data_8ZUC
# 
_entry.id   8ZUC 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   8ZUC         pdb_00008zuc 10.2210/pdb8zuc/pdb 
WWPDB D_1300048555 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-11 
_pdbx_audit_revision_history.part_number         ? 
# 
_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_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZUC 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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              948805786@qq.com 
_pdbx_contact_author.name_first         Ming 
_pdbx_contact_author.name_last          Yan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6340-6759 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yan, M.'   1 ? 
'Zhang, H.' 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            Bioorg.Chem. 
_citation.journal_id_ASTM           BOCMBM 
_citation.journal_id_CSD            0368 
_citation.journal_id_ISSN           0045-2068 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            154 
_citation.language                  ? 
_citation.page_first                107988 
_citation.page_last                 107988 
_citation.title                     
;Development of pyrimidone derivatives as nonpeptidic and noncovalent 3-chymotrypsin-like protease (3CL pro ) inhibitors with anti-coronavirus activities.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bioorg.2024.107988 
_citation.pdbx_database_id_PubMed   39591689 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Pan, F.'   1  ? 
primary 'Zhou, Q.'  2  ? 
primary 'Yan, M.'   3  ? 
primary 'Yang, S.'  4  ? 
primary 'Hu, R.'    5  ? 
primary 'Chen, Y.'  6  ? 
primary 'Wen, Y.'   7  ? 
primary 'Chao, Y.'  8  ? 
primary 'Xie, C.'   9  ? 
primary 'Ou, W.'    10 ? 
primary 'Li, Y.'    11 ? 
primary 'Zhang, H.' 12 ? 
primary 'Guo, D.'   13 ? 
primary 'Zhang, X.' 14 ? 
# 
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 '3C-like proteinase' 33292.965 1   3.4.22.69 ? ? ? 
2 polymer     man '3C-like proteinase' 33192.820 1   3.4.22.69 ? ? ? 
3 non-polymer syn 
;6-[[6-chloranyl-2-(3-methylbutyl)indazol-5-yl]amino]-3-[(1-methyl-1,2,4-triazol-3-yl)methyl]-1-[[2,4,5-tris(fluoranyl)phenyl]methyl]pyrimidine-2,4-dione
;
586.996   2   ?         ? ? ? 
4 water       nat water 18.015    505 ?         ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
2 '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
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 
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCS
;
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCS
;
A ? 
2 'polypeptide(L)' no no 
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGGTILGSALLEDEFTPFDVVRQCS
;
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGGTILGSALLEDEFTPFDVVRQCS
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 
;6-[[6-chloranyl-2-(3-methylbutyl)indazol-5-yl]amino]-3-[(1-methyl-1,2,4-triazol-3-yl)methyl]-1-[[2,4,5-tris(fluoranyl)phenyl]methyl]pyrimidine-2,4-dione
;
A1D81 
4 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
2 1   SER n 
2 2   GLY n 
2 3   PHE n 
2 4   ARG n 
2 5   LYS n 
2 6   MET n 
2 7   ALA n 
2 8   PHE n 
2 9   PRO n 
2 10  SER n 
2 11  GLY n 
2 12  LYS n 
2 13  VAL n 
2 14  GLU n 
2 15  GLY n 
2 16  CYS n 
2 17  MET n 
2 18  VAL n 
2 19  GLN n 
2 20  VAL n 
2 21  THR n 
2 22  CYS n 
2 23  GLY n 
2 24  THR n 
2 25  THR n 
2 26  THR n 
2 27  LEU n 
2 28  ASN n 
2 29  GLY n 
2 30  LEU n 
2 31  TRP n 
2 32  LEU n 
2 33  ASP n 
2 34  ASP n 
2 35  VAL n 
2 36  VAL n 
2 37  TYR n 
2 38  CYS n 
2 39  PRO n 
2 40  ARG n 
2 41  HIS n 
2 42  VAL n 
2 43  ILE n 
2 44  CYS n 
2 45  THR n 
2 46  SER n 
2 47  GLU n 
2 48  ASP n 
2 49  MET n 
2 50  LEU n 
2 51  ASN n 
2 52  PRO n 
2 53  ASN n 
2 54  TYR n 
2 55  GLU n 
2 56  ASP n 
2 57  LEU n 
2 58  LEU n 
2 59  ILE n 
2 60  ARG n 
2 61  LYS n 
2 62  SER n 
2 63  ASN n 
2 64  HIS n 
2 65  ASN n 
2 66  PHE n 
2 67  LEU n 
2 68  VAL n 
2 69  GLN n 
2 70  ALA n 
2 71  GLY n 
2 72  ASN n 
2 73  VAL n 
2 74  GLN n 
2 75  LEU n 
2 76  ARG n 
2 77  VAL n 
2 78  ILE n 
2 79  GLY n 
2 80  HIS n 
2 81  SER n 
2 82  MET n 
2 83  GLN n 
2 84  ASN n 
2 85  CYS n 
2 86  VAL n 
2 87  LEU n 
2 88  LYS n 
2 89  LEU n 
2 90  LYS n 
2 91  VAL n 
2 92  ASP n 
2 93  THR n 
2 94  ALA n 
2 95  ASN n 
2 96  PRO n 
2 97  LYS n 
2 98  THR n 
2 99  PRO n 
2 100 LYS n 
2 101 TYR n 
2 102 LYS n 
2 103 PHE n 
2 104 VAL n 
2 105 ARG n 
2 106 ILE n 
2 107 GLN n 
2 108 PRO n 
2 109 GLY n 
2 110 GLN n 
2 111 THR n 
2 112 PHE n 
2 113 SER n 
2 114 VAL n 
2 115 LEU n 
2 116 ALA n 
2 117 CYS n 
2 118 TYR n 
2 119 ASN n 
2 120 GLY n 
2 121 SER n 
2 122 PRO n 
2 123 SER n 
2 124 GLY n 
2 125 VAL n 
2 126 TYR n 
2 127 GLN n 
2 128 CYS n 
2 129 ALA n 
2 130 MET n 
2 131 ARG n 
2 132 PRO n 
2 133 ASN n 
2 134 PHE n 
2 135 THR n 
2 136 ILE n 
2 137 LYS n 
2 138 GLY n 
2 139 SER n 
2 140 PHE n 
2 141 LEU n 
2 142 ASN n 
2 143 GLY n 
2 144 SER n 
2 145 CYS n 
2 146 GLY n 
2 147 SER n 
2 148 VAL n 
2 149 GLY n 
2 150 PHE n 
2 151 ASN n 
2 152 ILE n 
2 153 ASP n 
2 154 TYR n 
2 155 ASP n 
2 156 CYS n 
2 157 VAL n 
2 158 SER n 
2 159 PHE n 
2 160 CYS n 
2 161 TYR n 
2 162 MET n 
2 163 HIS n 
2 164 HIS n 
2 165 MET n 
2 166 GLU n 
2 167 LEU n 
2 168 PRO n 
2 169 THR n 
2 170 GLY n 
2 171 VAL n 
2 172 HIS n 
2 173 ALA n 
2 174 GLY n 
2 175 THR n 
2 176 ASP n 
2 177 LEU n 
2 178 GLU n 
2 179 GLY n 
2 180 ASN n 
2 181 PHE n 
2 182 TYR n 
2 183 GLY n 
2 184 PRO n 
2 185 PHE n 
2 186 VAL n 
2 187 ASP n 
2 188 ARG n 
2 189 GLN n 
2 190 THR n 
2 191 ALA n 
2 192 GLN n 
2 193 ALA n 
2 194 ALA n 
2 195 GLY n 
2 196 THR n 
2 197 ASP n 
2 198 THR n 
2 199 THR n 
2 200 ILE n 
2 201 THR n 
2 202 VAL n 
2 203 ASN n 
2 204 VAL n 
2 205 LEU n 
2 206 ALA n 
2 207 TRP n 
2 208 LEU n 
2 209 TYR n 
2 210 ALA n 
2 211 ALA n 
2 212 VAL n 
2 213 ILE n 
2 214 ASN n 
2 215 GLY n 
2 216 ASP n 
2 217 ARG n 
2 218 TRP n 
2 219 PHE n 
2 220 LEU n 
2 221 ASN n 
2 222 ARG n 
2 223 PHE n 
2 224 THR n 
2 225 THR n 
2 226 THR n 
2 227 LEU n 
2 228 ASN n 
2 229 ASP n 
2 230 PHE n 
2 231 ASN n 
2 232 LEU n 
2 233 VAL n 
2 234 ALA n 
2 235 MET n 
2 236 LYS n 
2 237 TYR n 
2 238 ASN n 
2 239 TYR n 
2 240 GLU n 
2 241 PRO n 
2 242 LEU n 
2 243 THR n 
2 244 GLN n 
2 245 ASP n 
2 246 HIS n 
2 247 VAL n 
2 248 ASP n 
2 249 ILE n 
2 250 LEU n 
2 251 GLY n 
2 252 PRO n 
2 253 LEU n 
2 254 SER n 
2 255 ALA n 
2 256 GLN n 
2 257 THR n 
2 258 GLY n 
2 259 ILE n 
2 260 ALA n 
2 261 VAL n 
2 262 LEU n 
2 263 ASP n 
2 264 MET n 
2 265 CYS n 
2 266 ALA n 
2 267 SER n 
2 268 LEU n 
2 269 LYS n 
2 270 GLU n 
2 271 LEU n 
2 272 LEU n 
2 273 GLN n 
2 274 ASN n 
2 275 GLY n 
2 276 MET n 
2 277 ASN n 
2 278 GLY n 
2 279 GLY n 
2 280 THR n 
2 281 ILE n 
2 282 LEU n 
2 283 GLY n 
2 284 SER n 
2 285 ALA n 
2 286 LEU n 
2 287 LEU n 
2 288 GLU n 
2 289 ASP n 
2 290 GLU n 
2 291 PHE n 
2 292 THR n 
2 293 PRO n 
2 294 PHE n 
2 295 ASP n 
2 296 VAL n 
2 297 VAL n 
2 298 ARG n 
2 299 GLN n 
2 300 CYS n 
2 301 SER 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' 1 301 '2019-nCoV, SARS-CoV-2' ? 'rep, 1a-1b' ? ? ? ? ? ? 
'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 301 '2019-nCoV, SARS-CoV-2' ? 'rep, 1a-1b' ? ? ? ? ? ? 
'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1D81 non-polymer         . 
;6-[[6-chloranyl-2-(3-methylbutyl)indazol-5-yl]amino]-3-[(1-methyl-1,2,4-triazol-3-yl)methyl]-1-[[2,4,5-tris(fluoranyl)phenyl]methyl]pyrimidine-2,4-dione
;
? 'C27 H26 Cl F3 N8 O2' 586.996 
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   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
B 2 1   SER 1   1   1   SER SER B . n 
B 2 2   GLY 2   2   2   GLY GLY B . n 
B 2 3   PHE 3   3   3   PHE PHE B . n 
B 2 4   ARG 4   4   4   ARG ARG B . n 
B 2 5   LYS 5   5   5   LYS LYS B . n 
B 2 6   MET 6   6   6   MET MET B . n 
B 2 7   ALA 7   7   7   ALA ALA B . n 
B 2 8   PHE 8   8   8   PHE PHE B . n 
B 2 9   PRO 9   9   9   PRO PRO B . n 
B 2 10  SER 10  10  10  SER SER B . n 
B 2 11  GLY 11  11  11  GLY GLY B . n 
B 2 12  LYS 12  12  12  LYS LYS B . n 
B 2 13  VAL 13  13  13  VAL VAL B . n 
B 2 14  GLU 14  14  14  GLU GLU B . n 
B 2 15  GLY 15  15  15  GLY GLY B . n 
B 2 16  CYS 16  16  16  CYS CYS B . n 
B 2 17  MET 17  17  17  MET MET B . n 
B 2 18  VAL 18  18  18  VAL VAL B . n 
B 2 19  GLN 19  19  19  GLN GLN B . n 
B 2 20  VAL 20  20  20  VAL VAL B . n 
B 2 21  THR 21  21  21  THR THR B . n 
B 2 22  CYS 22  22  22  CYS CYS B . n 
B 2 23  GLY 23  23  23  GLY GLY B . n 
B 2 24  THR 24  24  24  THR THR B . n 
B 2 25  THR 25  25  25  THR THR B . n 
B 2 26  THR 26  26  26  THR THR B . n 
B 2 27  LEU 27  27  27  LEU LEU B . n 
B 2 28  ASN 28  28  28  ASN ASN B . n 
B 2 29  GLY 29  29  29  GLY GLY B . n 
B 2 30  LEU 30  30  30  LEU LEU B . n 
B 2 31  TRP 31  31  31  TRP TRP B . n 
B 2 32  LEU 32  32  32  LEU LEU B . n 
B 2 33  ASP 33  33  33  ASP ASP B . n 
B 2 34  ASP 34  34  34  ASP ASP B . n 
B 2 35  VAL 35  35  35  VAL VAL B . n 
B 2 36  VAL 36  36  36  VAL VAL B . n 
B 2 37  TYR 37  37  37  TYR TYR B . n 
B 2 38  CYS 38  38  38  CYS CYS B . n 
B 2 39  PRO 39  39  39  PRO PRO B . n 
B 2 40  ARG 40  40  40  ARG ARG B . n 
B 2 41  HIS 41  41  41  HIS HIS B . n 
B 2 42  VAL 42  42  42  VAL VAL B . n 
B 2 43  ILE 43  43  43  ILE ILE B . n 
B 2 44  CYS 44  44  44  CYS CYS B . n 
B 2 45  THR 45  45  45  THR THR B . n 
B 2 46  SER 46  46  46  SER SER B . n 
B 2 47  GLU 47  47  47  GLU GLU B . n 
B 2 48  ASP 48  48  48  ASP ASP B . n 
B 2 49  MET 49  49  49  MET MET B . n 
B 2 50  LEU 50  50  50  LEU LEU B . n 
B 2 51  ASN 51  51  51  ASN ASN B . n 
B 2 52  PRO 52  52  52  PRO PRO B . n 
B 2 53  ASN 53  53  53  ASN ASN B . n 
B 2 54  TYR 54  54  54  TYR TYR B . n 
B 2 55  GLU 55  55  55  GLU GLU B . n 
B 2 56  ASP 56  56  56  ASP ASP B . n 
B 2 57  LEU 57  57  57  LEU LEU B . n 
B 2 58  LEU 58  58  58  LEU LEU B . n 
B 2 59  ILE 59  59  59  ILE ILE B . n 
B 2 60  ARG 60  60  60  ARG ARG B . n 
B 2 61  LYS 61  61  61  LYS LYS B . n 
B 2 62  SER 62  62  62  SER SER B . n 
B 2 63  ASN 63  63  63  ASN ASN B . n 
B 2 64  HIS 64  64  64  HIS HIS B . n 
B 2 65  ASN 65  65  65  ASN ASN B . n 
B 2 66  PHE 66  66  66  PHE PHE B . n 
B 2 67  LEU 67  67  67  LEU LEU B . n 
B 2 68  VAL 68  68  68  VAL VAL B . n 
B 2 69  GLN 69  69  69  GLN GLN B . n 
B 2 70  ALA 70  70  70  ALA ALA B . n 
B 2 71  GLY 71  71  71  GLY GLY B . n 
B 2 72  ASN 72  72  72  ASN ASN B . n 
B 2 73  VAL 73  73  73  VAL VAL B . n 
B 2 74  GLN 74  74  74  GLN GLN B . n 
B 2 75  LEU 75  75  75  LEU LEU B . n 
B 2 76  ARG 76  76  76  ARG ARG B . n 
B 2 77  VAL 77  77  77  VAL VAL B . n 
B 2 78  ILE 78  78  78  ILE ILE B . n 
B 2 79  GLY 79  79  79  GLY GLY B . n 
B 2 80  HIS 80  80  80  HIS HIS B . n 
B 2 81  SER 81  81  81  SER SER B . n 
B 2 82  MET 82  82  82  MET MET B . n 
B 2 83  GLN 83  83  83  GLN GLN B . n 
B 2 84  ASN 84  84  84  ASN ASN B . n 
B 2 85  CYS 85  85  85  CYS CYS B . n 
B 2 86  VAL 86  86  86  VAL VAL B . n 
B 2 87  LEU 87  87  87  LEU LEU B . n 
B 2 88  LYS 88  88  88  LYS LYS B . n 
B 2 89  LEU 89  89  89  LEU LEU B . n 
B 2 90  LYS 90  90  90  LYS LYS B . n 
B 2 91  VAL 91  91  91  VAL VAL B . n 
B 2 92  ASP 92  92  92  ASP ASP B . n 
B 2 93  THR 93  93  93  THR THR B . n 
B 2 94  ALA 94  94  94  ALA ALA B . n 
B 2 95  ASN 95  95  95  ASN ASN B . n 
B 2 96  PRO 96  96  96  PRO PRO B . n 
B 2 97  LYS 97  97  97  LYS LYS B . n 
B 2 98  THR 98  98  98  THR THR B . n 
B 2 99  PRO 99  99  99  PRO PRO B . n 
B 2 100 LYS 100 100 100 LYS LYS B . n 
B 2 101 TYR 101 101 101 TYR TYR B . n 
B 2 102 LYS 102 102 102 LYS LYS B . n 
B 2 103 PHE 103 103 103 PHE PHE B . n 
B 2 104 VAL 104 104 104 VAL VAL B . n 
B 2 105 ARG 105 105 105 ARG ARG B . n 
B 2 106 ILE 106 106 106 ILE ILE B . n 
B 2 107 GLN 107 107 107 GLN GLN B . n 
B 2 108 PRO 108 108 108 PRO PRO B . n 
B 2 109 GLY 109 109 109 GLY GLY B . n 
B 2 110 GLN 110 110 110 GLN GLN B . n 
B 2 111 THR 111 111 111 THR THR B . n 
B 2 112 PHE 112 112 112 PHE PHE B . n 
B 2 113 SER 113 113 113 SER SER B . n 
B 2 114 VAL 114 114 114 VAL VAL B . n 
B 2 115 LEU 115 115 115 LEU LEU B . n 
B 2 116 ALA 116 116 116 ALA ALA B . n 
B 2 117 CYS 117 117 117 CYS CYS B . n 
B 2 118 TYR 118 118 118 TYR TYR B . n 
B 2 119 ASN 119 119 119 ASN ASN B . n 
B 2 120 GLY 120 120 120 GLY GLY B . n 
B 2 121 SER 121 121 121 SER SER B . n 
B 2 122 PRO 122 122 122 PRO PRO B . n 
B 2 123 SER 123 123 123 SER SER B . n 
B 2 124 GLY 124 124 124 GLY GLY B . n 
B 2 125 VAL 125 125 125 VAL VAL B . n 
B 2 126 TYR 126 126 126 TYR TYR B . n 
B 2 127 GLN 127 127 127 GLN GLN B . n 
B 2 128 CYS 128 128 128 CYS CYS B . n 
B 2 129 ALA 129 129 129 ALA ALA B . n 
B 2 130 MET 130 130 130 MET MET B . n 
B 2 131 ARG 131 131 131 ARG ARG B . n 
B 2 132 PRO 132 132 132 PRO PRO B . n 
B 2 133 ASN 133 133 133 ASN ASN B . n 
B 2 134 PHE 134 134 134 PHE PHE B . n 
B 2 135 THR 135 135 135 THR THR B . n 
B 2 136 ILE 136 136 136 ILE ILE B . n 
B 2 137 LYS 137 137 137 LYS LYS B . n 
B 2 138 GLY 138 138 138 GLY GLY B . n 
B 2 139 SER 139 139 139 SER SER B . n 
B 2 140 PHE 140 140 140 PHE PHE B . n 
B 2 141 LEU 141 141 141 LEU LEU B . n 
B 2 142 ASN 142 142 142 ASN ASN B . n 
B 2 143 GLY 143 143 143 GLY GLY B . n 
B 2 144 SER 144 144 144 SER SER B . n 
B 2 145 CYS 145 145 145 CYS CYS B . n 
B 2 146 GLY 146 146 146 GLY GLY B . n 
B 2 147 SER 147 147 147 SER SER B . n 
B 2 148 VAL 148 148 148 VAL VAL B . n 
B 2 149 GLY 149 149 149 GLY GLY B . n 
B 2 150 PHE 150 150 150 PHE PHE B . n 
B 2 151 ASN 151 151 151 ASN ASN B . n 
B 2 152 ILE 152 152 152 ILE ILE B . n 
B 2 153 ASP 153 153 153 ASP ASP B . n 
B 2 154 TYR 154 154 154 TYR TYR B . n 
B 2 155 ASP 155 155 155 ASP ASP B . n 
B 2 156 CYS 156 156 156 CYS CYS B . n 
B 2 157 VAL 157 157 157 VAL VAL B . n 
B 2 158 SER 158 158 158 SER SER B . n 
B 2 159 PHE 159 159 159 PHE PHE B . n 
B 2 160 CYS 160 160 160 CYS CYS B . n 
B 2 161 TYR 161 161 161 TYR TYR B . n 
B 2 162 MET 162 162 162 MET MET B . n 
B 2 163 HIS 163 163 163 HIS HIS B . n 
B 2 164 HIS 164 164 164 HIS HIS B . n 
B 2 165 MET 165 165 165 MET MET B . n 
B 2 166 GLU 166 166 166 GLU GLU B . n 
B 2 167 LEU 167 167 167 LEU LEU B . n 
B 2 168 PRO 168 168 168 PRO PRO B . n 
B 2 169 THR 169 169 169 THR THR B . n 
B 2 170 GLY 170 170 170 GLY GLY B . n 
B 2 171 VAL 171 171 171 VAL VAL B . n 
B 2 172 HIS 172 172 172 HIS HIS B . n 
B 2 173 ALA 173 173 173 ALA ALA B . n 
B 2 174 GLY 174 174 174 GLY GLY B . n 
B 2 175 THR 175 175 175 THR THR B . n 
B 2 176 ASP 176 176 176 ASP ASP B . n 
B 2 177 LEU 177 177 177 LEU LEU B . n 
B 2 178 GLU 178 178 178 GLU GLU B . n 
B 2 179 GLY 179 179 179 GLY GLY B . n 
B 2 180 ASN 180 180 180 ASN ASN B . n 
B 2 181 PHE 181 181 181 PHE PHE B . n 
B 2 182 TYR 182 182 182 TYR TYR B . n 
B 2 183 GLY 183 183 183 GLY GLY B . n 
B 2 184 PRO 184 184 184 PRO PRO B . n 
B 2 185 PHE 185 185 185 PHE PHE B . n 
B 2 186 VAL 186 186 186 VAL VAL B . n 
B 2 187 ASP 187 187 187 ASP ASP B . n 
B 2 188 ARG 188 188 188 ARG ARG B . n 
B 2 189 GLN 189 189 189 GLN GLN B . n 
B 2 190 THR 190 190 190 THR THR B . n 
B 2 191 ALA 191 191 191 ALA ALA B . n 
B 2 192 GLN 192 192 192 GLN GLN B . n 
B 2 193 ALA 193 193 193 ALA ALA B . n 
B 2 194 ALA 194 194 194 ALA ALA B . n 
B 2 195 GLY 195 195 195 GLY GLY B . n 
B 2 196 THR 196 196 196 THR THR B . n 
B 2 197 ASP 197 197 197 ASP ASP B . n 
B 2 198 THR 198 198 198 THR THR B . n 
B 2 199 THR 199 199 199 THR THR B . n 
B 2 200 ILE 200 200 200 ILE ILE B . n 
B 2 201 THR 201 201 201 THR THR B . n 
B 2 202 VAL 202 202 202 VAL VAL B . n 
B 2 203 ASN 203 203 203 ASN ASN B . n 
B 2 204 VAL 204 204 204 VAL VAL B . n 
B 2 205 LEU 205 205 205 LEU LEU B . n 
B 2 206 ALA 206 206 206 ALA ALA B . n 
B 2 207 TRP 207 207 207 TRP TRP B . n 
B 2 208 LEU 208 208 208 LEU LEU B . n 
B 2 209 TYR 209 209 209 TYR TYR B . n 
B 2 210 ALA 210 210 210 ALA ALA B . n 
B 2 211 ALA 211 211 211 ALA ALA B . n 
B 2 212 VAL 212 212 212 VAL VAL B . n 
B 2 213 ILE 213 213 213 ILE ILE B . n 
B 2 214 ASN 214 214 214 ASN ASN B . n 
B 2 215 GLY 215 215 215 GLY GLY B . n 
B 2 216 ASP 216 216 216 ASP ASP B . n 
B 2 217 ARG 217 217 217 ARG ARG B . n 
B 2 218 TRP 218 218 218 TRP TRP B . n 
B 2 219 PHE 219 219 219 PHE PHE B . n 
B 2 220 LEU 220 220 220 LEU LEU B . n 
B 2 221 ASN 221 221 221 ASN ASN B . n 
B 2 222 ARG 222 222 222 ARG ARG B . n 
B 2 223 PHE 223 223 223 PHE PHE B . n 
B 2 224 THR 224 224 224 THR THR B . n 
B 2 225 THR 225 225 225 THR THR B . n 
B 2 226 THR 226 226 226 THR THR B . n 
B 2 227 LEU 227 227 227 LEU LEU B . n 
B 2 228 ASN 228 228 228 ASN ASN B . n 
B 2 229 ASP 229 229 229 ASP ASP B . n 
B 2 230 PHE 230 230 230 PHE PHE B . n 
B 2 231 ASN 231 231 231 ASN ASN B . n 
B 2 232 LEU 232 232 232 LEU LEU B . n 
B 2 233 VAL 233 233 233 VAL VAL B . n 
B 2 234 ALA 234 234 234 ALA ALA B . n 
B 2 235 MET 235 235 235 MET MET B . n 
B 2 236 LYS 236 236 236 LYS LYS B . n 
B 2 237 TYR 237 237 237 TYR TYR B . n 
B 2 238 ASN 238 238 238 ASN ASN B . n 
B 2 239 TYR 239 239 239 TYR TYR B . n 
B 2 240 GLU 240 240 240 GLU GLU B . n 
B 2 241 PRO 241 241 241 PRO PRO B . n 
B 2 242 LEU 242 242 242 LEU LEU B . n 
B 2 243 THR 243 243 243 THR THR B . n 
B 2 244 GLN 244 244 244 GLN GLN B . n 
B 2 245 ASP 245 245 245 ASP ASP B . n 
B 2 246 HIS 246 246 246 HIS HIS B . n 
B 2 247 VAL 247 247 247 VAL VAL B . n 
B 2 248 ASP 248 248 248 ASP ASP B . n 
B 2 249 ILE 249 249 249 ILE ILE B . n 
B 2 250 LEU 250 250 250 LEU LEU B . n 
B 2 251 GLY 251 251 251 GLY GLY B . n 
B 2 252 PRO 252 252 252 PRO PRO B . n 
B 2 253 LEU 253 253 253 LEU LEU B . n 
B 2 254 SER 254 254 254 SER SER B . n 
B 2 255 ALA 255 255 255 ALA ALA B . n 
B 2 256 GLN 256 256 256 GLN GLN B . n 
B 2 257 THR 257 257 257 THR THR B . n 
B 2 258 GLY 258 258 258 GLY GLY B . n 
B 2 259 ILE 259 259 259 ILE ILE B . n 
B 2 260 ALA 260 260 260 ALA ALA B . n 
B 2 261 VAL 261 261 261 VAL VAL B . n 
B 2 262 LEU 262 262 262 LEU LEU B . n 
B 2 263 ASP 263 263 263 ASP ASP B . n 
B 2 264 MET 264 264 264 MET MET B . n 
B 2 265 CYS 265 265 265 CYS CYS B . n 
B 2 266 ALA 266 266 266 ALA ALA B . n 
B 2 267 SER 267 267 267 SER SER B . n 
B 2 268 LEU 268 268 268 LEU LEU B . n 
B 2 269 LYS 269 269 269 LYS LYS B . n 
B 2 270 GLU 270 270 270 GLU GLU B . n 
B 2 271 LEU 271 271 271 LEU LEU B . n 
B 2 272 LEU 272 272 272 LEU LEU B . n 
B 2 273 GLN 273 273 273 GLN GLN B . n 
B 2 274 ASN 274 274 274 ASN ASN B . n 
B 2 275 GLY 275 275 275 GLY GLY B . n 
B 2 276 MET 276 276 276 MET MET B . n 
B 2 277 ASN 277 277 277 ASN ASN B . n 
B 2 278 GLY 278 278 278 GLY GLY B . n 
B 2 279 GLY 279 279 279 GLY GLY B . n 
B 2 280 THR 280 280 280 THR THR B . n 
B 2 281 ILE 281 281 281 ILE ILE B . n 
B 2 282 LEU 282 282 282 LEU LEU B . n 
B 2 283 GLY 283 283 283 GLY GLY B . n 
B 2 284 SER 284 284 284 SER SER B . n 
B 2 285 ALA 285 285 285 ALA ALA B . n 
B 2 286 LEU 286 286 286 LEU LEU B . n 
B 2 287 LEU 287 287 287 LEU LEU B . n 
B 2 288 GLU 288 288 288 GLU GLU B . n 
B 2 289 ASP 289 289 289 ASP ASP B . n 
B 2 290 GLU 290 290 290 GLU GLU B . n 
B 2 291 PHE 291 291 291 PHE PHE B . n 
B 2 292 THR 292 292 292 THR THR B . n 
B 2 293 PRO 293 293 293 PRO PRO B . n 
B 2 294 PHE 294 294 294 PHE PHE B . n 
B 2 295 ASP 295 295 295 ASP ASP B . n 
B 2 296 VAL 296 296 296 VAL VAL B . n 
B 2 297 VAL 297 297 297 VAL VAL B . n 
B 2 298 ARG 298 298 298 ARG ARG B . n 
B 2 299 GLN 299 299 299 GLN GLN B . n 
B 2 300 CYS 300 300 300 CYS CYS B . n 
B 2 301 SER 301 301 301 SER SER B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1D81 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1D81 
_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 A1D81 1   401 401 A1D81 LIG A . 
D 3 A1D81 1   401 401 A1D81 LIG B . 
E 4 HOH   1   501 415 HOH   HOH A . 
E 4 HOH   2   502 331 HOH   HOH A . 
E 4 HOH   3   503 470 HOH   HOH A . 
E 4 HOH   4   504 308 HOH   HOH A . 
E 4 HOH   5   505 372 HOH   HOH A . 
E 4 HOH   6   506 284 HOH   HOH A . 
E 4 HOH   7   507 305 HOH   HOH A . 
E 4 HOH   8   508 439 HOH   HOH A . 
E 4 HOH   9   509 330 HOH   HOH A . 
E 4 HOH   10  510 289 HOH   HOH A . 
E 4 HOH   11  511 332 HOH   HOH A . 
E 4 HOH   12  512 417 HOH   HOH A . 
E 4 HOH   13  513 193 HOH   HOH A . 
E 4 HOH   14  514 472 HOH   HOH A . 
E 4 HOH   15  515 329 HOH   HOH A . 
E 4 HOH   16  516 286 HOH   HOH A . 
E 4 HOH   17  517 283 HOH   HOH A . 
E 4 HOH   18  518 327 HOH   HOH A . 
E 4 HOH   19  519 285 HOH   HOH A . 
E 4 HOH   20  520 367 HOH   HOH A . 
E 4 HOH   21  521 157 HOH   HOH A . 
E 4 HOH   22  522 277 HOH   HOH A . 
E 4 HOH   23  523 360 HOH   HOH A . 
E 4 HOH   24  524 175 HOH   HOH A . 
E 4 HOH   25  525 153 HOH   HOH A . 
E 4 HOH   26  526 166 HOH   HOH A . 
E 4 HOH   27  527 299 HOH   HOH A . 
E 4 HOH   28  528 64  HOH   HOH A . 
E 4 HOH   29  529 306 HOH   HOH A . 
E 4 HOH   30  530 106 HOH   HOH A . 
E 4 HOH   31  531 90  HOH   HOH A . 
E 4 HOH   32  532 282 HOH   HOH A . 
E 4 HOH   33  533 158 HOH   HOH A . 
E 4 HOH   34  534 97  HOH   HOH A . 
E 4 HOH   35  535 297 HOH   HOH A . 
E 4 HOH   36  536 139 HOH   HOH A . 
E 4 HOH   37  537 450 HOH   HOH A . 
E 4 HOH   38  538 61  HOH   HOH A . 
E 4 HOH   39  539 155 HOH   HOH A . 
E 4 HOH   40  540 301 HOH   HOH A . 
E 4 HOH   41  541 264 HOH   HOH A . 
E 4 HOH   42  542 94  HOH   HOH A . 
E 4 HOH   43  543 202 HOH   HOH A . 
E 4 HOH   44  544 422 HOH   HOH A . 
E 4 HOH   45  545 183 HOH   HOH A . 
E 4 HOH   46  546 294 HOH   HOH A . 
E 4 HOH   47  547 201 HOH   HOH A . 
E 4 HOH   48  548 24  HOH   HOH A . 
E 4 HOH   49  549 102 HOH   HOH A . 
E 4 HOH   50  550 374 HOH   HOH A . 
E 4 HOH   51  551 77  HOH   HOH A . 
E 4 HOH   52  552 149 HOH   HOH A . 
E 4 HOH   53  553 66  HOH   HOH A . 
E 4 HOH   54  554 101 HOH   HOH A . 
E 4 HOH   55  555 124 HOH   HOH A . 
E 4 HOH   56  556 333 HOH   HOH A . 
E 4 HOH   57  557 416 HOH   HOH A . 
E 4 HOH   58  558 23  HOH   HOH A . 
E 4 HOH   59  559 245 HOH   HOH A . 
E 4 HOH   60  560 208 HOH   HOH A . 
E 4 HOH   61  561 493 HOH   HOH A . 
E 4 HOH   62  562 222 HOH   HOH A . 
E 4 HOH   63  563 99  HOH   HOH A . 
E 4 HOH   64  564 112 HOH   HOH A . 
E 4 HOH   65  565 173 HOH   HOH A . 
E 4 HOH   66  566 176 HOH   HOH A . 
E 4 HOH   67  567 265 HOH   HOH A . 
E 4 HOH   68  568 13  HOH   HOH A . 
E 4 HOH   69  569 198 HOH   HOH A . 
E 4 HOH   70  570 135 HOH   HOH A . 
E 4 HOH   71  571 28  HOH   HOH A . 
E 4 HOH   72  572 405 HOH   HOH A . 
E 4 HOH   73  573 215 HOH   HOH A . 
E 4 HOH   74  574 65  HOH   HOH A . 
E 4 HOH   75  575 55  HOH   HOH A . 
E 4 HOH   76  576 10  HOH   HOH A . 
E 4 HOH   77  577 248 HOH   HOH A . 
E 4 HOH   78  578 230 HOH   HOH A . 
E 4 HOH   79  579 6   HOH   HOH A . 
E 4 HOH   80  580 56  HOH   HOH A . 
E 4 HOH   81  581 263 HOH   HOH A . 
E 4 HOH   82  582 338 HOH   HOH A . 
E 4 HOH   83  583 270 HOH   HOH A . 
E 4 HOH   84  584 71  HOH   HOH A . 
E 4 HOH   85  585 82  HOH   HOH A . 
E 4 HOH   86  586 111 HOH   HOH A . 
E 4 HOH   87  587 354 HOH   HOH A . 
E 4 HOH   88  588 197 HOH   HOH A . 
E 4 HOH   89  589 29  HOH   HOH A . 
E 4 HOH   90  590 195 HOH   HOH A . 
E 4 HOH   91  591 84  HOH   HOH A . 
E 4 HOH   92  592 70  HOH   HOH A . 
E 4 HOH   93  593 98  HOH   HOH A . 
E 4 HOH   94  594 92  HOH   HOH A . 
E 4 HOH   95  595 69  HOH   HOH A . 
E 4 HOH   96  596 145 HOH   HOH A . 
E 4 HOH   97  597 130 HOH   HOH A . 
E 4 HOH   98  598 144 HOH   HOH A . 
E 4 HOH   99  599 463 HOH   HOH A . 
E 4 HOH   100 600 227 HOH   HOH A . 
E 4 HOH   101 601 224 HOH   HOH A . 
E 4 HOH   102 602 36  HOH   HOH A . 
E 4 HOH   103 603 462 HOH   HOH A . 
E 4 HOH   104 604 104 HOH   HOH A . 
E 4 HOH   105 605 16  HOH   HOH A . 
E 4 HOH   106 606 12  HOH   HOH A . 
E 4 HOH   107 607 34  HOH   HOH A . 
E 4 HOH   108 608 373 HOH   HOH A . 
E 4 HOH   109 609 50  HOH   HOH A . 
E 4 HOH   110 610 179 HOH   HOH A . 
E 4 HOH   111 611 466 HOH   HOH A . 
E 4 HOH   112 612 32  HOH   HOH A . 
E 4 HOH   113 613 310 HOH   HOH A . 
E 4 HOH   114 614 40  HOH   HOH A . 
E 4 HOH   115 615 429 HOH   HOH A . 
E 4 HOH   116 616 138 HOH   HOH A . 
E 4 HOH   117 617 268 HOH   HOH A . 
E 4 HOH   118 618 205 HOH   HOH A . 
E 4 HOH   119 619 20  HOH   HOH A . 
E 4 HOH   120 620 325 HOH   HOH A . 
E 4 HOH   121 621 424 HOH   HOH A . 
E 4 HOH   122 622 45  HOH   HOH A . 
E 4 HOH   123 623 311 HOH   HOH A . 
E 4 HOH   124 624 233 HOH   HOH A . 
E 4 HOH   125 625 413 HOH   HOH A . 
E 4 HOH   126 626 113 HOH   HOH A . 
E 4 HOH   127 627 178 HOH   HOH A . 
E 4 HOH   128 628 206 HOH   HOH A . 
E 4 HOH   129 629 123 HOH   HOH A . 
E 4 HOH   130 630 334 HOH   HOH A . 
E 4 HOH   131 631 446 HOH   HOH A . 
E 4 HOH   132 632 251 HOH   HOH A . 
E 4 HOH   133 633 100 HOH   HOH A . 
E 4 HOH   134 634 392 HOH   HOH A . 
E 4 HOH   135 635 88  HOH   HOH A . 
E 4 HOH   136 636 281 HOH   HOH A . 
E 4 HOH   137 637 261 HOH   HOH A . 
E 4 HOH   138 638 218 HOH   HOH A . 
E 4 HOH   139 639 393 HOH   HOH A . 
E 4 HOH   140 640 406 HOH   HOH A . 
E 4 HOH   141 641 141 HOH   HOH A . 
E 4 HOH   142 642 243 HOH   HOH A . 
E 4 HOH   143 643 54  HOH   HOH A . 
E 4 HOH   144 644 355 HOH   HOH A . 
E 4 HOH   145 645 194 HOH   HOH A . 
E 4 HOH   146 646 9   HOH   HOH A . 
E 4 HOH   147 647 259 HOH   HOH A . 
E 4 HOH   148 648 1   HOH   HOH A . 
E 4 HOH   149 649 397 HOH   HOH A . 
E 4 HOH   150 650 37  HOH   HOH A . 
E 4 HOH   151 651 247 HOH   HOH A . 
E 4 HOH   152 652 258 HOH   HOH A . 
E 4 HOH   153 653 172 HOH   HOH A . 
E 4 HOH   154 654 133 HOH   HOH A . 
E 4 HOH   155 655 467 HOH   HOH A . 
E 4 HOH   156 656 328 HOH   HOH A . 
E 4 HOH   157 657 295 HOH   HOH A . 
E 4 HOH   158 658 423 HOH   HOH A . 
E 4 HOH   159 659 142 HOH   HOH A . 
E 4 HOH   160 660 167 HOH   HOH A . 
E 4 HOH   161 661 383 HOH   HOH A . 
E 4 HOH   162 662 341 HOH   HOH A . 
E 4 HOH   163 663 73  HOH   HOH A . 
E 4 HOH   164 664 48  HOH   HOH A . 
E 4 HOH   165 665 217 HOH   HOH A . 
E 4 HOH   166 666 63  HOH   HOH A . 
E 4 HOH   167 667 122 HOH   HOH A . 
E 4 HOH   168 668 260 HOH   HOH A . 
E 4 HOH   169 669 418 HOH   HOH A . 
E 4 HOH   170 670 134 HOH   HOH A . 
E 4 HOH   171 671 316 HOH   HOH A . 
E 4 HOH   172 672 414 HOH   HOH A . 
E 4 HOH   173 673 108 HOH   HOH A . 
E 4 HOH   174 674 350 HOH   HOH A . 
E 4 HOH   175 675 177 HOH   HOH A . 
E 4 HOH   176 676 410 HOH   HOH A . 
E 4 HOH   177 677 497 HOH   HOH A . 
E 4 HOH   178 678 430 HOH   HOH A . 
E 4 HOH   179 679 339 HOH   HOH A . 
E 4 HOH   180 680 231 HOH   HOH A . 
E 4 HOH   181 681 161 HOH   HOH A . 
E 4 HOH   182 682 353 HOH   HOH A . 
E 4 HOH   183 683 344 HOH   HOH A . 
E 4 HOH   184 684 475 HOH   HOH A . 
E 4 HOH   185 685 313 HOH   HOH A . 
E 4 HOH   186 686 196 HOH   HOH A . 
E 4 HOH   187 687 168 HOH   HOH A . 
E 4 HOH   188 688 126 HOH   HOH A . 
E 4 HOH   189 689 402 HOH   HOH A . 
E 4 HOH   190 690 225 HOH   HOH A . 
E 4 HOH   191 691 254 HOH   HOH A . 
E 4 HOH   192 692 189 HOH   HOH A . 
E 4 HOH   193 693 359 HOH   HOH A . 
E 4 HOH   194 694 438 HOH   HOH A . 
E 4 HOH   195 695 370 HOH   HOH A . 
E 4 HOH   196 696 242 HOH   HOH A . 
E 4 HOH   197 697 187 HOH   HOH A . 
E 4 HOH   198 698 240 HOH   HOH A . 
E 4 HOH   199 699 442 HOH   HOH A . 
E 4 HOH   200 700 503 HOH   HOH A . 
E 4 HOH   201 701 437 HOH   HOH A . 
E 4 HOH   202 702 460 HOH   HOH A . 
E 4 HOH   203 703 137 HOH   HOH A . 
E 4 HOH   204 704 449 HOH   HOH A . 
E 4 HOH   205 705 212 HOH   HOH A . 
E 4 HOH   206 706 461 HOH   HOH A . 
E 4 HOH   207 707 390 HOH   HOH A . 
E 4 HOH   208 708 419 HOH   HOH A . 
E 4 HOH   209 709 459 HOH   HOH A . 
E 4 HOH   210 710 252 HOH   HOH A . 
E 4 HOH   211 711 511 HOH   HOH A . 
E 4 HOH   212 712 116 HOH   HOH A . 
E 4 HOH   213 713 336 HOH   HOH A . 
E 4 HOH   214 714 495 HOH   HOH A . 
E 4 HOH   215 715 131 HOH   HOH A . 
E 4 HOH   216 716 400 HOH   HOH A . 
E 4 HOH   217 717 507 HOH   HOH A . 
E 4 HOH   218 718 436 HOH   HOH A . 
E 4 HOH   219 719 312 HOH   HOH A . 
E 4 HOH   220 720 391 HOH   HOH A . 
E 4 HOH   221 721 147 HOH   HOH A . 
E 4 HOH   222 722 351 HOH   HOH A . 
E 4 HOH   223 723 451 HOH   HOH A . 
E 4 HOH   224 724 340 HOH   HOH A . 
E 4 HOH   225 725 473 HOH   HOH A . 
E 4 HOH   226 726 464 HOH   HOH A . 
E 4 HOH   227 727 474 HOH   HOH A . 
E 4 HOH   228 728 352 HOH   HOH A . 
E 4 HOH   229 729 42  HOH   HOH A . 
E 4 HOH   230 730 468 HOH   HOH A . 
E 4 HOH   231 731 335 HOH   HOH A . 
E 4 HOH   232 732 192 HOH   HOH A . 
E 4 HOH   233 733 465 HOH   HOH A . 
E 4 HOH   234 734 509 HOH   HOH A . 
E 4 HOH   235 735 502 HOH   HOH A . 
E 4 HOH   236 736 448 HOH   HOH A . 
E 4 HOH   237 737 431 HOH   HOH A . 
E 4 HOH   238 738 381 HOH   HOH A . 
E 4 HOH   239 739 469 HOH   HOH A . 
E 4 HOH   240 740 244 HOH   HOH A . 
E 4 HOH   241 741 510 HOH   HOH A . 
E 4 HOH   242 742 388 HOH   HOH A . 
E 4 HOH   243 743 401 HOH   HOH A . 
E 4 HOH   244 744 440 HOH   HOH A . 
F 4 HOH   1   501 379 HOH   HOH B . 
F 4 HOH   2   502 323 HOH   HOH B . 
F 4 HOH   3   503 235 HOH   HOH B . 
F 4 HOH   4   504 41  HOH   HOH B . 
F 4 HOH   5   505 290 HOH   HOH B . 
F 4 HOH   6   506 275 HOH   HOH B . 
F 4 HOH   7   507 349 HOH   HOH B . 
F 4 HOH   8   508 105 HOH   HOH B . 
F 4 HOH   9   509 67  HOH   HOH B . 
F 4 HOH   10  510 288 HOH   HOH B . 
F 4 HOH   11  511 220 HOH   HOH B . 
F 4 HOH   12  512 276 HOH   HOH B . 
F 4 HOH   13  513 169 HOH   HOH B . 
F 4 HOH   14  514 170 HOH   HOH B . 
F 4 HOH   15  515 421 HOH   HOH B . 
F 4 HOH   16  516 358 HOH   HOH B . 
F 4 HOH   17  517 163 HOH   HOH B . 
F 4 HOH   18  518 302 HOH   HOH B . 
F 4 HOH   19  519 293 HOH   HOH B . 
F 4 HOH   20  520 234 HOH   HOH B . 
F 4 HOH   21  521 120 HOH   HOH B . 
F 4 HOH   22  522 278 HOH   HOH B . 
F 4 HOH   23  523 219 HOH   HOH B . 
F 4 HOH   24  524 292 HOH   HOH B . 
F 4 HOH   25  525 59  HOH   HOH B . 
F 4 HOH   26  526 287 HOH   HOH B . 
F 4 HOH   27  527 496 HOH   HOH B . 
F 4 HOH   28  528 266 HOH   HOH B . 
F 4 HOH   29  529 17  HOH   HOH B . 
F 4 HOH   30  530 164 HOH   HOH B . 
F 4 HOH   31  531 151 HOH   HOH B . 
F 4 HOH   32  532 398 HOH   HOH B . 
F 4 HOH   33  533 190 HOH   HOH B . 
F 4 HOH   34  534 380 HOH   HOH B . 
F 4 HOH   35  535 322 HOH   HOH B . 
F 4 HOH   36  536 232 HOH   HOH B . 
F 4 HOH   37  537 143 HOH   HOH B . 
F 4 HOH   38  538 103 HOH   HOH B . 
F 4 HOH   39  539 376 HOH   HOH B . 
F 4 HOH   40  540 304 HOH   HOH B . 
F 4 HOH   41  541 165 HOH   HOH B . 
F 4 HOH   42  542 223 HOH   HOH B . 
F 4 HOH   43  543 211 HOH   HOH B . 
F 4 HOH   44  544 38  HOH   HOH B . 
F 4 HOH   45  545 109 HOH   HOH B . 
F 4 HOH   46  546 74  HOH   HOH B . 
F 4 HOH   47  547 39  HOH   HOH B . 
F 4 HOH   48  548 362 HOH   HOH B . 
F 4 HOH   49  549 75  HOH   HOH B . 
F 4 HOH   50  550 79  HOH   HOH B . 
F 4 HOH   51  551 156 HOH   HOH B . 
F 4 HOH   52  552 207 HOH   HOH B . 
F 4 HOH   53  553 81  HOH   HOH B . 
F 4 HOH   54  554 371 HOH   HOH B . 
F 4 HOH   55  555 229 HOH   HOH B . 
F 4 HOH   56  556 51  HOH   HOH B . 
F 4 HOH   57  557 280 HOH   HOH B . 
F 4 HOH   58  558 43  HOH   HOH B . 
F 4 HOH   59  559 321 HOH   HOH B . 
F 4 HOH   60  560 119 HOH   HOH B . 
F 4 HOH   61  561 249 HOH   HOH B . 
F 4 HOH   62  562 452 HOH   HOH B . 
F 4 HOH   63  563 256 HOH   HOH B . 
F 4 HOH   64  564 291 HOH   HOH B . 
F 4 HOH   65  565 91  HOH   HOH B . 
F 4 HOH   66  566 62  HOH   HOH B . 
F 4 HOH   67  567 7   HOH   HOH B . 
F 4 HOH   68  568 274 HOH   HOH B . 
F 4 HOH   69  569 93  HOH   HOH B . 
F 4 HOH   70  570 356 HOH   HOH B . 
F 4 HOH   71  571 31  HOH   HOH B . 
F 4 HOH   72  572 368 HOH   HOH B . 
F 4 HOH   73  573 300 HOH   HOH B . 
F 4 HOH   74  574 148 HOH   HOH B . 
F 4 HOH   75  575 46  HOH   HOH B . 
F 4 HOH   76  576 199 HOH   HOH B . 
F 4 HOH   77  577 425 HOH   HOH B . 
F 4 HOH   78  578 21  HOH   HOH B . 
F 4 HOH   79  579 58  HOH   HOH B . 
F 4 HOH   80  580 35  HOH   HOH B . 
F 4 HOH   81  581 296 HOH   HOH B . 
F 4 HOH   82  582 53  HOH   HOH B . 
F 4 HOH   83  583 15  HOH   HOH B . 
F 4 HOH   84  584 162 HOH   HOH B . 
F 4 HOH   85  585 298 HOH   HOH B . 
F 4 HOH   86  586 185 HOH   HOH B . 
F 4 HOH   87  587 57  HOH   HOH B . 
F 4 HOH   88  588 500 HOH   HOH B . 
F 4 HOH   89  589 399 HOH   HOH B . 
F 4 HOH   90  590 140 HOH   HOH B . 
F 4 HOH   91  591 272 HOH   HOH B . 
F 4 HOH   92  592 226 HOH   HOH B . 
F 4 HOH   93  593 214 HOH   HOH B . 
F 4 HOH   94  594 317 HOH   HOH B . 
F 4 HOH   95  595 269 HOH   HOH B . 
F 4 HOH   96  596 78  HOH   HOH B . 
F 4 HOH   97  597 487 HOH   HOH B . 
F 4 HOH   98  598 324 HOH   HOH B . 
F 4 HOH   99  599 80  HOH   HOH B . 
F 4 HOH   100 600 181 HOH   HOH B . 
F 4 HOH   101 601 150 HOH   HOH B . 
F 4 HOH   102 602 171 HOH   HOH B . 
F 4 HOH   103 603 49  HOH   HOH B . 
F 4 HOH   104 604 320 HOH   HOH B . 
F 4 HOH   105 605 114 HOH   HOH B . 
F 4 HOH   106 606 180 HOH   HOH B . 
F 4 HOH   107 607 186 HOH   HOH B . 
F 4 HOH   108 608 237 HOH   HOH B . 
F 4 HOH   109 609 52  HOH   HOH B . 
F 4 HOH   110 610 309 HOH   HOH B . 
F 4 HOH   111 611 127 HOH   HOH B . 
F 4 HOH   112 612 26  HOH   HOH B . 
F 4 HOH   113 613 128 HOH   HOH B . 
F 4 HOH   114 614 117 HOH   HOH B . 
F 4 HOH   115 615 213 HOH   HOH B . 
F 4 HOH   116 616 19  HOH   HOH B . 
F 4 HOH   117 617 5   HOH   HOH B . 
F 4 HOH   118 618 4   HOH   HOH B . 
F 4 HOH   119 619 129 HOH   HOH B . 
F 4 HOH   120 620 508 HOH   HOH B . 
F 4 HOH   121 621 25  HOH   HOH B . 
F 4 HOH   122 622 22  HOH   HOH B . 
F 4 HOH   123 623 95  HOH   HOH B . 
F 4 HOH   124 624 396 HOH   HOH B . 
F 4 HOH   125 625 444 HOH   HOH B . 
F 4 HOH   126 626 434 HOH   HOH B . 
F 4 HOH   127 627 184 HOH   HOH B . 
F 4 HOH   128 628 136 HOH   HOH B . 
F 4 HOH   129 629 87  HOH   HOH B . 
F 4 HOH   130 630 246 HOH   HOH B . 
F 4 HOH   131 631 342 HOH   HOH B . 
F 4 HOH   132 632 262 HOH   HOH B . 
F 4 HOH   133 633 385 HOH   HOH B . 
F 4 HOH   134 634 307 HOH   HOH B . 
F 4 HOH   135 635 115 HOH   HOH B . 
F 4 HOH   136 636 68  HOH   HOH B . 
F 4 HOH   137 637 420 HOH   HOH B . 
F 4 HOH   138 638 18  HOH   HOH B . 
F 4 HOH   139 639 257 HOH   HOH B . 
F 4 HOH   140 640 363 HOH   HOH B . 
F 4 HOH   141 641 3   HOH   HOH B . 
F 4 HOH   142 642 255 HOH   HOH B . 
F 4 HOH   143 643 27  HOH   HOH B . 
F 4 HOH   144 644 60  HOH   HOH B . 
F 4 HOH   145 645 121 HOH   HOH B . 
F 4 HOH   146 646 432 HOH   HOH B . 
F 4 HOH   147 647 453 HOH   HOH B . 
F 4 HOH   148 648 395 HOH   HOH B . 
F 4 HOH   149 649 14  HOH   HOH B . 
F 4 HOH   150 650 346 HOH   HOH B . 
F 4 HOH   151 651 86  HOH   HOH B . 
F 4 HOH   152 652 411 HOH   HOH B . 
F 4 HOH   153 653 303 HOH   HOH B . 
F 4 HOH   154 654 188 HOH   HOH B . 
F 4 HOH   155 655 476 HOH   HOH B . 
F 4 HOH   156 656 479 HOH   HOH B . 
F 4 HOH   157 657 8   HOH   HOH B . 
F 4 HOH   158 658 96  HOH   HOH B . 
F 4 HOH   159 659 326 HOH   HOH B . 
F 4 HOH   160 660 279 HOH   HOH B . 
F 4 HOH   161 661 210 HOH   HOH B . 
F 4 HOH   162 662 132 HOH   HOH B . 
F 4 HOH   163 663 146 HOH   HOH B . 
F 4 HOH   164 664 504 HOH   HOH B . 
F 4 HOH   165 665 204 HOH   HOH B . 
F 4 HOH   166 666 30  HOH   HOH B . 
F 4 HOH   167 667 85  HOH   HOH B . 
F 4 HOH   168 668 44  HOH   HOH B . 
F 4 HOH   169 669 2   HOH   HOH B . 
F 4 HOH   170 670 267 HOH   HOH B . 
F 4 HOH   171 671 209 HOH   HOH B . 
F 4 HOH   172 672 273 HOH   HOH B . 
F 4 HOH   173 673 239 HOH   HOH B . 
F 4 HOH   174 674 200 HOH   HOH B . 
F 4 HOH   175 675 11  HOH   HOH B . 
F 4 HOH   176 676 343 HOH   HOH B . 
F 4 HOH   177 677 387 HOH   HOH B . 
F 4 HOH   178 678 83  HOH   HOH B . 
F 4 HOH   179 679 228 HOH   HOH B . 
F 4 HOH   180 680 107 HOH   HOH B . 
F 4 HOH   181 681 125 HOH   HOH B . 
F 4 HOH   182 682 72  HOH   HOH B . 
F 4 HOH   183 683 76  HOH   HOH B . 
F 4 HOH   184 684 216 HOH   HOH B . 
F 4 HOH   185 685 490 HOH   HOH B . 
F 4 HOH   186 686 191 HOH   HOH B . 
F 4 HOH   187 687 236 HOH   HOH B . 
F 4 HOH   188 688 366 HOH   HOH B . 
F 4 HOH   189 689 154 HOH   HOH B . 
F 4 HOH   190 690 382 HOH   HOH B . 
F 4 HOH   191 691 488 HOH   HOH B . 
F 4 HOH   192 692 314 HOH   HOH B . 
F 4 HOH   193 693 485 HOH   HOH B . 
F 4 HOH   194 694 160 HOH   HOH B . 
F 4 HOH   195 695 238 HOH   HOH B . 
F 4 HOH   196 696 384 HOH   HOH B . 
F 4 HOH   197 697 364 HOH   HOH B . 
F 4 HOH   198 698 369 HOH   HOH B . 
F 4 HOH   199 699 33  HOH   HOH B . 
F 4 HOH   200 700 345 HOH   HOH B . 
F 4 HOH   201 701 182 HOH   HOH B . 
F 4 HOH   202 702 378 HOH   HOH B . 
F 4 HOH   203 703 403 HOH   HOH B . 
F 4 HOH   204 704 494 HOH   HOH B . 
F 4 HOH   205 705 271 HOH   HOH B . 
F 4 HOH   206 706 471 HOH   HOH B . 
F 4 HOH   207 707 498 HOH   HOH B . 
F 4 HOH   208 708 394 HOH   HOH B . 
F 4 HOH   209 709 118 HOH   HOH B . 
F 4 HOH   210 710 348 HOH   HOH B . 
F 4 HOH   211 711 412 HOH   HOH B . 
F 4 HOH   212 712 319 HOH   HOH B . 
F 4 HOH   213 713 152 HOH   HOH B . 
F 4 HOH   214 714 481 HOH   HOH B . 
F 4 HOH   215 715 445 HOH   HOH B . 
F 4 HOH   216 716 347 HOH   HOH B . 
F 4 HOH   217 717 458 HOH   HOH B . 
F 4 HOH   218 718 47  HOH   HOH B . 
F 4 HOH   219 719 221 HOH   HOH B . 
F 4 HOH   220 720 386 HOH   HOH B . 
F 4 HOH   221 721 407 HOH   HOH B . 
F 4 HOH   222 722 478 HOH   HOH B . 
F 4 HOH   223 723 159 HOH   HOH B . 
F 4 HOH   224 724 365 HOH   HOH B . 
F 4 HOH   225 725 505 HOH   HOH B . 
F 4 HOH   226 726 480 HOH   HOH B . 
F 4 HOH   227 727 174 HOH   HOH B . 
F 4 HOH   228 728 454 HOH   HOH B . 
F 4 HOH   229 729 428 HOH   HOH B . 
F 4 HOH   230 730 408 HOH   HOH B . 
F 4 HOH   231 731 253 HOH   HOH B . 
F 4 HOH   232 732 457 HOH   HOH B . 
F 4 HOH   233 733 318 HOH   HOH B . 
F 4 HOH   234 734 455 HOH   HOH B . 
F 4 HOH   235 735 427 HOH   HOH B . 
F 4 HOH   236 736 361 HOH   HOH B . 
F 4 HOH   237 737 89  HOH   HOH B . 
F 4 HOH   238 738 499 HOH   HOH B . 
F 4 HOH   239 739 250 HOH   HOH B . 
F 4 HOH   240 740 409 HOH   HOH B . 
F 4 HOH   241 741 492 HOH   HOH B . 
F 4 HOH   242 742 377 HOH   HOH B . 
F 4 HOH   243 743 404 HOH   HOH B . 
F 4 HOH   244 744 241 HOH   HOH B . 
F 4 HOH   245 745 447 HOH   HOH B . 
F 4 HOH   246 746 389 HOH   HOH B . 
F 4 HOH   247 747 477 HOH   HOH B . 
F 4 HOH   248 748 203 HOH   HOH B . 
F 4 HOH   249 749 482 HOH   HOH B . 
F 4 HOH   250 750 491 HOH   HOH B . 
F 4 HOH   251 751 426 HOH   HOH B . 
F 4 HOH   252 752 486 HOH   HOH B . 
F 4 HOH   253 753 357 HOH   HOH B . 
F 4 HOH   254 754 110 HOH   HOH B . 
F 4 HOH   255 755 441 HOH   HOH B . 
F 4 HOH   256 756 456 HOH   HOH B . 
F 4 HOH   257 757 337 HOH   HOH B . 
F 4 HOH   258 758 435 HOH   HOH B . 
F 4 HOH   259 759 375 HOH   HOH B . 
F 4 HOH   260 760 484 HOH   HOH B . 
F 4 HOH   261 761 506 HOH   HOH B . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0415 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   108.05 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZUC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     55.449 
_cell.length_a_esd                 ? 
_cell.length_b                     99.411 
_cell.length_b_esd                 ? 
_cell.length_c                     58.542 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         8ZUC 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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                   8ZUC 
_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             2.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.35 
_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              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M Ammonium acetate, 15% (w/v) PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZUC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.10 
_reflns.d_resolution_low                               52.78 
_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                                     34208 
_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                           97.04 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          27.24 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_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                                    2.1 
_reflns_shell.d_res_low                                     2.175 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1717 
_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                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  1 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_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]                            -0.45 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -1.39 
_refine.aniso_B[2][2]                            -0.07 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            1.17 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               18.249 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.940 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8ZUC 
_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                            2.10 
_refine.ls_d_res_low                             52.78 
_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                     32491 
_refine.ls_number_reflns_R_free                  1717 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.07 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.15305 
_refine.ls_R_factor_R_free                       0.19336 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.15091 
_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                    MASK 
_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                          ? 
_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       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.223 
_refine.pdbx_overall_ESU_R_Free                  0.169 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             4.098 
_refine.overall_SU_ML                            0.109 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        52.78 
_refine_hist.number_atoms_solvent             505 
_refine_hist.number_atoms_total               5239 
_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        4734 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  0.011  4922  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  4511  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.333  1.655  6718  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.450  1.573  10379 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.884  5.000  622   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 7.433  5.000  21    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.125 10.000 776   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.064  0.200  743   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  5899  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1163  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.757  1.768  2449  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.757  1.768  2449  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.796  3.164  3072  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.796  3.165  3073  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.607  2.077  2473  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.607  2.078  2474  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.139  3.670  3643  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.204  20.51  5556  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.055  19.41  5447  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.100 
_refine_ls_shell.d_res_low                        2.154 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             125 
_refine_ls_shell.number_reflns_R_work             2457 
_refine_ls_shell.percent_reflns_obs               99.85 
_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                  0.174 
_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   20 
_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                  0.236 
# 
_struct.entry_id                     8ZUC 
_struct.title                        'The Crystal structure of mol080 bound to the main protease (3CLpro/Mpro) of SARS-CoV-2' 
_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        8ZUC 
_struct_keywords.text            'inhibitor, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL 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 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
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 R1AB_SARS2 P0DTD1 ? 1 
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCS
;
3264 
2 UNP R1AB_SARS2 P0DTD1 ? 2 
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCS
;
3264 
# 
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 8ZUC A 1 ? 301 ? P0DTD1 3264 ? 3564 ? 1 301 
2 2 8ZUC B 1 ? 301 ? P0DTD1 3264 ? 3564 ? 1 301 
# 
_struct_ref_seq_dif.align_id                     2 
_struct_ref_seq_dif.pdbx_pdb_id_code             8ZUC 
_struct_ref_seq_dif.mon_id                       GLY 
_struct_ref_seq_dif.pdbx_pdb_strand_id           B 
_struct_ref_seq_dif.seq_num                      279 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P0DTD1 
_struct_ref_seq_dif.db_mon_id                    ARG 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          3542 
_struct_ref_seq_dif.details                      conflict 
_struct_ref_seq_dif.pdbx_auth_seq_num            279 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_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)' 2210  ? 
1 MORE         -7    ? 
1 'SSA (A^2)'  25620 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 GLU A 47  ? ASN A 51  ? GLU A 47  ASN A 51  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 292 ? SER A 301 ? THR A 292 SER A 301 1 ? 10 
HELX_P HELX_P12 AB3 SER B 10  ? GLY B 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P13 AB4 HIS B 41  ? CYS B 44  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P14 AB5 THR B 45  ? MET B 49  ? THR B 45  MET B 49  5 ? 5  
HELX_P HELX_P15 AB6 ASN B 53  ? ARG B 60  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P16 AB7 SER B 62  ? PHE B 66  ? SER B 62  PHE B 66  5 ? 5  
HELX_P HELX_P17 AB8 ILE B 200 ? ASN B 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P18 AB9 THR B 226 ? TYR B 237 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P19 AC1 THR B 243 ? LEU B 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P20 AC2 LEU B 250 ? GLY B 258 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P21 AC3 ALA B 260 ? GLY B 275 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P22 AC4 THR B 292 ? SER B 301 ? THR B 292 SER B 301 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? 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 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
AA4 1 VAL B 73  ? LEU B 75  ? VAL B 73  LEU B 75  
AA4 2 LEU B 67  ? ALA B 70  ? LEU B 67  ALA B 70  
AA4 3 MET B 17  ? CYS B 22  ? MET B 17  CYS B 22  
AA4 4 THR B 25  ? LEU B 32  ? THR B 25  LEU B 32  
AA4 5 VAL B 35  ? PRO B 39  ? VAL B 35  PRO B 39  
AA4 6 VAL B 86  ? VAL B 91  ? VAL B 86  VAL B 91  
AA4 7 VAL B 77  ? GLN B 83  ? VAL B 77  GLN B 83  
AA5 1 LYS B 100 ? PHE B 103 ? LYS B 100 PHE B 103 
AA5 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA5 3 VAL B 148 ? ASP B 153 ? VAL B 148 ASP B 153 
AA5 4 THR B 111 ? TYR B 118 ? THR B 111 TYR B 118 
AA5 5 SER B 121 ? ALA B 129 ? SER B 121 ALA B 129 
AA6 1 LYS B 100 ? PHE B 103 ? LYS B 100 PHE B 103 
AA6 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA6 3 HIS B 172 ? THR B 175 ? HIS B 172 THR B 175 
# 
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 O VAL A 73  ? O VAL A 73  N ALA A 70  ? N ALA A 70  
AA1 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N VAL A 36  ? N VAL A 36  O LEU A 89  ? O LEU A 89  
AA1 6 7 O VAL A 86  ? O VAL A 86  N GLN A 83  ? N GLN A 83  
AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N VAL A 114 ? N VAL A 114 O TYR A 126 ? O TYR A 126 
AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
AA4 1 2 O LEU B 75  ? O LEU B 75  N VAL B 68  ? N VAL B 68  
AA4 2 3 O LEU B 67  ? O LEU B 67  N THR B 21  ? N THR B 21  
AA4 3 4 N VAL B 20  ? N VAL B 20  O LEU B 27  ? O LEU B 27  
AA4 4 5 N LEU B 30  ? N LEU B 30  O TYR B 37  ? O TYR B 37  
AA4 5 6 N CYS B 38  ? N CYS B 38  O LEU B 87  ? O LEU B 87  
AA4 6 7 O LYS B 90  ? O LYS B 90  N ILE B 78  ? N ILE B 78  
AA5 1 2 N LYS B 100 ? N LYS B 100 O VAL B 157 ? O VAL B 157 
AA5 2 3 O SER B 158 ? O SER B 158 N ASN B 151 ? N ASN B 151 
AA5 3 4 O PHE B 150 ? O PHE B 150 N SER B 113 ? N SER B 113 
AA5 4 5 N ALA B 116 ? N ALA B 116 O SER B 123 ? O SER B 123 
AA6 1 2 N LYS B 100 ? N LYS B 100 O VAL B 157 ? O VAL B 157 
AA6 2 3 N MET B 165 ? N MET B 165 O ALA B 173 ? O ALA B 173 
# 
_pdbx_entry_details.entry_id                   8ZUC 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LEU A 27  ? ? -164.52 -169.67 
2  1 ASP A 33  ? ? 51.19   -123.45 
3  1 ASN A 51  ? ? -151.31 68.09   
4  1 ASN A 84  ? ? 52.91   -122.18 
5  1 TYR A 154 ? ? 64.52   -110.09 
6  1 PRO A 184 ? ? -85.93  36.14   
7  1 ASP B 33  ? ? 48.27   -129.52 
8  1 ASN B 84  ? ? 53.51   -123.16 
9  1 TYR B 154 ? ? 61.66   60.56   
10 1 PRO B 184 ? ? -87.00  39.52   
11 1 ARG B 217 ? ? -141.12 21.18   
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 744 ? 6.09 . 
2 1 O ? B HOH 760 ? 5.95 . 
3 1 O ? B HOH 761 ? 6.06 . 
# 
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 
A1D81 N1   N  N N 1   
A1D81 N3   N  N N 2   
A1D81 C4   C  Y N 3   
A1D81 C5   C  Y N 4   
A1D81 C6   C  Y N 5   
A1D81 C7   C  N N 6   
A1D81 C8   C  N N 7   
A1D81 C10  C  N N 8   
A1D81 C13  C  Y N 9   
A1D81 C15  C  Y N 10  
A1D81 C17  C  Y N 11  
A1D81 C20  C  Y N 12  
A1D81 C21  C  N N 13  
A1D81 C22  C  Y N 14  
A1D81 C24  C  N N 15  
A1D81 C26  C  N N 16  
A1D81 C1   C  Y N 17  
A1D81 C2   C  Y N 18  
A1D81 C3   C  Y N 19  
A1D81 CL1  CL N N 20  
A1D81 N2   N  N N 21  
A1D81 C9   C  N N 22  
A1D81 O1   O  N N 23  
A1D81 O2   O  N N 24  
A1D81 C11  C  N N 25  
A1D81 C12  C  Y N 26  
A1D81 C14  C  Y N 27  
A1D81 C16  C  Y N 28  
A1D81 F1   F  N N 29  
A1D81 F2   F  N N 30  
A1D81 F3   F  N N 31  
A1D81 C18  C  N N 32  
A1D81 C19  C  Y N 33  
A1D81 N4   N  Y N 34  
A1D81 N5   N  Y N 35  
A1D81 N6   N  Y N 36  
A1D81 N7   N  Y N 37  
A1D81 N8   N  Y N 38  
A1D81 C23  C  N N 39  
A1D81 C25  C  N N 40  
A1D81 C27  C  N N 41  
A1D81 H1   H  N N 42  
A1D81 H2   H  N N 43  
A1D81 H3   H  N N 44  
A1D81 H4   H  N N 45  
A1D81 H5   H  N N 46  
A1D81 H6   H  N N 47  
A1D81 H7   H  N N 48  
A1D81 H8   H  N N 49  
A1D81 H9   H  N N 50  
A1D81 H10  H  N N 51  
A1D81 H11  H  N N 52  
A1D81 H12  H  N N 53  
A1D81 H13  H  N N 54  
A1D81 H14  H  N N 55  
A1D81 H15  H  N N 56  
A1D81 H16  H  N N 57  
A1D81 H17  H  N N 58  
A1D81 H18  H  N N 59  
A1D81 H19  H  N N 60  
A1D81 H20  H  N N 61  
A1D81 H21  H  N N 62  
A1D81 H22  H  N N 63  
A1D81 H23  H  N N 64  
A1D81 H24  H  N N 65  
A1D81 H25  H  N N 66  
A1D81 H26  H  N N 67  
ALA   N    N  N N 68  
ALA   CA   C  N S 69  
ALA   C    C  N N 70  
ALA   O    O  N N 71  
ALA   CB   C  N N 72  
ALA   OXT  O  N N 73  
ALA   H    H  N N 74  
ALA   H2   H  N N 75  
ALA   HA   H  N N 76  
ALA   HB1  H  N N 77  
ALA   HB2  H  N N 78  
ALA   HB3  H  N N 79  
ALA   HXT  H  N N 80  
ARG   N    N  N N 81  
ARG   CA   C  N S 82  
ARG   C    C  N N 83  
ARG   O    O  N N 84  
ARG   CB   C  N N 85  
ARG   CG   C  N N 86  
ARG   CD   C  N N 87  
ARG   NE   N  N N 88  
ARG   CZ   C  N N 89  
ARG   NH1  N  N N 90  
ARG   NH2  N  N N 91  
ARG   OXT  O  N N 92  
ARG   H    H  N N 93  
ARG   H2   H  N N 94  
ARG   HA   H  N N 95  
ARG   HB2  H  N N 96  
ARG   HB3  H  N N 97  
ARG   HG2  H  N N 98  
ARG   HG3  H  N N 99  
ARG   HD2  H  N N 100 
ARG   HD3  H  N N 101 
ARG   HE   H  N N 102 
ARG   HH11 H  N N 103 
ARG   HH12 H  N N 104 
ARG   HH21 H  N N 105 
ARG   HH22 H  N N 106 
ARG   HXT  H  N N 107 
ASN   N    N  N N 108 
ASN   CA   C  N S 109 
ASN   C    C  N N 110 
ASN   O    O  N N 111 
ASN   CB   C  N N 112 
ASN   CG   C  N N 113 
ASN   OD1  O  N N 114 
ASN   ND2  N  N N 115 
ASN   OXT  O  N N 116 
ASN   H    H  N N 117 
ASN   H2   H  N N 118 
ASN   HA   H  N N 119 
ASN   HB2  H  N N 120 
ASN   HB3  H  N N 121 
ASN   HD21 H  N N 122 
ASN   HD22 H  N N 123 
ASN   HXT  H  N N 124 
ASP   N    N  N N 125 
ASP   CA   C  N S 126 
ASP   C    C  N N 127 
ASP   O    O  N N 128 
ASP   CB   C  N N 129 
ASP   CG   C  N N 130 
ASP   OD1  O  N N 131 
ASP   OD2  O  N N 132 
ASP   OXT  O  N N 133 
ASP   H    H  N N 134 
ASP   H2   H  N N 135 
ASP   HA   H  N N 136 
ASP   HB2  H  N N 137 
ASP   HB3  H  N N 138 
ASP   HD2  H  N N 139 
ASP   HXT  H  N N 140 
CYS   N    N  N N 141 
CYS   CA   C  N R 142 
CYS   C    C  N N 143 
CYS   O    O  N N 144 
CYS   CB   C  N N 145 
CYS   SG   S  N N 146 
CYS   OXT  O  N N 147 
CYS   H    H  N N 148 
CYS   H2   H  N N 149 
CYS   HA   H  N N 150 
CYS   HB2  H  N N 151 
CYS   HB3  H  N N 152 
CYS   HG   H  N N 153 
CYS   HXT  H  N N 154 
GLN   N    N  N N 155 
GLN   CA   C  N S 156 
GLN   C    C  N N 157 
GLN   O    O  N N 158 
GLN   CB   C  N N 159 
GLN   CG   C  N N 160 
GLN   CD   C  N N 161 
GLN   OE1  O  N N 162 
GLN   NE2  N  N N 163 
GLN   OXT  O  N N 164 
GLN   H    H  N N 165 
GLN   H2   H  N N 166 
GLN   HA   H  N N 167 
GLN   HB2  H  N N 168 
GLN   HB3  H  N N 169 
GLN   HG2  H  N N 170 
GLN   HG3  H  N N 171 
GLN   HE21 H  N N 172 
GLN   HE22 H  N N 173 
GLN   HXT  H  N N 174 
GLU   N    N  N N 175 
GLU   CA   C  N S 176 
GLU   C    C  N N 177 
GLU   O    O  N N 178 
GLU   CB   C  N N 179 
GLU   CG   C  N N 180 
GLU   CD   C  N N 181 
GLU   OE1  O  N N 182 
GLU   OE2  O  N N 183 
GLU   OXT  O  N N 184 
GLU   H    H  N N 185 
GLU   H2   H  N N 186 
GLU   HA   H  N N 187 
GLU   HB2  H  N N 188 
GLU   HB3  H  N N 189 
GLU   HG2  H  N N 190 
GLU   HG3  H  N N 191 
GLU   HE2  H  N N 192 
GLU   HXT  H  N N 193 
GLY   N    N  N N 194 
GLY   CA   C  N N 195 
GLY   C    C  N N 196 
GLY   O    O  N N 197 
GLY   OXT  O  N N 198 
GLY   H    H  N N 199 
GLY   H2   H  N N 200 
GLY   HA2  H  N N 201 
GLY   HA3  H  N N 202 
GLY   HXT  H  N N 203 
HIS   N    N  N N 204 
HIS   CA   C  N S 205 
HIS   C    C  N N 206 
HIS   O    O  N N 207 
HIS   CB   C  N N 208 
HIS   CG   C  Y N 209 
HIS   ND1  N  Y N 210 
HIS   CD2  C  Y N 211 
HIS   CE1  C  Y N 212 
HIS   NE2  N  Y N 213 
HIS   OXT  O  N N 214 
HIS   H    H  N N 215 
HIS   H2   H  N N 216 
HIS   HA   H  N N 217 
HIS   HB2  H  N N 218 
HIS   HB3  H  N N 219 
HIS   HD1  H  N N 220 
HIS   HD2  H  N N 221 
HIS   HE1  H  N N 222 
HIS   HE2  H  N N 223 
HIS   HXT  H  N N 224 
HOH   O    O  N N 225 
HOH   H1   H  N N 226 
HOH   H2   H  N N 227 
ILE   N    N  N N 228 
ILE   CA   C  N S 229 
ILE   C    C  N N 230 
ILE   O    O  N N 231 
ILE   CB   C  N S 232 
ILE   CG1  C  N N 233 
ILE   CG2  C  N N 234 
ILE   CD1  C  N N 235 
ILE   OXT  O  N N 236 
ILE   H    H  N N 237 
ILE   H2   H  N N 238 
ILE   HA   H  N N 239 
ILE   HB   H  N N 240 
ILE   HG12 H  N N 241 
ILE   HG13 H  N N 242 
ILE   HG21 H  N N 243 
ILE   HG22 H  N N 244 
ILE   HG23 H  N N 245 
ILE   HD11 H  N N 246 
ILE   HD12 H  N N 247 
ILE   HD13 H  N N 248 
ILE   HXT  H  N N 249 
LEU   N    N  N N 250 
LEU   CA   C  N S 251 
LEU   C    C  N N 252 
LEU   O    O  N N 253 
LEU   CB   C  N N 254 
LEU   CG   C  N N 255 
LEU   CD1  C  N N 256 
LEU   CD2  C  N N 257 
LEU   OXT  O  N N 258 
LEU   H    H  N N 259 
LEU   H2   H  N N 260 
LEU   HA   H  N N 261 
LEU   HB2  H  N N 262 
LEU   HB3  H  N N 263 
LEU   HG   H  N N 264 
LEU   HD11 H  N N 265 
LEU   HD12 H  N N 266 
LEU   HD13 H  N N 267 
LEU   HD21 H  N N 268 
LEU   HD22 H  N N 269 
LEU   HD23 H  N N 270 
LEU   HXT  H  N N 271 
LYS   N    N  N N 272 
LYS   CA   C  N S 273 
LYS   C    C  N N 274 
LYS   O    O  N N 275 
LYS   CB   C  N N 276 
LYS   CG   C  N N 277 
LYS   CD   C  N N 278 
LYS   CE   C  N N 279 
LYS   NZ   N  N N 280 
LYS   OXT  O  N N 281 
LYS   H    H  N N 282 
LYS   H2   H  N N 283 
LYS   HA   H  N N 284 
LYS   HB2  H  N N 285 
LYS   HB3  H  N N 286 
LYS   HG2  H  N N 287 
LYS   HG3  H  N N 288 
LYS   HD2  H  N N 289 
LYS   HD3  H  N N 290 
LYS   HE2  H  N N 291 
LYS   HE3  H  N N 292 
LYS   HZ1  H  N N 293 
LYS   HZ2  H  N N 294 
LYS   HZ3  H  N N 295 
LYS   HXT  H  N N 296 
MET   N    N  N N 297 
MET   CA   C  N S 298 
MET   C    C  N N 299 
MET   O    O  N N 300 
MET   CB   C  N N 301 
MET   CG   C  N N 302 
MET   SD   S  N N 303 
MET   CE   C  N N 304 
MET   OXT  O  N N 305 
MET   H    H  N N 306 
MET   H2   H  N N 307 
MET   HA   H  N N 308 
MET   HB2  H  N N 309 
MET   HB3  H  N N 310 
MET   HG2  H  N N 311 
MET   HG3  H  N N 312 
MET   HE1  H  N N 313 
MET   HE2  H  N N 314 
MET   HE3  H  N N 315 
MET   HXT  H  N N 316 
PHE   N    N  N N 317 
PHE   CA   C  N S 318 
PHE   C    C  N N 319 
PHE   O    O  N N 320 
PHE   CB   C  N N 321 
PHE   CG   C  Y N 322 
PHE   CD1  C  Y N 323 
PHE   CD2  C  Y N 324 
PHE   CE1  C  Y N 325 
PHE   CE2  C  Y N 326 
PHE   CZ   C  Y N 327 
PHE   OXT  O  N N 328 
PHE   H    H  N N 329 
PHE   H2   H  N N 330 
PHE   HA   H  N N 331 
PHE   HB2  H  N N 332 
PHE   HB3  H  N N 333 
PHE   HD1  H  N N 334 
PHE   HD2  H  N N 335 
PHE   HE1  H  N N 336 
PHE   HE2  H  N N 337 
PHE   HZ   H  N N 338 
PHE   HXT  H  N N 339 
PRO   N    N  N N 340 
PRO   CA   C  N S 341 
PRO   C    C  N N 342 
PRO   O    O  N N 343 
PRO   CB   C  N N 344 
PRO   CG   C  N N 345 
PRO   CD   C  N N 346 
PRO   OXT  O  N N 347 
PRO   H    H  N N 348 
PRO   HA   H  N N 349 
PRO   HB2  H  N N 350 
PRO   HB3  H  N N 351 
PRO   HG2  H  N N 352 
PRO   HG3  H  N N 353 
PRO   HD2  H  N N 354 
PRO   HD3  H  N N 355 
PRO   HXT  H  N N 356 
SER   N    N  N N 357 
SER   CA   C  N S 358 
SER   C    C  N N 359 
SER   O    O  N N 360 
SER   CB   C  N N 361 
SER   OG   O  N N 362 
SER   OXT  O  N N 363 
SER   H    H  N N 364 
SER   H2   H  N N 365 
SER   HA   H  N N 366 
SER   HB2  H  N N 367 
SER   HB3  H  N N 368 
SER   HG   H  N N 369 
SER   HXT  H  N N 370 
THR   N    N  N N 371 
THR   CA   C  N S 372 
THR   C    C  N N 373 
THR   O    O  N N 374 
THR   CB   C  N R 375 
THR   OG1  O  N N 376 
THR   CG2  C  N N 377 
THR   OXT  O  N N 378 
THR   H    H  N N 379 
THR   H2   H  N N 380 
THR   HA   H  N N 381 
THR   HB   H  N N 382 
THR   HG1  H  N N 383 
THR   HG21 H  N N 384 
THR   HG22 H  N N 385 
THR   HG23 H  N N 386 
THR   HXT  H  N N 387 
TRP   N    N  N N 388 
TRP   CA   C  N S 389 
TRP   C    C  N N 390 
TRP   O    O  N N 391 
TRP   CB   C  N N 392 
TRP   CG   C  Y N 393 
TRP   CD1  C  Y N 394 
TRP   CD2  C  Y N 395 
TRP   NE1  N  Y N 396 
TRP   CE2  C  Y N 397 
TRP   CE3  C  Y N 398 
TRP   CZ2  C  Y N 399 
TRP   CZ3  C  Y N 400 
TRP   CH2  C  Y N 401 
TRP   OXT  O  N N 402 
TRP   H    H  N N 403 
TRP   H2   H  N N 404 
TRP   HA   H  N N 405 
TRP   HB2  H  N N 406 
TRP   HB3  H  N N 407 
TRP   HD1  H  N N 408 
TRP   HE1  H  N N 409 
TRP   HE3  H  N N 410 
TRP   HZ2  H  N N 411 
TRP   HZ3  H  N N 412 
TRP   HH2  H  N N 413 
TRP   HXT  H  N N 414 
TYR   N    N  N N 415 
TYR   CA   C  N S 416 
TYR   C    C  N N 417 
TYR   O    O  N N 418 
TYR   CB   C  N N 419 
TYR   CG   C  Y N 420 
TYR   CD1  C  Y N 421 
TYR   CD2  C  Y N 422 
TYR   CE1  C  Y N 423 
TYR   CE2  C  Y N 424 
TYR   CZ   C  Y N 425 
TYR   OH   O  N N 426 
TYR   OXT  O  N N 427 
TYR   H    H  N N 428 
TYR   H2   H  N N 429 
TYR   HA   H  N N 430 
TYR   HB2  H  N N 431 
TYR   HB3  H  N N 432 
TYR   HD1  H  N N 433 
TYR   HD2  H  N N 434 
TYR   HE1  H  N N 435 
TYR   HE2  H  N N 436 
TYR   HH   H  N N 437 
TYR   HXT  H  N N 438 
VAL   N    N  N N 439 
VAL   CA   C  N S 440 
VAL   C    C  N N 441 
VAL   O    O  N N 442 
VAL   CB   C  N N 443 
VAL   CG1  C  N N 444 
VAL   CG2  C  N N 445 
VAL   OXT  O  N N 446 
VAL   H    H  N N 447 
VAL   H2   H  N N 448 
VAL   HA   H  N N 449 
VAL   HB   H  N N 450 
VAL   HG11 H  N N 451 
VAL   HG12 H  N N 452 
VAL   HG13 H  N N 453 
VAL   HG21 H  N N 454 
VAL   HG22 H  N N 455 
VAL   HG23 H  N N 456 
VAL   HXT  H  N N 457 
# 
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 
A1D81 C26 C25  sing N N 1   
A1D81 C25 C27  sing N N 2   
A1D81 C25 C24  sing N N 3   
A1D81 C24 C23  sing N N 4   
A1D81 C23 N7   sing N N 5   
A1D81 N7  N8   sing Y N 6   
A1D81 N7  C22  sing Y N 7   
A1D81 N8  C2   doub Y N 8   
A1D81 C22 C1   doub Y N 9   
A1D81 C2  C1   sing Y N 10  
A1D81 C2  C3   sing Y N 11  
A1D81 C1  C6   sing Y N 12  
A1D81 C3  C4   doub Y N 13  
A1D81 C6  C5   doub Y N 14  
A1D81 C4  C5   sing Y N 15  
A1D81 C4  CL1  sing N N 16  
A1D81 C5  N1   sing N N 17  
A1D81 N1  C7   sing N N 18  
A1D81 C10 C7   doub N N 19  
A1D81 C10 C9   sing N N 20  
A1D81 C7  N2   sing N N 21  
A1D81 C9  O1   doub N N 22  
A1D81 C9  N3   sing N N 23  
A1D81 N2  C11  sing N N 24  
A1D81 N2  C8   sing N N 25  
A1D81 C11 C12  sing N N 26  
A1D81 C12 C17  doub Y N 27  
A1D81 C12 C13  sing Y N 28  
A1D81 C17 C16  sing Y N 29  
A1D81 F3  C13  sing N N 30  
A1D81 C13 C14  doub Y N 31  
A1D81 C16 F1   sing N N 32  
A1D81 C16 C15  doub Y N 33  
A1D81 N3  C8   sing N N 34  
A1D81 N3  C18  sing N N 35  
A1D81 C8  O2   doub N N 36  
A1D81 C14 C15  sing Y N 37  
A1D81 C15 F2   sing N N 38  
A1D81 N6  C19  doub Y N 39  
A1D81 N6  N5   sing Y N 40  
A1D81 C18 C19  sing N N 41  
A1D81 C21 N5   sing N N 42  
A1D81 C19 N4   sing Y N 43  
A1D81 N5  C20  sing Y N 44  
A1D81 N4  C20  doub Y N 45  
A1D81 N1  H1   sing N N 46  
A1D81 C6  H2   sing N N 47  
A1D81 C10 H3   sing N N 48  
A1D81 C17 H4   sing N N 49  
A1D81 C20 H5   sing N N 50  
A1D81 C21 H6   sing N N 51  
A1D81 C21 H7   sing N N 52  
A1D81 C21 H8   sing N N 53  
A1D81 C22 H9   sing N N 54  
A1D81 C24 H10  sing N N 55  
A1D81 C24 H11  sing N N 56  
A1D81 C26 H12  sing N N 57  
A1D81 C26 H13  sing N N 58  
A1D81 C26 H14  sing N N 59  
A1D81 C3  H15  sing N N 60  
A1D81 C11 H16  sing N N 61  
A1D81 C11 H17  sing N N 62  
A1D81 C14 H18  sing N N 63  
A1D81 C18 H19  sing N N 64  
A1D81 C18 H20  sing N N 65  
A1D81 C23 H21  sing N N 66  
A1D81 C23 H22  sing N N 67  
A1D81 C25 H23  sing N N 68  
A1D81 C27 H24  sing N N 69  
A1D81 C27 H25  sing N N 70  
A1D81 C27 H26  sing N N 71  
ALA   N   CA   sing N N 72  
ALA   N   H    sing N N 73  
ALA   N   H2   sing N N 74  
ALA   CA  C    sing N N 75  
ALA   CA  CB   sing N N 76  
ALA   CA  HA   sing N N 77  
ALA   C   O    doub N N 78  
ALA   C   OXT  sing N N 79  
ALA   CB  HB1  sing N N 80  
ALA   CB  HB2  sing N N 81  
ALA   CB  HB3  sing N N 82  
ALA   OXT HXT  sing N N 83  
ARG   N   CA   sing N N 84  
ARG   N   H    sing N N 85  
ARG   N   H2   sing N N 86  
ARG   CA  C    sing N N 87  
ARG   CA  CB   sing N N 88  
ARG   CA  HA   sing N N 89  
ARG   C   O    doub N N 90  
ARG   C   OXT  sing N N 91  
ARG   CB  CG   sing N N 92  
ARG   CB  HB2  sing N N 93  
ARG   CB  HB3  sing N N 94  
ARG   CG  CD   sing N N 95  
ARG   CG  HG2  sing N N 96  
ARG   CG  HG3  sing N N 97  
ARG   CD  NE   sing N N 98  
ARG   CD  HD2  sing N N 99  
ARG   CD  HD3  sing N N 100 
ARG   NE  CZ   sing N N 101 
ARG   NE  HE   sing N N 102 
ARG   CZ  NH1  sing N N 103 
ARG   CZ  NH2  doub N N 104 
ARG   NH1 HH11 sing N N 105 
ARG   NH1 HH12 sing N N 106 
ARG   NH2 HH21 sing N N 107 
ARG   NH2 HH22 sing N N 108 
ARG   OXT HXT  sing N N 109 
ASN   N   CA   sing N N 110 
ASN   N   H    sing N N 111 
ASN   N   H2   sing N N 112 
ASN   CA  C    sing N N 113 
ASN   CA  CB   sing N N 114 
ASN   CA  HA   sing N N 115 
ASN   C   O    doub N N 116 
ASN   C   OXT  sing N N 117 
ASN   CB  CG   sing N N 118 
ASN   CB  HB2  sing N N 119 
ASN   CB  HB3  sing N N 120 
ASN   CG  OD1  doub N N 121 
ASN   CG  ND2  sing N N 122 
ASN   ND2 HD21 sing N N 123 
ASN   ND2 HD22 sing N N 124 
ASN   OXT HXT  sing N N 125 
ASP   N   CA   sing N N 126 
ASP   N   H    sing N N 127 
ASP   N   H2   sing N N 128 
ASP   CA  C    sing N N 129 
ASP   CA  CB   sing N N 130 
ASP   CA  HA   sing N N 131 
ASP   C   O    doub N N 132 
ASP   C   OXT  sing N N 133 
ASP   CB  CG   sing N N 134 
ASP   CB  HB2  sing N N 135 
ASP   CB  HB3  sing N N 136 
ASP   CG  OD1  doub N N 137 
ASP   CG  OD2  sing N N 138 
ASP   OD2 HD2  sing N N 139 
ASP   OXT HXT  sing N N 140 
CYS   N   CA   sing N N 141 
CYS   N   H    sing N N 142 
CYS   N   H2   sing N N 143 
CYS   CA  C    sing N N 144 
CYS   CA  CB   sing N N 145 
CYS   CA  HA   sing N N 146 
CYS   C   O    doub N N 147 
CYS   C   OXT  sing N N 148 
CYS   CB  SG   sing N N 149 
CYS   CB  HB2  sing N N 150 
CYS   CB  HB3  sing N N 151 
CYS   SG  HG   sing N N 152 
CYS   OXT HXT  sing N N 153 
GLN   N   CA   sing N N 154 
GLN   N   H    sing N N 155 
GLN   N   H2   sing N N 156 
GLN   CA  C    sing N N 157 
GLN   CA  CB   sing N N 158 
GLN   CA  HA   sing N N 159 
GLN   C   O    doub N N 160 
GLN   C   OXT  sing N N 161 
GLN   CB  CG   sing N N 162 
GLN   CB  HB2  sing N N 163 
GLN   CB  HB3  sing N N 164 
GLN   CG  CD   sing N N 165 
GLN   CG  HG2  sing N N 166 
GLN   CG  HG3  sing N N 167 
GLN   CD  OE1  doub N N 168 
GLN   CD  NE2  sing N N 169 
GLN   NE2 HE21 sing N N 170 
GLN   NE2 HE22 sing N N 171 
GLN   OXT HXT  sing N N 172 
GLU   N   CA   sing N N 173 
GLU   N   H    sing N N 174 
GLU   N   H2   sing N N 175 
GLU   CA  C    sing N N 176 
GLU   CA  CB   sing N N 177 
GLU   CA  HA   sing N N 178 
GLU   C   O    doub N N 179 
GLU   C   OXT  sing N N 180 
GLU   CB  CG   sing N N 181 
GLU   CB  HB2  sing N N 182 
GLU   CB  HB3  sing N N 183 
GLU   CG  CD   sing N N 184 
GLU   CG  HG2  sing N N 185 
GLU   CG  HG3  sing N N 186 
GLU   CD  OE1  doub N N 187 
GLU   CD  OE2  sing N N 188 
GLU   OE2 HE2  sing N N 189 
GLU   OXT HXT  sing N N 190 
GLY   N   CA   sing N N 191 
GLY   N   H    sing N N 192 
GLY   N   H2   sing N N 193 
GLY   CA  C    sing N N 194 
GLY   CA  HA2  sing N N 195 
GLY   CA  HA3  sing N N 196 
GLY   C   O    doub N N 197 
GLY   C   OXT  sing N N 198 
GLY   OXT HXT  sing N N 199 
HIS   N   CA   sing N N 200 
HIS   N   H    sing N N 201 
HIS   N   H2   sing N N 202 
HIS   CA  C    sing N N 203 
HIS   CA  CB   sing N N 204 
HIS   CA  HA   sing N N 205 
HIS   C   O    doub N N 206 
HIS   C   OXT  sing N N 207 
HIS   CB  CG   sing N N 208 
HIS   CB  HB2  sing N N 209 
HIS   CB  HB3  sing N N 210 
HIS   CG  ND1  sing Y N 211 
HIS   CG  CD2  doub Y N 212 
HIS   ND1 CE1  doub Y N 213 
HIS   ND1 HD1  sing N N 214 
HIS   CD2 NE2  sing Y N 215 
HIS   CD2 HD2  sing N N 216 
HIS   CE1 NE2  sing Y N 217 
HIS   CE1 HE1  sing N N 218 
HIS   NE2 HE2  sing N N 219 
HIS   OXT HXT  sing N N 220 
HOH   O   H1   sing N N 221 
HOH   O   H2   sing N N 222 
ILE   N   CA   sing N N 223 
ILE   N   H    sing N N 224 
ILE   N   H2   sing N N 225 
ILE   CA  C    sing N N 226 
ILE   CA  CB   sing N N 227 
ILE   CA  HA   sing N N 228 
ILE   C   O    doub N N 229 
ILE   C   OXT  sing N N 230 
ILE   CB  CG1  sing N N 231 
ILE   CB  CG2  sing N N 232 
ILE   CB  HB   sing N N 233 
ILE   CG1 CD1  sing N N 234 
ILE   CG1 HG12 sing N N 235 
ILE   CG1 HG13 sing N N 236 
ILE   CG2 HG21 sing N N 237 
ILE   CG2 HG22 sing N N 238 
ILE   CG2 HG23 sing N N 239 
ILE   CD1 HD11 sing N N 240 
ILE   CD1 HD12 sing N N 241 
ILE   CD1 HD13 sing N N 242 
ILE   OXT HXT  sing N N 243 
LEU   N   CA   sing N N 244 
LEU   N   H    sing N N 245 
LEU   N   H2   sing N N 246 
LEU   CA  C    sing N N 247 
LEU   CA  CB   sing N N 248 
LEU   CA  HA   sing N N 249 
LEU   C   O    doub N N 250 
LEU   C   OXT  sing N N 251 
LEU   CB  CG   sing N N 252 
LEU   CB  HB2  sing N N 253 
LEU   CB  HB3  sing N N 254 
LEU   CG  CD1  sing N N 255 
LEU   CG  CD2  sing N N 256 
LEU   CG  HG   sing N N 257 
LEU   CD1 HD11 sing N N 258 
LEU   CD1 HD12 sing N N 259 
LEU   CD1 HD13 sing N N 260 
LEU   CD2 HD21 sing N N 261 
LEU   CD2 HD22 sing N N 262 
LEU   CD2 HD23 sing N N 263 
LEU   OXT HXT  sing N N 264 
LYS   N   CA   sing N N 265 
LYS   N   H    sing N N 266 
LYS   N   H2   sing N N 267 
LYS   CA  C    sing N N 268 
LYS   CA  CB   sing N N 269 
LYS   CA  HA   sing N N 270 
LYS   C   O    doub N N 271 
LYS   C   OXT  sing N N 272 
LYS   CB  CG   sing N N 273 
LYS   CB  HB2  sing N N 274 
LYS   CB  HB3  sing N N 275 
LYS   CG  CD   sing N N 276 
LYS   CG  HG2  sing N N 277 
LYS   CG  HG3  sing N N 278 
LYS   CD  CE   sing N N 279 
LYS   CD  HD2  sing N N 280 
LYS   CD  HD3  sing N N 281 
LYS   CE  NZ   sing N N 282 
LYS   CE  HE2  sing N N 283 
LYS   CE  HE3  sing N N 284 
LYS   NZ  HZ1  sing N N 285 
LYS   NZ  HZ2  sing N N 286 
LYS   NZ  HZ3  sing N N 287 
LYS   OXT HXT  sing N N 288 
MET   N   CA   sing N N 289 
MET   N   H    sing N N 290 
MET   N   H2   sing N N 291 
MET   CA  C    sing N N 292 
MET   CA  CB   sing N N 293 
MET   CA  HA   sing N N 294 
MET   C   O    doub N N 295 
MET   C   OXT  sing N N 296 
MET   CB  CG   sing N N 297 
MET   CB  HB2  sing N N 298 
MET   CB  HB3  sing N N 299 
MET   CG  SD   sing N N 300 
MET   CG  HG2  sing N N 301 
MET   CG  HG3  sing N N 302 
MET   SD  CE   sing N N 303 
MET   CE  HE1  sing N N 304 
MET   CE  HE2  sing N N 305 
MET   CE  HE3  sing N N 306 
MET   OXT HXT  sing N N 307 
PHE   N   CA   sing N N 308 
PHE   N   H    sing N N 309 
PHE   N   H2   sing N N 310 
PHE   CA  C    sing N N 311 
PHE   CA  CB   sing N N 312 
PHE   CA  HA   sing N N 313 
PHE   C   O    doub N N 314 
PHE   C   OXT  sing N N 315 
PHE   CB  CG   sing N N 316 
PHE   CB  HB2  sing N N 317 
PHE   CB  HB3  sing N N 318 
PHE   CG  CD1  doub Y N 319 
PHE   CG  CD2  sing Y N 320 
PHE   CD1 CE1  sing Y N 321 
PHE   CD1 HD1  sing N N 322 
PHE   CD2 CE2  doub Y N 323 
PHE   CD2 HD2  sing N N 324 
PHE   CE1 CZ   doub Y N 325 
PHE   CE1 HE1  sing N N 326 
PHE   CE2 CZ   sing Y N 327 
PHE   CE2 HE2  sing N N 328 
PHE   CZ  HZ   sing N N 329 
PHE   OXT HXT  sing N N 330 
PRO   N   CA   sing N N 331 
PRO   N   CD   sing N N 332 
PRO   N   H    sing N N 333 
PRO   CA  C    sing N N 334 
PRO   CA  CB   sing N N 335 
PRO   CA  HA   sing N N 336 
PRO   C   O    doub N N 337 
PRO   C   OXT  sing N N 338 
PRO   CB  CG   sing N N 339 
PRO   CB  HB2  sing N N 340 
PRO   CB  HB3  sing N N 341 
PRO   CG  CD   sing N N 342 
PRO   CG  HG2  sing N N 343 
PRO   CG  HG3  sing N N 344 
PRO   CD  HD2  sing N N 345 
PRO   CD  HD3  sing N N 346 
PRO   OXT HXT  sing N N 347 
SER   N   CA   sing N N 348 
SER   N   H    sing N N 349 
SER   N   H2   sing N N 350 
SER   CA  C    sing N N 351 
SER   CA  CB   sing N N 352 
SER   CA  HA   sing N N 353 
SER   C   O    doub N N 354 
SER   C   OXT  sing N N 355 
SER   CB  OG   sing N N 356 
SER   CB  HB2  sing N N 357 
SER   CB  HB3  sing N N 358 
SER   OG  HG   sing N N 359 
SER   OXT HXT  sing N N 360 
THR   N   CA   sing N N 361 
THR   N   H    sing N N 362 
THR   N   H2   sing N N 363 
THR   CA  C    sing N N 364 
THR   CA  CB   sing N N 365 
THR   CA  HA   sing N N 366 
THR   C   O    doub N N 367 
THR   C   OXT  sing N N 368 
THR   CB  OG1  sing N N 369 
THR   CB  CG2  sing N N 370 
THR   CB  HB   sing N N 371 
THR   OG1 HG1  sing N N 372 
THR   CG2 HG21 sing N N 373 
THR   CG2 HG22 sing N N 374 
THR   CG2 HG23 sing N N 375 
THR   OXT HXT  sing N N 376 
TRP   N   CA   sing N N 377 
TRP   N   H    sing N N 378 
TRP   N   H2   sing N N 379 
TRP   CA  C    sing N N 380 
TRP   CA  CB   sing N N 381 
TRP   CA  HA   sing N N 382 
TRP   C   O    doub N N 383 
TRP   C   OXT  sing N N 384 
TRP   CB  CG   sing N N 385 
TRP   CB  HB2  sing N N 386 
TRP   CB  HB3  sing N N 387 
TRP   CG  CD1  doub Y N 388 
TRP   CG  CD2  sing Y N 389 
TRP   CD1 NE1  sing Y N 390 
TRP   CD1 HD1  sing N N 391 
TRP   CD2 CE2  doub Y N 392 
TRP   CD2 CE3  sing Y N 393 
TRP   NE1 CE2  sing Y N 394 
TRP   NE1 HE1  sing N N 395 
TRP   CE2 CZ2  sing Y N 396 
TRP   CE3 CZ3  doub Y N 397 
TRP   CE3 HE3  sing N N 398 
TRP   CZ2 CH2  doub Y N 399 
TRP   CZ2 HZ2  sing N N 400 
TRP   CZ3 CH2  sing Y N 401 
TRP   CZ3 HZ3  sing N N 402 
TRP   CH2 HH2  sing N N 403 
TRP   OXT HXT  sing N N 404 
TYR   N   CA   sing N N 405 
TYR   N   H    sing N N 406 
TYR   N   H2   sing N N 407 
TYR   CA  C    sing N N 408 
TYR   CA  CB   sing N N 409 
TYR   CA  HA   sing N N 410 
TYR   C   O    doub N N 411 
TYR   C   OXT  sing N N 412 
TYR   CB  CG   sing N N 413 
TYR   CB  HB2  sing N N 414 
TYR   CB  HB3  sing N N 415 
TYR   CG  CD1  doub Y N 416 
TYR   CG  CD2  sing Y N 417 
TYR   CD1 CE1  sing Y N 418 
TYR   CD1 HD1  sing N N 419 
TYR   CD2 CE2  doub Y N 420 
TYR   CD2 HD2  sing N N 421 
TYR   CE1 CZ   doub Y N 422 
TYR   CE1 HE1  sing N N 423 
TYR   CE2 CZ   sing Y N 424 
TYR   CE2 HE2  sing N N 425 
TYR   CZ  OH   sing N N 426 
TYR   OH  HH   sing N N 427 
TYR   OXT HXT  sing N N 428 
VAL   N   CA   sing N N 429 
VAL   N   H    sing N N 430 
VAL   N   H2   sing N N 431 
VAL   CA  C    sing N N 432 
VAL   CA  CB   sing N N 433 
VAL   CA  HA   sing N N 434 
VAL   C   O    doub N N 435 
VAL   C   OXT  sing N N 436 
VAL   CB  CG1  sing N N 437 
VAL   CB  CG2  sing N N 438 
VAL   CB  HB   sing N N 439 
VAL   CG1 HG11 sing N N 440 
VAL   CG1 HG12 sing N N 441 
VAL   CG1 HG13 sing N N 442 
VAL   CG2 HG21 sing N N 443 
VAL   CG2 HG22 sing N N 444 
VAL   CG2 HG23 sing N N 445 
VAL   OXT HXT  sing N N 446 
# 
_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   8HEF 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZUC 
_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]   0.018035 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005877 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010059 
_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]   0.017966 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 28.905  -8.659  26.793  1.00 67.21 ? 1   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 30.248  -8.018  26.878  1.00 58.49 ? 1   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 30.453  -7.079  25.689  1.00 50.16 ? 1   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 30.677  -7.532  24.557  1.00 36.26 ? 1   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 31.350  -9.041  26.959  1.00 54.38 ? 1   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 31.095  -9.972  27.992  1.00 57.83 ? 1   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 30.422  -5.773  25.995  1.00 46.69 ? 2   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 30.249  -4.722  25.002  1.00 48.21 ? 2   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 28.761  -4.490  24.735  1.00 45.40 ? 2   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 27.963  -5.393  24.985  1.00 50.30 ? 2   GLY   A O   1 
ATOM   11   N  N   . PHE   A 1 3   ? 28.392  -3.291  24.246  1.00 41.03 ? 3   PHE   A N   1 
ATOM   12   C  CA  . PHE   A 1 3   ? 26.982  -2.958  24.059  1.00 34.45 ? 3   PHE   A CA  1 
ATOM   13   C  C   . PHE   A 1 3   ? 26.777  -2.002  22.885  1.00 32.66 ? 3   PHE   A C   1 
ATOM   14   O  O   . PHE   A 1 3   ? 27.215  -0.864  22.915  1.00 37.97 ? 3   PHE   A O   1 
ATOM   15   C  CB  . PHE   A 1 3   ? 26.379  -2.380  25.343  1.00 28.89 ? 3   PHE   A CB  1 
ATOM   16   C  CG  . PHE   A 1 3   ? 24.900  -2.610  25.385  1.00 23.77 ? 3   PHE   A CG  1 
ATOM   17   C  CD1 . PHE   A 1 3   ? 24.397  -3.856  25.678  1.00 21.96 ? 3   PHE   A CD1 1 
ATOM   18   C  CD2 . PHE   A 1 3   ? 24.024  -1.608  25.012  1.00 21.63 ? 3   PHE   A CD2 1 
ATOM   19   C  CE1 . PHE   A 1 3   ? 23.038  -4.103  25.611  1.00 22.38 ? 3   PHE   A CE1 1 
ATOM   20   C  CE2 . PHE   A 1 3   ? 22.660  -1.845  24.982  1.00 22.27 ? 3   PHE   A CE2 1 
ATOM   21   C  CZ  . PHE   A 1 3   ? 22.168  -3.095  25.268  1.00 21.61 ? 3   PHE   A CZ  1 
ATOM   22   N  N   . ARG   A 1 4   ? 26.096  -2.500  21.851  1.00 29.82 ? 4   ARG   A N   1 
ATOM   23   C  CA  . ARG   A 1 4   ? 25.843  -1.776  20.611  1.00 26.64 ? 4   ARG   A CA  1 
ATOM   24   C  C   . ARG   A 1 4   ? 24.416  -2.065  20.141  1.00 21.37 ? 4   ARG   A C   1 
ATOM   25   O  O   . ARG   A 1 4   ? 23.843  -3.075  20.508  1.00 17.52 ? 4   ARG   A O   1 
ATOM   26   C  CB  . ARG   A 1 4   ? 26.776  -2.273  19.499  1.00 29.40 ? 4   ARG   A CB  1 
ATOM   27   C  CG  . ARG   A 1 4   ? 28.259  -2.051  19.747  1.00 29.91 ? 4   ARG   A CG  1 
ATOM   28   C  CD  . ARG   A 1 4   ? 29.036  -2.149  18.457  1.00 27.40 ? 4   ARG   A CD  1 
ATOM   29   N  NE  . ARG   A 1 4   ? 30.378  -1.578  18.567  1.00 27.53 ? 4   ARG   A NE  1 
ATOM   30   C  CZ  . ARG   A 1 4   ? 30.793  -0.485  17.925  1.00 29.18 ? 4   ARG   A CZ  1 
ATOM   31   N  NH1 . ARG   A 1 4   ? 29.919  0.307   17.320  1.00 29.49 ? 4   ARG   A NH1 1 
ATOM   32   N  NH2 . ARG   A 1 4   ? 32.080  -0.166  17.906  1.00 28.87 ? 4   ARG   A NH2 1 
ATOM   33   N  N   . LYS   A 1 5   ? 23.885  -1.203  19.280  1.00 20.65 ? 5   LYS   A N   1 
ATOM   34   C  CA  . LYS   A 1 5   ? 22.654  -1.487  18.572  1.00 24.30 ? 5   LYS   A CA  1 
ATOM   35   C  C   . LYS   A 1 5   ? 22.885  -2.653  17.615  1.00 21.36 ? 5   LYS   A C   1 
ATOM   36   O  O   . LYS   A 1 5   ? 23.682  -2.587  16.700  1.00 30.85 ? 5   LYS   A O   1 
ATOM   37   C  CB  . LYS   A 1 5   ? 22.148  -0.241  17.848  1.00 27.60 ? 5   LYS   A CB  1 
ATOM   38   C  CG  . LYS   A 1 5   ? 21.098  0.508   18.644  1.00 34.11 ? 5   LYS   A CG  1 
ATOM   39   C  CD  . LYS   A 1 5   ? 20.940  1.959   18.287  1.00 38.98 ? 5   LYS   A CD  1 
ATOM   40   C  CE  . LYS   A 1 5   ? 20.163  2.677   19.370  1.00 40.03 ? 5   LYS   A CE  1 
ATOM   41   N  NZ  . LYS   A 1 5   ? 19.923  4.084   18.994  1.00 43.79 ? 5   LYS   A NZ  1 
ATOM   42   N  N   . MET   A 1 6   ? 22.175  -3.720  17.860  1.00 18.87 ? 6   MET   A N   1 
ATOM   43   C  CA  . MET   A 1 6   ? 22.321  -4.964  17.143  1.00 19.55 ? 6   MET   A CA  1 
ATOM   44   C  C   . MET   A 1 6   ? 21.008  -5.233  16.412  1.00 17.66 ? 6   MET   A C   1 
ATOM   45   O  O   . MET   A 1 6   ? 19.942  -5.258  17.042  1.00 15.36 ? 6   MET   A O   1 
ATOM   46   C  CB  . MET   A 1 6   ? 22.588  -6.065  18.175  1.00 22.42 ? 6   MET   A CB  1 
ATOM   47   C  CG  . MET   A 1 6   ? 22.932  -7.420  17.610  1.00 29.59 ? 6   MET   A CG  1 
ATOM   48   S  SD  . MET   A 1 6   ? 23.844  -8.476  18.814  1.00 37.85 ? 6   MET   A SD  1 
ATOM   49   C  CE  . MET   A 1 6   ? 25.051  -7.344  19.487  1.00 30.70 ? 6   MET   A CE  1 
ATOM   50   N  N   . ALA   A 1 7   ? 21.101  -5.438  15.091  1.00 13.68 ? 7   ALA   A N   1 
ATOM   51   C  CA  . ALA   A 1 7   ? 19.966  -5.853  14.286  1.00 12.17 ? 7   ALA   A CA  1 
ATOM   52   C  C   . ALA   A 1 7   ? 19.876  -7.376  14.229  1.00 11.63 ? 7   ALA   A C   1 
ATOM   53   O  O   . ALA   A 1 7   ? 20.858  -8.068  14.456  1.00 14.04 ? 7   ALA   A O   1 
ATOM   54   C  CB  . ALA   A 1 7   ? 20.124  -5.268  12.904  1.00 11.15 ? 7   ALA   A CB  1 
ATOM   55   N  N   . PHE   A 1 8   ? 18.730  -7.883  13.821  1.00 10.94 ? 8   PHE   A N   1 
ATOM   56   C  CA  . PHE   A 1 8   ? 18.588  -9.273  13.447  1.00 11.60 ? 8   PHE   A CA  1 
ATOM   57   C  C   . PHE   A 1 8   ? 19.320  -9.539  12.140  1.00 10.33 ? 8   PHE   A C   1 
ATOM   58   O  O   . PHE   A 1 8   ? 19.365  -8.691  11.276  1.00 10.47 ? 8   PHE   A O   1 
ATOM   59   C  CB  . PHE   A 1 8   ? 17.113  -9.664  13.353  1.00 12.47 ? 8   PHE   A CB  1 
ATOM   60   C  CG  . PHE   A 1 8   ? 16.474  -9.823  14.715  1.00 14.41 ? 8   PHE   A CG  1 
ATOM   61   C  CD1 . PHE   A 1 8   ? 16.766  -10.917 15.514  1.00 15.20 ? 8   PHE   A CD1 1 
ATOM   62   C  CD2 . PHE   A 1 8   ? 15.636  -8.848  15.220  1.00 15.06 ? 8   PHE   A CD2 1 
ATOM   63   C  CE1 . PHE   A 1 8   ? 16.223  -11.027 16.788  1.00 16.93 ? 8   PHE   A CE1 1 
ATOM   64   C  CE2 . PHE   A 1 8   ? 15.074  -8.975  16.482  1.00 15.78 ? 8   PHE   A CE2 1 
ATOM   65   C  CZ  . PHE   A 1 8   ? 15.379  -10.054 17.266  1.00 15.97 ? 8   PHE   A CZ  1 
ATOM   66   N  N   . PRO   A 1 9   ? 19.870  -10.746 11.923  1.00 11.26 ? 9   PRO   A N   1 
ATOM   67   C  CA  . PRO   A 1 9   ? 20.420  -11.102 10.612  1.00 10.62 ? 9   PRO   A CA  1 
ATOM   68   C  C   . PRO   A 1 9   ? 19.310  -10.952 9.582   1.00 10.12 ? 9   PRO   A C   1 
ATOM   69   O  O   . PRO   A 1 9   ? 18.183  -11.405 9.825   1.00 10.06 ? 9   PRO   A O   1 
ATOM   70   C  CB  . PRO   A 1 9   ? 20.838  -12.569 10.778  1.00 11.16 ? 9   PRO   A CB  1 
ATOM   71   C  CG  . PRO   A 1 9   ? 21.022  -12.739 12.284  1.00 11.01 ? 9   PRO   A CG  1 
ATOM   72   C  CD  . PRO   A 1 9   ? 19.936  -11.858 12.883  1.00 11.21 ? 9   PRO   A CD  1 
ATOM   73   N  N   . SER   A 1 10  ? 19.637  -10.349 8.436   1.00 9.59  ? 10  SER   A N   1 
ATOM   74   C  CA  . SER   A 1 10  ? 18.640  -9.874  7.487   1.00 9.84  ? 10  SER   A CA  1 
ATOM   75   C  C   . SER   A 1 10  ? 18.356  -10.848 6.337   1.00 10.22 ? 10  SER   A C   1 
ATOM   76   O  O   . SER   A 1 10  ? 17.508  -10.576 5.488   1.00 9.27  ? 10  SER   A O   1 
ATOM   77   C  CB  . SER   A 1 10  ? 19.089  -8.544  6.949   1.00 9.87  ? 10  SER   A CB  1 
ATOM   78   O  OG  . SER   A 1 10  ? 20.373  -8.637  6.340   1.00 10.17 ? 10  SER   A OG  1 
ATOM   79   N  N   . GLY   A 1 11  ? 19.064  -11.980 6.293   1.00 10.48 ? 11  GLY   A N   1 
ATOM   80   C  CA  . GLY   A 1 11  ? 19.022  -12.870 5.134   1.00 10.26 ? 11  GLY   A CA  1 
ATOM   81   C  C   . GLY   A 1 11  ? 17.608  -13.341 4.801   1.00 10.29 ? 11  GLY   A C   1 
ATOM   82   O  O   . GLY   A 1 11  ? 17.208  -13.398 3.638   1.00 9.59  ? 11  GLY   A O   1 
ATOM   83   N  N   . LYS   A 1 12  ? 16.836  -13.681 5.824   1.00 11.29 ? 12  LYS   A N   1 
ATOM   84   C  CA  . LYS   A 1 12  ? 15.469  -14.163 5.602   1.00 12.92 ? 12  LYS   A CA  1 
ATOM   85   C  C   . LYS   A 1 12  ? 14.593  -13.115 4.933   1.00 12.13 ? 12  LYS   A C   1 
ATOM   86   O  O   . LYS   A 1 12  ? 13.648  -13.469 4.226   1.00 14.86 ? 12  LYS   A O   1 
ATOM   87   C  CB  . LYS   A 1 12  ? 14.809  -14.625 6.897   1.00 14.36 ? 12  LYS   A CB  1 
ATOM   88   C  CG  . LYS   A 1 12  ? 15.374  -15.913 7.469   1.00 17.17 ? 12  LYS   A CG  1 
ATOM   89   C  CD  . LYS   A 1 12  ? 14.633  -16.315 8.741   1.00 19.56 ? 12  LYS   A CD  1 
ATOM   90   C  CE  . LYS   A 1 12  ? 15.428  -17.202 9.667   1.00 23.63 ? 12  LYS   A CE  1 
ATOM   91   N  NZ  . LYS   A 1 12  ? 15.932  -18.377 8.924   1.00 26.82 ? 12  LYS   A NZ  1 
ATOM   92   N  N   . VAL   A 1 13  ? 14.914  -11.831 5.116   1.00 12.32 ? 13  VAL   A N   1 
ATOM   93   C  CA  . VAL   A 1 13  ? 14.139  -10.759 4.503   1.00 12.17 ? 13  VAL   A CA  1 
ATOM   94   C  C   . VAL   A 1 13  ? 14.721  -10.395 3.130   1.00 12.40 ? 13  VAL   A C   1 
ATOM   95   O  O   . VAL   A 1 13  ? 13.962  -10.049 2.219   1.00 10.56 ? 13  VAL   A O   1 
ATOM   96   C  CB  . VAL   A 1 13  ? 14.051  -9.546  5.447   1.00 12.10 ? 13  VAL   A CB  1 
ATOM   97   C  CG1 . VAL   A 1 13  ? 13.300  -8.385  4.805   1.00 12.56 ? 13  VAL   A CG1 1 
ATOM   98   C  CG2 . VAL   A 1 13  ? 13.395  -9.923  6.768   1.00 12.11 ? 13  VAL   A CG2 1 
ATOM   99   N  N   . GLU   A 1 14  ? 16.066  -10.473 2.972   1.00 12.23 ? 14  GLU   A N   1 
ATOM   100  C  CA  . GLU   A 1 14  ? 16.711  -10.114 1.716   1.00 11.73 ? 14  GLU   A CA  1 
ATOM   101  C  C   . GLU   A 1 14  ? 16.122  -10.901 0.539   1.00 12.59 ? 14  GLU   A C   1 
ATOM   102  O  O   . GLU   A 1 14  ? 15.912  -10.357 -0.545  1.00 11.22 ? 14  GLU   A O   1 
ATOM   103  C  CB  . GLU   A 1 14  ? 18.218  -10.396 1.760   1.00 11.95 ? 14  GLU   A CB  1 
ATOM   104  C  CG  . GLU   A 1 14  ? 18.996  -9.427  2.638   1.00 12.35 ? 14  GLU   A CG  1 
ATOM   105  C  CD  . GLU   A 1 14  ? 20.420  -9.875  2.918   1.00 11.52 ? 14  GLU   A CD  1 
ATOM   106  O  OE1 . GLU   A 1 14  ? 21.072  -10.143 1.939   1.00 11.27 ? 14  GLU   A OE1 1 
ATOM   107  O  OE2 . GLU   A 1 14  ? 20.852  -9.929  4.105   1.00 10.42 ? 14  GLU   A OE2 1 
ATOM   108  N  N   . GLY   A 1 15  ? 15.874  -12.194 0.763   1.00 13.48 ? 15  GLY   A N   1 
ATOM   109  C  CA  . GLY   A 1 15  ? 15.341  -13.061 -0.266  1.00 14.99 ? 15  GLY   A CA  1 
ATOM   110  C  C   . GLY   A 1 15  ? 13.900  -12.738 -0.663  1.00 14.59 ? 15  GLY   A C   1 
ATOM   111  O  O   . GLY   A 1 15  ? 13.378  -13.374 -1.576  1.00 15.27 ? 15  GLY   A O   1 
ATOM   112  N  N   . CYS   A 1 16  ? 13.271  -11.755 -0.008  1.00 14.92 ? 16  CYS   A N   1 
ATOM   113  C  CA  . CYS   A 1 16  ? 11.883  -11.401 -0.303  1.00 14.35 ? 16  CYS   A CA  1 
ATOM   114  C  C   . CYS   A 1 16  ? 11.779  -10.042 -0.989  1.00 13.48 ? 16  CYS   A C   1 
ATOM   115  O  O   . CYS   A 1 16  ? 10.686  -9.638  -1.401  1.00 13.51 ? 16  CYS   A O   1 
ATOM   116  C  CB  . CYS   A 1 16  ? 11.032  -11.379 0.963   1.00 14.49 ? 16  CYS   A CB  1 
ATOM   117  S  SG  . CYS   A 1 16  ? 10.975  -12.954 1.860   1.00 16.74 ? 16  CYS   A SG  1 
ATOM   118  N  N   . MET   A 1 17  ? 12.893  -9.324  -1.141  1.00 13.00 ? 17  MET   A N   1 
ATOM   119  C  CA  . MET   A 1 17  ? 12.794  -7.959  -1.644  1.00 12.84 ? 17  MET   A CA  1 
ATOM   120  C  C   . MET   A 1 17  ? 12.749  -7.975  -3.170  1.00 12.60 ? 17  MET   A C   1 
ATOM   121  O  O   . MET   A 1 17  ? 13.518  -8.670  -3.792  1.00 11.72 ? 17  MET   A O   1 
ATOM   122  C  CB  . MET   A 1 17  ? 13.958  -7.084  -1.174  1.00 13.00 ? 17  MET   A CB  1 
ATOM   123  C  CG  . MET   A 1 17  ? 14.032  -6.945  0.339   1.00 12.85 ? 17  MET   A CG  1 
ATOM   124  S  SD  . MET   A 1 17  ? 12.443  -6.480  1.092   1.00 13.58 ? 17  MET   A SD  1 
ATOM   125  C  CE  . MET   A 1 17  ? 12.134  -4.953  0.210   1.00 13.06 ? 17  MET   A CE  1 
ATOM   126  N  N   . VAL   A 1 18  ? 11.833  -7.193  -3.751  1.00 11.92 ? 18  VAL   A N   1 
ATOM   127  C  CA  . VAL   A 1 18  ? 11.690  -7.054  -5.192  1.00 12.73 ? 18  VAL   A CA  1 
ATOM   128  C  C   . VAL   A 1 18  ? 11.495  -5.573  -5.510  1.00 13.14 ? 18  VAL   A C   1 
ATOM   129  O  O   . VAL   A 1 18  ? 11.347  -4.737  -4.622  1.00 12.59 ? 18  VAL   A O   1 
ATOM   130  C  CB  . VAL   A 1 18  ? 10.513  -7.897  -5.741  1.00 12.73 ? 18  VAL   A CB  1 
ATOM   131  C  CG1 . VAL   A 1 18  ? 10.751  -9.380  -5.525  1.00 12.50 ? 18  VAL   A CG1 1 
ATOM   132  C  CG2 . VAL   A 1 18  ? 9.179   -7.473  -5.133  1.00 12.40 ? 18  VAL   A CG2 1 
ATOM   133  N  N   . GLN   A 1 19  ? 11.478  -5.267  -6.805  1.00 14.11 ? 19  GLN   A N   1 
ATOM   134  C  CA  . GLN   A 1 19  ? 11.229  -3.936  -7.297  1.00 14.71 ? 19  GLN   A CA  1 
ATOM   135  C  C   . GLN   A 1 19  ? 9.857   -3.944  -7.955  1.00 15.23 ? 19  GLN   A C   1 
ATOM   136  O  O   . GLN   A 1 19  ? 9.515   -4.890  -8.651  1.00 15.58 ? 19  GLN   A O   1 
ATOM   137  C  CB  . GLN   A 1 19  ? 12.344  -3.551  -8.267  1.00 16.55 ? 19  GLN   A CB  1 
ATOM   138  C  CG  . GLN   A 1 19  ? 12.255  -2.120  -8.760  1.00 17.97 ? 19  GLN   A CG  1 
ATOM   139  C  CD  . GLN   A 1 19  ? 13.393  -1.750  -9.687  1.00 20.11 ? 19  GLN   A CD  1 
ATOM   140  O  OE1 . GLN   A 1 19  ? 14.166  -2.594  -10.123 1.00 24.86 ? 19  GLN   A OE1 1 
ATOM   141  N  NE2 . GLN   A 1 19  ? 13.502  -0.478  -10.010 1.00 21.73 ? 19  GLN   A NE2 1 
ATOM   142  N  N   . VAL   A 1 20  ? 9.074   -2.889  -7.699  1.00 15.34 ? 20  VAL   A N   1 
ATOM   143  C  CA  . VAL   A 1 20  ? 7.768   -2.708  -8.297  1.00 14.30 ? 20  VAL   A CA  1 
ATOM   144  C  C   . VAL   A 1 20  ? 7.759   -1.361  -9.036  1.00 14.99 ? 20  VAL   A C   1 
ATOM   145  O  O   . VAL   A 1 20  ? 8.159   -0.332  -8.509  1.00 14.48 ? 20  VAL   A O   1 
ATOM   146  C  CB  . VAL   A 1 20  ? 6.662   -2.789  -7.230  1.00 14.40 ? 20  VAL   A CB  1 
ATOM   147  C  CG1 . VAL   A 1 20  ? 5.283   -2.646  -7.848  1.00 13.95 ? 20  VAL   A CG1 1 
ATOM   148  C  CG2 . VAL   A 1 20  ? 6.749   -4.052  -6.392  1.00 13.81 ? 20  VAL   A CG2 1 
ATOM   149  N  N   . THR   A 1 21  ? 7.265   -1.386  -10.276 1.00 14.97 ? 21  THR   A N   1 
ATOM   150  C  CA  . THR   A 1 21  ? 7.178   -0.222  -11.127 1.00 16.84 ? 21  THR   A CA  1 
ATOM   151  C  C   . THR   A 1 21  ? 5.762   -0.142  -11.715 1.00 17.23 ? 21  THR   A C   1 
ATOM   152  O  O   . THR   A 1 21  ? 5.150   -1.157  -12.072 1.00 16.12 ? 21  THR   A O   1 
ATOM   153  C  CB  . THR   A 1 21  ? 8.239   -0.244  -12.237 1.00 17.31 ? 21  THR   A CB  1 
ATOM   154  O  OG1 . THR   A 1 21  ? 9.529   -0.436  -11.655 1.00 17.05 ? 21  THR   A OG1 1 
ATOM   155  C  CG2 . THR   A 1 21  ? 8.222   1.036   -13.044 1.00 18.16 ? 21  THR   A CG2 1 
ATOM   156  N  N   . CYS   A 1 22  ? 5.246   1.081   -11.739 1.00 16.79 ? 22  CYS   A N   1 
ATOM   157  C  CA  . CYS   A 1 22  ? 3.961   1.386   -12.341 1.00 19.43 ? 22  CYS   A CA  1 
ATOM   158  C  C   . CYS   A 1 22  ? 4.156   2.674   -13.127 1.00 17.90 ? 22  CYS   A C   1 
ATOM   159  O  O   . CYS   A 1 22  ? 4.315   3.745   -12.560 1.00 16.81 ? 22  CYS   A O   1 
ATOM   160  C  CB  . CYS   A 1 22  ? 2.858   1.487   -11.290 1.00 20.16 ? 22  CYS   A CB  1 
ATOM   161  S  SG  . CYS   A 1 22  ? 1.196   1.652   -11.987 1.00 27.62 ? 22  CYS   A SG  1 
ATOM   162  N  N   . GLY   A 1 23  ? 4.242   2.535   -14.456 1.00 19.33 ? 23  GLY   A N   1 
ATOM   163  C  CA  . GLY   A 1 23  ? 4.608   3.657   -15.306 1.00 18.58 ? 23  GLY   A CA  1 
ATOM   164  C  C   . GLY   A 1 23  ? 6.096   3.913   -15.173 1.00 19.03 ? 23  GLY   A C   1 
ATOM   165  O  O   . GLY   A 1 23  ? 6.884   3.037   -15.499 1.00 22.90 ? 23  GLY   A O   1 
ATOM   166  N  N   . THR   A 1 24  ? 6.465   5.092   -14.660 1.00 20.18 ? 24  THR   A N   1 
ATOM   167  C  CA  . THR   A 1 24  ? 7.837   5.364   -14.268 1.00 20.69 ? 24  THR   A CA  1 
ATOM   168  C  C   . THR   A 1 24  ? 8.006   5.365   -12.746 1.00 20.19 ? 24  THR   A C   1 
ATOM   169  O  O   . THR   A 1 24  ? 9.129   5.382   -12.250 1.00 22.74 ? 24  THR   A O   1 
ATOM   170  C  CB  . THR   A 1 24  ? 8.279   6.713   -14.837 1.00 23.82 ? 24  THR   A CB  1 
ATOM   171  O  OG1 . THR   A 1 24  ? 7.374   7.702   -14.345 1.00 26.95 ? 24  THR   A OG1 1 
ATOM   172  C  CG2 . THR   A 1 24  ? 8.289   6.740   -16.352 1.00 24.64 ? 24  THR   A CG2 1 
ATOM   173  N  N   . THR   A 1 25  ? 6.903   5.372   -11.987 1.00 17.91 ? 25  THR   A N   1 
ATOM   174  C  CA  . THR   A 1 25  ? 7.002   5.347   -10.532 1.00 15.81 ? 25  THR   A CA  1 
ATOM   175  C  C   . THR   A 1 25  ? 7.491   3.974   -10.056 1.00 14.19 ? 25  THR   A C   1 
ATOM   176  O  O   . THR   A 1 25  ? 6.955   2.940   -10.462 1.00 13.99 ? 25  THR   A O   1 
ATOM   177  C  CB  . THR   A 1 25  ? 5.646   5.675   -9.902  1.00 15.08 ? 25  THR   A CB  1 
ATOM   178  O  OG1 . THR   A 1 25  ? 5.186   6.897   -10.491 1.00 13.29 ? 25  THR   A OG1 1 
ATOM   179  C  CG2 . THR   A 1 25  ? 5.745   5.819   -8.395  1.00 14.54 ? 25  THR   A CG2 1 
ATOM   180  N  N   . THR   A 1 26  ? 8.479   3.960   -9.159  1.00 14.09 ? 26  THR   A N   1 
ATOM   181  C  CA  . THR   A 1 26  ? 9.143   2.726   -8.766  1.00 14.57 ? 26  THR   A CA  1 
ATOM   182  C  C   . THR   A 1 26  ? 9.518   2.767   -7.279  1.00 12.86 ? 26  THR   A C   1 
ATOM   183  O  O   . THR   A 1 26  ? 9.777   3.834   -6.735  1.00 12.81 ? 26  THR   A O   1 
ATOM   184  C  CB  . THR   A 1 26  ? 10.363  2.436   -9.669  1.00 16.07 ? 26  THR   A CB  1 
ATOM   185  O  OG1 . THR   A 1 26  ? 10.706  1.057   -9.489  1.00 19.45 ? 26  THR   A OG1 1 
ATOM   186  C  CG2 . THR   A 1 26  ? 11.565  3.317   -9.386  1.00 16.32 ? 26  THR   A CG2 1 
ATOM   187  N  N   . LEU   A 1 27  ? 9.470   1.595   -6.636  1.00 11.71 ? 27  LEU   A N   1 
ATOM   188  C  CA  . LEU   A 1 27  ? 9.832   1.436   -5.241  1.00 12.14 ? 27  LEU   A CA  1 
ATOM   189  C  C   . LEU   A 1 27  ? 10.035  -0.052  -4.936  1.00 12.02 ? 27  LEU   A C   1 
ATOM   190  O  O   . LEU   A 1 27  ? 10.093  -0.888  -5.858  1.00 11.87 ? 27  LEU   A O   1 
ATOM   191  C  CB  . LEU   A 1 27  ? 8.776   2.095   -4.339  1.00 12.21 ? 27  LEU   A CB  1 
ATOM   192  C  CG  . LEU   A 1 27  ? 7.303   1.848   -4.671  1.00 12.86 ? 27  LEU   A CG  1 
ATOM   193  C  CD1 . LEU   A 1 27  ? 6.942   0.355   -4.650  1.00 12.31 ? 27  LEU   A CD1 1 
ATOM   194  C  CD2 . LEU   A 1 27  ? 6.433   2.609   -3.681  1.00 12.67 ? 27  LEU   A CD2 1 
ATOM   195  N  N   . ASN   A 1 28  ? 10.161  -0.362  -3.639  1.00 11.07 ? 28  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 28  ? 10.497  -1.705  -3.188  1.00 11.42 ? 28  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 28  ? 9.226   -2.437  -2.798  1.00 11.05 ? 28  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 28  ? 8.328   -1.824  -2.251  1.00 11.35 ? 28  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 28  ? 11.431  -1.672  -1.982  1.00 10.69 ? 28  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 28  ? 12.712  -0.940  -2.312  1.00 11.39 ? 28  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 28  ? 13.609  -1.489  -2.955  1.00 12.09 ? 28  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 28  ? 12.827  0.300   -1.873  1.00 12.42 ? 28  ASN   A ND2 1 
ATOM   203  N  N   . GLY   A 1 29  ? 9.204   -3.751  -3.027  1.00 11.24 ? 29  GLY   A N   1 
ATOM   204  C  CA  . GLY   A 1 29  ? 8.118   -4.614  -2.604  1.00 10.62 ? 29  GLY   A CA  1 
ATOM   205  C  C   . GLY   A 1 29  ? 8.641   -5.849  -1.866  1.00 11.14 ? 29  GLY   A C   1 
ATOM   206  O  O   . GLY   A 1 29  ? 9.833   -6.146  -1.895  1.00 10.45 ? 29  GLY   A O   1 
ATOM   207  N  N   . LEU   A 1 30  ? 7.728   -6.505  -1.151  1.00 11.06 ? 30  LEU   A N   1 
ATOM   208  C  CA  . LEU   A 1 30  ? 8.007   -7.660  -0.325  1.00 11.65 ? 30  LEU   A CA  1 
ATOM   209  C  C   . LEU   A 1 30  ? 7.246   -8.862  -0.890  1.00 11.87 ? 30  LEU   A C   1 
ATOM   210  O  O   . LEU   A 1 30  ? 6.017   -8.860  -0.896  1.00 12.55 ? 30  LEU   A O   1 
ATOM   211  C  CB  . LEU   A 1 30  ? 7.583   -7.327  1.103   1.00 11.66 ? 30  LEU   A CB  1 
ATOM   212  C  CG  . LEU   A 1 30  ? 7.807   -8.429  2.133   1.00 12.41 ? 30  LEU   A CG  1 
ATOM   213  C  CD1 . LEU   A 1 30  ? 9.272   -8.535  2.509   1.00 13.22 ? 30  LEU   A CD1 1 
ATOM   214  C  CD2 . LEU   A 1 30  ? 6.948   -8.205  3.362   1.00 12.37 ? 30  LEU   A CD2 1 
ATOM   215  N  N   . TRP   A 1 31  ? 8.000   -9.884  -1.327  1.00 11.94 ? 31  TRP   A N   1 
ATOM   216  C  CA  . TRP   A 1 31  ? 7.480   -11.040 -2.048  1.00 11.88 ? 31  TRP   A CA  1 
ATOM   217  C  C   . TRP   A 1 31  ? 7.407   -12.238 -1.119  1.00 12.06 ? 31  TRP   A C   1 
ATOM   218  O  O   . TRP   A 1 31  ? 8.443   -12.791 -0.706  1.00 11.63 ? 31  TRP   A O   1 
ATOM   219  C  CB  . TRP   A 1 31  ? 8.381   -11.323 -3.249  1.00 11.66 ? 31  TRP   A CB  1 
ATOM   220  C  CG  . TRP   A 1 31  ? 7.941   -12.455 -4.137  1.00 13.11 ? 31  TRP   A CG  1 
ATOM   221  C  CD1 . TRP   A 1 31  ? 6.708   -13.016 -4.253  1.00 13.94 ? 31  TRP   A CD1 1 
ATOM   222  C  CD2 . TRP   A 1 31  ? 8.803   -13.177 -5.038  1.00 13.67 ? 31  TRP   A CD2 1 
ATOM   223  N  NE1 . TRP   A 1 31  ? 6.739   -14.033 -5.175  1.00 15.23 ? 31  TRP   A NE1 1 
ATOM   224  C  CE2 . TRP   A 1 31  ? 8.009   -14.145 -5.679  1.00 14.84 ? 31  TRP   A CE2 1 
ATOM   225  C  CE3 . TRP   A 1 31  ? 10.167  -13.091 -5.351  1.00 14.69 ? 31  TRP   A CE3 1 
ATOM   226  C  CZ2 . TRP   A 1 31  ? 8.540   -15.035 -6.606  1.00 15.16 ? 31  TRP   A CZ2 1 
ATOM   227  C  CZ3 . TRP   A 1 31  ? 10.696  -13.985 -6.254  1.00 15.47 ? 31  TRP   A CZ3 1 
ATOM   228  C  CH2 . TRP   A 1 31  ? 9.887   -14.941 -6.871  1.00 15.39 ? 31  TRP   A CH2 1 
ATOM   229  N  N   . LEU   A 1 32  ? 6.165   -12.598 -0.754  1.00 11.64 ? 32  LEU   A N   1 
ATOM   230  C  CA  . LEU   A 1 32  ? 5.927   -13.688 0.174   1.00 12.81 ? 32  LEU   A CA  1 
ATOM   231  C  C   . LEU   A 1 32  ? 4.934   -14.654 -0.481  1.00 14.47 ? 32  LEU   A C   1 
ATOM   232  O  O   . LEU   A 1 32  ? 3.844   -14.257 -0.876  1.00 13.68 ? 32  LEU   A O   1 
ATOM   233  C  CB  . LEU   A 1 32  ? 5.385   -13.155 1.504   1.00 13.06 ? 32  LEU   A CB  1 
ATOM   234  C  CG  . LEU   A 1 32  ? 6.289   -12.211 2.280   1.00 13.08 ? 32  LEU   A CG  1 
ATOM   235  C  CD1 . LEU   A 1 32  ? 5.495   -11.504 3.387   1.00 13.19 ? 32  LEU   A CD1 1 
ATOM   236  C  CD2 . LEU   A 1 32  ? 7.485   -12.933 2.859   1.00 13.22 ? 32  LEU   A CD2 1 
ATOM   237  N  N   . ASP   A 1 33  ? 5.336   -15.924 -0.613  1.00 16.89 ? 33  ASP   A N   1 
ATOM   238  C  CA  . ASP   A 1 33  ? 4.547   -16.893 -1.368  1.00 17.47 ? 33  ASP   A CA  1 
ATOM   239  C  C   . ASP   A 1 33  ? 4.248   -16.273 -2.724  1.00 16.42 ? 33  ASP   A C   1 
ATOM   240  O  O   . ASP   A 1 33  ? 5.207   -15.863 -3.394  1.00 17.14 ? 33  ASP   A O   1 
ATOM   241  C  CB  . ASP   A 1 33  ? 3.324   -17.349 -0.565  1.00 18.13 ? 33  ASP   A CB  1 
ATOM   242  C  CG  . ASP   A 1 33  ? 3.733   -18.034 0.724   1.00 19.76 ? 33  ASP   A CG  1 
ATOM   243  O  OD1 . ASP   A 1 33  ? 4.568   -18.924 0.667   1.00 21.72 ? 33  ASP   A OD1 1 
ATOM   244  O  OD2 . ASP   A 1 33  ? 3.230   -17.651 1.780   1.00 22.46 ? 33  ASP   A OD2 1 
ATOM   245  N  N   . ASP   A 1 34  ? 2.963   -16.150 -3.115  1.00 14.04 ? 34  ASP   A N   1 
ATOM   246  C  CA  . ASP   A 1 34  ? 2.651   -15.646 -4.446  1.00 14.50 ? 34  ASP   A CA  1 
ATOM   247  C  C   . ASP   A 1 34  ? 2.054   -14.241 -4.402  1.00 14.32 ? 34  ASP   A C   1 
ATOM   248  O  O   . ASP   A 1 34  ? 1.353   -13.839 -5.323  1.00 14.60 ? 34  ASP   A O   1 
ATOM   249  C  CB  . ASP   A 1 34  ? 1.713   -16.569 -5.232  1.00 16.69 ? 34  ASP   A CB  1 
ATOM   250  C  CG  . ASP   A 1 34  ? 0.360   -16.803 -4.571  1.00 18.88 ? 34  ASP   A CG  1 
ATOM   251  O  OD1 . ASP   A 1 34  ? 0.200   -16.459 -3.376  1.00 18.68 ? 34  ASP   A OD1 1 
ATOM   252  O  OD2 . ASP   A 1 34  ? -0.506  -17.368 -5.234  1.00 21.85 ? 34  ASP   A OD2 1 
ATOM   253  N  N   . VAL   A 1 35  ? 2.407   -13.440 -3.390  1.00 14.56 ? 35  VAL   A N   1 
ATOM   254  C  CA  . VAL   A 1 35  ? 1.930   -12.061 -3.300  1.00 13.63 ? 35  VAL   A CA  1 
ATOM   255  C  C   . VAL   A 1 35  ? 3.110   -11.107 -3.078  1.00 12.96 ? 35  VAL   A C   1 
ATOM   256  O  O   . VAL   A 1 35  ? 4.014   -11.382 -2.309  1.00 12.25 ? 35  VAL   A O   1 
ATOM   257  C  CB  . VAL   A 1 35  ? 0.888   -11.900 -2.179  1.00 13.34 ? 35  VAL   A CB  1 
ATOM   258  C  CG1 . VAL   A 1 35  ? 0.491   -10.451 -1.979  1.00 12.29 ? 35  VAL   A CG1 1 
ATOM   259  C  CG2 . VAL   A 1 35  ? -0.342  -12.746 -2.413  1.00 14.18 ? 35  VAL   A CG2 1 
ATOM   260  N  N   . VAL   A 1 36  ? 3.077   -9.974  -3.774  1.00 12.49 ? 36  VAL   A N   1 
ATOM   261  C  CA  . VAL   A 1 36  ? 4.011   -8.890  -3.531  1.00 12.72 ? 36  VAL   A CA  1 
ATOM   262  C  C   . VAL   A 1 36  ? 3.251   -7.768  -2.828  1.00 12.20 ? 36  VAL   A C   1 
ATOM   263  O  O   . VAL   A 1 36  ? 2.221   -7.310  -3.335  1.00 11.36 ? 36  VAL   A O   1 
ATOM   264  C  CB  . VAL   A 1 36  ? 4.668   -8.422  -4.838  1.00 12.40 ? 36  VAL   A CB  1 
ATOM   265  C  CG1 . VAL   A 1 36  ? 5.519   -7.198  -4.650  1.00 12.09 ? 36  VAL   A CG1 1 
ATOM   266  C  CG2 . VAL   A 1 36  ? 5.486   -9.539  -5.475  1.00 14.05 ? 36  VAL   A CG2 1 
ATOM   267  N  N   . TYR   A 1 37  ? 3.806   -7.327  -1.680  1.00 12.15 ? 37  TYR   A N   1 
ATOM   268  C  CA  . TYR   A 1 37  ? 3.266   -6.219  -0.903  1.00 11.85 ? 37  TYR   A CA  1 
ATOM   269  C  C   . TYR   A 1 37  ? 4.143   -4.996  -1.136  1.00 12.20 ? 37  TYR   A C   1 
ATOM   270  O  O   . TYR   A 1 37  ? 5.366   -5.062  -1.024  1.00 11.31 ? 37  TYR   A O   1 
ATOM   271  C  CB  . TYR   A 1 37  ? 3.194   -6.561  0.593   1.00 11.97 ? 37  TYR   A CB  1 
ATOM   272  C  CG  . TYR   A 1 37  ? 2.485   -7.872  0.914   1.00 12.70 ? 37  TYR   A CG  1 
ATOM   273  C  CD1 . TYR   A 1 37  ? 3.099   -9.095  0.695   1.00 13.04 ? 37  TYR   A CD1 1 
ATOM   274  C  CD2 . TYR   A 1 37  ? 1.192   -7.888  1.421   1.00 13.21 ? 37  TYR   A CD2 1 
ATOM   275  C  CE1 . TYR   A 1 37  ? 2.447   -10.291 0.956   1.00 14.10 ? 37  TYR   A CE1 1 
ATOM   276  C  CE2 . TYR   A 1 37  ? 0.516   -9.074  1.661   1.00 13.40 ? 37  TYR   A CE2 1 
ATOM   277  C  CZ  . TYR   A 1 37  ? 1.153   -10.276 1.444   1.00 14.33 ? 37  TYR   A CZ  1 
ATOM   278  O  OH  . TYR   A 1 37  ? 0.506   -11.451 1.691   1.00 16.83 ? 37  TYR   A OH  1 
ATOM   279  N  N   . CYS   A 1 38  ? 3.525   -3.853  -1.406  1.00 11.76 ? 38  CYS   A N   1 
ATOM   280  C  CA  . CYS   A 1 38  ? 4.279   -2.623  -1.513  1.00 11.92 ? 38  CYS   A CA  1 
ATOM   281  C  C   . CYS   A 1 38  ? 3.374   -1.446  -1.178  1.00 11.38 ? 38  CYS   A C   1 
ATOM   282  O  O   . CYS   A 1 38  ? 2.166   -1.615  -1.108  1.00 11.78 ? 38  CYS   A O   1 
ATOM   283  C  CB  . CYS   A 1 38  ? 4.904   -2.454  -2.892  1.00 12.23 ? 38  CYS   A CB  1 
ATOM   284  S  SG  . CYS   A 1 38  ? 3.700   -2.124  -4.204  1.00 14.42 ? 38  CYS   A SG  1 
ATOM   285  N  N   . PRO   A 1 39  ? 3.936   -0.240  -0.976  1.00 11.30 ? 39  PRO   A N   1 
ATOM   286  C  CA  . PRO   A 1 39  ? 3.147   0.965   -0.771  1.00 12.13 ? 39  PRO   A CA  1 
ATOM   287  C  C   . PRO   A 1 39  ? 2.307   1.260   -1.994  1.00 11.98 ? 39  PRO   A C   1 
ATOM   288  O  O   . PRO   A 1 39  ? 2.817   1.205   -3.113  1.00 12.61 ? 39  PRO   A O   1 
ATOM   289  C  CB  . PRO   A 1 39  ? 4.197   2.069   -0.519  1.00 11.87 ? 39  PRO   A CB  1 
ATOM   290  C  CG  . PRO   A 1 39  ? 5.409   1.307   -0.020  1.00 11.72 ? 39  PRO   A CG  1 
ATOM   291  C  CD  . PRO   A 1 39  ? 5.374   0.028   -0.821  1.00 12.10 ? 39  PRO   A CD  1 
ATOM   292  N  N   . ARG   A 1 40  ? 1.048   1.628   -1.757  1.00 12.03 ? 40  ARG   A N   1 
ATOM   293  C  CA  . ARG   A 1 40  ? 0.121   1.911   -2.841  1.00 12.71 ? 40  ARG   A CA  1 
ATOM   294  C  C   . ARG   A 1 40  ? 0.519   3.197   -3.541  1.00 12.53 ? 40  ARG   A C   1 
ATOM   295  O  O   . ARG   A 1 40  ? 0.047   3.435   -4.648  1.00 14.41 ? 40  ARG   A O   1 
ATOM   296  C  CB  . ARG   A 1 40  ? -1.331  1.995   -2.341  1.00 12.84 ? 40  ARG   A CB  1 
ATOM   297  C  CG  . ARG   A 1 40  ? -1.636  3.206   -1.468  1.00 12.57 ? 40  ARG   A CG  1 
ATOM   298  C  CD  . ARG   A 1 40  ? -3.100  3.214   -1.080  1.00 12.43 ? 40  ARG   A CD  1 
ATOM   299  N  NE  . ARG   A 1 40  ? -3.373  4.259   -0.117  1.00 12.75 ? 40  ARG   A NE  1 
ATOM   300  C  CZ  . ARG   A 1 40  ? -4.571  4.613   0.339   1.00 13.31 ? 40  ARG   A CZ  1 
ATOM   301  N  NH1 . ARG   A 1 40  ? -5.626  3.873   0.035   1.00 13.05 ? 40  ARG   A NH1 1 
ATOM   302  N  NH2 . ARG   A 1 40  ? -4.689  5.682   1.136   1.00 13.23 ? 40  ARG   A NH2 1 
ATOM   303  N  N   . HIS   A 1 41  ? 1.386   4.009   -2.926  1.00 11.81 ? 41  HIS   A N   1 
ATOM   304  C  CA  . HIS   A 1 41  ? 1.874   5.225   -3.566  1.00 11.98 ? 41  HIS   A CA  1 
ATOM   305  C  C   . HIS   A 1 41  ? 2.462   4.969   -4.974  1.00 13.25 ? 41  HIS   A C   1 
ATOM   306  O  O   . HIS   A 1 41  ? 2.588   5.909   -5.776  1.00 13.40 ? 41  HIS   A O   1 
ATOM   307  C  CB  . HIS   A 1 41  ? 2.896   5.903   -2.664  1.00 11.97 ? 41  HIS   A CB  1 
ATOM   308  C  CG  . HIS   A 1 41  ? 3.087   7.356   -2.909  1.00 12.63 ? 41  HIS   A CG  1 
ATOM   309  N  ND1 . HIS   A 1 41  ? 2.047   8.251   -2.823  1.00 12.75 ? 41  HIS   A ND1 1 
ATOM   310  C  CD2 . HIS   A 1 41  ? 4.162   8.062   -3.219  1.00 14.41 ? 41  HIS   A CD2 1 
ATOM   311  C  CE1 . HIS   A 1 41  ? 2.500   9.461   -3.074  1.00 14.18 ? 41  HIS   A CE1 1 
ATOM   312  N  NE2 . HIS   A 1 41  ? 3.787   9.382   -3.293  1.00 15.76 ? 41  HIS   A NE2 1 
ATOM   313  N  N   . VAL   A 1 42  ? 2.868   3.722   -5.256  1.00 13.55 ? 42  VAL   A N   1 
ATOM   314  C  CA  . VAL   A 1 42  ? 3.504   3.358   -6.522  1.00 14.89 ? 42  VAL   A CA  1 
ATOM   315  C  C   . VAL   A 1 42  ? 2.544   3.564   -7.702  1.00 16.01 ? 42  VAL   A C   1 
ATOM   316  O  O   . VAL   A 1 42  ? 2.982   3.736   -8.829  1.00 14.76 ? 42  VAL   A O   1 
ATOM   317  C  CB  . VAL   A 1 42  ? 4.014   1.910   -6.506  1.00 14.15 ? 42  VAL   A CB  1 
ATOM   318  C  CG1 . VAL   A 1 42  ? 2.873   0.903   -6.555  1.00 13.94 ? 42  VAL   A CG1 1 
ATOM   319  C  CG2 . VAL   A 1 42  ? 5.010   1.655   -7.637  1.00 14.32 ? 42  VAL   A CG2 1 
ATOM   320  N  N   . ILE   A 1 43  ? 1.226   3.597   -7.444  1.00 17.47 ? 43  ILE   A N   1 
ATOM   321  C  CA  . ILE   A 1 43  ? 0.284   3.799   -8.528  1.00 17.63 ? 43  ILE   A CA  1 
ATOM   322  C  C   . ILE   A 1 43  ? 0.163   5.271   -8.896  1.00 18.54 ? 43  ILE   A C   1 
ATOM   323  O  O   . ILE   A 1 43  ? -0.557  5.539   -9.839  1.00 23.25 ? 43  ILE   A O   1 
ATOM   324  C  CB  . ILE   A 1 43  ? -1.101  3.182   -8.258  1.00 16.97 ? 43  ILE   A CB  1 
ATOM   325  C  CG1 . ILE   A 1 43  ? -1.889  3.949   -7.193  1.00 17.20 ? 43  ILE   A CG1 1 
ATOM   326  C  CG2 . ILE   A 1 43  ? -0.938  1.723   -7.950  1.00 17.92 ? 43  ILE   A CG2 1 
ATOM   327  C  CD1 . ILE   A 1 43  ? -3.232  3.348   -6.869  1.00 18.98 ? 43  ILE   A CD1 1 
ATOM   328  N  N   . CYS   A 1 44  ? 0.821   6.192   -8.183  1.00 17.34 ? 44  CYS   A N   1 
ATOM   329  C  CA  . CYS   A 1 44  ? 0.747   7.608   -8.497  1.00 17.28 ? 44  CYS   A CA  1 
ATOM   330  C  C   . CYS   A 1 44  ? 1.765   8.015   -9.564  1.00 20.84 ? 44  CYS   A C   1 
ATOM   331  O  O   . CYS   A 1 44  ? 2.969   7.724   -9.444  1.00 21.55 ? 44  CYS   A O   1 
ATOM   332  C  CB  . CYS   A 1 44  ? 1.016   8.466   -7.261  1.00 16.40 ? 44  CYS   A CB  1 
ATOM   333  S  SG  . CYS   A 1 44  ? -0.172  8.221   -5.907  1.00 14.43 ? 44  CYS   A SG  1 
ATOM   334  N  N   . THR   A 1 45  ? 1.290   8.784   -10.560 1.00 19.84 ? 45  THR   A N   1 
ATOM   335  C  CA  . THR   A 1 45  ? 2.173   9.605   -11.367 1.00 20.11 ? 45  THR   A CA  1 
ATOM   336  C  C   . THR   A 1 45  ? 2.617   10.771  -10.506 1.00 22.04 ? 45  THR   A C   1 
ATOM   337  O  O   . THR   A 1 45  ? 2.049   11.024  -9.434  1.00 21.09 ? 45  THR   A O   1 
ATOM   338  C  CB  . THR   A 1 45  ? 1.492   10.181  -12.621 1.00 23.43 ? 45  THR   A CB  1 
ATOM   339  O  OG1 . THR   A 1 45  ? 0.561   11.156  -12.136 1.00 24.86 ? 45  THR   A OG1 1 
ATOM   340  C  CG2 . THR   A 1 45  ? 0.798   9.162   -13.496 1.00 22.39 ? 45  THR   A CG2 1 
ATOM   341  N  N   . SER   A 1 46  ? 3.610   11.504  -11.003 1.00 21.79 ? 46  SER   A N   1 
ATOM   342  C  CA  . SER   A 1 46  ? 4.101   12.705  -10.359 1.00 25.31 ? 46  SER   A CA  1 
ATOM   343  C  C   . SER   A 1 46  ? 2.966   13.633  -9.926  1.00 25.35 ? 46  SER   A C   1 
ATOM   344  O  O   . SER   A 1 46  ? 2.991   14.189  -8.830  1.00 26.96 ? 46  SER   A O   1 
ATOM   345  C  CB  . SER   A 1 46  ? 5.047   13.425  -11.299 1.00 28.01 ? 46  SER   A CB  1 
ATOM   346  O  OG  . SER   A 1 46  ? 5.487   14.608  -10.676 1.00 32.75 ? 46  SER   A OG  1 
ATOM   347  N  N   . GLU   A 1 47  ? 1.989   13.852  -10.806 1.00 25.95 ? 47  GLU   A N   1 
ATOM   348  C  CA  . GLU   A 1 47  ? 0.939   14.808  -10.498 1.00 28.49 ? 47  GLU   A CA  1 
ATOM   349  C  C   . GLU   A 1 47  ? 0.005   14.204  -9.443  1.00 26.43 ? 47  GLU   A C   1 
ATOM   350  O  O   . GLU   A 1 47  ? -0.538  14.921  -8.627  1.00 27.41 ? 47  GLU   A O   1 
ATOM   351  C  CB  . GLU   A 1 47  ? 0.181   15.263  -11.752 1.00 29.29 ? 47  GLU   A CB  1 
ATOM   352  C  CG  . GLU   A 1 47  ? -0.483  14.161  -12.567 1.00 33.81 ? 47  GLU   A CG  1 
ATOM   353  C  CD  . GLU   A 1 47  ? -1.197  14.686  -13.806 1.00 38.84 ? 47  GLU   A CD  1 
ATOM   354  O  OE1 . GLU   A 1 47  ? -2.021  15.617  -13.655 1.00 38.86 ? 47  GLU   A OE1 1 
ATOM   355  O  OE2 . GLU   A 1 47  ? -0.911  14.184  -14.925 1.00 45.09 ? 47  GLU   A OE2 1 
ATOM   356  N  N   . ASP   A 1 48  ? -0.128  12.873  -9.426  1.00 24.83 ? 48  ASP   A N   1 
ATOM   357  C  CA  . ASP   A 1 48  ? -1.023  12.206  -8.496  1.00 20.82 ? 48  ASP   A CA  1 
ATOM   358  C  C   . ASP   A 1 48  ? -0.539  12.319  -7.053  1.00 19.61 ? 48  ASP   A C   1 
ATOM   359  O  O   . ASP   A 1 48  ? -1.359  12.365  -6.136  1.00 21.03 ? 48  ASP   A O   1 
ATOM   360  C  CB  . ASP   A 1 48  ? -1.196  10.747  -8.890  1.00 21.25 ? 48  ASP   A CB  1 
ATOM   361  C  CG  . ASP   A 1 48  ? -1.884  10.535  -10.224 1.00 22.46 ? 48  ASP   A CG  1 
ATOM   362  O  OD1 . ASP   A 1 48  ? -2.808  11.298  -10.521 1.00 22.42 ? 48  ASP   A OD1 1 
ATOM   363  O  OD2 . ASP   A 1 48  ? -1.515  9.570   -10.943 1.00 22.46 ? 48  ASP   A OD2 1 
ATOM   364  N  N   . MET   A 1 49  ? 0.783   12.370  -6.862  1.00 17.92 ? 49  MET   A N   1 
ATOM   365  C  CA  . MET   A 1 49  ? 1.424   12.200  -5.565  1.00 17.73 ? 49  MET   A CA  1 
ATOM   366  C  C   . MET   A 1 49  ? 0.986   13.256  -4.555  1.00 17.87 ? 49  MET   A C   1 
ATOM   367  O  O   . MET   A 1 49  ? 0.928   12.977  -3.363  1.00 14.69 ? 49  MET   A O   1 
ATOM   368  C  CB  . MET   A 1 49  ? 2.947   12.269  -5.734  1.00 17.41 ? 49  MET   A CB  1 
ATOM   369  C  CG  . MET   A 1 49  ? 3.516   11.023  -6.363  1.00 17.62 ? 49  MET   A CG  1 
ATOM   370  S  SD  . MET   A 1 49  ? 5.268   11.201  -6.796  1.00 20.95 ? 49  MET   A SD  1 
ATOM   371  C  CE  . MET   A 1 49  ? 5.601   9.619   -7.556  1.00 19.89 ? 49  MET   A CE  1 
ATOM   372  N  N   . LEU   A 1 50  ? 0.703   14.480  -5.030  1.00 20.01 ? 50  LEU   A N   1 
ATOM   373  C  CA  . LEU   A 1 50  ? 0.359   15.587  -4.142  1.00 20.69 ? 50  LEU   A CA  1 
ATOM   374  C  C   . LEU   A 1 50  ? -0.994  15.361  -3.473  1.00 19.68 ? 50  LEU   A C   1 
ATOM   375  O  O   . LEU   A 1 50  ? -1.155  15.634  -2.287  1.00 22.47 ? 50  LEU   A O   1 
ATOM   376  C  CB  . LEU   A 1 50  ? 0.360   16.896  -4.940  1.00 24.33 ? 50  LEU   A CB  1 
ATOM   377  C  CG  . LEU   A 1 50  ? 1.676   17.225  -5.654  1.00 29.94 ? 50  LEU   A CG  1 
ATOM   378  C  CD1 . LEU   A 1 50  ? 1.486   18.281  -6.751  1.00 33.92 ? 50  LEU   A CD1 1 
ATOM   379  C  CD2 . LEU   A 1 50  ? 2.737   17.698  -4.665  1.00 29.45 ? 50  LEU   A CD2 1 
ATOM   380  N  N   . ASN   A 1 51  ? -1.981  14.838  -4.212  1.00 20.07 ? 51  ASN   A N   1 
ATOM   381  C  CA  . ASN   A 1 51  ? -3.314  14.717  -3.669  1.00 18.77 ? 51  ASN   A CA  1 
ATOM   382  C  C   . ASN   A 1 51  ? -4.041  13.545  -4.308  1.00 17.95 ? 51  ASN   A C   1 
ATOM   383  O  O   . ASN   A 1 51  ? -5.005  13.713  -5.063  1.00 16.67 ? 51  ASN   A O   1 
ATOM   384  C  CB  . ASN   A 1 51  ? -4.120  16.000  -3.833  1.00 21.59 ? 51  ASN   A CB  1 
ATOM   385  C  CG  . ASN   A 1 51  ? -5.294  16.013  -2.875  1.00 23.36 ? 51  ASN   A CG  1 
ATOM   386  O  OD1 . ASN   A 1 51  ? -5.342  15.217  -1.943  1.00 27.20 ? 51  ASN   A OD1 1 
ATOM   387  N  ND2 . ASN   A 1 51  ? -6.273  16.863  -3.118  1.00 24.95 ? 51  ASN   A ND2 1 
ATOM   388  N  N   . PRO   A 1 52  ? -3.597  12.303  -4.026  1.00 16.75 ? 52  PRO   A N   1 
ATOM   389  C  CA  . PRO   A 1 52  ? -4.181  11.134  -4.674  1.00 15.56 ? 52  PRO   A CA  1 
ATOM   390  C  C   . PRO   A 1 52  ? -5.553  10.744  -4.122  1.00 16.03 ? 52  PRO   A C   1 
ATOM   391  O  O   . PRO   A 1 52  ? -5.775  10.799  -2.917  1.00 15.14 ? 52  PRO   A O   1 
ATOM   392  C  CB  . PRO   A 1 52  ? -3.123  10.064  -4.385  1.00 15.86 ? 52  PRO   A CB  1 
ATOM   393  C  CG  . PRO   A 1 52  ? -2.480  10.481  -3.120  1.00 15.95 ? 52  PRO   A CG  1 
ATOM   394  C  CD  . PRO   A 1 52  ? -2.495  11.985  -3.115  1.00 16.20 ? 52  PRO   A CD  1 
ATOM   395  N  N   . ASN   A 1 53  ? -6.439  10.313  -5.028  1.00 15.90 ? 53  ASN   A N   1 
ATOM   396  C  CA  . ASN   A 1 53  ? -7.617  9.535   -4.712  1.00 15.79 ? 53  ASN   A CA  1 
ATOM   397  C  C   . ASN   A 1 53  ? -7.335  8.102   -5.119  1.00 14.63 ? 53  ASN   A C   1 
ATOM   398  O  O   . ASN   A 1 53  ? -7.442  7.768   -6.290  1.00 16.15 ? 53  ASN   A O   1 
ATOM   399  C  CB  . ASN   A 1 53  ? -8.856  10.051  -5.459  1.00 17.05 ? 53  ASN   A CB  1 
ATOM   400  C  CG  . ASN   A 1 53  ? -10.126 9.350   -5.029  1.00 17.94 ? 53  ASN   A CG  1 
ATOM   401  O  OD1 . ASN   A 1 53  ? -10.235 8.126   -5.030  1.00 19.35 ? 53  ASN   A OD1 1 
ATOM   402  N  ND2 . ASN   A 1 53  ? -11.118 10.131  -4.654  1.00 19.82 ? 53  ASN   A ND2 1 
ATOM   403  N  N   . TYR   A 1 54  ? -6.984  7.260   -4.156  1.00 13.80 ? 54  TYR   A N   1 
ATOM   404  C  CA  . TYR   A 1 54  ? -6.359  5.981   -4.450  1.00 14.32 ? 54  TYR   A CA  1 
ATOM   405  C  C   . TYR   A 1 54  ? -7.369  4.985   -5.014  1.00 15.62 ? 54  TYR   A C   1 
ATOM   406  O  O   . TYR   A 1 54  ? -7.014  4.188   -5.867  1.00 15.82 ? 54  TYR   A O   1 
ATOM   407  C  CB  . TYR   A 1 54  ? -5.696  5.389   -3.203  1.00 13.60 ? 54  TYR   A CB  1 
ATOM   408  C  CG  . TYR   A 1 54  ? -4.336  6.010   -2.893  1.00 13.56 ? 54  TYR   A CG  1 
ATOM   409  C  CD1 . TYR   A 1 54  ? -3.223  5.674   -3.655  1.00 13.27 ? 54  TYR   A CD1 1 
ATOM   410  C  CD2 . TYR   A 1 54  ? -4.152  6.907   -1.837  1.00 13.63 ? 54  TYR   A CD2 1 
ATOM   411  C  CE1 . TYR   A 1 54  ? -1.966  6.195   -3.384  1.00 12.86 ? 54  TYR   A CE1 1 
ATOM   412  C  CE2 . TYR   A 1 54  ? -2.898  7.451   -1.569  1.00 13.75 ? 54  TYR   A CE2 1 
ATOM   413  C  CZ  . TYR   A 1 54  ? -1.807  7.088   -2.347  1.00 12.88 ? 54  TYR   A CZ  1 
ATOM   414  O  OH  . TYR   A 1 54  ? -0.565  7.574   -2.117  1.00 14.41 ? 54  TYR   A OH  1 
ATOM   415  N  N   . GLU   A 1 55  ? -8.621  4.998   -4.534  1.00 15.87 ? 55  GLU   A N   1 
ATOM   416  C  CA  . GLU   A 1 55  ? -9.632  4.126   -5.116  1.00 18.10 ? 55  GLU   A CA  1 
ATOM   417  C  C   . GLU   A 1 55  ? -9.840  4.441   -6.596  1.00 16.65 ? 55  GLU   A C   1 
ATOM   418  O  O   . GLU   A 1 55  ? -9.999  3.523   -7.389  1.00 15.98 ? 55  GLU   A O   1 
ATOM   419  C  CB  . GLU   A 1 55  ? -10.965 4.215   -4.381  1.00 20.19 ? 55  GLU   A CB  1 
ATOM   420  C  CG  . GLU   A 1 55  ? -10.934 3.610   -3.007  1.00 24.31 ? 55  GLU   A CG  1 
ATOM   421  C  CD  . GLU   A 1 55  ? -10.866 2.096   -2.942  1.00 29.02 ? 55  GLU   A CD  1 
ATOM   422  O  OE1 . GLU   A 1 55  ? -10.883 1.422   -3.999  1.00 31.49 ? 55  GLU   A OE1 1 
ATOM   423  O  OE2 . GLU   A 1 55  ? -10.803 1.587   -1.821  1.00 33.36 ? 55  GLU   A OE2 1 
ATOM   424  N  N   . ASP   A 1 56  ? -9.816  5.725   -6.945  1.00 17.65 ? 56  ASP   A N   1 
ATOM   425  C  CA  . ASP   A 1 56  ? -9.936  6.169   -8.330  1.00 18.74 ? 56  ASP   A CA  1 
ATOM   426  C  C   . ASP   A 1 56  ? -8.730  5.729   -9.154  1.00 18.97 ? 56  ASP   A C   1 
ATOM   427  O  O   . ASP   A 1 56  ? -8.882  5.222   -10.258 1.00 17.27 ? 56  ASP   A O   1 
ATOM   428  C  CB  . ASP   A 1 56  ? -9.999  7.691   -8.418  1.00 19.16 ? 56  ASP   A CB  1 
ATOM   429  C  CG  . ASP   A 1 56  ? -11.383 8.257   -8.235  1.00 20.95 ? 56  ASP   A CG  1 
ATOM   430  O  OD1 . ASP   A 1 56  ? -12.336 7.433   -8.114  1.00 20.89 ? 56  ASP   A OD1 1 
ATOM   431  O  OD2 . ASP   A 1 56  ? -11.481 9.517   -8.217  1.00 23.07 ? 56  ASP   A OD2 1 
ATOM   432  N  N   . LEU   A 1 57  ? -7.532  5.910   -8.595  1.00 17.96 ? 57  LEU   A N   1 
ATOM   433  C  CA  . LEU   A 1 57  ? -6.315  5.611   -9.328  1.00 17.80 ? 57  LEU   A CA  1 
ATOM   434  C  C   . LEU   A 1 57  ? -6.229  4.116   -9.590  1.00 17.60 ? 57  LEU   A C   1 
ATOM   435  O  O   . LEU   A 1 57  ? -5.799  3.707   -10.665 1.00 20.68 ? 57  LEU   A O   1 
ATOM   436  C  CB  . LEU   A 1 57  ? -5.112  6.111   -8.530  1.00 17.84 ? 57  LEU   A CB  1 
ATOM   437  C  CG  . LEU   A 1 57  ? -4.923  7.620   -8.485  1.00 18.78 ? 57  LEU   A CG  1 
ATOM   438  C  CD1 . LEU   A 1 57  ? -3.792  7.983   -7.541  1.00 19.01 ? 57  LEU   A CD1 1 
ATOM   439  C  CD2 . LEU   A 1 57  ? -4.604  8.196   -9.871  1.00 19.62 ? 57  LEU   A CD2 1 
ATOM   440  N  N   . LEU   A 1 58  ? -6.647  3.303   -8.624  1.00 16.85 ? 58  LEU   A N   1 
ATOM   441  C  CA  . LEU   A 1 58  ? -6.482  1.874   -8.716  1.00 17.08 ? 58  LEU   A CA  1 
ATOM   442  C  C   . LEU   A 1 58  ? -7.458  1.272   -9.738  1.00 18.62 ? 58  LEU   A C   1 
ATOM   443  O  O   . LEU   A 1 58  ? -7.097  0.341   -10.473 1.00 18.91 ? 58  LEU   A O   1 
ATOM   444  C  CB  . LEU   A 1 58  ? -6.692  1.250   -7.340  1.00 18.55 ? 58  LEU   A CB  1 
ATOM   445  C  CG  . LEU   A 1 58  ? -6.289  -0.223  -7.275  1.00 21.49 ? 58  LEU   A CG  1 
ATOM   446  C  CD1 . LEU   A 1 58  ? -4.810  -0.388  -7.561  1.00 23.82 ? 58  LEU   A CD1 1 
ATOM   447  C  CD2 . LEU   A 1 58  ? -6.619  -0.858  -5.937  1.00 22.98 ? 58  LEU   A CD2 1 
ATOM   448  N  N   . ILE   A 1 59  ? -8.705  1.779   -9.766  1.00 18.07 ? 59  ILE   A N   1 
ATOM   449  C  CA  . ILE   A 1 59  ? -9.701  1.284   -10.706 1.00 18.54 ? 59  ILE   A CA  1 
ATOM   450  C  C   . ILE   A 1 59  ? -9.253  1.529   -12.155 1.00 17.68 ? 59  ILE   A C   1 
ATOM   451  O  O   . ILE   A 1 59  ? -9.649  0.789   -13.047 1.00 19.32 ? 59  ILE   A O   1 
ATOM   452  C  CB  . ILE   A 1 59  ? -11.113 1.842   -10.388 1.00 19.56 ? 59  ILE   A CB  1 
ATOM   453  C  CG1 . ILE   A 1 59  ? -12.197 0.901   -10.902 1.00 22.06 ? 59  ILE   A CG1 1 
ATOM   454  C  CG2 . ILE   A 1 59  ? -11.340 3.256   -10.893 1.00 18.15 ? 59  ILE   A CG2 1 
ATOM   455  C  CD1 . ILE   A 1 59  ? -12.075 -0.484  -10.309 1.00 24.14 ? 59  ILE   A CD1 1 
ATOM   456  N  N   . ARG   A 1 60  ? -8.387  2.519   -12.378 1.00 17.61 ? 60  ARG   A N   1 
ATOM   457  C  CA  . ARG   A 1 60  ? -7.855  2.847   -13.687 1.00 18.64 ? 60  ARG   A CA  1 
ATOM   458  C  C   . ARG   A 1 60  ? -6.616  2.038   -14.050 1.00 20.11 ? 60  ARG   A C   1 
ATOM   459  O  O   . ARG   A 1 60  ? -6.085  2.238   -15.123 1.00 20.17 ? 60  ARG   A O   1 
ATOM   460  C  CB  . ARG   A 1 60  ? -7.501  4.327   -13.707 1.00 18.76 ? 60  ARG   A CB  1 
ATOM   461  C  CG  . ARG   A 1 60  ? -8.737  5.179   -13.488 1.00 18.43 ? 60  ARG   A CG  1 
ATOM   462  C  CD  . ARG   A 1 60  ? -8.442  6.618   -13.192 1.00 18.25 ? 60  ARG   A CD  1 
ATOM   463  N  NE  . ARG   A 1 60  ? -9.735  7.256   -13.026 1.00 19.45 ? 60  ARG   A NE  1 
ATOM   464  C  CZ  . ARG   A 1 60  ? -9.931  8.387   -12.349 1.00 20.23 ? 60  ARG   A CZ  1 
ATOM   465  N  NH1 . ARG   A 1 60  ? -8.899  9.129   -12.002 1.00 20.66 ? 60  ARG   A NH1 1 
ATOM   466  N  NH2 . ARG   A 1 60  ? -11.157 8.751   -12.010 1.00 20.07 ? 60  ARG   A NH2 1 
ATOM   467  N  N   . LYS   A 1 61  ? -6.239  1.068   -13.214 1.00 22.30 ? 61  LYS   A N   1 
ATOM   468  C  CA  . LYS   A 1 61  ? -5.130  0.179   -13.492 1.00 22.59 ? 61  LYS   A CA  1 
ATOM   469  C  C   . LYS   A 1 61  ? -5.618  -1.238  -13.756 1.00 22.29 ? 61  LYS   A C   1 
ATOM   470  O  O   . LYS   A 1 61  ? -6.624  -1.677  -13.192 1.00 22.67 ? 61  LYS   A O   1 
ATOM   471  C  CB  . LYS   A 1 61  ? -4.204  0.136   -12.278 1.00 23.02 ? 61  LYS   A CB  1 
ATOM   472  C  CG  . LYS   A 1 61  ? -3.514  1.442   -11.952 1.00 27.15 ? 61  LYS   A CG  1 
ATOM   473  C  CD  . LYS   A 1 61  ? -2.528  1.892   -12.998 1.00 32.48 ? 61  LYS   A CD  1 
ATOM   474  C  CE  . LYS   A 1 61  ? -1.878  3.208   -12.627 1.00 36.62 ? 61  LYS   A CE  1 
ATOM   475  N  NZ  . LYS   A 1 61  ? -2.887  4.278   -12.421 1.00 43.10 ? 61  LYS   A NZ  1 
ATOM   476  N  N   . SER   A 1 62  ? -4.835  -1.973  -14.555 1.00 21.85 ? 62  SER   A N   1 
ATOM   477  C  CA  . SER   A 1 62  ? -5.004  -3.412  -14.674 1.00 24.16 ? 62  SER   A CA  1 
ATOM   478  C  C   . SER   A 1 62  ? -3.688  -4.104  -14.298 1.00 22.66 ? 62  SER   A C   1 
ATOM   479  O  O   . SER   A 1 62  ? -2.683  -3.448  -14.057 1.00 20.48 ? 62  SER   A O   1 
ATOM   480  C  CB  . SER   A 1 62  ? -5.415  -3.783  -16.078 1.00 26.36 ? 62  SER   A CB  1 
ATOM   481  O  OG  . SER   A 1 62  ? -4.343  -3.511  -16.975 1.00 28.40 ? 62  SER   A OG  1 
ATOM   482  N  N   . ASN   A 1 63  ? -3.706  -5.430  -14.298 1.00 22.94 ? 63  ASN   A N   1 
ATOM   483  C  CA  . ASN   A 1 63  ? -2.558  -6.238  -13.920 1.00 23.91 ? 63  ASN   A CA  1 
ATOM   484  C  C   . ASN   A 1 63  ? -1.335  -5.877  -14.751 1.00 24.79 ? 63  ASN   A C   1 
ATOM   485  O  O   . ASN   A 1 63  ? -0.236  -5.798  -14.195 1.00 24.84 ? 63  ASN   A O   1 
ATOM   486  C  CB  . ASN   A 1 63  ? -2.871  -7.725  -14.036 1.00 23.65 ? 63  ASN   A CB  1 
ATOM   487  C  CG  . ASN   A 1 63  ? -3.911  -8.154  -13.034 1.00 24.29 ? 63  ASN   A CG  1 
ATOM   488  O  OD1 . ASN   A 1 63  ? -4.008  -7.569  -11.959 1.00 26.07 ? 63  ASN   A OD1 1 
ATOM   489  N  ND2 . ASN   A 1 63  ? -4.635  -9.218  -13.341 1.00 24.16 ? 63  ASN   A ND2 1 
ATOM   490  N  N   . HIS   A 1 64  ? -1.522  -5.634  -16.058 1.00 26.56 ? 64  HIS   A N   1 
ATOM   491  C  CA  . HIS   A 1 64  ? -0.391  -5.448  -16.967 1.00 27.35 ? 64  HIS   A CA  1 
ATOM   492  C  C   . HIS   A 1 64  ? 0.286   -4.086  -16.789 1.00 24.41 ? 64  HIS   A C   1 
ATOM   493  O  O   . HIS   A 1 64  ? 1.343   -3.862  -17.360 1.00 24.67 ? 64  HIS   A O   1 
ATOM   494  C  CB  . HIS   A 1 64  ? -0.787  -5.677  -18.438 1.00 29.74 ? 64  HIS   A CB  1 
ATOM   495  C  CG  . HIS   A 1 64  ? -1.538  -4.546  -19.055 1.00 37.21 ? 64  HIS   A CG  1 
ATOM   496  N  ND1 . HIS   A 1 64  ? -2.874  -4.628  -19.394 1.00 48.06 ? 64  HIS   A ND1 1 
ATOM   497  C  CD2 . HIS   A 1 64  ? -1.150  -3.302  -19.402 1.00 44.12 ? 64  HIS   A CD2 1 
ATOM   498  C  CE1 . HIS   A 1 64  ? -3.271  -3.468  -19.917 1.00 48.93 ? 64  HIS   A CE1 1 
ATOM   499  N  NE2 . HIS   A 1 64  ? -2.242  -2.643  -19.928 1.00 47.70 ? 64  HIS   A NE2 1 
ATOM   500  N  N   . ASN   A 1 65  ? -0.304  -3.161  -16.023 1.00 22.27 ? 65  ASN   A N   1 
ATOM   501  C  CA  . ASN   A 1 65  ? 0.357   -1.909  -15.681 1.00 20.53 ? 65  ASN   A CA  1 
ATOM   502  C  C   . ASN   A 1 65  ? 1.440   -2.085  -14.598 1.00 19.97 ? 65  ASN   A C   1 
ATOM   503  O  O   . ASN   A 1 65  ? 2.151   -1.128  -14.283 1.00 21.68 ? 65  ASN   A O   1 
ATOM   504  C  CB  . ASN   A 1 65  ? -0.651  -0.854  -15.215 1.00 21.92 ? 65  ASN   A CB  1 
ATOM   505  C  CG  . ASN   A 1 65  ? -1.722  -0.480  -16.231 1.00 21.87 ? 65  ASN   A CG  1 
ATOM   506  O  OD1 . ASN   A 1 65  ? -2.913  -0.482  -15.939 1.00 19.81 ? 65  ASN   A OD1 1 
ATOM   507  N  ND2 . ASN   A 1 65  ? -1.310  -0.138  -17.432 1.00 24.12 ? 65  ASN   A ND2 1 
ATOM   508  N  N   . PHE   A 1 66  ? 1.575   -3.273  -13.997 1.00 20.29 ? 66  PHE   A N   1 
ATOM   509  C  CA  . PHE   A 1 66  ? 2.533   -3.456  -12.907 1.00 21.19 ? 66  PHE   A CA  1 
ATOM   510  C  C   . PHE   A 1 66  ? 3.713   -4.298  -13.377 1.00 21.66 ? 66  PHE   A C   1 
ATOM   511  O  O   . PHE   A 1 66  ? 3.525   -5.420  -13.816 1.00 23.46 ? 66  PHE   A O   1 
ATOM   512  C  CB  . PHE   A 1 66  ? 1.876   -4.133  -11.705 1.00 20.44 ? 66  PHE   A CB  1 
ATOM   513  C  CG  . PHE   A 1 66  ? 0.755   -3.322  -11.118 1.00 21.02 ? 66  PHE   A CG  1 
ATOM   514  C  CD1 . PHE   A 1 66  ? 1.016   -2.253  -10.272 1.00 21.53 ? 66  PHE   A CD1 1 
ATOM   515  C  CD2 . PHE   A 1 66  ? -0.550  -3.578  -11.474 1.00 21.00 ? 66  PHE   A CD2 1 
ATOM   516  C  CE1 . PHE   A 1 66  ? -0.012  -1.497  -9.742  1.00 22.00 ? 66  PHE   A CE1 1 
ATOM   517  C  CE2 . PHE   A 1 66  ? -1.579  -2.826  -10.935 1.00 22.32 ? 66  PHE   A CE2 1 
ATOM   518  C  CZ  . PHE   A 1 66  ? -1.311  -1.767  -10.106 1.00 22.73 ? 66  PHE   A CZ  1 
ATOM   519  N  N   . LEU   A 1 67  ? 4.924   -3.752  -13.248 1.00 23.21 ? 67  LEU   A N   1 
ATOM   520  C  CA  . LEU   A 1 67  ? 6.153   -4.482  -13.527 1.00 23.80 ? 67  LEU   A CA  1 
ATOM   521  C  C   . LEU   A 1 67  ? 6.835   -4.840  -12.198 1.00 22.17 ? 67  LEU   A C   1 
ATOM   522  O  O   . LEU   A 1 67  ? 7.265   -3.946  -11.461 1.00 20.45 ? 67  LEU   A O   1 
ATOM   523  C  CB  . LEU   A 1 67  ? 7.045   -3.617  -14.429 1.00 24.94 ? 67  LEU   A CB  1 
ATOM   524  C  CG  . LEU   A 1 67  ? 8.452   -4.165  -14.681 1.00 30.34 ? 67  LEU   A CG  1 
ATOM   525  C  CD1 . LEU   A 1 67  ? 8.421   -5.462  -15.487 1.00 31.09 ? 67  LEU   A CD1 1 
ATOM   526  C  CD2 . LEU   A 1 67  ? 9.329   -3.140  -15.391 1.00 33.71 ? 67  LEU   A CD2 1 
ATOM   527  N  N   . VAL   A 1 68  ? 6.840   -6.139  -11.877 1.00 19.70 ? 68  VAL   A N   1 
ATOM   528  C  CA  . VAL   A 1 68  ? 7.526   -6.693  -10.724 1.00 20.68 ? 68  VAL   A CA  1 
ATOM   529  C  C   . VAL   A 1 68  ? 8.793   -7.414  -11.191 1.00 23.89 ? 68  VAL   A C   1 
ATOM   530  O  O   . VAL   A 1 68  ? 8.727   -8.315  -12.028 1.00 22.17 ? 68  VAL   A O   1 
ATOM   531  C  CB  . VAL   A 1 68  ? 6.636   -7.660  -9.921  1.00 20.28 ? 68  VAL   A CB  1 
ATOM   532  C  CG1 . VAL   A 1 68  ? 7.380   -8.226  -8.728  1.00 18.75 ? 68  VAL   A CG1 1 
ATOM   533  C  CG2 . VAL   A 1 68  ? 5.347   -7.000  -9.464  1.00 21.70 ? 68  VAL   A CG2 1 
ATOM   534  N  N   . GLN   A 1 69  ? 9.940   -7.022  -10.610 1.00 22.40 ? 69  GLN   A N   1 
ATOM   535  C  CA  . GLN   A 1 69  ? 11.215  -7.624  -10.926 1.00 22.88 ? 69  GLN   A CA  1 
ATOM   536  C  C   . GLN   A 1 69  ? 11.900  -8.139  -9.657  1.00 20.61 ? 69  GLN   A C   1 
ATOM   537  O  O   . GLN   A 1 69  ? 12.039  -7.408  -8.668  1.00 16.02 ? 69  GLN   A O   1 
ATOM   538  C  CB  . GLN   A 1 69  ? 12.062  -6.582  -11.648 1.00 29.11 ? 69  GLN   A CB  1 
ATOM   539  C  CG  . GLN   A 1 69  ? 11.459  -6.189  -12.993 1.00 34.04 ? 69  GLN   A CG  1 
ATOM   540  C  CD  . GLN   A 1 69  ? 12.124  -4.972  -13.579 1.00 37.17 ? 69  GLN   A CD  1 
ATOM   541  O  OE1 . GLN   A 1 69  ? 11.937  -3.838  -13.132 1.00 41.59 ? 69  GLN   A OE1 1 
ATOM   542  N  NE2 . GLN   A 1 69  ? 12.906  -5.204  -14.617 1.00 43.65 ? 69  GLN   A NE2 1 
ATOM   543  N  N   . ALA   A 1 70  ? 12.264  -9.426  -9.695  1.00 18.91 ? 70  ALA   A N   1 
ATOM   544  C  CA  . ALA   A 1 70  ? 13.068  -10.069 -8.682  1.00 19.95 ? 70  ALA   A CA  1 
ATOM   545  C  C   . ALA   A 1 70  ? 14.443  -10.253 -9.299  1.00 23.53 ? 70  ALA   A C   1 
ATOM   546  O  O   . ALA   A 1 70  ? 14.658  -11.195 -10.073 1.00 22.86 ? 70  ALA   A O   1 
ATOM   547  C  CB  . ALA   A 1 70  ? 12.456  -11.390 -8.281  1.00 20.66 ? 70  ALA   A CB  1 
ATOM   548  N  N   . GLY   A 1 71  ? 15.353  -9.334  -8.986  1.00 26.84 ? 71  GLY   A N   1 
ATOM   549  C  CA  . GLY   A 1 71  ? 16.587  -9.234  -9.741  1.00 30.21 ? 71  GLY   A CA  1 
ATOM   550  C  C   . GLY   A 1 71  ? 16.271  -8.846  -11.179 1.00 37.82 ? 71  GLY   A C   1 
ATOM   551  O  O   . GLY   A 1 71  ? 15.613  -7.832  -11.416 1.00 45.09 ? 71  GLY   A O   1 
ATOM   552  N  N   . ASN   A 1 72  ? 16.698  -9.698  -12.117 1.00 40.75 ? 72  ASN   A N   1 
ATOM   553  C  CA  . ASN   A 1 72  ? 16.442  -9.499  -13.533 1.00 46.45 ? 72  ASN   A CA  1 
ATOM   554  C  C   . ASN   A 1 72  ? 15.277  -10.369 -14.022 1.00 44.72 ? 72  ASN   A C   1 
ATOM   555  O  O   . ASN   A 1 72  ? 14.983  -10.381 -15.211 1.00 39.16 ? 72  ASN   A O   1 
ATOM   556  C  CB  . ASN   A 1 72  ? 17.697  -9.791  -14.359 1.00 56.06 ? 72  ASN   A CB  1 
ATOM   557  C  CG  . ASN   A 1 72  ? 18.162  -11.228 -14.223 1.00 64.42 ? 72  ASN   A CG  1 
ATOM   558  O  OD1 . ASN   A 1 72  ? 17.871  -12.065 -15.073 1.00 74.48 ? 72  ASN   A OD1 1 
ATOM   559  N  ND2 . ASN   A 1 72  ? 18.855  -11.544 -13.141 1.00 70.37 ? 72  ASN   A ND2 1 
ATOM   560  N  N   . VAL   A 1 73  ? 14.595  -11.082 -13.119 1.00 38.88 ? 73  VAL   A N   1 
ATOM   561  C  CA  . VAL   A 1 73  ? 13.461  -11.912 -13.489 1.00 35.49 ? 73  VAL   A CA  1 
ATOM   562  C  C   . VAL   A 1 73  ? 12.177  -11.112 -13.276 1.00 30.57 ? 73  VAL   A C   1 
ATOM   563  O  O   . VAL   A 1 73  ? 11.937  -10.643 -12.169 1.00 26.44 ? 73  VAL   A O   1 
ATOM   564  C  CB  . VAL   A 1 73  ? 13.473  -13.196 -12.642 1.00 38.96 ? 73  VAL   A CB  1 
ATOM   565  C  CG1 . VAL   A 1 73  ? 12.158  -13.946 -12.679 1.00 40.17 ? 73  VAL   A CG1 1 
ATOM   566  C  CG2 . VAL   A 1 73  ? 14.632  -14.092 -13.046 1.00 42.94 ? 73  VAL   A CG2 1 
ATOM   567  N  N   . GLN   A 1 74  ? 11.348  -11.001 -14.323 1.00 26.41 ? 74  GLN   A N   1 
ATOM   568  C  CA  . GLN   A 1 74  ? 10.055  -10.343 -14.230 1.00 28.40 ? 74  GLN   A CA  1 
ATOM   569  C  C   . GLN   A 1 74  ? 9.046   -11.356 -13.693 1.00 28.24 ? 74  GLN   A C   1 
ATOM   570  O  O   . GLN   A 1 74  ? 8.972   -12.481 -14.170 1.00 27.29 ? 74  GLN   A O   1 
ATOM   571  C  CB  . GLN   A 1 74  ? 9.611   -9.806  -15.593 1.00 33.63 ? 74  GLN   A CB  1 
ATOM   572  C  CG  . GLN   A 1 74  ? 8.162   -9.322  -15.642 1.00 40.52 ? 74  GLN   A CG  1 
ATOM   573  C  CD  . GLN   A 1 74  ? 7.746   -8.752  -16.987 1.00 46.09 ? 74  GLN   A CD  1 
ATOM   574  O  OE1 . GLN   A 1 74  ? 8.523   -8.716  -17.938 1.00 52.42 ? 74  GLN   A OE1 1 
ATOM   575  N  NE2 . GLN   A 1 74  ? 6.507   -8.293  -17.081 1.00 41.47 ? 74  GLN   A NE2 1 
ATOM   576  N  N   . LEU   A 1 75  ? 8.248   -10.941 -12.710 1.00 23.02 ? 75  LEU   A N   1 
ATOM   577  C  CA  . LEU   A 1 75  ? 7.180   -11.772 -12.199 1.00 22.74 ? 75  LEU   A CA  1 
ATOM   578  C  C   . LEU   A 1 75  ? 5.869   -11.221 -12.766 1.00 25.49 ? 75  LEU   A C   1 
ATOM   579  O  O   . LEU   A 1 75  ? 5.520   -10.060 -12.551 1.00 30.60 ? 75  LEU   A O   1 
ATOM   580  C  CB  . LEU   A 1 75  ? 7.169   -11.725 -10.666 1.00 20.84 ? 75  LEU   A CB  1 
ATOM   581  C  CG  . LEU   A 1 75  ? 8.481   -12.014 -9.937  1.00 20.48 ? 75  LEU   A CG  1 
ATOM   582  C  CD1 . LEU   A 1 75  ? 8.278   -11.978 -8.428  1.00 20.16 ? 75  LEU   A CD1 1 
ATOM   583  C  CD2 . LEU   A 1 75  ? 9.045   -13.363 -10.337 1.00 23.22 ? 75  LEU   A CD2 1 
ATOM   584  N  N   . ARG   A 1 76  ? 5.105   -12.082 -13.419 1.00 22.86 ? 76  ARG   A N   1 
ATOM   585  C  CA  . ARG   A 1 76  ? 3.865   -11.689 -14.053 1.00 23.49 ? 76  ARG   A CA  1 
ATOM   586  C  C   . ARG   A 1 76  ? 2.764   -11.532 -12.998 1.00 19.17 ? 76  ARG   A C   1 
ATOM   587  O  O   . ARG   A 1 76  ? 2.501   -12.441 -12.202 1.00 17.31 ? 76  ARG   A O   1 
ATOM   588  C  CB  . ARG   A 1 76  ? 3.503   -12.739 -15.111 1.00 26.35 ? 76  ARG   A CB  1 
ATOM   589  C  CG  . ARG   A 1 76  ? 2.080   -12.610 -15.622 1.00 31.63 ? 76  ARG   A CG  1 
ATOM   590  C  CD  . ARG   A 1 76  ? 1.744   -13.581 -16.733 1.00 36.37 ? 76  ARG   A CD  1 
ATOM   591  N  NE  . ARG   A 1 76  ? 1.983   -12.903 -18.003 1.00 43.90 ? 76  ARG   A NE  1 
ATOM   592  C  CZ  . ARG   A 1 76  ? 1.040   -12.419 -18.815 1.00 55.39 ? 76  ARG   A CZ  1 
ATOM   593  N  NH1 . ARG   A 1 76  ? -0.245  -12.625 -18.567 1.00 57.44 ? 76  ARG   A NH1 1 
ATOM   594  N  NH2 . ARG   A 1 76  ? 1.393   -11.742 -19.898 1.00 61.48 ? 76  ARG   A NH2 1 
ATOM   595  N  N   . VAL   A 1 77  ? 2.139   -10.352 -13.006 1.00 17.81 ? 77  VAL   A N   1 
ATOM   596  C  CA  . VAL   A 1 77  ? 1.076   -10.007 -12.069 1.00 18.70 ? 77  VAL   A CA  1 
ATOM   597  C  C   . VAL   A 1 77  ? -0.245  -10.562 -12.605 1.00 17.81 ? 77  VAL   A C   1 
ATOM   598  O  O   . VAL   A 1 77  ? -0.616  -10.249 -13.720 1.00 17.43 ? 77  VAL   A O   1 
ATOM   599  C  CB  . VAL   A 1 77  ? 1.008   -8.475  -11.883 1.00 17.85 ? 77  VAL   A CB  1 
ATOM   600  C  CG1 . VAL   A 1 77  ? -0.188  -8.046  -11.036 1.00 16.50 ? 77  VAL   A CG1 1 
ATOM   601  C  CG2 . VAL   A 1 77  ? 2.297   -7.947  -11.279 1.00 18.04 ? 77  VAL   A CG2 1 
ATOM   602  N  N   . ILE   A 1 78  ? -0.927  -11.404 -11.827 1.00 18.78 ? 78  ILE   A N   1 
ATOM   603  C  CA  . ILE   A 1 78  ? -2.209  -11.969 -12.245 1.00 18.89 ? 78  ILE   A CA  1 
ATOM   604  C  C   . ILE   A 1 78  ? -3.373  -11.468 -11.372 1.00 20.99 ? 78  ILE   A C   1 
ATOM   605  O  O   . ILE   A 1 78  ? -4.537  -11.829 -11.561 1.00 20.91 ? 78  ILE   A O   1 
ATOM   606  C  CB  . ILE   A 1 78  ? -2.111  -13.508 -12.271 1.00 18.98 ? 78  ILE   A CB  1 
ATOM   607  C  CG1 . ILE   A 1 78  ? -1.799  -14.083 -10.892 1.00 19.11 ? 78  ILE   A CG1 1 
ATOM   608  C  CG2 . ILE   A 1 78  ? -1.074  -13.927 -13.324 1.00 18.95 ? 78  ILE   A CG2 1 
ATOM   609  C  CD1 . ILE   A 1 78  ? -1.881  -15.582 -10.795 1.00 20.35 ? 78  ILE   A CD1 1 
ATOM   610  N  N   . GLY   A 1 79  ? -3.096  -10.607 -10.397 1.00 21.00 ? 79  GLY   A N   1 
ATOM   611  C  CA  . GLY   A 1 79  ? -4.172  -10.017 -9.620  1.00 20.32 ? 79  GLY   A CA  1 
ATOM   612  C  C   . GLY   A 1 79  ? -3.663  -8.811  -8.845  1.00 19.54 ? 79  GLY   A C   1 
ATOM   613  O  O   . GLY   A 1 79  ? -2.460  -8.710  -8.565  1.00 17.59 ? 79  GLY   A O   1 
ATOM   614  N  N   . HIS   A 1 80  ? -4.580  -7.887  -8.534  1.00 19.75 ? 80  HIS   A N   1 
ATOM   615  C  CA  . HIS   A 1 80  ? -4.222  -6.753  -7.705  1.00 19.83 ? 80  HIS   A CA  1 
ATOM   616  C  C   . HIS   A 1 80  ? -5.392  -6.411  -6.786  1.00 20.87 ? 80  HIS   A C   1 
ATOM   617  O  O   . HIS   A 1 80  ? -6.562  -6.606  -7.133  1.00 16.53 ? 80  HIS   A O   1 
ATOM   618  C  CB  . HIS   A 1 80  ? -3.742  -5.584  -8.554  1.00 21.46 ? 80  HIS   A CB  1 
ATOM   619  C  CG  . HIS   A 1 80  ? -4.788  -5.036  -9.455  1.00 24.48 ? 80  HIS   A CG  1 
ATOM   620  N  ND1 . HIS   A 1 80  ? -5.065  -5.564  -10.701 1.00 25.30 ? 80  HIS   A ND1 1 
ATOM   621  C  CD2 . HIS   A 1 80  ? -5.616  -3.980  -9.293  1.00 25.48 ? 80  HIS   A CD2 1 
ATOM   622  C  CE1 . HIS   A 1 80  ? -6.050  -4.856  -11.270 1.00 24.11 ? 80  HIS   A CE1 1 
ATOM   623  N  NE2 . HIS   A 1 80  ? -6.398  -3.889  -10.433 1.00 25.27 ? 80  HIS   A NE2 1 
ATOM   624  N  N   . SER   A 1 81  ? -5.042  -5.927  -5.587  1.00 19.21 ? 81  SER   A N   1 
ATOM   625  C  CA  . SER   A 1 81  ? -5.995  -5.326  -4.672  1.00 18.00 ? 81  SER   A CA  1 
ATOM   626  C  C   . SER   A 1 81  ? -5.219  -4.409  -3.743  1.00 18.42 ? 81  SER   A C   1 
ATOM   627  O  O   . SER   A 1 81  ? -3.978  -4.329  -3.817  1.00 16.64 ? 81  SER   A O   1 
ATOM   628  C  CB  . SER   A 1 81  ? -6.760  -6.354  -3.917  1.00 20.09 ? 81  SER   A CB  1 
ATOM   629  O  OG  . SER   A 1 81  ? -5.909  -7.180  -3.151  1.00 19.75 ? 81  SER   A OG  1 
ATOM   630  N  N   . MET   A 1 82  ? -5.965  -3.672  -2.939  1.00 15.30 ? 82  MET   A N   1 
ATOM   631  C  CA  . MET   A 1 82  ? -5.384  -2.696  -2.047  1.00 15.00 ? 82  MET   A CA  1 
ATOM   632  C  C   . MET   A 1 82  ? -6.022  -2.927  -0.672  1.00 14.31 ? 82  MET   A C   1 
ATOM   633  O  O   . MET   A 1 82  ? -7.203  -3.265  -0.562  1.00 14.06 ? 82  MET   A O   1 
ATOM   634  C  CB  . MET   A 1 82  ? -5.641  -1.316  -2.654  1.00 16.61 ? 82  MET   A CB  1 
ATOM   635  C  CG  . MET   A 1 82  ? -5.586  -0.171  -1.718  1.00 16.77 ? 82  MET   A CG  1 
ATOM   636  S  SD  . MET   A 1 82  ? -5.711  1.377   -2.624  1.00 17.75 ? 82  MET   A SD  1 
ATOM   637  C  CE  . MET   A 1 82  ? -7.488  1.609   -2.654  1.00 18.74 ? 82  MET   A CE  1 
ATOM   638  N  N   . GLN   A 1 83  ? -5.188  -2.934  0.357   1.00 12.93 ? 83  GLN   A N   1 
ATOM   639  C  CA  . GLN   A 1 83  ? -5.623  -3.064  1.734   1.00 13.96 ? 83  GLN   A CA  1 
ATOM   640  C  C   . GLN   A 1 83  ? -5.050  -1.856  2.472   1.00 14.57 ? 83  GLN   A C   1 
ATOM   641  O  O   . GLN   A 1 83  ? -3.821  -1.792  2.738   1.00 12.87 ? 83  GLN   A O   1 
ATOM   642  C  CB  . GLN   A 1 83  ? -5.119  -4.366  2.358   1.00 14.03 ? 83  GLN   A CB  1 
ATOM   643  C  CG  . GLN   A 1 83  ? -5.494  -4.527  3.818   1.00 15.01 ? 83  GLN   A CG  1 
ATOM   644  C  CD  . GLN   A 1 83  ? -4.994  -5.835  4.361   1.00 16.10 ? 83  GLN   A CD  1 
ATOM   645  O  OE1 . GLN   A 1 83  ? -4.277  -6.570  3.681   1.00 17.64 ? 83  GLN   A OE1 1 
ATOM   646  N  NE2 . GLN   A 1 83  ? -5.407  -6.165  5.576   1.00 16.17 ? 83  GLN   A NE2 1 
ATOM   647  N  N   . ASN   A 1 84  ? -5.938  -0.886  2.735   1.00 13.19 ? 84  ASN   A N   1 
ATOM   648  C  CA  . ASN   A 1 84  ? -5.531  0.394   3.288   1.00 12.81 ? 84  ASN   A CA  1 
ATOM   649  C  C   . ASN   A 1 84  ? -4.422  0.980   2.413   1.00 11.81 ? 84  ASN   A C   1 
ATOM   650  O  O   . ASN   A 1 84  ? -4.610  1.114   1.202   1.00 11.21 ? 84  ASN   A O   1 
ATOM   651  C  CB  . ASN   A 1 84  ? -5.185  0.209   4.752   1.00 12.59 ? 84  ASN   A CB  1 
ATOM   652  C  CG  . ASN   A 1 84  ? -6.361  -0.360  5.500   1.00 13.85 ? 84  ASN   A CG  1 
ATOM   653  O  OD1 . ASN   A 1 84  ? -7.423  0.247   5.481   1.00 14.12 ? 84  ASN   A OD1 1 
ATOM   654  N  ND2 . ASN   A 1 84  ? -6.195  -1.500  6.142   1.00 13.65 ? 84  ASN   A ND2 1 
ATOM   655  N  N   . CYS   A 1 85  ? -3.245  1.265   2.990   1.00 11.22 ? 85  CYS   A N   1 
ATOM   656  C  CA  . CYS   A 1 85  ? -2.188  1.904   2.223   1.00 11.06 ? 85  CYS   A CA  1 
ATOM   657  C  C   . CYS   A 1 85  ? -1.214  0.931   1.546   1.00 11.07 ? 85  CYS   A C   1 
ATOM   658  O  O   . CYS   A 1 85  ? -0.240  1.392   0.939   1.00 11.57 ? 85  CYS   A O   1 
ATOM   659  C  CB  . CYS   A 1 85  ? -1.419  2.884   3.099   1.00 12.08 ? 85  CYS   A CB  1 
ATOM   660  S  SG  . CYS   A 1 85  ? -2.459  4.200   3.781   1.00 13.41 ? 85  CYS   A SG  1 
ATOM   661  N  N   . VAL   A 1 86  ? -1.481  -0.380  1.604   1.00 11.21 ? 86  VAL   A N   1 
ATOM   662  C  CA  . VAL   A 1 86  ? -0.630  -1.406  1.006   1.00 12.35 ? 86  VAL   A CA  1 
ATOM   663  C  C   . VAL   A 1 86  ? -1.307  -2.015  -0.239  1.00 13.46 ? 86  VAL   A C   1 
ATOM   664  O  O   . VAL   A 1 86  ? -2.463  -2.437  -0.172  1.00 12.39 ? 86  VAL   A O   1 
ATOM   665  C  CB  . VAL   A 1 86  ? -0.266  -2.460  2.059   1.00 13.21 ? 86  VAL   A CB  1 
ATOM   666  C  CG1 . VAL   A 1 86  ? 0.075   -3.816  1.470   1.00 14.82 ? 86  VAL   A CG1 1 
ATOM   667  C  CG2 . VAL   A 1 86  ? 0.899   -1.983  2.911   1.00 14.04 ? 86  VAL   A CG2 1 
ATOM   668  N  N   . LEU   A 1 87  ? -0.567  -2.041  -1.366  1.00 13.16 ? 87  LEU   A N   1 
ATOM   669  C  CA  . LEU   A 1 87  ? -0.980  -2.718  -2.578  1.00 13.78 ? 87  LEU   A CA  1 
ATOM   670  C  C   . LEU   A 1 87  ? -0.529  -4.174  -2.510  1.00 14.44 ? 87  LEU   A C   1 
ATOM   671  O  O   . LEU   A 1 87  ? 0.596   -4.443  -2.081  1.00 12.50 ? 87  LEU   A O   1 
ATOM   672  C  CB  . LEU   A 1 87  ? -0.343  -1.951  -3.727  1.00 15.25 ? 87  LEU   A CB  1 
ATOM   673  C  CG  . LEU   A 1 87  ? -0.689  -2.402  -5.134  1.00 17.80 ? 87  LEU   A CG  1 
ATOM   674  C  CD1 . LEU   A 1 87  ? -2.083  -1.958  -5.488  1.00 19.36 ? 87  LEU   A CD1 1 
ATOM   675  C  CD2 . LEU   A 1 87  ? 0.322   -1.857  -6.146  1.00 18.43 ? 87  LEU   A CD2 1 
ATOM   676  N  N   . LYS   A 1 88  ? -1.418  -5.108  -2.909  1.00 14.51 ? 88  LYS   A N   1 
ATOM   677  C  CA  . LYS   A 1 88  ? -1.108  -6.530  -2.916  1.00 14.64 ? 88  LYS   A CA  1 
ATOM   678  C  C   . LYS   A 1 88  ? -1.207  -7.033  -4.353  1.00 16.85 ? 88  LYS   A C   1 
ATOM   679  O  O   . LYS   A 1 88  ? -2.286  -6.999  -4.977  1.00 16.77 ? 88  LYS   A O   1 
ATOM   680  C  CB  . LYS   A 1 88  ? -2.013  -7.310  -1.963  1.00 15.50 ? 88  LYS   A CB  1 
ATOM   681  C  CG  . LYS   A 1 88  ? -1.954  -6.805  -0.529  1.00 16.78 ? 88  LYS   A CG  1 
ATOM   682  C  CD  . LYS   A 1 88  ? -2.677  -7.620  0.472   1.00 18.10 ? 88  LYS   A CD  1 
ATOM   683  C  CE  . LYS   A 1 88  ? -4.180  -7.552  0.369   1.00 21.32 ? 88  LYS   A CE  1 
ATOM   684  N  NZ  . LYS   A 1 88  ? -4.801  -8.224  1.536   1.00 20.93 ? 88  LYS   A NZ  1 
ATOM   685  N  N   . LEU   A 1 89  ? -0.063  -7.465  -4.895  1.00 15.72 ? 89  LEU   A N   1 
ATOM   686  C  CA  . LEU   A 1 89  ? -0.014  -7.944  -6.268  1.00 16.19 ? 89  LEU   A CA  1 
ATOM   687  C  C   . LEU   A 1 89  ? 0.167   -9.461  -6.267  1.00 17.23 ? 89  LEU   A C   1 
ATOM   688  O  O   . LEU   A 1 89  ? 1.194   -9.980  -5.831  1.00 16.04 ? 89  LEU   A O   1 
ATOM   689  C  CB  . LEU   A 1 89  ? 1.132   -7.247  -6.999  1.00 16.72 ? 89  LEU   A CB  1 
ATOM   690  C  CG  . LEU   A 1 89  ? 1.036   -5.734  -7.089  1.00 17.91 ? 89  LEU   A CG  1 
ATOM   691  C  CD1 . LEU   A 1 89  ? 2.242   -5.177  -7.812  1.00 18.37 ? 89  LEU   A CD1 1 
ATOM   692  C  CD2 . LEU   A 1 89  ? -0.250  -5.292  -7.770  1.00 17.40 ? 89  LEU   A CD2 1 
ATOM   693  N  N   . LYS   A 1 90  ? -0.862  -10.176 -6.741  1.00 17.99 ? 90  LYS   A N   1 
ATOM   694  C  CA  . LYS   A 1 90  ? -0.762  -11.607 -6.909  1.00 18.99 ? 90  LYS   A CA  1 
ATOM   695  C  C   . LYS   A 1 90  ? 0.087   -11.874 -8.141  1.00 16.89 ? 90  LYS   A C   1 
ATOM   696  O  O   . LYS   A 1 90  ? -0.131  -11.241 -9.150  1.00 17.08 ? 90  LYS   A O   1 
ATOM   697  C  CB  . LYS   A 1 90  ? -2.149  -12.237 -7.059  1.00 22.70 ? 90  LYS   A CB  1 
ATOM   698  C  CG  . LYS   A 1 90  ? -2.159  -13.746 -6.881  1.00 25.63 ? 90  LYS   A CG  1 
ATOM   699  C  CD  . LYS   A 1 90  ? -3.488  -14.354 -7.237  1.00 30.68 ? 90  LYS   A CD  1 
ATOM   700  C  CE  . LYS   A 1 90  ? -3.549  -15.828 -6.899  1.00 37.03 ? 90  LYS   A CE  1 
ATOM   701  N  NZ  . LYS   A 1 90  ? -3.521  -16.022 -5.427  1.00 42.38 ? 90  LYS   A NZ  1 
ATOM   702  N  N   . VAL   A 1 91  ? 1.093   -12.747 -8.014  1.00 16.76 ? 91  VAL   A N   1 
ATOM   703  C  CA  . VAL   A 1 91  ? 1.969   -13.076 -9.123  1.00 16.18 ? 91  VAL   A CA  1 
ATOM   704  C  C   . VAL   A 1 91  ? 1.818   -14.579 -9.369  1.00 16.09 ? 91  VAL   A C   1 
ATOM   705  O  O   . VAL   A 1 91  ? 1.277   -15.297 -8.532  1.00 15.46 ? 91  VAL   A O   1 
ATOM   706  C  CB  . VAL   A 1 91  ? 3.433   -12.644 -8.841  1.00 16.19 ? 91  VAL   A CB  1 
ATOM   707  C  CG1 . VAL   A 1 91  ? 3.580   -11.127 -8.829  1.00 17.02 ? 91  VAL   A CG1 1 
ATOM   708  C  CG2 . VAL   A 1 91  ? 3.988   -13.216 -7.551  1.00 16.96 ? 91  VAL   A CG2 1 
ATOM   709  N  N   . ASP   A 1 92  ? 2.321   -15.061 -10.506 1.00 18.79 ? 92  ASP   A N   1 
ATOM   710  C  CA  . ASP   A 1 92  ? 2.101   -16.438 -10.941 1.00 22.06 ? 92  ASP   A CA  1 
ATOM   711  C  C   . ASP   A 1 92  ? 3.197   -17.380 -10.426 1.00 26.10 ? 92  ASP   A C   1 
ATOM   712  O  O   . ASP   A 1 92  ? 3.213   -18.555 -10.777 1.00 25.23 ? 92  ASP   A O   1 
ATOM   713  C  CB  . ASP   A 1 92  ? 1.973   -16.485 -12.470 1.00 24.05 ? 92  ASP   A CB  1 
ATOM   714  C  CG  . ASP   A 1 92  ? 3.234   -16.126 -13.248 1.00 26.78 ? 92  ASP   A CG  1 
ATOM   715  O  OD1 . ASP   A 1 92  ? 4.251   -15.769 -12.635 1.00 29.41 ? 92  ASP   A OD1 1 
ATOM   716  O  OD2 . ASP   A 1 92  ? 3.207   -16.239 -14.479 1.00 30.07 ? 92  ASP   A OD2 1 
ATOM   717  N  N   . THR   A 1 93  ? 4.106   -16.907 -9.553  1.00 29.70 ? 93  THR   A N   1 
ATOM   718  C  CA  . THR   A 1 93  ? 5.159   -17.765 -9.018  1.00 27.72 ? 93  THR   A CA  1 
ATOM   719  C  C   . THR   A 1 93  ? 5.350   -17.532 -7.525  1.00 21.94 ? 93  THR   A C   1 
ATOM   720  O  O   . THR   A 1 93  ? 5.385   -16.393 -7.079  1.00 20.24 ? 93  THR   A O   1 
ATOM   721  C  CB  . THR   A 1 93  ? 6.483   -17.542 -9.758  1.00 33.57 ? 93  THR   A CB  1 
ATOM   722  O  OG1 . THR   A 1 93  ? 6.786   -16.158 -9.661  1.00 37.66 ? 93  THR   A OG1 1 
ATOM   723  C  CG2 . THR   A 1 93  ? 6.422   -17.962 -11.209 1.00 37.64 ? 93  THR   A CG2 1 
ATOM   724  N  N   . ALA   A 1 94  ? 5.500   -18.633 -6.785  1.00 19.24 ? 94  ALA   A N   1 
ATOM   725  C  CA  . ALA   A 1 94  ? 5.734   -18.617 -5.355  1.00 19.85 ? 94  ALA   A CA  1 
ATOM   726  C  C   . ALA   A 1 94  ? 7.211   -18.320 -5.096  1.00 19.61 ? 94  ALA   A C   1 
ATOM   727  O  O   . ALA   A 1 94  ? 8.094   -18.922 -5.730  1.00 18.84 ? 94  ALA   A O   1 
ATOM   728  C  CB  . ALA   A 1 94  ? 5.344   -19.951 -4.746  1.00 20.22 ? 94  ALA   A CB  1 
ATOM   729  N  N   . ASN   A 1 95  ? 7.478   -17.446 -4.120  1.00 17.33 ? 95  ASN   A N   1 
ATOM   730  C  CA  . ASN   A 1 95  ? 8.848   -17.191 -3.696  1.00 16.10 ? 95  ASN   A CA  1 
ATOM   731  C  C   . ASN   A 1 95  ? 9.364   -18.393 -2.906  1.00 16.65 ? 95  ASN   A C   1 
ATOM   732  O  O   . ASN   A 1 95  ? 8.922   -18.664 -1.779  1.00 16.38 ? 95  ASN   A O   1 
ATOM   733  C  CB  . ASN   A 1 95  ? 8.962   -15.902 -2.890  1.00 15.22 ? 95  ASN   A CB  1 
ATOM   734  C  CG  . ASN   A 1 95  ? 10.392  -15.548 -2.527  1.00 16.18 ? 95  ASN   A CG  1 
ATOM   735  O  OD1 . ASN   A 1 95  ? 11.333  -16.258 -2.881  1.00 16.68 ? 95  ASN   A OD1 1 
ATOM   736  N  ND2 . ASN   A 1 95  ? 10.578  -14.439 -1.823  1.00 16.27 ? 95  ASN   A ND2 1 
ATOM   737  N  N   . PRO   A 1 96  ? 10.365  -19.139 -3.412  1.00 16.38 ? 96  PRO   A N   1 
ATOM   738  C  CA  . PRO   A 1 96  ? 10.881  -20.284 -2.666  1.00 17.98 ? 96  PRO   A CA  1 
ATOM   739  C  C   . PRO   A 1 96  ? 11.623  -19.882 -1.396  1.00 17.11 ? 96  PRO   A C   1 
ATOM   740  O  O   . PRO   A 1 96  ? 11.781  -20.679 -0.478  1.00 16.76 ? 96  PRO   A O   1 
ATOM   741  C  CB  . PRO   A 1 96  ? 11.853  -20.979 -3.649  1.00 18.11 ? 96  PRO   A CB  1 
ATOM   742  C  CG  . PRO   A 1 96  ? 12.207  -19.931 -4.655  1.00 17.31 ? 96  PRO   A CG  1 
ATOM   743  C  CD  . PRO   A 1 96  ? 11.033  -18.963 -4.698  1.00 16.90 ? 96  PRO   A CD  1 
ATOM   744  N  N   . LYS   A 1 97  ? 12.059  -18.620 -1.337  1.00 18.55 ? 97  LYS   A N   1 
ATOM   745  C  CA  . LYS   A 1 97  ? 12.818  -18.151 -0.193  1.00 19.04 ? 97  LYS   A CA  1 
ATOM   746  C  C   . LYS   A 1 97  ? 11.910  -17.577 0.903   1.00 17.92 ? 97  LYS   A C   1 
ATOM   747  O  O   . LYS   A 1 97  ? 12.402  -17.023 1.863   1.00 16.06 ? 97  LYS   A O   1 
ATOM   748  C  CB  . LYS   A 1 97  ? 13.787  -17.084 -0.678  1.00 21.66 ? 97  LYS   A CB  1 
ATOM   749  C  CG  . LYS   A 1 97  ? 14.798  -17.574 -1.698  1.00 27.00 ? 97  LYS   A CG  1 
ATOM   750  C  CD  . LYS   A 1 97  ? 15.990  -16.638 -1.791  1.00 30.33 ? 97  LYS   A CD  1 
ATOM   751  C  CE  . LYS   A 1 97  ? 16.976  -17.048 -2.859  1.00 34.29 ? 97  LYS   A CE  1 
ATOM   752  N  NZ  . LYS   A 1 97  ? 16.529  -16.548 -4.183  1.00 39.25 ? 97  LYS   A NZ  1 
ATOM   753  N  N   . THR   A 1 98  ? 10.591  -17.657 0.734   1.00 17.42 ? 98  THR   A N   1 
ATOM   754  C  CA  . THR   A 1 98  ? 9.651   -17.155 1.725   1.00 16.35 ? 98  THR   A CA  1 
ATOM   755  C  C   . THR   A 1 98  ? 9.963   -17.800 3.057   1.00 16.92 ? 98  THR   A C   1 
ATOM   756  O  O   . THR   A 1 98  ? 9.920   -19.024 3.138   1.00 16.26 ? 98  THR   A O   1 
ATOM   757  C  CB  . THR   A 1 98  ? 8.196   -17.519 1.384   1.00 15.66 ? 98  THR   A CB  1 
ATOM   758  O  OG1 . THR   A 1 98  ? 7.876   -17.050 0.079   1.00 16.28 ? 98  THR   A OG1 1 
ATOM   759  C  CG2 . THR   A 1 98  ? 7.219   -16.939 2.374   1.00 16.03 ? 98  THR   A CG2 1 
ATOM   760  N  N   . PRO   A 1 99  ? 10.262  -17.032 4.134   1.00 16.62 ? 99  PRO   A N   1 
ATOM   761  C  CA  . PRO   A 1 99  ? 10.414  -17.622 5.458   1.00 16.95 ? 99  PRO   A CA  1 
ATOM   762  C  C   . PRO   A 1 99  ? 9.044   -17.832 6.096   1.00 18.35 ? 99  PRO   A C   1 
ATOM   763  O  O   . PRO   A 1 99  ? 8.040   -17.293 5.631   1.00 20.18 ? 99  PRO   A O   1 
ATOM   764  C  CB  . PRO   A 1 99  ? 11.196  -16.528 6.197   1.00 16.73 ? 99  PRO   A CB  1 
ATOM   765  C  CG  . PRO   A 1 99  ? 10.640  -15.235 5.609   1.00 16.21 ? 99  PRO   A CG  1 
ATOM   766  C  CD  . PRO   A 1 99  ? 10.438  -15.569 4.148   1.00 16.47 ? 99  PRO   A CD  1 
ATOM   767  N  N   . LYS   A 1 100 ? 9.017   -18.589 7.183   1.00 18.85 ? 100 LYS   A N   1 
ATOM   768  C  CA  . LYS   A 1 100 ? 7.903   -18.548 8.102   1.00 21.67 ? 100 LYS   A CA  1 
ATOM   769  C  C   . LYS   A 1 100 ? 7.739   -17.100 8.571   1.00 19.61 ? 100 LYS   A C   1 
ATOM   770  O  O   . LYS   A 1 100 ? 8.737   -16.460 8.939   1.00 16.70 ? 100 LYS   A O   1 
ATOM   771  C  CB  . LYS   A 1 100 ? 8.160   -19.470 9.296   1.00 27.14 ? 100 LYS   A CB  1 
ATOM   772  C  CG  . LYS   A 1 100 ? 7.045   -19.502 10.336  1.00 35.63 ? 100 LYS   A CG  1 
ATOM   773  C  CD  . LYS   A 1 100 ? 7.334   -20.417 11.514  1.00 44.43 ? 100 LYS   A CD  1 
ATOM   774  C  CE  . LYS   A 1 100 ? 6.444   -20.149 12.711  1.00 49.56 ? 100 LYS   A CE  1 
ATOM   775  N  NZ  . LYS   A 1 100 ? 5.011   -20.203 12.334  1.00 54.00 ? 100 LYS   A NZ  1 
ATOM   776  N  N   . TYR   A 1 101 ? 6.489   -16.590 8.578   1.00 16.61 ? 101 TYR   A N   1 
ATOM   777  C  CA  . TYR   A 1 101 ? 6.292   -15.192 8.933   1.00 17.20 ? 101 TYR   A CA  1 
ATOM   778  C  C   . TYR   A 1 101 ? 4.919   -14.909 9.517   1.00 18.59 ? 101 TYR   A C   1 
ATOM   779  O  O   . TYR   A 1 101 ? 3.981   -15.688 9.363   1.00 16.72 ? 101 TYR   A O   1 
ATOM   780  C  CB  . TYR   A 1 101 ? 6.502   -14.259 7.738   1.00 16.74 ? 101 TYR   A CB  1 
ATOM   781  C  CG  . TYR   A 1 101 ? 5.357   -14.269 6.752   1.00 16.65 ? 101 TYR   A CG  1 
ATOM   782  C  CD1 . TYR   A 1 101 ? 5.245   -15.277 5.788   1.00 18.52 ? 101 TYR   A CD1 1 
ATOM   783  C  CD2 . TYR   A 1 101 ? 4.355   -13.316 6.837   1.00 17.04 ? 101 TYR   A CD2 1 
ATOM   784  C  CE1 . TYR   A 1 101 ? 4.171   -15.317 4.913   1.00 19.52 ? 101 TYR   A CE1 1 
ATOM   785  C  CE2 . TYR   A 1 101 ? 3.259   -13.365 5.987   1.00 18.85 ? 101 TYR   A CE2 1 
ATOM   786  C  CZ  . TYR   A 1 101 ? 3.174   -14.356 5.026   1.00 19.43 ? 101 TYR   A CZ  1 
ATOM   787  O  OH  . TYR   A 1 101 ? 2.130   -14.382 4.159   1.00 21.40 ? 101 TYR   A OH  1 
ATOM   788  N  N   . LYS   A 1 102 ? 4.848   -13.749 10.185  1.00 19.18 ? 102 LYS   A N   1 
ATOM   789  C  CA  . LYS   A 1 102 ? 3.585   -13.131 10.549  1.00 20.78 ? 102 LYS   A CA  1 
ATOM   790  C  C   . LYS   A 1 102 ? 3.656   -11.624 10.307  1.00 16.88 ? 102 LYS   A C   1 
ATOM   791  O  O   . LYS   A 1 102 ? 4.741   -11.040 10.248  1.00 14.29 ? 102 LYS   A O   1 
ATOM   792  C  CB  . LYS   A 1 102 ? 3.288   -13.303 12.039  1.00 26.54 ? 102 LYS   A CB  1 
ATOM   793  C  CG  . LYS   A 1 102 ? 3.305   -14.732 12.571  1.00 33.26 ? 102 LYS   A CG  1 
ATOM   794  C  CD  . LYS   A 1 102 ? 3.280   -14.748 14.092  1.00 39.29 ? 102 LYS   A CD  1 
ATOM   795  C  CE  . LYS   A 1 102 ? 4.536   -14.157 14.701  1.00 46.20 ? 102 LYS   A CE  1 
ATOM   796  N  NZ  . LYS   A 1 102 ? 4.296   -13.553 16.034  1.00 52.19 ? 102 LYS   A NZ  1 
ATOM   797  N  N   . PHE   A 1 103 ? 2.477   -11.014 10.200  1.00 14.98 ? 103 PHE   A N   1 
ATOM   798  C  CA  . PHE   A 1 103 ? 2.343   -9.565  10.187  1.00 15.27 ? 103 PHE   A CA  1 
ATOM   799  C  C   . PHE   A 1 103 ? 1.876   -9.142  11.575  1.00 16.42 ? 103 PHE   A C   1 
ATOM   800  O  O   . PHE   A 1 103 ? 0.894   -9.681  12.052  1.00 17.21 ? 103 PHE   A O   1 
ATOM   801  C  CB  . PHE   A 1 103 ? 1.340   -9.134  9.126   1.00 14.35 ? 103 PHE   A CB  1 
ATOM   802  C  CG  . PHE   A 1 103 ? 1.723   -9.360  7.684   1.00 13.02 ? 103 PHE   A CG  1 
ATOM   803  C  CD1 . PHE   A 1 103 ? 3.026   -9.645  7.312   1.00 13.46 ? 103 PHE   A CD1 1 
ATOM   804  C  CD2 . PHE   A 1 103 ? 0.773   -9.240  6.689   1.00 13.03 ? 103 PHE   A CD2 1 
ATOM   805  C  CE1 . PHE   A 1 103 ? 3.367   -9.781  5.972   1.00 13.19 ? 103 PHE   A CE1 1 
ATOM   806  C  CE2 . PHE   A 1 103 ? 1.109   -9.405  5.350   1.00 13.02 ? 103 PHE   A CE2 1 
ATOM   807  C  CZ  . PHE   A 1 103 ? 2.412   -9.642  4.995   1.00 12.65 ? 103 PHE   A CZ  1 
ATOM   808  N  N   . VAL   A 1 104 ? 2.601   -8.232  12.224  1.00 16.19 ? 104 VAL   A N   1 
ATOM   809  C  CA  . VAL   A 1 104 ? 2.230   -7.761  13.549  1.00 17.52 ? 104 VAL   A CA  1 
ATOM   810  C  C   . VAL   A 1 104 ? 2.254   -6.235  13.541  1.00 17.78 ? 104 VAL   A C   1 
ATOM   811  O  O   . VAL   A 1 104 ? 3.034   -5.633  12.818  1.00 17.58 ? 104 VAL   A O   1 
ATOM   812  C  CB  . VAL   A 1 104 ? 3.174   -8.309  14.637  1.00 19.61 ? 104 VAL   A CB  1 
ATOM   813  C  CG1 . VAL   A 1 104 ? 3.243   -9.839  14.640  1.00 21.14 ? 104 VAL   A CG1 1 
ATOM   814  C  CG2 . VAL   A 1 104 ? 4.566   -7.717  14.523  1.00 20.55 ? 104 VAL   A CG2 1 
ATOM   815  N  N   . ARG   A 1 105 ? 1.472   -5.629  14.431  1.00 17.22 ? 105 ARG   A N   1 
ATOM   816  C  CA  . ARG   A 1 105 ? 1.526   -4.201  14.675  1.00 17.37 ? 105 ARG   A CA  1 
ATOM   817  C  C   . ARG   A 1 105 ? 2.184   -3.978  16.033  1.00 17.77 ? 105 ARG   A C   1 
ATOM   818  O  O   . ARG   A 1 105 ? 1.716   -4.494  17.036  1.00 17.54 ? 105 ARG   A O   1 
ATOM   819  C  CB  . ARG   A 1 105 ? 0.124   -3.603  14.655  1.00 17.20 ? 105 ARG   A CB  1 
ATOM   820  C  CG  . ARG   A 1 105 ? 0.146   -2.083  14.778  1.00 17.42 ? 105 ARG   A CG  1 
ATOM   821  C  CD  . ARG   A 1 105 ? -1.193  -1.447  14.519  1.00 15.87 ? 105 ARG   A CD  1 
ATOM   822  N  NE  . ARG   A 1 105 ? -1.064  -0.008  14.689  1.00 15.06 ? 105 ARG   A NE  1 
ATOM   823  C  CZ  . ARG   A 1 105 ? -1.007  0.873   13.704  1.00 13.77 ? 105 ARG   A CZ  1 
ATOM   824  N  NH1 . ARG   A 1 105 ? -0.866  0.513   12.437  1.00 13.68 ? 105 ARG   A NH1 1 
ATOM   825  N  NH2 . ARG   A 1 105 ? -1.043  2.146   14.016  1.00 14.00 ? 105 ARG   A NH2 1 
ATOM   826  N  N   . ILE   A 1 106 ? 3.306   -3.260  16.048  1.00 17.54 ? 106 ILE   A N   1 
ATOM   827  C  CA  . ILE   A 1 106 ? 4.035   -3.038  17.289  1.00 18.63 ? 106 ILE   A CA  1 
ATOM   828  C  C   . ILE   A 1 106 ? 3.502   -1.808  18.023  1.00 16.28 ? 106 ILE   A C   1 
ATOM   829  O  O   . ILE   A 1 106 ? 2.814   -0.980  17.439  1.00 14.04 ? 106 ILE   A O   1 
ATOM   830  C  CB  . ILE   A 1 106 ? 5.547   -2.909  17.030  1.00 19.66 ? 106 ILE   A CB  1 
ATOM   831  C  CG1 . ILE   A 1 106 ? 5.855   -1.799  16.032  1.00 19.62 ? 106 ILE   A CG1 1 
ATOM   832  C  CG2 . ILE   A 1 106 ? 6.136   -4.253  16.614  1.00 23.22 ? 106 ILE   A CG2 1 
ATOM   833  C  CD1 . ILE   A 1 106 ? 7.305   -1.411  15.995  1.00 20.10 ? 106 ILE   A CD1 1 
ATOM   834  N  N   . GLN   A 1 107 ? 3.915   -1.684  19.288  1.00 17.63 ? 107 GLN   A N   1 
ATOM   835  C  CA  . GLN   A 1 107 ? 3.561   -0.564  20.147  1.00 20.62 ? 107 GLN   A CA  1 
ATOM   836  C  C   . GLN   A 1 107 ? 4.733   0.410   20.198  1.00 18.10 ? 107 GLN   A C   1 
ATOM   837  O  O   . GLN   A 1 107 ? 5.884   0.030   19.980  1.00 15.11 ? 107 GLN   A O   1 
ATOM   838  C  CB  . GLN   A 1 107 ? 3.319   -0.998  21.598  1.00 25.98 ? 107 GLN   A CB  1 
ATOM   839  C  CG  . GLN   A 1 107 ? 2.443   -2.226  21.786  1.00 32.66 ? 107 GLN   A CG  1 
ATOM   840  C  CD  . GLN   A 1 107 ? 0.978   -1.891  21.731  1.00 39.17 ? 107 GLN   A CD  1 
ATOM   841  O  OE1 . GLN   A 1 107 ? 0.230   -2.439  20.927  1.00 49.27 ? 107 GLN   A OE1 1 
ATOM   842  N  NE2 . GLN   A 1 107 ? 0.550   -0.997  22.604  1.00 42.89 ? 107 GLN   A NE2 1 
ATOM   843  N  N   . PRO   A 1 108 ? 4.486   1.693   20.528  1.00 19.18 ? 108 PRO   A N   1 
ATOM   844  C  CA  . PRO   A 1 108 ? 5.568   2.644   20.742  1.00 19.66 ? 108 PRO   A CA  1 
ATOM   845  C  C   . PRO   A 1 108 ? 6.508   2.074   21.785  1.00 17.04 ? 108 PRO   A C   1 
ATOM   846  O  O   . PRO   A 1 108 ? 6.064   1.476   22.766  1.00 15.99 ? 108 PRO   A O   1 
ATOM   847  C  CB  . PRO   A 1 108 ? 4.888   3.924   21.260  1.00 21.16 ? 108 PRO   A CB  1 
ATOM   848  C  CG  . PRO   A 1 108 ? 3.456   3.795   20.829  1.00 21.14 ? 108 PRO   A CG  1 
ATOM   849  C  CD  . PRO   A 1 108 ? 3.164   2.309   20.707  1.00 21.74 ? 108 PRO   A CD  1 
ATOM   850  N  N   . GLY   A 1 109 ? 7.802   2.258   21.553  1.00 16.24 ? 109 GLY   A N   1 
ATOM   851  C  CA  . GLY   A 1 109 ? 8.803   1.761   22.474  1.00 16.38 ? 109 GLY   A CA  1 
ATOM   852  C  C   . GLY   A 1 109 ? 9.435   0.459   22.014  1.00 16.94 ? 109 GLY   A C   1 
ATOM   853  O  O   . GLY   A 1 109 ? 10.536  0.147   22.451  1.00 18.58 ? 109 GLY   A O   1 
ATOM   854  N  N   . GLN   A 1 110 ? 8.711   -0.314  21.193  1.00 15.58 ? 110 GLN   A N   1 
ATOM   855  C  CA  . GLN   A 1 110 ? 9.203   -1.589  20.724  1.00 16.65 ? 110 GLN   A CA  1 
ATOM   856  C  C   . GLN   A 1 110 ? 10.193  -1.305  19.601  1.00 14.61 ? 110 GLN   A C   1 
ATOM   857  O  O   . GLN   A 1 110 ? 10.042  -0.313  18.893  1.00 14.59 ? 110 GLN   A O   1 
ATOM   858  C  CB  . GLN   A 1 110 ? 8.070   -2.510  20.284  1.00 19.44 ? 110 GLN   A CB  1 
ATOM   859  C  CG  . GLN   A 1 110 ? 7.122   -2.821  21.445  1.00 24.04 ? 110 GLN   A CG  1 
ATOM   860  C  CD  . GLN   A 1 110 ? 6.119   -3.929  21.195  1.00 29.68 ? 110 GLN   A CD  1 
ATOM   861  O  OE1 . GLN   A 1 110 ? 5.304   -3.916  20.267  1.00 26.32 ? 110 GLN   A OE1 1 
ATOM   862  N  NE2 . GLN   A 1 110 ? 6.152   -4.919  22.076  1.00 38.49 ? 110 GLN   A NE2 1 
ATOM   863  N  N   . THR   A 1 111 ? 11.201  -2.175  19.495  1.00 12.73 ? 111 THR   A N   1 
ATOM   864  C  CA  . THR   A 1 111 ? 12.266  -2.043  18.520  1.00 12.58 ? 111 THR   A CA  1 
ATOM   865  C  C   . THR   A 1 111 ? 12.087  -3.060  17.390  1.00 11.22 ? 111 THR   A C   1 
ATOM   866  O  O   . THR   A 1 111 ? 11.378  -4.042  17.509  1.00 10.42 ? 111 THR   A O   1 
ATOM   867  C  CB  . THR   A 1 111 ? 13.641  -2.196  19.182  1.00 13.06 ? 111 THR   A CB  1 
ATOM   868  O  OG1 . THR   A 1 111 ? 13.613  -3.423  19.913  1.00 13.79 ? 111 THR   A OG1 1 
ATOM   869  C  CG2 . THR   A 1 111 ? 13.988  -1.031  20.084  1.00 13.82 ? 111 THR   A CG2 1 
ATOM   870  N  N   . PHE   A 1 112 ? 12.809  -2.838  16.303  1.00 11.10 ? 112 PHE   A N   1 
ATOM   871  C  CA  . PHE   A 1 112 ? 12.792  -3.718  15.156  1.00 10.83 ? 112 PHE   A CA  1 
ATOM   872  C  C   . PHE   A 1 112 ? 13.997  -3.391  14.290  1.00 10.71 ? 112 PHE   A C   1 
ATOM   873  O  O   . PHE   A 1 112 ? 14.558  -2.305  14.380  1.00 10.49 ? 112 PHE   A O   1 
ATOM   874  C  CB  . PHE   A 1 112 ? 11.495  -3.578  14.356  1.00 11.08 ? 112 PHE   A CB  1 
ATOM   875  C  CG  . PHE   A 1 112 ? 11.170  -2.187  13.892  1.00 12.13 ? 112 PHE   A CG  1 
ATOM   876  C  CD1 . PHE   A 1 112 ? 10.530  -1.289  14.725  1.00 13.50 ? 112 PHE   A CD1 1 
ATOM   877  C  CD2 . PHE   A 1 112 ? 11.506  -1.763  12.623  1.00 13.48 ? 112 PHE   A CD2 1 
ATOM   878  C  CE1 . PHE   A 1 112 ? 10.186  -0.014  14.281  1.00 14.43 ? 112 PHE   A CE1 1 
ATOM   879  C  CE2 . PHE   A 1 112 ? 11.209  -0.475  12.196  1.00 14.11 ? 112 PHE   A CE2 1 
ATOM   880  C  CZ  . PHE   A 1 112 ? 10.534  0.392   13.014  1.00 13.65 ? 112 PHE   A CZ  1 
ATOM   881  N  N   . SER   A 1 113 ? 14.356  -4.352  13.452  1.00 10.37 ? 113 SER   A N   1 
ATOM   882  C  CA  . SER   A 1 113 ? 15.411  -4.205  12.478  1.00 10.04 ? 113 SER   A CA  1 
ATOM   883  C  C   . SER   A 1 113 ? 14.817  -3.687  11.177  1.00 10.60 ? 113 SER   A C   1 
ATOM   884  O  O   . SER   A 1 113 ? 13.758  -4.135  10.755  1.00 11.55 ? 113 SER   A O   1 
ATOM   885  C  CB  . SER   A 1 113 ? 16.104  -5.519  12.266  1.00 9.60  ? 113 SER   A CB  1 
ATOM   886  O  OG  . SER   A 1 113 ? 16.655  -6.013  13.475  1.00 9.32  ? 113 SER   A OG  1 
ATOM   887  N  N   . VAL   A 1 114 ? 15.522  -2.753  10.531  1.00 11.59 ? 114 VAL   A N   1 
ATOM   888  C  CA  . VAL   A 1 114 ? 15.124  -2.245  9.227   1.00 11.46 ? 114 VAL   A CA  1 
ATOM   889  C  C   . VAL   A 1 114 ? 16.131  -2.749  8.208   1.00 9.91  ? 114 VAL   A C   1 
ATOM   890  O  O   . VAL   A 1 114 ? 17.313  -2.639  8.465   1.00 10.19 ? 114 VAL   A O   1 
ATOM   891  C  CB  . VAL   A 1 114 ? 15.059  -0.710  9.238   1.00 12.42 ? 114 VAL   A CB  1 
ATOM   892  C  CG1 . VAL   A 1 114 ? 14.973  -0.128  7.834   1.00 12.47 ? 114 VAL   A CG1 1 
ATOM   893  C  CG2 . VAL   A 1 114 ? 13.905  -0.208  10.090  1.00 13.15 ? 114 VAL   A CG2 1 
ATOM   894  N  N   . LEU   A 1 115 ? 15.641  -3.268  7.078   1.00 9.92  ? 115 LEU   A N   1 
ATOM   895  C  CA  . LEU   A 1 115 ? 16.457  -3.549  5.895   1.00 10.60 ? 115 LEU   A CA  1 
ATOM   896  C  C   . LEU   A 1 115 ? 16.185  -2.473  4.848   1.00 10.79 ? 115 LEU   A C   1 
ATOM   897  O  O   . LEU   A 1 115 ? 15.134  -2.483  4.185   1.00 12.24 ? 115 LEU   A O   1 
ATOM   898  C  CB  . LEU   A 1 115 ? 16.139  -4.936  5.330   1.00 10.52 ? 115 LEU   A CB  1 
ATOM   899  C  CG  . LEU   A 1 115 ? 16.955  -5.343  4.109   1.00 11.53 ? 115 LEU   A CG  1 
ATOM   900  C  CD1 . LEU   A 1 115 ? 18.439  -5.492  4.452   1.00 11.23 ? 115 LEU   A CD1 1 
ATOM   901  C  CD2 . LEU   A 1 115 ? 16.419  -6.640  3.528   1.00 12.30 ? 115 LEU   A CD2 1 
ATOM   902  N  N   . ALA   A 1 116 ? 17.062  -1.476  4.777   1.00 10.83 ? 116 ALA   A N   1 
ATOM   903  C  CA  . ALA   A 1 116 ? 16.915  -0.418  3.781   1.00 11.64 ? 116 ALA   A CA  1 
ATOM   904  C  C   . ALA   A 1 116 ? 17.256  -0.980  2.395   1.00 12.40 ? 116 ALA   A C   1 
ATOM   905  O  O   . ALA   A 1 116 ? 18.280  -1.645  2.224   1.00 12.48 ? 116 ALA   A O   1 
ATOM   906  C  CB  . ALA   A 1 116 ? 17.813  0.759   4.130   1.00 11.76 ? 116 ALA   A CB  1 
ATOM   907  N  N   A CYS   A 1 117 ? 16.368  -0.751  1.423   0.78 12.43 ? 117 CYS   A N   1 
ATOM   908  N  N   B CYS   A 1 117 ? 16.395  -0.673  1.421   0.22 12.25 ? 117 CYS   A N   1 
ATOM   909  C  CA  A CYS   A 1 117 ? 16.546  -1.255  0.070   0.78 13.11 ? 117 CYS   A CA  1 
ATOM   910  C  CA  B CYS   A 1 117 ? 16.482  -1.238  0.087   0.22 12.45 ? 117 CYS   A CA  1 
ATOM   911  C  C   A CYS   A 1 117 ? 16.309  -0.127  -0.928  0.78 12.94 ? 117 CYS   A C   1 
ATOM   912  C  C   B CYS   A 1 117 ? 16.283  -0.125  -0.941  0.22 12.75 ? 117 CYS   A C   1 
ATOM   913  O  O   A CYS   A 1 117 ? 15.574  0.808   -0.638  0.78 11.81 ? 117 CYS   A O   1 
ATOM   914  O  O   B CYS   A 1 117 ? 15.549  0.821   -0.675  0.22 12.26 ? 117 CYS   A O   1 
ATOM   915  C  CB  A CYS   A 1 117 ? 15.561  -2.369  -0.253  0.78 13.93 ? 117 CYS   A CB  1 
ATOM   916  C  CB  B CYS   A 1 117 ? 15.406  -2.303  -0.065  0.22 12.42 ? 117 CYS   A CB  1 
ATOM   917  S  SG  A CYS   A 1 117 ? 15.643  -3.766  0.885   0.78 16.10 ? 117 CYS   A SG  1 
ATOM   918  S  SG  B CYS   A 1 117 ? 15.772  -3.549  -1.318  0.22 12.26 ? 117 CYS   A SG  1 
ATOM   919  N  N   . TYR   A 1 118 ? 16.947  -0.246  -2.099  1.00 13.21 ? 118 TYR   A N   1 
ATOM   920  C  CA  . TYR   A 1 118 ? 16.852  0.720   -3.192  1.00 14.90 ? 118 TYR   A CA  1 
ATOM   921  C  C   . TYR   A 1 118 ? 16.738  -0.097  -4.480  1.00 15.80 ? 118 TYR   A C   1 
ATOM   922  O  O   . TYR   A 1 118 ? 17.569  -0.973  -4.723  1.00 16.46 ? 118 TYR   A O   1 
ATOM   923  C  CB  . TYR   A 1 118 ? 18.057  1.680   -3.213  1.00 15.09 ? 118 TYR   A CB  1 
ATOM   924  C  CG  . TYR   A 1 118 ? 18.125  2.464   -1.915  1.00 15.21 ? 118 TYR   A CG  1 
ATOM   925  C  CD1 . TYR   A 1 118 ? 17.337  3.602   -1.728  1.00 14.68 ? 118 TYR   A CD1 1 
ATOM   926  C  CD2 . TYR   A 1 118 ? 18.864  2.003   -0.828  1.00 14.12 ? 118 TYR   A CD2 1 
ATOM   927  C  CE1 . TYR   A 1 118 ? 17.319  4.276   -0.521  1.00 13.69 ? 118 TYR   A CE1 1 
ATOM   928  C  CE2 . TYR   A 1 118 ? 18.838  2.669   0.387   1.00 13.62 ? 118 TYR   A CE2 1 
ATOM   929  C  CZ  . TYR   A 1 118 ? 18.075  3.815   0.540   1.00 13.25 ? 118 TYR   A CZ  1 
ATOM   930  O  OH  . TYR   A 1 118 ? 18.015  4.468   1.748   1.00 13.32 ? 118 TYR   A OH  1 
ATOM   931  N  N   . ASN   A 1 119 ? 15.664  0.124   -5.247  1.00 18.49 ? 119 ASN   A N   1 
ATOM   932  C  CA  . ASN   A 1 119 ? 15.427  -0.601  -6.494  1.00 20.66 ? 119 ASN   A CA  1 
ATOM   933  C  C   . ASN   A 1 119 ? 15.365  -2.115  -6.274  1.00 19.76 ? 119 ASN   A C   1 
ATOM   934  O  O   . ASN   A 1 119 ? 15.873  -2.874  -7.079  1.00 19.93 ? 119 ASN   A O   1 
ATOM   935  C  CB  . ASN   A 1 119 ? 16.503  -0.245  -7.524  1.00 22.62 ? 119 ASN   A CB  1 
ATOM   936  C  CG  . ASN   A 1 119 ? 16.561  1.248   -7.783  1.00 29.33 ? 119 ASN   A CG  1 
ATOM   937  O  OD1 . ASN   A 1 119 ? 17.589  1.907   -7.564  1.00 30.78 ? 119 ASN   A OD1 1 
ATOM   938  N  ND2 . ASN   A 1 119 ? 15.427  1.802   -8.197  1.00 30.74 ? 119 ASN   A ND2 1 
ATOM   939  N  N   . GLY   A 1 120 ? 14.754  -2.556  -5.173  1.00 19.92 ? 120 GLY   A N   1 
ATOM   940  C  CA  . GLY   A 1 120 ? 14.640  -3.965  -4.837  1.00 18.04 ? 120 GLY   A CA  1 
ATOM   941  C  C   . GLY   A 1 120 ? 15.936  -4.616  -4.339  1.00 18.02 ? 120 GLY   A C   1 
ATOM   942  O  O   . GLY   A 1 120 ? 15.914  -5.800  -4.050  1.00 19.10 ? 120 GLY   A O   1 
ATOM   943  N  N   . SER   A 1 121 ? 17.031  -3.850  -4.195  1.00 17.24 ? 121 SER   A N   1 
ATOM   944  C  CA  A SER   A 1 121 ? 18.321  -4.380  -3.765  0.46 16.23 ? 121 SER   A CA  1 
ATOM   945  C  CA  B SER   A 1 121 ? 18.320  -4.379  -3.765  0.54 16.49 ? 121 SER   A CA  1 
ATOM   946  C  C   . SER   A 1 121 ? 18.628  -3.939  -2.335  1.00 15.39 ? 121 SER   A C   1 
ATOM   947  O  O   . SER   A 1 121 ? 18.745  -2.741  -2.057  1.00 13.17 ? 121 SER   A O   1 
ATOM   948  C  CB  A SER   A 1 121 ? 19.423  -3.956  -4.702  0.46 16.71 ? 121 SER   A CB  1 
ATOM   949  C  CB  B SER   A 1 121 ? 19.420  -3.936  -4.686  0.54 17.33 ? 121 SER   A CB  1 
ATOM   950  O  OG  A SER   A 1 121 ? 19.245  -4.561  -5.976  0.46 15.94 ? 121 SER   A OG  1 
ATOM   951  O  OG  B SER   A 1 121 ? 20.624  -4.596  -4.353  0.54 17.02 ? 121 SER   A OG  1 
ATOM   952  N  N   . PRO   A 1 122 ? 18.803  -4.884  -1.387  1.00 13.82 ? 122 PRO   A N   1 
ATOM   953  C  CA  . PRO   A 1 122 ? 19.136  -4.511  -0.016  1.00 13.90 ? 122 PRO   A CA  1 
ATOM   954  C  C   . PRO   A 1 122 ? 20.466  -3.773  0.090   1.00 13.17 ? 122 PRO   A C   1 
ATOM   955  O  O   . PRO   A 1 122 ? 21.432  -4.164  -0.536  1.00 12.76 ? 122 PRO   A O   1 
ATOM   956  C  CB  . PRO   A 1 122 ? 19.180  -5.874  0.711   1.00 14.69 ? 122 PRO   A CB  1 
ATOM   957  C  CG  . PRO   A 1 122 ? 18.333  -6.777  -0.139  1.00 15.64 ? 122 PRO   A CG  1 
ATOM   958  C  CD  . PRO   A 1 122 ? 18.631  -6.342  -1.557  1.00 14.58 ? 122 PRO   A CD  1 
ATOM   959  N  N   A SER   A 1 123 ? 20.510  -2.730  0.925   0.44 13.49 ? 123 SER   A N   1 
ATOM   960  N  N   B SER   A 1 123 ? 20.506  -2.718  0.913   0.56 13.14 ? 123 SER   A N   1 
ATOM   961  C  CA  A SER   A 1 123 ? 21.680  -1.874  1.018   0.44 13.82 ? 123 SER   A CA  1 
ATOM   962  C  CA  B SER   A 1 123 ? 21.674  -1.859  1.019   0.56 13.18 ? 123 SER   A CA  1 
ATOM   963  C  C   A SER   A 1 123 ? 22.244  -1.856  2.437   0.44 13.48 ? 123 SER   A C   1 
ATOM   964  C  C   B SER   A 1 123 ? 22.243  -1.869  2.436   0.56 13.16 ? 123 SER   A C   1 
ATOM   965  O  O   A SER   A 1 123 ? 23.454  -1.737  2.611   0.44 13.16 ? 123 SER   A O   1 
ATOM   966  O  O   B SER   A 1 123 ? 23.456  -1.779  2.609   0.56 12.85 ? 123 SER   A O   1 
ATOM   967  C  CB  A SER   A 1 123 ? 21.358  -0.487  0.538   0.44 14.37 ? 123 SER   A CB  1 
ATOM   968  C  CB  B SER   A 1 123 ? 21.356  -0.455  0.557   0.56 13.26 ? 123 SER   A CB  1 
ATOM   969  O  OG  A SER   A 1 123 ? 20.399  0.124   1.390   0.44 15.53 ? 123 SER   A OG  1 
ATOM   970  O  OG  B SER   A 1 123 ? 22.267  0.496   1.109   0.56 13.28 ? 123 SER   A OG  1 
ATOM   971  N  N   . GLY   A 1 124 ? 21.377  -1.927  3.456   1.00 13.14 ? 124 GLY   A N   1 
ATOM   972  C  CA  . GLY   A 1 124 ? 21.863  -1.873  4.837   1.00 13.01 ? 124 GLY   A CA  1 
ATOM   973  C  C   . GLY   A 1 124 ? 20.815  -2.281  5.857   1.00 12.38 ? 124 GLY   A C   1 
ATOM   974  O  O   . GLY   A 1 124 ? 19.638  -2.314  5.534   1.00 12.51 ? 124 GLY   A O   1 
ATOM   975  N  N   . VAL   A 1 125 ? 21.278  -2.603  7.061   1.00 12.49 ? 125 VAL   A N   1 
ATOM   976  C  CA  . VAL   A 1 125 ? 20.429  -3.057  8.140   1.00 14.00 ? 125 VAL   A CA  1 
ATOM   977  C  C   . VAL   A 1 125 ? 20.855  -2.360  9.435   1.00 14.99 ? 125 VAL   A C   1 
ATOM   978  O  O   . VAL   A 1 125 ? 22.052  -2.159  9.713   1.00 13.48 ? 125 VAL   A O   1 
ATOM   979  C  CB  . VAL   A 1 125 ? 20.446  -4.599  8.237   1.00 16.61 ? 125 VAL   A CB  1 
ATOM   980  C  CG1 . VAL   A 1 125 ? 21.844  -5.127  8.490   1.00 19.00 ? 125 VAL   A CG1 1 
ATOM   981  C  CG2 . VAL   A 1 125 ? 19.486  -5.119  9.295   1.00 16.44 ? 125 VAL   A CG2 1 
ATOM   982  N  N   . TYR   A 1 126 ? 19.839  -1.970  10.213  1.00 14.93 ? 126 TYR   A N   1 
ATOM   983  C  CA  . TYR   A 1 126 ? 20.040  -1.332  11.508  1.00 15.83 ? 126 TYR   A CA  1 
ATOM   984  C  C   . TYR   A 1 126 ? 18.790  -1.450  12.368  1.00 14.81 ? 126 TYR   A C   1 
ATOM   985  O  O   . TYR   A 1 126 ? 17.714  -1.731  11.857  1.00 14.79 ? 126 TYR   A O   1 
ATOM   986  C  CB  . TYR   A 1 126 ? 20.357  0.152   11.305  1.00 17.42 ? 126 TYR   A CB  1 
ATOM   987  C  CG  . TYR   A 1 126 ? 19.313  0.912   10.491  1.00 18.49 ? 126 TYR   A CG  1 
ATOM   988  C  CD1 . TYR   A 1 126 ? 18.212  1.492   11.106  1.00 19.53 ? 126 TYR   A CD1 1 
ATOM   989  C  CD2 . TYR   A 1 126 ? 19.446  1.065   9.117   1.00 17.98 ? 126 TYR   A CD2 1 
ATOM   990  C  CE1 . TYR   A 1 126 ? 17.272  2.213   10.381  1.00 21.27 ? 126 TYR   A CE1 1 
ATOM   991  C  CE2 . TYR   A 1 126 ? 18.513  1.773   8.377   1.00 18.93 ? 126 TYR   A CE2 1 
ATOM   992  C  CZ  . TYR   A 1 126 ? 17.430  2.355   9.012   1.00 20.99 ? 126 TYR   A CZ  1 
ATOM   993  O  OH  . TYR   A 1 126 ? 16.511  3.067   8.296   1.00 22.55 ? 126 TYR   A OH  1 
ATOM   994  N  N   . GLN   A 1 127 ? 18.959  -1.186  13.660  1.00 15.10 ? 127 GLN   A N   1 
ATOM   995  C  CA  . GLN   A 1 127 ? 17.896  -1.201  14.639  1.00 17.75 ? 127 GLN   A CA  1 
ATOM   996  C  C   . GLN   A 1 127 ? 17.255  0.166   14.815  1.00 18.48 ? 127 GLN   A C   1 
ATOM   997  O  O   . GLN   A 1 127 ? 17.980  1.151   14.904  1.00 19.49 ? 127 GLN   A O   1 
ATOM   998  C  CB  . GLN   A 1 127 ? 18.437  -1.472  16.044  1.00 20.68 ? 127 GLN   A CB  1 
ATOM   999  C  CG  . GLN   A 1 127 ? 18.619  -2.929  16.327  1.00 22.56 ? 127 GLN   A CG  1 
ATOM   1000 C  CD  . GLN   A 1 127 ? 17.324  -3.694  16.401  1.00 22.21 ? 127 GLN   A CD  1 
ATOM   1001 O  OE1 . GLN   A 1 127 ? 16.675  -3.758  17.440  1.00 23.63 ? 127 GLN   A OE1 1 
ATOM   1002 N  NE2 . GLN   A 1 127 ? 17.015  -4.393  15.324  1.00 22.02 ? 127 GLN   A NE2 1 
ATOM   1003 N  N   . CYS   A 1 128 ? 15.936  0.150   15.031  1.00 16.83 ? 128 CYS   A N   1 
ATOM   1004 C  CA  . CYS   A 1 128 ? 15.087  1.318   15.208  1.00 19.48 ? 128 CYS   A CA  1 
ATOM   1005 C  C   . CYS   A 1 128 ? 14.070  1.046   16.311  1.00 16.41 ? 128 CYS   A C   1 
ATOM   1006 O  O   . CYS   A 1 128 ? 13.752  -0.106  16.596  1.00 14.95 ? 128 CYS   A O   1 
ATOM   1007 C  CB  . CYS   A 1 128 ? 14.260  1.580   13.942  1.00 22.34 ? 128 CYS   A CB  1 
ATOM   1008 S  SG  . CYS   A 1 128 ? 15.012  2.808   12.887  1.00 42.54 ? 128 CYS   A SG  1 
ATOM   1009 N  N   . ALA   A 1 129 ? 13.519  2.118   16.884  1.00 16.54 ? 129 ALA   A N   1 
ATOM   1010 C  CA  . ALA   A 1 129 ? 12.347  2.014   17.742  1.00 15.72 ? 129 ALA   A CA  1 
ATOM   1011 C  C   . ALA   A 1 129 ? 11.222  2.839   17.139  1.00 14.73 ? 129 ALA   A C   1 
ATOM   1012 O  O   . ALA   A 1 129 ? 11.446  3.894   16.561  1.00 14.73 ? 129 ALA   A O   1 
ATOM   1013 C  CB  . ALA   A 1 129 ? 12.631  2.430   19.165  1.00 15.70 ? 129 ALA   A CB  1 
ATOM   1014 N  N   . MET   A 1 130 ? 10.015  2.317   17.291  1.00 14.38 ? 130 MET   A N   1 
ATOM   1015 C  CA  . MET   A 1 130 ? 8.805   3.086   17.103  1.00 16.14 ? 130 MET   A CA  1 
ATOM   1016 C  C   . MET   A 1 130 ? 8.736   4.107   18.239  1.00 15.74 ? 130 MET   A C   1 
ATOM   1017 O  O   . MET   A 1 130 ? 8.644   3.714   19.388  1.00 16.57 ? 130 MET   A O   1 
ATOM   1018 C  CB  . MET   A 1 130 ? 7.588   2.155   17.168  1.00 16.76 ? 130 MET   A CB  1 
ATOM   1019 C  CG  . MET   A 1 130 ? 6.221   2.850   16.950  1.00 18.16 ? 130 MET   A CG  1 
ATOM   1020 S  SD  . MET   A 1 130 ? 6.109   3.625   15.327  1.00 19.78 ? 130 MET   A SD  1 
ATOM   1021 C  CE  . MET   A 1 130 ? 6.287   2.194   14.253  1.00 19.06 ? 130 MET   A CE  1 
ATOM   1022 N  N   . ARG   A 1 131 ? 8.822   5.386   17.893  1.00 14.74 ? 131 ARG   A N   1 
ATOM   1023 C  CA  . ARG   A 1 131 ? 8.754   6.484   18.840  1.00 14.56 ? 131 ARG   A CA  1 
ATOM   1024 C  C   . ARG   A 1 131 ? 7.345   6.593   19.418  1.00 14.52 ? 131 ARG   A C   1 
ATOM   1025 O  O   . ARG   A 1 131 ? 6.351   6.259   18.762  1.00 13.20 ? 131 ARG   A O   1 
ATOM   1026 C  CB  . ARG   A 1 131 ? 9.093   7.818   18.168  1.00 13.73 ? 131 ARG   A CB  1 
ATOM   1027 C  CG  . ARG   A 1 131 ? 10.456  7.911   17.498  1.00 14.98 ? 131 ARG   A CG  1 
ATOM   1028 C  CD  . ARG   A 1 131 ? 11.600  7.540   18.387  1.00 14.76 ? 131 ARG   A CD  1 
ATOM   1029 N  NE  . ARG   A 1 131 ? 11.566  8.344   19.615  1.00 16.50 ? 131 ARG   A NE  1 
ATOM   1030 C  CZ  . ARG   A 1 131 ? 12.320  8.079   20.675  1.00 15.64 ? 131 ARG   A CZ  1 
ATOM   1031 N  NH1 . ARG   A 1 131 ? 13.260  7.154   20.590  1.00 14.73 ? 131 ARG   A NH1 1 
ATOM   1032 N  NH2 . ARG   A 1 131 ? 12.126  8.729   21.802  1.00 14.46 ? 131 ARG   A NH2 1 
ATOM   1033 N  N   . PRO   A 1 132 ? 7.194   7.123   20.649  1.00 15.10 ? 132 PRO   A N   1 
ATOM   1034 C  CA  . PRO   A 1 132 ? 5.861   7.427   21.181  1.00 15.01 ? 132 PRO   A CA  1 
ATOM   1035 C  C   . PRO   A 1 132 ? 4.964   8.286   20.285  1.00 13.55 ? 132 PRO   A C   1 
ATOM   1036 O  O   . PRO   A 1 132 ? 3.757   8.087   20.321  1.00 15.27 ? 132 PRO   A O   1 
ATOM   1037 C  CB  . PRO   A 1 132 ? 6.177   8.128   22.514  1.00 15.17 ? 132 PRO   A CB  1 
ATOM   1038 C  CG  . PRO   A 1 132 ? 7.498   7.533   22.908  1.00 16.48 ? 132 PRO   A CG  1 
ATOM   1039 C  CD  . PRO   A 1 132 ? 8.267   7.441   21.601  1.00 15.88 ? 132 PRO   A CD  1 
ATOM   1040 N  N   . ASN   A 1 133 ? 5.534   9.180   19.460  1.00 12.36 ? 133 ASN   A N   1 
ATOM   1041 C  CA  . ASN   A 1 133 ? 4.755   9.950   18.491  1.00 13.25 ? 133 ASN   A CA  1 
ATOM   1042 C  C   . ASN   A 1 133 ? 4.559   9.228   17.143  1.00 13.72 ? 133 ASN   A C   1 
ATOM   1043 O  O   . ASN   A 1 133 ? 4.123   9.855   16.171  1.00 13.56 ? 133 ASN   A O   1 
ATOM   1044 C  CB  . ASN   A 1 133 ? 5.360   11.333  18.222  1.00 13.02 ? 133 ASN   A CB  1 
ATOM   1045 C  CG  . ASN   A 1 133 ? 6.666   11.358  17.447  1.00 13.10 ? 133 ASN   A CG  1 
ATOM   1046 O  OD1 . ASN   A 1 133 ? 7.256   10.331  17.092  1.00 12.86 ? 133 ASN   A OD1 1 
ATOM   1047 N  ND2 . ASN   A 1 133 ? 7.155   12.565  17.220  1.00 12.06 ? 133 ASN   A ND2 1 
ATOM   1048 N  N   . PHE   A 1 134 ? 4.929   7.941   17.086  1.00 14.42 ? 134 PHE   A N   1 
ATOM   1049 C  CA  . PHE   A 1 134 ? 4.681   7.048   15.955  1.00 15.83 ? 134 PHE   A CA  1 
ATOM   1050 C  C   . PHE   A 1 134 ? 5.507   7.380   14.708  1.00 15.31 ? 134 PHE   A C   1 
ATOM   1051 O  O   . PHE   A 1 134 ? 5.206   6.870   13.638  1.00 16.12 ? 134 PHE   A O   1 
ATOM   1052 C  CB  . PHE   A 1 134 ? 3.181   6.988   15.633  1.00 16.80 ? 134 PHE   A CB  1 
ATOM   1053 C  CG  . PHE   A 1 134 ? 2.354   6.306   16.693  1.00 19.91 ? 134 PHE   A CG  1 
ATOM   1054 C  CD1 . PHE   A 1 134 ? 2.468   4.939   16.910  1.00 23.59 ? 134 PHE   A CD1 1 
ATOM   1055 C  CD2 . PHE   A 1 134 ? 1.500   7.031   17.510  1.00 21.58 ? 134 PHE   A CD2 1 
ATOM   1056 C  CE1 . PHE   A 1 134 ? 1.702   4.304   17.883  1.00 25.97 ? 134 PHE   A CE1 1 
ATOM   1057 C  CE2 . PHE   A 1 134 ? 0.734   6.396   18.488  1.00 22.96 ? 134 PHE   A CE2 1 
ATOM   1058 C  CZ  . PHE   A 1 134 ? 0.855   5.043   18.688  1.00 23.69 ? 134 PHE   A CZ  1 
ATOM   1059 N  N   . THR   A 1 135 ? 6.586   8.147   14.838  1.00 15.09 ? 135 THR   A N   1 
ATOM   1060 C  CA  . THR   A 1 135 ? 7.596   8.213   13.792  1.00 14.22 ? 135 THR   A CA  1 
ATOM   1061 C  C   . THR   A 1 135 ? 8.720   7.232   14.090  1.00 13.86 ? 135 THR   A C   1 
ATOM   1062 O  O   . THR   A 1 135 ? 8.778   6.665   15.171  1.00 14.38 ? 135 THR   A O   1 
ATOM   1063 C  CB  . THR   A 1 135 ? 8.170   9.625   13.669  1.00 14.08 ? 135 THR   A CB  1 
ATOM   1064 O  OG1 . THR   A 1 135 ? 8.858   9.934   14.883  1.00 14.34 ? 135 THR   A OG1 1 
ATOM   1065 C  CG2 . THR   A 1 135 ? 7.081   10.630  13.380  1.00 14.92 ? 135 THR   A CG2 1 
ATOM   1066 N  N   . ILE   A 1 136 ? 9.634   7.049   13.129  1.00 14.98 ? 136 ILE   A N   1 
ATOM   1067 C  CA  . ILE   A 1 136 ? 10.891  6.389   13.430  1.00 15.65 ? 136 ILE   A CA  1 
ATOM   1068 C  C   . ILE   A 1 136 ? 12.042  7.282   13.004  1.00 16.14 ? 136 ILE   A C   1 
ATOM   1069 O  O   . ILE   A 1 136 ? 11.938  8.055   12.054  1.00 15.75 ? 136 ILE   A O   1 
ATOM   1070 C  CB  . ILE   A 1 136 ? 10.943  4.958   12.866  1.00 18.70 ? 136 ILE   A CB  1 
ATOM   1071 C  CG1 . ILE   A 1 136 ? 11.320  4.914   11.393  1.00 21.12 ? 136 ILE   A CG1 1 
ATOM   1072 C  CG2 . ILE   A 1 136 ? 9.634   4.206   13.156  1.00 18.73 ? 136 ILE   A CG2 1 
ATOM   1073 C  CD1 . ILE   A 1 136 ? 11.602  3.528   10.904  1.00 23.06 ? 136 ILE   A CD1 1 
ATOM   1074 N  N   . LYS   A 1 137 ? 13.128  7.214   13.770  1.00 17.54 ? 137 LYS   A N   1 
ATOM   1075 C  CA  . LYS   A 1 137 ? 14.329  7.951   13.439  1.00 20.19 ? 137 LYS   A CA  1 
ATOM   1076 C  C   . LYS   A 1 137 ? 15.205  7.018   12.606  1.00 20.96 ? 137 LYS   A C   1 
ATOM   1077 O  O   . LYS   A 1 137 ? 16.135  6.389   13.110  1.00 21.71 ? 137 LYS   A O   1 
ATOM   1078 C  CB  . LYS   A 1 137 ? 14.999  8.475   14.713  1.00 23.14 ? 137 LYS   A CB  1 
ATOM   1079 C  CG  . LYS   A 1 137 ? 14.194  9.526   15.479  1.00 25.59 ? 137 LYS   A CG  1 
ATOM   1080 C  CD  . LYS   A 1 137 ? 14.904  10.005  16.725  1.00 29.91 ? 137 LYS   A CD  1 
ATOM   1081 C  CE  . LYS   A 1 137 ? 14.118  11.010  17.536  1.00 34.46 ? 137 LYS   A CE  1 
ATOM   1082 N  NZ  . LYS   A 1 137 ? 14.327  12.382  17.021  1.00 39.90 ? 137 LYS   A NZ  1 
ATOM   1083 N  N   . GLY   A 1 138 ? 14.858  6.918   11.319  1.00 18.64 ? 138 GLY   A N   1 
ATOM   1084 C  CA  . GLY   A 1 138 ? 15.490  5.976   10.421  1.00 17.91 ? 138 GLY   A CA  1 
ATOM   1085 C  C   . GLY   A 1 138 ? 16.641  6.602   9.656   1.00 17.04 ? 138 GLY   A C   1 
ATOM   1086 O  O   . GLY   A 1 138 ? 16.967  7.768   9.846   1.00 15.67 ? 138 GLY   A O   1 
ATOM   1087 N  N   . SER   A 1 139 ? 17.262  5.765   8.836   1.00 18.32 ? 139 SER   A N   1 
ATOM   1088 C  CA  . SER   A 1 139 ? 18.272  6.170   7.873   1.00 19.07 ? 139 SER   A CA  1 
ATOM   1089 C  C   . SER   A 1 139 ? 17.815  5.665   6.511   1.00 18.64 ? 139 SER   A C   1 
ATOM   1090 O  O   . SER   A 1 139 ? 17.972  4.476   6.174   1.00 20.35 ? 139 SER   A O   1 
ATOM   1091 C  CB  . SER   A 1 139 ? 19.632  5.627   8.217   1.00 20.70 ? 139 SER   A CB  1 
ATOM   1092 O  OG  . SER   A 1 139 ? 20.087  6.197   9.429   1.00 23.49 ? 139 SER   A OG  1 
ATOM   1093 N  N   . PHE   A 1 140 ? 17.213  6.588   5.775   1.00 16.03 ? 140 PHE   A N   1 
ATOM   1094 C  CA  . PHE   A 1 140 ? 16.526  6.298   4.542   1.00 16.01 ? 140 PHE   A CA  1 
ATOM   1095 C  C   . PHE   A 1 140 ? 16.789  7.451   3.583   1.00 16.78 ? 140 PHE   A C   1 
ATOM   1096 O  O   . PHE   A 1 140 ? 16.691  8.606   3.996   1.00 16.55 ? 140 PHE   A O   1 
ATOM   1097 C  CB  . PHE   A 1 140 ? 15.018  6.207   4.776   1.00 15.88 ? 140 PHE   A CB  1 
ATOM   1098 C  CG  . PHE   A 1 140 ? 14.508  4.990   5.505   1.00 15.84 ? 140 PHE   A CG  1 
ATOM   1099 C  CD1 . PHE   A 1 140 ? 14.669  3.712   4.979   1.00 16.36 ? 140 PHE   A CD1 1 
ATOM   1100 C  CD2 . PHE   A 1 140 ? 13.816  5.127   6.685   1.00 16.76 ? 140 PHE   A CD2 1 
ATOM   1101 C  CE1 . PHE   A 1 140 ? 14.155  2.600   5.625   1.00 16.17 ? 140 PHE   A CE1 1 
ATOM   1102 C  CE2 . PHE   A 1 140 ? 13.266  4.019   7.318   1.00 17.35 ? 140 PHE   A CE2 1 
ATOM   1103 C  CZ  . PHE   A 1 140 ? 13.428  2.760   6.779   1.00 17.28 ? 140 PHE   A CZ  1 
ATOM   1104 N  N   . LEU   A 1 141 ? 17.119  7.101   2.335   1.00 16.69 ? 141 LEU   A N   1 
ATOM   1105 C  CA  . LEU   A 1 141 ? 17.308  8.044   1.252   1.00 17.37 ? 141 LEU   A CA  1 
ATOM   1106 C  C   . LEU   A 1 141 ? 16.137  7.898   0.284   1.00 17.20 ? 141 LEU   A C   1 
ATOM   1107 O  O   . LEU   A 1 141 ? 15.304  6.980   0.408   1.00 16.34 ? 141 LEU   A O   1 
ATOM   1108 C  CB  . LEU   A 1 141 ? 18.642  7.722   0.572   1.00 18.16 ? 141 LEU   A CB  1 
ATOM   1109 C  CG  . LEU   A 1 141 ? 19.861  7.789   1.498   1.00 21.40 ? 141 LEU   A CG  1 
ATOM   1110 C  CD1 . LEU   A 1 141 ? 21.152  7.470   0.742   1.00 21.31 ? 141 LEU   A CD1 1 
ATOM   1111 C  CD2 . LEU   A 1 141 ? 19.959  9.146   2.174   1.00 21.91 ? 141 LEU   A CD2 1 
ATOM   1112 N  N   . ASN   A 1 142 ? 16.118  8.784   -0.717  1.00 16.34 ? 142 ASN   A N   1 
ATOM   1113 C  CA  . ASN   A 1 142 ? 15.179  8.682   -1.832  1.00 17.62 ? 142 ASN   A CA  1 
ATOM   1114 C  C   . ASN   A 1 142 ? 15.281  7.283   -2.453  1.00 15.67 ? 142 ASN   A C   1 
ATOM   1115 O  O   . ASN   A 1 142 ? 16.383  6.787   -2.673  1.00 13.79 ? 142 ASN   A O   1 
ATOM   1116 C  CB  . ASN   A 1 142 ? 15.440  9.748   -2.902  1.00 20.75 ? 142 ASN   A CB  1 
ATOM   1117 C  CG  . ASN   A 1 142 ? 15.210  11.193  -2.469  1.00 26.42 ? 142 ASN   A CG  1 
ATOM   1118 O  OD1 . ASN   A 1 142 ? 14.484  11.929  -3.128  1.00 31.27 ? 142 ASN   A OD1 1 
ATOM   1119 N  ND2 . ASN   A 1 142 ? 15.890  11.666  -1.438  1.00 28.46 ? 142 ASN   A ND2 1 
ATOM   1120 N  N   . GLY   A 1 143 ? 14.132  6.636   -2.711  1.00 14.32 ? 143 GLY   A N   1 
ATOM   1121 C  CA  . GLY   A 1 143 ? 14.115  5.289   -3.271  1.00 12.99 ? 143 GLY   A CA  1 
ATOM   1122 C  C   . GLY   A 1 143 ? 13.950  4.172   -2.229  1.00 12.18 ? 143 GLY   A C   1 
ATOM   1123 O  O   . GLY   A 1 143 ? 13.879  3.014   -2.602  1.00 12.14 ? 143 GLY   A O   1 
ATOM   1124 N  N   . SER   A 1 144 ? 13.880  4.517   -0.938  1.00 12.20 ? 144 SER   A N   1 
ATOM   1125 C  CA  . SER   A 1 144 ? 13.811  3.540   0.150   1.00 11.96 ? 144 SER   A CA  1 
ATOM   1126 C  C   . SER   A 1 144 ? 12.374  3.079   0.394   1.00 12.27 ? 144 SER   A C   1 
ATOM   1127 O  O   . SER   A 1 144 ? 12.165  2.109   1.117   1.00 11.62 ? 144 SER   A O   1 
ATOM   1128 C  CB  . SER   A 1 144 ? 14.410  4.084   1.417   1.00 11.22 ? 144 SER   A CB  1 
ATOM   1129 O  OG  . SER   A 1 144 ? 13.674  5.211   1.878   1.00 11.84 ? 144 SER   A OG  1 
ATOM   1130 N  N   . CYS   A 1 145 ? 11.399  3.804   -0.185  1.00 11.68 ? 145 CYS   A N   1 
ATOM   1131 C  CA  . CYS   A 1 145 ? 9.986   3.511   -0.026  1.00 11.46 ? 145 CYS   A CA  1 
ATOM   1132 C  C   . CYS   A 1 145 ? 9.741   2.009   -0.216  1.00 11.24 ? 145 CYS   A C   1 
ATOM   1133 O  O   . CYS   A 1 145 ? 10.186  1.419   -1.203  1.00 11.74 ? 145 CYS   A O   1 
ATOM   1134 C  CB  . CYS   A 1 145 ? 9.168   4.340   -1.015  1.00 12.33 ? 145 CYS   A CB  1 
ATOM   1135 S  SG  . CYS   A 1 145 ? 7.392   4.449   -0.654  1.00 11.76 ? 145 CYS   A SG  1 
ATOM   1136 N  N   . GLY   A 1 146 ? 9.023   1.404   0.739   1.00 10.41 ? 146 GLY   A N   1 
ATOM   1137 C  CA  . GLY   A 1 146 ? 8.676   -0.014  0.725   1.00 10.41 ? 146 GLY   A CA  1 
ATOM   1138 C  C   . GLY   A 1 146 ? 9.678   -0.927  1.448   1.00 10.44 ? 146 GLY   A C   1 
ATOM   1139 O  O   . GLY   A 1 146 ? 9.426   -2.129  1.575   1.00 10.84 ? 146 GLY   A O   1 
ATOM   1140 N  N   . SER   A 1 147 ? 10.825  -0.388  1.881   1.00 10.09 ? 147 SER   A N   1 
ATOM   1141 C  CA  . SER   A 1 147 ? 11.715  -1.104  2.788   1.00 9.98  ? 147 SER   A CA  1 
ATOM   1142 C  C   . SER   A 1 147 ? 10.913  -1.546  4.018   1.00 10.16 ? 147 SER   A C   1 
ATOM   1143 O  O   . SER   A 1 147 ? 10.002  -0.839  4.435   1.00 9.56  ? 147 SER   A O   1 
ATOM   1144 C  CB  . SER   A 1 147 ? 12.880  -0.234  3.205   1.00 9.91  ? 147 SER   A CB  1 
ATOM   1145 O  OG  . SER   A 1 147 ? 13.671  0.199   2.095   1.00 9.34  ? 147 SER   A OG  1 
ATOM   1146 N  N   . VAL   A 1 148 ? 11.282  -2.683  4.625   1.00 10.10 ? 148 VAL   A N   1 
ATOM   1147 C  CA  . VAL   A 1 148 ? 10.507  -3.225  5.729   1.00 10.53 ? 148 VAL   A CA  1 
ATOM   1148 C  C   . VAL   A 1 148 ? 11.313  -3.283  7.023   1.00 11.34 ? 148 VAL   A C   1 
ATOM   1149 O  O   . VAL   A 1 148 ? 12.546  -3.336  7.017   1.00 12.12 ? 148 VAL   A O   1 
ATOM   1150 C  CB  . VAL   A 1 148 ? 9.880   -4.589  5.405   1.00 10.41 ? 148 VAL   A CB  1 
ATOM   1151 C  CG1 . VAL   A 1 148 ? 8.867   -4.463  4.277   1.00 10.27 ? 148 VAL   A CG1 1 
ATOM   1152 C  CG2 . VAL   A 1 148 ? 10.930  -5.639  5.077   1.00 10.44 ? 148 VAL   A CG2 1 
ATOM   1153 N  N   . GLY   A 1 149 ? 10.558  -3.253  8.129   1.00 10.78 ? 149 GLY   A N   1 
ATOM   1154 C  CA  . GLY   A 1 149 ? 11.063  -3.486  9.461   1.00 10.76 ? 149 GLY   A CA  1 
ATOM   1155 C  C   . GLY   A 1 149 ? 10.493  -4.790  10.021  1.00 10.99 ? 149 GLY   A C   1 
ATOM   1156 O  O   . GLY   A 1 149 ? 9.359   -5.157  9.671   1.00 11.07 ? 149 GLY   A O   1 
ATOM   1157 N  N   . PHE   A 1 150 ? 11.283  -5.454  10.882  1.00 10.50 ? 150 PHE   A N   1 
ATOM   1158 C  CA  . PHE   A 1 150 ? 10.982  -6.812  11.303  1.00 12.16 ? 150 PHE   A CA  1 
ATOM   1159 C  C   . PHE   A 1 150 ? 11.746  -7.224  12.575  1.00 12.03 ? 150 PHE   A C   1 
ATOM   1160 O  O   . PHE   A 1 150 ? 12.771  -6.650  12.949  1.00 12.04 ? 150 PHE   A O   1 
ATOM   1161 C  CB  . PHE   A 1 150 ? 11.300  -7.815  10.183  1.00 11.81 ? 150 PHE   A CB  1 
ATOM   1162 C  CG  . PHE   A 1 150 ? 12.760  -7.859  9.823   1.00 11.73 ? 150 PHE   A CG  1 
ATOM   1163 C  CD1 . PHE   A 1 150 ? 13.312  -6.909  8.993   1.00 12.70 ? 150 PHE   A CD1 1 
ATOM   1164 C  CD2 . PHE   A 1 150 ? 13.610  -8.769  10.415  1.00 12.44 ? 150 PHE   A CD2 1 
ATOM   1165 C  CE1 . PHE   A 1 150 ? 14.670  -6.900  8.712   1.00 13.22 ? 150 PHE   A CE1 1 
ATOM   1166 C  CE2 . PHE   A 1 150 ? 14.968  -8.765  10.128  1.00 12.58 ? 150 PHE   A CE2 1 
ATOM   1167 C  CZ  . PHE   A 1 150 ? 15.498  -7.835  9.278   1.00 12.35 ? 150 PHE   A CZ  1 
ATOM   1168 N  N   . ASN   A 1 151 ? 11.187  -8.237  13.230  1.00 12.99 ? 151 ASN   A N   1 
ATOM   1169 C  CA  . ASN   A 1 151 ? 11.827  -8.966  14.301  1.00 14.03 ? 151 ASN   A CA  1 
ATOM   1170 C  C   . ASN   A 1 151 ? 11.885  -10.439 13.893  1.00 14.12 ? 151 ASN   A C   1 
ATOM   1171 O  O   . ASN   A 1 151 ? 11.067  -10.909 13.106  1.00 13.37 ? 151 ASN   A O   1 
ATOM   1172 C  CB  . ASN   A 1 151 ? 11.062  -8.764  15.604  1.00 14.96 ? 151 ASN   A CB  1 
ATOM   1173 C  CG  . ASN   A 1 151 ? 11.328  -7.408  16.214  1.00 16.34 ? 151 ASN   A CG  1 
ATOM   1174 O  OD1 . ASN   A 1 151 ? 12.405  -7.165  16.726  1.00 20.23 ? 151 ASN   A OD1 1 
ATOM   1175 N  ND2 . ASN   A 1 151 ? 10.390  -6.486  16.109  1.00 16.23 ? 151 ASN   A ND2 1 
ATOM   1176 N  N   . ILE   A 1 152 ? 12.848  -11.170 14.440  1.00 14.67 ? 152 ILE   A N   1 
ATOM   1177 C  CA  . ILE   A 1 152 ? 12.953  -12.594 14.161  1.00 17.95 ? 152 ILE   A CA  1 
ATOM   1178 C  C   . ILE   A 1 152 ? 12.909  -13.325 15.494  1.00 21.17 ? 152 ILE   A C   1 
ATOM   1179 O  O   . ILE   A 1 152 ? 13.656  -12.998 16.410  1.00 21.61 ? 152 ILE   A O   1 
ATOM   1180 C  CB  . ILE   A 1 152 ? 14.209  -12.967 13.351  1.00 17.05 ? 152 ILE   A CB  1 
ATOM   1181 C  CG1 . ILE   A 1 152 ? 14.245  -12.219 12.021  1.00 18.33 ? 152 ILE   A CG1 1 
ATOM   1182 C  CG2 . ILE   A 1 152 ? 14.308  -14.482 13.158  1.00 17.25 ? 152 ILE   A CG2 1 
ATOM   1183 C  CD1 . ILE   A 1 152 ? 15.395  -12.621 11.108  1.00 20.83 ? 152 ILE   A CD1 1 
ATOM   1184 N  N   . ASP   A 1 153 ? 12.001  -14.293 15.584  1.00 24.97 ? 153 ASP   A N   1 
ATOM   1185 C  CA  . ASP   A 1 153 ? 11.941  -15.160 16.747  1.00 33.45 ? 153 ASP   A CA  1 
ATOM   1186 C  C   . ASP   A 1 153 ? 12.043  -16.607 16.268  1.00 35.50 ? 153 ASP   A C   1 
ATOM   1187 O  O   . ASP   A 1 153 ? 11.119  -17.124 15.643  1.00 35.96 ? 153 ASP   A O   1 
ATOM   1188 C  CB  . ASP   A 1 153 ? 10.667  -14.930 17.557  1.00 38.04 ? 153 ASP   A CB  1 
ATOM   1189 C  CG  . ASP   A 1 153 ? 10.637  -15.811 18.791  1.00 48.26 ? 153 ASP   A CG  1 
ATOM   1190 O  OD1 . ASP   A 1 153 ? 11.740  -16.240 19.218  1.00 47.99 ? 153 ASP   A OD1 1 
ATOM   1191 O  OD2 . ASP   A 1 153 ? 9.516   -16.096 19.298  1.00 57.70 ? 153 ASP   A OD2 1 
ATOM   1192 N  N   . TYR   A 1 154 ? 13.192  -17.225 16.559  1.00 41.10 ? 154 TYR   A N   1 
ATOM   1193 C  CA  . TYR   A 1 154 ? 13.551  -18.544 16.063  1.00 45.57 ? 154 TYR   A CA  1 
ATOM   1194 C  C   . TYR   A 1 154 ? 13.685  -18.458 14.547  1.00 42.83 ? 154 TYR   A C   1 
ATOM   1195 O  O   . TYR   A 1 154 ? 14.608  -17.840 14.023  1.00 47.21 ? 154 TYR   A O   1 
ATOM   1196 C  CB  . TYR   A 1 154 ? 12.540  -19.602 16.533  1.00 54.51 ? 154 TYR   A CB  1 
ATOM   1197 C  CG  . TYR   A 1 154 ? 12.327  -19.626 18.043  1.00 68.58 ? 154 TYR   A CG  1 
ATOM   1198 C  CD1 . TYR   A 1 154 ? 13.343  -20.030 18.911  1.00 71.27 ? 154 TYR   A CD1 1 
ATOM   1199 C  CD2 . TYR   A 1 154 ? 11.123  -19.202 18.602  1.00 70.04 ? 154 TYR   A CD2 1 
ATOM   1200 C  CE1 . TYR   A 1 154 ? 13.165  -20.020 20.285  1.00 69.09 ? 154 TYR   A CE1 1 
ATOM   1201 C  CE2 . TYR   A 1 154 ? 10.932  -19.198 19.974  1.00 71.16 ? 154 TYR   A CE2 1 
ATOM   1202 C  CZ  . TYR   A 1 154 ? 11.955  -19.607 20.814  1.00 69.20 ? 154 TYR   A CZ  1 
ATOM   1203 O  OH  . TYR   A 1 154 ? 11.773  -19.610 22.162  1.00 66.46 ? 154 TYR   A OH  1 
ATOM   1204 N  N   . ASP   A 1 155 ? 12.743  -19.079 13.844  1.00 39.93 ? 155 ASP   A N   1 
ATOM   1205 C  CA  . ASP   A 1 155 ? 12.787  -19.131 12.393  1.00 37.99 ? 155 ASP   A CA  1 
ATOM   1206 C  C   . ASP   A 1 155 ? 11.692  -18.236 11.795  1.00 30.64 ? 155 ASP   A C   1 
ATOM   1207 O  O   . ASP   A 1 155 ? 11.564  -18.196 10.573  1.00 28.29 ? 155 ASP   A O   1 
ATOM   1208 C  CB  . ASP   A 1 155 ? 12.650  -20.586 11.924  1.00 39.54 ? 155 ASP   A CB  1 
ATOM   1209 C  CG  . ASP   A 1 155 ? 11.381  -21.293 12.403  1.00 46.03 ? 155 ASP   A CG  1 
ATOM   1210 O  OD1 . ASP   A 1 155 ? 10.738  -20.790 13.364  1.00 43.84 ? 155 ASP   A OD1 1 
ATOM   1211 O  OD2 . ASP   A 1 155 ? 11.032  -22.344 11.816  1.00 48.69 ? 155 ASP   A OD2 1 
ATOM   1212 N  N   . CYS   A 1 156 ? 10.891  -17.558 12.652  1.00 24.10 ? 156 CYS   A N   1 
ATOM   1213 C  CA  . CYS   A 1 156 ? 9.733   -16.802 12.194  1.00 21.49 ? 156 CYS   A CA  1 
ATOM   1214 C  C   . CYS   A 1 156 ? 10.053  -15.295 12.121  1.00 17.96 ? 156 CYS   A C   1 
ATOM   1215 O  O   . CYS   A 1 156 ? 10.446  -14.703 13.121  1.00 16.45 ? 156 CYS   A O   1 
ATOM   1216 C  CB  . CYS   A 1 156 ? 8.553   -17.071 13.123  1.00 23.10 ? 156 CYS   A CB  1 
ATOM   1217 S  SG  . CYS   A 1 156 ? 7.012   -16.263 12.602  1.00 26.02 ? 156 CYS   A SG  1 
ATOM   1218 N  N   . VAL   A 1 157 ? 9.870   -14.695 10.940  1.00 15.51 ? 157 VAL   A N   1 
ATOM   1219 C  CA  . VAL   A 1 157 ? 9.970   -13.257 10.734  1.00 15.22 ? 157 VAL   A CA  1 
ATOM   1220 C  C   . VAL   A 1 157 ? 8.617   -12.597 11.002  1.00 13.72 ? 157 VAL   A C   1 
ATOM   1221 O  O   . VAL   A 1 157 ? 7.656   -12.899 10.326  1.00 13.58 ? 157 VAL   A O   1 
ATOM   1222 C  CB  . VAL   A 1 157 ? 10.479  -12.934 9.313   1.00 15.88 ? 157 VAL   A CB  1 
ATOM   1223 C  CG1 . VAL   A 1 157 ? 10.684  -11.426 9.108   1.00 16.07 ? 157 VAL   A CG1 1 
ATOM   1224 C  CG2 . VAL   A 1 157 ? 11.764  -13.701 9.019   1.00 17.34 ? 157 VAL   A CG2 1 
ATOM   1225 N  N   . SER   A 1 158 ? 8.568   -11.714 11.999  1.00 12.70 ? 158 SER   A N   1 
ATOM   1226 C  CA  . SER   A 1 158 ? 7.446   -10.835 12.259  1.00 13.39 ? 158 SER   A CA  1 
ATOM   1227 C  C   . SER   A 1 158 ? 7.672   -9.484  11.599  1.00 12.48 ? 158 SER   A C   1 
ATOM   1228 O  O   . SER   A 1 158 ? 8.467   -8.667  12.093  1.00 12.24 ? 158 SER   A O   1 
ATOM   1229 C  CB  . SER   A 1 158 ? 7.246   -10.658 13.768  1.00 14.10 ? 158 SER   A CB  1 
ATOM   1230 O  OG  . SER   A 1 158 ? 6.781   -11.882 14.331  1.00 15.22 ? 158 SER   A OG  1 
ATOM   1231 N  N   . PHE   A 1 159 ? 7.015   -9.267  10.463  1.00 11.76 ? 159 PHE   A N   1 
ATOM   1232 C  CA  . PHE   A 1 159 ? 7.057   -7.969  9.818   1.00 11.24 ? 159 PHE   A CA  1 
ATOM   1233 C  C   . PHE   A 1 159 ? 6.159   -6.986  10.565  1.00 11.85 ? 159 PHE   A C   1 
ATOM   1234 O  O   . PHE   A 1 159 ? 4.983   -7.265  10.755  1.00 11.44 ? 159 PHE   A O   1 
ATOM   1235 C  CB  . PHE   A 1 159 ? 6.598   -8.111  8.376   1.00 11.15 ? 159 PHE   A CB  1 
ATOM   1236 C  CG  . PHE   A 1 159 ? 7.530   -8.933  7.539   1.00 10.81 ? 159 PHE   A CG  1 
ATOM   1237 C  CD1 . PHE   A 1 159 ? 8.714   -8.390  7.069   1.00 10.80 ? 159 PHE   A CD1 1 
ATOM   1238 C  CD2 . PHE   A 1 159 ? 7.217   -10.243 7.203   1.00 11.03 ? 159 PHE   A CD2 1 
ATOM   1239 C  CE1 . PHE   A 1 159 ? 9.583   -9.148  6.295   1.00 10.74 ? 159 PHE   A CE1 1 
ATOM   1240 C  CE2 . PHE   A 1 159 ? 8.063   -10.988 6.388   1.00 10.83 ? 159 PHE   A CE2 1 
ATOM   1241 C  CZ  . PHE   A 1 159 ? 9.249   -10.439 5.943   1.00 10.71 ? 159 PHE   A CZ  1 
ATOM   1242 N  N   . CYS   A 1 160 ? 6.694   -5.806  10.891  1.00 11.84 ? 160 CYS   A N   1 
ATOM   1243 C  CA  . CYS   A 1 160 ? 5.935   -4.814  11.639  1.00 12.47 ? 160 CYS   A CA  1 
ATOM   1244 C  C   . CYS   A 1 160 ? 5.896   -3.426  10.985  1.00 11.60 ? 160 CYS   A C   1 
ATOM   1245 O  O   . CYS   A 1 160 ? 5.092   -2.583  11.395  1.00 12.90 ? 160 CYS   A O   1 
ATOM   1246 C  CB  . CYS   A 1 160 ? 6.474   -4.715  13.054  1.00 12.91 ? 160 CYS   A CB  1 
ATOM   1247 S  SG  . CYS   A 1 160 ? 8.212   -4.245  13.129  1.00 16.06 ? 160 CYS   A SG  1 
ATOM   1248 N  N   . TYR   A 1 161 ? 6.727   -3.163  9.976   1.00 9.97  ? 161 TYR   A N   1 
ATOM   1249 C  CA  . TYR   A 1 161 ? 6.827   -1.819  9.429   1.00 10.26 ? 161 TYR   A CA  1 
ATOM   1250 C  C   . TYR   A 1 161 ? 7.067   -1.898  7.925   1.00 9.92  ? 161 TYR   A C   1 
ATOM   1251 O  O   . TYR   A 1 161 ? 7.855   -2.710  7.464   1.00 9.26  ? 161 TYR   A O   1 
ATOM   1252 C  CB  . TYR   A 1 161 ? 7.939   -1.027  10.130  1.00 10.22 ? 161 TYR   A CB  1 
ATOM   1253 C  CG  . TYR   A 1 161 ? 8.152   0.399   9.631   1.00 10.43 ? 161 TYR   A CG  1 
ATOM   1254 C  CD1 . TYR   A 1 161 ? 7.337   1.448   10.060  1.00 11.11 ? 161 TYR   A CD1 1 
ATOM   1255 C  CD2 . TYR   A 1 161 ? 9.169   0.712   8.747   1.00 10.68 ? 161 TYR   A CD2 1 
ATOM   1256 C  CE1 . TYR   A 1 161 ? 7.536   2.747   9.622   1.00 11.11 ? 161 TYR   A CE1 1 
ATOM   1257 C  CE2 . TYR   A 1 161 ? 9.406   2.022   8.335   1.00 11.25 ? 161 TYR   A CE2 1 
ATOM   1258 C  CZ  . TYR   A 1 161 ? 8.567   3.037   8.741   1.00 11.04 ? 161 TYR   A CZ  1 
ATOM   1259 O  OH  . TYR   A 1 161 ? 8.745   4.324   8.309   1.00 11.25 ? 161 TYR   A OH  1 
ATOM   1260 N  N   . MET   A 1 162 ? 6.374   -1.045  7.175   1.00 10.37 ? 162 MET   A N   1 
ATOM   1261 C  CA  . MET   A 1 162 ? 6.725   -0.788  5.781   1.00 10.64 ? 162 MET   A CA  1 
ATOM   1262 C  C   . MET   A 1 162 ? 6.908   0.715   5.617   1.00 10.02 ? 162 MET   A C   1 
ATOM   1263 O  O   . MET   A 1 162 ? 6.018   1.486   5.939   1.00 10.00 ? 162 MET   A O   1 
ATOM   1264 C  CB  . MET   A 1 162 ? 5.662   -1.327  4.822   1.00 11.48 ? 162 MET   A CB  1 
ATOM   1265 C  CG  . MET   A 1 162 ? 5.843   -0.898  3.390   1.00 13.73 ? 162 MET   A CG  1 
ATOM   1266 S  SD  . MET   A 1 162 ? 4.810   -1.872  2.260   1.00 16.98 ? 162 MET   A SD  1 
ATOM   1267 C  CE  . MET   A 1 162 ? 5.815   -3.350  2.144   1.00 18.78 ? 162 MET   A CE  1 
ATOM   1268 N  N   . HIS   A 1 163 ? 8.078   1.112   5.126   1.00 10.43 ? 163 HIS   A N   1 
ATOM   1269 C  CA  . HIS   A 1 163 ? 8.469   2.511   5.017   1.00 10.13 ? 163 HIS   A CA  1 
ATOM   1270 C  C   . HIS   A 1 163 ? 7.744   3.220   3.878   1.00 10.33 ? 163 HIS   A C   1 
ATOM   1271 O  O   . HIS   A 1 163 ? 7.682   2.715   2.758   1.00 9.76  ? 163 HIS   A O   1 
ATOM   1272 C  CB  . HIS   A 1 163 ? 9.972   2.625   4.791   1.00 10.28 ? 163 HIS   A CB  1 
ATOM   1273 C  CG  . HIS   A 1 163 ? 10.452  4.016   4.805   1.00 9.69  ? 163 HIS   A CG  1 
ATOM   1274 N  ND1 . HIS   A 1 163 ? 10.067  4.929   5.754   1.00 9.50  ? 163 HIS   A ND1 1 
ATOM   1275 C  CD2 . HIS   A 1 163 ? 11.224  4.659   3.913   1.00 9.61  ? 163 HIS   A CD2 1 
ATOM   1276 C  CE1 . HIS   A 1 163 ? 10.660  6.080   5.448   1.00 11.35 ? 163 HIS   A CE1 1 
ATOM   1277 N  NE2 . HIS   A 1 163 ? 11.368  5.927   4.331   1.00 10.04 ? 163 HIS   A NE2 1 
ATOM   1278 N  N   . HIS   A 1 164 ? 7.197   4.404   4.177   1.00 10.63 ? 164 HIS   A N   1 
ATOM   1279 C  CA  . HIS   A 1 164 ? 6.574   5.205   3.125   1.00 11.24 ? 164 HIS   A CA  1 
ATOM   1280 C  C   . HIS   A 1 164 ? 7.328   6.511   2.862   1.00 11.92 ? 164 HIS   A C   1 
ATOM   1281 O  O   . HIS   A 1 164 ? 7.675   6.787   1.714   1.00 11.36 ? 164 HIS   A O   1 
ATOM   1282 C  CB  . HIS   A 1 164 ? 5.102   5.493   3.434   1.00 10.38 ? 164 HIS   A CB  1 
ATOM   1283 C  CG  . HIS   A 1 164 ? 4.201   4.318   3.217   1.00 10.30 ? 164 HIS   A CG  1 
ATOM   1284 N  ND1 . HIS   A 1 164 ? 4.312   3.150   3.934   1.00 10.47 ? 164 HIS   A ND1 1 
ATOM   1285 C  CD2 . HIS   A 1 164 ? 3.150   4.163   2.407   1.00 9.47  ? 164 HIS   A CD2 1 
ATOM   1286 C  CE1 . HIS   A 1 164 ? 3.354   2.314   3.515   1.00 10.36 ? 164 HIS   A CE1 1 
ATOM   1287 N  NE2 . HIS   A 1 164 ? 2.640   2.929   2.619   1.00 10.06 ? 164 HIS   A NE2 1 
ATOM   1288 N  N   . MET   A 1 165 ? 7.503   7.349   3.892   1.00 13.03 ? 165 MET   A N   1 
ATOM   1289 C  CA  . MET   A 1 165 ? 7.936   8.710   3.621   1.00 15.21 ? 165 MET   A CA  1 
ATOM   1290 C  C   . MET   A 1 165 ? 8.825   9.299   4.705   1.00 14.50 ? 165 MET   A C   1 
ATOM   1291 O  O   . MET   A 1 165 ? 8.813   8.870   5.853   1.00 14.42 ? 165 MET   A O   1 
ATOM   1292 C  CB  . MET   A 1 165 ? 6.741   9.650   3.401   1.00 17.36 ? 165 MET   A CB  1 
ATOM   1293 C  CG  . MET   A 1 165 ? 5.651   9.526   4.419   1.00 19.05 ? 165 MET   A CG  1 
ATOM   1294 S  SD  . MET   A 1 165 ? 4.089   10.305  3.861   1.00 21.86 ? 165 MET   A SD  1 
ATOM   1295 C  CE  . MET   A 1 165 ? 3.451   10.534  5.527   1.00 21.01 ? 165 MET   A CE  1 
ATOM   1296 N  N   . GLU   A 1 166 ? 9.593   10.319  4.303   1.00 14.21 ? 166 GLU   A N   1 
ATOM   1297 C  CA  . GLU   A 1 166 ? 10.309  11.161  5.241   1.00 14.38 ? 166 GLU   A CA  1 
ATOM   1298 C  C   . GLU   A 1 166 ? 9.516   12.442  5.487   1.00 14.23 ? 166 GLU   A C   1 
ATOM   1299 O  O   . GLU   A 1 166 ? 8.992   13.027  4.555   1.00 13.98 ? 166 GLU   A O   1 
ATOM   1300 C  CB  . GLU   A 1 166 ? 11.709  11.455  4.710   1.00 15.76 ? 166 GLU   A CB  1 
ATOM   1301 C  CG  . GLU   A 1 166 ? 12.550  12.311  5.659   1.00 17.03 ? 166 GLU   A CG  1 
ATOM   1302 C  CD  . GLU   A 1 166 ? 14.010  12.355  5.230   1.00 19.86 ? 166 GLU   A CD  1 
ATOM   1303 O  OE1 . GLU   A 1 166 ? 14.654  11.281  5.227   1.00 15.76 ? 166 GLU   A OE1 1 
ATOM   1304 O  OE2 . GLU   A 1 166 ? 14.486  13.473  4.842   1.00 22.68 ? 166 GLU   A OE2 1 
ATOM   1305 N  N   . LEU   A 1 167 ? 9.431   12.869  6.754   1.00 14.96 ? 167 LEU   A N   1 
ATOM   1306 C  CA  . LEU   A 1 167 ? 8.775   14.117  7.122   1.00 15.62 ? 167 LEU   A CA  1 
ATOM   1307 C  C   . LEU   A 1 167 ? 9.794   15.255  7.018   1.00 18.31 ? 167 LEU   A C   1 
ATOM   1308 O  O   . LEU   A 1 167 ? 11.007  15.011  6.970   1.00 16.57 ? 167 LEU   A O   1 
ATOM   1309 C  CB  . LEU   A 1 167 ? 8.235   14.007  8.551   1.00 15.09 ? 167 LEU   A CB  1 
ATOM   1310 C  CG  . LEU   A 1 167 ? 7.309   12.820  8.800   1.00 15.66 ? 167 LEU   A CG  1 
ATOM   1311 C  CD1 . LEU   A 1 167 ? 6.792   12.796  10.229  1.00 16.19 ? 167 LEU   A CD1 1 
ATOM   1312 C  CD2 . LEU   A 1 167 ? 6.146   12.841  7.826   1.00 15.51 ? 167 LEU   A CD2 1 
ATOM   1313 N  N   . PRO   A 1 168 ? 9.346   16.530  6.992   1.00 19.20 ? 168 PRO   A N   1 
ATOM   1314 C  CA  . PRO   A 1 168 ? 10.267  17.672  6.916   1.00 18.67 ? 168 PRO   A CA  1 
ATOM   1315 C  C   . PRO   A 1 168 ? 11.316  17.750  8.009   1.00 17.92 ? 168 PRO   A C   1 
ATOM   1316 O  O   . PRO   A 1 168 ? 12.398  18.258  7.743   1.00 16.57 ? 168 PRO   A O   1 
ATOM   1317 C  CB  . PRO   A 1 168 ? 9.335   18.880  6.947   1.00 20.52 ? 168 PRO   A CB  1 
ATOM   1318 C  CG  . PRO   A 1 168 ? 8.058   18.332  6.328   1.00 20.67 ? 168 PRO   A CG  1 
ATOM   1319 C  CD  . PRO   A 1 168 ? 7.938   16.946  6.940   1.00 20.83 ? 168 PRO   A CD  1 
ATOM   1320 N  N   . THR   A 1 169 ? 11.050  17.191  9.202   1.00 17.25 ? 169 THR   A N   1 
ATOM   1321 C  CA  . THR   A 1 169 ? 12.058  17.172  10.245  1.00 17.80 ? 169 THR   A CA  1 
ATOM   1322 C  C   . THR   A 1 169 ? 13.110  16.076  10.024  1.00 19.19 ? 169 THR   A C   1 
ATOM   1323 O  O   . THR   A 1 169 ? 14.067  16.023  10.772  1.00 19.63 ? 169 THR   A O   1 
ATOM   1324 C  CB  . THR   A 1 169 ? 11.444  16.947  11.624  1.00 20.29 ? 169 THR   A CB  1 
ATOM   1325 O  OG1 . THR   A 1 169 ? 10.663  15.761  11.499  1.00 18.95 ? 169 THR   A OG1 1 
ATOM   1326 C  CG2 . THR   A 1 169 ? 10.626  18.132  12.119  1.00 19.70 ? 169 THR   A CG2 1 
ATOM   1327 N  N   . GLY   A 1 170 ? 12.962  15.206  9.010   1.00 17.63 ? 170 GLY   A N   1 
ATOM   1328 C  CA  . GLY   A 1 170 ? 13.942  14.171  8.718   1.00 16.72 ? 170 GLY   A CA  1 
ATOM   1329 C  C   . GLY   A 1 170 ? 13.654  12.840  9.431   1.00 16.90 ? 170 GLY   A C   1 
ATOM   1330 O  O   . GLY   A 1 170 ? 14.438  11.911  9.322   1.00 19.82 ? 170 GLY   A O   1 
ATOM   1331 N  N   . VAL   A 1 171 ? 12.569  12.759  10.209  1.00 16.78 ? 171 VAL   A N   1 
ATOM   1332 C  CA  . VAL   A 1 171 ? 12.090  11.491  10.746  1.00 15.38 ? 171 VAL   A CA  1 
ATOM   1333 C  C   . VAL   A 1 171 ? 11.199  10.839  9.687   1.00 13.55 ? 171 VAL   A C   1 
ATOM   1334 O  O   . VAL   A 1 171 ? 10.912  11.442  8.644   1.00 12.72 ? 171 VAL   A O   1 
ATOM   1335 C  CB  . VAL   A 1 171 ? 11.375  11.657  12.104  1.00 15.63 ? 171 VAL   A CB  1 
ATOM   1336 C  CG1 . VAL   A 1 171 ? 12.284  12.314  13.122  1.00 17.75 ? 171 VAL   A CG1 1 
ATOM   1337 C  CG2 . VAL   A 1 171 ? 10.081  12.440  11.995  1.00 16.67 ? 171 VAL   A CG2 1 
ATOM   1338 N  N   . HIS   A 1 172 ? 10.786  9.598   9.958   1.00 11.81 ? 172 HIS   A N   1 
ATOM   1339 C  CA  . HIS   A 1 172 ? 10.197  8.733   8.962   1.00 11.23 ? 172 HIS   A CA  1 
ATOM   1340 C  C   . HIS   A 1 172 ? 8.857   8.194   9.443   1.00 11.36 ? 172 HIS   A C   1 
ATOM   1341 O  O   . HIS   A 1 172 ? 8.637   8.037   10.656  1.00 10.07 ? 172 HIS   A O   1 
ATOM   1342 C  CB  . HIS   A 1 172 ? 11.162  7.597   8.655   1.00 12.00 ? 172 HIS   A CB  1 
ATOM   1343 C  CG  . HIS   A 1 172 ? 12.437  8.120   8.106   1.00 12.66 ? 172 HIS   A CG  1 
ATOM   1344 N  ND1 . HIS   A 1 172 ? 13.606  8.150   8.847   1.00 13.03 ? 172 HIS   A ND1 1 
ATOM   1345 C  CD2 . HIS   A 1 172 ? 12.693  8.743   6.938   1.00 13.20 ? 172 HIS   A CD2 1 
ATOM   1346 C  CE1 . HIS   A 1 172 ? 14.563  8.708   8.114   1.00 14.02 ? 172 HIS   A CE1 1 
ATOM   1347 N  NE2 . HIS   A 1 172 ? 14.035  9.067   6.936   1.00 14.79 ? 172 HIS   A NE2 1 
ATOM   1348 N  N   . ALA   A 1 173 ? 7.984   7.909   8.458   1.00 10.41 ? 173 ALA   A N   1 
ATOM   1349 C  CA  . ALA   A 1 173 ? 6.623   7.472   8.720   1.00 10.46 ? 173 ALA   A CA  1 
ATOM   1350 C  C   . ALA   A 1 173 ? 6.258   6.309   7.799   1.00 10.24 ? 173 ALA   A C   1 
ATOM   1351 O  O   . ALA   A 1 173 ? 6.651   6.269   6.620   1.00 11.00 ? 173 ALA   A O   1 
ATOM   1352 C  CB  . ALA   A 1 173 ? 5.655   8.613   8.528   1.00 10.50 ? 173 ALA   A CB  1 
ATOM   1353 N  N   . GLY   A 1 174 ? 5.499   5.376   8.349   1.00 9.13  ? 174 GLY   A N   1 
ATOM   1354 C  CA  . GLY   A 1 174 ? 5.093   4.211   7.599   1.00 9.73  ? 174 GLY   A CA  1 
ATOM   1355 C  C   . GLY   A 1 174 ? 3.925   3.487   8.237   1.00 9.48  ? 174 GLY   A C   1 
ATOM   1356 O  O   . GLY   A 1 174 ? 3.310   3.989   9.155   1.00 8.82  ? 174 GLY   A O   1 
ATOM   1357 N  N   . THR   A 1 175 ? 3.666   2.293   7.708   1.00 9.82  ? 175 THR   A N   1 
ATOM   1358 C  CA  . THR   A 1 175 ? 2.489   1.522   8.004   1.00 9.90  ? 175 THR   A CA  1 
ATOM   1359 C  C   . THR   A 1 175 ? 2.915   0.169   8.541   1.00 10.35 ? 175 THR   A C   1 
ATOM   1360 O  O   . THR   A 1 175 ? 4.078   -0.217  8.444   1.00 10.42 ? 175 THR   A O   1 
ATOM   1361 C  CB  . THR   A 1 175 ? 1.594   1.351   6.771   1.00 9.94  ? 175 THR   A CB  1 
ATOM   1362 O  OG1 . THR   A 1 175 ? 2.244   0.502   5.829   1.00 9.76  ? 175 THR   A OG1 1 
ATOM   1363 C  CG2 . THR   A 1 175 ? 1.242   2.659   6.110   1.00 9.88  ? 175 THR   A CG2 1 
ATOM   1364 N  N   . ASP   A 1 176 ? 1.931   -0.552  9.068   1.00 10.27 ? 176 ASP   A N   1 
ATOM   1365 C  CA  . ASP   A 1 176 ? 2.089   -1.970  9.300   1.00 11.10 ? 176 ASP   A CA  1 
ATOM   1366 C  C   . ASP   A 1 176 ? 1.828   -2.662  7.967   1.00 10.82 ? 176 ASP   A C   1 
ATOM   1367 O  O   . ASP   A 1 176 ? 1.595   -1.992  6.976   1.00 10.40 ? 176 ASP   A O   1 
ATOM   1368 C  CB  . ASP   A 1 176 ? 1.213   -2.410  10.467  1.00 12.37 ? 176 ASP   A CB  1 
ATOM   1369 C  CG  . ASP   A 1 176 ? -0.268  -2.225  10.232  1.00 13.62 ? 176 ASP   A CG  1 
ATOM   1370 O  OD1 . ASP   A 1 176 ? -0.677  -2.145  9.053   1.00 12.28 ? 176 ASP   A OD1 1 
ATOM   1371 O  OD2 . ASP   A 1 176 ? -0.996  -2.168  11.263  1.00 18.01 ? 176 ASP   A OD2 1 
ATOM   1372 N  N   . LEU   A 1 177 ? 1.861   -3.993  7.945   1.00 12.15 ? 177 LEU   A N   1 
ATOM   1373 C  CA  . LEU   A 1 177 ? 1.739   -4.734  6.700   1.00 13.76 ? 177 LEU   A CA  1 
ATOM   1374 C  C   . LEU   A 1 177 ? 0.274   -4.970  6.335   1.00 14.95 ? 177 LEU   A C   1 
ATOM   1375 O  O   . LEU   A 1 177 ? -0.012  -5.560  5.292   1.00 15.50 ? 177 LEU   A O   1 
ATOM   1376 C  CB  . LEU   A 1 177 ? 2.534   -6.039  6.803   1.00 15.00 ? 177 LEU   A CB  1 
ATOM   1377 C  CG  . LEU   A 1 177 ? 3.975   -5.933  6.312   1.00 15.07 ? 177 LEU   A CG  1 
ATOM   1378 C  CD1 . LEU   A 1 177 ? 4.022   -5.590  4.832   1.00 15.63 ? 177 LEU   A CD1 1 
ATOM   1379 C  CD2 . LEU   A 1 177 ? 4.738   -4.915  7.135   1.00 14.79 ? 177 LEU   A CD2 1 
ATOM   1380 N  N   . GLU   A 1 178 ? -0.640  -4.401  7.123   1.00 15.72 ? 178 GLU   A N   1 
ATOM   1381 C  CA  . GLU   A 1 178 ? -2.044  -4.324  6.751   1.00 17.75 ? 178 GLU   A CA  1 
ATOM   1382 C  C   . GLU   A 1 178 ? -2.358  -2.942  6.191   1.00 16.57 ? 178 GLU   A C   1 
ATOM   1383 O  O   . GLU   A 1 178 ? -3.524  -2.641  5.958   1.00 15.61 ? 178 GLU   A O   1 
ATOM   1384 C  CB  . GLU   A 1 178 ? -2.974  -4.592  7.942   1.00 19.57 ? 178 GLU   A CB  1 
ATOM   1385 C  CG  . GLU   A 1 178 ? -2.871  -5.994  8.494   1.00 24.93 ? 178 GLU   A CG  1 
ATOM   1386 C  CD  . GLU   A 1 178 ? -3.964  -6.386  9.483   1.00 29.81 ? 178 GLU   A CD  1 
ATOM   1387 O  OE1 . GLU   A 1 178 ? -5.163  -6.377  9.114   1.00 38.92 ? 178 GLU   A OE1 1 
ATOM   1388 O  OE2 . GLU   A 1 178 ? -3.615  -6.711  10.617  1.00 40.14 ? 178 GLU   A OE2 1 
ATOM   1389 N  N   . GLY   A 1 179 ? -1.333  -2.094  6.051   1.00 14.22 ? 179 GLY   A N   1 
ATOM   1390 C  CA  . GLY   A 1 179 ? -1.492  -0.816  5.394   1.00 13.22 ? 179 GLY   A CA  1 
ATOM   1391 C  C   . GLY   A 1 179 ? -2.037  0.314   6.271   1.00 12.23 ? 179 GLY   A C   1 
ATOM   1392 O  O   . GLY   A 1 179 ? -2.365  1.383   5.737   1.00 10.88 ? 179 GLY   A O   1 
ATOM   1393 N  N   . ASN   A 1 180 ? -2.077  0.122   7.591   1.00 11.59 ? 180 ASN   A N   1 
ATOM   1394 C  CA  . ASN   A 1 180 ? -2.434  1.216   8.490   1.00 11.73 ? 180 ASN   A CA  1 
ATOM   1395 C  C   . ASN   A 1 180 ? -1.198  1.968   8.973   1.00 11.50 ? 180 ASN   A C   1 
ATOM   1396 O  O   . ASN   A 1 180 ? -0.289  1.376   9.546   1.00 10.61 ? 180 ASN   A O   1 
ATOM   1397 C  CB  . ASN   A 1 180 ? -3.172  0.709   9.722   1.00 13.20 ? 180 ASN   A CB  1 
ATOM   1398 C  CG  . ASN   A 1 180 ? -4.427  -0.025  9.328   1.00 13.84 ? 180 ASN   A CG  1 
ATOM   1399 O  OD1 . ASN   A 1 180 ? -4.543  -1.218  9.552   1.00 20.89 ? 180 ASN   A OD1 1 
ATOM   1400 N  ND2 . ASN   A 1 180 ? -5.317  0.649   8.671   1.00 13.55 ? 180 ASN   A ND2 1 
ATOM   1401 N  N   . PHE   A 1 181 ? -1.205  3.289   8.786   1.00 11.34 ? 181 PHE   A N   1 
ATOM   1402 C  CA  . PHE   A 1 181 ? -0.143  4.123   9.310   1.00 11.37 ? 181 PHE   A CA  1 
ATOM   1403 C  C   . PHE   A 1 181 ? 0.034   3.938   10.817  1.00 10.85 ? 181 PHE   A C   1 
ATOM   1404 O  O   . PHE   A 1 181 ? -0.904  3.675   11.549  1.00 10.71 ? 181 PHE   A O   1 
ATOM   1405 C  CB  . PHE   A 1 181 ? -0.359  5.594   8.948   1.00 11.48 ? 181 PHE   A CB  1 
ATOM   1406 C  CG  . PHE   A 1 181 ? 0.381   6.005   7.697   1.00 11.89 ? 181 PHE   A CG  1 
ATOM   1407 C  CD1 . PHE   A 1 181 ? 1.719   6.381   7.761   1.00 11.79 ? 181 PHE   A CD1 1 
ATOM   1408 C  CD2 . PHE   A 1 181 ? -0.223  5.927   6.456   1.00 11.81 ? 181 PHE   A CD2 1 
ATOM   1409 C  CE1 . PHE   A 1 181 ? 2.403   6.752   6.619   1.00 11.91 ? 181 PHE   A CE1 1 
ATOM   1410 C  CE2 . PHE   A 1 181 ? 0.455   6.312   5.315   1.00 12.81 ? 181 PHE   A CE2 1 
ATOM   1411 C  CZ  . PHE   A 1 181 ? 1.772   6.709   5.394   1.00 12.75 ? 181 PHE   A CZ  1 
ATOM   1412 N  N   . TYR   A 1 182 ? 1.283   4.003   11.248  1.00 10.83 ? 182 TYR   A N   1 
ATOM   1413 C  CA  . TYR   A 1 182 ? 1.618   4.353   12.611  1.00 11.30 ? 182 TYR   A CA  1 
ATOM   1414 C  C   . TYR   A 1 182 ? 1.530   5.868   12.683  1.00 11.36 ? 182 TYR   A C   1 
ATOM   1415 O  O   . TYR   A 1 182 ? 2.154   6.544   11.889  1.00 10.88 ? 182 TYR   A O   1 
ATOM   1416 C  CB  . TYR   A 1 182 ? 3.027   3.861   12.942  1.00 11.61 ? 182 TYR   A CB  1 
ATOM   1417 C  CG  . TYR   A 1 182 ? 3.161   2.353   13.034  1.00 11.33 ? 182 TYR   A CG  1 
ATOM   1418 C  CD1 . TYR   A 1 182 ? 2.763   1.666   14.169  1.00 11.00 ? 182 TYR   A CD1 1 
ATOM   1419 C  CD2 . TYR   A 1 182 ? 3.661   1.618   11.959  1.00 11.64 ? 182 TYR   A CD2 1 
ATOM   1420 C  CE1 . TYR   A 1 182 ? 2.903   0.289   14.261  1.00 11.57 ? 182 TYR   A CE1 1 
ATOM   1421 C  CE2 . TYR   A 1 182 ? 3.783   0.241   12.031  1.00 11.44 ? 182 TYR   A CE2 1 
ATOM   1422 C  CZ  . TYR   A 1 182 ? 3.410   -0.421  13.189  1.00 11.45 ? 182 TYR   A CZ  1 
ATOM   1423 O  OH  . TYR   A 1 182 ? 3.544   -1.765  13.260  1.00 11.88 ? 182 TYR   A OH  1 
ATOM   1424 N  N   . GLY   A 1 183 ? 0.663   6.391   13.546  1.00 11.97 ? 183 GLY   A N   1 
ATOM   1425 C  CA  . GLY   A 1 183 ? 0.598   7.827   13.736  1.00 12.18 ? 183 GLY   A CA  1 
ATOM   1426 C  C   . GLY   A 1 183 ? -0.394  8.503   12.799  1.00 13.66 ? 183 GLY   A C   1 
ATOM   1427 O  O   . GLY   A 1 183 ? -1.021  7.865   11.953  1.00 12.87 ? 183 GLY   A O   1 
ATOM   1428 N  N   . PRO   A 1 184 ? -0.540  9.843   12.920  1.00 14.59 ? 184 PRO   A N   1 
ATOM   1429 C  CA  . PRO   A 1 184 ? -1.606  10.573  12.225  1.00 14.59 ? 184 PRO   A CA  1 
ATOM   1430 C  C   . PRO   A 1 184 ? -1.281  11.002  10.799  1.00 13.99 ? 184 PRO   A C   1 
ATOM   1431 O  O   . PRO   A 1 184 ? -1.687  12.073  10.354  1.00 15.51 ? 184 PRO   A O   1 
ATOM   1432 C  CB  . PRO   A 1 184 ? -1.720  11.824  13.112  1.00 15.52 ? 184 PRO   A CB  1 
ATOM   1433 C  CG  . PRO   A 1 184 ? -0.277  12.081  13.555  1.00 15.21 ? 184 PRO   A CG  1 
ATOM   1434 C  CD  . PRO   A 1 184 ? 0.286   10.703  13.793  1.00 14.49 ? 184 PRO   A CD  1 
ATOM   1435 N  N   . PHE   A 1 185 ? -0.543  10.164  10.078  1.00 14.29 ? 185 PHE   A N   1 
ATOM   1436 C  CA  . PHE   A 1 185 ? -0.008  10.525  8.773   1.00 13.74 ? 185 PHE   A CA  1 
ATOM   1437 C  C   . PHE   A 1 185 ? -0.833  9.942   7.634   1.00 12.95 ? 185 PHE   A C   1 
ATOM   1438 O  O   . PHE   A 1 185 ? -1.591  9.003   7.848   1.00 11.62 ? 185 PHE   A O   1 
ATOM   1439 C  CB  . PHE   A 1 185 ? 1.434   10.029  8.686   1.00 14.21 ? 185 PHE   A CB  1 
ATOM   1440 C  CG  . PHE   A 1 185 ? 2.270   10.493  9.840   1.00 13.40 ? 185 PHE   A CG  1 
ATOM   1441 C  CD1 . PHE   A 1 185 ? 2.557   11.841  10.013  1.00 13.55 ? 185 PHE   A CD1 1 
ATOM   1442 C  CD2 . PHE   A 1 185 ? 2.737   9.592   10.775  1.00 13.53 ? 185 PHE   A CD2 1 
ATOM   1443 C  CE1 . PHE   A 1 185 ? 3.333   12.279  11.075  1.00 13.35 ? 185 PHE   A CE1 1 
ATOM   1444 C  CE2 . PHE   A 1 185 ? 3.493   10.030  11.850  1.00 13.80 ? 185 PHE   A CE2 1 
ATOM   1445 C  CZ  . PHE   A 1 185 ? 3.779   11.379  12.008  1.00 13.87 ? 185 PHE   A CZ  1 
ATOM   1446 N  N   . VAL   A 1 186 ? -0.647  10.508  6.420   1.00 12.39 ? 186 VAL   A N   1 
ATOM   1447 C  CA  . VAL   A 1 186 ? -1.340  10.035  5.241   1.00 12.49 ? 186 VAL   A CA  1 
ATOM   1448 C  C   . VAL   A 1 186 ? -0.350  9.925   4.083   1.00 12.04 ? 186 VAL   A C   1 
ATOM   1449 O  O   . VAL   A 1 186 ? 0.659   10.633  4.036   1.00 10.87 ? 186 VAL   A O   1 
ATOM   1450 C  CB  . VAL   A 1 186 ? -2.547  10.933  4.908   1.00 15.62 ? 186 VAL   A CB  1 
ATOM   1451 C  CG1 . VAL   A 1 186 ? -3.553  10.940  6.053   1.00 15.69 ? 186 VAL   A CG1 1 
ATOM   1452 C  CG2 . VAL   A 1 186 ? -2.147  12.360  4.587   1.00 17.23 ? 186 VAL   A CG2 1 
ATOM   1453 N  N   . ASP   A 1 187 ? -0.637  9.000   3.166   1.00 11.91 ? 187 ASP   A N   1 
ATOM   1454 C  CA  . ASP   A 1 187 ? 0.278   8.686   2.079   1.00 12.72 ? 187 ASP   A CA  1 
ATOM   1455 C  C   . ASP   A 1 187 ? 0.044   9.673   0.940   1.00 14.53 ? 187 ASP   A C   1 
ATOM   1456 O  O   . ASP   A 1 187 ? -0.496  9.325   -0.100  1.00 15.63 ? 187 ASP   A O   1 
ATOM   1457 C  CB  . ASP   A 1 187 ? 0.208   7.232   1.628   1.00 12.24 ? 187 ASP   A CB  1 
ATOM   1458 C  CG  . ASP   A 1 187 ? -1.157  6.607   1.420   1.00 12.06 ? 187 ASP   A CG  1 
ATOM   1459 O  OD1 . ASP   A 1 187 ? -2.168  7.195   1.865   1.00 11.35 ? 187 ASP   A OD1 1 
ATOM   1460 O  OD2 . ASP   A 1 187 ? -1.186  5.517   0.817   1.00 10.90 ? 187 ASP   A OD2 1 
ATOM   1461 N  N   . ARG   A 1 188 ? 0.542   10.882  1.150   1.00 16.59 ? 188 ARG   A N   1 
ATOM   1462 C  CA  . ARG   A 1 188 ? 0.400   11.979  0.214   1.00 19.65 ? 188 ARG   A CA  1 
ATOM   1463 C  C   . ARG   A 1 188 ? 1.650   12.858  0.327   1.00 18.93 ? 188 ARG   A C   1 
ATOM   1464 O  O   . ARG   A 1 188 ? 2.219   12.973  1.405   1.00 16.47 ? 188 ARG   A O   1 
ATOM   1465 C  CB  . ARG   A 1 188 ? -0.946  12.621  0.553   1.00 21.86 ? 188 ARG   A CB  1 
ATOM   1466 C  CG  . ARG   A 1 188 ? -0.985  14.124  0.444   1.00 27.42 ? 188 ARG   A CG  1 
ATOM   1467 C  CD  . ARG   A 1 188 ? -2.380  14.686  0.693   1.00 29.24 ? 188 ARG   A CD  1 
ATOM   1468 N  NE  . ARG   A 1 188 ? -2.468  15.935  -0.056  1.00 34.20 ? 188 ARG   A NE  1 
ATOM   1469 C  CZ  . ARG   A 1 188 ? -3.293  16.946  0.194   1.00 34.72 ? 188 ARG   A CZ  1 
ATOM   1470 N  NH1 . ARG   A 1 188 ? -4.052  16.967  1.273   1.00 35.47 ? 188 ARG   A NH1 1 
ATOM   1471 N  NH2 . ARG   A 1 188 ? -3.311  17.970  -0.638  1.00 37.91 ? 188 ARG   A NH2 1 
ATOM   1472 N  N   . GLN   A 1 189 ? 2.092   13.449  -0.793  1.00 18.62 ? 189 GLN   A N   1 
ATOM   1473 C  CA  . GLN   A 1 189 ? 3.243   14.345  -0.786  1.00 19.59 ? 189 GLN   A CA  1 
ATOM   1474 C  C   . GLN   A 1 189 ? 2.822   15.753  -0.345  1.00 19.64 ? 189 GLN   A C   1 
ATOM   1475 O  O   . GLN   A 1 189 ? 2.644   16.663  -1.144  1.00 23.04 ? 189 GLN   A O   1 
ATOM   1476 C  CB  . GLN   A 1 189 ? 3.884   14.338  -2.174  1.00 21.21 ? 189 GLN   A CB  1 
ATOM   1477 C  CG  . GLN   A 1 189 ? 5.257   14.992  -2.236  1.00 24.11 ? 189 GLN   A CG  1 
ATOM   1478 C  CD  . GLN   A 1 189 ? 5.768   15.045  -3.660  1.00 29.64 ? 189 GLN   A CD  1 
ATOM   1479 O  OE1 . GLN   A 1 189 ? 5.743   14.059  -4.395  1.00 32.63 ? 189 GLN   A OE1 1 
ATOM   1480 N  NE2 . GLN   A 1 189 ? 6.237   16.209  -4.081  1.00 33.46 ? 189 GLN   A NE2 1 
ATOM   1481 N  N   . THR   A 1 190 ? 2.602   15.915  0.943   1.00 19.24 ? 190 THR   A N   1 
ATOM   1482 C  CA  . THR   A 1 190 ? 2.318   17.209  1.535   1.00 21.94 ? 190 THR   A CA  1 
ATOM   1483 C  C   . THR   A 1 190 ? 3.112   17.233  2.840   1.00 21.12 ? 190 THR   A C   1 
ATOM   1484 O  O   . THR   A 1 190 ? 3.427   16.162  3.363   1.00 22.12 ? 190 THR   A O   1 
ATOM   1485 C  CB  . THR   A 1 190 ? 0.801   17.393  1.729   1.00 24.91 ? 190 THR   A CB  1 
ATOM   1486 O  OG1 . THR   A 1 190 ? 0.568   18.739  2.148   1.00 31.38 ? 190 THR   A OG1 1 
ATOM   1487 C  CG2 . THR   A 1 190 ? 0.214   16.466  2.779   1.00 23.31 ? 190 THR   A CG2 1 
ATOM   1488 N  N   . ALA   A 1 191 ? 3.451   18.426  3.350   1.00 19.14 ? 191 ALA   A N   1 
ATOM   1489 C  CA  . ALA   A 1 191 ? 4.242   18.549  4.565   1.00 17.58 ? 191 ALA   A CA  1 
ATOM   1490 C  C   . ALA   A 1 191 ? 3.411   18.099  5.768   1.00 17.01 ? 191 ALA   A C   1 
ATOM   1491 O  O   . ALA   A 1 191 ? 2.270   18.533  5.958   1.00 16.48 ? 191 ALA   A O   1 
ATOM   1492 C  CB  . ALA   A 1 191 ? 4.753   19.967  4.743   1.00 19.45 ? 191 ALA   A CB  1 
ATOM   1493 N  N   . GLN   A 1 192 ? 3.980   17.177  6.563   1.00 16.14 ? 192 GLN   A N   1 
ATOM   1494 C  CA  . GLN   A 1 192 ? 3.294   16.624  7.713   1.00 15.18 ? 192 GLN   A CA  1 
ATOM   1495 C  C   . GLN   A 1 192 ? 4.204   16.700  8.936   1.00 14.42 ? 192 GLN   A C   1 
ATOM   1496 O  O   . GLN   A 1 192 ? 5.295   16.161  8.940   1.00 15.60 ? 192 GLN   A O   1 
ATOM   1497 C  CB  . GLN   A 1 192 ? 2.847   15.199  7.387   1.00 13.93 ? 192 GLN   A CB  1 
ATOM   1498 C  CG  . GLN   A 1 192 ? 1.820   15.137  6.265   1.00 13.87 ? 192 GLN   A CG  1 
ATOM   1499 C  CD  . GLN   A 1 192 ? 1.403   13.724  5.894   1.00 12.85 ? 192 GLN   A CD  1 
ATOM   1500 O  OE1 . GLN   A 1 192 ? 0.855   12.961  6.690   1.00 13.56 ? 192 GLN   A OE1 1 
ATOM   1501 N  NE2 . GLN   A 1 192 ? 1.601   13.384  4.642   1.00 13.63 ? 192 GLN   A NE2 1 
ATOM   1502 N  N   . ALA   A 1 193 ? 3.736   17.371  9.974   1.00 14.45 ? 193 ALA   A N   1 
ATOM   1503 C  CA  . ALA   A 1 193 ? 4.402   17.372  11.263  1.00 15.59 ? 193 ALA   A CA  1 
ATOM   1504 C  C   . ALA   A 1 193 ? 3.874   16.211  12.098  1.00 15.44 ? 193 ALA   A C   1 
ATOM   1505 O  O   . ALA   A 1 193 ? 2.717   15.821  11.952  1.00 13.46 ? 193 ALA   A O   1 
ATOM   1506 C  CB  . ALA   A 1 193 ? 4.170   18.687  11.982  1.00 16.17 ? 193 ALA   A CB  1 
ATOM   1507 N  N   . ALA   A 1 194 ? 4.754   15.656  12.941  1.00 15.14 ? 194 ALA   A N   1 
ATOM   1508 C  CA  . ALA   A 1 194 ? 4.349   14.731  13.991  1.00 15.05 ? 194 ALA   A CA  1 
ATOM   1509 C  C   . ALA   A 1 194 ? 4.015   15.494  15.274  1.00 15.87 ? 194 ALA   A C   1 
ATOM   1510 O  O   . ALA   A 1 194 ? 4.383   16.657  15.425  1.00 15.37 ? 194 ALA   A O   1 
ATOM   1511 C  CB  . ALA   A 1 194 ? 5.462   13.724  14.237  1.00 15.06 ? 194 ALA   A CB  1 
ATOM   1512 N  N   . GLY   A 1 195 ? 3.301   14.825  16.187  1.00 17.06 ? 195 GLY   A N   1 
ATOM   1513 C  CA  . GLY   A 1 195 ? 3.120   15.318  17.546  1.00 18.24 ? 195 GLY   A CA  1 
ATOM   1514 C  C   . GLY   A 1 195 ? 4.470   15.351  18.274  1.00 20.92 ? 195 GLY   A C   1 
ATOM   1515 O  O   . GLY   A 1 195 ? 5.462   14.760  17.834  1.00 17.06 ? 195 GLY   A O   1 
ATOM   1516 N  N   . THR   A 1 196 ? 4.520   16.082  19.384  1.00 23.13 ? 196 THR   A N   1 
ATOM   1517 C  CA  . THR   A 1 196 ? 5.737   16.225  20.159  1.00 22.90 ? 196 THR   A CA  1 
ATOM   1518 C  C   . THR   A 1 196 ? 6.129   14.845  20.681  1.00 19.84 ? 196 THR   A C   1 
ATOM   1519 O  O   . THR   A 1 196 ? 5.277   14.067  21.059  1.00 19.31 ? 196 THR   A O   1 
ATOM   1520 C  CB  . THR   A 1 196 ? 5.522   17.294  21.238  1.00 26.53 ? 196 THR   A CB  1 
ATOM   1521 O  OG1 . THR   A 1 196 ? 4.355   16.923  21.964  1.00 31.42 ? 196 THR   A OG1 1 
ATOM   1522 C  CG2 . THR   A 1 196 ? 5.312   18.674  20.670  1.00 25.25 ? 196 THR   A CG2 1 
ATOM   1523 N  N   . ASP   A 1 197 ? 7.420   14.513  20.635  1.00 19.35 ? 197 ASP   A N   1 
ATOM   1524 C  CA  . ASP   A 1 197 ? 7.884   13.172  20.976  1.00 18.13 ? 197 ASP   A CA  1 
ATOM   1525 C  C   . ASP   A 1 197 ? 8.262   13.128  22.453  1.00 17.30 ? 197 ASP   A C   1 
ATOM   1526 O  O   . ASP   A 1 197 ? 8.433   14.160  23.085  1.00 17.06 ? 197 ASP   A O   1 
ATOM   1527 C  CB  . ASP   A 1 197 ? 9.078   12.731  20.124  1.00 18.11 ? 197 ASP   A CB  1 
ATOM   1528 C  CG  . ASP   A 1 197 ? 9.281   11.221  20.072  1.00 17.48 ? 197 ASP   A CG  1 
ATOM   1529 O  OD1 . ASP   A 1 197 ? 8.331   10.454  20.430  1.00 16.41 ? 197 ASP   A OD1 1 
ATOM   1530 O  OD2 . ASP   A 1 197 ? 10.385  10.819  19.697  1.00 18.24 ? 197 ASP   A OD2 1 
ATOM   1531 N  N   . THR   A 1 198 ? 8.269   11.915  23.015  1.00 16.38 ? 198 THR   A N   1 
ATOM   1532 C  CA  . THR   A 1 198 ? 8.672   11.696  24.388  1.00 15.51 ? 198 THR   A CA  1 
ATOM   1533 C  C   . THR   A 1 198 ? 9.746   10.620  24.389  1.00 15.38 ? 198 THR   A C   1 
ATOM   1534 O  O   . THR   A 1 198 ? 9.975   9.958   23.369  1.00 15.11 ? 198 THR   A O   1 
ATOM   1535 C  CB  . THR   A 1 198 ? 7.444   11.378  25.242  1.00 16.94 ? 198 THR   A CB  1 
ATOM   1536 O  OG1 . THR   A 1 198 ? 6.733   10.333  24.589  1.00 16.72 ? 198 THR   A OG1 1 
ATOM   1537 C  CG2 . THR   A 1 198 ? 6.516   12.564  25.411  1.00 17.60 ? 198 THR   A CG2 1 
ATOM   1538 N  N   . THR   A 1 199 ? 10.412  10.488  25.536  1.00 13.37 ? 199 THR   A N   1 
ATOM   1539 C  CA  . THR   A 1 199 ? 11.459  9.512   25.724  1.00 12.47 ? 199 THR   A CA  1 
ATOM   1540 C  C   . THR   A 1 199 ? 10.869  8.225   26.283  1.00 12.54 ? 199 THR   A C   1 
ATOM   1541 O  O   . THR   A 1 199 ? 9.964   8.251   27.120  1.00 13.61 ? 199 THR   A O   1 
ATOM   1542 C  CB  . THR   A 1 199 ? 12.545  10.092  26.622  1.00 12.53 ? 199 THR   A CB  1 
ATOM   1543 O  OG1 . THR   A 1 199 ? 13.019  11.315  26.070  1.00 13.31 ? 199 THR   A OG1 1 
ATOM   1544 C  CG2 . THR   A 1 199 ? 13.674  9.115   26.808  1.00 12.87 ? 199 THR   A CG2 1 
ATOM   1545 N  N   . ILE   A 1 200 ? 11.389  7.080   25.810  1.00 11.64 ? 200 ILE   A N   1 
ATOM   1546 C  CA  . ILE   A 1 200 ? 10.850  5.793   26.205  1.00 11.27 ? 200 ILE   A CA  1 
ATOM   1547 C  C   . ILE   A 1 200 ? 11.510  5.339   27.520  1.00 11.33 ? 200 ILE   A C   1 
ATOM   1548 O  O   . ILE   A 1 200 ? 12.575  4.732   27.540  1.00 10.14 ? 200 ILE   A O   1 
ATOM   1549 C  CB  . ILE   A 1 200 ? 11.031  4.777   25.071  1.00 11.02 ? 200 ILE   A CB  1 
ATOM   1550 C  CG1 . ILE   A 1 200 ? 10.616  5.328   23.691  1.00 11.68 ? 200 ILE   A CG1 1 
ATOM   1551 C  CG2 . ILE   A 1 200 ? 10.299  3.523   25.409  1.00 10.73 ? 200 ILE   A CG2 1 
ATOM   1552 C  CD1 . ILE   A 1 200 ? 11.283  4.620   22.542  1.00 10.98 ? 200 ILE   A CD1 1 
ATOM   1553 N  N   . THR   A 1 201 ? 10.821  5.602   28.625  1.00 11.20 ? 201 THR   A N   1 
ATOM   1554 C  CA  . THR   A 1 201 ? 11.329  5.414   29.982  1.00 10.83 ? 201 THR   A CA  1 
ATOM   1555 C  C   . THR   A 1 201 ? 11.826  3.990   30.261  1.00 10.45 ? 201 THR   A C   1 
ATOM   1556 O  O   . THR   A 1 201 ? 12.961  3.808   30.685  1.00 10.36 ? 201 THR   A O   1 
ATOM   1557 C  CB  . THR   A 1 201 ? 10.268  5.871   30.996  1.00 10.20 ? 201 THR   A CB  1 
ATOM   1558 O  OG1 . THR   A 1 201 ? 9.803   7.147   30.566  1.00 10.75 ? 201 THR   A OG1 1 
ATOM   1559 C  CG2 . THR   A 1 201 ? 10.824  5.969   32.398  1.00 10.22 ? 201 THR   A CG2 1 
ATOM   1560 N  N   . VAL   A 1 202 ? 10.984  2.985   30.042  1.00 10.83 ? 202 VAL   A N   1 
ATOM   1561 C  CA  . VAL   A 1 202 ? 11.333  1.609   30.336  1.00 10.80 ? 202 VAL   A CA  1 
ATOM   1562 C  C   . VAL   A 1 202 ? 12.613  1.228   29.601  1.00 11.22 ? 202 VAL   A C   1 
ATOM   1563 O  O   . VAL   A 1 202 ? 13.402  0.467   30.138  1.00 10.95 ? 202 VAL   A O   1 
ATOM   1564 C  CB  . VAL   A 1 202 ? 10.203  0.612   30.012  1.00 11.21 ? 202 VAL   A CB  1 
ATOM   1565 C  CG1 . VAL   A 1 202 ? 9.800   0.605   28.541  1.00 10.59 ? 202 VAL   A CG1 1 
ATOM   1566 C  CG2 . VAL   A 1 202 ? 10.587  -0.790  30.484  1.00 11.03 ? 202 VAL   A CG2 1 
ATOM   1567 N  N   . ASN   A 1 203 ? 12.807  1.765   28.388  1.00 11.28 ? 203 ASN   A N   1 
ATOM   1568 C  CA  . ASN   A 1 203 ? 13.976  1.477   27.577  1.00 10.68 ? 203 ASN   A CA  1 
ATOM   1569 C  C   . ASN   A 1 203 ? 15.218  2.165   28.146  1.00 10.52 ? 203 ASN   A C   1 
ATOM   1570 O  O   . ASN   A 1 203 ? 16.315  1.602   28.135  1.00 10.74 ? 203 ASN   A O   1 
ATOM   1571 C  CB  . ASN   A 1 203 ? 13.733  1.890   26.119  1.00 10.18 ? 203 ASN   A CB  1 
ATOM   1572 C  CG  . ASN   A 1 203 ? 12.776  0.996   25.356  1.00 10.33 ? 203 ASN   A CG  1 
ATOM   1573 O  OD1 . ASN   A 1 203 ? 12.173  0.061   25.883  1.00 10.79 ? 203 ASN   A OD1 1 
ATOM   1574 N  ND2 . ASN   A 1 203 ? 12.649  1.243   24.066  1.00 10.24 ? 203 ASN   A ND2 1 
ATOM   1575 N  N   . VAL   A 1 204 ? 15.079  3.402   28.633  1.00 11.02 ? 204 VAL   A N   1 
ATOM   1576 C  CA  . VAL   A 1 204 ? 16.216  4.068   29.273  1.00 11.45 ? 204 VAL   A CA  1 
ATOM   1577 C  C   . VAL   A 1 204 ? 16.670  3.234   30.470  1.00 11.09 ? 204 VAL   A C   1 
ATOM   1578 O  O   . VAL   A 1 204 ? 17.867  2.985   30.661  1.00 11.52 ? 204 VAL   A O   1 
ATOM   1579 C  CB  . VAL   A 1 204 ? 15.915  5.530   29.658  1.00 11.76 ? 204 VAL   A CB  1 
ATOM   1580 C  CG1 . VAL   A 1 204 ? 17.053  6.172   30.436  1.00 12.32 ? 204 VAL   A CG1 1 
ATOM   1581 C  CG2 . VAL   A 1 204 ? 15.604  6.382   28.422  1.00 11.85 ? 204 VAL   A CG2 1 
ATOM   1582 N  N   . LEU   A 1 205 ? 15.711  2.753   31.251  1.00 10.69 ? 205 LEU   A N   1 
ATOM   1583 C  CA  . LEU   A 1 205 ? 16.040  1.955   32.427  1.00 11.49 ? 205 LEU   A CA  1 
ATOM   1584 C  C   . LEU   A 1 205 ? 16.772  0.663   32.019  1.00 11.58 ? 205 LEU   A C   1 
ATOM   1585 O  O   . LEU   A 1 205 ? 17.753  0.285   32.654  1.00 11.50 ? 205 LEU   A O   1 
ATOM   1586 C  CB  . LEU   A 1 205 ? 14.747  1.645   33.193  1.00 11.28 ? 205 LEU   A CB  1 
ATOM   1587 C  CG  . LEU   A 1 205 ? 14.096  2.835   33.903  1.00 11.77 ? 205 LEU   A CG  1 
ATOM   1588 C  CD1 . LEU   A 1 205 ? 12.776  2.429   34.546  1.00 12.36 ? 205 LEU   A CD1 1 
ATOM   1589 C  CD2 . LEU   A 1 205 ? 15.004  3.434   34.962  1.00 11.79 ? 205 LEU   A CD2 1 
ATOM   1590 N  N   . ALA   A 1 206 ? 16.266  -0.024  30.981  1.00 11.04 ? 206 ALA   A N   1 
ATOM   1591 C  CA  . ALA   A 1 206 ? 16.900  -1.225  30.453  1.00 12.08 ? 206 ALA   A CA  1 
ATOM   1592 C  C   . ALA   A 1 206 ? 18.359  -0.930  30.081  1.00 11.98 ? 206 ALA   A C   1 
ATOM   1593 O  O   . ALA   A 1 206 ? 19.255  -1.696  30.440  1.00 13.29 ? 206 ALA   A O   1 
ATOM   1594 C  CB  . ALA   A 1 206 ? 16.102  -1.748  29.277  1.00 12.60 ? 206 ALA   A CB  1 
ATOM   1595 N  N   . TRP   A 1 207 ? 18.601  0.216   29.446  1.00 11.59 ? 207 TRP   A N   1 
ATOM   1596 C  CA  . TRP   A 1 207 ? 19.934  0.590   28.995  1.00 11.97 ? 207 TRP   A CA  1 
ATOM   1597 C  C   . TRP   A 1 207 ? 20.846  0.934   30.177  1.00 13.26 ? 207 TRP   A C   1 
ATOM   1598 O  O   . TRP   A 1 207 ? 22.057  0.657   30.125  1.00 12.14 ? 207 TRP   A O   1 
ATOM   1599 C  CB  . TRP   A 1 207 ? 19.813  1.765   28.021  1.00 13.07 ? 207 TRP   A CB  1 
ATOM   1600 C  CG  . TRP   A 1 207 ? 21.103  2.410   27.578  1.00 13.70 ? 207 TRP   A CG  1 
ATOM   1601 C  CD1 . TRP   A 1 207 ? 22.038  1.925   26.708  1.00 12.89 ? 207 TRP   A CD1 1 
ATOM   1602 C  CD2 . TRP   A 1 207 ? 21.585  3.693   28.011  1.00 14.36 ? 207 TRP   A CD2 1 
ATOM   1603 N  NE1 . TRP   A 1 207 ? 23.042  2.830   26.542  1.00 13.84 ? 207 TRP   A NE1 1 
ATOM   1604 C  CE2 . TRP   A 1 207 ? 22.809  3.912   27.332  1.00 13.80 ? 207 TRP   A CE2 1 
ATOM   1605 C  CE3 . TRP   A 1 207 ? 21.108  4.658   28.909  1.00 15.11 ? 207 TRP   A CE3 1 
ATOM   1606 C  CZ2 . TRP   A 1 207 ? 23.546  5.066   27.508  1.00 14.14 ? 207 TRP   A CZ2 1 
ATOM   1607 C  CZ3 . TRP   A 1 207 ? 21.861  5.792   29.113  1.00 15.08 ? 207 TRP   A CZ3 1 
ATOM   1608 C  CH2 . TRP   A 1 207 ? 23.054  5.987   28.413  1.00 15.28 ? 207 TRP   A CH2 1 
ATOM   1609 N  N   . LEU   A 1 208 ? 20.282  1.523   31.258  1.00 12.79 ? 208 LEU   A N   1 
ATOM   1610 C  CA  . LEU   A 1 208 ? 21.070  1.754   32.471  1.00 12.34 ? 208 LEU   A CA  1 
ATOM   1611 C  C   . LEU   A 1 208 ? 21.506  0.425   33.087  1.00 12.19 ? 208 LEU   A C   1 
ATOM   1612 O  O   . LEU   A 1 208 ? 22.620  0.330   33.609  1.00 12.32 ? 208 LEU   A O   1 
ATOM   1613 C  CB  . LEU   A 1 208 ? 20.274  2.609   33.471  1.00 12.09 ? 208 LEU   A CB  1 
ATOM   1614 C  CG  . LEU   A 1 208 ? 20.005  4.050   33.043  1.00 11.40 ? 208 LEU   A CG  1 
ATOM   1615 C  CD1 . LEU   A 1 208 ? 19.167  4.776   34.074  1.00 11.97 ? 208 LEU   A CD1 1 
ATOM   1616 C  CD2 . LEU   A 1 208 ? 21.309  4.800   32.830  1.00 12.12 ? 208 LEU   A CD2 1 
ATOM   1617 N  N   . TYR   A 1 209 ? 20.626  -0.572  33.075  1.00 12.16 ? 209 TYR   A N   1 
ATOM   1618 C  CA  . TYR   A 1 209 ? 20.953  -1.904  33.555  1.00 12.91 ? 209 TYR   A CA  1 
ATOM   1619 C  C   . TYR   A 1 209 ? 22.051  -2.536  32.688  1.00 14.77 ? 209 TYR   A C   1 
ATOM   1620 O  O   . TYR   A 1 209 ? 22.969  -3.183  33.211  1.00 16.11 ? 209 TYR   A O   1 
ATOM   1621 C  CB  . TYR   A 1 209 ? 19.719  -2.816  33.571  1.00 13.47 ? 209 TYR   A CB  1 
ATOM   1622 C  CG  . TYR   A 1 209 ? 18.842  -2.698  34.808  1.00 15.02 ? 209 TYR   A CG  1 
ATOM   1623 C  CD1 . TYR   A 1 209 ? 19.274  -3.190  36.039  1.00 15.50 ? 209 TYR   A CD1 1 
ATOM   1624 C  CD2 . TYR   A 1 209 ? 17.570  -2.119  34.757  1.00 15.17 ? 209 TYR   A CD2 1 
ATOM   1625 C  CE1 . TYR   A 1 209 ? 18.491  -3.067  37.181  1.00 14.97 ? 209 TYR   A CE1 1 
ATOM   1626 C  CE2 . TYR   A 1 209 ? 16.774  -2.016  35.887  1.00 14.96 ? 209 TYR   A CE2 1 
ATOM   1627 C  CZ  . TYR   A 1 209 ? 17.244  -2.483  37.104  1.00 15.97 ? 209 TYR   A CZ  1 
ATOM   1628 O  OH  . TYR   A 1 209 ? 16.450  -2.392  38.234  1.00 17.45 ? 209 TYR   A OH  1 
ATOM   1629 N  N   . ALA   A 1 210 ? 21.969  -2.381  31.355  1.00 15.02 ? 210 ALA   A N   1 
ATOM   1630 C  CA  . ALA   A 1 210 ? 23.050  -2.811  30.470  1.00 14.91 ? 210 ALA   A CA  1 
ATOM   1631 C  C   . ALA   A 1 210 ? 24.348  -2.154  30.897  1.00 14.74 ? 210 ALA   A C   1 
ATOM   1632 O  O   . ALA   A 1 210 ? 25.403  -2.788  30.878  1.00 15.86 ? 210 ALA   A O   1 
ATOM   1633 C  CB  . ALA   A 1 210 ? 22.771  -2.450  29.011  1.00 15.77 ? 210 ALA   A CB  1 
ATOM   1634 N  N   . ALA   A 1 211 ? 24.304  -0.857  31.189  1.00 14.35 ? 211 ALA   A N   1 
ATOM   1635 C  CA  . ALA   A 1 211 ? 25.514  -0.163  31.574  1.00 15.91 ? 211 ALA   A CA  1 
ATOM   1636 C  C   . ALA   A 1 211 ? 26.131  -0.803  32.820  1.00 16.64 ? 211 ALA   A C   1 
ATOM   1637 O  O   . ALA   A 1 211 ? 27.327  -1.060  32.870  1.00 16.84 ? 211 ALA   A O   1 
ATOM   1638 C  CB  . ALA   A 1 211 ? 25.242  1.288   31.773  1.00 16.73 ? 211 ALA   A CB  1 
ATOM   1639 N  N   . VAL   A 1 212 ? 25.295  -1.151  33.802  1.00 16.96 ? 212 VAL   A N   1 
ATOM   1640 C  CA  . VAL   A 1 212 ? 25.783  -1.724  35.043  1.00 17.54 ? 212 VAL   A CA  1 
ATOM   1641 C  C   . VAL   A 1 212 ? 26.405  -3.099  34.757  1.00 18.74 ? 212 VAL   A C   1 
ATOM   1642 O  O   . VAL   A 1 212 ? 27.482  -3.419  35.252  1.00 17.23 ? 212 VAL   A O   1 
ATOM   1643 C  CB  . VAL   A 1 212 ? 24.640  -1.789  36.075  1.00 17.45 ? 212 VAL   A CB  1 
ATOM   1644 C  CG1 . VAL   A 1 212 ? 24.956  -2.702  37.255  1.00 18.60 ? 212 VAL   A CG1 1 
ATOM   1645 C  CG2 . VAL   A 1 212 ? 24.271  -0.395  36.527  1.00 17.19 ? 212 VAL   A CG2 1 
ATOM   1646 N  N   . ILE   A 1 213 ? 25.709  -3.935  33.981  1.00 19.80 ? 213 ILE   A N   1 
ATOM   1647 C  CA  . ILE   A 1 213 ? 26.217  -5.251  33.603  1.00 18.91 ? 213 ILE   A CA  1 
ATOM   1648 C  C   . ILE   A 1 213 ? 27.588  -5.120  32.932  1.00 21.53 ? 213 ILE   A C   1 
ATOM   1649 O  O   . ILE   A 1 213 ? 28.428  -6.009  33.051  1.00 22.46 ? 213 ILE   A O   1 
ATOM   1650 C  CB  . ILE   A 1 213 ? 25.201  -5.939  32.675  1.00 19.34 ? 213 ILE   A CB  1 
ATOM   1651 C  CG1 . ILE   A 1 213 ? 23.936  -6.330  33.433  1.00 18.42 ? 213 ILE   A CG1 1 
ATOM   1652 C  CG2 . ILE   A 1 213 ? 25.835  -7.131  31.947  1.00 19.98 ? 213 ILE   A CG2 1 
ATOM   1653 C  CD1 . ILE   A 1 213 ? 22.754  -6.651  32.569  1.00 18.94 ? 213 ILE   A CD1 1 
ATOM   1654 N  N   . ASN   A 1 214 ? 27.825  -4.019  32.212  1.00 20.31 ? 214 ASN   A N   1 
ATOM   1655 C  CA  . ASN   A 1 214 ? 29.087  -3.812  31.533  1.00 21.77 ? 214 ASN   A CA  1 
ATOM   1656 C  C   . ASN   A 1 214 ? 30.049  -2.961  32.364  1.00 22.94 ? 214 ASN   A C   1 
ATOM   1657 O  O   . ASN   A 1 214 ? 31.027  -2.437  31.825  1.00 24.47 ? 214 ASN   A O   1 
ATOM   1658 C  CB  . ASN   A 1 214 ? 28.823  -3.172  30.170  1.00 22.94 ? 214 ASN   A CB  1 
ATOM   1659 C  CG  . ASN   A 1 214 ? 28.288  -4.196  29.195  1.00 23.13 ? 214 ASN   A CG  1 
ATOM   1660 O  OD1 . ASN   A 1 214 ? 29.061  -4.918  28.567  1.00 25.53 ? 214 ASN   A OD1 1 
ATOM   1661 N  ND2 . ASN   A 1 214 ? 26.973  -4.287  29.069  1.00 22.16 ? 214 ASN   A ND2 1 
ATOM   1662 N  N   . GLY   A 1 215 ? 29.756  -2.773  33.659  1.00 22.95 ? 215 GLY   A N   1 
ATOM   1663 C  CA  . GLY   A 1 215 ? 30.705  -2.157  34.577  1.00 22.96 ? 215 GLY   A CA  1 
ATOM   1664 C  C   . GLY   A 1 215 ? 30.671  -0.633  34.604  1.00 21.10 ? 215 GLY   A C   1 
ATOM   1665 O  O   . GLY   A 1 215 ? 31.553  -0.021  35.193  1.00 21.39 ? 215 GLY   A O   1 
ATOM   1666 N  N   . ASP   A 1 216 ? 29.668  0.002   33.998  1.00 19.60 ? 216 ASP   A N   1 
ATOM   1667 C  CA  . ASP   A 1 216 ? 29.600  1.453   34.016  1.00 21.88 ? 216 ASP   A CA  1 
ATOM   1668 C  C   . ASP   A 1 216 ? 28.496  1.847   35.016  1.00 23.55 ? 216 ASP   A C   1 
ATOM   1669 O  O   . ASP   A 1 216 ? 27.301  1.677   34.701  1.00 21.45 ? 216 ASP   A O   1 
ATOM   1670 C  CB  . ASP   A 1 216 ? 29.351  1.951   32.586  1.00 24.22 ? 216 ASP   A CB  1 
ATOM   1671 C  CG  . ASP   A 1 216 ? 29.889  3.326   32.238  1.00 27.76 ? 216 ASP   A CG  1 
ATOM   1672 O  OD1 . ASP   A 1 216 ? 30.439  3.994   33.146  1.00 29.37 ? 216 ASP   A OD1 1 
ATOM   1673 O  OD2 . ASP   A 1 216 ? 29.787  3.713   31.029  1.00 28.54 ? 216 ASP   A OD2 1 
ATOM   1674 N  N   . ARG   A 1 217 ? 28.900  2.408   36.188  1.00 21.06 ? 217 ARG   A N   1 
ATOM   1675 C  CA  . ARG   A 1 217 ? 28.048  2.444   37.373  1.00 20.46 ? 217 ARG   A CA  1 
ATOM   1676 C  C   . ARG   A 1 217 ? 28.011  3.790   38.091  1.00 17.90 ? 217 ARG   A C   1 
ATOM   1677 O  O   . ARG   A 1 217 ? 27.394  3.902   39.151  1.00 17.44 ? 217 ARG   A O   1 
ATOM   1678 C  CB  . ARG   A 1 217 ? 28.539  1.435   38.412  1.00 20.81 ? 217 ARG   A CB  1 
ATOM   1679 C  CG  . ARG   A 1 217 ? 28.429  -0.021  38.009  1.00 20.59 ? 217 ARG   A CG  1 
ATOM   1680 C  CD  . ARG   A 1 217 ? 29.004  -0.869  39.123  1.00 21.06 ? 217 ARG   A CD  1 
ATOM   1681 N  NE  . ARG   A 1 217 ? 28.117  -0.891  40.276  1.00 19.73 ? 217 ARG   A NE  1 
ATOM   1682 C  CZ  . ARG   A 1 217 ? 27.386  -1.916  40.661  1.00 18.94 ? 217 ARG   A CZ  1 
ATOM   1683 N  NH1 . ARG   A 1 217 ? 27.379  -3.026  39.955  1.00 20.38 ? 217 ARG   A NH1 1 
ATOM   1684 N  NH2 . ARG   A 1 217 ? 26.617  -1.808  41.733  1.00 19.40 ? 217 ARG   A NH2 1 
ATOM   1685 N  N   . TRP   A 1 218 ? 28.639  4.809   37.525  1.00 16.75 ? 218 TRP   A N   1 
ATOM   1686 C  CA  . TRP   A 1 218 ? 28.852  6.057   38.228  1.00 17.20 ? 218 TRP   A CA  1 
ATOM   1687 C  C   . TRP   A 1 218 ? 27.537  6.724   38.651  1.00 18.48 ? 218 TRP   A C   1 
ATOM   1688 O  O   . TRP   A 1 218 ? 27.505  7.510   39.613  1.00 17.47 ? 218 TRP   A O   1 
ATOM   1689 C  CB  . TRP   A 1 218 ? 29.708  6.983   37.356  1.00 17.56 ? 218 TRP   A CB  1 
ATOM   1690 C  CG  . TRP   A 1 218 ? 29.069  7.445   36.066  1.00 18.38 ? 218 TRP   A CG  1 
ATOM   1691 C  CD1 . TRP   A 1 218 ? 29.288  6.932   34.820  1.00 17.88 ? 218 TRP   A CD1 1 
ATOM   1692 C  CD2 . TRP   A 1 218 ? 28.169  8.561   35.879  1.00 18.35 ? 218 TRP   A CD2 1 
ATOM   1693 N  NE1 . TRP   A 1 218 ? 28.569  7.638   33.882  1.00 17.89 ? 218 TRP   A NE1 1 
ATOM   1694 C  CE2 . TRP   A 1 218 ? 27.872  8.633   34.500  1.00 18.33 ? 218 TRP   A CE2 1 
ATOM   1695 C  CE3 . TRP   A 1 218 ? 27.573  9.492   36.734  1.00 21.50 ? 218 TRP   A CE3 1 
ATOM   1696 C  CZ2 . TRP   A 1 218 ? 27.006  9.586   33.972  1.00 20.48 ? 218 TRP   A CZ2 1 
ATOM   1697 C  CZ3 . TRP   A 1 218 ? 26.696  10.423  36.217  1.00 20.38 ? 218 TRP   A CZ3 1 
ATOM   1698 C  CH2 . TRP   A 1 218 ? 26.448  10.491  34.852  1.00 20.40 ? 218 TRP   A CH2 1 
ATOM   1699 N  N   . PHE   A 1 219 ? 26.436  6.399   37.940  1.00 17.58 ? 219 PHE   A N   1 
ATOM   1700 C  CA  . PHE   A 1 219 ? 25.183  7.139   38.035  1.00 16.35 ? 219 PHE   A CA  1 
ATOM   1701 C  C   . PHE   A 1 219 ? 24.259  6.551   39.094  1.00 15.09 ? 219 PHE   A C   1 
ATOM   1702 O  O   . PHE   A 1 219 ? 23.190  7.096   39.329  1.00 16.07 ? 219 PHE   A O   1 
ATOM   1703 C  CB  . PHE   A 1 219 ? 24.459  7.120   36.670  1.00 15.75 ? 219 PHE   A CB  1 
ATOM   1704 C  CG  . PHE   A 1 219 ? 24.329  5.740   36.087  1.00 14.77 ? 219 PHE   A CG  1 
ATOM   1705 C  CD1 . PHE   A 1 219 ? 23.327  4.885   36.506  1.00 14.71 ? 219 PHE   A CD1 1 
ATOM   1706 C  CD2 . PHE   A 1 219 ? 25.269  5.258   35.192  1.00 15.55 ? 219 PHE   A CD2 1 
ATOM   1707 C  CE1 . PHE   A 1 219 ? 23.239  3.590   36.022  1.00 13.96 ? 219 PHE   A CE1 1 
ATOM   1708 C  CE2 . PHE   A 1 219 ? 25.177  3.960   34.691  1.00 15.16 ? 219 PHE   A CE2 1 
ATOM   1709 C  CZ  . PHE   A 1 219 ? 24.162  3.130   35.113  1.00 14.81 ? 219 PHE   A CZ  1 
ATOM   1710 N  N   . LEU   A 1 220 ? 24.605  5.391   39.640  1.00 15.49 ? 220 LEU   A N   1 
ATOM   1711 C  CA  . LEU   A 1 220 ? 23.829  4.801   40.707  1.00 16.52 ? 220 LEU   A CA  1 
ATOM   1712 C  C   . LEU   A 1 220 ? 23.923  5.676   41.953  1.00 19.89 ? 220 LEU   A C   1 
ATOM   1713 O  O   . LEU   A 1 220 ? 24.960  6.255   42.254  1.00 18.84 ? 220 LEU   A O   1 
ATOM   1714 C  CB  . LEU   A 1 220 ? 24.329  3.394   41.019  1.00 16.50 ? 220 LEU   A CB  1 
ATOM   1715 C  CG  . LEU   A 1 220 ? 24.241  2.372   39.891  1.00 16.05 ? 220 LEU   A CG  1 
ATOM   1716 C  CD1 . LEU   A 1 220 ? 24.886  1.065   40.327  1.00 16.09 ? 220 LEU   A CD1 1 
ATOM   1717 C  CD2 . LEU   A 1 220 ? 22.791  2.127   39.468  1.00 15.59 ? 220 LEU   A CD2 1 
ATOM   1718 N  N   . ASN   A 1 221 ? 22.814  5.726   42.690  1.00 24.35 ? 221 ASN   A N   1 
ATOM   1719 C  CA  . ASN   A 1 221 ? 22.769  6.364   43.991  1.00 30.29 ? 221 ASN   A CA  1 
ATOM   1720 C  C   . ASN   A 1 221 ? 21.980  5.471   44.952  1.00 33.57 ? 221 ASN   A C   1 
ATOM   1721 O  O   . ASN   A 1 221 ? 21.513  4.401   44.569  1.00 30.84 ? 221 ASN   A O   1 
ATOM   1722 C  CB  . ASN   A 1 221 ? 22.163  7.760   43.894  1.00 30.91 ? 221 ASN   A CB  1 
ATOM   1723 C  CG  . ASN   A 1 221 ? 20.753  7.736   43.358  1.00 35.03 ? 221 ASN   A CG  1 
ATOM   1724 O  OD1 . ASN   A 1 221 ? 19.922  6.925   43.771  1.00 42.73 ? 221 ASN   A OD1 1 
ATOM   1725 N  ND2 . ASN   A 1 221 ? 20.476  8.617   42.417  1.00 41.44 ? 221 ASN   A ND2 1 
ATOM   1726 N  N   . ARG   A 1 222 ? 21.857  5.905   46.215  1.00 39.13 ? 222 ARG   A N   1 
ATOM   1727 C  CA  . ARG   A 1 222 ? 21.217  5.096   47.244  1.00 43.30 ? 222 ARG   A CA  1 
ATOM   1728 C  C   . ARG   A 1 222 ? 19.834  5.644   47.599  1.00 46.31 ? 222 ARG   A C   1 
ATOM   1729 O  O   . ARG   A 1 222 ? 19.143  5.081   48.441  1.00 51.89 ? 222 ARG   A O   1 
ATOM   1730 C  CB  . ARG   A 1 222 ? 22.098  4.992   48.489  1.00 48.75 ? 222 ARG   A CB  1 
ATOM   1731 C  CG  . ARG   A 1 222 ? 23.518  4.526   48.203  1.00 51.84 ? 222 ARG   A CG  1 
ATOM   1732 C  CD  . ARG   A 1 222 ? 23.904  3.322   49.035  1.00 60.86 ? 222 ARG   A CD  1 
ATOM   1733 N  NE  . ARG   A 1 222 ? 23.319  2.071   48.555  1.00 72.10 ? 222 ARG   A NE  1 
ATOM   1734 C  CZ  . ARG   A 1 222 ? 22.959  1.034   49.317  1.00 77.00 ? 222 ARG   A CZ  1 
ATOM   1735 N  NH1 . ARG   A 1 222 ? 23.012  1.112   50.638  1.00 76.10 ? 222 ARG   A NH1 1 
ATOM   1736 N  NH2 . ARG   A 1 222 ? 22.538  -0.085  48.743  1.00 73.58 ? 222 ARG   A NH2 1 
ATOM   1737 N  N   . PHE   A 1 223 ? 19.395  6.720   46.937  1.00 47.74 ? 223 PHE   A N   1 
ATOM   1738 C  CA  . PHE   A 1 223 ? 18.001  7.113   47.042  1.00 46.40 ? 223 PHE   A CA  1 
ATOM   1739 C  C   . PHE   A 1 223 ? 17.125  5.952   46.571  1.00 42.87 ? 223 PHE   A C   1 
ATOM   1740 O  O   . PHE   A 1 223 ? 17.590  5.008   45.937  1.00 43.99 ? 223 PHE   A O   1 
ATOM   1741 C  CB  . PHE   A 1 223 ? 17.678  8.354   46.199  1.00 46.68 ? 223 PHE   A CB  1 
ATOM   1742 C  CG  . PHE   A 1 223 ? 18.521  9.573   46.470  1.00 53.53 ? 223 PHE   A CG  1 
ATOM   1743 C  CD1 . PHE   A 1 223 ? 18.567  10.139  47.734  1.00 54.21 ? 223 PHE   A CD1 1 
ATOM   1744 C  CD2 . PHE   A 1 223 ? 19.276  10.159  45.463  1.00 57.01 ? 223 PHE   A CD2 1 
ATOM   1745 C  CE1 . PHE   A 1 223 ? 19.345  11.261  47.980  1.00 54.12 ? 223 PHE   A CE1 1 
ATOM   1746 C  CE2 . PHE   A 1 223 ? 20.052  11.283  45.714  1.00 55.86 ? 223 PHE   A CE2 1 
ATOM   1747 C  CZ  . PHE   A 1 223 ? 20.085  11.831  46.971  1.00 54.63 ? 223 PHE   A CZ  1 
ATOM   1748 N  N   . THR   A 1 224 ? 15.842  6.027   46.903  1.00 39.17 ? 224 THR   A N   1 
ATOM   1749 C  CA  . THR   A 1 224 ? 14.835  5.251   46.200  1.00 36.79 ? 224 THR   A CA  1 
ATOM   1750 C  C   . THR   A 1 224 ? 13.624  6.167   46.059  1.00 28.45 ? 224 THR   A C   1 
ATOM   1751 O  O   . THR   A 1 224 ? 13.677  7.341   46.406  1.00 30.43 ? 224 THR   A O   1 
ATOM   1752 C  CB  . THR   A 1 224 ? 14.530  3.895   46.862  1.00 42.35 ? 224 THR   A CB  1 
ATOM   1753 O  OG1 . THR   A 1 224 ? 13.764  3.103   45.934  1.00 37.67 ? 224 THR   A OG1 1 
ATOM   1754 C  CG2 . THR   A 1 224 ? 13.797  4.037   48.181  1.00 41.11 ? 224 THR   A CG2 1 
ATOM   1755 N  N   . THR   A 1 225 ? 12.559  5.641   45.479  1.00 22.27 ? 225 THR   A N   1 
ATOM   1756 C  CA  . THR   A 1 225 ? 11.416  6.450   45.119  1.00 19.18 ? 225 THR   A CA  1 
ATOM   1757 C  C   . THR   A 1 225 ? 10.252  5.486   45.027  1.00 17.98 ? 225 THR   A C   1 
ATOM   1758 O  O   . THR   A 1 225 ? 10.445  4.265   44.896  1.00 18.05 ? 225 THR   A O   1 
ATOM   1759 C  CB  . THR   A 1 225 ? 11.664  7.210   43.795  1.00 18.01 ? 225 THR   A CB  1 
ATOM   1760 O  OG1 . THR   A 1 225 ? 10.538  8.007   43.406  1.00 17.62 ? 225 THR   A OG1 1 
ATOM   1761 C  CG2 . THR   A 1 225 ? 11.937  6.261   42.648  1.00 16.06 ? 225 THR   A CG2 1 
ATOM   1762 N  N   . THR   A 1 226 ? 9.054   6.044   45.127  1.00 17.85 ? 226 THR   A N   1 
ATOM   1763 C  CA  . THR   A 1 226 ? 7.854   5.315   44.780  1.00 17.77 ? 226 THR   A CA  1 
ATOM   1764 C  C   . THR   A 1 226 ? 7.709   5.414   43.264  1.00 18.13 ? 226 THR   A C   1 
ATOM   1765 O  O   . THR   A 1 226 ? 8.310   6.309   42.633  1.00 15.86 ? 226 THR   A O   1 
ATOM   1766 C  CB  . THR   A 1 226 ? 6.614   5.851   45.494  1.00 18.38 ? 226 THR   A CB  1 
ATOM   1767 O  OG1 . THR   A 1 226 ? 6.491   7.190   45.016  1.00 19.16 ? 226 THR   A OG1 1 
ATOM   1768 C  CG2 . THR   A 1 226 ? 6.682   5.781   47.013  1.00 19.40 ? 226 THR   A CG2 1 
ATOM   1769 N  N   . LEU   A 1 227 ? 6.919   4.486   42.727  1.00 15.58 ? 227 LEU   A N   1 
ATOM   1770 C  CA  . LEU   A 1 227 ? 6.620   4.472   41.313  1.00 16.32 ? 227 LEU   A CA  1 
ATOM   1771 C  C   . LEU   A 1 227 ? 5.897   5.770   40.955  1.00 17.07 ? 227 LEU   A C   1 
ATOM   1772 O  O   . LEU   A 1 227 ? 6.224   6.397   39.938  1.00 14.80 ? 227 LEU   A O   1 
ATOM   1773 C  CB  . LEU   A 1 227 ? 5.786   3.229   40.972  1.00 15.71 ? 227 LEU   A CB  1 
ATOM   1774 C  CG  . LEU   A 1 227 ? 5.510   3.041   39.476  1.00 16.63 ? 227 LEU   A CG  1 
ATOM   1775 C  CD1 . LEU   A 1 227 ? 6.797   2.782   38.714  1.00 16.66 ? 227 LEU   A CD1 1 
ATOM   1776 C  CD2 . LEU   A 1 227 ? 4.522   1.899   39.246  1.00 17.11 ? 227 LEU   A CD2 1 
ATOM   1777 N  N   . ASN   A 1 228 ? 4.931   6.183   41.798  1.00 15.64 ? 228 ASN   A N   1 
ATOM   1778 C  CA  . ASN   A 1 228 ? 4.171   7.383   41.497  1.00 16.55 ? 228 ASN   A CA  1 
ATOM   1779 C  C   . ASN   A 1 228 ? 5.063   8.621   41.475  1.00 15.80 ? 228 ASN   A C   1 
ATOM   1780 O  O   . ASN   A 1 228 ? 4.921   9.432   40.576  1.00 17.44 ? 228 ASN   A O   1 
ATOM   1781 C  CB  . ASN   A 1 228 ? 2.987   7.614   42.429  1.00 19.94 ? 228 ASN   A CB  1 
ATOM   1782 C  CG  . ASN   A 1 228 ? 2.195   8.830   41.982  1.00 22.21 ? 228 ASN   A CG  1 
ATOM   1783 O  OD1 . ASN   A 1 228 ? 1.598   8.842   40.911  1.00 25.54 ? 228 ASN   A OD1 1 
ATOM   1784 N  ND2 . ASN   A 1 228 ? 2.237   9.887   42.766  1.00 25.17 ? 228 ASN   A ND2 1 
ATOM   1785 N  N   . ASP   A 1 229 ? 5.932   8.797   42.472  1.00 15.20 ? 229 ASP   A N   1 
ATOM   1786 C  CA  . ASP   A 1 229 ? 6.794   9.958   42.530  1.00 15.50 ? 229 ASP   A CA  1 
ATOM   1787 C  C   . ASP   A 1 229 ? 7.755   9.971   41.328  1.00 16.31 ? 229 ASP   A C   1 
ATOM   1788 O  O   . ASP   A 1 229 ? 8.095   11.014  40.770  1.00 18.06 ? 229 ASP   A O   1 
ATOM   1789 C  CB  . ASP   A 1 229 ? 7.543   10.004  43.861  1.00 15.92 ? 229 ASP   A CB  1 
ATOM   1790 C  CG  . ASP   A 1 229 ? 6.655   10.269  45.084  1.00 17.88 ? 229 ASP   A CG  1 
ATOM   1791 O  OD1 . ASP   A 1 229 ? 5.521   10.718  44.899  1.00 15.98 ? 229 ASP   A OD1 1 
ATOM   1792 O  OD2 . ASP   A 1 229 ? 7.107   9.956   46.212  1.00 18.40 ? 229 ASP   A OD2 1 
ATOM   1793 N  N   . PHE   A 1 230 ? 8.236   8.809   40.913  1.00 14.69 ? 230 PHE   A N   1 
ATOM   1794 C  CA  . PHE   A 1 230 ? 9.099   8.767   39.745  1.00 14.17 ? 230 PHE   A CA  1 
ATOM   1795 C  C   . PHE   A 1 230 ? 8.309   9.206   38.507  1.00 13.55 ? 230 PHE   A C   1 
ATOM   1796 O  O   . PHE   A 1 230 ? 8.805   9.991   37.695  1.00 14.05 ? 230 PHE   A O   1 
ATOM   1797 C  CB  . PHE   A 1 230 ? 9.674   7.362   39.554  1.00 13.90 ? 230 PHE   A CB  1 
ATOM   1798 C  CG  . PHE   A 1 230 ? 10.342  7.223   38.212  1.00 13.29 ? 230 PHE   A CG  1 
ATOM   1799 C  CD1 . PHE   A 1 230 ? 11.588  7.794   38.007  1.00 13.31 ? 230 PHE   A CD1 1 
ATOM   1800 C  CD2 . PHE   A 1 230 ? 9.702   6.613   37.144  1.00 13.42 ? 230 PHE   A CD2 1 
ATOM   1801 C  CE1 . PHE   A 1 230 ? 12.219  7.716   36.771  1.00 13.08 ? 230 PHE   A CE1 1 
ATOM   1802 C  CE2 . PHE   A 1 230 ? 10.332  6.536   35.902  1.00 13.78 ? 230 PHE   A CE2 1 
ATOM   1803 C  CZ  . PHE   A 1 230 ? 11.584  7.088   35.725  1.00 12.95 ? 230 PHE   A CZ  1 
ATOM   1804 N  N   . ASN   A 1 231 ? 7.080   8.704   38.365  1.00 13.15 ? 231 ASN   A N   1 
ATOM   1805 C  CA  . ASN   A 1 231 ? 6.223   9.049   37.241  1.00 14.80 ? 231 ASN   A CA  1 
ATOM   1806 C  C   . ASN   A 1 231 ? 5.857   10.542  37.227  1.00 15.02 ? 231 ASN   A C   1 
ATOM   1807 O  O   . ASN   A 1 231 ? 5.720   11.130  36.157  1.00 14.70 ? 231 ASN   A O   1 
ATOM   1808 C  CB  . ASN   A 1 231 ? 4.967   8.175   37.167  1.00 15.80 ? 231 ASN   A CB  1 
ATOM   1809 C  CG  . ASN   A 1 231 ? 5.268   6.826   36.532  1.00 18.41 ? 231 ASN   A CG  1 
ATOM   1810 O  OD1 . ASN   A 1 231 ? 6.053   6.745   35.595  1.00 18.74 ? 231 ASN   A OD1 1 
ATOM   1811 N  ND2 . ASN   A 1 231 ? 4.709   5.761   37.074  1.00 17.02 ? 231 ASN   A ND2 1 
ATOM   1812 N  N   . LEU   A 1 232 ? 5.748   11.185  38.386  1.00 13.83 ? 232 LEU   A N   1 
ATOM   1813 C  CA  . LEU   A 1 232 ? 5.512   12.623  38.374  1.00 14.26 ? 232 LEU   A CA  1 
ATOM   1814 C  C   . LEU   A 1 232 ? 6.714   13.334  37.757  1.00 13.96 ? 232 LEU   A C   1 
ATOM   1815 O  O   . LEU   A 1 232 ? 6.555   14.264  36.977  1.00 13.90 ? 232 LEU   A O   1 
ATOM   1816 C  CB  . LEU   A 1 232 ? 5.240   13.150  39.796  1.00 14.30 ? 232 LEU   A CB  1 
ATOM   1817 C  CG  . LEU   A 1 232 ? 3.935   12.711  40.440  1.00 15.11 ? 232 LEU   A CG  1 
ATOM   1818 C  CD1 . LEU   A 1 232 ? 3.889   13.134  41.899  1.00 15.81 ? 232 LEU   A CD1 1 
ATOM   1819 C  CD2 . LEU   A 1 232 ? 2.756   13.311  39.692  1.00 16.36 ? 232 LEU   A CD2 1 
ATOM   1820 N  N   . VAL   A 1 233 ? 7.924   12.941  38.138  1.00 14.68 ? 233 VAL   A N   1 
ATOM   1821 C  CA  . VAL   A 1 233 ? 9.123   13.582  37.610  1.00 15.42 ? 233 VAL   A CA  1 
ATOM   1822 C  C   . VAL   A 1 233 ? 9.297   13.273  36.113  1.00 16.44 ? 233 VAL   A C   1 
ATOM   1823 O  O   . VAL   A 1 233 ? 9.489   14.174  35.296  1.00 14.70 ? 233 VAL   A O   1 
ATOM   1824 C  CB  . VAL   A 1 233 ? 10.362  13.187  38.421  1.00 16.99 ? 233 VAL   A CB  1 
ATOM   1825 C  CG1 . VAL   A 1 233 ? 11.637  13.746  37.805  1.00 18.63 ? 233 VAL   A CG1 1 
ATOM   1826 C  CG2 . VAL   A 1 233 ? 10.243  13.627  39.866  1.00 17.44 ? 233 VAL   A CG2 1 
ATOM   1827 N  N   . ALA   A 1 234 ? 9.144   11.999  35.733  1.00 17.36 ? 234 ALA   A N   1 
ATOM   1828 C  CA  . ALA   A 1 234 ? 9.248   11.584  34.345  1.00 17.07 ? 234 ALA   A CA  1 
ATOM   1829 C  C   . ALA   A 1 234 ? 8.351   12.425  33.442  1.00 17.49 ? 234 ALA   A C   1 
ATOM   1830 O  O   . ALA   A 1 234 ? 8.787   12.903  32.400  1.00 17.89 ? 234 ALA   A O   1 
ATOM   1831 C  CB  . ALA   A 1 234 ? 8.901   10.120  34.229  1.00 18.19 ? 234 ALA   A CB  1 
ATOM   1832 N  N   . MET   A 1 235 ? 7.074   12.539  33.812  1.00 18.44 ? 235 MET   A N   1 
ATOM   1833 C  CA  . MET   A 1 235 ? 6.109   13.299  33.043  1.00 20.16 ? 235 MET   A CA  1 
ATOM   1834 C  C   . MET   A 1 235 ? 6.583   14.738  32.852  1.00 17.84 ? 235 MET   A C   1 
ATOM   1835 O  O   . MET   A 1 235 ? 6.377   15.330  31.803  1.00 17.28 ? 235 MET   A O   1 
ATOM   1836 C  CB  . MET   A 1 235 ? 4.765   13.342  33.761  1.00 25.23 ? 235 MET   A CB  1 
ATOM   1837 C  CG  . MET   A 1 235 ? 3.926   12.089  33.600  1.00 33.64 ? 235 MET   A CG  1 
ATOM   1838 S  SD  . MET   A 1 235 ? 2.313   12.326  34.437  1.00 47.06 ? 235 MET   A SD  1 
ATOM   1839 C  CE  . MET   A 1 235 ? 1.481   13.260  33.154  1.00 43.51 ? 235 MET   A CE  1 
ATOM   1840 N  N   . LYS   A 1 236 ? 7.196   15.305  33.891  1.00 18.05 ? 236 LYS   A N   1 
ATOM   1841 C  CA  . LYS   A 1 236 ? 7.636   16.687  33.870  1.00 18.19 ? 236 LYS   A CA  1 
ATOM   1842 C  C   . LYS   A 1 236 ? 8.738   16.866  32.842  1.00 18.12 ? 236 LYS   A C   1 
ATOM   1843 O  O   . LYS   A 1 236 ? 8.840   17.936  32.261  1.00 18.80 ? 236 LYS   A O   1 
ATOM   1844 C  CB  . LYS   A 1 236 ? 8.131   17.109  35.256  1.00 19.15 ? 236 LYS   A CB  1 
ATOM   1845 C  CG  . LYS   A 1 236 ? 8.621   18.547  35.376  1.00 21.19 ? 236 LYS   A CG  1 
ATOM   1846 C  CD  . LYS   A 1 236 ? 9.206   18.828  36.742  1.00 21.09 ? 236 LYS   A CD  1 
ATOM   1847 C  CE  . LYS   A 1 236 ? 9.760   20.226  36.899  1.00 23.34 ? 236 LYS   A CE  1 
ATOM   1848 N  NZ  . LYS   A 1 236 ? 10.659  20.279  38.094  1.00 24.17 ? 236 LYS   A NZ  1 
ATOM   1849 N  N   . TYR   A 1 237 ? 9.549   15.822  32.615  1.00 17.92 ? 237 TYR   A N   1 
ATOM   1850 C  CA  . TYR   A 1 237 ? 10.648  15.859  31.653  1.00 16.65 ? 237 TYR   A CA  1 
ATOM   1851 C  C   . TYR   A 1 237 ? 10.325  15.192  30.312  1.00 16.06 ? 237 TYR   A C   1 
ATOM   1852 O  O   . TYR   A 1 237 ? 11.239  14.834  29.548  1.00 14.92 ? 237 TYR   A O   1 
ATOM   1853 C  CB  . TYR   A 1 237 ? 11.813  15.128  32.314  1.00 17.77 ? 237 TYR   A CB  1 
ATOM   1854 C  CG  . TYR   A 1 237 ? 12.544  15.986  33.340  1.00 20.58 ? 237 TYR   A CG  1 
ATOM   1855 C  CD1 . TYR   A 1 237 ? 13.576  16.856  32.959  1.00 22.05 ? 237 TYR   A CD1 1 
ATOM   1856 C  CD2 . TYR   A 1 237 ? 12.160  15.971  34.675  1.00 19.74 ? 237 TYR   A CD2 1 
ATOM   1857 C  CE1 . TYR   A 1 237 ? 14.224  17.656  33.890  1.00 20.76 ? 237 TYR   A CE1 1 
ATOM   1858 C  CE2 . TYR   A 1 237 ? 12.804  16.760  35.612  1.00 20.46 ? 237 TYR   A CE2 1 
ATOM   1859 C  CZ  . TYR   A 1 237 ? 13.823  17.612  35.211  1.00 21.72 ? 237 TYR   A CZ  1 
ATOM   1860 O  OH  . TYR   A 1 237 ? 14.489  18.377  36.120  1.00 22.72 ? 237 TYR   A OH  1 
ATOM   1861 N  N   . ASN   A 1 238 ? 9.038   15.024  30.014  1.00 16.20 ? 238 ASN   A N   1 
ATOM   1862 C  CA  . ASN   A 1 238 ? 8.587   14.478  28.736  1.00 17.32 ? 238 ASN   A CA  1 
ATOM   1863 C  C   . ASN   A 1 238 ? 9.102   13.055  28.540  1.00 16.46 ? 238 ASN   A C   1 
ATOM   1864 O  O   . ASN   A 1 238 ? 9.538   12.696  27.440  1.00 16.21 ? 238 ASN   A O   1 
ATOM   1865 C  CB  . ASN   A 1 238 ? 8.984   15.405  27.585  1.00 18.43 ? 238 ASN   A CB  1 
ATOM   1866 C  CG  . ASN   A 1 238 ? 8.249   16.723  27.717  1.00 22.44 ? 238 ASN   A CG  1 
ATOM   1867 O  OD1 . ASN   A 1 238 ? 8.859   17.751  27.995  1.00 30.78 ? 238 ASN   A OD1 1 
ATOM   1868 N  ND2 . ASN   A 1 238 ? 6.934   16.690  27.632  1.00 23.82 ? 238 ASN   A ND2 1 
ATOM   1869 N  N   . TYR   A 1 239 ? 9.041   12.275  29.626  1.00 15.33 ? 239 TYR   A N   1 
ATOM   1870 C  CA  . TYR   A 1 239 ? 9.282   10.843  29.614  1.00 16.08 ? 239 TYR   A CA  1 
ATOM   1871 C  C   . TYR   A 1 239 ? 7.931   10.132  29.684  1.00 17.03 ? 239 TYR   A C   1 
ATOM   1872 O  O   . TYR   A 1 239 ? 7.036   10.576  30.388  1.00 17.31 ? 239 TYR   A O   1 
ATOM   1873 C  CB  . TYR   A 1 239 ? 10.183  10.382  30.769  1.00 15.13 ? 239 TYR   A CB  1 
ATOM   1874 C  CG  . TYR   A 1 239 ? 11.675  10.411  30.475  1.00 14.71 ? 239 TYR   A CG  1 
ATOM   1875 C  CD1 . TYR   A 1 239 ? 12.292  11.563  30.015  1.00 15.13 ? 239 TYR   A CD1 1 
ATOM   1876 C  CD2 . TYR   A 1 239 ? 12.454  9.281   30.642  1.00 14.70 ? 239 TYR   A CD2 1 
ATOM   1877 C  CE1 . TYR   A 1 239 ? 13.645  11.573  29.711  1.00 15.79 ? 239 TYR   A CE1 1 
ATOM   1878 C  CE2 . TYR   A 1 239 ? 13.803  9.276   30.354  1.00 14.30 ? 239 TYR   A CE2 1 
ATOM   1879 C  CZ  . TYR   A 1 239 ? 14.402  10.435  29.902  1.00 14.51 ? 239 TYR   A CZ  1 
ATOM   1880 O  OH  . TYR   A 1 239 ? 15.739  10.477  29.622  1.00 16.17 ? 239 TYR   A OH  1 
ATOM   1881 N  N   . GLU   A 1 240 ? 7.819   8.984   29.003  1.00 17.46 ? 240 GLU   A N   1 
ATOM   1882 C  CA  . GLU   A 1 240 ? 6.608   8.178   29.083  1.00 18.37 ? 240 GLU   A CA  1 
ATOM   1883 C  C   . GLU   A 1 240 ? 6.406   7.658   30.511  1.00 17.09 ? 240 GLU   A C   1 
ATOM   1884 O  O   . GLU   A 1 240 ? 7.348   7.458   31.276  1.00 14.33 ? 240 GLU   A O   1 
ATOM   1885 C  CB  . GLU   A 1 240 ? 6.658   6.984   28.111  1.00 19.29 ? 240 GLU   A CB  1 
ATOM   1886 C  CG  . GLU   A 1 240 ? 6.497   7.367   26.659  1.00 20.59 ? 240 GLU   A CG  1 
ATOM   1887 C  CD  . GLU   A 1 240 ? 5.105   7.876   26.332  1.00 23.88 ? 240 GLU   A CD  1 
ATOM   1888 O  OE1 . GLU   A 1 240 ? 4.177   7.070   26.382  1.00 30.16 ? 240 GLU   A OE1 1 
ATOM   1889 O  OE2 . GLU   A 1 240 ? 4.956   9.076   26.025  1.00 26.53 ? 240 GLU   A OE2 1 
ATOM   1890 N  N   . PRO   A 1 241 ? 5.151   7.393   30.918  1.00 18.50 ? 241 PRO   A N   1 
ATOM   1891 C  CA  . PRO   A 1 241 ? 4.916   6.772   32.218  1.00 19.45 ? 241 PRO   A CA  1 
ATOM   1892 C  C   . PRO   A 1 241 ? 5.548   5.378   32.245  1.00 16.65 ? 241 PRO   A C   1 
ATOM   1893 O  O   . PRO   A 1 241 ? 5.654   4.710   31.224  1.00 14.70 ? 241 PRO   A O   1 
ATOM   1894 C  CB  . PRO   A 1 241 ? 3.380   6.665   32.319  1.00 20.31 ? 241 PRO   A CB  1 
ATOM   1895 C  CG  . PRO   A 1 241 ? 2.843   7.576   31.229  1.00 20.62 ? 241 PRO   A CG  1 
ATOM   1896 C  CD  . PRO   A 1 241 ? 3.918   7.649   30.165  1.00 19.17 ? 241 PRO   A CD  1 
ATOM   1897 N  N   . LEU   A 1 242 ? 5.982   4.972   33.432  1.00 16.63 ? 242 LEU   A N   1 
ATOM   1898 C  CA  . LEU   A 1 242 ? 6.431   3.616   33.693  1.00 15.60 ? 242 LEU   A CA  1 
ATOM   1899 C  C   . LEU   A 1 242 ? 5.312   2.893   34.429  1.00 15.22 ? 242 LEU   A C   1 
ATOM   1900 O  O   . LEU   A 1 242 ? 4.848   3.373   35.465  1.00 14.84 ? 242 LEU   A O   1 
ATOM   1901 C  CB  . LEU   A 1 242 ? 7.693   3.692   34.550  1.00 15.30 ? 242 LEU   A CB  1 
ATOM   1902 C  CG  . LEU   A 1 242 ? 8.471   2.391   34.668  1.00 15.47 ? 242 LEU   A CG  1 
ATOM   1903 C  CD1 . LEU   A 1 242 ? 9.181   2.097   33.346  1.00 15.02 ? 242 LEU   A CD1 1 
ATOM   1904 C  CD2 . LEU   A 1 242 ? 9.432   2.455   35.844  1.00 14.52 ? 242 LEU   A CD2 1 
ATOM   1905 N  N   . THR   A 1 243 ? 4.869   1.771   33.875  1.00 15.09 ? 243 THR   A N   1 
ATOM   1906 C  CA  . THR   A 1 243 ? 3.755   1.005   34.409  1.00 17.76 ? 243 THR   A CA  1 
ATOM   1907 C  C   . THR   A 1 243 ? 4.263   -0.126  35.301  1.00 17.83 ? 243 THR   A C   1 
ATOM   1908 O  O   . THR   A 1 243 ? 5.431   -0.467  35.281  1.00 18.09 ? 243 THR   A O   1 
ATOM   1909 C  CB  . THR   A 1 243 ? 2.924   0.397   33.278  1.00 19.22 ? 243 THR   A CB  1 
ATOM   1910 O  OG1 . THR   A 1 243 ? 3.733   -0.611  32.655  1.00 18.94 ? 243 THR   A OG1 1 
ATOM   1911 C  CG2 . THR   A 1 243 ? 2.471   1.436   32.271  1.00 20.66 ? 243 THR   A CG2 1 
ATOM   1912 N  N   . GLN   A 1 244 ? 3.376   -0.750  36.065  1.00 19.77 ? 244 GLN   A N   1 
ATOM   1913 C  CA  . GLN   A 1 244 ? 3.769   -1.921  36.835  1.00 20.06 ? 244 GLN   A CA  1 
ATOM   1914 C  C   . GLN   A 1 244 ? 4.246   -3.027  35.892  1.00 18.77 ? 244 GLN   A C   1 
ATOM   1915 O  O   . GLN   A 1 244 ? 5.187   -3.735  36.225  1.00 19.90 ? 244 GLN   A O   1 
ATOM   1916 C  CB  . GLN   A 1 244 ? 2.627   -2.418  37.732  1.00 22.84 ? 244 GLN   A CB  1 
ATOM   1917 C  CG  . GLN   A 1 244 ? 3.006   -3.613  38.611  1.00 23.70 ? 244 GLN   A CG  1 
ATOM   1918 C  CD  . GLN   A 1 244 ? 4.153   -3.313  39.551  1.00 23.16 ? 244 GLN   A CD  1 
ATOM   1919 O  OE1 . GLN   A 1 244 ? 4.237   -2.239  40.131  1.00 27.38 ? 244 GLN   A OE1 1 
ATOM   1920 N  NE2 . GLN   A 1 244 ? 5.063   -4.260  39.720  1.00 23.24 ? 244 GLN   A NE2 1 
ATOM   1921 N  N   . ASP   A 1 245 ? 3.616   -3.197  34.724  1.00 19.16 ? 245 ASP   A N   1 
ATOM   1922 C  CA  A ASP   A 1 245 ? 4.039   -4.219  33.778  0.50 19.38 ? 245 ASP   A CA  1 
ATOM   1923 C  CA  B ASP   A 1 245 ? 4.046   -4.227  33.790  0.50 19.23 ? 245 ASP   A CA  1 
ATOM   1924 C  C   . ASP   A 1 245 ? 5.488   -3.951  33.366  1.00 18.63 ? 245 ASP   A C   1 
ATOM   1925 O  O   . ASP   A 1 245 ? 6.300   -4.875  33.273  1.00 18.13 ? 245 ASP   A O   1 
ATOM   1926 C  CB  A ASP   A 1 245 ? 3.123   -4.250  32.550  0.50 20.14 ? 245 ASP   A CB  1 
ATOM   1927 C  CB  B ASP   A 1 245 ? 3.133   -4.314  32.565  0.50 19.82 ? 245 ASP   A CB  1 
ATOM   1928 C  CG  A ASP   A 1 245 ? 1.690   -4.691  32.804  0.50 20.23 ? 245 ASP   A CG  1 
ATOM   1929 C  CG  B ASP   A 1 245 ? 3.393   -5.558  31.730  0.50 19.56 ? 245 ASP   A CG  1 
ATOM   1930 O  OD1 A ASP   A 1 245 ? 1.391   -5.175  33.920  0.50 20.91 ? 245 ASP   A OD1 1 
ATOM   1931 O  OD1 B ASP   A 1 245 ? 3.214   -6.658  32.269  0.50 19.72 ? 245 ASP   A OD1 1 
ATOM   1932 O  OD2 A ASP   A 1 245 ? 0.887   -4.577  31.870  0.50 20.11 ? 245 ASP   A OD2 1 
ATOM   1933 O  OD2 B ASP   A 1 245 ? 3.777   -5.416  30.550  0.50 20.59 ? 245 ASP   A OD2 1 
ATOM   1934 N  N   . HIS   A 1 246 ? 5.819   -2.669  33.124  1.00 16.79 ? 246 HIS   A N   1 
ATOM   1935 C  CA  . HIS   A 1 246 ? 7.197   -2.292  32.867  1.00 15.38 ? 246 HIS   A CA  1 
ATOM   1936 C  C   . HIS   A 1 246 ? 8.119   -2.722  34.008  1.00 15.47 ? 246 HIS   A C   1 
ATOM   1937 O  O   . HIS   A 1 246 ? 9.209   -3.253  33.760  1.00 14.82 ? 246 HIS   A O   1 
ATOM   1938 C  CB  . HIS   A 1 246 ? 7.343   -0.795  32.620  1.00 15.80 ? 246 HIS   A CB  1 
ATOM   1939 C  CG  . HIS   A 1 246 ? 6.729   -0.341  31.355  1.00 16.80 ? 246 HIS   A CG  1 
ATOM   1940 N  ND1 . HIS   A 1 246 ? 6.253   0.939   31.185  1.00 16.83 ? 246 HIS   A ND1 1 
ATOM   1941 C  CD2 . HIS   A 1 246 ? 6.632   -0.953  30.154  1.00 17.42 ? 246 HIS   A CD2 1 
ATOM   1942 C  CE1 . HIS   A 1 246 ? 5.801   1.057   29.933  1.00 17.91 ? 246 HIS   A CE1 1 
ATOM   1943 N  NE2 . HIS   A 1 246 ? 6.029   -0.076  29.287  1.00 16.77 ? 246 HIS   A NE2 1 
ATOM   1944 N  N   . VAL   A 1 247 ? 7.733   -2.421  35.255  1.00 14.57 ? 247 VAL   A N   1 
ATOM   1945 C  CA  . VAL   A 1 247 ? 8.529   -2.834  36.401  1.00 15.36 ? 247 VAL   A CA  1 
ATOM   1946 C  C   . VAL   A 1 247 ? 8.761   -4.349  36.337  1.00 16.22 ? 247 VAL   A C   1 
ATOM   1947 O  O   . VAL   A 1 247 ? 9.880   -4.834  36.559  1.00 14.69 ? 247 VAL   A O   1 
ATOM   1948 C  CB  . VAL   A 1 247 ? 7.864   -2.409  37.733  1.00 15.64 ? 247 VAL   A CB  1 
ATOM   1949 C  CG1 . VAL   A 1 247 ? 8.564   -3.037  38.923  1.00 16.53 ? 247 VAL   A CG1 1 
ATOM   1950 C  CG2 . VAL   A 1 247 ? 7.825   -0.888  37.909  1.00 15.21 ? 247 VAL   A CG2 1 
ATOM   1951 N  N   . ASP   A 1 248 ? 7.697   -5.097  36.004  1.00 17.81 ? 248 ASP   A N   1 
ATOM   1952 C  CA  . ASP   A 1 248 ? 7.773   -6.557  35.949  1.00 20.45 ? 248 ASP   A CA  1 
ATOM   1953 C  C   . ASP   A 1 248 ? 8.770   -7.047  34.897  1.00 20.47 ? 248 ASP   A C   1 
ATOM   1954 O  O   . ASP   A 1 248 ? 9.539   -7.944  35.190  1.00 22.21 ? 248 ASP   A O   1 
ATOM   1955 C  CB  . ASP   A 1 248 ? 6.399   -7.173  35.699  1.00 21.38 ? 248 ASP   A CB  1 
ATOM   1956 C  CG  . ASP   A 1 248 ? 5.432   -7.006  36.856  1.00 24.15 ? 248 ASP   A CG  1 
ATOM   1957 O  OD1 . ASP   A 1 248 ? 5.868   -6.624  37.963  1.00 27.20 ? 248 ASP   A OD1 1 
ATOM   1958 O  OD2 . ASP   A 1 248 ? 4.248   -7.209  36.634  1.00 27.48 ? 248 ASP   A OD2 1 
ATOM   1959 N  N   A ILE   A 1 249 ? 8.749   -6.443  33.700  0.56 21.45 ? 249 ILE   A N   1 
ATOM   1960 N  N   B ILE   A 1 249 ? 8.765   -6.459  33.693  0.44 20.40 ? 249 ILE   A N   1 
ATOM   1961 C  CA  A ILE   A 1 249 ? 9.615   -6.831  32.594  0.56 22.18 ? 249 ILE   A CA  1 
ATOM   1962 C  CA  B ILE   A 1 249 ? 9.644   -6.926  32.631  0.44 20.25 ? 249 ILE   A CA  1 
ATOM   1963 C  C   A ILE   A 1 249 ? 11.076  -6.525  32.926  0.56 21.26 ? 249 ILE   A C   1 
ATOM   1964 C  C   B ILE   A 1 249 ? 11.091  -6.520  32.911  0.44 20.12 ? 249 ILE   A C   1 
ATOM   1965 O  O   A ILE   A 1 249 ? 11.972  -7.120  32.346  0.56 22.48 ? 249 ILE   A O   1 
ATOM   1966 O  O   B ILE   A 1 249 ? 11.994  -7.054  32.282  0.44 21.07 ? 249 ILE   A O   1 
ATOM   1967 C  CB  A ILE   A 1 249 ? 9.181   -6.156  31.277  0.56 22.26 ? 249 ILE   A CB  1 
ATOM   1968 C  CB  B ILE   A 1 249 ? 9.187   -6.462  31.235  0.44 19.04 ? 249 ILE   A CB  1 
ATOM   1969 C  CG1 A ILE   A 1 249 ? 7.769   -6.573  30.867  0.56 23.94 ? 249 ILE   A CG1 1 
ATOM   1970 C  CG1 B ILE   A 1 249 ? 9.235   -4.946  31.081  0.44 18.41 ? 249 ILE   A CG1 1 
ATOM   1971 C  CG2 A ILE   A 1 249 ? 10.178  -6.450  30.164  0.56 23.77 ? 249 ILE   A CG2 1 
ATOM   1972 C  CG2 B ILE   A 1 249 ? 7.812   -7.003  30.902  0.44 20.09 ? 249 ILE   A CG2 1 
ATOM   1973 C  CD1 A ILE   A 1 249 ? 7.123   -5.661  29.852  0.56 24.31 ? 249 ILE   A CD1 1 
ATOM   1974 C  CD1 B ILE   A 1 249 ? 8.945   -4.489  29.675  0.44 17.94 ? 249 ILE   A CD1 1 
ATOM   1975 N  N   . LEU   A 1 250 ? 11.326  -5.574  33.833  1.00 19.16 ? 250 LEU   A N   1 
ATOM   1976 C  CA  . LEU   A 1 250 ? 12.692  -5.246  34.206  1.00 17.38 ? 250 LEU   A CA  1 
ATOM   1977 C  C   . LEU   A 1 250 ? 13.219  -6.211  35.266  1.00 16.97 ? 250 LEU   A C   1 
ATOM   1978 O  O   . LEU   A 1 250 ? 14.400  -6.154  35.584  1.00 18.36 ? 250 LEU   A O   1 
ATOM   1979 C  CB  . LEU   A 1 250 ? 12.778  -3.784  34.663  1.00 17.80 ? 250 LEU   A CB  1 
ATOM   1980 C  CG  . LEU   A 1 250 ? 12.595  -2.758  33.547  1.00 17.75 ? 250 LEU   A CG  1 
ATOM   1981 C  CD1 . LEU   A 1 250 ? 12.309  -1.381  34.120  1.00 17.45 ? 250 LEU   A CD1 1 
ATOM   1982 C  CD2 . LEU   A 1 250 ? 13.842  -2.728  32.646  1.00 16.98 ? 250 LEU   A CD2 1 
ATOM   1983 N  N   . GLY   A 1 251 ? 12.350  -7.094  35.781  1.00 19.12 ? 251 GLY   A N   1 
ATOM   1984 C  CA  . GLY   A 1 251 ? 12.674  -8.042  36.844  1.00 19.78 ? 251 GLY   A CA  1 
ATOM   1985 C  C   . GLY   A 1 251 ? 13.994  -8.781  36.621  1.00 19.07 ? 251 GLY   A C   1 
ATOM   1986 O  O   . GLY   A 1 251 ? 14.917  -8.684  37.423  1.00 20.88 ? 251 GLY   A O   1 
ATOM   1987 N  N   . PRO   A 1 252 ? 14.164  -9.524  35.514  1.00 21.27 ? 252 PRO   A N   1 
ATOM   1988 C  CA  . PRO   A 1 252 ? 15.413  -10.260 35.271  1.00 20.86 ? 252 PRO   A CA  1 
ATOM   1989 C  C   . PRO   A 1 252 ? 16.672  -9.407  35.312  1.00 19.98 ? 252 PRO   A C   1 
ATOM   1990 O  O   . PRO   A 1 252 ? 17.695  -9.842  35.867  1.00 22.64 ? 252 PRO   A O   1 
ATOM   1991 C  CB  . PRO   A 1 252 ? 15.195  -10.876 33.880  1.00 22.63 ? 252 PRO   A CB  1 
ATOM   1992 C  CG  . PRO   A 1 252 ? 13.690  -11.031 33.806  1.00 23.67 ? 252 PRO   A CG  1 
ATOM   1993 C  CD  . PRO   A 1 252 ? 13.142  -9.786  34.488  1.00 23.13 ? 252 PRO   A CD  1 
ATOM   1994 N  N   . LEU   A 1 253 ? 16.630  -8.172  34.775  1.00 18.13 ? 253 LEU   A N   1 
ATOM   1995 C  CA  . LEU   A 1 253 ? 17.807  -7.308  34.865  1.00 17.92 ? 253 LEU   A CA  1 
ATOM   1996 C  C   . LEU   A 1 253 ? 18.027  -6.823  36.305  1.00 17.22 ? 253 LEU   A C   1 
ATOM   1997 O  O   . LEU   A 1 253 ? 19.149  -6.639  36.747  1.00 18.33 ? 253 LEU   A O   1 
ATOM   1998 C  CB  . LEU   A 1 253 ? 17.641  -6.132  33.898  1.00 17.79 ? 253 LEU   A CB  1 
ATOM   1999 C  CG  . LEU   A 1 253 ? 17.657  -6.495  32.410  1.00 17.00 ? 253 LEU   A CG  1 
ATOM   2000 C  CD1 . LEU   A 1 253 ? 17.318  -5.283  31.574  1.00 16.66 ? 253 LEU   A CD1 1 
ATOM   2001 C  CD2 . LEU   A 1 253 ? 19.013  -7.044  31.995  1.00 16.86 ? 253 LEU   A CD2 1 
ATOM   2002 N  N   . SER   A 1 254 ? 16.939  -6.564  37.031  1.00 19.77 ? 254 SER   A N   1 
ATOM   2003 C  CA  . SER   A 1 254 ? 17.025  -6.207  38.440  1.00 19.89 ? 254 SER   A CA  1 
ATOM   2004 C  C   . SER   A 1 254 ? 17.718  -7.321  39.228  1.00 20.50 ? 254 SER   A C   1 
ATOM   2005 O  O   . SER   A 1 254 ? 18.676  -7.062  39.941  1.00 23.27 ? 254 SER   A O   1 
ATOM   2006 C  CB  . SER   A 1 254 ? 15.666  -5.920  39.019  1.00 19.56 ? 254 SER   A CB  1 
ATOM   2007 O  OG  . SER   A 1 254 ? 15.832  -5.431  40.358  1.00 20.52 ? 254 SER   A OG  1 
ATOM   2008 N  N   . ALA   A 1 255 ? 17.246  -8.559  39.051  1.00 22.41 ? 255 ALA   A N   1 
ATOM   2009 C  CA  . ALA   A 1 255 ? 17.798  -9.724  39.738  1.00 26.12 ? 255 ALA   A CA  1 
ATOM   2010 C  C   . ALA   A 1 255 ? 19.267  -9.959  39.378  1.00 27.55 ? 255 ALA   A C   1 
ATOM   2011 O  O   . ALA   A 1 255 ? 20.108  -10.197 40.248  1.00 28.45 ? 255 ALA   A O   1 
ATOM   2012 C  CB  . ALA   A 1 255 ? 16.949  -10.924 39.391  1.00 28.75 ? 255 ALA   A CB  1 
ATOM   2013 N  N   . GLN   A 1 256 ? 19.603  -9.855  38.093  1.00 28.18 ? 256 GLN   A N   1 
ATOM   2014 C  CA  . GLN   A 1 256 ? 20.965  -10.066 37.641  1.00 26.64 ? 256 GLN   A CA  1 
ATOM   2015 C  C   . GLN   A 1 256 ? 21.933  -9.097  38.315  1.00 27.75 ? 256 GLN   A C   1 
ATOM   2016 O  O   . GLN   A 1 256 ? 23.046  -9.490  38.646  1.00 27.63 ? 256 GLN   A O   1 
ATOM   2017 C  CB  . GLN   A 1 256 ? 21.013  -9.899  36.121  1.00 30.19 ? 256 GLN   A CB  1 
ATOM   2018 C  CG  . GLN   A 1 256 ? 22.368  -10.180 35.487  1.00 32.85 ? 256 GLN   A CG  1 
ATOM   2019 C  CD  . GLN   A 1 256 ? 22.260  -10.231 33.978  1.00 38.05 ? 256 GLN   A CD  1 
ATOM   2020 O  OE1 . GLN   A 1 256 ? 21.166  -10.282 33.417  1.00 48.54 ? 256 GLN   A OE1 1 
ATOM   2021 N  NE2 . GLN   A 1 256 ? 23.395  -10.232 33.296  1.00 40.28 ? 256 GLN   A NE2 1 
ATOM   2022 N  N   . THR   A 1 257 ? 21.552  -7.816  38.442  1.00 25.88 ? 257 THR   A N   1 
ATOM   2023 C  CA  . THR   A 1 257 ? 22.465  -6.779  38.891  1.00 22.04 ? 257 THR   A CA  1 
ATOM   2024 C  C   . THR   A 1 257 ? 22.336  -6.518  40.384  1.00 21.08 ? 257 THR   A C   1 
ATOM   2025 O  O   . THR   A 1 257 ? 23.183  -5.815  40.923  1.00 22.49 ? 257 THR   A O   1 
ATOM   2026 C  CB  . THR   A 1 257 ? 22.198  -5.453  38.176  1.00 23.98 ? 257 THR   A CB  1 
ATOM   2027 O  OG1 . THR   A 1 257 ? 20.838  -5.077  38.445  1.00 22.79 ? 257 THR   A OG1 1 
ATOM   2028 C  CG2 . THR   A 1 257 ? 22.452  -5.566  36.683  1.00 25.39 ? 257 THR   A CG2 1 
ATOM   2029 N  N   . GLY   A 1 258 ? 21.269  -7.032  41.005  1.00 20.32 ? 258 GLY   A N   1 
ATOM   2030 C  CA  . GLY   A 1 258 ? 20.962  -6.746  42.398  1.00 21.36 ? 258 GLY   A CA  1 
ATOM   2031 C  C   . GLY   A 1 258 ? 20.477  -5.314  42.629  1.00 22.15 ? 258 GLY   A C   1 
ATOM   2032 O  O   . GLY   A 1 258 ? 20.466  -4.841  43.770  1.00 23.51 ? 258 GLY   A O   1 
ATOM   2033 N  N   . ILE   A 1 259 ? 20.050  -4.610  41.564  1.00 21.22 ? 259 ILE   A N   1 
ATOM   2034 C  CA  . ILE   A 1 259 ? 19.585  -3.229  41.707  1.00 19.23 ? 259 ILE   A CA  1 
ATOM   2035 C  C   . ILE   A 1 259 ? 18.080  -3.228  41.507  1.00 18.82 ? 259 ILE   A C   1 
ATOM   2036 O  O   . ILE   A 1 259 ? 17.615  -3.556  40.407  1.00 20.38 ? 259 ILE   A O   1 
ATOM   2037 C  CB  . ILE   A 1 259 ? 20.290  -2.251  40.743  1.00 19.09 ? 259 ILE   A CB  1 
ATOM   2038 C  CG1 . ILE   A 1 259 ? 21.806  -2.367  40.846  1.00 19.43 ? 259 ILE   A CG1 1 
ATOM   2039 C  CG2 . ILE   A 1 259 ? 19.822  -0.805  40.983  1.00 19.68 ? 259 ILE   A CG2 1 
ATOM   2040 C  CD1 . ILE   A 1 259 ? 22.576  -1.533  39.873  1.00 20.84 ? 259 ILE   A CD1 1 
ATOM   2041 N  N   . ALA   A 1 260 ? 17.330  -2.902  42.578  1.00 16.08 ? 260 ALA   A N   1 
ATOM   2042 C  CA  . ALA   A 1 260 ? 15.880  -2.857  42.537  1.00 15.34 ? 260 ALA   A CA  1 
ATOM   2043 C  C   . ALA   A 1 260 ? 15.431  -1.866  41.470  1.00 13.88 ? 260 ALA   A C   1 
ATOM   2044 O  O   . ALA   A 1 260 ? 16.075  -0.843  41.256  1.00 13.91 ? 260 ALA   A O   1 
ATOM   2045 C  CB  . ALA   A 1 260 ? 15.316  -2.446  43.894  1.00 16.76 ? 260 ALA   A CB  1 
ATOM   2046 N  N   . VAL   A 1 261 ? 14.302  -2.168  40.836  1.00 13.70 ? 261 VAL   A N   1 
ATOM   2047 C  CA  . VAL   A 1 261 ? 13.791  -1.326  39.778  1.00 14.43 ? 261 VAL   A CA  1 
ATOM   2048 C  C   . VAL   A 1 261 ? 13.590  0.112   40.250  1.00 14.96 ? 261 VAL   A C   1 
ATOM   2049 O  O   . VAL   A 1 261 ? 13.959  1.036   39.537  1.00 16.04 ? 261 VAL   A O   1 
ATOM   2050 C  CB  . VAL   A 1 261 ? 12.501  -1.890  39.185  1.00 13.93 ? 261 VAL   A CB  1 
ATOM   2051 C  CG1 . VAL   A 1 261 ? 11.899  -0.920  38.172  1.00 13.99 ? 261 VAL   A CG1 1 
ATOM   2052 C  CG2 . VAL   A 1 261 ? 12.762  -3.248  38.551  1.00 14.67 ? 261 VAL   A CG2 1 
ATOM   2053 N  N   . LEU   A 1 262 ? 13.005  0.308   41.440  1.00 15.55 ? 262 LEU   A N   1 
ATOM   2054 C  CA  . LEU   A 1 262 ? 12.724  1.652   41.931  1.00 14.89 ? 262 LEU   A CA  1 
ATOM   2055 C  C   . LEU   A 1 262 ? 14.002  2.368   42.334  1.00 14.65 ? 262 LEU   A C   1 
ATOM   2056 O  O   . LEU   A 1 262 ? 14.028  3.597   42.299  1.00 14.44 ? 262 LEU   A O   1 
ATOM   2057 C  CB  . LEU   A 1 262 ? 11.734  1.596   43.097  1.00 15.82 ? 262 LEU   A CB  1 
ATOM   2058 C  CG  . LEU   A 1 262 ? 10.315  1.173   42.717  1.00 17.18 ? 262 LEU   A CG  1 
ATOM   2059 C  CD1 . LEU   A 1 262 ? 9.435   1.042   43.954  1.00 18.40 ? 262 LEU   A CD1 1 
ATOM   2060 C  CD2 . LEU   A 1 262 ? 9.690   2.162   41.725  1.00 17.14 ? 262 LEU   A CD2 1 
ATOM   2061 N  N   . ASP   A 1 263 ? 15.069  1.626   42.679  1.00 14.89 ? 263 ASP   A N   1 
ATOM   2062 C  CA  . ASP   A 1 263 ? 16.370  2.247   42.890  1.00 14.24 ? 263 ASP   A CA  1 
ATOM   2063 C  C   . ASP   A 1 263 ? 16.954  2.759   41.574  1.00 13.34 ? 263 ASP   A C   1 
ATOM   2064 O  O   . ASP   A 1 263 ? 17.569  3.825   41.506  1.00 13.35 ? 263 ASP   A O   1 
ATOM   2065 C  CB  . ASP   A 1 263 ? 17.371  1.290   43.526  1.00 15.48 ? 263 ASP   A CB  1 
ATOM   2066 C  CG  . ASP   A 1 263 ? 17.023  0.907   44.949  1.00 17.30 ? 263 ASP   A CG  1 
ATOM   2067 O  OD1 . ASP   A 1 263 ? 15.989  1.360   45.436  1.00 17.17 ? 263 ASP   A OD1 1 
ATOM   2068 O  OD2 . ASP   A 1 263 ? 17.781  0.119   45.528  1.00 18.88 ? 263 ASP   A OD2 1 
ATOM   2069 N  N   . MET   A 1 264 ? 16.771  1.999   40.496  1.00 13.71 ? 264 MET   A N   1 
ATOM   2070 C  CA  . MET   A 1 264 ? 17.264  2.466   39.199  1.00 12.78 ? 264 MET   A CA  1 
ATOM   2071 C  C   . MET   A 1 264 ? 16.420  3.673   38.748  1.00 12.12 ? 264 MET   A C   1 
ATOM   2072 O  O   . MET   A 1 264 ? 16.925  4.603   38.134  1.00 12.57 ? 264 MET   A O   1 
ATOM   2073 C  CB  . MET   A 1 264 ? 17.216  1.336   38.169  1.00 12.24 ? 264 MET   A CB  1 
ATOM   2074 C  CG  . MET   A 1 264 ? 17.929  1.707   36.869  1.00 12.65 ? 264 MET   A CG  1 
ATOM   2075 S  SD  . MET   A 1 264 ? 19.717  1.922   37.102  1.00 12.78 ? 264 MET   A SD  1 
ATOM   2076 C  CE  . MET   A 1 264 ? 20.213  0.209   37.075  1.00 12.42 ? 264 MET   A CE  1 
ATOM   2077 N  N   . CYS   A 1 265 ? 15.112  3.666   39.046  1.00 12.75 ? 265 CYS   A N   1 
ATOM   2078 C  CA  . CYS   A 1 265 ? 14.266  4.837   38.814  1.00 12.91 ? 265 CYS   A CA  1 
ATOM   2079 C  C   . CYS   A 1 265 ? 14.809  6.065   39.541  1.00 13.26 ? 265 CYS   A C   1 
ATOM   2080 O  O   . CYS   A 1 265 ? 14.843  7.175   38.996  1.00 13.18 ? 265 CYS   A O   1 
ATOM   2081 C  CB  . CYS   A 1 265 ? 12.835  4.568   39.266  1.00 13.28 ? 265 CYS   A CB  1 
ATOM   2082 S  SG  . CYS   A 1 265 ? 11.908  3.399   38.238  1.00 14.08 ? 265 CYS   A SG  1 
ATOM   2083 N  N   . ALA   A 1 266 ? 15.236  5.888   40.800  1.00 14.08 ? 266 ALA   A N   1 
ATOM   2084 C  CA  . ALA   A 1 266 ? 15.796  7.004   41.559  1.00 14.63 ? 266 ALA   A CA  1 
ATOM   2085 C  C   . ALA   A 1 266 ? 17.069  7.515   40.905  1.00 14.20 ? 266 ALA   A C   1 
ATOM   2086 O  O   . ALA   A 1 266 ? 17.342  8.710   40.918  1.00 14.05 ? 266 ALA   A O   1 
ATOM   2087 C  CB  . ALA   A 1 266 ? 16.043  6.619   42.996  1.00 15.59 ? 266 ALA   A CB  1 
ATOM   2088 N  N   . SER   A 1 267 ? 17.833  6.614   40.285  1.00 15.41 ? 267 SER   A N   1 
ATOM   2089 C  CA  . SER   A 1 267 ? 19.054  7.001   39.591  1.00 15.35 ? 267 SER   A CA  1 
ATOM   2090 C  C   . SER   A 1 267 ? 18.738  7.838   38.357  1.00 13.59 ? 267 SER   A C   1 
ATOM   2091 O  O   . SER   A 1 267 ? 19.357  8.868   38.104  1.00 13.55 ? 267 SER   A O   1 
ATOM   2092 C  CB  . SER   A 1 267 ? 19.870  5.769   39.257  1.00 17.45 ? 267 SER   A CB  1 
ATOM   2093 O  OG  . SER   A 1 267 ? 20.353  5.188   40.480  1.00 19.74 ? 267 SER   A OG  1 
ATOM   2094 N  N   . LEU   A 1 268 ? 17.749  7.381   37.593  1.00 13.30 ? 268 LEU   A N   1 
ATOM   2095 C  CA  . LEU   A 1 268 ? 17.323  8.095   36.411  1.00 12.66 ? 268 LEU   A CA  1 
ATOM   2096 C  C   . LEU   A 1 268 ? 16.750  9.460   36.784  1.00 13.25 ? 268 LEU   A C   1 
ATOM   2097 O  O   . LEU   A 1 268 ? 17.017  10.450  36.113  1.00 13.64 ? 268 LEU   A O   1 
ATOM   2098 C  CB  . LEU   A 1 268 ? 16.277  7.255   35.681  1.00 12.32 ? 268 LEU   A CB  1 
ATOM   2099 C  CG  . LEU   A 1 268 ? 15.679  7.905   34.432  1.00 12.26 ? 268 LEU   A CG  1 
ATOM   2100 C  CD1 . LEU   A 1 268 ? 16.777  8.412   33.500  1.00 11.94 ? 268 LEU   A CD1 1 
ATOM   2101 C  CD2 . LEU   A 1 268 ? 14.802  6.905   33.706  1.00 12.29 ? 268 LEU   A CD2 1 
ATOM   2102 N  N   . LYS   A 1 269 ? 15.937  9.508   37.835  1.00 14.56 ? 269 LYS   A N   1 
ATOM   2103 C  CA  . LYS   A 1 269 ? 15.407  10.770  38.317  1.00 16.81 ? 269 LYS   A CA  1 
ATOM   2104 C  C   . LYS   A 1 269 ? 16.523  11.786  38.532  1.00 16.73 ? 269 LYS   A C   1 
ATOM   2105 O  O   . LYS   A 1 269 ? 16.386  12.932  38.096  1.00 18.85 ? 269 LYS   A O   1 
ATOM   2106 C  CB  . LYS   A 1 269 ? 14.636  10.560  39.616  1.00 18.32 ? 269 LYS   A CB  1 
ATOM   2107 C  CG  . LYS   A 1 269 ? 13.884  11.770  40.096  1.00 19.21 ? 269 LYS   A CG  1 
ATOM   2108 C  CD  . LYS   A 1 269 ? 13.387  11.622  41.503  1.00 20.84 ? 269 LYS   A CD  1 
ATOM   2109 C  CE  . LYS   A 1 269 ? 12.189  10.699  41.613  1.00 21.59 ? 269 LYS   A CE  1 
ATOM   2110 N  NZ  . LYS   A 1 269 ? 11.791  10.559  43.022  1.00 21.41 ? 269 LYS   A NZ  1 
ATOM   2111 N  N   . GLU   A 1 270 ? 17.636  11.367  39.149  1.00 17.32 ? 270 GLU   A N   1 
ATOM   2112 C  CA  . GLU   A 1 270 ? 18.722  12.297  39.439  1.00 19.63 ? 270 GLU   A CA  1 
ATOM   2113 C  C   . GLU   A 1 270 ? 19.435  12.719  38.152  1.00 18.73 ? 270 GLU   A C   1 
ATOM   2114 O  O   . GLU   A 1 270 ? 19.889  13.855  38.021  1.00 17.36 ? 270 GLU   A O   1 
ATOM   2115 C  CB  . GLU   A 1 270 ? 19.718  11.685  40.427  1.00 23.56 ? 270 GLU   A CB  1 
ATOM   2116 C  CG  . GLU   A 1 270 ? 19.158  11.573  41.833  1.00 29.82 ? 270 GLU   A CG  1 
ATOM   2117 C  CD  . GLU   A 1 270 ? 18.709  12.894  42.451  1.00 35.37 ? 270 GLU   A CD  1 
ATOM   2118 O  OE1 . GLU   A 1 270 ? 19.575  13.786  42.559  1.00 40.77 ? 270 GLU   A OE1 1 
ATOM   2119 O  OE2 . GLU   A 1 270 ? 17.486  13.042  42.794  1.00 36.63 ? 270 GLU   A OE2 1 
ATOM   2120 N  N   . LEU   A 1 271 ? 19.563  11.790  37.197  1.00 18.65 ? 271 LEU   A N   1 
ATOM   2121 C  CA  . LEU   A 1 271 ? 20.120  12.121  35.887  1.00 17.20 ? 271 LEU   A CA  1 
ATOM   2122 C  C   . LEU   A 1 271 ? 19.265  13.172  35.198  1.00 18.15 ? 271 LEU   A C   1 
ATOM   2123 O  O   . LEU   A 1 271 ? 19.813  14.081  34.575  1.00 18.57 ? 271 LEU   A O   1 
ATOM   2124 C  CB  . LEU   A 1 271 ? 20.240  10.854  35.033  1.00 16.02 ? 271 LEU   A CB  1 
ATOM   2125 C  CG  . LEU   A 1 271 ? 21.366  9.916   35.455  1.00 16.47 ? 271 LEU   A CG  1 
ATOM   2126 C  CD1 . LEU   A 1 271 ? 21.402  8.635   34.629  1.00 17.07 ? 271 LEU   A CD1 1 
ATOM   2127 C  CD2 . LEU   A 1 271 ? 22.702  10.621  35.366  1.00 16.53 ? 271 LEU   A CD2 1 
ATOM   2128 N  N   . LEU   A 1 272 ? 17.931  13.057  35.308  1.00 18.06 ? 272 LEU   A N   1 
ATOM   2129 C  CA  . LEU   A 1 272 ? 17.068  14.041  34.674  1.00 19.37 ? 272 LEU   A CA  1 
ATOM   2130 C  C   . LEU   A 1 272 ? 17.230  15.404  35.341  1.00 21.20 ? 272 LEU   A C   1 
ATOM   2131 O  O   . LEU   A 1 272 ? 17.255  16.419  34.653  1.00 21.60 ? 272 LEU   A O   1 
ATOM   2132 C  CB  . LEU   A 1 272 ? 15.605  13.599  34.734  1.00 19.54 ? 272 LEU   A CB  1 
ATOM   2133 C  CG  . LEU   A 1 272 ? 15.275  12.348  33.923  1.00 20.39 ? 272 LEU   A CG  1 
ATOM   2134 C  CD1 . LEU   A 1 272 ? 13.817  11.974  34.074  1.00 20.89 ? 272 LEU   A CD1 1 
ATOM   2135 C  CD2 . LEU   A 1 272 ? 15.610  12.559  32.464  1.00 19.89 ? 272 LEU   A CD2 1 
ATOM   2136 N  N   . GLN   A 1 273 ? 17.277  15.426  36.678  1.00 20.90 ? 273 GLN   A N   1 
ATOM   2137 C  CA  . GLN   A 1 273 ? 17.298  16.687  37.407  1.00 23.81 ? 273 GLN   A CA  1 
ATOM   2138 C  C   . GLN   A 1 273 ? 18.669  17.354  37.355  1.00 24.40 ? 273 GLN   A C   1 
ATOM   2139 O  O   . GLN   A 1 273 ? 18.728  18.576  37.331  1.00 25.17 ? 273 GLN   A O   1 
ATOM   2140 C  CB  . GLN   A 1 273 ? 16.862  16.474  38.853  1.00 21.91 ? 273 GLN   A CB  1 
ATOM   2141 C  CG  . GLN   A 1 273 ? 15.383  16.151  38.962  1.00 21.89 ? 273 GLN   A CG  1 
ATOM   2142 C  CD  . GLN   A 1 273 ? 14.964  15.728  40.351  1.00 23.71 ? 273 GLN   A CD  1 
ATOM   2143 O  OE1 . GLN   A 1 273 ? 15.777  15.401  41.211  1.00 25.60 ? 273 GLN   A OE1 1 
ATOM   2144 N  NE2 . GLN   A 1 273 ? 13.667  15.673  40.569  1.00 25.00 ? 273 GLN   A NE2 1 
ATOM   2145 N  N   . ASN   A 1 274 ? 19.748  16.573  37.301  1.00 26.31 ? 274 ASN   A N   1 
ATOM   2146 C  CA  . ASN   A 1 274 ? 21.093  17.114  37.433  1.00 29.15 ? 274 ASN   A CA  1 
ATOM   2147 C  C   . ASN   A 1 274 ? 21.872  17.075  36.124  1.00 31.72 ? 274 ASN   A C   1 
ATOM   2148 O  O   . ASN   A 1 274 ? 22.921  17.721  36.018  1.00 34.13 ? 274 ASN   A O   1 
ATOM   2149 C  CB  . ASN   A 1 274 ? 21.880  16.327  38.483  1.00 32.71 ? 274 ASN   A CB  1 
ATOM   2150 C  CG  . ASN   A 1 274 ? 21.242  16.414  39.854  1.00 37.12 ? 274 ASN   A CG  1 
ATOM   2151 O  OD1 . ASN   A 1 274 ? 20.533  17.373  40.158  1.00 41.65 ? 274 ASN   A OD1 1 
ATOM   2152 N  ND2 . ASN   A 1 274 ? 21.486  15.416  40.685  1.00 40.22 ? 274 ASN   A ND2 1 
ATOM   2153 N  N   . GLY   A 1 275 ? 21.395  16.305  35.138  1.00 30.71 ? 275 GLY   A N   1 
ATOM   2154 C  CA  . GLY   A 1 275 ? 22.148  16.123  33.906  1.00 29.50 ? 275 GLY   A CA  1 
ATOM   2155 C  C   . GLY   A 1 275 ? 23.324  15.176  34.105  1.00 28.70 ? 275 GLY   A C   1 
ATOM   2156 O  O   . GLY   A 1 275 ? 23.554  14.671  35.207  1.00 32.02 ? 275 GLY   A O   1 
ATOM   2157 N  N   . MET   A 1 276 ? 24.036  14.896  33.015  1.00 28.42 ? 276 MET   A N   1 
ATOM   2158 C  CA  . MET   A 1 276 ? 25.136  13.947  33.046  1.00 33.82 ? 276 MET   A CA  1 
ATOM   2159 C  C   . MET   A 1 276 ? 26.466  14.649  33.307  1.00 33.07 ? 276 MET   A C   1 
ATOM   2160 O  O   . MET   A 1 276 ? 27.460  13.966  33.548  1.00 30.85 ? 276 MET   A O   1 
ATOM   2161 C  CB  . MET   A 1 276 ? 25.197  13.159  31.734  1.00 35.05 ? 276 MET   A CB  1 
ATOM   2162 C  CG  . MET   A 1 276 ? 24.116  12.118  31.704  1.00 34.72 ? 276 MET   A CG  1 
ATOM   2163 S  SD  . MET   A 1 276 ? 23.851  11.455  30.062  1.00 40.54 ? 276 MET   A SD  1 
ATOM   2164 C  CE  . MET   A 1 276 ? 25.160  10.241  30.009  1.00 34.17 ? 276 MET   A CE  1 
ATOM   2165 N  N   . ASN   A 1 277 ? 26.441  15.993  33.285  1.00 39.88 ? 277 ASN   A N   1 
ATOM   2166 C  CA  . ASN   A 1 277 ? 27.558  16.852  33.652  1.00 45.41 ? 277 ASN   A CA  1 
ATOM   2167 C  C   . ASN   A 1 277 ? 28.825  16.367  32.947  1.00 41.18 ? 277 ASN   A C   1 
ATOM   2168 O  O   . ASN   A 1 277 ? 29.852  16.112  33.572  1.00 39.14 ? 277 ASN   A O   1 
ATOM   2169 C  CB  . ASN   A 1 277 ? 27.670  17.010  35.180  1.00 51.38 ? 277 ASN   A CB  1 
ATOM   2170 C  CG  . ASN   A 1 277 ? 28.190  15.791  35.924  1.00 57.08 ? 277 ASN   A CG  1 
ATOM   2171 O  OD1 . ASN   A 1 277 ? 27.572  14.728  35.926  1.00 63.95 ? 277 ASN   A OD1 1 
ATOM   2172 N  ND2 . ASN   A 1 277 ? 29.311  15.948  36.610  1.00 63.33 ? 277 ASN   A ND2 1 
ATOM   2173 N  N   . GLY   A 1 278 ? 28.730  16.199  31.626  1.00 41.85 ? 278 GLY   A N   1 
ATOM   2174 C  CA  . GLY   A 1 278 ? 29.908  15.967  30.807  1.00 39.40 ? 278 GLY   A CA  1 
ATOM   2175 C  C   . GLY   A 1 278 ? 30.285  14.489  30.722  1.00 43.08 ? 278 GLY   A C   1 
ATOM   2176 O  O   . GLY   A 1 278 ? 31.117  14.113  29.899  1.00 48.46 ? 278 GLY   A O   1 
ATOM   2177 N  N   . ARG   A 1 279 ? 29.655  13.640  31.542  1.00 36.33 ? 279 ARG   A N   1 
ATOM   2178 C  CA  . ARG   A 1 279 ? 30.042  12.242  31.598  1.00 32.51 ? 279 ARG   A CA  1 
ATOM   2179 C  C   . ARG   A 1 279 ? 29.307  11.450  30.524  1.00 26.94 ? 279 ARG   A C   1 
ATOM   2180 O  O   . ARG   A 1 279 ? 28.306  11.912  30.008  1.00 26.03 ? 279 ARG   A O   1 
ATOM   2181 C  CB  . ARG   A 1 279 ? 29.750  11.699  32.993  1.00 34.73 ? 279 ARG   A CB  1 
ATOM   2182 C  CG  . ARG   A 1 279 ? 30.454  12.478  34.093  1.00 36.66 ? 279 ARG   A CG  1 
ATOM   2183 C  CD  . ARG   A 1 279 ? 30.550  11.710  35.404  1.00 38.11 ? 279 ARG   A CD  1 
ATOM   2184 N  NE  . ARG   A 1 279 ? 31.382  10.507  35.276  1.00 38.82 ? 279 ARG   A NE  1 
ATOM   2185 C  CZ  . ARG   A 1 279 ? 31.907  9.815   36.286  1.00 39.93 ? 279 ARG   A CZ  1 
ATOM   2186 N  NH1 . ARG   A 1 279 ? 31.831  10.269  37.527  1.00 45.38 ? 279 ARG   A NH1 1 
ATOM   2187 N  NH2 . ARG   A 1 279 ? 32.541  8.679   36.045  1.00 38.88 ? 279 ARG   A NH2 1 
ATOM   2188 N  N   . THR   A 1 280 ? 29.791  10.238  30.222  1.00 24.12 ? 280 THR   A N   1 
ATOM   2189 C  CA  . THR   A 1 280 ? 29.116  9.350   29.289  1.00 23.19 ? 280 THR   A CA  1 
ATOM   2190 C  C   . THR   A 1 280 ? 28.656  8.067   29.987  1.00 20.75 ? 280 THR   A C   1 
ATOM   2191 O  O   . THR   A 1 280 ? 29.188  7.683   31.022  1.00 19.51 ? 280 THR   A O   1 
ATOM   2192 C  CB  . THR   A 1 280 ? 30.019  9.049   28.088  1.00 24.88 ? 280 THR   A CB  1 
ATOM   2193 O  OG1 . THR   A 1 280 ? 31.121  8.252   28.544  1.00 21.86 ? 280 THR   A OG1 1 
ATOM   2194 C  CG2 . THR   A 1 280 ? 30.496  10.319  27.407  1.00 25.31 ? 280 THR   A CG2 1 
ATOM   2195 N  N   . ILE   A 1 281 ? 27.669  7.393   29.389  1.00 19.51 ? 281 ILE   A N   1 
ATOM   2196 C  CA  . ILE   A 1 281 ? 27.271  6.056   29.792  1.00 18.84 ? 281 ILE   A CA  1 
ATOM   2197 C  C   . ILE   A 1 281 ? 27.317  5.194   28.545  1.00 20.11 ? 281 ILE   A C   1 
ATOM   2198 O  O   . ILE   A 1 281 ? 26.710  5.542   27.525  1.00 18.69 ? 281 ILE   A O   1 
ATOM   2199 C  CB  . ILE   A 1 281 ? 25.853  6.050   30.401  1.00 18.97 ? 281 ILE   A CB  1 
ATOM   2200 C  CG1 . ILE   A 1 281 ? 25.762  6.974   31.609  1.00 19.07 ? 281 ILE   A CG1 1 
ATOM   2201 C  CG2 . ILE   A 1 281 ? 25.396  4.636   30.722  1.00 18.49 ? 281 ILE   A CG2 1 
ATOM   2202 C  CD1 . ILE   A 1 281 ? 24.343  7.233   32.057  1.00 20.18 ? 281 ILE   A CD1 1 
ATOM   2203 N  N   . LEU   A 1 282 ? 28.023  4.063   28.648  1.00 21.16 ? 282 LEU   A N   1 
ATOM   2204 C  CA  . LEU   A 1 282 ? 28.274  3.192   27.508  1.00 21.36 ? 282 LEU   A CA  1 
ATOM   2205 C  C   . LEU   A 1 282 ? 28.694  4.018   26.291  1.00 23.68 ? 282 LEU   A C   1 
ATOM   2206 O  O   . LEU   A 1 282 ? 28.235  3.750   25.178  1.00 25.68 ? 282 LEU   A O   1 
ATOM   2207 C  CB  . LEU   A 1 282 ? 27.012  2.370   27.243  1.00 22.29 ? 282 LEU   A CB  1 
ATOM   2208 C  CG  . LEU   A 1 282 ? 26.728  1.279   28.276  1.00 21.74 ? 282 LEU   A CG  1 
ATOM   2209 C  CD1 . LEU   A 1 282 ? 25.353  0.682   28.051  1.00 21.74 ? 282 LEU   A CD1 1 
ATOM   2210 C  CD2 . LEU   A 1 282 ? 27.792  0.193   28.226  1.00 21.02 ? 282 LEU   A CD2 1 
ATOM   2211 N  N   . GLY   A 1 283 ? 29.542  5.031   26.526  1.00 22.66 ? 283 GLY   A N   1 
ATOM   2212 C  CA  . GLY   A 1 283 ? 30.140  5.831   25.468  1.00 26.07 ? 283 GLY   A CA  1 
ATOM   2213 C  C   . GLY   A 1 283 ? 29.206  6.901   24.903  1.00 25.43 ? 283 GLY   A C   1 
ATOM   2214 O  O   . GLY   A 1 283 ? 29.561  7.601   23.974  1.00 22.90 ? 283 GLY   A O   1 
ATOM   2215 N  N   . SER   A 1 284 ? 28.010  7.038   25.492  1.00 26.31 ? 284 SER   A N   1 
ATOM   2216 C  CA  . SER   A 1 284 ? 27.022  7.984   25.010  1.00 23.36 ? 284 SER   A CA  1 
ATOM   2217 C  C   . SER   A 1 284 ? 26.868  9.153   25.983  1.00 22.84 ? 284 SER   A C   1 
ATOM   2218 O  O   . SER   A 1 284 ? 26.823  8.979   27.198  1.00 22.16 ? 284 SER   A O   1 
ATOM   2219 C  CB  . SER   A 1 284 ? 25.720  7.277   24.790  1.00 22.86 ? 284 SER   A CB  1 
ATOM   2220 O  OG  . SER   A 1 284 ? 24.684  8.223   24.787  1.00 23.87 ? 284 SER   A OG  1 
ATOM   2221 N  N   . ALA   A 1 285 ? 26.742  10.347  25.413  1.00 22.22 ? 285 ALA   A N   1 
ATOM   2222 C  CA  . ALA   A 1 285 ? 26.537  11.578  26.158  1.00 23.41 ? 285 ALA   A CA  1 
ATOM   2223 C  C   . ALA   A 1 285 ? 25.045  11.823  26.398  1.00 24.57 ? 285 ALA   A C   1 
ATOM   2224 O  O   . ALA   A 1 285 ? 24.688  12.731  27.142  1.00 27.29 ? 285 ALA   A O   1 
ATOM   2225 C  CB  . ALA   A 1 285 ? 27.156  12.717  25.390  1.00 21.92 ? 285 ALA   A CB  1 
ATOM   2226 N  N   . LEU   A 1 286 ? 24.181  11.035  25.743  1.00 24.45 ? 286 LEU   A N   1 
ATOM   2227 C  CA  . LEU   A 1 286 ? 22.733  11.165  25.872  1.00 24.72 ? 286 LEU   A CA  1 
ATOM   2228 C  C   . LEU   A 1 286 ? 22.172  9.894   26.489  1.00 22.47 ? 286 LEU   A C   1 
ATOM   2229 O  O   . LEU   A 1 286 ? 22.792  8.846   26.377  1.00 20.77 ? 286 LEU   A O   1 
ATOM   2230 C  CB  . LEU   A 1 286 ? 22.107  11.352  24.482  1.00 26.93 ? 286 LEU   A CB  1 
ATOM   2231 C  CG  . LEU   A 1 286 ? 22.619  12.525  23.644  1.00 29.76 ? 286 LEU   A CG  1 
ATOM   2232 C  CD1 . LEU   A 1 286 ? 21.951  12.546  22.272  1.00 30.03 ? 286 LEU   A CD1 1 
ATOM   2233 C  CD2 . LEU   A 1 286 ? 22.393  13.850  24.369  1.00 31.01 ? 286 LEU   A CD2 1 
ATOM   2234 N  N   . LEU   A 1 287 ? 20.975  9.991   27.097  1.00 21.38 ? 287 LEU   A N   1 
ATOM   2235 C  CA  . LEU   A 1 287 ? 20.288  8.825   27.617  1.00 20.04 ? 287 LEU   A CA  1 
ATOM   2236 C  C   . LEU   A 1 287 ? 19.634  8.079   26.462  1.00 19.82 ? 287 LEU   A C   1 
ATOM   2237 O  O   . LEU   A 1 287 ? 18.791  8.622   25.774  1.00 22.44 ? 287 LEU   A O   1 
ATOM   2238 C  CB  . LEU   A 1 287 ? 19.258  9.256   28.656  1.00 20.51 ? 287 LEU   A CB  1 
ATOM   2239 C  CG  . LEU   A 1 287 ? 19.837  9.926   29.900  1.00 21.88 ? 287 LEU   A CG  1 
ATOM   2240 C  CD1 . LEU   A 1 287 ? 18.745  10.433  30.822  1.00 22.66 ? 287 LEU   A CD1 1 
ATOM   2241 C  CD2 . LEU   A 1 287 ? 20.743  8.981   30.652  1.00 21.80 ? 287 LEU   A CD2 1 
ATOM   2242 N  N   . GLU   A 1 288 ? 19.998  6.819   26.270  1.00 17.62 ? 288 GLU   A N   1 
ATOM   2243 C  CA  A GLU   A 1 288 ? 19.537  6.057   25.121  0.55 17.05 ? 288 GLU   A CA  1 
ATOM   2244 C  CA  B GLU   A 1 288 ? 19.530  6.069   25.114  0.45 17.49 ? 288 GLU   A CA  1 
ATOM   2245 C  C   . GLU   A 1 288 ? 18.211  5.368   25.460  1.00 16.68 ? 288 GLU   A C   1 
ATOM   2246 O  O   . GLU   A 1 288 ? 18.084  4.741   26.508  1.00 15.51 ? 288 GLU   A O   1 
ATOM   2247 C  CB  A GLU   A 1 288 ? 20.627  5.051   24.744  0.55 16.66 ? 288 GLU   A CB  1 
ATOM   2248 C  CB  B GLU   A 1 288 ? 20.597  5.065   24.669  0.45 17.81 ? 288 GLU   A CB  1 
ATOM   2249 C  CG  A GLU   A 1 288 ? 20.241  4.104   23.636  0.55 16.53 ? 288 GLU   A CG  1 
ATOM   2250 C  CG  B GLU   A 1 288 ? 21.974  5.670   24.455  0.45 18.32 ? 288 GLU   A CG  1 
ATOM   2251 C  CD  A GLU   A 1 288 ? 20.102  4.831   22.315  0.55 16.03 ? 288 GLU   A CD  1 
ATOM   2252 C  CD  B GLU   A 1 288 ? 22.291  6.124   23.041  0.45 18.83 ? 288 GLU   A CD  1 
ATOM   2253 O  OE1 A GLU   A 1 288 ? 21.103  5.488   21.899  0.55 14.47 ? 288 GLU   A OE1 1 
ATOM   2254 O  OE1 B GLU   A 1 288 ? 21.641  7.051   22.549  0.45 19.55 ? 288 GLU   A OE1 1 
ATOM   2255 O  OE2 A GLU   A 1 288 ? 19.026  4.708   21.716  0.55 14.12 ? 288 GLU   A OE2 1 
ATOM   2256 O  OE2 B GLU   A 1 288 ? 23.203  5.541   22.448  0.45 19.95 ? 288 GLU   A OE2 1 
ATOM   2257 N  N   . ASP   A 1 289 ? 17.233  5.453   24.544  1.00 14.63 ? 289 ASP   A N   1 
ATOM   2258 C  CA  . ASP   A 1 289 ? 15.914  4.886   24.762  1.00 14.52 ? 289 ASP   A CA  1 
ATOM   2259 C  C   . ASP   A 1 289 ? 15.471  3.922   23.652  1.00 14.82 ? 289 ASP   A C   1 
ATOM   2260 O  O   . ASP   A 1 289 ? 14.294  3.598   23.580  1.00 13.89 ? 289 ASP   A O   1 
ATOM   2261 C  CB  . ASP   A 1 289 ? 14.903  6.005   24.979  1.00 14.26 ? 289 ASP   A CB  1 
ATOM   2262 C  CG  . ASP   A 1 289 ? 14.460  6.759   23.735  1.00 15.36 ? 289 ASP   A CG  1 
ATOM   2263 O  OD1 . ASP   A 1 289 ? 15.171  6.725   22.699  1.00 14.42 ? 289 ASP   A OD1 1 
ATOM   2264 O  OD2 . ASP   A 1 289 ? 13.396  7.357   23.819  1.00 14.14 ? 289 ASP   A OD2 1 
ATOM   2265 N  N   . GLU   A 1 290 ? 16.403  3.406   22.829  1.00 14.96 ? 290 GLU   A N   1 
ATOM   2266 C  CA  . GLU   A 1 290 ? 16.016  2.512   21.745  1.00 15.74 ? 290 GLU   A CA  1 
ATOM   2267 C  C   . GLU   A 1 290 ? 16.595  1.122   21.964  1.00 15.57 ? 290 GLU   A C   1 
ATOM   2268 O  O   . GLU   A 1 290 ? 16.729  0.346   21.020  1.00 15.48 ? 290 GLU   A O   1 
ATOM   2269 C  CB  . GLU   A 1 290 ? 16.334  3.126   20.379  1.00 16.38 ? 290 GLU   A CB  1 
ATOM   2270 C  CG  . GLU   A 1 290 ? 15.503  4.385   20.094  1.00 17.78 ? 290 GLU   A CG  1 
ATOM   2271 C  CD  . GLU   A 1 290 ? 15.362  4.837   18.632  1.00 18.50 ? 290 GLU   A CD  1 
ATOM   2272 O  OE1 . GLU   A 1 290 ? 15.945  4.182   17.757  1.00 16.29 ? 290 GLU   A OE1 1 
ATOM   2273 O  OE2 . GLU   A 1 290 ? 14.687  5.873   18.380  1.00 17.90 ? 290 GLU   A OE2 1 
ATOM   2274 N  N   . PHE   A 1 291 ? 16.818  0.766   23.230  1.00 14.42 ? 291 PHE   A N   1 
ATOM   2275 C  CA  . PHE   A 1 291 ? 16.977  -0.623  23.620  1.00 14.82 ? 291 PHE   A CA  1 
ATOM   2276 C  C   . PHE   A 1 291 ? 15.863  -1.036  24.576  1.00 15.01 ? 291 PHE   A C   1 
ATOM   2277 O  O   . PHE   A 1 291 ? 15.730  -0.444  25.644  1.00 14.76 ? 291 PHE   A O   1 
ATOM   2278 C  CB  . PHE   A 1 291 ? 18.314  -0.793  24.346  1.00 17.43 ? 291 PHE   A CB  1 
ATOM   2279 C  CG  . PHE   A 1 291 ? 19.560  -0.543  23.550  1.00 18.62 ? 291 PHE   A CG  1 
ATOM   2280 C  CD1 . PHE   A 1 291 ? 20.031  -1.510  22.672  1.00 22.52 ? 291 PHE   A CD1 1 
ATOM   2281 C  CD2 . PHE   A 1 291 ? 20.287  0.625   23.696  1.00 20.80 ? 291 PHE   A CD2 1 
ATOM   2282 C  CE1 . PHE   A 1 291 ? 21.219  -1.330  21.974  1.00 21.92 ? 291 PHE   A CE1 1 
ATOM   2283 C  CE2 . PHE   A 1 291 ? 21.472  0.811   22.984  1.00 22.92 ? 291 PHE   A CE2 1 
ATOM   2284 C  CZ  . PHE   A 1 291 ? 21.924  -0.161  22.111  1.00 21.90 ? 291 PHE   A CZ  1 
ATOM   2285 N  N   . THR   A 1 292 ? 15.098  -2.072  24.231  1.00 14.40 ? 292 THR   A N   1 
ATOM   2286 C  CA  . THR   A 1 292 ? 14.093  -2.620  25.126  1.00 14.42 ? 292 THR   A CA  1 
ATOM   2287 C  C   . THR   A 1 292 ? 14.709  -3.581  26.155  1.00 14.45 ? 292 THR   A C   1 
ATOM   2288 O  O   . THR   A 1 292 ? 15.838  -4.074  26.002  1.00 12.92 ? 292 THR   A O   1 
ATOM   2289 C  CB  . THR   A 1 292 ? 13.018  -3.427  24.382  1.00 15.31 ? 292 THR   A CB  1 
ATOM   2290 O  OG1 . THR   A 1 292 ? 13.624  -4.663  23.954  1.00 15.71 ? 292 THR   A OG1 1 
ATOM   2291 C  CG2 . THR   A 1 292 ? 12.366  -2.662  23.251  1.00 14.60 ? 292 THR   A CG2 1 
ATOM   2292 N  N   . PRO   A 1 293 ? 13.970  -3.904  27.243  1.00 15.07 ? 293 PRO   A N   1 
ATOM   2293 C  CA  . PRO   A 1 293 ? 14.465  -4.870  28.221  1.00 15.48 ? 293 PRO   A CA  1 
ATOM   2294 C  C   . PRO   A 1 293 ? 14.855  -6.193  27.547  1.00 17.06 ? 293 PRO   A C   1 
ATOM   2295 O  O   . PRO   A 1 293 ? 15.896  -6.763  27.862  1.00 16.51 ? 293 PRO   A O   1 
ATOM   2296 C  CB  . PRO   A 1 293 ? 13.303  -5.011  29.214  1.00 14.80 ? 293 PRO   A CB  1 
ATOM   2297 C  CG  . PRO   A 1 293 ? 12.563  -3.703  29.114  1.00 15.57 ? 293 PRO   A CG  1 
ATOM   2298 C  CD  . PRO   A 1 293 ? 12.664  -3.336  27.631  1.00 15.02 ? 293 PRO   A CD  1 
ATOM   2299 N  N   . PHE   A 1 294 ? 14.016  -6.668  26.618  1.00 19.63 ? 294 PHE   A N   1 
ATOM   2300 C  CA  . PHE   A 1 294 ? 14.291  -7.898  25.867  1.00 21.16 ? 294 PHE   A CA  1 
ATOM   2301 C  C   . PHE   A 1 294 ? 15.597  -7.797  25.061  1.00 21.32 ? 294 PHE   A C   1 
ATOM   2302 O  O   . PHE   A 1 294 ? 16.400  -8.766  25.024  1.00 19.73 ? 294 PHE   A O   1 
ATOM   2303 C  CB  . PHE   A 1 294 ? 13.094  -8.250  24.977  1.00 23.87 ? 294 PHE   A CB  1 
ATOM   2304 C  CG  . PHE   A 1 294 ? 13.379  -9.337  23.975  1.00 33.00 ? 294 PHE   A CG  1 
ATOM   2305 C  CD1 . PHE   A 1 294 ? 14.068  -9.062  22.800  1.00 36.22 ? 294 PHE   A CD1 1 
ATOM   2306 C  CD2 . PHE   A 1 294 ? 13.001  -10.649 24.227  1.00 40.06 ? 294 PHE   A CD2 1 
ATOM   2307 C  CE1 . PHE   A 1 294 ? 14.352  -10.071 21.892  1.00 42.12 ? 294 PHE   A CE1 1 
ATOM   2308 C  CE2 . PHE   A 1 294 ? 13.289  -11.656 23.317  1.00 42.04 ? 294 PHE   A CE2 1 
ATOM   2309 C  CZ  . PHE   A 1 294 ? 13.958  -11.364 22.151  1.00 41.04 ? 294 PHE   A CZ  1 
ATOM   2310 N  N   . ASP   A 1 295 ? 15.810  -6.641  24.398  1.00 18.58 ? 295 ASP   A N   1 
ATOM   2311 C  CA  . ASP   A 1 295 ? 17.020  -6.397  23.634  1.00 18.59 ? 295 ASP   A CA  1 
ATOM   2312 C  C   . ASP   A 1 295 ? 18.250  -6.530  24.532  1.00 19.10 ? 295 ASP   A C   1 
ATOM   2313 O  O   . ASP   A 1 295 ? 19.284  -7.056  24.124  1.00 16.22 ? 295 ASP   A O   1 
ATOM   2314 C  CB  . ASP   A 1 295 ? 17.030  -4.989  23.036  1.00 20.02 ? 295 ASP   A CB  1 
ATOM   2315 C  CG  . ASP   A 1 295 ? 15.997  -4.761  21.935  1.00 21.62 ? 295 ASP   A CG  1 
ATOM   2316 O  OD1 . ASP   A 1 295 ? 15.515  -5.780  21.362  1.00 20.17 ? 295 ASP   A OD1 1 
ATOM   2317 O  OD2 . ASP   A 1 295 ? 15.643  -3.552  21.691  1.00 19.42 ? 295 ASP   A OD2 1 
ATOM   2318 N  N   . VAL   A 1 296 ? 18.154  -5.972  25.746  1.00 17.88 ? 296 VAL   A N   1 
ATOM   2319 C  CA  . VAL   A 1 296 ? 19.296  -5.956  26.645  1.00 19.01 ? 296 VAL   A CA  1 
ATOM   2320 C  C   . VAL   A 1 296 ? 19.595  -7.401  27.072  1.00 20.05 ? 296 VAL   A C   1 
ATOM   2321 O  O   . VAL   A 1 296 ? 20.748  -7.823  26.988  1.00 21.36 ? 296 VAL   A O   1 
ATOM   2322 C  CB  . VAL   A 1 296 ? 19.078  -4.984  27.829  1.00 18.16 ? 296 VAL   A CB  1 
ATOM   2323 C  CG1 . VAL   A 1 296 ? 20.132  -5.141  28.915  1.00 17.79 ? 296 VAL   A CG1 1 
ATOM   2324 C  CG2 . VAL   A 1 296 ? 18.999  -3.530  27.375  1.00 16.83 ? 296 VAL   A CG2 1 
ATOM   2325 N  N   . VAL   A 1 297 ? 18.568  -8.152  27.501  1.00 21.82 ? 297 VAL   A N   1 
ATOM   2326 C  CA  . VAL   A 1 297 ? 18.750  -9.529  27.948  1.00 25.52 ? 297 VAL   A CA  1 
ATOM   2327 C  C   . VAL   A 1 297 ? 19.346  -10.407 26.841  1.00 28.19 ? 297 VAL   A C   1 
ATOM   2328 O  O   . VAL   A 1 297 ? 20.196  -11.245 27.120  1.00 29.93 ? 297 VAL   A O   1 
ATOM   2329 C  CB  . VAL   A 1 297 ? 17.438  -10.135 28.482  1.00 26.83 ? 297 VAL   A CB  1 
ATOM   2330 C  CG1 . VAL   A 1 297 ? 17.498  -11.659 28.570  1.00 27.39 ? 297 VAL   A CG1 1 
ATOM   2331 C  CG2 . VAL   A 1 297 ? 17.089  -9.545  29.837  1.00 28.72 ? 297 VAL   A CG2 1 
ATOM   2332 N  N   . ARG   A 1 298 ? 18.920  -10.211 25.591  1.00 30.95 ? 298 ARG   A N   1 
ATOM   2333 C  CA  . ARG   A 1 298 ? 19.382  -11.046 24.494  1.00 32.63 ? 298 ARG   A CA  1 
ATOM   2334 C  C   . ARG   A 1 298 ? 20.848  -10.717 24.204  1.00 29.96 ? 298 ARG   A C   1 
ATOM   2335 O  O   . ARG   A 1 298 ? 21.637  -11.606 23.917  1.00 34.26 ? 298 ARG   A O   1 
ATOM   2336 C  CB  . ARG   A 1 298 ? 18.437  -10.969 23.280  1.00 36.19 ? 298 ARG   A CB  1 
ATOM   2337 C  CG  . ARG   A 1 298 ? 18.830  -9.988  22.181  1.00 42.28 ? 298 ARG   A CG  1 
ATOM   2338 C  CD  . ARG   A 1 298 ? 18.034  -10.231 20.892  1.00 45.42 ? 298 ARG   A CD  1 
ATOM   2339 N  NE  . ARG   A 1 298 ? 18.625  -9.610  19.702  1.00 43.99 ? 298 ARG   A NE  1 
ATOM   2340 C  CZ  . ARG   A 1 298 ? 19.393  -10.238 18.801  1.00 43.14 ? 298 ARG   A CZ  1 
ATOM   2341 N  NH1 . ARG   A 1 298 ? 19.715  -11.514 18.959  1.00 49.30 ? 298 ARG   A NH1 1 
ATOM   2342 N  NH2 . ARG   A 1 298 ? 19.856  -9.587  17.744  1.00 32.67 ? 298 ARG   A NH2 1 
ATOM   2343 N  N   . GLN   A 1 299 ? 21.248  -9.454  24.315  1.00 28.26 ? 299 GLN   A N   1 
ATOM   2344 C  CA  . GLN   A 1 299 ? 22.620  -9.083  24.004  1.00 26.46 ? 299 GLN   A CA  1 
ATOM   2345 C  C   . GLN   A 1 299 ? 23.564  -9.335  25.186  1.00 29.93 ? 299 GLN   A C   1 
ATOM   2346 O  O   . GLN   A 1 299 ? 24.766  -9.496  24.985  1.00 30.02 ? 299 GLN   A O   1 
ATOM   2347 C  CB  . GLN   A 1 299 ? 22.678  -7.625  23.556  1.00 25.51 ? 299 GLN   A CB  1 
ATOM   2348 C  CG  . GLN   A 1 299 ? 24.079  -7.148  23.240  1.00 25.83 ? 299 GLN   A CG  1 
ATOM   2349 C  CD  . GLN   A 1 299 ? 24.162  -5.824  22.523  1.00 27.79 ? 299 GLN   A CD  1 
ATOM   2350 O  OE1 . GLN   A 1 299 ? 25.255  -5.352  22.227  1.00 26.94 ? 299 GLN   A OE1 1 
ATOM   2351 N  NE2 . GLN   A 1 299 ? 23.026  -5.216  22.210  1.00 26.98 ? 299 GLN   A NE2 1 
ATOM   2352 N  N   . CYS   A 1 300 ? 23.042  -9.375  26.422  1.00 30.53 ? 300 CYS   A N   1 
ATOM   2353 C  CA  . CYS   A 1 300 ? 23.894  -9.504  27.599  1.00 29.63 ? 300 CYS   A CA  1 
ATOM   2354 C  C   . CYS   A 1 300 ? 23.967  -10.956 28.089  1.00 32.76 ? 300 CYS   A C   1 
ATOM   2355 O  O   . CYS   A 1 300 ? 24.906  -11.322 28.790  1.00 36.43 ? 300 CYS   A O   1 
ATOM   2356 C  CB  . CYS   A 1 300 ? 23.417  -8.594  28.724  1.00 27.45 ? 300 CYS   A CB  1 
ATOM   2357 S  SG  . CYS   A 1 300 ? 23.804  -6.843  28.449  1.00 31.50 ? 300 CYS   A SG  1 
ATOM   2358 N  N   . SER   A 1 301 ? 23.006  -11.797 27.700  1.00 35.31 ? 301 SER   A N   1 
ATOM   2359 C  CA  . SER   A 1 301 ? 22.891  -13.140 28.253  1.00 37.05 ? 301 SER   A CA  1 
ATOM   2360 C  C   . SER   A 1 301 ? 22.761  -14.173 27.125  1.00 37.19 ? 301 SER   A C   1 
ATOM   2361 O  O   . SER   A 1 301 ? 22.310  -13.766 26.030  1.00 41.79 ? 301 SER   A O   1 
ATOM   2362 C  CB  . SER   A 1 301 ? 21.719  -13.225 29.222  1.00 38.30 ? 301 SER   A CB  1 
ATOM   2363 O  OG  . SER   A 1 301 ? 21.727  -12.137 30.142  1.00 45.59 ? 301 SER   A OG  1 
ATOM   2364 N  N   . SER   B 2 1   ? 21.480  11.204  15.994  1.00 71.99 ? 1   SER   B N   1 
ATOM   2365 C  CA  . SER   B 2 1   ? 20.850  12.320  15.231  1.00 68.72 ? 1   SER   B CA  1 
ATOM   2366 C  C   . SER   B 2 1   ? 21.449  12.419  13.822  1.00 67.17 ? 1   SER   B C   1 
ATOM   2367 O  O   . SER   B 2 1   ? 22.542  12.965  13.642  1.00 70.54 ? 1   SER   B O   1 
ATOM   2368 C  CB  . SER   B 2 1   ? 20.978  13.622  15.990  1.00 62.07 ? 1   SER   B CB  1 
ATOM   2369 O  OG  . SER   B 2 1   ? 20.521  14.713  15.205  1.00 57.20 ? 1   SER   B OG  1 
ATOM   2370 N  N   . GLY   B 2 2   ? 20.725  11.889  12.824  1.00 55.66 ? 2   GLY   B N   1 
ATOM   2371 C  CA  . GLY   B 2 2   ? 21.142  11.986  11.434  1.00 54.84 ? 2   GLY   B CA  1 
ATOM   2372 C  C   . GLY   B 2 2   ? 21.918  10.752  10.967  1.00 52.96 ? 2   GLY   B C   1 
ATOM   2373 O  O   . GLY   B 2 2   ? 21.498  10.067  10.036  1.00 54.10 ? 2   GLY   B O   1 
ATOM   2374 N  N   . PHE   B 2 3   ? 23.068  10.487  11.600  1.00 45.35 ? 3   PHE   B N   1 
ATOM   2375 C  CA  . PHE   B 2 3   ? 23.895  9.351   11.224  1.00 40.12 ? 3   PHE   B CA  1 
ATOM   2376 C  C   . PHE   B 2 3   ? 23.748  8.256   12.267  1.00 36.36 ? 3   PHE   B C   1 
ATOM   2377 O  O   . PHE   B 2 3   ? 23.665  8.548   13.453  1.00 40.31 ? 3   PHE   B O   1 
ATOM   2378 C  CB  . PHE   B 2 3   ? 25.363  9.749   11.069  1.00 36.51 ? 3   PHE   B CB  1 
ATOM   2379 C  CG  . PHE   B 2 3   ? 25.583  10.768  9.988   1.00 34.76 ? 3   PHE   B CG  1 
ATOM   2380 C  CD1 . PHE   B 2 3   ? 25.334  12.113  10.226  1.00 33.46 ? 3   PHE   B CD1 1 
ATOM   2381 C  CD2 . PHE   B 2 3   ? 25.902  10.367  8.700   1.00 31.10 ? 3   PHE   B CD2 1 
ATOM   2382 C  CE1 . PHE   B 2 3   ? 25.482  13.044  9.213   1.00 31.72 ? 3   PHE   B CE1 1 
ATOM   2383 C  CE2 . PHE   B 2 3   ? 26.024  11.295  7.688   1.00 28.17 ? 3   PHE   B CE2 1 
ATOM   2384 C  CZ  . PHE   B 2 3   ? 25.827  12.632  7.947   1.00 29.01 ? 3   PHE   B CZ  1 
ATOM   2385 N  N   . ARG   B 2 4   ? 23.727  7.003   11.804  1.00 32.70 ? 4   ARG   B N   1 
ATOM   2386 C  CA  . ARG   B 2 4   ? 23.782  5.857   12.700  1.00 31.86 ? 4   ARG   B CA  1 
ATOM   2387 C  C   . ARG   B 2 4   ? 24.731  4.803   12.142  1.00 24.88 ? 4   ARG   B C   1 
ATOM   2388 O  O   . ARG   B 2 4   ? 25.049  4.799   10.965  1.00 21.92 ? 4   ARG   B O   1 
ATOM   2389 C  CB  . ARG   B 2 4   ? 22.387  5.263   12.917  1.00 33.97 ? 4   ARG   B CB  1 
ATOM   2390 C  CG  . ARG   B 2 4   ? 21.622  4.987   11.638  1.00 34.55 ? 4   ARG   B CG  1 
ATOM   2391 C  CD  . ARG   B 2 4   ? 20.366  4.180   11.865  1.00 37.88 ? 4   ARG   B CD  1 
ATOM   2392 N  NE  . ARG   B 2 4   ? 19.412  4.770   12.799  1.00 41.24 ? 4   ARG   B NE  1 
ATOM   2393 C  CZ  . ARG   B 2 4   ? 19.013  4.192   13.933  1.00 44.28 ? 4   ARG   B CZ  1 
ATOM   2394 N  NH1 . ARG   B 2 4   ? 19.677  3.150   14.423  1.00 49.10 ? 4   ARG   B NH1 1 
ATOM   2395 N  NH2 . ARG   B 2 4   ? 17.986  4.690   14.609  1.00 43.93 ? 4   ARG   B NH2 1 
ATOM   2396 N  N   . LYS   B 2 5   ? 25.156  3.897   13.013  1.00 24.73 ? 5   LYS   B N   1 
ATOM   2397 C  CA  . LYS   B 2 5   ? 25.957  2.761   12.607  1.00 27.51 ? 5   LYS   B CA  1 
ATOM   2398 C  C   . LYS   B 2 5   ? 25.054  1.831   11.790  1.00 26.61 ? 5   LYS   B C   1 
ATOM   2399 O  O   . LYS   B 2 5   ? 24.121  1.260   12.325  1.00 29.41 ? 5   LYS   B O   1 
ATOM   2400 C  CB  . LYS   B 2 5   ? 26.551  2.076   13.843  1.00 29.01 ? 5   LYS   B CB  1 
ATOM   2401 C  CG  . LYS   B 2 5   ? 27.329  2.998   14.780  1.00 30.00 ? 5   LYS   B CG  1 
ATOM   2402 C  CD  . LYS   B 2 5   ? 28.529  3.625   14.126  1.00 32.47 ? 5   LYS   B CD  1 
ATOM   2403 C  CE  . LYS   B 2 5   ? 29.218  4.681   14.965  1.00 31.48 ? 5   LYS   B CE  1 
ATOM   2404 N  NZ  . LYS   B 2 5   ? 29.803  4.131   16.208  1.00 31.98 ? 5   LYS   B NZ  1 
ATOM   2405 N  N   . MET   B 2 6   ? 25.321  1.715   10.492  1.00 24.64 ? 6   MET   B N   1 
ATOM   2406 C  CA  . MET   B 2 6   ? 24.579  0.823   9.617   1.00 25.07 ? 6   MET   B CA  1 
ATOM   2407 C  C   . MET   B 2 6   ? 25.463  -0.337  9.167   1.00 20.44 ? 6   MET   B C   1 
ATOM   2408 O  O   . MET   B 2 6   ? 26.573  -0.101  8.682   1.00 19.69 ? 6   MET   B O   1 
ATOM   2409 C  CB  . MET   B 2 6   ? 24.115  1.574   8.373   1.00 29.04 ? 6   MET   B CB  1 
ATOM   2410 C  CG  . MET   B 2 6   ? 22.797  2.253   8.574   1.00 35.52 ? 6   MET   B CG  1 
ATOM   2411 S  SD  . MET   B 2 6   ? 22.394  3.311   7.179   1.00 43.00 ? 6   MET   B SD  1 
ATOM   2412 C  CE  . MET   B 2 6   ? 22.034  2.044   5.975   1.00 36.06 ? 6   MET   B CE  1 
ATOM   2413 N  N   . ALA   B 2 7   ? 24.939  -1.571  9.287   1.00 16.59 ? 7   ALA   B N   1 
ATOM   2414 C  CA  . ALA   B 2 7   ? 25.632  -2.761  8.820   1.00 14.71 ? 7   ALA   B CA  1 
ATOM   2415 C  C   . ALA   B 2 7   ? 25.233  -3.078  7.379   1.00 13.61 ? 7   ALA   B C   1 
ATOM   2416 O  O   . ALA   B 2 7   ? 24.136  -2.717  6.928   1.00 13.61 ? 7   ALA   B O   1 
ATOM   2417 C  CB  . ALA   B 2 7   ? 25.304  -3.929  9.714   1.00 13.90 ? 7   ALA   B CB  1 
ATOM   2418 N  N   . PHE   B 2 8   ? 26.076  -3.854  6.705   1.00 12.24 ? 8   PHE   B N   1 
ATOM   2419 C  CA  . PHE   B 2 8   ? 25.694  -4.462  5.450   1.00 12.59 ? 8   PHE   B CA  1 
ATOM   2420 C  C   . PHE   B 2 8   ? 24.663  -5.556  5.670   1.00 12.12 ? 8   PHE   B C   1 
ATOM   2421 O  O   . PHE   B 2 8   ? 24.643  -6.208  6.708   1.00 11.14 ? 8   PHE   B O   1 
ATOM   2422 C  CB  . PHE   B 2 8   ? 26.906  -5.048  4.748   1.00 13.57 ? 8   PHE   B CB  1 
ATOM   2423 C  CG  . PHE   B 2 8   ? 27.725  -3.969  4.113   1.00 14.87 ? 8   PHE   B CG  1 
ATOM   2424 C  CD1 . PHE   B 2 8   ? 27.285  -3.358  2.953   1.00 15.51 ? 8   PHE   B CD1 1 
ATOM   2425 C  CD2 . PHE   B 2 8   ? 28.879  -3.519  4.720   1.00 15.46 ? 8   PHE   B CD2 1 
ATOM   2426 C  CE1 . PHE   B 2 8   ? 28.019  -2.322  2.388   1.00 17.87 ? 8   PHE   B CE1 1 
ATOM   2427 C  CE2 . PHE   B 2 8   ? 29.598  -2.473  4.165   1.00 16.71 ? 8   PHE   B CE2 1 
ATOM   2428 C  CZ  . PHE   B 2 8   ? 29.192  -1.904  2.983   1.00 16.78 ? 8   PHE   B CZ  1 
ATOM   2429 N  N   . PRO   B 2 9   ? 23.795  -5.833  4.670   1.00 12.08 ? 9   PRO   B N   1 
ATOM   2430 C  CA  . PRO   B 2 9   ? 22.877  -6.954  4.785   1.00 12.35 ? 9   PRO   B CA  1 
ATOM   2431 C  C   . PRO   B 2 9   ? 23.724  -8.222  4.968   1.00 11.95 ? 9   PRO   B C   1 
ATOM   2432 O  O   . PRO   B 2 9   ? 24.740  -8.389  4.275   1.00 10.91 ? 9   PRO   B O   1 
ATOM   2433 C  CB  . PRO   B 2 9   ? 22.095  -6.919  3.463   1.00 12.80 ? 9   PRO   B CB  1 
ATOM   2434 C  CG  . PRO   B 2 9   ? 22.266  -5.486  2.959   1.00 13.05 ? 9   PRO   B CG  1 
ATOM   2435 C  CD  . PRO   B 2 9   ? 23.661  -5.113  3.403   1.00 12.90 ? 9   PRO   B CD  1 
ATOM   2436 N  N   . SER   B 2 10  ? 23.300  -9.093  5.900   1.00 10.49 ? 10  SER   B N   1 
ATOM   2437 C  CA  . SER   B 2 10  ? 24.145  -10.196 6.345   1.00 10.62 ? 10  SER   B CA  1 
ATOM   2438 C  C   . SER   B 2 10  ? 23.887  -11.535 5.627   1.00 9.82  ? 10  SER   B C   1 
ATOM   2439 O  O   . SER   B 2 10  ? 24.573  -12.512 5.910   1.00 9.54  ? 10  SER   B O   1 
ATOM   2440 C  CB  . SER   B 2 10  ? 24.013  -10.344 7.824   1.00 10.63 ? 10  SER   B CB  1 
ATOM   2441 O  OG  . SER   B 2 10  ? 22.671  -10.615 8.186   1.00 9.12  ? 10  SER   B OG  1 
ATOM   2442 N  N   . GLY   B 2 11  ? 22.912  -11.597 4.722   1.00 9.43  ? 11  GLY   B N   1 
ATOM   2443 C  CA  . GLY   B 2 11  ? 22.478  -12.850 4.115   1.00 10.24 ? 11  GLY   B CA  1 
ATOM   2444 C  C   . GLY   B 2 11  ? 23.599  -13.651 3.438   1.00 11.45 ? 11  GLY   B C   1 
ATOM   2445 O  O   . GLY   B 2 11  ? 23.736  -14.876 3.639   1.00 10.50 ? 11  GLY   B O   1 
ATOM   2446 N  N   . LYS   B 2 12  ? 24.447  -12.942 2.680   1.00 12.12 ? 12  LYS   B N   1 
ATOM   2447 C  CA  . LYS   B 2 12  ? 25.527  -13.594 1.969   1.00 13.83 ? 12  LYS   B CA  1 
ATOM   2448 C  C   . LYS   B 2 12  ? 26.500  -14.261 2.935   1.00 12.90 ? 12  LYS   B C   1 
ATOM   2449 O  O   . LYS   B 2 12  ? 27.179  -15.208 2.551   1.00 13.85 ? 12  LYS   B O   1 
ATOM   2450 C  CB  . LYS   B 2 12  ? 26.262  -12.602 1.076   1.00 15.47 ? 12  LYS   B CB  1 
ATOM   2451 C  CG  . LYS   B 2 12  ? 25.534  -12.221 -0.202  1.00 17.53 ? 12  LYS   B CG  1 
ATOM   2452 C  CD  . LYS   B 2 12  ? 26.387  -11.250 -1.016  1.00 20.03 ? 12  LYS   B CD  1 
ATOM   2453 C  CE  . LYS   B 2 12  ? 25.850  -10.994 -2.405  1.00 23.91 ? 12  LYS   B CE  1 
ATOM   2454 N  NZ  . LYS   B 2 12  ? 24.589  -10.226 -2.356  1.00 28.17 ? 12  LYS   B NZ  1 
ATOM   2455 N  N   . VAL   B 2 13  ? 26.597  -13.744 4.162   1.00 11.18 ? 13  VAL   B N   1 
ATOM   2456 C  CA  . VAL   B 2 13  ? 27.497  -14.341 5.134   1.00 11.61 ? 13  VAL   B CA  1 
ATOM   2457 C  C   . VAL   B 2 13  ? 26.769  -15.410 5.963   1.00 10.86 ? 13  VAL   B C   1 
ATOM   2458 O  O   . VAL   B 2 13  ? 27.374  -16.422 6.309   1.00 10.06 ? 13  VAL   B O   1 
ATOM   2459 C  CB  . VAL   B 2 13  ? 28.146  -13.264 6.016   1.00 11.56 ? 13  VAL   B CB  1 
ATOM   2460 C  CG1 . VAL   B 2 13  ? 28.989  -13.871 7.123   1.00 12.15 ? 13  VAL   B CG1 1 
ATOM   2461 C  CG2 . VAL   B 2 13  ? 28.973  -12.308 5.174   1.00 11.93 ? 13  VAL   B CG2 1 
ATOM   2462 N  N   . GLU   B 2 14  ? 25.481  -15.195 6.286   1.00 9.95  ? 14  GLU   B N   1 
ATOM   2463 C  CA  . GLU   B 2 14  ? 24.691  -16.167 7.033   1.00 9.87  ? 14  GLU   B CA  1 
ATOM   2464 C  C   . GLU   B 2 14  ? 24.756  -17.563 6.406   1.00 9.66  ? 14  GLU   B C   1 
ATOM   2465 O  O   . GLU   B 2 14  ? 24.914  -18.557 7.116   1.00 8.81  ? 14  GLU   B O   1 
ATOM   2466 C  CB  . GLU   B 2 14  ? 23.213  -15.756 7.104   1.00 10.27 ? 14  GLU   B CB  1 
ATOM   2467 C  CG  . GLU   B 2 14  ? 22.933  -14.592 8.048   1.00 10.49 ? 14  GLU   B CG  1 
ATOM   2468 C  CD  . GLU   B 2 14  ? 21.537  -14.008 7.881   1.00 11.81 ? 14  GLU   B CD  1 
ATOM   2469 O  OE1 . GLU   B 2 14  ? 20.572  -14.788 7.967   1.00 11.60 ? 14  GLU   B OE1 1 
ATOM   2470 O  OE2 . GLU   B 2 14  ? 21.418  -12.766 7.634   1.00 11.70 ? 14  GLU   B OE2 1 
ATOM   2471 N  N   . GLY   B 2 15  ? 24.696  -17.623 5.075   1.00 9.67  ? 15  GLY   B N   1 
ATOM   2472 C  CA  . GLY   B 2 15  ? 24.705  -18.891 4.366   1.00 10.75 ? 15  GLY   B CA  1 
ATOM   2473 C  C   . GLY   B 2 15  ? 26.054  -19.628 4.401   1.00 10.88 ? 15  GLY   B C   1 
ATOM   2474 O  O   . GLY   B 2 15  ? 26.153  -20.726 3.868   1.00 11.68 ? 15  GLY   B O   1 
ATOM   2475 N  N   . CYS   B 2 16  ? 27.091  -19.004 4.982   1.00 10.74 ? 16  CYS   B N   1 
ATOM   2476 C  CA  . CYS   B 2 16  ? 28.419  -19.600 5.077   1.00 11.05 ? 16  CYS   B CA  1 
ATOM   2477 C  C   . CYS   B 2 16  ? 28.779  -20.004 6.510   1.00 11.24 ? 16  CYS   B C   1 
ATOM   2478 O  O   . CYS   B 2 16  ? 29.876  -20.520 6.724   1.00 10.34 ? 16  CYS   B O   1 
ATOM   2479 C  CB  . CYS   B 2 16  ? 29.469  -18.612 4.607   1.00 11.76 ? 16  CYS   B CB  1 
ATOM   2480 S  SG  . CYS   B 2 16  ? 29.217  -18.076 2.899   1.00 13.88 ? 16  CYS   B SG  1 
ATOM   2481 N  N   . MET   B 2 17  ? 27.895  -19.764 7.490   1.00 10.39 ? 17  MET   B N   1 
ATOM   2482 C  CA  . MET   B 2 17  ? 28.279  -19.992 8.884   1.00 11.18 ? 17  MET   B CA  1 
ATOM   2483 C  C   . MET   B 2 17  ? 28.022  -21.449 9.242   1.00 11.80 ? 17  MET   B C   1 
ATOM   2484 O  O   . MET   B 2 17  ? 26.969  -21.977 8.921   1.00 10.96 ? 17  MET   B O   1 
ATOM   2485 C  CB  . MET   B 2 17  ? 27.524  -19.110 9.877   1.00 11.98 ? 17  MET   B CB  1 
ATOM   2486 C  CG  . MET   B 2 17  ? 27.823  -17.645 9.706   1.00 12.69 ? 17  MET   B CG  1 
ATOM   2487 S  SD  . MET   B 2 17  ? 29.550  -17.146 9.611   1.00 14.25 ? 17  MET   B SD  1 
ATOM   2488 C  CE  . MET   B 2 17  ? 30.205  -17.871 11.111  1.00 15.71 ? 17  MET   B CE  1 
ATOM   2489 N  N   . VAL   B 2 18  ? 29.026  -22.079 9.856   1.00 10.64 ? 18  VAL   B N   1 
ATOM   2490 C  CA  . VAL   B 2 18  ? 28.908  -23.448 10.311  1.00 11.14 ? 18  VAL   B CA  1 
ATOM   2491 C  C   . VAL   B 2 18  ? 29.442  -23.507 11.738  1.00 11.19 ? 18  VAL   B C   1 
ATOM   2492 O  O   . VAL   B 2 18  ? 29.959  -22.535 12.266  1.00 10.43 ? 18  VAL   B O   1 
ATOM   2493 C  CB  . VAL   B 2 18  ? 29.652  -24.427 9.375   1.00 10.62 ? 18  VAL   B CB  1 
ATOM   2494 C  CG1 . VAL   B 2 18  ? 29.034  -24.450 7.984   1.00 10.73 ? 18  VAL   B CG1 1 
ATOM   2495 C  CG2 . VAL   B 2 18  ? 31.146  -24.121 9.309   1.00 10.80 ? 18  VAL   B CG2 1 
ATOM   2496 N  N   . GLN   B 2 19  ? 29.318  -24.685 12.337  1.00 11.63 ? 19  GLN   B N   1 
ATOM   2497 C  CA  . GLN   B 2 19  ? 29.819  -24.963 13.661  1.00 12.33 ? 19  GLN   B CA  1 
ATOM   2498 C  C   . GLN   B 2 19  ? 30.953  -25.972 13.479  1.00 11.57 ? 19  GLN   B C   1 
ATOM   2499 O  O   . GLN   B 2 19  ? 30.802  -26.912 12.703  1.00 10.95 ? 19  GLN   B O   1 
ATOM   2500 C  CB  . GLN   B 2 19  ? 28.659  -25.521 14.496  1.00 15.26 ? 19  GLN   B CB  1 
ATOM   2501 C  CG  . GLN   B 2 19  ? 28.999  -25.729 15.960  1.00 19.70 ? 19  GLN   B CG  1 
ATOM   2502 C  CD  . GLN   B 2 19  ? 27.822  -26.260 16.753  1.00 21.63 ? 19  GLN   B CD  1 
ATOM   2503 O  OE1 . GLN   B 2 19  ? 26.807  -26.693 16.212  1.00 22.38 ? 19  GLN   B OE1 1 
ATOM   2504 N  NE2 . GLN   B 2 19  ? 27.994  -26.265 18.058  1.00 25.91 ? 19  GLN   B NE2 1 
ATOM   2505 N  N   . VAL   B 2 20  ? 32.038  -25.797 14.236  1.00 10.78 ? 20  VAL   B N   1 
ATOM   2506 C  CA  . VAL   B 2 20  ? 33.174  -26.689 14.241  1.00 11.19 ? 20  VAL   B CA  1 
ATOM   2507 C  C   . VAL   B 2 20  ? 33.446  -27.114 15.686  1.00 12.36 ? 20  VAL   B C   1 
ATOM   2508 O  O   . VAL   B 2 20  ? 33.573  -26.272 16.591  1.00 11.07 ? 20  VAL   B O   1 
ATOM   2509 C  CB  . VAL   B 2 20  ? 34.424  -26.062 13.595  1.00 12.06 ? 20  VAL   B CB  1 
ATOM   2510 C  CG1 . VAL   B 2 20  ? 35.572  -27.057 13.503  1.00 13.44 ? 20  VAL   B CG1 1 
ATOM   2511 C  CG2 . VAL   B 2 20  ? 34.132  -25.466 12.222  1.00 12.16 ? 20  VAL   B CG2 1 
ATOM   2512 N  N   . THR   B 2 21  ? 33.504  -28.446 15.877  1.00 12.24 ? 21  THR   B N   1 
ATOM   2513 C  CA  . THR   B 2 21  ? 33.720  -29.053 17.171  1.00 12.79 ? 21  THR   B CA  1 
ATOM   2514 C  C   . THR   B 2 21  ? 34.897  -30.033 17.081  1.00 13.56 ? 21  THR   B C   1 
ATOM   2515 O  O   . THR   B 2 21  ? 35.024  -30.790 16.130  1.00 12.51 ? 21  THR   B O   1 
ATOM   2516 C  CB  . THR   B 2 21  ? 32.445  -29.725 17.694  1.00 13.39 ? 21  THR   B CB  1 
ATOM   2517 O  OG1 . THR   B 2 21  ? 31.361  -28.797 17.717  1.00 13.45 ? 21  THR   B OG1 1 
ATOM   2518 C  CG2 . THR   B 2 21  ? 32.608  -30.297 19.079  1.00 13.53 ? 21  THR   B CG2 1 
ATOM   2519 N  N   A CYS   B 2 22  ? 35.747  -30.020 18.118  0.59 14.56 ? 22  CYS   B N   1 
ATOM   2520 N  N   B CYS   B 2 22  ? 35.804  -29.878 18.047  0.41 13.85 ? 22  CYS   B N   1 
ATOM   2521 C  CA  A CYS   B 2 22  ? 36.855  -30.953 18.270  0.59 15.64 ? 22  CYS   B CA  1 
ATOM   2522 C  CA  B CYS   B 2 22  ? 36.828  -30.849 18.370  0.41 14.28 ? 22  CYS   B CA  1 
ATOM   2523 C  C   A CYS   B 2 22  ? 36.869  -31.406 19.735  0.59 16.16 ? 22  CYS   B C   1 
ATOM   2524 C  C   B CYS   B 2 22  ? 36.580  -31.310 19.800  0.41 15.19 ? 22  CYS   B C   1 
ATOM   2525 O  O   A CYS   B 2 22  ? 37.339  -30.671 20.614  0.59 15.89 ? 22  CYS   B O   1 
ATOM   2526 O  O   B CYS   B 2 22  ? 36.605  -30.493 20.724  0.41 15.07 ? 22  CYS   B O   1 
ATOM   2527 C  CB  A CYS   B 2 22  ? 38.160  -30.308 17.809  0.59 16.08 ? 22  CYS   B CB  1 
ATOM   2528 C  CB  B CYS   B 2 22  ? 38.209  -30.225 18.279  0.41 13.96 ? 22  CYS   B CB  1 
ATOM   2529 S  SG  A CYS   B 2 22  ? 39.599  -31.416 17.692  0.59 19.46 ? 22  CYS   B SG  1 
ATOM   2530 S  SG  B CYS   B 2 22  ? 38.925  -30.279 16.623  0.41 13.33 ? 22  CYS   B SG  1 
ATOM   2531 N  N   . GLY   B 2 23  ? 36.310  -32.602 19.979  1.00 15.29 ? 23  GLY   B N   1 
ATOM   2532 C  CA  . GLY   B 2 23  ? 36.024  -33.094 21.317  1.00 15.65 ? 23  GLY   B CA  1 
ATOM   2533 C  C   . GLY   B 2 23  ? 34.762  -32.446 21.871  1.00 15.48 ? 23  GLY   B C   1 
ATOM   2534 O  O   . GLY   B 2 23  ? 33.669  -32.625 21.327  1.00 14.83 ? 23  GLY   B O   1 
ATOM   2535 N  N   . THR   B 2 24  ? 34.928  -31.614 22.907  1.00 15.96 ? 24  THR   B N   1 
ATOM   2536 C  CA  . THR   B 2 24  ? 33.839  -30.743 23.343  1.00 17.88 ? 24  THR   B CA  1 
ATOM   2537 C  C   . THR   B 2 24  ? 34.100  -29.274 22.977  1.00 16.58 ? 24  THR   B C   1 
ATOM   2538 O  O   . THR   B 2 24  ? 33.251  -28.416 23.184  1.00 18.07 ? 24  THR   B O   1 
ATOM   2539 C  CB  . THR   B 2 24  ? 33.626  -30.855 24.862  1.00 19.16 ? 24  THR   B CB  1 
ATOM   2540 O  OG1 . THR   B 2 24  ? 34.843  -30.446 25.500  1.00 20.34 ? 24  THR   B OG1 1 
ATOM   2541 C  CG2 . THR   B 2 24  ? 33.249  -32.259 25.277  1.00 21.31 ? 24  THR   B CG2 1 
ATOM   2542 N  N   . THR   B 2 25  ? 35.303  -28.950 22.510  1.00 17.07 ? 25  THR   B N   1 
ATOM   2543 C  CA  . THR   B 2 25  ? 35.628  -27.565 22.182  1.00 17.18 ? 25  THR   B CA  1 
ATOM   2544 C  C   . THR   B 2 25  ? 34.880  -27.194 20.898  1.00 18.45 ? 25  THR   B C   1 
ATOM   2545 O  O   . THR   B 2 25  ? 34.965  -27.920 19.912  1.00 14.88 ? 25  THR   B O   1 
ATOM   2546 C  CB  . THR   B 2 25  ? 37.135  -27.355 22.070  1.00 17.01 ? 25  THR   B CB  1 
ATOM   2547 O  OG1 . THR   B 2 25  ? 37.770  -27.871 23.248  1.00 16.49 ? 25  THR   B OG1 1 
ATOM   2548 C  CG2 . THR   B 2 25  ? 37.495  -25.892 21.861  1.00 15.77 ? 25  THR   B CG2 1 
ATOM   2549 N  N   . THR   B 2 26  ? 34.082  -26.109 20.953  1.00 18.88 ? 26  THR   B N   1 
ATOM   2550 C  CA  . THR   B 2 26  ? 33.180  -25.786 19.865  1.00 18.20 ? 26  THR   B CA  1 
ATOM   2551 C  C   . THR   B 2 26  ? 33.210  -24.286 19.588  1.00 16.61 ? 26  THR   B C   1 
ATOM   2552 O  O   . THR   B 2 26  ? 33.399  -23.473 20.489  1.00 15.40 ? 26  THR   B O   1 
ATOM   2553 C  CB  . THR   B 2 26  ? 31.777  -26.306 20.155  1.00 21.75 ? 26  THR   B CB  1 
ATOM   2554 O  OG1 . THR   B 2 26  ? 31.021  -26.266 18.944  1.00 23.97 ? 26  THR   B OG1 1 
ATOM   2555 C  CG2 . THR   B 2 26  ? 31.064  -25.518 21.232  1.00 23.73 ? 26  THR   B CG2 1 
ATOM   2556 N  N   . LEU   B 2 27  ? 33.106  -23.933 18.299  1.00 13.96 ? 27  LEU   B N   1 
ATOM   2557 C  CA  . LEU   B 2 27  ? 33.075  -22.544 17.881  1.00 12.27 ? 27  LEU   B CA  1 
ATOM   2558 C  C   . LEU   B 2 27  ? 32.518  -22.445 16.462  1.00 11.01 ? 27  LEU   B C   1 
ATOM   2559 O  O   . LEU   B 2 27  ? 32.039  -23.427 15.889  1.00 10.18 ? 27  LEU   B O   1 
ATOM   2560 C  CB  . LEU   B 2 27  ? 34.474  -21.926 18.001  1.00 13.09 ? 27  LEU   B CB  1 
ATOM   2561 C  CG  . LEU   B 2 27  ? 35.671  -22.739 17.525  1.00 13.11 ? 27  LEU   B CG  1 
ATOM   2562 C  CD1 . LEU   B 2 27  ? 35.557  -23.062 16.052  1.00 13.97 ? 27  LEU   B CD1 1 
ATOM   2563 C  CD2 . LEU   B 2 27  ? 36.960  -21.965 17.791  1.00 13.70 ? 27  LEU   B CD2 1 
ATOM   2564 N  N   . ASN   B 2 28  ? 32.576  -21.240 15.897  1.00 10.05 ? 28  ASN   B N   1 
ATOM   2565 C  CA  . ASN   B 2 28  ? 31.970  -20.969 14.603  1.00 10.20 ? 28  ASN   B CA  1 
ATOM   2566 C  C   . ASN   B 2 28  ? 33.036  -21.055 13.514  1.00 9.26  ? 28  ASN   B C   1 
ATOM   2567 O  O   . ASN   B 2 28  ? 34.202  -20.712 13.734  1.00 9.36  ? 28  ASN   B O   1 
ATOM   2568 C  CB  . ASN   B 2 28  ? 31.321  -19.587 14.574  1.00 10.50 ? 28  ASN   B CB  1 
ATOM   2569 C  CG  . ASN   B 2 28  ? 30.279  -19.415 15.660  1.00 11.52 ? 28  ASN   B CG  1 
ATOM   2570 O  OD1 . ASN   B 2 28  ? 29.168  -19.928 15.567  1.00 12.56 ? 28  ASN   B OD1 1 
ATOM   2571 N  ND2 . ASN   B 2 28  ? 30.643  -18.698 16.701  1.00 12.09 ? 28  ASN   B ND2 1 
ATOM   2572 N  N   . GLY   B 2 29  ? 32.604  -21.506 12.340  1.00 8.71  ? 29  GLY   B N   1 
ATOM   2573 C  CA  . GLY   B 2 29  ? 33.467  -21.558 11.178  1.00 8.84  ? 29  GLY   B CA  1 
ATOM   2574 C  C   . GLY   B 2 29  ? 32.810  -20.911 9.966   1.00 8.55  ? 29  GLY   B C   1 
ATOM   2575 O  O   . GLY   B 2 29  ? 31.598  -20.708 9.945   1.00 8.61  ? 29  GLY   B O   1 
ATOM   2576 N  N   . LEU   B 2 30  ? 33.627  -20.695 8.933   1.00 8.71  ? 30  LEU   B N   1 
ATOM   2577 C  CA  . LEU   B 2 30  ? 33.187  -20.052 7.710   1.00 8.49  ? 30  LEU   B CA  1 
ATOM   2578 C  C   . LEU   B 2 30  ? 33.389  -20.996 6.527   1.00 8.19  ? 30  LEU   B C   1 
ATOM   2579 O  O   . LEU   B 2 30  ? 34.507  -21.349 6.172   1.00 8.54  ? 30  LEU   B O   1 
ATOM   2580 C  CB  . LEU   B 2 30  ? 33.950  -18.734 7.559   1.00 9.19  ? 30  LEU   B CB  1 
ATOM   2581 C  CG  . LEU   B 2 30  ? 33.591  -17.880 6.333   1.00 9.41  ? 30  LEU   B CG  1 
ATOM   2582 C  CD1 . LEU   B 2 30  ? 32.253  -17.183 6.543   1.00 9.80  ? 30  LEU   B CD1 1 
ATOM   2583 C  CD2 . LEU   B 2 30  ? 34.659  -16.858 6.052   1.00 10.08 ? 30  LEU   B CD2 1 
ATOM   2584 N  N   . TRP   B 2 31  ? 32.291  -21.346 5.865   1.00 8.07  ? 31  TRP   B N   1 
ATOM   2585 C  CA  . TRP   B 2 31  ? 32.270  -22.334 4.812   1.00 8.18  ? 31  TRP   B CA  1 
ATOM   2586 C  C   . TRP   B 2 31  ? 32.181  -21.644 3.450   1.00 8.40  ? 31  TRP   B C   1 
ATOM   2587 O  O   . TRP   B 2 31  ? 31.128  -21.106 3.088   1.00 8.29  ? 31  TRP   B O   1 
ATOM   2588 C  CB  . TRP   B 2 31  ? 31.079  -23.280 5.042   1.00 8.93  ? 31  TRP   B CB  1 
ATOM   2589 C  CG  . TRP   B 2 31  ? 30.938  -24.408 4.045   1.00 9.13  ? 31  TRP   B CG  1 
ATOM   2590 C  CD1 . TRP   B 2 31  ? 31.891  -24.951 3.227   1.00 9.49  ? 31  TRP   B CD1 1 
ATOM   2591 C  CD2 . TRP   B 2 31  ? 29.720  -25.120 3.762   1.00 9.06  ? 31  TRP   B CD2 1 
ATOM   2592 N  NE1 . TRP   B 2 31  ? 31.359  -25.981 2.499   1.00 9.30  ? 31  TRP   B NE1 1 
ATOM   2593 C  CE2 . TRP   B 2 31  ? 30.034  -26.104 2.798   1.00 9.57  ? 31  TRP   B CE2 1 
ATOM   2594 C  CE3 . TRP   B 2 31  ? 28.413  -25.030 4.242   1.00 9.28  ? 31  TRP   B CE3 1 
ATOM   2595 C  CZ2 . TRP   B 2 31  ? 29.073  -26.991 2.316   1.00 10.01 ? 31  TRP   B CZ2 1 
ATOM   2596 C  CZ3 . TRP   B 2 31  ? 27.461  -25.907 3.771   1.00 9.75  ? 31  TRP   B CZ3 1 
ATOM   2597 C  CH2 . TRP   B 2 31  ? 27.791  -26.876 2.818   1.00 9.80  ? 31  TRP   B CH2 1 
ATOM   2598 N  N   . LEU   B 2 32  ? 33.286  -21.698 2.699   1.00 7.78  ? 32  LEU   B N   1 
ATOM   2599 C  CA  . LEU   B 2 32  ? 33.381  -21.071 1.388   1.00 8.95  ? 32  LEU   B CA  1 
ATOM   2600 C  C   . LEU   B 2 32  ? 33.919  -22.087 0.401   1.00 8.62  ? 32  LEU   B C   1 
ATOM   2601 O  O   . LEU   B 2 32  ? 34.961  -22.667 0.635   1.00 8.35  ? 32  LEU   B O   1 
ATOM   2602 C  CB  . LEU   B 2 32  ? 34.333  -19.864 1.429   1.00 9.39  ? 32  LEU   B CB  1 
ATOM   2603 C  CG  . LEU   B 2 32  ? 33.942  -18.754 2.408   1.00 9.49  ? 32  LEU   B CG  1 
ATOM   2604 C  CD1 . LEU   B 2 32  ? 35.121  -17.819 2.598   1.00 9.99  ? 32  LEU   B CD1 1 
ATOM   2605 C  CD2 . LEU   B 2 32  ? 32.721  -17.979 1.906   1.00 9.51  ? 32  LEU   B CD2 1 
ATOM   2606 N  N   . ASP   B 2 33  ? 33.200  -22.280 -0.700  1.00 9.75  ? 33  ASP   B N   1 
ATOM   2607 C  CA  . ASP   B 2 33  ? 33.511  -23.382 -1.606  1.00 10.98 ? 33  ASP   B CA  1 
ATOM   2608 C  C   . ASP   B 2 33  ? 33.662  -24.639 -0.746  1.00 10.82 ? 33  ASP   B C   1 
ATOM   2609 O  O   . ASP   B 2 33  ? 32.792  -24.917 0.061   1.00 11.44 ? 33  ASP   B O   1 
ATOM   2610 C  CB  . ASP   B 2 33  ? 34.717  -23.043 -2.490  1.00 11.36 ? 33  ASP   B CB  1 
ATOM   2611 C  CG  . ASP   B 2 33  ? 34.448  -21.806 -3.331  1.00 12.88 ? 33  ASP   B CG  1 
ATOM   2612 O  OD1 . ASP   B 2 33  ? 33.440  -21.782 -4.053  1.00 14.00 ? 33  ASP   B OD1 1 
ATOM   2613 O  OD2 . ASP   B 2 33  ? 35.247  -20.904 -3.282  1.00 14.27 ? 33  ASP   B OD2 1 
ATOM   2614 N  N   . ASP   B 2 34  ? 34.756  -25.398 -0.904  1.00 12.20 ? 34  ASP   B N   1 
ATOM   2615 C  CA  . ASP   B 2 34  ? 34.885  -26.665 -0.181  1.00 11.76 ? 34  ASP   B CA  1 
ATOM   2616 C  C   . ASP   B 2 34  ? 35.856  -26.548 0.990   1.00 10.66 ? 34  ASP   B C   1 
ATOM   2617 O  O   . ASP   B 2 34  ? 36.477  -27.538 1.371   1.00 11.29 ? 34  ASP   B O   1 
ATOM   2618 C  CB  . ASP   B 2 34  ? 35.286  -27.801 -1.111  1.00 12.67 ? 34  ASP   B CB  1 
ATOM   2619 C  CG  . ASP   B 2 34  ? 36.629  -27.598 -1.806  1.00 13.44 ? 34  ASP   B CG  1 
ATOM   2620 O  OD1 . ASP   B 2 34  ? 37.137  -26.500 -1.771  1.00 13.99 ? 34  ASP   B OD1 1 
ATOM   2621 O  OD2 . ASP   B 2 34  ? 37.121  -28.549 -2.393  1.00 15.86 ? 34  ASP   B OD2 1 
ATOM   2622 N  N   . VAL   B 2 35  ? 35.963  -25.355 1.588   1.00 9.94  ? 35  VAL   B N   1 
ATOM   2623 C  CA  . VAL   B 2 35  ? 36.855  -25.173 2.719   1.00 10.17 ? 35  VAL   B CA  1 
ATOM   2624 C  C   . VAL   B 2 35  ? 36.082  -24.489 3.856   1.00 9.90  ? 35  VAL   B C   1 
ATOM   2625 O  O   . VAL   B 2 35  ? 35.356  -23.544 3.622   1.00 8.72  ? 35  VAL   B O   1 
ATOM   2626 C  CB  . VAL   B 2 35  ? 38.116  -24.372 2.342   1.00 9.97  ? 35  VAL   B CB  1 
ATOM   2627 C  CG1 . VAL   B 2 35  ? 38.978  -24.129 3.566   1.00 10.24 ? 35  VAL   B CG1 1 
ATOM   2628 C  CG2 . VAL   B 2 35  ? 38.924  -25.044 1.242   1.00 10.98 ? 35  VAL   B CG2 1 
ATOM   2629 N  N   . VAL   B 2 36  ? 36.321  -24.966 5.083   1.00 10.07 ? 36  VAL   B N   1 
ATOM   2630 C  CA  . VAL   B 2 36  ? 35.841  -24.327 6.292   1.00 10.19 ? 36  VAL   B CA  1 
ATOM   2631 C  C   . VAL   B 2 36  ? 37.015  -23.716 7.046   1.00 10.16 ? 36  VAL   B C   1 
ATOM   2632 O  O   . VAL   B 2 36  ? 37.979  -24.409 7.353   1.00 10.19 ? 36  VAL   B O   1 
ATOM   2633 C  CB  . VAL   B 2 36  ? 35.079  -25.324 7.165   1.00 10.40 ? 36  VAL   B CB  1 
ATOM   2634 C  CG1 . VAL   B 2 36  ? 34.739  -24.731 8.528   1.00 10.99 ? 36  VAL   B CG1 1 
ATOM   2635 C  CG2 . VAL   B 2 36  ? 33.816  -25.804 6.453   1.00 10.78 ? 36  VAL   B CG2 1 
ATOM   2636 N  N   . TYR   B 2 37  ? 36.917  -22.407 7.296   1.00 9.78  ? 37  TYR   B N   1 
ATOM   2637 C  CA  . TYR   B 2 37  ? 37.915  -21.644 8.014   1.00 10.29 ? 37  TYR   B CA  1 
ATOM   2638 C  C   . TYR   B 2 37  ? 37.412  -21.409 9.439   1.00 10.32 ? 37  TYR   B C   1 
ATOM   2639 O  O   . TYR   B 2 37  ? 36.285  -20.970 9.640   1.00 9.00  ? 37  TYR   B O   1 
ATOM   2640 C  CB  . TYR   B 2 37  ? 38.160  -20.282 7.343   1.00 10.79 ? 37  TYR   B CB  1 
ATOM   2641 C  CG  . TYR   B 2 37  ? 38.503  -20.368 5.866   1.00 11.67 ? 37  TYR   B CG  1 
ATOM   2642 C  CD1 . TYR   B 2 37  ? 37.514  -20.621 4.917   1.00 11.99 ? 37  TYR   B CD1 1 
ATOM   2643 C  CD2 . TYR   B 2 37  ? 39.819  -20.288 5.428   1.00 11.65 ? 37  TYR   B CD2 1 
ATOM   2644 C  CE1 . TYR   B 2 37  ? 37.822  -20.776 3.574   1.00 11.86 ? 37  TYR   B CE1 1 
ATOM   2645 C  CE2 . TYR   B 2 37  ? 40.127  -20.409 4.080   1.00 11.65 ? 37  TYR   B CE2 1 
ATOM   2646 C  CZ  . TYR   B 2 37  ? 39.134  -20.673 3.161   1.00 11.57 ? 37  TYR   B CZ  1 
ATOM   2647 O  OH  . TYR   B 2 37  ? 39.441  -20.807 1.841   1.00 12.20 ? 37  TYR   B OH  1 
ATOM   2648 N  N   . CYS   B 2 38  ? 38.273  -21.653 10.432  1.00 10.56 ? 38  CYS   B N   1 
ATOM   2649 C  CA  . CYS   B 2 38  ? 37.909  -21.376 11.811  1.00 10.65 ? 38  CYS   B CA  1 
ATOM   2650 C  C   . CYS   B 2 38  ? 39.160  -21.122 12.639  1.00 11.25 ? 38  CYS   B C   1 
ATOM   2651 O  O   . CYS   B 2 38  ? 40.269  -21.403 12.185  1.00 11.22 ? 38  CYS   B O   1 
ATOM   2652 C  CB  . CYS   B 2 38  ? 37.069  -22.514 12.387  1.00 11.21 ? 38  CYS   B CB  1 
ATOM   2653 S  SG  . CYS   B 2 38  ? 38.004  -24.018 12.766  1.00 12.38 ? 38  CYS   B SG  1 
ATOM   2654 N  N   . PRO   B 2 39  ? 39.026  -20.564 13.861  1.00 11.32 ? 39  PRO   B N   1 
ATOM   2655 C  CA  . PRO   B 2 39  ? 40.177  -20.397 14.752  1.00 11.24 ? 39  PRO   B CA  1 
ATOM   2656 C  C   . PRO   B 2 39  ? 40.773  -21.747 15.140  1.00 11.96 ? 39  PRO   B C   1 
ATOM   2657 O  O   . PRO   B 2 39  ? 40.038  -22.666 15.511  1.00 11.41 ? 39  PRO   B O   1 
ATOM   2658 C  CB  . PRO   B 2 39  ? 39.589  -19.664 15.972  1.00 11.79 ? 39  PRO   B CB  1 
ATOM   2659 C  CG  . PRO   B 2 39  ? 38.322  -19.021 15.425  1.00 11.70 ? 39  PRO   B CG  1 
ATOM   2660 C  CD  . PRO   B 2 39  ? 37.782  -20.029 14.430  1.00 11.06 ? 39  PRO   B CD  1 
ATOM   2661 N  N   . ARG   B 2 40  ? 42.110  -21.859 15.049  1.00 12.07 ? 40  ARG   B N   1 
ATOM   2662 C  CA  . ARG   B 2 40  ? 42.800  -23.100 15.388  1.00 13.31 ? 40  ARG   B CA  1 
ATOM   2663 C  C   . ARG   B 2 40  ? 42.650  -23.434 16.871  1.00 12.75 ? 40  ARG   B C   1 
ATOM   2664 O  O   . ARG   B 2 40  ? 42.873  -24.580 17.235  1.00 13.01 ? 40  ARG   B O   1 
ATOM   2665 C  CB  . ARG   B 2 40  ? 44.281  -23.036 14.990  1.00 13.40 ? 40  ARG   B CB  1 
ATOM   2666 C  CG  . ARG   B 2 40  ? 45.111  -22.085 15.834  1.00 14.42 ? 40  ARG   B CG  1 
ATOM   2667 C  CD  . ARG   B 2 40  ? 46.564  -22.144 15.444  1.00 15.18 ? 40  ARG   B CD  1 
ATOM   2668 N  NE  . ARG   B 2 40  ? 47.322  -21.150 16.181  1.00 16.15 ? 40  ARG   B NE  1 
ATOM   2669 C  CZ  . ARG   B 2 40  ? 48.640  -21.026 16.140  1.00 16.61 ? 40  ARG   B CZ  1 
ATOM   2670 N  NH1 . ARG   B 2 40  ? 49.357  -21.743 15.303  1.00 16.92 ? 40  ARG   B NH1 1 
ATOM   2671 N  NH2 . ARG   B 2 40  ? 49.232  -20.159 16.932  1.00 17.32 ? 40  ARG   B NH2 1 
ATOM   2672 N  N   . HIS   B 2 41  ? 42.234  -22.454 17.706  1.00 12.83 ? 41  HIS   B N   1 
ATOM   2673 C  CA  . HIS   B 2 41  ? 41.973  -22.677 19.127  1.00 13.35 ? 41  HIS   B CA  1 
ATOM   2674 C  C   . HIS   B 2 41  ? 41.023  -23.847 19.379  1.00 13.84 ? 41  HIS   B C   1 
ATOM   2675 O  O   . HIS   B 2 41  ? 40.995  -24.379 20.487  1.00 15.42 ? 41  HIS   B O   1 
ATOM   2676 C  CB  . HIS   B 2 41  ? 41.422  -21.409 19.807  1.00 14.43 ? 41  HIS   B CB  1 
ATOM   2677 C  CG  . HIS   B 2 41  ? 41.613  -21.334 21.271  1.00 14.82 ? 41  HIS   B CG  1 
ATOM   2678 N  ND1 . HIS   B 2 41  ? 42.875  -21.278 21.841  1.00 17.41 ? 41  HIS   B ND1 1 
ATOM   2679 C  CD2 . HIS   B 2 41  ? 40.731  -21.293 22.288  1.00 15.57 ? 41  HIS   B CD2 1 
ATOM   2680 C  CE1 . HIS   B 2 41  ? 42.736  -21.192 23.175  1.00 16.73 ? 41  HIS   B CE1 1 
ATOM   2681 N  NE2 . HIS   B 2 41  ? 41.434  -21.215 23.462  1.00 15.27 ? 41  HIS   B NE2 1 
ATOM   2682 N  N   . VAL   B 2 42  ? 40.217  -24.229 18.376  1.00 13.87 ? 42  VAL   B N   1 
ATOM   2683 C  CA  . VAL   B 2 42  ? 39.230  -25.294 18.509  1.00 13.15 ? 42  VAL   B CA  1 
ATOM   2684 C  C   . VAL   B 2 42  ? 39.892  -26.635 18.854  1.00 13.66 ? 42  VAL   B C   1 
ATOM   2685 O  O   . VAL   B 2 42  ? 39.224  -27.519 19.383  1.00 13.65 ? 42  VAL   B O   1 
ATOM   2686 C  CB  . VAL   B 2 42  ? 38.366  -25.415 17.228  1.00 12.17 ? 42  VAL   B CB  1 
ATOM   2687 C  CG1 . VAL   B 2 42  ? 39.112  -26.015 16.052  1.00 12.48 ? 42  VAL   B CG1 1 
ATOM   2688 C  CG2 . VAL   B 2 42  ? 37.081  -26.201 17.459  1.00 12.52 ? 42  VAL   B CG2 1 
ATOM   2689 N  N   . ILE   B 2 43  ? 41.167  -26.826 18.495  1.00 15.13 ? 43  ILE   B N   1 
ATOM   2690 C  CA  . ILE   B 2 43  ? 41.849  -28.088 18.754  1.00 16.31 ? 43  ILE   B CA  1 
ATOM   2691 C  C   . ILE   B 2 43  ? 42.340  -28.163 20.204  1.00 18.37 ? 43  ILE   B C   1 
ATOM   2692 O  O   . ILE   B 2 43  ? 42.838  -29.218 20.605  1.00 17.87 ? 43  ILE   B O   1 
ATOM   2693 C  CB  . ILE   B 2 43  ? 43.005  -28.365 17.768  1.00 15.33 ? 43  ILE   B CB  1 
ATOM   2694 C  CG1 . ILE   B 2 43  ? 44.197  -27.420 17.963  1.00 15.64 ? 43  ILE   B CG1 1 
ATOM   2695 C  CG2 . ILE   B 2 43  ? 42.519  -28.349 16.335  1.00 15.82 ? 43  ILE   B CG2 1 
ATOM   2696 C  CD1 . ILE   B 2 43  ? 45.360  -27.710 17.046  1.00 15.50 ? 43  ILE   B CD1 1 
ATOM   2697 N  N   . CYS   B 2 44  ? 42.179  -27.091 21.003  1.00 18.83 ? 44  CYS   B N   1 
ATOM   2698 C  CA  . CYS   B 2 44  ? 42.567  -27.149 22.413  1.00 19.70 ? 44  CYS   B CA  1 
ATOM   2699 C  C   . CYS   B 2 44  ? 41.508  -27.786 23.305  1.00 20.16 ? 44  CYS   B C   1 
ATOM   2700 O  O   . CYS   B 2 44  ? 40.354  -27.356 23.284  1.00 22.35 ? 44  CYS   B O   1 
ATOM   2701 C  CB  . CYS   B 2 44  ? 42.844  -25.759 22.978  1.00 17.94 ? 44  CYS   B CB  1 
ATOM   2702 S  SG  . CYS   B 2 44  ? 44.197  -24.955 22.110  1.00 17.68 ? 44  CYS   B SG  1 
ATOM   2703 N  N   . THR   B 2 45  ? 41.948  -28.748 24.147  1.00 19.69 ? 45  THR   B N   1 
ATOM   2704 C  CA  . THR   B 2 45  ? 41.222  -29.146 25.338  1.00 21.37 ? 45  THR   B CA  1 
ATOM   2705 C  C   . THR   B 2 45  ? 41.358  -28.032 26.362  1.00 23.82 ? 45  THR   B C   1 
ATOM   2706 O  O   . THR   B 2 45  ? 42.210  -27.156 26.227  1.00 23.60 ? 45  THR   B O   1 
ATOM   2707 C  CB  . THR   B 2 45  ? 41.748  -30.443 25.999  1.00 21.91 ? 45  THR   B CB  1 
ATOM   2708 O  OG1 . THR   B 2 45  ? 43.060  -30.162 26.494  1.00 20.40 ? 45  THR   B OG1 1 
ATOM   2709 C  CG2 . THR   B 2 45  ? 41.828  -31.635 25.059  1.00 22.52 ? 45  THR   B CG2 1 
ATOM   2710 N  N   . SER   B 2 46  ? 40.542  -28.101 27.417  1.00 26.47 ? 46  SER   B N   1 
ATOM   2711 C  CA  . SER   B 2 46  ? 40.638  -27.122 28.495  1.00 30.67 ? 46  SER   B CA  1 
ATOM   2712 C  C   . SER   B 2 46  ? 42.083  -26.910 28.949  1.00 30.44 ? 46  SER   B C   1 
ATOM   2713 O  O   . SER   B 2 46  ? 42.495  -25.774 29.190  1.00 32.83 ? 46  SER   B O   1 
ATOM   2714 C  CB  . SER   B 2 46  ? 39.787  -27.528 29.649  1.00 32.56 ? 46  SER   B CB  1 
ATOM   2715 O  OG  . SER   B 2 46  ? 38.435  -27.492 29.252  1.00 39.11 ? 46  SER   B OG  1 
ATOM   2716 N  N   . GLU   B 2 47  ? 42.849  -27.999 29.067  1.00 27.85 ? 47  GLU   B N   1 
ATOM   2717 C  CA  . GLU   B 2 47  ? 44.180  -27.948 29.661  1.00 29.39 ? 47  GLU   B CA  1 
ATOM   2718 C  C   . GLU   B 2 47  ? 45.192  -27.398 28.670  1.00 27.77 ? 47  GLU   B C   1 
ATOM   2719 O  O   . GLU   B 2 47  ? 46.274  -26.962 29.064  1.00 30.40 ? 47  GLU   B O   1 
ATOM   2720 C  CB  . GLU   B 2 47  ? 44.627  -29.343 30.096  1.00 31.34 ? 47  GLU   B CB  1 
ATOM   2721 C  CG  . GLU   B 2 47  ? 43.813  -29.888 31.263  1.00 32.33 ? 47  GLU   B CG  1 
ATOM   2722 C  CD  . GLU   B 2 47  ? 42.331  -30.114 31.010  1.00 35.46 ? 47  GLU   B CD  1 
ATOM   2723 O  OE1 . GLU   B 2 47  ? 41.988  -30.718 29.967  1.00 31.72 ? 47  GLU   B OE1 1 
ATOM   2724 O  OE2 . GLU   B 2 47  ? 41.517  -29.718 31.873  1.00 41.51 ? 47  GLU   B OE2 1 
ATOM   2725 N  N   . ASP   B 2 48  ? 44.831  -27.423 27.382  1.00 22.97 ? 48  ASP   B N   1 
ATOM   2726 C  CA  . ASP   B 2 48  ? 45.680  -26.886 26.334  1.00 22.99 ? 48  ASP   B CA  1 
ATOM   2727 C  C   . ASP   B 2 48  ? 45.569  -25.359 26.226  1.00 21.45 ? 48  ASP   B C   1 
ATOM   2728 O  O   . ASP   B 2 48  ? 46.484  -24.715 25.732  1.00 25.08 ? 48  ASP   B O   1 
ATOM   2729 C  CB  . ASP   B 2 48  ? 45.325  -27.545 24.996  1.00 22.58 ? 48  ASP   B CB  1 
ATOM   2730 C  CG  . ASP   B 2 48  ? 45.530  -29.055 24.986  1.00 22.36 ? 48  ASP   B CG  1 
ATOM   2731 O  OD1 . ASP   B 2 48  ? 46.568  -29.470 25.529  1.00 20.21 ? 48  ASP   B OD1 1 
ATOM   2732 O  OD2 . ASP   B 2 48  ? 44.661  -29.804 24.392  1.00 21.42 ? 48  ASP   B OD2 1 
ATOM   2733 N  N   . MET   B 2 49  ? 44.451  -24.777 26.648  1.00 22.56 ? 49  MET   B N   1 
ATOM   2734 C  CA  . MET   B 2 49  ? 44.089  -23.427 26.214  1.00 25.33 ? 49  MET   B CA  1 
ATOM   2735 C  C   . MET   B 2 49  ? 45.053  -22.362 26.755  1.00 26.76 ? 49  MET   B C   1 
ATOM   2736 O  O   . MET   B 2 49  ? 45.294  -21.347 26.097  1.00 24.26 ? 49  MET   B O   1 
ATOM   2737 C  CB  . MET   B 2 49  ? 42.651  -23.107 26.634  1.00 24.55 ? 49  MET   B CB  1 
ATOM   2738 C  CG  . MET   B 2 49  ? 41.608  -23.767 25.742  1.00 22.29 ? 49  MET   B CG  1 
ATOM   2739 S  SD  . MET   B 2 49  ? 39.966  -23.729 26.491  1.00 21.56 ? 49  MET   B SD  1 
ATOM   2740 C  CE  . MET   B 2 49  ? 38.974  -24.625 25.302  1.00 23.60 ? 49  MET   B CE  1 
ATOM   2741 N  N   . LEU   B 2 50  ? 45.670  -22.612 27.918  1.00 28.96 ? 50  LEU   B N   1 
ATOM   2742 C  CA  . LEU   B 2 50  ? 46.534  -21.624 28.556  1.00 29.79 ? 50  LEU   B CA  1 
ATOM   2743 C  C   . LEU   B 2 50  ? 47.830  -21.431 27.769  1.00 29.91 ? 50  LEU   B C   1 
ATOM   2744 O  O   . LEU   B 2 50  ? 48.280  -20.295 27.579  1.00 26.23 ? 50  LEU   B O   1 
ATOM   2745 C  CB  . LEU   B 2 50  ? 46.831  -22.040 30.000  1.00 32.29 ? 50  LEU   B CB  1 
ATOM   2746 C  CG  . LEU   B 2 50  ? 48.000  -21.316 30.681  1.00 36.49 ? 50  LEU   B CG  1 
ATOM   2747 C  CD1 . LEU   B 2 50  ? 47.852  -19.795 30.672  1.00 36.46 ? 50  LEU   B CD1 1 
ATOM   2748 C  CD2 . LEU   B 2 50  ? 48.153  -21.805 32.122  1.00 38.18 ? 50  LEU   B CD2 1 
ATOM   2749 N  N   . ASN   B 2 51  ? 48.425  -22.540 27.312  1.00 27.22 ? 51  ASN   B N   1 
ATOM   2750 C  CA  . ASN   B 2 51  ? 49.719  -22.464 26.654  1.00 30.22 ? 51  ASN   B CA  1 
ATOM   2751 C  C   . ASN   B 2 51  ? 49.846  -23.574 25.605  1.00 26.76 ? 51  ASN   B C   1 
ATOM   2752 O  O   . ASN   B 2 51  ? 50.580  -24.547 25.764  1.00 22.85 ? 51  ASN   B O   1 
ATOM   2753 C  CB  . ASN   B 2 51  ? 50.879  -22.541 27.656  1.00 32.37 ? 51  ASN   B CB  1 
ATOM   2754 C  CG  . ASN   B 2 51  ? 52.186  -22.115 27.026  1.00 37.03 ? 51  ASN   B CG  1 
ATOM   2755 O  OD1 . ASN   B 2 51  ? 52.218  -21.505 25.955  1.00 43.41 ? 51  ASN   B OD1 1 
ATOM   2756 N  ND2 . ASN   B 2 51  ? 53.284  -22.396 27.697  1.00 47.18 ? 51  ASN   B ND2 1 
ATOM   2757 N  N   . PRO   B 2 52  ? 49.069  -23.486 24.511  1.00 25.23 ? 52  PRO   B N   1 
ATOM   2758 C  CA  . PRO   B 2 52  ? 49.042  -24.551 23.515  1.00 23.80 ? 52  PRO   B CA  1 
ATOM   2759 C  C   . PRO   B 2 52  ? 50.288  -24.619 22.651  1.00 23.79 ? 52  PRO   B C   1 
ATOM   2760 O  O   . PRO   B 2 52  ? 50.845  -23.618 22.214  1.00 22.67 ? 52  PRO   B O   1 
ATOM   2761 C  CB  . PRO   B 2 52  ? 47.801  -24.207 22.667  1.00 24.59 ? 52  PRO   B CB  1 
ATOM   2762 C  CG  . PRO   B 2 52  ? 47.644  -22.702 22.832  1.00 24.80 ? 52  PRO   B CG  1 
ATOM   2763 C  CD  . PRO   B 2 52  ? 48.117  -22.401 24.233  1.00 23.83 ? 52  PRO   B CD  1 
ATOM   2764 N  N   . ASN   B 2 53  ? 50.710  -25.850 22.377  1.00 24.91 ? 53  ASN   B N   1 
ATOM   2765 C  CA  . ASN   B 2 53  ? 51.636  -26.098 21.293  1.00 26.18 ? 53  ASN   B CA  1 
ATOM   2766 C  C   . ASN   B 2 53  ? 50.811  -26.559 20.090  1.00 24.95 ? 53  ASN   B C   1 
ATOM   2767 O  O   . ASN   B 2 53  ? 50.438  -27.733 19.995  1.00 24.54 ? 53  ASN   B O   1 
ATOM   2768 C  CB  . ASN   B 2 53  ? 52.707  -27.103 21.715  1.00 26.44 ? 53  ASN   B CB  1 
ATOM   2769 C  CG  . ASN   B 2 53  ? 53.797  -27.220 20.681  1.00 30.28 ? 53  ASN   B CG  1 
ATOM   2770 O  OD1 . ASN   B 2 53  ? 53.534  -27.355 19.491  1.00 32.27 ? 53  ASN   B OD1 1 
ATOM   2771 N  ND2 . ASN   B 2 53  ? 55.038  -27.123 21.111  1.00 35.52 ? 53  ASN   B ND2 1 
ATOM   2772 N  N   . TYR   B 2 54  ? 50.561  -25.649 19.145  1.00 21.45 ? 54  TYR   B N   1 
ATOM   2773 C  CA  . TYR   B 2 54  ? 49.536  -25.909 18.145  1.00 21.88 ? 54  TYR   B CA  1 
ATOM   2774 C  C   . TYR   B 2 54  ? 50.039  -26.946 17.140  1.00 21.32 ? 54  TYR   B C   1 
ATOM   2775 O  O   . TYR   B 2 54  ? 49.266  -27.800 16.698  1.00 17.92 ? 54  TYR   B O   1 
ATOM   2776 C  CB  . TYR   B 2 54  ? 49.102  -24.598 17.482  1.00 19.75 ? 54  TYR   B CB  1 
ATOM   2777 C  CG  . TYR   B 2 54  ? 48.096  -23.788 18.284  1.00 17.81 ? 54  TYR   B CG  1 
ATOM   2778 C  CD1 . TYR   B 2 54  ? 46.787  -24.221 18.399  1.00 17.19 ? 54  TYR   B CD1 1 
ATOM   2779 C  CD2 . TYR   B 2 54  ? 48.451  -22.596 18.920  1.00 17.86 ? 54  TYR   B CD2 1 
ATOM   2780 C  CE1 . TYR   B 2 54  ? 45.855  -23.507 19.130  1.00 17.68 ? 54  TYR   B CE1 1 
ATOM   2781 C  CE2 . TYR   B 2 54  ? 47.517  -21.860 19.637  1.00 17.28 ? 54  TYR   B CE2 1 
ATOM   2782 C  CZ  . TYR   B 2 54  ? 46.216  -22.309 19.730  1.00 15.85 ? 54  TYR   B CZ  1 
ATOM   2783 O  OH  . TYR   B 2 54  ? 45.282  -21.621 20.436  1.00 16.52 ? 54  TYR   B OH  1 
ATOM   2784 N  N   . GLU   B 2 55  ? 51.330  -26.869 16.771  1.00 22.56 ? 55  GLU   B N   1 
ATOM   2785 C  CA  . GLU   B 2 55  ? 51.919  -27.862 15.889  1.00 24.05 ? 55  GLU   B CA  1 
ATOM   2786 C  C   . GLU   B 2 55  ? 51.787  -29.259 16.496  1.00 24.18 ? 55  GLU   B C   1 
ATOM   2787 O  O   . GLU   B 2 55  ? 51.502  -30.218 15.781  1.00 25.05 ? 55  GLU   B O   1 
ATOM   2788 C  CB  . GLU   B 2 55  ? 53.389  -27.580 15.594  1.00 28.42 ? 55  GLU   B CB  1 
ATOM   2789 C  CG  . GLU   B 2 55  ? 53.584  -26.356 14.737  1.00 32.34 ? 55  GLU   B CG  1 
ATOM   2790 C  CD  . GLU   B 2 55  ? 53.397  -25.045 15.480  1.00 34.64 ? 55  GLU   B CD  1 
ATOM   2791 O  OE1 . GLU   B 2 55  ? 53.409  -25.057 16.756  1.00 32.94 ? 55  GLU   B OE1 1 
ATOM   2792 O  OE2 . GLU   B 2 55  ? 53.217  -24.013 14.784  1.00 39.07 ? 55  GLU   B OE2 1 
ATOM   2793 N  N   . ASP   B 2 56  ? 51.967  -29.357 17.812  1.00 26.10 ? 56  ASP   B N   1 
ATOM   2794 C  CA  . ASP   B 2 56  ? 51.928  -30.625 18.530  1.00 29.16 ? 56  ASP   B CA  1 
ATOM   2795 C  C   . ASP   B 2 56  ? 50.507  -31.161 18.583  1.00 28.57 ? 56  ASP   B C   1 
ATOM   2796 O  O   . ASP   B 2 56  ? 50.283  -32.366 18.411  1.00 29.46 ? 56  ASP   B O   1 
ATOM   2797 C  CB  . ASP   B 2 56  ? 52.414  -30.436 19.968  1.00 34.44 ? 56  ASP   B CB  1 
ATOM   2798 C  CG  . ASP   B 2 56  ? 52.857  -31.686 20.711  1.00 44.33 ? 56  ASP   B CG  1 
ATOM   2799 O  OD1 . ASP   B 2 56  ? 52.059  -32.652 20.814  1.00 49.31 ? 56  ASP   B OD1 1 
ATOM   2800 O  OD2 . ASP   B 2 56  ? 54.004  -31.657 21.224  1.00 56.69 ? 56  ASP   B OD2 1 
ATOM   2801 N  N   . LEU   B 2 57  ? 49.556  -30.267 18.880  1.00 24.69 ? 57  LEU   B N   1 
ATOM   2802 C  CA  . LEU   B 2 57  ? 48.164  -30.654 19.017  1.00 23.91 ? 57  LEU   B CA  1 
ATOM   2803 C  C   . LEU   B 2 57  ? 47.601  -31.113 17.671  1.00 23.17 ? 57  LEU   B C   1 
ATOM   2804 O  O   . LEU   B 2 57  ? 46.754  -31.992 17.618  1.00 23.74 ? 57  LEU   B O   1 
ATOM   2805 C  CB  . LEU   B 2 57  ? 47.373  -29.457 19.545  1.00 25.59 ? 57  LEU   B CB  1 
ATOM   2806 C  CG  . LEU   B 2 57  ? 47.652  -29.057 20.989  1.00 25.99 ? 57  LEU   B CG  1 
ATOM   2807 C  CD1 . LEU   B 2 57  ? 46.935  -27.753 21.328  1.00 27.71 ? 57  LEU   B CD1 1 
ATOM   2808 C  CD2 . LEU   B 2 57  ? 47.208  -30.158 21.934  1.00 26.57 ? 57  LEU   B CD2 1 
ATOM   2809 N  N   . LEU   B 2 58  ? 48.042  -30.482 16.585  1.00 23.69 ? 58  LEU   B N   1 
ATOM   2810 C  CA  . LEU   B 2 58  ? 47.466  -30.728 15.275  1.00 24.68 ? 58  LEU   B CA  1 
ATOM   2811 C  C   . LEU   B 2 58  ? 47.986  -32.052 14.693  1.00 25.61 ? 58  LEU   B C   1 
ATOM   2812 O  O   . LEU   B 2 58  ? 47.268  -32.762 13.980  1.00 23.19 ? 58  LEU   B O   1 
ATOM   2813 C  CB  . LEU   B 2 58  ? 47.777  -29.529 14.374  1.00 23.66 ? 58  LEU   B CB  1 
ATOM   2814 C  CG  . LEU   B 2 58  ? 47.035  -29.550 13.052  1.00 26.85 ? 58  LEU   B CG  1 
ATOM   2815 C  CD1 . LEU   B 2 58  ? 45.534  -29.451 13.281  1.00 28.09 ? 58  LEU   B CD1 1 
ATOM   2816 C  CD2 . LEU   B 2 58  ? 47.531  -28.451 12.123  1.00 29.43 ? 58  LEU   B CD2 1 
ATOM   2817 N  N   . ILE   B 2 59  ? 49.226  -32.412 15.049  1.00 25.67 ? 59  ILE   B N   1 
ATOM   2818 C  CA  . ILE   B 2 59  ? 49.850  -33.652 14.599  1.00 27.81 ? 59  ILE   B CA  1 
ATOM   2819 C  C   . ILE   B 2 59  ? 49.102  -34.866 15.135  1.00 24.81 ? 59  ILE   B C   1 
ATOM   2820 O  O   . ILE   B 2 59  ? 49.053  -35.898 14.475  1.00 20.61 ? 59  ILE   B O   1 
ATOM   2821 C  CB  . ILE   B 2 59  ? 51.347  -33.649 14.987  1.00 30.77 ? 59  ILE   B CB  1 
ATOM   2822 C  CG1 . ILE   B 2 59  ? 52.139  -32.823 13.969  1.00 34.66 ? 59  ILE   B CG1 1 
ATOM   2823 C  CG2 . ILE   B 2 59  ? 51.916  -35.058 15.177  1.00 31.57 ? 59  ILE   B CG2 1 
ATOM   2824 C  CD1 . ILE   B 2 59  ? 52.057  -33.328 12.542  1.00 37.65 ? 59  ILE   B CD1 1 
ATOM   2825 N  N   . ARG   B 2 60  ? 48.500  -34.711 16.311  1.00 26.75 ? 60  ARG   B N   1 
ATOM   2826 C  CA  . ARG   B 2 60  ? 47.720  -35.760 16.944  1.00 29.02 ? 60  ARG   B CA  1 
ATOM   2827 C  C   . ARG   B 2 60  ? 46.299  -35.853 16.366  1.00 28.95 ? 60  ARG   B C   1 
ATOM   2828 O  O   . ARG   B 2 60  ? 45.518  -36.701 16.790  1.00 31.32 ? 60  ARG   B O   1 
ATOM   2829 C  CB  . ARG   B 2 60  ? 47.588  -35.453 18.439  1.00 33.37 ? 60  ARG   B CB  1 
ATOM   2830 C  CG  . ARG   B 2 60  ? 48.897  -35.153 19.155  1.00 44.50 ? 60  ARG   B CG  1 
ATOM   2831 C  CD  . ARG   B 2 60  ? 49.711  -36.384 19.482  1.00 53.16 ? 60  ARG   B CD  1 
ATOM   2832 N  NE  . ARG   B 2 60  ? 50.974  -36.003 20.099  1.00 65.54 ? 60  ARG   B NE  1 
ATOM   2833 C  CZ  . ARG   B 2 60  ? 51.937  -36.854 20.443  1.00 74.66 ? 60  ARG   B CZ  1 
ATOM   2834 N  NH1 . ARG   B 2 60  ? 51.773  -38.158 20.274  1.00 73.64 ? 60  ARG   B NH1 1 
ATOM   2835 N  NH2 . ARG   B 2 60  ? 53.063  -36.391 20.965  1.00 78.45 ? 60  ARG   B NH2 1 
ATOM   2836 N  N   . LYS   B 2 61  ? 45.905  -34.919 15.490  1.00 27.30 ? 61  LYS   B N   1 
ATOM   2837 C  CA  . LYS   B 2 61  ? 44.563  -34.920 14.913  1.00 26.20 ? 61  LYS   B CA  1 
ATOM   2838 C  C   . LYS   B 2 61  ? 44.589  -35.524 13.519  1.00 21.52 ? 61  LYS   B C   1 
ATOM   2839 O  O   . LYS   B 2 61  ? 45.582  -35.376 12.799  1.00 22.44 ? 61  LYS   B O   1 
ATOM   2840 C  CB  . LYS   B 2 61  ? 44.023  -33.493 14.790  1.00 27.53 ? 61  LYS   B CB  1 
ATOM   2841 C  CG  . LYS   B 2 61  ? 43.784  -32.777 16.113  1.00 30.88 ? 61  LYS   B CG  1 
ATOM   2842 C  CD  . LYS   B 2 61  ? 42.752  -33.393 17.029  1.00 30.56 ? 61  LYS   B CD  1 
ATOM   2843 C  CE  . LYS   B 2 61  ? 42.555  -32.569 18.286  1.00 35.36 ? 61  LYS   B CE  1 
ATOM   2844 N  NZ  . LYS   B 2 61  ? 43.779  -32.534 19.137  1.00 41.66 ? 61  LYS   B NZ  1 
ATOM   2845 N  N   . SER   B 2 62  ? 43.489  -36.182 13.157  1.00 18.27 ? 62  SER   B N   1 
ATOM   2846 C  CA  . SER   B 2 62  ? 43.213  -36.554 11.777  1.00 17.98 ? 62  SER   B CA  1 
ATOM   2847 C  C   . SER   B 2 62  ? 41.884  -35.915 11.352  1.00 16.38 ? 62  SER   B C   1 
ATOM   2848 O  O   . SER   B 2 62  ? 41.165  -35.362 12.179  1.00 17.13 ? 62  SER   B O   1 
ATOM   2849 C  CB  . SER   B 2 62  ? 43.169  -38.071 11.630  1.00 20.11 ? 62  SER   B CB  1 
ATOM   2850 O  OG  . SER   B 2 62  ? 41.931  -38.592 12.110  1.00 22.11 ? 62  SER   B OG  1 
ATOM   2851 N  N   . ASN   B 2 63  ? 41.524  -36.054 10.081  1.00 14.65 ? 63  ASN   B N   1 
ATOM   2852 C  CA  . ASN   B 2 63  ? 40.272  -35.524 9.563   1.00 15.77 ? 63  ASN   B CA  1 
ATOM   2853 C  C   . ASN   B 2 63  ? 39.067  -35.948 10.408  1.00 16.33 ? 63  ASN   B C   1 
ATOM   2854 O  O   . ASN   B 2 63  ? 38.150  -35.153 10.619  1.00 15.98 ? 63  ASN   B O   1 
ATOM   2855 C  CB  . ASN   B 2 63  ? 40.091  -36.005 8.128   1.00 15.79 ? 63  ASN   B CB  1 
ATOM   2856 C  CG  . ASN   B 2 63  ? 41.107  -35.397 7.185   1.00 15.89 ? 63  ASN   B CG  1 
ATOM   2857 O  OD1 . ASN   B 2 63  ? 41.671  -34.339 7.448   1.00 14.49 ? 63  ASN   B OD1 1 
ATOM   2858 N  ND2 . ASN   B 2 63  ? 41.340  -36.069 6.072   1.00 16.94 ? 63  ASN   B ND2 1 
ATOM   2859 N  N   . HIS   B 2 64  ? 39.101  -37.195 10.906  1.00 16.44 ? 64  HIS   B N   1 
ATOM   2860 C  CA  . HIS   B 2 64  ? 38.014  -37.822 11.642  1.00 20.70 ? 64  HIS   B CA  1 
ATOM   2861 C  C   . HIS   B 2 64  ? 37.728  -37.184 12.998  1.00 16.52 ? 64  HIS   B C   1 
ATOM   2862 O  O   . HIS   B 2 64  ? 36.710  -37.519 13.587  1.00 16.16 ? 64  HIS   B O   1 
ATOM   2863 C  CB  . HIS   B 2 64  ? 38.328  -39.305 11.931  1.00 27.23 ? 64  HIS   B CB  1 
ATOM   2864 C  CG  . HIS   B 2 64  ? 38.160  -40.180 10.754  1.00 33.80 ? 64  HIS   B CG  1 
ATOM   2865 N  ND1 . HIS   B 2 64  ? 38.372  -41.539 10.809  1.00 44.90 ? 64  HIS   B ND1 1 
ATOM   2866 C  CD2 . HIS   B 2 64  ? 37.801  -39.904 9.488   1.00 43.56 ? 64  HIS   B CD2 1 
ATOM   2867 C  CE1 . HIS   B 2 64  ? 38.150  -42.059 9.604   1.00 50.43 ? 64  HIS   B CE1 1 
ATOM   2868 N  NE2 . HIS   B 2 64  ? 37.816  -41.080 8.781   1.00 49.60 ? 64  HIS   B NE2 1 
ATOM   2869 N  N   . ASN   B 2 65  ? 38.637  -36.353 13.516  1.00 15.56 ? 65  ASN   B N   1 
ATOM   2870 C  CA  . ASN   B 2 65  ? 38.471  -35.727 14.821  1.00 16.08 ? 65  ASN   B CA  1 
ATOM   2871 C  C   . ASN   B 2 65  ? 37.656  -34.430 14.718  1.00 14.53 ? 65  ASN   B C   1 
ATOM   2872 O  O   . ASN   B 2 65  ? 37.349  -33.816 15.760  1.00 13.61 ? 65  ASN   B O   1 
ATOM   2873 C  CB  . ASN   B 2 65  ? 39.816  -35.395 15.480  1.00 17.19 ? 65  ASN   B CB  1 
ATOM   2874 C  CG  . ASN   B 2 65  ? 40.651  -36.622 15.772  1.00 19.89 ? 65  ASN   B CG  1 
ATOM   2875 O  OD1 . ASN   B 2 65  ? 41.798  -36.725 15.356  1.00 19.81 ? 65  ASN   B OD1 1 
ATOM   2876 N  ND2 . ASN   B 2 65  ? 40.083  -37.573 16.491  1.00 22.54 ? 65  ASN   B ND2 1 
ATOM   2877 N  N   . PHE   B 2 66  ? 37.352  -33.982 13.484  1.00 12.40 ? 66  PHE   B N   1 
ATOM   2878 C  CA  . PHE   B 2 66  ? 36.688  -32.697 13.306  1.00 11.72 ? 66  PHE   B CA  1 
ATOM   2879 C  C   . PHE   B 2 66  ? 35.215  -32.903 12.974  1.00 10.88 ? 66  PHE   B C   1 
ATOM   2880 O  O   . PHE   B 2 66  ? 34.886  -33.540 11.983  1.00 10.86 ? 66  PHE   B O   1 
ATOM   2881 C  CB  . PHE   B 2 66  ? 37.372  -31.880 12.210  1.00 12.18 ? 66  PHE   B CB  1 
ATOM   2882 C  CG  . PHE   B 2 66  ? 38.787  -31.518 12.543  1.00 13.25 ? 66  PHE   B CG  1 
ATOM   2883 C  CD1 . PHE   B 2 66  ? 39.068  -30.463 13.394  1.00 14.15 ? 66  PHE   B CD1 1 
ATOM   2884 C  CD2 . PHE   B 2 66  ? 39.836  -32.262 12.033  1.00 13.68 ? 66  PHE   B CD2 1 
ATOM   2885 C  CE1 . PHE   B 2 66  ? 40.382  -30.139 13.697  1.00 14.48 ? 66  PHE   B CE1 1 
ATOM   2886 C  CE2 . PHE   B 2 66  ? 41.146  -31.943 12.337  1.00 14.10 ? 66  PHE   B CE2 1 
ATOM   2887 C  CZ  . PHE   B 2 66  ? 41.415  -30.894 13.183  1.00 14.45 ? 66  PHE   B CZ  1 
ATOM   2888 N  N   . LEU   B 2 67  ? 34.320  -32.316 13.785  1.00 11.44 ? 67  LEU   B N   1 
ATOM   2889 C  CA  . LEU   B 2 67  ? 32.893  -32.340 13.475  1.00 11.13 ? 67  LEU   B CA  1 
ATOM   2890 C  C   . LEU   B 2 67  ? 32.476  -30.970 12.946  1.00 11.01 ? 67  LEU   B C   1 
ATOM   2891 O  O   . LEU   B 2 67  ? 32.496  -29.984 13.691  1.00 11.05 ? 67  LEU   B O   1 
ATOM   2892 C  CB  . LEU   B 2 67  ? 32.109  -32.702 14.743  1.00 11.82 ? 67  LEU   B CB  1 
ATOM   2893 C  CG  . LEU   B 2 67  ? 30.591  -32.642 14.617  1.00 11.41 ? 67  LEU   B CG  1 
ATOM   2894 C  CD1 . LEU   B 2 67  ? 30.101  -33.652 13.597  1.00 11.83 ? 67  LEU   B CD1 1 
ATOM   2895 C  CD2 . LEU   B 2 67  ? 29.930  -32.862 15.968  1.00 12.11 ? 67  LEU   B CD2 1 
ATOM   2896 N  N   . VAL   B 2 68  ? 32.125  -30.921 11.660  1.00 10.48 ? 68  VAL   B N   1 
ATOM   2897 C  CA  . VAL   B 2 68  ? 31.671  -29.699 11.016  1.00 10.66 ? 68  VAL   B CA  1 
ATOM   2898 C  C   . VAL   B 2 68  ? 30.186  -29.905 10.735  1.00 11.49 ? 68  VAL   B C   1 
ATOM   2899 O  O   . VAL   B 2 68  ? 29.794  -30.926 10.176  1.00 11.18 ? 68  VAL   B O   1 
ATOM   2900 C  CB  . VAL   B 2 68  ? 32.438  -29.376 9.707   1.00 11.26 ? 68  VAL   B CB  1 
ATOM   2901 C  CG1 . VAL   B 2 68  ? 31.873  -28.130 9.023   1.00 11.28 ? 68  VAL   B CG1 1 
ATOM   2902 C  CG2 . VAL   B 2 68  ? 33.947  -29.255 9.896   1.00 10.68 ? 68  VAL   B CG2 1 
ATOM   2903 N  N   . GLN   B 2 69  ? 29.375  -28.911 11.108  1.00 12.49 ? 69  GLN   B N   1 
ATOM   2904 C  CA  . GLN   B 2 69  ? 27.927  -28.992 10.994  1.00 13.12 ? 69  GLN   B CA  1 
ATOM   2905 C  C   . GLN   B 2 69  ? 27.342  -27.686 10.461  1.00 12.65 ? 69  GLN   B C   1 
ATOM   2906 O  O   . GLN   B 2 69  ? 27.591  -26.615 11.013  1.00 11.40 ? 69  GLN   B O   1 
ATOM   2907 C  CB  . GLN   B 2 69  ? 27.350  -29.286 12.379  1.00 13.99 ? 69  GLN   B CB  1 
ATOM   2908 C  CG  . GLN   B 2 69  ? 27.755  -30.652 12.897  1.00 15.27 ? 69  GLN   B CG  1 
ATOM   2909 C  CD  . GLN   B 2 69  ? 27.233  -30.882 14.294  1.00 16.95 ? 69  GLN   B CD  1 
ATOM   2910 O  OE1 . GLN   B 2 69  ? 27.618  -30.200 15.239  1.00 18.58 ? 69  GLN   B OE1 1 
ATOM   2911 N  NE2 . GLN   B 2 69  ? 26.312  -31.813 14.409  1.00 17.34 ? 69  GLN   B NE2 1 
ATOM   2912 N  N   . ALA   B 2 70  ? 26.565  -27.809 9.386   1.00 13.13 ? 70  ALA   B N   1 
ATOM   2913 C  CA  . ALA   B 2 70  ? 25.706  -26.749 8.878   1.00 14.84 ? 70  ALA   B CA  1 
ATOM   2914 C  C   . ALA   B 2 70  ? 24.305  -27.011 9.427   1.00 15.81 ? 70  ALA   B C   1 
ATOM   2915 O  O   . ALA   B 2 70  ? 23.628  -27.946 8.990   1.00 14.80 ? 70  ALA   B O   1 
ATOM   2916 C  CB  . ALA   B 2 70  ? 25.726  -26.793 7.360   1.00 16.35 ? 70  ALA   B CB  1 
ATOM   2917 N  N   . GLY   B 2 71  ? 23.928  -26.278 10.476  1.00 16.80 ? 71  GLY   B N   1 
ATOM   2918 C  CA  . GLY   B 2 71  ? 22.785  -26.681 11.283  1.00 18.41 ? 71  GLY   B CA  1 
ATOM   2919 C  C   . GLY   B 2 71  ? 23.068  -28.029 11.948  1.00 19.60 ? 71  GLY   B C   1 
ATOM   2920 O  O   . GLY   B 2 71  ? 24.061  -28.151 12.656  1.00 20.12 ? 71  GLY   B O   1 
ATOM   2921 N  N   . ASN   B 2 72  ? 22.247  -29.055 11.684  1.00 20.40 ? 72  ASN   B N   1 
ATOM   2922 C  CA  . ASN   B 2 72  ? 22.517  -30.396 12.206  1.00 21.98 ? 72  ASN   B CA  1 
ATOM   2923 C  C   . ASN   B 2 72  ? 23.087  -31.343 11.142  1.00 20.10 ? 72  ASN   B C   1 
ATOM   2924 O  O   . ASN   B 2 72  ? 23.340  -32.527 11.401  1.00 18.77 ? 72  ASN   B O   1 
ATOM   2925 C  CB  . ASN   B 2 72  ? 21.261  -31.017 12.804  1.00 28.04 ? 72  ASN   B CB  1 
ATOM   2926 C  CG  . ASN   B 2 72  ? 20.907  -30.400 14.139  1.00 32.61 ? 72  ASN   B CG  1 
ATOM   2927 O  OD1 . ASN   B 2 72  ? 21.783  -29.990 14.908  1.00 36.90 ? 72  ASN   B OD1 1 
ATOM   2928 N  ND2 . ASN   B 2 72  ? 19.618  -30.296 14.398  1.00 36.43 ? 72  ASN   B ND2 1 
ATOM   2929 N  N   . VAL   B 2 73  ? 23.400  -30.802 9.964   1.00 17.32 ? 73  VAL   B N   1 
ATOM   2930 C  CA  . VAL   B 2 73  ? 23.946  -31.610 8.893   1.00 15.93 ? 73  VAL   B CA  1 
ATOM   2931 C  C   . VAL   B 2 73  ? 25.471  -31.621 8.998   1.00 14.78 ? 73  VAL   B C   1 
ATOM   2932 O  O   . VAL   B 2 73  ? 26.139  -30.601 8.904   1.00 13.12 ? 73  VAL   B O   1 
ATOM   2933 C  CB  . VAL   B 2 73  ? 23.446  -31.078 7.540   1.00 17.14 ? 73  VAL   B CB  1 
ATOM   2934 C  CG1 . VAL   B 2 73  ? 24.070  -31.824 6.380   1.00 17.01 ? 73  VAL   B CG1 1 
ATOM   2935 C  CG2 . VAL   B 2 73  ? 21.923  -31.114 7.479   1.00 18.00 ? 73  VAL   B CG2 1 
ATOM   2936 N  N   . GLN   B 2 74  ? 26.031  -32.806 9.154   1.00 13.66 ? 74  GLN   B N   1 
ATOM   2937 C  CA  . GLN   B 2 74  ? 27.475  -32.964 9.188   1.00 15.14 ? 74  GLN   B CA  1 
ATOM   2938 C  C   . GLN   B 2 74  ? 28.079  -32.809 7.786   1.00 13.96 ? 74  GLN   B C   1 
ATOM   2939 O  O   . GLN   B 2 74  ? 27.578  -33.379 6.845   1.00 14.40 ? 74  GLN   B O   1 
ATOM   2940 C  CB  . GLN   B 2 74  ? 27.835  -34.332 9.768   1.00 14.77 ? 74  GLN   B CB  1 
ATOM   2941 C  CG  . GLN   B 2 74  ? 29.335  -34.543 9.802   1.00 17.20 ? 74  GLN   B CG  1 
ATOM   2942 C  CD  . GLN   B 2 74  ? 29.754  -35.807 10.505  1.00 18.80 ? 74  GLN   B CD  1 
ATOM   2943 O  OE1 . GLN   B 2 74  ? 28.933  -36.653 10.818  1.00 20.70 ? 74  GLN   B OE1 1 
ATOM   2944 N  NE2 . GLN   B 2 74  ? 31.051  -35.958 10.708  1.00 20.36 ? 74  GLN   B NE2 1 
ATOM   2945 N  N   . LEU   B 2 75  ? 29.168  -32.051 7.672   1.00 14.59 ? 75  LEU   B N   1 
ATOM   2946 C  CA  . LEU   B 2 75  ? 29.989  -31.983 6.470   1.00 15.10 ? 75  LEU   B CA  1 
ATOM   2947 C  C   . LEU   B 2 75  ? 31.269  -32.776 6.714   1.00 14.29 ? 75  LEU   B C   1 
ATOM   2948 O  O   . LEU   B 2 75  ? 32.056  -32.453 7.606   1.00 15.23 ? 75  LEU   B O   1 
ATOM   2949 C  CB  . LEU   B 2 75  ? 30.356  -30.527 6.173   1.00 15.96 ? 75  LEU   B CB  1 
ATOM   2950 C  CG  . LEU   B 2 75  ? 29.210  -29.544 5.982   1.00 18.21 ? 75  LEU   B CG  1 
ATOM   2951 C  CD1 . LEU   B 2 75  ? 29.774  -28.159 5.644   1.00 18.60 ? 75  LEU   B CD1 1 
ATOM   2952 C  CD2 . LEU   B 2 75  ? 28.231  -30.052 4.911   1.00 19.27 ? 75  LEU   B CD2 1 
ATOM   2953 N  N   . ARG   B 2 76  ? 31.518  -33.767 5.873   1.00 14.99 ? 76  ARG   B N   1 
ATOM   2954 C  CA  . ARG   B 2 76  ? 32.641  -34.663 6.076   1.00 15.89 ? 76  ARG   B CA  1 
ATOM   2955 C  C   . ARG   B 2 76  ? 33.950  -33.958 5.724   1.00 14.78 ? 76  ARG   B C   1 
ATOM   2956 O  O   . ARG   B 2 76  ? 34.113  -33.456 4.610   1.00 14.61 ? 76  ARG   B O   1 
ATOM   2957 C  CB  . ARG   B 2 76  ? 32.437  -35.932 5.243   1.00 18.28 ? 76  ARG   B CB  1 
ATOM   2958 C  CG  . ARG   B 2 76  ? 33.623  -36.888 5.262   1.00 20.85 ? 76  ARG   B CG  1 
ATOM   2959 C  CD  . ARG   B 2 76  ? 33.332  -38.205 4.530   1.00 24.04 ? 76  ARG   B CD  1 
ATOM   2960 N  NE  . ARG   B 2 76  ? 33.404  -38.001 3.076   1.00 25.24 ? 76  ARG   B NE  1 
ATOM   2961 C  CZ  . ARG   B 2 76  ? 34.418  -38.354 2.291   1.00 27.50 ? 76  ARG   B CZ  1 
ATOM   2962 N  NH1 . ARG   B 2 76  ? 35.384  -39.137 2.751   1.00 27.48 ? 76  ARG   B NH1 1 
ATOM   2963 N  NH2 . ARG   B 2 76  ? 34.454  -37.917 1.037   1.00 28.06 ? 76  ARG   B NH2 1 
ATOM   2964 N  N   . VAL   B 2 77  ? 34.904  -33.990 6.658   1.00 12.96 ? 77  VAL   B N   1 
ATOM   2965 C  CA  . VAL   B 2 77  ? 36.201  -33.373 6.478   1.00 12.96 ? 77  VAL   B CA  1 
ATOM   2966 C  C   . VAL   B 2 77  ? 37.118  -34.350 5.744   1.00 13.76 ? 77  VAL   B C   1 
ATOM   2967 O  O   . VAL   B 2 77  ? 37.215  -35.504 6.169   1.00 14.48 ? 77  VAL   B O   1 
ATOM   2968 C  CB  . VAL   B 2 77  ? 36.763  -32.977 7.849   1.00 12.80 ? 77  VAL   B CB  1 
ATOM   2969 C  CG1 . VAL   B 2 77  ? 38.216  -32.511 7.778   1.00 12.21 ? 77  VAL   B CG1 1 
ATOM   2970 C  CG2 . VAL   B 2 77  ? 35.872  -31.921 8.492   1.00 12.04 ? 77  VAL   B CG2 1 
ATOM   2971 N  N   . ILE   B 2 78  ? 37.761  -33.900 4.655   1.00 12.79 ? 78  ILE   B N   1 
ATOM   2972 C  CA  . ILE   B 2 78  ? 38.630  -34.772 3.867   1.00 12.93 ? 78  ILE   B CA  1 
ATOM   2973 C  C   . ILE   B 2 78  ? 40.074  -34.253 3.838   1.00 13.75 ? 78  ILE   B C   1 
ATOM   2974 O  O   . ILE   B 2 78  ? 40.931  -34.868 3.189   1.00 12.78 ? 78  ILE   B O   1 
ATOM   2975 C  CB  . ILE   B 2 78  ? 38.073  -34.976 2.446   1.00 12.74 ? 78  ILE   B CB  1 
ATOM   2976 C  CG1 . ILE   B 2 78  ? 37.912  -33.648 1.702   1.00 13.41 ? 78  ILE   B CG1 1 
ATOM   2977 C  CG2 . ILE   B 2 78  ? 36.758  -35.753 2.482   1.00 12.58 ? 78  ILE   B CG2 1 
ATOM   2978 C  CD1 . ILE   B 2 78  ? 37.573  -33.782 0.215   1.00 13.65 ? 78  ILE   B CD1 1 
ATOM   2979 N  N   . GLY   B 2 79  ? 40.344  -33.114 4.495   1.00 12.60 ? 79  GLY   B N   1 
ATOM   2980 C  CA  . GLY   B 2 79  ? 41.698  -32.577 4.589   1.00 12.69 ? 79  GLY   B CA  1 
ATOM   2981 C  C   . GLY   B 2 79  ? 41.756  -31.513 5.689   1.00 13.82 ? 79  GLY   B C   1 
ATOM   2982 O  O   . GLY   B 2 79  ? 40.723  -30.985 6.080   1.00 12.90 ? 79  GLY   B O   1 
ATOM   2983 N  N   . HIS   B 2 80  ? 42.945  -31.261 6.242   1.00 13.36 ? 80  HIS   B N   1 
ATOM   2984 C  CA  . HIS   B 2 80  ? 43.083  -30.235 7.258   1.00 14.62 ? 80  HIS   B CA  1 
ATOM   2985 C  C   . HIS   B 2 80  ? 44.488  -29.661 7.197   1.00 15.28 ? 80  HIS   B C   1 
ATOM   2986 O  O   . HIS   B 2 80  ? 45.446  -30.381 6.931   1.00 15.03 ? 80  HIS   B O   1 
ATOM   2987 C  CB  . HIS   B 2 80  ? 42.792  -30.778 8.663   1.00 15.12 ? 80  HIS   B CB  1 
ATOM   2988 C  CG  . HIS   B 2 80  ? 43.756  -31.796 9.144   1.00 15.24 ? 80  HIS   B CG  1 
ATOM   2989 N  ND1 . HIS   B 2 80  ? 43.660  -33.123 8.771   1.00 16.84 ? 80  HIS   B ND1 1 
ATOM   2990 C  CD2 . HIS   B 2 80  ? 44.791  -31.705 10.001  1.00 16.00 ? 80  HIS   B CD2 1 
ATOM   2991 C  CE1 . HIS   B 2 80  ? 44.625  -33.801 9.394   1.00 17.82 ? 80  HIS   B CE1 1 
ATOM   2992 N  NE2 . HIS   B 2 80  ? 45.339  -32.958 10.129  1.00 16.98 ? 80  HIS   B NE2 1 
ATOM   2993 N  N   . SER   B 2 81  ? 44.592  -28.357 7.419   1.00 16.41 ? 81  SER   B N   1 
ATOM   2994 C  CA  . SER   B 2 81  ? 45.883  -27.717 7.600   1.00 17.35 ? 81  SER   B CA  1 
ATOM   2995 C  C   . SER   B 2 81  ? 45.687  -26.460 8.440   1.00 19.68 ? 81  SER   B C   1 
ATOM   2996 O  O   . SER   B 2 81  ? 44.555  -26.094 8.794   1.00 17.39 ? 81  SER   B O   1 
ATOM   2997 C  CB  . SER   B 2 81  ? 46.506  -27.396 6.278   1.00 17.73 ? 81  SER   B CB  1 
ATOM   2998 O  OG  . SER   B 2 81  ? 45.675  -26.507 5.543   1.00 20.04 ? 81  SER   B OG  1 
ATOM   2999 N  N   . MET   B 2 82  ? 46.814  -25.825 8.778   1.00 18.44 ? 82  MET   B N   1 
ATOM   3000 C  CA  . MET   B 2 82  ? 46.797  -24.676 9.655   1.00 19.53 ? 82  MET   B CA  1 
ATOM   3001 C  C   . MET   B 2 82  ? 47.610  -23.596 8.959   1.00 20.26 ? 82  MET   B C   1 
ATOM   3002 O  O   . MET   B 2 82  ? 48.650  -23.888 8.371   1.00 19.16 ? 82  MET   B O   1 
ATOM   3003 C  CB  . MET   B 2 82  ? 47.351  -25.096 11.017  1.00 20.30 ? 82  MET   B CB  1 
ATOM   3004 C  CG  . MET   B 2 82  ? 47.817  -23.995 11.900  1.00 21.30 ? 82  MET   B CG  1 
ATOM   3005 S  SD  . MET   B 2 82  ? 48.166  -24.625 13.558  1.00 23.60 ? 82  MET   B SD  1 
ATOM   3006 C  CE  . MET   B 2 82  ? 49.873  -25.159 13.336  1.00 23.79 ? 82  MET   B CE  1 
ATOM   3007 N  N   . GLN   B 2 83  ? 47.030  -22.399 8.856   1.00 20.06 ? 83  GLN   B N   1 
ATOM   3008 C  CA  . GLN   B 2 83  ? 47.714  -21.246 8.296   1.00 18.40 ? 83  GLN   B CA  1 
ATOM   3009 C  C   . GLN   B 2 83  ? 47.658  -20.163 9.370   1.00 17.45 ? 83  GLN   B C   1 
ATOM   3010 O  O   . GLN   B 2 83  ? 46.591  -19.634 9.669   1.00 16.77 ? 83  GLN   B O   1 
ATOM   3011 C  CB  . GLN   B 2 83  ? 47.050  -20.808 6.983   1.00 19.70 ? 83  GLN   B CB  1 
ATOM   3012 C  CG  . GLN   B 2 83  ? 47.627  -19.540 6.370   1.00 20.02 ? 83  GLN   B CG  1 
ATOM   3013 C  CD  . GLN   B 2 83  ? 46.877  -19.099 5.140   1.00 21.62 ? 83  GLN   B CD  1 
ATOM   3014 O  OE1 . GLN   B 2 83  ? 45.832  -19.632 4.794   1.00 24.46 ? 83  GLN   B OE1 1 
ATOM   3015 N  NE2 . GLN   B 2 83  ? 47.418  -18.125 4.435   1.00 23.05 ? 83  GLN   B NE2 1 
ATOM   3016 N  N   . ASN   B 2 84  ? 48.820  -19.877 9.966   1.00 16.04 ? 84  ASN   B N   1 
ATOM   3017 C  CA  . ASN   B 2 84  ? 48.925  -18.961 11.082  1.00 14.98 ? 84  ASN   B CA  1 
ATOM   3018 C  C   . ASN   B 2 84  ? 47.945  -19.423 12.147  1.00 14.58 ? 84  ASN   B C   1 
ATOM   3019 O  O   . ASN   B 2 84  ? 48.030  -20.582 12.550  1.00 15.40 ? 84  ASN   B O   1 
ATOM   3020 C  CB  . ASN   B 2 84  ? 48.772  -17.516 10.605  1.00 14.35 ? 84  ASN   B CB  1 
ATOM   3021 C  CG  . ASN   B 2 84  ? 49.760  -17.187 9.506   1.00 15.19 ? 84  ASN   B CG  1 
ATOM   3022 O  OD1 . ASN   B 2 84  ? 50.953  -17.360 9.673   1.00 16.28 ? 84  ASN   B OD1 1 
ATOM   3023 N  ND2 . ASN   B 2 84  ? 49.295  -16.729 8.358   1.00 15.19 ? 84  ASN   B ND2 1 
ATOM   3024 N  N   . CYS   B 2 85  ? 47.004  -18.557 12.579  1.00 13.63 ? 85  CYS   B N   1 
ATOM   3025 C  CA  . CYS   B 2 85  ? 46.077  -18.911 13.646  1.00 13.27 ? 85  CYS   B CA  1 
ATOM   3026 C  C   . CYS   B 2 85  ? 44.735  -19.471 13.161  1.00 13.28 ? 85  CYS   B C   1 
ATOM   3027 O  O   . CYS   B 2 85  ? 43.843  -19.671 13.974  1.00 13.55 ? 85  CYS   B O   1 
ATOM   3028 C  CB  . CYS   B 2 85  ? 45.842  -17.715 14.541  1.00 15.33 ? 85  CYS   B CB  1 
ATOM   3029 S  SG  . CYS   B 2 85  ? 47.379  -17.126 15.299  1.00 17.88 ? 85  CYS   B SG  1 
ATOM   3030 N  N   . VAL   B 2 86  ? 44.572  -19.725 11.852  1.00 14.52 ? 86  VAL   B N   1 
ATOM   3031 C  CA  . VAL   B 2 86  ? 43.328  -20.306 11.345  1.00 14.99 ? 86  VAL   B CA  1 
ATOM   3032 C  C   . VAL   B 2 86  ? 43.561  -21.747 10.870  1.00 15.24 ? 86  VAL   B C   1 
ATOM   3033 O  O   . VAL   B 2 86  ? 44.558  -22.104 10.250  1.00 14.27 ? 86  VAL   B O   1 
ATOM   3034 C  CB  . VAL   B 2 86  ? 42.636  -19.476 10.238  1.00 15.36 ? 86  VAL   B CB  1 
ATOM   3035 C  CG1 . VAL   B 2 86  ? 42.151  -18.126 10.750  1.00 15.09 ? 86  VAL   B CG1 1 
ATOM   3036 C  CG2 . VAL   B 2 86  ? 43.506  -19.270 9.013   1.00 17.55 ? 86  VAL   B CG2 1 
ATOM   3037 N  N   . LEU   B 2 87  ? 42.566  -22.569 11.166  1.00 14.52 ? 87  LEU   B N   1 
ATOM   3038 C  CA  . LEU   B 2 87  ? 42.464  -23.922 10.691  1.00 13.98 ? 87  LEU   B CA  1 
ATOM   3039 C  C   . LEU   B 2 87  ? 41.646  -23.916 9.401   1.00 13.80 ? 87  LEU   B C   1 
ATOM   3040 O  O   . LEU   B 2 87  ? 40.646  -23.211 9.292   1.00 12.37 ? 87  LEU   B O   1 
ATOM   3041 C  CB  . LEU   B 2 87  ? 41.801  -24.694 11.824  1.00 15.68 ? 87  LEU   B CB  1 
ATOM   3042 C  CG  . LEU   B 2 87  ? 41.710  -26.199 11.679  1.00 18.52 ? 87  LEU   B CG  1 
ATOM   3043 C  CD1 . LEU   B 2 87  ? 43.081  -26.826 11.809  1.00 19.96 ? 87  LEU   B CD1 1 
ATOM   3044 C  CD2 . LEU   B 2 87  ? 40.770  -26.754 12.746  1.00 18.60 ? 87  LEU   B CD2 1 
ATOM   3045 N  N   . LYS   B 2 88  ? 42.132  -24.637 8.392   1.00 12.54 ? 88  LYS   B N   1 
ATOM   3046 C  CA  . LYS   B 2 88  ? 41.396  -24.811 7.161   1.00 13.48 ? 88  LYS   B CA  1 
ATOM   3047 C  C   . LYS   B 2 88  ? 41.030  -26.286 7.009   1.00 13.40 ? 88  LYS   B C   1 
ATOM   3048 O  O   . LYS   B 2 88  ? 41.921  -27.136 6.960   1.00 12.20 ? 88  LYS   B O   1 
ATOM   3049 C  CB  . LYS   B 2 88  ? 42.224  -24.292 5.992   1.00 14.58 ? 88  LYS   B CB  1 
ATOM   3050 C  CG  . LYS   B 2 88  ? 42.581  -22.825 6.117   1.00 15.89 ? 88  LYS   B CG  1 
ATOM   3051 C  CD  . LYS   B 2 88  ? 43.273  -22.269 4.868   1.00 19.54 ? 88  LYS   B CD  1 
ATOM   3052 C  CE  . LYS   B 2 88  ? 44.654  -22.833 4.648   1.00 21.58 ? 88  LYS   B CE  1 
ATOM   3053 N  NZ  . LYS   B 2 88  ? 45.394  -22.088 3.590   1.00 23.85 ? 88  LYS   B NZ  1 
ATOM   3054 N  N   . LEU   B 2 89  ? 39.715  -26.566 7.017   1.00 11.65 ? 89  LEU   B N   1 
ATOM   3055 C  CA  . LEU   B 2 89  ? 39.221  -27.922 6.891   1.00 12.53 ? 89  LEU   B CA  1 
ATOM   3056 C  C   . LEU   B 2 89  ? 38.586  -28.088 5.519   1.00 12.70 ? 89  LEU   B C   1 
ATOM   3057 O  O   . LEU   B 2 89  ? 37.558  -27.479 5.219   1.00 12.24 ? 89  LEU   B O   1 
ATOM   3058 C  CB  . LEU   B 2 89  ? 38.196  -28.181 7.998   1.00 13.14 ? 89  LEU   B CB  1 
ATOM   3059 C  CG  . LEU   B 2 89  ? 38.707  -28.001 9.429   1.00 13.17 ? 89  LEU   B CG  1 
ATOM   3060 C  CD1 . LEU   B 2 89  ? 37.613  -28.276 10.412  1.00 13.22 ? 89  LEU   B CD1 1 
ATOM   3061 C  CD2 . LEU   B 2 89  ? 39.877  -28.922 9.722   1.00 14.26 ? 89  LEU   B CD2 1 
ATOM   3062 N  N   . LYS   B 2 90  ? 39.212  -28.911 4.687   1.00 13.23 ? 90  LYS   B N   1 
ATOM   3063 C  CA  . LYS   B 2 90  ? 38.632  -29.258 3.401   1.00 14.13 ? 90  LYS   B CA  1 
ATOM   3064 C  C   . LYS   B 2 90  ? 37.478  -30.225 3.650   1.00 13.22 ? 90  LYS   B C   1 
ATOM   3065 O  O   . LYS   B 2 90  ? 37.662  -31.203 4.364   1.00 11.92 ? 90  LYS   B O   1 
ATOM   3066 C  CB  . LYS   B 2 90  ? 39.690  -29.883 2.494   1.00 15.43 ? 90  LYS   B CB  1 
ATOM   3067 C  CG  . LYS   B 2 90  ? 39.270  -30.002 1.043   1.00 17.98 ? 90  LYS   B CG  1 
ATOM   3068 C  CD  . LYS   B 2 90  ? 40.298  -30.701 0.210   1.00 21.28 ? 90  LYS   B CD  1 
ATOM   3069 C  CE  . LYS   B 2 90  ? 39.875  -30.726 -1.236  1.00 25.75 ? 90  LYS   B CE  1 
ATOM   3070 N  NZ  . LYS   B 2 90  ? 40.944  -31.293 -2.080  1.00 29.33 ? 90  LYS   B NZ  1 
ATOM   3071 N  N   . VAL   B 2 91  ? 36.309  -29.922 3.070   1.00 12.36 ? 91  VAL   B N   1 
ATOM   3072 C  CA  . VAL   B 2 91  ? 35.131  -30.783 3.206   1.00 12.39 ? 91  VAL   B CA  1 
ATOM   3073 C  C   . VAL   B 2 91  ? 34.740  -31.334 1.831   1.00 12.68 ? 91  VAL   B C   1 
ATOM   3074 O  O   . VAL   B 2 91  ? 35.188  -30.814 0.820   1.00 12.62 ? 91  VAL   B O   1 
ATOM   3075 C  CB  . VAL   B 2 91  ? 33.965  -30.031 3.872   1.00 10.95 ? 91  VAL   B CB  1 
ATOM   3076 C  CG1 . VAL   B 2 91  ? 34.270  -29.736 5.319   1.00 11.64 ? 91  VAL   B CG1 1 
ATOM   3077 C  CG2 . VAL   B 2 91  ? 33.599  -28.751 3.132   1.00 10.65 ? 91  VAL   B CG2 1 
ATOM   3078 N  N   . ASP   B 2 92  ? 33.864  -32.345 1.783   1.00 13.20 ? 92  ASP   B N   1 
ATOM   3079 C  CA  . ASP   B 2 92  ? 33.551  -33.003 0.518   1.00 14.33 ? 92  ASP   B CA  1 
ATOM   3080 C  C   . ASP   B 2 92  ? 32.419  -32.319 -0.265  1.00 13.91 ? 92  ASP   B C   1 
ATOM   3081 O  O   . ASP   B 2 92  ? 32.017  -32.824 -1.316  1.00 13.38 ? 92  ASP   B O   1 
ATOM   3082 C  CB  . ASP   B 2 92  ? 33.252  -34.488 0.753   1.00 16.27 ? 92  ASP   B CB  1 
ATOM   3083 C  CG  . ASP   B 2 92  ? 31.956  -34.802 1.491   1.00 17.96 ? 92  ASP   B CG  1 
ATOM   3084 O  OD1 . ASP   B 2 92  ? 31.231  -33.855 1.918   1.00 19.55 ? 92  ASP   B OD1 1 
ATOM   3085 O  OD2 . ASP   B 2 92  ? 31.679  -36.000 1.638   1.00 19.90 ? 92  ASP   B OD2 1 
ATOM   3086 N  N   . THR   B 2 93  ? 31.904  -31.174 0.231   1.00 12.52 ? 93  THR   B N   1 
ATOM   3087 C  CA  . THR   B 2 93  ? 30.794  -30.466 -0.382  1.00 11.65 ? 93  THR   B CA  1 
ATOM   3088 C  C   . THR   B 2 93  ? 31.124  -28.989 -0.561  1.00 10.54 ? 93  THR   B C   1 
ATOM   3089 O  O   . THR   B 2 93  ? 31.516  -28.322 0.395   1.00 9.28  ? 93  THR   B O   1 
ATOM   3090 C  CB  . THR   B 2 93  ? 29.558  -30.593 0.519   1.00 11.91 ? 93  THR   B CB  1 
ATOM   3091 O  OG1 . THR   B 2 93  ? 29.307  -31.971 0.738   1.00 12.34 ? 93  THR   B OG1 1 
ATOM   3092 C  CG2 . THR   B 2 93  ? 28.314  -29.977 -0.060  1.00 12.46 ? 93  THR   B CG2 1 
ATOM   3093 N  N   . ALA   B 2 94  ? 30.952  -28.489 -1.789  1.00 10.56 ? 94  ALA   B N   1 
ATOM   3094 C  CA  . ALA   B 2 94  ? 31.129  -27.078 -2.084  1.00 10.65 ? 94  ALA   B CA  1 
ATOM   3095 C  C   . ALA   B 2 94  ? 29.860  -26.341 -1.677  1.00 10.98 ? 94  ALA   B C   1 
ATOM   3096 O  O   . ALA   B 2 94  ? 28.760  -26.748 -2.058  1.00 11.67 ? 94  ALA   B O   1 
ATOM   3097 C  CB  . ALA   B 2 94  ? 31.440  -26.823 -3.550  1.00 10.50 ? 94  ALA   B CB  1 
ATOM   3098 N  N   . ASN   B 2 95  ? 30.022  -25.288 -0.866  1.00 10.78 ? 95  ASN   B N   1 
ATOM   3099 C  CA  . ASN   B 2 95  ? 28.884  -24.561 -0.337  1.00 10.74 ? 95  ASN   B CA  1 
ATOM   3100 C  C   . ASN   B 2 95  ? 28.152  -23.889 -1.490  1.00 10.81 ? 95  ASN   B C   1 
ATOM   3101 O  O   . ASN   B 2 95  ? 28.692  -22.977 -2.116  1.00 11.32 ? 95  ASN   B O   1 
ATOM   3102 C  CB  . ASN   B 2 95  ? 29.282  -23.516 0.716   1.00 10.57 ? 95  ASN   B CB  1 
ATOM   3103 C  CG  . ASN   B 2 95  ? 28.100  -22.779 1.329   1.00 11.41 ? 95  ASN   B CG  1 
ATOM   3104 O  OD1 . ASN   B 2 95  ? 26.938  -23.056 1.004   1.00 9.95  ? 95  ASN   B OD1 1 
ATOM   3105 N  ND2 . ASN   B 2 95  ? 28.388  -21.843 2.235   1.00 12.00 ? 95  ASN   B ND2 1 
ATOM   3106 N  N   . PRO   B 2 96  ? 26.894  -24.270 -1.787  1.00 11.25 ? 96  PRO   B N   1 
ATOM   3107 C  CA  . PRO   B 2 96  ? 26.164  -23.680 -2.907  1.00 11.54 ? 96  PRO   B CA  1 
ATOM   3108 C  C   . PRO   B 2 96  ? 25.812  -22.212 -2.655  1.00 12.53 ? 96  PRO   B C   1 
ATOM   3109 O  O   . PRO   B 2 96  ? 25.464  -21.525 -3.602  1.00 12.26 ? 96  PRO   B O   1 
ATOM   3110 C  CB  . PRO   B 2 96  ? 24.884  -24.550 -3.023  1.00 11.23 ? 96  PRO   B CB  1 
ATOM   3111 C  CG  . PRO   B 2 96  ? 25.161  -25.761 -2.188  1.00 11.61 ? 96  PRO   B CG  1 
ATOM   3112 C  CD  . PRO   B 2 96  ? 26.095  -25.294 -1.092  1.00 11.59 ? 96  PRO   B CD  1 
ATOM   3113 N  N   . LYS   B 2 97  ? 25.889  -21.762 -1.382  1.00 13.06 ? 97  LYS   B N   1 
ATOM   3114 C  CA  . LYS   B 2 97  ? 25.579  -20.385 -1.005  1.00 15.29 ? 97  LYS   B CA  1 
ATOM   3115 C  C   . LYS   B 2 97  ? 26.839  -19.510 -0.965  1.00 13.58 ? 97  LYS   B C   1 
ATOM   3116 O  O   . LYS   B 2 97  ? 26.765  -18.357 -0.580  1.00 13.12 ? 97  LYS   B O   1 
ATOM   3117 C  CB  . LYS   B 2 97  ? 24.880  -20.315 0.359   1.00 17.47 ? 97  LYS   B CB  1 
ATOM   3118 C  CG  . LYS   B 2 97  ? 23.567  -21.077 0.469   1.00 22.40 ? 97  LYS   B CG  1 
ATOM   3119 C  CD  . LYS   B 2 97  ? 22.454  -20.446 -0.322  1.00 28.65 ? 97  LYS   B CD  1 
ATOM   3120 C  CE  . LYS   B 2 97  ? 21.106  -21.127 -0.159  1.00 29.55 ? 97  LYS   B CE  1 
ATOM   3121 N  NZ  . LYS   B 2 97  ? 21.022  -22.368 -0.974  1.00 29.63 ? 97  LYS   B NZ  1 
ATOM   3122 N  N   . THR   B 2 98  ? 27.976  -20.032 -1.431  1.00 13.16 ? 98  THR   B N   1 
ATOM   3123 C  CA  . THR   B 2 98  ? 29.205  -19.267 -1.448  1.00 13.18 ? 98  THR   B CA  1 
ATOM   3124 C  C   . THR   B 2 98  ? 28.993  -18.001 -2.265  1.00 12.84 ? 98  THR   B C   1 
ATOM   3125 O  O   . THR   B 2 98  ? 28.600  -18.084 -3.418  1.00 13.17 ? 98  THR   B O   1 
ATOM   3126 C  CB  . THR   B 2 98  ? 30.377  -20.045 -2.057  1.00 13.16 ? 98  THR   B CB  1 
ATOM   3127 O  OG1 . THR   B 2 98  ? 30.578  -21.277 -1.362  1.00 11.64 ? 98  THR   B OG1 1 
ATOM   3128 C  CG2 . THR   B 2 98  ? 31.648  -19.218 -2.033  1.00 13.12 ? 98  THR   B CG2 1 
ATOM   3129 N  N   . PRO   B 2 99  ? 29.225  -16.794 -1.724  1.00 12.48 ? 99  PRO   B N   1 
ATOM   3130 C  CA  . PRO   B 2 99  ? 29.131  -15.582 -2.537  1.00 13.41 ? 99  PRO   B CA  1 
ATOM   3131 C  C   . PRO   B 2 99  ? 30.454  -15.380 -3.268  1.00 13.98 ? 99  PRO   B C   1 
ATOM   3132 O  O   . PRO   B 2 99  ? 31.439  -16.057 -2.951  1.00 13.43 ? 99  PRO   B O   1 
ATOM   3133 C  CB  . PRO   B 2 99  ? 28.876  -14.489 -1.481  1.00 13.05 ? 99  PRO   B CB  1 
ATOM   3134 C  CG  . PRO   B 2 99  ? 29.651  -14.983 -0.291  1.00 12.50 ? 99  PRO   B CG  1 
ATOM   3135 C  CD  . PRO   B 2 99  ? 29.531  -16.497 -0.323  1.00 12.87 ? 99  PRO   B CD  1 
ATOM   3136 N  N   . LYS   B 2 100 ? 30.493  -14.409 -4.189  1.00 15.01 ? 100 LYS   B N   1 
ATOM   3137 C  CA  . LYS   B 2 100 ? 31.774  -13.877 -4.638  1.00 17.50 ? 100 LYS   B CA  1 
ATOM   3138 C  C   . LYS   B 2 100 ? 32.451  -13.272 -3.410  1.00 14.62 ? 100 LYS   B C   1 
ATOM   3139 O  O   . LYS   B 2 100 ? 31.790  -12.564 -2.664  1.00 15.78 ? 100 LYS   B O   1 
ATOM   3140 C  CB  . LYS   B 2 100 ? 31.616  -12.795 -5.718  1.00 22.84 ? 100 LYS   B CB  1 
ATOM   3141 C  CG  . LYS   B 2 100 ? 30.579  -13.104 -6.794  1.00 31.42 ? 100 LYS   B CG  1 
ATOM   3142 C  CD  . LYS   B 2 100 ? 30.248  -11.939 -7.735  1.00 39.56 ? 100 LYS   B CD  1 
ATOM   3143 C  CE  . LYS   B 2 100 ? 28.756  -11.655 -7.895  1.00 47.24 ? 100 LYS   B CE  1 
ATOM   3144 N  NZ  . LYS   B 2 100 ? 27.895  -12.871 -7.948  1.00 49.30 ? 100 LYS   B NZ  1 
ATOM   3145 N  N   . TYR   B 2 101 ? 33.725  -13.569 -3.176  1.00 13.09 ? 101 TYR   B N   1 
ATOM   3146 C  CA  . TYR   B 2 101 ? 34.386  -13.103 -1.970  1.00 14.44 ? 101 TYR   B CA  1 
ATOM   3147 C  C   . TYR   B 2 101 ? 35.880  -12.886 -2.189  1.00 14.74 ? 101 TYR   B C   1 
ATOM   3148 O  O   . TYR   B 2 101 ? 36.443  -13.390 -3.142  1.00 16.55 ? 101 TYR   B O   1 
ATOM   3149 C  CB  . TYR   B 2 101 ? 34.177  -14.078 -0.802  1.00 14.78 ? 101 TYR   B CB  1 
ATOM   3150 C  CG  . TYR   B 2 101 ? 35.008  -15.343 -0.892  1.00 14.98 ? 101 TYR   B CG  1 
ATOM   3151 C  CD1 . TYR   B 2 101 ? 36.276  -15.387 -0.333  1.00 16.11 ? 101 TYR   B CD1 1 
ATOM   3152 C  CD2 . TYR   B 2 101 ? 34.582  -16.428 -1.643  1.00 15.44 ? 101 TYR   B CD2 1 
ATOM   3153 C  CE1 . TYR   B 2 101 ? 37.067  -16.517 -0.449  1.00 18.20 ? 101 TYR   B CE1 1 
ATOM   3154 C  CE2 . TYR   B 2 101 ? 35.363  -17.564 -1.763  1.00 16.88 ? 101 TYR   B CE2 1 
ATOM   3155 C  CZ  . TYR   B 2 101 ? 36.602  -17.609 -1.154  1.00 18.83 ? 101 TYR   B CZ  1 
ATOM   3156 O  OH  . TYR   B 2 101 ? 37.371  -18.735 -1.248  1.00 26.44 ? 101 TYR   B OH  1 
ATOM   3157 N  N   . LYS   B 2 102 ? 36.492  -12.165 -1.246  1.00 16.09 ? 102 LYS   B N   1 
ATOM   3158 C  CA  . LYS   B 2 102 ? 37.927  -12.133 -1.065  1.00 18.29 ? 102 LYS   B CA  1 
ATOM   3159 C  C   . LYS   B 2 102 ? 38.266  -11.880 0.401   1.00 17.01 ? 102 LYS   B C   1 
ATOM   3160 O  O   . LYS   B 2 102 ? 37.419  -11.482 1.206   1.00 15.05 ? 102 LYS   B O   1 
ATOM   3161 C  CB  . LYS   B 2 102 ? 38.587  -11.083 -1.961  1.00 25.00 ? 102 LYS   B CB  1 
ATOM   3162 C  CG  . LYS   B 2 102 ? 38.006  -9.690  -1.946  1.00 31.05 ? 102 LYS   B CG  1 
ATOM   3163 C  CD  . LYS   B 2 102 ? 38.410  -8.943  -3.202  1.00 37.95 ? 102 LYS   B CD  1 
ATOM   3164 C  CE  . LYS   B 2 102 ? 37.700  -7.621  -3.361  1.00 40.92 ? 102 LYS   B CE  1 
ATOM   3165 N  NZ  . LYS   B 2 102 ? 38.345  -6.561  -2.551  1.00 44.58 ? 102 LYS   B NZ  1 
ATOM   3166 N  N   . PHE   B 2 103 ? 39.514  -12.189 0.730   1.00 14.36 ? 103 PHE   B N   1 
ATOM   3167 C  CA  . PHE   B 2 103 ? 40.068  -11.950 2.044   1.00 14.84 ? 103 PHE   B CA  1 
ATOM   3168 C  C   . PHE   B 2 103 ? 40.887  -10.658 2.000   1.00 16.52 ? 103 PHE   B C   1 
ATOM   3169 O  O   . PHE   B 2 103 ? 41.710  -10.489 1.111   1.00 14.66 ? 103 PHE   B O   1 
ATOM   3170 C  CB  . PHE   B 2 103 ? 40.924  -13.143 2.455   1.00 14.71 ? 103 PHE   B CB  1 
ATOM   3171 C  CG  . PHE   B 2 103 ? 40.208  -14.454 2.690   1.00 14.17 ? 103 PHE   B CG  1 
ATOM   3172 C  CD1 . PHE   B 2 103 ? 38.828  -14.519 2.819   1.00 14.42 ? 103 PHE   B CD1 1 
ATOM   3173 C  CD2 . PHE   B 2 103 ? 40.927  -15.640 2.766   1.00 14.14 ? 103 PHE   B CD2 1 
ATOM   3174 C  CE1 . PHE   B 2 103 ? 38.182  -15.735 3.012   1.00 13.46 ? 103 PHE   B CE1 1 
ATOM   3175 C  CE2 . PHE   B 2 103 ? 40.282  -16.855 2.967   1.00 14.35 ? 103 PHE   B CE2 1 
ATOM   3176 C  CZ  . PHE   B 2 103 ? 38.904  -16.899 3.100   1.00 13.21 ? 103 PHE   B CZ  1 
ATOM   3177 N  N   . VAL   B 2 104 ? 40.625  -9.737  2.932   1.00 16.00 ? 104 VAL   B N   1 
ATOM   3178 C  CA  . VAL   B 2 104 ? 41.368  -8.489  2.986   1.00 16.87 ? 104 VAL   B CA  1 
ATOM   3179 C  C   . VAL   B 2 104 ? 41.821  -8.252  4.422   1.00 16.21 ? 104 VAL   B C   1 
ATOM   3180 O  O   . VAL   B 2 104 ? 41.158  -8.669  5.371   1.00 16.11 ? 104 VAL   B O   1 
ATOM   3181 C  CB  . VAL   B 2 104 ? 40.536  -7.298  2.472   1.00 18.55 ? 104 VAL   B CB  1 
ATOM   3182 C  CG1 . VAL   B 2 104 ? 40.013  -7.505  1.059   1.00 17.99 ? 104 VAL   B CG1 1 
ATOM   3183 C  CG2 . VAL   B 2 104 ? 39.392  -6.959  3.412   1.00 19.47 ? 104 VAL   B CG2 1 
ATOM   3184 N  N   . ARG   B 2 105 ? 42.944  -7.545  4.569   1.00 14.79 ? 105 ARG   B N   1 
ATOM   3185 C  CA  . ARG   B 2 105 ? 43.414  -7.120  5.873   1.00 14.06 ? 105 ARG   B CA  1 
ATOM   3186 C  C   . ARG   B 2 105 ? 43.240  -5.603  5.955   1.00 14.73 ? 105 ARG   B C   1 
ATOM   3187 O  O   . ARG   B 2 105 ? 43.752  -4.870  5.102   1.00 14.53 ? 105 ARG   B O   1 
ATOM   3188 C  CB  . ARG   B 2 105 ? 44.871  -7.541  6.059   1.00 15.58 ? 105 ARG   B CB  1 
ATOM   3189 C  CG  . ARG   B 2 105 ? 45.447  -7.202  7.419   1.00 15.49 ? 105 ARG   B CG  1 
ATOM   3190 C  CD  . ARG   B 2 105 ? 46.858  -7.733  7.565   1.00 15.92 ? 105 ARG   B CD  1 
ATOM   3191 N  NE  . ARG   B 2 105 ? 47.424  -7.461  8.871   1.00 15.33 ? 105 ARG   B NE  1 
ATOM   3192 C  CZ  . ARG   B 2 105 ? 47.121  -8.106  9.996   1.00 16.90 ? 105 ARG   B CZ  1 
ATOM   3193 N  NH1 . ARG   B 2 105 ? 46.353  -9.187  9.981   1.00 17.46 ? 105 ARG   B NH1 1 
ATOM   3194 N  NH2 . ARG   B 2 105 ? 47.643  -7.705  11.145  1.00 17.64 ? 105 ARG   B NH2 1 
ATOM   3195 N  N   . ILE   B 2 106 ? 42.448  -5.149  6.933   1.00 14.34 ? 106 ILE   B N   1 
ATOM   3196 C  CA  . ILE   B 2 106 ? 42.049  -3.755  7.048   1.00 14.77 ? 106 ILE   B CA  1 
ATOM   3197 C  C   . ILE   B 2 106 ? 43.028  -3.011  7.942   1.00 15.76 ? 106 ILE   B C   1 
ATOM   3198 O  O   . ILE   B 2 106 ? 43.749  -3.628  8.703   1.00 16.65 ? 106 ILE   B O   1 
ATOM   3199 C  CB  . ILE   B 2 106 ? 40.610  -3.602  7.596   1.00 14.84 ? 106 ILE   B CB  1 
ATOM   3200 C  CG1 . ILE   B 2 106 ? 40.446  -4.237  8.985   1.00 14.84 ? 106 ILE   B CG1 1 
ATOM   3201 C  CG2 . ILE   B 2 106 ? 39.628  -4.137  6.558   1.00 14.92 ? 106 ILE   B CG2 1 
ATOM   3202 C  CD1 . ILE   B 2 106 ? 39.146  -3.870  9.710   1.00 16.05 ? 106 ILE   B CD1 1 
ATOM   3203 N  N   . GLN   B 2 107 ? 42.969  -1.676  7.874   1.00 17.32 ? 107 GLN   B N   1 
ATOM   3204 C  CA  . GLN   B 2 107 ? 43.736  -0.779  8.711   1.00 16.66 ? 107 GLN   B CA  1 
ATOM   3205 C  C   . GLN   B 2 107 ? 42.881  -0.279  9.853   1.00 16.42 ? 107 GLN   B C   1 
ATOM   3206 O  O   . GLN   B 2 107 ? 41.659  -0.211  9.705   1.00 15.16 ? 107 GLN   B O   1 
ATOM   3207 C  CB  . GLN   B 2 107 ? 44.187  0.446   7.907   1.00 19.10 ? 107 GLN   B CB  1 
ATOM   3208 C  CG  . GLN   B 2 107 ? 45.354  0.135   6.986   1.00 21.38 ? 107 GLN   B CG  1 
ATOM   3209 C  CD  . GLN   B 2 107 ? 46.593  -0.174  7.801   1.00 23.04 ? 107 GLN   B CD  1 
ATOM   3210 O  OE1 . GLN   B 2 107 ? 46.969  -1.327  7.983   1.00 26.93 ? 107 GLN   B OE1 1 
ATOM   3211 N  NE2 . GLN   B 2 107 ? 47.224  0.869   8.323   1.00 23.33 ? 107 GLN   B NE2 1 
ATOM   3212 N  N   . PRO   B 2 108 ? 43.516  0.190   10.954  1.00 15.59 ? 108 PRO   B N   1 
ATOM   3213 C  CA  . PRO   B 2 108 ? 42.816  0.920   12.005  1.00 14.58 ? 108 PRO   B CA  1 
ATOM   3214 C  C   . PRO   B 2 108 ? 42.009  2.058   11.393  1.00 14.48 ? 108 PRO   B C   1 
ATOM   3215 O  O   . PRO   B 2 108 ? 42.420  2.679   10.428  1.00 14.04 ? 108 PRO   B O   1 
ATOM   3216 C  CB  . PRO   B 2 108 ? 43.936  1.441   12.921  1.00 15.48 ? 108 PRO   B CB  1 
ATOM   3217 C  CG  . PRO   B 2 108 ? 45.087  0.495   12.684  1.00 15.61 ? 108 PRO   B CG  1 
ATOM   3218 C  CD  . PRO   B 2 108 ? 44.959  0.083   11.220  1.00 15.90 ? 108 PRO   B CD  1 
ATOM   3219 N  N   . GLY   B 2 109 ? 40.804  2.270   11.929  1.00 14.97 ? 109 GLY   B N   1 
ATOM   3220 C  CA  . GLY   B 2 109 ? 39.903  3.290   11.429  1.00 14.42 ? 109 GLY   B CA  1 
ATOM   3221 C  C   . GLY   B 2 109 ? 38.824  2.715   10.515  1.00 15.62 ? 109 GLY   B C   1 
ATOM   3222 O  O   . GLY   B 2 109 ? 37.714  3.237   10.482  1.00 15.43 ? 109 GLY   B O   1 
ATOM   3223 N  N   . GLN   B 2 110 ? 39.136  1.631   9.794   1.00 16.23 ? 110 GLN   B N   1 
ATOM   3224 C  CA  . GLN   B 2 110 ? 38.196  1.065   8.845   1.00 16.35 ? 110 GLN   B CA  1 
ATOM   3225 C  C   . GLN   B 2 110 ? 37.090  0.349   9.601   1.00 15.64 ? 110 GLN   B C   1 
ATOM   3226 O  O   . GLN   B 2 110 ? 37.322  -0.295  10.621  1.00 16.43 ? 110 GLN   B O   1 
ATOM   3227 C  CB  . GLN   B 2 110 ? 38.858  0.088   7.870   1.00 18.75 ? 110 GLN   B CB  1 
ATOM   3228 C  CG  . GLN   B 2 110 ? 39.822  0.759   6.901   1.00 21.70 ? 110 GLN   B CG  1 
ATOM   3229 C  CD  . GLN   B 2 110 ? 40.259  -0.201  5.812   1.00 24.89 ? 110 GLN   B CD  1 
ATOM   3230 O  OE1 . GLN   B 2 110 ? 41.353  -0.745  5.819   1.00 19.69 ? 110 GLN   B OE1 1 
ATOM   3231 N  NE2 . GLN   B 2 110 ? 39.366  -0.455  4.874   1.00 31.75 ? 110 GLN   B NE2 1 
ATOM   3232 N  N   . THR   B 2 111 ? 35.879  0.487   9.077   1.00 14.93 ? 111 THR   B N   1 
ATOM   3233 C  CA  . THR   B 2 111 ? 34.713  -0.122  9.685   1.00 13.09 ? 111 THR   B CA  1 
ATOM   3234 C  C   . THR   B 2 111 ? 34.357  -1.387  8.922   1.00 12.00 ? 111 THR   B C   1 
ATOM   3235 O  O   . THR   B 2 111 ? 34.742  -1.557  7.779   1.00 11.72 ? 111 THR   B O   1 
ATOM   3236 C  CB  . THR   B 2 111 ? 33.523  0.840   9.709   1.00 12.09 ? 111 THR   B CB  1 
ATOM   3237 O  OG1 . THR   B 2 111 ? 33.284  1.323   8.397   1.00 11.18 ? 111 THR   B OG1 1 
ATOM   3238 C  CG2 . THR   B 2 111 ? 33.735  2.017   10.634  1.00 12.87 ? 111 THR   B CG2 1 
ATOM   3239 N  N   . PHE   B 2 112 ? 33.594  -2.253  9.585   1.00 12.26 ? 112 PHE   B N   1 
ATOM   3240 C  CA  . PHE   B 2 112 ? 33.080  -3.465  8.970   1.00 11.17 ? 112 PHE   B CA  1 
ATOM   3241 C  C   . PHE   B 2 112 ? 31.853  -3.925  9.737   1.00 11.05 ? 112 PHE   B C   1 
ATOM   3242 O  O   . PHE   B 2 112 ? 31.638  -3.495  10.876  1.00 10.28 ? 112 PHE   B O   1 
ATOM   3243 C  CB  . PHE   B 2 112 ? 34.147  -4.548  8.961   1.00 10.97 ? 112 PHE   B CB  1 
ATOM   3244 C  CG  . PHE   B 2 112 ? 34.769  -4.823  10.308  1.00 11.28 ? 112 PHE   B CG  1 
ATOM   3245 C  CD1 . PHE   B 2 112 ? 35.772  -4.019  10.802  1.00 11.54 ? 112 PHE   B CD1 1 
ATOM   3246 C  CD2 . PHE   B 2 112 ? 34.368  -5.918  11.055  1.00 10.99 ? 112 PHE   B CD2 1 
ATOM   3247 C  CE1 . PHE   B 2 112 ? 36.348  -4.290  12.037  1.00 12.90 ? 112 PHE   B CE1 1 
ATOM   3248 C  CE2 . PHE   B 2 112 ? 34.954  -6.209  12.271  1.00 12.34 ? 112 PHE   B CE2 1 
ATOM   3249 C  CZ  . PHE   B 2 112 ? 35.966  -5.405  12.754  1.00 12.94 ? 112 PHE   B CZ  1 
ATOM   3250 N  N   . SER   B 2 113 ? 31.079  -4.809  9.100   1.00 11.04 ? 113 SER   B N   1 
ATOM   3251 C  CA  . SER   B 2 113 ? 29.918  -5.422  9.728   1.00 11.28 ? 113 SER   B CA  1 
ATOM   3252 C  C   . SER   B 2 113 ? 30.345  -6.738  10.372  1.00 11.87 ? 113 SER   B C   1 
ATOM   3253 O  O   . SER   B 2 113 ? 31.112  -7.496  9.773   1.00 11.93 ? 113 SER   B O   1 
ATOM   3254 C  CB  . SER   B 2 113 ? 28.829  -5.677  8.738   1.00 12.21 ? 113 SER   B CB  1 
ATOM   3255 O  OG  . SER   B 2 113 ? 28.428  -4.494  8.111   1.00 12.18 ? 113 SER   B OG  1 
ATOM   3256 N  N   . VAL   B 2 114 ? 29.843  -6.987  11.582  1.00 10.51 ? 114 VAL   B N   1 
ATOM   3257 C  CA  . VAL   B 2 114 ? 30.084  -8.206  12.293  1.00 11.09 ? 114 VAL   B CA  1 
ATOM   3258 C  C   . VAL   B 2 114 ? 28.783  -8.987  12.328  1.00 11.99 ? 114 VAL   B C   1 
ATOM   3259 O  O   . VAL   B 2 114 ? 27.762  -8.425  12.744  1.00 12.00 ? 114 VAL   B O   1 
ATOM   3260 C  CB  . VAL   B 2 114 ? 30.570  -7.941  13.726  1.00 12.26 ? 114 VAL   B CB  1 
ATOM   3261 C  CG1 . VAL   B 2 114 ? 30.576  -9.231  14.550  1.00 11.94 ? 114 VAL   B CG1 1 
ATOM   3262 C  CG2 . VAL   B 2 114 ? 31.937  -7.259  13.748  1.00 12.42 ? 114 VAL   B CG2 1 
ATOM   3263 N  N   . LEU   B 2 115 ? 28.861  -10.276 11.966  1.00 10.79 ? 115 LEU   B N   1 
ATOM   3264 C  CA  . LEU   B 2 115 ? 27.775  -11.209 12.186  1.00 11.76 ? 115 LEU   B CA  1 
ATOM   3265 C  C   . LEU   B 2 115 ? 28.083  -12.087 13.395  1.00 12.25 ? 115 LEU   B C   1 
ATOM   3266 O  O   . LEU   B 2 115 ? 28.849  -13.035 13.296  1.00 12.09 ? 115 LEU   B O   1 
ATOM   3267 C  CB  . LEU   B 2 115 ? 27.525  -12.056 10.933  1.00 11.74 ? 115 LEU   B CB  1 
ATOM   3268 C  CG  . LEU   B 2 115 ? 26.356  -13.024 11.039  1.00 12.07 ? 115 LEU   B CG  1 
ATOM   3269 C  CD1 . LEU   B 2 115 ? 25.033  -12.275 11.155  1.00 12.05 ? 115 LEU   B CD1 1 
ATOM   3270 C  CD2 . LEU   B 2 115 ? 26.322  -13.953 9.851   1.00 12.49 ? 115 LEU   B CD2 1 
ATOM   3271 N  N   . ALA   B 2 116 ? 27.505  -11.745 14.553  1.00 12.74 ? 116 ALA   B N   1 
ATOM   3272 C  CA  . ALA   B 2 116 ? 27.735  -12.515 15.764  1.00 13.81 ? 116 ALA   B CA  1 
ATOM   3273 C  C   . ALA   B 2 116 ? 26.964  -13.824 15.680  1.00 14.33 ? 116 ALA   B C   1 
ATOM   3274 O  O   . ALA   B 2 116 ? 25.777  -13.820 15.363  1.00 15.45 ? 116 ALA   B O   1 
ATOM   3275 C  CB  . ALA   B 2 116 ? 27.327  -11.718 16.978  1.00 15.09 ? 116 ALA   B CB  1 
ATOM   3276 N  N   . CYS   B 2 117 ? 27.651  -14.935 15.977  1.00 14.90 ? 117 CYS   B N   1 
ATOM   3277 C  CA  . CYS   B 2 117 ? 27.113  -16.267 15.807  1.00 15.86 ? 117 CYS   B CA  1 
ATOM   3278 C  C   . CYS   B 2 117 ? 27.441  -17.089 17.049  1.00 16.41 ? 117 CYS   B C   1 
ATOM   3279 O  O   . CYS   B 2 117 ? 28.470  -16.869 17.684  1.00 16.41 ? 117 CYS   B O   1 
ATOM   3280 C  CB  . CYS   B 2 117 ? 27.719  -16.984 14.602  1.00 18.38 ? 117 CYS   B CB  1 
ATOM   3281 S  SG  . CYS   B 2 117 ? 27.343  -16.228 13.012  1.00 22.81 ? 117 CYS   B SG  1 
ATOM   3282 N  N   . TYR   B 2 118 ? 26.558  -18.044 17.348  1.00 17.07 ? 118 TYR   B N   1 
ATOM   3283 C  CA  . TYR   B 2 118 ? 26.676  -18.942 18.489  1.00 17.69 ? 118 TYR   B CA  1 
ATOM   3284 C  C   . TYR   B 2 118 ? 26.238  -20.325 18.005  1.00 16.57 ? 118 TYR   B C   1 
ATOM   3285 O  O   . TYR   B 2 118 ? 25.155  -20.463 17.457  1.00 15.29 ? 118 TYR   B O   1 
ATOM   3286 C  CB  . TYR   B 2 118 ? 25.838  -18.444 19.682  1.00 17.13 ? 118 TYR   B CB  1 
ATOM   3287 C  CG  . TYR   B 2 118 ? 26.307  -17.071 20.116  1.00 18.13 ? 118 TYR   B CG  1 
ATOM   3288 C  CD1 . TYR   B 2 118 ? 27.428  -16.918 20.927  1.00 18.83 ? 118 TYR   B CD1 1 
ATOM   3289 C  CD2 . TYR   B 2 118 ? 25.697  -15.921 19.629  1.00 17.48 ? 118 TYR   B CD2 1 
ATOM   3290 C  CE1 . TYR   B 2 118 ? 27.900  -15.659 21.263  1.00 18.23 ? 118 TYR   B CE1 1 
ATOM   3291 C  CE2 . TYR   B 2 118 ? 26.163  -14.660 19.963  1.00 16.99 ? 118 TYR   B CE2 1 
ATOM   3292 C  CZ  . TYR   B 2 118 ? 27.275  -14.529 20.772  1.00 17.57 ? 118 TYR   B CZ  1 
ATOM   3293 O  OH  . TYR   B 2 118 ? 27.769  -13.285 21.110  1.00 19.24 ? 118 TYR   B OH  1 
ATOM   3294 N  N   . ASN   B 2 119 ? 27.128  -21.314 18.111  1.00 19.42 ? 119 ASN   B N   1 
ATOM   3295 C  CA  . ASN   B 2 119 ? 26.869  -22.667 17.618  1.00 20.38 ? 119 ASN   B CA  1 
ATOM   3296 C  C   . ASN   B 2 119 ? 26.564  -22.697 16.121  1.00 20.57 ? 119 ASN   B C   1 
ATOM   3297 O  O   . ASN   B 2 119 ? 25.704  -23.440 15.657  1.00 19.64 ? 119 ASN   B O   1 
ATOM   3298 C  CB  . ASN   B 2 119 ? 25.712  -23.295 18.374  1.00 23.37 ? 119 ASN   B CB  1 
ATOM   3299 C  CG  . ASN   B 2 119 ? 25.912  -23.178 19.862  1.00 27.48 ? 119 ASN   B CG  1 
ATOM   3300 O  OD1 . ASN   B 2 119 ? 26.858  -23.739 20.406  1.00 31.60 ? 119 ASN   B OD1 1 
ATOM   3301 N  ND2 . ASN   B 2 119 ? 25.057  -22.396 20.495  1.00 32.21 ? 119 ASN   B ND2 1 
ATOM   3302 N  N   . GLY   B 2 120 ? 27.254  -21.854 15.342  1.00 20.56 ? 120 GLY   B N   1 
ATOM   3303 C  CA  . GLY   B 2 120 ? 27.025  -21.804 13.908  1.00 18.36 ? 120 GLY   B CA  1 
ATOM   3304 C  C   . GLY   B 2 120 ? 25.720  -21.111 13.514  1.00 17.69 ? 120 GLY   B C   1 
ATOM   3305 O  O   . GLY   B 2 120 ? 25.425  -21.050 12.333  1.00 17.60 ? 120 GLY   B O   1 
ATOM   3306 N  N   . SER   B 2 121 ? 24.996  -20.513 14.480  1.00 17.30 ? 121 SER   B N   1 
ATOM   3307 C  CA  A SER   B 2 121 ? 23.702  -19.899 14.213  0.39 16.76 ? 121 SER   B CA  1 
ATOM   3308 C  CA  B SER   B 2 121 ? 23.694  -19.904 14.235  0.61 16.60 ? 121 SER   B CA  1 
ATOM   3309 C  C   . SER   B 2 121 ? 23.816  -18.380 14.358  1.00 16.94 ? 121 SER   B C   1 
ATOM   3310 O  O   . SER   B 2 121 ? 24.159  -17.866 15.440  1.00 15.67 ? 121 SER   B O   1 
ATOM   3311 C  CB  A SER   B 2 121 ? 22.642  -20.460 15.108  0.39 16.82 ? 121 SER   B CB  1 
ATOM   3312 C  CB  B SER   B 2 121 ? 22.673  -20.441 15.197  0.61 16.54 ? 121 SER   B CB  1 
ATOM   3313 O  OG  A SER   B 2 121 ? 22.406  -21.824 14.793  0.39 17.09 ? 121 SER   B OG  1 
ATOM   3314 O  OG  B SER   B 2 121 ? 21.379  -19.936 14.902  0.61 16.89 ? 121 SER   B OG  1 
ATOM   3315 N  N   . PRO   B 2 122 ? 23.602  -17.607 13.270  1.00 15.02 ? 122 PRO   B N   1 
ATOM   3316 C  CA  . PRO   B 2 122 ? 23.666  -16.145 13.365  1.00 15.98 ? 122 PRO   B CA  1 
ATOM   3317 C  C   . PRO   B 2 122 ? 22.663  -15.597 14.380  1.00 14.51 ? 122 PRO   B C   1 
ATOM   3318 O  O   . PRO   B 2 122 ? 21.521  -16.027 14.430  1.00 15.56 ? 122 PRO   B O   1 
ATOM   3319 C  CB  . PRO   B 2 122 ? 23.370  -15.696 11.917  1.00 17.27 ? 122 PRO   B CB  1 
ATOM   3320 C  CG  . PRO   B 2 122 ? 23.824  -16.894 11.048  1.00 17.66 ? 122 PRO   B CG  1 
ATOM   3321 C  CD  . PRO   B 2 122 ? 23.374  -18.075 11.886  1.00 17.14 ? 122 PRO   B CD  1 
ATOM   3322 N  N   A SER   B 2 123 ? 23.107  -14.647 15.209  0.55 14.53 ? 123 SER   B N   1 
ATOM   3323 N  N   B SER   B 2 123 ? 23.111  -14.636 15.183  0.45 14.18 ? 123 SER   B N   1 
ATOM   3324 C  CA  A SER   B 2 123 ? 22.268  -14.067 16.244  0.55 14.49 ? 123 SER   B CA  1 
ATOM   3325 C  CA  B SER   B 2 123 ? 22.288  -14.065 16.229  0.45 13.80 ? 123 SER   B CA  1 
ATOM   3326 C  C   A SER   B 2 123 ? 22.040  -12.568 16.028  0.55 13.71 ? 123 SER   B C   1 
ATOM   3327 C  C   B SER   B 2 123 ? 22.033  -12.575 16.004  0.45 13.42 ? 123 SER   B C   1 
ATOM   3328 O  O   A SER   B 2 123 ? 21.016  -12.048 16.439  0.55 12.31 ? 123 SER   B O   1 
ATOM   3329 O  O   B SER   B 2 123 ? 20.980  -12.074 16.365  0.45 12.29 ? 123 SER   B O   1 
ATOM   3330 C  CB  A SER   B 2 123 ? 22.851  -14.323 17.619  0.55 14.96 ? 123 SER   B CB  1 
ATOM   3331 C  CB  B SER   B 2 123 ? 22.933  -14.302 17.562  0.45 13.76 ? 123 SER   B CB  1 
ATOM   3332 O  OG  A SER   B 2 123 ? 24.085  -13.645 17.781  0.55 16.57 ? 123 SER   B OG  1 
ATOM   3333 O  OG  B SER   B 2 123 ? 22.279  -13.546 18.548  0.45 13.91 ? 123 SER   B OG  1 
ATOM   3334 N  N   . GLY   B 2 124 ? 23.020  -11.853 15.466  1.00 13.74 ? 124 GLY   B N   1 
ATOM   3335 C  CA  . GLY   B 2 124 ? 22.867  -10.415 15.270  1.00 13.31 ? 124 GLY   B CA  1 
ATOM   3336 C  C   . GLY   B 2 124 ? 23.976  -9.815  14.415  1.00 13.38 ? 124 GLY   B C   1 
ATOM   3337 O  O   . GLY   B 2 124 ? 25.017  -10.444 14.237  1.00 13.07 ? 124 GLY   B O   1 
ATOM   3338 N  N   . VAL   B 2 125 ? 23.720  -8.598  13.890  1.00 12.95 ? 125 VAL   B N   1 
ATOM   3339 C  CA  . VAL   B 2 125 ? 24.648  -7.897  13.028  1.00 12.81 ? 125 VAL   B CA  1 
ATOM   3340 C  C   . VAL   B 2 125 ? 24.744  -6.431  13.465  1.00 13.94 ? 125 VAL   B C   1 
ATOM   3341 O  O   . VAL   B 2 125 ? 23.747  -5.805  13.825  1.00 12.47 ? 125 VAL   B O   1 
ATOM   3342 C  CB  . VAL   B 2 125 ? 24.258  -8.067  11.544  1.00 14.45 ? 125 VAL   B CB  1 
ATOM   3343 C  CG1 . VAL   B 2 125 ? 22.874  -7.564  11.228  1.00 15.48 ? 125 VAL   B CG1 1 
ATOM   3344 C  CG2 . VAL   B 2 125 ? 25.276  -7.442  10.593  1.00 14.88 ? 125 VAL   B CG2 1 
ATOM   3345 N  N   . TYR   B 2 126 ? 25.974  -5.906  13.452  1.00 14.53 ? 126 TYR   B N   1 
ATOM   3346 C  CA  . TYR   B 2 126 ? 26.259  -4.526  13.830  1.00 15.79 ? 126 TYR   B CA  1 
ATOM   3347 C  C   . TYR   B 2 126 ? 27.550  -4.080  13.155  1.00 16.42 ? 126 TYR   B C   1 
ATOM   3348 O  O   . TYR   B 2 126 ? 28.346  -4.913  12.718  1.00 15.30 ? 126 TYR   B O   1 
ATOM   3349 C  CB  . TYR   B 2 126 ? 26.368  -4.385  15.350  1.00 15.71 ? 126 TYR   B CB  1 
ATOM   3350 C  CG  . TYR   B 2 126 ? 27.412  -5.276  16.014  1.00 16.71 ? 126 TYR   B CG  1 
ATOM   3351 C  CD1 . TYR   B 2 126 ? 28.754  -4.896  16.077  1.00 17.10 ? 126 TYR   B CD1 1 
ATOM   3352 C  CD2 . TYR   B 2 126 ? 27.067  -6.511  16.555  1.00 16.84 ? 126 TYR   B CD2 1 
ATOM   3353 C  CE1 . TYR   B 2 126 ? 29.709  -5.708  16.670  1.00 16.98 ? 126 TYR   B CE1 1 
ATOM   3354 C  CE2 . TYR   B 2 126 ? 28.014  -7.336  17.143  1.00 16.65 ? 126 TYR   B CE2 1 
ATOM   3355 C  CZ  . TYR   B 2 126 ? 29.338  -6.927  17.214  1.00 17.53 ? 126 TYR   B CZ  1 
ATOM   3356 O  OH  . TYR   B 2 126 ? 30.281  -7.742  17.804  1.00 17.89 ? 126 TYR   B OH  1 
ATOM   3357 N  N   . GLN   B 2 127 ? 27.742  -2.763  13.087  1.00 18.59 ? 127 GLN   B N   1 
ATOM   3358 C  CA  . GLN   B 2 127 ? 28.942  -2.171  12.531  1.00 19.74 ? 127 GLN   B CA  1 
ATOM   3359 C  C   . GLN   B 2 127 ? 29.905  -1.828  13.656  1.00 20.56 ? 127 GLN   B C   1 
ATOM   3360 O  O   . GLN   B 2 127 ? 29.508  -1.412  14.750  1.00 19.40 ? 127 GLN   B O   1 
ATOM   3361 C  CB  . GLN   B 2 127 ? 28.652  -0.900  11.728  1.00 23.67 ? 127 GLN   B CB  1 
ATOM   3362 C  CG  . GLN   B 2 127 ? 29.812  -0.547  10.785  1.00 27.14 ? 127 GLN   B CG  1 
ATOM   3363 C  CD  . GLN   B 2 127 ? 29.735  0.751   9.999   1.00 32.86 ? 127 GLN   B CD  1 
ATOM   3364 O  OE1 . GLN   B 2 127 ? 29.506  1.833   10.548  1.00 34.04 ? 127 GLN   B OE1 1 
ATOM   3365 N  NE2 . GLN   B 2 127 ? 30.011  0.668   8.697   1.00 30.59 ? 127 GLN   B NE2 1 
ATOM   3366 N  N   . CYS   B 2 128 ? 31.197  -1.953  13.374  1.00 19.83 ? 128 CYS   B N   1 
ATOM   3367 C  CA  . CYS   B 2 128 ? 32.181  -1.396  14.280  1.00 21.14 ? 128 CYS   B CA  1 
ATOM   3368 C  C   . CYS   B 2 128 ? 33.455  -1.065  13.528  1.00 19.07 ? 128 CYS   B C   1 
ATOM   3369 O  O   . CYS   B 2 128 ? 33.529  -1.276  12.329  1.00 17.56 ? 128 CYS   B O   1 
ATOM   3370 C  CB  . CYS   B 2 128 ? 32.488  -2.339  15.422  1.00 25.19 ? 128 CYS   B CB  1 
ATOM   3371 S  SG  . CYS   B 2 128 ? 33.072  -3.918  14.806  1.00 32.07 ? 128 CYS   B SG  1 
ATOM   3372 N  N   . ALA   B 2 129 ? 34.412  -0.460  14.248  1.00 19.44 ? 129 ALA   B N   1 
ATOM   3373 C  CA  . ALA   B 2 129 ? 35.668  -0.044  13.645  1.00 19.34 ? 129 ALA   B CA  1 
ATOM   3374 C  C   . ALA   B 2 129 ? 36.819  -0.723  14.372  1.00 17.03 ? 129 ALA   B C   1 
ATOM   3375 O  O   . ALA   B 2 129 ? 36.715  -1.014  15.551  1.00 18.01 ? 129 ALA   B O   1 
ATOM   3376 C  CB  . ALA   B 2 129 ? 35.824  1.447   13.697  1.00 19.71 ? 129 ALA   B CB  1 
ATOM   3377 N  N   . MET   B 2 130 ? 37.875  -0.993  13.611  1.00 16.32 ? 130 MET   B N   1 
ATOM   3378 C  CA  . MET   B 2 130 ? 39.171  -1.370  14.134  1.00 15.99 ? 130 MET   B CA  1 
ATOM   3379 C  C   . MET   B 2 130 ? 39.781  -0.134  14.806  1.00 14.71 ? 130 MET   B C   1 
ATOM   3380 O  O   . MET   B 2 130 ? 39.961  0.907   14.183  1.00 13.49 ? 130 MET   B O   1 
ATOM   3381 C  CB  . MET   B 2 130 ? 40.043  -1.844  12.972  1.00 16.87 ? 130 MET   B CB  1 
ATOM   3382 C  CG  . MET   B 2 130 ? 41.441  -2.283  13.334  1.00 19.65 ? 130 MET   B CG  1 
ATOM   3383 S  SD  . MET   B 2 130 ? 41.410  -3.754  14.330  1.00 24.31 ? 130 MET   B SD  1 
ATOM   3384 C  CE  . MET   B 2 130 ? 40.892  -4.962  13.110  1.00 24.23 ? 130 MET   B CE  1 
ATOM   3385 N  N   . ARG   B 2 131 ? 40.054  -0.253  16.104  1.00 15.07 ? 131 ARG   B N   1 
ATOM   3386 C  CA  . ARG   B 2 131 ? 40.713  0.792   16.879  1.00 14.61 ? 131 ARG   B CA  1 
ATOM   3387 C  C   . ARG   B 2 131 ? 42.199  0.875   16.548  1.00 15.21 ? 131 ARG   B C   1 
ATOM   3388 O  O   . ARG   B 2 131 ? 42.785  -0.093  16.067  1.00 14.23 ? 131 ARG   B O   1 
ATOM   3389 C  CB  . ARG   B 2 131 ? 40.587  0.531   18.377  1.00 14.83 ? 131 ARG   B CB  1 
ATOM   3390 C  CG  . ARG   B 2 131 ? 39.161  0.513   18.920  1.00 14.48 ? 131 ARG   B CG  1 
ATOM   3391 C  CD  . ARG   B 2 131 ? 38.351  1.717   18.500  1.00 13.88 ? 131 ARG   B CD  1 
ATOM   3392 N  NE  . ARG   B 2 131 ? 38.973  2.977   18.887  1.00 13.91 ? 131 ARG   B NE  1 
ATOM   3393 C  CZ  . ARG   B 2 131 ? 38.454  4.189   18.642  1.00 12.49 ? 131 ARG   B CZ  1 
ATOM   3394 N  NH1 . ARG   B 2 131 ? 37.251  4.306   18.107  1.00 10.58 ? 131 ARG   B NH1 1 
ATOM   3395 N  NH2 . ARG   B 2 131 ? 39.162  5.274   18.927  1.00 12.40 ? 131 ARG   B NH2 1 
ATOM   3396 N  N   . PRO   B 2 132 ? 42.846  2.051   16.750  1.00 15.00 ? 132 PRO   B N   1 
ATOM   3397 C  CA  . PRO   B 2 132 ? 44.284  2.187   16.475  1.00 15.53 ? 132 PRO   B CA  1 
ATOM   3398 C  C   . PRO   B 2 132 ? 45.180  1.221   17.258  1.00 16.07 ? 132 PRO   B C   1 
ATOM   3399 O  O   . PRO   B 2 132 ? 46.242  0.877   16.770  1.00 16.49 ? 132 PRO   B O   1 
ATOM   3400 C  CB  . PRO   B 2 132 ? 44.592  3.656   16.840  1.00 15.65 ? 132 PRO   B CB  1 
ATOM   3401 C  CG  . PRO   B 2 132 ? 43.252  4.362   16.578  1.00 15.23 ? 132 PRO   B CG  1 
ATOM   3402 C  CD  . PRO   B 2 132 ? 42.201  3.348   17.032  1.00 14.48 ? 132 PRO   B CD  1 
ATOM   3403 N  N   . ASN   B 2 133 ? 44.712  0.733   18.413  1.00 16.19 ? 133 ASN   B N   1 
ATOM   3404 C  CA  . ASN   B 2 133 ? 45.413  -0.305  19.156  1.00 18.44 ? 133 ASN   B CA  1 
ATOM   3405 C  C   . ASN   B 2 133 ? 45.031  -1.735  18.722  1.00 20.20 ? 133 ASN   B C   1 
ATOM   3406 O  O   . ASN   B 2 133 ? 45.338  -2.681  19.432  1.00 18.72 ? 133 ASN   B O   1 
ATOM   3407 C  CB  . ASN   B 2 133 ? 45.207  -0.164  20.659  1.00 16.53 ? 133 ASN   B CB  1 
ATOM   3408 C  CG  . ASN   B 2 133 ? 43.792  -0.395  21.126  1.00 16.90 ? 133 ASN   B CG  1 
ATOM   3409 O  OD1 . ASN   B 2 133 ? 42.889  -0.719  20.352  1.00 17.60 ? 133 ASN   B OD1 1 
ATOM   3410 N  ND2 . ASN   B 2 133 ? 43.595  -0.253  22.417  1.00 17.27 ? 133 ASN   B ND2 1 
ATOM   3411 N  N   . PHE   B 2 134 ? 44.354  -1.885  17.578  1.00 21.42 ? 134 PHE   B N   1 
ATOM   3412 C  CA  . PHE   B 2 134 ? 44.084  -3.166  16.917  1.00 20.41 ? 134 PHE   B CA  1 
ATOM   3413 C  C   . PHE   B 2 134 ? 43.079  -4.019  17.685  1.00 20.59 ? 134 PHE   B C   1 
ATOM   3414 O  O   . PHE   B 2 134 ? 42.989  -5.224  17.485  1.00 27.67 ? 134 PHE   B O   1 
ATOM   3415 C  CB  . PHE   B 2 134 ? 45.390  -3.919  16.613  1.00 19.59 ? 134 PHE   B CB  1 
ATOM   3416 C  CG  . PHE   B 2 134 ? 46.225  -3.256  15.543  1.00 19.89 ? 134 PHE   B CG  1 
ATOM   3417 C  CD1 . PHE   B 2 134 ? 45.788  -3.228  14.231  1.00 20.67 ? 134 PHE   B CD1 1 
ATOM   3418 C  CD2 . PHE   B 2 134 ? 47.408  -2.607  15.848  1.00 20.83 ? 134 PHE   B CD2 1 
ATOM   3419 C  CE1 . PHE   B 2 134 ? 46.529  -2.610  13.237  1.00 21.55 ? 134 PHE   B CE1 1 
ATOM   3420 C  CE2 . PHE   B 2 134 ? 48.141  -1.967  14.857  1.00 20.70 ? 134 PHE   B CE2 1 
ATOM   3421 C  CZ  . PHE   B 2 134 ? 47.701  -1.966  13.553  1.00 22.58 ? 134 PHE   B CZ  1 
ATOM   3422 N  N   . THR   B 2 135 ? 42.301  -3.421  18.560  1.00 18.31 ? 135 THR   B N   1 
ATOM   3423 C  CA  . THR   B 2 135 ? 41.190  -4.127  19.158  1.00 18.04 ? 135 THR   B CA  1 
ATOM   3424 C  C   . THR   B 2 135 ? 39.914  -3.655  18.476  1.00 18.78 ? 135 THR   B C   1 
ATOM   3425 O  O   . THR   B 2 135 ? 39.955  -2.722  17.667  1.00 18.51 ? 135 THR   B O   1 
ATOM   3426 C  CB  . THR   B 2 135 ? 41.135  -3.877  20.671  1.00 19.88 ? 135 THR   B CB  1 
ATOM   3427 O  OG1 . THR   B 2 135 ? 40.877  -2.500  20.948  1.00 17.89 ? 135 THR   B OG1 1 
ATOM   3428 C  CG2 . THR   B 2 135 ? 42.408  -4.305  21.368  1.00 21.23 ? 135 THR   B CG2 1 
ATOM   3429 N  N   . ILE   B 2 136 ? 38.788  -4.276  18.827  1.00 19.49 ? 136 ILE   B N   1 
ATOM   3430 C  CA  . ILE   B 2 136 ? 37.499  -3.747  18.421  1.00 20.17 ? 136 ILE   B CA  1 
ATOM   3431 C  C   . ILE   B 2 136 ? 36.606  -3.699  19.647  1.00 19.76 ? 136 ILE   B C   1 
ATOM   3432 O  O   . ILE   B 2 136 ? 36.688  -4.541  20.526  1.00 19.23 ? 136 ILE   B O   1 
ATOM   3433 C  CB  . ILE   B 2 136 ? 36.861  -4.522  17.244  1.00 21.62 ? 136 ILE   B CB  1 
ATOM   3434 C  CG1 . ILE   B 2 136 ? 36.221  -5.835  17.675  1.00 23.54 ? 136 ILE   B CG1 1 
ATOM   3435 C  CG2 . ILE   B 2 136 ? 37.858  -4.739  16.111  1.00 20.47 ? 136 ILE   B CG2 1 
ATOM   3436 C  CD1 . ILE   B 2 136 ? 35.532  -6.579  16.530  1.00 26.15 ? 136 ILE   B CD1 1 
ATOM   3437 N  N   . LYS   B 2 137 ? 35.757  -2.686  19.680  1.00 22.12 ? 137 LYS   B N   1 
ATOM   3438 C  CA  . LYS   B 2 137 ? 34.758  -2.555  20.714  1.00 25.44 ? 137 LYS   B CA  1 
ATOM   3439 C  C   . LYS   B 2 137 ? 33.503  -3.244  20.204  1.00 23.29 ? 137 LYS   B C   1 
ATOM   3440 O  O   . LYS   B 2 137 ? 32.580  -2.588  19.739  1.00 22.06 ? 137 LYS   B O   1 
ATOM   3441 C  CB  . LYS   B 2 137 ? 34.502  -1.089  21.084  1.00 30.04 ? 137 LYS   B CB  1 
ATOM   3442 C  CG  . LYS   B 2 137 ? 35.675  -0.372  21.740  1.00 35.99 ? 137 LYS   B CG  1 
ATOM   3443 C  CD  . LYS   B 2 137 ? 35.239  0.817   22.600  1.00 39.90 ? 137 LYS   B CD  1 
ATOM   3444 C  CE  . LYS   B 2 137 ? 36.393  1.683   23.043  1.00 42.75 ? 137 LYS   B CE  1 
ATOM   3445 N  NZ  . LYS   B 2 137 ? 36.933  2.463   21.905  1.00 50.52 ? 137 LYS   B NZ  1 
ATOM   3446 N  N   . GLY   B 2 138 ? 33.508  -4.576  20.314  1.00 22.07 ? 138 GLY   B N   1 
ATOM   3447 C  CA  . GLY   B 2 138 ? 32.446  -5.415  19.801  1.00 21.28 ? 138 GLY   B CA  1 
ATOM   3448 C  C   . GLY   B 2 138 ? 31.361  -5.651  20.843  1.00 21.43 ? 138 GLY   B C   1 
ATOM   3449 O  O   . GLY   B 2 138 ? 31.404  -5.128  21.944  1.00 23.93 ? 138 GLY   B O   1 
ATOM   3450 N  N   . SER   B 2 139 ? 30.393  -6.459  20.456  1.00 21.41 ? 139 SER   B N   1 
ATOM   3451 C  CA  . SER   B 2 139 ? 29.427  -7.057  21.352  1.00 22.70 ? 139 SER   B CA  1 
ATOM   3452 C  C   . SER   B 2 139 ? 29.448  -8.545  21.049  1.00 21.64 ? 139 SER   B C   1 
ATOM   3453 O  O   . SER   B 2 139 ? 28.988  -8.973  19.992  1.00 21.22 ? 139 SER   B O   1 
ATOM   3454 C  CB  . SER   B 2 139 ? 28.037  -6.488  21.150  1.00 22.96 ? 139 SER   B CB  1 
ATOM   3455 O  OG  . SER   B 2 139 ? 27.137  -7.055  22.086  1.00 25.38 ? 139 SER   B OG  1 
ATOM   3456 N  N   . PHE   B 2 140 ? 29.992  -9.304  21.999  1.00 21.29 ? 140 PHE   B N   1 
ATOM   3457 C  CA  . PHE   B 2 140 ? 30.263  -10.717 21.833  1.00 18.96 ? 140 PHE   B CA  1 
ATOM   3458 C  C   . PHE   B 2 140 ? 30.128  -11.399 23.188  1.00 19.08 ? 140 PHE   B C   1 
ATOM   3459 O  O   . PHE   B 2 140 ? 30.705  -10.936 24.169  1.00 22.27 ? 140 PHE   B O   1 
ATOM   3460 C  CB  . PHE   B 2 140 ? 31.689  -10.934 21.330  1.00 17.37 ? 140 PHE   B CB  1 
ATOM   3461 C  CG  . PHE   B 2 140 ? 31.977  -10.580 19.899  1.00 16.24 ? 140 PHE   B CG  1 
ATOM   3462 C  CD1 . PHE   B 2 140 ? 31.377  -11.277 18.872  1.00 16.64 ? 140 PHE   B CD1 1 
ATOM   3463 C  CD2 . PHE   B 2 140 ? 32.956  -9.646  19.582  1.00 16.34 ? 140 PHE   B CD2 1 
ATOM   3464 C  CE1 . PHE   B 2 140 ? 31.724  -11.015 17.553  1.00 17.47 ? 140 PHE   B CE1 1 
ATOM   3465 C  CE2 . PHE   B 2 140 ? 33.293  -9.383  18.266  1.00 16.68 ? 140 PHE   B CE2 1 
ATOM   3466 C  CZ  . PHE   B 2 140 ? 32.675  -10.070 17.253  1.00 16.76 ? 140 PHE   B CZ  1 
ATOM   3467 N  N   . LEU   B 2 141 ? 29.393  -12.505 23.222  1.00 17.89 ? 141 LEU   B N   1 
ATOM   3468 C  CA  . LEU   B 2 141 ? 29.336  -13.364 24.393  1.00 20.29 ? 141 LEU   B CA  1 
ATOM   3469 C  C   . LEU   B 2 141 ? 30.212  -14.607 24.199  1.00 21.79 ? 141 LEU   B C   1 
ATOM   3470 O  O   . LEU   B 2 141 ? 30.741  -14.849 23.117  1.00 18.55 ? 141 LEU   B O   1 
ATOM   3471 C  CB  . LEU   B 2 141 ? 27.875  -13.772 24.582  1.00 21.22 ? 141 LEU   B CB  1 
ATOM   3472 C  CG  . LEU   B 2 141 ? 26.900  -12.609 24.788  1.00 22.19 ? 141 LEU   B CG  1 
ATOM   3473 C  CD1 . LEU   B 2 141 ? 25.503  -13.117 25.044  1.00 22.79 ? 141 LEU   B CD1 1 
ATOM   3474 C  CD2 . LEU   B 2 141 ? 27.343  -11.732 25.938  1.00 23.68 ? 141 LEU   B CD2 1 
ATOM   3475 N  N   . ASN   B 2 142 ? 30.341  -15.400 25.263  1.00 21.10 ? 142 ASN   B N   1 
ATOM   3476 C  CA  . ASN   B 2 142 ? 31.017  -16.673 25.178  1.00 22.07 ? 142 ASN   B CA  1 
ATOM   3477 C  C   . ASN   B 2 142 ? 30.367  -17.516 24.083  1.00 19.09 ? 142 ASN   B C   1 
ATOM   3478 O  O   . ASN   B 2 142 ? 29.143  -17.612 24.016  1.00 17.64 ? 142 ASN   B O   1 
ATOM   3479 C  CB  . ASN   B 2 142 ? 31.010  -17.379 26.533  1.00 26.31 ? 142 ASN   B CB  1 
ATOM   3480 C  CG  . ASN   B 2 142 ? 31.877  -18.621 26.512  1.00 31.23 ? 142 ASN   B CG  1 
ATOM   3481 O  OD1 . ASN   B 2 142 ? 32.968  -18.619 25.927  1.00 28.06 ? 142 ASN   B OD1 1 
ATOM   3482 N  ND2 . ASN   B 2 142 ? 31.391  -19.691 27.118  1.00 37.79 ? 142 ASN   B ND2 1 
ATOM   3483 N  N   . GLY   B 2 143 ? 31.200  -18.114 23.207  1.00 17.54 ? 143 GLY   B N   1 
ATOM   3484 C  CA  . GLY   B 2 143 ? 30.684  -18.934 22.117  1.00 16.74 ? 143 GLY   B CA  1 
ATOM   3485 C  C   . GLY   B 2 143 ? 30.657  -18.201 20.776  1.00 15.63 ? 143 GLY   B C   1 
ATOM   3486 O  O   . GLY   B 2 143 ? 30.317  -18.795 19.748  1.00 15.84 ? 143 GLY   B O   1 
ATOM   3487 N  N   . SER   B 2 144 ? 31.086  -16.935 20.780  1.00 14.86 ? 144 SER   B N   1 
ATOM   3488 C  CA  . SER   B 2 144 ? 31.110  -16.095 19.585  1.00 13.64 ? 144 SER   B CA  1 
ATOM   3489 C  C   . SER   B 2 144 ? 32.378  -16.305 18.743  1.00 13.71 ? 144 SER   B C   1 
ATOM   3490 O  O   . SER   B 2 144 ? 32.451  -15.835 17.601  1.00 12.52 ? 144 SER   B O   1 
ATOM   3491 C  CB  . SER   B 2 144 ? 30.984  -14.653 19.970  1.00 13.27 ? 144 SER   B CB  1 
ATOM   3492 O  OG  . SER   B 2 144 ? 32.098  -14.231 20.736  1.00 13.38 ? 144 SER   B OG  1 
ATOM   3493 N  N   . CYS   B 2 145 ? 33.403  -16.932 19.345  1.00 12.53 ? 145 CYS   B N   1 
ATOM   3494 C  CA  . CYS   B 2 145 ? 34.658  -17.260 18.682  1.00 13.06 ? 145 CYS   B CA  1 
ATOM   3495 C  C   . CYS   B 2 145 ? 34.401  -17.809 17.282  1.00 12.35 ? 145 CYS   B C   1 
ATOM   3496 O  O   . CYS   B 2 145 ? 33.593  -18.737 17.116  1.00 12.46 ? 145 CYS   B O   1 
ATOM   3497 C  CB  . CYS   B 2 145 ? 35.444  -18.291 19.497  1.00 13.84 ? 145 CYS   B CB  1 
ATOM   3498 S  SG  . CYS   B 2 145 ? 37.185  -18.453 19.038  1.00 15.96 ? 145 CYS   B SG  1 
ATOM   3499 N  N   . GLY   B 2 146 ? 35.077  -17.202 16.286  1.00 12.04 ? 146 GLY   B N   1 
ATOM   3500 C  CA  . GLY   B 2 146 ? 34.953  -17.610 14.892  1.00 12.28 ? 146 GLY   B CA  1 
ATOM   3501 C  C   . GLY   B 2 146 ? 33.909  -16.811 14.092  1.00 11.58 ? 146 GLY   B C   1 
ATOM   3502 O  O   . GLY   B 2 146 ? 33.848  -16.946 12.871  1.00 11.06 ? 146 GLY   B O   1 
ATOM   3503 N  N   . SER   B 2 147 ? 33.145  -15.943 14.769  1.00 11.29 ? 147 SER   B N   1 
ATOM   3504 C  CA  . SER   B 2 147 ? 32.269  -14.985 14.105  1.00 11.39 ? 147 SER   B CA  1 
ATOM   3505 C  C   . SER   B 2 147 ? 33.132  -14.081 13.218  1.00 11.41 ? 147 SER   B C   1 
ATOM   3506 O  O   . SER   B 2 147 ? 34.282  -13.817 13.582  1.00 11.56 ? 147 SER   B O   1 
ATOM   3507 C  CB  . SER   B 2 147 ? 31.493  -14.147 15.091  1.00 10.72 ? 147 SER   B CB  1 
ATOM   3508 O  OG  . SER   B 2 147 ? 30.610  -14.925 15.900  1.00 10.29 ? 147 SER   B OG  1 
ATOM   3509 N  N   . VAL   B 2 148 ? 32.585  -13.616 12.080  1.00 10.87 ? 148 VAL   B N   1 
ATOM   3510 C  CA  . VAL   B 2 148 ? 33.403  -12.894 11.115  1.00 11.06 ? 148 VAL   B CA  1 
ATOM   3511 C  C   . VAL   B 2 148 ? 32.887  -11.481 10.910  1.00 10.73 ? 148 VAL   B C   1 
ATOM   3512 O  O   . VAL   B 2 148 ? 31.706  -11.178 11.081  1.00 10.50 ? 148 VAL   B O   1 
ATOM   3513 C  CB  . VAL   B 2 148 ? 33.535  -13.617 9.751   1.00 11.79 ? 148 VAL   B CB  1 
ATOM   3514 C  CG1 . VAL   B 2 148 ? 34.277  -14.936 9.878   1.00 11.55 ? 148 VAL   B CG1 1 
ATOM   3515 C  CG2 . VAL   B 2 148 ? 32.181  -13.815 9.068   1.00 11.56 ? 148 VAL   B CG2 1 
ATOM   3516 N  N   . GLY   B 2 149 ? 33.822  -10.636 10.463  1.00 10.59 ? 149 GLY   B N   1 
ATOM   3517 C  CA  . GLY   B 2 149 ? 33.530  -9.286  10.037  1.00 10.57 ? 149 GLY   B CA  1 
ATOM   3518 C  C   . GLY   B 2 149 ? 33.814  -9.119  8.547   1.00 11.27 ? 149 GLY   B C   1 
ATOM   3519 O  O   . GLY   B 2 149 ? 34.666  -9.821  7.978   1.00 11.61 ? 149 GLY   B O   1 
ATOM   3520 N  N   . PHE   B 2 150 ? 33.086  -8.196  7.915   1.00 10.42 ? 150 PHE   B N   1 
ATOM   3521 C  CA  . PHE   B 2 150 ? 33.069  -8.117  6.463   1.00 11.33 ? 150 PHE   B CA  1 
ATOM   3522 C  C   . PHE   B 2 150 ? 32.517  -6.770  5.976   1.00 11.07 ? 150 PHE   B C   1 
ATOM   3523 O  O   . PHE   B 2 150 ? 31.786  -6.091  6.685   1.00 9.58  ? 150 PHE   B O   1 
ATOM   3524 C  CB  . PHE   B 2 150 ? 32.218  -9.248  5.872   1.00 10.83 ? 150 PHE   B CB  1 
ATOM   3525 C  CG  . PHE   B 2 150 ? 30.763  -9.195  6.274   1.00 11.03 ? 150 PHE   B CG  1 
ATOM   3526 C  CD1 . PHE   B 2 150 ? 30.347  -9.697  7.501   1.00 11.71 ? 150 PHE   B CD1 1 
ATOM   3527 C  CD2 . PHE   B 2 150 ? 29.813  -8.601  5.456   1.00 10.67 ? 150 PHE   B CD2 1 
ATOM   3528 C  CE1 . PHE   B 2 150 ? 29.018  -9.615  7.894   1.00 12.06 ? 150 PHE   B CE1 1 
ATOM   3529 C  CE2 . PHE   B 2 150 ? 28.485  -8.542  5.840   1.00 10.96 ? 150 PHE   B CE2 1 
ATOM   3530 C  CZ  . PHE   B 2 150 ? 28.085  -9.036  7.069   1.00 11.33 ? 150 PHE   B CZ  1 
ATOM   3531 N  N   . ASN   B 2 151 ? 32.884  -6.456  4.735   1.00 12.19 ? 151 ASN   B N   1 
ATOM   3532 C  CA  . ASN   B 2 151 ? 32.276  -5.416  3.919   1.00 13.62 ? 151 ASN   B CA  1 
ATOM   3533 C  C   . ASN   B 2 151 ? 31.746  -6.043  2.634   1.00 14.46 ? 151 ASN   B C   1 
ATOM   3534 O  O   . ASN   B 2 151 ? 32.242  -7.064  2.189   1.00 14.02 ? 151 ASN   B O   1 
ATOM   3535 C  CB  . ASN   B 2 151 ? 33.295  -4.319  3.615   1.00 14.24 ? 151 ASN   B CB  1 
ATOM   3536 C  CG  . ASN   B 2 151 ? 33.538  -3.485  4.850   1.00 15.31 ? 151 ASN   B CG  1 
ATOM   3537 O  OD1 . ASN   B 2 151 ? 32.660  -2.729  5.260   1.00 17.78 ? 151 ASN   B OD1 1 
ATOM   3538 N  ND2 . ASN   B 2 151 ? 34.654  -3.704  5.505   1.00 15.03 ? 151 ASN   B ND2 1 
ATOM   3539 N  N   . ILE   B 2 152 ? 30.707  -5.443  2.057   1.00 16.78 ? 152 ILE   B N   1 
ATOM   3540 C  CA  . ILE   B 2 152 ? 30.151  -5.917  0.800   1.00 18.11 ? 152 ILE   B CA  1 
ATOM   3541 C  C   . ILE   B 2 152 ? 30.262  -4.767  -0.189  1.00 23.22 ? 152 ILE   B C   1 
ATOM   3542 O  O   . ILE   B 2 152 ? 29.732  -3.684  0.070   1.00 22.09 ? 152 ILE   B O   1 
ATOM   3543 C  CB  . ILE   B 2 152 ? 28.698  -6.397  0.934   1.00 19.17 ? 152 ILE   B CB  1 
ATOM   3544 C  CG1 . ILE   B 2 152 ? 28.555  -7.482  2.003   1.00 19.04 ? 152 ILE   B CG1 1 
ATOM   3545 C  CG2 . ILE   B 2 152 ? 28.169  -6.858  -0.428  1.00 22.43 ? 152 ILE   B CG2 1 
ATOM   3546 C  CD1 . ILE   B 2 152 ? 27.175  -8.095  2.124   1.00 18.30 ? 152 ILE   B CD1 1 
ATOM   3547 N  N   . ASP   B 2 153 ? 30.973  -5.016  -1.292  1.00 26.04 ? 153 ASP   B N   1 
ATOM   3548 C  CA  . ASP   B 2 153 ? 31.138  -4.028  -2.337  1.00 32.49 ? 153 ASP   B CA  1 
ATOM   3549 C  C   . ASP   B 2 153 ? 30.770  -4.712  -3.644  1.00 36.58 ? 153 ASP   B C   1 
ATOM   3550 O  O   . ASP   B 2 153 ? 31.521  -5.564  -4.100  1.00 31.50 ? 153 ASP   B O   1 
ATOM   3551 C  CB  . ASP   B 2 153 ? 32.548  -3.440  -2.262  1.00 39.47 ? 153 ASP   B CB  1 
ATOM   3552 C  CG  . ASP   B 2 153 ? 32.901  -3.116  -0.810  1.00 49.59 ? 153 ASP   B CG  1 
ATOM   3553 O  OD1 . ASP   B 2 153 ? 32.276  -2.169  -0.251  1.00 42.55 ? 153 ASP   B OD1 1 
ATOM   3554 O  OD2 . ASP   B 2 153 ? 33.719  -3.885  -0.200  1.00 53.97 ? 153 ASP   B OD2 1 
ATOM   3555 N  N   . TYR   B 2 154 ? 29.547  -4.424  -4.128  1.00 44.72 ? 154 TYR   B N   1 
ATOM   3556 C  CA  . TYR   B 2 154 ? 29.049  -4.881  -5.417  1.00 53.24 ? 154 TYR   B CA  1 
ATOM   3557 C  C   . TYR   B 2 154 ? 28.994  -6.402  -5.458  1.00 48.50 ? 154 TYR   B C   1 
ATOM   3558 O  O   . TYR   B 2 154 ? 29.671  -7.026  -6.275  1.00 42.82 ? 154 TYR   B O   1 
ATOM   3559 C  CB  . TYR   B 2 154 ? 29.946  -4.293  -6.506  1.00 64.59 ? 154 TYR   B CB  1 
ATOM   3560 C  CG  . TYR   B 2 154 ? 30.020  -2.777  -6.406  1.00 80.18 ? 154 TYR   B CG  1 
ATOM   3561 C  CD1 . TYR   B 2 154 ? 28.899  -1.990  -6.661  1.00 80.96 ? 154 TYR   B CD1 1 
ATOM   3562 C  CD2 . TYR   B 2 154 ? 31.195  -2.144  -6.009  1.00 86.67 ? 154 TYR   B CD2 1 
ATOM   3563 C  CE1 . TYR   B 2 154 ? 28.957  -0.610  -6.559  1.00 85.77 ? 154 TYR   B CE1 1 
ATOM   3564 C  CE2 . TYR   B 2 154 ? 31.265  -0.764  -5.907  1.00 86.83 ? 154 TYR   B CE2 1 
ATOM   3565 C  CZ  . TYR   B 2 154 ? 30.141  -0.001  -6.177  1.00 86.50 ? 154 TYR   B CZ  1 
ATOM   3566 O  OH  . TYR   B 2 154 ? 30.198  1.355   -6.086  1.00 89.05 ? 154 TYR   B OH  1 
ATOM   3567 N  N   . ASP   B 2 155 ? 28.195  -6.967  -4.543  1.00 49.30 ? 155 ASP   B N   1 
ATOM   3568 C  CA  . ASP   B 2 155 ? 27.948  -8.402  -4.434  1.00 47.62 ? 155 ASP   B CA  1 
ATOM   3569 C  C   . ASP   B 2 155 ? 29.203  -9.225  -4.130  1.00 33.99 ? 155 ASP   B C   1 
ATOM   3570 O  O   . ASP   B 2 155 ? 29.085  -10.452 -4.049  1.00 31.26 ? 155 ASP   B O   1 
ATOM   3571 C  CB  . ASP   B 2 155 ? 27.221  -8.947  -5.670  1.00 54.43 ? 155 ASP   B CB  1 
ATOM   3572 C  CG  . ASP   B 2 155 ? 25.739  -8.595  -5.702  1.00 64.95 ? 155 ASP   B CG  1 
ATOM   3573 O  OD1 . ASP   B 2 155 ? 25.244  -7.982  -4.721  1.00 68.71 ? 155 ASP   B OD1 1 
ATOM   3574 O  OD2 . ASP   B 2 155 ? 25.086  -8.928  -6.712  1.00 77.10 ? 155 ASP   B OD2 1 
ATOM   3575 N  N   . CYS   B 2 156 ? 30.363  -8.574  -3.934  1.00 24.33 ? 156 CYS   B N   1 
ATOM   3576 C  CA  . CYS   B 2 156 ? 31.545  -9.249  -3.426  1.00 21.71 ? 156 CYS   B CA  1 
ATOM   3577 C  C   . CYS   B 2 156 ? 31.694  -8.987  -1.925  1.00 16.89 ? 156 CYS   B C   1 
ATOM   3578 O  O   . CYS   B 2 156 ? 31.805  -7.837  -1.496  1.00 15.39 ? 156 CYS   B O   1 
ATOM   3579 C  CB  . CYS   B 2 156 ? 32.801  -8.819  -4.183  1.00 23.05 ? 156 CYS   B CB  1 
ATOM   3580 S  SG  . CYS   B 2 156 ? 34.320  -9.671  -3.665  1.00 25.11 ? 156 CYS   B SG  1 
ATOM   3581 N  N   . VAL   B 2 157 ? 31.740  -10.070 -1.135  1.00 14.47 ? 157 VAL   B N   1 
ATOM   3582 C  CA  . VAL   B 2 157 ? 32.010  -10.010 0.297   1.00 13.17 ? 157 VAL   B CA  1 
ATOM   3583 C  C   . VAL   B 2 157 ? 33.530  -10.032 0.543   1.00 12.01 ? 157 VAL   B C   1 
ATOM   3584 O  O   . VAL   B 2 157 ? 34.211  -11.019 0.245   1.00 10.95 ? 157 VAL   B O   1 
ATOM   3585 C  CB  . VAL   B 2 157 ? 31.321  -11.169 1.051   1.00 13.21 ? 157 VAL   B CB  1 
ATOM   3586 C  CG1 . VAL   B 2 157 ? 31.501  -11.032 2.563   1.00 12.70 ? 157 VAL   B CG1 1 
ATOM   3587 C  CG2 . VAL   B 2 157 ? 29.847  -11.287 0.696   1.00 13.00 ? 157 VAL   B CG2 1 
ATOM   3588 N  N   . SER   B 2 158 ? 34.045  -8.938  1.099   1.00 12.18 ? 158 SER   B N   1 
ATOM   3589 C  CA  . SER   B 2 158 ? 35.423  -8.845  1.590   1.00 12.52 ? 158 SER   B CA  1 
ATOM   3590 C  C   . SER   B 2 158 ? 35.481  -9.196  3.075   1.00 11.78 ? 158 SER   B C   1 
ATOM   3591 O  O   . SER   B 2 158 ? 35.157  -8.368  3.920   1.00 11.98 ? 158 SER   B O   1 
ATOM   3592 C  CB  . SER   B 2 158 ? 35.975  -7.458  1.374   1.00 13.54 ? 158 SER   B CB  1 
ATOM   3593 O  OG  . SER   B 2 158 ? 36.225  -7.252  0.001   1.00 17.24 ? 158 SER   B OG  1 
ATOM   3594 N  N   . PHE   B 2 159 ? 35.886  -10.424 3.394   1.00 11.21 ? 159 PHE   B N   1 
ATOM   3595 C  CA  . PHE   B 2 159 ? 36.073  -10.825 4.781   1.00 11.46 ? 159 PHE   B CA  1 
ATOM   3596 C  C   . PHE   B 2 159 ? 37.350  -10.228 5.359   1.00 11.94 ? 159 PHE   B C   1 
ATOM   3597 O  O   . PHE   B 2 159 ? 38.414  -10.413 4.774   1.00 13.48 ? 159 PHE   B O   1 
ATOM   3598 C  CB  . PHE   B 2 159 ? 36.118  -12.346 4.879   1.00 10.92 ? 159 PHE   B CB  1 
ATOM   3599 C  CG  . PHE   B 2 159 ? 34.826  -13.007 4.514   1.00 10.41 ? 159 PHE   B CG  1 
ATOM   3600 C  CD1 . PHE   B 2 159 ? 33.762  -12.996 5.401   1.00 10.20 ? 159 PHE   B CD1 1 
ATOM   3601 C  CD2 . PHE   B 2 159 ? 34.650  -13.578 3.272   1.00 9.99  ? 159 PHE   B CD2 1 
ATOM   3602 C  CE1 . PHE   B 2 159 ? 32.571  -13.619 5.080   1.00 10.28 ? 159 PHE   B CE1 1 
ATOM   3603 C  CE2 . PHE   B 2 159 ? 33.459  -14.203 2.951   1.00 9.98  ? 159 PHE   B CE2 1 
ATOM   3604 C  CZ  . PHE   B 2 159 ? 32.415  -14.204 3.847   1.00 10.07 ? 159 PHE   B CZ  1 
ATOM   3605 N  N   . CYS   B 2 160 ? 37.247  -9.570  6.527   1.00 12.01 ? 160 CYS   B N   1 
ATOM   3606 C  CA  . CYS   B 2 160 ? 38.373  -8.840  7.087   1.00 12.04 ? 160 CYS   B CA  1 
ATOM   3607 C  C   . CYS   B 2 160 ? 38.696  -9.230  8.517   1.00 12.03 ? 160 CYS   B C   1 
ATOM   3608 O  O   . CYS   B 2 160 ? 39.783  -8.885  8.978   1.00 13.41 ? 160 CYS   B O   1 
ATOM   3609 C  CB  . CYS   B 2 160 ? 38.158  -7.339  7.002   1.00 13.97 ? 160 CYS   B CB  1 
ATOM   3610 S  SG  . CYS   B 2 160 ? 36.711  -6.720  7.898   1.00 15.74 ? 160 CYS   B SG  1 
ATOM   3611 N  N   . TYR   B 2 161 ? 37.813  -9.965  9.203   1.00 10.04 ? 161 TYR   B N   1 
ATOM   3612 C  CA  . TYR   B 2 161 ? 37.996  -10.188 10.623  1.00 10.67 ? 161 TYR   B CA  1 
ATOM   3613 C  C   . TYR   B 2 161 ? 37.431  -11.556 10.986  1.00 10.67 ? 161 TYR   B C   1 
ATOM   3614 O  O   . TYR   B 2 161 ? 36.346  -11.869 10.559  1.00 10.84 ? 161 TYR   B O   1 
ATOM   3615 C  CB  . TYR   B 2 161 ? 37.333  -9.104  11.485  1.00 10.32 ? 161 TYR   B CB  1 
ATOM   3616 C  CG  . TYR   B 2 161 ? 37.473  -9.291  12.992  1.00 10.49 ? 161 TYR   B CG  1 
ATOM   3617 C  CD1 . TYR   B 2 161 ? 38.659  -8.958  13.653  1.00 11.57 ? 161 TYR   B CD1 1 
ATOM   3618 C  CD2 . TYR   B 2 161 ? 36.393  -9.719  13.779  1.00 10.41 ? 161 TYR   B CD2 1 
ATOM   3619 C  CE1 . TYR   B 2 161 ? 38.784  -9.086  15.032  1.00 11.48 ? 161 TYR   B CE1 1 
ATOM   3620 C  CE2 . TYR   B 2 161 ? 36.513  -9.879  15.150  1.00 10.30 ? 161 TYR   B CE2 1 
ATOM   3621 C  CZ  . TYR   B 2 161 ? 37.711  -9.569  15.780  1.00 11.76 ? 161 TYR   B CZ  1 
ATOM   3622 O  OH  . TYR   B 2 161 ? 37.813  -9.736  17.148  1.00 12.77 ? 161 TYR   B OH  1 
ATOM   3623 N  N   . MET   B 2 162 ? 38.177  -12.342 11.760  1.00 10.46 ? 162 MET   B N   1 
ATOM   3624 C  CA  . MET   B 2 162 ? 37.629  -13.493 12.452  1.00 11.50 ? 162 MET   B CA  1 
ATOM   3625 C  C   . MET   B 2 162 ? 37.882  -13.328 13.954  1.00 11.27 ? 162 MET   B C   1 
ATOM   3626 O  O   . MET   B 2 162 ? 39.023  -13.117 14.388  1.00 12.06 ? 162 MET   B O   1 
ATOM   3627 C  CB  . MET   B 2 162 ? 38.234  -14.789 11.915  1.00 11.93 ? 162 MET   B CB  1 
ATOM   3628 C  CG  . MET   B 2 162 ? 37.826  -16.018 12.700  1.00 13.48 ? 162 MET   B CG  1 
ATOM   3629 S  SD  . MET   B 2 162 ? 38.220  -17.547 11.806  1.00 16.22 ? 162 MET   B SD  1 
ATOM   3630 C  CE  . MET   B 2 162 ? 36.819  -17.676 10.700  1.00 16.24 ? 162 MET   B CE  1 
ATOM   3631 N  N   . HIS   B 2 163 ? 36.809  -13.411 14.740  1.00 10.59 ? 163 HIS   B N   1 
ATOM   3632 C  CA  . HIS   B 2 163 ? 36.856  -13.145 16.165  1.00 11.33 ? 163 HIS   B CA  1 
ATOM   3633 C  C   . HIS   B 2 163 ? 37.493  -14.322 16.918  1.00 12.48 ? 163 HIS   B C   1 
ATOM   3634 O  O   . HIS   B 2 163 ? 37.093  -15.470 16.733  1.00 12.06 ? 163 HIS   B O   1 
ATOM   3635 C  CB  . HIS   B 2 163 ? 35.444  -12.909 16.692  1.00 11.29 ? 163 HIS   B CB  1 
ATOM   3636 C  CG  . HIS   B 2 163 ? 35.404  -12.590 18.140  1.00 11.94 ? 163 HIS   B CG  1 
ATOM   3637 N  ND1 . HIS   B 2 163 ? 36.195  -11.611 18.671  1.00 12.67 ? 163 HIS   B ND1 1 
ATOM   3638 C  CD2 . HIS   B 2 163 ? 34.702  -13.101 19.166  1.00 12.57 ? 163 HIS   B CD2 1 
ATOM   3639 C  CE1 . HIS   B 2 163 ? 35.963  -11.535 19.985  1.00 13.48 ? 163 HIS   B CE1 1 
ATOM   3640 N  NE2 . HIS   B 2 163 ? 35.045  -12.409 20.300  1.00 12.71 ? 163 HIS   B NE2 1 
ATOM   3641 N  N   . HIS   B 2 164 ? 38.435  -14.022 17.822  1.00 12.93 ? 164 HIS   B N   1 
ATOM   3642 C  CA  . HIS   B 2 164 ? 39.082  -15.042 18.652  1.00 14.73 ? 164 HIS   B CA  1 
ATOM   3643 C  C   . HIS   B 2 164 ? 38.776  -14.865 20.140  1.00 16.48 ? 164 HIS   B C   1 
ATOM   3644 O  O   . HIS   B 2 164 ? 38.276  -15.809 20.780  1.00 15.22 ? 164 HIS   B O   1 
ATOM   3645 C  CB  . HIS   B 2 164 ? 40.599  -15.060 18.427  1.00 14.44 ? 164 HIS   B CB  1 
ATOM   3646 C  CG  . HIS   B 2 164 ? 41.024  -15.728 17.160  1.00 14.74 ? 164 HIS   B CG  1 
ATOM   3647 N  ND1 . HIS   B 2 164 ? 40.689  -15.250 15.909  1.00 15.81 ? 164 HIS   B ND1 1 
ATOM   3648 C  CD2 . HIS   B 2 164 ? 41.805  -16.802 16.949  1.00 13.66 ? 164 HIS   B CD2 1 
ATOM   3649 C  CE1 . HIS   B 2 164 ? 41.236  -16.036 14.980  1.00 14.49 ? 164 HIS   B CE1 1 
ATOM   3650 N  NE2 . HIS   B 2 164 ? 41.925  -16.972 15.601  1.00 14.66 ? 164 HIS   B NE2 1 
ATOM   3651 N  N   . MET   B 2 165 ? 39.061  -13.665 20.693  1.00 16.23 ? 165 MET   B N   1 
ATOM   3652 C  CA  . MET   B 2 165 ? 38.996  -13.538 22.140  1.00 18.23 ? 165 MET   B CA  1 
ATOM   3653 C  C   . MET   B 2 165 ? 38.585  -12.158 22.632  1.00 18.30 ? 165 MET   B C   1 
ATOM   3654 O  O   . MET   B 2 165 ? 38.773  -11.150 21.943  1.00 16.76 ? 165 MET   B O   1 
ATOM   3655 C  CB  . MET   B 2 165 ? 40.354  -13.875 22.770  1.00 20.52 ? 165 MET   B CB  1 
ATOM   3656 C  CG  . MET   B 2 165 ? 41.516  -13.223 22.123  1.00 21.17 ? 165 MET   B CG  1 
ATOM   3657 S  SD  . MET   B 2 165 ? 43.112  -14.049 22.499  1.00 24.33 ? 165 MET   B SD  1 
ATOM   3658 C  CE  . MET   B 2 165 ? 44.173  -12.636 22.273  1.00 25.09 ? 165 MET   B CE  1 
ATOM   3659 N  N   . GLU   B 2 166 ? 38.023  -12.168 23.853  1.00 18.84 ? 166 GLU   B N   1 
ATOM   3660 C  CA  . GLU   B 2 166 ? 37.832  -10.957 24.630  1.00 22.02 ? 166 GLU   B CA  1 
ATOM   3661 C  C   . GLU   B 2 166 ? 39.023  -10.722 25.562  1.00 22.54 ? 166 GLU   B C   1 
ATOM   3662 O  O   . GLU   B 2 166 ? 39.493  -11.654 26.216  1.00 21.22 ? 166 GLU   B O   1 
ATOM   3663 C  CB  . GLU   B 2 166 ? 36.536  -11.048 25.419  1.00 24.53 ? 166 GLU   B CB  1 
ATOM   3664 C  CG  . GLU   B 2 166 ? 36.234  -9.778  26.207  1.00 29.13 ? 166 GLU   B CG  1 
ATOM   3665 C  CD  . GLU   B 2 166 ? 34.819  -9.764  26.750  1.00 31.55 ? 166 GLU   B CD  1 
ATOM   3666 O  OE1 . GLU   B 2 166 ? 33.851  -9.683  25.906  1.00 34.06 ? 166 GLU   B OE1 1 
ATOM   3667 O  OE2 . GLU   B 2 166 ? 34.681  -9.882  27.992  1.00 34.38 ? 166 GLU   B OE2 1 
ATOM   3668 N  N   . LEU   B 2 167 ? 39.504  -9.469  25.596  1.00 23.51 ? 167 LEU   B N   1 
ATOM   3669 C  CA  . LEU   B 2 167 ? 40.583  -9.037  26.471  1.00 23.44 ? 167 LEU   B CA  1 
ATOM   3670 C  C   . LEU   B 2 167 ? 40.019  -8.579  27.809  1.00 24.07 ? 167 LEU   B C   1 
ATOM   3671 O  O   . LEU   B 2 167 ? 38.831  -8.341  27.924  1.00 20.99 ? 167 LEU   B O   1 
ATOM   3672 C  CB  . LEU   B 2 167 ? 41.338  -7.886  25.804  1.00 25.17 ? 167 LEU   B CB  1 
ATOM   3673 C  CG  . LEU   B 2 167 ? 41.913  -8.195  24.427  1.00 25.39 ? 167 LEU   B CG  1 
ATOM   3674 C  CD1 . LEU   B 2 167 ? 42.736  -7.036  23.905  1.00 25.85 ? 167 LEU   B CD1 1 
ATOM   3675 C  CD2 . LEU   B 2 167 ? 42.777  -9.444  24.448  1.00 25.70 ? 167 LEU   B CD2 1 
ATOM   3676 N  N   . PRO   B 2 168 ? 40.859  -8.445  28.867  1.00 30.68 ? 168 PRO   B N   1 
ATOM   3677 C  CA  . PRO   B 2 168 ? 40.369  -8.086  30.205  1.00 31.57 ? 168 PRO   B CA  1 
ATOM   3678 C  C   . PRO   B 2 168 ? 39.552  -6.799  30.287  1.00 29.20 ? 168 PRO   B C   1 
ATOM   3679 O  O   . PRO   B 2 168 ? 38.670  -6.690  31.141  1.00 30.61 ? 168 PRO   B O   1 
ATOM   3680 C  CB  . PRO   B 2 168 ? 41.659  -7.994  31.042  1.00 32.51 ? 168 PRO   B CB  1 
ATOM   3681 C  CG  . PRO   B 2 168 ? 42.612  -8.948  30.341  1.00 33.26 ? 168 PRO   B CG  1 
ATOM   3682 C  CD  . PRO   B 2 168 ? 42.302  -8.740  28.868  1.00 32.18 ? 168 PRO   B CD  1 
ATOM   3683 N  N   . THR   B 2 169 ? 39.821  -5.831  29.402  1.00 27.50 ? 169 THR   B N   1 
ATOM   3684 C  CA  . THR   B 2 169 ? 39.057  -4.591  29.393  1.00 27.94 ? 169 THR   B CA  1 
ATOM   3685 C  C   . THR   B 2 169 ? 37.676  -4.733  28.734  1.00 26.50 ? 169 THR   B C   1 
ATOM   3686 O  O   . THR   B 2 169 ? 36.879  -3.796  28.763  1.00 26.94 ? 169 THR   B O   1 
ATOM   3687 C  CB  . THR   B 2 169 ? 39.843  -3.465  28.717  1.00 30.71 ? 169 THR   B CB  1 
ATOM   3688 O  OG1 . THR   B 2 169 ? 40.401  -3.986  27.514  1.00 28.42 ? 169 THR   B OG1 1 
ATOM   3689 C  CG2 . THR   B 2 169 ? 40.980  -2.943  29.569  1.00 33.78 ? 169 THR   B CG2 1 
ATOM   3690 N  N   . GLY   B 2 170 ? 37.374  -5.889  28.144  1.00 23.73 ? 170 GLY   B N   1 
ATOM   3691 C  CA  . GLY   B 2 170 ? 36.080  -6.096  27.519  1.00 22.63 ? 170 GLY   B CA  1 
ATOM   3692 C  C   . GLY   B 2 170 ? 36.085  -5.796  26.018  1.00 20.87 ? 170 GLY   B C   1 
ATOM   3693 O  O   . GLY   B 2 170 ? 35.037  -5.881  25.366  1.00 21.76 ? 170 GLY   B O   1 
ATOM   3694 N  N   . VAL   B 2 171 ? 37.250  -5.420  25.479  1.00 19.52 ? 171 VAL   B N   1 
ATOM   3695 C  CA  . VAL   B 2 171 ? 37.396  -5.221  24.045  1.00 17.97 ? 171 VAL   B CA  1 
ATOM   3696 C  C   . VAL   B 2 171 ? 37.801  -6.553  23.432  1.00 17.85 ? 171 VAL   B C   1 
ATOM   3697 O  O   . VAL   B 2 171 ? 38.037  -7.520  24.170  1.00 16.44 ? 171 VAL   B O   1 
ATOM   3698 C  CB  . VAL   B 2 171 ? 38.388  -4.093  23.705  1.00 19.62 ? 171 VAL   B CB  1 
ATOM   3699 C  CG1 . VAL   B 2 171 ? 37.922  -2.770  24.319  1.00 20.31 ? 171 VAL   B CG1 1 
ATOM   3700 C  CG2 . VAL   B 2 171 ? 39.823  -4.407  24.109  1.00 20.68 ? 171 VAL   B CG2 1 
ATOM   3701 N  N   . HIS   B 2 172 ? 37.877  -6.595  22.080  1.00 16.09 ? 172 HIS   B N   1 
ATOM   3702 C  CA  . HIS   B 2 172 ? 37.932  -7.850  21.355  1.00 14.56 ? 172 HIS   B CA  1 
ATOM   3703 C  C   . HIS   B 2 172 ? 39.097  -7.881  20.391  1.00 13.64 ? 172 HIS   B C   1 
ATOM   3704 O  O   . HIS   B 2 172 ? 39.494  -6.861  19.865  1.00 14.16 ? 172 HIS   B O   1 
ATOM   3705 C  CB  . HIS   B 2 172 ? 36.605  -8.088  20.643  1.00 15.45 ? 172 HIS   B CB  1 
ATOM   3706 C  CG  . HIS   B 2 172 ? 35.481  -8.108  21.625  1.00 14.90 ? 172 HIS   B CG  1 
ATOM   3707 N  ND1 . HIS   B 2 172 ? 34.541  -7.096  21.718  1.00 15.02 ? 172 HIS   B ND1 1 
ATOM   3708 C  CD2 . HIS   B 2 172 ? 35.203  -8.990  22.594  1.00 14.95 ? 172 HIS   B CD2 1 
ATOM   3709 C  CE1 . HIS   B 2 172 ? 33.681  -7.409  22.691  1.00 16.22 ? 172 HIS   B CE1 1 
ATOM   3710 N  NE2 . HIS   B 2 172 ? 34.079  -8.552  23.251  1.00 15.18 ? 172 HIS   B NE2 1 
ATOM   3711 N  N   . ALA   B 2 173 ? 39.661  -9.078  20.204  1.00 13.14 ? 173 ALA   B N   1 
ATOM   3712 C  CA  . ALA   B 2 173 ? 40.825  -9.270  19.378  1.00 12.41 ? 173 ALA   B CA  1 
ATOM   3713 C  C   . ALA   B 2 173 ? 40.614  -10.457 18.449  1.00 12.92 ? 173 ALA   B C   1 
ATOM   3714 O  O   . ALA   B 2 173 ? 39.978  -11.459 18.811  1.00 12.40 ? 173 ALA   B O   1 
ATOM   3715 C  CB  . ALA   B 2 173 ? 42.032  -9.465  20.249  1.00 12.90 ? 173 ALA   B CB  1 
ATOM   3716 N  N   . GLY   B 2 174 ? 41.232  -10.362 17.268  1.00 12.80 ? 174 GLY   B N   1 
ATOM   3717 C  CA  . GLY   B 2 174 ? 41.092  -11.410 16.277  1.00 12.46 ? 174 GLY   B CA  1 
ATOM   3718 C  C   . GLY   B 2 174 ? 42.067  -11.271 15.116  1.00 12.25 ? 174 GLY   B C   1 
ATOM   3719 O  O   . GLY   B 2 174 ? 43.020  -10.495 15.183  1.00 12.67 ? 174 GLY   B O   1 
ATOM   3720 N  N   . THR   B 2 175 ? 41.818  -12.071 14.075  1.00 11.26 ? 175 THR   B N   1 
ATOM   3721 C  CA  . THR   B 2 175 ? 42.727  -12.227 12.959  1.00 11.59 ? 175 THR   B CA  1 
ATOM   3722 C  C   . THR   B 2 175 ? 42.011  -11.824 11.682  1.00 11.31 ? 175 THR   B C   1 
ATOM   3723 O  O   . THR   B 2 175 ? 40.786  -11.618 11.688  1.00 10.26 ? 175 THR   B O   1 
ATOM   3724 C  CB  . THR   B 2 175 ? 43.237  -13.681 12.856  1.00 12.12 ? 175 THR   B CB  1 
ATOM   3725 O  OG1 . THR   B 2 175 ? 42.145  -14.526 12.477  1.00 11.59 ? 175 THR   B OG1 1 
ATOM   3726 C  CG2 . THR   B 2 175 ? 43.846  -14.181 14.144  1.00 11.70 ? 175 THR   B CG2 1 
ATOM   3727 N  N   . ASP   B 2 176 ? 42.803  -11.698 10.607  1.00 11.19 ? 176 ASP   B N   1 
ATOM   3728 C  CA  . ASP   B 2 176 ? 42.257  -11.697 9.261   1.00 12.05 ? 176 ASP   B CA  1 
ATOM   3729 C  C   . ASP   B 2 176 ? 41.931  -13.151 8.902   1.00 11.53 ? 176 ASP   B C   1 
ATOM   3730 O  O   . ASP   B 2 176 ? 42.082  -14.050 9.740   1.00 11.19 ? 176 ASP   B O   1 
ATOM   3731 C  CB  . ASP   B 2 176 ? 43.175  -10.976 8.262   1.00 12.68 ? 176 ASP   B CB  1 
ATOM   3732 C  CG  . ASP   B 2 176 ? 44.564  -11.579 8.109   1.00 14.58 ? 176 ASP   B CG  1 
ATOM   3733 O  OD1 . ASP   B 2 176 ? 44.739  -12.797 8.420   1.00 14.43 ? 176 ASP   B OD1 1 
ATOM   3734 O  OD2 . ASP   B 2 176 ? 45.481  -10.819 7.705   1.00 17.10 ? 176 ASP   B OD2 1 
ATOM   3735 N  N   . LEU   B 2 177 ? 41.513  -13.382 7.662   1.00 11.12 ? 177 LEU   B N   1 
ATOM   3736 C  CA  . LEU   B 2 177 ? 41.134  -14.733 7.253   1.00 12.33 ? 177 LEU   B CA  1 
ATOM   3737 C  C   . LEU   B 2 177 ? 42.322  -15.576 6.795   1.00 12.94 ? 177 LEU   B C   1 
ATOM   3738 O  O   . LEU   B 2 177 ? 42.143  -16.734 6.427   1.00 13.34 ? 177 LEU   B O   1 
ATOM   3739 C  CB  . LEU   B 2 177 ? 40.045  -14.672 6.185   1.00 11.13 ? 177 LEU   B CB  1 
ATOM   3740 C  CG  . LEU   B 2 177 ? 38.620  -14.714 6.753   1.00 11.78 ? 177 LEU   B CG  1 
ATOM   3741 C  CD1 . LEU   B 2 177 ? 38.346  -16.066 7.369   1.00 12.93 ? 177 LEU   B CD1 1 
ATOM   3742 C  CD2 . LEU   B 2 177 ? 38.379  -13.597 7.780   1.00 11.47 ? 177 LEU   B CD2 1 
ATOM   3743 N  N   . GLU   B 2 178 ? 43.525  -15.005 6.811   1.00 15.31 ? 178 GLU   B N   1 
ATOM   3744 C  CA  . GLU   B 2 178 ? 44.755  -15.780 6.661   1.00 16.46 ? 178 GLU   B CA  1 
ATOM   3745 C  C   . GLU   B 2 178 ? 45.338  -16.097 8.025   1.00 14.93 ? 178 GLU   B C   1 
ATOM   3746 O  O   . GLU   B 2 178 ? 46.437  -16.643 8.104   1.00 17.08 ? 178 GLU   B O   1 
ATOM   3747 C  CB  . GLU   B 2 178 ? 45.790  -15.021 5.831   1.00 19.26 ? 178 GLU   B CB  1 
ATOM   3748 C  CG  . GLU   B 2 178 ? 45.299  -14.688 4.446   1.00 21.88 ? 178 GLU   B CG  1 
ATOM   3749 C  CD  . GLU   B 2 178 ? 46.371  -14.074 3.557   1.00 25.33 ? 178 GLU   B CD  1 
ATOM   3750 O  OE1 . GLU   B 2 178 ? 46.964  -13.050 3.950   1.00 29.73 ? 178 GLU   B OE1 1 
ATOM   3751 O  OE2 . GLU   B 2 178 ? 46.612  -14.621 2.479   1.00 29.49 ? 178 GLU   B OE2 1 
ATOM   3752 N  N   . GLY   B 2 179 ? 44.610  -15.749 9.092   1.00 14.22 ? 179 GLY   B N   1 
ATOM   3753 C  CA  . GLY   B 2 179 ? 44.979  -16.135 10.444  1.00 14.19 ? 179 GLY   B CA  1 
ATOM   3754 C  C   . GLY   B 2 179 ? 46.069  -15.292 11.095  1.00 14.53 ? 179 GLY   B C   1 
ATOM   3755 O  O   . GLY   B 2 179 ? 46.582  -15.676 12.150  1.00 15.27 ? 179 GLY   B O   1 
ATOM   3756 N  N   . ASN   B 2 180 ? 46.384  -14.121 10.534  1.00 14.80 ? 180 ASN   B N   1 
ATOM   3757 C  CA  . ASN   B 2 180 ? 47.294  -13.191 11.202  1.00 14.77 ? 180 ASN   B CA  1 
ATOM   3758 C  C   . ASN   B 2 180 ? 46.538  -12.239 12.119  1.00 14.27 ? 180 ASN   B C   1 
ATOM   3759 O  O   . ASN   B 2 180 ? 45.630  -11.547 11.690  1.00 14.20 ? 180 ASN   B O   1 
ATOM   3760 C  CB  . ASN   B 2 180 ? 48.075  -12.341 10.203  1.00 16.09 ? 180 ASN   B CB  1 
ATOM   3761 C  CG  . ASN   B 2 180 ? 48.967  -13.177 9.311   1.00 17.08 ? 180 ASN   B CG  1 
ATOM   3762 O  OD1 . ASN   B 2 180 ? 48.834  -13.180 8.088   1.00 22.77 ? 180 ASN   B OD1 1 
ATOM   3763 N  ND2 . ASN   B 2 180 ? 49.856  -13.925 9.912   1.00 16.36 ? 180 ASN   B ND2 1 
ATOM   3764 N  N   . PHE   B 2 181 ? 46.913  -12.210 13.396  1.00 14.90 ? 181 PHE   B N   1 
ATOM   3765 C  CA  . PHE   B 2 181 ? 46.288  -11.326 14.360  1.00 13.87 ? 181 PHE   B CA  1 
ATOM   3766 C  C   . PHE   B 2 181 ? 46.408  -9.869  13.923  1.00 13.76 ? 181 PHE   B C   1 
ATOM   3767 O  O   . PHE   B 2 181 ? 47.366  -9.460  13.280  1.00 14.23 ? 181 PHE   B O   1 
ATOM   3768 C  CB  . PHE   B 2 181 ? 46.877  -11.525 15.753  1.00 13.44 ? 181 PHE   B CB  1 
ATOM   3769 C  CG  . PHE   B 2 181 ? 46.039  -12.399 16.641  1.00 13.77 ? 181 PHE   B CG  1 
ATOM   3770 C  CD1 . PHE   B 2 181 ? 44.970  -11.888 17.350  1.00 13.81 ? 181 PHE   B CD1 1 
ATOM   3771 C  CD2 . PHE   B 2 181 ? 46.265  -13.774 16.687  1.00 14.00 ? 181 PHE   B CD2 1 
ATOM   3772 C  CE1 . PHE   B 2 181 ? 44.188  -12.717 18.153  1.00 13.66 ? 181 PHE   B CE1 1 
ATOM   3773 C  CE2 . PHE   B 2 181 ? 45.480  -14.598 17.476  1.00 13.57 ? 181 PHE   B CE2 1 
ATOM   3774 C  CZ  . PHE   B 2 181 ? 44.438  -14.068 18.204  1.00 13.53 ? 181 PHE   B CZ  1 
ATOM   3775 N  N   . TYR   B 2 182 ? 45.364  -9.108  14.233  1.00 14.96 ? 182 TYR   B N   1 
ATOM   3776 C  CA  . TYR   B 2 182 ? 45.456  -7.658  14.317  1.00 15.10 ? 182 TYR   B CA  1 
ATOM   3777 C  C   . TYR   B 2 182 ? 46.016  -7.337  15.701  1.00 15.76 ? 182 TYR   B C   1 
ATOM   3778 O  O   . TYR   B 2 182 ? 45.466  -7.783  16.712  1.00 16.50 ? 182 TYR   B O   1 
ATOM   3779 C  CB  . TYR   B 2 182 ? 44.080  -7.025  14.147  1.00 13.95 ? 182 TYR   B CB  1 
ATOM   3780 C  CG  . TYR   B 2 182 ? 43.502  -7.169  12.755  1.00 14.41 ? 182 TYR   B CG  1 
ATOM   3781 C  CD1 . TYR   B 2 182 ? 43.933  -6.348  11.721  1.00 14.42 ? 182 TYR   B CD1 1 
ATOM   3782 C  CD2 . TYR   B 2 182 ? 42.533  -8.132  12.474  1.00 14.27 ? 182 TYR   B CD2 1 
ATOM   3783 C  CE1 . TYR   B 2 182 ? 43.422  -6.478  10.446  1.00 15.60 ? 182 TYR   B CE1 1 
ATOM   3784 C  CE2 . TYR   B 2 182 ? 42.014  -8.266  11.193  1.00 13.79 ? 182 TYR   B CE2 1 
ATOM   3785 C  CZ  . TYR   B 2 182 ? 42.445  -7.431  10.186  1.00 14.54 ? 182 TYR   B CZ  1 
ATOM   3786 O  OH  . TYR   B 2 182 ? 41.949  -7.525  8.917   1.00 14.10 ? 182 TYR   B OH  1 
ATOM   3787 N  N   . GLY   B 2 183 ? 47.122  -6.589  15.719  1.00 16.99 ? 183 GLY   B N   1 
ATOM   3788 C  CA  . GLY   B 2 183 ? 47.771  -6.196  16.957  1.00 17.54 ? 183 GLY   B CA  1 
ATOM   3789 C  C   . GLY   B 2 183 ? 48.668  -7.282  17.545  1.00 19.44 ? 183 GLY   B C   1 
ATOM   3790 O  O   . GLY   B 2 183 ? 48.810  -8.361  16.962  1.00 17.77 ? 183 GLY   B O   1 
ATOM   3791 N  N   . PRO   B 2 184 ? 49.252  -7.015  18.743  1.00 21.82 ? 184 PRO   B N   1 
ATOM   3792 C  CA  . PRO   B 2 184 ? 50.297  -7.863  19.335  1.00 23.94 ? 184 PRO   B CA  1 
ATOM   3793 C  C   . PRO   B 2 184 ? 49.774  -9.022  20.173  1.00 24.28 ? 184 PRO   B C   1 
ATOM   3794 O  O   . PRO   B 2 184 ? 50.329  -9.329  21.216  1.00 36.36 ? 184 PRO   B O   1 
ATOM   3795 C  CB  . PRO   B 2 184 ? 51.048  -6.841  20.230  1.00 23.09 ? 184 PRO   B CB  1 
ATOM   3796 C  CG  . PRO   B 2 184 ? 49.950  -5.934  20.729  1.00 23.24 ? 184 PRO   B CG  1 
ATOM   3797 C  CD  . PRO   B 2 184 ? 49.006  -5.803  19.544  1.00 22.69 ? 184 PRO   B CD  1 
ATOM   3798 N  N   . PHE   B 2 185 ? 48.701  -9.664  19.726  1.00 21.82 ? 185 PHE   B N   1 
ATOM   3799 C  CA  . PHE   B 2 185 ? 48.007  -10.639 20.559  1.00 20.35 ? 185 PHE   B CA  1 
ATOM   3800 C  C   . PHE   B 2 185 ? 48.333  -12.048 20.059  1.00 17.99 ? 185 PHE   B C   1 
ATOM   3801 O  O   . PHE   B 2 185 ? 48.746  -12.214 18.928  1.00 18.05 ? 185 PHE   B O   1 
ATOM   3802 C  CB  . PHE   B 2 185 ? 46.503  -10.354 20.543  1.00 19.46 ? 185 PHE   B CB  1 
ATOM   3803 C  CG  . PHE   B 2 185 ? 46.159  -8.940  20.916  1.00 18.72 ? 185 PHE   B CG  1 
ATOM   3804 C  CD1 . PHE   B 2 185 ? 46.315  -8.497  22.216  1.00 17.57 ? 185 PHE   B CD1 1 
ATOM   3805 C  CD2 . PHE   B 2 185 ? 45.675  -8.059  19.958  1.00 19.40 ? 185 PHE   B CD2 1 
ATOM   3806 C  CE1 . PHE   B 2 185 ? 46.016  -7.184  22.550  1.00 18.59 ? 185 PHE   B CE1 1 
ATOM   3807 C  CE2 . PHE   B 2 185 ? 45.352  -6.760  20.298  1.00 19.26 ? 185 PHE   B CE2 1 
ATOM   3808 C  CZ  . PHE   B 2 185 ? 45.542  -6.319  21.593  1.00 18.81 ? 185 PHE   B CZ  1 
ATOM   3809 N  N   . VAL   B 2 186 ? 48.138  -13.045 20.920  1.00 19.14 ? 186 VAL   B N   1 
ATOM   3810 C  CA  . VAL   B 2 186 ? 48.343  -14.441 20.560  1.00 18.41 ? 186 VAL   B CA  1 
ATOM   3811 C  C   . VAL   B 2 186 ? 47.130  -15.252 21.010  1.00 17.55 ? 186 VAL   B C   1 
ATOM   3812 O  O   . VAL   B 2 186 ? 46.433  -14.878 21.954  1.00 14.41 ? 186 VAL   B O   1 
ATOM   3813 C  CB  . VAL   B 2 186 ? 49.647  -14.993 21.165  1.00 18.94 ? 186 VAL   B CB  1 
ATOM   3814 C  CG1 . VAL   B 2 186 ? 50.874  -14.326 20.566  1.00 19.14 ? 186 VAL   B CG1 1 
ATOM   3815 C  CG2 . VAL   B 2 186 ? 49.652  -14.855 22.661  1.00 19.96 ? 186 VAL   B CG2 1 
ATOM   3816 N  N   . ASP   B 2 187 ? 46.905  -16.398 20.333  1.00 18.48 ? 187 ASP   B N   1 
ATOM   3817 C  CA  . ASP   B 2 187 ? 45.729  -17.220 20.613  1.00 19.42 ? 187 ASP   B CA  1 
ATOM   3818 C  C   . ASP   B 2 187 ? 46.028  -18.191 21.756  1.00 21.59 ? 187 ASP   B C   1 
ATOM   3819 O  O   . ASP   B 2 187 ? 46.171  -19.401 21.560  1.00 22.18 ? 187 ASP   B O   1 
ATOM   3820 C  CB  . ASP   B 2 187 ? 45.180  -17.938 19.368  1.00 18.15 ? 187 ASP   B CB  1 
ATOM   3821 C  CG  . ASP   B 2 187 ? 46.181  -18.677 18.506  1.00 17.69 ? 187 ASP   B CG  1 
ATOM   3822 O  OD1 . ASP   B 2 187 ? 47.414  -18.481 18.680  1.00 17.69 ? 187 ASP   B OD1 1 
ATOM   3823 O  OD2 . ASP   B 2 187 ? 45.707  -19.407 17.609  1.00 18.22 ? 187 ASP   B OD2 1 
ATOM   3824 N  N   . ARG   B 2 188 ? 46.087  -17.645 22.969  1.00 23.07 ? 188 ARG   B N   1 
ATOM   3825 C  CA  . ARG   B 2 188 ? 46.118  -18.459 24.167  1.00 24.65 ? 188 ARG   B CA  1 
ATOM   3826 C  C   . ARG   B 2 188 ? 45.369  -17.723 25.266  1.00 22.57 ? 188 ARG   B C   1 
ATOM   3827 O  O   . ARG   B 2 188 ? 45.215  -16.511 25.214  1.00 22.54 ? 188 ARG   B O   1 
ATOM   3828 C  CB  . ARG   B 2 188 ? 47.556  -18.796 24.579  1.00 27.86 ? 188 ARG   B CB  1 
ATOM   3829 C  CG  . ARG   B 2 188 ? 48.485  -17.607 24.680  1.00 32.24 ? 188 ARG   B CG  1 
ATOM   3830 C  CD  . ARG   B 2 188 ? 49.950  -18.013 24.743  1.00 36.55 ? 188 ARG   B CD  1 
ATOM   3831 N  NE  . ARG   B 2 188 ? 50.269  -18.594 26.050  1.00 46.50 ? 188 ARG   B NE  1 
ATOM   3832 C  CZ  . ARG   B 2 188 ? 51.344  -18.317 26.795  1.00 48.66 ? 188 ARG   B CZ  1 
ATOM   3833 N  NH1 . ARG   B 2 188 ? 52.374  -17.662 26.286  1.00 48.84 ? 188 ARG   B NH1 1 
ATOM   3834 N  NH2 . ARG   B 2 188 ? 51.397  -18.745 28.047  1.00 51.48 ? 188 ARG   B NH2 1 
ATOM   3835 N  N   . GLN   B 2 189 ? 44.886  -18.491 26.235  1.00 23.60 ? 189 GLN   B N   1 
ATOM   3836 C  CA  . GLN   B 2 189 ? 44.007  -17.988 27.271  1.00 26.26 ? 189 GLN   B CA  1 
ATOM   3837 C  C   . GLN   B 2 189 ? 44.857  -17.466 28.419  1.00 27.75 ? 189 GLN   B C   1 
ATOM   3838 O  O   . GLN   B 2 189 ? 44.985  -18.124 29.447  1.00 32.14 ? 189 GLN   B O   1 
ATOM   3839 C  CB  . GLN   B 2 189 ? 43.051  -19.087 27.714  1.00 27.63 ? 189 GLN   B CB  1 
ATOM   3840 C  CG  . GLN   B 2 189 ? 41.955  -18.599 28.643  1.00 30.01 ? 189 GLN   B CG  1 
ATOM   3841 C  CD  . GLN   B 2 189 ? 40.809  -19.578 28.666  1.00 31.48 ? 189 GLN   B CD  1 
ATOM   3842 O  OE1 . GLN   B 2 189 ? 39.662  -19.240 28.362  1.00 33.47 ? 189 GLN   B OE1 1 
ATOM   3843 N  NE2 . GLN   B 2 189 ? 41.109  -20.811 29.029  1.00 33.21 ? 189 GLN   B NE2 1 
ATOM   3844 N  N   . THR   B 2 190 ? 45.495  -16.323 28.164  1.00 28.14 ? 190 THR   B N   1 
ATOM   3845 C  CA  . THR   B 2 190 ? 46.226  -15.547 29.157  1.00 28.36 ? 190 THR   B CA  1 
ATOM   3846 C  C   . THR   B 2 190 ? 45.782  -14.095 29.020  1.00 28.49 ? 190 THR   B C   1 
ATOM   3847 O  O   . THR   B 2 190 ? 45.394  -13.696 27.922  1.00 24.28 ? 190 THR   B O   1 
ATOM   3848 C  CB  . THR   B 2 190 ? 47.743  -15.574 28.946  1.00 28.02 ? 190 THR   B CB  1 
ATOM   3849 O  OG1 . THR   B 2 190 ? 48.076  -15.002 27.676  1.00 30.13 ? 190 THR   B OG1 1 
ATOM   3850 C  CG2 . THR   B 2 190 ? 48.324  -16.961 29.005  1.00 31.40 ? 190 THR   B CG2 1 
ATOM   3851 N  N   . ALA   B 2 191 ? 45.803  -13.348 30.137  1.00 29.43 ? 191 ALA   B N   1 
ATOM   3852 C  CA  . ALA   B 2 191 ? 45.557  -11.913 30.133  1.00 28.39 ? 191 ALA   B CA  1 
ATOM   3853 C  C   . ALA   B 2 191 ? 46.574  -11.226 29.231  1.00 28.87 ? 191 ALA   B C   1 
ATOM   3854 O  O   . ALA   B 2 191 ? 47.780  -11.352 29.422  1.00 32.52 ? 191 ALA   B O   1 
ATOM   3855 C  CB  . ALA   B 2 191 ? 45.627  -11.336 31.532  1.00 29.47 ? 191 ALA   B CB  1 
ATOM   3856 N  N   . GLN   B 2 192 ? 46.059  -10.530 28.215  1.00 25.53 ? 192 GLN   B N   1 
ATOM   3857 C  CA  . GLN   B 2 192 ? 46.866  -9.719  27.328  1.00 24.91 ? 192 GLN   B CA  1 
ATOM   3858 C  C   . GLN   B 2 192 ? 46.172  -8.358  27.298  1.00 24.91 ? 192 GLN   B C   1 
ATOM   3859 O  O   . GLN   B 2 192 ? 44.958  -8.282  27.120  1.00 28.94 ? 192 GLN   B O   1 
ATOM   3860 C  CB  . GLN   B 2 192 ? 46.961  -10.342 25.929  1.00 21.99 ? 192 GLN   B CB  1 
ATOM   3861 C  CG  . GLN   B 2 192 ? 47.477  -11.784 25.906  1.00 20.95 ? 192 GLN   B CG  1 
ATOM   3862 C  CD  . GLN   B 2 192 ? 47.196  -12.468 24.588  1.00 18.26 ? 192 GLN   B CD  1 
ATOM   3863 O  OE1 . GLN   B 2 192 ? 47.579  -12.017 23.516  1.00 19.59 ? 192 GLN   B OE1 1 
ATOM   3864 N  NE2 . GLN   B 2 192 ? 46.521  -13.590 24.643  1.00 18.85 ? 192 GLN   B NE2 1 
ATOM   3865 N  N   . ALA   B 2 193 ? 46.942  -7.298  27.493  1.00 24.58 ? 193 ALA   B N   1 
ATOM   3866 C  CA  . ALA   B 2 193 ? 46.381  -5.956  27.549  1.00 26.48 ? 193 ALA   B CA  1 
ATOM   3867 C  C   . ALA   B 2 193 ? 46.577  -5.299  26.189  1.00 26.42 ? 193 ALA   B C   1 
ATOM   3868 O  O   . ALA   B 2 193 ? 47.611  -5.449  25.548  1.00 29.67 ? 193 ALA   B O   1 
ATOM   3869 C  CB  . ALA   B 2 193 ? 47.042  -5.142  28.640  1.00 25.11 ? 193 ALA   B CB  1 
ATOM   3870 N  N   . ALA   B 2 194 ? 45.587  -4.535  25.753  1.00 28.79 ? 194 ALA   B N   1 
ATOM   3871 C  CA  . ALA   B 2 194 ? 45.788  -3.711  24.576  1.00 31.80 ? 194 ALA   B CA  1 
ATOM   3872 C  C   . ALA   B 2 194 ? 46.671  -2.521  24.933  1.00 30.65 ? 194 ALA   B C   1 
ATOM   3873 O  O   . ALA   B 2 194 ? 46.614  -2.052  26.060  1.00 35.51 ? 194 ALA   B O   1 
ATOM   3874 C  CB  . ALA   B 2 194 ? 44.446  -3.266  24.079  1.00 34.97 ? 194 ALA   B CB  1 
ATOM   3875 N  N   . GLY   B 2 195 ? 47.497  -2.074  23.985  1.00 30.89 ? 195 GLY   B N   1 
ATOM   3876 C  CA  . GLY   B 2 195 ? 48.177  -0.789  24.068  1.00 34.22 ? 195 GLY   B CA  1 
ATOM   3877 C  C   . GLY   B 2 195 ? 47.181  0.359   24.198  1.00 31.34 ? 195 GLY   B C   1 
ATOM   3878 O  O   . GLY   B 2 195 ? 45.989  0.185   23.946  1.00 31.41 ? 195 GLY   B O   1 
ATOM   3879 N  N   . THR   B 2 196 ? 47.663  1.530   24.624  1.00 29.11 ? 196 THR   B N   1 
ATOM   3880 C  CA  . THR   B 2 196 ? 46.777  2.662   24.891  1.00 27.09 ? 196 THR   B CA  1 
ATOM   3881 C  C   . THR   B 2 196 ? 46.119  3.064   23.569  1.00 22.98 ? 196 THR   B C   1 
ATOM   3882 O  O   . THR   B 2 196 ? 46.752  3.068   22.530  1.00 25.96 ? 196 THR   B O   1 
ATOM   3883 C  CB  . THR   B 2 196 ? 47.563  3.785   25.580  1.00 27.50 ? 196 THR   B CB  1 
ATOM   3884 O  OG1 . THR   B 2 196 ? 48.710  4.021   24.771  1.00 33.97 ? 196 THR   B OG1 1 
ATOM   3885 C  CG2 . THR   B 2 196 ? 48.075  3.434   26.957  1.00 27.21 ? 196 THR   B CG2 1 
ATOM   3886 N  N   . ASP   B 2 197 ? 44.821  3.349   23.586  1.00 23.41 ? 197 ASP   B N   1 
ATOM   3887 C  CA  . ASP   B 2 197 ? 44.109  3.634   22.347  1.00 21.64 ? 197 ASP   B CA  1 
ATOM   3888 C  C   . ASP   B 2 197 ? 44.202  5.127   22.057  1.00 20.53 ? 197 ASP   B C   1 
ATOM   3889 O  O   . ASP   B 2 197 ? 44.522  5.902   22.959  1.00 19.13 ? 197 ASP   B O   1 
ATOM   3890 C  CB  . ASP   B 2 197 ? 42.650  3.176   22.404  1.00 21.95 ? 197 ASP   B CB  1 
ATOM   3891 C  CG  . ASP   B 2 197 ? 42.032  2.915   21.030  1.00 22.44 ? 197 ASP   B CG  1 
ATOM   3892 O  OD1 . ASP   B 2 197 ? 42.800  2.685   20.052  1.00 24.55 ? 197 ASP   B OD1 1 
ATOM   3893 O  OD2 . ASP   B 2 197 ? 40.812  2.946   20.930  1.00 21.58 ? 197 ASP   B OD2 1 
ATOM   3894 N  N   . THR   B 2 198 ? 43.961  5.496   20.788  1.00 17.77 ? 198 THR   B N   1 
ATOM   3895 C  CA  . THR   B 2 198 ? 43.936  6.887   20.344  1.00 17.01 ? 198 THR   B CA  1 
ATOM   3896 C  C   . THR   B 2 198 ? 42.643  7.135   19.569  1.00 14.98 ? 198 THR   B C   1 
ATOM   3897 O  O   . THR   B 2 198 ? 41.941  6.190   19.231  1.00 13.86 ? 198 THR   B O   1 
ATOM   3898 C  CB  . THR   B 2 198 ? 45.196  7.183   19.529  1.00 17.20 ? 198 THR   B CB  1 
ATOM   3899 O  OG1 . THR   B 2 198 ? 45.344  6.203   18.501  1.00 17.92 ? 198 THR   B OG1 1 
ATOM   3900 C  CG2 . THR   B 2 198 ? 46.446  7.164   20.388  1.00 19.01 ? 198 THR   B CG2 1 
ATOM   3901 N  N   . THR   B 2 199 ? 42.345  8.409   19.293  1.00 13.08 ? 199 THR   B N   1 
ATOM   3902 C  CA  . THR   B 2 199 ? 41.208  8.805   18.483  1.00 12.13 ? 199 THR   B CA  1 
ATOM   3903 C  C   . THR   B 2 199 ? 41.563  8.701   16.994  1.00 10.16 ? 199 THR   B C   1 
ATOM   3904 O  O   . THR   B 2 199 ? 42.671  9.038   16.600  1.00 10.97 ? 199 THR   B O   1 
ATOM   3905 C  CB  . THR   B 2 199 ? 40.771  10.223  18.853  1.00 12.34 ? 199 THR   B CB  1 
ATOM   3906 O  OG1 . THR   B 2 199 ? 40.541  10.203  20.262  1.00 13.71 ? 199 THR   B OG1 1 
ATOM   3907 C  CG2 . THR   B 2 199 ? 39.514  10.659  18.139  1.00 11.96 ? 199 THR   B CG2 1 
ATOM   3908 N  N   . ILE   B 2 200 ? 40.629  8.197   16.192  1.00 9.29  ? 200 ILE   B N   1 
ATOM   3909 C  CA  . ILE   B 2 200 ? 40.835  7.958   14.758  1.00 9.51  ? 200 ILE   B CA  1 
ATOM   3910 C  C   . ILE   B 2 200 ? 40.589  9.263   13.991  1.00 9.09  ? 200 ILE   B C   1 
ATOM   3911 O  O   . ILE   B 2 200 ? 39.452  9.560   13.591  1.00 9.27  ? 200 ILE   B O   1 
ATOM   3912 C  CB  . ILE   B 2 200 ? 39.907  6.850   14.222  1.00 9.48  ? 200 ILE   B CB  1 
ATOM   3913 C  CG1 . ILE   B 2 200 ? 39.965  5.563   15.070  1.00 9.70  ? 200 ILE   B CG1 1 
ATOM   3914 C  CG2 . ILE   B 2 200 ? 40.231  6.544   12.770  1.00 9.14  ? 200 ILE   B CG2 1 
ATOM   3915 C  CD1 . ILE   B 2 200 ? 38.779  4.610   14.863  1.00 9.74  ? 200 ILE   B CD1 1 
ATOM   3916 N  N   . THR   B 2 201 ? 41.662  10.016  13.819  1.00 8.81  ? 201 THR   B N   1 
ATOM   3917 C  CA  . THR   B 2 201 ? 41.634  11.333  13.196  1.00 9.41  ? 201 THR   B CA  1 
ATOM   3918 C  C   . THR   B 2 201 ? 40.897  11.371  11.853  1.00 8.69  ? 201 THR   B C   1 
ATOM   3919 O  O   . THR   B 2 201 ? 40.085  12.257  11.650  1.00 7.78  ? 201 THR   B O   1 
ATOM   3920 C  CB  . THR   B 2 201 ? 43.063  11.837  13.022  1.00 9.29  ? 201 THR   B CB  1 
ATOM   3921 O  OG1 . THR   B 2 201 ? 43.707  11.631  14.280  1.00 9.10  ? 201 THR   B OG1 1 
ATOM   3922 C  CG2 . THR   B 2 201 ? 43.106  13.296  12.623  1.00 10.04 ? 201 THR   B CG2 1 
ATOM   3923 N  N   . VAL   B 2 202 ? 41.206  10.450  10.925  1.00 8.55  ? 202 VAL   B N   1 
ATOM   3924 C  CA  . VAL   B 2 202 ? 40.610  10.483  9.595   1.00 8.55  ? 202 VAL   B CA  1 
ATOM   3925 C  C   . VAL   B 2 202 ? 39.088  10.377  9.684   1.00 8.42  ? 202 VAL   B C   1 
ATOM   3926 O  O   . VAL   B 2 202 ? 38.387  10.989  8.877   1.00 8.95  ? 202 VAL   B O   1 
ATOM   3927 C  CB  . VAL   B 2 202 ? 41.177  9.403   8.665   1.00 8.69  ? 202 VAL   B CB  1 
ATOM   3928 C  CG1 . VAL   B 2 202 ? 40.879  8.000   9.155   1.00 9.08  ? 202 VAL   B CG1 1 
ATOM   3929 C  CG2 . VAL   B 2 202 ? 40.677  9.597   7.250   1.00 9.27  ? 202 VAL   B CG2 1 
ATOM   3930 N  N   . ASN   B 2 203 ? 38.589  9.650   10.682  1.00 8.66  ? 203 ASN   B N   1 
ATOM   3931 C  CA  . ASN   B 2 203 ? 37.155  9.479   10.844  1.00 9.10  ? 203 ASN   B CA  1 
ATOM   3932 C  C   . ASN   B 2 203 ? 36.526  10.709  11.507  1.00 9.20  ? 203 ASN   B C   1 
ATOM   3933 O  O   . ASN   B 2 203 ? 35.419  11.094  11.155  1.00 9.08  ? 203 ASN   B O   1 
ATOM   3934 C  CB  . ASN   B 2 203 ? 36.840  8.212   11.624  1.00 9.16  ? 203 ASN   B CB  1 
ATOM   3935 C  CG  . ASN   B 2 203 ? 37.143  6.930   10.868  1.00 9.49  ? 203 ASN   B CG  1 
ATOM   3936 O  OD1 . ASN   B 2 203 ? 37.525  6.935   9.697   1.00 10.22 ? 203 ASN   B OD1 1 
ATOM   3937 N  ND2 . ASN   B 2 203 ? 36.951  5.811   11.531  1.00 8.78  ? 203 ASN   B ND2 1 
ATOM   3938 N  N   . VAL   B 2 204 ? 37.232  11.342  12.453  1.00 9.71  ? 204 VAL   B N   1 
ATOM   3939 C  CA  . VAL   B 2 204 ? 36.738  12.604  13.007  1.00 10.46 ? 204 VAL   B CA  1 
ATOM   3940 C  C   . VAL   B 2 204 ? 36.606  13.653  11.892  1.00 10.41 ? 204 VAL   B C   1 
ATOM   3941 O  O   . VAL   B 2 204 ? 35.603  14.391  11.842  1.00 10.29 ? 204 VAL   B O   1 
ATOM   3942 C  CB  . VAL   B 2 204 ? 37.618  13.104  14.170  1.00 10.85 ? 204 VAL   B CB  1 
ATOM   3943 C  CG1 . VAL   B 2 204 ? 37.238  14.517  14.647  1.00 11.54 ? 204 VAL   B CG1 1 
ATOM   3944 C  CG2 . VAL   B 2 204 ? 37.566  12.147  15.336  1.00 11.56 ? 204 VAL   B CG2 1 
ATOM   3945 N  N   . LEU   B 2 205 ? 37.599  13.689  10.991  1.00 9.34  ? 205 LEU   B N   1 
ATOM   3946 C  CA  . LEU   B 2 205 ? 37.561  14.608  9.859   1.00 9.60  ? 205 LEU   B CA  1 
ATOM   3947 C  C   . LEU   B 2 205 ? 36.355  14.297  8.972   1.00 9.26  ? 205 LEU   B C   1 
ATOM   3948 O  O   . LEU   B 2 205 ? 35.658  15.216  8.550   1.00 9.37  ? 205 LEU   B O   1 
ATOM   3949 C  CB  . LEU   B 2 205 ? 38.883  14.532  9.079   1.00 9.43  ? 205 LEU   B CB  1 
ATOM   3950 C  CG  . LEU   B 2 205 ? 40.084  15.132  9.802   1.00 10.12 ? 205 LEU   B CG  1 
ATOM   3951 C  CD1 . LEU   B 2 205 ? 41.379  14.841  9.068   1.00 10.47 ? 205 LEU   B CD1 1 
ATOM   3952 C  CD2 . LEU   B 2 205 ? 39.912  16.643  9.978   1.00 10.55 ? 205 LEU   B CD2 1 
ATOM   3953 N  N   . ALA   B 2 206 ? 36.091  13.011  8.728   1.00 9.58  ? 206 ALA   B N   1 
ATOM   3954 C  CA  . ALA   B 2 206 ? 34.940  12.602  7.935   1.00 10.41 ? 206 ALA   B CA  1 
ATOM   3955 C  C   . ALA   B 2 206 ? 33.644  13.109  8.565   1.00 10.77 ? 206 ALA   B C   1 
ATOM   3956 O  O   . ALA   B 2 206 ? 32.735  13.545  7.857   1.00 9.67  ? 206 ALA   B O   1 
ATOM   3957 C  CB  . ALA   B 2 206 ? 34.894  11.099  7.793   1.00 10.91 ? 206 ALA   B CB  1 
ATOM   3958 N  N   . TRP   B 2 207 ? 33.586  13.043  9.905   1.00 11.48 ? 207 TRP   B N   1 
ATOM   3959 C  CA  . TRP   B 2 207 ? 32.415  13.472  10.665  1.00 11.62 ? 207 TRP   B CA  1 
ATOM   3960 C  C   . TRP   B 2 207 ? 32.263  14.995  10.625  1.00 11.22 ? 207 TRP   B C   1 
ATOM   3961 O  O   . TRP   B 2 207 ? 31.159  15.508  10.575  1.00 10.59 ? 207 TRP   B O   1 
ATOM   3962 C  CB  . TRP   B 2 207 ? 32.560  12.964  12.108  1.00 13.12 ? 207 TRP   B CB  1 
ATOM   3963 C  CG  . TRP   B 2 207 ? 31.499  13.376  13.091  1.00 14.33 ? 207 TRP   B CG  1 
ATOM   3964 C  CD1 . TRP   B 2 207 ? 31.581  14.309  14.077  1.00 16.58 ? 207 TRP   B CD1 1 
ATOM   3965 C  CD2 . TRP   B 2 207 ? 30.201  12.796  13.208  1.00 16.95 ? 207 TRP   B CD2 1 
ATOM   3966 N  NE1 . TRP   B 2 207 ? 30.414  14.377  14.785  1.00 17.39 ? 207 TRP   B NE1 1 
ATOM   3967 C  CE2 . TRP   B 2 207 ? 29.556  13.447  14.276  1.00 18.49 ? 207 TRP   B CE2 1 
ATOM   3968 C  CE3 . TRP   B 2 207 ? 29.538  11.780  12.523  1.00 19.45 ? 207 TRP   B CE3 1 
ATOM   3969 C  CZ2 . TRP   B 2 207 ? 28.265  13.119  14.662  1.00 21.20 ? 207 TRP   B CZ2 1 
ATOM   3970 C  CZ3 . TRP   B 2 207 ? 28.242  11.484  12.882  1.00 20.80 ? 207 TRP   B CZ3 1 
ATOM   3971 C  CH2 . TRP   B 2 207 ? 27.630  12.136  13.944  1.00 22.07 ? 207 TRP   B CH2 1 
ATOM   3972 N  N   . LEU   B 2 208 ? 33.376  15.750  10.624  1.00 11.57 ? 208 LEU   B N   1 
ATOM   3973 C  CA  . LEU   B 2 208 ? 33.287  17.198  10.414  1.00 10.77 ? 208 LEU   B CA  1 
ATOM   3974 C  C   . LEU   B 2 208 ? 32.739  17.525  9.017   1.00 10.74 ? 208 LEU   B C   1 
ATOM   3975 O  O   . LEU   B 2 208 ? 31.898  18.419  8.857   1.00 10.42 ? 208 LEU   B O   1 
ATOM   3976 C  CB  . LEU   B 2 208 ? 34.652  17.842  10.640  1.00 10.72 ? 208 LEU   B CB  1 
ATOM   3977 C  CG  . LEU   B 2 208 ? 35.192  17.744  12.070  1.00 11.27 ? 208 LEU   B CG  1 
ATOM   3978 C  CD1 . LEU   B 2 208 ? 36.544  18.391  12.174  1.00 11.55 ? 208 LEU   B CD1 1 
ATOM   3979 C  CD2 . LEU   B 2 208 ? 34.256  18.401  13.060  1.00 12.03 ? 208 LEU   B CD2 1 
ATOM   3980 N  N   . TYR   B 2 209 ? 33.170  16.760  8.007   1.00 9.78  ? 209 TYR   B N   1 
ATOM   3981 C  CA  . TYR   B 2 209 ? 32.632  16.919  6.669   1.00 9.75  ? 209 TYR   B CA  1 
ATOM   3982 C  C   . TYR   B 2 209 ? 31.123  16.643  6.661   1.00 9.15  ? 209 TYR   B C   1 
ATOM   3983 O  O   . TYR   B 2 209 ? 30.377  17.373  6.008   1.00 8.60  ? 209 TYR   B O   1 
ATOM   3984 C  CB  . TYR   B 2 209 ? 33.374  16.075  5.635   1.00 9.61  ? 209 TYR   B CB  1 
ATOM   3985 C  CG  . TYR   B 2 209 ? 34.686  16.655  5.135   1.00 10.21 ? 209 TYR   B CG  1 
ATOM   3986 C  CD1 . TYR   B 2 209 ? 34.695  17.722  4.258   1.00 10.60 ? 209 TYR   B CD1 1 
ATOM   3987 C  CD2 . TYR   B 2 209 ? 35.909  16.126  5.511   1.00 10.21 ? 209 TYR   B CD2 1 
ATOM   3988 C  CE1 . TYR   B 2 209 ? 35.870  18.265  3.772   1.00 10.27 ? 209 TYR   B CE1 1 
ATOM   3989 C  CE2 . TYR   B 2 209 ? 37.098  16.658  5.019   1.00 11.01 ? 209 TYR   B CE2 1 
ATOM   3990 C  CZ  . TYR   B 2 209 ? 37.079  17.735  4.159   1.00 10.54 ? 209 TYR   B CZ  1 
ATOM   3991 O  OH  . TYR   B 2 209 ? 38.226  18.268  3.671   1.00 11.06 ? 209 TYR   B OH  1 
ATOM   3992 N  N   . ALA   B 2 210 ? 30.704  15.535  7.276   1.00 8.94  ? 210 ALA   B N   1 
ATOM   3993 C  CA  . ALA   B 2 210 ? 29.294  15.188  7.414   1.00 9.28  ? 210 ALA   B CA  1 
ATOM   3994 C  C   . ALA   B 2 210 ? 28.510  16.371  7.990   1.00 9.44  ? 210 ALA   B C   1 
ATOM   3995 O  O   . ALA   B 2 210 ? 27.430  16.689  7.503   1.00 9.69  ? 210 ALA   B O   1 
ATOM   3996 C  CB  . ALA   B 2 210 ? 29.107  13.981  8.308   1.00 9.14  ? 210 ALA   B CB  1 
ATOM   3997 N  N   . ALA   B 2 211 ? 29.055  16.990  9.028   1.00 9.44  ? 211 ALA   B N   1 
ATOM   3998 C  CA  . ALA   B 2 211 ? 28.416  18.115  9.681   1.00 9.89  ? 211 ALA   B CA  1 
ATOM   3999 C  C   . ALA   B 2 211 ? 28.255  19.280  8.708   1.00 10.41 ? 211 ALA   B C   1 
ATOM   4000 O  O   . ALA   B 2 211 ? 27.182  19.874  8.620   1.00 10.52 ? 211 ALA   B O   1 
ATOM   4001 C  CB  . ALA   B 2 211 ? 29.234  18.510  10.873  1.00 10.07 ? 211 ALA   B CB  1 
ATOM   4002 N  N   . VAL   B 2 212 ? 29.321  19.599  7.960   1.00 10.65 ? 212 VAL   B N   1 
ATOM   4003 C  CA  . VAL   B 2 212 ? 29.274  20.639  6.937   1.00 10.00 ? 212 VAL   B CA  1 
ATOM   4004 C  C   . VAL   B 2 212 ? 28.195  20.336  5.898   1.00 10.18 ? 212 VAL   B C   1 
ATOM   4005 O  O   . VAL   B 2 212 ? 27.438  21.231  5.550   1.00 10.23 ? 212 VAL   B O   1 
ATOM   4006 C  CB  . VAL   B 2 212 ? 30.657  20.843  6.308   1.00 10.01 ? 212 VAL   B CB  1 
ATOM   4007 C  CG1 . VAL   B 2 212 ? 30.627  21.683  5.037   1.00 10.06 ? 212 VAL   B CG1 1 
ATOM   4008 C  CG2 . VAL   B 2 212 ? 31.594  21.440  7.338   1.00 10.73 ? 212 VAL   B CG2 1 
ATOM   4009 N  N   . ILE   B 2 213 ? 28.153  19.100  5.380   1.00 10.63 ? 213 ILE   B N   1 
ATOM   4010 C  CA  . ILE   B 2 213 ? 27.183  18.704  4.368   1.00 11.22 ? 213 ILE   B CA  1 
ATOM   4011 C  C   . ILE   B 2 213 ? 25.774  19.018  4.871   1.00 12.34 ? 213 ILE   B C   1 
ATOM   4012 O  O   . ILE   B 2 213 ? 24.912  19.448  4.088   1.00 11.66 ? 213 ILE   B O   1 
ATOM   4013 C  CB  . ILE   B 2 213 ? 27.357  17.219  3.988   1.00 11.32 ? 213 ILE   B CB  1 
ATOM   4014 C  CG1 . ILE   B 2 213 ? 28.578  16.992  3.101   1.00 11.43 ? 213 ILE   B CG1 1 
ATOM   4015 C  CG2 . ILE   B 2 213 ? 26.116  16.637  3.313   1.00 11.67 ? 213 ILE   B CG2 1 
ATOM   4016 C  CD1 . ILE   B 2 213 ? 29.085  15.533  3.186   1.00 11.38 ? 213 ILE   B CD1 1 
ATOM   4017 N  N   . ASN   B 2 214 ? 25.570  18.831  6.182   1.00 13.32 ? 214 ASN   B N   1 
ATOM   4018 C  CA  . ASN   B 2 214 ? 24.270  19.017  6.802   1.00 16.09 ? 214 ASN   B CA  1 
ATOM   4019 C  C   . ASN   B 2 214 ? 24.079  20.435  7.321   1.00 16.21 ? 214 ASN   B C   1 
ATOM   4020 O  O   . ASN   B 2 214 ? 23.110  20.669  8.037   1.00 17.88 ? 214 ASN   B O   1 
ATOM   4021 C  CB  . ASN   B 2 214 ? 24.049  18.005  7.932   1.00 17.07 ? 214 ASN   B CB  1 
ATOM   4022 C  CG  . ASN   B 2 214 ? 23.754  16.645  7.355   1.00 20.07 ? 214 ASN   B CG  1 
ATOM   4023 O  OD1 . ASN   B 2 214 ? 22.616  16.399  6.958   1.00 21.47 ? 214 ASN   B OD1 1 
ATOM   4024 N  ND2 . ASN   B 2 214 ? 24.783  15.813  7.173   1.00 21.04 ? 214 ASN   B ND2 1 
ATOM   4025 N  N   . GLY   B 2 215 ? 24.978  21.353  6.975   1.00 15.16 ? 215 GLY   B N   1 
ATOM   4026 C  CA  . GLY   B 2 215 ? 24.803  22.762  7.255   1.00 16.57 ? 215 GLY   B CA  1 
ATOM   4027 C  C   . GLY   B 2 215 ? 25.365  23.238  8.594   1.00 17.09 ? 215 GLY   B C   1 
ATOM   4028 O  O   . GLY   B 2 215 ? 25.177  24.405  8.953   1.00 17.11 ? 215 GLY   B O   1 
ATOM   4029 N  N   . ASP   B 2 216 ? 26.096  22.377  9.312   1.00 16.85 ? 216 ASP   B N   1 
ATOM   4030 C  CA  . ASP   B 2 216 ? 26.614  22.726  10.625  1.00 16.73 ? 216 ASP   B CA  1 
ATOM   4031 C  C   . ASP   B 2 216 ? 28.107  23.003  10.515  1.00 17.10 ? 216 ASP   B C   1 
ATOM   4032 O  O   . ASP   B 2 216 ? 28.914  22.066  10.455  1.00 18.26 ? 216 ASP   B O   1 
ATOM   4033 C  CB  . ASP   B 2 216 ? 26.252  21.599  11.599  1.00 18.57 ? 216 ASP   B CB  1 
ATOM   4034 C  CG  . ASP   B 2 216 ? 26.258  21.997  13.071  1.00 20.19 ? 216 ASP   B CG  1 
ATOM   4035 O  OD1 . ASP   B 2 216 ? 26.481  23.200  13.363  1.00 19.64 ? 216 ASP   B OD1 1 
ATOM   4036 O  OD2 . ASP   B 2 216 ? 26.090  21.098  13.912  1.00 22.01 ? 216 ASP   B OD2 1 
ATOM   4037 N  N   . ARG   B 2 217 ? 28.492  24.287  10.433  1.00 15.99 ? 217 ARG   B N   1 
ATOM   4038 C  CA  . ARG   B 2 217 ? 29.817  24.629  9.941   1.00 16.14 ? 217 ARG   B CA  1 
ATOM   4039 C  C   . ARG   B 2 217 ? 30.440  25.791  10.713  1.00 16.79 ? 217 ARG   B C   1 
ATOM   4040 O  O   . ARG   B 2 217 ? 31.411  26.401  10.245  1.00 14.82 ? 217 ARG   B O   1 
ATOM   4041 C  CB  . ARG   B 2 217 ? 29.751  24.923  8.432   1.00 16.87 ? 217 ARG   B CB  1 
ATOM   4042 C  CG  . ARG   B 2 217 ? 28.882  26.112  8.062   1.00 16.32 ? 217 ARG   B CG  1 
ATOM   4043 C  CD  . ARG   B 2 217 ? 28.706  26.226  6.566   1.00 15.24 ? 217 ARG   B CD  1 
ATOM   4044 N  NE  . ARG   B 2 217 ? 27.791  27.327  6.298   1.00 13.88 ? 217 ARG   B NE  1 
ATOM   4045 C  CZ  . ARG   B 2 217 ? 26.534  27.191  5.902   1.00 14.57 ? 217 ARG   B CZ  1 
ATOM   4046 N  NH1 . ARG   B 2 217 ? 26.094  26.018  5.494   1.00 13.69 ? 217 ARG   B NH1 1 
ATOM   4047 N  NH2 . ARG   B 2 217 ? 25.737  28.257  5.840   1.00 14.85 ? 217 ARG   B NH2 1 
ATOM   4048 N  N   . TRP   B 2 218 ? 29.949  26.036  11.939  1.00 17.78 ? 218 TRP   B N   1 
ATOM   4049 C  CA  . TRP   B 2 218 ? 30.490  27.101  12.768  1.00 17.30 ? 218 TRP   B CA  1 
ATOM   4050 C  C   . TRP   B 2 218 ? 31.994  26.938  12.957  1.00 17.32 ? 218 TRP   B C   1 
ATOM   4051 O  O   . TRP   B 2 218 ? 32.683  27.934  13.126  1.00 18.82 ? 218 TRP   B O   1 
ATOM   4052 C  CB  . TRP   B 2 218 ? 29.750  27.157  14.114  1.00 17.68 ? 218 TRP   B CB  1 
ATOM   4053 C  CG  . TRP   B 2 218 ? 29.891  25.925  14.974  1.00 17.62 ? 218 TRP   B CG  1 
ATOM   4054 C  CD1 . TRP   B 2 218 ? 29.010  24.895  15.082  1.00 18.24 ? 218 TRP   B CD1 1 
ATOM   4055 C  CD2 . TRP   B 2 218 ? 30.949  25.635  15.908  1.00 18.81 ? 218 TRP   B CD2 1 
ATOM   4056 N  NE1 . TRP   B 2 218 ? 29.480  23.958  15.968  1.00 19.28 ? 218 TRP   B NE1 1 
ATOM   4057 C  CE2 . TRP   B 2 218 ? 30.660  24.394  16.503  1.00 18.45 ? 218 TRP   B CE2 1 
ATOM   4058 C  CE3 . TRP   B 2 218 ? 32.125  26.295  16.283  1.00 20.81 ? 218 TRP   B CE3 1 
ATOM   4059 C  CZ2 . TRP   B 2 218 ? 31.493  23.802  17.454  1.00 20.52 ? 218 TRP   B CZ2 1 
ATOM   4060 C  CZ3 . TRP   B 2 218 ? 32.951  25.712  17.221  1.00 21.51 ? 218 TRP   B CZ3 1 
ATOM   4061 C  CH2 . TRP   B 2 218 ? 32.633  24.487  17.806  1.00 20.64 ? 218 TRP   B CH2 1 
ATOM   4062 N  N   . PHE   B 2 219 ? 32.505  25.699  12.908  1.00 16.62 ? 219 PHE   B N   1 
ATOM   4063 C  CA  . PHE   B 2 219 ? 33.879  25.398  13.303  1.00 17.96 ? 219 PHE   B CA  1 
ATOM   4064 C  C   . PHE   B 2 219 ? 34.895  25.601  12.169  1.00 19.57 ? 219 PHE   B C   1 
ATOM   4065 O  O   . PHE   B 2 219 ? 36.094  25.520  12.413  1.00 20.04 ? 219 PHE   B O   1 
ATOM   4066 C  CB  . PHE   B 2 219 ? 33.958  23.966  13.839  1.00 18.27 ? 219 PHE   B CB  1 
ATOM   4067 C  CG  . PHE   B 2 219 ? 33.373  22.957  12.890  1.00 18.13 ? 219 PHE   B CG  1 
ATOM   4068 C  CD1 . PHE   B 2 219 ? 34.109  22.498  11.801  1.00 18.05 ? 219 PHE   B CD1 1 
ATOM   4069 C  CD2 . PHE   B 2 219 ? 32.059  22.554  13.021  1.00 18.40 ? 219 PHE   B CD2 1 
ATOM   4070 C  CE1 . PHE   B 2 219 ? 33.538  21.627  10.893  1.00 17.46 ? 219 PHE   B CE1 1 
ATOM   4071 C  CE2 . PHE   B 2 219 ? 31.491  21.694  12.098  1.00 19.29 ? 219 PHE   B CE2 1 
ATOM   4072 C  CZ  . PHE   B 2 219 ? 32.245  21.218  11.042  1.00 17.60 ? 219 PHE   B CZ  1 
ATOM   4073 N  N   . LEU   B 2 220 ? 34.435  25.867  10.939  1.00 19.17 ? 220 LEU   B N   1 
ATOM   4074 C  CA  . LEU   B 2 220 ? 35.333  26.210  9.845   1.00 20.71 ? 220 LEU   B CA  1 
ATOM   4075 C  C   . LEU   B 2 220 ? 35.956  27.566  10.137  1.00 24.09 ? 220 LEU   B C   1 
ATOM   4076 O  O   . LEU   B 2 220 ? 35.239  28.458  10.575  1.00 24.38 ? 220 LEU   B O   1 
ATOM   4077 C  CB  . LEU   B 2 220 ? 34.556  26.277  8.525   1.00 19.78 ? 220 LEU   B CB  1 
ATOM   4078 C  CG  . LEU   B 2 220 ? 33.879  24.984  8.076   1.00 18.66 ? 220 LEU   B CG  1 
ATOM   4079 C  CD1 . LEU   B 2 220 ? 33.031  25.194  6.845   1.00 19.09 ? 220 LEU   B CD1 1 
ATOM   4080 C  CD2 . LEU   B 2 220 ? 34.904  23.891  7.802   1.00 19.48 ? 220 LEU   B CD2 1 
ATOM   4081 N  N   . ASN   B 2 221 ? 37.266  27.717  9.876   1.00 25.22 ? 221 ASN   B N   1 
ATOM   4082 C  CA  . ASN   B 2 221 ? 37.986  28.929  10.241  1.00 28.23 ? 221 ASN   B CA  1 
ATOM   4083 C  C   . ASN   B 2 221 ? 38.745  29.417  9.023   1.00 29.32 ? 221 ASN   B C   1 
ATOM   4084 O  O   . ASN   B 2 221 ? 38.586  28.869  7.935   1.00 28.29 ? 221 ASN   B O   1 
ATOM   4085 C  CB  . ASN   B 2 221 ? 38.888  28.717  11.468  1.00 30.12 ? 221 ASN   B CB  1 
ATOM   4086 C  CG  . ASN   B 2 221 ? 39.986  27.679  11.260  1.00 35.05 ? 221 ASN   B CG  1 
ATOM   4087 O  OD1 . ASN   B 2 221 ? 40.524  27.479  10.161  1.00 31.09 ? 221 ASN   B OD1 1 
ATOM   4088 N  ND2 . ASN   B 2 221 ? 40.358  27.022  12.341  1.00 36.17 ? 221 ASN   B ND2 1 
ATOM   4089 N  N   . ARG   B 2 222 ? 39.607  30.422  9.227   1.00 36.87 ? 222 ARG   B N   1 
ATOM   4090 C  CA  . ARG   B 2 222 ? 40.277  31.085  8.121   1.00 38.75 ? 222 ARG   B CA  1 
ATOM   4091 C  C   . ARG   B 2 222 ? 41.698  30.567  7.899   1.00 32.61 ? 222 ARG   B C   1 
ATOM   4092 O  O   . ARG   B 2 222 ? 42.403  31.108  7.058   1.00 32.93 ? 222 ARG   B O   1 
ATOM   4093 C  CB  . ARG   B 2 222 ? 40.324  32.587  8.406   1.00 45.58 ? 222 ARG   B CB  1 
ATOM   4094 C  CG  . ARG   B 2 222 ? 40.342  33.431  7.148   1.00 47.19 ? 222 ARG   B CG  1 
ATOM   4095 C  CD  . ARG   B 2 222 ? 41.079  34.725  7.418   1.00 56.27 ? 222 ARG   B CD  1 
ATOM   4096 N  NE  . ARG   B 2 222 ? 40.878  35.696  6.349   1.00 55.72 ? 222 ARG   B NE  1 
ATOM   4097 C  CZ  . ARG   B 2 222 ? 41.251  35.526  5.083   1.00 48.40 ? 222 ARG   B CZ  1 
ATOM   4098 N  NH1 . ARG   B 2 222 ? 41.901  34.433  4.703   1.00 43.65 ? 222 ARG   B NH1 1 
ATOM   4099 N  NH2 . ARG   B 2 222 ? 40.974  36.471  4.197   1.00 48.92 ? 222 ARG   B NH2 1 
ATOM   4100 N  N   . PHE   B 2 223 ? 42.083  29.496  8.598   1.00 32.31 ? 223 PHE   B N   1 
ATOM   4101 C  CA  . PHE   B 2 223 ? 43.463  29.031  8.643   1.00 30.65 ? 223 PHE   B CA  1 
ATOM   4102 C  C   . PHE   B 2 223 ? 43.667  27.716  7.885   1.00 24.99 ? 223 PHE   B C   1 
ATOM   4103 O  O   . PHE   B 2 223 ? 42.713  27.060  7.447   1.00 20.46 ? 223 PHE   B O   1 
ATOM   4104 C  CB  . PHE   B 2 223 ? 43.876  28.812  10.093  1.00 38.02 ? 223 PHE   B CB  1 
ATOM   4105 C  CG  . PHE   B 2 223 ? 43.799  30.041  10.964  1.00 49.65 ? 223 PHE   B CG  1 
ATOM   4106 C  CD1 . PHE   B 2 223 ? 44.441  31.217  10.594  1.00 55.45 ? 223 PHE   B CD1 1 
ATOM   4107 C  CD2 . PHE   B 2 223 ? 43.121  30.002  12.178  1.00 55.07 ? 223 PHE   B CD2 1 
ATOM   4108 C  CE1 . PHE   B 2 223 ? 44.388  32.336  11.413  1.00 60.63 ? 223 PHE   B CE1 1 
ATOM   4109 C  CE2 . PHE   B 2 223 ? 43.072  31.121  12.995  1.00 58.68 ? 223 PHE   B CE2 1 
ATOM   4110 C  CZ  . PHE   B 2 223 ? 43.706  32.283  12.612  1.00 57.23 ? 223 PHE   B CZ  1 
ATOM   4111 N  N   . THR   B 2 224 ? 44.949  27.371  7.701   1.00 19.77 ? 224 THR   B N   1 
ATOM   4112 C  CA  . THR   B 2 224 ? 45.356  26.084  7.167   1.00 18.40 ? 224 THR   B CA  1 
ATOM   4113 C  C   . THR   B 2 224 ? 46.601  25.612  7.922   1.00 17.22 ? 224 THR   B C   1 
ATOM   4114 O  O   . THR   B 2 224 ? 47.081  26.272  8.857   1.00 16.40 ? 224 THR   B O   1 
ATOM   4115 C  CB  . THR   B 2 224 ? 45.585  26.170  5.653   1.00 17.57 ? 224 THR   B CB  1 
ATOM   4116 O  OG1 . THR   B 2 224 ? 45.573  24.859  5.062   1.00 16.87 ? 224 THR   B OG1 1 
ATOM   4117 C  CG2 . THR   B 2 224 ? 46.872  26.882  5.291   1.00 17.26 ? 224 THR   B CG2 1 
ATOM   4118 N  N   . THR   B 2 225 ? 47.083  24.436  7.532   1.00 14.82 ? 225 THR   B N   1 
ATOM   4119 C  CA  . THR   B 2 225 ? 48.215  23.815  8.186   1.00 15.41 ? 225 THR   B CA  1 
ATOM   4120 C  C   . THR   B 2 225 ? 48.853  22.890  7.159   1.00 15.35 ? 225 THR   B C   1 
ATOM   4121 O  O   . THR   B 2 225 ? 48.209  22.515  6.163   1.00 14.79 ? 225 THR   B O   1 
ATOM   4122 C  CB  . THR   B 2 225 ? 47.761  23.095  9.468   1.00 15.64 ? 225 THR   B CB  1 
ATOM   4123 O  OG1 . THR   B 2 225 ? 48.862  22.445  10.085  1.00 15.30 ? 225 THR   B OG1 1 
ATOM   4124 C  CG2 . THR   B 2 225 ? 46.755  22.009  9.171   1.00 15.50 ? 225 THR   B CG2 1 
ATOM   4125 N  N   . THR   B 2 226 ? 50.119  22.548  7.385   1.00 15.11 ? 226 THR   B N   1 
ATOM   4126 C  CA  . THR   B 2 226 ? 50.725  21.445  6.657   1.00 15.31 ? 226 THR   B CA  1 
ATOM   4127 C  C   . THR   B 2 226 ? 50.260  20.151  7.319   1.00 14.33 ? 226 THR   B C   1 
ATOM   4128 O  O   . THR   B 2 226 ? 49.890  20.138  8.491   1.00 13.30 ? 226 THR   B O   1 
ATOM   4129 C  CB  . THR   B 2 226 ? 52.261  21.552  6.640   1.00 16.27 ? 226 THR   B CB  1 
ATOM   4130 O  OG1 . THR   B 2 226 ? 52.695  21.488  7.987   1.00 15.73 ? 226 THR   B OG1 1 
ATOM   4131 C  CG2 . THR   B 2 226 ? 52.781  22.846  6.035   1.00 17.10 ? 226 THR   B CG2 1 
ATOM   4132 N  N   . LEU   B 2 227 ? 50.331  19.043  6.571   1.00 14.42 ? 227 LEU   B N   1 
ATOM   4133 C  CA  . LEU   B 2 227 ? 50.005  17.744  7.143   1.00 14.03 ? 227 LEU   B CA  1 
ATOM   4134 C  C   . LEU   B 2 227 ? 50.957  17.411  8.291   1.00 13.92 ? 227 LEU   B C   1 
ATOM   4135 O  O   . LEU   B 2 227 ? 50.524  16.934  9.344   1.00 13.40 ? 227 LEU   B O   1 
ATOM   4136 C  CB  . LEU   B 2 227 ? 50.079  16.677  6.054   1.00 14.52 ? 227 LEU   B CB  1 
ATOM   4137 C  CG  . LEU   B 2 227 ? 49.506  15.313  6.444   1.00 14.66 ? 227 LEU   B CG  1 
ATOM   4138 C  CD1 . LEU   B 2 227 ? 48.010  15.406  6.744   1.00 15.47 ? 227 LEU   B CD1 1 
ATOM   4139 C  CD2 . LEU   B 2 227 ? 49.755  14.301  5.327   1.00 14.34 ? 227 LEU   B CD2 1 
ATOM   4140 N  N   . ASN   B 2 228 ? 52.248  17.694  8.106   1.00 14.02 ? 228 ASN   B N   1 
ATOM   4141 C  CA  . ASN   B 2 228 ? 53.250  17.354  9.115   1.00 13.75 ? 228 ASN   B CA  1 
ATOM   4142 C  C   . ASN   B 2 228 ? 52.971  18.116  10.409  1.00 13.69 ? 228 ASN   B C   1 
ATOM   4143 O  O   . ASN   B 2 228 ? 52.976  17.520  11.483  1.00 13.43 ? 228 ASN   B O   1 
ATOM   4144 C  CB  . ASN   B 2 228 ? 54.666  17.599  8.574   1.00 13.49 ? 228 ASN   B CB  1 
ATOM   4145 C  CG  . ASN   B 2 228 ? 55.779  17.362  9.577   1.00 13.49 ? 228 ASN   B CG  1 
ATOM   4146 O  OD1 . ASN   B 2 228 ? 56.514  18.285  9.920   1.00 12.74 ? 228 ASN   B OD1 1 
ATOM   4147 N  ND2 . ASN   B 2 228 ? 55.897  16.136  10.083  1.00 13.84 ? 228 ASN   B ND2 1 
ATOM   4148 N  N   A ASP   B 2 229 ? 52.735  19.433  10.315  0.50 14.65 ? 229 ASP   B N   1 
ATOM   4149 N  N   B ASP   B 2 229 ? 52.728  19.428  10.320  0.50 14.43 ? 229 ASP   B N   1 
ATOM   4150 C  CA  A ASP   B 2 229 ? 52.490  20.242  11.502  0.50 15.23 ? 229 ASP   B CA  1 
ATOM   4151 C  CA  B ASP   B 2 229 ? 52.498  20.204  11.529  0.50 14.78 ? 229 ASP   B CA  1 
ATOM   4152 C  C   A ASP   B 2 229 ? 51.251  19.730  12.238  0.50 14.67 ? 229 ASP   B C   1 
ATOM   4153 C  C   B ASP   B 2 229 ? 51.256  19.688  12.249  0.50 14.47 ? 229 ASP   B C   1 
ATOM   4154 O  O   A ASP   B 2 229 ? 51.233  19.668  13.472  0.50 14.52 ? 229 ASP   B O   1 
ATOM   4155 O  O   B ASP   B 2 229 ? 51.241  19.587  13.482  0.50 14.31 ? 229 ASP   B O   1 
ATOM   4156 C  CB  A ASP   B 2 229 ? 52.312  21.726  11.154  0.50 17.05 ? 229 ASP   B CB  1 
ATOM   4157 C  CB  B ASP   B 2 229 ? 52.315  21.696  11.242  0.50 16.32 ? 229 ASP   B CB  1 
ATOM   4158 C  CG  A ASP   B 2 229 ? 53.601  22.470  10.838  0.50 17.81 ? 229 ASP   B CG  1 
ATOM   4159 C  CG  B ASP   B 2 229 ? 52.358  22.505  12.520  0.50 16.12 ? 229 ASP   B CG  1 
ATOM   4160 O  OD1 A ASP   B 2 229 ? 54.698  21.912  11.117  0.50 18.30 ? 229 ASP   B OD1 1 
ATOM   4161 O  OD1 B ASP   B 2 229 ? 53.433  22.581  13.097  0.50 16.86 ? 229 ASP   B OD1 1 
ATOM   4162 O  OD2 A ASP   B 2 229 ? 53.496  23.591  10.287  0.50 17.24 ? 229 ASP   B OD2 1 
ATOM   4163 O  OD2 B ASP   B 2 229 ? 51.295  22.957  12.971  0.50 18.53 ? 229 ASP   B OD2 1 
ATOM   4164 N  N   . PHE   B 2 230 ? 50.208  19.372  11.471  1.00 13.97 ? 230 PHE   B N   1 
ATOM   4165 C  CA  . PHE   B 2 230 ? 48.965  18.867  12.036  1.00 13.20 ? 230 PHE   B CA  1 
ATOM   4166 C  C   . PHE   B 2 230 ? 49.255  17.582  12.815  1.00 12.89 ? 230 PHE   B C   1 
ATOM   4167 O  O   . PHE   B 2 230 ? 48.755  17.381  13.918  1.00 11.86 ? 230 PHE   B O   1 
ATOM   4168 C  CB  . PHE   B 2 230 ? 47.912  18.606  10.948  1.00 13.13 ? 230 PHE   B CB  1 
ATOM   4169 C  CG  . PHE   B 2 230 ? 46.691  17.937  11.497  1.00 14.06 ? 230 PHE   B CG  1 
ATOM   4170 C  CD1 . PHE   B 2 230 ? 45.786  18.640  12.274  1.00 14.05 ? 230 PHE   B CD1 1 
ATOM   4171 C  CD2 . PHE   B 2 230 ? 46.492  16.579  11.313  1.00 15.33 ? 230 PHE   B CD2 1 
ATOM   4172 C  CE1 . PHE   B 2 230 ? 44.688  18.012  12.841  1.00 15.22 ? 230 PHE   B CE1 1 
ATOM   4173 C  CE2 . PHE   B 2 230 ? 45.394  15.948  11.883  1.00 16.51 ? 230 PHE   B CE2 1 
ATOM   4174 C  CZ  . PHE   B 2 230 ? 44.493  16.671  12.650  1.00 16.10 ? 230 PHE   B CZ  1 
ATOM   4175 N  N   . ASN   B 2 231 ? 50.024  16.685  12.189  1.00 12.53 ? 231 ASN   B N   1 
ATOM   4176 C  CA  . ASN   B 2 231 ? 50.286  15.374  12.751  1.00 12.69 ? 231 ASN   B CA  1 
ATOM   4177 C  C   . ASN   B 2 231 ? 50.998  15.518  14.084  1.00 13.49 ? 231 ASN   B C   1 
ATOM   4178 O  O   . ASN   B 2 231 ? 50.663  14.812  15.040  1.00 14.66 ? 231 ASN   B O   1 
ATOM   4179 C  CB  . ASN   B 2 231 ? 51.080  14.489  11.784  1.00 12.61 ? 231 ASN   B CB  1 
ATOM   4180 C  CG  . ASN   B 2 231 ? 50.190  13.768  10.798  1.00 12.12 ? 231 ASN   B CG  1 
ATOM   4181 O  OD1 . ASN   B 2 231 ? 48.962  13.878  10.865  1.00 12.74 ? 231 ASN   B OD1 1 
ATOM   4182 N  ND2 . ASN   B 2 231 ? 50.779  13.009  9.898   1.00 12.72 ? 231 ASN   B ND2 1 
ATOM   4183 N  N   . LEU   B 2 232 ? 51.917  16.484  14.147  1.00 13.26 ? 232 LEU   B N   1 
ATOM   4184 C  CA  . LEU   B 2 232 ? 52.678  16.710  15.345  1.00 14.68 ? 232 LEU   B CA  1 
ATOM   4185 C  C   . LEU   B 2 232 ? 51.772  17.215  16.462  1.00 15.83 ? 232 LEU   B C   1 
ATOM   4186 O  O   . LEU   B 2 232 ? 51.930  16.784  17.610  1.00 15.14 ? 232 LEU   B O   1 
ATOM   4187 C  CB  . LEU   B 2 232 ? 53.829  17.679  15.062  1.00 15.23 ? 232 LEU   B CB  1 
ATOM   4188 C  CG  . LEU   B 2 232 ? 54.957  17.134  14.186  1.00 15.41 ? 232 LEU   B CG  1 
ATOM   4189 C  CD1 . LEU   B 2 232 ? 56.016  18.194  13.988  1.00 15.64 ? 232 LEU   B CD1 1 
ATOM   4190 C  CD2 . LEU   B 2 232 ? 55.592  15.871  14.769  1.00 16.78 ? 232 LEU   B CD2 1 
ATOM   4191 N  N   . VAL   B 2 233 ? 50.819  18.094  16.123  1.00 16.22 ? 233 VAL   B N   1 
ATOM   4192 C  CA  . VAL   B 2 233 ? 49.886  18.603  17.116  1.00 18.15 ? 233 VAL   B CA  1 
ATOM   4193 C  C   . VAL   B 2 233 ? 48.949  17.483  17.563  1.00 17.80 ? 233 VAL   B C   1 
ATOM   4194 O  O   . VAL   B 2 233 ? 48.722  17.345  18.754  1.00 18.16 ? 233 VAL   B O   1 
ATOM   4195 C  CB  . VAL   B 2 233 ? 49.096  19.823  16.596  1.00 19.98 ? 233 VAL   B CB  1 
ATOM   4196 C  CG1 . VAL   B 2 233 ? 47.993  20.228  17.553  1.00 21.92 ? 233 VAL   B CG1 1 
ATOM   4197 C  CG2 . VAL   B 2 233 ? 50.010  21.014  16.365  1.00 22.15 ? 233 VAL   B CG2 1 
ATOM   4198 N  N   . ALA   B 2 234 ? 48.363  16.752  16.605  1.00 17.29 ? 234 ALA   B N   1 
ATOM   4199 C  CA  . ALA   B 2 234 ? 47.378  15.715  16.892  1.00 18.13 ? 234 ALA   B CA  1 
ATOM   4200 C  C   . ALA   B 2 234 ? 47.891  14.728  17.945  1.00 18.16 ? 234 ALA   B C   1 
ATOM   4201 O  O   . ALA   B 2 234 ? 47.155  14.300  18.838  1.00 17.74 ? 234 ALA   B O   1 
ATOM   4202 C  CB  . ALA   B 2 234 ? 47.010  14.992  15.629  1.00 18.64 ? 234 ALA   B CB  1 
ATOM   4203 N  N   . MET   B 2 235 ? 49.145  14.320  17.801  1.00 18.76 ? 235 MET   B N   1 
ATOM   4204 C  CA  . MET   B 2 235 ? 49.718  13.323  18.680  1.00 21.59 ? 235 MET   B CA  1 
ATOM   4205 C  C   . MET   B 2 235 ? 49.754  13.857  20.109  1.00 21.53 ? 235 MET   B C   1 
ATOM   4206 O  O   . MET   B 2 235 ? 49.625  13.069  21.034  1.00 19.89 ? 235 MET   B O   1 
ATOM   4207 C  CB  . MET   B 2 235 ? 51.117  12.932  18.204  1.00 27.08 ? 235 MET   B CB  1 
ATOM   4208 C  CG  . MET   B 2 235 ? 51.008  12.041  16.952  1.00 33.34 ? 235 MET   B CG  1 
ATOM   4209 S  SD  . MET   B 2 235 ? 52.473  11.142  16.482  1.00 44.75 ? 235 MET   B SD  1 
ATOM   4210 C  CE  . MET   B 2 235 ? 53.751  12.309  16.984  1.00 40.96 ? 235 MET   B CE  1 
ATOM   4211 N  N   . LYS   B 2 236 ? 49.818  15.185  20.281  1.00 20.09 ? 236 LYS   B N   1 
ATOM   4212 C  CA  . LYS   B 2 236 ? 49.831  15.768  21.610  1.00 21.97 ? 236 LYS   B CA  1 
ATOM   4213 C  C   . LYS   B 2 236 ? 48.466  15.655  22.263  1.00 20.31 ? 236 LYS   B C   1 
ATOM   4214 O  O   . LYS   B 2 236 ? 48.383  15.743  23.479  1.00 19.99 ? 236 LYS   B O   1 
ATOM   4215 C  CB  . LYS   B 2 236 ? 50.227  17.242  21.554  1.00 26.03 ? 236 LYS   B CB  1 
ATOM   4216 C  CG  . LYS   B 2 236 ? 51.619  17.491  21.018  1.00 29.80 ? 236 LYS   B CG  1 
ATOM   4217 C  CD  . LYS   B 2 236 ? 52.720  17.039  21.936  1.00 35.63 ? 236 LYS   B CD  1 
ATOM   4218 C  CE  . LYS   B 2 236 ? 54.093  17.274  21.338  1.00 39.82 ? 236 LYS   B CE  1 
ATOM   4219 N  NZ  . LYS   B 2 236 ? 54.204  18.643  20.762  1.00 44.05 ? 236 LYS   B NZ  1 
ATOM   4220 N  N   . TYR   B 2 237 ? 47.395  15.486  21.458  1.00 17.84 ? 237 TYR   B N   1 
ATOM   4221 C  CA  . TYR   B 2 237 ? 46.065  15.274  22.000  1.00 17.22 ? 237 TYR   B CA  1 
ATOM   4222 C  C   . TYR   B 2 237 ? 45.584  13.820  21.881  1.00 16.88 ? 237 TYR   B C   1 
ATOM   4223 O  O   . TYR   B 2 237 ? 44.381  13.571  21.952  1.00 17.59 ? 237 TYR   B O   1 
ATOM   4224 C  CB  . TYR   B 2 237 ? 45.082  16.215  21.294  1.00 16.86 ? 237 TYR   B CB  1 
ATOM   4225 C  CG  . TYR   B 2 237 ? 45.361  17.672  21.632  1.00 18.79 ? 237 TYR   B CG  1 
ATOM   4226 C  CD1 . TYR   B 2 237 ? 46.240  18.428  20.877  1.00 18.31 ? 237 TYR   B CD1 1 
ATOM   4227 C  CD2 . TYR   B 2 237 ? 44.784  18.265  22.754  1.00 19.38 ? 237 TYR   B CD2 1 
ATOM   4228 C  CE1 . TYR   B 2 237 ? 46.546  19.735  21.227  1.00 20.42 ? 237 TYR   B CE1 1 
ATOM   4229 C  CE2 . TYR   B 2 237 ? 45.084  19.567  23.118  1.00 19.50 ? 237 TYR   B CE2 1 
ATOM   4230 C  CZ  . TYR   B 2 237 ? 45.965  20.303  22.352  1.00 19.95 ? 237 TYR   B CZ  1 
ATOM   4231 O  OH  . TYR   B 2 237 ? 46.255  21.593  22.649  1.00 21.49 ? 237 TYR   B OH  1 
ATOM   4232 N  N   A ASN   B 2 238 ? 46.520  12.887  21.676  0.47 16.59 ? 238 ASN   B N   1 
ATOM   4233 N  N   B ASN   B 2 238 ? 46.505  12.882  21.660  0.53 16.49 ? 238 ASN   B N   1 
ATOM   4234 C  CA  A ASN   B 2 238 ? 46.230  11.462  21.543  0.47 16.16 ? 238 ASN   B CA  1 
ATOM   4235 C  CA  B ASN   B 2 238 ? 46.168  11.465  21.590  0.53 16.02 ? 238 ASN   B CA  1 
ATOM   4236 C  C   A ASN   B 2 238 ? 45.288  11.184  20.370  0.47 15.66 ? 238 ASN   B C   1 
ATOM   4237 C  C   B ASN   B 2 238 ? 45.288  11.169  20.367  0.53 15.55 ? 238 ASN   B C   1 
ATOM   4238 O  O   A ASN   B 2 238 ? 44.412  10.329  20.467  0.47 14.15 ? 238 ASN   B O   1 
ATOM   4239 O  O   B ASN   B 2 238 ? 44.434  10.290  20.427  0.53 13.93 ? 238 ASN   B O   1 
ATOM   4240 C  CB  A ASN   B 2 238 ? 45.683  10.868  22.839  0.47 16.12 ? 238 ASN   B CB  1 
ATOM   4241 C  CB  B ASN   B 2 238 ? 45.483  11.006  22.881  0.53 15.99 ? 238 ASN   B CB  1 
ATOM   4242 C  CG  A ASN   B 2 238 ? 46.663  11.057  23.977  0.47 16.28 ? 238 ASN   B CG  1 
ATOM   4243 C  CG  B ASN   B 2 238 ? 45.708  9.545   23.206  0.53 16.20 ? 238 ASN   B CG  1 
ATOM   4244 O  OD1 A ASN   B 2 238 ? 47.838  10.741  23.848  0.47 16.85 ? 238 ASN   B OD1 1 
ATOM   4245 O  OD1 B ASN   B 2 238 ? 46.843  9.097   23.346  0.53 18.15 ? 238 ASN   B OD1 1 
ATOM   4246 N  ND2 A ASN   B 2 238 ? 46.213  11.650  25.064  0.47 17.79 ? 238 ASN   B ND2 1 
ATOM   4247 N  ND2 B ASN   B 2 238 ? 44.635  8.789   23.338  0.53 16.01 ? 238 ASN   B ND2 1 
ATOM   4248 N  N   . TYR   B 2 239 ? 45.511  11.902  19.267  1.00 15.61 ? 239 TYR   B N   1 
ATOM   4249 C  CA  . TYR   B 2 239 ? 44.878  11.624  17.987  1.00 15.02 ? 239 TYR   B CA  1 
ATOM   4250 C  C   . TYR   B 2 239 ? 45.894  10.932  17.095  1.00 14.93 ? 239 TYR   B C   1 
ATOM   4251 O  O   . TYR   B 2 239 ? 47.078  11.228  17.176  1.00 15.40 ? 239 TYR   B O   1 
ATOM   4252 C  CB  . TYR   B 2 239 ? 44.426  12.922  17.310  1.00 13.69 ? 239 TYR   B CB  1 
ATOM   4253 C  CG  . TYR   B 2 239 ? 43.002  13.326  17.636  1.00 14.14 ? 239 TYR   B CG  1 
ATOM   4254 C  CD1 . TYR   B 2 239 ? 42.595  13.555  18.945  1.00 15.03 ? 239 TYR   B CD1 1 
ATOM   4255 C  CD2 . TYR   B 2 239 ? 42.063  13.475  16.630  1.00 14.76 ? 239 TYR   B CD2 1 
ATOM   4256 C  CE1 . TYR   B 2 239 ? 41.290  13.914  19.240  1.00 15.41 ? 239 TYR   B CE1 1 
ATOM   4257 C  CE2 . TYR   B 2 239 ? 40.769  13.852  16.899  1.00 14.09 ? 239 TYR   B CE2 1 
ATOM   4258 C  CZ  . TYR   B 2 239 ? 40.391  14.077  18.202  1.00 15.82 ? 239 TYR   B CZ  1 
ATOM   4259 O  OH  . TYR   B 2 239 ? 39.096  14.422  18.389  1.00 17.73 ? 239 TYR   B OH  1 
ATOM   4260 N  N   . GLU   B 2 240 ? 45.428  10.001  16.272  1.00 16.01 ? 240 GLU   B N   1 
ATOM   4261 C  CA  . GLU   B 2 240 ? 46.303  9.292   15.343  1.00 16.91 ? 240 GLU   B CA  1 
ATOM   4262 C  C   . GLU   B 2 240 ? 46.846  10.265  14.309  1.00 15.13 ? 240 GLU   B C   1 
ATOM   4263 O  O   . GLU   B 2 240 ? 46.160  11.220  13.938  1.00 15.00 ? 240 GLU   B O   1 
ATOM   4264 C  CB  . GLU   B 2 240 ? 45.537  8.179   14.623  1.00 20.09 ? 240 GLU   B CB  1 
ATOM   4265 C  CG  . GLU   B 2 240 ? 45.461  6.920   15.441  1.00 24.19 ? 240 GLU   B CG  1 
ATOM   4266 C  CD  . GLU   B 2 240 ? 46.835  6.322   15.674  1.00 29.51 ? 240 GLU   B CD  1 
ATOM   4267 O  OE1 . GLU   B 2 240 ? 47.477  5.884   14.666  1.00 30.07 ? 240 GLU   B OE1 1 
ATOM   4268 O  OE2 . GLU   B 2 240 ? 47.266  6.310   16.867  1.00 35.18 ? 240 GLU   B OE2 1 
ATOM   4269 N  N   . PRO   B 2 241 ? 48.107  10.103  13.870  1.00 14.57 ? 241 PRO   B N   1 
ATOM   4270 C  CA  . PRO   B 2 241 ? 48.601  10.876  12.741  1.00 13.56 ? 241 PRO   B CA  1 
ATOM   4271 C  C   . PRO   B 2 241 ? 47.862  10.458  11.477  1.00 13.76 ? 241 PRO   B C   1 
ATOM   4272 O  O   . PRO   B 2 241 ? 47.428  9.314   11.360  1.00 14.87 ? 241 PRO   B O   1 
ATOM   4273 C  CB  . PRO   B 2 241 ? 50.105  10.587  12.705  1.00 13.46 ? 241 PRO   B CB  1 
ATOM   4274 C  CG  . PRO   B 2 241 ? 50.288  9.307   13.484  1.00 14.51 ? 241 PRO   B CG  1 
ATOM   4275 C  CD  . PRO   B 2 241 ? 49.123  9.202   14.446  1.00 14.44 ? 241 PRO   B CD  1 
ATOM   4276 N  N   . LEU   B 2 242 ? 47.745  11.377  10.512  1.00 13.24 ? 242 LEU   B N   1 
ATOM   4277 C  CA  . LEU   B 2 242 ? 47.169  11.041  9.225   1.00 12.58 ? 242 LEU   B CA  1 
ATOM   4278 C  C   . LEU   B 2 242 ? 48.240  10.464  8.313   1.00 12.61 ? 242 LEU   B C   1 
ATOM   4279 O  O   . LEU   B 2 242 ? 49.360  10.973  8.286   1.00 12.60 ? 242 LEU   B O   1 
ATOM   4280 C  CB  . LEU   B 2 242 ? 46.582  12.284  8.566   1.00 12.73 ? 242 LEU   B CB  1 
ATOM   4281 C  CG  . LEU   B 2 242 ? 45.368  12.921  9.222   1.00 13.23 ? 242 LEU   B CG  1 
ATOM   4282 C  CD1 . LEU   B 2 242 ? 45.066  14.286  8.577   1.00 13.77 ? 242 LEU   B CD1 1 
ATOM   4283 C  CD2 . LEU   B 2 242 ? 44.160  12.010  9.119   1.00 12.97 ? 242 LEU   B CD2 1 
ATOM   4284 N  N   . THR   B 2 243 ? 47.821  9.483   7.495   1.00 11.29 ? 243 THR   B N   1 
ATOM   4285 C  CA  . THR   B 2 243 ? 48.625  8.942   6.421   1.00 11.50 ? 243 THR   B CA  1 
ATOM   4286 C  C   . THR   B 2 243 ? 48.240  9.606   5.086   1.00 11.43 ? 243 THR   B C   1 
ATOM   4287 O  O   . THR   B 2 243 ? 47.211  10.307  4.958   1.00 9.91  ? 243 THR   B O   1 
ATOM   4288 C  CB  . THR   B 2 243 ? 48.422  7.419   6.335   1.00 11.27 ? 243 THR   B CB  1 
ATOM   4289 O  OG1 . THR   B 2 243 ? 47.067  7.215   5.893   1.00 10.74 ? 243 THR   B OG1 1 
ATOM   4290 C  CG2 . THR   B 2 243 ? 48.680  6.695   7.639   1.00 10.71 ? 243 THR   B CG2 1 
ATOM   4291 N  N   . GLN   B 2 244 ? 49.085  9.382   4.074   1.00 12.06 ? 244 GLN   B N   1 
ATOM   4292 C  CA  . GLN   B 2 244 ? 48.753  9.843   2.731   1.00 12.75 ? 244 GLN   B CA  1 
ATOM   4293 C  C   . GLN   B 2 244 ? 47.454  9.191   2.233   1.00 11.68 ? 244 GLN   B C   1 
ATOM   4294 O  O   . GLN   B 2 244 ? 46.624  9.818   1.575   1.00 11.61 ? 244 GLN   B O   1 
ATOM   4295 C  CB  . GLN   B 2 244 ? 49.898  9.531   1.765   1.00 14.79 ? 244 GLN   B CB  1 
ATOM   4296 C  CG  . GLN   B 2 244 ? 49.743  10.233  0.421   1.00 16.03 ? 244 GLN   B CG  1 
ATOM   4297 C  CD  . GLN   B 2 244 ? 50.086  11.706  0.459   1.00 18.81 ? 244 GLN   B CD  1 
ATOM   4298 O  OE1 . GLN   B 2 244 ? 50.351  12.306  1.500   1.00 17.92 ? 244 GLN   B OE1 1 
ATOM   4299 N  NE2 . GLN   B 2 244 ? 50.118  12.303  -0.719  1.00 22.53 ? 244 GLN   B NE2 1 
ATOM   4300 N  N   . ASP   B 2 245 ? 47.275  7.905   2.528   1.00 12.54 ? 245 ASP   B N   1 
ATOM   4301 C  CA  . ASP   B 2 245 ? 46.053  7.189   2.168   1.00 13.59 ? 245 ASP   B CA  1 
ATOM   4302 C  C   . ASP   B 2 245 ? 44.825  7.856   2.802   1.00 13.02 ? 245 ASP   B C   1 
ATOM   4303 O  O   . ASP   B 2 245 ? 43.787  7.962   2.149   1.00 12.44 ? 245 ASP   B O   1 
ATOM   4304 C  CB  . ASP   B 2 245 ? 46.133  5.704   2.535   1.00 13.66 ? 245 ASP   B CB  1 
ATOM   4305 C  CG  . ASP   B 2 245 ? 47.071  4.894   1.645   1.00 14.91 ? 245 ASP   B CG  1 
ATOM   4306 O  OD1 . ASP   B 2 245 ? 47.601  5.450   0.677   1.00 15.39 ? 245 ASP   B OD1 1 
ATOM   4307 O  OD2 . ASP   B 2 245 ? 47.251  3.678   1.928   1.00 17.44 ? 245 ASP   B OD2 1 
ATOM   4308 N  N   . HIS   B 2 246 ? 44.938  8.253   4.079   1.00 12.93 ? 246 HIS   B N   1 
ATOM   4309 C  CA  . HIS   B 2 246 ? 43.869  8.969   4.764   1.00 13.31 ? 246 HIS   B CA  1 
ATOM   4310 C  C   . HIS   B 2 246 ? 43.496  10.258  4.042   1.00 14.22 ? 246 HIS   B C   1 
ATOM   4311 O  O   . HIS   B 2 246 ? 42.321  10.551  3.854   1.00 15.25 ? 246 HIS   B O   1 
ATOM   4312 C  CB  . HIS   B 2 246 ? 44.289  9.337   6.182   1.00 13.91 ? 246 HIS   B CB  1 
ATOM   4313 C  CG  . HIS   B 2 246 ? 44.296  8.180   7.100   1.00 14.21 ? 246 HIS   B CG  1 
ATOM   4314 N  ND1 . HIS   B 2 246 ? 45.036  8.199   8.264   1.00 15.00 ? 246 HIS   B ND1 1 
ATOM   4315 C  CD2 . HIS   B 2 246 ? 43.672  7.000   7.043   1.00 13.78 ? 246 HIS   B CD2 1 
ATOM   4316 C  CE1 . HIS   B 2 246 ? 44.854  7.040   8.895   1.00 14.81 ? 246 HIS   B CE1 1 
ATOM   4317 N  NE2 . HIS   B 2 246 ? 44.008  6.313   8.181   1.00 13.69 ? 246 HIS   B NE2 1 
ATOM   4318 N  N   . VAL   B 2 247 ? 44.505  11.039  3.642   1.00 13.57 ? 247 VAL   B N   1 
ATOM   4319 C  CA  . VAL   B 2 247 ? 44.260  12.255  2.895   1.00 13.67 ? 247 VAL   B CA  1 
ATOM   4320 C  C   . VAL   B 2 247 ? 43.484  11.941  1.618   1.00 13.09 ? 247 VAL   B C   1 
ATOM   4321 O  O   . VAL   B 2 247 ? 42.536  12.642  1.294   1.00 11.44 ? 247 VAL   B O   1 
ATOM   4322 C  CB  . VAL   B 2 247 ? 45.553  13.014  2.583   1.00 14.34 ? 247 VAL   B CB  1 
ATOM   4323 C  CG1 . VAL   B 2 247 ? 45.252  14.139  1.610   1.00 14.85 ? 247 VAL   B CG1 1 
ATOM   4324 C  CG2 . VAL   B 2 247 ? 46.207  13.543  3.863   1.00 14.15 ? 247 VAL   B CG2 1 
ATOM   4325 N  N   . ASP   B 2 248 ? 43.853  10.852  0.935   1.00 12.99 ? 248 ASP   B N   1 
ATOM   4326 C  CA  . ASP   B 2 248 ? 43.222  10.474  -0.320  1.00 13.89 ? 248 ASP   B CA  1 
ATOM   4327 C  C   . ASP   B 2 248 ? 41.761  10.025  -0.140  1.00 12.69 ? 248 ASP   B C   1 
ATOM   4328 O  O   . ASP   B 2 248 ? 40.934  10.360  -0.971  1.00 12.49 ? 248 ASP   B O   1 
ATOM   4329 C  CB  . ASP   B 2 248 ? 44.084  9.438   -1.048  1.00 16.30 ? 248 ASP   B CB  1 
ATOM   4330 C  CG  . ASP   B 2 248 ? 45.360  10.068  -1.597  1.00 18.93 ? 248 ASP   B CG  1 
ATOM   4331 O  OD1 . ASP   B 2 248 ? 45.380  11.310  -1.702  1.00 22.53 ? 248 ASP   B OD1 1 
ATOM   4332 O  OD2 . ASP   B 2 248 ? 46.332  9.344   -1.880  1.00 21.87 ? 248 ASP   B OD2 1 
ATOM   4333 N  N   . ILE   B 2 249 ? 41.413  9.296   0.929   1.00 12.90 ? 249 ILE   B N   1 
ATOM   4334 C  CA  . ILE   B 2 249 ? 40.034  8.845   1.103   1.00 13.31 ? 249 ILE   B CA  1 
ATOM   4335 C  C   . ILE   B 2 249 ? 39.139  10.001  1.566   1.00 13.52 ? 249 ILE   B C   1 
ATOM   4336 O  O   . ILE   B 2 249 ? 37.927  9.884   1.490   1.00 14.58 ? 249 ILE   B O   1 
ATOM   4337 C  CB  . ILE   B 2 249 ? 39.904  7.623   2.041   1.00 13.87 ? 249 ILE   B CB  1 
ATOM   4338 C  CG1 . ILE   B 2 249 ? 40.340  7.919   3.476   1.00 13.54 ? 249 ILE   B CG1 1 
ATOM   4339 C  CG2 . ILE   B 2 249 ? 40.660  6.421   1.464   1.00 14.84 ? 249 ILE   B CG2 1 
ATOM   4340 C  CD1 . ILE   B 2 249 ? 39.924  6.827   4.464   1.00 14.05 ? 249 ILE   B CD1 1 
ATOM   4341 N  N   . LEU   B 2 250 ? 39.702  11.104  2.070   1.00 13.00 ? 250 LEU   B N   1 
ATOM   4342 C  CA  . LEU   B 2 250 ? 38.896  12.298  2.335   1.00 13.40 ? 250 LEU   B CA  1 
ATOM   4343 C  C   . LEU   B 2 250 ? 38.624  13.128  1.077   1.00 13.38 ? 250 LEU   B C   1 
ATOM   4344 O  O   . LEU   B 2 250 ? 37.856  14.080  1.142   1.00 12.44 ? 250 LEU   B O   1 
ATOM   4345 C  CB  . LEU   B 2 250 ? 39.585  13.163  3.395   1.00 12.18 ? 250 LEU   B CB  1 
ATOM   4346 C  CG  . LEU   B 2 250 ? 39.586  12.578  4.802   1.00 11.09 ? 250 LEU   B CG  1 
ATOM   4347 C  CD1 . LEU   B 2 250 ? 40.569  13.302  5.674   1.00 10.81 ? 250 LEU   B CD1 1 
ATOM   4348 C  CD2 . LEU   B 2 250 ? 38.196  12.636  5.413   1.00 11.87 ? 250 LEU   B CD2 1 
ATOM   4349 N  N   . GLY   B 2 251 ? 39.233  12.754  -0.059  1.00 13.86 ? 251 GLY   B N   1 
ATOM   4350 C  CA  . GLY   B 2 251 ? 39.129  13.488  -1.315  1.00 13.14 ? 251 GLY   B CA  1 
ATOM   4351 C  C   . GLY   B 2 251 ? 37.688  13.758  -1.737  1.00 12.69 ? 251 GLY   B C   1 
ATOM   4352 O  O   . GLY   B 2 251 ? 37.336  14.902  -1.981  1.00 12.67 ? 251 GLY   B O   1 
ATOM   4353 N  N   . PRO   B 2 252 ? 36.832  12.726  -1.870  1.00 12.42 ? 252 PRO   B N   1 
ATOM   4354 C  CA  . PRO   B 2 252 ? 35.431  12.920  -2.253  1.00 12.37 ? 252 PRO   B CA  1 
ATOM   4355 C  C   . PRO   B 2 252 ? 34.656  13.888  -1.349  1.00 11.85 ? 252 PRO   B C   1 
ATOM   4356 O  O   . PRO   B 2 252 ? 33.933  14.719  -1.877  1.00 11.72 ? 252 PRO   B O   1 
ATOM   4357 C  CB  . PRO   B 2 252 ? 34.849  11.494  -2.253  1.00 12.89 ? 252 PRO   B CB  1 
ATOM   4358 C  CG  . PRO   B 2 252 ? 36.051  10.610  -2.518  1.00 13.28 ? 252 PRO   B CG  1 
ATOM   4359 C  CD  . PRO   B 2 252 ? 37.195  11.300  -1.795  1.00 13.51 ? 252 PRO   B CD  1 
ATOM   4360 N  N   . LEU   B 2 253 ? 34.846  13.833  -0.015  1.00 11.30 ? 253 LEU   B N   1 
ATOM   4361 C  CA  . LEU   B 2 253 ? 34.165  14.757  0.891   1.00 11.38 ? 253 LEU   B CA  1 
ATOM   4362 C  C   . LEU   B 2 253 ? 34.712  16.169  0.707   1.00 11.45 ? 253 LEU   B C   1 
ATOM   4363 O  O   . LEU   B 2 253 ? 33.963  17.143  0.801   1.00 11.28 ? 253 LEU   B O   1 
ATOM   4364 C  CB  . LEU   B 2 253 ? 34.300  14.289  2.346   1.00 11.04 ? 253 LEU   B CB  1 
ATOM   4365 C  CG  . LEU   B 2 253 ? 33.478  13.051  2.676   1.00 11.13 ? 253 LEU   B CG  1 
ATOM   4366 C  CD1 . LEU   B 2 253 ? 33.821  12.495  4.047   1.00 11.03 ? 253 LEU   B CD1 1 
ATOM   4367 C  CD2 . LEU   B 2 253 ? 32.000  13.326  2.579   1.00 10.99 ? 253 LEU   B CD2 1 
ATOM   4368 N  N   . SER   B 2 254 ? 36.023  16.276  0.465   1.00 10.99 ? 254 SER   B N   1 
ATOM   4369 C  CA  . SER   B 2 254 ? 36.637  17.565  0.230   1.00 11.15 ? 254 SER   B CA  1 
ATOM   4370 C  C   . SER   B 2 254 ? 36.032  18.226  -1.013  1.00 11.42 ? 254 SER   B C   1 
ATOM   4371 O  O   . SER   B 2 254 ? 35.672  19.395  -1.021  1.00 10.70 ? 254 SER   B O   1 
ATOM   4372 C  CB  . SER   B 2 254 ? 38.137  17.428  0.098   1.00 10.94 ? 254 SER   B CB  1 
ATOM   4373 O  OG  . SER   B 2 254 ? 38.727  18.720  -0.031  1.00 11.29 ? 254 SER   B OG  1 
ATOM   4374 N  N   . ALA   B 2 255 ? 35.925  17.448  -2.083  1.00 12.32 ? 255 ALA   B N   1 
ATOM   4375 C  CA  . ALA   B 2 255 ? 35.390  17.921  -3.353  1.00 12.27 ? 255 ALA   B CA  1 
ATOM   4376 C  C   . ALA   B 2 255 ? 33.912  18.310  -3.207  1.00 11.74 ? 255 ALA   B C   1 
ATOM   4377 O  O   . ALA   B 2 255 ? 33.494  19.345  -3.710  1.00 11.70 ? 255 ALA   B O   1 
ATOM   4378 C  CB  . ALA   B 2 255 ? 35.593  16.839  -4.398  1.00 12.47 ? 255 ALA   B CB  1 
ATOM   4379 N  N   . GLN   B 2 256 ? 33.128  17.480  -2.515  1.00 12.01 ? 256 GLN   B N   1 
ATOM   4380 C  CA  . GLN   B 2 256 ? 31.697  17.708  -2.343  1.00 12.09 ? 256 GLN   B CA  1 
ATOM   4381 C  C   . GLN   B 2 256 ? 31.431  19.004  -1.579  1.00 11.64 ? 256 GLN   B C   1 
ATOM   4382 O  O   . GLN   B 2 256 ? 30.473  19.709  -1.870  1.00 12.67 ? 256 GLN   B O   1 
ATOM   4383 C  CB  . GLN   B 2 256 ? 31.078  16.527  -1.592  1.00 12.21 ? 256 GLN   B CB  1 
ATOM   4384 C  CG  . GLN   B 2 256 ? 29.564  16.619  -1.403  1.00 12.55 ? 256 GLN   B CG  1 
ATOM   4385 C  CD  . GLN   B 2 256 ? 29.013  15.412  -0.680  1.00 12.92 ? 256 GLN   B CD  1 
ATOM   4386 O  OE1 . GLN   B 2 256 ? 29.727  14.446  -0.456  1.00 13.70 ? 256 GLN   B OE1 1 
ATOM   4387 N  NE2 . GLN   B 2 256 ? 27.751  15.451  -0.252  1.00 13.40 ? 256 GLN   B NE2 1 
ATOM   4388 N  N   . THR   B 2 257 ? 32.241  19.310  -0.569  1.00 11.40 ? 257 THR   B N   1 
ATOM   4389 C  CA  . THR   B 2 257 ? 32.009  20.482  0.259   1.00 11.17 ? 257 THR   B CA  1 
ATOM   4390 C  C   . THR   B 2 257 ? 32.817  21.696  -0.200  1.00 12.28 ? 257 THR   B C   1 
ATOM   4391 O  O   . THR   B 2 257 ? 32.520  22.820  0.213   1.00 13.53 ? 257 THR   B O   1 
ATOM   4392 C  CB  . THR   B 2 257 ? 32.364  20.197  1.720   1.00 11.07 ? 257 THR   B CB  1 
ATOM   4393 O  OG1 . THR   B 2 257 ? 33.753  19.858  1.775   1.00 10.55 ? 257 THR   B OG1 1 
ATOM   4394 C  CG2 . THR   B 2 257 ? 31.507  19.101  2.307   1.00 11.80 ? 257 THR   B CG2 1 
ATOM   4395 N  N   . GLY   B 2 258 ? 33.849  21.484  -1.022  1.00 12.98 ? 258 GLY   B N   1 
ATOM   4396 C  CA  . GLY   B 2 258 ? 34.758  22.561  -1.404  1.00 13.27 ? 258 GLY   B CA  1 
ATOM   4397 C  C   . GLY   B 2 258 ? 35.725  22.958  -0.279  1.00 14.76 ? 258 GLY   B C   1 
ATOM   4398 O  O   . GLY   B 2 258 ? 36.293  24.059  -0.314  1.00 13.92 ? 258 GLY   B O   1 
ATOM   4399 N  N   . ILE   B 2 259 ? 35.835  22.115  0.776   1.00 14.45 ? 259 ILE   B N   1 
ATOM   4400 C  CA  . ILE   B 2 259 ? 36.722  22.405  1.895   1.00 14.33 ? 259 ILE   B CA  1 
ATOM   4401 C  C   . ILE   B 2 259 ? 37.947  21.503  1.768   1.00 14.31 ? 259 ILE   B C   1 
ATOM   4402 O  O   . ILE   B 2 259 ? 37.841  20.278  1.926   1.00 14.50 ? 259 ILE   B O   1 
ATOM   4403 C  CB  . ILE   B 2 259 ? 36.047  22.242  3.282   1.00 15.58 ? 259 ILE   B CB  1 
ATOM   4404 C  CG1 . ILE   B 2 259 ? 34.696  22.953  3.429   1.00 15.40 ? 259 ILE   B CG1 1 
ATOM   4405 C  CG2 . ILE   B 2 259 ? 37.011  22.668  4.373   1.00 15.69 ? 259 ILE   B CG2 1 
ATOM   4406 C  CD1 . ILE   B 2 259 ? 34.743  24.391  3.085   1.00 17.15 ? 259 ILE   B CD1 1 
ATOM   4407 N  N   . ALA   B 2 260 ? 39.106  22.132  1.527   1.00 12.76 ? 260 ALA   B N   1 
ATOM   4408 C  CA  . ALA   B 2 260 ? 40.367  21.438  1.401   1.00 13.38 ? 260 ALA   B CA  1 
ATOM   4409 C  C   . ALA   B 2 260 ? 40.649  20.638  2.672   1.00 12.00 ? 260 ALA   B C   1 
ATOM   4410 O  O   . ALA   B 2 260 ? 40.350  21.092  3.766   1.00 10.60 ? 260 ALA   B O   1 
ATOM   4411 C  CB  . ALA   B 2 260 ? 41.478  22.421  1.088   1.00 14.22 ? 260 ALA   B CB  1 
ATOM   4412 N  N   . VAL   B 2 261 ? 41.231  19.435  2.503   1.00 12.09 ? 261 VAL   B N   1 
ATOM   4413 C  CA  . VAL   B 2 261 ? 41.520  18.559  3.633   1.00 11.76 ? 261 VAL   B CA  1 
ATOM   4414 C  C   . VAL   B 2 261 ? 42.336  19.278  4.700   1.00 12.80 ? 261 VAL   B C   1 
ATOM   4415 O  O   . VAL   B 2 261 ? 42.020  19.182  5.888   1.00 13.54 ? 261 VAL   B O   1 
ATOM   4416 C  CB  . VAL   B 2 261 ? 42.227  17.280  3.173   1.00 11.89 ? 261 VAL   B CB  1 
ATOM   4417 C  CG1 . VAL   B 2 261 ? 42.716  16.483  4.372   1.00 11.94 ? 261 VAL   B CG1 1 
ATOM   4418 C  CG2 . VAL   B 2 261 ? 41.338  16.448  2.268   1.00 12.45 ? 261 VAL   B CG2 1 
ATOM   4419 N  N   . LEU   B 2 262 ? 43.377  20.024  4.300   1.00 13.85 ? 262 LEU   B N   1 
ATOM   4420 C  CA  . LEU   B 2 262 ? 44.265  20.673  5.274   1.00 14.83 ? 262 LEU   B CA  1 
ATOM   4421 C  C   . LEU   B 2 262 ? 43.560  21.847  5.970   1.00 15.17 ? 262 LEU   B C   1 
ATOM   4422 O  O   . LEU   B 2 262 ? 43.886  22.168  7.106   1.00 13.65 ? 262 LEU   B O   1 
ATOM   4423 C  CB  . LEU   B 2 262 ? 45.555  21.129  4.585   1.00 15.91 ? 262 LEU   B CB  1 
ATOM   4424 C  CG  . LEU   B 2 262 ? 46.469  20.016  4.072   1.00 17.39 ? 262 LEU   B CG  1 
ATOM   4425 C  CD1 . LEU   B 2 262 ? 47.685  20.585  3.344   1.00 18.57 ? 262 LEU   B CD1 1 
ATOM   4426 C  CD2 . LEU   B 2 262 ? 46.932  19.140  5.228   1.00 20.06 ? 262 LEU   B CD2 1 
ATOM   4427 N  N   . ASP   B 2 263 ? 42.547  22.453  5.319   1.00 14.42 ? 263 ASP   B N   1 
ATOM   4428 C  CA  . ASP   B 2 263 ? 41.737  23.480  5.969   1.00 14.24 ? 263 ASP   B CA  1 
ATOM   4429 C  C   . ASP   B 2 263 ? 40.872  22.845  7.060   1.00 14.18 ? 263 ASP   B C   1 
ATOM   4430 O  O   . ASP   B 2 263 ? 40.748  23.380  8.172   1.00 13.62 ? 263 ASP   B O   1 
ATOM   4431 C  CB  . ASP   B 2 263 ? 40.888  24.247  4.945   1.00 15.53 ? 263 ASP   B CB  1 
ATOM   4432 C  CG  . ASP   B 2 263 ? 41.696  25.054  3.921   1.00 17.40 ? 263 ASP   B CG  1 
ATOM   4433 O  OD1 . ASP   B 2 263 ? 42.948  25.108  4.036   1.00 16.54 ? 263 ASP   B OD1 1 
ATOM   4434 O  OD2 . ASP   B 2 263 ? 41.075  25.663  3.029   1.00 18.24 ? 263 ASP   B OD2 1 
ATOM   4435 N  N   . MET   B 2 264 ? 40.319  21.656  6.768   1.00 13.19 ? 264 MET   B N   1 
ATOM   4436 C  CA  . MET   B 2 264 ? 39.550  20.939  7.765   1.00 13.08 ? 264 MET   B CA  1 
ATOM   4437 C  C   . MET   B 2 264 ? 40.460  20.521  8.917   1.00 12.45 ? 264 MET   B C   1 
ATOM   4438 O  O   . MET   B 2 264 ? 40.050  20.575  10.061  1.00 13.83 ? 264 MET   B O   1 
ATOM   4439 C  CB  . MET   B 2 264 ? 38.843  19.706  7.174   1.00 12.77 ? 264 MET   B CB  1 
ATOM   4440 C  CG  . MET   B 2 264 ? 37.801  19.148  8.104   1.00 12.82 ? 264 MET   B CG  1 
ATOM   4441 S  SD  . MET   B 2 264 ? 36.467  20.364  8.449   1.00 14.24 ? 264 MET   B SD  1 
ATOM   4442 C  CE  . MET   B 2 264 ? 35.417  20.015  7.047   1.00 13.94 ? 264 MET   B CE  1 
ATOM   4443 N  N   . CYS   B 2 265 ? 41.682  20.077  8.619   1.00 12.68 ? 265 CYS   B N   1 
ATOM   4444 C  CA  . CYS   B 2 265 ? 42.655  19.741  9.642   1.00 12.73 ? 265 CYS   B CA  1 
ATOM   4445 C  C   . CYS   B 2 265 ? 42.903  20.936  10.565  1.00 13.12 ? 265 CYS   B C   1 
ATOM   4446 O  O   . CYS   B 2 265 ? 42.915  20.802  11.779  1.00 11.62 ? 265 CYS   B O   1 
ATOM   4447 C  CB  . CYS   B 2 265 ? 43.966  19.306  9.011   1.00 13.03 ? 265 CYS   B CB  1 
ATOM   4448 S  SG  . CYS   B 2 265 ? 43.889  17.674  8.241   1.00 12.71 ? 265 CYS   B SG  1 
ATOM   4449 N  N   . ALA   B 2 266 ? 43.112  22.121  9.983   1.00 14.15 ? 266 ALA   B N   1 
ATOM   4450 C  CA  . ALA   B 2 266 ? 43.295  23.328  10.780  1.00 13.62 ? 266 ALA   B CA  1 
ATOM   4451 C  C   . ALA   B 2 266 ? 42.067  23.596  11.649  1.00 13.83 ? 266 ALA   B C   1 
ATOM   4452 O  O   . ALA   B 2 266 ? 42.210  24.058  12.790  1.00 15.18 ? 266 ALA   B O   1 
ATOM   4453 C  CB  . ALA   B 2 266 ? 43.637  24.495  9.890   1.00 13.38 ? 266 ALA   B CB  1 
ATOM   4454 N  N   . SER   B 2 267 ? 40.866  23.265  11.160  1.00 14.48 ? 267 SER   B N   1 
ATOM   4455 C  CA  . SER   B 2 267 ? 39.649  23.462  11.939  1.00 14.66 ? 267 SER   B CA  1 
ATOM   4456 C  C   . SER   B 2 267 ? 39.621  22.520  13.138  1.00 14.28 ? 267 SER   B C   1 
ATOM   4457 O  O   . SER   B 2 267 ? 39.243  22.900  14.249  1.00 13.97 ? 267 SER   B O   1 
ATOM   4458 C  CB  . SER   B 2 267 ? 38.391  23.319  11.085  1.00 16.68 ? 267 SER   B CB  1 
ATOM   4459 O  OG  . SER   B 2 267 ? 38.278  24.412  10.158  1.00 19.81 ? 267 SER   B OG  1 
ATOM   4460 N  N   . LEU   B 2 268 ? 39.983  21.259  12.903  1.00 14.63 ? 268 LEU   B N   1 
ATOM   4461 C  CA  . LEU   B 2 268 ? 40.027  20.279  13.967  1.00 14.81 ? 268 LEU   B CA  1 
ATOM   4462 C  C   . LEU   B 2 268 ? 41.122  20.668  14.969  1.00 16.43 ? 268 LEU   B C   1 
ATOM   4463 O  O   . LEU   B 2 268 ? 40.939  20.538  16.174  1.00 17.95 ? 268 LEU   B O   1 
ATOM   4464 C  CB  . LEU   B 2 268 ? 40.299  18.900  13.350  1.00 13.80 ? 268 LEU   B CB  1 
ATOM   4465 C  CG  . LEU   B 2 268 ? 40.531  17.774  14.348  1.00 13.66 ? 268 LEU   B CG  1 
ATOM   4466 C  CD1 . LEU   B 2 268 ? 39.363  17.657  15.318  1.00 13.75 ? 268 LEU   B CD1 1 
ATOM   4467 C  CD2 . LEU   B 2 268 ? 40.776  16.467  13.591  1.00 13.20 ? 268 LEU   B CD2 1 
ATOM   4468 N  N   . LYS   B 2 269 ? 42.258  21.147  14.473  1.00 18.31 ? 269 LYS   B N   1 
ATOM   4469 C  CA  . LYS   B 2 269 ? 43.343  21.566  15.340  1.00 19.80 ? 269 LYS   B CA  1 
ATOM   4470 C  C   . LYS   B 2 269 ? 42.863  22.618  16.346  1.00 22.27 ? 269 LYS   B C   1 
ATOM   4471 O  O   . LYS   B 2 269 ? 43.164  22.521  17.545  1.00 21.11 ? 269 LYS   B O   1 
ATOM   4472 C  CB  . LYS   B 2 269 ? 44.505  22.081  14.503  1.00 23.26 ? 269 LYS   B CB  1 
ATOM   4473 C  CG  . LYS   B 2 269 ? 45.773  22.263  15.310  1.00 27.39 ? 269 LYS   B CG  1 
ATOM   4474 C  CD  . LYS   B 2 269 ? 46.934  22.719  14.504  1.00 31.08 ? 269 LYS   B CD  1 
ATOM   4475 C  CE  . LYS   B 2 269 ? 46.882  24.208  14.259  1.00 34.49 ? 269 LYS   B CE  1 
ATOM   4476 N  NZ  . LYS   B 2 269 ? 48.214  24.744  13.924  1.00 38.99 ? 269 LYS   B NZ  1 
ATOM   4477 N  N   . GLU   B 2 270 ? 42.079  23.603  15.877  1.00 22.77 ? 270 GLU   B N   1 
ATOM   4478 C  CA  . GLU   B 2 270 ? 41.537  24.618  16.767  1.00 22.75 ? 270 GLU   B CA  1 
ATOM   4479 C  C   . GLU   B 2 270 ? 40.576  24.003  17.778  1.00 23.30 ? 270 GLU   B C   1 
ATOM   4480 O  O   . GLU   B 2 270 ? 40.557  24.441  18.927  1.00 24.69 ? 270 GLU   B O   1 
ATOM   4481 C  CB  . GLU   B 2 270 ? 40.856  25.746  15.985  1.00 25.26 ? 270 GLU   B CB  1 
ATOM   4482 C  CG  . GLU   B 2 270 ? 41.829  26.634  15.246  1.00 29.39 ? 270 GLU   B CG  1 
ATOM   4483 C  CD  . GLU   B 2 270 ? 42.898  27.283  16.118  1.00 38.36 ? 270 GLU   B CD  1 
ATOM   4484 O  OE1 . GLU   B 2 270 ? 42.524  27.939  17.120  1.00 45.50 ? 270 GLU   B OE1 1 
ATOM   4485 O  OE2 . GLU   B 2 270 ? 44.108  27.111  15.824  1.00 43.30 ? 270 GLU   B OE2 1 
ATOM   4486 N  N   . LEU   B 2 271 ? 39.743  23.031  17.359  1.00 21.75 ? 271 LEU   B N   1 
ATOM   4487 C  CA  . LEU   B 2 271 ? 38.849  22.352  18.284  1.00 21.76 ? 271 LEU   B CA  1 
ATOM   4488 C  C   . LEU   B 2 271 ? 39.652  21.628  19.369  1.00 23.28 ? 271 LEU   B C   1 
ATOM   4489 O  O   . LEU   B 2 271 ? 39.258  21.603  20.534  1.00 24.73 ? 271 LEU   B O   1 
ATOM   4490 C  CB  . LEU   B 2 271 ? 37.960  21.354  17.533  1.00 23.67 ? 271 LEU   B CB  1 
ATOM   4491 C  CG  . LEU   B 2 271 ? 36.894  21.928  16.606  1.00 25.54 ? 271 LEU   B CG  1 
ATOM   4492 C  CD1 . LEU   B 2 271 ? 36.108  20.811  15.947  1.00 23.58 ? 271 LEU   B CD1 1 
ATOM   4493 C  CD2 . LEU   B 2 271 ? 35.940  22.865  17.348  1.00 25.20 ? 271 LEU   B CD2 1 
ATOM   4494 N  N   . LEU   B 2 272 ? 40.787  21.021  18.995  1.00 24.51 ? 272 LEU   B N   1 
ATOM   4495 C  CA  . LEU   B 2 272 ? 41.601  20.289  19.958  1.00 27.06 ? 272 LEU   B CA  1 
ATOM   4496 C  C   . LEU   B 2 272 ? 42.219  21.248  20.973  1.00 26.96 ? 272 LEU   B C   1 
ATOM   4497 O  O   . LEU   B 2 272 ? 42.245  20.947  22.168  1.00 26.42 ? 272 LEU   B O   1 
ATOM   4498 C  CB  . LEU   B 2 272 ? 42.698  19.496  19.236  1.00 26.65 ? 272 LEU   B CB  1 
ATOM   4499 C  CG  . LEU   B 2 272 ? 42.208  18.320  18.390  1.00 26.34 ? 272 LEU   B CG  1 
ATOM   4500 C  CD1 . LEU   B 2 272 ? 43.384  17.544  17.844  1.00 27.53 ? 272 LEU   B CD1 1 
ATOM   4501 C  CD2 . LEU   B 2 272 ? 41.290  17.403  19.167  1.00 26.93 ? 272 LEU   B CD2 1 
ATOM   4502 N  N   . GLN   B 2 273 ? 42.719  22.381  20.473  1.00 27.27 ? 273 GLN   B N   1 
ATOM   4503 C  CA  . GLN   B 2 273 ? 43.462  23.325  21.287  1.00 29.50 ? 273 GLN   B CA  1 
ATOM   4504 C  C   . GLN   B 2 273 ? 42.535  24.154  22.166  1.00 31.02 ? 273 GLN   B C   1 
ATOM   4505 O  O   . GLN   B 2 273 ? 42.957  24.546  23.243  1.00 28.78 ? 273 GLN   B O   1 
ATOM   4506 C  CB  . GLN   B 2 273 ? 44.278  24.260  20.408  1.00 28.00 ? 273 GLN   B CB  1 
ATOM   4507 C  CG  . GLN   B 2 273 ? 45.468  23.549  19.813  1.00 28.57 ? 273 GLN   B CG  1 
ATOM   4508 C  CD  . GLN   B 2 273 ? 46.209  24.393  18.821  1.00 27.11 ? 273 GLN   B CD  1 
ATOM   4509 O  OE1 . GLN   B 2 273 ? 45.695  25.371  18.301  1.00 28.90 ? 273 GLN   B OE1 1 
ATOM   4510 N  NE2 . GLN   B 2 273 ? 47.412  23.962  18.499  1.00 30.74 ? 273 GLN   B NE2 1 
ATOM   4511 N  N   . ASN   B 2 274 ? 41.303  24.412  21.707  1.00 31.74 ? 274 ASN   B N   1 
ATOM   4512 C  CA  . ASN   B 2 274 ? 40.451  25.417  22.338  1.00 31.55 ? 274 ASN   B CA  1 
ATOM   4513 C  C   . ASN   B 2 274 ? 39.214  24.785  22.947  1.00 30.70 ? 274 ASN   B C   1 
ATOM   4514 O  O   . ASN   B 2 274 ? 38.463  25.459  23.634  1.00 35.14 ? 274 ASN   B O   1 
ATOM   4515 C  CB  . ASN   B 2 274 ? 40.003  26.503  21.349  1.00 29.55 ? 274 ASN   B CB  1 
ATOM   4516 C  CG  . ASN   B 2 274 ? 41.149  27.401  20.961  1.00 31.53 ? 274 ASN   B CG  1 
ATOM   4517 O  OD1 . ASN   B 2 274 ? 41.694  28.079  21.822  1.00 37.73 ? 274 ASN   B OD1 1 
ATOM   4518 N  ND2 . ASN   B 2 274 ? 41.541  27.406  19.699  1.00 36.35 ? 274 ASN   B ND2 1 
ATOM   4519 N  N   . GLY   B 2 275 ? 38.959  23.522  22.641  1.00 29.15 ? 275 GLY   B N   1 
ATOM   4520 C  CA  . GLY   B 2 275 ? 37.742  22.887  23.103  1.00 29.48 ? 275 GLY   B CA  1 
ATOM   4521 C  C   . GLY   B 2 275 ? 36.532  23.368  22.311  1.00 32.13 ? 275 GLY   B C   1 
ATOM   4522 O  O   . GLY   B 2 275 ? 36.659  24.213  21.423  1.00 32.51 ? 275 GLY   B O   1 
ATOM   4523 N  N   . MET   B 2 276 ? 35.376  22.806  22.665  1.00 32.84 ? 276 MET   B N   1 
ATOM   4524 C  CA  . MET   B 2 276 ? 34.120  23.026  21.979  1.00 39.30 ? 276 MET   B CA  1 
ATOM   4525 C  C   . MET   B 2 276 ? 33.430  24.291  22.506  1.00 44.21 ? 276 MET   B C   1 
ATOM   4526 O  O   . MET   B 2 276 ? 32.487  24.803  21.890  1.00 40.42 ? 276 MET   B O   1 
ATOM   4527 C  CB  . MET   B 2 276 ? 33.214  21.814  22.216  1.00 41.44 ? 276 MET   B CB  1 
ATOM   4528 C  CG  . MET   B 2 276 ? 33.785  20.515  21.667  1.00 45.10 ? 276 MET   B CG  1 
ATOM   4529 S  SD  . MET   B 2 276 ? 33.602  20.373  19.863  1.00 43.78 ? 276 MET   B SD  1 
ATOM   4530 C  CE  . MET   B 2 276 ? 31.853  20.033  19.712  1.00 36.35 ? 276 MET   B CE  1 
ATOM   4531 N  N   . ASN   B 2 277 ? 33.875  24.766  23.675  1.00 50.15 ? 277 ASN   B N   1 
ATOM   4532 C  CA  . ASN   B 2 277 ? 33.432  26.042  24.221  1.00 54.58 ? 277 ASN   B CA  1 
ATOM   4533 C  C   . ASN   B 2 277 ? 31.901  26.091  24.243  1.00 50.69 ? 277 ASN   B C   1 
ATOM   4534 O  O   . ASN   B 2 277 ? 31.305  27.116  23.913  1.00 50.29 ? 277 ASN   B O   1 
ATOM   4535 C  CB  . ASN   B 2 277 ? 34.083  27.198  23.448  1.00 64.14 ? 277 ASN   B CB  1 
ATOM   4536 C  CG  . ASN   B 2 277 ? 33.881  28.570  24.064  1.00 76.78 ? 277 ASN   B CG  1 
ATOM   4537 O  OD1 . ASN   B 2 277 ? 34.275  28.803  25.209  1.00 79.70 ? 277 ASN   B OD1 1 
ATOM   4538 N  ND2 . ASN   B 2 277 ? 33.303  29.489  23.300  1.00 77.21 ? 277 ASN   B ND2 1 
ATOM   4539 N  N   . GLY   B 2 278 ? 31.267  24.972  24.634  1.00 45.45 ? 278 GLY   B N   1 
ATOM   4540 C  CA  . GLY   B 2 278 ? 29.827  24.929  24.848  1.00 40.67 ? 278 GLY   B CA  1 
ATOM   4541 C  C   . GLY   B 2 278 ? 29.037  24.534  23.606  1.00 41.16 ? 278 GLY   B C   1 
ATOM   4542 O  O   . GLY   B 2 278 ? 27.835  24.306  23.714  1.00 39.36 ? 278 GLY   B O   1 
ATOM   4543 N  N   . GLY   B 2 279 ? 29.702  24.482  22.437  1.00 41.49 ? 279 GLY   B N   1 
ATOM   4544 C  CA  . GLY   B 2 279 ? 29.013  24.252  21.170  1.00 36.88 ? 279 GLY   B CA  1 
ATOM   4545 C  C   . GLY   B 2 279 ? 28.878  22.759  20.899  1.00 30.97 ? 279 GLY   B C   1 
ATOM   4546 O  O   . GLY   B 2 279 ? 29.559  21.958  21.535  1.00 33.23 ? 279 GLY   B O   1 
ATOM   4547 N  N   . THR   B 2 280 ? 27.998  22.404  19.962  1.00 25.91 ? 280 THR   B N   1 
ATOM   4548 C  CA  . THR   B 2 280 ? 27.810  21.023  19.551  1.00 27.75 ? 280 THR   B CA  1 
ATOM   4549 C  C   . THR   B 2 280 ? 27.956  20.902  18.032  1.00 25.47 ? 280 THR   B C   1 
ATOM   4550 O  O   . THR   B 2 280 ? 27.811  21.876  17.289  1.00 25.54 ? 280 THR   B O   1 
ATOM   4551 C  CB  . THR   B 2 280 ? 26.447  20.481  19.999  1.00 27.09 ? 280 THR   B CB  1 
ATOM   4552 O  OG1 . THR   B 2 280 ? 25.399  21.109  19.261  1.00 25.60 ? 280 THR   B OG1 1 
ATOM   4553 C  CG2 . THR   B 2 280 ? 26.196  20.669  21.482  1.00 27.30 ? 280 THR   B CG2 1 
ATOM   4554 N  N   . ILE   B 2 281 ? 28.242  19.681  17.579  1.00 23.78 ? 281 ILE   B N   1 
ATOM   4555 C  CA  . ILE   B 2 281 ? 28.359  19.381  16.163  1.00 21.71 ? 281 ILE   B CA  1 
ATOM   4556 C  C   . ILE   B 2 281 ? 27.468  18.186  15.904  1.00 20.94 ? 281 ILE   B C   1 
ATOM   4557 O  O   . ILE   B 2 281 ? 27.582  17.176  16.586  1.00 20.85 ? 281 ILE   B O   1 
ATOM   4558 C  CB  . ILE   B 2 281 ? 29.830  19.123  15.753  1.00 21.88 ? 281 ILE   B CB  1 
ATOM   4559 C  CG1 . ILE   B 2 281 ? 30.679  20.373  15.990  1.00 21.62 ? 281 ILE   B CG1 1 
ATOM   4560 C  CG2 . ILE   B 2 281 ? 29.933  18.631  14.310  1.00 21.28 ? 281 ILE   B CG2 1 
ATOM   4561 C  CD1 . ILE   B 2 281 ? 32.169  20.133  15.904  1.00 23.19 ? 281 ILE   B CD1 1 
ATOM   4562 N  N   . LEU   B 2 282 ? 26.583  18.325  14.917  1.00 19.86 ? 282 LEU   B N   1 
ATOM   4563 C  CA  . LEU   B 2 282 ? 25.566  17.320  14.651  1.00 20.14 ? 282 LEU   B CA  1 
ATOM   4564 C  C   . LEU   B 2 282 ? 24.864  16.929  15.937  1.00 20.55 ? 282 LEU   B C   1 
ATOM   4565 O  O   . LEU   B 2 282 ? 24.567  15.764  16.124  1.00 21.07 ? 282 LEU   B O   1 
ATOM   4566 C  CB  . LEU   B 2 282 ? 26.200  16.123  13.953  1.00 20.36 ? 282 LEU   B CB  1 
ATOM   4567 C  CG  . LEU   B 2 282 ? 26.547  16.400  12.499  1.00 20.84 ? 282 LEU   B CG  1 
ATOM   4568 C  CD1 . LEU   B 2 282 ? 27.493  15.353  11.949  1.00 20.74 ? 282 LEU   B CD1 1 
ATOM   4569 C  CD2 . LEU   B 2 282 ? 25.276  16.469  11.666  1.00 22.48 ? 282 LEU   B CD2 1 
ATOM   4570 N  N   . GLY   B 2 283 ? 24.595  17.928  16.791  1.00 22.61 ? 283 GLY   B N   1 
ATOM   4571 C  CA  . GLY   B 2 283 ? 23.806  17.705  17.994  1.00 25.28 ? 283 GLY   B CA  1 
ATOM   4572 C  C   . GLY   B 2 283 ? 24.616  17.164  19.165  1.00 27.40 ? 283 GLY   B C   1 
ATOM   4573 O  O   . GLY   B 2 283 ? 24.060  16.992  20.235  1.00 28.31 ? 283 GLY   B O   1 
ATOM   4574 N  N   . SER   B 2 284 ? 25.921  16.918  18.983  1.00 29.37 ? 284 SER   B N   1 
ATOM   4575 C  CA  . SER   B 2 284 ? 26.719  16.261  20.013  1.00 28.92 ? 284 SER   B CA  1 
ATOM   4576 C  C   . SER   B 2 284 ? 27.913  17.108  20.440  1.00 26.69 ? 284 SER   B C   1 
ATOM   4577 O  O   . SER   B 2 284 ? 28.532  17.811  19.628  1.00 25.54 ? 284 SER   B O   1 
ATOM   4578 C  CB  . SER   B 2 284 ? 27.201  14.908  19.567  1.00 29.43 ? 284 SER   B CB  1 
ATOM   4579 O  OG  . SER   B 2 284 ? 27.834  14.288  20.671  1.00 33.28 ? 284 SER   B OG  1 
ATOM   4580 N  N   . ALA   B 2 285 ? 28.259  16.993  21.730  1.00 27.67 ? 285 ALA   B N   1 
ATOM   4581 C  CA  . ALA   B 2 285 ? 29.463  17.614  22.275  1.00 25.88 ? 285 ALA   B CA  1 
ATOM   4582 C  C   . ALA   B 2 285 ? 30.679  16.728  22.030  1.00 22.01 ? 285 ALA   B C   1 
ATOM   4583 O  O   . ALA   B 2 285 ? 31.794  17.207  22.152  1.00 24.17 ? 285 ALA   B O   1 
ATOM   4584 C  CB  . ALA   B 2 285 ? 29.301  17.901  23.760  1.00 28.28 ? 285 ALA   B CB  1 
ATOM   4585 N  N   . LEU   B 2 286 ? 30.472  15.455  21.687  1.00 22.24 ? 286 LEU   B N   1 
ATOM   4586 C  CA  . LEU   B 2 286 ? 31.564  14.536  21.389  1.00 25.31 ? 286 LEU   B CA  1 
ATOM   4587 C  C   . LEU   B 2 286 ? 31.829  14.433  19.887  1.00 22.50 ? 286 LEU   B C   1 
ATOM   4588 O  O   . LEU   B 2 286 ? 30.897  14.333  19.110  1.00 27.60 ? 286 LEU   B O   1 
ATOM   4589 C  CB  . LEU   B 2 286 ? 31.194  13.140  21.900  1.00 27.69 ? 286 LEU   B CB  1 
ATOM   4590 C  CG  . LEU   B 2 286 ? 30.746  13.032  23.350  1.00 31.89 ? 286 LEU   B CG  1 
ATOM   4591 C  CD1 . LEU   B 2 286 ? 30.569  11.559  23.723  1.00 35.42 ? 286 LEU   B CD1 1 
ATOM   4592 C  CD2 . LEU   B 2 286 ? 31.730  13.727  24.280  1.00 31.17 ? 286 LEU   B CD2 1 
ATOM   4593 N  N   . LEU   B 2 287 ? 33.099  14.386  19.487  1.00 21.94 ? 287 LEU   B N   1 
ATOM   4594 C  CA  . LEU   B 2 287 ? 33.466  14.113  18.099  1.00 21.21 ? 287 LEU   B CA  1 
ATOM   4595 C  C   . LEU   B 2 287 ? 33.509  12.599  17.857  1.00 21.91 ? 287 LEU   B C   1 
ATOM   4596 O  O   . LEU   B 2 287 ? 34.316  11.886  18.446  1.00 24.97 ? 287 LEU   B O   1 
ATOM   4597 C  CB  . LEU   B 2 287 ? 34.831  14.729  17.808  1.00 21.04 ? 287 LEU   B CB  1 
ATOM   4598 C  CG  . LEU   B 2 287 ? 34.927  16.249  17.993  1.00 21.16 ? 287 LEU   B CG  1 
ATOM   4599 C  CD1 . LEU   B 2 287 ? 36.338  16.756  17.717  1.00 19.79 ? 287 LEU   B CD1 1 
ATOM   4600 C  CD2 . LEU   B 2 287 ? 33.907  16.974  17.128  1.00 22.47 ? 287 LEU   B CD2 1 
ATOM   4601 N  N   . GLU   B 2 288 ? 32.665  12.122  16.939  1.00 18.63 ? 288 GLU   B N   1 
ATOM   4602 C  CA  . GLU   B 2 288 ? 32.552  10.717  16.585  1.00 16.58 ? 288 GLU   B CA  1 
ATOM   4603 C  C   . GLU   B 2 288 ? 33.743  10.275  15.728  1.00 14.98 ? 288 GLU   B C   1 
ATOM   4604 O  O   . GLU   B 2 288 ? 34.138  10.991  14.804  1.00 12.96 ? 288 GLU   B O   1 
ATOM   4605 C  CB  . GLU   B 2 288 ? 31.223  10.580  15.846  1.00 19.05 ? 288 GLU   B CB  1 
ATOM   4606 C  CG  . GLU   B 2 288 ? 30.935  9.212   15.285  1.00 22.01 ? 288 GLU   B CG  1 
ATOM   4607 C  CD  . GLU   B 2 288 ? 30.785  8.104   16.325  1.00 24.76 ? 288 GLU   B CD  1 
ATOM   4608 O  OE1 . GLU   B 2 288 ? 29.972  8.303   17.274  1.00 20.40 ? 288 GLU   B OE1 1 
ATOM   4609 O  OE2 . GLU   B 2 288 ? 31.489  7.053   16.165  1.00 21.30 ? 288 GLU   B OE2 1 
ATOM   4610 N  N   . ASP   B 2 289 ? 34.311  9.087   16.036  1.00 12.85 ? 289 ASP   B N   1 
ATOM   4611 C  CA  . ASP   B 2 289 ? 35.459  8.595   15.296  1.00 12.92 ? 289 ASP   B CA  1 
ATOM   4612 C  C   . ASP   B 2 289 ? 35.256  7.209   14.690  1.00 13.16 ? 289 ASP   B C   1 
ATOM   4613 O  O   . ASP   B 2 289 ? 36.227  6.637   14.218  1.00 13.54 ? 289 ASP   B O   1 
ATOM   4614 C  CB  . ASP   B 2 289 ? 36.742  8.687   16.120  1.00 12.90 ? 289 ASP   B CB  1 
ATOM   4615 C  CG  . ASP   B 2 289 ? 36.986  7.609   17.164  1.00 12.53 ? 289 ASP   B CG  1 
ATOM   4616 O  OD1 . ASP   B 2 289 ? 36.034  6.909   17.519  1.00 12.17 ? 289 ASP   B OD1 1 
ATOM   4617 O  OD2 . ASP   B 2 289 ? 38.166  7.474   17.578  1.00 11.91 ? 289 ASP   B OD2 1 
ATOM   4618 N  N   . GLU   B 2 290 ? 34.026  6.691   14.620  1.00 12.76 ? 290 GLU   B N   1 
ATOM   4619 C  CA  . GLU   B 2 290 ? 33.805  5.375   14.047  1.00 14.74 ? 290 GLU   B CA  1 
ATOM   4620 C  C   . GLU   B 2 290 ? 32.976  5.455   12.772  1.00 13.12 ? 290 GLU   B C   1 
ATOM   4621 O  O   . GLU   B 2 290 ? 32.452  4.456   12.319  1.00 12.91 ? 290 GLU   B O   1 
ATOM   4622 C  CB  . GLU   B 2 290 ? 33.240  4.390   15.088  1.00 16.19 ? 290 GLU   B CB  1 
ATOM   4623 C  CG  . GLU   B 2 290 ? 34.259  4.084   16.207  1.00 17.62 ? 290 GLU   B CG  1 
ATOM   4624 C  CD  . GLU   B 2 290 ? 34.225  2.691   16.870  1.00 19.26 ? 290 GLU   B CD  1 
ATOM   4625 O  OE1 . GLU   B 2 290 ? 33.335  1.857   16.524  1.00 18.96 ? 290 GLU   B OE1 1 
ATOM   4626 O  OE2 . GLU   B 2 290 ? 35.124  2.412   17.718  1.00 17.03 ? 290 GLU   B OE2 1 
ATOM   4627 N  N   . PHE   B 2 291 ? 32.939  6.613   12.131  1.00 13.87 ? 291 PHE   B N   1 
ATOM   4628 C  CA  . PHE   B 2 291 ? 32.394  6.692   10.787  1.00 15.06 ? 291 PHE   B CA  1 
ATOM   4629 C  C   . PHE   B 2 291 ? 33.499  7.070   9.808   1.00 14.75 ? 291 PHE   B C   1 
ATOM   4630 O  O   . PHE   B 2 291 ? 34.053  8.160   9.926   1.00 15.51 ? 291 PHE   B O   1 
ATOM   4631 C  CB  . PHE   B 2 291 ? 31.303  7.755   10.672  1.00 17.01 ? 291 PHE   B CB  1 
ATOM   4632 C  CG  . PHE   B 2 291 ? 30.008  7.454   11.375  1.00 20.03 ? 291 PHE   B CG  1 
ATOM   4633 C  CD1 . PHE   B 2 291 ? 29.162  6.464   10.915  1.00 22.91 ? 291 PHE   B CD1 1 
ATOM   4634 C  CD2 . PHE   B 2 291 ? 29.631  8.170   12.502  1.00 24.84 ? 291 PHE   B CD2 1 
ATOM   4635 C  CE1 . PHE   B 2 291 ? 27.954  6.207   11.553  1.00 24.82 ? 291 PHE   B CE1 1 
ATOM   4636 C  CE2 . PHE   B 2 291 ? 28.416  7.923   13.141  1.00 25.79 ? 291 PHE   B CE2 1 
ATOM   4637 C  CZ  . PHE   B 2 291 ? 27.579  6.942   12.662  1.00 26.20 ? 291 PHE   B CZ  1 
ATOM   4638 N  N   . THR   B 2 292 ? 33.755  6.193   8.832   1.00 13.63 ? 292 THR   B N   1 
ATOM   4639 C  CA  . THR   B 2 292 ? 34.754  6.454   7.811   1.00 14.21 ? 292 THR   B CA  1 
ATOM   4640 C  C   . THR   B 2 292 ? 34.205  7.414   6.762   1.00 14.05 ? 292 THR   B C   1 
ATOM   4641 O  O   . THR   B 2 292 ? 32.987  7.668   6.706   1.00 11.77 ? 292 THR   B O   1 
ATOM   4642 C  CB  . THR   B 2 292 ? 35.210  5.175   7.108   1.00 15.15 ? 292 THR   B CB  1 
ATOM   4643 O  OG1 . THR   B 2 292 ? 34.147  4.714   6.273   1.00 16.36 ? 292 THR   B OG1 1 
ATOM   4644 C  CG2 . THR   B 2 292 ? 35.630  4.109   8.098   1.00 15.67 ? 292 THR   B CG2 1 
ATOM   4645 N  N   . PRO   B 2 293 ? 35.103  7.996   5.938   1.00 13.48 ? 293 PRO   B N   1 
ATOM   4646 C  CA  . PRO   B 2 293 ? 34.675  8.811   4.806   1.00 14.41 ? 293 PRO   B CA  1 
ATOM   4647 C  C   . PRO   B 2 293 ? 33.700  8.070   3.899   1.00 16.21 ? 293 PRO   B C   1 
ATOM   4648 O  O   . PRO   B 2 293 ? 32.727  8.663   3.470   1.00 14.89 ? 293 PRO   B O   1 
ATOM   4649 C  CB  . PRO   B 2 293 ? 35.982  9.163   4.082   1.00 13.93 ? 293 PRO   B CB  1 
ATOM   4650 C  CG  . PRO   B 2 293 ? 37.040  9.094   5.184   1.00 13.91 ? 293 PRO   B CG  1 
ATOM   4651 C  CD  . PRO   B 2 293 ? 36.570  7.998   6.121   1.00 13.65 ? 293 PRO   B CD  1 
ATOM   4652 N  N   . PHE   B 2 294 ? 33.934  6.771   3.674   1.00 18.01 ? 294 PHE   B N   1 
ATOM   4653 C  CA  . PHE   B 2 294 ? 33.010  5.954   2.906   1.00 21.51 ? 294 PHE   B CA  1 
ATOM   4654 C  C   . PHE   B 2 294 ? 31.653  5.841   3.599   1.00 19.67 ? 294 PHE   B C   1 
ATOM   4655 O  O   . PHE   B 2 294 ? 30.642  5.973   2.926   1.00 19.26 ? 294 PHE   B O   1 
ATOM   4656 C  CB  . PHE   B 2 294 ? 33.595  4.567   2.655   1.00 28.71 ? 294 PHE   B CB  1 
ATOM   4657 C  CG  . PHE   B 2 294 ? 34.799  4.576   1.741   1.00 38.70 ? 294 PHE   B CG  1 
ATOM   4658 C  CD1 . PHE   B 2 294 ? 34.698  4.984   0.418   1.00 46.86 ? 294 PHE   B CD1 1 
ATOM   4659 C  CD2 . PHE   B 2 294 ? 36.039  4.166   2.204   1.00 44.26 ? 294 PHE   B CD2 1 
ATOM   4660 C  CE1 . PHE   B 2 294 ? 35.812  4.975   -0.412  1.00 52.59 ? 294 PHE   B CE1 1 
ATOM   4661 C  CE2 . PHE   B 2 294 ? 37.153  4.174   1.379   1.00 46.91 ? 294 PHE   B CE2 1 
ATOM   4662 C  CZ  . PHE   B 2 294 ? 37.040  4.581   0.072   1.00 50.24 ? 294 PHE   B CZ  1 
ATOM   4663 N  N   . ASP   B 2 295 ? 31.635  5.611   4.922   1.00 16.62 ? 295 ASP   B N   1 
ATOM   4664 C  CA  . ASP   B 2 295 ? 30.391  5.588   5.693   1.00 17.80 ? 295 ASP   B CA  1 
ATOM   4665 C  C   . ASP   B 2 295 ? 29.573  6.864   5.507   1.00 17.58 ? 295 ASP   B C   1 
ATOM   4666 O  O   . ASP   B 2 295 ? 28.352  6.794   5.418   1.00 18.71 ? 295 ASP   B O   1 
ATOM   4667 C  CB  . ASP   B 2 295 ? 30.607  5.402   7.202   1.00 18.28 ? 295 ASP   B CB  1 
ATOM   4668 C  CG  . ASP   B 2 295 ? 31.031  3.983   7.537   1.00 20.80 ? 295 ASP   B CG  1 
ATOM   4669 O  OD1 . ASP   B 2 295 ? 30.315  3.087   7.090   1.00 22.90 ? 295 ASP   B OD1 1 
ATOM   4670 O  OD2 . ASP   B 2 295 ? 32.038  3.787   8.248   1.00 21.73 ? 295 ASP   B OD2 1 
ATOM   4671 N  N   . VAL   B 2 296 ? 30.241  8.017   5.528   1.00 17.59 ? 296 VAL   B N   1 
ATOM   4672 C  CA  . VAL   B 2 296 ? 29.583  9.310   5.401   1.00 19.02 ? 296 VAL   B CA  1 
ATOM   4673 C  C   . VAL   B 2 296 ? 28.952  9.457   4.010   1.00 21.86 ? 296 VAL   B C   1 
ATOM   4674 O  O   . VAL   B 2 296 ? 27.768  9.806   3.926   1.00 23.15 ? 296 VAL   B O   1 
ATOM   4675 C  CB  . VAL   B 2 296 ? 30.546  10.470  5.725   1.00 18.07 ? 296 VAL   B CB  1 
ATOM   4676 C  CG1 . VAL   B 2 296 ? 29.967  11.831  5.333   1.00 19.54 ? 296 VAL   B CG1 1 
ATOM   4677 C  CG2 . VAL   B 2 296 ? 30.954  10.449  7.188   1.00 17.55 ? 296 VAL   B CG2 1 
ATOM   4678 N  N   . VAL   B 2 297 ? 29.696  9.169   2.924   1.00 20.62 ? 297 VAL   B N   1 
ATOM   4679 C  CA  . VAL   B 2 297 ? 29.093  9.275   1.597   1.00 23.23 ? 297 VAL   B CA  1 
ATOM   4680 C  C   . VAL   B 2 297 ? 27.923  8.292   1.440   1.00 25.99 ? 297 VAL   B C   1 
ATOM   4681 O  O   . VAL   B 2 297 ? 26.937  8.624   0.794   1.00 27.66 ? 297 VAL   B O   1 
ATOM   4682 C  CB  . VAL   B 2 297 ? 30.090  9.121   0.435   1.00 24.51 ? 297 VAL   B CB  1 
ATOM   4683 C  CG1 . VAL   B 2 297 ? 31.158  10.210  0.488   1.00 24.55 ? 297 VAL   B CG1 1 
ATOM   4684 C  CG2 . VAL   B 2 297 ? 30.720  7.734   0.385   1.00 26.40 ? 297 VAL   B CG2 1 
ATOM   4685 N  N   . ARG   B 2 298 ? 28.016  7.086   1.997   1.00 25.84 ? 298 ARG   B N   1 
ATOM   4686 C  CA  . ARG   B 2 298 ? 26.938  6.110   1.894   1.00 30.40 ? 298 ARG   B CA  1 
ATOM   4687 C  C   . ARG   B 2 298 ? 25.653  6.661   2.509   1.00 29.31 ? 298 ARG   B C   1 
ATOM   4688 O  O   . ARG   B 2 298 ? 24.590  6.581   1.904   1.00 31.15 ? 298 ARG   B O   1 
ATOM   4689 C  CB  . ARG   B 2 298 ? 27.270  4.816   2.634   1.00 32.93 ? 298 ARG   B CB  1 
ATOM   4690 C  CG  . ARG   B 2 298 ? 28.137  3.837   1.863   1.00 39.01 ? 298 ARG   B CG  1 
ATOM   4691 C  CD  . ARG   B 2 298 ? 28.337  2.585   2.708   1.00 46.55 ? 298 ARG   B CD  1 
ATOM   4692 N  NE  . ARG   B 2 298 ? 29.244  1.638   2.062   1.00 54.76 ? 298 ARG   B NE  1 
ATOM   4693 C  CZ  . ARG   B 2 298 ? 30.547  1.510   2.312   1.00 59.81 ? 298 ARG   B CZ  1 
ATOM   4694 N  NH1 . ARG   B 2 298 ? 31.130  2.198   3.280   1.00 65.25 ? 298 ARG   B NH1 1 
ATOM   4695 N  NH2 . ARG   B 2 298 ? 31.269  0.674   1.582   1.00 62.39 ? 298 ARG   B NH2 1 
ATOM   4696 N  N   . GLN   B 2 299 ? 25.772  7.269   3.692   1.00 27.36 ? 299 GLN   B N   1 
ATOM   4697 C  CA  . GLN   B 2 299 ? 24.606  7.736   4.427   1.00 28.67 ? 299 GLN   B CA  1 
ATOM   4698 C  C   . GLN   B 2 299 ? 24.096  9.088   3.933   1.00 30.58 ? 299 GLN   B C   1 
ATOM   4699 O  O   . GLN   B 2 299 ? 22.914  9.371   4.089   1.00 29.09 ? 299 GLN   B O   1 
ATOM   4700 C  CB  . GLN   B 2 299 ? 24.903  7.756   5.924   1.00 27.36 ? 299 GLN   B CB  1 
ATOM   4701 C  CG  . GLN   B 2 299 ? 24.786  6.358   6.509   1.00 27.74 ? 299 GLN   B CG  1 
ATOM   4702 C  CD  . GLN   B 2 299 ? 24.998  6.311   7.999   1.00 28.54 ? 299 GLN   B CD  1 
ATOM   4703 O  OE1 . GLN   B 2 299 ? 24.246  6.879   8.793   1.00 29.63 ? 299 GLN   B OE1 1 
ATOM   4704 N  NE2 . GLN   B 2 299 ? 26.007  5.555   8.391   1.00 30.95 ? 299 GLN   B NE2 1 
ATOM   4705 N  N   . CYS   B 2 300 ? 24.965  9.915   3.345   1.00 31.01 ? 300 CYS   B N   1 
ATOM   4706 C  CA  . CYS   B 2 300 ? 24.572  11.244  2.910   1.00 33.16 ? 300 CYS   B CA  1 
ATOM   4707 C  C   . CYS   B 2 300 ? 24.010  11.175  1.487   1.00 36.56 ? 300 CYS   B C   1 
ATOM   4708 O  O   . CYS   B 2 300 ? 23.026  11.857  1.187   1.00 34.81 ? 300 CYS   B O   1 
ATOM   4709 C  CB  . CYS   B 2 300 ? 25.740  12.228  3.011   1.00 37.70 ? 300 CYS   B CB  1 
ATOM   4710 S  SG  . CYS   B 2 300 ? 26.206  12.661  4.718   1.00 41.32 ? 300 CYS   B SG  1 
ATOM   4711 N  N   . SER   B 2 301 ? 24.594  10.295  0.653   1.00 37.68 ? 301 SER   B N   1 
ATOM   4712 C  CA  . SER   B 2 301 ? 24.404  10.303  -0.791  1.00 37.68 ? 301 SER   B CA  1 
ATOM   4713 C  C   . SER   B 2 301 ? 24.009  8.924   -1.337  1.00 34.36 ? 301 SER   B C   1 
ATOM   4714 O  O   . SER   B 2 301 ? 24.118  7.935   -0.598  1.00 34.73 ? 301 SER   B O   1 
ATOM   4715 C  CB  . SER   B 2 301 ? 25.668  10.812  -1.479  1.00 39.08 ? 301 SER   B CB  1 
ATOM   4716 O  OG  . SER   B 2 301 ? 25.964  12.155  -1.083  1.00 34.74 ? 301 SER   B OG  1 
ATOM   4717 O  OXT . SER   B 2 301 ? 23.636  8.888   -2.516  1.00 36.32 ? 301 SER   B OXT 1 
HETATM 4718 N  N1  . A1D81 C 3 .   ? 8.386   9.257   -3.473  1.00 17.16 ? 401 A1D81 A N1  1 
HETATM 4719 N  N3  . A1D81 C 3 .   ? 10.532  8.144   -0.072  1.00 15.71 ? 401 A1D81 A N3  1 
HETATM 4720 C  C4  . A1D81 C 3 .   ? 8.178   7.233   -4.837  1.00 17.65 ? 401 A1D81 A C4  1 
HETATM 4721 C  C5  . A1D81 C 3 .   ? 8.534   8.581   -4.694  1.00 18.35 ? 401 A1D81 A C5  1 
HETATM 4722 C  C6  . A1D81 C 3 .   ? 9.139   9.298   -5.705  1.00 19.62 ? 401 A1D81 A C6  1 
HETATM 4723 C  C7  . A1D81 C 3 .   ? 9.120   8.899   -2.343  1.00 15.94 ? 401 A1D81 A C7  1 
HETATM 4724 C  C8  . A1D81 C 3 .   ? 9.552   9.114   0.035   1.00 14.97 ? 401 A1D81 A C8  1 
HETATM 4725 C  C10 . A1D81 C 3 .   ? 10.120  7.923   -2.425  1.00 17.45 ? 401 A1D81 A C10 1 
HETATM 4726 C  C13 . A1D81 C 3 .   ? 5.439   10.709  -0.212  1.00 18.10 ? 401 A1D81 A C13 1 
HETATM 4727 C  C15 . A1D81 C 3 .   ? 4.057   8.857   0.212   1.00 17.32 ? 401 A1D81 A C15 1 
HETATM 4728 C  C17 . A1D81 C 3 .   ? 6.312   8.524   -0.527  1.00 16.18 ? 401 A1D81 A C17 1 
HETATM 4729 C  C20 . A1D81 C 3 .   ? 13.852  9.177   2.919   1.00 13.94 ? 401 A1D81 A C20 1 
HETATM 4730 C  C21 . A1D81 C 3 .   ? 14.627  11.160  1.563   1.00 14.73 ? 401 A1D81 A C21 1 
HETATM 4731 C  C22 . A1D81 C 3 .   ? 9.905   9.017   -8.160  1.00 21.76 ? 401 A1D81 A C22 1 
HETATM 4732 C  C24 . A1D81 C 3 .   ? 11.836  7.654   -10.319 1.00 33.41 ? 401 A1D81 A C24 1 
HETATM 4733 C  C26 . A1D81 C 3 .   ? 12.312  7.101   -12.729 1.00 42.21 ? 401 A1D81 A C26 1 
HETATM 4734 C  C1  . A1D81 C 3 .   ? 9.363   8.657   -6.929  1.00 21.41 ? 401 A1D81 A C1  1 
HETATM 4735 C  C2  . A1D81 C 3 .   ? 8.981   7.298   -7.095  1.00 20.08 ? 401 A1D81 A C2  1 
HETATM 4736 C  C3  . A1D81 C 3 .   ? 8.385   6.585   -6.035  1.00 17.21 ? 401 A1D81 A C3  1 
HETATM 4737 CL CL1 . A1D81 C 3 .   ? 7.455   6.334   -3.528  1.00 18.28 ? 401 A1D81 A CL1 1 
HETATM 4738 N  N2  . A1D81 C 3 .   ? 8.888   9.507   -1.121  1.00 15.91 ? 401 A1D81 A N2  1 
HETATM 4739 C  C9  . A1D81 C 3 .   ? 10.867  7.523   -1.279  1.00 15.66 ? 401 A1D81 A C9  1 
HETATM 4740 O  O1  . A1D81 C 3 .   ? 11.734  6.652   -1.250  1.00 15.24 ? 401 A1D81 A O1  1 
HETATM 4741 O  O2  . A1D81 C 3 .   ? 9.333   9.659   1.101   1.00 14.80 ? 401 A1D81 A O2  1 
HETATM 4742 C  C11 . A1D81 C 3 .   ? 7.831   10.523  -0.943  1.00 16.44 ? 401 A1D81 A C11 1 
HETATM 4743 C  C12 . A1D81 C 3 .   ? 6.514   9.900   -0.541  1.00 16.15 ? 401 A1D81 A C12 1 
HETATM 4744 C  C14 . A1D81 C 3 .   ? 4.209   10.217  0.190   1.00 16.83 ? 401 A1D81 A C14 1 
HETATM 4745 C  C16 . A1D81 C 3 .   ? 5.090   8.020   -0.139  1.00 16.34 ? 401 A1D81 A C16 1 
HETATM 4746 F  F1  . A1D81 C 3 .   ? 4.884   6.687   -0.065  1.00 16.51 ? 401 A1D81 A F1  1 
HETATM 4747 F  F2  . A1D81 C 3 .   ? 2.879   8.300   0.552   1.00 18.94 ? 401 A1D81 A F2  1 
HETATM 4748 F  F3  . A1D81 C 3 .   ? 5.603   12.061  -0.266  1.00 19.97 ? 401 A1D81 A F3  1 
HETATM 4749 C  C18 . A1D81 C 3 .   ? 11.215  7.663   1.159   1.00 15.41 ? 401 A1D81 A C18 1 
HETATM 4750 C  C19 . A1D81 C 3 .   ? 12.332  8.514   1.641   1.00 15.49 ? 401 A1D81 A C19 1 
HETATM 4751 N  N4  . A1D81 C 3 .   ? 12.938  8.241   2.810   1.00 14.19 ? 401 A1D81 A N4  1 
HETATM 4752 N  N5  . A1D81 C 3 .   ? 13.800  9.986   1.860   1.00 14.80 ? 401 A1D81 A N5  1 
HETATM 4753 N  N6  . A1D81 C 3 .   ? 12.825  9.565   1.023   1.00 13.51 ? 401 A1D81 A N6  1 
HETATM 4754 N  N7  . A1D81 C 3 .   ? 9.827   7.944   -8.937  1.00 23.89 ? 401 A1D81 A N7  1 
HETATM 4755 N  N8  . A1D81 C 3 .   ? 9.288   6.850   -8.334  1.00 20.43 ? 401 A1D81 A N8  1 
HETATM 4756 C  C23 . A1D81 C 3 .   ? 10.324  7.816   -10.306 1.00 29.22 ? 401 A1D81 A C23 1 
HETATM 4757 C  C25 . A1D81 C 3 .   ? 12.343  6.606   -11.296 1.00 41.11 ? 401 A1D81 A C25 1 
HETATM 4758 C  C27 . A1D81 C 3 .   ? 13.758  6.173   -10.936 1.00 43.82 ? 401 A1D81 A C27 1 
HETATM 4759 N  N1  . A1D81 D 3 .   ? 37.142  -19.956 24.475  1.00 18.55 ? 401 A1D81 B N1  1 
HETATM 4760 N  N3  . A1D81 D 3 .   ? 35.531  -16.319 23.234  1.00 19.69 ? 401 A1D81 B N3  1 
HETATM 4761 C  C4  . A1D81 D 3 .   ? 36.373  -21.667 22.905  1.00 20.97 ? 401 A1D81 B C4  1 
HETATM 4762 C  C5  . A1D81 D 3 .   ? 36.511  -21.188 24.214  1.00 20.50 ? 401 A1D81 B C5  1 
HETATM 4763 C  C6  . A1D81 D 3 .   ? 35.989  -21.864 25.292  1.00 21.62 ? 401 A1D81 B C6  1 
HETATM 4764 C  C7  . A1D81 D 3 .   ? 36.579  -18.754 24.047  1.00 18.09 ? 401 A1D81 B C7  1 
HETATM 4765 C  C8  . A1D81 D 3 .   ? 36.786  -16.362 23.825  1.00 18.75 ? 401 A1D81 B C8  1 
HETATM 4766 C  C10 . A1D81 D 3 .   ? 35.315  -18.697 23.455  1.00 18.21 ? 401 A1D81 B C10 1 
HETATM 4767 C  C13 . A1D81 D 3 .   ? 41.018  -17.496 24.282  1.00 21.92 ? 401 A1D81 B C13 1 
HETATM 4768 C  C15 . A1D81 D 3 .   ? 41.849  -17.786 22.119  1.00 22.54 ? 401 A1D81 B C15 1 
HETATM 4769 C  C17 . A1D81 D 3 .   ? 39.500  -17.893 22.505  1.00 20.89 ? 401 A1D81 B C17 1 
HETATM 4770 C  C20 . A1D81 D 3 .   ? 33.359  -12.432 24.329  1.00 23.03 ? 401 A1D81 B C20 1 
HETATM 4771 C  C21 . A1D81 D 3 .   ? 32.853  -13.245 26.658  1.00 22.62 ? 401 A1D81 B C21 1 
HETATM 4772 C  C22 . A1D81 D 3 .   ? 34.659  -23.984 25.870  1.00 26.32 ? 401 A1D81 B C22 1 
HETATM 4773 C  C24 . A1D81 D 3 .   ? 31.979  -25.991 24.936  1.00 34.76 ? 401 A1D81 B C24 1 
HETATM 4774 C  C26 . A1D81 D 3 .   ? 29.951  -24.565 25.364  1.00 42.46 ? 401 A1D81 B C26 1 
HETATM 4775 C  C1  . A1D81 D 3 .   ? 35.310  -23.057 25.068  1.00 23.62 ? 401 A1D81 B C1  1 
HETATM 4776 C  C2  . A1D81 D 3 .   ? 35.158  -23.558 23.749  1.00 23.70 ? 401 A1D81 B C2  1 
HETATM 4777 C  C3  . A1D81 D 3 .   ? 35.706  -22.852 22.662  1.00 22.18 ? 401 A1D81 B C3  1 
HETATM 4778 CL CL1 . A1D81 D 3 .   ? 37.075  -20.784 21.570  1.00 20.82 ? 401 A1D81 B CL1 1 
HETATM 4779 N  N2  . A1D81 D 3 .   ? 37.279  -17.588 24.232  1.00 19.34 ? 401 A1D81 B N2  1 
HETATM 4780 C  C9  . A1D81 D 3 .   ? 34.757  -17.474 23.021  1.00 18.52 ? 401 A1D81 B C9  1 
HETATM 4781 O  O1  . A1D81 D 3 .   ? 33.661  -17.360 22.477  1.00 18.55 ? 401 A1D81 B O1  1 
HETATM 4782 O  O2  . A1D81 D 3 .   ? 37.458  -15.369 23.993  1.00 20.26 ? 401 A1D81 B O2  1 
HETATM 4783 C  C11 . A1D81 D 3 .   ? 38.611  -17.558 24.859  1.00 20.01 ? 401 A1D81 B C11 1 
HETATM 4784 C  C12 . A1D81 D 3 .   ? 39.722  -17.624 23.848  1.00 20.73 ? 401 A1D81 B C12 1 
HETATM 4785 C  C14 . A1D81 D 3 .   ? 42.105  -17.547 23.440  1.00 20.88 ? 401 A1D81 B C14 1 
HETATM 4786 C  C16 . A1D81 D 3 .   ? 40.567  -17.956 21.647  1.00 22.41 ? 401 A1D81 B C16 1 
HETATM 4787 F  F1  . A1D81 D 3 .   ? 40.377  -18.186 20.330  1.00 21.26 ? 401 A1D81 B F1  1 
HETATM 4788 F  F2  . A1D81 D 3 .   ? 42.873  -17.875 21.257  1.00 26.88 ? 401 A1D81 B F2  1 
HETATM 4789 F  F3  . A1D81 D 3 .   ? 41.243  -17.242 25.600  1.00 23.52 ? 401 A1D81 B F3  1 
HETATM 4790 C  C18 . A1D81 D 3 .   ? 35.034  -15.041 22.663  1.00 21.64 ? 401 A1D81 B C18 1 
HETATM 4791 C  C19 . A1D81 D 3 .   ? 34.317  -14.153 23.619  1.00 22.73 ? 401 A1D81 B C19 1 
HETATM 4792 N  N4  . A1D81 D 3 .   ? 33.956  -12.930 23.266  1.00 22.29 ? 401 A1D81 B N4  1 
HETATM 4793 N  N5  . A1D81 D 3 .   ? 33.386  -13.329 25.309  1.00 22.88 ? 401 A1D81 B N5  1 
HETATM 4794 N  N6  . A1D81 D 3 .   ? 33.990  -14.450 24.847  1.00 21.82 ? 401 A1D81 B N6  1 
HETATM 4795 N  N7  . A1D81 D 3 .   ? 34.191  -24.928 25.062  1.00 28.74 ? 401 A1D81 B N7  1 
HETATM 4796 N  N8  . A1D81 D 3 .   ? 34.458  -24.719 23.740  1.00 25.07 ? 401 A1D81 B N8  1 
HETATM 4797 C  C23 . A1D81 D 3 .   ? 33.397  -26.081 25.466  1.00 31.13 ? 401 A1D81 B C23 1 
HETATM 4798 C  C25 . A1D81 D 3 .   ? 30.954  -25.536 25.958  1.00 41.39 ? 401 A1D81 B C25 1 
HETATM 4799 C  C27 . A1D81 D 3 .   ? 30.226  -26.736 26.554  1.00 44.92 ? 401 A1D81 B C27 1 
HETATM 4800 O  O   . HOH   E 4 .   ? 17.705  11.246  -0.106  1.00 23.93 ? 501 HOH   A O   1 
HETATM 4801 O  O   . HOH   E 4 .   ? 1.859   -15.760 2.321   1.00 36.51 ? 502 HOH   A O   1 
HETATM 4802 O  O   . HOH   E 4 .   ? 4.863   -8.282  31.916  1.00 48.74 ? 503 HOH   A O   1 
HETATM 4803 O  O   . HOH   E 4 .   ? 16.705  12.243  28.392  1.00 26.52 ? 504 HOH   A O   1 
HETATM 4804 O  O   . HOH   E 4 .   ? 2.322   -0.999  40.735  1.00 45.67 ? 505 HOH   A O   1 
HETATM 4805 O  O   . HOH   E 4 .   ? 30.924  5.952   29.164  1.00 31.14 ? 506 HOH   A O   1 
HETATM 4806 O  O   . HOH   E 4 .   ? 9.147   8.707   46.330  1.00 34.54 ? 507 HOH   A O   1 
HETATM 4807 O  O   . HOH   E 4 .   ? 20.255  -14.805 25.371  1.00 38.86 ? 508 HOH   A O   1 
HETATM 4808 O  O   . HOH   E 4 .   ? 20.803  -9.037  -0.177  1.00 31.13 ? 509 HOH   A O   1 
HETATM 4809 O  O   . HOH   E 4 .   ? 18.647  -2.092  45.142  1.00 28.70 ? 510 HOH   A O   1 
HETATM 4810 O  O   . HOH   E 4 .   ? 6.020   -20.154 -0.820  1.00 48.15 ? 511 HOH   A O   1 
HETATM 4811 O  O   . HOH   E 4 .   ? -2.117  6.661   -11.366 1.00 28.06 ? 512 HOH   A O   1 
HETATM 4812 O  O   . HOH   E 4 .   ? 21.891  9.193   39.138  1.00 21.52 ? 513 HOH   A O   1 
HETATM 4813 O  O   . HOH   E 4 .   ? 2.620   3.527   36.538  1.00 34.44 ? 514 HOH   A O   1 
HETATM 4814 O  O   . HOH   E 4 .   ? 17.927  2.734   17.359  1.00 29.63 ? 515 HOH   A O   1 
HETATM 4815 O  O   . HOH   E 4 .   ? 2.493   6.931   22.130  1.00 23.92 ? 516 HOH   A O   1 
HETATM 4816 O  O   . HOH   E 4 .   ? 5.810   -7.969  -13.896 1.00 27.75 ? 517 HOH   A O   1 
HETATM 4817 O  O   . HOH   E 4 .   ? 3.809   10.699  27.554  1.00 37.93 ? 518 HOH   A O   1 
HETATM 4818 O  O   . HOH   E 4 .   ? -0.163  -17.485 -7.726  1.00 29.71 ? 519 HOH   A O   1 
HETATM 4819 O  O   . HOH   E 4 .   ? 17.408  0.207   18.596  1.00 30.94 ? 520 HOH   A O   1 
HETATM 4820 O  O   . HOH   E 4 .   ? 11.819  11.029  -0.811  1.00 23.03 ? 521 HOH   A O   1 
HETATM 4821 O  O   . HOH   E 4 .   ? 2.817   -1.203  30.331  1.00 20.09 ? 522 HOH   A O   1 
HETATM 4822 O  O   . HOH   E 4 .   ? 16.185  -7.384  19.471  1.00 38.23 ? 523 HOH   A O   1 
HETATM 4823 O  O   . HOH   E 4 .   ? 3.982   -3.332  29.058  1.00 36.76 ? 524 HOH   A O   1 
HETATM 4824 O  O   . HOH   E 4 .   ? 28.830  -3.792  37.411  1.00 26.04 ? 525 HOH   A O   1 
HETATM 4825 O  O   . HOH   E 4 .   ? 11.728  -19.407 8.297   1.00 28.06 ? 526 HOH   A O   1 
HETATM 4826 O  O   . HOH   E 4 .   ? -3.552  -2.503  11.568  1.00 34.09 ? 527 HOH   A O   1 
HETATM 4827 O  O   . HOH   E 4 .   ? 13.434  5.440   15.944  1.00 13.47 ? 528 HOH   A O   1 
HETATM 4828 O  O   . HOH   E 4 .   ? 5.199   10.979  -12.997 1.00 33.84 ? 529 HOH   A O   1 
HETATM 4829 O  O   . HOH   E 4 .   ? -10.550 1.087   -6.639  1.00 23.69 ? 530 HOH   A O   1 
HETATM 4830 O  O   . HOH   E 4 .   ? -8.275  -2.102  -10.738 1.00 25.17 ? 531 HOH   A O   1 
HETATM 4831 O  O   . HOH   E 4 .   ? 8.744   -13.712 14.833  1.00 28.20 ? 532 HOH   A O   1 
HETATM 4832 O  O   . HOH   E 4 .   ? 11.534  -9.437  31.228  1.00 35.48 ? 533 HOH   A O   1 
HETATM 4833 O  O   . HOH   E 4 .   ? 8.486   -20.178 -7.984  1.00 21.80 ? 534 HOH   A O   1 
HETATM 4834 O  O   . HOH   E 4 .   ? 7.079   8.510   -11.287 1.00 40.00 ? 535 HOH   A O   1 
HETATM 4835 O  O   . HOH   E 4 .   ? 17.216  11.410  4.700   1.00 24.79 ? 536 HOH   A O   1 
HETATM 4836 O  O   . HOH   E 4 .   ? 12.584  12.195  20.073  1.00 46.64 ? 537 HOH   A O   1 
HETATM 4837 O  O   . HOH   E 4 .   ? 13.729  2.315   -5.145  1.00 26.70 ? 538 HOH   A O   1 
HETATM 4838 O  O   . HOH   E 4 .   ? 5.099   14.418  29.674  1.00 38.71 ? 539 HOH   A O   1 
HETATM 4839 O  O   . HOH   E 4 .   ? 9.014   16.284  19.464  1.00 31.19 ? 540 HOH   A O   1 
HETATM 4840 O  O   . HOH   E 4 .   ? 6.158   -19.056 4.972   1.00 34.42 ? 541 HOH   A O   1 
HETATM 4841 O  O   . HOH   E 4 .   ? 12.514  18.487  38.764  1.00 33.57 ? 542 HOH   A O   1 
HETATM 4842 O  O   . HOH   E 4 .   ? 18.771  7.940   -2.943  1.00 30.57 ? 543 HOH   A O   1 
HETATM 4843 O  O   . HOH   E 4 .   ? -2.203  -19.216 -4.330  1.00 42.09 ? 544 HOH   A O   1 
HETATM 4844 O  O   . HOH   E 4 .   ? 17.746  7.069   22.094  1.00 34.32 ? 545 HOH   A O   1 
HETATM 4845 O  O   . HOH   E 4 .   ? 19.584  3.762   3.788   1.00 28.74 ? 546 HOH   A O   1 
HETATM 4846 O  O   . HOH   E 4 .   ? 1.637   9.684   20.032  1.00 28.08 ? 547 HOH   A O   1 
HETATM 4847 O  O   . HOH   E 4 .   ? 10.008  -3.050  -11.344 1.00 16.03 ? 548 HOH   A O   1 
HETATM 4848 O  O   . HOH   E 4 .   ? 14.007  -5.789  18.377  1.00 21.89 ? 549 HOH   A O   1 
HETATM 4849 O  O   . HOH   E 4 .   ? 24.887  18.093  33.910  1.00 41.84 ? 550 HOH   A O   1 
HETATM 4850 O  O   . HOH   E 4 .   ? 1.162   0.707   36.512  1.00 31.76 ? 551 HOH   A O   1 
HETATM 4851 O  O   . HOH   E 4 .   ? 3.989   4.208   29.173  1.00 31.25 ? 552 HOH   A O   1 
HETATM 4852 O  O   . HOH   E 4 .   ? 14.369  -15.234 2.271   1.00 17.49 ? 553 HOH   A O   1 
HETATM 4853 O  O   . HOH   E 4 .   ? 13.283  -4.177  3.215   1.00 17.70 ? 554 HOH   A O   1 
HETATM 4854 O  O   . HOH   E 4 .   ? 18.273  -7.339  17.404  1.00 24.92 ? 555 HOH   A O   1 
HETATM 4855 O  O   . HOH   E 4 .   ? 5.660   -20.258 2.735   1.00 37.84 ? 556 HOH   A O   1 
HETATM 4856 O  O   . HOH   E 4 .   ? 3.815   -18.744 4.172   1.00 43.26 ? 557 HOH   A O   1 
HETATM 4857 O  O   . HOH   E 4 .   ? 9.703   -0.855  25.308  1.00 15.12 ? 558 HOH   A O   1 
HETATM 4858 O  O   . HOH   E 4 .   ? 3.050   -7.953  -14.612 1.00 33.85 ? 559 HOH   A O   1 
HETATM 4859 O  O   . HOH   E 4 .   ? 12.089  13.825  26.427  1.00 33.59 ? 560 HOH   A O   1 
HETATM 4860 O  O   . HOH   E 4 .   ? 12.749  0.691   46.617  1.00 46.82 ? 561 HOH   A O   1 
HETATM 4861 O  O   . HOH   E 4 .   ? 12.980  15.724  4.732   1.00 37.29 ? 562 HOH   A O   1 
HETATM 4862 O  O   . HOH   E 4 .   ? -9.399  10.986  -9.147  1.00 35.31 ? 563 HOH   A O   1 
HETATM 4863 O  O   . HOH   E 4 .   ? -4.427  -8.930  -4.600  1.00 29.86 ? 564 HOH   A O   1 
HETATM 4864 O  O   . HOH   E 4 .   ? 14.147  9.982   44.243  1.00 40.54 ? 565 HOH   A O   1 
HETATM 4865 O  O   . HOH   E 4 .   ? -0.029  19.949  5.668   1.00 36.90 ? 566 HOH   A O   1 
HETATM 4866 O  O   . HOH   E 4 .   ? 2.335   5.214   -11.418 1.00 33.63 ? 567 HOH   A O   1 
HETATM 4867 O  O   . HOH   E 4 .   ? 2.484   12.008  15.890  1.00 13.65 ? 568 HOH   A O   1 
HETATM 4868 O  O   . HOH   E 4 .   ? 14.140  -12.571 19.058  1.00 43.17 ? 569 HOH   A O   1 
HETATM 4869 O  O   . HOH   E 4 .   ? 3.268   18.993  16.286  1.00 35.11 ? 570 HOH   A O   1 
HETATM 4870 O  O   . HOH   E 4 .   ? 17.533  -2.614  19.764  1.00 25.46 ? 571 HOH   A O   1 
HETATM 4871 O  O   . HOH   E 4 .   ? 4.536   -0.435  -15.416 1.00 37.14 ? 572 HOH   A O   1 
HETATM 4872 O  O   . HOH   E 4 .   ? 21.338  1.674   3.432   1.00 27.65 ? 573 HOH   A O   1 
HETATM 4873 O  O   . HOH   E 4 .   ? 1.749   -13.737 0.830   1.00 24.28 ? 574 HOH   A O   1 
HETATM 4874 O  O   . HOH   E 4 .   ? -5.014  -8.465  7.337   1.00 26.93 ? 575 HOH   A O   1 
HETATM 4875 O  O   . HOH   E 4 .   ? -0.967  14.081  8.620   1.00 19.25 ? 576 HOH   A O   1 
HETATM 4876 O  O   . HOH   E 4 .   ? -3.431  7.277   6.736   1.00 9.50  ? 577 HOH   A O   1 
HETATM 4877 O  O   . HOH   E 4 .   ? 5.444   -0.752  26.674  1.00 34.44 ? 578 HOH   A O   1 
HETATM 4878 O  O   . HOH   E 4 .   ? 4.836   6.263   10.968  1.00 9.79  ? 579 HOH   A O   1 
HETATM 4879 O  O   . HOH   E 4 .   ? 7.347   16.615  12.966  1.00 22.34 ? 580 HOH   A O   1 
HETATM 4880 O  O   . HOH   E 4 .   ? -5.542  -13.026 -13.845 1.00 33.44 ? 581 HOH   A O   1 
HETATM 4881 O  O   . HOH   E 4 .   ? 9.731   2.818   47.145  1.00 33.51 ? 582 HOH   A O   1 
HETATM 4882 O  O   . HOH   E 4 .   ? 0.626   0.663   17.885  1.00 33.49 ? 583 HOH   A O   1 
HETATM 4883 O  O   . HOH   E 4 .   ? 15.431  10.078  11.158  1.00 21.97 ? 584 HOH   A O   1 
HETATM 4884 O  O   . HOH   E 4 .   ? 11.839  5.587   -6.100  1.00 24.91 ? 585 HOH   A O   1 
HETATM 4885 O  O   . HOH   E 4 .   ? 16.238  14.326  2.858   1.00 27.96 ? 586 HOH   A O   1 
HETATM 4886 O  O   . HOH   E 4 .   ? -14.817 8.567   -8.666  1.00 32.30 ? 587 HOH   A O   1 
HETATM 4887 O  O   . HOH   E 4 .   ? 2.463   6.259   38.645  1.00 33.25 ? 588 HOH   A O   1 
HETATM 4888 O  O   . HOH   E 4 .   ? 17.402  2.176   25.634  1.00 12.66 ? 589 HOH   A O   1 
HETATM 4889 O  O   . HOH   E 4 .   ? 10.473  -6.367  38.812  1.00 25.11 ? 590 HOH   A O   1 
HETATM 4890 O  O   . HOH   E 4 .   ? 1.992   -5.710  10.141  1.00 16.18 ? 591 HOH   A O   1 
HETATM 4891 O  O   . HOH   E 4 .   ? 0.276   -12.716 9.921   1.00 26.17 ? 592 HOH   A O   1 
HETATM 4892 O  O   . HOH   E 4 .   ? 9.518   15.116  13.969  1.00 25.08 ? 593 HOH   A O   1 
HETATM 4893 O  O   . HOH   E 4 .   ? -1.645  -7.509  4.118   1.00 28.22 ? 594 HOH   A O   1 
HETATM 4894 O  O   . HOH   E 4 .   ? 16.433  10.298  43.045  1.00 21.77 ? 595 HOH   A O   1 
HETATM 4895 O  O   . HOH   E 4 .   ? 13.038  -4.447  41.893  1.00 33.06 ? 596 HOH   A O   1 
HETATM 4896 O  O   . HOH   E 4 .   ? 32.283  8.203   23.602  1.00 40.56 ? 597 HOH   A O   1 
HETATM 4897 O  O   . HOH   E 4 .   ? 3.041   20.703  1.741   1.00 33.41 ? 598 HOH   A O   1 
HETATM 4898 O  O   . HOH   E 4 .   ? 7.942   13.466  -2.723  1.00 40.77 ? 599 HOH   A O   1 
HETATM 4899 O  O   . HOH   E 4 .   ? 24.600  -4.349  42.882  1.00 36.35 ? 600 HOH   A O   1 
HETATM 4900 O  O   . HOH   E 4 .   ? 20.824  -1.124  -3.100  1.00 38.53 ? 601 HOH   A O   1 
HETATM 4901 O  O   . HOH   E 4 .   ? 8.041   -7.332  14.556  1.00 23.55 ? 602 HOH   A O   1 
HETATM 4902 O  O   . HOH   E 4 .   ? -8.536  -0.762  1.608   1.00 26.06 ? 603 HOH   A O   1 
HETATM 4903 O  O   . HOH   E 4 .   ? 6.123   10.923  -3.850  1.00 18.85 ? 604 HOH   A O   1 
HETATM 4904 O  O   . HOH   E 4 .   ? 5.720   15.193  4.726   1.00 18.71 ? 605 HOH   A O   1 
HETATM 4905 O  O   . HOH   E 4 .   ? -6.247  5.857   3.509   1.00 14.22 ? 606 HOH   A O   1 
HETATM 4906 O  O   . HOH   E 4 .   ? -1.088  4.935   15.253  1.00 18.70 ? 607 HOH   A O   1 
HETATM 4907 O  O   . HOH   E 4 .   ? 26.077  -5.555  39.803  1.00 35.85 ? 608 HOH   A O   1 
HETATM 4908 O  O   . HOH   E 4 .   ? 9.673   12.570  15.592  1.00 26.41 ? 609 HOH   A O   1 
HETATM 4909 O  O   . HOH   E 4 .   ? 10.435  -4.745  20.464  1.00 33.10 ? 610 HOH   A O   1 
HETATM 4910 O  O   . HOH   E 4 .   ? -4.441  14.360  -7.783  1.00 39.95 ? 611 HOH   A O   1 
HETATM 4911 O  O   . HOH   E 4 .   ? 5.867   2.618   44.611  1.00 18.12 ? 612 HOH   A O   1 
HETATM 4912 O  O   . HOH   E 4 .   ? -4.353  -10.887 2.469   1.00 41.72 ? 613 HOH   A O   1 
HETATM 4913 O  O   . HOH   E 4 .   ? -3.833  9.332   9.601   1.00 18.15 ? 614 HOH   A O   1 
HETATM 4914 O  O   . HOH   E 4 .   ? 27.270  -9.968  29.681  1.00 36.50 ? 615 HOH   A O   1 
HETATM 4915 O  O   . HOH   E 4 .   ? 4.371   6.843   -13.777 1.00 28.71 ? 616 HOH   A O   1 
HETATM 4916 O  O   . HOH   E 4 .   ? -6.578  17.128  2.624   1.00 31.26 ? 617 HOH   A O   1 
HETATM 4917 O  O   . HOH   E 4 .   ? 15.149  -7.771  -6.586  1.00 40.37 ? 618 HOH   A O   1 
HETATM 4918 O  O   . HOH   E 4 .   ? 1.353   4.407   -0.080  1.00 13.15 ? 619 HOH   A O   1 
HETATM 4919 O  O   . HOH   E 4 .   ? -7.257  3.113   5.321   1.00 33.19 ? 620 HOH   A O   1 
HETATM 4920 O  O   . HOH   E 4 .   ? 15.593  9.512   22.128  1.00 37.05 ? 621 HOH   A O   1 
HETATM 4921 O  O   . HOH   E 4 .   ? 11.720  -1.834  42.876  1.00 18.04 ? 622 HOH   A O   1 
HETATM 4922 O  O   . HOH   E 4 .   ? -7.398  -4.600  6.962   1.00 23.37 ? 623 HOH   A O   1 
HETATM 4923 O  O   . HOH   E 4 .   ? -7.077  -10.055 -12.041 1.00 38.13 ? 624 HOH   A O   1 
HETATM 4924 O  O   . HOH   E 4 .   ? -0.121  -12.572 4.286   1.00 36.01 ? 625 HOH   A O   1 
HETATM 4925 O  O   . HOH   E 4 .   ? 20.351  -6.110  21.538  1.00 24.68 ? 626 HOH   A O   1 
HETATM 4926 O  O   . HOH   E 4 .   ? -1.142  2.481   16.899  1.00 28.06 ? 627 HOH   A O   1 
HETATM 4927 O  O   . HOH   E 4 .   ? 17.343  16.210  31.757  1.00 31.64 ? 628 HOH   A O   1 
HETATM 4928 O  O   . HOH   E 4 .   ? 12.521  -6.037  21.638  1.00 24.23 ? 629 HOH   A O   1 
HETATM 4929 O  O   . HOH   E 4 .   ? 15.867  -13.823 -9.660  1.00 40.90 ? 630 HOH   A O   1 
HETATM 4930 O  O   . HOH   E 4 .   ? 17.180  11.746  8.313   1.00 48.39 ? 631 HOH   A O   1 
HETATM 4931 O  O   . HOH   E 4 .   ? 5.784   -21.062 -8.394  1.00 31.85 ? 632 HOH   A O   1 
HETATM 4932 O  O   . HOH   E 4 .   ? -8.769  -3.461  -3.752  1.00 21.16 ? 633 HOH   A O   1 
HETATM 4933 O  O   . HOH   E 4 .   ? 26.665  10.295  22.481  1.00 30.03 ? 634 HOH   A O   1 
HETATM 4934 O  O   . HOH   E 4 .   ? -0.295  -7.464  15.892  1.00 25.96 ? 635 HOH   A O   1 
HETATM 4935 O  O   . HOH   E 4 .   ? 21.797  -0.930  14.397  1.00 20.64 ? 636 HOH   A O   1 
HETATM 4936 O  O   . HOH   E 4 .   ? 31.425  3.905   35.969  1.00 37.52 ? 637 HOH   A O   1 
HETATM 4937 O  O   . HOH   E 4 .   ? -6.173  9.062   -13.126 1.00 30.55 ? 638 HOH   A O   1 
HETATM 4938 O  O   . HOH   E 4 .   ? 2.780   8.993   24.032  1.00 40.73 ? 639 HOH   A O   1 
HETATM 4939 O  O   . HOH   E 4 .   ? 1.260   -16.063 8.275   1.00 41.18 ? 640 HOH   A O   1 
HETATM 4940 O  O   . HOH   E 4 .   ? 25.039  3.142   24.384  1.00 33.32 ? 641 HOH   A O   1 
HETATM 4941 O  O   . HOH   E 4 .   ? 12.463  9.841   -3.678  1.00 35.57 ? 642 HOH   A O   1 
HETATM 4942 O  O   . HOH   E 4 .   ? 4.546   -18.507 7.424   1.00 21.30 ? 643 HOH   A O   1 
HETATM 4943 O  O   . HOH   E 4 .   ? 13.844  -9.097  40.159  1.00 34.47 ? 644 HOH   A O   1 
HETATM 4944 O  O   . HOH   E 4 .   ? 19.876  12.729  27.419  1.00 32.02 ? 645 HOH   A O   1 
HETATM 4945 O  O   . HOH   E 4 .   ? -4.027  7.338   4.178   1.00 16.23 ? 646 HOH   A O   1 
HETATM 4946 O  O   . HOH   E 4 .   ? 29.600  0.269   24.279  1.00 39.84 ? 647 HOH   A O   1 
HETATM 4947 O  O   . HOH   E 4 .   ? 8.143   3.761   29.538  1.00 14.44 ? 648 HOH   A O   1 
HETATM 4948 O  O   . HOH   E 4 .   ? 19.487  14.682  31.661  1.00 47.33 ? 649 HOH   A O   1 
HETATM 4949 O  O   . HOH   E 4 .   ? 7.882   17.167  10.081  1.00 16.41 ? 650 HOH   A O   1 
HETATM 4950 O  O   . HOH   E 4 .   ? -3.645  4.865   8.018   1.00 15.02 ? 651 HOH   A O   1 
HETATM 4951 O  O   . HOH   E 4 .   ? 4.881   13.569  2.844   1.00 27.54 ? 652 HOH   A O   1 
HETATM 4952 O  O   . HOH   E 4 .   ? -7.336  -8.393  -9.671  1.00 25.06 ? 653 HOH   A O   1 
HETATM 4953 O  O   . HOH   E 4 .   ? 17.779  9.553   6.673   1.00 26.03 ? 654 HOH   A O   1 
HETATM 4954 O  O   . HOH   E 4 .   ? -5.642  11.383  -7.762  1.00 29.08 ? 655 HOH   A O   1 
HETATM 4955 O  O   . HOH   E 4 .   ? 6.868   19.927  28.756  1.00 40.59 ? 656 HOH   A O   1 
HETATM 4956 O  O   . HOH   E 4 .   ? 3.754   8.134   46.010  1.00 38.59 ? 657 HOH   A O   1 
HETATM 4957 O  O   . HOH   E 4 .   ? 11.346  13.711  23.932  1.00 44.49 ? 658 HOH   A O   1 
HETATM 4958 O  O   . HOH   E 4 .   ? 0.849   -2.030  34.090  1.00 26.86 ? 659 HOH   A O   1 
HETATM 4959 O  O   . HOH   E 4 .   ? 6.651   -0.860  41.438  1.00 29.69 ? 660 HOH   A O   1 
HETATM 4960 O  O   . HOH   E 4 .   ? -11.589 3.394   0.543   1.00 34.36 ? 661 HOH   A O   1 
HETATM 4961 O  O   . HOH   E 4 .   ? 32.170  9.491   32.047  1.00 50.50 ? 662 HOH   A O   1 
HETATM 4962 O  O   . HOH   E 4 .   ? 12.416  -8.734  19.393  1.00 35.12 ? 663 HOH   A O   1 
HETATM 4963 O  O   . HOH   E 4 .   ? 11.062  -5.845  26.197  1.00 21.42 ? 664 HOH   A O   1 
HETATM 4964 O  O   . HOH   E 4 .   ? -5.505  3.228   6.965   1.00 33.32 ? 665 HOH   A O   1 
HETATM 4965 O  O   . HOH   E 4 .   ? 19.839  -3.903  19.905  1.00 21.96 ? 666 HOH   A O   1 
HETATM 4966 O  O   . HOH   E 4 .   ? 3.713   4.555   44.152  1.00 27.90 ? 667 HOH   A O   1 
HETATM 4967 O  O   . HOH   E 4 .   ? -4.120  -6.854  -17.257 1.00 30.27 ? 668 HOH   A O   1 
HETATM 4968 O  O   . HOH   E 4 .   ? 20.147  0.101   -6.096  1.00 44.27 ? 669 HOH   A O   1 
HETATM 4969 O  O   . HOH   E 4 .   ? -6.702  -6.303  -14.253 1.00 30.86 ? 670 HOH   A O   1 
HETATM 4970 O  O   . HOH   E 4 .   ? 8.182   16.357  -6.530  1.00 41.32 ? 671 HOH   A O   1 
HETATM 4971 O  O   . HOH   E 4 .   ? 3.189   -5.960  -18.829 1.00 42.47 ? 672 HOH   A O   1 
HETATM 4972 O  O   . HOH   E 4 .   ? 26.193  10.344  40.116  1.00 42.43 ? 673 HOH   A O   1 
HETATM 4973 O  O   . HOH   E 4 .   ? 16.809  -16.216 2.256   1.00 34.94 ? 674 HOH   A O   1 
HETATM 4974 O  O   . HOH   E 4 .   ? 4.482   11.278  22.570  1.00 41.02 ? 675 HOH   A O   1 
HETATM 4975 O  O   . HOH   E 4 .   ? 28.040  8.284   21.254  1.00 49.13 ? 676 HOH   A O   1 
HETATM 4976 O  O   . HOH   E 4 .   ? -5.006  -5.504  -21.608 1.00 47.25 ? 677 HOH   A O   1 
HETATM 4977 O  O   . HOH   E 4 .   ? 19.978  1.794   48.241  1.00 43.17 ? 678 HOH   A O   1 
HETATM 4978 O  O   . HOH   E 4 .   ? 7.347   -4.336  41.982  1.00 34.79 ? 679 HOH   A O   1 
HETATM 4979 O  O   . HOH   E 4 .   ? -2.607  -11.447 0.793   1.00 34.56 ? 680 HOH   A O   1 
HETATM 4980 O  O   . HOH   E 4 .   ? -7.334  -8.368  3.552   1.00 27.40 ? 681 HOH   A O   1 
HETATM 4981 O  O   . HOH   E 4 .   ? 15.246  16.855  7.000   1.00 36.08 ? 682 HOH   A O   1 
HETATM 4982 O  O   . HOH   E 4 .   ? 5.726   17.791  -11.466 1.00 33.02 ? 683 HOH   A O   1 
HETATM 4983 O  O   . HOH   E 4 .   ? 25.498  -0.032  4.545   1.00 28.50 ? 684 HOH   A O   1 
HETATM 4984 O  O   . HOH   E 4 .   ? 25.828  1.050   17.760  1.00 29.28 ? 685 HOH   A O   1 
HETATM 4985 O  O   . HOH   E 4 .   ? -0.337  -6.175  11.192  1.00 30.44 ? 686 HOH   A O   1 
HETATM 4986 O  O   . HOH   E 4 .   ? 13.894  4.576   -6.909  1.00 43.48 ? 687 HOH   A O   1 
HETATM 4987 O  O   . HOH   E 4 .   ? 7.431   0.659   25.825  1.00 29.72 ? 688 HOH   A O   1 
HETATM 4988 O  O   . HOH   E 4 .   ? -5.608  -10.488 -6.507  1.00 39.07 ? 689 HOH   A O   1 
HETATM 4989 O  O   . HOH   E 4 .   ? 7.103   -15.533 16.473  1.00 37.50 ? 690 HOH   A O   1 
HETATM 4990 O  O   . HOH   E 4 .   ? 6.381   -3.075  27.500  1.00 32.39 ? 691 HOH   A O   1 
HETATM 4991 O  O   . HOH   E 4 .   ? 12.586  8.057   -5.542  1.00 38.84 ? 692 HOH   A O   1 
HETATM 4992 O  O   . HOH   E 4 .   ? 24.548  -5.718  0.012   1.00 38.64 ? 693 HOH   A O   1 
HETATM 4993 O  O   . HOH   E 4 .   ? 9.612   -11.758 16.495  1.00 35.95 ? 694 HOH   A O   1 
HETATM 4994 O  O   . HOH   E 4 .   ? 21.162  -13.688 1.222   1.00 43.96 ? 695 HOH   A O   1 
HETATM 4995 O  O   . HOH   E 4 .   ? -9.716  -1.392  -8.346  1.00 40.31 ? 696 HOH   A O   1 
HETATM 4996 O  O   . HOH   E 4 .   ? -9.239  -6.555  -9.592  1.00 42.82 ? 697 HOH   A O   1 
HETATM 4997 O  O   . HOH   E 4 .   ? 2.203   3.716   42.180  1.00 35.74 ? 698 HOH   A O   1 
HETATM 4998 O  O   . HOH   E 4 .   ? 24.506  -13.969 31.798  1.00 40.49 ? 699 HOH   A O   1 
HETATM 4999 O  O   . HOH   E 4 .   ? -4.758  -17.863 -2.416  1.00 50.73 ? 700 HOH   A O   1 
HETATM 5000 O  O   . HOH   E 4 .   ? 13.706  -19.126 6.013   1.00 35.18 ? 701 HOH   A O   1 
HETATM 5001 O  O   . HOH   E 4 .   ? -4.126  6.670   10.236  1.00 27.84 ? 702 HOH   A O   1 
HETATM 5002 O  O   . HOH   E 4 .   ? 31.692  1.987   26.149  1.00 33.51 ? 703 HOH   A O   1 
HETATM 5003 O  O   . HOH   E 4 .   ? 7.109   16.430  2.717   1.00 40.09 ? 704 HOH   A O   1 
HETATM 5004 O  O   . HOH   E 4 .   ? 2.468   1.080   28.952  1.00 34.77 ? 705 HOH   A O   1 
HETATM 5005 O  O   . HOH   E 4 .   ? -4.568  -0.730  13.301  1.00 32.44 ? 706 HOH   A O   1 
HETATM 5006 O  O   . HOH   E 4 .   ? 17.714  -4.129  46.294  1.00 42.95 ? 707 HOH   A O   1 
HETATM 5007 O  O   . HOH   E 4 .   ? 2.291   -19.873 -2.633  1.00 38.41 ? 708 HOH   A O   1 
HETATM 5008 O  O   . HOH   E 4 .   ? -4.520  2.724   12.440  1.00 48.23 ? 709 HOH   A O   1 
HETATM 5009 O  O   . HOH   E 4 .   ? 21.300  5.661   4.525   1.00 29.12 ? 710 HOH   A O   1 
HETATM 5010 O  O   . HOH   E 4 .   ? 5.640   -7.517  18.792  1.00 39.53 ? 711 HOH   A O   1 
HETATM 5011 O  O   . HOH   E 4 .   ? 6.979   3.052   27.081  1.00 27.05 ? 712 HOH   A O   1 
HETATM 5012 O  O   . HOH   E 4 .   ? 26.147  -6.423  37.481  1.00 30.01 ? 713 HOH   A O   1 
HETATM 5013 O  O   . HOH   E 4 .   ? 12.415  -4.385  -18.476 1.00 48.74 ? 714 HOH   A O   1 
HETATM 5014 O  O   . HOH   E 4 .   ? 7.172   -8.701  16.887  1.00 28.76 ? 715 HOH   A O   1 
HETATM 5015 O  O   . HOH   E 4 .   ? 12.990  10.171  -7.974  1.00 40.85 ? 716 HOH   A O   1 
HETATM 5016 O  O   . HOH   E 4 .   ? 12.733  2.381   -12.720 1.00 51.53 ? 717 HOH   A O   1 
HETATM 5017 O  O   . HOH   E 4 .   ? 17.858  -15.487 10.969  1.00 30.59 ? 718 HOH   A O   1 
HETATM 5018 O  O   . HOH   E 4 .   ? 17.814  12.583  2.120   1.00 26.14 ? 719 HOH   A O   1 
HETATM 5019 O  O   . HOH   E 4 .   ? -3.044  18.398  -6.079  1.00 41.32 ? 720 HOH   A O   1 
HETATM 5020 O  O   . HOH   E 4 .   ? 5.916   20.568  8.422   1.00 27.30 ? 721 HOH   A O   1 
HETATM 5021 O  O   . HOH   E 4 .   ? 1.864   -20.688 -6.641  1.00 34.13 ? 722 HOH   A O   1 
HETATM 5022 O  O   . HOH   E 4 .   ? 14.022  16.519  14.950  1.00 50.03 ? 723 HOH   A O   1 
HETATM 5023 O  O   . HOH   E 4 .   ? 4.980   0.343   43.382  1.00 28.49 ? 724 HOH   A O   1 
HETATM 5024 O  O   . HOH   E 4 .   ? 12.102  20.639  32.228  1.00 41.01 ? 725 HOH   A O   1 
HETATM 5025 O  O   . HOH   E 4 .   ? -7.084  20.175  -0.568  1.00 34.33 ? 726 HOH   A O   1 
HETATM 5026 O  O   . HOH   E 4 .   ? 8.496   -8.455  22.479  1.00 49.77 ? 727 HOH   A O   1 
HETATM 5027 O  O   . HOH   E 4 .   ? -2.214  -18.905 -8.862  1.00 42.50 ? 728 HOH   A O   1 
HETATM 5028 O  O   . HOH   E 4 .   ? 7.760   19.868  10.147  1.00 25.16 ? 729 HOH   A O   1 
HETATM 5029 O  O   . HOH   E 4 .   ? 15.576  15.315  29.742  1.00 35.42 ? 730 HOH   A O   1 
HETATM 5030 O  O   . HOH   E 4 .   ? 10.081  21.588  9.422   1.00 40.96 ? 731 HOH   A O   1 
HETATM 5031 O  O   . HOH   E 4 .   ? -3.871  -11.120 -2.246  1.00 40.15 ? 732 HOH   A O   1 
HETATM 5032 O  O   . HOH   E 4 .   ? -2.249  22.291  2.258   1.00 32.75 ? 733 HOH   A O   1 
HETATM 5033 O  O   . HOH   E 4 .   ? 14.806  -15.060 22.472  1.00 49.40 ? 734 HOH   A O   1 
HETATM 5034 O  O   . HOH   E 4 .   ? -5.906  -15.773 -9.472  1.00 40.60 ? 735 HOH   A O   1 
HETATM 5035 O  O   . HOH   E 4 .   ? 8.646   14.160  -0.597  1.00 28.47 ? 736 HOH   A O   1 
HETATM 5036 O  O   . HOH   E 4 .   ? 13.304  -5.155  44.389  1.00 35.59 ? 737 HOH   A O   1 
HETATM 5037 O  O   . HOH   E 4 .   ? 2.862   21.072  14.480  1.00 36.66 ? 738 HOH   A O   1 
HETATM 5038 O  O   . HOH   E 4 .   ? 0.151   5.729   22.498  1.00 37.71 ? 739 HOH   A O   1 
HETATM 5039 O  O   . HOH   E 4 .   ? 8.811   -2.305  42.600  1.00 26.49 ? 740 HOH   A O   1 
HETATM 5040 O  O   . HOH   E 4 .   ? 10.065  -11.500 21.577  1.00 48.02 ? 741 HOH   A O   1 
HETATM 5041 O  O   . HOH   E 4 .   ? 0.389   4.884   32.297  1.00 39.22 ? 742 HOH   A O   1 
HETATM 5042 O  O   . HOH   E 4 .   ? 6.909   21.913  6.559   1.00 33.96 ? 743 HOH   A O   1 
HETATM 5043 O  O   . HOH   E 4 .   ? 17.093  -18.022 24.674  1.00 44.53 ? 744 HOH   A O   1 
HETATM 5044 O  O   . HOH   F 4 .   ? 24.255  11.599  14.149  1.00 42.64 ? 501 HOH   B O   1 
HETATM 5045 O  O   . HOH   F 4 .   ? 56.484  20.822  9.935   1.00 37.34 ? 502 HOH   B O   1 
HETATM 5046 O  O   . HOH   F 4 .   ? 20.797  -16.444 9.750   1.00 34.91 ? 503 HOH   B O   1 
HETATM 5047 O  O   . HOH   F 4 .   ? 35.471  -0.560  17.609  1.00 15.73 ? 504 HOH   B O   1 
HETATM 5048 O  O   . HOH   F 4 .   ? 48.384  22.638  22.011  1.00 28.86 ? 505 HOH   B O   1 
HETATM 5049 O  O   . HOH   F 4 .   ? 29.601  -34.321 3.703   1.00 18.54 ? 506 HOH   B O   1 
HETATM 5050 O  O   . HOH   F 4 .   ? 40.990  19.080  23.186  1.00 43.18 ? 507 HOH   B O   1 
HETATM 5051 O  O   . HOH   F 4 .   ? 47.472  12.410  -2.425  1.00 42.79 ? 508 HOH   B O   1 
HETATM 5052 O  O   . HOH   F 4 .   ? 30.894  1.978   15.627  1.00 31.39 ? 509 HOH   B O   1 
HETATM 5053 O  O   . HOH   F 4 .   ? 26.728  -11.137 20.395  1.00 29.70 ? 510 HOH   B O   1 
HETATM 5054 O  O   . HOH   F 4 .   ? 55.866  21.717  13.313  1.00 36.62 ? 511 HOH   B O   1 
HETATM 5055 O  O   . HOH   F 4 .   ? 47.201  -11.565 6.055   1.00 25.27 ? 512 HOH   B O   1 
HETATM 5056 O  O   . HOH   F 4 .   ? 49.512  7.096   17.651  1.00 30.01 ? 513 HOH   B O   1 
HETATM 5057 O  O   . HOH   F 4 .   ? 44.365  4.268   10.238  1.00 34.36 ? 514 HOH   B O   1 
HETATM 5058 O  O   . HOH   F 4 .   ? 30.789  2.160   12.692  1.00 33.88 ? 515 HOH   B O   1 
HETATM 5059 O  O   . HOH   F 4 .   ? 36.062  25.774  -2.155  1.00 34.15 ? 516 HOH   B O   1 
HETATM 5060 O  O   . HOH   F 4 .   ? 34.800  21.054  -5.040  1.00 27.27 ? 517 HOH   B O   1 
HETATM 5061 O  O   . HOH   F 4 .   ? 51.341  24.435  9.244   1.00 33.71 ? 518 HOH   B O   1 
HETATM 5062 O  O   . HOH   F 4 .   ? 48.003  6.866   11.715  1.00 31.21 ? 519 HOH   B O   1 
HETATM 5063 O  O   . HOH   F 4 .   ? 39.565  -29.751 21.453  1.00 30.74 ? 520 HOH   B O   1 
HETATM 5064 O  O   . HOH   F 4 .   ? 41.348  11.176  -3.352  1.00 28.56 ? 521 HOH   B O   1 
HETATM 5065 O  O   . HOH   F 4 .   ? 22.819  1.147   14.521  1.00 26.88 ? 522 HOH   B O   1 
HETATM 5066 O  O   . HOH   F 4 .   ? 32.037  30.383  13.496  1.00 43.82 ? 523 HOH   B O   1 
HETATM 5067 O  O   . HOH   F 4 .   ? 48.027  7.633   -1.011  1.00 20.48 ? 524 HOH   B O   1 
HETATM 5068 O  O   . HOH   F 4 .   ? 34.272  -6.443  -1.445  1.00 26.52 ? 525 HOH   B O   1 
HETATM 5069 O  O   . HOH   F 4 .   ? 21.963  7.920   8.272   1.00 31.56 ? 526 HOH   B O   1 
HETATM 5070 O  O   . HOH   F 4 .   ? 32.666  -21.815 27.793  1.00 39.64 ? 527 HOH   B O   1 
HETATM 5071 O  O   . HOH   F 4 .   ? 49.965  14.847  1.701   1.00 31.12 ? 528 HOH   B O   1 
HETATM 5072 O  O   . HOH   F 4 .   ? 46.280  4.784   6.254   1.00 14.37 ? 529 HOH   B O   1 
HETATM 5073 O  O   . HOH   F 4 .   ? 26.973  -36.660 12.509  1.00 31.06 ? 530 HOH   B O   1 
HETATM 5074 O  O   . HOH   F 4 .   ? 39.180  25.118  1.350   1.00 33.59 ? 531 HOH   B O   1 
HETATM 5075 O  O   . HOH   F 4 .   ? 29.958  21.506  24.057  1.00 46.36 ? 532 HOH   B O   1 
HETATM 5076 O  O   . HOH   F 4 .   ? 33.282  -0.742  2.415   1.00 39.28 ? 533 HOH   B O   1 
HETATM 5077 O  O   . HOH   F 4 .   ? 46.930  3.580   19.988  1.00 41.48 ? 534 HOH   B O   1 
HETATM 5078 O  O   . HOH   F 4 .   ? 43.629  -31.537 21.542  1.00 33.05 ? 535 HOH   B O   1 
HETATM 5079 O  O   . HOH   F 4 .   ? 36.604  -37.439 7.807   1.00 33.38 ? 536 HOH   B O   1 
HETATM 5080 O  O   . HOH   F 4 .   ? 48.138  1.559   0.671   1.00 28.48 ? 537 HOH   B O   1 
HETATM 5081 O  O   . HOH   F 4 .   ? 47.532  -33.588 11.418  1.00 20.02 ? 538 HOH   B O   1 
HETATM 5082 O  O   . HOH   F 4 .   ? 31.985  1.577   -4.179  1.00 44.43 ? 539 HOH   B O   1 
HETATM 5083 O  O   . HOH   F 4 .   ? 29.291  12.327  18.564  1.00 37.97 ? 540 HOH   B O   1 
HETATM 5084 O  O   . HOH   F 4 .   ? 50.360  -21.789 12.403  1.00 23.86 ? 541 HOH   B O   1 
HETATM 5085 O  O   . HOH   F 4 .   ? 37.749  13.866  20.580  1.00 36.17 ? 542 HOH   B O   1 
HETATM 5086 O  O   . HOH   F 4 .   ? 40.249  -14.175 26.171  1.00 37.97 ? 543 HOH   B O   1 
HETATM 5087 O  O   . HOH   F 4 .   ? 49.132  -16.570 18.090  1.00 18.29 ? 544 HOH   B O   1 
HETATM 5088 O  O   . HOH   F 4 .   ? 27.247  4.004   6.654   1.00 26.53 ? 545 HOH   B O   1 
HETATM 5089 O  O   . HOH   F 4 .   ? 26.430  -9.555  22.568  1.00 27.60 ? 546 HOH   B O   1 
HETATM 5090 O  O   . HOH   F 4 .   ? 32.061  -0.474  6.501   1.00 16.77 ? 547 HOH   B O   1 
HETATM 5091 O  O   . HOH   F 4 .   ? 21.912  -27.548 7.015   1.00 25.13 ? 548 HOH   B O   1 
HETATM 5092 O  O   . HOH   F 4 .   ? 27.492  23.682  4.547   1.00 15.21 ? 549 HOH   B O   1 
HETATM 5093 O  O   . HOH   F 4 .   ? 32.067  -23.756 -5.171  1.00 27.07 ? 550 HOH   B O   1 
HETATM 5094 O  O   . HOH   F 4 .   ? 35.707  11.294  1.146   1.00 25.77 ? 551 HOH   B O   1 
HETATM 5095 O  O   . HOH   F 4 .   ? 29.914  15.814  17.141  1.00 29.53 ? 552 HOH   B O   1 
HETATM 5096 O  O   . HOH   F 4 .   ? 42.349  14.203  -0.846  1.00 17.89 ? 553 HOH   B O   1 
HETATM 5097 O  O   . HOH   F 4 .   ? 19.040  10.454  9.106   1.00 41.46 ? 554 HOH   B O   1 
HETATM 5098 O  O   . HOH   F 4 .   ? 41.937  11.647  22.001  1.00 35.61 ? 555 HOH   B O   1 
HETATM 5099 O  O   . HOH   F 4 .   ? 36.047  -34.400 18.003  1.00 26.09 ? 556 HOH   B O   1 
HETATM 5100 O  O   . HOH   F 4 .   ? 27.443  2.845   9.209   1.00 25.43 ? 557 HOH   B O   1 
HETATM 5101 O  O   . HOH   F 4 .   ? 23.462  29.614  5.593   1.00 21.55 ? 558 HOH   B O   1 
HETATM 5102 O  O   . HOH   F 4 .   ? 32.713  -34.726 -3.050  1.00 30.45 ? 559 HOH   B O   1 
HETATM 5103 O  O   . HOH   F 4 .   ? 26.424  -19.231 -4.566  1.00 24.84 ? 560 HOH   B O   1 
HETATM 5104 O  O   . HOH   F 4 .   ? 32.778  25.442  -0.224  1.00 18.83 ? 561 HOH   B O   1 
HETATM 5105 O  O   . HOH   F 4 .   ? 26.817  25.797  12.824  1.00 31.59 ? 562 HOH   B O   1 
HETATM 5106 O  O   . HOH   F 4 .   ? 48.793  -5.691  13.833  1.00 27.10 ? 563 HOH   B O   1 
HETATM 5107 O  O   . HOH   F 4 .   ? 36.375  -27.957 25.531  1.00 35.97 ? 564 HOH   B O   1 
HETATM 5108 O  O   . HOH   F 4 .   ? 35.093  -31.173 -1.834  1.00 24.26 ? 565 HOH   B O   1 
HETATM 5109 O  O   . HOH   F 4 .   ? 29.908  -14.670 11.454  1.00 12.20 ? 566 HOH   B O   1 
HETATM 5110 O  O   . HOH   F 4 .   ? 37.451  -21.518 0.191   1.00 10.54 ? 567 HOH   B O   1 
HETATM 5111 O  O   . HOH   F 4 .   ? 27.703  -0.575  6.297   1.00 21.73 ? 568 HOH   B O   1 
HETATM 5112 O  O   . HOH   F 4 .   ? 34.088  2.207   5.306   1.00 28.17 ? 569 HOH   B O   1 
HETATM 5113 O  O   . HOH   F 4 .   ? 47.965  -24.955 28.478  1.00 31.24 ? 570 HOH   B O   1 
HETATM 5114 O  O   . HOH   F 4 .   ? 25.522  -17.132 1.657   1.00 14.52 ? 571 HOH   B O   1 
HETATM 5115 O  O   . HOH   F 4 .   ? 54.167  15.520  18.424  1.00 31.31 ? 572 HOH   B O   1 
HETATM 5116 O  O   . HOH   F 4 .   ? 36.587  -26.334 27.667  1.00 34.91 ? 573 HOH   B O   1 
HETATM 5117 O  O   . HOH   F 4 .   ? 23.118  25.969  8.185   1.00 30.80 ? 574 HOH   B O   1 
HETATM 5118 O  O   . HOH   F 4 .   ? 24.687  -23.985 2.182   1.00 19.20 ? 575 HOH   B O   1 
HETATM 5119 O  O   . HOH   F 4 .   ? 40.948  -1.005  23.203  1.00 32.72 ? 576 HOH   B O   1 
HETATM 5120 O  O   . HOH   F 4 .   ? 49.725  -10.415 23.910  1.00 42.09 ? 577 HOH   B O   1 
HETATM 5121 O  O   . HOH   F 4 .   ? 30.258  -28.896 15.245  1.00 16.20 ? 578 HOH   B O   1 
HETATM 5122 O  O   . HOH   F 4 .   ? 37.736  25.133  14.539  1.00 19.51 ? 579 HOH   B O   1 
HETATM 5123 O  O   . HOH   F 4 .   ? 43.012  -19.606 17.367  1.00 12.15 ? 580 HOH   B O   1 
HETATM 5124 O  O   . HOH   F 4 .   ? 48.997  9.685   18.323  1.00 23.90 ? 581 HOH   B O   1 
HETATM 5125 O  O   . HOH   F 4 .   ? 29.732  -21.439 19.506  1.00 19.90 ? 582 HOH   B O   1 
HETATM 5126 O  O   . HOH   F 4 .   ? 18.077  -13.868 8.544   1.00 16.88 ? 583 HOH   B O   1 
HETATM 5127 O  O   . HOH   F 4 .   ? 46.553  3.485   8.683   1.00 24.82 ? 584 HOH   B O   1 
HETATM 5128 O  O   . HOH   F 4 .   ? 19.459  -16.592 6.253   1.00 39.86 ? 585 HOH   B O   1 
HETATM 5129 O  O   . HOH   F 4 .   ? 34.775  -16.636 26.411  1.00 28.50 ? 586 HOH   B O   1 
HETATM 5130 O  O   . HOH   F 4 .   ? 42.644  -7.913  17.191  1.00 17.43 ? 587 HOH   B O   1 
HETATM 5131 O  O   . HOH   F 4 .   ? 18.438  -23.138 -1.413  1.00 32.36 ? 588 HOH   B O   1 
HETATM 5132 O  O   . HOH   F 4 .   ? 26.737  -16.956 25.135  1.00 37.50 ? 589 HOH   B O   1 
HETATM 5133 O  O   . HOH   F 4 .   ? 35.082  14.165  21.357  1.00 28.19 ? 590 HOH   B O   1 
HETATM 5134 O  O   . HOH   F 4 .   ? 46.234  -17.275 1.899   1.00 28.64 ? 591 HOH   B O   1 
HETATM 5135 O  O   . HOH   F 4 .   ? 31.021  21.287  -4.046  1.00 36.10 ? 592 HOH   B O   1 
HETATM 5136 O  O   . HOH   F 4 .   ? 47.511  -2.979  21.088  1.00 32.71 ? 593 HOH   B O   1 
HETATM 5137 O  O   . HOH   F 4 .   ? 46.349  -4.103  4.607   1.00 20.85 ? 594 HOH   B O   1 
HETATM 5138 O  O   . HOH   F 4 .   ? 55.438  21.708  8.102   1.00 39.47 ? 595 HOH   B O   1 
HETATM 5139 O  O   . HOH   F 4 .   ? 41.575  4.211   8.299   1.00 26.88 ? 596 HOH   B O   1 
HETATM 5140 O  O   . HOH   F 4 .   ? 36.343  5.507   4.119   1.00 30.22 ? 597 HOH   B O   1 
HETATM 5141 O  O   . HOH   F 4 .   ? 25.990  23.628  16.187  1.00 35.58 ? 598 HOH   B O   1 
HETATM 5142 O  O   . HOH   F 4 .   ? 33.518  7.543   18.457  1.00 28.01 ? 599 HOH   B O   1 
HETATM 5143 O  O   . HOH   F 4 .   ? 45.703  6.689   -2.312  1.00 24.73 ? 600 HOH   B O   1 
HETATM 5144 O  O   . HOH   F 4 .   ? 32.832  14.304  -4.381  1.00 22.16 ? 601 HOH   B O   1 
HETATM 5145 O  O   . HOH   F 4 .   ? 25.429  -33.811 12.697  1.00 29.83 ? 602 HOH   B O   1 
HETATM 5146 O  O   . HOH   F 4 .   ? 33.249  -34.106 19.014  1.00 21.43 ? 603 HOH   B O   1 
HETATM 5147 O  O   . HOH   F 4 .   ? 42.887  -5.209  27.777  1.00 41.28 ? 604 HOH   B O   1 
HETATM 5148 O  O   . HOH   F 4 .   ? 49.199  23.829  3.916   1.00 28.30 ? 605 HOH   B O   1 
HETATM 5149 O  O   . HOH   F 4 .   ? 49.706  -13.925 16.951  1.00 23.39 ? 606 HOH   B O   1 
HETATM 5150 O  O   . HOH   F 4 .   ? 24.839  20.763  16.549  1.00 30.52 ? 607 HOH   B O   1 
HETATM 5151 O  O   . HOH   F 4 .   ? 41.540  -1.956  25.973  1.00 36.49 ? 608 HOH   B O   1 
HETATM 5152 O  O   . HOH   F 4 .   ? 39.881  -20.411 25.638  1.00 16.21 ? 609 HOH   B O   1 
HETATM 5153 O  O   . HOH   F 4 .   ? 21.089  7.883   5.592   1.00 32.21 ? 610 HOH   B O   1 
HETATM 5154 O  O   . HOH   F 4 .   ? 32.566  -21.389 25.236  1.00 41.02 ? 611 HOH   B O   1 
HETATM 5155 O  O   . HOH   F 4 .   ? 33.512  9.306   12.624  1.00 9.19  ? 612 HOH   B O   1 
HETATM 5156 O  O   . HOH   F 4 .   ? 19.891  -28.496 10.280  1.00 29.09 ? 613 HOH   B O   1 
HETATM 5157 O  O   . HOH   F 4 .   ? 32.570  -17.532 -5.044  1.00 32.14 ? 614 HOH   B O   1 
HETATM 5158 O  O   . HOH   F 4 .   ? 39.890  1.165   22.884  1.00 34.51 ? 615 HOH   B O   1 
HETATM 5159 O  O   . HOH   F 4 .   ? 43.122  -18.502 4.481   1.00 18.42 ? 616 HOH   B O   1 
HETATM 5160 O  O   . HOH   F 4 .   ? 23.996  -10.063 2.149   1.00 13.55 ? 617 HOH   B O   1 
HETATM 5161 O  O   . HOH   F 4 .   ? 49.056  -13.783 14.322  1.00 19.26 ? 618 HOH   B O   1 
HETATM 5162 O  O   . HOH   F 4 .   ? 40.330  27.537  6.020   1.00 26.21 ? 619 HOH   B O   1 
HETATM 5163 O  O   . HOH   F 4 .   ? 25.806  6.319   -2.189  1.00 30.65 ? 620 HOH   B O   1 
HETATM 5164 O  O   . HOH   F 4 .   ? 32.531  -33.434 10.215  1.00 11.47 ? 621 HOH   B O   1 
HETATM 5165 O  O   . HOH   F 4 .   ? 41.254  -11.541 5.530   1.00 17.50 ? 622 HOH   B O   1 
HETATM 5166 O  O   . HOH   F 4 .   ? 31.934  -22.306 22.609  1.00 25.07 ? 623 HOH   B O   1 
HETATM 5167 O  O   . HOH   F 4 .   ? 41.858  -22.173 1.273   1.00 34.26 ? 624 HOH   B O   1 
HETATM 5168 O  O   . HOH   F 4 .   ? 25.472  -1.267  13.887  1.00 22.68 ? 625 HOH   B O   1 
HETATM 5169 O  O   . HOH   F 4 .   ? 46.344  25.900  11.574  1.00 41.17 ? 626 HOH   B O   1 
HETATM 5170 O  O   . HOH   F 4 .   ? 38.534  -29.878 26.468  1.00 34.15 ? 627 HOH   B O   1 
HETATM 5171 O  O   . HOH   F 4 .   ? 45.007  -33.035 5.409   1.00 24.16 ? 628 HOH   B O   1 
HETATM 5172 O  O   . HOH   F 4 .   ? 49.112  -27.503 8.645   1.00 24.67 ? 629 HOH   B O   1 
HETATM 5173 O  O   . HOH   F 4 .   ? 30.352  10.003  19.528  1.00 42.89 ? 630 HOH   B O   1 
HETATM 5174 O  O   . HOH   F 4 .   ? 49.594  -27.899 24.020  1.00 34.53 ? 631 HOH   B O   1 
HETATM 5175 O  O   . HOH   F 4 .   ? 29.023  29.698  7.315   1.00 35.89 ? 632 HOH   B O   1 
HETATM 5176 O  O   . HOH   F 4 .   ? 39.515  32.370  11.318  1.00 45.27 ? 633 HOH   B O   1 
HETATM 5177 O  O   . HOH   F 4 .   ? 43.080  -1.102  3.568   1.00 29.71 ? 634 HOH   B O   1 
HETATM 5178 O  O   . HOH   F 4 .   ? 36.824  7.627   0.120   1.00 27.93 ? 635 HOH   B O   1 
HETATM 5179 O  O   . HOH   F 4 .   ? 38.978  5.159   7.986   1.00 15.09 ? 636 HOH   B O   1 
HETATM 5180 O  O   . HOH   F 4 .   ? 49.721  -27.144 26.612  1.00 42.16 ? 637 HOH   B O   1 
HETATM 5181 O  O   . HOH   F 4 .   ? 36.344  -5.793  4.513   1.00 16.86 ? 638 HOH   B O   1 
HETATM 5182 O  O   . HOH   F 4 .   ? 33.807  -4.104  23.471  1.00 27.97 ? 639 HOH   B O   1 
HETATM 5183 O  O   . HOH   F 4 .   ? 29.104  -17.154 -6.097  1.00 44.63 ? 640 HOH   B O   1 
HETATM 5184 O  O   . HOH   F 4 .   ? 51.069  19.099  3.785   1.00 17.34 ? 641 HOH   B O   1 
HETATM 5185 O  O   . HOH   F 4 .   ? 39.180  16.538  -3.484  1.00 35.51 ? 642 HOH   B O   1 
HETATM 5186 O  O   . HOH   F 4 .   ? 27.927  -13.094 -4.405  1.00 19.29 ? 643 HOH   B O   1 
HETATM 5187 O  O   . HOH   F 4 .   ? 41.109  -13.393 -1.363  1.00 26.93 ? 644 HOH   B O   1 
HETATM 5188 O  O   . HOH   F 4 .   ? 43.208  -27.601 4.408   1.00 26.63 ? 645 HOH   B O   1 
HETATM 5189 O  O   . HOH   F 4 .   ? 51.459  4.915   24.476  1.00 50.13 ? 646 HOH   B O   1 
HETATM 5190 O  O   . HOH   F 4 .   ? 26.690  26.554  10.681  1.00 29.97 ? 647 HOH   B O   1 
HETATM 5191 O  O   . HOH   F 4 .   ? 47.119  -24.394 4.161   1.00 41.12 ? 648 HOH   B O   1 
HETATM 5192 O  O   . HOH   F 4 .   ? 48.435  -4.902  11.015  1.00 33.84 ? 649 HOH   B O   1 
HETATM 5193 O  O   . HOH   F 4 .   ? 50.165  -10.267 13.116  1.00 45.30 ? 650 HOH   B O   1 
HETATM 5194 O  O   . HOH   F 4 .   ? 22.000  19.618  3.819   1.00 27.76 ? 651 HOH   B O   1 
HETATM 5195 O  O   . HOH   F 4 .   ? 23.358  14.037  5.330   1.00 38.04 ? 652 HOH   B O   1 
HETATM 5196 O  O   . HOH   F 4 .   ? 40.234  28.395  3.686   1.00 37.26 ? 653 HOH   B O   1 
HETATM 5197 O  O   . HOH   F 4 .   ? 44.420  25.968  13.056  1.00 29.35 ? 654 HOH   B O   1 
HETATM 5198 O  O   . HOH   F 4 .   ? 25.432  -23.891 11.324  1.00 23.45 ? 655 HOH   B O   1 
HETATM 5199 O  O   . HOH   F 4 .   ? 52.092  -23.123 19.128  1.00 27.52 ? 656 HOH   B O   1 
HETATM 5200 O  O   . HOH   F 4 .   ? 44.372  -6.852  2.070   1.00 16.35 ? 657 HOH   B O   1 
HETATM 5201 O  O   . HOH   F 4 .   ? 24.313  -8.410  -0.009  1.00 25.72 ? 658 HOH   B O   1 
HETATM 5202 O  O   . HOH   F 4 .   ? 49.588  10.089  20.982  1.00 37.63 ? 659 HOH   B O   1 
HETATM 5203 O  O   . HOH   F 4 .   ? 30.251  -2.232  7.425   1.00 23.72 ? 660 HOH   B O   1 
HETATM 5204 O  O   . HOH   F 4 .   ? 50.208  -17.109 4.754   1.00 31.80 ? 661 HOH   B O   1 
HETATM 5205 O  O   . HOH   F 4 .   ? 29.129  -22.710 22.053  1.00 39.87 ? 662 HOH   B O   1 
HETATM 5206 O  O   . HOH   F 4 .   ? 29.511  -14.201 27.881  1.00 27.25 ? 663 HOH   B O   1 
HETATM 5207 O  O   . HOH   F 4 .   ? 38.460  19.206  22.151  1.00 48.14 ? 664 HOH   B O   1 
HETATM 5208 O  O   . HOH   F 4 .   ? 22.046  -35.192 10.924  1.00 38.94 ? 665 HOH   B O   1 
HETATM 5209 O  O   . HOH   F 4 .   ? 42.080  18.858  -0.329  1.00 15.77 ? 666 HOH   B O   1 
HETATM 5210 O  O   . HOH   F 4 .   ? 36.352  0.660   6.098   1.00 41.30 ? 667 HOH   B O   1 
HETATM 5211 O  O   . HOH   F 4 .   ? 53.455  18.196  5.379   1.00 18.96 ? 668 HOH   B O   1 
HETATM 5212 O  O   . HOH   F 4 .   ? 43.744  8.836   11.241  1.00 13.40 ? 669 HOH   B O   1 
HETATM 5213 O  O   . HOH   F 4 .   ? 42.353  -3.502  2.793   1.00 37.30 ? 670 HOH   B O   1 
HETATM 5214 O  O   . HOH   F 4 .   ? 40.105  -2.624  2.895   1.00 33.33 ? 671 HOH   B O   1 
HETATM 5215 O  O   . HOH   F 4 .   ? 43.303  -11.591 27.305  1.00 28.29 ? 672 HOH   B O   1 
HETATM 5216 O  O   . HOH   F 4 .   ? 44.622  -10.337 2.041   1.00 42.82 ? 673 HOH   B O   1 
HETATM 5217 O  O   . HOH   F 4 .   ? 22.234  -18.053 17.825  1.00 34.13 ? 674 HOH   B O   1 
HETATM 5218 O  O   . HOH   F 4 .   ? 44.401  19.939  1.402   1.00 14.69 ? 675 HOH   B O   1 
HETATM 5219 O  O   . HOH   F 4 .   ? 49.823  -18.883 20.562  1.00 37.35 ? 676 HOH   B O   1 
HETATM 5220 O  O   . HOH   F 4 .   ? 21.724  -21.660 -3.893  1.00 35.87 ? 677 HOH   B O   1 
HETATM 5221 O  O   . HOH   F 4 .   ? 34.354  -35.456 9.318   1.00 26.72 ? 678 HOH   B O   1 
HETATM 5222 O  O   . HOH   F 4 .   ? 37.763  -31.167 24.079  1.00 33.35 ? 679 HOH   B O   1 
HETATM 5223 O  O   . HOH   F 4 .   ? 34.989  -15.442 -5.299  1.00 26.86 ? 680 HOH   B O   1 
HETATM 5224 O  O   . HOH   F 4 .   ? 24.237  -35.315 9.550   1.00 29.67 ? 681 HOH   B O   1 
HETATM 5225 O  O   . HOH   F 4 .   ? 51.468  -21.017 8.778   1.00 31.01 ? 682 HOH   B O   1 
HETATM 5226 O  O   . HOH   F 4 .   ? 40.200  -38.982 6.231   1.00 28.19 ? 683 HOH   B O   1 
HETATM 5227 O  O   . HOH   F 4 .   ? 41.015  -34.248 -1.041  1.00 44.41 ? 684 HOH   B O   1 
HETATM 5228 O  O   . HOH   F 4 .   ? 38.588  21.133  -2.097  1.00 38.51 ? 685 HOH   B O   1 
HETATM 5229 O  O   . HOH   F 4 .   ? 43.592  6.183   -0.485  1.00 26.62 ? 686 HOH   B O   1 
HETATM 5230 O  O   . HOH   F 4 .   ? 22.929  -16.840 1.257   1.00 33.16 ? 687 HOH   B O   1 
HETATM 5231 O  O   . HOH   F 4 .   ? 38.293  12.567  -4.720  1.00 37.14 ? 688 HOH   B O   1 
HETATM 5232 O  O   . HOH   F 4 .   ? 23.302  -2.811  12.687  1.00 31.24 ? 689 HOH   B O   1 
HETATM 5233 O  O   . HOH   F 4 .   ? 42.986  13.075  -2.989  1.00 34.60 ? 690 HOH   B O   1 
HETATM 5234 O  O   . HOH   F 4 .   ? 26.707  -0.751  16.270  1.00 41.77 ? 691 HOH   B O   1 
HETATM 5235 O  O   . HOH   F 4 .   ? 43.917  -37.259 8.227   1.00 10.48 ? 692 HOH   B O   1 
HETATM 5236 O  O   . HOH   F 4 .   ? 34.248  8.975   0.590   1.00 38.82 ? 693 HOH   B O   1 
HETATM 5237 O  O   . HOH   F 4 .   ? 50.434  -14.996 5.821   1.00 33.58 ? 694 HOH   B O   1 
HETATM 5238 O  O   . HOH   F 4 .   ? 51.254  -29.128 12.677  1.00 35.30 ? 695 HOH   B O   1 
HETATM 5239 O  O   . HOH   F 4 .   ? 38.618  19.121  -3.310  1.00 44.23 ? 696 HOH   B O   1 
HETATM 5240 O  O   . HOH   F 4 .   ? 42.689  2.704   26.069  1.00 42.83 ? 697 HOH   B O   1 
HETATM 5241 O  O   . HOH   F 4 .   ? 19.823  -16.842 17.185  1.00 45.62 ? 698 HOH   B O   1 
HETATM 5242 O  O   . HOH   F 4 .   ? 44.363  -35.959 4.651   1.00 33.09 ? 699 HOH   B O   1 
HETATM 5243 O  O   . HOH   F 4 .   ? 24.526  -23.360 5.229   1.00 39.23 ? 700 HOH   B O   1 
HETATM 5244 O  O   . HOH   F 4 .   ? 35.351  -6.060  -4.162  1.00 41.07 ? 701 HOH   B O   1 
HETATM 5245 O  O   . HOH   F 4 .   ? 52.889  -14.743 8.458   1.00 43.23 ? 702 HOH   B O   1 
HETATM 5246 O  O   . HOH   F 4 .   ? 48.204  -21.486 1.653   1.00 45.58 ? 703 HOH   B O   1 
HETATM 5247 O  O   . HOH   F 4 .   ? 25.158  24.096  21.112  1.00 41.84 ? 704 HOH   B O   1 
HETATM 5248 O  O   . HOH   F 4 .   ? 35.985  28.840  13.992  1.00 43.56 ? 705 HOH   B O   1 
HETATM 5249 O  O   . HOH   F 4 .   ? 37.603  -44.976 10.934  1.00 45.79 ? 706 HOH   B O   1 
HETATM 5250 O  O   . HOH   F 4 .   ? 18.206  -14.244 16.009  1.00 46.79 ? 707 HOH   B O   1 
HETATM 5251 O  O   . HOH   F 4 .   ? 17.292  16.000  15.971  1.00 48.22 ? 708 HOH   B O   1 
HETATM 5252 O  O   . HOH   F 4 .   ? 43.910  -11.168 4.498   1.00 26.48 ? 709 HOH   B O   1 
HETATM 5253 O  O   . HOH   F 4 .   ? 43.704  -18.104 2.336   1.00 30.63 ? 710 HOH   B O   1 
HETATM 5254 O  O   . HOH   F 4 .   ? 32.846  9.357   20.571  1.00 37.68 ? 711 HOH   B O   1 
HETATM 5255 O  O   . HOH   F 4 .   ? 31.691  23.400  -3.265  1.00 32.98 ? 712 HOH   B O   1 
HETATM 5256 O  O   . HOH   F 4 .   ? 41.513  16.905  -1.471  1.00 29.36 ? 713 HOH   B O   1 
HETATM 5257 O  O   . HOH   F 4 .   ? 49.278  -29.004 29.280  1.00 36.81 ? 714 HOH   B O   1 
HETATM 5258 O  O   . HOH   F 4 .   ? 18.183  -14.869 13.531  1.00 39.84 ? 715 HOH   B O   1 
HETATM 5259 O  O   . HOH   F 4 .   ? 40.326  6.416   22.530  1.00 37.57 ? 716 HOH   B O   1 
HETATM 5260 O  O   . HOH   F 4 .   ? 20.959  21.613  5.180   1.00 37.59 ? 717 HOH   B O   1 
HETATM 5261 O  O   . HOH   F 4 .   ? 43.416  3.614   5.720   1.00 30.91 ? 718 HOH   B O   1 
HETATM 5262 O  O   . HOH   F 4 .   ? 40.167  -42.471 6.269   1.00 31.71 ? 719 HOH   B O   1 
HETATM 5263 O  O   . HOH   F 4 .   ? 25.416  -35.217 4.402   1.00 32.75 ? 720 HOH   B O   1 
HETATM 5264 O  O   . HOH   F 4 .   ? 37.520  26.204  5.493   1.00 38.48 ? 721 HOH   B O   1 
HETATM 5265 O  O   . HOH   F 4 .   ? 40.977  -17.685 -0.863  1.00 47.89 ? 722 HOH   B O   1 
HETATM 5266 O  O   . HOH   F 4 .   ? 41.185  20.728  -2.081  1.00 40.10 ? 723 HOH   B O   1 
HETATM 5267 O  O   . HOH   F 4 .   ? 41.951  6.885   -2.096  1.00 43.20 ? 724 HOH   B O   1 
HETATM 5268 O  O   . HOH   F 4 .   ? 30.820  25.168  28.420  1.00 50.57 ? 725 HOH   B O   1 
HETATM 5269 O  O   . HOH   F 4 .   ? 46.862  25.381  22.985  1.00 31.92 ? 726 HOH   B O   1 
HETATM 5270 O  O   . HOH   F 4 .   ? 37.248  -4.003  2.656   1.00 33.46 ? 727 HOH   B O   1 
HETATM 5271 O  O   . HOH   F 4 .   ? 22.873  23.353  11.957  1.00 40.93 ? 728 HOH   B O   1 
HETATM 5272 O  O   . HOH   F 4 .   ? 50.488  26.560  6.990   1.00 37.23 ? 729 HOH   B O   1 
HETATM 5273 O  O   . HOH   F 4 .   ? 51.655  13.989  24.688  1.00 47.49 ? 730 HOH   B O   1 
HETATM 5274 O  O   . HOH   F 4 .   ? 46.744  -6.094  2.909   1.00 25.34 ? 731 HOH   B O   1 
HETATM 5275 O  O   . HOH   F 4 .   ? 19.088  18.341  15.520  1.00 51.79 ? 732 HOH   B O   1 
HETATM 5276 O  O   . HOH   F 4 .   ? 53.781  15.639  5.113   1.00 35.82 ? 733 HOH   B O   1 
HETATM 5277 O  O   . HOH   F 4 .   ? 22.840  19.378  11.887  1.00 43.79 ? 734 HOH   B O   1 
HETATM 5278 O  O   . HOH   F 4 .   ? 29.590  26.889  19.131  1.00 40.72 ? 735 HOH   B O   1 
HETATM 5279 O  O   . HOH   F 4 .   ? 34.349  -27.173 29.010  1.00 36.66 ? 736 HOH   B O   1 
HETATM 5280 O  O   . HOH   F 4 .   ? 43.967  6.268   12.339  1.00 29.34 ? 737 HOH   B O   1 
HETATM 5281 O  O   . HOH   F 4 .   ? 22.938  -22.422 7.841   1.00 52.81 ? 738 HOH   B O   1 
HETATM 5282 O  O   . HOH   F 4 .   ? 38.227  3.951   5.625   1.00 16.83 ? 739 HOH   B O   1 
HETATM 5283 O  O   . HOH   F 4 .   ? 54.366  16.308  24.272  1.00 53.59 ? 740 HOH   B O   1 
HETATM 5284 O  O   . HOH   F 4 .   ? 54.641  20.791  17.155  1.00 41.76 ? 741 HOH   B O   1 
HETATM 5285 O  O   . HOH   F 4 .   ? 33.606  -1.884  25.225  1.00 32.13 ? 742 HOH   B O   1 
HETATM 5286 O  O   . HOH   F 4 .   ? 51.020  -4.798  15.580  1.00 41.16 ? 743 HOH   B O   1 
HETATM 5287 O  O   . HOH   F 4 .   ? 36.745  26.565  16.491  1.00 40.26 ? 744 HOH   B O   1 
HETATM 5288 O  O   . HOH   F 4 .   ? 35.911  -33.552 -2.954  1.00 36.87 ? 745 HOH   B O   1 
HETATM 5289 O  O   . HOH   F 4 .   ? 43.686  -4.722  0.762   1.00 42.44 ? 746 HOH   B O   1 
HETATM 5290 O  O   . HOH   F 4 .   ? 39.516  -22.620 -2.116  1.00 44.92 ? 747 HOH   B O   1 
HETATM 5291 O  O   . HOH   F 4 .   ? 27.970  27.810  17.422  1.00 40.98 ? 748 HOH   B O   1 
HETATM 5292 O  O   . HOH   F 4 .   ? 25.540  -14.413 -3.329  1.00 36.99 ? 749 HOH   B O   1 
HETATM 5293 O  O   . HOH   F 4 .   ? 18.823  18.704  6.746   1.00 39.92 ? 750 HOH   B O   1 
HETATM 5294 O  O   . HOH   F 4 .   ? 52.560  -13.972 17.392  1.00 36.52 ? 751 HOH   B O   1 
HETATM 5295 O  O   . HOH   F 4 .   ? 51.189  21.278  2.756   1.00 33.44 ? 752 HOH   B O   1 
HETATM 5296 O  O   . HOH   F 4 .   ? 50.436  26.308  4.633   1.00 42.38 ? 753 HOH   B O   1 
HETATM 5297 O  O   . HOH   F 4 .   ? 45.269  22.374  0.660   1.00 25.54 ? 754 HOH   B O   1 
HETATM 5298 O  O   . HOH   F 4 .   ? 22.952  -16.569 22.150  1.00 44.95 ? 755 HOH   B O   1 
HETATM 5299 O  O   . HOH   F 4 .   ? 22.112  22.944  16.033  1.00 48.76 ? 756 HOH   B O   1 
HETATM 5300 O  O   . HOH   F 4 .   ? 29.719  -1.835  -9.829  1.00 25.27 ? 757 HOH   B O   1 
HETATM 5301 O  O   . HOH   F 4 .   ? 34.014  14.653  -6.972  1.00 40.80 ? 758 HOH   B O   1 
HETATM 5302 O  O   . HOH   F 4 .   ? 40.982  -10.943 -4.801  1.00 37.66 ? 759 HOH   B O   1 
HETATM 5303 O  O   . HOH   F 4 .   ? 33.226  7.873   -2.404  1.00 33.33 ? 760 HOH   B O   1 
HETATM 5304 O  O   . HOH   F 4 .   ? 18.751  21.139  12.218  1.00 54.98 ? 761 HOH   B O   1 
# 
