? 472  PHE   A CE1  1 
ATOM   546  C  CE2  . PHE   A 1 94  ? 7.027   -12.300 23.808  1.00 35.71 ? 472  PHE   A CE2  1 
ATOM   547  C  CZ   . PHE   A 1 94  ? 7.052   -12.432 25.183  1.00 28.27 ? 472  PHE   A CZ   1 
ATOM   548  N  N    . THR   A 1 95  ? 12.978  -11.946 24.769  1.00 31.86 ? 473  THR   A N    1 
ATOM   549  C  CA   . THR   A 1 95  ? 13.467  -12.350 26.078  1.00 32.45 ? 473  THR   A CA   1 
ATOM   550  C  C    . THR   A 1 95  ? 12.702  -11.603 27.165  1.00 35.78 ? 473  THR   A C    1 
ATOM   551  O  O    . THR   A 1 95  ? 12.115  -10.545 26.928  1.00 37.03 ? 473  THR   A O    1 
ATOM   552  C  CB   . THR   A 1 95  ? 14.968  -12.079 26.204  1.00 33.92 ? 473  THR   A CB   1 
ATOM   553  O  OG1  . THR   A 1 95  ? 15.228  -10.697 25.929  1.00 38.94 ? 473  THR   A OG1  1 
ATOM   554  C  CG2  . THR   A 1 95  ? 15.743  -12.937 25.216  1.00 29.23 ? 473  THR   A CG2  1 
ATOM   555  N  N    . TYR   A 1 96  ? 12.716  -12.165 28.372  1.00 35.95 ? 474  TYR   A N    1 
ATOM   556  C  CA   . TYR   A 1 96  ? 11.870  -11.639 29.432  1.00 34.24 ? 474  TYR   A CA   1 
ATOM   557  C  C    . TYR   A 1 96  ? 12.485  -11.907 30.796  1.00 32.48 ? 474  TYR   A C    1 
ATOM   558  O  O    . TYR   A 1 96  ? 13.260  -12.850 30.976  1.00 34.02 ? 474  TYR   A O    1 
ATOM   559  C  CB   . TYR   A 1 96  ? 10.465  -12.248 29.371  1.00 25.91 ? 474  TYR   A CB   1 
ATOM   560  C  CG   . TYR   A 1 96  ? 10.457  -13.755 29.483  1.00 29.43 ? 474  TYR   A CG   1 
ATOM   561  C  CD1  . TYR   A 1 96  ? 10.602  -14.553 28.357  1.00 29.96 ? 474  TYR   A CD1  1 
ATOM   562  C  CD2  . TYR   A 1 96  ? 10.311  -14.380 30.715  1.00 29.01 ? 474  TYR   A CD2  1 
ATOM   563  C  CE1  . TYR   A 1 96  ? 10.601  -15.929 28.453  1.00 24.68 ? 474  TYR   A CE1  1 
ATOM   564  C  CE2  . TYR   A 1 96  ? 10.308  -15.758 30.821  1.00 24.32 ? 474  TYR   A CE2  1 
ATOM   565  C  CZ   . TYR   A 1 96  ? 10.453  -16.527 29.686  1.00 26.26 ? 474  TYR   A CZ   1 
ATOM   566  O  OH   . TYR   A 1 96  ? 10.451  -17.899 29.783  1.00 34.50 ? 474  TYR   A OH   1 
ATOM   567  N  N    . GLU   A 1 97  ? 12.118  -11.060 31.756  1.00 33.32 ? 475  GLU   A N    1 
ATOM   568  C  CA   . GLU   A 1 97  ? 12.412  -11.257 33.168  1.00 32.95 ? 475  GLU   A CA   1 
ATOM   569  C  C    . GLU   A 1 97  ? 11.115  -11.077 33.942  1.00 26.65 ? 475  GLU   A C    1 
ATOM   570  O  O    . GLU   A 1 97  ? 10.386  -10.106 33.715  1.00 28.01 ? 475  GLU   A O    1 
ATOM   571  C  CB   . GLU   A 1 97  ? 13.478  -10.273 33.664  1.00 24.69 ? 475  GLU   A CB   1 
ATOM   572  N  N    . VAL   A 1 98  ? 10.825  -12.009 34.845  1.00 28.15 ? 476  VAL   A N    1 
ATOM   573  C  CA   . VAL   A 1 98  ? 9.550   -12.056 35.550  1.00 25.57 ? 476  VAL   A CA   1 
ATOM   574  C  C    . VAL   A 1 98  ? 9.753   -11.606 36.989  1.00 27.64 ? 476  VAL   A C    1 
ATOM   575  O  O    . VAL   A 1 98  ? 10.733  -11.989 37.639  1.00 26.72 ? 476  VAL   A O    1 
ATOM   576  C  CB   . VAL   A 1 98  ? 8.939   -13.470 35.503  1.00 22.19 ? 476  VAL   A CB   1 
ATOM   577  C  CG1  . VAL   A 1 98  ? 7.494   -13.444 35.981  1.00 23.61 ? 476  VAL   A CG1  1 
ATOM   578  C  CG2  . VAL   A 1 98  ? 9.037   -14.040 34.097  1.00 27.08 ? 476  VAL   A CG2  1 
ATOM   579  N  N    . HIS   A 1 99  ? 8.823   -10.791 37.484  1.00 25.47 ? 477  HIS   A N    1 
ATOM   580  C  CA   . HIS   A 1 99  ? 8.809   -10.391 38.883  1.00 23.72 ? 477  HIS   A CA   1 
ATOM   581  C  C    . HIS   A 1 99  ? 7.368   -10.250 39.351  1.00 21.80 ? 477  HIS   A C    1 
ATOM   582  O  O    . HIS   A 1 99  ? 6.473   -9.923  38.567  1.00 23.93 ? 477  HIS   A O    1 
ATOM   583  C  CB   . HIS   A 1 99  ? 9.578   -9.080  39.117  1.00 22.39 ? 477  HIS   A CB   1 
ATOM   584  C  CG   . HIS   A 1 99  ? 8.841   -7.851  38.679  1.00 24.24 ? 477  HIS   A CG   1 
ATOM   585  N  ND1  . HIS   A 1 99  ? 8.898   -7.369  37.390  1.00 24.84 ? 477  HIS   A ND1  1 
ATOM   586  C  CD2  . HIS   A 1 99  ? 8.042   -7.000  39.365  1.00 21.55 ? 477  HIS   A CD2  1 
ATOM   587  C  CE1  . HIS   A 1 99  ? 8.160   -6.276  37.298  1.00 26.26 ? 477  HIS   A CE1  1 
ATOM   588  N  NE2  . HIS   A 1 99  ? 7.629   -6.031  38.482  1.00 24.62 ? 477  HIS   A NE2  1 
ATOM   589  N  N    . LEU   A 1 100 ? 7.151   -10.513 40.637  1.00 23.38 ? 478  LEU   A N    1 
ATOM   590  C  CA   . LEU   A 1 100 ? 5.827   -10.386 41.226  1.00 22.87 ? 478  LEU   A CA   1 
ATOM   591  C  C    . LEU   A 1 100 ? 5.497   -8.920  41.483  1.00 21.25 ? 478  LEU   A C    1 
ATOM   592  O  O    . LEU   A 1 100 ? 6.383   -8.098  41.737  1.00 26.53 ? 478  LEU   A O    1 
ATOM   593  C  CB   . LEU   A 1 100 ? 5.734   -11.172 42.536  1.00 20.17 ? 478  LEU   A CB   1 
ATOM   594  C  CG   . LEU   A 1 100 ? 5.658   -12.703 42.487  1.00 25.29 ? 478  LEU   A CG   1 
ATOM   595  C  CD1  . LEU   A 1 100 ? 4.639   -13.168 41.455  1.00 22.63 ? 478  LEU   A CD1  1 
ATOM   596  C  CD2  . LEU   A 1 100 ? 7.023   -13.333 42.235  1.00 35.39 ? 478  LEU   A CD2  1 
ATOM   597  N  N    . VAL   A 1 101 ? 4.203   -8.596  41.413  1.00 24.67 ? 479  VAL   A N    1 
ATOM   598  C  CA   . VAL   A 1 101 ? 3.771   -7.230  41.676  1.00 20.74 ? 479  VAL   A CA   1 
ATOM   599  C  C    . VAL   A 1 101 ? 4.088   -6.868  43.121  1.00 24.06 ? 479  VAL   A C    1 
ATOM   600  O  O    . VAL   A 1 101 ? 3.898   -7.672  44.044  1.00 26.03 ? 479  VAL   A O    1 
ATOM   601  C  CB   . VAL   A 1 101 ? 2.275   -7.065  41.354  1.00 21.61 ? 479  VAL   A CB   1 
ATOM   602  C  CG1  . VAL   A 1 101 ? 1.432   -8.050  42.153  1.00 19.61 ? 479  VAL   A CG1  1 
ATOM   603  C  CG2  . VAL   A 1 101 ? 1.825   -5.630  41.596  1.00 21.80 ? 479  VAL   A CG2  1 
ATOM   604  N  N    . ALA   A 1 102 ? 4.590   -5.646  43.320  1.00 23.84 ? 480  ALA   A N    1 
ATOM   605  C  CA   . ALA   A 1 102 ? 5.192   -5.286  44.601  1.00 28.30 ? 480  ALA   A CA   1 
ATOM   606  C  C    . ALA   A 1 102 ? 4.160   -5.219  45.721  1.00 32.68 ? 480  ALA   A C    1 
ATOM   607  O  O    . ALA   A 1 102 ? 4.455   -5.595  46.861  1.00 27.89 ? 480  ALA   A O    1 
ATOM   608  C  CB   . ALA   A 1 102 ? 5.932   -3.955  44.474  1.00 29.91 ? 480  ALA   A CB   1 
ATOM   609  N  N    . ASP   A 1 103 ? 2.953   -4.736  45.428  1.00 27.02 ? 481  ASP   A N    1 
ATOM   610  C  CA   . ASP   A 1 103 ? 1.922   -4.590  46.447  1.00 27.51 ? 481  ASP   A CA   1 
ATOM   611  C  C    . ASP   A 1 103 ? 0.903   -5.724  46.429  1.00 25.30 ? 481  ASP   A C    1 
ATOM   612  O  O    . ASP   A 1 103 ? -0.127  -5.627  47.105  1.00 28.45 ? 481  ASP   A O    1 
ATOM   613  C  CB   . ASP   A 1 103 ? 1.218   -3.236  46.302  1.00 23.47 ? 481  ASP   A CB   1 
ATOM   614  C  CG   . ASP   A 1 103 ? 0.493   -3.080  44.975  1.00 25.26 ? 481  ASP   A CG   1 
ATOM   615  O  OD1  . ASP   A 1 103 ? 0.507   -4.024  44.158  1.00 32.48 ? 481  ASP   A OD1  1 
ATOM   616  O  OD2  . ASP   A 1 103 ? -0.098  -2.002  44.750  1.00 24.44 ? 481  ASP   A OD2  1 
ATOM   617  N  N    . GLY   A 1 104 ? 1.165   -6.788  45.672  1.00 24.73 ? 482  GLY   A N    1 
ATOM   618  C  CA   . GLY   A 1 104 ? 0.285   -7.942  45.654  1.00 23.78 ? 482  GLY   A CA   1 
ATOM   619  C  C    . GLY   A 1 104 ? -1.124  -7.670  45.179  1.00 25.51 ? 482  GLY   A C    1 
ATOM   620  O  O    . GLY   A 1 104 ? -2.025  -8.463  45.460  1.00 21.12 ? 482  GLY   A O    1 
ATOM   621  N  N    . LYS   A 1 105 ? -1.342  -6.574  44.460  1.00 19.52 ? 483  LYS   A N    1 
ATOM   622  C  CA   . LYS   A 1 105 ? -2.671  -6.176  44.024  1.00 22.79 ? 483  LYS   A CA   1 
ATOM   623  C  C    . LYS   A 1 105 ? -2.795  -6.291  42.510  1.00 21.78 ? 483  LYS   A C    1 
ATOM   624  O  O    . LYS   A 1 105 ? -1.807  -6.188  41.777  1.00 21.75 ? 483  LYS   A O    1 
ATOM   625  C  CB   . LYS   A 1 105 ? -2.987  -4.746  44.470  1.00 26.57 ? 483  LYS   A CB   1 
ATOM   626  C  CG   . LYS   A 1 105 ? -3.077  -4.584  45.978  1.00 24.37 ? 483  LYS   A CG   1 
ATOM   627  C  CD   . LYS   A 1 105 ? -3.973  -5.653  46.585  1.00 24.17 ? 483  LYS   A CD   1 
ATOM   628  C  CE   . LYS   A 1 105 ? -4.187  -5.422  48.071  1.00 26.19 ? 483  LYS   A CE   1 
ATOM   629  N  NZ   . LYS   A 1 105 ? -2.920  -5.547  48.845  1.00 23.21 ? 483  LYS   A NZ   1 
ATOM   630  N  N    . PHE   A 1 106 ? -4.030  -6.506  42.050  1.00 23.04 ? 484  PHE   A N    1 
ATOM   631  C  CA   . PHE   A 1 106 ? -4.273  -6.660  40.619  1.00 17.34 ? 484  PHE   A CA   1 
ATOM   632  C  C    . PHE   A 1 106 ? -4.182  -5.321  39.896  1.00 20.57 ? 484  PHE   A C    1 
ATOM   633  O  O    . PHE   A 1 106 ? -3.416  -5.173  38.936  1.00 18.57 ? 484  PHE   A O    1 
ATOM   634  C  CB   . PHE   A 1 106 ? -5.637  -7.312  40.387  1.00 19.13 ? 484  PHE   A CB   1 
ATOM   635  C  CG   . PHE   A 1 106 ? -5.602  -8.816  40.404  1.00 18.98 ? 484  PHE   A CG   1 
ATOM   636  C  CD1  . PHE   A 1 106 ? -5.767  -9.514  41.589  1.00 19.40 ? 484  PHE   A CD1  1 
ATOM   637  C  CD2  . PHE   A 1 106 ? -5.403  -9.529  39.234  1.00 15.31 ? 484  PHE   A CD2  1 
ATOM   638  C  CE1  . PHE   A 1 106 ? -5.734  -10.899 41.606  1.00 20.04 ? 484  PHE   A CE1  1 
ATOM   639  C  CE2  . PHE   A 1 106 ? -5.371  -10.911 39.243  1.00 17.65 ? 484  PHE   A CE2  1 
ATOM   640  C  CZ   . PHE   A 1 106 ? -5.537  -11.598 40.430  1.00 19.18 ? 484  PHE   A CZ   1 
ATOM   641  N  N    . GLY   A 1 107 ? -4.958  -4.333  40.340  1.00 16.95 ? 485  GLY   A N    1 
ATOM   642  C  CA   . GLY   A 1 107 ? -4.909  -3.016  39.734  1.00 21.58 ? 485  GLY   A CA   1 
ATOM   643  C  C    . GLY   A 1 107 ? -6.208  -2.240  39.810  1.00 24.93 ? 485  GLY   A C    1 
ATOM   644  O  O    . GLY   A 1 107 ? -7.226  -2.656  39.244  1.00 24.66 ? 485  GLY   A O    1 
ATOM   645  N  N    . THR   A 1 108 ? -6.177  -1.100  40.499  1.00 25.13 ? 486  THR   A N    1 
ATOM   646  C  CA   . THR   A 1 108 ? -7.345  -0.248  40.663  1.00 22.15 ? 486  THR   A CA   1 
ATOM   647  C  C    . THR   A 1 108 ? -6.913  1.209   40.618  1.00 27.39 ? 486  THR   A C    1 
ATOM   648  O  O    . THR   A 1 108 ? -5.806  1.557   41.037  1.00 32.33 ? 486  THR   A O    1 
ATOM   649  C  CB   . THR   A 1 108 ? -8.058  -0.484  41.993  1.00 25.17 ? 486  THR   A CB   1 
ATOM   650  O  OG1  . THR   A 1 108 ? -7.083  -0.688  43.022  1.00 41.41 ? 486  THR   A OG1  1 
ATOM   651  C  CG2  . THR   A 1 108 ? -8.944  -1.708  41.898  1.00 28.03 ? 486  THR   A CG2  1 
ATOM   652  N  N    . GLN   A 1 109 ? -7.805  2.064   40.124  1.00 27.74 ? 487  GLN   A N    1 
ATOM   653  C  CA   . GLN   A 1 109 ? -7.581  3.506   40.120  1.00 29.52 ? 487  GLN   A CA   1 
ATOM   654  C  C    . GLN   A 1 109 ? -8.338  4.110   41.298  1.00 32.51 ? 487  GLN   A C    1 
ATOM   655  O  O    . GLN   A 1 109 ? -9.573  4.130   41.305  1.00 29.86 ? 487  GLN   A O    1 
ATOM   656  C  CB   . GLN   A 1 109 ? -8.024  4.133   38.801  1.00 29.88 ? 487  GLN   A CB   1 
ATOM   657  C  CG   . GLN   A 1 109 ? -7.442  5.518   38.562  1.00 38.17 ? 487  GLN   A CG   1 
ATOM   658  C  CD   . GLN   A 1 109 ? -7.831  6.093   37.216  1.00 37.97 ? 487  GLN   A CD   1 
ATOM   659  O  OE1  . GLN   A 1 109 ? -8.976  5.969   36.782  1.00 27.37 ? 487  GLN   A OE1  1 
ATOM   660  N  NE2  . GLN   A 1 109 ? -6.877  6.729   36.547  1.00 32.72 ? 487  GLN   A NE2  1 
ATOM   661  N  N    . GLU   A 1 110 ? -7.600  4.601   42.287  1.00 29.00 ? 488  GLU   A N    1 
ATOM   662  C  CA   . GLU   A 1 110 ? -8.208  5.167   43.485  1.00 35.26 ? 488  GLU   A CA   1 
ATOM   663  C  C    . GLU   A 1 110 ? -7.973  6.672   43.563  1.00 31.70 ? 488  GLU   A C    1 
ATOM   664  O  O    . GLU   A 1 110 ? -6.862  7.149   43.333  1.00 32.84 ? 488  GLU   A O    1 
ATOM   665  C  CB   . GLU   A 1 110 ? -7.656  4.483   44.739  1.00 28.17 ? 488  GLU   A CB   1 
ATOM   666  C  CG   . GLU   A 1 110 ? -7.800  2.966   44.736  1.00 35.67 ? 488  GLU   A CG   1 
ATOM   667  C  CD   . GLU   A 1 110 ? -9.229  2.499   44.968  1.00 37.82 ? 488  GLU   A CD   1 
ATOM   668  O  OE1  . GLU   A 1 110 ? -10.108 3.347   45.233  1.00 33.11 ? 488  GLU   A OE1  1 
ATOM   669  O  OE2  . GLU   A 1 110 ? -9.474  1.278   44.879  1.00 38.98 ? 488  GLU   A OE2  1 
ATOM   670  N  N    . ASN   A 1 116 ? -8.226  14.679  44.804  1.00 42.25 ? 494  ASN   A N    1 
ATOM   671  C  CA   . ASN   A 1 116 ? -8.213  15.365  43.518  1.00 50.43 ? 494  ASN   A CA   1 
ATOM   672  C  C    . ASN   A 1 116 ? -7.703  14.446  42.412  1.00 58.96 ? 494  ASN   A C    1 
ATOM   673  O  O    . ASN   A 1 116 ? -8.394  14.206  41.422  1.00 56.66 ? 494  ASN   A O    1 
ATOM   674  C  CB   . ASN   A 1 116 ? -7.351  16.628  43.593  1.00 62.12 ? 494  ASN   A CB   1 
ATOM   675  C  CG   . ASN   A 1 116 ? -7.244  17.346  42.259  1.00 67.75 ? 494  ASN   A CG   1 
ATOM   676  O  OD1  . ASN   A 1 116 ? -8.116  17.222  41.398  1.00 56.20 ? 494  ASN   A OD1  1 
ATOM   677  N  ND2  . ASN   A 1 116 ? -6.166  18.101  42.081  1.00 65.23 ? 494  ASN   A ND2  1 
ATOM   678  N  N    . LYS   A 1 117 ? -6.488  13.937  42.587  1.00 60.91 ? 495  LYS   A N    1 
ATOM   679  C  CA   . LYS   A 1 117 ? -5.860  13.087  41.588  1.00 46.39 ? 495  LYS   A CA   1 
ATOM   680  C  C    . LYS   A 1 117 ? -6.159  11.618  41.861  1.00 37.59 ? 495  LYS   A C    1 
ATOM   681  O  O    . LYS   A 1 117 ? -6.313  11.195  43.010  1.00 38.05 ? 495  LYS   A O    1 
ATOM   682  C  CB   . LYS   A 1 117 ? -4.347  13.310  41.562  1.00 40.68 ? 495  LYS   A CB   1 
ATOM   683  N  N    . LYS   A 1 118 ? -6.246  10.845  40.785  1.00 34.92 ? 496  LYS   A N    1 
ATOM   684  C  CA   . LYS   A 1 118 ? -6.395  9.401   40.860  1.00 32.31 ? 496  LYS   A CA   1 
ATOM   685  C  C    . LYS   A 1 118 ? -5.062  8.727   40.556  1.00 36.27 ? 496  LYS   A C    1 
ATOM   686  O  O    . LYS   A 1 118 ? -4.181  9.299   39.911  1.00 37.38 ? 496  LYS   A O    1 
ATOM   687  C  CB   . LYS   A 1 118 ? -7.470  8.913   39.885  1.00 35.24 ? 496  LYS   A CB   1 
ATOM   688  N  N    . GLU   A 1 119 ? -4.923  7.493   41.033  1.00 32.65 ? 497  GLU   A N    1 
ATOM   689  C  CA   . GLU   A 1 119 ? -3.669  6.769   40.886  1.00 27.21 ? 497  GLU   A CA   1 
ATOM   690  C  C    . GLU   A 1 119 ? -3.949  5.281   40.740  1.00 28.62 ? 497  GLU   A C    1 
ATOM   691  O  O    . GLU   A 1 119 ? -4.769  4.722   41.473  1.00 32.10 ? 497  GLU   A O    1 
ATOM   692  C  CB   . GLU   A 1 119 ? -2.746  7.022   42.084  1.00 28.62 ? 497  GLU   A CB   1 
ATOM   693  C  CG   . GLU   A 1 119 ? -1.578  6.061   42.182  1.00 38.75 ? 497  GLU   A CG   1 
ATOM   694  C  CD   . GLU   A 1 119 ? -1.167  5.794   43.613  1.00 52.78 ? 497  GLU   A CD   1 
ATOM   695  O  OE1  . GLU   A 1 119 ? -0.007  5.389   43.832  1.00 43.74 ? 497  GLU   A OE1  1 
ATOM   696  O  OE2  . GLU   A 1 119 ? -2.003  5.992   44.519  1.00 49.00 ? 497  GLU   A OE2  1 
ATOM   697  N  N    . TRP   A 1 120 ? -3.262  4.649   39.792  1.00 24.89 ? 498  TRP   A N    1 
ATOM   698  C  CA   . TRP   A 1 120 ? -3.363  3.209   39.613  1.00 30.73 ? 498  TRP   A CA   1 
ATOM   699  C  C    . TRP   A 1 120 ? -2.401  2.489   40.547  1.00 26.11 ? 498  TRP   A C    1 
ATOM   700  O  O    . TRP   A 1 120 ? -1.246  2.893   40.708  1.00 28.58 ? 498  TRP   A O    1 
ATOM   701  C  CB   . TRP   A 1 120 ? -3.062  2.823   38.165  1.00 26.16 ? 498  TRP   A CB   1 
ATOM   702  C  CG   . TRP   A 1 120 ? -4.192  3.080   37.219  1.00 25.45 ? 498  TRP   A CG   1 
ATOM   703  C  CD1  . TRP   A 1 120 ? -4.353  4.166   36.411  1.00 24.62 ? 498  TRP   A CD1  1 
ATOM   704  C  CD2  . TRP   A 1 120 ? -5.322  2.232   36.980  1.00 29.05 ? 498  TRP   A CD2  1 
ATOM   705  N  NE1  . TRP   A 1 120 ? -5.512  4.049   35.683  1.00 28.91 ? 498  TRP   A NE1  1 
ATOM   706  C  CE2  . TRP   A 1 120 ? -6.125  2.870   36.015  1.00 27.90 ? 498  TRP   A CE2  1 
ATOM   707  C  CE3  . TRP   A 1 120 ? -5.732  0.996   37.489  1.00 24.33 ? 498  TRP   A CE3  1 
ATOM   708  C  CZ2  . TRP   A 1 120 ? -7.314  2.314   35.548  1.00 27.54 ? 498  TRP   A CZ2  1 
ATOM   709  C  CZ3  . TRP   A 1 120 ? -6.912  0.446   37.024  1.00 21.36 ? 498  TRP   A CZ3  1 
ATOM   710  C  CH2  . TRP   A 1 120 ? -7.690  1.104   36.064  1.00 26.75 ? 498  TRP   A CH2  1 
ATOM   711  N  N    . ASN   A 1 121 ? -2.886  1.417   41.164  1.00 26.49 ? 499  ASN   A N    1 
ATOM   712  C  CA   . ASN   A 1 121 ? -2.077  0.557   42.014  1.00 28.61 ? 499  ASN   A CA   1 
ATOM   713  C  C    . ASN   A 1 121 ? -1.905  -0.803  41.345  1.00 20.46 ? 499  ASN   A C    1 
ATOM   714  O  O    . ASN   A 1 121 ? -2.378  -1.040  40.229  1.00 19.33 ? 499  ASN   A O    1 
ATOM   715  C  CB   . ASN   A 1 121 ? -2.709  0.417   43.404  1.00 27.34 ? 499  ASN   A CB   1 
ATOM   716  C  CG   . ASN   A 1 121 ? -4.167  -0.008  43.348  1.00 26.22 ? 499  ASN   A CG   1 
ATOM   717  O  OD1  . ASN   A 1 121 ? -4.537  -0.914  42.601  1.00 20.78 ? 499  ASN   A OD1  1 
ATOM   718  N  ND2  . ASN   A 1 121 ? -5.003  0.644   44.149  1.00 31.05 ? 499  ASN   A ND2  1 
ATOM   719  N  N    . GLY   A 1 122 ? -1.211  -1.701  42.043  1.00 21.18 ? 500  GLY   A N    1 
ATOM   720  C  CA   . GLY   A 1 122 ? -1.091  -3.072  41.586  1.00 20.38 ? 500  GLY   A CA   1 
ATOM   721  C  C    . GLY   A 1 122 ? -0.332  -3.204  40.277  1.00 22.25 ? 500  GLY   A C    1 
ATOM   722  O  O    . GLY   A 1 122 ? 0.538   -2.396  39.937  1.00 19.45 ? 500  GLY   A O    1 
ATOM   723  N  N    . MET   A 1 123 ? -0.675  -4.258  39.529  1.00 17.80 ? 501  MET   A N    1 
ATOM   724  C  CA   . MET   A 1 123 ? -0.009  -4.518  38.256  1.00 17.89 ? 501  MET   A CA   1 
ATOM   725  C  C    . MET   A 1 123 ? -0.292  -3.422  37.238  1.00 18.94 ? 501  MET   A C    1 
ATOM   726  O  O    . MET   A 1 123 ? 0.551   -3.142  36.378  1.00 19.33 ? 501  MET   A O    1 
ATOM   727  C  CB   . MET   A 1 123 ? -0.439  -5.880  37.709  1.00 16.39 ? 501  MET   A CB   1 
ATOM   728  C  CG   . MET   A 1 123 ? 0.176   -7.055  38.449  1.00 16.55 ? 501  MET   A CG   1 
ATOM   729  S  SD   . MET   A 1 123 ? -0.380  -8.672  37.871  1.00 18.62 ? 501  MET   A SD   1 
ATOM   730  C  CE   . MET   A 1 123 ? -2.157  -8.457  37.886  1.00 15.00 ? 501  MET   A CE   1 
ATOM   731  N  N    . MET   A 1 124 ? -1.469  -2.797  37.313  1.00 19.39 ? 502  MET   A N    1 
ATOM   732  C  CA   . MET   A 1 124 ? -1.775  -1.680  36.425  1.00 21.58 ? 502  MET   A CA   1 
ATOM   733  C  C    . MET   A 1 124 ? -0.816  -0.519  36.657  1.00 22.08 ? 502  MET   A C    1 
ATOM   734  O  O    . MET   A 1 124 ? -0.303  0.079   35.704  1.00 21.63 ? 502  MET   A O    1 
ATOM   735  C  CB   . MET   A 1 124 ? -3.222  -1.235  36.628  1.00 17.81 ? 502  MET   A CB   1 
ATOM   736  C  CG   . MET   A 1 124 ? -4.253  -2.252  36.177  1.00 21.90 ? 502  MET   A CG   1 
ATOM   737  S  SD   . MET   A 1 124 ? -4.348  -2.362  34.379  1.00 25.11 ? 502  MET   A SD   1 
ATOM   738  C  CE   . MET   A 1 124 ? -4.651  -0.649  33.958  1.00 19.96 ? 502  MET   A CE   1 
ATOM   739  N  N    . GLY   A 1 125 ? -0.561  -0.188  37.924  1.00 21.75 ? 503  GLY   A N    1 
ATOM   740  C  CA   . GLY   A 1 125 ? 0.373   0.885   38.220  1.00 21.54 ? 503  GLY   A CA   1 
ATOM   741  C  C    . GLY   A 1 125 ? 1.785   0.573   37.762  1.00 22.69 ? 503  GLY   A C    1 
ATOM   742  O  O    . GLY   A 1 125 ? 2.510   1.459   37.304  1.00 23.27 ? 503  GLY   A O    1 
ATOM   743  N  N    . GLU   A 1 126 ? 2.192   -0.694  37.869  1.00 22.01 ? 504  GLU   A N    1 
ATOM   744  C  CA   . GLU   A 1 126 ? 3.532   -1.077  37.436  1.00 23.78 ? 504  GLU   A CA   1 
ATOM   745  C  C    . GLU   A 1 126 ? 3.664   -1.026  35.919  1.00 27.39 ? 504  GLU   A C    1 
ATOM   746  O  O    . GLU   A 1 126 ? 4.729   -0.683  35.394  1.00 27.76 ? 504  GLU   A O    1 
ATOM   747  C  CB   . GLU   A 1 126 ? 3.874   -2.472  37.958  1.00 22.55 ? 504  GLU   A CB   1 
ATOM   748  C  CG   . GLU   A 1 126 ? 3.933   -2.572  39.476  1.00 24.37 ? 504  GLU   A CG   1 
ATOM   749  C  CD   . GLU   A 1 126 ? 4.890   -3.648  39.951  1.00 29.44 ? 504  GLU   A CD   1 
ATOM   750  O  OE1  . GLU   A 1 126 ? 5.505   -4.319  39.096  1.00 24.50 ? 504  GLU   A OE1  1 
ATOM   751  O  OE2  . GLU   A 1 126 ? 5.031   -3.816  41.180  1.00 27.60 ? 504  GLU   A OE2  1 
ATOM   752  N  N    . LEU   A 1 127 ? 2.593   -1.364  35.197  1.00 23.20 ? 505  LEU   A N    1 
ATOM   753  C  CA   . LEU   A 1 127 ? 2.645   -1.323  33.739  1.00 26.37 ? 505  LEU   A CA   1 
ATOM   754  C  C    . LEU   A 1 127 ? 2.705   0.110   33.227  1.00 22.72 ? 505  LEU   A C    1 
ATOM   755  O  O    . LEU   A 1 127 ? 3.430   0.403   32.268  1.00 20.65 ? 505  LEU   A O    1 
ATOM   756  C  CB   . LEU   A 1 127 ? 1.438   -2.054  33.149  1.00 22.93 ? 505  LEU   A CB   1 
ATOM   757  C  CG   . LEU   A 1 127 ? 1.402   -2.150  31.624  1.00 23.36 ? 505  LEU   A CG   1 
ATOM   758  C  CD1  . LEU   A 1 127 ? 2.606   -2.921  31.108  1.00 25.63 ? 505  LEU   A CD1  1 
ATOM   759  C  CD2  . LEU   A 1 127 ? 0.106   -2.789  31.150  1.00 19.57 ? 505  LEU   A CD2  1 
ATOM   760  N  N    . LEU   A 1 128 ? 1.955   1.019   33.854  1.00 22.64 ? 506  LEU   A N    1 
ATOM   761  C  CA   . LEU   A 1 128 ? 1.919   2.403   33.393  1.00 27.00 ? 506  LEU   A CA   1 
ATOM   762  C  C    . LEU   A 1 128 ? 3.147   3.191   33.832  1.00 26.39 ? 506  LEU   A C    1 
ATOM   763  O  O    . LEU   A 1 128 ? 3.572   4.110   33.123  1.00 23.58 ? 506  LEU   A O    1 
ATOM   764  C  CB   . LEU   A 1 128 ? 0.647   3.087   33.895  1.00 22.31 ? 506  LEU   A CB   1 
ATOM   765  C  CG   . LEU   A 1 128 ? -0.665  2.489   33.384  1.00 23.69 ? 506  LEU   A CG   1 
ATOM   766  C  CD1  . LEU   A 1 128 ? -1.828  2.904   34.270  1.00 23.10 ? 506  LEU   A CD1  1 
ATOM   767  C  CD2  . LEU   A 1 128 ? -0.910  2.903   31.943  1.00 26.21 ? 506  LEU   A CD2  1 
ATOM   768  N  N    . SER   A 1 129 ? 3.727   2.854   34.984  1.00 26.29 ? 507  SER   A N    1 
ATOM   769  C  CA   . SER   A 1 129 ? 4.904   3.558   35.476  1.00 26.71 ? 507  SER   A CA   1 
ATOM   770  C  C    . SER   A 1 129 ? 6.194   3.100   34.810  1.00 29.43 ? 507  SER   A C    1 
ATOM   771  O  O    . SER   A 1 129 ? 7.241   3.714   35.041  1.00 28.94 ? 507  SER   A O    1 
ATOM   772  C  CB   . SER   A 1 129 ? 5.029   3.383   36.992  1.00 26.66 ? 507  SER   A CB   1 
ATOM   773  O  OG   . SER   A 1 129 ? 5.457   2.072   37.320  1.00 32.07 ? 507  SER   A OG   1 
ATOM   774  N  N    . GLY   A 1 130 ? 6.148   2.048   33.996  1.00 27.19 ? 508  GLY   A N    1 
ATOM   775  C  CA   . GLY   A 1 130 ? 7.333   1.520   33.362  1.00 23.37 ? 508  GLY   A CA   1 
ATOM   776  C  C    . GLY   A 1 130 ? 8.027   0.414   34.125  1.00 24.12 ? 508  GLY   A C    1 
ATOM   777  O  O    . GLY   A 1 130 ? 8.974   -0.181  33.593  1.00 30.51 ? 508  GLY   A O    1 
ATOM   778  N  N    . GLN   A 1 131 ? 7.595   0.120   35.355  1.00 23.23 ? 509  GLN   A N    1 
ATOM   779  C  CA   . GLN   A 1 131 ? 8.170   -0.993  36.102  1.00 23.26 ? 509  GLN   A CA   1 
ATOM   780  C  C    . GLN   A 1 131 ? 7.945   -2.323  35.401  1.00 24.72 ? 509  GLN   A C    1 
ATOM   781  O  O    . GLN   A 1 131 ? 8.695   -3.276  35.642  1.00 28.10 ? 509  GLN   A O    1 
ATOM   782  C  CB   . GLN   A 1 131 ? 7.583   -1.044  37.513  1.00 23.24 ? 509  GLN   A CB   1 
ATOM   783  C  CG   . GLN   A 1 131 ? 8.009   0.106   38.408  1.00 24.59 ? 509  GLN   A CG   1 
ATOM   784  C  CD   . GLN   A 1 131 ? 7.112   0.259   39.619  1.00 35.49 ? 509  GLN   A CD   1 
ATOM   785  O  OE1  . GLN   A 1 131 ? 6.250   1.136   39.661  1.00 43.80 ? 509  GLN   A OE1  1 
ATOM   786  N  NE2  . GLN   A 1 131 ? 7.309   -0.599  40.613  1.00 36.17 ? 509  GLN   A NE2  1 
ATOM   787  N  N    . ALA   A 1 132 ? 6.930   -2.408  34.545  1.00 25.23 ? 510  ALA   A N    1 
ATOM   788  C  CA   . ALA   A 1 132 ? 6.666   -3.597  33.754  1.00 23.79 ? 510  ALA   A CA   1 
ATOM   789  C  C    . ALA   A 1 132 ? 6.337   -3.182  32.329  1.00 28.48 ? 510  ALA   A C    1 
ATOM   790  O  O    . ALA   A 1 132 ? 5.790   -2.102  32.089  1.00 31.49 ? 510  ALA   A O    1 
ATOM   791  C  CB   . ALA   A 1 132 ? 5.514   -4.421  34.338  1.00 22.72 ? 510  ALA   A CB   1 
ATOM   792  N  N    . ASP   A 1 133 ? 6.685   -4.051  31.383  1.00 24.29 ? 511  ASP   A N    1 
ATOM   793  C  CA   . ASP   A 1 133 ? 6.336   -3.854  29.984  1.00 23.69 ? 511  ASP   A CA   1 
ATOM   794  C  C    . ASP   A 1 133 ? 5.133   -4.682  29.557  1.00 27.08 ? 511  ASP   A C    1 
ATOM   795  O  O    . ASP   A 1 133 ? 4.564   -4.418  28.492  1.00 22.82 ? 511  ASP   A O    1 
ATOM   796  C  CB   . ASP   A 1 133 ? 7.532   -4.194  29.085  1.00 22.34 ? 511  ASP   A CB   1 
ATOM   797  C  CG   . ASP   A 1 133 ? 8.753   -3.352  29.398  1.00 27.60 ? 511  ASP   A CG   1 
ATOM   798  O  OD1  . ASP   A 1 133 ? 8.604   -2.123  29.554  1.00 28.12 ? 511  ASP   A OD1  1 
ATOM   799  O  OD2  . ASP   A 1 133 ? 9.861   -3.921  29.491  1.00 31.08 ? 511  ASP   A OD2  1 
ATOM   800  N  N    . MET   A 1 134 ? 4.726   -5.659  30.363  1.00 22.88 ? 512  MET   A N    1 
ATOM   801  C  CA   . MET   A 1 134 ? 3.632   -6.546  30.002  1.00 23.56 ? 512  MET   A CA   1 
ATOM   802  C  C    . MET   A 1 134 ? 3.084   -7.193  31.265  1.00 19.57 ? 512  MET   A C    1 
ATOM   803  O  O    . MET   A 1 134 ? 3.848   -7.567  32.158  1.00 22.44 ? 512  MET   A O    1 
ATOM   804  C  CB   . MET   A 1 134 ? 4.098   -7.620  29.013  1.00 21.25 ? 512  MET   A CB   1 
ATOM   805  C  CG   . MET   A 1 134 ? 2.975   -8.363  28.321  1.00 17.92 ? 512  MET   A CG   1 
ATOM   806  S  SD   . MET   A 1 134 ? 3.595   -9.615  27.184  1.00 25.97 ? 512  MET   A SD   1 
ATOM   807  C  CE   . MET   A 1 134 ? 4.065   -8.590  25.791  1.00 25.52 ? 512  MET   A CE   1 
ATOM   808  N  N    . ILE   A 1 135 ? 1.762   -7.315  31.333  1.00 21.04 ? 513  ILE   A N    1 
ATOM   809  C  CA   . ILE   A 1 135 ? 1.088   -8.017  32.420  1.00 20.78 ? 513  ILE   A CA   1 
ATOM   810  C  C    . ILE   A 1 135 ? 0.672   -9.388  31.909  1.00 18.48 ? 513  ILE   A C    1 
ATOM   811  O  O    . ILE   A 1 135 ? -0.096  -9.494  30.945  1.00 18.95 ? 513  ILE   A O    1 
ATOM   812  C  CB   . ILE   A 1 135 ? -0.128  -7.232  32.938  1.00 17.41 ? 513  ILE   A CB   1 
ATOM   813  C  CG1  . ILE   A 1 135 ? 0.263   -5.795  33.285  1.00 17.24 ? 513  ILE   A CG1  1 
ATOM   814  C  CG2  . ILE   A 1 135 ? -0.732  -7.928  34.149  1.00 14.52 ? 513  ILE   A CG2  1 
ATOM   815  C  CD1  . ILE   A 1 135 ? -0.863  -4.995  33.910  1.00 15.24 ? 513  ILE   A CD1  1 
ATOM   816  N  N    . VAL   A 1 136 ? 1.179   -10.435 32.545  1.00 17.03 ? 514  VAL   A N    1 
ATOM   817  C  CA   . VAL   A 1 136 ? 0.804   -11.813 32.231  1.00 18.88 ? 514  VAL   A CA   1 
ATOM   818  C  C    . VAL   A 1 136 ? 0.222   -12.397 33.513  1.00 17.51 ? 514  VAL   A C    1 
ATOM   819  O  O    . VAL   A 1 136 ? 0.944   -12.911 34.371  1.00 17.21 ? 514  VAL   A O    1 
ATOM   820  C  CB   . VAL   A 1 136 ? 1.983   -12.641 31.714  1.00 17.92 ? 514  VAL   A CB   1 
ATOM   821  C  CG1  . VAL   A 1 136 ? 1.525   -14.048 31.354  1.00 16.04 ? 514  VAL   A CG1  1 
ATOM   822  C  CG2  . VAL   A 1 136 ? 2.618   -11.962 30.509  1.00 15.55 ? 514  VAL   A CG2  1 
ATOM   823  N  N    . ALA   A 1 137 ? -1.096  -12.315 33.651  1.00 14.39 ? 515  ALA   A N    1 
ATOM   824  C  CA   . ALA   A 1 137 ? -1.776  -12.711 34.877  1.00 17.92 ? 515  ALA   A CA   1 
ATOM   825  C  C    . ALA   A 1 137 ? -3.254  -12.884 34.561  1.00 15.89 ? 515  ALA   A C    1 
ATOM   826  O  O    . ALA   A 1 137 ? -3.727  -12.444 33.504  1.00 14.05 ? 515  ALA   A O    1 
ATOM   827  C  CB   . ALA   A 1 137 ? -1.569  -11.667 35.989  1.00 15.68 ? 515  ALA   A CB   1 
ATOM   828  N  N    . PRO   A 1 138 ? -4.016  -13.538 35.451  1.00 15.45 ? 516  PRO   A N    1 
ATOM   829  C  CA   . PRO   A 1 138 ? -5.478  -13.545 35.289  1.00 15.72 ? 516  PRO   A CA   1 
ATOM   830  C  C    . PRO   A 1 138 ? -6.066  -12.156 35.482  1.00 17.70 ? 516  PRO   A C    1 
ATOM   831  O  O    . PRO   A 1 138 ? -6.729  -11.883 36.488  1.00 18.42 ? 516  PRO   A O    1 
ATOM   832  C  CB   . PRO   A 1 138 ? -5.951  -14.521 36.377  1.00 15.78 ? 516  PRO   A CB   1 
ATOM   833  C  CG   . PRO   A 1 138 ? -4.835  -14.557 37.372  1.00 13.28 ? 516  PRO   A CG   1 
ATOM   834  C  CD   . PRO   A 1 138 ? -3.583  -14.399 36.567  1.00 13.39 ? 516  PRO   A CD   1 
ATOM   835  N  N    . LEU   A 1 139 ? -5.829  -11.274 34.512  1.00 16.77 ? 517  LEU   A N    1 
ATOM   836  C  CA   . LEU   A 1 139 ? -6.190  -9.865  34.609  1.00 17.07 ? 517  LEU   A CA   1 
ATOM   837  C  C    . LEU   A 1 139 ? -7.499  -9.637  33.860  1.00 16.66 ? 517  LEU   A C    1 
ATOM   838  O  O    . LEU   A 1 139 ? -7.546  -9.747  32.630  1.00 14.26 ? 517  LEU   A O    1 
ATOM   839  C  CB   . LEU   A 1 139 ? -5.072  -8.989  34.048  1.00 15.99 ? 517  LEU   A CB   1 
ATOM   840  C  CG   . LEU   A 1 139 ? -5.196  -7.479  34.253  1.00 15.71 ? 517  LEU   A CG   1 
ATOM   841  C  CD1  . LEU   A 1 139 ? -5.038  -7.124  35.725  1.00 14.26 ? 517  LEU   A CD1  1 
ATOM   842  C  CD2  . LEU   A 1 139 ? -4.171  -6.743  33.403  1.00 13.27 ? 517  LEU   A CD2  1 
ATOM   843  N  N    . THR   A 1 140 ? -8.552  -9.305  34.601  1.00 15.49 ? 518  THR   A N    1 
ATOM   844  C  CA   . THR   A 1 140 ? -9.868  -9.123  34.004  1.00 15.53 ? 518  THR   A CA   1 
ATOM   845  C  C    . THR   A 1 140 ? -9.906  -7.873  33.132  1.00 16.01 ? 518  THR   A C    1 
ATOM   846  O  O    . THR   A 1 140 ? -9.390  -6.815  33.506  1.00 13.76 ? 518  THR   A O    1 
ATOM   847  C  CB   . THR   A 1 140 ? -10.934 -9.027  35.096  1.00 14.76 ? 518  THR   A CB   1 
ATOM   848  O  OG1  . THR   A 1 140 ? -10.954 -10.241 35.857  1.00 12.41 ? 518  THR   A OG1  1 
ATOM   849  C  CG2  . THR   A 1 140 ? -12.314 -8.788  34.490  1.00 11.84 ? 518  THR   A CG2  1 
ATOM   850  N  N    . ILE   A 1 141 ? -10.524 -8.002  31.962  1.00 12.75 ? 519  ILE   A N    1 
ATOM   851  C  CA   . ILE   A 1 141 ? -10.714 -6.877  31.054  1.00 18.40 ? 519  ILE   A CA   1 
ATOM   852  C  C    . ILE   A 1 141 ? -11.959 -6.108  31.482  1.00 18.19 ? 519  ILE   A C    1 
ATOM   853  O  O    . ILE   A 1 141 ? -13.066 -6.656  31.487  1.00 17.70 ? 519  ILE   A O    1 
ATOM   854  C  CB   . ILE   A 1 141 ? -10.841 -7.358  29.602  1.00 18.35 ? 519  ILE   A CB   1 
ATOM   855  C  CG1  . ILE   A 1 141 ? -9.655  -8.247  29.224  1.00 15.21 ? 519  ILE   A CG1  1 
ATOM   856  C  CG2  . ILE   A 1 141 ? -10.958 -6.174  28.655  1.00 18.36 ? 519  ILE   A CG2  1 
ATOM   857  C  CD1  . ILE   A 1 141 ? -9.839  -8.976  27.911  1.00 17.06 ? 519  ILE   A CD1  1 
ATOM   858  N  N    . ASN   A 1 142 ? -11.783 -4.838  31.841  1.00 15.94 ? 520  ASN   A N    1 
ATOM   859  C  CA   . ASN   A 1 142 ? -12.909 -3.975  32.164  1.00 17.31 ? 520  ASN   A CA   1 
ATOM   860  C  C    . ASN   A 1 142 ? -12.708 -2.615  31.510  1.00 21.10 ? 520  ASN   A C    1 
ATOM   861  O  O    . ASN   A 1 142 ? -11.625 -2.289  31.015  1.00 18.51 ? 520  ASN   A O    1 
ATOM   862  C  CB   . ASN   A 1 142 ? -13.114 -3.843  33.685  1.00 17.48 ? 520  ASN   A CB   1 
ATOM   863  C  CG   . ASN   A 1 142 ? -11.907 -3.258  34.408  1.00 24.35 ? 520  ASN   A CG   1 
ATOM   864  O  OD1  . ASN   A 1 142 ? -11.107 -2.518  33.835  1.00 18.57 ? 520  ASN   A OD1  1 
ATOM   865  N  ND2  . ASN   A 1 142 ? -11.779 -3.588  35.688  1.00 20.77 ? 520  ASN   A ND2  1 
ATOM   866  N  N    . ASN   A 1 143 ? -13.780 -1.818  31.516  1.00 24.88 ? 521  ASN   A N    1 
ATOM   867  C  CA   . ASN   A 1 143 ? -13.737 -0.496  30.897  1.00 21.90 ? 521  ASN   A CA   1 
ATOM   868  C  C    . ASN   A 1 143 ? -12.706 0.402   31.570  1.00 22.75 ? 521  ASN   A C    1 
ATOM   869  O  O    . ASN   A 1 143 ? -12.042 1.204   30.903  1.00 23.32 ? 521  ASN   A O    1 
ATOM   870  C  CB   . ASN   A 1 143 ? -15.126 0.144   30.950  1.00 24.70 ? 521  ASN   A CB   1 
ATOM   871  C  CG   . ASN   A 1 143 ? -15.112 1.614   30.572  1.00 26.11 ? 521  ASN   A CG   1 
ATOM   872  O  OD1  . ASN   A 1 143 ? -14.800 2.478   31.393  1.00 28.99 ? 521  ASN   A OD1  1 
ATOM   873  N  ND2  . ASN   A 1 143 ? -15.458 1.905   29.324  1.00 25.80 ? 521  ASN   A ND2  1 
ATOM   874  N  N    . GLU   A 1 144 ? -12.560 0.280   32.891  1.00 22.97 ? 522  GLU   A N    1 
ATOM   875  C  CA   . GLU   A 1 144 ? -11.636 1.141   33.624  1.00 23.93 ? 522  GLU   A CA   1 
ATOM   876  C  C    . GLU   A 1 144 ? -10.204 0.955   33.140  1.00 23.52 ? 522  GLU   A C    1 
ATOM   877  O  O    . GLU   A 1 144 ? -9.503  1.930   32.845  1.00 24.38 ? 522  GLU   A O    1 
ATOM   878  C  CB   . GLU   A 1 144 ? -11.738 0.858   35.124  1.00 24.16 ? 522  GLU   A CB   1 
ATOM   879  C  CG   . GLU   A 1 144 ? -13.050 1.295   35.760  1.00 24.99 ? 522  GLU   A CG   1 
ATOM   880  C  CD   . GLU   A 1 144 ? -14.136 0.240   35.659  1.00 28.75 ? 522  GLU   A CD   1 
ATOM   881  O  OE1  . GLU   A 1 144 ? -13.913 -0.791  34.989  1.00 22.82 ? 522  GLU   A OE1  1 
ATOM   882  O  OE2  . GLU   A 1 144 ? -15.219 0.447   36.244  1.00 32.58 ? 522  GLU   A OE2  1 
ATOM   883  N  N    . ARG   A 1 145 ? -9.753  -0.297  33.043  1.00 22.32 ? 523  ARG   A N    1 
ATOM   884  C  CA   . ARG   A 1 145 ? -8.360  -0.550  32.689  1.00 22.04 ? 523  ARG   A CA   1 
ATOM   885  C  C    . ARG   A 1 145 ? -8.104  -0.309  31.207  1.00 21.90 ? 523  ARG   A C    1 
ATOM   886  O  O    . ARG   A 1 145 ? -7.048  0.214   30.833  1.00 22.36 ? 523  ARG   A O    1 
ATOM   887  C  CB   . ARG   A 1 145 ? -7.972  -1.976  33.076  1.00 22.00 ? 523  ARG   A CB   1 
ATOM   888  C  CG   . ARG   A 1 145 ? -7.951  -2.226  34.573  1.00 21.32 ? 523  ARG   A CG   1 
ATOM   889  C  CD   . ARG   A 1 145 ? -7.990  -3.712  34.882  1.00 20.64 ? 523  ARG   A CD   1 
ATOM   890  N  NE   . ARG   A 1 145 ? -7.838  -3.974  36.308  1.00 20.76 ? 523  ARG   A NE   1 
ATOM   891  C  CZ   . ARG   A 1 145 ? -8.030  -5.156  36.877  1.00 20.26 ? 523  ARG   A CZ   1 
ATOM   892  N  NH1  . ARG   A 1 145 ? -8.386  -6.215  36.168  1.00 19.35 ? 523  ARG   A NH1  1 
ATOM   893  N  NH2  . ARG   A 1 145 ? -7.860  -5.279  38.190  1.00 20.80 ? 523  ARG   A NH2  1 
ATOM   894  N  N    . ALA   A 1 146 ? -9.057  -0.679  30.346  1.00 21.36 ? 524  ALA   A N    1 
ATOM   895  C  CA   . ALA   A 1 146 ? -8.874  -0.500  28.910  1.00 21.27 ? 524  ALA   A CA   1 
ATOM   896  C  C    . ALA   A 1 146 ? -8.749  0.965   28.518  1.00 23.04 ? 524  ALA   A C    1 
ATOM   897  O  O    . ALA   A 1 146 ? -8.278  1.264   27.415  1.00 27.98 ? 524  ALA   A O    1 
ATOM   898  C  CB   . ALA   A 1 146 ? -10.032 -1.144  28.147  1.00 20.59 ? 524  ALA   A CB   1 
ATOM   899  N  N    . GLN   A 1 147 ? -9.160  1.884   29.394  1.00 23.57 ? 525  GLN   A N    1 
ATOM   900  C  CA   . GLN   A 1 147 ? -9.006  3.307   29.126  1.00 25.33 ? 525  GLN   A CA   1 
ATOM   901  C  C    . GLN   A 1 147 ? -7.549  3.750   29.171  1.00 28.08 ? 525  GLN   A C    1 
ATOM   902  O  O    . GLN   A 1 147 ? -7.207  4.775   28.570  1.00 31.05 ? 525  GLN   A O    1 
ATOM   903  C  CB   . GLN   A 1 147 ? -9.828  4.113   30.135  1.00 26.12 ? 525  GLN   A CB   1 
ATOM   904  C  CG   . GLN   A 1 147 ? -10.448 5.382   29.582  1.00 34.08 ? 525  GLN   A CG   1 
ATOM   905  C  CD   . GLN   A 1 147 ? -11.587 5.887   30.446  1.00 45.66 ? 525  GLN   A CD   1 
ATOM   906  O  OE1  . GLN   A 1 147 ? -12.541 5.160   30.720  1.00 41.66 ? 525  GLN   A OE1  1 
ATOM   907  N  NE2  . GLN   A 1 147 ? -11.492 7.138   30.880  1.00 46.84 ? 525  GLN   A NE2  1 
ATOM   908  N  N    . TYR   A 1 148 ? -6.687  3.004   29.860  1.00 24.89 ? 526  TYR   A N    1 
ATOM   909  C  CA   . TYR   A 1 148 ? -5.292  3.382   30.037  1.00 28.99 ? 526  TYR   A CA   1 
ATOM   910  C  C    . TYR   A 1 148 ? -4.299  2.405   29.427  1.00 34.60 ? 526  TYR   A C    1 
ATOM   911  O  O    . TYR   A 1 148 ? -3.189  2.817   29.082  1.00 35.00 ? 526  TYR   A O    1 
ATOM   912  C  CB   . TYR   A 1 148 ? -4.970  3.539   31.531  1.00 27.26 ? 526  TYR   A CB   1 
ATOM   913  C  CG   . TYR   A 1 148 ? -5.615  4.748   32.167  1.00 31.72 ? 526  TYR   A CG   1 
ATOM   914  C  CD1  . TYR   A 1 148 ? -6.898  4.679   32.695  1.00 29.62 ? 526  TYR   A CD1  1 
ATOM   915  C  CD2  . TYR   A 1 148 ? -4.941  5.959   32.241  1.00 29.85 ? 526  TYR   A CD2  1 
ATOM   916  C  CE1  . TYR   A 1 148 ? -7.491  5.784   33.278  1.00 29.50 ? 526  TYR   A CE1  1 
ATOM   917  C  CE2  . TYR   A 1 148 ? -5.524  7.068   32.822  1.00 37.15 ? 526  TYR   A CE2  1 
ATOM   918  C  CZ   . TYR   A 1 148 ? -6.799  6.975   33.339  1.00 34.21 ? 526  TYR   A CZ   1 
ATOM   919  O  OH   . TYR   A 1 148 ? -7.385  8.077   33.919  1.00 39.50 ? 526  TYR   A OH   1 
ATOM   920  N  N    . ILE   A 1 149 ? -4.656  1.128   29.289  1.00 26.46 ? 527  ILE   A N    1 
ATOM   921  C  CA   . ILE   A 1 149 ? -3.759  0.119   28.745  1.00 27.18 ? 527  ILE   A CA   1 
ATOM   922  C  C    . ILE   A 1 149 ? -4.442  -0.573  27.572  1.00 29.37 ? 527  ILE   A C    1 
ATOM   923  O  O    . ILE   A 1 149 ? -5.631  -0.386  27.312  1.00 30.18 ? 527  ILE   A O    1 
ATOM   924  C  CB   . ILE   A 1 149 ? -3.331  -0.924  29.799  1.00 27.75 ? 527  ILE   A CB   1 
ATOM   925  C  CG1  . ILE   A 1 149 ? -4.543  -1.736  30.264  1.00 25.94 ? 527  ILE   A CG1  1 
ATOM   926  C  CG2  . ILE   A 1 149 ? -2.628  -0.248  30.965  1.00 29.14 ? 527  ILE   A CG2  1 
ATOM   927  C  CD1  . ILE   A 1 149 ? -4.185  -3.076  30.867  1.00 24.32 ? 527  ILE   A CD1  1 
ATOM   928  N  N    . GLU   A 1 150 ? -3.663  -1.385  26.865  1.00 30.53 ? 528  GLU   A N    1 
ATOM   929  C  CA   . GLU   A 1 150 ? -4.159  -2.192  25.760  1.00 23.15 ? 528  GLU   A CA   1 
ATOM   930  C  C    . GLU   A 1 150 ? -4.332  -3.631  26.223  1.00 24.26 ? 528  GLU   A C    1 
ATOM   931  O  O    . GLU   A 1 150 ? -3.401  -4.228  26.773  1.00 25.90 ? 528  GLU   A O    1 
ATOM   932  C  CB   . GLU   A 1 150 ? -3.204  -2.133  24.567  1.00 35.35 ? 528  GLU   A CB   1 
ATOM   933  C  CG   . GLU   A 1 150 ? -3.418  -3.242  23.545  1.00 33.86 ? 528  GLU   A CG   1 
ATOM   934  C  CD   . GLU   A 1 150 ? -4.452  -2.881  22.495  1.00 33.65 ? 528  GLU   A CD   1 
ATOM   935  O  OE1  . GLU   A 1 150 ? -4.962  -1.741  22.525  1.00 46.15 ? 528  GLU   A OE1  1 
ATOM   936  O  OE2  . GLU   A 1 150 ? -4.755  -3.738  21.638  1.00 34.97 ? 528  GLU   A OE2  1 
ATOM   937  N  N    . PHE   A 1 151 ? -5.523  -4.178  26.011  1.00 30.36 ? 529  PHE   A N    1 
ATOM   938  C  CA   . PHE   A 1 151 ? -5.807  -5.573  26.307  1.00 17.88 ? 529  PHE   A CA   1 
ATOM   939  C  C    . PHE   A 1 151 ? -5.748  -6.390  25.026  1.00 22.70 ? 529  PHE   A C    1 
ATOM   940  O  O    . PHE   A 1 151 ? -6.247  -5.962  23.981  1.00 24.17 ? 529  PHE   A O    1 
ATOM   941  C  CB   . PHE   A 1 151 ? -7.185  -5.739  26.950  1.00 17.56 ? 529  PHE   A CB   1 
ATOM   942  C  CG   . PHE   A 1 151 ? -7.212  -5.452  28.421  1.00 18.35 ? 529  PHE   A CG   1 
ATOM   943  C  CD1  . PHE   A 1 151 ? -6.568  -6.291  29.316  1.00 20.15 ? 529  PHE   A CD1  1 
ATOM   944  C  CD2  . PHE   A 1 151 ? -7.899  -4.355  28.913  1.00 19.53 ? 529  PHE   A CD2  1 
ATOM   945  C  CE1  . PHE   A 1 151 ? -6.598  -6.032  30.673  1.00 19.57 ? 529  PHE   A CE1  1 
ATOM   946  C  CE2  . PHE   A 1 151 ? -7.934  -4.093  30.267  1.00 19.37 ? 529  PHE   A CE2  1 
ATOM   947  C  CZ   . PHE   A 1 151 ? -7.283  -4.932  31.149  1.00 20.33 ? 529  PHE   A CZ   1 
ATOM   948  N  N    . SER   A 1 152 ? -5.134  -7.565  25.111  1.00 17.84 ? 530  SER   A N    1 
ATOM   949  C  CA   . SER   A 1 152 ? -5.242  -8.516  24.021  1.00 17.86 ? 530  SER   A CA   1 
ATOM   950  C  C    . SER   A 1 152 ? -6.645  -9.117  24.004  1.00 16.10 ? 530  SER   A C    1 
ATOM   951  O  O    . SER   A 1 152 ? -7.463  -8.885  24.900  1.00 17.01 ? 530  SER   A O    1 
ATOM   952  C  CB   . SER   A 1 152 ? -4.193  -9.619  24.160  1.00 17.09 ? 530  SER   A CB   1 
ATOM   953  O  OG   . SER   A 1 152 ? -4.523  -10.505 25.216  1.00 16.34 ? 530  SER   A OG   1 
ATOM   954  N  N    . LYS   A 1 153 ? -6.929  -9.888  22.960  1.00 15.82 ? 531  LYS   A N    1 
ATOM   955  C  CA   . LYS   A 1 153 ? -8.136  -10.692 22.972  1.00 16.70 ? 531  LYS   A CA   1 
ATOM   956  C  C    . LYS   A 1 153 ? -8.072  -11.661 24.152  1.00 17.15 ? 531  LYS   A C    1 
ATOM   957  O  O    . LYS   A 1 153 ? -6.984  -12.087 24.552  1.00 15.27 ? 531  LYS   A O    1 
ATOM   958  C  CB   . LYS   A 1 153 ? -8.291  -11.452 21.658  1.00 15.23 ? 531  LYS   A CB   1 
ATOM   959  C  CG   . LYS   A 1 153 ? -8.703  -10.578 20.485  1.00 15.46 ? 531  LYS   A CG   1 
ATOM   960  C  CD   . LYS   A 1 153 ? -10.131 -10.080 20.642  1.00 20.74 ? 531  LYS   A CD   1 
ATOM   961  C  CE   . LYS   A 1 153 ? -10.591 -9.324  19.406  1.00 16.10 ? 531  LYS   A CE   1 
ATOM   962  N  NZ   . LYS   A 1 153 ? -9.897  -8.013  19.267  1.00 17.36 ? 531  LYS   A NZ   1 
ATOM   963  N  N    . PRO   A 1 154 ? -9.214  -12.008 24.742  1.00 16.14 ? 532  PRO   A N    1 
ATOM   964  C  CA   . PRO   A 1 154 ? -9.189  -12.834 25.957  1.00 16.17 ? 532  PRO   A CA   1 
ATOM   965  C  C    . PRO   A 1 154 ? -8.513  -14.174 25.710  1.00 14.68 ? 532  PRO   A C    1 
ATOM   966  O  O    . PRO   A 1 154 ? -8.812  -14.871 24.738  1.00 14.69 ? 532  PRO   A O    1 
ATOM   967  C  CB   . PRO   A 1 154 ? -10.674 -13.004 26.302  1.00 15.25 ? 532  PRO   A CB   1 
ATOM   968  C  CG   . PRO   A 1 154 ? -11.365 -11.884 25.602  1.00 14.51 ? 532  PRO   A CG   1 
ATOM   969  C  CD   . PRO   A 1 154 ? -10.587 -11.652 24.346  1.00 14.63 ? 532  PRO   A CD   1 
ATOM   970  N  N    . PHE   A 1 155 ? -7.576  -14.524 26.592  1.00 14.97 ? 533  PHE   A N    1 
ATOM   971  C  CA   . PHE   A 1 155 ? -6.990  -15.855 26.560  1.00 16.84 ? 533  PHE   A CA   1 
ATOM   972  C  C    . PHE   A 1 155 ? -7.726  -16.837 27.460  1.00 19.73 ? 533  PHE   A C    1 
ATOM   973  O  O    . PHE   A 1 155 ? -7.467  -18.041 27.379  1.00 18.20 ? 533  PHE   A O    1 
ATOM   974  C  CB   . PHE   A 1 155 ? -5.495  -15.805 26.927  1.00 15.71 ? 533  PHE   A CB   1 
ATOM   975  C  CG   . PHE   A 1 155 ? -5.209  -15.405 28.354  1.00 15.95 ? 533  PHE   A CG   1 
ATOM   976  C  CD1  . PHE   A 1 155 ? -5.213  -16.347 29.373  1.00 16.20 ? 533  PHE   A CD1  1 
ATOM   977  C  CD2  . PHE   A 1 155 ? -4.895  -14.092 28.669  1.00 18.11 ? 533  PHE   A CD2  1 
ATOM   978  C  CE1  . PHE   A 1 155 ? -4.938  -15.983 30.677  1.00 19.04 ? 533  PHE   A CE1  1 
ATOM   979  C  CE2  . PHE   A 1 155 ? -4.616  -13.723 29.974  1.00 18.61 ? 533  PHE   A CE2  1 
ATOM   980  C  CZ   . PHE   A 1 155 ? -4.635  -14.671 30.978  1.00 18.50 ? 533  PHE   A CZ   1 
ATOM   981  N  N    . LYS   A 1 156 ? -8.642  -16.359 28.297  1.00 16.73 ? 534  LYS   A N    1 
ATOM   982  C  CA   . LYS   A 1 156 ? -9.468  -17.228 29.121  1.00 17.03 ? 534  LYS   A CA   1 
ATOM   983  C  C    . LYS   A 1 156 ? -10.861 -16.631 29.216  1.00 19.62 ? 534  LYS   A C    1 
ATOM   984  O  O    . LYS   A 1 156 ? -11.007 -15.435 29.488  1.00 20.13 ? 534  LYS   A O    1 
ATOM   985  C  CB   . LYS   A 1 156 ? -8.871  -17.408 30.522  1.00 17.00 ? 534  LYS   A CB   1 
ATOM   986  C  CG   . LYS   A 1 156 ? -9.782  -18.141 31.493  1.00 18.06 ? 534  LYS   A CG   1 
ATOM   987  C  CD   . LYS   A 1 156 ? -10.022 -19.576 31.053  1.00 24.42 ? 534  LYS   A CD   1 
ATOM   988  C  CE   . LYS   A 1 156 ? -10.931 -20.305 32.028  1.00 23.90 ? 534  LYS   A CE   1 
ATOM   989  N  NZ   . LYS   A 1 156 ? -11.204 -21.701 31.591  1.00 18.89 ? 534  LYS   A NZ   1 
ATOM   990  N  N    . TYR   A 1 157 ? -11.875 -17.456 28.979  1.00 17.82 ? 535  TYR   A N    1 
ATOM   991  C  CA   . TYR   A 1 157 ? -13.269 -17.055 29.118  1.00 18.54 ? 535  TYR   A CA   1 
ATOM   992  C  C    . TYR   A 1 157 ? -13.830 -17.702 30.375  1.00 21.30 ? 535  TYR   A C    1 
ATOM   993  O  O    . TYR   A 1 157 ? -13.839 -18.932 30.494  1.00 20.35 ? 535  TYR   A O    1 
ATOM   994  C  CB   . TYR   A 1 157 ? -14.086 -17.451 27.889  1.00 20.63 ? 535  TYR   A CB   1 
ATOM   995  C  CG   . TYR   A 1 157 ? -13.791 -16.609 26.668  1.00 19.91 ? 535  TYR   A CG   1 
ATOM   996  C  CD1  . TYR   A 1 157 ? -12.756 -16.942 25.804  1.00 17.28 ? 535  TYR   A CD1  1 
ATOM   997  C  CD2  . TYR   A 1 157 ? -14.544 -15.478 26.382  1.00 19.24 ? 535  TYR   A CD2  1 
ATOM   998  C  CE1  . TYR   A 1 157 ? -12.482 -16.174 24.688  1.00 16.72 ? 535  TYR   A CE1  1 
ATOM   999  C  CE2  . TYR   A 1 157 ? -14.277 -14.703 25.268  1.00 17.23 ? 535  TYR   A CE2  1 
ATOM   1000 C  CZ   . TYR   A 1 157 ? -13.245 -15.057 24.425  1.00 20.13 ? 535  TYR   A CZ   1 
ATOM   1001 O  OH   . TYR   A 1 157 ? -12.971 -14.293 23.313  1.00 24.04 ? 535  TYR   A OH   1 
ATOM   1002 N  N    . GLN   A 1 158 ? -14.284 -16.874 31.313  1.00 20.93 ? 536  GLN   A N    1 
ATOM   1003 C  CA   . GLN   A 1 158 ? -14.834 -17.367 32.569  1.00 19.74 ? 536  GLN   A CA   1 
ATOM   1004 C  C    . GLN   A 1 158 ? -15.905 -16.414 33.085  1.00 20.82 ? 536  GLN   A C    1 
ATOM   1005 O  O    . GLN   A 1 158 ? -16.692 -15.868 32.304  1.00 22.51 ? 536  GLN   A O    1 
ATOM   1006 C  CB   . GLN   A 1 158 ? -13.732 -17.534 33.619  1.00 18.75 ? 536  GLN   A CB   1 
ATOM   1007 C  CG   . GLN   A 1 158 ? -12.903 -16.278 33.822  1.00 18.70 ? 536  GLN   A CG   1 
ATOM   1008 C  CD   . GLN   A 1 158 ? -12.659 -15.992 35.284  1.00 18.88 ? 536  GLN   A CD   1 
ATOM   1009 O  OE1  . GLN   A 1 158 ? -12.463 -16.901 36.088  1.00 17.18 ? 536  GLN   A OE1  1 
ATOM   1010 N  NE2  . GLN   A 1 158 ? -12.710 -14.717 35.647  1.00 16.27 ? 536  GLN   A NE2  1 
ATOM   1011 N  N    . GLY   A 1 159 ? -15.944 -16.207 34.395  1.00 21.22 ? 537  GLY   A N    1 
ATOM   1012 C  CA   . GLY   A 1 159 ? -16.876 -15.255 34.957  1.00 18.22 ? 537  GLY   A CA   1 
ATOM   1013 C  C    . GLY   A 1 159 ? -16.733 -15.152 36.457  1.00 21.81 ? 537  GLY   A C    1 
ATOM   1014 O  O    . GLY   A 1 159 ? -15.709 -15.531 37.030  1.00 26.04 ? 537  GLY   A O    1 
ATOM   1015 N  N    . LEU   A 1 160 ? -17.780 -14.628 37.088  1.00 17.96 ? 538  LEU   A N    1 
ATOM   1016 C  CA   . LEU   A 1 160 ? -17.824 -14.429 38.529  1.00 22.56 ? 538  LEU   A CA   1 
ATOM   1017 C  C    . LEU   A 1 160 ? -18.767 -15.441 39.165  1.00 23.50 ? 538  LEU   A C    1 
ATOM   1018 O  O    . LEU   A 1 160 ? -19.832 -15.743 38.618  1.00 24.38 ? 538  LEU   A O    1 
ATOM   1019 C  CB   . LEU   A 1 160 ? -18.279 -13.005 38.871  1.00 21.79 ? 538  LEU   A CB   1 
ATOM   1020 C  CG   . LEU   A 1 160 ? -17.226 -11.905 39.050  1.00 22.87 ? 538  LEU   A CG   1 
ATOM   1021 C  CD1  . LEU   A 1 160 ? -16.117 -12.004 38.012  1.00 20.19 ? 538  LEU   A CD1  1 
ATOM   1022 C  CD2  . LEU   A 1 160 ? -17.885 -10.532 38.998  1.00 23.48 ? 538  LEU   A CD2  1 
ATOM   1023 N  N    . THR   A 1 161 ? -18.369 -15.961 40.324  1.00 24.72 ? 539  THR   A N    1 
ATOM   1024 C  CA   . THR   A 1 161 ? -19.198 -16.889 41.080  1.00 26.33 ? 539  THR   A CA   1 
ATOM   1025 C  C    . THR   A 1 161 ? -18.845 -16.750 42.557  1.00 27.88 ? 539  THR   A C    1 
ATOM   1026 O  O    . THR   A 1 161 ? -17.990 -15.946 42.939  1.00 25.32 ? 539  THR   A O    1 
ATOM   1027 C  CB   . THR   A 1 161 ? -19.023 -18.328 40.580  1.00 24.02 ? 539  THR   A CB   1 
ATOM   1028 O  OG1  . THR   A 1 161 ? -20.068 -19.152 41.113  1.00 30.53 ? 539  THR   A OG1  1 
ATOM   1029 C  CG2  . THR   A 1 161 ? -17.672 -18.885 41.002  1.00 25.08 ? 539  THR   A CG2  1 
ATOM   1030 N  N    . ILE   A 1 162 ? -19.514 -17.543 43.392  1.00 25.41 ? 540  ILE   A N    1 
ATOM   1031 C  CA   . ILE   A 1 162 ? -19.418 -17.427 44.842  1.00 28.11 ? 540  ILE   A CA   1 
ATOM   1032 C  C    . ILE   A 1 162 ? -18.897 -18.739 45.411  1.00 28.59 ? 540  ILE   A C    1 
ATOM   1033 O  O    . ILE   A 1 162 ? -19.427 -19.811 45.097  1.00 26.17 ? 540  ILE   A O    1 
ATOM   1034 C  CB   . ILE   A 1 162 ? -20.778 -17.065 45.467  1.00 27.58 ? 540  ILE   A CB   1 
ATOM   1035 C  CG1  . ILE   A 1 162 ? -21.350 -15.811 44.804  1.00 31.27 ? 540  ILE   A CG1  1 
ATOM   1036 C  CG2  . ILE   A 1 162 ? -20.640 -16.871 46.969  1.00 23.33 ? 540  ILE   A CG2  1 
ATOM   1037 C  CD1  . ILE   A 1 162 ? -22.777 -15.514 45.193  1.00 31.57 ? 540  ILE   A CD1  1 
ATOM   1038 N  N    . LEU   A 1 163 ? -17.867 -18.650 46.249  1.00 27.13 ? 541  LEU   A N    1 
ATOM   1039 C  CA   . LEU   A 1 163 ? -17.318 -19.797 46.959  1.00 28.31 ? 541  LEU   A CA   1 
ATOM   1040 C  C    . LEU   A 1 163 ? -17.787 -19.775 48.407  1.00 30.49 ? 541  LEU   A C    1 
ATOM   1041 O  O    . LEU   A 1 163 ? -17.769 -18.726 49.059  1.00 29.35 ? 541  LEU   A O    1 
ATOM   1042 C  CB   . LEU   A 1 163 ? -15.789 -19.793 46.907  1.00 29.06 ? 541  LEU   A CB   1 
ATOM   1043 C  CG   . LEU   A 1 163 ? -15.078 -21.006 47.511  1.00 30.66 ? 541  LEU   A CG   1 
ATOM   1044 C  CD1  . LEU   A 1 163 ? -14.883 -22.093 46.465  1.00 32.46 ? 541  LEU   A CD1  1 
ATOM   1045 C  CD2  . LEU   A 1 163 ? -13.745 -20.600 48.124  1.00 26.69 ? 541  LEU   A CD2  1 
ATOM   1046 N  N    . VAL   A 1 164 ? -18.210 -20.938 48.908  1.00 34.51 ? 542  VAL   A N    1 
ATOM   1047 C  CA   . VAL   A 1 164 ? -18.729 -21.064 50.264  1.00 35.98 ? 542  VAL   A CA   1 
ATOM   1048 C  C    . VAL   A 1 164 ? -18.244 -22.372 50.876  1.00 34.73 ? 542  VAL   A C    1 
ATOM   1049 O  O    . VAL   A 1 164 ? -17.798 -23.286 50.180  1.00 30.65 ? 542  VAL   A O    1 
ATOM   1050 C  CB   . VAL   A 1 164 ? -20.274 -21.010 50.314  1.00 38.25 ? 542  VAL   A CB   1 
ATOM   1051 C  CG1  . VAL   A 1 164 ? -20.785 -19.624 49.947  1.00 33.83 ? 542  VAL   A CG1  1 
ATOM   1052 C  CG2  . VAL   A 1 164 ? -20.870 -22.067 49.396  1.00 36.00 ? 542  VAL   A CG2  1 
ATOM   1053 N  N    . LYS   A 1 165 ? -18.340 -22.446 52.201  1.00 37.13 ? 543  LYS   A N    1 
ATOM   1054 C  CA   . LYS   A 1 165 ? -18.070 -23.691 52.906  1.00 37.75 ? 543  LYS   A CA   1 
ATOM   1055 C  C    . LYS   A 1 165 ? -19.180 -24.696 52.628  1.00 38.69 ? 543  LYS   A C    1 
ATOM   1056 O  O    . LYS   A 1 165 ? -20.362 -24.343 52.594  1.00 40.46 ? 543  LYS   A O    1 
ATOM   1057 C  CB   . LYS   A 1 165 ? -17.954 -23.432 54.409  1.00 37.32 ? 543  LYS   A CB   1 
ATOM   1058 C  CG   . LYS   A 1 165 ? -17.765 -24.680 55.258  1.00 41.76 ? 543  LYS   A CG   1 
ATOM   1059 C  CD   . LYS   A 1 165 ? -16.380 -25.272 55.067  1.00 47.83 ? 543  LYS   A CD   1 
ATOM   1060 C  CE   . LYS   A 1 165 ? -15.673 -25.459 56.399  1.00 57.84 ? 543  LYS   A CE   1 
ATOM   1061 N  NZ   . LYS   A 1 165 ? -14.194 -25.491 56.239  1.00 54.41 ? 543  LYS   A NZ   1 
ATOM   1062 N  N    . LYS   A 1 166 ? -18.795 -25.954 52.413  1.00 40.32 ? 544  LYS   A N    1 
ATOM   1063 C  CA   . LYS   A 1 166 ? -19.776 -26.994 52.127  1.00 43.34 ? 544  LYS   A CA   1 
ATOM   1064 C  C    . LYS   A 1 166 ? -20.765 -27.119 53.279  1.00 43.72 ? 544  LYS   A C    1 
ATOM   1065 O  O    . LYS   A 1 166 ? -20.373 -27.280 54.438  1.00 46.94 ? 544  LYS   A O    1 
ATOM   1066 C  CB   . LYS   A 1 166 ? -19.080 -28.331 51.875  1.00 44.13 ? 544  LYS   A CB   1 
ATOM   1067 C  CG   . LYS   A 1 166 ? -20.003 -29.402 51.315  1.00 44.79 ? 544  LYS   A CG   1 
ATOM   1068 C  CD   . LYS   A 1 166 ? -19.229 -30.476 50.570  1.00 46.04 ? 544  LYS   A CD   1 
ATOM   1069 C  CE   . LYS   A 1 166 ? -20.005 -31.783 50.527  1.00 48.73 ? 544  LYS   A CE   1 
ATOM   1070 N  NZ   . LYS   A 1 166 ? -19.559 -32.724 51.592  1.00 63.03 ? 544  LYS   A NZ   1 
ATOM   1071 N  N    . GLY   A 1 167 ? -22.056 -27.040 52.952  1.00 43.64 ? 545  GLY   A N    1 
ATOM   1072 C  CA   . GLY   A 1 167 ? -23.123 -26.977 53.926  1.00 45.25 ? 545  GLY   A CA   1 
ATOM   1073 C  C    . GLY   A 1 167 ? -23.810 -25.626 53.973  1.00 48.85 ? 545  GLY   A C    1 
ATOM   1074 O  O    . GLY   A 1 167 ? -25.017 -25.562 54.237  1.00 54.78 ? 545  GLY   A O    1 
ATOM   1075 N  N    . THR   A 1 168 ? -23.065 -24.550 53.727  1.00 51.71 ? 546  THR   A N    1 
ATOM   1076 C  CA   . THR   A 1 168 ? -23.664 -23.227 53.607  1.00 51.50 ? 546  THR   A CA   1 
ATOM   1077 C  C    . THR   A 1 168 ? -24.601 -23.197 52.409  1.00 48.10 ? 546  THR   A C    1 
ATOM   1078 O  O    . THR   A 1 168 ? -24.192 -23.492 51.281  1.00 45.14 ? 546  THR   A O    1 
ATOM   1079 C  CB   . THR   A 1 168 ? -22.574 -22.165 53.462  1.00 43.64 ? 546  THR   A CB   1 
ATOM   1080 O  OG1  . THR   A 1 168 ? -21.848 -22.050 54.692  1.00 35.89 ? 546  THR   A OG1  1 
ATOM   1081 C  CG2  . THR   A 1 168 ? -23.184 -20.816 53.108  1.00 45.50 ? 546  THR   A CG2  1 
ATOM   1082 N  N    . ARG   A 1 169 ? -25.860 -22.848 52.652  1.00 41.53 ? 663  ARG   A N    1 
ATOM   1083 C  CA   . ARG   A 1 169 ? -26.905 -22.897 51.633  1.00 47.52 ? 663  ARG   A CA   1 
ATOM   1084 C  C    . ARG   A 1 169 ? -27.311 -21.473 51.270  1.00 48.34 ? 663  ARG   A C    1 
ATOM   1085 O  O    . ARG   A 1 169 ? -28.087 -20.836 51.989  1.00 51.32 ? 663  ARG   A O    1 
ATOM   1086 C  CB   . ARG   A 1 169 ? -28.102 -23.705 52.126  1.00 49.42 ? 663  ARG   A CB   1 
ATOM   1087 N  N    . ILE   A 1 170 ? -26.779 -20.973 50.157  1.00 40.78 ? 664  ILE   A N    1 
ATOM   1088 C  CA   . ILE   A 1 170 ? -27.233 -19.723 49.560  1.00 43.92 ? 664  ILE   A CA   1 
ATOM   1089 C  C    . ILE   A 1 170 ? -27.422 -19.962 48.068  1.00 45.19 ? 664  ILE   A C    1 
ATOM   1090 O  O    . ILE   A 1 170 ? -26.663 -20.717 47.450  1.00 41.16 ? 664  ILE   A O    1 
ATOM   1091 C  CB   . ILE   A 1 170 ? -26.262 -18.546 49.824  1.00 43.13 ? 664  ILE   A CB   1 
ATOM   1092 C  CG1  . ILE   A 1 170 ? -24.910 -18.750 49.138  1.00 40.01 ? 664  ILE   A CG1  1 
ATOM   1093 C  CG2  . ILE   A 1 170 ? -26.065 -18.323 51.318  1.00 45.11 ? 664  ILE   A CG2  1 
ATOM   1094 C  CD1  . ILE   A 1 170 ? -24.688 -17.795 47.983  1.00 45.35 ? 664  ILE   A CD1  1 
ATOM   1095 N  N    . THR   A 1 171 ? -28.455 -19.338 47.496  1.00 44.99 ? 665  THR   A N    1 
ATOM   1096 C  CA   . THR   A 1 171 ? -28.787 -19.595 46.097  1.00 44.77 ? 665  THR   A CA   1 
ATOM   1097 C  C    . THR   A 1 171 ? -27.740 -19.009 45.158  1.00 50.00 ? 665  THR   A C    1 
ATOM   1098 O  O    . THR   A 1 171 ? -27.325 -19.666 44.195  1.00 50.36 ? 665  THR   A O    1 
ATOM   1099 C  CB   . THR   A 1 171 ? -30.169 -19.030 45.769  1.00 43.86 ? 665  THR   A CB   1 
ATOM   1100 O  OG1  . THR   A 1 171 ? -30.043 -17.666 45.345  1.00 36.55 ? 665  THR   A OG1  1 
ATOM   1101 C  CG2  . THR   A 1 171 ? -31.080 -19.101 46.986  1.00 46.01 ? 665  THR   A CG2  1 
ATOM   1102 N  N    . GLY   A 1 172 ? -27.307 -17.779 45.414  1.00 56.51 ? 666  GLY   A N    1 
ATOM   1103 C  CA   . GLY   A 1 172 ? -26.335 -17.127 44.561  1.00 46.72 ? 666  GLY   A CA   1 
ATOM   1104 C  C    . GLY   A 1 172 ? -26.302 -15.626 44.751  1.00 47.66 ? 666  GLY   A C    1 
ATOM   1105 O  O    . GLY   A 1 172 ? -26.449 -15.133 45.874  1.00 51.87 ? 666  GLY   A O    1 
ATOM   1106 N  N    . ILE   A 1 173 ? -26.120 -14.886 43.654  1.00 40.53 ? 667  ILE   A N    1 
ATOM   1107 C  CA   . ILE   A 1 173 ? -26.019 -13.433 43.727  1.00 34.43 ? 667  ILE   A CA   1 
ATOM   1108 C  C    . ILE   A 1 173 ? -27.314 -12.799 44.219  1.00 36.88 ? 667  ILE   A C    1 
ATOM   1109 O  O    . ILE   A 1 173 ? -27.304 -11.654 44.683  1.00 40.45 ? 667  ILE   A O    1 
ATOM   1110 C  CB   . ILE   A 1 173 ? -25.608 -12.867 42.349  1.00 35.31 ? 667  ILE   A CB   1 
ATOM   1111 C  CG1  . ILE   A 1 173 ? -25.115 -11.424 42.477  1.00 35.90 ? 667  ILE   A CG1  1 
ATOM   1112 C  CG2  . ILE   A 1 173 ? -26.765 -12.957 41.364  1.00 29.77 ? 667  ILE   A CG2  1 
ATOM   1113 C  CD1  . ILE   A 1 173 ? -23.850 -11.280 43.294  1.00 32.82 ? 667  ILE   A CD1  1 
ATOM   1114 N  N    . ASN   A 1 174 ? -28.432 -13.522 44.147  1.00 36.61 ? 668  ASN   A N    1 
ATOM   1115 C  CA   . ASN   A 1 174 ? -29.734 -12.997 44.539  1.00 38.42 ? 668  ASN   A CA   1 
ATOM   1116 C  C    . ASN   A 1 174 ? -30.254 -13.643 45.820  1.00 38.80 ? 668  ASN   A C    1 
ATOM   1117 O  O    . ASN   A 1 174 ? -31.464 -13.694 46.047  1.00 41.66 ? 668  ASN   A O    1 
ATOM   1118 C  CB   . ASN   A 1 174 ? -30.741 -13.175 43.404  1.00 36.07 ? 668  ASN   A CB   1 
ATOM   1119 C  CG   . ASN   A 1 174 ? -30.358 -12.399 42.160  1.00 40.03 ? 668  ASN   A CG   1 
ATOM   1120 O  OD1  . ASN   A 1 174 ? -29.664 -11.385 42.236  1.00 40.30 ? 668  ASN   A OD1  1 
ATOM   1121 N  ND2  . ASN   A 1 174 ? -30.808 -12.875 41.006  1.00 40.50 ? 668  ASN   A ND2  1 
ATOM   1122 N  N    . ASP   A 1 175 ? -29.352 -14.143 46.665  1.00 39.68 ? 669  ASP   A N    1 
ATOM   1123 C  CA   . ASP   A 1 175 ? -29.782 -14.706 47.936  1.00 41.63 ? 669  ASP   A CA   1 
ATOM   1124 C  C    . ASP   A 1 175 ? -30.034 -13.586 48.945  1.00 37.49 ? 669  ASP   A C    1 
ATOM   1125 O  O    . ASP   A 1 175 ? -29.276 -12.614 48.992  1.00 42.50 ? 669  ASP   A O    1 
ATOM   1126 C  CB   . ASP   A 1 175 ? -28.733 -15.676 48.479  1.00 41.02 ? 669  ASP   A CB   1 
ATOM   1127 C  CG   . ASP   A 1 175 ? -29.234 -16.472 49.669  1.00 39.76 ? 669  ASP   A CG   1 
ATOM   1128 O  OD1  . ASP   A 1 175 ? -29.228 -15.931 50.794  1.00 39.90 ? 669  ASP   A OD1  1 
ATOM   1129 O  OD2  . ASP   A 1 175 ? -29.648 -17.635 49.479  1.00 39.40 ? 669  ASP   A OD2  1 
ATOM   1130 N  N    . PRO   A 1 176 ? -31.094 -13.695 49.752  1.00 38.34 ? 670  PRO   A N    1 
ATOM   1131 C  CA   . PRO   A 1 176 ? -31.396 -12.623 50.716  1.00 40.20 ? 670  PRO   A CA   1 
ATOM   1132 C  C    . PRO   A 1 176 ? -30.262 -12.321 51.681  1.00 38.71 ? 670  PRO   A C    1 
ATOM   1133 O  O    . PRO   A 1 176 ? -30.111 -11.165 52.098  1.00 35.40 ? 670  PRO   A O    1 
ATOM   1134 C  CB   . PRO   A 1 176 ? -32.633 -13.158 51.451  1.00 38.65 ? 670  PRO   A CB   1 
ATOM   1135 C  CG   . PRO   A 1 176 ? -33.277 -14.079 50.473  1.00 39.09 ? 670  PRO   A CG   1 
ATOM   1136 C  CD   . PRO   A 1 176 ? -32.151 -14.720 49.712  1.00 37.19 ? 670  PRO   A CD   1 
ATOM   1137 N  N    . ARG   A 1 177 ? -29.458 -13.321 52.052  1.00 35.92 ? 671  ARG   A N    1 
ATOM   1138 C  CA   . ARG   A 1 177 ? -28.322 -13.066 52.932  1.00 36.51 ? 671  ARG   A CA   1 
ATOM   1139 C  C    . ARG   A 1 177 ? -27.273 -12.181 52.274  1.00 37.65 ? 671  ARG   A C    1 
ATOM   1140 O  O    . ARG   A 1 177 ? -26.424 -11.617 52.973  1.00 45.12 ? 671  ARG   A O    1 
ATOM   1141 C  CB   . ARG   A 1 177 ? -27.693 -14.388 53.375  1.00 36.22 ? 671  ARG   A CB   1 
ATOM   1142 C  CG   . ARG   A 1 177 ? -28.601 -15.245 54.240  1.00 40.37 ? 671  ARG   A CG   1 
ATOM   1143 C  CD   . ARG   A 1 177 ? -28.169 -16.703 54.223  1.00 39.93 ? 671  ARG   A CD   1 
ATOM   1144 N  NE   . ARG   A 1 177 ? -27.443 -17.075 55.431  1.00 47.45 ? 671  ARG   A NE   1 
ATOM   1145 C  CZ   . ARG   A 1 177 ? -26.942 -18.282 55.661  1.00 49.46 ? 671  ARG   A CZ   1 
ATOM   1146 N  NH1  . ARG   A 1 177 ? -27.068 -19.262 54.781  1.00 44.15 ? 671  ARG   A NH1  1 
ATOM   1147 N  NH2  . ARG   A 1 177 ? -26.298 -18.510 56.802  1.00 50.91 ? 671  ARG   A NH2  1 
ATOM   1148 N  N    . LEU   A 1 178 ? -27.309 -12.051 50.949  1.00 31.35 ? 672  LEU   A N    1 
ATOM   1149 C  CA   . LEU   A 1 178 ? -26.423 -11.159 50.210  1.00 35.11 ? 672  LEU   A CA   1 
ATOM   1150 C  C    . LEU   A 1 178 ? -27.086 -9.838  49.847  1.00 39.03 ? 672  LEU   A C    1 
ATOM   1151 O  O    . LEU   A 1 178 ? -26.449 -8.784  49.941  1.00 37.79 ? 672  LEU   A O    1 
ATOM   1152 C  CB   . LEU   A 1 178 ? -25.929 -11.841 48.929  1.00 35.61 ? 672  LEU   A CB   1 
ATOM   1153 C  CG   . LEU   A 1 178 ? -24.653 -12.686 48.983  1.00 34.79 ? 672  LEU   A CG   1 
ATOM   1154 C  CD1  . LEU   A 1 178 ? -24.762 -13.814 50.000  1.00 35.68 ? 672  LEU   A CD1  1 
ATOM   1155 C  CD2  . LEU   A 1 178 ? -24.326 -13.234 47.602  1.00 28.58 ? 672  LEU   A CD2  1 
ATOM   1156 N  N    . ARG   A 1 179 ? -28.356 -9.870  49.437  1.00 36.57 ? 673  ARG   A N    1 
ATOM   1157 C  CA   . ARG   A 1 179 ? -29.038 -8.657  49.003  1.00 36.92 ? 673  ARG   A CA   1 
ATOM   1158 C  C    . ARG   A 1 179 ? -29.539 -7.825  50.176  1.00 36.43 ? 673  ARG   A C    1 
ATOM   1159 O  O    . ARG   A 1 179 ? -29.623 -6.597  50.067  1.00 38.97 ? 673  ARG   A O    1 
ATOM   1160 C  CB   . ARG   A 1 179 ? -30.200 -9.016  48.076  1.00 33.56 ? 673  ARG   A CB   1 
ATOM   1161 C  CG   . ARG   A 1 179 ? -29.757 -9.613  46.754  1.00 32.43 ? 673  ARG   A CG   1 
ATOM   1162 C  CD   . ARG   A 1 179 ? -28.873 -8.639  45.996  1.00 34.65 ? 673  ARG   A CD   1 
ATOM   1163 N  NE   . ARG   A 1 179 ? -28.478 -9.154  44.691  1.00 39.32 ? 673  ARG   A NE   1 
ATOM   1164 C  CZ   . ARG   A 1 179 ? -28.146 -8.391  43.659  1.00 36.46 ? 673  ARG   A CZ   1 
ATOM   1165 N  NH1  . ARG   A 1 179 ? -28.160 -7.071  43.744  1.00 39.88 ? 673  ARG   A NH1  1 
ATOM   1166 N  NH2  . ARG   A 1 179 ? -27.794 -8.966  42.513  1.00 36.67 ? 673  ARG   A NH2  1 
ATOM   1167 N  N    . ASN   A 1 180 ? -29.882 -8.467  51.292  1.00 38.36 ? 674  ASN   A N    1 
ATOM   1168 C  CA   . ASN   A 1 180 ? -30.282 -7.785  52.521  1.00 36.40 ? 674  ASN   A CA   1 
ATOM   1169 C  C    . ASN   A 1 180 ? -29.357 -8.255  53.639  1.00 36.29 ? 674  ASN   A C    1 
ATOM   1170 O  O    . ASN   A 1 180 ? -29.774 -8.994  54.540  1.00 39.75 ? 674  ASN   A O    1 
ATOM   1171 C  CB   . ASN   A 1 180 ? -31.746 -8.061  52.861  1.00 37.96 ? 674  ASN   A CB   1 
ATOM   1172 C  CG   . ASN   A 1 180 ? -32.300 -7.091  53.885  1.00 39.74 ? 674  ASN   A CG   1 
ATOM   1173 O  OD1  . ASN   A 1 180 ? -31.681 -6.073  54.192  1.00 39.33 ? 674  ASN   A OD1  1 
ATOM   1174 N  ND2  . ASN   A 1 180 ? -33.478 -7.401  54.416  1.00 41.89 ? 674  ASN   A ND2  1 
ATOM   1175 N  N    . PRO   A 1 181 ? -28.095 -7.841  53.610  1.00 39.90 ? 675  PRO   A N    1 
ATOM   1176 C  CA   . PRO   A 1 181 ? -27.094 -8.449  54.489  1.00 39.39 ? 675  PRO   A CA   1 
ATOM   1177 C  C    . PRO   A 1 181 ? -27.157 -7.914  55.912  1.00 40.11 ? 675  PRO   A C    1 
ATOM   1178 O  O    . PRO   A 1 181 ? -27.700 -6.844  56.192  1.00 36.64 ? 675  PRO   A O    1 
ATOM   1179 C  CB   . PRO   A 1 181 ? -25.771 -8.063  53.822  1.00 39.36 ? 675  PRO   A CB   1 
ATOM   1180 C  CG   . PRO   A 1 181 ? -26.063 -6.739  53.200  1.00 39.69 ? 675  PRO   A CG   1 
ATOM   1181 C  CD   . PRO   A 1 181 ? -27.513 -6.779  52.768  1.00 40.13 ? 675  PRO   A CD   1 
ATOM   1182 N  N    . SER   A 1 182 ? -26.582 -8.701  56.815  1.00 42.77 ? 676  SER   A N    1 
ATOM   1183 C  CA   . SER   A 1 182 ? -26.368 -8.307  58.200  1.00 46.40 ? 676  SER   A CA   1 
ATOM   1184 C  C    . SER   A 1 182 ? -24.964 -8.754  58.588  1.00 47.80 ? 676  SER   A C    1 
ATOM   1185 O  O    . SER   A 1 182 ? -24.153 -9.126  57.735  1.00 52.58 ? 676  SER   A O    1 
ATOM   1186 C  CB   . SER   A 1 182 ? -27.448 -8.903  59.112  1.00 45.97 ? 676  SER   A CB   1 
ATOM   1187 O  OG   . SER   A 1 182 ? -27.484 -10.316 59.003  1.00 55.00 ? 676  SER   A OG   1 
ATOM   1188 N  N    . ASP   A 1 183 ? -24.668 -8.722  59.884  1.00 51.06 ? 677  ASP   A N    1 
ATOM   1189 C  CA   . ASP   A 1 183 ? -23.388 -9.207  60.379  1.00 46.57 ? 677  ASP   A CA   1 
ATOM   1190 C  C    . ASP   A 1 183 ? -23.390 -10.707 60.643  1.00 43.05 ? 677  ASP   A C    1 
ATOM   1191 O  O    . ASP   A 1 183 ? -22.348 -11.257 61.013  1.00 47.42 ? 677  ASP   A O    1 
ATOM   1192 C  CB   . ASP   A 1 183 ? -22.992 -8.454  61.652  1.00 57.44 ? 677  ASP   A CB   1 
ATOM   1193 C  CG   . ASP   A 1 183 ? -21.994 -7.344  61.384  1.00 68.67 ? 677  ASP   A CG   1 
ATOM   1194 O  OD1  . ASP   A 1 183 ? -21.736 -7.048  60.198  1.00 62.89 ? 677  ASP   A OD1  1 
ATOM   1195 O  OD2  . ASP   A 1 183 ? -21.466 -6.768  62.359  1.00 73.42 ? 677  ASP   A OD2  1 
ATOM   1196 N  N    . LYS   A 1 184 ? -24.528 -11.378 60.458  1.00 48.72 ? 678  LYS   A N    1 
ATOM   1197 C  CA   . LYS   A 1 184 ? -24.612 -12.820 60.648  1.00 53.75 ? 678  LYS   A CA   1 
ATOM   1198 C  C    . LYS   A 1 184 ? -24.099 -13.607 59.451  1.00 49.16 ? 678  LYS   A C    1 
ATOM   1199 O  O    . LYS   A 1 184 ? -23.946 -14.829 59.554  1.00 49.23 ? 678  LYS   A O    1 
ATOM   1200 C  CB   . LYS   A 1 184 ? -26.058 -13.225 60.946  1.00 52.21 ? 678  LYS   A CB   1 
ATOM   1201 C  CG   . LYS   A 1 184 ? -26.204 -14.210 62.094  1.00 63.53 ? 678  LYS   A CG   1 
ATOM   1202 C  CD   . LYS   A 1 184 ? -25.709 -13.614 63.401  1.00 67.44 ? 678  LYS   A CD   1 
ATOM   1203 C  CE   . LYS   A 1 184 ? -26.217 -14.405 64.595  1.00 65.94 ? 678  LYS   A CE   1 
ATOM   1204 N  NZ   . LYS   A 1 184 ? -25.797 -13.791 65.884  1.00 66.12 ? 678  LYS   A NZ   1 
ATOM   1205 N  N    . PHE   A 1 185 ? -23.838 -12.947 58.325  1.00 45.85 ? 679  PHE   A N    1 
ATOM   1206 C  CA   . PHE   A 1 185 ? -23.314 -13.604 57.131  1.00 43.88 ? 679  PHE   A CA   1 
ATOM   1207 C  C    . PHE   A 1 185 ? -22.344 -12.644 56.457  1.00 38.22 ? 679  PHE   A C    1 
ATOM   1208 O  O    . PHE   A 1 185 ? -22.766 -11.662 55.838  1.00 39.25 ? 679  PHE   A O    1 
ATOM   1209 C  CB   . PHE   A 1 185 ? -24.438 -14.007 56.177  1.00 42.10 ? 679  PHE   A CB   1 
ATOM   1210 C  CG   . PHE   A 1 185 ? -24.000 -14.947 55.087  1.00 44.98 ? 679  PHE   A CG   1 
ATOM   1211 C  CD1  . PHE   A 1 185 ? -23.476 -14.461 53.900  1.00 42.86 ? 679  PHE   A CD1  1 
ATOM   1212 C  CD2  . PHE   A 1 185 ? -24.113 -16.318 55.251  1.00 39.83 ? 679  PHE   A CD2  1 
ATOM   1213 C  CE1  . PHE   A 1 185 ? -23.074 -15.324 52.898  1.00 38.91 ? 679  PHE   A CE1  1 
ATOM   1214 C  CE2  . PHE   A 1 185 ? -23.713 -17.185 54.253  1.00 42.22 ? 679  PHE   A CE2  1 
ATOM   1215 C  CZ   . PHE   A 1 185 ? -23.193 -16.687 53.075  1.00 36.07 ? 679  PHE   A CZ   1 
ATOM   1216 N  N    . ILE   A 1 186 ? -21.050 -12.929 56.573  1.00 38.79 ? 680  ILE   A N    1 
ATOM   1217 C  CA   . ILE   A 1 186 ? -19.994 -12.075 56.043  1.00 38.46 ? 680  ILE   A CA   1 
ATOM   1218 C  C    . ILE   A 1 186 ? -19.575 -12.598 54.677  1.00 36.61 ? 680  ILE   A C    1 
ATOM   1219 O  O    . ILE   A 1 186 ? -19.254 -13.784 54.526  1.00 35.21 ? 680  ILE   A O    1 
ATOM   1220 C  CB   . ILE   A 1 186 ? -18.790 -12.024 56.998  1.00 37.46 ? 680  ILE   A CB   1 
ATOM   1221 C  CG1  . ILE   A 1 186 ? -19.252 -11.712 58.422  1.00 40.42 ? 680  ILE   A CG1  1 
ATOM   1222 C  CG2  . ILE   A 1 186 ? -17.775 -10.998 56.524  1.00 37.71 ? 680  ILE   A CG2  1 
ATOM   1223 C  CD1  . ILE   A 1 186 ? -20.032 -10.422 58.543  1.00 42.88 ? 680  ILE   A CD1  1 
ATOM   1224 N  N    . TYR   A 1 187 ? -19.582 -11.715 53.681  1.00 36.12 ? 681  TYR   A N    1 
ATOM   1225 C  CA   . TYR   A 1 187 ? -19.047 -12.016 52.362  1.00 34.05 ? 681  TYR   A CA   1 
ATOM   1226 C  C    . TYR   A 1 187 ? -18.178 -10.853 51.909  1.00 32.00 ? 681  TYR   A C    1 
ATOM   1227 O  O    . TYR   A 1 187 ? -18.374 -9.711  52.335  1.00 35.56 ? 681  TYR   A O    1 
ATOM   1228 C  CB   . TYR   A 1 187 ? -20.160 -12.290 51.337  1.00 28.47 ? 681  TYR   A CB   1 
ATOM   1229 C  CG   . TYR   A 1 187 ? -21.179 -11.183 51.205  1.00 31.35 ? 681  TYR   A CG   1 
ATOM   1230 C  CD1  . TYR   A 1 187 ? -22.309 -11.153 52.010  1.00 34.82 ? 681  TYR   A CD1  1 
ATOM   1231 C  CD2  . TYR   A 1 187 ? -21.021 -10.176 50.261  1.00 34.31 ? 681  TYR   A CD2  1 
ATOM   1232 C  CE1  . TYR   A 1 187 ? -23.248 -10.145 51.889  1.00 37.49 ? 681  TYR   A CE1  1 
ATOM   1233 C  CE2  . TYR   A 1 187 ? -21.953 -9.164  50.133  1.00 35.15 ? 681  TYR   A CE2  1 
ATOM   1234 C  CZ   . TYR   A 1 187 ? -23.064 -9.153  50.948  1.00 35.56 ? 681  TYR   A CZ   1 
ATOM   1235 O  OH   . TYR   A 1 187 ? -23.993 -8.147  50.822  1.00 36.73 ? 681  TYR   A OH   1 
ATOM   1236 N  N    . ALA   A 1 188 ? -17.209 -11.151 51.047  1.00 31.81 ? 682  ALA   A N    1 
ATOM   1237 C  CA   . ALA   A 1 188 ? -16.250 -10.145 50.608  1.00 31.41 ? 682  ALA   A CA   1 
ATOM   1238 C  C    . ALA   A 1 188 ? -15.559 -10.632 49.340  1.00 26.61 ? 682  ALA   A C    1 
ATOM   1239 O  O    . ALA   A 1 188 ? -15.814 -11.738 48.850  1.00 26.25 ? 682  ALA   A O    1 
ATOM   1240 C  CB   . ALA   A 1 188 ? -15.234 -9.839  51.711  1.00 30.47 ? 682  ALA   A CB   1 
ATOM   1241 N  N    . THR   A 1 189 ? -14.676 -9.783  48.813  1.00 27.48 ? 683  THR   A N    1 
ATOM   1242 C  CA   . THR   A 1 189 ? -13.853 -10.103 47.653  1.00 29.69 ? 683  THR   A CA   1 
ATOM   1243 C  C    . THR   A 1 189 ? -12.427 -9.647  47.955  1.00 24.88 ? 683  THR   A C    1 
ATOM   1244 O  O    . THR   A 1 189 ? -12.083 -9.343  49.102  1.00 20.35 ? 683  THR   A O    1 
ATOM   1245 C  CB   . THR   A 1 189 ? -14.421 -9.460  46.379  1.00 27.55 ? 683  THR   A CB   1 
ATOM   1246 O  OG1  . THR   A 1 189 ? -13.685 -9.920  45.241  1.00 23.51 ? 683  THR   A OG1  1 
ATOM   1247 C  CG2  . THR   A 1 189 ? -14.338 -7.938  46.462  1.00 25.57 ? 683  THR   A CG2  1 
ATOM   1248 N  N    . VAL   A 1 190 ? -11.590 -9.590  46.925  1.00 23.60 ? 684  VAL   A N    1 
ATOM   1249 C  CA   . VAL   A 1 190 ? -10.200 -9.179  47.082  1.00 24.74 ? 684  VAL   A CA   1 
ATOM   1250 C  C    . VAL   A 1 190 ? -10.108 -7.665  46.954  1.00 25.49 ? 684  VAL   A C    1 
ATOM   1251 O  O    . VAL   A 1 190 ? -10.722 -7.070  46.060  1.00 25.58 ? 684  VAL   A O    1 
ATOM   1252 C  CB   . VAL   A 1 190 ? -9.302  -9.876  46.049  1.00 23.88 ? 684  VAL   A CB   1 
ATOM   1253 C  CG1  . VAL   A 1 190 ? -7.853  -9.434  46.217  1.00 23.18 ? 684  VAL   A CG1  1 
ATOM   1254 C  CG2  . VAL   A 1 190 ? -9.414  -11.385 46.189  1.00 25.56 ? 684  VAL   A CG2  1 
ATOM   1255 N  N    . LYS   A 1 191 ? -9.351  -7.041  47.857  1.00 24.20 ? 685  LYS   A N    1 
ATOM   1256 C  CA   . LYS   A 1 191 ? -9.131  -5.604  47.785  1.00 25.87 ? 685  LYS   A CA   1 
ATOM   1257 C  C    . LYS   A 1 191 ? -8.451  -5.228  46.479  1.00 24.67 ? 685  LYS   A C    1 
ATOM   1258 O  O    . LYS   A 1 191 ? -7.555  -5.929  46.000  1.00 20.00 ? 685  LYS   A O    1 
ATOM   1259 C  CB   . LYS   A 1 191 ? -8.267  -5.129  48.952  1.00 20.74 ? 685  LYS   A CB   1 
ATOM   1260 C  CG   . LYS   A 1 191 ? -8.977  -4.979  50.278  1.00 23.49 ? 685  LYS   A CG   1 
ATOM   1261 C  CD   . LYS   A 1 191 ? -8.048  -4.318  51.284  1.00 27.00 ? 685  LYS   A CD   1 
ATOM   1262 C  CE   . LYS   A 1 191 ? -8.677  -4.212  52.660  1.00 36.59 ? 685  LYS   A CE   1 
ATOM   1263 N  NZ   . LYS   A 1 191 ? -7.703  -3.685  53.658  1.00 26.02 ? 685  LYS   A NZ   1 
ATOM   1264 N  N    . GLN   A 1 192 ? -8.882  -4.104  45.910  1.00 25.40 ? 686  GLN   A N    1 
ATOM   1265 C  CA   . GLN   A 1 192 ? -8.224  -3.497  44.755  1.00 25.48 ? 686  GLN   A CA   1 
ATOM   1266 C  C    . GLN   A 1 192 ? -8.124  -4.471  43.583  1.00 19.92 ? 686  GLN   A C    1 
ATOM   1267 O  O    . GLN   A 1 192 ? -7.113  -4.528  42.880  1.00 21.19 ? 686  GLN   A O    1 
ATOM   1268 C  CB   . GLN   A 1 192 ? -6.849  -2.946  45.139  1.00 21.64 ? 686  GLN   A CB   1 
ATOM   1269 C  CG   . GLN   A 1 192 ? -6.940  -1.755  46.081  1.00 24.21 ? 686  GLN   A CG   1 
ATOM   1270 C  CD   . GLN   A 1 192 ? -5.630  -1.435  46.766  1.00 36.47 ? 686  GLN   A CD   1 
ATOM   1271 O  OE1  . GLN   A 1 192 ? -4.555  -1.632  46.202  1.00 40.47 ? 686  GLN   A OE1  1 
ATOM   1272 N  NE2  . GLN   A 1 192 ? -5.714  -0.924  47.989  1.00 34.34 ? 686  GLN   A NE2  1 
ATOM   1273 N  N    . SER   A 1 193 ? -9.186  -5.239  43.370  1.00 17.96 ? 687  SER   A N    1 
ATOM   1274 C  CA   . SER   A 1 193 ? -9.307  -6.138  42.234  1.00 23.86 ? 687  SER   A CA   1 
ATOM   1275 C  C    . SER   A 1 193 ? -10.408 -5.644  41.304  1.00 24.91 ? 687  SER   A C    1 
ATOM   1276 O  O    . SER   A 1 193 ? -11.141 -4.700  41.611  1.00 20.60 ? 687  SER   A O    1 
ATOM   1277 C  CB   . SER   A 1 193 ? -9.602  -7.569  42.699  1.00 23.13 ? 687  SER   A CB   1 
ATOM   1278 O  OG   . SER   A 1 193 ? -10.930 -7.683  43.181  1.00 21.18 ? 687  SER   A OG   1 
ATOM   1279 N  N    . SER   A 1 194 ? -10.513 -6.296  40.144  1.00 19.80 ? 688  SER   A N    1 
ATOM   1280 C  CA   . SER   A 1 194 ? -11.588 -5.962  39.216  1.00 21.84 ? 688  SER   A CA   1 
ATOM   1281 C  C    . SER   A 1 194 ? -12.952 -6.262  39.819  1.00 18.39 ? 688  SER   A C    1 
ATOM   1282 O  O    . SER   A 1 194 ? -13.933 -5.574  39.512  1.00 20.26 ? 688  SER   A O    1 
ATOM   1283 C  CB   . SER   A 1 194 ? -11.409 -6.725  37.904  1.00 18.25 ? 688  SER   A CB   1 
ATOM   1284 O  OG   . SER   A 1 194 ? -11.746 -8.092  38.067  1.00 17.13 ? 688  SER   A OG   1 
ATOM   1285 N  N    . VAL   A 1 195 ? -13.033 -7.282  40.676  1.00 20.06 ? 689  VAL   A N    1 
ATOM   1286 C  CA   . VAL   A 1 195 ? -14.289 -7.583  41.352  1.00 19.70 ? 689  VAL   A CA   1 
ATOM   1287 C  C    . VAL   A 1 195 ? -14.638 -6.477  42.337  1.00 24.98 ? 689  VAL   A C    1 
ATOM   1288 O  O    . VAL   A 1 195 ? -15.819 -6.186  42.565  1.00 25.36 ? 689  VAL   A O    1 
ATOM   1289 C  CB   . VAL   A 1 195 ? -14.202 -8.955  42.047  1.00 22.40 ? 689  VAL   A CB   1 
ATOM   1290 C  CG1  . VAL   A 1 195 ? -15.565 -9.374  42.585  1.00 25.23 ? 689  VAL   A CG1  1 
ATOM   1291 C  CG2  . VAL   A 1 195 ? -13.650 -10.001 41.090  1.00 17.45 ? 689  VAL   A CG2  1 
ATOM   1292 N  N    . ASP   A 1 196 ? -13.627 -5.839  42.932  1.00 24.07 ? 690  ASP   A N    1 
ATOM   1293 C  CA   . ASP   A 1 196 ? -13.887 -4.743  43.859  1.00 18.77 ? 690  ASP   A CA   1 
ATOM   1294 C  C    . ASP   A 1 196 ? -14.520 -3.560  43.135  1.00 26.14 ? 690  ASP   A C    1 
ATOM   1295 O  O    . ASP   A 1 196 ? -15.492 -2.970  43.622  1.00 19.83 ? 690  ASP   A O    1 
ATOM   1296 C  CB   . ASP   A 1 196 ? -12.592 -4.325  44.557  1.00 24.14 ? 690  ASP   A CB   1 
ATOM   1297 C  CG   . ASP   A 1 196 ? -12.830 -3.363  45.713  1.00 24.78 ? 690  ASP   A CG   1 
ATOM   1298 O  OD1  . ASP   A 1 196 ? -14.002 -3.151  46.091  1.00 27.33 ? 690  ASP   A OD1  1 
ATOM   1299 O  OD2  . ASP   A 1 196 ? -11.840 -2.823  46.250  1.00 20.68 ? 690  ASP   A OD2  1 
ATOM   1300 N  N    . ILE   A 1 197 ? -13.980 -3.200  41.962  1.00 22.44 ? 691  ILE   A N    1 
ATOM   1301 C  CA   . ILE   A 1 197 ? -14.583 -2.130  41.170  1.00 25.35 ? 691  ILE   A CA   1 
ATOM   1302 C  C    . ILE   A 1 197 ? -15.977 -2.544  40.734  1.00 23.49 ? 691  ILE   A C    1 
ATOM   1303 O  O    . ILE   A 1 197 ? -16.895 -1.717  40.675  1.00 23.47 ? 691  ILE   A O    1 
ATOM   1304 C  CB   . ILE   A 1 197 ? -13.738 -1.774  39.926  1.00 29.73 ? 691  ILE   A CB   1 
ATOM   1305 C  CG1  . ILE   A 1 197 ? -12.326 -1.307  40.271  1.00 33.07 ? 691  ILE   A CG1  1 
ATOM   1306 C  CG2  . ILE   A 1 197 ? -14.398 -0.655  39.147  1.00 27.07 ? 691  ILE   A CG2  1 
ATOM   1307 C  CD1  . ILE   A 1 197 ? -11.276 -2.024  39.427  1.00 33.81 ? 691  ILE   A CD1  1 
ATOM   1308 N  N    . TYR   A 1 198 ? -16.155 -3.834  40.430  1.00 23.35 ? 692  TYR   A N    1 
ATOM   1309 C  CA   . TYR   A 1 198 ? -17.416 -4.321  39.881  1.00 26.19 ? 692  TYR   A CA   1 
ATOM   1310 C  C    . TYR   A 1 198 ? -18.584 -3.965  40.790  1.00 26.59 ? 692  TYR   A C    1 
ATOM   1311 O  O    . TYR   A 1 198 ? -19.629 -3.495  40.324  1.00 30.13 ? 692  TYR   A O    1 
ATOM   1312 C  CB   . TYR   A 1 198 ? -17.334 -5.833  39.663  1.00 23.54 ? 692  TYR   A CB   1 
ATOM   1313 C  CG   . TYR   A 1 198 ? -18.638 -6.470  39.240  1.00 24.40 ? 692  TYR   A CG   1 
ATOM   1314 C  CD1  . TYR   A 1 198 ? -19.002 -6.526  37.901  1.00 30.05 ? 692  TYR   A CD1  1 
ATOM   1315 C  CD2  . TYR   A 1 198 ? -19.499 -7.026  40.177  1.00 22.61 ? 692  TYR   A CD2  1 
ATOM   1316 C  CE1  . TYR   A 1 198 ? -20.191 -7.110  37.509  1.00 28.33 ? 692  TYR   A CE1  1 
ATOM   1317 C  CE2  . TYR   A 1 198 ? -20.690 -7.609  39.796  1.00 26.87 ? 692  TYR   A CE2  1 
ATOM   1318 C  CZ   . TYR   A 1 198 ? -21.031 -7.649  38.461  1.00 27.76 ? 692  TYR   A CZ   1 
ATOM   1319 O  OH   . TYR   A 1 198 ? -22.216 -8.231  38.076  1.00 34.74 ? 692  TYR   A OH   1 
ATOM   1320 N  N    . PHE   A 1 199 ? -18.417 -4.162  42.097  1.00 23.15 ? 693  PHE   A N    1 
ATOM   1321 C  CA   . PHE   A 1 199 ? -19.483 -3.843  43.037  1.00 30.22 ? 693  PHE   A CA   1 
ATOM   1322 C  C    . PHE   A 1 199 ? -19.507 -2.372  43.427  1.00 23.29 ? 693  PHE   A C    1 
ATOM   1323 O  O    . PHE   A 1 199 ? -20.516 -1.907  43.967  1.00 29.43 ? 693  PHE   A O    1 
ATOM   1324 C  CB   . PHE   A 1 199 ? -19.359 -4.705  44.295  1.00 26.21 ? 693  PHE   A CB   1 
ATOM   1325 C  CG   . PHE   A 1 199 ? -19.783 -6.132  44.095  1.00 30.06 ? 693  PHE   A CG   1 
ATOM   1326 C  CD1  . PHE   A 1 199 ? -18.875 -7.092  43.681  1.00 25.51 ? 693  PHE   A CD1  1 
ATOM   1327 C  CD2  . PHE   A 1 199 ? -21.102 -6.505  44.291  1.00 27.97 ? 693  PHE   A CD2  1 
ATOM   1328 C  CE1  . PHE   A 1 199 ? -19.269 -8.404  43.494  1.00 25.68 ? 693  PHE   A CE1  1 
ATOM   1329 C  CE2  . PHE   A 1 199 ? -21.502 -7.815  44.105  1.00 30.19 ? 693  PHE   A CE2  1 
ATOM   1330 C  CZ   . PHE   A 1 199 ? -20.584 -8.765  43.703  1.00 28.69 ? 693  PHE   A CZ   1 
ATOM   1331 N  N    . ARG   A 1 200 ? -18.431 -1.628  43.164  1.00 23.69 ? 694  ARG   A N    1 
ATOM   1332 C  CA   . ARG   A 1 200 ? -18.412 -0.211  43.511  1.00 28.54 ? 694  ARG   A CA   1 
ATOM   1333 C  C    . ARG   A 1 200 ? -19.092 0.650   42.455  1.00 30.36 ? 694  ARG   A C    1 
ATOM   1334 O  O    . ARG   A 1 200 ? -19.740 1.646   42.797  1.00 34.43 ? 694  ARG   A O    1 
ATOM   1335 C  CB   . ARG   A 1 200 ? -16.972 0.266   43.721  1.00 27.10 ? 694  ARG   A CB   1 
ATOM   1336 C  CG   . ARG   A 1 200 ? -16.866 1.725   44.145  1.00 29.74 ? 694  ARG   A CG   1 
ATOM   1337 C  CD   . ARG   A 1 200 ? -15.518 2.045   44.772  1.00 27.72 ? 694  ARG   A CD   1 
ATOM   1338 N  NE   . ARG   A 1 200 ? -14.447 2.106   43.785  1.00 35.67 ? 694  ARG   A NE   1 
ATOM   1339 C  CZ   . ARG   A 1 200 ? -13.164 2.248   44.084  1.00 37.45 ? 694  ARG   A CZ   1 
ATOM   1340 N  NH1  . ARG   A 1 200 ? -12.752 2.341   45.338  1.00 31.51 ? 694  ARG   A NH1  1 
ATOM   1341 N  NH2  . ARG   A 1 200 ? -12.270 2.299   43.100  1.00 39.23 ? 694  ARG   A NH2  1 
ATOM   1342 N  N    . ARG   A 1 201 ? -18.969 0.285   41.178  1.00 24.59 ? 695  ARG   A N    1 
ATOM   1343 C  CA   . ARG   A 1 201 ? -19.462 1.136   40.102  1.00 27.36 ? 695  ARG   A CA   1 
ATOM   1344 C  C    . ARG   A 1 201 ? -20.956 0.980   39.845  1.00 24.19 ? 695  ARG   A C    1 
ATOM   1345 O  O    . ARG   A 1 201 ? -21.574 1.900   39.298  1.00 31.20 ? 695  ARG   A O    1 
ATOM   1346 C  CB   . ARG   A 1 201 ? -18.694 0.849   38.808  1.00 29.78 ? 695  ARG   A CB   1 
ATOM   1347 C  CG   . ARG   A 1 201 ? -19.301 -0.262  37.963  1.00 31.24 ? 695  ARG   A CG   1 
ATOM   1348 C  CD   . ARG   A 1 201 ? -18.572 -0.435  36.641  1.00 36.72 ? 695  ARG   A CD   1 
ATOM   1349 N  NE   . ARG   A 1 201 ? -18.539 -1.830  36.219  1.00 30.37 ? 695  ARG   A NE   1 
ATOM   1350 C  CZ   . ARG   A 1 201 ? -17.575 -2.685  36.531  1.00 31.07 ? 695  ARG   A CZ   1 
ATOM   1351 N  NH1  . ARG   A 1 201 ? -16.532 -2.314  37.256  1.00 33.41 ? 695  ARG   A NH1  1 
ATOM   1352 N  NH2  . ARG   A 1 201 ? -17.657 -3.941  36.104  1.00 33.18 ? 695  ARG   A NH2  1 
ATOM   1353 N  N    . GLN   A 1 202 ? -21.551 -0.149  40.221  1.00 23.77 ? 696  GLN   A N    1 
ATOM   1354 C  CA   . GLN   A 1 202 ? -22.943 -0.445  39.898  1.00 31.14 ? 696  GLN   A CA   1 
ATOM   1355 C  C    . GLN   A 1 202 ? -23.812 -0.103  41.103  1.00 30.28 ? 696  GLN   A C    1 
ATOM   1356 O  O    . GLN   A 1 202 ? -23.758 -0.787  42.132  1.00 25.33 ? 696  GLN   A O    1 
ATOM   1357 C  CB   . GLN   A 1 202 ? -23.100 -1.907  39.487  1.00 29.01 ? 696  GLN   A CB   1 
ATOM   1358 C  CG   . GLN   A 1 202 ? -22.588 -2.192  38.084  1.00 32.33 ? 696  GLN   A CG   1 
ATOM   1359 C  CD   . GLN   A 1 202 ? -22.690 -3.654  37.708  1.00 34.52 ? 696  GLN   A CD   1 
ATOM   1360 O  OE1  . GLN   A 1 202 ? -23.603 -4.061  36.990  1.00 36.82 ? 696  GLN   A OE1  1 
ATOM   1361 N  NE2  . GLN   A 1 202 ? -21.749 -4.454  38.193  1.00 34.94 ? 696  GLN   A NE2  1 
ATOM   1362 N  N    . VAL   A 1 203 ? -24.619 0.954   40.967  1.00 24.12 ? 697  VAL   A N    1 
ATOM   1363 C  CA   . VAL   A 1 203 ? -25.448 1.425   42.074  1.00 28.32 ? 697  VAL   A CA   1 
ATOM   1364 C  C    . VAL   A 1 203 ? -26.463 0.369   42.490  1.00 25.42 ? 697  VAL   A C    1 
ATOM   1365 O  O    . VAL   A 1 203 ? -26.916 0.353   43.641  1.00 31.42 ? 697  VAL   A O    1 
ATOM   1366 C  CB   . VAL   A 1 203 ? -26.141 2.749   41.697  1.00 29.24 ? 697  VAL   A CB   1 
ATOM   1367 C  CG1  . VAL   A 1 203 ? -25.108 3.819   41.383  1.00 37.67 ? 697  VAL   A CG1  1 
ATOM   1368 C  CG2  . VAL   A 1 203 ? -27.071 2.542   40.512  1.00 30.86 ? 697  VAL   A CG2  1 
ATOM   1369 N  N    . GLU   A 1 204 ? -26.839 -0.524  41.571  1.00 29.12 ? 698  GLU   A N    1 
ATOM   1370 C  CA   . GLU   A 1 204 ? -27.757 -1.602  41.916  1.00 28.91 ? 698  GLU   A CA   1 
ATOM   1371 C  C    . GLU   A 1 204 ? -27.160 -2.553  42.943  1.00 29.11 ? 698  GLU   A C    1 
ATOM   1372 O  O    . GLU   A 1 204 ? -27.908 -3.251  43.636  1.00 30.07 ? 698  GLU   A O    1 
ATOM   1373 C  CB   . GLU   A 1 204 ? -28.157 -2.374  40.658  1.00 28.08 ? 698  GLU   A CB   1 
ATOM   1374 N  N    . LEU   A 1 205 ? -25.833 -2.592  43.057  1.00 30.94 ? 699  LEU   A N    1 
ATOM   1375 C  CA   . LEU   A 1 205 ? -25.139 -3.436  44.018  1.00 30.38 ? 699  LEU   A CA   1 
ATOM   1376 C  C    . LEU   A 1 205 ? -24.616 -2.650  45.213  1.00 31.90 ? 699  LEU   A C    1 
ATOM   1377 O  O    . LEU   A 1 205 ? -23.767 -3.160  45.951  1.00 32.59 ? 699  LEU   A O    1 
ATOM   1378 C  CB   . LEU   A 1 205 ? -23.979 -4.164  43.335  1.00 24.70 ? 699  LEU   A CB   1 
ATOM   1379 C  CG   . LEU   A 1 205 ? -24.293 -4.944  42.058  1.00 27.77 ? 699  LEU   A CG   1 
ATOM   1380 C  CD1  . LEU   A 1 205 ? -23.016 -5.502  41.455  1.00 24.31 ? 699  LEU   A CD1  1 
ATOM   1381 C  CD2  . LEU   A 1 205 ? -25.286 -6.057  42.337  1.00 30.72 ? 699  LEU   A CD2  1 
ATOM   1382 N  N    . SER   A 1 206 ? -25.101 -1.423  45.420  1.00 28.77 ? 700  SER   A N    1 
ATOM   1383 C  CA   . SER   A 1 206 ? -24.545 -0.567  46.464  1.00 32.66 ? 700  SER   A CA   1 
ATOM   1384 C  C    . SER   A 1 206 ? -24.731 -1.177  47.848  1.00 35.14 ? 700  SER   A C    1 
ATOM   1385 O  O    . SER   A 1 206 ? -23.859 -1.042  48.715  1.00 34.20 ? 700  SER   A O    1 
ATOM   1386 C  CB   . SER   A 1 206 ? -25.185 0.818   46.402  1.00 29.23 ? 700  SER   A CB   1 
ATOM   1387 O  OG   . SER   A 1 206 ? -26.589 0.742   46.570  1.00 36.88 ? 700  SER   A OG   1 
ATOM   1388 N  N    . THR   A 1 207 ? -25.860 -1.851  48.074  1.00 31.58 ? 701  THR   A N    1 
ATOM   1389 C  CA   . THR   A 1 207 ? -26.087 -2.504  49.360  1.00 34.84 ? 701  THR   A CA   1 
ATOM   1390 C  C    . THR   A 1 207 ? -25.018 -3.553  49.637  1.00 33.47 ? 701  THR   A C    1 
ATOM   1391 O  O    . THR   A 1 207 ? -24.470 -3.626  50.743  1.00 29.78 ? 701  THR   A O    1 
ATOM   1392 C  CB   . THR   A 1 207 ? -27.478 -3.141  49.388  1.00 36.25 ? 701  THR   A CB   1 
ATOM   1393 O  OG1  . THR   A 1 207 ? -28.471 -2.143  49.122  1.00 38.10 ? 701  THR   A OG1  1 
ATOM   1394 C  CG2  . THR   A 1 207 ? -27.746 -3.769  50.745  1.00 35.11 ? 701  THR   A CG2  1 
ATOM   1395 N  N    . MET   A 1 208 ? -24.709 -4.378  48.636  1.00 30.19 ? 702  MET   A N    1 
ATOM   1396 C  CA   . MET   A 1 208 ? -23.695 -5.412  48.811  1.00 32.23 ? 702  MET   A CA   1 
ATOM   1397 C  C    . MET   A 1 208 ? -22.306 -4.808  48.991  1.00 34.77 ? 702  MET   A C    1 
ATOM   1398 O  O    . MET   A 1 208 ? -21.513 -5.296  49.806  1.00 30.67 ? 702  MET   A O    1 
ATOM   1399 C  CB   . MET   A 1 208 ? -23.710 -6.364  47.617  1.00 29.73 ? 702  MET   A CB   1 
ATOM   1400 C  CG   . MET   A 1 208 ? -24.983 -7.174  47.463  1.00 31.99 ? 702  MET   A CG   1 
ATOM   1401 S  SD   . MET   A 1 208 ? -24.840 -8.380  46.131  1.00 35.47 ? 702  MET   A SD   1 
ATOM   1402 C  CE   . MET   A 1 208 ? -23.687 -9.539  46.862  1.00 29.05 ? 702  MET   A CE   1 
ATOM   1403 N  N    . TYR   A 1 209 ? -21.997 -3.744  48.244  1.00 33.78 ? 703  TYR   A N    1 
ATOM   1404 C  CA   . TYR   A 1 209 ? -20.652 -3.175  48.278  1.00 33.35 ? 703  TYR   A CA   1 
ATOM   1405 C  C    . TYR   A 1 209 ? -20.309 -2.622  49.657  1.00 32.86 ? 703  TYR   A C    1 
ATOM   1406 O  O    . TYR   A 1 209 ? -19.187 -2.807  50.143  1.00 34.02 ? 703  TYR   A O    1 
ATOM   1407 C  CB   . TYR   A 1 209 ? -20.516 -2.083  47.217  1.00 33.89 ? 703  TYR   A CB   1 
ATOM   1408 C  CG   . TYR   A 1 209 ? -19.269 -1.236  47.367  1.00 33.48 ? 703  TYR   A CG   1 
ATOM   1409 C  CD1  . TYR   A 1 209 ? -18.026 -1.714  46.971  1.00 31.93 ? 703  TYR   A CD1  1 
ATOM   1410 C  CD2  . TYR   A 1 209 ? -19.337 0.043   47.906  1.00 36.54 ? 703  TYR   A CD2  1 
ATOM   1411 C  CE1  . TYR   A 1 209 ? -16.887 -0.943  47.109  1.00 33.72 ? 703  TYR   A CE1  1 
ATOM   1412 C  CE2  . TYR   A 1 209 ? -18.204 0.820   48.048  1.00 33.85 ? 703  TYR   A CE2  1 
ATOM   1413 C  CZ   . TYR   A 1 209 ? -16.983 0.323   47.648  1.00 31.40 ? 703  TYR   A CZ   1 
ATOM   1414 O  OH   . TYR   A 1 209 ? -15.854 1.097   47.789  1.00 37.92 ? 703  TYR   A OH   1 
ATOM   1415 N  N    . ARG   A 1 210 ? -21.257 -1.934  50.299  1.00 30.74 ? 704  ARG   A N    1 
ATOM   1416 C  CA   . ARG   A 1 210 ? -20.995 -1.371  51.620  1.00 39.51 ? 704  ARG   A CA   1 
ATOM   1417 C  C    . ARG   A 1 210 ? -20.853 -2.445  52.690  1.00 31.79 ? 704  ARG   A C    1 
ATOM   1418 O  O    . ARG   A 1 210 ? -20.255 -2.182  53.739  1.00 30.74 ? 704  ARG   A O    1 
ATOM   1419 C  CB   . ARG   A 1 210 ? -22.099 -0.383  51.999  1.00 31.11 ? 704  ARG   A CB   1 
ATOM   1420 C  CG   . ARG   A 1 210 ? -22.370 0.657   50.926  1.00 32.13 ? 704  ARG   A CG   1 
ATOM   1421 C  CD   . ARG   A 1 210 ? -23.411 1.672   51.365  1.00 49.14 ? 704  ARG   A CD   1 
ATOM   1422 N  NE   . ARG   A 1 210 ? -24.765 1.219   51.071  1.00 46.66 ? 704  ARG   A NE   1 
ATOM   1423 C  CZ   . ARG   A 1 210 ? -25.522 1.705   50.098  1.00 48.12 ? 704  ARG   A CZ   1 
ATOM   1424 N  NH1  . ARG   A 1 210 ? -25.080 2.651   49.286  1.00 44.44 ? 704  ARG   A NH1  1 
ATOM   1425 N  NH2  . ARG   A 1 210 ? -26.753 1.228   49.933  1.00 43.94 ? 704  ARG   A NH2  1 
ATOM   1426 N  N    . HIS   A 1 211 ? -21.386 -3.644  52.453  1.00 33.34 ? 705  HIS   A N    1 
ATOM   1427 C  CA   . HIS   A 1 211 ? -21.124 -4.754  53.362  1.00 36.32 ? 705  HIS   A CA   1 
ATOM   1428 C  C    . HIS   A 1 211 ? -19.725 -5.319  53.148  1.00 37.27 ? 705  HIS   A C    1 
ATOM   1429 O  O    . HIS   A 1 211 ? -19.040 -5.677  54.112  1.00 40.26 ? 705  HIS   A O    1 
ATOM   1430 C  CB   . HIS   A 1 211 ? -22.180 -5.845  53.178  1.00 41.51 ? 705  HIS   A CB   1 
ATOM   1431 C  CG   . HIS   A 1 211 ? -21.888 -7.107  53.931  1.00 40.19 ? 705  HIS   A CG   1 
ATOM   1432 N  ND1  . HIS   A 1 211 ? -22.482 -7.408  55.138  1.00 41.95 ? 705  HIS   A ND1  1 
ATOM   1433 C  CD2  . HIS   A 1 211 ? -21.074 -8.150  53.642  1.00 37.42 ? 705  HIS   A CD2  1 
ATOM   1434 C  CE1  . HIS   A 1 211 ? -22.042 -8.579  55.563  1.00 40.00 ? 705  HIS   A CE1  1 
ATOM   1435 N  NE2  . HIS   A 1 211 ? -21.187 -9.050  54.674  1.00 40.55 ? 705  HIS   A NE2  1 
ATOM   1436 N  N    . MET   A 1 212 ? -19.282 -5.402  51.891  1.00 36.18 ? 706  MET   A N    1 
ATOM   1437 C  CA   . MET   A 1 212 ? -17.988 -6.007  51.594  1.00 34.81 ? 706  MET   A CA   1 
ATOM   1438 C  C    . MET   A 1 212 ? -16.818 -5.087  51.907  1.00 33.34 ? 706  MET   A C    1 
ATOM   1439 O  O    . MET   A 1 212 ? -15.736 -5.576  52.251  1.00 37.60 ? 706  MET   A O    1 
ATOM   1440 C  CB   . MET   A 1 212 ? -17.908 -6.419  50.126  1.00 33.29 ? 706  MET   A CB   1 
ATOM   1441 C  CG   . MET   A 1 212 ? -18.825 -7.548  49.737  1.00 35.45 ? 706  MET   A CG   1 
ATOM   1442 S  SD   . MET   A 1 212 ? -18.728 -7.872  47.971  1.00 39.57 ? 706  MET   A SD   1 
ATOM   1443 C  CE   . MET   A 1 212 ? -20.344 -7.324  47.461  1.00 33.90 ? 706  MET   A CE   1 
ATOM   1444 N  N    . GLU   A 1 213 ? -17.002 -3.769  51.775  1.00 37.52 ? 707  GLU   A N    1 
ATOM   1445 C  CA   . GLU   A 1 213 ? -15.889 -2.841  51.952  1.00 34.00 ? 707  GLU   A CA   1 
ATOM   1446 C  C    . GLU   A 1 213 ? -15.230 -3.000  53.316  1.00 37.35 ? 707  GLU   A C    1 
ATOM   1447 O  O    . GLU   A 1 213 ? -14.025 -2.761  53.453  1.00 45.40 ? 707  GLU   A O    1 
ATOM   1448 C  CB   . GLU   A 1 213 ? -16.369 -1.402  51.758  1.00 40.36 ? 707  GLU   A CB   1 
ATOM   1449 N  N    . LYS   A 1 214 ? -15.992 -3.414  54.327  1.00 37.13 ? 708  LYS   A N    1 
ATOM   1450 C  CA   . LYS   A 1 214 ? -15.446 -3.616  55.661  1.00 42.94 ? 708  LYS   A CA   1 
ATOM   1451 C  C    . LYS   A 1 214 ? -14.757 -4.965  55.829  1.00 44.27 ? 708  LYS   A C    1 
ATOM   1452 O  O    . LYS   A 1 214 ? -14.086 -5.172  56.846  1.00 49.58 ? 708  LYS   A O    1 
ATOM   1453 C  CB   . LYS   A 1 214 ? -16.557 -3.479  56.705  1.00 46.30 ? 708  LYS   A CB   1 
ATOM   1454 N  N    . HIS   A 1 215 ? -14.896 -5.881  54.867  1.00 41.09 ? 709  HIS   A N    1 
ATOM   1455 C  CA   . HIS   A 1 215 ? -14.378 -7.232  55.025  1.00 41.88 ? 709  HIS   A CA   1 
ATOM   1456 C  C    . HIS   A 1 215 ? -13.511 -7.715  53.869  1.00 34.45 ? 709  HIS   A C    1 
ATOM   1457 O  O    . HIS   A 1 215 ? -13.102 -8.880  53.880  1.00 34.75 ? 709  HIS   A O    1 
ATOM   1458 C  CB   . HIS   A 1 215 ? -15.533 -8.227  55.221  1.00 40.46 ? 709  HIS   A CB   1 
ATOM   1459 C  CG   . HIS   A 1 215 ? -16.538 -7.794  56.241  1.00 43.55 ? 709  HIS   A CG   1 
ATOM   1460 N  ND1  . HIS   A 1 215 ? -17.735 -7.200  55.901  1.00 43.06 ? 709  HIS   A ND1  1 
ATOM   1461 C  CD2  . HIS   A 1 215 ? -16.526 -7.870  57.593  1.00 44.60 ? 709  HIS   A CD2  1 
ATOM   1462 C  CE1  . HIS   A 1 215 ? -18.417 -6.929  57.000  1.00 48.07 ? 709  HIS   A CE1  1 
ATOM   1463 N  NE2  . HIS   A 1 215 ? -17.705 -7.325  58.040  1.00 46.57 ? 709  HIS   A NE2  1 
ATOM   1464 N  N    . ASN   A 1 216 ? -13.219 -6.869  52.883  1.00 33.91 ? 710  ASN   A N    1 
ATOM   1465 C  CA   . ASN   A 1 216 ? -12.432 -7.306  51.737  1.00 31.87 ? 710  ASN   A CA   1 
ATOM   1466 C  C    . ASN   A 1 216 ? -11.036 -7.739  52.173  1.00 33.87 ? 710  ASN   A C    1 
ATOM   1467 O  O    . ASN   A 1 216 ? -10.432 -7.143  53.069  1.00 31.74 ? 710  ASN   A O    1 
ATOM   1468 C  CB   . ASN   A 1 216 ? -12.338 -6.187  50.700  1.00 29.22 ? 710  ASN   A CB   1 
ATOM   1469 C  CG   . ASN   A 1 216 ? -13.568 -6.104  49.819  1.00 31.55 ? 710  ASN   A CG   1 
ATOM   1470 O  OD1  . ASN   A 1 216 ? -14.291 -7.085  49.649  1.00 26.49 ? 710  ASN   A OD1  1 
ATOM   1471 N  ND2  . ASN   A 1 216 ? -13.811 -4.929  49.251  1.00 28.50 ? 710  ASN   A ND2  1 
ATOM   1472 N  N    . TYR   A 1 217 ? -10.526 -8.784  51.530  1.00 29.87 ? 711  TYR   A N    1 
ATOM   1473 C  CA   . TYR   A 1 217 ? -9.257  -9.389  51.903  1.00 28.95 ? 711  TYR   A CA   1 
ATOM   1474 C  C    . TYR   A 1 217 ? -8.135  -8.926  50.979  1.00 28.33 ? 711  TYR   A C    1 
ATOM   1475 O  O    . TYR   A 1 217 ? -8.362  -8.484  49.850  1.00 27.45 ? 711  TYR   A O    1 
ATOM   1476 C  CB   . TYR   A 1 217 ? -9.364  -10.917 51.881  1.00 27.77 ? 711  TYR   A CB   1 
ATOM   1477 C  CG   . TYR   A 1 217 ? -10.061 -11.488 53.095  1.00 29.92 ? 711  TYR   A CG   1 
ATOM   1478 C  CD1  . TYR   A 1 217 ? -11.445 -11.448 53.209  1.00 28.13 ? 711  TYR   A CD1  1 
ATOM   1479 C  CD2  . TYR   A 1 217 ? -9.335  -12.058 54.132  1.00 31.57 ? 711  TYR   A CD2  1 
ATOM   1480 C  CE1  . TYR   A 1 217 ? -12.086 -11.964 54.320  1.00 26.28 ? 711  TYR   A CE1  1 
ATOM   1481 C  CE2  . TYR   A 1 217 ? -9.967  -12.577 55.246  1.00 32.61 ? 711  TYR   A CE2  1 
ATOM   1482 C  CZ   . TYR   A 1 217 ? -11.341 -12.527 55.335  1.00 32.59 ? 711  TYR   A CZ   1 
ATOM   1483 O  OH   . TYR   A 1 217 ? -11.972 -13.044 56.443  1.00 43.07 ? 711  TYR   A OH   1 
ATOM   1484 N  N    . GLU   A 1 218 ? -6.903  -9.039  51.484  1.00 25.56 ? 712  GLU   A N    1 
ATOM   1485 C  CA   . GLU   A 1 218 ? -5.747  -8.551  50.741  1.00 27.02 ? 712  GLU   A CA   1 
ATOM   1486 C  C    . GLU   A 1 218 ? -5.402  -9.452  49.562  1.00 23.63 ? 712  GLU   A C    1 
ATOM   1487 O  O    . GLU   A 1 218 ? -4.845  -8.977  48.566  1.00 22.72 ? 712  GLU   A O    1 
ATOM   1488 C  CB   . GLU   A 1 218 ? -4.544  -8.419  51.675  1.00 27.46 ? 712  GLU   A CB   1 
ATOM   1489 C  CG   . GLU   A 1 218 ? -4.752  -7.447  52.826  1.00 25.67 ? 712  GLU   A CG   1 
ATOM   1490 C  CD   . GLU   A 1 218 ? -4.838  -6.003  52.368  1.00 32.20 ? 712  GLU   A CD   1 
ATOM   1491 O  OE1  . GLU   A 1 218 ? -4.322  -5.692  51.274  1.00 35.80 ? 712  GLU   A OE1  1 
ATOM   1492 O  OE2  . GLU   A 1 218 ? -5.422  -5.179  53.101  1.00 35.64 ? 712  GLU   A OE2  1 
ATOM   1493 N  N    . SER   A 1 219 ? -5.714  -10.743 49.651  1.00 23.43 ? 713  SER   A N    1 
ATOM   1494 C  CA   . SER   A 1 219 ? -5.384  -11.679 48.589  1.00 21.38 ? 713  SER   A CA   1 
ATOM   1495 C  C    . SER   A 1 219 ? -6.456  -12.756 48.520  1.00 25.26 ? 713  SER   A C    1 
ATOM   1496 O  O    . SER   A 1 219 ? -7.141  -13.035 49.507  1.00 26.34 ? 713  SER   A O    1 
ATOM   1497 C  CB   . SER   A 1 219 ? -4.007  -12.316 48.804  1.00 21.05 ? 713  SER   A CB   1 
ATOM   1498 O  OG   . SER   A 1 219 ? -3.995  -13.121 49.971  1.00 26.88 ? 713  SER   A OG   1 
ATOM   1499 N  N    . ALA   A 1 220 ? -6.591  -13.357 47.335  1.00 23.46 ? 714  ALA   A N    1 
ATOM   1500 C  CA   . ALA   A 1 220 ? -7.568  -14.425 47.154  1.00 20.42 ? 714  ALA   A CA   1 
ATOM   1501 C  C    . ALA   A 1 220 ? -7.246  -15.623 48.037  1.00 27.30 ? 714  ALA   A C    1 
ATOM   1502 O  O    . ALA   A 1 220 ? -8.150  -16.239 48.613  1.00 29.99 ? 714  ALA   A O    1 
ATOM   1503 C  CB   . ALA   A 1 220 ? -7.622  -14.842 45.684  1.00 17.99 ? 714  ALA   A CB   1 
ATOM   1504 N  N    . ALA   A 1 221 ? -5.960  -15.962 48.162  1.00 21.04 ? 715  ALA   A N    1 
ATOM   1505 C  CA   . ALA   A 1 221 ? -5.570  -17.109 48.976  1.00 23.46 ? 715  ALA   A CA   1 
ATOM   1506 C  C    . ALA   A 1 221 ? -5.968  -16.916 50.433  1.00 29.41 ? 715  ALA   A C    1 
ATOM   1507 O  O    . ALA   A 1 221 ? -6.401  -17.866 51.098  1.00 31.74 ? 715  ALA   A O    1 
ATOM   1508 C  CB   . ALA   A 1 221 ? -4.066  -17.348 48.856  1.00 23.52 ? 715  ALA   A CB   1 
ATOM   1509 N  N    . GLU   A 1 222 ? -5.829  -15.693 50.949  1.00 25.61 ? 716  GLU   A N    1 
ATOM   1510 C  CA   . GLU   A 1 222 ? -6.237  -15.422 52.324  1.00 25.68 ? 716  GLU   A CA   1 
ATOM   1511 C  C    . GLU   A 1 222 ? -7.750  -15.518 52.479  1.00 30.67 ? 716  GLU   A C    1 
ATOM   1512 O  O    . GLU   A 1 222 ? -8.244  -16.064 53.472  1.00 30.62 ? 716  GLU   A O    1 
ATOM   1513 C  CB   . GLU   A 1 222 ? -5.736  -14.044 52.757  1.00 25.10 ? 716  GLU   A CB   1 
ATOM   1514 N  N    . ALA   A 1 223 ? -8.501  -14.996 51.505  1.00 30.72 ? 717  ALA   A N    1 
ATOM   1515 C  CA   . ALA   A 1 223 ? -9.956  -15.081 51.570  1.00 31.11 ? 717  ALA   A CA   1 
ATOM   1516 C  C    . ALA   A 1 223 ? -10.430 -16.525 51.457  1.00 31.81 ? 717  ALA   A C    1 
ATOM   1517 O  O    . ALA   A 1 223 ? -11.358 -16.935 52.165  1.00 31.39 ? 717  ALA   A O    1 
ATOM   1518 C  CB   . ALA   A 1 223 ? -10.582 -14.220 50.473  1.00 24.06 ? 717  ALA   A CB   1 
ATOM   1519 N  N    . ILE   A 1 224 ? -9.806  -17.309 50.574  1.00 26.19 ? 718  ILE   A N    1 
ATOM   1520 C  CA   . ILE   A 1 224 ? -10.144 -18.726 50.460  1.00 30.49 ? 718  ILE   A CA   1 
ATOM   1521 C  C    . ILE   A 1 224 ? -9.861  -19.442 51.775  1.00 34.15 ? 718  ILE   A C    1 
ATOM   1522 O  O    . ILE   A 1 224 ? -10.667 -20.251 52.251  1.00 35.84 ? 718  ILE   A O    1 
ATOM   1523 C  CB   . ILE   A 1 224 ? -9.376  -19.367 49.291  1.00 30.45 ? 718  ILE   A CB   1 
ATOM   1524 C  CG1  . ILE   A 1 224 ? -9.881  -18.820 47.954  1.00 28.56 ? 718  ILE   A CG1  1 
ATOM   1525 C  CG2  . ILE   A 1 224 ? -9.497  -20.883 49.336  1.00 28.39 ? 718  ILE   A CG2  1 
ATOM   1526 C  CD1  . ILE   A 1 224 ? -8.931  -19.058 46.803  1.00 25.15 ? 718  ILE   A CD1  1 
ATOM   1527 N  N    . GLN   A 1 225 ? -8.706  -19.153 52.381  1.00 34.42 ? 719  GLN   A N    1 
ATOM   1528 C  CA   . GLN   A 1 225 ? -8.388  -19.720 53.687  1.00 35.32 ? 719  GLN   A CA   1 
ATOM   1529 C  C    . GLN   A 1 225 ? -9.397  -19.278 54.739  1.00 37.26 ? 719  GLN   A C    1 
ATOM   1530 O  O    . GLN   A 1 225 ? -9.740  -20.047 55.645  1.00 41.57 ? 719  GLN   A O    1 
ATOM   1531 C  CB   . GLN   A 1 225 ? -6.972  -19.319 54.100  1.00 29.25 ? 719  GLN   A CB   1 
ATOM   1532 C  CG   . GLN   A 1 225 ? -6.498  -19.939 55.403  1.00 33.81 ? 719  GLN   A CG   1 
ATOM   1533 C  CD   . GLN   A 1 225 ? -6.402  -21.450 55.330  1.00 40.80 ? 719  GLN   A CD   1 
ATOM   1534 O  OE1  . GLN   A 1 225 ? -5.828  -22.002 54.392  1.00 43.92 ? 719  GLN   A OE1  1 
ATOM   1535 N  NE2  . GLN   A 1 225 ? -6.961  -22.128 56.326  1.00 35.72 ? 719  GLN   A NE2  1 
ATOM   1536 N  N    . ALA   A 1 226 ? -9.886  -18.040 54.633  1.00 37.06 ? 720  ALA   A N    1 
ATOM   1537 C  CA   . ALA   A 1 226 ? -10.871 -17.550 55.590  1.00 38.18 ? 720  ALA   A CA   1 
ATOM   1538 C  C    . ALA   A 1 226 ? -12.197 -18.290 55.465  1.00 40.57 ? 720  ALA   A C    1 
ATOM   1539 O  O    . ALA   A 1 226 ? -12.922 -18.431 56.456  1.00 42.71 ? 720  ALA   A O    1 
ATOM   1540 C  CB   . ALA   A 1 226 ? -11.080 -16.047 55.406  1.00 35.57 ? 720  ALA   A CB   1 
ATOM   1541 N  N    . VAL   A 1 227 ? -12.533 -18.765 54.263  1.00 36.76 ? 721  VAL   A N    1 
ATOM   1542 C  CA   . VAL   A 1 227 ? -13.746 -19.559 54.100  1.00 41.49 ? 721  VAL   A CA   1 
ATOM   1543 C  C    . VAL   A 1 227 ? -13.550 -20.951 54.689  1.00 46.01 ? 721  VAL   A C    1 
ATOM   1544 O  O    . VAL   A 1 227 ? -14.474 -21.527 55.276  1.00 45.49 ? 721  VAL   A O    1 
ATOM   1545 C  CB   . VAL   A 1 227 ? -14.152 -19.619 52.616  1.00 36.91 ? 721  VAL   A CB   1 
ATOM   1546 C  CG1  . VAL   A 1 227 ? -15.444 -20.404 52.449  1.00 39.18 ? 721  VAL   A CG1  1 
ATOM   1547 C  CG2  . VAL   A 1 227 ? -14.305 -18.216 52.051  1.00 33.56 ? 721  VAL   A CG2  1 
ATOM   1548 N  N    . ARG   A 1 228 ? -12.344 -21.509 54.547  1.00 46.25 ? 722  ARG   A N    1 
ATOM   1549 C  CA   . ARG   A 1 228 ? -12.052 -22.813 55.134  1.00 46.12 ? 722  ARG   A CA   1 
ATOM   1550 C  C    . ARG   A 1 228 ? -12.182 -22.775 56.651  1.00 44.35 ? 722  ARG   A C    1 
ATOM   1551 O  O    . ARG   A 1 228 ? -12.732 -23.699 57.260  1.00 44.81 ? 722  ARG   A O    1 
ATOM   1552 C  CB   . ARG   A 1 228 ? -10.647 -23.267 54.733  1.00 38.80 ? 722  ARG   A CB   1 
ATOM   1553 C  CG   . ARG   A 1 228 ? -10.428 -23.406 53.234  1.00 42.36 ? 722  ARG   A CG   1 
ATOM   1554 C  CD   . ARG   A 1 228 ? -10.280 -24.864 52.833  1.00 45.20 ? 722  ARG   A CD   1 
ATOM   1555 N  NE   . ARG   A 1 228 ? -8.906  -25.333 52.955  1.00 40.41 ? 722  ARG   A NE   1 
ATOM   1556 C  CZ   . ARG   A 1 228 ? -8.515  -26.575 52.704  1.00 44.35 ? 722  ARG   A CZ   1 
ATOM   1557 N  NH1  . ARG   A 1 228 ? -9.373  -27.505 52.318  1.00 36.00 ? 722  ARG   A NH1  1 
ATOM   1558 N  NH2  . ARG   A 1 228 ? -7.231  -26.892 52.846  1.00 50.99 ? 722  ARG   A NH2  1 
ATOM   1559 N  N    . ASP   A 1 229 ? -11.688 -21.711 57.278  1.00 45.23 ? 723  ASP   A N    1 
ATOM   1560 C  CA   . ASP   A 1 229 ? -11.693 -21.576 58.728  1.00 48.12 ? 723  ASP   A CA   1 
ATOM   1561 C  C    . ASP   A 1 229 ? -12.970 -20.934 59.260  1.00 48.75 ? 723  ASP   A C    1 
ATOM   1562 O  O    . ASP   A 1 229 ? -13.031 -20.605 60.450  1.00 49.69 ? 723  ASP   A O    1 
ATOM   1563 C  CB   . ASP   A 1 229 ? -10.471 -20.767 59.178  1.00 52.72 ? 723  ASP   A CB   1 
ATOM   1564 C  CG   . ASP   A 1 229 ? -9.170  -21.330 58.640  1.00 44.70 ? 723  ASP   A CG   1 
ATOM   1565 O  OD1  . ASP   A 1 229 ? -9.175  -22.480 58.145  1.00 54.70 ? 723  ASP   A OD1  1 
ATOM   1566 O  OD2  . ASP   A 1 229 ? -8.141  -20.627 58.706  1.00 40.60 ? 723  ASP   A OD2  1 
ATOM   1567 N  N    . ASN   A 1 230 ? -13.981 -20.752 58.406  1.00 62.63 ? 724  ASN   A N    1 
ATOM   1568 C  CA   . ASN   A 1 230 ? -15.280 -20.204 58.805  1.00 65.00 ? 724  ASN   A CA   1 
ATOM   1569 C  C    . ASN   A 1 230 ? -15.138 -18.819 59.437  1.00 64.85 ? 724  ASN   A C    1 
ATOM   1570 O  O    . ASN   A 1 230 ? -15.836 -18.476 60.394  1.00 66.68 ? 724  ASN   A O    1 
ATOM   1571 C  CB   . ASN   A 1 230 ? -16.025 -21.161 59.740  1.00 63.64 ? 724  ASN   A CB   1 
ATOM   1572 C  CG   . ASN   A 1 230 ? -17.533 -20.964 59.698  1.00 80.76 ? 724  ASN   A CG   1 
ATOM   1573 O  OD1  . ASN   A 1 230 ? -18.082 -20.104 60.386  1.00 86.99 ? 724  ASN   A OD1  1 
ATOM   1574 N  ND2  . ASN   A 1 230 ? -18.210 -21.764 58.879  1.00 84.02 ? 724  ASN   A ND2  1 
ATOM   1575 N  N    . LYS   A 1 231 ? -14.216 -18.016 58.905  1.00 55.82 ? 725  LYS   A N    1 
ATOM   1576 C  CA   . LYS   A 1 231 ? -14.167 -16.595 59.216  1.00 43.70 ? 725  LYS   A CA   1 
ATOM   1577 C  C    . LYS   A 1 231 ? -14.849 -15.748 58.153  1.00 44.63 ? 725  LYS   A C    1 
ATOM   1578 O  O    . LYS   A 1 231 ? -15.282 -14.630 58.453  1.00 42.04 ? 725  LYS   A O    1 
ATOM   1579 C  CB   . LYS   A 1 231 ? -12.714 -16.131 59.381  1.00 40.65 ? 725  LYS   A CB   1 
ATOM   1580 N  N    . LEU   A 1 232 ? -14.951 -16.263 56.930  1.00 43.53 ? 726  LEU   A N    1 
ATOM   1581 C  CA   . LEU   A 1 232 ? -15.672 -15.626 55.838  1.00 39.32 ? 726  LEU   A CA   1 
ATOM   1582 C  C    . LEU   A 1 232 ? -16.676 -16.633 55.300  1.00 39.32 ? 726  LEU   A C    1 
ATOM   1583 O  O    . LEU   A 1 232 ? -16.320 -17.789 55.049  1.00 38.42 ? 726  LEU   A O    1 
ATOM   1584 C  CB   . LEU   A 1 232 ? -14.710 -15.173 54.734  1.00 38.26 ? 726  LEU   A CB   1 
ATOM   1585 C  CG   . LEU   A 1 232 ? -15.312 -14.569 53.467  1.00 33.39 ? 726  LEU   A CG   1 
ATOM   1586 C  CD1  . LEU   A 1 232 ? -15.983 -13.248 53.787  1.00 31.01 ? 726  LEU   A CD1  1 
ATOM   1587 C  CD2  . LEU   A 1 232 ? -14.240 -14.386 52.406  1.00 34.92 ? 726  LEU   A CD2  1 
ATOM   1588 N  N    . HIS   A 1 233 ? -17.925 -16.205 55.132  1.00 37.10 ? 727  HIS   A N    1 
ATOM   1589 C  CA   . HIS   A 1 233 ? -18.994 -17.128 54.777  1.00 37.20 ? 727  HIS   A CA   1 
ATOM   1590 C  C    . HIS   A 1 233 ? -19.261 -17.209 53.278  1.00 34.50 ? 727  HIS   A C    1 
ATOM   1591 O  O    . HIS   A 1 233 ? -19.959 -18.131 52.842  1.00 40.45 ? 727  HIS   A O    1 
ATOM   1592 C  CB   . HIS   A 1 233 ? -20.283 -16.743 55.511  1.00 35.08 ? 727  HIS   A CB   1 
ATOM   1593 C  CG   . HIS   A 1 233 ? -20.113 -16.610 56.993  1.00 40.94 ? 727  HIS   A CG   1 
ATOM   1594 N  ND1  . HIS   A 1 233 ? -20.667 -15.578 57.717  1.00 43.59 ? 727  HIS   A ND1  1 
ATOM   1595 C  CD2  . HIS   A 1 233 ? -19.444 -17.379 57.885  1.00 43.61 ? 727  HIS   A CD2  1 
ATOM   1596 C  CE1  . HIS   A 1 233 ? -20.350 -15.716 58.992  1.00 45.71 ? 727  HIS   A CE1  1 
ATOM   1597 N  NE2  . HIS   A 1 233 ? -19.609 -16.802 59.121  1.00 45.85 ? 727  HIS   A NE2  1 
ATOM   1598 N  N    . ALA   A 1 234 ? -18.729 -16.281 52.484  1.00 34.55 ? 728  ALA   A N    1 
ATOM   1599 C  CA   . ALA   A 1 234 ? -18.900 -16.328 51.037  1.00 31.68 ? 728  ALA   A CA   1 
ATOM   1600 C  C    . ALA   A 1 234 ? -17.809 -15.492 50.388  1.00 29.43 ? 728  ALA   A C    1 
ATOM   1601 O  O    . ALA   A 1 234 ? -17.553 -14.364 50.819  1.00 28.00 ? 728  ALA   A O    1 
ATOM   1602 C  CB   . ALA   A 1 234 ? -20.285 -15.821 50.621  1.00 29.93 ? 728  ALA   A CB   1 
ATOM   1603 N  N    . PHE   A 1 235 ? -17.172 -16.044 49.358  1.00 26.95 ? 729  PHE   A N    1 
ATOM   1604 C  CA   . PHE   A 1 235 ? -16.106 -15.367 48.630  1.00 24.07 ? 729  PHE   A CA   1 
ATOM   1605 C  C    . PHE   A 1 235 ? -16.540 -15.192 47.182  1.00 24.34 ? 729  PHE   A C    1 
ATOM   1606 O  O    . PHE   A 1 235 ? -16.767 -16.179 46.474  1.00 25.51 ? 729  PHE   A O    1 
ATOM   1607 C  CB   . PHE   A 1 235 ? -14.798 -16.157 48.712  1.00 27.22 ? 729  PHE   A CB   1 
ATOM   1608 C  CG   . PHE   A 1 235 ? -13.626 -15.466 48.070  1.00 25.27 ? 729  PHE   A CG   1 
ATOM   1609 C  CD1  . PHE   A 1 235 ? -13.538 -14.084 48.053  1.00 23.49 ? 729  PHE   A CD1  1 
ATOM   1610 C  CD2  . PHE   A 1 235 ? -12.611 -16.204 47.481  1.00 26.01 ? 729  PHE   A CD2  1 
ATOM   1611 C  CE1  . PHE   A 1 235 ? -12.461 -13.451 47.461  1.00 27.09 ? 729  PHE   A CE1  1 
ATOM   1612 C  CE2  . PHE   A 1 235 ? -11.532 -15.577 46.889  1.00 21.13 ? 729  PHE   A CE2  1 
ATOM   1613 C  CZ   . PHE   A 1 235 ? -11.457 -14.199 46.879  1.00 28.14 ? 729  PHE   A CZ   1 
ATOM   1614 N  N    . ILE   A 1 236 ? -16.656 -13.941 46.747  1.00 24.44 ? 730  ILE   A N    1 
ATOM   1615 C  CA   . ILE   A 1 236 ? -17.020 -13.608 45.375  1.00 26.43 ? 730  ILE   A CA   1 
ATOM   1616 C  C    . ILE   A 1 236 ? -15.735 -13.331 44.607  1.00 25.55 ? 730  ILE   A C    1 
ATOM   1617 O  O    . ILE   A 1 236 ? -15.013 -12.374 44.914  1.00 23.71 ? 730  ILE   A O    1 
ATOM   1618 C  CB   . ILE   A 1 236 ? -17.974 -12.405 45.325  1.00 22.21 ? 730  ILE   A CB   1 
ATOM   1619 C  CG1  . ILE   A 1 236 ? -19.228 -12.692 46.155  1.00 23.30 ? 730  ILE   A CG1  1 
ATOM   1620 C  CG2  . ILE   A 1 236 ? -18.346 -12.079 43.887  1.00 22.71 ? 730  ILE   A CG2  1 
ATOM   1621 C  CD1  . ILE   A 1 236 ? -20.237 -11.564 46.151  1.00 22.57 ? 730  ILE   A CD1  1 
ATOM   1622 N  N    . TRP   A 1 237 ? -15.446 -14.165 43.612  1.00 22.84 ? 731  TRP   A N    1 
ATOM   1623 C  CA   . TRP   A 1 237 ? -14.159 -14.128 42.929  1.00 18.93 ? 731  TRP   A CA   1 
ATOM   1624 C  C    . TRP   A 1 237 ? -14.310 -14.792 41.565  1.00 20.90 ? 731  TRP   A C    1 
ATOM   1625 O  O    . TRP   A 1 237 ? -15.398 -15.229 41.181  1.00 23.97 ? 731  TRP   A O    1 
ATOM   1626 C  CB   . TRP   A 1 237 ? -13.082 -14.806 43.783  1.00 20.66 ? 731  TRP   A CB   1 
ATOM   1627 C  CG   . TRP   A 1 237 ? -11.668 -14.535 43.359  1.00 21.74 ? 731  TRP   A CG   1 
ATOM   1628 C  CD1  . TRP   A 1 237 ? -10.700 -15.464 43.109  1.00 19.99 ? 731  TRP   A CD1  1 
ATOM   1629 C  CD2  . TRP   A 1 237 ? -11.063 -13.255 43.134  1.00 21.75 ? 731  TRP   A CD2  1 
ATOM   1630 N  NE1  . TRP   A 1 237 ? -9.531  -14.843 42.744  1.00 20.94 ? 731  TRP   A NE1  1 
ATOM   1631 C  CE2  . TRP   A 1 237 ? -9.727  -13.487 42.752  1.00 21.72 ? 731  TRP   A CE2  1 
ATOM   1632 C  CE3  . TRP   A 1 237 ? -11.519 -11.936 43.220  1.00 19.57 ? 731  TRP   A CE3  1 
ATOM   1633 C  CZ2  . TRP   A 1 237 ? -8.844  -12.451 42.455  1.00 19.86 ? 731  TRP   A CZ2  1 
ATOM   1634 C  CZ3  . TRP   A 1 237 ? -10.643 -10.910 42.923  1.00 20.32 ? 731  TRP   A CZ3  1 
ATOM   1635 C  CH2  . TRP   A 1 237 ? -9.320  -11.173 42.547  1.00 19.82 ? 731  TRP   A CH2  1 
ATOM   1636 N  N    . ASP   A 1 238 ? -13.199 -14.860 40.832  1.00 19.53 ? 732  ASP   A N    1 
ATOM   1637 C  CA   . ASP   A 1 238 ? -13.204 -15.432 39.492  1.00 17.86 ? 732  ASP   A CA   1 
ATOM   1638 C  C    . ASP   A 1 238 ? -13.578 -16.909 39.531  1.00 22.61 ? 732  ASP   A C    1 
ATOM   1639 O  O    . ASP   A 1 238 ? -13.148 -17.654 40.415  1.00 22.09 ? 732  ASP   A O    1 
ATOM   1640 C  CB   . ASP   A 1 238 ? -11.830 -15.259 38.844  1.00 18.38 ? 732  ASP   A CB   1 
ATOM   1641 C  CG   . ASP   A 1 238 ? -11.510 -13.811 38.537  1.00 19.36 ? 732  ASP   A CG   1 
ATOM   1642 O  OD1  . ASP   A 1 238 ? -12.395 -13.104 38.010  1.00 14.26 ? 732  ASP   A OD1  1 
ATOM   1643 O  OD2  . ASP   A 1 238 ? -10.374 -13.377 38.824  1.00 16.63 ? 732  ASP   A OD2  1 
ATOM   1644 N  N    . SER   A 1 239 ? -14.376 -17.335 38.548  1.00 18.69 ? 733  SER   A N    1 
ATOM   1645 C  CA   . SER   A 1 239 ? -14.860 -18.712 38.536  1.00 20.84 ? 733  SER   A CA   1 
ATOM   1646 C  C    . SER   A 1 239 ? -13.758 -19.703 38.179  1.00 20.81 ? 733  SER   A C    1 
ATOM   1647 O  O    . SER   A 1 239 ? -13.748 -20.824 38.700  1.00 18.23 ? 733  SER   A O    1 
ATOM   1648 C  CB   . SER   A 1 239 ? -16.034 -18.849 37.565  1.00 21.58 ? 733  SER   A CB   1 
ATOM   1649 O  OG   . SER   A 1 239 ? -15.671 -18.439 36.259  1.00 18.04 ? 733  SER   A OG   1 
ATOM   1650 N  N    . ALA   A 1 240 ? -12.829 -19.320 37.300  1.00 19.46 ? 734  ALA   A N    1 
ATOM   1651 C  CA   . ALA   A 1 240 ? -11.736 -20.224 36.955  1.00 18.91 ? 734  ALA   A CA   1 
ATOM   1652 C  C    . ALA   A 1 240 ? -10.834 -20.490 38.152  1.00 21.93 ? 734  ALA   A C    1 
ATOM   1653 O  O    . ALA   A 1 240 ? -10.163 -21.527 38.207  1.00 25.07 ? 734  ALA   A O    1 
ATOM   1654 C  CB   . ALA   A 1 240 ? -10.926 -19.658 35.788  1.00 19.31 ? 734  ALA   A CB   1 
ATOM   1655 N  N    . VAL   A 1 241 ? -10.806 -19.576 39.117  1.00 17.34 ? 735  VAL   A N    1 
ATOM   1656 C  CA   . VAL   A 1 241 ? -10.027 -19.771 40.335  1.00 22.97 ? 735  VAL   A CA   1 
ATOM   1657 C  C    . VAL   A 1 241 ? -10.824 -20.536 41.383  1.00 25.04 ? 735  VAL   A C    1 
ATOM   1658 O  O    . VAL   A 1 241 ? -10.332 -21.503 41.969  1.00 25.34 ? 735  VAL   A O    1 
ATOM   1659 C  CB   . VAL   A 1 241 ? -9.549  -18.407 40.879  1.00 20.28 ? 735  VAL   A CB   1 
ATOM   1660 C  CG1  . VAL   A 1 241 ? -9.010  -18.558 42.291  1.00 19.59 ? 735  VAL   A CG1  1 
ATOM   1661 C  CG2  . VAL   A 1 241 ? -8.494  -17.809 39.961  1.00 19.91 ? 735  VAL   A CG2  1 
ATOM   1662 N  N    . LEU   A 1 242 ? -12.072 -20.121 41.621  1.00 22.21 ? 736  LEU   A N    1 
ATOM   1663 C  CA   . LEU   A 1 242 ? -12.868 -20.730 42.682  1.00 24.35 ? 736  LEU   A CA   1 
ATOM   1664 C  C    . LEU   A 1 242 ? -13.221 -22.177 42.358  1.00 30.88 ? 736  LEU   A C    1 
ATOM   1665 O  O    . LEU   A 1 242 ? -13.230 -23.032 43.251  1.00 34.82 ? 736  LEU   A O    1 
ATOM   1666 C  CB   . LEU   A 1 242 ? -14.134 -19.910 42.926  1.00 21.59 ? 736  LEU   A CB   1 
ATOM   1667 C  CG   . LEU   A 1 242 ? -13.923 -18.473 43.408  1.00 22.30 ? 736  LEU   A CG   1 
ATOM   1668 C  CD1  . LEU   A 1 242 ? -15.250 -17.820 43.771  1.00 22.91 ? 736  LEU   A CD1  1 
ATOM   1669 C  CD2  . LEU   A 1 242 ? -12.956 -18.433 44.583  1.00 22.31 ? 736  LEU   A CD2  1 
ATOM   1670 N  N    . GLU   A 1 243 ? -13.521 -22.471 41.090  1.00 31.35 ? 737  GLU   A N    1 
ATOM   1671 C  CA   . GLU   A 1 243 ? -13.858 -23.843 40.723  1.00 27.55 ? 737  GLU   A CA   1 
ATOM   1672 C  C    . GLU   A 1 243 ? -12.646 -24.762 40.802  1.00 30.14 ? 737  GLU   A C    1 
ATOM   1673 O  O    . GLU   A 1 243 ? -12.791 -25.948 41.118  1.00 27.34 ? 737  GLU   A O    1 
ATOM   1674 C  CB   . GLU   A 1 243 ? -14.474 -23.881 39.325  1.00 21.79 ? 737  GLU   A CB   1 
ATOM   1675 C  CG   . GLU   A 1 243 ? -15.914 -23.394 39.280  1.00 31.39 ? 737  GLU   A CG   1 
ATOM   1676 C  CD   . GLU   A 1 243 ? -16.348 -22.966 37.893  1.00 42.74 ? 737  GLU   A CD   1 
ATOM   1677 O  OE1  . GLU   A 1 243 ? -15.480 -22.849 37.004  1.00 37.26 ? 737  GLU   A OE1  1 
ATOM   1678 O  OE2  . GLU   A 1 243 ? -17.561 -22.743 37.693  1.00 45.10 ? 737  GLU   A OE2  1 
ATOM   1679 N  N    . PHE   A 1 244 ? -11.449 -24.240 40.522  1.00 32.38 ? 738  PHE   A N    1 
ATOM   1680 C  CA   . PHE   A 1 244 ? -10.240 -25.031 40.732  1.00 32.80 ? 738  PHE   A CA   1 
ATOM   1681 C  C    . PHE   A 1 244 ? -10.038 -25.332 42.211  1.00 32.58 ? 738  PHE   A C    1 
ATOM   1682 O  O    . PHE   A 1 244 ? -9.622  -26.437 42.577  1.00 35.64 ? 738  PHE   A O    1 
ATOM   1683 C  CB   . PHE   A 1 244 ? -9.021  -24.302 40.164  1.00 27.47 ? 738  PHE   A CB   1 
ATOM   1684 C  CG   . PHE   A 1 244 ? -7.706  -24.887 40.604  1.00 32.50 ? 738  PHE   A CG   1 
ATOM   1685 C  CD1  . PHE   A 1 244 ? -7.172  -25.987 39.953  1.00 31.44 ? 738  PHE   A CD1  1 
ATOM   1686 C  CD2  . PHE   A 1 244 ? -7.003  -24.338 41.666  1.00 30.79 ? 738  PHE   A CD2  1 
ATOM   1687 C  CE1  . PHE   A 1 244 ? -5.965  -26.529 40.353  1.00 35.51 ? 738  PHE   A CE1  1 
ATOM   1688 C  CE2  . PHE   A 1 244 ? -5.796  -24.877 42.070  1.00 27.67 ? 738  PHE   A CE2  1 
ATOM   1689 C  CZ   . PHE   A 1 244 ? -5.277  -25.973 41.413  1.00 27.18 ? 738  PHE   A CZ   1 
ATOM   1690 N  N    . GLU   A 1 245 ? -10.318 -24.353 43.075  1.00 30.19 ? 739  GLU   A N    1 
ATOM   1691 C  CA   . GLU   A 1 245 ? -10.180 -24.567 44.511  1.00 31.25 ? 739  GLU   A CA   1 
ATOM   1692 C  C    . GLU   A 1 245 ? -11.179 -25.599 45.013  1.00 36.40 ? 739  GLU   A C    1 
ATOM   1693 O  O    . GLU   A 1 245 ? -10.857 -26.408 45.892  1.00 38.58 ? 739  GLU   A O    1 
ATOM   1694 C  CB   . GLU   A 1 245 ? -10.357 -23.244 45.257  1.00 31.87 ? 739  GLU   A CB   1 
ATOM   1695 C  CG   . GLU   A 1 245 ? -9.239  -22.244 45.022  1.00 33.39 ? 739  GLU   A CG   1 
ATOM   1696 C  CD   . GLU   A 1 245 ? -7.987  -22.569 45.812  1.00 34.68 ? 739  GLU   A CD   1 
ATOM   1697 O  OE1  . GLU   A 1 245 ? -8.058  -23.425 46.718  1.00 35.68 ? 739  GLU   A OE1  1 
ATOM   1698 O  OE2  . GLU   A 1 245 ? -6.930  -21.968 45.528  1.00 34.67 ? 739  GLU   A OE2  1 
ATOM   1699 N  N    . ALA   A 1 246 ? -12.398 -25.587 44.469  1.00 36.73 ? 740  ALA   A N    1 
ATOM   1700 C  CA   . ALA   A 1 246 ? -13.396 -26.566 44.882  1.00 37.08 ? 740  ALA   A CA   1 
ATOM   1701 C  C    . ALA   A 1 246 ? -13.046 -27.965 44.394  1.00 38.13 ? 740  ALA   A C    1 
ATOM   1702 O  O    . ALA   A 1 246 ? -13.476 -28.955 44.996  1.00 38.28 ? 740  ALA   A O    1 
ATOM   1703 C  CB   . ALA   A 1 246 ? -14.776 -26.157 44.374  1.00 35.04 ? 740  ALA   A CB   1 
ATOM   1704 N  N    . SER   A 1 247 ? -12.270 -28.070 43.312  1.00 38.66 ? 741  SER   A N    1 
ATOM   1705 C  CA   . SER   A 1 247 ? -11.897 -29.377 42.783  1.00 37.74 ? 741  SER   A CA   1 
ATOM   1706 C  C    . SER   A 1 247 ? -10.772 -30.020 43.582  1.00 39.14 ? 741  SER   A C    1 
ATOM   1707 O  O    . SER   A 1 247 ? -10.663 -31.250 43.604  1.00 43.03 ? 741  SER   A O    1 
ATOM   1708 C  CB   . SER   A 1 247 ? -11.492 -29.253 41.313  1.00 34.83 ? 741  SER   A CB   1 
ATOM   1709 O  OG   . SER   A 1 247 ? -10.250 -28.585 41.179  1.00 43.77 ? 741  SER   A OG   1 
ATOM   1710 N  N    . GLN   A 1 248 ? -9.932  -29.218 44.235  1.00 43.11 ? 742  GLN   A N    1 
ATOM   1711 C  CA   . GLN   A 1 248 ? -8.835  -29.738 45.042  1.00 47.65 ? 742  GLN   A CA   1 
ATOM   1712 C  C    . GLN   A 1 248 ? -9.151  -29.781 46.529  1.00 46.61 ? 742  GLN   A C    1 
ATOM   1713 O  O    . GLN   A 1 248 ? -8.572  -30.599 47.251  1.00 47.52 ? 742  GLN   A O    1 
ATOM   1714 C  CB   . GLN   A 1 248 ? -7.570  -28.899 44.824  1.00 48.16 ? 742  GLN   A CB   1 
ATOM   1715 C  CG   . GLN   A 1 248 ? -7.035  -28.928 43.400  1.00 47.89 ? 742  GLN   A CG   1 
ATOM   1716 C  CD   . GLN   A 1 248 ? -6.929  -30.335 42.838  1.00 62.43 ? 742  GLN   A CD   1 
ATOM   1717 O  OE1  . GLN   A 1 248 ? -7.426  -30.618 41.748  1.00 56.20 ? 742  GLN   A OE1  1 
ATOM   1718 N  NE2  . GLN   A 1 248 ? -6.268  -31.221 43.575  1.00 66.97 ? 742  GLN   A NE2  1 
ATOM   1719 N  N    . LYS   A 1 249 ? -10.048 -28.921 47.002  1.00 45.28 ? 743  LYS   A N    1 
ATOM   1720 C  CA   . LYS   A 1 249 ? -10.438 -28.858 48.408  1.00 44.48 ? 743  LYS   A CA   1 
ATOM   1721 C  C    . LYS   A 1 249 ? -11.937 -29.137 48.479  1.00 43.34 ? 743  LYS   A C    1 
ATOM   1722 O  O    . LYS   A 1 249 ? -12.755 -28.263 48.179  1.00 43.60 ? 743  LYS   A O    1 
ATOM   1723 C  CB   . LYS   A 1 249 ? -10.076 -27.503 49.009  1.00 41.61 ? 743  LYS   A CB   1 
ATOM   1724 C  CG   . LYS   A 1 249 ? -8.596  -27.169 48.880  1.00 37.94 ? 743  LYS   A CG   1 
ATOM   1725 C  CD   . LYS   A 1 249 ? -8.304  -25.715 49.203  1.00 35.21 ? 743  LYS   A CD   1 
ATOM   1726 C  CE   . LYS   A 1 249 ? -6.838  -25.391 48.955  1.00 34.36 ? 743  LYS   A CE   1 
ATOM   1727 N  NZ   . LYS   A 1 249 ? -6.578  -23.925 48.959  1.00 34.25 ? 743  LYS   A NZ   1 
ATOM   1728 N  N    . CYS   A 1 250 ? -12.290 -30.360 48.875  1.00 41.16 ? 744  CYS   A N    1 
ATOM   1729 C  CA   . CYS   A 1 250 ? -13.666 -30.836 48.809  1.00 41.28 ? 744  CYS   A CA   1 
ATOM   1730 C  C    . CYS   A 1 250 ? -14.547 -30.308 49.935  1.00 42.97 ? 744  CYS   A C    1 
ATOM   1731 O  O    . CYS   A 1 250 ? -15.742 -30.622 49.958  1.00 41.02 ? 744  CYS   A O    1 
ATOM   1732 C  CB   . CYS   A 1 250 ? -13.687 -32.366 48.808  1.00 34.54 ? 744  CYS   A CB   1 
ATOM   1733 S  SG   . CYS   A 1 250 ? -12.947 -33.106 47.332  1.00 52.33 ? 744  CYS   A SG   1 
ATOM   1734 N  N    . ASP   A 1 251 ? -14.001 -29.529 50.865  1.00 33.41 ? 745  ASP   A N    1 
ATOM   1735 C  CA   . ASP   A 1 251 ? -14.811 -28.833 51.854  1.00 34.21 ? 745  ASP   A CA   1 
ATOM   1736 C  C    . ASP   A 1 251 ? -15.292 -27.479 51.351  1.00 41.40 ? 745  ASP   A C    1 
ATOM   1737 O  O    . ASP   A 1 251 ? -15.901 -26.724 52.117  1.00 40.11 ? 745  ASP   A O    1 
ATOM   1738 C  CB   . ASP   A 1 251 ? -14.030 -28.661 53.160  1.00 38.92 ? 745  ASP   A CB   1 
ATOM   1739 C  CG   . ASP   A 1 251 ? -12.679 -28.011 52.950  1.00 42.21 ? 745  ASP   A CG   1 
ATOM   1740 O  OD1  . ASP   A 1 251 ? -11.983 -28.378 51.980  1.00 44.13 ? 745  ASP   A OD1  1 
ATOM   1741 O  OD2  . ASP   A 1 251 ? -12.314 -27.130 53.756  1.00 46.04 ? 745  ASP   A OD2  1 
ATOM   1742 N  N    . LEU   A 1 252 ? -15.032 -27.160 50.085  1.00 37.75 ? 746  LEU   A N    1 
ATOM   1743 C  CA   . LEU   A 1 252 ? -15.442 -25.905 49.476  1.00 38.17 ? 746  LEU   A CA   1 
ATOM   1744 C  C    . LEU   A 1 252 ? -16.239 -26.194 48.214  1.00 40.21 ? 746  LEU   A C    1 
ATOM   1745 O  O    . LEU   A 1 252 ? -15.871 -27.068 47.423  1.00 38.03 ? 746  LEU   A O    1 
ATOM   1746 C  CB   . LEU   A 1 252 ? -14.231 -25.030 49.135  1.00 35.23 ? 746  LEU   A CB   1 
ATOM   1747 C  CG   . LEU   A 1 252 ? -13.385 -24.540 50.310  1.00 32.93 ? 746  LEU   A CG   1 
ATOM   1748 C  CD1  . LEU   A 1 252 ? -12.061 -23.980 49.813  1.00 35.29 ? 746  LEU   A CD1  1 
ATOM   1749 C  CD2  . LEU   A 1 252 ? -14.147 -23.502 51.114  1.00 36.44 ? 746  LEU   A CD2  1 
ATOM   1750 N  N    . VAL   A 1 253 ? -17.334 -25.458 48.031  1.00 36.64 ? 747  VAL   A N    1 
ATOM   1751 C  CA   . VAL   A 1 253 ? -18.185 -25.596 46.858  1.00 36.10 ? 747  VAL   A CA   1 
ATOM   1752 C  C    . VAL   A 1 253 ? -18.511 -24.212 46.317  1.00 34.36 ? 747  VAL   A C    1 
ATOM   1753 O  O    . VAL   A 1 253 ? -18.500 -23.216 47.048  1.00 34.20 ? 747  VAL   A O    1 
ATOM   1754 C  CB   . VAL   A 1 253 ? -19.487 -26.373 47.166  1.00 34.58 ? 747  VAL   A CB   1 
ATOM   1755 C  CG1  . VAL   A 1 253 ? -19.173 -27.778 47.663  1.00 40.18 ? 747  VAL   A CG1  1 
ATOM   1756 C  CG2  . VAL   A 1 253 ? -20.330 -25.617 48.181  1.00 36.19 ? 747  VAL   A CG2  1 
ATOM   1757 N  N    . THR   A 1 254 ? -18.790 -24.154 45.019  1.00 34.56 ? 748  THR   A N    1 
ATOM   1758 C  CA   . THR   A 1 254 ? -19.275 -22.944 44.374  1.00 32.70 ? 748  THR   A CA   1 
ATOM   1759 C  C    . THR   A 1 254 ? -20.782 -23.061 44.198  1.00 43.36 ? 748  THR   A C    1 
ATOM   1760 O  O    . THR   A 1 254 ? -21.282 -24.109 43.776  1.00 51.15 ? 748  THR   A O    1 
ATOM   1761 C  CB   . THR   A 1 254 ? -18.600 -22.723 43.020  1.00 34.54 ? 748  THR   A CB   1 
ATOM   1762 O  OG1  . THR   A 1 254 ? -19.033 -23.731 42.098  1.00 29.54 ? 748  THR   A OG1  1 
ATOM   1763 C  CG2  . THR   A 1 254 ? -17.086 -22.786 43.161  1.00 30.00 ? 748  THR   A CG2  1 
ATOM   1764 N  N    . THR   A 1 255 ? -21.499 -21.995 44.531  1.00 41.79 ? 749  THR   A N    1 
ATOM   1765 C  CA   . THR   A 1 255 ? -22.953 -21.977 44.464  1.00 46.64 ? 749  THR   A CA   1 
ATOM   1766 C  C    . THR   A 1 255 ? -23.408 -21.260 43.201  1.00 49.69 ? 749  THR   A C    1 
ATOM   1767 O  O    . THR   A 1 255 ? -22.875 -20.200 42.855  1.00 46.92 ? 749  THR   A O    1 
ATOM   1768 C  CB   . THR   A 1 255 ? -23.544 -21.308 45.706  1.00 47.03 ? 749  THR   A CB   1 
ATOM   1769 O  OG1  . THR   A 1 255 ? -24.949 -21.100 45.520  1.00 50.54 ? 749  THR   A OG1  1 
ATOM   1770 C  CG2  . THR   A 1 255 ? -22.846 -19.986 45.991  1.00 38.08 ? 749  THR   A CG2  1 
ATOM   1771 N  N    . GLY   A 1 256 ? -24.379 -21.850 42.510  1.00 67.43 ? 750  GLY   A N    1 
ATOM   1772 C  CA   . GLY   A 1 256 ? -24.863 -21.299 41.260  1.00 68.47 ? 750  GLY   A CA   1 
ATOM   1773 C  C    . GLY   A 1 256 ? -23.811 -21.352 40.164  1.00 69.95 ? 750  GLY   A C    1 
ATOM   1774 O  O    . GLY   A 1 256 ? -22.682 -21.804 40.347  1.00 64.95 ? 750  GLY   A O    1 
ATOM   1775 N  N    . GLU   A 1 257 ? -24.212 -20.873 38.988  1.00 56.31 ? 751  GLU   A N    1 
ATOM   1776 C  CA   . GLU   A 1 257 ? -23.297 -20.793 37.858  1.00 47.69 ? 751  GLU   A CA   1 
ATOM   1777 C  C    . GLU   A 1 257 ? -22.554 -19.465 37.882  1.00 42.39 ? 751  GLU   A C    1 
ATOM   1778 O  O    . GLU   A 1 257 ? -22.027 -19.058 38.923  1.00 40.43 ? 751  GLU   A O    1 
ATOM   1779 C  CB   . GLU   A 1 257 ? -24.055 -20.963 36.540  1.00 50.84 ? 751  GLU   A CB   1 
ATOM   1780 N  N    . LEU   A 1 258 ? -22.511 -18.782 36.744  1.00 37.60 ? 752  LEU   A N    1 
ATOM   1781 C  CA   . LEU   A 1 258 ? -21.893 -17.468 36.640  1.00 30.70 ? 752  LEU   A CA   1 
ATOM   1782 C  C    . LEU   A 1 258 ? -22.985 -16.410 36.565  1.00 30.46 ? 752  LEU   A C    1 
ATOM   1783 O  O    . LEU   A 1 258 ? -23.859 -16.475 35.694  1.00 41.89 ? 752  LEU   A O    1 
ATOM   1784 C  CB   . LEU   A 1 258 ? -20.990 -17.378 35.407  1.00 27.77 ? 752  LEU   A CB   1 
ATOM   1785 C  CG   . LEU   A 1 258 ? -20.167 -18.588 34.950  1.00 31.78 ? 752  LEU   A CG   1 
ATOM   1786 C  CD1  . LEU   A 1 258 ? -19.191 -18.173 33.862  1.00 24.80 ? 752  LEU   A CD1  1 
ATOM   1787 C  CD2  . LEU   A 1 258 ? -19.412 -19.227 36.107  1.00 30.62 ? 752  LEU   A CD2  1 
ATOM   1788 N  N    . PHE   A 1 259 ? -22.943 -15.447 37.484  1.00 27.71 ? 753  PHE   A N    1 
ATOM   1789 C  CA   . PHE   A 1 259 ? -23.842 -14.302 37.422  1.00 26.72 ? 753  PHE   A CA   1 
ATOM   1790 C  C    . PHE   A 1 259 ? -23.258 -13.151 36.614  1.00 22.39 ? 753  PHE   A C    1 
ATOM   1791 O  O    . PHE   A 1 259 ? -23.879 -12.086 36.536  1.00 21.72 ? 753  PHE   A O    1 
ATOM   1792 C  CB   . PHE   A 1 259 ? -24.208 -13.825 38.835  1.00 25.88 ? 753  PHE   A CB   1 
ATOM   1793 C  CG   . PHE   A 1 259 ? -23.042 -13.308 39.637  1.00 24.11 ? 753  PHE   A CG   1 
ATOM   1794 C  CD1  . PHE   A 1 259 ? -22.676 -11.972 39.575  1.00 27.06 ? 753  PHE   A CD1  1 
ATOM   1795 C  CD2  . PHE   A 1 259 ? -22.327 -14.153 40.471  1.00 24.70 ? 753  PHE   A CD2  1 
ATOM   1796 C  CE1  . PHE   A 1 259 ? -21.613 -11.492 40.315  1.00 25.76 ? 753  PHE   A CE1  1 
ATOM   1797 C  CE2  . PHE   A 1 259 ? -21.261 -13.677 41.216  1.00 26.92 ? 753  PHE   A CE2  1 
ATOM   1798 C  CZ   . PHE   A 1 259 ? -20.906 -12.345 41.138  1.00 25.49 ? 753  PHE   A CZ   1 
ATOM   1799 N  N    . PHE   A 1 260 ? -22.089 -13.348 36.009  1.00 20.97 ? 754  PHE   A N    1 
ATOM   1800 C  CA   . PHE   A 1 260 ? -21.404 -12.324 35.234  1.00 18.80 ? 754  PHE   A CA   1 
ATOM   1801 C  C    . PHE   A 1 260 ? -20.276 -12.986 34.460  1.00 23.21 ? 754  PHE   A C    1 
ATOM   1802 O  O    . PHE   A 1 260 ? -19.561 -13.826 35.007  1.00 24.95 ? 754  PHE   A O    1 
ATOM   1803 C  CB   . PHE   A 1 260 ? -20.849 -11.221 36.145  1.00 23.20 ? 754  PHE   A CB   1 
ATOM   1804 C  CG   . PHE   A 1 260 ? -20.291 -10.044 35.402  1.00 26.26 ? 754  PHE   A CG   1 
ATOM   1805 C  CD1  . PHE   A 1 260 ? -21.123 -9.211  34.673  1.00 24.07 ? 754  PHE   A CD1  1 
ATOM   1806 C  CD2  . PHE   A 1 260 ? -18.934 -9.765  35.437  1.00 27.93 ? 754  PHE   A CD2  1 
ATOM   1807 C  CE1  . PHE   A 1 260 ? -20.613 -8.125  33.991  1.00 28.02 ? 754  PHE   A CE1  1 
ATOM   1808 C  CE2  . PHE   A 1 260 ? -18.417 -8.677  34.755  1.00 28.22 ? 754  PHE   A CE2  1 
ATOM   1809 C  CZ   . PHE   A 1 260 ? -19.258 -7.857  34.032  1.00 28.58 ? 754  PHE   A CZ   1 
ATOM   1810 N  N    . ARG   A 1 261 ? -20.129 -12.614 33.192  1.00 18.08 ? 755  ARG   A N    1 
ATOM   1811 C  CA   . ARG   A 1 261 ? -19.066 -13.134 32.344  1.00 18.01 ? 755  ARG   A CA   1 
ATOM   1812 C  C    . ARG   A 1 261 ? -17.897 -12.159 32.312  1.00 22.40 ? 755  ARG   A C    1 
ATOM   1813 O  O    . ARG   A 1 261 ? -18.088 -10.948 32.174  1.00 23.67 ? 755  ARG   A O    1 
ATOM   1814 C  CB   . ARG   A 1 261 ? -19.561 -13.384 30.917  1.00 20.06 ? 755  ARG   A CB   1 
ATOM   1815 C  CG   . ARG   A 1 261 ? -20.605 -14.478 30.781  1.00 25.74 ? 755  ARG   A CG   1 
ATOM   1816 C  CD   . ARG   A 1 261 ? -20.897 -14.750 29.311  1.00 21.18 ? 755  ARG   A CD   1 
ATOM   1817 N  NE   . ARG   A 1 261 ? -22.109 -15.537 29.119  1.00 23.09 ? 755  ARG   A NE   1 
ATOM   1818 C  CZ   . ARG   A 1 261 ? -23.333 -15.030 29.093  1.00 30.37 ? 755  ARG   A CZ   1 
ATOM   1819 N  NH1  . ARG   A 1 261 ? -23.549 -13.736 29.263  1.00 23.07 ? 755  ARG   A NH1  1 
ATOM   1820 N  NH2  . ARG   A 1 261 ? -24.368 -15.841 28.891  1.00 27.11 ? 755  ARG   A NH2  1 
ATOM   1821 N  N    . SER   A 1 262 ? -16.686 -12.694 32.439  1.00 21.18 ? 756  SER   A N    1 
ATOM   1822 C  CA   . SER   A 1 262 ? -15.479 -11.886 32.346  1.00 18.99 ? 756  SER   A CA   1 
ATOM   1823 C  C    . SER   A 1 262 ? -14.377 -12.725 31.716  1.00 18.95 ? 756  SER   A C    1 
ATOM   1824 O  O    . SER   A 1 262 ? -14.477 -13.951 31.618  1.00 16.84 ? 756  SER   A O    1 
ATOM   1825 C  CB   . SER   A 1 262 ? -15.048 -11.353 33.717  1.00 18.72 ? 756  SER   A CB   1 
ATOM   1826 O  OG   . SER   A 1 262 ? -14.916 -12.401 34.660  1.00 21.64 ? 756  SER   A OG   1 
ATOM   1827 N  N    . GLY   A 1 263 ? -13.321 -12.048 31.287  1.00 19.06 ? 757  GLY   A N    1 
ATOM   1828 C  CA   . GLY   A 1 263 ? -12.215 -12.714 30.627  1.00 18.02 ? 757  GLY   A CA   1 
ATOM   1829 C  C    . GLY   A 1 263 ? -10.892 -12.087 31.005  1.00 18.29 ? 757  GLY   A C    1 
ATOM   1830 O  O    . GLY   A 1 263 ? -10.814 -10.911 31.374  1.00 18.74 ? 757  GLY   A O    1 
ATOM   1831 N  N    . PHE   A 1 264 ? -9.841  -12.897 30.912  1.00 15.95 ? 758  PHE   A N    1 
ATOM   1832 C  CA   . PHE   A 1 264 ? -8.482  -12.463 31.205  1.00 16.48 ? 758  PHE   A CA   1 
ATOM   1833 C  C    . PHE   A 1 264 ? -7.753  -12.109 29.917  1.00 15.92 ? 758  PHE   A C    1 
ATOM   1834 O  O    . PHE   A 1 264 ? -7.955  -12.754 28.885  1.00 16.80 ? 758  PHE   A O    1 
ATOM   1835 C  CB   . PHE   A 1 264 ? -7.701  -13.551 31.945  1.00 18.64 ? 758  PHE   A CB   1 
ATOM   1836 C  CG   . PHE   A 1 264 ? -8.354  -14.025 33.206  1.00 17.97 ? 758  PHE   A CG   1 
ATOM   1837 C  CD1  . PHE   A 1 264 ? -9.033  -13.142 34.029  1.00 14.16 ? 758  PHE   A CD1  1 
ATOM   1838 C  CD2  . PHE   A 1 264 ? -8.281  -15.358 33.573  1.00 18.14 ? 758  PHE   A CD2  1 
ATOM   1839 C  CE1  . PHE   A 1 264 ? -9.632  -13.583 35.197  1.00 14.56 ? 758  PHE   A CE1  1 
ATOM   1840 C  CE2  . PHE   A 1 264 ? -8.878  -15.806 34.739  1.00 18.09 ? 758  PHE   A CE2  1 
ATOM   1841 C  CZ   . PHE   A 1 264 ? -9.549  -14.916 35.553  1.00 15.81 ? 758  PHE   A CZ   1 
ATOM   1842 N  N    . GLY   A 1 265 ? -6.891  -11.104 29.986  1.00 17.38 ? 759  GLY   A N    1 
ATOM   1843 C  CA   . GLY   A 1 265 ? -6.160  -10.663 28.814  1.00 15.59 ? 759  GLY   A CA   1 
ATOM   1844 C  C    . GLY   A 1 265 ? -4.750  -10.244 29.164  1.00 19.63 ? 759  GLY   A C    1 
ATOM   1845 O  O    . GLY   A 1 265 ? -4.459  -9.818  30.286  1.00 17.32 ? 759  GLY   A O    1 
ATOM   1846 N  N    . ILE   A 1 266 ? -3.864  -10.375 28.174  1.00 15.99 ? 760  ILE   A N    1 
ATOM   1847 C  CA   . ILE   A 1 266 ? -2.519  -9.834  28.314  1.00 15.02 ? 760  ILE   A CA   1 
ATOM   1848 C  C    . ILE   A 1 266 ? -2.616  -8.314  28.364  1.00 17.07 ? 760  ILE   A C    1 
ATOM   1849 O  O    . ILE   A 1 266 ? -3.429  -7.701  27.654  1.00 17.16 ? 760  ILE   A O    1 
ATOM   1850 C  CB   . ILE   A 1 266 ? -1.622  -10.307 27.156  1.00 18.30 ? 760  ILE   A CB   1 
ATOM   1851 C  CG1  . ILE   A 1 266 ? -1.684  -11.827 27.004  1.00 18.64 ? 760  ILE   A CG1  1 
ATOM   1852 C  CG2  . ILE   A 1 266 ? -0.193  -9.845  27.355  1.00 12.86 ? 760  ILE   A CG2  1 
ATOM   1853 C  CD1  . ILE   A 1 266 ? -0.948  -12.587 28.110  1.00 16.22 ? 760  ILE   A CD1  1 
ATOM   1854 N  N    . GLY   A 1 267 ? -1.806  -7.698  29.221  1.00 14.98 ? 761  GLY   A N    1 
ATOM   1855 C  CA   . GLY   A 1 267 ? -1.827  -6.262  29.421  1.00 18.60 ? 761  GLY   A CA   1 
ATOM   1856 C  C    . GLY   A 1 267 ? -0.520  -5.622  28.989  1.00 17.91 ? 761  GLY   A C    1 
ATOM   1857 O  O    . GLY   A 1 267 ? 0.558   -6.007  29.452  1.00 19.50 ? 761  GLY   A O    1 
ATOM   1858 N  N    . MET   A 1 268 ? -0.633  -4.668  28.064  1.00 20.78 ? 762  MET   A N    1 
ATOM   1859 C  CA   . MET   A 1 268 ? 0.505   -3.903  27.581  1.00 23.13 ? 762  MET   A CA   1 
ATOM   1860 C  C    . MET   A 1 268 ? 0.123   -2.433  27.514  1.00 24.24 ? 762  MET   A C    1 
ATOM   1861 O  O    . MET   A 1 268 ? -1.059  -2.077  27.521  1.00 25.63 ? 762  MET   A O    1 
ATOM   1862 C  CB   . MET   A 1 268 ? 0.967   -4.366  26.190  1.00 26.26 ? 762  MET   A CB   1 
ATOM   1863 C  CG   . MET   A 1 268 ? 1.342   -5.831  26.078  1.00 28.08 ? 762  MET   A CG   1 
ATOM   1864 S  SD   . MET   A 1 268 ? 0.609   -6.615  24.626  1.00 42.60 ? 762  MET   A SD   1 
ATOM   1865 C  CE   . MET   A 1 268 ? -1.126  -6.615  25.078  1.00 21.30 ? 762  MET   A CE   1 
ATOM   1866 N  N    . ARG   A 1 269 ? 1.141   -1.580  27.445  1.00 25.87 ? 763  ARG   A N    1 
ATOM   1867 C  CA   . ARG   A 1 269 ? 0.906   -0.167  27.198  1.00 25.32 ? 763  ARG   A CA   1 
ATOM   1868 C  C    . ARG   A 1 269 ? 0.418   0.040   25.769  1.00 26.78 ? 763  ARG   A C    1 
ATOM   1869 O  O    . ARG   A 1 269 ? 0.710   -0.748  24.866  1.00 25.13 ? 763  ARG   A O    1 
ATOM   1870 C  CB   . ARG   A 1 269 ? 2.179   0.640   27.445  1.00 28.09 ? 763  ARG   A CB   1 
ATOM   1871 C  CG   . ARG   A 1 269 ? 2.515   0.835   28.914  1.00 27.83 ? 763  ARG   A CG   1 
ATOM   1872 C  CD   . ARG   A 1 269 ? 3.745   1.711   29.090  1.00 21.37 ? 763  ARG   A CD   1 
ATOM   1873 N  NE   . ARG   A 1 269 ? 4.933   1.112   28.492  1.00 28.56 ? 763  ARG   A NE   1 
ATOM   1874 C  CZ   . ARG   A 1 269 ? 5.730   0.254   29.113  1.00 24.14 ? 763  ARG   A CZ   1 
ATOM   1875 N  NH1  . ARG   A 1 269 ? 5.495   -0.131  30.356  1.00 19.30 ? 763  ARG   A NH1  1 
ATOM   1876 N  NH2  . ARG   A 1 269 ? 6.788   -0.231  28.470  1.00 21.87 ? 763  ARG   A NH2  1 
ATOM   1877 N  N    . LYS   A 1 270 ? -0.328  1.128   25.568  1.00 28.00 ? 764  LYS   A N    1 
ATOM   1878 C  CA   . LYS   A 1 270 ? -1.014  1.339   24.298  1.00 29.11 ? 764  LYS   A CA   1 
ATOM   1879 C  C    . LYS   A 1 270 ? -0.057  1.592   23.138  1.00 31.91 ? 764  LYS   A C    1 
ATOM   1880 O  O    . LYS   A 1 270 ? -0.459  1.439   21.979  1.00 37.91 ? 764  LYS   A O    1 
ATOM   1881 C  CB   . LYS   A 1 270 ? -2.003  2.497   24.431  1.00 33.71 ? 764  LYS   A CB   1 
ATOM   1882 C  CG   . LYS   A 1 270 ? -3.139  2.206   25.401  1.00 36.69 ? 764  LYS   A CG   1 
ATOM   1883 C  CD   . LYS   A 1 270 ? -4.279  3.199   25.257  1.00 37.09 ? 764  LYS   A CD   1 
ATOM   1884 C  CE   . LYS   A 1 270 ? -4.094  4.389   26.183  1.00 36.79 ? 764  LYS   A CE   1 
ATOM   1885 N  NZ   . LYS   A 1 270 ? -5.287  5.280   26.182  1.00 45.24 ? 764  LYS   A NZ   1 
ATOM   1886 N  N    . ASP   A 1 271 ? 1.192   1.963   23.413  1.00 26.99 ? 765  ASP   A N    1 
ATOM   1887 C  CA   . ASP   A 1 271 ? 2.181   2.194   22.370  1.00 31.29 ? 765  ASP   A CA   1 
ATOM   1888 C  C    . ASP   A 1 271 ? 3.126   1.012   22.184  1.00 32.86 ? 765  ASP   A C    1 
ATOM   1889 O  O    . ASP   A 1 271 ? 4.156   1.155   21.517  1.00 34.48 ? 765  ASP   A O    1 
ATOM   1890 C  CB   . ASP   A 1 271 ? 2.985   3.462   22.670  1.00 35.59 ? 765  ASP   A CB   1 
ATOM   1891 C  CG   . ASP   A 1 271 ? 3.982   3.273   23.800  1.00 40.68 ? 765  ASP   A CG   1 
ATOM   1892 O  OD1  . ASP   A 1 271 ? 3.701   2.485   24.727  1.00 37.94 ? 765  ASP   A OD1  1 
ATOM   1893 O  OD2  . ASP   A 1 271 ? 5.053   3.914   23.758  1.00 40.02 ? 765  ASP   A OD2  1 
ATOM   1894 N  N    . SER   A 1 272 ? 2.799   -0.144  22.752  1.00 29.58 ? 766  SER   A N    1 
ATOM   1895 C  CA   . SER   A 1 272 ? 3.679   -1.298  22.649  1.00 29.07 ? 766  SER   A CA   1 
ATOM   1896 C  C    . SER   A 1 272 ? 3.716   -1.811  21.211  1.00 29.10 ? 766  SER   A C    1 
ATOM   1897 O  O    . SER   A 1 272 ? 2.674   -1.905  20.556  1.00 36.92 ? 766  SER   A O    1 
ATOM   1898 C  CB   . SER   A 1 272 ? 3.216   -2.412  23.586  1.00 33.67 ? 766  SER   A CB   1 
ATOM   1899 O  OG   . SER   A 1 272 ? 3.945   -3.605  23.356  1.00 34.86 ? 766  SER   A OG   1 
ATOM   1900 N  N    . PRO   A 1 273 ? 4.899   -2.151  20.692  1.00 36.15 ? 767  PRO   A N    1 
ATOM   1901 C  CA   . PRO   A 1 273 ? 4.979   -2.714  19.338  1.00 31.75 ? 767  PRO   A CA   1 
ATOM   1902 C  C    . PRO   A 1 273 ? 4.596   -4.182  19.255  1.00 30.23 ? 767  PRO   A C    1 
ATOM   1903 O  O    . PRO   A 1 273 ? 4.454   -4.703  18.140  1.00 34.04 ? 767  PRO   A O    1 
ATOM   1904 C  CB   . PRO   A 1 273 ? 6.454   -2.513  18.970  1.00 32.08 ? 767  PRO   A CB   1 
ATOM   1905 C  CG   . PRO   A 1 273 ? 7.164   -2.576  20.283  1.00 34.69 ? 767  PRO   A CG   1 
ATOM   1906 C  CD   . PRO   A 1 273 ? 6.230   -1.968  21.299  1.00 34.04 ? 767  PRO   A CD   1 
ATOM   1907 N  N    . TRP   A 1 274 ? 4.422   -4.861  20.388  1.00 34.16 ? 768  TRP   A N    1 
ATOM   1908 C  CA   . TRP   A 1 274 ? 4.099   -6.281  20.406  1.00 34.14 ? 768  TRP   A CA   1 
ATOM   1909 C  C    . TRP   A 1 274 ? 2.604   -6.562  20.476  1.00 33.84 ? 768  TRP   A C    1 
ATOM   1910 O  O    . TRP   A 1 274 ? 2.210   -7.730  20.390  1.00 32.79 ? 768  TRP   A O    1 
ATOM   1911 C  CB   . TRP   A 1 274 ? 4.776   -6.969  21.599  1.00 37.47 ? 768  TRP   A CB   1 
ATOM   1912 C  CG   . TRP   A 1 274 ? 6.221   -6.620  21.798  1.00 44.05 ? 768  TRP   A CG   1 
ATOM   1913 C  CD1  . TRP   A 1 274 ? 6.720   -5.505  22.408  1.00 41.66 ? 768  TRP   A CD1  1 
ATOM   1914 C  CD2  . TRP   A 1 274 ? 7.355   -7.401  21.400  1.00 43.47 ? 768  TRP   A CD2  1 
ATOM   1915 N  NE1  . TRP   A 1 274 ? 8.094   -5.541  22.407  1.00 42.86 ? 768  TRP   A NE1  1 
ATOM   1916 C  CE2  . TRP   A 1 274 ? 8.508   -6.694  21.795  1.00 45.36 ? 768  TRP   A CE2  1 
ATOM   1917 C  CE3  . TRP   A 1 274 ? 7.506   -8.626  20.746  1.00 40.38 ? 768  TRP   A CE3  1 
ATOM   1918 C  CZ2  . TRP   A 1 274 ? 9.794   -7.173  21.556  1.00 46.65 ? 768  TRP   A CZ2  1 
ATOM   1919 C  CZ3  . TRP   A 1 274 ? 8.783   -9.100  20.510  1.00 42.57 ? 768  TRP   A CZ3  1 
ATOM   1920 C  CH2  . TRP   A 1 274 ? 9.910   -8.373  20.910  1.00 47.29 ? 768  TRP   A CH2  1 
ATOM   1921 N  N    . LYS   A 1 275 ? 1.766   -5.530  20.616  1.00 27.96 ? 769  LYS   A N    1 
ATOM   1922 C  CA   . LYS   A 1 275 ? 0.378   -5.753  21.015  1.00 28.04 ? 769  LYS   A CA   1 
ATOM   1923 C  C    . LYS   A 1 275 ? -0.406  -6.526  19.959  1.00 28.74 ? 769  LYS   A C    1 
ATOM   1924 O  O    . LYS   A 1 275 ? -1.244  -7.369  20.299  1.00 27.53 ? 769  LYS   A O    1 
ATOM   1925 C  CB   . LYS   A 1 275 ? -0.303  -4.419  21.326  1.00 29.79 ? 769  LYS   A CB   1 
ATOM   1926 C  CG   . LYS   A 1 275 ? -0.224  -3.382  20.219  1.00 31.35 ? 769  LYS   A CG   1 
ATOM   1927 C  CD   . LYS   A 1 275 ? -0.876  -2.081  20.657  1.00 33.74 ? 769  LYS   A CD   1 
ATOM   1928 C  CE   . LYS   A 1 275 ? -0.795  -1.021  19.572  1.00 34.07 ? 769  LYS   A CE   1 
ATOM   1929 N  NZ   . LYS   A 1 275 ? -1.607  0.179   19.915  1.00 40.16 ? 769  LYS   A NZ   1 
ATOM   1930 N  N    . GLN   A 1 276 ? -0.153  -6.263  18.675  1.00 28.56 ? 770  GLN   A N    1 
ATOM   1931 C  CA   . GLN   A 1 276 ? -0.926  -6.942  17.639  1.00 28.67 ? 770  GLN   A CA   1 
ATOM   1932 C  C    . GLN   A 1 276 ? -0.543  -8.413  17.531  1.00 29.01 ? 770  GLN   A C    1 
ATOM   1933 O  O    . GLN   A 1 276 ? -1.418  -9.279  17.416  1.00 26.28 ? 770  GLN   A O    1 
ATOM   1934 C  CB   . GLN   A 1 276 ? -0.748  -6.242  16.291  1.00 30.53 ? 770  GLN   A CB   1 
ATOM   1935 C  CG   . GLN   A 1 276 ? -1.211  -7.065  15.084  1.00 39.80 ? 770  GLN   A CG   1 
ATOM   1936 C  CD   . GLN   A 1 276 ? -2.728  -7.180  14.963  1.00 45.60 ? 770  GLN   A CD   1 
ATOM   1937 O  OE1  . GLN   A 1 276 ? -3.457  -7.161  15.956  1.00 41.21 ? 770  GLN   A OE1  1 
ATOM   1938 N  NE2  . GLN   A 1 276 ? -3.207  -7.310  13.731  1.00 36.06 ? 770  GLN   A NE2  1 
ATOM   1939 N  N    . ASN   A 1 277 ? 0.756   -8.718  17.568  1.00 27.27 ? 771  ASN   A N    1 
ATOM   1940 C  CA   . ASN   A 1 277 ? 1.181   -10.109 17.455  1.00 30.39 ? 771  ASN   A CA   1 
ATOM   1941 C  C    . ASN   A 1 277 ? 0.847   -10.905 18.710  1.00 30.43 ? 771  ASN   A C    1 
ATOM   1942 O  O    . ASN   A 1 277 ? 0.609   -12.116 18.627  1.00 28.31 ? 771  ASN   A O    1 
ATOM   1943 C  CB   . ASN   A 1 277 ? 2.678   -10.182 17.156  1.00 24.41 ? 771  ASN   A CB   1 
ATOM   1944 C  CG   . ASN   A 1 277 ? 3.000   -9.840  15.716  1.00 33.36 ? 771  ASN   A CG   1 
ATOM   1945 O  OD1  . ASN   A 1 277 ? 2.137   -9.914  14.841  1.00 38.01 ? 771  ASN   A OD1  1 
ATOM   1946 N  ND2  . ASN   A 1 277 ? 4.248   -9.468  15.463  1.00 40.15 ? 771  ASN   A ND2  1 
ATOM   1947 N  N    . VAL   A 1 278 ? 0.829   -10.253 19.876  1.00 26.37 ? 772  VAL   A N    1 
ATOM   1948 C  CA   . VAL   A 1 278 ? 0.380   -10.925 21.093  1.00 26.88 ? 772  VAL   A CA   1 
ATOM   1949 C  C    . VAL   A 1 278 ? -1.070  -11.367 20.943  1.00 22.97 ? 772  VAL   A C    1 
ATOM   1950 O  O    . VAL   A 1 278 ? -1.420  -12.520 21.219  1.00 23.49 ? 772  VAL   A O    1 
ATOM   1951 C  CB   . VAL   A 1 278 ? 0.562   -10.008 22.316  1.00 26.58 ? 772  VAL   A CB   1 
ATOM   1952 C  CG1  . VAL   A 1 278 ? -0.252  -10.528 23.491  1.00 21.37 ? 772  VAL   A CG1  1 
ATOM   1953 C  CG2  . VAL   A 1 278 ? 2.028   -9.907  22.698  1.00 23.99 ? 772  VAL   A CG2  1 
ATOM   1954 N  N    . SER   A 1 279 ? -1.933  -10.454 20.490  1.00 23.01 ? 773  SER   A N    1 
ATOM   1955 C  CA   . SER   A 1 279 ? -3.347  -10.776 20.336  1.00 22.80 ? 773  SER   A CA   1 
ATOM   1956 C  C    . SER   A 1 279 ? -3.559  -11.872 19.298  1.00 24.70 ? 773  SER   A C    1 
ATOM   1957 O  O    . SER   A 1 279 ? -4.395  -12.764 19.487  1.00 21.52 ? 773  SER   A O    1 
ATOM   1958 C  CB   . SER   A 1 279 ? -4.129  -9.518  19.958  1.00 16.84 ? 773  SER   A CB   1 
ATOM   1959 O  OG   . SER   A 1 279 ? -5.511  -9.795  19.828  1.00 25.82 ? 773  SER   A OG   1 
ATOM   1960 N  N    . LEU   A 1 280 ? -2.812  -11.822 18.192  1.00 22.29 ? 774  LEU   A N    1 
ATOM   1961 C  CA   . LEU   A 1 280 ? -2.935  -12.857 17.171  1.00 24.73 ? 774  LEU   A CA   1 
ATOM   1962 C  C    . LEU   A 1 280 ? -2.497  -14.214 17.707  1.00 26.48 ? 774  LEU   A C    1 
ATOM   1963 O  O    . LEU   A 1 280 ? -3.098  -15.244 17.376  1.00 21.77 ? 774  LEU   A O    1 
ATOM   1964 C  CB   . LEU   A 1 280 ? -2.116  -12.481 15.936  1.00 24.27 ? 774  LEU   A CB   1 
ATOM   1965 C  CG   . LEU   A 1 280 ? -2.625  -11.313 15.089  1.00 27.78 ? 774  LEU   A CG   1 
ATOM   1966 C  CD1  . LEU   A 1 280 ? -1.617  -10.953 14.008  1.00 23.20 ? 774  LEU   A CD1  1 
ATOM   1967 C  CD2  . LEU   A 1 280 ? -3.971  -11.655 14.477  1.00 22.53 ? 774  LEU   A CD2  1 
ATOM   1968 N  N    . SER   A 1 281 ? -1.449  -14.237 18.534  1.00 22.21 ? 775  SER   A N    1 
ATOM   1969 C  CA   . SER   A 1 281 ? -0.993  -15.495 19.114  1.00 24.25 ? 775  SER   A CA   1 
ATOM   1970 C  C    . SER   A 1 281 ? -2.022  -16.076 20.075  1.00 20.42 ? 775  SER   A C    1 
ATOM   1971 O  O    . SER   A 1 281 ? -2.142  -17.302 20.185  1.00 19.55 ? 775  SER   A O    1 
ATOM   1972 C  CB   . SER   A 1 281 ? 0.346   -15.294 19.824  1.00 20.86 ? 775  SER   A CB   1 
ATOM   1973 O  OG   . SER   A 1 281 ? 1.341   -14.851 18.917  1.00 35.38 ? 775  SER   A OG   1 
ATOM   1974 N  N    . ILE   A 1 282 ? -2.768  -15.218 20.775  1.00 22.21 ? 776  ILE   A N    1 
ATOM   1975 C  CA   . ILE   A 1 282 ? -3.839  -15.699 21.644  1.00 17.38 ? 776  ILE   A CA   1 
ATOM   1976 C  C    . ILE   A 1 282 ? -4.903  -16.414 20.822  1.00 17.99 ? 776  ILE   A C    1 
ATOM   1977 O  O    . ILE   A 1 282 ? -5.358  -17.508 21.176  1.00 20.16 ? 776  ILE   A O    1 
ATOM   1978 C  CB   . ILE   A 1 282 ? -4.441  -14.535 22.452  1.00 20.29 ? 776  ILE   A CB   1 
ATOM   1979 C  CG1  . ILE   A 1 282 ? -3.370  -13.867 23.318  1.00 17.56 ? 776  ILE   A CG1  1 
ATOM   1980 C  CG2  . ILE   A 1 282 ? -5.603  -15.022 23.303  1.00 15.92 ? 776  ILE   A CG2  1 
ATOM   1981 C  CD1  . ILE   A 1 282 ? -2.696  -14.805 24.288  1.00 14.31 ? 776  ILE   A CD1  1 
ATOM   1982 N  N    . LEU   A 1 283 ? -5.314  -15.802 19.709  1.00 17.69 ? 777  LEU   A N    1 
ATOM   1983 C  CA   . LEU   A 1 283 ? -6.316  -16.417 18.844  1.00 22.55 ? 777  LEU   A CA   1 
ATOM   1984 C  C    . LEU   A 1 283 ? -5.807  -17.732 18.269  1.00 20.35 ? 777  LEU   A C    1 
ATOM   1985 O  O    . LEU   A 1 283 ? -6.530  -18.734 18.242  1.00 19.07 ? 777  LEU   A O    1 
ATOM   1986 C  CB   . LEU   A 1 283 ? -6.700  -15.454 17.721  1.00 18.81 ? 777  LEU   A CB   1 
ATOM   1987 C  CG   . LEU   A 1 283 ? -7.220  -14.081 18.149  1.00 20.14 ? 777  LEU   A CG   1 
ATOM   1988 C  CD1  . LEU   A 1 283 ? -7.542  -13.230 16.930  1.00 19.62 ? 777  LEU   A CD1  1 
ATOM   1989 C  CD2  . LEU   A 1 283 ? -8.439  -14.229 19.045  1.00 17.99 ? 777  LEU   A CD2  1 
ATOM   1990 N  N    . LYS   A 1 284 ? -4.556  -17.742 17.801  1.00 22.83 ? 778  LYS   A N    1 
ATOM   1991 C  CA   . LYS   A 1 284 ? -3.979  -18.962 17.246  1.00 21.73 ? 778  LYS   A CA   1 
ATOM   1992 C  C    . LYS   A 1 284 ? -3.964  -20.083 18.276  1.00 21.07 ? 778  LYS   A C    1 
ATOM   1993 O  O    . LYS   A 1 284 ? -4.289  -21.232 17.956  1.00 20.64 ? 778  LYS   A O    1 
ATOM   1994 C  CB   . LYS   A 1 284 ? -2.566  -18.684 16.732  1.00 20.88 ? 778  LYS   A CB   1 
ATOM   1995 C  CG   . LYS   A 1 284 ? -1.888  -19.878 16.076  1.00 25.78 ? 778  LYS   A CG   1 
ATOM   1996 C  CD   . LYS   A 1 284 ? -0.494  -19.517 15.585  1.00 27.66 ? 778  LYS   A CD   1 
ATOM   1997 C  CE   . LYS   A 1 284 ? 0.180   -20.697 14.902  1.00 29.52 ? 778  LYS   A CE   1 
ATOM   1998 N  NZ   . LYS   A 1 284 ? -0.534  -21.105 13.660  1.00 39.11 ? 778  LYS   A NZ   1 
ATOM   1999 N  N    . SER   A 1 285 ? -3.607  -19.766 19.523  1.00 18.74 ? 779  SER   A N    1 
ATOM   2000 C  CA   . SER   A 1 285 ? -3.558  -20.791 20.561  1.00 18.56 ? 779  SER   A CA   1 
ATOM   2001 C  C    . SER   A 1 285 ? -4.950  -21.312 20.894  1.00 20.99 ? 779  SER   A C    1 
ATOM   2002 O  O    . SER   A 1 285 ? -5.119  -22.501 21.187  1.00 21.65 ? 779  SER   A O    1 
ATOM   2003 C  CB   . SER   A 1 285 ? -2.873  -20.239 21.810  1.00 18.45 ? 779  SER   A CB   1 
ATOM   2004 O  OG   . SER   A 1 285 ? -1.559  -19.801 21.513  1.00 18.06 ? 779  SER   A OG   1 
ATOM   2005 N  N    . HIS   A 1 286 ? -5.958  -20.435 20.863  1.00 19.86 ? 780  HIS   A N    1 
ATOM   2006 C  CA   . HIS   A 1 286 ? -7.335  -20.890 21.019  1.00 18.10 ? 780  HIS   A CA   1 
ATOM   2007 C  C    . HIS   A 1 286 ? -7.734  -21.827 19.886  1.00 21.42 ? 780  HIS   A C    1 
ATOM   2008 O  O    . HIS   A 1 286 ? -8.351  -22.872 20.120  1.00 21.44 ? 780  HIS   A O    1 
ATOM   2009 C  CB   . HIS   A 1 286 ? -8.288  -19.693 21.065  1.00 19.24 ? 780  HIS   A CB   1 
ATOM   2010 C  CG   . HIS   A 1 286 ? -8.442  -19.083 22.423  1.00 19.43 ? 780  HIS   A CG   1 
ATOM   2011 N  ND1  . HIS   A 1 286 ? -8.854  -19.805 23.522  1.00 17.82 ? 780  HIS   A ND1  1 
ATOM   2012 C  CD2  . HIS   A 1 286 ? -8.264  -17.811 22.854  1.00 16.11 ? 780  HIS   A CD2  1 
ATOM   2013 C  CE1  . HIS   A 1 286 ? -8.909  -19.008 24.574  1.00 19.50 ? 780  HIS   A CE1  1 
ATOM   2014 N  NE2  . HIS   A 1 286 ? -8.557  -17.793 24.196  1.00 17.68 ? 780  HIS   A NE2  1 
ATOM   2015 N  N    . GLU   A 1 287 ? -7.372  -21.476 18.651  1.00 19.92 ? 781  GLU   A N    1 
ATOM   2016 C  CA   . GLU   A 1 287 ? -7.888  -22.171 17.480  1.00 21.19 ? 781  GLU   A CA   1 
ATOM   2017 C  C    . GLU   A 1 287 ? -7.154  -23.472 17.174  1.00 22.08 ? 781  GLU   A C    1 
ATOM   2018 O  O    . GLU   A 1 287 ? -7.685  -24.293 16.418  1.00 23.20 ? 781  GLU   A O    1 
ATOM   2019 C  CB   . GLU   A 1 287 ? -7.832  -21.244 16.263  1.00 21.78 ? 781  GLU   A CB   1 
ATOM   2020 C  CG   . GLU   A 1 287 ? -8.758  -20.042 16.374  1.00 21.37 ? 781  GLU   A CG   1 
ATOM   2021 C  CD   . GLU   A 1 287 ? -8.418  -18.942 15.388  1.00 21.94 ? 781  GLU   A CD   1 
ATOM   2022 O  OE1  . GLU   A 1 287 ? -8.064  -19.257 14.233  1.00 23.10 ? 781  GLU   A OE1  1 
ATOM   2023 O  OE2  . GLU   A 1 287 ? -8.496  -17.757 15.775  1.00 23.82 ? 781  GLU   A OE2  1 
ATOM   2024 N  N    . ASN   A 1 288 ? -5.959  -23.685 17.725  1.00 23.53 ? 782  ASN   A N    1 
ATOM   2025 C  CA   . ASN   A 1 288 ? -5.228  -24.928 17.505  1.00 24.53 ? 782  ASN   A CA   1 
ATOM   2026 C  C    . ASN   A 1 288 ? -5.213  -25.831 18.734  1.00 24.76 ? 782  ASN   A C    1 
ATOM   2027 O  O    . ASN   A 1 288 ? -4.499  -26.839 18.742  1.00 26.15 ? 782  ASN   A O    1 
ATOM   2028 C  CB   . ASN   A 1 288 ? -3.796  -24.644 17.032  1.00 24.04 ? 782  ASN   A CB   1 
ATOM   2029 C  CG   . ASN   A 1 288 ? -2.977  -23.847 18.038  1.00 23.01 ? 782  ASN   A CG   1 
ATOM   2030 O  OD1  . ASN   A 1 288 ? -3.262  -23.835 19.235  1.00 22.69 ? 782  ASN   A OD1  1 
ATOM   2031 N  ND2  . ASN   A 1 288 ? -1.944  -23.174 17.545  1.00 22.13 ? 782  ASN   A ND2  1 
ATOM   2032 N  N    . GLY   A 1 289 ? -5.977  -25.492 19.770  1.00 24.18 ? 783  GLY   A N    1 
ATOM   2033 C  CA   . GLY   A 1 289 ? -6.108  -26.342 20.933  1.00 24.70 ? 783  GLY   A CA   1 
ATOM   2034 C  C    . GLY   A 1 289 ? -5.083  -26.129 22.025  1.00 23.35 ? 783  GLY   A C    1 
ATOM   2035 O  O    . GLY   A 1 289 ? -5.125  -26.845 23.033  1.00 23.88 ? 783  GLY   A O    1 
ATOM   2036 N  N    . PHE   A 1 290 ? -4.166  -25.171 21.866  1.00 21.90 ? 784  PHE   A N    1 
ATOM   2037 C  CA   . PHE   A 1 290 ? -3.149  -24.961 22.892  1.00 22.21 ? 784  PHE   A CA   1 
ATOM   2038 C  C    . PHE   A 1 290 ? -3.764  -24.438 24.184  1.00 23.07 ? 784  PHE   A C    1 
ATOM   2039 O  O    . PHE   A 1 290 ? -3.410  -24.899 25.276  1.00 24.69 ? 784  PHE   A O    1 
ATOM   2040 C  CB   . PHE   A 1 290 ? -2.072  -24.002 22.387  1.00 21.68 ? 784  PHE   A CB   1 
ATOM   2041 C  CG   . PHE   A 1 290 ? -0.985  -23.735 23.391  1.00 25.74 ? 784  PHE   A CG   1 
ATOM   2042 C  CD1  . PHE   A 1 290 ? -0.082  -24.728 23.735  1.00 26.73 ? 784  PHE   A CD1  1 
ATOM   2043 C  CD2  . PHE   A 1 290 ? -0.872  -22.495 23.995  1.00 23.05 ? 784  PHE   A CD2  1 
ATOM   2044 C  CE1  . PHE   A 1 290 ? 0.917   -24.486 24.662  1.00 28.39 ? 784  PHE   A CE1  1 
ATOM   2045 C  CE2  . PHE   A 1 290 ? 0.125   -22.246 24.922  1.00 29.91 ? 784  PHE   A CE2  1 
ATOM   2046 C  CZ   . PHE   A 1 290 ? 1.020   -23.244 25.255  1.00 28.28 ? 784  PHE   A CZ   1 
ATOM   2047 N  N    . MET   A 1 291 ? -4.680  -23.470 24.082  1.00 19.47 ? 785  MET   A N    1 
ATOM   2048 C  CA   . MET   A 1 291 ? -5.360  -22.976 25.274  1.00 22.42 ? 785  MET   A CA   1 
ATOM   2049 C  C    . MET   A 1 291 ? -6.151  -24.083 25.952  1.00 20.34 ? 785  MET   A C    1 
ATOM   2050 O  O    . MET   A 1 291 ? -6.261  -24.106 27.184  1.00 20.84 ? 785  MET   A O    1 
ATOM   2051 C  CB   . MET   A 1 291 ? -6.289  -21.815 24.914  1.00 19.41 ? 785  MET   A CB   1 
ATOM   2052 C  CG   . MET   A 1 291 ? -5.587  -20.592 24.347  1.00 27.01 ? 785  MET   A CG   1 
ATOM   2053 S  SD   . MET   A 1 291 ? -4.229  -19.989 25.372  1.00 19.86 ? 785  MET   A SD   1 
ATOM   2054 C  CE   . MET   A 1 291 ? -5.012  -19.867 26.970  1.00 16.16 ? 785  MET   A CE   1 
ATOM   2055 N  N    . GLU   A 1 292 ? -6.701  -25.011 25.166  1.00 23.65 ? 786  GLU   A N    1 
ATOM   2056 C  CA   . GLU   A 1 292 ? -7.445  -26.123 25.747  1.00 27.53 ? 786  GLU   A CA   1 
ATOM   2057 C  C    . GLU   A 1 292 ? -6.514  -27.092 26.465  1.00 28.78 ? 786  GLU   A C    1 
ATOM   2058 O  O    . GLU   A 1 292 ? -6.862  -27.619 27.528  1.00 30.59 ? 786  GLU   A O    1 
ATOM   2059 C  CB   . GLU   A 1 292 ? -8.239  -26.851 24.664  1.00 26.61 ? 786  GLU   A CB   1 
ATOM   2060 C  CG   . GLU   A 1 292 ? -9.268  -27.822 25.214  1.00 30.77 ? 786  GLU   A CG   1 
ATOM   2061 C  CD   . GLU   A 1 292 ? -10.397 -28.099 24.244  1.00 45.60 ? 786  GLU   A CD   1 
ATOM   2062 O  OE1  . GLU   A 1 292 ? -10.244 -29.010 23.403  1.00 54.46 ? 786  GLU   A OE1  1 
ATOM   2063 O  OE2  . GLU   A 1 292 ? -11.436 -27.413 24.320  1.00 51.47 ? 786  GLU   A OE2  1 
ATOM   2064 N  N    . ASP   A 1 293 ? -5.328  -27.341 25.900  1.00 23.78 ? 787  ASP   A N    1 
ATOM   2065 C  CA   . ASP   A 1 293 ? -4.343  -28.182 26.575  1.00 24.40 ? 787  ASP   A CA   1 
ATOM   2066 C  C    . ASP   A 1 293 ? -3.942  -27.582 27.916  1.00 30.15 ? 787  ASP   A C    1 
ATOM   2067 O  O    . ASP   A 1 293 ? -3.849  -28.291 28.925  1.00 26.40 ? 787  ASP   A O    1 
ATOM   2068 C  CB   . ASP   A 1 293 ? -3.112  -28.371 25.688  1.00 24.30 ? 787  ASP   A CB   1 
ATOM   2069 C  CG   . ASP   A 1 293 ? -3.433  -29.058 24.377  1.00 33.81 ? 787  ASP   A CG   1 
ATOM   2070 O  OD1  . ASP   A 1 293 ? -4.373  -29.879 24.351  1.00 40.08 ? 787  ASP   A OD1  1 
ATOM   2071 O  OD2  . ASP   A 1 293 ? -2.746  -28.776 23.373  1.00 33.89 ? 787  ASP   A OD2  1 
ATOM   2072 N  N    . LEU   A 1 294 ? -3.691  -26.271 27.941  1.00 25.46 ? 788  LEU   A N    1 
ATOM   2073 C  CA   . LEU   A 1 294 ? -3.380  -25.599 29.198  1.00 27.50 ? 788  LEU   A CA   1 
ATOM   2074 C  C    . LEU   A 1 294 ? -4.515  -25.759 30.199  1.00 27.30 ? 788  LEU   A C    1 
ATOM   2075 O  O    . LEU   A 1 294 ? -4.275  -25.929 31.400  1.00 30.91 ? 788  LEU   A O    1 
ATOM   2076 C  CB   . LEU   A 1 294 ? -3.098  -24.119 28.944  1.00 23.14 ? 788  LEU   A CB   1 
ATOM   2077 C  CG   . LEU   A 1 294 ? -1.801  -23.787 28.207  1.00 23.43 ? 788  LEU   A CG   1 
ATOM   2078 C  CD1  . LEU   A 1 294 ? -1.604  -22.282 28.115  1.00 24.73 ? 788  LEU   A CD1  1 
ATOM   2079 C  CD2  . LEU   A 1 294 ? -0.616  -24.446 28.893  1.00 21.09 ? 788  LEU   A CD2  1 
ATOM   2080 N  N    . ASP   A 1 295 ? -5.760  -25.708 29.722  1.00 26.14 ? 789  ASP   A N    1 
ATOM   2081 C  CA   . ASP   A 1 295 ? -6.900  -25.918 30.607  1.00 31.62 ? 789  ASP   A CA   1 
ATOM   2082 C  C    . ASP   A 1 295 ? -6.919  -27.343 31.141  1.00 36.44 ? 789  ASP   A C    1 
ATOM   2083 O  O    . ASP   A 1 295 ? -7.313  -27.580 32.288  1.00 40.46 ? 789  ASP   A O    1 
ATOM   2084 C  CB   . ASP   A 1 295 ? -8.198  -25.599 29.868  1.00 43.06 ? 789  ASP   A CB   1 
ATOM   2085 C  CG   . ASP   A 1 295 ? -9.229  -24.935 30.759  1.00 53.15 ? 789  ASP   A CG   1 
ATOM   2086 O  OD1  . ASP   A 1 295 ? -8.978  -23.801 31.221  1.00 35.60 ? 789  ASP   A OD1  1 
ATOM   2087 O  OD2  . ASP   A 1 295 ? -10.294 -25.534 30.992  1.00 53.63 ? 789  ASP   A OD2  1 
ATOM   2088 N  N    . LYS   A 1 296 ? -6.490  -28.309 30.326  1.00 31.98 ? 790  LYS   A N    1 
ATOM   2089 C  CA   . LYS   A 1 296 ? -6.383  -29.681 30.813  1.00 32.86 ? 790  LYS   A CA   1 
ATOM   2090 C  C    . LYS   A 1 296 ? -5.191  -29.860 31.742  1.00 32.75 ? 790  LYS   A C    1 
ATOM   2091 O  O    . LYS   A 1 296 ? -5.259  -30.652 32.689  1.00 40.26 ? 790  LYS   A O    1 
ATOM   2092 C  CB   . LYS   A 1 296 ? -6.266  -30.667 29.649  1.00 33.97 ? 790  LYS   A CB   1 
ATOM   2093 C  CG   . LYS   A 1 296 ? -7.573  -31.034 28.961  1.00 38.81 ? 790  LYS   A CG   1 
ATOM   2094 C  CD   . LYS   A 1 296 ? -7.485  -30.865 27.451  1.00 40.80 ? 790  LYS   A CD   1 
ATOM   2095 C  CE   . LYS   A 1 296 ? -8.863  -30.792 26.819  1.00 51.44 ? 790  LYS   A CE   1 
ATOM   2096 N  NZ   . LYS   A 1 296 ? -9.786  -31.838 27.326  1.00 42.88 ? 790  LYS   A NZ   1 
ATOM   2097 N  N    . THR   A 1 297 ? -4.091  -29.153 31.481  1.00 30.49 ? 791  THR   A N    1 
ATOM   2098 C  CA   . THR   A 1 297 ? -2.888  -29.340 32.283  1.00 30.03 ? 791  THR   A CA   1 
ATOM   2099 C  C    . THR   A 1 297 ? -3.032  -28.707 33.661  1.00 27.42 ? 791  THR   A C    1 
ATOM   2100 O  O    . THR   A 1 297 ? -2.590  -29.281 34.663  1.00 28.31 ? 791  THR   A O    1 
ATOM   2101 C  CB   . THR   A 1 297 ? -1.675  -28.757 31.554  1.00 31.08 ? 791  THR   A CB   1 
ATOM   2102 O  OG1  . THR   A 1 297 ? -1.488  -29.441 30.308  1.00 34.41 ? 791  THR   A OG1  1 
ATOM   2103 C  CG2  . THR   A 1 297 ? -0.414  -28.901 32.399  1.00 33.32 ? 791  THR   A CG2  1 
ATOM   2104 N  N    . TRP   A 1 298 ? -3.657  -27.532 33.737  1.00 29.64 ? 792  TRP   A N    1 
ATOM   2105 C  CA   . TRP   A 1 298 ? -3.625  -26.726 34.950  1.00 26.59 ? 792  TRP   A CA   1 
ATOM   2106 C  C    . TRP   A 1 298 ? -4.969  -26.568 35.643  1.00 30.07 ? 792  TRP   A C    1 
ATOM   2107 O  O    . TRP   A 1 298 ? -4.995  -26.393 36.863  1.00 27.92 ? 792  TRP   A O    1 
ATOM   2108 C  CB   . TRP   A 1 298 ? -3.071  -25.329 34.639  1.00 26.74 ? 792  TRP   A CB   1 
ATOM   2109 C  CG   . TRP   A 1 298 ? -1.654  -25.348 34.157  1.00 23.62 ? 792  TRP   A CG   1 
ATOM   2110 C  CD1  . TRP   A 1 298 ? -1.220  -25.188 32.873  1.00 25.75 ? 792  TRP   A CD1  1 
ATOM   2111 C  CD2  . TRP   A 1 298 ? -0.482  -25.543 34.955  1.00 19.27 ? 792  TRP   A CD2  1 
ATOM   2112 N  NE1  . TRP   A 1 298 ? 0.151   -25.271 32.823  1.00 23.39 ? 792  TRP   A NE1  1 
ATOM   2113 C  CE2  . TRP   A 1 298 ? 0.628   -25.489 34.089  1.00 22.79 ? 792  TRP   A CE2  1 
ATOM   2114 C  CE3  . TRP   A 1 298 ? -0.263  -25.758 36.319  1.00 20.17 ? 792  TRP   A CE3  1 
ATOM   2115 C  CZ2  . TRP   A 1 298 ? 1.936   -25.641 34.542  1.00 19.57 ? 792  TRP   A CZ2  1 
ATOM   2116 C  CZ3  . TRP   A 1 298 ? 1.036   -25.909 36.767  1.00 21.20 ? 792  TRP   A CZ3  1 
ATOM   2117 C  CH2  . TRP   A 1 298 ? 2.119   -25.851 35.881  1.00 24.76 ? 792  TRP   A CH2  1 
ATOM   2118 N  N    . VAL   A 1 299 ? -6.082  -26.625 34.914  1.00 31.09 ? 793  VAL   A N    1 
ATOM   2119 C  CA   . VAL   A 1 299 ? -7.390  -26.243 35.443  1.00 38.63 ? 793  VAL   A CA   1 
ATOM   2120 C  C    . VAL   A 1 299 ? -8.263  -27.464 35.732  1.00 44.14 ? 793  VAL   A C    1 
ATOM   2121 O  O    . VAL   A 1 299 ? -8.726  -27.652 36.859  1.00 47.91 ? 793  VAL   A O    1 
ATOM   2122 C  CB   . VAL   A 1 299 ? -8.104  -25.254 34.494  1.00 41.57 ? 793  VAL   A CB   1 
ATOM   2123 C  CG1  . VAL   A 1 299 ? -9.488  -24.917 35.027  1.00 37.18 ? 793  VAL   A CG1  1 
ATOM   2124 C  CG2  . VAL   A 1 299 ? -7.266  -23.997 34.325  1.00 30.79 ? 793  VAL   A CG2  1 
ATOM   2125 N  N    . ARG   A 1 300 ? -8.507  -28.299 34.725  1.00 61.09 ? 794  ARG   A N    1 
ATOM   2126 C  CA   . ARG   A 1 300 ? -9.469  -29.396 34.825  1.00 65.16 ? 794  ARG   A CA   1 
ATOM   2127 C  C    . ARG   A 1 300 ? -8.733  -30.732 34.899  1.00 65.39 ? 794  ARG   A C    1 
ATOM   2128 O  O    . ARG   A 1 300 ? -8.331  -31.286 33.873  1.00 74.64 ? 794  ARG   A O    1 
ATOM   2129 C  CB   . ARG   A 1 300 ? -10.434 -29.371 33.642  1.00 66.04 ? 794  ARG   A CB   1 
ATOM   2130 C  CG   . ARG   A 1 300 ? -11.309 -28.130 33.566  1.00 67.76 ? 794  ARG   A CG   1 
ATOM   2131 C  CD   . ARG   A 1 300 ? -11.873 -27.945 32.164  1.00 75.11 ? 794  ARG   A CD   1 
ATOM   2132 N  NE   . ARG   A 1 300 ? -11.015 -28.549 31.151  1.00 75.27 ? 794  ARG   A NE   1 
ATOM   2133 C  CZ   . ARG   A 1 300 ? -11.004 -28.203 29.871  1.00 71.77 ? 794  ARG   A CZ   1 
ATOM   2134 N  NH1  . ARG   A 1 300 ? -11.791 -27.246 29.407  1.00 74.23 ? 794  ARG   A NH1  1 
ATOM   2135 N  NH2  . ARG   A 1 300 ? -10.178 -28.827 29.037  1.00 67.52 ? 794  ARG   A NH2  1 
ATOM   2136 N  N    . TYR   A 1 301 ? -8.574  -31.253 36.113  1.00 59.51 ? 795  TYR   A N    1 
ATOM   2137 C  CA   . TYR   A 1 301 ? -8.063  -32.609 36.303  1.00 63.68 ? 795  TYR   A CA   1 
ATOM   2138 C  C    . TYR   A 1 301 ? -8.490  -33.183 37.653  1.00 59.45 ? 795  TYR   A C    1 
ATOM   2139 O  O    . TYR   A 1 301 ? -9.411  -32.675 38.293  1.00 66.14 ? 795  TYR   A O    1 
ATOM   2140 C  CB   . TYR   A 1 301 ? -6.535  -32.640 36.147  1.00 66.77 ? 795  TYR   A CB   1 
ATOM   2141 C  CG   . TYR   A 1 301 ? -5.735  -31.744 37.083  1.00 67.61 ? 795  TYR   A CG   1 
ATOM   2142 C  CD1  . TYR   A 1 301 ? -4.853  -30.801 36.572  1.00 56.60 ? 795  TYR   A CD1  1 
ATOM   2143 C  CD2  . TYR   A 1 301 ? -5.815  -31.877 38.465  1.00 66.87 ? 795  TYR   A CD2  1 
ATOM   2144 C  CE1  . TYR   A 1 301 ? -4.108  -29.989 37.408  1.00 54.31 ? 795  TYR   A CE1  1 
ATOM   2145 C  CE2  . TYR   A 1 301 ? -5.073  -31.070 39.308  1.00 65.36 ? 795  TYR   A CE2  1 
ATOM   2146 C  CZ   . TYR   A 1 301 ? -4.220  -30.129 38.774  1.00 57.94 ? 795  TYR   A CZ   1 
ATOM   2147 O  OH   . TYR   A 1 301 ? -3.476  -29.325 39.608  1.00 54.85 ? 795  TYR   A OH   1 
ATOM   2148 N  N    . ASP   B 2 17  ? -18.999 11.175  6.927   1.00 64.28 ? 403  ASP   B N    1 
ATOM   2149 C  CA   . ASP   B 2 17  ? -17.887 11.406  7.841   1.00 76.38 ? 403  ASP   B CA   1 
ATOM   2150 C  C    . ASP   B 2 17  ? -18.233 10.876  9.231   1.00 65.14 ? 403  ASP   B C    1 
ATOM   2151 O  O    . ASP   B 2 17  ? -17.551 9.998   9.762   1.00 59.17 ? 403  ASP   B O    1 
ATOM   2152 C  CB   . ASP   B 2 17  ? -17.541 12.894  7.901   1.00 77.40 ? 403  ASP   B CB   1 
ATOM   2153 C  CG   . ASP   B 2 17  ? -16.076 13.136  8.199   1.00 90.07 ? 403  ASP   B CG   1 
ATOM   2154 O  OD1  . ASP   B 2 17  ? -15.224 12.505  7.539   1.00 89.74 ? 403  ASP   B OD1  1 
ATOM   2155 O  OD2  . ASP   B 2 17  ? -15.774 13.957  9.090   1.00 87.15 ? 403  ASP   B OD2  1 
ATOM   2156 N  N    . ASN   B 2 18  ? -19.295 11.422  9.819   1.00 61.94 ? 404  ASN   B N    1 
ATOM   2157 C  CA   . ASN   B 2 18  ? -19.884 10.876  11.033  1.00 42.94 ? 404  ASN   B CA   1 
ATOM   2158 C  C    . ASN   B 2 18  ? -21.071 9.969   10.736  1.00 43.88 ? 404  ASN   B C    1 
ATOM   2159 O  O    . ASN   B 2 18  ? -21.669 9.422   11.668  1.00 38.39 ? 404  ASN   B O    1 
ATOM   2160 C  CB   . ASN   B 2 18  ? -20.311 12.010  11.972  1.00 53.17 ? 404  ASN   B CB   1 
ATOM   2161 C  CG   . ASN   B 2 18  ? -20.375 11.575  13.425  1.00 53.60 ? 404  ASN   B CG   1 
ATOM   2162 O  OD1  . ASN   B 2 18  ? -19.350 11.466  14.099  1.00 54.64 ? 404  ASN   B OD1  1 
ATOM   2163 N  ND2  . ASN   B 2 18  ? -21.583 11.325  13.915  1.00 48.33 ? 404  ASN   B ND2  1 
ATOM   2164 N  N    . HIS   B 2 19  ? -21.421 9.803   9.461   1.00 45.23 ? 405  HIS   B N    1 
ATOM   2165 C  CA   . HIS   B 2 19  ? -22.489 8.914   9.015   1.00 38.48 ? 405  HIS   B CA   1 
ATOM   2166 C  C    . HIS   B 2 19  ? -21.826 7.711   8.356   1.00 37.84 ? 405  HIS   B C    1 
ATOM   2167 O  O    . HIS   B 2 19  ? -21.185 7.846   7.308   1.00 45.53 ? 405  HIS   B O    1 
ATOM   2168 C  CB   . HIS   B 2 19  ? -23.426 9.641   8.053   1.00 29.00 ? 405  HIS   B CB   1 
ATOM   2169 C  CG   . HIS   B 2 19  ? -24.623 8.841   7.646   1.00 26.85 ? 405  HIS   B CG   1 
ATOM   2170 N  ND1  . HIS   B 2 19  ? -25.647 8.537   8.517   1.00 34.20 ? 405  HIS   B ND1  1 
ATOM   2171 C  CD2  . HIS   B 2 19  ? -24.967 8.296   6.455   1.00 30.36 ? 405  HIS   B CD2  1 
ATOM   2172 C  CE1  . HIS   B 2 19  ? -26.567 7.832   7.883   1.00 36.49 ? 405  HIS   B CE1  1 
ATOM   2173 N  NE2  . HIS   B 2 19  ? -26.179 7.673   6.630   1.00 38.96 ? 405  HIS   B NE2  1 
ATOM   2174 N  N    . LEU   B 2 20  ? -21.978 6.540   8.965   1.00 29.66 ? 406  LEU   B N    1 
ATOM   2175 C  CA   . LEU   B 2 20  ? -21.157 5.382   8.647   1.00 29.28 ? 406  LEU   B CA   1 
ATOM   2176 C  C    . LEU   B 2 20  ? -21.924 4.358   7.819   1.00 30.34 ? 406  LEU   B C    1 
ATOM   2177 O  O    . LEU   B 2 20  ? -23.134 4.176   7.981   1.00 23.92 ? 406  LEU   B O    1 
ATOM   2178 C  CB   . LEU   B 2 20  ? -20.640 4.719   9.929   1.00 29.61 ? 406  LEU   B CB   1 
ATOM   2179 C  CG   . LEU   B 2 20  ? -20.004 5.646   10.969  1.00 33.59 ? 406  LEU   B CG   1 
ATOM   2180 C  CD1  . LEU   B 2 20  ? -19.311 4.838   12.055  1.00 28.96 ? 406  LEU   B CD1  1 
ATOM   2181 C  CD2  . LEU   B 2 20  ? -19.029 6.619   10.316  1.00 36.19 ? 406  LEU   B CD2  1 
ATOM   2182 N  N    . SER   B 2 21  ? -21.199 3.686   6.929   1.00 28.82 ? 407  SER   B N    1 
ATOM   2183 C  CA   . SER   B 2 21  ? -21.732 2.558   6.175   1.00 25.52 ? 407  SER   B CA   1 
ATOM   2184 C  C    . SER   B 2 21  ? -21.445 1.277   6.950   1.00 26.40 ? 407  SER   B C    1 
ATOM   2185 O  O    . SER   B 2 21  ? -20.280 0.943   7.196   1.00 24.37 ? 407  SER   B O    1 
ATOM   2186 C  CB   . SER   B 2 21  ? -21.116 2.500   4.778   1.00 19.99 ? 407  SER   B CB   1 
ATOM   2187 O  OG   . SER   B 2 21  ? -21.327 1.236   4.175   1.00 21.60 ? 407  SER   B OG   1 
ATOM   2188 N  N    . ILE   B 2 22  ? -22.500 0.565   7.339   1.00 24.20 ? 408  ILE   B N    1 
ATOM   2189 C  CA   . ILE   B 2 22  ? -22.384 -0.622  8.177   1.00 22.18 ? 408  ILE   B CA   1 
ATOM   2190 C  C    . ILE   B 2 22  ? -23.080 -1.782  7.480   1.00 20.78 ? 408  ILE   B C    1 
ATOM   2191 O  O    . ILE   B 2 22  ? -24.215 -1.640  7.010   1.00 23.94 ? 408  ILE   B O    1 
ATOM   2192 C  CB   . ILE   B 2 22  ? -22.984 -0.391  9.578   1.00 22.96 ? 408  ILE   B CB   1 
ATOM   2193 C  CG1  . ILE   B 2 22  ? -22.296 0.793   10.261  1.00 23.93 ? 408  ILE   B CG1  1 
ATOM   2194 C  CG2  . ILE   B 2 22  ? -22.857 -1.645  10.430  1.00 19.20 ? 408  ILE   B CG2  1 
ATOM   2195 C  CD1  . ILE   B 2 22  ? -22.693 0.987   11.706  1.00 20.04 ? 408  ILE   B CD1  1 
ATOM   2196 N  N    . VAL   B 2 23  ? -22.401 -2.925  7.413   1.00 16.16 ? 409  VAL   B N    1 
ATOM   2197 C  CA   . VAL   B 2 23  ? -22.931 -4.123  6.774   1.00 19.93 ? 409  VAL   B CA   1 
ATOM   2198 C  C    . VAL   B 2 23  ? -23.319 -5.123  7.855   1.00 20.36 ? 409  VAL   B C    1 
ATOM   2199 O  O    . VAL   B 2 23  ? -22.740 -5.146  8.947   1.00 18.28 ? 409  VAL   B O    1 
ATOM   2200 C  CB   . VAL   B 2 23  ? -21.911 -4.729  5.783   1.00 19.41 ? 409  VAL   B CB   1 
ATOM   2201 C  CG1  . VAL   B 2 23  ? -20.688 -5.254  6.519   1.00 15.74 ? 409  VAL   B CG1  1 
ATOM   2202 C  CG2  . VAL   B 2 23  ? -22.552 -5.822  4.935   1.00 17.99 ? 409  VAL   B CG2  1 
ATOM   2203 N  N    . THR   B 2 24  ? -24.326 -5.942  7.552   1.00 18.62 ? 410  THR   B N    1 
ATOM   2204 C  CA   . THR   B 2 24  ? -24.767 -6.993  8.458   1.00 15.38 ? 410  THR   B CA   1 
ATOM   2205 C  C    . THR   B 2 24  ? -25.227 -8.192  7.635   1.00 17.38 ? 410  THR   B C    1 
ATOM   2206 O  O    . THR   B 2 24  ? -25.181 -8.181  6.402   1.00 18.10 ? 410  THR   B O    1 
ATOM   2207 C  CB   . THR   B 2 24  ? -25.879 -6.496  9.391   1.00 17.53 ? 410  THR   B CB   1 
ATOM   2208 O  OG1  . THR   B 2 24  ? -26.182 -7.510  10.357  1.00 12.52 ? 410  THR   B OG1  1 
ATOM   2209 C  CG2  . THR   B 2 24  ? -27.134 -6.164  8.599   1.00 14.37 ? 410  THR   B CG2  1 
ATOM   2210 N  N    . LEU   B 2 25  ? -25.671 -9.234  8.334   1.00 14.11 ? 411  LEU   B N    1 
ATOM   2211 C  CA   . LEU   B 2 25  ? -26.109 -10.473 7.708   1.00 16.30 ? 411  LEU   B CA   1 
ATOM   2212 C  C    . LEU   B 2 25  ? -27.119 -11.143 8.628   1.00 17.98 ? 411  LEU   B C    1 
ATOM   2213 O  O    . LEU   B 2 25  ? -26.943 -11.142 9.848   1.00 13.65 ? 411  LEU   B O    1 
ATOM   2214 C  CB   . LEU   B 2 25  ? -24.925 -11.410 7.438   1.00 14.30 ? 411  LEU   B CB   1 
ATOM   2215 C  CG   . LEU   B 2 25  ? -25.231 -12.884 7.162   1.00 12.70 ? 411  LEU   B CG   1 
ATOM   2216 C  CD1  . LEU   B 2 25  ? -25.785 -13.072 5.757   1.00 13.70 ? 411  LEU   B CD1  1 
ATOM   2217 C  CD2  . LEU   B 2 25  ? -23.992 -13.738 7.376   1.00 14.09 ? 411  LEU   B CD2  1 
ATOM   2218 N  N    . GLU   B 2 26  ? -28.170 -11.713 8.042   1.00 17.14 ? 412  GLU   B N    1 
ATOM   2219 C  CA   . GLU   B 2 26  ? -29.264 -12.276 8.827   1.00 15.49 ? 412  GLU   B CA   1 
ATOM   2220 C  C    . GLU   B 2 26  ? -28.865 -13.625 9.412   1.00 16.86 ? 412  GLU   B C    1 
ATOM   2221 O  O    . GLU   B 2 26  ? -28.478 -14.541 8.678   1.00 14.68 ? 412  GLU   B O    1 
ATOM   2222 C  CB   . GLU   B 2 26  ? -30.525 -12.426 7.979   1.00 15.94 ? 412  GLU   B CB   1 
ATOM   2223 C  CG   . GLU   B 2 26  ? -31.655 -13.126 8.723   1.00 16.91 ? 412  GLU   B CG   1 
ATOM   2224 C  CD   . GLU   B 2 26  ? -32.972 -13.092 7.976   1.00 18.65 ? 412  GLU   B CD   1 
ATOM   2225 O  OE1  . GLU   B 2 26  ? -32.950 -12.999 6.731   1.00 28.06 ? 412  GLU   B OE1  1 
ATOM   2226 O  OE2  . GLU   B 2 26  ? -34.030 -13.161 8.637   1.00 20.05 ? 412  GLU   B OE2  1 
ATOM   2227 N  N    . GLU   B 2 27  ? -28.971 -13.744 10.738  1.00 14.21 ? 413  GLU   B N    1 
ATOM   2228 C  CA   . GLU   B 2 27  ? -28.851 -15.035 11.413  1.00 14.10 ? 413  GLU   B CA   1 
ATOM   2229 C  C    . GLU   B 2 27  ? -29.561 -14.896 12.759  1.00 14.44 ? 413  GLU   B C    1 
ATOM   2230 O  O    . GLU   B 2 27  ? -29.021 -14.285 13.685  1.00 13.77 ? 413  GLU   B O    1 
ATOM   2231 C  CB   . GLU   B 2 27  ? -27.399 -15.453 11.586  1.00 13.12 ? 413  GLU   B CB   1 
ATOM   2232 C  CG   . GLU   B 2 27  ? -27.241 -16.784 12.305  1.00 14.95 ? 413  GLU   B CG   1 
ATOM   2233 C  CD   . GLU   B 2 27  ? -25.889 -17.428 12.067  1.00 16.99 ? 413  GLU   B CD   1 
ATOM   2234 O  OE1  . GLU   B 2 27  ? -24.883 -16.693 11.979  1.00 19.13 ? 413  GLU   B OE1  1 
ATOM   2235 O  OE2  . GLU   B 2 27  ? -25.835 -18.671 11.968  1.00 18.37 ? 413  GLU   B OE2  1 
ATOM   2236 N  N    . ALA   B 2 28  ? -30.763 -15.455 12.847  1.00 15.72 ? 414  ALA   B N    1 
ATOM   2237 C  CA   . ALA   B 2 28  ? -31.527 -15.375 14.081  1.00 17.47 ? 414  ALA   B CA   1 
ATOM   2238 C  C    . ALA   B 2 28  ? -30.785 -16.102 15.200  1.00 17.57 ? 414  ALA   B C    1 
ATOM   2239 O  O    . ALA   B 2 28  ? -30.137 -17.127 14.952  1.00 19.90 ? 414  ALA   B O    1 
ATOM   2240 C  CB   . ALA   B 2 28  ? -32.918 -15.978 13.889  1.00 18.16 ? 414  ALA   B CB   1 
ATOM   2241 N  N    . PRO   B 2 29  ? -30.855 -15.606 16.440  1.00 15.88 ? 415  PRO   B N    1 
ATOM   2242 C  CA   . PRO   B 2 29  ? -31.603 -14.434 16.907  1.00 20.21 ? 415  PRO   B CA   1 
ATOM   2243 C  C    . PRO   B 2 29  ? -30.767 -13.162 16.918  1.00 18.65 ? 415  PRO   B C    1 
ATOM   2244 O  O    . PRO   B 2 29  ? -31.172 -12.153 17.486  1.00 15.94 ? 415  PRO   B O    1 
ATOM   2245 C  CB   . PRO   B 2 29  ? -31.996 -14.850 18.322  1.00 20.98 ? 415  PRO   B CB   1 
ATOM   2246 C  CG   . PRO   B 2 29  ? -30.777 -15.612 18.798  1.00 17.13 ? 415  PRO   B CG   1 
ATOM   2247 C  CD   . PRO   B 2 29  ? -30.196 -16.293 17.566  1.00 17.64 ? 415  PRO   B CD   1 
ATOM   2248 N  N    . PHE   B 2 30  ? -29.587 -13.180 16.298  1.00 14.19 ? 416  PHE   B N    1 
ATOM   2249 C  CA   . PHE   B 2 30  ? -28.686 -12.040 16.412  1.00 17.18 ? 416  PHE   B CA   1 
ATOM   2250 C  C    . PHE   B 2 30  ? -29.010 -10.954 15.393  1.00 15.62 ? 416  PHE   B C    1 
ATOM   2251 O  O    . PHE   B 2 30  ? -28.915 -9.763  15.705  1.00 20.20 ? 416  PHE   B O    1 
ATOM   2252 C  CB   . PHE   B 2 30  ? -27.239 -12.516 16.287  1.00 18.72 ? 416  PHE   B CB   1 
ATOM   2253 C  CG   . PHE   B 2 30  ? -26.850 -13.528 17.334  1.00 20.08 ? 416  PHE   B CG   1 
ATOM   2254 C  CD1  . PHE   B 2 30  ? -26.576 -13.127 18.632  1.00 18.87 ? 416  PHE   B CD1  1 
ATOM   2255 C  CD2  . PHE   B 2 30  ? -26.778 -14.878 17.028  1.00 14.45 ? 416  PHE   B CD2  1 
ATOM   2256 C  CE1  . PHE   B 2 30  ? -26.226 -14.050 19.602  1.00 15.57 ? 416  PHE   B CE1  1 
ATOM   2257 C  CE2  . PHE   B 2 30  ? -26.430 -15.806 17.994  1.00 15.64 ? 416  PHE   B CE2  1 
ATOM   2258 C  CZ   . PHE   B 2 30  ? -26.153 -15.392 19.283  1.00 16.98 ? 416  PHE   B CZ   1 
ATOM   2259 N  N    . VAL   B 2 31  ? -29.397 -11.338 14.179  1.00 13.71 ? 417  VAL   B N    1 
ATOM   2260 C  CA   . VAL   B 2 31  ? -29.873 -10.395 13.170  1.00 17.13 ? 417  VAL   B CA   1 
ATOM   2261 C  C    . VAL   B 2 31  ? -31.083 -11.019 12.487  1.00 19.36 ? 417  VAL   B C    1 
ATOM   2262 O  O    . VAL   B 2 31  ? -30.972 -12.093 11.884  1.00 16.41 ? 417  VAL   B O    1 
ATOM   2263 C  CB   . VAL   B 2 31  ? -28.798 -10.040 12.126  1.00 13.35 ? 417  VAL   B CB   1 
ATOM   2264 C  CG1  . VAL   B 2 31  ? -29.372 -9.097  11.081  1.00 14.11 ? 417  VAL   B CG1  1 
ATOM   2265 C  CG2  . VAL   B 2 31  ? -27.582 -9.414  12.790  1.00 12.60 ? 417  VAL   B CG2  1 
ATOM   2266 N  N    . ILE   B 2 32  ? -32.232 -10.355 12.579  1.00 18.62 ? 418  ILE   B N    1 
ATOM   2267 C  CA   . ILE   B 2 32  ? -33.482 -10.834 12.005  1.00 17.68 ? 418  ILE   B CA   1 
ATOM   2268 C  C    . ILE   B 2 32  ? -33.995 -9.788  11.026  1.00 22.28 ? 418  ILE   B C    1 
ATOM   2269 O  O    . ILE   B 2 32  ? -33.981 -8.589  11.322  1.00 26.29 ? 418  ILE   B O    1 
ATOM   2270 C  CB   . ILE   B 2 32  ? -34.529 -11.127 13.101  1.00 20.99 ? 418  ILE   B CB   1 
ATOM   2271 C  CG1  . ILE   B 2 32  ? -33.987 -12.167 14.084  1.00 23.73 ? 418  ILE   B CG1  1 
ATOM   2272 C  CG2  . ILE   B 2 32  ? -35.837 -11.601 12.487  1.00 20.66 ? 418  ILE   B CG2  1 
ATOM   2273 C  CD1  . ILE   B 2 32  ? -34.830 -12.335 15.328  1.00 21.14 ? 418  ILE   B CD1  1 
ATOM   2274 N  N    . VAL   B 2 33  ? -34.449 -10.244 9.860   1.00 25.22 ? 419  VAL   B N    1 
ATOM   2275 C  CA   . VAL   B 2 33  ? -34.893 -9.369  8.781   1.00 20.11 ? 419  VAL   B CA   1 
ATOM   2276 C  C    . VAL   B 2 33  ? -36.398 -9.519  8.607   1.00 22.52 ? 419  VAL   B C    1 
ATOM   2277 O  O    . VAL   B 2 33  ? -36.932 -10.634 8.644   1.00 24.83 ? 419  VAL   B O    1 
ATOM   2278 C  CB   . VAL   B 2 33  ? -34.152 -9.683  7.466   1.00 20.33 ? 419  VAL   B CB   1 
ATOM   2279 C  CG1  . VAL   B 2 33  ? -34.655 -8.793  6.338   1.00 26.08 ? 419  VAL   B CG1  1 
ATOM   2280 C  CG2  . VAL   B 2 33  ? -32.655 -9.513  7.651   1.00 17.84 ? 419  VAL   B CG2  1 
ATOM   2281 N  N    . GLU   B 2 34  ? -37.080 -8.390  8.421   1.00 23.02 ? 420  GLU   B N    1 
ATOM   2282 C  CA   . GLU   B 2 34  ? -38.513 -8.363  8.174   1.00 27.77 ? 420  GLU   B CA   1 
ATOM   2283 C  C    . GLU   B 2 34  ? -38.808 -7.464  6.982   1.00 32.83 ? 420  GLU   B C    1 
ATOM   2284 O  O    . GLU   B 2 34  ? -37.994 -6.621  6.595   1.00 29.73 ? 420  GLU   B O    1 
ATOM   2285 C  CB   . GLU   B 2 34  ? -39.296 -7.860  9.395   1.00 29.02 ? 420  GLU   B CB   1 
ATOM   2286 C  CG   . GLU   B 2 34  ? -39.078 -8.655  10.668  1.00 34.20 ? 420  GLU   B CG   1 
ATOM   2287 C  CD   . GLU   B 2 34  ? -39.857 -8.084  11.836  1.00 35.71 ? 420  GLU   B CD   1 
ATOM   2288 O  OE1  . GLU   B 2 34  ? -40.026 -6.848  11.890  1.00 33.18 ? 420  GLU   B OE1  1 
ATOM   2289 O  OE2  . GLU   B 2 34  ? -40.308 -8.871  12.694  1.00 42.33 ? 420  GLU   B OE2  1 
ATOM   2290 N  N    . ASP   B 2 35  ? -39.993 -7.652  6.405   1.00 33.00 ? 421  ASP   B N    1 
ATOM   2291 C  CA   . ASP   B 2 35  ? -40.478 -6.757  5.367   1.00 39.42 ? 421  ASP   B CA   1 
ATOM   2292 C  C    . ASP   B 2 35  ? -41.031 -5.483  6.002   1.00 38.87 ? 421  ASP   B C    1 
ATOM   2293 O  O    . ASP   B 2 35  ? -40.978 -5.287  7.219   1.00 39.85 ? 421  ASP   B O    1 
ATOM   2294 C  CB   . ASP   B 2 35  ? -41.540 -7.450  4.515   1.00 41.80 ? 421  ASP   B CB   1 
ATOM   2295 C  CG   . ASP   B 2 35  ? -40.985 -8.621  3.726   1.00 46.25 ? 421  ASP   B CG   1 
ATOM   2296 O  OD1  . ASP   B 2 35  ? -40.040 -8.415  2.937   1.00 42.43 ? 421  ASP   B OD1  1 
ATOM   2297 O  OD2  . ASP   B 2 35  ? -41.500 -9.748  3.891   1.00 57.76 ? 421  ASP   B OD2  1 
ATOM   2298 N  N    . ILE   B 2 36  ? -41.575 -4.602  5.169   1.00 47.93 ? 422  ILE   B N    1 
ATOM   2299 C  CA   . ILE   B 2 36  ? -42.168 -3.369  5.669   1.00 50.64 ? 422  ILE   B CA   1 
ATOM   2300 C  C    . ILE   B 2 36  ? -43.356 -2.949  4.811   1.00 55.05 ? 422  ILE   B C    1 
ATOM   2301 O  O    . ILE   B 2 36  ? -44.359 -2.454  5.326   1.00 59.65 ? 422  ILE   B O    1 
ATOM   2302 C  CB   . ILE   B 2 36  ? -41.125 -2.242  5.742   1.00 44.79 ? 422  ILE   B CB   1 
ATOM   2303 C  CG1  . ILE   B 2 36  ? -41.621 -1.133  6.668   1.00 52.48 ? 422  ILE   B CG1  1 
ATOM   2304 C  CG2  . ILE   B 2 36  ? -40.839 -1.688  4.355   1.00 43.81 ? 422  ILE   B CG2  1 
ATOM   2305 C  CD1  . ILE   B 2 36  ? -42.223 -1.652  7.957   1.00 49.95 ? 422  ILE   B CD1  1 
ATOM   2306 N  N    . GLU   B 2 41  ? -44.370 1.847   4.541   1.00 62.48 ? 427  GLU   B N    1 
ATOM   2307 C  CA   . GLU   B 2 41  ? -42.950 1.707   4.241   1.00 66.34 ? 427  GLU   B CA   1 
ATOM   2308 C  C    . GLU   B 2 41  ? -42.094 2.422   5.281   1.00 72.34 ? 427  GLU   B C    1 
ATOM   2309 O  O    . GLU   B 2 41  ? -41.248 3.248   4.939   1.00 80.30 ? 427  GLU   B O    1 
ATOM   2310 C  CB   . GLU   B 2 41  ? -42.643 2.248   2.843   1.00 65.31 ? 427  GLU   B CB   1 
ATOM   2311 N  N    . THR   B 2 42  ? -42.318 2.095   6.553   1.00 62.28 ? 428  THR   B N    1 
ATOM   2312 C  CA   . THR   B 2 42  ? -41.582 2.710   7.654   1.00 56.53 ? 428  THR   B CA   1 
ATOM   2313 C  C    . THR   B 2 42  ? -41.364 1.667   8.738   1.00 59.14 ? 428  THR   B C    1 
ATOM   2314 O  O    . THR   B 2 42  ? -42.334 1.179   9.326   1.00 69.02 ? 428  THR   B O    1 
ATOM   2315 C  CB   . THR   B 2 42  ? -42.340 3.914   8.220   1.00 58.66 ? 428  THR   B CB   1 
ATOM   2316 O  OG1  . THR   B 2 42  ? -43.747 3.642   8.208   1.00 76.52 ? 428  THR   B OG1  1 
ATOM   2317 C  CG2  . THR   B 2 42  ? -42.059 5.166   7.398   1.00 63.92 ? 428  THR   B CG2  1 
ATOM   2318 N  N    . CYS   B 2 43  ? -40.101 1.333   9.002   1.00 53.15 ? 429  CYS   B N    1 
ATOM   2319 C  CA   . CYS   B 2 43  ? -39.781 0.370   10.048  1.00 47.10 ? 429  CYS   B CA   1 
ATOM   2320 C  C    . CYS   B 2 43  ? -40.281 0.863   11.401  1.00 51.99 ? 429  CYS   B C    1 
ATOM   2321 O  O    . CYS   B 2 43  ? -40.255 2.062   11.692  1.00 55.98 ? 429  CYS   B O    1 
ATOM   2322 C  CB   . CYS   B 2 43  ? -38.273 0.122   10.097  1.00 40.45 ? 429  CYS   B CB   1 
ATOM   2323 S  SG   . CYS   B 2 43  ? -37.604 -0.667  8.615   1.00 31.66 ? 429  CYS   B SG   1 
ATOM   2324 N  N    . VAL   B 2 44  ? -40.740 -0.073  12.233  1.00 54.05 ? 430  VAL   B N    1 
ATOM   2325 C  CA   . VAL   B 2 44  ? -41.448 0.250   13.464  1.00 57.27 ? 430  VAL   B CA   1 
ATOM   2326 C  C    . VAL   B 2 44  ? -40.809 -0.487  14.635  1.00 52.93 ? 430  VAL   B C    1 
ATOM   2327 O  O    . VAL   B 2 44  ? -40.008 -1.406  14.463  1.00 56.27 ? 430  VAL   B O    1 
ATOM   2328 C  CB   . VAL   B 2 44  ? -42.948 -0.098  13.376  1.00 62.85 ? 430  VAL   B CB   1 
ATOM   2329 C  CG1  . VAL   B 2 44  ? -43.641 0.778   12.343  1.00 61.69 ? 430  VAL   B CG1  1 
ATOM   2330 C  CG2  . VAL   B 2 44  ? -43.128 -1.573  13.044  1.00 63.45 ? 430  VAL   B CG2  1 
ATOM   2331 N  N    . ARG   B 2 45  ? -41.181 -0.052  15.838  1.00 60.94 ? 431  ARG   B N    1 
ATOM   2332 C  CA   . ARG   B 2 45  ? -40.875 -0.734  17.106  1.00 58.64 ? 431  ARG   B CA   1 
ATOM   2333 C  C    . ARG   B 2 45  ? -39.360 -0.863  17.247  1.00 54.69 ? 431  ARG   B C    1 
ATOM   2334 O  O    . ARG   B 2 45  ? -38.643 0.129   17.040  1.00 54.70 ? 431  ARG   B O    1 
ATOM   2335 C  CB   . ARG   B 2 45  ? -41.657 -2.042  17.158  1.00 62.68 ? 431  ARG   B CB   1 
ATOM   2336 C  CG   . ARG   B 2 45  ? -43.163 -1.871  17.028  1.00 64.61 ? 431  ARG   B CG   1 
ATOM   2337 C  CD   . ARG   B 2 45  ? -43.912 -3.011  17.700  1.00 65.61 ? 431  ARG   B CD   1 
ATOM   2338 N  NE   . ARG   B 2 45  ? -44.209 -2.725  19.099  1.00 67.96 ? 431  ARG   B NE   1 
ATOM   2339 C  CZ   . ARG   B 2 45  ? -43.465 -3.123  20.121  1.00 67.74 ? 431  ARG   B CZ   1 
ATOM   2340 N  NH1  . ARG   B 2 45  ? -42.364 -3.834  19.940  1.00 72.04 ? 431  ARG   B NH1  1 
ATOM   2341 N  NH2  . ARG   B 2 45  ? -43.834 -2.800  21.358  1.00 55.56 ? 431  ARG   B NH2  1 
ATOM   2342 N  N    . ASN   B 2 46  ? -38.832 -2.037  17.592  1.00 59.55 ? 432  ASN   B N    1 
ATOM   2343 C  CA   . ASN   B 2 46  ? -37.415 -2.229  17.871  1.00 58.57 ? 432  ASN   B CA   1 
ATOM   2344 C  C    . ASN   B 2 46  ? -36.582 -2.460  16.618  1.00 53.30 ? 432  ASN   B C    1 
ATOM   2345 O  O    . ASN   B 2 46  ? -35.398 -2.795  16.736  1.00 52.95 ? 432  ASN   B O    1 
ATOM   2346 C  CB   . ASN   B 2 46  ? -37.233 -3.405  18.833  1.00 62.38 ? 432  ASN   B CB   1 
ATOM   2347 C  CG   . ASN   B 2 46  ? -37.938 -4.662  18.355  1.00 63.57 ? 432  ASN   B CG   1 
ATOM   2348 O  OD1  . ASN   B 2 46  ? -39.053 -4.602  17.836  1.00 58.88 ? 432  ASN   B OD1  1 
ATOM   2349 N  ND2  . ASN   B 2 46  ? -37.290 -5.808  18.528  1.00 56.87 ? 432  ASN   B ND2  1 
ATOM   2350 N  N    . THR   B 2 47  ? -37.158 -2.296  15.433  1.00 37.90 ? 433  THR   B N    1 
ATOM   2351 C  CA   . THR   B 2 47  ? -36.439 -2.548  14.194  1.00 39.94 ? 433  THR   B CA   1 
ATOM   2352 C  C    . THR   B 2 47  ? -35.821 -1.263  13.658  1.00 38.24 ? 433  THR   B C    1 
ATOM   2353 O  O    . THR   B 2 47  ? -36.325 -0.161  13.891  1.00 38.57 ? 433  THR   B O    1 
ATOM   2354 C  CB   . THR   B 2 47  ? -37.365 -3.156  13.140  1.00 35.96 ? 433  THR   B CB   1 
ATOM   2355 O  OG1  . THR   B 2 47  ? -38.117 -2.115  12.504  1.00 36.87 ? 433  THR   B OG1  1 
ATOM   2356 C  CG2  . THR   B 2 47  ? -38.324 -4.146  13.781  1.00 33.75 ? 433  THR   B CG2  1 
ATOM   2357 N  N    . VAL   B 2 48  ? -34.714 -1.418  12.939  1.00 32.30 ? 434  VAL   B N    1 
ATOM   2358 C  CA   . VAL   B 2 48  ? -34.032 -0.300  12.292  1.00 30.62 ? 434  VAL   B CA   1 
ATOM   2359 C  C    . VAL   B 2 48  ? -34.017 -0.564  10.790  1.00 30.08 ? 434  VAL   B C    1 
ATOM   2360 O  O    . VAL   B 2 48  ? -34.067 -1.729  10.368  1.00 25.38 ? 434  VAL   B O    1 
ATOM   2361 C  CB   . VAL   B 2 48  ? -32.611 -0.107  12.848  1.00 26.91 ? 434  VAL   B CB   1 
ATOM   2362 C  CG1  . VAL   B 2 48  ? -32.654 0.106   14.353  1.00 28.50 ? 434  VAL   B CG1  1 
ATOM   2363 C  CG2  . VAL   B 2 48  ? -31.729 -1.295  12.494  1.00 24.65 ? 434  VAL   B CG2  1 
ATOM   2364 N  N    . PRO   B 2 49  ? -33.963 0.469   9.949   1.00 26.69 ? 435  PRO   B N    1 
ATOM   2365 C  CA   . PRO   B 2 49  ? -34.000 0.238   8.498   1.00 25.67 ? 435  PRO   B CA   1 
ATOM   2366 C  C    . PRO   B 2 49  ? -32.698 -0.368  7.995   1.00 27.47 ? 435  PRO   B C    1 
ATOM   2367 O  O    . PRO   B 2 49  ? -31.606 0.091   8.338   1.00 24.03 ? 435  PRO   B O    1 
ATOM   2368 C  CB   . PRO   B 2 49  ? -34.230 1.640   7.922   1.00 29.11 ? 435  PRO   B CB   1 
ATOM   2369 C  CG   . PRO   B 2 49  ? -33.680 2.562   8.958   1.00 29.42 ? 435  PRO   B CG   1 
ATOM   2370 C  CD   . PRO   B 2 49  ? -33.960 1.905   10.281  1.00 29.12 ? 435  PRO   B CD   1 
ATOM   2371 N  N    . CYS   B 2 50  ? -32.825 -1.407  7.174   1.00 26.22 ? 436  CYS   B N    1 
ATOM   2372 C  CA   . CYS   B 2 50  ? -31.686 -2.038  6.520   1.00 20.92 ? 436  CYS   B CA   1 
ATOM   2373 C  C    . CYS   B 2 50  ? -32.079 -2.380  5.092   1.00 27.26 ? 436  CYS   B C    1 
ATOM   2374 O  O    . CYS   B 2 50  ? -33.169 -2.910  4.856   1.00 26.83 ? 436  CYS   B O    1 
ATOM   2375 C  CB   . CYS   B 2 50  ? -31.232 -3.297  7.271   1.00 23.87 ? 436  CYS   B CB   1 
ATOM   2376 S  SG   . CYS   B 2 50  ? -32.520 -4.542  7.525   1.00 27.58 ? 436  CYS   B SG   1 
ATOM   2377 N  N    . ARG   B 2 51  ? -31.200 -2.070  4.145   1.00 25.06 ? 437  ARG   B N    1 
ATOM   2378 C  CA   . ARG   B 2 51  ? -31.467 -2.282  2.731   1.00 23.55 ? 437  ARG   B CA   1 
ATOM   2379 C  C    . ARG   B 2 51  ? -30.736 -3.521  2.228   1.00 20.86 ? 437  ARG   B C    1 
ATOM   2380 O  O    . ARG   B 2 51  ? -29.704 -3.922  2.772   1.00 23.41 ? 437  ARG   B O    1 
ATOM   2381 C  CB   . ARG   B 2 51  ? -31.049 -1.060  1.909   1.00 28.89 ? 437  ARG   B CB   1 
ATOM   2382 C  CG   . ARG   B 2 51  ? -29.644 -0.558  2.209   1.00 30.10 ? 437  ARG   B CG   1 
ATOM   2383 C  CD   . ARG   B 2 51  ? -29.272 0.618   1.319   1.00 31.93 ? 437  ARG   B CD   1 
ATOM   2384 N  NE   . ARG   B 2 51  ? -28.101 1.331   1.815   1.00 39.41 ? 437  ARG   B NE   1 
ATOM   2385 C  CZ   . ARG   B 2 51  ? -26.850 1.046   1.480   1.00 38.08 ? 437  ARG   B CZ   1 
ATOM   2386 N  NH1  . ARG   B 2 51  ? -26.566 0.066   0.638   1.00 32.62 ? 437  ARG   B NH1  1 
ATOM   2387 N  NH2  . ARG   B 2 51  ? -25.859 1.762   2.004   1.00 37.63 ? 437  ARG   B NH2  1 
ATOM   2388 N  N    . LYS   B 2 52  ? -31.286 -4.128  1.177   1.00 22.58 ? 438  LYS   B N    1 
ATOM   2389 C  CA   . LYS   B 2 52  ? -30.682 -5.307  0.566   1.00 22.27 ? 438  LYS   B CA   1 
ATOM   2390 C  C    . LYS   B 2 52  ? -30.711 -5.151  -0.946  1.00 22.06 ? 438  LYS   B C    1 
ATOM   2391 O  O    . LYS   B 2 52  ? -31.778 -4.935  -1.529  1.00 22.79 ? 438  LYS   B O    1 
ATOM   2392 C  CB   . LYS   B 2 52  ? -31.405 -6.591  0.987   1.00 22.74 ? 438  LYS   B CB   1 
ATOM   2393 C  CG   . LYS   B 2 52  ? -30.785 -7.851  0.399   1.00 25.56 ? 438  LYS   B CG   1 
ATOM   2394 C  CD   . LYS   B 2 52  ? -31.388 -9.110  0.998   1.00 23.40 ? 438  LYS   B CD   1 
ATOM   2395 C  CE   . LYS   B 2 52  ? -32.834 -9.283  0.574   1.00 33.73 ? 438  LYS   B CE   1 
ATOM   2396 N  NZ   . LYS   B 2 52  ? -33.342 -10.644 0.895   1.00 38.69 ? 438  LYS   B NZ   1 
ATOM   2397 N  N    . PHE   B 2 53  ? -29.542 -5.260  -1.571  1.00 20.27 ? 439  PHE   B N    1 
ATOM   2398 C  CA   . PHE   B 2 53  ? -29.443 -5.208  -3.024  1.00 19.02 ? 439  PHE   B CA   1 
ATOM   2399 C  C    . PHE   B 2 53  ? -29.946 -6.518  -3.619  1.00 19.52 ? 439  PHE   B C    1 
ATOM   2400 O  O    . PHE   B 2 53  ? -29.403 -7.588  -3.327  1.00 16.29 ? 439  PHE   B O    1 
ATOM   2401 C  CB   . PHE   B 2 53  ? -27.997 -4.946  -3.437  1.00 22.51 ? 439  PHE   B CB   1 
ATOM   2402 C  CG   . PHE   B 2 53  ? -27.820 -4.656  -4.900  1.00 25.20 ? 439  PHE   B CG   1 
ATOM   2403 C  CD1  . PHE   B 2 53  ? -28.109 -3.401  -5.413  1.00 25.74 ? 439  PHE   B CD1  1 
ATOM   2404 C  CD2  . PHE   B 2 53  ? -27.351 -5.634  -5.761  1.00 21.93 ? 439  PHE   B CD2  1 
ATOM   2405 C  CE1  . PHE   B 2 53  ? -27.940 -3.131  -6.759  1.00 23.19 ? 439  PHE   B CE1  1 
ATOM   2406 C  CE2  . PHE   B 2 53  ? -27.181 -5.371  -7.107  1.00 22.53 ? 439  PHE   B CE2  1 
ATOM   2407 C  CZ   . PHE   B 2 53  ? -27.474 -4.118  -7.606  1.00 24.35 ? 439  PHE   B CZ   1 
ATOM   2408 N  N    . VAL   B 2 54  ? -30.985 -6.438  -4.447  1.00 17.76 ? 440  VAL   B N    1 
ATOM   2409 C  CA   . VAL   B 2 54  ? -31.606 -7.611  -5.051  1.00 19.57 ? 440  VAL   B CA   1 
ATOM   2410 C  C    . VAL   B 2 54  ? -31.525 -7.470  -6.565  1.00 22.31 ? 440  VAL   B C    1 
ATOM   2411 O  O    . VAL   B 2 54  ? -31.953 -6.453  -7.123  1.00 21.18 ? 440  VAL   B O    1 
ATOM   2412 C  CB   . VAL   B 2 54  ? -33.064 -7.781  -4.589  1.00 21.30 ? 440  VAL   B CB   1 
ATOM   2413 C  CG1  . VAL   B 2 54  ? -33.701 -8.963  -5.288  1.00 18.93 ? 440  VAL   B CG1  1 
ATOM   2414 C  CG2  . VAL   B 2 54  ? -33.126 -7.953  -3.079  1.00 19.80 ? 440  VAL   B CG2  1 
ATOM   2415 N  N    . LYS   B 2 55  ? -30.985 -8.492  -7.224  1.00 24.39 ? 441  LYS   B N    1 
ATOM   2416 C  CA   . LYS   B 2 55  ? -30.738 -8.424  -8.658  1.00 26.00 ? 441  LYS   B CA   1 
ATOM   2417 C  C    . LYS   B 2 55  ? -32.037 -8.529  -9.451  1.00 25.71 ? 441  LYS   B C    1 
ATOM   2418 O  O    . LYS   B 2 55  ? -33.010 -9.154  -9.021  1.00 20.97 ? 441  LYS   B O    1 
ATOM   2419 C  CB   . LYS   B 2 55  ? -29.782 -9.537  -9.087  1.00 25.43 ? 441  LYS   B CB   1 
ATOM   2420 C  CG   . LYS   B 2 55  ? -28.511 -9.622  -8.259  1.00 33.50 ? 441  LYS   B CG   1 
ATOM   2421 C  CD   . LYS   B 2 55  ? -27.679 -10.832 -8.654  1.00 50.99 ? 441  LYS   B CD   1 
ATOM   2422 C  CE   . LYS   B 2 55  ? -27.188 -10.724 -10.090 1.00 56.72 ? 441  LYS   B CE   1 
ATOM   2423 N  NZ   . LYS   B 2 55  ? -27.323 -12.016 -10.821 1.00 43.87 ? 441  LYS   B NZ   1 
ATOM   2424 N  N    . ILE   B 2 56  ? -32.037 -7.905  -10.631 1.00 23.07 ? 442  ILE   B N    1 
ATOM   2425 C  CA   . ILE   B 2 56  ? -33.188 -7.996  -11.525 1.00 26.96 ? 442  ILE   B CA   1 
ATOM   2426 C  C    . ILE   B 2 56  ? -33.261 -9.382  -12.154 1.00 27.47 ? 442  ILE   B C    1 
ATOM   2427 O  O    . ILE   B 2 56  ? -34.316 -10.028 -12.151 1.00 29.83 ? 442  ILE   B O    1 
ATOM   2428 C  CB   . ILE   B 2 56  ? -33.126 -6.890  -12.594 1.00 31.90 ? 442  ILE   B CB   1 
ATOM   2429 C  CG1  . ILE   B 2 56  ? -33.074 -5.510  -11.934 1.00 28.55 ? 442  ILE   B CG1  1 
ATOM   2430 C  CG2  . ILE   B 2 56  ? -34.312 -6.992  -13.539 1.00 30.36 ? 442  ILE   B CG2  1 
ATOM   2431 C  CD1  . ILE   B 2 56  ? -34.285 -5.191  -11.083 1.00 32.98 ? 442  ILE   B CD1  1 
ATOM   2432 N  N    . ASN   B 2 57  ? -32.147 -9.855  -12.706 1.00 30.47 ? 443  ASN   B N    1 
ATOM   2433 C  CA   . ASN   B 2 57  ? -32.051 -11.220 -13.210 1.00 31.07 ? 443  ASN   B CA   1 
ATOM   2434 C  C    . ASN   B 2 57  ? -30.581 -11.622 -13.201 1.00 35.17 ? 443  ASN   B C    1 
ATOM   2435 O  O    . ASN   B 2 57  ? -29.718 -10.882 -12.722 1.00 39.30 ? 443  ASN   B O    1 
ATOM   2436 C  CB   . ASN   B 2 57  ? -32.684 -11.352 -14.601 1.00 29.90 ? 443  ASN   B CB   1 
ATOM   2437 C  CG   . ASN   B 2 57  ? -31.996 -10.500 -15.647 1.00 37.72 ? 443  ASN   B CG   1 
ATOM   2438 O  OD1  . ASN   B 2 57  ? -30.884 -10.801 -16.074 1.00 40.71 ? 443  ASN   B OD1  1 
ATOM   2439 N  ND2  . ASN   B 2 57  ? -32.656 -9.424  -16.064 1.00 37.19 ? 443  ASN   B ND2  1 
ATOM   2440 N  N    . ASN   B 2 58  ? -30.301 -12.812 -13.731 1.00 37.79 ? 444  ASN   B N    1 
ATOM   2441 C  CA   . ASN   B 2 58  ? -28.955 -13.368 -13.729 1.00 35.38 ? 444  ASN   B CA   1 
ATOM   2442 C  C    . ASN   B 2 58  ? -28.223 -13.150 -15.047 1.00 40.90 ? 444  ASN   B C    1 
ATOM   2443 O  O    . ASN   B 2 58  ? -27.131 -13.696 -15.237 1.00 41.82 ? 444  ASN   B O    1 
ATOM   2444 C  CB   . ASN   B 2 58  ? -29.002 -14.859 -13.392 1.00 24.64 ? 444  ASN   B CB   1 
ATOM   2445 C  CG   . ASN   B 2 58  ? -29.660 -15.129 -12.053 1.00 31.40 ? 444  ASN   B CG   1 
ATOM   2446 O  OD1  . ASN   B 2 58  ? -29.536 -14.338 -11.117 1.00 28.83 ? 444  ASN   B OD1  1 
ATOM   2447 N  ND2  . ASN   B 2 58  ? -30.366 -16.249 -11.954 1.00 26.91 ? 444  ASN   B ND2  1 
ATOM   2448 N  N    . SER   B 2 59  ? -28.797 -12.368 -15.958 1.00 45.28 ? 445  SER   B N    1 
ATOM   2449 C  CA   . SER   B 2 59  ? -28.119 -11.965 -17.181 1.00 47.03 ? 445  SER   B CA   1 
ATOM   2450 C  C    . SER   B 2 59  ? -27.624 -10.526 -17.124 1.00 50.54 ? 445  SER   B C    1 
ATOM   2451 O  O    . SER   B 2 59  ? -27.078 -10.033 -18.115 1.00 56.04 ? 445  SER   B O    1 
ATOM   2452 C  CB   . SER   B 2 59  ? -29.049 -12.142 -18.387 1.00 45.19 ? 445  SER   B CB   1 
ATOM   2453 O  OG   . SER   B 2 59  ? -29.664 -13.418 -18.383 1.00 45.99 ? 445  SER   B OG   1 
ATOM   2454 N  N    . THR   B 2 60  ? -27.798 -9.844  -15.993 1.00 42.94 ? 446  THR   B N    1 
ATOM   2455 C  CA   . THR   B 2 60  ? -27.404 -8.450  -15.867 1.00 45.47 ? 446  THR   B CA   1 
ATOM   2456 C  C    . THR   B 2 60  ? -26.781 -8.220  -14.499 1.00 41.95 ? 446  THR   B C    1 
ATOM   2457 O  O    . THR   B 2 60  ? -26.952 -9.016  -13.571 1.00 38.22 ? 446  THR   B O    1 
ATOM   2458 C  CB   . THR   B 2 60  ? -28.592 -7.494  -16.026 1.00 42.08 ? 446  THR   B CB   1 
ATOM   2459 O  OG1  . THR   B 2 60  ? -28.191 -6.179  -15.623 1.00 47.54 ? 446  THR   B OG1  1 
ATOM   2460 C  CG2  . THR   B 2 60  ? -29.741 -7.937  -15.129 1.00 44.67 ? 446  THR   B CG2  1 
ATOM   2461 N  N    . ASN   B 2 61  ? -26.061 -7.108  -14.385 1.00 32.60 ? 447  ASN   B N    1 
ATOM   2462 C  CA   . ASN   B 2 61  ? -25.594 -6.604  -13.102 1.00 32.28 ? 447  ASN   B CA   1 
ATOM   2463 C  C    . ASN   B 2 61  ? -26.598 -5.661  -12.455 1.00 36.80 ? 447  ASN   B C    1 
ATOM   2464 O  O    . ASN   B 2 61  ? -26.332 -5.142  -11.365 1.00 36.74 ? 447  ASN   B O    1 
ATOM   2465 C  CB   . ASN   B 2 61  ? -24.251 -5.887  -13.274 1.00 35.20 ? 447  ASN   B CB   1 
ATOM   2466 C  CG   . ASN   B 2 61  ? -23.160 -6.810  -13.779 1.00 34.84 ? 447  ASN   B CG   1 
ATOM   2467 O  OD1  . ASN   B 2 61  ? -22.992 -7.922  -13.279 1.00 43.24 ? 447  ASN   B OD1  1 
ATOM   2468 N  ND2  . ASN   B 2 61  ? -22.414 -6.353  -14.778 1.00 33.06 ? 447  ASN   B ND2  1 
ATOM   2469 N  N    . GLU   B 2 62  ? -27.739 -5.431  -13.099 1.00 31.60 ? 448  GLU   B N    1 
ATOM   2470 C  CA   . GLU   B 2 62  ? -28.730 -4.497  -12.587 1.00 30.64 ? 448  GLU   B CA   1 
ATOM   2471 C  C    . GLU   B 2 62  ? -29.421 -5.060  -11.351 1.00 26.87 ? 448  GLU   B C    1 
ATOM   2472 O  O    . GLU   B 2 62  ? -29.622 -6.269  -11.214 1.00 32.47 ? 448  GLU   B O    1 
ATOM   2473 C  CB   . GLU   B 2 62  ? -29.770 -4.182  -13.663 1.00 37.43 ? 448  GLU   B CB   1 
ATOM   2474 C  CG   . GLU   B 2 62  ? -29.936 -2.702  -13.962 1.00 46.34 ? 448  GLU   B CG   1 
ATOM   2475 C  CD   . GLU   B 2 62  ? -31.138 -2.422  -14.841 1.00 50.99 ? 448  GLU   B CD   1 
ATOM   2476 O  OE1  . GLU   B 2 62  ? -31.655 -3.375  -15.461 1.00 49.78 ? 448  GLU   B OE1  1 
ATOM   2477 O  OE2  . GLU   B 2 62  ? -31.564 -1.250  -14.918 1.00 57.30 ? 448  GLU   B OE2  1 
ATOM   2478 N  N    . GLY   B 2 63  ? -29.785 -4.160  -10.446 1.00 31.42 ? 449  GLY   B N    1 
ATOM   2479 C  CA   . GLY   B 2 63  ? -30.499 -4.539  -9.243  1.00 24.38 ? 449  GLY   B CA   1 
ATOM   2480 C  C    . GLY   B 2 63  ? -31.043 -3.301  -8.572  1.00 24.90 ? 449  GLY   B C    1 
ATOM   2481 O  O    . GLY   B 2 63  ? -30.824 -2.175  -9.025  1.00 26.00 ? 449  GLY   B O    1 
ATOM   2482 N  N    . MET   B 2 64  ? -31.762 -3.521  -7.475  1.00 20.32 ? 450  MET   B N    1 
ATOM   2483 C  CA   . MET   B 2 64  ? -32.352 -2.411  -6.743  1.00 21.06 ? 450  MET   B CA   1 
ATOM   2484 C  C    . MET   B 2 64  ? -32.343 -2.722  -5.256  1.00 23.42 ? 450  MET   B C    1 
ATOM   2485 O  O    . MET   B 2 64  ? -32.501 -3.874  -4.845  1.00 21.69 ? 450  MET   B O    1 
ATOM   2486 C  CB   . MET   B 2 64  ? -33.779 -2.114  -7.214  1.00 25.34 ? 450  MET   B CB   1 
ATOM   2487 C  CG   . MET   B 2 64  ? -33.854 -1.189  -8.420  1.00 29.36 ? 450  MET   B CG   1 
ATOM   2488 S  SD   . MET   B 2 64  ? -35.485 -1.176  -9.176  1.00 44.12 ? 450  MET   B SD   1 
ATOM   2489 C  CE   . MET   B 2 64  ? -36.454 -0.539  -7.813  1.00 40.16 ? 450  MET   B CE   1 
ATOM   2490 N  N    . ASN   B 2 65  ? -32.153 -1.676  -4.457  1.00 25.47 ? 451  ASN   B N    1 
ATOM   2491 C  CA   . ASN   B 2 65  ? -32.147 -1.805  -3.007  1.00 24.40 ? 451  ASN   B CA   1 
ATOM   2492 C  C    . ASN   B 2 65  ? -33.580 -1.920  -2.504  1.00 25.48 ? 451  ASN   B C    1 
ATOM   2493 O  O    . ASN   B 2 65  ? -34.390 -1.010  -2.708  1.00 29.20 ? 451  ASN   B O    1 
ATOM   2494 C  CB   . ASN   B 2 65  ? -31.450 -0.605  -2.370  1.00 26.30 ? 451  ASN   B CB   1 
ATOM   2495 C  CG   . ASN   B 2 65  ? -30.003 -0.475  -2.801  1.00 31.42 ? 451  ASN   B CG   1 
ATOM   2496 O  OD1  . ASN   B 2 65  ? -29.253 -1.451  -2.801  1.00 35.23 ? 451  ASN   B OD1  1 
ATOM   2497 N  ND2  . ASN   B 2 65  ? -29.603 0.736   -3.173  1.00 33.69 ? 451  ASN   B ND2  1 
ATOM   2498 N  N    . VAL   B 2 66  ? -33.895 -3.038  -1.858  1.00 24.06 ? 452  VAL   B N    1 
ATOM   2499 C  CA   . VAL   B 2 66  ? -35.203 -3.239  -1.245  1.00 23.35 ? 452  VAL   B CA   1 
ATOM   2500 C  C    . VAL   B 2 66  ? -35.121 -2.788  0.206   1.00 25.05 ? 452  VAL   B C    1 
ATOM   2501 O  O    . VAL   B 2 66  ? -34.296 -3.292  0.977   1.00 25.00 ? 452  VAL   B O    1 
ATOM   2502 C  CB   . VAL   B 2 66  ? -35.648 -4.705  -1.342  1.00 25.40 ? 452  VAL   B CB   1 
ATOM   2503 C  CG1  . VAL   B 2 66  ? -37.025 -4.884  -0.714  1.00 24.36 ? 452  VAL   B CG1  1 
ATOM   2504 C  CG2  . VAL   B 2 66  ? -35.651 -5.166  -2.790  1.00 22.89 ? 452  VAL   B CG2  1 
ATOM   2505 N  N    . LYS   B 2 67  ? -35.970 -1.835  0.579   1.00 23.64 ? 453  LYS   B N    1 
ATOM   2506 C  CA   . LYS   B 2 67  ? -36.003 -1.352  1.953   1.00 25.49 ? 453  LYS   B CA   1 
ATOM   2507 C  C    . LYS   B 2 67  ? -36.619 -2.414  2.856   1.00 24.89 ? 453  LYS   B C    1 
ATOM   2508 O  O    . LYS   B 2 67  ? -37.773 -2.811  2.662   1.00 34.49 ? 453  LYS   B O    1 
ATOM   2509 C  CB   . LYS   B 2 67  ? -36.791 -0.047  2.036   1.00 23.32 ? 453  LYS   B CB   1 
ATOM   2510 N  N    . LYS   B 2 68  ? -35.848 -2.882  3.835   1.00 19.85 ? 454  LYS   B N    1 
ATOM   2511 C  CA   . LYS   B 2 68  ? -36.306 -3.872  4.799   1.00 26.15 ? 454  LYS   B CA   1 
ATOM   2512 C  C    . LYS   B 2 68  ? -36.043 -3.352  6.208   1.00 30.88 ? 454  LYS   B C    1 
ATOM   2513 O  O    . LYS   B 2 68  ? -35.543 -2.239  6.403   1.00 26.97 ? 454  LYS   B O    1 
ATOM   2514 C  CB   . LYS   B 2 68  ? -35.621 -5.227  4.573   1.00 25.68 ? 454  LYS   B CB   1 
ATOM   2515 C  CG   . LYS   B 2 68  ? -35.537 -5.648  3.113   1.00 28.63 ? 454  LYS   B CG   1 
ATOM   2516 C  CD   . LYS   B 2 68  ? -35.498 -7.161  2.973   1.00 29.87 ? 454  LYS   B CD   1 
ATOM   2517 C  CE   . LYS   B 2 68  ? -36.835 -7.782  3.349   1.00 33.13 ? 454  LYS   B CE   1 
ATOM   2518 N  NZ   . LYS   B 2 68  ? -36.820 -9.265  3.211   1.00 42.49 ? 454  LYS   B NZ   1 
ATOM   2519 N  N    . CYS   B 2 69  ? -36.389 -4.168  7.201   1.00 22.90 ? 455  CYS   B N    1 
ATOM   2520 C  CA   . CYS   B 2 69  ? -36.216 -3.817  8.603   1.00 24.44 ? 455  CYS   B CA   1 
ATOM   2521 C  C    . CYS   B 2 69  ? -35.419 -4.906  9.303   1.00 23.29 ? 455  CYS   B C    1 
ATOM   2522 O  O    . CYS   B 2 69  ? -35.590 -6.095  9.018   1.00 24.67 ? 455  CYS   B O    1 
ATOM   2523 C  CB   . CYS   B 2 69  ? -37.568 -3.617  9.297   1.00 25.33 ? 455  CYS   B CB   1 
ATOM   2524 S  SG   . CYS   B 2 69  ? -38.637 -2.411  8.481   1.00 32.07 ? 455  CYS   B SG   1 
ATOM   2525 N  N    . CYS   B 2 70  ? -34.548 -4.493  10.222  1.00 21.03 ? 456  CYS   B N    1 
ATOM   2526 C  CA   . CYS   B 2 70  ? -33.637 -5.401  10.901  1.00 22.99 ? 456  CYS   B CA   1 
ATOM   2527 C  C    . CYS   B 2 70  ? -33.785 -5.263  12.408  1.00 23.82 ? 456  CYS   B C    1 
ATOM   2528 O  O    . CYS   B 2 70  ? -33.949 -4.155  12.927  1.00 23.86 ? 456  CYS   B O    1 
ATOM   2529 C  CB   . CYS   B 2 70  ? -32.185 -5.130  10.492  1.00 21.85 ? 456  CYS   B CB   1 
ATOM   2530 S  SG   . CYS   B 2 70  ? -31.720 -5.823  8.886   1.00 25.85 ? 456  CYS   B SG   1 
ATOM   2531 N  N    . LYS   B 2 71  ? -33.716 -6.395  13.105  1.00 21.07 ? 457  LYS   B N    1 
ATOM   2532 C  CA   . LYS   B 2 71  ? -33.788 -6.424  14.558  1.00 25.37 ? 457  LYS   B CA   1 
ATOM   2533 C  C    . LYS   B 2 71  ? -32.984 -7.617  15.055  1.00 22.96 ? 457  LYS   B C    1 
ATOM   2534 O  O    . LYS   B 2 71  ? -32.506 -8.441  14.271  1.00 22.43 ? 457  LYS   B O    1 
ATOM   2535 C  CB   . LYS   B 2 71  ? -35.239 -6.501  15.047  1.00 21.39 ? 457  LYS   B CB   1 
ATOM   2536 C  CG   . LYS   B 2 71  ? -35.934 -7.806  14.700  1.00 23.02 ? 457  LYS   B CG   1 
ATOM   2537 C  CD   . LYS   B 2 71  ? -37.369 -7.825  15.200  1.00 26.72 ? 457  LYS   B CD   1 
ATOM   2538 C  CE   . LYS   B 2 71  ? -38.034 -9.158  14.901  1.00 25.85 ? 457  LYS   B CE   1 
ATOM   2539 N  NZ   . LYS   B 2 71  ? -39.450 -9.192  15.360  1.00 27.92 ? 457  LYS   B NZ   1 
ATOM   2540 N  N    . GLY   B 2 72  ? -32.833 -7.701  16.372  1.00 22.86 ? 458  GLY   B N    1 
ATOM   2541 C  CA   . GLY   B 2 72  ? -32.137 -8.804  16.998  1.00 25.31 ? 458  GLY   B CA   1 
ATOM   2542 C  C    . GLY   B 2 72  ? -31.132 -8.330  18.024  1.00 21.15 ? 458  GLY   B C    1 
ATOM   2543 O  O    . GLY   B 2 72  ? -30.984 -7.140  18.294  1.00 19.01 ? 458  GLY   B O    1 
ATOM   2544 N  N    . PHE   B 2 73  ? -30.423 -9.306  18.599  1.00 20.54 ? 459  PHE   B N    1 
ATOM   2545 C  CA   . PHE   B 2 73  ? -29.470 -9.017  19.666  1.00 20.87 ? 459  PHE   B CA   1 
ATOM   2546 C  C    . PHE   B 2 73  ? -28.367 -8.082  19.183  1.00 18.63 ? 459  PHE   B C    1 
ATOM   2547 O  O    . PHE   B 2 73  ? -28.090 -7.053  19.809  1.00 20.57 ? 459  PHE   B O    1 
ATOM   2548 C  CB   . PHE   B 2 73  ? -28.879 -10.324 20.199  1.00 18.40 ? 459  PHE   B CB   1 
ATOM   2549 C  CG   . PHE   B 2 73  ? -27.970 -10.147 21.386  1.00 16.64 ? 459  PHE   B CG   1 
ATOM   2550 C  CD1  . PHE   B 2 73  ? -26.632 -9.824  21.214  1.00 18.23 ? 459  PHE   B CD1  1 
ATOM   2551 C  CD2  . PHE   B 2 73  ? -28.451 -10.318 22.673  1.00 18.13 ? 459  PHE   B CD2  1 
ATOM   2552 C  CE1  . PHE   B 2 73  ? -25.798 -9.662  22.303  1.00 16.83 ? 459  PHE   B CE1  1 
ATOM   2553 C  CE2  . PHE   B 2 73  ? -27.617 -10.162 23.766  1.00 20.91 ? 459  PHE   B CE2  1 
ATOM   2554 C  CZ   . PHE   B 2 73  ? -26.290 -9.833  23.580  1.00 16.87 ? 459  PHE   B CZ   1 
ATOM   2555 N  N    . CYS   B 2 74  ? -27.717 -8.432  18.071  1.00 18.19 ? 460  CYS   B N    1 
ATOM   2556 C  CA   . CYS   B 2 74  ? -26.634 -7.604  17.555  1.00 19.99 ? 460  CYS   B CA   1 
ATOM   2557 C  C    . CYS   B 2 74  ? -27.130 -6.264  17.028  1.00 17.79 ? 460  CYS   B C    1 
ATOM   2558 O  O    . CYS   B 2 74  ? -26.355 -5.302  16.995  1.00 14.20 ? 460  CYS   B O    1 
ATOM   2559 C  CB   . CYS   B 2 74  ? -25.874 -8.355  16.462  1.00 17.44 ? 460  CYS   B CB   1 
ATOM   2560 S  SG   . CYS   B 2 74  ? -24.972 -9.807  17.060  1.00 15.56 ? 460  CYS   B SG   1 
ATOM   2561 N  N    . ILE   B 2 75  ? -28.396 -6.179  16.617  1.00 20.05 ? 461  ILE   B N    1 
ATOM   2562 C  CA   . ILE   B 2 75  ? -28.958 -4.892  16.221  1.00 21.58 ? 461  ILE   B CA   1 
ATOM   2563 C  C    . ILE   B 2 75  ? -29.148 -4.000  17.441  1.00 21.74 ? 461  ILE   B C    1 
ATOM   2564 O  O    . ILE   B 2 75  ? -28.891 -2.791  17.390  1.00 23.93 ? 461  ILE   B O    1 
ATOM   2565 C  CB   . ILE   B 2 75  ? -30.277 -5.100  15.453  1.00 23.03 ? 461  ILE   B CB   1 
ATOM   2566 C  CG1  . ILE   B 2 75  ? -30.038 -5.951  14.204  1.00 23.60 ? 461  ILE   B CG1  1 
ATOM   2567 C  CG2  . ILE   B 2 75  ? -30.904 -3.763  15.084  1.00 18.22 ? 461  ILE   B CG2  1 
ATOM   2568 C  CD1  . ILE   B 2 75  ? -28.967 -5.404  13.286  1.00 22.92 ? 461  ILE   B CD1  1 
ATOM   2569 N  N    . ASP   B 2 76  ? -29.597 -4.580  18.559  1.00 16.02 ? 462  ASP   B N    1 
ATOM   2570 C  CA   . ASP   B 2 76  ? -29.700 -3.816  19.798  1.00 22.36 ? 462  ASP   B CA   1 
ATOM   2571 C  C    . ASP   B 2 76  ? -28.334 -3.335  20.265  1.00 24.46 ? 462  ASP   B C    1 
ATOM   2572 O  O    . ASP   B 2 76  ? -28.221 -2.245  20.839  1.00 23.63 ? 462  ASP   B O    1 
ATOM   2573 C  CB   . ASP   B 2 76  ? -30.363 -4.659  20.888  1.00 26.14 ? 462  ASP   B CB   1 
ATOM   2574 C  CG   . ASP   B 2 76  ? -31.868 -4.738  20.731  1.00 30.13 ? 462  ASP   B CG   1 
ATOM   2575 O  OD1  . ASP   B 2 76  ? -32.401 -4.134  19.778  1.00 22.43 ? 462  ASP   B OD1  1 
ATOM   2576 O  OD2  . ASP   B 2 76  ? -32.522 -5.398  21.566  1.00 34.19 ? 462  ASP   B OD2  1 
ATOM   2577 N  N    . ILE   B 2 77  ? -27.289 -4.133  20.037  1.00 20.51 ? 463  ILE   B N    1 
ATOM   2578 C  CA   . ILE   B 2 77  ? -25.932 -3.690  20.343  1.00 22.34 ? 463  ILE   B CA   1 
ATOM   2579 C  C    . ILE   B 2 77  ? -25.554 -2.508  19.462  1.00 19.66 ? 463  ILE   B C    1 
ATOM   2580 O  O    . ILE   B 2 77  ? -24.963 -1.526  19.930  1.00 19.45 ? 463  ILE   B O    1 
ATOM   2581 C  CB   . ILE   B 2 77  ? -24.941 -4.859  20.183  1.00 17.92 ? 463  ILE   B CB   1 
ATOM   2582 C  CG1  . ILE   B 2 77  ? -25.145 -5.893  21.292  1.00 14.81 ? 463  ILE   B CG1  1 
ATOM   2583 C  CG2  . ILE   B 2 77  ? -23.508 -4.353  20.181  1.00 20.43 ? 463  ILE   B CG2  1 
ATOM   2584 C  CD1  . ILE   B 2 77  ? -24.593 -5.467  22.636  1.00 22.25 ? 463  ILE   B CD1  1 
ATOM   2585 N  N    . LEU   B 2 78  ? -25.901 -2.578  18.174  1.00 20.95 ? 464  LEU   B N    1 
ATOM   2586 C  CA   . LEU   B 2 78  ? -25.620 -1.471  17.265  1.00 23.29 ? 464  LEU   B CA   1 
ATOM   2587 C  C    . LEU   B 2 78  ? -26.395 -0.222  17.662  1.00 21.07 ? 464  LEU   B C    1 
ATOM   2588 O  O    . LEU   B 2 78  ? -25.866 0.894   17.591  1.00 19.72 ? 464  LEU   B O    1 
ATOM   2589 C  CB   . LEU   B 2 78  ? -25.949 -1.878  15.828  1.00 28.80 ? 464  LEU   B CB   1 
ATOM   2590 C  CG   . LEU   B 2 78  ? -25.866 -0.796  14.749  1.00 23.17 ? 464  LEU   B CG   1 
ATOM   2591 C  CD1  . LEU   B 2 78  ? -24.496 -0.135  14.741  1.00 21.92 ? 464  LEU   B CD1  1 
ATOM   2592 C  CD2  . LEU   B 2 78  ? -26.190 -1.379  13.381  1.00 24.45 ? 464  LEU   B CD2  1 
ATOM   2593 N  N    . LYS   B 2 79  ? -27.652 -0.389  18.083  1.00 26.00 ? 465  LYS   B N    1 
ATOM   2594 C  CA   . LYS   B 2 79  ? -28.430 0.753   18.555  1.00 25.59 ? 465  LYS   B CA   1 
ATOM   2595 C  C    . LYS   B 2 79  ? -27.782 1.390   19.778  1.00 24.22 ? 465  LYS   B C    1 
ATOM   2596 O  O    . LYS   B 2 79  ? -27.749 2.620   19.904  1.00 24.07 ? 465  LYS   B O    1 
ATOM   2597 C  CB   . LYS   B 2 79  ? -29.862 0.320   18.872  1.00 21.93 ? 465  LYS   B CB   1 
ATOM   2598 C  CG   . LYS   B 2 79  ? -30.774 0.237   17.660  1.00 26.63 ? 465  LYS   B CG   1 
ATOM   2599 C  CD   . LYS   B 2 79  ? -32.234 0.166   18.076  1.00 25.77 ? 465  LYS   B CD   1 
ATOM   2600 C  CE   . LYS   B 2 79  ? -32.602 -1.227  18.553  1.00 30.89 ? 465  LYS   B CE   1 
ATOM   2601 N  NZ   . LYS   B 2 79  ? -34.030 -1.316  18.970  1.00 35.49 ? 465  LYS   B NZ   1 
ATOM   2602 N  N    . LYS   B 2 80  ? -27.263 0.566   20.690  1.00 23.37 ? 466  LYS   B N    1 
ATOM   2603 C  CA   . LYS   B 2 80  ? -26.562 1.091   21.857  1.00 22.83 ? 466  LYS   B CA   1 
ATOM   2604 C  C    . LYS   B 2 80  ? -25.280 1.804   21.448  1.00 24.78 ? 466  LYS   B C    1 
ATOM   2605 O  O    . LYS   B 2 80  ? -24.989 2.905   21.930  1.00 23.65 ? 466  LYS   B O    1 
ATOM   2606 C  CB   . LYS   B 2 80  ? -26.257 -0.042  22.836  1.00 24.38 ? 466  LYS   B CB   1 
ATOM   2607 C  CG   . LYS   B 2 80  ? -27.417 -0.424  23.739  1.00 26.47 ? 466  LYS   B CG   1 
ATOM   2608 C  CD   . LYS   B 2 80  ? -27.096 -1.680  24.535  1.00 26.40 ? 466  LYS   B CD   1 
ATOM   2609 C  CE   . LYS   B 2 80  ? -27.888 -1.740  25.830  1.00 34.62 ? 466  LYS   B CE   1 
ATOM   2610 N  NZ   . LYS   B 2 80  ? -27.390 -0.758  26.831  1.00 27.08 ? 466  LYS   B NZ   1 
ATOM   2611 N  N    . LEU   B 2 81  ? -24.498 1.186   20.559  1.00 23.06 ? 467  LEU   B N    1 
ATOM   2612 C  CA   . LEU   B 2 81  ? -23.247 1.796   20.119  1.00 28.56 ? 467  LEU   B CA   1 
ATOM   2613 C  C    . LEU   B 2 81  ? -23.497 3.104   19.379  1.00 27.61 ? 467  LEU   B C    1 
ATOM   2614 O  O    . LEU   B 2 81  ? -22.763 4.082   19.566  1.00 24.58 ? 467  LEU   B O    1 
ATOM   2615 C  CB   . LEU   B 2 81  ? -22.472 0.819   19.234  1.00 26.03 ? 467  LEU   B CB   1 
ATOM   2616 C  CG   . LEU   B 2 81  ? -21.901 -0.423  19.921  1.00 23.85 ? 467  LEU   B CG   1 
ATOM   2617 C  CD1  . LEU   B 2 81  ? -21.367 -1.403  18.890  1.00 16.47 ? 467  LEU   B CD1  1 
ATOM   2618 C  CD2  . LEU   B 2 81  ? -20.813 -0.035  20.906  1.00 22.15 ? 467  LEU   B CD2  1 
ATOM   2619 N  N    . SER   B 2 82  ? -24.531 3.141   18.535  1.00 28.18 ? 468  SER   B N    1 
ATOM   2620 C  CA   . SER   B 2 82  ? -24.862 4.371   17.824  1.00 26.06 ? 468  SER   B CA   1 
ATOM   2621 C  C    . SER   B 2 82  ? -25.239 5.484   18.794  1.00 28.88 ? 468  SER   B C    1 
ATOM   2622 O  O    . SER   B 2 82  ? -24.896 6.652   18.576  1.00 24.23 ? 468  SER   B O    1 
ATOM   2623 C  CB   . SER   B 2 82  ? -25.998 4.113   16.835  1.00 22.03 ? 468  SER   B CB   1 
ATOM   2624 O  OG   . SER   B 2 82  ? -26.525 5.329   16.335  1.00 24.81 ? 468  SER   B OG   1 
ATOM   2625 N  N    . ARG   B 2 83  ? -25.943 5.140   19.873  1.00 28.09 ? 469  ARG   B N    1 
ATOM   2626 C  CA   . ARG   B 2 83  ? -26.338 6.145   20.853  1.00 26.45 ? 469  ARG   B CA   1 
ATOM   2627 C  C    . ARG   B 2 83  ? -25.149 6.599   21.693  1.00 30.73 ? 469  ARG   B C    1 
ATOM   2628 O  O    . ARG   B 2 83  ? -24.991 7.796   21.959  1.00 29.16 ? 469  ARG   B O    1 
ATOM   2629 C  CB   . ARG   B 2 83  ? -27.451 5.588   21.742  1.00 31.22 ? 469  ARG   B CB   1 
ATOM   2630 C  CG   . ARG   B 2 83  ? -27.480 6.149   23.154  1.00 41.58 ? 469  ARG   B CG   1 
ATOM   2631 C  CD   . ARG   B 2 83  ? -28.818 6.797   23.458  1.00 50.05 ? 469  ARG   B CD   1 
ATOM   2632 N  NE   . ARG   B 2 83  ? -28.740 7.714   24.588  1.00 62.29 ? 469  ARG   B NE   1 
ATOM   2633 C  CZ   . ARG   B 2 83  ? -29.627 8.666   24.842  1.00 61.94 ? 469  ARG   B CZ   1 
ATOM   2634 N  NH1  . ARG   B 2 83  ? -30.676 8.859   24.060  1.00 62.60 ? 469  ARG   B NH1  1 
ATOM   2635 N  NH2  . ARG   B 2 83  ? -29.459 9.441   25.910  1.00 68.77 ? 469  ARG   B NH2  1 
ATOM   2636 N  N    . THR   B 2 84  ? -24.295 5.660   22.106  1.00 25.18 ? 470  THR   B N    1 
ATOM   2637 C  CA   . THR   B 2 84  ? -23.192 5.985   23.005  1.00 31.53 ? 470  THR   B CA   1 
ATOM   2638 C  C    . THR   B 2 84  ? -22.038 6.649   22.259  1.00 29.99 ? 470  THR   B C    1 
ATOM   2639 O  O    . THR   B 2 84  ? -21.642 7.774   22.582  1.00 31.56 ? 470  THR   B O    1 
ATOM   2640 C  CB   . THR   B 2 84  ? -22.712 4.719   23.722  1.00 30.52 ? 470  THR   B CB   1 
ATOM   2641 O  OG1  . THR   B 2 84  ? -23.730 4.266   24.623  1.00 33.05 ? 470  THR   B OG1  1 
ATOM   2642 C  CG2  . THR   B 2 84  ? -21.438 4.999   24.505  1.00 31.12 ? 470  THR   B CG2  1 
ATOM   2643 N  N    . VAL   B 2 85  ? -21.484 5.961   21.257  1.00 26.94 ? 471  VAL   B N    1 
ATOM   2644 C  CA   . VAL   B 2 85  ? -20.392 6.519   20.465  1.00 29.96 ? 471  VAL   B CA   1 
ATOM   2645 C  C    . VAL   B 2 85  ? -20.836 7.704   19.621  1.00 30.93 ? 471  VAL   B C    1 
ATOM   2646 O  O    . VAL   B 2 85  ? -19.988 8.429   19.087  1.00 29.38 ? 471  VAL   B O    1 
ATOM   2647 C  CB   . VAL   B 2 85  ? -19.774 5.413   19.582  1.00 25.96 ? 471  VAL   B CB   1 
ATOM   2648 C  CG1  . VAL   B 2 85  ? -18.427 5.845   19.016  1.00 23.23 ? 471  VAL   B CG1  1 
ATOM   2649 C  CG2  . VAL   B 2 85  ? -19.624 4.127   20.378  1.00 31.78 ? 471  VAL   B CG2  1 
ATOM   2650 N  N    . LYS   B 2 86  ? -22.148 7.922   19.498  1.00 29.14 ? 472  LYS   B N    1 
ATOM   2651 C  CA   . LYS   B 2 86  ? -22.716 9.054   18.773  1.00 35.76 ? 472  LYS   B CA   1 
ATOM   2652 C  C    . LYS   B 2 86  ? -22.354 9.014   17.293  1.00 34.45 ? 472  LYS   B C    1 
ATOM   2653 O  O    . LYS   B 2 86  ? -21.433 9.710   16.851  1.00 36.60 ? 472  LYS   B O    1 
ATOM   2654 C  CB   . LYS   B 2 86  ? -22.268 10.379  19.398  1.00 27.89 ? 472  LYS   B CB   1 
ATOM   2655 C  CG   . LYS   B 2 86  ? -22.786 10.606  20.809  1.00 33.21 ? 472  LYS   B CG   1 
ATOM   2656 C  CD   . LYS   B 2 86  ? -22.782 12.085  21.164  1.00 37.24 ? 472  LYS   B CD   1 
ATOM   2657 C  CE   . LYS   B 2 86  ? -21.385 12.565  21.517  1.00 40.55 ? 472  LYS   B CE   1 
ATOM   2658 N  NZ   . LYS   B 2 86  ? -20.939 12.042  22.838  1.00 38.80 ? 472  LYS   B NZ   1 
ATOM   2659 N  N    . PHE   B 2 87  ? -23.074 8.201   16.524  1.00 31.49 ? 473  PHE   B N    1 
ATOM   2660 C  CA   . PHE   B 2 87  ? -22.929 8.183   15.076  1.00 29.68 ? 473  PHE   B CA   1 
ATOM   2661 C  C    . PHE   B 2 87  ? -24.218 7.654   14.465  1.00 29.58 ? 473  PHE   B C    1 
ATOM   2662 O  O    . PHE   B 2 87  ? -24.942 6.874   15.089  1.00 28.59 ? 473  PHE   B O    1 
ATOM   2663 C  CB   . PHE   B 2 87  ? -21.730 7.333   14.625  1.00 27.82 ? 473  PHE   B CB   1 
ATOM   2664 C  CG   . PHE   B 2 87  ? -21.822 5.878   15.011  1.00 27.61 ? 473  PHE   B CG   1 
ATOM   2665 C  CD1  . PHE   B 2 87  ? -22.482 4.967   14.199  1.00 24.63 ? 473  PHE   B CD1  1 
ATOM   2666 C  CD2  . PHE   B 2 87  ? -21.229 5.418   16.175  1.00 28.03 ? 473  PHE   B CD2  1 
ATOM   2667 C  CE1  . PHE   B 2 87  ? -22.562 3.631   14.549  1.00 24.39 ? 473  PHE   B CE1  1 
ATOM   2668 C  CE2  . PHE   B 2 87  ? -21.304 4.082   16.530  1.00 27.29 ? 473  PHE   B CE2  1 
ATOM   2669 C  CZ   . PHE   B 2 87  ? -21.971 3.189   15.716  1.00 25.93 ? 473  PHE   B CZ   1 
ATOM   2670 N  N    . THR   B 2 88  ? -24.498 8.098   13.246  1.00 31.59 ? 474  THR   B N    1 
ATOM   2671 C  CA   . THR   B 2 88  ? -25.592 7.569   12.448  1.00 26.09 ? 474  THR   B CA   1 
ATOM   2672 C  C    . THR   B 2 88  ? -25.038 6.593   11.417  1.00 31.29 ? 474  THR   B C    1 
ATOM   2673 O  O    . THR   B 2 88  ? -23.836 6.565   11.142  1.00 31.29 ? 474  THR   B O    1 
ATOM   2674 C  CB   . THR   B 2 88  ? -26.364 8.696   11.759  1.00 29.02 ? 474  THR   B CB   1 
ATOM   2675 O  OG1  . THR   B 2 88  ? -25.502 9.379   10.841  1.00 29.92 ? 474  THR   B OG1  1 
ATOM   2676 C  CG2  . THR   B 2 88  ? -26.883 9.689   12.790  1.00 29.43 ? 474  THR   B CG2  1 
ATOM   2677 N  N    . TYR   B 2 89  ? -25.926 5.781   10.848  1.00 28.47 ? 475  TYR   B N    1 
ATOM   2678 C  CA   . TYR   B 2 89  ? -25.466 4.705   9.983   1.00 26.57 ? 475  TYR   B CA   1 
ATOM   2679 C  C    . TYR   B 2 89  ? -26.496 4.389   8.909   1.00 29.59 ? 475  TYR   B C    1 
ATOM   2680 O  O    . TYR   B 2 89  ? -27.699 4.589   9.095   1.00 28.44 ? 475  TYR   B O    1 
ATOM   2681 C  CB   . TYR   B 2 89  ? -25.153 3.439   10.792  1.00 25.87 ? 475  TYR   B CB   1 
ATOM   2682 C  CG   . TYR   B 2 89  ? -26.310 2.933   11.626  1.00 23.07 ? 475  TYR   B CG   1 
ATOM   2683 C  CD1  . TYR   B 2 89  ? -27.232 2.034   11.102  1.00 21.89 ? 475  TYR   B CD1  1 
ATOM   2684 C  CD2  . TYR   B 2 89  ? -26.478 3.352   12.939  1.00 20.52 ? 475  TYR   B CD2  1 
ATOM   2685 C  CE1  . TYR   B 2 89  ? -28.288 1.570   11.862  1.00 19.45 ? 475  TYR   B CE1  1 
ATOM   2686 C  CE2  . TYR   B 2 89  ? -27.533 2.893   13.706  1.00 20.64 ? 475  TYR   B CE2  1 
ATOM   2687 C  CZ   . TYR   B 2 89  ? -28.434 2.003   13.163  1.00 20.18 ? 475  TYR   B CZ   1 
ATOM   2688 O  OH   . TYR   B 2 89  ? -29.484 1.545   13.925  1.00 18.31 ? 475  TYR   B OH   1 
ATOM   2689 N  N    . ASP   B 2 90  ? -25.998 3.891   7.778   1.00 26.68 ? 476  ASP   B N    1 
ATOM   2690 C  CA   . ASP   B 2 90  ? -26.811 3.290   6.724   1.00 28.61 ? 476  ASP   B CA   1 
ATOM   2691 C  C    . ASP   B 2 90  ? -26.503 1.797   6.730   1.00 22.77 ? 476  ASP   B C    1 
ATOM   2692 O  O    . ASP   B 2 90  ? -25.452 1.369   6.246   1.00 23.49 ? 476  ASP   B O    1 
ATOM   2693 C  CB   . ASP   B 2 90  ? -26.519 3.919   5.365   1.00 32.81 ? 476  ASP   B CB   1 
ATOM   2694 C  CG   . ASP   B 2 90  ? -27.302 5.197   5.132   1.00 50.50 ? 476  ASP   B CG   1 
ATOM   2695 O  OD1  . ASP   B 2 90  ? -26.875 6.013   4.289   1.00 48.57 ? 476  ASP   B OD1  1 
ATOM   2696 O  OD2  . ASP   B 2 90  ? -28.344 5.385   5.793   1.00 50.83 ? 476  ASP   B OD2  1 
ATOM   2697 N  N    . LEU   B 2 91  ? -27.417 1.010   7.289   1.00 22.07 ? 477  LEU   B N    1 
ATOM   2698 C  CA   . LEU   B 2 91  ? -27.220 -0.426  7.422   1.00 21.07 ? 477  LEU   B CA   1 
ATOM   2699 C  C    . LEU   B 2 91  ? -27.679 -1.140  6.157   1.00 21.44 ? 477  LEU   B C    1 
ATOM   2700 O  O    . LEU   B 2 91  ? -28.725 -0.814  5.589   1.00 23.39 ? 477  LEU   B O    1 
ATOM   2701 C  CB   . LEU   B 2 91  ? -27.980 -0.959  8.638   1.00 18.91 ? 477  LEU   B CB   1 
ATOM   2702 C  CG   . LEU   B 2 91  ? -27.762 -2.419  9.044   1.00 21.70 ? 477  LEU   B CG   1 
ATOM   2703 C  CD1  . LEU   B 2 91  ? -26.314 -2.658  9.436   1.00 18.96 ? 477  LEU   B CD1  1 
ATOM   2704 C  CD2  . LEU   B 2 91  ? -28.694 -2.798  10.187  1.00 21.74 ? 477  LEU   B CD2  1 
ATOM   2705 N  N    . TYR   B 2 92  ? -26.884 -2.113  5.717   1.00 22.24 ? 478  TYR   B N    1 
ATOM   2706 C  CA   . TYR   B 2 92  ? -27.225 -2.893  4.537   1.00 19.96 ? 478  TYR   B CA   1 
ATOM   2707 C  C    . TYR   B 2 92  ? -26.758 -4.327  4.736   1.00 22.91 ? 478  TYR   B C    1 
ATOM   2708 O  O    . TYR   B 2 92  ? -25.839 -4.603  5.511   1.00 24.17 ? 478  TYR   B O    1 
ATOM   2709 C  CB   . TYR   B 2 92  ? -26.615 -2.289  3.265   1.00 20.18 ? 478  TYR   B CB   1 
ATOM   2710 C  CG   . TYR   B 2 92  ? -25.130 -2.519  3.114   1.00 19.60 ? 478  TYR   B CG   1 
ATOM   2711 C  CD1  . TYR   B 2 92  ? -24.212 -1.764  3.833   1.00 18.22 ? 478  TYR   B CD1  1 
ATOM   2712 C  CD2  . TYR   B 2 92  ? -24.646 -3.485  2.244   1.00 23.44 ? 478  TYR   B CD2  1 
ATOM   2713 C  CE1  . TYR   B 2 92  ? -22.853 -1.971  3.693   1.00 20.26 ? 478  TYR   B CE1  1 
ATOM   2714 C  CE2  . TYR   B 2 92  ? -23.289 -3.700  2.098   1.00 23.11 ? 478  TYR   B CE2  1 
ATOM   2715 C  CZ   . TYR   B 2 92  ? -22.397 -2.941  2.823   1.00 20.50 ? 478  TYR   B CZ   1 
ATOM   2716 O  OH   . TYR   B 2 92  ? -21.046 -3.154  2.678   1.00 16.53 ? 478  TYR   B OH   1 
ATOM   2717 N  N    . LEU   B 2 93  ? -27.411 -5.241  4.025   1.00 19.65 ? 479  LEU   B N    1 
ATOM   2718 C  CA   . LEU   B 2 93  ? -27.153 -6.669  4.151   1.00 23.11 ? 479  LEU   B CA   1 
ATOM   2719 C  C    . LEU   B 2 93  ? -26.177 -7.114  3.071   1.00 18.84 ? 479  LEU   B C    1 
ATOM   2720 O  O    . LEU   B 2 93  ? -26.321 -6.737  1.904   1.00 21.40 ? 479  LEU   B O    1 
ATOM   2721 C  CB   . LEU   B 2 93  ? -28.456 -7.464  4.052   1.00 19.74 ? 479  LEU   B CB   1 
ATOM   2722 C  CG   . LEU   B 2 93  ? -29.453 -7.227  5.187   1.00 19.91 ? 479  LEU   B CG   1 
ATOM   2723 C  CD1  . LEU   B 2 93  ? -30.882 -7.324  4.680   1.00 24.36 ? 479  LEU   B CD1  1 
ATOM   2724 C  CD2  . LEU   B 2 93  ? -29.216 -8.211  6.321   1.00 15.29 ? 479  LEU   B CD2  1 
ATOM   2725 N  N    . VAL   B 2 94  ? -25.185 -7.914  3.466   1.00 16.09 ? 480  VAL   B N    1 
ATOM   2726 C  CA   . VAL   B 2 94  ? -24.183 -8.385  2.519   1.00 16.51 ? 480  VAL   B CA   1 
ATOM   2727 C  C    . VAL   B 2 94  ? -24.826 -9.336  1.517   1.00 22.20 ? 480  VAL   B C    1 
ATOM   2728 O  O    . VAL   B 2 94  ? -25.665 -10.177 1.872   1.00 15.26 ? 480  VAL   B O    1 
ATOM   2729 C  CB   . VAL   B 2 94  ? -23.010 -9.050  3.264   1.00 17.34 ? 480  VAL   B CB   1 
ATOM   2730 C  CG1  . VAL   B 2 94  ? -23.470 -10.294 4.014   1.00 20.64 ? 480  VAL   B CG1  1 
ATOM   2731 C  CG2  . VAL   B 2 94  ? -21.882 -9.388  2.297   1.00 19.03 ? 480  VAL   B CG2  1 
ATOM   2732 N  N    . THR   B 2 95  ? -24.453 -9.185  0.246   1.00 19.85 ? 481  THR   B N    1 
ATOM   2733 C  CA   . THR   B 2 95  ? -24.920 -10.061 -0.815  1.00 18.01 ? 481  THR   B CA   1 
ATOM   2734 C  C    . THR   B 2 95  ? -23.800 -10.848 -1.479  1.00 22.34 ? 481  THR   B C    1 
ATOM   2735 O  O    . THR   B 2 95  ? -24.089 -11.810 -2.199  1.00 25.33 ? 481  THR   B O    1 
ATOM   2736 C  CB   . THR   B 2 95  ? -25.668 -9.256  -1.890  1.00 19.58 ? 481  THR   B CB   1 
ATOM   2737 O  OG1  . THR   B 2 95  ? -24.826 -8.200  -2.368  1.00 18.86 ? 481  THR   B OG1  1 
ATOM   2738 C  CG2  . THR   B 2 95  ? -26.942 -8.655  -1.316  1.00 18.07 ? 481  THR   B CG2  1 
ATOM   2739 N  N    . ASN   B 2 96  ? -22.541 -10.472 -1.259  1.00 22.13 ? 482  ASN   B N    1 
ATOM   2740 C  CA   . ASN   B 2 96  ? -21.395 -11.171 -1.835  1.00 19.99 ? 482  ASN   B CA   1 
ATOM   2741 C  C    . ASN   B 2 96  ? -20.836 -12.114 -0.773  1.00 18.01 ? 482  ASN   B C    1 
ATOM   2742 O  O    . ASN   B 2 96  ? -19.887 -11.803 -0.055  1.00 17.78 ? 482  ASN   B O    1 
ATOM   2743 C  CB   . ASN   B 2 96  ? -20.349 -10.172 -2.320  1.00 16.68 ? 482  ASN   B CB   1 
ATOM   2744 C  CG   . ASN   B 2 96  ? -19.092 -10.845 -2.827  1.00 16.39 ? 482  ASN   B CG   1 
ATOM   2745 O  OD1  . ASN   B 2 96  ? -19.156 -11.806 -3.593  1.00 23.93 ? 482  ASN   B OD1  1 
ATOM   2746 N  ND2  . ASN   B 2 96  ? -17.939 -10.347 -2.396  1.00 17.15 ? 482  ASN   B ND2  1 
ATOM   2747 N  N    . GLY   B 2 97  ? -21.447 -13.288 -0.677  1.00 16.64 ? 483  GLY   B N    1 
ATOM   2748 C  CA   . GLY   B 2 97  ? -21.065 -14.250 0.336   1.00 15.20 ? 483  GLY   B CA   1 
ATOM   2749 C  C    . GLY   B 2 97  ? -21.859 -14.075 1.616   1.00 15.78 ? 483  GLY   B C    1 
ATOM   2750 O  O    . GLY   B 2 97  ? -22.928 -13.457 1.650   1.00 17.30 ? 483  GLY   B O    1 
ATOM   2751 N  N    . LYS   B 2 98  ? -21.312 -14.630 2.695   1.00 16.49 ? 484  LYS   B N    1 
ATOM   2752 C  CA   . LYS   B 2 98  ? -22.004 -14.604 3.977   1.00 16.64 ? 484  LYS   B CA   1 
ATOM   2753 C  C    . LYS   B 2 98  ? -21.167 -13.916 5.047   1.00 16.13 ? 484  LYS   B C    1 
ATOM   2754 O  O    . LYS   B 2 98  ? -21.002 -12.692 5.023   1.00 23.35 ? 484  LYS   B O    1 
ATOM   2755 C  CB   . LYS   B 2 98  ? -22.365 -16.026 4.410   1.00 18.66 ? 484  LYS   B CB   1 
ATOM   2756 C  CG   . LYS   B 2 98  ? -23.279 -16.740 3.429   1.00 18.89 ? 484  LYS   B CG   1 
ATOM   2757 C  CD   . LYS   B 2 98  ? -24.505 -17.312 4.119   1.00 31.74 ? 484  LYS   B CD   1 
ATOM   2758 C  CE   . LYS   B 2 98  ? -24.128 -18.414 5.093   1.00 37.18 ? 484  LYS   B CE   1 
ATOM   2759 N  NZ   . LYS   B 2 98  ? -25.329 -19.105 5.638   1.00 39.44 ? 484  LYS   B NZ   1 
ATOM   2760 N  N    . HIS   B 2 99  ? -20.639 -14.693 5.994   1.00 15.42 ? 485  HIS   B N    1 
ATOM   2761 C  CA   . HIS   B 2 99  ? -19.862 -14.107 7.082   1.00 13.13 ? 485  HIS   B CA   1 
ATOM   2762 C  C    . HIS   B 2 99  ? -18.510 -13.609 6.584   1.00 18.43 ? 485  HIS   B C    1 
ATOM   2763 O  O    . HIS   B 2 99  ? -18.145 -12.449 6.807   1.00 15.34 ? 485  HIS   B O    1 
ATOM   2764 C  CB   . HIS   B 2 99  ? -19.684 -15.127 8.206   1.00 13.36 ? 485  HIS   B CB   1 
ATOM   2765 C  CG   . HIS   B 2 99  ? -20.974 -15.623 8.783   1.00 15.88 ? 485  HIS   B CG   1 
ATOM   2766 N  ND1  . HIS   B 2 99  ? -21.780 -16.533 8.132   1.00 15.44 ? 485  HIS   B ND1  1 
ATOM   2767 C  CD2  . HIS   B 2 99  ? -21.598 -15.335 9.950   1.00 14.21 ? 485  HIS   B CD2  1 
ATOM   2768 C  CE1  . HIS   B 2 99  ? -22.844 -16.785 8.874   1.00 13.43 ? 485  HIS   B CE1  1 
ATOM   2769 N  NE2  . HIS   B 2 99  ? -22.758 -16.071 9.982   1.00 12.87 ? 485  HIS   B NE2  1 
ATOM   2770 N  N    . GLY   B 2 100 ? -17.755 -14.470 5.908   1.00 18.57 ? 486  GLY   B N    1 
ATOM   2771 C  CA   . GLY   B 2 100 ? -16.464 -14.082 5.374   1.00 11.64 ? 486  GLY   B CA   1 
ATOM   2772 C  C    . GLY   B 2 100 ? -15.540 -15.251 5.108   1.00 17.76 ? 486  GLY   B C    1 
ATOM   2773 O  O    . GLY   B 2 100 ? -15.220 -16.020 6.020   1.00 18.99 ? 486  GLY   B O    1 
ATOM   2774 N  N    . LYS   B 2 101 ? -15.107 -15.397 3.858   1.00 17.64 ? 487  LYS   B N    1 
ATOM   2775 C  CA   . LYS   B 2 101 ? -14.180 -16.449 3.470   1.00 19.50 ? 487  LYS   B CA   1 
ATOM   2776 C  C    . LYS   B 2 101 ? -13.171 -15.883 2.484   1.00 23.47 ? 487  LYS   B C    1 
ATOM   2777 O  O    . LYS   B 2 101 ? -13.526 -15.093 1.605   1.00 22.39 ? 487  LYS   B O    1 
ATOM   2778 C  CB   . LYS   B 2 101 ? -14.910 -17.645 2.843   1.00 19.64 ? 487  LYS   B CB   1 
ATOM   2779 C  CG   . LYS   B 2 101 ? -13.990 -18.795 2.460   1.00 19.43 ? 487  LYS   B CG   1 
ATOM   2780 C  CD   . LYS   B 2 101 ? -14.734 -19.878 1.698   1.00 20.88 ? 487  LYS   B CD   1 
ATOM   2781 C  CE   . LYS   B 2 101 ? -13.797 -21.010 1.306   1.00 22.87 ? 487  LYS   B CE   1 
ATOM   2782 N  NZ   . LYS   B 2 101 ? -14.488 -22.056 0.503   1.00 17.08 ? 487  LYS   B NZ   1 
ATOM   2783 N  N    . LYS   B 2 102 ? -11.911 -16.284 2.639   1.00 22.68 ? 488  LYS   B N    1 
ATOM   2784 C  CA   . LYS   B 2 102 ? -10.846 -15.869 1.733   1.00 20.94 ? 488  LYS   B CA   1 
ATOM   2785 C  C    . LYS   B 2 102 ? -10.797 -16.847 0.564   1.00 21.94 ? 488  LYS   B C    1 
ATOM   2786 O  O    . LYS   B 2 102 ? -10.448 -18.019 0.738   1.00 23.53 ? 488  LYS   B O    1 
ATOM   2787 C  CB   . LYS   B 2 102 ? -9.504  -15.809 2.459   1.00 22.96 ? 488  LYS   B CB   1 
ATOM   2788 C  CG   . LYS   B 2 102 ? -8.398  -15.153 1.646   1.00 28.20 ? 488  LYS   B CG   1 
ATOM   2789 C  CD   . LYS   B 2 102 ? -7.203  -14.785 2.511   1.00 25.95 ? 488  LYS   B CD   1 
ATOM   2790 C  CE   . LYS   B 2 102 ? -6.434  -16.020 2.948   1.00 29.36 ? 488  LYS   B CE   1 
ATOM   2791 N  NZ   . LYS   B 2 102 ? -5.165  -15.662 3.641   1.00 46.35 ? 488  LYS   B NZ   1 
ATOM   2792 N  N    . VAL   B 2 103 ? -11.154 -16.367 -0.624  1.00 24.04 ? 489  VAL   B N    1 
ATOM   2793 C  CA   . VAL   B 2 103 ? -11.146 -17.168 -1.843  1.00 23.52 ? 489  VAL   B CA   1 
ATOM   2794 C  C    . VAL   B 2 103 ? -10.109 -16.574 -2.783  1.00 27.42 ? 489  VAL   B C    1 
ATOM   2795 O  O    . VAL   B 2 103 ? -10.246 -15.423 -3.216  1.00 25.82 ? 489  VAL   B O    1 
ATOM   2796 C  CB   . VAL   B 2 103 ? -12.529 -17.211 -2.511  1.00 20.68 ? 489  VAL   B CB   1 
ATOM   2797 C  CG1  . VAL   B 2 103 ? -12.520 -18.183 -3.683  1.00 19.58 ? 489  VAL   B CG1  1 
ATOM   2798 C  CG2  . VAL   B 2 103 ? -13.599 -17.592 -1.498  1.00 20.22 ? 489  VAL   B CG2  1 
ATOM   2799 N  N    . ASN   B 2 104 ? -9.077  -17.359 -3.098  1.00 23.75 ? 490  ASN   B N    1 
ATOM   2800 C  CA   . ASN   B 2 104 ? -7.986  -16.919 -3.967  1.00 25.53 ? 490  ASN   B CA   1 
ATOM   2801 C  C    . ASN   B 2 104 ? -7.358  -15.629 -3.446  1.00 32.17 ? 490  ASN   B C    1 
ATOM   2802 O  O    . ASN   B 2 104 ? -7.110  -14.683 -4.198  1.00 27.03 ? 490  ASN   B O    1 
ATOM   2803 C  CB   . ASN   B 2 104 ? -8.464  -16.755 -5.410  1.00 22.21 ? 490  ASN   B CB   1 
ATOM   2804 C  CG   . ASN   B 2 104 ? -8.930  -18.063 -6.019  1.00 25.22 ? 490  ASN   B CG   1 
ATOM   2805 O  OD1  . ASN   B 2 104 ? -8.223  -19.069 -5.974  1.00 20.79 ? 490  ASN   B OD1  1 
ATOM   2806 N  ND2  . ASN   B 2 104 ? -10.129 -18.055 -6.589  1.00 21.95 ? 490  ASN   B ND2  1 
ATOM   2807 N  N    . ASN   B 2 105 ? -7.109  -15.595 -2.136  1.00 31.39 ? 491  ASN   B N    1 
ATOM   2808 C  CA   . ASN   B 2 105 ? -6.528  -14.446 -1.441  1.00 30.77 ? 491  ASN   B CA   1 
ATOM   2809 C  C    . ASN   B 2 105 ? -7.424  -13.213 -1.506  1.00 26.01 ? 491  ASN   B C    1 
ATOM   2810 O  O    . ASN   B 2 105 ? -6.947  -12.086 -1.339  1.00 33.79 ? 491  ASN   B O    1 
ATOM   2811 C  CB   . ASN   B 2 105 ? -5.130  -14.115 -1.981  1.00 28.37 ? 491  ASN   B CB   1 
ATOM   2812 C  CG   . ASN   B 2 105 ? -4.171  -13.688 -0.890  1.00 32.18 ? 491  ASN   B CG   1 
ATOM   2813 O  OD1  . ASN   B 2 105 ? -4.445  -13.866 0.297   1.00 37.17 ? 491  ASN   B OD1  1 
ATOM   2814 N  ND2  . ASN   B 2 105 ? -3.038  -13.121 -1.287  1.00 35.51 ? 491  ASN   B ND2  1 
ATOM   2815 N  N    . VAL   B 2 106 ? -8.722  -13.404 -1.736  1.00 27.35 ? 492  VAL   B N    1 
ATOM   2816 C  CA   . VAL   B 2 106 ? -9.691  -12.314 -1.804  1.00 27.33 ? 492  VAL   B CA   1 
ATOM   2817 C  C    . VAL   B 2 106 ? -10.816 -12.620 -0.825  1.00 28.17 ? 492  VAL   B C    1 
ATOM   2818 O  O    . VAL   B 2 106 ? -11.435 -13.688 -0.899  1.00 20.73 ? 492  VAL   B O    1 
ATOM   2819 C  CB   . VAL   B 2 106 ? -10.243 -12.118 -3.226  1.00 29.69 ? 492  VAL   B CB   1 
ATOM   2820 C  CG1  . VAL   B 2 106 ? -11.336 -11.062 -3.231  1.00 20.53 ? 492  VAL   B CG1  1 
ATOM   2821 C  CG2  . VAL   B 2 106 ? -9.122  -11.732 -4.182  1.00 33.06 ? 492  VAL   B CG2  1 
ATOM   2822 N  N    . TRP   B 2 107 ? -11.082 -11.686 0.085   1.00 26.88 ? 493  TRP   B N    1 
ATOM   2823 C  CA   . TRP   B 2 107 ? -12.081 -11.875 1.129   1.00 22.68 ? 493  TRP   B CA   1 
ATOM   2824 C  C    . TRP   B 2 107 ? -13.464 -11.493 0.615   1.00 24.15 ? 493  TRP   B C    1 
ATOM   2825 O  O    . TRP   B 2 107 ? -13.638 -10.426 0.017   1.00 24.37 ? 493  TRP   B O    1 
ATOM   2826 C  CB   . TRP   B 2 107 ? -11.731 -11.037 2.359   1.00 17.64 ? 493  TRP   B CB   1 
ATOM   2827 C  CG   . TRP   B 2 107 ? -10.752 -11.693 3.282   1.00 24.78 ? 493  TRP   B CG   1 
ATOM   2828 C  CD1  . TRP   B 2 107 ? -9.421  -11.415 3.397   1.00 21.17 ? 493  TRP   B CD1  1 
ATOM   2829 C  CD2  . TRP   B 2 107 ? -11.029 -12.732 4.228   1.00 17.84 ? 493  TRP   B CD2  1 
ATOM   2830 N  NE1  . TRP   B 2 107 ? -8.851  -12.219 4.353   1.00 22.23 ? 493  TRP   B NE1  1 
ATOM   2831 C  CE2  . TRP   B 2 107 ? -9.817  -13.037 4.879   1.00 16.14 ? 493  TRP   B CE2  1 
ATOM   2832 C  CE3  . TRP   B 2 107 ? -12.183 -13.434 4.587   1.00 17.59 ? 493  TRP   B CE3  1 
ATOM   2833 C  CZ2  . TRP   B 2 107 ? -9.727  -14.014 5.868   1.00 21.22 ? 493  TRP   B CZ2  1 
ATOM   2834 C  CZ3  . TRP   B 2 107 ? -12.091 -14.403 5.569   1.00 18.02 ? 493  TRP   B CZ3  1 
ATOM   2835 C  CH2  . TRP   B 2 107 ? -10.872 -14.684 6.197   1.00 25.65 ? 493  TRP   B CH2  1 
ATOM   2836 N  N    . ASN   B 2 108 ? -14.445 -12.362 0.853   1.00 18.49 ? 494  ASN   B N    1 
ATOM   2837 C  CA   . ASN   B 2 108 ? -15.837 -12.067 0.555   1.00 19.24 ? 494  ASN   B CA   1 
ATOM   2838 C  C    . ASN   B 2 108 ? -16.607 -11.862 1.860   1.00 18.08 ? 494  ASN   B C    1 
ATOM   2839 O  O    . ASN   B 2 108 ? -16.018 -11.714 2.938   1.00 16.53 ? 494  ASN   B O    1 
ATOM   2840 C  CB   . ASN   B 2 108 ? -16.448 -13.172 -0.323  1.00 16.40 ? 494  ASN   B CB   1 
ATOM   2841 C  CG   . ASN   B 2 108 ? -16.567 -14.522 0.390   1.00 20.09 ? 494  ASN   B CG   1 
ATOM   2842 O  OD1  . ASN   B 2 108 ? -16.557 -14.612 1.617   1.00 17.93 ? 494  ASN   B OD1  1 
ATOM   2843 N  ND2  . ASN   B 2 108 ? -16.696 -15.583 -0.399  1.00 20.03 ? 494  ASN   B ND2  1 
ATOM   2844 N  N    . GLY   B 2 109 ? -17.934 -11.859 1.760   1.00 14.37 ? 495  GLY   B N    1 
ATOM   2845 C  CA   . GLY   B 2 109 ? -18.762 -11.755 2.944   1.00 16.17 ? 495  GLY   B CA   1 
ATOM   2846 C  C    . GLY   B 2 109 ? -18.638 -10.409 3.640   1.00 16.64 ? 495  GLY   B C    1 
ATOM   2847 O  O    . GLY   B 2 109 ? -18.264 -9.391  3.050   1.00 13.68 ? 495  GLY   B O    1 
ATOM   2848 N  N    . MET   B 2 110 ? -18.964 -10.422 4.936   1.00 16.86 ? 496  MET   B N    1 
ATOM   2849 C  CA   . MET   B 2 110 ? -18.911 -9.196  5.727   1.00 16.36 ? 496  MET   B CA   1 
ATOM   2850 C  C    . MET   B 2 110 ? -17.480 -8.694  5.880   1.00 17.45 ? 496  MET   B C    1 
ATOM   2851 O  O    . MET   B 2 110 ? -17.235 -7.481  5.856   1.00 18.48 ? 496  MET   B O    1 
ATOM   2852 C  CB   . MET   B 2 110 ? -19.549 -9.426  7.097   1.00 13.77 ? 496  MET   B CB   1 
ATOM   2853 C  CG   . MET   B 2 110 ? -21.060 -9.586  7.058   1.00 14.00 ? 496  MET   B CG   1 
ATOM   2854 S  SD   . MET   B 2 110 ? -21.830 -9.430  8.683   1.00 17.01 ? 496  MET   B SD   1 
ATOM   2855 C  CE   . MET   B 2 110 ? -21.641 -11.094 9.320   1.00 10.91 ? 496  MET   B CE   1 
ATOM   2856 N  N    . ILE   B 2 111 ? -16.523 -9.611  6.046   1.00 14.12 ? 497  ILE   B N    1 
ATOM   2857 C  CA   . ILE   B 2 111 ? -15.119 -9.214  6.133   1.00 17.06 ? 497  ILE   B CA   1 
ATOM   2858 C  C    . ILE   B 2 111 ? -14.690 -8.511  4.853   1.00 21.06 ? 497  ILE   B C    1 
ATOM   2859 O  O    . ILE   B 2 111 ? -14.037 -7.462  4.887   1.00 21.67 ? 497  ILE   B O    1 
ATOM   2860 C  CB   . ILE   B 2 111 ? -14.228 -10.436 6.429   1.00 20.08 ? 497  ILE   B CB   1 
ATOM   2861 C  CG1  . ILE   B 2 111 ? -14.310 -10.821 7.905   1.00 14.16 ? 497  ILE   B CG1  1 
ATOM   2862 C  CG2  . ILE   B 2 111 ? -12.784 -10.162 6.034   1.00 17.35 ? 497  ILE   B CG2  1 
ATOM   2863 C  CD1  . ILE   B 2 111 ? -15.261 -11.955 8.169   1.00 21.98 ? 497  ILE   B CD1  1 
ATOM   2864 N  N    . GLY   B 2 112 ? -15.060 -9.079  3.702   1.00 21.46 ? 498  GLY   B N    1 
ATOM   2865 C  CA   . GLY   B 2 112 ? -14.718 -8.451  2.437   1.00 20.92 ? 498  GLY   B CA   1 
ATOM   2866 C  C    . GLY   B 2 112 ? -15.287 -7.052  2.307   1.00 23.51 ? 498  GLY   B C    1 
ATOM   2867 O  O    . GLY   B 2 112 ? -14.619 -6.144  1.807   1.00 21.79 ? 498  GLY   B O    1 
ATOM   2868 N  N    . GLU   B 2 113 ? -16.524 -6.854  2.771   1.00 21.01 ? 499  GLU   B N    1 
ATOM   2869 C  CA   . GLU   B 2 113 ? -17.123 -5.523  2.735   1.00 22.77 ? 499  GLU   B CA   1 
ATOM   2870 C  C    . GLU   B 2 113 ? -16.297 -4.525  3.538   1.00 25.23 ? 499  GLU   B C    1 
ATOM   2871 O  O    . GLU   B 2 113 ? -16.198 -3.349  3.170   1.00 25.95 ? 499  GLU   B O    1 
ATOM   2872 C  CB   . GLU   B 2 113 ? -18.555 -5.577  3.262   1.00 21.68 ? 499  GLU   B CB   1 
ATOM   2873 C  CG   . GLU   B 2 113 ? -19.517 -6.348  2.372   1.00 20.46 ? 499  GLU   B CG   1 
ATOM   2874 C  CD   . GLU   B 2 113 ? -19.611 -5.762  0.979   1.00 25.33 ? 499  GLU   B CD   1 
ATOM   2875 O  OE1  . GLU   B 2 113 ? -19.856 -4.542  0.862   1.00 29.32 ? 499  GLU   B OE1  1 
ATOM   2876 O  OE2  . GLU   B 2 113 ? -19.440 -6.520  0.001   1.00 25.68 ? 499  GLU   B OE2  1 
ATOM   2877 N  N    . VAL   B 2 114 ? -15.688 -4.980  4.631   1.00 24.44 ? 500  VAL   B N    1 
ATOM   2878 C  CA   . VAL   B 2 114 ? -14.861 -4.098  5.446   1.00 25.31 ? 500  VAL   B CA   1 
ATOM   2879 C  C    . VAL   B 2 114 ? -13.457 -3.983  4.867   1.00 25.15 ? 500  VAL   B C    1 
ATOM   2880 O  O    . VAL   B 2 114 ? -12.864 -2.899  4.865   1.00 32.15 ? 500  VAL   B O    1 
ATOM   2881 C  CB   . VAL   B 2 114 ? -14.835 -4.596  6.902   1.00 19.89 ? 500  VAL   B CB   1 
ATOM   2882 C  CG1  . VAL   B 2 114 ? -13.942 -3.711  7.752   1.00 20.83 ? 500  VAL   B CG1  1 
ATOM   2883 C  CG2  . VAL   B 2 114 ? -16.244 -4.642  7.472   1.00 21.51 ? 500  VAL   B CG2  1 
ATOM   2884 N  N    . VAL   B 2 115 ? -12.905 -5.093  4.369   1.00 25.29 ? 501  VAL   B N    1 
ATOM   2885 C  CA   . VAL   B 2 115 ? -11.549 -5.079  3.822   1.00 28.64 ? 501  VAL   B CA   1 
ATOM   2886 C  C    . VAL   B 2 115 ? -11.451 -4.089  2.668   1.00 31.33 ? 501  VAL   B C    1 
ATOM   2887 O  O    . VAL   B 2 115 ? -10.555 -3.237  2.627   1.00 30.29 ? 501  VAL   B O    1 
ATOM   2888 C  CB   . VAL   B 2 115 ? -11.130 -6.494  3.382   1.00 30.48 ? 501  VAL   B CB   1 
ATOM   2889 C  CG1  . VAL   B 2 115 ? -9.944  -6.428  2.431   1.00 29.23 ? 501  VAL   B CG1  1 
ATOM   2890 C  CG2  . VAL   B 2 115 ? -10.792 -7.347  4.588   1.00 23.13 ? 501  VAL   B CG2  1 
ATOM   2891 N  N    . TYR   B 2 116 ? -12.381 -4.179  1.720   1.00 30.56 ? 502  TYR   B N    1 
ATOM   2892 C  CA   . TYR   B 2 116 ? -12.368 -3.338  0.534   1.00 31.48 ? 502  TYR   B CA   1 
ATOM   2893 C  C    . TYR   B 2 116 ? -13.142 -2.039  0.731   1.00 34.20 ? 502  TYR   B C    1 
ATOM   2894 O  O    . TYR   B 2 116 ? -13.530 -1.399  -0.255  1.00 36.94 ? 502  TYR   B O    1 
ATOM   2895 C  CB   . TYR   B 2 116 ? -12.894 -4.134  -0.662  1.00 36.55 ? 502  TYR   B CB   1 
ATOM   2896 C  CG   . TYR   B 2 116 ? -12.104 -5.410  -0.860  1.00 40.50 ? 502  TYR   B CG   1 
ATOM   2897 C  CD1  . TYR   B 2 116 ? -10.840 -5.382  -1.435  1.00 38.71 ? 502  TYR   B CD1  1 
ATOM   2898 C  CD2  . TYR   B 2 116 ? -12.601 -6.635  -0.434  1.00 33.11 ? 502  TYR   B CD2  1 
ATOM   2899 C  CE1  . TYR   B 2 116 ? -10.104 -6.540  -1.602  1.00 36.97 ? 502  TYR   B CE1  1 
ATOM   2900 C  CE2  . TYR   B 2 116 ? -11.872 -7.798  -0.596  1.00 31.90 ? 502  TYR   B CE2  1 
ATOM   2901 C  CZ   . TYR   B 2 116 ? -10.624 -7.745  -1.181  1.00 42.77 ? 502  TYR   B CZ   1 
ATOM   2902 O  OH   . TYR   B 2 116 ? -9.892  -8.898  -1.347  1.00 42.72 ? 502  TYR   B OH   1 
ATOM   2903 N  N    . GLN   B 2 117 ? -13.376 -1.650  1.986   1.00 31.92 ? 503  GLN   B N    1 
ATOM   2904 C  CA   . GLN   B 2 117 ? -13.775 -0.291  2.355   1.00 29.14 ? 503  GLN   B CA   1 
ATOM   2905 C  C    . GLN   B 2 117 ? -15.140 0.098   1.795   1.00 25.67 ? 503  GLN   B C    1 
ATOM   2906 O  O    . GLN   B 2 117 ? -15.412 1.278   1.563   1.00 26.53 ? 503  GLN   B O    1 
ATOM   2907 C  CB   . GLN   B 2 117 ? -12.709 0.724   1.931   1.00 28.05 ? 503  GLN   B CB   1 
ATOM   2908 C  CG   . GLN   B 2 117 ? -11.297 0.328   2.335   1.00 35.60 ? 503  GLN   B CG   1 
ATOM   2909 C  CD   . GLN   B 2 117 ? -10.267 1.373   1.963   1.00 37.30 ? 503  GLN   B CD   1 
ATOM   2910 O  OE1  . GLN   B 2 117 ? -10.171 1.781   0.806   1.00 36.58 ? 503  GLN   B OE1  1 
ATOM   2911 N  NE2  . GLN   B 2 117 ? -9.484  1.807   2.944   1.00 44.95 ? 503  GLN   B NE2  1 
ATOM   2912 N  N    . ARG   B 2 118 ? -16.015 -0.881  1.578   1.00 28.26 ? 504  ARG   B N    1 
ATOM   2913 C  CA   . ARG   B 2 118 ? -17.408 -0.585  1.277   1.00 23.72 ? 504  ARG   B CA   1 
ATOM   2914 C  C    . ARG   B 2 118 ? -18.249 -0.402  2.533   1.00 24.85 ? 504  ARG   B C    1 
ATOM   2915 O  O    . ARG   B 2 118 ? -19.381 0.082   2.438   1.00 26.52 ? 504  ARG   B O    1 
ATOM   2916 C  CB   . ARG   B 2 118 ? -18.016 -1.690  0.408   1.00 27.71 ? 504  ARG   B CB   1 
ATOM   2917 C  CG   . ARG   B 2 118 ? -17.605 -1.617  -1.052  1.00 28.43 ? 504  ARG   B CG   1 
ATOM   2918 C  CD   . ARG   B 2 118 ? -18.345 -2.649  -1.887  1.00 36.93 ? 504  ARG   B CD   1 
ATOM   2919 N  NE   . ARG   B 2 118 ? -17.766 -3.978  -1.740  1.00 37.50 ? 504  ARG   B NE   1 
ATOM   2920 C  CZ   . ARG   B 2 118 ? -16.665 -4.388  -2.353  1.00 45.66 ? 504  ARG   B CZ   1 
ATOM   2921 N  NH1  . ARG   B 2 118 ? -15.996 -3.596  -3.176  1.00 42.28 ? 504  ARG   B NH1  1 
ATOM   2922 N  NH2  . ARG   B 2 118 ? -16.222 -5.622  -2.134  1.00 43.85 ? 504  ARG   B NH2  1 
ATOM   2923 N  N    . ALA   B 2 119 ? -17.721 -0.771  3.698   1.00 20.42 ? 505  ALA   B N    1 
ATOM   2924 C  CA   . ALA   B 2 119 ? -18.412 -0.599  4.966   1.00 23.01 ? 505  ALA   B CA   1 
ATOM   2925 C  C    . ALA   B 2 119 ? -17.406 -0.186  6.027   1.00 30.14 ? 505  ALA   B C    1 
ATOM   2926 O  O    . ALA   B 2 119 ? -16.281 -0.692  6.057   1.00 30.19 ? 505  ALA   B O    1 
ATOM   2927 C  CB   . ALA   B 2 119 ? -19.131 -1.884  5.394   1.00 17.06 ? 505  ALA   B CB   1 
ATOM   2928 N  N    . VAL   B 2 120 ? -17.816 0.742   6.895   1.00 25.74 ? 506  VAL   B N    1 
ATOM   2929 C  CA   . VAL   B 2 120 ? -16.934 1.172   7.974   1.00 20.18 ? 506  VAL   B CA   1 
ATOM   2930 C  C    . VAL   B 2 120 ? -16.821 0.087   9.036   1.00 27.72 ? 506  VAL   B C    1 
ATOM   2931 O  O    . VAL   B 2 120 ? -15.761 -0.081  9.652   1.00 22.33 ? 506  VAL   B O    1 
ATOM   2932 C  CB   . VAL   B 2 120 ? -17.431 2.504   8.566   1.00 25.19 ? 506  VAL   B CB   1 
ATOM   2933 C  CG1  . VAL   B 2 120 ? -16.525 2.962   9.701   1.00 25.15 ? 506  VAL   B CG1  1 
ATOM   2934 C  CG2  . VAL   B 2 120 ? -17.508 3.566   7.478   1.00 28.72 ? 506  VAL   B CG2  1 
ATOM   2935 N  N    . MET   B 2 121 ? -17.890 -0.675  9.260   1.00 21.32 ? 507  MET   B N    1 
ATOM   2936 C  CA   . MET   B 2 121 ? -17.856 -1.755  10.236  1.00 21.33 ? 507  MET   B CA   1 
ATOM   2937 C  C    . MET   B 2 121 ? -18.904 -2.798  9.873   1.00 19.98 ? 507  MET   B C    1 
ATOM   2938 O  O    . MET   B 2 121 ? -19.758 -2.581  9.011   1.00 20.03 ? 507  MET   B O    1 
ATOM   2939 C  CB   . MET   B 2 121 ? -18.066 -1.228  11.660  1.00 23.11 ? 507  MET   B CB   1 
ATOM   2940 C  CG   . MET   B 2 121 ? -19.454 -0.688  11.931  1.00 24.42 ? 507  MET   B CG   1 
ATOM   2941 S  SD   . MET   B 2 121 ? -19.592 0.002   13.593  1.00 32.79 ? 507  MET   B SD   1 
ATOM   2942 C  CE   . MET   B 2 121 ? -18.338 1.274   13.525  1.00 18.10 ? 507  MET   B CE   1 
ATOM   2943 N  N    . ALA   B 2 122 ? -18.819 -3.944  10.547  1.00 19.47 ? 508  ALA   B N    1 
ATOM   2944 C  CA   . ALA   B 2 122 ? -19.726 -5.064  10.336  1.00 19.73 ? 508  ALA   B CA   1 
ATOM   2945 C  C    . ALA   B 2 122 ? -20.231 -5.552  11.684  1.00 17.63 ? 508  ALA   B C    1 
ATOM   2946 O  O    . ALA   B 2 122 ? -19.433 -5.797  12.594  1.00 21.20 ? 508  ALA   B O    1 
ATOM   2947 C  CB   . ALA   B 2 122 ? -19.035 -6.207  9.586   1.00 17.58 ? 508  ALA   B CB   1 
ATOM   2948 N  N    . VAL   B 2 123 ? -21.548 -5.695  11.811  1.00 15.88 ? 509  VAL   B N    1 
ATOM   2949 C  CA   . VAL   B 2 123 ? -22.177 -6.137  13.049  1.00 15.46 ? 509  VAL   B CA   1 
ATOM   2950 C  C    . VAL   B 2 123 ? -23.038 -7.358  12.754  1.00 15.01 ? 509  VAL   B C    1 
ATOM   2951 O  O    . VAL   B 2 123 ? -23.779 -7.383  11.765  1.00 17.25 ? 509  VAL   B O    1 
ATOM   2952 C  CB   . VAL   B 2 123 ? -23.021 -5.015  13.692  1.00 18.57 ? 509  VAL   B CB   1 
ATOM   2953 C  CG1  . VAL   B 2 123 ? -23.488 -5.426  15.082  1.00 14.27 ? 509  VAL   B CG1  1 
ATOM   2954 C  CG2  . VAL   B 2 123 ? -22.229 -3.715  13.747  1.00 24.57 ? 509  VAL   B CG2  1 
ATOM   2955 N  N    . GLY   B 2 124 ? -22.938 -8.368  13.611  1.00 16.65 ? 510  GLY   B N    1 
ATOM   2956 C  CA   . GLY   B 2 124 ? -23.722 -9.579  13.445  1.00 16.47 ? 510  GLY   B CA   1 
ATOM   2957 C  C    . GLY   B 2 124 ? -23.065 -10.746 14.165  1.00 14.38 ? 510  GLY   B C    1 
ATOM   2958 O  O    . GLY   B 2 124 ? -22.301 -10.559 15.109  1.00 16.92 ? 510  GLY   B O    1 
ATOM   2959 N  N    . SER   B 2 125 ? -23.390 -11.949 13.693  1.00 10.65 ? 511  SER   B N    1 
ATOM   2960 C  CA   . SER   B 2 125 ? -22.810 -13.181 14.229  1.00 14.19 ? 511  SER   B CA   1 
ATOM   2961 C  C    . SER   B 2 125 ? -21.477 -13.481 13.540  1.00 15.44 ? 511  SER   B C    1 
ATOM   2962 O  O    . SER   B 2 125 ? -21.282 -14.512 12.897  1.00 16.60 ? 511  SER   B O    1 
ATOM   2963 C  CB   . SER   B 2 125 ? -23.792 -14.337 14.075  1.00 13.00 ? 511  SER   B CB   1 
ATOM   2964 O  OG   . SER   B 2 125 ? -24.263 -14.433 12.742  1.00 16.77 ? 511  SER   B OG   1 
ATOM   2965 N  N    . LEU   B 2 126 ? -20.547 -12.544 13.697  1.00 11.63 ? 512  LEU   B N    1 
ATOM   2966 C  CA   . LEU   B 2 126 ? -19.266 -12.573 13.005  1.00 10.35 ? 512  LEU   B CA   1 
ATOM   2967 C  C    . LEU   B 2 126 ? -18.186 -13.051 13.967  1.00 14.19 ? 512  LEU   B C    1 
ATOM   2968 O  O    . LEU   B 2 126 ? -17.880 -12.369 14.951  1.00 12.75 ? 512  LEU   B O    1 
ATOM   2969 C  CB   . LEU   B 2 126 ? -18.930 -11.187 12.459  1.00 11.08 ? 512  LEU   B CB   1 
ATOM   2970 C  CG   . LEU   B 2 126 ? -17.773 -11.101 11.472  1.00 14.62 ? 512  LEU   B CG   1 
ATOM   2971 C  CD1  . LEU   B 2 126 ? -18.153 -11.824 10.197  1.00 12.38 ? 512  LEU   B CD1  1 
ATOM   2972 C  CD2  . LEU   B 2 126 ? -17.449 -9.653  11.191  1.00 11.95 ? 512  LEU   B CD2  1 
ATOM   2973 N  N    . THR   B 2 127 ? -17.601 -14.211 13.676  1.00 14.93 ? 513  THR   B N    1 
ATOM   2974 C  CA   . THR   B 2 127 ? -16.667 -14.849 14.595  1.00 16.12 ? 513  THR   B CA   1 
ATOM   2975 C  C    . THR   B 2 127 ? -15.273 -14.243 14.471  1.00 11.22 ? 513  THR   B C    1 
ATOM   2976 O  O    . THR   B 2 127 ? -14.753 -14.073 13.363  1.00 12.56 ? 513  THR   B O    1 
ATOM   2977 C  CB   . THR   B 2 127 ? -16.610 -16.354 14.329  1.00 11.51 ? 513  THR   B CB   1 
ATOM   2978 O  OG1  . THR   B 2 127 ? -17.890 -16.936 14.604  1.00 16.47 ? 513  THR   B OG1  1 
ATOM   2979 C  CG2  . THR   B 2 127 ? -15.560 -17.019 15.207  1.00 10.44 ? 513  THR   B CG2  1 
ATOM   2980 N  N    . ILE   B 2 128 ? -14.671 -13.924 15.613  1.00 10.49 ? 514  ILE   B N    1 
ATOM   2981 C  CA   . ILE   B 2 128 ? -13.289 -13.457 15.660  1.00 13.27 ? 514  ILE   B CA   1 
ATOM   2982 C  C    . ILE   B 2 128 ? -12.363 -14.660 15.534  1.00 13.54 ? 514  ILE   B C    1 
ATOM   2983 O  O    . ILE   B 2 128 ? -12.428 -15.592 16.343  1.00 12.59 ? 514  ILE   B O    1 
ATOM   2984 C  CB   . ILE   B 2 128 ? -13.009 -12.693 16.963  1.00 14.87 ? 514  ILE   B CB   1 
ATOM   2985 C  CG1  . ILE   B 2 128 ? -13.868 -11.431 17.055  1.00 18.25 ? 514  ILE   B CG1  1 
ATOM   2986 C  CG2  . ILE   B 2 128 ? -11.529 -12.353 17.075  1.00 17.28 ? 514  ILE   B CG2  1 
ATOM   2987 C  CD1  . ILE   B 2 128 ? -13.904 -10.824 18.442  1.00 12.10 ? 514  ILE   B CD1  1 
ATOM   2988 N  N    . ASN   B 2 129 ? -11.496 -14.646 14.523  1.00 13.24 ? 515  ASN   B N    1 
ATOM   2989 C  CA   . ASN   B 2 129 ? -10.430 -15.634 14.427  1.00 19.40 ? 515  ASN   B CA   1 
ATOM   2990 C  C    . ASN   B 2 129 ? -9.166  -14.954 13.917  1.00 20.21 ? 515  ASN   B C    1 
ATOM   2991 O  O    . ASN   B 2 129 ? -9.167  -13.772 13.562  1.00 14.25 ? 515  ASN   B O    1 
ATOM   2992 C  CB   . ASN   B 2 129 ? -10.833 -16.840 13.553  1.00 14.92 ? 515  ASN   B CB   1 
ATOM   2993 C  CG   . ASN   B 2 129 ? -11.111 -16.473 12.102  1.00 19.11 ? 515  ASN   B CG   1 
ATOM   2994 O  OD1  . ASN   B 2 129 ? -10.640 -15.458 11.594  1.00 19.43 ? 515  ASN   B OD1  1 
ATOM   2995 N  ND2  . ASN   B 2 129 ? -11.883 -17.316 11.426  1.00 12.75 ? 515  ASN   B ND2  1 
ATOM   2996 N  N    . GLU   B 2 130 ? -8.077  -15.724 13.881  1.00 19.29 ? 516  GLU   B N    1 
ATOM   2997 C  CA   . GLU   B 2 130 ? -6.762  -15.148 13.614  1.00 22.08 ? 516  GLU   B CA   1 
ATOM   2998 C  C    . GLU   B 2 130 ? -6.661  -14.610 12.191  1.00 23.07 ? 516  GLU   B C    1 
ATOM   2999 O  O    . GLU   B 2 130 ? -6.230  -13.470 11.979  1.00 21.95 ? 516  GLU   B O    1 
ATOM   3000 C  CB   . GLU   B 2 130 ? -5.672  -16.189 13.870  1.00 19.23 ? 516  GLU   B CB   1 
ATOM   3001 C  CG   . GLU   B 2 130 ? -4.261  -15.665 13.654  1.00 18.29 ? 516  GLU   B CG   1 
ATOM   3002 C  CD   . GLU   B 2 130 ? -3.214  -16.761 13.702  1.00 24.13 ? 516  GLU   B CD   1 
ATOM   3003 O  OE1  . GLU   B 2 130 ? -3.587  -17.949 13.601  1.00 23.64 ? 516  GLU   B OE1  1 
ATOM   3004 O  OE2  . GLU   B 2 130 ? -2.016  -16.434 13.837  1.00 32.94 ? 516  GLU   B OE2  1 
ATOM   3005 N  N    . GLU   B 2 131 ? -7.050  -15.416 11.199  1.00 21.21 ? 517  GLU   B N    1 
ATOM   3006 C  CA   . GLU   B 2 131 ? -6.837  -15.020 9.810   1.00 25.06 ? 517  GLU   B CA   1 
ATOM   3007 C  C    . GLU   B 2 131 ? -7.688  -13.817 9.422   1.00 26.19 ? 517  GLU   B C    1 
ATOM   3008 O  O    . GLU   B 2 131 ? -7.313  -13.064 8.516   1.00 21.34 ? 517  GLU   B O    1 
ATOM   3009 C  CB   . GLU   B 2 131 ? -7.109  -16.200 8.875   1.00 18.30 ? 517  GLU   B CB   1 
ATOM   3010 C  CG   . GLU   B 2 131 ? -8.576  -16.527 8.664   1.00 26.51 ? 517  GLU   B CG   1 
ATOM   3011 C  CD   . GLU   B 2 131 ? -8.786  -17.514 7.533   1.00 27.86 ? 517  GLU   B CD   1 
ATOM   3012 O  OE1  . GLU   B 2 131 ? -7.782  -18.066 7.035   1.00 27.49 ? 517  GLU   B OE1  1 
ATOM   3013 O  OE2  . GLU   B 2 131 ? -9.950  -17.737 7.141   1.00 29.55 ? 517  GLU   B OE2  1 
ATOM   3014 N  N    . ARG   B 2 132 ? -8.827  -13.613 10.090  1.00 25.34 ? 518  ARG   B N    1 
ATOM   3015 C  CA   . ARG   B 2 132 ? -9.623  -12.418 9.829   1.00 20.83 ? 518  ARG   B CA   1 
ATOM   3016 C  C    . ARG   B 2 132 ? -8.999  -11.193 10.482  1.00 26.61 ? 518  ARG   B C    1 
ATOM   3017 O  O    . ARG   B 2 132 ? -9.009  -10.100 9.904   1.00 24.58 ? 518  ARG   B O    1 
ATOM   3018 C  CB   . ARG   B 2 132 ? -11.056 -12.617 10.321  1.00 18.12 ? 518  ARG   B CB   1 
ATOM   3019 C  CG   . ARG   B 2 132 ? -11.875 -13.557 9.459   1.00 21.99 ? 518  ARG   B CG   1 
ATOM   3020 C  CD   . ARG   B 2 132 ? -13.162 -13.970 10.151  1.00 14.48 ? 518  ARG   B CD   1 
ATOM   3021 N  NE   . ARG   B 2 132 ? -13.939 -14.884 9.324   1.00 15.54 ? 518  ARG   B NE   1 
ATOM   3022 C  CZ   . ARG   B 2 132 ? -15.132 -15.362 9.649   1.00 18.40 ? 518  ARG   B CZ   1 
ATOM   3023 N  NH1  . ARG   B 2 132 ? -15.727 -15.025 10.782  1.00 17.94 ? 518  ARG   B NH1  1 
ATOM   3024 N  NH2  . ARG   B 2 132 ? -15.743 -16.200 8.817   1.00 13.32 ? 518  ARG   B NH2  1 
ATOM   3025 N  N    . SER   B 2 133 ? -8.445  -11.357 11.685  1.00 20.37 ? 519  SER   B N    1 
ATOM   3026 C  CA   . SER   B 2 133 ? -7.777  -10.254 12.361  1.00 20.45 ? 519  SER   B CA   1 
ATOM   3027 C  C    . SER   B 2 133 ? -6.551  -9.760  11.606  1.00 25.39 ? 519  SER   B C    1 
ATOM   3028 O  O    . SER   B 2 133 ? -6.043  -8.679  11.924  1.00 25.64 ? 519  SER   B O    1 
ATOM   3029 C  CB   . SER   B 2 133 ? -7.380  -10.674 13.778  1.00 20.47 ? 519  SER   B CB   1 
ATOM   3030 O  OG   . SER   B 2 133 ? -8.508  -11.119 14.510  1.00 23.32 ? 519  SER   B OG   1 
ATOM   3031 N  N    . GLU   B 2 134 ? -6.065  -10.519 10.621  1.00 26.69 ? 520  GLU   B N    1 
ATOM   3032 C  CA   . GLU   B 2 134 ? -4.944  -10.051 9.814   1.00 24.03 ? 520  GLU   B CA   1 
ATOM   3033 C  C    . GLU   B 2 134 ? -5.375  -8.986  8.815   1.00 25.10 ? 520  GLU   B C    1 
ATOM   3034 O  O    . GLU   B 2 134 ? -4.569  -8.125  8.445   1.00 28.67 ? 520  GLU   B O    1 
ATOM   3035 C  CB   . GLU   B 2 134 ? -4.297  -11.225 9.082   1.00 23.57 ? 520  GLU   B CB   1 
ATOM   3036 C  CG   . GLU   B 2 134 ? -3.538  -12.194 9.979   1.00 30.83 ? 520  GLU   B CG   1 
ATOM   3037 C  CD   . GLU   B 2 134 ? -3.042  -13.410 9.222   1.00 31.82 ? 520  GLU   B CD   1 
ATOM   3038 O  OE1  . GLU   B 2 134 ? -3.104  -13.398 7.975   1.00 37.40 ? 520  GLU   B OE1  1 
ATOM   3039 O  OE2  . GLU   B 2 134 ? -2.590  -14.377 9.870   1.00 41.01 ? 520  GLU   B OE2  1 
ATOM   3040 N  N    . VAL   B 2 135 ? -6.632  -9.019  8.378   1.00 23.61 ? 521  VAL   B N    1 
ATOM   3041 C  CA   . VAL   B 2 135 ? -7.119  -8.095  7.362   1.00 23.50 ? 521  VAL   B CA   1 
ATOM   3042 C  C    . VAL   B 2 135 ? -8.105  -7.067  7.909   1.00 22.81 ? 521  VAL   B C    1 
ATOM   3043 O  O    . VAL   B 2 135 ? -8.308  -6.028  7.261   1.00 28.89 ? 521  VAL   B O    1 
ATOM   3044 C  CB   . VAL   B 2 135 ? -7.750  -8.854  6.176   1.00 25.20 ? 521  VAL   B CB   1 
ATOM   3045 C  CG1  . VAL   B 2 135 ? -6.683  -9.626  5.417   1.00 25.99 ? 521  VAL   B CG1  1 
ATOM   3046 C  CG2  . VAL   B 2 135 ? -8.843  -9.789  6.666   1.00 21.06 ? 521  VAL   B CG2  1 
ATOM   3047 N  N    . VAL   B 2 136 ? -8.732  -7.317  9.060   1.00 22.82 ? 522  VAL   B N    1 
ATOM   3048 C  CA   . VAL   B 2 136 ? -9.629  -6.356  9.687   1.00 21.76 ? 522  VAL   B CA   1 
ATOM   3049 C  C    . VAL   B 2 136 ? -9.291  -6.256  11.167  1.00 26.35 ? 522  VAL   B C    1 
ATOM   3050 O  O    . VAL   B 2 136 ? -8.595  -7.102  11.732  1.00 26.74 ? 522  VAL   B O    1 
ATOM   3051 C  CB   . VAL   B 2 136 ? -11.123 -6.720  9.516   1.00 16.91 ? 522  VAL   B CB   1 
ATOM   3052 C  CG1  . VAL   B 2 136 ? -11.477 -6.883  8.053   1.00 17.98 ? 522  VAL   B CG1  1 
ATOM   3053 C  CG2  . VAL   B 2 136 ? -11.461 -7.981  10.301  1.00 19.26 ? 522  VAL   B CG2  1 
ATOM   3054 N  N    . ASP   B 2 137 ? -9.797  -5.198  11.791  1.00 19.67 ? 523  ASP   B N    1 
ATOM   3055 C  CA   . ASP   B 2 137 ? -9.714  -5.024  13.232  1.00 18.09 ? 523  ASP   B CA   1 
ATOM   3056 C  C    . ASP   B 2 137 ? -11.011 -5.493  13.872  1.00 19.28 ? 523  ASP   B C    1 
ATOM   3057 O  O    . ASP   B 2 137 ? -12.101 -5.251  13.344  1.00 19.88 ? 523  ASP   B O    1 
ATOM   3058 C  CB   . ASP   B 2 137 ? -9.448  -3.562  13.596  1.00 23.66 ? 523  ASP   B CB   1 
ATOM   3059 C  CG   . ASP   B 2 137 ? -7.973  -3.216  13.581  1.00 24.89 ? 523  ASP   B CG   1 
ATOM   3060 O  OD1  . ASP   B 2 137 ? -7.145  -4.145  13.481  1.00 28.10 ? 523  ASP   B OD1  1 
ATOM   3061 O  OD2  . ASP   B 2 137 ? -7.641  -2.015  13.670  1.00 25.30 ? 523  ASP   B OD2  1 
ATOM   3062 N  N    . PHE   B 2 138 ? -10.890 -6.174  15.006  1.00 18.94 ? 524  PHE   B N    1 
ATOM   3063 C  CA   . PHE   B 2 138 ? -12.041 -6.676  15.738  1.00 20.46 ? 524  PHE   B CA   1 
ATOM   3064 C  C    . PHE   B 2 138 ? -12.142 -5.973  17.082  1.00 18.51 ? 524  PHE   B C    1 
ATOM   3065 O  O    . PHE   B 2 138 ? -11.134 -5.770  17.766  1.00 23.85 ? 524  PHE   B O    1 
ATOM   3066 C  CB   . PHE   B 2 138 ? -11.952 -8.189  15.954  1.00 21.31 ? 524  PHE   B CB   1 
ATOM   3067 C  CG   . PHE   B 2 138 ? -12.497 -8.997  14.813  1.00 20.28 ? 524  PHE   B CG   1 
ATOM   3068 C  CD1  . PHE   B 2 138 ? -13.859 -9.035  14.564  1.00 17.19 ? 524  PHE   B CD1  1 
ATOM   3069 C  CD2  . PHE   B 2 138 ? -11.649 -9.723  13.995  1.00 19.05 ? 524  PHE   B CD2  1 
ATOM   3070 C  CE1  . PHE   B 2 138 ? -14.364 -9.782  13.517  1.00 15.51 ? 524  PHE   B CE1  1 
ATOM   3071 C  CE2  . PHE   B 2 138 ? -12.148 -10.471 12.947  1.00 21.51 ? 524  PHE   B CE2  1 
ATOM   3072 C  CZ   . PHE   B 2 138 ? -13.508 -10.500 12.707  1.00 14.27 ? 524  PHE   B CZ   1 
ATOM   3073 N  N    . SER   B 2 139 ? -13.364 -5.605  17.456  1.00 20.28 ? 525  SER   B N    1 
ATOM   3074 C  CA   . SER   B 2 139 ? -13.612 -5.099  18.794  1.00 20.90 ? 525  SER   B CA   1 
ATOM   3075 C  C    . SER   B 2 139 ? -13.415 -6.221  19.811  1.00 22.24 ? 525  SER   B C    1 
ATOM   3076 O  O    . SER   B 2 139 ? -13.091 -7.363  19.468  1.00 19.97 ? 525  SER   B O    1 
ATOM   3077 C  CB   . SER   B 2 139 ? -15.021 -4.518  18.890  1.00 20.20 ? 525  SER   B CB   1 
ATOM   3078 O  OG   . SER   B 2 139 ? -15.998 -5.545  18.830  1.00 19.94 ? 525  SER   B OG   1 
ATOM   3079 N  N    . VAL   B 2 140 ? -13.607 -5.895  21.084  1.00 20.02 ? 526  VAL   B N    1 
ATOM   3080 C  CA   . VAL   B 2 140 ? -13.626 -6.922  22.122  1.00 15.85 ? 526  VAL   B CA   1 
ATOM   3081 C  C    . VAL   B 2 140 ? -14.794 -7.850  21.815  1.00 19.90 ? 526  VAL   B C    1 
ATOM   3082 O  O    . VAL   B 2 140 ? -15.808 -7.400  21.261  1.00 20.03 ? 526  VAL   B O    1 
ATOM   3083 C  CB   . VAL   B 2 140 ? -13.748 -6.311  23.527  1.00 20.22 ? 526  VAL   B CB   1 
ATOM   3084 C  CG1  . VAL   B 2 140 ? -12.475 -5.566  23.897  1.00 16.43 ? 526  VAL   B CG1  1 
ATOM   3085 C  CG2  . VAL   B 2 140 ? -14.955 -5.390  23.600  1.00 21.15 ? 526  VAL   B CG2  1 
ATOM   3086 N  N    . PRO   B 2 141 ? -14.698 -9.142  22.118  1.00 16.57 ? 527  PRO   B N    1 
ATOM   3087 C  CA   . PRO   B 2 141 ? -15.858 -10.017 21.928  1.00 15.72 ? 527  PRO   B CA   1 
ATOM   3088 C  C    . PRO   B 2 141 ? -16.992 -9.602  22.852  1.00 16.20 ? 527  PRO   B C    1 
ATOM   3089 O  O    . PRO   B 2 141 ? -16.771 -9.217  24.001  1.00 16.06 ? 527  PRO   B O    1 
ATOM   3090 C  CB   . PRO   B 2 141 ? -15.316 -11.408 22.279  1.00 20.70 ? 527  PRO   B CB   1 
ATOM   3091 C  CG   . PRO   B 2 141 ? -14.148 -11.141 23.170  1.00 14.30 ? 527  PRO   B CG   1 
ATOM   3092 C  CD   . PRO   B 2 141 ? -13.536 -9.872  22.653  1.00 16.23 ? 527  PRO   B CD   1 
ATOM   3093 N  N    . PHE   B 2 142 ? -18.218 -9.657  22.331  1.00 18.59 ? 528  PHE   B N    1 
ATOM   3094 C  CA   . PHE   B 2 142 ? -19.391 -9.328  23.127  1.00 22.16 ? 528  PHE   B CA   1 
ATOM   3095 C  C    . PHE   B 2 142 ? -20.436 -10.433 23.166  1.00 15.59 ? 528  PHE   B C    1 
ATOM   3096 O  O    . PHE   B 2 142 ? -21.410 -10.305 23.917  1.00 19.88 ? 528  PHE   B O    1 
ATOM   3097 C  CB   . PHE   B 2 142 ? -20.039 -8.022  22.631  1.00 13.78 ? 528  PHE   B CB   1 
ATOM   3098 C  CG   . PHE   B 2 142 ? -20.513 -8.069  21.204  1.00 17.02 ? 528  PHE   B CG   1 
ATOM   3099 C  CD1  . PHE   B 2 142 ? -19.634 -7.835  20.158  1.00 18.35 ? 528  PHE   B CD1  1 
ATOM   3100 C  CD2  . PHE   B 2 142 ? -21.845 -8.320  20.910  1.00 17.17 ? 528  PHE   B CD2  1 
ATOM   3101 C  CE1  . PHE   B 2 142 ? -20.070 -7.870  18.844  1.00 17.33 ? 528  PHE   B CE1  1 
ATOM   3102 C  CE2  . PHE   B 2 142 ? -22.286 -8.356  19.599  1.00 17.39 ? 528  PHE   B CE2  1 
ATOM   3103 C  CZ   . PHE   B 2 142 ? -21.398 -8.130  18.566  1.00 17.25 ? 528  PHE   B CZ   1 
ATOM   3104 N  N    . VAL   B 2 143 ? -20.271 -11.504 22.394  1.00 15.60 ? 529  VAL   B N    1 
ATOM   3105 C  CA   . VAL   B 2 143 ? -21.070 -12.718 22.523  1.00 17.45 ? 529  VAL   B CA   1 
ATOM   3106 C  C    . VAL   B 2 143 ? -20.110 -13.897 22.493  1.00 12.98 ? 529  VAL   B C    1 
ATOM   3107 O  O    . VAL   B 2 143 ? -19.422 -14.111 21.488  1.00 15.43 ? 529  VAL   B O    1 
ATOM   3108 C  CB   . VAL   B 2 143 ? -22.124 -12.856 21.412  1.00 15.22 ? 529  VAL   B CB   1 
ATOM   3109 C  CG1  . VAL   B 2 143 ? -22.806 -14.215 21.501  1.00 11.90 ? 529  VAL   B CG1  1 
ATOM   3110 C  CG2  . VAL   B 2 143 ? -23.146 -11.741 21.502  1.00 12.24 ? 529  VAL   B CG2  1 
ATOM   3111 N  N    . GLU   B 2 144 ? -20.059 -14.652 23.587  1.00 17.26 ? 530  GLU   B N    1 
ATOM   3112 C  CA   . GLU   B 2 144 ? -19.163 -15.797 23.673  1.00 17.24 ? 530  GLU   B CA   1 
ATOM   3113 C  C    . GLU   B 2 144 ? -19.593 -16.877 22.688  1.00 18.01 ? 530  GLU   B C    1 
ATOM   3114 O  O    . GLU   B 2 144 ? -20.769 -17.251 22.636  1.00 24.98 ? 530  GLU   B O    1 
ATOM   3115 C  CB   . GLU   B 2 144 ? -19.156 -16.348 25.098  1.00 18.94 ? 530  GLU   B CB   1 
ATOM   3116 C  CG   . GLU   B 2 144 ? -17.858 -17.023 25.510  1.00 36.40 ? 530  GLU   B CG   1 
ATOM   3117 C  CD   . GLU   B 2 144 ? -17.945 -17.647 26.889  1.00 36.03 ? 530  GLU   B CD   1 
ATOM   3118 O  OE1  . GLU   B 2 144 ? -17.665 -18.857 27.016  1.00 38.25 ? 530  GLU   B OE1  1 
ATOM   3119 O  OE2  . GLU   B 2 144 ? -18.306 -16.928 27.843  1.00 30.74 ? 530  GLU   B OE2  1 
ATOM   3120 N  N    . THR   B 2 145 ? -18.643 -17.378 21.903  1.00 13.81 ? 531  THR   B N    1 
ATOM   3121 C  CA   . THR   B 2 145 ? -18.952 -18.390 20.901  1.00 15.41 ? 531  THR   B CA   1 
ATOM   3122 C  C    . THR   B 2 145 ? -17.696 -19.201 20.605  1.00 19.67 ? 531  THR   B C    1 
ATOM   3123 O  O    . THR   B 2 145 ? -16.644 -19.013 21.223  1.00 18.88 ? 531  THR   B O    1 
ATOM   3124 C  CB   . THR   B 2 145 ? -19.519 -17.757 19.627  1.00 17.03 ? 531  THR   B CB   1 
ATOM   3125 O  OG1  . THR   B 2 145 ? -20.085 -18.779 18.797  1.00 19.05 ? 531  THR   B OG1  1 
ATOM   3126 C  CG2  . THR   B 2 145 ? -18.429 -17.030 18.852  1.00 13.32 ? 531  THR   B CG2  1 
ATOM   3127 N  N    . GLY   B 2 146 ? -17.826 -20.116 19.648  1.00 19.66 ? 532  GLY   B N    1 
ATOM   3128 C  CA   . GLY   B 2 146 ? -16.763 -21.017 19.255  1.00 17.75 ? 532  GLY   B CA   1 
ATOM   3129 C  C    . GLY   B 2 146 ? -17.322 -22.163 18.440  1.00 19.04 ? 532  GLY   B C    1 
ATOM   3130 O  O    . GLY   B 2 146 ? -18.186 -21.953 17.584  1.00 18.82 ? 532  GLY   B O    1 
ATOM   3131 N  N    . ILE   B 2 147 ? -16.858 -23.381 18.703  1.00 15.14 ? 533  ILE   B N    1 
ATOM   3132 C  CA   . ILE   B 2 147 ? -17.302 -24.567 17.979  1.00 18.48 ? 533  ILE   B CA   1 
ATOM   3133 C  C    . ILE   B 2 147 ? -17.972 -25.511 18.967  1.00 21.81 ? 533  ILE   B C    1 
ATOM   3134 O  O    . ILE   B 2 147 ? -17.357 -25.919 19.961  1.00 25.29 ? 533  ILE   B O    1 
ATOM   3135 C  CB   . ILE   B 2 147 ? -16.139 -25.264 17.258  1.00 19.83 ? 533  ILE   B CB   1 
ATOM   3136 C  CG1  . ILE   B 2 147 ? -15.539 -24.338 16.198  1.00 19.38 ? 533  ILE   B CG1  1 
ATOM   3137 C  CG2  . ILE   B 2 147 ? -16.604 -26.564 16.634  1.00 17.89 ? 533  ILE   B CG2  1 
ATOM   3138 C  CD1  . ILE   B 2 147 ? -14.412 -24.966 15.410  1.00 20.77 ? 533  ILE   B CD1  1 
ATOM   3139 N  N    . SER   B 2 148 ? -19.228 -25.853 18.697  1.00 20.57 ? 534  SER   B N    1 
ATOM   3140 C  CA   . SER   B 2 148 ? -19.976 -26.832 19.470  1.00 18.04 ? 534  SER   B CA   1 
ATOM   3141 C  C    . SER   B 2 148 ? -20.495 -27.923 18.542  1.00 17.51 ? 534  SER   B C    1 
ATOM   3142 O  O    . SER   B 2 148 ? -20.438 -27.809 17.315  1.00 18.27 ? 534  SER   B O    1 
ATOM   3143 C  CB   . SER   B 2 148 ? -21.138 -26.176 20.228  1.00 15.59 ? 534  SER   B CB   1 
ATOM   3144 O  OG   . SER   B 2 148 ? -20.664 -25.305 21.239  1.00 19.48 ? 534  SER   B OG   1 
ATOM   3145 N  N    . VAL   B 2 149 ? -21.005 -28.995 19.144  1.00 17.62 ? 535  VAL   B N    1 
ATOM   3146 C  CA   . VAL   B 2 149 ? -21.539 -30.134 18.407  1.00 20.76 ? 535  VAL   B CA   1 
ATOM   3147 C  C    . VAL   B 2 149 ? -22.951 -30.398 18.905  1.00 23.84 ? 535  VAL   B C    1 
ATOM   3148 O  O    . VAL   B 2 149 ? -23.146 -30.726 20.081  1.00 23.45 ? 535  VAL   B O    1 
ATOM   3149 C  CB   . VAL   B 2 149 ? -20.667 -31.391 18.570  1.00 20.02 ? 535  VAL   B CB   1 
ATOM   3150 C  CG1  . VAL   B 2 149 ? -21.212 -32.528 17.718  1.00 22.00 ? 535  VAL   B CG1  1 
ATOM   3151 C  CG2  . VAL   B 2 149 ? -19.222 -31.091 18.206  1.00 23.02 ? 535  VAL   B CG2  1 
ATOM   3152 N  N    . MET   B 2 150 ? -23.931 -30.256 18.018  1.00 19.26 ? 536  MET   B N    1 
ATOM   3153 C  CA   . MET   B 2 150 ? -25.319 -30.557 18.340  1.00 20.81 ? 536  MET   B CA   1 
ATOM   3154 C  C    . MET   B 2 150 ? -25.640 -31.978 17.898  1.00 21.11 ? 536  MET   B C    1 
ATOM   3155 O  O    . MET   B 2 150 ? -25.370 -32.354 16.751  1.00 21.89 ? 536  MET   B O    1 
ATOM   3156 C  CB   . MET   B 2 150 ? -26.275 -29.567 17.673  1.00 18.87 ? 536  MET   B CB   1 
ATOM   3157 C  CG   . MET   B 2 150 ? -27.745 -29.926 17.853  1.00 15.66 ? 536  MET   B CG   1 
ATOM   3158 S  SD   . MET   B 2 150 ? -28.871 -28.667 17.223  1.00 32.27 ? 536  MET   B SD   1 
ATOM   3159 C  CE   . MET   B 2 150 ? -29.143 -27.701 18.704  1.00 18.27 ? 536  MET   B CE   1 
ATOM   3160 N  N    . VAL   B 2 151 ? -26.206 -32.764 18.814  1.00 16.70 ? 537  VAL   B N    1 
ATOM   3161 C  CA   . VAL   B 2 151 ? -26.591 -34.143 18.547  1.00 21.64 ? 537  VAL   B CA   1 
ATOM   3162 C  C    . VAL   B 2 151 ? -27.964 -34.384 19.156  1.00 21.89 ? 537  VAL   B C    1 
ATOM   3163 O  O    . VAL   B 2 151 ? -28.447 -33.611 19.986  1.00 22.86 ? 537  VAL   B O    1 
ATOM   3164 C  CB   . VAL   B 2 151 ? -25.577 -35.160 19.118  1.00 23.65 ? 537  VAL   B CB   1 
ATOM   3165 C  CG1  . VAL   B 2 151 ? -24.211 -34.989 18.471  1.00 27.57 ? 537  VAL   B CG1  1 
ATOM   3166 C  CG2  . VAL   B 2 151 ? -25.480 -35.011 20.627  1.00 19.28 ? 537  VAL   B CG2  1 
ATOM   3167 N  N    . SER   B 2 152 ? -28.597 -35.472 18.729  1.00 23.68 ? 538  SER   B N    1 
ATOM   3168 C  CA   . SER   B 2 152 ? -29.806 -35.922 19.400  1.00 25.42 ? 538  SER   B CA   1 
ATOM   3169 C  C    . SER   B 2 152 ? -29.456 -36.363 20.816  1.00 27.69 ? 538  SER   B C    1 
ATOM   3170 O  O    . SER   B 2 152 ? -28.375 -36.906 21.060  1.00 30.18 ? 538  SER   B O    1 
ATOM   3171 C  CB   . SER   B 2 152 ? -30.460 -37.065 18.625  1.00 27.18 ? 538  SER   B CB   1 
ATOM   3172 O  OG   . SER   B 2 152 ? -31.746 -37.361 19.140  1.00 37.44 ? 538  SER   B OG   1 
ATOM   3173 N  N    . ARG   B 2 153 ? -30.369 -36.110 21.752  1.00 29.71 ? 539  ARG   B N    1 
ATOM   3174 C  CA   . ARG   B 2 153 ? -30.089 -36.359 23.161  1.00 30.46 ? 539  ARG   B CA   1 
ATOM   3175 C  C    . ARG   B 2 153 ? -29.719 -37.819 23.395  1.00 31.36 ? 539  ARG   B C    1 
ATOM   3176 O  O    . ARG   B 2 153 ? -30.420 -38.732 22.950  1.00 24.62 ? 539  ARG   B O    1 
ATOM   3177 C  CB   . ARG   B 2 153 ? -31.298 -35.977 24.016  1.00 29.57 ? 539  ARG   B CB   1 
ATOM   3178 C  CG   . ARG   B 2 153 ? -31.109 -36.242 25.502  1.00 30.63 ? 539  ARG   B CG   1 
ATOM   3179 C  CD   . ARG   B 2 153 ? -32.291 -35.742 26.314  1.00 35.10 ? 539  ARG   B CD   1 
ATOM   3180 N  NE   . ARG   B 2 153 ? -31.908 -34.667 27.222  1.00 41.25 ? 539  ARG   B NE   1 
ATOM   3181 C  CZ   . ARG   B 2 153 ? -32.185 -33.386 27.023  1.00 30.03 ? 539  ARG   B CZ   1 
ATOM   3182 N  NH1  . ARG   B 2 153 ? -32.861 -32.982 25.960  1.00 33.41 ? 539  ARG   B NH1  1 
ATOM   3183 N  NH2  . ARG   B 2 153 ? -31.776 -32.488 27.915  1.00 37.96 ? 539  ARG   B NH2  1 
ATOM   3184 N  N    . GLY   B 2 154 ? -28.603 -38.032 24.092  1.00 31.02 ? 540  GLY   B N    1 
ATOM   3185 C  CA   . GLY   B 2 154 ? -28.125 -39.359 24.411  1.00 30.88 ? 540  GLY   B CA   1 
ATOM   3186 C  C    . GLY   B 2 154 ? -26.939 -39.826 23.595  1.00 34.62 ? 540  GLY   B C    1 
ATOM   3187 O  O    . GLY   B 2 154 ? -26.314 -40.828 23.965  1.00 42.57 ? 540  GLY   B O    1 
ATOM   3188 N  N    . THR   B 2 155 ? -26.615 -39.139 22.501  1.00 34.27 ? 541  THR   B N    1 
ATOM   3189 C  CA   . THR   B 2 155 ? -25.491 -39.543 21.666  1.00 32.78 ? 541  THR   B CA   1 
ATOM   3190 C  C    . THR   B 2 155 ? -24.190 -39.484 22.458  1.00 38.13 ? 541  THR   B C    1 
ATOM   3191 O  O    . THR   B 2 155 ? -23.919 -38.506 23.161  1.00 38.63 ? 541  THR   B O    1 
ATOM   3192 C  CB   . THR   B 2 155 ? -25.398 -38.646 20.431  1.00 30.96 ? 541  THR   B CB   1 
ATOM   3193 O  OG1  . THR   B 2 155 ? -26.638 -38.690 19.712  1.00 28.76 ? 541  THR   B OG1  1 
ATOM   3194 C  CG2  . THR   B 2 155 ? -24.272 -39.107 19.517  1.00 29.56 ? 541  THR   B CG2  1 
ATOM   3195 N  N    . GLN   B 2 156 ? -23.389 -40.541 22.346  1.00 37.32 ? 542  GLN   B N    1 
ATOM   3196 C  CA   . GLN   B 2 156 ? -22.129 -40.652 23.078  1.00 36.42 ? 542  GLN   B CA   1 
ATOM   3197 C  C    . GLN   B 2 156 ? -21.018 -40.062 22.219  1.00 37.38 ? 542  GLN   B C    1 
ATOM   3198 O  O    . GLN   B 2 156 ? -20.449 -40.743 21.363  1.00 38.27 ? 542  GLN   B O    1 
ATOM   3199 C  CB   . GLN   B 2 156 ? -21.845 -42.105 23.440  1.00 36.09 ? 542  GLN   B CB   1 
ATOM   3200 N  N    . VAL   B 2 157 ? -20.708 -38.787 22.448  1.00 37.08 ? 662  VAL   B N    1 
ATOM   3201 C  CA   . VAL   B 2 157 ? -19.636 -38.090 21.743  1.00 32.86 ? 662  VAL   B CA   1 
ATOM   3202 C  C    . VAL   B 2 157 ? -18.886 -37.257 22.775  1.00 39.48 ? 662  VAL   B C    1 
ATOM   3203 O  O    . VAL   B 2 157 ? -19.451 -36.313 23.339  1.00 44.17 ? 662  VAL   B O    1 
ATOM   3204 C  CB   . VAL   B 2 157 ? -20.157 -37.201 20.604  1.00 36.32 ? 662  VAL   B CB   1 
ATOM   3205 C  CG1  . VAL   B 2 157 ? -19.057 -36.277 20.106  1.00 40.08 ? 662  VAL   B CG1  1 
ATOM   3206 C  CG2  . VAL   B 2 157 ? -20.692 -38.054 19.462  1.00 34.15 ? 662  VAL   B CG2  1 
ATOM   3207 N  N    . THR   B 2 158 ? -17.622 -37.605 23.028  1.00 39.27 ? 663  THR   B N    1 
ATOM   3208 C  CA   . THR   B 2 158 ? -16.846 -36.889 24.036  1.00 42.42 ? 663  THR   B CA   1 
ATOM   3209 C  C    . THR   B 2 158 ? -16.597 -35.444 23.622  1.00 46.59 ? 663  THR   B C    1 
ATOM   3210 O  O    . THR   B 2 158 ? -16.697 -34.528 24.450  1.00 47.63 ? 663  THR   B O    1 
ATOM   3211 C  CB   . THR   B 2 158 ? -15.518 -37.602 24.290  1.00 42.24 ? 663  THR   B CB   1 
ATOM   3212 O  OG1  . THR   B 2 158 ? -14.639 -37.390 23.179  1.00 40.84 ? 663  THR   B OG1  1 
ATOM   3213 C  CG2  . THR   B 2 158 ? -15.739 -39.094 24.480  1.00 40.22 ? 663  THR   B CG2  1 
ATOM   3214 N  N    . GLY   B 2 159 ? -16.269 -35.219 22.357  1.00 51.43 ? 664  GLY   B N    1 
ATOM   3215 C  CA   . GLY   B 2 159 ? -16.000 -33.872 21.901  1.00 50.36 ? 664  GLY   B CA   1 
ATOM   3216 C  C    . GLY   B 2 159 ? -15.591 -33.857 20.449  1.00 52.51 ? 664  GLY   B C    1 
ATOM   3217 O  O    . GLY   B 2 159 ? -15.828 -34.813 19.709  1.00 52.01 ? 664  GLY   B O    1 
ATOM   3218 N  N    . LEU   B 2 160 ? -14.969 -32.746 20.046  1.00 42.32 ? 665  LEU   B N    1 
ATOM   3219 C  CA   . LEU   B 2 160 ? -14.488 -32.619 18.675  1.00 40.42 ? 665  LEU   B CA   1 
ATOM   3220 C  C    . LEU   B 2 160 ? -13.402 -33.640 18.365  1.00 31.46 ? 665  LEU   B C    1 
ATOM   3221 O  O    . LEU   B 2 160 ? -13.260 -34.066 17.213  1.00 32.45 ? 665  LEU   B O    1 
ATOM   3222 C  CB   . LEU   B 2 160 ? -13.970 -31.200 18.433  1.00 37.54 ? 665  LEU   B CB   1 
ATOM   3223 C  CG   . LEU   B 2 160 ? -14.305 -30.565 17.082  1.00 33.28 ? 665  LEU   B CG   1 
ATOM   3224 C  CD1  . LEU   B 2 160 ? -15.805 -30.567 16.841  1.00 30.50 ? 665  LEU   B CD1  1 
ATOM   3225 C  CD2  . LEU   B 2 160 ? -13.752 -29.153 17.007  1.00 30.78 ? 665  LEU   B CD2  1 
ATOM   3226 N  N    . SER   B 2 161 ? -12.633 -34.046 19.372  1.00 31.32 ? 666  SER   B N    1 
ATOM   3227 C  CA   . SER   B 2 161 ? -11.562 -35.017 19.200  1.00 36.56 ? 666  SER   B CA   1 
ATOM   3228 C  C    . SER   B 2 161 ? -12.025 -36.455 19.408  1.00 35.98 ? 666  SER   B C    1 
ATOM   3229 O  O    . SER   B 2 161 ? -11.181 -37.349 19.533  1.00 37.56 ? 666  SER   B O    1 
ATOM   3230 C  CB   . SER   B 2 161 ? -10.406 -34.700 20.153  1.00 39.57 ? 666  SER   B CB   1 
ATOM   3231 O  OG   . SER   B 2 161 ? -9.423  -33.903 19.514  1.00 52.30 ? 666  SER   B OG   1 
ATOM   3232 N  N    . ASP   B 2 162 ? -13.334 -36.697 19.453  1.00 36.37 ? 667  ASP   B N    1 
ATOM   3233 C  CA   . ASP   B 2 162 ? -13.834 -38.061 19.555  1.00 32.39 ? 667  ASP   B CA   1 
ATOM   3234 C  C    . ASP   B 2 162 ? -13.405 -38.863 18.333  1.00 34.07 ? 667  ASP   B C    1 
ATOM   3235 O  O    . ASP   B 2 162 ? -13.369 -38.347 17.212  1.00 28.85 ? 667  ASP   B O    1 
ATOM   3236 C  CB   . ASP   B 2 162 ? -15.359 -38.061 19.687  1.00 30.35 ? 667  ASP   B CB   1 
ATOM   3237 C  CG   . ASP   B 2 162 ? -15.908 -39.401 20.152  1.00 34.83 ? 667  ASP   B CG   1 
ATOM   3238 O  OD1  . ASP   B 2 162 ? -15.833 -40.380 19.380  1.00 31.74 ? 667  ASP   B OD1  1 
ATOM   3239 O  OD2  . ASP   B 2 162 ? -16.417 -39.473 21.290  1.00 36.32 ? 667  ASP   B OD2  1 
ATOM   3240 N  N    . LYS   B 2 163 ? -13.075 -40.138 18.557  1.00 29.11 ? 668  LYS   B N    1 
ATOM   3241 C  CA   . LYS   B 2 163 ? -12.576 -40.976 17.472  1.00 31.67 ? 668  LYS   B CA   1 
ATOM   3242 C  C    . LYS   B 2 163 ? -13.605 -41.159 16.364  1.00 33.44 ? 668  LYS   B C    1 
ATOM   3243 O  O    . LYS   B 2 163 ? -13.225 -41.436 15.221  1.00 29.30 ? 668  LYS   B O    1 
ATOM   3244 C  CB   . LYS   B 2 163 ? -12.140 -42.339 18.014  1.00 30.96 ? 668  LYS   B CB   1 
ATOM   3245 C  CG   . LYS   B 2 163 ? -10.655 -42.441 18.362  1.00 43.54 ? 668  LYS   B CG   1 
ATOM   3246 C  CD   . LYS   B 2 163 ? -10.127 -41.170 19.018  1.00 49.19 ? 668  LYS   B CD   1 
ATOM   3247 C  CE   . LYS   B 2 163 ? -8.640  -41.272 19.323  1.00 46.68 ? 668  LYS   B CE   1 
ATOM   3248 N  NZ   . LYS   B 2 163 ? -7.821  -41.408 18.087  1.00 49.27 ? 668  LYS   B NZ   1 
ATOM   3249 N  N    . LYS   B 2 164 ? -14.896 -41.008 16.672  1.00 28.66 ? 669  LYS   B N    1 
ATOM   3250 C  CA   . LYS   B 2 164 ? -15.910 -41.036 15.624  1.00 26.34 ? 669  LYS   B CA   1 
ATOM   3251 C  C    . LYS   B 2 164 ? -15.753 -39.859 14.670  1.00 27.80 ? 669  LYS   B C    1 
ATOM   3252 O  O    . LYS   B 2 164 ? -16.124 -39.959 13.495  1.00 28.44 ? 669  LYS   B O    1 
ATOM   3253 C  CB   . LYS   B 2 164 ? -17.307 -41.041 16.245  1.00 24.61 ? 669  LYS   B CB   1 
ATOM   3254 C  CG   . LYS   B 2 164 ? -17.754 -42.402 16.752  1.00 31.45 ? 669  LYS   B CG   1 
ATOM   3255 C  CD   . LYS   B 2 164 ? -19.167 -42.349 17.304  1.00 35.06 ? 669  LYS   B CD   1 
ATOM   3256 C  CE   . LYS   B 2 164 ? -19.162 -42.018 18.785  1.00 36.61 ? 669  LYS   B CE   1 
ATOM   3257 N  NZ   . LYS   B 2 164 ? -19.513 -43.197 19.624  1.00 38.37 ? 669  LYS   B NZ   1 
ATOM   3258 N  N    . PHE   B 2 165 ? -15.205 -38.743 15.153  1.00 27.33 ? 670  PHE   B N    1 
ATOM   3259 C  CA   . PHE   B 2 165 ? -14.915 -37.589 14.312  1.00 26.15 ? 670  PHE   B CA   1 
ATOM   3260 C  C    . PHE   B 2 165 ? -13.526 -37.668 13.688  1.00 26.70 ? 670  PHE   B C    1 
ATOM   3261 O  O    . PHE   B 2 165 ? -13.357 -37.347 12.506  1.00 23.33 ? 670  PHE   B O    1 
ATOM   3262 C  CB   . PHE   B 2 165 ? -15.033 -36.297 15.126  1.00 26.57 ? 670  PHE   B CB   1 
ATOM   3263 C  CG   . PHE   B 2 165 ? -16.446 -35.906 15.454  1.00 25.07 ? 670  PHE   B CG   1 
ATOM   3264 C  CD1  . PHE   B 2 165 ? -17.465 -36.096 14.537  1.00 25.59 ? 670  PHE   B CD1  1 
ATOM   3265 C  CD2  . PHE   B 2 165 ? -16.753 -35.335 16.678  1.00 24.05 ? 670  PHE   B CD2  1 
ATOM   3266 C  CE1  . PHE   B 2 165 ? -18.765 -35.733 14.839  1.00 24.39 ? 670  PHE   B CE1  1 
ATOM   3267 C  CE2  . PHE   B 2 165 ? -18.049 -34.969 16.984  1.00 27.92 ? 670  PHE   B CE2  1 
ATOM   3268 C  CZ   . PHE   B 2 165 ? -19.056 -35.168 16.063  1.00 27.69 ? 670  PHE   B CZ   1 
ATOM   3269 N  N    . GLN   B 2 166 ? -12.528 -38.095 14.465  1.00 25.83 ? 671  GLN   B N    1 
ATOM   3270 C  CA   . GLN   B 2 166 ? -11.147 -38.096 13.993  1.00 27.82 ? 671  GLN   B CA   1 
ATOM   3271 C  C    . GLN   B 2 166 ? -10.897 -39.224 13.000  1.00 26.64 ? 671  GLN   B C    1 
ATOM   3272 O  O    . GLN   B 2 166 ? -10.325 -39.002 11.927  1.00 26.85 ? 671  GLN   B O    1 
ATOM   3273 C  CB   . GLN   B 2 166 ? -10.191 -38.202 15.182  1.00 32.05 ? 671  GLN   B CB   1 
ATOM   3274 C  CG   . GLN   B 2 166 ? -10.423 -37.148 16.252  1.00 34.12 ? 671  GLN   B CG   1 
ATOM   3275 C  CD   . GLN   B 2 166 ? -9.841  -35.801 15.876  1.00 44.95 ? 671  GLN   B CD   1 
ATOM   3276 O  OE1  . GLN   B 2 166 ? -8.678  -35.702 15.485  1.00 41.30 ? 671  GLN   B OE1  1 
ATOM   3277 N  NE2  . GLN   B 2 166 ? -10.652 -34.754 15.983  1.00 35.35 ? 671  GLN   B NE2  1 
ATOM   3278 N  N    . ARG   B 2 167 ? -11.314 -40.443 13.343  1.00 26.25 ? 672  ARG   B N    1 
ATOM   3279 C  CA   . ARG   B 2 167 ? -11.156 -41.617 12.488  1.00 31.31 ? 672  ARG   B CA   1 
ATOM   3280 C  C    . ARG   B 2 167 ? -12.538 -42.182 12.178  1.00 28.10 ? 672  ARG   B C    1 
ATOM   3281 O  O    . ARG   B 2 167 ? -12.916 -43.246 12.687  1.00 34.50 ? 672  ARG   B O    1 
ATOM   3282 C  CB   . ARG   B 2 167 ? -10.271 -42.667 13.156  1.00 38.08 ? 672  ARG   B CB   1 
ATOM   3283 C  CG   . ARG   B 2 167 ? -8.913  -42.144 13.598  1.00 38.22 ? 672  ARG   B CG   1 
ATOM   3284 C  CD   . ARG   B 2 167 ? -8.090  -43.241 14.252  1.00 39.85 ? 672  ARG   B CD   1 
ATOM   3285 N  NE   . ARG   B 2 167 ? -7.994  -44.423 13.405  1.00 44.20 ? 672  ARG   B NE   1 
ATOM   3286 C  CZ   . ARG   B 2 167 ? -6.989  -44.669 12.576  1.00 45.64 ? 672  ARG   B CZ   1 
ATOM   3287 N  NH1  . ARG   B 2 167 ? -5.961  -43.842 12.473  1.00 41.78 ? 672  ARG   B NH1  1 
ATOM   3288 N  NH2  . ARG   B 2 167 ? -7.016  -45.770 11.831  1.00 40.47 ? 672  ARG   B NH2  1 
ATOM   3289 N  N    . PRO   B 2 168 ? -13.315 -41.499 11.330  1.00 27.21 ? 673  PRO   B N    1 
ATOM   3290 C  CA   . PRO   B 2 168 ? -14.726 -41.882 11.156  1.00 30.34 ? 673  PRO   B CA   1 
ATOM   3291 C  C    . PRO   B 2 168 ? -14.931 -43.230 10.489  1.00 30.75 ? 673  PRO   B C    1 
ATOM   3292 O  O    . PRO   B 2 168 ? -15.994 -43.834 10.681  1.00 31.40 ? 673  PRO   B O    1 
ATOM   3293 C  CB   . PRO   B 2 168 ? -15.294 -40.746 10.293  1.00 24.82 ? 673  PRO   B CB   1 
ATOM   3294 C  CG   . PRO   B 2 168 ? -14.113 -40.200 9.566   1.00 25.81 ? 673  PRO   B CG   1 
ATOM   3295 C  CD   . PRO   B 2 168 ? -12.950 -40.334 10.506  1.00 25.18 ? 673  PRO   B CD   1 
ATOM   3296 N  N    . HIS   B 2 169 ? -13.967 -43.725 9.717   1.00 30.63 ? 674  HIS   B N    1 
ATOM   3297 C  CA   . HIS   B 2 169 ? -14.120 -45.000 9.029   1.00 27.56 ? 674  HIS   B CA   1 
ATOM   3298 C  C    . HIS   B 2 169 ? -13.683 -46.189 9.874   1.00 28.53 ? 674  HIS   B C    1 
ATOM   3299 O  O    . HIS   B 2 169 ? -13.680 -47.319 9.376   1.00 39.83 ? 674  HIS   B O    1 
ATOM   3300 C  CB   . HIS   B 2 169 ? -13.357 -44.982 7.703   1.00 29.53 ? 674  HIS   B CB   1 
ATOM   3301 C  CG   . HIS   B 2 169 ? -14.152 -44.426 6.564   1.00 27.40 ? 674  HIS   B CG   1 
ATOM   3302 N  ND1  . HIS   B 2 169 ? -13.669 -43.444 5.726   1.00 32.14 ? 674  HIS   B ND1  1 
ATOM   3303 C  CD2  . HIS   B 2 169 ? -15.404 -44.706 6.133   1.00 24.05 ? 674  HIS   B CD2  1 
ATOM   3304 C  CE1  . HIS   B 2 169 ? -14.587 -43.150 4.822   1.00 32.00 ? 674  HIS   B CE1  1 
ATOM   3305 N  NE2  . HIS   B 2 169 ? -15.650 -43.901 5.047   1.00 28.89 ? 674  HIS   B NE2  1 
ATOM   3306 N  N    . ASP   B 2 170 ? -13.319 -45.964 11.136  1.00 27.70 ? 675  ASP   B N    1 
ATOM   3307 C  CA   . ASP   B 2 170 ? -13.123 -47.047 12.090  1.00 37.40 ? 675  ASP   B CA   1 
ATOM   3308 C  C    . ASP   B 2 170 ? -14.441 -47.607 12.611  1.00 36.78 ? 675  ASP   B C    1 
ATOM   3309 O  O    . ASP   B 2 170 ? -14.430 -48.457 13.509  1.00 39.93 ? 675  ASP   B O    1 
ATOM   3310 C  CB   . ASP   B 2 170 ? -12.264 -46.571 13.266  1.00 35.43 ? 675  ASP   B CB   1 
ATOM   3311 C  CG   . ASP   B 2 170 ? -10.828 -46.299 12.868  1.00 41.99 ? 675  ASP   B CG   1 
ATOM   3312 O  OD1  . ASP   B 2 170 ? -10.503 -46.456 11.673  1.00 44.43 ? 675  ASP   B OD1  1 
ATOM   3313 O  OD2  . ASP   B 2 170 ? -10.024 -45.934 13.751  1.00 40.36 ? 675  ASP   B OD2  1 
ATOM   3314 N  N    . TYR   B 2 171 ? -15.567 -47.151 12.067  1.00 33.85 ? 676  TYR   B N    1 
ATOM   3315 C  CA   . TYR   B 2 171 ? -16.890 -47.549 12.520  1.00 37.31 ? 676  TYR   B CA   1 
ATOM   3316 C  C    . TYR   B 2 171 ? -17.737 -47.955 11.323  1.00 40.31 ? 676  TYR   B C    1 
ATOM   3317 O  O    . TYR   B 2 171 ? -17.724 -47.286 10.286  1.00 35.64 ? 676  TYR   B O    1 
ATOM   3318 C  CB   . TYR   B 2 171 ? -17.580 -46.411 13.286  1.00 32.83 ? 676  TYR   B CB   1 
ATOM   3319 C  CG   . TYR   B 2 171 ? -16.839 -45.965 14.526  1.00 31.57 ? 676  TYR   B CG   1 
ATOM   3320 C  CD1  . TYR   B 2 171 ? -15.772 -45.078 14.441  1.00 29.78 ? 676  TYR   B CD1  1 
ATOM   3321 C  CD2  . TYR   B 2 171 ? -17.206 -46.429 15.781  1.00 33.68 ? 676  TYR   B CD2  1 
ATOM   3322 C  CE1  . TYR   B 2 171 ? -15.091 -44.670 15.571  1.00 26.13 ? 676  TYR   B CE1  1 
ATOM   3323 C  CE2  . TYR   B 2 171 ? -16.531 -46.024 16.917  1.00 33.16 ? 676  TYR   B CE2  1 
ATOM   3324 C  CZ   . TYR   B 2 171 ? -15.475 -45.145 16.806  1.00 25.46 ? 676  TYR   B CZ   1 
ATOM   3325 O  OH   . TYR   B 2 171 ? -14.802 -44.741 17.934  1.00 32.76 ? 676  TYR   B OH   1 
ATOM   3326 N  N    . SER   B 2 172 ? -18.469 -49.052 11.473  1.00 48.10 ? 677  SER   B N    1 
ATOM   3327 C  CA   . SER   B 2 172 ? -19.372 -49.541 10.432  1.00 49.88 ? 677  SER   B CA   1 
ATOM   3328 C  C    . SER   B 2 172 ? -20.779 -49.649 10.998  1.00 47.21 ? 677  SER   B C    1 
ATOM   3329 O  O    . SER   B 2 172 ? -21.038 -50.534 11.835  1.00 53.46 ? 677  SER   B O    1 
ATOM   3330 C  CB   . SER   B 2 172 ? -18.904 -50.893 9.894   1.00 46.62 ? 677  SER   B CB   1 
ATOM   3331 O  OG   . SER   B 2 172 ? -17.736 -50.752 9.105   1.00 55.85 ? 677  SER   B OG   1 
ATOM   3332 N  N    . PRO   B 2 173 ? -21.720 -48.790 10.587  1.00 30.28 ? 678  PRO   B N    1 
ATOM   3333 C  CA   . PRO   B 2 173 ? -21.576 -47.679 9.632   1.00 35.74 ? 678  PRO   B CA   1 
ATOM   3334 C  C    . PRO   B 2 173 ? -20.832 -46.490 10.235  1.00 31.87 ? 678  PRO   B C    1 
ATOM   3335 O  O    . PRO   B 2 173 ? -20.844 -46.295 11.447  1.00 29.60 ? 678  PRO   B O    1 
ATOM   3336 C  CB   . PRO   B 2 173 ? -23.035 -47.319 9.288   1.00 32.64 ? 678  PRO   B CB   1 
ATOM   3337 C  CG   . PRO   B 2 173 ? -23.873 -48.470 9.788   1.00 36.74 ? 678  PRO   B CG   1 
ATOM   3338 C  CD   . PRO   B 2 173 ? -23.124 -48.986 10.974  1.00 39.12 ? 678  PRO   B CD   1 
ATOM   3339 N  N    . PRO   B 2 174 ? -20.174 -45.680 9.410   1.00 32.13 ? 679  PRO   B N    1 
ATOM   3340 C  CA   . PRO   B 2 174 ? -19.431 -44.534 9.940   1.00 23.25 ? 679  PRO   B CA   1 
ATOM   3341 C  C    . PRO   B 2 174 ? -20.359 -43.438 10.438  1.00 27.38 ? 679  PRO   B C    1 
ATOM   3342 O  O    . PRO   B 2 174 ? -21.518 -43.324 10.032  1.00 26.07 ? 679  PRO   B O    1 
ATOM   3343 C  CB   . PRO   B 2 174 ? -18.608 -44.060 8.738   1.00 28.15 ? 679  PRO   B CB   1 
ATOM   3344 C  CG   . PRO   B 2 174 ? -19.405 -44.493 7.555   1.00 27.21 ? 679  PRO   B CG   1 
ATOM   3345 C  CD   . PRO   B 2 174 ? -20.038 -45.799 7.947   1.00 28.58 ? 679  PRO   B CD   1 
ATOM   3346 N  N    . PHE   B 2 175 ? -19.822 -42.624 11.343  1.00 26.35 ? 680  PHE   B N    1 
ATOM   3347 C  CA   . PHE   B 2 175 ? -20.569 -41.497 11.884  1.00 24.09 ? 680  PHE   B CA   1 
ATOM   3348 C  C    . PHE   B 2 175 ? -20.829 -40.463 10.796  1.00 22.45 ? 680  PHE   B C    1 
ATOM   3349 O  O    . PHE   B 2 175 ? -19.936 -40.120 10.016  1.00 19.73 ? 680  PHE   B O    1 
ATOM   3350 C  CB   . PHE   B 2 175 ? -19.796 -40.862 13.041  1.00 22.65 ? 680  PHE   B CB   1 
ATOM   3351 C  CG   . PHE   B 2 175 ? -20.668 -40.357 14.157  1.00 25.17 ? 680  PHE   B CG   1 
ATOM   3352 C  CD1  . PHE   B 2 175 ? -21.644 -41.167 14.714  1.00 24.47 ? 680  PHE   B CD1  1 
ATOM   3353 C  CD2  . PHE   B 2 175 ? -20.501 -39.076 14.657  1.00 24.57 ? 680  PHE   B CD2  1 
ATOM   3354 C  CE1  . PHE   B 2 175 ? -22.442 -40.704 15.746  1.00 27.58 ? 680  PHE   B CE1  1 
ATOM   3355 C  CE2  . PHE   B 2 175 ? -21.295 -38.608 15.688  1.00 22.66 ? 680  PHE   B CE2  1 
ATOM   3356 C  CZ   . PHE   B 2 175 ? -22.267 -39.422 16.232  1.00 27.09 ? 680  PHE   B CZ   1 
ATOM   3357 N  N    . ARG   B 2 176 ? -22.062 -39.969 10.741  1.00 19.26 ? 681  ARG   B N    1 
ATOM   3358 C  CA   . ARG   B 2 176 ? -22.460 -38.960 9.767   1.00 26.81 ? 681  ARG   B CA   1 
ATOM   3359 C  C    . ARG   B 2 176 ? -22.519 -37.605 10.459  1.00 22.69 ? 681  ARG   B C    1 
ATOM   3360 O  O    . ARG   B 2 176 ? -23.323 -37.406 11.375  1.00 18.22 ? 681  ARG   B O    1 
ATOM   3361 C  CB   . ARG   B 2 176 ? -23.812 -39.300 9.142   1.00 24.06 ? 681  ARG   B CB   1 
ATOM   3362 C  CG   . ARG   B 2 176 ? -23.855 -40.646 8.442   1.00 28.65 ? 681  ARG   B CG   1 
ATOM   3363 C  CD   . ARG   B 2 176 ? -25.290 -41.072 8.206   1.00 25.28 ? 681  ARG   B CD   1 
ATOM   3364 N  NE   . ARG   B 2 176 ? -26.065 -41.008 9.438   1.00 25.76 ? 681  ARG   B NE   1 
ATOM   3365 C  CZ   . ARG   B 2 176 ? -27.389 -40.978 9.492   1.00 35.32 ? 681  ARG   B CZ   1 
ATOM   3366 N  NH1  . ARG   B 2 176 ? -28.127 -41.022 8.395   1.00 34.11 ? 681  ARG   B NH1  1 
ATOM   3367 N  NH2  . ARG   B 2 176 ? -27.987 -40.893 10.676  1.00 27.82 ? 681  ARG   B NH2  1 
ATOM   3368 N  N    . PHE   B 2 177 ? -21.675 -36.676 10.019  1.00 18.88 ? 682  PHE   B N    1 
ATOM   3369 C  CA   . PHE   B 2 177 ? -21.621 -35.357 10.626  1.00 19.64 ? 682  PHE   B CA   1 
ATOM   3370 C  C    . PHE   B 2 177 ? -21.150 -34.350 9.590   1.00 20.84 ? 682  PHE   B C    1 
ATOM   3371 O  O    . PHE   B 2 177 ? -20.337 -34.668 8.719   1.00 17.39 ? 682  PHE   B O    1 
ATOM   3372 C  CB   . PHE   B 2 177 ? -20.697 -35.335 11.850  1.00 20.80 ? 682  PHE   B CB   1 
ATOM   3373 C  CG   . PHE   B 2 177 ? -19.305 -35.827 11.570  1.00 24.43 ? 682  PHE   B CG   1 
ATOM   3374 C  CD1  . PHE   B 2 177 ? -19.013 -37.182 11.612  1.00 22.10 ? 682  PHE   B CD1  1 
ATOM   3375 C  CD2  . PHE   B 2 177 ? -18.286 -34.937 11.273  1.00 20.48 ? 682  PHE   B CD2  1 
ATOM   3376 C  CE1  . PHE   B 2 177 ? -17.735 -37.639 11.359  1.00 19.37 ? 682  PHE   B CE1  1 
ATOM   3377 C  CE2  . PHE   B 2 177 ? -17.004 -35.389 11.018  1.00 22.33 ? 682  PHE   B CE2  1 
ATOM   3378 C  CZ   . PHE   B 2 177 ? -16.730 -36.742 11.061  1.00 20.29 ? 682  PHE   B CZ   1 
ATOM   3379 N  N    . GLY   B 2 178 ? -21.671 -33.131 9.696   1.00 21.43 ? 683  GLY   B N    1 
ATOM   3380 C  CA   . GLY   B 2 178 ? -21.288 -32.077 8.780   1.00 19.96 ? 683  GLY   B CA   1 
ATOM   3381 C  C    . GLY   B 2 178 ? -21.502 -30.716 9.405   1.00 17.05 ? 683  GLY   B C    1 
ATOM   3382 O  O    . GLY   B 2 178 ? -21.954 -30.590 10.545  1.00 19.19 ? 683  GLY   B O    1 
ATOM   3383 N  N    . THR   B 2 179 ? -21.164 -29.689 8.632   1.00 15.22 ? 684  THR   B N    1 
ATOM   3384 C  CA   . THR   B 2 179 ? -21.301 -28.302 9.044   1.00 18.07 ? 684  THR   B CA   1 
ATOM   3385 C  C    . THR   B 2 179 ? -21.889 -27.500 7.891   1.00 14.58 ? 684  THR   B C    1 
ATOM   3386 O  O    . THR   B 2 179 ? -22.189 -28.035 6.819   1.00 16.68 ? 684  THR   B O    1 
ATOM   3387 C  CB   . THR   B 2 179 ? -19.951 -27.709 9.470   1.00 16.14 ? 684  THR   B CB   1 
ATOM   3388 O  OG1  . THR   B 2 179 ? -20.157 -26.401 10.019  1.00 15.67 ? 684  THR   B OG1  1 
ATOM   3389 C  CG2  . THR   B 2 179 ? -19.014 -27.606 8.276   1.00 13.54 ? 684  THR   B CG2  1 
ATOM   3390 N  N    . VAL   B 2 180 ? -22.060 -26.201 8.119   1.00 15.71 ? 685  VAL   B N    1 
ATOM   3391 C  CA   . VAL   B 2 180 ? -22.382 -25.253 7.059   1.00 17.69 ? 685  VAL   B CA   1 
ATOM   3392 C  C    . VAL   B 2 180 ? -21.062 -24.664 6.561   1.00 18.05 ? 685  VAL   B C    1 
ATOM   3393 O  O    . VAL   B 2 180 ? -20.406 -23.930 7.318   1.00 20.65 ? 685  VAL   B O    1 
ATOM   3394 C  CB   . VAL   B 2 180 ? -23.333 -24.156 7.551   1.00 17.83 ? 685  VAL   B CB   1 
ATOM   3395 C  CG1  . VAL   B 2 180 ? -23.658 -23.189 6.421   1.00 14.97 ? 685  VAL   B CG1  1 
ATOM   3396 C  CG2  . VAL   B 2 180 ? -24.603 -24.773 8.113   1.00 16.15 ? 685  VAL   B CG2  1 
ATOM   3397 N  N    . PRO   B 2 181 ? -20.645 -24.952 5.332   1.00 16.70 ? 686  PRO   B N    1 
ATOM   3398 C  CA   . PRO   B 2 181 ? -19.282 -24.608 4.911   1.00 15.23 ? 686  PRO   B CA   1 
ATOM   3399 C  C    . PRO   B 2 181 ? -19.085 -23.106 4.761   1.00 15.36 ? 686  PRO   B C    1 
ATOM   3400 O  O    . PRO   B 2 181 ? -20.008 -22.299 4.894   1.00 14.23 ? 686  PRO   B O    1 
ATOM   3401 C  CB   . PRO   B 2 181 ? -19.139 -25.323 3.563   1.00 20.12 ? 686  PRO   B CB   1 
ATOM   3402 C  CG   . PRO   B 2 181 ? -20.541 -25.432 3.050   1.00 14.26 ? 686  PRO   B CG   1 
ATOM   3403 C  CD   . PRO   B 2 181 ? -21.407 -25.623 4.265   1.00 14.49 ? 686  PRO   B CD   1 
ATOM   3404 N  N    . ASN   B 2 182 ? -17.829 -22.746 4.489   1.00 18.63 ? 687  ASN   B N    1 
ATOM   3405 C  CA   . ASN   B 2 182 ? -17.353 -21.406 4.157   1.00 15.39 ? 687  ASN   B CA   1 
ATOM   3406 C  C    . ASN   B 2 182 ? -17.343 -20.452 5.346   1.00 19.18 ? 687  ASN   B C    1 
ATOM   3407 O  O    . ASN   B 2 182 ? -17.033 -19.268 5.165   1.00 17.36 ? 687  ASN   B O    1 
ATOM   3408 C  CB   . ASN   B 2 182 ? -18.159 -20.771 3.014   1.00 15.94 ? 687  ASN   B CB   1 
ATOM   3409 C  CG   . ASN   B 2 182 ? -18.213 -21.655 1.784   1.00 24.70 ? 687  ASN   B CG   1 
ATOM   3410 O  OD1  . ASN   B 2 182 ? -17.299 -22.441 1.529   1.00 19.54 ? 687  ASN   B OD1  1 
ATOM   3411 N  ND2  . ASN   B 2 182 ? -19.290 -21.538 1.018   1.00 23.14 ? 687  ASN   B ND2  1 
ATOM   3412 N  N    . GLY   B 2 183 ? -17.657 -20.920 6.555   1.00 16.81 ? 688  GLY   B N    1 
ATOM   3413 C  CA   . GLY   B 2 183 ? -17.599 -20.098 7.742   1.00 15.82 ? 688  GLY   B CA   1 
ATOM   3414 C  C    . GLY   B 2 183 ? -16.366 -20.384 8.582   1.00 15.07 ? 688  GLY   B C    1 
ATOM   3415 O  O    . GLY   B 2 183 ? -15.477 -21.151 8.206   1.00 13.53 ? 688  GLY   B O    1 
ATOM   3416 N  N    . SER   B 2 184 ? -16.324 -19.747 9.755   1.00 14.35 ? 689  SER   B N    1 
ATOM   3417 C  CA   . SER   B 2 184 ? -15.173 -19.905 10.639  1.00 13.25 ? 689  SER   B CA   1 
ATOM   3418 C  C    . SER   B 2 184 ? -15.051 -21.332 11.158  1.00 13.59 ? 689  SER   B C    1 
ATOM   3419 O  O    . SER   B 2 184 ? -13.943 -21.786 11.469  1.00 14.06 ? 689  SER   B O    1 
ATOM   3420 C  CB   . SER   B 2 184 ? -15.268 -18.925 11.809  1.00 15.85 ? 689  SER   B CB   1 
ATOM   3421 O  OG   . SER   B 2 184 ? -16.346 -19.255 12.668  1.00 12.99 ? 689  SER   B OG   1 
ATOM   3422 N  N    . THR   B 2 185 ? -16.170 -22.055 11.254  1.00 15.53 ? 690  THR   B N    1 
ATOM   3423 C  CA   . THR   B 2 185 ? -16.130 -23.416 11.782  1.00 16.01 ? 690  THR   B CA   1 
ATOM   3424 C  C    . THR   B 2 185 ? -15.421 -24.362 10.820  1.00 15.99 ? 690  THR   B C    1 
ATOM   3425 O  O    . THR   B 2 185 ? -14.531 -25.120 11.226  1.00 16.30 ? 690  THR   B O    1 
ATOM   3426 C  CB   . THR   B 2 185 ? -17.546 -23.908 12.079  1.00 13.92 ? 690  THR   B CB   1 
ATOM   3427 O  OG1  . THR   B 2 185 ? -18.095 -23.159 13.172  1.00 11.76 ? 690  THR   B OG1  1 
ATOM   3428 C  CG2  . THR   B 2 185 ? -17.533 -25.385 12.444  1.00 16.24 ? 690  THR   B CG2  1 
ATOM   3429 N  N    . GLU   B 2 186 ? -15.801 -24.339 9.539   1.00 13.74 ? 691  GLU   B N    1 
ATOM   3430 C  CA   . GLU   B 2 186 ? -15.132 -25.198 8.567   1.00 17.42 ? 691  GLU   B CA   1 
ATOM   3431 C  C    . GLU   B 2 186 ? -13.661 -24.832 8.434   1.00 18.81 ? 691  GLU   B C    1 
ATOM   3432 O  O    . GLU   B 2 186 ? -12.805 -25.713 8.286   1.00 16.01 ? 691  GLU   B O    1 
ATOM   3433 C  CB   . GLU   B 2 186 ? -15.817 -25.112 7.203   1.00 14.58 ? 691  GLU   B CB   1 
ATOM   3434 C  CG   . GLU   B 2 186 ? -15.250 -26.114 6.203   1.00 15.79 ? 691  GLU   B CG   1 
ATOM   3435 C  CD   . GLU   B 2 186 ? -15.693 -25.864 4.775   1.00 20.49 ? 691  GLU   B CD   1 
ATOM   3436 O  OE1  . GLU   B 2 186 ? -16.059 -24.715 4.451   1.00 19.07 ? 691  GLU   B OE1  1 
ATOM   3437 O  OE2  . GLU   B 2 186 ? -15.661 -26.819 3.972   1.00 21.76 ? 691  GLU   B OE2  1 
ATOM   3438 N  N    . ARG   B 2 187 ? -13.349 -23.533 8.478   1.00 14.85 ? 692  ARG   B N    1 
ATOM   3439 C  CA   . ARG   B 2 187 ? -11.959 -23.097 8.394   1.00 16.75 ? 692  ARG   B CA   1 
ATOM   3440 C  C    . ARG   B 2 187 ? -11.123 -23.715 9.505   1.00 22.15 ? 692  ARG   B C    1 
ATOM   3441 O  O    . ARG   B 2 187 ? -10.003 -24.183 9.265   1.00 21.14 ? 692  ARG   B O    1 
ATOM   3442 C  CB   . ARG   B 2 187 ? -11.885 -21.571 8.452   1.00 17.59 ? 692  ARG   B CB   1 
ATOM   3443 C  CG   . ARG   B 2 187 ? -10.490 -21.008 8.237   1.00 22.41 ? 692  ARG   B CG   1 
ATOM   3444 C  CD   . ARG   B 2 187 ? -9.914  -21.464 6.909   1.00 24.26 ? 692  ARG   B CD   1 
ATOM   3445 N  NE   . ARG   B 2 187 ? -8.558  -20.973 6.701   1.00 27.63 ? 692  ARG   B NE   1 
ATOM   3446 C  CZ   . ARG   B 2 187 ? -7.637  -21.603 5.985   1.00 41.50 ? 692  ARG   B CZ   1 
ATOM   3447 N  NH1  . ARG   B 2 187 ? -7.893  -22.758 5.393   1.00 40.66 ? 692  ARG   B NH1  1 
ATOM   3448 N  NH2  . ARG   B 2 187 ? -6.430  -21.059 5.858   1.00 49.03 ? 692  ARG   B NH2  1 
ATOM   3449 N  N    . ASN   B 2 188 ? -11.654 -23.732 10.730  1.00 19.17 ? 693  ASN   B N    1 
ATOM   3450 C  CA   . ASN   B 2 188 ? -10.930 -24.332 11.845  1.00 16.57 ? 693  ASN   B CA   1 
ATOM   3451 C  C    . ASN   B 2 188 ? -10.771 -25.835 11.657  1.00 17.27 ? 693  ASN   B C    1 
ATOM   3452 O  O    . ASN   B 2 188 ? -9.705  -26.392 11.946  1.00 16.86 ? 693  ASN   B O    1 
ATOM   3453 C  CB   . ASN   B 2 188 ? -11.649 -24.025 13.160  1.00 15.47 ? 693  ASN   B CB   1 
ATOM   3454 C  CG   . ASN   B 2 188 ? -10.907 -24.559 14.371  1.00 21.74 ? 693  ASN   B CG   1 
ATOM   3455 O  OD1  . ASN   B 2 188 ? -11.043 -25.730 14.730  1.00 16.33 ? 693  ASN   B OD1  1 
ATOM   3456 N  ND2  . ASN   B 2 188 ? -10.125 -23.700 15.014  1.00 14.16 ? 693  ASN   B ND2  1 
ATOM   3457 N  N    . ILE   B 2 189 ? -11.816 -26.508 11.170  1.00 17.02 ? 694  ILE   B N    1 
ATOM   3458 C  CA   . ILE   B 2 189 ? -11.743 -27.953 10.979  1.00 18.57 ? 694  ILE   B CA   1 
ATOM   3459 C  C    . ILE   B 2 189 ? -10.784 -28.292 9.846   1.00 15.97 ? 694  ILE   B C    1 
ATOM   3460 O  O    . ILE   B 2 189 ? -10.061 -29.294 9.903   1.00 17.04 ? 694  ILE   B O    1 
ATOM   3461 C  CB   . ILE   B 2 189 ? -13.146 -28.532 10.727  1.00 19.48 ? 694  ILE   B CB   1 
ATOM   3462 C  CG1  . ILE   B 2 189 ? -14.057 -28.268 11.926  1.00 18.53 ? 694  ILE   B CG1  1 
ATOM   3463 C  CG2  . ILE   B 2 189 ? -13.064 -30.029 10.452  1.00 20.77 ? 694  ILE   B CG2  1 
ATOM   3464 C  CD1  . ILE   B 2 189 ? -15.451 -28.839 11.773  1.00 23.62 ? 694  ILE   B CD1  1 
ATOM   3465 N  N    . ARG   B 2 190 ? -10.754 -27.459 8.802   1.00 19.06 ? 695  ARG   B N    1 
ATOM   3466 C  CA   . ARG   B 2 190 ? -9.865  -27.716 7.673   1.00 21.07 ? 695  ARG   B CA   1 
ATOM   3467 C  C    . ARG   B 2 190 ? -8.402  -27.661 8.093   1.00 22.68 ? 695  ARG   B C    1 
ATOM   3468 O  O    . ARG   B 2 190 ? -7.574  -28.427 7.585   1.00 21.06 ? 695  ARG   B O    1 
ATOM   3469 C  CB   . ARG   B 2 190 ? -10.141 -26.714 6.552   1.00 21.59 ? 695  ARG   B CB   1 
ATOM   3470 C  CG   . ARG   B 2 190 ? -9.251  -26.876 5.329   1.00 20.85 ? 695  ARG   B CG   1 
ATOM   3471 C  CD   . ARG   B 2 190 ? -9.484  -25.764 4.317   1.00 22.31 ? 695  ARG   B CD   1 
ATOM   3472 N  NE   . ARG   B 2 190 ? -10.852 -25.753 3.813   1.00 35.01 ? 695  ARG   B NE   1 
ATOM   3473 C  CZ   . ARG   B 2 190 ? -11.267 -26.434 2.753   1.00 36.36 ? 695  ARG   B CZ   1 
ATOM   3474 N  NH1  . ARG   B 2 190 ? -10.444 -27.206 2.063   1.00 30.01 ? 695  ARG   B NH1  1 
ATOM   3475 N  NH2  . ARG   B 2 190 ? -12.540 -26.342 2.379   1.00 29.39 ? 695  ARG   B NH2  1 
ATOM   3476 N  N    . ASN   B 2 191 ? -8.064  -26.773 9.031   1.00 21.63 ? 696  ASN   B N    1 
ATOM   3477 C  CA   . ASN   B 2 191 ? -6.675  -26.640 9.454   1.00 20.08 ? 696  ASN   B CA   1 
ATOM   3478 C  C    . ASN   B 2 191 ? -6.297  -27.645 10.536  1.00 21.17 ? 696  ASN   B C    1 
ATOM   3479 O  O    . ASN   B 2 191 ? -5.156  -28.118 10.561  1.00 20.71 ? 696  ASN   B O    1 
ATOM   3480 C  CB   . ASN   B 2 191 ? -6.411  -25.221 9.956   1.00 21.95 ? 696  ASN   B CB   1 
ATOM   3481 C  CG   . ASN   B 2 191 ? -6.538  -24.181 8.860   1.00 40.83 ? 696  ASN   B CG   1 
ATOM   3482 O  OD1  . ASN   B 2 191 ? -6.838  -23.017 9.122   1.00 38.69 ? 696  ASN   B OD1  1 
ATOM   3483 N  ND2  . ASN   B 2 191 ? -6.299  -24.595 7.623   1.00 38.47 ? 696  ASN   B ND2  1 
ATOM   3484 N  N    . ASN   B 2 192 ? -7.228  -27.988 11.425  1.00 18.29 ? 697  ASN   B N    1 
ATOM   3485 C  CA   . ASN   B 2 192 ? -6.899  -28.821 12.576  1.00 18.76 ? 697  ASN   B CA   1 
ATOM   3486 C  C    . ASN   B 2 192 ? -7.054  -30.312 12.300  1.00 22.36 ? 697  ASN   B C    1 
ATOM   3487 O  O    . ASN   B 2 192 ? -6.221  -31.109 12.744  1.00 25.61 ? 697  ASN   B O    1 
ATOM   3488 C  CB   . ASN   B 2 192 ? -7.766  -28.427 13.776  1.00 20.66 ? 697  ASN   B CB   1 
ATOM   3489 C  CG   . ASN   B 2 192 ? -7.355  -27.099 14.376  1.00 21.05 ? 697  ASN   B CG   1 
ATOM   3490 O  OD1  . ASN   B 2 192 ? -6.180  -26.733 14.352  1.00 19.94 ? 697  ASN   B OD1  1 
ATOM   3491 N  ND2  . ASN   B 2 192 ? -8.321  -26.372 14.923  1.00 18.92 ? 697  ASN   B ND2  1 
ATOM   3492 N  N    . TYR   B 2 193 ? -8.098  -30.710 11.577  1.00 21.19 ? 698  TYR   B N    1 
ATOM   3493 C  CA   . TYR   B 2 193 ? -8.427  -32.120 11.366  1.00 23.30 ? 698  TYR   B CA   1 
ATOM   3494 C  C    . TYR   B 2 193 ? -8.583  -32.381 9.874   1.00 21.60 ? 698  TYR   B C    1 
ATOM   3495 O  O    . TYR   B 2 193 ? -9.703  -32.386 9.344   1.00 20.89 ? 698  TYR   B O    1 
ATOM   3496 C  CB   . TYR   B 2 193 ? -9.689  -32.499 12.140  1.00 23.36 ? 698  TYR   B CB   1 
ATOM   3497 C  CG   . TYR   B 2 193 ? -9.707  -31.945 13.548  1.00 25.61 ? 698  TYR   B CG   1 
ATOM   3498 C  CD1  . TYR   B 2 193 ? -8.848  -32.441 14.520  1.00 21.47 ? 698  TYR   B CD1  1 
ATOM   3499 C  CD2  . TYR   B 2 193 ? -10.570 -30.914 13.901  1.00 20.35 ? 698  TYR   B CD2  1 
ATOM   3500 C  CE1  . TYR   B 2 193 ? -8.854  -31.935 15.806  1.00 27.02 ? 698  TYR   B CE1  1 
ATOM   3501 C  CE2  . TYR   B 2 193 ? -10.582 -30.401 15.186  1.00 25.55 ? 698  TYR   B CE2  1 
ATOM   3502 C  CZ   . TYR   B 2 193 ? -9.722  -30.916 16.134  1.00 31.21 ? 698  TYR   B CZ   1 
ATOM   3503 O  OH   . TYR   B 2 193 ? -9.730  -30.410 17.413  1.00 32.11 ? 698  TYR   B OH   1 
ATOM   3504 N  N    . PRO   B 2 194 ? -7.472  -32.604 9.164   1.00 21.07 ? 699  PRO   B N    1 
ATOM   3505 C  CA   . PRO   B 2 194 ? -7.567  -32.807 7.704   1.00 20.56 ? 699  PRO   B CA   1 
ATOM   3506 C  C    . PRO   B 2 194 ? -8.431  -33.993 7.302   1.00 21.60 ? 699  PRO   B C    1 
ATOM   3507 O  O    . PRO   B 2 194 ? -9.314  -33.846 6.447   1.00 21.65 ? 699  PRO   B O    1 
ATOM   3508 C  CB   . PRO   B 2 194 ? -6.101  -32.995 7.290   1.00 21.50 ? 699  PRO   B CB   1 
ATOM   3509 C  CG   . PRO   B 2 194 ? -5.316  -32.290 8.348   1.00 21.40 ? 699  PRO   B CG   1 
ATOM   3510 C  CD   . PRO   B 2 194 ? -6.076  -32.506 9.623   1.00 19.49 ? 699  PRO   B CD   1 
ATOM   3511 N  N    . TYR   B 2 195 ? -8.197  -35.172 7.887   1.00 22.87 ? 700  TYR   B N    1 
ATOM   3512 C  CA   . TYR   B 2 195 ? -8.986  -36.343 7.513   1.00 22.85 ? 700  TYR   B CA   1 
ATOM   3513 C  C    . TYR   B 2 195 ? -10.457 -36.146 7.847   1.00 20.12 ? 700  TYR   B C    1 
ATOM   3514 O  O    . TYR   B 2 195 ? -11.336 -36.504 7.054   1.00 22.29 ? 700  TYR   B O    1 
ATOM   3515 C  CB   . TYR   B 2 195 ? -8.450  -37.595 8.206   1.00 19.47 ? 700  TYR   B CB   1 
ATOM   3516 C  CG   . TYR   B 2 195 ? -9.074  -38.870 7.684   1.00 21.20 ? 700  TYR   B CG   1 
ATOM   3517 C  CD1  . TYR   B 2 195 ? -8.537  -39.528 6.586   1.00 21.53 ? 700  TYR   B CD1  1 
ATOM   3518 C  CD2  . TYR   B 2 195 ? -10.210 -39.407 8.278   1.00 26.01 ? 700  TYR   B CD2  1 
ATOM   3519 C  CE1  . TYR   B 2 195 ? -9.107  -40.689 6.099   1.00 22.09 ? 700  TYR   B CE1  1 
ATOM   3520 C  CE2  . TYR   B 2 195 ? -10.787 -40.568 7.797   1.00 27.79 ? 700  TYR   B CE2  1 
ATOM   3521 C  CZ   . TYR   B 2 195 ? -10.232 -41.204 6.708   1.00 23.60 ? 700  TYR   B CZ   1 
ATOM   3522 O  OH   . TYR   B 2 195 ? -10.803 -42.360 6.225   1.00 30.91 ? 700  TYR   B OH   1 
ATOM   3523 N  N    . MET   B 2 196 ? -10.742 -35.586 9.023   1.00 20.42 ? 701  MET   B N    1 
ATOM   3524 C  CA   . MET   B 2 196 ? -12.121 -35.296 9.397   1.00 24.04 ? 701  MET   B CA   1 
ATOM   3525 C  C    . MET   B 2 196 ? -12.770 -34.332 8.412   1.00 22.14 ? 701  MET   B C    1 
ATOM   3526 O  O    . MET   B 2 196 ? -13.940 -34.498 8.048   1.00 21.80 ? 701  MET   B O    1 
ATOM   3527 C  CB   . MET   B 2 196 ? -12.155 -34.726 10.814  1.00 23.48 ? 701  MET   B CB   1 
ATOM   3528 C  CG   . MET   B 2 196 ? -13.504 -34.218 11.274  1.00 21.64 ? 701  MET   B CG   1 
ATOM   3529 S  SD   . MET   B 2 196 ? -13.382 -33.600 12.962  1.00 33.86 ? 701  MET   B SD   1 
ATOM   3530 C  CE   . MET   B 2 196 ? -15.036 -32.976 13.214  1.00 22.59 ? 701  MET   B CE   1 
ATOM   3531 N  N    . HIS   B 2 197 ? -12.020 -33.324 7.957   1.00 18.45 ? 702  HIS   B N    1 
ATOM   3532 C  CA   . HIS   B 2 197 ? -12.598 -32.315 7.075   1.00 19.25 ? 702  HIS   B CA   1 
ATOM   3533 C  C    . HIS   B 2 197 ? -12.949 -32.893 5.709   1.00 24.25 ? 702  HIS   B C    1 
ATOM   3534 O  O    . HIS   B 2 197 ? -14.026 -32.609 5.171   1.00 24.84 ? 702  HIS   B O    1 
ATOM   3535 C  CB   . HIS   B 2 197 ? -11.640 -31.137 6.917   1.00 20.09 ? 702  HIS   B CB   1 
ATOM   3536 C  CG   . HIS   B 2 197 ? -12.044 -30.180 5.839   1.00 18.59 ? 702  HIS   B CG   1 
ATOM   3537 N  ND1  . HIS   B 2 197 ? -13.047 -29.250 6.006   1.00 20.63 ? 702  HIS   B ND1  1 
ATOM   3538 C  CD2  . HIS   B 2 197 ? -11.591 -30.021 4.573   1.00 19.45 ? 702  HIS   B CD2  1 
ATOM   3539 C  CE1  . HIS   B 2 197 ? -13.189 -28.553 4.893   1.00 24.60 ? 702  HIS   B CE1  1 
ATOM   3540 N  NE2  . HIS   B 2 197 ? -12.318 -29.002 4.007   1.00 26.59 ? 702  HIS   B NE2  1 
ATOM   3541 N  N    . GLN   B 2 198 ? -12.054 -33.695 5.124   1.00 18.80 ? 703  GLN   B N    1 
ATOM   3542 C  CA   . GLN   B 2 198 ? -12.326 -34.244 3.799   1.00 23.22 ? 703  GLN   B CA   1 
ATOM   3543 C  C    . GLN   B 2 198 ? -13.452 -35.270 3.836   1.00 22.06 ? 703  GLN   B C    1 
ATOM   3544 O  O    . GLN   B 2 198 ? -14.175 -35.429 2.846   1.00 26.41 ? 703  GLN   B O    1 
ATOM   3545 C  CB   . GLN   B 2 198 ? -11.054 -34.855 3.205   1.00 24.94 ? 703  GLN   B CB   1 
ATOM   3546 C  CG   . GLN   B 2 198 ? -10.533 -36.092 3.925   1.00 23.21 ? 703  GLN   B CG   1 
ATOM   3547 C  CD   . GLN   B 2 198 ? -11.121 -37.380 3.380   1.00 22.24 ? 703  GLN   B CD   1 
ATOM   3548 O  OE1  . GLN   B 2 198 ? -11.359 -37.506 2.179   1.00 26.52 ? 703  GLN   B OE1  1 
ATOM   3549 N  NE2  . GLN   B 2 198 ? -11.360 -38.343 4.263   1.00 21.46 ? 703  GLN   B NE2  1 
ATOM   3550 N  N    . TYR   B 2 199 ? -13.612 -35.976 4.957   1.00 20.52 ? 704  TYR   B N    1 
ATOM   3551 C  CA   . TYR   B 2 199 ? -14.747 -36.879 5.106   1.00 23.26 ? 704  TYR   B CA   1 
ATOM   3552 C  C    . TYR   B 2 199 ? -16.043 -36.107 5.309   1.00 20.52 ? 704  TYR   B C    1 
ATOM   3553 O  O    . TYR   B 2 199 ? -17.123 -36.604 4.969   1.00 21.04 ? 704  TYR   B O    1 
ATOM   3554 C  CB   . TYR   B 2 199 ? -14.507 -37.833 6.280   1.00 21.08 ? 704  TYR   B CB   1 
ATOM   3555 C  CG   . TYR   B 2 199 ? -15.717 -38.656 6.677   1.00 21.17 ? 704  TYR   B CG   1 
ATOM   3556 C  CD1  . TYR   B 2 199 ? -15.974 -39.880 6.075   1.00 20.82 ? 704  TYR   B CD1  1 
ATOM   3557 C  CD2  . TYR   B 2 199 ? -16.598 -38.212 7.659   1.00 21.61 ? 704  TYR   B CD2  1 
ATOM   3558 C  CE1  . TYR   B 2 199 ? -17.075 -40.636 6.432   1.00 19.39 ? 704  TYR   B CE1  1 
ATOM   3559 C  CE2  . TYR   B 2 199 ? -17.704 -38.961 8.020   1.00 16.69 ? 704  TYR   B CE2  1 
ATOM   3560 C  CZ   . TYR   B 2 199 ? -17.935 -40.173 7.404   1.00 21.64 ? 704  TYR   B CZ   1 
ATOM   3561 O  OH   . TYR   B 2 199 ? -19.031 -40.924 7.761   1.00 23.72 ? 704  TYR   B OH   1 
ATOM   3562 N  N    . MET   B 2 200 ? -15.949 -34.890 5.844   1.00 24.07 ? 705  MET   B N    1 
ATOM   3563 C  CA   . MET   B 2 200 ? -17.123 -34.136 6.265   1.00 22.60 ? 705  MET   B CA   1 
ATOM   3564 C  C    . MET   B 2 200 ? -17.871 -33.505 5.099   1.00 24.50 ? 705  MET   B C    1 
ATOM   3565 O  O    . MET   B 2 200 ? -19.081 -33.273 5.203   1.00 25.31 ? 705  MET   B O    1 
ATOM   3566 C  CB   . MET   B 2 200 ? -16.701 -33.036 7.238   1.00 23.30 ? 705  MET   B CB   1 
ATOM   3567 C  CG   . MET   B 2 200 ? -17.705 -32.691 8.316   1.00 28.65 ? 705  MET   B CG   1 
ATOM   3568 S  SD   . MET   B 2 200 ? -16.870 -31.741 9.593   1.00 24.59 ? 705  MET   B SD   1 
ATOM   3569 C  CE   . MET   B 2 200 ? -16.078 -30.500 8.571   1.00 28.74 ? 705  MET   B CE   1 
ATOM   3570 N  N    . THR   B 2 201 ? -17.176 -33.221 3.993   1.00 18.20 ? 706  THR   B N    1 
ATOM   3571 C  CA   . THR   B 2 201 ? -17.730 -32.342 2.966   1.00 20.36 ? 706  THR   B CA   1 
ATOM   3572 C  C    . THR   B 2 201 ? -18.983 -32.918 2.317   1.00 21.98 ? 706  THR   B C    1 
ATOM   3573 O  O    . THR   B 2 201 ? -19.862 -32.157 1.896   1.00 21.56 ? 706  THR   B O    1 
ATOM   3574 C  CB   . THR   B 2 201 ? -16.675 -32.048 1.901   1.00 24.82 ? 706  THR   B CB   1 
ATOM   3575 O  OG1  . THR   B 2 201 ? -16.252 -33.274 1.292   1.00 30.76 ? 706  THR   B OG1  1 
ATOM   3576 C  CG2  . THR   B 2 201 ? -15.473 -31.351 2.524   1.00 22.30 ? 706  THR   B CG2  1 
ATOM   3577 N  N    . LYS   B 2 202 ? -19.091 -34.245 2.223   1.00 20.60 ? 707  LYS   B N    1 
ATOM   3578 C  CA   . LYS   B 2 202 ? -20.294 -34.828 1.641   1.00 21.69 ? 707  LYS   B CA   1 
ATOM   3579 C  C    . LYS   B 2 202 ? -21.520 -34.652 2.528   1.00 22.23 ? 707  LYS   B C    1 
ATOM   3580 O  O    . LYS   B 2 202 ? -22.633 -34.949 2.081   1.00 26.07 ? 707  LYS   B O    1 
ATOM   3581 C  CB   . LYS   B 2 202 ? -20.082 -36.314 1.341   1.00 22.60 ? 707  LYS   B CB   1 
ATOM   3582 C  CG   . LYS   B 2 202 ? -19.687 -37.159 2.539   1.00 21.35 ? 707  LYS   B CG   1 
ATOM   3583 C  CD   . LYS   B 2 202 ? -19.541 -38.620 2.137   1.00 22.54 ? 707  LYS   B CD   1 
ATOM   3584 C  CE   . LYS   B 2 202 ? -18.659 -39.384 3.109   1.00 23.79 ? 707  LYS   B CE   1 
ATOM   3585 N  NZ   . LYS   B 2 202 ? -17.263 -38.868 3.112   1.00 24.54 ? 707  LYS   B NZ   1 
ATOM   3586 N  N    . PHE   B 2 203 ? -21.345 -34.182 3.763   1.00 20.30 ? 708  PHE   B N    1 
ATOM   3587 C  CA   . PHE   B 2 203 ? -22.453 -33.885 4.661   1.00 22.22 ? 708  PHE   B CA   1 
ATOM   3588 C  C    . PHE   B 2 203 ? -22.640 -32.385 4.860   1.00 24.36 ? 708  PHE   B C    1 
ATOM   3589 O  O    . PHE   B 2 203 ? -23.240 -31.966 5.855   1.00 16.54 ? 708  PHE   B O    1 
ATOM   3590 C  CB   . PHE   B 2 203 ? -22.246 -34.578 6.007   1.00 24.15 ? 708  PHE   B CB   1 
ATOM   3591 C  CG   . PHE   B 2 203 ? -22.124 -36.069 5.904   1.00 25.81 ? 708  PHE   B CG   1 
ATOM   3592 C  CD1  . PHE   B 2 203 ? -23.182 -36.831 5.437   1.00 23.86 ? 708  PHE   B CD1  1 
ATOM   3593 C  CD2  . PHE   B 2 203 ? -20.952 -36.710 6.272   1.00 18.43 ? 708  PHE   B CD2  1 
ATOM   3594 C  CE1  . PHE   B 2 203 ? -23.074 -38.205 5.339   1.00 22.12 ? 708  PHE   B CE1  1 
ATOM   3595 C  CE2  . PHE   B 2 203 ? -20.839 -38.083 6.176   1.00 20.82 ? 708  PHE   B CE2  1 
ATOM   3596 C  CZ   . PHE   B 2 203 ? -21.901 -38.832 5.709   1.00 24.18 ? 708  PHE   B CZ   1 
ATOM   3597 N  N    . ASN   B 2 204 ? -22.130 -31.571 3.937   1.00 22.34 ? 709  ASN   B N    1 
ATOM   3598 C  CA   . ASN   B 2 204 ? -22.318 -30.129 4.018   1.00 20.94 ? 709  ASN   B CA   1 
ATOM   3599 C  C    . ASN   B 2 204 ? -23.800 -29.785 3.974   1.00 21.26 ? 709  ASN   B C    1 
ATOM   3600 O  O    . ASN   B 2 204 ? -24.551 -30.319 3.153   1.00 21.10 ? 709  ASN   B O    1 
ATOM   3601 C  CB   . ASN   B 2 204 ? -21.584 -29.431 2.871   1.00 17.43 ? 709  ASN   B CB   1 
ATOM   3602 C  CG   . ASN   B 2 204 ? -20.107 -29.239 3.151   1.00 22.77 ? 709  ASN   B CG   1 
ATOM   3603 O  OD1  . ASN   B 2 204 ? -19.646 -29.437 4.274   1.00 21.67 ? 709  ASN   B OD1  1 
ATOM   3604 N  ND2  . ASN   B 2 204 ? -19.356 -28.848 2.127   1.00 19.15 ? 709  ASN   B ND2  1 
ATOM   3605 N  N    . GLN   B 2 205 ? -24.220 -28.894 4.866   1.00 20.08 ? 710  GLN   B N    1 
ATOM   3606 C  CA   . GLN   B 2 205 ? -25.600 -28.442 4.942   1.00 19.75 ? 710  GLN   B CA   1 
ATOM   3607 C  C    . GLN   B 2 205 ? -25.704 -27.021 4.407   1.00 20.52 ? 710  GLN   B C    1 
ATOM   3608 O  O    . GLN   B 2 205 ? -24.850 -26.176 4.694   1.00 18.94 ? 710  GLN   B O    1 
ATOM   3609 C  CB   . GLN   B 2 205 ? -26.121 -28.503 6.380   1.00 16.12 ? 710  GLN   B CB   1 
ATOM   3610 C  CG   . GLN   B 2 205 ? -25.945 -29.862 7.043   1.00 18.03 ? 710  GLN   B CG   1 
ATOM   3611 C  CD   . GLN   B 2 205 ? -26.892 -30.912 6.494   1.00 24.62 ? 710  GLN   B CD   1 
ATOM   3612 O  OE1  . GLN   B 2 205 ? -28.113 -30.777 6.591   1.00 18.99 ? 710  GLN   B OE1  1 
ATOM   3613 N  NE2  . GLN   B 2 205 ? -26.333 -31.966 5.913   1.00 24.14 ? 710  GLN   B NE2  1 
ATOM   3614 N  N    . LYS   B 2 206 ? -26.755 -26.767 3.621   1.00 25.70 ? 711  LYS   B N    1 
ATOM   3615 C  CA   . LYS   B 2 206 ? -26.956 -25.438 3.051   1.00 21.93 ? 711  LYS   B CA   1 
ATOM   3616 C  C    . LYS   B 2 206 ? -27.109 -24.378 4.133   1.00 20.45 ? 711  LYS   B C    1 
ATOM   3617 O  O    . LYS   B 2 206 ? -26.653 -23.242 3.957   1.00 21.97 ? 711  LYS   B O    1 
ATOM   3618 C  CB   . LYS   B 2 206 ? -28.184 -25.437 2.137   1.00 24.90 ? 711  LYS   B CB   1 
ATOM   3619 C  CG   . LYS   B 2 206 ? -27.888 -25.189 0.665   1.00 29.00 ? 711  LYS   B CG   1 
ATOM   3620 C  CD   . LYS   B 2 206 ? -26.624 -25.900 0.216   1.00 40.63 ? 711  LYS   B CD   1 
ATOM   3621 C  CE   . LYS   B 2 206 ? -26.456 -25.818 -1.293  1.00 50.99 ? 711  LYS   B CE   1 
ATOM   3622 N  NZ   . LYS   B 2 206 ? -25.027 -25.898 -1.703  1.00 54.58 ? 711  LYS   B NZ   1 
ATOM   3623 N  N    . GLY   B 2 207 ? -27.743 -24.726 5.247   1.00 20.43 ? 712  GLY   B N    1 
ATOM   3624 C  CA   . GLY   B 2 207 ? -27.934 -23.776 6.326   1.00 20.65 ? 712  GLY   B CA   1 
ATOM   3625 C  C    . GLY   B 2 207 ? -28.305 -24.493 7.604   1.00 22.24 ? 712  GLY   B C    1 
ATOM   3626 O  O    . GLY   B 2 207 ? -28.418 -25.721 7.648   1.00 22.49 ? 712  GLY   B O    1 
ATOM   3627 N  N    . VAL   B 2 208 ? -28.505 -23.692 8.653   1.00 20.48 ? 713  VAL   B N    1 
ATOM   3628 C  CA   . VAL   B 2 208 ? -28.764 -24.243 9.982   1.00 21.20 ? 713  VAL   B CA   1 
ATOM   3629 C  C    . VAL   B 2 208 ? -30.075 -25.020 9.996   1.00 22.51 ? 713  VAL   B C    1 
ATOM   3630 O  O    . VAL   B 2 208 ? -30.149 -26.135 10.526  1.00 20.90 ? 713  VAL   B O    1 
ATOM   3631 C  CB   . VAL   B 2 208 ? -28.763 -23.122 11.036  1.00 17.38 ? 713  VAL   B CB   1 
ATOM   3632 C  CG1  . VAL   B 2 208 ? -29.303 -23.636 12.364  1.00 16.02 ? 713  VAL   B CG1  1 
ATOM   3633 C  CG2  . VAL   B 2 208 ? -27.362 -22.566 11.208  1.00 16.51 ? 713  VAL   B CG2  1 
ATOM   3634 N  N    . GLU   B 2 209 ? -31.129 -24.441 9.414   1.00 21.23 ? 714  GLU   B N    1 
ATOM   3635 C  CA   . GLU   B 2 209 ? -32.431 -25.101 9.421   1.00 25.65 ? 714  GLU   B CA   1 
ATOM   3636 C  C    . GLU   B 2 209 ? -32.384 -26.436 8.686   1.00 23.35 ? 714  GLU   B C    1 
ATOM   3637 O  O    . GLU   B 2 209 ? -32.992 -27.417 9.129   1.00 21.11 ? 714  GLU   B O    1 
ATOM   3638 C  CB   . GLU   B 2 209 ? -33.489 -24.183 8.807   1.00 20.72 ? 714  GLU   B CB   1 
ATOM   3639 C  CG   . GLU   B 2 209 ? -33.366 -22.727 9.227   1.00 30.99 ? 714  GLU   B CG   1 
ATOM   3640 C  CD   . GLU   B 2 209 ? -33.850 -22.489 10.645  1.00 42.45 ? 714  GLU   B CD   1 
ATOM   3641 O  OE1  . GLU   B 2 209 ? -34.834 -23.141 11.053  1.00 44.64 ? 714  GLU   B OE1  1 
ATOM   3642 O  OE2  . GLU   B 2 209 ? -33.253 -21.646 11.348  1.00 36.07 ? 714  GLU   B OE2  1 
ATOM   3643 N  N    . ASP   B 2 210 ? -31.666 -26.492 7.561   1.00 21.80 ? 715  ASP   B N    1 
ATOM   3644 C  CA   . ASP   B 2 210 ? -31.488 -27.763 6.864   1.00 20.88 ? 715  ASP   B CA   1 
ATOM   3645 C  C    . ASP   B 2 210 ? -30.777 -28.776 7.749   1.00 23.09 ? 715  ASP   B C    1 
ATOM   3646 O  O    . ASP   B 2 210 ? -31.115 -29.966 7.742   1.00 21.66 ? 715  ASP   B O    1 
ATOM   3647 C  CB   . ASP   B 2 210 ? -30.706 -27.552 5.567   1.00 20.67 ? 715  ASP   B CB   1 
ATOM   3648 C  CG   . ASP   B 2 210 ? -31.554 -26.963 4.461   1.00 24.82 ? 715  ASP   B CG   1 
ATOM   3649 O  OD1  . ASP   B 2 210 ? -32.729 -26.636 4.722   1.00 24.24 ? 715  ASP   B OD1  1 
ATOM   3650 O  OD2  . ASP   B 2 210 ? -31.045 -26.835 3.328   1.00 27.12 ? 715  ASP   B OD2  1 
ATOM   3651 N  N    . ALA   B 2 211 ? -29.788 -28.321 8.522   1.00 19.71 ? 716  ALA   B N    1 
ATOM   3652 C  CA   . ALA   B 2 211 ? -29.058 -29.223 9.406   1.00 24.04 ? 716  ALA   B CA   1 
ATOM   3653 C  C    . ALA   B 2 211 ? -29.945 -29.741 10.530  1.00 20.79 ? 716  ALA   B C    1 
ATOM   3654 O  O    . ALA   B 2 211 ? -29.868 -30.920 10.894  1.00 25.30 ? 716  ALA   B O    1 
ATOM   3655 C  CB   . ALA   B 2 211 ? -27.829 -28.516 9.975   1.00 19.21 ? 716  ALA   B CB   1 
ATOM   3656 N  N    . LEU   B 2 212 ? -30.789 -28.874 11.096  1.00 22.56 ? 717  LEU   B N    1 
ATOM   3657 C  CA   . LEU   B 2 212 ? -31.693 -29.305 12.159  1.00 21.17 ? 717  LEU   B CA   1 
ATOM   3658 C  C    . LEU   B 2 212 ? -32.643 -30.388 11.662  1.00 24.19 ? 717  LEU   B C    1 
ATOM   3659 O  O    . LEU   B 2 212 ? -32.851 -31.406 12.333  1.00 26.53 ? 717  LEU   B O    1 
ATOM   3660 C  CB   . LEU   B 2 212 ? -32.478 -28.110 12.701  1.00 19.63 ? 717  LEU   B CB   1 
ATOM   3661 C  CG   . LEU   B 2 212 ? -31.668 -26.947 13.274  1.00 23.84 ? 717  LEU   B CG   1 
ATOM   3662 C  CD1  . LEU   B 2 212 ? -32.594 -25.856 13.788  1.00 26.14 ? 717  LEU   B CD1  1 
ATOM   3663 C  CD2  . LEU   B 2 212 ? -30.744 -27.433 14.377  1.00 20.94 ? 717  LEU   B CD2  1 
ATOM   3664 N  N    . VAL   B 2 213 ? -33.231 -30.183 10.481  1.00 19.79 ? 718  VAL   B N    1 
ATOM   3665 C  CA   . VAL   B 2 213 ? -34.118 -31.189 9.903   1.00 28.42 ? 718  VAL   B CA   1 
ATOM   3666 C  C    . VAL   B 2 213 ? -33.345 -32.466 9.603   1.00 26.99 ? 718  VAL   B C    1 
ATOM   3667 O  O    . VAL   B 2 213 ? -33.843 -33.578 9.820   1.00 22.85 ? 718  VAL   B O    1 
ATOM   3668 C  CB   . VAL   B 2 213 ? -34.809 -30.628 8.645   1.00 24.37 ? 718  VAL   B CB   1 
ATOM   3669 C  CG1  . VAL   B 2 213 ? -35.472 -31.742 7.850   1.00 23.12 ? 718  VAL   B CG1  1 
ATOM   3670 C  CG2  . VAL   B 2 213 ? -35.827 -29.564 9.031   1.00 22.70 ? 718  VAL   B CG2  1 
ATOM   3671 N  N    . SER   B 2 214 ? -32.111 -32.329 9.110   1.00 22.44 ? 719  SER   B N    1 
ATOM   3672 C  CA   . SER   B 2 214 ? -31.277 -33.502 8.867   1.00 26.11 ? 719  SER   B CA   1 
ATOM   3673 C  C    . SER   B 2 214 ? -31.027 -34.274 10.156  1.00 26.19 ? 719  SER   B C    1 
ATOM   3674 O  O    . SER   B 2 214 ? -30.966 -35.510 10.148  1.00 24.80 ? 719  SER   B O    1 
ATOM   3675 C  CB   . SER   B 2 214 ? -29.952 -33.082 8.230   1.00 24.29 ? 719  SER   B CB   1 
ATOM   3676 O  OG   . SER   B 2 214 ? -30.163 -32.440 6.984   1.00 24.88 ? 719  SER   B OG   1 
ATOM   3677 N  N    . LEU   B 2 215 ? -30.885 -33.562 11.275  1.00 25.14 ? 720  LEU   B N    1 
ATOM   3678 C  CA   . LEU   B 2 215 ? -30.680 -34.222 12.561  1.00 25.15 ? 720  LEU   B CA   1 
ATOM   3679 C  C    . LEU   B 2 215 ? -31.940 -34.954 13.008  1.00 27.48 ? 720  LEU   B C    1 
ATOM   3680 O  O    . LEU   B 2 215 ? -31.907 -36.156 13.297  1.00 32.32 ? 720  LEU   B O    1 
ATOM   3681 C  CB   . LEU   B 2 215 ? -30.254 -33.196 13.614  1.00 24.04 ? 720  LEU   B CB   1 
ATOM   3682 C  CG   . LEU   B 2 215 ? -28.773 -32.819 13.679  1.00 24.41 ? 720  LEU   B CG   1 
ATOM   3683 C  CD1  . LEU   B 2 215 ? -28.544 -31.736 14.724  1.00 20.89 ? 720  LEU   B CD1  1 
ATOM   3684 C  CD2  . LEU   B 2 215 ? -27.926 -34.043 13.980  1.00 22.61 ? 720  LEU   B CD2  1 
ATOM   3685 N  N    . LYS   B 2 216 ? -33.068 -34.239 13.061  1.00 24.40 ? 721  LYS   B N    1 
ATOM   3686 C  CA   . LYS   B 2 216 ? -34.291 -34.815 13.611  1.00 22.94 ? 721  LYS   B CA   1 
ATOM   3687 C  C    . LYS   B 2 216 ? -34.809 -35.972 12.767  1.00 27.29 ? 721  LYS   B C    1 
ATOM   3688 O  O    . LYS   B 2 216 ? -35.422 -36.902 13.303  1.00 30.14 ? 721  LYS   B O    1 
ATOM   3689 C  CB   . LYS   B 2 216 ? -35.363 -33.732 13.742  1.00 28.91 ? 721  LYS   B CB   1 
ATOM   3690 C  CG   . LYS   B 2 216 ? -35.085 -32.724 14.845  1.00 34.50 ? 721  LYS   B CG   1 
ATOM   3691 C  CD   . LYS   B 2 216 ? -36.239 -31.750 15.013  1.00 33.78 ? 721  LYS   B CD   1 
ATOM   3692 C  CE   . LYS   B 2 216 ? -36.662 -31.651 16.468  1.00 34.15 ? 721  LYS   B CE   1 
ATOM   3693 N  NZ   . LYS   B 2 216 ? -37.781 -30.690 16.662  1.00 45.19 ? 721  LYS   B NZ   1 
ATOM   3694 N  N    . THR   B 2 217 ? -34.576 -35.939 11.458  1.00 25.83 ? 722  THR   B N    1 
ATOM   3695 C  CA   . THR   B 2 217 ? -35.034 -36.997 10.567  1.00 27.48 ? 722  THR   B CA   1 
ATOM   3696 C  C    . THR   B 2 217 ? -34.040 -38.145 10.443  1.00 29.94 ? 722  THR   B C    1 
ATOM   3697 O  O    . THR   B 2 217 ? -34.287 -39.077 9.671   1.00 32.66 ? 722  THR   B O    1 
ATOM   3698 C  CB   . THR   B 2 217 ? -35.336 -36.428 9.178   1.00 31.89 ? 722  THR   B CB   1 
ATOM   3699 O  OG1  . THR   B 2 217 ? -34.168 -35.777 8.661   1.00 31.21 ? 722  THR   B OG1  1 
ATOM   3700 C  CG2  . THR   B 2 217 ? -36.486 -35.430 9.248   1.00 27.24 ? 722  THR   B CG2  1 
ATOM   3701 N  N    . GLY   B 2 218 ? -32.930 -38.103 11.174  1.00 29.07 ? 723  GLY   B N    1 
ATOM   3702 C  CA   . GLY   B 2 218 ? -31.991 -39.205 11.181  1.00 30.45 ? 723  GLY   B CA   1 
ATOM   3703 C  C    . GLY   B 2 218 ? -31.029 -39.255 10.017  1.00 34.00 ? 723  GLY   B C    1 
ATOM   3704 O  O    . GLY   B 2 218 ? -30.275 -40.227 9.903   1.00 33.38 ? 723  GLY   B O    1 
ATOM   3705 N  N    . LYS   B 2 219 ? -31.030 -38.248 9.143   1.00 29.59 ? 724  LYS   B N    1 
ATOM   3706 C  CA   . LYS   B 2 219 ? -30.068 -38.203 8.049   1.00 33.28 ? 724  LYS   B CA   1 
ATOM   3707 C  C    . LYS   B 2 219 ? -28.676 -37.791 8.506   1.00 26.87 ? 724  LYS   B C    1 
ATOM   3708 O  O    . LYS   B 2 219 ? -27.723 -37.920 7.731   1.00 23.96 ? 724  LYS   B O    1 
ATOM   3709 C  CB   . LYS   B 2 219 ? -30.542 -37.238 6.959   1.00 35.46 ? 724  LYS   B CB   1 
ATOM   3710 C  CG   . LYS   B 2 219 ? -32.042 -37.230 6.731   1.00 41.51 ? 724  LYS   B CG   1 
ATOM   3711 C  CD   . LYS   B 2 219 ? -32.369 -36.992 5.265   1.00 53.32 ? 724  LYS   B CD   1 
ATOM   3712 C  CE   . LYS   B 2 219 ? -33.715 -36.304 5.103   1.00 51.96 ? 724  LYS   B CE   1 
ATOM   3713 N  NZ   . LYS   B 2 219 ? -33.726 -34.949 5.720   1.00 40.07 ? 724  LYS   B NZ   1 
ATOM   3714 N  N    . LEU   B 2 220 ? -28.538 -37.303 9.736   1.00 28.08 ? 725  LEU   B N    1 
ATOM   3715 C  CA   . LEU   B 2 220 ? -27.273 -36.774 10.226  1.00 22.07 ? 725  LEU   B CA   1 
ATOM   3716 C  C    . LEU   B 2 220 ? -27.151 -37.113 11.703  1.00 23.15 ? 725  LEU   B C    1 
ATOM   3717 O  O    . LEU   B 2 220 ? -28.115 -36.950 12.457  1.00 29.34 ? 725  LEU   B O    1 
ATOM   3718 C  CB   . LEU   B 2 220 ? -27.202 -35.258 10.011  1.00 24.69 ? 725  LEU   B CB   1 
ATOM   3719 C  CG   . LEU   B 2 220 ? -25.835 -34.577 9.978   1.00 24.68 ? 725  LEU   B CG   1 
ATOM   3720 C  CD1  . LEU   B 2 220 ? -24.954 -35.189 8.902   1.00 20.81 ? 725  LEU   B CD1  1 
ATOM   3721 C  CD2  . LEU   B 2 220 ? -26.001 -33.082 9.748   1.00 24.57 ? 725  LEU   B CD2  1 
ATOM   3722 N  N    . ASP   B 2 221 ? -25.974 -37.586 12.113  1.00 23.30 ? 726  ASP   B N    1 
ATOM   3723 C  CA   . ASP   B 2 221 ? -25.754 -37.944 13.509  1.00 25.85 ? 726  ASP   B CA   1 
ATOM   3724 C  C    . ASP   B 2 221 ? -25.272 -36.772 14.352  1.00 21.98 ? 726  ASP   B C    1 
ATOM   3725 O  O    . ASP   B 2 221 ? -25.584 -36.711 15.547  1.00 18.50 ? 726  ASP   B O    1 
ATOM   3726 C  CB   . ASP   B 2 221 ? -24.746 -39.093 13.611  1.00 21.79 ? 726  ASP   B CB   1 
ATOM   3727 C  CG   . ASP   B 2 221 ? -25.203 -40.340 12.879  1.00 28.10 ? 726  ASP   B CG   1 
ATOM   3728 O  OD1  . ASP   B 2 221 ? -26.369 -40.746 13.064  1.00 25.77 ? 726  ASP   B OD1  1 
ATOM   3729 O  OD2  . ASP   B 2 221 ? -24.396 -40.914 12.119  1.00 26.47 ? 726  ASP   B OD2  1 
ATOM   3730 N  N    . ALA   B 2 222 ? -24.526 -35.838 13.765  1.00 19.77 ? 727  ALA   B N    1 
ATOM   3731 C  CA   . ALA   B 2 222 ? -24.001 -34.704 14.508  1.00 18.28 ? 727  ALA   B CA   1 
ATOM   3732 C  C    . ALA   B 2 222 ? -23.902 -33.497 13.588  1.00 19.53 ? 727  ALA   B C    1 
ATOM   3733 O  O    . ALA   B 2 222 ? -23.666 -33.632 12.384  1.00 19.20 ? 727  ALA   B O    1 
ATOM   3734 C  CB   . ALA   B 2 222 ? -22.630 -35.015 15.121  1.00 17.72 ? 727  ALA   B CB   1 
ATOM   3735 N  N    . PHE   B 2 223 ? -24.085 -32.314 14.169  1.00 17.58 ? 728  PHE   B N    1 
ATOM   3736 C  CA   . PHE   B 2 223 ? -23.992 -31.051 13.445  1.00 15.31 ? 728  PHE   B CA   1 
ATOM   3737 C  C    . PHE   B 2 223 ? -23.023 -30.144 14.186  1.00 16.66 ? 728  PHE   B C    1 
ATOM   3738 O  O    . PHE   B 2 223 ? -23.282 -29.761 15.332  1.00 20.61 ? 728  PHE   B O    1 
ATOM   3739 C  CB   . PHE   B 2 223 ? -25.365 -30.387 13.311  1.00 17.23 ? 728  PHE   B CB   1 
ATOM   3740 C  CG   . PHE   B 2 223 ? -25.327 -29.031 12.661  1.00 14.92 ? 728  PHE   B CG   1 
ATOM   3741 C  CD1  . PHE   B 2 223 ? -24.550 -28.805 11.535  1.00 17.66 ? 728  PHE   B CD1  1 
ATOM   3742 C  CD2  . PHE   B 2 223 ? -26.076 -27.984 13.172  1.00 19.22 ? 728  PHE   B CD2  1 
ATOM   3743 C  CE1  . PHE   B 2 223 ? -24.517 -27.559 10.937  1.00 18.37 ? 728  PHE   B CE1  1 
ATOM   3744 C  CE2  . PHE   B 2 223 ? -26.048 -26.736 12.577  1.00 19.18 ? 728  PHE   B CE2  1 
ATOM   3745 C  CZ   . PHE   B 2 223 ? -25.268 -26.523 11.458  1.00 19.62 ? 728  PHE   B CZ   1 
ATOM   3746 N  N    . ILE   B 2 224 ? -21.916 -29.807 13.535  1.00 16.41 ? 729  ILE   B N    1 
ATOM   3747 C  CA   . ILE   B 2 224 ? -20.857 -28.995 14.125  1.00 16.15 ? 729  ILE   B CA   1 
ATOM   3748 C  C    . ILE   B 2 224 ? -21.008 -27.575 13.600  1.00 17.56 ? 729  ILE   B C    1 
ATOM   3749 O  O    . ILE   B 2 224 ? -21.010 -27.354 12.383  1.00 17.52 ? 729  ILE   B O    1 
ATOM   3750 C  CB   . ILE   B 2 224 ? -19.474 -29.571 13.789  1.00 20.60 ? 729  ILE   B CB   1 
ATOM   3751 C  CG1  . ILE   B 2 224 ? -19.427 -31.052 14.170  1.00 17.45 ? 729  ILE   B CG1  1 
ATOM   3752 C  CG2  . ILE   B 2 224 ? -18.382 -28.791 14.493  1.00 12.81 ? 729  ILE   B CG2  1 
ATOM   3753 C  CD1  . ILE   B 2 224 ? -18.364 -31.833 13.453  1.00 16.13 ? 729  ILE   B CD1  1 
ATOM   3754 N  N    . TYR   B 2 225 ? -21.133 -26.606 14.503  1.00 16.70 ? 730  TYR   B N    1 
ATOM   3755 C  CA   . TYR   B 2 225 ? -21.455 -25.249 14.082  1.00 13.14 ? 730  TYR   B CA   1 
ATOM   3756 C  C    . TYR   B 2 225 ? -21.097 -24.268 15.191  1.00 14.22 ? 730  TYR   B C    1 
ATOM   3757 O  O    . TYR   B 2 225 ? -20.675 -24.655 16.284  1.00 13.00 ? 730  TYR   B O    1 
ATOM   3758 C  CB   . TYR   B 2 225 ? -22.937 -25.139 13.701  1.00 13.33 ? 730  TYR   B CB   1 
ATOM   3759 C  CG   . TYR   B 2 225 ? -23.297 -23.877 12.951  1.00 15.91 ? 730  TYR   B CG   1 
ATOM   3760 C  CD1  . TYR   B 2 225 ? -22.871 -23.676 11.645  1.00 16.36 ? 730  TYR   B CD1  1 
ATOM   3761 C  CD2  . TYR   B 2 225 ? -24.064 -22.887 13.551  1.00 13.65 ? 730  TYR   B CD2  1 
ATOM   3762 C  CE1  . TYR   B 2 225 ? -23.197 -22.522 10.959  1.00 17.17 ? 730  TYR   B CE1  1 
ATOM   3763 C  CE2  . TYR   B 2 225 ? -24.391 -21.730 12.876  1.00 18.75 ? 730  TYR   B CE2  1 
ATOM   3764 C  CZ   . TYR   B 2 225 ? -23.958 -21.553 11.580  1.00 15.98 ? 730  TYR   B CZ   1 
ATOM   3765 O  OH   . TYR   B 2 225 ? -24.287 -20.400 10.905  1.00 12.29 ? 730  TYR   B OH   1 
ATOM   3766 N  N    . ASP   B 2 226 ? -21.260 -22.980 14.871  1.00 13.31 ? 731  ASP   B N    1 
ATOM   3767 C  CA   . ASP   B 2 226 ? -21.086 -21.880 15.813  1.00 15.97 ? 731  ASP   B CA   1 
ATOM   3768 C  C    . ASP   B 2 226 ? -21.751 -22.182 17.150  1.00 17.88 ? 731  ASP   B C    1 
ATOM   3769 O  O    . ASP   B 2 226 ? -22.867 -22.704 17.204  1.00 14.68 ? 731  ASP   B O    1 
ATOM   3770 C  CB   . ASP   B 2 226 ? -21.674 -20.600 15.205  1.00 16.56 ? 731  ASP   B CB   1 
ATOM   3771 C  CG   . ASP   B 2 226 ? -21.657 -19.430 16.166  1.00 17.10 ? 731  ASP   B CG   1 
ATOM   3772 O  OD1  . ASP   B 2 226 ? -20.587 -18.808 16.333  1.00 18.33 ? 731  ASP   B OD1  1 
ATOM   3773 O  OD2  . ASP   B 2 226 ? -22.719 -19.126 16.749  1.00 16.83 ? 731  ASP   B OD2  1 
ATOM   3774 N  N    . ALA   B 2 227 ? -21.050 -21.839 18.233  1.00 17.70 ? 732  ALA   B N    1 
ATOM   3775 C  CA   . ALA   B 2 227 ? -21.505 -22.219 19.567  1.00 22.73 ? 732  ALA   B CA   1 
ATOM   3776 C  C    . ALA   B 2 227 ? -22.758 -21.451 19.970  1.00 20.62 ? 732  ALA   B C    1 
ATOM   3777 O  O    . ALA   B 2 227 ? -23.726 -22.041 20.465  1.00 20.24 ? 732  ALA   B O    1 
ATOM   3778 C  CB   . ALA   B 2 227 ? -20.386 -21.994 20.583  1.00 19.32 ? 732  ALA   B CB   1 
ATOM   3779 N  N    . ALA   B 2 228 ? -22.759 -20.131 19.768  1.00 13.90 ? 733  ALA   B N    1 
ATOM   3780 C  CA   . ALA   B 2 228 ? -23.873 -19.311 20.232  1.00 20.19 ? 733  ALA   B CA   1 
ATOM   3781 C  C    . ALA   B 2 228 ? -25.167 -19.661 19.506  1.00 20.69 ? 733  ALA   B C    1 
ATOM   3782 O  O    . ALA   B 2 228 ? -26.245 -19.664 20.112  1.00 20.85 ? 733  ALA   B O    1 
ATOM   3783 C  CB   . ALA   B 2 228 ? -23.542 -17.829 20.055  1.00 18.80 ? 733  ALA   B CB   1 
ATOM   3784 N  N    . VAL   B 2 229 ? -25.081 -19.958 18.209  1.00 17.49 ? 734  VAL   B N    1 
ATOM   3785 C  CA   . VAL   B 2 229 ? -26.277 -20.300 17.446  1.00 15.97 ? 734  VAL   B CA   1 
ATOM   3786 C  C    . VAL   B 2 229 ? -26.834 -21.643 17.902  1.00 16.19 ? 734  VAL   B C    1 
ATOM   3787 O  O    . VAL   B 2 229 ? -28.041 -21.786 18.136  1.00 15.63 ? 734  VAL   B O    1 
ATOM   3788 C  CB   . VAL   B 2 229 ? -25.970 -20.295 15.937  1.00 15.24 ? 734  VAL   B CB   1 
ATOM   3789 C  CG1  . VAL   B 2 229 ? -27.088 -20.976 15.165  1.00 13.45 ? 734  VAL   B CG1  1 
ATOM   3790 C  CG2  . VAL   B 2 229 ? -25.766 -18.871 15.442  1.00 15.90 ? 734  VAL   B CG2  1 
ATOM   3791 N  N    . LEU   B 2 230 ? -25.964 -22.648 18.036  1.00 14.67 ? 735  LEU   B N    1 
ATOM   3792 C  CA   . LEU   B 2 230 ? -26.409 -23.958 18.503  1.00 19.87 ? 735  LEU   B CA   1 
ATOM   3793 C  C    . LEU   B 2 230 ? -26.991 -23.873 19.908  1.00 18.15 ? 735  LEU   B C    1 
ATOM   3794 O  O    . LEU   B 2 230 ? -27.979 -24.548 20.221  1.00 21.57 ? 735  LEU   B O    1 
ATOM   3795 C  CB   . LEU   B 2 230 ? -25.250 -24.953 18.462  1.00 13.21 ? 735  LEU   B CB   1 
ATOM   3796 C  CG   . LEU   B 2 230 ? -24.774 -25.398 17.078  1.00 17.56 ? 735  LEU   B CG   1 
ATOM   3797 C  CD1  . LEU   B 2 230 ? -23.806 -26.567 17.195  1.00 16.40 ? 735  LEU   B CD1  1 
ATOM   3798 C  CD2  . LEU   B 2 230 ? -25.954 -25.760 16.188  1.00 18.13 ? 735  LEU   B CD2  1 
ATOM   3799 N  N    . ASN   B 2 231 ? -26.386 -23.051 20.769  1.00 20.20 ? 736  ASN   B N    1 
ATOM   3800 C  CA   . ASN   B 2 231 ? -26.928 -22.842 22.107  1.00 22.13 ? 736  ASN   B CA   1 
ATOM   3801 C  C    . ASN   B 2 231 ? -28.353 -22.309 22.045  1.00 24.74 ? 736  ASN   B C    1 
ATOM   3802 O  O    . ASN   B 2 231 ? -29.225 -22.749 22.804  1.00 20.54 ? 736  ASN   B O    1 
ATOM   3803 C  CB   . ASN   B 2 231 ? -26.027 -21.880 22.884  1.00 23.97 ? 736  ASN   B CB   1 
ATOM   3804 C  CG   . ASN   B 2 231 ? -26.372 -21.814 24.359  1.00 27.17 ? 736  ASN   B CG   1 
ATOM   3805 O  OD1  . ASN   B 2 231 ? -27.450 -21.357 24.740  1.00 28.57 ? 736  ASN   B OD1  1 
ATOM   3806 N  ND2  . ASN   B 2 231 ? -25.450 -22.268 25.199  1.00 33.07 ? 736  ASN   B ND2  1 
ATOM   3807 N  N    . TYR   B 2 232 ? -28.610 -21.364 21.139  1.00 23.09 ? 737  TYR   B N    1 
ATOM   3808 C  CA   . TYR   B 2 232 ? -29.948 -20.798 21.011  1.00 22.57 ? 737  TYR   B CA   1 
ATOM   3809 C  C    . TYR   B 2 232 ? -30.932 -21.818 20.451  1.00 22.76 ? 737  TYR   B C    1 
ATOM   3810 O  O    . TYR   B 2 232 ? -32.063 -21.929 20.938  1.00 24.47 ? 737  TYR   B O    1 
ATOM   3811 C  CB   . TYR   B 2 232 ? -29.898 -19.552 20.129  1.00 22.88 ? 737  TYR   B CB   1 
ATOM   3812 C  CG   . TYR   B 2 232 ? -31.251 -19.033 19.699  1.00 23.67 ? 737  TYR   B CG   1 
ATOM   3813 C  CD1  . TYR   B 2 232 ? -32.037 -18.284 20.566  1.00 24.53 ? 737  TYR   B CD1  1 
ATOM   3814 C  CD2  . TYR   B 2 232 ? -31.738 -19.282 18.422  1.00 23.04 ? 737  TYR   B CD2  1 
ATOM   3815 C  CE1  . TYR   B 2 232 ? -33.271 -17.801 20.173  1.00 27.79 ? 737  TYR   B CE1  1 
ATOM   3816 C  CE2  . TYR   B 2 232 ? -32.971 -18.803 18.021  1.00 24.30 ? 737  TYR   B CE2  1 
ATOM   3817 C  CZ   . TYR   B 2 232 ? -33.732 -18.063 18.900  1.00 28.82 ? 737  TYR   B CZ   1 
ATOM   3818 O  OH   . TYR   B 2 232 ? -34.962 -17.587 18.505  1.00 38.60 ? 737  TYR   B OH   1 
ATOM   3819 N  N    . LYS   B 2 233 ? -30.519 -22.572 19.429  1.00 16.96 ? 738  LYS   B N    1 
ATOM   3820 C  CA   . LYS   B 2 233 ? -31.413 -23.556 18.830  1.00 23.23 ? 738  LYS   B CA   1 
ATOM   3821 C  C    . LYS   B 2 233 ? -31.715 -24.701 19.788  1.00 27.92 ? 738  LYS   B C    1 
ATOM   3822 O  O    . LYS   B 2 233 ? -32.818 -25.259 19.755  1.00 28.02 ? 738  LYS   B O    1 
ATOM   3823 C  CB   . LYS   B 2 233 ? -30.807 -24.094 17.534  1.00 26.54 ? 738  LYS   B CB   1 
ATOM   3824 C  CG   . LYS   B 2 233 ? -30.704 -23.062 16.423  1.00 27.17 ? 738  LYS   B CG   1 
ATOM   3825 C  CD   . LYS   B 2 233 ? -32.078 -22.672 15.902  1.00 23.47 ? 738  LYS   B CD   1 
ATOM   3826 C  CE   . LYS   B 2 233 ? -31.971 -21.742 14.705  1.00 33.18 ? 738  LYS   B CE   1 
ATOM   3827 N  NZ   . LYS   B 2 233 ? -33.263 -21.624 13.974  1.00 25.56 ? 738  LYS   B NZ   1 
ATOM   3828 N  N    . ALA   B 2 234 ? -30.756 -25.066 20.643  1.00 24.23 ? 739  ALA   B N    1 
ATOM   3829 C  CA   . ALA   B 2 234 ? -30.995 -26.137 21.603  1.00 25.99 ? 739  ALA   B CA   1 
ATOM   3830 C  C    . ALA   B 2 234 ? -32.063 -25.742 22.614  1.00 32.71 ? 739  ALA   B C    1 
ATOM   3831 O  O    . ALA   B 2 234 ? -32.939 -26.547 22.951  1.00 30.21 ? 739  ALA   B O    1 
ATOM   3832 C  CB   . ALA   B 2 234 ? -29.692 -26.507 22.312  1.00 24.67 ? 739  ALA   B CB   1 
ATOM   3833 N  N    . GLY   B 2 235 ? -32.015 -24.502 23.100  1.00 39.09 ? 740  GLY   B N    1 
ATOM   3834 C  CA   . GLY   B 2 235 ? -32.996 -24.031 24.060  1.00 38.65 ? 740  GLY   B CA   1 
ATOM   3835 C  C    . GLY   B 2 235 ? -34.393 -23.857 23.502  1.00 41.08 ? 740  GLY   B C    1 
ATOM   3836 O  O    . GLY   B 2 235 ? -35.338 -23.721 24.287  1.00 47.07 ? 740  GLY   B O    1 
ATOM   3837 N  N    . ARG   B 2 236 ? -34.549 -23.861 22.178  1.00 30.47 ? 741  ARG   B N    1 
ATOM   3838 C  CA   . ARG   B 2 236 ? -35.850 -23.673 21.547  1.00 31.20 ? 741  ARG   B CA   1 
ATOM   3839 C  C    . ARG   B 2 236 ? -36.292 -24.885 20.738  1.00 32.42 ? 741  ARG   B C    1 
ATOM   3840 O  O    . ARG   B 2 236 ? -37.261 -24.787 19.977  1.00 33.29 ? 741  ARG   B O    1 
ATOM   3841 C  CB   . ARG   B 2 236 ? -35.831 -22.431 20.652  1.00 29.78 ? 741  ARG   B CB   1 
ATOM   3842 C  CG   . ARG   B 2 236 ? -36.071 -21.133 21.397  1.00 38.51 ? 741  ARG   B CG   1 
ATOM   3843 C  CD   . ARG   B 2 236 ? -36.082 -19.955 20.443  1.00 36.82 ? 741  ARG   B CD   1 
ATOM   3844 N  NE   . ARG   B 2 236 ? -37.202 -19.055 20.689  1.00 46.11 ? 741  ARG   B NE   1 
ATOM   3845 C  CZ   . ARG   B 2 236 ? -37.240 -18.151 21.659  1.00 43.99 ? 741  ARG   B CZ   1 
ATOM   3846 N  NH1  . ARG   B 2 236 ? -36.230 -17.996 22.500  1.00 38.13 ? 741  ARG   B NH1  1 
ATOM   3847 N  NH2  . ARG   B 2 236 ? -38.316 -17.381 21.787  1.00 57.00 ? 741  ARG   B NH2  1 
ATOM   3848 N  N    . ASP   B 2 237 ? -35.611 -26.019 20.877  1.00 32.46 ? 742  ASP   B N    1 
ATOM   3849 C  CA   . ASP   B 2 237 ? -35.985 -27.211 20.132  1.00 30.60 ? 742  ASP   B CA   1 
ATOM   3850 C  C    . ASP   B 2 237 ? -37.284 -27.790 20.679  1.00 31.90 ? 742  ASP   B C    1 
ATOM   3851 O  O    . ASP   B 2 237 ? -37.461 -27.904 21.897  1.00 35.17 ? 742  ASP   B O    1 
ATOM   3852 C  CB   . ASP   B 2 237 ? -34.869 -28.251 20.203  1.00 32.12 ? 742  ASP   B CB   1 
ATOM   3853 C  CG   . ASP   B 2 237 ? -35.153 -29.466 19.347  1.00 32.17 ? 742  ASP   B CG   1 
ATOM   3854 O  OD1  . ASP   B 2 237 ? -35.251 -29.311 18.113  1.00 32.71 ? 742  ASP   B OD1  1 
ATOM   3855 O  OD2  . ASP   B 2 237 ? -35.278 -30.575 19.908  1.00 36.88 ? 742  ASP   B OD2  1 
ATOM   3856 N  N    . GLU   B 2 238 ? -38.194 -28.149 19.777  1.00 33.52 ? 743  GLU   B N    1 
ATOM   3857 C  CA   . GLU   B 2 238 ? -39.462 -28.745 20.179  1.00 35.01 ? 743  GLU   B CA   1 
ATOM   3858 C  C    . GLU   B 2 238 ? -39.217 -30.089 20.851  1.00 35.23 ? 743  GLU   B C    1 
ATOM   3859 O  O    . GLU   B 2 238 ? -38.602 -30.985 20.264  1.00 35.09 ? 743  GLU   B O    1 
ATOM   3860 C  CB   . GLU   B 2 238 ? -40.374 -28.911 18.965  1.00 30.20 ? 743  GLU   B CB   1 
ATOM   3861 N  N    . GLY   B 2 239 ? -39.696 -30.227 22.087  1.00 32.22 ? 744  GLY   B N    1 
ATOM   3862 C  CA   . GLY   B 2 239 ? -39.463 -31.419 22.871  1.00 34.84 ? 744  GLY   B CA   1 
ATOM   3863 C  C    . GLY   B 2 239 ? -38.087 -31.518 23.489  1.00 38.18 ? 744  GLY   B C    1 
ATOM   3864 O  O    . GLY   B 2 239 ? -37.840 -32.459 24.256  1.00 33.59 ? 744  GLY   B O    1 
ATOM   3865 N  N    . CYS   B 2 240 ? -37.184 -30.584 23.178  1.00 38.39 ? 745  CYS   B N    1 
ATOM   3866 C  CA   . CYS   B 2 240 ? -35.831 -30.554 23.738  1.00 31.33 ? 745  CYS   B CA   1 
ATOM   3867 C  C    . CYS   B 2 240 ? -35.069 -31.841 23.420  1.00 32.63 ? 745  CYS   B C    1 
ATOM   3868 O  O    . CYS   B 2 240 ? -34.419 -32.436 24.282  1.00 30.32 ? 745  CYS   B O    1 
ATOM   3869 C  CB   . CYS   B 2 240 ? -35.866 -30.293 25.246  1.00 29.65 ? 745  CYS   B CB   1 
ATOM   3870 S  SG   . CYS   B 2 240 ? -36.816 -28.830 25.733  1.00 33.48 ? 745  CYS   B SG   1 
ATOM   3871 N  N    . LYS   B 2 241 ? -35.149 -32.267 22.160  1.00 29.17 ? 746  LYS   B N    1 
ATOM   3872 C  CA   . LYS   B 2 241 ? -34.494 -33.496 21.728  1.00 36.38 ? 746  LYS   B CA   1 
ATOM   3873 C  C    . LYS   B 2 241 ? -33.070 -33.270 21.239  1.00 29.20 ? 746  LYS   B C    1 
ATOM   3874 O  O    . LYS   B 2 241 ? -32.232 -34.171 21.361  1.00 30.50 ? 746  LYS   B O    1 
ATOM   3875 C  CB   . LYS   B 2 241 ? -35.313 -34.169 20.623  1.00 31.25 ? 746  LYS   B CB   1 
ATOM   3876 N  N    . LEU   B 2 242 ? -32.775 -32.095 20.690  1.00 27.82 ? 747  LEU   B N    1 
ATOM   3877 C  CA   . LEU   B 2 242 ? -31.440 -31.765 20.207  1.00 25.77 ? 747  LEU   B CA   1 
ATOM   3878 C  C    . LEU   B 2 242 ? -30.682 -31.009 21.289  1.00 25.05 ? 747  LEU   B C    1 
ATOM   3879 O  O    . LEU   B 2 242 ? -31.210 -30.058 21.875  1.00 28.86 ? 747  LEU   B O    1 
ATOM   3880 C  CB   . LEU   B 2 242 ? -31.512 -30.932 18.926  1.00 27.89 ? 747  LEU   B CB   1 
ATOM   3881 C  CG   . LEU   B 2 242 ? -32.347 -31.520 17.787  1.00 28.71 ? 747  LEU   B CG   1 
ATOM   3882 C  CD1  . LEU   B 2 242 ? -32.283 -30.632 16.554  1.00 25.33 ? 747  LEU   B CD1  1 
ATOM   3883 C  CD2  . LEU   B 2 242 ? -31.888 -32.933 17.461  1.00 25.34 ? 747  LEU   B CD2  1 
ATOM   3884 N  N    . VAL   B 2 243 ? -29.446 -31.438 21.555  1.00 21.57 ? 748  VAL   B N    1 
ATOM   3885 C  CA   . VAL   B 2 243 ? -28.627 -30.864 22.614  1.00 25.12 ? 748  VAL   B CA   1 
ATOM   3886 C  C    . VAL   B 2 243 ? -27.202 -30.686 22.110  1.00 25.68 ? 748  VAL   B C    1 
ATOM   3887 O  O    . VAL   B 2 243 ? -26.758 -31.354 21.173  1.00 22.36 ? 748  VAL   B O    1 
ATOM   3888 C  CB   . VAL   B 2 243 ? -28.621 -31.734 23.894  1.00 26.88 ? 748  VAL   B CB   1 
ATOM   3889 C  CG1  . VAL   B 2 243 ? -30.025 -31.887 24.456  1.00 21.10 ? 748  VAL   B CG1  1 
ATOM   3890 C  CG2  . VAL   B 2 243 ? -28.007 -33.095 23.607  1.00 22.08 ? 748  VAL   B CG2  1 
ATOM   3891 N  N    . THR   B 2 244 ? -26.483 -29.769 22.752  1.00 24.38 ? 749  THR   B N    1 
ATOM   3892 C  CA   . THR   B 2 244 ? -25.054 -29.612 22.531  1.00 28.30 ? 749  THR   B CA   1 
ATOM   3893 C  C    . THR   B 2 244 ? -24.291 -30.466 23.536  1.00 31.11 ? 749  THR   B C    1 
ATOM   3894 O  O    . THR   B 2 244 ? -24.686 -30.580 24.700  1.00 32.89 ? 749  THR   B O    1 
ATOM   3895 C  CB   . THR   B 2 244 ? -24.633 -28.146 22.659  1.00 28.38 ? 749  THR   B CB   1 
ATOM   3896 O  OG1  . THR   B 2 244 ? -25.062 -27.630 23.925  1.00 30.29 ? 749  THR   B OG1  1 
ATOM   3897 C  CG2  . THR   B 2 244 ? -25.247 -27.315 21.541  1.00 23.02 ? 749  THR   B CG2  1 
ATOM   3898 N  N    . ILE   B 2 245 ? -23.198 -31.070 23.077  1.00 34.85 ? 750  ILE   B N    1 
ATOM   3899 C  CA   . ILE   B 2 245 ? -22.458 -32.011 23.907  1.00 35.15 ? 750  ILE   B CA   1 
ATOM   3900 C  C    . ILE   B 2 245 ? -21.660 -31.263 24.970  1.00 41.79 ? 750  ILE   B C    1 
ATOM   3901 O  O    . ILE   B 2 245 ? -21.400 -30.061 24.870  1.00 42.87 ? 750  ILE   B O    1 
ATOM   3902 C  CB   . ILE   B 2 245 ? -21.547 -32.901 23.047  1.00 33.58 ? 750  ILE   B CB   1 
ATOM   3903 C  CG1  . ILE   B 2 245 ? -20.599 -32.038 22.215  1.00 34.31 ? 750  ILE   B CG1  1 
ATOM   3904 C  CG2  . ILE   B 2 245 ? -22.377 -33.798 22.146  1.00 35.08 ? 750  ILE   B CG2  1 
ATOM   3905 C  CD1  . ILE   B 2 245 ? -19.347 -32.754 21.793  1.00 44.96 ? 750  ILE   B CD1  1 
ATOM   3906 N  N    . GLY   B 2 246 ? -21.262 -32.000 26.007  1.00 41.21 ? 751  GLY   B N    1 
ATOM   3907 C  CA   . GLY   B 2 246 ? -20.536 -31.412 27.114  1.00 38.96 ? 751  GLY   B CA   1 
ATOM   3908 C  C    . GLY   B 2 246 ? -21.321 -30.399 27.912  1.00 44.79 ? 751  GLY   B C    1 
ATOM   3909 O  O    . GLY   B 2 246 ? -20.718 -29.548 28.573  1.00 50.43 ? 751  GLY   B O    1 
ATOM   3910 N  N    . SER   B 2 247 ? -22.652 -30.476 27.878  1.00 46.44 ? 752  SER   B N    1 
ATOM   3911 C  CA   . SER   B 2 247 ? -23.527 -29.482 28.499  1.00 46.51 ? 752  SER   B CA   1 
ATOM   3912 C  C    . SER   B 2 247 ? -23.171 -28.078 28.014  1.00 52.30 ? 752  SER   B C    1 
ATOM   3913 O  O    . SER   B 2 247 ? -22.948 -27.154 28.798  1.00 48.81 ? 752  SER   B O    1 
ATOM   3914 C  CB   . SER   B 2 247 ? -23.473 -29.572 30.025  1.00 49.88 ? 752  SER   B CB   1 
ATOM   3915 O  OG   . SER   B 2 247 ? -24.490 -28.782 30.618  1.00 52.11 ? 752  SER   B OG   1 
ATOM   3916 N  N    . GLY   B 2 248 ? -23.110 -27.931 26.693  1.00 55.97 ? 753  GLY   B N    1 
ATOM   3917 C  CA   . GLY   B 2 248 ? -22.752 -26.667 26.085  1.00 50.43 ? 753  GLY   B CA   1 
ATOM   3918 C  C    . GLY   B 2 248 ? -21.262 -26.400 26.099  1.00 53.44 ? 753  GLY   B C    1 
ATOM   3919 O  O    . GLY   B 2 248 ? -20.824 -25.327 26.526  1.00 56.59 ? 753  GLY   B O    1 
ATOM   3920 N  N    . TYR   B 2 249 ? -20.470 -27.364 25.637  1.00 43.60 ? 754  TYR   B N    1 
ATOM   3921 C  CA   . TYR   B 2 249 ? -19.030 -27.172 25.567  1.00 39.34 ? 754  TYR   B CA   1 
ATOM   3922 C  C    . TYR   B 2 249 ? -18.649 -26.452 24.280  1.00 33.12 ? 754  TYR   B C    1 
ATOM   3923 O  O    . TYR   B 2 249 ? -19.327 -26.561 23.254  1.00 36.45 ? 754  TYR   B O    1 
ATOM   3924 C  CB   . TYR   B 2 249 ? -18.290 -28.507 25.654  1.00 40.81 ? 754  TYR   B CB   1 
ATOM   3925 C  CG   . TYR   B 2 249 ? -16.798 -28.335 25.824  1.00 47.38 ? 754  TYR   B CG   1 
ATOM   3926 C  CD1  . TYR   B 2 249 ? -16.251 -28.081 27.075  1.00 54.02 ? 754  TYR   B CD1  1 
ATOM   3927 C  CD2  . TYR   B 2 249 ? -15.937 -28.410 24.736  1.00 43.41 ? 754  TYR   B CD2  1 
ATOM   3928 C  CE1  . TYR   B 2 249 ? -14.889 -27.914 27.239  1.00 55.41 ? 754  TYR   B CE1  1 
ATOM   3929 C  CE2  . TYR   B 2 249 ? -14.572 -28.242 24.890  1.00 48.01 ? 754  TYR   B CE2  1 
ATOM   3930 C  CZ   . TYR   B 2 249 ? -14.054 -27.996 26.145  1.00 58.23 ? 754  TYR   B CZ   1 
ATOM   3931 O  OH   . TYR   B 2 249 ? -12.697 -27.829 26.310  1.00 61.31 ? 754  TYR   B OH   1 
ATOM   3932 N  N    . ILE   B 2 250 ? -17.543 -25.714 24.344  1.00 32.69 ? 755  ILE   B N    1 
ATOM   3933 C  CA   . ILE   B 2 250 ? -17.087 -24.869 23.248  1.00 30.84 ? 755  ILE   B CA   1 
ATOM   3934 C  C    . ILE   B 2 250 ? -15.605 -25.131 23.021  1.00 32.28 ? 755  ILE   B C    1 
ATOM   3935 O  O    . ILE   B 2 250 ? -14.789 -24.923 23.927  1.00 28.08 ? 755  ILE   B O    1 
ATOM   3936 C  CB   . ILE   B 2 250 ? -17.330 -23.379 23.537  1.00 28.31 ? 755  ILE   B CB   1 
ATOM   3937 C  CG1  . ILE   B 2 250 ? -18.827 -23.095 23.679  1.00 26.38 ? 755  ILE   B CG1  1 
ATOM   3938 C  CG2  . ILE   B 2 250 ? -16.708 -22.517 22.453  1.00 24.81 ? 755  ILE   B CG2  1 
ATOM   3939 C  CD1  . ILE   B 2 250 ? -19.141 -21.694 24.156  1.00 21.43 ? 755  ILE   B CD1  1 
ATOM   3940 N  N    . PHE   B 2 251 ? -15.259 -25.587 21.821  1.00 27.99 ? 756  PHE   B N    1 
ATOM   3941 C  CA   . PHE   B 2 251 ? -13.867 -25.688 21.411  1.00 26.93 ? 756  PHE   B CA   1 
ATOM   3942 C  C    . PHE   B 2 251 ? -13.443 -24.399 20.718  1.00 22.50 ? 756  PHE   B C    1 
ATOM   3943 O  O    . PHE   B 2 251 ? -14.235 -23.760 20.020  1.00 24.83 ? 756  PHE   B O    1 
ATOM   3944 C  CB   . PHE   B 2 251 ? -13.649 -26.879 20.474  1.00 26.56 ? 756  PHE   B CB   1 
ATOM   3945 C  CG   . PHE   B 2 251 ? -12.238 -26.998 19.964  1.00 35.82 ? 756  PHE   B CG   1 
ATOM   3946 C  CD1  . PHE   B 2 251 ? -11.240 -27.527 20.765  1.00 37.23 ? 756  PHE   B CD1  1 
ATOM   3947 C  CD2  . PHE   B 2 251 ? -11.908 -26.570 18.687  1.00 32.52 ? 756  PHE   B CD2  1 
ATOM   3948 C  CE1  . PHE   B 2 251 ? -9.940  -27.633 20.302  1.00 38.44 ? 756  PHE   B CE1  1 
ATOM   3949 C  CE2  . PHE   B 2 251 ? -10.610 -26.672 18.218  1.00 27.96 ? 756  PHE   B CE2  1 
ATOM   3950 C  CZ   . PHE   B 2 251 ? -9.624  -27.205 19.027  1.00 36.50 ? 756  PHE   B CZ   1 
ATOM   3951 N  N    . ALA   B 2 252 ? -12.179 -24.024 20.921  1.00 24.41 ? 757  ALA   B N    1 
ATOM   3952 C  CA   . ALA   B 2 252 ? -11.609 -22.801 20.356  1.00 19.07 ? 757  ALA   B CA   1 
ATOM   3953 C  C    . ALA   B 2 252 ? -12.452 -21.585 20.742  1.00 19.15 ? 757  ALA   B C    1 
ATOM   3954 O  O    . ALA   B 2 252 ? -13.055 -20.914 19.901  1.00 16.16 ? 757  ALA   B O    1 
ATOM   3955 C  CB   . ALA   B 2 252 ? -11.458 -22.916 18.835  1.00 17.68 ? 757  ALA   B CB   1 
ATOM   3956 N  N    . THR   B 2 253 ? -12.482 -21.317 22.046  1.00 21.51 ? 758  THR   B N    1 
ATOM   3957 C  CA   . THR   B 2 253 ? -13.321 -20.253 22.580  1.00 18.56 ? 758  THR   B CA   1 
ATOM   3958 C  C    . THR   B 2 253 ? -12.933 -18.904 21.990  1.00 21.40 ? 758  THR   B C    1 
ATOM   3959 O  O    . THR   B 2 253 ? -11.759 -18.520 21.991  1.00 17.82 ? 758  THR   B O    1 
ATOM   3960 C  CB   . THR   B 2 253 ? -13.216 -20.208 24.104  1.00 22.67 ? 758  THR   B CB   1 
ATOM   3961 O  OG1  . THR   B 2 253 ? -11.852 -19.987 24.484  1.00 27.37 ? 758  THR   B OG1  1 
ATOM   3962 C  CG2  . THR   B 2 253 ? -13.705 -21.515 24.712  1.00 25.88 ? 758  THR   B CG2  1 
ATOM   3963 N  N    . THR   B 2 254 ? -13.933 -18.192 21.476  1.00 16.90 ? 759  THR   B N    1 
ATOM   3964 C  CA   . THR   B 2 254 ? -13.753 -16.845 20.953  1.00 15.19 ? 759  THR   B CA   1 
ATOM   3965 C  C    . THR   B 2 254 ? -15.052 -16.072 21.135  1.00 17.54 ? 759  THR   B C    1 
ATOM   3966 O  O    . THR   B 2 254 ? -15.824 -16.362 22.056  1.00 17.11 ? 759  THR   B O    1 
ATOM   3967 C  CB   . THR   B 2 254 ? -13.328 -16.884 19.483  1.00 14.78 ? 759  THR   B CB   1 
ATOM   3968 O  OG1  . THR   B 2 254 ? -13.212 -15.548 18.976  1.00 14.53 ? 759  THR   B OG1  1 
ATOM   3969 C  CG2  . THR   B 2 254 ? -14.333 -17.672 18.645  1.00 14.02 ? 759  THR   B CG2  1 
ATOM   3970 N  N    . GLY   B 2 255 ? -15.312 -15.092 20.276  1.00 13.87 ? 760  GLY   B N    1 
ATOM   3971 C  CA   . GLY   B 2 255 ? -16.563 -14.367 20.390  1.00 13.54 ? 760  GLY   B CA   1 
ATOM   3972 C  C    . GLY   B 2 255 ? -16.922 -13.653 19.109  1.00 16.82 ? 760  GLY   B C    1 
ATOM   3973 O  O    . GLY   B 2 255 ? -16.100 -13.488 18.205  1.00 19.49 ? 760  GLY   B O    1 
ATOM   3974 N  N    . TYR   B 2 256 ? -18.188 -13.246 19.038  1.00 17.95 ? 761  TYR   B N    1 
ATOM   3975 C  CA   . TYR   B 2 256 ? -18.606 -12.303 18.012  1.00 17.16 ? 761  TYR   B CA   1 
ATOM   3976 C  C    . TYR   B 2 256 ? -17.942 -10.958 18.267  1.00 15.00 ? 761  TYR   B C    1 
ATOM   3977 O  O    . TYR   B 2 256 ? -17.790 -10.533 19.415  1.00 15.28 ? 761  TYR   B O    1 
ATOM   3978 C  CB   . TYR   B 2 256 ? -20.127 -12.129 18.006  1.00 17.05 ? 761  TYR   B CB   1 
ATOM   3979 C  CG   . TYR   B 2 256 ? -20.933 -13.362 17.653  1.00 16.76 ? 761  TYR   B CG   1 
ATOM   3980 C  CD1  . TYR   B 2 256 ? -20.341 -14.466 17.053  1.00 16.11 ? 761  TYR   B CD1  1 
ATOM   3981 C  CD2  . TYR   B 2 256 ? -22.299 -13.409 17.907  1.00 11.90 ? 761  TYR   B CD2  1 
ATOM   3982 C  CE1  . TYR   B 2 256 ? -21.088 -15.588 16.729  1.00 15.75 ? 761  TYR   B CE1  1 
ATOM   3983 C  CE2  . TYR   B 2 256 ? -23.050 -14.522 17.588  1.00 13.44 ? 761  TYR   B CE2  1 
ATOM   3984 C  CZ   . TYR   B 2 256 ? -22.441 -15.609 17.000  1.00 17.34 ? 761  TYR   B CZ   1 
ATOM   3985 O  OH   . TYR   B 2 256 ? -23.192 -16.717 16.681  1.00 16.61 ? 761  TYR   B OH   1 
ATOM   3986 N  N    . GLY   B 2 257 ? -17.545 -10.286 17.197  1.00 17.79 ? 762  GLY   B N    1 
ATOM   3987 C  CA   . GLY   B 2 257 ? -16.878 -9.005  17.323  1.00 13.15 ? 762  GLY   B CA   1 
ATOM   3988 C  C    . GLY   B 2 257 ? -17.262 -8.072  16.198  1.00 15.10 ? 762  GLY   B C    1 
ATOM   3989 O  O    . GLY   B 2 257 ? -17.531 -8.495  15.071  1.00 15.68 ? 762  GLY   B O    1 
ATOM   3990 N  N    . ILE   B 2 258 ? -17.294 -6.781  16.524  1.00 15.65 ? 763  ILE   B N    1 
ATOM   3991 C  CA   . ILE   B 2 258 ? -17.456 -5.756  15.501  1.00 16.29 ? 763  ILE   B CA   1 
ATOM   3992 C  C    . ILE   B 2 258 ? -16.194 -5.728  14.650  1.00 19.59 ? 763  ILE   B C    1 
ATOM   3993 O  O    . ILE   B 2 258 ? -15.089 -5.512  15.160  1.00 22.37 ? 763  ILE   B O    1 
ATOM   3994 C  CB   . ILE   B 2 258 ? -17.730 -4.383  16.129  1.00 18.05 ? 763  ILE   B CB   1 
ATOM   3995 C  CG1  . ILE   B 2 258 ? -18.806 -4.484  17.214  1.00 18.53 ? 763  ILE   B CG1  1 
ATOM   3996 C  CG2  . ILE   B 2 258 ? -18.144 -3.385  15.059  1.00 19.13 ? 763  ILE   B CG2  1 
ATOM   3997 C  CD1  . ILE   B 2 258 ? -20.202 -4.713  16.676  1.00 21.05 ? 763  ILE   B CD1  1 
ATOM   3998 N  N    . ALA   B 2 259 ? -16.348 -5.969  13.352  1.00 14.69 ? 764  ALA   B N    1 
ATOM   3999 C  CA   . ALA   B 2 259 ? -15.236 -5.854  12.423  1.00 21.25 ? 764  ALA   B CA   1 
ATOM   4000 C  C    . ALA   B 2 259 ? -15.091 -4.405  11.986  1.00 22.16 ? 764  ALA   B C    1 
ATOM   4001 O  O    . ALA   B 2 259 ? -16.084 -3.726  11.718  1.00 20.15 ? 764  ALA   B O    1 
ATOM   4002 C  CB   . ALA   B 2 259 ? -15.443 -6.751  11.204  1.00 15.22 ? 764  ALA   B CB   1 
ATOM   4003 N  N    . LEU   B 2 260 ? -13.850 -3.931  11.933  1.00 19.95 ? 765  LEU   B N    1 
ATOM   4004 C  CA   . LEU   B 2 260 ? -13.557 -2.587  11.460  1.00 22.79 ? 765  LEU   B CA   1 
ATOM   4005 C  C    . LEU   B 2 260 ? -12.319 -2.635  10.579  1.00 25.41 ? 765  LEU   B C    1 
ATOM   4006 O  O    . LEU   B 2 260 ? -11.552 -3.601  10.602  1.00 19.81 ? 765  LEU   B O    1 
ATOM   4007 C  CB   . LEU   B 2 260 ? -13.340 -1.599  12.617  1.00 19.10 ? 765  LEU   B CB   1 
ATOM   4008 C  CG   . LEU   B 2 260 ? -14.389 -1.534  13.731  1.00 21.69 ? 765  LEU   B CG   1 
ATOM   4009 C  CD1  . LEU   B 2 260 ? -13.988 -2.411  14.907  1.00 17.92 ? 765  LEU   B CD1  1 
ATOM   4010 C  CD2  . LEU   B 2 260 ? -14.604 -0.096  14.179  1.00 21.63 ? 765  LEU   B CD2  1 
ATOM   4011 N  N    . GLN   B 2 261 ? -12.137 -1.580  9.790   1.00 25.59 ? 766  GLN   B N    1 
ATOM   4012 C  CA   . GLN   B 2 261 ? -10.937 -1.463  8.977   1.00 25.60 ? 766  GLN   B CA   1 
ATOM   4013 C  C    . GLN   B 2 261 ? -9.709  -1.338  9.871   1.00 26.57 ? 766  GLN   B C    1 
ATOM   4014 O  O    . GLN   B 2 261 ? -9.777  -0.818  10.988  1.00 27.00 ? 766  GLN   B O    1 
ATOM   4015 C  CB   . GLN   B 2 261 ? -11.040 -0.258  8.041   1.00 25.03 ? 766  GLN   B CB   1 
ATOM   4016 C  CG   . GLN   B 2 261 ? -12.240 -0.308  7.105   1.00 32.27 ? 766  GLN   B CG   1 
ATOM   4017 C  CD   . GLN   B 2 261 ? -12.415 0.969   6.304   1.00 35.88 ? 766  GLN   B CD   1 
ATOM   4018 O  OE1  . GLN   B 2 261 ? -11.511 1.801   6.232   1.00 39.24 ? 766  GLN   B OE1  1 
ATOM   4019 N  NE2  . GLN   B 2 261 ? -13.585 1.128   5.695   1.00 35.18 ? 766  GLN   B NE2  1 
ATOM   4020 N  N    . LYS   B 2 262 ? -8.582  -1.841  9.376   1.00 27.43 ? 767  LYS   B N    1 
ATOM   4021 C  CA   . LYS   B 2 262 ? -7.353  -1.813  10.157  1.00 26.13 ? 767  LYS   B CA   1 
ATOM   4022 C  C    . LYS   B 2 262 ? -6.923  -0.375  10.409  1.00 26.21 ? 767  LYS   B C    1 
ATOM   4023 O  O    . LYS   B 2 262 ? -6.764  0.415   9.473   1.00 27.53 ? 767  LYS   B O    1 
ATOM   4024 C  CB   . LYS   B 2 262 ? -6.250  -2.588  9.437   1.00 28.65 ? 767  LYS   B CB   1 
ATOM   4025 C  CG   . LYS   B 2 262 ? -6.608  -4.039  9.164   1.00 28.56 ? 767  LYS   B CG   1 
ATOM   4026 C  CD   . LYS   B 2 262 ? -5.392  -4.847  8.747   1.00 34.77 ? 767  LYS   B CD   1 
ATOM   4027 C  CE   . LYS   B 2 262 ? -4.485  -5.129  9.933   1.00 37.30 ? 767  LYS   B CE   1 
ATOM   4028 N  NZ   . LYS   B 2 262 ? -5.197  -5.845  11.029  1.00 41.48 ? 767  LYS   B NZ   1 
ATOM   4029 N  N    . GLY   B 2 263 ? -6.745  -0.035  11.684  1.00 26.96 ? 768  GLY   B N    1 
ATOM   4030 C  CA   . GLY   B 2 263 ? -6.451  1.331   12.061  1.00 31.32 ? 768  GLY   B CA   1 
ATOM   4031 C  C    . GLY   B 2 263 ? -7.664  2.221   12.182  1.00 28.56 ? 768  GLY   B C    1 
ATOM   4032 O  O    . GLY   B 2 263 ? -7.523  3.447   12.156  1.00 38.72 ? 768  GLY   B O    1 
ATOM   4033 N  N    . SER   B 2 264 ? -8.852  1.639   12.318  1.00 32.12 ? 769  SER   B N    1 
ATOM   4034 C  CA   . SER   B 2 264 ? -10.076 2.425   12.364  1.00 30.47 ? 769  SER   B CA   1 
ATOM   4035 C  C    . SER   B 2 264 ? -10.075 3.342   13.583  1.00 27.94 ? 769  SER   B C    1 
ATOM   4036 O  O    . SER   B 2 264 ? -9.784  2.885   14.697  1.00 28.93 ? 769  SER   B O    1 
ATOM   4037 C  CB   . SER   B 2 264 ? -11.296 1.507   12.406  1.00 27.07 ? 769  SER   B CB   1 
ATOM   4038 O  OG   . SER   B 2 264 ? -12.494 2.253   12.535  1.00 30.23 ? 769  SER   B OG   1 
ATOM   4039 N  N    . PRO   B 2 265 ? -10.391 4.630   13.421  1.00 29.61 ? 770  PRO   B N    1 
ATOM   4040 C  CA   . PRO   B 2 265 ? -10.487 5.517   14.590  1.00 28.61 ? 770  PRO   B CA   1 
ATOM   4041 C  C    . PRO   B 2 265 ? -11.698 5.241   15.465  1.00 28.52 ? 770  PRO   B C    1 
ATOM   4042 O  O    . PRO   B 2 265 ? -11.795 5.822   16.554  1.00 34.50 ? 770  PRO   B O    1 
ATOM   4043 C  CB   . PRO   B 2 265 ? -10.562 6.915   13.963  1.00 30.37 ? 770  PRO   B CB   1 
ATOM   4044 C  CG   . PRO   B 2 265 ? -11.147 6.683   12.609  1.00 30.72 ? 770  PRO   B CG   1 
ATOM   4045 C  CD   . PRO   B 2 265 ? -10.637 5.343   12.156  1.00 29.07 ? 770  PRO   B CD   1 
ATOM   4046 N  N    . TRP   B 2 266 ? -12.617 4.380   15.031  1.00 27.47 ? 771  TRP   B N    1 
ATOM   4047 C  CA   . TRP   B 2 266 ? -13.805 4.056   15.807  1.00 25.34 ? 771  TRP   B CA   1 
ATOM   4048 C  C    . TRP   B 2 266 ? -13.582 2.931   16.809  1.00 31.61 ? 771  TRP   B C    1 
ATOM   4049 O  O    . TRP   B 2 266 ? -14.412 2.756   17.706  1.00 27.59 ? 771  TRP   B O    1 
ATOM   4050 C  CB   . TRP   B 2 266 ? -14.961 3.665   14.875  1.00 24.32 ? 771  TRP   B CB   1 
ATOM   4051 C  CG   . TRP   B 2 266 ? -15.411 4.761   13.953  1.00 26.48 ? 771  TRP   B CG   1 
ATOM   4052 C  CD1  . TRP   B 2 266 ? -15.146 4.871   12.619  1.00 24.97 ? 771  TRP   B CD1  1 
ATOM   4053 C  CD2  . TRP   B 2 266 ? -16.212 5.897   14.298  1.00 25.13 ? 771  TRP   B CD2  1 
ATOM   4054 N  NE1  . TRP   B 2 266 ? -15.730 6.007   12.112  1.00 25.76 ? 771  TRP   B NE1  1 
ATOM   4055 C  CE2  . TRP   B 2 266 ? -16.390 6.654   13.123  1.00 26.11 ? 771  TRP   B CE2  1 
ATOM   4056 C  CE3  . TRP   B 2 266 ? -16.795 6.348   15.486  1.00 25.45 ? 771  TRP   B CE3  1 
ATOM   4057 C  CZ2  . TRP   B 2 266 ? -17.126 7.837   13.102  1.00 31.07 ? 771  TRP   B CZ2  1 
ATOM   4058 C  CZ3  . TRP   B 2 266 ? -17.525 7.522   15.463  1.00 28.13 ? 771  TRP   B CZ3  1 
ATOM   4059 C  CH2  . TRP   B 2 266 ? -17.684 8.253   14.279  1.00 27.62 ? 771  TRP   B CH2  1 
ATOM   4060 N  N    . LYS   B 2 267 ? -12.484 2.178   16.691  1.00 26.99 ? 772  LYS   B N    1 
ATOM   4061 C  CA   . LYS   B 2 267 ? -12.331 0.956   17.478  1.00 23.81 ? 772  LYS   B CA   1 
ATOM   4062 C  C    . LYS   B 2 267 ? -12.286 1.249   18.973  1.00 23.77 ? 772  LYS   B C    1 
ATOM   4063 O  O    . LYS   B 2 267 ? -12.975 0.595   19.764  1.00 22.38 ? 772  LYS   B O    1 
ATOM   4064 C  CB   . LYS   B 2 267 ? -11.072 0.202   17.047  1.00 21.66 ? 772  LYS   B CB   1 
ATOM   4065 C  CG   . LYS   B 2 267 ? -10.759 -0.996  17.933  1.00 26.22 ? 772  LYS   B CG   1 
ATOM   4066 C  CD   . LYS   B 2 267 ? -9.441  -1.653  17.564  1.00 31.18 ? 772  LYS   B CD   1 
ATOM   4067 C  CE   . LYS   B 2 267 ? -8.910  -2.487  18.718  1.00 22.82 ? 772  LYS   B CE   1 
ATOM   4068 N  NZ   . LYS   B 2 267 ? -9.891  -3.522  19.152  1.00 38.19 ? 772  LYS   B NZ   1 
ATOM   4069 N  N    . ARG   B 2 268 ? -11.470 2.226   19.381  1.00 22.48 ? 773  ARG   B N    1 
ATOM   4070 C  CA   . ARG   B 2 268 ? -11.295 2.499   20.805  1.00 26.36 ? 773  ARG   B CA   1 
ATOM   4071 C  C    . ARG   B 2 268 ? -12.621 2.864   21.463  1.00 30.52 ? 773  ARG   B C    1 
ATOM   4072 O  O    . ARG   B 2 268 ? -12.954 2.354   22.540  1.00 27.56 ? 773  ARG   B O    1 
ATOM   4073 C  CB   . ARG   B 2 268 ? -10.271 3.616   21.008  1.00 25.84 ? 773  ARG   B CB   1 
ATOM   4074 C  CG   . ARG   B 2 268 ? -10.287 4.204   22.411  1.00 33.63 ? 773  ARG   B CG   1 
ATOM   4075 C  CD   . ARG   B 2 268 ? -9.350  5.391   22.535  1.00 41.76 ? 773  ARG   B CD   1 
ATOM   4076 N  NE   . ARG   B 2 268 ? -9.880  6.574   21.868  1.00 53.93 ? 773  ARG   B NE   1 
ATOM   4077 C  CZ   . ARG   B 2 268 ? -10.795 7.381   22.388  1.00 57.27 ? 773  ARG   B CZ   1 
ATOM   4078 N  NH1  . ARG   B 2 268 ? -11.326 7.148   23.577  1.00 48.40 ? 773  ARG   B NH1  1 
ATOM   4079 N  NH2  . ARG   B 2 268 ? -11.190 8.446   21.697  1.00 61.70 ? 773  ARG   B NH2  1 
ATOM   4080 N  N    . GLN   B 2 269 ? -13.395 3.745   20.825  1.00 29.95 ? 774  GLN   B N    1 
ATOM   4081 C  CA   . GLN   B 2 269 ? -14.687 4.126   21.386  1.00 30.31 ? 774  GLN   B CA   1 
ATOM   4082 C  C    . GLN   B 2 269 ? -15.670 2.962   21.384  1.00 24.77 ? 774  GLN   B C    1 
ATOM   4083 O  O    . GLN   B 2 269 ? -16.492 2.848   22.301  1.00 26.80 ? 774  GLN   B O    1 
ATOM   4084 C  CB   . GLN   B 2 269 ? -15.267 5.312   20.615  1.00 34.49 ? 774  GLN   B CB   1 
ATOM   4085 C  CG   . GLN   B 2 269 ? -14.669 6.655   20.995  1.00 32.75 ? 774  GLN   B CG   1 
ATOM   4086 C  CD   . GLN   B 2 269 ? -15.311 7.808   20.249  1.00 41.06 ? 774  GLN   B CD   1 
ATOM   4087 O  OE1  . GLN   B 2 269 ? -14.883 8.170   19.154  1.00 35.71 ? 774  GLN   B OE1  1 
ATOM   4088 N  NE2  . GLN   B 2 269 ? -16.345 8.393   20.842  1.00 43.08 ? 774  GLN   B NE2  1 
ATOM   4089 N  N    . ILE   B 2 270 ? -15.607 2.094   20.372  1.00 24.19 ? 775  ILE   B N    1 
ATOM   4090 C  CA   . ILE   B 2 270 ? -16.478 0.922   20.347  1.00 25.63 ? 775  ILE   B CA   1 
ATOM   4091 C  C    . ILE   B 2 270 ? -16.127 -0.025  21.486  1.00 25.08 ? 775  ILE   B C    1 
ATOM   4092 O  O    . ILE   B 2 270 ? -17.014 -0.566  22.159  1.00 20.88 ? 775  ILE   B O    1 
ATOM   4093 C  CB   . ILE   B 2 270 ? -16.397 0.216   18.979  1.00 23.67 ? 775  ILE   B CB   1 
ATOM   4094 C  CG1  . ILE   B 2 270 ? -16.994 1.096   17.879  1.00 22.81 ? 775  ILE   B CG1  1 
ATOM   4095 C  CG2  . ILE   B 2 270 ? -17.104 -1.131  19.027  1.00 20.74 ? 775  ILE   B CG2  1 
ATOM   4096 C  CD1  . ILE   B 2 270 ? -18.465 1.382   18.050  1.00 22.10 ? 775  ILE   B CD1  1 
ATOM   4097 N  N    . ASP   B 2 271 ? -14.830 -0.237  21.723  1.00 21.89 ? 776  ASP   B N    1 
ATOM   4098 C  CA   . ASP   B 2 271 ? -14.405 -1.125  22.802  1.00 21.09 ? 776  ASP   B CA   1 
ATOM   4099 C  C    . ASP   B 2 271 ? -14.851 -0.596  24.158  1.00 25.76 ? 776  ASP   B C    1 
ATOM   4100 O  O    . ASP   B 2 271 ? -15.431 -1.332  24.964  1.00 23.29 ? 776  ASP   B O    1 
ATOM   4101 C  CB   . ASP   B 2 271 ? -12.887 -1.303  22.769  1.00 21.71 ? 776  ASP   B CB   1 
ATOM   4102 C  CG   . ASP   B 2 271 ? -12.435 -2.226  21.659  1.00 22.71 ? 776  ASP   B CG   1 
ATOM   4103 O  OD1  . ASP   B 2 271 ? -13.284 -2.975  21.135  1.00 26.02 ? 776  ASP   B OD1  1 
ATOM   4104 O  OD2  . ASP   B 2 271 ? -11.235 -2.210  21.314  1.00 21.17 ? 776  ASP   B OD2  1 
ATOM   4105 N  N    . LEU   B 2 272 ? -14.591 0.686   24.425  1.00 26.62 ? 777  LEU   B N    1 
ATOM   4106 C  CA   . LEU   B 2 272 ? -14.964 1.265   25.712  1.00 28.01 ? 777  LEU   B CA   1 
ATOM   4107 C  C    . LEU   B 2 272 ? -16.469 1.204   25.931  1.00 25.44 ? 777  LEU   B C    1 
ATOM   4108 O  O    . LEU   B 2 272 ? -16.931 0.978   27.056  1.00 26.42 ? 777  LEU   B O    1 
ATOM   4109 C  CB   . LEU   B 2 272 ? -14.466 2.707   25.800  1.00 27.36 ? 777  LEU   B CB   1 
ATOM   4110 C  CG   . LEU   B 2 272 ? -12.950 2.868   25.905  1.00 27.98 ? 777  LEU   B CG   1 
ATOM   4111 C  CD1  . LEU   B 2 272 ? -12.562 4.338   25.890  1.00 30.05 ? 777  LEU   B CD1  1 
ATOM   4112 C  CD2  . LEU   B 2 272 ? -12.426 2.182   27.157  1.00 28.64 ? 777  LEU   B CD2  1 
ATOM   4113 N  N    . ALA   B 2 273 ? -17.251 1.398   24.868  1.00 24.99 ? 778  ALA   B N    1 
ATOM   4114 C  CA   . ALA   B 2 273 ? -18.702 1.317   24.991  1.00 27.86 ? 778  ALA   B CA   1 
ATOM   4115 C  C    . ALA   B 2 273 ? -19.147 -0.103  25.320  1.00 25.60 ? 778  ALA   B C    1 
ATOM   4116 O  O    . ALA   B 2 273 ? -19.971 -0.316  26.217  1.00 24.25 ? 778  ALA   B O    1 
ATOM   4117 C  CB   . ALA   B 2 273 ? -19.366 1.810   23.706  1.00 24.07 ? 778  ALA   B CB   1 
ATOM   4118 N  N    . LEU   B 2 274 ? -18.604 -1.092  24.604  1.00 23.21 ? 779  LEU   B N    1 
ATOM   4119 C  CA   . LEU   B 2 274 ? -18.976 -2.483  24.852  1.00 25.05 ? 779  LEU   B CA   1 
ATOM   4120 C  C    . LEU   B 2 274 ? -18.611 -2.907  26.270  1.00 27.86 ? 779  LEU   B C    1 
ATOM   4121 O  O    . LEU   B 2 274 ? -19.419 -3.527  26.972  1.00 24.19 ? 779  LEU   B O    1 
ATOM   4122 C  CB   . LEU   B 2 274 ? -18.305 -3.396  23.825  1.00 18.49 ? 779  LEU   B CB   1 
ATOM   4123 C  CG   . LEU   B 2 274 ? -18.835 -3.320  22.391  1.00 21.38 ? 779  LEU   B CG   1 
ATOM   4124 C  CD1  . LEU   B 2 274 ? -18.040 -4.237  21.473  1.00 15.73 ? 779  LEU   B CD1  1 
ATOM   4125 C  CD2  . LEU   B 2 274 ? -20.318 -3.661  22.347  1.00 17.17 ? 779  LEU   B CD2  1 
ATOM   4126 N  N    . LEU   B 2 275 ? -17.393 -2.581  26.709  1.00 23.76 ? 780  LEU   B N    1 
ATOM   4127 C  CA   . LEU   B 2 275 ? -16.994 -2.900  28.077  1.00 23.85 ? 780  LEU   B CA   1 
ATOM   4128 C  C    . LEU   B 2 275 ? -17.828 -2.136  29.096  1.00 25.58 ? 780  LEU   B C    1 
ATOM   4129 O  O    . LEU   B 2 275 ? -18.076 -2.640  30.198  1.00 26.58 ? 780  LEU   B O    1 
ATOM   4130 C  CB   . LEU   B 2 275 ? -15.505 -2.606  28.274  1.00 26.33 ? 780  LEU   B CB   1 
ATOM   4131 C  CG   . LEU   B 2 275 ? -14.546 -3.285  27.294  1.00 22.45 ? 780  LEU   B CG   1 
ATOM   4132 C  CD1  . LEU   B 2 275 ? -13.101 -2.994  27.656  1.00 23.42 ? 780  LEU   B CD1  1 
ATOM   4133 C  CD2  . LEU   B 2 275 ? -14.793 -4.780  27.260  1.00 28.14 ? 780  LEU   B CD2  1 
ATOM   4134 N  N    . GLN   B 2 276 ? -18.275 -0.926  28.750  1.00 26.39 ? 781  GLN   B N    1 
ATOM   4135 C  CA   . GLN   B 2 276 ? -19.153 -0.185  29.649  1.00 28.43 ? 781  GLN   B CA   1 
ATOM   4136 C  C    . GLN   B 2 276 ? -20.546 -0.801  29.687  1.00 28.05 ? 781  GLN   B C    1 
ATOM   4137 O  O    . GLN   B 2 276 ? -21.204 -0.795  30.734  1.00 32.25 ? 781  GLN   B O    1 
ATOM   4138 C  CB   . GLN   B 2 276 ? -19.225 1.282   29.224  1.00 29.55 ? 781  GLN   B CB   1 
ATOM   4139 C  CG   . GLN   B 2 276 ? -20.061 2.155   30.144  1.00 31.94 ? 781  GLN   B CG   1 
ATOM   4140 C  CD   . GLN   B 2 276 ? -21.375 2.573   29.515  1.00 41.52 ? 781  GLN   B CD   1 
ATOM   4141 O  OE1  . GLN   B 2 276 ? -21.428 3.518   28.727  1.00 43.26 ? 781  GLN   B OE1  1 
ATOM   4142 N  NE2  . GLN   B 2 276 ? -22.444 1.865   29.856  1.00 34.06 ? 781  GLN   B NE2  1 
ATOM   4143 N  N    . PHE   B 2 277 ? -21.010 -1.336  28.555  1.00 26.14 ? 782  PHE   B N    1 
ATOM   4144 C  CA   . PHE   B 2 277 ? -22.310 -2.001  28.524  1.00 31.05 ? 782  PHE   B CA   1 
ATOM   4145 C  C    . PHE   B 2 277 ? -22.334 -3.192  29.473  1.00 31.79 ? 782  PHE   B C    1 
ATOM   4146 O  O    . PHE   B 2 277 ? -23.206 -3.291  30.345  1.00 27.27 ? 782  PHE   B O    1 
ATOM   4147 C  CB   . PHE   B 2 277 ? -22.644 -2.451  27.100  1.00 23.74 ? 782  PHE   B CB   1 
ATOM   4148 C  CG   . PHE   B 2 277 ? -22.813 -1.322  26.120  1.00 25.13 ? 782  PHE   B CG   1 
ATOM   4149 C  CD1  . PHE   B 2 277 ? -23.062 -0.030  26.555  1.00 28.79 ? 782  PHE   B CD1  1 
ATOM   4150 C  CD2  . PHE   B 2 277 ? -22.725 -1.559  24.758  1.00 22.81 ? 782  PHE   B CD2  1 
ATOM   4151 C  CE1  . PHE   B 2 277 ? -23.216 1.004   25.648  1.00 28.39 ? 782  PHE   B CE1  1 
ATOM   4152 C  CE2  . PHE   B 2 277 ? -22.879 -0.531  23.848  1.00 26.18 ? 782  PHE   B CE2  1 
ATOM   4153 C  CZ   . PHE   B 2 277 ? -23.125 0.752   24.293  1.00 27.75 ? 782  PHE   B CZ   1 
ATOM   4154 N  N    . VAL   B 2 278 ? -21.376 -4.108  29.319  1.00 25.58 ? 783  VAL   B N    1 
ATOM   4155 C  CA   . VAL   B 2 278 ? -21.346 -5.293  30.168  1.00 28.45 ? 783  VAL   B CA   1 
ATOM   4156 C  C    . VAL   B 2 278 ? -21.029 -4.919  31.611  1.00 29.02 ? 783  VAL   B C    1 
ATOM   4157 O  O    . VAL   B 2 278 ? -21.541 -5.543  32.548  1.00 30.94 ? 783  VAL   B O    1 
ATOM   4158 C  CB   . VAL   B 2 278 ? -20.345 -6.325  29.608  1.00 26.86 ? 783  VAL   B CB   1 
ATOM   4159 C  CG1  . VAL   B 2 278 ? -18.937 -5.747  29.555  1.00 23.67 ? 783  VAL   B CG1  1 
ATOM   4160 C  CG2  . VAL   B 2 278 ? -20.374 -7.602  30.435  1.00 26.32 ? 783  VAL   B CG2  1 
ATOM   4161 N  N    . GLY   B 2 279 ? -20.208 -3.887  31.819  1.00 31.91 ? 784  GLY   B N    1 
ATOM   4162 C  CA   . GLY   B 2 279 ? -19.824 -3.501  33.165  1.00 32.91 ? 784  GLY   B CA   1 
ATOM   4163 C  C    . GLY   B 2 279 ? -20.964 -2.974  34.011  1.00 34.93 ? 784  GLY   B C    1 
ATOM   4164 O  O    . GLY   B 2 279 ? -20.885 -3.035  35.242  1.00 39.19 ? 784  GLY   B O    1 
ATOM   4165 N  N    . ASP   B 2 280 ? -22.021 -2.461  33.380  1.00 32.09 ? 785  ASP   B N    1 
ATOM   4166 C  CA   . ASP   B 2 280 ? -23.165 -1.908  34.093  1.00 34.11 ? 785  ASP   B CA   1 
ATOM   4167 C  C    . ASP   B 2 280 ? -24.392 -2.810  34.012  1.00 33.62 ? 785  ASP   B C    1 
ATOM   4168 O  O    . ASP   B 2 280 ? -25.511 -2.355  34.270  1.00 38.65 ? 785  ASP   B O    1 
ATOM   4169 C  CB   . ASP   B 2 280 ? -23.493 -0.512  33.562  1.00 34.80 ? 785  ASP   B CB   1 
ATOM   4170 C  CG   . ASP   B 2 280 ? -22.315 0.438   33.654  1.00 35.57 ? 785  ASP   B CG   1 
ATOM   4171 O  OD1  . ASP   B 2 280 ? -21.487 0.272   34.574  1.00 38.00 ? 785  ASP   B OD1  1 
ATOM   4172 O  OD2  . ASP   B 2 280 ? -22.215 1.350   32.807  1.00 35.28 ? 785  ASP   B OD2  1 
ATOM   4173 N  N    . GLY   B 2 281 ? -24.206 -4.079  33.656  1.00 31.87 ? 786  GLY   B N    1 
ATOM   4174 C  CA   . GLY   B 2 281 ? -25.303 -5.025  33.622  1.00 35.87 ? 786  GLY   B CA   1 
ATOM   4175 C  C    . GLY   B 2 281 ? -26.290 -4.847  32.491  1.00 32.20 ? 786  GLY   B C    1 
ATOM   4176 O  O    . GLY   B 2 281 ? -27.368 -5.447  32.533  1.00 36.57 ? 786  GLY   B O    1 
ATOM   4177 N  N    . GLU   B 2 282 ? -25.959 -4.048  31.475  1.00 33.16 ? 787  GLU   B N    1 
ATOM   4178 C  CA   . GLU   B 2 282 ? -26.899 -3.804  30.386  1.00 32.49 ? 787  GLU   B CA   1 
ATOM   4179 C  C    . GLU   B 2 282 ? -27.039 -5.001  29.454  1.00 31.99 ? 787  GLU   B C    1 
ATOM   4180 O  O    . GLU   B 2 282 ? -27.995 -5.050  28.672  1.00 31.00 ? 787  GLU   B O    1 
ATOM   4181 C  CB   . GLU   B 2 282 ? -26.470 -2.571  29.588  1.00 32.70 ? 787  GLU   B CB   1 
ATOM   4182 C  CG   . GLU   B 2 282 ? -25.822 -1.479  30.426  1.00 34.38 ? 787  GLU   B CG   1 
ATOM   4183 C  CD   . GLU   B 2 282 ? -25.958 -0.105  29.798  1.00 40.78 ? 787  GLU   B CD   1 
ATOM   4184 O  OE1  . GLU   B 2 282 ? -26.245 0.862   30.535  1.00 48.32 ? 787  GLU   B OE1  1 
ATOM   4185 O  OE2  . GLU   B 2 282 ? -25.780 0.008   28.567  1.00 40.06 ? 787  GLU   B OE2  1 
ATOM   4186 N  N    . MET   B 2 283 ? -26.117 -5.964  29.518  1.00 31.00 ? 788  MET   B N    1 
ATOM   4187 C  CA   . MET   B 2 283 ? -26.201 -7.127  28.640  1.00 27.80 ? 788  MET   B CA   1 
ATOM   4188 C  C    . MET   B 2 283 ? -27.326 -8.067  29.052  1.00 30.09 ? 788  MET   B C    1 
ATOM   4189 O  O    . MET   B 2 283 ? -27.912 -8.740  28.196  1.00 23.13 ? 788  MET   B O    1 
ATOM   4190 C  CB   . MET   B 2 283 ? -24.871 -7.881  28.631  1.00 23.55 ? 788  MET   B CB   1 
ATOM   4191 C  CG   . MET   B 2 283 ? -23.749 -7.180  27.883  1.00 22.31 ? 788  MET   B CG   1 
ATOM   4192 S  SD   . MET   B 2 283 ? -24.022 -7.127  26.104  1.00 25.24 ? 788  MET   B SD   1 
ATOM   4193 C  CE   . MET   B 2 283 ? -22.409 -6.604  25.528  1.00 21.11 ? 788  MET   B CE   1 
ATOM   4194 N  N    . GLU   B 2 284 ? -27.637 -8.129  30.352  1.00 26.04 ? 789  GLU   B N    1 
ATOM   4195 C  CA   . GLU   B 2 284 ? -28.624 -9.088  30.842  1.00 35.22 ? 789  GLU   B CA   1 
ATOM   4196 C  C    . GLU   B 2 284 ? -29.982 -8.881  30.184  1.00 35.54 ? 789  GLU   B C    1 
ATOM   4197 O  O    . GLU   B 2 284 ? -30.676 -9.852  29.859  1.00 36.81 ? 789  GLU   B O    1 
ATOM   4198 C  CB   . GLU   B 2 284 ? -28.745 -8.983  32.363  1.00 29.10 ? 789  GLU   B CB   1 
ATOM   4199 N  N    . GLU   B 2 285 ? -30.380 -7.623  29.979  1.00 34.32 ? 790  GLU   B N    1 
ATOM   4200 C  CA   . GLU   B 2 285 ? -31.665 -7.352  29.343  1.00 31.65 ? 790  GLU   B CA   1 
ATOM   4201 C  C    . GLU   B 2 285 ? -31.665 -7.795  27.885  1.00 31.43 ? 790  GLU   B C    1 
ATOM   4202 O  O    . GLU   B 2 285 ? -32.657 -8.349  27.399  1.00 33.64 ? 790  GLU   B O    1 
ATOM   4203 C  CB   . GLU   B 2 285 ? -32.005 -5.866  29.453  1.00 31.01 ? 790  GLU   B CB   1 
ATOM   4204 C  CG   . GLU   B 2 285 ? -33.168 -5.433  28.574  1.00 38.02 ? 790  GLU   B CG   1 
ATOM   4205 C  CD   . GLU   B 2 285 ? -33.518 -3.969  28.745  1.00 48.57 ? 790  GLU   B CD   1 
ATOM   4206 O  OE1  . GLU   B 2 285 ? -34.177 -3.629  29.749  1.00 46.27 ? 790  GLU   B OE1  1 
ATOM   4207 O  OE2  . GLU   B 2 285 ? -33.139 -3.159  27.873  1.00 54.82 ? 790  GLU   B OE2  1 
ATOM   4208 N  N    . LEU   B 2 286 ? -30.567 -7.552  27.168  1.00 30.40 ? 791  LEU   B N    1 
ATOM   4209 C  CA   . LEU   B 2 286 ? -30.481 -8.029  25.793  1.00 34.02 ? 791  LEU   B CA   1 
ATOM   4210 C  C    . LEU   B 2 286 ? -30.449 -9.550  25.740  1.00 31.32 ? 791  LEU   B C    1 
ATOM   4211 O  O    . LEU   B 2 286 ? -30.940 -10.149 24.776  1.00 29.19 ? 791  LEU   B O    1 
ATOM   4212 C  CB   . LEU   B 2 286 ? -29.249 -7.440  25.107  1.00 26.97 ? 791  LEU   B CB   1 
ATOM   4213 C  CG   . LEU   B 2 286 ? -29.203 -5.915  25.013  1.00 31.39 ? 791  LEU   B CG   1 
ATOM   4214 C  CD1  . LEU   B 2 286 ? -28.031 -5.469  24.158  1.00 26.42 ? 791  LEU   B CD1  1 
ATOM   4215 C  CD2  . LEU   B 2 286 ? -30.515 -5.373  24.462  1.00 22.82 ? 791  LEU   B CD2  1 
ATOM   4216 N  N    . GLU   B 2 287 ? -29.888 -10.188 26.768  1.00 31.30 ? 792  GLU   B N    1 
ATOM   4217 C  CA   . GLU   B 2 287 ? -29.868 -11.645 26.819  1.00 26.95 ? 792  GLU   B CA   1 
ATOM   4218 C  C    . GLU   B 2 287 ? -31.270 -12.204 27.028  1.00 28.35 ? 792  GLU   B C    1 
ATOM   4219 O  O    . GLU   B 2 287 ? -31.690 -13.131 26.325  1.00 27.94 ? 792  GLU   B O    1 
ATOM   4220 C  CB   . GLU   B 2 287 ? -28.926 -12.118 27.926  1.00 25.55 ? 792  GLU   B CB   1 
ATOM   4221 C  CG   . GLU   B 2 287 ? -27.590 -12.639 27.423  1.00 26.45 ? 792  GLU   B CG   1 
ATOM   4222 C  CD   . GLU   B 2 287 ? -26.593 -12.855 28.543  1.00 24.69 ? 792  GLU   B CD   1 
ATOM   4223 O  OE1  . GLU   B 2 287 ? -25.724 -11.981 28.740  1.00 25.48 ? 792  GLU   B OE1  1 
ATOM   4224 O  OE2  . GLU   B 2 287 ? -26.673 -13.900 29.223  1.00 36.70 ? 792  GLU   B OE2  1 
ATOM   4225 N  N    . THR   B 2 288 ? -32.014 -11.653 27.992  1.00 31.52 ? 793  THR   B N    1 
ATOM   4226 C  CA   . THR   B 2 288 ? -33.377 -12.120 28.216  1.00 29.97 ? 793  THR   B CA   1 
ATOM   4227 C  C    . THR   B 2 288 ? -34.311 -11.725 27.080  1.00 34.39 ? 793  THR   B C    1 
ATOM   4228 O  O    . THR   B 2 288 ? -35.364 -12.348 26.913  1.00 39.50 ? 793  THR   B O    1 
ATOM   4229 C  CB   . THR   B 2 288 ? -33.917 -11.595 29.551  1.00 33.80 ? 793  THR   B CB   1 
ATOM   4230 O  OG1  . THR   B 2 288 ? -35.172 -12.225 29.842  1.00 42.58 ? 793  THR   B OG1  1 
ATOM   4231 C  CG2  . THR   B 2 288 ? -34.119 -10.090 29.507  1.00 35.02 ? 793  THR   B CG2  1 
ATOM   4232 N  N    . LEU   B 2 289 ? -33.937 -10.722 26.283  1.00 35.77 ? 794  LEU   B N    1 
ATOM   4233 C  CA   . LEU   B 2 289 ? -34.790 -10.268 25.192  1.00 31.84 ? 794  LEU   B CA   1 
ATOM   4234 C  C    . LEU   B 2 289 ? -34.684 -11.158 23.960  1.00 35.81 ? 794  LEU   B C    1 
ATOM   4235 O  O    . LEU   B 2 289 ? -35.657 -11.278 23.208  1.00 39.35 ? 794  LEU   B O    1 
ATOM   4236 C  CB   . LEU   B 2 289 ? -34.438 -8.827  24.817  1.00 33.90 ? 794  LEU   B CB   1 
ATOM   4237 C  CG   . LEU   B 2 289 ? -35.568 -7.802  24.689  1.00 41.08 ? 794  LEU   B CG   1 
ATOM   4238 C  CD1  . LEU   B 2 289 ? -36.581 -7.960  25.813  1.00 37.36 ? 794  LEU   B CD1  1 
ATOM   4239 C  CD2  . LEU   B 2 289 ? -35.005 -6.388  24.661  1.00 39.71 ? 794  LEU   B CD2  1 
ATOM   4240 N  N    . TRP   B 2 290 ? -33.531 -11.790 23.734  1.00 31.09 ? 795  TRP   B N    1 
ATOM   4241 C  CA   . TRP   B 2 290 ? -33.293 -12.456 22.458  1.00 30.39 ? 795  TRP   B CA   1 
ATOM   4242 C  C    . TRP   B 2 290 ? -32.810 -13.896 22.600  1.00 23.92 ? 795  TRP   B C    1 
ATOM   4243 O  O    . TRP   B 2 290 ? -33.041 -14.717 21.707  1.00 20.29 ? 795  TRP   B O    1 
ATOM   4244 C  CB   . TRP   B 2 290 ? -32.271 -11.662 21.637  1.00 23.74 ? 795  TRP   B CB   1 
ATOM   4245 C  CG   . TRP   B 2 290 ? -32.704 -10.267 21.294  1.00 26.52 ? 795  TRP   B CG   1 
ATOM   4246 C  CD1  . TRP   B 2 290 ? -32.267 -9.107  21.867  1.00 26.92 ? 795  TRP   B CD1  1 
ATOM   4247 C  CD2  . TRP   B 2 290 ? -33.656 -9.887  20.294  1.00 27.13 ? 795  TRP   B CD2  1 
ATOM   4248 N  NE1  . TRP   B 2 290 ? -32.891 -8.029  21.285  1.00 23.60 ? 795  TRP   B NE1  1 
ATOM   4249 C  CE2  . TRP   B 2 290 ? -33.749 -8.481  20.318  1.00 27.72 ? 795  TRP   B CE2  1 
ATOM   4250 C  CE3  . TRP   B 2 290 ? -34.441 -10.599 19.382  1.00 24.96 ? 795  TRP   B CE3  1 
ATOM   4251 C  CZ2  . TRP   B 2 290 ? -34.594 -7.775  19.464  1.00 32.27 ? 795  TRP   B CZ2  1 
ATOM   4252 C  CZ3  . TRP   B 2 290 ? -35.278 -9.896  18.537  1.00 32.35 ? 795  TRP   B CZ3  1 
ATOM   4253 C  CH2  . TRP   B 2 290 ? -35.349 -8.499  18.584  1.00 32.82 ? 795  TRP   B CH2  1 
ATOM   4254 N  N    . LEU   B 2 291 ? -32.140 -14.220 23.706  1.00 24.01 ? 796  LEU   B N    1 
ATOM   4255 C  CA   . LEU   B 2 291 ? -31.358 -15.447 23.789  1.00 24.44 ? 796  LEU   B CA   1 
ATOM   4256 C  C    . LEU   B 2 291 ? -31.962 -16.523 24.683  1.00 29.24 ? 796  LEU   B C    1 
ATOM   4257 O  O    . LEU   B 2 291 ? -31.406 -17.625 24.750  1.00 29.89 ? 796  LEU   B O    1 
ATOM   4258 C  CB   . LEU   B 2 291 ? -29.939 -15.126 24.272  1.00 25.28 ? 796  LEU   B CB   1 
ATOM   4259 C  CG   . LEU   B 2 291 ? -29.151 -14.149 23.399  1.00 26.24 ? 796  LEU   B CG   1 
ATOM   4260 C  CD1  . LEU   B 2 291 ? -27.717 -14.015 23.889  1.00 20.88 ? 796  LEU   B CD1  1 
ATOM   4261 C  CD2  . LEU   B 2 291 ? -29.184 -14.583 21.942  1.00 21.08 ? 796  LEU   B CD2  1 
ATOM   4262 N  N    . THR   B 2 292 ? -33.070 -16.252 25.366  1.00 28.56 ? 797  THR   B N    1 
ATOM   4263 C  CA   . THR   B 2 292 ? -33.629 -17.242 26.277  1.00 34.74 ? 797  THR   B CA   1 
ATOM   4264 C  C    . THR   B 2 292 ? -34.177 -18.446 25.520  1.00 31.16 ? 797  THR   B C    1 
ATOM   4265 O  O    . THR   B 2 292 ? -34.579 -18.355 24.357  1.00 37.70 ? 797  THR   B O    1 
ATOM   4266 C  CB   . THR   B 2 292 ? -34.741 -16.634 27.134  1.00 32.35 ? 797  THR   B CB   1 
ATOM   4267 O  OG1  . THR   B 2 292 ? -35.773 -16.112 26.287  1.00 34.38 ? 797  THR   B OG1  1 
ATOM   4268 C  CG2  . THR   B 2 292 ? -34.191 -15.536 28.020  1.00 35.85 ? 797  THR   B CG2  1 
ATOM   4269 N  N    . GLY   B 2 293 ? -34.187 -19.582 26.202  1.00 32.99 ? 798  GLY   B N    1 
ATOM   4270 C  CA   . GLY   B 2 293 ? -34.746 -20.798 25.646  1.00 34.94 ? 798  GLY   B CA   1 
ATOM   4271 C  C    . GLY   B 2 293 ? -35.399 -21.617 26.736  1.00 40.16 ? 798  GLY   B C    1 
ATOM   4272 O  O    . GLY   B 2 293 ? -34.943 -21.643 27.882  1.00 40.02 ? 798  GLY   B O    1 
ATOM   4273 N  N    . ILE   B 2 294 ? -36.491 -22.287 26.365  1.00 37.10 ? 799  ILE   B N    1 
ATOM   4274 C  CA   . ILE   B 2 294 ? -37.241 -23.075 27.336  1.00 37.53 ? 799  ILE   B CA   1 
ATOM   4275 C  C    . ILE   B 2 294 ? -36.441 -24.297 27.766  1.00 35.80 ? 799  ILE   B C    1 
ATOM   4276 O  O    . ILE   B 2 294 ? -36.411 -24.653 28.951  1.00 43.46 ? 799  ILE   B O    1 
ATOM   4277 C  CB   . ILE   B 2 294 ? -38.609 -23.465 26.752  1.00 43.28 ? 799  ILE   B CB   1 
ATOM   4278 C  CG1  . ILE   B 2 294 ? -39.386 -22.204 26.370  1.00 48.99 ? 799  ILE   B CG1  1 
ATOM   4279 C  CG2  . ILE   B 2 294 ? -39.387 -24.317 27.742  1.00 40.32 ? 799  ILE   B CG2  1 
ATOM   4280 C  CD1  . ILE   B 2 294 ? -40.878 -22.374 26.364  1.00 38.91 ? 799  ILE   B CD1  1 
ATOM   4281 N  N    . CYS   B 2 295 ? -35.784 -24.958 26.819  1.00 41.16 ? 800  CYS   B N    1 
ATOM   4282 C  CA   . CYS   B 2 295 ? -34.945 -26.105 27.135  1.00 41.95 ? 800  CYS   B CA   1 
ATOM   4283 C  C    . CYS   B 2 295 ? -33.710 -25.668 27.916  1.00 41.37 ? 800  CYS   B C    1 
ATOM   4284 O  O    . CYS   B 2 295 ? -33.510 -26.077 29.059  1.00 57.00 ? 800  CYS   B O    1 
ATOM   4285 C  CB   . CYS   B 2 295 ? -34.532 -26.838 25.858  1.00 39.62 ? 800  CYS   B CB   1 
ATOM   4286 S  SG   . CYS   B 2 295 ? -35.906 -27.288 24.773  1.00 35.57 ? 800  CYS   B SG   1 
HETATM 4287 N  N    . GLY   C 3 .   ? -9.264  -11.150 37.738  1.00 18.54 ? 1001 GLY   A N    1 
HETATM 4288 C  CA   . GLY   C 3 .   ? -9.073  -10.236 38.848  1.00 19.22 ? 1001 GLY   A CA   1 
HETATM 4289 C  C    . GLY   C 3 .   ? -8.575  -8.870  38.419  1.00 19.61 ? 1001 GLY   A C    1 
HETATM 4290 O  O    . GLY   C 3 .   ? -8.622  -7.909  39.188  1.00 20.59 ? 1001 GLY   A O    1 
HETATM 4291 O  OXT  . GLY   C 3 .   ? -8.108  -8.687  37.295  1.00 19.17 ? 1001 GLY   A OXT  1 
HETATM 4292 N  N    . GLU   D 4 .   ? -20.164 -17.175 12.856  1.00 13.99 ? 1001 GLU   B N    1 
HETATM 4293 C  CA   . GLU   D 4 .   ? -19.442 -17.872 11.799  1.00 14.93 ? 1001 GLU   B CA   1 
HETATM 4294 C  C    . GLU   D 4 .   ? -18.518 -16.929 11.040  1.00 15.34 ? 1001 GLU   B C    1 
HETATM 4295 O  O    . GLU   D 4 .   ? -18.433 -15.738 11.342  1.00 16.68 ? 1001 GLU   B O    1 
HETATM 4296 C  CB   . GLU   D 4 .   ? -20.420 -18.537 10.830  1.00 11.63 ? 1001 GLU   B CB   1 
HETATM 4297 C  CG   . GLU   D 4 .   ? -20.963 -19.864 11.320  1.00 14.82 ? 1001 GLU   B CG   1 
HETATM 4298 C  CD   . GLU   D 4 .   ? -19.872 -20.894 11.542  1.00 13.77 ? 1001 GLU   B CD   1 
HETATM 4299 O  OE1  . GLU   D 4 .   ? -18.932 -20.956 10.721  1.00 16.45 ? 1001 GLU   B OE1  1 
HETATM 4300 O  OE2  . GLU   D 4 .   ? -19.956 -21.641 12.539  1.00 14.85 ? 1001 GLU   B OE2  1 
HETATM 4301 O  OXT  . GLU   D 4 .   ? -17.831 -17.340 10.105  1.00 14.44 ? 1001 GLU   B OXT  1 
HETATM 4302 C  C1   . A1BRA E 5 .   ? -18.070 -7.153  25.757  1.00 16.55 ? 1002 A1BRA B C1   1 
HETATM 4303 C  C13  . A1BRA E 5 .   ? -15.375 -11.097 27.359  1.00 20.52 ? 1002 A1BRA B C13  1 
HETATM 4304 C  C14  . A1BRA E 5 .   ? -15.304 -12.074 28.350  1.00 19.95 ? 1002 A1BRA B C14  1 
HETATM 4305 C  C15  . A1BRA E 5 .   ? -16.195 -13.146 28.289  1.00 20.47 ? 1002 A1BRA B C15  1 
HETATM 4306 C  C16  . A1BRA E 5 .   ? -17.129 -13.223 27.253  1.00 17.53 ? 1002 A1BRA B C16  1 
HETATM 4307 C  C17  . A1BRA E 5 .   ? -17.180 -12.231 26.272  1.00 21.75 ? 1002 A1BRA B C17  1 
HETATM 4308 C  C19  . A1BRA E 5 .   ? -16.298 -11.151 26.315  1.00 18.03 ? 1002 A1BRA B C19  1 
HETATM 4309 C  C2   . A1BRA E 5 .   ? -18.300 -8.208  26.778  1.00 19.52 ? 1002 A1BRA B C2   1 
HETATM 4310 C  C20  . A1BRA E 5 .   ? -20.902 -10.478 27.801  1.00 17.72 ? 1002 A1BRA B C20  1 
HETATM 4311 C  C23  . A1BRA E 5 .   ? -23.009 -10.768 26.629  1.00 19.20 ? 1002 A1BRA B C23  1 
HETATM 4312 C  C24  . A1BRA E 5 .   ? -23.103 -12.189 26.202  1.00 23.12 ? 1002 A1BRA B C24  1 
HETATM 4313 C  C25  . A1BRA E 5 .   ? -24.336 -12.780 25.949  1.00 20.73 ? 1002 A1BRA B C25  1 
HETATM 4314 C  C26  . A1BRA E 5 .   ? -24.392 -14.111 25.551  1.00 20.24 ? 1002 A1BRA B C26  1 
HETATM 4315 C  C27  . A1BRA E 5 .   ? -23.195 -14.799 25.422  1.00 16.30 ? 1002 A1BRA B C27  1 
HETATM 4316 C  C29  . A1BRA E 5 .   ? -21.964 -12.962 26.044  1.00 20.57 ? 1002 A1BRA B C29  1 
HETATM 4317 C  C4   . A1BRA E 5 .   ? -19.627 -9.774  27.743  1.00 21.15 ? 1002 A1BRA B C4   1 
HETATM 4318 C  C5   . A1BRA E 5 .   ? -18.646 -10.104 28.651  1.00 18.66 ? 1002 A1BRA B C5   1 
HETATM 4319 C  C7   . A1BRA E 5 .   ? -17.309 -8.532  27.681  1.00 18.55 ? 1002 A1BRA B C7   1 
HETATM 4320 C  C9   . A1BRA E 5 .   ? -15.212 -8.596  28.398  1.00 17.70 ? 1002 A1BRA B C9   1 
HETATM 4321 N  N22  . A1BRA E 5 .   ? -21.639 -10.336 26.655  1.00 18.18 ? 1002 A1BRA B N22  1 
HETATM 4322 N  N28  . A1BRA E 5 .   ? -21.979 -14.258 25.658  1.00 19.02 ? 1002 A1BRA B N28  1 
HETATM 4323 N  N3   . A1BRA E 5 .   ? -19.495 -8.830  26.790  1.00 22.29 ? 1002 A1BRA B N3   1 
HETATM 4324 N  N6   . A1BRA E 5 .   ? -17.452 -9.477  28.634  1.00 21.22 ? 1002 A1BRA B N6   1 
HETATM 4325 O  O11  . A1BRA E 5 .   ? -13.117 -10.170 28.231  1.00 20.01 ? 1002 A1BRA B O11  1 
HETATM 4326 O  O12  . A1BRA E 5 .   ? -14.111 -9.225  26.088  1.00 19.27 ? 1002 A1BRA B O12  1 
HETATM 4327 O  O21  . A1BRA E 5 .   ? -21.207 -11.103 28.805  1.00 20.17 ? 1002 A1BRA B O21  1 
HETATM 4328 O  O8   . A1BRA E 5 .   ? -16.114 -7.846  27.600  1.00 18.88 ? 1002 A1BRA B O8   1 
HETATM 4329 S  S10  . A1BRA E 5 .   ? -14.250 -9.736  27.438  1.00 17.49 ? 1002 A1BRA B S10  1 
HETATM 4330 CL CL18 . A1BRA E 5 .   ? -18.342 -12.346 25.005  1.00 19.70 ? 1002 A1BRA B CL18 1 
HETATM 4331 O  O    . HOH   F 6 .   ? -4.231  -9.072  45.537  1.00 21.02 ? 1101 HOH   A O    1 
HETATM 4332 O  O    . HOH   F 6 .   ? -4.879  0.401   23.339  1.00 31.38 ? 1102 HOH   A O    1 
HETATM 4333 O  O    . HOH   F 6 .   ? -21.461 -5.909  58.211  1.00 46.56 ? 1103 HOH   A O    1 
HETATM 4334 O  O    . HOH   F 6 .   ? -22.363 -23.707 41.626  1.00 47.69 ? 1104 HOH   A O    1 
HETATM 4335 O  O    . HOH   F 6 .   ? -1.984  -30.369 41.117  1.00 41.96 ? 1105 HOH   A O    1 
HETATM 4336 O  O    . HOH   F 6 .   ? 11.403  -20.865 27.434  1.00 65.86 ? 1106 HOH   A O    1 
HETATM 4337 O  O    . HOH   F 6 .   ? -2.168  -10.481 31.612  1.00 16.91 ? 1107 HOH   A O    1 
HETATM 4338 O  O    . HOH   F 6 .   ? -29.556 -5.123  54.776  1.00 37.29 ? 1108 HOH   A O    1 
HETATM 4339 O  O    . HOH   F 6 .   ? -4.163  -23.290 46.070  1.00 39.83 ? 1109 HOH   A O    1 
HETATM 4340 O  O    . HOH   F 6 .   ? -3.182  -26.627 38.439  1.00 23.92 ? 1110 HOH   A O    1 
HETATM 4341 O  O    . HOH   F 6 .   ? 11.842  -18.748 27.952  1.00 38.14 ? 1111 HOH   A O    1 
HETATM 4342 O  O    . HOH   F 6 .   ? 2.521   -26.948 29.387  1.00 31.23 ? 1112 HOH   A O    1 
HETATM 4343 O  O    . HOH   F 6 .   ? 19.756  -28.416 43.012  1.00 47.19 ? 1113 HOH   A O    1 
HETATM 4344 O  O    . HOH   F 6 .   ? -8.096  -18.545 11.845  1.00 21.16 ? 1114 HOH   A O    1 
HETATM 4345 O  O    . HOH   F 6 .   ? 1.867   -0.840  41.379  1.00 22.62 ? 1115 HOH   A O    1 
HETATM 4346 O  O    . HOH   F 6 .   ? 10.421  -8.019  35.507  1.00 23.90 ? 1116 HOH   A O    1 
HETATM 4347 O  O    . HOH   F 6 .   ? 9.567   -0.065  31.132  1.00 21.01 ? 1117 HOH   A O    1 
HETATM 4348 O  O    . HOH   F 6 .   ? -12.849 2.852   40.670  1.00 29.40 ? 1118 HOH   A O    1 
HETATM 4349 O  O    . HOH   F 6 .   ? -16.748 -20.218 55.806  1.00 49.01 ? 1119 HOH   A O    1 
HETATM 4350 O  O    . HOH   F 6 .   ? 10.092  -28.708 37.261  1.00 31.55 ? 1120 HOH   A O    1 
HETATM 4351 O  O    . HOH   F 6 .   ? 4.250   -4.781  50.588  1.00 40.48 ? 1121 HOH   A O    1 
HETATM 4352 O  O    . HOH   F 6 .   ? -7.937  -24.079 22.372  1.00 23.60 ? 1122 HOH   A O    1 
HETATM 4353 O  O    . HOH   F 6 .   ? -29.876 -5.415  47.775  1.00 39.00 ? 1123 HOH   A O    1 
HETATM 4354 O  O    . HOH   F 6 .   ? -14.571 -12.627 56.956  1.00 27.03 ? 1124 HOH   A O    1 
HETATM 4355 O  O    . HOH   F 6 .   ? -1.744  -7.832  48.435  1.00 19.84 ? 1125 HOH   A O    1 
HETATM 4356 O  O    . HOH   F 6 .   ? 2.543   -21.825 47.944  1.00 34.95 ? 1126 HOH   A O    1 
HETATM 4357 O  O    . HOH   F 6 .   ? -13.345 -10.891 36.690  1.00 12.79 ? 1127 HOH   A O    1 
HETATM 4358 O  O    . HOH   F 6 .   ? 1.352   -37.979 28.470  1.00 29.44 ? 1128 HOH   A O    1 
HETATM 4359 O  O    . HOH   F 6 .   ? 2.212   -21.126 44.885  1.00 25.28 ? 1129 HOH   A O    1 
HETATM 4360 O  O    . HOH   F 6 .   ? 4.086   -25.623 22.750  1.00 38.76 ? 1130 HOH   A O    1 
HETATM 4361 O  O    . HOH   F 6 .   ? -10.300 -14.771 22.522  1.00 14.12 ? 1131 HOH   A O    1 
HETATM 4362 O  O    . HOH   F 6 .   ? -13.860 -9.209  31.457  1.00 18.50 ? 1132 HOH   A O    1 
HETATM 4363 O  O    . HOH   F 6 .   ? 1.647   -13.770 16.477  1.00 28.44 ? 1133 HOH   A O    1 
HETATM 4364 O  O    . HOH   F 6 .   ? -15.714 3.180   33.825  1.00 27.55 ? 1134 HOH   A O    1 
HETATM 4365 O  O    . HOH   F 6 .   ? -19.659 -20.597 54.066  1.00 38.36 ? 1135 HOH   A O    1 
HETATM 4366 O  O    . HOH   F 6 .   ? 9.008   -25.185 42.667  1.00 25.25 ? 1136 HOH   A O    1 
HETATM 4367 O  O    . HOH   F 6 .   ? 2.486   5.051   30.831  1.00 31.28 ? 1137 HOH   A O    1 
HETATM 4368 O  O    . HOH   F 6 .   ? -5.511  -20.129 14.000  1.00 23.18 ? 1138 HOH   A O    1 
HETATM 4369 O  O    . HOH   F 6 .   ? -24.639 -10.114 34.843  1.00 23.51 ? 1139 HOH   A O    1 
HETATM 4370 O  O    . HOH   F 6 .   ? 3.351   -2.645  42.960  1.00 30.16 ? 1140 HOH   A O    1 
HETATM 4371 O  O    . HOH   F 6 .   ? -22.137 0.262   44.300  1.00 27.73 ? 1141 HOH   A O    1 
HETATM 4372 O  O    . HOH   F 6 .   ? 2.689   -6.861  17.030  1.00 33.86 ? 1142 HOH   A O    1 
HETATM 4373 O  O    . HOH   F 6 .   ? 4.419   -23.205 33.958  1.00 17.22 ? 1143 HOH   A O    1 
HETATM 4374 O  O    . HOH   F 6 .   ? -27.543 -4.947  45.761  1.00 37.75 ? 1144 HOH   A O    1 
HETATM 4375 O  O    . HOH   F 6 .   ? -23.851 -18.464 28.272  1.00 35.77 ? 1145 HOH   A O    1 
HETATM 4376 O  O    . HOH   F 6 .   ? 13.299  -18.372 47.176  1.00 30.93 ? 1146 HOH   A O    1 
HETATM 4377 O  O    . HOH   F 6 .   ? -9.530  -21.367 13.248  1.00 18.71 ? 1147 HOH   A O    1 
HETATM 4378 O  O    . HOH   F 6 .   ? -7.793  -14.255 39.287  1.00 16.68 ? 1148 HOH   A O    1 
HETATM 4379 O  O    . HOH   F 6 .   ? -6.017  -7.176  44.065  1.00 21.26 ? 1149 HOH   A O    1 
HETATM 4380 O  O    . HOH   F 6 .   ? -11.403 -19.653 27.361  1.00 17.07 ? 1150 HOH   A O    1 
HETATM 4381 O  O    . HOH   F 6 .   ? 3.376   -7.709  48.295  1.00 34.38 ? 1151 HOH   A O    1 
HETATM 4382 O  O    . HOH   F 6 .   ? 4.039   -1.989  27.236  1.00 24.21 ? 1152 HOH   A O    1 
HETATM 4383 O  O    . HOH   F 6 .   ? 3.334   -10.184 45.127  1.00 26.05 ? 1153 HOH   A O    1 
HETATM 4384 O  O    . HOH   F 6 .   ? -14.302 -4.367  37.003  1.00 25.40 ? 1154 HOH   A O    1 
HETATM 4385 O  O    . HOH   F 6 .   ? -8.990  -20.335 27.955  1.00 24.69 ? 1155 HOH   A O    1 
HETATM 4386 O  O    . HOH   F 6 .   ? 13.793  -14.769 28.571  1.00 27.97 ? 1156 HOH   A O    1 
HETATM 4387 O  O    . HOH   F 6 .   ? -9.898  -6.317  21.527  1.00 26.41 ? 1157 HOH   A O    1 
HETATM 4388 O  O    . HOH   F 6 .   ? 17.799  -27.298 48.435  1.00 36.39 ? 1158 HOH   A O    1 
HETATM 4389 O  O    . HOH   F 6 .   ? -0.624  -29.638 27.614  1.00 36.22 ? 1159 HOH   A O    1 
HETATM 4390 O  O    . HOH   F 6 .   ? -8.279  -22.658 28.557  1.00 31.53 ? 1160 HOH   A O    1 
HETATM 4391 O  O    . HOH   F 6 .   ? -25.901 -21.751 55.498  1.00 47.60 ? 1161 HOH   A O    1 
HETATM 4392 O  O    . HOH   F 6 .   ? -1.125  6.067   38.564  1.00 27.18 ? 1162 HOH   A O    1 
HETATM 4393 O  O    . HOH   F 6 .   ? -14.871 -21.003 34.925  1.00 33.22 ? 1163 HOH   A O    1 
HETATM 4394 O  O    . HOH   F 6 .   ? -5.702  -20.673 47.746  1.00 31.04 ? 1164 HOH   A O    1 
HETATM 4395 O  O    . HOH   F 6 .   ? 4.786   -26.560 32.367  1.00 17.05 ? 1165 HOH   A O    1 
HETATM 4396 O  O    . HOH   F 6 .   ? 15.492  -36.077 34.706  1.00 47.02 ? 1166 HOH   A O    1 
HETATM 4397 O  O    . HOH   F 6 .   ? -16.732 -8.463  31.808  1.00 23.34 ? 1167 HOH   A O    1 
HETATM 4398 O  O    . HOH   F 6 .   ? 12.437  -14.402 34.549  1.00 30.58 ? 1168 HOH   A O    1 
HETATM 4399 O  O    . HOH   F 6 .   ? 6.295   -27.064 44.051  1.00 43.60 ? 1169 HOH   A O    1 
HETATM 4400 O  O    . HOH   F 6 .   ? 1.351   -12.186 44.531  1.00 16.74 ? 1170 HOH   A O    1 
HETATM 4401 O  O    . HOH   F 6 .   ? -11.887 -2.793  49.353  1.00 30.23 ? 1171 HOH   A O    1 
HETATM 4402 O  O    . HOH   F 6 .   ? -10.593 6.139   45.738  1.00 30.23 ? 1172 HOH   A O    1 
HETATM 4403 O  O    . HOH   F 6 .   ? 2.198   -12.780 14.481  1.00 34.91 ? 1173 HOH   A O    1 
HETATM 4404 O  O    . HOH   F 6 .   ? -6.863  -22.030 51.127  1.00 37.32 ? 1174 HOH   A O    1 
HETATM 4405 O  O    . HOH   F 6 .   ? 10.095  -19.041 25.764  1.00 36.05 ? 1175 HOH   A O    1 
HETATM 4406 O  O    . HOH   F 6 .   ? -18.567 -26.445 43.236  1.00 26.46 ? 1176 HOH   A O    1 
HETATM 4407 O  O    . HOH   F 6 .   ? -0.477  2.723   28.005  1.00 25.92 ? 1177 HOH   A O    1 
HETATM 4408 O  O    . HOH   F 6 .   ? -14.584 -8.437  37.479  1.00 5.12  ? 1178 HOH   A O    1 
HETATM 4409 O  O    . HOH   F 6 .   ? -16.138 4.663   28.629  1.00 39.06 ? 1179 HOH   A O    1 
HETATM 4410 O  O    . HOH   F 6 .   ? 11.497  -25.224 44.289  1.00 34.78 ? 1180 HOH   A O    1 
HETATM 4411 O  O    . HOH   F 6 .   ? -7.046  -7.347  19.004  1.00 20.97 ? 1181 HOH   A O    1 
HETATM 4412 O  O    . HOH   F 6 .   ? 1.729   -39.043 33.696  1.00 38.65 ? 1182 HOH   A O    1 
HETATM 4413 O  O    . HOH   F 6 .   ? -6.140  -19.312 44.403  1.00 29.65 ? 1183 HOH   A O    1 
HETATM 4414 O  O    . HOH   F 6 .   ? 3.376   1.325   40.536  1.00 24.83 ? 1184 HOH   A O    1 
HETATM 4415 O  O    . HOH   F 6 .   ? 1.325   -4.019  17.317  1.00 32.73 ? 1185 HOH   A O    1 
HETATM 4416 O  O    . HOH   F 6 .   ? -15.675 -6.184  35.720  1.00 26.92 ? 1186 HOH   A O    1 
HETATM 4417 O  O    . HOH   F 6 .   ? -15.795 -6.481  32.772  1.00 22.96 ? 1187 HOH   A O    1 
HETATM 4418 O  O    . HOH   F 6 .   ? -4.190  3.236   45.512  1.00 30.76 ? 1188 HOH   A O    1 
HETATM 4419 O  O    . HOH   F 6 .   ? -4.973  -12.007 45.135  1.00 27.23 ? 1189 HOH   A O    1 
HETATM 4420 O  O    . HOH   F 6 .   ? 16.682  -12.669 17.489  1.00 30.77 ? 1190 HOH   A O    1 
HETATM 4421 O  O    . HOH   F 6 .   ? -31.603 -19.423 51.015  1.00 37.92 ? 1191 HOH   A O    1 
HETATM 4422 O  O    . HOH   F 6 .   ? 4.684   -23.305 26.729  1.00 25.99 ? 1192 HOH   A O    1 
HETATM 4423 O  O    . HOH   F 6 .   ? -24.734 -8.923  39.703  1.00 29.63 ? 1193 HOH   A O    1 
HETATM 4424 O  O    . HOH   F 6 .   ? -4.846  -31.359 46.311  1.00 36.54 ? 1194 HOH   A O    1 
HETATM 4425 O  O    . HOH   F 6 .   ? -20.011 3.478   45.307  1.00 30.77 ? 1195 HOH   A O    1 
HETATM 4426 O  O    . HOH   F 6 .   ? -4.046  -22.017 14.944  1.00 26.37 ? 1196 HOH   A O    1 
HETATM 4427 O  O    . HOH   F 6 .   ? -23.718 -5.085  56.827  1.00 33.11 ? 1197 HOH   A O    1 
HETATM 4428 O  O    . HOH   F 6 .   ? -3.410  -24.010 49.013  1.00 40.23 ? 1198 HOH   A O    1 
HETATM 4429 O  O    . HOH   F 6 .   ? -6.806  -10.220 54.424  1.00 25.27 ? 1199 HOH   A O    1 
HETATM 4430 O  O    . HOH   F 6 .   ? -3.873  -17.995 44.805  1.00 25.07 ? 1200 HOH   A O    1 
HETATM 4431 O  O    . HOH   F 6 .   ? -0.810  -39.764 33.221  1.00 29.52 ? 1201 HOH   A O    1 
HETATM 4432 O  O    . HOH   F 6 .   ? 4.499   -27.527 30.364  1.00 36.25 ? 1202 HOH   A O    1 
HETATM 4433 O  O    . HOH   F 6 .   ? -7.766  -1.012  24.812  1.00 33.89 ? 1203 HOH   A O    1 
HETATM 4434 O  O    . HOH   F 6 .   ? 3.271   -7.644  55.895  1.00 39.68 ? 1204 HOH   A O    1 
HETATM 4435 O  O    . HOH   F 6 .   ? -5.465  10.148  46.149  1.00 27.66 ? 1205 HOH   A O    1 
HETATM 4436 O  O    . HOH   F 6 .   ? -30.832 -18.103 52.923  1.00 33.44 ? 1206 HOH   A O    1 
HETATM 4437 O  O    . HOH   F 6 .   ? -8.708  -3.563  23.568  1.00 24.45 ? 1207 HOH   A O    1 
HETATM 4438 O  O    . HOH   F 6 .   ? -21.717 3.306   48.744  1.00 33.19 ? 1208 HOH   A O    1 
HETATM 4439 O  O    . HOH   F 6 .   ? 3.472   -25.602 27.624  1.00 31.00 ? 1209 HOH   A O    1 
HETATM 4440 O  O    . HOH   F 6 .   ? 6.240   -23.117 24.141  1.00 37.96 ? 1210 HOH   A O    1 
HETATM 4441 O  O    . HOH   F 6 .   ? 3.345   -10.084 51.831  1.00 29.22 ? 1211 HOH   A O    1 
HETATM 4442 O  O    . HOH   F 6 .   ? 1.836   -6.162  54.772  1.00 21.47 ? 1212 HOH   A O    1 
HETATM 4443 O  O    . HOH   F 6 .   ? -21.668 -18.639 26.880  1.00 25.83 ? 1213 HOH   A O    1 
HETATM 4444 O  O    . HOH   F 6 .   ? 4.286   -13.821 15.777  1.00 29.25 ? 1214 HOH   A O    1 
HETATM 4445 O  O    . HOH   F 6 .   ? -3.554  -20.366 46.940  1.00 26.39 ? 1215 HOH   A O    1 
HETATM 4446 O  O    . HOH   F 6 .   ? -8.011  -8.385  56.092  1.00 27.88 ? 1216 HOH   A O    1 
HETATM 4447 O  O    . HOH   F 6 .   ? -26.624 -9.626  38.258  1.00 34.04 ? 1217 HOH   A O    1 
HETATM 4448 O  O    . HOH   F 6 .   ? -21.968 2.504   46.172  1.00 33.44 ? 1218 HOH   A O    1 
HETATM 4449 O  O    . HOH   F 6 .   ? -0.180  -5.219  55.697  1.00 32.20 ? 1219 HOH   A O    1 
HETATM 4450 O  O    . HOH   F 6 .   ? 2.544   -8.475  53.651  1.00 23.36 ? 1220 HOH   A O    1 
HETATM 4451 O  O    . HOH   G 6 .   ? -12.483 5.995   18.738  1.00 33.99 ? 1101 HOH   B O    1 
HETATM 4452 O  O    . HOH   G 6 .   ? -14.619 -6.256  -3.697  1.00 45.00 ? 1102 HOH   B O    1 
HETATM 4453 O  O    . HOH   G 6 .   ? -45.660 2.953   6.139   1.00 43.44 ? 1103 HOH   B O    1 
HETATM 4454 O  O    . HOH   G 6 .   ? -39.719 -11.143 12.809  1.00 34.44 ? 1104 HOH   B O    1 
HETATM 4455 O  O    . HOH   G 6 .   ? -16.786 -27.352 1.961   1.00 25.86 ? 1105 HOH   B O    1 
HETATM 4456 O  O    . HOH   G 6 .   ? -32.924 -29.230 23.283  1.00 25.84 ? 1106 HOH   B O    1 
HETATM 4457 O  O    . HOH   G 6 .   ? -19.830 -30.752 6.249   1.00 18.58 ? 1107 HOH   B O    1 
HETATM 4458 O  O    . HOH   G 6 .   ? -34.344 -14.212 10.755  1.00 22.98 ? 1108 HOH   B O    1 
HETATM 4459 O  O    . HOH   G 6 .   ? -33.776 -10.938 3.229   1.00 29.75 ? 1109 HOH   B O    1 
HETATM 4460 O  O    . HOH   G 6 .   ? -18.279 -19.306 15.847  1.00 19.97 ? 1110 HOH   B O    1 
HETATM 4461 O  O    . HOH   G 6 .   ? -7.285  -29.660 5.533   1.00 25.99 ? 1111 HOH   B O    1 
HETATM 4462 O  O    . HOH   G 6 .   ? -3.956  -27.751 14.318  1.00 21.42 ? 1112 HOH   B O    1 
HETATM 4463 O  O    . HOH   G 6 .   ? -32.425 -38.508 21.565  1.00 27.98 ? 1113 HOH   B O    1 
HETATM 4464 O  O    . HOH   G 6 .   ? -27.926 -10.810 2.706   1.00 24.86 ? 1114 HOH   B O    1 
HETATM 4465 O  O    . HOH   G 6 .   ? -6.457  -6.544  13.387  1.00 32.93 ? 1115 HOH   B O    1 
HETATM 4466 O  O    . HOH   G 6 .   ? -13.712 1.169   10.363  1.00 25.12 ? 1116 HOH   B O    1 
HETATM 4467 O  O    . HOH   G 6 .   ? -29.671 1.958   7.871   1.00 22.88 ? 1117 HOH   B O    1 
HETATM 4468 O  O    . HOH   G 6 .   ? -34.910 -15.007 20.030  1.00 31.17 ? 1118 HOH   B O    1 
HETATM 4469 O  O    . HOH   G 6 .   ? -24.816 -11.966 10.964  1.00 11.65 ? 1119 HOH   B O    1 
HETATM 4470 O  O    . HOH   G 6 .   ? -18.413 -17.135 5.202   1.00 13.26 ? 1120 HOH   B O    1 
HETATM 4471 O  O    . HOH   G 6 .   ? -24.766 -24.534 24.264  1.00 30.34 ? 1121 HOH   B O    1 
HETATM 4472 O  O    . HOH   G 6 .   ? -27.013 -18.044 21.930  1.00 26.88 ? 1122 HOH   B O    1 
HETATM 4473 O  O    . HOH   G 6 .   ? -32.940 -20.531 22.944  1.00 25.44 ? 1123 HOH   B O    1 
HETATM 4474 O  O    . HOH   G 6 .   ? -26.637 -29.505 26.048  1.00 34.83 ? 1124 HOH   B O    1 
HETATM 4475 O  O    . HOH   G 6 .   ? -27.668 -37.478 16.929  1.00 24.35 ? 1125 HOH   B O    1 
HETATM 4476 O  O    . HOH   G 6 .   ? -9.179  -35.925 11.101  1.00 20.50 ? 1126 HOH   B O    1 
HETATM 4477 O  O    . HOH   G 6 .   ? -16.649 -21.055 14.553  1.00 19.63 ? 1127 HOH   B O    1 
HETATM 4478 O  O    . HOH   G 6 .   ? -39.101 -9.150  17.973  1.00 33.00 ? 1128 HOH   B O    1 
HETATM 4479 O  O    . HOH   G 6 .   ? -33.432 -4.962  17.496  1.00 25.51 ? 1129 HOH   B O    1 
HETATM 4480 O  O    . HOH   G 6 .   ? -35.015 -4.735  20.969  1.00 37.71 ? 1130 HOH   B O    1 
HETATM 4481 O  O    . HOH   G 6 .   ? -8.945  -2.322  4.534   1.00 30.19 ? 1131 HOH   B O    1 
HETATM 4482 O  O    . HOH   G 6 .   ? -11.327 -43.378 9.693   1.00 34.76 ? 1132 HOH   B O    1 
HETATM 4483 O  O    . HOH   G 6 .   ? -4.935  -13.914 -5.547  1.00 23.03 ? 1133 HOH   B O    1 
HETATM 4484 O  O    . HOH   G 6 .   ? -14.337 -21.164 5.787   1.00 15.81 ? 1134 HOH   B O    1 
HETATM 4485 O  O    . HOH   G 6 .   ? -11.970 -20.224 12.375  1.00 14.16 ? 1135 HOH   B O    1 
HETATM 4486 O  O    . HOH   G 6 .   ? -39.326 -4.988  2.751   1.00 38.94 ? 1136 HOH   B O    1 
HETATM 4487 O  O    . HOH   G 6 .   ? -17.860 -17.568 30.417  1.00 26.68 ? 1137 HOH   B O    1 
HETATM 4488 O  O    . HOH   G 6 .   ? -10.597 -17.127 17.597  1.00 13.41 ? 1138 HOH   B O    1 
HETATM 4489 O  O    . HOH   G 6 .   ? -22.494 -18.646 24.181  1.00 23.61 ? 1139 HOH   B O    1 
HETATM 4490 O  O    . HOH   G 6 .   ? -32.407 -22.540 27.564  1.00 43.71 ? 1140 HOH   B O    1 
HETATM 4491 O  O    . HOH   G 6 .   ? -10.320 -43.630 3.873   1.00 20.96 ? 1141 HOH   B O    1 
HETATM 4492 O  O    . HOH   G 6 .   ? -20.228 -8.128  15.232  1.00 21.24 ? 1142 HOH   B O    1 
HETATM 4493 O  O    . HOH   G 6 .   ? -20.731 -28.751 22.386  1.00 26.02 ? 1143 HOH   B O    1 
HETATM 4494 O  O    . HOH   G 6 .   ? -12.304 -17.268 8.475   1.00 15.49 ? 1144 HOH   B O    1 
HETATM 4495 O  O    . HOH   G 6 .   ? -7.537  -22.332 11.692  1.00 21.13 ? 1145 HOH   B O    1 
HETATM 4496 O  O    . HOH   G 6 .   ? -29.023 -19.323 23.760  1.00 27.59 ? 1146 HOH   B O    1 
HETATM 4497 O  O    . HOH   G 6 .   ? -10.248 -16.639 20.646  1.00 14.84 ? 1147 HOH   B O    1 
HETATM 4498 O  O    . HOH   G 6 .   ? -24.697 -5.544  -1.617  1.00 18.79 ? 1148 HOH   B O    1 
HETATM 4499 O  O    . HOH   G 6 .   ? -11.472 -18.049 4.847   1.00 16.98 ? 1149 HOH   B O    1 
HETATM 4500 O  O    . HOH   G 6 .   ? -28.042 -2.361  -0.479  1.00 30.88 ? 1150 HOH   B O    1 
HETATM 4501 O  O    . HOH   G 6 .   ? -9.385  -1.401  23.214  1.00 30.85 ? 1151 HOH   B O    1 
HETATM 4502 O  O    . HOH   G 6 .   ? -9.800  -36.548 0.095   1.00 37.45 ? 1152 HOH   B O    1 
HETATM 4503 O  O    . HOH   G 6 .   ? -19.101 -0.321  33.286  1.00 29.96 ? 1153 HOH   B O    1 
HETATM 4504 O  O    . HOH   G 6 .   ? -13.985 -18.497 6.279   1.00 14.60 ? 1154 HOH   B O    1 
HETATM 4505 O  O    . HOH   G 6 .   ? -9.544  -19.359 3.009   1.00 28.22 ? 1155 HOH   B O    1 
HETATM 4506 O  O    . HOH   G 6 .   ? -22.878 -17.812 13.560  1.00 15.73 ? 1156 HOH   B O    1 
HETATM 4507 O  O    . HOH   G 6 .   ? -18.229 -22.980 8.930   1.00 16.34 ? 1157 HOH   B O    1 
HETATM 4508 O  O    . HOH   G 6 .   ? -26.093 -11.072 31.361  1.00 29.23 ? 1158 HOH   B O    1 
HETATM 4509 O  O    . HOH   G 6 .   ? -41.256 -10.008 7.235   1.00 39.09 ? 1159 HOH   B O    1 
HETATM 4510 O  O    . HOH   G 6 .   ? -27.150 -4.964  -0.127  1.00 13.11 ? 1160 HOH   B O    1 
HETATM 4511 O  O    . HOH   G 6 .   ? -8.280  0.247   15.221  1.00 30.96 ? 1161 HOH   B O    1 
HETATM 4512 O  O    . HOH   G 6 .   ? -7.560  -38.687 17.364  1.00 39.98 ? 1162 HOH   B O    1 
HETATM 4513 O  O    . HOH   G 6 .   ? -8.489  -9.446  16.792  1.00 16.22 ? 1163 HOH   B O    1 
HETATM 4514 O  O    . HOH   G 6 .   ? -28.728 -28.670 2.882   1.00 24.28 ? 1164 HOH   B O    1 
HETATM 4515 O  O    . HOH   G 6 .   ? -18.916 -16.147 2.529   1.00 20.00 ? 1165 HOH   B O    1 
HETATM 4516 O  O    . HOH   G 6 .   ? -7.180  -17.831 -0.376  1.00 25.89 ? 1166 HOH   B O    1 
HETATM 4517 O  O    . HOH   G 6 .   ? -8.407  -6.561  16.361  1.00 21.21 ? 1167 HOH   B O    1 
HETATM 4518 O  O    . HOH   G 6 .   ? -12.088 -19.923 17.401  1.00 19.42 ? 1168 HOH   B O    1 
HETATM 4519 O  O    . HOH   G 6 .   ? -17.126 4.698   24.385  1.00 31.74 ? 1169 HOH   B O    1 
HETATM 4520 O  O    . HOH   G 6 .   ? -8.313  -32.342 4.219   1.00 28.46 ? 1170 HOH   B O    1 
HETATM 4521 O  O    . HOH   G 6 .   ? -6.466  -5.527  5.119   1.00 23.82 ? 1171 HOH   B O    1 
HETATM 4522 O  O    . HOH   G 6 .   ? -18.361 11.487  16.799  1.00 41.64 ? 1172 HOH   B O    1 
HETATM 4523 O  O    . HOH   G 6 .   ? -17.819 -8.925  0.246   1.00 14.62 ? 1173 HOH   B O    1 
HETATM 4524 O  O    . HOH   G 6 .   ? -9.615  -3.507  6.771   1.00 28.97 ? 1174 HOH   B O    1 
HETATM 4525 O  O    . HOH   G 6 .   ? -20.929 -21.133 7.810   1.00 18.90 ? 1175 HOH   B O    1 
HETATM 4526 O  O    . HOH   G 6 .   ? -24.080 -42.774 20.650  1.00 34.70 ? 1176 HOH   B O    1 
HETATM 4527 O  O    . HOH   G 6 .   ? -6.683  -20.401 10.357  1.00 26.35 ? 1177 HOH   B O    1 
HETATM 4528 O  O    . HOH   G 6 .   ? -16.963 -25.139 0.521   1.00 20.30 ? 1178 HOH   B O    1 
HETATM 4529 O  O    . HOH   G 6 .   ? -30.632 1.340   5.206   1.00 26.04 ? 1179 HOH   B O    1 
HETATM 4530 O  O    . HOH   G 6 .   ? -23.900 -6.819  31.426  1.00 28.13 ? 1180 HOH   B O    1 
HETATM 4531 O  O    . HOH   G 6 .   ? -16.219 -4.003  31.979  1.00 18.35 ? 1181 HOH   B O    1 
HETATM 4532 O  O    . HOH   G 6 .   ? -35.217 -10.306 -1.328  1.00 37.11 ? 1182 HOH   B O    1 
HETATM 4533 O  O    . HOH   G 6 .   ? -23.073 -44.404 7.798   1.00 27.46 ? 1183 HOH   B O    1 
HETATM 4534 O  O    . HOH   G 6 .   ? -12.487 -23.753 -0.798  1.00 29.66 ? 1184 HOH   B O    1 
HETATM 4535 O  O    . HOH   G 6 .   ? -29.014 -14.801 5.801   1.00 30.28 ? 1185 HOH   B O    1 
HETATM 4536 O  O    . HOH   G 6 .   ? -23.097 -24.334 22.606  1.00 30.11 ? 1186 HOH   B O    1 
HETATM 4537 O  O    . HOH   G 6 .   ? -38.430 -10.364 22.652  1.00 41.48 ? 1187 HOH   B O    1 
HETATM 4538 O  O    . HOH   G 6 .   ? -31.113 -24.101 5.857   1.00 14.33 ? 1188 HOH   B O    1 
HETATM 4539 O  O    . HOH   G 6 .   ? -22.319 -7.346  -0.755  1.00 24.75 ? 1189 HOH   B O    1 
HETATM 4540 O  O    . HOH   G 6 .   ? -22.231 -22.782 25.793  1.00 34.27 ? 1190 HOH   B O    1 
HETATM 4541 O  O    . HOH   G 6 .   ? -5.989  -23.804 13.691  1.00 19.84 ? 1191 HOH   B O    1 
HETATM 4542 O  O    . HOH   G 6 .   ? -23.662 -20.172 7.916   1.00 13.83 ? 1192 HOH   B O    1 
HETATM 4543 O  O    . HOH   G 6 .   ? -35.339 0.370   4.885   1.00 27.64 ? 1193 HOH   B O    1 
HETATM 4544 O  O    . HOH   G 6 .   ? -16.177 -20.627 -1.568  1.00 32.54 ? 1194 HOH   B O    1 
HETATM 4545 O  O    . HOH   G 6 .   ? -31.917 -14.906 -15.228 1.00 23.86 ? 1195 HOH   B O    1 
HETATM 4546 O  O    . HOH   G 6 .   ? -20.271 -18.444 6.305   1.00 15.03 ? 1196 HOH   B O    1 
HETATM 4547 O  O    . HOH   G 6 .   ? -28.704 -11.763 5.041   1.00 13.35 ? 1197 HOH   B O    1 
HETATM 4548 O  O    . HOH   G 6 .   ? -30.346 -11.158 -5.871  1.00 26.48 ? 1198 HOH   B O    1 
HETATM 4549 O  O    . HOH   G 6 .   ? -21.504 -19.468 1.452   1.00 23.61 ? 1199 HOH   B O    1 
HETATM 4550 O  O    . HOH   G 6 .   ? -34.412 -25.001 17.141  1.00 31.35 ? 1200 HOH   B O    1 
HETATM 4551 O  O    . HOH   G 6 .   ? -15.800 -50.487 15.378  1.00 36.98 ? 1201 HOH   B O    1 
HETATM 4552 O  O    . HOH   G 6 .   ? -25.409 -33.705 2.656   1.00 29.80 ? 1202 HOH   B O    1 
HETATM 4553 O  O    . HOH   G 6 .   ? -41.091 -4.248  10.142  1.00 32.05 ? 1203 HOH   B O    1 
HETATM 4554 O  O    . HOH   G 6 .   ? -21.840 -4.113  -1.504  1.00 32.57 ? 1204 HOH   B O    1 
HETATM 4555 O  O    . HOH   G 6 .   ? -20.340 -8.490  -15.715 1.00 17.69 ? 1205 HOH   B O    1 
HETATM 4556 O  O    . HOH   G 6 .   ? -30.770 -21.772 7.668   1.00 21.96 ? 1206 HOH   B O    1 
HETATM 4557 O  O    . HOH   G 6 .   ? -17.351 -18.643 -0.191  1.00 22.77 ? 1207 HOH   B O    1 
HETATM 4558 O  O    . HOH   G 6 .   ? -21.165 -6.129  -2.624  1.00 37.90 ? 1208 HOH   B O    1 
HETATM 4559 O  O    . HOH   G 6 .   ? -36.521 0.090   20.342  1.00 44.10 ? 1209 HOH   B O    1 
HETATM 4560 O  O    . HOH   G 6 .   ? -18.493 -49.925 14.531  1.00 38.27 ? 1210 HOH   B O    1 
HETATM 4561 O  O    . HOH   G 6 .   ? -28.418 9.812   21.884  1.00 47.49 ? 1211 HOH   B O    1 
HETATM 4562 O  O    . HOH   G 6 .   ? -31.658 -28.692 25.088  1.00 33.95 ? 1212 HOH   B O    1 
HETATM 4563 O  O    . HOH   G 6 .   ? -10.345 -22.988 23.938  1.00 28.16 ? 1213 HOH   B O    1 
HETATM 4564 O  O    . HOH   G 6 .   ? -30.741 -27.918 29.505  1.00 39.55 ? 1214 HOH   B O    1 
HETATM 4565 O  O    . HOH   G 6 .   ? -47.334 0.355   3.976   1.00 47.70 ? 1215 HOH   B O    1 
HETATM 4566 O  O    . HOH   G 6 .   ? -28.222 -28.092 25.157  1.00 26.19 ? 1216 HOH   B O    1 
HETATM 4567 O  O    . HOH   G 6 .   ? -23.802 -9.679  -17.165 1.00 33.26 ? 1217 HOH   B O    1 
HETATM 4568 O  O    . HOH   G 6 .   ? -17.703 -22.956 -1.856  1.00 37.76 ? 1218 HOH   B O    1 
HETATM 4569 O  O    . HOH   G 6 .   ? -19.709 -17.969 0.940   1.00 18.42 ? 1219 HOH   B O    1 
HETATM 4570 O  O    . HOH   G 6 .   ? -47.387 -0.438  6.283   1.00 39.56 ? 1220 HOH   B O    1 
HETATM 4571 O  O    . HOH   G 6 .   ? -33.193 1.125   4.312   1.00 28.34 ? 1221 HOH   B O    1 
HETATM 4572 O  O    . HOH   G 6 .   ? -6.524  -4.571  17.340  1.00 28.77 ? 1222 HOH   B O    1 
HETATM 4573 O  O    . HOH   G 6 .   ? -26.246 -35.606 4.310   1.00 32.71 ? 1223 HOH   B O    1 
HETATM 4574 O  O    . HOH   G 6 .   ? -46.449 0.294   1.502   1.00 36.08 ? 1224 HOH   B O    1 
HETATM 4575 O  O    . HOH   G 6 .   ? -24.359 -9.621  32.243  1.00 25.96 ? 1225 HOH   B O    1 
HETATM 4576 O  O    . HOH   G 6 .   ? -10.432 -23.227 26.506  1.00 34.14 ? 1226 HOH   B O    1 
HETATM 4577 O  O    . HOH   G 6 .   ? -12.460 -6.781  -3.756  1.00 49.95 ? 1227 HOH   B O    1 
HETATM 4578 O  O    . HOH   G 6 .   ? -19.031 -25.640 -0.674  1.00 35.08 ? 1228 HOH   B O    1 
HETATM 4579 O  O    . HOH   G 6 .   ? -21.139 -11.652 -14.233 1.00 24.93 ? 1229 HOH   B O    1 
HETATM 4580 O  O    . HOH   G 6 .   ? -24.920 -17.798 23.754  1.00 29.27 ? 1230 HOH   B O    1 
HETATM 4581 O  O    . HOH   G 6 .   ? -5.899  -6.846  2.815   1.00 21.49 ? 1231 HOH   B O    1 
HETATM 4582 O  O    . HOH   G 6 .   ? -6.002  -5.505  0.556   1.00 35.08 ? 1232 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  ? 0.2258 0.4273 0.4993 0.0697  0.0540  -0.0450 397  ARG A N   
2    C CA  . ARG A 19  ? 0.3186 0.5088 0.5884 0.0681  0.0409  -0.0533 397  ARG A CA  
3    C C   . ARG A 19  ? 0.2698 0.4464 0.5250 0.0644  0.0437  -0.0547 397  ARG A C   
4    O O   . ARG A 19  ? 0.2476 0.4197 0.5149 0.0578  0.0472  -0.0573 397  ARG A O   
5    C CB  . ARG A 19  ? 0.1600 0.3520 0.4588 0.0629  0.0248  -0.0637 397  ARG A CB  
6    N N   . LEU A 20  ? 0.2207 0.3903 0.4513 0.0684  0.0428  -0.0529 398  LEU A N   
7    C CA  . LEU A 20  ? 0.2803 0.4388 0.4923 0.0665  0.0469  -0.0524 398  LEU A CA  
8    C C   . LEU A 20  ? 0.2572 0.4079 0.4822 0.0615  0.0329  -0.0646 398  LEU A C   
9    O O   . LEU A 20  ? 0.2434 0.3943 0.4779 0.0622  0.0170  -0.0715 398  LEU A O   
10   C CB  . LEU A 20  ? 0.2175 0.3720 0.4014 0.0718  0.0509  -0.0451 398  LEU A CB  
11   C CG  . LEU A 20  ? 0.3134 0.4706 0.4819 0.0784  0.0650  -0.0296 398  LEU A CG  
12   C CD1 . LEU A 20  ? 0.3743 0.5170 0.5263 0.0769  0.0678  -0.0261 398  LEU A CD1 
13   C CD2 . LEU A 20  ? 0.3191 0.4785 0.4738 0.0783  0.0728  -0.0237 398  LEU A CD2 
14   N N   . LYS A 21  ? 0.2274 0.3700 0.4509 0.0578  0.0382  -0.0662 399  LYS A N   
15   C CA  . LYS A 21  ? 0.2007 0.3209 0.4080 0.0498  0.0219  -0.0683 399  LYS A CA  
16   C C   . LYS A 21  ? 0.2746 0.3853 0.4493 0.0523  0.0225  -0.0647 399  LYS A C   
17   O O   . LYS A 21  ? 0.3051 0.4127 0.4599 0.0540  0.0371  -0.0589 399  LYS A O   
18   C CB  . LYS A 21  ? 0.2283 0.3329 0.4324 0.0405  0.0244  -0.0669 399  LYS A CB  
19   C CG  . LYS A 21  ? 0.3125 0.4206 0.5464 0.0337  0.0138  -0.0725 399  LYS A CG  
20   C CD  . LYS A 21  ? 0.3775 0.4700 0.6092 0.0240  0.0179  -0.0720 399  LYS A CD  
21   C CE  . LYS A 21  ? 0.5050 0.6116 0.7748 0.0190  0.0204  -0.0747 399  LYS A CE  
22   N NZ  . LYS A 21  ? 0.6158 0.7341 0.8967 0.0230  0.0447  -0.0681 399  LYS A NZ  
23   N N   . ILE A 22  ? 0.2237 0.3301 0.3932 0.0529  0.0069  -0.0677 400  ILE A N   
24   C CA  . ILE A 22  ? 0.1903 0.2895 0.3329 0.0544  0.0060  -0.0643 400  ILE A CA  
25   C C   . ILE A 22  ? 0.2290 0.3045 0.3484 0.0472  -0.0053 -0.0613 400  ILE A C   
26   O O   . ILE A 22  ? 0.2323 0.2986 0.3592 0.0430  -0.0210 -0.0647 400  ILE A O   
27   C CB  . ILE A 22  ? 0.2600 0.3674 0.4112 0.0592  -0.0033 -0.0688 400  ILE A CB  
28   C CG1 . ILE A 22  ? 0.2144 0.3458 0.3907 0.0676  0.0057  -0.0733 400  ILE A CG1 
29   C CG2 . ILE A 22  ? 0.1836 0.2867 0.3100 0.0599  -0.0019 -0.0652 400  ILE A CG2 
30   C CD1 . ILE A 22  ? 0.2505 0.3862 0.4065 0.0690  0.0245  -0.0637 400  ILE A CD1 
31   N N   . VAL A 23  ? 0.1856 0.2531 0.2766 0.0469  0.0027  -0.0549 401  VAL A N   
32   C CA  . VAL A 23  ? 0.1814 0.2280 0.2463 0.0422  -0.0067 -0.0509 401  VAL A CA  
33   C C   . VAL A 23  ? 0.2336 0.2802 0.2822 0.0439  -0.0100 -0.0469 401  VAL A C   
34   O O   . VAL A 23  ? 0.2153 0.2764 0.2635 0.0483  0.0006  -0.0457 401  VAL A O   
35   C CB  . VAL A 23  ? 0.2502 0.2857 0.2938 0.0406  0.0048  -0.0460 401  VAL A CB  
36   C CG1 . VAL A 23  ? 0.2335 0.2779 0.2595 0.0461  0.0228  -0.0393 401  VAL A CG1 
37   C CG2 . VAL A 23  ? 0.2278 0.2414 0.2481 0.0362  -0.0076 -0.0438 401  VAL A CG2 
38   N N   . THR A 24  ? 0.2261 0.2573 0.2625 0.0405  -0.0250 -0.0448 402  THR A N   
39   C CA  . THR A 24  ? 0.2115 0.2402 0.2329 0.0405  -0.0289 -0.0397 402  THR A CA  
40   C C   . THR A 24  ? 0.2108 0.2196 0.2085 0.0372  -0.0392 -0.0337 402  THR A C   
41   O O   . THR A 24  ? 0.2591 0.2572 0.2504 0.0356  -0.0425 -0.0345 402  THR A O   
42   C CB  . THR A 24  ? 0.1875 0.2227 0.2299 0.0420  -0.0383 -0.0451 402  THR A CB  
43   O OG1 . THR A 24  ? 0.2369 0.2699 0.2662 0.0409  -0.0402 -0.0402 402  THR A OG1 
44   C CG2 . THR A 24  ? 0.2033 0.2280 0.2584 0.0407  -0.0558 -0.0489 402  THR A CG2 
45   N N   . ILE A 25  ? 0.2156 0.2199 0.2005 0.0363  -0.0444 -0.0276 403  ILE A N   
46   C CA  . ILE A 25  ? 0.2571 0.2448 0.2167 0.0346  -0.0519 -0.0196 403  ILE A CA  
47   C C   . ILE A 25  ? 0.2652 0.2478 0.2263 0.0333  -0.0632 -0.0157 403  ILE A C   
48   O O   . ILE A 25  ? 0.2490 0.2411 0.2225 0.0329  -0.0608 -0.0174 403  ILE A O   
49   C CB  . ILE A 25  ? 0.2502 0.2384 0.1818 0.0356  -0.0382 -0.0112 403  ILE A CB  
50   C CG1 . ILE A 25  ? 0.2547 0.2259 0.1588 0.0354  -0.0455 -0.0031 403  ILE A CG1 
51   C CG2 . ILE A 25  ? 0.2237 0.2264 0.1536 0.0358  -0.0288 -0.0069 403  ILE A CG2 
52   C CD1 . ILE A 25  ? 0.3445 0.3157 0.2197 0.0378  -0.0322 0.0052  403  ILE A CD1 
53   N N   . HIS A 26  ? 0.2604 0.2274 0.2087 0.0329  -0.0756 -0.0107 404  HIS A N   
54   C CA  . HIS A 26  ? 0.2770 0.2361 0.2244 0.0318  -0.0857 -0.0048 404  HIS A CA  
55   C C   . HIS A 26  ? 0.3423 0.3052 0.2735 0.0294  -0.0765 0.0050  404  HIS A C   
56   O O   . HIS A 26  ? 0.3644 0.3250 0.2707 0.0299  -0.0702 0.0132  404  HIS A O   
57   C CB  . HIS A 26  ? 0.2971 0.2399 0.2318 0.0336  -0.0998 -0.0003 404  HIS A CB  
58   C CG  . HIS A 26  ? 0.3988 0.3315 0.3310 0.0333  -0.1093 0.0079  404  HIS A CG  
59   N ND1 . HIS A 26  ? 0.4382 0.3593 0.3458 0.0345  -0.1136 0.0199  404  HIS A ND1 
60   C CD2 . HIS A 26  ? 0.3805 0.3120 0.3315 0.0326  -0.1148 0.0062  404  HIS A CD2 
61   C CE1 . HIS A 26  ? 0.4186 0.3318 0.3309 0.0339  -0.1208 0.0262  404  HIS A CE1 
62   N NE2 . HIS A 26  ? 0.3991 0.3172 0.3375 0.0325  -0.1219 0.0177  404  HIS A NE2 
63   N N   . GLN A 27  ? 0.3562 0.3253 0.3017 0.0270  -0.0759 0.0038  405  GLN A N   
64   C CA  . GLN A 27  ? 0.3716 0.3478 0.3062 0.0234  -0.0673 0.0118  405  GLN A CA  
65   C C   . GLN A 27  ? 0.3575 0.3340 0.3116 0.0199  -0.0728 0.0086  405  GLN A C   
66   O O   . GLN A 27  ? 0.3226 0.3128 0.2934 0.0199  -0.0675 -0.0007 405  GLN A O   
67   C CB  . GLN A 27  ? 0.2998 0.2942 0.2289 0.0247  -0.0509 0.0099  405  GLN A CB  
68   C CG  . GLN A 27  ? 0.2740 0.2771 0.1850 0.0221  -0.0416 0.0206  405  GLN A CG  
69   C CD  . GLN A 27  ? 0.3061 0.3008 0.1875 0.0241  -0.0391 0.0322  405  GLN A CD  
70   O OE1 . GLN A 27  ? 0.2880 0.2906 0.1528 0.0231  -0.0311 0.0420  405  GLN A OE1 
71   N NE2 . GLN A 27  ? 0.2664 0.2465 0.1411 0.0274  -0.0461 0.0306  405  GLN A NE2 
72   N N   . GLU A 28  ? 0.3480 0.3086 0.2991 0.0175  -0.0831 0.0162  406  GLU A N   
73   C CA  . GLU A 28  ? 0.3489 0.3056 0.3166 0.0134  -0.0883 0.0142  406  GLU A CA  
74   C C   . GLU A 28  ? 0.3317 0.3012 0.2952 0.0071  -0.0784 0.0185  406  GLU A C   
75   O O   . GLU A 28  ? 0.4012 0.3757 0.3444 0.0054  -0.0711 0.0293  406  GLU A O   
76   C CB  . GLU A 28  ? 0.3015 0.2361 0.2661 0.0130  -0.1010 0.0231  406  GLU A CB  
77   C CG  . GLU A 28  ? 0.3507 0.2746 0.3149 0.0199  -0.1113 0.0209  406  GLU A CG  
78   C CD  . GLU A 28  ? 0.4204 0.3239 0.3818 0.0214  -0.1237 0.0299  406  GLU A CD  
79   O OE1 . GLU A 28  ? 0.4197 0.3153 0.3797 0.0163  -0.1236 0.0387  406  GLU A OE1 
80   O OE2 . GLU A 28  ? 0.4939 0.3896 0.4552 0.0276  -0.1336 0.0284  406  GLU A OE2 
81   N N   . PRO A 29  ? 0.3413 0.3173 0.3236 0.0038  -0.0782 0.0098  407  PRO A N   
82   C CA  . PRO A 29  ? 0.2916 0.2618 0.2975 0.0064  -0.0864 -0.0030 407  PRO A CA  
83   C C   . PRO A 29  ? 0.3085 0.2962 0.3264 0.0129  -0.0804 -0.0167 407  PRO A C   
84   O O   . PRO A 29  ? 0.2721 0.2603 0.3097 0.0160  -0.0849 -0.0283 407  PRO A O   
85   C CB  . PRO A 29  ? 0.2986 0.2681 0.3144 -0.0012 -0.0874 -0.0044 407  PRO A CB  
86   C CG  . PRO A 29  ? 0.3051 0.2963 0.3095 -0.0055 -0.0747 -0.0004 407  PRO A CG  
87   C CD  . PRO A 29  ? 0.3479 0.3393 0.3285 -0.0029 -0.0696 0.0121  407  PRO A CD  
88   N N   . PHE A 30  ? 0.3107 0.3125 0.3168 0.0156  -0.0697 -0.0151 408  PHE A N   
89   C CA  . PHE A 30  ? 0.2562 0.2758 0.2738 0.0217  -0.0619 -0.0264 408  PHE A CA  
90   C C   . PHE A 30  ? 0.2907 0.3032 0.3187 0.0274  -0.0683 -0.0317 408  PHE A C   
91   O O   . PHE A 30  ? 0.2805 0.3023 0.3277 0.0324  -0.0678 -0.0426 408  PHE A O   
92   C CB  . PHE A 30  ? 0.2299 0.2667 0.2313 0.0229  -0.0468 -0.0219 408  PHE A CB  
93   C CG  . PHE A 30  ? 0.2151 0.2674 0.2114 0.0189  -0.0390 -0.0199 408  PHE A CG  
94   C CD1 . PHE A 30  ? 0.1887 0.2610 0.1986 0.0215  -0.0330 -0.0306 408  PHE A CD1 
95   C CD2 . PHE A 30  ? 0.2210 0.2697 0.1994 0.0129  -0.0379 -0.0073 408  PHE A CD2 
96   C CE1 . PHE A 30  ? 0.2264 0.3154 0.2324 0.0177  -0.0268 -0.0297 408  PHE A CE1 
97   C CE2 . PHE A 30  ? 0.2060 0.2717 0.1817 0.0086  -0.0311 -0.0054 408  PHE A CE2 
98   C CZ  . PHE A 30  ? 0.1937 0.2798 0.1835 0.0107  -0.0260 -0.0171 408  PHE A CZ  
99   N N   . VAL A 31  ? 0.2713 0.2693 0.2872 0.0271  -0.0744 -0.0243 409  VAL A N   
100  C CA  . VAL A 31  ? 0.2648 0.2574 0.2907 0.0316  -0.0818 -0.0292 409  VAL A CA  
101  C C   . VAL A 31  ? 0.3360 0.3077 0.3538 0.0307  -0.0958 -0.0219 409  VAL A C   
102  O O   . VAL A 31  ? 0.3020 0.2657 0.2979 0.0289  -0.0957 -0.0122 409  VAL A O   
103  C CB  . VAL A 31  ? 0.2948 0.2954 0.3134 0.0335  -0.0727 -0.0296 409  VAL A CB  
104  C CG1 . VAL A 31  ? 0.3072 0.3026 0.3381 0.0364  -0.0818 -0.0349 409  VAL A CG1 
105  C CG2 . VAL A 31  ? 0.2023 0.2240 0.2285 0.0360  -0.0577 -0.0355 409  VAL A CG2 
106  N N   . TYR A 32  ? 0.2823 0.2454 0.3166 0.0332  -0.1074 -0.0262 410  TYR A N   
107  C CA  . TYR A 32  ? 0.2795 0.2242 0.3082 0.0347  -0.1210 -0.0200 410  TYR A CA  
108  C C   . TYR A 32  ? 0.3612 0.3083 0.3964 0.0393  -0.1272 -0.0252 410  TYR A C   
109  O O   . TYR A 32  ? 0.3254 0.2863 0.3782 0.0417  -0.1234 -0.0352 410  TYR A O   
110  C CB  . TYR A 32  ? 0.2874 0.2204 0.3301 0.0361  -0.1305 -0.0215 410  TYR A CB  
111  C CG  . TYR A 32  ? 0.3370 0.2624 0.3729 0.0299  -0.1277 -0.0146 410  TYR A CG  
112  C CD1 . TYR A 32  ? 0.2829 0.2208 0.3259 0.0263  -0.1183 -0.0207 410  TYR A CD1 
113  C CD2 . TYR A 32  ? 0.3161 0.2227 0.3392 0.0278  -0.1345 -0.0020 410  TYR A CD2 
114  C CE1 . TYR A 32  ? 0.2909 0.2232 0.3299 0.0193  -0.1164 -0.0153 410  TYR A CE1 
115  C CE2 . TYR A 32  ? 0.3491 0.2490 0.3684 0.0208  -0.1315 0.0049  410  TYR A CE2 
116  C CZ  . TYR A 32  ? 0.3539 0.2669 0.3819 0.0159  -0.1229 -0.0023 410  TYR A CZ  
117  O OH  . TYR A 32  ? 0.3748 0.2826 0.4011 0.0077  -0.1206 0.0037  410  TYR A OH  
118  N N   . VAL A 33  ? 0.3786 0.3134 0.3997 0.0406  -0.1366 -0.0183 411  VAL A N   
119  C CA  . VAL A 33  ? 0.3683 0.3052 0.3941 0.0441  -0.1444 -0.0232 411  VAL A CA  
120  C C   . VAL A 33  ? 0.3580 0.2807 0.3809 0.0487  -0.1602 -0.0182 411  VAL A C   
121  O O   . VAL A 33  ? 0.3814 0.2915 0.3822 0.0485  -0.1634 -0.0071 411  VAL A O   
122  C CB  . VAL A 33  ? 0.3942 0.3331 0.4006 0.0416  -0.1384 -0.0211 411  VAL A CB  
123  C CG1 . VAL A 33  ? 0.3024 0.2398 0.3110 0.0444  -0.1498 -0.0255 411  VAL A CG1 
124  C CG2 . VAL A 33  ? 0.2727 0.2267 0.2854 0.0390  -0.1227 -0.0269 411  VAL A CG2 
125  N N   . LYS A 34  ? 0.3277 0.2535 0.3722 0.0539  -0.1696 -0.0255 412  LYS A N   
126  C CA  . LYS A 34  ? 0.3356 0.2502 0.3798 0.0602  -0.1847 -0.0215 412  LYS A CA  
127  C C   . LYS A 34  ? 0.4077 0.3334 0.4670 0.0646  -0.1940 -0.0303 412  LYS A C   
128  O O   . LYS A 34  ? 0.3591 0.3008 0.4379 0.0634  -0.1888 -0.0404 412  LYS A O   
129  C CB  . LYS A 34  ? 0.3889 0.2946 0.4463 0.0637  -0.1881 -0.0207 412  LYS A CB  
130  C CG  . LYS A 34  ? 0.4097 0.3041 0.4556 0.0582  -0.1804 -0.0125 412  LYS A CG  
131  C CD  . LYS A 34  ? 0.3631 0.2440 0.3818 0.0565  -0.1824 0.0022  412  LYS A CD  
132  C CE  . LYS A 34  ? 0.4803 0.3510 0.4913 0.0504  -0.1752 0.0111  412  LYS A CE  
133  N NZ  . LYS A 34  ? 0.5345 0.3957 0.5185 0.0485  -0.1745 0.0265  412  LYS A NZ  
134  N N   . PRO A 35  ? 0.4218 0.3411 0.4730 0.0700  -0.2076 -0.0263 413  PRO A N   
135  C CA  . PRO A 35  ? 0.4532 0.3853 0.5209 0.0742  -0.2181 -0.0352 413  PRO A CA  
136  C C   . PRO A 35  ? 0.3911 0.3310 0.4869 0.0793  -0.2200 -0.0419 413  PRO A C   
137  O O   . PRO A 35  ? 0.3530 0.2831 0.4523 0.0829  -0.2199 -0.0384 413  PRO A O   
138  C CB  . PRO A 35  ? 0.3956 0.3176 0.4432 0.0783  -0.2273 -0.0279 413  PRO A CB  
139  C CG  . PRO A 35  ? 0.4710 0.3773 0.4897 0.0761  -0.2232 -0.0156 413  PRO A CG  
140  C CD  . PRO A 35  ? 0.3754 0.2775 0.4009 0.0726  -0.2136 -0.0132 413  PRO A CD  
141  N N   . THR A 36  ? 0.3828 0.3402 0.4981 0.0793  -0.2208 -0.0516 414  THR A N   
142  C CA  . THR A 36  ? 0.3650 0.3318 0.5051 0.0847  -0.2211 -0.0578 414  THR A CA  
143  C C   . THR A 36  ? 0.3778 0.3362 0.5136 0.0925  -0.2316 -0.0533 414  THR A C   
144  O O   . THR A 36  ? 0.4363 0.3846 0.5518 0.0936  -0.2383 -0.0462 414  THR A O   
145  C CB  . THR A 36  ? 0.3972 0.3864 0.5593 0.0819  -0.2177 -0.0679 414  THR A CB  
146  O OG1 . THR A 36  ? 0.4070 0.4004 0.5646 0.0811  -0.2262 -0.0688 414  THR A OG1 
147  C CG2 . THR A 36  ? 0.4119 0.4094 0.5769 0.0745  -0.2068 -0.0713 414  THR A CG2 
148  N N   . LEU A 37  ? 0.3630 0.3263 0.5172 0.0987  -0.2322 -0.0572 415  LEU A N   
149  C CA  . LEU A 37  ? 0.4818 0.4409 0.6348 0.1073  -0.2416 -0.0539 415  LEU A CA  
150  C C   . LEU A 37  ? 0.4769 0.4546 0.6380 0.1077  -0.2474 -0.0591 415  LEU A C   
151  O O   . LEU A 37  ? 0.4897 0.4818 0.6586 0.1007  -0.2438 -0.0653 415  LEU A O   
152  C CB  . LEU A 37  ? 0.3941 0.3511 0.5623 0.1144  -0.2401 -0.0564 415  LEU A CB  
153  C CG  . LEU A 37  ? 0.4654 0.4023 0.6267 0.1142  -0.2359 -0.0521 415  LEU A CG  
154  C CD1 . LEU A 37  ? 0.4455 0.3803 0.6218 0.1218  -0.2349 -0.0565 415  LEU A CD1 
155  C CD2 . LEU A 37  ? 0.4276 0.3418 0.5647 0.1147  -0.2412 -0.0394 415  LEU A CD2 
156  N N   . SER A 38  ? 0.5280 0.5058 0.6877 0.1160  -0.2563 -0.0562 416  SER A N   
157  C CA  . SER A 38  ? 0.5788 0.5753 0.7459 0.1169  -0.2632 -0.0608 416  SER A CA  
158  C C   . SER A 38  ? 0.4996 0.5194 0.6947 0.1140  -0.2582 -0.0708 416  SER A C   
159  O O   . SER A 38  ? 0.4784 0.5146 0.6816 0.1086  -0.2600 -0.0764 416  SER A O   
160  C CB  . SER A 38  ? 0.5918 0.5864 0.7540 0.1280  -0.2729 -0.0555 416  SER A CB  
161  N N   . ASP A 39  ? 0.4826 0.5040 0.6923 0.1173  -0.2516 -0.0731 417  ASP A N   
162  C CA  . ASP A 39  ? 0.4794 0.5231 0.7148 0.1157  -0.2450 -0.0810 417  ASP A CA  
163  C C   . ASP A 39  ? 0.4686 0.5168 0.7097 0.1061  -0.2333 -0.0851 417  ASP A C   
164  O O   . ASP A 39  ? 0.4922 0.5564 0.7531 0.1053  -0.2249 -0.0902 417  ASP A O   
165  C CB  . ASP A 39  ? 0.4693 0.5137 0.7158 0.1253  -0.2428 -0.0815 417  ASP A CB  
166  C CG  . ASP A 39  ? 0.5745 0.5988 0.8123 0.1263  -0.2366 -0.0794 417  ASP A CG  
167  O OD1 . ASP A 39  ? 0.5814 0.5888 0.8015 0.1212  -0.2365 -0.0750 417  ASP A OD1 
168  O OD2 . ASP A 39  ? 0.6257 0.6513 0.8737 0.1321  -0.2320 -0.0822 417  ASP A OD2 
169  N N   . GLY A 40  ? 0.4768 0.5122 0.7003 0.0994  -0.2322 -0.0822 418  GLY A N   
170  C CA  . GLY A 40  ? 0.4032 0.4432 0.6306 0.0910  -0.2212 -0.0854 418  GLY A CA  
171  C C   . GLY A 40  ? 0.4557 0.4909 0.6859 0.0924  -0.2107 -0.0856 418  GLY A C   
172  O O   . GLY A 40  ? 0.3918 0.4365 0.6302 0.0873  -0.1998 -0.0890 418  GLY A O   
173  N N   . THR A 41  ? 0.4162 0.4372 0.6400 0.0994  -0.2136 -0.0823 419  THR A N   
174  C CA  . THR A 41  ? 0.4289 0.4440 0.6544 0.1009  -0.2050 -0.0835 419  THR A CA  
175  C C   . THR A 41  ? 0.4152 0.4075 0.6194 0.0994  -0.2076 -0.0765 419  THR A C   
176  O O   . THR A 41  ? 0.4246 0.4047 0.6116 0.0983  -0.2157 -0.0696 419  THR A O   
177  C CB  . THR A 41  ? 0.4311 0.4479 0.6684 0.1101  -0.2056 -0.0864 419  THR A CB  
178  O OG1 . THR A 41  ? 0.4677 0.4645 0.6927 0.1162  -0.2158 -0.0805 419  THR A OG1 
179  C CG2 . THR A 41  ? 0.5047 0.5437 0.7605 0.1126  -0.2060 -0.0906 419  THR A CG2 
180  N N   . CYS A 42  ? 0.4069 0.3942 0.6122 0.0994  -0.2002 -0.0781 420  CYS A N   
181  C CA  . CYS A 42  ? 0.3895 0.3567 0.5779 0.0974  -0.2014 -0.0716 420  CYS A CA  
182  C C   . CYS A 42  ? 0.4458 0.3956 0.6343 0.1041  -0.2061 -0.0702 420  CYS A C   
183  O O   . CYS A 42  ? 0.4184 0.3745 0.6214 0.1095  -0.2034 -0.0773 420  CYS A O   
184  C CB  . CYS A 42  ? 0.2955 0.2702 0.4850 0.0923  -0.1901 -0.0746 420  CYS A CB  
185  S SG  . CYS A 42  ? 0.3273 0.3221 0.5184 0.0849  -0.1826 -0.0768 420  CYS A SG  
186  N N   . LYS A 43  ? 0.3952 0.3221 0.5665 0.1037  -0.2124 -0.0604 421  LYS A N   
187  C CA  . LYS A 43  ? 0.4980 0.4043 0.6682 0.1094  -0.2170 -0.0575 421  LYS A CA  
188  C C   . LYS A 43  ? 0.4746 0.3778 0.6543 0.1092  -0.2101 -0.0648 421  LYS A C   
189  O O   . LYS A 43  ? 0.4746 0.3799 0.6511 0.1029  -0.2034 -0.0655 421  LYS A O   
190  C CB  . LYS A 43  ? 0.5132 0.3954 0.6620 0.1075  -0.2229 -0.0437 421  LYS A CB  
191  C CG  . LYS A 43  ? 0.5072 0.3654 0.6536 0.1129  -0.2273 -0.0385 421  LYS A CG  
192  C CD  . LYS A 43  ? 0.6399 0.5054 0.8013 0.1224  -0.2300 -0.0460 421  LYS A CD  
193  C CE  . LYS A 43  ? 0.6115 0.4541 0.7746 0.1269  -0.2309 -0.0453 421  LYS A CE  
194  N NZ  . LYS A 43  ? 0.6064 0.4558 0.7820 0.1374  -0.2333 -0.0517 421  LYS A NZ  
195  N N   . GLU A 44  ? 0.5425 0.4419 0.7325 0.1161  -0.2112 -0.0705 422  GLU A N   
196  C CA  . GLU A 44  ? 0.5452 0.4385 0.7422 0.1168  -0.2060 -0.0783 422  GLU A CA  
197  C C   . GLU A 44  ? 0.5334 0.3984 0.7183 0.1118  -0.2081 -0.0710 422  GLU A C   
198  O O   . GLU A 44  ? 0.6207 0.4631 0.7968 0.1134  -0.2147 -0.0620 422  GLU A O   
199  C CB  . GLU A 44  ? 0.5428 0.4355 0.7499 0.1261  -0.2080 -0.0846 422  GLU A CB  
200  C CG  . GLU A 44  ? 0.6995 0.5854 0.9126 0.1278  -0.2037 -0.0940 422  GLU A CG  
201  C CD  . GLU A 44  ? 0.9210 0.8045 1.1412 0.1380  -0.2064 -0.0988 422  GLU A CD  
202  O OE1 . GLU A 44  ? 0.8762 0.7655 1.0979 0.1440  -0.2110 -0.0948 422  GLU A OE1 
203  O OE2 . GLU A 44  ? 0.9468 0.8231 1.1706 0.1406  -0.2040 -0.1068 422  GLU A OE2 
204  N N   . GLU A 45  ? 0.4637 0.3320 0.6459 0.1036  -0.1999 -0.0739 423  GLU A N   
205  C CA  . GLU A 45  ? 0.4850 0.3321 0.6536 0.0934  -0.1973 -0.0672 423  GLU A CA  
206  C C   . GLU A 45  ? 0.4528 0.3038 0.6293 0.0901  -0.1898 -0.0793 423  GLU A C   
207  O O   . GLU A 45  ? 0.4393 0.3118 0.6286 0.0955  -0.1851 -0.0916 423  GLU A O   
208  C CB  . GLU A 45  ? 0.5219 0.3731 0.6716 0.0821  -0.1923 -0.0557 423  GLU A CB  
209  C CG  . GLU A 45  ? 0.5706 0.4107 0.7075 0.0845  -0.2008 -0.0420 423  GLU A CG  
210  C CD  . GLU A 45  ? 0.6370 0.4775 0.7527 0.0742  -0.1957 -0.0302 423  GLU A CD  
211  O OE1 . GLU A 45  ? 0.6291 0.4901 0.7416 0.0696  -0.1881 -0.0334 423  GLU A OE1 
212  O OE2 . GLU A 45  ? 0.7021 0.5222 0.8041 0.0713  -0.1988 -0.0170 423  GLU A OE2 
213  N N   . PHE A 46  ? 0.4594 0.2904 0.6286 0.0814  -0.1888 -0.0758 424  PHE A N   
214  C CA  . PHE A 46  ? 0.4688 0.2998 0.6455 0.0783  -0.1841 -0.0883 424  PHE A CA  
215  C C   . PHE A 46  ? 0.5589 0.3900 0.7239 0.0628  -0.1768 -0.0829 424  PHE A C   
216  O O   . PHE A 46  ? 0.5898 0.4064 0.7418 0.0549  -0.1781 -0.0681 424  PHE A O   
217  C CB  . PHE A 46  ? 0.4299 0.2328 0.6149 0.0847  -0.1922 -0.0933 424  PHE A CB  
218  C CG  . PHE A 46  ? 0.4810 0.2884 0.6769 0.1004  -0.1978 -0.0990 424  PHE A CG  
219  C CD1 . PHE A 46  ? 0.5258 0.3251 0.7169 0.1058  -0.2045 -0.0876 424  PHE A CD1 
220  C CD2 . PHE A 46  ? 0.5437 0.3712 0.7511 0.1075  -0.1937 -0.1139 424  PHE A CD2 
221  C CE1 . PHE A 46  ? 0.5530 0.3635 0.7515 0.1172  -0.2070 -0.0917 424  PHE A CE1 
222  C CE2 . PHE A 46  ? 0.5638 0.4016 0.7779 0.1188  -0.1960 -0.1169 424  PHE A CE2 
223  C CZ  . PHE A 46  ? 0.5512 0.3802 0.7613 0.1233  -0.2027 -0.1061 424  PHE A CZ  
224  N N   . THR A 47  ? 0.5551 0.4044 0.7249 0.0594  -0.1690 -0.0947 425  THR A N   
225  C CA  . THR A 47  ? 0.6571 0.5134 0.8173 0.0456  -0.1613 -0.0910 425  THR A CA  
226  C C   . THR A 47  ? 0.6528 0.4815 0.8124 0.0360  -0.1655 -0.0879 425  THR A C   
227  O O   . THR A 47  ? 0.5263 0.3278 0.6914 0.0403  -0.1741 -0.0876 425  THR A O   
228  C CB  . THR A 47  ? 0.6261 0.5113 0.7921 0.0465  -0.1522 -0.1053 425  THR A CB  
229  O OG1 . THR A 47  ? 0.5141 0.3911 0.6914 0.0485  -0.1554 -0.1200 425  THR A OG1 
230  C CG2 . THR A 47  ? 0.6036 0.5126 0.7757 0.0582  -0.1486 -0.1105 425  THR A CG2 
231  N N   . VAL A 48  ? 0.7356 0.5720 0.8890 0.0229  -0.1590 -0.0852 426  VAL A N   
232  C CA  . VAL A 48  ? 0.7469 0.5604 0.9018 0.0112  -0.1619 -0.0824 426  VAL A CA  
233  C C   . VAL A 48  ? 0.6937 0.4976 0.8637 0.0139  -0.1662 -0.1012 426  VAL A C   
234  O O   . VAL A 48  ? 0.7171 0.4931 0.8918 0.0070  -0.1715 -0.1007 426  VAL A O   
235  C CB  . VAL A 48  ? 0.7613 0.5909 0.9073 -0.0035 -0.1534 -0.0753 426  VAL A CB  
236  C CG1 . VAL A 48  ? 0.8241 0.6594 0.9531 -0.0053 -0.1496 -0.0561 426  VAL A CG1 
237  C CG2 . VAL A 48  ? 0.7071 0.5700 0.8568 -0.0025 -0.1456 -0.0904 426  VAL A CG2 
238  N N   . ASN A 49  ? 0.6257 0.4515 0.8035 0.0242  -0.1639 -0.1179 427  ASN A N   
239  C CA  . ASN A 49  ? 0.5772 0.3969 0.7677 0.0291  -0.1678 -0.1377 427  ASN A CA  
240  C C   . ASN A 49  ? 0.5891 0.3955 0.7879 0.0461  -0.1749 -0.1444 427  ASN A C   
241  O O   . ASN A 49  ? 0.5505 0.3613 0.7576 0.0543  -0.1758 -0.1603 427  ASN A O   
242  C CB  . ASN A 49  ? 0.6304 0.4856 0.8233 0.0305  -0.1599 -0.1524 427  ASN A CB  
243  C CG  . ASN A 49  ? 0.8392 0.7154 1.0222 0.0168  -0.1512 -0.1438 427  ASN A CG  
244  O OD1 . ASN A 49  ? 0.8033 0.6670 0.9841 0.0022  -0.1523 -0.1378 427  ASN A OD1 
245  N ND2 . ASN A 49  ? 0.6931 0.6015 0.8703 0.0218  -0.1420 -0.1426 427  ASN A ND2 
246  N N   . GLY A 50  ? 0.5791 0.3748 0.7739 0.0520  -0.1787 -0.1309 428  GLY A N   
247  C CA  . GLY A 50  ? 0.5548 0.3410 0.7565 0.0679  -0.1850 -0.1342 428  GLY A CA  
248  C C   . GLY A 50  ? 0.4409 0.2577 0.6487 0.0817  -0.1817 -0.1417 428  GLY A C   
249  O O   . GLY A 50  ? 0.4770 0.2944 0.6894 0.0936  -0.1852 -0.1416 428  GLY A O   
250  N N   . ASP A 51  ? 0.3885 0.3230 0.8035 0.0413  -0.1355 -0.0592 429  ASP A N   
251  C CA  . ASP A 51  ? 0.3938 0.3264 0.7831 0.0447  -0.1350 -0.0616 429  ASP A CA  
252  C C   . ASP A 51  ? 0.3917 0.3300 0.7694 0.0465  -0.1323 -0.0524 429  ASP A C   
253  O O   . ASP A 51  ? 0.4166 0.3620 0.8014 0.0460  -0.1328 -0.0466 429  ASP A O   
254  C CB  . ASP A 51  ? 0.4085 0.3423 0.7858 0.0472  -0.1418 -0.0737 429  ASP A CB  
255  C CG  . ASP A 51  ? 0.3288 0.2563 0.7135 0.0462  -0.1455 -0.0838 429  ASP A CG  
256  O OD1 . ASP A 51  ? 0.2963 0.2146 0.6789 0.0452  -0.1404 -0.0831 429  ASP A OD1 
257  O OD2 . ASP A 51  ? 0.3603 0.2919 0.7526 0.0465  -0.1534 -0.0925 429  ASP A OD2 
258  N N   . PRO A 52  ? 0.3637 0.2994 0.7242 0.0485  -0.1291 -0.0510 430  PRO A N   
259  C CA  . PRO A 52  ? 0.3676 0.3089 0.7176 0.0500  -0.1275 -0.0438 430  PRO A CA  
260  C C   . PRO A 52  ? 0.3381 0.2851 0.6755 0.0519  -0.1306 -0.0485 430  PRO A C   
261  O O   . PRO A 52  ? 0.3633 0.3084 0.6908 0.0535  -0.1332 -0.0580 430  PRO A O   
262  C CB  . PRO A 52  ? 0.3418 0.2783 0.6794 0.0516  -0.1234 -0.0437 430  PRO A CB  
263  C CG  . PRO A 52  ? 0.3551 0.2838 0.6881 0.0521  -0.1233 -0.0533 430  PRO A CG  
264  C CD  . PRO A 52  ? 0.3608 0.2881 0.7121 0.0496  -0.1261 -0.0554 430  PRO A CD  
265  N N   . VAL A 53  ? 0.2970 0.2511 0.6341 0.0522  -0.1301 -0.0411 431  VAL A N   
266  C CA  . VAL A 53  ? 0.2786 0.2385 0.6034 0.0544  -0.1313 -0.0442 431  VAL A CA  
267  C C   . VAL A 53  ? 0.3232 0.2810 0.6278 0.0568  -0.1293 -0.0464 431  VAL A C   
268  O O   . VAL A 53  ? 0.2610 0.2200 0.5638 0.0567  -0.1275 -0.0399 431  VAL A O   
269  C CB  . VAL A 53  ? 0.2837 0.2523 0.6163 0.0540  -0.1309 -0.0353 431  VAL A CB  
270  C CG1 . VAL A 53  ? 0.2467 0.2211 0.5656 0.0567  -0.1308 -0.0382 431  VAL A CG1 
271  C CG2 . VAL A 53  ? 0.2797 0.2507 0.6344 0.0516  -0.1319 -0.0335 431  VAL A CG2 
272  N N   . LYS A 54  ? 0.2481 0.2029 0.5386 0.0592  -0.1298 -0.0555 432  LYS A N   
273  C CA  . LYS A 54  ? 0.2359 0.1881 0.5078 0.0617  -0.1269 -0.0580 432  LYS A CA  
274  C C   . LYS A 54  ? 0.2696 0.2281 0.5354 0.0631  -0.1261 -0.0545 432  LYS A C   
275  O O   . LYS A 54  ? 0.2619 0.2252 0.5274 0.0645  -0.1272 -0.0557 432  LYS A O   
276  C CB  . LYS A 54  ? 0.2660 0.2129 0.5234 0.0646  -0.1273 -0.0674 432  LYS A CB  
277  C CG  . LYS A 54  ? 0.2755 0.2160 0.5373 0.0638  -0.1287 -0.0715 432  LYS A CG  
278  C CD  . LYS A 54  ? 0.3235 0.2625 0.5797 0.0665  -0.1335 -0.0800 432  LYS A CD  
279  C CE  . LYS A 54  ? 0.4592 0.3899 0.6952 0.0700  -0.1311 -0.0851 432  LYS A CE  
280  N NZ  . LYS A 54  ? 0.5929 0.5184 0.8307 0.0710  -0.1363 -0.0919 432  LYS A NZ  
281  N N   . LYS A 55  ? 0.2314 0.1905 0.4939 0.0630  -0.1244 -0.0504 433  LYS A N   
282  C CA  . LYS A 55  ? 0.2277 0.1924 0.4850 0.0644  -0.1245 -0.0475 433  LYS A CA  
283  C C   . LYS A 55  ? 0.2361 0.1966 0.4796 0.0664  -0.1217 -0.0522 433  LYS A C   
284  O O   . LYS A 55  ? 0.2516 0.2069 0.4939 0.0658  -0.1197 -0.0539 433  LYS A O   
285  C CB  . LYS A 55  ? 0.2636 0.2354 0.5332 0.0622  -0.1270 -0.0369 433  LYS A CB  
286  C CG  . LYS A 55  ? 0.2835 0.2589 0.5679 0.0602  -0.1285 -0.0310 433  LYS A CG  
287  C CD  . LYS A 55  ? 0.2301 0.2124 0.5236 0.0587  -0.1308 -0.0191 433  LYS A CD  
288  C CE  . LYS A 55  ? 0.2496 0.2346 0.5584 0.0571  -0.1312 -0.0129 433  LYS A CE  
289  N NZ  . LYS A 55  ? 0.3729 0.3641 0.6889 0.0564  -0.1335 0.0001  433  LYS A NZ  
290  N N   . VAL A 56  ? 0.2271 0.1895 0.4611 0.0690  -0.1210 -0.0544 434  VAL A N   
291  C CA  . VAL A 56  ? 0.2728 0.2307 0.4949 0.0710  -0.1179 -0.0591 434  VAL A CA  
292  C C   . VAL A 56  ? 0.3387 0.3032 0.5637 0.0716  -0.1209 -0.0557 434  VAL A C   
293  O O   . VAL A 56  ? 0.3398 0.3117 0.5701 0.0716  -0.1240 -0.0509 434  VAL A O   
294  C CB  . VAL A 56  ? 0.2797 0.2307 0.4834 0.0747  -0.1129 -0.0669 434  VAL A CB  
295  C CG1 . VAL A 56  ? 0.2342 0.1814 0.4358 0.0747  -0.1126 -0.0694 434  VAL A CG1 
296  C CG2 . VAL A 56  ? 0.2814 0.2360 0.4810 0.0778  -0.1127 -0.0674 434  VAL A CG2 
297  N N   . ILE A 57  ? 0.2704 0.2329 0.4931 0.0719  -0.1205 -0.0583 435  ILE A N   
298  C CA  . ILE A 57  ? 0.2870 0.2566 0.5054 0.0691  -0.1220 -0.0563 435  ILE A CA  
299  C C   . ILE A 57  ? 0.3097 0.2736 0.5074 0.0703  -0.1147 -0.0629 435  ILE A C   
300  O O   . ILE A 57  ? 0.3782 0.3305 0.5666 0.0751  -0.1094 -0.0712 435  ILE A O   
301  C CB  . ILE A 57  ? 0.3319 0.3031 0.5533 0.0659  -0.1225 -0.0570 435  ILE A CB  
302  C CG1 . ILE A 57  ? 0.3684 0.3482 0.6113 0.0647  -0.1299 -0.0480 435  ILE A CG1 
303  C CG2 . ILE A 57  ? 0.2481 0.2252 0.4542 0.0591  -0.1204 -0.0577 435  ILE A CG2 
304  C CD1 . ILE A 57  ? 0.3334 0.3262 0.5785 0.0597  -0.1354 -0.0372 435  ILE A CD1 
305  N N   . CYS A 58  ? 0.3304 0.3011 0.5199 0.0664  -0.1136 -0.0588 436  CYS A N   
306  C CA  . CYS A 58  ? 0.2971 0.2626 0.4674 0.0673  -0.1056 -0.0640 436  CYS A CA  
307  C C   . CYS A 58  ? 0.3732 0.3440 0.5299 0.0590  -0.1033 -0.0616 436  CYS A C   
308  O O   . CYS A 58  ? 0.3436 0.3242 0.5050 0.0538  -0.1082 -0.0533 436  CYS A O   
309  C CB  . CYS A 58  ? 0.2797 0.2463 0.4530 0.0718  -0.1046 -0.0626 436  CYS A CB  
310  S SG  . CYS A 58  ? 0.3675 0.3471 0.5547 0.0670  -0.1097 -0.0513 436  CYS A SG  
311  N N   . THR A 59  ? 0.3755 0.3386 0.5142 0.0576  -0.0956 -0.0689 437  THR A N   
312  C CA  . THR A 59  ? 0.3595 0.3257 0.4823 0.0489  -0.0926 -0.0686 437  THR A CA  
313  C C   . THR A 59  ? 0.4057 0.3686 0.5133 0.0491  -0.0846 -0.0686 437  THR A C   
314  O O   . THR A 59  ? 0.3561 0.3124 0.4628 0.0568  -0.0793 -0.0714 437  THR A O   
315  C CB  . THR A 59  ? 0.3078 0.2667 0.4200 0.0459  -0.0874 -0.0774 437  THR A CB  
316  O OG1 . THR A 59  ? 0.3122 0.2564 0.4148 0.0532  -0.0778 -0.0852 437  THR A OG1 
317  C CG2 . THR A 59  ? 0.3282 0.2918 0.4575 0.0449  -0.0946 -0.0769 437  THR A CG2 
318  N N   . GLY A 60  ? 0.4651 0.4326 0.5605 0.0409  -0.0838 -0.0651 438  GLY A N   
319  C CA  . GLY A 60  ? 0.3810 0.3445 0.4611 0.0402  -0.0749 -0.0647 438  GLY A CA  
320  C C   . GLY A 60  ? 0.4377 0.4062 0.5040 0.0302  -0.0757 -0.0599 438  GLY A C   
321  O O   . GLY A 60  ? 0.4613 0.4388 0.5323 0.0245  -0.0853 -0.0551 438  GLY A O   
322  N N   . PRO A 61  ? 0.5099 0.4721 0.5581 0.0283  -0.0653 -0.0610 439  PRO A N   
323  C CA  . PRO A 61  ? 0.5744 0.5388 0.6051 0.0186  -0.0649 -0.0567 439  PRO A CA  
324  C C   . PRO A 61  ? 0.6106 0.5839 0.6523 0.0186  -0.0711 -0.0451 439  PRO A C   
325  O O   . PRO A 61  ? 0.6225 0.5992 0.6843 0.0258  -0.0727 -0.0412 439  PRO A O   
326  C CB  . PRO A 61  ? 0.5234 0.4754 0.5324 0.0182  -0.0494 -0.0620 439  PRO A CB  
327  C CG  . PRO A 61  ? 0.4511 0.3993 0.4737 0.0298  -0.0437 -0.0638 439  PRO A CG  
328  C CD  . PRO A 61  ? 0.4143 0.3660 0.4557 0.0352  -0.0528 -0.0662 439  PRO A CD  
329  N N   . ASN A 62  ? 0.7329 0.7095 0.7602 0.0101  -0.0745 -0.0398 440  ASN A N   
330  C CA  . ASN A 62  ? 0.7406 0.7231 0.7735 0.0094  -0.0786 -0.0281 440  ASN A CA  
331  C C   . ASN A 62  ? 0.8775 0.8521 0.8956 0.0086  -0.0655 -0.0263 440  ASN A C   
332  O O   . ASN A 62  ? 0.9854 0.9522 0.9768 0.0021  -0.0580 -0.0298 440  ASN A O   
333  C CB  . ASN A 62  ? 0.7566 0.7465 0.7808 0.0015  -0.0898 -0.0219 440  ASN A CB  
334  C CG  . ASN A 62  ? 0.8450 0.8453 0.8920 0.0041  -0.1033 -0.0193 440  ASN A CG  
335  O OD1 . ASN A 62  ? 0.8516 0.8576 0.8942 -0.0012 -0.1114 -0.0211 440  ASN A OD1 
336  N ND2 . ASN A 62  ? 0.7789 0.7820 0.8514 0.0119  -0.1056 -0.0155 440  ASN A ND2 
337  N N   . SER A 68  ? 0.5359 0.3980 0.3503 -0.0243 0.0478  -0.0833 446  SER A N   
338  C CA  . SER A 68  ? 0.5846 0.4628 0.4073 -0.0299 0.0268  -0.0794 446  SER A CA  
339  C C   . SER A 68  ? 0.5938 0.4788 0.4332 -0.0277 0.0171  -0.0857 446  SER A C   
340  O O   . SER A 68  ? 0.5755 0.4597 0.4337 -0.0168 0.0209  -0.0876 446  SER A O   
341  C CB  . SER A 68  ? 0.5784 0.4705 0.4243 -0.0238 0.0171  -0.0665 446  SER A CB  
342  O OG  . SER A 68  ? 0.6980 0.5844 0.5262 -0.0282 0.0240  -0.0599 446  SER A OG  
343  N N   . PRO A 69  ? 0.6428 0.5343 0.4749 -0.0379 0.0047  -0.0890 447  PRO A N   
344  C CA  . PRO A 69  ? 0.5607 0.4600 0.4113 -0.0362 -0.0049 -0.0942 447  PRO A CA  
345  C C   . PRO A 69  ? 0.6642 0.5783 0.5488 -0.0254 -0.0171 -0.0855 447  PRO A C   
346  O O   . PRO A 69  ? 0.5902 0.5127 0.4838 -0.0229 -0.0234 -0.0749 447  PRO A O   
347  C CB  . PRO A 69  ? 0.5339 0.4405 0.3712 -0.0502 -0.0169 -0.0974 447  PRO A CB  
348  C CG  . PRO A 69  ? 0.5491 0.4445 0.3520 -0.0602 -0.0084 -0.0986 447  PRO A CG  
349  C CD  . PRO A 69  ? 0.6246 0.5156 0.4294 -0.0519 0.0001  -0.0892 447  PRO A CD  
350  N N   . ARG A 70  ? 0.7170 0.6327 0.6195 -0.0194 -0.0195 -0.0904 448  ARG A N   
351  C CA  . ARG A 70  ? 0.6946 0.6214 0.6281 -0.0090 -0.0295 -0.0841 448  ARG A CA  
352  C C   . ARG A 70  ? 0.7491 0.6865 0.6962 -0.0125 -0.0432 -0.0861 448  ARG A C   
353  O O   . ARG A 70  ? 0.7340 0.6664 0.6861 -0.0102 -0.0402 -0.0941 448  ARG A O   
354  C CB  . ARG A 70  ? 0.6207 0.5383 0.5635 0.0034  -0.0190 -0.0875 448  ARG A CB  
355  C CG  . ARG A 70  ? 0.6531 0.5626 0.5877 0.0083  -0.0057 -0.0848 448  ARG A CG  
356  C CD  . ARG A 70  ? 0.5840 0.4831 0.5231 0.0199  0.0055  -0.0897 448  ARG A CD  
357  N NE  . ARG A 70  ? 0.6414 0.5329 0.5727 0.0244  0.0196  -0.0877 448  ARG A NE  
358  C CZ  . ARG A 70  ? 0.6372 0.5175 0.5662 0.0337  0.0325  -0.0916 448  ARG A CZ  
359  N NH1 . ARG A 70  ? 0.6051 0.4788 0.5364 0.0398  0.0337  -0.0978 448  ARG A NH1 
360  N NH2 . ARG A 70  ? 0.6042 0.4793 0.5284 0.0376  0.0452  -0.0887 448  ARG A NH2 
361  N N   . HIS A 71  ? 0.8004 0.7521 0.7540 -0.0175 -0.0576 -0.0782 449  HIS A N   
362  C CA  . HIS A 71  ? 0.6768 0.6411 0.6480 -0.0195 -0.0715 -0.0780 449  HIS A CA  
363  C C   . HIS A 71  ? 0.6202 0.5904 0.6210 -0.0081 -0.0775 -0.0722 449  HIS A C   
364  O O   . HIS A 71  ? 0.6619 0.6383 0.6731 -0.0039 -0.0825 -0.0622 449  HIS A O   
365  C CB  . HIS A 71  ? 0.6023 0.5795 0.5676 -0.0288 -0.0848 -0.0712 449  HIS A CB  
366  N N   . THR A 72  ? 0.5364 0.5035 0.5500 -0.0034 -0.0761 -0.0789 450  THR A N   
367  C CA  . THR A 72  ? 0.5167 0.4862 0.5552 0.0074  -0.0801 -0.0754 450  THR A CA  
368  C C   . THR A 72  ? 0.4531 0.4377 0.5127 0.0063  -0.0951 -0.0680 450  THR A C   
369  O O   . THR A 72  ? 0.5533 0.5449 0.6148 -0.0004 -0.1012 -0.0705 450  THR A O   
370  C CB  . THR A 72  ? 0.4362 0.3940 0.4767 0.0132  -0.0717 -0.0852 450  THR A CB  
371  O OG1 . THR A 72  ? 0.5404 0.4855 0.5701 0.0200  -0.0595 -0.0880 450  THR A OG1 
372  C CG2 . THR A 72  ? 0.4749 0.4368 0.5406 0.0208  -0.0791 -0.0831 450  THR A CG2 
373  N N   . VAL A 73  ? 0.4356 0.4254 0.5123 0.0129  -0.1008 -0.0591 451  VAL A N   
374  C CA  . VAL A 73  ? 0.4233 0.4259 0.5212 0.0135  -0.1138 -0.0507 451  VAL A CA  
375  C C   . VAL A 73  ? 0.4326 0.4326 0.5526 0.0236  -0.1145 -0.0491 451  VAL A C   
376  O O   . VAL A 73  ? 0.3757 0.3693 0.4950 0.0292  -0.1086 -0.0490 451  VAL A O   
377  C CB  . VAL A 73  ? 0.4999 0.5113 0.5930 0.0091  -0.1206 -0.0393 451  VAL A CB  
378  C CG1 . VAL A 73  ? 0.5369 0.5414 0.6212 0.0121  -0.1125 -0.0361 451  VAL A CG1 
379  C CG2 . VAL A 73  ? 0.4911 0.5136 0.6078 0.0122  -0.1325 -0.0291 451  VAL A CG2 
380  N N   . PRO A 74  ? 0.4010 0.4056 0.5409 0.0261  -0.1211 -0.0483 452  PRO A N   
381  C CA  . PRO A 74  ? 0.3796 0.3806 0.5389 0.0351  -0.1219 -0.0469 452  PRO A CA  
382  C C   . PRO A 74  ? 0.3291 0.3352 0.4978 0.0372  -0.1263 -0.0363 452  PRO A C   
383  O O   . PRO A 74  ? 0.3537 0.3692 0.5246 0.0331  -0.1331 -0.0270 452  PRO A O   
384  C CB  . PRO A 74  ? 0.3526 0.3580 0.5299 0.0356  -0.1278 -0.0471 452  PRO A CB  
385  C CG  . PRO A 74  ? 0.3393 0.3564 0.5118 0.0269  -0.1339 -0.0445 452  PRO A CG  
386  C CD  . PRO A 74  ? 0.3482 0.3608 0.4941 0.0209  -0.1272 -0.0499 452  PRO A CD  
387  N N   . GLN A 75  ? 0.3360 0.3354 0.5100 0.0436  -0.1222 -0.0378 453  GLN A N   
388  C CA  . GLN A 75  ? 0.2863 0.2894 0.4715 0.0455  -0.1248 -0.0293 453  GLN A CA  
389  C C   . GLN A 75  ? 0.3114 0.3101 0.5157 0.0526  -0.1262 -0.0312 453  GLN A C   
390  O O   . GLN A 75  ? 0.3095 0.3022 0.5171 0.0562  -0.1256 -0.0383 453  GLN A O   
391  C CB  . GLN A 75  ? 0.3357 0.3367 0.5071 0.0444  -0.1177 -0.0290 453  GLN A CB  
392  C CG  . GLN A 75  ? 0.3412 0.3438 0.4901 0.0369  -0.1150 -0.0279 453  GLN A CG  
393  C CD  . GLN A 75  ? 0.4371 0.4351 0.5714 0.0364  -0.1054 -0.0290 453  GLN A CD  
394  O OE1 . GLN A 75  ? 0.4137 0.4134 0.5562 0.0383  -0.1037 -0.0235 453  GLN A OE1 
395  N NE2 . GLN A 75  ? 0.4311 0.4228 0.5446 0.0338  -0.0979 -0.0364 453  GLN A NE2 
396  N N   . CYS A 76  ? 0.3288 0.3295 0.5451 0.0543  -0.1274 -0.0255 454  CYS A N   
397  C CA  . CYS A 76  ? 0.2563 0.2533 0.4913 0.0597  -0.1296 -0.0270 454  CYS A CA  
398  C C   . CYS A 76  ? 0.2489 0.2433 0.4843 0.0631  -0.1256 -0.0312 454  CYS A C   
399  O O   . CYS A 76  ? 0.2660 0.2649 0.4999 0.0607  -0.1228 -0.0265 454  CYS A O   
400  C CB  . CYS A 76  ? 0.2964 0.2982 0.5492 0.0584  -0.1351 -0.0167 454  CYS A CB  
401  S SG  . CYS A 76  ? 0.3471 0.3532 0.6060 0.0568  -0.1412 -0.0115 454  CYS A SG  
402  N N   . CYS A 77  ? 0.2368 0.2241 0.4747 0.0689  -0.1251 -0.0398 455  CYS A N   
403  C CA  . CYS A 77  ? 0.2432 0.2291 0.4822 0.0731  -0.1228 -0.0447 455  CYS A CA  
404  C C   . CYS A 77  ? 0.2441 0.2269 0.4914 0.0720  -0.1236 -0.0464 455  CYS A C   
405  O O   . CYS A 77  ? 0.2605 0.2371 0.5053 0.0704  -0.1237 -0.0485 455  CYS A O   
406  C CB  . CYS A 77  ? 0.2291 0.2078 0.4505 0.0778  -0.1178 -0.0537 455  CYS A CB  
407  S SG  . CYS A 77  ? 0.4050 0.3855 0.6052 0.0744  -0.1093 -0.0529 455  CYS A SG  
408  N N   . TYR A 78  ? 0.2250 0.2123 0.4817 0.0719  -0.1235 -0.0459 456  TYR A N   
409  C CA  . TYR A 78  ? 0.2257 0.2104 0.4896 0.0701  -0.1247 -0.0491 456  TYR A CA  
410  C C   . TYR A 78  ? 0.2512 0.2429 0.5243 0.0714  -0.1246 -0.0504 456  TYR A C   
411  O O   . TYR A 78  ? 0.2248 0.2237 0.5020 0.0730  -0.1227 -0.0469 456  TYR A O   
412  C CB  . TYR A 78  ? 0.2258 0.2099 0.5038 0.0656  -0.1270 -0.0430 456  TYR A CB  
413  C CG  . TYR A 78  ? 0.2461 0.2382 0.5393 0.0635  -0.1278 -0.0331 456  TYR A CG  
414  C CD1 . TYR A 78  ? 0.2288 0.2244 0.5199 0.0632  -0.1289 -0.0253 456  TYR A CD1 
415  C CD2 . TYR A 78  ? 0.2261 0.2225 0.5366 0.0619  -0.1280 -0.0315 456  TYR A CD2 
416  C CE1 . TYR A 78  ? 0.2279 0.2303 0.5315 0.0616  -0.1301 -0.0151 456  TYR A CE1 
417  C CE2 . TYR A 78  ? 0.2270 0.2299 0.5522 0.0602  -0.1277 -0.0217 456  TYR A CE2 
418  C CZ  . TYR A 78  ? 0.2297 0.2348 0.5491 0.0600  -0.1283 -0.0131 456  TYR A CZ  
419  O OH  . TYR A 78  ? 0.3164 0.3249 0.6388 0.0555  -0.1247 -0.0027 456  TYR A OH  
420  N N   . GLY A 79  ? 0.2276 0.2174 0.5052 0.0710  -0.1269 -0.0560 457  GLY A N   
421  C CA  . GLY A 79  ? 0.2281 0.2259 0.5185 0.0717  -0.1279 -0.0578 457  GLY A CA  
422  C C   . GLY A 79  ? 0.2322 0.2270 0.5151 0.0748  -0.1309 -0.0668 457  GLY A C   
423  O O   . GLY A 79  ? 0.2351 0.2204 0.5050 0.0756  -0.1324 -0.0714 457  GLY A O   
424  N N   . PHE A 80  ? 0.2800 0.2764 0.3279 0.0129  -0.1026 -0.0033 458  PHE A N   
425  C CA  . PHE A 80  ? 0.2554 0.2465 0.2917 0.0094  -0.0927 -0.0042 458  PHE A CA  
426  C C   . PHE A 80  ? 0.2097 0.2099 0.2547 0.0088  -0.0812 -0.0108 458  PHE A C   
427  O O   . PHE A 80  ? 0.2284 0.2266 0.2762 0.0099  -0.0726 -0.0162 458  PHE A O   
428  C CB  . PHE A 80  ? 0.2745 0.2643 0.2920 0.0035  -0.0947 0.0057  458  PHE A CB  
429  C CG  . PHE A 80  ? 0.2656 0.2478 0.2696 -0.0012 -0.0877 0.0076  458  PHE A CG  
430  C CD1 . PHE A 80  ? 0.2610 0.2482 0.2651 -0.0036 -0.0764 0.0038  458  PHE A CD1 
431  C CD2 . PHE A 80  ? 0.2825 0.2525 0.2739 -0.0042 -0.0936 0.0144  458  PHE A CD2 
432  C CE1 . PHE A 80  ? 0.3152 0.2957 0.3066 -0.0087 -0.0707 0.0064  458  PHE A CE1 
433  C CE2 . PHE A 80  ? 0.2322 0.1945 0.2105 -0.0095 -0.0885 0.0168  458  PHE A CE2 
434  C CZ  . PHE A 80  ? 0.2505 0.2185 0.2286 -0.0116 -0.0768 0.0127  458  PHE A CZ  
435  N N   . CYS A 81  ? 0.1884 0.1985 0.2371 0.0072  -0.0814 -0.0103 459  CYS A N   
436  C CA  . CYS A 81  ? 0.2416 0.2596 0.2984 0.0051  -0.0722 -0.0147 459  CYS A CA  
437  C C   . CYS A 81  ? 0.2075 0.2332 0.2866 0.0091  -0.0695 -0.0211 459  CYS A C   
438  O O   . CYS A 81  ? 0.2043 0.2361 0.2908 0.0076  -0.0600 -0.0242 459  CYS A O   
439  C CB  . CYS A 81  ? 0.1719 0.1953 0.2257 0.0027  -0.0752 -0.0129 459  CYS A CB  
440  S SG  . CYS A 81  ? 0.2608 0.2797 0.2911 -0.0013 -0.0734 -0.0054 459  CYS A SG  
441  N N   . ILE A 82  ? 0.1811 0.2084 0.2721 0.0139  -0.0779 -0.0220 460  ILE A N   
442  C CA  . ILE A 82  ? 0.1677 0.2041 0.2823 0.0186  -0.0752 -0.0268 460  ILE A CA  
443  C C   . ILE A 82  ? 0.2356 0.2677 0.3503 0.0230  -0.0664 -0.0310 460  ILE A C   
444  O O   . ILE A 82  ? 0.2301 0.2724 0.3585 0.0251  -0.0569 -0.0349 460  ILE A O   
445  C CB  . ILE A 82  ? 0.2255 0.2644 0.3533 0.0226  -0.0873 -0.0257 460  ILE A CB  
446  C CG1 . ILE A 82  ? 0.1983 0.2416 0.3244 0.0184  -0.0957 -0.0229 460  ILE A CG1 
447  C CG2 . ILE A 82  ? 0.2430 0.2922 0.3971 0.0285  -0.0844 -0.0296 460  ILE A CG2 
448  C CD1 . ILE A 82  ? 0.1728 0.2252 0.3080 0.0143  -0.0907 -0.0249 460  ILE A CD1 
449  N N   . ASP A 83  ? 0.2231 0.2403 0.3219 0.0245  -0.0698 -0.0301 461  ASP A N   
450  C CA  . ASP A 83  ? 0.2266 0.2357 0.3198 0.0286  -0.0622 -0.0352 461  ASP A CA  
451  C C   . ASP A 83  ? 0.2694 0.2816 0.3530 0.0234  -0.0496 -0.0362 461  ASP A C   
452  O O   . ASP A 83  ? 0.2768 0.2925 0.3643 0.0272  -0.0393 -0.0418 461  ASP A O   
453  C CB  . ASP A 83  ? 0.2571 0.2466 0.3325 0.0290  -0.0708 -0.0327 461  ASP A CB  
454  C CG  . ASP A 83  ? 0.2427 0.2266 0.3300 0.0369  -0.0805 -0.0343 461  ASP A CG  
455  O OD1 . ASP A 83  ? 0.2871 0.2835 0.3970 0.0422  -0.0804 -0.0370 461  ASP A OD1 
456  O OD2 . ASP A 83  ? 0.3047 0.2716 0.3800 0.0374  -0.0892 -0.0320 461  ASP A OD2 
457  N N   . LEU A 84  ? 0.2399 0.2518 0.3111 0.0152  -0.0501 -0.0306 462  LEU A N   
458  C CA  . LEU A 84  ? 0.2594 0.2747 0.3229 0.0094  -0.0393 -0.0302 462  LEU A CA  
459  C C   . LEU A 84  ? 0.2410 0.2742 0.3247 0.0091  -0.0317 -0.0324 462  LEU A C   
460  O O   . LEU A 84  ? 0.2523 0.2913 0.3360 0.0074  -0.0208 -0.0341 462  LEU A O   
461  C CB  . LEU A 84  ? 0.2127 0.2238 0.2605 0.0017  -0.0425 -0.0229 462  LEU A CB  
462  C CG  . LEU A 84  ? 0.2333 0.2460 0.2719 -0.0052 -0.0332 -0.0208 462  LEU A CG  
463  C CD1 . LEU A 84  ? 0.1820 0.1851 0.2070 -0.0054 -0.0273 -0.0231 462  LEU A CD1 
464  C CD2 . LEU A 84  ? 0.2094 0.2191 0.2355 -0.0111 -0.0370 -0.0132 462  LEU A CD2 
465  N N   . LEU A 85  ? 0.2261 0.2685 0.3268 0.0100  -0.0381 -0.0316 463  LEU A N   
466  C CA  . LEU A 85  ? 0.2194 0.2791 0.3420 0.0089  -0.0331 -0.0322 463  LEU A CA  
467  C C   . LEU A 85  ? 0.2142 0.2837 0.3520 0.0160  -0.0248 -0.0366 463  LEU A C   
468  O O   . LEU A 85  ? 0.1741 0.2572 0.3216 0.0142  -0.0146 -0.0364 463  LEU A O   
469  C CB  . LEU A 85  ? 0.1544 0.2195 0.2910 0.0084  -0.0441 -0.0304 463  LEU A CB  
470  C CG  . LEU A 85  ? 0.2379 0.3209 0.4017 0.0080  -0.0425 -0.0301 463  LEU A CG  
471  C CD1 . LEU A 85  ? 0.2286 0.3188 0.3944 0.0000  -0.0360 -0.0273 463  LEU A CD1 
472  C CD2 . LEU A 85  ? 0.2689 0.3538 0.4446 0.0083  -0.0559 -0.0289 463  LEU A CD2 
473  N N   . ILE A 86  ? 0.2378 0.3012 0.3784 0.0245  -0.0290 -0.0402 464  ILE A N   
474  C CA  . ILE A 86  ? 0.2343 0.3066 0.3895 0.0338  -0.0210 -0.0452 464  ILE A CA  
475  C C   . ILE A 86  ? 0.2807 0.3492 0.4196 0.0346  -0.0082 -0.0491 464  ILE A C   
476  O O   . ILE A 86  ? 0.2863 0.3702 0.4367 0.0386  0.0037  -0.0514 464  ILE A O   
477  C CB  . ILE A 86  ? 0.3093 0.3722 0.4693 0.0432  -0.0299 -0.0483 464  ILE A CB  
478  C CG1 . ILE A 86  ? 0.2572 0.3271 0.4354 0.0421  -0.0421 -0.0439 464  ILE A CG1 
479  C CG2 . ILE A 86  ? 0.3743 0.4437 0.5466 0.0549  -0.0207 -0.0548 464  ILE A CG2 
480  C CD1 . ILE A 86  ? 0.2202 0.2805 0.4029 0.0497  -0.0530 -0.0450 464  ILE A CD1 
481  N N   . LYS A 87  ? 0.2655 0.3148 0.3773 0.0305  -0.0104 -0.0490 465  LYS A N   
482  C CA  . LYS A 87  ? 0.2910 0.3345 0.3840 0.0297  0.0001  -0.0522 465  LYS A CA  
483  C C   . LYS A 87  ? 0.3294 0.3899 0.4269 0.0220  0.0106  -0.0483 465  LYS A C   
484  O O   . LYS A 87  ? 0.3369 0.4073 0.4350 0.0247  0.0230  -0.0513 465  LYS A O   
485  C CB  . LYS A 87  ? 0.3190 0.3391 0.3836 0.0247  -0.0068 -0.0504 465  LYS A CB  
486  C CG  . LYS A 87  ? 0.3644 0.3732 0.4066 0.0250  0.0010  -0.0549 465  LYS A CG  
487  C CD  . LYS A 87  ? 0.4578 0.4579 0.4995 0.0378  0.0024  -0.0647 465  LYS A CD  
488  C CE  . LYS A 87  ? 0.4621 0.4468 0.4769 0.0383  0.0084  -0.0703 465  LYS A CE  
489  N NZ  . LYS A 87  ? 0.4486 0.4207 0.4603 0.0522  0.0085  -0.0814 465  LYS A NZ  
490  N N   . LEU A 88  ? 0.3011 0.3654 0.4018 0.0127  0.0056  -0.0414 466  LEU A N   
491  C CA  . LEU A 88  ? 0.2666 0.3453 0.3728 0.0044  0.0133  -0.0366 466  LEU A CA  
492  C C   . LEU A 88  ? 0.3001 0.4030 0.4337 0.0078  0.0206  -0.0364 466  LEU A C   
493  O O   . LEU A 88  ? 0.3012 0.4182 0.4383 0.0041  0.0313  -0.0339 466  LEU A O   
494  C CB  . LEU A 88  ? 0.2711 0.3470 0.3769 -0.0043 0.0046  -0.0303 466  LEU A CB  
495  C CG  . LEU A 88  ? 0.3041 0.3614 0.3845 -0.0091 -0.0003 -0.0275 466  LEU A CG  
496  C CD1 . LEU A 88  ? 0.1915 0.2470 0.2739 -0.0138 -0.0094 -0.0229 466  LEU A CD1 
497  C CD2 . LEU A 88  ? 0.2694 0.3249 0.3342 -0.0154 0.0088  -0.0252 466  LEU A CD2 
498  N N   . ALA A 89  ? 0.2703 0.3797 0.4244 0.0144  0.0146  -0.0379 467  ALA A N   
499  C CA  . ALA A 89  ? 0.3071 0.4415 0.4904 0.0176  0.0206  -0.0360 467  ALA A CA  
500  C C   . ALA A 89  ? 0.3699 0.5134 0.5532 0.0272  0.0347  -0.0413 467  ALA A C   
501  O O   . ALA A 89  ? 0.3679 0.5333 0.5636 0.0260  0.0461  -0.0379 467  ALA A O   
502  C CB  . ALA A 89  ? 0.2638 0.4019 0.4687 0.0221  0.0093  -0.0355 467  ALA A CB  
503  N N   . ARG A 90  ? 0.3550 0.4818 0.5241 0.0371  0.0339  -0.0494 468  ARG A N   
504  C CA  . ARG A 90  ? 0.3843 0.5158 0.5492 0.0481  0.0470  -0.0565 468  ARG A CA  
505  C C   . ARG A 90  ? 0.3832 0.5130 0.5246 0.0423  0.0580  -0.0569 468  ARG A C   
506  O O   . ARG A 90  ? 0.4489 0.5949 0.5927 0.0477  0.0723  -0.0591 468  ARG A O   
507  C CB  . ARG A 90  ? 0.4401 0.5490 0.5928 0.0595  0.0410  -0.0656 468  ARG A CB  
508  C CG  . ARG A 90  ? 0.6346 0.7540 0.8142 0.0725  0.0393  -0.0684 468  ARG A CG  
509  C CD  . ARG A 90  ? 0.7274 0.8206 0.8976 0.0785  0.0257  -0.0733 468  ARG A CD  
510  N NE  . ARG A 90  ? 0.8031 0.9030 0.9991 0.0803  0.0141  -0.0690 468  ARG A NE  
511  C CZ  . ARG A 90  ? 0.7593 0.8426 0.9555 0.0867  0.0021  -0.0717 468  ARG A CZ  
512  N NH1 . ARG A 90  ? 0.8246 0.8825 0.9977 0.0921  -0.0008 -0.0786 468  ARG A NH1 
513  N NH2 . ARG A 90  ? 0.6608 0.7523 0.8806 0.0870  -0.0085 -0.0665 468  ARG A NH2 
514  N N   . THR A 91  ? 0.3951 0.5067 0.5137 0.0315  0.0518  -0.0540 469  THR A N   
515  C CA  . THR A 91  ? 0.4250 0.5328 0.5198 0.0251  0.0605  -0.0535 469  THR A CA  
516  C C   . THR A 91  ? 0.4472 0.5811 0.5567 0.0165  0.0696  -0.0450 469  THR A C   
517  O O   . THR A 91  ? 0.4878 0.6329 0.5899 0.0169  0.0826  -0.0456 469  THR A O   
518  C CB  . THR A 91  ? 0.4063 0.4891 0.4760 0.0159  0.0503  -0.0510 469  THR A CB  
519  O OG1 . THR A 91  ? 0.4467 0.5052 0.4992 0.0232  0.0432  -0.0582 469  THR A OG1 
520  C CG2 . THR A 91  ? 0.3847 0.4666 0.4340 0.0063  0.0578  -0.0474 469  THR A CG2 
521  N N   . MET A 92  ? 0.3705 0.5137 0.5000 0.0084  0.0622  -0.0368 470  MET A N   
522  C CA  . MET A 92  ? 0.3662 0.5307 0.5100 -0.0019 0.0673  -0.0271 470  MET A CA  
523  C C   . MET A 92  ? 0.3260 0.5193 0.5046 0.0015  0.0710  -0.0228 470  MET A C   
524  O O   . MET A 92  ? 0.3812 0.5941 0.5756 -0.0076 0.0741  -0.0133 470  MET A O   
525  C CB  . MET A 92  ? 0.3131 0.4666 0.4542 -0.0140 0.0557  -0.0204 470  MET A CB  
526  C CG  . MET A 92  ? 0.4260 0.5539 0.5356 -0.0178 0.0519  -0.0224 470  MET A CG  
527  S SD  . MET A 92  ? 0.4721 0.5873 0.5794 -0.0283 0.0385  -0.0156 470  MET A SD  
528  C CE  . MET A 92  ? 0.3610 0.4993 0.4928 -0.0383 0.0415  -0.0059 470  MET A CE  
529  N N   . ASN A 93  ? 0.3694 0.5661 0.5618 0.0137  0.0699  -0.0284 471  ASN A N   
530  C CA  . ASN A 93  ? 0.3780 0.6042 0.6044 0.0189  0.0748  -0.0241 471  ASN A CA  
531  C C   . ASN A 93  ? 0.2948 0.5324 0.5467 0.0077  0.0642  -0.0134 471  ASN A C   
532  O O   . ASN A 93  ? 0.3875 0.6481 0.6569 -0.0001 0.0690  -0.0036 471  ASN A O   
533  C CB  . ASN A 93  ? 0.3132 0.5641 0.5418 0.0221  0.0933  -0.0223 471  ASN A CB  
534  C CG  . ASN A 93  ? 0.3189 0.6015 0.5817 0.0312  0.1006  -0.0189 471  ASN A CG  
535  O OD1 . ASN A 93  ? 0.4426 0.7239 0.7218 0.0399  0.0937  -0.0219 471  ASN A OD1 
536  N ND2 . ASN A 93  ? 0.2810 0.5939 0.5555 0.0292  0.1145  -0.0112 471  ASN A ND2 
537  N N   . PHE A 94  ? 0.3001 0.5204 0.5530 0.0069  0.0487  -0.0152 472  PHE A N   
538  C CA  . PHE A 94  ? 0.2153 0.4424 0.4907 -0.0018 0.0364  -0.0072 472  PHE A CA  
539  C C   . PHE A 94  ? 0.2848 0.5055 0.5720 0.0051  0.0243  -0.0106 472  PHE A C   
540  O O   . PHE A 94  ? 0.2618 0.4645 0.5330 0.0134  0.0217  -0.0189 472  PHE A O   
541  C CB  . PHE A 94  ? 0.2723 0.4820 0.5316 -0.0145 0.0275  -0.0042 472  PHE A CB  
542  C CG  . PHE A 94  ? 0.3232 0.5032 0.5553 -0.0125 0.0189  -0.0114 472  PHE A CG  
543  C CD1 . PHE A 94  ? 0.3303 0.4990 0.5659 -0.0110 0.0046  -0.0133 472  PHE A CD1 
544  C CD2 . PHE A 94  ? 0.3461 0.5106 0.5491 -0.0130 0.0248  -0.0150 472  PHE A CD2 
545  C CE1 . PHE A 94  ? 0.2895 0.4342 0.5008 -0.0094 -0.0027 -0.0183 472  PHE A CE1 
546  C CE2 . PHE A 94  ? 0.3456 0.4855 0.5257 -0.0120 0.0167  -0.0194 472  PHE A CE2 
547  C CZ  . PHE A 94  ? 0.2528 0.3838 0.4374 -0.0099 0.0034  -0.0208 472  PHE A CZ  
548  N N   . THR A 95  ? 0.2197 0.4553 0.5354 0.0006  0.0158  -0.0033 473  THR A N   
549  C CA  . THR A 95  ? 0.2245 0.4552 0.5533 0.0044  0.0020  -0.0044 473  THR A CA  
550  C C   . THR A 95  ? 0.2778 0.4875 0.5940 -0.0048 -0.0143 -0.0043 473  THR A C   
551  O O   . THR A 95  ? 0.2983 0.5030 0.6057 -0.0148 -0.0156 -0.0010 473  THR A O   
552  C CB  . THR A 95  ? 0.2203 0.4801 0.5882 0.0049  0.0011  0.0042  473  THR A CB  
553  O OG1 . THR A 95  ? 0.2749 0.5479 0.6566 -0.0082 -0.0009 0.0145  473  THR A OG1 
554  C CG2 . THR A 95  ? 0.1495 0.4311 0.5299 0.0171  0.0181  0.0031  473  THR A CG2 
555  N N   . TYR A 96  ? 0.2845 0.4820 0.5994 -0.0008 -0.0268 -0.0078 474  TYR A N   
556  C CA  . TYR A 96  ? 0.2760 0.4518 0.5731 -0.0069 -0.0409 -0.0095 474  TYR A CA  
557  C C   . TYR A 96  ? 0.2503 0.4240 0.5596 -0.0051 -0.0563 -0.0092 474  TYR A C   
558  O O   . TYR A 96  ? 0.2616 0.4444 0.5866 0.0030  -0.0561 -0.0095 474  TYR A O   
559  C CB  . TYR A 96  ? 0.1894 0.3427 0.4524 -0.0039 -0.0383 -0.0162 474  TYR A CB  
560  C CG  . TYR A 96  ? 0.2377 0.3853 0.4950 0.0072  -0.0364 -0.0216 474  TYR A CG  
561  C CD1 . TYR A 96  ? 0.2429 0.3965 0.4991 0.0144  -0.0226 -0.0247 474  TYR A CD1 
562  C CD2 . TYR A 96  ? 0.2380 0.3737 0.4905 0.0105  -0.0491 -0.0237 474  TYR A CD2 
563  C CE1 . TYR A 96  ? 0.1805 0.3259 0.4314 0.0249  -0.0223 -0.0301 474  TYR A CE1 
564  C CE2 . TYR A 96  ? 0.1820 0.3115 0.4307 0.0200  -0.0489 -0.0277 474  TYR A CE2 
565  C CZ  . TYR A 96  ? 0.2054 0.3387 0.4537 0.0273  -0.0359 -0.0312 474  TYR A CZ  
566  O OH  . TYR A 96  ? 0.3142 0.4383 0.5584 0.0372  -0.0371 -0.0357 474  TYR A OH  
567  N N   . GLU A 97  ? 0.2680 0.4289 0.5691 -0.0123 -0.0701 -0.0088 475  GLU A N   
568  C CA  . GLU A 97  ? 0.2651 0.4185 0.5684 -0.0116 -0.0864 -0.0096 475  GLU A CA  
569  C C   . GLU A 97  ? 0.2041 0.3335 0.4748 -0.0129 -0.0935 -0.0149 475  GLU A C   
570  O O   . GLU A 97  ? 0.2288 0.3497 0.4857 -0.0187 -0.0926 -0.0154 475  GLU A O   
571  C CB  . GLU A 97  ? 0.1531 0.3126 0.4725 -0.0190 -0.0955 -0.0030 475  GLU A CB  
572  N N   . VAL A 98  ? 0.2301 0.3500 0.4895 -0.0072 -0.1003 -0.0180 476  VAL A N   
573  C CA  . VAL A 98  ? 0.2143 0.3149 0.4424 -0.0066 -0.1051 -0.0220 476  VAL A CA  
574  C C   . VAL A 98  ? 0.2456 0.3374 0.4672 -0.0091 -0.1205 -0.0221 476  VAL A C   
575  O O   . VAL A 98  ? 0.2290 0.3246 0.4616 -0.0080 -0.1261 -0.0194 476  VAL A O   
576  C CB  . VAL A 98  ? 0.1778 0.2725 0.3926 0.0010  -0.1006 -0.0239 476  VAL A CB  
577  C CG1 . VAL A 98  ? 0.2118 0.2902 0.3949 0.0007  -0.1025 -0.0258 476  VAL A CG1 
578  C CG2 . VAL A 98  ? 0.2352 0.3374 0.4563 0.0047  -0.0852 -0.0244 476  VAL A CG2 
579  N N   . HIS A 99  ? 0.2308 0.3083 0.4286 -0.0118 -0.1243 -0.0249 477  HIS A N   
580  C CA  . HIS A 99  ? 0.2188 0.2833 0.3991 -0.0124 -0.1348 -0.0261 477  HIS A CA  
581  C C   . HIS A 99  ? 0.2091 0.2603 0.3588 -0.0099 -0.1350 -0.0300 477  HIS A C   
582  O O   . HIS A 99  ? 0.2387 0.2885 0.3820 -0.0104 -0.1287 -0.0315 477  HIS A O   
583  C CB  . HIS A 99  ? 0.2004 0.2622 0.3882 -0.0188 -0.1409 -0.0250 477  HIS A CB  
584  C CG  . HIS A 99  ? 0.2300 0.2832 0.4077 -0.0226 -0.1393 -0.0276 477  HIS A CG  
585  N ND1 . HIS A 99  ? 0.2296 0.2916 0.4225 -0.0268 -0.1313 -0.0250 477  HIS A ND1 
586  C CD2 . HIS A 99  ? 0.2093 0.2459 0.3635 -0.0223 -0.1446 -0.0322 477  HIS A CD2 
587  C CE1 . HIS A 99  ? 0.2560 0.3062 0.4357 -0.0297 -0.1323 -0.0274 477  HIS A CE1 
588  N NE2 . HIS A 99  ? 0.2482 0.2827 0.4046 -0.0264 -0.1404 -0.0324 477  HIS A NE2 
589  N N   . LEU A 100 ? 0.2380 0.2810 0.3695 -0.0072 -0.1418 -0.0307 478  LEU A N   
590  C CA  . LEU A 100 ? 0.2445 0.2776 0.3470 -0.0039 -0.1415 -0.0333 478  LEU A CA  
591  C C   . LEU A 100 ? 0.2314 0.2536 0.3222 -0.0059 -0.1450 -0.0379 478  LEU A C   
592  O O   . LEU A 100 ? 0.2964 0.3153 0.3965 -0.0099 -0.1514 -0.0388 478  LEU A O   
593  C CB  . LEU A 100 ? 0.2159 0.2466 0.3037 -0.0006 -0.1466 -0.0316 478  LEU A CB  
594  C CG  . LEU A 100 ? 0.2777 0.3147 0.3686 0.0025  -0.1438 -0.0268 478  LEU A CG  
595  C CD1 . LEU A 100 ? 0.2448 0.2834 0.3314 0.0044  -0.1352 -0.0257 478  LEU A CD1 
596  C CD2 . LEU A 100 ? 0.3939 0.4391 0.5118 0.0015  -0.1460 -0.0242 478  LEU A CD2 
597  N N   . VAL A 101 ? 0.2835 0.2997 0.3541 -0.0029 -0.1412 -0.0403 479  VAL A N   
598  C CA  . VAL A 101 ? 0.2420 0.2461 0.2999 -0.0030 -0.1445 -0.0456 479  VAL A CA  
599  C C   . VAL A 101 ? 0.2919 0.2868 0.3355 -0.0010 -0.1540 -0.0490 479  VAL A C   
600  O O   . VAL A 101 ? 0.3201 0.3174 0.3514 0.0027  -0.1553 -0.0476 479  VAL A O   
601  C CB  . VAL A 101 ? 0.2604 0.2613 0.2992 0.0013  -0.1383 -0.0470 479  VAL A CB  
602  C CG1 . VAL A 101 ? 0.2408 0.2449 0.2595 0.0075  -0.1360 -0.0443 479  VAL A CG1 
603  C CG2 . VAL A 101 ? 0.2716 0.2587 0.2979 0.0026  -0.1420 -0.0532 479  VAL A CG2 
604  N N   . ALA A 102 ? 0.2921 0.2762 0.3376 -0.0039 -0.1610 -0.0530 480  ALA A N   
605  C CA  . ALA A 102 ? 0.3546 0.3298 0.3910 -0.0036 -0.1715 -0.0559 480  ALA A CA  
606  C C   . ALA A 102 ? 0.4232 0.3904 0.4282 0.0041  -0.1725 -0.0610 480  ALA A C   
607  O O   . ALA A 102 ? 0.3661 0.3327 0.3609 0.0056  -0.1781 -0.0612 480  ALA A O   
608  C CB  . ALA A 102 ? 0.3756 0.3395 0.4213 -0.0088 -0.1794 -0.0582 480  ALA A CB  
609  N N   . ASP A 103 ? 0.3584 0.3206 0.3476 0.0094  -0.1670 -0.0647 481  ASP A N   
610  C CA  . ASP A 103 ? 0.3765 0.3330 0.3358 0.0181  -0.1665 -0.0693 481  ASP A CA  
611  C C   . ASP A 103 ? 0.3471 0.3175 0.2966 0.0226  -0.1569 -0.0636 481  ASP A C   
612  O O   . ASP A 103 ? 0.3952 0.3647 0.3210 0.0304  -0.1538 -0.0655 481  ASP A O   
613  C CB  . ASP A 103 ? 0.3347 0.2759 0.2810 0.0227  -0.1672 -0.0772 481  ASP A CB  
614  C CG  . ASP A 103 ? 0.3534 0.2983 0.3080 0.0222  -0.1589 -0.0751 481  ASP A CG  
615  O OD1 . ASP A 103 ? 0.4353 0.3944 0.4043 0.0184  -0.1524 -0.0679 481  ASP A OD1 
616  O OD2 . ASP A 103 ? 0.3499 0.2825 0.2962 0.0258  -0.1593 -0.0808 481  ASP A OD2 
617  N N   . GLY A 104 ? 0.3297 0.3129 0.2972 0.0183  -0.1521 -0.0560 482  GLY A N   
618  C CA  . GLY A 104 ? 0.3161 0.3113 0.2762 0.0213  -0.1442 -0.0488 482  GLY A CA  
619  C C   . GLY A 104 ? 0.3423 0.3385 0.2883 0.0267  -0.1360 -0.0481 482  GLY A C   
620  O O   . GLY A 104 ? 0.2873 0.2929 0.2221 0.0299  -0.1299 -0.0414 482  GLY A O   
621  N N   . LYS A 105 ? 0.2690 0.2563 0.2165 0.0271  -0.1357 -0.0536 483  LYS A N   
622  C CA  . LYS A 105 ? 0.3149 0.3023 0.2487 0.0329  -0.1286 -0.0532 483  LYS A CA  
623  C C   . LYS A 105 ? 0.2947 0.2861 0.2467 0.0270  -0.1206 -0.0481 483  LYS A C   
624  O O   . LYS A 105 ? 0.2874 0.2778 0.2611 0.0195  -0.1225 -0.0486 483  LYS A O   
625  C CB  . LYS A 105 ? 0.3727 0.3452 0.2916 0.0391  -0.1325 -0.0633 483  LYS A CB  
626  C CG  . LYS A 105 ? 0.3533 0.3217 0.2509 0.0460  -0.1360 -0.0677 483  LYS A CG  
627  C CD  . LYS A 105 ? 0.3499 0.3342 0.2342 0.0506  -0.1281 -0.0591 483  LYS A CD  
628  C CE  . LYS A 105 ? 0.3837 0.3657 0.2456 0.0578  -0.1305 -0.0633 483  LYS A CE  
629  N NZ  . LYS A 105 ? 0.3461 0.3226 0.2130 0.0521  -0.1410 -0.0665 483  LYS A NZ  
630  N N   . PHE A 106 ? 0.3115 0.3087 0.2553 0.0301  -0.1096 -0.0415 484  PHE A N   
631  C CA  . PHE A 106 ? 0.2332 0.2339 0.1917 0.0239  -0.0999 -0.0352 484  PHE A CA  
632  C C   . PHE A 106 ? 0.2749 0.2656 0.2412 0.0214  -0.0985 -0.0397 484  PHE A C   
633  O O   . PHE A 106 ? 0.2430 0.2336 0.2289 0.0134  -0.0976 -0.0390 484  PHE A O   
634  C CB  . PHE A 106 ? 0.2566 0.2663 0.2040 0.0269  -0.0904 -0.0255 484  PHE A CB  
635  C CG  . PHE A 106 ? 0.2506 0.2701 0.2003 0.0243  -0.0904 -0.0176 484  PHE A CG  
636  C CD1 . PHE A 106 ? 0.2581 0.2837 0.1952 0.0290  -0.0959 -0.0152 484  PHE A CD1 
637  C CD2 . PHE A 106 ? 0.1987 0.2206 0.1625 0.0173  -0.0855 -0.0124 484  PHE A CD2 
638  C CE1 . PHE A 106 ? 0.2625 0.2956 0.2033 0.0258  -0.0967 -0.0070 484  PHE A CE1 
639  C CE2 . PHE A 106 ? 0.2259 0.2535 0.1913 0.0155  -0.0869 -0.0059 484  PHE A CE2 
640  C CZ  . PHE A 106 ? 0.2470 0.2800 0.2017 0.0196  -0.0933 -0.0029 484  PHE A CZ  
641  N N   . GLY A 107 ? 0.2365 0.2194 0.1880 0.0285  -0.0983 -0.0439 485  GLY A N   
642  C CA  . GLY A 107 ? 0.2966 0.2680 0.2554 0.0265  -0.0989 -0.0480 485  GLY A CA  
643  C C   . GLY A 107 ? 0.3454 0.3124 0.2895 0.0349  -0.0931 -0.0480 485  GLY A C   
644  O O   . GLY A 107 ? 0.3395 0.3160 0.2816 0.0357  -0.0828 -0.0390 485  GLY A O   
645  N N   . THR A 108 ? 0.3563 0.3081 0.2906 0.0415  -0.1004 -0.0581 486  THR A N   
646  C CA  . THR A 108 ? 0.3251 0.2709 0.2456 0.0518  -0.0958 -0.0600 486  THR A CA  
647  C C   . THR A 108 ? 0.3973 0.3218 0.3215 0.0520  -0.1049 -0.0697 486  THR A C   
648  O O   . THR A 108 ? 0.4626 0.3757 0.3903 0.0480  -0.1174 -0.0776 486  THR A O   
649  C CB  . THR A 108 ? 0.3709 0.3203 0.2651 0.0657  -0.0952 -0.0637 486  THR A CB  
650  O OG1 . THR A 108 ? 0.5810 0.5249 0.4675 0.0659  -0.1067 -0.0721 486  THR A OG1 
651  C CG2 . THR A 108 ? 0.4012 0.3722 0.2916 0.0667  -0.0843 -0.0508 486  THR A CG2 
652  N N   . GLN A 109 ? 0.4039 0.3225 0.3277 0.0565  -0.0997 -0.0685 487  GLN A N   
653  C CA  . GLN A 109 ? 0.4333 0.3294 0.3589 0.0583  -0.1090 -0.0775 487  GLN A CA  
654  C C   . GLN A 109 ? 0.4838 0.3685 0.3828 0.0760  -0.1107 -0.0883 487  GLN A C   
655  O O   . GLN A 109 ? 0.4509 0.3433 0.3405 0.0864  -0.0999 -0.0843 487  GLN A O   
656  C CB  . GLN A 109 ? 0.4322 0.3274 0.3757 0.0519  -0.1034 -0.0694 487  GLN A CB  
657  C CG  . GLN A 109 ? 0.5415 0.4138 0.4950 0.0481  -0.1157 -0.0761 487  GLN A CG  
658  C CD  . GLN A 109 ? 0.5322 0.4055 0.5050 0.0402  -0.1108 -0.0662 487  GLN A CD  
659  O OE1 . GLN A 109 ? 0.3958 0.2782 0.3660 0.0449  -0.0993 -0.0587 487  GLN A OE1 
660  N NE2 . GLN A 109 ? 0.4618 0.3268 0.4546 0.0274  -0.1199 -0.0648 487  GLN A NE2 
661  N N   . GLU A 110 ? 0.4493 0.3165 0.3361 0.0798  -0.1244 -0.1016 488  GLU A N   
662  C CA  . GLU A 110 ? 0.5424 0.3971 0.4002 0.0976  -0.1270 -0.1141 488  GLU A CA  
663  C C   . GLU A 110 ? 0.5083 0.3322 0.3641 0.1013  -0.1397 -0.1265 488  GLU A C   
664  O O   . GLU A 110 ? 0.5232 0.3319 0.3926 0.0896  -0.1537 -0.1298 488  GLU A O   
665  C CB  . GLU A 110 ? 0.4582 0.3156 0.2966 0.1010  -0.1336 -0.1207 488  GLU A CB  
666  C CG  . GLU A 110 ? 0.5428 0.4288 0.3838 0.0968  -0.1237 -0.1083 488  GLU A CG  
667  C CD  . GLU A 110 ? 0.5686 0.4733 0.3950 0.1093  -0.1083 -0.1013 488  GLU A CD  
668  O OE1 . GLU A 110 ? 0.5162 0.4130 0.3289 0.1231  -0.1044 -0.1070 488  GLU A OE1 
669  O OE2 . GLU A 110 ? 0.5746 0.5021 0.4043 0.1053  -0.1005 -0.0894 488  GLU A OE2 
670  N N   . ASN A 116 ? 0.6948 0.3777 0.5327 0.1325  -0.1952 -0.1709 494  ASN A N   
671  C CA  . ASN A 116 ? 0.7913 0.4681 0.6566 0.1217  -0.1985 -0.1628 494  ASN A CA  
672  C C   . ASN A 116 ? 0.8847 0.5802 0.7753 0.1040  -0.1941 -0.1496 494  ASN A C   
673  O O   . ASN A 116 ? 0.8481 0.5528 0.7518 0.1025  -0.1839 -0.1418 494  ASN A O   
674  C CB  . ASN A 116 ? 0.9446 0.5976 0.8180 0.1142  -0.2178 -0.1654 494  ASN A CB  
675  C CG  . ASN A 116 ? 1.0073 0.6562 0.9107 0.1012  -0.2224 -0.1550 494  ASN A CG  
676  O OD1 . ASN A 116 ? 0.8549 0.5121 0.7684 0.1027  -0.2111 -0.1488 494  ASN A OD1 
677  N ND2 . ASN A 116 ? 0.9744 0.6113 0.8927 0.0880  -0.2391 -0.1516 494  ASN A ND2 
678  N N   . LYS A 117 ? 0.9050 0.6063 0.8029 0.0909  -0.2015 -0.1466 495  LYS A N   
679  C CA  . LYS A 117 ? 0.7068 0.4265 0.6292 0.0736  -0.1980 -0.1343 495  LYS A CA  
680  C C   . LYS A 117 ? 0.5922 0.3327 0.5033 0.0774  -0.1855 -0.1339 495  LYS A C   
681  O O   . LYS A 117 ? 0.6055 0.3479 0.4924 0.0886  -0.1838 -0.1418 495  LYS A O   
682  C CB  . LYS A 117 ? 0.6293 0.3473 0.5690 0.0575  -0.2117 -0.1291 495  LYS A CB  
683  N N   . LYS A 118 ? 0.5470 0.3037 0.4759 0.0676  -0.1770 -0.1240 496  LYS A N   
684  C CA  . LYS A 118 ? 0.5082 0.2879 0.4314 0.0676  -0.1657 -0.1205 496  LYS A CA  
685  C C   . LYS A 118 ? 0.5483 0.3394 0.4904 0.0501  -0.1715 -0.1142 496  LYS A C   
686  O O   . LYS A 118 ? 0.5555 0.3438 0.5211 0.0365  -0.1791 -0.1075 496  LYS A O   
687  C CB  . LYS A 118 ? 0.5347 0.3371 0.4673 0.0679  -0.1466 -0.1066 496  LYS A CB  
688  N N   . GLU A 119 ? 0.4986 0.3092 0.4329 0.0511  -0.1648 -0.1121 497  GLU A N   
689  C CA  . GLU A 119 ? 0.4203 0.2423 0.3711 0.0371  -0.1699 -0.1071 497  GLU A CA  
690  C C   . GLU A 119 ? 0.4288 0.2791 0.3794 0.0368  -0.1548 -0.0981 497  GLU A C   
691  O O   . GLU A 119 ? 0.4780 0.3349 0.4067 0.0488  -0.1474 -0.1006 497  GLU A O   
692  C CB  . GLU A 119 ? 0.4439 0.2574 0.3863 0.0387  -0.1808 -0.1123 497  GLU A CB  
693  C CG  . GLU A 119 ? 0.5622 0.3918 0.5182 0.0283  -0.1823 -0.1058 497  GLU A CG  
694  C CD  . GLU A 119 ? 0.7475 0.5732 0.6845 0.0347  -0.1882 -0.1120 497  GLU A CD  
695  O OE1 . GLU A 119 ? 0.6268 0.4588 0.5763 0.0260  -0.1936 -0.1075 497  GLU A OE1 
696  O OE2 . GLU A 119 ? 0.7117 0.5287 0.6215 0.0485  -0.1870 -0.1208 497  GLU A OE2 
697  N N   . TRP A 120 ? 0.3679 0.2349 0.3429 0.0232  -0.1507 -0.0874 498  TRP A N   
698  C CA  . TRP A 120 ? 0.4334 0.3243 0.4099 0.0218  -0.1389 -0.0794 498  TRP A CA  
699  C C   . TRP A 120 ? 0.3750 0.2691 0.3481 0.0207  -0.1476 -0.0835 498  TRP A C   
700  O O   . TRP A 120 ? 0.4049 0.2910 0.3900 0.0132  -0.1608 -0.0864 498  TRP A O   
701  C CB  . TRP A 120 ? 0.3618 0.2683 0.3639 0.0092  -0.1301 -0.0672 498  TRP A CB  
702  C CG  . TRP A 120 ? 0.3513 0.2614 0.3543 0.0102  -0.1182 -0.0601 498  TRP A CG  
703  C CD1 . TRP A 120 ? 0.3399 0.2409 0.3545 0.0054  -0.1197 -0.0575 498  TRP A CD1 
704  C CD2 . TRP A 120 ? 0.3956 0.3196 0.3887 0.0154  -0.1041 -0.0534 498  TRP A CD2 
705  N NE1 . TRP A 120 ? 0.3926 0.3012 0.4048 0.0076  -0.1071 -0.0498 498  TRP A NE1 
706  C CE2 . TRP A 120 ? 0.3794 0.3022 0.3785 0.0136  -0.0975 -0.0471 498  TRP A CE2 
707  C CE3 . TRP A 120 ? 0.3355 0.2728 0.3160 0.0207  -0.0975 -0.0511 498  TRP A CE3 
708  C CZ2 . TRP A 120 ? 0.3729 0.3075 0.3659 0.0167  -0.0848 -0.0385 498  TRP A CZ2 
709  C CZ3 . TRP A 120 ? 0.2961 0.2447 0.2707 0.0235  -0.0852 -0.0424 498  TRP A CZ3 
710  C CH2 . TRP A 120 ? 0.3628 0.3101 0.3435 0.0215  -0.0790 -0.0362 498  TRP A CH2 
711  N N   . ASN A 121 ? 0.3807 0.2870 0.3386 0.0277  -0.1409 -0.0823 499  ASN A N   
712  C CA  . ASN A 121 ? 0.4066 0.3189 0.3617 0.0266  -0.1479 -0.0840 499  ASN A CA  
713  C C   . ASN A 121 ? 0.2913 0.2254 0.2609 0.0207  -0.1379 -0.0732 499  ASN A C   
714  O O   . ASN A 121 ? 0.2703 0.2136 0.2504 0.0170  -0.1263 -0.0652 499  ASN A O   
715  C CB  . ASN A 121 ? 0.4023 0.3102 0.3264 0.0396  -0.1505 -0.0916 499  ASN A CB  
716  C CG  . ASN A 121 ? 0.3893 0.3084 0.2983 0.0492  -0.1355 -0.0865 499  ASN A CG  
717  O OD1 . ASN A 121 ? 0.3114 0.2475 0.2305 0.0453  -0.1244 -0.0757 499  ASN A OD1 
718  N ND2 . ASN A 121 ? 0.4619 0.3715 0.3463 0.0622  -0.1356 -0.0942 499  ASN A ND2 
719  N N   . GLY A 122 ? 0.2981 0.2393 0.2675 0.0197  -0.1435 -0.0732 500  GLY A N   
720  C CA  . GLY A 122 ? 0.2784 0.2378 0.2584 0.0163  -0.1354 -0.0643 500  GLY A CA  
721  C C   . GLY A 122 ? 0.2899 0.2572 0.2983 0.0059  -0.1311 -0.0581 500  GLY A C   
722  O O   . GLY A 122 ? 0.2509 0.2125 0.2755 -0.0008 -0.1379 -0.0598 500  GLY A O   
723  N N   . MET A 123 ? 0.2273 0.2079 0.2410 0.0045  -0.1197 -0.0504 501  MET A N   
724  C CA  . MET A 123 ? 0.2175 0.2072 0.2552 -0.0038 -0.1137 -0.0449 501  MET A CA  
725  C C   . MET A 123 ? 0.2298 0.2149 0.2748 -0.0085 -0.1091 -0.0434 501  MET A C   
726  O O   . MET A 123 ? 0.2259 0.2161 0.2923 -0.0164 -0.1085 -0.0404 501  MET A O   
727  C CB  . MET A 123 ? 0.1947 0.1961 0.2318 -0.0031 -0.1033 -0.0383 501  MET A CB  
728  C CG  . MET A 123 ? 0.1941 0.2018 0.2329 -0.0011 -0.1087 -0.0380 501  MET A CG  
729  S SD  . MET A 123 ? 0.2179 0.2351 0.2544 0.0001  -0.0991 -0.0307 501  MET A SD  
730  C CE  . MET A 123 ? 0.1812 0.1950 0.1936 0.0043  -0.0920 -0.0269 501  MET A CE  
731  N N   . MET A 124 ? 0.2437 0.2207 0.2723 -0.0035 -0.1057 -0.0444 502  MET A N   
732  C CA  . MET A 124 ? 0.2712 0.2422 0.3067 -0.0077 -0.1030 -0.0426 502  MET A CA  
733  C C   . MET A 124 ? 0.2774 0.2373 0.3245 -0.0123 -0.1157 -0.0476 502  MET A C   
734  O O   . MET A 124 ? 0.2646 0.2265 0.3308 -0.0212 -0.1154 -0.0432 502  MET A O   
735  C CB  . MET A 124 ? 0.2322 0.1964 0.2481 0.0002  -0.0981 -0.0430 502  MET A CB  
736  C CG  . MET A 124 ? 0.2829 0.2586 0.2905 0.0023  -0.0858 -0.0352 502  MET A CG  
737  S SD  . MET A 124 ? 0.3154 0.2995 0.3394 -0.0082 -0.0750 -0.0254 502  MET A SD  
738  C CE  . MET A 124 ? 0.2525 0.2241 0.2816 -0.0102 -0.0779 -0.0264 502  MET A CE  
739  N N   . GLY A 125 ? 0.2810 0.2292 0.3162 -0.0070 -0.1278 -0.0561 503  GLY A N   
740  C CA  . GLY A 125 ? 0.2794 0.2146 0.3246 -0.0120 -0.1425 -0.0608 503  GLY A CA  
741  C C   . GLY A 125 ? 0.2810 0.2281 0.3530 -0.0224 -0.1459 -0.0552 503  GLY A C   
742  O O   . GLY A 125 ? 0.2838 0.2282 0.3720 -0.0296 -0.1494 -0.0512 503  GLY A O   
743  N N   . GLU A 126 ? 0.2658 0.2281 0.3423 -0.0219 -0.1420 -0.0526 504  GLU A N   
744  C CA  . GLU A 126 ? 0.2754 0.2515 0.3767 -0.0292 -0.1412 -0.0460 504  GLU A CA  
745  C C   . GLU A 126 ? 0.3096 0.2991 0.4318 -0.0371 -0.1315 -0.0381 504  GLU A C   
746  O O   . GLU A 126 ? 0.3047 0.3024 0.4478 -0.0440 -0.1316 -0.0319 504  GLU A O   
747  C CB  . GLU A 126 ? 0.2563 0.2438 0.3567 -0.0253 -0.1397 -0.0457 504  GLU A CB  
748  C CG  . GLU A 126 ? 0.2892 0.2662 0.3706 -0.0189 -0.1488 -0.0514 504  GLU A CG  
749  C CD  . GLU A 126 ? 0.3465 0.3346 0.4374 -0.0190 -0.1505 -0.0483 504  GLU A CD  
750  O OE1 . GLU A 126 ? 0.2716 0.2751 0.3840 -0.0228 -0.1445 -0.0426 504  GLU A OE1 
751  O OE2 . GLU A 126 ? 0.3302 0.3115 0.4071 -0.0150 -0.1576 -0.0515 504  GLU A OE2 
752  N N   . LEU A 127 ? 0.2587 0.2513 0.3713 -0.0347 -0.1189 -0.0359 505  LEU A N   
753  C CA  . LEU A 127 ? 0.2898 0.2946 0.4176 -0.0416 -0.1076 -0.0279 505  LEU A CA  
754  C C   . LEU A 127 ? 0.2428 0.2401 0.3805 -0.0490 -0.1127 -0.0252 505  LEU A C   
755  O O   . LEU A 127 ? 0.2056 0.2148 0.3643 -0.0576 -0.1096 -0.0176 505  LEU A O   
756  C CB  . LEU A 127 ? 0.2506 0.2584 0.3624 -0.0373 -0.0936 -0.0256 505  LEU A CB  
757  C CG  . LEU A 127 ? 0.2482 0.2682 0.3711 -0.0441 -0.0813 -0.0178 505  LEU A CG  
758  C CD1 . LEU A 127 ? 0.2647 0.3021 0.4071 -0.0472 -0.0774 -0.0148 505  LEU A CD1 
759  C CD2 . LEU A 127 ? 0.2066 0.2259 0.3111 -0.0404 -0.0702 -0.0156 505  LEU A CD2 
760  N N   . LEU A 128 ? 0.2533 0.2312 0.3755 -0.0451 -0.1201 -0.0307 506  LEU A N   
761  C CA  . LEU A 128 ? 0.3094 0.2771 0.4395 -0.0511 -0.1255 -0.0280 506  LEU A CA  
762  C C   . LEU A 128 ? 0.2999 0.2627 0.4403 -0.0544 -0.1357 -0.0266 506  LEU A C   
763  O O   . LEU A 128 ? 0.2596 0.2230 0.4133 -0.0615 -0.1365 -0.0194 506  LEU A O   
764  C CB  . LEU A 128 ? 0.2638 0.2117 0.3721 -0.0432 -0.1282 -0.0345 506  LEU A CB  
765  C CG  . LEU A 128 ? 0.2843 0.2380 0.3778 -0.0375 -0.1128 -0.0315 506  LEU A CG  
766  C CD1 . LEU A 128 ? 0.2904 0.2277 0.3597 -0.0257 -0.1148 -0.0389 506  LEU A CD1 
767  C CD2 . LEU A 128 ? 0.3092 0.2704 0.4162 -0.0465 -0.1046 -0.0214 506  LEU A CD2 
768  N N   . SER A 129 ? 0.3023 0.2605 0.4364 -0.0499 -0.1439 -0.0324 507  SER A N   
769  C CA  . SER A 129 ? 0.3062 0.2590 0.4497 -0.0536 -0.1548 -0.0305 507  SER A CA  
770  C C   . SER A 129 ? 0.3251 0.2997 0.4934 -0.0612 -0.1505 -0.0207 507  SER A C   
771  O O   . SER A 129 ? 0.3156 0.2885 0.4954 -0.0658 -0.1592 -0.0165 507  SER A O   
772  C CB  . SER A 129 ? 0.3159 0.2551 0.4418 -0.0461 -0.1654 -0.0398 507  SER A CB  
773  O OG  . SER A 129 ? 0.3789 0.3328 0.5069 -0.0441 -0.1615 -0.0397 507  SER A OG  
774  N N   . GLY A 130 ? 0.2871 0.2820 0.4638 -0.0621 -0.1376 -0.0168 508  GLY A N   
775  C CA  . GLY A 130 ? 0.2238 0.2409 0.4232 -0.0672 -0.1322 -0.0086 508  GLY A CA  
776  C C   . GLY A 130 ? 0.2296 0.2548 0.4322 -0.0631 -0.1343 -0.0112 508  GLY A C   
777  O O   . GLY A 130 ? 0.2972 0.3426 0.5196 -0.0657 -0.1288 -0.0048 508  GLY A O   
778  N N   . GLN A 131 ? 0.2294 0.2402 0.4130 -0.0561 -0.1420 -0.0199 509  GLN A N   
779  C CA  . GLN A 131 ? 0.2269 0.2449 0.4119 -0.0519 -0.1439 -0.0218 509  GLN A CA  
780  C C   . GLN A 131 ? 0.2373 0.2734 0.4286 -0.0491 -0.1316 -0.0205 509  GLN A C   
781  O O   . GLN A 131 ? 0.2727 0.3205 0.4744 -0.0469 -0.1312 -0.0190 509  GLN A O   
782  C CB  . GLN A 131 ? 0.2414 0.2408 0.4008 -0.0446 -0.1531 -0.0310 509  GLN A CB  
783  C CG  . GLN A 131 ? 0.2667 0.2479 0.4198 -0.0462 -0.1669 -0.0333 509  GLN A CG  
784  C CD  . GLN A 131 ? 0.4212 0.3828 0.5444 -0.0380 -0.1735 -0.0435 509  GLN A CD  
785  O OE1 . GLN A 131 ? 0.5365 0.4826 0.6451 -0.0354 -0.1753 -0.0485 509  GLN A OE1 
786  N NE2 . GLN A 131 ? 0.4325 0.3954 0.5464 -0.0334 -0.1766 -0.0464 509  GLN A NE2 
787  N N   . ALA A 132 ? 0.2453 0.2829 0.4307 -0.0489 -0.1222 -0.0208 510  ALA A N   
788  C CA  . ALA A 132 ? 0.2199 0.2730 0.4111 -0.0468 -0.1107 -0.0194 510  ALA A CA  
789  C C   . ALA A 132 ? 0.2740 0.3354 0.4728 -0.0525 -0.0993 -0.0137 510  ALA A C   
790  O O   . ALA A 132 ? 0.3177 0.3687 0.5102 -0.0565 -0.1010 -0.0128 510  ALA A O   
791  C CB  . ALA A 132 ? 0.2183 0.2618 0.3832 -0.0382 -0.1081 -0.0254 510  ALA A CB  
792  N N   . ASP A 133 ? 0.2118 0.2906 0.4205 -0.0517 -0.0864 -0.0098 511  ASP A N   
793  C CA  . ASP A 133 ? 0.2007 0.2881 0.4112 -0.0560 -0.0732 -0.0044 511  ASP A CA  
794  C C   . ASP A 133 ? 0.2537 0.3350 0.4403 -0.0505 -0.0621 -0.0072 511  ASP A C   
795  O O   . ASP A 133 ? 0.2005 0.2841 0.3825 -0.0544 -0.0527 -0.0032 511  ASP A O   
796  C CB  . ASP A 133 ? 0.1668 0.2787 0.4032 -0.0588 -0.0653 0.0020  511  ASP A CB  
797  C CG  . ASP A 133 ? 0.2243 0.3429 0.4817 -0.0645 -0.0746 0.0074  511  ASP A CG  
798  O OD1 . ASP A 133 ? 0.2369 0.3429 0.4885 -0.0697 -0.0815 0.0094  511  ASP A OD1 
799  O OD2 . ASP A 133 ? 0.2573 0.3913 0.5324 -0.0622 -0.0740 0.0098  511  ASP A OD2 
800  N N   . MET A 134 ? 0.2081 0.2818 0.3796 -0.0425 -0.0639 -0.0127 512  MET A N   
801  C CA  . MET A 134 ? 0.2255 0.2938 0.3758 -0.0379 -0.0551 -0.0139 512  MET A CA  
802  C C   . MET A 134 ? 0.1843 0.2413 0.3179 -0.0307 -0.0625 -0.0187 512  MET A C   
803  O O   . MET A 134 ? 0.2174 0.2763 0.3589 -0.0276 -0.0706 -0.0213 512  MET A O   
804  C CB  . MET A 134 ? 0.1899 0.2709 0.3466 -0.0359 -0.0437 -0.0128 512  MET A CB  
805  C CG  . MET A 134 ? 0.1569 0.2315 0.2923 -0.0339 -0.0347 -0.0127 512  MET A CG  
806  S SD  . MET A 134 ? 0.2535 0.3395 0.3937 -0.0303 -0.0226 -0.0136 512  MET A SD  
807  C CE  . MET A 134 ? 0.2381 0.3395 0.3920 -0.0388 -0.0129 -0.0076 512  MET A CE  
808  N N   . ILE A 135 ? 0.2136 0.2606 0.3252 -0.0285 -0.0599 -0.0186 513  ILE A N   
809  C CA  . ILE A 135 ? 0.2187 0.2578 0.3130 -0.0219 -0.0651 -0.0210 513  ILE A CA  
810  C C   . ILE A 135 ? 0.1917 0.2326 0.2779 -0.0191 -0.0581 -0.0191 513  ILE A C   
811  O O   . ILE A 135 ? 0.2009 0.2406 0.2786 -0.0216 -0.0497 -0.0158 513  ILE A O   
812  C CB  . ILE A 135 ? 0.1857 0.2140 0.2616 -0.0205 -0.0675 -0.0211 513  ILE A CB  
813  C CG1 . ILE A 135 ? 0.1829 0.2060 0.2660 -0.0233 -0.0749 -0.0238 513  ILE A CG1 
814  C CG2 . ILE A 135 ? 0.1563 0.1800 0.2152 -0.0135 -0.0730 -0.0225 513  ILE A CG2 
815  C CD1 . ILE A 135 ? 0.1677 0.1789 0.2325 -0.0195 -0.0778 -0.0255 513  ILE A CD1 
816  N N   . VAL A 136 ? 0.1718 0.2144 0.2608 -0.0145 -0.0627 -0.0210 514  VAL A N   
817  C CA  . VAL A 136 ? 0.1985 0.2395 0.2793 -0.0112 -0.0591 -0.0196 514  VAL A CA  
818  C C   . VAL A 136 ? 0.1875 0.2228 0.2548 -0.0068 -0.0679 -0.0188 514  VAL A C   
819  O O   . VAL A 136 ? 0.1807 0.2181 0.2552 -0.0036 -0.0757 -0.0206 514  VAL A O   
820  C CB  . VAL A 136 ? 0.1780 0.2267 0.2760 -0.0090 -0.0563 -0.0218 514  VAL A CB  
821  C CG1 . VAL A 136 ? 0.1596 0.2026 0.2471 -0.0053 -0.0538 -0.0213 514  VAL A CG1 
822  C CG2 . VAL A 136 ? 0.1403 0.1984 0.2523 -0.0132 -0.0472 -0.0216 514  VAL A CG2 
823  N N   . ALA A 137 ? 0.1561 0.1859 0.2045 -0.0070 -0.0667 -0.0149 515  ALA A N   
824  C CA  . ALA A 137 ? 0.2064 0.2337 0.2408 -0.0030 -0.0740 -0.0124 515  ALA A CA  
825  C C   . ALA A 137 ? 0.1876 0.2118 0.2043 -0.0040 -0.0695 -0.0056 515  ALA A C   
826  O O   . ALA A 137 ? 0.1651 0.1881 0.1805 -0.0079 -0.0617 -0.0036 515  ALA A O   
827  C CB  . ALA A 137 ? 0.1787 0.2055 0.2115 -0.0011 -0.0810 -0.0163 515  ALA A CB  
828  N N   . PRO A 138 ? 0.1863 0.2107 0.1901 -0.0010 -0.0745 -0.0003 516  PRO A N   
829  C CA  . PRO A 138 ? 0.1948 0.2192 0.1832 -0.0018 -0.0708 0.0080  516  PRO A CA  
830  C C   . PRO A 138 ? 0.2216 0.2468 0.2043 -0.0004 -0.0674 0.0070  516  PRO A C   
831  O O   . PRO A 138 ? 0.2335 0.2617 0.2046 0.0044  -0.0700 0.0093  516  PRO A O   
832  C CB  . PRO A 138 ? 0.1978 0.2253 0.1766 0.0013  -0.0782 0.0144  516  PRO A CB  
833  C CG  . PRO A 138 ? 0.1632 0.1922 0.1493 0.0047  -0.0860 0.0078  516  PRO A CG  
834  C CD  . PRO A 138 ? 0.1595 0.1858 0.1635 0.0026  -0.0839 0.0000  516  PRO A CD  
835  N N   . LEU A 139 ? 0.2081 0.2307 0.1985 -0.0041 -0.0616 0.0038  517  LEU A N   
836  C CA  . LEU A 139 ? 0.2131 0.2341 0.2016 -0.0029 -0.0596 0.0016  517  LEU A CA  
837  C C   . LEU A 139 ? 0.2104 0.2318 0.1908 -0.0052 -0.0525 0.0100  517  LEU A C   
838  O O   . LEU A 139 ? 0.1789 0.1991 0.1639 -0.0115 -0.0471 0.0129  517  LEU A O   
839  C CB  . LEU A 139 ? 0.1948 0.2134 0.1992 -0.0066 -0.0593 -0.0054 517  LEU A CB  
840  C CG  . LEU A 139 ? 0.1929 0.2065 0.1976 -0.0056 -0.0604 -0.0092 517  LEU A CG  
841  C CD1 . LEU A 139 ? 0.1782 0.1886 0.1749 0.0016  -0.0690 -0.0152 517  LEU A CD1 
842  C CD2 . LEU A 139 ? 0.1561 0.1691 0.1789 -0.0120 -0.0597 -0.0124 517  LEU A CD2 
843  N N   . THR A 140 ? 0.1988 0.2227 0.1670 0.0003  -0.0525 0.0142  518  THR A N   
844  C CA  . THR A 140 ? 0.2006 0.2271 0.1624 -0.0013 -0.0465 0.0240  518  THR A CA  
845  C C   . THR A 140 ? 0.2058 0.2277 0.1747 -0.0045 -0.0419 0.0220  518  THR A C   
846  O O   . THR A 140 ? 0.1774 0.1946 0.1506 -0.0014 -0.0442 0.0139  518  THR A O   
847  C CB  . THR A 140 ? 0.1930 0.2263 0.1415 0.0069  -0.0470 0.0293  518  THR A CB  
848  O OG1 . THR A 140 ? 0.1633 0.2024 0.1057 0.0085  -0.0518 0.0335  518  THR A OG1 
849  C CG2 . THR A 140 ? 0.1557 0.1938 0.1002 0.0057  -0.0407 0.0409  518  THR A CG2 
850  N N   . ILE A 141 ? 0.1640 0.1864 0.1339 -0.0113 -0.0365 0.0300  519  ILE A N   
851  C CA  . ILE A 141 ? 0.2344 0.2537 0.2109 -0.0155 -0.0323 0.0309  519  ILE A CA  
852  C C   . ILE A 141 ? 0.2332 0.2548 0.2033 -0.0094 -0.0304 0.0366  519  ILE A C   
853  O O   . ILE A 141 ? 0.2274 0.2553 0.1897 -0.0088 -0.0281 0.0473  519  ILE A O   
854  C CB  . ILE A 141 ? 0.2331 0.2523 0.2120 -0.0257 -0.0277 0.0374  519  ILE A CB  
855  C CG1 . ILE A 141 ? 0.1920 0.2099 0.1759 -0.0292 -0.0287 0.0314  519  ILE A CG1 
856  C CG2 . ILE A 141 ? 0.2312 0.2482 0.2180 -0.0310 -0.0241 0.0392  519  ILE A CG2 
857  C CD1 . ILE A 141 ? 0.2169 0.2336 0.1978 -0.0375 -0.0246 0.0367  519  ILE A CD1 
858  N N   . ASN A 142 ? 0.2053 0.2215 0.1790 -0.0047 -0.0317 0.0300  520  ASN A N   
859  C CA  . ASN A 142 ? 0.2240 0.2410 0.1929 0.0025  -0.0293 0.0341  520  ASN A CA  
860  C C   . ASN A 142 ? 0.2713 0.2796 0.2509 -0.0003 -0.0295 0.0310  520  ASN A C   
861  O O   . ASN A 142 ? 0.2369 0.2394 0.2269 -0.0070 -0.0323 0.0251  520  ASN A O   
862  C CB  . ASN A 142 ? 0.2294 0.2479 0.1868 0.0157  -0.0322 0.0283  520  ASN A CB  
863  C CG  . ASN A 142 ? 0.3193 0.3275 0.2784 0.0191  -0.0394 0.0135  520  ASN A CG  
864  O OD1 . ASN A 142 ? 0.2452 0.2444 0.2158 0.0135  -0.0422 0.0080  520  ASN A OD1 
865  N ND2 . ASN A 142 ? 0.2771 0.2873 0.2246 0.0278  -0.0432 0.0082  520  ASN A ND2 
866  N N   . ASN A 143 ? 0.4296 0.1931 0.3227 0.0723  -0.0931 -0.0563 521  ASN A N   
867  C CA  . ASN A 143 ? 0.4030 0.1454 0.2837 0.0726  -0.1003 -0.0525 521  ASN A CA  
868  C C   . ASN A 143 ? 0.4324 0.1444 0.2878 0.0597  -0.1081 -0.0488 521  ASN A C   
869  O O   . ASN A 143 ? 0.4493 0.1440 0.2928 0.0533  -0.1181 -0.0414 521  ASN A O   
870  C CB  . ASN A 143 ? 0.4369 0.1798 0.3216 0.0839  -0.0931 -0.0588 521  ASN A CB  
871  C CG  . ASN A 143 ? 0.4688 0.1844 0.3388 0.0846  -0.1002 -0.0556 521  ASN A CG  
872  O OD1 . ASN A 143 ? 0.5196 0.2102 0.3716 0.0790  -0.1019 -0.0570 521  ASN A OD1 
873  N ND2 . ASN A 143 ? 0.4610 0.1810 0.3384 0.0909  -0.1044 -0.0511 521  ASN A ND2 
874  N N   . GLU A 144 ? 0.4404 0.1462 0.2861 0.0539  -0.1040 -0.0534 522  GLU A N   
875  C CA  . GLU A 144 ? 0.4697 0.1490 0.2905 0.0399  -0.1101 -0.0506 522  GLU A CA  
876  C C   . GLU A 144 ? 0.4682 0.1441 0.2812 0.0251  -0.1214 -0.0401 522  GLU A C   
877  O O   . GLU A 144 ? 0.4914 0.1476 0.2872 0.0148  -0.1297 -0.0336 522  GLU A O   
878  C CB  . GLU A 144 ? 0.4754 0.1538 0.2888 0.0353  -0.1033 -0.0577 522  GLU A CB  
879  C CG  . GLU A 144 ? 0.4850 0.1625 0.3019 0.0460  -0.0930 -0.0687 522  GLU A CG  
880  C CD  . GLU A 144 ? 0.5154 0.2213 0.3555 0.0580  -0.0836 -0.0740 522  GLU A CD  
881  O OE1 . GLU A 144 ? 0.4292 0.1543 0.2836 0.0597  -0.0848 -0.0695 522  GLU A OE1 
882  O OE2 . GLU A 144 ? 0.5615 0.2708 0.4057 0.0650  -0.0748 -0.0830 522  GLU A OE2 
883  N N   . ARG A 145 ? 0.4408 0.1393 0.2682 0.0230  -0.1215 -0.0376 523  ARG A N   
884  C CA  . ARG A 145 ? 0.4310 0.1468 0.2597 0.0076  -0.1279 -0.0251 523  ARG A CA  
885  C C   . ARG A 145 ? 0.4231 0.1486 0.2604 0.0081  -0.1335 -0.0176 523  ARG A C   
886  O O   . ARG A 145 ? 0.4330 0.1569 0.2597 -0.0064 -0.1417 -0.0081 523  ARG A O   
887  C CB  . ARG A 145 ? 0.4128 0.1620 0.2609 0.0063  -0.1229 -0.0227 523  ARG A CB  
888  C CG  . ARG A 145 ? 0.4098 0.1528 0.2473 0.0009  -0.1194 -0.0265 523  ARG A CG  
889  C CD  . ARG A 145 ? 0.3837 0.1567 0.2437 0.0050  -0.1132 -0.0254 523  ARG A CD  
890  N NE  . ARG A 145 ? 0.3899 0.1599 0.2390 -0.0028 -0.1113 -0.0263 523  ARG A NE  
891  C CZ  . ARG A 145 ? 0.3725 0.1614 0.2359 0.0000  -0.1059 -0.0259 523  ARG A CZ  
892  N NH1 . ARG A 145 ? 0.3451 0.1557 0.2345 0.0107  -0.1012 -0.0258 523  ARG A NH1 
893  N NH2 . ARG A 145 ? 0.3846 0.1703 0.2353 -0.0091 -0.1052 -0.0256 523  ARG A NH2 
894  N N   . ALA A 146 ? 0.4059 0.1437 0.2618 0.0233  -0.1292 -0.0215 524  ALA A N   
895  C CA  . ALA A 146 ? 0.3975 0.1483 0.2624 0.0232  -0.1342 -0.0144 524  ALA A CA  
896  C C   . ALA A 146 ? 0.4383 0.1566 0.2804 0.0176  -0.1437 -0.0094 524  ALA A C   
897  O O   . ALA A 146 ? 0.4974 0.2247 0.3410 0.0113  -0.1502 -0.0005 524  ALA A O   
898  C CB  . ALA A 146 ? 0.3750 0.1448 0.2626 0.0402  -0.1274 -0.0205 524  ALA A CB  
899  N N   . GLN A 147 ? 0.4649 0.1452 0.2857 0.0191  -0.1445 -0.0151 525  GLN A N   
900  C CA  . GLN A 147 ? 0.5069 0.1512 0.3044 0.0132  -0.1535 -0.0104 525  GLN A CA  
901  C C   . GLN A 147 ? 0.5493 0.1889 0.3288 -0.0100 -0.1622 0.0001  525  GLN A C   
902  O O   . GLN A 147 ? 0.5994 0.2175 0.3628 -0.0185 -0.1713 0.0079  525  GLN A O   
903  C CB  . GLN A 147 ? 0.5259 0.1529 0.3138 0.0207  -0.1457 -0.0199 525  GLN A CB  
904  C CG  . GLN A 147 ? 0.6359 0.2424 0.4167 0.0271  -0.1484 -0.0187 525  GLN A CG  
905  C CD  . GLN A 147 ? 0.7848 0.3830 0.5670 0.0400  -0.1384 -0.0301 525  GLN A CD  
906  O OE1 . GLN A 147 ? 0.7213 0.3401 0.5216 0.0529  -0.1286 -0.0383 525  GLN A OE1 
907  N NE2 . GLN A 147 ? 0.8160 0.3845 0.5793 0.0355  -0.1406 -0.0308 525  GLN A NE2 
908  N N   . TYR A 148 ? 0.5009 0.1617 0.2830 -0.0209 -0.1599 0.0014  526  TYR A N   
909  C CA  . TYR A 148 ? 0.5584 0.2193 0.3237 -0.0435 -0.1675 0.0108  526  TYR A CA  
910  C C   . TYR A 148 ? 0.6076 0.3145 0.3924 -0.0515 -0.1683 0.0193  526  TYR A C   
911  O O   . TYR A 148 ? 0.6145 0.3270 0.3885 -0.0694 -0.1762 0.0289  526  TYR A O   
912  C CB  . TYR A 148 ? 0.5482 0.1922 0.2953 -0.0525 -0.1655 0.0057  526  TYR A CB  
913  C CG  . TYR A 148 ? 0.6247 0.2300 0.3507 -0.0487 -0.1634 -0.0010 526  TYR A CG  
914  C CD1 . TYR A 148 ? 0.5965 0.1976 0.3313 -0.0296 -0.1532 -0.0127 526  TYR A CD1 
915  C CD2 . TYR A 148 ? 0.6164 0.1999 0.3179 -0.0632 -0.1692 0.0050  526  TYR A CD2 
916  C CE1 . TYR A 148 ? 0.6075 0.1842 0.3292 -0.0251 -0.1491 -0.0191 526  TYR A CE1 
917  C CE2 . TYR A 148 ? 0.7230 0.2786 0.4100 -0.0583 -0.1653 -0.0016 526  TYR A CE2 
918  C CZ  . TYR A 148 ? 0.6830 0.2356 0.3811 -0.0390 -0.1553 -0.0139 526  TYR A CZ  
919  O OH  . TYR A 148 ? 0.7626 0.2894 0.4489 -0.0343 -0.1511 -0.0214 526  TYR A OH  
920  N N   . ILE A 149 ? 0.4842 0.2241 0.2970 -0.0392 -0.1604 0.0155  527  ILE A N   
921  C CA  . ILE A 149 ? 0.4718 0.2552 0.3057 -0.0445 -0.1601 0.0216  527  ILE A CA  
922  C C   . ILE A 149 ? 0.4827 0.2907 0.3427 -0.0306 -0.1555 0.0190  527  ILE A C   
923  O O   . ILE A 149 ? 0.4965 0.2908 0.3595 -0.0164 -0.1520 0.0128  527  ILE A O   
924  C CB  . ILE A 149 ? 0.4694 0.2717 0.3134 -0.0451 -0.1549 0.0201  527  ILE A CB  
925  C CG1 . ILE A 149 ? 0.4414 0.2437 0.3007 -0.0267 -0.1447 0.0098  527  ILE A CG1 
926  C CG2 . ILE A 149 ? 0.5026 0.2843 0.3202 -0.0607 -0.1596 0.0229  527  ILE A CG2 
927  C CD1 . ILE A 149 ? 0.4050 0.2352 0.2838 -0.0246 -0.1393 0.0101  527  ILE A CD1 
928  N N   . GLU A 150 ? 0.4778 0.3248 0.3574 -0.0350 -0.1553 0.0234  528  GLU A N   
929  C CA  . GLU A 150 ? 0.3659 0.2419 0.2718 -0.0242 -0.1500 0.0201  528  GLU A CA  
930  C C   . GLU A 150 ? 0.3639 0.2633 0.2945 -0.0139 -0.1404 0.0137  528  GLU A C   
931  O O   . GLU A 150 ? 0.3774 0.2928 0.3137 -0.0203 -0.1404 0.0169  528  GLU A O   
932  C CB  . GLU A 150 ? 0.5088 0.4136 0.4207 -0.0363 -0.1556 0.0277  528  GLU A CB  
933  C CG  . GLU A 150 ? 0.4666 0.4107 0.4091 -0.0278 -0.1488 0.0230  528  GLU A CG  
934  C CD  . GLU A 150 ? 0.4639 0.4054 0.4092 -0.0201 -0.1484 0.0209  528  GLU A CD  
935  O OE1 . GLU A 150 ? 0.6401 0.5489 0.5643 -0.0205 -0.1543 0.0242  528  GLU A OE1 
936  O OE2 . GLU A 150 ? 0.4625 0.4350 0.4314 -0.0135 -0.1423 0.0160  528  GLU A OE2 
937  N N   . PHE A 151 ? 0.4358 0.3370 0.3808 0.0018  -0.1325 0.0051  529  PHE A N   
938  C CA  . PHE A 151 ? 0.2628 0.1849 0.2317 0.0115  -0.1230 -0.0012 529  PHE A CA  
939  C C   . PHE A 151 ? 0.3035 0.2609 0.2980 0.0149  -0.1191 -0.0034 529  PHE A C   
940  O O   . PHE A 151 ? 0.3205 0.2820 0.3160 0.0168  -0.1203 -0.0042 529  PHE A O   
941  C CB  . PHE A 151 ? 0.2650 0.1689 0.2334 0.0252  -0.1159 -0.0103 529  PHE A CB  
942  C CG  . PHE A 151 ? 0.2895 0.1679 0.2400 0.0229  -0.1162 -0.0109 529  PHE A CG  
943  C CD1 . PHE A 151 ? 0.3069 0.1954 0.2633 0.0189  -0.1142 -0.0086 529  PHE A CD1 
944  C CD2 . PHE A 151 ? 0.3229 0.1681 0.2511 0.0248  -0.1183 -0.0141 529  PHE A CD2 
945  C CE1 . PHE A 151 ? 0.3121 0.1800 0.2514 0.0152  -0.1146 -0.0089 529  PHE A CE1 
946  C CE2 . PHE A 151 ? 0.3336 0.1573 0.2451 0.0217  -0.1178 -0.0163 529  PHE A CE2 
947  C CZ  . PHE A 151 ? 0.3399 0.1761 0.2564 0.0160  -0.1160 -0.0135 529  PHE A CZ  
948  N N   . SER A 152 ? 0.2264 0.2097 0.2418 0.0155  -0.1147 -0.0043 530  SER A N   
949  C CA  . SER A 152 ? 0.2071 0.2225 0.2490 0.0208  -0.1084 -0.0099 530  SER A CA  
950  C C   . SER A 152 ? 0.1828 0.1941 0.2350 0.0346  -0.0991 -0.0199 530  SER A C   
951  O O   . SER A 152 ? 0.2064 0.1927 0.2471 0.0405  -0.0973 -0.0224 530  SER A O   
952  C CB  . SER A 152 ? 0.1818 0.2234 0.2441 0.0190  -0.1060 -0.0089 530  SER A CB  
953  O OG  . SER A 152 ? 0.1727 0.2059 0.2425 0.0270  -0.1002 -0.0118 530  SER A OG  
954  N N   . LYS A 153 ? 0.1631 0.2011 0.2371 0.0390  -0.0929 -0.0264 531  LYS A N   
955  C CA  . LYS A 153 ? 0.1694 0.2088 0.2562 0.0506  -0.0831 -0.0363 531  LYS A CA  
956  C C   . LYS A 153 ? 0.1752 0.2075 0.2689 0.0548  -0.0780 -0.0380 531  LYS A C   
957  O O   . LYS A 153 ? 0.1471 0.1866 0.2465 0.0502  -0.0803 -0.0329 531  LYS A O   
958  C CB  . LYS A 153 ? 0.1324 0.2043 0.2419 0.0522  -0.0768 -0.0435 531  LYS A CB  
959  C CG  . LYS A 153 ? 0.1348 0.2146 0.2379 0.0493  -0.0807 -0.0424 531  LYS A CG  
960  C CD  . LYS A 153 ? 0.2111 0.2725 0.3044 0.0582  -0.0791 -0.0456 531  LYS A CD  
961  C CE  . LYS A 153 ? 0.1498 0.2223 0.2399 0.0564  -0.0830 -0.0436 531  LYS A CE  
962  N NZ  . LYS A 153 ? 0.1775 0.2352 0.2468 0.0471  -0.0952 -0.0319 531  LYS A NZ  
963  N N   . PRO A 154 ? 0.1669 0.1864 0.2600 0.0632  -0.0716 -0.0443 532  PRO A N   
964  C CA  . PRO A 154 ? 0.1695 0.1795 0.2654 0.0654  -0.0679 -0.0442 532  PRO A CA  
965  C C   . PRO A 154 ? 0.1350 0.1665 0.2561 0.0663  -0.0632 -0.0454 532  PRO A C   
966  O O   . PRO A 154 ? 0.1269 0.1739 0.2574 0.0649  -0.0536 -0.0506 532  PRO A O   
967  C CB  . PRO A 154 ? 0.1625 0.1619 0.2548 0.0728  -0.0604 -0.0523 532  PRO A CB  
968  C CG  . PRO A 154 ? 0.1584 0.1531 0.2400 0.0756  -0.0636 -0.0545 532  PRO A CG  
969  C CD  . PRO A 154 ? 0.1507 0.1652 0.2399 0.0704  -0.0679 -0.0512 532  PRO A CD  
970  N N   . PHE A 155 ? 0.1396 0.1678 0.2613 0.0630  -0.0667 -0.0378 533  PHE A N   
971  C CA  . PHE A 155 ? 0.1518 0.1943 0.2937 0.0640  -0.0607 -0.0376 533  PHE A CA  
972  C C   . PHE A 155 ? 0.1930 0.2223 0.3344 0.0665  -0.0526 -0.0388 533  PHE A C   
973  O O   . PHE A 155 ? 0.1674 0.2035 0.3204 0.0664  -0.0456 -0.0386 533  PHE A O   
974  C CB  . PHE A 155 ? 0.1323 0.1844 0.2801 0.0601  -0.0700 -0.0278 533  PHE A CB  
975  C CG  . PHE A 155 ? 0.1484 0.1805 0.2773 0.0553  -0.0762 -0.0180 533  PHE A CG  
976  C CD1 . PHE A 155 ? 0.1514 0.1769 0.2871 0.0584  -0.0740 -0.0143 533  PHE A CD1 
977  C CD2 . PHE A 155 ? 0.1880 0.2082 0.2918 0.0466  -0.0843 -0.0120 533  PHE A CD2 
978  C CE1 . PHE A 155 ? 0.1984 0.2087 0.3162 0.0525  -0.0798 -0.0050 533  PHE A CE1 
979  C CE2 . PHE A 155 ? 0.2060 0.2095 0.2917 0.0407  -0.0895 -0.0041 533  PHE A CE2 
980  C CZ  . PHE A 155 ? 0.2033 0.2034 0.2961 0.0434  -0.0872 -0.0005 533  PHE A CZ  
981  N N   . LYS A 156 ? 0.1662 0.1765 0.2931 0.0684  -0.0535 -0.0402 534  LYS A N   
982  C CA  . LYS A 156 ? 0.1739 0.1744 0.2988 0.0692  -0.0460 -0.0416 534  LYS A CA  
983  C C   . LYS A 156 ? 0.2153 0.2060 0.3242 0.0699  -0.0417 -0.0480 534  LYS A C   
984  O O   . LYS A 156 ? 0.2304 0.2092 0.3251 0.0714  -0.0484 -0.0485 534  LYS A O   
985  C CB  . LYS A 156 ? 0.1777 0.1659 0.3024 0.0698  -0.0535 -0.0334 534  LYS A CB  
986  C CG  . LYS A 156 ? 0.1962 0.1726 0.3173 0.0704  -0.0477 -0.0348 534  LYS A CG  
987  C CD  . LYS A 156 ? 0.2690 0.2550 0.4038 0.0699  -0.0373 -0.0366 534  LYS A CD  
988  C CE  . LYS A 156 ? 0.2672 0.2415 0.3993 0.0701  -0.0330 -0.0375 534  LYS A CE  
989  N NZ  . LYS A 156 ? 0.1981 0.1783 0.3415 0.0694  -0.0242 -0.0394 534  LYS A NZ  
990  N N   . TYR A 157 ? 0.1905 0.1859 0.3008 0.0687  -0.0313 -0.0522 535  TYR A N   
991  C CA  . TYR A 157 ? 0.2056 0.1961 0.3029 0.0690  -0.0265 -0.0569 535  TYR A CA  
992  C C   . TYR A 157 ? 0.2450 0.2253 0.3391 0.0692  -0.0233 -0.0572 535  TYR A C   
993  O O   . TYR A 157 ? 0.2285 0.2120 0.3326 0.0680  -0.0186 -0.0563 535  TYR A O   
994  C CB  . TYR A 157 ? 0.2262 0.2308 0.3268 0.0668  -0.0189 -0.0606 535  TYR A CB  
995  C CG  . TYR A 157 ? 0.2137 0.2276 0.3153 0.0669  -0.0226 -0.0617 535  TYR A CG  
996  C CD1 . TYR A 157 ? 0.1724 0.1982 0.2860 0.0652  -0.0242 -0.0609 535  TYR A CD1 
997  C CD2 . TYR A 157 ? 0.2095 0.2209 0.3006 0.0690  -0.0247 -0.0636 535  TYR A CD2 
998  C CE1 . TYR A 157 ? 0.1613 0.1973 0.2766 0.0651  -0.0280 -0.0625 535  TYR A CE1 
999  C CE2 . TYR A 157 ? 0.1808 0.2002 0.2736 0.0699  -0.0292 -0.0645 535  TYR A CE2 
1000 C CZ  . TYR A 157 ? 0.2091 0.2415 0.3141 0.0677  -0.0310 -0.0642 535  TYR A CZ  
1001 O OH  . TYR A 157 ? 0.2544 0.2972 0.3618 0.0683  -0.0359 -0.0653 535  TYR A OH  
1002 N N   . GLN A 158 ? 0.2496 0.2165 0.3293 0.0708  -0.0264 -0.0590 536  GLN A N   
1003 C CA  . GLN A 158 ? 0.2392 0.1961 0.3146 0.0708  -0.0243 -0.0608 536  GLN A CA  
1004 C C   . GLN A 158 ? 0.2613 0.2110 0.3189 0.0718  -0.0227 -0.0667 536  GLN A C   
1005 O O   . GLN A 158 ? 0.2812 0.2390 0.3351 0.0723  -0.0188 -0.0690 536  GLN A O   
1006 C CB  . GLN A 158 ? 0.2305 0.1736 0.3082 0.0713  -0.0337 -0.0550 536  GLN A CB  
1007 C CG  . GLN A 158 ? 0.2380 0.1721 0.3003 0.0685  -0.0431 -0.0496 536  GLN A CG  
1008 C CD  . GLN A 158 ? 0.2511 0.1721 0.2944 0.0604  -0.0472 -0.0430 536  GLN A CD  
1009 O OE1 . GLN A 158 ? 0.2282 0.1494 0.2753 0.0560  -0.0467 -0.0366 536  GLN A OE1 
1010 N NE2 . GLN A 158 ? 0.2291 0.1381 0.2512 0.0578  -0.0512 -0.0448 536  GLN A NE2 
1011 N N   . GLY A 159 ? 0.2752 0.2094 0.3216 0.0721  -0.0262 -0.0691 537  GLY A N   
1012 C CA  . GLY A 159 ? 0.2455 0.1729 0.2737 0.0727  -0.0243 -0.0755 537  GLY A CA  
1013 C C   . GLY A 159 ? 0.3015 0.2131 0.3140 0.0688  -0.0280 -0.0767 537  GLY A C   
1014 O O   . GLY A 159 ? 0.3565 0.2645 0.3683 0.0610  -0.0332 -0.0653 537  GLY A O   
1015 N N   . LEU A 160 ? 0.2586 0.1667 0.2573 0.0701  -0.0239 -0.0864 538  LEU A N   
1016 C CA  . LEU A 160 ? 0.3259 0.2255 0.3057 0.0612  -0.0245 -0.0857 538  LEU A CA  
1017 C C   . LEU A 160 ? 0.3336 0.2435 0.3159 0.0575  -0.0168 -0.0898 538  LEU A C   
1018 O O   . LEU A 160 ? 0.3380 0.2592 0.3290 0.0642  -0.0096 -0.0996 538  LEU A O   
1019 C CB  . LEU A 160 ? 0.3266 0.2141 0.2872 0.0645  -0.0253 -0.0951 538  LEU A CB  
1020 C CG  . LEU A 160 ? 0.3510 0.2211 0.2968 0.0603  -0.0341 -0.0893 538  LEU A CG  
1021 C CD1 . LEU A 160 ? 0.3123 0.1840 0.2708 0.0611  -0.0405 -0.0787 538  LEU A CD1 
1022 C CD2 . LEU A 160 ? 0.3660 0.2266 0.2997 0.0658  -0.0325 -0.0984 538  LEU A CD2 
1023 N N   . THR A 161 ? 0.3526 0.2599 0.3266 0.0458  -0.0186 -0.0817 539  THR A N   
1024 C CA  . THR A 161 ? 0.3706 0.2865 0.3435 0.0392  -0.0123 -0.0839 539  THR A CA  
1025 C C   . THR A 161 ? 0.3985 0.3089 0.3519 0.0258  -0.0158 -0.0778 539  THR A C   
1026 O O   . THR A 161 ? 0.3733 0.2738 0.3148 0.0221  -0.0226 -0.0728 539  THR A O   
1027 C CB  . THR A 161 ? 0.3323 0.2548 0.3256 0.0383  -0.0105 -0.0763 539  THR A CB  
1028 O OG1 . THR A 161 ? 0.4123 0.3433 0.4043 0.0327  -0.0032 -0.0810 539  THR A OG1 
1029 C CG2 . THR A 161 ? 0.3467 0.2624 0.3436 0.0310  -0.0185 -0.0587 539  THR A CG2 
1030 N N   . ILE A 162 ? 0.3660 0.2842 0.3152 0.0170  -0.0112 -0.0781 540  ILE A N   
1031 C CA  . ILE A 162 ? 0.4071 0.3245 0.3363 0.0027  -0.0131 -0.0743 540  ILE A CA  
1032 C C   . ILE A 162 ? 0.4107 0.3300 0.3455 -0.0086 -0.0164 -0.0574 540  ILE A C   
1033 O O   . ILE A 162 ? 0.3740 0.2990 0.3215 -0.0083 -0.0119 -0.0565 540  ILE A O   
1034 C CB  . ILE A 162 ? 0.4017 0.3288 0.3173 0.0008  -0.0047 -0.0908 540  ILE A CB  
1035 C CG1 . ILE A 162 ? 0.4501 0.3744 0.3634 0.0150  -0.0015 -0.1073 540  ILE A CG1 
1036 C CG2 . ILE A 162 ? 0.3549 0.2829 0.2485 -0.0153 -0.0065 -0.0880 540  ILE A CG2 
1037 C CD1 . ILE A 162 ? 0.4523 0.3896 0.3578 0.0171  0.0077  -0.1252 540  ILE A CD1 
1038 N N   . LEU A 163 ? 0.3971 0.3115 0.3222 -0.0190 -0.0245 -0.0437 541  LEU A N   
1039 C CA  . LEU A 163 ? 0.4105 0.3262 0.3388 -0.0305 -0.0293 -0.0256 541  LEU A CA  
1040 C C   . LEU A 163 ? 0.4434 0.3657 0.3494 -0.0471 -0.0283 -0.0253 541  LEU A C   
1041 O O   . LEU A 163 ? 0.4354 0.3579 0.3219 -0.0524 -0.0290 -0.0322 541  LEU A O   
1042 C CB  . LEU A 163 ? 0.4200 0.3298 0.3544 -0.0311 -0.0399 -0.0085 541  LEU A CB  
1043 C CG  . LEU A 163 ? 0.4374 0.3481 0.3795 -0.0399 -0.0463 0.0126  541  LEU A CG  
1044 C CD1 . LEU A 163 ? 0.4521 0.3596 0.4218 -0.0290 -0.0453 0.0177  541  LEU A CD1 
1045 C CD2 . LEU A 163 ? 0.3897 0.3001 0.3244 -0.0471 -0.0570 0.0278  541  LEU A CD2 
1046 N N   . VAL A 164 ? 0.4918 0.4194 0.4002 -0.0563 -0.0267 -0.0175 542  VAL A N   
1047 C CA  . VAL A 164 ? 0.5141 0.4511 0.4019 -0.0741 -0.0254 -0.0164 542  VAL A CA  
1048 C C   . VAL A 164 ? 0.4969 0.4331 0.3894 -0.0861 -0.0316 0.0058  542  VAL A C   
1049 O O   . VAL A 164 ? 0.4409 0.3691 0.3544 -0.0790 -0.0343 0.0166  542  VAL A O   
1050 C CB  . VAL A 164 ? 0.5410 0.4898 0.4223 -0.0745 -0.0140 -0.0358 542  VAL A CB  
1051 C CG1 . VAL A 164 ? 0.4871 0.4372 0.3610 -0.0635 -0.0087 -0.0573 542  VAL A CG1 
1052 C CG2 . VAL A 164 ? 0.5058 0.4547 0.4071 -0.0673 -0.0088 -0.0367 542  VAL A CG2 
1053 N N   . LYS A 165 ? 0.5311 0.4758 0.4037 -0.1048 -0.0339 0.0125  543  LYS A N   
1054 C CA  . LYS A 165 ? 0.5385 0.4834 0.4126 -0.1183 -0.0396 0.0339  543  LYS A CA  
1055 C C   . LYS A 165 ? 0.5474 0.4937 0.4287 -0.1196 -0.0319 0.0292  543  LYS A C   
1056 O O   . LYS A 165 ? 0.5692 0.5260 0.4421 -0.1202 -0.0221 0.0098  543  LYS A O   
1057 C CB  . LYS A 165 ? 0.5375 0.4941 0.3862 -0.1399 -0.0439 0.0414  543  LYS A CB  
1058 C CG  . LYS A 165 ? 0.5937 0.5520 0.4410 -0.1563 -0.0505 0.0647  543  LYS A CG  
1059 C CD  . LYS A 165 ? 0.6687 0.6158 0.5329 -0.1513 -0.0625 0.0894  543  LYS A CD  
1060 C CE  . LYS A 165 ? 0.7977 0.7536 0.6464 -0.1711 -0.0731 0.1112  543  LYS A CE  
1061 N NZ  . LYS A 165 ? 0.7516 0.7023 0.6134 -0.1645 -0.0848 0.1304  543  LYS A NZ  
1062 N N   . LYS A 166 ? 0.4788 0.4021 0.6510 -0.0729 0.0130  0.0632  544  LYS A N   
1063 C CA  . LYS A 166 ? 0.5053 0.4304 0.7109 -0.0860 0.0195  0.0669  544  LYS A CA  
1064 C C   . LYS A 166 ? 0.5106 0.4415 0.7090 -0.0940 0.0373  0.0849  544  LYS A C   
1065 O O   . LYS A 166 ? 0.5656 0.4818 0.7361 -0.0928 0.0412  0.1025  544  LYS A O   
1066 C CB  . LYS A 166 ? 0.5186 0.4173 0.7407 -0.0902 0.0096  0.0714  544  LYS A CB  
1067 C CG  . LYS A 166 ? 0.5137 0.4124 0.7756 -0.1041 0.0131  0.0700  544  LYS A CG  
1068 C CD  . LYS A 166 ? 0.5305 0.4059 0.8127 -0.1047 -0.0003 0.0637  544  LYS A CD  
1069 C CE  . LYS A 166 ? 0.5573 0.4212 0.8732 -0.1203 0.0042  0.0705  544  LYS A CE  
1070 N NZ  . LYS A 166 ? 0.7512 0.5853 1.0583 -0.1237 0.0065  0.0948  544  LYS A NZ  
1071 N N   . GLY A 167 ? 0.4935 0.4474 0.7173 -0.1018 0.0481  0.0806  545  GLY A N   
1072 C CA  . GLY A 167 ? 0.5106 0.4775 0.7311 -0.1085 0.0675  0.0951  545  GLY A CA  
1073 C C   . GLY A 167 ? 0.5501 0.5455 0.7606 -0.1010 0.0767  0.0857  545  GLY A C   
1074 O O   . GLY A 167 ? 0.6126 0.6296 0.8393 -0.1075 0.0924  0.0899  545  GLY A O   
1075 N N   . THR A 168 ? 0.5940 0.5901 0.7806 -0.0873 0.0677  0.0734  546  THR A N   
1076 C CA  . THR A 168 ? 0.5853 0.6059 0.7655 -0.0788 0.0744  0.0622  546  THR A CA  
1077 C C   . THR A 168 ? 0.5204 0.5654 0.7417 -0.0827 0.0731  0.0484  546  THR A C   
1078 O O   . THR A 168 ? 0.4781 0.5196 0.7175 -0.0829 0.0585  0.0364  546  THR A O   
1079 C CB  . THR A 168 ? 0.4985 0.5109 0.6487 -0.0647 0.0627  0.0515  546  THR A CB  
1080 O OG1 . THR A 168 ? 0.4196 0.4139 0.5301 -0.0609 0.0645  0.0636  546  THR A OG1 
1081 C CG2 . THR A 168 ? 0.5146 0.5501 0.6641 -0.0557 0.0676  0.0382  546  THR A CG2 
1082 N N   . ARG A 169 ? 0.4237 0.4946 0.6596 -0.0853 0.0884  0.0499  663  ARG A N   
1083 C CA  . ARG A 169 ? 0.4765 0.5743 0.7547 -0.0903 0.0878  0.0389  663  ARG A CA  
1084 C C   . ARG A 169 ? 0.4808 0.6016 0.7541 -0.0769 0.0894  0.0262  663  ARG A C   
1085 O O   . ARG A 169 ? 0.5146 0.6525 0.7827 -0.0734 0.1055  0.0305  663  ARG A O   
1086 C CB  . ARG A 169 ? 0.4858 0.5983 0.7934 -0.1049 0.1038  0.0512  663  ARG A CB  
1087 N N   . ILE A 170 ? 0.3847 0.5052 0.6593 -0.0690 0.0735  0.0110  664  ILE A N   
1088 C CA  . ILE A 170 ? 0.4164 0.5588 0.6937 -0.0571 0.0726  -0.0012 664  ILE A CA  
1089 C C   . ILE A 170 ? 0.4184 0.5730 0.7257 -0.0589 0.0576  -0.0148 664  ILE A C   
1090 O O   . ILE A 170 ? 0.3721 0.5098 0.6821 -0.0634 0.0446  -0.0187 664  ILE A O   
1091 C CB  . ILE A 170 ? 0.4245 0.5521 0.6622 -0.0424 0.0689  -0.0052 664  ILE A CB  
1092 C CG1 . ILE A 170 ? 0.3967 0.5013 0.6221 -0.0403 0.0511  -0.0109 664  ILE A CG1 
1093 C CG2 . ILE A 170 ? 0.4647 0.5799 0.6695 -0.0406 0.0822  0.0066  664  ILE A CG2 
1094 C CD1 . ILE A 170 ? 0.4609 0.5739 0.6881 -0.0297 0.0403  -0.0249 664  ILE A CD1 
1095 N N   . THR A 171 ? 0.3982 0.5830 0.7283 -0.0548 0.0595  -0.0223 665  THR A N   
1096 C CA  . THR A 171 ? 0.3807 0.5808 0.7397 -0.0569 0.0450  -0.0350 665  THR A CA  
1097 C C   . THR A 171 ? 0.4581 0.6454 0.7964 -0.0459 0.0295  -0.0455 665  THR A C   
1098 O O   . THR A 171 ? 0.4615 0.6429 0.8092 -0.0500 0.0158  -0.0538 665  THR A O   
1099 C CB  . THR A 171 ? 0.3467 0.5844 0.7354 -0.0541 0.0502  -0.0392 665  THR A CB  
1100 O OG1 . THR A 171 ? 0.2572 0.5019 0.6298 -0.0370 0.0466  -0.0459 665  THR A OG1 
1101 C CG2 . THR A 171 ? 0.3665 0.6174 0.7644 -0.0592 0.0712  -0.0269 665  THR A CG2 
1102 N N   . GLY A 172 ? 0.5512 0.7339 0.8619 -0.0321 0.0320  -0.0457 666  GLY A N   
1103 C CA  . GLY A 172 ? 0.4371 0.6088 0.7292 -0.0220 0.0192  -0.0539 666  GLY A CA  
1104 C C   . GLY A 172 ? 0.4547 0.6293 0.7270 -0.0072 0.0235  -0.0547 666  GLY A C   
1105 O O   . GLY A 172 ? 0.5142 0.6849 0.7716 -0.0042 0.0360  -0.0481 666  GLY A O   
1106 N N   . ILE A 173 ? 0.3626 0.5434 0.6340 0.0022  0.0132  -0.0628 667  ILE A N   
1107 C CA  . ILE A 173 ? 0.2915 0.4715 0.5452 0.0165  0.0160  -0.0635 667  ILE A CA  
1108 C C   . ILE A 173 ? 0.3101 0.5129 0.5780 0.0219  0.0280  -0.0616 667  ILE A C   
1109 O O   . ILE A 173 ? 0.3622 0.5606 0.6140 0.0332  0.0345  -0.0610 667  ILE A O   
1110 C CB  . ILE A 173 ? 0.3023 0.4850 0.5543 0.0247  0.0026  -0.0706 667  ILE A CB  
1111 C CG1 . ILE A 173 ? 0.3213 0.4927 0.5501 0.0380  0.0044  -0.0698 667  ILE A CG1 
1112 C CG2 . ILE A 173 ? 0.2121 0.4254 0.4935 0.0258  -0.0029 -0.0758 667  ILE A CG2 
1113 C CD1 . ILE A 173 ? 0.3017 0.4434 0.5017 0.0368  0.0062  -0.0665 667  ILE A CD1 
1114 N N   . ASN A 174 ? 0.2882 0.5153 0.5877 0.0142  0.0314  -0.0611 668  ASN A N   
1115 C CA  . ASN A 174 ? 0.2954 0.5494 0.6149 0.0192  0.0432  -0.0596 668  ASN A CA  
1116 C C   . ASN A 174 ? 0.2976 0.5543 0.6223 0.0097  0.0602  -0.0511 668  ASN A C   
1117 O O   . ASN A 174 ? 0.3152 0.5997 0.6678 0.0084  0.0701  -0.0494 668  ASN A O   
1118 C CB  . ASN A 174 ? 0.2427 0.5289 0.5989 0.0189  0.0341  -0.0655 668  ASN A CB  
1119 C CG  . ASN A 174 ? 0.2953 0.5817 0.6440 0.0305  0.0189  -0.0721 668  ASN A CG  
1120 O OD1 . ASN A 174 ? 0.3136 0.5823 0.6353 0.0420  0.0191  -0.0715 668  ASN A OD1 
1121 N ND2 . ASN A 174 ? 0.2868 0.5930 0.6589 0.0273  0.0054  -0.0784 668  ASN A ND2 
1122 N N   . ASP A 175 ? 0.3267 0.5558 0.6252 0.0032  0.0638  -0.0451 669  ASP A N   
1123 C CA  . ASP A 175 ? 0.3515 0.5811 0.6491 -0.0051 0.0808  -0.0350 669  ASP A CA  
1124 C C   . ASP A 175 ? 0.3062 0.5362 0.5822 0.0071  0.0961  -0.0333 669  ASP A C   
1125 O O   . ASP A 175 ? 0.3852 0.5973 0.6324 0.0184  0.0920  -0.0379 669  ASP A O   
1126 C CB  . ASP A 175 ? 0.3607 0.5606 0.6373 -0.0156 0.0780  -0.0279 669  ASP A CB  
1127 C CG  . ASP A 175 ? 0.3436 0.5448 0.6225 -0.0263 0.0945  -0.0152 669  ASP A CG  
1128 O OD1 . ASP A 175 ? 0.3559 0.5513 0.6087 -0.0208 0.1082  -0.0097 669  ASP A OD1 
1129 O OD2 . ASP A 175 ? 0.3277 0.5352 0.6339 -0.0404 0.0941  -0.0108 669  ASP A OD2 
1130 N N   . PRO A 176 ? 0.3055 0.5557 0.5956 0.0049  0.1144  -0.0275 670  PRO A N   
1131 C CA  . PRO A 176 ? 0.3356 0.5871 0.6047 0.0177  0.1305  -0.0278 670  PRO A CA  
1132 C C   . PRO A 176 ? 0.3445 0.5619 0.5646 0.0207  0.1322  -0.0255 670  PRO A C   
1133 O O   . PRO A 176 ? 0.3129 0.5226 0.5095 0.0342  0.1368  -0.0314 670  PRO A O   
1134 C CB  . PRO A 176 ? 0.2986 0.5773 0.5925 0.0107  0.1509  -0.0196 670  PRO A CB  
1135 C CG  . PRO A 176 ? 0.2813 0.5827 0.6213 -0.0013 0.1422  -0.0195 670  PRO A CG  
1136 C CD  . PRO A 176 ? 0.2691 0.5451 0.5990 -0.0086 0.1214  -0.0219 670  PRO A CD  
1137 N N   . ARG A 177 ? 0.3212 0.5177 0.5260 0.0087  0.1278  -0.0177 671  ARG A N   
1138 C CA  . ARG A 177 ? 0.3542 0.5196 0.5133 0.0114  0.1264  -0.0156 671  ARG A CA  
1139 C C   . ARG A 177 ? 0.3809 0.5272 0.5224 0.0208  0.1097  -0.0258 671  ARG A C   
1140 O O   . ARG A 177 ? 0.4952 0.6189 0.6004 0.0260  0.1084  -0.0274 671  ARG A O   
1141 C CB  . ARG A 177 ? 0.3591 0.5073 0.5099 -0.0029 0.1233  -0.0038 671  ARG A CB  
1142 C CG  . ARG A 177 ? 0.4036 0.5653 0.5650 -0.0130 0.1418  0.0093  671  ARG A CG  
1143 C CD  . ARG A 177 ? 0.3998 0.5482 0.5693 -0.0286 0.1355  0.0207  671  ARG A CD  
1144 N NE  . ARG A 177 ? 0.5159 0.6403 0.6467 -0.0312 0.1399  0.0326  671  ARG A NE  
1145 C CZ  . ARG A 177 ? 0.5473 0.6547 0.6772 -0.0428 0.1355  0.0450  671  ARG A CZ  
1146 N NH1 . ARG A 177 ? 0.4673 0.5772 0.6331 -0.0535 0.1269  0.0457  671  ARG A NH1 
1147 N NH2 . ARG A 177 ? 0.5853 0.6721 0.6769 -0.0431 0.1390  0.0565  671  ARG A NH2 
1148 N N   . LEU A 178 ? 0.2899 0.4453 0.4560 0.0227  0.0969  -0.0326 672  LEU A N   
1149 C CA  . LEU A 178 ? 0.3466 0.4873 0.5001 0.0316  0.0828  -0.0411 672  LEU A CA  
1150 C C   . LEU A 178 ? 0.3897 0.5431 0.5500 0.0463  0.0864  -0.0489 672  LEU A C   
1151 O O   . LEU A 178 ? 0.3874 0.5234 0.5250 0.0559  0.0830  -0.0543 672  LEU A O   
1152 C CB  . LEU A 178 ? 0.3469 0.4873 0.5187 0.0254  0.0660  -0.0430 672  LEU A CB  
1153 C CG  . LEU A 178 ? 0.3496 0.4659 0.5062 0.0168  0.0554  -0.0395 672  LEU A CG  
1154 C CD1 . LEU A 178 ? 0.3638 0.4750 0.5167 0.0055  0.0637  -0.0289 672  LEU A CD1 
1155 C CD2 . LEU A 178 ? 0.2631 0.3829 0.4400 0.0131  0.0407  -0.0441 672  LEU A CD2 
1156 N N   . ARG A 179 ? 0.3376 0.5212 0.5308 0.0481  0.0928  -0.0493 673  ARG A N   
1157 C CA  . ARG A 179 ? 0.3338 0.5313 0.5378 0.0632  0.0951  -0.0558 673  ARG A CA  
1158 C C   . ARG A 179 ? 0.3328 0.5300 0.5212 0.0732  0.1130  -0.0574 673  ARG A C   
1159 O O   . ARG A 179 ? 0.3686 0.5616 0.5507 0.0878  0.1138  -0.0640 673  ARG A O   
1160 C CB  . ARG A 179 ? 0.2651 0.4974 0.5125 0.0621  0.0931  -0.0561 673  ARG A CB  
1161 C CG  . ARG A 179 ? 0.2461 0.4793 0.5070 0.0557  0.0741  -0.0578 673  ARG A CG  
1162 C CD  . ARG A 179 ? 0.2864 0.5012 0.5288 0.0661  0.0615  -0.0626 673  ARG A CD  
1163 N NE  . ARG A 179 ? 0.3411 0.5587 0.5942 0.0615  0.0446  -0.0647 673  ARG A NE  
1164 C CZ  . ARG A 179 ? 0.3067 0.5219 0.5567 0.0708  0.0335  -0.0679 673  ARG A CZ  
1165 N NH1 . ARG A 179 ? 0.3559 0.5642 0.5949 0.0851  0.0366  -0.0689 673  ARG A NH1 
1166 N NH2 . ARG A 179 ? 0.3057 0.5244 0.5630 0.0660  0.0194  -0.0701 673  ARG A NH2 
1167 N N   . ASN A 180 ? 0.3584 0.5593 0.5398 0.0660  0.1280  -0.0513 674  ASN A N   
1168 C CA  . ASN A 180 ? 0.3411 0.5404 0.5017 0.0748  0.1466  -0.0531 674  ASN A CA  
1169 C C   . ASN A 180 ? 0.3619 0.5347 0.4823 0.0670  0.1491  -0.0483 674  ASN A C   
1170 O O   . ASN A 180 ? 0.4046 0.5850 0.5208 0.0595  0.1632  -0.0400 674  ASN A O   
1171 C CB  . ASN A 180 ? 0.3388 0.5735 0.5301 0.0751  0.1654  -0.0493 674  ASN A CB  
1172 C CG  . ASN A 180 ? 0.3659 0.6033 0.5407 0.0891  0.1850  -0.0544 674  ASN A CG  
1173 O OD1 . ASN A 180 ? 0.3791 0.5923 0.5231 0.1002  0.1827  -0.0629 674  ASN A OD1 
1174 N ND2 . ASN A 180 ? 0.3760 0.6431 0.5725 0.0884  0.2049  -0.0499 674  ASN A ND2 
1175 N N   . PRO A 181 ? 0.4276 0.5701 0.5183 0.0686  0.1354  -0.0526 675  PRO A N   
1176 C CA  . PRO A 181 ? 0.4405 0.5592 0.4970 0.0598  0.1326  -0.0471 675  PRO A CA  
1177 C C   . PRO A 181 ? 0.4652 0.5741 0.4849 0.0660  0.1473  -0.0493 675  PRO A C   
1178 O O   . PRO A 181 ? 0.4215 0.5343 0.4362 0.0791  0.1572  -0.0585 675  PRO A O   
1179 C CB  . PRO A 181 ? 0.4525 0.5465 0.4965 0.0605  0.1119  -0.0524 675  PRO A CB  
1180 C CG  . PRO A 181 ? 0.4531 0.5496 0.5055 0.0744  0.1106  -0.0630 675  PRO A CG  
1181 C CD  . PRO A 181 ? 0.4357 0.5650 0.5242 0.0785  0.1217  -0.0620 675  PRO A CD  
1182 N N   . SER A 182 ? 0.5123 0.6077 0.5050 0.0570  0.1482  -0.0406 676  SER A N   
1183 C CA  . SER A 182 ? 0.5776 0.6590 0.5264 0.0615  0.1583  -0.0424 676  SER A CA  
1184 C C   . SER A 182 ? 0.6151 0.6687 0.5324 0.0542  0.1422  -0.0383 676  SER A C   
1185 O O   . SER A 182 ? 0.6741 0.7189 0.6047 0.0484  0.1241  -0.0369 676  SER A O   
1186 C CB  . SER A 182 ? 0.5654 0.6670 0.5142 0.0586  0.1819  -0.0325 676  SER A CB  
1187 O OG  . SER A 182 ? 0.6720 0.7801 0.6375 0.0434  0.1809  -0.0165 676  SER A OG  
1188 N N   . ASP A 183 ? 0.6747 0.7155 0.5497 0.0552  0.1486  -0.0366 677  ASP A N   
1189 C CA  . ASP A 183 ? 0.6361 0.6530 0.4805 0.0486  0.1333  -0.0313 677  ASP A CA  
1190 C C   . ASP A 183 ? 0.5886 0.6091 0.4379 0.0358  0.1351  -0.0119 677  ASP A C   
1191 O O   . ASP A 183 ? 0.6573 0.6594 0.4852 0.0303  0.1218  -0.0050 677  ASP A O   
1192 C CB  . ASP A 183 ? 0.7963 0.7965 0.5897 0.0560  0.1364  -0.0391 677  ASP A CB  
1193 C CG  . ASP A 183 ? 0.9501 0.9290 0.7302 0.0623  0.1188  -0.0554 677  ASP A CG  
1194 O OD1 . ASP A 183 ? 0.8663 0.8457 0.6775 0.0624  0.1075  -0.0602 677  ASP A OD1 
1195 O OD2 . ASP A 183 ? 1.0298 0.9917 0.7682 0.0667  0.1163  -0.0634 677  ASP A OD2 
1196 N N   . LYS A 184 ? 0.6429 0.6865 0.5218 0.0307  0.1508  -0.0026 678  LYS A N   
1197 C CA  . LYS A 184 ? 0.7025 0.7485 0.5911 0.0175  0.1534  0.0164  678  LYS A CA  
1198 C C   . LYS A 184 ? 0.6338 0.6767 0.5573 0.0089  0.1357  0.0193  678  LYS A C   
1199 O O   . LYS A 184 ? 0.6336 0.6722 0.5645 -0.0020 0.1340  0.0341  678  LYS A O   
1200 C CB  . LYS A 184 ? 0.6672 0.7400 0.5767 0.0142  0.1780  0.0251  678  LYS A CB  
1201 C CG  . LYS A 184 ? 0.8190 0.8889 0.7058 0.0058  0.1910  0.0446  678  LYS A CG  
1202 C CD  . LYS A 184 ? 0.8934 0.9474 0.7215 0.0140  0.1952  0.0428  678  LYS A CD  
1203 C CE  . LYS A 184 ? 0.8807 0.9391 0.6858 0.0081  0.2152  0.0623  678  LYS A CE  
1204 N NZ  . LYS A 184 ? 0.9079 0.9525 0.6520 0.0170  0.2197  0.0592  678  LYS A NZ  
1205 N N   . PHE A 185 ? 0.5845 0.6287 0.5287 0.0139  0.1231  0.0059  679  PHE A N   
1206 C CA  . PHE A 185 ? 0.5505 0.5920 0.5249 0.0072  0.1065  0.0063  679  PHE A CA  
1207 C C   . PHE A 185 ? 0.4852 0.5140 0.4531 0.0150  0.0897  -0.0074 679  PHE A C   
1208 O O   . PHE A 185 ? 0.4910 0.5294 0.4711 0.0232  0.0910  -0.0188 679  PHE A O   
1209 C CB  . PHE A 185 ? 0.5040 0.5709 0.5247 0.0029  0.1128  0.0063  679  PHE A CB  
1210 C CG  . PHE A 185 ? 0.5318 0.5960 0.5813 -0.0058 0.0979  0.0080  679  PHE A CG  
1211 C CD1 . PHE A 185 ? 0.5011 0.5637 0.5638 -0.0012 0.0828  -0.0035 679  PHE A CD1 
1212 C CD2 . PHE A 185 ? 0.4629 0.5250 0.5256 -0.0183 0.0996  0.0212  679  PHE A CD2 
1213 C CE1 . PHE A 185 ? 0.4438 0.5042 0.5306 -0.0082 0.0700  -0.0034 679  PHE A CE1 
1214 C CE2 . PHE A 185 ? 0.4858 0.5438 0.5746 -0.0255 0.0860  0.0208  679  PHE A CE2 
1215 C CZ  . PHE A 185 ? 0.4043 0.4620 0.5042 -0.0201 0.0713  0.0077  679  PHE A CZ  
1216 N N   . ILE A 186 ? 0.5052 0.5129 0.4558 0.0125  0.0740  -0.0053 680  ILE A N   
1217 C CA  . ILE A 186 ? 0.5077 0.5022 0.4513 0.0182  0.0582  -0.0166 680  ILE A CA  
1218 C C   . ILE A 186 ? 0.4726 0.4699 0.4487 0.0140  0.0456  -0.0177 680  ILE A C   
1219 O O   . ILE A 186 ? 0.4523 0.4462 0.4394 0.0059  0.0404  -0.0087 680  ILE A O   
1220 C CB  . ILE A 186 ? 0.5146 0.4870 0.4215 0.0182  0.0480  -0.0145 680  ILE A CB  
1221 C CG1 . ILE A 186 ? 0.5650 0.5350 0.4357 0.0215  0.0612  -0.0122 680  ILE A CG1 
1222 C CG2 . ILE A 186 ? 0.5236 0.4842 0.4252 0.0236  0.0334  -0.0270 680  ILE A CG2 
1223 C CD1 . ILE A 186 ? 0.5957 0.5731 0.4604 0.0314  0.0729  -0.0253 680  ILE A CD1 
1224 N N   . TYR A 187 ? 0.4597 0.4623 0.4504 0.0202  0.0410  -0.0286 681  TYR A N   
1225 C CA  . TYR A 187 ? 0.4248 0.4290 0.4401 0.0181  0.0286  -0.0315 681  TYR A CA  
1226 C C   . TYR A 187 ? 0.4049 0.3990 0.4118 0.0250  0.0189  -0.0410 681  TYR A C   
1227 O O   . TYR A 187 ? 0.4563 0.4469 0.4478 0.0323  0.0235  -0.0474 681  TYR A O   
1228 C CB  . TYR A 187 ? 0.3353 0.3618 0.3845 0.0171  0.0337  -0.0331 681  TYR A CB  
1229 C CG  . TYR A 187 ? 0.3654 0.4064 0.4195 0.0261  0.0435  -0.0399 681  TYR A CG  
1230 C CD1 . TYR A 187 ? 0.4055 0.4590 0.4587 0.0270  0.0595  -0.0368 681  TYR A CD1 
1231 C CD2 . TYR A 187 ? 0.4000 0.4426 0.4609 0.0341  0.0373  -0.0484 681  TYR A CD2 
1232 C CE1 . TYR A 187 ? 0.4321 0.4998 0.4924 0.0366  0.0687  -0.0433 681  TYR A CE1 
1233 C CE2 . TYR A 187 ? 0.4047 0.4594 0.4716 0.0435  0.0456  -0.0537 681  TYR A CE2 
1234 C CZ  . TYR A 187 ? 0.4054 0.4728 0.4727 0.0452  0.0610  -0.0517 681  TYR A CZ  
1235 O OH  . TYR A 187 ? 0.4132 0.4936 0.4889 0.0561  0.0695  -0.0573 681  TYR A OH  
1236 N N   . ALA A 188 ? 0.4007 0.3895 0.4184 0.0227  0.0061  -0.0420 682  ALA A N   
1237 C CA  . ALA A 188 ? 0.4009 0.3798 0.4128 0.0274  -0.0032 -0.0490 682  ALA A CA  
1238 C C   . ALA A 188 ? 0.3320 0.3138 0.3651 0.0250  -0.0131 -0.0495 682  ALA A C   
1239 O O   . ALA A 188 ? 0.3190 0.3088 0.3695 0.0202  -0.0135 -0.0460 682  ALA A O   
1240 C CB  . ALA A 188 ? 0.4045 0.3647 0.3884 0.0268  -0.0094 -0.0489 682  ALA A CB  
1241 N N   . THR A 189 ? 0.3458 0.3207 0.3775 0.0283  -0.0205 -0.0544 683  THR A N   
1242 C CA  . THR A 189 ? 0.3676 0.3448 0.4158 0.0270  -0.0289 -0.0552 683  THR A CA  
1243 C C   . THR A 189 ? 0.3148 0.2777 0.3529 0.0263  -0.0384 -0.0562 683  THR A C   
1244 O O   . THR A 189 ? 0.2679 0.2191 0.2863 0.0255  -0.0402 -0.0558 683  THR A O   
1245 C CB  . THR A 189 ? 0.3314 0.3209 0.3943 0.0323  -0.0265 -0.0594 683  THR A CB  
1246 O OG1 . THR A 189 ? 0.2743 0.2677 0.3513 0.0310  -0.0332 -0.0601 683  THR A OG1 
1247 C CG2 . THR A 189 ? 0.3123 0.2943 0.3648 0.0386  -0.0250 -0.0632 683  THR A CG2 
1248 N N   . VAL A 190 ? 0.2935 0.2583 0.3450 0.0264  -0.0444 -0.0576 684  VAL A N   
1249 C CA  . VAL A 190 ? 0.3123 0.2671 0.3606 0.0249  -0.0533 -0.0583 684  VAL A CA  
1250 C C   . VAL A 190 ? 0.3257 0.2745 0.3681 0.0285  -0.0522 -0.0627 684  VAL A C   
1251 O O   . VAL A 190 ? 0.3222 0.2776 0.3721 0.0329  -0.0468 -0.0642 684  VAL A O   
1252 C CB  . VAL A 190 ? 0.2929 0.2540 0.3604 0.0235  -0.0587 -0.0573 684  VAL A CB  
1253 C CG1 . VAL A 190 ? 0.2862 0.2400 0.3546 0.0216  -0.0674 -0.0575 684  VAL A CG1 
1254 C CG2 . VAL A 190 ? 0.3110 0.2748 0.3854 0.0204  -0.0600 -0.0536 684  VAL A CG2 
1255 N N   . LYS A 191 ? 0.3184 0.2537 0.3474 0.0266  -0.0580 -0.0648 685  LYS A N   
1256 C CA  . LYS A 191 ? 0.3441 0.2699 0.3690 0.0287  -0.0582 -0.0697 685  LYS A CA  
1257 C C   . LYS A 191 ? 0.3208 0.2516 0.3651 0.0287  -0.0597 -0.0682 685  LYS A C   
1258 O O   . LYS A 191 ? 0.2552 0.1923 0.3125 0.0253  -0.0648 -0.0652 685  LYS A O   
1259 C CB  . LYS A 191 ? 0.2893 0.2001 0.2985 0.0251  -0.0668 -0.0735 685  LYS A CB  
1260 C CG  . LYS A 191 ? 0.3356 0.2379 0.3189 0.0268  -0.0637 -0.0770 685  LYS A CG  
1261 C CD  . LYS A 191 ? 0.3907 0.2774 0.3579 0.0235  -0.0741 -0.0830 685  LYS A CD  
1262 C CE  . LYS A 191 ? 0.5251 0.4033 0.4617 0.0256  -0.0713 -0.0873 685  LYS A CE  
1263 N NZ  . LYS A 191 ? 0.4020 0.2658 0.3209 0.0219  -0.0840 -0.0941 685  LYS A NZ  
1264 N N   . GLN A 192 ? 0.3304 0.2583 0.3763 0.0331  -0.0546 -0.0697 686  GLN A N   
1265 C CA  . GLN A 192 ? 0.3260 0.2557 0.3866 0.0330  -0.0549 -0.0669 686  GLN A CA  
1266 C C   . GLN A 192 ? 0.2448 0.1920 0.3202 0.0335  -0.0535 -0.0626 686  GLN A C   
1267 O O   . GLN A 192 ? 0.2554 0.2067 0.3431 0.0308  -0.0560 -0.0600 686  GLN A O   
1268 C CB  . GLN A 192 ? 0.2800 0.1986 0.3435 0.0266  -0.0631 -0.0682 686  GLN A CB  
1269 C CG  . GLN A 192 ? 0.3237 0.2228 0.3732 0.0265  -0.0647 -0.0744 686  GLN A CG  
1270 C CD  . GLN A 192 ? 0.4820 0.3709 0.5327 0.0186  -0.0756 -0.0777 686  GLN A CD  
1271 O OE1 . GLN A 192 ? 0.5245 0.4202 0.5929 0.0136  -0.0800 -0.0738 686  GLN A OE1 
1272 N NE2 . GLN A 192 ? 0.4663 0.3400 0.4985 0.0176  -0.0800 -0.0855 686  GLN A NE2 
1273 N N   . SER A 193 ? 0.2164 0.1746 0.2915 0.0367  -0.0492 -0.0625 687  SER A N   
1274 C CA  . SER A 193 ? 0.2817 0.2559 0.3690 0.0378  -0.0479 -0.0608 687  SER A CA  
1275 C C   . SER A 193 ? 0.2914 0.2749 0.3802 0.0446  -0.0421 -0.0601 687  SER A C   
1276 O O   . SER A 193 ? 0.2409 0.2187 0.3230 0.0490  -0.0385 -0.0603 687  SER A O   
1277 C CB  . SER A 193 ? 0.2701 0.2498 0.3589 0.0349  -0.0495 -0.0618 687  SER A CB  
1278 O OG  . SER A 193 ? 0.2465 0.2291 0.3292 0.0369  -0.0446 -0.0627 687  SER A OG  
1279 N N   . SER A 194 ? 0.2188 0.2170 0.3165 0.0462  -0.0417 -0.0596 688  SER A N   
1280 C CA  . SER A 194 ? 0.2403 0.2501 0.3393 0.0530  -0.0382 -0.0589 688  SER A CA  
1281 C C   . SER A 194 ? 0.1951 0.2105 0.2933 0.0547  -0.0358 -0.0614 688  SER A C   
1282 O O   . SER A 194 ? 0.2169 0.2380 0.3150 0.0613  -0.0328 -0.0605 688  SER A O   
1283 C CB  . SER A 194 ? 0.1874 0.2125 0.2936 0.0539  -0.0394 -0.0597 688  SER A CB  
1284 O OG  . SER A 194 ? 0.1688 0.2012 0.2809 0.0503  -0.0416 -0.0647 688  SER A OG  
1285 N N   . VAL A 195 ? 0.2162 0.2308 0.3150 0.0491  -0.0368 -0.0637 689  VAL A N   
1286 C CA  . VAL A 195 ? 0.2097 0.2301 0.3089 0.0495  -0.0328 -0.0650 689  VAL A CA  
1287 C C   . VAL A 195 ? 0.2840 0.2932 0.3718 0.0531  -0.0283 -0.0647 689  VAL A C   
1288 O O   . VAL A 195 ? 0.2859 0.3025 0.3751 0.0577  -0.0228 -0.0655 689  VAL A O   
1289 C CB  . VAL A 195 ? 0.2431 0.2629 0.3450 0.0420  -0.0342 -0.0655 689  VAL A CB  
1290 C CG1 . VAL A 195 ? 0.2744 0.3037 0.3804 0.0413  -0.0286 -0.0657 689  VAL A CG1 
1291 C CG2 . VAL A 195 ? 0.1745 0.2010 0.2874 0.0390  -0.0391 -0.0674 689  VAL A CG2 
1292 N N   . ASP A 196 ? 0.2819 0.2736 0.3592 0.0513  -0.0306 -0.0646 690  ASP A N   
1293 C CA  . ASP A 196 ? 0.2234 0.2018 0.2882 0.0549  -0.0270 -0.0666 690  ASP A CA  
1294 C C   . ASP A 196 ? 0.3149 0.2948 0.3833 0.0639  -0.0234 -0.0659 690  ASP A C   
1295 O O   . ASP A 196 ? 0.2364 0.2158 0.3013 0.0701  -0.0174 -0.0681 690  ASP A O   
1296 C CB  . ASP A 196 ? 0.3010 0.2607 0.3556 0.0501  -0.0325 -0.0678 690  ASP A CB  
1297 C CG  . ASP A 196 ? 0.3198 0.2637 0.3582 0.0526  -0.0298 -0.0724 690  ASP A CG  
1298 O OD1 . ASP A 196 ? 0.3519 0.3000 0.3864 0.0583  -0.0222 -0.0744 690  ASP A OD1 
1299 O OD2 . ASP A 196 ? 0.2758 0.2038 0.3061 0.0490  -0.0354 -0.0749 690  ASP A OD2 
1300 N N   . ILE A 197 ? 0.2653 0.2470 0.3405 0.0654  -0.0264 -0.0623 691  ILE A N   
1301 C CA  . ILE A 197 ? 0.3005 0.2837 0.3791 0.0746  -0.0236 -0.0593 691  ILE A CA  
1302 C C   . ILE A 197 ? 0.2671 0.2712 0.3542 0.0806  -0.0208 -0.0594 691  ILE A C   
1303 O O   . ILE A 197 ? 0.2655 0.2715 0.3547 0.0897  -0.0170 -0.0587 691  ILE A O   
1304 C CB  . ILE A 197 ? 0.3546 0.3377 0.4374 0.0747  -0.0266 -0.0534 691  ILE A CB  
1305 C CG1 . ILE A 197 ? 0.4041 0.3689 0.4834 0.0680  -0.0293 -0.0526 691  ILE A CG1 
1306 C CG2 . ILE A 197 ? 0.3203 0.3034 0.4048 0.0849  -0.0240 -0.0481 691  ILE A CG2 
1307 C CD1 . ILE A 197 ? 0.4085 0.3819 0.4945 0.0624  -0.0324 -0.0496 691  ILE A CD1 
1308 N N   . TYR A 198 ? 0.2576 0.2779 0.3519 0.0756  -0.0230 -0.0606 692  TYR A N   
1309 C CA  . TYR A 198 ? 0.2821 0.3248 0.3883 0.0795  -0.0222 -0.0613 692  TYR A CA  
1310 C C   . TYR A 198 ? 0.2854 0.3315 0.3935 0.0842  -0.0154 -0.0633 692  TYR A C   
1311 O O   . TYR A 198 ? 0.3225 0.3822 0.4399 0.0929  -0.0137 -0.0623 692  TYR A O   
1312 C CB  . TYR A 198 ? 0.2420 0.2967 0.3558 0.0711  -0.0258 -0.0641 692  TYR A CB  
1313 C CG  . TYR A 198 ? 0.2402 0.3181 0.3687 0.0725  -0.0258 -0.0663 692  TYR A CG  
1314 C CD1 . TYR A 198 ? 0.3038 0.3982 0.4396 0.0768  -0.0311 -0.0665 692  TYR A CD1 
1315 C CD2 . TYR A 198 ? 0.2132 0.2975 0.3485 0.0690  -0.0208 -0.0680 692  TYR A CD2 
1316 C CE1 . TYR A 198 ? 0.2693 0.3864 0.4206 0.0773  -0.0331 -0.0696 692  TYR A CE1 
1317 C CE2 . TYR A 198 ? 0.2535 0.3608 0.4064 0.0689  -0.0211 -0.0701 692  TYR A CE2 
1318 C CZ  . TYR A 198 ? 0.2565 0.3802 0.4183 0.0729  -0.0280 -0.0715 692  TYR A CZ  
1319 O OH  . TYR A 198 ? 0.3302 0.4782 0.5114 0.0722  -0.0301 -0.0745 692  TYR A OH  
1320 N N   . PHE A 199 ? 0.2485 0.2833 0.3477 0.0794  -0.0112 -0.0658 693  PHE A N   
1321 C CA  . PHE A 199 ? 0.3370 0.3753 0.4360 0.0841  -0.0026 -0.0681 693  PHE A CA  
1322 C C   . PHE A 199 ? 0.2579 0.2797 0.3473 0.0935  0.0013  -0.0697 693  PHE A C   
1323 O O   . PHE A 199 ? 0.3333 0.3601 0.4250 0.1009  0.0092  -0.0721 693  PHE A O   
1324 C CB  . PHE A 199 ? 0.2907 0.3243 0.3809 0.0756  0.0012  -0.0696 693  PHE A CB  
1325 C CG  . PHE A 199 ? 0.3290 0.3801 0.4329 0.0678  0.0004  -0.0680 693  PHE A CG  
1326 C CD1 . PHE A 199 ? 0.2720 0.3200 0.3772 0.0594  -0.0072 -0.0669 693  PHE A CD1 
1327 C CD2 . PHE A 199 ? 0.2913 0.3622 0.4093 0.0689  0.0075  -0.0680 693  PHE A CD2 
1328 C CE1 . PHE A 199 ? 0.2654 0.3264 0.3841 0.0521  -0.0082 -0.0663 693  PHE A CE1 
1329 C CE2 . PHE A 199 ? 0.3095 0.3952 0.4426 0.0603  0.0065  -0.0668 693  PHE A CE2 
1330 C CZ  . PHE A 199 ? 0.2927 0.3719 0.4255 0.0519  -0.0017 -0.0662 693  PHE A CZ  
1331 N N   . ARG A 200 ? 0.2724 0.2747 0.3528 0.0932  -0.0035 -0.0687 694  ARG A N   
1332 C CA  . ARG A 200 ? 0.3429 0.3259 0.4155 0.1013  -0.0005 -0.0707 694  ARG A CA  
1333 C C   . ARG A 200 ? 0.3598 0.3495 0.4442 0.1130  -0.0002 -0.0661 694  ARG A C   
1334 O O   . ARG A 200 ? 0.4139 0.3962 0.4982 0.1233  0.0052  -0.0683 694  ARG A O   
1335 C CB  . ARG A 200 ? 0.3367 0.2952 0.3975 0.0949  -0.0060 -0.0714 694  ARG A CB  
1336 C CG  . ARG A 200 ? 0.3807 0.3153 0.4338 0.1016  -0.0037 -0.0749 694  ARG A CG  
1337 C CD  . ARG A 200 ? 0.3670 0.2781 0.4080 0.0927  -0.0093 -0.0786 694  ARG A CD  
1338 N NE  . ARG A 200 ? 0.4660 0.3744 0.5147 0.0870  -0.0158 -0.0717 694  ARG A NE  
1339 C CZ  . ARG A 200 ? 0.4949 0.3884 0.5395 0.0779  -0.0219 -0.0730 694  ARG A CZ  
1340 N NH1 . ARG A 200 ? 0.4291 0.3080 0.4602 0.0732  -0.0243 -0.0815 694  ARG A NH1 
1341 N NH2 . ARG A 200 ? 0.5139 0.4085 0.5683 0.0734  -0.0258 -0.0658 694  ARG A NH2 
1342 N N   . ARG A 201 ? 0.2791 0.2825 0.3727 0.1125  -0.0060 -0.0599 695  ARG A N   
1343 C CA  . ARG A 201 ? 0.3100 0.3181 0.4114 0.1237  -0.0075 -0.0534 695  ARG A CA  
1344 C C   . ARG A 201 ? 0.2564 0.2899 0.3728 0.1330  -0.0052 -0.0535 695  ARG A C   
1345 O O   . ARG A 201 ? 0.3425 0.3777 0.4653 0.1454  -0.0051 -0.0490 695  ARG A O   
1346 C CB  . ARG A 201 ? 0.3388 0.3520 0.4406 0.1200  -0.0144 -0.0465 695  ARG A CB  
1347 C CG  . ARG A 201 ? 0.3444 0.3867 0.4561 0.1188  -0.0187 -0.0462 695  ARG A CG  
1348 C CD  . ARG A 201 ? 0.4132 0.4601 0.5218 0.1172  -0.0246 -0.0403 695  ARG A CD  
1349 N NE  . ARG A 201 ? 0.3251 0.3908 0.4380 0.1097  -0.0289 -0.0446 695  ARG A NE  
1350 C CZ  . ARG A 201 ? 0.3372 0.3969 0.4464 0.0988  -0.0297 -0.0484 695  ARG A CZ  
1351 N NH1 . ARG A 201 ? 0.3766 0.4147 0.4780 0.0936  -0.0274 -0.0480 695  ARG A NH1 
1352 N NH2 . ARG A 201 ? 0.3567 0.4324 0.4714 0.0932  -0.0335 -0.0530 695  ARG A NH2 
1353 N N   . GLN A 202 ? 0.2419 0.2954 0.3660 0.1273  -0.0037 -0.0577 696  GLN A N   
1354 C CA  . GLN A 202 ? 0.3194 0.4014 0.4624 0.1340  -0.0026 -0.0578 696  GLN A CA  
1355 C C   . GLN A 202 ? 0.3071 0.3898 0.4536 0.1394  0.0083  -0.0628 696  GLN A C   
1356 O O   . GLN A 202 ? 0.2466 0.3279 0.3879 0.1310  0.0141  -0.0673 696  GLN A O   
1357 C CB  . GLN A 202 ? 0.2817 0.3860 0.4344 0.1236  -0.0074 -0.0594 696  GLN A CB  
1358 C CG  . GLN A 202 ? 0.3218 0.4327 0.4739 0.1222  -0.0177 -0.0557 696  GLN A CG  
1359 C CD  . GLN A 202 ? 0.3404 0.4698 0.5013 0.1118  -0.0228 -0.0597 696  GLN A CD  
1360 O OE1 . GLN A 202 ? 0.3561 0.5106 0.5325 0.1142  -0.0278 -0.0608 696  GLN A OE1 
1361 N NE2 . GLN A 202 ? 0.3529 0.4696 0.5052 0.1002  -0.0224 -0.0624 696  GLN A NE2 
1362 N N   . VAL A 203 ? 0.2789 0.2781 0.3595 0.1123  -0.0128 -0.0636 697  VAL A N   
1363 C CA  . VAL A 203 ? 0.3333 0.3311 0.4117 0.1300  -0.0002 -0.0756 697  VAL A CA  
1364 C C   . VAL A 203 ? 0.2837 0.3147 0.3676 0.1318  0.0152  -0.0722 697  VAL A C   
1365 O O   . VAL A 203 ? 0.3619 0.3970 0.4348 0.1423  0.0282  -0.0824 697  VAL A O   
1366 C CB  . VAL A 203 ? 0.3408 0.3284 0.4418 0.1453  -0.0034 -0.0763 697  VAL A CB  
1367 C CG1 . VAL A 203 ? 0.4618 0.4129 0.5566 0.1420  -0.0188 -0.0792 697  VAL A CG1 
1368 C CG2 . VAL A 203 ? 0.3409 0.3574 0.4743 0.1443  -0.0054 -0.0590 697  VAL A CG2 
1369 N N   . GLU A 204 ? 0.3165 0.3727 0.4171 0.1207  0.0140  -0.0581 698  GLU A N   
1370 C CA  . GLU A 204 ? 0.3014 0.3886 0.4084 0.1189  0.0273  -0.0533 698  GLU A CA  
1371 C C   . GLU A 204 ? 0.3143 0.3979 0.3939 0.1121  0.0344  -0.0578 698  GLU A C   
1372 O O   . GLU A 204 ? 0.3193 0.4242 0.3991 0.1137  0.0478  -0.0561 698  GLU A O   
1373 C CB  . GLU A 204 ? 0.2758 0.3869 0.4044 0.1054  0.0221  -0.0388 698  GLU A CB  
1374 N N   . LEU A 205 ? 0.3530 0.4124 0.4103 0.1044  0.0255  -0.0617 699  LEU A N   
1375 C CA  . LEU A 205 ? 0.3560 0.4110 0.3873 0.0985  0.0299  -0.0642 699  LEU A CA  
1376 C C   . LEU A 205 ? 0.3906 0.4256 0.3960 0.1079  0.0314  -0.0787 699  LEU A C   
1377 O O   . LEU A 205 ? 0.4098 0.4375 0.3910 0.1023  0.0309  -0.0807 699  LEU A O   
1378 C CB  . LEU A 205 ? 0.2890 0.3351 0.3143 0.0830  0.0190  -0.0578 699  LEU A CB  
1379 C CG  . LEU A 205 ? 0.3154 0.3775 0.3622 0.0717  0.0155  -0.0466 699  LEU A CG  
1380 C CD1 . LEU A 205 ? 0.2780 0.3291 0.3165 0.0593  0.0053  -0.0439 699  LEU A CD1 
1381 C CD2 . LEU A 205 ? 0.3420 0.4276 0.3976 0.0683  0.0277  -0.0399 699  LEU A CD2 
1382 N N   . SER A 206 ? 0.3522 0.3783 0.3626 0.1223  0.0329  -0.0891 700  SER A N   
1383 C CA  . SER A 206 ? 0.4177 0.4206 0.4027 0.1304  0.0325  -0.1060 700  SER A CA  
1384 C C   . SER A 206 ? 0.4528 0.4688 0.4136 0.1334  0.0462  -0.1116 700  SER A C   
1385 O O   . SER A 206 ? 0.4556 0.4568 0.3872 0.1314  0.0432  -0.1211 700  SER A O   
1386 C CB  . SER A 206 ? 0.3742 0.3642 0.3724 0.1469  0.0330  -0.1169 700  SER A CB  
1387 O OG  . SER A 206 ? 0.4560 0.4725 0.4728 0.1597  0.0478  -0.1155 700  SER A OG  
1388 N N   . THR A 207 ? 0.3938 0.4399 0.3662 0.1371  0.0608  -0.1047 701  THR A N   
1389 C CA  . THR A 207 ? 0.4368 0.4998 0.3870 0.1385  0.0746  -0.1066 701  THR A CA  
1390 C C   . THR A 207 ? 0.4278 0.4868 0.3573 0.1230  0.0686  -0.0977 701  THR A C   
1391 O O   . THR A 207 ? 0.3922 0.4477 0.2915 0.1231  0.0708  -0.1040 701  THR A O   
1392 C CB  . THR A 207 ? 0.4357 0.5349 0.4069 0.1420  0.0904  -0.0967 701  THR A CB  
1393 O OG1 . THR A 207 ? 0.4496 0.5551 0.4431 0.1583  0.0958  -0.1043 701  THR A OG1 
1394 C CG2 . THR A 207 ? 0.4223 0.5416 0.3703 0.1430  0.1054  -0.0970 701  THR A CG2 
1395 N N   . MET A 208 ? 0.3804 0.4408 0.3258 0.1101  0.0609  -0.0830 702  MET A N   
1396 C CA  . MET A 208 ? 0.4129 0.4687 0.3431 0.0971  0.0553  -0.0738 702  MET A CA  
1397 C C   . MET A 208 ? 0.4606 0.4909 0.3698 0.0949  0.0415  -0.0825 702  MET A C   
1398 O O   . MET A 208 ? 0.4172 0.4453 0.3027 0.0903  0.0397  -0.0809 702  MET A O   
1399 C CB  . MET A 208 ? 0.3715 0.4329 0.3252 0.0852  0.0506  -0.0592 702  MET A CB  
1400 C CG  . MET A 208 ? 0.3846 0.4722 0.3586 0.0830  0.0627  -0.0487 702  MET A CG  
1401 S SD  . MET A 208 ? 0.4206 0.5103 0.4168 0.0668  0.0558  -0.0349 702  MET A SD  
1402 C CE  . MET A 208 ? 0.3508 0.4289 0.3241 0.0583  0.0538  -0.0274 702  MET A CE  
1403 N N   . TYR A 209 ? 0.4511 0.4631 0.3694 0.0972  0.0309  -0.0904 703  TYR A N   
1404 C CA  . TYR A 209 ? 0.4586 0.4476 0.3608 0.0923  0.0164  -0.0970 703  TYR A CA  
1405 C C   . TYR A 209 ? 0.4656 0.4465 0.3363 0.0978  0.0183  -0.1115 703  TYR A C   
1406 O O   . TYR A 209 ? 0.4897 0.4635 0.3396 0.0905  0.0098  -0.1119 703  TYR A O   
1407 C CB  . TYR A 209 ? 0.4653 0.4372 0.3853 0.0932  0.0055  -0.1010 703  TYR A CB  
1408 C CG  . TYR A 209 ? 0.4736 0.4209 0.3776 0.0887  -0.0089 -0.1099 703  TYR A CG  
1409 C CD1 . TYR A 209 ? 0.4562 0.4008 0.3562 0.0760  -0.0203 -0.1020 703  TYR A CD1 
1410 C CD2 . TYR A 209 ? 0.5225 0.4494 0.4165 0.0970  -0.0109 -0.1267 703  TYR A CD2 
1411 C CE1 . TYR A 209 ? 0.4894 0.4151 0.3768 0.0703  -0.0338 -0.1090 703  TYR A CE1 
1412 C CE2 . TYR A 209 ? 0.5007 0.4044 0.3809 0.0906  -0.0249 -0.1349 703  TYR A CE2 
1413 C CZ  . TYR A 209 ? 0.4704 0.3751 0.3476 0.0765  -0.0365 -0.1252 703  TYR A CZ  
1414 O OH  . TYR A 209 ? 0.5635 0.4485 0.4288 0.0686  -0.0509 -0.1322 703  TYR A OH  
1415 N N   . ARG A 210 ? 0.4392 0.4227 0.3060 0.1108  0.0292  -0.1241 704  ARG A N   
1416 C CA  . ARG A 210 ? 0.5634 0.5401 0.3978 0.1164  0.0319  -0.1411 704  ARG A CA  
1417 C C   . ARG A 210 ? 0.4665 0.4642 0.2770 0.1120  0.0397  -0.1336 704  ARG A C   
1418 O O   . ARG A 210 ? 0.4650 0.4584 0.2446 0.1112  0.0374  -0.1439 704  ARG A O   
1419 C CB  . ARG A 210 ? 0.4556 0.4311 0.2952 0.1318  0.0432  -0.1562 704  ARG A CB  
1420 C CG  . ARG A 210 ? 0.4661 0.4218 0.3330 0.1376  0.0360  -0.1602 704  ARG A CG  
1421 C CD  . ARG A 210 ? 0.6795 0.6322 0.5553 0.1503  0.0467  -0.1715 704  ARG A CD  
1422 N NE  . ARG A 210 ? 0.6305 0.6118 0.5307 0.1598  0.0611  -0.1629 704  ARG A NE  
1423 C CZ  . ARG A 210 ? 0.6381 0.6197 0.5707 0.1681  0.0608  -0.1587 704  ARG A CZ  
1424 N NH1 . ARG A 210 ? 0.5967 0.5502 0.5415 0.1684  0.0470  -0.1612 704  ARG A NH1 
1425 N NH2 . ARG A 210 ? 0.5674 0.5801 0.5220 0.1750  0.0741  -0.1499 704  ARG A NH2 
1426 N N   . HIS A 211 ? 0.4740 0.4941 0.2985 0.1079  0.0480  -0.1151 705  HIS A N   
1427 C CA  . HIS A 211 ? 0.5126 0.5501 0.3171 0.1017  0.0530  -0.1034 705  HIS A CA  
1428 C C   . HIS A 211 ? 0.5306 0.5574 0.3281 0.0897  0.0377  -0.0935 705  HIS A C   
1429 O O   . HIS A 211 ? 0.5757 0.6072 0.3466 0.0860  0.0353  -0.0910 705  HIS A O   
1430 C CB  . HIS A 211 ? 0.5637 0.6261 0.3875 0.1002  0.0666  -0.0862 705  HIS A CB  
1431 C CG  . HIS A 211 ? 0.5470 0.6243 0.3558 0.0920  0.0703  -0.0692 705  HIS A CG  
1432 N ND1 . HIS A 211 ? 0.5682 0.6682 0.3573 0.0952  0.0842  -0.0670 705  HIS A ND1 
1433 C CD2 . HIS A 211 ? 0.5123 0.5854 0.3241 0.0812  0.0620  -0.0525 705  HIS A CD2 
1434 C CE1 . HIS A 211 ? 0.5437 0.6519 0.3242 0.0859  0.0834  -0.0478 705  HIS A CE1 
1435 N NE2 . HIS A 211 ? 0.5517 0.6424 0.3465 0.0780  0.0700  -0.0393 705  HIS A NE2 
1436 N N   . MET A 212 ? 0.5128 0.5279 0.3340 0.0838  0.0274  -0.0874 706  MET A N   
1437 C CA  . MET A 212 ? 0.4984 0.5070 0.3174 0.0737  0.0144  -0.0773 706  MET A CA  
1438 C C   . MET A 212 ? 0.4915 0.4839 0.2915 0.0713  0.0001  -0.0893 706  MET A C   
1439 O O   . MET A 212 ? 0.5490 0.5430 0.3367 0.0646  -0.0087 -0.0822 706  MET A O   
1440 C CB  . MET A 212 ? 0.4701 0.4750 0.3198 0.0682  0.0093  -0.0680 706  MET A CB  
1441 C CG  . MET A 212 ? 0.4861 0.5058 0.3549 0.0664  0.0202  -0.0544 706  MET A CG  
1442 S SD  . MET A 212 ? 0.5290 0.5442 0.4302 0.0596  0.0133  -0.0483 706  MET A SD  
1443 C CE  . MET A 212 ? 0.4468 0.4723 0.3691 0.0658  0.0233  -0.0525 706  MET A CE  
1444 N N   . GLU A 213 ? 0.5499 0.5266 0.3492 0.0762  -0.0030 -0.1066 707  GLU A N   
1445 C CA  . GLU A 213 ? 0.5164 0.4748 0.3008 0.0715  -0.0181 -0.1182 707  GLU A CA  
1446 C C   . GLU A 213 ? 0.5681 0.5332 0.3179 0.0689  -0.0205 -0.1222 707  GLU A C   
1447 O O   . GLU A 213 ? 0.6758 0.6343 0.4147 0.0604  -0.0351 -0.1236 707  GLU A O   
1448 C CB  . GLU A 213 ? 0.6025 0.5403 0.3906 0.0785  -0.0192 -0.1370 707  GLU A CB  
1449 N N   . LYS A 214 ? 0.5655 0.5470 0.2982 0.0751  -0.0068 -0.1229 708  LYS A N   
1450 C CA  . LYS A 214 ? 0.6455 0.6374 0.3486 0.0701  -0.0079 -0.1226 708  LYS A CA  
1451 C C   . LYS A 214 ? 0.6587 0.6681 0.3551 0.0649  -0.0119 -0.1015 708  LYS A C   
1452 O O   . LYS A 214 ? 0.7299 0.7481 0.4057 0.0584  -0.0163 -0.0973 708  LYS A O   
1453 C CB  . LYS A 214 ? 0.6883 0.6927 0.3781 0.0770  0.0092  -0.1298 708  LYS A CB  
1454 N N   . HIS A 215 ? 0.6077 0.6202 0.3333 0.0631  -0.0097 -0.0837 709  HIS A N   
1455 C CA  . HIS A 215 ? 0.6126 0.6385 0.3402 0.0582  -0.0111 -0.0612 709  HIS A CA  
1456 C C   . HIS A 215 ? 0.5124 0.5308 0.2658 0.0528  -0.0217 -0.0503 709  HIS A C   
1457 O O   . HIS A 215 ? 0.5112 0.5379 0.2711 0.0504  -0.0224 -0.0318 709  HIS A O   
1458 C CB  . HIS A 215 ? 0.5870 0.6280 0.3223 0.0615  0.0058  -0.0476 709  HIS A CB  
1459 C CG  . HIS A 215 ? 0.6291 0.6824 0.3432 0.0678  0.0194  -0.0577 709  HIS A CG  
1460 N ND1 . HIS A 215 ? 0.6190 0.6717 0.3455 0.0752  0.0311  -0.0693 709  HIS A ND1 
1461 C CD2 . HIS A 215 ? 0.6481 0.7174 0.3293 0.0685  0.0235  -0.0578 709  HIS A CD2 
1462 C CE1 . HIS A 215 ? 0.6852 0.7530 0.3883 0.0810  0.0429  -0.0772 709  HIS A CE1 
1463 N NE2 . HIS A 215 ? 0.6723 0.7502 0.3470 0.0762  0.0387  -0.0706 709  HIS A NE2 
1464 N N   . ASN A 216 ? 0.5054 0.5089 0.2741 0.0511  -0.0297 -0.0606 710  ASN A N   
1465 C CA  . ASN A 216 ? 0.4727 0.4728 0.2656 0.0461  -0.0383 -0.0512 710  ASN A CA  
1466 C C   . ASN A 216 ? 0.4987 0.5061 0.2821 0.0412  -0.0506 -0.0420 710  ASN A C   
1467 O O   . ASN A 216 ? 0.4791 0.4884 0.2385 0.0387  -0.0587 -0.0490 710  ASN A O   
1468 C CB  . ASN A 216 ? 0.4390 0.4245 0.2465 0.0441  -0.0453 -0.0632 710  ASN A CB  
1469 C CG  . ASN A 216 ? 0.4625 0.4447 0.2915 0.0483  -0.0351 -0.0650 710  ASN A CG  
1470 O OD1 . ASN A 216 ? 0.3917 0.3831 0.2317 0.0502  -0.0246 -0.0550 710  ASN A OD1 
1471 N ND2 . ASN A 216 ? 0.4259 0.3951 0.2620 0.0491  -0.0388 -0.0767 710  ASN A ND2 
1472 N N   . TYR A 217 ? 0.4399 0.4522 0.2428 0.0401  -0.0521 -0.0269 711  TYR A N   
1473 C CA  . TYR A 217 ? 0.4261 0.4486 0.2254 0.0378  -0.0623 -0.0149 711  TYR A CA  
1474 C C   . TYR A 217 ? 0.4135 0.4347 0.2281 0.0328  -0.0751 -0.0176 711  TYR A C   
1475 O O   . TYR A 217 ? 0.3990 0.4120 0.2318 0.0312  -0.0745 -0.0242 711  TYR A O   
1476 C CB  . TYR A 217 ? 0.4049 0.4333 0.2169 0.0414  -0.0554 0.0044  711  TYR A CB  
1477 C CG  . TYR A 217 ? 0.4362 0.4721 0.2287 0.0440  -0.0464 0.0132  711  TYR A CG  
1478 C CD1 . TYR A 217 ? 0.4148 0.4485 0.2056 0.0460  -0.0324 0.0089  711  TYR A CD1 
1479 C CD2 . TYR A 217 ? 0.4581 0.5067 0.2346 0.0442  -0.0522 0.0273  711  TYR A CD2 
1480 C CE1 . TYR A 217 ? 0.3937 0.4380 0.1667 0.0475  -0.0233 0.0182  711  TYR A CE1 
1481 C CE2 . TYR A 217 ? 0.4745 0.5327 0.2320 0.0456  -0.0440 0.0374  711  TYR A CE2 
1482 C CZ  . TYR A 217 ? 0.4755 0.5316 0.2309 0.0469  -0.0291 0.0327  711  TYR A CZ  
1483 O OH  . TYR A 217 ? 0.6102 0.6794 0.3468 0.0474  -0.0202 0.0440  711  TYR A OH  
1484 N N   . GLU A 218 ? 0.3770 0.4098 0.1843 0.0300  -0.0871 -0.0110 712  GLU A N   
1485 C CA  . GLU A 218 ? 0.3896 0.4265 0.2104 0.0241  -0.0999 -0.0126 712  GLU A CA  
1486 C C   . GLU A 218 ? 0.3351 0.3765 0.1862 0.0271  -0.0970 -0.0026 712  GLU A C   
1487 O O   . GLU A 218 ? 0.3178 0.3607 0.1848 0.0226  -0.1026 -0.0064 712  GLU A O   
1488 C CB  . GLU A 218 ? 0.3945 0.4456 0.2035 0.0179  -0.1116 -0.0070 712  GLU A CB  
1489 C CG  . GLU A 218 ? 0.3822 0.4284 0.1648 0.0108  -0.1130 -0.0184 712  GLU A CG  
1490 C CD  . GLU A 218 ? 0.4681 0.5011 0.2542 0.0027  -0.1151 -0.0357 712  GLU A CD  
1491 O OE1 . GLU A 218 ? 0.5058 0.5393 0.3151 -0.0014 -0.1186 -0.0350 712  GLU A OE1 
1492 O OE2 . GLU A 218 ? 0.5218 0.5443 0.2880 0.0010  -0.1124 -0.0496 712  GLU A OE2 
1493 N N   . SER A 219 ? 0.3294 0.3726 0.1884 0.0341  -0.0882 0.0098  713  SER A N   
1494 C CA  . SER A 219 ? 0.2935 0.3389 0.1799 0.0379  -0.0848 0.0171  713  SER A CA  
1495 C C   . SER A 219 ? 0.3437 0.3791 0.2370 0.0433  -0.0711 0.0229  713  SER A C   
1496 O O   . SER A 219 ? 0.3636 0.3965 0.2409 0.0449  -0.0656 0.0279  713  SER A O   
1497 C CB  . SER A 219 ? 0.2811 0.3431 0.1757 0.0411  -0.0938 0.0299  713  SER A CB  
1498 O OG  . SER A 219 ? 0.3576 0.4236 0.2402 0.0462  -0.0932 0.0438  713  SER A OG  
1499 N N   . ALA A 220 ? 0.3145 0.3454 0.2313 0.0449  -0.0655 0.0221  714  ALA A N   
1500 C CA  . ALA A 220 ? 0.2766 0.2967 0.2026 0.0480  -0.0534 0.0270  714  ALA A CA  
1501 C C   . ALA A 220 ? 0.3640 0.3844 0.2890 0.0540  -0.0524 0.0442  714  ALA A C   
1502 O O   . ALA A 220 ? 0.4022 0.4152 0.3220 0.0544  -0.0441 0.0516  714  ALA A O   
1503 C CB  . ALA A 220 ? 0.2390 0.2552 0.1891 0.0476  -0.0494 0.0209  714  ALA A CB  
1504 N N   . ALA A 221 ? 0.2793 0.3097 0.2106 0.0586  -0.0609 0.0525  715  ALA A N   
1505 C CA  . ALA A 221 ? 0.3091 0.3400 0.2421 0.0656  -0.0613 0.0715  715  ALA A CA  
1506 C C   . ALA A 221 ? 0.3919 0.4278 0.2977 0.0635  -0.0623 0.0805  715  ALA A C   
1507 O O   . ALA A 221 ? 0.4239 0.4544 0.3278 0.0663  -0.0568 0.0959  715  ALA A O   
1508 C CB  . ALA A 221 ? 0.3008 0.3463 0.2466 0.0718  -0.0715 0.0786  715  ALA A CB  
1509 N N   . GLU A 222 ? 0.3477 0.3936 0.2316 0.0580  -0.0690 0.0711  716  GLU A N   
1510 C CA  . GLU A 222 ? 0.3562 0.4087 0.2107 0.0557  -0.0692 0.0761  716  GLU A CA  
1511 C C   . GLU A 222 ? 0.4252 0.4672 0.2729 0.0538  -0.0551 0.0728  716  GLU A C   
1512 O O   . GLU A 222 ? 0.4280 0.4738 0.2617 0.0544  -0.0500 0.0858  716  GLU A O   
1513 C CB  . GLU A 222 ? 0.3526 0.4155 0.1857 0.0498  -0.0798 0.0627  716  GLU A CB  
1514 N N   . ALA A 223 ? 0.4258 0.4576 0.2840 0.0512  -0.0488 0.0571  717  ALA A N   
1515 C CA  . ALA A 223 ? 0.4337 0.4590 0.2894 0.0495  -0.0354 0.0542  717  ALA A CA  
1516 C C   . ALA A 223 ? 0.4396 0.4573 0.3118 0.0509  -0.0269 0.0704  717  ALA A C   
1517 O O   . ALA A 223 ? 0.4366 0.4558 0.3001 0.0494  -0.0177 0.0790  717  ALA A O   
1518 C CB  . ALA A 223 ? 0.3432 0.3613 0.2099 0.0468  -0.0323 0.0357  717  ALA A CB  
1519 N N   . ILE A 224 ? 0.3633 0.3724 0.2595 0.0536  -0.0294 0.0744  718  ILE A N   
1520 C CA  . ILE A 224 ? 0.4161 0.4131 0.3292 0.0550  -0.0226 0.0890  718  ILE A CA  
1521 C C   . ILE A 224 ? 0.4649 0.4674 0.3653 0.0577  -0.0243 0.1116  718  ILE A C   
1522 O O   . ILE A 224 ? 0.4880 0.4849 0.3888 0.0552  -0.0160 0.1254  718  ILE A O   
1523 C CB  . ILE A 224 ? 0.4101 0.3969 0.3501 0.0591  -0.0257 0.0861  718  ILE A CB  
1524 C CG1 . ILE A 224 ? 0.3835 0.3660 0.3357 0.0546  -0.0223 0.0662  718  ILE A CG1 
1525 C CG2 . ILE A 224 ? 0.3837 0.3545 0.3405 0.0620  -0.0207 0.1023  718  ILE A CG2 
1526 C CD1 . ILE A 224 ? 0.3344 0.3148 0.3066 0.0585  -0.0266 0.0588  718  ILE A CD1 
1527 N N   . GLN A 225 ? 0.4677 0.4832 0.3570 0.0618  -0.0356 0.1172  719  GLN A N   
1528 C CA  . GLN A 225 ? 0.4809 0.5061 0.3550 0.0640  -0.0390 0.1397  719  GLN A CA  
1529 C C   . GLN A 225 ? 0.5114 0.5472 0.3572 0.0582  -0.0320 0.1411  719  GLN A C   
1530 O O   . GLN A 225 ? 0.5674 0.6071 0.4050 0.0574  -0.0280 0.1620  719  GLN A O   
1531 C CB  . GLN A 225 ? 0.4010 0.4430 0.2674 0.0681  -0.0539 0.1431  719  GLN A CB  
1532 C CG  . GLN A 225 ? 0.4590 0.5145 0.3111 0.0708  -0.0598 0.1686  719  GLN A CG  
1533 C CD  . GLN A 225 ? 0.5444 0.5857 0.4203 0.0774  -0.0569 0.1920  719  GLN A CD  
1534 O OE1 . GLN A 225 ? 0.5784 0.6071 0.4832 0.0842  -0.0584 0.1906  719  GLN A OE1 
1535 N NE2 . GLN A 225 ? 0.4834 0.5264 0.3474 0.0753  -0.0526 0.2139  719  GLN A NE2 
1536 N N   . ALA A 226 ? 0.5119 0.5531 0.3431 0.0544  -0.0299 0.1195  720  ALA A N   
1537 C CA  . ALA A 226 ? 0.5311 0.5837 0.3359 0.0506  -0.0217 0.1174  720  ALA A CA  
1538 C C   . ALA A 226 ? 0.5597 0.6059 0.3759 0.0474  -0.0067 0.1251  720  ALA A C   
1539 O O   . ALA A 226 ? 0.5886 0.6475 0.3865 0.0447  0.0012  0.1349  720  ALA A O   
1540 C CB  . ALA A 226 ? 0.5015 0.5574 0.2924 0.0491  -0.0229 0.0909  720  ALA A CB  
1541 N N   . VAL A 227 ? 0.5075 0.5362 0.3530 0.0465  -0.0027 0.1208  721  VAL A N   
1542 C CA  . VAL A 227 ? 0.5650 0.5874 0.4240 0.0415  0.0100  0.1293  721  VAL A CA  
1543 C C   . VAL A 227 ? 0.6222 0.6388 0.4872 0.0409  0.0105  0.1574  721  VAL A C   
1544 O O   . VAL A 227 ? 0.6151 0.6360 0.4773 0.0353  0.0202  0.1722  721  VAL A O   
1545 C CB  . VAL A 227 ? 0.5030 0.5094 0.3900 0.0393  0.0128  0.1147  721  VAL A CB  
1546 C CG1 . VAL A 227 ? 0.5285 0.5303 0.4299 0.0319  0.0250  0.1226  721  VAL A CG1 
1547 C CG2 . VAL A 227 ? 0.4604 0.4726 0.3422 0.0401  0.0112  0.0901  721  VAL A CG2 
1548 N N   . ARG A 228 ? 0.6250 0.6328 0.4997 0.0468  0.0000  0.1665  722  ARG A N   
1549 C CA  . ARG A 228 ? 0.6233 0.6237 0.5052 0.0482  -0.0011 0.1951  722  ARG A CA  
1550 C C   . ARG A 228 ? 0.6033 0.6260 0.4556 0.0461  -0.0006 0.2142  722  ARG A C   
1551 O O   . ARG A 228 ? 0.6093 0.6305 0.4627 0.0417  0.0055  0.2378  722  ARG A O   
1552 C CB  . ARG A 228 ? 0.5285 0.5194 0.4265 0.0577  -0.0130 0.1998  722  ARG A CB  
1553 C CG  . ARG A 228 ? 0.5706 0.5416 0.4972 0.0604  -0.0130 0.1815  722  ARG A CG  
1554 C CD  . ARG A 228 ? 0.6059 0.5510 0.5605 0.0637  -0.0114 0.1964  722  ARG A CD  
1555 N NE  . ARG A 228 ? 0.5423 0.4865 0.5067 0.0757  -0.0219 0.2079  722  ARG A NE  
1556 C CZ  . ARG A 228 ? 0.5914 0.5130 0.5808 0.0825  -0.0225 0.2217  722  ARG A CZ  
1557 N NH1 . ARG A 228 ? 0.4888 0.3840 0.4950 0.0769  -0.0138 0.2254  722  ARG A NH1 
1558 N NH2 . ARG A 228 ? 0.6710 0.5964 0.6701 0.0953  -0.0322 0.2318  722  ARG A NH2 
1559 N N   . ASP A 229 ? 0.6167 0.6607 0.4413 0.0481  -0.0071 0.2044  723  ASP A N   
1560 C CA  . ASP A 229 ? 0.6558 0.7246 0.4478 0.0462  -0.0079 0.2196  723  ASP A CA  
1561 C C   . ASP A 229 ? 0.6657 0.7504 0.4361 0.0400  0.0055  0.2102  723  ASP A C   
1562 O O   . ASP A 229 ? 0.6801 0.7859 0.4222 0.0374  0.0059  0.2126  723  ASP A O   
1563 C CB  . ASP A 229 ? 0.7155 0.7989 0.4886 0.0501  -0.0226 0.2107  723  ASP A CB  
1564 C CG  . ASP A 229 ? 0.6096 0.6817 0.4069 0.0570  -0.0353 0.2178  723  ASP A CG  
1565 O OD1 . ASP A 229 ? 0.7335 0.7868 0.5582 0.0602  -0.0329 0.2339  723  ASP A OD1 
1566 O OD2 . ASP A 229 ? 0.5569 0.6383 0.3474 0.0589  -0.0473 0.2062  723  ASP A OD2 
1567 N N   . ASN A 230 ? 0.8393 0.9135 0.6267 0.0369  0.0163  0.1949  724  ASN A N   
1568 C CA  . ASN A 230 ? 0.8687 0.9592 0.6420 0.0325  0.0305  0.1864  724  ASN A CA  
1569 C C   . ASN A 230 ? 0.8713 0.9810 0.6117 0.0358  0.0286  0.1652  724  ASN A C   
1570 O O   . ASN A 230 ? 0.8954 1.0276 0.6107 0.0340  0.0379  0.1655  724  ASN A O   
1571 C CB  . ASN A 230 ? 0.8491 0.9526 0.6163 0.0259  0.0405  0.2147  724  ASN A CB  
1572 C CG  . ASN A 230 ? 1.0609 1.1761 0.8313 0.0203  0.0576  0.2085  724  ASN A CG  
1573 O OD1 . ASN A 230 ? 1.1401 1.2796 0.8854 0.0214  0.0653  0.1972  724  ASN A OD1 
1574 N ND2 . ASN A 230 ? 1.0972 1.1960 0.8993 0.0143  0.0635  0.2151  724  ASN A ND2 
1575 N N   . LYS A 231 ? 0.7598 0.8607 0.5003 0.0402  0.0165  0.1461  725  LYS A N   
1576 C CA  . LYS A 231 ? 0.6114 0.7221 0.3270 0.0425  0.0145  0.1205  725  LYS A CA  
1577 C C   . LYS A 231 ? 0.6217 0.7201 0.3540 0.0441  0.0199  0.0954  725  LYS A C   
1578 O O   . LYS A 231 ? 0.5924 0.6981 0.3069 0.0464  0.0238  0.0748  725  LYS A O   
1579 C CB  . LYS A 231 ? 0.5768 0.6875 0.2803 0.0444  -0.0034 0.1160  725  LYS A CB  
1580 N N   . LEU A 232 ? 0.6026 0.6828 0.3686 0.0433  0.0201  0.0966  726  LEU A N   
1581 C CA  . LEU A 232 ? 0.5460 0.6166 0.3313 0.0438  0.0251  0.0773  726  LEU A CA  
1582 C C   . LEU A 232 ? 0.5388 0.6055 0.3496 0.0393  0.0361  0.0894  726  LEU A C   
1583 O O   . LEU A 232 ? 0.5257 0.5818 0.3524 0.0365  0.0335  0.1068  726  LEU A O   
1584 C CB  . LEU A 232 ? 0.5330 0.5872 0.3336 0.0454  0.0124  0.0646  726  LEU A CB  
1585 C CG  . LEU A 232 ? 0.4673 0.5115 0.2897 0.0454  0.0151  0.0474  726  LEU A CG  
1586 C CD1 . LEU A 232 ? 0.4401 0.4911 0.2470 0.0486  0.0197  0.0284  726  LEU A CD1 
1587 C CD2 . LEU A 232 ? 0.4859 0.5170 0.3237 0.0455  0.0027  0.0408  726  LEU A CD2 
1588 N N   . HIS A 233 ? 0.5062 0.5813 0.3221 0.0387  0.0479  0.0803  727  HIS A N   
1589 C CA  . HIS A 233 ? 0.4995 0.5761 0.3377 0.0323  0.0588  0.0926  727  HIS A CA  
1590 C C   . HIS A 233 ? 0.4600 0.5212 0.3296 0.0296  0.0570  0.0830  727  HIS A C   
1591 O O   . HIS A 233 ? 0.5293 0.5874 0.4200 0.0223  0.0630  0.0935  727  HIS A O   
1592 C CB  . HIS A 233 ? 0.4679 0.5691 0.2959 0.0323  0.0740  0.0913  727  HIS A CB  
1593 C CG  . HIS A 233 ? 0.5471 0.6675 0.3409 0.0345  0.0773  0.0988  727  HIS A CG  
1594 N ND1 . HIS A 233 ? 0.5815 0.7217 0.3529 0.0404  0.0855  0.0838  727  HIS A ND1 
1595 C CD2 . HIS A 233 ? 0.5851 0.7091 0.3627 0.0318  0.0733  0.1195  727  HIS A CD2 
1596 C CE1 . HIS A 233 ? 0.6132 0.7697 0.3539 0.0403  0.0867  0.0937  727  HIS A CE1 
1597 N NE2 . HIS A 233 ? 0.6168 0.7647 0.3607 0.0348  0.0789  0.1168  727  HIS A NE2 
1598 N N   . ALA A 234 ? 0.4625 0.5148 0.3353 0.0340  0.0484  0.0642  728  ALA A N   
1599 C CA  . ALA A 234 ? 0.4211 0.4616 0.3211 0.0311  0.0457  0.0555  728  ALA A CA  
1600 C C   . ALA A 234 ? 0.3967 0.4268 0.2947 0.0355  0.0330  0.0411  728  ALA A C   
1601 O O   . ALA A 234 ? 0.3830 0.4175 0.2633 0.0407  0.0297  0.0295  728  ALA A O   
1602 C CB  . ALA A 234 ? 0.3907 0.4436 0.3030 0.0298  0.0554  0.0471  728  ALA A CB  
1603 N N   . PHE A 235 ? 0.3638 0.3803 0.2799 0.0330  0.0263  0.0413  729  PHE A N   
1604 C CA  . PHE A 235 ? 0.3292 0.3387 0.2467 0.0357  0.0147  0.0298  729  PHE A CA  
1605 C C   . PHE A 235 ? 0.3263 0.3324 0.2661 0.0321  0.0145  0.0196  729  PHE A C   
1606 O O   . PHE A 235 ? 0.3372 0.3371 0.2951 0.0272  0.0170  0.0239  729  PHE A O   
1607 C CB  . PHE A 235 ? 0.3714 0.3730 0.2896 0.0374  0.0067  0.0393  729  PHE A CB  
1608 C CG  . PHE A 235 ? 0.3471 0.3466 0.2665 0.0397  -0.0049 0.0294  729  PHE A CG  
1609 C CD1 . PHE A 235 ? 0.3267 0.3306 0.2352 0.0405  -0.0097 0.0161  729  PHE A CD1 
1610 C CD2 . PHE A 235 ? 0.3540 0.3473 0.2868 0.0411  -0.0106 0.0336  729  PHE A CD2 
1611 C CE1 . PHE A 235 ? 0.3717 0.3749 0.2825 0.0406  -0.0206 0.0089  729  PHE A CE1 
1612 C CE2 . PHE A 235 ? 0.2906 0.2865 0.2257 0.0425  -0.0205 0.0257  729  PHE A CE2 
1613 C CZ  . PHE A 235 ? 0.3813 0.3827 0.3054 0.0412  -0.0258 0.0142  729  PHE A CZ  
1614 N N   . ILE A 236 ? 0.3270 0.3364 0.2651 0.0340  0.0110  0.0064  730  ILE A N   
1615 C CA  . ILE A 236 ? 0.3459 0.3553 0.3030 0.0305  0.0091  -0.0023 730  ILE A CA  
1616 C C   . ILE A 236 ? 0.3358 0.3396 0.2955 0.0304  -0.0020 -0.0073 730  ILE A C   
1617 O O   . ILE A 236 ? 0.3168 0.3201 0.2641 0.0334  -0.0094 -0.0123 730  ILE A O   
1618 C CB  . ILE A 236 ? 0.2899 0.3071 0.2467 0.0332  0.0120  -0.0112 730  ILE A CB  
1619 C CG1 . ILE A 236 ? 0.3008 0.3287 0.2557 0.0342  0.0244  -0.0059 730  ILE A CG1 
1620 C CG2 . ILE A 236 ? 0.2888 0.3086 0.2656 0.0292  0.0088  -0.0172 730  ILE A CG2 
1621 C CD1 . ILE A 236 ? 0.2875 0.3251 0.2449 0.0393  0.0288  -0.0145 730  ILE A CD1 
1622 N N   . TRP A 237 ? 0.2972 0.2976 0.2729 0.0264  -0.0031 -0.0065 731  TRP A N   
1623 C CA  . TRP A 237 ? 0.2472 0.2458 0.2264 0.0269  -0.0118 -0.0097 731  TRP A CA  
1624 C C   . TRP A 237 ? 0.2658 0.2644 0.2639 0.0217  -0.0105 -0.0140 731  TRP A C   
1625 O O   . TRP A 237 ? 0.3014 0.3004 0.3091 0.0169  -0.0042 -0.0147 731  TRP A O   
1626 C CB  . TRP A 237 ? 0.2731 0.2675 0.2443 0.0316  -0.0147 -0.0008 731  TRP A CB  
1627 C CG  . TRP A 237 ? 0.2851 0.2831 0.2577 0.0335  -0.0242 -0.0031 731  TRP A CG  
1628 C CD1 . TRP A 237 ? 0.2604 0.2569 0.2423 0.0368  -0.0261 0.0013  731  TRP A CD1 
1629 C CD2 . TRP A 237 ? 0.2851 0.2897 0.2517 0.0322  -0.0330 -0.0099 731  TRP A CD2 
1630 N NE1 . TRP A 237 ? 0.2692 0.2751 0.2515 0.0377  -0.0349 -0.0020 731  TRP A NE1 
1631 C CE2 . TRP A 237 ? 0.2808 0.2911 0.2534 0.0337  -0.0397 -0.0083 731  TRP A CE2 
1632 C CE3 . TRP A 237 ? 0.2601 0.2655 0.2180 0.0301  -0.0357 -0.0168 731  TRP A CE3 
1633 C CZ2 . TRP A 237 ? 0.2551 0.2741 0.2253 0.0311  -0.0493 -0.0123 731  TRP A CZ2 
1634 C CZ3 . TRP A 237 ? 0.2692 0.2785 0.2244 0.0277  -0.0458 -0.0211 731  TRP A CZ3 
1635 C CH2 . TRP A 237 ? 0.2584 0.2753 0.2195 0.0272  -0.0526 -0.0183 731  TRP A CH2 
1636 N N   . ASP A 238 ? 0.2463 0.2465 0.2494 0.0223  -0.0165 -0.0176 732  ASP A N   
1637 C CA  . ASP A 238 ? 0.2194 0.2215 0.2376 0.0178  -0.0154 -0.0243 732  ASP A CA  
1638 C C   . ASP A 238 ? 0.2806 0.2707 0.3079 0.0168  -0.0082 -0.0216 732  ASP A C   
1639 O O   . ASP A 238 ? 0.2783 0.2583 0.3028 0.0220  -0.0067 -0.0128 732  ASP A O   
1640 C CB  . ASP A 238 ? 0.2228 0.2319 0.2436 0.0200  -0.0219 -0.0280 732  ASP A CB  
1641 C CG  . ASP A 238 ? 0.2333 0.2539 0.2485 0.0176  -0.0296 -0.0307 732  ASP A CG  
1642 O OD1 . ASP A 238 ? 0.1665 0.1916 0.1836 0.0126  -0.0297 -0.0341 732  ASP A OD1 
1643 O OD2 . ASP A 238 ? 0.1987 0.2240 0.2091 0.0204  -0.0362 -0.0285 732  ASP A OD2 
1644 N N   . SER A 239 ? 0.2270 0.2178 0.2656 0.0093  -0.0047 -0.0285 733  SER A N   
1645 C CA  . SER A 239 ? 0.2557 0.2321 0.3039 0.0059  0.0016  -0.0271 733  SER A CA  
1646 C C   . SER A 239 ? 0.2568 0.2218 0.3121 0.0111  0.0013  -0.0303 733  SER A C   
1647 O O   . SER A 239 ? 0.2284 0.1754 0.2888 0.0132  0.0052  -0.0239 733  SER A O   
1648 C CB  . SER A 239 ? 0.2599 0.2420 0.3180 -0.0053 0.0042  -0.0349 733  SER A CB  
1649 O OG  . SER A 239 ? 0.2100 0.2041 0.2713 -0.0084 -0.0001 -0.0468 733  SER A OG  
1650 N N   . ALA A 240 ? 0.2357 0.2112 0.2924 0.0137  -0.0030 -0.0394 734  ALA A N   
1651 C CA  . ALA A 240 ? 0.2287 0.1965 0.2935 0.0210  -0.0023 -0.0435 734  ALA A CA  
1652 C C   . ALA A 240 ? 0.2703 0.2310 0.3320 0.0321  -0.0042 -0.0301 734  ALA A C   
1653 O O   . ALA A 240 ? 0.3112 0.2591 0.3824 0.0398  -0.0022 -0.0288 734  ALA A O   
1654 C CB  . ALA A 240 ? 0.2267 0.2137 0.2932 0.0213  -0.0057 -0.0551 734  ALA A CB  
1655 N N   . VAL A 241 ? 0.2138 0.1826 0.2623 0.0334  -0.0083 -0.0203 735  VAL A N   
1656 C CA  . VAL A 241 ? 0.2881 0.2536 0.3309 0.0424  -0.0113 -0.0065 735  VAL A CA  
1657 C C   . VAL A 241 ? 0.3206 0.2702 0.3606 0.0415  -0.0063 0.0063  735  VAL A C   
1658 O O   . VAL A 241 ? 0.3268 0.2641 0.3720 0.0483  -0.0057 0.0171  735  VAL A O   
1659 C CB  . VAL A 241 ? 0.2534 0.2359 0.2814 0.0429  -0.0189 -0.0038 735  VAL A CB  
1660 C CG1 . VAL A 241 ? 0.2486 0.2295 0.2664 0.0495  -0.0223 0.0110  735  VAL A CG1 
1661 C CG2 . VAL A 241 ? 0.2416 0.2403 0.2745 0.0440  -0.0246 -0.0121 735  VAL A CG2 
1662 N N   . LEU A 242 ? 0.2865 0.2375 0.3198 0.0333  -0.0026 0.0066  736  LEU A N   
1663 C CA  . LEU A 242 ? 0.3181 0.2594 0.3475 0.0313  0.0026  0.0204  736  LEU A CA  
1664 C C   . LEU A 242 ? 0.4025 0.3227 0.4482 0.0283  0.0081  0.0230  736  LEU A C   
1665 O O   . LEU A 242 ? 0.4564 0.3638 0.5029 0.0305  0.0103  0.0386  736  LEU A O   
1666 C CB  . LEU A 242 ? 0.2825 0.2345 0.3034 0.0239  0.0064  0.0189  736  LEU A CB  
1667 C CG  . LEU A 242 ? 0.2919 0.2597 0.2957 0.0270  0.0016  0.0162  736  LEU A CG  
1668 C CD1 . LEU A 242 ? 0.2987 0.2752 0.2964 0.0223  0.0072  0.0155  736  LEU A CD1 
1669 C CD2 . LEU A 242 ? 0.2963 0.2653 0.2859 0.0346  -0.0031 0.0270  736  LEU A CD2 
1670 N N   . GLU A 243 ? 0.4055 0.3214 0.4641 0.0226  0.0099  0.0081  737  GLU A N   
1671 C CA  . GLU A 243 ? 0.3600 0.2526 0.4341 0.0186  0.0146  0.0074  737  GLU A CA  
1672 C C   . GLU A 243 ? 0.3954 0.2712 0.4787 0.0305  0.0130  0.0109  737  GLU A C   
1673 O O   . GLU A 243 ? 0.3645 0.2159 0.4583 0.0305  0.0161  0.0194  737  GLU A O   
1674 C CB  . GLU A 243 ? 0.2835 0.1779 0.3667 0.0085  0.0162  -0.0116 737  GLU A CB  
1675 C CG  . GLU A 243 ? 0.4018 0.3081 0.4830 -0.0044 0.0189  -0.0117 737  GLU A CG  
1676 C CD  . GLU A 243 ? 0.5396 0.4590 0.6252 -0.0128 0.0174  -0.0298 737  GLU A CD  
1677 O OE1 . GLU A 243 ? 0.4688 0.3916 0.5554 -0.0084 0.0143  -0.0424 737  GLU A OE1 
1678 O OE2 . GLU A 243 ? 0.5653 0.4945 0.6537 -0.0240 0.0192  -0.0304 737  GLU A OE2 
1679 N N   . PHE A 244 ? 0.4201 0.3088 0.5013 0.0407  0.0080  0.0055  738  PHE A N   
1680 C CA  . PHE A 244 ? 0.4257 0.3035 0.5169 0.0545  0.0062  0.0113  738  PHE A CA  
1681 C C   . PHE A 244 ? 0.4266 0.2992 0.5119 0.0602  0.0041  0.0356  738  PHE A C   
1682 O O   . PHE A 244 ? 0.4682 0.3204 0.5655 0.0679  0.0049  0.0465  738  PHE A O   
1683 C CB  . PHE A 244 ? 0.3511 0.2508 0.4418 0.0631  0.0013  0.0020  738  PHE A CB  
1684 C CG  . PHE A 244 ? 0.4125 0.3097 0.5128 0.0789  -0.0018 0.0116  738  PHE A CG  
1685 C CD1 . PHE A 244 ? 0.3982 0.2785 0.5179 0.0880  0.0021  0.0041  738  PHE A CD1 
1686 C CD2 . PHE A 244 ? 0.3889 0.3017 0.4794 0.0851  -0.0087 0.0276  738  PHE A CD2 
1687 C CE1 . PHE A 244 ? 0.4459 0.3257 0.5776 0.1046  -0.0006 0.0139  738  PHE A CE1 
1688 C CE2 . PHE A 244 ? 0.3452 0.2596 0.4465 0.0998  -0.0124 0.0382  738  PHE A CE2 
1689 C CZ  . PHE A 244 ? 0.3371 0.2354 0.4602 0.1103  -0.0082 0.0321  738  PHE A CZ  
1690 N N   . GLU A 245 ? 0.3966 0.2874 0.4630 0.0568  0.0013  0.0443  739  GLU A N   
1691 C CA  . GLU A 245 ? 0.4134 0.3039 0.4700 0.0607  -0.0007 0.0671  739  GLU A CA  
1692 C C   . GLU A 245 ? 0.4839 0.3532 0.5458 0.0539  0.0057  0.0805  739  GLU A C   
1693 O O   . GLU A 245 ? 0.5144 0.3724 0.5789 0.0593  0.0047  0.1008  739  GLU A O   
1694 C CB  . GLU A 245 ? 0.4210 0.3356 0.4541 0.0575  -0.0042 0.0691  739  GLU A CB  
1695 C CG  . GLU A 245 ? 0.4356 0.3702 0.4628 0.0635  -0.0125 0.0609  739  GLU A CG  
1696 C CD  . GLU A 245 ? 0.4502 0.3902 0.4772 0.0746  -0.0197 0.0760  739  GLU A CD  
1697 O OE1 . GLU A 245 ? 0.4663 0.3960 0.4933 0.0777  -0.0188 0.0949  739  GLU A OE1 
1698 O OE2 . GLU A 245 ? 0.4444 0.4006 0.4722 0.0797  -0.0268 0.0704  739  GLU A OE2 
1699 N N   . ALA A 246 ? 0.4887 0.3538 0.5532 0.0412  0.0118  0.0710  740  ALA A N   
1700 C CA  . ALA A 246 ? 0.4969 0.3435 0.5686 0.0320  0.0179  0.0838  740  ALA A CA  
1701 C C   . ALA A 246 ? 0.5137 0.3276 0.6075 0.0350  0.0190  0.0845  740  ALA A C   
1702 O O   . ALA A 246 ? 0.5200 0.3134 0.6212 0.0309  0.0218  0.1020  740  ALA A O   
1703 C CB  . ALA A 246 ? 0.4686 0.3231 0.5397 0.0171  0.0235  0.0732  740  ALA A CB  
1704 N N   . SER A 247 ? 0.5187 0.3269 0.6235 0.0423  0.0170  0.0657  741  SER A N   
1705 C CA  . SER A 247 ? 0.5107 0.2862 0.6370 0.0471  0.0187  0.0622  741  SER A CA  
1706 C C   . SER A 247 ? 0.5297 0.2945 0.6630 0.0637  0.0147  0.0814  741  SER A C   
1707 O O   . SER A 247 ? 0.5839 0.3160 0.7350 0.0674  0.0164  0.0884  741  SER A O   
1708 C CB  . SER A 247 ? 0.4707 0.2475 0.6052 0.0494  0.0193  0.0334  741  SER A CB  
1709 O OG  . SER A 247 ? 0.5780 0.3762 0.7089 0.0636  0.0147  0.0290  741  SER A OG  
1710 N N   . GLN A 248 ? 0.5755 0.3665 0.6959 0.0734  0.0089  0.0904  742  GLN A N   
1711 C CA  . GLN A 248 ? 0.6321 0.4195 0.7587 0.0892  0.0037  0.1106  742  GLN A CA  
1712 C C   . GLN A 248 ? 0.6218 0.4147 0.7344 0.0861  0.0014  0.1403  742  GLN A C   
1713 O O   . GLN A 248 ? 0.6344 0.4150 0.7560 0.0959  -0.0019 0.1625  742  GLN A O   
1714 C CB  . GLN A 248 ? 0.6302 0.4462 0.7533 0.1017  -0.0027 0.1028  742  GLN A CB  
1715 C CG  . GLN A 248 ? 0.6223 0.4373 0.7602 0.1074  -0.0002 0.0763  742  GLN A CG  
1716 C CD  . GLN A 248 ? 0.8103 0.5888 0.9732 0.1145  0.0047  0.0716  742  GLN A CD  
1717 O OE1 . GLN A 248 ? 0.7337 0.4981 0.9037 0.1080  0.0104  0.0492  742  GLN A OE1 
1718 N NE2 . GLN A 248 ? 0.8684 0.6311 1.0448 0.1282  0.0020  0.0924  742  GLN A NE2 
1719 N N   . LYS A 249 ? 0.6565 0.4599 0.6039 0.0389  0.0199  0.1108  743  LYS A N   
1720 C CA  . LYS A 249 ? 0.6514 0.4563 0.5824 0.0332  0.0243  0.1238  743  LYS A CA  
1721 C C   . LYS A 249 ? 0.6323 0.4458 0.5685 0.0150  0.0354  0.1192  743  LYS A C   
1722 O O   . LYS A 249 ? 0.6225 0.4660 0.5680 0.0117  0.0371  0.1081  743  LYS A O   
1723 C CB  . LYS A 249 ? 0.6109 0.4388 0.5312 0.0417  0.0174  0.1246  743  LYS A CB  
1724 C CG  . LYS A 249 ? 0.5640 0.3933 0.4844 0.0547  0.0036  0.1266  743  LYS A CG  
1725 C CD  . LYS A 249 ? 0.5240 0.3774 0.4363 0.0578  -0.0052 0.1212  743  LYS A CD  
1726 C CE  . LYS A 249 ? 0.5059 0.3712 0.4284 0.0610  -0.0205 0.1165  743  LYS A CE  
1727 N NZ  . LYS A 249 ? 0.4986 0.3850 0.4178 0.0602  -0.0284 0.1087  743  LYS A NZ  
1728 N N   . CYS A 250 ? 0.6151 0.4028 0.5458 0.0033  0.0429  0.1288  744  CYS A N   
1729 C CA  . CYS A 250 ? 0.6118 0.4063 0.5505 -0.0174 0.0531  0.1257  744  CYS A CA  
1730 C C   . CYS A 250 ? 0.6273 0.4464 0.5589 -0.0245 0.0620  0.1324  744  CYS A C   
1731 O O   . CYS A 250 ? 0.5948 0.4277 0.5361 -0.0420 0.0715  0.1315  744  CYS A O   
1732 C CB  . CYS A 250 ? 0.5424 0.2954 0.4747 -0.0291 0.0578  0.1340  744  CYS A CB  
1733 S SG  . CYS A 250 ? 0.7763 0.4969 0.7152 -0.0229 0.0514  0.1229  744  CYS A SG  
1734 N N   . ASP A 251 ? 0.5100 0.3353 0.4240 -0.0123 0.0595  0.1395  745  ASP A N   
1735 C CA  . ASP A 251 ? 0.5156 0.3646 0.4195 -0.0158 0.0688  0.1431  745  ASP A CA  
1736 C C   . ASP A 251 ? 0.5907 0.4764 0.5060 -0.0081 0.0676  0.1279  745  ASP A C   
1737 O O   . ASP A 251 ? 0.5712 0.4766 0.4763 -0.0063 0.0756  0.1290  745  ASP A O   
1738 C CB  . ASP A 251 ? 0.5911 0.4239 0.4638 -0.0077 0.0665  0.1581  745  ASP A CB  
1739 C CG  . ASP A 251 ? 0.6371 0.4638 0.5028 0.0096  0.0508  0.1565  745  ASP A CG  
1740 O OD1 . ASP A 251 ? 0.6597 0.4763 0.5406 0.0152  0.0425  0.1519  745  ASP A OD1 
1741 O OD2 . ASP A 251 ? 0.6912 0.5230 0.5349 0.0171  0.0471  0.1601  745  ASP A OD2 
1742 N N   . LEU A 252 ? 0.5358 0.4287 0.4697 -0.0025 0.0586  0.1141  746  LEU A N   
1743 C CA  . LEU A 252 ? 0.5272 0.4512 0.4718 0.0055  0.0559  0.0999  746  LEU A CA  
1744 C C   . LEU A 252 ? 0.5379 0.4784 0.5114 -0.0041 0.0560  0.0879  746  LEU A C   
1745 O O   . LEU A 252 ? 0.5144 0.4347 0.4959 -0.0098 0.0512  0.0855  746  LEU A O   
1746 C CB  . LEU A 252 ? 0.4952 0.4129 0.4305 0.0221  0.0422  0.0949  746  LEU A CB  
1747 C CG  . LEU A 252 ? 0.4804 0.3850 0.3857 0.0308  0.0384  0.1056  746  LEU A CG  
1748 C CD1 . LEU A 252 ? 0.5140 0.4111 0.4155 0.0428  0.0230  0.1029  746  LEU A CD1 
1749 C CD2 . LEU A 252 ? 0.5243 0.4466 0.4138 0.0339  0.0463  0.1039  746  LEU A CD2 
1750 N N   . VAL A 253 ? 0.4761 0.4525 0.4636 -0.0052 0.0614  0.0808  747  VAL A N   
1751 C CA  . VAL A 253 ? 0.4525 0.4510 0.4680 -0.0147 0.0599  0.0700  747  VAL A CA  
1752 C C   . VAL A 253 ? 0.4175 0.4469 0.4412 -0.0010 0.0557  0.0586  747  VAL A C   
1753 O O   . VAL A 253 ? 0.4172 0.4558 0.4265 0.0123  0.0592  0.0600  747  VAL A O   
1754 C CB  . VAL A 253 ? 0.4217 0.4390 0.4530 -0.0353 0.0720  0.0763  747  VAL A CB  
1755 C CG1 . VAL A 253 ? 0.5087 0.4894 0.5286 -0.0501 0.0757  0.0881  747  VAL A CG1 
1756 C CG2 . VAL A 253 ? 0.4321 0.4813 0.4616 -0.0303 0.0850  0.0819  747  VAL A CG2 
1757 N N   . THR A 254 ? 0.4091 0.4510 0.4529 -0.0043 0.0479  0.0472  748  THR A N   
1758 C CA  . THR A 254 ? 0.3716 0.4445 0.4265 0.0068  0.0436  0.0369  748  THR A CA  
1759 C C   . THR A 254 ? 0.4837 0.5977 0.5660 -0.0046 0.0509  0.0370  748  THR A C   
1760 O O   . THR A 254 ? 0.5766 0.6922 0.6748 -0.0248 0.0511  0.0382  748  THR A O   
1761 C CB  . THR A 254 ? 0.3972 0.4598 0.4554 0.0112  0.0293  0.0250  748  THR A CB  
1762 O OG1 . THR A 254 ? 0.3284 0.3900 0.4039 -0.0066 0.0263  0.0210  748  THR A OG1 
1763 C CG2 . THR A 254 ? 0.3593 0.3852 0.3953 0.0204  0.0229  0.0271  748  THR A CG2 
1764 N N   . THR A 255 ? 0.4514 0.5980 0.5386 0.0081  0.0568  0.0362  749  THR A N   
1765 C CA  . THR A 255 ? 0.4873 0.6812 0.6037 0.0006  0.0650  0.0384  749  THR A CA  
1766 C C   . THR A 255 ? 0.5097 0.7313 0.6469 0.0066  0.0539  0.0276  749  THR A C   
1767 O O   . THR A 255 ? 0.4815 0.6955 0.6057 0.0258  0.0466  0.0201  749  THR A O   
1768 C CB  . THR A 255 ? 0.4877 0.7024 0.5968 0.0129  0.0815  0.0460  749  THR A CB  
1769 O OG1 . THR A 255 ? 0.5033 0.7717 0.6452 0.0103  0.0892  0.0478  749  THR A OG1 
1770 C CG2 . THR A 255 ? 0.3891 0.5875 0.4702 0.0387  0.0788  0.0405  749  THR A CG2 
1771 N N   . GLY A 256 ? 0.7140 0.9663 0.8818 -0.0114 0.0517  0.0275  750  GLY A N   
1772 C CA  . GLY A 256 ? 0.7111 0.9909 0.8995 -0.0087 0.0394  0.0185  750  GLY A CA  
1773 C C   . GLY A 256 ? 0.7471 0.9904 0.9205 -0.0082 0.0231  0.0073  750  GLY A C   
1774 O O   . GLY A 256 ? 0.7065 0.9053 0.8561 -0.0085 0.0216  0.0067  750  GLY A O   
1775 N N   . GLU A 257 ? 0.5620 0.8271 0.7504 -0.0067 0.0111  -0.0007 751  GLU A N   
1776 C CA  . GLU A 257 ? 0.4678 0.7026 0.6417 -0.0049 -0.0036 -0.0118 751  GLU A CA  
1777 C C   . GLU A 257 ? 0.4111 0.6346 0.5650 0.0215  -0.0068 -0.0161 751  GLU A C   
1778 O O   . GLU A 257 ? 0.3976 0.6054 0.5329 0.0342  0.0016  -0.0113 751  GLU A O   
1779 C CB  . GLU A 257 ? 0.4923 0.7521 0.6874 -0.0184 -0.0164 -0.0182 751  GLU A CB  
1780 N N   . LEU A 258 ? 0.3479 0.5774 0.5032 0.0282  -0.0195 -0.0247 752  LEU A N   
1781 C CA  . LEU A 258 ? 0.2705 0.4894 0.4066 0.0511  -0.0239 -0.0287 752  LEU A CA  
1782 C C   . LEU A 258 ? 0.2487 0.5083 0.4005 0.0656  -0.0236 -0.0276 752  LEU A C   
1783 O O   . LEU A 258 ? 0.3749 0.6665 0.5504 0.0588  -0.0312 -0.0295 752  LEU A O   
1784 C CB  . LEU A 258 ? 0.2464 0.4398 0.3690 0.0502  -0.0378 -0.0383 752  LEU A CB  
1785 C CG  . LEU A 258 ? 0.3106 0.4714 0.4256 0.0339  -0.0404 -0.0416 752  LEU A CG  
1786 C CD1 . LEU A 258 ? 0.2355 0.3734 0.3334 0.0397  -0.0513 -0.0503 752  LEU A CD1 
1787 C CD2 . LEU A 258 ? 0.3092 0.4431 0.4112 0.0329  -0.0299 -0.0342 752  LEU A CD2 
1788 N N   . PHE A 259 ? 0.2193 0.4771 0.3566 0.0858  -0.0151 -0.0243 753  PHE A N   
1789 C CA  . PHE A 259 ? 0.2041 0.4718 0.3394 0.0976  -0.0128 -0.0219 753  PHE A CA  
1790 C C   . PHE A 259 ? 0.1705 0.4035 0.2769 0.1049  -0.0228 -0.0273 753  PHE A C   
1791 O O   . PHE A 259 ? 0.1633 0.3986 0.2634 0.1154  -0.0215 -0.0259 753  PHE A O   
1792 C CB  . PHE A 259 ? 0.1953 0.4667 0.3213 0.1109  0.0034  -0.0153 753  PHE A CB  
1793 C CG  . PHE A 259 ? 0.1999 0.4290 0.2872 0.1209  0.0059  -0.0165 753  PHE A CG  
1794 C CD1 . PHE A 259 ? 0.2583 0.4566 0.3134 0.1319  0.0015  -0.0195 753  PHE A CD1 
1795 C CD2 . PHE A 259 ? 0.2115 0.4329 0.2940 0.1180  0.0125  -0.0136 753  PHE A CD2 
1796 C CE1 . PHE A 259 ? 0.2663 0.4272 0.2854 0.1373  0.0019  -0.0199 753  PHE A CE1 
1797 C CE2 . PHE A 259 ? 0.2651 0.4471 0.3108 0.1262  0.0133  -0.0135 753  PHE A CE2 
1798 C CZ  . PHE A 259 ? 0.2672 0.4197 0.2815 0.1345  0.0071  -0.0168 753  PHE A CZ  
1799 N N   . PHE A 260 ? 0.1682 0.3707 0.2578 0.0988  -0.0316 -0.0328 754  PHE A N   
1800 C CA  . PHE A 260 ? 0.1608 0.3310 0.2224 0.1015  -0.0386 -0.0371 754  PHE A CA  
1801 C C   . PHE A 260 ? 0.2265 0.3744 0.2808 0.0907  -0.0460 -0.0423 754  PHE A C   
1802 O O   . PHE A 260 ? 0.2510 0.3910 0.3058 0.0874  -0.0445 -0.0419 754  PHE A O   
1803 C CB  . PHE A 260 ? 0.2361 0.3798 0.2656 0.1126  -0.0334 -0.0358 754  PHE A CB  
1804 C CG  . PHE A 260 ? 0.2924 0.4097 0.2957 0.1140  -0.0391 -0.0402 754  PHE A CG  
1805 C CD1 . PHE A 260 ? 0.2604 0.3876 0.2667 0.1195  -0.0416 -0.0409 754  PHE A CD1 
1806 C CD2 . PHE A 260 ? 0.3329 0.4178 0.3106 0.1096  -0.0413 -0.0430 754  PHE A CD2 
1807 C CE1 . PHE A 260 ? 0.3260 0.4297 0.3088 0.1210  -0.0458 -0.0451 754  PHE A CE1 
1808 C CE2 . PHE A 260 ? 0.3505 0.4146 0.3072 0.1097  -0.0445 -0.0476 754  PHE A CE2 
1809 C CZ  . PHE A 260 ? 0.3517 0.4241 0.3100 0.1157  -0.0467 -0.0489 754  PHE A CZ  
1810 N N   . ARG A 261 ? 0.1670 0.3051 0.2148 0.0864  -0.0529 -0.0466 755  ARG A N   
1811 C CA  . ARG A 261 ? 0.1765 0.2924 0.2154 0.0778  -0.0577 -0.0516 755  ARG A CA  
1812 C C   . ARG A 261 ? 0.2529 0.3356 0.2625 0.0809  -0.0550 -0.0527 755  ARG A C   
1813 O O   . ARG A 261 ? 0.2753 0.3520 0.2721 0.0866  -0.0540 -0.0529 755  ARG A O   
1814 C CB  . ARG A 261 ? 0.1960 0.3212 0.2449 0.0702  -0.0652 -0.0553 755  ARG A CB  
1815 C CG  . ARG A 261 ? 0.2470 0.4054 0.3255 0.0604  -0.0701 -0.0553 755  ARG A CG  
1816 C CD  . ARG A 261 ? 0.1880 0.3479 0.2687 0.0497  -0.0791 -0.0589 755  ARG A CD  
1817 N NE  . ARG A 261 ? 0.1918 0.3859 0.2998 0.0371  -0.0851 -0.0576 755  ARG A NE  
1818 C CZ  . ARG A 261 ? 0.2682 0.4923 0.3935 0.0396  -0.0865 -0.0511 755  ARG A CZ  
1819 N NH1 . ARG A 261 ? 0.1791 0.4014 0.2960 0.0555  -0.0825 -0.0468 755  ARG A NH1 
1820 N NH2 . ARG A 261 ? 0.2076 0.4632 0.3594 0.0246  -0.0922 -0.0489 755  ARG A NH2 
1821 N N   . SER A 262 ? 0.2467 0.3099 0.2481 0.0766  -0.0541 -0.0534 756  SER A N   
1822 C CA  . SER A 262 ? 0.2346 0.2717 0.2151 0.0763  -0.0509 -0.0538 756  SER A CA  
1823 C C   . SER A 262 ? 0.2378 0.2625 0.2198 0.0707  -0.0516 -0.0552 756  SER A C   
1824 O O   . SER A 262 ? 0.2046 0.2363 0.1988 0.0682  -0.0552 -0.0568 756  SER A O   
1825 C CB  . SER A 262 ? 0.2390 0.2672 0.2051 0.0800  -0.0469 -0.0497 756  SER A CB  
1826 O OG  . SER A 262 ? 0.2718 0.3052 0.2452 0.0793  -0.0464 -0.0452 756  SER A OG  
1827 N N   . GLY A 263 ? 0.2472 0.2562 0.2207 0.0677  -0.0480 -0.0520 757  GLY A N   
1828 C CA  . GLY A 263 ? 0.2356 0.2373 0.2120 0.0624  -0.0474 -0.0495 757  GLY A CA  
1829 C C   . GLY A 263 ? 0.2449 0.2364 0.2136 0.0597  -0.0439 -0.0435 757  GLY A C   
1830 O O   . GLY A 263 ? 0.2541 0.2414 0.2164 0.0613  -0.0427 -0.0415 757  GLY A O   
1831 N N   . PHE A 264 ? 0.2162 0.2043 0.1857 0.0567  -0.0434 -0.0416 758  PHE A N   
1832 C CA  . PHE A 264 ? 0.2270 0.2086 0.1906 0.0555  -0.0419 -0.0380 758  PHE A CA  
1833 C C   . PHE A 264 ? 0.2199 0.2001 0.1847 0.0548  -0.0417 -0.0377 758  PHE A C   
1834 O O   . PHE A 264 ? 0.2285 0.2117 0.1981 0.0546  -0.0425 -0.0394 758  PHE A O   
1835 C CB  . PHE A 264 ? 0.2555 0.2356 0.2171 0.0559  -0.0431 -0.0372 758  PHE A CB  
1836 C CG  . PHE A 264 ? 0.2473 0.2283 0.2073 0.0582  -0.0442 -0.0368 758  PHE A CG  
1837 C CD1 . PHE A 264 ? 0.2008 0.1813 0.1557 0.0606  -0.0430 -0.0367 758  PHE A CD1 
1838 C CD2 . PHE A 264 ? 0.2455 0.2297 0.2140 0.0585  -0.0453 -0.0321 758  PHE A CD2 
1839 C CE1 . PHE A 264 ? 0.2034 0.1890 0.1607 0.0611  -0.0423 -0.0313 758  PHE A CE1 
1840 C CE2 . PHE A 264 ? 0.2428 0.2291 0.2154 0.0608  -0.0447 -0.0271 758  PHE A CE2 
1841 C CZ  . PHE A 264 ? 0.2155 0.2038 0.1815 0.0619  -0.0435 -0.0267 758  PHE A CZ  
1842 N N   . GLY A 265 ? 0.1816 0.2022 0.2765 -0.0248 -0.0069 -0.0175 759  GLY A N   
1843 C CA  . GLY A 265 ? 0.1548 0.1862 0.2515 -0.0170 -0.0087 -0.0151 759  GLY A CA  
1844 C C   . GLY A 265 ? 0.2121 0.2298 0.3039 -0.0183 -0.0089 -0.0119 759  GLY A C   
1845 O O   . GLY A 265 ? 0.1912 0.1903 0.2766 -0.0229 -0.0073 -0.0086 759  GLY A O   
1846 N N   . ILE A 266 ? 0.1614 0.1894 0.2565 -0.0153 -0.0104 -0.0140 760  ILE A N   
1847 C CA  . ILE A 266 ? 0.1512 0.1731 0.2463 -0.0168 -0.0093 -0.0120 760  ILE A CA  
1848 C C   . ILE A 266 ? 0.1826 0.1982 0.2677 -0.0158 -0.0027 -0.0027 760  ILE A C   
1849 O O   . ILE A 266 ? 0.1833 0.2055 0.2632 -0.0109 -0.0001 0.0013  760  ILE A O   
1850 C CB  . ILE A 266 ? 0.1849 0.2232 0.2875 -0.0149 -0.0092 -0.0187 760  ILE A CB  
1851 C CG1 . ILE A 266 ? 0.1847 0.2272 0.2963 -0.0140 -0.0161 -0.0290 760  ILE A CG1 
1852 C CG2 . ILE A 266 ? 0.1144 0.1512 0.2229 -0.0177 -0.0075 -0.0191 760  ILE A CG2 
1853 C CD1 . ILE A 266 ? 0.1568 0.1834 0.2759 -0.0165 -0.0248 -0.0328 760  ILE A CD1 
1854 N N   . GLY A 267 ? 0.1625 0.1628 0.2440 -0.0203 -0.0018 0.0009  761  GLY A N   
1855 C CA  . GLY A 267 ? 0.2161 0.2045 0.2859 -0.0206 0.0040  0.0094  761  GLY A CA  
1856 C C   . GLY A 267 ? 0.2075 0.1970 0.2758 -0.0249 0.0065  0.0114  761  GLY A C   
1857 O O   . GLY A 267 ? 0.2248 0.2141 0.3022 -0.0301 0.0032  0.0075  761  GLY A O   
1858 N N   . MET A 268 ? 0.2472 0.2381 0.3041 -0.0233 0.0117  0.0171  762  MET A N   
1859 C CA  . MET A 268 ? 0.2791 0.2696 0.3300 -0.0304 0.0166  0.0197  762  MET A CA  
1860 C C   . MET A 268 ? 0.3072 0.2773 0.3366 -0.0303 0.0203  0.0305  762  MET A C   
1861 O O   . MET A 268 ? 0.3298 0.2919 0.3522 -0.0220 0.0186  0.0347  762  MET A O   
1862 C CB  . MET A 268 ? 0.3108 0.3226 0.3643 -0.0317 0.0199  0.0143  762  MET A CB  
1863 C CG  . MET A 268 ? 0.3202 0.3515 0.3952 -0.0300 0.0164  0.0020  762  MET A CG  
1864 S SD  . MET A 268 ? 0.4996 0.5486 0.5706 -0.0251 0.0168  -0.0033 762  MET A SD  
1865 C CE  . MET A 268 ? 0.2352 0.2742 0.3001 -0.0165 0.0098  0.0030  762  MET A CE  
1866 N N   . ARG A 269 ? 0.3336 0.2954 0.3540 -0.0397 0.0250  0.0341  763  ARG A N   
1867 C CA  . ARG A 269 ? 0.3425 0.2813 0.3382 -0.0410 0.0280  0.0447  763  ARG A CA  
1868 C C   . ARG A 269 ? 0.3648 0.3075 0.3451 -0.0377 0.0283  0.0487  763  ARG A C   
1869 O O   . ARG A 269 ? 0.3348 0.2991 0.3208 -0.0399 0.0297  0.0428  763  ARG A O   
1870 C CB  . ARG A 269 ? 0.3835 0.3120 0.3718 -0.0550 0.0331  0.0471  763  ARG A CB  
1871 C CG  . ARG A 269 ? 0.3833 0.2971 0.3769 -0.0588 0.0308  0.0466  763  ARG A CG  
1872 C CD  . ARG A 269 ? 0.3073 0.2114 0.2931 -0.0739 0.0349  0.0492  763  ARG A CD  
1873 N NE  . ARG A 269 ? 0.3826 0.3154 0.3872 -0.0831 0.0379  0.0412  763  ARG A NE  
1874 C CZ  . ARG A 269 ? 0.3115 0.2623 0.3434 -0.0856 0.0330  0.0321  763  ARG A CZ  
1875 N NH1 . ARG A 269 ? 0.2518 0.1915 0.2900 -0.0817 0.0241  0.0312  763  ARG A NH1 
1876 N NH2 . ARG A 269 ? 0.2662 0.2457 0.3189 -0.0923 0.0369  0.0230  763  ARG A NH2 
1877 N N   . LYS A 270 ? 0.3953 0.3144 0.3543 -0.0324 0.0259  0.0587  764  LYS A N   
1878 C CA  . LYS A 270 ? 0.4155 0.3332 0.3572 -0.0271 0.0215  0.0640  764  LYS A CA  
1879 C C   . LYS A 270 ? 0.4580 0.3763 0.3784 -0.0413 0.0274  0.0662  764  LYS A C   
1880 O O   . LYS A 270 ? 0.5377 0.4595 0.4431 -0.0401 0.0241  0.0683  764  LYS A O   
1881 C CB  . LYS A 270 ? 0.4887 0.3777 0.4143 -0.0165 0.0150  0.0740  764  LYS A CB  
1882 C CG  . LYS A 270 ? 0.5176 0.4109 0.4657 -0.0021 0.0110  0.0695  764  LYS A CG  
1883 C CD  . LYS A 270 ? 0.5327 0.4050 0.4714 0.0124  0.0031  0.0765  764  LYS A CD  
1884 C CE  . LYS A 270 ? 0.5436 0.3833 0.4709 0.0121  0.0069  0.0808  764  LYS A CE  
1885 N NZ  . LYS A 270 ? 0.6577 0.4783 0.5829 0.0296  -0.0010 0.0848  764  LYS A NZ  
1886 N N   . ASP A 271 ? 0.3972 0.3127 0.3154 -0.0561 0.0363  0.0651  765  ASP A N   
1887 C CA  . ASP A 271 ? 0.4566 0.3757 0.3565 -0.0728 0.0454  0.0650  765  ASP A CA  
1888 C C   . ASP A 271 ? 0.4550 0.4109 0.3825 -0.0796 0.0534  0.0500  765  ASP A C   
1889 O O   . ASP A 271 ? 0.4749 0.4397 0.3954 -0.0956 0.0645  0.0460  765  ASP A O   
1890 C CB  . ASP A 271 ? 0.5266 0.4198 0.4059 -0.0872 0.0513  0.0726  765  ASP A CB  
1891 C CG  . ASP A 271 ? 0.5779 0.4832 0.4845 -0.0944 0.0561  0.0650  765  ASP A CG  
1892 O OD1 . ASP A 271 ? 0.5295 0.4477 0.4645 -0.0837 0.0506  0.0585  765  ASP A OD1 
1893 O OD2 . ASP A 271 ? 0.5739 0.4746 0.4721 -0.1121 0.0645  0.0655  765  ASP A OD2 
1894 N N   . SER A 272 ? 0.3964 0.3729 0.3549 -0.0684 0.0482  0.0408  766  SER A N   
1895 C CA  . SER A 272 ? 0.3697 0.3781 0.3569 -0.0720 0.0534  0.0257  766  SER A CA  
1896 C C   . SER A 272 ? 0.3684 0.3925 0.3446 -0.0760 0.0594  0.0198  766  SER A C   
1897 O O   . SER A 272 ? 0.4759 0.4930 0.4342 -0.0688 0.0533  0.0247  766  SER A O   
1898 C CB  . SER A 272 ? 0.4146 0.4336 0.4310 -0.0592 0.0442  0.0188  766  SER A CB  
1899 O OG  . SER A 272 ? 0.4117 0.4585 0.4545 -0.0599 0.0466  0.0040  766  SER A OG  
1900 N N   . PRO A 273 ? 0.4468 0.4929 0.4339 -0.0880 0.0716  0.0081  767  PRO A N   
1901 C CA  . PRO A 273 ? 0.3898 0.4511 0.3654 -0.0932 0.0797  -0.0002 767  PRO A CA  
1902 C C   . PRO A 273 ? 0.3552 0.4377 0.3556 -0.0807 0.0744  -0.0130 767  PRO A C   
1903 O O   . PRO A 273 ? 0.4047 0.4964 0.3922 -0.0833 0.0793  -0.0198 767  PRO A O   
1904 C CB  . PRO A 273 ? 0.3851 0.4648 0.3690 -0.1112 0.0970  -0.0107 767  PRO A CB  
1905 C CG  . PRO A 273 ? 0.4027 0.4913 0.4239 -0.1085 0.0933  -0.0148 767  PRO A CG  
1906 C CD  . PRO A 273 ? 0.4081 0.4668 0.4185 -0.0985 0.0790  0.0010  767  PRO A CD  
1907 N N   . TRP A 274 ? 0.3932 0.4804 0.4244 -0.0687 0.0644  -0.0165 768  TRP A N   
1908 C CA  . TRP A 274 ? 0.3803 0.4832 0.4338 -0.0579 0.0584  -0.0285 768  TRP A CA  
1909 C C   . TRP A 274 ? 0.3845 0.4749 0.4262 -0.0468 0.0461  -0.0207 768  TRP A C   
1910 O O   . TRP A 274 ? 0.3634 0.4640 0.4183 -0.0396 0.0409  -0.0298 768  TRP A O   
1911 C CB  . TRP A 274 ? 0.4067 0.5188 0.4983 -0.0525 0.0527  -0.0370 768  TRP A CB  
1912 C CG  . TRP A 274 ? 0.4788 0.6048 0.5901 -0.0621 0.0614  -0.0442 768  TRP A CG  
1913 C CD1 . TRP A 274 ? 0.4536 0.5690 0.5602 -0.0707 0.0634  -0.0353 768  TRP A CD1 
1914 C CD2 . TRP A 274 ? 0.4516 0.6066 0.5934 -0.0641 0.0691  -0.0634 768  TRP A CD2 
1915 N NE1 . TRP A 274 ? 0.4524 0.5903 0.5855 -0.0791 0.0714  -0.0473 768  TRP A NE1 
1916 C CE2 . TRP A 274 ? 0.4674 0.6314 0.6247 -0.0745 0.0753  -0.0653 768  TRP A CE2 
1917 C CE3 . TRP A 274 ? 0.4002 0.5747 0.5591 -0.0580 0.0715  -0.0804 768  TRP A CE3 
1918 C CZ2 . TRP A 274 ? 0.4610 0.6568 0.6545 -0.0783 0.0839  -0.0842 768  TRP A CZ2 
1919 C CZ3 . TRP A 274 ? 0.4070 0.6102 0.6002 -0.0606 0.0805  -0.0995 768  TRP A CZ3 
1920 C CH2 . TRP A 274 ? 0.4563 0.6719 0.6686 -0.0704 0.0867  -0.1016 768  TRP A CH2 
1921 N N   . LYS A 275 ? 0.3248 0.3939 0.3436 -0.0452 0.0411  -0.0052 769  LYS A N   
1922 C CA  . LYS A 275 ? 0.3286 0.3896 0.3472 -0.0336 0.0291  0.0006  769  LYS A CA  
1923 C C   . LYS A 275 ? 0.3371 0.4078 0.3470 -0.0303 0.0249  -0.0039 769  LYS A C   
1924 O O   . LYS A 275 ? 0.3155 0.3916 0.3388 -0.0224 0.0166  -0.0075 769  LYS A O   
1925 C CB  . LYS A 275 ? 0.3651 0.4026 0.3643 -0.0312 0.0251  0.0161  769  LYS A CB  
1926 C CG  . LYS A 275 ? 0.4009 0.4248 0.3657 -0.0384 0.0282  0.0253  769  LYS A CG  
1927 C CD  . LYS A 275 ? 0.4455 0.4423 0.3940 -0.0336 0.0222  0.0399  769  LYS A CD  
1928 C CE  . LYS A 275 ? 0.4698 0.4457 0.3789 -0.0413 0.0228  0.0506  769  LYS A CE  
1929 N NZ  . LYS A 275 ? 0.5619 0.5086 0.4556 -0.0329 0.0135  0.0643  769  LYS A NZ  
1930 N N   . GLN A 276 ? 0.3429 0.4145 0.3279 -0.0382 0.0306  -0.0040 770  GLN A N   
1931 C CA  . GLN A 276 ? 0.3465 0.4244 0.3185 -0.0363 0.0252  -0.0077 770  GLN A CA  
1932 C C   . GLN A 276 ? 0.3368 0.4348 0.3307 -0.0354 0.0283  -0.0253 770  GLN A C   
1933 O O   . GLN A 276 ? 0.2988 0.4018 0.2978 -0.0294 0.0194  -0.0294 770  GLN A O   
1934 C CB  . GLN A 276 ? 0.3864 0.4548 0.3190 -0.0471 0.0299  -0.0026 770  GLN A CB  
1935 C CG  . GLN A 276 ? 0.5068 0.5829 0.4226 -0.0494 0.0272  -0.0099 770  GLN A CG  
1936 C CD  . GLN A 276 ? 0.5835 0.6549 0.4944 -0.0389 0.0086  -0.0024 770  GLN A CD  
1937 O OE1 . GLN A 276 ? 0.5200 0.5918 0.4542 -0.0278 -0.0003 0.0019  770  GLN A OE1 
1938 N NE2 . GLN A 276 ? 0.4740 0.5416 0.3547 -0.0436 0.0029  -0.0017 770  GLN A NE2 
1939 N N   . ASN A 277 ? 0.3060 0.4156 0.3147 -0.0413 0.0403  -0.0368 771  ASN A N   
1940 C CA  . ASN A 277 ? 0.3323 0.4588 0.3635 -0.0386 0.0425  -0.0550 771  ASN A CA  
1941 C C   . ASN A 277 ? 0.3237 0.4489 0.3838 -0.0282 0.0314  -0.0571 771  ASN A C   
1942 O O   . ASN A 277 ? 0.2912 0.4219 0.3624 -0.0236 0.0267  -0.0681 771  ASN A O   
1943 C CB  . ASN A 277 ? 0.2471 0.3891 0.2914 -0.0464 0.0582  -0.0685 771  ASN A CB  
1944 C CG  . ASN A 277 ? 0.3694 0.5151 0.3830 -0.0592 0.0718  -0.0724 771  ASN A CG  
1945 O OD1 . ASN A 277 ? 0.4408 0.5786 0.4248 -0.0609 0.0675  -0.0685 771  ASN A OD1 
1946 N ND2 . ASN A 277 ? 0.4494 0.6072 0.4691 -0.0699 0.0883  -0.0806 771  ASN A ND2 
1947 N N   . VAL A 278 ? 0.2728 0.3874 0.3417 -0.0258 0.0271  -0.0470 772  VAL A N   
1948 C CA  . VAL A 278 ? 0.2751 0.3832 0.3630 -0.0187 0.0164  -0.0470 772  VAL A CA  
1949 C C   . VAL A 278 ? 0.2298 0.3344 0.3086 -0.0144 0.0075  -0.0437 772  VAL A C   
1950 O O   . VAL A 278 ? 0.2324 0.3380 0.3223 -0.0115 0.0011  -0.0515 772  VAL A O   
1951 C CB  . VAL A 278 ? 0.2744 0.3691 0.3664 -0.0191 0.0147  -0.0363 772  VAL A CB  
1952 C CG1 . VAL A 278 ? 0.2096 0.2928 0.3097 -0.0143 0.0045  -0.0336 772  VAL A CG1 
1953 C CG2 . VAL A 278 ? 0.2338 0.3343 0.3434 -0.0230 0.0198  -0.0425 772  VAL A CG2 
1954 N N   . SER A 279 ? 0.2384 0.3384 0.2976 -0.0144 0.0060  -0.0324 773  SER A N   
1955 C CA  . SER A 279 ? 0.2367 0.3376 0.2919 -0.0103 -0.0033 -0.0296 773  SER A CA  
1956 C C   . SER A 279 ? 0.2587 0.3704 0.3092 -0.0119 -0.0054 -0.0406 773  SER A C   
1957 O O   . SER A 279 ? 0.2149 0.3297 0.2732 -0.0100 -0.0130 -0.0450 773  SER A O   
1958 C CB  . SER A 279 ? 0.1695 0.2637 0.2068 -0.0082 -0.0065 -0.0161 773  SER A CB  
1959 O OG  . SER A 279 ? 0.2807 0.3801 0.3202 -0.0033 -0.0167 -0.0146 773  SER A OG  
1960 N N   . LEU A 280 ? 0.2316 0.3481 0.2675 -0.0171 0.0022  -0.0459 774  LEU A N   
1961 C CA  . LEU A 280 ? 0.2622 0.3869 0.2906 -0.0197 0.0018  -0.0580 774  LEU A CA  
1962 C C   . LEU A 280 ? 0.2753 0.4034 0.3272 -0.0169 0.0013  -0.0727 774  LEU A C   
1963 O O   . LEU A 280 ? 0.2154 0.3452 0.2666 -0.0167 -0.0048 -0.0806 774  LEU A O   
1964 C CB  . LEU A 280 ? 0.2630 0.3907 0.2686 -0.0278 0.0132  -0.0622 774  LEU A CB  
1965 C CG  . LEU A 280 ? 0.3218 0.4404 0.2934 -0.0326 0.0109  -0.0483 774  LEU A CG  
1966 C CD1 . LEU A 280 ? 0.2721 0.3907 0.2186 -0.0445 0.0254  -0.0533 774  LEU A CD1 
1967 C CD2 . LEU A 280 ? 0.2601 0.3781 0.2178 -0.0304 -0.0035 -0.0453 774  LEU A CD2 
1968 N N   . SER A 281 ? 0.2149 0.3420 0.2870 -0.0151 0.0060  -0.0763 775  SER A N   
1969 C CA  . SER A 281 ? 0.2338 0.3595 0.3281 -0.0110 0.0022  -0.0892 775  SER A CA  
1970 C C   . SER A 281 ? 0.1874 0.3014 0.2869 -0.0087 -0.0102 -0.0846 775  SER A C   
1971 O O   . SER A 281 ? 0.1758 0.2848 0.2820 -0.0073 -0.0163 -0.0947 775  SER A O   
1972 C CB  . SER A 281 ? 0.1831 0.3103 0.2991 -0.0091 0.0068  -0.0930 775  SER A CB  
1973 O OG  . SER A 281 ? 0.3629 0.5043 0.4771 -0.0134 0.0206  -0.1002 775  SER A OG  
1974 N N   . ILE A 282 ? 0.2133 0.3218 0.3089 -0.0090 -0.0133 -0.0704 776  ILE A N   
1975 C CA  . ILE A 282 ? 0.1537 0.2537 0.2529 -0.0095 -0.0221 -0.0669 776  ILE A CA  
1976 C C   . ILE A 282 ? 0.1619 0.2690 0.2527 -0.0118 -0.0272 -0.0716 776  ILE A C   
1977 O O   . ILE A 282 ? 0.1901 0.2908 0.2850 -0.0143 -0.0335 -0.0779 776  ILE A O   
1978 C CB  . ILE A 282 ? 0.1925 0.2882 0.2901 -0.0093 -0.0215 -0.0530 776  ILE A CB  
1979 C CG1 . ILE A 282 ? 0.1590 0.2453 0.2629 -0.0088 -0.0175 -0.0487 776  ILE A CG1 
1980 C CG2 . ILE A 282 ? 0.1376 0.2280 0.2394 -0.0120 -0.0274 -0.0515 776  ILE A CG2 
1981 C CD1 . ILE A 282 ? 0.1181 0.1917 0.2339 -0.0094 -0.0227 -0.0552 776  ILE A CD1 
1982 N N   . LEU A 283 ? 0.1593 0.2771 0.2358 -0.0122 -0.0258 -0.0682 777  LEU A N   
1983 C CA  . LEU A 283 ? 0.2214 0.3468 0.2887 -0.0151 -0.0325 -0.0724 777  LEU A CA  
1984 C C   . LEU A 283 ? 0.1949 0.3182 0.2602 -0.0174 -0.0321 -0.0881 777  LEU A C   
1985 O O   . LEU A 283 ? 0.1791 0.3006 0.2449 -0.0208 -0.0393 -0.0945 777  LEU A O   
1986 C CB  . LEU A 283 ? 0.1778 0.3109 0.2259 -0.0151 -0.0332 -0.0650 777  LEU A CB  
1987 C CG  . LEU A 283 ? 0.1947 0.3272 0.2433 -0.0109 -0.0350 -0.0499 777  LEU A CG  
1988 C CD1 . LEU A 283 ? 0.1954 0.3298 0.2204 -0.0110 -0.0390 -0.0426 777  LEU A CD1 
1989 C CD2 . LEU A 283 ? 0.1601 0.2971 0.2264 -0.0091 -0.0421 -0.0471 777  LEU A CD2 
1990 N N   . LYS A 284 ? 0.2266 0.3503 0.2907 -0.0160 -0.0231 -0.0958 778  LYS A N   
1991 C CA  . LYS A 284 ? 0.2129 0.3346 0.2779 -0.0164 -0.0213 -0.1133 778  LYS A CA  
1992 C C   . LYS A 284 ? 0.2038 0.3114 0.2854 -0.0141 -0.0291 -0.1195 778  LYS A C   
1993 O O   . LYS A 284 ? 0.2019 0.3028 0.2797 -0.0161 -0.0344 -0.1303 778  LYS A O   
1994 C CB  . LYS A 284 ? 0.1992 0.3273 0.2670 -0.0148 -0.0082 -0.1218 778  LYS A CB  
1995 C CG  . LYS A 284 ? 0.2600 0.3882 0.3315 -0.0136 -0.0040 -0.1428 778  LYS A CG  
1996 C CD  . LYS A 284 ? 0.2774 0.4174 0.3563 -0.0129 0.0117  -0.1529 778  LYS A CD  
1997 C CE  . LYS A 284 ? 0.2980 0.4400 0.3837 -0.0104 0.0176  -0.1767 778  LYS A CE  
1998 N NZ  . LYS A 284 ? 0.4300 0.5709 0.4849 -0.0179 0.0190  -0.1828 778  LYS A NZ  
1999 N N   . SER A 285 ? 0.1722 0.2713 0.2685 -0.0111 -0.0309 -0.1123 779  SER A N   
2000 C CA  . SER A 285 ? 0.1730 0.2527 0.2794 -0.0103 -0.0401 -0.1165 779  SER A CA  
2001 C C   . SER A 285 ? 0.2091 0.2816 0.3067 -0.0179 -0.0483 -0.1125 779  SER A C   
2002 O O   . SER A 285 ? 0.2235 0.2791 0.3199 -0.0207 -0.0560 -0.1201 779  SER A O   
2003 C CB  . SER A 285 ? 0.1704 0.2409 0.2896 -0.0073 -0.0411 -0.1086 779  SER A CB  
2004 O OG  . SER A 285 ? 0.1582 0.2383 0.2895 -0.0016 -0.0338 -0.1137 779  SER A OG  
2005 N N   . HIS A 286 ? 0.1924 0.2773 0.2848 -0.0215 -0.0470 -0.1012 780  HIS A N   
2006 C CA  . HIS A 286 ? 0.1712 0.2571 0.2596 -0.0296 -0.0533 -0.0997 780  HIS A CA  
2007 C C   . HIS A 286 ? 0.2153 0.3051 0.2936 -0.0334 -0.0573 -0.1108 780  HIS A C   
2008 O O   . HIS A 286 ? 0.2198 0.2993 0.2954 -0.0409 -0.0639 -0.1165 780  HIS A O   
2009 C CB  . HIS A 286 ? 0.1792 0.2823 0.2696 -0.0299 -0.0514 -0.0876 780  HIS A CB  
2010 C CG  . HIS A 286 ? 0.1813 0.2771 0.2799 -0.0306 -0.0489 -0.0785 780  HIS A CG  
2011 N ND1 . HIS A 286 ? 0.1655 0.2460 0.2657 -0.0388 -0.0516 -0.0797 780  HIS A ND1 
2012 C CD2 . HIS A 286 ? 0.1368 0.2360 0.2392 -0.0257 -0.0434 -0.0684 780  HIS A CD2 
2013 C CE1 . HIS A 286 ? 0.1870 0.2627 0.2912 -0.0391 -0.0471 -0.0713 780  HIS A CE1 
2014 N NE2 . HIS A 286 ? 0.1594 0.2464 0.2660 -0.0305 -0.0423 -0.0646 780  HIS A NE2 
2015 N N   . GLU A 287 ? 0.1951 0.2972 0.2644 -0.0301 -0.0531 -0.1143 781  GLU A N   
2016 C CA  . GLU A 287 ? 0.2143 0.3214 0.2693 -0.0352 -0.0570 -0.1237 781  GLU A CA  
2017 C C   . GLU A 287 ? 0.2321 0.3232 0.2838 -0.0349 -0.0570 -0.1405 781  GLU A C   
2018 O O   . GLU A 287 ? 0.2511 0.3403 0.2902 -0.0410 -0.0617 -0.1497 781  GLU A O   
2019 C CB  . GLU A 287 ? 0.2216 0.3441 0.2617 -0.0339 -0.0530 -0.1202 781  GLU A CB  
2020 C CG  . GLU A 287 ? 0.2116 0.3476 0.2529 -0.0333 -0.0570 -0.1046 781  GLU A CG  
2021 C CD  . GLU A 287 ? 0.2223 0.3651 0.2461 -0.0310 -0.0531 -0.0982 781  GLU A CD  
2022 O OE1 . GLU A 287 ? 0.2441 0.3862 0.2473 -0.0347 -0.0508 -0.1065 781  GLU A OE1 
2023 O OE2 . GLU A 287 ? 0.2437 0.3897 0.2716 -0.0265 -0.0520 -0.0852 781  GLU A OE2 
2024 N N   . ASN A 288 ? 0.3905 0.2452 0.2582 0.0756  -0.0522 -0.0885 782  ASN A N   
2025 C CA  . ASN A 288 ? 0.4248 0.2364 0.2707 0.0794  -0.0712 -0.0968 782  ASN A CA  
2026 C C   . ASN A 288 ? 0.4264 0.2310 0.2832 0.0557  -0.0865 -0.0903 782  ASN A C   
2027 O O   . ASN A 288 ? 0.4649 0.2292 0.2995 0.0615  -0.1012 -0.0969 782  ASN A O   
2028 C CB  . ASN A 288 ? 0.4262 0.2265 0.2606 0.1057  -0.0514 -0.1066 782  ASN A CB  
2029 C CG  . ASN A 288 ? 0.3929 0.2248 0.2564 0.1011  -0.0243 -0.1026 782  ASN A CG  
2030 O OD1 . ASN A 288 ? 0.3763 0.2243 0.2614 0.0832  -0.0256 -0.0963 782  ASN A OD1 
2031 N ND2 . ASN A 288 ? 0.3706 0.2249 0.2453 0.1061  0.0003  -0.0987 782  ASN A ND2 
2032 N N   . GLY A 289 ? 0.3972 0.2385 0.2831 0.0319  -0.0833 -0.0775 783  GLY A N   
2033 C CA  . GLY A 289 ? 0.4034 0.2384 0.2968 0.0073  -0.0976 -0.0686 783  GLY A CA  
2034 C C   . GLY A 289 ? 0.3785 0.2221 0.2866 0.0119  -0.0812 -0.0679 783  GLY A C   
2035 O O   . GLY A 289 ? 0.3874 0.2225 0.2975 -0.0054 -0.0924 -0.0602 783  GLY A O   
2036 N N   . PHE A 290 ? 0.3517 0.2119 0.2685 0.0333  -0.0553 -0.0757 784  PHE A N   
2037 C CA  . PHE A 290 ? 0.3459 0.2198 0.2783 0.0370  -0.0409 -0.0776 784  PHE A CA  
2038 C C   . PHE A 290 ? 0.3337 0.2464 0.2963 0.0170  -0.0332 -0.0646 784  PHE A C   
2039 O O   . PHE A 290 ? 0.3517 0.2655 0.3210 0.0097  -0.0371 -0.0610 784  PHE A O   
2040 C CB  . PHE A 290 ? 0.3334 0.2210 0.2693 0.0585  -0.0144 -0.0891 784  PHE A CB  
2041 C CG  . PHE A 290 ? 0.3716 0.2808 0.3258 0.0612  0.0002  -0.0938 784  PHE A CG  
2042 C CD1 . PHE A 290 ? 0.3938 0.2859 0.3359 0.0714  -0.0119 -0.1012 784  PHE A CD1 
2043 C CD2 . PHE A 290 ? 0.3169 0.2621 0.2968 0.0553  0.0245  -0.0919 784  PHE A CD2 
2044 C CE1 . PHE A 290 ? 0.4000 0.3189 0.3598 0.0758  0.0004  -0.1073 784  PHE A CE1 
2045 C CE2 . PHE A 290 ? 0.3903 0.3584 0.3879 0.0562  0.0364  -0.0981 784  PHE A CE2 
2046 C CZ  . PHE A 290 ? 0.3753 0.3344 0.3649 0.0664  0.0244  -0.1060 784  PHE A CZ  
2047 N N   . MET A 291 ? 0.2726 0.2174 0.2499 0.0117  -0.0225 -0.0580 785  MET A N   
2048 C CA  . MET A 291 ? 0.2881 0.2731 0.2909 -0.0037 -0.0164 -0.0458 785  MET A CA  
2049 C C   . MET A 291 ? 0.2620 0.2454 0.2655 -0.0286 -0.0394 -0.0333 785  MET A C   
2050 O O   . MET A 291 ? 0.2555 0.2612 0.2752 -0.0406 -0.0371 -0.0240 785  MET A O   
2051 C CB  . MET A 291 ? 0.2368 0.2538 0.2470 0.0005  -0.0040 -0.0419 785  MET A CB  
2052 C CG  . MET A 291 ? 0.3365 0.3492 0.3406 0.0215  0.0212  -0.0515 785  MET A CG  
2053 S SD  . MET A 291 ? 0.2387 0.2578 0.2580 0.0241  0.0426  -0.0582 785  MET A SD  
2054 C CE  . MET A 291 ? 0.1706 0.2292 0.2143 0.0086  0.0396  -0.0452 785  MET A CE  
2055 N N   . GLU A 292 ? 0.3199 0.2752 0.3035 -0.0380 -0.0620 -0.0327 786  GLU A N   
2056 C CA  . GLU A 292 ? 0.3737 0.3198 0.3526 -0.0675 -0.0847 -0.0202 786  GLU A CA  
2057 C C   . GLU A 292 ? 0.4098 0.3126 0.3712 -0.0681 -0.0935 -0.0207 786  GLU A C   
2058 O O   . GLU A 292 ? 0.4303 0.3369 0.3952 -0.0897 -0.1004 -0.0072 786  GLU A O   
2059 C CB  . GLU A 292 ? 0.3767 0.2992 0.3352 -0.0795 -0.1080 -0.0218 786  GLU A CB  
2060 C CG  . GLU A 292 ? 0.4295 0.3531 0.3867 -0.1187 -0.1299 -0.0070 786  GLU A CG  
2061 C CD  . GLU A 292 ? 0.6159 0.5485 0.5679 -0.1353 -0.1481 -0.0077 786  GLU A CD  
2062 O OE1 . GLU A 292 ? 0.7586 0.6334 0.6774 -0.1373 -0.1697 -0.0162 786  GLU A OE1 
2063 O OE2 . GLU A 292 ? 0.6593 0.6581 0.6383 -0.1442 -0.1419 -0.0010 786  GLU A OE2 
2064 N N   . ASP A 293 ? 0.3668 0.2302 0.3067 -0.0425 -0.0931 -0.0358 787  ASP A N   
2065 C CA  . ASP A 293 ? 0.3936 0.2199 0.3137 -0.0346 -0.1006 -0.0387 787  ASP A CA  
2066 C C   . ASP A 293 ? 0.4439 0.3102 0.3914 -0.0339 -0.0826 -0.0337 787  ASP A C   
2067 O O   . ASP A 293 ? 0.4047 0.2555 0.3430 -0.0431 -0.0917 -0.0253 787  ASP A O   
2068 C CB  . ASP A 293 ? 0.4111 0.2050 0.3073 -0.0015 -0.1000 -0.0578 787  ASP A CB  
2069 C CG  . ASP A 293 ? 0.5580 0.3059 0.4207 0.0020  -0.1201 -0.0643 787  ASP A CG  
2070 O OD1 . ASP A 293 ? 0.6530 0.3715 0.4985 -0.0232 -0.1429 -0.0550 787  ASP A OD1 
2071 O OD2 . ASP A 293 ? 0.5643 0.3065 0.4168 0.0288  -0.1131 -0.0788 787  ASP A OD2 
2072 N N   . LEU A 294 ? 0.3589 0.2723 0.3359 -0.0225 -0.0576 -0.0391 788  LEU A N   
2073 C CA  . LEU A 294 ? 0.3631 0.3159 0.3660 -0.0224 -0.0412 -0.0359 788  LEU A CA  
2074 C C   . LEU A 294 ? 0.3487 0.3250 0.3637 -0.0482 -0.0469 -0.0163 788  LEU A C   
2075 O O   . LEU A 294 ? 0.3891 0.3755 0.4097 -0.0513 -0.0454 -0.0102 788  LEU A O   
2076 C CB  . LEU A 294 ? 0.2874 0.2783 0.3136 -0.0103 -0.0151 -0.0444 788  LEU A CB  
2077 C CG  . LEU A 294 ? 0.2964 0.2775 0.3165 0.0122  -0.0031 -0.0629 788  LEU A CG  
2078 C CD1 . LEU A 294 ? 0.2955 0.3090 0.3352 0.0168  0.0235  -0.0684 788  LEU A CD1 
2079 C CD2 . LEU A 294 ? 0.2713 0.2444 0.2859 0.0240  -0.0073 -0.0716 788  LEU A CD2 
2080 N N   . ASP A 295 ? 0.3279 0.3184 0.3469 -0.0660 -0.0534 -0.0065 789  ASP A N   
2081 C CA  . ASP A 295 ? 0.3828 0.4046 0.4140 -0.0929 -0.0590 0.0129  789  ASP A CA  
2082 C C   . ASP A 295 ? 0.4670 0.4447 0.4727 -0.1128 -0.0800 0.0234  789  ASP A C   
2083 O O   . ASP A 295 ? 0.5095 0.5061 0.5216 -0.1297 -0.0801 0.0387  789  ASP A O   
2084 C CB  . ASP A 295 ? 0.5141 0.5672 0.5546 -0.1064 -0.0628 0.0187  789  ASP A CB  
2085 C CG  . ASP A 295 ? 0.6101 0.7312 0.6782 -0.1184 -0.0534 0.0331  789  ASP A CG  
2086 O OD1 . ASP A 295 ? 0.3712 0.5255 0.4561 -0.0993 -0.0333 0.0292  789  ASP A OD1 
2087 O OD2 . ASP A 295 ? 0.6079 0.7505 0.6793 -0.1471 -0.0661 0.0480  789  ASP A OD2 
2088 N N   . LYS A 296 ? 0.4432 0.3574 0.4146 -0.1099 -0.0981 0.0156  790  LYS A N   
2089 C CA  . LYS A 296 ? 0.4858 0.3416 0.4212 -0.1250 -0.1191 0.0242  790  LYS A CA  
2090 C C   . LYS A 296 ? 0.4938 0.3320 0.4185 -0.1024 -0.1135 0.0195  790  LYS A C   
2091 O O   . LYS A 296 ? 0.6041 0.4166 0.5088 -0.1157 -0.1229 0.0326  790  LYS A O   
2092 C CB  . LYS A 296 ? 0.5371 0.3226 0.4311 -0.1246 -0.1423 0.0154  790  LYS A CB  
2093 C CG  . LYS A 296 ? 0.5993 0.3846 0.4905 -0.1583 -0.1584 0.0237  790  LYS A CG  
2094 C CD  . LYS A 296 ? 0.6331 0.4024 0.5149 -0.1410 -0.1640 0.0065  790  LYS A CD  
2095 C CE  . LYS A 296 ? 0.7530 0.5534 0.6480 -0.1700 -0.1735 0.0128  790  LYS A CE  
2096 N NZ  . LYS A 296 ? 0.6530 0.4412 0.5349 -0.2068 -0.1871 0.0308  790  LYS A NZ  
2097 N N   . THR A 297 ? 0.4567 0.3091 0.3925 -0.0689 -0.0986 0.0009  791  THR A N   
2098 C CA  . THR A 297 ? 0.4574 0.3000 0.3838 -0.0449 -0.0949 -0.0072 791  THR A CA  
2099 C C   . THR A 297 ? 0.3974 0.2915 0.3530 -0.0506 -0.0799 0.0026  791  THR A C   
2100 O O   . THR A 297 ? 0.4198 0.2973 0.3587 -0.0454 -0.0851 0.0071  791  THR A O   
2101 C CB  . THR A 297 ? 0.4653 0.3177 0.3980 -0.0113 -0.0829 -0.0307 791  THR A CB  
2102 O OG1 . THR A 297 ? 0.5349 0.3374 0.4351 -0.0016 -0.0980 -0.0400 791  THR A OG1 
2103 C CG2 . THR A 297 ? 0.4941 0.3502 0.4216 0.0143  -0.0791 -0.0414 791  THR A CG2 
2104 N N   . TRP A 298 ? 0.3926 0.3464 0.3869 -0.0584 -0.0623 0.0058  792  TRP A N   
2105 C CA  . TRP A 298 ? 0.3278 0.3330 0.3496 -0.0558 -0.0460 0.0099  792  TRP A CA  
2106 C C   . TRP A 298 ? 0.3543 0.3969 0.3914 -0.0821 -0.0448 0.0318  792  TRP A C   
2107 O O   . TRP A 298 ? 0.3148 0.3849 0.3611 -0.0823 -0.0383 0.0400  792  TRP A O   
2108 C CB  . TRP A 298 ? 0.3069 0.3520 0.3572 -0.0374 -0.0242 -0.0070 792  TRP A CB  
2109 C CG  . TRP A 298 ? 0.2761 0.3028 0.3184 -0.0127 -0.0211 -0.0286 792  TRP A CG  
2110 C CD1 . TRP A 298 ? 0.3104 0.3213 0.3467 -0.0022 -0.0188 -0.0420 792  TRP A CD1 
2111 C CD2 . TRP A 298 ? 0.2209 0.2507 0.2605 0.0060  -0.0198 -0.0396 792  TRP A CD2 
2112 N NE1 . TRP A 298 ? 0.2831 0.2911 0.3147 0.0204  -0.0152 -0.0602 792  TRP A NE1 
2113 C CE2 . TRP A 298 ? 0.2702 0.2913 0.3045 0.0262  -0.0164 -0.0600 792  TRP A CE2 
2114 C CE3 . TRP A 298 ? 0.2278 0.2706 0.2680 0.0091  -0.0212 -0.0346 792  TRP A CE3 
2115 C CZ2 . TRP A 298 ? 0.2266 0.2580 0.2590 0.0488  -0.0149 -0.0764 792  TRP A CZ2 
2116 C CZ3 . TRP A 298 ? 0.2406 0.2880 0.2767 0.0330  -0.0206 -0.0513 792  TRP A CZ3 
2117 C CH2 . TRP A 298 ? 0.2875 0.3321 0.3210 0.0523  -0.0177 -0.0725 792  TRP A CH2 
2118 N N   . VAL A 299 ? 0.3638 0.4138 0.4038 -0.1029 -0.0508 0.0408  793  VAL A N   
2119 C CA  . VAL A 299 ? 0.4337 0.5390 0.4951 -0.1245 -0.0463 0.0589  793  VAL A CA  
2120 C C   . VAL A 299 ? 0.5158 0.6024 0.5587 -0.1600 -0.0644 0.0800  793  VAL A C   
2121 O O   . VAL A 299 ? 0.5536 0.6663 0.6006 -0.1749 -0.0621 0.0975  793  VAL A O   
2122 C CB  . VAL A 299 ? 0.4515 0.5952 0.5329 -0.1210 -0.0381 0.0535  793  VAL A CB  
2123 C CG1 . VAL A 299 ? 0.3674 0.5762 0.4692 -0.1398 -0.0351 0.0713  793  VAL A CG1 
2124 C CG2 . VAL A 299 ? 0.3063 0.4629 0.4006 -0.0903 -0.0185 0.0352  793  VAL A CG2 
2125 N N   . ARG A 300 ? 0.7537 0.7937 0.7738 -0.1753 -0.0825 0.0789  794  ARG A N   
2126 C CA  . ARG A 300 ? 0.8176 0.8388 0.8194 -0.2164 -0.1007 0.0983  794  ARG A CA  
2127 C C   . ARG A 300 ? 0.8682 0.7967 0.8198 -0.2197 -0.1195 0.0988  794  ARG A C   
2128 O O   . ARG A 300 ? 1.0146 0.8833 0.9382 -0.2130 -0.1344 0.0861  794  ARG A O   
2129 C CB  . ARG A 300 ? 0.8220 0.8579 0.8292 -0.2292 -0.1081 0.0952  794  ARG A CB  
2130 C CG  . ARG A 300 ? 0.8033 0.9236 0.8477 -0.2172 -0.0896 0.0939  794  ARG A CG  
2131 C CD  . ARG A 300 ? 0.8939 1.0192 0.9406 -0.2171 -0.0965 0.0838  794  ARG A CD  
2132 N NE  . ARG A 300 ? 0.9285 0.9820 0.9495 -0.2157 -0.1137 0.0706  794  ARG A NE  
2133 C CZ  . ARG A 300 ? 0.8868 0.9338 0.9065 -0.2033 -0.1180 0.0559  794  ARG A CZ  
2134 N NH1 . ARG A 300 ? 0.8885 0.9982 0.9335 -0.1969 -0.1089 0.0538  794  ARG A NH1 
2135 N NH2 . ARG A 300 ? 0.8679 0.8424 0.8551 -0.1901 -0.1301 0.0422  794  ARG A NH2 
2136 N N   . TYR A 301 ? 0.8039 0.7180 0.7394 -0.2272 -0.1196 0.1135  795  TYR A N   
2137 C CA  . TYR A 301 ? 0.9068 0.7274 0.7853 -0.2333 -0.1393 0.1182  795  TYR A CA  
2138 C C   . TYR A 301 ? 0.8593 0.6775 0.7222 -0.2587 -0.1391 0.1440  795  TYR A C   
2139 O O   . TYR A 301 ? 0.9066 0.8024 0.8040 -0.2735 -0.1253 0.1567  795  TYR A O   
2140 C CB  . TYR A 301 ? 0.9682 0.7436 0.8251 -0.1856 -0.1394 0.0958  795  TYR A CB  
2141 C CG  . TYR A 301 ? 0.9527 0.7787 0.8373 -0.1531 -0.1187 0.0883  795  TYR A CG  
2142 C CD1 . TYR A 301 ? 0.7950 0.6504 0.7052 -0.1179 -0.1055 0.0644  795  TYR A CD1 
2143 C CD2 . TYR A 301 ? 0.9395 0.7803 0.8209 -0.1583 -0.1130 0.1045  795  TYR A CD2 
2144 C CE1 . TYR A 301 ? 0.7431 0.6430 0.6775 -0.0921 -0.0883 0.0557  795  TYR A CE1 
2145 C CE2 . TYR A 301 ? 0.8974 0.7834 0.8025 -0.1281 -0.0962 0.0954  795  TYR A CE2 
2146 C CZ  . TYR A 301 ? 0.7848 0.6999 0.7168 -0.0964 -0.0846 0.0703  795  TYR A CZ  
2147 O OH  . TYR A 301 ? 0.7234 0.6825 0.6782 -0.0704 -0.0694 0.0598  795  TYR A OH  
2148 N N   . ASP B 17  ? 0.9449 0.5716 0.9259 0.0126  -0.1322 0.0053  403  ASP B N   
2149 C CA  . ASP B 17  ? 1.0906 0.7174 1.0943 -0.0056 -0.1400 -0.0048 403  ASP B CA  
2150 C C   . ASP B 17  ? 0.9402 0.5894 0.9454 0.0040  -0.1527 -0.0262 403  ASP B C   
2151 O O   . ASP B 17  ? 0.8505 0.5251 0.8725 -0.0034 -0.1564 -0.0309 403  ASP B O   
2152 C CB  . ASP B 17  ? 1.1149 0.7060 1.1199 -0.0162 -0.1413 -0.0071 403  ASP B CB  
2153 C CG  . ASP B 17  ? 1.2650 0.8577 1.2994 -0.0434 -0.1437 -0.0067 403  ASP B CG  
2154 O OD1 . ASP B 17  ? 1.2492 0.8585 1.3018 -0.0566 -0.1346 0.0095  403  ASP B OD1 
2155 O OD2 . ASP B 17  ? 1.2307 0.8103 1.2702 -0.0513 -0.1541 -0.0219 403  ASP B OD2 
2156 N N   . ASN B 18  ? 0.9084 0.5492 0.8957 0.0217  -0.1579 -0.0382 404  ASN B N   
2157 C CA  . ASN B 18  ? 0.6615 0.3257 0.6443 0.0370  -0.1657 -0.0555 404  ASN B CA  
2158 C C   . ASN B 18  ? 0.6689 0.3574 0.6409 0.0566  -0.1602 -0.0507 404  ASN B C   
2159 O O   . ASN B 18  ? 0.5925 0.3046 0.5615 0.0706  -0.1633 -0.0619 404  ASN B O   
2160 C CB  . ASN B 18  ? 0.8025 0.4454 0.7723 0.0450  -0.1735 -0.0705 404  ASN B CB  
2161 C CG  . ASN B 18  ? 0.8009 0.4662 0.7695 0.0542  -0.1821 -0.0891 404  ASN B CG  
2162 O OD1 . ASN B 18  ? 0.8073 0.4801 0.7888 0.0407  -0.1894 -0.0981 404  ASN B OD1 
2163 N ND2 . ASN B 18  ? 0.7345 0.4135 0.6882 0.0773  -0.1804 -0.0937 404  ASN B ND2 
2164 N N   . HIS B 19  ? 0.6889 0.3745 0.6549 0.0574  -0.1514 -0.0337 405  HIS B N   
2165 C CA  . HIS B 19  ? 0.5975 0.3089 0.5556 0.0714  -0.1465 -0.0278 405  HIS B CA  
2166 C C   . HIS B 19  ? 0.5813 0.3102 0.5462 0.0623  -0.1403 -0.0167 405  HIS B C   
2167 O O   . HIS B 19  ? 0.6842 0.3980 0.6478 0.0514  -0.1336 -0.0022 405  HIS B O   
2168 C CB  . HIS B 19  ? 0.4874 0.1836 0.4308 0.0798  -0.1424 -0.0180 405  HIS B CB  
2169 C CG  . HIS B 19  ? 0.4524 0.1770 0.3906 0.0920  -0.1396 -0.0139 405  HIS B CG  
2170 N ND1 . HIS B 19  ? 0.5369 0.2858 0.4767 0.1053  -0.1419 -0.0236 405  HIS B ND1 
2171 C CD2 . HIS B 19  ? 0.4963 0.2292 0.4281 0.0915  -0.1343 -0.0011 405  HIS B CD2 
2172 C CE1 . HIS B 19  ? 0.5586 0.3305 0.4974 0.1102  -0.1383 -0.0168 405  HIS B CE1 
2173 N NE2 . HIS B 19  ? 0.5953 0.3571 0.5280 0.1023  -0.1351 -0.0042 405  HIS B NE2 
2174 N N   . LEU B 20  ? 0.4654 0.2259 0.4359 0.0679  -0.1405 -0.0224 406  LEU B N   
2175 C CA  . LEU B 20  ? 0.4502 0.2343 0.4280 0.0576  -0.1320 -0.0144 406  LEU B CA  
2176 C C   . LEU B 20  ? 0.4627 0.2614 0.4289 0.0649  -0.1265 -0.0048 406  LEU B C   
2177 O O   . LEU B 20  ? 0.3780 0.1916 0.3393 0.0755  -0.1275 -0.0094 406  LEU B O   
2178 C CB  . LEU B 20  ? 0.4394 0.2552 0.4305 0.0561  -0.1323 -0.0269 406  LEU B CB  
2179 C CG  . LEU B 20  ? 0.4904 0.2950 0.4909 0.0507  -0.1420 -0.0410 406  LEU B CG  
2180 C CD1 . LEU B 20  ? 0.4161 0.2559 0.4283 0.0483  -0.1416 -0.0501 406  LEU B CD1 
2181 C CD2 . LEU B 20  ? 0.5304 0.3060 0.5386 0.0324  -0.1426 -0.0333 406  LEU B CD2 
2182 N N   . SER B 21  ? 0.4433 0.2459 0.4059 0.0549  -0.1164 0.0081  407  SER B N   
2183 C CA  . SER B 21  ? 0.4019 0.2168 0.3508 0.0592  -0.1115 0.0157  407  SER B CA  
2184 C C   . SER B 21  ? 0.3989 0.2480 0.3561 0.0581  -0.1053 0.0101  407  SER B C   
2185 O O   . SER B 21  ? 0.3666 0.2266 0.3327 0.0491  -0.0973 0.0122  407  SER B O   
2186 C CB  . SER B 21  ? 0.3431 0.1396 0.2768 0.0520  -0.1023 0.0324  407  SER B CB  
2187 O OG  . SER B 21  ? 0.3630 0.1748 0.2829 0.0528  -0.0948 0.0368  407  SER B OG  
2188 N N   . ILE B 22  ? 0.3653 0.2331 0.3211 0.0670  -0.1078 0.0040  408  ILE B N   
2189 C CA  . ILE B 22  ? 0.3278 0.2248 0.2904 0.0685  -0.1022 -0.0011 408  ILE B CA  
2190 C C   . ILE B 22  ? 0.3107 0.2170 0.2620 0.0666  -0.0951 0.0037  408  ILE B C   
2191 O O   . ILE B 22  ? 0.3520 0.2574 0.3003 0.0680  -0.0980 0.0032  408  ILE B O   
2192 C CB  . ILE B 22  ? 0.3270 0.2429 0.3025 0.0757  -0.1044 -0.0151 408  ILE B CB  
2193 C CG1 . ILE B 22  ? 0.3411 0.2431 0.3248 0.0771  -0.1138 -0.0226 408  ILE B CG1 
2194 C CG2 . ILE B 22  ? 0.2680 0.2131 0.2485 0.0765  -0.0947 -0.0184 408  ILE B CG2 
2195 C CD1 . ILE B 22  ? 0.2848 0.2019 0.2747 0.0863  -0.1162 -0.0372 408  ILE B CD1 
2196 N N   . VAL B 23  ? 0.2515 0.1657 0.1967 0.0639  -0.0867 0.0083  409  VAL B N   
2197 C CA  . VAL B 23  ? 0.3027 0.2197 0.2347 0.0614  -0.0810 0.0118  409  VAL B CA  
2198 C C   . VAL B 23  ? 0.2962 0.2387 0.2389 0.0641  -0.0759 0.0054  409  VAL B C   
2199 O O   . VAL B 23  ? 0.2608 0.2189 0.2149 0.0677  -0.0722 0.0007  409  VAL B O   
2200 C CB  . VAL B 23  ? 0.3089 0.2094 0.2192 0.0571  -0.0719 0.0229  409  VAL B CB  
2201 C CG1 . VAL B 23  ? 0.2549 0.1706 0.1727 0.0564  -0.0602 0.0241  409  VAL B CG1 
2202 C CG2 . VAL B 23  ? 0.2988 0.1939 0.1909 0.0539  -0.0685 0.0245  409  VAL B CG2 
2203 N N   . THR B 24  ? 0.2739 0.2204 0.2131 0.0624  -0.0761 0.0054  410  THR B N   
2204 C CA  . THR B 24  ? 0.2233 0.1900 0.1711 0.0646  -0.0706 0.0022  410  THR B CA  
2205 C C   . THR B 24  ? 0.2574 0.2143 0.1885 0.0598  -0.0711 0.0065  410  THR B C   
2206 O O   . THR B 24  ? 0.2801 0.2155 0.1923 0.0547  -0.0747 0.0107  410  THR B O   
2207 C CB  . THR B 24  ? 0.2369 0.2227 0.2063 0.0687  -0.0731 -0.0039 410  THR B CB  
2208 O OG1 . THR B 24  ? 0.1644 0.1694 0.1420 0.0716  -0.0654 -0.0052 410  THR B OG1 
2209 C CG2 . THR B 24  ? 0.1971 0.1798 0.1691 0.0668  -0.0826 -0.0020 410  THR B CG2 
2210 N N   . LEU B 25  ? 0.2096 0.1805 0.1460 0.0617  -0.0673 0.0054  411  LEU B N   
2211 C CA  . LEU B 25  ? 0.2468 0.2059 0.1668 0.0552  -0.0676 0.0083  411  LEU B CA  
2212 C C   . LEU B 25  ? 0.2528 0.2355 0.1948 0.0554  -0.0659 0.0063  411  LEU B C   
2213 O O   . LEU B 25  ? 0.1858 0.1894 0.1435 0.0636  -0.0567 0.0046  411  LEU B O   
2214 C CB  . LEU B 25  ? 0.2356 0.1773 0.1304 0.0533  -0.0525 0.0124  411  LEU B CB  
2215 C CG  . LEU B 25  ? 0.2254 0.1536 0.1035 0.0467  -0.0464 0.0137  411  LEU B CG  
2216 C CD1 . LEU B 25  ? 0.2554 0.1557 0.1096 0.0379  -0.0591 0.0141  411  LEU B CD1 
2217 C CD2 . LEU B 25  ? 0.2525 0.1713 0.1117 0.0508  -0.0273 0.0179  411  LEU B CD2 
2218 N N   . GLU B 26  ? 0.2427 0.2224 0.1860 0.0465  -0.0749 0.0071  412  GLU B N   
2219 C CA  . GLU B 26  ? 0.2045 0.2093 0.1747 0.0448  -0.0739 0.0073  412  GLU B CA  
2220 C C   . GLU B 26  ? 0.2253 0.2267 0.1885 0.0417  -0.0565 0.0095  412  GLU B C   
2221 O O   . GLU B 26  ? 0.2158 0.1895 0.1525 0.0329  -0.0533 0.0106  412  GLU B O   
2222 C CB  . GLU B 26  ? 0.2072 0.2130 0.1855 0.0341  -0.0913 0.0080  412  GLU B CB  
2223 C CG  . GLU B 26  ? 0.1995 0.2332 0.2099 0.0294  -0.0891 0.0105  412  GLU B CG  
2224 C CD  . GLU B 26  ? 0.2121 0.2564 0.2400 0.0191  -0.1092 0.0115  412  GLU B CD  
2225 O OE1 . GLU B 26  ? 0.3471 0.3674 0.3516 0.0118  -0.1243 0.0095  412  GLU B OE1 
2226 O OE2 . GLU B 26  ? 0.2061 0.2844 0.2714 0.0193  -0.1097 0.0152  412  GLU B OE2 
2227 N N   . GLU B 27  ? 0.1764 0.2033 0.1602 0.0508  -0.0445 0.0104  413  GLU B N   
2228 C CA  . GLU B 27  ? 0.1759 0.2027 0.1573 0.0493  -0.0275 0.0142  413  GLU B CA  
2229 C C   . GLU B 27  ? 0.1582 0.2199 0.1707 0.0595  -0.0200 0.0162  413  GLU B C   
2230 O O   . GLU B 27  ? 0.1441 0.2199 0.1591 0.0750  -0.0136 0.0140  413  GLU B O   
2231 C CB  . GLU B 27  ? 0.1777 0.1882 0.1324 0.0558  -0.0129 0.0149  413  GLU B CB  
2232 C CG  . GLU B 27  ? 0.2037 0.2116 0.1527 0.0570  0.0060  0.0200  413  GLU B CG  
2233 C CD  . GLU B 27  ? 0.2481 0.2325 0.1650 0.0611  0.0189  0.0222  413  GLU B CD  
2234 O OE1 . GLU B 27  ? 0.2770 0.2635 0.1863 0.0689  0.0180  0.0207  413  GLU B OE1 
2235 O OE2 . GLU B 27  ? 0.2780 0.2418 0.1781 0.0566  0.0304  0.0263  413  GLU B OE2 
2236 N N   . ALA B 28  ? 0.1624 0.2374 0.1977 0.0510  -0.0211 0.0206  414  ALA B N   
2237 C CA  . ALA B 28  ? 0.1630 0.2721 0.2286 0.0617  -0.0117 0.0250  414  ALA B CA  
2238 C C   . ALA B 28  ? 0.1677 0.2775 0.2223 0.0727  0.0107  0.0283  414  ALA B C   
2239 O O   . ALA B 28  ? 0.2128 0.2984 0.2451 0.0659  0.0200  0.0305  414  ALA B O   
2240 C CB  . ALA B 28  ? 0.1566 0.2812 0.2522 0.0476  -0.0156 0.0316  414  ALA B CB  
2241 N N   . PRO B 29  ? 0.1338 0.2691 0.2004 0.0918  0.0198  0.0289  415  PRO B N   
2242 C CA  . PRO B 29  ? 0.1790 0.3280 0.2609 0.0961  0.0114  0.0246  415  PRO B CA  
2243 C C   . PRO B 29  ? 0.1728 0.3026 0.2332 0.0971  0.0020  0.0138  415  PRO B C   
2244 O O   . PRO B 29  ? 0.1369 0.2677 0.2009 0.0998  -0.0013 0.0100  415  PRO B O   
2245 C CB  . PRO B 29  ? 0.1863 0.3411 0.2698 0.0999  0.0268  0.0284  415  PRO B CB  
2246 C CG  . PRO B 29  ? 0.1538 0.2893 0.2078 0.1005  0.0371  0.0286  415  PRO B CG  
2247 C CD  . PRO B 29  ? 0.1646 0.2924 0.2133 0.0974  0.0376  0.0311  415  PRO B CD  
2248 N N   . PHE B 30  ? 0.1289 0.2418 0.1682 0.0954  -0.0009 0.0104  416  PHE B N   
2249 C CA  . PHE B 30  ? 0.1769 0.2758 0.2003 0.0947  -0.0069 0.0023  416  PHE B CA  
2250 C C   . PHE B 30  ? 0.1570 0.2499 0.1867 0.0917  -0.0223 -0.0010 416  PHE B C   
2251 O O   . PHE B 30  ? 0.2174 0.3051 0.2449 0.0929  -0.0265 -0.0062 416  PHE B O   
2252 C CB  . PHE B 30  ? 0.2079 0.2943 0.2089 0.0937  -0.0019 0.0018  416  PHE B CB  
2253 C CG  . PHE B 30  ? 0.2279 0.3160 0.2191 0.0954  0.0111  0.0066  416  PHE B CG  
2254 C CD1 . PHE B 30  ? 0.2139 0.3044 0.1988 0.0977  0.0120  0.0045  416  PHE B CD1 
2255 C CD2 . PHE B 30  ? 0.1594 0.2438 0.1459 0.0955  0.0214  0.0142  416  PHE B CD2 
2256 C CE1 . PHE B 30  ? 0.1753 0.2654 0.1510 0.0996  0.0200  0.0105  416  PHE B CE1 
2257 C CE2 . PHE B 30  ? 0.1785 0.2595 0.1562 0.0960  0.0312  0.0201  416  PHE B CE2 
2258 C CZ  . PHE B 30  ? 0.1957 0.2804 0.1691 0.0982  0.0290  0.0185  416  PHE B CZ  
2259 N N   . VAL B 31  ? 0.1318 0.2232 0.1659 0.0879  -0.0323 0.0027  417  VAL B N   
2260 C CA  . VAL B 31  ? 0.1766 0.2603 0.2141 0.0831  -0.0482 0.0015  417  VAL B CA  
2261 C C   . VAL B 31  ? 0.1945 0.2919 0.2492 0.0789  -0.0592 0.0069  417  VAL B C   
2262 O O   . VAL B 31  ? 0.1648 0.2496 0.2090 0.0666  -0.0581 0.0096  417  VAL B O   
2263 C CB  . VAL B 31  ? 0.1448 0.2033 0.1592 0.0785  -0.0551 -0.0006 417  VAL B CB  
2264 C CG1 . VAL B 31  ? 0.1574 0.2060 0.1727 0.0734  -0.0692 -0.0003 417  VAL B CG1 
2265 C CG2 . VAL B 31  ? 0.1408 0.1927 0.1453 0.0813  -0.0468 -0.0056 417  VAL B CG2 
2266 N N   . ILE B 32  ? 0.1731 0.2849 0.2496 0.0789  -0.0643 0.0092  418  ILE B N   
2267 C CA  . ILE B 32  ? 0.1465 0.2784 0.2468 0.0729  -0.0765 0.0144  418  ILE B CA  
2268 C C   . ILE B 32  ? 0.2084 0.3321 0.3060 0.0688  -0.0904 0.0152  418  ILE B C   
2269 O O   . ILE B 32  ? 0.2619 0.3802 0.3566 0.0756  -0.0862 0.0145  418  ILE B O   
2270 C CB  . ILE B 32  ? 0.1669 0.3303 0.3003 0.0779  -0.0656 0.0203  418  ILE B CB  
2271 C CG1 . ILE B 32  ? 0.2004 0.3705 0.3308 0.0822  -0.0462 0.0222  418  ILE B CG1 
2272 C CG2 . ILE B 32  ? 0.1428 0.3340 0.3084 0.0685  -0.0790 0.0269  418  ILE B CG2 
2273 C CD1 . ILE B 32  ? 0.1537 0.3438 0.3059 0.0879  -0.0309 0.0265  418  ILE B CD1 
2274 N N   . VAL B 33  ? 0.2476 0.3674 0.3433 0.0573  -0.1070 0.0157  419  VAL B N   
2275 C CA  . VAL B 33  ? 0.1889 0.2999 0.2755 0.0544  -0.1184 0.0161  419  VAL B CA  
2276 C C   . VAL B 33  ? 0.1987 0.3418 0.3152 0.0509  -0.1277 0.0212  419  VAL B C   
2277 O O   . VAL B 33  ? 0.2165 0.3740 0.3528 0.0398  -0.1335 0.0225  419  VAL B O   
2278 C CB  . VAL B 33  ? 0.2152 0.2897 0.2677 0.0440  -0.1285 0.0123  419  VAL B CB  
2279 C CG1 . VAL B 33  ? 0.2934 0.3603 0.3370 0.0436  -0.1386 0.0131  419  VAL B CG1 
2280 C CG2 . VAL B 33  ? 0.2013 0.2495 0.2272 0.0485  -0.1175 0.0089  419  VAL B CG2 
2281 N N   . GLU B 34  ? 0.1995 0.3534 0.3217 0.0590  -0.1294 0.0249  420  GLU B N   
2282 C CA  . GLU B 34  ? 0.2397 0.4273 0.3883 0.0587  -0.1383 0.0296  420  GLU B CA  
2283 C C   . GLU B 34  ? 0.3126 0.4885 0.4461 0.0597  -0.1504 0.0301  420  GLU B C   
2284 O O   . GLU B 34  ? 0.2922 0.4376 0.3998 0.0642  -0.1483 0.0280  420  GLU B O   
2285 C CB  . GLU B 34  ? 0.2345 0.4567 0.4115 0.0727  -0.1251 0.0384  420  GLU B CB  
2286 C CG  . GLU B 34  ? 0.2929 0.5238 0.4829 0.0741  -0.1089 0.0387  420  GLU B CG  
2287 C CD  . GLU B 34  ? 0.3020 0.5229 0.5320 0.0835  -0.1075 0.0347  420  GLU B CD  
2288 O OE1 . GLU B 34  ? 0.2725 0.4898 0.4983 0.0921  -0.1051 0.0427  420  GLU B OE1 
2289 O OE2 . GLU B 34  ? 0.3701 0.6192 0.6191 0.0893  -0.0985 0.0284  420  GLU B OE2 
2290 N N   . ASP B 35  ? 0.3112 0.6224 0.3203 0.0160  -0.0529 0.0918  421  ASP B N   
2291 C CA  . ASP B 35  ? 0.3947 0.7058 0.3975 0.0429  -0.0525 0.0867  421  ASP B CA  
2292 C C   . ASP B 35  ? 0.3912 0.7124 0.3733 0.0825  -0.0493 0.0791  421  ASP B C   
2293 O O   . ASP B 35  ? 0.4040 0.7335 0.3766 0.0887  -0.0473 0.0769  421  ASP B O   
2294 C CB  . ASP B 35  ? 0.4022 0.7622 0.4236 0.0323  -0.0486 0.0876  421  ASP B CB  
2295 C CG  . ASP B 35  ? 0.4612 0.7998 0.4963 -0.0014 -0.0522 0.0920  421  ASP B CG  
2296 O OD1 . ASP B 35  ? 0.4305 0.7212 0.4604 -0.0014 -0.0580 0.0914  421  ASP B OD1 
2297 O OD2 . ASP B 35  ? 0.5933 0.9609 0.6403 -0.0275 -0.0488 0.0960  421  ASP B OD2 
2298 N N   . ILE B 36  ? 0.5109 0.8282 0.4821 0.1112  -0.0495 0.0741  422  ILE B N   
2299 C CA  . ILE B 36  ? 0.5515 0.8724 0.5002 0.1530  -0.0471 0.0644  422  ILE B CA  
2300 C C   . ILE B 36  ? 0.5954 0.9516 0.5447 0.1768  -0.0453 0.0592  422  ILE B C   
2301 O O   . ILE B 36  ? 0.6397 1.0421 0.5845 0.2043  -0.0404 0.0500  422  ILE B O   
2302 C CB  . ILE B 36  ? 0.5173 0.7529 0.4315 0.1725  -0.0528 0.0614  422  ILE B CB  
2303 C CG1 . ILE B 36  ? 0.6235 0.8585 0.5120 0.2124  -0.0507 0.0489  422  ILE B CG1 
2304 C CG2 . ILE B 36  ? 0.5272 0.7113 0.4260 0.1796  -0.0568 0.0646  422  ILE B CG2 
2305 C CD1 . ILE B 36  ? 0.5636 0.8688 0.4655 0.2101  -0.0443 0.0452  422  ILE B CD1 
2306 N N   . GLU B 41  ? 0.7755 0.9991 0.5994 0.3257  -0.0547 0.0253  427  GLU B N   
2307 C CA  . GLU B 41  ? 0.8512 1.0004 0.6691 0.2974  -0.0577 0.0363  427  GLU B CA  
2308 C C   . GLU B 41  ? 0.9573 1.0441 0.7471 0.3061  -0.0589 0.0297  427  GLU B C   
2309 O O   . GLU B 41  ? 1.0991 1.0964 0.8555 0.3079  -0.0626 0.0307  427  GLU B O   
2310 C CB  . GLU B 41  ? 0.8664 0.9539 0.6611 0.2991  -0.0627 0.0435  427  GLU B CB  
2311 N N   . THR B 42  ? 0.8103 0.9443 0.6118 0.3092  -0.0554 0.0226  428  THR B N   
2312 C CA  . THR B 42  ? 0.7637 0.8459 0.5385 0.3194  -0.0579 0.0137  428  THR B CA  
2313 C C   . THR B 42  ? 0.7692 0.9071 0.5708 0.2964  -0.0552 0.0165  428  THR B C   
2314 O O   . THR B 42  ? 0.8592 1.0832 0.6802 0.3019  -0.0484 0.0132  428  THR B O   
2315 C CB  . THR B 42  ? 0.8057 0.8784 0.5445 0.3659  -0.0585 -0.0045 428  THR B CB  
2316 O OG1 . THR B 42  ? 0.9946 1.1611 0.7516 0.3837  -0.0532 -0.0093 428  THR B OG1 
2317 C CG2 . THR B 42  ? 0.9186 0.8965 0.6135 0.3820  -0.0649 -0.0068 428  THR B CG2 
2318 N N   . CYS B 43  ? 0.7100 0.7977 0.5116 0.2654  -0.0584 0.0210  429  CYS B N   
2319 C CA  . CYS B 43  ? 0.6141 0.7391 0.4365 0.2343  -0.0545 0.0218  429  CYS B CA  
2320 C C   . CYS B 43  ? 0.6742 0.8244 0.4770 0.2612  -0.0513 0.0069  429  CYS B C   
2321 O O   . CYS B 43  ? 0.7526 0.8537 0.5207 0.2954  -0.0546 -0.0080 429  CYS B O   
2322 C CB  . CYS B 43  ? 0.5516 0.6089 0.3762 0.1978  -0.0582 0.0231  429  CYS B CB  
2323 S SG  . CYS B 43  ? 0.4374 0.4767 0.2888 0.1622  -0.0595 0.0385  429  CYS B SG  
2324 N N   . VAL B 44  ? 0.6693 0.8935 0.4908 0.2448  -0.0447 0.0107  430  VAL B N   
2325 C CA  . VAL B 44  ? 0.6999 0.9709 0.5052 0.2701  -0.0382 -0.0022 430  VAL B CA  
2326 C C   . VAL B 44  ? 0.6449 0.9183 0.4481 0.2385  -0.0365 0.0001  430  VAL B C   
2327 O O   . VAL B 44  ? 0.6879 0.9419 0.5082 0.1982  -0.0404 0.0132  430  VAL B O   
2328 C CB  . VAL B 44  ? 0.7275 1.1069 0.5537 0.2863  -0.0289 -0.0002 430  VAL B CB  
2329 C CG1 . VAL B 44  ? 0.7145 1.0928 0.5365 0.3282  -0.0338 -0.0060 430  VAL B CG1 
2330 C CG2 . VAL B 44  ? 0.7032 1.1400 0.5674 0.2394  -0.0244 0.0197  430  VAL B CG2 
2331 N N   . ARG B 45  ? 0.7466 1.0434 0.5253 0.2607  -0.0315 -0.0140 431  ARG B N   
2332 C CA  . ARG B 45  ? 0.7141 1.0305 0.4833 0.2376  -0.0282 -0.0118 431  ARG B CA  
2333 C C   . ARG B 45  ? 0.6944 0.9272 0.4565 0.2109  -0.0414 -0.0109 431  ARG B C   
2334 O O   . ARG B 45  ? 0.7248 0.8838 0.4698 0.2260  -0.0502 -0.0250 431  ARG B O   
2335 C CB  . ARG B 45  ? 0.7272 1.1309 0.5235 0.2077  -0.0173 0.0076  431  ARG B CB  
2336 C CG  . ARG B 45  ? 0.7157 1.2121 0.5273 0.2324  -0.0039 0.0033  431  ARG B CG  
2337 C CD  . ARG B 45  ? 0.6934 1.2696 0.5298 0.1987  0.0096  0.0166  431  ARG B CD  
2338 N NE  . ARG B 45  ? 0.7221 1.3209 0.5393 0.2100  0.0174  0.0060  431  ARG B NE  
2339 C CZ  . ARG B 45  ? 0.7392 1.3018 0.5326 0.1880  0.0160  0.0101  431  ARG B CZ  
2340 N NH1 . ARG B 45  ? 0.8154 1.3183 0.6033 0.1548  0.0055  0.0240  431  ARG B NH1 
2341 N NH2 . ARG B 45  ? 0.5832 1.1704 0.3574 0.2010  0.0234  -0.0005 431  ARG B NH2 
2342 N N   . ASN B 46  ? 0.7494 0.9898 0.5233 0.1719  -0.0439 0.0043  432  ASN B N   
2343 C CA  . ASN B 46  ? 0.7607 0.9347 0.5298 0.1497  -0.0578 0.0027  432  ASN B CA  
2344 C C   . ASN B 46  ? 0.6998 0.8279 0.4973 0.1292  -0.0656 0.0098  432  ASN B C   
2345 O O   . ASN B 46  ? 0.7081 0.7931 0.5108 0.1076  -0.0769 0.0092  432  ASN B O   
2346 C CB  . ASN B 46  ? 0.8019 1.0024 0.5660 0.1217  -0.0591 0.0160  432  ASN B CB  
2347 C CG  . ASN B 46  ? 0.7902 1.0454 0.5798 0.0948  -0.0511 0.0396  432  ASN B CG  
2348 O OD1 . ASN B 46  ? 0.7079 1.0177 0.5114 0.1043  -0.0390 0.0429  432  ASN B OD1 
2349 N ND2 . ASN B 46  ? 0.7086 0.9484 0.5037 0.0616  -0.0594 0.0549  432  ASN B ND2 
2350 N N   . THR B 47  ? 0.4948 0.6349 0.3103 0.1365  -0.0602 0.0153  433  THR B N   
2351 C CA  . THR B 47  ? 0.5253 0.6275 0.3648 0.1169  -0.0653 0.0223  433  THR B CA  
2352 C C   . THR B 47  ? 0.5320 0.5647 0.3563 0.1339  -0.0692 0.0083  433  THR B C   
2353 O O   . THR B 47  ? 0.5495 0.5692 0.3468 0.1671  -0.0670 -0.0041 433  THR B O   
2354 C CB  . THR B 47  ? 0.4501 0.6017 0.3145 0.1120  -0.0586 0.0369  433  THR B CB  
2355 O OG1 . THR B 47  ? 0.4646 0.6179 0.3186 0.1460  -0.0545 0.0302  433  THR B OG1 
2356 C CG2 . THR B 47  ? 0.3942 0.6220 0.2663 0.1005  -0.0513 0.0482  433  THR B CG2 
2357 N N   . VAL B 48  ? 0.4670 0.4535 0.3069 0.1103  -0.0748 0.0099  434  VAL B N   
2358 C CA  . VAL B 48  ? 0.4732 0.3905 0.2997 0.1164  -0.0767 -0.0002 434  VAL B CA  
2359 C C   . VAL B 48  ? 0.4617 0.3740 0.3073 0.1048  -0.0727 0.0123  434  VAL B C   
2360 O O   . VAL B 48  ? 0.3796 0.3304 0.2542 0.0837  -0.0720 0.0248  434  VAL B O   
2361 C CB  . VAL B 48  ? 0.4426 0.3111 0.2686 0.0964  -0.0857 -0.0134 434  VAL B CB  
2362 C CG1 . VAL B 48  ? 0.4679 0.3437 0.2714 0.1086  -0.0913 -0.0263 434  VAL B CG1 
2363 C CG2 . VAL B 48  ? 0.3977 0.2787 0.2602 0.0620  -0.0901 -0.0052 434  VAL B CG2 
2364 N N   . PRO B 49  ? 0.4419 0.3042 0.2679 0.1178  -0.0704 0.0098  435  PRO B N   
2365 C CA  . PRO B 49  ? 0.4263 0.2850 0.2642 0.1084  -0.0661 0.0224  435  PRO B CA  
2366 C C   . PRO B 49  ? 0.4473 0.2852 0.3112 0.0704  -0.0667 0.0233  435  PRO B C   
2367 O O   . PRO B 49  ? 0.4198 0.2129 0.2803 0.0563  -0.0693 0.0118  435  PRO B O   
2368 C CB  . PRO B 49  ? 0.5030 0.3017 0.3014 0.1346  -0.0647 0.0191  435  PRO B CB  
2369 C CG  . PRO B 49  ? 0.5325 0.2805 0.3049 0.1416  -0.0689 0.0018  435  PRO B CG  
2370 C CD  . PRO B 49  ? 0.5058 0.3093 0.2913 0.1438  -0.0720 -0.0041 435  PRO B CD  
2371 N N   . CYS B 50  ? 0.4103 0.2846 0.3014 0.0543  -0.0647 0.0350  436  CYS B N   
2372 C CA  . CYS B 50  ? 0.3387 0.2005 0.2557 0.0228  -0.0642 0.0349  436  CYS B CA  
2373 C C   . CYS B 50  ? 0.4130 0.2869 0.3358 0.0195  -0.0586 0.0464  436  CYS B C   
2374 O O   . CYS B 50  ? 0.3908 0.3106 0.3180 0.0300  -0.0591 0.0557  436  CYS B O   
2375 C CB  . CYS B 50  ? 0.3544 0.2508 0.3016 0.0036  -0.0717 0.0336  436  CYS B CB  
2376 S SG  . CYS B 50  ? 0.3745 0.3396 0.3338 0.0065  -0.0734 0.0478  436  CYS B SG  
2377 N N   . ARG B 51  ? 0.3982 0.2340 0.3201 0.0035  -0.0529 0.0450  437  ARG B N   
2378 C CA  . ARG B 51  ? 0.3781 0.2184 0.2984 0.0003  -0.0470 0.0550  437  ARG B CA  
2379 C C   . ARG B 51  ? 0.3232 0.1892 0.2800 -0.0272 -0.0468 0.0533  437  ARG B C   
2380 O O   . ARG B 51  ? 0.3487 0.2121 0.3287 -0.0452 -0.0496 0.0430  437  ARG B O   
2381 C CB  . ARG B 51  ? 0.4781 0.2555 0.3641 0.0016  -0.0388 0.0563  437  ARG B CB  
2382 C CG  . ARG B 51  ? 0.5070 0.2402 0.3965 -0.0227 -0.0346 0.0442  437  ARG B CG  
2383 C CD  . ARG B 51  ? 0.5650 0.2322 0.4159 -0.0273 -0.0244 0.0483  437  ARG B CD  
2384 N NE  . ARG B 51  ? 0.6606 0.3126 0.5243 -0.0453 -0.0190 0.0327  437  ARG B NE  
2385 C CZ  . ARG B 51  ? 0.6219 0.3004 0.5244 -0.0716 -0.0103 0.0233  437  ARG B CZ  
2386 N NH1 . ARG B 51  ? 0.5309 0.2476 0.4610 -0.0829 -0.0052 0.0255  437  ARG B NH1 
2387 N NH2 . ARG B 51  ? 0.6154 0.2842 0.5302 -0.0837 -0.0079 0.0106  437  ARG B NH2 
2388 N N   . LYS B 52  ? 0.3352 0.2266 0.2962 -0.0281 -0.0451 0.0617  438  LYS B N   
2389 C CA  . LYS B 52  ? 0.3141 0.2268 0.3053 -0.0506 -0.0452 0.0586  438  LYS B CA  
2390 C C   . LYS B 52  ? 0.3193 0.2225 0.2964 -0.0536 -0.0368 0.0636  438  LYS B C   
2391 O O   . LYS B 52  ? 0.3315 0.2463 0.2881 -0.0368 -0.0377 0.0735  438  LYS B O   
2392 C CB  . LYS B 52  ? 0.2965 0.2579 0.3097 -0.0526 -0.0549 0.0623  438  LYS B CB  
2393 C CG  . LYS B 52  ? 0.3184 0.2934 0.3591 -0.0733 -0.0576 0.0572  438  LYS B CG  
2394 C CD  . LYS B 52  ? 0.2741 0.2832 0.3316 -0.0791 -0.0685 0.0611  438  LYS B CD  
2395 C CE  . LYS B 52  ? 0.3960 0.4410 0.4445 -0.0714 -0.0693 0.0717  438  LYS B CE  
2396 N NZ  . LYS B 52  ? 0.4481 0.5157 0.5061 -0.0803 -0.0732 0.0729  438  LYS B NZ  
2397 N N   . PHE B 53  ? 0.2987 0.1850 0.2863 -0.0741 -0.0288 0.0558  439  PHE B N   
2398 C CA  . PHE B 53  ? 0.2903 0.1694 0.2630 -0.0801 -0.0191 0.0596  439  PHE B CA  
2399 C C   . PHE B 53  ? 0.2757 0.1984 0.2677 -0.0830 -0.0255 0.0596  439  PHE B C   
2400 O O   . PHE B 53  ? 0.2167 0.1602 0.2421 -0.0960 -0.0308 0.0496  439  PHE B O   
2401 C CB  . PHE B 53  ? 0.3370 0.1981 0.3200 -0.0995 -0.0052 0.0472  439  PHE B CB  
2402 C CG  . PHE B 53  ? 0.3839 0.2307 0.3429 -0.1071 0.0079  0.0524  439  PHE B CG  
2403 C CD1 . PHE B 53  ? 0.4226 0.2224 0.3331 -0.1011 0.0158  0.0655  439  PHE B CD1 
2404 C CD2 . PHE B 53  ? 0.3248 0.2028 0.3058 -0.1167 0.0120  0.0434  439  PHE B CD2 
2405 C CE1 . PHE B 53  ? 0.4038 0.1902 0.2871 -0.1073 0.0280  0.0713  439  PHE B CE1 
2406 C CE2 . PHE B 53  ? 0.3456 0.2110 0.2995 -0.1255 0.0249  0.0483  439  PHE B CE2 
2407 C CZ  . PHE B 53  ? 0.4005 0.2204 0.3043 -0.1216 0.0335  0.0632  439  PHE B CZ  
2408 N N   . VAL B 54  ? 0.2571 0.1915 0.2262 -0.0699 -0.0269 0.0699  440  VAL B N   
2409 C CA  . VAL B 54  ? 0.2616 0.2370 0.2450 -0.0733 -0.0345 0.0692  440  VAL B CA  
2410 C C   . VAL B 54  ? 0.3070 0.2742 0.2665 -0.0753 -0.0266 0.0710  440  VAL B C   
2411 O O   . VAL B 54  ? 0.3131 0.2578 0.2339 -0.0607 -0.0223 0.0817  440  VAL B O   
2412 C CB  . VAL B 54  ? 0.2717 0.2836 0.2539 -0.0568 -0.0461 0.0776  440  VAL B CB  
2413 C CG1 . VAL B 54  ? 0.2236 0.2760 0.2195 -0.0651 -0.0541 0.0757  440  VAL B CG1 
2414 C CG2 . VAL B 54  ? 0.2432 0.2643 0.2448 -0.0565 -0.0519 0.0763  440  VAL B CG2 
2415 N N   . LYS B 55  ? 0.3219 0.3046 0.3002 -0.0916 -0.0255 0.0602  441  LYS B N   
2416 C CA  . LYS B 55  ? 0.3523 0.3284 0.3072 -0.0960 -0.0161 0.0593  441  LYS B CA  
2417 C C   . LYS B 55  ? 0.3489 0.3479 0.2801 -0.0813 -0.0254 0.0681  441  LYS B C   
2418 O O   . LYS B 55  ? 0.2717 0.3057 0.2193 -0.0758 -0.0397 0.0690  441  LYS B O   
2419 C CB  . LYS B 55  ? 0.3310 0.3209 0.3142 -0.1144 -0.0130 0.0414  441  LYS B CB  
2420 C CG  . LYS B 55  ? 0.4259 0.4060 0.4409 -0.1267 -0.0079 0.0291  441  LYS B CG  
2421 C CD  . LYS B 55  ? 0.6313 0.6303 0.6760 -0.1303 -0.0079 0.0083  441  LYS B CD  
2422 C CE  . LYS B 55  ? 0.7100 0.7098 0.7352 -0.1451 0.0074  0.0027  441  LYS B CE  
2423 N NZ  . LYS B 55  ? 0.5362 0.5592 0.5714 -0.1460 -0.0005 -0.0113 441  LYS B NZ  
2424 N N   . ILE B 56  ? 0.3351 0.3155 0.2259 -0.0765 -0.0170 0.0745  442  ILE B N   
2425 C CA  . ILE B 56  ? 0.3851 0.3888 0.2505 -0.0612 -0.0274 0.0811  442  ILE B CA  
2426 C C   . ILE B 56  ? 0.3718 0.4128 0.2591 -0.0749 -0.0346 0.0666  442  ILE B C   
2427 O O   . ILE B 56  ? 0.3848 0.4652 0.2834 -0.0702 -0.0506 0.0654  442  ILE B O   
2428 C CB  . ILE B 56  ? 0.4798 0.4450 0.2873 -0.0507 -0.0175 0.0938  442  ILE B CB  
2429 C CG1 . ILE B 56  ? 0.4619 0.3794 0.2433 -0.0371 -0.0123 0.1075  442  ILE B CG1 
2430 C CG2 . ILE B 56  ? 0.4606 0.4529 0.2401 -0.0318 -0.0313 0.0996  442  ILE B CG2 
2431 C CD1 . ILE B 56  ? 0.5100 0.4472 0.2959 -0.0100 -0.0286 0.1140  442  ILE B CD1 
2432 N N   . ASN B 57  ? 0.4112 0.4416 0.3049 -0.0926 -0.0229 0.0538  443  ASN B N   
2433 C CA  . ASN B 57  ? 0.4025 0.4600 0.3178 -0.1049 -0.0298 0.0362  443  ASN B CA  
2434 C C   . ASN B 57  ? 0.4516 0.4958 0.3888 -0.1211 -0.0161 0.0198  443  ASN B C   
2435 O O   . ASN B 57  ? 0.5106 0.5315 0.4511 -0.1251 -0.0025 0.0224  443  ASN B O   
2436 C CB  . ASN B 57  ? 0.3945 0.4668 0.2747 -0.0990 -0.0338 0.0358  443  ASN B CB  
2437 C CG  . ASN B 57  ? 0.5181 0.5613 0.3538 -0.0984 -0.0146 0.0409  443  ASN B CG  
2438 O OD1 . ASN B 57  ? 0.5568 0.5925 0.3977 -0.1130 0.0005  0.0277  443  ASN B OD1 
2439 N ND2 . ASN B 57  ? 0.5322 0.5589 0.3218 -0.0810 -0.0149 0.0601  443  ASN B ND2 
2440 N N   . ASN B 58  ? 0.4740 0.5349 0.4269 -0.1296 -0.0207 0.0008  444  ASN B N   
2441 C CA  . ASN B 58  ? 0.4361 0.4933 0.4149 -0.1404 -0.0107 -0.0193 444  ASN B CA  
2442 C C   . ASN B 58  ? 0.5147 0.5718 0.4675 -0.1449 0.0085  -0.0285 444  ASN B C   
2443 O O   . ASN B 58  ? 0.5166 0.5812 0.4912 -0.1520 0.0176  -0.0493 444  ASN B O   
2444 C CB  . ASN B 58  ? 0.2851 0.3543 0.2967 -0.1444 -0.0285 -0.0369 444  ASN B CB  
2445 C CG  . ASN B 58  ? 0.3637 0.4316 0.3979 -0.1427 -0.0450 -0.0265 444  ASN B CG  
2446 O OD1 . ASN B 58  ? 0.3326 0.3901 0.3727 -0.1380 -0.0406 -0.0143 444  ASN B OD1 
2447 N ND2 . ASN B 58  ? 0.3028 0.3734 0.3461 -0.1351 -0.0588 -0.0303 444  ASN B ND2 
2448 N N   . SER B 59  ? 0.5883 0.6389 0.4933 -0.1396 0.0148  -0.0139 445  SER B N   
2449 C CA  . SER B 59  ? 0.6236 0.6695 0.4938 -0.1456 0.0362  -0.0175 445  SER B CA  
2450 C C   . SER B 59  ? 0.6880 0.7021 0.5302 -0.1508 0.0570  0.0010  445  SER B C   
2451 O O   . SER B 59  ? 0.7728 0.7778 0.5786 -0.1593 0.0777  0.0027  445  SER B O   
2452 C CB  . SER B 59  ? 0.6118 0.6673 0.4380 -0.1369 0.0283  -0.0144 445  SER B CB  
2453 O OG  . SER B 59  ? 0.6056 0.6864 0.4553 -0.1345 0.0064  -0.0305 445  SER B OG  
2454 N N   . THR B 60  ? 0.5942 0.5886 0.4489 -0.1475 0.0523  0.0147  446  THR B N   
2455 C CA  . THR B 60  ? 0.6492 0.6043 0.4740 -0.1530 0.0692  0.0323  446  THR B CA  
2456 C C   . THR B 60  ? 0.5929 0.5407 0.4604 -0.1600 0.0693  0.0284  446  THR B C   
2457 O O   . THR B 60  ? 0.5239 0.4929 0.4355 -0.1549 0.0526  0.0186  446  THR B O   
2458 C CB  . THR B 60  ? 0.6332 0.5588 0.4069 -0.1335 0.0599  0.0583  446  THR B CB  
2459 O OG1 . THR B 60  ? 0.7267 0.6039 0.4756 -0.1384 0.0728  0.0739  446  THR B OG1 
2460 C CG2 . THR B 60  ? 0.6503 0.5971 0.4500 -0.1147 0.0338  0.0606  446  THR B CG2 
2461 N N   . ASN B 61  ? 0.4914 0.4058 0.3413 -0.1734 0.0877  0.0365  447  ASN B N   
2462 C CA  . ASN B 61  ? 0.4829 0.3821 0.3615 -0.1790 0.0866  0.0359  447  ASN B CA  
2463 C C   . ASN B 61  ? 0.5628 0.4241 0.4114 -0.1606 0.0746  0.0574  447  ASN B C   
2464 O O   . ASN B 61  ? 0.5594 0.4079 0.4287 -0.1576 0.0701  0.0559  447  ASN B O   
2465 C CB  . ASN B 61  ? 0.5198 0.4123 0.4056 -0.1918 0.1042  0.0274  447  ASN B CB  
2466 C CG  . ASN B 61  ? 0.4886 0.4255 0.4095 -0.2047 0.1148  0.0029  447  ASN B CG  
2467 O OD1 . ASN B 61  ? 0.5684 0.5398 0.5348 -0.1992 0.1030  -0.0146 447  ASN B OD1 
2468 N ND2 . ASN B 61  ? 0.4743 0.4092 0.3724 -0.2195 0.1360  0.0011  447  ASN B ND2 
2469 N N   . GLU B 62  ? 0.5147 0.3660 0.3200 -0.1407 0.0659  0.0735  448  GLU B N   
2470 C CA  . GLU B 62  ? 0.5241 0.3424 0.2979 -0.1178 0.0543  0.0923  448  GLU B CA  
2471 C C   . GLU B 62  ? 0.4518 0.3010 0.2680 -0.1028 0.0338  0.0870  448  GLU B C   
2472 O O   . GLU B 62  ? 0.4944 0.3901 0.3493 -0.1041 0.0234  0.0748  448  GLU B O   
2473 C CB  . GLU B 62  ? 0.6317 0.4401 0.3503 -0.0969 0.0481  0.1086  448  GLU B CB  
2474 C CG  . GLU B 62  ? 0.7825 0.5316 0.4467 -0.0842 0.0530  0.1269  448  GLU B CG  
2475 C CD  . GLU B 62  ? 0.8558 0.6053 0.4763 -0.0542 0.0395  0.1407  448  GLU B CD  
2476 O OE1 . GLU B 62  ? 0.8283 0.6170 0.4461 -0.0510 0.0313  0.1376  448  GLU B OE1 
2477 O OE2 . GLU B 62  ? 0.9576 0.6710 0.5486 -0.0344 0.0352  0.1524  448  GLU B OE2 
2478 N N   . GLY B 63  ? 0.4408 0.4816 0.2714 0.0057  -0.0169 0.0928  449  GLY B N   
2479 C CA  . GLY B 63  ? 0.3489 0.3863 0.1910 0.0044  -0.0213 0.0840  449  GLY B CA  
2480 C C   . GLY B 63  ? 0.3548 0.3840 0.2074 0.0064  -0.0234 0.0902  449  GLY B C   
2481 O O   . GLY B 63  ? 0.3707 0.3949 0.2225 0.0080  -0.0220 0.1010  449  GLY B O   
2482 N N   . MET B 64  ? 0.2939 0.3218 0.1565 0.0069  -0.0270 0.0834  450  MET B N   
2483 C CA  . MET B 64  ? 0.3027 0.3231 0.1746 0.0107  -0.0296 0.0874  450  MET B CA  
2484 C C   . MET B 64  ? 0.3298 0.3465 0.2135 0.0098  -0.0294 0.0790  450  MET B C   
2485 O O   . MET B 64  ? 0.3051 0.3287 0.1903 0.0074  -0.0298 0.0708  450  MET B O   
2486 C CB  . MET B 64  ? 0.3555 0.3829 0.2244 0.0163  -0.0360 0.0909  450  MET B CB  
2487 C CG  . MET B 64  ? 0.4098 0.4361 0.2696 0.0195  -0.0367 0.1024  450  MET B CG  
2488 S SD  . MET B 64  ? 0.5947 0.6330 0.4486 0.0258  -0.0448 0.1052  450  MET B SD  
2489 C CE  . MET B 64  ? 0.5407 0.5755 0.4098 0.0310  -0.0483 0.1031  450  MET B CE  
2490 N N   . ASN B 65  ? 0.3568 0.3622 0.2487 0.0121  -0.0293 0.0812  451  ASN B N   
2491 C CA  . ASN B 65  ? 0.3412 0.3428 0.2430 0.0130  -0.0293 0.0736  451  ASN B CA  
2492 C C   . ASN B 65  ? 0.3510 0.3610 0.2561 0.0191  -0.0338 0.0713  451  ASN B C   
2493 O O   . ASN B 65  ? 0.3986 0.4072 0.3036 0.0253  -0.0374 0.0766  451  ASN B O   
2494 C CB  . ASN B 65  ? 0.3685 0.3541 0.2768 0.0142  -0.0290 0.0761  451  ASN B CB  
2495 C CG  . ASN B 65  ? 0.4356 0.4146 0.3437 0.0075  -0.0245 0.0796  451  ASN B CG  
2496 O OD1 . ASN B 65  ? 0.4823 0.4669 0.3894 0.0023  -0.0205 0.0750  451  ASN B OD1 
2497 N ND2 . ASN B 65  ? 0.4673 0.4351 0.3775 0.0076  -0.0252 0.0885  451  ASN B ND2 
2498 N N   . VAL B 66  ? 0.3287 0.3481 0.2374 0.0174  -0.0337 0.0641  452  VAL B N   
2499 C CA  . VAL B 66  ? 0.3142 0.3444 0.2286 0.0225  -0.0371 0.0626  452  VAL B CA  
2500 C C   . VAL B 66  ? 0.3349 0.3596 0.2571 0.0274  -0.0359 0.0587  452  VAL B C   
2501 O O   . VAL B 66  ? 0.3347 0.3557 0.2596 0.0240  -0.0327 0.0530  452  VAL B O   
2502 C CB  . VAL B 66  ? 0.3351 0.3792 0.2506 0.0176  -0.0381 0.0584  452  VAL B CB  
2503 C CG1 . VAL B 66  ? 0.3147 0.3724 0.2386 0.0224  -0.0415 0.0589  452  VAL B CG1 
2504 C CG2 . VAL B 66  ? 0.3052 0.3533 0.2111 0.0137  -0.0403 0.0606  452  VAL B CG2 
2505 N N   . LYS B 67  ? 0.3164 0.3406 0.2413 0.0364  -0.0387 0.0612  453  LYS B N   
2506 C CA  . LYS B 67  ? 0.3395 0.3591 0.2699 0.0434  -0.0383 0.0568  453  LYS B CA  
2507 C C   . LYS B 67  ? 0.3245 0.3603 0.2608 0.0440  -0.0369 0.0526  453  LYS B C   
2508 O O   . LYS B 67  ? 0.4397 0.4916 0.3792 0.0461  -0.0388 0.0556  453  LYS B O   
2509 C CB  . LYS B 67  ? 0.3136 0.3283 0.2442 0.0543  -0.0421 0.0604  453  LYS B CB  
2510 N N   . LYS B 68  ? 0.2611 0.2935 0.1997 0.0420  -0.0338 0.0466  454  LYS B N   
2511 C CA  . LYS B 68  ? 0.3342 0.3809 0.2787 0.0426  -0.0319 0.0436  454  LYS B CA  
2512 C C   . LYS B 68  ? 0.3952 0.4367 0.3413 0.0508  -0.0305 0.0386  454  LYS B C   
2513 O O   . LYS B 68  ? 0.3520 0.3776 0.2950 0.0557  -0.0322 0.0366  454  LYS B O   
2514 C CB  . LYS B 68  ? 0.3272 0.3768 0.2719 0.0316  -0.0295 0.0412  454  LYS B CB  
2515 C CG  . LYS B 68  ? 0.3660 0.4160 0.3059 0.0240  -0.0312 0.0441  454  LYS B CG  
2516 C CD  . LYS B 68  ? 0.3781 0.4368 0.3202 0.0158  -0.0309 0.0418  454  LYS B CD  
2517 C CE  . LYS B 68  ? 0.4105 0.4871 0.3611 0.0173  -0.0333 0.0445  454  LYS B CE  
2518 N NZ  . LYS B 68  ? 0.5257 0.6089 0.4798 0.0087  -0.0344 0.0427  454  LYS B NZ  
2519 N N   . CYS B 69  ? 0.2882 0.3429 0.2391 0.0525  -0.0281 0.0367  455  CYS B N   
2520 C CA  . CYS B 69  ? 0.3082 0.3612 0.2593 0.0615  -0.0267 0.0316  455  CYS B CA  
2521 C C   . CYS B 69  ? 0.2924 0.3473 0.2452 0.0553  -0.0232 0.0277  455  CYS B C   
2522 O O   . CYS B 69  ? 0.3049 0.3707 0.2616 0.0473  -0.0217 0.0303  455  CYS B O   
2523 C CB  . CYS B 69  ? 0.3124 0.3829 0.2672 0.0732  -0.0265 0.0344  455  CYS B CB  
2524 S SG  . CYS B 69  ? 0.3980 0.4687 0.3517 0.0817  -0.0308 0.0395  455  CYS B SG  
2525 N N   . CYS B 70  ? 0.2686 0.3121 0.2184 0.0592  -0.0229 0.0213  456  CYS B N   
2526 C CA  . CYS B 70  ? 0.2933 0.3363 0.2439 0.0541  -0.0201 0.0172  456  CYS B CA  
2527 C C   . CYS B 70  ? 0.3024 0.3507 0.2521 0.0651  -0.0190 0.0131  456  CYS B C   
2528 O O   . CYS B 70  ? 0.3064 0.3479 0.2522 0.0760  -0.0216 0.0096  456  CYS B O   
2529 C CB  . CYS B 70  ? 0.2861 0.3102 0.2340 0.0468  -0.0210 0.0131  456  CYS B CB  
2530 S SG  . CYS B 70  ? 0.3373 0.3596 0.2851 0.0329  -0.0201 0.0173  456  CYS B SG  
2531 N N   . LYS B 71  ? 0.2626 0.3226 0.2154 0.0626  -0.0154 0.0136  457  LYS B N   
2532 C CA  . LYS B 71  ? 0.3152 0.3824 0.2662 0.0729  -0.0136 0.0105  457  LYS B CA  
2533 C C   . LYS B 71  ? 0.2833 0.3528 0.2361 0.0657  -0.0107 0.0094  457  LYS B C   
2534 O O   . LYS B 71  ? 0.2766 0.3432 0.2326 0.0536  -0.0101 0.0111  457  LYS B O   
2535 C CB  . LYS B 71  ? 0.2564 0.3457 0.2108 0.0824  -0.0113 0.0166  457  LYS B CB  
2536 C CG  . LYS B 71  ? 0.2676 0.3756 0.2313 0.0736  -0.0083 0.0254  457  LYS B CG  
2537 C CD  . LYS B 71  ? 0.3045 0.4367 0.2738 0.0829  -0.0060 0.0328  457  LYS B CD  
2538 C CE  . LYS B 71  ? 0.2836 0.4341 0.2647 0.0728  -0.0041 0.0423  457  LYS B CE  
2539 N NZ  . LYS B 71  ? 0.2982 0.4752 0.2875 0.0809  -0.0016 0.0513  457  LYS B NZ  
2540 N N   . GLY B 72  ? 0.2813 0.3559 0.2312 0.0743  -0.0091 0.0062  458  GLY B N   
2541 C CA  . GLY B 72  ? 0.3107 0.3888 0.2621 0.0695  -0.0064 0.0058  458  GLY B CA  
2542 C C   . GLY B 72  ? 0.2638 0.3313 0.2083 0.0763  -0.0081 -0.0031 458  GLY B C   
2543 O O   . GLY B 72  ? 0.2423 0.2990 0.1809 0.0849  -0.0120 -0.0095 458  GLY B O   
2544 N N   . PHE B 73  ? 0.2550 0.3250 0.2004 0.0723  -0.0059 -0.0036 459  PHE B N   
2545 C CA  . PHE B 73  ? 0.2638 0.3263 0.2029 0.0789  -0.0079 -0.0118 459  PHE B CA  
2546 C C   . PHE B 73  ? 0.2435 0.2838 0.1805 0.0753  -0.0134 -0.0200 459  PHE B C   
2547 O O   . PHE B 73  ? 0.2732 0.3041 0.2044 0.0845  -0.0180 -0.0276 459  PHE B O   
2548 C CB  . PHE B 73  ? 0.2296 0.2985 0.1710 0.0737  -0.0046 -0.0096 459  PHE B CB  
2549 C CG  . PHE B 73  ? 0.2110 0.2753 0.1458 0.0812  -0.0066 -0.0173 459  PHE B CG  
2550 C CD1 . PHE B 73  ? 0.2371 0.2843 0.1713 0.0761  -0.0109 -0.0252 459  PHE B CD1 
2551 C CD2 . PHE B 73  ? 0.2269 0.3056 0.1564 0.0934  -0.0043 -0.0162 459  PHE B CD2 
2552 C CE1 . PHE B 73  ? 0.2225 0.2659 0.1511 0.0829  -0.0138 -0.0326 459  PHE B CE1 
2553 C CE2 . PHE B 73  ? 0.2659 0.3407 0.1879 0.1011  -0.0069 -0.0237 459  PHE B CE2 
2554 C CZ  . PHE B 73  ? 0.2209 0.2775 0.1427 0.0956  -0.0121 -0.0324 459  PHE B CZ  
2555 N N   . CYS B 74  ? 0.2390 0.2712 0.1811 0.0621  -0.0133 -0.0184 460  CYS B N   
2556 C CA  . CYS B 74  ? 0.2679 0.2814 0.2103 0.0575  -0.0178 -0.0240 460  CYS B CA  
2557 C C   . CYS B 74  ? 0.2437 0.2477 0.1845 0.0616  -0.0218 -0.0246 460  CYS B C   
2558 O O   . CYS B 74  ? 0.2037 0.1916 0.1442 0.0616  -0.0271 -0.0300 460  CYS B O   
2559 C CB  . CYS B 74  ? 0.2349 0.2450 0.1826 0.0436  -0.0156 -0.0210 460  CYS B CB  
2560 S SG  . CYS B 74  ? 0.2085 0.2245 0.1583 0.0388  -0.0125 -0.0220 460  CYS B SG  
2561 N N   . ILE B 75  ? 0.2692 0.2826 0.2099 0.0649  -0.0200 -0.0188 461  ILE B N   
2562 C CA  . ILE B 75  ? 0.2922 0.2971 0.2307 0.0708  -0.0240 -0.0193 461  ILE B CA  
2563 C C   . ILE B 75  ? 0.2976 0.2988 0.2296 0.0860  -0.0281 -0.0267 461  ILE B C   
2564 O O   . ILE B 75  ? 0.3317 0.3161 0.2616 0.0902  -0.0343 -0.0317 461  ILE B O   
2565 C CB  . ILE B 75  ? 0.3055 0.3234 0.2461 0.0707  -0.0212 -0.0109 461  ILE B CB  
2566 C CG1 . ILE B 75  ? 0.3106 0.3302 0.2560 0.0564  -0.0185 -0.0051 461  ILE B CG1 
2567 C CG2 . ILE B 75  ? 0.2482 0.2577 0.1863 0.0782  -0.0254 -0.0110 461  ILE B CG2 
2568 C CD1 . ILE B 75  ? 0.3075 0.3098 0.2535 0.0480  -0.0210 -0.0066 461  ILE B CD1 
2569 N N   . ASP B 76  ? 0.2213 0.2376 0.1498 0.0948  -0.0250 -0.0274 462  ASP B N   
2570 C CA  . ASP B 76  ? 0.3052 0.3191 0.2254 0.1106  -0.0288 -0.0355 462  ASP B CA  
2571 C C   . ASP B 76  ? 0.3388 0.3337 0.2568 0.1094  -0.0353 -0.0455 462  ASP B C   
2572 O O   . ASP B 76  ? 0.3346 0.3166 0.2467 0.1199  -0.0424 -0.0541 462  ASP B O   
2573 C CB  . ASP B 76  ? 0.3467 0.3832 0.2634 0.1197  -0.0231 -0.0328 462  ASP B CB  
2574 C CG  . ASP B 76  ? 0.3902 0.4460 0.3086 0.1263  -0.0186 -0.0244 462  ASP B CG  
2575 O OD1 . ASP B 76  ? 0.2933 0.3442 0.2146 0.1243  -0.0203 -0.0216 462  ASP B OD1 
2576 O OD2 . ASP B 76  ? 0.4349 0.5119 0.3522 0.1337  -0.0133 -0.0200 462  ASP B OD2 
2577 N N   . ILE B 77  ? 0.2877 0.2806 0.2109 0.0970  -0.0337 -0.0447 463  ILE B N   
2578 C CA  . ILE B 77  ? 0.3163 0.2922 0.2403 0.0938  -0.0402 -0.0530 463  ILE B CA  
2579 C C   . ILE B 77  ? 0.2877 0.2433 0.2159 0.0887  -0.0465 -0.0544 463  ILE B C   
2580 O O   . ILE B 77  ? 0.2910 0.2300 0.2178 0.0931  -0.0551 -0.0627 463  ILE B O   
2581 C CB  . ILE B 77  ? 0.2568 0.2373 0.1866 0.0816  -0.0363 -0.0507 463  ILE B CB  
2582 C CG1 . ILE B 77  ? 0.2134 0.2107 0.1385 0.0880  -0.0319 -0.0505 463  ILE B CG1 
2583 C CG2 . ILE B 77  ? 0.2928 0.2565 0.2269 0.0754  -0.0428 -0.0572 463  ILE B CG2 
2584 C CD1 . ILE B 77  ? 0.3117 0.3045 0.2293 0.0992  -0.0377 -0.0606 463  ILE B CD1 
2585 N N   . LEU B 78  ? 0.3020 0.2585 0.2356 0.0796  -0.0430 -0.0458 464  LEU B N   
2586 C CA  . LEU B 78  ? 0.3363 0.2748 0.2740 0.0747  -0.0483 -0.0447 464  LEU B CA  
2587 C C   . LEU B 78  ? 0.3133 0.2421 0.2453 0.0882  -0.0547 -0.0493 464  LEU B C   
2588 O O   . LEU B 78  ? 0.3023 0.2107 0.2363 0.0884  -0.0629 -0.0535 464  LEU B O   
2589 C CB  . LEU B 78  ? 0.4025 0.3467 0.3449 0.0639  -0.0426 -0.0342 464  LEU B CB  
2590 C CG  . LEU B 78  ? 0.3350 0.2642 0.2812 0.0593  -0.0466 -0.0301 464  LEU B CG  
2591 C CD1 . LEU B 78  ? 0.3229 0.2345 0.2756 0.0525  -0.0525 -0.0335 464  LEU B CD1 
2592 C CD2 . LEU B 78  ? 0.3475 0.2855 0.2962 0.0496  -0.0404 -0.0200 464  LEU B CD2 
2593 N N   . LYS B 79  ? 0.3731 0.3162 0.2986 0.0999  -0.0513 -0.0480 465  LYS B N   
2594 C CA  . LYS B 79  ? 0.3727 0.3082 0.2915 0.1153  -0.0570 -0.0532 465  LYS B CA  
2595 C C   . LYS B 79  ? 0.3618 0.2839 0.2745 0.1254  -0.0654 -0.0660 465  LYS B C   
2596 O O   . LYS B 79  ? 0.3673 0.2698 0.2775 0.1326  -0.0746 -0.0725 465  LYS B O   
2597 C CB  . LYS B 79  ? 0.3206 0.2785 0.2343 0.1265  -0.0507 -0.0489 465  LYS B CB  
2598 C CG  . LYS B 79  ? 0.3758 0.3417 0.2944 0.1212  -0.0465 -0.0381 465  LYS B CG  
2599 C CD  . LYS B 79  ? 0.3595 0.3454 0.2742 0.1350  -0.0426 -0.0350 465  LYS B CD  
2600 C CE  . LYS B 79  ? 0.4152 0.4269 0.3317 0.1331  -0.0342 -0.0297 465  LYS B CE  
2601 N NZ  . LYS B 79  ? 0.4665 0.5006 0.3813 0.1461  -0.0299 -0.0249 465  LYS B NZ  
2602 N N   . LYS B 80  ? 0.3487 0.2805 0.2586 0.1263  -0.0632 -0.0701 466  LYS B N   
2603 C CA  . LYS B 80  ? 0.3479 0.2678 0.2516 0.1354  -0.0718 -0.0829 466  LYS B CA  
2604 C C   . LYS B 80  ? 0.3780 0.2735 0.2901 0.1243  -0.0810 -0.0870 466  LYS B C   
2605 O O   . LYS B 80  ? 0.3696 0.2489 0.2801 0.1290  -0.0913 -0.0944 466  LYS B O   
2606 C CB  . LYS B 80  ? 0.3632 0.3006 0.2627 0.1377  -0.0668 -0.0845 466  LYS B CB  
2607 C CG  . LYS B 80  ? 0.3850 0.3454 0.2753 0.1509  -0.0611 -0.0816 466  LYS B CG  
2608 C CD  . LYS B 80  ? 0.3785 0.3573 0.2674 0.1494  -0.0550 -0.0791 466  LYS B CD  
2609 C CE  . LYS B 80  ? 0.4800 0.4765 0.3590 0.1624  -0.0538 -0.0778 466  LYS B CE  
2610 N NZ  . LYS B 80  ? 0.3906 0.3754 0.2630 0.1694  -0.0646 -0.0871 466  LYS B NZ  
2611 N N   . LEU B 81  ? 0.3520 0.2491 0.2751 0.1066  -0.0767 -0.0794 467  LEU B N   
2612 C CA  . LEU B 81  ? 0.4247 0.3023 0.3582 0.0949  -0.0842 -0.0810 467  LEU B CA  
2613 C C   . LEU B 81  ? 0.4180 0.2757 0.3553 0.0945  -0.0911 -0.0793 467  LEU B C   
2614 O O   . LEU B 81  ? 0.3852 0.2214 0.3272 0.0933  -0.1022 -0.0854 467  LEU B O   
2615 C CB  . LEU B 81  ? 0.3861 0.2729 0.3299 0.0776  -0.0765 -0.0720 467  LEU B CB  
2616 C CG  . LEU B 81  ? 0.3538 0.2559 0.2966 0.0757  -0.0716 -0.0739 467  LEU B CG  
2617 C CD1 . LEU B 81  ? 0.2542 0.1660 0.2057 0.0604  -0.0632 -0.0644 467  LEU B CD1 
2618 C CD2 . LEU B 81  ? 0.3355 0.2265 0.2795 0.0779  -0.0812 -0.0847 467  LEU B CD2 
2619 N N   . SER B 82  ? 0.4236 0.2876 0.3595 0.0952  -0.0853 -0.0706 468  SER B N   
2620 C CA  . SER B 82  ? 0.4020 0.2476 0.3406 0.0959  -0.0915 -0.0680 468  SER B CA  
2621 C C   . SER B 82  ? 0.4460 0.2751 0.3764 0.1128  -0.1026 -0.0799 468  SER B C   
2622 O O   . SER B 82  ? 0.3931 0.1993 0.3283 0.1113  -0.1126 -0.0818 468  SER B O   
2623 C CB  . SER B 82  ? 0.3471 0.2057 0.2844 0.0956  -0.0832 -0.0570 468  SER B CB  
2624 O OG  . SER B 82  ? 0.3879 0.2298 0.3252 0.1004  -0.0895 -0.0553 468  SER B OG  
2625 N N   . ARG B 83  ? 0.4353 0.2784 0.3537 0.1278  -0.1004 -0.0867 469  ARG B N   
2626 C CA  . ARG B 83  ? 0.4184 0.2578 0.3288 0.1391  -0.1079 -0.0942 469  ARG B CA  
2627 C C   . ARG B 83  ? 0.4750 0.3040 0.3886 0.1349  -0.1176 -0.1023 469  ARG B C   
2628 O O   . ARG B 83  ? 0.4603 0.2733 0.3745 0.1373  -0.1281 -0.1071 469  ARG B O   
2629 C CB  . ARG B 83  ? 0.4750 0.3386 0.3725 0.1535  -0.1009 -0.0956 469  ARG B CB  
2630 C CG  . ARG B 83  ? 0.6091 0.4744 0.4965 0.1644  -0.1078 -0.1049 469  ARG B CG  
2631 C CD  . ARG B 83  ? 0.7180 0.5892 0.5946 0.1792  -0.1076 -0.1057 469  ARG B CD  
2632 N NE  . ARG B 83  ? 0.8783 0.7424 0.7459 0.1893  -0.1179 -0.1155 469  ARG B NE  
2633 C CZ  . ARG B 83  ? 0.8781 0.7384 0.7370 0.2014  -0.1221 -0.1189 469  ARG B CZ  
2634 N NH1 . ARG B 83  ? 0.8855 0.7490 0.7441 0.2048  -0.1168 -0.1130 469  ARG B NH1 
2635 N NH2 . ARG B 83  ? 0.9697 0.8233 0.8199 0.2109  -0.1323 -0.1286 469  ARG B NH2 
2636 N N   . THR B 84  ? 0.4008 0.2390 0.3171 0.1288  -0.1147 -0.1035 470  THR B N   
2637 C CA  . THR B 84  ? 0.4821 0.3144 0.4017 0.1263  -0.1236 -0.1106 470  THR B CA  
2638 C C   . THR B 84  ? 0.4640 0.2761 0.3995 0.1113  -0.1311 -0.1086 470  THR B C   
2639 O O   . THR B 84  ? 0.4877 0.2846 0.4267 0.1117  -0.1423 -0.1131 470  THR B O   
2640 C CB  . THR B 84  ? 0.4638 0.3146 0.3811 0.1255  -0.1174 -0.1116 470  THR B CB  
2641 O OG1 . THR B 84  ? 0.4943 0.3640 0.3974 0.1400  -0.1122 -0.1129 470  THR B OG1 
2642 C CG2 . THR B 84  ? 0.4716 0.3160 0.3947 0.1214  -0.1266 -0.1177 470  THR B CG2 
2643 N N   . VAL B 85  ? 0.4219 0.2342 0.3675 0.0977  -0.1251 -0.1013 471  VAL B N   
2644 C CA  . VAL B 85  ? 0.4598 0.2563 0.4221 0.0822  -0.1306 -0.0966 471  VAL B CA  
2645 C C   . VAL B 85  ? 0.4767 0.2552 0.4433 0.0808  -0.1356 -0.0917 471  VAL B C   
2646 O O   . VAL B 85  ? 0.4570 0.2217 0.4378 0.0691  -0.1419 -0.0873 471  VAL B O   
2647 C CB  . VAL B 85  ? 0.4040 0.2075 0.3747 0.0687  -0.1221 -0.0892 471  VAL B CB  
2648 C CG1 . VAL B 85  ? 0.3667 0.1600 0.3560 0.0522  -0.1272 -0.0842 471  VAL B CG1 
2649 C CG2 . VAL B 85  ? 0.4736 0.2967 0.4373 0.0724  -0.1154 -0.0936 471  VAL B CG2 
2650 N N   . LYS B 86  ? 0.4573 0.2373 0.4127 0.0926  -0.1328 -0.0913 472  LYS B N   
2651 C CA  . LYS B 86  ? 0.5457 0.3097 0.5033 0.0936  -0.1374 -0.0868 472  LYS B CA  
2652 C C   . LYS B 86  ? 0.5276 0.2835 0.4978 0.0789  -0.1341 -0.0737 472  LYS B C   
2653 O O   . LYS B 86  ? 0.5545 0.2973 0.5387 0.0668  -0.1401 -0.0690 472  LYS B O   
2654 C CB  . LYS B 86  ? 0.4502 0.1981 0.4113 0.0952  -0.1507 -0.0933 472  LYS B CB  
2655 C CG  . LYS B 86  ? 0.5204 0.2743 0.4669 0.1117  -0.1553 -0.1056 472  LYS B CG  
2656 C CD  . LYS B 86  ? 0.5777 0.3125 0.5249 0.1163  -0.1687 -0.1111 472  LYS B CD  
2657 C CE  . LYS B 86  ? 0.6189 0.3426 0.5791 0.1063  -0.1793 -0.1141 472  LYS B CE  
2658 N NZ  . LYS B 86  ? 0.5952 0.3306 0.5486 0.1128  -0.1816 -0.1237 472  LYS B NZ  
2659 N N   . PHE B 87  ? 0.4885 0.2535 0.4543 0.0801  -0.1245 -0.0666 473  PHE B N   
2660 C CA  . PHE B 87  ? 0.4615 0.2291 0.4371 0.0658  -0.1183 -0.0508 473  PHE B CA  
2661 C C   . PHE B 87  ? 0.4571 0.2431 0.4236 0.0713  -0.1077 -0.0436 473  PHE B C   
2662 O O   . PHE B 87  ? 0.4422 0.2459 0.3983 0.0809  -0.1018 -0.0484 473  PHE B O   
2663 C CB  . PHE B 87  ? 0.4305 0.2096 0.4170 0.0487  -0.1119 -0.0444 473  PHE B CB  
2664 C CG  . PHE B 87  ? 0.4215 0.2263 0.4013 0.0496  -0.1012 -0.0466 473  PHE B CG  
2665 C CD1 . PHE B 87  ? 0.3784 0.2034 0.3540 0.0469  -0.0891 -0.0375 473  PHE B CD1 
2666 C CD2 . PHE B 87  ? 0.4264 0.2343 0.4042 0.0530  -0.1041 -0.0575 473  PHE B CD2 
2667 C CE1 . PHE B 87  ? 0.3698 0.2164 0.3404 0.0471  -0.0803 -0.0392 473  PHE B CE1 
2668 C CE2 . PHE B 87  ? 0.4114 0.2418 0.3836 0.0537  -0.0945 -0.0585 473  PHE B CE2 
2669 C CZ  . PHE B 87  ? 0.3890 0.2381 0.3581 0.0505  -0.0828 -0.0492 473  PHE B CZ  
2670 N N   . THR B 88  ? 0.4824 0.2644 0.4534 0.0651  -0.1058 -0.0314 474  THR B N   
2671 C CA  . THR B 88  ? 0.4089 0.2090 0.3735 0.0673  -0.0961 -0.0228 474  THR B CA  
2672 C C   . THR B 88  ? 0.4674 0.2839 0.4375 0.0518  -0.0859 -0.0120 474  THR B C   
2673 O O   . THR B 88  ? 0.4657 0.2775 0.4458 0.0395  -0.0865 -0.0088 474  THR B O   
2674 C CB  . THR B 88  ? 0.4510 0.2366 0.4148 0.0725  -0.1010 -0.0167 474  THR B CB  
2675 O OG1 . THR B 88  ? 0.4637 0.2339 0.4393 0.0594  -0.1045 -0.0068 474  THR B OG1 
2676 C CG2 . THR B 88  ? 0.4642 0.2320 0.4219 0.0893  -0.1119 -0.0286 474  THR B CG2 
2677 N N   . TYR B 89  ? 0.4271 0.2636 0.3909 0.0530  -0.0768 -0.0064 475  TYR B N   
2678 C CA  . TYR B 89  ? 0.3966 0.2499 0.3632 0.0406  -0.0674 0.0014  475  TYR B CA  
2679 C C   . TYR B 89  ? 0.4322 0.2984 0.3936 0.0409  -0.0614 0.0106  475  TYR B C   
2680 O O   . TYR B 89  ? 0.4185 0.2885 0.3735 0.0518  -0.0623 0.0094  475  TYR B O   
2681 C CB  . TYR B 89  ? 0.3832 0.2523 0.3475 0.0401  -0.0622 -0.0057 475  TYR B CB  
2682 C CG  . TYR B 89  ? 0.3465 0.2285 0.3017 0.0527  -0.0602 -0.0118 475  TYR B CG  
2683 C CD1 . TYR B 89  ? 0.3265 0.2279 0.2774 0.0528  -0.0527 -0.0065 475  TYR B CD1 
2684 C CD2 . TYR B 89  ? 0.3177 0.1932 0.2687 0.0647  -0.0660 -0.0225 475  TYR B CD2 
2685 C CE1 . TYR B 89  ? 0.2930 0.2082 0.2379 0.0636  -0.0506 -0.0102 475  TYR B CE1 
2686 C CE2 . TYR B 89  ? 0.3172 0.2071 0.2601 0.0768  -0.0632 -0.0266 475  TYR B CE2 
2687 C CZ  . TYR B 89  ? 0.3051 0.2155 0.2461 0.0757  -0.0552 -0.0197 475  TYR B CZ  
2688 O OH  . TYR B 89  ? 0.2779 0.2046 0.2132 0.0871  -0.0522 -0.0221 475  TYR B OH  
2689 N N   . ASP B 90  ? 0.3919 0.2658 0.3560 0.0294  -0.0555 0.0198  476  ASP B N   
2690 C CA  . ASP B 90  ? 0.4130 0.3023 0.3716 0.0281  -0.0493 0.0276  476  ASP B CA  
2691 C C   . ASP B 90  ? 0.3336 0.2412 0.2905 0.0224  -0.0418 0.0253  476  ASP B C   
2692 O O   . ASP B 90  ? 0.3407 0.2504 0.3015 0.0126  -0.0383 0.0282  476  ASP B O   
2693 C CB  . ASP B 90  ? 0.4674 0.3508 0.4284 0.0210  -0.0489 0.0399  476  ASP B CB  
2694 C CG  . ASP B 90  ? 0.6964 0.5659 0.6564 0.0284  -0.0553 0.0441  476  ASP B CG  
2695 O OD1 . ASP B 90  ? 0.6741 0.5328 0.6384 0.0231  -0.0572 0.0538  476  ASP B OD1 
2696 O OD2 . ASP B 90  ? 0.7019 0.5721 0.6571 0.0401  -0.0583 0.0382  476  ASP B OD2 
2697 N N   . LEU B 91  ? 0.3219 0.2430 0.2738 0.0288  -0.0396 0.0206  477  LEU B N   
2698 C CA  . LEU B 91  ? 0.3044 0.2412 0.2551 0.0242  -0.0337 0.0180  477  LEU B CA  
2699 C C   . LEU B 91  ? 0.3061 0.2553 0.2532 0.0190  -0.0292 0.0251  477  LEU B C   
2700 O O   . LEU B 91  ? 0.3308 0.2834 0.2744 0.0231  -0.0304 0.0297  477  LEU B O   
2701 C CB  . LEU B 91  ? 0.2747 0.2208 0.2230 0.0330  -0.0336 0.0109  477  LEU B CB  
2702 C CG  . LEU B 91  ? 0.3053 0.2655 0.2536 0.0291  -0.0285 0.0078  477  LEU B CG  
2703 C CD1 . LEU B 91  ? 0.2715 0.2251 0.2238 0.0229  -0.0281 0.0036  477  LEU B CD1 
2704 C CD2 . LEU B 91  ? 0.3030 0.2737 0.2493 0.0387  -0.0283 0.0036  477  LEU B CD2 
2705 N N   . TYR B 92  ? 0.3140 0.2697 0.2613 0.0107  -0.0246 0.0254  478  TYR B N   
2706 C CA  . TYR B 92  ? 0.2830 0.2498 0.2254 0.0062  -0.0210 0.0304  478  TYR B CA  
2707 C C   . TYR B 92  ? 0.3174 0.2938 0.2594 0.0017  -0.0170 0.0257  478  TYR B C   
2708 O O   . TYR B 92  ? 0.3329 0.3064 0.2789 -0.0001 -0.0160 0.0207  478  TYR B O   
2709 C CB  . TYR B 92  ? 0.2880 0.2496 0.2293 0.0009  -0.0200 0.0386  478  TYR B CB  
2710 C CG  . TYR B 92  ? 0.2800 0.2394 0.2254 -0.0066 -0.0165 0.0388  478  TYR B CG  
2711 C CD1 . TYR B 92  ? 0.2637 0.2114 0.2173 -0.0079 -0.0189 0.0372  478  TYR B CD1 
2712 C CD2 . TYR B 92  ? 0.3267 0.2959 0.2679 -0.0118 -0.0115 0.0404  478  TYR B CD2 
2713 C CE1 . TYR B 92  ? 0.2876 0.2353 0.2468 -0.0149 -0.0158 0.0382  478  TYR B CE1 
2714 C CE2 . TYR B 92  ? 0.3212 0.2905 0.2665 -0.0176 -0.0078 0.0411  478  TYR B CE2 
2715 C CZ  . TYR B 92  ? 0.2881 0.2475 0.2432 -0.0195 -0.0098 0.0405  478  TYR B CZ  
2716 O OH  . TYR B 92  ? 0.2351 0.1967 0.1962 -0.0255 -0.0062 0.0419  478  TYR B OH  
2717 N N   . LEU B 93  ? 0.2740 0.2614 0.2113 0.0000  -0.0156 0.0272  479  LEU B N   
2718 C CA  . LEU B 93  ? 0.3153 0.3109 0.2519 -0.0038 -0.0129 0.0228  479  LEU B CA  
2719 C C   . LEU B 93  ? 0.2623 0.2583 0.1952 -0.0099 -0.0096 0.0245  479  LEU B C   
2720 O O   . LEU B 93  ? 0.2963 0.2929 0.2239 -0.0109 -0.0094 0.0301  479  LEU B O   
2721 C CB  . LEU B 93  ? 0.2695 0.2763 0.2044 -0.0021 -0.0145 0.0229  479  LEU B CB  
2722 C CG  . LEU B 93  ? 0.2687 0.2797 0.2080 0.0047  -0.0166 0.0218  479  LEU B CG  
2723 C CD1 . LEU B 93  ? 0.3219 0.3431 0.2604 0.0070  -0.0192 0.0260  479  LEU B CD1 
2724 C CD2 . LEU B 93  ? 0.2074 0.2229 0.1507 0.0044  -0.0149 0.0168  479  LEU B CD2 
2725 N N   . VAL B 94  ? 0.2266 0.2231 0.1616 -0.0131 -0.0068 0.0198  480  VAL B N   
2726 C CA  . VAL B 94  ? 0.2325 0.2309 0.1639 -0.0176 -0.0030 0.0208  480  VAL B CA  
2727 C C   . VAL B 94  ? 0.3049 0.3108 0.2277 -0.0182 -0.0034 0.0206  480  VAL B C   
2728 O O   . VAL B 94  ? 0.2157 0.2257 0.1383 -0.0174 -0.0059 0.0170  480  VAL B O   
2729 C CB  . VAL B 94  ? 0.2416 0.2394 0.1779 -0.0197 -0.0003 0.0154  480  VAL B CB  
2730 C CG1 . VAL B 94  ? 0.2820 0.2840 0.2184 -0.0188 -0.0013 0.0092  480  VAL B CG1 
2731 C CG2 . VAL B 94  ? 0.2629 0.2638 0.1963 -0.0232 0.0042  0.0171  480  VAL B CG2 
2732 N N   . THR B 95  ? 0.2769 0.2848 0.1927 -0.0194 -0.0013 0.0248  481  THR B N   
2733 C CA  . THR B 95  ? 0.2548 0.2690 0.1605 -0.0193 -0.0023 0.0235  481  THR B CA  
2734 C C   . THR B 95  ? 0.3106 0.3277 0.2105 -0.0206 0.0019  0.0209  481  THR B C   
2735 O O   . THR B 95  ? 0.3501 0.3711 0.2412 -0.0198 0.0002  0.0170  481  THR B O   
2736 C CB  . THR B 95  ? 0.2764 0.2925 0.1752 -0.0174 -0.0042 0.0307  481  THR B CB  
2737 O OG1 . THR B 95  ? 0.2680 0.2814 0.1672 -0.0180 -0.0004 0.0382  481  THR B OG1 
2738 C CG2 . THR B 95  ? 0.2561 0.2711 0.1596 -0.0148 -0.0090 0.0325  481  THR B CG2 
2739 N N   . ASN B 96  ? 0.3067 0.3225 0.2118 -0.0221 0.0068  0.0226  482  ASN B N   
2740 C CA  . ASN B 96  ? 0.2794 0.3000 0.1802 -0.0223 0.0116  0.0206  482  ASN B CA  
2741 C C   . ASN B 96  ? 0.2529 0.2716 0.1600 -0.0231 0.0120  0.0126  482  ASN B C   
2742 O O   . ASN B 96  ? 0.2473 0.2646 0.1636 -0.0247 0.0147  0.0130  482  ASN B O   
2743 C CB  . ASN B 96  ? 0.2356 0.2585 0.1396 -0.0237 0.0170  0.0293  482  ASN B CB  
2744 C CG  . ASN B 96  ? 0.2303 0.2608 0.1316 -0.0232 0.0230  0.0280  482  ASN B CG  
2745 O OD1 . ASN B 96  ? 0.3281 0.3636 0.2176 -0.0199 0.0236  0.0234  482  ASN B OD1 
2746 N ND2 . ASN B 96  ? 0.2358 0.2675 0.1482 -0.0260 0.0270  0.0316  482  ASN B ND2 
2747 N N   . GLY B 97  ? 0.2370 0.2555 0.1397 -0.0222 0.0085  0.0057  483  GLY B N   
2748 C CA  . GLY B 97  ? 0.2177 0.2339 0.1261 -0.0227 0.0081  -0.0012 483  GLY B CA  
2749 C C   . GLY B 97  ? 0.2233 0.2359 0.1403 -0.0234 0.0045  -0.0017 483  GLY B C   
2750 O O   . GLY B 97  ? 0.2424 0.2549 0.1599 -0.0230 0.0013  0.0017  483  GLY B O   
2751 N N   . LYS B 98  ? 0.2307 0.2414 0.1544 -0.0237 0.0051  -0.0059 484  LYS B N   
2752 C CA  . LYS B 98  ? 0.2307 0.2399 0.1617 -0.0232 0.0023  -0.0066 484  LYS B CA  
2753 C C   . LYS B 98  ? 0.2224 0.2291 0.1613 -0.0225 0.0042  -0.0067 484  LYS B C   
2754 O O   . LYS B 98  ? 0.3137 0.3182 0.2552 -0.0224 0.0046  -0.0030 484  LYS B O   
2755 C CB  . LYS B 98  ? 0.2562 0.2655 0.1875 -0.0236 -0.0001 -0.0111 484  LYS B CB  
2756 C CG  . LYS B 98  ? 0.2609 0.2714 0.1856 -0.0247 -0.0040 -0.0118 484  LYS B CG  
2757 C CD  . LYS B 98  ? 0.4211 0.4335 0.3513 -0.0259 -0.0086 -0.0109 484  LYS B CD  
2758 C CE  . LYS B 98  ? 0.4889 0.4992 0.4245 -0.0265 -0.0088 -0.0142 484  LYS B CE  
2759 N NZ  . LYS B 98  ? 0.5145 0.5278 0.4562 -0.0285 -0.0133 -0.0118 484  LYS B NZ  
2760 N N   . HIS B 99  ? 0.2122 0.2185 0.1553 -0.0221 0.0046  -0.0110 485  HIS B N   
2761 C CA  . HIS B 99  ? 0.1814 0.1856 0.1317 -0.0210 0.0052  -0.0121 485  HIS B CA  
2762 C C   . HIS B 99  ? 0.2477 0.2520 0.2007 -0.0230 0.0084  -0.0111 485  HIS B C   
2763 O O   . HIS B 99  ? 0.2077 0.2093 0.1660 -0.0236 0.0079  -0.0085 485  HIS B O   
2764 C CB  . HIS B 99  ? 0.1831 0.1881 0.1365 -0.0195 0.0046  -0.0163 485  HIS B CB  
2765 C CG  . HIS B 99  ? 0.2145 0.2214 0.1674 -0.0179 0.0020  -0.0154 485  HIS B CG  
2766 N ND1 . HIS B 99  ? 0.2096 0.2182 0.1590 -0.0198 0.0005  -0.0147 485  HIS B ND1 
2767 C CD2 . HIS B 99  ? 0.1918 0.2004 0.1478 -0.0145 0.0004  -0.0146 485  HIS B CD2 
2768 C CE1 . HIS B 99  ? 0.1821 0.1940 0.1343 -0.0186 -0.0017 -0.0125 485  HIS B CE1 
2769 N NE2 . HIS B 99  ? 0.1735 0.1863 0.1291 -0.0148 -0.0012 -0.0123 485  HIS B NE2 
2770 N N   . GLY B 100 ? 0.2492 0.2569 0.1994 -0.0237 0.0115  -0.0129 486  GLY B N   
2771 C CA  . GLY B 100 ? 0.1591 0.1703 0.1127 -0.0252 0.0155  -0.0108 486  GLY B CA  
2772 C C   . GLY B 100 ? 0.2357 0.2514 0.1876 -0.0239 0.0186  -0.0148 486  GLY B C   
2773 O O   . GLY B 100 ? 0.2506 0.2652 0.2058 -0.0225 0.0176  -0.0196 486  GLY B O   
2774 N N   . LYS B 101 ? 0.2343 0.2554 0.1804 -0.0235 0.0225  -0.0129 487  LYS B N   
2775 C CA  . LYS B 101 ? 0.2572 0.2833 0.2005 -0.0207 0.0259  -0.0169 487  LYS B CA  
2776 C C   . LYS B 101 ? 0.3039 0.3396 0.2481 -0.0208 0.0319  -0.0113 487  LYS B C   
2777 O O   . LYS B 101 ? 0.2908 0.3287 0.2310 -0.0220 0.0332  -0.0051 487  LYS B O   
2778 C CB  . LYS B 101 ? 0.2640 0.2871 0.1950 -0.0177 0.0238  -0.0222 487  LYS B CB  
2779 C CG  . LYS B 101 ? 0.2617 0.2880 0.1885 -0.0133 0.0264  -0.0278 487  LYS B CG  
2780 C CD  . LYS B 101 ? 0.2860 0.3074 0.1999 -0.0102 0.0228  -0.0335 487  LYS B CD  
2781 C CE  . LYS B 101 ? 0.3124 0.3354 0.2210 -0.0043 0.0248  -0.0400 487  LYS B CE  
2782 N NZ  . LYS B 101 ? 0.2457 0.2621 0.1410 -0.0009 0.0200  -0.0468 487  LYS B NZ  
2783 N N   . LYS B 102 ? 0.2897 0.3324 0.2397 -0.0192 0.0357  -0.0127 488  LYS B N   
2784 C CA  . LYS B 102 ? 0.2626 0.3179 0.2151 -0.0188 0.0423  -0.0066 488  LYS B CA  
2785 C C   . LYS B 102 ? 0.2784 0.3390 0.2161 -0.0124 0.0457  -0.0100 488  LYS B C   
2786 O O   . LYS B 102 ? 0.3000 0.3600 0.2339 -0.0076 0.0455  -0.0178 488  LYS B O   
2787 C CB  . LYS B 102 ? 0.2809 0.3433 0.2481 -0.0198 0.0446  -0.0060 488  LYS B CB  
2788 C CG  . LYS B 102 ? 0.3399 0.4173 0.3143 -0.0210 0.0515  0.0030  488  LYS B CG  
2789 C CD  . LYS B 102 ? 0.3031 0.3868 0.2962 -0.0244 0.0518  0.0052  488  LYS B CD  
2790 C CE  . LYS B 102 ? 0.3446 0.4331 0.3381 -0.0187 0.0531  -0.0026 488  LYS B CE  
2791 N NZ  . LYS B 102 ? 0.5503 0.6483 0.5627 -0.0216 0.0538  0.0003  488  LYS B NZ  
2792 N N   . VAL B 103 ? 0.3065 0.3717 0.2351 -0.0116 0.0482  -0.0046 489  VAL B N   
2793 C CA  . VAL B 103 ? 0.3035 0.3743 0.2158 -0.0045 0.0510  -0.0079 489  VAL B CA  
2794 C C   . VAL B 103 ? 0.3467 0.4347 0.2604 -0.0026 0.0597  0.0013  489  VAL B C   
2795 O O   . VAL B 103 ? 0.3240 0.4160 0.2411 -0.0068 0.0618  0.0119  489  VAL B O   
2796 C CB  . VAL B 103 ? 0.2749 0.3380 0.1729 -0.0039 0.0460  -0.0095 489  VAL B CB  
2797 C CG1 . VAL B 103 ? 0.2657 0.3326 0.1456 0.0045  0.0470  -0.0156 489  VAL B CG1 
2798 C CG2 . VAL B 103 ? 0.2730 0.3215 0.1736 -0.0072 0.0378  -0.0156 489  VAL B CG2 
2799 N N   . ASN B 104 ? 0.2974 0.3960 0.2090 0.0040  0.0649  -0.0020 490  ASN B N   
2800 C CA  . ASN B 104 ? 0.3125 0.4312 0.2265 0.0069  0.0743  0.0073  490  ASN B CA  
2801 C C   . ASN B 104 ? 0.3874 0.5123 0.3227 -0.0023 0.0768  0.0196  490  ASN B C   
2802 O O   . ASN B 104 ? 0.3177 0.4535 0.2560 -0.0046 0.0819  0.0321  490  ASN B O   
2803 C CB  . ASN B 104 ? 0.2743 0.3994 0.1702 0.0120  0.0774  0.0113  490  ASN B CB  
2804 C CG  . ASN B 104 ? 0.3213 0.4412 0.1959 0.0220  0.0743  -0.0017 490  ASN B CG  
2805 O OD1 . ASN B 104 ? 0.2651 0.3884 0.1365 0.0293  0.0760  -0.0097 490  ASN B OD1 
2806 N ND2 . ASN B 104 ? 0.2877 0.3984 0.1478 0.0225  0.0688  -0.0042 490  ASN B ND2 
2807 N N   . ASN B 105 ? 0.3749 0.4923 0.3254 -0.0074 0.0725  0.0162  491  ASN B N   
2808 C CA  . ASN B 105 ? 0.3591 0.4791 0.3309 -0.0162 0.0722  0.0253  491  ASN B CA  
2809 C C   . ASN B 105 ? 0.3015 0.4117 0.2750 -0.0232 0.0683  0.0328  491  ASN B C   
2810 O O   . ASN B 105 ? 0.3936 0.5071 0.3830 -0.0303 0.0687  0.0430  491  ASN B O   
2811 C CB  . ASN B 105 ? 0.3174 0.4595 0.3011 -0.0161 0.0809  0.0355  491  ASN B CB  
2812 C CG  . ASN B 105 ? 0.3568 0.5020 0.3640 -0.0225 0.0790  0.0379  491  ASN B CG  
2813 O OD1 . ASN B 105 ? 0.4229 0.5544 0.4349 -0.0249 0.0717  0.0297  491  ASN B OD1 
2814 N ND2 . ASN B 105 ? 0.3875 0.5518 0.4098 -0.0253 0.0854  0.0496  491  ASN B ND2 
2815 N N   . VAL B 106 ? 0.3275 0.4255 0.2860 -0.0214 0.0639  0.0279  492  VAL B N   
2816 C CA  . VAL B 106 ? 0.3306 0.4188 0.2890 -0.0265 0.0597  0.0340  492  VAL B CA  
2817 C C   . VAL B 106 ? 0.3481 0.4191 0.3032 -0.0270 0.0513  0.0243  492  VAL B C   
2818 O O   . VAL B 106 ? 0.2595 0.3263 0.2018 -0.0222 0.0492  0.0152  492  VAL B O   
2819 C CB  . VAL B 106 ? 0.3638 0.4576 0.3068 -0.0231 0.0632  0.0402  492  VAL B CB  
2820 C CG1 . VAL B 106 ? 0.2517 0.3341 0.1943 -0.0275 0.0581  0.0456  492  VAL B CG1 
2821 C CG2 . VAL B 106 ? 0.3986 0.5118 0.3456 -0.0223 0.0724  0.0519  492  VAL B CG2 
2822 N N   . TRP B 107 ? 0.3311 0.3925 0.2977 -0.0326 0.0462  0.0265  493  TRP B N   
2823 C CA  . TRP B 107 ? 0.2831 0.3305 0.2480 -0.0325 0.0389  0.0184  493  TRP B CA  
2824 C C   . TRP B 107 ? 0.3077 0.3481 0.2619 -0.0318 0.0358  0.0202  493  TRP B C   
2825 O O   . TRP B 107 ? 0.3099 0.3504 0.2655 -0.0343 0.0364  0.0293  493  TRP B O   
2826 C CB  . TRP B 107 ? 0.2163 0.2570 0.1970 -0.0370 0.0345  0.0189  493  TRP B CB  
2827 C CG  . TRP B 107 ? 0.3027 0.3468 0.2921 -0.0365 0.0345  0.0129  493  TRP B CG  
2828 C CD1 . TRP B 107 ? 0.2493 0.3024 0.2526 -0.0394 0.0372  0.0168  493  TRP B CD1 
2829 C CD2 . TRP B 107 ? 0.2176 0.2568 0.2034 -0.0329 0.0315  0.0028  493  TRP B CD2 
2830 N NE1 . TRP B 107 ? 0.2610 0.3150 0.2687 -0.0373 0.0358  0.0090  493  TRP B NE1 
2831 C CE2 . TRP B 107 ? 0.1904 0.2356 0.1871 -0.0332 0.0324  0.0006  493  TRP B CE2 
2832 C CE3 . TRP B 107 ? 0.2204 0.2518 0.1959 -0.0298 0.0280  -0.0036 493  TRP B CE3 
2833 C CZ2 . TRP B 107 ? 0.2559 0.2984 0.2521 -0.0298 0.0300  -0.0079 493  TRP B CZ2 
2834 C CZ3 . TRP B 107 ? 0.2265 0.2556 0.2025 -0.0271 0.0259  -0.0112 493  TRP B CZ3 
2835 C CH2 . TRP B 107 ? 0.3183 0.3524 0.3038 -0.0269 0.0269  -0.0133 493  TRP B CH2 
2836 N N   . ASN B 108 ? 0.2410 0.2758 0.1856 -0.0287 0.0321  0.0123  494  ASN B N   
2837 C CA  . ASN B 108 ? 0.2553 0.2840 0.1917 -0.0281 0.0279  0.0132  494  ASN B CA  
2838 C C   . ASN B 108 ? 0.2419 0.2610 0.1841 -0.0288 0.0220  0.0091  494  ASN B C   
2839 O O   . ASN B 108 ? 0.2197 0.2362 0.1720 -0.0300 0.0210  0.0067  494  ASN B O   
2840 C CB  . ASN B 108 ? 0.2236 0.2548 0.1449 -0.0241 0.0277  0.0084  494  ASN B CB  
2841 C CG  . ASN B 108 ? 0.2718 0.2996 0.1918 -0.0221 0.0250  -0.0017 494  ASN B CG  
2842 O OD1 . ASN B 108 ? 0.2431 0.2662 0.1718 -0.0235 0.0226  -0.0048 494  ASN B OD1 
2843 N ND2 . ASN B 108 ? 0.2742 0.3041 0.1826 -0.0186 0.0249  -0.0067 494  ASN B ND2 
2844 N N   . GLY B 109 ? 0.1984 0.2136 0.1340 -0.0274 0.0180  0.0085  495  GLY B N   
2845 C CA  . GLY B 109 ? 0.2219 0.2308 0.1617 -0.0267 0.0132  0.0051  495  GLY B CA  
2846 C C   . GLY B 109 ? 0.2268 0.2297 0.1757 -0.0277 0.0111  0.0087  495  GLY B C   
2847 O O   . GLY B 109 ? 0.1887 0.1907 0.1403 -0.0298 0.0123  0.0155  495  GLY B O   
2848 N N   . MET B 110 ? 0.2295 0.2281 0.1831 -0.0259 0.0077  0.0040  496  MET B N   
2849 C CA  . MET B 110 ? 0.2231 0.2143 0.1840 -0.0254 0.0042  0.0051  496  MET B CA  
2850 C C   . MET B 110 ? 0.2341 0.2242 0.2046 -0.0290 0.0053  0.0065  496  MET B C   
2851 O O   . MET B 110 ? 0.2472 0.2311 0.2240 -0.0308 0.0029  0.0109  496  MET B O   
2852 C CB  . MET B 110 ? 0.1908 0.1796 0.1526 -0.0210 0.0005  -0.0008 496  MET B CB  
2853 C CG  . MET B 110 ? 0.1952 0.1858 0.1509 -0.0175 -0.0013 -0.0002 496  MET B CG  
2854 S SD  . MET B 110 ? 0.2332 0.2223 0.1908 -0.0109 -0.0051 -0.0047 496  MET B SD  
2855 C CE  . MET B 110 ? 0.1536 0.1499 0.1109 -0.0112 -0.0029 -0.0090 496  MET B CE  
2856 N N   . ILE B 111 ? 0.1892 0.1852 0.1621 -0.0301 0.0084  0.0031  497  ILE B N   
2857 C CA  . ILE B 111 ? 0.2223 0.2201 0.2060 -0.0338 0.0097  0.0050  497  ILE B CA  
2858 C C   . ILE B 111 ? 0.2711 0.2725 0.2565 -0.0378 0.0133  0.0146  497  ILE B C   
2859 O O   . ILE B 111 ? 0.2763 0.2746 0.2725 -0.0418 0.0117  0.0199  497  ILE B O   
2860 C CB  . ILE B 111 ? 0.2575 0.2629 0.2425 -0.0332 0.0129  -0.0001 497  ILE B CB  
2861 C CG1 . ILE B 111 ? 0.1831 0.1845 0.1704 -0.0301 0.0087  -0.0077 497  ILE B CG1 
2862 C CG2 . ILE B 111 ? 0.2172 0.2295 0.2124 -0.0373 0.0163  0.0043  497  ILE B CG2 
2863 C CD1 . ILE B 111 ? 0.2850 0.2871 0.2628 -0.0262 0.0088  -0.0122 497  ILE B CD1 
2864 N N   . GLY B 112 ? 0.2774 0.2854 0.2524 -0.0367 0.0177  0.0173  498  GLY B N   
2865 C CA  . GLY B 112 ? 0.2691 0.2823 0.2436 -0.0393 0.0217  0.0273  498  GLY B CA  
2866 C C   . GLY B 112 ? 0.3037 0.3080 0.2816 -0.0411 0.0178  0.0344  498  GLY B C   
2867 O O   . GLY B 112 ? 0.2788 0.2840 0.2649 -0.0454 0.0192  0.0437  498  GLY B O   
2868 N N   . GLU B 113 ? 0.2767 0.2725 0.2491 -0.0378 0.0128  0.0306  499  GLU B N   
2869 C CA  . GLU B 113 ? 0.3015 0.2872 0.2766 -0.0381 0.0083  0.0363  499  GLU B CA  
2870 C C   . GLU B 113 ? 0.3306 0.3075 0.3205 -0.0417 0.0040  0.0374  499  GLU B C   
2871 O O   . GLU B 113 ? 0.3399 0.3100 0.3360 -0.0447 0.0017  0.0456  499  GLU B O   
2872 C CB  . GLU B 113 ? 0.2920 0.2720 0.2597 -0.0326 0.0037  0.0310  499  GLU B CB  
2873 C CG  . GLU B 113 ? 0.2785 0.2658 0.2333 -0.0300 0.0059  0.0313  499  GLU B CG  
2874 C CD  . GLU B 113 ? 0.3409 0.3309 0.2907 -0.0313 0.0083  0.0414  499  GLU B CD  
2875 O OE1 . GLU B 113 ? 0.3928 0.3750 0.3464 -0.0317 0.0054  0.0480  499  GLU B OE1 
2876 O OE2 . GLU B 113 ? 0.3448 0.3444 0.2863 -0.0313 0.0128  0.0427  499  GLU B OE2 
2877 N N   . VAL B 114 ? 0.3188 0.2953 0.3147 -0.0416 0.0023  0.0294  500  VAL B N   
2878 C CA  . VAL B 114 ? 0.3278 0.2960 0.3380 -0.0449 -0.0031 0.0289  500  VAL B CA  
2879 C C   . VAL B 114 ? 0.3189 0.2957 0.3411 -0.0521 0.0010  0.0366  500  VAL B C   
2880 O O   . VAL B 114 ? 0.4053 0.3757 0.4405 -0.0574 -0.0028 0.0430  500  VAL B O   
2881 C CB  . VAL B 114 ? 0.2599 0.2249 0.2708 -0.0409 -0.0074 0.0171  500  VAL B CB  
2882 C CG1 . VAL B 114 ? 0.2701 0.2263 0.2952 -0.0441 -0.0143 0.0154  500  VAL B CG1 
2883 C CG2 . VAL B 114 ? 0.2861 0.2451 0.2862 -0.0335 -0.0108 0.0113  500  VAL B CG2 
2884 N N   . VAL B 115 ? 0.3169 0.3083 0.3355 -0.0520 0.0084  0.0363  501  VAL B N   
2885 C CA  . VAL B 115 ? 0.3517 0.3547 0.3818 -0.0576 0.0134  0.0438  501  VAL B CA  
2886 C C   . VAL B 115 ? 0.3840 0.3885 0.4180 -0.0622 0.0159  0.0581  501  VAL B C   
2887 O O   . VAL B 115 ? 0.3652 0.3699 0.4157 -0.0689 0.0146  0.0664  501  VAL B O   
2888 C CB  . VAL B 115 ? 0.3726 0.3909 0.3948 -0.0544 0.0212  0.0404  501  VAL B CB  
2889 C CG1 . VAL B 115 ? 0.3488 0.3825 0.3794 -0.0584 0.0285  0.0507  501  VAL B CG1 
2890 C CG2 . VAL B 115 ? 0.2789 0.2968 0.3033 -0.0518 0.0187  0.0289  501  VAL B CG2 
2891 N N   . TYR B 116 ? 0.3786 0.3844 0.3982 -0.0587 0.0191  0.0618  502  TYR B N   
2892 C CA  . TYR B 116 ? 0.3889 0.3977 0.4094 -0.0619 0.0223  0.0762  502  TYR B CA  
2893 C C   . TYR B 116 ? 0.4281 0.4194 0.4518 -0.0631 0.0146  0.0803  502  TYR B C   
2894 O O   . TYR B 116 ? 0.4641 0.4553 0.4840 -0.0637 0.0164  0.0913  502  TYR B O   
2895 C CB  . TYR B 116 ? 0.4553 0.4758 0.4576 -0.0568 0.0295  0.0781  502  TYR B CB  
2896 C CG  . TYR B 116 ? 0.5012 0.5374 0.5000 -0.0544 0.0364  0.0732  502  TYR B CG  
2897 C CD1 . TYR B 116 ? 0.4705 0.5218 0.4785 -0.0576 0.0432  0.0822  502  TYR B CD1 
2898 C CD2 . TYR B 116 ? 0.4117 0.4475 0.3989 -0.0488 0.0357  0.0601  502  TYR B CD2 
2899 C CE1 . TYR B 116 ? 0.4448 0.5106 0.4493 -0.0540 0.0494  0.0772  502  TYR B CE1 
2900 C CE2 . TYR B 116 ? 0.3933 0.4414 0.3772 -0.0459 0.0412  0.0552  502  TYR B CE2 
2901 C CZ  . TYR B 116 ? 0.5234 0.5864 0.5153 -0.0480 0.0481  0.0633  502  TYR B CZ  
2902 O OH  . TYR B 116 ? 0.5198 0.5953 0.5080 -0.0438 0.0535  0.0580  502  TYR B OH  
2903 N N   . GLN B 117 ? 0.4023 0.3788 0.4319 -0.0625 0.0060  0.0714  503  GLN B N   
2904 C CA  . GLN B 117 ? 0.3707 0.3288 0.4076 -0.0640 -0.0028 0.0745  503  GLN B CA  
2905 C C   . GLN B 117 ? 0.3335 0.2849 0.3570 -0.0587 -0.0040 0.0772  503  GLN B C   
2906 O O   . GLN B 117 ? 0.3468 0.2859 0.3752 -0.0603 -0.0088 0.0849  503  GLN B O   
2907 C CB  . GLN B 117 ? 0.3510 0.3083 0.4065 -0.0732 -0.0035 0.0881  503  GLN B CB  
2908 C CG  . GLN B 117 ? 0.4381 0.4059 0.5086 -0.0790 -0.0016 0.0874  503  GLN B CG  
2909 C CD  . GLN B 117 ? 0.4527 0.4201 0.5444 -0.0891 -0.0032 0.1019  503  GLN B CD  
2910 O OE1 . GLN B 117 ? 0.4407 0.4155 0.5336 -0.0924 0.0025  0.1170  503  GLN B OE1 
2911 N NE2 . GLN B 117 ? 0.5463 0.5060 0.6555 -0.0942 -0.0112 0.0978  503  GLN B NE2 
2912 N N   . ARG B 118 ? 0.3692 0.3281 0.3765 -0.0524 -0.0003 0.0709  504  ARG B N   
2913 C CA  . ARG B 118 ? 0.3176 0.2704 0.3131 -0.0465 -0.0029 0.0711  504  ARG B CA  
2914 C C   . ARG B 118 ? 0.3366 0.2771 0.3306 -0.0405 -0.0105 0.0599  504  ARG B C   
2915 O O   . ARG B 118 ? 0.3622 0.2961 0.3495 -0.0353 -0.0140 0.0604  504  ARG B O   
2916 C CB  . ARG B 118 ? 0.3687 0.3356 0.3484 -0.0428 0.0034  0.0702  504  ARG B CB  
2917 C CG  . ARG B 118 ? 0.3754 0.3533 0.3515 -0.0455 0.0101  0.0828  504  ARG B CG  
2918 C CD  . ARG B 118 ? 0.4850 0.4743 0.4437 -0.0406 0.0142  0.0801  504  ARG B CD  
2919 N NE  . ARG B 118 ? 0.4898 0.4899 0.4452 -0.0401 0.0187  0.0718  504  ARG B NE  
2920 C CZ  . ARG B 118 ? 0.5886 0.6008 0.5455 -0.0424 0.0255  0.0760  504  ARG B CZ  
2921 N NH1 . ARG B 118 ? 0.5424 0.5595 0.5045 -0.0460 0.0294  0.0895  504  ARG B NH1 
2922 N NH2 . ARG B 118 ? 0.5642 0.5844 0.5176 -0.0407 0.0286  0.0671  504  ARG B NH2 
2923 N N   . ALA B 119 ? 0.2791 0.2176 0.2790 -0.0404 -0.0131 0.0501  505  ALA B N   
2924 C CA  . ALA B 119 ? 0.3159 0.2443 0.3139 -0.0338 -0.0199 0.0394  505  ALA B CA  
2925 C C   . ALA B 119 ? 0.4049 0.3249 0.4155 -0.0364 -0.0256 0.0341  505  ALA B C   
2926 O O   . ALA B 119 ? 0.4004 0.3282 0.4184 -0.0420 -0.0224 0.0343  505  ALA B O   
2927 C CB  . ALA B 119 ? 0.2408 0.1795 0.2280 -0.0282 -0.0167 0.0306  505  ALA B CB  
2928 N N   . VAL B 120 ? 0.3538 0.2579 0.3664 -0.0318 -0.0345 0.0289  506  VAL B N   
2929 C CA  . VAL B 120 ? 0.2829 0.1774 0.3063 -0.0333 -0.0418 0.0222  506  VAL B CA  
2930 C C   . VAL B 120 ? 0.3772 0.2801 0.3960 -0.0288 -0.0405 0.0106  506  VAL B C   
2931 O O   . VAL B 120 ? 0.3056 0.2093 0.3334 -0.0325 -0.0427 0.0065  506  VAL B O   
2932 C CB  . VAL B 120 ? 0.3528 0.2262 0.3781 -0.0283 -0.0527 0.0190  506  VAL B CB  
2933 C CG1 . VAL B 120 ? 0.3525 0.2147 0.3883 -0.0294 -0.0620 0.0107  506  VAL B CG1 
2934 C CG2 . VAL B 120 ? 0.3986 0.2630 0.4295 -0.0331 -0.0541 0.0319  506  VAL B CG2 
2935 N N   . MET B 121 ? 0.2980 0.2082 0.3038 -0.0212 -0.0371 0.0059  507  MET B N   
2936 C CA  . MET B 121 ? 0.2968 0.2156 0.2980 -0.0170 -0.0354 -0.0033 507  MET B CA  
2937 C C   . MET B 121 ? 0.2794 0.2107 0.2690 -0.0131 -0.0287 -0.0027 507  MET B C   
2938 O O   . MET B 121 ? 0.2814 0.2137 0.2658 -0.0124 -0.0267 0.0032  507  MET B O   
2939 C CB  . MET B 121 ? 0.3232 0.2316 0.3233 -0.0088 -0.0439 -0.0137 507  MET B CB  
2940 C CG  . MET B 121 ? 0.3449 0.2476 0.3355 0.0013  -0.0469 -0.0159 507  MET B CG  
2941 S SD  . MET B 121 ? 0.4559 0.3463 0.4436 0.0127  -0.0572 -0.0288 507  MET B SD  
2942 C CE  . MET B 121 ? 0.2714 0.1425 0.2738 0.0050  -0.0671 -0.0283 507  MET B CE  
2943 N N   . ALA B 122 ? 0.2709 0.2117 0.2572 -0.0110 -0.0257 -0.0086 508  ALA B N   
2944 C CA  . ALA B 122 ? 0.2732 0.2257 0.2507 -0.0083 -0.0204 -0.0084 508  ALA B CA  
2945 C C   . ALA B 122 ? 0.2470 0.2025 0.2203 -0.0004 -0.0221 -0.0159 508  ALA B C   
2946 O O   . ALA B 122 ? 0.2913 0.2463 0.2679 0.0003  -0.0239 -0.0215 508  ALA B O   
2947 C CB  . ALA B 122 ? 0.2424 0.2053 0.2204 -0.0147 -0.0138 -0.0059 508  ALA B CB  
2948 N N   . VAL B 123 ? 0.2256 0.1856 0.1922 0.0057  -0.0216 -0.0153 509  VAL B N   
2949 C CA  . VAL B 123 ? 0.2198 0.1854 0.1822 0.0141  -0.0223 -0.0205 509  VAL B CA  
2950 C C   . VAL B 123 ? 0.2108 0.1899 0.1696 0.0135  -0.0171 -0.0170 509  VAL B C   
2951 O O   . VAL B 123 ? 0.2388 0.2209 0.1958 0.0112  -0.0154 -0.0116 509  VAL B O   
2952 C CB  . VAL B 123 ? 0.2625 0.2216 0.2215 0.0239  -0.0275 -0.0231 509  VAL B CB  
2953 C CG1 . VAL B 123 ? 0.2073 0.1735 0.1615 0.0337  -0.0279 -0.0285 509  VAL B CG1 
2954 C CG2 . VAL B 123 ? 0.3425 0.2851 0.3060 0.0232  -0.0342 -0.0258 509  VAL B CG2 
2955 N N   . GLY B 124 ? 0.2293 0.2160 0.1874 0.0153  -0.0152 -0.0198 510  GLY B N   
2956 C CA  . GLY B 124 ? 0.2236 0.2221 0.1802 0.0141  -0.0113 -0.0162 510  GLY B CA  
2957 C C   . GLY B 124 ? 0.1950 0.1983 0.1529 0.0129  -0.0092 -0.0187 510  GLY B C   
2958 O O   . GLY B 124 ? 0.2281 0.2283 0.1867 0.0162  -0.0110 -0.0236 510  GLY B O   
2959 N N   . SER B 125 ? 0.1454 0.1556 0.1037 0.0085  -0.0063 -0.0154 511  SER B N   
2960 C CA  . SER B 125 ? 0.1885 0.2024 0.1484 0.0068  -0.0044 -0.0167 511  SER B CA  
2961 C C   . SER B 125 ? 0.2056 0.2138 0.1674 0.0005  -0.0034 -0.0192 511  SER B C   
2962 O O   . SER B 125 ? 0.2198 0.2294 0.1816 -0.0041 -0.0015 -0.0183 511  SER B O   
2963 C CB  . SER B 125 ? 0.1702 0.1928 0.1309 0.0048  -0.0028 -0.0119 511  SER B CB  
2964 O OG  . SER B 125 ? 0.2184 0.2403 0.1784 -0.0006 -0.0030 -0.0091 511  SER B OG  
2965 N N   . LEU B 126 ? 0.1588 0.1605 0.1225 0.0009  -0.0051 -0.0225 512  LEU B N   
2966 C CA  . LEU B 126 ? 0.1427 0.1408 0.1098 -0.0047 -0.0039 -0.0236 512  LEU B CA  
2967 C C   . LEU B 126 ? 0.1899 0.1887 0.1604 -0.0033 -0.0044 -0.0281 512  LEU B C   
2968 O O   . LEU B 126 ? 0.1722 0.1682 0.1442 0.0008  -0.0079 -0.0316 512  LEU B O   
2969 C CB  . LEU B 126 ? 0.1534 0.1446 0.1230 -0.0065 -0.0060 -0.0225 512  LEU B CB  
2970 C CG  . LEU B 126 ? 0.1970 0.1872 0.1710 -0.0129 -0.0037 -0.0207 512  LEU B CG  
2971 C CD1 . LEU B 126 ? 0.1689 0.1635 0.1380 -0.0162 0.0003  -0.0170 512  LEU B CD1 
2972 C CD2 . LEU B 126 ? 0.1641 0.1470 0.1428 -0.0146 -0.0067 -0.0186 512  LEU B CD2 
2973 N N   . THR B 127 ? 0.1980 0.2001 0.1693 -0.0062 -0.0015 -0.0283 513  THR B N   
2974 C CA  . THR B 127 ? 0.2116 0.2154 0.1857 -0.0043 -0.0019 -0.0320 513  THR B CA  
2975 C C   . THR B 127 ? 0.1479 0.1498 0.1287 -0.0069 -0.0028 -0.0343 513  THR B C   
2976 O O   . THR B 127 ? 0.1640 0.1660 0.1473 -0.0117 -0.0004 -0.0321 513  THR B O   
2977 C CB  . THR B 127 ? 0.1525 0.1596 0.1252 -0.0057 0.0010  -0.0313 513  THR B CB  
2978 O OG1 . THR B 127 ? 0.2158 0.2253 0.1848 -0.0040 0.0009  -0.0283 513  THR B OG1 
2979 C CG2 . THR B 127 ? 0.1373 0.1461 0.1132 -0.0035 0.0006  -0.0346 513  THR B CG2 
2980 N N   . ILE B 128 ? 0.1377 0.1390 0.1218 -0.0034 -0.0065 -0.0384 514  ILE B N   
2981 C CA  . ILE B 128 ? 0.1703 0.1711 0.1630 -0.0062 -0.0084 -0.0407 514  ILE B CA  
2982 C C   . ILE B 128 ? 0.1708 0.1777 0.1662 -0.0073 -0.0050 -0.0413 514  ILE B C   
2983 O O   . ILE B 128 ? 0.1589 0.1683 0.1512 -0.0031 -0.0050 -0.0432 514  ILE B O   
2984 C CB  . ILE B 128 ? 0.1910 0.1884 0.1857 -0.0015 -0.0151 -0.0458 514  ILE B CB  
2985 C CG1 . ILE B 128 ? 0.2373 0.2271 0.2291 0.0006  -0.0191 -0.0461 514  ILE B CG1 
2986 C CG2 . ILE B 128 ? 0.2176 0.2158 0.2232 -0.0050 -0.0180 -0.0481 514  ILE B CG2 
2987 C CD1 . ILE B 128 ? 0.1614 0.1474 0.1508 0.0081  -0.0261 -0.0526 514  ILE B CD1 
2988 N N   . ASN B 129 ? 0.1640 0.1739 0.1651 -0.0122 -0.0019 -0.0391 515  ASN B N   
2989 C CA  . ASN B 129 ? 0.2386 0.2550 0.2436 -0.0122 0.0009  -0.0403 515  ASN B CA  
2990 C C   . ASN B 129 ? 0.2434 0.2645 0.2598 -0.0167 0.0014  -0.0386 515  ASN B C   
2991 O O   . ASN B 129 ? 0.1673 0.1856 0.1886 -0.0206 -0.0004 -0.0358 515  ASN B O   
2992 C CB  . ASN B 129 ? 0.1838 0.2017 0.1815 -0.0119 0.0060  -0.0390 515  ASN B CB  
2993 C CG  . ASN B 129 ? 0.2375 0.2558 0.2326 -0.0158 0.0096  -0.0349 515  ASN B CG  
2994 O OD1 . ASN B 129 ? 0.2392 0.2590 0.2402 -0.0194 0.0100  -0.0319 515  ASN B OD1 
2995 N ND2 . ASN B 129 ? 0.1604 0.1772 0.1469 -0.0151 0.0118  -0.0345 515  ASN B ND2 
2996 N N   . GLU B 130 ? 0.2275 0.2563 0.2492 -0.0160 0.0038  -0.0397 516  GLU B N   
2997 C CA  . GLU B 130 ? 0.2557 0.2921 0.2911 -0.0199 0.0039  -0.0376 516  GLU B CA  
2998 C C   . GLU B 130 ? 0.2662 0.3064 0.3039 -0.0249 0.0089  -0.0309 516  GLU B C   
2999 O O   . GLU B 130 ? 0.2483 0.2893 0.2964 -0.0302 0.0070  -0.0268 516  GLU B O   
3000 C CB  . GLU B 130 ? 0.2151 0.2606 0.2551 -0.0168 0.0059  -0.0400 516  GLU B CB  
3001 C CG  . GLU B 130 ? 0.1940 0.2505 0.2504 -0.0207 0.0061  -0.0372 516  GLU B CG  
3002 C CD  . GLU B 130 ? 0.2630 0.3305 0.3235 -0.0166 0.0093  -0.0389 516  GLU B CD  
3003 O OE1 . GLU B 130 ? 0.2611 0.3265 0.3107 -0.0112 0.0124  -0.0416 516  GLU B OE1 
3004 O OE2 . GLU B 130 ? 0.3661 0.4440 0.4415 -0.0188 0.0083  -0.0374 516  GLU B OE2 
3005 N N   . GLU B 131 ? 0.2451 0.2876 0.2732 -0.0232 0.0150  -0.0296 517  GLU B N   
3006 C CA  . GLU B 131 ? 0.2916 0.3403 0.3205 -0.0265 0.0205  -0.0231 517  GLU B CA  
3007 C C   . GLU B 131 ? 0.3088 0.3502 0.3362 -0.0307 0.0185  -0.0184 517  GLU B C   
3008 O O   . GLU B 131 ? 0.2439 0.2903 0.2767 -0.0350 0.0215  -0.0112 517  GLU B O   
3009 C CB  . GLU B 131 ? 0.2090 0.2606 0.2256 -0.0223 0.0262  -0.0243 517  GLU B CB  
3010 C CG  . GLU B 131 ? 0.3211 0.3626 0.3236 -0.0208 0.0248  -0.0261 517  GLU B CG  
3011 C CD  . GLU B 131 ? 0.3412 0.3850 0.3323 -0.0174 0.0292  -0.0272 517  GLU B CD  
3012 O OE1 . GLU B 131 ? 0.3329 0.3859 0.3258 -0.0147 0.0336  -0.0276 517  GLU B OE1 
3013 O OE2 . GLU B 131 ? 0.3685 0.4053 0.3490 -0.0171 0.0279  -0.0279 517  GLU B OE2 
3014 N N   . ARG B 132 ? 0.3040 0.3343 0.3243 -0.0291 0.0138  -0.0216 518  ARG B N   
3015 C CA  . ARG B 132 ? 0.2498 0.2724 0.2692 -0.0320 0.0111  -0.0176 518  ARG B CA  
3016 C C   . ARG B 132 ? 0.3198 0.3388 0.3525 -0.0358 0.0052  -0.0166 518  ARG B C   
3017 O O   . ARG B 132 ? 0.2932 0.3094 0.3313 -0.0404 0.0043  -0.0104 518  ARG B O   
3018 C CB  . ARG B 132 ? 0.2223 0.2362 0.2302 -0.0281 0.0082  -0.0212 518  ARG B CB  
3019 C CG  . ARG B 132 ? 0.2747 0.2901 0.2706 -0.0262 0.0124  -0.0207 518  ARG B CG  
3020 C CD  . ARG B 132 ? 0.1843 0.1939 0.1720 -0.0226 0.0093  -0.0240 518  ARG B CD  
3021 N NE  . ARG B 132 ? 0.2006 0.2112 0.1786 -0.0218 0.0119  -0.0236 518  ARG B NE  
3022 C CZ  . ARG B 132 ? 0.2398 0.2475 0.2117 -0.0197 0.0099  -0.0246 518  ARG B CZ  
3023 N NH1 . ARG B 132 ? 0.2345 0.2394 0.2076 -0.0172 0.0064  -0.0258 518  ARG B NH1 
3024 N NH2 . ARG B 132 ? 0.1778 0.1861 0.1423 -0.0198 0.0112  -0.0245 518  ARG B NH2 
3025 N N   . SER B 133 ? 0.2390 0.2575 0.2774 -0.0338 0.0005  -0.0225 519  SER B N   
3026 C CA  . SER B 133 ? 0.2369 0.2514 0.2885 -0.0373 -0.0067 -0.0230 519  SER B CA  
3027 C C   . SER B 133 ? 0.2913 0.3148 0.3587 -0.0444 -0.0045 -0.0156 519  SER B C   
3028 O O   . SER B 133 ? 0.2915 0.3108 0.3721 -0.0493 -0.0109 -0.0138 519  SER B O   
3029 C CB  . SER B 133 ? 0.2369 0.2508 0.2901 -0.0328 -0.0123 -0.0313 519  SER B CB  
3030 O OG  . SER B 133 ? 0.2797 0.2873 0.3190 -0.0259 -0.0138 -0.0366 519  SER B OG  
3031 N N   . GLU B 134 ? 0.3036 0.3400 0.3705 -0.0449 0.0042  -0.0110 520  GLU B N   
3032 C CA  . GLU B 134 ? 0.2610 0.3092 0.3429 -0.0511 0.0078  -0.0021 520  GLU B CA  
3033 C C   . GLU B 134 ? 0.2753 0.3199 0.3585 -0.0564 0.0092  0.0075  520  GLU B C   
3034 O O   . GLU B 134 ? 0.3135 0.3632 0.4128 -0.0634 0.0087  0.0160  520  GLU B O   
3035 C CB  . GLU B 134 ? 0.2507 0.3150 0.3300 -0.0479 0.0171  -0.0007 520  GLU B CB  
3036 C CG  . GLU B 134 ? 0.3394 0.4098 0.4220 -0.0436 0.0159  -0.0079 520  GLU B CG  
3037 C CD  . GLU B 134 ? 0.3493 0.4331 0.4266 -0.0385 0.0247  -0.0076 520  GLU B CD  
3038 O OE1 . GLU B 134 ? 0.4191 0.5098 0.4920 -0.0389 0.0318  -0.0013 520  GLU B OE1 
3039 O OE2 . GLU B 134 ? 0.4647 0.5520 0.5414 -0.0335 0.0243  -0.0139 520  GLU B OE2 
3040 N N   . VAL B 135 ? 0.2645 0.3006 0.3318 -0.0533 0.0106  0.0071  521  VAL B N   
3041 C CA  . VAL B 135 ? 0.2645 0.2975 0.3308 -0.0572 0.0123  0.0165  521  VAL B CA  
3042 C C   . VAL B 135 ? 0.2625 0.2776 0.3265 -0.0574 0.0041  0.0145  521  VAL B C   
3043 O O   . VAL B 135 ? 0.3398 0.3500 0.4078 -0.0618 0.0031  0.0230  521  VAL B O   
3044 C CB  . VAL B 135 ? 0.2892 0.3287 0.3395 -0.0533 0.0207  0.0190  521  VAL B CB  
3045 C CG1 . VAL B 135 ? 0.2921 0.3499 0.3454 -0.0526 0.0292  0.0227  521  VAL B CG1 
3046 C CG2 . VAL B 135 ? 0.2447 0.2769 0.2786 -0.0465 0.0193  0.0092  521  VAL B CG2 
3047 N N   . VAL B 136 ? 0.2682 0.2737 0.3254 -0.0522 -0.0018 0.0042  522  VAL B N   
3048 C CA  . VAL B 136 ? 0.2610 0.2503 0.3155 -0.0505 -0.0098 0.0012  522  VAL B CA  
3049 C C   . VAL B 136 ? 0.3196 0.3027 0.3790 -0.0479 -0.0183 -0.0084 522  VAL B C   
3050 O O   . VAL B 136 ? 0.3210 0.3122 0.3827 -0.0463 -0.0173 -0.0132 522  VAL B O   
3051 C CB  . VAL B 136 ? 0.2070 0.1917 0.2438 -0.0443 -0.0080 -0.0013 522  VAL B CB  
3052 C CG1 . VAL B 136 ? 0.2205 0.2117 0.2510 -0.0462 -0.0006 0.0072  522  VAL B CG1 
3053 C CG2 . VAL B 136 ? 0.2386 0.2272 0.2660 -0.0380 -0.0068 -0.0100 522  VAL B CG2 
3054 N N   . ASP B 137 ? 0.2397 0.2080 0.2998 -0.0465 -0.0270 -0.0115 523  ASP B N   
3055 C CA  . ASP B 137 ? 0.2221 0.1827 0.2826 -0.0416 -0.0360 -0.0220 523  ASP B CA  
3056 C C   . ASP B 137 ? 0.2442 0.2012 0.2873 -0.0318 -0.0358 -0.0288 523  ASP B C   
3057 O O   . ASP B 137 ? 0.2561 0.2090 0.2902 -0.0295 -0.0337 -0.0258 523  ASP B O   
3058 C CB  . ASP B 137 ? 0.2939 0.2396 0.3655 -0.0449 -0.0470 -0.0224 523  ASP B CB  
3059 C CG  . ASP B 137 ? 0.3013 0.2512 0.3933 -0.0538 -0.0506 -0.0190 523  ASP B CG  
3060 O OD1 . ASP B 137 ? 0.3352 0.3006 0.4318 -0.0557 -0.0448 -0.0180 523  ASP B OD1 
3061 O OD2 . ASP B 137 ? 0.3063 0.2443 0.4106 -0.0589 -0.0597 -0.0172 523  ASP B OD2 
3062 N N   . PHE B 138 ? 0.2403 0.2002 0.2792 -0.0258 -0.0380 -0.0371 524  PHE B N   
3063 C CA  . PHE B 138 ? 0.2648 0.2240 0.2887 -0.0163 -0.0376 -0.0426 524  PHE B CA  
3064 C C   . PHE B 138 ? 0.2440 0.1936 0.2659 -0.0092 -0.0476 -0.0517 524  PHE B C   
3065 O O   . PHE B 138 ? 0.3093 0.2575 0.3394 -0.0104 -0.0540 -0.0564 524  PHE B O   
3066 C CB  . PHE B 138 ? 0.2733 0.2449 0.2916 -0.0138 -0.0309 -0.0438 524  PHE B CB  
3067 C CG  . PHE B 138 ? 0.2598 0.2383 0.2725 -0.0163 -0.0219 -0.0374 524  PHE B CG  
3068 C CD1 . PHE B 138 ? 0.2247 0.2013 0.2270 -0.0126 -0.0199 -0.0357 524  PHE B CD1 
3069 C CD2 . PHE B 138 ? 0.2395 0.2269 0.2573 -0.0215 -0.0160 -0.0335 524  PHE B CD2 
3070 C CE1 . PHE B 138 ? 0.2032 0.1856 0.2004 -0.0149 -0.0131 -0.0307 524  PHE B CE1 
3071 C CE2 . PHE B 138 ? 0.2712 0.2639 0.2823 -0.0227 -0.0088 -0.0291 524  PHE B CE2 
3072 C CZ  . PHE B 138 ? 0.1838 0.1735 0.1848 -0.0198 -0.0079 -0.0279 524  PHE B CZ  
3073 N N   . SER B 139 ? 0.2722 0.2158 0.2827 -0.0012 -0.0494 -0.0543 525  SER B N   
3074 C CA  . SER B 139 ? 0.2844 0.2209 0.2890 0.0086  -0.0580 -0.0639 525  SER B CA  
3075 C C   . SER B 139 ? 0.2997 0.2470 0.2982 0.0145  -0.0561 -0.0687 525  SER B C   
3076 O O   . SER B 139 ? 0.2667 0.2254 0.2666 0.0108  -0.0486 -0.0646 525  SER B O   
3077 C CB  . SER B 139 ? 0.2813 0.2117 0.2746 0.0170  -0.0589 -0.0647 525  SER B CB  
3078 O OG  . SER B 139 ? 0.2772 0.2199 0.2607 0.0212  -0.0502 -0.0613 525  SER B OG  
3079 N N   . VAL B 140 ? 0.2754 0.2189 0.2666 0.0248  -0.0632 -0.0774 526  VAL B N   
3080 C CA  . VAL B 140 ? 0.2217 0.1759 0.2047 0.0324  -0.0610 -0.0810 526  VAL B CA  
3081 C C   . VAL B 140 ? 0.2725 0.2371 0.2466 0.0352  -0.0510 -0.0744 526  VAL B C   
3082 O O   . VAL B 140 ? 0.2764 0.2381 0.2467 0.0362  -0.0489 -0.0709 526  VAL B O   
3083 C CB  . VAL B 140 ? 0.2817 0.2305 0.2560 0.0447  -0.0705 -0.0915 526  VAL B CB  
3084 C CG1 . VAL B 140 ? 0.2335 0.1728 0.2182 0.0410  -0.0818 -0.0986 526  VAL B CG1 
3085 C CG2 . VAL B 140 ? 0.2993 0.2401 0.2644 0.0530  -0.0730 -0.0934 526  VAL B CG2 
3086 N N   . PRO B 141 ? 0.2272 0.2037 0.1988 0.0360  -0.0451 -0.0720 527  PRO B N   
3087 C CA  . PRO B 141 ? 0.2158 0.2015 0.1801 0.0385  -0.0370 -0.0656 527  PRO B CA  
3088 C C   . PRO B 141 ? 0.2249 0.2126 0.1780 0.0508  -0.0388 -0.0680 527  PRO B C   
3089 O O   . PRO B 141 ? 0.2254 0.2117 0.1729 0.0599  -0.0447 -0.0753 527  PRO B O   
3090 C CB  . PRO B 141 ? 0.2753 0.2710 0.2404 0.0374  -0.0327 -0.0636 527  PRO B CB  
3091 C CG  . PRO B 141 ? 0.1941 0.1874 0.1619 0.0400  -0.0397 -0.0710 527  PRO B CG  
3092 C CD  . PRO B 141 ? 0.2197 0.2014 0.1957 0.0346  -0.0462 -0.0745 527  PRO B CD  
3093 N N   . PHE B 142 ? 0.2551 0.2466 0.2047 0.0517  -0.0338 -0.0621 528  PHE B N   
3094 C CA  . PHE B 142 ? 0.3019 0.2985 0.2415 0.0639  -0.0340 -0.0629 528  PHE B CA  
3095 C C   . PHE B 142 ? 0.2146 0.2265 0.1513 0.0655  -0.0259 -0.0542 528  PHE B C   
3096 O O   . PHE B 142 ? 0.2687 0.2889 0.1979 0.0762  -0.0248 -0.0533 528  PHE B O   
3097 C CB  . PHE B 142 ? 0.1995 0.1862 0.1380 0.0663  -0.0377 -0.0645 528  PHE B CB  
3098 C CG  . PHE B 142 ? 0.2389 0.2247 0.1831 0.0566  -0.0331 -0.0567 528  PHE B CG  
3099 C CD1 . PHE B 142 ? 0.2558 0.2326 0.2088 0.0451  -0.0340 -0.0555 528  PHE B CD1 
3100 C CD2 . PHE B 142 ? 0.2388 0.2338 0.1796 0.0596  -0.0281 -0.0503 528  PHE B CD2 
3101 C CE1 . PHE B 142 ? 0.2417 0.2185 0.1981 0.0374  -0.0299 -0.0484 528  PHE B CE1 
3102 C CE2 . PHE B 142 ? 0.2404 0.2347 0.1857 0.0512  -0.0248 -0.0437 528  PHE B CE2 
3103 C CZ  . PHE B 142 ? 0.2395 0.2243 0.1916 0.0405  -0.0258 -0.0431 528  PHE B CZ  
3104 N N   . VAL B 143 ? 0.2113 0.2272 0.1542 0.0555  -0.0205 -0.0477 529  VAL B N   
3105 C CA  . VAL B 143 ? 0.2305 0.2597 0.1728 0.0555  -0.0142 -0.0395 529  VAL B CA  
3106 C C   . VAL B 143 ? 0.1721 0.2023 0.1189 0.0490  -0.0123 -0.0383 529  VAL B C   
3107 O O   . VAL B 143 ? 0.2033 0.2270 0.1561 0.0395  -0.0118 -0.0384 529  VAL B O   
3108 C CB  . VAL B 143 ? 0.2003 0.2323 0.1458 0.0498  -0.0104 -0.0323 529  VAL B CB  
3109 C CG1 . VAL B 143 ? 0.1533 0.1977 0.1010 0.0476  -0.0052 -0.0236 529  VAL B CG1 
3110 C CG2 . VAL B 143 ? 0.1638 0.1964 0.1049 0.0576  -0.0120 -0.0328 529  VAL B CG2 
3111 N N   . GLU B 144 ? 0.2245 0.2633 0.1679 0.0551  -0.0111 -0.0368 530  GLU B N   
3112 C CA  . GLU B 144 ? 0.2228 0.2624 0.1700 0.0504  -0.0097 -0.0355 530  GLU B CA  
3113 C C   . GLU B 144 ? 0.2301 0.2713 0.1830 0.0412  -0.0051 -0.0279 530  GLU B C   
3114 O O   . GLU B 144 ? 0.3159 0.3646 0.2688 0.0417  -0.0020 -0.0206 530  GLU B O   
3115 C CB  . GLU B 144 ? 0.2430 0.2921 0.1844 0.0598  -0.0094 -0.0342 530  GLU B CB  
3116 C CG  . GLU B 144 ? 0.4642 0.5112 0.4077 0.0586  -0.0112 -0.0372 530  GLU B CG  
3117 C CD  . GLU B 144 ? 0.4581 0.5157 0.3952 0.0682  -0.0104 -0.0342 530  GLU B CD  
3118 O OE1 . GLU B 144 ? 0.4841 0.5449 0.4243 0.0655  -0.0078 -0.0286 530  GLU B OE1 
3119 O OE2 . GLU B 144 ? 0.3924 0.4548 0.3208 0.0792  -0.0126 -0.0373 530  GLU B OE2 
3120 N N   . THR B 145 ? 0.1774 0.2119 0.1355 0.0333  -0.0050 -0.0296 531  THR B N   
3121 C CA  . THR B 145 ? 0.1964 0.2301 0.1587 0.0253  -0.0020 -0.0244 531  THR B CA  
3122 C C   . THR B 145 ? 0.2508 0.2798 0.2167 0.0211  -0.0020 -0.0270 531  THR B C   
3123 O O   . THR B 145 ? 0.2410 0.2691 0.2072 0.0242  -0.0041 -0.0319 531  THR B O   
3124 C CB  . THR B 145 ? 0.2181 0.2476 0.1815 0.0197  -0.0016 -0.0239 531  THR B CB  
3125 O OG1 . THR B 145 ? 0.2426 0.2727 0.2087 0.0135  0.0004  -0.0187 531  THR B OG1 
3126 C CG2 . THR B 145 ? 0.1731 0.1942 0.1386 0.0157  -0.0032 -0.0297 531  THR B CG2 
3127 N N   . GLY B 146 ? 0.2507 0.2769 0.2194 0.0146  -0.0002 -0.0242 532  GLY B N   
3128 C CA  . GLY B 146 ? 0.2270 0.2489 0.1986 0.0116  0.0002  -0.0264 532  GLY B CA  
3129 C C   . GLY B 146 ? 0.2439 0.2628 0.2167 0.0064  0.0012  -0.0224 532  GLY B C   
3130 O O   . GLY B 146 ? 0.2416 0.2597 0.2139 0.0025  0.0014  -0.0205 532  GLY B O   
3131 N N   . ILE B 147 ? 0.1947 0.2114 0.1692 0.0066  0.0010  -0.0214 533  ILE B N   
3132 C CA  . ILE B 147 ? 0.2381 0.2496 0.2143 0.0020  0.0004  -0.0186 533  ILE B CA  
3133 C C   . ILE B 147 ? 0.2784 0.2930 0.2572 0.0034  -0.0002 -0.0108 533  ILE B C   
3134 O O   . ILE B 147 ? 0.3218 0.3382 0.3008 0.0080  -0.0001 -0.0099 533  ILE B O   
3135 C CB  . ILE B 147 ? 0.2576 0.2618 0.2339 0.0010  0.0002  -0.0242 533  ILE B CB  
3136 C CG1 . ILE B 147 ? 0.2528 0.2563 0.2273 -0.0007 0.0016  -0.0299 533  ILE B CG1 
3137 C CG2 . ILE B 147 ? 0.2354 0.2319 0.2125 -0.0025 -0.0020 -0.0223 533  ILE B CG2 
3138 C CD1 . ILE B 147 ? 0.2719 0.2711 0.2462 -0.0005 0.0023  -0.0350 533  ILE B CD1 
3139 N N   . SER B 148 ? 0.2614 0.2774 0.2427 -0.0006 -0.0010 -0.0044 534  SER B N   
3140 C CA  . SER B 148 ? 0.2266 0.2461 0.2128 -0.0011 -0.0017 0.0051  534  SER B CA  
3141 C C   . SER B 148 ? 0.2213 0.2318 0.2121 -0.0084 -0.0052 0.0074  534  SER B C   
3142 O O   . SER B 148 ? 0.2340 0.2375 0.2226 -0.0123 -0.0070 0.0013  534  SER B O   
3143 C CB  . SER B 148 ? 0.1909 0.2237 0.1779 0.0015  0.0004  0.0127  534  SER B CB  
3144 O OG  . SER B 148 ? 0.2395 0.2794 0.2213 0.0097  0.0025  0.0103  534  SER B OG  
3145 N N   . VAL B 149 ? 0.2205 0.2314 0.2177 -0.0102 -0.0068 0.0163  535  VAL B N   
3146 C CA  . VAL B 149 ? 0.2615 0.2625 0.2648 -0.0176 -0.0119 0.0191  535  VAL B CA  
3147 C C   . VAL B 149 ? 0.2941 0.3052 0.3066 -0.0216 -0.0125 0.0322  535  VAL B C   
3148 O O   . VAL B 149 ? 0.2849 0.3045 0.3015 -0.0188 -0.0103 0.0418  535  VAL B O   
3149 C CB  . VAL B 149 ? 0.2559 0.2444 0.2606 -0.0169 -0.0148 0.0179  535  VAL B CB  
3150 C CG1 . VAL B 149 ? 0.2834 0.2588 0.2939 -0.0244 -0.0216 0.0190  535  VAL B CG1 
3151 C CG2 . VAL B 149 ? 0.2985 0.2809 0.2952 -0.0117 -0.0133 0.0060  535  VAL B CG2 
3152 N N   . MET B 150 ? 0.2347 0.2463 0.2509 -0.0278 -0.0154 0.0331  536  MET B N   
3153 C CA  . MET B 150 ? 0.2471 0.2693 0.2744 -0.0328 -0.0166 0.0460  536  MET B CA  
3154 C C   . MET B 150 ? 0.2518 0.2615 0.2888 -0.0412 -0.0241 0.0500  536  MET B C   
3155 O O   . MET B 150 ? 0.2677 0.2623 0.3018 -0.0450 -0.0298 0.0408  536  MET B O   
3156 C CB  . MET B 150 ? 0.2195 0.2508 0.2466 -0.0346 -0.0162 0.0454  536  MET B CB  
3157 C CG  . MET B 150 ? 0.1703 0.2137 0.2110 -0.0406 -0.0182 0.0588  536  MET B CG  
3158 S SD  . MET B 150 ? 0.3761 0.4333 0.4167 -0.0407 -0.0171 0.0589  536  MET B SD  
3159 C CE  . MET B 150 ? 0.1923 0.2712 0.2307 -0.0300 -0.0082 0.0665  536  MET B CE  
3160 N N   . VAL B 151 ? 0.1901 0.2061 0.2385 -0.0437 -0.0244 0.0640  537  VAL B N   
3161 C CA  . VAL B 151 ? 0.2526 0.2566 0.3129 -0.0525 -0.0324 0.0701  537  VAL B CA  
3162 C C   . VAL B 151 ? 0.2449 0.2656 0.3212 -0.0582 -0.0323 0.0879  537  VAL B C   
3163 O O   . VAL B 151 ? 0.2500 0.2918 0.3266 -0.0532 -0.0249 0.0958  537  VAL B O   
3164 C CB  . VAL B 151 ? 0.2828 0.2734 0.3424 -0.0498 -0.0337 0.0703  537  VAL B CB  
3165 C CG1 . VAL B 151 ? 0.3422 0.3179 0.3876 -0.0440 -0.0339 0.0532  537  VAL B CG1 
3166 C CG2 . VAL B 151 ? 0.2218 0.2283 0.2824 -0.0433 -0.0263 0.0817  537  VAL B CG2 
3167 N N   . SER B 152 ? 0.2660 0.2774 0.3561 -0.0685 -0.0410 0.0941  538  SER B N   
3168 C CA  . SER B 152 ? 0.2767 0.3039 0.3854 -0.0750 -0.0413 0.1136  538  SER B CA  
3169 C C   . SER B 152 ? 0.3019 0.3369 0.4134 -0.0701 -0.0354 0.1262  538  SER B C   
3170 O O   . SER B 152 ? 0.3408 0.3606 0.4454 -0.0662 -0.0362 0.1210  538  SER B O   
3171 C CB  . SER B 152 ? 0.2987 0.3113 0.4229 -0.0881 -0.0537 0.1172  538  SER B CB  
3172 O OG  . SER B 152 ? 0.4157 0.4466 0.5603 -0.0957 -0.0542 0.1367  538  SER B OG  
3173 N N   . ARG B 153 ? 0.3753 0.4030 0.3505 -0.0980 0.0635  0.0498  539  ARG B N   
3174 C CA  . ARG B 153 ? 0.3886 0.4232 0.3455 -0.0979 0.0737  0.0594  539  ARG B CA  
3175 C C   . ARG B 153 ? 0.4062 0.4290 0.3562 -0.0931 0.0740  0.0733  539  ARG B C   
3176 O O   . ARG B 153 ? 0.3204 0.3273 0.2878 -0.0950 0.0747  0.0771  539  ARG B O   
3177 C CB  . ARG B 153 ? 0.3727 0.4106 0.3401 -0.1049 0.0881  0.0601  539  ARG B CB  
3178 C CG  . ARG B 153 ? 0.3918 0.4347 0.3371 -0.1046 0.1000  0.0703  539  ARG B CG  
3179 C CD  . ARG B 153 ? 0.4447 0.4899 0.3991 -0.1110 0.1163  0.0700  539  ARG B CD  
3180 N NE  . ARG B 153 ? 0.5260 0.5822 0.4592 -0.1085 0.1200  0.0635  539  ARG B NE  
3181 C CZ  . ARG B 153 ? 0.3800 0.4412 0.3198 -0.1095 0.1202  0.0505  539  ARG B CZ  
3182 N NH1 . ARG B 153 ? 0.4146 0.4739 0.3811 -0.1126 0.1176  0.0438  539  ARG B NH1 
3183 N NH2 . ARG B 153 ? 0.4854 0.5525 0.4044 -0.1071 0.1228  0.0442  539  ARG B NH2 
3184 N N   . GLY B 154 ? 0.4076 0.4384 0.3327 -0.0870 0.0734  0.0809  540  GLY B N   
3185 C CA  . GLY B 154 ? 0.4121 0.4331 0.3280 -0.0801 0.0749  0.0961  540  GLY B CA  
3186 C C   . GLY B 154 ? 0.4631 0.4803 0.3721 -0.0710 0.0637  0.0979  540  GLY B C   
3187 O O   . GLY B 154 ? 0.5692 0.5814 0.4671 -0.0631 0.0654  0.1118  540  GLY B O   
3188 N N   . THR B 155 ? 0.4560 0.4747 0.3713 -0.0709 0.0537  0.0853  541  THR B N   
3189 C CA  . THR B 155 ? 0.4407 0.4548 0.3501 -0.0617 0.0447  0.0868  541  THR B CA  
3190 C C   . THR B 155 ? 0.5086 0.5423 0.3977 -0.0544 0.0431  0.0954  541  THR B C   
3191 O O   . THR B 155 ? 0.5108 0.5662 0.3907 -0.0582 0.0430  0.0907  541  THR B O   
3192 C CB  . THR B 155 ? 0.4150 0.4287 0.3326 -0.0629 0.0360  0.0716  541  THR B CB  
3193 O OG1 . THR B 155 ? 0.3859 0.3844 0.3224 -0.0695 0.0357  0.0642  541  THR B OG1 
3194 C CG2 . THR B 155 ? 0.4018 0.4080 0.3133 -0.0528 0.0287  0.0735  541  THR B CG2 
3195 N N   . GLN B 156 ? 0.5029 0.5293 0.3857 -0.0439 0.0419  0.1079  542  GLN B N   
3196 C CA  . GLN B 156 ? 0.4902 0.5372 0.3564 -0.0353 0.0394  0.1189  542  GLN B CA  
3197 C C   . GLN B 156 ? 0.4984 0.5561 0.3657 -0.0305 0.0297  0.1117  542  GLN B C   
3198 O O   . GLN B 156 ? 0.5131 0.5573 0.3838 -0.0215 0.0274  0.1159  542  GLN B O   
3199 C CB  . GLN B 156 ? 0.4923 0.5262 0.3526 -0.0248 0.0449  0.1383  542  GLN B CB  
3200 N N   . VAL B 157 ? 0.4879 0.5684 0.3524 -0.0368 0.0255  0.1007  662  VAL B N   
3201 C CA  . VAL B 157 ? 0.4294 0.5229 0.2963 -0.0338 0.0177  0.0936  662  VAL B CA  
3202 C C   . VAL B 157 ? 0.5059 0.6324 0.3619 -0.0378 0.0142  0.0925  662  VAL B C   
3203 O O   . VAL B 157 ? 0.5639 0.6984 0.4161 -0.0486 0.0166  0.0820  662  VAL B O   
3204 C CB  . VAL B 157 ? 0.4730 0.5551 0.3518 -0.0398 0.0162  0.0765  662  VAL B CB  
3205 C CG1 . VAL B 157 ? 0.5147 0.6135 0.3948 -0.0384 0.0106  0.0690  662  VAL B CG1 
3206 C CG2 . VAL B 157 ? 0.4529 0.5042 0.3404 -0.0352 0.0167  0.0770  662  VAL B CG2 
3207 N N   . THR B 158 ? 0.4984 0.6412 0.3525 -0.0284 0.0084  0.1009  663  THR B N   
3208 C CA  . THR B 158 ? 0.5303 0.7002 0.3813 -0.0315 0.0028  0.0959  663  THR B CA  
3209 C C   . THR B 158 ? 0.5769 0.7590 0.4343 -0.0415 -0.0004 0.0782  663  THR B C   
3210 O O   . THR B 158 ? 0.5873 0.7816 0.4407 -0.0509 -0.0009 0.0679  663  THR B O   
3211 C CB  . THR B 158 ? 0.5219 0.7077 0.3752 -0.0193 -0.0033 0.1088  663  THR B CB  
3212 O OG1 . THR B 158 ? 0.4986 0.6895 0.3635 -0.0147 -0.0070 0.1072  663  THR B OG1 
3213 C CG2 . THR B 158 ? 0.5038 0.6717 0.3527 -0.0078 0.0018  0.1265  663  THR B CG2 
3214 N N   . GLY B 159 ? 0.6371 0.8138 0.5033 -0.0393 -0.0015 0.0745  664  GLY B N   
3215 C CA  . GLY B 159 ? 0.6183 0.8043 0.4910 -0.0480 -0.0028 0.0585  664  GLY B CA  
3216 C C   . GLY B 159 ? 0.6459 0.8217 0.5276 -0.0419 -0.0030 0.0573  664  GLY B C   
3217 O O   . GLY B 159 ? 0.6461 0.7991 0.5309 -0.0323 -0.0013 0.0648  664  GLY B O   
3218 N N   . LEU B 160 ? 0.5104 0.6984 0.3993 -0.0472 -0.0042 0.0459  665  LEU B N   
3219 C CA  . LEU B 160 ? 0.4867 0.6622 0.3870 -0.0401 -0.0032 0.0432  665  LEU B CA  
3220 C C   . LEU B 160 ? 0.3699 0.5509 0.2744 -0.0260 -0.0062 0.0583  665  LEU B C   
3221 O O   . LEU B 160 ? 0.3878 0.5479 0.2971 -0.0162 -0.0035 0.0604  665  LEU B O   
3222 C CB  . LEU B 160 ? 0.4432 0.6323 0.3509 -0.0490 -0.0022 0.0291  665  LEU B CB  
3223 C CG  . LEU B 160 ? 0.3947 0.5602 0.3096 -0.0474 0.0033  0.0193  665  LEU B CG  
3224 C CD1 . LEU B 160 ? 0.3696 0.5092 0.2800 -0.0500 0.0070  0.0141  665  LEU B CD1 
3225 C CD2 . LEU B 160 ? 0.3560 0.5356 0.2781 -0.0568 0.0062  0.0065  665  LEU B CD2 
3226 N N   . SER B 161 ? 0.3597 0.5685 0.2616 -0.0240 -0.0114 0.0692  666  SER B N   
3227 C CA  . SER B 161 ? 0.4213 0.6391 0.3289 -0.0093 -0.0136 0.0857  666  SER B CA  
3228 C C   . SER B 161 ? 0.4232 0.6218 0.3223 0.0015  -0.0111 0.1013  666  SER B C   
3229 O O   . SER B 161 ? 0.4392 0.6458 0.3419 0.0142  -0.0120 0.1168  666  SER B O   
3230 C CB  . SER B 161 ? 0.4435 0.7045 0.3557 -0.0117 -0.0216 0.0905  666  SER B CB  
3231 O OG  . SER B 161 ? 0.5940 0.8713 0.5220 -0.0132 -0.0226 0.0842  666  SER B OG  
3232 N N   . ASP B 162 ? 0.4395 0.6120 0.3302 -0.0034 -0.0069 0.0971  667  ASP B N   
3233 C CA  . ASP B 162 ? 0.3988 0.5488 0.2832 0.0056  -0.0027 0.1106  667  ASP B CA  
3234 C C   . ASP B 162 ? 0.4264 0.5520 0.3163 0.0191  0.0010  0.1163  667  ASP B C   
3235 O O   . ASP B 162 ? 0.3628 0.4751 0.2582 0.0187  0.0020  0.1053  667  ASP B O   
3236 C CB  . ASP B 162 ? 0.3825 0.5090 0.2615 -0.0039 0.0015  0.1029  667  ASP B CB  
3237 C CG  . ASP B 162 ? 0.4475 0.5561 0.3200 0.0021  0.0065  0.1173  667  ASP B CG  
3238 O OD1 . ASP B 162 ? 0.4159 0.4995 0.2906 0.0121  0.0100  0.1241  667  ASP B OD1 
3239 O OD2 . ASP B 162 ? 0.4661 0.5836 0.3301 -0.0031 0.0080  0.1217  667  ASP B OD2 
3240 N N   . LYS B 163 ? 0.3670 0.4852 0.2539 0.0318  0.0042  0.1339  668  LYS B N   
3241 C CA  . LYS B 163 ? 0.4066 0.5003 0.2966 0.0458  0.0094  0.1403  668  LYS B CA  
3242 C C   . LYS B 163 ? 0.4439 0.4961 0.3306 0.0424  0.0135  0.1283  668  LYS B C   
3243 O O   . LYS B 163 ? 0.3982 0.4294 0.2855 0.0509  0.0169  0.1266  668  LYS B O   
3244 C CB  . LYS B 163 ? 0.3994 0.4880 0.2891 0.0586  0.0137  0.1579  668  LYS B CB  
3245 C CG  . LYS B 163 ? 0.5444 0.6636 0.4465 0.0688  0.0110  0.1672  668  LYS B CG  
3246 C CD  . LYS B 163 ? 0.5996 0.7617 0.5077 0.0591  0.0016  0.1606  668  LYS B CD  
3247 C CE  . LYS B 163 ? 0.5516 0.7472 0.4747 0.0687  -0.0016 0.1711  668  LYS B CE  
3248 N NZ  . LYS B 163 ? 0.5837 0.7712 0.5173 0.0805  0.0037  0.1745  668  LYS B NZ  
3249 N N   . LYS B 164 ? 0.3884 0.4291 0.2715 0.0304  0.0131  0.1200  669  LYS B N   
3250 C CA  . LYS B 164 ? 0.3706 0.3775 0.2526 0.0254  0.0144  0.1071  669  LYS B CA  
3251 C C   . LYS B 164 ? 0.3869 0.3966 0.2726 0.0218  0.0110  0.0919  669  LYS B C   
3252 O O   . LYS B 164 ? 0.4052 0.3873 0.2882 0.0234  0.0115  0.0836  669  LYS B O   
3253 C CB  . LYS B 164 ? 0.3510 0.3513 0.2329 0.0128  0.0147  0.1024  669  LYS B CB  
3254 C CG  . LYS B 164 ? 0.4451 0.4264 0.3234 0.0164  0.0207  0.1153  669  LYS B CG  
3255 C CD  . LYS B 164 ? 0.4920 0.4670 0.3733 0.0033  0.0222  0.1102  669  LYS B CD  
3256 C CE  . LYS B 164 ? 0.5032 0.5069 0.3811 -0.0007 0.0234  0.1177  669  LYS B CE  
3257 N NZ  . LYS B 164 ? 0.5305 0.5233 0.4041 0.0025  0.0312  0.1333  669  LYS B NZ  
3258 N N   . PHE B 165 ? 0.3687 0.4103 0.2593 0.0168  0.0077  0.0879  670  PHE B N   
3259 C CA  . PHE B 165 ? 0.3510 0.3965 0.2461 0.0142  0.0064  0.0752  670  PHE B CA  
3260 C C   . PHE B 165 ? 0.3545 0.4063 0.2535 0.0263  0.0085  0.0813  670  PHE B C   
3261 O O   . PHE B 165 ? 0.3177 0.3528 0.2160 0.0304  0.0109  0.0743  670  PHE B O   
3262 C CB  . PHE B 165 ? 0.3454 0.4195 0.2447 0.0013  0.0036  0.0665  670  PHE B CB  
3263 C CG  . PHE B 165 ? 0.3297 0.3954 0.2274 -0.0105 0.0036  0.0573  670  PHE B CG  
3264 C CD1 . PHE B 165 ? 0.3463 0.3828 0.2434 -0.0112 0.0041  0.0505  670  PHE B CD1 
3265 C CD2 . PHE B 165 ? 0.3098 0.3974 0.2065 -0.0208 0.0031  0.0554  670  PHE B CD2 
3266 C CE1 . PHE B 165 ? 0.3317 0.3636 0.2313 -0.0215 0.0042  0.0432  670  PHE B CE1 
3267 C CE2 . PHE B 165 ? 0.3615 0.4413 0.2582 -0.0306 0.0051  0.0479  670  PHE B CE2 
3268 C CZ  . PHE B 165 ? 0.3663 0.4194 0.2665 -0.0308 0.0057  0.0423  670  PHE B CZ  
3269 N N   . GLN B 166 ? 0.3340 0.4103 0.2373 0.0327  0.0080  0.0951  671  GLN B N   
3270 C CA  . GLN B 166 ? 0.3520 0.4411 0.2638 0.0440  0.0103  0.1021  671  GLN B CA  
3271 C C   . GLN B 166 ? 0.3499 0.4060 0.2563 0.0594  0.0174  0.1099  671  GLN B C   
3272 O O   . GLN B 166 ? 0.3556 0.4007 0.2638 0.0665  0.0220  0.1068  671  GLN B O   
3273 C CB  . GLN B 166 ? 0.3896 0.5190 0.3093 0.0461  0.0061  0.1151  671  GLN B CB  
3274 C CG  . GLN B 166 ? 0.4050 0.5655 0.3260 0.0301  -0.0009 0.1067  671  GLN B CG  
3275 C CD  . GLN B 166 ? 0.5322 0.7113 0.4644 0.0224  -0.0020 0.0941  671  GLN B CD  
3276 O OE1 . GLN B 166 ? 0.4765 0.6713 0.4216 0.0296  -0.0009 0.0992  671  GLN B OE1 
3277 N NE2 . GLN B 166 ? 0.4126 0.5893 0.3414 0.0079  -0.0027 0.0781  671  GLN B NE2 
3278 N N   . ARG B 167 ? 0.3535 0.3917 0.2523 0.0647  0.0197  0.1201  672  ARG B N   
3279 C CA  . ARG B 167 ? 0.4319 0.4345 0.3234 0.0785  0.0278  0.1271  672  ARG B CA  
3280 C C   . ARG B 167 ? 0.4078 0.3729 0.2870 0.0717  0.0282  0.1191  672  ARG B C   
3281 O O   . ARG B 167 ? 0.4948 0.4462 0.3697 0.0743  0.0314  0.1286  672  ARG B O   
3282 C CB  . ARG B 167 ? 0.5126 0.5263 0.4080 0.0926  0.0322  0.1485  672  ARG B CB  
3283 C CG  . ARG B 167 ? 0.4944 0.5518 0.4060 0.0983  0.0297  0.1575  672  ARG B CG  
3284 C CD  . ARG B 167 ? 0.5082 0.5764 0.4297 0.1096  0.0331  0.1724  672  ARG B CD  
3285 N NE  . ARG B 167 ? 0.5778 0.6069 0.4946 0.1216  0.0443  0.1754  672  ARG B NE  
3286 C CZ  . ARG B 167 ? 0.5952 0.6196 0.5194 0.1342  0.0524  0.1788  672  ARG B CZ  
3287 N NH1 . ARG B 167 ? 0.5304 0.5875 0.4696 0.1376  0.0508  0.1819  672  ARG B NH1 
3288 N NH2 . ARG B 167 ? 0.5448 0.5312 0.4615 0.1431  0.0632  0.1790  672  ARG B NH2 
3289 N N   . PRO B 168 ? 0.4036 0.3520 0.2782 0.0632  0.0252  0.1020  673  PRO B N   
3290 C CA  . PRO B 168 ? 0.4549 0.3756 0.3222 0.0537  0.0229  0.0933  673  PRO B CA  
3291 C C   . PRO B 168 ? 0.4774 0.3571 0.3337 0.0614  0.0289  0.0968  673  PRO B C   
3292 O O   . PRO B 168 ? 0.4929 0.3536 0.3467 0.0537  0.0280  0.0941  673  PRO B O   
3293 C CB  . PRO B 168 ? 0.3869 0.3034 0.2528 0.0456  0.0178  0.0758  673  PRO B CB  
3294 C CG  . PRO B 168 ? 0.3970 0.3203 0.2633 0.0554  0.0213  0.0761  673  PRO B CG  
3295 C CD  . PRO B 168 ? 0.3749 0.3300 0.2518 0.0619  0.0238  0.0908  673  PRO B CD  
3296 N N   . HIS B 169 ? 0.4832 0.3472 0.3334 0.0759  0.0360  0.1022  674  HIS B N   
3297 C CA  . HIS B 169 ? 0.4632 0.2839 0.3002 0.0834  0.0432  0.1042  674  HIS B CA  
3298 C C   . HIS B 169 ? 0.4751 0.2940 0.3148 0.0927  0.0516  0.1231  674  HIS B C   
3299 O O   . HIS B 169 ? 0.6314 0.4178 0.4642 0.0983  0.0592  0.1237  674  HIS B O   
3300 C CB  . HIS B 169 ? 0.4990 0.2980 0.3248 0.0953  0.0490  0.1002  674  HIS B CB  
3301 C CG  . HIS B 169 ? 0.4837 0.2602 0.2969 0.0877  0.0429  0.0811  674  HIS B CG  
3302 N ND1 . HIS B 169 ? 0.5431 0.3251 0.3529 0.0912  0.0423  0.0738  674  HIS B ND1 
3303 C CD2 . HIS B 169 ? 0.4532 0.2032 0.2572 0.0768  0.0368  0.0684  674  HIS B CD2 
3304 C CE1 . HIS B 169 ? 0.5533 0.3126 0.3499 0.0841  0.0359  0.0581  674  HIS B CE1 
3305 N NE2 . HIS B 169 ? 0.5210 0.2620 0.3147 0.0748  0.0316  0.0542  674  HIS B NE2 
3306 N N   . ASP B 170 ? 0.4479 0.3048 0.2997 0.0925  0.0496  0.1354  675  ASP B N   
3307 C CA  . ASP B 170 ? 0.5674 0.4287 0.4252 0.0971  0.0548  0.1495  675  ASP B CA  
3308 C C   . ASP B 170 ? 0.5682 0.4086 0.4206 0.0868  0.0555  0.1495  675  ASP B C   
3309 O O   . ASP B 170 ? 0.6051 0.4496 0.4623 0.0889  0.0599  0.1606  675  ASP B O   
3310 C CB  . ASP B 170 ? 0.5213 0.4321 0.3927 0.0995  0.0506  0.1606  675  ASP B CB  
3311 C CG  . ASP B 170 ? 0.5941 0.5257 0.4757 0.1112  0.0523  0.1641  675  ASP B CG  
3312 O OD1 . ASP B 170 ? 0.6346 0.5418 0.5117 0.1177  0.0581  0.1581  675  ASP B OD1 
3313 O OD2 . ASP B 170 ? 0.5558 0.5280 0.4497 0.1135  0.0483  0.1728  675  ASP B OD2 
3314 N N   . TYR B 171 ? 0.5380 0.3617 0.3863 0.0730  0.0497  0.1328  676  TYR B N   
3315 C CA  . TYR B 171 ? 0.5859 0.3957 0.4360 0.0596  0.0489  0.1287  676  TYR B CA  
3316 C C   . TYR B 171 ? 0.6403 0.4084 0.4828 0.0528  0.0480  0.1128  676  TYR B C   
3317 O O   . TYR B 171 ? 0.5847 0.3476 0.4219 0.0514  0.0419  0.0989  676  TYR B O   
3318 C CB  . TYR B 171 ? 0.5149 0.3581 0.3745 0.0453  0.0399  0.1217  676  TYR B CB  
3319 C CG  . TYR B 171 ? 0.4836 0.3682 0.3479 0.0493  0.0392  0.1350  676  TYR B CG  
3320 C CD1 . TYR B 171 ? 0.4503 0.3642 0.3171 0.0550  0.0349  0.1351  676  TYR B CD1 
3321 C CD2 . TYR B 171 ? 0.5066 0.4009 0.3722 0.0469  0.0429  0.1471  676  TYR B CD2 
3322 C CE1 . TYR B 171 ? 0.3896 0.3427 0.2604 0.0572  0.0326  0.1459  676  TYR B CE1 
3323 C CE2 . TYR B 171 ? 0.4871 0.4194 0.3536 0.0504  0.0410  0.1587  676  TYR B CE2 
3324 C CZ  . TYR B 171 ? 0.3786 0.3409 0.2478 0.0550  0.0349  0.1574  676  TYR B CZ  
3325 O OH  . TYR B 171 ? 0.4576 0.4591 0.3281 0.0567  0.0310  0.1665  676  TYR B OH  
3326 N N   . SER B 172 ? 0.7492 0.4878 0.5907 0.0485  0.0540  0.1151  677  SER B N   
3327 C CA  . SER B 172 ? 0.7870 0.4860 0.6220 0.0395  0.0521  0.0994  677  SER B CA  
3328 C C   . SER B 172 ? 0.7492 0.4479 0.5968 0.0218  0.0487  0.0942  677  SER B C   
3329 O O   . SER B 172 ? 0.8294 0.5197 0.6821 0.0211  0.0581  0.1062  677  SER B O   
3330 C CB  . SER B 172 ? 0.7645 0.4204 0.5865 0.0502  0.0646  0.1051  677  SER B CB  
3331 O OG  . SER B 172 ? 0.8840 0.5409 0.6971 0.0646  0.0667  0.1047  677  SER B OG  
3332 N N   . PRO B 173 ? 0.5294 0.2373 0.3838 0.0080  0.0367  0.0779  678  PRO B N   
3333 C CA  . PRO B 173 ? 0.5969 0.3149 0.4460 0.0081  0.0258  0.0640  678  PRO B CA  
3334 C C   . PRO B 173 ? 0.5324 0.2922 0.3863 0.0134  0.0236  0.0697  678  PRO B C   
3335 O O   . PRO B 173 ? 0.4917 0.2776 0.3554 0.0113  0.0262  0.0798  678  PRO B O   
3336 C CB  . PRO B 173 ? 0.5550 0.2708 0.4144 -0.0094 0.0151  0.0485  678  PRO B CB  
3337 C CG  . PRO B 173 ? 0.6109 0.3060 0.4792 -0.0186 0.0212  0.0520  678  PRO B CG  
3338 C CD  . PRO B 173 ? 0.6375 0.3421 0.5066 -0.0090 0.0341  0.0722  678  PRO B CD  
3339 N N   . PRO B 174 ? 0.5363 0.3021 0.3825 0.0199  0.0193  0.0630  679  PRO B N   
3340 C CA  . PRO B 174 ? 0.4091 0.2134 0.2610 0.0235  0.0178  0.0671  679  PRO B CA  
3341 C C   . PRO B 174 ? 0.4486 0.2785 0.3131 0.0099  0.0103  0.0590  679  PRO B C   
3342 O O   . PRO B 174 ? 0.4341 0.2535 0.3029 -0.0007 0.0043  0.0480  679  PRO B O   
3343 C CB  . PRO B 174 ? 0.4777 0.2738 0.3180 0.0333  0.0169  0.0608  679  PRO B CB  
3344 C CG  . PRO B 174 ? 0.4818 0.2414 0.3107 0.0291  0.0127  0.0475  679  PRO B CG  
3345 C CD  . PRO B 174 ? 0.5067 0.2426 0.3368 0.0243  0.0168  0.0516  679  PRO B CD  
3346 N N   . PHE B 175 ? 0.4219 0.2865 0.2927 0.0104  0.0109  0.0648  680  PHE B N   
3347 C CA  . PHE B 175 ? 0.3817 0.2708 0.2630 -0.0012 0.0062  0.0576  680  PHE B CA  
3348 C C   . PHE B 175 ? 0.3619 0.2488 0.2422 -0.0034 -0.0002 0.0431  680  PHE B C   
3349 O O   . PHE B 175 ? 0.3310 0.2153 0.2034 0.0055  0.0000  0.0413  680  PHE B O   
3350 C CB  . PHE B 175 ? 0.3505 0.2749 0.2351 0.0001  0.0085  0.0658  680  PHE B CB  
3351 C CG  . PHE B 175 ? 0.3732 0.3169 0.2661 -0.0117 0.0086  0.0649  680  PHE B CG  
3352 C CD1 . PHE B 175 ? 0.3667 0.2989 0.2640 -0.0177 0.0118  0.0692  680  PHE B CD1 
3353 C CD2 . PHE B 175 ? 0.3552 0.3269 0.2514 -0.0168 0.0070  0.0597  680  PHE B CD2 
3354 C CE1 . PHE B 175 ? 0.3982 0.3472 0.3026 -0.0277 0.0138  0.0691  680  PHE B CE1 
3355 C CE2 . PHE B 175 ? 0.3243 0.3112 0.2257 -0.0270 0.0088  0.0586  680  PHE B CE2 
3356 C CZ  . PHE B 175 ? 0.3826 0.3585 0.2880 -0.0319 0.0125  0.0636  680  PHE B CZ  
3357 N N   . ARG B 176 ? 0.3181 0.2064 0.2074 -0.0144 -0.0052 0.0339  681  ARG B N   
3358 C CA  . ARG B 176 ? 0.4140 0.3014 0.3032 -0.0162 -0.0114 0.0214  681  ARG B CA  
3359 C C   . ARG B 176 ? 0.3488 0.2661 0.2474 -0.0214 -0.0102 0.0190  681  ARG B C   
3360 O O   . ARG B 176 ? 0.2839 0.2145 0.1939 -0.0305 -0.0089 0.0197  681  ARG B O   
3361 C CB  . ARG B 176 ? 0.3835 0.2529 0.2777 -0.0242 -0.0186 0.0129  681  ARG B CB  
3362 C CG  . ARG B 176 ? 0.4561 0.2925 0.3400 -0.0216 -0.0198 0.0128  681  ARG B CG  
3363 C CD  . ARG B 176 ? 0.4136 0.2387 0.3083 -0.0334 -0.0269 0.0055  681  ARG B CD  
3364 N NE  . ARG B 176 ? 0.4065 0.2509 0.3212 -0.0433 -0.0232 0.0106  681  ARG B NE  
3365 C CZ  . ARG B 176 ? 0.5208 0.3681 0.4532 -0.0549 -0.0281 0.0053  681  ARG B CZ  
3366 N NH1 . ARG B 176 ? 0.5096 0.3436 0.4429 -0.0589 -0.0390 -0.0055 681  ARG B NH1 
3367 N NH2 . ARG B 176 ? 0.4143 0.2791 0.3637 -0.0625 -0.0220 0.0114  681  ARG B NH2 
3368 N N   . PHE B 177 ? 0.2991 0.2254 0.1929 -0.0157 -0.0092 0.0160  682  PHE B N   
3369 C CA  . PHE B 177 ? 0.2976 0.2496 0.1990 -0.0208 -0.0067 0.0126  682  PHE B CA  
3370 C C   . PHE B 177 ? 0.3151 0.2648 0.2120 -0.0154 -0.0069 0.0054  682  PHE B C   
3371 O O   . PHE B 177 ? 0.2793 0.2155 0.1658 -0.0057 -0.0064 0.0067  682  PHE B O   
3372 C CB  . PHE B 177 ? 0.3042 0.2796 0.2063 -0.0211 -0.0018 0.0208  682  PHE B CB  
3373 C CG  . PHE B 177 ? 0.3530 0.3278 0.2476 -0.0102 0.0000  0.0282  682  PHE B CG  
3374 C CD1 . PHE B 177 ? 0.3299 0.2906 0.2191 -0.0035 0.0010  0.0381  682  PHE B CD1 
3375 C CD2 . PHE B 177 ? 0.2985 0.2864 0.1933 -0.0064 0.0022  0.0259  682  PHE B CD2 
3376 C CE1 . PHE B 177 ? 0.2970 0.2577 0.1813 0.0079  0.0040  0.0462  682  PHE B CE1 
3377 C CE2 . PHE B 177 ? 0.3225 0.3120 0.2140 0.0040  0.0047  0.0337  682  PHE B CE2 
3378 C CZ  . PHE B 177 ? 0.3027 0.2791 0.1890 0.0118  0.0055  0.0442  682  PHE B CZ  
3379 N N   . GLY B 178 ? 0.3161 0.2778 0.2205 -0.0211 -0.0058 -0.0015 683  GLY B N   
3380 C CA  . GLY B 178 ? 0.2994 0.2587 0.2002 -0.0162 -0.0040 -0.0075 683  GLY B CA  
3381 C C   . GLY B 178 ? 0.2529 0.2316 0.1635 -0.0234 0.0014  -0.0125 683  GLY B C   
3382 O O   . GLY B 178 ? 0.2724 0.2660 0.1908 -0.0322 0.0036  -0.0119 683  GLY B O   
3383 N N   . THR B 179 ? 0.2312 0.2073 0.1397 -0.0192 0.0050  -0.0174 684  THR B N   
3384 C CA  . THR B 179 ? 0.2603 0.2498 0.1767 -0.0250 0.0123  -0.0231 684  THR B CA  
3385 C C   . THR B 179 ? 0.2211 0.1968 0.1362 -0.0194 0.0127  -0.0278 684  THR B C   
3386 O O   . THR B 179 ? 0.2565 0.2141 0.1632 -0.0117 0.0059  -0.0271 684  THR B O   
3387 C CB  . THR B 179 ? 0.2306 0.2352 0.1473 -0.0262 0.0194  -0.0233 684  THR B CB  
3388 O OG1 . THR B 179 ? 0.2184 0.2345 0.1425 -0.0342 0.0273  -0.0301 684  THR B OG1 
3389 C CG2 . THR B 179 ? 0.2042 0.1966 0.1136 -0.0154 0.0216  -0.0223 684  THR B CG2 
3390 N N   . VAL B 180 ? 0.2305 0.2140 0.1526 -0.0231 0.0210  -0.0327 685  VAL B N   
3391 C CA  . VAL B 180 ? 0.2600 0.2318 0.1804 -0.0162 0.0243  -0.0357 685  VAL B CA  
3392 C C   . VAL B 180 ? 0.2675 0.2367 0.1815 -0.0110 0.0326  -0.0362 685  VAL B C   
3393 O O   . VAL B 180 ? 0.2936 0.2766 0.2143 -0.0181 0.0416  -0.0391 685  VAL B O   
3394 C CB  . VAL B 180 ? 0.2553 0.2344 0.1880 -0.0219 0.0311  -0.0397 685  VAL B CB  
3395 C CG1 . VAL B 180 ? 0.2239 0.1904 0.1544 -0.0126 0.0350  -0.0408 685  VAL B CG1 
3396 C CG2 . VAL B 180 ? 0.2291 0.2131 0.1714 -0.0273 0.0243  -0.0382 685  VAL B CG2 
3397 N N   . PRO B 181 ? 0.2604 0.2123 0.1618 0.0005  0.0304  -0.0338 686  PRO B N   
3398 C CA  . PRO B 181 ? 0.2439 0.1940 0.1408 0.0057  0.0391  -0.0326 686  PRO B CA  
3399 C C   . PRO B 181 ? 0.2431 0.1944 0.1459 0.0048  0.0523  -0.0366 686  PRO B C   
3400 O O   . PRO B 181 ? 0.2269 0.1781 0.1355 0.0020  0.0553  -0.0399 686  PRO B O   
3401 C CB  . PRO B 181 ? 0.3196 0.2465 0.1986 0.0192  0.0340  -0.0292 686  PRO B CB  
3402 C CG  . PRO B 181 ? 0.2504 0.1664 0.1249 0.0213  0.0245  -0.0308 686  PRO B CG  
3403 C CD  . PRO B 181 ? 0.2425 0.1755 0.1326 0.0090  0.0200  -0.0323 686  PRO B CD  
3404 N N   . ASN B 182 ? 0.2843 0.2365 0.1871 0.0074  0.0614  -0.0358 687  ASN B N   
3405 C CA  . ASN B 182 ? 0.2410 0.1923 0.1515 0.0077  0.0739  -0.0377 687  ASN B CA  
3406 C C   . ASN B 182 ? 0.2769 0.2467 0.2050 -0.0064 0.0785  -0.0428 687  ASN B C   
3407 O O   . ASN B 182 ? 0.2511 0.2195 0.1888 -0.0075 0.0853  -0.0431 687  ASN B O   
3408 C CB  . ASN B 182 ? 0.2558 0.1891 0.1609 0.0176  0.0736  -0.0353 687  ASN B CB  
3409 C CG  . ASN B 182 ? 0.3796 0.2933 0.2656 0.0311  0.0664  -0.0304 687  ASN B CG  
3410 O OD1 . ASN B 182 ? 0.3173 0.2282 0.1971 0.0350  0.0654  -0.0272 687  ASN B OD1 
3411 N ND2 . ASN B 182 ? 0.3677 0.2676 0.2439 0.0384  0.0611  -0.0294 687  ASN B ND2 
3412 N N   . GLY B 183 ? 0.2408 0.2261 0.1720 -0.0174 0.0746  -0.0463 688  GLY B N   
3413 C CA  . GLY B 183 ? 0.2185 0.2192 0.1633 -0.0306 0.0772  -0.0511 688  GLY B CA  
3414 C C   . GLY B 183 ? 0.2004 0.2218 0.1503 -0.0394 0.0766  -0.0526 688  GLY B C   
3415 O O   . GLY B 183 ? 0.1807 0.2067 0.1267 -0.0346 0.0759  -0.0488 688  GLY B O   
3416 N N   . SER B 184 ? 0.1421 0.1944 0.2087 -0.0128 -0.0303 0.0446  689  SER B N   
3417 C CA  . SER B 184 ? 0.1079 0.1788 0.2165 -0.0119 -0.0229 0.0330  689  SER B CA  
3418 C C   . SER B 184 ? 0.1083 0.1900 0.2182 -0.0082 -0.0296 0.0234  689  SER B C   
3419 O O   . SER B 184 ? 0.1037 0.1940 0.2367 -0.0063 -0.0209 0.0126  689  SER B O   
3420 C CB  . SER B 184 ? 0.1233 0.2107 0.2682 -0.0089 -0.0327 0.0307  689  SER B CB  
3421 O OG  . SER B 184 ? 0.0965 0.1810 0.2162 -0.0030 -0.0445 0.0252  689  SER B OG  
3422 N N   . THR B 185 ? 0.1407 0.2214 0.2281 -0.0070 -0.0449 0.0262  690  THR B N   
3423 C CA  . THR B 185 ? 0.1453 0.2315 0.2316 -0.0041 -0.0510 0.0184  690  THR B CA  
3424 C C   . THR B 185 ? 0.1563 0.2290 0.2224 -0.0054 -0.0389 0.0142  690  THR B C   
3425 O O   . THR B 185 ? 0.1537 0.2319 0.2338 -0.0015 -0.0346 0.0040  690  THR B O   
3426 C CB  . THR B 185 ? 0.1320 0.2069 0.1898 -0.0022 -0.0558 0.0162  690  THR B CB  
3427 O OG1 . THR B 185 ? 0.1044 0.1795 0.1630 0.0029  -0.0497 0.0103  690  THR B OG1 
3428 C CG2 . THR B 185 ? 0.1649 0.2381 0.2141 -0.0002 -0.0559 0.0094  690  THR B CG2 
3429 N N   . GLU B 186 ? 0.1459 0.1994 0.1767 -0.0091 -0.0343 0.0211  691  GLU B N   
3430 C CA  . GLU B 186 ? 0.2052 0.2438 0.2128 -0.0091 -0.0217 0.0168  691  GLU B CA  
3431 C C   . GLU B 186 ? 0.2135 0.2561 0.2449 -0.0089 0.0005  0.0109  691  GLU B C   
3432 O O   . GLU B 186 ? 0.1769 0.2199 0.2114 -0.0061 0.0095  0.0012  691  GLU B O   
3433 C CB  . GLU B 186 ? 0.1932 0.2070 0.1538 -0.0109 -0.0216 0.0251  691  GLU B CB  
3434 C CG  . GLU B 186 ? 0.2244 0.2205 0.1549 -0.0093 -0.0106 0.0198  691  GLU B CG  
3435 C CD  . GLU B 186 ? 0.3108 0.2777 0.1902 -0.0085 -0.0074 0.0275  691  GLU B CD  
3436 O OE1 . GLU B 186 ? 0.2989 0.2570 0.1685 -0.0091 -0.0062 0.0377  691  GLU B OE1 
3437 O OE2 . GLU B 186 ? 0.3435 0.2936 0.1896 -0.0057 -0.0067 0.0229  691  GLU B OE2 
3438 N N   . ARG B 187 ? 0.1558 0.2015 0.2069 -0.0118 0.0098  0.0158  692  ARG B N   
3439 C CA  . ARG B 187 ? 0.1672 0.2192 0.2501 -0.0134 0.0322  0.0091  692  ARG B CA  
3440 C C   . ARG B 187 ? 0.2132 0.2893 0.3390 -0.0077 0.0274  -0.0069 692  ARG B C   
3441 O O   . ARG B 187 ? 0.1934 0.2741 0.3358 -0.0061 0.0425  -0.0177 692  ARG B O   
3442 C CB  . ARG B 187 ? 0.1716 0.2230 0.2739 -0.0183 0.0398  0.0165  692  ARG B CB  
3443 C CG  . ARG B 187 ? 0.2189 0.2752 0.3573 -0.0228 0.0661  0.0102  692  ARG B CG  
3444 C CD  . ARG B 187 ? 0.2592 0.2954 0.3671 -0.0254 0.0916  0.0121  692  ARG B CD  
3445 N NE  . ARG B 187 ? 0.2863 0.3294 0.4341 -0.0309 0.1204  0.0049  692  ARG B NE  
3446 C CZ  . ARG B 187 ? 0.4633 0.5037 0.6098 -0.0311 0.1438  -0.0022 692  ARG B CZ  
3447 N NH1 . ARG B 187 ? 0.4708 0.4996 0.5747 -0.0254 0.1409  -0.0032 692  ARG B NH1 
3448 N NH2 . ARG B 187 ? 0.5406 0.5905 0.7319 -0.0374 0.1713  -0.0095 692  ARG B NH2 
3449 N N   . ASN B 188 ? 0.1653 0.2555 0.3076 -0.0031 0.0062  -0.0093 693  ASN B N   
3450 C CA  . ASN B 188 ? 0.1154 0.2234 0.2907 0.0055  -0.0018 -0.0243 693  ASN B CA  
3451 C C   . ASN B 188 ? 0.1337 0.2346 0.2877 0.0104  -0.0041 -0.0310 693  ASN B C   
3452 O O   . ASN B 188 ? 0.1178 0.2276 0.2952 0.0171  -0.0001 -0.0452 693  ASN B O   
3453 C CB  . ASN B 188 ? 0.1050 0.2117 0.2711 0.0096  -0.0204 -0.0204 693  ASN B CB  
3454 C CG  . ASN B 188 ? 0.1897 0.2879 0.3486 0.0166  -0.0246 -0.0285 693  ASN B CG  
3455 O OD1 . ASN B 188 ? 0.1280 0.2203 0.2722 0.0211  -0.0306 -0.0313 693  ASN B OD1 
3456 N ND2 . ASN B 188 ? 0.0905 0.1864 0.2611 0.0171  -0.0224 -0.0330 693  ASN B ND2 
3457 N N   . ILE B 189 ? 0.1500 0.2348 0.2618 0.0078  -0.0115 -0.0222 694  ILE B N   
3458 C CA  . ILE B 189 ? 0.1804 0.2550 0.2702 0.0118  -0.0147 -0.0283 694  ILE B CA  
3459 C C   . ILE B 189 ? 0.1525 0.2193 0.2348 0.0114  0.0053  -0.0341 694  ILE B C   
3460 O O   . ILE B 189 ? 0.1651 0.2316 0.2506 0.0182  0.0071  -0.0458 694  ILE B O   
3461 C CB  . ILE B 189 ? 0.2095 0.2694 0.2612 0.0076  -0.0282 -0.0187 694  ILE B CB  
3462 C CG1 . ILE B 189 ? 0.1907 0.2601 0.2532 0.0084  -0.0448 -0.0141 694  ILE B CG1 
3463 C CG2 . ILE B 189 ? 0.2383 0.2840 0.2668 0.0108  -0.0310 -0.0254 694  ILE B CG2 
3464 C CD1 . ILE B 189 ? 0.2678 0.3268 0.3027 0.0032  -0.0570 -0.0066 694  ILE B CD1 
3465 N N   . ARG B 190 ? 0.1985 0.2569 0.2687 0.0046  0.0216  -0.0260 695  ARG B N   
3466 C CA  . ARG B 190 ? 0.2309 0.2794 0.2900 0.0042  0.0447  -0.0303 695  ARG B CA  
3467 C C   . ARG B 190 ? 0.2279 0.2969 0.3369 0.0083  0.0588  -0.0456 695  ARG B C   
3468 O O   . ARG B 190 ? 0.2082 0.2755 0.3165 0.0126  0.0717  -0.0560 695  ARG B O   
3469 C CB  . ARG B 190 ? 0.2522 0.2833 0.2849 -0.0031 0.0608  -0.0168 695  ARG B CB  
3470 C CG  . ARG B 190 ? 0.2533 0.2702 0.2686 -0.0034 0.0892  -0.0193 695  ARG B CG  
3471 C CD  . ARG B 190 ? 0.2887 0.2837 0.2753 -0.0096 0.1066  -0.0043 695  ARG B CD  
3472 N NE  . ARG B 190 ? 0.4747 0.4469 0.4087 -0.0091 0.0883  0.0081  695  ARG B NE  
3473 C CZ  . ARG B 190 ? 0.5189 0.4648 0.3978 -0.0053 0.0878  0.0103  695  ARG B CZ  
3474 N NH1 . ARG B 190 ? 0.4462 0.3836 0.3107 -0.0014 0.1059  0.0021  695  ARG B NH1 
3475 N NH2 . ARG B 190 ? 0.4500 0.3784 0.2884 -0.0042 0.0675  0.0194  695  ARG B NH2 
3476 N N   . ASN B 191 ? 0.1925 0.2819 0.3474 0.0080  0.0553  -0.0490 696  ASN B N   
3477 C CA  . ASN B 191 ? 0.1471 0.2588 0.3570 0.0120  0.0662  -0.0661 696  ASN B CA  
3478 C C   . ASN B 191 ? 0.1521 0.2744 0.3779 0.0249  0.0457  -0.0809 696  ASN B C   
3479 O O   . ASN B 191 ? 0.1419 0.2655 0.3794 0.0284  0.0492  -0.0915 696  ASN B O   
3480 C CB  . ASN B 191 ? 0.1549 0.2776 0.4016 0.0061  0.0682  -0.0637 696  ASN B CB  
3481 C CG  . ASN B 191 ? 0.4008 0.5119 0.6388 -0.0060 0.0939  -0.0507 696  ASN B CG  
3482 O OD1 . ASN B 191 ? 0.3688 0.4807 0.6205 -0.0119 0.0928  -0.0429 696  ASN B OD1 
3483 N ND2 . ASN B 191 ? 0.3875 0.4810 0.5932 -0.0088 0.1158  -0.0471 696  ASN B ND2 
3484 N N   . ASN B 192 ? 0.1220 0.2411 0.3319 0.0297  0.0213  -0.0767 697  ASN B N   
3485 C CA  . ASN B 192 ? 0.1336 0.2449 0.3342 0.0381  0.0011  -0.0825 697  ASN B CA  
3486 C C   . ASN B 192 ? 0.1881 0.2923 0.3691 0.0476  -0.0034 -0.0900 697  ASN B C   
3487 O O   . ASN B 192 ? 0.2310 0.3305 0.4118 0.0538  -0.0092 -0.0989 697  ASN B O   
3488 C CB  . ASN B 192 ? 0.1665 0.2688 0.3497 0.0372  -0.0173 -0.0725 697  ASN B CB  
3489 C CG  . ASN B 192 ? 0.1669 0.2695 0.3633 0.0319  -0.0161 -0.0697 697  ASN B CG  
3490 O OD1 . ASN B 192 ? 0.1433 0.2510 0.3633 0.0310  -0.0095 -0.0788 697  ASN B OD1 
3491 N ND2 . ASN B 192 ? 0.1470 0.2436 0.3281 0.0289  -0.0225 -0.0581 697  ASN B ND2 
3492 N N   . TYR B 193 ? 0.1920 0.2799 0.3331 0.0422  -0.0032 -0.0790 698  TYR B N   
3493 C CA  . TYR B 193 ? 0.2376 0.3053 0.3424 0.0465  -0.0108 -0.0806 698  TYR B CA  
3494 C C   . TYR B 193 ? 0.2324 0.2843 0.3040 0.0392  0.0044  -0.0757 698  TYR B C   
3495 O O   . TYR B 193 ? 0.2404 0.2769 0.2766 0.0310  -0.0002 -0.0630 698  TYR B O   
3496 C CB  . TYR B 193 ? 0.2505 0.3062 0.3308 0.0451  -0.0306 -0.0703 698  TYR B CB  
3497 C CG  . TYR B 193 ? 0.2658 0.3349 0.3722 0.0516  -0.0433 -0.0716 698  TYR B CG  
3498 C CD1 . TYR B 193 ? 0.2115 0.2780 0.3262 0.0610  -0.0499 -0.0819 698  TYR B CD1 
3499 C CD2 . TYR B 193 ? 0.1956 0.2719 0.3058 0.0444  -0.0474 -0.0598 698  TYR B CD2 
3500 C CE1 . TYR B 193 ? 0.2854 0.3456 0.3956 0.0577  -0.0553 -0.0772 698  TYR B CE1 
3501 C CE2 . TYR B 193 ? 0.2645 0.3339 0.3725 0.0433  -0.0502 -0.0554 698  TYR B CE2 
3502 C CZ  . TYR B 193 ? 0.3396 0.4003 0.4461 0.0498  -0.0536 -0.0646 698  TYR B CZ  
3503 O OH  . TYR B 193 ? 0.3557 0.4087 0.4555 0.0489  -0.0558 -0.0618 698  TYR B OH  
3504 N N   . PRO B 194 ? 0.2211 0.2764 0.3033 0.0431  0.0225  -0.0869 699  PRO B N   
3505 C CA  . PRO B 194 ? 0.2328 0.2702 0.2781 0.0380  0.0390  -0.0825 699  PRO B CA  
3506 C C   . PRO B 194 ? 0.2708 0.2822 0.2676 0.0389  0.0256  -0.0797 699  PRO B C   
3507 O O   . PRO B 194 ? 0.2899 0.2841 0.2487 0.0317  0.0255  -0.0688 699  PRO B O   
3508 C CB  . PRO B 194 ? 0.2317 0.2805 0.3045 0.0448  0.0604  -0.0985 699  PRO B CB  
3509 C CG  . PRO B 194 ? 0.2009 0.2786 0.3335 0.0482  0.0589  -0.1077 699  PRO B CG  
3510 C CD  . PRO B 194 ? 0.1772 0.2546 0.3087 0.0522  0.0302  -0.1043 699  PRO B CD  
3511 N N   . TYR B 195 ? 0.2888 0.2948 0.2853 0.0482  0.0130  -0.0902 700  TYR B N   
3512 C CA  . TYR B 195 ? 0.3118 0.2912 0.2653 0.0480  0.0006  -0.0887 700  TYR B CA  
3513 C C   . TYR B 195 ? 0.2856 0.2572 0.2217 0.0381  -0.0162 -0.0744 700  TYR B C   
3514 O O   . TYR B 195 ? 0.3312 0.2840 0.2318 0.0321  -0.0214 -0.0691 700  TYR B O   
3515 C CB  . TYR B 195 ? 0.2699 0.2421 0.2278 0.0603  -0.0100 -0.1019 700  TYR B CB  
3516 C CG  . TYR B 195 ? 0.3159 0.2581 0.2314 0.0602  -0.0197 -0.1029 700  TYR B CG  
3517 C CD1 . TYR B 195 ? 0.3319 0.2607 0.2254 0.0654  -0.0092 -0.1123 700  TYR B CD1 
3518 C CD2 . TYR B 195 ? 0.3877 0.3141 0.2863 0.0546  -0.0383 -0.0950 700  TYR B CD2 
3519 C CE1 . TYR B 195 ? 0.3615 0.2612 0.2167 0.0657  -0.0198 -0.1147 700  TYR B CE1 
3520 C CE2 . TYR B 195 ? 0.4311 0.3294 0.2954 0.0531  -0.0473 -0.0971 700  TYR B CE2 
3521 C CZ  . TYR B 195 ? 0.3899 0.2745 0.2323 0.0589  -0.0394 -0.1073 700  TYR B CZ  
3522 O OH  . TYR B 195 ? 0.5020 0.3590 0.3133 0.0570  -0.0495 -0.1094 700  TYR B OH  
3523 N N   . MET B 196 ? 0.2758 0.2623 0.2378 0.0371  -0.0254 -0.0695 701  MET B N   
3524 C CA  . MET B 196 ? 0.3260 0.3095 0.2778 0.0277  -0.0388 -0.0566 701  MET B CA  
3525 C C   . MET B 196 ? 0.3065 0.2904 0.2441 0.0183  -0.0334 -0.0463 701  MET B C   
3526 O O   . MET B 196 ? 0.3137 0.2863 0.2281 0.0112  -0.0441 -0.0394 701  MET B O   
3527 C CB  . MET B 196 ? 0.3032 0.3035 0.2854 0.0305  -0.0463 -0.0542 701  MET B CB  
3528 C CG  . MET B 196 ? 0.2801 0.2829 0.2590 0.0215  -0.0567 -0.0413 701  MET B CG  
3529 S SD  . MET B 196 ? 0.4188 0.4387 0.4289 0.0284  -0.0638 -0.0405 701  MET B SD  
3530 C CE  . MET B 196 ? 0.2768 0.3003 0.2813 0.0168  -0.0720 -0.0257 701  MET B CE  
3531 N N   . HIS B 197 ? 0.2515 0.2465 0.2030 0.0186  -0.0168 -0.0458 702  HIS B N   
3532 C CA  . HIS B 197 ? 0.2688 0.2596 0.2031 0.0114  -0.0112 -0.0348 702  HIS B CA  
3533 C C   . HIS B 197 ? 0.3560 0.3216 0.2436 0.0108  -0.0094 -0.0346 702  HIS B C   
3534 O O   . HIS B 197 ? 0.3759 0.3305 0.2375 0.0061  -0.0194 -0.0263 702  HIS B O   
3535 C CB  . HIS B 197 ? 0.2664 0.2708 0.2262 0.0112  0.0090  -0.0340 702  HIS B CB  
3536 C CG  . HIS B 197 ? 0.2603 0.2521 0.1939 0.0057  0.0188  -0.0226 702  HIS B CG  
3537 N ND1 . HIS B 197 ? 0.2867 0.2798 0.2175 0.0005  0.0082  -0.0107 702  HIS B ND1 
3538 C CD2 . HIS B 197 ? 0.2866 0.2610 0.1915 0.0062  0.0383  -0.0212 702  HIS B CD2 
3539 C CE1 . HIS B 197 ? 0.3530 0.3285 0.2534 -0.0015 0.0191  -0.0023 702  HIS B CE1 
3540 N NE2 . HIS B 197 ? 0.3885 0.3511 0.2707 0.0018  0.0383  -0.0078 702  HIS B NE2 
3541 N N   . GLN B 198 ? 0.2942 0.2501 0.1700 0.0172  0.0022  -0.0449 703  GLN B N   
3542 C CA  . GLN B 198 ? 0.3751 0.3046 0.2025 0.0188  0.0042  -0.0461 703  GLN B CA  
3543 C C   . GLN B 198 ? 0.3731 0.2874 0.1778 0.0166  -0.0201 -0.0477 703  GLN B C   
3544 O O   . GLN B 198 ? 0.4480 0.3419 0.2136 0.0158  -0.0273 -0.0460 703  GLN B O   
3545 C CB  . GLN B 198 ? 0.4004 0.3243 0.2227 0.0271  0.0240  -0.0581 703  GLN B CB  
3546 C CG  . GLN B 198 ? 0.3719 0.2989 0.2110 0.0340  0.0163  -0.0715 703  GLN B CG  
3547 C CD  . GLN B 198 ? 0.3818 0.2821 0.1813 0.0364  0.0020  -0.0771 703  GLN B CD  
3548 O OE1 . GLN B 198 ? 0.4568 0.3361 0.2148 0.0377  0.0059  -0.0770 703  GLN B OE1 
3549 N NE2 . GLN B 198 ? 0.3691 0.2671 0.1789 0.0377  -0.0149 -0.0822 703  GLN B NE2 
3550 N N   . TYR B 199 ? 0.3433 0.2651 0.1713 0.0161  -0.0327 -0.0515 704  TYR B N   
3551 C CA  . TYR B 199 ? 0.3873 0.2955 0.2008 0.0111  -0.0537 -0.0519 704  TYR B CA  
3552 C C   . TYR B 199 ? 0.3483 0.2646 0.1668 0.0020  -0.0667 -0.0411 704  TYR B C   
3553 O O   . TYR B 199 ? 0.3639 0.2687 0.1669 -0.0033 -0.0826 -0.0415 704  TYR B O   
3554 C CB  . TYR B 199 ? 0.3525 0.2620 0.1863 0.0135  -0.0601 -0.0575 704  TYR B CB  
3555 C CG  . TYR B 199 ? 0.3598 0.2570 0.1874 0.0057  -0.0786 -0.0559 704  TYR B CG  
3556 C CD1 . TYR B 199 ? 0.3692 0.2450 0.1769 0.0054  -0.0841 -0.0622 704  TYR B CD1 
3557 C CD2 . TYR B 199 ? 0.3536 0.2642 0.2034 -0.0019 -0.0866 -0.0470 704  TYR B CD2 
3558 C CE1 . TYR B 199 ? 0.3495 0.2208 0.1666 -0.0032 -0.0939 -0.0583 704  TYR B CE1 
3559 C CE2 . TYR B 199 ? 0.2902 0.1963 0.1477 -0.0100 -0.0939 -0.0431 704  TYR B CE2 
3560 C CZ  . TYR B 199 ? 0.3651 0.2508 0.2063 -0.0111 -0.0979 -0.0492 704  TYR B CZ  
3561 O OH  . TYR B 199 ? 0.3908 0.2701 0.2402 -0.0199 -0.1053 -0.0469 704  TYR B OH  
3562 N N   . MET B 200 ? 0.3782 0.3149 0.2214 0.0004  -0.0606 -0.0328 705  MET B N   
3563 C CA  . MET B 200 ? 0.3519 0.3000 0.2069 -0.0067 -0.0729 -0.0235 705  MET B CA  
3564 C C   . MET B 200 ? 0.3891 0.3266 0.2153 -0.0084 -0.0785 -0.0187 705  MET B C   
3565 O O   . MET B 200 ? 0.3918 0.3386 0.2312 -0.0129 -0.0891 -0.0143 705  MET B O   
3566 C CB  . MET B 200 ? 0.3414 0.3129 0.2311 -0.0060 -0.0652 -0.0176 705  MET B CB  
3567 C CG  . MET B 200 ? 0.3963 0.3829 0.3093 -0.0111 -0.0776 -0.0115 705  MET B CG  
3568 S SD  . MET B 200 ? 0.3242 0.3341 0.2760 -0.0063 -0.0689 -0.0096 705  MET B SD  
3569 C CE  . MET B 200 ? 0.3777 0.3885 0.3258 -0.0049 -0.0527 -0.0065 705  MET B CE  
3570 N N   . THR B 201 ? 0.3238 0.2465 0.1212 -0.0028 -0.0651 -0.0192 706  THR B N   
3571 C CA  . THR B 201 ? 0.3655 0.2756 0.1324 -0.0016 -0.0676 -0.0123 706  THR B CA  
3572 C C   . THR B 201 ? 0.3903 0.2950 0.1499 -0.0024 -0.0846 -0.0152 706  THR B C   
3573 O O   . THR B 201 ? 0.3836 0.2917 0.1440 -0.0020 -0.0911 -0.0097 706  THR B O   
3574 C CB  . THR B 201 ? 0.4385 0.3305 0.1742 0.0053  -0.0449 -0.0120 706  THR B CB  
3575 O OG1 . THR B 201 ? 0.5280 0.4024 0.2382 0.0102  -0.0430 -0.0230 706  THR B OG1 
3576 C CG2 . THR B 201 ? 0.3887 0.2992 0.1596 0.0048  -0.0214 -0.0095 706  THR B CG2 
3577 N N   . LYS B 202 ? 0.3749 0.2734 0.1345 -0.0029 -0.0899 -0.0243 707  LYS B N   
3578 C CA  . LYS B 202 ? 0.3889 0.2851 0.1502 -0.0044 -0.1038 -0.0280 707  LYS B CA  
3579 C C   . LYS B 202 ? 0.3745 0.2940 0.1763 -0.0117 -0.1131 -0.0251 707  LYS B C   
3580 O O   . LYS B 202 ? 0.4215 0.3414 0.2274 -0.0132 -0.1245 -0.0286 707  LYS B O   
3581 C CB  . LYS B 202 ? 0.4091 0.2902 0.1595 -0.0035 -0.1067 -0.0384 707  LYS B CB  
3582 C CG  . LYS B 202 ? 0.3829 0.2707 0.1577 -0.0081 -0.1046 -0.0415 707  LYS B CG  
3583 C CD  . LYS B 202 ? 0.4084 0.2778 0.1702 -0.0065 -0.1084 -0.0516 707  LYS B CD  
3584 C CE  . LYS B 202 ? 0.4215 0.2888 0.1937 -0.0061 -0.1022 -0.0553 707  LYS B CE  
3585 N NZ  . LYS B 202 ? 0.4361 0.3016 0.1946 0.0020  -0.0877 -0.0571 707  LYS B NZ  
3586 N N   . PHE B 203 ? 0.3340 0.2723 0.1651 -0.0155 -0.1077 -0.0198 708  PHE B N   
3587 C CA  . PHE B 203 ? 0.3391 0.2990 0.2064 -0.0206 -0.1115 -0.0167 708  PHE B CA  
3588 C C   . PHE B 203 ? 0.3579 0.3322 0.2356 -0.0183 -0.1082 -0.0088 708  PHE B C   
3589 O O   . PHE B 203 ? 0.2425 0.2356 0.1503 -0.0206 -0.1062 -0.0060 708  PHE B O   
3590 C CB  . PHE B 203 ? 0.3529 0.3204 0.2443 -0.0252 -0.1073 -0.0170 708  PHE B CB  
3591 C CG  . PHE B 203 ? 0.3826 0.3334 0.2645 -0.0277 -0.1111 -0.0244 708  PHE B CG  
3592 C CD1 . PHE B 203 ? 0.3594 0.3048 0.2425 -0.0321 -0.1210 -0.0297 708  PHE B CD1 
3593 C CD2 . PHE B 203 ? 0.2961 0.2357 0.1684 -0.0251 -0.1057 -0.0273 708  PHE B CD2 
3594 C CE1 . PHE B 203 ? 0.3461 0.2739 0.2206 -0.0347 -0.1250 -0.0368 708  PHE B CE1 
3595 C CE2 . PHE B 203 ? 0.3358 0.2573 0.1981 -0.0263 -0.1092 -0.0345 708  PHE B CE2 
3596 C CZ  . PHE B 203 ? 0.3803 0.2951 0.2433 -0.0316 -0.1187 -0.0387 708  PHE B CZ  
3597 N N   . ASN B 204 ? 0.3780 0.2227 0.2482 -0.0866 -0.0073 0.0058  709  ASN B N   
3598 C CA  . ASN B 204 ? 0.3627 0.2053 0.2276 -0.0822 -0.0158 0.0138  709  ASN B CA  
3599 C C   . ASN B 204 ? 0.3600 0.2245 0.2232 -0.0829 -0.0330 0.0190  709  ASN B C   
3600 O O   . ASN B 204 ? 0.3625 0.2297 0.2094 -0.0937 -0.0401 0.0163  709  ASN B O   
3601 C CB  . ASN B 204 ? 0.3325 0.1552 0.1743 -0.0823 -0.0091 0.0135  709  ASN B CB  
3602 C CG  . ASN B 204 ? 0.3916 0.2173 0.2561 -0.0704 0.0059  0.0089  709  ASN B CG  
3603 O OD1 . ASN B 204 ? 0.3619 0.2034 0.2580 -0.0614 0.0076  0.0082  709  ASN B OD1 
3604 N ND2 . ASN B 204 ? 0.3568 0.1666 0.2043 -0.0723 0.0157  0.0065  709  ASN B ND2 
3605 N N   . GLN B 205 ? 0.3325 0.2153 0.2152 -0.0708 -0.0395 0.0252  710  GLN B N   
3606 C CA  . GLN B 205 ? 0.3170 0.2256 0.2077 -0.0674 -0.0545 0.0300  710  GLN B CA  
3607 C C   . GLN B 205 ? 0.3306 0.2363 0.2128 -0.0568 -0.0618 0.0379  710  GLN B C   
3608 O O   . GLN B 205 ? 0.3145 0.2065 0.1987 -0.0482 -0.0543 0.0399  710  GLN B O   
3609 C CB  . GLN B 205 ? 0.2538 0.1849 0.1738 -0.0611 -0.0543 0.0306  710  GLN B CB  
3610 C CG  . GLN B 205 ? 0.2760 0.2058 0.2033 -0.0702 -0.0458 0.0255  710  GLN B CG  
3611 C CD  . GLN B 205 ? 0.3573 0.2965 0.2816 -0.0847 -0.0507 0.0216  710  GLN B CD  
3612 O OE1 . GLN B 205 ? 0.2730 0.2382 0.2104 -0.0856 -0.0604 0.0230  710  GLN B OE1 
3613 N NE2 . GLN B 205 ? 0.3630 0.2816 0.2726 -0.0965 -0.0433 0.0154  710  GLN B NE2 
3614 N N   . LYS B 206 ? 0.3950 0.3130 0.2684 -0.0579 -0.0771 0.0424  711  LYS B N   
3615 C CA  . LYS B 206 ? 0.3520 0.2654 0.2160 -0.0467 -0.0859 0.0524  711  LYS B CA  
3616 C C   . LYS B 206 ? 0.3199 0.2445 0.2126 -0.0303 -0.0846 0.0566  711  LYS B C   
3617 O O   . LYS B 206 ? 0.3467 0.2547 0.2333 -0.0205 -0.0823 0.0627  711  LYS B O   
3618 C CB  . LYS B 206 ? 0.3872 0.3175 0.2416 -0.0494 -0.1064 0.0574  711  LYS B CB  
3619 C CG  . LYS B 206 ? 0.4609 0.3672 0.2737 -0.0544 -0.1105 0.0616  711  LYS B CG  
3620 C CD  . LYS B 206 ? 0.6290 0.5027 0.4120 -0.0676 -0.0932 0.0540  711  LYS B CD  
3621 C CE  . LYS B 206 ? 0.7793 0.6334 0.5248 -0.0741 -0.0934 0.0545  711  LYS B CE  
3622 N NZ  . LYS B 206 ? 0.8452 0.6630 0.5657 -0.0805 -0.0720 0.0501  711  LYS B NZ  
3623 N N   . GLY B 207 ? 0.3013 0.2514 0.2236 -0.0281 -0.0845 0.0527  712  GLY B N   
3624 C CA  . GLY B 207 ? 0.2923 0.2526 0.2399 -0.0137 -0.0815 0.0542  712  GLY B CA  
3625 C C   . GLY B 207 ? 0.2978 0.2787 0.2686 -0.0161 -0.0754 0.0476  712  GLY B C   
3626 O O   . GLY B 207 ? 0.2997 0.2861 0.2687 -0.0286 -0.0735 0.0431  712  GLY B O   
3627 N N   . VAL B 208 ? 0.2657 0.2556 0.2566 -0.0044 -0.0710 0.0470  713  VAL B N   
3628 C CA  . VAL B 208 ? 0.2642 0.2696 0.2717 -0.0061 -0.0627 0.0412  713  VAL B CA  
3629 C C   . VAL B 208 ? 0.2654 0.3002 0.2897 -0.0128 -0.0679 0.0407  713  VAL B C   
3630 O O   . VAL B 208 ? 0.2428 0.2829 0.2684 -0.0235 -0.0617 0.0369  713  VAL B O   
3631 C CB  . VAL B 208 ? 0.2104 0.2179 0.2321 0.0074  -0.0563 0.0391  713  VAL B CB  
3632 C CG1 . VAL B 208 ? 0.1821 0.2083 0.2181 0.0055  -0.0479 0.0338  713  VAL B CG1 
3633 C CG2 . VAL B 208 ? 0.2133 0.1930 0.2209 0.0100  -0.0499 0.0369  713  VAL B CG2 
3634 N N   . GLU B 209 ? 0.2376 0.2920 0.2770 -0.0064 -0.0795 0.0449  714  GLU B N   
3635 C CA  . GLU B 209 ? 0.2748 0.3623 0.3374 -0.0129 -0.0853 0.0434  714  GLU B CA  
3636 C C   . GLU B 209 ? 0.2520 0.3365 0.2989 -0.0317 -0.0895 0.0407  714  GLU B C   
3637 O O   . GLU B 209 ? 0.2133 0.3149 0.2740 -0.0430 -0.0853 0.0360  714  GLU B O   
3638 C CB  . GLU B 209 ? 0.1979 0.3076 0.2818 -0.0012 -0.1004 0.0492  714  GLU B CB  
3639 C CG  . GLU B 209 ? 0.3270 0.4296 0.4209 0.0186  -0.0969 0.0528  714  GLU B CG  
3640 C CD  . GLU B 209 ? 0.4569 0.5769 0.5789 0.0251  -0.0822 0.0462  714  GLU B CD  
3641 O OE1 . GLU B 209 ? 0.4662 0.6165 0.6133 0.0190  -0.0803 0.0424  714  GLU B OE1 
3642 O OE2 . GLU B 209 ? 0.3832 0.4859 0.5014 0.0351  -0.0717 0.0440  714  GLU B OE2 
3643 N N   . ASP B 210 ? 0.2501 0.3108 0.2673 -0.0360 -0.0959 0.0429  715  ASP B N   
3644 C CA  . ASP B 210 ? 0.2474 0.2996 0.2461 -0.0543 -0.0970 0.0381  715  ASP B CA  
3645 C C   . ASP B 210 ? 0.2811 0.3194 0.2768 -0.0627 -0.0802 0.0327  715  ASP B C   
3646 O O   . ASP B 210 ? 0.2608 0.3036 0.2584 -0.0774 -0.0777 0.0277  715  ASP B O   
3647 C CB  . ASP B 210 ? 0.2658 0.2903 0.2290 -0.0567 -0.1026 0.0406  715  ASP B CB  
3648 C CG  . ASP B 210 ? 0.3156 0.3532 0.2740 -0.0539 -0.1231 0.0466  715  ASP B CG  
3649 O OD1 . ASP B 210 ? 0.2872 0.3578 0.2759 -0.0479 -0.1338 0.0490  715  ASP B OD1 
3650 O OD2 . ASP B 210 ? 0.3637 0.3787 0.2879 -0.0576 -0.1284 0.0491  715  ASP B OD2 
3651 N N   . ALA B 211 ? 0.2456 0.2663 0.2370 -0.0535 -0.0694 0.0338  716  ALA B N   
3652 C CA  . ALA B 211 ? 0.3059 0.3132 0.2941 -0.0590 -0.0561 0.0307  716  ALA B CA  
3653 C C   . ALA B 211 ? 0.2507 0.2796 0.2594 -0.0622 -0.0503 0.0297  716  ALA B C   
3654 O O   . ALA B 211 ? 0.3108 0.3335 0.3170 -0.0733 -0.0427 0.0279  716  ALA B O   
3655 C CB  . ALA B 211 ? 0.2538 0.2414 0.2348 -0.0482 -0.0492 0.0319  716  ALA B CB  
3656 N N   . LEU B 212 ? 0.2586 0.3109 0.2878 -0.0525 -0.0518 0.0309  717  LEU B N   
3657 C CA  . LEU B 212 ? 0.2272 0.3010 0.2763 -0.0561 -0.0433 0.0294  717  LEU B CA  
3658 C C   . LEU B 212 ? 0.2561 0.3465 0.3166 -0.0724 -0.0462 0.0267  717  LEU B C   
3659 O O   . LEU B 212 ? 0.2849 0.3751 0.3480 -0.0834 -0.0354 0.0253  717  LEU B O   
3660 C CB  . LEU B 212 ? 0.1923 0.2891 0.2644 -0.0423 -0.0433 0.0295  717  LEU B CB  
3661 C CG  . LEU B 212 ? 0.2537 0.3351 0.3172 -0.0270 -0.0395 0.0300  717  LEU B CG  
3662 C CD1 . LEU B 212 ? 0.2667 0.3706 0.3560 -0.0141 -0.0375 0.0286  717  LEU B CD1 
3663 C CD2 . LEU B 212 ? 0.2294 0.2915 0.2748 -0.0296 -0.0279 0.0288  717  LEU B CD2 
3664 N N   . VAL B 213 ? 0.1939 0.2979 0.2603 -0.0748 -0.0613 0.0260  718  VAL B N   
3665 C CA  . VAL B 213 ? 0.2939 0.4147 0.3712 -0.0921 -0.0666 0.0215  718  VAL B CA  
3666 C C   . VAL B 213 ? 0.2938 0.3853 0.3464 -0.1075 -0.0600 0.0181  718  VAL B C   
3667 O O   . VAL B 213 ? 0.2370 0.3331 0.2981 -0.1233 -0.0534 0.0139  718  VAL B O   
3668 C CB  . VAL B 213 ? 0.2340 0.3740 0.3179 -0.0905 -0.0879 0.0220  718  VAL B CB  
3669 C CG1 . VAL B 213 ? 0.2136 0.3647 0.3001 -0.1113 -0.0960 0.0152  718  VAL B CG1 
3670 C CG2 . VAL B 213 ? 0.1895 0.3641 0.3088 -0.0760 -0.0935 0.0250  718  VAL B CG2 
3671 N N   . SER B 214 ? 0.2563 0.3161 0.2802 -0.1034 -0.0599 0.0194  719  SER B N   
3672 C CA  . SER B 214 ? 0.3196 0.3495 0.3230 -0.1154 -0.0513 0.0158  719  SER B CA  
3673 C C   . SER B 214 ? 0.3221 0.3427 0.3305 -0.1177 -0.0354 0.0179  719  SER B C   
3674 O O   . SER B 214 ? 0.3106 0.3170 0.3148 -0.1315 -0.0277 0.0150  719  SER B O   
3675 C CB  . SER B 214 ? 0.3151 0.3153 0.2926 -0.1082 -0.0514 0.0168  719  SER B CB  
3676 O OG  . SER B 214 ? 0.3254 0.3290 0.2911 -0.1077 -0.0650 0.0162  719  SER B OG  
3677 N N   . LEU B 215 ? 0.3046 0.3310 0.3198 -0.1044 -0.0302 0.0232  720  LEU B N   
3678 C CA  . LEU B 215 ? 0.3079 0.3251 0.3225 -0.1058 -0.0164 0.0269  720  LEU B CA  
3679 C C   . LEU B 215 ? 0.3244 0.3619 0.3577 -0.1190 -0.0096 0.0254  720  LEU B C   
3680 O O   . LEU B 215 ? 0.3924 0.4147 0.4210 -0.1314 0.0002  0.0261  720  LEU B O   
3681 C CB  . LEU B 215 ? 0.2939 0.3127 0.3069 -0.0894 -0.0137 0.0311  720  LEU B CB  
3682 C CG  . LEU B 215 ? 0.3130 0.3063 0.3081 -0.0790 -0.0149 0.0333  720  LEU B CG  
3683 C CD1 . LEU B 215 ? 0.2664 0.2654 0.2618 -0.0651 -0.0135 0.0350  720  LEU B CD1 
3684 C CD2 . LEU B 215 ? 0.3033 0.2701 0.2859 -0.0850 -0.0078 0.0362  720  LEU B CD2 
3685 N N   . LYS B 216 ? 0.2661 0.3377 0.3232 -0.1165 -0.0139 0.0234  721  LYS B N   
3686 C CA  . LYS B 216 ? 0.2318 0.3270 0.3128 -0.1284 -0.0049 0.0214  721  LYS B CA  
3687 C C   . LYS B 216 ? 0.2844 0.3808 0.3718 -0.1492 -0.0074 0.0155  721  LYS B C   
3688 O O   . LYS B 216 ? 0.3169 0.4142 0.4140 -0.1597 0.0051  0.0141  721  LYS B O   
3689 C CB  . LYS B 216 ? 0.2842 0.4184 0.3957 -0.1195 -0.0095 0.0195  721  LYS B CB  
3690 C CG  . LYS B 216 ? 0.3562 0.4902 0.4646 -0.1024 -0.0013 0.0230  721  LYS B CG  
3691 C CD  . LYS B 216 ? 0.3226 0.4948 0.4662 -0.0938 -0.0025 0.0199  721  LYS B CD  
3692 C CE  . LYS B 216 ? 0.3225 0.5022 0.4728 -0.0920 0.0183  0.0197  721  LYS B CE  
3693 N NZ  . LYS B 216 ? 0.4370 0.6540 0.6259 -0.0826 0.0201  0.0153  721  LYS B NZ  
3694 N N   . THR B 217 ? 0.2702 0.3622 0.3489 -0.1521 -0.0223 0.0109  722  THR B N   
3695 C CA  . THR B 217 ? 0.2930 0.3795 0.3714 -0.1633 -0.0247 0.0023  722  THR B CA  
3696 C C   . THR B 217 ? 0.3469 0.3914 0.3992 -0.1657 -0.0144 0.0014  722  THR B C   
3697 O O   . THR B 217 ? 0.3849 0.4213 0.4347 -0.1749 -0.0152 -0.0062 722  THR B O   
3698 C CB  . THR B 217 ? 0.3445 0.4454 0.4216 -0.1628 -0.0453 -0.0028 722  THR B CB  
3699 O OG1 . THR B 217 ? 0.3528 0.4313 0.4018 -0.1540 -0.0514 0.0010  722  THR B OG1 
3700 C CG2 . THR B 217 ? 0.2596 0.4053 0.3701 -0.1573 -0.0570 -0.0019 722  THR B CG2 
3701 N N   . GLY B 218 ? 0.3499 0.3692 0.3853 -0.1563 -0.0057 0.0087  723  GLY B N   
3702 C CA  . GLY B 218 ? 0.3850 0.3687 0.4034 -0.1544 0.0039  0.0089  723  GLY B CA  
3703 C C   . GLY B 218 ? 0.4430 0.4065 0.4425 -0.1507 -0.0015 0.0040  723  GLY B C   
3704 O O   . GLY B 218 ? 0.4464 0.3844 0.4374 -0.1485 0.0064  0.0029  723  GLY B O   
3705 N N   . LYS B 219 ? 0.3855 0.3599 0.3788 -0.1497 -0.0142 0.0015  724  LYS B N   
3706 C CA  . LYS B 219 ? 0.4464 0.3999 0.4182 -0.1464 -0.0168 -0.0025 724  LYS B CA  
3707 C C   . LYS B 219 ? 0.3750 0.3083 0.3376 -0.1318 -0.0110 0.0033  724  LYS B C   
3708 O O   . LYS B 219 ? 0.3490 0.2636 0.2978 -0.1277 -0.0085 -0.0003 724  LYS B O   
3709 C CB  . LYS B 219 ? 0.4710 0.4407 0.4357 -0.1500 -0.0331 -0.0053 724  LYS B CB  
3710 C CG  . LYS B 219 ? 0.5304 0.5329 0.5139 -0.1597 -0.0439 -0.0090 724  LYS B CG  
3711 C CD  . LYS B 219 ? 0.6833 0.6908 0.6519 -0.1651 -0.0587 -0.0149 724  LYS B CD  
3712 C CE  . LYS B 219 ? 0.6452 0.6927 0.6365 -0.1654 -0.0760 -0.0143 724  LYS B CE  
3713 N NZ  . LYS B 219 ? 0.4845 0.5498 0.4883 -0.1517 -0.0830 -0.0044 724  LYS B NZ  
3714 N N   . LEU B 220 ? 0.3859 0.3242 0.3568 -0.1241 -0.0086 0.0115  725  LEU B N   
3715 C CA  . LEU B 220 ? 0.3164 0.2404 0.2817 -0.1100 -0.0060 0.0165  725  LEU B CA  
3716 C C   . LEU B 220 ? 0.3286 0.2505 0.3004 -0.1048 0.0010  0.0242  725  LEU B C   
3717 O O   . LEU B 220 ? 0.3992 0.3373 0.3783 -0.1106 0.0016  0.0279  725  LEU B O   
3718 C CB  . LEU B 220 ? 0.3476 0.2809 0.3096 -0.1059 -0.0162 0.0193  725  LEU B CB  
3719 C CG  . LEU B 220 ? 0.3551 0.2726 0.3101 -0.0926 -0.0150 0.0208  725  LEU B CG  
3720 C CD1 . LEU B 220 ? 0.3145 0.2151 0.2610 -0.0911 -0.0092 0.0140  725  LEU B CD1 
3721 C CD2 . LEU B 220 ? 0.3498 0.2793 0.3043 -0.0854 -0.0244 0.0230  725  LEU B CD2 
3722 N N   . ASP B 221 ? 0.3370 0.2411 0.3074 -0.0945 0.0064  0.0269  726  ASP B N   
3723 C CA  . ASP B 221 ? 0.3707 0.2696 0.3420 -0.0895 0.0111  0.0358  726  ASP B CA  
3724 C C   . ASP B 221 ? 0.3222 0.2248 0.2880 -0.0807 0.0059  0.0415  726  ASP B C   
3725 O O   . ASP B 221 ? 0.2789 0.1840 0.2399 -0.0806 0.0079  0.0491  726  ASP B O   
3726 C CB  . ASP B 221 ? 0.3240 0.2041 0.2998 -0.0834 0.0166  0.0379  726  ASP B CB  
3727 C CG  . ASP B 221 ? 0.4044 0.2781 0.3851 -0.0926 0.0215  0.0330  726  ASP B CG  
3728 O OD1 . ASP B 221 ? 0.3723 0.2528 0.3540 -0.1034 0.0244  0.0327  726  ASP B OD1 
3729 O OD2 . ASP B 221 ? 0.3865 0.2487 0.3706 -0.0898 0.0226  0.0290  726  ASP B OD2 
3730 N N   . ALA B 222 ? 0.2946 0.1968 0.2599 -0.0738 0.0000  0.0381  727  ALA B N   
3731 C CA  . ALA B 222 ? 0.2763 0.1803 0.2381 -0.0655 -0.0059 0.0425  727  ALA B CA  
3732 C C   . ALA B 222 ? 0.2893 0.1999 0.2528 -0.0625 -0.0119 0.0372  727  ALA B C   
3733 O O   . ALA B 222 ? 0.2871 0.1923 0.2500 -0.0650 -0.0110 0.0314  727  ALA B O   
3734 C CB  . ALA B 222 ? 0.2730 0.1642 0.2361 -0.0546 -0.0058 0.0452  727  ALA B CB  
3735 N N   . PHE B 223 ? 0.2590 0.1842 0.2247 -0.0537 -0.0161 0.0371  728  PHE B N   
3736 C CA  . PHE B 223 ? 0.2276 0.1583 0.1957 -0.0478 -0.0210 0.0331  728  PHE B CA  
3737 C C   . PHE B 223 ? 0.2454 0.1727 0.2148 -0.0370 -0.0230 0.0324  728  PHE B C   
3738 O O   . PHE B 223 ? 0.2927 0.2291 0.2614 -0.0322 -0.0235 0.0333  728  PHE B O   
3739 C CB  . PHE B 223 ? 0.2425 0.1956 0.2166 -0.0478 -0.0241 0.0324  728  PHE B CB  
3740 C CG  . PHE B 223 ? 0.2115 0.1678 0.1875 -0.0398 -0.0295 0.0306  728  PHE B CG  
3741 C CD1 . PHE B 223 ? 0.2542 0.1945 0.2224 -0.0405 -0.0309 0.0294  728  PHE B CD1 
3742 C CD2 . PHE B 223 ? 0.2573 0.2304 0.2425 -0.0316 -0.0314 0.0304  728  PHE B CD2 
3743 C CE1 . PHE B 223 ? 0.2639 0.2031 0.2310 -0.0335 -0.0347 0.0297  728  PHE B CE1 
3744 C CE2 . PHE B 223 ? 0.2565 0.2287 0.2437 -0.0233 -0.0358 0.0302  728  PHE B CE2 
3745 C CZ  . PHE B 223 ? 0.2713 0.2258 0.2483 -0.0245 -0.0379 0.0307  728  PHE B CZ  
3746 N N   . ILE B 224 ? 0.2461 0.1602 0.2170 -0.0344 -0.0233 0.0297  729  ILE B N   
3747 C CA  . ILE B 224 ? 0.2423 0.1531 0.2184 -0.0263 -0.0255 0.0274  729  ILE B CA  
3748 C C   . ILE B 224 ? 0.2586 0.1723 0.2363 -0.0218 -0.0268 0.0239  729  ILE B C   
3749 O O   . ILE B 224 ? 0.2616 0.1680 0.2362 -0.0246 -0.0250 0.0235  729  ILE B O   
3750 C CB  . ILE B 224 ? 0.3014 0.1970 0.2845 -0.0266 -0.0232 0.0262  729  ILE B CB  
3751 C CG1 . ILE B 224 ? 0.2623 0.1554 0.2451 -0.0291 -0.0202 0.0300  729  ILE B CG1 
3752 C CG2 . ILE B 224 ? 0.1993 0.0954 0.1923 -0.0194 -0.0274 0.0230  729  ILE B CG2 
3753 C CD1 . ILE B 224 ? 0.2440 0.1318 0.2372 -0.0276 -0.0114 0.0257  729  ILE B CD1 
3754 N N   . TYR B 225 ? 0.2443 0.1658 0.2243 -0.0150 -0.0292 0.0215  730  TYR B N   
3755 C CA  . TYR B 225 ? 0.1981 0.1206 0.1806 -0.0099 -0.0294 0.0190  730  TYR B CA  
3756 C C   . TYR B 225 ? 0.2098 0.1345 0.1959 -0.0033 -0.0304 0.0133  730  TYR B C   
3757 O O   . TYR B 225 ? 0.1943 0.1217 0.1779 -0.0033 -0.0326 0.0116  730  TYR B O   
3758 C CB  . TYR B 225 ? 0.1962 0.1320 0.1781 -0.0097 -0.0305 0.0224  730  TYR B CB  
3759 C CG  . TYR B 225 ? 0.2288 0.1623 0.2132 -0.0036 -0.0320 0.0230  730  TYR B CG  
3760 C CD1 . TYR B 225 ? 0.2418 0.1607 0.2192 -0.0060 -0.0322 0.0256  730  TYR B CD1 
3761 C CD2 . TYR B 225 ? 0.1941 0.1378 0.1866 0.0050  -0.0320 0.0213  730  TYR B CD2 
3762 C CE1 . TYR B 225 ? 0.2543 0.1676 0.2306 0.0002  -0.0340 0.0287  730  TYR B CE1 
3763 C CE2 . TYR B 225 ? 0.2591 0.1981 0.2552 0.0123  -0.0335 0.0234  730  TYR B CE2 
3764 C CZ  . TYR B 225 ? 0.2323 0.1555 0.2193 0.0100  -0.0354 0.0282  730  TYR B CZ  
3765 O OH  . TYR B 225 ? 0.1881 0.1032 0.1755 0.0178  -0.0374 0.0327  730  TYR B OH  
3766 N N   . ASP B 226 ? 0.1983 0.1195 0.1882 0.0019  -0.0292 0.0105  731  ASP B N   
3767 C CA  . ASP B 226 ? 0.2309 0.1520 0.2240 0.0076  -0.0287 0.0030  731  ASP B CA  
3768 C C   . ASP B 226 ? 0.2526 0.1872 0.2395 0.0089  -0.0287 0.0006  731  ASP B C   
3769 O O   . ASP B 226 ? 0.2085 0.1553 0.1939 0.0083  -0.0267 0.0050  731  ASP B O   
3770 C CB  . ASP B 226 ? 0.2384 0.1544 0.2364 0.0141  -0.0260 0.0029  731  ASP B CB  
3771 C CG  . ASP B 226 ? 0.2447 0.1586 0.2466 0.0199  -0.0232 -0.0065 731  ASP B CG  
3772 O OD1 . ASP B 226 ? 0.2633 0.1649 0.2683 0.0185  -0.0227 -0.0134 731  ASP B OD1 
3773 O OD2 . ASP B 226 ? 0.2371 0.1619 0.2405 0.0254  -0.0207 -0.0081 731  ASP B OD2 
3774 N N   . ALA B 227 ? 0.2524 0.1849 0.2352 0.0095  -0.0307 -0.0069 732  ALA B N   
3775 C CA  . ALA B 227 ? 0.3175 0.2591 0.2869 0.0092  -0.0304 -0.0089 732  ALA B CA  
3776 C C   . ALA B 227 ? 0.2880 0.2378 0.2578 0.0143  -0.0223 -0.0131 732  ALA B C   
3777 O O   . ALA B 227 ? 0.2811 0.2426 0.2453 0.0131  -0.0174 -0.0100 732  ALA B O   
3778 C CB  . ALA B 227 ? 0.2785 0.2154 0.2401 0.0082  -0.0370 -0.0165 732  ALA B CB  
3779 N N   . ALA B 228 ? 0.2021 0.1452 0.1810 0.0200  -0.0194 -0.0204 733  ALA B N   
3780 C CA  . ALA B 228 ? 0.2782 0.2278 0.2613 0.0267  -0.0106 -0.0260 733  ALA B CA  
3781 C C   . ALA B 228 ? 0.2753 0.2395 0.2715 0.0296  -0.0075 -0.0172 733  ALA B C   
3782 O O   . ALA B 228 ? 0.2713 0.2497 0.2712 0.0322  0.0004  -0.0193 733  ALA B O   
3783 C CB  . ALA B 228 ? 0.2623 0.1975 0.2546 0.0328  -0.0078 -0.0348 733  ALA B CB  
3784 N N   . VAL B 229 ? 0.2329 0.1949 0.2367 0.0285  -0.0134 -0.0080 734  VAL B N   
3785 C CA  . VAL B 229 ? 0.2042 0.1817 0.2207 0.0302  -0.0141 -0.0001 734  VAL B CA  
3786 C C   . VAL B 229 ? 0.2034 0.1965 0.2152 0.0219  -0.0123 0.0034  734  VAL B C   
3787 O O   . VAL B 229 ? 0.1860 0.1983 0.2097 0.0232  -0.0072 0.0038  734  VAL B O   
3788 C CB  . VAL B 229 ? 0.1974 0.1656 0.2159 0.0294  -0.0217 0.0082  734  VAL B CB  
3789 C CG1 . VAL B 229 ? 0.1659 0.1520 0.1929 0.0273  -0.0261 0.0160  734  VAL B CG1 
3790 C CG2 . VAL B 229 ? 0.2087 0.1618 0.2337 0.0387  -0.0213 0.0072  734  VAL B CG2 
3791 N N   . LEU B 230 ? 0.1919 0.1767 0.1888 0.0134  -0.0156 0.0060  735  LEU B N   
3792 C CA  . LEU B 230 ? 0.2568 0.2509 0.2471 0.0051  -0.0128 0.0104  735  LEU B CA  
3793 C C   . LEU B 230 ? 0.2347 0.2372 0.2178 0.0058  -0.0032 0.0055  735  LEU B C   
3794 O O   . LEU B 230 ? 0.2721 0.2889 0.2587 0.0011  0.0039  0.0082  735  LEU B O   
3795 C CB  . LEU B 230 ? 0.1819 0.1614 0.1586 -0.0016 -0.0178 0.0144  735  LEU B CB  
3796 C CG  . LEU B 230 ? 0.2383 0.2093 0.2195 -0.0054 -0.0234 0.0190  735  LEU B CG  
3797 C CD1 . LEU B 230 ? 0.2308 0.1896 0.2028 -0.0115 -0.0253 0.0227  735  LEU B CD1 
3798 C CD2 . LEU B 230 ? 0.2379 0.2221 0.2289 -0.0091 -0.0234 0.0228  735  LEU B CD2 
3799 N N   . ASN B 231 ? 0.2674 0.2607 0.2395 0.0104  -0.0019 -0.0026 736  ASN B N   
3800 C CA  . ASN B 231 ? 0.2940 0.2928 0.2541 0.0109  0.0088  -0.0092 736  ASN B CA  
3801 C C   . ASN B 231 ? 0.3137 0.3309 0.2956 0.0160  0.0199  -0.0124 736  ASN B C   
3802 O O   . ASN B 231 ? 0.2573 0.2865 0.2365 0.0124  0.0318  -0.0132 736  ASN B O   
3803 C CB  . ASN B 231 ? 0.3268 0.3117 0.2722 0.0146  0.0069  -0.0199 736  ASN B CB  
3804 C CG  . ASN B 231 ? 0.3748 0.3606 0.2969 0.0128  0.0170  -0.0273 736  ASN B CG  
3805 O OD1 . ASN B 231 ? 0.3867 0.3828 0.3162 0.0160  0.0309  -0.0332 736  ASN B OD1 
3806 N ND2 . ASN B 231 ? 0.4626 0.4377 0.3562 0.0078  0.0100  -0.0272 736  ASN B ND2 
3807 N N   . TYR B 232 ? 0.2843 0.3038 0.2892 0.0247  0.0168  -0.0137 737  TYR B N   
3808 C CA  . TYR B 232 ? 0.2622 0.3010 0.2943 0.0321  0.0253  -0.0161 737  TYR B CA  
3809 C C   . TYR B 232 ? 0.2516 0.3126 0.3007 0.0259  0.0247  -0.0077 737  TYR B C   
3810 O O   . TYR B 232 ? 0.2609 0.3426 0.3262 0.0259  0.0363  -0.0104 737  TYR B O   
3811 C CB  . TYR B 232 ? 0.2620 0.2943 0.3129 0.0441  0.0197  -0.0169 737  TYR B CB  
3812 C CG  . TYR B 232 ? 0.2534 0.3071 0.3386 0.0540  0.0233  -0.0157 737  TYR B CG  
3813 C CD1 . TYR B 232 ? 0.2566 0.3192 0.3563 0.0623  0.0384  -0.0256 737  TYR B CD1 
3814 C CD2 . TYR B 232 ? 0.2354 0.3010 0.3392 0.0553  0.0113  -0.0051 737  TYR B CD2 
3815 C CE1 . TYR B 232 ? 0.2779 0.3625 0.4155 0.0731  0.0414  -0.0244 737  TYR B CE1 
3816 C CE2 . TYR B 232 ? 0.2323 0.3204 0.3708 0.0654  0.0113  -0.0031 737  TYR B CE2 
3817 C CZ  . TYR B 232 ? 0.2793 0.3779 0.4376 0.0750  0.0264  -0.0124 737  TYR B CZ  
3818 O OH  . TYR B 232 ? 0.3812 0.5048 0.5805 0.0867  0.0263  -0.0104 737  TYR B OH  
3819 N N   . LYS B 233 ? 0.1803 0.2374 0.2269 0.0196  0.0123  0.0012  738  LYS B N   
3820 C CA  . LYS B 233 ? 0.2480 0.3247 0.3100 0.0116  0.0103  0.0074  738  LYS B CA  
3821 C C   . LYS B 233 ? 0.3095 0.3912 0.3600 -0.0001 0.0215  0.0080  738  LYS B C   
3822 O O   . LYS B 233 ? 0.2968 0.4007 0.3669 -0.0060 0.0275  0.0090  738  LYS B O   
3823 C CB  . LYS B 233 ? 0.2952 0.3618 0.3515 0.0064  -0.0041 0.0147  738  LYS B CB  
3824 C CG  . LYS B 233 ? 0.3013 0.3635 0.3675 0.0165  -0.0147 0.0168  738  LYS B CG  
3825 C CD  . LYS B 233 ? 0.2350 0.3242 0.3325 0.0225  -0.0180 0.0186  738  LYS B CD  
3826 C CE  . LYS B 233 ? 0.3589 0.4406 0.4612 0.0325  -0.0308 0.0240  738  LYS B CE  
3827 N NZ  . LYS B 233 ? 0.2433 0.3529 0.3748 0.0369  -0.0400 0.0285  738  LYS B NZ  
3828 N N   . ALA B 234 ? 0.2798 0.3413 0.2996 -0.0039 0.0240  0.0079  739  ALA B N   
3829 C CA  . ALA B 234 ? 0.3077 0.3689 0.3109 -0.0145 0.0348  0.0107  739  ALA B CA  
3830 C C   . ALA B 234 ? 0.3850 0.4625 0.3955 -0.0131 0.0529  0.0040  739  ALA B C   
3831 O O   . ALA B 234 ? 0.3468 0.4374 0.3637 -0.0225 0.0647  0.0064  739  ALA B O   
3832 C CB  . ALA B 234 ? 0.3114 0.3469 0.2791 -0.0165 0.0306  0.0133  739  ALA B CB  
3833 N N   . GLY B 235 ? 0.4662 0.5422 0.4769 -0.0023 0.0573  -0.0054 740  GLY B N   
3834 C CA  . GLY B 235 ? 0.4536 0.5434 0.4716 0.0000  0.0771  -0.0141 740  GLY B CA  
3835 C C   . GLY B 235 ? 0.4584 0.5798 0.5228 0.0029  0.0837  -0.0155 740  GLY B C   
3836 O O   . GLY B 235 ? 0.5252 0.6621 0.6011 0.0025  0.1034  -0.0221 740  GLY B O   
3837 N N   . ARG B 236 ? 0.3116 0.4435 0.4026 0.0057  0.0678  -0.0098 741  ARG B N   
3838 C CA  . ARG B 236 ? 0.2942 0.4591 0.4323 0.0094  0.0688  -0.0104 741  ARG B CA  
3839 C C   . ARG B 236 ? 0.3003 0.4800 0.4516 -0.0040 0.0606  -0.0025 741  ARG B C   
3840 O O   . ARG B 236 ? 0.2884 0.4968 0.4796 -0.0018 0.0547  -0.0020 741  ARG B O   
3841 C CB  . ARG B 236 ? 0.2682 0.4347 0.4287 0.0261  0.0557  -0.0110 741  ARG B CB  
3842 C CG  . ARG B 236 ? 0.3760 0.5410 0.5462 0.0406  0.0691  -0.0215 741  ARG B CG  
3843 C CD  . ARG B 236 ? 0.3474 0.5109 0.5408 0.0573  0.0560  -0.0195 741  ARG B CD  
3844 N NE  . ARG B 236 ? 0.4438 0.6293 0.6791 0.0715  0.0675  -0.0262 741  ARG B NE  
3845 C CZ  . ARG B 236 ? 0.4206 0.5966 0.6545 0.0803  0.0856  -0.0384 741  ARG B CZ  
3846 N NH1 . ARG B 236 ? 0.3707 0.5167 0.5615 0.0756  0.0925  -0.0455 741  ARG B NH1 
3847 N NH2 . ARG B 236 ? 0.5635 0.7610 0.8415 0.0942  0.0967  -0.0442 741  ARG B NH2 
3848 N N   . ASP B 237 ? 0.3173 0.4784 0.4377 -0.0175 0.0593  0.0032  742  ASP B N   
3849 C CA  . ASP B 237 ? 0.2871 0.4579 0.4178 -0.0318 0.0531  0.0089  742  ASP B CA  
3850 C C   . ASP B 237 ? 0.2854 0.4839 0.4427 -0.0420 0.0707  0.0060  742  ASP B C   
3851 O O   . ASP B 237 ? 0.3326 0.5273 0.4765 -0.0452 0.0911  0.0034  742  ASP B O   
3852 C CB  . ASP B 237 ? 0.3297 0.4693 0.4215 -0.0421 0.0493  0.0156  742  ASP B CB  
3853 C CG  . ASP B 237 ? 0.3260 0.4700 0.4263 -0.0571 0.0430  0.0200  742  ASP B CG  
3854 O OD1 . ASP B 237 ? 0.3248 0.4772 0.4407 -0.0557 0.0270  0.0202  742  ASP B OD1 
3855 O OD2 . ASP B 237 ? 0.3918 0.5286 0.4809 -0.0707 0.0545  0.0233  742  ASP B OD2 
3856 N N   . GLU B 238 ? 0.2841 0.5109 0.4787 -0.0480 0.0629  0.0061  743  GLU B N   
3857 C CA  . GLU B 238 ? 0.2818 0.5390 0.5094 -0.0597 0.0791  0.0025  743  GLU B CA  
3858 C C   . GLU B 238 ? 0.3009 0.5381 0.4994 -0.0788 0.0934  0.0069  743  GLU B C   
3859 O O   . GLU B 238 ? 0.3124 0.5299 0.4910 -0.0888 0.0826  0.0126  743  GLU B O   
3860 C CB  . GLU B 238 ? 0.1943 0.4860 0.4672 -0.0637 0.0629  0.0016  743  GLU B CB  
3861 N N   . GLY B 239 ? 0.2633 0.5030 0.4578 -0.0836 0.1191  0.0044  744  GLY B N   
3862 C CA  . GLY B 239 ? 0.3152 0.5315 0.4770 -0.1002 0.1349  0.0106  744  GLY B CA  
3863 C C   . GLY B 239 ? 0.3915 0.5642 0.4949 -0.0958 0.1320  0.0177  744  GLY B C   
3864 O O   . GLY B 239 ? 0.3517 0.5014 0.4233 -0.1074 0.1447  0.0250  744  GLY B O   
3865 N N   . CYS B 240 ? 0.4027 0.5634 0.4925 -0.0797 0.1152  0.0165  745  CYS B N   
3866 C CA  . CYS B 240 ? 0.3419 0.4660 0.3824 -0.0744 0.1095  0.0217  745  CYS B CA  
3867 C C   . CYS B 240 ? 0.3749 0.4728 0.3920 -0.0852 0.1015  0.0324  745  CYS B C   
3868 O O   . CYS B 240 ? 0.3675 0.4382 0.3461 -0.0888 0.1071  0.0400  745  CYS B O   
3869 C CB  . CYS B 240 ? 0.3342 0.4481 0.3444 -0.0736 0.1296  0.0197  745  CYS B CB  
3870 S SG  . CYS B 240 ? 0.3639 0.5058 0.4023 -0.0614 0.1447  0.0048  745  CYS B SG  
3871 N N   . LYS B 241 ? 0.3211 0.4261 0.3610 -0.0899 0.0880  0.0329  746  LYS B N   
3872 C CA  . LYS B 241 ? 0.4263 0.5065 0.4493 -0.1003 0.0820  0.0410  746  LYS B CA  
3873 C C   . LYS B 241 ? 0.3508 0.4062 0.3522 -0.0901 0.0640  0.0439  746  LYS B C   
3874 O O   . LYS B 241 ? 0.3845 0.4120 0.3624 -0.0942 0.0622  0.0518  746  LYS B O   
3875 C CB  . LYS B 241 ? 0.3443 0.4429 0.4001 -0.1133 0.0783  0.0380  746  LYS B CB  
3876 N N   . LEU B 242 ? 0.3272 0.3916 0.3383 -0.0768 0.0518  0.0381  747  LEU B N   
3877 C CA  . LEU B 242 ? 0.3136 0.3569 0.3085 -0.0678 0.0368  0.0395  747  LEU B CA  
3878 C C   . LEU B 242 ? 0.3166 0.3477 0.2876 -0.0570 0.0380  0.0390  747  LEU B C   
3879 O O   . LEU B 242 ? 0.3584 0.4036 0.3346 -0.0504 0.0447  0.0328  747  LEU B O   
3880 C CB  . LEU B 242 ? 0.3291 0.3852 0.3453 -0.0611 0.0233  0.0342  747  LEU B CB  
3881 C CG  . LEU B 242 ? 0.3266 0.3987 0.3657 -0.0716 0.0187  0.0329  747  LEU B CG  
3882 C CD1 . LEU B 242 ? 0.2771 0.3571 0.3281 -0.0636 0.0033  0.0299  747  LEU B CD1 
3883 C CD2 . LEU B 242 ? 0.2954 0.3462 0.3211 -0.0849 0.0194  0.0372  747  LEU B CD2 
3884 N N   . VAL B 243 ? 0.2892 0.2948 0.2355 -0.0552 0.0314  0.0448  748  VAL B N   
3885 C CA  . VAL B 243 ? 0.3467 0.3401 0.2677 -0.0469 0.0294  0.0444  748  VAL B CA  
3886 C C   . VAL B 243 ? 0.3607 0.3379 0.2771 -0.0400 0.0139  0.0451  748  VAL B C   
3887 O O   . VAL B 243 ? 0.3187 0.2874 0.2435 -0.0431 0.0080  0.0486  748  VAL B O   
3888 C CB  . VAL B 243 ? 0.3838 0.3630 0.2745 -0.0530 0.0388  0.0530  748  VAL B CB  
3889 C CG1 . VAL B 243 ? 0.3037 0.2988 0.1993 -0.0611 0.0581  0.0515  748  VAL B CG1 
3890 C CG2 . VAL B 243 ? 0.3327 0.2907 0.2154 -0.0591 0.0346  0.0645  748  VAL B CG2 
3891 N N   . THR B 244 ? 0.3497 0.3227 0.2537 -0.0314 0.0084  0.0403  749  THR B N   
3892 C CA  . THR B 244 ? 0.4054 0.3644 0.3057 -0.0256 -0.0054 0.0405  749  THR B CA  
3893 C C   . THR B 244 ? 0.4550 0.3976 0.3294 -0.0265 -0.0096 0.0496  749  THR B C   
3894 O O   . THR B 244 ? 0.4862 0.4273 0.3364 -0.0285 -0.0035 0.0521  749  THR B O   
3895 C CB  . THR B 244 ? 0.4040 0.3671 0.3074 -0.0171 -0.0102 0.0295  749  THR B CB  
3896 O OG1 . THR B 244 ? 0.4334 0.4001 0.3175 -0.0159 -0.0035 0.0247  749  THR B OG1 
3897 C CG2 . THR B 244 ? 0.3236 0.2986 0.2526 -0.0143 -0.0083 0.0235  749  THR B CG2 
3898 N N   . ILE B 245 ? 0.5050 0.4347 0.3843 -0.0247 -0.0198 0.0549  750  ILE B N   
3899 C CA  . ILE B 245 ? 0.5210 0.4345 0.3802 -0.0239 -0.0260 0.0662  750  ILE B CA  
3900 C C   . ILE B 245 ? 0.6114 0.5245 0.4518 -0.0172 -0.0373 0.0627  750  ILE B C   
3901 O O   . ILE B 245 ? 0.6192 0.5418 0.4678 -0.0132 -0.0414 0.0505  750  ILE B O   
3902 C CB  . ILE B 245 ? 0.4997 0.4004 0.3758 -0.0227 -0.0323 0.0721  750  ILE B CB  
3903 C CG1 . ILE B 245 ? 0.4996 0.4054 0.3985 -0.0167 -0.0410 0.0623  750  ILE B CG1 
3904 C CG2 . ILE B 245 ? 0.5159 0.4135 0.4035 -0.0316 -0.0208 0.0751  750  ILE B CG2 
3905 C CD1 . ILE B 245 ? 0.6339 0.5275 0.5470 -0.0126 -0.0489 0.0671  750  ILE B CD1 
3906 N N   . GLY B 246 ? 0.6172 0.5177 0.4307 -0.0165 -0.0432 0.0740  751  GLY B N   
3907 C CA  . GLY B 246 ? 0.5969 0.4967 0.3866 -0.0117 -0.0563 0.0714  751  GLY B CA  
3908 C C   . GLY B 246 ? 0.6751 0.5835 0.4431 -0.0142 -0.0475 0.0603  751  GLY B C   
3909 O O   . GLY B 246 ? 0.7501 0.6611 0.5050 -0.0109 -0.0580 0.0513  751  GLY B O   
3910 N N   . SER B 247 ? 0.6952 0.6085 0.4608 -0.0204 -0.0279 0.0596  752  SER B N   
3911 C CA  . SER B 247 ? 0.6971 0.6201 0.4498 -0.0221 -0.0152 0.0473  752  SER B CA  
3912 C C   . SER B 247 ? 0.7594 0.6931 0.5344 -0.0163 -0.0206 0.0304  752  SER B C   
3913 O O   . SER B 247 ? 0.7213 0.6551 0.4783 -0.0144 -0.0230 0.0191  752  SER B O   
3914 C CB  . SER B 247 ? 0.7598 0.6721 0.4631 -0.0244 -0.0151 0.0503  752  SER B CB  
3915 O OG  . SER B 247 ? 0.7897 0.7098 0.4803 -0.0274 0.0031  0.0383  752  SER B OG  
3916 N N   . GLY B 248 ? 0.7914 0.7316 0.6036 -0.0141 -0.0220 0.0286  753  GLY B N   
3917 C CA  . GLY B 248 ? 0.7117 0.6582 0.5462 -0.0088 -0.0261 0.0152  753  GLY B CA  
3918 C C   . GLY B 248 ? 0.7511 0.6912 0.5883 -0.0053 -0.0442 0.0124  753  GLY B C   
3919 O O   . GLY B 248 ? 0.7920 0.7328 0.6254 -0.0032 -0.0488 -0.0003 753  GLY B O   
3920 N N   . TYR B 249 ? 0.6466 0.3994 0.6107 -0.0173 -0.1031 0.0161  754  TYR B N   
3921 C CA  . TYR B 249 ? 0.5912 0.3497 0.5540 -0.0125 -0.1232 0.0176  754  TYR B CA  
3922 C C   . TYR B 249 ? 0.4955 0.2832 0.4796 -0.0096 -0.1278 0.0083  754  TYR B C   
3923 O O   . TYR B 249 ? 0.5259 0.3296 0.5293 -0.0087 -0.1178 0.0009  754  TYR B O   
3924 C CB  . TYR B 249 ? 0.6101 0.3590 0.5815 -0.0067 -0.1306 0.0222  754  TYR B CB  
3925 C CG  . TYR B 249 ? 0.6926 0.4447 0.6628 -0.0022 -0.1515 0.0249  754  TYR B CG  
3926 C CD1 . TYR B 249 ? 0.7924 0.5257 0.7343 -0.0037 -0.1624 0.0340  754  TYR B CD1 
3927 C CD2 . TYR B 249 ? 0.6260 0.3998 0.6237 0.0033  -0.1599 0.0176  754  TYR B CD2 
3928 C CE1 . TYR B 249 ? 0.8076 0.5457 0.7520 -0.0004 -0.1812 0.0355  754  TYR B CE1 
3929 C CE2 . TYR B 249 ? 0.6814 0.4595 0.6833 0.0066  -0.1770 0.0193  754  TYR B CE2 
3930 C CZ  . TYR B 249 ? 0.8248 0.5860 0.8017 0.0045  -0.1875 0.0281  754  TYR B CZ  
3931 O OH  . TYR B 249 ? 0.8590 0.6268 0.8435 0.0073  -0.2025 0.0293  754  TYR B OH  
3932 N N   . ILE B 250 ? 0.4894 0.2830 0.4696 -0.0082 -0.1435 0.0092  755  ILE B N   
3933 C CA  . ILE B 250 ? 0.4518 0.2703 0.4497 -0.0053 -0.1474 0.0029  755  ILE B CA  
3934 C C   . ILE B 250 ? 0.4634 0.2875 0.4755 -0.0010 -0.1657 0.0025  755  ILE B C   
3935 O O   . ILE B 250 ? 0.4189 0.2303 0.4177 -0.0040 -0.1792 0.0069  755  ILE B O   
3936 C CB  . ILE B 250 ? 0.4244 0.2449 0.4063 -0.0095 -0.1448 0.0038  755  ILE B CB  
3937 C CG1 . ILE B 250 ? 0.4038 0.2211 0.3775 -0.0140 -0.1252 0.0019  755  ILE B CG1 
3938 C CG2 . ILE B 250 ? 0.3666 0.2093 0.3668 -0.0050 -0.1477 0.0006  755  ILE B CG2 
3939 C CD1 . ILE B 250 ? 0.3479 0.1624 0.3038 -0.0185 -0.1206 0.0025  755  ILE B CD1 
3940 N N   . PHE B 251 ? 0.3941 0.2359 0.4336 0.0048  -0.1654 -0.0043 756  PHE B N   
3941 C CA  . PHE B 251 ? 0.3717 0.2212 0.4302 0.0071  -0.1777 -0.0083 756  PHE B CA  
3942 C C   . PHE B 251 ? 0.3096 0.1732 0.3721 0.0070  -0.1667 -0.0108 756  PHE B C   
3943 O O   . PHE B 251 ? 0.3350 0.2109 0.3974 0.0103  -0.1559 -0.0109 756  PHE B O   
3944 C CB  . PHE B 251 ? 0.3566 0.2137 0.4387 0.0146  -0.1739 -0.0143 756  PHE B CB  
3945 C CG  . PHE B 251 ? 0.4649 0.3293 0.5667 0.0189  -0.1785 -0.0181 756  PHE B CG  
3946 C CD1 . PHE B 251 ? 0.4852 0.3419 0.5874 0.0222  -0.1861 -0.0106 756  PHE B CD1 
3947 C CD2 . PHE B 251 ? 0.4123 0.2928 0.5307 0.0220  -0.1720 -0.0271 756  PHE B CD2 
3948 C CE1 . PHE B 251 ? 0.4890 0.3600 0.6115 0.0289  -0.1874 -0.0115 756  PHE B CE1 
3949 C CE2 . PHE B 251 ? 0.3446 0.2376 0.4803 0.0288  -0.1712 -0.0274 756  PHE B CE2 
3950 C CZ  . PHE B 251 ? 0.4523 0.3427 0.5920 0.0320  -0.1792 -0.0197 756  PHE B CZ  
3951 N N   . ALA B 252 ? 0.3339 0.1912 0.4025 0.0068  -0.1728 -0.0093 757  ALA B N   
3952 C CA  . ALA B 252 ? 0.2610 0.1270 0.3367 0.0074  -0.1678 -0.0093 757  ALA B CA  
3953 C C   . ALA B 252 ? 0.2696 0.1335 0.3246 0.0038  -0.1603 -0.0043 757  ALA B C   
3954 O O   . ALA B 252 ? 0.2270 0.1025 0.2845 0.0056  -0.1501 -0.0064 757  ALA B O   
3955 C CB  . ALA B 252 ? 0.2294 0.1161 0.3261 0.0134  -0.1591 -0.0173 757  ALA B CB  
3956 N N   . THR B 253 ? 0.3119 0.1595 0.3458 -0.0015 -0.1673 0.0020  758  THR B N   
3957 C CA  . THR B 253 ? 0.2835 0.1263 0.2953 -0.0053 -0.1625 0.0061  758  THR B CA  
3958 C C   . THR B 253 ? 0.3124 0.1689 0.3318 -0.0070 -0.1564 0.0047  758  THR B C   
3959 O O   . THR B 253 ? 0.2606 0.1259 0.2907 -0.0092 -0.1603 0.0042  758  THR B O   
3960 C CB  . THR B 253 ? 0.3524 0.1718 0.3373 -0.0113 -0.1727 0.0114  758  THR B CB  
3961 O OG1 . THR B 253 ? 0.4101 0.2278 0.4020 -0.0136 -0.1834 0.0122  758  THR B OG1 
3962 C CG2 . THR B 253 ? 0.4007 0.2081 0.3746 -0.0115 -0.1773 0.0124  758  THR B CG2 
3963 N N   . THR B 254 ? 0.2540 0.1192 0.2690 -0.0073 -0.1451 0.0030  759  THR B N   
3964 C CA  . THR B 254 ? 0.2267 0.1046 0.2458 -0.0106 -0.1377 0.0012  759  THR B CA  
3965 C C   . THR B 254 ? 0.2626 0.1381 0.2655 -0.0137 -0.1283 0.0003  759  THR B C   
3966 O O   . THR B 254 ? 0.2678 0.1303 0.2521 -0.0161 -0.1282 0.0015  759  THR B O   
3967 C CB  . THR B 254 ? 0.2074 0.1040 0.2501 -0.0065 -0.1326 -0.0031 759  THR B CB  
3968 O OG1 . THR B 254 ? 0.2001 0.1065 0.2455 -0.0104 -0.1271 -0.0036 759  THR B OG1 
3969 C CG2 . THR B 254 ? 0.1950 0.0954 0.2423 -0.0005 -0.1267 -0.0071 759  THR B CG2 
3970 N N   . GLY B 255 ? 0.2102 0.0969 0.2200 -0.0144 -0.1200 -0.0021 760  GLY B N   
3971 C CA  . GLY B 255 ? 0.2109 0.0948 0.2088 -0.0170 -0.1103 -0.0040 760  GLY B CA  
3972 C C   . GLY B 255 ? 0.2443 0.1402 0.2545 -0.0151 -0.1037 -0.0064 760  GLY B C   
3973 O O   . GLY B 255 ? 0.2699 0.1756 0.2951 -0.0134 -0.1064 -0.0064 760  GLY B O   
3974 N N   . TYR B 256 ? 0.2615 0.1553 0.2654 -0.0157 -0.0952 -0.0085 761  TYR B N   
3975 C CA  . TYR B 256 ? 0.2471 0.1466 0.2584 -0.0147 -0.0908 -0.0098 761  TYR B CA  
3976 C C   . TYR B 256 ? 0.2229 0.1165 0.2304 -0.0204 -0.0906 -0.0081 761  TYR B C   
3977 O O   . TYR B 256 ? 0.2348 0.1172 0.2287 -0.0255 -0.0896 -0.0081 761  TYR B O   
3978 C CB  . TYR B 256 ? 0.2483 0.1443 0.2553 -0.0140 -0.0822 -0.0124 761  TYR B CB  
3979 C CG  . TYR B 256 ? 0.2400 0.1427 0.2541 -0.0097 -0.0818 -0.0153 761  TYR B CG  
3980 C CD1 . TYR B 256 ? 0.2251 0.1370 0.2500 -0.0051 -0.0881 -0.0162 761  TYR B CD1 
3981 C CD2 . TYR B 256 ? 0.1804 0.0791 0.1926 -0.0103 -0.0741 -0.0178 761  TYR B CD2 
3982 C CE1 . TYR B 256 ? 0.2165 0.1334 0.2486 -0.0019 -0.0871 -0.0199 761  TYR B CE1 
3983 C CE2 . TYR B 256 ? 0.1949 0.0997 0.2162 -0.0079 -0.0738 -0.0211 761  TYR B CE2 
3984 C CZ  . TYR B 256 ? 0.2380 0.1521 0.2687 -0.0039 -0.0805 -0.0222 761  TYR B CZ  
3985 O OH  . TYR B 256 ? 0.2239 0.1431 0.2643 -0.0021 -0.0797 -0.0264 761  TYR B OH  
3986 N N   . GLY B 257 ? 0.2521 0.1518 0.2721 -0.0201 -0.0917 -0.0070 762  GLY B N   
3987 C CA  . GLY B 257 ? 0.1951 0.0890 0.2153 -0.0267 -0.0908 -0.0051 762  GLY B CA  
3988 C C   . GLY B 257 ? 0.2175 0.1101 0.2463 -0.0260 -0.0869 -0.0029 762  GLY B C   
3989 O O   . GLY B 257 ? 0.2184 0.1190 0.2584 -0.0206 -0.0898 -0.0027 762  GLY B O   
3990 N N   . ILE B 258 ? 0.2305 0.1105 0.2536 -0.0310 -0.0802 -0.0014 763  ILE B N   
3991 C CA  . ILE B 258 ? 0.2376 0.1119 0.2693 -0.0303 -0.0751 0.0043  763  ILE B CA  
3992 C C   . ILE B 258 ? 0.2695 0.1537 0.3211 -0.0341 -0.0808 0.0095  763  ILE B C   
3993 O O   . ILE B 258 ? 0.3018 0.1895 0.3588 -0.0418 -0.0837 0.0087  763  ILE B O   
3994 C CB  . ILE B 258 ? 0.2692 0.1260 0.2908 -0.0345 -0.0646 0.0046  763  ILE B CB  
3995 C CG1 . ILE B 258 ? 0.2839 0.1318 0.2885 -0.0327 -0.0584 -0.0015 763  ILE B CG1 
3996 C CG2 . ILE B 258 ? 0.2832 0.1321 0.3116 -0.0302 -0.0568 0.0134  763  ILE B CG2 
3997 C CD1 . ILE B 258 ? 0.3158 0.1635 0.3206 -0.0237 -0.0537 -0.0004 763  ILE B CD1 
3998 N N   . ALA B 259 ? 0.1987 0.1011 0.2584 -0.0244 -0.0766 0.0146  764  ALA B N   
3999 C CA  . ALA B 259 ? 0.2699 0.1919 0.3455 -0.0241 -0.0736 0.0209  764  ALA B CA  
4000 C C   . ALA B 259 ? 0.2837 0.1964 0.3617 -0.0269 -0.0621 0.0312  764  ALA B C   
4001 O O   . ALA B 259 ? 0.2656 0.1670 0.3330 -0.0209 -0.0547 0.0356  764  ALA B O   
4002 C CB  . ALA B 259 ? 0.1845 0.1315 0.2623 -0.0111 -0.0718 0.0213  764  ALA B CB  
4003 N N   . LEU B 260 ? 0.2489 0.1660 0.3433 -0.0361 -0.0606 0.0353  765  LEU B N   
4004 C CA  . LEU B 260 ? 0.2859 0.1939 0.3861 -0.0401 -0.0485 0.0461  765  LEU B CA  
4005 C C   . LEU B 260 ? 0.3041 0.2358 0.4255 -0.0416 -0.0427 0.0534  765  LEU B C   
4006 O O   . LEU B 260 ? 0.2221 0.1742 0.3562 -0.0422 -0.0499 0.0481  765  LEU B O   
4007 C CB  . LEU B 260 ? 0.2485 0.1282 0.3490 -0.0549 -0.0507 0.0426  765  LEU B CB  
4008 C CG  . LEU B 260 ? 0.2963 0.1538 0.3739 -0.0544 -0.0543 0.0327  765  LEU B CG  
4009 C CD1 . LEU B 260 ? 0.2485 0.1137 0.3189 -0.0583 -0.0659 0.0198  765  LEU B CD1 
4010 C CD2 . LEU B 260 ? 0.3059 0.1419 0.3738 -0.0585 -0.0428 0.0323  765  LEU B CD2 
4011 N N   . GLN B 261 ? 0.3062 0.2343 0.4317 -0.0417 -0.0284 0.0663  766  GLN B N   
4012 C CA  . GLN B 261 ? 0.2925 0.2410 0.4393 -0.0446 -0.0192 0.0748  766  GLN B CA  
4013 C C   . GLN B 261 ? 0.2955 0.2452 0.4687 -0.0621 -0.0268 0.0692  766  GLN B C   
4014 O O   . GLN B 261 ? 0.3088 0.2360 0.4809 -0.0738 -0.0350 0.0626  766  GLN B O   
4015 C CB  . GLN B 261 ? 0.2891 0.2287 0.4333 -0.0421 -0.0010 0.0917  766  GLN B CB  
4016 C CG  . GLN B 261 ? 0.3894 0.3293 0.5073 -0.0238 0.0047  0.0986  766  GLN B CG  
4017 C CD  . GLN B 261 ? 0.4416 0.3676 0.5539 -0.0207 0.0215  0.1170  766  GLN B CD  
4018 O OE1 . GLN B 261 ? 0.4803 0.4001 0.6105 -0.0320 0.0320  0.1260  766  GLN B OE1 
4019 N NE2 . GLN B 261 ? 0.4422 0.3632 0.5313 -0.0053 0.0239  0.1234  766  GLN B NE2 
4020 N N   . LYS B 262 ? 0.2891 0.2666 0.4864 -0.0634 -0.0245 0.0712  767  LYS B N   
4021 C CA  . LYS B 262 ? 0.2599 0.2449 0.4878 -0.0791 -0.0334 0.0659  767  LYS B CA  
4022 C C   . LYS B 262 ? 0.2626 0.2286 0.5046 -0.0951 -0.0261 0.0721  767  LYS B C   
4023 O O   . LYS B 262 ? 0.2773 0.2433 0.5254 -0.0946 -0.0075 0.0859  767  LYS B O   
4024 C CB  . LYS B 262 ? 0.2709 0.2919 0.5258 -0.0754 -0.0293 0.0682  767  LYS B CB  
4025 C CG  . LYS B 262 ? 0.2682 0.3061 0.5109 -0.0597 -0.0360 0.0607  767  LYS B CG  
4026 C CD  . LYS B 262 ? 0.3253 0.3966 0.5991 -0.0574 -0.0347 0.0599  767  LYS B CD  
4027 C CE  . LYS B 262 ? 0.3463 0.4234 0.6475 -0.0696 -0.0530 0.0516  767  LYS B CE  
4028 N NZ  . LYS B 262 ? 0.4121 0.4726 0.6912 -0.0678 -0.0732 0.0402  767  LYS B NZ  
4029 N N   . GLY B 263 ? 0.2783 0.2276 0.5186 -0.1070 -0.0397 0.0605  768  GLY B N   
4030 C CA  . GLY B 263 ? 0.3411 0.2707 0.5782 -0.1171 -0.0328 0.0595  768  GLY B CA  
4031 C C   . GLY B 263 ? 0.3277 0.2240 0.5335 -0.1130 -0.0251 0.0607  768  GLY B C   
4032 O O   . GLY B 263 ? 0.4627 0.3414 0.6671 -0.1197 -0.0147 0.0636  768  GLY B O   
4033 N N   . SER B 264 ? 0.3838 0.2711 0.5654 -0.1019 -0.0298 0.0581  769  SER B N   
4034 C CA  . SER B 264 ? 0.3816 0.2406 0.5356 -0.0953 -0.0215 0.0597  769  SER B CA  
4035 C C   . SER B 264 ? 0.3629 0.1983 0.5006 -0.1044 -0.0232 0.0465  769  SER B C   
4036 O O   . SER B 264 ? 0.3765 0.2148 0.5081 -0.1091 -0.0356 0.0325  769  SER B O   
4037 C CB  . SER B 264 ? 0.3456 0.2033 0.4797 -0.0822 -0.0279 0.0572  769  SER B CB  
4038 O OG  . SER B 264 ? 0.4017 0.2349 0.5118 -0.0750 -0.0201 0.0575  769  SER B OG  
4039 N N   . PRO B 265 ? 0.3949 0.2063 0.5238 -0.1064 -0.0105 0.0510  770  PRO B N   
4040 C CA  . PRO B 265 ? 0.3967 0.1823 0.5079 -0.1151 -0.0107 0.0379  770  PRO B CA  
4041 C C   . PRO B 265 ? 0.4101 0.1811 0.4927 -0.1069 -0.0129 0.0275  770  PRO B C   
4042 O O   . PRO B 265 ? 0.4966 0.2489 0.5654 -0.1134 -0.0119 0.0152  770  PRO B O   
4043 C CB  . PRO B 265 ? 0.4269 0.1903 0.5369 -0.1177 0.0034  0.0486  770  PRO B CB  
4044 C CG  . PRO B 265 ? 0.4266 0.1997 0.5409 -0.1032 0.0120  0.0664  770  PRO B CG  
4045 C CD  . PRO B 265 ? 0.3880 0.1945 0.5219 -0.1002 0.0051  0.0692  770  PRO B CD  
4046 N N   . TRP B 266 ? 0.3959 0.1760 0.4717 -0.0931 -0.0146 0.0318  771  TRP B N   
4047 C CA  . TRP B 266 ? 0.3798 0.1500 0.4331 -0.0848 -0.0150 0.0230  771  TRP B CA  
4048 C C   . TRP B 266 ? 0.4548 0.2409 0.5055 -0.0863 -0.0286 0.0110  771  TRP B C   
4049 O O   . TRP B 266 ? 0.4118 0.1902 0.4463 -0.0822 -0.0280 0.0025  771  TRP B O   
4050 C CB  . TRP B 266 ? 0.3677 0.1407 0.4155 -0.0693 -0.0113 0.0333  771  TRP B CB  
4051 C CG  . TRP B 266 ? 0.4015 0.1584 0.4464 -0.0636 0.0004  0.0466  771  TRP B CG  
4052 C CD1 . TRP B 266 ? 0.3733 0.1420 0.4335 -0.0584 0.0052  0.0633  771  TRP B CD1 
4053 C CD2 . TRP B 266 ? 0.4006 0.1282 0.4259 -0.0615 0.0073  0.0458  771  TRP B CD2 
4054 N NE1 . TRP B 266 ? 0.3917 0.1427 0.4444 -0.0522 0.0151  0.0730  771  TRP B NE1 
4055 C CE2 . TRP B 266 ? 0.4108 0.1369 0.4443 -0.0542 0.0139  0.0624  771  TRP B CE2 
4056 C CE3 . TRP B 266 ? 0.4190 0.1252 0.4227 -0.0640 0.0078  0.0333  771  TRP B CE3 
4057 C CZ2 . TRP B 266 ? 0.4832 0.1881 0.5092 -0.0493 0.0185  0.0667  771  TRP B CZ2 
4058 C CZ3 . TRP B 266 ? 0.4620 0.1477 0.4592 -0.0598 0.0051  0.0386  771  TRP B CZ3 
4059 C CH2 . TRP B 266 ? 0.4514 0.1358 0.4624 -0.0525 0.0128  0.0546  771  TRP B CH2 
4060 N N   . LYS B 267 ? 0.3423 0.2231 0.4601 0.0058  -0.1245 -0.0032 772  LYS B N   
4061 C CA  . LYS B 267 ? 0.2980 0.2037 0.4031 0.0109  -0.1212 -0.0080 772  LYS B CA  
4062 C C   . LYS B 267 ? 0.3058 0.2029 0.3944 0.0216  -0.1303 -0.0286 772  LYS B C   
4063 O O   . LYS B 267 ? 0.2910 0.1996 0.3597 0.0349  -0.1250 -0.0338 772  LYS B O   
4064 C CB  . LYS B 267 ? 0.2598 0.1841 0.3791 -0.0044 -0.1212 -0.0008 772  LYS B CB  
4065 C CG  . LYS B 267 ? 0.3142 0.2605 0.4214 0.0011  -0.1203 -0.0058 772  LYS B CG  
4066 C CD  . LYS B 267 ? 0.3654 0.3293 0.4898 -0.0124 -0.1219 -0.0003 772  LYS B CD  
4067 C CE  . LYS B 267 ? 0.2585 0.2370 0.3717 -0.0060 -0.1273 -0.0091 772  LYS B CE  
4068 N NZ  . LYS B 267 ? 0.4569 0.4465 0.5476 0.0076  -0.1169 -0.0061 772  LYS B NZ  
4069 N N   . ARG B 268 ? 0.2937 0.1708 0.3897 0.0151  -0.1440 -0.0406 773  ARG B N   
4070 C CA  . ARG B 268 ? 0.3509 0.2207 0.4300 0.0238  -0.1544 -0.0618 773  ARG B CA  
4071 C C   . ARG B 268 ? 0.4144 0.2731 0.4723 0.0432  -0.1499 -0.0717 773  ARG B C   
4072 O O   . ARG B 268 ? 0.3813 0.2499 0.4161 0.0553  -0.1486 -0.0821 773  ARG B O   
4073 C CB  . ARG B 268 ? 0.3471 0.1945 0.4403 0.0121  -0.1703 -0.0739 773  ARG B CB  
4074 C CG  . ARG B 268 ? 0.4571 0.2894 0.5312 0.0221  -0.1821 -0.0986 773  ARG B CG  
4075 C CD  . ARG B 268 ? 0.5607 0.3766 0.6494 0.0107  -0.1920 -0.1059 773  ARG B CD  
4076 N NE  . ARG B 268 ? 0.7203 0.5103 0.8185 0.0101  -0.1885 -0.1017 773  ARG B NE  
4077 C CZ  . ARG B 268 ? 0.7743 0.5430 0.8588 0.0239  -0.1886 -0.1136 773  ARG B CZ  
4078 N NH1 . ARG B 268 ? 0.6699 0.4399 0.7290 0.0397  -0.1906 -0.1310 773  ARG B NH1 
4079 N NH2 . ARG B 268 ? 0.8339 0.5814 0.9290 0.0223  -0.1851 -0.1070 773  ARG B NH2 
4080 N N   . GLN B 269 ? 0.4112 0.2500 0.4767 0.0470  -0.1469 -0.0681 774  GLN B N   
4081 C CA  . GLN B 269 ? 0.4242 0.2542 0.4735 0.0666  -0.1417 -0.0776 774  GLN B CA  
4082 C C   . GLN B 269 ? 0.3484 0.2072 0.3855 0.0768  -0.1264 -0.0683 774  GLN B C   
4083 O O   . GLN B 269 ? 0.3793 0.2421 0.3968 0.0927  -0.1215 -0.0794 774  GLN B O   
4084 C CB  . GLN B 269 ? 0.4815 0.2841 0.5449 0.0689  -0.1427 -0.0739 774  GLN B CB  
4085 C CG  . GLN B 269 ? 0.4685 0.2388 0.5371 0.0643  -0.1557 -0.0885 774  GLN B CG  
4086 C CD  . GLN B 269 ? 0.5760 0.3292 0.6550 0.0656  -0.1517 -0.0802 774  GLN B CD  
4087 O OE1 . GLN B 269 ? 0.5040 0.2529 0.6000 0.0515  -0.1512 -0.0639 774  GLN B OE1 
4088 N NE2 . GLN B 269 ? 0.6082 0.3528 0.6757 0.0829  -0.1480 -0.0912 774  GLN B NE2 
4089 N N   . ILE B 270 ? 0.3306 0.2096 0.3790 0.0675  -0.1183 -0.0486 775  ILE B N   
4090 C CA  . ILE B 270 ? 0.3431 0.2492 0.3816 0.0748  -0.1041 -0.0399 775  ILE B CA  
4091 C C   . ILE B 270 ? 0.3376 0.2595 0.3559 0.0783  -0.1032 -0.0475 775  ILE B C   
4092 O O   . ILE B 270 ? 0.2862 0.2204 0.2869 0.0906  -0.0938 -0.0507 775  ILE B O   
4093 C CB  . ILE B 270 ? 0.3075 0.2296 0.3622 0.0627  -0.0967 -0.0189 775  ILE B CB  
4094 C CG1 . ILE B 270 ? 0.2962 0.2046 0.3659 0.0622  -0.0964 -0.0096 775  ILE B CG1 
4095 C CG2 . ILE B 270 ? 0.2643 0.2143 0.3093 0.0672  -0.0831 -0.0112 775  ILE B CG2 
4096 C CD1 . ILE B 270 ? 0.2888 0.1980 0.3528 0.0795  -0.0898 -0.0124 775  ILE B CD1 
4097 N N   . ASP B 271 ? 0.2960 0.2187 0.3170 0.0675  -0.1129 -0.0499 776  ASP B N   
4098 C CA  . ASP B 271 ? 0.2877 0.2246 0.2890 0.0713  -0.1143 -0.0558 776  ASP B CA  
4099 C C   . ASP B 271 ? 0.3588 0.2851 0.3348 0.0859  -0.1183 -0.0753 776  ASP B C   
4100 O O   . ASP B 271 ? 0.3308 0.2703 0.2837 0.0965  -0.1102 -0.0771 776  ASP B O   
4101 C CB  . ASP B 271 ? 0.2907 0.2305 0.3036 0.0576  -0.1264 -0.0556 776  ASP B CB  
4102 C CG  . ASP B 271 ? 0.2912 0.2489 0.3228 0.0457  -0.1193 -0.0369 776  ASP B CG  
4103 O OD1 . ASP B 271 ? 0.3298 0.2998 0.3591 0.0488  -0.1052 -0.0251 776  ASP B OD1 
4104 O OD2 . ASP B 271 ? 0.2650 0.2252 0.3140 0.0331  -0.1274 -0.0348 776  ASP B OD2 
4105 N N   . LEU B 272 ? 0.3769 0.2785 0.3560 0.0864  -0.1302 -0.0904 777  LEU B N   
4106 C CA  . LEU B 272 ? 0.4068 0.2965 0.3610 0.1003  -0.1346 -0.1117 777  LEU B CA  
4107 C C   . LEU B 272 ? 0.3771 0.2715 0.3180 0.1169  -0.1192 -0.1126 777  LEU B C   
4108 O O   . LEU B 272 ? 0.3968 0.2967 0.3102 0.1295  -0.1152 -0.1241 777  LEU B O   
4109 C CB  . LEU B 272 ? 0.4056 0.2645 0.3693 0.0967  -0.1496 -0.1278 777  LEU B CB  
4110 C CG  . LEU B 272 ? 0.4113 0.2663 0.3857 0.0811  -0.1667 -0.1326 777  LEU B CG  
4111 C CD1 . LEU B 272 ? 0.4442 0.2664 0.4310 0.0759  -0.1802 -0.1477 777  LEU B CD1 
4112 C CD2 . LEU B 272 ? 0.4234 0.2931 0.3718 0.0855  -0.1734 -0.1430 777  LEU B CD2 
4113 N N   . ALA B 273 ? 0.3650 0.2592 0.3251 0.1171  -0.1103 -0.1004 778  ALA B N   
4114 C CA  . ALA B 273 ? 0.4008 0.3039 0.3537 0.1325  -0.0956 -0.1003 778  ALA B CA  
4115 C C   . ALA B 273 ? 0.3672 0.3002 0.3053 0.1349  -0.0817 -0.0905 778  ALA B C   
4116 O O   . ALA B 273 ? 0.3541 0.2959 0.2714 0.1484  -0.0722 -0.0986 778  ALA B O   
4117 C CB  . ALA B 273 ? 0.3459 0.2441 0.3246 0.1314  -0.0915 -0.0879 778  ALA B CB  
4118 N N   . LEU B 274 ? 0.3284 0.2767 0.2769 0.1218  -0.0796 -0.0732 779  LEU B N   
4119 C CA  . LEU B 274 ? 0.3475 0.3209 0.2836 0.1226  -0.0665 -0.0627 779  LEU B CA  
4120 C C   . LEU B 274 ? 0.3923 0.3685 0.2975 0.1290  -0.0688 -0.0731 779  LEU B C   
4121 O O   . LEU B 274 ? 0.3481 0.3377 0.2334 0.1383  -0.0561 -0.0731 779  LEU B O   
4122 C CB  . LEU B 274 ? 0.2547 0.2398 0.2082 0.1071  -0.0656 -0.0444 779  LEU B CB  
4123 C CG  . LEU B 274 ? 0.2815 0.2707 0.2602 0.1008  -0.0597 -0.0308 779  LEU B CG  
4124 C CD1 . LEU B 274 ? 0.2018 0.2018 0.1941 0.0856  -0.0591 -0.0155 779  LEU B CD1 
4125 C CD2 . LEU B 274 ? 0.2238 0.2285 0.2003 0.1105  -0.0444 -0.0272 779  LEU B CD2 
4126 N N   . LEU B 275 ? 0.3458 0.3104 0.2465 0.1237  -0.0851 -0.0817 780  LEU B N   
4127 C CA  . LEU B 275 ? 0.3568 0.3233 0.2260 0.1304  -0.0900 -0.0924 780  LEU B CA  
4128 C C   . LEU B 275 ? 0.3897 0.3473 0.2351 0.1462  -0.0870 -0.1113 780  LEU B C   
4129 O O   . LEU B 275 ? 0.4100 0.3759 0.2239 0.1552  -0.0820 -0.1163 780  LEU B O   
4130 C CB  . LEU B 275 ? 0.3900 0.3473 0.2632 0.1210  -0.1103 -0.0990 780  LEU B CB  
4131 C CG  . LEU B 275 ? 0.3291 0.2960 0.2278 0.1057  -0.1139 -0.0824 780  LEU B CG  
4132 C CD1 . LEU B 275 ? 0.3418 0.3036 0.2445 0.0978  -0.1339 -0.0908 780  LEU B CD1 
4133 C CD2 . LEU B 275 ? 0.3969 0.3848 0.2873 0.1062  -0.1009 -0.0654 780  LEU B CD2 
4134 N N   . GLN B 276 ? 0.4011 0.3413 0.2603 0.1503  -0.0894 -0.1218 781  GLN B N   
4135 C CA  . GLN B 276 ? 0.4364 0.3682 0.2755 0.1669  -0.0846 -0.1406 781  GLN B CA  
4136 C C   . GLN B 276 ? 0.4265 0.3790 0.2600 0.1773  -0.0627 -0.1328 781  GLN B C   
4137 O O   . GLN B 276 ? 0.4842 0.4441 0.2971 0.1859  -0.0539 -0.1393 781  GLN B O   
4138 C CB  . GLN B 276 ? 0.4534 0.3582 0.3113 0.1691  -0.0936 -0.1535 781  GLN B CB  
4139 C CG  . GLN B 276 ? 0.4903 0.3884 0.3351 0.1820  -0.0886 -0.1692 781  GLN B CG  
4140 C CD  . GLN B 276 ? 0.6042 0.5056 0.4677 0.1899  -0.0751 -0.1637 781  GLN B CD  
4141 O OE1 . GLN B 276 ? 0.6245 0.5073 0.5117 0.1881  -0.0810 -0.1639 781  GLN B OE1 
4142 N NE2 . GLN B 276 ? 0.5043 0.4307 0.3590 0.1970  -0.0570 -0.1568 781  GLN B NE2 
4143 N N   . PHE B 277 ? 0.3895 0.3554 0.2482 0.1707  -0.0533 -0.1135 782  PHE B N   
4144 C CA  . PHE B 277 ? 0.4445 0.4333 0.3020 0.1781  -0.0329 -0.1052 782  PHE B CA  
4145 C C   . PHE B 277 ? 0.4575 0.4641 0.2863 0.1786  -0.0232 -0.1000 782  PHE B C   
4146 O O   . PHE B 277 ? 0.4006 0.4176 0.2180 0.1831  -0.0118 -0.1007 782  PHE B O   
4147 C CB  . PHE B 277 ? 0.3374 0.3379 0.2267 0.1681  -0.0273 -0.0852 782  PHE B CB  
4148 C CG  . PHE B 277 ? 0.3511 0.3358 0.2678 0.1683  -0.0347 -0.0866 782  PHE B CG  
4149 C CD1 . PHE B 277 ? 0.4051 0.3691 0.3197 0.1804  -0.0407 -0.1049 782  PHE B CD1 
4150 C CD2 . PHE B 277 ? 0.3112 0.3006 0.2547 0.1565  -0.0356 -0.0694 782  PHE B CD2 
4151 C CE1 . PHE B 277 ? 0.3974 0.3443 0.3370 0.1806  -0.0477 -0.1042 782  PHE B CE1 
4152 C CE2 . PHE B 277 ? 0.3514 0.3255 0.3178 0.1567  -0.0426 -0.0686 782  PHE B CE2 
4153 C CZ  . PHE B 277 ? 0.3792 0.3311 0.3441 0.1691  -0.0488 -0.0853 782  PHE B CZ  
4154 N N   . VAL B 278 ? 0.3785 0.3891 0.2044 0.1671  -0.0288 -0.0880 783  VAL B N   
4155 C CA  . VAL B 278 ? 0.4182 0.4430 0.2198 0.1662  -0.0205 -0.0792 783  VAL B CA  
4156 C C   . VAL B 278 ? 0.4364 0.4533 0.2129 0.1709  -0.0270 -0.0913 783  VAL B C   
4157 O O   . VAL B 278 ? 0.4624 0.4896 0.2238 0.1718  -0.0159 -0.0857 783  VAL B O   
4158 C CB  . VAL B 278 ? 0.3947 0.4237 0.2020 0.1538  -0.0261 -0.0635 783  VAL B CB  
4159 C CG1 . VAL B 278 ? 0.3580 0.3708 0.1707 0.1474  -0.0483 -0.0708 783  VAL B CG1 
4160 C CG2 . VAL B 278 ? 0.3892 0.4296 0.1811 0.1505  -0.0167 -0.0504 783  VAL B CG2 
4161 N N   . GLY B 279 ? 0.4806 0.4783 0.2536 0.1728  -0.0450 -0.1082 784  GLY B N   
4162 C CA  . GLY B 279 ? 0.5031 0.4940 0.2532 0.1763  -0.0522 -0.1203 784  GLY B CA  
4163 C C   . GLY B 279 ? 0.5317 0.5248 0.2706 0.1859  -0.0400 -0.1294 784  GLY B C   
4164 O O   . GLY B 279 ? 0.5935 0.5874 0.3082 0.1887  -0.0396 -0.1349 784  GLY B O   
4165 N N   . ASP B 280 ? 0.4891 0.4841 0.2459 0.1909  -0.0299 -0.1309 785  ASP B N   
4166 C CA  . ASP B 280 ? 0.5156 0.5141 0.2663 0.1997  -0.0179 -0.1397 785  ASP B CA  
4167 C C   . ASP B 280 ? 0.4996 0.5216 0.2563 0.1988  0.0035  -0.1245 785  ASP B C   
4168 O O   . ASP B 280 ? 0.5598 0.5877 0.3210 0.2052  0.0151  -0.1300 785  ASP B O   
4169 C CB  . ASP B 280 ? 0.5236 0.5055 0.2932 0.2060  -0.0234 -0.1541 785  ASP B CB  
4170 C CG  . ASP B 280 ? 0.5426 0.4989 0.3101 0.2043  -0.0448 -0.1696 785  ASP B CG  
4171 O OD1 . ASP B 280 ? 0.5820 0.5350 0.3269 0.2018  -0.0537 -0.1752 785  ASP B OD1 
4172 O OD2 . ASP B 280 ? 0.5372 0.4763 0.3271 0.2041  -0.0531 -0.1751 785  ASP B OD2 
4173 N N   . GLY B 281 ? 0.4724 0.5072 0.2313 0.1899  0.0087  -0.1058 786  GLY B N   
4174 C CA  . GLY B 281 ? 0.5139 0.5690 0.2799 0.1856  0.0278  -0.0910 786  GLY B CA  
4175 C C   . GLY B 281 ? 0.4538 0.5189 0.2507 0.1849  0.0361  -0.0857 786  GLY B C   
4176 O O   . GLY B 281 ? 0.5009 0.5827 0.3061 0.1814  0.0515  -0.0770 786  GLY B O   
4177 N N   . GLU B 282 ? 0.4633 0.5180 0.2787 0.1873  0.0258  -0.0907 787  GLU B N   
4178 C CA  . GLU B 282 ? 0.4416 0.5054 0.2873 0.1869  0.0323  -0.0853 787  GLU B CA  
4179 C C   . GLU B 282 ? 0.4247 0.5045 0.2865 0.1747  0.0390  -0.0654 787  GLU B C   
4180 O O   . GLU B 282 ? 0.3998 0.4922 0.2857 0.1718  0.0464  -0.0587 787  GLU B O   
4181 C CB  . GLU B 282 ? 0.4455 0.4899 0.3070 0.1922  0.0185  -0.0955 787  GLU B CB  
4182 C CG  . GLU B 282 ? 0.4805 0.5014 0.3246 0.2002  0.0060  -0.1154 787  GLU B CG  
4183 C CD  . GLU B 282 ? 0.5610 0.5627 0.4257 0.2060  -0.0028 -0.1256 787  GLU B CD  
4184 O OE1 . GLU B 282 ? 0.6629 0.6527 0.5203 0.2145  -0.0043 -0.1413 787  GLU B OE1 
4185 O OE2 . GLU B 282 ? 0.5453 0.5428 0.4341 0.2014  -0.0081 -0.1170 787  GLU B OE2 
4186 N N   . MET B 283 ? 0.4163 0.4954 0.2664 0.1669  0.0358  -0.0560 788  MET B N   
4187 C CA  . MET B 283 ? 0.3662 0.4578 0.2321 0.1541  0.0418  -0.0377 788  MET B CA  
4188 C C   . MET B 283 ? 0.3890 0.4962 0.2580 0.1468  0.0571  -0.0283 788  MET B C   
4189 O O   . MET B 283 ? 0.2903 0.4083 0.1803 0.1366  0.0630  -0.0170 788  MET B O   
4190 C CB  . MET B 283 ? 0.3188 0.4034 0.1727 0.1481  0.0339  -0.0309 788  MET B CB  
4191 C CG  . MET B 283 ? 0.3064 0.3776 0.1637 0.1513  0.0192  -0.0378 788  MET B CG  
4192 S SD  . MET B 283 ? 0.3286 0.4069 0.2234 0.1441  0.0204  -0.0275 788  MET B SD  
4193 C CE  . MET B 283 ? 0.2805 0.3365 0.1850 0.1341  -0.0018 -0.0283 788  MET B CE  
4194 N N   . GLU B 284 ? 0.3447 0.4519 0.1929 0.1510  0.0630  -0.0338 789  GLU B N   
4195 C CA  . GLU B 284 ? 0.4565 0.5762 0.3055 0.1433  0.0777  -0.0258 789  GLU B CA  
4196 C C   . GLU B 284 ? 0.4471 0.5813 0.3221 0.1415  0.0869  -0.0255 789  GLU B C   
4197 O O   . GLU B 284 ? 0.4554 0.5996 0.3435 0.1299  0.0954  -0.0154 789  GLU B O   
4198 C CB  . GLU B 284 ? 0.3892 0.5064 0.2101 0.1497  0.0829  -0.0337 789  GLU B CB  
4199 N N   . GLU B 285 ? 0.4288 0.5628 0.3123 0.1528  0.0843  -0.0373 790  GLU B N   
4200 C CA  . GLU B 285 ? 0.3815 0.5299 0.2913 0.1525  0.0917  -0.0374 790  GLU B CA  
4201 C C   . GLU B 285 ? 0.3687 0.5220 0.3035 0.1420  0.0873  -0.0259 790  GLU B C   
4202 O O   . GLU B 285 ? 0.3858 0.5531 0.3394 0.1337  0.0948  -0.0198 790  GLU B O   
4203 C CB  . GLU B 285 ? 0.3733 0.5172 0.2876 0.1680  0.0885  -0.0528 790  GLU B CB  
4204 C CG  . GLU B 285 ? 0.4474 0.6044 0.3928 0.1694  0.0923  -0.0524 790  GLU B CG  
4205 C CD  . GLU B 285 ? 0.5815 0.7313 0.5325 0.1854  0.0893  -0.0676 790  GLU B CD  
4206 O OE1 . GLU B 285 ? 0.5538 0.7079 0.4963 0.1934  0.0986  -0.0778 790  GLU B OE1 
4207 O OE2 . GLU B 285 ? 0.6601 0.7984 0.6245 0.1897  0.0777  -0.0694 790  GLU B OE2 
4208 N N   . LEU B 286 ? 0.3594 0.5011 0.2946 0.1418  0.0751  -0.0237 791  LEU B N   
4209 C CA  . LEU B 286 ? 0.3970 0.5427 0.3531 0.1307  0.0712  -0.0124 791  LEU B CA  
4210 C C   . LEU B 286 ? 0.3618 0.5113 0.3168 0.1150  0.0763  -0.0002 791  LEU B C   
4211 O O   . LEU B 286 ? 0.3263 0.4827 0.3000 0.1038  0.0774  0.0073  791  LEU B O   
4212 C CB  . LEU B 286 ? 0.3123 0.4443 0.2682 0.1339  0.0582  -0.0133 791  LEU B CB  
4213 C CG  . LEU B 286 ? 0.3703 0.4913 0.3311 0.1480  0.0502  -0.0261 791  LEU B CG  
4214 C CD1 . LEU B 286 ? 0.3104 0.4166 0.2770 0.1474  0.0371  -0.0250 791  LEU B CD1 
4215 C CD2 . LEU B 286 ? 0.2502 0.3821 0.2346 0.1504  0.0543  -0.0270 791  LEU B CD2 
4216 N N   . GLU B 287 ? 0.3710 0.5140 0.3042 0.1140  0.0786  0.0010  792  GLU B N   
4217 C CA  . GLU B 287 ? 0.3162 0.4587 0.2489 0.0997  0.0833  0.0114  792  GLU B CA  
4218 C C   . GLU B 287 ? 0.3268 0.4812 0.2690 0.0930  0.0957  0.0119  792  GLU B C   
4219 O O   . GLU B 287 ? 0.3160 0.4729 0.2726 0.0799  0.0980  0.0181  792  GLU B O   
4220 C CB  . GLU B 287 ? 0.3108 0.4425 0.2175 0.1016  0.0822  0.0124  792  GLU B CB  
4221 C CG  . GLU B 287 ? 0.3263 0.4473 0.2315 0.0966  0.0725  0.0193  792  GLU B CG  
4222 C CD  . GLU B 287 ? 0.3160 0.4269 0.1951 0.1016  0.0690  0.0185  792  GLU B CD  
4223 O OE1 . GLU B 287 ? 0.3321 0.4366 0.1993 0.1118  0.0597  0.0112  792  GLU B OE1 
4224 O OE2 . GLU B 287 ? 0.4721 0.5804 0.3418 0.0953  0.0749  0.0243  792  GLU B OE2 
4225 N N   . THR B 288 ? 0.3673 0.5288 0.3014 0.1019  0.1041  0.0038  793  THR B N   
4226 C CA  . THR B 288 ? 0.3398 0.5149 0.2842 0.0962  0.1174  0.0034  793  THR B CA  
4227 C C   . THR B 288 ? 0.3819 0.5696 0.3552 0.0947  0.1170  0.0022  793  THR B C   
4228 O O   . THR B 288 ? 0.4382 0.6372 0.4255 0.0863  0.1260  0.0036  793  THR B O   
4229 C CB  . THR B 288 ? 0.3919 0.5722 0.3201 0.1065  0.1275  -0.0056 793  THR B CB  
4230 O OG1 . THR B 288 ? 0.4956 0.6895 0.4328 0.0992  0.1422  -0.0050 793  THR B OG1 
4231 C CG2 . THR B 288 ? 0.4048 0.5882 0.3378 0.1226  0.1238  -0.0173 793  THR B CG2 
4232 N N   . LEU B 289 ? 0.3969 0.5827 0.3794 0.1026  0.1065  -0.0004 794  LEU B N   
4233 C CA  . LEU B 289 ? 0.3344 0.5320 0.3434 0.1024  0.1047  -0.0010 794  LEU B CA  
4234 C C   . LEU B 289 ? 0.3805 0.5769 0.4030 0.0874  0.0994  0.0081  794  LEU B C   
4235 O O   . LEU B 289 ? 0.4146 0.6232 0.4575 0.0828  0.1013  0.0085  794  LEU B O   
4236 C CB  . LEU B 289 ? 0.3605 0.5539 0.3738 0.1167  0.0954  -0.0075 794  LEU B CB  
4237 C CG  . LEU B 289 ? 0.4410 0.6467 0.4731 0.1279  0.0984  -0.0156 794  LEU B CG  
4238 C CD1 . LEU B 289 ? 0.3908 0.6088 0.4200 0.1313  0.1130  -0.0218 794  LEU B CD1 
4239 C CD2 . LEU B 289 ? 0.4286 0.6218 0.4584 0.1433  0.0890  -0.0240 794  LEU B CD2 
4240 N N   . TRP B 290 ? 0.3294 0.5113 0.3408 0.0802  0.0927  0.0144  795  TRP B N   
4241 C CA  . TRP B 290 ? 0.3179 0.4959 0.3408 0.0678  0.0860  0.0209  795  TRP B CA  
4242 C C   . TRP B 290 ? 0.2424 0.4100 0.2566 0.0553  0.0876  0.0265  795  TRP B C   
4243 O O   . TRP B 290 ? 0.1924 0.3622 0.2162 0.0460  0.0861  0.0314  795  TRP B O   
4244 C CB  . TRP B 290 ? 0.2361 0.4064 0.2597 0.0723  0.0740  0.0228  795  TRP B CB  
4245 C CG  . TRP B 290 ? 0.2651 0.4429 0.2996 0.0846  0.0709  0.0177  795  TRP B CG  
4246 C CD1 . TRP B 290 ? 0.2744 0.4472 0.3012 0.0994  0.0682  0.0109  795  TRP B CD1 
4247 C CD2 . TRP B 290 ? 0.2619 0.4511 0.3176 0.0839  0.0691  0.0177  795  TRP B CD2 
4248 N NE1 . TRP B 290 ? 0.2249 0.4031 0.2686 0.1078  0.0647  0.0067  795  TRP B NE1 
4249 C CE2 . TRP B 290 ? 0.2672 0.4571 0.3289 0.0988  0.0652  0.0117  795  TRP B CE2 
4250 C CE3 . TRP B 290 ? 0.2269 0.4247 0.2969 0.0728  0.0697  0.0212  795  TRP B CE3 
4251 C CZ2 . TRP B 290 ? 0.3147 0.5140 0.3975 0.1028  0.0617  0.0107  795  TRP B CZ2 
4252 C CZ3 . TRP B 290 ? 0.3100 0.5197 0.3993 0.0769  0.0664  0.0200  795  TRP B CZ3 
4253 C CH2 . TRP B 290 ? 0.3133 0.5241 0.4094 0.0919  0.0623  0.0155  795  TRP B CH2 
4254 N N   . LEU B 291 ? 0.2529 0.4113 0.2481 0.0571  0.0903  0.0268  796  LEU B N   
4255 C CA  . LEU B 291 ? 0.2649 0.4125 0.2512 0.0493  0.0890  0.0338  796  LEU B CA  
4256 C C   . LEU B 291 ? 0.3273 0.4779 0.3057 0.0445  0.1006  0.0365  796  LEU B C   
4257 O O   . LEU B 291 ? 0.3407 0.4822 0.3130 0.0380  0.1004  0.0424  796  LEU B O   
4258 C CB  . LEU B 291 ? 0.2853 0.4191 0.2560 0.0544  0.0818  0.0338  796  LEU B CB  
4259 C CG  . LEU B 291 ? 0.2959 0.4285 0.2727 0.0602  0.0711  0.0338  796  LEU B CG  
4260 C CD1 . LEU B 291 ? 0.2364 0.3591 0.1980 0.0662  0.0649  0.0353  796  LEU B CD1 
4261 C CD2 . LEU B 291 ? 0.2256 0.3560 0.2193 0.0492  0.0657  0.0368  796  LEU B CD2 
4262 N N   . THR B 292 ? 0.3144 0.4775 0.2932 0.0476  0.1113  0.0324  797  THR B N   
4263 C CA  . THR B 292 ? 0.3948 0.5609 0.3644 0.0424  0.1238  0.0353  797  THR B CA  
4264 C C   . THR B 292 ? 0.3439 0.5132 0.3269 0.0298  0.1275  0.0402  797  THR B C   
4265 O O   . THR B 292 ? 0.4184 0.5939 0.4203 0.0262  0.1231  0.0393  797  THR B O   
4266 C CB  . THR B 292 ? 0.3599 0.5406 0.3286 0.0483  0.1358  0.0287  797  THR B CB  
4267 O OG1 . THR B 292 ? 0.3723 0.5687 0.3651 0.0488  0.1369  0.0247  797  THR B OG1 
4268 C CG2 . THR B 292 ? 0.4117 0.5871 0.3634 0.0607  0.1333  0.0221  797  THR B CG2 
4269 N N   . GLY B 293 ? 0.3725 0.5368 0.3441 0.0230  0.1357  0.0452  798  GLY B N   
4270 C CA  . GLY B 293 ? 0.3931 0.5592 0.3752 0.0102  0.1414  0.0488  798  GLY B CA  
4271 C C   . GLY B 293 ? 0.4618 0.6314 0.4326 0.0045  0.1569  0.0517  798  GLY B C   
4272 O O   . GLY B 293 ? 0.4694 0.6325 0.4186 0.0088  0.1601  0.0543  798  GLY B O   
4273 N N   . ILE B 294 ? 0.4145 0.5952 0.4000 -0.0059 0.1668  0.0511  799  ILE B N   
4274 C CA  . ILE B 294 ? 0.4210 0.6072 0.3978 -0.0135 0.1833  0.0539  799  ILE B CA  
4275 C C   . ILE B 294 ? 0.4111 0.5799 0.3695 -0.0206 0.1836  0.0627  799  ILE B C   
4276 O O   . ILE B 294 ? 0.5158 0.6818 0.4538 -0.0209 0.1923  0.0676  799  ILE B O   
4277 C CB  . ILE B 294 ? 0.4803 0.6838 0.4805 -0.0236 0.1941  0.0504  799  ILE B CB  
4278 C CG1 . ILE B 294 ? 0.5400 0.7619 0.5596 -0.0144 0.1932  0.0426  799  ILE B CG1 
4279 C CG2 . ILE B 294 ? 0.4433 0.6534 0.4353 -0.0334 0.2125  0.0534  799  ILE B CG2 
4280 C CD1 . ILE B 294 ? 0.3982 0.6419 0.4384 -0.0205 0.2085  0.0388  799  ILE B CD1 
4281 N N   . CYS B 295 ? 0.4807 0.6378 0.4453 -0.0261 0.1742  0.0652  800  CYS B N   
4282 C CA  . CYS B 295 ? 0.5015 0.6416 0.4509 -0.0314 0.1730  0.0739  800  CYS B CA  
4283 C C   . CYS B 295 ? 0.5054 0.6321 0.4342 -0.0192 0.1649  0.0777  800  CYS B C   
4284 O O   . CYS B 295 ? 0.7123 0.8334 0.6202 -0.0184 0.1710  0.0842  800  CYS B O   
4285 C CB  . CYS B 295 ? 0.4704 0.6022 0.4328 -0.0389 0.1649  0.0739  800  CYS B CB  
4286 S SG  . CYS B 295 ? 0.4057 0.5530 0.3927 -0.0532 0.1724  0.0674  800  CYS B SG  
4287 N N   . GLY C .   ? 0.1543 0.3574 0.1927 0.0586  0.0669  -0.0091 1001 GLY A N   
4288 C CA  . GLY C .   ? 0.1665 0.3683 0.1955 0.0680  0.0680  -0.0127 1001 GLY A CA  
4289 C C   . GLY C .   ? 0.1905 0.3536 0.2008 0.0752  0.0794  -0.0242 1001 GLY A C   
4290 O O   . GLY C .   ? 0.2091 0.3681 0.2050 0.0866  0.0803  -0.0277 1001 GLY A O   
4291 O OXT . GLY C .   ? 0.1964 0.3298 0.2023 0.0689  0.0882  -0.0309 1001 GLY A OXT 
4292 N N   . GLU D .   ? 0.1401 0.2164 0.1751 0.0078  0.0088  0.0525  1001 GLU B N   
4293 C CA  . GLU D .   ? 0.1527 0.2255 0.1890 0.0038  0.0076  0.0513  1001 GLU B CA  
4294 C C   . GLU D .   ? 0.1576 0.2293 0.1959 0.0027  0.0028  0.0524  1001 GLU B C   
4295 O O   . GLU D .   ? 0.1757 0.2447 0.2133 0.0031  0.0017  0.0513  1001 GLU B O   
4296 C CB  . GLU D .   ? 0.1107 0.1852 0.1459 -0.0006 0.0097  0.0495  1001 GLU B CB  
4297 C CG  . GLU D .   ? 0.1521 0.2247 0.1861 -0.0024 0.0160  0.0478  1001 GLU B CG  
4298 C CD  . GLU D .   ? 0.1410 0.2068 0.1752 -0.0028 0.0187  0.0470  1001 GLU B CD  
4299 O OE1 . GLU D .   ? 0.1755 0.2387 0.2109 -0.0044 0.0170  0.0458  1001 GLU B OE1 
4300 O OE2 . GLU D .   ? 0.1561 0.2192 0.1889 -0.0013 0.0232  0.0480  1001 GLU B OE2 
4301 O OXT . GLU D .   ? 0.1468 0.2164 0.1855 -0.0004 0.0024  0.0513  1001 GLU B OXT 
# 
