data_9EZ4
# 
_entry.id   9EZ4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EZ4         pdb_00009ez4 10.2210/pdb9ez4/pdb 
WWPDB D_1292137809 ?            ?                   
# 
_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       2025-02-12 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EZ4 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9EX8 unspecified 
PDB . 9EXU unspecified 
PDB . 9EYA unspecified 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              roberto.battistutta@unipd.it 
_pdbx_contact_author.name_first         Roberto 
_pdbx_contact_author.name_last          Battistutta 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0193-0694 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Battistutta, R.' 1 ? 
'Fornasier, E.'   2 ? 
'Giachin, G.'     3 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Biol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3642 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            7 
_citation.language                  ? 
_citation.page_first                1435 
_citation.page_last                 1435 
_citation.title                     'Allostery in homodimeric SARS-CoV-2 main protease.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42003-024-07138-w 
_citation.pdbx_database_id_PubMed   39496839 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Fornasier, E.'   1  ?                   
primary 'Fabbian, S.'     2  ?                   
primary 'Shehi, H.'       3  ?                   
primary 'Enderle, J.'     4  ?                   
primary 'Gatto, B.'       5  0000-0001-9465-6913 
primary 'Volpin, D.'      6  ?                   
primary 'Biondi, B.'      7  ?                   
primary 'Bellanda, M.'    8  0000-0002-8187-0264 
primary 'Giachin, G.'     9  0000-0001-7550-0307 
primary 'Sosic, A.'       10 ?                   
primary 'Battistutta, R.' 11 0000-0002-0193-0694 
# 
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 'Replicase polyprotein 1a'      33774.410 1   ? ? ? ? 
2 polymer     man 'Non-structural protein 7'      33726.410 1   ? ? ? ? 
3 polymer     syn GLY-VAL-THR-PHE-GLN-SER-ALA-VAL 1181.342  1   ? ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                  62.068    5   ? ? ? ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'         106.120   2   ? ? ? ? 
6 non-polymer syn GLUTAMINE                       146.144   1   ? ? ? ? 
7 water       nat water                           18.015    325 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'ORF1a polyprotein' 
2 nsp7                
# 
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 yes 
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRAVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSAGSVGFNIDYD(OCS)
VSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMK
YNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRAVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSAGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
A ? 
2 'polypeptide(L)' no no  
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRAVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSAGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRAVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSAGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
B ? 
3 'polypeptide(L)' no no  SGVTFQSAVKR SGVTFQSAVKR C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 1,2-ETHANEDIOL          EDO 
5 'DI(HYDROXYETHYL)ETHER' PEG 
6 GLUTAMINE               GLN 
7 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  ALA 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 ALA 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 OCS 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 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN 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  ALA 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 ALA 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 ARG 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 
2 302 GLY n 
2 303 VAL n 
2 304 THR n 
2 305 PHE n 
2 306 GLN n 
3 1   SER n 
3 2   GLY n 
3 3   VAL n 
3 4   THR n 
3 5   PHE n 
3 6   GLN n 
3 7   SER n 
3 8   ALA n 
3 9   VAL n 
3 10  LYS n 
3 11  ARG 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' 1 306 ? ? ORF1ab       ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? 
? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 306 ? ? 'rep, 1a-1b' ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? 
? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_pdbx_entity_src_syn.entity_id              3 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       11 
_pdbx_entity_src_syn.organism_scientific    'Severe acute respiratory syndrome coronavirus 2' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       2697049 
_pdbx_entity_src_syn.details                ? 
# 
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 
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 
EDO non-polymer         . 1,2-ETHANEDIOL          'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
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 
OCS 'L-peptide linking' n 'CYSTEINESULFONIC ACID' ?                 'C3 H7 N O5 S'   169.156 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                 'C4 H10 O3'      106.120 
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  ALA 41  41  41  ALA ALA 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 ALA 145 145 145 ALA ALA 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 OCS 156 156 156 OCS OCS 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 
A 1 302 GLY 302 302 ?   ?   ?   A . n 
A 1 303 VAL 303 303 ?   ?   ?   A . n 
A 1 304 THR 304 304 ?   ?   ?   A . n 
A 1 305 PHE 305 305 ?   ?   ?   A . n 
A 1 306 GLN 306 306 ?   ?   ?   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  ALA 41  41  41  ALA ALA 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  ?   ?   ?   B . n 
B 2 46  SER 46  46  ?   ?   ?   B . n 
B 2 47  GLU 47  47  ?   ?   ?   B . n 
B 2 48  ASP 48  48  ?   ?   ?   B . n 
B 2 49  MET 49  49  ?   ?   ?   B . n 
B 2 50  LEU 50  50  ?   ?   ?   B . n 
B 2 51  ASN 51  51  ?   ?   ?   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 ALA 145 145 145 ALA ALA 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 ARG 279 279 279 ARG ARG 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 
B 2 302 GLY 302 302 302 GLY GLY B . n 
B 2 303 VAL 303 303 303 VAL VAL B . n 
B 2 304 THR 304 304 304 THR THR B . n 
B 2 305 PHE 305 305 305 PHE PHE B . n 
B 2 306 GLN 306 306 306 GLN GLN B . n 
C 3 1   SER 1   1   ?   ?   ?   C . n 
C 3 2   GLY 2   2   2   GLY GLY C . n 
C 3 3   VAL 3   3   3   VAL VAL C . n 
C 3 4   THR 4   4   4   THR THR C . n 
C 3 5   PHE 5   5   5   PHE PHE C . n 
C 3 6   GLN 6   6   6   GLN GLN C . n 
C 3 7   SER 7   7   7   SER SER C . n 
C 3 8   ALA 8   8   8   ALA ALA C . n 
C 3 9   VAL 9   9   9   VAL VAL C . n 
C 3 10  LYS 10  10  ?   ?   ?   C . n 
C 3 11  ARG 11  11  ?   ?   ?   C . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 4 EDO 1   401 1   EDO EDO A . 
E 4 EDO 1   402 2   EDO EDO A . 
F 4 EDO 1   403 3   EDO EDO A . 
G 4 EDO 1   404 5   EDO EDO A . 
H 5 PEG 1   405 6   PEG PEG A . 
I 4 EDO 1   401 4   EDO EDO B . 
J 5 PEG 1   402 8   PEG PEG B . 
K 6 GLN 1   403 6   GLN GLN B . 
L 7 HOH 1   501 303 HOH HOH A . 
L 7 HOH 2   502 324 HOH HOH A . 
L 7 HOH 3   503 305 HOH HOH A . 
L 7 HOH 4   504 312 HOH HOH A . 
L 7 HOH 5   505 244 HOH HOH A . 
L 7 HOH 6   506 89  HOH HOH A . 
L 7 HOH 7   507 280 HOH HOH A . 
L 7 HOH 8   508 189 HOH HOH A . 
L 7 HOH 9   509 355 HOH HOH A . 
L 7 HOH 10  510 267 HOH HOH A . 
L 7 HOH 11  511 276 HOH HOH A . 
L 7 HOH 12  512 166 HOH HOH A . 
L 7 HOH 13  513 214 HOH HOH A . 
L 7 HOH 14  514 349 HOH HOH A . 
L 7 HOH 15  515 152 HOH HOH A . 
L 7 HOH 16  516 124 HOH HOH A . 
L 7 HOH 17  517 240 HOH HOH A . 
L 7 HOH 18  518 118 HOH HOH A . 
L 7 HOH 19  519 62  HOH HOH A . 
L 7 HOH 20  520 40  HOH HOH A . 
L 7 HOH 21  521 141 HOH HOH A . 
L 7 HOH 22  522 90  HOH HOH A . 
L 7 HOH 23  523 29  HOH HOH A . 
L 7 HOH 24  524 107 HOH HOH A . 
L 7 HOH 25  525 100 HOH HOH A . 
L 7 HOH 26  526 354 HOH HOH A . 
L 7 HOH 27  527 18  HOH HOH A . 
L 7 HOH 28  528 119 HOH HOH A . 
L 7 HOH 29  529 61  HOH HOH A . 
L 7 HOH 30  530 182 HOH HOH A . 
L 7 HOH 31  531 85  HOH HOH A . 
L 7 HOH 32  532 143 HOH HOH A . 
L 7 HOH 33  533 300 HOH HOH A . 
L 7 HOH 34  534 179 HOH HOH A . 
L 7 HOH 35  535 25  HOH HOH A . 
L 7 HOH 36  536 116 HOH HOH A . 
L 7 HOH 37  537 121 HOH HOH A . 
L 7 HOH 38  538 57  HOH HOH A . 
L 7 HOH 39  539 37  HOH HOH A . 
L 7 HOH 40  540 35  HOH HOH A . 
L 7 HOH 41  541 45  HOH HOH A . 
L 7 HOH 42  542 270 HOH HOH A . 
L 7 HOH 43  543 36  HOH HOH A . 
L 7 HOH 44  544 265 HOH HOH A . 
L 7 HOH 45  545 7   HOH HOH A . 
L 7 HOH 46  546 176 HOH HOH A . 
L 7 HOH 47  547 114 HOH HOH A . 
L 7 HOH 48  548 75  HOH HOH A . 
L 7 HOH 49  549 115 HOH HOH A . 
L 7 HOH 50  550 150 HOH HOH A . 
L 7 HOH 51  551 339 HOH HOH A . 
L 7 HOH 52  552 69  HOH HOH A . 
L 7 HOH 53  553 32  HOH HOH A . 
L 7 HOH 54  554 284 HOH HOH A . 
L 7 HOH 55  555 274 HOH HOH A . 
L 7 HOH 56  556 78  HOH HOH A . 
L 7 HOH 57  557 325 HOH HOH A . 
L 7 HOH 58  558 242 HOH HOH A . 
L 7 HOH 59  559 261 HOH HOH A . 
L 7 HOH 60  560 51  HOH HOH A . 
L 7 HOH 61  561 228 HOH HOH A . 
L 7 HOH 62  562 206 HOH HOH A . 
L 7 HOH 63  563 194 HOH HOH A . 
L 7 HOH 64  564 148 HOH HOH A . 
L 7 HOH 65  565 22  HOH HOH A . 
L 7 HOH 66  566 288 HOH HOH A . 
L 7 HOH 67  567 105 HOH HOH A . 
L 7 HOH 68  568 87  HOH HOH A . 
L 7 HOH 69  569 257 HOH HOH A . 
L 7 HOH 70  570 127 HOH HOH A . 
L 7 HOH 71  571 193 HOH HOH A . 
L 7 HOH 72  572 4   HOH HOH A . 
L 7 HOH 73  573 165 HOH HOH A . 
L 7 HOH 74  574 125 HOH HOH A . 
L 7 HOH 75  575 260 HOH HOH A . 
L 7 HOH 76  576 1   HOH HOH A . 
L 7 HOH 77  577 233 HOH HOH A . 
L 7 HOH 78  578 76  HOH HOH A . 
L 7 HOH 79  579 73  HOH HOH A . 
L 7 HOH 80  580 223 HOH HOH A . 
L 7 HOH 81  581 15  HOH HOH A . 
L 7 HOH 82  582 50  HOH HOH A . 
L 7 HOH 83  583 33  HOH HOH A . 
L 7 HOH 84  584 77  HOH HOH A . 
L 7 HOH 85  585 84  HOH HOH A . 
L 7 HOH 86  586 64  HOH HOH A . 
L 7 HOH 87  587 328 HOH HOH A . 
L 7 HOH 88  588 59  HOH HOH A . 
L 7 HOH 89  589 52  HOH HOH A . 
L 7 HOH 90  590 234 HOH HOH A . 
L 7 HOH 91  591 86  HOH HOH A . 
L 7 HOH 92  592 147 HOH HOH A . 
L 7 HOH 93  593 13  HOH HOH A . 
L 7 HOH 94  594 97  HOH HOH A . 
L 7 HOH 95  595 135 HOH HOH A . 
L 7 HOH 96  596 8   HOH HOH A . 
L 7 HOH 97  597 3   HOH HOH A . 
L 7 HOH 98  598 268 HOH HOH A . 
L 7 HOH 99  599 53  HOH HOH A . 
L 7 HOH 100 600 27  HOH HOH A . 
L 7 HOH 101 601 184 HOH HOH A . 
L 7 HOH 102 602 44  HOH HOH A . 
L 7 HOH 103 603 229 HOH HOH A . 
L 7 HOH 104 604 298 HOH HOH A . 
L 7 HOH 105 605 34  HOH HOH A . 
L 7 HOH 106 606 106 HOH HOH A . 
L 7 HOH 107 607 161 HOH HOH A . 
L 7 HOH 108 608 195 HOH HOH A . 
L 7 HOH 109 609 151 HOH HOH A . 
L 7 HOH 110 610 153 HOH HOH A . 
L 7 HOH 111 611 198 HOH HOH A . 
L 7 HOH 112 612 92  HOH HOH A . 
L 7 HOH 113 613 264 HOH HOH A . 
L 7 HOH 114 614 128 HOH HOH A . 
L 7 HOH 115 615 16  HOH HOH A . 
L 7 HOH 116 616 99  HOH HOH A . 
L 7 HOH 117 617 146 HOH HOH A . 
L 7 HOH 118 618 21  HOH HOH A . 
L 7 HOH 119 619 6   HOH HOH A . 
L 7 HOH 120 620 72  HOH HOH A . 
L 7 HOH 121 621 177 HOH HOH A . 
L 7 HOH 122 622 209 HOH HOH A . 
L 7 HOH 123 623 111 HOH HOH A . 
L 7 HOH 124 624 259 HOH HOH A . 
L 7 HOH 125 625 74  HOH HOH A . 
L 7 HOH 126 626 277 HOH HOH A . 
L 7 HOH 127 627 319 HOH HOH A . 
L 7 HOH 128 628 23  HOH HOH A . 
L 7 HOH 129 629 253 HOH HOH A . 
L 7 HOH 130 630 14  HOH HOH A . 
L 7 HOH 131 631 197 HOH HOH A . 
L 7 HOH 132 632 167 HOH HOH A . 
L 7 HOH 133 633 341 HOH HOH A . 
L 7 HOH 134 634 138 HOH HOH A . 
L 7 HOH 135 635 155 HOH HOH A . 
L 7 HOH 136 636 129 HOH HOH A . 
L 7 HOH 137 637 256 HOH HOH A . 
L 7 HOH 138 638 201 HOH HOH A . 
L 7 HOH 139 639 181 HOH HOH A . 
L 7 HOH 140 640 213 HOH HOH A . 
L 7 HOH 141 641 248 HOH HOH A . 
L 7 HOH 142 642 24  HOH HOH A . 
L 7 HOH 143 643 180 HOH HOH A . 
L 7 HOH 144 644 202 HOH HOH A . 
L 7 HOH 145 645 291 HOH HOH A . 
L 7 HOH 146 646 131 HOH HOH A . 
L 7 HOH 147 647 251 HOH HOH A . 
L 7 HOH 148 648 39  HOH HOH A . 
L 7 HOH 149 649 227 HOH HOH A . 
L 7 HOH 150 650 172 HOH HOH A . 
L 7 HOH 151 651 323 HOH HOH A . 
L 7 HOH 152 652 343 HOH HOH A . 
L 7 HOH 153 653 145 HOH HOH A . 
L 7 HOH 154 654 226 HOH HOH A . 
L 7 HOH 155 655 19  HOH HOH A . 
L 7 HOH 156 656 142 HOH HOH A . 
L 7 HOH 157 657 293 HOH HOH A . 
L 7 HOH 158 658 130 HOH HOH A . 
L 7 HOH 159 659 245 HOH HOH A . 
L 7 HOH 160 660 283 HOH HOH A . 
L 7 HOH 161 661 49  HOH HOH A . 
L 7 HOH 162 662 98  HOH HOH A . 
L 7 HOH 163 663 133 HOH HOH A . 
L 7 HOH 164 664 269 HOH HOH A . 
L 7 HOH 165 665 306 HOH HOH A . 
L 7 HOH 166 666 241 HOH HOH A . 
L 7 HOH 167 667 304 HOH HOH A . 
L 7 HOH 168 668 320 HOH HOH A . 
L 7 HOH 169 669 322 HOH HOH A . 
L 7 HOH 170 670 340 HOH HOH A . 
L 7 HOH 171 671 200 HOH HOH A . 
L 7 HOH 172 672 342 HOH HOH A . 
L 7 HOH 173 673 83  HOH HOH A . 
L 7 HOH 174 674 136 HOH HOH A . 
L 7 HOH 175 675 327 HOH HOH A . 
L 7 HOH 176 676 326 HOH HOH A . 
L 7 HOH 177 677 225 HOH HOH A . 
L 7 HOH 178 678 243 HOH HOH A . 
L 7 HOH 179 679 236 HOH HOH A . 
L 7 HOH 180 680 157 HOH HOH A . 
L 7 HOH 181 681 218 HOH HOH A . 
L 7 HOH 182 682 252 HOH HOH A . 
L 7 HOH 183 683 275 HOH HOH A . 
L 7 HOH 184 684 175 HOH HOH A . 
L 7 HOH 185 685 292 HOH HOH A . 
L 7 HOH 186 686 230 HOH HOH A . 
L 7 HOH 187 687 350 HOH HOH A . 
L 7 HOH 188 688 247 HOH HOH A . 
L 7 HOH 189 689 81  HOH HOH A . 
L 7 HOH 190 690 192 HOH HOH A . 
L 7 HOH 191 691 187 HOH HOH A . 
L 7 HOH 192 692 296 HOH HOH A . 
L 7 HOH 193 693 302 HOH HOH A . 
L 7 HOH 194 694 321 HOH HOH A . 
L 7 HOH 195 695 297 HOH HOH A . 
L 7 HOH 196 696 224 HOH HOH A . 
L 7 HOH 197 697 278 HOH HOH A . 
L 7 HOH 198 698 344 HOH HOH A . 
L 7 HOH 199 699 287 HOH HOH A . 
L 7 HOH 200 700 239 HOH HOH A . 
L 7 HOH 201 701 279 HOH HOH A . 
L 7 HOH 202 702 159 HOH HOH A . 
L 7 HOH 203 703 271 HOH HOH A . 
L 7 HOH 204 704 199 HOH HOH A . 
L 7 HOH 205 705 281 HOH HOH A . 
L 7 HOH 206 706 108 HOH HOH A . 
L 7 HOH 207 707 162 HOH HOH A . 
L 7 HOH 208 708 286 HOH HOH A . 
L 7 HOH 209 709 237 HOH HOH A . 
M 7 HOH 1   501 55  HOH HOH B . 
M 7 HOH 2   502 68  HOH HOH B . 
M 7 HOH 3   503 185 HOH HOH B . 
M 7 HOH 4   504 140 HOH HOH B . 
M 7 HOH 5   505 301 HOH HOH B . 
M 7 HOH 6   506 110 HOH HOH B . 
M 7 HOH 7   507 46  HOH HOH B . 
M 7 HOH 8   508 42  HOH HOH B . 
M 7 HOH 9   509 134 HOH HOH B . 
M 7 HOH 10  510 30  HOH HOH B . 
M 7 HOH 11  511 117 HOH HOH B . 
M 7 HOH 12  512 235 HOH HOH B . 
M 7 HOH 13  513 71  HOH HOH B . 
M 7 HOH 14  514 183 HOH HOH B . 
M 7 HOH 15  515 56  HOH HOH B . 
M 7 HOH 16  516 20  HOH HOH B . 
M 7 HOH 17  517 70  HOH HOH B . 
M 7 HOH 18  518 232 HOH HOH B . 
M 7 HOH 19  519 12  HOH HOH B . 
M 7 HOH 20  520 93  HOH HOH B . 
M 7 HOH 21  521 158 HOH HOH B . 
M 7 HOH 22  522 2   HOH HOH B . 
M 7 HOH 23  523 65  HOH HOH B . 
M 7 HOH 24  524 212 HOH HOH B . 
M 7 HOH 25  525 139 HOH HOH B . 
M 7 HOH 26  526 112 HOH HOH B . 
M 7 HOH 27  527 26  HOH HOH B . 
M 7 HOH 28  528 109 HOH HOH B . 
M 7 HOH 29  529 80  HOH HOH B . 
M 7 HOH 30  530 94  HOH HOH B . 
M 7 HOH 31  531 9   HOH HOH B . 
M 7 HOH 32  532 263 HOH HOH B . 
M 7 HOH 33  533 221 HOH HOH B . 
M 7 HOH 34  534 5   HOH HOH B . 
M 7 HOH 35  535 60  HOH HOH B . 
M 7 HOH 36  536 47  HOH HOH B . 
M 7 HOH 37  537 308 HOH HOH B . 
M 7 HOH 38  538 96  HOH HOH B . 
M 7 HOH 39  539 17  HOH HOH B . 
M 7 HOH 40  540 63  HOH HOH B . 
M 7 HOH 41  541 82  HOH HOH B . 
M 7 HOH 42  542 58  HOH HOH B . 
M 7 HOH 43  543 66  HOH HOH B . 
M 7 HOH 44  544 43  HOH HOH B . 
M 7 HOH 45  545 132 HOH HOH B . 
M 7 HOH 46  546 38  HOH HOH B . 
M 7 HOH 47  547 173 HOH HOH B . 
M 7 HOH 48  548 41  HOH HOH B . 
M 7 HOH 49  549 168 HOH HOH B . 
M 7 HOH 50  550 203 HOH HOH B . 
M 7 HOH 51  551 113 HOH HOH B . 
M 7 HOH 52  552 205 HOH HOH B . 
M 7 HOH 53  553 285 HOH HOH B . 
M 7 HOH 54  554 207 HOH HOH B . 
M 7 HOH 55  555 211 HOH HOH B . 
M 7 HOH 56  556 79  HOH HOH B . 
M 7 HOH 57  557 208 HOH HOH B . 
M 7 HOH 58  558 10  HOH HOH B . 
M 7 HOH 59  559 210 HOH HOH B . 
M 7 HOH 60  560 216 HOH HOH B . 
M 7 HOH 61  561 120 HOH HOH B . 
M 7 HOH 62  562 336 HOH HOH B . 
M 7 HOH 63  563 103 HOH HOH B . 
M 7 HOH 64  564 154 HOH HOH B . 
M 7 HOH 65  565 95  HOH HOH B . 
M 7 HOH 66  566 54  HOH HOH B . 
M 7 HOH 67  567 282 HOH HOH B . 
M 7 HOH 68  568 28  HOH HOH B . 
M 7 HOH 69  569 220 HOH HOH B . 
M 7 HOH 70  570 67  HOH HOH B . 
M 7 HOH 71  571 101 HOH HOH B . 
M 7 HOH 72  572 156 HOH HOH B . 
M 7 HOH 73  573 190 HOH HOH B . 
M 7 HOH 74  574 337 HOH HOH B . 
M 7 HOH 75  575 186 HOH HOH B . 
M 7 HOH 76  576 345 HOH HOH B . 
M 7 HOH 77  577 346 HOH HOH B . 
M 7 HOH 78  578 11  HOH HOH B . 
M 7 HOH 79  579 123 HOH HOH B . 
M 7 HOH 80  580 31  HOH HOH B . 
M 7 HOH 81  581 262 HOH HOH B . 
M 7 HOH 82  582 318 HOH HOH B . 
M 7 HOH 83  583 217 HOH HOH B . 
M 7 HOH 84  584 311 HOH HOH B . 
M 7 HOH 85  585 160 HOH HOH B . 
M 7 HOH 86  586 170 HOH HOH B . 
M 7 HOH 87  587 163 HOH HOH B . 
M 7 HOH 88  588 169 HOH HOH B . 
M 7 HOH 89  589 334 HOH HOH B . 
M 7 HOH 90  590 178 HOH HOH B . 
M 7 HOH 91  591 314 HOH HOH B . 
M 7 HOH 92  592 219 HOH HOH B . 
M 7 HOH 93  593 290 HOH HOH B . 
M 7 HOH 94  594 347 HOH HOH B . 
M 7 HOH 95  595 102 HOH HOH B . 
M 7 HOH 96  596 294 HOH HOH B . 
M 7 HOH 97  597 222 HOH HOH B . 
M 7 HOH 98  598 273 HOH HOH B . 
M 7 HOH 99  599 149 HOH HOH B . 
M 7 HOH 100 600 164 HOH HOH B . 
M 7 HOH 101 601 258 HOH HOH B . 
M 7 HOH 102 602 196 HOH HOH B . 
M 7 HOH 103 603 348 HOH HOH B . 
M 7 HOH 104 604 266 HOH HOH B . 
M 7 HOH 105 605 272 HOH HOH B . 
M 7 HOH 106 606 238 HOH HOH B . 
M 7 HOH 107 607 295 HOH HOH B . 
M 7 HOH 108 608 299 HOH HOH B . 
M 7 HOH 109 609 289 HOH HOH B . 
M 7 HOH 110 610 333 HOH HOH B . 
M 7 HOH 111 611 335 HOH HOH B . 
N 7 HOH 1   101 351 HOH HOH C . 
N 7 HOH 2   102 352 HOH HOH C . 
N 7 HOH 3   103 204 HOH HOH C . 
N 7 HOH 4   104 338 HOH HOH C . 
N 7 HOH 5   105 353 HOH HOH C . 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     N 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     GLN 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      403 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     OXT 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    K 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    GLN 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     1 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    OXT 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EZ4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     67.754 
_cell.length_a_esd                 ? 
_cell.length_b                     99.036 
_cell.length_b_esd                 ? 
_cell.length_c                     101.986 
_cell.length_c_esd                 ? 
_cell.volume                       684334.743 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9EZ4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EZ4 
_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             2.49 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.62 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M MMT (DL-malic acid, MES, and Tris base in molar ratio 1:2:2), pH 7.0, 25% PEG 1500' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-06-04 
_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   0.8856 
_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                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8856 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          32.30 
_reflns.entry_id                                       9EZ4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               49.52 
_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                                     64002 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.081 
_reflns.pdbx_Rpim_I_all                                0.025 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.077 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.077 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.80 
_reflns_shell.d_res_low                                     1.84 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3564 
_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                               1.726 
_reflns_shell.pdbx_Rpim_I_all                               0.603 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.485 
_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                                  1.461 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               40.38 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EZ4 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.80 
_refine.ls_d_res_low                             44.54 
_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                     63916 
_refine.ls_number_reflns_R_free                  3172 
_refine.ls_number_reflns_R_work                  60744 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.44 
_refine.ls_percent_reflns_R_free                 4.96 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1848 
_refine.ls_R_factor_R_free                       0.2146 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1832 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 21.9914 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2395 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        44.54 
_refine_hist.number_atoms_solvent             325 
_refine_hist.number_atoms_total               5057 
_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        4689 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_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' ? 0.0134  ? 4880 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.2946  ? 6622 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0797  ? 744  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0099  ? 860  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.2872 ? 1742 ? f_dihedral_angle_d ? ? 
# 
_refine_ls_restr_ncs.pdbx_ordinal        1 
_refine_ls_restr_ncs.pdbx_refine_id      'X-RAY DIFFRACTION' 
_refine_ls_restr_ncs.dom_id              d_2 
_refine_ls_restr_ncs.pdbx_ens_id         ens_1 
_refine_ls_restr_ncs.rms_dev_position    1.50602989305 
_refine_ls_restr_ncs.weight_position     ? 
_refine_ls_restr_ncs.rms_dev_B_iso       ? 
_refine_ls_restr_ncs.weight_B_iso        ? 
_refine_ls_restr_ncs.pdbx_type           'Torsion NCS' 
_refine_ls_restr_ncs.pdbx_asym_id        A 
_refine_ls_restr_ncs.pdbx_auth_asym_id   A 
_refine_ls_restr_ncs.pdbx_number         ? 
_refine_ls_restr_ncs.pdbx_rms            ? 
_refine_ls_restr_ncs.pdbx_weight         ? 
_refine_ls_restr_ncs.ncs_model_details   ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.80 1.83  . . 125 2453 93.00  . . . . 0.3890 . . . . . . . . . . . 0.3512 
'X-RAY DIFFRACTION' 1.83 1.86  . . 134 2542 97.59  . . . . 0.3262 . . . . . . . . . . . 0.3519 
'X-RAY DIFFRACTION' 1.86 1.89  . . 134 2575 97.38  . . . . 0.2766 . . . . . . . . . . . 0.3156 
'X-RAY DIFFRACTION' 1.89 1.92  . . 125 2598 99.96  . . . . 0.2539 . . . . . . . . . . . 0.2770 
'X-RAY DIFFRACTION' 1.92 1.95  . . 158 2592 99.57  . . . . 0.2167 . . . . . . . . . . . 0.2460 
'X-RAY DIFFRACTION' 1.95 1.99  . . 135 2637 99.96  . . . . 0.2074 . . . . . . . . . . . 0.2615 
'X-RAY DIFFRACTION' 1.99 2.03  . . 132 2616 99.93  . . . . 0.1934 . . . . . . . . . . . 0.2511 
'X-RAY DIFFRACTION' 2.03 2.08  . . 147 2631 100.00 . . . . 0.2005 . . . . . . . . . . . 0.2484 
'X-RAY DIFFRACTION' 2.08 2.12  . . 119 2643 100.00 . . . . 0.1900 . . . . . . . . . . . 0.2152 
'X-RAY DIFFRACTION' 2.12 2.18  . . 115 2665 100.00 . . . . 0.1933 . . . . . . . . . . . 0.2546 
'X-RAY DIFFRACTION' 2.18 2.24  . . 134 2633 99.96  . . . . 0.1968 . . . . . . . . . . . 0.2182 
'X-RAY DIFFRACTION' 2.24 2.30  . . 148 2621 100.00 . . . . 0.1965 . . . . . . . . . . . 0.2359 
'X-RAY DIFFRACTION' 2.30 2.38  . . 132 2639 99.96  . . . . 0.1919 . . . . . . . . . . . 0.2228 
'X-RAY DIFFRACTION' 2.38 2.46  . . 145 2649 99.96  . . . . 0.1755 . . . . . . . . . . . 0.2220 
'X-RAY DIFFRACTION' 2.46 2.56  . . 154 2626 100.00 . . . . 0.1781 . . . . . . . . . . . 0.2234 
'X-RAY DIFFRACTION' 2.56 2.68  . . 132 2666 100.00 . . . . 0.1808 . . . . . . . . . . . 0.2359 
'X-RAY DIFFRACTION' 2.68 2.82  . . 136 2659 100.00 . . . . 0.1873 . . . . . . . . . . . 0.2126 
'X-RAY DIFFRACTION' 2.82 2.99  . . 155 2647 100.00 . . . . 0.1936 . . . . . . . . . . . 0.2146 
'X-RAY DIFFRACTION' 2.99 3.22  . . 110 2710 100.00 . . . . 0.1954 . . . . . . . . . . . 0.2629 
'X-RAY DIFFRACTION' 3.22 3.55  . . 174 2641 100.00 . . . . 0.1741 . . . . . . . . . . . 0.2090 
'X-RAY DIFFRACTION' 3.55 4.06  . . 116 2737 100.00 . . . . 0.1582 . . . . . . . . . . . 0.1814 
'X-RAY DIFFRACTION' 4.06 5.12  . . 162 2706 100.00 . . . . 0.1416 . . . . . . . . . . . 0.1538 
'X-RAY DIFFRACTION' 5.12 44.54 . . 150 2858 99.87  . . . . 0.1923 . . . . . . . . . . . 0.2297 
# 
_struct_ncs_oper.id             1 
_struct_ncs_oper.code           given 
_struct_ncs_oper.matrix[1][1]   -0.227662839422 
_struct_ncs_oper.matrix[1][2]   0.678081298992 
_struct_ncs_oper.matrix[1][3]   0.698838596175 
_struct_ncs_oper.matrix[2][1]   0.692283507561 
_struct_ncs_oper.matrix[2][2]   -0.391991921669 
_struct_ncs_oper.matrix[2][3]   0.60587612472 
_struct_ncs_oper.matrix[3][1]   0.684772353929 
_struct_ncs_oper.matrix[3][2]   0.621729913471 
_struct_ncs_oper.matrix[3][3]   -0.38018250616 
_struct_ncs_oper.vector[1]      -11.9629433853 
_struct_ncs_oper.vector[2]      -12.0787550497 
_struct_ncs_oper.vector[3]      25.1515346535 
_struct_ncs_oper.details        ? 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
ens_1 d_1 
;(chain "A" and (resid 1 through 21 or resid 23 through 44 or resid 52 through 64 or resid 66 through 141 or resid 143 through 155 or resid 157 through 300))
;
ens_1 d_2 
;(chain "B" and (resid 1 through 21 or resid 23 through 64 or resid 66 through 141 or resid 143 through 155 or resid 157 through 300))
;
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
ens_1 d_1 1 A SER 1   . A THR 21  . A SER 1   A THR 21  ? ? 
ens_1 d_1 2 A GLY 23  . A CYS 44  . A GLY 23  A CYS 44  ? ? 
ens_1 d_1 3 A PRO 52  . A HIS 64  . A PRO 52  A HIS 64  ? ? 
ens_1 d_1 4 A PHE 66  . A LEU 141 . A PHE 66  A LEU 141 ? ? 
ens_1 d_1 5 A GLY 143 . A ASP 155 . A GLY 143 A ASP 155 ? ? 
ens_1 d_1 6 A VAL 157 . A CYS 300 . A VAL 157 A CYS 300 ? ? 
ens_1 d_2 1 B SER 1   . B THR 21  . B SER 1   B THR 21  ? ? 
ens_1 d_2 2 B GLY 23  . B HIS 64  . B GLY 23  B HIS 64  ? ? 
ens_1 d_2 3 B PHE 66  . B LEU 141 . B PHE 66  B LEU 141 ? ? 
ens_1 d_2 4 B GLY 143 . B ASP 155 . B GLY 143 B ASP 155 ? ? 
ens_1 d_2 5 B VAL 157 . B CYS 300 . B VAL 157 B CYS 300 ? ? 
# 
_struct_ncs_ens.id        ens_1 
_struct_ncs_ens.details   ? 
# 
_struct_ncs_ens_gen.ens_id     ens_1 
_struct_ncs_ens_gen.dom_id_1   d_2 
_struct_ncs_ens_gen.dom_id_2   d_1 
_struct_ncs_ens_gen.oper_id    1 
# 
_struct.entry_id                     9EZ4 
_struct.title                        'Complex of a mutant of the SARS-CoV-2 main protease Mpro with the nsp5/6 substrate peptide.' 
_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        9EZ4 
_struct_keywords.text            'SARS-CoV-2, main protease, nsp5, Cys-peptidase, 3CLpro, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 5 ? 
I N N 4 ? 
J N N 5 ? 
K N N 6 ? 
L N N 7 ? 
M N N 7 ? 
N N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP A0A8B1KJN1_SARS2 A0A8B1KJN1 ? 1 
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
3264 
2 UNP R1AB_SARS2       P0DTD1     ? 2 
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
3264 
3 PDB 9EZ4             9EZ4       ? 3 ? 1    
# 
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 9EZ4 A 1 ? 306 ? A0A8B1KJN1 3264 ? 3569 ? 1 306 
2 2 9EZ4 B 1 ? 306 ? P0DTD1     3264 ? 3569 ? 1 306 
3 3 9EZ4 C 1 ? 11  ? 9EZ4       1    ? 11   ? 1 11  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9EZ4 ALA A 41  ? UNP A0A8B1KJN1 HIS 3304 conflict 41  1 
1 9EZ4 ALA A 145 ? UNP A0A8B1KJN1 CYS 3408 conflict 145 2 
2 9EZ4 ALA B 41  ? UNP P0DTD1     HIS 3304 conflict 41  3 
2 9EZ4 ALA B 145 ? UNP P0DTD1     CYS 3408 conflict 145 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6030  ? 
1 MORE         2     ? 
1 'SSA (A^2)'  24360 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_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 ALA A 41  ? CYS A 44  ? ALA A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P4  AA4 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P5  AA5 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P6  AA6 THR A 226 ? LYS A 236 ? THR A 226 LYS A 236 1 ? 11 
HELX_P HELX_P7  AA7 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P8  AA8 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P9  AA9 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P10 AB1 THR A 292 ? CYS A 300 ? THR A 292 CYS A 300 1 ? 9  
HELX_P HELX_P11 AB2 SER B 10  ? GLY B 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P12 AB3 ALA B 41  ? CYS B 44  ? ALA B 41  CYS B 44  5 ? 4  
HELX_P HELX_P13 AB4 TYR B 54  ? ILE B 59  ? TYR B 54  ILE B 59  1 ? 6  
HELX_P HELX_P14 AB5 SER B 62  ? HIS B 64  ? SER B 62  HIS B 64  5 ? 3  
HELX_P HELX_P15 AB6 ILE B 200 ? ASN B 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P16 AB7 THR B 226 ? LYS B 236 ? THR B 226 LYS B 236 1 ? 11 
HELX_P HELX_P17 AB8 THR B 243 ? LEU B 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P18 AB9 LEU B 250 ? GLY B 258 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P19 AC1 ALA B 260 ? GLY B 275 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P20 AC2 THR B 292 ? GLY B 302 ? THR B 292 GLY B 302 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A ASP 155 C ? ? ? 1_555 A OCS 156 N ? ? A ASP 155 A OCS 156 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale2 covale both ? A OCS 156 C ? ? ? 1_555 A VAL 157 N ? ? A OCS 156 A VAL 157 1_555 ? ? ? ? ? ? ? 1.319 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 OCS A 156 ? . . . . OCS A 156 ? 1_555 . . . . . . . CYS 1 OCS Oxidation     'Named protein modification' 
2 OCS A 156 ? . . . . OCS A 156 ? 1_555 . . . . . . . CYS 2 OCS Hydroxylation 'Named protein modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 3 ? 
AA3 ? 5 ? 
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 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? 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 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA2 2 VAL A 157 ? GLU A 166 ? VAL A 157 GLU A 166 
AA2 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
AA3 1 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 2 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA3 3 VAL A 148 ? ASN A 151 ? VAL A 148 ASN A 151 
AA3 4 VAL A 157 ? GLU A 166 ? VAL A 157 GLU A 166 
AA3 5 THR C 4   ? PHE C 5   ? THR C 4   PHE C 5   
AA4 1 VAL B 73  ? LEU B 75  ? VAL B 73  LEU B 75  
AA4 2 PHE B 66  ? ALA B 70  ? PHE B 66  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 TYR B 101 ? PHE B 103 ? TYR B 101 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 TYR B 101 ? PHE B 103 ? TYR B 101 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 LEU A 75  ? O LEU A 75  N VAL A 68  ? N VAL A 68  
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 CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O LYS A 88  ? O LYS A 88  N SER A 81  ? N SER A 81  
AA2 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA2 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
AA3 1 2 O SER A 123 ? O SER A 123 N ALA A 116 ? N ALA A 116 
AA3 2 3 N SER A 113 ? N SER A 113 O PHE A 150 ? O PHE A 150 
AA3 3 4 N ASN A 151 ? N ASN A 151 O SER A 158 ? O SER A 158 
AA3 4 5 N GLU A 166 ? N GLU A 166 O THR C 4   ? O THR C 4   
AA4 1 2 O LEU B 75  ? O LEU B 75  N VAL B 68  ? N VAL B 68  
AA4 2 3 O GLN B 69  ? O GLN B 69  N GLN B 19  ? N GLN B 19  
AA4 3 4 N VAL B 18  ? N VAL B 18  O GLY B 29  ? O GLY B 29  
AA4 4 5 N LEU B 32  ? N LEU B 32  O VAL B 35  ? O VAL B 35  
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 102 ? N LYS B 102 O PHE B 159 ? O PHE B 159 
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 VAL B 114 ? N VAL B 114 O TYR B 126 ? O TYR B 126 
AA6 1 2 N LYS B 102 ? N LYS B 102 O PHE B 159 ? O PHE B 159 
AA6 2 3 N MET B 162 ? N MET B 162 O THR B 175 ? O THR B 175 
# 
_pdbx_entry_details.entry_id                   9EZ4 
_pdbx_entry_details.has_ligand_of_interest     N 
_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   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 HD22 A ASN 238 ? ? O A HOH 513 ? ? 1.56 
2 1 HD22 B ASN 180 ? ? O B HOH 502 ? ? 1.57 
# 
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 LYS A 5   ? ? -69.45  99.98   
2  1 ASP A 33  ? ? 52.88   -130.19 
3  1 ASP A 48  ? ? -101.52 78.74   
4  1 ASN A 84  ? ? 53.66   -124.40 
5  1 TYR A 154 ? ? 71.63   -121.59 
6  1 HIS A 164 ? ? -122.90 -55.15  
7  1 PRO A 184 ? ? -87.47  32.03   
8  1 ASP B 33  ? ? 51.67   -135.43 
9  1 ILE B 59  ? ? -83.34  36.27   
10 1 ASN B 84  ? ? 54.49   -127.33 
11 1 TYR B 154 ? ? 62.00   -102.17 
12 1 PRO B 184 ? ? -83.76  46.15   
13 1 GLN C 6   ? ? -109.60 40.23   
14 1 GLN C 6   ? ? -86.71  40.23   
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    OCS 
_pdbx_struct_mod_residue.label_seq_id     156 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     OCS 
_pdbx_struct_mod_residue.auth_seq_id      156 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   CYS 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -2.91167295591 
_pdbx_refine_tls.origin_y         -2.71810716794 
_pdbx_refine_tls.origin_z         16.6681188957 
_pdbx_refine_tls.T[1][1]          0.176257211181 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.00116389444399 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.00485937462423 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.151301998459 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0141351619045 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.220151609063 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.646297574699 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.00557819086716 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.267171100753 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.425218841664 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0202624256705 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.07164889315 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0118315129813 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.057111763923 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0109430626581 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.044330657878 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0364363372786 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0460017682304 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.058021821676 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0834165936564 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0238268428876 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   L 
_pdbx_refine_tls_group.end_label_seq_id    1 
_pdbx_refine_tls_group.end_auth_asym_id    D 
_pdbx_refine_tls_group.end_auth_seq_id     6 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 709 ? 6.59 . 
2 1 O ? B HOH 611 ? 6.19 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 302 ? A GLY 302 
2  1 Y 1 A VAL 303 ? A VAL 303 
3  1 Y 1 A THR 304 ? A THR 304 
4  1 Y 1 A PHE 305 ? A PHE 305 
5  1 Y 1 A GLN 306 ? A GLN 306 
6  1 Y 1 B THR 45  ? B THR 45  
7  1 Y 1 B SER 46  ? B SER 46  
8  1 Y 1 B GLU 47  ? B GLU 47  
9  1 Y 1 B ASP 48  ? B ASP 48  
10 1 Y 1 B MET 49  ? B MET 49  
11 1 Y 1 B LEU 50  ? B LEU 50  
12 1 Y 1 B ASN 51  ? B ASN 51  
13 1 Y 1 C SER 1   ? C SER 1   
14 1 Y 1 C LYS 10  ? C LYS 10  
15 1 Y 1 C ARG 11  ? C ARG 11  
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
OCS N    N N N 260 
OCS CA   C N R 261 
OCS CB   C N N 262 
OCS SG   S N N 263 
OCS C    C N N 264 
OCS O    O N N 265 
OCS OXT  O N N 266 
OCS OD1  O N N 267 
OCS OD2  O N N 268 
OCS OD3  O N N 269 
OCS H    H N N 270 
OCS H2   H N N 271 
OCS HA   H N N 272 
OCS HB2  H N N 273 
OCS HB3  H N N 274 
OCS HXT  H N N 275 
OCS HD2  H N N 276 
PEG C1   C N N 277 
PEG O1   O N N 278 
PEG C2   C N N 279 
PEG O2   O N N 280 
PEG C3   C N N 281 
PEG C4   C N N 282 
PEG O4   O N N 283 
PEG H11  H N N 284 
PEG H12  H N N 285 
PEG HO1  H N N 286 
PEG H21  H N N 287 
PEG H22  H N N 288 
PEG H31  H N N 289 
PEG H32  H N N 290 
PEG H41  H N N 291 
PEG H42  H N N 292 
PEG HO4  H N N 293 
PHE N    N N N 294 
PHE CA   C N S 295 
PHE C    C N N 296 
PHE O    O N N 297 
PHE CB   C N N 298 
PHE CG   C Y N 299 
PHE CD1  C Y N 300 
PHE CD2  C Y N 301 
PHE CE1  C Y N 302 
PHE CE2  C Y N 303 
PHE CZ   C Y N 304 
PHE OXT  O N N 305 
PHE H    H N N 306 
PHE H2   H N N 307 
PHE HA   H N N 308 
PHE HB2  H N N 309 
PHE HB3  H N N 310 
PHE HD1  H N N 311 
PHE HD2  H N N 312 
PHE HE1  H N N 313 
PHE HE2  H N N 314 
PHE HZ   H N N 315 
PHE HXT  H N N 316 
PRO N    N N N 317 
PRO CA   C N S 318 
PRO C    C N N 319 
PRO O    O N N 320 
PRO CB   C N N 321 
PRO CG   C N N 322 
PRO CD   C N N 323 
PRO OXT  O N N 324 
PRO H    H N N 325 
PRO HA   H N N 326 
PRO HB2  H N N 327 
PRO HB3  H N N 328 
PRO HG2  H N N 329 
PRO HG3  H N N 330 
PRO HD2  H N N 331 
PRO HD3  H N N 332 
PRO HXT  H N N 333 
SER N    N N N 334 
SER CA   C N S 335 
SER C    C N N 336 
SER O    O N N 337 
SER CB   C N N 338 
SER OG   O N N 339 
SER OXT  O N N 340 
SER H    H N N 341 
SER H2   H N N 342 
SER HA   H N N 343 
SER HB2  H N N 344 
SER HB3  H N N 345 
SER HG   H N N 346 
SER HXT  H N N 347 
THR N    N N N 348 
THR CA   C N S 349 
THR C    C N N 350 
THR O    O N N 351 
THR CB   C N R 352 
THR OG1  O N N 353 
THR CG2  C N N 354 
THR OXT  O N N 355 
THR H    H N N 356 
THR H2   H N N 357 
THR HA   H N N 358 
THR HB   H N N 359 
THR HG1  H N N 360 
THR HG21 H N N 361 
THR HG22 H N N 362 
THR HG23 H N N 363 
THR HXT  H N N 364 
TRP N    N N N 365 
TRP CA   C N S 366 
TRP C    C N N 367 
TRP O    O N N 368 
TRP CB   C N N 369 
TRP CG   C Y N 370 
TRP CD1  C Y N 371 
TRP CD2  C Y N 372 
TRP NE1  N Y N 373 
TRP CE2  C Y N 374 
TRP CE3  C Y N 375 
TRP CZ2  C Y N 376 
TRP CZ3  C Y N 377 
TRP CH2  C Y N 378 
TRP OXT  O N N 379 
TRP H    H N N 380 
TRP H2   H N N 381 
TRP HA   H N N 382 
TRP HB2  H N N 383 
TRP HB3  H N N 384 
TRP HD1  H N N 385 
TRP HE1  H N N 386 
TRP HE3  H N N 387 
TRP HZ2  H N N 388 
TRP HZ3  H N N 389 
TRP HH2  H N N 390 
TRP HXT  H N N 391 
TYR N    N N N 392 
TYR CA   C N S 393 
TYR C    C N N 394 
TYR O    O N N 395 
TYR CB   C N N 396 
TYR CG   C Y N 397 
TYR CD1  C Y N 398 
TYR CD2  C Y N 399 
TYR CE1  C Y N 400 
TYR CE2  C Y N 401 
TYR CZ   C Y N 402 
TYR OH   O N N 403 
TYR OXT  O N N 404 
TYR H    H N N 405 
TYR H2   H N N 406 
TYR HA   H N N 407 
TYR HB2  H N N 408 
TYR HB3  H N N 409 
TYR HD1  H N N 410 
TYR HD2  H N N 411 
TYR HE1  H N N 412 
TYR HE2  H N N 413 
TYR HH   H N N 414 
TYR HXT  H N N 415 
VAL N    N N N 416 
VAL CA   C N S 417 
VAL C    C N N 418 
VAL O    O N N 419 
VAL CB   C N N 420 
VAL CG1  C N N 421 
VAL CG2  C N N 422 
VAL OXT  O N N 423 
VAL H    H N N 424 
VAL H2   H N N 425 
VAL HA   H N N 426 
VAL HB   H N N 427 
VAL HG11 H N N 428 
VAL HG12 H N N 429 
VAL HG13 H N N 430 
VAL HG21 H N N 431 
VAL HG22 H N N 432 
VAL HG23 H N N 433 
VAL HXT  H N N 434 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
OCS N   CA   sing N N 246 
OCS N   H    sing N N 247 
OCS N   H2   sing N N 248 
OCS CA  CB   sing N N 249 
OCS CA  C    sing N N 250 
OCS CA  HA   sing N N 251 
OCS CB  SG   sing N N 252 
OCS CB  HB2  sing N N 253 
OCS CB  HB3  sing N N 254 
OCS SG  OD1  doub N N 255 
OCS SG  OD2  sing N N 256 
OCS SG  OD3  doub N N 257 
OCS C   O    doub N N 258 
OCS C   OXT  sing N N 259 
OCS OXT HXT  sing N N 260 
OCS OD2 HD2  sing N N 261 
PEG C1  O1   sing N N 262 
PEG C1  C2   sing N N 263 
PEG C1  H11  sing N N 264 
PEG C1  H12  sing N N 265 
PEG O1  HO1  sing N N 266 
PEG C2  O2   sing N N 267 
PEG C2  H21  sing N N 268 
PEG C2  H22  sing N N 269 
PEG O2  C3   sing N N 270 
PEG C3  C4   sing N N 271 
PEG C3  H31  sing N N 272 
PEG C3  H32  sing N N 273 
PEG C4  O4   sing N N 274 
PEG C4  H41  sing N N 275 
PEG C4  H42  sing N N 276 
PEG O4  HO4  sing N N 277 
PHE N   CA   sing N N 278 
PHE N   H    sing N N 279 
PHE N   H2   sing N N 280 
PHE CA  C    sing N N 281 
PHE CA  CB   sing N N 282 
PHE CA  HA   sing N N 283 
PHE C   O    doub N N 284 
PHE C   OXT  sing N N 285 
PHE CB  CG   sing N N 286 
PHE CB  HB2  sing N N 287 
PHE CB  HB3  sing N N 288 
PHE CG  CD1  doub Y N 289 
PHE CG  CD2  sing Y N 290 
PHE CD1 CE1  sing Y N 291 
PHE CD1 HD1  sing N N 292 
PHE CD2 CE2  doub Y N 293 
PHE CD2 HD2  sing N N 294 
PHE CE1 CZ   doub Y N 295 
PHE CE1 HE1  sing N N 296 
PHE CE2 CZ   sing Y N 297 
PHE CE2 HE2  sing N N 298 
PHE CZ  HZ   sing N N 299 
PHE OXT HXT  sing N N 300 
PRO N   CA   sing N N 301 
PRO N   CD   sing N N 302 
PRO N   H    sing N N 303 
PRO CA  C    sing N N 304 
PRO CA  CB   sing N N 305 
PRO CA  HA   sing N N 306 
PRO C   O    doub N N 307 
PRO C   OXT  sing N N 308 
PRO CB  CG   sing N N 309 
PRO CB  HB2  sing N N 310 
PRO CB  HB3  sing N N 311 
PRO CG  CD   sing N N 312 
PRO CG  HG2  sing N N 313 
PRO CG  HG3  sing N N 314 
PRO CD  HD2  sing N N 315 
PRO CD  HD3  sing N N 316 
PRO OXT HXT  sing N N 317 
SER N   CA   sing N N 318 
SER N   H    sing N N 319 
SER N   H2   sing N N 320 
SER CA  C    sing N N 321 
SER CA  CB   sing N N 322 
SER CA  HA   sing N N 323 
SER C   O    doub N N 324 
SER C   OXT  sing N N 325 
SER CB  OG   sing N N 326 
SER CB  HB2  sing N N 327 
SER CB  HB3  sing N N 328 
SER OG  HG   sing N N 329 
SER OXT HXT  sing N N 330 
THR N   CA   sing N N 331 
THR N   H    sing N N 332 
THR N   H2   sing N N 333 
THR CA  C    sing N N 334 
THR CA  CB   sing N N 335 
THR CA  HA   sing N N 336 
THR C   O    doub N N 337 
THR C   OXT  sing N N 338 
THR CB  OG1  sing N N 339 
THR CB  CG2  sing N N 340 
THR CB  HB   sing N N 341 
THR OG1 HG1  sing N N 342 
THR CG2 HG21 sing N N 343 
THR CG2 HG22 sing N N 344 
THR CG2 HG23 sing N N 345 
THR OXT HXT  sing N N 346 
TRP N   CA   sing N N 347 
TRP N   H    sing N N 348 
TRP N   H2   sing N N 349 
TRP CA  C    sing N N 350 
TRP CA  CB   sing N N 351 
TRP CA  HA   sing N N 352 
TRP C   O    doub N N 353 
TRP C   OXT  sing N N 354 
TRP CB  CG   sing N N 355 
TRP CB  HB2  sing N N 356 
TRP CB  HB3  sing N N 357 
TRP CG  CD1  doub Y N 358 
TRP CG  CD2  sing Y N 359 
TRP CD1 NE1  sing Y N 360 
TRP CD1 HD1  sing N N 361 
TRP CD2 CE2  doub Y N 362 
TRP CD2 CE3  sing Y N 363 
TRP NE1 CE2  sing Y N 364 
TRP NE1 HE1  sing N N 365 
TRP CE2 CZ2  sing Y N 366 
TRP CE3 CZ3  doub Y N 367 
TRP CE3 HE3  sing N N 368 
TRP CZ2 CH2  doub Y N 369 
TRP CZ2 HZ2  sing N N 370 
TRP CZ3 CH2  sing Y N 371 
TRP CZ3 HZ3  sing N N 372 
TRP CH2 HH2  sing N N 373 
TRP OXT HXT  sing N N 374 
TYR N   CA   sing N N 375 
TYR N   H    sing N N 376 
TYR N   H2   sing N N 377 
TYR CA  C    sing N N 378 
TYR CA  CB   sing N N 379 
TYR CA  HA   sing N N 380 
TYR C   O    doub N N 381 
TYR C   OXT  sing N N 382 
TYR CB  CG   sing N N 383 
TYR CB  HB2  sing N N 384 
TYR CB  HB3  sing N N 385 
TYR CG  CD1  doub Y N 386 
TYR CG  CD2  sing Y N 387 
TYR CD1 CE1  sing Y N 388 
TYR CD1 HD1  sing N N 389 
TYR CD2 CE2  doub Y N 390 
TYR CD2 HD2  sing N N 391 
TYR CE1 CZ   doub Y N 392 
TYR CE1 HE1  sing N N 393 
TYR CE2 CZ   sing Y N 394 
TYR CE2 HE2  sing N N 395 
TYR CZ  OH   sing N N 396 
TYR OH  HH   sing N N 397 
TYR OXT HXT  sing N N 398 
VAL N   CA   sing N N 399 
VAL N   H    sing N N 400 
VAL N   H2   sing N N 401 
VAL CA  C    sing N N 402 
VAL CA  CB   sing N N 403 
VAL CA  HA   sing N N 404 
VAL C   O    doub N N 405 
VAL C   OXT  sing N N 406 
VAL CB  CG1  sing N N 407 
VAL CB  CG2  sing N N 408 
VAL CB  HB   sing N N 409 
VAL CG1 HG11 sing N N 410 
VAL CG1 HG12 sing N N 411 
VAL CG1 HG13 sing N N 412 
VAL CG2 HG21 sing N N 413 
VAL CG2 HG22 sing N N 414 
VAL CG2 HG23 sing N N 415 
VAL OXT HXT  sing N N 416 
# 
_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   7NIJ 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9EZ4 
_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]   0.014759 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010097 
_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]   0.009805 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   ? 13.24800  -9.97000  12.81700  1.000 41.53341  ? 1   SER A N    1 
ATOM   2    C CA   . SER A 1 1   ? 13.63300  -8.92700  13.75300  1.000 41.43017  ? 1   SER A CA   1 
ATOM   3    C C    . SER A 1 1   ? 12.57600  -7.81400  13.78700  1.000 39.90531  ? 1   SER A C    1 
ATOM   4    O O    . SER A 1 1   ? 11.71200  -7.73300  12.88100  1.000 32.63520  ? 1   SER A O    1 
ATOM   5    C CB   . SER A 1 1   ? 15.02300  -8.39600  13.36000  1.000 50.67301  ? 1   SER A CB   1 
ATOM   6    O OG   . SER A 1 1   ? 15.40100  -7.25100  14.08900  1.000 51.68459  ? 1   SER A OG   1 
ATOM   7    H H1   . SER A 1 1   ? 13.27200  -10.76000 13.22700  1.000 49.84089  ? 1   SER A H1   1 
ATOM   8    H H2   . SER A 1 1   ? 12.42300  -9.81400  12.52200  1.000 49.84089  ? 1   SER A H2   1 
ATOM   9    H H3   . SER A 1 1   ? 13.81300  -9.97500  12.12900  1.000 49.84089  ? 1   SER A H3   1 
ATOM   10   H HA   . SER A 1 1   ? 13.69700  -9.30800  14.64300  1.000 49.71700  ? 1   SER A HA   1 
ATOM   11   H HB2  . SER A 1 1   ? 15.69100  -9.09300  13.45400  1.000 60.80842  ? 1   SER A HB2  1 
ATOM   12   H HB3  . SER A 1 1   ? 14.94800  -8.10900  12.45700  1.000 60.80842  ? 1   SER A HB3  1 
ATOM   13   H HG   . SER A 1 1   ? 16.16300  -6.99400  13.84500  1.000 62.02231  ? 1   SER A HG   1 
ATOM   14   N N    . GLY A 1 2   ? 12.65100  -6.96500  14.81300  1.000 33.91437  ? 2   GLY A N    1 
ATOM   15   C CA   . GLY A 1 2   ? 11.70700  -5.89700  15.04800  1.000 38.65131  ? 2   GLY A CA   1 
ATOM   16   C C    . GLY A 1 2   ? 10.75600  -6.27700  16.15800  1.000 33.84637  ? 2   GLY A C    1 
ATOM   17   O O    . GLY A 1 2   ? 10.63700  -7.43500  16.53900  1.000 35.77757  ? 2   GLY A O    1 
ATOM   18   H H    . GLY A 1 2   ? 13.27200  -6.99900  15.40700  1.000 40.69805  ? 2   GLY A H    1 
ATOM   19   H HA2  . GLY A 1 2   ? 12.17900  -5.08800  15.30000  1.000 46.38237  ? 2   GLY A HA2  1 
ATOM   20   H HA3  . GLY A 1 2   ? 11.19700  -5.72600  14.24200  1.000 46.38237  ? 2   GLY A HA3  1 
ATOM   21   N N    . PHE A 1 3   ? 10.05800  -5.28900  16.69600  1.000 32.69286  ? 3   PHE A N    1 
ATOM   22   C CA   . PHE A 1 3   ? 9.11800   -5.60500  17.76200  1.000 34.17470  ? 3   PHE A CA   1 
ATOM   23   C C    . PHE A 1 3   ? 8.03400   -4.53900  17.74900  1.000 38.37805  ? 3   PHE A C    1 
ATOM   24   O O    . PHE A 1 3   ? 8.32800   -3.35500  17.95200  1.000 38.87648  ? 3   PHE A O    1 
ATOM   25   C CB   . PHE A 1 3   ? 9.83000   -5.68600  19.13800  1.000 34.71727  ? 3   PHE A CB   1 
ATOM   26   C CG   . PHE A 1 3   ? 9.07200   -6.50100  20.14000  1.000 31.86110  ? 3   PHE A CG   1 
ATOM   27   C CD1  . PHE A 1 3   ? 9.07700   -7.88500  20.05200  1.000 34.39090  ? 3   PHE A CD1  1 
ATOM   28   C CD2  . PHE A 1 3   ? 8.29300   -5.87600  21.11200  1.000 34.14416  ? 3   PHE A CD2  1 
ATOM   29   C CE1  . PHE A 1 3   ? 8.35000   -8.66100  20.92800  1.000 37.04061  ? 3   PHE A CE1  1 
ATOM   30   C CE2  . PHE A 1 3   ? 7.56000   -6.64500  22.03400  1.000 35.91531  ? 3   PHE A CE2  1 
ATOM   31   C CZ   . PHE A 1 3   ? 7.57100   -8.05800  21.91800  1.000 37.20555  ? 3   PHE A CZ   1 
ATOM   32   H H    . PHE A 1 3   ? 10.10400  -4.45900  16.47500  1.000 39.23223  ? 3   PHE A H    1 
ATOM   33   H HA   . PHE A 1 3   ? 8.70500   -6.46300  17.58300  1.000 41.01045  ? 3   PHE A HA   1 
ATOM   34   H HB2  . PHE A 1 3   ? 10.70200  -6.09400  19.01900  1.000 41.66153  ? 3   PHE A HB2  1 
ATOM   35   H HB3  . PHE A 1 3   ? 9.92900   -4.79000  19.49500  1.000 41.66153  ? 3   PHE A HB3  1 
ATOM   36   H HD1  . PHE A 1 3   ? 9.57900   -8.29800  19.38700  1.000 41.26988  ? 3   PHE A HD1  1 
ATOM   37   H HD2  . PHE A 1 3   ? 8.28200   -4.94800  21.17000  1.000 40.97380  ? 3   PHE A HD2  1 
ATOM   38   H HE1  . PHE A 1 3   ? 8.37600   -9.58800  20.85800  1.000 44.44953  ? 3   PHE A HE1  1 
ATOM   39   H HE2  . PHE A 1 3   ? 7.04400   -6.23100  22.68700  1.000 43.09917  ? 3   PHE A HE2  1 
ATOM   40   H HZ   . PHE A 1 3   ? 7.09600   -8.58100  22.52300  1.000 44.64746  ? 3   PHE A HZ   1 
ATOM   41   N N    . ARG A 1 4   ? 6.79000   -4.95500  17.47300  1.000 28.50976  ? 4   ARG A N    1 
ATOM   42   C CA   . ARG A 1 4   ? 5.66900   -4.04200  17.33600  1.000 31.69967  ? 4   ARG A CA   1 
ATOM   43   C C    . ARG A 1 4   ? 4.52300   -4.49200  18.22000  1.000 29.99326  ? 4   ARG A C    1 
ATOM   44   O O    . ARG A 1 4   ? 4.37300   -5.68000  18.50300  1.000 28.09790  ? 4   ARG A O    1 
ATOM   45   C CB   . ARG A 1 4   ? 5.16100   -4.01800  15.89600  1.000 35.09319  ? 4   ARG A CB   1 
ATOM   46   C CG   . ARG A 1 4   ? 6.10200   -3.29100  14.91100  1.000 34.15626  ? 4   ARG A CG   1 
ATOM   47   C CD   . ARG A 1 4   ? 5.95500   -1.79300  15.16100  1.000 42.00513  ? 4   ARG A CD   1 
ATOM   48   N NE   . ARG A 1 4   ? 6.49800   -0.98600  14.07100  1.000 45.59334  ? 4   ARG A NE   1 
ATOM   49   C CZ   . ARG A 1 4   ? 6.31900   0.32600   13.95600  1.000 44.32290  ? 4   ARG A CZ   1 
ATOM   50   N NH1  . ARG A 1 4   ? 5.54800   0.99200   14.80600  1.000 50.34595  ? 4   ARG A NH1  1 
ATOM   51   N NH2  . ARG A 1 4   ? 6.94800   0.98900   12.97900  1.000 41.32288  ? 4   ARG A NH2  1 
ATOM   52   H H    . ARG A 1 4   ? 6.57600   -5.78000  17.36000  1.000 34.21252  ? 4   ARG A H    1 
ATOM   53   H HA   . ARG A 1 4   ? 5.93300   -3.14600  17.59500  1.000 38.04040  ? 4   ARG A HA   1 
ATOM   54   H HB2  . ARG A 1 4   ? 5.06200   -4.93200  15.58700  1.000 42.11263  ? 4   ARG A HB2  1 
ATOM   55   H HB3  . ARG A 1 4   ? 4.30000   -3.57200  15.87500  1.000 42.11263  ? 4   ARG A HB3  1 
ATOM   56   H HG2  . ARG A 1 4   ? 7.02200   -3.55100  15.07600  1.000 40.98832  ? 4   ARG A HG2  1 
ATOM   57   H HG3  . ARG A 1 4   ? 5.84300   -3.48600  13.99700  1.000 40.98832  ? 4   ARG A HG3  1 
ATOM   58   H HD2  . ARG A 1 4   ? 5.02100   -1.59000  15.25300  1.000 50.40696  ? 4   ARG A HD2  1 
ATOM   59   H HD3  . ARG A 1 4   ? 6.42900   -1.55800  15.97400  1.000 50.40696  ? 4   ARG A HD3  1 
ATOM   60   H HE   . ARG A 1 4   ? 6.90900   -1.39300  13.43500  1.000 54.71281  ? 4   ARG A HE   1 
ATOM   61   H HH11 . ARG A 1 4   ? 5.14500   0.57600   15.44100  1.000 60.41594  ? 4   ARG A HH11 1 
ATOM   62   H HH12 . ARG A 1 4   ? 5.44500   1.84100   14.71600  1.000 60.41594  ? 4   ARG A HH12 1 
ATOM   63   H HH21 . ARG A 1 4   ? 7.44900   0.56400   12.42400  1.000 49.58825  ? 4   ARG A HH21 1 
ATOM   64   H HH22 . ARG A 1 4   ? 6.83600   1.83700   12.89400  1.000 49.58825  ? 4   ARG A HH22 1 
ATOM   65   N N    . LYS A 1 5   ? 3.65500   -3.53900  18.56300  1.000 34.47305  ? 5   LYS A N    1 
ATOM   66   C CA   . LYS A 1 5   ? 2.38000   -3.88300  19.18800  1.000 35.55698  ? 5   LYS A CA   1 
ATOM   67   C C    . LYS A 1 5   ? 1.55300   -4.57000  18.09500  1.000 30.02014  ? 5   LYS A C    1 
ATOM   68   O O    . LYS A 1 5   ? 1.02200   -3.93000  17.19700  1.000 33.64140  ? 5   LYS A O    1 
ATOM   69   C CB   . LYS A 1 5   ? 1.71100   -2.61600  19.73000  1.000 38.98967  ? 5   LYS A CB   1 
ATOM   70   C CG   . LYS A 1 5   ? 0.95500   -2.75700  21.03900  1.000 43.52669  ? 5   LYS A CG   1 
ATOM   71   C CD   . LYS A 1 5   ? 1.88200   -3.31900  22.10600  1.000 40.79276  ? 5   LYS A CD   1 
ATOM   72   C CE   . LYS A 1 5   ? 1.72800   -2.72600  23.52100  1.000 40.90500  ? 5   LYS A CE   1 
ATOM   73   N NZ   . LYS A 1 5   ? 1.81100   -1.24500  23.64400  1.000 41.68847  ? 5   LYS A NZ   1 
ATOM   74   H H    . LYS A 1 5   ? 3.78000   -2.69600  18.44500  1.000 41.36846  ? 5   LYS A H    1 
ATOM   75   H HA   . LYS A 1 5   ? 2.52600   -4.51300  19.90900  1.000 42.66918  ? 5   LYS A HA   1 
ATOM   76   H HB2  . LYS A 1 5   ? 2.39700   -1.94300  19.86500  1.000 46.78841  ? 5   LYS A HB2  1 
ATOM   77   H HB3  . LYS A 1 5   ? 1.07800   -2.29900  19.06700  1.000 46.78841  ? 5   LYS A HB3  1 
ATOM   78   H HG2  . LYS A 1 5   ? 0.62700   -1.89100  21.32800  1.000 52.23283  ? 5   LYS A HG2  1 
ATOM   79   H HG3  . LYS A 1 5   ? 0.22900   -3.38000  20.91800  1.000 52.23283  ? 5   LYS A HG3  1 
ATOM   80   H HD2  . LYS A 1 5   ? 1.78800   -4.28300  22.15400  1.000 48.95211  ? 5   LYS A HD2  1 
ATOM   81   H HD3  . LYS A 1 5   ? 2.76500   -3.07200  21.81700  1.000 48.95211  ? 5   LYS A HD3  1 
ATOM   82   H HE2  . LYS A 1 5   ? 0.90200   -3.03400  23.89700  1.000 49.08680  ? 5   LYS A HE2  1 
ATOM   83   H HE3  . LYS A 1 5   ? 2.45400   -3.08000  24.05800  1.000 49.08680  ? 5   LYS A HE3  1 
ATOM   84   H HZ1  . LYS A 1 5   ? 1.72200   -1.00500  24.49700  1.000 50.02697  ? 5   LYS A HZ1  1 
ATOM   85   H HZ2  . LYS A 1 5   ? 2.59800   -0.95900  23.34400  1.000 50.02697  ? 5   LYS A HZ2  1 
ATOM   86   H HZ3  . LYS A 1 5   ? 1.16300   -0.86300  23.16700  1.000 50.02697  ? 5   LYS A HZ3  1 
ATOM   87   N N    . MET A 1 6   ? 1.49900   -5.87700  18.10300  1.000 28.72337  ? 6   MET A N    1 
ATOM   88   C CA   . MET A 1 6   ? 0.95500   -6.61600  16.97600  1.000 29.46617  ? 6   MET A CA   1 
ATOM   89   C C    . MET A 1 6   ? -0.38900  -7.20100  17.39100  1.000 26.85472  ? 6   MET A C    1 
ATOM   90   O O    . MET A 1 6   ? -0.46300  -7.98000  18.35700  1.000 29.64958  ? 6   MET A O    1 
ATOM   91   C CB   . MET A 1 6   ? 1.92100   -7.73100  16.56700  1.000 29.20590  ? 6   MET A CB   1 
ATOM   92   C CG   . MET A 1 6   ? 1.45200   -8.55600  15.44300  1.000 36.52588  ? 6   MET A CG   1 
ATOM   93   S SD   . MET A 1 6   ? 2.72700   -9.75500  14.98800  1.000 40.55473  ? 6   MET A SD   1 
ATOM   94   C CE   . MET A 1 6   ? 4.00800   -8.66600  14.44400  1.000 39.23871  ? 6   MET A CE   1 
ATOM   95   H H    . MET A 1 6   ? 1.77100   -6.37200  18.75100  1.000 34.46885  ? 6   MET A H    1 
ATOM   96   H HA   . MET A 1 6   ? 0.83200   -6.02600  16.21700  1.000 35.36020  ? 6   MET A HA   1 
ATOM   97   H HB2  . MET A 1 6   ? 2.76400   -7.32500  16.31600  1.000 35.04788  ? 6   MET A HB2  1 
ATOM   98   H HB3  . MET A 1 6   ? 2.05500   -8.31900  17.32700  1.000 35.04788  ? 6   MET A HB3  1 
ATOM   99   H HG2  . MET A 1 6   ? 0.65400   -9.04200  15.70300  1.000 43.83185  ? 6   MET A HG2  1 
ATOM   100  H HG3  . MET A 1 6   ? 1.27200   -7.99000  14.67600  1.000 43.83185  ? 6   MET A HG3  1 
ATOM   101  H HE1  . MET A 1 6   ? 4.38700   -9.01000  13.62000  1.000 47.08725  ? 6   MET A HE1  1 
ATOM   102  H HE2  . MET A 1 6   ? 3.63000   -7.78700  14.29500  1.000 47.08725  ? 6   MET A HE2  1 
ATOM   103  H HE3  . MET A 1 6   ? 4.69200   -8.61700  15.13000  1.000 47.08725  ? 6   MET A HE3  1 
ATOM   104  N N    . ALA A 1 7   ? -1.42800  -6.84700  16.66200  1.000 22.82882  ? 7   ALA A N    1 
ATOM   105  C CA   . ALA A 1 7   ? -2.75800  -7.38100  16.88200  1.000 23.32038  ? 7   ALA A CA   1 
ATOM   106  C C    . ALA A 1 7   ? -2.97000  -8.64400  16.05000  1.000 24.14174  ? 7   ALA A C    1 
ATOM   107  O O    . ALA A 1 7   ? -2.15000  -8.99900  15.18900  1.000 24.82966  ? 7   ALA A O    1 
ATOM   108  C CB   . ALA A 1 7   ? -3.80900  -6.30700  16.55200  1.000 24.13259  ? 7   ALA A CB   1 
ATOM   109  H H    . ALA A 1 7   ? -1.38800  -6.28200  16.01500  1.000 27.39539  ? 7   ALA A H    1 
ATOM   110  H HA   . ALA A 1 7   ? -2.85400  -7.61800  17.81800  1.000 27.98526  ? 7   ALA A HA   1 
ATOM   111  H HB1  . ALA A 1 7   ? -4.69400  -6.67500  16.70300  1.000 28.95991  ? 7   ALA A HB1  1 
ATOM   112  H HB2  . ALA A 1 7   ? -3.66700  -5.53900  17.12800  1.000 28.95991  ? 7   ALA A HB2  1 
ATOM   113  H HB3  . ALA A 1 7   ? -3.71200  -6.04600  15.62300  1.000 28.95991  ? 7   ALA A HB3  1 
ATOM   114  N N    . PHE A 1 8   ? -4.02000  -9.41900  16.41000  1.000 23.47697  ? 8   PHE A N    1 
ATOM   115  C CA   . PHE A 1 8   ? -4.38600  -10.52200 15.54000  1.000 22.64975  ? 8   PHE A CA   1 
ATOM   116  C C    . PHE A 1 8   ? -5.11400  -10.00900 14.31100  1.000 24.51933  ? 8   PHE A C    1 
ATOM   117  O O    . PHE A 1 8   ? -5.77400  -8.98200  14.39600  1.000 22.84490  ? 8   PHE A O    1 
ATOM   118  C CB   . PHE A 1 8   ? -5.26300  -11.51500 16.30200  1.000 23.82729  ? 8   PHE A CB   1 
ATOM   119  C CG   . PHE A 1 8   ? -4.43800  -12.36700 17.24400  1.000 24.69777  ? 8   PHE A CG   1 
ATOM   120  C CD1  . PHE A 1 8   ? -3.73300  -13.45100 16.73200  1.000 27.81350  ? 8   PHE A CD1  1 
ATOM   121  C CD2  . PHE A 1 8   ? -4.32800  -12.03400 18.58600  1.000 25.19343  ? 8   PHE A CD2  1 
ATOM   122  C CE1  . PHE A 1 8   ? -2.93100  -14.24000 17.56900  1.000 36.69460  ? 8   PHE A CE1  1 
ATOM   123  C CE2  . PHE A 1 8   ? -3.55900  -12.80400 19.44300  1.000 25.78376  ? 8   PHE A CE2  1 
ATOM   124  C CZ   . PHE A 1 8   ? -2.84400  -13.92000 18.92100  1.000 31.73854  ? 8   PHE A CZ   1 
ATOM   125  H H    . PHE A 1 8   ? -4.50200  -9.32300  17.11600  1.000 28.17317  ? 8   PHE A H    1 
ATOM   126  H HA   . PHE A 1 8   ? -3.57600  -10.97800 15.26800  1.000 27.18050  ? 8   PHE A HA   1 
ATOM   127  H HB2  . PHE A 1 8   ? -5.91800  -11.02800 16.82600  1.000 28.59355  ? 8   PHE A HB2  1 
ATOM   128  H HB3  . PHE A 1 8   ? -5.70700  -12.10200 15.67000  1.000 28.59355  ? 8   PHE A HB3  1 
ATOM   129  H HD1  . PHE A 1 8   ? -3.79800  -13.65700 15.82700  1.000 33.37701  ? 8   PHE A HD1  1 
ATOM   130  H HD2  . PHE A 1 8   ? -4.79900  -11.30500 18.92000  1.000 30.23292  ? 8   PHE A HD2  1 
ATOM   131  H HE1  . PHE A 1 8   ? -2.47200  -14.97300 17.22800  1.000 44.03432  ? 8   PHE A HE1  1 
ATOM   132  H HE2  . PHE A 1 8   ? -3.49600  -12.58500 20.34500  1.000 30.94132  ? 8   PHE A HE2  1 
ATOM   133  H HZ   . PHE A 1 8   ? -2.32100  -14.44000 19.48700  1.000 38.08705  ? 8   PHE A HZ   1 
ATOM   134  N N    . PRO A 1 9   ? -4.99400  -10.69800 13.16100  1.000 22.42825  ? 9   PRO A N    1 
ATOM   135  C CA   . PRO A 1 9   ? -5.80800  -10.32400 11.98800  1.000 22.93689  ? 9   PRO A CA   1 
ATOM   136  C C    . PRO A 1 9   ? -7.28800  -10.36900 12.38100  1.000 24.08099  ? 9   PRO A C    1 
ATOM   137  O O    . PRO A 1 9   ? -7.72900  -11.28100 13.08200  1.000 25.81827  ? 9   PRO A O    1 
ATOM   138  C CB   . PRO A 1 9   ? -5.46300  -11.39700 10.93500  1.000 26.98801  ? 9   PRO A CB   1 
ATOM   139  C CG   . PRO A 1 9   ? -4.14700  -12.05700 11.44700  1.000 28.09853  ? 9   PRO A CG   1 
ATOM   140  C CD   . PRO A 1 9   ? -4.28200  -11.97400 12.98100  1.000 24.27513  ? 9   PRO A CD   1 
ATOM   141  H HA   . PRO A 1 9   ? -5.57100  -9.44200  11.66100  1.000 27.52507  ? 9   PRO A HA   1 
ATOM   142  H HB2  . PRO A 1 9   ? -6.17900  -12.05000 10.88700  1.000 32.38642  ? 9   PRO A HB2  1 
ATOM   143  H HB3  . PRO A 1 9   ? -5.32300  -10.97600 10.07200  1.000 32.38642  ? 9   PRO A HB3  1 
ATOM   144  H HG2  . PRO A 1 9   ? -4.10100  -12.98000 11.15100  1.000 33.71904  ? 9   PRO A HG2  1 
ATOM   145  H HG3  . PRO A 1 9   ? -3.37900  -11.55100 11.13700  1.000 33.71904  ? 9   PRO A HG3  1 
ATOM   146  H HD2  . PRO A 1 9   ? -4.81200  -12.71300 13.31800  1.000 29.13096  ? 9   PRO A HD2  1 
ATOM   147  H HD3  . PRO A 1 9   ? -3.40300  -11.94500 13.38800  1.000 29.13096  ? 9   PRO A HD3  1 
ATOM   148  N N    . SER A 1 10  ? -8.04600  -9.36400  11.95700  1.000 25.17397  ? 10  SER A N    1 
ATOM   149  C CA   . SER A 1 10  ? -9.37500  -9.12100  12.51200  1.000 24.10819  ? 10  SER A CA   1 
ATOM   150  C C    . SER A 1 10  ? -10.51700 -9.72500  11.68900  1.000 24.33365  ? 10  SER A C    1 
ATOM   151  O O    . SER A 1 10  ? -11.66900 -9.69700  12.15100  1.000 24.46683  ? 10  SER A O    1 
ATOM   152  C CB   . SER A 1 10  ? -9.59300  -7.61100  12.67700  1.000 23.69448  ? 10  SER A CB   1 
ATOM   153  O OG   . SER A 1 10  ? -9.51000  -6.90000  11.42900  1.000 25.26307  ? 10  SER A OG   1 
ATOM   154  H H    . SER A 1 10  ? -7.81400  -8.80500  11.34600  1.000 30.20956  ? 10  SER A H    1 
ATOM   155  H HA   . SER A 1 10  ? -9.41500  -9.51800  13.39600  1.000 28.93063  ? 10  SER A HA   1 
ATOM   156  H HB2  . SER A 1 10  ? -10.47300 -7.46600  13.05800  1.000 28.43418  ? 10  SER A HB2  1 
ATOM   157  H HB3  . SER A 1 10  ? -8.91500  -7.26300  13.27800  1.000 28.43418  ? 10  SER A HB3  1 
ATOM   158  H HG   . SER A 1 10  ? -10.09400 -7.18500  10.89700  1.000 30.31648  ? 10  SER A HG   1 
ATOM   159  N N    . GLY A 1 11  ? -10.21600 -10.32800 10.53300  1.000 23.78956  ? 11  GLY A N    1 
ATOM   160  C CA   . GLY A 1 11  ? -11.27500 -10.76100 9.62900   1.000 25.43402  ? 11  GLY A CA   1 
ATOM   161  C C    . GLY A 1 11  ? -12.27500 -11.70900 10.27400  1.000 26.16345  ? 11  GLY A C    1 
ATOM   162  O O    . GLY A 1 11  ? -13.47500 -11.58100 10.05800  1.000 24.34839  ? 11  GLY A O    1 
ATOM   163  H H    . GLY A 1 11  ? -9.41900  -10.49400 10.25600  1.000 28.54827  ? 11  GLY A H    1 
ATOM   164  H HA2  . GLY A 1 11  ? -11.75800 -9.98400  9.30700   1.000 30.52163  ? 11  GLY A HA2  1 
ATOM   165  H HA3  . GLY A 1 11  ? -10.87900 -11.21100 8.86600   1.000 30.52163  ? 11  GLY A HA3  1 
ATOM   166  N N    . LYS A 1 12  ? -11.79100 -12.69700 11.04300  1.000 26.92354  ? 12  LYS A N    1 
ATOM   167  C CA   . LYS A 1 12  ? -12.72300 -13.63600 11.68300  1.000 27.41790  ? 12  LYS A CA   1 
ATOM   168  C C    . LYS A 1 12  ? -13.72000 -12.92700 12.59500  1.000 27.71572  ? 12  LYS A C    1 
ATOM   169  O O    . LYS A 1 12  ? -14.84900 -13.40300 12.77100  1.000 29.25170  ? 12  LYS A O    1 
ATOM   170  C CB   . LYS A 1 12  ? -11.96400 -14.69100 12.49300  1.000 27.71899  ? 12  LYS A CB   1 
ATOM   171  C CG   . LYS A 1 12  ? -11.27300 -15.72600 11.56000  1.000 37.52684  ? 12  LYS A CG   1 
ATOM   172  C CD   . LYS A 1 12  ? -10.44600 -16.72300 12.37200  1.000 30.98137  ? 12  LYS A CD   1 
ATOM   173  C CE   . LYS A 1 12  ? -9.93000  -17.84800 11.45600  1.000 42.47800  ? 12  LYS A CE   1 
ATOM   174  N NZ   . LYS A 1 12  ? -8.90100  -17.25100 10.57300  1.000 45.32814  ? 12  LYS A NZ   1 
ATOM   175  H H    . LYS A 1 12  ? -10.95900 -12.84100 11.20500  1.000 32.30905  ? 12  LYS A H    1 
ATOM   176  H HA   . LYS A 1 12  ? -13.22600 -14.09600 10.99300  1.000 32.90228  ? 12  LYS A HA   1 
ATOM   177  H HB2  . LYS A 1 12  ? -11.28000 -14.25600 13.02600  1.000 33.26359  ? 12  LYS A HB2  1 
ATOM   178  H HB3  . LYS A 1 12  ? -12.58700 -15.16500 13.06600  1.000 33.26359  ? 12  LYS A HB3  1 
ATOM   179  H HG2  . LYS A 1 12  ? -11.94900 -16.21800 11.06800  1.000 45.03301  ? 12  LYS A HG2  1 
ATOM   180  H HG3  . LYS A 1 12  ? -10.68000 -15.26200 10.94800  1.000 45.03301  ? 12  LYS A HG3  1 
ATOM   181  H HD2  . LYS A 1 12  ? -9.68300  -16.27000 12.76400  1.000 37.17844  ? 12  LYS A HD2  1 
ATOM   182  H HD3  . LYS A 1 12  ? -11.00000 -17.11800 13.06400  1.000 37.17844  ? 12  LYS A HD3  1 
ATOM   183  H HE2  . LYS A 1 12  ? -9.52400  -18.55100 11.98700  1.000 50.97440  ? 12  LYS A HE2  1 
ATOM   184  H HE3  . LYS A 1 12  ? -10.65400 -18.19400 10.91100  1.000 50.97440  ? 12  LYS A HE3  1 
ATOM   185  H HZ1  . LYS A 1 12  ? -8.54900  -17.87900 10.04900  1.000 54.39457  ? 12  LYS A HZ1  1 
ATOM   186  H HZ2  . LYS A 1 12  ? -9.26600  -16.62000 10.06300  1.000 54.39457  ? 12  LYS A HZ2  1 
ATOM   187  H HZ3  . LYS A 1 12  ? -8.25300  -16.88800 11.06300  1.000 54.39457  ? 12  LYS A HZ3  1 
ATOM   188  N N    . VAL A 1 13  ? -13.34100 -11.81300 13.18500  1.000 23.40706  ? 13  VAL A N    1 
ATOM   189  C CA   . VAL A 1 13  ? -14.26600 -11.06500 14.05100  1.000 24.44966  ? 13  VAL A CA   1 
ATOM   190  C C    . VAL A 1 13  ? -15.12300 -10.09600 13.25900  1.000 25.60072  ? 13  VAL A C    1 
ATOM   191  O O    . VAL A 1 13  ? -16.29000 -9.85300  13.60600  1.000 23.97808  ? 13  VAL A O    1 
ATOM   192  C CB   . VAL A 1 13  ? -13.47200 -10.32000 15.15600  1.000 21.67888  ? 13  VAL A CB   1 
ATOM   193  C CG1  . VAL A 1 13  ? -14.45900 -9.49600  16.07900  1.000 24.11746  ? 13  VAL A CG1  1 
ATOM   194  C CG2  . VAL A 1 13  ? -12.64400 -11.34100 15.97100  1.000 28.01398  ? 13  VAL A CG2  1 
ATOM   195  H H    . VAL A 1 13  ? -12.56100 -11.46000 13.10900  1.000 28.08927  ? 13  VAL A H    1 
ATOM   196  H HA   . VAL A 1 13  ? -14.86100 -11.69300 14.49000  1.000 29.34039  ? 13  VAL A HA   1 
ATOM   197  H HB   . VAL A 1 13  ? -12.85700 -9.69600  14.74000  1.000 26.01546  ? 13  VAL A HB   1 
ATOM   198  H HG11 . VAL A 1 13  ? -13.97400 -9.18800  16.86000  1.000 28.94175  ? 13  VAL A HG11 1 
ATOM   199  H HG12 . VAL A 1 13  ? -14.80000 -8.73600  15.58200  1.000 28.94175  ? 13  VAL A HG12 1 
ATOM   200  H HG13 . VAL A 1 13  ? -15.19100 -10.07200 16.35100  1.000 28.94175  ? 13  VAL A HG13 1 
ATOM   201  H HG21 . VAL A 1 13  ? -12.22900 -10.88500 16.71900  1.000 33.61758  ? 13  VAL A HG21 1 
ATOM   202  H HG22 . VAL A 1 13  ? -13.23500 -12.03800 16.29600  1.000 33.61758  ? 13  VAL A HG22 1 
ATOM   203  H HG23 . VAL A 1 13  ? -11.96200 -11.72500 15.39800  1.000 33.61758  ? 13  VAL A HG23 1 
ATOM   204  N N    . GLU A 1 14  ? -14.52000 -9.45200  12.25100  1.000 22.89511  ? 14  GLU A N    1 
ATOM   205  C CA   . GLU A 1 14  ? -15.28000 -8.57200  11.38100  1.000 24.06749  ? 14  GLU A CA   1 
ATOM   206  C C    . GLU A 1 14  ? -16.53100 -9.26200  10.88400  1.000 26.76140  ? 14  GLU A C    1 
ATOM   207  O O    . GLU A 1 14  ? -17.56800 -8.62600  10.73400  1.000 25.97609  ? 14  GLU A O    1 
ATOM   208  C CB   . GLU A 1 14  ? -14.46400 -8.16000  10.15200  1.000 24.07189  ? 14  GLU A CB   1 
ATOM   209  C CG   . GLU A 1 14  ? -13.31400 -7.21800  10.51400  1.000 26.37781  ? 14  GLU A CG   1 
ATOM   210  C CD   . GLU A 1 14  ? -12.39900 -7.00900  9.31400   1.000 27.95849  ? 14  GLU A CD   1 
ATOM   211  O OE1  . GLU A 1 14  ? -12.91900 -6.69200  8.21500   1.000 31.27522  ? 14  GLU A OE1  1 
ATOM   212  O OE2  . GLU A 1 14  ? -11.18300 -7.18600  9.51800   1.000 25.16708  ? 14  GLU A OE2  1 
ATOM   213  H H    . GLU A 1 14  ? -13.68400 -9.51200  12.05900  1.000 27.47493  ? 14  GLU A H    1 
ATOM   214  H HA   . GLU A 1 14  ? -15.53700 -7.77300  11.86700  1.000 28.88179  ? 14  GLU A HA   1 
ATOM   215  H HB2  . GLU A 1 14  ? -14.08700 -8.95300  9.74000   1.000 28.88707  ? 14  GLU A HB2  1 
ATOM   216  H HB3  . GLU A 1 14  ? -15.04400 -7.70100  9.52400   1.000 28.88707  ? 14  GLU A HB3  1 
ATOM   217  H HG2  . GLU A 1 14  ? -13.67300 -6.35700  10.78000  1.000 31.65417  ? 14  GLU A HG2  1 
ATOM   218  H HG3  . GLU A 1 14  ? -12.79300 -7.60600  11.23400  1.000 31.65417  ? 14  GLU A HG3  1 
ATOM   219  N N    . GLY A 1 15  ? -16.43500 -10.54600 10.60100  1.000 24.18542  ? 15  GLY A N    1 
ATOM   220  C CA   . GLY A 1 15  ? -17.58600 -11.22400 10.01500  1.000 30.02958  ? 15  GLY A CA   1 
ATOM   221  C C    . GLY A 1 15  ? -18.67700 -11.53500 11.00500  1.000 29.60329  ? 15  GLY A C    1 
ATOM   222  O O    . GLY A 1 15  ? -19.70700 -12.11900 10.65400  1.000 28.99649  ? 15  GLY A O    1 
ATOM   223  H H    . GLY A 1 15  ? -15.74200 -11.03900 10.73100  1.000 29.02331  ? 15  GLY A H    1 
ATOM   224  H HA2  . GLY A 1 15  ? -17.96200 -10.66700 9.31500   1.000 36.03630  ? 15  GLY A HA2  1 
ATOM   225  H HA3  . GLY A 1 15  ? -17.29400 -12.05800 9.61500   1.000 36.03630  ? 15  GLY A HA3  1 
ATOM   226  N N    . CYS A 1 16  ? -18.43900 -11.19200 12.26600  1.000 25.73484  ? 16  CYS A N    1 
ATOM   227  C CA   . CYS A 1 16  ? -19.43100 -11.39900 13.31400  1.000 27.72498  ? 16  CYS A CA   1 
ATOM   228  C C    . CYS A 1 16  ? -20.08600 -10.10800 13.75700  1.000 26.76200  ? 16  CYS A C    1 
ATOM   229  O O    . CYS A 1 16  ? -21.02400 -10.16700 14.56200  1.000 26.51797  ? 16  CYS A O    1 
ATOM   230  C CB   . CYS A 1 16  ? -18.77700 -12.06000 14.53600  1.000 27.21865  ? 16  CYS A CB   1 
ATOM   231  S SG   . CYS A 1 16  ? -18.08800 -13.67900 14.09600  1.000 33.24005  ? 16  CYS A SG   1 
ATOM   232  H H    . CYS A 1 16  ? -17.70800 -10.83800 12.54600  1.000 30.88260  ? 16  CYS A H    1 
ATOM   233  H HA   . CYS A 1 16  ? -20.12500 -11.99200 12.98800  1.000 33.27078  ? 16  CYS A HA   1 
ATOM   234  H HB2  . CYS A 1 16  ? -18.05600 -11.49800 14.86000  1.000 32.66318  ? 16  CYS A HB2  1 
ATOM   235  H HB3  . CYS A 1 16  ? -19.44400 -12.18800 15.22900  1.000 32.66318  ? 16  CYS A HB3  1 
ATOM   236  H HG   . CYS A 1 16  ? -17.27700 -13.53400 13.22400  1.000 39.88886  ? 16  CYS A HG   1 
ATOM   237  N N    . MET A 1 17  ? -19.62400 -8.94100  13.27900  1.000 28.44744  ? 17  MET A N    1 
ATOM   238  C CA   . MET A 1 17  ? -20.11800 -7.69600  13.86700  1.000 27.85102  ? 17  MET A CA   1 
ATOM   239  C C    . MET A 1 17  ? -21.44100 -7.30100  13.23500  1.000 29.74433  ? 17  MET A C    1 
ATOM   240  O O    . MET A 1 17  ? -21.60700 -7.37900  12.00700  1.000 29.59115  ? 17  MET A O    1 
ATOM   241  C CB   . MET A 1 17  ? -19.10000 -6.55300  13.71300  1.000 25.66525  ? 17  MET A CB   1 
ATOM   242  C CG   . MET A 1 17  ? -17.77600 -6.85100  14.39400  1.000 27.12170  ? 17  MET A CG   1 
ATOM   243  S SD   . MET A 1 17  ? -17.93800 -7.36700  16.13800  1.000 28.47307  ? 17  MET A SD   1 
ATOM   244  C CE   . MET A 1 17  ? -18.88500 -6.02500  16.89100  1.000 25.07991  ? 17  MET A CE   1 
ATOM   245  H H    . MET A 1 17  ? -19.05100 -8.84800  12.64400  1.000 34.13773  ? 17  MET A H    1 
ATOM   246  H HA   . MET A 1 17  ? -20.26700 -7.83800  14.81400  1.000 33.42203  ? 17  MET A HA   1 
ATOM   247  H HB2  . MET A 1 17  ? -18.92600 -6.40900  12.77000  1.000 30.79910  ? 17  MET A HB2  1 
ATOM   248  H HB3  . MET A 1 17  ? -19.46700 -5.74700  14.10900  1.000 30.79910  ? 17  MET A HB3  1 
ATOM   249  H HG2  . MET A 1 17  ? -17.33400 -7.56800  13.91400  1.000 32.54684  ? 17  MET A HG2  1 
ATOM   250  H HG3  . MET A 1 17  ? -17.22600 -6.05300  14.37000  1.000 32.54684  ? 17  MET A HG3  1 
ATOM   251  H HE1  . MET A 1 17  ? -19.00900 -6.21700  17.83400  1.000 30.09669  ? 17  MET A HE1  1 
ATOM   252  H HE2  . MET A 1 17  ? -18.39500 -5.19500  16.78300  1.000 30.09669  ? 17  MET A HE2  1 
ATOM   253  H HE3  . MET A 1 17  ? -19.74700 -5.96100  16.45000  1.000 30.09669  ? 17  MET A HE3  1 
ATOM   254  N N    . VAL A 1 18  ? -22.38900 -6.88900  14.08100  1.000 25.78656  ? 18  VAL A N    1 
ATOM   255  C CA   . VAL A 1 18  ? -23.70300 -6.41200  13.64600  1.000 30.59670  ? 18  VAL A CA   1 
ATOM   256  C C    . VAL A 1 18  ? -24.05000 -5.16400  14.45100  1.000 28.89504  ? 18  VAL A C    1 
ATOM   257  O O    . VAL A 1 18  ? -23.35400 -4.78300  15.39300  1.000 26.37806  ? 18  VAL A O    1 
ATOM   258  C CB   . VAL A 1 18  ? -24.82800 -7.47000  13.79100  1.000 30.87391  ? 18  VAL A CB   1 
ATOM   259  C CG1  . VAL A 1 18  ? -24.50500 -8.68700  12.90300  1.000 32.59147  ? 18  VAL A CG1  1 
ATOM   260  C CG2  . VAL A 1 18  ? -25.04100 -7.88600  15.30100  1.000 29.05535  ? 18  VAL A CG2  1 
ATOM   261  H H    . VAL A 1 18  ? -22.29000 -6.87700  14.93500  1.000 30.94468  ? 18  VAL A H    1 
ATOM   262  H HA   . VAL A 1 18  ? -23.65200 -6.15900  12.71100  1.000 36.71685  ? 18  VAL A HA   1 
ATOM   263  H HB   . VAL A 1 18  ? -25.65900 -7.08500  13.47200  1.000 37.04949  ? 18  VAL A HB   1 
ATOM   264  H HG11 . VAL A 1 18  ? -25.23400 -9.32400  12.96300  1.000 39.11056  ? 18  VAL A HG11 1 
ATOM   265  H HG12 . VAL A 1 18  ? -24.40000 -8.38900  11.98600  1.000 39.11056  ? 18  VAL A HG12 1 
ATOM   266  H HG13 . VAL A 1 18  ? -23.68200 -9.09500  13.21400  1.000 39.11056  ? 18  VAL A HG13 1 
ATOM   267  H HG21 . VAL A 1 18  ? -25.67000 -8.62300  15.33900  1.000 34.86722  ? 18  VAL A HG21 1 
ATOM   268  H HG22 . VAL A 1 18  ? -24.18900 -8.15900  15.67600  1.000 34.86722  ? 18  VAL A HG22 1 
ATOM   269  H HG23 . VAL A 1 18  ? -25.39100 -7.12700  15.79300  1.000 34.86722  ? 18  VAL A HG23 1 
ATOM   270  N N    . GLN A 1 19  ? -25.10800 -4.50500  13.98500  1.000 27.54289  ? 19  GLN A N    1 
ATOM   271  C CA   . GLN A 1 19  ? -25.62200 -3.30200  14.66500  1.000 30.98857  ? 19  GLN A CA   1 
ATOM   272  C C    . GLN A 1 19  ? -26.90900 -3.70200  15.37500  1.000 31.15840  ? 19  GLN A C    1 
ATOM   273  O O    . GLN A 1 19  ? -27.71100 -4.40700  14.77000  1.000 34.14374  ? 19  GLN A O    1 
ATOM   274  C CB   . GLN A 1 19  ? -25.96100 -2.21300  13.65400  1.000 33.02974  ? 19  GLN A CB   1 
ATOM   275  C CG   . GLN A 1 19  ? -26.40500 -0.90300  14.27700  1.000 36.05931  ? 19  GLN A CG   1 
ATOM   276  C CD   . GLN A 1 19  ? -26.57100 0.15700   13.22000  1.000 44.43504  ? 19  GLN A CD   1 
ATOM   277  O OE1  . GLN A 1 19  ? -26.62800 1.34400   13.51000  1.000 49.03261  ? 19  GLN A OE1  1 
ATOM   278  N NE2  . GLN A 1 19  ? -26.64100 -0.27200  11.97400  1.000 50.73120  ? 19  GLN A NE2  1 
ATOM   279  H H    . GLN A 1 19  ? -25.54900 -4.72700  13.28100  1.000 33.05227  ? 19  GLN A H    1 
ATOM   280  H HA   . GLN A 1 19  ? -24.98100 -2.96500  15.31000  1.000 37.18708  ? 19  GLN A HA   1 
ATOM   281  H HB2  . GLN A 1 19  ? -25.17800 -2.03800  13.10900  1.000 39.63648  ? 19  GLN A HB2  1 
ATOM   282  H HB3  . GLN A 1 19  ? -26.68600 -2.54100  13.10000  1.000 39.63648  ? 19  GLN A HB3  1 
ATOM   283  H HG2  . GLN A 1 19  ? -27.25800 -1.02800  14.72100  1.000 43.27197  ? 19  GLN A HG2  1 
ATOM   284  H HG3  . GLN A 1 19  ? -25.73400 -0.60300  14.91000  1.000 43.27197  ? 19  GLN A HG3  1 
ATOM   285  H HE21 . GLN A 1 19  ? -26.60300 -1.10400  11.77400  1.000 60.87824  ? 19  GLN A HE21 1 
ATOM   286  H HE22 . GLN A 1 19  ? -26.73700 0.30300   11.34200  1.000 60.87824  ? 19  GLN A HE22 1 
ATOM   287  N N    . VAL A 1 20  ? -27.05000 -3.29700  16.62300  1.000 29.17643  ? 20  VAL A N    1 
ATOM   288  C CA   . VAL A 1 20  ? -28.24600 -3.56400  17.40400  1.000 31.73555  ? 20  VAL A CA   1 
ATOM   289  C C    . VAL A 1 20  ? -28.85200 -2.24000  17.82600  1.000 35.05550  ? 20  VAL A C    1 
ATOM   290  O O    . VAL A 1 20  ? -28.17100 -1.40900  18.45600  1.000 31.79650  ? 20  VAL A O    1 
ATOM   291  C CB   . VAL A 1 20  ? -27.95700 -4.43600  18.64500  1.000 30.36969  ? 20  VAL A CB   1 
ATOM   292  C CG1  . VAL A 1 20  ? -29.27100 -4.72000  19.37900  1.000 31.38204  ? 20  VAL A CG1  1 
ATOM   293  C CG2  . VAL A 1 20  ? -27.26900 -5.75000  18.21600  1.000 29.00582  ? 20  VAL A CG2  1 
ATOM   294  H H    . VAL A 1 20  ? -26.45100 -2.85400  17.05300  1.000 35.01252  ? 20  VAL A H    1 
ATOM   295  H HA   . VAL A 1 20  ? -28.89300 -4.03000  16.85200  1.000 38.08346  ? 20  VAL A HA   1 
ATOM   296  H HB   . VAL A 1 20  ? -27.36400 -3.95900  19.24600  1.000 36.44443  ? 20  VAL A HB   1 
ATOM   297  H HG11 . VAL A 1 20  ? -29.13200 -5.45000  20.00200  1.000 37.65925  ? 20  VAL A HG11 1 
ATOM   298  H HG12 . VAL A 1 20  ? -29.54600 -3.92300  19.85900  1.000 37.65925  ? 20  VAL A HG12 1 
ATOM   299  H HG13 . VAL A 1 20  ? -29.94800 -4.96700  18.73000  1.000 37.65925  ? 20  VAL A HG13 1 
ATOM   300  H HG21 . VAL A 1 20  ? -27.14400 -6.31000  18.99800  1.000 34.80779  ? 20  VAL A HG21 1 
ATOM   301  H HG22 . VAL A 1 20  ? -27.83200 -6.20400  17.57000  1.000 34.80779  ? 20  VAL A HG22 1 
ATOM   302  H HG23 . VAL A 1 20  ? -26.40900 -5.54200  17.81800  1.000 34.80779  ? 20  VAL A HG23 1 
ATOM   303  N N    . THR A 1 21  ? -30.15100 -2.09900  17.57300  1.000 34.42650  ? 21  THR A N    1 
ATOM   304  C CA   . THR A 1 21  ? -30.89400 -0.91100  17.94600  1.000 34.92797  ? 21  THR A CA   1 
ATOM   305  C C    . THR A 1 21  ? -32.14200 -1.25900  18.76400  1.000 38.37813  ? 21  THR A C    1 
ATOM   306  O O    . THR A 1 21  ? -32.91100 -2.16800  18.42200  1.000 36.80095  ? 21  THR A O    1 
ATOM   307  C CB   . THR A 1 21  ? -31.27300 -0.11700  16.68800  1.000 40.84514  ? 21  THR A CB   1 
ATOM   308  O OG1  . THR A 1 21  ? -30.08300 0.38000   16.07100  1.000 37.89679  ? 21  THR A OG1  1 
ATOM   309  C CG2  . THR A 1 21  ? -32.14400 1.06100   17.01200  1.000 37.80216  ? 21  THR A CG2  1 
ATOM   310  H H    . THR A 1 21  ? -30.63000 -2.69400  17.17700  1.000 41.31260  ? 21  THR A H    1 
ATOM   311  H HA   . THR A 1 21  ? -30.32900 -0.34500  18.49500  1.000 41.91437  ? 21  THR A HA   1 
ATOM   312  H HB   . THR A 1 21  ? -31.74200 -0.69000  16.06600  1.000 49.01497  ? 21  THR A HB   1 
ATOM   313  H HG1  . THR A 1 21  ? -30.27800 0.81700   15.38100  1.000 45.47695  ? 21  THR A HG1  1 
ATOM   314  H HG21 . THR A 1 21  ? -32.17300 1.66700   16.25500  1.000 45.36340  ? 21  THR A HG21 1 
ATOM   315  H HG22 . THR A 1 21  ? -33.04600 0.76500   17.21200  1.000 45.36340  ? 21  THR A HG22 1 
ATOM   316  H HG23 . THR A 1 21  ? -31.78800 1.53500   17.78000  1.000 45.36340  ? 21  THR A HG23 1 
ATOM   317  N N    A CYS A 1 22  ? -32.36900 -0.50500  19.82800  0.640 36.57186  ? 22  CYS A N    1 
ATOM   318  N N    B CYS A 1 22  ? -32.30600 -0.52300  19.85600  0.360 35.56703  ? 22  CYS A N    1 
ATOM   319  C CA   A CYS A 1 22  ? -33.57700 -0.64600  20.63200  0.640 40.26838  ? 22  CYS A CA   1 
ATOM   320  C CA   B CYS A 1 22  ? -33.49300 -0.53600  20.69500  0.360 40.22938  ? 22  CYS A CA   1 
ATOM   321  C C    A CYS A 1 22  ? -34.02900 0.76700   20.97400  0.640 40.28300  ? 22  CYS A C    1 
ATOM   322  C C    B CYS A 1 22  ? -33.95100 0.89800   20.82800  0.360 40.25364  ? 22  CYS A C    1 
ATOM   323  O O    A CYS A 1 22  ? -33.29300 1.51000   21.62800  0.640 38.33842  ? 22  CYS A O    1 
ATOM   324  O O    B CYS A 1 22  ? -33.16600 1.75500   21.25000  0.360 37.56293  ? 22  CYS A O    1 
ATOM   325  C CB   A CYS A 1 22  ? -33.31300 -1.48000  21.88700  0.640 38.16862  ? 22  CYS A CB   1 
ATOM   326  C CB   B CYS A 1 22  ? -33.19800 -1.09300  22.07800  0.360 38.64253  ? 22  CYS A CB   1 
ATOM   327  S SG   A CYS A 1 22  ? -34.78400 -1.95600  22.79700  0.640 39.11040  ? 22  CYS A SG   1 
ATOM   328  S SG   B CYS A 1 22  ? -33.29800 -2.81100  22.14500  0.360 40.13097  ? 22  CYS A SG   1 
ATOM   329  H H    A CYS A 1 22  ? -31.83200 0.10500   20.11100  0.640 43.88703  ? 22  CYS A H    1 
ATOM   330  H H    B CYS A 1 22  ? -31.70600 0.02200   20.14400  0.360 42.68124  ? 22  CYS A H    1 
ATOM   331  H HA   A CYS A 1 22  ? -34.27200 -1.07700  20.11100  0.640 48.32285  ? 22  CYS A HA   1 
ATOM   332  H HA   B CYS A 1 22  ? -34.19500 -1.06100  20.28000  0.360 48.27605  ? 22  CYS A HA   1 
ATOM   333  H HB2  A CYS A 1 22  ? -32.85300 -2.29300  21.62700  0.640 45.80315  ? 22  CYS A HB2  1 
ATOM   334  H HB2  B CYS A 1 22  ? -32.29900 -0.83600  22.33200  0.360 46.37183  ? 22  CYS A HB2  1 
ATOM   335  H HB3  A CYS A 1 22  ? -32.75100 -0.96600  22.48700  0.640 45.80315  ? 22  CYS A HB3  1 
ATOM   336  H HB3  B CYS A 1 22  ? -33.83900 -0.73000  22.70900  0.360 46.37183  ? 22  CYS A HB3  1 
ATOM   337  H HG   A CYS A 1 22  ? -34.45900 -2.60200  23.75500  0.640 46.93328  ? 22  CYS A HG   1 
ATOM   338  H HG   B CYS A 1 22  ? -32.48100 -3.25900  21.38900  0.360 48.15796  ? 22  CYS A HG   1 
ATOM   339  N N    . GLY A 1 23  ? -35.19600 1.15900   20.46900  1.000 42.91233  ? 23  GLY A N    1 
ATOM   340  C CA   . GLY A 1 23  ? -35.67200 2.52400   20.59100  1.000 48.97626  ? 23  GLY A CA   1 
ATOM   341  C C    . GLY A 1 23  ? -34.72100 3.44700   19.85900  1.000 39.14076  ? 23  GLY A C    1 
ATOM   342  O O    . GLY A 1 23  ? -34.39900 3.23000   18.68900  1.000 45.33587  ? 23  GLY A O    1 
ATOM   343  H H    A GLY A 1 23  ? -35.73600 0.64100   20.04500  0.640 51.49560  ? 23  GLY A H    1 
ATOM   344  H H    B GLY A 1 23  ? -35.76500 0.59100   20.16400  0.360 51.49560  ? 23  GLY A H    1 
ATOM   345  H HA2  . GLY A 1 23  ? -36.55700 2.60500   20.20200  1.000 58.77231  ? 23  GLY A HA2  1 
ATOM   346  H HA3  . GLY A 1 23  ? -35.71000 2.78200   21.52500  1.000 58.77231  ? 23  GLY A HA3  1 
ATOM   347  N N    . THR A 1 24  ? -34.18600 4.44300   20.56000  1.000 40.91201  ? 24  THR A N    1 
ATOM   348  C CA   . THR A 1 24  ? -33.23500 5.38300   19.97000  1.000 45.10419  ? 24  THR A CA   1 
ATOM   349  C C    . THR A 1 24  ? -31.78000 5.05900   20.29000  1.000 44.96059  ? 24  THR A C    1 
ATOM   350  O O    . THR A 1 24  ? -30.91000 5.87900   19.99800  1.000 43.47646  ? 24  THR A O    1 
ATOM   351  C CB   . THR A 1 24  ? -33.53100 6.80300   20.44300  1.000 44.68409  ? 24  THR A CB   1 
ATOM   352  O OG1  . THR A 1 24  ? -33.36700 6.87900   21.86700  1.000 51.88990  ? 24  THR A OG1  1 
ATOM   353  C CG2  . THR A 1 24  ? -34.97100 7.19000   20.05900  1.000 51.51616  ? 24  THR A CG2  1 
ATOM   354  H H    . THR A 1 24  ? -34.35900 4.59800   21.38800  1.000 49.09522  ? 24  THR A H    1 
ATOM   355  H HA   . THR A 1 24  ? -33.33600 5.36700   19.00500  1.000 54.12583  ? 24  THR A HA   1 
ATOM   356  H HB   . THR A 1 24  ? -32.92100 7.42200   20.01300  1.000 53.62170  ? 24  THR A HB   1 
ATOM   357  H HG1  . THR A 1 24  ? -33.52900 7.65900   22.13400  1.000 62.26869  ? 24  THR A HG1  1 
ATOM   358  H HG21 . THR A 1 24  ? -35.13700 8.11800   20.28900  1.000 61.82019  ? 24  THR A HG21 1 
ATOM   359  H HG22 . THR A 1 24  ? -35.10200 7.07400   19.10500  1.000 61.82019  ? 24  THR A HG22 1 
ATOM   360  H HG23 . THR A 1 24  ? -35.60400 6.62900   20.53400  1.000 61.82019  ? 24  THR A HG23 1 
ATOM   361  N N    . THR A 1 25  ? -31.55100 3.92100   20.94000  1.000 40.23818  ? 25  THR A N    1 
ATOM   362  C CA   . THR A 1 25  ? -30.19000 3.53000   21.38700  1.000 38.20527  ? 25  THR A CA   1 
ATOM   363  C C    . THR A 1 25  ? -29.59100 2.52200   20.41200  1.000 35.13518  ? 25  THR A C    1 
ATOM   364  O O    . THR A 1 25  ? -30.26200 1.53900   20.11500  1.000 34.55352  ? 25  THR A O    1 
ATOM   365  C CB   . THR A 1 25  ? -30.24300 2.92900   22.79800  1.000 36.70168  ? 25  THR A CB   1 
ATOM   366  O OG1  . THR A 1 25  ? -30.81000 3.88600   23.69000  1.000 40.86804  ? 25  THR A OG1  1 
ATOM   367  C CG2  . THR A 1 25  ? -28.88800 2.50500   23.31400  1.000 39.34921  ? 25  THR A CG2  1 
ATOM   368  H H    . THR A 1 25  ? -32.15900 3.34700   21.14100  1.000 48.28662  ? 25  THR A H    1 
ATOM   369  H HA   . THR A 1 25  ? -29.61800 4.31300   21.40900  1.000 45.84712  ? 25  THR A HA   1 
ATOM   370  H HB   . THR A 1 25  ? -30.81200 2.14300   22.78100  1.000 44.04282  ? 25  THR A HB   1 
ATOM   371  H HG1  . THR A 1 25  ? -30.84500 3.56900   24.46700  1.000 49.04245  ? 25  THR A HG1  1 
ATOM   372  H HG21 . THR A 1 25  ? -28.95500 2.25000   24.24800  1.000 47.21985  ? 25  THR A HG21 1 
ATOM   373  H HG22 . THR A 1 25  ? -28.55800 1.74800   22.80500  1.000 47.21985  ? 25  THR A HG22 1 
ATOM   374  H HG23 . THR A 1 25  ? -28.25900 3.23900   23.23300  1.000 47.21985  ? 25  THR A HG23 1 
ATOM   375  N N    . THR A 1 26  ? -28.36000 2.77200   19.97600  1.000 33.90834  ? 26  THR A N    1 
ATOM   376  C CA   . THR A 1 26  ? -27.67800 1.86100   19.03100  1.000 34.75116  ? 26  THR A CA   1 
ATOM   377  C C    . THR A 1 26  ? -26.26800 1.49800   19.50700  1.000 33.42781  ? 26  THR A C    1 
ATOM   378  O O    . THR A 1 26  ? -25.58300 2.36700   20.04000  1.000 32.04044  ? 26  THR A O    1 
ATOM   379  C CB   . THR A 1 26  ? -27.60600 2.49300   17.63700  1.000 37.41643  ? 26  THR A CB   1 
ATOM   380  O OG1  . THR A 1 26  ? -28.93600 2.66400   17.15100  1.000 45.55399  ? 26  THR A OG1  1 
ATOM   381  C CG2  . THR A 1 26  ? -26.80600 1.68200   16.65000  1.000 38.29000  ? 26  THR A CG2  1 
ATOM   382  H H    . THR A 1 26  ? -27.89200 3.45600   20.20500  1.000 40.69081  ? 26  THR A H    1 
ATOM   383  H HA   . THR A 1 26  ? -28.18800 1.03900   18.96000  1.000 41.70220  ? 26  THR A HA   1 
ATOM   384  H HB   . THR A 1 26  ? -27.18700 3.36500   17.71100  1.000 44.90052  ? 26  THR A HB   1 
ATOM   385  H HG1  . THR A 1 26  ? -29.32300 1.92000   17.10600  1.000 54.66558  ? 26  THR A HG1  1 
ATOM   386  H HG21 . THR A 1 26  ? -26.94500 2.02900   15.75600  1.000 45.94880  ? 26  THR A HG21 1 
ATOM   387  H HG22 . THR A 1 26  ? -25.86100 1.73200   16.86200  1.000 45.94880  ? 26  THR A HG22 1 
ATOM   388  H HG23 . THR A 1 26  ? -27.08900 0.75400   16.67500  1.000 45.94880  ? 26  THR A HG23 1 
ATOM   389  N N    . LEU A 1 27  ? -25.90200 0.23500   19.34900  1.000 28.27727  ? 27  LEU A N    1 
ATOM   390  C CA   . LEU A 1 27  ? -24.51600 -0.19300  19.63300  1.000 26.64636  ? 27  LEU A CA   1 
ATOM   391  C C    . LEU A 1 27  ? -24.19400 -1.39400  18.74400  1.000 25.69611  ? 27  LEU A C    1 
ATOM   392  O O    . LEU A 1 27  ? -24.98400 -1.69400  17.85700  1.000 27.85001  ? 27  LEU A O    1 
ATOM   393  C CB   . LEU A 1 27  ? -24.30500 -0.50600  21.11900  1.000 26.56395  ? 27  LEU A CB   1 
ATOM   394  C CG   . LEU A 1 27  ? -25.43500 -1.16600  21.90200  1.000 31.04263  ? 27  LEU A CG   1 
ATOM   395  C CD1  . LEU A 1 27  ? -25.64100 -2.61300  21.48600  1.000 30.49852  ? 27  LEU A CD1  1 
ATOM   396  C CD2  . LEU A 1 27  ? -25.12900 -1.10000  23.38900  1.000 29.90008  ? 27  LEU A CD2  1 
ATOM   397  H H    . LEU A 1 27  ? -26.42200 -0.39600  19.08200  1.000 33.93352  ? 27  LEU A H    1 
ATOM   398  H HA   . LEU A 1 27  ? -23.91100 0.52600   19.39200  1.000 31.97644  ? 27  LEU A HA   1 
ATOM   399  H HB2  . LEU A 1 27  ? -23.53000 -1.07800  21.21500  1.000 31.87754  ? 27  LEU A HB2  1 
ATOM   400  H HB3  . LEU A 1 27  ? -24.12200 0.33600   21.56500  1.000 31.87754  ? 27  LEU A HB3  1 
ATOM   401  H HG   . LEU A 1 27  ? -26.26100 -0.68400  21.74200  1.000 37.25196  ? 27  LEU A HG   1 
ATOM   402  H HD11 . LEU A 1 27  ? -26.29800 -3.02200  22.06900  1.000 36.59903  ? 27  LEU A HD11 1 
ATOM   403  H HD12 . LEU A 1 27  ? -25.95400 -2.63500  20.56800  1.000 36.59903  ? 27  LEU A HD12 1 
ATOM   404  H HD13 . LEU A 1 27  ? -24.79600 -3.08400  21.55900  1.000 36.59903  ? 27  LEU A HD13 1 
ATOM   405  H HD21 . LEU A 1 27  ? -25.74600 -1.67400  23.86800  1.000 35.88090  ? 27  LEU A HD21 1 
ATOM   406  H HD22 . LEU A 1 27  ? -24.21800 -1.40100  23.53500  1.000 35.88090  ? 27  LEU A HD22 1 
ATOM   407  H HD23 . LEU A 1 27  ? -25.22600 -0.18400  23.69000  1.000 35.88090  ? 27  LEU A HD23 1 
ATOM   408  N N    . ASN A 1 28  ? -23.09400 -2.06800  19.03300  1.000 24.82886  ? 28  ASN A N    1 
ATOM   409  C CA   . ASN A 1 28  ? -22.65000 -3.21000  18.25300  1.000 25.03955  ? 28  ASN A CA   1 
ATOM   410  C C    . ASN A 1 28  ? -23.04200 -4.51000  18.93700  1.000 26.61597  ? 28  ASN A C    1 
ATOM   411  O O    . ASN A 1 28  ? -23.07500 -4.59400  20.17000  1.000 27.07777  ? 28  ASN A O    1 
ATOM   412  C CB   . ASN A 1 28  ? -21.12700 -3.21100  18.08400  1.000 26.38439  ? 28  ASN A CB   1 
ATOM   413  C CG   . ASN A 1 28  ? -20.62100 -1.89900  17.53000  1.000 24.68906  ? 28  ASN A CG   1 
ATOM   414  O OD1  . ASN A 1 28  ? -20.73900 -1.67000  16.33100  1.000 26.54148  ? 28  ASN A OD1  1 
ATOM   415  N ND2  . ASN A 1 28  ? -20.05000 -1.03300  18.39400  1.000 26.81030  ? 28  ASN A ND2  1 
ATOM   416  H H    . ASN A 1 28  ? -22.56900 -1.87800  19.68600  1.000 29.79543  ? 28  ASN A H    1 
ATOM   417  H HA   . ASN A 1 28  ? -23.06000 -3.18500  17.37400  1.000 30.04827  ? 28  ASN A HA   1 
ATOM   418  H HB2  . ASN A 1 28  ? -20.71000 -3.35600  18.94800  1.000 31.66207  ? 28  ASN A HB2  1 
ATOM   419  H HB3  . ASN A 1 28  ? -20.87500 -3.91700  17.46800  1.000 31.66207  ? 28  ASN A HB3  1 
ATOM   420  H HD21 . ASN A 1 28  ? -19.75100 -0.27800  18.11100  1.000 32.17317  ? 28  ASN A HD21 1 
ATOM   421  H HD22 . ASN A 1 28  ? -19.98700 -1.23600  19.22700  1.000 32.17317  ? 28  ASN A HD22 1 
ATOM   422  N N    . GLY A 1 29  ? -23.27500 -5.53700  18.10600  1.000 26.25628  ? 29  GLY A N    1 
ATOM   423  C CA   . GLY A 1 29  ? -23.51800 -6.87300  18.59400  1.000 25.83708  ? 29  GLY A CA   1 
ATOM   424  C C    . GLY A 1 29  ? -22.55900 -7.87200  17.97100  1.000 24.32062  ? 29  GLY A C    1 
ATOM   425  O O    . GLY A 1 29  ? -21.92500 -7.60100  16.94300  1.000 26.27823  ? 29  GLY A O    1 
ATOM   426  H H    . GLY A 1 29  ? -23.29500 -5.47000  17.24900  1.000 31.50833  ? 29  GLY A H    1 
ATOM   427  H HA2  . GLY A 1 29  ? -23.40800 -6.89800  19.55700  1.000 31.00529  ? 29  GLY A HA2  1 
ATOM   428  H HA3  . GLY A 1 29  ? -24.42600 -7.13900  18.37900  1.000 31.00529  ? 29  GLY A HA3  1 
ATOM   429  N N    . LEU A 1 30  ? -22.45500 -9.03800  18.60900  1.000 26.04830  ? 30  LEU A N    1 
ATOM   430  C CA   . LEU A 1 30  ? -21.53800 -10.10000 18.15900  1.000 24.37346  ? 30  LEU A CA   1 
ATOM   431  C C    . LEU A 1 30  ? -22.38900 -11.30000 17.77600  1.000 27.71986  ? 30  LEU A C    1 
ATOM   432  O O    . LEU A 1 30  ? -22.99700 -11.94000 18.65200  1.000 29.87361  ? 30  LEU A O    1 
ATOM   433  C CB   . LEU A 1 30  ? -20.53600 -10.46700 19.24300  1.000 26.30236  ? 30  LEU A CB   1 
ATOM   434  C CG   . LEU A 1 30  ? -19.45300 -11.49800 18.84800  1.000 25.87234  ? 30  LEU A CG   1 
ATOM   435  C CD1  . LEU A 1 30  ? -18.44800 -10.88300 17.86200  1.000 30.52260  ? 30  LEU A CD1  1 
ATOM   436  C CD2  . LEU A 1 30  ? -18.76900 -11.93400 20.12900  1.000 26.00200  ? 30  LEU A CD2  1 
ATOM   437  H H    . LEU A 1 30  ? -22.90600 -9.24500  19.31100  1.000 31.25876  ? 30  LEU A H    1 
ATOM   438  H HA   . LEU A 1 30  ? -21.05100 -9.80300  17.37500  1.000 29.24895  ? 30  LEU A HA   1 
ATOM   439  H HB2  . LEU A 1 30  ? -20.07700 -9.65800  19.52000  1.000 31.56364  ? 30  LEU A HB2  1 
ATOM   440  H HB3  . LEU A 1 30  ? -21.02400 -10.83500 19.99700  1.000 31.56364  ? 30  LEU A HB3  1 
ATOM   441  H HG   . LEU A 1 30  ? -19.86700 -12.27100 18.43400  1.000 31.04761  ? 30  LEU A HG   1 
ATOM   442  H HD11 . LEU A 1 30  ? -17.76300 -11.53900 17.66000  1.000 36.62792  ? 30  LEU A HD11 1 
ATOM   443  H HD12 . LEU A 1 30  ? -18.91500 -10.63200 17.05000  1.000 36.62792  ? 30  LEU A HD12 1 
ATOM   444  H HD13 . LEU A 1 30  ? -18.04600 -10.10000 18.26900  1.000 36.62792  ? 30  LEU A HD13 1 
ATOM   445  H HD21 . LEU A 1 30  ? -17.96900 -12.43600 19.90600  1.000 31.20320  ? 30  LEU A HD21 1 
ATOM   446  H HD22 . LEU A 1 30  ? -18.53400 -11.14800 20.64400  1.000 31.20320  ? 30  LEU A HD22 1 
ATOM   447  H HD23 . LEU A 1 30  ? -19.37900 -12.49100 20.63800  1.000 31.20320  ? 30  LEU A HD23 1 
ATOM   448  N N    . TRP A 1 31  ? -22.43300 -11.59700 16.46800  1.000 27.12098  ? 31  TRP A N    1 
ATOM   449  C CA   . TRP A 1 31  ? -23.33900 -12.59600 15.90800  1.000 25.19802  ? 31  TRP A CA   1 
ATOM   450  C C    . TRP A 1 31  ? -22.54700 -13.87400 15.73300  1.000 32.24068  ? 31  TRP A C    1 
ATOM   451  O O    . TRP A 1 31  ? -21.70800 -13.97700 14.81900  1.000 31.25575  ? 31  TRP A O    1 
ATOM   452  C CB   . TRP A 1 31  ? -23.89200 -12.10600 14.57500  1.000 28.93346  ? 31  TRP A CB   1 
ATOM   453  C CG   . TRP A 1 31  ? -24.87700 -12.97500 13.85400  1.000 31.19767  ? 31  TRP A CG   1 
ATOM   454  C CD1  . TRP A 1 31  ? -25.67800 -13.96900 14.37600  1.000 33.45816  ? 31  TRP A CD1  1 
ATOM   455  C CD2  . TRP A 1 31  ? -25.17800 -12.90700 12.45300  1.000 33.32078  ? 31  TRP A CD2  1 
ATOM   456  N NE1  . TRP A 1 31  ? -26.46600 -14.51800 13.35900  1.000 33.49386  ? 31  TRP A NE1  1 
ATOM   457  C CE2  . TRP A 1 31  ? -26.17800 -13.86800 12.18500  1.000 36.27837  ? 31  TRP A CE2  1 
ATOM   458  C CE3  . TRP A 1 31  ? -24.70700 -12.10400 11.40500  1.000 37.95951  ? 31  TRP A CE3  1 
ATOM   459  C CZ2  . TRP A 1 31  ? -26.69700 -14.05900 10.90100  1.000 42.13919  ? 31  TRP A CZ2  1 
ATOM   460  C CZ3  . TRP A 1 31  ? -25.22600 -12.29400 10.13400  1.000 36.51004  ? 31  TRP A CZ3  1 
ATOM   461  C CH2  . TRP A 1 31  ? -26.20000 -13.26200 9.90100   1.000 37.92977  ? 31  TRP A CH2  1 
ATOM   462  H H    . TRP A 1 31  ? -21.93400 -11.22100 15.87700  1.000 32.54597  ? 31  TRP A H    1 
ATOM   463  H HA   . TRP A 1 31  ? -24.07600 -12.75900 16.51800  1.000 30.23843  ? 31  TRP A HA   1 
ATOM   464  H HB2  . TRP A 1 31  ? -24.32900 -11.25400 14.73000  1.000 34.72095  ? 31  TRP A HB2  1 
ATOM   465  H HB3  . TRP A 1 31  ? -23.14300 -11.97200 13.97400  1.000 34.72095  ? 31  TRP A HB3  1 
ATOM   466  H HD1  . TRP A 1 31  ? -25.69500 -14.23100 15.26800  1.000 40.15060  ? 31  TRP A HD1  1 
ATOM   467  H HE1  . TRP A 1 31  ? -27.04100 -15.15000 13.45500  1.000 40.19344  ? 31  TRP A HE1  1 
ATOM   468  H HE3  . TRP A 1 31  ? -24.05900 -11.45500 11.56000  1.000 45.55222  ? 31  TRP A HE3  1 
ATOM   469  H HZ2  . TRP A 1 31  ? -27.34400 -14.70500 10.73000  1.000 50.56783  ? 31  TRP A HZ2  1 
ATOM   470  H HZ3  . TRP A 1 31  ? -24.92000 -11.77000 9.42900   1.000 43.81285  ? 31  TRP A HZ3  1 
ATOM   471  H HH2  . TRP A 1 31  ? -26.52900 -13.36800 9.03800   1.000 45.51653  ? 31  TRP A HH2  1 
ATOM   472  N N    . LEU A 1 32  ? -22.81500 -14.85000 16.59700  1.000 29.90692  ? 32  LEU A N    1 
ATOM   473  C CA   . LEU A 1 32  ? -22.15800 -16.15000 16.54600  1.000 30.64945  ? 32  LEU A CA   1 
ATOM   474  C C    . LEU A 1 32  ? -23.25300 -17.20400 16.47600  1.000 35.33892  ? 32  LEU A C    1 
ATOM   475  O O    . LEU A 1 32  ? -24.15100 -17.22700 17.32900  1.000 33.17223  ? 32  LEU A O    1 
ATOM   476  C CB   . LEU A 1 32  ? -21.29300 -16.37000 17.78300  1.000 29.07799  ? 32  LEU A CB   1 
ATOM   477  C CG   . LEU A 1 32  ? -20.22500 -15.31700 18.01100  1.000 32.51195  ? 32  LEU A CG   1 
ATOM   478  C CD1  . LEU A 1 32  ? -19.69300 -15.51800 19.43000  1.000 31.07928  ? 32  LEU A CD1  1 
ATOM   479  C CD2  . LEU A 1 32  ? -19.10600 -15.47500 16.94500  1.000 32.84079  ? 32  LEU A CD2  1 
ATOM   480  H H    . LEU A 1 32  ? -23.38700 -14.78000 17.23500  1.000 35.88911  ? 32  LEU A H    1 
ATOM   481  H HA   . LEU A 1 32  ? -21.60300 -16.21600 15.75300  1.000 36.78014  ? 32  LEU A HA   1 
ATOM   482  H HB2  . LEU A 1 32  ? -21.86900 -16.37900 18.56300  1.000 34.89439  ? 32  LEU A HB2  1 
ATOM   483  H HB3  . LEU A 1 32  ? -20.84600 -17.22700 17.69900  1.000 34.89439  ? 32  LEU A HB3  1 
ATOM   484  H HG   . LEU A 1 32  ? -20.61000 -14.43000 17.93900  1.000 39.01514  ? 32  LEU A HG   1 
ATOM   485  H HD11 . LEU A 1 32  ? -19.03200 -14.83300 19.61800  1.000 37.29593  ? 32  LEU A HD11 1 
ATOM   486  H HD12 . LEU A 1 32  ? -20.42900 -15.44900 20.05800  1.000 37.29593  ? 32  LEU A HD12 1 
ATOM   487  H HD13 . LEU A 1 32  ? -19.28600 -16.39500 19.49100  1.000 37.29593  ? 32  LEU A HD13 1 
ATOM   488  H HD21 . LEU A 1 32  ? -18.41400 -14.81700 17.11400  1.000 39.40975  ? 32  LEU A HD21 1 
ATOM   489  H HD22 . LEU A 1 32  ? -18.73500 -16.36900 17.00800  1.000 39.40975  ? 32  LEU A HD22 1 
ATOM   490  H HD23 . LEU A 1 32  ? -19.48700 -15.33600 16.06400  1.000 39.40975  ? 32  LEU A HD23 1 
ATOM   491  N N    . ASP A 1 33  ? -23.19400 -18.06900 15.45700  1.000 35.54337  ? 33  ASP A N    1 
ATOM   492  C CA   . ASP A 1 33  ? -24.26300 -19.03800 15.22400  1.000 35.88114  ? 33  ASP A CA   1 
ATOM   493  C C    . ASP A 1 33  ? -25.58000 -18.26300 15.16700  1.000 38.66266  ? 33  ASP A C    1 
ATOM   494  O O    . ASP A 1 33  ? -25.66300 -17.26000 14.44100  1.000 35.06745  ? 33  ASP A O    1 
ATOM   495  C CB   . ASP A 1 33  ? -24.17100 -20.12400 16.27500  1.000 42.81443  ? 33  ASP A CB   1 
ATOM   496  C CG   . ASP A 1 33  ? -22.90100 -20.93300 16.15100  1.000 50.95719  ? 33  ASP A CG   1 
ATOM   497  O OD1  . ASP A 1 33  ? -22.63400 -21.42000 15.02200  1.000 58.71173  ? 33  ASP A OD1  1 
ATOM   498  O OD2  . ASP A 1 33  ? -22.19800 -21.11400 17.18000  1.000 47.13491  ? 33  ASP A OD2  1 
ATOM   499  H H    . ASP A 1 33  ? -22.54800 -18.11300 14.89100  1.000 42.65284  ? 33  ASP A H    1 
ATOM   500  H HA   . ASP A 1 33  ? -24.12700 -19.45300 14.35800  1.000 43.05816  ? 33  ASP A HA   1 
ATOM   501  H HB2  . ASP A 1 33  ? -24.18600 -19.71900 17.15600  1.000 51.37812  ? 33  ASP A HB2  1 
ATOM   502  H HB3  . ASP A 1 33  ? -24.92300 -20.72800 16.17400  1.000 51.37812  ? 33  ASP A HB3  1 
ATOM   503  N N    . ASP A 1 34  ? -26.62200 -18.67200 15.90400  1.000 37.02687  ? 34  ASP A N    1 
ATOM   504  C CA   . ASP A 1 34  ? -27.89200 -17.96900 15.84700  1.000 38.52894  ? 34  ASP A CA   1 
ATOM   505  C C    . ASP A 1 34  ? -28.13700 -17.07400 17.05800  1.000 37.67029  ? 34  ASP A C    1 
ATOM   506  O O    . ASP A 1 34  ? -29.30000 -16.78300 17.37800  1.000 38.88751  ? 34  ASP A O    1 
ATOM   507  C CB   . ASP A 1 34  ? -29.03300 -18.97300 15.70900  1.000 40.64514  ? 34  ASP A CB   1 
ATOM   508  C CG   . ASP A 1 34  ? -29.13400 -19.95300 16.90100  1.000 42.17208  ? 34  ASP A CG   1 
ATOM   509  O OD1  . ASP A 1 34  ? -28.24600 -20.00500 17.77500  1.000 40.39394  ? 34  ASP A OD1  1 
ATOM   510  O OD2  . ASP A 1 34  ? -30.13900 -20.70500 16.96000  1.000 53.14079  ? 34  ASP A OD2  1 
ATOM   511  H H    . ASP A 1 34  ? -26.61300 -19.34700 16.43700  1.000 44.43304  ? 34  ASP A H    1 
ATOM   512  H HA   . ASP A 1 34  ? -27.90700 -17.40400 15.05900  1.000 46.23553  ? 34  ASP A HA   1 
ATOM   513  H HB2  . ASP A 1 34  ? -29.87200 -18.49000 15.64800  1.000 48.77497  ? 34  ASP A HB2  1 
ATOM   514  H HB3  . ASP A 1 34  ? -28.89500 -19.49600 14.90400  1.000 48.77497  ? 34  ASP A HB3  1 
ATOM   515  N N    . VAL A 1 35  ? -27.08800 -16.56100 17.67900  1.000 35.55353  ? 35  VAL A N    1 
ATOM   516  C CA   . VAL A 1 35  ? -27.23400 -15.67900 18.83100  1.000 35.05191  ? 35  VAL A CA   1 
ATOM   517  C C    . VAL A 1 35  ? -26.46000 -14.39800 18.55700  1.000 35.39396  ? 35  VAL A C    1 
ATOM   518  O O    . VAL A 1 35  ? -25.32800 -14.43600 18.04300  1.000 31.43504  ? 35  VAL A O    1 
ATOM   519  C CB   . VAL A 1 35  ? -26.72900 -16.35300 20.11700  1.000 33.02989  ? 35  VAL A CB   1 
ATOM   520  C CG1  . VAL A 1 35  ? -26.84900 -15.39000 21.33300  1.000 33.31805  ? 35  VAL A CG1  1 
ATOM   521  C CG2  . VAL A 1 35  ? -27.53900 -17.64500 20.38000  1.000 35.87346  ? 35  VAL A CG2  1 
ATOM   522  H H    . VAL A 1 35  ? -26.27100 -16.70800 17.45300  1.000 42.66504  ? 35  VAL A H    1 
ATOM   523  H HA   . VAL A 1 35  ? -28.16800 -15.45000 18.95400  1.000 42.06310  ? 35  VAL A HA   1 
ATOM   524  H HB   . VAL A 1 35  ? -25.79600 -16.59400 20.00900  1.000 39.63667  ? 35  VAL A HB   1 
ATOM   525  H HG11 . VAL A 1 35  ? -26.67400 -15.88900 22.14700  1.000 39.98247  ? 35  VAL A HG11 1 
ATOM   526  H HG12 . VAL A 1 35  ? -26.20000 -14.67500 21.23900  1.000 39.98247  ? 35  VAL A HG12 1 
ATOM   527  H HG13 . VAL A 1 35  ? -27.74700 -15.02300 21.35700  1.000 39.98247  ? 35  VAL A HG13 1 
ATOM   528  H HG21 . VAL A 1 35  ? -27.24600 -18.03500 21.21800  1.000 43.04896  ? 35  VAL A HG21 1 
ATOM   529  H HG22 . VAL A 1 35  ? -28.48100 -17.42100 20.43100  1.000 43.04896  ? 35  VAL A HG22 1 
ATOM   530  H HG23 . VAL A 1 35  ? -27.38500 -18.26800 19.65300  1.000 43.04896  ? 35  VAL A HG23 1 
ATOM   531  N N    . VAL A 1 36  ? -27.05700 -13.26200 18.92700  1.000 31.56214  ? 36  VAL A N    1 
ATOM   532  C CA   . VAL A 1 36  ? -26.37800 -11.97000 18.87000  1.000 29.45266  ? 36  VAL A CA   1 
ATOM   533  C C    . VAL A 1 36  ? -26.13200 -11.54000 20.30900  1.000 31.11673  ? 36  VAL A C    1 
ATOM   534  O O    . VAL A 1 36  ? -27.08300 -11.42400 21.08700  1.000 32.06281  ? 36  VAL A O    1 
ATOM   535  C CB   . VAL A 1 36  ? -27.20300 -10.93400 18.09200  1.000 30.30105  ? 36  VAL A CB   1 
ATOM   536  C CG1  . VAL A 1 36  ? -26.54700 -9.54800  18.21000  1.000 32.03529  ? 36  VAL A CG1  1 
ATOM   537  C CG2  . VAL A 1 36  ? -27.31100 -11.34800 16.58300  1.000 31.85486  ? 36  VAL A CG2  1 
ATOM   538  H H    . VAL A 1 36  ? -27.86500 -13.21600 19.21800  1.000 37.87537  ? 36  VAL A H    1 
ATOM   539  H HA   . VAL A 1 36  ? -25.52000 -12.07100 18.42900  1.000 35.34399  ? 36  VAL A HA   1 
ATOM   540  H HB   . VAL A 1 36  ? -28.09700 -10.88500 18.46300  1.000 36.36206  ? 36  VAL A HB   1 
ATOM   541  H HG11 . VAL A 1 36  ? -26.93400 -8.96000  17.54300  1.000 38.44315  ? 36  VAL A HG11 1 
ATOM   542  H HG12 . VAL A 1 36  ? -26.71100 -9.19200  19.09700  1.000 38.44315  ? 36  VAL A HG12 1 
ATOM   543  H HG13 . VAL A 1 36  ? -25.59300 -9.63700  18.05800  1.000 38.44315  ? 36  VAL A HG13 1 
ATOM   544  H HG21 . VAL A 1 36  ? -27.84700 -10.69000 16.11300  1.000 38.22663  ? 36  VAL A HG21 1 
ATOM   545  H HG22 . VAL A 1 36  ? -26.42000 -11.38300 16.20100  1.000 38.22663  ? 36  VAL A HG22 1 
ATOM   546  H HG23 . VAL A 1 36  ? -27.73100 -12.22000 16.52500  1.000 38.22663  ? 36  VAL A HG23 1 
ATOM   547  N N    . TYR A 1 37  ? -24.85400 -11.31500 20.68100  1.000 30.70247  ? 37  TYR A N    1 
ATOM   548  C CA   . TYR A 1 37  ? -24.48700 -10.91900 22.04400  1.000 29.21048  ? 37  TYR A CA   1 
ATOM   549  C C    . TYR A 1 37  ? -24.28500 -9.41200  22.06700  1.000 28.61306  ? 37  TYR A C    1 
ATOM   550  O O    . TYR A 1 37  ? -23.60900 -8.89100  21.19000  1.000 27.95921  ? 37  TYR A O    1 
ATOM   551  C CB   . TYR A 1 37  ? -23.18900 -11.60500 22.49500  1.000 27.27688  ? 37  TYR A CB   1 
ATOM   552  C CG   . TYR A 1 37  ? -23.32200 -13.10900 22.51200  1.000 29.93893  ? 37  TYR A CG   1 
ATOM   553  C CD1  . TYR A 1 37  ? -23.26100 -13.83600 21.31000  1.000 28.15314  ? 37  TYR A CD1  1 
ATOM   554  C CD2  . TYR A 1 37  ? -23.48800 -13.81300 23.71500  1.000 30.36933  ? 37  TYR A CD2  1 
ATOM   555  C CE1  . TYR A 1 37  ? -23.38900 -15.21600 21.29600  1.000 29.30431  ? 37  TYR A CE1  1 
ATOM   556  C CE2  . TYR A 1 37  ? -23.61700 -15.22100 23.71300  1.000 30.63646  ? 37  TYR A CE2  1 
ATOM   557  C CZ   . TYR A 1 37  ? -23.55800 -15.89700 22.50200  1.000 34.40556  ? 37  TYR A CZ   1 
ATOM   558  O OH   . TYR A 1 37  ? -23.70600 -17.27300 22.42800  1.000 33.55355  ? 37  TYR A OH   1 
ATOM   559  H H    . TYR A 1 37  ? -24.18100 -11.38800 20.15100  1.000 36.84376  ? 37  TYR A H    1 
ATOM   560  H HA   . TYR A 1 37  ? -25.19800 -11.15200 22.66100  1.000 35.05337  ? 37  TYR A HA   1 
ATOM   561  H HB2  . TYR A 1 37  ? -22.47500 -11.37100 21.88100  1.000 32.73306  ? 37  TYR A HB2  1 
ATOM   562  H HB3  . TYR A 1 37  ? -22.96800 -11.31100 23.39200  1.000 32.73306  ? 37  TYR A HB3  1 
ATOM   563  H HD1  . TYR A 1 37  ? -23.15200 -13.38000 20.50700  1.000 33.78457  ? 37  TYR A HD1  1 
ATOM   564  H HD2  . TYR A 1 37  ? -23.52800 -13.34800 24.51900  1.000 36.44400  ? 37  TYR A HD2  1 
ATOM   565  H HE1  . TYR A 1 37  ? -23.35800 -15.68300 20.49200  1.000 35.16598  ? 37  TYR A HE1  1 
ATOM   566  H HE2  . TYR A 1 37  ? -23.73800 -15.68600 24.50900  1.000 36.76455  ? 37  TYR A HE2  1 
ATOM   567  H HH   . TYR A 1 37  ? -23.80100 -17.59400 23.19900  1.000 40.26507  ? 37  TYR A HH   1 
ATOM   568  N N    . CYS A 1 38  ? -24.83400 -8.70200  23.05700  1.000 27.10151  ? 38  CYS A N    1 
ATOM   569  C CA   . CYS A 1 38  ? -24.53800 -7.26900  23.09000  1.000 26.67258  ? 38  CYS A CA   1 
ATOM   570  C C    . CYS A 1 38  ? -24.76400 -6.76600  24.49700  1.000 29.25086  ? 38  CYS A C    1 
ATOM   571  O O    . CYS A 1 38  ? -25.28800 -7.48900  25.35000  1.000 25.74291  ? 38  CYS A O    1 
ATOM   572  C CB   . CYS A 1 38  ? -25.40300 -6.48200  22.08800  1.000 28.83351  ? 38  CYS A CB   1 
ATOM   573  S SG   . CYS A 1 38  ? -27.16400 -6.39000  22.60600  1.000 30.39324  ? 38  CYS A SG   1 
ATOM   574  H H    . CYS A 1 38  ? -25.34600 -9.00100  23.68000  1.000 32.52262  ? 38  CYS A H    1 
ATOM   575  H HA   . CYS A 1 38  ? -23.60600 -7.14100  22.85800  1.000 32.00789  ? 38  CYS A HA   1 
ATOM   576  H HB2  . CYS A 1 38  ? -25.06300 -5.57700  22.01400  1.000 34.60101  ? 38  CYS A HB2  1 
ATOM   577  H HB3  . CYS A 1 38  ? -25.36700 -6.92200  21.22400  1.000 34.60101  ? 38  CYS A HB3  1 
ATOM   578  H HG   . CYS A 1 38  ? -27.77500 -5.74600  21.79900  1.000 36.47269  ? 38  CYS A HG   1 
ATOM   579  N N    . PRO A 1 39  ? -24.31300 -5.55900  24.79400  1.000 27.81099  ? 39  PRO A N    1 
ATOM   580  C CA   . PRO A 1 39  ? -24.44900 -5.06400  26.16900  1.000 26.87892  ? 39  PRO A CA   1 
ATOM   581  C C    . PRO A 1 39  ? -25.91100 -4.83000  26.45900  1.000 24.02526  ? 39  PRO A C    1 
ATOM   582  O O    . PRO A 1 39  ? -26.66400 -4.37400  25.58900  1.000 26.14666  ? 39  PRO A O    1 
ATOM   583  C CB   . PRO A 1 39  ? -23.65300 -3.75200  26.15500  1.000 24.51405  ? 39  PRO A CB   1 
ATOM   584  C CG   . PRO A 1 39  ? -22.63800 -3.99700  25.05400  1.000 25.59313  ? 39  PRO A CG   1 
ATOM   585  C CD   . PRO A 1 39  ? -23.39000 -4.73400  23.99300  1.000 24.51908  ? 39  PRO A CD   1 
ATOM   586  H HA   . PRO A 1 39  ? -24.06900 -5.68600  26.80900  1.000 32.25550  ? 39  PRO A HA   1 
ATOM   587  H HB2  . PRO A 1 39  ? -24.23900 -3.01300  25.93100  1.000 29.41766  ? 39  PRO A HB2  1 
ATOM   588  H HB3  . PRO A 1 39  ? -23.22000 -3.60900  27.00900  1.000 29.41766  ? 39  PRO A HB3  1 
ATOM   589  H HG2  . PRO A 1 39  ? -22.31000 -3.14900  24.71600  1.000 30.71256  ? 39  PRO A HG2  1 
ATOM   590  H HG3  . PRO A 1 39  ? -21.90800 -4.53700  25.39600  1.000 30.71256  ? 39  PRO A HG3  1 
ATOM   591  H HD2  . PRO A 1 39  ? -23.88300 -4.11500  23.43200  1.000 29.42370  ? 39  PRO A HD2  1 
ATOM   592  H HD3  . PRO A 1 39  ? -22.78000 -5.28300  23.47700  1.000 29.42370  ? 39  PRO A HD3  1 
ATOM   593  N N    . ARG A 1 40  ? -26.33300 -5.19300  27.66400  1.000 24.02035  ? 40  ARG A N    1 
ATOM   594  C CA   . ARG A 1 40  ? -27.76000 -5.03600  27.97100  1.000 27.62778  ? 40  ARG A CA   1 
ATOM   595  C C    . ARG A 1 40  ? -28.17700 -3.57300  28.09200  1.000 26.74325  ? 40  ARG A C    1 
ATOM   596  O O    . ARG A 1 40  ? -29.35700 -3.28300  27.93300  1.000 29.66632  ? 40  ARG A O    1 
ATOM   597  C CB   . ARG A 1 40  ? -28.14300 -5.79600  29.24700  1.000 24.73919  ? 40  ARG A CB   1 
ATOM   598  C CG   . ARG A 1 40  ? -27.45700 -5.31600  30.52600  1.000 27.56295  ? 40  ARG A CG   1 
ATOM   599  C CD   . ARG A 1 40  ? -27.96800 -6.09500  31.73400  1.000 27.23842  ? 40  ARG A CD   1 
ATOM   600  N NE   . ARG A 1 40  ? -27.29700 -5.61400  32.94800  1.000 27.72674  ? 40  ARG A NE   1 
ATOM   601  C CZ   . ARG A 1 40  ? -27.63600 -5.98200  34.17600  1.000 31.36426  ? 40  ARG A CZ   1 
ATOM   602  N NH1  . ARG A 1 40  ? -28.55300 -6.91400  34.38700  1.000 30.34354  ? 40  ARG A NH1  1 
ATOM   603  N NH2  . ARG A 1 40  ? -27.07200 -5.37300  35.21000  1.000 28.88837  ? 40  ARG A NH2  1 
ATOM   604  H H    . ARG A 1 40  ? -25.84700 -5.51700  28.29500  1.000 28.82522  ? 40  ARG A H    1 
ATOM   605  H HA   . ARG A 1 40  ? -28.27100 -5.42100  27.24200  1.000 33.15414  ? 40  ARG A HA   1 
ATOM   606  H HB2  . ARG A 1 40  ? -29.10000 -5.71000  29.38000  1.000 29.68783  ? 40  ARG A HB2  1 
ATOM   607  H HB3  . ARG A 1 40  ? -27.91500 -6.73100  29.12800  1.000 29.68783  ? 40  ARG A HB3  1 
ATOM   608  H HG2  . ARG A 1 40  ? -26.50000 -5.45600  30.45300  1.000 33.07634  ? 40  ARG A HG2  1 
ATOM   609  H HG3  . ARG A 1 40  ? -27.65200 -4.37600  30.66500  1.000 33.07634  ? 40  ARG A HG3  1 
ATOM   610  H HD2  . ARG A 1 40  ? -28.92300 -5.95500  31.83200  1.000 32.68690  ? 40  ARG A HD2  1 
ATOM   611  H HD3  . ARG A 1 40  ? -27.77100 -7.03800  31.62200  1.000 32.68690  ? 40  ARG A HD3  1 
ATOM   612  H HE   . ARG A 1 40  ? -26.59300 -5.12900  32.85300  1.000 33.27289  ? 40  ARG A HE   1 
ATOM   613  H HH11 . ARG A 1 40  ? -28.93200 -7.30700  33.72200  1.000 36.41305  ? 40  ARG A HH11 1 
ATOM   614  H HH12 . ARG A 1 40  ? -28.76100 -7.13700  35.19100  1.000 36.41305  ? 40  ARG A HH12 1 
ATOM   615  H HH21 . ARG A 1 40  ? -26.47600 -4.76700  35.07900  1.000 34.66684  ? 40  ARG A HH21 1 
ATOM   616  H HH22 . ARG A 1 40  ? -27.28000 -5.60500  36.01100  1.000 34.66684  ? 40  ARG A HH22 1 
ATOM   617  N N    . ALA A 1 41  ? -27.23600 -2.64700  28.24400  1.000 27.92439  ? 41  ALA A N    1 
ATOM   618  C CA   . ALA A 1 41  ? -27.58100 -1.23000  28.27000  1.000 28.91859  ? 41  ALA A CA   1 
ATOM   619  C C    . ALA A 1 41  ? -28.21700 -0.73500  26.97500  1.000 29.79010  ? 41  ALA A C    1 
ATOM   620  O O    . ALA A 1 41  ? -28.72300 0.39300   26.94100  1.000 33.25815  ? 41  ALA A O    1 
ATOM   621  C CB   . ALA A 1 41  ? -26.33700 -0.41700  28.60300  1.000 31.64928  ? 41  ALA A CB   1 
ATOM   622  H H    . ALA A 1 41  ? -26.39700 -2.81200  28.33400  1.000 33.51007  ? 41  ALA A H    1 
ATOM   623  H HA   . ALA A 1 41  ? -28.22000 -1.08700  28.98300  1.000 34.70311  ? 41  ALA A HA   1 
ATOM   624  H HB1  . ALA A 1 41  ? -26.43700 0.46000   28.21700  1.000 37.97994  ? 41  ALA A HB1  1 
ATOM   625  H HB2  . ALA A 1 41  ? -26.27500 -0.33700  29.56800  1.000 37.97994  ? 41  ALA A HB2  1 
ATOM   626  H HB3  . ALA A 1 41  ? -25.57500 -0.89800  28.27600  1.000 37.97994  ? 41  ALA A HB3  1 
ATOM   627  N N    . VAL A 1 42  ? -28.21800 -1.53600  25.90800  1.000 28.13194  ? 42  VAL A N    1 
ATOM   628  C CA   . VAL A 1 42  ? -28.98000 -1.12700  24.72100  1.000 31.74068  ? 42  VAL A CA   1 
ATOM   629  C C    . VAL A 1 42  ? -30.47000 -0.99000  25.03600  1.000 31.94706  ? 42  VAL A C    1 
ATOM   630  O O    . VAL A 1 42  ? -31.16900 -0.25400  24.34500  1.000 35.37565  ? 42  VAL A O    1 
ATOM   631  C CB   . VAL A 1 42  ? -28.74300 -2.10800  23.54900  1.000 29.84827  ? 42  VAL A CB   1 
ATOM   632  C CG1  . VAL A 1 42  ? -29.54700 -3.38400  23.79000  1.000 29.44786  ? 42  VAL A CG1  1 
ATOM   633  C CG2  . VAL A 1 42  ? -29.12200 -1.44400  22.17600  1.000 33.45613  ? 42  VAL A CG2  1 
ATOM   634  H H    . VAL A 1 42  ? -27.80600 -2.28800  25.84200  1.000 33.75913  ? 42  VAL A H    1 
ATOM   635  H HA   . VAL A 1 42  ? -28.66200 -0.25500  24.43900  1.000 38.08962  ? 42  VAL A HA   1 
ATOM   636  H HB   . VAL A 1 42  ? -27.80500 -2.34700  23.52100  1.000 35.81873  ? 42  VAL A HB   1 
ATOM   637  H HG11 . VAL A 1 42  ? -29.17900 -4.09600  23.24400  1.000 35.33823  ? 42  VAL A HG11 1 
ATOM   638  H HG12 . VAL A 1 42  ? -29.48600 -3.62200  24.72800  1.000 35.33823  ? 42  VAL A HG12 1 
ATOM   639  H HG13 . VAL A 1 42  ? -30.47300 -3.22700  23.54800  1.000 35.33823  ? 42  VAL A HG13 1 
ATOM   640  H HG21 . VAL A 1 42  ? -28.94900 -2.07700  21.46100  1.000 40.14815  ? 42  VAL A HG21 1 
ATOM   641  H HG22 . VAL A 1 42  ? -30.06200 -1.20800  22.18900  1.000 40.14815  ? 42  VAL A HG22 1 
ATOM   642  H HG23 . VAL A 1 42  ? -28.58200 -0.64800  22.05100  1.000 40.14815  ? 42  VAL A HG23 1 
ATOM   643  N N    . ILE A 1 43  ? -30.99400 -1.64500  26.09500  1.000 30.91901  ? 43  ILE A N    1 
ATOM   644  C CA   . ILE A 1 43  ? -32.41500 -1.49900  26.40100  1.000 34.83235  ? 43  ILE A CA   1 
ATOM   645  C C    . ILE A 1 43  ? -32.70200 -0.31200  27.32200  1.000 41.44454  ? 43  ILE A C    1 
ATOM   646  O O    . ILE A 1 43  ? -33.86400 -0.10200  27.68500  1.000 39.05009  ? 43  ILE A O    1 
ATOM   647  C CB   . ILE A 1 43  ? -33.01800 -2.77500  27.01400  1.000 36.07886  ? 43  ILE A CB   1 
ATOM   648  C CG1  . ILE A 1 43  ? -32.54400 -2.98400  28.44600  1.000 29.54233  ? 43  ILE A CG1  1 
ATOM   649  C CG2  . ILE A 1 43  ? -32.65600 -3.99600  26.15000  1.000 38.73641  ? 43  ILE A CG2  1 
ATOM   650  C CD1  . ILE A 1 43  ? -33.21400 -4.16400  29.06000  1.000 35.27620  ? 43  ILE A CD1  1 
ATOM   651  H H    . ILE A 1 43  ? -30.55700 -2.16000  26.62800  1.000 37.10361  ? 43  ILE A H    1 
ATOM   652  H HA   . ILE A 1 43  ? -32.88900 -1.33600  25.57100  1.000 41.79962  ? 43  ILE A HA   1 
ATOM   653  H HB   . ILE A 1 43  ? -33.98400 -2.68200  27.02200  1.000 43.29543  ? 43  ILE A HB   1 
ATOM   654  H HG12 . ILE A 1 43  ? -31.58900 -3.14000  28.45200  1.000 35.45160  ? 43  ILE A HG12 1 
ATOM   655  H HG13 . ILE A 1 43  ? -32.76300 -2.21200  28.99000  1.000 35.45160  ? 43  ILE A HG13 1 
ATOM   656  H HG21 . ILE A 1 43  ? -33.22000 -4.74300  26.40200  1.000 46.48450  ? 43  ILE A HG21 1 
ATOM   657  H HG22 . ILE A 1 43  ? -32.80100 -3.77400  25.21700  1.000 46.48450  ? 43  ILE A HG22 1 
ATOM   658  H HG23 . ILE A 1 43  ? -31.72300 -4.21900  26.29500  1.000 46.48450  ? 43  ILE A HG23 1 
ATOM   659  H HD11 . ILE A 1 43  ? -33.06300 -4.14900  30.01800  1.000 42.33224  ? 43  ILE A HD11 1 
ATOM   660  H HD12 . ILE A 1 43  ? -34.16500 -4.11800  28.87500  1.000 42.33224  ? 43  ILE A HD12 1 
ATOM   661  H HD13 . ILE A 1 43  ? -32.84200 -4.97500  28.68000  1.000 42.33224  ? 43  ILE A HD13 1 
ATOM   662  N N    . CYS A 1 44  ? -31.67800 0.38500   27.81700  1.000 36.66427  ? 44  CYS A N    1 
ATOM   663  C CA   . CYS A 1 44  ? -31.92400 1.54400   28.67600  1.000 46.52467  ? 44  CYS A CA   1 
ATOM   664  C C    . CYS A 1 44  ? -32.49200 2.72000   27.90000  1.000 51.58287  ? 44  CYS A C    1 
ATOM   665  O O    . CYS A 1 44  ? -32.14200 2.95400   26.75300  1.000 57.00462  ? 44  CYS A O    1 
ATOM   666  C CB   . CYS A 1 44  ? -30.64900 2.01700   29.32900  1.000 49.10258  ? 44  CYS A CB   1 
ATOM   667  S SG   . CYS A 1 44  ? -30.00100 0.84600   30.44200  1.000 46.19666  ? 44  CYS A SG   1 
ATOM   668  H H    . CYS A 1 44  ? -30.84800 0.21300   27.67500  1.000 43.99792  ? 44  CYS A H    1 
ATOM   669  H HA   . CYS A 1 44  ? -32.55400 1.30200   29.37200  1.000 55.83041  ? 44  CYS A HA   1 
ATOM   670  H HB2  . CYS A 1 44  ? -29.98300 2.18100   28.64300  1.000 58.92390  ? 44  CYS A HB2  1 
ATOM   671  H HB3  . CYS A 1 44  ? -30.82900 2.83300   29.82100  1.000 58.92390  ? 44  CYS A HB3  1 
ATOM   672  H HG   . CYS A 1 44  ? -29.97400 -0.17200  29.81300  1.000 55.43679  ? 44  CYS A HG   1 
ATOM   673  N N    . THR A 1 45  ? -33.29300 3.52500   28.57200  1.000 66.37159  ? 45  THR A N    1 
ATOM   674  C CA   . THR A 1 45  ? -33.66600 4.81500   28.01000  1.000 71.15503  ? 45  THR A CA   1 
ATOM   675  C C    . THR A 1 45  ? -32.64900 5.87600   28.43700  1.000 77.51688  ? 45  THR A C    1 
ATOM   676  O O    . THR A 1 45  ? -32.00600 5.76200   29.48800  1.000 74.47447  ? 45  THR A O    1 
ATOM   677  C CB   . THR A 1 45  ? -35.07100 5.19900   28.46600  1.000 71.09968  ? 45  THR A CB   1 
ATOM   678  O OG1  . THR A 1 45  ? -35.02800 5.55300   29.85000  1.000 71.95040  ? 45  THR A OG1  1 
ATOM   679  C CG2  . THR A 1 45  ? -36.00500 4.00800   28.29600  1.000 67.16439  ? 45  THR A CG2  1 
ATOM   680  H H    . THR A 1 45  ? -33.63200 3.35500   29.34400  1.000 79.64671  ? 45  THR A H    1 
ATOM   681  H HA   . THR A 1 45  ? -33.66500 4.76200   27.04200  1.000 85.38683  ? 45  THR A HA   1 
ATOM   682  H HB   . THR A 1 45  ? -35.40300 5.94300   27.94000  1.000 85.32042  ? 45  THR A HB   1 
ATOM   683  H HG1  . THR A 1 45  ? -34.74500 4.90500   30.30200  1.000 86.34128  ? 45  THR A HG1  1 
ATOM   684  H HG21 . THR A 1 45  ? -36.92700 4.29600   28.38200  1.000 80.59807  ? 45  THR A HG21 1 
ATOM   685  H HG22 . THR A 1 45  ? -35.87900 3.61100   27.42000  1.000 80.59807  ? 45  THR A HG22 1 
ATOM   686  H HG23 . THR A 1 45  ? -35.82000 3.33900   28.97400  1.000 80.59807  ? 45  THR A HG23 1 
ATOM   687  N N    . SER A 1 46  ? -32.49700 6.91300   27.60300  1.000 93.89163  ? 46  SER A N    1 
ATOM   688  C CA   . SER A 1 46  ? -31.58700 8.00900   27.94200  1.000 95.44841  ? 46  SER A CA   1 
ATOM   689  C C    . SER A 1 46  ? -31.88300 8.58800   29.32300  1.000 98.24762  ? 46  SER A C    1 
ATOM   690  O O    . SER A 1 46  ? -30.96700 9.05100   30.01700  1.000 98.32407  ? 46  SER A O    1 
ATOM   691  C CB   . SER A 1 46  ? -31.67400 9.11200   26.88200  1.000 95.64569  ? 46  SER A CB   1 
ATOM   692  O OG   . SER A 1 46  ? -32.99100 9.63900   26.79700  1.000 95.48249  ? 46  SER A OG   1 
ATOM   693  H H    . SER A 1 46  ? -32.90200 7.00300   26.85000  1.000 112.67075 ? 46  SER A H    1 
ATOM   694  H HA   . SER A 1 46  ? -30.68700 7.69300   27.95800  1.000 114.53889 ? 46  SER A HA   1 
ATOM   695  H HB2  . SER A 1 46  ? -31.06400 9.82700   27.12100  1.000 114.77562 ? 46  SER A HB2  1 
ATOM   696  H HB3  . SER A 1 46  ? -31.42700 8.74100   26.02000  1.000 114.77562 ? 46  SER A HB3  1 
ATOM   697  H HG   . SER A 1 46  ? -33.02200 10.24200  26.21300  1.000 114.57979 ? 46  SER A HG   1 
ATOM   698  N N    . GLU A 1 47  ? -33.15200 8.57500   29.73600  1.000 85.75189  ? 47  GLU A N    1 
ATOM   699  C CA   . GLU A 1 47  ? -33.52700 9.10900   31.04000  1.000 81.00339  ? 47  GLU A CA   1 
ATOM   700  C C    . GLU A 1 47  ? -32.90000 8.29100   32.16100  1.000 78.60020  ? 47  GLU A C    1 
ATOM   701  O O    . GLU A 1 47  ? -32.14500 8.81800   32.98800  1.000 86.33639  ? 47  GLU A O    1 
ATOM   702  C CB   . GLU A 1 47  ? -35.05500 9.12800   31.18900  1.000 82.43166  ? 47  GLU A CB   1 
ATOM   703  C CG   . GLU A 1 47  ? -35.83900 9.72000   30.01300  1.000 90.93581  ? 47  GLU A CG   1 
ATOM   704  C CD   . GLU A 1 47  ? -35.83400 11.24900  29.97700  1.000 95.05217  ? 47  GLU A CD   1 
ATOM   705  O OE1  . GLU A 1 47  ? -34.74100 11.84200  29.82800  1.000 99.71100  ? 47  GLU A OE1  1 
ATOM   706  O OE2  . GLU A 1 47  ? -36.92500 11.85900  30.09400  1.000 84.13401  ? 47  GLU A OE2  1 
ATOM   707  H H    . GLU A 1 47  ? -33.80800 8.25700   29.28100  1.000 102.90307 ? 47  GLU A H    1 
ATOM   708  H HA   . GLU A 1 47  ? -33.20500 10.02100  31.11500  1.000 97.20487  ? 47  GLU A HA   1 
ATOM   709  H HB2  . GLU A 1 47  ? -35.36100 8.21600   31.31000  1.000 98.91879  ? 47  GLU A HB2  1 
ATOM   710  H HB3  . GLU A 1 47  ? -35.27800 9.64900   31.97600  1.000 98.91879  ? 47  GLU A HB3  1 
ATOM   711  H HG2  . GLU A 1 47  ? -35.46100 9.40300   29.17900  1.000 109.12377 ? 47  GLU A HG2  1 
ATOM   712  H HG3  . GLU A 1 47  ? -36.76300 9.43200   30.08200  1.000 109.12377 ? 47  GLU A HG3  1 
ATOM   713  N N    . ASP A 1 48  ? -33.19300 6.99000   32.20000  1.000 76.29522  ? 48  ASP A N    1 
ATOM   714  C CA   . ASP A 1 48  ? -32.82800 6.15700   33.34000  1.000 74.25091  ? 48  ASP A CA   1 
ATOM   715  C C    . ASP A 1 48  ? -31.58300 5.33000   33.02000  1.000 69.00179  ? 48  ASP A C    1 
ATOM   716  O O    . ASP A 1 48  ? -31.65300 4.14000   32.69900  1.000 67.24333  ? 48  ASP A O    1 
ATOM   717  C CB   . ASP A 1 48  ? -34.02100 5.28500   33.77700  1.000 83.54937  ? 48  ASP A CB   1 
ATOM   718  C CG   . ASP A 1 48  ? -34.40800 4.18700   32.75200  1.000 87.41401  ? 48  ASP A CG   1 
ATOM   719  O OD1  . ASP A 1 48  ? -33.70000 3.97100   31.73100  1.000 76.34507  ? 48  ASP A OD1  1 
ATOM   720  O OD2  . ASP A 1 48  ? -35.44200 3.51400   32.99900  1.000 79.02005  ? 48  ASP A OD2  1 
ATOM   721  H H    . ASP A 1 48  ? -33.60500 6.56700   31.57500  1.000 91.55507  ? 48  ASP A H    1 
ATOM   722  H HA   . ASP A 1 48  ? -32.62200 6.75900   34.06100  1.000 89.10189  ? 48  ASP A HA   1 
ATOM   723  H HB2  . ASP A 1 48  ? -33.75300 4.84000   34.58900  1.000 100.26004 ? 48  ASP A HB2  1 
ATOM   724  H HB3  . ASP A 1 48  ? -34.79500 5.84800   33.93600  1.000 100.26004 ? 48  ASP A HB3  1 
ATOM   725  N N    A MET A 1 49  ? -30.41800 5.97200   33.13200  0.510 55.82651  ? 49  MET A N    1 
ATOM   726  N N    B MET A 1 49  ? -30.41900 5.98900   33.10200  0.490 55.81846  ? 49  MET A N    1 
ATOM   727  C CA   A MET A 1 49  ? -29.15800 5.25600   33.05100  0.510 49.48462  ? 49  MET A CA   1 
ATOM   728  C CA   B MET A 1 49  ? -29.13500 5.31100   33.01800  0.490 49.35232  ? 49  MET A CA   1 
ATOM   729  C C    A MET A 1 49  ? -28.40000 5.26900   34.37300  0.510 39.53479  ? 49  MET A C    1 
ATOM   730  C C    B MET A 1 49  ? -28.40200 5.27600   34.36100  0.490 40.12573  ? 49  MET A C    1 
ATOM   731  O O    A MET A 1 49  ? -27.32700 4.67500   34.45700  0.510 38.40526  ? 49  MET A O    1 
ATOM   732  O O    B MET A 1 49  ? -27.34400 4.65500   34.44900  0.490 38.15699  ? 49  MET A O    1 
ATOM   733  C CB   A MET A 1 49  ? -28.29900 5.82500   31.91900  0.510 49.81694  ? 49  MET A CB   1 
ATOM   734  C CB   B MET A 1 49  ? -28.24500 5.95600   31.93500  0.490 49.81960  ? 49  MET A CB   1 
ATOM   735  C CG   A MET A 1 49  ? -29.10000 5.99900   30.63100  0.510 53.86333  ? 49  MET A CG   1 
ATOM   736  C CG   B MET A 1 49  ? -28.83500 5.94700   30.49600  0.490 53.46988  ? 49  MET A CG   1 
ATOM   737  S SD   A MET A 1 49  ? -28.63000 4.82500   29.36700  0.510 51.45554  ? 49  MET A SD   1 
ATOM   738  S SD   B MET A 1 49  ? -27.97400 7.04000   29.30700  0.490 55.57409  ? 49  MET A SD   1 
ATOM   739  C CE   A MET A 1 49  ? -27.18400 5.67900   28.72000  0.510 42.99802  ? 49  MET A CE   1 
ATOM   740  C CE   B MET A 1 49  ? -28.64500 6.45900   27.74400  0.490 58.13242  ? 49  MET A CE   1 
ATOM   741  H H    A MET A 1 49  ? -30.33700 6.81900   33.25500  0.510 66.99261  ? 49  MET A H    1 
ATOM   742  H H    B MET A 1 49  ? -30.35400 6.84000   33.20800  0.490 66.98295  ? 49  MET A H    1 
ATOM   743  H HA   A MET A 1 49  ? -29.34300 4.33200   32.82500  0.510 59.38235  ? 49  MET A HA   1 
ATOM   744  H HA   B MET A 1 49  ? -29.29300 4.39500   32.74200  0.490 59.22359  ? 49  MET A HA   1 
ATOM   745  H HB2  A MET A 1 49  ? -27.95800 6.69400   32.18300  0.510 59.78113  ? 49  MET A HB2  1 
ATOM   746  H HB2  B MET A 1 49  ? -28.08600 6.88100   32.17900  0.490 59.78432  ? 49  MET A HB2  1 
ATOM   747  H HB3  A MET A 1 49  ? -27.56500 5.21700   31.73900  0.510 59.78113  ? 49  MET A HB3  1 
ATOM   748  H HB3  B MET A 1 49  ? -27.40100 5.47900   31.90700  0.490 59.78432  ? 49  MET A HB3  1 
ATOM   749  H HG2  A MET A 1 49  ? -30.04300 5.87400   30.80400  0.510 64.63680  ? 49  MET A HG2  1 
ATOM   750  H HG2  B MET A 1 49  ? -28.79000 5.04200   30.14900  0.490 64.16466  ? 49  MET A HG2  1 
ATOM   751  H HG3  A MET A 1 49  ? -28.94400 6.89100   30.28200  0.510 64.63680  ? 49  MET A HG3  1 
ATOM   752  H HG3  B MET A 1 49  ? -29.76100 6.23300   30.53900  0.490 64.16466  ? 49  MET A HG3  1 
ATOM   753  H HE1  A MET A 1 49  ? -26.80300 5.15700   27.99700  0.510 51.59842  ? 49  MET A HE1  1 
ATOM   754  H HE1  B MET A 1 49  ? -28.78800 7.21700   27.15600  0.490 69.75970  ? 49  MET A HE1  1 
ATOM   755  H HE2  A MET A 1 49  ? -27.45700 6.54900   28.38900  0.510 51.59842  ? 49  MET A HE2  1 
ATOM   756  H HE2  B MET A 1 49  ? -28.00500 5.85200   27.34000  0.490 69.75970  ? 49  MET A HE2  1 
ATOM   757  H HE3  A MET A 1 49  ? -26.53500 5.78800   29.43200  0.510 51.59842  ? 49  MET A HE3  1 
ATOM   758  H HE3  B MET A 1 49  ? -29.47800 5.99000   27.90800  0.490 69.75970  ? 49  MET A HE3  1 
ATOM   759  N N    . LEU A 1 50  ? -28.94700 5.89300   35.41700  1.000 36.05375  ? 50  LEU A N    1 
ATOM   760  C CA   . LEU A 1 50  ? -28.27400 5.83900   36.71700  1.000 34.74389  ? 50  LEU A CA   1 
ATOM   761  C C    . LEU A 1 50  ? -28.59400 4.55400   37.47300  1.000 36.36327  ? 50  LEU A C    1 
ATOM   762  O O    . LEU A 1 50  ? -27.72200 3.97900   38.14900  1.000 32.10005  ? 50  LEU A O    1 
ATOM   763  C CB   . LEU A 1 50  ? -28.69200 7.04300   37.57800  1.000 41.25870  ? 50  LEU A CB   1 
ATOM   764  C CG   . LEU A 1 50  ? -27.89800 8.34300   37.43300  1.000 42.49345  ? 50  LEU A CG   1 
ATOM   765  C CD1  . LEU A 1 50  ? -28.41500 9.35200   38.44500  1.000 40.84263  ? 50  LEU A CD1  1 
ATOM   766  C CD2  . LEU A 1 50  ? -26.40500 8.09800   37.66700  1.000 38.69693  ? 50  LEU A CD2  1 
ATOM   767  H H    A LEU A 1 50  ? -29.68100 6.34000   35.40400  0.510 43.26530  ? 50  LEU A H    1 
ATOM   768  H H    B LEU A 1 50  ? -29.68400 6.33700   35.40800  0.490 43.26530  ? 50  LEU A H    1 
ATOM   769  H HA   . LEU A 1 50  ? -27.31500 5.87300   36.58100  1.000 41.69347  ? 50  LEU A HA   1 
ATOM   770  H HB2  . LEU A 1 50  ? -29.61600 7.25200   37.37000  1.000 49.51124  ? 50  LEU A HB2  1 
ATOM   771  H HB3  . LEU A 1 50  ? -28.63000 6.77800   38.50900  1.000 49.51124  ? 50  LEU A HB3  1 
ATOM   772  H HG   . LEU A 1 50  ? -28.02000 8.70500   36.54100  1.000 50.99295  ? 50  LEU A HG   1 
ATOM   773  H HD11 . LEU A 1 50  ? -27.92000 10.18000  38.34600  1.000 49.01196  ? 50  LEU A HD11 1 
ATOM   774  H HD12 . LEU A 1 50  ? -29.35800 9.50900   38.28000  1.000 49.01196  ? 50  LEU A HD12 1 
ATOM   775  H HD13 . LEU A 1 50  ? -28.29000 8.99500   39.33800  1.000 49.01196  ? 50  LEU A HD13 1 
ATOM   776  H HD21 . LEU A 1 50  ? -25.96700 8.94900   37.82300  1.000 46.43712  ? 50  LEU A HD21 1 
ATOM   777  H HD22 . LEU A 1 50  ? -26.29800 7.52400   38.44100  1.000 46.43712  ? 50  LEU A HD22 1 
ATOM   778  H HD23 . LEU A 1 50  ? -26.02700 7.67000   36.88300  1.000 46.43712  ? 50  LEU A HD23 1 
ATOM   779  N N    . ASN A 1 51  ? -29.86500 4.16500   37.46800  1.000 34.77226  ? 51  ASN A N    1 
ATOM   780  C CA   . ASN A 1 51  ? -30.36200 3.01600   38.21800  1.000 33.93889  ? 51  ASN A CA   1 
ATOM   781  C C    . ASN A 1 51  ? -31.34600 2.19700   37.38400  1.000 32.16235  ? 51  ASN A C    1 
ATOM   782  O O    . ASN A 1 51  ? -32.43700 1.86700   37.84600  1.000 33.89884  ? 51  ASN A O    1 
ATOM   783  C CB   . ASN A 1 51  ? -30.99300 3.49700   39.51600  1.000 36.34150  ? 51  ASN A CB   1 
ATOM   784  C CG   . ASN A 1 51  ? -29.96000 4.13700   40.40200  1.000 32.18988  ? 51  ASN A CG   1 
ATOM   785  O OD1  . ASN A 1 51  ? -29.07300 3.44900   40.87200  1.000 31.75303  ? 51  ASN A OD1  1 
ATOM   786  N ND2  . ASN A 1 51  ? -30.00100 5.45900   40.54000  1.000 31.18594  ? 51  ASN A ND2  1 
ATOM   787  H H    . ASN A 1 51  ? -30.48000 4.56600   37.02100  1.000 41.72752  ? 51  ASN A H    1 
ATOM   788  H HA   . ASN A 1 51  ? -29.61500 2.44100   38.44500  1.000 40.72746  ? 51  ASN A HA   1 
ATOM   789  H HB2  . ASN A 1 51  ? -31.67800 4.15500   39.31800  1.000 43.61060  ? 51  ASN A HB2  1 
ATOM   790  H HB3  . ASN A 1 51  ? -31.37600 2.74100   39.98800  1.000 43.61060  ? 51  ASN A HB3  1 
ATOM   791  H HD21 . ASN A 1 51  ? -29.41900 5.85800   41.03100  1.000 37.42393  ? 51  ASN A HD21 1 
ATOM   792  H HD22 . ASN A 1 51  ? -30.63500 5.91000   40.17300  1.000 37.42393  ? 51  ASN A HD22 1 
ATOM   793  N N    . PRO A 1 52  ? -30.97000 1.79800   36.16800  1.000 34.43640  ? 52  PRO A N    1 
ATOM   794  C CA   . PRO A 1 52  ? -31.87900 0.95900   35.37100  1.000 40.99098  ? 52  PRO A CA   1 
ATOM   795  C C    . PRO A 1 52  ? -32.21800 -0.33700  36.11100  1.000 35.42945  ? 52  PRO A C    1 
ATOM   796  O O    . PRO A 1 52  ? -31.37200 -0.93900  36.77700  1.000 37.84702  ? 52  PRO A O    1 
ATOM   797  C CB   . PRO A 1 52  ? -31.09000 0.70000   34.08300  1.000 37.19433  ? 52  PRO A CB   1 
ATOM   798  C CG   . PRO A 1 52  ? -29.66700 0.99000   34.42000  1.000 42.32945  ? 52  PRO A CG   1 
ATOM   799  C CD   . PRO A 1 52  ? -29.68800 2.03800   35.51600  1.000 34.58950  ? 52  PRO A CD   1 
ATOM   800  H HA   . PRO A 1 52  ? -32.69500 1.44000   35.16300  1.000 49.18998  ? 52  PRO A HA   1 
ATOM   801  H HB2  . PRO A 1 52  ? -31.19600 -0.22700  33.81700  1.000 44.63399  ? 52  PRO A HB2  1 
ATOM   802  H HB3  . PRO A 1 52  ? -31.40400 1.29500   33.38400  1.000 44.63399  ? 52  PRO A HB3  1 
ATOM   803  H HG2  . PRO A 1 52  ? -29.23800 0.17900   34.73500  1.000 50.79614  ? 52  PRO A HG2  1 
ATOM   804  H HG3  . PRO A 1 52  ? -29.21200 1.33100   33.63400  1.000 50.79614  ? 52  PRO A HG3  1 
ATOM   805  H HD2  . PRO A 1 52  ? -28.95800 1.89600   36.13700  1.000 41.50820  ? 52  PRO A HD2  1 
ATOM   806  H HD3  . PRO A 1 52  ? -29.66400 2.92800   35.13300  1.000 41.50820  ? 52  PRO A HD3  1 
ATOM   807  N N    . ASN A 1 53  ? -33.46300 -0.75500  36.01900  1.000 34.50016  ? 53  ASN A N    1 
ATOM   808  C CA   . ASN A 1 53  ? -33.84200 -2.08000  36.47000  1.000 32.76321  ? 53  ASN A CA   1 
ATOM   809  C C    . ASN A 1 53  ? -33.92900 -2.91000  35.20200  1.000 34.83067  ? 53  ASN A C    1 
ATOM   810  O O    . ASN A 1 53  ? -34.94500 -2.89100  34.51300  1.000 34.57652  ? 53  ASN A O    1 
ATOM   811  C CB   . ASN A 1 53  ? -35.16100 -2.04000  37.22500  1.000 40.76952  ? 53  ASN A CB   1 
ATOM   812  C CG   . ASN A 1 53  ? -35.46000 -3.34000  37.90700  1.000 46.34722  ? 53  ASN A CG   1 
ATOM   813  O OD1  . ASN A 1 53  ? -35.40100 -4.40900  37.30900  1.000 41.80707  ? 53  ASN A OD1  1 
ATOM   814  N ND2  . ASN A 1 53  ? -35.76000 -3.25700  39.18900  1.000 53.42495  ? 53  ASN A ND2  1 
ATOM   815  H H    . ASN A 1 53  ? -34.11200 -0.29100  35.69800  1.000 41.40099  ? 53  ASN A H    1 
ATOM   816  H HA   . ASN A 1 53  ? -33.15800 -2.45300  37.04800  1.000 39.31665  ? 53  ASN A HA   1 
ATOM   817  H HB2  . ASN A 1 53  ? -35.11900 -1.34600  37.90100  1.000 48.92422  ? 53  ASN A HB2  1 
ATOM   818  H HB3  . ASN A 1 53  ? -35.88000 -1.85400  36.60100  1.000 48.92422  ? 53  ASN A HB3  1 
ATOM   819  H HD21 . ASN A 1 53  ? -35.92900 -3.97000  39.63400  1.000 64.11074  ? 53  ASN A HD21 1 
ATOM   820  H HD22 . ASN A 1 53  ? -35.78300 -2.49000  39.57800  1.000 64.11074  ? 53  ASN A HD22 1 
ATOM   821  N N    . TYR A 1 54  ? -32.89200 -3.69000  34.91900  1.000 35.69805  ? 54  TYR A N    1 
ATOM   822  C CA   . TYR A 1 54  ? -32.84900 -4.32200  33.60000  1.000 32.71088  ? 54  TYR A CA   1 
ATOM   823  C C    . TYR A 1 54  ? -33.88600 -5.40400  33.46500  1.000 30.80870  ? 54  TYR A C    1 
ATOM   824  O O    . TYR A 1 54  ? -34.39800 -5.63400  32.36000  1.000 32.39049  ? 54  TYR A O    1 
ATOM   825  C CB   . TYR A 1 54  ? -31.46700 -4.90400  33.34000  1.000 31.14692  ? 54  TYR A CB   1 
ATOM   826  C CG   . TYR A 1 54  ? -30.45600 -3.84500  33.03600  1.000 30.50910  ? 54  TYR A CG   1 
ATOM   827  C CD1  . TYR A 1 54  ? -30.41900 -3.23900  31.79300  1.000 31.80636  ? 54  TYR A CD1  1 
ATOM   828  C CD2  . TYR A 1 54  ? -29.56400 -3.41400  34.01400  1.000 33.02326  ? 54  TYR A CD2  1 
ATOM   829  C CE1  . TYR A 1 54  ? -29.48700 -2.24600  31.50000  1.000 33.74391  ? 54  TYR A CE1  1 
ATOM   830  C CE2  . TYR A 1 54  ? -28.62900 -2.42200  33.73100  1.000 29.68786  ? 54  TYR A CE2  1 
ATOM   831  C CZ   . TYR A 1 54  ? -28.60200 -1.84700  32.48500  1.000 30.18068  ? 54  TYR A CZ   1 
ATOM   832  O OH   . TYR A 1 54  ? -27.65800 -0.88600  32.23900  1.000 29.89574  ? 54  TYR A OH   1 
ATOM   833  H H    . TYR A 1 54  ? -32.23100 -3.86500  35.44100  1.000 42.83846  ? 54  TYR A H    1 
ATOM   834  H HA   . TYR A 1 54  ? -33.02500 -3.65100  32.92200  1.000 39.25386  ? 54  TYR A HA   1 
ATOM   835  H HB2  . TYR A 1 54  ? -31.17200 -5.38600  34.12800  1.000 37.37711  ? 54  TYR A HB2  1 
ATOM   836  H HB3  . TYR A 1 54  ? -31.51300 -5.50400  32.58000  1.000 37.37711  ? 54  TYR A HB3  1 
ATOM   837  H HD1  . TYR A 1 54  ? -31.01400 -3.51500  31.13300  1.000 38.16844  ? 54  TYR A HD1  1 
ATOM   838  H HD2  . TYR A 1 54  ? -29.58000 -3.80600  34.85700  1.000 39.62872  ? 54  TYR A HD2  1 
ATOM   839  H HE1  . TYR A 1 54  ? -29.46100 -1.85900  30.65700  1.000 40.49349  ? 54  TYR A HE1  1 
ATOM   840  H HE2  . TYR A 1 54  ? -28.02600 -2.14900  34.38400  1.000 35.62623  ? 54  TYR A HE2  1 
ATOM   841  H HH   . TYR A 1 54  ? -27.19800 -0.75200  32.92900  1.000 35.87569  ? 54  TYR A HH   1 
ATOM   842  N N    . GLU A 1 55  ? -34.19000 -6.09200  34.55900  1.000 35.50385  ? 55  GLU A N    1 
ATOM   843  C CA   . GLU A 1 55  ? -35.21000 -7.12600  34.49200  1.000 37.94899  ? 55  GLU A CA   1 
ATOM   844  C C    . GLU A 1 55  ? -36.54600 -6.49600  34.11900  1.000 38.67289  ? 55  GLU A C    1 
ATOM   845  O O    . GLU A 1 55  ? -37.28100 -7.00200  33.25900  1.000 35.11702  ? 55  GLU A O    1 
ATOM   846  C CB   . GLU A 1 55  ? -35.28400 -7.83100  35.84300  1.000 42.69201  ? 55  GLU A CB   1 
ATOM   847  C CG   . GLU A 1 55  ? -34.10400 -8.79300  36.03700  1.000 47.50609  ? 55  GLU A CG   1 
ATOM   848  C CD   . GLU A 1 55  ? -32.83300 -8.07900  36.60800  1.000 60.01039  ? 55  GLU A CD   1 
ATOM   849  O OE1  . GLU A 1 55  ? -32.90400 -6.88800  37.04500  1.000 56.43014  ? 55  GLU A OE1  1 
ATOM   850  O OE2  . GLU A 1 55  ? -31.74900 -8.71400  36.61900  1.000 58.85233  ? 55  GLU A OE2  1 
ATOM   851  H H    . GLU A 1 55  ? -33.83100 -5.98300  35.33300  1.000 42.60542  ? 55  GLU A H    1 
ATOM   852  H HA   . GLU A 1 55  ? -34.97300 -7.77600  33.81200  1.000 45.53959  ? 55  GLU A HA   1 
ATOM   853  H HB2  . GLU A 1 55  ? -35.26100 -7.17000  36.55200  1.000 51.23121  ? 55  GLU A HB2  1 
ATOM   854  H HB3  . GLU A 1 55  ? -36.10500 -8.34500  35.89000  1.000 51.23121  ? 55  GLU A HB3  1 
ATOM   855  H HG2  . GLU A 1 55  ? -34.36300 -9.48800  36.66200  1.000 57.00811  ? 55  GLU A HG2  1 
ATOM   856  H HG3  . GLU A 1 55  ? -33.86900 -9.18700  35.18200  1.000 57.00811  ? 55  GLU A HG3  1 
ATOM   857  N N    . ASP A 1 56  ? -36.86900 -5.37300  34.76400  1.000 34.02456  ? 56  ASP A N    1 
ATOM   858  C CA   . ASP A 1 56  ? -38.11400 -4.67200  34.45300  1.000 39.87042  ? 56  ASP A CA   1 
ATOM   859  C C    . ASP A 1 56  ? -38.11500 -4.13900  33.02100  1.000 38.77382  ? 56  ASP A C    1 
ATOM   860  O O    . ASP A 1 56  ? -39.13800 -4.19300  32.34000  1.000 38.35299  ? 56  ASP A O    1 
ATOM   861  C CB   . ASP A 1 56  ? -38.32800 -3.53200  35.43100  1.000 36.49602  ? 56  ASP A CB   1 
ATOM   862  C CG   . ASP A 1 56  ? -39.73600 -2.95300  35.31700  1.000 43.19219  ? 56  ASP A CG   1 
ATOM   863  O OD1  . ASP A 1 56  ? -40.70400 -3.64600  35.72500  1.000 43.82400  ? 56  ASP A OD1  1 
ATOM   864  O OD2  . ASP A 1 56  ? -39.86500 -1.81400  34.84500  1.000 45.30696  ? 56  ASP A OD2  1 
ATOM   865  H H    . ASP A 1 56  ? -36.39200 -5.00200  35.37600  1.000 40.83028  ? 56  ASP A H    1 
ATOM   866  H HA   . ASP A 1 56  ? -38.85600 -5.29000  34.54400  1.000 47.84530  ? 56  ASP A HA   1 
ATOM   867  H HB2  . ASP A 1 56  ? -38.20600 -3.86000  36.33600  1.000 43.79602  ? 56  ASP A HB2  1 
ATOM   868  H HB3  . ASP A 1 56  ? -37.69200 -2.82400  35.24200  1.000 43.79602  ? 56  ASP A HB3  1 
ATOM   869  N N    . LEU A 1 57  ? -36.99000 -3.56400  32.57700  1.000 35.36789  ? 57  LEU A N    1 
ATOM   870  C CA   . LEU A 1 57  ? -36.91300 -3.02000  31.23100  1.000 33.70538  ? 57  LEU A CA   1 
ATOM   871  C C    . LEU A 1 57  ? -37.05300 -4.13100  30.20200  1.000 36.98787  ? 57  LEU A C    1 
ATOM   872  O O    . LEU A 1 57  ? -37.69900 -3.95100  29.16200  1.000 36.13201  ? 57  LEU A O    1 
ATOM   873  C CB   . LEU A 1 57  ? -35.56800 -2.29200  31.03400  1.000 38.40213  ? 57  LEU A CB   1 
ATOM   874  C CG   . LEU A 1 57  ? -35.35100 -1.00800  31.85700  1.000 39.99381  ? 57  LEU A CG   1 
ATOM   875  C CD1  . LEU A 1 57  ? -33.87500 -0.50400  31.64100  1.000 38.76401  ? 57  LEU A CD1  1 
ATOM   876  C CD2  . LEU A 1 57  ? -36.40600 0.08600   31.50800  1.000 46.94344  ? 57  LEU A CD2  1 
ATOM   877  H H    . LEU A 1 57  ? -36.26800 -3.48000  33.03600  1.000 42.44227  ? 57  LEU A H    1 
ATOM   878  H HA   . LEU A 1 57  ? -37.63300 -2.38400  31.09600  1.000 40.44725  ? 57  LEU A HA   1 
ATOM   879  H HB2  . LEU A 1 57  ? -34.85400 -2.90600  31.26700  1.000 46.08335  ? 57  LEU A HB2  1 
ATOM   880  H HB3  . LEU A 1 57  ? -35.48900 -2.05000  30.09800  1.000 46.08335  ? 57  LEU A HB3  1 
ATOM   881  H HG   . LEU A 1 57  ? -35.45300 -1.22200  32.79700  1.000 47.99338  ? 57  LEU A HG   1 
ATOM   882  H HD11 . LEU A 1 57  ? -33.73900 0.30500   32.15900  1.000 46.51761  ? 57  LEU A HD11 1 
ATOM   883  H HD12 . LEU A 1 57  ? -33.26000 -1.19400  31.93600  1.000 46.51761  ? 57  LEU A HD12 1 
ATOM   884  H HD13 . LEU A 1 57  ? -33.73900 -0.32000  30.69800  1.000 46.51761  ? 57  LEU A HD13 1 
ATOM   885  H HD21 . LEU A 1 57  ? -36.18700 0.90000   31.98800  1.000 56.33293  ? 57  LEU A HD21 1 
ATOM   886  H HD22 . LEU A 1 57  ? -36.38600 0.25000   30.55200  1.000 56.33293  ? 57  LEU A HD22 1 
ATOM   887  H HD23 . LEU A 1 57  ? -37.28500 -0.22700  31.77200  1.000 56.33293  ? 57  LEU A HD23 1 
ATOM   888  N N    . LEU A 1 58  ? -36.40700 -5.27500  30.44800  1.000 33.13115  ? 58  LEU A N    1 
ATOM   889  C CA   . LEU A 1 58  ? -36.42100 -6.33200  29.44000  1.000 35.27868  ? 58  LEU A CA   1 
ATOM   890  C C    . LEU A 1 58  ? -37.79500 -6.97700  29.29700  1.000 35.95547  ? 58  LEU A C    1 
ATOM   891  O O    . LEU A 1 58  ? -38.20400 -7.35200  28.17800  1.000 37.33612  ? 58  LEU A O    1 
ATOM   892  C CB   . LEU A 1 58  ? -35.40600 -7.39800  29.82700  1.000 34.72656  ? 58  LEU A CB   1 
ATOM   893  C CG   . LEU A 1 58  ? -35.13300 -8.38500  28.68100  1.000 41.57020  ? 58  LEU A CG   1 
ATOM   894  C CD1  . LEU A 1 58  ? -34.73800 -7.70700  27.35200  1.000 40.20497  ? 58  LEU A CD1  1 
ATOM   895  C CD2  . LEU A 1 58  ? -34.07900 -9.38300  29.11100  1.000 38.31657  ? 58  LEU A CD2  1 
ATOM   896  H H    . LEU A 1 58  ? -35.96900 -5.45800  31.16500  1.000 39.75818  ? 58  LEU A H    1 
ATOM   897  H HA   . LEU A 1 58  ? -36.17200 -5.94900  28.58500  1.000 42.33522  ? 58  LEU A HA   1 
ATOM   898  H HB2  . LEU A 1 58  ? -34.56800 -6.96900  30.06100  1.000 41.67267  ? 58  LEU A HB2  1 
ATOM   899  H HB3  . LEU A 1 58  ? -35.74600 -7.90100  30.58300  1.000 41.67267  ? 58  LEU A HB3  1 
ATOM   900  H HG   . LEU A 1 58  ? -35.94700 -8.88600  28.51400  1.000 49.88504  ? 58  LEU A HG   1 
ATOM   901  H HD11 . LEU A 1 58  ? -34.34900 -8.37300  26.76400  1.000 48.24677  ? 58  LEU A HD11 1 
ATOM   902  H HD12 . LEU A 1 58  ? -35.53000 -7.32700  26.94100  1.000 48.24677  ? 58  LEU A HD12 1 
ATOM   903  H HD13 . LEU A 1 58  ? -34.09000 -7.00900  27.53400  1.000 48.24677  ? 58  LEU A HD13 1 
ATOM   904  H HD21 . LEU A 1 58  ? -33.92300 -10.00900 28.38700  1.000 45.98069  ? 58  LEU A HD21 1 
ATOM   905  H HD22 . LEU A 1 58  ? -33.26100 -8.90600  29.31900  1.000 45.98069  ? 58  LEU A HD22 1 
ATOM   906  H HD23 . LEU A 1 58  ? -34.39500 -9.85700  29.89600  1.000 45.98069  ? 58  LEU A HD23 1 
ATOM   907  N N    . ILE A 1 59  ? -38.55700 -7.05800  30.39500  1.000 34.91939  ? 59  ILE A N    1 
ATOM   908  C CA   . ILE A 1 59  ? -39.81900 -7.75100  30.26600  1.000 35.79034  ? 59  ILE A CA   1 
ATOM   909  C C    . ILE A 1 59  ? -40.82000 -6.92000  29.46700  1.000 41.14372  ? 59  ILE A C    1 
ATOM   910  O O    . ILE A 1 59  ? -41.74400 -7.48800  28.87200  1.000 40.93771  ? 59  ILE A O    1 
ATOM   911  C CB   . ILE A 1 59  ? -40.35800 -8.15100  31.64500  1.000 41.43261  ? 59  ILE A CB   1 
ATOM   912  C CG1  . ILE A 1 59  ? -41.52800 -9.12400  31.46300  1.000 44.54805  ? 59  ILE A CG1  1 
ATOM   913  C CG2  . ILE A 1 59  ? -40.81300 -6.92500  32.43100  1.000 44.92921  ? 59  ILE A CG2  1 
ATOM   914  C CD1  . ILE A 1 59  ? -42.02200 -9.72100  32.72400  1.000 48.30385  ? 59  ILE A CD1  1 
ATOM   915  H H    . ILE A 1 59  ? -38.37300 -6.74000  31.17200  1.000 41.90406  ? 59  ILE A H    1 
ATOM   916  H HA   . ILE A 1 59  ? -39.66600 -8.57000  29.77000  1.000 42.94920  ? 59  ILE A HA   1 
ATOM   917  H HB   . ILE A 1 59  ? -39.65300 -8.59700  32.14000  1.000 49.71994  ? 59  ILE A HB   1 
ATOM   918  H HG12 . ILE A 1 59  ? -42.26800 -8.64900  31.05300  1.000 53.45846  ? 59  ILE A HG12 1 
ATOM   919  H HG13 . ILE A 1 59  ? -41.24400 -9.84900  30.88500  1.000 53.45846  ? 59  ILE A HG13 1 
ATOM   920  H HG21 . ILE A 1 59  ? -41.04100 -7.19600  33.33400  1.000 53.91585  ? 59  ILE A HG21 1 
ATOM   921  H HG22 . ILE A 1 59  ? -40.08800 -6.28500  32.45400  1.000 53.91585  ? 59  ILE A HG22 1 
ATOM   922  H HG23 . ILE A 1 59  ? -41.58800 -6.53500  31.99800  1.000 53.91585  ? 59  ILE A HG23 1 
ATOM   923  H HD11 . ILE A 1 59  ? -42.68000 -10.40200 32.51400  1.000 57.96542  ? 59  ILE A HD11 1 
ATOM   924  H HD12 . ILE A 1 59  ? -41.27500 -10.11800 33.19800  1.000 57.96542  ? 59  ILE A HD12 1 
ATOM   925  H HD13 . ILE A 1 59  ? -42.42700 -9.02600  33.26600  1.000 57.96542  ? 59  ILE A HD13 1 
ATOM   926  N N    . ARG A 1 60  ? -40.59800 -5.60500  29.34800  1.000 37.33517  ? 60  ARG A N    1 
ATOM   927  C CA   . ARG A 1 60  ? -41.48200 -4.75000  28.56500  1.000 39.15074  ? 60  ARG A CA   1 
ATOM   928  C C    . ARG A 1 60  ? -41.16400 -4.77100  27.06800  1.000 39.74402  ? 60  ARG A C    1 
ATOM   929  O O    . ARG A 1 60  ? -41.89000 -4.15000  26.29400  1.000 39.68150  ? 60  ARG A O    1 
ATOM   930  C CB   . ARG A 1 60  ? -41.35300 -3.32900  29.07500  1.000 37.52277  ? 60  ARG A CB   1 
ATOM   931  C CG   . ARG A 1 60  ? -41.64800 -3.21800  30.56000  1.000 37.88222  ? 60  ARG A CG   1 
ATOM   932  C CD   . ARG A 1 60  ? -41.52900 -1.80400  31.06200  1.000 40.01560  ? 60  ARG A CD   1 
ATOM   933  N NE   . ARG A 1 60  ? -41.73700 -1.75200  32.50300  1.000 38.98161  ? 60  ARG A NE   1 
ATOM   934  C CZ   . ARG A 1 60  ? -42.85600 -1.37300  33.10000  1.000 39.69453  ? 60  ARG A CZ   1 
ATOM   935  N NH1  . ARG A 1 60  ? -43.93600 -1.01900  32.40400  1.000 41.27842  ? 60  ARG A NH1  1 
ATOM   936  N NH2  . ARG A 1 60  ? -42.90600 -1.36000  34.43700  1.000 42.61121  ? 60  ARG A NH2  1 
ATOM   937  H H    . ARG A 1 60  ? -39.94100 -5.18800  29.71300  1.000 44.80301  ? 60  ARG A H    1 
ATOM   938  H HA   . ARG A 1 60  ? -42.39900 -5.03800  28.68800  1.000 46.98169  ? 60  ARG A HA   1 
ATOM   939  H HB2  . ARG A 1 60  ? -40.44600 -3.01900  28.92400  1.000 45.02332  ? 60  ARG A HB2  1 
ATOM   940  H HB3  . ARG A 1 60  ? -41.98100 -2.76300  28.60000  1.000 45.02332  ? 60  ARG A HB3  1 
ATOM   941  H HG2  . ARG A 1 60  ? -42.55600 -3.51800  30.72100  1.000 45.45465  ? 60  ARG A HG2  1 
ATOM   942  H HG3  . ARG A 1 60  ? -41.02400 -3.76900  31.05400  1.000 45.45465  ? 60  ARG A HG3  1 
ATOM   943  H HD2  . ARG A 1 60  ? -40.63500 -1.47600  30.87500  1.000 48.01952  ? 60  ARG A HD2  1 
ATOM   944  H HD3  . ARG A 1 60  ? -42.18600 -1.24600  30.62100  1.000 48.01952  ? 60  ARG A HD3  1 
ATOM   945  H HE   . ARG A 1 60  ? -41.08000 -1.98600  33.00600  1.000 46.77873  ? 60  ARG A HE   1 
ATOM   946  H HH11 . ARG A 1 60  ? -43.92200 -1.02400  31.54500  1.000 49.53009  ? 60  ARG A HH11 1 
ATOM   947  H HH12 . ARG A 1 60  ? -44.65100 -0.78000  32.81800  1.000 49.53009  ? 60  ARG A HH12 1 
ATOM   948  H HH21 . ARG A 1 60  ? -42.21500 -1.58900  34.89500  1.000 51.13425  ? 60  ARG A HH21 1 
ATOM   949  H HH22 . ARG A 1 60  ? -43.62700 -1.11900  34.83800  1.000 51.13425  ? 60  ARG A HH22 1 
ATOM   950  N N    . LYS A 1 61  ? -40.13800 -5.48500  26.65800  1.000 39.02623  ? 61  LYS A N    1 
ATOM   951  C CA   . LYS A 1 61  ? -39.72200 -5.53600  25.27100  1.000 44.88351  ? 61  LYS A CA   1 
ATOM   952  C C    . LYS A 1 61  ? -40.31600 -6.73800  24.56800  1.000 45.01626  ? 61  LYS A C    1 
ATOM   953  O O    . LYS A 1 61  ? -40.36300 -7.83700  25.12400  1.000 48.11873  ? 61  LYS A O    1 
ATOM   954  C CB   . LYS A 1 61  ? -38.20200 -5.62400  25.15300  1.000 38.42778  ? 61  LYS A CB   1 
ATOM   955  C CG   . LYS A 1 61  ? -37.41300 -4.45700  25.76300  1.000 41.34594  ? 61  LYS A CG   1 
ATOM   956  C CD   . LYS A 1 61  ? -37.66400 -3.19500  24.99400  1.000 44.52511  ? 61  LYS A CD   1 
ATOM   957  C CE   . LYS A 1 61  ? -36.97800 -1.99200  25.60600  1.000 51.78224  ? 61  LYS A CE   1 
ATOM   958  N NZ   . LYS A 1 61  ? -37.41300 -0.76900  24.85900  1.000 63.15737  ? 61  LYS A NZ   1 
ATOM   959  H H    . LYS A 1 61  ? -39.65000 -5.96500  27.17800  1.000 46.83228  ? 61  LYS A H    1 
ATOM   960  H HA   . LYS A 1 61  ? -40.02200 -4.73600  24.81200  1.000 53.86102  ? 61  LYS A HA   1 
ATOM   961  H HB2  . LYS A 1 61  ? -37.90800 -6.43500  25.59600  1.000 46.11414  ? 61  LYS A HB2  1 
ATOM   962  H HB3  . LYS A 1 61  ? -37.97100 -5.66900  24.21200  1.000 46.11414  ? 61  LYS A HB3  1 
ATOM   963  H HG2  . LYS A 1 61  ? -37.69700 -4.31900  26.68000  1.000 49.61593  ? 61  LYS A HG2  1 
ATOM   964  H HG3  . LYS A 1 61  ? -36.46400 -4.65500  25.72800  1.000 49.61593  ? 61  LYS A HG3  1 
ATOM   965  H HD2  . LYS A 1 61  ? -37.33000 -3.30400  24.09000  1.000 53.43094  ? 61  LYS A HD2  1 
ATOM   966  H HD3  . LYS A 1 61  ? -38.61700 -3.01600  24.97700  1.000 53.43094  ? 61  LYS A HD3  1 
ATOM   967  H HE2  . LYS A 1 61  ? -37.23900 -1.90100  26.53600  1.000 62.13949  ? 61  LYS A HE2  1 
ATOM   968  H HE3  . LYS A 1 61  ? -36.01600 -2.08400  25.52400  1.000 62.13949  ? 61  LYS A HE3  1 
ATOM   969  H HZ1  . LYS A 1 61  ? -37.05900 -0.04300  25.23300  1.000 75.78965  ? 61  LYS A HZ1  1 
ATOM   970  H HZ2  . LYS A 1 61  ? -37.14500 -0.81900  24.01200  1.000 75.78965  ? 61  LYS A HZ2  1 
ATOM   971  H HZ3  . LYS A 1 61  ? -38.30000 -0.70100  24.87900  1.000 75.78965  ? 61  LYS A HZ3  1 
ATOM   972  N N    . SER A 1 62  ? -40.62800 -6.53900  23.29900  1.000 44.19673  ? 62  SER A N    1 
ATOM   973  C CA   . SER A 1 62  ? -40.96200 -7.59700  22.36300  1.000 43.00797  ? 62  SER A CA   1 
ATOM   974  C C    . SER A 1 62  ? -39.74700 -7.91500  21.51700  1.000 48.31699  ? 62  SER A C    1 
ATOM   975  O O    . SER A 1 62  ? -38.89300 -7.05900  21.27800  1.000 43.39330  ? 62  SER A O    1 
ATOM   976  C CB   . SER A 1 62  ? -42.11200 -7.16500  21.46600  1.000 50.19122  ? 62  SER A CB   1 
ATOM   977  O OG   . SER A 1 62  ? -43.27500 -6.81600  22.23300  1.000 50.33937  ? 62  SER A OG   1 
ATOM   978  H H    . SER A 1 62  ? -40.65400 -5.75800  22.94000  1.000 53.03688  ? 62  SER A H    1 
ATOM   979  H HA   . SER A 1 62  ? -41.22500 -8.39500  22.84700  1.000 51.61037  ? 62  SER A HA   1 
ATOM   980  H HB2  . SER A 1 62  ? -41.83400 -6.39300  20.94900  1.000 60.23026  ? 62  SER A HB2  1 
ATOM   981  H HB3  . SER A 1 62  ? -42.33700 -7.89700  20.87100  1.000 60.23026  ? 62  SER A HB3  1 
ATOM   982  H HG   . SER A 1 62  ? -43.89700 -6.58100  21.72000  1.000 60.40805  ? 62  SER A HG   1 
ATOM   983  N N    . ASN A 1 63  ? -39.73200 -9.11900  20.95100  1.000 46.64304  ? 63  ASN A N    1 
ATOM   984  C CA   . ASN A 1 63  ? -38.64600 -9.42900  20.02500  1.000 44.10806  ? 63  ASN A CA   1 
ATOM   985  C C    . ASN A 1 63  ? -38.53600 -8.36500  18.94200  1.000 42.12472  ? 63  ASN A C    1 
ATOM   986  O O    . ASN A 1 63  ? -37.42200 -7.97500  18.55000  1.000 44.62824  ? 63  ASN A O    1 
ATOM   987  C CB   . ASN A 1 63  ? -38.86500 -10.79100 19.37200  1.000 50.42803  ? 63  ASN A CB   1 
ATOM   988  C CG   . ASN A 1 63  ? -38.69800 -11.94500 20.34900  1.000 48.46133  ? 63  ASN A CG   1 
ATOM   989  O OD1  . ASN A 1 63  ? -37.83900 -11.92100 21.24800  1.000 47.65149  ? 63  ASN A OD1  1 
ATOM   990  N ND2  . ASN A 1 63  ? -39.49500 -12.99200 20.14500  1.000 54.44919  ? 63  ASN A ND2  1 
ATOM   991  H H    . ASN A 1 63  ? -40.30700 -9.74600  21.07700  1.000 55.97245  ? 63  ASN A H    1 
ATOM   992  H HA   . ASN A 1 63  ? -37.80800 -9.45600  20.51200  1.000 52.93048  ? 63  ASN A HA   1 
ATOM   993  H HB2  . ASN A 1 63  ? -39.76500 -10.82900 19.01300  1.000 60.51443  ? 63  ASN A HB2  1 
ATOM   994  H HB3  . ASN A 1 63  ? -38.21800 -10.90600 18.65900  1.000 60.51443  ? 63  ASN A HB3  1 
ATOM   995  H HD21 . ASN A 1 63  ? -39.44500 -13.67700 20.66200  1.000 65.33983  ? 63  ASN A HD21 1 
ATOM   996  H HD22 . ASN A 1 63  ? -40.07200 -12.97500 19.50700  1.000 65.33983  ? 63  ASN A HD22 1 
ATOM   997  N N    . HIS A 1 64  ? -39.67500 -7.86500  18.45700  1.000 43.63477  ? 64  HIS A N    1 
ATOM   998  C CA   . HIS A 1 64  ? -39.64300 -6.90600  17.35200  1.000 48.12109  ? 64  HIS A CA   1 
ATOM   999  C C    . HIS A 1 64  ? -39.19200 -5.51200  17.76100  1.000 47.74534  ? 64  HIS A C    1 
ATOM   1000 O O    . HIS A 1 64  ? -38.97200 -4.68100  16.87100  1.000 46.89190  ? 64  HIS A O    1 
ATOM   1001 C CB   . HIS A 1 64  ? -41.00500 -6.83400  16.64100  1.000 53.38362  ? 64  HIS A CB   1 
ATOM   1002 C CG   . HIS A 1 64  ? -42.11800 -6.40000  17.52900  1.000 53.48782  ? 64  HIS A CG   1 
ATOM   1003 N ND1  . HIS A 1 64  ? -42.96600 -7.29600  18.14400  1.000 56.66359  ? 64  HIS A ND1  1 
ATOM   1004 C CD2  . HIS A 1 64  ? -42.52700 -5.16500  17.91200  1.000 56.68676  ? 64  HIS A CD2  1 
ATOM   1005 C CE1  . HIS A 1 64  ? -43.87000 -6.63000  18.84600  1.000 54.90177  ? 64  HIS A CE1  1 
ATOM   1006 N NE2  . HIS A 1 64  ? -43.61800 -5.33700  18.73400  1.000 60.50757  ? 64  HIS A NE2  1 
ATOM   1007 H H    . HIS A 1 64  ? -40.46200 -8.06100  18.74300  1.000 52.36252  ? 64  HIS A H    1 
ATOM   1008 H HA   . HIS A 1 64  ? -39.00200 -7.22800  16.69900  1.000 57.74611  ? 64  HIS A HA   1 
ATOM   1009 H HB2  . HIS A 1 64  ? -40.94400 -6.20000  15.91000  1.000 64.06114  ? 64  HIS A HB2  1 
ATOM   1010 H HB3  . HIS A 1 64  ? -41.22500 -7.71400  16.29600  1.000 64.06114  ? 64  HIS A HB3  1 
ATOM   1011 H HD2  . HIS A 1 64  ? -42.14800 -4.35400  17.65900  1.000 68.02492  ? 64  HIS A HD2  1 
ATOM   1012 H HE1  . HIS A 1 64  ? -44.54800 -7.01000  19.35700  1.000 65.88293  ? 64  HIS A HE1  1 
ATOM   1013 H HE2  . HIS A 1 64  ? -44.06500 -4.70600  19.11100  1.000 72.60988  ? 64  HIS A HE2  1 
ATOM   1014 N N    . ASN A 1 65  ? -39.01400 -5.24200  19.06400  1.000 41.07478  ? 65  ASN A N    1 
ATOM   1015 C CA   . ASN A 1 65  ? -38.36800 -4.00100  19.49000  1.000 45.11493  ? 65  ASN A CA   1 
ATOM   1016 C C    . ASN A 1 65  ? -36.86600 -3.98000  19.21100  1.000 46.17317  ? 65  ASN A C    1 
ATOM   1017 O O    . ASN A 1 65  ? -36.25600 -2.91100  19.30200  1.000 45.03155  ? 65  ASN A O    1 
ATOM   1018 C CB   . ASN A 1 65  ? -38.56300 -3.75700  20.99100  1.000 42.40318  ? 65  ASN A CB   1 
ATOM   1019 C CG   . ASN A 1 65  ? -40.00300 -3.46400  21.33300  1.000 51.53531  ? 65  ASN A CG   1 
ATOM   1020 O OD1  . ASN A 1 65  ? -40.53700 -3.96000  22.32700  1.000 48.39139  ? 65  ASN A OD1  1 
ATOM   1021 N ND2  . ASN A 1 65  ? -40.66200 -2.68600  20.47800  1.000 52.16581  ? 65  ASN A ND2  1 
ATOM   1022 H H    . ASN A 1 65  ? -39.25700 -5.75600  19.70900  1.000 49.29053  ? 65  ASN A H    1 
ATOM   1023 H HA   . ASN A 1 65  ? -38.75500 -3.26200  18.99800  1.000 54.13871  ? 65  ASN A HA   1 
ATOM   1024 H HB2  . ASN A 1 65  ? -38.29100 -4.54900  21.48000  1.000 50.88462  ? 65  ASN A HB2  1 
ATOM   1025 H HB3  . ASN A 1 65  ? -38.02700 -2.99600  21.26200  1.000 50.88462  ? 65  ASN A HB3  1 
ATOM   1026 H HD21 . ASN A 1 65  ? -41.48600 -2.49200  20.62800  1.000 62.59978  ? 65  ASN A HD21 1 
ATOM   1027 H HD22 . ASN A 1 65  ? -40.26700 -2.35700  19.79100  1.000 62.59978  ? 65  ASN A HD22 1 
ATOM   1028 N N    . PHE A 1 66  ? -36.24900 -5.12500  18.92500  1.000 43.79049  ? 66  PHE A N    1 
ATOM   1029 C CA   . PHE A 1 66  ? -34.81200 -5.20000  18.64800  1.000 38.55561  ? 66  PHE A CA   1 
ATOM   1030 C C    . PHE A 1 66  ? -34.58000 -5.20100  17.14100  1.000 42.83992  ? 66  PHE A C    1 
ATOM   1031 O O    . PHE A 1 66  ? -34.98600 -6.14300  16.45900  1.000 42.98599  ? 66  PHE A O    1 
ATOM   1032 C CB   . PHE A 1 66  ? -34.18000 -6.45200  19.25400  1.000 39.48872  ? 66  PHE A CB   1 
ATOM   1033 C CG   . PHE A 1 66  ? -34.29000 -6.51200  20.73900  1.000 44.34918  ? 66  PHE A CG   1 
ATOM   1034 C CD1  . PHE A 1 66  ? -33.36900 -5.87000  21.52800  1.000 45.33689  ? 66  PHE A CD1  1 
ATOM   1035 C CD2  . PHE A 1 66  ? -35.35000 -7.18800  21.34500  1.000 42.45873  ? 66  PHE A CD2  1 
ATOM   1036 C CE1  . PHE A 1 66  ? -33.50000 -5.90700  22.91200  1.000 42.30626  ? 66  PHE A CE1  1 
ATOM   1037 C CE2  . PHE A 1 66  ? -35.46900 -7.21900  22.72500  1.000 41.04274  ? 66  PHE A CE2  1 
ATOM   1038 C CZ   . PHE A 1 66  ? -34.55600 -6.59200  23.49600  1.000 39.75509  ? 66  PHE A CZ   1 
ATOM   1039 H H    . PHE A 1 66  ? -36.64600 -5.88700  18.88400  1.000 52.54938  ? 66  PHE A H    1 
ATOM   1040 H HA   . PHE A 1 66  ? -34.36900 -4.42400  19.02500  1.000 46.26753  ? 66  PHE A HA   1 
ATOM   1041 H HB2  . PHE A 1 66  ? -34.62300 -7.23400  18.89100  1.000 47.38726  ? 66  PHE A HB2  1 
ATOM   1042 H HB3  . PHE A 1 66  ? -33.23800 -6.47000  19.02400  1.000 47.38726  ? 66  PHE A HB3  1 
ATOM   1043 H HD1  . PHE A 1 66  ? -32.66200 -5.40800  21.13800  1.000 54.40507  ? 66  PHE A HD1  1 
ATOM   1044 H HD2  . PHE A 1 66  ? -35.98400 -7.61900  20.81800  1.000 50.95127  ? 66  PHE A HD2  1 
ATOM   1045 H HE1  . PHE A 1 66  ? -32.87200 -5.47900  23.44800  1.000 50.76832  ? 66  PHE A HE1  1 
ATOM   1046 H HE2  . PHE A 1 66  ? -36.17500 -7.67800  23.12000  1.000 49.25208  ? 66  PHE A HE2  1 
ATOM   1047 H HZ   . PHE A 1 66  ? -34.63500 -6.62000  24.42200  1.000 47.70691  ? 66  PHE A HZ   1 
ATOM   1048 N N    . LEU A 1 67  ? -33.92400 -4.16100  16.63500  1.000 37.82303  ? 67  LEU A N    1 
ATOM   1049 C CA   . LEU A 1 67  ? -33.55000 -4.04200  15.22400  1.000 38.85958  ? 67  LEU A CA   1 
ATOM   1050 C C    . LEU A 1 67  ? -32.09700 -4.50000  15.08800  1.000 40.05815  ? 67  LEU A C    1 
ATOM   1051 O O    . LEU A 1 67  ? -31.18600 -3.89300  15.67300  1.000 36.26478  ? 67  LEU A O    1 
ATOM   1052 C CB   . LEU A 1 67  ? -33.72800 -2.59200  14.77800  1.000 46.10921  ? 67  LEU A CB   1 
ATOM   1053 C CG   . LEU A 1 67  ? -33.36900 -2.08800  13.38400  1.000 48.25814  ? 67  LEU A CG   1 
ATOM   1054 C CD1  . LEU A 1 67  ? -34.22600 -2.77400  12.33800  1.000 58.93442  ? 67  LEU A CD1  1 
ATOM   1055 C CD2  . LEU A 1 67  ? -33.38900 -0.54900  13.26500  1.000 55.50513  ? 67  LEU A CD2  1 
ATOM   1056 H H    . LEU A 1 67  ? -33.67500 -3.48600  17.10600  1.000 45.38844  ? 67  LEU A H    1 
ATOM   1057 H HA   . LEU A 1 67  ? -34.11500 -4.61300  14.68000  1.000 46.63230  ? 67  LEU A HA   1 
ATOM   1058 H HB2  . LEU A 1 67  ? -34.66700 -2.38100  14.89600  1.000 55.33185  ? 67  LEU A HB2  1 
ATOM   1059 H HB3  . LEU A 1 67  ? -33.22000 -2.04800  15.39600  1.000 55.33185  ? 67  LEU A HB3  1 
ATOM   1060 H HG   . LEU A 1 67  ? -32.45500 -2.36100  13.20700  1.000 57.91057  ? 67  LEU A HG   1 
ATOM   1061 H HD11 . LEU A 1 67  ? -33.98100 -2.43900  11.46100  1.000 70.72211  ? 67  LEU A HD11 1 
ATOM   1062 H HD12 . LEU A 1 67  ? -34.07200 -3.73100  12.38200  1.000 70.72211  ? 67  LEU A HD12 1 
ATOM   1063 H HD13 . LEU A 1 67  ? -35.15900 -2.58000  12.51800  1.000 70.72211  ? 67  LEU A HD13 1 
ATOM   1064 H HD21 . LEU A 1 67  ? -33.15300 -0.30000  12.35800  1.000 66.60695  ? 67  LEU A HD21 1 
ATOM   1065 H HD22 . LEU A 1 67  ? -34.28000 -0.22800  13.47500  1.000 66.60695  ? 67  LEU A HD22 1 
ATOM   1066 H HD23 . LEU A 1 67  ? -32.74700 -0.17600  13.88900  1.000 66.60695  ? 67  LEU A HD23 1 
ATOM   1067 N N    . VAL A 1 68  ? -31.87000 -5.60500  14.38200  1.000 35.76530  ? 68  VAL A N    1 
ATOM   1068 C CA   . VAL A 1 68  ? -30.52200 -6.14700  14.24000  1.000 32.22181  ? 68  VAL A CA   1 
ATOM   1069 C C    . VAL A 1 68  ? -30.19500 -6.14900  12.75500  1.000 37.58582  ? 68  VAL A C    1 
ATOM   1070 O O    . VAL A 1 68  ? -30.95900 -6.69700  11.95000  1.000 39.18659  ? 68  VAL A O    1 
ATOM   1071 C CB   . VAL A 1 68  ? -30.36200 -7.54500  14.85400  1.000 37.56530  ? 68  VAL A CB   1 
ATOM   1072 C CG1  . VAL A 1 68  ? -28.93800 -8.04300  14.61900  1.000 39.65170  ? 68  VAL A CG1  1 
ATOM   1073 C CG2  . VAL A 1 68  ? -30.70300 -7.53200  16.38100  1.000 35.91670  ? 68  VAL A CG2  1 
ATOM   1074 H H    . VAL A 1 68  ? -32.47800 -6.05800  13.97600  1.000 42.91916  ? 68  VAL A H    1 
ATOM   1075 H HA   . VAL A 1 68  ? -29.89100 -5.55800  14.68100  1.000 38.66697  ? 68  VAL A HA   1 
ATOM   1076 H HB   . VAL A 1 68  ? -30.97200 -8.15700  14.41400  1.000 45.07916  ? 68  VAL A HB   1 
ATOM   1077 H HG11 . VAL A 1 68  ? -28.77700 -8.81100  15.18900  1.000 47.58284  ? 68  VAL A HG11 1 
ATOM   1078 H HG12 . VAL A 1 68  ? -28.83800 -8.29600  13.68800  1.000 47.58284  ? 68  VAL A HG12 1 
ATOM   1079 H HG13 . VAL A 1 68  ? -28.31500 -7.33300  14.84000  1.000 47.58284  ? 68  VAL A HG13 1 
ATOM   1080 H HG21 . VAL A 1 68  ? -30.58400 -8.42600  16.73800  1.000 43.10084  ? 68  VAL A HG21 1 
ATOM   1081 H HG22 . VAL A 1 68  ? -30.10700 -6.91300  16.83200  1.000 43.10084  ? 68  VAL A HG22 1 
ATOM   1082 H HG23 . VAL A 1 68  ? -31.62400 -7.24900  16.49600  1.000 43.10084  ? 68  VAL A HG23 1 
ATOM   1083 N N    . GLN A 1 69  ? -29.11300 -5.45500  12.41100  1.000 35.79366  ? 69  GLN A N    1 
ATOM   1084 C CA   . GLN A 1 69  ? -28.74400 -5.29300  10.99200  1.000 43.05082  ? 69  GLN A CA   1 
ATOM   1085 C C    . GLN A 1 69  ? -27.33000 -5.80200  10.72800  1.000 42.54674  ? 69  GLN A C    1 
ATOM   1086 O O    . GLN A 1 69  ? -26.40000 -5.29500  11.35900  1.000 36.07353  ? 69  GLN A O    1 
ATOM   1087 C CB   . GLN A 1 69  ? -28.80000 -3.82600  10.59400  1.000 43.86091  ? 69  GLN A CB   1 
ATOM   1088 C CG   . GLN A 1 69  ? -30.18500 -3.20800  10.69400  1.000 53.37033  ? 69  GLN A CG   1 
ATOM   1089 C CD   . GLN A 1 69  ? -30.22100 -1.81000  10.13100  1.000 63.89975  ? 69  GLN A CD   1 
ATOM   1090 O OE1  . GLN A 1 69  ? -29.22900 -1.30100  9.61900   1.000 66.36326  ? 69  GLN A OE1  1 
ATOM   1091 N NE2  . GLN A 1 69  ? -31.37800 -1.17600  10.21900  1.000 66.55849  ? 69  GLN A NE2  1 
ATOM   1092 H H    . GLN A 1 69  ? -28.57900 -5.07100  12.96500  1.000 42.95319  ? 69  GLN A H    1 
ATOM   1093 H HA   . GLN A 1 69  ? -29.36100 -5.78900  10.43200  1.000 51.66179  ? 69  GLN A HA   1 
ATOM   1094 H HB2  . GLN A 1 69  ? -28.20900 -3.32300  11.17600  1.000 52.63390  ? 69  GLN A HB2  1 
ATOM   1095 H HB3  . GLN A 1 69  ? -28.50400 -3.74200  9.67400   1.000 52.63390  ? 69  GLN A HB3  1 
ATOM   1096 H HG2  . GLN A 1 69  ? -30.81300 -3.75200  10.19400  1.000 64.04520  ? 69  GLN A HG2  1 
ATOM   1097 H HG3  . GLN A 1 69  ? -30.44800 -3.16500  11.62700  1.000 64.04520  ? 69  GLN A HG3  1 
ATOM   1098 H HE21 . GLN A 1 69  ? -32.05400 -1.56300  10.58400  1.000 79.87098  ? 69  GLN A HE21 1 
ATOM   1099 H HE22 . GLN A 1 69  ? -31.45400 -0.37600  9.91300   1.000 79.87098  ? 69  GLN A HE22 1 
ATOM   1100 N N    . ALA A 1 70  ? -27.20300 -6.79500  9.85700   1.000 41.75082  ? 70  ALA A N    1 
ATOM   1101 C CA   . ALA A 1 70  ? -25.90200 -7.28000  9.41500   1.000 43.22197  ? 70  ALA A CA   1 
ATOM   1102 C C    . ALA A 1 70  ? -25.71500 -6.73600  8.00300   1.000 51.92782  ? 70  ALA A C    1 
ATOM   1103 O O    . ALA A 1 70  ? -26.43300 -7.13800  7.07400   1.000 47.61005  ? 70  ALA A O    1 
ATOM   1104 C CB   . ALA A 1 70  ? -25.80700 -8.80300  9.48400   1.000 45.00178  ? 70  ALA A CB   1 
ATOM   1105 H H    . ALA A 1 70  ? -27.86600 -7.21100  9.50200   1.000 50.10178  ? 70  ALA A H    1 
ATOM   1106 H HA   . ALA A 1 70  ? -25.20800 -6.90600  9.98000   1.000 51.86716  ? 70  ALA A HA   1 
ATOM   1107 H HB1  . ALA A 1 70  ? -24.92500 -9.07800  9.18800   1.000 54.00294  ? 70  ALA A HB1  1 
ATOM   1108 H HB2  . ALA A 1 70  ? -25.95200 -9.08700  10.40000  1.000 54.00294  ? 70  ALA A HB2  1 
ATOM   1109 H HB3  . ALA A 1 70  ? -26.48500 -9.18700  8.90700   1.000 54.00294  ? 70  ALA A HB3  1 
ATOM   1110 N N    . GLY A 1 71  ? -24.81300 -5.76900  7.85900   1.000 50.79638  ? 71  GLY A N    1 
ATOM   1111 C CA   . GLY A 1 71  ? -24.72000 -5.07400  6.58500   1.000 58.96788  ? 71  GLY A CA   1 
ATOM   1112 C C    . GLY A 1 71  ? -26.03600 -4.39900  6.27300   1.000 62.22522  ? 71  GLY A C    1 
ATOM   1113 O O    . GLY A 1 71  ? -26.53800 -3.59700  7.06100   1.000 61.13598  ? 71  GLY A O    1 
ATOM   1114 H H    . GLY A 1 71  ? -24.26100 -5.50500  8.46300   1.000 60.95646  ? 71  GLY A H    1 
ATOM   1115 H HA2  . GLY A 1 71  ? -24.02200 -4.40200  6.62400   1.000 70.76226  ? 71  GLY A HA2  1 
ATOM   1116 H HA3  . GLY A 1 71  ? -24.51300 -5.70400  5.87700   1.000 70.76226  ? 71  GLY A HA3  1 
ATOM   1117 N N    . ASN A 1 72  ? -26.59000 -4.69000  5.09700   1.000 67.94076  ? 72  ASN A N    1 
ATOM   1118 C CA   . ASN A 1 72  ? -27.87400 -4.15400  4.66900   1.000 68.64535  ? 72  ASN A CA   1 
ATOM   1119 C C    . ASN A 1 72  ? -29.02700 -5.11800  4.94000   1.000 64.08250  ? 72  ASN A C    1 
ATOM   1120 O O    . ASN A 1 72  ? -30.16200 -4.83900  4.55000   1.000 65.72443  ? 72  ASN A O    1 
ATOM   1121 C CB   . ASN A 1 72  ? -27.82400 -3.78100  3.18100   1.000 76.42923  ? 72  ASN A CB   1 
ATOM   1122 C CG   . ASN A 1 72  ? -27.33300 -4.92400  2.30100   1.000 81.77308  ? 72  ASN A CG   1 
ATOM   1123 O OD1  . ASN A 1 72  ? -28.11900 -5.76900  1.86300   1.000 82.06732  ? 72  ASN A OD1  1 
ATOM   1124 N ND2  . ASN A 1 72  ? -26.03000 -4.95000  2.03300   1.000 84.06073  ? 72  ASN A ND2  1 
ATOM   1125 H H    . ASN A 1 72  ? -26.22700 -5.21300  4.51900   1.000 81.52972  ? 72  ASN A H    1 
ATOM   1126 H HA   . ASN A 1 72  ? -28.05100 -3.34100  5.16700   1.000 82.37522  ? 72  ASN A HA   1 
ATOM   1127 H HB2  . ASN A 1 72  ? -28.71500 -3.53800  2.88600   1.000 91.71588  ? 72  ASN A HB2  1 
ATOM   1128 H HB3  . ASN A 1 72  ? -27.22000 -3.03100  3.06400   1.000 91.71588  ? 72  ASN A HB3  1 
ATOM   1129 H HD21 . ASN A 1 72  ? -25.70500 -5.57500  1.54000   1.000 100.87367 ? 72  ASN A HD21 1 
ATOM   1130 H HD22 . ASN A 1 72  ? -25.51300 -4.34300  2.35500   1.000 100.87367 ? 72  ASN A HD22 1 
ATOM   1131 N N    . VAL A 1 73  ? -28.75800 -6.23000  5.61700   1.000 60.11975  ? 73  VAL A N    1 
ATOM   1132 C CA   . VAL A 1 73  ? -29.72600 -7.28800  5.87700   1.000 55.09320  ? 73  VAL A CA   1 
ATOM   1133 C C    . VAL A 1 73  ? -30.24700 -7.10400  7.29600   1.000 53.48563  ? 73  VAL A C    1 
ATOM   1134 O O    . VAL A 1 73  ? -29.46100 -6.90900  8.22200   1.000 48.76105  ? 73  VAL A O    1 
ATOM   1135 C CB   . VAL A 1 73  ? -29.06500 -8.67000  5.73600   1.000 54.34807  ? 73  VAL A CB   1 
ATOM   1136 C CG1  . VAL A 1 73  ? -29.98700 -9.76500  6.23200   1.000 57.70928  ? 73  VAL A CG1  1 
ATOM   1137 C CG2  . VAL A 1 73  ? -28.58700 -8.92000  4.28700   1.000 62.01141  ? 73  VAL A CG2  1 
ATOM   1138 H H    . VAL A 1 73  ? -27.98500 -6.40100  5.95200   1.000 72.14450  ? 73  VAL A H    1 
ATOM   1139 H HA   . VAL A 1 73  ? -30.46700 -7.22400  5.25500   1.000 66.11264  ? 73  VAL A HA   1 
ATOM   1140 H HB   . VAL A 1 73  ? -28.27700 -8.68500  6.30100   1.000 65.21849  ? 73  VAL A HB   1 
ATOM   1141 H HG11 . VAL A 1 73  ? -29.67900 -10.61600 5.88300   1.000 69.25194  ? 73  VAL A HG11 1 
ATOM   1142 H HG12 . VAL A 1 73  ? -29.97000 -9.78200  7.20200   1.000 69.25194  ? 73  VAL A HG12 1 
ATOM   1143 H HG13 . VAL A 1 73  ? -30.88700 -9.58600  5.91700   1.000 69.25194  ? 73  VAL A HG13 1 
ATOM   1144 H HG21 . VAL A 1 73  ? -28.18200 -9.80000  4.23600   1.000 74.41449  ? 73  VAL A HG21 1 
ATOM   1145 H HG22 . VAL A 1 73  ? -29.35000 -8.87200  3.69000   1.000 74.41449  ? 73  VAL A HG22 1 
ATOM   1146 H HG23 . VAL A 1 73  ? -27.93700 -8.24100  4.04800   1.000 74.41449  ? 73  VAL A HG23 1 
ATOM   1147 N N    . GLN A 1 74  ? -31.56900 -7.14300  7.48100   1.000 56.29264  ? 74  GLN A N    1 
ATOM   1148 C CA   . GLN A 1 74  ? -32.14100 -7.08700  8.84800   1.000 49.89071  ? 74  GLN A CA   1 
ATOM   1149 C C    . GLN A 1 74  ? -32.38300 -8.50900  9.34300   1.000 50.24373  ? 74  GLN A C    1 
ATOM   1150 O O    . GLN A 1 74  ? -33.06400 -9.25700  8.63900   1.000 52.67440  ? 74  GLN A O    1 
ATOM   1151 C CB   . GLN A 1 74  ? -33.39300 -6.21600  8.89800   1.000 56.47271  ? 74  GLN A CB   1 
ATOM   1152 C CG   . GLN A 1 74  ? -34.08600 -6.22700  10.24900  1.000 62.22079  ? 74  GLN A CG   1 
ATOM   1153 C CD   . GLN A 1 74  ? -35.43800 -5.56200  10.19500  1.000 67.22506  ? 74  GLN A CD   1 
ATOM   1154 O OE1  . GLN A 1 74  ? -35.68800 -4.69400  9.36300   1.000 68.66996  ? 74  GLN A OE1  1 
ATOM   1155 N NE2  . GLN A 1 74  ? -36.31900 -5.96100  11.09600  1.000 61.23579  ? 74  GLN A NE2  1 
ATOM   1156 H H    . GLN A 1 74  ? -32.15200 -7.20000  6.85100   1.000 67.55197  ? 74  GLN A H    1 
ATOM   1157 H HA   . GLN A 1 74  ? -31.48900 -6.68200  9.44100   1.000 59.86966  ? 74  GLN A HA   1 
ATOM   1158 H HB2  . GLN A 1 74  ? -33.14500 -5.30000  8.69800   1.000 67.76805  ? 74  GLN A HB2  1 
ATOM   1159 H HB3  . GLN A 1 74  ? -34.02500 -6.53800  8.23700   1.000 67.76805  ? 74  GLN A HB3  1 
ATOM   1160 H HG2  . GLN A 1 74  ? -34.22100 -7.14100  10.54200  1.000 74.66575  ? 74  GLN A HG2  1 
ATOM   1161 H HG3  . GLN A 1 74  ? -33.53900 -5.74800  10.89100  1.000 74.66575  ? 74  GLN A HG3  1 
ATOM   1162 H HE21 . GLN A 1 74  ? -36.10700 -6.57100  11.66400  1.000 73.48375  ? 74  GLN A HE21 1 
ATOM   1163 H HE22 . GLN A 1 74  ? -37.10600 -5.61400  11.11100  1.000 73.48375  ? 74  GLN A HE22 1 
ATOM   1164 N N    . LEU A 1 75  ? -31.80800 -8.87100  10.48300  1.000 41.04708  ? 75  LEU A N    1 
ATOM   1165 C CA   . LEU A 1 75  ? -32.00300 -10.18900 11.08800  1.000 39.49247  ? 75  LEU A CA   1 
ATOM   1166 C C    . LEU A 1 75  ? -33.26400 -10.18900 11.94400  1.000 45.43965  ? 75  LEU A C    1 
ATOM   1167 O O    . LEU A 1 75  ? -33.50100 -9.24700  12.70600  1.000 53.66747  ? 75  LEU A O    1 
ATOM   1168 C CB   . LEU A 1 75  ? -30.81600 -10.59200 11.97000  1.000 41.54364  ? 75  LEU A CB   1 
ATOM   1169 C CG   . LEU A 1 75  ? -29.46400 -10.72800 11.29100  1.000 45.02896  ? 75  LEU A CG   1 
ATOM   1170 C CD1  . LEU A 1 75  ? -28.42700 -11.30400 12.29200  1.000 40.26300  ? 75  LEU A CD1  1 
ATOM   1171 C CD2  . LEU A 1 75  ? -29.67400 -11.58200 10.02300  1.000 49.31924  ? 75  LEU A CD2  1 
ATOM   1172 H H    . LEU A 1 75  ? -31.28700 -8.36000  10.93800  1.000 49.25730  ? 75  LEU A H    1 
ATOM   1173 H HA   . LEU A 1 75  ? -32.12000 -10.85100 10.39000  1.000 47.39177  ? 75  LEU A HA   1 
ATOM   1174 H HB2  . LEU A 1 75  ? -30.71900 -9.92500  12.66800  1.000 49.85316  ? 75  LEU A HB2  1 
ATOM   1175 H HB3  . LEU A 1 75  ? -31.01900 -11.45000 12.37500  1.000 49.85316  ? 75  LEU A HB3  1 
ATOM   1176 H HG   . LEU A 1 75  ? -29.15900 -9.85000  11.01500  1.000 54.03556  ? 75  LEU A HG   1 
ATOM   1177 H HD11 . LEU A 1 75  ? -27.56500 -11.36800 11.85100  1.000 48.31640  ? 75  LEU A HD11 1 
ATOM   1178 H HD12 . LEU A 1 75  ? -28.36400 -10.71100 13.05700  1.000 48.31640  ? 75  LEU A HD12 1 
ATOM   1179 H HD13 . LEU A 1 75  ? -28.71900 -12.18400 12.57800  1.000 48.31640  ? 75  LEU A HD13 1 
ATOM   1180 H HD21 . LEU A 1 75  ? -28.81300 -11.90700 9.71600   1.000 59.18389  ? 75  LEU A HD21 1 
ATOM   1181 H HD22 . LEU A 1 75  ? -30.25300 -12.33000 10.23900  1.000 59.18389  ? 75  LEU A HD22 1 
ATOM   1182 H HD23 . LEU A 1 75  ? -30.08400 -11.03400 9.33600   1.000 59.18389  ? 75  LEU A HD23 1 
ATOM   1183 N N    . ARG A 1 76  ? -34.03900 -11.27100 11.86900  1.000 39.93556  ? 76  ARG A N    1 
ATOM   1184 C CA   . ARG A 1 76  ? -35.27400 -11.39400 12.65900  1.000 46.58256  ? 76  ARG A CA   1 
ATOM   1185 C C    . ARG A 1 76  ? -34.98000 -11.95800 14.05400  1.000 43.78258  ? 76  ARG A C    1 
ATOM   1186 O O    . ARG A 1 76  ? -34.45600 -13.07000 14.19600  1.000 44.11536  ? 76  ARG A O    1 
ATOM   1187 C CB   . ARG A 1 76  ? -36.28800 -12.26000 11.90800  1.000 50.89870  ? 76  ARG A CB   1 
ATOM   1188 C CG   . ARG A 1 76  ? -37.51500 -12.71500 12.72100  1.000 57.09324  ? 76  ARG A CG   1 
ATOM   1189 C CD   . ARG A 1 76  ? -38.52500 -13.36400 11.79700  1.000 61.22350  ? 76  ARG A CD   1 
ATOM   1190 N NE   . ARG A 1 76  ? -39.38200 -14.33300 12.47200  1.000 69.44176  ? 76  ARG A NE   1 
ATOM   1191 C CZ   . ARG A 1 76  ? -40.35000 -14.03300 13.32600  1.000 73.69268  ? 76  ARG A CZ   1 
ATOM   1192 N NH1  . ARG A 1 76  ? -40.60700 -12.77700 13.66600  1.000 74.45660  ? 76  ARG A NH1  1 
ATOM   1193 N NH2  . ARG A 1 76  ? -41.07000 -15.02000 13.86400  1.000 72.46560  ? 76  ARG A NH2  1 
ATOM   1194 H H    . ARG A 1 76  ? -33.87500 -11.95100 11.36900  1.000 47.92347  ? 76  ARG A H    1 
ATOM   1195 H HA   . ARG A 1 76  ? -35.66300 -10.51300 12.77200  1.000 55.89987  ? 76  ARG A HA   1 
ATOM   1196 H HB2  . ARG A 1 76  ? -36.61700 -11.75400 11.14900  1.000 61.07924  ? 76  ARG A HB2  1 
ATOM   1197 H HB3  . ARG A 1 76  ? -35.83300 -13.05300 11.59200  1.000 61.07924  ? 76  ARG A HB3  1 
ATOM   1198 H HG2  . ARG A 1 76  ? -37.24300 -13.36600 13.38700  1.000 68.51269  ? 76  ARG A HG2  1 
ATOM   1199 H HG3  . ARG A 1 76  ? -37.93000 -11.94700 13.14300  1.000 68.51269  ? 76  ARG A HG3  1 
ATOM   1200 H HD2  . ARG A 1 76  ? -38.99100 -12.75000 11.20800  1.000 73.46900  ? 76  ARG A HD2  1 
ATOM   1201 H HD3  . ARG A 1 76  ? -37.85400 -13.87700 11.39000  1.000 73.46900  ? 76  ARG A HD3  1 
ATOM   1202 H HE   . ARG A 1 76  ? -39.24800 -15.16500 12.30200  1.000 83.33091  ? 76  ARG A HE   1 
ATOM   1203 H HH11 . ARG A 1 76  ? -40.14800 -12.13500 13.32600  1.000 89.34872  ? 76  ARG A HH11 1 
ATOM   1204 H HH12 . ARG A 1 76  ? -41.23800 -12.60400 14.22400  1.000 89.34872  ? 76  ARG A HH12 1 
ATOM   1205 H HH21 . ARG A 1 76  ? -40.90700 -15.83700 13.65000  1.000 86.95952  ? 76  ARG A HH21 1 
ATOM   1206 H HH22 . ARG A 1 76  ? -41.69900 -14.83900 14.42200  1.000 86.95952  ? 76  ARG A HH22 1 
ATOM   1207 N N    . VAL A 1 77  ? -35.30500 -11.19200 15.09100  1.000 45.03219  ? 77  VAL A N    1 
ATOM   1208 C CA   . VAL A 1 77  ? -35.10200 -11.67000 16.46200  1.000 40.23746  ? 77  VAL A CA   1 
ATOM   1209 C C    . VAL A 1 77  ? -36.28100 -12.55000 16.86700  1.000 43.24016  ? 77  VAL A C    1 
ATOM   1210 O O    . VAL A 1 77  ? -37.44800 -12.16800 16.71300  1.000 42.36383  ? 77  VAL A O    1 
ATOM   1211 C CB   . VAL A 1 77  ? -34.91600 -10.48900 17.42700  1.000 39.36952  ? 77  VAL A CB   1 
ATOM   1212 C CG1  . VAL A 1 77  ? -34.87300 -10.98700 18.90400  1.000 42.02925  ? 77  VAL A CG1  1 
ATOM   1213 C CG2  . VAL A 1 77  ? -33.64500 -9.69400  17.03700  1.000 39.97772  ? 77  VAL A CG2  1 
ATOM   1214 H H    . VAL A 1 77  ? -35.64000 -10.40200 15.03300  1.000 54.03943  ? 77  VAL A H    1 
ATOM   1215 H HA   . VAL A 1 77  ? -34.29800 -12.21200 16.49400  1.000 48.28575  ? 77  VAL A HA   1 
ATOM   1216 H HB   . VAL A 1 77  ? -35.67600 -9.89200  17.33900  1.000 47.24422  ? 77  VAL A HB   1 
ATOM   1217 H HG11 . VAL A 1 77  ? -34.54400 -10.26900 19.46700  1.000 50.43591  ? 77  VAL A HG11 1 
ATOM   1218 H HG12 . VAL A 1 77  ? -35.76700 -11.24000 19.18100  1.000 50.43591  ? 77  VAL A HG12 1 
ATOM   1219 H HG13 . VAL A 1 77  ? -34.27800 -11.75100 18.96200  1.000 50.43591  ? 77  VAL A HG13 1 
ATOM   1220 H HG21 . VAL A 1 77  ? -33.51600 -8.97400  17.67400  1.000 47.97407  ? 77  VAL A HG21 1 
ATOM   1221 H HG22 . VAL A 1 77  ? -32.88200 -10.29200 17.05400  1.000 47.97407  ? 77  VAL A HG22 1 
ATOM   1222 H HG23 . VAL A 1 77  ? -33.76100 -9.33000  16.14500  1.000 47.97407  ? 77  VAL A HG23 1 
ATOM   1223 N N    . ILE A 1 78  ? -35.98700 -13.76500 17.33400  1.000 41.90478  ? 78  ILE A N    1 
ATOM   1224 C CA   . ILE A 1 78  ? -37.03800 -14.72100 17.69200  1.000 45.94998  ? 78  ILE A CA   1 
ATOM   1225 C C    . ILE A 1 78  ? -37.00800 -15.09500 19.16300  1.000 46.24106  ? 78  ILE A C    1 
ATOM   1226 O O    . ILE A 1 78  ? -37.82000 -15.92000 19.60300  1.000 44.53202  ? 78  ILE A O    1 
ATOM   1227 C CB   . ILE A 1 78  ? -36.95900 -15.99300 16.81600  1.000 47.73859  ? 78  ILE A CB   1 
ATOM   1228 C CG1  . ILE A 1 78  ? -35.61300 -16.70500 17.01700  1.000 45.63619  ? 78  ILE A CG1  1 
ATOM   1229 C CG2  . ILE A 1 78  ? -37.13000 -15.63100 15.36300  1.000 47.01197  ? 78  ILE A CG2  1 
ATOM   1230 C CD1  . ILE A 1 78  ? -35.57100 -18.09700 16.39500  1.000 50.37902  ? 78  ILE A CD1  1 
ATOM   1231 H H    . ILE A 1 78  ? -35.18800 -14.06000 17.45300  1.000 50.28654  ? 78  ILE A H    1 
ATOM   1232 H HA   . ILE A 1 78  ? -37.90000 -14.31200 17.52100  1.000 55.14078  ? 78  ILE A HA   1 
ATOM   1233 H HB   . ILE A 1 78  ? -37.67400 -16.59600 17.07500  1.000 57.28711  ? 78  ILE A HB   1 
ATOM   1234 H HG12 . ILE A 1 78  ? -34.91300 -16.17400 16.60600  1.000 54.76422  ? 78  ILE A HG12 1 
ATOM   1235 H HG13 . ILE A 1 78  ? -35.43800 -16.80400 17.96500  1.000 54.76422  ? 78  ILE A HG13 1 
ATOM   1236 H HG21 . ILE A 1 78  ? -37.20000 -16.44500 14.84000  1.000 56.41517  ? 78  ILE A HG21 1 
ATOM   1237 H HG22 . ILE A 1 78  ? -37.93800 -15.10400 15.26300  1.000 56.41517  ? 78  ILE A HG22 1 
ATOM   1238 H HG23 . ILE A 1 78  ? -36.36100 -15.11500 15.07300  1.000 56.41517  ? 78  ILE A HG23 1 
ATOM   1239 H HD11 . ILE A 1 78  ? -34.73100 -18.52200 16.63000  1.000 60.45563  ? 78  ILE A HD11 1 
ATOM   1240 H HD12 . ILE A 1 78  ? -36.31300 -18.61800 16.73900  1.000 60.45563  ? 78  ILE A HD12 1 
ATOM   1241 H HD13 . ILE A 1 78  ? -35.64200 -18.01500 15.43100  1.000 60.45563  ? 78  ILE A HD13 1 
ATOM   1242 N N    . GLY A 1 79  ? -36.13700 -14.48800 19.94500  1.000 43.39795  ? 79  GLY A N    1 
ATOM   1243 C CA   . GLY A 1 79  ? -36.11500 -14.73300 21.37700  1.000 40.63268  ? 79  GLY A CA   1 
ATOM   1244 C C    . GLY A 1 79  ? -35.05500 -13.85700 22.00500  1.000 40.34880  ? 79  GLY A C    1 
ATOM   1245 O O    . GLY A 1 79  ? -34.16600 -13.34000 21.32100  1.000 36.64795  ? 79  GLY A O    1 
ATOM   1246 H H    . GLY A 1 79  ? -35.54400 -13.92700 19.67500  1.000 52.07834  ? 79  GLY A H    1 
ATOM   1247 H HA2  . GLY A 1 79  ? -36.97700 -14.52000 21.76700  1.000 48.76002  ? 79  GLY A HA2  1 
ATOM   1248 H HA3  . GLY A 1 79  ? -35.90600 -15.66300 21.55500  1.000 48.76002  ? 79  GLY A HA3  1 
ATOM   1249 N N    . HIS A 1 80  ? -35.15200 -13.71000 23.33500  1.000 41.14022  ? 80  HIS A N    1 
ATOM   1250 C CA   . HIS A 1 80  ? -34.14500 -12.88100 23.99500  1.000 43.75729  ? 80  HIS A CA   1 
ATOM   1251 C C    . HIS A 1 80  ? -34.04700 -13.28000 25.45200  1.000 44.86221  ? 80  HIS A C    1 
ATOM   1252 O O    . HIS A 1 80  ? -35.04600 -13.67600 26.06900  1.000 40.86805  ? 80  HIS A O    1 
ATOM   1253 C CB   . HIS A 1 80  ? -34.48000 -11.38700 23.87000  1.000 40.10839  ? 80  HIS A CB   1 
ATOM   1254 C CG   . HIS A 1 80  ? -35.79400 -11.01200 24.48700  1.000 43.82162  ? 80  HIS A CG   1 
ATOM   1255 N ND1  . HIS A 1 80  ? -36.96800 -10.94200 23.76600  1.000 47.34375  ? 80  HIS A ND1  1 
ATOM   1256 C CD2  . HIS A 1 80  ? -36.12200 -10.70300 25.76700  1.000 40.01194  ? 80  HIS A CD2  1 
ATOM   1257 C CE1  . HIS A 1 80  ? -37.96300 -10.59900 24.57200  1.000 48.61846  ? 80  HIS A CE1  1 
ATOM   1258 N NE2  . HIS A 1 80  ? -37.46700 -10.42200 25.78300  1.000 41.29978  ? 80  HIS A NE2  1 
ATOM   1259 H H    . HIS A 1 80  ? -35.75100 -14.05600 23.84500  1.000 49.36906  ? 80  HIS A H    1 
ATOM   1260 H HA   . HIS A 1 80  ? -33.28400 -13.03500 23.57900  1.000 52.50955  ? 80  HIS A HA   1 
ATOM   1261 H HB2  . HIS A 1 80  ? -33.78700 -10.87300 24.31200  1.000 48.13087  ? 80  HIS A HB2  1 
ATOM   1262 H HB3  . HIS A 1 80  ? -34.51500 -11.15200 22.93000  1.000 48.13087  ? 80  HIS A HB3  1 
ATOM   1263 H HD1  . HIS A 1 80  ? -37.04300 -11.10000 22.92400  1.000 56.81330  ? 80  HIS A HD1  1 
ATOM   1264 H HD2  . HIS A 1 80  ? -35.53900 -10.65500 26.49000  1.000 48.01513  ? 80  HIS A HD2  1 
ATOM   1265 H HE1  . HIS A 1 80  ? -38.85000 -10.47600 24.32200  1.000 58.34295  ? 80  HIS A HE1  1 
ATOM   1266 N N    . SER A 1 81  ? -32.83200 -13.19400 25.98200  1.000 39.78801  ? 81  SER A N    1 
ATOM   1267 C CA   . SER A 1 81  ? -32.60400 -13.40300 27.40300  1.000 40.52289  ? 81  SER A CA   1 
ATOM   1268 C C    . SER A 1 81  ? -31.40200 -12.59300 27.83600  1.000 39.69137  ? 81  SER A C    1 
ATOM   1269 O O    . SER A 1 81  ? -30.58900 -12.15400 27.02900  1.000 37.63100  ? 81  SER A O    1 
ATOM   1270 C CB   . SER A 1 81  ? -32.34800 -14.86400 27.77200  1.000 46.01341  ? 81  SER A CB   1 
ATOM   1271 O OG   . SER A 1 81  ? -31.22200 -15.32200 27.07400  1.000 42.18393  ? 81  SER A OG   1 
ATOM   1272 H H    . SER A 1 81  ? -32.11900 -13.01500 25.53500  1.000 47.74642  ? 81  SER A H    1 
ATOM   1273 H HA   . SER A 1 81  ? -33.37700 -13.09300 27.90100  1.000 48.62826  ? 81  SER A HA   1 
ATOM   1274 H HB2  . SER A 1 81  ? -32.18400 -14.93100 28.72600  1.000 55.21689  ? 81  SER A HB2  1 
ATOM   1275 H HB3  . SER A 1 81  ? -33.11900 -15.39800 27.52400  1.000 55.21689  ? 81  SER A HB3  1 
ATOM   1276 H HG   . SER A 1 81  ? -31.07000 -16.12500 27.26800  1.000 50.62152  ? 81  SER A HG   1 
ATOM   1277 N N    . MET A 1 82  ? -31.28700 -12.43000 29.13900  1.000 34.66931  ? 82  MET A N    1 
ATOM   1278 C CA   . MET A 1 82  ? -30.22200 -11.64200 29.70300  1.000 32.87425  ? 82  MET A CA   1 
ATOM   1279 C C    . MET A 1 82  ? -29.37400 -12.58400 30.53600  1.000 37.40208  ? 82  MET A C    1 
ATOM   1280 O O    . MET A 1 82  ? -29.91100 -13.42300 31.27900  1.000 36.90233  ? 82  MET A O    1 
ATOM   1281 C CB   . MET A 1 82  ? -30.80100 -10.52400 30.55800  1.000 36.34825  ? 82  MET A CB   1 
ATOM   1282 C CG   . MET A 1 82  ? -29.81500 -9.66900  31.21400  1.000 35.87333  ? 82  MET A CG   1 
ATOM   1283 S SD   . MET A 1 82  ? -30.71300 -8.29500  31.96100  1.000 39.93286  ? 82  MET A SD   1 
ATOM   1284 C CE   . MET A 1 82  ? -31.87100 -9.06500  33.10900  1.000 42.65993  ? 82  MET A CE   1 
ATOM   1285 H H    . MET A 1 82  ? -31.82000 -12.77000 29.72100  1.000 41.60397  ? 82  MET A H    1 
ATOM   1286 H HA   . MET A 1 82  ? -29.68300 -11.24900 28.99900  1.000 39.44990  ? 82  MET A HA   1 
ATOM   1287 H HB2  . MET A 1 82  ? -31.35000 -9.95800  29.99400  1.000 43.61871  ? 82  MET A HB2  1 
ATOM   1288 H HB3  . MET A 1 82  ? -31.34900 -10.92600 31.24900  1.000 43.61871  ? 82  MET A HB3  1 
ATOM   1289 H HG2  . MET A 1 82  ? -29.35500 -10.16300 31.91100  1.000 43.04880  ? 82  MET A HG2  1 
ATOM   1290 H HG3  . MET A 1 82  ? -29.18800 -9.32100  30.56100  1.000 43.04880  ? 82  MET A HG3  1 
ATOM   1291 H HE1  . MET A 1 82  ? -32.29400 -8.37200  33.64000  1.000 51.19271  ? 82  MET A HE1  1 
ATOM   1292 H HE2  . MET A 1 82  ? -32.54200 -9.55000  32.60400  1.000 51.19271  ? 82  MET A HE2  1 
ATOM   1293 H HE3  . MET A 1 82  ? -31.38500 -9.67400  33.68700  1.000 51.19271  ? 82  MET A HE3  1 
ATOM   1294 N N    . GLN A 1 83  ? -28.07000 -12.46600 30.38600  1.000 33.26459  ? 83  GLN A N    1 
ATOM   1295 C CA   . GLN A 1 83  ? -27.11800 -13.21900 31.18400  1.000 33.76457  ? 83  GLN A CA   1 
ATOM   1296 C C    . GLN A 1 83  ? -26.17000 -12.20800 31.79400  1.000 33.63525  ? 83  GLN A C    1 
ATOM   1297 O O    . GLN A 1 83  ? -25.30700 -11.65600 31.09500  1.000 30.57380  ? 83  GLN A O    1 
ATOM   1298 C CB   . GLN A 1 83  ? -26.37300 -14.25600 30.33700  1.000 36.28091  ? 83  GLN A CB   1 
ATOM   1299 C CG   . GLN A 1 83  ? -25.29600 -14.98100 31.14700  1.000 37.93818  ? 83  GLN A CG   1 
ATOM   1300 C CD   . GLN A 1 83  ? -24.52700 -16.03000 30.35900  1.000 39.43240  ? 83  GLN A CD   1 
ATOM   1301 O OE1  . GLN A 1 83  ? -24.62700 -16.10600 29.13600  1.000 39.39020  ? 83  GLN A OE1  1 
ATOM   1302 N NE2  . GLN A 1 83  ? -23.73100 -16.83600 31.06700  1.000 45.04582  ? 83  GLN A NE2  1 
ATOM   1303 H H    . GLN A 1 83  ? -27.69900 -11.94200 29.81300  1.000 39.91830  ? 83  GLN A H    1 
ATOM   1304 H HA   . GLN A 1 83  ? -27.58100 -13.68000 31.90100  1.000 40.51829  ? 83  GLN A HA   1 
ATOM   1305 H HB2  . GLN A 1 83  ? -27.00500 -14.91700 30.01300  1.000 43.53789  ? 83  GLN A HB2  1 
ATOM   1306 H HB3  . GLN A 1 83  ? -25.94300 -13.81000 29.59100  1.000 43.53789  ? 83  GLN A HB3  1 
ATOM   1307 H HG2  . GLN A 1 83  ? -24.65100 -14.33300 31.47000  1.000 45.52662  ? 83  GLN A HG2  1 
ATOM   1308 H HG3  . GLN A 1 83  ? -25.71800 -15.42600 31.89900  1.000 45.52662  ? 83  GLN A HG3  1 
ATOM   1309 H HE21 . GLN A 1 83  ? -23.68300 -16.75100 31.92100  1.000 54.05579  ? 83  GLN A HE21 1 
ATOM   1310 H HE22 . GLN A 1 83  ? -23.27300 -17.44500 30.66900  1.000 54.05579  ? 83  GLN A HE22 1 
ATOM   1311 N N    . ASN A 1 84  ? -26.30800 -11.98300 33.10800  1.000 29.90762  ? 84  ASN A N    1 
ATOM   1312 C CA   . ASN A 1 84  ? -25.49300 -10.96900 33.75900  1.000 30.61803  ? 84  ASN A CA   1 
ATOM   1313 C C    . ASN A 1 84  ? -25.67700 -9.66200  32.98700  1.000 29.28102  ? 84  ASN A C    1 
ATOM   1314 O O    . ASN A 1 84  ? -26.82100 -9.22000  32.83400  1.000 30.82877  ? 84  ASN A O    1 
ATOM   1315 C CB   . ASN A 1 84  ? -24.04300 -11.45700 33.86200  1.000 30.73639  ? 84  ASN A CB   1 
ATOM   1316 C CG   . ASN A 1 84  ? -23.96000 -12.76000 34.61800  1.000 35.25361  ? 84  ASN A CG   1 
ATOM   1317 O OD1  . ASN A 1 84  ? -24.55200 -12.86000 35.69600  1.000 33.72690  ? 84  ASN A OD1  1 
ATOM   1318 N ND2  . ASN A 1 84  ? -23.33900 -13.79800 34.02000  1.000 31.61428  ? 84  ASN A ND2  1 
ATOM   1319 H H    . ASN A 1 84  ? -26.85500 -12.39700 33.62700  1.000 35.88994  ? 84  ASN A H    1 
ATOM   1320 H HA   . ASN A 1 84  ? -25.82400 -10.83100 34.66000  1.000 36.74244  ? 84  ASN A HA   1 
ATOM   1321 H HB2  . ASN A 1 84  ? -23.68600 -11.59800 32.97100  1.000 36.88447  ? 84  ASN A HB2  1 
ATOM   1322 H HB3  . ASN A 1 84  ? -23.51500 -10.79600 34.33600  1.000 36.88447  ? 84  ASN A HB3  1 
ATOM   1323 H HD21 . ASN A 1 84  ? -23.28600 -14.55600 34.42200  1.000 37.93794  ? 84  ASN A HD21 1 
ATOM   1324 H HD22 . ASN A 1 84  ? -22.95700 -13.68800 33.25700  1.000 37.93794  ? 84  ASN A HD22 1 
ATOM   1325 N N    . CYS A 1 85  ? -24.60900 -9.02900  32.50300  1.000 26.67658  ? 85  CYS A N    1 
ATOM   1326 C CA   . CYS A 1 85  ? -24.73500 -7.73400  31.84100  1.000 27.24856  ? 85  CYS A CA   1 
ATOM   1327 C C    . CYS A 1 85  ? -24.77700 -7.83300  30.31800  1.000 27.04295  ? 85  CYS A C    1 
ATOM   1328 O O    . CYS A 1 85  ? -24.65100 -6.81200  29.63500  1.000 25.48964  ? 85  CYS A O    1 
ATOM   1329 C CB   . CYS A 1 85  ? -23.61700 -6.80300  32.27400  1.000 27.57703  ? 85  CYS A CB   1 
ATOM   1330 S SG   . CYS A 1 85  ? -23.67900 -6.49100  34.06500  1.000 28.92635  ? 85  CYS A SG   1 
ATOM   1331 H H    . CYS A 1 85  ? -23.80300 -9.32600  32.54400  1.000 32.01269  ? 85  CYS A H    1 
ATOM   1332 H HA   . CYS A 1 85  ? -25.56700 -7.32700  32.12400  1.000 32.69907  ? 85  CYS A HA   1 
ATOM   1333 H HB2  . CYS A 1 85  ? -22.76200 -7.20900  32.06400  1.000 33.09324  ? 85  CYS A HB2  1 
ATOM   1334 H HB3  . CYS A 1 85  ? -23.70900 -5.95400  31.81300  1.000 33.09324  ? 85  CYS A HB3  1 
ATOM   1335 H HG   . CYS A 1 85  ? -22.81100 -5.73200  34.38900  1.000 34.71242  ? 85  CYS A HG   1 
ATOM   1336 N N    . VAL A 1 86  ? -25.01000 -9.01900  29.77300  1.000 27.58039  ? 86  VAL A N    1 
ATOM   1337 C CA   . VAL A 1 86  ? -25.07400 -9.19000  28.32700  1.000 26.52266  ? 86  VAL A CA   1 
ATOM   1338 C C    . VAL A 1 86  ? -26.45800 -9.69100  27.92400  1.000 28.18900  ? 86  VAL A C    1 
ATOM   1339 O O    . VAL A 1 86  ? -27.09100 -10.49700 28.62200  1.000 31.32795  ? 86  VAL A O    1 
ATOM   1340 C CB   . VAL A 1 86  ? -23.93600 -10.13600 27.88800  1.000 27.88356  ? 86  VAL A CB   1 
ATOM   1341 C CG1  . VAL A 1 86  ? -24.31700 -10.93600 26.74300  1.000 39.08571  ? 86  VAL A CG1  1 
ATOM   1342 C CG2  . VAL A 1 86  ? -22.66100 -9.25200  27.59800  1.000 29.54460  ? 86  VAL A CG2  1 
ATOM   1343 H H    . VAL A 1 86  ? -25.13500 -9.74400  30.21900  1.000 33.09727  ? 86  VAL A H    1 
ATOM   1344 H HA   . VAL A 1 86  ? -24.93200 -8.33500  27.89300  1.000 31.82799  ? 86  VAL A HA   1 
ATOM   1345 H HB   . VAL A 1 86  ? -23.72500 -10.73800 28.61900  1.000 33.46107  ? 86  VAL A HB   1 
ATOM   1346 H HG11 . VAL A 1 86  ? -23.52200 -11.36100 26.38600  1.000 46.90365  ? 86  VAL A HG11 1 
ATOM   1347 H HG12 . VAL A 1 86  ? -24.95100 -11.61600 27.02000  1.000 46.90365  ? 86  VAL A HG12 1 
ATOM   1348 H HG13 . VAL A 1 86  ? -24.71000 -10.36200 26.06600  1.000 46.90365  ? 86  VAL A HG13 1 
ATOM   1349 H HG21 . VAL A 1 86  ? -21.92400 -9.83300  27.35200  1.000 35.45432  ? 86  VAL A HG21 1 
ATOM   1350 H HG22 . VAL A 1 86  ? -22.85900 -8.64200  26.87000  1.000 35.45432  ? 86  VAL A HG22 1 
ATOM   1351 H HG23 . VAL A 1 86  ? -22.43600 -8.75200  28.39800  1.000 35.45432  ? 86  VAL A HG23 1 
ATOM   1352 N N    . LEU A 1 87  ? -26.96000 -9.14300  26.82500  1.000 27.98949  ? 87  LEU A N    1 
ATOM   1353 C CA   . LEU A 1 87  ? -28.19000 -9.60000  26.23700  1.000 27.16524  ? 87  LEU A CA   1 
ATOM   1354 C C    . LEU A 1 87  ? -27.89400 -10.60600 25.12900  1.000 30.79606  ? 87  LEU A C    1 
ATOM   1355 O O    . LEU A 1 87  ? -26.93200 -10.44400 24.35700  1.000 29.21080  ? 87  LEU A O    1 
ATOM   1356 C CB   . LEU A 1 87  ? -28.92200 -8.37100  25.71200  1.000 34.70172  ? 87  LEU A CB   1 
ATOM   1357 C CG   . LEU A 1 87  ? -30.29300 -8.39200  25.10400  1.000 40.52532  ? 87  LEU A CG   1 
ATOM   1358 C CD1  . LEU A 1 87  ? -31.38100 -8.88800  26.09200  1.000 41.86729  ? 87  LEU A CD1  1 
ATOM   1359 C CD2  . LEU A 1 87  ? -30.58800 -6.98800  24.60900  1.000 39.95501  ? 87  LEU A CD2  1 
ATOM   1360 H H    . LEU A 1 87  ? -26.59200 -8.49200  26.39900  1.000 33.58819  ? 87  LEU A H    1 
ATOM   1361 H HA   . LEU A 1 87  ? -28.74100 -10.02800 26.91000  1.000 32.59909  ? 87  LEU A HA   1 
ATOM   1362 H HB2  . LEU A 1 87  ? -28.97900 -7.75000  26.45500  1.000 41.64287  ? 87  LEU A HB2  1 
ATOM   1363 H HB3  . LEU A 1 87  ? -28.34700 -7.97800  25.03700  1.000 41.64287  ? 87  LEU A HB3  1 
ATOM   1364 H HG   . LEU A 1 87  ? -30.29000 -8.98600  24.33700  1.000 48.63119  ? 87  LEU A HG   1 
ATOM   1365 H HD11 . LEU A 1 87  ? -32.24100 -8.88000  25.64400  1.000 50.24155  ? 87  LEU A HD11 1 
ATOM   1366 H HD12 . LEU A 1 87  ? -31.16300 -9.79000  26.37500  1.000 50.24155  ? 87  LEU A HD12 1 
ATOM   1367 H HD13 . LEU A 1 87  ? -31.40300 -8.29600  26.86000  1.000 50.24155  ? 87  LEU A HD13 1 
ATOM   1368 H HD21 . LEU A 1 87  ? -31.53200 -6.92400  24.40200  1.000 47.94682  ? 87  LEU A HD21 1 
ATOM   1369 H HD22 . LEU A 1 87  ? -30.35900 -6.35200  25.30500  1.000 47.94682  ? 87  LEU A HD22 1 
ATOM   1370 H HD23 . LEU A 1 87  ? -30.05900 -6.81400  23.81500  1.000 47.94682  ? 87  LEU A HD23 1 
ATOM   1371 N N    . LYS A 1 88  ? -28.69600 -11.66300 25.07700  1.000 34.55650  ? 88  LYS A N    1 
ATOM   1372 C CA   . LYS A 1 88  ? -28.57600 -12.69600 24.06700  1.000 35.12930  ? 88  LYS A CA   1 
ATOM   1373 C C    . LYS A 1 88  ? -29.83900 -12.67300 23.23100  1.000 35.47326  ? 88  LYS A C    1 
ATOM   1374 O O    . LYS A 1 88  ? -30.92700 -13.03800 23.70300  1.000 35.03855  ? 88  LYS A O    1 
ATOM   1375 C CB   . LYS A 1 88  ? -28.33900 -14.06600 24.67700  1.000 38.64017  ? 88  LYS A CB   1 
ATOM   1376 C CG   . LYS A 1 88  ? -27.08100 -14.09100 25.49000  1.000 38.34185  ? 88  LYS A CG   1 
ATOM   1377 C CD   . LYS A 1 88  ? -26.61800 -15.48400 25.86400  1.000 45.19529  ? 88  LYS A CD   1 
ATOM   1378 C CE   . LYS A 1 88  ? -27.41400 -16.01000 27.00400  1.000 48.87245  ? 88  LYS A CE   1 
ATOM   1379 N NZ   . LYS A 1 88  ? -26.89800 -17.30900 27.47300  1.000 60.45028  ? 88  LYS A NZ   1 
ATOM   1380 H H    . LYS A 1 88  ? -29.33500 -11.80400 25.63500  1.000 41.46860  ? 88  LYS A H    1 
ATOM   1381 H HA   . LYS A 1 88  ? -27.82700 -12.49200 23.48600  1.000 42.15596  ? 88  LYS A HA   1 
ATOM   1382 H HB2  . LYS A 1 88  ? -29.08200 -14.29100 25.25900  1.000 46.36901  ? 88  LYS A HB2  1 
ATOM   1383 H HB3  . LYS A 1 88  ? -28.25700 -14.72200 23.96800  1.000 46.36901  ? 88  LYS A HB3  1 
ATOM   1384 H HG2  . LYS A 1 88  ? -26.37100 -13.67100 24.97900  1.000 46.01102  ? 88  LYS A HG2  1 
ATOM   1385 H HG3  . LYS A 1 88  ? -27.23000 -13.59700 26.31100  1.000 46.01102  ? 88  LYS A HG3  1 
ATOM   1386 H HD2  . LYS A 1 88  ? -26.73600 -16.07900 25.10700  1.000 54.23515  ? 88  LYS A HD2  1 
ATOM   1387 H HD3  . LYS A 1 88  ? -25.68500 -15.45400 26.12900  1.000 54.23515  ? 88  LYS A HD3  1 
ATOM   1388 H HE2  . LYS A 1 88  ? -27.36800 -15.38300 27.74200  1.000 58.64774  ? 88  LYS A HE2  1 
ATOM   1389 H HE3  . LYS A 1 88  ? -28.33500 -16.13100 26.72500  1.000 58.64774  ? 88  LYS A HE3  1 
ATOM   1390 H HZ1  . LYS A 1 88  ? -27.38900 -17.60300 28.15400  1.000 72.54113  ? 88  LYS A HZ1  1 
ATOM   1391 H HZ2  . LYS A 1 88  ? -26.93200 -17.90500 26.81300  1.000 72.54113  ? 88  LYS A HZ2  1 
ATOM   1392 H HZ3  . LYS A 1 88  ? -26.05400 -17.22200 27.74200  1.000 72.54113  ? 88  LYS A HZ3  1 
ATOM   1393 N N    . LEU A 1 89  ? -29.69900 -12.19800 22.00200  1.000 32.02400  ? 89  LEU A N    1 
ATOM   1394 C CA   . LEU A 1 89  ? -30.80700 -12.11800 21.06500  1.000 30.02636  ? 89  LEU A CA   1 
ATOM   1395 C C    . LEU A 1 89  ? -30.71700 -13.33200 20.15400  1.000 37.35374  ? 89  LEU A C    1 
ATOM   1396 O O    . LEU A 1 89  ? -29.74700 -13.48000 19.39900  1.000 37.28719  ? 89  LEU A O    1 
ATOM   1397 C CB   . LEU A 1 89  ? -30.75500 -10.82800 20.26600  1.000 33.39215  ? 89  LEU A CB   1 
ATOM   1398 C CG   . LEU A 1 89  ? -30.66900 -9.52300  21.04600  1.000 37.97374  ? 89  LEU A CG   1 
ATOM   1399 C CD1  . LEU A 1 89  ? -30.53400 -8.39600  20.03700  1.000 38.72089  ? 89  LEU A CD1  1 
ATOM   1400 C CD2  . LEU A 1 89  ? -31.96200 -9.35700  21.90500  1.000 36.37108  ? 89  LEU A CD2  1 
ATOM   1401 H H    . LEU A 1 89  ? -28.95500 -11.91000 21.68100  1.000 38.42960  ? 89  LEU A H    1 
ATOM   1402 H HA   . LEU A 1 89  ? -31.64900 -12.15200 21.54600  1.000 36.03243  ? 89  LEU A HA   1 
ATOM   1403 H HB2  . LEU A 1 89  ? -29.97800 -10.86500 19.68700  1.000 40.07139  ? 89  LEU A HB2  1 
ATOM   1404 H HB3  . LEU A 1 89  ? -31.55600 -10.78100 19.72100  1.000 40.07139  ? 89  LEU A HB3  1 
ATOM   1405 H HG   . LEU A 1 89  ? -29.89300 -9.52800  21.62800  1.000 45.56929  ? 89  LEU A HG   1 
ATOM   1406 H HD11 . LEU A 1 89  ? -30.48800 -7.55200  20.51200  1.000 46.46587  ? 89  LEU A HD11 1 
ATOM   1407 H HD12 . LEU A 1 89  ? -29.72400 -8.53000  19.52000  1.000 46.46587  ? 89  LEU A HD12 1 
ATOM   1408 H HD13 . LEU A 1 89  ? -31.30600 -8.40400  19.45000  1.000 46.46587  ? 89  LEU A HD13 1 
ATOM   1409 H HD21 . LEU A 1 89  ? -31.93100 -8.50000  22.35800  1.000 43.64609  ? 89  LEU A HD21 1 
ATOM   1410 H HD22 . LEU A 1 89  ? -32.73500 -9.39500  21.32100  1.000 43.64609  ? 89  LEU A HD22 1 
ATOM   1411 H HD23 . LEU A 1 89  ? -32.00300 -10.07500 22.55600  1.000 43.64609  ? 89  LEU A HD23 1 
ATOM   1412 N N    . LYS A 1 90  ? -31.71900 -14.20700 20.24000  1.000 37.59612  ? 90  LYS A N    1 
ATOM   1413 C CA   . LYS A 1 90  ? -31.80900 -15.34700 19.34700  1.000 42.20921  ? 90  LYS A CA   1 
ATOM   1414 C C    . LYS A 1 90  ? -32.35100 -14.85900 18.01600  1.000 43.31076  ? 90  LYS A C    1 
ATOM   1415 O O    . LYS A 1 90  ? -33.33100 -14.10900 17.98000  1.000 40.90356  ? 90  LYS A O    1 
ATOM   1416 C CB   . LYS A 1 90  ? -32.73300 -16.41700 19.93800  1.000 41.24053  ? 90  LYS A CB   1 
ATOM   1417 C CG   . LYS A 1 90  ? -32.72500 -17.74600 19.20100  1.000 47.67525  ? 90  LYS A CG   1 
ATOM   1418 C CD   . LYS A 1 90  ? -31.63400 -18.64000 19.77100  1.000 54.78665  ? 90  LYS A CD   1 
ATOM   1419 C CE   . LYS A 1 90  ? -31.92000 -20.09900 19.44400  1.000 60.81029  ? 90  LYS A CE   1 
ATOM   1420 N NZ   . LYS A 1 90  ? -30.83800 -20.98400 19.95900  1.000 71.85304  ? 90  LYS A NZ   1 
ATOM   1421 H H    . LYS A 1 90  ? -32.36000 -14.15700 20.81200  1.000 45.11614  ? 90  LYS A H    1 
ATOM   1422 H HA   . LYS A 1 90  ? -30.92900 -15.73100 19.20800  1.000 50.65186  ? 90  LYS A HA   1 
ATOM   1423 H HB2  . LYS A 1 90  ? -32.47000 -16.57900 20.85700  1.000 49.48944  ? 90  LYS A HB2  1 
ATOM   1424 H HB3  . LYS A 1 90  ? -33.64200 -16.08000 19.91800  1.000 49.48944  ? 90  LYS A HB3  1 
ATOM   1425 H HG2  . LYS A 1 90  ? -33.58000 -18.18800 19.31800  1.000 57.21110  ? 90  LYS A HG2  1 
ATOM   1426 H HG3  . LYS A 1 90  ? -32.54300 -17.59800 18.26000  1.000 57.21110  ? 90  LYS A HG3  1 
ATOM   1427 H HD2  . LYS A 1 90  ? -30.78000 -18.39900 19.37800  1.000 65.74478  ? 90  LYS A HD2  1 
ATOM   1428 H HD3  . LYS A 1 90  ? -31.60100 -18.54800 20.73600  1.000 65.74478  ? 90  LYS A HD3  1 
ATOM   1429 H HE2  . LYS A 1 90  ? -32.75500 -20.36400 19.86100  1.000 72.97315  ? 90  LYS A HE2  1 
ATOM   1430 H HE3  . LYS A 1 90  ? -31.97500 -20.20900 18.48200  1.000 72.97315  ? 90  LYS A HE3  1 
ATOM   1431 H HZ1  . LYS A 1 90  ? -31.01900 -21.83200 19.76000  1.000 86.22445  ? 90  LYS A HZ1  1 
ATOM   1432 H HZ2  . LYS A 1 90  ? -30.06000 -20.76000 19.58900  1.000 86.22445  ? 90  LYS A HZ2  1 
ATOM   1433 H HZ3  . LYS A 1 90  ? -30.77300 -20.90100 20.84300  1.000 86.22445  ? 90  LYS A HZ3  1 
ATOM   1434 N N    . VAL A 1 91  ? -31.69100 -15.23900 16.92800  1.000 36.16941  ? 91  VAL A N    1 
ATOM   1435 C CA   . VAL A 1 91  ? -32.13000 -14.82600 15.61100  1.000 39.34207  ? 91  VAL A CA   1 
ATOM   1436 C C    . VAL A 1 91  ? -32.42600 -16.07600 14.78000  1.000 45.07974  ? 91  VAL A C    1 
ATOM   1437 O O    . VAL A 1 91  ? -32.00900 -17.19000 15.10600  1.000 45.58244  ? 91  VAL A O    1 
ATOM   1438 C CB   . VAL A 1 91  ? -31.11700 -13.90500 14.90600  1.000 42.07841  ? 91  VAL A CB   1 
ATOM   1439 C CG1  . VAL A 1 91  ? -31.03800 -12.57100 15.63300  1.000 42.92797  ? 91  VAL A CG1  1 
ATOM   1440 C CG2  . VAL A 1 91  ? -29.71200 -14.55100 14.79500  1.000 39.73308  ? 91  VAL A CG2  1 
ATOM   1441 H H    . VAL A 1 91  ? -30.98800 -15.73500 16.92900  1.000 43.40409  ? 91  VAL A H    1 
ATOM   1442 H HA   . VAL A 1 91  ? -32.96000 -14.33200 15.69500  1.000 47.21129  ? 91  VAL A HA   1 
ATOM   1443 H HB   . VAL A 1 91  ? -31.43200 -13.73000 14.00500  1.000 50.49489  ? 91  VAL A HB   1 
ATOM   1444 H HG11 . VAL A 1 91  ? -30.39900 -12.00100 15.17700  1.000 51.51437  ? 91  VAL A HG11 1 
ATOM   1445 H HG12 . VAL A 1 91  ? -31.91500 -12.15700 15.62800  1.000 51.51437  ? 91  VAL A HG12 1 
ATOM   1446 H HG13 . VAL A 1 91  ? -30.75100 -12.72600 16.54600  1.000 51.51437  ? 91  VAL A HG13 1 
ATOM   1447 H HG21 . VAL A 1 91  ? -29.11900 -13.93800 14.33400  1.000 47.68049  ? 91  VAL A HG21 1 
ATOM   1448 H HG22 . VAL A 1 91  ? -29.37500 -14.72900 15.68700  1.000 47.68049  ? 91  VAL A HG22 1 
ATOM   1449 H HG23 . VAL A 1 91  ? -29.78400 -15.38000 14.29600  1.000 47.68049  ? 91  VAL A HG23 1 
ATOM   1450 N N    . ASP A 1 92  ? -33.17000 -15.89300 13.69200  1.000 41.17420  ? 92  ASP A N    1 
ATOM   1451 C CA   . ASP A 1 92  ? -33.64300 -17.04800 12.87400  1.000 57.08760  ? 92  ASP A CA   1 
ATOM   1452 C C    . ASP A 1 92  ? -32.60400 -17.51900 11.85700  1.000 52.11242  ? 92  ASP A C    1 
ATOM   1453 O O    . ASP A 1 92  ? -32.89900 -18.47200 11.12100  1.000 52.44674  ? 92  ASP A O    1 
ATOM   1454 C CB   . ASP A 1 92  ? -34.90600 -16.68000 12.11800  1.000 56.98014  ? 92  ASP A CB   1 
ATOM   1455 C CG   . ASP A 1 92  ? -34.79200 -15.41600 11.29000  1.000 59.29695  ? 92  ASP A CG   1 
ATOM   1456 O OD1  . ASP A 1 92  ? -33.92300 -14.59300 11.62800  1.000 68.24318  ? 92  ASP A OD1  1 
ATOM   1457 O OD2  . ASP A 1 92  ? -35.56200 -15.27300 10.32200  1.000 65.66876  ? 92  ASP A OD2  1 
ATOM   1458 H H    . ASP A 1 92  ? -33.41900 -15.12500 13.39800  1.000 49.40985  ? 92  ASP A H    1 
ATOM   1459 H HA   . ASP A 1 92  ? -33.84800 -17.79100 13.46200  1.000 68.50592  ? 92  ASP A HA   1 
ATOM   1460 H HB2  . ASP A 1 92  ? -35.13200 -17.40700 11.51700  1.000 68.37697  ? 92  ASP A HB2  1 
ATOM   1461 H HB3  . ASP A 1 92  ? -35.62400 -16.54900 12.75700  1.000 68.37697  ? 92  ASP A HB3  1 
ATOM   1462 N N    . THR A 1 93  ? -31.44500 -16.88300 11.82500  1.000 44.29458  ? 93  THR A N    1 
ATOM   1463 C CA   . THR A 1 93  ? -30.37400 -17.22300 10.89600  1.000 48.51773  ? 93  THR A CA   1 
ATOM   1464 C C    . THR A 1 93  ? -29.07400 -17.41200 11.65400  1.000 42.16959  ? 93  THR A C    1 
ATOM   1465 O O    . THR A 1 93  ? -28.65700 -16.52100 12.40200  1.000 37.99145  ? 93  THR A O    1 
ATOM   1466 C CB   . THR A 1 93  ? -30.18400 -16.11800 9.86100   1.000 46.39656  ? 93  THR A CB   1 
ATOM   1467 O OG1  . THR A 1 93  ? -31.43900 -15.92600 9.20300   1.000 49.41971  ? 93  THR A OG1  1 
ATOM   1468 C CG2  . THR A 1 93  ? -29.10500 -16.52200 8.82700   1.000 45.95875  ? 93  THR A CG2  1 
ATOM   1469 H H    . THR A 1 93  ? -31.24500 -16.23000 12.34700  1.000 53.15429  ? 93  THR A H    1 
ATOM   1470 H HA   . THR A 1 93  ? -30.58800 -18.04900 10.43400  1.000 58.22208  ? 93  THR A HA   1 
ATOM   1471 H HB   . THR A 1 93  ? -29.91000 -15.29700 10.29900  1.000 55.67667  ? 93  THR A HB   1 
ATOM   1472 H HG1  . THR A 1 93  ? -31.37000 -15.32200 8.62400   1.000 59.30445  ? 93  THR A HG1  1 
ATOM   1473 H HG21 . THR A 1 93  ? -29.11100 -15.89900 8.08400   1.000 55.15130  ? 93  THR A HG21 1 
ATOM   1474 H HG22 . THR A 1 93  ? -28.22700 -16.51100 9.23800   1.000 55.15130  ? 93  THR A HG22 1 
ATOM   1475 H HG23 . THR A 1 93  ? -29.28600 -17.41400 8.49100   1.000 55.15130  ? 93  THR A HG23 1 
ATOM   1476 N N    . ALA A 1 94  ? -28.42400 -18.55200 11.45200  1.000 38.39955  ? 94  ALA A N    1 
ATOM   1477 C CA   . ALA A 1 94  ? -27.07800 -18.72800 11.98700  1.000 38.80529  ? 94  ALA A CA   1 
ATOM   1478 C C    . ALA A 1 94  ? -26.09200 -17.96700 11.10700  1.000 38.77852  ? 94  ALA A C    1 
ATOM   1479 O O    . ALA A 1 94  ? -26.20700 -17.97100 9.87900   1.000 38.14578  ? 94  ALA A O    1 
ATOM   1480 C CB   . ALA A 1 94  ? -26.71200 -20.21500 12.04800  1.000 46.11137  ? 94  ALA A CB   1 
ATOM   1481 H H    . ALA A 1 94  ? -28.73200 -19.22700 11.01700  1.000 46.08026  ? 94  ALA A H    1 
ATOM   1482 H HA   . ALA A 1 94  ? -27.04000 -18.36400 12.88400  1.000 46.56715  ? 94  ALA A HA   1 
ATOM   1483 H HB1  . ALA A 1 94  ? -25.81500 -20.30500 12.40600  1.000 55.33444  ? 94  ALA A HB1  1 
ATOM   1484 H HB2  . ALA A 1 94  ? -27.34500 -20.67200 12.62300  1.000 55.33444  ? 94  ALA A HB2  1 
ATOM   1485 H HB3  . ALA A 1 94  ? -26.75000 -20.58600 11.15300  1.000 55.33444  ? 94  ALA A HB3  1 
ATOM   1486 N N    . ASN A 1 95  ? -25.13400 -17.30300 11.73200  1.000 36.72995  ? 95  ASN A N    1 
ATOM   1487 C CA   . ASN A 1 95  ? -24.17000 -16.51100 10.97200  1.000 34.43355  ? 95  ASN A CA   1 
ATOM   1488 C C    . ASN A 1 95  ? -23.30300 -17.44100 10.13000  1.000 32.25380  ? 95  ASN A C    1 
ATOM   1489 O O    . ASN A 1 95  ? -22.57500 -18.25700 10.69900  1.000 30.70505  ? 95  ASN A O    1 
ATOM   1490 C CB   . ASN A 1 95  ? -23.29200 -15.68100 11.93400  1.000 33.14210  ? 95  ASN A CB   1 
ATOM   1491 C CG   . ASN A 1 95  ? -22.34200 -14.77200 11.20300  1.000 33.95705  ? 95  ASN A CG   1 
ATOM   1492 O OD1  . ASN A 1 95  ? -22.31400 -14.75000 9.96500   1.000 31.44207  ? 95  ASN A OD1  1 
ATOM   1493 N ND2  . ASN A 1 95  ? -21.53600 -14.00600 11.96700  1.000 35.06494  ? 95  ASN A ND2  1 
ATOM   1494 H H    . ASN A 1 95  ? -25.01700 -17.29100 12.58400  1.000 44.07674  ? 95  ASN A H    1 
ATOM   1495 H HA   . ASN A 1 95  ? -24.64600 -15.89800 10.39300  1.000 41.32106  ? 95  ASN A HA   1 
ATOM   1496 H HB2  . ASN A 1 95  ? -23.85600 -15.14600 12.50500  1.000 39.77132  ? 95  ASN A HB2  1 
ATOM   1497 H HB3  . ASN A 1 95  ? -22.76700 -16.27900 12.47900  1.000 39.77132  ? 95  ASN A HB3  1 
ATOM   1498 H HD21 . ASN A 1 95  ? -20.97500 -13.47000 11.59700  1.000 42.07873  ? 95  ASN A HD21 1 
ATOM   1499 H HD22 . ASN A 1 95  ? -21.58500 -14.05200 12.82400  1.000 42.07873  ? 95  ASN A HD22 1 
ATOM   1500 N N    . PRO A 1 96  ? -23.35800 -17.39000 8.80000   1.000 35.49889  ? 96  PRO A N    1 
ATOM   1501 C CA   . PRO A 1 96  ? -22.52900 -18.31600 8.00800   1.000 39.57166  ? 96  PRO A CA   1 
ATOM   1502 C C    . PRO A 1 96  ? -21.04200 -18.03400 8.15000   1.000 39.54966  ? 96  PRO A C    1 
ATOM   1503 O O    . PRO A 1 96  ? -20.21600 -18.88700 7.77300   1.000 37.90045  ? 96  PRO A O    1 
ATOM   1504 C CB   . PRO A 1 96  ? -23.03700 -18.09500 6.57200   1.000 44.49690  ? 96  PRO A CB   1 
ATOM   1505 C CG   . PRO A 1 96  ? -23.53500 -16.67000 6.55300   1.000 44.93619  ? 96  PRO A CG   1 
ATOM   1506 C CD   . PRO A 1 96  ? -24.10800 -16.43800 7.95800   1.000 42.85193  ? 96  PRO A CD   1 
ATOM   1507 H HA   . PRO A 1 96  ? -22.70600 -19.23300 8.27100   1.000 47.48680  ? 96  PRO A HA   1 
ATOM   1508 H HB2  . PRO A 1 96  ? -22.30700 -18.21300 5.94400   1.000 53.39708  ? 96  PRO A HB2  1 
ATOM   1509 H HB3  . PRO A 1 96  ? -23.75900 -18.71400 6.38100   1.000 53.39708  ? 96  PRO A HB3  1 
ATOM   1510 H HG2  . PRO A 1 96  ? -22.79600 -16.06600 6.37900   1.000 53.92423  ? 96  PRO A HG2  1 
ATOM   1511 H HG3  . PRO A 1 96  ? -24.22600 -16.57300 5.87900   1.000 53.92423  ? 96  PRO A HG3  1 
ATOM   1512 H HD2  . PRO A 1 96  ? -23.93900 -15.52700 8.24400   1.000 51.42312  ? 96  PRO A HD2  1 
ATOM   1513 H HD3  . PRO A 1 96  ? -25.05500 -16.64600 7.97500   1.000 51.42312  ? 96  PRO A HD3  1 
ATOM   1514 N N    . LYS A 1 97  ? -20.67100 -16.86800 8.68500   1.000 36.08142  ? 97  LYS A N    1 
ATOM   1515 C CA   . LYS A 1 97  ? -19.27400 -16.50300 8.86800   1.000 36.42317  ? 97  LYS A CA   1 
ATOM   1516 C C    . LYS A 1 97  ? -18.77500 -16.80600 10.27500  1.000 33.83164  ? 97  LYS A C    1 
ATOM   1517 O O    . LYS A 1 97  ? -17.68000 -16.36900 10.64700  1.000 31.92752  ? 97  LYS A O    1 
ATOM   1518 C CB   . LYS A 1 97  ? -19.06200 -15.01900 8.54400   1.000 35.22023  ? 97  LYS A CB   1 
ATOM   1519 C CG   . LYS A 1 97  ? -19.37700 -14.61700 7.09300   1.000 42.72600  ? 97  LYS A CG   1 
ATOM   1520 C CD   . LYS A 1 97  ? -19.26700 -13.08600 6.98800   1.000 50.19832  ? 97  LYS A CD   1 
ATOM   1521 C CE   . LYS A 1 97  ? -19.67300 -12.52900 5.63600   1.000 63.14143  ? 97  LYS A CE   1 
ATOM   1522 N NZ   . LYS A 1 97  ? -20.09600 -11.08300 5.73800   1.000 63.04142  ? 97  LYS A NZ   1 
ATOM   1523 H H    . LYS A 1 97  ? -21.22200 -16.26400 8.95200   1.000 43.29850  ? 97  LYS A H    1 
ATOM   1524 H HA   . LYS A 1 97  ? -18.73400 -17.01800 8.24800   1.000 43.70860  ? 97  LYS A HA   1 
ATOM   1525 H HB2  . LYS A 1 97  ? -19.63400 -14.49200 9.12400   1.000 42.26508  ? 97  LYS A HB2  1 
ATOM   1526 H HB3  . LYS A 1 97  ? -18.13300 -14.79600 8.71400   1.000 42.26508  ? 97  LYS A HB3  1 
ATOM   1527 H HG2  . LYS A 1 97  ? -18.73300 -15.02100 6.49000   1.000 51.27200  ? 97  LYS A HG2  1 
ATOM   1528 H HG3  . LYS A 1 97  ? -20.28100 -14.88400 6.86400   1.000 51.27200  ? 97  LYS A HG3  1 
ATOM   1529 H HD2  . LYS A 1 97  ? -19.84300 -12.68500 7.65800   1.000 60.23879  ? 97  LYS A HD2  1 
ATOM   1530 H HD3  . LYS A 1 97  ? -18.34600 -12.82800 7.15000   1.000 60.23879  ? 97  LYS A HD3  1 
ATOM   1531 H HE2  . LYS A 1 97  ? -18.91900 -12.58300 5.02800   1.000 75.77052  ? 97  LYS A HE2  1 
ATOM   1532 H HE3  . LYS A 1 97  ? -20.42100 -13.04100 5.29000   1.000 75.77052  ? 97  LYS A HE3  1 
ATOM   1533 H HZ1  . LYS A 1 97  ? -20.96000 -11.01400 5.53800   1.000 75.65050  ? 97  LYS A HZ1  1 
ATOM   1534 H HZ2  . LYS A 1 97  ? -19.97600 -10.78800 6.56800   1.000 75.65050  ? 97  LYS A HZ2  1 
ATOM   1535 H HZ3  . LYS A 1 97  ? -19.63400 -10.58900 5.16100   1.000 75.65050  ? 97  LYS A HZ3  1 
ATOM   1536 N N    . THR A 1 98  ? -19.56300 -17.50600 11.07400  1.000 31.65893  ? 98  THR A N    1 
ATOM   1537 C CA   . THR A 1 98  ? -19.16200 -17.78300 12.44500  1.000 32.80647  ? 98  THR A CA   1 
ATOM   1538 C C    . THR A 1 98  ? -17.84700 -18.54200 12.42300  1.000 34.52021  ? 98  THR A C    1 
ATOM   1539 O O    . THR A 1 98  ? -17.79400 -19.62200 11.82100  1.000 32.03656  ? 98  THR A O    1 
ATOM   1540 C CB   . THR A 1 98  ? -20.21700 -18.63400 13.17900  1.000 36.04255  ? 98  THR A CB   1 
ATOM   1541 O OG1  . THR A 1 98  ? -21.48900 -17.97700 13.11600  1.000 34.71244  ? 98  THR A OG1  1 
ATOM   1542 C CG2  . THR A 1 98  ? -19.80100 -18.81900 14.61900  1.000 33.87231  ? 98  THR A CG2  1 
ATOM   1543 H H    . THR A 1 98  ? -20.32800 -17.83100 10.85300  1.000 37.99151  ? 98  THR A H    1 
ATOM   1544 H HA   . THR A 1 98  ? -19.05800 -16.94700 12.92300  1.000 39.36856  ? 98  THR A HA   1 
ATOM   1545 H HB   . THR A 1 98  ? -20.28000 -19.50700 12.76000  1.000 43.25186  ? 98  THR A HB   1 
ATOM   1546 H HG1  . THR A 1 98  ? -21.81000 -18.05600 12.34400  1.000 41.65573  ? 98  THR A HG1  1 
ATOM   1547 H HG21 . THR A 1 98  ? -20.54100 -19.17900 15.13200  1.000 40.64757  ? 98  THR A HG21 1 
ATOM   1548 H HG22 . THR A 1 98  ? -19.05300 -19.43300 14.67500  1.000 40.64757  ? 98  THR A HG22 1 
ATOM   1549 H HG23 . THR A 1 98  ? -19.54000 -17.96600 15.00100  1.000 40.64757  ? 98  THR A HG23 1 
ATOM   1550 N N    . PRO A 1 99  ? -16.80100 -18.05700 13.06700  1.000 32.74737  ? 99  PRO A N    1 
ATOM   1551 C CA   . PRO A 1 99  ? -15.55200 -18.83000 13.14200  1.000 34.17784  ? 99  PRO A CA   1 
ATOM   1552 C C    . PRO A 1 99  ? -15.61900 -19.86800 14.25000  1.000 38.35948  ? 99  PRO A C    1 
ATOM   1553 O O    . PRO A 1 99  ? -16.53700 -19.88500 15.06700  1.000 36.76443  ? 99  PRO A O    1 
ATOM   1554 C CB   . PRO A 1 99  ? -14.49600 -17.77000 13.48100  1.000 31.97413  ? 99  PRO A CB   1 
ATOM   1555 C CG   . PRO A 1 99  ? -15.27600 -16.81100 14.40900  1.000 28.30509  ? 99  PRO A CG   1 
ATOM   1556 C CD   . PRO A 1 99  ? -16.70000 -16.76400 13.79600  1.000 31.57367  ? 99  PRO A CD   1 
ATOM   1557 H HA   . PRO A 1 99  ? -15.34600 -19.25200 12.29300  1.000 41.01421  ? 99  PRO A HA   1 
ATOM   1558 H HB2  . PRO A 1 99  ? -13.74900 -18.17800 13.94600  1.000 38.36975  ? 99  PRO A HB2  1 
ATOM   1559 H HB3  . PRO A 1 99  ? -14.20500 -17.31800 12.67400  1.000 38.36975  ? 99  PRO A HB3  1 
ATOM   1560 H HG2  . PRO A 1 99  ? -15.29900 -17.17000 15.31000  1.000 33.96691  ? 99  PRO A HG2  1 
ATOM   1561 H HG3  . PRO A 1 99  ? -14.86500 -15.93300 14.39600  1.000 33.96691  ? 99  PRO A HG3  1 
ATOM   1562 H HD2  . PRO A 1 99  ? -17.36900 -16.71600 14.49700  1.000 37.88920  ? 99  PRO A HD2  1 
ATOM   1563 H HD3  . PRO A 1 99  ? -16.77700 -16.02200 13.17700  1.000 37.88920  ? 99  PRO A HD3  1 
ATOM   1564 N N    . LYS A 1 100 ? -14.60500 -20.72000 14.29300  1.000 35.26369  ? 100 LYS A N    1 
ATOM   1565 C CA   . LYS A 1 100 ? -14.39900 -21.53000 15.48800  1.000 35.02701  ? 100 LYS A CA   1 
ATOM   1566 C C    . LYS A 1 100 ? -14.06500 -20.60400 16.65100  1.000 38.30779  ? 100 LYS A C    1 
ATOM   1567 O O    . LYS A 1 100 ? -13.22000 -19.72200 16.51200  1.000 32.91710  ? 100 LYS A O    1 
ATOM   1568 C CB   . LYS A 1 100 ? -13.26800 -22.53400 15.24900  1.000 43.44632  ? 100 LYS A CB   1 
ATOM   1569 C CG   . LYS A 1 100 ? -12.78300 -23.28600 16.47200  1.000 50.73688  ? 100 LYS A CG   1 
ATOM   1570 C CD   . LYS A 1 100 ? -11.93000 -24.50100 16.06100  1.000 63.00822  ? 100 LYS A CD   1 
ATOM   1571 C CE   . LYS A 1 100 ? -11.30700 -25.17600 17.28500  1.000 69.60701  ? 100 LYS A CE   1 
ATOM   1572 N NZ   . LYS A 1 100 ? -12.35500 -25.54400 18.28600  1.000 73.01982  ? 100 LYS A NZ   1 
ATOM   1573 H H    . LYS A 1 100 ? -14.03400 -20.84800 13.66200  1.000 42.31722  ? 100 LYS A H    1 
ATOM   1574 H HA   . LYS A 1 100 ? -15.21100 -22.01700 15.69900  1.000 42.03321  ? 100 LYS A HA   1 
ATOM   1575 H HB2  . LYS A 1 100 ? -13.57500 -23.19300 14.60700  1.000 52.13638  ? 100 LYS A HB2  1 
ATOM   1576 H HB3  . LYS A 1 100 ? -12.50800 -22.05600 14.88200  1.000 52.13638  ? 100 LYS A HB3  1 
ATOM   1577 H HG2  . LYS A 1 100 ? -12.23100 -22.69800 17.00800  1.000 60.88506  ? 100 LYS A HG2  1 
ATOM   1578 H HG3  . LYS A 1 100 ? -13.54500 -23.60000 16.98300  1.000 60.88506  ? 100 LYS A HG3  1 
ATOM   1579 H HD2  . LYS A 1 100 ? -12.49100 -25.14900 15.60800  1.000 75.61066  ? 100 LYS A HD2  1 
ATOM   1580 H HD3  . LYS A 1 100 ? -11.21400 -24.20800 15.47600  1.000 75.61066  ? 100 LYS A HD3  1 
ATOM   1581 H HE2  . LYS A 1 100 ? -10.85100 -25.98600 17.00800  1.000 83.52922  ? 100 LYS A HE2  1 
ATOM   1582 H HE3  . LYS A 1 100 ? -10.68300 -24.56500 17.70700  1.000 83.52922  ? 100 LYS A HE3  1 
ATOM   1583 H HZ1  . LYS A 1 100 ? -11.98500 -25.98500 18.96500  1.000 87.62458  ? 100 LYS A HZ1  1 
ATOM   1584 H HZ2  . LYS A 1 100 ? -12.74900 -24.81000 18.59900  1.000 87.62458  ? 100 LYS A HZ2  1 
ATOM   1585 H HZ3  . LYS A 1 100 ? -12.97000 -26.06300 17.90600  1.000 87.62458  ? 100 LYS A HZ3  1 
ATOM   1586 N N    . TYR A 1 101 ? -14.75900 -20.74300 17.78900  1.000 31.80322  ? 101 TYR A N    1 
ATOM   1587 C CA   . TYR A 1 101 ? -14.54200 -19.75100 18.83700  1.000 34.82513  ? 101 TYR A CA   1 
ATOM   1588 C C    . TYR A 1 101 ? -14.80100 -20.33100 20.21900  1.000 34.40974  ? 101 TYR A C    1 
ATOM   1589 O O    . TYR A 1 101 ? -15.42800 -21.38000 20.37100  1.000 32.69856  ? 101 TYR A O    1 
ATOM   1590 C CB   . TYR A 1 101 ? -15.43600 -18.51700 18.64600  1.000 32.80823  ? 101 TYR A CB   1 
ATOM   1591 C CG   . TYR A 1 101 ? -16.89200 -18.84500 18.93600  1.000 31.32906  ? 101 TYR A CG   1 
ATOM   1592 C CD1  . TYR A 1 101 ? -17.69500 -19.41700 17.94600  1.000 31.17519  ? 101 TYR A CD1  1 
ATOM   1593 C CD2  . TYR A 1 101 ? -17.45500 -18.59200 20.18800  1.000 33.18231  ? 101 TYR A CD2  1 
ATOM   1594 C CE1  . TYR A 1 101 ? -19.05000 -19.74400 18.20500  1.000 34.37762  ? 101 TYR A CE1  1 
ATOM   1595 C CE2  . TYR A 1 101 ? -18.78000 -18.89900 20.46700  1.000 33.50455  ? 101 TYR A CE2  1 
ATOM   1596 C CZ   . TYR A 1 101 ? -19.57000 -19.45700 19.46800  1.000 34.34128  ? 101 TYR A CZ   1 
ATOM   1597 O OH   . TYR A 1 101 ? -20.86700 -19.77600 19.73600  1.000 40.75482  ? 101 TYR A OH   1 
ATOM   1598 H H    . TYR A 1 101 ? -15.32600 -21.36400 17.96800  1.000 38.16467  ? 101 TYR A H    1 
ATOM   1599 H HA   . TYR A 1 101 ? -13.61800 -19.46300 18.80600  1.000 41.79095  ? 101 TYR A HA   1 
ATOM   1600 H HB2  . TYR A 1 101 ? -15.15300 -17.81800 19.25600  1.000 39.37067  ? 101 TYR A HB2  1 
ATOM   1601 H HB3  . TYR A 1 101 ? -15.36900 -18.21100 17.72800  1.000 39.37067  ? 101 TYR A HB3  1 
ATOM   1602 H HD1  . TYR A 1 101 ? -17.33300 -19.59500 17.10900  1.000 37.41103  ? 101 TYR A HD1  1 
ATOM   1603 H HD2  . TYR A 1 101 ? -16.92800 -18.21200 20.85400  1.000 39.81958  ? 101 TYR A HD2  1 
ATOM   1604 H HE1  . TYR A 1 101 ? -19.58400 -20.12200 17.54400  1.000 41.25394  ? 101 TYR A HE1  1 
ATOM   1605 H HE2  . TYR A 1 101 ? -19.13800 -18.72100 21.30700  1.000 40.20626  ? 101 TYR A HE2  1 
ATOM   1606 H HH   . TYR A 1 101 ? -21.22100 -20.13100 19.06200  1.000 48.90659  ? 101 TYR A HH   1 
ATOM   1607 N N    . LYS A 1 102 ? -14.31900 -19.61300 21.22800  1.000 30.59934  ? 102 LYS A N    1 
ATOM   1608 C CA   . LYS A 1 102 ? -14.69700 -19.90900 22.59500  1.000 32.77083  ? 102 LYS A CA   1 
ATOM   1609 C C    . LYS A 1 102 ? -14.70900 -18.61000 23.36700  1.000 32.09733  ? 102 LYS A C    1 
ATOM   1610 O O    . LYS A 1 102 ? -14.19500 -17.58700 22.90200  1.000 29.07582  ? 102 LYS A O    1 
ATOM   1611 C CB   . LYS A 1 102 ? -13.73700 -20.92000 23.24400  1.000 38.03716  ? 102 LYS A CB   1 
ATOM   1612 C CG   . LYS A 1 102 ? -12.34500 -20.36200 23.31300  1.000 38.73202  ? 102 LYS A CG   1 
ATOM   1613 C CD   . LYS A 1 102 ? -11.32800 -21.40000 23.73300  1.000 49.61221  ? 102 LYS A CD   1 
ATOM   1614 C CE   . LYS A 1 102 ? -9.97500  -20.73500 23.67900  1.000 47.45253  ? 102 LYS A CE   1 
ATOM   1615 N NZ   . LYS A 1 102 ? -8.85500  -21.59000 24.03200  1.000 55.84873  ? 102 LYS A NZ   1 
ATOM   1616 H H    . LYS A 1 102 ? -13.77400 -18.95300 21.14400  1.000 36.72001  ? 102 LYS A H    1 
ATOM   1617 H HA   . LYS A 1 102 ? -15.59200 -20.28300 22.61000  1.000 39.32579  ? 102 LYS A HA   1 
ATOM   1618 H HB2  . LYS A 1 102 ? -14.03500 -21.11400 24.14700  1.000 45.64539  ? 102 LYS A HB2  1 
ATOM   1619 H HB3  . LYS A 1 102 ? -13.71600 -21.73200 22.71300  1.000 45.64539  ? 102 LYS A HB3  1 
ATOM   1620 H HG2  . LYS A 1 102 ? -12.09100 -20.02700 22.44000  1.000 46.47922  ? 102 LYS A HG2  1 
ATOM   1621 H HG3  . LYS A 1 102 ? -12.32000 -19.64400 23.96500  1.000 46.47922  ? 102 LYS A HG3  1 
ATOM   1622 H HD2  . LYS A 1 102 ? -11.50300 -21.69100 24.64100  1.000 59.53545  ? 102 LYS A HD2  1 
ATOM   1623 H HD3  . LYS A 1 102 ? -11.34000 -22.14800 23.11600  1.000 59.53545  ? 102 LYS A HD3  1 
ATOM   1624 H HE2  . LYS A 1 102 ? -9.82400  -20.41500 22.77600  1.000 56.94384  ? 102 LYS A HE2  1 
ATOM   1625 H HE3  . LYS A 1 102 ? -9.97500  -19.98500 24.29400  1.000 56.94384  ? 102 LYS A HE3  1 
ATOM   1626 H HZ1  . LYS A 1 102 ? -8.09400  -21.13200 23.97800  1.000 67.01928  ? 102 LYS A HZ1  1 
ATOM   1627 H HZ2  . LYS A 1 102 ? -8.95300  -21.89100 24.86400  1.000 67.01928  ? 102 LYS A HZ2  1 
ATOM   1628 H HZ3  . LYS A 1 102 ? -8.81500  -22.28400 23.47600  1.000 67.01928  ? 102 LYS A HZ3  1 
ATOM   1629 N N    . PHE A 1 103 ? -15.35200 -18.64300 24.52900  1.000 28.54021  ? 103 PHE A N    1 
ATOM   1630 C CA   . PHE A 1 103 ? -15.33700 -17.51800 25.47200  1.000 27.99953  ? 103 PHE A CA   1 
ATOM   1631 C C    . PHE A 1 103 ? -14.36000 -17.81800 26.61000  1.000 27.69739  ? 103 PHE A C    1 
ATOM   1632 O O    . PHE A 1 103 ? -14.40700 -18.89300 27.21800  1.000 31.48863  ? 103 PHE A O    1 
ATOM   1633 C CB   . PHE A 1 103 ? -16.74700 -17.27500 26.05400  1.000 27.80020  ? 103 PHE A CB   1 
ATOM   1634 C CG   . PHE A 1 103 ? -17.80300 -16.87800 25.03800  1.000 29.83365  ? 103 PHE A CG   1 
ATOM   1635 C CD1  . PHE A 1 103 ? -17.47000 -16.45300 23.75700  1.000 30.66552  ? 103 PHE A CD1  1 
ATOM   1636 C CD2  . PHE A 1 103 ? -19.16000 -16.90000 25.41100  1.000 31.55069  ? 103 PHE A CD2  1 
ATOM   1637 C CE1  . PHE A 1 103 ? -18.45800 -16.08000 22.84400  1.000 27.84458  ? 103 PHE A CE1  1 
ATOM   1638 C CE2  . PHE A 1 103 ? -20.15000 -16.49400 24.51100  1.000 30.88795  ? 103 PHE A CE2  1 
ATOM   1639 C CZ   . PHE A 1 103 ? -19.78700 -16.10000 23.22400  1.000 35.12405  ? 103 PHE A CZ   1 
ATOM   1640 H H    . PHE A 1 103 ? -15.81300 -19.31500 24.80300  1.000 34.24905  ? 103 PHE A H    1 
ATOM   1641 H HA   . PHE A 1 103 ? -15.04300 -16.71200 25.01900  1.000 33.60023  ? 103 PHE A HA   1 
ATOM   1642 H HB2  . PHE A 1 103 ? -17.04800 -18.09100 26.48400  1.000 33.36104  ? 103 PHE A HB2  1 
ATOM   1643 H HB3  . PHE A 1 103 ? -16.69100 -16.56300 26.71100  1.000 33.36104  ? 103 PHE A HB3  1 
ATOM   1644 H HD1  . PHE A 1 103 ? -16.57800 -16.43700 23.49600  1.000 36.79943  ? 103 PHE A HD1  1 
ATOM   1645 H HD2  . PHE A 1 103 ? -19.39800 -17.16100 26.27100  1.000 37.86163  ? 103 PHE A HD2  1 
ATOM   1646 H HE1  . PHE A 1 103 ? -18.22200 -15.80300 21.98800  1.000 33.41430  ? 103 PHE A HE1  1 
ATOM   1647 H HE2  . PHE A 1 103 ? -21.04600 -16.52200 24.75700  1.000 37.06634  ? 103 PHE A HE2  1 
ATOM   1648 H HZ   . PHE A 1 103 ? -20.44400 -15.84700 22.61700  1.000 42.14966  ? 103 PHE A HZ   1 
ATOM   1649 N N    . VAL A 1 104 ? -13.52500 -16.85000 26.96200  1.000 25.68879  ? 104 VAL A N    1 
ATOM   1650 C CA   . VAL A 1 104 ? -12.57500 -17.02300 28.06400  1.000 29.13541  ? 104 VAL A CA   1 
ATOM   1651 C C    . VAL A 1 104 ? -12.57800 -15.76100 28.91200  1.000 27.32646  ? 104 VAL A C    1 
ATOM   1652 O O    . VAL A 1 104 ? -12.52900 -14.64900 28.37500  1.000 30.58850  ? 104 VAL A O    1 
ATOM   1653 C CB   . VAL A 1 104 ? -11.13700 -17.27700 27.53200  1.000 28.47907  ? 104 VAL A CB   1 
ATOM   1654 C CG1  . VAL A 1 104 ? -10.15100 -17.46700 28.70800  1.000 36.76682  ? 104 VAL A CG1  1 
ATOM   1655 C CG2  . VAL A 1 104 ? -11.12100 -18.45600 26.58200  1.000 35.37637  ? 104 VAL A CG2  1 
ATOM   1656 H H    . VAL A 1 104 ? -13.48500 -16.08000 26.58100  1.000 30.82735  ? 104 VAL A H    1 
ATOM   1657 H HA   . VAL A 1 104 ? -12.84000 -17.77200 28.62000  1.000 34.96329  ? 104 VAL A HA   1 
ATOM   1658 H HB   . VAL A 1 104 ? -10.85000 -16.49600 27.03300  1.000 34.17569  ? 104 VAL A HB   1 
ATOM   1659 H HG11 . VAL A 1 104 ? -9.30700  -17.79600 28.36000  1.000 44.12098  ? 104 VAL A HG11 1 
ATOM   1660 H HG12 . VAL A 1 104 ? -10.01500 -16.61500 29.15100  1.000 44.12098  ? 104 VAL A HG12 1 
ATOM   1661 H HG13 . VAL A 1 104 ? -10.52400 -18.11000 29.33100  1.000 44.12098  ? 104 VAL A HG13 1 
ATOM   1662 H HG21 . VAL A 1 104 ? -10.20400 -18.64200 26.32600  1.000 42.45244  ? 104 VAL A HG21 1 
ATOM   1663 H HG22 . VAL A 1 104 ? -11.50200 -19.22700 27.03000  1.000 42.45244  ? 104 VAL A HG22 1 
ATOM   1664 H HG23 . VAL A 1 104 ? -11.64600 -18.23700 25.79700  1.000 42.45244  ? 104 VAL A HG23 1 
ATOM   1665 N N    . ARG A 1 105 ? -12.51500 -15.91800 30.22800  1.000 26.79829  ? 105 ARG A N    1 
ATOM   1666 C CA   . ARG A 1 105 ? -12.36900 -14.78400 31.11900  1.000 26.77036  ? 105 ARG A CA   1 
ATOM   1667 C C    . ARG A 1 105 ? -10.89400 -14.69000 31.43400  1.000 25.41755  ? 105 ARG A C    1 
ATOM   1668 O O    . ARG A 1 105 ? -10.30600 -15.68900 31.86400  1.000 28.59686  ? 105 ARG A O    1 
ATOM   1669 C CB   . ARG A 1 105 ? -13.16000 -14.96000 32.41100  1.000 28.41256  ? 105 ARG A CB   1 
ATOM   1670 C CG   . ARG A 1 105 ? -13.04900 -13.74800 33.31300  1.000 30.65173  ? 105 ARG A CG   1 
ATOM   1671 C CD   . ARG A 1 105 ? -13.97700 -13.90800 34.53500  1.000 33.31309  ? 105 ARG A CD   1 
ATOM   1672 N NE   . ARG A 1 105 ? -13.82700 -12.73700 35.39200  1.000 30.21113  ? 105 ARG A NE   1 
ATOM   1673 C CZ   . ARG A 1 105 ? -14.53700 -11.62300 35.26900  1.000 27.99529  ? 105 ARG A CZ   1 
ATOM   1674 N NH1  . ARG A 1 105 ? -15.40400 -11.45700 34.27500  1.000 28.07528  ? 105 ARG A NH1  1 
ATOM   1675 N NH2  . ARG A 1 105 ? -14.37800 -10.65800 36.16500  1.000 30.51426  ? 105 ARG A NH2  1 
ATOM   1676 H H    . ARG A 1 105 ? -12.55500 -16.67700 30.62900  1.000 32.15875  ? 105 ARG A H    1 
ATOM   1677 H HA   . ARG A 1 105 ? -12.65500 -13.96800 30.67900  1.000 32.12523  ? 105 ARG A HA   1 
ATOM   1678 H HB2  . ARG A 1 105 ? -14.09700 -15.09200 32.19600  1.000 34.09588  ? 105 ARG A HB2  1 
ATOM   1679 H HB3  . ARG A 1 105 ? -12.81600 -15.72800 32.89300  1.000 34.09588  ? 105 ARG A HB3  1 
ATOM   1680 H HG2  . ARG A 1 105 ? -12.13700 -13.66000 33.63100  1.000 36.78287  ? 105 ARG A HG2  1 
ATOM   1681 H HG3  . ARG A 1 105 ? -13.31700 -12.95400 32.82400  1.000 36.78287  ? 105 ARG A HG3  1 
ATOM   1682 H HD2  . ARG A 1 105 ? -14.90000 -13.97400 34.24400  1.000 39.97651  ? 105 ARG A HD2  1 
ATOM   1683 H HD3  . ARG A 1 105 ? -13.72000 -14.69600 35.03900  1.000 39.97651  ? 105 ARG A HD3  1 
ATOM   1684 H HE   . ARG A 1 105 ? -13.23900 -12.77100 36.01900  1.000 36.25416  ? 105 ARG A HE   1 
ATOM   1685 H HH11 . ARG A 1 105 ? -15.51800 -12.07700 33.69100  1.000 33.69114  ? 105 ARG A HH11 1 
ATOM   1686 H HH12 . ARG A 1 105 ? -15.85200 -10.72500 34.21500  1.000 33.69114  ? 105 ARG A HH12 1 
ATOM   1687 H HH21 . ARG A 1 105 ? -13.81700 -10.75800 36.80900  1.000 36.61791  ? 105 ARG A HH21 1 
ATOM   1688 H HH22 . ARG A 1 105 ? -14.82800 -9.92800  36.09500  1.000 36.61791  ? 105 ARG A HH22 1 
ATOM   1689 N N    . ILE A 1 106 ? -10.28700 -13.52300 31.17200  1.000 25.33660  ? 106 ILE A N    1 
ATOM   1690 C CA   . ILE A 1 106 ? -8.84200  -13.35400 31.31800  1.000 26.84232  ? 106 ILE A CA   1 
ATOM   1691 C C    . ILE A 1 106 ? -8.49400  -12.74100 32.67100  1.000 27.39334  ? 106 ILE A C    1 
ATOM   1692 O O    . ILE A 1 106 ? -9.34200  -12.23500 33.41600  1.000 27.55971  ? 106 ILE A O    1 
ATOM   1693 C CB   . ILE A 1 106 ? -8.24000  -12.53300 30.14100  1.000 22.16649  ? 106 ILE A CB   1 
ATOM   1694 C CG1  . ILE A 1 106 ? -8.86900  -11.12600 30.10300  1.000 24.62624  ? 106 ILE A CG1  1 
ATOM   1695 C CG2  . ILE A 1 106 ? -8.50900  -13.29900 28.85900  1.000 23.79023  ? 106 ILE A CG2  1 
ATOM   1696 C CD1  . ILE A 1 106 ? -8.18200  -10.13000 29.08200  1.000 27.23113  ? 106 ILE A CD1  1 
ATOM   1697 H H    . ILE A 1 106 ? -10.69700 -12.81500 30.90800  1.000 30.40472  ? 106 ILE A H    1 
ATOM   1698 H HA   . ILE A 1 106 ? -8.43100  -14.23200 31.29000  1.000 32.21158  ? 106 ILE A HA   1 
ATOM   1699 H HB   . ILE A 1 106 ? -7.28200  -12.45000 30.26800  1.000 26.60059  ? 106 ILE A HB   1 
ATOM   1700 H HG12 . ILE A 1 106 ? -9.80100  -11.20900 29.84800  1.000 29.55229  ? 106 ILE A HG12 1 
ATOM   1701 H HG13 . ILE A 1 106 ? -8.80600  -10.72700 30.98400  1.000 29.55229  ? 106 ILE A HG13 1 
ATOM   1702 H HG21 . ILE A 1 106 ? -8.12000  -12.81400 28.11400  1.000 28.54907  ? 106 ILE A HG21 1 
ATOM   1703 H HG22 . ILE A 1 106 ? -8.10600  -14.17900 28.92800  1.000 28.54907  ? 106 ILE A HG22 1 
ATOM   1704 H HG23 . ILE A 1 106 ? -9.46700  -13.38300 28.73500  1.000 28.54907  ? 106 ILE A HG23 1 
ATOM   1705 H HD11 . ILE A 1 106 ? -8.63300  -9.27200  29.12700  1.000 32.67816  ? 106 ILE A HD11 1 
ATOM   1706 H HD12 . ILE A 1 106 ? -7.24800  -10.02600 29.32200  1.000 32.67816  ? 106 ILE A HD12 1 
ATOM   1707 H HD13 . ILE A 1 106 ? -8.25500  -10.49600 28.18700  1.000 32.67816  ? 106 ILE A HD13 1 
ATOM   1708 N N    . GLN A 1 107 ? -7.24000  -12.85600 33.03300  1.000 27.77831  ? 107 GLN A N    1 
ATOM   1709 C CA   . GLN A 1 107 ? -6.65500  -12.30300 34.24200  1.000 28.17159  ? 107 GLN A CA   1 
ATOM   1710 C C    . GLN A 1 107 ? -5.97800  -10.95800 33.94900  1.000 25.42972  ? 107 GLN A C    1 
ATOM   1711 O O    . GLN A 1 107 ? -5.51800  -10.71400 32.81800  1.000 25.88732  ? 107 GLN A O    1 
ATOM   1712 C CB   . GLN A 1 107 ? -5.62900  -13.29800 34.80400  1.000 30.50850  ? 107 GLN A CB   1 
ATOM   1713 C CG   . GLN A 1 107 ? -6.29500  -14.62400 35.19600  1.000 36.18144  ? 107 GLN A CG   1 
ATOM   1714 C CD   . GLN A 1 107 ? -7.20100  -14.45400 36.40200  1.000 41.69684  ? 107 GLN A CD   1 
ATOM   1715 O OE1  . GLN A 1 107 ? -6.81700  -13.80400 37.38200  1.000 41.85670  ? 107 GLN A OE1  1 
ATOM   1716 N NE2  . GLN A 1 107 ? -8.41900  -15.00600 36.33400  1.000 46.28823  ? 107 GLN A NE2  1 
ATOM   1717 H H    . GLN A 1 107 ? -6.66200  -13.28200 32.56000  1.000 33.33477  ? 107 GLN A H    1 
ATOM   1718 H HA   . GLN A 1 107 ? -7.35300  -12.17000 34.90100  1.000 33.80671  ? 107 GLN A HA   1 
ATOM   1719 H HB2  . GLN A 1 107 ? -4.95800  -13.48200 34.12900  1.000 36.61100  ? 107 GLN A HB2  1 
ATOM   1720 H HB3  . GLN A 1 107 ? -5.21500  -12.91900 35.59500  1.000 36.61100  ? 107 GLN A HB3  1 
ATOM   1721 H HG2  . GLN A 1 107 ? -6.83100  -14.94800 34.45600  1.000 43.41853  ? 107 GLN A HG2  1 
ATOM   1722 H HG3  . GLN A 1 107 ? -5.60900  -15.27100 35.42200  1.000 43.41853  ? 107 GLN A HG3  1 
ATOM   1723 H HE21 . GLN A 1 107 ? -8.65300  -15.44700 35.63400  1.000 55.54668  ? 107 GLN A HE21 1 
ATOM   1724 H HE22 . GLN A 1 107 ? -8.96300  -14.93000 36.99600  1.000 55.54668  ? 107 GLN A HE22 1 
ATOM   1725 N N    . PRO A 1 108 ? -5.88000  -10.07000 34.91900  1.000 25.82803  ? 108 PRO A N    1 
ATOM   1726 C CA   . PRO A 1 108 ? -5.09700  -8.83800  34.70200  1.000 26.57744  ? 108 PRO A CA   1 
ATOM   1727 C C    . PRO A 1 108 ? -3.68200  -9.16600  34.25000  1.000 28.55310  ? 108 PRO A C    1 
ATOM   1728 O O    . PRO A 1 108 ? -3.08100  -10.15200 34.68400  1.000 27.27094  ? 108 PRO A O    1 
ATOM   1729 C CB   . PRO A 1 108 ? -5.11400  -8.14100  36.06500  1.000 28.87042  ? 108 PRO A CB   1 
ATOM   1730 C CG   . PRO A 1 108 ? -5.69700  -9.11500  37.02500  1.000 35.96160  ? 108 PRO A CG   1 
ATOM   1731 C CD   . PRO A 1 108 ? -6.48700  -10.12100 36.25200  1.000 31.24590  ? 108 PRO A CD   1 
ATOM   1732 H HA   . PRO A 1 108 ? -5.52400  -8.27300  34.04100  1.000 31.89373  ? 108 PRO A HA   1 
ATOM   1733 H HB2  . PRO A 1 108 ? -4.20700  -7.91200  36.32200  1.000 34.64531  ? 108 PRO A HB2  1 
ATOM   1734 H HB3  . PRO A 1 108 ? -5.66400  -7.34400  36.01400  1.000 34.64531  ? 108 PRO A HB3  1 
ATOM   1735 H HG2  . PRO A 1 108 ? -4.97900  -9.55400  37.50700  1.000 43.15472  ? 108 PRO A HG2  1 
ATOM   1736 H HG3  . PRO A 1 108 ? -6.27400  -8.64300  37.64500  1.000 43.15472  ? 108 PRO A HG3  1 
ATOM   1737 H HD2  . PRO A 1 108 ? -6.38100  -11.00300 36.64100  1.000 37.49588  ? 108 PRO A HD2  1 
ATOM   1738 H HD3  . PRO A 1 108 ? -7.42000  -9.86100  36.20800  1.000 37.49588  ? 108 PRO A HD3  1 
ATOM   1739 N N    . GLY A 1 109 ? -3.18200  -8.35500  33.33600  1.000 24.72714  ? 109 GLY A N    1 
ATOM   1740 C CA   . GLY A 1 109 ? -1.90000  -8.58500  32.67300  1.000 26.46015  ? 109 GLY A CA   1 
ATOM   1741 C C    . GLY A 1 109 ? -2.01500  -9.25000  31.31600  1.000 26.31879  ? 109 GLY A C    1 
ATOM   1742 O O    . GLY A 1 109 ? -1.12700  -9.08600  30.47800  1.000 26.47469  ? 109 GLY A O    1 
ATOM   1743 H H    . GLY A 1 109 ? -3.57700  -7.63900  33.07000  1.000 29.67337  ? 109 GLY A H    1 
ATOM   1744 H HA2  . GLY A 1 109 ? -1.44800  -7.73600  32.55500  1.000 31.75299  ? 109 GLY A HA2  1 
ATOM   1745 H HA3  . GLY A 1 109 ? -1.34500  -9.14600  33.23800  1.000 31.75299  ? 109 GLY A HA3  1 
ATOM   1746 N N    . GLN A 1 110 ? -3.12400  -9.93400  31.05100  1.000 23.73977  ? 110 GLN A N    1 
ATOM   1747 C CA   . GLN A 1 110 ? -3.30900  -10.59400 29.78000  1.000 22.16659  ? 110 GLN A CA   1 
ATOM   1748 C C    . GLN A 1 110 ? -3.55600  -9.53700  28.70400  1.000 23.67689  ? 110 GLN A C    1 
ATOM   1749 O O    . GLN A 1 110 ? -4.13400  -8.47800  28.97100  1.000 22.87647  ? 110 GLN A O    1 
ATOM   1750 C CB   . GLN A 1 110 ? -4.50600  -11.57500 29.85000  1.000 22.95233  ? 110 GLN A CB   1 
ATOM   1751 C CG   . GLN A 1 110 ? -4.72500  -12.31000 28.54200  1.000 24.15895  ? 110 GLN A CG   1 
ATOM   1752 C CD   . GLN A 1 110 ? -3.52200  -13.17300 28.17000  1.000 27.54156  ? 110 GLN A CD   1 
ATOM   1753 O OE1  . GLN A 1 110 ? -2.66100  -12.76800 27.32100  1.000 26.59647  ? 110 GLN A OE1  1 
ATOM   1754 N NE2  . GLN A 1 110 ? -3.44900  -14.38800 28.76300  1.000 26.26514  ? 110 GLN A NE2  1 
ATOM   1755 H H    . GLN A 1 110 ? -3.78200  -10.02700 31.59700  1.000 28.48852  ? 110 GLN A H    1 
ATOM   1756 H HA   . GLN A 1 110 ? -2.50800  -11.09000 29.55200  1.000 26.60071  ? 110 GLN A HA   1 
ATOM   1757 H HB2  . GLN A 1 110 ? -4.33600  -12.23400 30.54100  1.000 27.54359  ? 110 GLN A HB2  1 
ATOM   1758 H HB3  . GLN A 1 110 ? -5.31300  -11.07700 30.05500  1.000 27.54359  ? 110 GLN A HB3  1 
ATOM   1759 H HG2  . GLN A 1 110 ? -5.49500  -12.89300 28.63300  1.000 28.99154  ? 110 GLN A HG2  1 
ATOM   1760 H HG3  . GLN A 1 110 ? -4.87500  -11.67100 27.82900  1.000 28.99154  ? 110 GLN A HG3  1 
ATOM   1761 H HE21 . GLN A 1 110 ? -4.05200  -14.62800 29.32700  1.000 31.51896  ? 110 GLN A HE21 1 
ATOM   1762 H HE22 . GLN A 1 110 ? -2.79200  -14.91400 28.58600  1.000 31.51896  ? 110 GLN A HE22 1 
ATOM   1763 N N    . THR A 1 111 ? -3.07500  -9.80800  27.49000  1.000 24.56013  ? 111 THR A N    1 
ATOM   1764 C CA   . THR A 1 111 ? -3.33200  -8.90400  26.37500  1.000 23.08425  ? 111 THR A CA   1 
ATOM   1765 C C    . THR A 1 111 ? -4.36800  -9.50500  25.43300  1.000 23.67285  ? 111 THR A C    1 
ATOM   1766 O O    . THR A 1 111 ? -4.67700  -10.70600 25.47800  1.000 23.78871  ? 111 THR A O    1 
ATOM   1767 C CB   . THR A 1 111 ? -2.04400  -8.64900  25.60900  1.000 23.54993  ? 111 THR A CB   1 
ATOM   1768 O OG1  . THR A 1 111 ? -1.58100  -9.92300  25.13700  1.000 24.75653  ? 111 THR A OG1  1 
ATOM   1769 C CG2  . THR A 1 111 ? -1.03500  -7.98300  26.57900  1.000 25.94890  ? 111 THR A CG2  1 
ATOM   1770 H H    . THR A 1 111 ? -2.60400  -10.49900 27.29000  1.000 29.47296  ? 111 THR A H    1 
ATOM   1771 H HA   . THR A 1 111 ? -3.66800  -8.05700  26.70300  1.000 27.70190  ? 111 THR A HA   1 
ATOM   1772 H HB   . THR A 1 111 ? -2.21100  -8.05400  24.86200  1.000 28.26072  ? 111 THR A HB   1 
ATOM   1773 H HG1  . THR A 1 111 ? -0.87200  -9.82600  24.69700  1.000 29.70864  ? 111 THR A HG1  1 
ATOM   1774 H HG21 . THR A 1 111 ? -0.18100  -7.86600  26.13500  1.000 31.13948  ? 111 THR A HG21 1 
ATOM   1775 H HG22 . THR A 1 111 ? -1.36700  -7.11500  26.85700  1.000 31.13948  ? 111 THR A HG22 1 
ATOM   1776 H HG23 . THR A 1 111 ? -0.90600  -8.53800  27.36400  1.000 31.13948  ? 111 THR A HG23 1 
ATOM   1777 N N    . PHE A 1 112 ? -4.88700  -8.65000  24.55500  1.000 24.31529  ? 112 PHE A N    1 
ATOM   1778 C CA   . PHE A 1 112 ? -5.83600  -9.08600  23.52100  1.000 22.83040  ? 112 PHE A CA   1 
ATOM   1779 C C    . PHE A 1 112 ? -5.95300  -7.97400  22.47900  1.000 22.11845  ? 112 PHE A C    1 
ATOM   1780 O O    . PHE A 1 112 ? -5.59200  -6.82600  22.73800  1.000 23.86307  ? 112 PHE A O    1 
ATOM   1781 C CB   . PHE A 1 112 ? -7.21200  -9.40200  24.11900  1.000 23.13291  ? 112 PHE A CB   1 
ATOM   1782 C CG   . PHE A 1 112 ? -7.77400  -8.26000  24.98100  1.000 22.23359  ? 112 PHE A CG   1 
ATOM   1783 C CD1  . PHE A 1 112 ? -7.43000  -8.15700  26.33100  1.000 26.05344  ? 112 PHE A CD1  1 
ATOM   1784 C CD2  . PHE A 1 112 ? -8.59600  -7.27300  24.42100  1.000 21.75551  ? 112 PHE A CD2  1 
ATOM   1785 C CE1  . PHE A 1 112 ? -7.94400  -7.10100  27.15900  1.000 27.59709  ? 112 PHE A CE1  1 
ATOM   1786 C CE2  . PHE A 1 112 ? -9.14400  -6.24100  25.24400  1.000 26.25333  ? 112 PHE A CE2  1 
ATOM   1787 C CZ   . PHE A 1 112 ? -8.79300  -6.13000  26.59700  1.000 26.80337  ? 112 PHE A CZ   1 
ATOM   1788 H H    . PHE A 1 112 ? -4.70800  -7.80900  24.53300  1.000 29.17915  ? 112 PHE A H    1 
ATOM   1789 H HA   . PHE A 1 112 ? -5.49800  -9.88400  23.08500  1.000 27.39729  ? 112 PHE A HA   1 
ATOM   1790 H HB2  . PHE A 1 112 ? -7.83800  -9.56700  23.39700  1.000 27.76030  ? 112 PHE A HB2  1 
ATOM   1791 H HB3  . PHE A 1 112 ? -7.13800  -10.19000 24.67900  1.000 27.76030  ? 112 PHE A HB3  1 
ATOM   1792 H HD1  . PHE A 1 112 ? -6.87300  -8.79900  26.70800  1.000 31.26494  ? 112 PHE A HD1  1 
ATOM   1793 H HD2  . PHE A 1 112 ? -8.84600  -7.33300  23.52700  1.000 26.10741  ? 112 PHE A HD2  1 
ATOM   1794 H HE1  . PHE A 1 112 ? -7.71100  -7.05500  28.05800  1.000 33.11731  ? 112 PHE A HE1  1 
ATOM   1795 H HE2  . PHE A 1 112 ? -9.69000  -5.59300  24.86000  1.000 31.50479  ? 112 PHE A HE2  1 
ATOM   1796 H HZ   . PHE A 1 112 ? -9.13400  -5.44100  27.11800  1.000 32.16484  ? 112 PHE A HZ   1 
ATOM   1797 N N    . SER A 1 113 ? -6.48500  -8.33000  21.31100  1.000 21.11180  ? 113 SER A N    1 
ATOM   1798 C CA   . SER A 1 113 ? -6.78400  -7.38200  20.23700  1.000 21.16979  ? 113 SER A CA   1 
ATOM   1799 C C    . SER A 1 113 ? -8.20600  -6.87100  20.40700  1.000 23.12843  ? 113 SER A C    1 
ATOM   1800 O O    . SER A 1 113 ? -9.09900  -7.61800  20.83400  1.000 22.97961  ? 113 SER A O    1 
ATOM   1801 C CB   . SER A 1 113 ? -6.68700  -8.06500  18.88200  1.000 21.73794  ? 113 SER A CB   1 
ATOM   1802 O OG   . SER A 1 113 ? -5.37800  -8.66400  18.73400  1.000 21.77987  ? 113 SER A OG   1 
ATOM   1803 H H    . SER A 1 113 ? -6.68800  -9.14100  21.11100  1.000 25.33496  ? 113 SER A H    1 
ATOM   1804 H HA   . SER A 1 113 ? -6.16700  -6.63400  20.26500  1.000 25.40455  ? 113 SER A HA   1 
ATOM   1805 H HB2  . SER A 1 113 ? -7.36400  -8.75700  18.82400  1.000 26.08633  ? 113 SER A HB2  1 
ATOM   1806 H HB3  . SER A 1 113 ? -6.81900  -7.40700  18.18200  1.000 26.08633  ? 113 SER A HB3  1 
ATOM   1807 H HG   . SER A 1 113 ? -4.78400  -8.07300  18.79000  1.000 26.13664  ? 113 SER A HG   1 
ATOM   1808 N N    . VAL A 1 114 ? -8.39900  -5.60000  20.09100  1.000 21.13809  ? 114 VAL A N    1 
ATOM   1809 C CA   . VAL A 1 114 ? -9.71700  -4.96300  20.10000  1.000 20.26923  ? 114 VAL A CA   1 
ATOM   1810 C C    . VAL A 1 114 ? -10.06300 -4.57700  18.66900  1.000 21.11143  ? 114 VAL A C    1 
ATOM   1811 O O    . VAL A 1 114 ? -9.26300  -3.91800  17.99900  1.000 20.56882  ? 114 VAL A O    1 
ATOM   1812 C CB   . VAL A 1 114 ? -9.73100  -3.72200  21.00600  1.000 21.06696  ? 114 VAL A CB   1 
ATOM   1813 C CG1  . VAL A 1 114 ? -11.09100 -2.90700  20.82200  1.000 20.88423  ? 114 VAL A CG1  1 
ATOM   1814 C CG2  . VAL A 1 114 ? -9.48400  -4.15700  22.47700  1.000 25.19957  ? 114 VAL A CG2  1 
ATOM   1815 H H    . VAL A 1 114 ? -7.76500  -5.06600  19.86000  1.000 25.36650  ? 114 VAL A H    1 
ATOM   1816 H HA   . VAL A 1 114 ? -10.38300 -5.59000  20.42200  1.000 24.32387  ? 114 VAL A HA   1 
ATOM   1817 H HB   . VAL A 1 114 ? -9.00100  -3.13900  20.74500  1.000 25.28116  ? 114 VAL A HB   1 
ATOM   1818 H HG11 . VAL A 1 114 ? -11.12200 -2.20700  21.49100  1.000 25.06188  ? 114 VAL A HG11 1 
ATOM   1819 H HG12 . VAL A 1 114 ? -11.11400 -2.51300  19.93600  1.000 25.06188  ? 114 VAL A HG12 1 
ATOM   1820 H HG13 . VAL A 1 114 ? -11.84100 -3.51100  20.93800  1.000 25.06188  ? 114 VAL A HG13 1 
ATOM   1821 H HG21 . VAL A 1 114 ? -9.51300  -3.37300  23.04700  1.000 30.24028  ? 114 VAL A HG21 1 
ATOM   1822 H HG22 . VAL A 1 114 ? -10.17600 -4.78400  22.74100  1.000 30.24028  ? 114 VAL A HG22 1 
ATOM   1823 H HG23 . VAL A 1 114 ? -8.61300  -4.57900  22.53900  1.000 30.24028  ? 114 VAL A HG23 1 
ATOM   1824 N N    . LEU A 1 115 ? -11.25100 -4.97400  18.21500  1.000 21.01592  ? 115 LEU A N    1 
ATOM   1825 C CA   . LEU A 1 115 ? -11.81200 -4.50000  16.94100  1.000 20.87377  ? 115 LEU A CA   1 
ATOM   1826 C C    . LEU A 1 115 ? -12.84600 -3.42600  17.27800  1.000 21.85475  ? 115 LEU A C    1 
ATOM   1827 O O    . LEU A 1 115 ? -13.98200 -3.72600  17.66300  1.000 22.80262  ? 115 LEU A O    1 
ATOM   1828 C CB   . LEU A 1 115 ? -12.39400 -5.67400  16.16800  1.000 20.09364  ? 115 LEU A CB   1 
ATOM   1829 C CG   . LEU A 1 115 ? -13.01300 -5.18400  14.84100  1.000 21.83693  ? 115 LEU A CG   1 
ATOM   1830 C CD1  . LEU A 1 115 ? -11.89800 -4.70900  13.80200  1.000 21.60688  ? 115 LEU A CD1  1 
ATOM   1831 C CD2  . LEU A 1 115 ? -13.80200 -6.28000  14.24200  1.000 25.17111  ? 115 LEU A CD2  1 
ATOM   1832 H H    . LEU A 1 115 ? -11.76200 -5.52600  18.63100  1.000 25.21991  ? 115 LEU A H    1 
ATOM   1833 H HA   . LEU A 1 115 ? -11.11100 -4.09600  16.40700  1.000 25.04932  ? 115 LEU A HA   1 
ATOM   1834 H HB2  . LEU A 1 115 ? -11.69000 -6.30900  15.96400  1.000 24.11317  ? 115 LEU A HB2  1 
ATOM   1835 H HB3  . LEU A 1 115 ? -13.09000 -6.09600  16.69500  1.000 24.11317  ? 115 LEU A HB3  1 
ATOM   1836 H HG   . LEU A 1 115 ? -13.61200 -4.44100  15.00800  1.000 26.20512  ? 115 LEU A HG   1 
ATOM   1837 H HD11 . LEU A 1 115 ? -12.32100 -4.52100  12.95000  1.000 25.92905  ? 115 LEU A HD11 1 
ATOM   1838 H HD12 . LEU A 1 115 ? -11.46900 -3.90800  14.14200  1.000 25.92905  ? 115 LEU A HD12 1 
ATOM   1839 H HD13 . LEU A 1 115 ? -11.24300 -5.41700  13.69700  1.000 25.92905  ? 115 LEU A HD13 1 
ATOM   1840 H HD21 . LEU A 1 115 ? -14.17300 -5.97700  13.39800  1.000 30.20613  ? 115 LEU A HD21 1 
ATOM   1841 H HD22 . LEU A 1 115 ? -13.22100 -7.04200  14.09400  1.000 30.20613  ? 115 LEU A HD22 1 
ATOM   1842 H HD23 . LEU A 1 115 ? -14.51800 -6.52200  14.85000  1.000 30.20613  ? 115 LEU A HD23 1 
ATOM   1843 N N    . ALA A 1 116 ? -12.41800 -2.17500  17.25000  1.000 21.60166  ? 116 ALA A N    1 
ATOM   1844 C CA   . ALA A 1 116 ? -13.31800 -1.07800  17.58700  1.000 22.38891  ? 116 ALA A CA   1 
ATOM   1845 C C    . ALA A 1 116 ? -14.27200 -0.83900  16.42300  1.000 23.39903  ? 116 ALA A C    1 
ATOM   1846 O O    . ALA A 1 116 ? -13.82200 -0.64300  15.28900  1.000 24.26045  ? 116 ALA A O    1 
ATOM   1847 C CB   . ALA A 1 116 ? -12.52600 0.19700   17.85900  1.000 23.30783  ? 116 ALA A CB   1 
ATOM   1848 H H    . ALA A 1 116 ? -11.62000 -1.93200  17.04200  1.000 25.92280  ? 116 ALA A H    1 
ATOM   1849 H HA   . ALA A 1 116 ? -13.83400 -1.30300  18.37700  1.000 26.86749  ? 116 ALA A HA   1 
ATOM   1850 H HB1  . ALA A 1 116 ? -13.14400 0.91100   18.08000  1.000 27.97019  ? 116 ALA A HB1  1 
ATOM   1851 H HB2  . ALA A 1 116 ? -11.92100 0.04000   18.60100  1.000 27.97019  ? 116 ALA A HB2  1 
ATOM   1852 H HB3  . ALA A 1 116 ? -12.02100 0.43000   17.06400  1.000 27.97019  ? 116 ALA A HB3  1 
ATOM   1853 N N    . CYS A 1 117 ? -15.58900 -0.84400  16.71600  1.000 20.47404  ? 117 CYS A N    1 
ATOM   1854 C CA   . CYS A 1 117 ? -16.64700 -0.77200  15.73200  1.000 22.93638  ? 117 CYS A CA   1 
ATOM   1855 C C    . CYS A 1 117 ? -17.65800 0.28600   16.11500  1.000 27.20861  ? 117 CYS A C    1 
ATOM   1856 O O    . CYS A 1 117 ? -17.88700 0.56000   17.30900  1.000 23.15246  ? 117 CYS A O    1 
ATOM   1857 C CB   . CYS A 1 117 ? -17.43100 -2.08600  15.59200  1.000 24.93057  ? 117 CYS A CB   1 
ATOM   1858 S SG   . CYS A 1 117 ? -16.43100 -3.45400  15.08900  1.000 25.28266  ? 117 CYS A SG   1 
ATOM   1859 H H    . CYS A 1 117 ? -15.88900 -0.89100  17.52100  1.000 24.56965  ? 117 CYS A H    1 
ATOM   1860 H HA   . CYS A 1 117 ? -16.27200 -0.54200  14.86800  1.000 27.52446  ? 117 CYS A HA   1 
ATOM   1861 H HB2  . CYS A 1 117 ? -17.82800 -2.30700  16.44900  1.000 29.91748  ? 117 CYS A HB2  1 
ATOM   1862 H HB3  . CYS A 1 117 ? -18.12700 -1.96600  14.92700  1.000 29.91748  ? 117 CYS A HB3  1 
ATOM   1863 H HG   . CYS A 1 117 ? -15.58100 -3.64100  15.91300  1.000 30.34000  ? 117 CYS A HG   1 
ATOM   1864 N N    . TYR A 1 118 ? -18.33100 0.80200   15.07400  1.000 25.73352  ? 118 TYR A N    1 
ATOM   1865 C CA   . TYR A 1 118 ? -19.41200 1.77700   15.22100  1.000 25.79767  ? 118 TYR A CA   1 
ATOM   1866 C C    . TYR A 1 118 ? -20.48100 1.36300   14.23000  1.000 26.96018  ? 118 TYR A C    1 
ATOM   1867 O O    . TYR A 1 118 ? -20.17200 1.06800   13.05800  1.000 25.92523  ? 118 TYR A O    1 
ATOM   1868 C CB   . TYR A 1 118 ? -18.95600 3.23300   14.95800  1.000 29.09027  ? 118 TYR A CB   1 
ATOM   1869 C CG   . TYR A 1 118 ? -17.87700 3.61000   15.94600  1.000 26.49385  ? 118 TYR A CG   1 
ATOM   1870 C CD1  . TYR A 1 118 ? -18.21100 4.12300   17.16800  1.000 26.70438  ? 118 TYR A CD1  1 
ATOM   1871 C CD2  . TYR A 1 118 ? -16.53200 3.31700   15.68500  1.000 25.30737  ? 118 TYR A CD2  1 
ATOM   1872 C CE1  . TYR A 1 118 ? -17.24400 4.40300   18.12200  1.000 26.73519  ? 118 TYR A CE1  1 
ATOM   1873 C CE2  . TYR A 1 118 ? -15.55100 3.59300   16.63400  1.000 27.43835  ? 118 TYR A CE2  1 
ATOM   1874 C CZ   . TYR A 1 118 ? -15.92100 4.13800   17.83200  1.000 27.97604  ? 118 TYR A CZ   1 
ATOM   1875 O OH   . TYR A 1 118 ? -14.95800 4.39300   18.78000  1.000 26.49319  ? 118 TYR A OH   1 
ATOM   1876 H H    . TYR A 1 118 ? -18.17100 0.59400   14.25500  1.000 30.88102  ? 118 TYR A H    1 
ATOM   1877 H HA   . TYR A 1 118 ? -19.78100 1.72400   16.11700  1.000 30.95800  ? 118 TYR A HA   1 
ATOM   1878 H HB2  . TYR A 1 118 ? -18.59400 3.30500   14.06100  1.000 34.90913  ? 118 TYR A HB2  1 
ATOM   1879 H HB3  . TYR A 1 118 ? -19.70700 3.83600   15.07300  1.000 34.90913  ? 118 TYR A HB3  1 
ATOM   1880 H HD1  . TYR A 1 118 ? -19.10400 4.29700   17.36000  1.000 32.04606  ? 118 TYR A HD1  1 
ATOM   1881 H HD2  . TYR A 1 118 ? -16.29100 2.94400   14.86800  1.000 30.36964  ? 118 TYR A HD2  1 
ATOM   1882 H HE1  . TYR A 1 118 ? -17.48300 4.76800   18.94300  1.000 32.08303  ? 118 TYR A HE1  1 
ATOM   1883 H HE2  . TYR A 1 118 ? -14.65600 3.41400   16.45300  1.000 32.92682  ? 118 TYR A HE2  1 
ATOM   1884 H HH   . TYR A 1 118 ? -14.20000 4.19200   18.48000  1.000 31.79262  ? 118 TYR A HH   1 
ATOM   1885 N N    . ASN A 1 119 ? -21.72300 1.30200   14.70800  1.000 29.00209  ? 119 ASN A N    1 
ATOM   1886 C CA   . ASN A 1 119 ? -22.83900 0.95800   13.82700  1.000 31.87040  ? 119 ASN A CA   1 
ATOM   1887 C C    . ASN A 1 119 ? -22.64500 -0.38900  13.15300  1.000 31.55500  ? 119 ASN A C    1 
ATOM   1888 O O    . ASN A 1 119 ? -23.07100 -0.58800  12.00900  1.000 33.55229  ? 119 ASN A O    1 
ATOM   1889 C CB   . ASN A 1 119 ? -23.04300 2.06100   12.78400  1.000 32.04278  ? 119 ASN A CB   1 
ATOM   1890 C CG   . ASN A 1 119 ? -23.49900 3.35400   13.44300  1.000 39.40080  ? 119 ASN A CG   1 
ATOM   1891 O OD1  . ASN A 1 119 ? -22.79600 4.34200   13.45500  1.000 45.54604  ? 119 ASN A OD1  1 
ATOM   1892 N ND2  . ASN A 1 119 ? -24.67300 3.31700   14.06500  1.000 47.01359  ? 119 ASN A ND2  1 
ATOM   1893 H H    . ASN A 1 119 ? -21.94400 1.45300   15.52500  1.000 34.80331  ? 119 ASN A H    1 
ATOM   1894 H HA   . ASN A 1 119 ? -23.64800 0.90400   14.36000  1.000 38.24528  ? 119 ASN A HA   1 
ATOM   1895 H HB2  . ASN A 1 119 ? -22.20800 2.23100   12.32100  1.000 38.45214  ? 119 ASN A HB2  1 
ATOM   1896 H HB3  . ASN A 1 119 ? -23.72700 1.78500   12.15400  1.000 38.45214  ? 119 ASN A HB3  1 
ATOM   1897 H HD21 . ASN A 1 119 ? -24.97300 4.02000   14.45900  1.000 56.41710  ? 119 ASN A HD21 1 
ATOM   1898 H HD22 . ASN A 1 119 ? -25.14500 2.59800   14.05100  1.000 56.41710  ? 119 ASN A HD22 1 
ATOM   1899 N N    . GLY A 1 120 ? -22.00100 -1.32000  13.84700  1.000 27.12867  ? 120 GLY A N    1 
ATOM   1900 C CA   . GLY A 1 120 ? -21.77300 -2.64900  13.31600  1.000 28.49997  ? 120 GLY A CA   1 
ATOM   1901 C C    . GLY A 1 120 ? -20.61700 -2.75500  12.33300  1.000 31.15642  ? 120 GLY A C    1 
ATOM   1902 O O    . GLY A 1 120 ? -20.37900 -3.84900  11.80700  1.000 32.44000  ? 120 GLY A O    1 
ATOM   1903 H H    . GLY A 1 120 ? -21.68400 -1.20100  14.63800  1.000 32.55520  ? 120 GLY A H    1 
ATOM   1904 H HA2  . GLY A 1 120 ? -21.59600 -3.25600  14.05200  1.000 34.20077  ? 120 GLY A HA2  1 
ATOM   1905 H HA3  . GLY A 1 120 ? -22.57700 -2.95000  12.86500  1.000 34.20077  ? 120 GLY A HA3  1 
ATOM   1906 N N    . SER A 1 121 ? -19.90200 -1.65800  12.06300  1.000 27.46674  ? 121 SER A N    1 
ATOM   1907 C CA   . SER A 1 121 ? -18.78800 -1.66200  11.09100  1.000 29.07511  ? 121 SER A CA   1 
ATOM   1908 C C    . SER A 1 121 ? -17.45600 -1.36800  11.76600  1.000 25.45602  ? 121 SER A C    1 
ATOM   1909 O O    . SER A 1 121 ? -17.38200 -0.51500  12.64800  1.000 25.80087  ? 121 SER A O    1 
ATOM   1910 C CB   . SER A 1 121 ? -19.02600 -0.64500  9.97300   1.000 33.58180  ? 121 SER A CB   1 
ATOM   1911 O OG   . SER A 1 121 ? -20.23900 -0.98300  9.31700   1.000 36.78263  ? 121 SER A OG   1 
ATOM   1912 H H    . SER A 1 121 ? -20.03900 -0.89200  12.42900  1.000 32.96089  ? 121 SER A H    1 
ATOM   1913 H HA   . SER A 1 121 ? -18.74700 -2.54000  10.68500  1.000 34.89094  ? 121 SER A HA   1 
ATOM   1914 H HB2  . SER A 1 121 ? -19.10000 0.24400   10.35400  1.000 40.29896  ? 121 SER A HB2  1 
ATOM   1915 H HB3  . SER A 1 121 ? -18.29300 -0.68300  9.33900   1.000 40.29896  ? 121 SER A HB3  1 
ATOM   1916 H HG   . SER A 1 121 ? -20.39200 -0.43700  8.69700   1.000 44.13996  ? 121 SER A HG   1 
ATOM   1917 N N    . PRO A 1 122 ? -16.40000 -2.06300  11.38000  1.000 30.65460  ? 122 PRO A N    1 
ATOM   1918 C CA   . PRO A 1 122 ? -15.10900 -1.89400  12.05400  1.000 27.58130  ? 122 PRO A CA   1 
ATOM   1919 C C    . PRO A 1 122 ? -14.42500 -0.58000  11.72700  1.000 27.68319  ? 122 PRO A C    1 
ATOM   1920 O O    . PRO A 1 122 ? -14.39700 -0.12200  10.57600  1.000 29.31856  ? 122 PRO A O    1 
ATOM   1921 C CB   . PRO A 1 122 ? -14.30400 -3.07800  11.52900  1.000 31.67890  ? 122 PRO A CB   1 
ATOM   1922 C CG   . PRO A 1 122 ? -14.79600 -3.19800  10.06700  1.000 34.47837  ? 122 PRO A CG   1 
ATOM   1923 C CD   . PRO A 1 122 ? -16.31300 -2.99800  10.23600  1.000 30.94834  ? 122 PRO A CD   1 
ATOM   1924 H HA   . PRO A 1 122 ? -15.21300 -1.97400  13.01500  1.000 33.09837  ? 122 PRO A HA   1 
ATOM   1925 H HB2  . PRO A 1 122 ? -13.35600 -2.88000  11.56700  1.000 38.01548  ? 122 PRO A HB2  1 
ATOM   1926 H HB3  . PRO A 1 122 ? -14.51700 -3.87700  12.03600  1.000 38.01548  ? 122 PRO A HB3  1 
ATOM   1927 H HG2  . PRO A 1 122 ? -14.40600 -2.49700  9.52100   1.000 41.37484  ? 122 PRO A HG2  1 
ATOM   1928 H HG3  . PRO A 1 122 ? -14.59300 -4.07800  9.71400   1.000 41.37484  ? 122 PRO A HG3  1 
ATOM   1929 H HD2  . PRO A 1 122 ? -16.69300 -2.59600  9.43900   1.000 37.13880  ? 122 PRO A HD2  1 
ATOM   1930 H HD3  . PRO A 1 122 ? -16.74400 -3.83900  10.45200  1.000 37.13880  ? 122 PRO A HD3  1 
ATOM   1931 N N    . SER A 1 123 ? -13.83400 0.01900   12.75100  1.000 25.73555  ? 123 SER A N    1 
ATOM   1932 C CA   . SER A 1 123 ? -13.04600 1.21700   12.51900  1.000 27.27291  ? 123 SER A CA   1 
ATOM   1933 C C    . SER A 1 123 ? -11.54900 0.91500   12.50900  1.000 30.32704  ? 123 SER A C    1 
ATOM   1934 O O    . SER A 1 123 ? -10.79800 1.46900   11.66800  1.000 27.97118  ? 123 SER A O    1 
ATOM   1935 C CB   . SER A 1 123 ? -13.35700 2.26800   13.60100  1.000 31.32288  ? 123 SER A CB   1 
ATOM   1936 O OG   . SER A 1 123 ? -12.46400 3.40500   13.56500  1.000 36.72181  ? 123 SER A OG   1 
ATOM   1937 H H    . SER A 1 123 ? -13.87200 -0.24000  13.57000  1.000 30.88346  ? 123 SER A H    1 
ATOM   1938 H HA   . SER A 1 123 ? -13.28000 1.59900   11.65900  1.000 32.72829  ? 123 SER A HA   1 
ATOM   1939 H HB2  . SER A 1 123 ? -14.26400 2.58500   13.47100  1.000 37.58825  ? 123 SER A HB2  1 
ATOM   1940 H HB3  . SER A 1 123 ? -13.28300 1.84600   14.47100  1.000 37.58825  ? 123 SER A HB3  1 
ATOM   1941 H HG   . SER A 1 123 ? -12.51900 3.79000   12.82000  1.000 44.06697  ? 123 SER A HG   1 
ATOM   1942 N N    . GLY A 1 124 ? -11.10400 0.00100   13.35800  1.000 25.94942  ? 124 GLY A N    1 
ATOM   1943 C CA   . GLY A 1 124 ? -9.66700  -0.25100  13.46200  1.000 25.99327  ? 124 GLY A CA   1 
ATOM   1944 C C    . GLY A 1 124 ? -9.41400  -1.37900  14.44000  1.000 23.10660  ? 124 GLY A C    1 
ATOM   1945 O O    . GLY A 1 124 ? -10.29900 -1.78600  15.20900  1.000 22.53774  ? 124 GLY A O    1 
ATOM   1946 H H    . GLY A 1 124 ? -11.59600 -0.47900  13.87500  1.000 31.14011  ? 124 GLY A H    1 
ATOM   1947 H HA2  . GLY A 1 124 ? -9.31100  -0.49900  12.59500  1.000 31.19273  ? 124 GLY A HA2  1 
ATOM   1948 H HA3  . GLY A 1 124 ? -9.21300  0.54700   13.77400  1.000 31.19273  ? 124 GLY A HA3  1 
ATOM   1949 N N    . VAL A 1 125 ? -8.16100  -1.84300  14.46700  1.000 22.31656  ? 125 VAL A N    1 
ATOM   1950 C CA   . VAL A 1 125 ? -7.79700  -2.92200  15.36700  1.000 21.76432  ? 125 VAL A CA   1 
ATOM   1951 C C    . VAL A 1 125 ? -6.52200  -2.51100  16.09900  1.000 23.13583  ? 125 VAL A C    1 
ATOM   1952 O O    . VAL A 1 125 ? -5.62200  -1.90000  15.49400  1.000 24.93330  ? 125 VAL A O    1 
ATOM   1953 C CB   . VAL A 1 125 ? -7.65800  -4.26000  14.61200  1.000 26.64951  ? 125 VAL A CB   1 
ATOM   1954 C CG1  . VAL A 1 125 ? -6.56000  -4.19200  13.60200  1.000 33.44797  ? 125 VAL A CG1  1 
ATOM   1955 C CG2  . VAL A 1 125 ? -7.42400  -5.42600  15.60700  1.000 25.08206  ? 125 VAL A CG2  1 
ATOM   1956 H H    . VAL A 1 125 ? -7.51600  -1.55000  13.97900  1.000 26.78068  ? 125 VAL A H    1 
ATOM   1957 H HA   . VAL A 1 125 ? -8.49500  -3.02800  16.02800  1.000 26.11799  ? 125 VAL A HA   1 
ATOM   1958 H HB   . VAL A 1 125 ? -8.48500  -4.43800  14.13800  1.000 31.98022  ? 125 VAL A HB   1 
ATOM   1959 H HG11 . VAL A 1 125 ? -6.56500  -5.00800  13.07800  1.000 40.13837  ? 125 VAL A HG11 1 
ATOM   1960 H HG12 . VAL A 1 125 ? -6.70800  -3.42800  13.02300  1.000 40.13837  ? 125 VAL A HG12 1 
ATOM   1961 H HG13 . VAL A 1 125 ? -5.71100  -4.10000  14.06100  1.000 40.13837  ? 125 VAL A HG13 1 
ATOM   1962 H HG21 . VAL A 1 125 ? -7.39100  -6.26000  15.11300  1.000 30.09927  ? 125 VAL A HG21 1 
ATOM   1963 H HG22 . VAL A 1 125 ? -6.58400  -5.28300  16.07100  1.000 30.09927  ? 125 VAL A HG22 1 
ATOM   1964 H HG23 . VAL A 1 125 ? -8.15500  -5.44800  16.24400  1.000 30.09927  ? 125 VAL A HG23 1 
ATOM   1965 N N    . TYR A 1 126 ? -6.49200  -2.73800  17.40400  1.000 20.10898  ? 126 TYR A N    1 
ATOM   1966 C CA   . TYR A 1 126 ? -5.29700  -2.42500  18.19800  1.000 22.51499  ? 126 TYR A CA   1 
ATOM   1967 C C    . TYR A 1 126 ? -5.14800  -3.39800  19.35400  1.000 25.16704  ? 126 TYR A C    1 
ATOM   1968 O O    . TYR A 1 126 ? -6.07600  -4.12300  19.70200  1.000 23.20187  ? 126 TYR A O    1 
ATOM   1969 C CB   . TYR A 1 126 ? -5.33800  -0.97900  18.74900  1.000 22.48270  ? 126 TYR A CB   1 
ATOM   1970 C CG   . TYR A 1 126 ? -6.60800  -0.62600  19.50300  1.000 23.34317  ? 126 TYR A CG   1 
ATOM   1971 C CD1  . TYR A 1 126 ? -6.76000  -0.92800  20.86500  1.000 22.94206  ? 126 TYR A CD1  1 
ATOM   1972 C CD2  . TYR A 1 126 ? -7.68300  0.02700   18.83600  1.000 25.70884  ? 126 TYR A CD2  1 
ATOM   1973 C CE1  . TYR A 1 126 ? -7.94200  -0.55500  21.54900  1.000 23.80250  ? 126 TYR A CE1  1 
ATOM   1974 C CE2  . TYR A 1 126 ? -8.82900  0.39200   19.53000  1.000 27.11098  ? 126 TYR A CE2  1 
ATOM   1975 C CZ   . TYR A 1 126 ? -8.94700  0.08400   20.85600  1.000 26.53314  ? 126 TYR A CZ   1 
ATOM   1976 O OH   . TYR A 1 126 ? -10.12900 0.43200   21.49900  1.000 28.93607  ? 126 TYR A OH   1 
ATOM   1977 H H    . TYR A 1 126 ? -7.14300  -3.07000  17.85800  1.000 24.13158  ? 126 TYR A H    1 
ATOM   1978 H HA   . TYR A 1 126 ? -4.51200  -2.50800  17.63400  1.000 27.01879  ? 126 TYR A HA   1 
ATOM   1979 H HB2  . TYR A 1 126 ? -4.59200  -0.85700  19.35700  1.000 26.98004  ? 126 TYR A HB2  1 
ATOM   1980 H HB3  . TYR A 1 126 ? -5.25700  -0.36200  18.00500  1.000 26.98004  ? 126 TYR A HB3  1 
ATOM   1981 H HD1  . TYR A 1 126 ? -6.07100  -1.35000  21.32600  1.000 27.53128  ? 126 TYR A HD1  1 
ATOM   1982 H HD2  . TYR A 1 126 ? -7.60000  0.24700   17.93600  1.000 30.85141  ? 126 TYR A HD2  1 
ATOM   1983 H HE1  . TYR A 1 126 ? -8.04700  -0.75700  22.45100  1.000 28.56380  ? 126 TYR A HE1  1 
ATOM   1984 H HE2  . TYR A 1 126 ? -9.52900  0.81300   19.08600  1.000 32.53397  ? 126 TYR A HE2  1 
ATOM   1985 H HH   . TYR A 1 126 ? -10.64800 0.81200   20.95900  1.000 34.72409  ? 126 TYR A HH   1 
ATOM   1986 N N    . GLN A 1 127 ? -3.95300  -3.40100  19.92500  1.000 24.21064  ? 127 GLN A N    1 
ATOM   1987 C CA   . GLN A 1 127 ? -3.67100  -4.28200  21.07100  1.000 24.22443  ? 127 GLN A CA   1 
ATOM   1988 C C    . GLN A 1 127 ? -3.98400  -3.55100  22.36700  1.000 27.99114  ? 127 GLN A C    1 
ATOM   1989 O O    . GLN A 1 127 ? -3.75500  -2.34100  22.44900  1.000 27.99383  ? 127 GLN A O    1 
ATOM   1990 C CB   . GLN A 1 127 ? -2.20600  -4.69500  21.13400  1.000 33.48937  ? 127 GLN A CB   1 
ATOM   1991 C CG   . GLN A 1 127 ? -1.85000  -5.91000  20.31500  1.000 31.41750  ? 127 GLN A CG   1 
ATOM   1992 C CD   . GLN A 1 127 ? -2.51400  -7.16000  20.82600  1.000 26.53426  ? 127 GLN A CD   1 
ATOM   1993 O OE1  . GLN A 1 127 ? -3.47700  -7.63800  20.25100  1.000 30.21272  ? 127 GLN A OE1  1 
ATOM   1994 N NE2  . GLN A 1 127 ? -1.98800  -7.71100  21.90200  1.000 30.15838  ? 127 GLN A NE2  1 
ATOM   1995 H H    . GLN A 1 127 ? -3.29000  -2.91200  19.67900  1.000 29.05357  ? 127 GLN A H    1 
ATOM   1996 H HA   . GLN A 1 127 ? -4.22300  -5.07800  21.01900  1.000 29.07012  ? 127 GLN A HA   1 
ATOM   1997 H HB2  . GLN A 1 127 ? -1.68800  -3.95500  20.79300  1.000 40.18804  ? 127 GLN A HB2  1 
ATOM   1998 H HB3  . GLN A 1 127 ? -1.96600  -4.87300  22.05700  1.000 40.18804  ? 127 GLN A HB3  1 
ATOM   1999 H HG2  . GLN A 1 127 ? -2.13600  -5.77000  19.39900  1.000 37.70180  ? 127 GLN A HG2  1 
ATOM   2000 H HG3  . GLN A 1 127 ? -0.89000  -6.04400  20.34700  1.000 37.70180  ? 127 GLN A HG3  1 
ATOM   2001 H HE21 . GLN A 1 127 ? -1.30600  -7.34900  22.28100  1.000 36.19086  ? 127 GLN A HE21 1 
ATOM   2002 H HE22 . GLN A 1 127 ? -2.33200  -8.42800  22.23000  1.000 36.19086  ? 127 GLN A HE22 1 
ATOM   2003 N N    . CYS A 1 128 ? -4.46700  -4.29700  23.33600  1.000 26.10140  ? 128 CYS A N    1 
ATOM   2004 C CA   . CYS A 1 128 ? -4.80800  -3.76000  24.66100  1.000 25.79102  ? 128 CYS A CA   1 
ATOM   2005 C C    . CYS A 1 128 ? -4.40500  -4.79800  25.70800  1.000 27.21392  ? 128 CYS A C    1 
ATOM   2006 O O    . CYS A 1 128 ? -4.07000  -5.91000  25.32800  1.000 27.65273  ? 128 CYS A O    1 
ATOM   2007 C CB   . CYS A 1 128 ? -6.31400  -3.57300  24.77300  1.000 27.98090  ? 128 CYS A CB   1 
ATOM   2008 S SG   . CYS A 1 128 ? -6.84000  -1.85400  24.91600  1.000 44.90402  ? 128 CYS A SG   1 
ATOM   2009 H H    . CYS A 1 128 ? -4.61500  -5.14100  23.26100  1.000 31.32248  ? 128 CYS A H    1 
ATOM   2010 H HA   . CYS A 1 128 ? -4.35200  -2.92000  24.82900  1.000 30.95002  ? 128 CYS A HA   1 
ATOM   2011 H HB2  . CYS A 1 128 ? -6.73300  -3.94400  23.98100  1.000 33.57789  ? 128 CYS A HB2  1 
ATOM   2012 H HB3  . CYS A 1 128 ? -6.62800  -4.04400  25.56100  1.000 33.57789  ? 128 CYS A HB3  1 
ATOM   2013 H HG   . CYS A 1 128 ? -8.03700  -1.81600  24.99300  1.000 53.88562  ? 128 CYS A HG   1 
ATOM   2014 N N    . ALA A 1 129 ? -4.37600  -4.40900  26.96700  1.000 29.51240  ? 129 ALA A N    1 
ATOM   2015 C CA   . ALA A 1 129 ? -4.11100  -5.31400  28.08800  1.000 24.23626  ? 129 ALA A CA   1 
ATOM   2016 C C    . ALA A 1 129 ? -5.16400  -5.09600  29.15500  1.000 25.13922  ? 129 ALA A C    1 
ATOM   2017 O O    . ALA A 1 129 ? -5.67900  -3.99700  29.31600  1.000 26.23031  ? 129 ALA A O    1 
ATOM   2018 C CB   . ALA A 1 129 ? -2.73700  -5.12900  28.73100  1.000 26.79849  ? 129 ALA A CB   1 
ATOM   2019 H H    . ALA A 1 129 ? -4.51100  -3.59600  27.21400  1.000 35.41569  ? 129 ALA A H    1 
ATOM   2020 H HA   . ALA A 1 129 ? -4.18000  -6.23000  27.78100  1.000 29.08432  ? 129 ALA A HA   1 
ATOM   2021 H HB1  . ALA A 1 129 ? -2.63600  -5.77200  29.45000  1.000 32.15899  ? 129 ALA A HB1  1 
ATOM   2022 H HB2  . ALA A 1 129 ? -2.05200  -5.27300  28.05900  1.000 32.15899  ? 129 ALA A HB2  1 
ATOM   2023 H HB3  . ALA A 1 129 ? -2.67200  -4.22700  29.08100  1.000 32.15899  ? 129 ALA A HB3  1 
ATOM   2024 N N    . MET A 1 130 ? -5.50400  -6.15200  29.85600  1.000 21.88317  ? 130 MET A N    1 
ATOM   2025 C CA   . MET A 1 130 ? -6.29500  -5.99900  31.06100  1.000 21.86992  ? 130 MET A CA   1 
ATOM   2026 C C    . MET A 1 130 ? -5.39700  -5.43700  32.16800  1.000 22.56032  ? 130 MET A C    1 
ATOM   2027 O O    . MET A 1 130 ? -4.43600  -6.09500  32.59900  1.000 24.85052  ? 130 MET A O    1 
ATOM   2028 C CB   . MET A 1 130 ? -6.93300  -7.34400  31.41700  1.000 22.96130  ? 130 MET A CB   1 
ATOM   2029 C CG   . MET A 1 130 ? -7.82000  -7.37400  32.75000  1.000 22.98510  ? 130 MET A CG   1 
ATOM   2030 S SD   . MET A 1 130 ? -9.20400  -6.22900  32.55000  1.000 26.81076  ? 130 MET A SD   1 
ATOM   2031 C CE   . MET A 1 130 ? -10.04900 -6.83900  31.07700  1.000 25.02473  ? 130 MET A CE   1 
ATOM   2032 H H    . MET A 1 130 ? -5.29400  -6.96300  29.66200  1.000 26.26061  ? 130 MET A H    1 
ATOM   2033 H HA   . MET A 1 130 ? -7.01100  -5.36800  30.88800  1.000 26.24471  ? 130 MET A HA   1 
ATOM   2034 H HB2  . MET A 1 130 ? -7.49900  -7.62000  30.68000  1.000 27.55436  ? 130 MET A HB2  1 
ATOM   2035 H HB3  . MET A 1 130 ? -6.22200  -7.99300  31.53300  1.000 27.55436  ? 130 MET A HB3  1 
ATOM   2036 H HG2  . MET A 1 130 ? -8.17000  -8.26700  32.89400  1.000 27.58292  ? 130 MET A HG2  1 
ATOM   2037 H HG3  . MET A 1 130 ? -7.28800  -7.08400  33.50700  1.000 27.58292  ? 130 MET A HG3  1 
ATOM   2038 H HE1  . MET A 1 130 ? -10.90200 -6.38600  30.99400  1.000 30.03048  ? 130 MET A HE1  1 
ATOM   2039 H HE2  . MET A 1 130 ? -9.50100  -6.65600  30.29800  1.000 30.03048  ? 130 MET A HE2  1 
ATOM   2040 H HE3  . MET A 1 130 ? -10.19000 -7.79400  31.16700  1.000 30.03048  ? 130 MET A HE3  1 
ATOM   2041 N N    . ARG A 1 131 ? -5.66200  -4.20900  32.60600  1.000 23.62874  ? 131 ARG A N    1 
ATOM   2042 C CA   . ARG A 1 131 ? -4.81400  -3.58800  33.64400  1.000 23.05184  ? 131 ARG A CA   1 
ATOM   2043 C C    . ARG A 1 131 ? -5.03100  -4.27000  34.98600  1.000 25.43576  ? 131 ARG A C    1 
ATOM   2044 O O    . ARG A 1 131 ? -6.06700  -4.91200  35.21600  1.000 24.58430  ? 131 ARG A O    1 
ATOM   2045 C CB   . ARG A 1 131 ? -5.11400  -2.09700  33.81000  1.000 23.11548  ? 131 ARG A CB   1 
ATOM   2046 C CG   . ARG A 1 131 ? -5.04500  -1.28700  32.46200  1.000 26.90144  ? 131 ARG A CG   1 
ATOM   2047 C CD   . ARG A 1 131 ? -3.64000  -1.34700  31.77800  1.000 26.98703  ? 131 ARG A CD   1 
ATOM   2048 N NE   . ARG A 1 131 ? -2.59400  -1.14500  32.78700  1.000 25.85057  ? 131 ARG A NE   1 
ATOM   2049 C CZ   . ARG A 1 131 ? -1.29600  -1.30800  32.53400  1.000 29.21832  ? 131 ARG A CZ   1 
ATOM   2050 N NH1  . ARG A 1 131 ? -0.87100  -1.65600  31.33100  1.000 26.70943  ? 131 ARG A NH1  1 
ATOM   2051 N NH2  . ARG A 1 131 ? -0.40900  -1.16600  33.52700  1.000 28.92900  ? 131 ARG A NH2  1 
ATOM   2052 H H    . ARG A 1 131 ? -6.31100  -3.71700  32.33000  1.000 28.35529  ? 131 ARG A H    1 
ATOM   2053 H HA   . ARG A 1 131 ? -3.88900  -3.68700  33.37600  1.000 27.66301  ? 131 ARG A HA   1 
ATOM   2054 H HB2  . ARG A 1 131 ? -6.01000  -1.99900  34.16700  1.000 27.73938  ? 131 ARG A HB2  1 
ATOM   2055 H HB3  . ARG A 1 131 ? -4.47200  -1.71200  34.42700  1.000 27.73938  ? 131 ARG A HB3  1 
ATOM   2056 H HG2  . ARG A 1 131 ? -5.69400  -1.65200  31.84100  1.000 32.28253  ? 131 ARG A HG2  1 
ATOM   2057 H HG3  . ARG A 1 131 ? -5.24900  -0.35600  32.64400  1.000 32.28253  ? 131 ARG A HG3  1 
ATOM   2058 H HD2  . ARG A 1 131 ? -3.51300  -2.21800  31.36900  1.000 32.38524  ? 131 ARG A HD2  1 
ATOM   2059 H HD3  . ARG A 1 131 ? -3.57000  -0.64400  31.11400  1.000 32.38524  ? 131 ARG A HD3  1 
ATOM   2060 H HE   . ARG A 1 131 ? -2.81100  -0.73600  33.51200  1.000 31.02148  ? 131 ARG A HE   1 
ATOM   2061 H HH11 . ARG A 1 131 ? -1.43100  -1.75800  30.68600  1.000 32.05212  ? 131 ARG A HH11 1 
ATOM   2062 H HH12 . ARG A 1 131 ? -0.03000  -1.76200  31.18800  1.000 32.05212  ? 131 ARG A HH12 1 
ATOM   2063 H HH21 . ARG A 1 131 ? -0.67600  -0.94500  34.31400  1.000 34.71560  ? 131 ARG A HH21 1 
ATOM   2064 H HH22 . ARG A 1 131 ? 0.43000   -1.27300  33.37200  1.000 34.71560  ? 131 ARG A HH22 1 
ATOM   2065 N N    . PRO A 1 132 ? -4.06800  -4.11600  35.89500  1.000 25.43573  ? 132 PRO A N    1 
ATOM   2066 C CA   . PRO A 1 132 ? -4.23700  -4.64800  37.24700  1.000 25.40144  ? 132 PRO A CA   1 
ATOM   2067 C C    . PRO A 1 132 ? -5.47800  -4.12400  37.94100  1.000 26.70883  ? 132 PRO A C    1 
ATOM   2068 O O    . PRO A 1 132 ? -6.03300  -4.83700  38.76700  1.000 26.90167  ? 132 PRO A O    1 
ATOM   2069 C CB   . PRO A 1 132 ? -2.95700  -4.18600  37.97200  1.000 27.62001  ? 132 PRO A CB   1 
ATOM   2070 C CG   . PRO A 1 132 ? -1.88200  -4.16600  36.83800  1.000 28.04224  ? 132 PRO A CG   1 
ATOM   2071 C CD   . PRO A 1 132 ? -2.71300  -3.55700  35.66100  1.000 26.02703  ? 132 PRO A CD   1 
ATOM   2072 H HA   . PRO A 1 132 ? -4.26400  -5.61700  37.22800  1.000 30.48252  ? 132 PRO A HA   1 
ATOM   2073 H HB2  . PRO A 1 132 ? -3.08800  -3.29900  38.34300  1.000 33.14481  ? 132 PRO A HB2  1 
ATOM   2074 H HB3  . PRO A 1 132 ? -2.72000  -4.82300  38.66500  1.000 33.14481  ? 132 PRO A HB3  1 
ATOM   2075 H HG2  . PRO A 1 132 ? -1.14000  -3.59200  37.08400  1.000 33.65149  ? 132 PRO A HG2  1 
ATOM   2076 H HG3  . PRO A 1 132 ? -1.58600  -5.06700  36.63500  1.000 33.65149  ? 132 PRO A HG3  1 
ATOM   2077 H HD2  . PRO A 1 132 ? -2.72200  -2.59100  35.71300  1.000 31.23324  ? 132 PRO A HD2  1 
ATOM   2078 H HD3  . PRO A 1 132 ? -2.35200  -3.86500  34.81600  1.000 31.23324  ? 132 PRO A HD3  1 
ATOM   2079 N N    . ASN A 1 133 ? -5.92900  -2.90700  37.64500  1.000 24.95431  ? 133 ASN A N    1 
ATOM   2080 C CA   . ASN A 1 133 ? -7.14200  -2.38100  38.26600  1.000 26.32208  ? 133 ASN A CA   1 
ATOM   2081 C C    . ASN A 1 133 ? -8.41300  -2.74300  37.48600  1.000 30.10483  ? 133 ASN A C    1 
ATOM   2082 O O    . ASN A 1 133 ? -9.47200  -2.11500  37.70300  1.000 25.78665  ? 133 ASN A O    1 
ATOM   2083 C CB   . ASN A 1 133 ? -7.02700  -0.86200  38.43500  1.000 27.23664  ? 133 ASN A CB   1 
ATOM   2084 C CG   . ASN A 1 133 ? -6.97600  -0.10200  37.09900  1.000 28.04848  ? 133 ASN A CG   1 
ATOM   2085 O OD1  . ASN A 1 133 ? -7.01100  -0.68900  36.02200  1.000 25.30485  ? 133 ASN A OD1  1 
ATOM   2086 N ND2  . ASN A 1 133 ? -6.91800  1.20200   37.18300  1.000 29.47808  ? 133 ASN A ND2  1 
ATOM   2087 H H    . ASN A 1 133 ? -5.55300  -2.36800  37.09000  1.000 29.94597  ? 133 ASN A H    1 
ATOM   2088 H HA   . ASN A 1 133 ? -7.22600  -2.76500  39.15300  1.000 31.58730  ? 133 ASN A HA   1 
ATOM   2089 H HB2  . ASN A 1 133 ? -7.79700  -0.54200  38.93100  1.000 32.68477  ? 133 ASN A HB2  1 
ATOM   2090 H HB3  . ASN A 1 133 ? -6.21300  -0.66100  38.92300  1.000 32.68477  ? 133 ASN A HB3  1 
ATOM   2091 H HD21 . ASN A 1 133 ? -6.88900  1.67800   36.46700  1.000 35.37450  ? 133 ASN A HD21 1 
ATOM   2092 H HD22 . ASN A 1 133 ? -6.89900  1.58300   37.95400  1.000 35.37450  ? 133 ASN A HD22 1 
ATOM   2093 N N    . PHE A 1 134 ? -8.31000  -3.70900  36.56600  1.000 27.47660  ? 134 PHE A N    1 
ATOM   2094 C CA   . PHE A 1 134 ? -9.40400  -4.26200  35.76300  1.000 25.70345  ? 134 PHE A CA   1 
ATOM   2095 C C    . PHE A 1 134 ? -10.01200 -3.24800  34.80600  1.000 25.71971  ? 134 PHE A C    1 
ATOM   2096 O O    . PHE A 1 134 ? -11.15000 -3.41500  34.39100  1.000 28.76281  ? 134 PHE A O    1 
ATOM   2097 C CB   . PHE A 1 134 ? -10.49800 -4.86700  36.67200  1.000 27.29505  ? 134 PHE A CB   1 
ATOM   2098 C CG   . PHE A 1 134 ? -10.03000 -6.11900  37.37700  1.000 27.65076  ? 134 PHE A CG   1 
ATOM   2099 C CD1  . PHE A 1 134 ? -9.95400  -7.33200  36.68500  1.000 34.96880  ? 134 PHE A CD1  1 
ATOM   2100 C CD2  . PHE A 1 134 ? -9.55700  -6.05600  38.67000  1.000 34.33918  ? 134 PHE A CD2  1 
ATOM   2101 C CE1  . PHE A 1 134 ? -9.49900  -8.51200  37.36700  1.000 35.35786  ? 134 PHE A CE1  1 
ATOM   2102 C CE2  . PHE A 1 134 ? -9.10100  -7.20400  39.32600  1.000 37.67414  ? 134 PHE A CE2  1 
ATOM   2103 C CZ   . PHE A 1 134 ? -9.07700  -8.41300  38.67200  1.000 36.10365  ? 134 PHE A CZ   1 
ATOM   2104 H H    . PHE A 1 134 ? -7.56000  -4.08500  36.37800  1.000 32.97272  ? 134 PHE A H    1 
ATOM   2105 H HA   . PHE A 1 134 ? -9.04700  -4.98500  35.22400  1.000 30.84494  ? 134 PHE A HA   1 
ATOM   2106 H HB2  . PHE A 1 134 ? -10.74900 -4.21700  37.34700  1.000 32.75486  ? 134 PHE A HB2  1 
ATOM   2107 H HB3  . PHE A 1 134 ? -11.26900 -5.09900  36.13100  1.000 32.75486  ? 134 PHE A HB3  1 
ATOM   2108 H HD1  . PHE A 1 134 ? -10.26200 -7.38900  35.80900  1.000 41.96337  ? 134 PHE A HD1  1 
ATOM   2109 H HD2  . PHE A 1 134 ? -9.58700  -5.24800  39.13000  1.000 41.20782  ? 134 PHE A HD2  1 
ATOM   2110 H HE1  . PHE A 1 134 ? -9.46900  -9.32900  36.92400  1.000 42.43023  ? 134 PHE A HE1  1 
ATOM   2111 H HE2  . PHE A 1 134 ? -8.81300  -7.14900  40.20900  1.000 45.20978  ? 134 PHE A HE2  1 
ATOM   2112 H HZ   . PHE A 1 134 ? -8.76200  -9.16900  39.11300  1.000 43.32518  ? 134 PHE A HZ   1 
ATOM   2113 N N    . THR A 1 135 ? -9.29400  -2.19400  34.43900  1.000 26.98523  ? 135 THR A N    1 
ATOM   2114 C CA   . THR A 1 135 ? -9.72900  -1.35700  33.33600  1.000 24.51100  ? 135 THR A CA   1 
ATOM   2115 C C    . THR A 1 135 ? -8.92900  -1.74100  32.11800  1.000 25.13989  ? 135 THR A C    1 
ATOM   2116 O O    . THR A 1 135 ? -7.95100  -2.49500  32.20000  1.000 23.67765  ? 135 THR A O    1 
ATOM   2117 C CB   . THR A 1 135 ? -9.55900  0.13300   33.63900  1.000 25.08617  ? 135 THR A CB   1 
ATOM   2118 O OG1  . THR A 1 135 ? -8.14800  0.47600   33.82000  1.000 25.80899  ? 135 THR A OG1  1 
ATOM   2119 C CG2  . THR A 1 135 ? -10.31100 0.49100   34.92800  1.000 28.32167  ? 135 THR A CG2  1 
ATOM   2120 H H    . THR A 1 135 ? -8.55900  -1.94500  34.80900  1.000 32.38308  ? 135 THR A H    1 
ATOM   2121 H HA   . THR A 1 135 ? -10.66600 -1.52000  33.14700  1.000 29.41400  ? 135 THR A HA   1 
ATOM   2122 H HB   . THR A 1 135 ? -9.92900  0.65600   32.91100  1.000 30.10421  ? 135 THR A HB   1 
ATOM   2123 H HG1  . THR A 1 135 ? -7.82500  0.03700   34.46000  1.000 30.97159  ? 135 THR A HG1  1 
ATOM   2124 H HG21 . THR A 1 135 ? -10.28000 1.44900   35.07200  1.000 33.98681  ? 135 THR A HG21 1 
ATOM   2125 H HG22 . THR A 1 135 ? -11.23800 0.21300   34.85900  1.000 33.98681  ? 135 THR A HG22 1 
ATOM   2126 H HG23 . THR A 1 135 ? -9.90300  0.04400   35.68600  1.000 33.98681  ? 135 THR A HG23 1 
ATOM   2127 N N    . ILE A 1 136 ? -9.34400  -1.22600  30.97100  1.000 23.36462  ? 136 ILE A N    1 
ATOM   2128 C CA   . ILE A 1 136 ? -8.47100  -1.34500  29.81600  1.000 25.35796  ? 136 ILE A CA   1 
ATOM   2129 C C    . ILE A 1 136 ? -8.28300  0.05000   29.27400  1.000 24.98341  ? 136 ILE A C    1 
ATOM   2130 O O    . ILE A 1 136 ? -9.18800  0.89800   29.35700  1.000 24.38306  ? 136 ILE A O    1 
ATOM   2131 C CB   . ILE A 1 136 ? -8.98900  -2.33900  28.73500  1.000 31.21239  ? 136 ILE A CB   1 
ATOM   2132 C CG1  . ILE A 1 136 ? -10.08900 -1.71900  27.90000  1.000 30.98493  ? 136 ILE A CG1  1 
ATOM   2133 C CG2  . ILE A 1 136 ? -9.47400  -3.63200  29.40700  1.000 29.21196  ? 136 ILE A CG2  1 
ATOM   2134 C CD1  . ILE A 1 136 ? -10.52000 -2.59600  26.74700  1.000 30.50202  ? 136 ILE A CD1  1 
ATOM   2135 H H    . ILE A 1 136 ? -10.09100 -0.82100  30.83700  1.000 28.03834  ? 136 ILE A H    1 
ATOM   2136 H HA   . ILE A 1 136 ? -7.60000  -1.65900  30.10300  1.000 30.43035  ? 136 ILE A HA   1 
ATOM   2137 H HB   . ILE A 1 136 ? -8.25000  -2.56100  28.14700  1.000 37.45567  ? 136 ILE A HB   1 
ATOM   2138 H HG12 . ILE A 1 136 ? -10.86300 -1.56000  28.46300  1.000 37.18272  ? 136 ILE A HG12 1 
ATOM   2139 H HG13 . ILE A 1 136 ? -9.78300  -0.88500  27.51300  1.000 37.18272  ? 136 ILE A HG13 1 
ATOM   2140 H HG21 . ILE A 1 136 ? -9.66600  -4.29400  28.72500  1.000 35.05515  ? 136 ILE A HG21 1 
ATOM   2141 H HG22 . ILE A 1 136 ? -8.77700  -3.95900  29.99700  1.000 35.05515  ? 136 ILE A HG22 1 
ATOM   2142 H HG23 . ILE A 1 136 ? -10.27600 -3.44100  29.91800  1.000 35.05515  ? 136 ILE A HG23 1 
ATOM   2143 H HD11 . ILE A 1 136 ? -11.13300 -2.09700  26.18400  1.000 36.60323  ? 136 ILE A HD11 1 
ATOM   2144 H HD12 . ILE A 1 136 ? -9.73600  -2.85300  26.23700  1.000 36.60323  ? 136 ILE A HD12 1 
ATOM   2145 H HD13 . ILE A 1 136 ? -10.96000 -3.38600  27.09600  1.000 36.60323  ? 136 ILE A HD13 1 
ATOM   2146 N N    . LYS A 1 137 ? -7.07700  0.29400   28.74000  1.000 25.10237  ? 137 LYS A N    1 
ATOM   2147 C CA   . LYS A 1 137 ? -6.71200  1.58900   28.16700  1.000 27.83057  ? 137 LYS A CA   1 
ATOM   2148 C C    . LYS A 1 137 ? -7.00100  1.49900   26.68300  1.000 27.46505  ? 137 LYS A C    1 
ATOM   2149 O O    . LYS A 1 137 ? -6.13400  1.20300   25.84700  1.000 27.65424  ? 137 LYS A O    1 
ATOM   2150 C CB   . LYS A 1 137 ? -5.24900  1.93100   28.46700  1.000 30.86705  ? 137 LYS A CB   1 
ATOM   2151 C CG   . LYS A 1 137 ? -5.05000  2.06300   29.95600  1.000 32.36412  ? 137 LYS A CG   1 
ATOM   2152 C CD   . LYS A 1 137 ? -3.55700  2.31900   30.31600  1.000 38.55442  ? 137 LYS A CD   1 
ATOM   2153 C CE   . LYS A 1 137 ? -3.10400  3.72900   29.98400  1.000 45.21387  ? 137 LYS A CE   1 
ATOM   2154 N NZ   . LYS A 1 137 ? -1.76100  3.92700   30.62800  1.000 58.64124  ? 137 LYS A NZ   1 
ATOM   2155 H H    . LYS A 1 137 ? -6.44600  -0.28800  28.70000  1.000 30.12365  ? 137 LYS A H    1 
ATOM   2156 H HA   . LYS A 1 137 ? -7.27300  2.28200   28.54800  1.000 33.39749  ? 137 LYS A HA   1 
ATOM   2157 H HB2  . LYS A 1 137 ? -4.67500  1.22100   28.14000  1.000 37.04127  ? 137 LYS A HB2  1 
ATOM   2158 H HB3  . LYS A 1 137 ? -5.02000  2.77500   28.04800  1.000 37.04127  ? 137 LYS A HB3  1 
ATOM   2159 H HG2  . LYS A 1 137 ? -5.57400  2.81100   30.28300  1.000 38.83774  ? 137 LYS A HG2  1 
ATOM   2160 H HG3  . LYS A 1 137 ? -5.32900  1.24300   30.39100  1.000 38.83774  ? 137 LYS A HG3  1 
ATOM   2161 H HD2  . LYS A 1 137 ? -3.43400  2.18100   31.26800  1.000 46.26610  ? 137 LYS A HD2  1 
ATOM   2162 H HD3  . LYS A 1 137 ? -3.00100  1.70000   29.81700  1.000 46.26610  ? 137 LYS A HD3  1 
ATOM   2163 H HE2  . LYS A 1 137 ? -3.01300  3.82800   29.02500  1.000 54.25744  ? 137 LYS A HE2  1 
ATOM   2164 H HE3  . LYS A 1 137 ? -3.73000  4.37600   30.34600  1.000 54.25744  ? 137 LYS A HE3  1 
ATOM   2165 H HZ1  . LYS A 1 137 ? -1.82800  3.82300   31.50900  1.000 70.37029  ? 137 LYS A HZ1  1 
ATOM   2166 H HZ2  . LYS A 1 137 ? -1.18100  3.33200   30.31000  1.000 70.37029  ? 137 LYS A HZ2  1 
ATOM   2167 H HZ3  . LYS A 1 137 ? -1.45900  4.74600   30.45600  1.000 70.37029  ? 137 LYS A HZ3  1 
ATOM   2168 N N    . GLY A 1 138 ? -8.27600  1.66600   26.35400  1.000 24.84971  ? 138 GLY A N    1 
ATOM   2169 C CA   . GLY A 1 138 ? -8.72300  1.50500   24.98400  1.000 28.20729  ? 138 GLY A CA   1 
ATOM   2170 C C    . GLY A 1 138 ? -8.75900  2.81500   24.22300  1.000 27.32899  ? 138 GLY A C    1 
ATOM   2171 O O    . GLY A 1 138 ? -8.30200  3.87100   24.68300  1.000 28.34569  ? 138 GLY A O    1 
ATOM   2172 H H    . GLY A 1 138 ? -8.89900  1.87100   26.90900  1.000 29.82046  ? 138 GLY A H    1 
ATOM   2173 H HA2  . GLY A 1 138 ? -8.13000  0.89500   24.51800  1.000 33.84955  ? 138 GLY A HA2  1 
ATOM   2174 H HA3  . GLY A 1 138 ? -9.61600  1.12500   24.98000  1.000 33.84955  ? 138 GLY A HA3  1 
ATOM   2175 N N    . SER A 1 139 ? -9.32700  2.73400   23.02200  1.000 24.69493  ? 139 SER A N    1 
ATOM   2176 C CA   . SER A 1 139 ? -9.57300  3.91700   22.20100  1.000 28.07982  ? 139 SER A CA   1 
ATOM   2177 C C    . SER A 1 139 ? -11.00000 3.75000   21.69700  1.000 25.64823  ? 139 SER A C    1 
ATOM   2178 O O    . SER A 1 139 ? -11.20200 3.02600   20.71000  1.000 23.17204  ? 139 SER A O    1 
ATOM   2179 C CB   . SER A 1 139 ? -8.59700  4.00900   21.02000  1.000 24.83851  ? 139 SER A CB   1 
ATOM   2180 O OG   . SER A 1 139 ? -8.92500  5.17600   20.27600  1.000 27.68421  ? 139 SER A OG   1 
ATOM   2181 H H    . SER A 1 139 ? -9.58200  1.99800   22.65700  1.000 29.63472  ? 139 SER A H    1 
ATOM   2182 H HA   . SER A 1 139 ? -9.51200  4.72400   22.73600  1.000 33.69658  ? 139 SER A HA   1 
ATOM   2183 H HB2  . SER A 1 139 ? -7.68900  4.08000   21.35300  1.000 29.80701  ? 139 SER A HB2  1 
ATOM   2184 H HB3  . SER A 1 139 ? -8.69300  3.22600   20.45600  1.000 29.80701  ? 139 SER A HB3  1 
ATOM   2185 H HG   . SER A 1 139 ? -8.40900  5.25100   19.61800  1.000 33.22185  ? 139 SER A HG   1 
ATOM   2186 N N    . PHE A 1 140 ? -11.95400 4.43100   22.35700  1.000 26.29876  ? 140 PHE A N    1 
ATOM   2187 C CA   . PHE A 1 140 ? -13.37300 4.17200   22.18100  1.000 24.25775  ? 140 PHE A CA   1 
ATOM   2188 C C    . PHE A 1 140 ? -14.13800 5.47200   22.29000  1.000 25.47246  ? 140 PHE A C    1 
ATOM   2189 O O    . PHE A 1 140 ? -13.88200 6.28500   23.18200  1.000 28.39650  ? 140 PHE A O    1 
ATOM   2190 C CB   . PHE A 1 140 ? -13.96000 3.22600   23.24700  1.000 23.91640  ? 140 PHE A CB   1 
ATOM   2191 C CG   . PHE A 1 140 ? -13.47300 1.78700   23.17100  1.000 23.06453  ? 140 PHE A CG   1 
ATOM   2192 C CD1  . PHE A 1 140 ? -13.76300 0.97300   22.07100  1.000 24.38397  ? 140 PHE A CD1  1 
ATOM   2193 C CD2  . PHE A 1 140 ? -12.85100 1.21600   24.29500  1.000 26.22709  ? 140 PHE A CD2  1 
ATOM   2194 C CE1  . PHE A 1 140 ? -13.38300 -0.37200  22.04100  1.000 23.14439  ? 140 PHE A CE1  1 
ATOM   2195 C CE2  . PHE A 1 140 ? -12.49500 -0.12600  24.29400  1.000 27.52784  ? 140 PHE A CE2  1 
ATOM   2196 C CZ   . PHE A 1 140 ? -12.77000 -0.93400  23.17100  1.000 23.32140  ? 140 PHE A CZ   1 
ATOM   2197 H H    . PHE A 1 140 ? -11.78900 5.05900   22.92100  1.000 31.55932  ? 140 PHE A H    1 
ATOM   2198 H HA   . PHE A 1 140 ? -13.53100 3.79000   21.30400  1.000 29.11010  ? 140 PHE A HA   1 
ATOM   2199 H HB2  . PHE A 1 140 ? -13.72200 3.56700   24.12300  1.000 28.70049  ? 140 PHE A HB2  1 
ATOM   2200 H HB3  . PHE A 1 140 ? -14.92400 3.21600   23.15600  1.000 28.70049  ? 140 PHE A HB3  1 
ATOM   2201 H HD1  . PHE A 1 140 ? -14.19300 1.34100   21.33300  1.000 29.26156  ? 140 PHE A HD1  1 
ATOM   2202 H HD2  . PHE A 1 140 ? -12.69200 1.73600   25.04900  1.000 31.47330  ? 140 PHE A HD2  1 
ATOM   2203 H HE1  . PHE A 1 140 ? -13.56700 -0.89700  21.29500  1.000 27.77407  ? 140 PHE A HE1  1 
ATOM   2204 H HE2  . PHE A 1 140 ? -12.06300 -0.49100  25.03200  1.000 33.03421  ? 140 PHE A HE2  1 
ATOM   2205 H HZ   . PHE A 1 140 ? -12.49200 -1.82100  23.15700  1.000 27.98648  ? 140 PHE A HZ   1 
ATOM   2206 N N    . LEU A 1 141 ? -15.13600 5.60100   21.43300  1.000 23.74865  ? 141 LEU A N    1 
ATOM   2207 C CA   . LEU A 1 141 ? -16.01800 6.74200   21.36200  1.000 26.33004  ? 141 LEU A CA   1 
ATOM   2208 C C    . LEU A 1 141 ? -17.45000 6.28100   21.60500  1.000 26.24743  ? 141 LEU A C    1 
ATOM   2209 O O    . LEU A 1 141 ? -17.75200 5.08100   21.64400  1.000 26.53177  ? 141 LEU A O    1 
ATOM   2210 C CB   . LEU A 1 141 ? -15.88800 7.40200   19.98200  1.000 27.24089  ? 141 LEU A CB   1 
ATOM   2211 C CG   . LEU A 1 141 ? -14.44500 7.74000   19.57000  1.000 32.12797  ? 141 LEU A CG   1 
ATOM   2212 C CD1  . LEU A 1 141 ? -14.35700 8.08300   18.02400  1.000 32.08144  ? 141 LEU A CD1  1 
ATOM   2213 C CD2  . LEU A 1 141 ? -13.91100 8.89500   20.44800  1.000 36.11802  ? 141 LEU A CD2  1 
ATOM   2214 H H    . LEU A 1 141 ? -15.32900 5.00000   20.84900  1.000 28.49918  ? 141 LEU A H    1 
ATOM   2215 H HA   . LEU A 1 141 ? -15.77800 7.38900   22.04300  1.000 31.59685  ? 141 LEU A HA   1 
ATOM   2216 H HB2  . LEU A 1 141 ? -16.25100 6.79900   19.31400  1.000 32.68987  ? 141 LEU A HB2  1 
ATOM   2217 H HB3  . LEU A 1 141 ? -16.39400 8.22900   19.98500  1.000 32.68987  ? 141 LEU A HB3  1 
ATOM   2218 H HG   . LEU A 1 141 ? -13.88200 6.96600   19.72800  1.000 38.55436  ? 141 LEU A HG   1 
ATOM   2219 H HD11 . LEU A 1 141 ? -13.43700 8.29100   17.79900  1.000 38.49853  ? 141 LEU A HD11 1 
ATOM   2220 H HD12 . LEU A 1 141 ? -14.65800 7.31500   17.51300  1.000 38.49853  ? 141 LEU A HD12 1 
ATOM   2221 H HD13 . LEU A 1 141 ? -14.92400 8.84800   17.83800  1.000 38.49853  ? 141 LEU A HD13 1 
ATOM   2222 H HD21 . LEU A 1 141 ? -13.01300 9.12200   20.15900  1.000 43.34243  ? 141 LEU A HD21 1 
ATOM   2223 H HD22 . LEU A 1 141 ? -14.49500 9.66300   20.34800  1.000 43.34243  ? 141 LEU A HD22 1 
ATOM   2224 H HD23 . LEU A 1 141 ? -13.89700 8.60700   21.37400  1.000 43.34243  ? 141 LEU A HD23 1 
ATOM   2225 N N    . ASN A 1 142 ? -18.35100 7.24500   21.72200  1.000 28.82567  ? 142 ASN A N    1 
ATOM   2226 C CA   . ASN A 1 142 ? -19.77000 6.91200   21.79700  1.000 29.97620  ? 142 ASN A CA   1 
ATOM   2227 C C    . ASN A 1 142 ? -20.16700 6.02500   20.62000  1.000 28.18588  ? 142 ASN A C    1 
ATOM   2228 O O    . ASN A 1 142 ? -19.81600 6.30000   19.46800  1.000 29.80755  ? 142 ASN A O    1 
ATOM   2229 C CB   . ASN A 1 142 ? -20.58900 8.19500   21.85900  1.000 32.00137  ? 142 ASN A CB   1 
ATOM   2230 C CG   . ASN A 1 142 ? -20.43700 8.91100   23.18300  1.000 45.44225  ? 142 ASN A CG   1 
ATOM   2231 O OD1  . ASN A 1 142 ? -20.13900 8.27300   24.18800  1.000 44.36351  ? 142 ASN A OD1  1 
ATOM   2232 N ND2  . ASN A 1 142 ? -20.69300 10.22600  23.21000  1.000 63.71053  ? 142 ASN A ND2  1 
ATOM   2233 H H    . ASN A 1 142 ? -18.17500 8.08600   21.76000  1.000 34.59160  ? 142 ASN A H    1 
ATOM   2234 H HA   . ASN A 1 142 ? -19.93300 6.41300   22.61200  1.000 35.97224  ? 142 ASN A HA   1 
ATOM   2235 H HB2  . ASN A 1 142 ? -20.29300 8.79500   21.15600  1.000 38.40245  ? 142 ASN A HB2  1 
ATOM   2236 H HB3  . ASN A 1 142 ? -21.52700 7.97900   21.73900  1.000 38.40245  ? 142 ASN A HB3  1 
ATOM   2237 H HD21 . ASN A 1 142 ? -20.62100 10.66300  23.94700  1.000 76.45344  ? 142 ASN A HD21 1 
ATOM   2238 H HD22 . ASN A 1 142 ? -20.90900 10.63700  22.48600  1.000 76.45344  ? 142 ASN A HD22 1 
ATOM   2239 N N    . GLY A 1 143 ? -20.89300 4.96000   20.91200  1.000 26.22860  ? 143 GLY A N    1 
ATOM   2240 C CA   . GLY A 1 143 ? -21.31600 4.00800   19.92300  1.000 26.72789  ? 143 GLY A CA   1 
ATOM   2241 C C    . GLY A 1 143 ? -20.42600 2.79700   19.79700  1.000 28.56541  ? 143 GLY A C    1 
ATOM   2242 O O    . GLY A 1 143 ? -20.73400 1.91700   18.98700  1.000 27.09717  ? 143 GLY A O    1 
ATOM   2243 H H    . GLY A 1 143 ? -21.15900 4.76700   21.70700  1.000 31.47512  ? 143 GLY A H    1 
ATOM   2244 H HA2  . GLY A 1 143 ? -22.20900 3.70100   20.14300  1.000 32.07427  ? 143 GLY A HA2  1 
ATOM   2245 H HA3  . GLY A 1 143 ? -21.35400 4.44400   19.05800  1.000 32.07427  ? 143 GLY A HA3  1 
ATOM   2246 N N    . SER A 1 144 ? -19.30300 2.76800   20.51800  1.000 25.31603  ? 144 SER A N    1 
ATOM   2247 C CA   . SER A 1 144 ? -18.35000 1.65800   20.43300  1.000 23.89663  ? 144 SER A CA   1 
ATOM   2248 C C    . SER A 1 144 ? -18.75500 0.51000   21.33500  1.000 23.49698  ? 144 SER A C    1 
ATOM   2249 O O    . SER A 1 144 ? -18.17100 -0.58300  21.23600  1.000 22.40056  ? 144 SER A O    1 
ATOM   2250 C CB   . SER A 1 144 ? -16.91400 2.12400   20.81600  1.000 21.98118  ? 144 SER A CB   1 
ATOM   2251 O OG   . SER A 1 144 ? -16.94500 2.60900   22.14200  1.000 25.18469  ? 144 SER A OG   1 
ATOM   2252 H H    . SER A 1 144 ? -19.06700 3.38500   21.06900  1.000 30.38004  ? 144 SER A H    1 
ATOM   2253 H HA   . SER A 1 144 ? -18.32700 1.33000   19.52100  1.000 28.67676  ? 144 SER A HA   1 
ATOM   2254 H HB2  . SER A 1 144 ? -16.30500 1.37100   20.76200  1.000 26.37822  ? 144 SER A HB2  1 
ATOM   2255 H HB3  . SER A 1 144 ? -16.62900 2.83300   20.22100  1.000 26.37822  ? 144 SER A HB3  1 
ATOM   2256 H HG   . SER A 1 144 ? -17.45700 3.27300   22.19400  1.000 30.22243  ? 144 SER A HG   1 
ATOM   2257 N N    . ALA A 1 145 ? -19.74400 0.71800   22.20800  1.000 23.25428  ? 145 ALA A N    1 
ATOM   2258 C CA   . ALA A 1 145 ? -20.11800 -0.38000  23.10200  1.000 22.02541  ? 145 ALA A CA   1 
ATOM   2259 C C    . ALA A 1 145 ? -20.49700 -1.59900  22.27100  1.000 23.50491  ? 145 ALA A C    1 
ATOM   2260 O O    . ALA A 1 145 ? -21.06100 -1.47300  21.16900  1.000 24.55787  ? 145 ALA A O    1 
ATOM   2261 C CB   . ALA A 1 145 ? -21.27800 0.03100   24.00800  1.000 24.02134  ? 145 ALA A CB   1 
ATOM   2262 H H    . ALA A 1 145 ? -20.19400 1.44500   22.30200  1.000 27.90594  ? 145 ALA A H    1 
ATOM   2263 H HA   . ALA A 1 145 ? -19.36000 -0.61300  23.66100  1.000 26.43129  ? 145 ALA A HA   1 
ATOM   2264 H HB1  . ALA A 1 145 ? -21.51500 -0.71900  24.57600  1.000 28.82641  ? 145 ALA A HB1  1 
ATOM   2265 H HB2  . ALA A 1 145 ? -21.00100 0.78500   24.55200  1.000 28.82641  ? 145 ALA A HB2  1 
ATOM   2266 H HB3  . ALA A 1 145 ? -22.03600 0.28000   23.45700  1.000 28.82641  ? 145 ALA A HB3  1 
ATOM   2267 N N    . GLY A 1 146 ? -20.13300 -2.77800  22.76300  1.000 23.88503  ? 146 GLY A N    1 
ATOM   2268 C CA   . GLY A 1 146 ? -20.36000 -4.00700  22.02800  1.000 23.80913  ? 146 GLY A CA   1 
ATOM   2269 C C    . GLY A 1 146 ? -19.18000 -4.41500  21.15800  1.000 26.08937  ? 146 GLY A C    1 
ATOM   2270 O O    . GLY A 1 146 ? -19.13600 -5.55400  20.69800  1.000 24.02592  ? 146 GLY A O    1 
ATOM   2271 H H    . GLY A 1 146 ? -19.75100 -2.89000  23.52500  1.000 28.66284  ? 146 GLY A H    1 
ATOM   2272 H HA2  . GLY A 1 146 ? -20.53900 -4.72600  22.65400  1.000 28.57176  ? 146 GLY A HA2  1 
ATOM   2273 H HA3  . GLY A 1 146 ? -21.13600 -3.90100  21.45700  1.000 28.57176  ? 146 GLY A HA3  1 
ATOM   2274 N N    . SER A 1 147 ? -18.21900 -3.53400  20.94600  1.000 19.96889  ? 147 SER A N    1 
ATOM   2275 C CA   . SER A 1 147 ? -16.94200 -3.96500  20.35100  1.000 22.07010  ? 147 SER A CA   1 
ATOM   2276 C C    . SER A 1 147 ? -16.31300 -5.02900  21.24100  1.000 21.36542  ? 147 SER A C    1 
ATOM   2277 O O    . SER A 1 147 ? -16.48500 -5.00900  22.46000  1.000 20.85566  ? 147 SER A O    1 
ATOM   2278 C CB   . SER A 1 147 ? -15.95400 -2.78600  20.23000  1.000 22.04996  ? 147 SER A CB   1 
ATOM   2279 O OG   . SER A 1 147 ? -16.42900 -1.78000  19.34500  1.000 24.18392  ? 147 SER A OG   1 
ATOM   2280 H H    . SER A 1 147 ? -18.26700 -2.69500  21.12900  1.000 23.96347  ? 147 SER A H    1 
ATOM   2281 H HA   . SER A 1 147 ? -17.09600 -4.34000  19.47000  1.000 26.48492  ? 147 SER A HA   1 
ATOM   2282 H HB2  . SER A 1 147 ? -15.82700 -2.39400  21.10800  1.000 26.46075  ? 147 SER A HB2  1 
ATOM   2283 H HB3  . SER A 1 147 ? -15.10800 -3.12100  19.89500  1.000 26.46075  ? 147 SER A HB3  1 
ATOM   2284 H HG   . SER A 1 147 ? -17.16100 -1.47600  19.62300  1.000 29.02151  ? 147 SER A HG   1 
ATOM   2285 N N    . VAL A 1 148 ? -15.52300 -5.93800  20.64900  1.000 22.31917  ? 148 VAL A N    1 
ATOM   2286 C CA   . VAL A 1 148 ? -14.98200 -7.04000  21.44600  1.000 20.16575  ? 148 VAL A CA   1 
ATOM   2287 C C    . VAL A 1 148 ? -13.46000 -7.06900  21.39400  1.000 23.47245  ? 148 VAL A C    1 
ATOM   2288 O O    . VAL A 1 148 ? -12.82400 -6.55000  20.45900  1.000 23.18835  ? 148 VAL A O    1 
ATOM   2289 C CB   . VAL A 1 148 ? -15.55800 -8.41800  21.02400  1.000 23.00737  ? 148 VAL A CB   1 
ATOM   2290 C CG1  . VAL A 1 148 ? -17.06600 -8.44200  21.34900  1.000 25.76143  ? 148 VAL A CG1  1 
ATOM   2291 C CG2  . VAL A 1 148 ? -15.35500 -8.74800  19.53600  1.000 24.95058  ? 148 VAL A CG2  1 
ATOM   2292 H H    . VAL A 1 148 ? -15.29500 -5.93800  19.82000  1.000 26.78381  ? 148 VAL A H    1 
ATOM   2293 H HA   . VAL A 1 148 ? -15.22900 -6.90300  22.37200  1.000 24.19971  ? 148 VAL A HA   1 
ATOM   2294 H HB   . VAL A 1 148 ? -15.12800 -9.11300  21.54600  1.000 27.60965  ? 148 VAL A HB   1 
ATOM   2295 H HG11 . VAL A 1 148 ? -17.43000 -9.30100  21.08700  1.000 30.91452  ? 148 VAL A HG11 1 
ATOM   2296 H HG12 . VAL A 1 148 ? -17.18500 -8.30800  22.30200  1.000 30.91452  ? 148 VAL A HG12 1 
ATOM   2297 H HG13 . VAL A 1 148 ? -17.50600 -7.73200  20.85700  1.000 30.91452  ? 148 VAL A HG13 1 
ATOM   2298 H HG21 . VAL A 1 148 ? -15.72500 -9.62600  19.35500  1.000 29.94150  ? 148 VAL A HG21 1 
ATOM   2299 H HG22 . VAL A 1 148 ? -15.81000 -8.08000  19.00000  1.000 29.94150  ? 148 VAL A HG22 1 
ATOM   2300 H HG23 . VAL A 1 148 ? -14.40600 -8.74200  19.33800  1.000 29.94150  ? 148 VAL A HG23 1 
ATOM   2301 N N    . GLY A 1 149 ? -12.88800 -7.71000  22.42600  1.000 22.58081  ? 149 GLY A N    1 
ATOM   2302 C CA   . GLY A 1 149 ? -11.48000 -8.03900  22.47700  1.000 22.90529  ? 149 GLY A CA   1 
ATOM   2303 C C    . GLY A 1 149 ? -11.32900 -9.54200  22.34500  1.000 23.11857  ? 149 GLY A C    1 
ATOM   2304 O O    . GLY A 1 149 ? -12.21300 -10.32000 22.76300  1.000 23.54613  ? 149 GLY A O    1 
ATOM   2305 H H    . GLY A 1 149 ? -13.32100 -7.96700  23.12300  1.000 27.09777  ? 149 GLY A H    1 
ATOM   2306 H HA2  . GLY A 1 149 ? -11.03300 -7.59800  21.74700  1.000 27.48715  ? 149 GLY A HA2  1 
ATOM   2307 H HA3  . GLY A 1 149 ? -11.09500 -7.74700  23.31800  1.000 27.48715  ? 149 GLY A HA3  1 
ATOM   2308 N N    . PHE A 1 150 ? -10.21700 -9.96300  21.74800  1.000 22.23565  ? 150 PHE A N    1 
ATOM   2309 C CA   . PHE A 1 150 ? -10.08100 -11.35600 21.39100  1.000 21.54869  ? 150 PHE A CA   1 
ATOM   2310 C C    . PHE A 1 150 ? -8.61600  -11.69900 21.14400  1.000 24.07087  ? 150 PHE A C    1 
ATOM   2311 O O    . PHE A 1 150 ? -7.78100  -10.82300 20.92200  1.000 22.47143  ? 150 PHE A O    1 
ATOM   2312 C CB   . PHE A 1 150 ? -10.87700 -11.65600 20.11200  1.000 25.16827  ? 150 PHE A CB   1 
ATOM   2313 C CG   . PHE A 1 150 ? -10.43100 -10.83600 18.95400  1.000 24.32799  ? 150 PHE A CG   1 
ATOM   2314 C CD1  . PHE A 1 150 ? -10.94900 -9.53400  18.77600  1.000 27.43177  ? 150 PHE A CD1  1 
ATOM   2315 C CD2  . PHE A 1 150 ? -9.52900  -11.33200 18.03000  1.000 24.57618  ? 150 PHE A CD2  1 
ATOM   2316 C CE1  . PHE A 1 150 ? -10.53100 -8.74700  17.66000  1.000 26.77785  ? 150 PHE A CE1  1 
ATOM   2317 C CE2  . PHE A 1 150 ? -9.06000  -10.52100 16.95600  1.000 24.76526  ? 150 PHE A CE2  1 
ATOM   2318 C CZ   . PHE A 1 150 ? -9.59500  -9.24700  16.76300  1.000 26.48930  ? 150 PHE A CZ   1 
ATOM   2319 H H    . PHE A 1 150 ? -9.54400  -9.46800  21.54500  1.000 26.68358  ? 150 PHE A H    1 
ATOM   2320 H HA   . PHE A 1 150 ? -10.41700 -11.91300 22.11000  1.000 25.85922  ? 150 PHE A HA   1 
ATOM   2321 H HB2  . PHE A 1 150 ? -10.76200 -12.59100 19.88000  1.000 30.20273  ? 150 PHE A HB2  1 
ATOM   2322 H HB3  . PHE A 1 150 ? -11.81500 -11.46600 20.27100  1.000 30.20273  ? 150 PHE A HB3  1 
ATOM   2323 H HD1  . PHE A 1 150 ? -11.57300 -9.19500  19.37600  1.000 32.91893  ? 150 PHE A HD1  1 
ATOM   2324 H HD2  . PHE A 1 150 ? -9.16400  -12.17800 18.15700  1.000 29.49222  ? 150 PHE A HD2  1 
ATOM   2325 H HE1  . PHE A 1 150 ? -10.86700 -7.88700  17.54800  1.000 32.13422  ? 150 PHE A HE1  1 
ATOM   2326 H HE2  . PHE A 1 150 ? -8.45800  -10.87000 16.33900  1.000 29.71911  ? 150 PHE A HE2  1 
ATOM   2327 H HZ   . PHE A 1 150 ? -9.31600  -8.72900  16.04300  1.000 31.78796  ? 150 PHE A HZ   1 
ATOM   2328 N N    . ASN A 1 151 ? -8.31400  -12.99700 21.24000  1.000 24.29647  ? 151 ASN A N    1 
ATOM   2329 C CA   . ASN A 1 151 ? -7.05300  -13.52400 20.73100  1.000 24.44600  ? 151 ASN A CA   1 
ATOM   2330 C C    . ASN A 1 151 ? -7.36400  -14.60000 19.70700  1.000 25.61516  ? 151 ASN A C    1 
ATOM   2331 O O    . ASN A 1 151 ? -8.45300  -15.16500 19.69100  1.000 26.12720  ? 151 ASN A O    1 
ATOM   2332 C CB   . ASN A 1 151 ? -6.16600  -14.10300 21.84800  1.000 25.01199  ? 151 ASN A CB   1 
ATOM   2333 C CG   . ASN A 1 151 ? -5.63200  -12.99400 22.73600  1.000 25.74823  ? 151 ASN A CG   1 
ATOM   2334 O OD1  . ASN A 1 151 ? -4.76700  -12.25500 22.31000  1.000 28.64545  ? 151 ASN A OD1  1 
ATOM   2335 N ND2  . ASN A 1 151 ? -6.18800  -12.83100 23.93100  1.000 25.67272  ? 151 ASN A ND2  1 
ATOM   2336 H H    . ASN A 1 151 ? -8.82500  -13.59000 21.59600  1.000 29.15657  ? 151 ASN A H    1 
ATOM   2337 H HA   . ASN A 1 151 ? -6.56100  -12.81500 20.28800  1.000 29.33600  ? 151 ASN A HA   1 
ATOM   2338 H HB2  . ASN A 1 151 ? -6.69000  -14.70900 22.39500  1.000 30.01519  ? 151 ASN A HB2  1 
ATOM   2339 H HB3  . ASN A 1 151 ? -5.41300  -14.56900 21.45300  1.000 30.01519  ? 151 ASN A HB3  1 
ATOM   2340 H HD21 . ASN A 1 151 ? -5.91000  -12.20700 24.45300  1.000 30.80806  ? 151 ASN A HD21 1 
ATOM   2341 H HD22 . ASN A 1 151 ? -6.80700  -13.36700 24.19400  1.000 30.80806  ? 151 ASN A HD22 1 
ATOM   2342 N N    . ILE A 1 152 ? -6.41600  -14.86000 18.80200  1.000 27.38710  ? 152 ILE A N    1 
ATOM   2343 C CA   . ILE A 1 152 ? -6.63500  -15.95100 17.86900  1.000 25.80659  ? 152 ILE A CA   1 
ATOM   2344 C C    . ILE A 1 152 ? -5.35000  -16.75200 17.81900  1.000 33.98611  ? 152 ILE A C    1 
ATOM   2345 O O    . ILE A 1 152 ? -4.65100  -16.76200 16.80000  1.000 35.70440  ? 152 ILE A O    1 
ATOM   2346 C CB   . ILE A 1 152 ? -7.00800  -15.46700 16.46000  1.000 26.58357  ? 152 ILE A CB   1 
ATOM   2347 C CG1  . ILE A 1 152 ? -8.06000  -14.35100 16.51500  1.000 27.01089  ? 152 ILE A CG1  1 
ATOM   2348 C CG2  . ILE A 1 152 ? -7.49900  -16.68000 15.60600  1.000 33.86889  ? 152 ILE A CG2  1 
ATOM   2349 C CD1  . ILE A 1 152 ? -8.54000  -13.86600 15.07300  1.000 27.85811  ? 152 ILE A CD1  1 
ATOM   2350 H H    . ILE A 1 152 ? -5.67200  -14.43700 18.71400  1.000 32.86532  ? 152 ILE A H    1 
ATOM   2351 H HA   . ILE A 1 152 ? -7.34100  -16.53100 18.19200  1.000 30.96871  ? 152 ILE A HA   1 
ATOM   2352 H HB   . ILE A 1 152 ? -6.21100  -15.10500 16.04200  1.000 31.90108  ? 152 ILE A HB   1 
ATOM   2353 H HG12 . ILE A 1 152 ? -8.83800  -14.67500 16.99500  1.000 32.41387  ? 152 ILE A HG12 1 
ATOM   2354 H HG13 . ILE A 1 152 ? -7.68400  -13.58400 16.97400  1.000 32.41387  ? 152 ILE A HG13 1 
ATOM   2355 H HG21 . ILE A 1 152 ? -7.61800  -16.39400 14.68700  1.000 40.64347  ? 152 ILE A HG21 1 
ATOM   2356 H HG22 . ILE A 1 152 ? -6.83600  -17.38600 15.64700  1.000 40.64347  ? 152 ILE A HG22 1 
ATOM   2357 H HG23 . ILE A 1 152 ? -8.34200  -16.99800 15.96600  1.000 40.64347  ? 152 ILE A HG23 1 
ATOM   2358 H HD11 . ILE A 1 152 ? -9.10500  -13.08400 15.17500  1.000 33.43053  ? 152 ILE A HD11 1 
ATOM   2359 H HD12 . ILE A 1 152 ? -7.76100  -13.64400 14.54000  1.000 33.43053  ? 152 ILE A HD12 1 
ATOM   2360 H HD13 . ILE A 1 152 ? -9.03900  -14.58100 14.64800  1.000 33.43053  ? 152 ILE A HD13 1 
ATOM   2361 N N    . ASP A 1 153 ? -5.07800  -17.46900 18.87400  1.000 33.06048  ? 153 ASP A N    1 
ATOM   2362 C CA   . ASP A 1 153 ? -3.94700  -18.36700 18.90000  1.000 47.34032  ? 153 ASP A CA   1 
ATOM   2363 C C    . ASP A 1 153 ? -4.44100  -19.60900 18.17700  1.000 51.04646  ? 153 ASP A C    1 
ATOM   2364 O O    . ASP A 1 153 ? -5.51500  -20.14100 18.48800  1.000 57.74515  ? 153 ASP A O    1 
ATOM   2365 C CB   . ASP A 1 153 ? -3.49900  -18.67800 20.33000  1.000 42.78813  ? 153 ASP A CB   1 
ATOM   2366 C CG   . ASP A 1 153 ? -3.12600  -17.41800 21.14800  1.000 42.77874  ? 153 ASP A CG   1 
ATOM   2367 O OD1  . ASP A 1 153 ? -2.34500  -16.55200 20.66700  1.000 36.27015  ? 153 ASP A OD1  1 
ATOM   2368 O OD2  . ASP A 1 153 ? -3.67000  -17.27800 22.28500  1.000 35.98413  ? 153 ASP A OD2  1 
ATOM   2369 H H    . ASP A 1 153 ? -5.53600  -17.45800 19.60200  1.000 39.67337  ? 153 ASP A H    1 
ATOM   2370 H HA   . ASP A 1 153 ? -3.20300  -17.98500 18.40800  1.000 56.80919  ? 153 ASP A HA   1 
ATOM   2371 H HB2  . ASP A 1 153 ? -4.21900  -19.13400 20.79400  1.000 51.34656  ? 153 ASP A HB2  1 
ATOM   2372 H HB3  . ASP A 1 153 ? -2.71600  -19.24800 20.29400  1.000 51.34656  ? 153 ASP A HB3  1 
ATOM   2373 N N    . TYR A 1 154 ? -3.72100  -19.98200 17.14100  1.000 56.27043  ? 154 TYR A N    1 
ATOM   2374 C CA   . TYR A 1 154 ? -4.02100  -21.14400 16.32100  1.000 58.61614  ? 154 TYR A CA   1 
ATOM   2375 C C    . TYR A 1 154 ? -5.26000  -20.91100 15.45300  1.000 55.52827  ? 154 TYR A C    1 
ATOM   2376 O O    . TYR A 1 154 ? -5.28900  -19.93200 14.70000  1.000 57.65845  ? 154 TYR A O    1 
ATOM   2377 C CB   . TYR A 1 154 ? -4.13700  -22.34400 17.27000  1.000 64.84681  ? 154 TYR A CB   1 
ATOM   2378 C CG   . TYR A 1 154 ? -2.97300  -22.30300 18.27300  1.000 63.95440  ? 154 TYR A CG   1 
ATOM   2379 C CD1  . TYR A 1 154 ? -1.65000  -22.50800 17.86400  1.000 70.71775  ? 154 TYR A CD1  1 
ATOM   2380 C CD2  . TYR A 1 154 ? -3.19700  -22.00100 19.61800  1.000 63.45668  ? 154 TYR A CD2  1 
ATOM   2381 C CE1  . TYR A 1 154 ? -0.58100  -22.42300 18.77700  1.000 72.19491  ? 154 TYR A CE1  1 
ATOM   2382 C CE2  . TYR A 1 154 ? -2.13400  -21.91400 20.54300  1.000 71.11200  ? 154 TYR A CE2  1 
ATOM   2383 C CZ   . TYR A 1 154 ? -0.82900  -22.13000 20.11600  1.000 75.39886  ? 154 TYR A CZ   1 
ATOM   2384 O OH   . TYR A 1 154 ? 0.21500   -22.05100 21.02400  1.000 71.29034  ? 154 TYR A OH   1 
ATOM   2385 H H    . TYR A 1 154 ? -3.02000  -19.55900 16.87800  1.000 67.52532  ? 154 TYR A H    1 
ATOM   2386 H HA   . TYR A 1 154 ? -3.27200  -21.30800 15.72700  1.000 70.34017  ? 154 TYR A HA   1 
ATOM   2387 H HB2  . TYR A 1 154 ? -4.97400  -22.30700 17.75800  1.000 77.81697  ? 154 TYR A HB2  1 
ATOM   2388 H HB3  . TYR A 1 154 ? -4.07600  -23.16700 16.76100  1.000 77.81697  ? 154 TYR A HB3  1 
ATOM   2389 H HD1  . TYR A 1 154 ? -1.47300  -22.69700 16.97100  1.000 84.86210  ? 154 TYR A HD1  1 
ATOM   2390 H HD2  . TYR A 1 154 ? -4.06700  -21.84800 19.91000  1.000 76.14882  ? 154 TYR A HD2  1 
ATOM   2391 H HE1  . TYR A 1 154 ? 0.29000   -22.57100 18.48700  1.000 86.63470  ? 154 TYR A HE1  1 
ATOM   2392 H HE2  . TYR A 1 154 ? -2.30700  -21.71900 21.43600  1.000 85.33520  ? 154 TYR A HE2  1 
ATOM   2393 H HH   . TYR A 1 154 ? -0.08200  -21.86800 21.78800  1.000 85.54921  ? 154 TYR A HH   1 
ATOM   2394 N N    . ASP A 1 155 ? -6.30500  -21.71500 15.55600  1.000 59.30469  ? 155 ASP A N    1 
ATOM   2395 C CA   . ASP A 1 155 ? -7.40200  -21.51500 14.58300  1.000 62.59175  ? 155 ASP A CA   1 
ATOM   2396 C C    . ASP A 1 155 ? -8.66700  -20.98200 15.22900  1.000 59.12534  ? 155 ASP A C    1 
ATOM   2397 O O    . ASP A 1 155 ? -9.75200  -20.88600 14.64300  1.000 57.94618  ? 155 ASP A O    1 
ATOM   2398 C CB   . ASP A 1 155 ? -7.71700  -22.82100 13.85600  1.000 71.83623  ? 155 ASP A CB   1 
ATOM   2399 C CG   . ASP A 1 155 ? -8.72700  -22.63000 12.73600  1.000 81.43583  ? 155 ASP A CG   1 
ATOM   2400 O OD1  . ASP A 1 155 ? -8.41300  -21.88600 11.77000  1.000 80.46862  ? 155 ASP A OD1  1 
ATOM   2401 O OD2  . ASP A 1 155 ? -9.82900  -23.22100 12.83000  1.000 78.61502  ? 155 ASP A OD2  1 
ATOM   2402 H H    . ASP A 1 155 ? -6.41600  -22.34500 16.13100  1.000 71.16643  ? 155 ASP A H    1 
ATOM   2403 H HA   . ASP A 1 155 ? -7.13100  -20.87500 13.90800  1.000 75.11090  ? 155 ASP A HA   1 
ATOM   2404 H HB2  . ASP A 1 155 ? -6.90100  -23.17300 13.46900  1.000 86.20428  ? 155 ASP A HB2  1 
ATOM   2405 H HB3  . ASP A 1 155 ? -8.08600  -23.45600 14.49000  1.000 86.20428  ? 155 ASP A HB3  1 
HETATM 2406 N N    . OCS A 1 156 ? -8.52200  -20.79500 16.53600  1.000 50.74801  ? 156 OCS A N    1 
HETATM 2407 C CA   . OCS A 1 156 ? -9.70100  -20.54100 17.37300  1.000 39.57558  ? 156 OCS A CA   1 
HETATM 2408 C CB   . OCS A 1 156 ? -9.60200  -21.51800 18.53600  1.000 47.95113  ? 156 OCS A CB   1 
HETATM 2409 S SG   . OCS A 1 156 ? -10.73400 -21.57700 19.86800  1.000 48.25099  ? 156 OCS A SG   1 
HETATM 2410 C C    . OCS A 1 156 ? -9.72800  -19.10900 17.88100  1.000 34.76284  ? 156 OCS A C    1 
HETATM 2411 O O    . OCS A 1 156 ? -8.74100  -18.66200 18.46200  1.000 32.30294  ? 156 OCS A O    1 
HETATM 2412 O OD1  . OCS A 1 156 ? -10.34700 -22.70800 20.65700  1.000 56.07520  ? 156 OCS A OD1  1 
HETATM 2413 O OD2  . OCS A 1 156 ? -12.05200 -21.87900 19.17900  1.000 49.22789  ? 156 OCS A OD2  1 
HETATM 2414 O OD3  . OCS A 1 156 ? -10.74200 -20.27400 20.45900  1.000 49.82603  ? 156 OCS A OD3  1 
HETATM 2415 H HA   . OCS A 1 156 ? -10.52400 -20.72100 16.87300  1.000 47.49150  ? 156 OCS A HA   1 
HETATM 2416 H HB2  . OCS A 1 156 ? -8.73200  -21.37600 18.94100  1.000 57.54216  ? 156 OCS A HB2  1 
HETATM 2417 H HB3  . OCS A 1 156 ? -9.61100  -22.40700 18.14900  1.000 57.54216  ? 156 OCS A HB3  1 
HETATM 2418 H HD2  . OCS A 1 156 ? -12.69600 -22.06100 19.87700  1.000 59.07426  ? 156 OCS A HD2  1 
ATOM   2419 N N    . VAL A 1 157 ? -10.87400 -18.48200 17.69700  1.000 31.02290  ? 157 VAL A N    1 
ATOM   2420 C CA   . VAL A 1 157 ? -11.04000 -17.10900 18.19700  1.000 26.81215  ? 157 VAL A CA   1 
ATOM   2421 C C    . VAL A 1 157 ? -11.50200 -17.18900 19.66500  1.000 29.26739  ? 157 VAL A C    1 
ATOM   2422 O O    . VAL A 1 157 ? -12.58900 -17.75900 19.95600  1.000 29.24638  ? 157 VAL A O    1 
ATOM   2423 C CB   . VAL A 1 157 ? -12.06200 -16.28200 17.39000  1.000 27.16753  ? 157 VAL A CB   1 
ATOM   2424 C CG1  . VAL A 1 157 ? -12.21600 -14.89300 17.98800  1.000 24.58337  ? 157 VAL A CG1  1 
ATOM   2425 C CG2  . VAL A 1 157 ? -11.69100 -16.23000 15.89100  1.000 30.14701  ? 157 VAL A CG2  1 
ATOM   2426 H H    . VAL A 1 157 ? -11.56200 -18.80900 17.29800  1.000 37.22828  ? 157 VAL A H    1 
ATOM   2427 H HA   . VAL A 1 157 ? -10.18600 -16.65000 18.16900  1.000 32.17538  ? 157 VAL A HA   1 
ATOM   2428 H HB   . VAL A 1 157 ? -12.92500 -16.72000 17.45600  1.000 32.60184  ? 157 VAL A HB   1 
ATOM   2429 H HG11 . VAL A 1 157 ? -12.66800 -14.32400 17.34600  1.000 29.50085  ? 157 VAL A HG11 1 
ATOM   2430 H HG12 . VAL A 1 157 ? -12.74100 -14.95200 18.80200  1.000 29.50085  ? 157 VAL A HG12 1 
ATOM   2431 H HG13 . VAL A 1 157 ? -11.33600 -14.53500 18.18400  1.000 29.50085  ? 157 VAL A HG13 1 
ATOM   2432 H HG21 . VAL A 1 157 ? -12.34900 -15.69300 15.42200  1.000 36.17721  ? 157 VAL A HG21 1 
ATOM   2433 H HG22 . VAL A 1 157 ? -10.81100 -15.83200 15.79800  1.000 36.17721  ? 157 VAL A HG22 1 
ATOM   2434 H HG23 . VAL A 1 157 ? -11.68600 -17.13300 15.53600  1.000 36.17721  ? 157 VAL A HG23 1 
ATOM   2435 N N    . SER A 1 158 ? -10.69000 -16.66500 20.58800  1.000 26.77971  ? 158 SER A N    1 
ATOM   2436 C CA   . SER A 1 158 ? -11.06500 -16.63700 22.00100  1.000 26.38611  ? 158 SER A CA   1 
ATOM   2437 C C    . SER A 1 158 ? -11.54500 -15.22400 22.32800  1.000 24.32958  ? 158 SER A C    1 
ATOM   2438 O O    . SER A 1 158 ? -10.75100 -14.28200 22.36200  1.000 26.44722  ? 158 SER A O    1 
ATOM   2439 C CB   . SER A 1 158 ? -9.92200  -17.10000 22.90700  1.000 28.67252  ? 158 SER A CB   1 
ATOM   2440 O OG   . SER A 1 158 ? -8.73000  -16.38400 22.62400  1.000 35.32014  ? 158 SER A OG   1 
ATOM   2441 H H    . SER A 1 158 ? -9.92000  -16.32100 20.42100  1.000 32.13646  ? 158 SER A H    1 
ATOM   2442 H HA   . SER A 1 158 ? -11.81100 -17.24100 22.14200  1.000 31.66414  ? 158 SER A HA   1 
ATOM   2443 H HB2  . SER A 1 158 ? -10.17000 -16.94600 23.83200  1.000 34.40783  ? 158 SER A HB2  1 
ATOM   2444 H HB3  . SER A 1 158 ? -9.76500  -18.04600 22.75800  1.000 34.40783  ? 158 SER A HB3  1 
ATOM   2445 H HG   . SER A 1 158 ? -8.85200  -15.56200 22.74800  1.000 42.38497  ? 158 SER A HG   1 
ATOM   2446 N N    . PHE A 1 159 ? -12.85700 -15.07100 22.54000  1.000 26.06308  ? 159 PHE A N    1 
ATOM   2447 C CA   . PHE A 1 159 ? -13.40500 -13.76900 22.89800  1.000 25.12530  ? 159 PHE A CA   1 
ATOM   2448 C C    . PHE A 1 159 ? -13.25100 -13.56700 24.39200  1.000 24.85688  ? 159 PHE A C    1 
ATOM   2449 O O    . PHE A 1 159 ? -13.69400 -14.40400 25.19300  1.000 27.63999  ? 159 PHE A O    1 
ATOM   2450 C CB   . PHE A 1 159 ? -14.90300 -13.67900 22.50000  1.000 25.44748  ? 159 PHE A CB   1 
ATOM   2451 C CG   . PHE A 1 159 ? -15.15000 -13.68200 21.00000  1.000 24.52729  ? 159 PHE A CG   1 
ATOM   2452 C CD1  . PHE A 1 159 ? -14.93500 -12.53200 20.25800  1.000 25.87686  ? 159 PHE A CD1  1 
ATOM   2453 C CD2  . PHE A 1 159 ? -15.60700 -14.81700 20.33900  1.000 27.84116  ? 159 PHE A CD2  1 
ATOM   2454 C CE1  . PHE A 1 159 ? -15.12700 -12.52100 18.84900  1.000 24.12465  ? 159 PHE A CE1  1 
ATOM   2455 C CE2  . PHE A 1 159 ? -15.83200 -14.80400 18.96400  1.000 28.28166  ? 159 PHE A CE2  1 
ATOM   2456 C CZ   . PHE A 1 159 ? -15.62400 -13.65100 18.22800  1.000 27.22456  ? 159 PHE A CZ   1 
ATOM   2457 H H    . PHE A 1 159 ? -13.44000 -15.70000 22.48300  1.000 31.27650  ? 159 PHE A H    1 
ATOM   2458 H HA   . PHE A 1 159 ? -12.91800 -13.06900 22.43600  1.000 30.15116  ? 159 PHE A HA   1 
ATOM   2459 H HB2  . PHE A 1 159 ? -15.37200 -14.44000 22.87800  1.000 30.53777  ? 159 PHE A HB2  1 
ATOM   2460 H HB3  . PHE A 1 159 ? -15.27100 -12.85600 22.85800  1.000 30.53777  ? 159 PHE A HB3  1 
ATOM   2461 H HD1  . PHE A 1 159 ? -14.61700 -11.76800 20.68200  1.000 31.05303  ? 159 PHE A HD1  1 
ATOM   2462 H HD2  . PHE A 1 159 ? -15.76900 -15.59500 20.82300  1.000 33.41020  ? 159 PHE A HD2  1 
ATOM   2463 H HE1  . PHE A 1 159 ? -14.99100 -11.74000 18.36300  1.000 28.95039  ? 159 PHE A HE1  1 
ATOM   2464 H HE2  . PHE A 1 159 ? -16.14200 -15.57200 18.54000  1.000 33.93879  ? 159 PHE A HE2  1 
ATOM   2465 H HZ   . PHE A 1 159 ? -15.75700 -13.65600 17.30800  1.000 32.67028  ? 159 PHE A HZ   1 
ATOM   2466 N N    . CYS A 1 160 ? -12.66400 -12.44100 24.79500  1.000 24.27510  ? 160 CYS A N    1 
ATOM   2467 C CA   . CYS A 1 160 ? -12.41600 -12.22300 26.22000  1.000 23.34433  ? 160 CYS A CA   1 
ATOM   2468 C C    . CYS A 1 160 ? -12.95400 -10.91000 26.74300  1.000 22.34416  ? 160 CYS A C    1 
ATOM   2469 O O    . CYS A 1 160 ? -12.92500 -10.70800 27.96700  1.000 24.77542  ? 160 CYS A O    1 
ATOM   2470 C CB   . CYS A 1 160 ? -10.92400 -12.26700 26.56300  1.000 25.57977  ? 160 CYS A CB   1 
ATOM   2471 S SG   . CYS A 1 160 ? -9.94700  -11.13700 25.59100  1.000 28.28259  ? 160 CYS A SG   1 
ATOM   2472 H H    . CYS A 1 160 ? -12.40600 -11.80300 24.27900  1.000 29.13092  ? 160 CYS A H    1 
ATOM   2473 H HA   . CYS A 1 160 ? -12.84800 -12.92700 26.72500  1.000 28.01400  ? 160 CYS A HA   1 
ATOM   2474 H HB2  . CYS A 1 160 ? -10.81000 -12.03100 27.49700  1.000 30.69653  ? 160 CYS A HB2  1 
ATOM   2475 H HB3  . CYS A 1 160 ? -10.59000 -13.16400 26.40500  1.000 30.69653  ? 160 CYS A HB3  1 
ATOM   2476 H HG   . CYS A 1 160 ? -10.33600 -10.01800 25.78400  1.000 33.93990  ? 160 CYS A HG   1 
ATOM   2477 N N    . TYR A 1 161 ? -13.43800 -10.01600 25.87800  1.000 22.34898  ? 161 TYR A N    1 
ATOM   2478 C CA   . TYR A 1 161 ? -13.87100 -8.70400  26.34500  1.000 21.88752  ? 161 TYR A CA   1 
ATOM   2479 C C    . TYR A 1 161 ? -15.00600 -8.19700  25.46300  1.000 22.37653  ? 161 TYR A C    1 
ATOM   2480 O O    . TYR A 1 161 ? -14.98200 -8.36300  24.23900  1.000 21.83591  ? 161 TYR A O    1 
ATOM   2481 C CB   . TYR A 1 161 ? -12.69400 -7.71800  26.30500  1.000 22.13680  ? 161 TYR A CB   1 
ATOM   2482 C CG   . TYR A 1 161 ? -13.06900 -6.33200  26.75000  1.000 20.62531  ? 161 TYR A CG   1 
ATOM   2483 C CD1  . TYR A 1 161 ? -13.16400 -6.01100  28.12900  1.000 21.81651  ? 161 TYR A CD1  1 
ATOM   2484 C CD2  . TYR A 1 161 ? -13.30400 -5.32600  25.80300  1.000 20.20020  ? 161 TYR A CD2  1 
ATOM   2485 C CE1  . TYR A 1 161 ? -13.48700 -4.71900  28.52500  1.000 22.69947  ? 161 TYR A CE1  1 
ATOM   2486 C CE2  . TYR A 1 161 ? -13.62800 -4.00200  26.19000  1.000 20.61897  ? 161 TYR A CE2  1 
ATOM   2487 C CZ   . TYR A 1 161 ? -13.74300 -3.71700  27.54000  1.000 22.11975  ? 161 TYR A CZ   1 
ATOM   2488 O OH   . TYR A 1 161 ? -14.03800 -2.44100  27.93400  1.000 22.84994  ? 161 TYR A OH   1 
ATOM   2489 H H    . TYR A 1 161 ? -13.52400 -10.14300 25.03200  1.000 26.81957  ? 161 TYR A H    1 
ATOM   2490 H HA   . TYR A 1 161 ? -14.19100 -8.76900  27.25800  1.000 26.26582  ? 161 TYR A HA   1 
ATOM   2491 H HB2  . TYR A 1 161 ? -11.99300 -8.04100  26.89200  1.000 26.56496  ? 161 TYR A HB2  1 
ATOM   2492 H HB3  . TYR A 1 161 ? -12.36300 -7.66000  25.39500  1.000 26.56496  ? 161 TYR A HB3  1 
ATOM   2493 H HD1  . TYR A 1 161 ? -13.00700 -6.66700  28.77000  1.000 26.18062  ? 161 TYR A HD1  1 
ATOM   2494 H HD2  . TYR A 1 161 ? -13.23400 -5.53000  24.89800  1.000 24.24104  ? 161 TYR A HD2  1 
ATOM   2495 H HE1  . TYR A 1 161 ? -13.55500 -4.51200  29.42900  1.000 27.24017  ? 161 TYR A HE1  1 
ATOM   2496 H HE2  . TYR A 1 161 ? -13.78800 -3.34600  25.55100  1.000 24.74357  ? 161 TYR A HE2  1 
ATOM   2497 H HH   . TYR A 1 161 ? -13.81400 -1.89900  27.33400  1.000 27.42073  ? 161 TYR A HH   1 
ATOM   2498 N N    . MET A 1 162 ? -16.01500 -7.59200  26.09100  1.000 21.12583  ? 162 MET A N    1 
ATOM   2499 C CA   . MET A 1 162 ? -17.01300 -6.82700  25.35600  1.000 21.14505  ? 162 MET A CA   1 
ATOM   2500 C C    . MET A 1 162 ? -17.09200 -5.46000  26.00100  1.000 19.39819  ? 162 MET A C    1 
ATOM   2501 O O    . MET A 1 162 ? -17.19300 -5.34100  27.22400  1.000 21.39629  ? 162 MET A O    1 
ATOM   2502 C CB   . MET A 1 162 ? -18.39900 -7.51800  25.32600  1.000 23.25437  ? 162 MET A CB   1 
ATOM   2503 C CG   . MET A 1 162 ? -19.47400 -6.64500  24.65100  1.000 24.63897  ? 162 MET A CG   1 
ATOM   2504 S SD   . MET A 1 162 ? -20.98800 -7.59800  24.25600  1.000 30.08359  ? 162 MET A SD   1 
ATOM   2505 C CE   . MET A 1 162 ? -20.55000 -8.20200  22.59000  1.000 29.09390  ? 162 MET A CE   1 
ATOM   2506 H H    . MET A 1 162 ? -16.14100 -7.61100  26.94100  1.000 25.35179  ? 162 MET A H    1 
ATOM   2507 H HA   . MET A 1 162 ? -16.71700 -6.72100  24.43900  1.000 25.37487  ? 162 MET A HA   1 
ATOM   2508 H HB2  . MET A 1 162 ? -18.32900 -8.34800  24.82900  1.000 27.90604  ? 162 MET A HB2  1 
ATOM   2509 H HB3  . MET A 1 162 ? -18.68400 -7.69700  26.23600  1.000 27.90604  ? 162 MET A HB3  1 
ATOM   2510 H HG2  . MET A 1 162 ? -19.72100 -5.92300  25.25000  1.000 29.56757  ? 162 MET A HG2  1 
ATOM   2511 H HG3  . MET A 1 162 ? -19.11800 -6.28600  23.82300  1.000 29.56757  ? 162 MET A HG3  1 
ATOM   2512 H HE1  . MET A 1 162 ? -21.28100 -8.74100  22.24800  1.000 34.91348  ? 162 MET A HE1  1 
ATOM   2513 H HE2  . MET A 1 162 ? -20.39900 -7.44100  22.00800  1.000 34.91348  ? 162 MET A HE2  1 
ATOM   2514 H HE3  . MET A 1 162 ? -19.74400 -8.73800  22.65100  1.000 34.91348  ? 162 MET A HE3  1 
ATOM   2515 N N    . HIS A 1 163 ? -16.98100 -4.42700  25.17400  1.000 22.47864  ? 163 HIS A N    1 
ATOM   2516 C CA   . HIS A 1 163 ? -16.87300 -3.08100  25.66900  1.000 23.86898  ? 163 HIS A CA   1 
ATOM   2517 C C    . HIS A 1 163 ? -18.24000 -2.53100  26.11100  1.000 22.55503  ? 163 HIS A C    1 
ATOM   2518 O O    . HIS A 1 163 ? -19.25900 -2.73200  25.43400  1.000 22.22840  ? 163 HIS A O    1 
ATOM   2519 C CB   . HIS A 1 163 ? -16.24700 -2.17300  24.58900  1.000 21.36658  ? 163 HIS A CB   1 
ATOM   2520 C CG   . HIS A 1 163 ? -16.06100 -0.78800  25.09500  1.000 23.49560  ? 163 HIS A CG   1 
ATOM   2521 N ND1  . HIS A 1 163 ? -15.41900 -0.55200  26.29500  1.000 22.02800  ? 163 HIS A ND1  1 
ATOM   2522 C CD2  . HIS A 1 163 ? -16.53700 0.41400   24.66900  1.000 23.39396  ? 163 HIS A CD2  1 
ATOM   2523 C CE1  . HIS A 1 163 ? -15.44800 0.75100   26.54900  1.000 23.11329  ? 163 HIS A CE1  1 
ATOM   2524 N NE2  . HIS A 1 163 ? -16.14200 1.35300   25.60200  1.000 23.65581  ? 163 HIS A NE2  1 
ATOM   2525 H H    . HIS A 1 163 ? -16.96700 -4.48900  24.31600  1.000 26.97516  ? 163 HIS A H    1 
ATOM   2526 H HA   . HIS A 1 163 ? -16.28700 -3.07600  26.44100  1.000 28.64358  ? 163 HIS A HA   1 
ATOM   2527 H HB2  . HIS A 1 163 ? -15.37900 -2.52500  24.33700  1.000 25.64070  ? 163 HIS A HB2  1 
ATOM   2528 H HB3  . HIS A 1 163 ? -16.83400 -2.14000  23.81800  1.000 25.64070  ? 163 HIS A HB3  1 
ATOM   2529 H HD2  . HIS A 1 163 ? -17.03400 0.57200   23.89900  1.000 28.07355  ? 163 HIS A HD2  1 
ATOM   2530 H HE1  . HIS A 1 163 ? -15.07000 1.16800   27.28800  1.000 27.73675  ? 163 HIS A HE1  1 
ATOM   2531 H HE2  . HIS A 1 163 ? -16.28200 2.20000   25.54700  1.000 28.38778  ? 163 HIS A HE2  1 
ATOM   2532 N N    . HIS A 1 164 ? -18.26400 -1.84300  27.27000  1.000 20.70739  ? 164 HIS A N    1 
ATOM   2533 C CA   . HIS A 1 164 ? -19.48100 -1.18200  27.72300  1.000 23.87195  ? 164 HIS A CA   1 
ATOM   2534 C C    . HIS A 1 164 ? -19.29900 0.30900   27.95600  1.000 24.69648  ? 164 HIS A C    1 
ATOM   2535 O O    . HIS A 1 164 ? -20.14700 1.10000   27.52400  1.000 25.22050  ? 164 HIS A O    1 
ATOM   2536 C CB   . HIS A 1 164 ? -20.00100 -1.80300  29.04600  1.000 24.65102  ? 164 HIS A CB   1 
ATOM   2537 C CG   . HIS A 1 164 ? -20.51100 -3.19100  28.90000  1.000 25.37576  ? 164 HIS A CG   1 
ATOM   2538 N ND1  . HIS A 1 164 ? -21.79500 -3.56400  29.24100  1.000 24.72944  ? 164 HIS A ND1  1 
ATOM   2539 C CD2  . HIS A 1 164 ? -19.89800 -4.30600  28.46200  1.000 24.49892  ? 164 HIS A CD2  1 
ATOM   2540 C CE1  . HIS A 1 164 ? -21.94000 -4.85500  29.03600  1.000 24.16394  ? 164 HIS A CE1  1 
ATOM   2541 N NE2  . HIS A 1 164 ? -20.80100 -5.32700  28.55700  1.000 24.70800  ? 164 HIS A NE2  1 
ATOM   2542 H H    . HIS A 1 164 ? -17.59200 -1.75100  27.79900  1.000 24.84966  ? 164 HIS A H    1 
ATOM   2543 H HA   . HIS A 1 164 ? -20.17300 -1.29300  27.05200  1.000 28.64714  ? 164 HIS A HA   1 
ATOM   2544 H HB2  . HIS A 1 164 ? -19.27500 -1.82000  29.68900  1.000 29.58203  ? 164 HIS A HB2  1 
ATOM   2545 H HB3  . HIS A 1 164 ? -20.72600 -1.25500  29.38400  1.000 29.58203  ? 164 HIS A HB3  1 
ATOM   2546 H HD2  . HIS A 1 164 ? -19.01900 -4.37200  28.16500  1.000 29.39951  ? 164 HIS A HD2  1 
ATOM   2547 H HE1  . HIS A 1 164 ? -22.71600 -5.34600  29.18000  1.000 28.99753  ? 164 HIS A HE1  1 
ATOM   2548 H HE2  . HIS A 1 164 ? -20.65500 -6.14400  28.33100  1.000 29.65041  ? 164 HIS A HE2  1 
ATOM   2549 N N    . MET A 1 165 ? -18.32600 0.66600   28.78900  1.000 24.79948  ? 165 MET A N    1 
ATOM   2550 C CA   . MET A 1 165 ? -18.31100 2.07700   29.22100  1.000 28.38659  ? 165 MET A CA   1 
ATOM   2551 C C    . MET A 1 165 ? -16.95000 2.74200   29.37100  1.000 24.27185  ? 165 MET A C    1 
ATOM   2552 O O    . MET A 1 165 ? -15.93500 2.05300   29.40500  1.000 22.15360  ? 165 MET A O    1 
ATOM   2553 C CB   . MET A 1 165 ? -19.00300 2.16900   30.58000  1.000 33.26003  ? 165 MET A CB   1 
ATOM   2554 C CG   . MET A 1 165 ? -18.43400 1.26700   31.63000  1.000 28.99780  ? 165 MET A CG   1 
ATOM   2555 S SD   . MET A 1 165 ? -19.73800 0.92500   32.80900  1.000 43.67661  ? 165 MET A SD   1 
ATOM   2556 C CE   . MET A 1 165 ? -21.16800 1.20700   31.76900  1.000 34.23692  ? 165 MET A CE   1 
ATOM   2557 H H    . MET A 1 165 ? -17.70400 0.16100   29.10200  1.000 29.76018  ? 165 MET A H    1 
ATOM   2558 H HA   . MET A 1 165 ? -18.82900 2.60500   28.59500  1.000 34.06471  ? 165 MET A HA   1 
ATOM   2559 H HB2  . MET A 1 165 ? -18.96300 3.08300   30.90300  1.000 39.91284  ? 165 MET A HB2  1 
ATOM   2560 H HB3  . MET A 1 165 ? -19.86900 1.96900   30.26500  1.000 39.91284  ? 165 MET A HB3  1 
ATOM   2561 H HG2  . MET A 1 165 ? -18.13900 0.43000   31.23900  1.000 34.79816  ? 165 MET A HG2  1 
ATOM   2562 H HG3  . MET A 1 165 ? -17.70400 1.71200   32.08900  1.000 34.79816  ? 165 MET A HG3  1 
ATOM   2563 H HE1  . MET A 1 165 ? -21.94300 0.91200   32.26400  1.000 41.08510  ? 165 MET A HE1  1 
ATOM   2564 H HE2  . MET A 1 165 ? -21.24600 2.15800   31.63100  1.000 41.08510  ? 165 MET A HE2  1 
ATOM   2565 H HE3  . MET A 1 165 ? -21.12100 0.69000   30.94900  1.000 41.08510  ? 165 MET A HE3  1 
ATOM   2566 N N    . GLU A 1 166 ? -17.00000 4.06900   29.48300  1.000 26.85091  ? 166 GLU A N    1 
ATOM   2567 C CA   . GLU A 1 166 ? -15.77900 4.82700   29.69400  1.000 28.18129  ? 166 GLU A CA   1 
ATOM   2568 C C    . GLU A 1 166 ? -15.85400 5.46700   31.08300  1.000 29.91513  ? 166 GLU A C    1 
ATOM   2569 O O    . GLU A 1 166 ? -16.87300 6.06700   31.44200  1.000 27.55136  ? 166 GLU A O    1 
ATOM   2570 C CB   . GLU A 1 166 ? -15.59000 5.87700   28.59500  1.000 28.04701  ? 166 GLU A CB   1 
ATOM   2571 C CG   . GLU A 1 166 ? -14.26800 6.63700   28.81700  1.000 30.42019  ? 166 GLU A CG   1 
ATOM   2572 C CD   . GLU A 1 166 ? -13.87600 7.51700   27.63300  1.000 33.98906  ? 166 GLU A CD   1 
ATOM   2573 O OE1  . GLU A 1 166 ? -13.66600 6.98800   26.49800  1.000 30.61176  ? 166 GLU A OE1  1 
ATOM   2574 O OE2  . GLU A 1 166 ? -13.83200 8.75300   27.84200  1.000 35.17800  ? 166 GLU A OE2  1 
ATOM   2575 H H    . GLU A 1 166 ? -17.71700 4.54300   29.44100  1.000 32.22190  ? 166 GLU A H    1 
ATOM   2576 H HA   . GLU A 1 166 ? -15.01600 4.22900   29.67600  1.000 33.81835  ? 166 GLU A HA   1 
ATOM   2577 H HB2  . GLU A 1 166 ? -15.55300 5.43900   27.73000  1.000 33.65721  ? 166 GLU A HB2  1 
ATOM   2578 H HB3  . GLU A 1 166 ? -16.32100 6.51400   28.62400  1.000 33.65721  ? 166 GLU A HB3  1 
ATOM   2579 H HG2  . GLU A 1 166 ? -14.35900 7.20900   29.59500  1.000 36.50503  ? 166 GLU A HG2  1 
ATOM   2580 H HG3  . GLU A 1 166 ? -13.55600 5.99500   28.96100  1.000 36.50503  ? 166 GLU A HG3  1 
ATOM   2581 N N    . LEU A 1 167 ? -14.78900 5.32500   31.86400  1.000 24.84127  ? 167 LEU A N    1 
ATOM   2582 C CA   . LEU A 1 167 ? -14.74200 5.90300   33.19500  1.000 28.12970  ? 167 LEU A CA   1 
ATOM   2583 C C    . LEU A 1 167 ? -14.22500 7.32000   33.11600  1.000 31.38310  ? 167 LEU A C    1 
ATOM   2584 O O    . LEU A 1 167 ? -13.70400 7.75100   32.08900  1.000 30.03434  ? 167 LEU A O    1 
ATOM   2585 C CB   . LEU A 1 167 ? -13.83900 5.06500   34.10000  1.000 28.88927  ? 167 LEU A CB   1 
ATOM   2586 C CG   . LEU A 1 167 ? -14.30100 3.63000   34.22400  1.000 27.61296  ? 167 LEU A CG   1 
ATOM   2587 C CD1  . LEU A 1 167 ? -13.24700 2.85900   34.95400  1.000 33.80877  ? 167 LEU A CD1  1 
ATOM   2588 C CD2  . LEU A 1 167 ? -15.62500 3.56300   34.95800  1.000 35.44432  ? 167 LEU A CD2  1 
ATOM   2589 H H    . LEU A 1 167 ? -14.07800 4.89500   31.64200  1.000 29.81033  ? 167 LEU A H    1 
ATOM   2590 H HA   . LEU A 1 167 ? -15.63600 5.91700   33.56900  1.000 33.75644  ? 167 LEU A HA   1 
ATOM   2591 H HB2  . LEU A 1 167 ? -12.94300 5.05800   33.72800  1.000 34.66793  ? 167 LEU A HB2  1 
ATOM   2592 H HB3  . LEU A 1 167 ? -13.82100 5.44500   34.99000  1.000 34.66793  ? 167 LEU A HB3  1 
ATOM   2593 H HG   . LEU A 1 167 ? -14.41400 3.24300   33.34200  1.000 33.13636  ? 167 LEU A HG   1 
ATOM   2594 H HD11 . LEU A 1 167 ? -13.54000 1.94000   35.05300  1.000 40.57133  ? 167 LEU A HD11 1 
ATOM   2595 H HD12 . LEU A 1 167 ? -12.42300 2.89000   34.44400  1.000 40.57133  ? 167 LEU A HD12 1 
ATOM   2596 H HD13 . LEU A 1 167 ? -13.11200 3.25900   35.82700  1.000 40.57133  ? 167 LEU A HD13 1 
ATOM   2597 H HD21 . LEU A 1 167 ? -15.82200 2.63700   35.16800  1.000 42.53399  ? 167 LEU A HD21 1 
ATOM   2598 H HD22 . LEU A 1 167 ? -15.55900 4.08100   35.77600  1.000 42.53399  ? 167 LEU A HD22 1 
ATOM   2599 H HD23 . LEU A 1 167 ? -16.32100 3.92800   34.39000  1.000 42.53399  ? 167 LEU A HD23 1 
ATOM   2600 N N    . PRO A 1 168 ? -14.32400 8.07500   34.21200  1.000 32.63809  ? 168 PRO A N    1 
ATOM   2601 C CA   . PRO A 1 168 ? -13.97700 9.50500   34.14000  1.000 35.99486  ? 168 PRO A CA   1 
ATOM   2602 C C    . PRO A 1 168 ? -12.51100 9.77200   33.84500  1.000 35.53375  ? 168 PRO A C    1 
ATOM   2603 O O    . PRO A 1 168 ? -12.20600 10.87100  33.36600  1.000 35.50136  ? 168 PRO A O    1 
ATOM   2604 C CB   . PRO A 1 168 ? -14.37500 10.04100  35.52700  1.000 37.92440  ? 168 PRO A CB   1 
ATOM   2605 C CG   . PRO A 1 168 ? -15.38500 9.05800   36.03700  1.000 45.56833  ? 168 PRO A CG   1 
ATOM   2606 C CD   . PRO A 1 168 ? -14.95500 7.71600   35.49700  1.000 36.24020  ? 168 PRO A CD   1 
ATOM   2607 H HA   . PRO A 1 168 ? -14.51900 9.94300   33.46500  1.000 43.19463  ? 168 PRO A HA   1 
ATOM   2608 H HB2  . PRO A 1 168 ? -13.59600 10.06600  36.10500  1.000 45.51008  ? 168 PRO A HB2  1 
ATOM   2609 H HB3  . PRO A 1 168 ? -14.76800 10.92300  35.43800  1.000 45.51008  ? 168 PRO A HB3  1 
ATOM   2610 H HG2  . PRO A 1 168 ? -15.37500 9.05500   37.00700  1.000 54.68280  ? 168 PRO A HG2  1 
ATOM   2611 H HG3  . PRO A 1 168 ? -16.26500 9.29400   35.70500  1.000 54.68280  ? 168 PRO A HG3  1 
ATOM   2612 H HD2  . PRO A 1 168 ? -14.30800 7.30600   36.09200  1.000 43.48904  ? 168 PRO A HD2  1 
ATOM   2613 H HD3  . PRO A 1 168 ? -15.72800 7.14800   35.36000  1.000 43.48904  ? 168 PRO A HD3  1 
ATOM   2614 N N    . THR A 1 169 ? -11.58700 8.83900   34.13400  1.000 31.64179  ? 169 THR A N    1 
ATOM   2615 C CA   . THR A 1 169 ? -10.20100 9.06300   33.74300  1.000 33.70807  ? 169 THR A CA   1 
ATOM   2616 C C    . THR A 1 169 ? -9.94000  8.76800   32.28400  1.000 35.87415  ? 169 THR A C    1 
ATOM   2617 O O    . THR A 1 169 ? -8.79600  8.89100   31.83900  1.000 33.95890  ? 169 THR A O    1 
ATOM   2618 C CB   . THR A 1 169 ? -9.25000  8.21600   34.59500  1.000 35.29322  ? 169 THR A CB   1 
ATOM   2619 O OG1  . THR A 1 169 ? -9.72700  6.86400   34.65900  1.000 32.18479  ? 169 THR A OG1  1 
ATOM   2620 C CG2  . THR A 1 169 ? -9.17500  8.78800   36.00700  1.000 42.30635  ? 169 THR A CG2  1 
ATOM   2621 H H    . THR A 1 169 ? -11.73800 8.09700   34.54100  1.000 37.97095  ? 169 THR A H    1 
ATOM   2622 H HA   . THR A 1 169 ? -9.98200  9.99500   33.89800  1.000 40.45049  ? 169 THR A HA   1 
ATOM   2623 H HB   . THR A 1 169 ? -8.36100  8.23100   34.20700  1.000 42.35266  ? 169 THR A HB   1 
ATOM   2624 H HG1  . THR A 1 169 ? -10.43100 6.82800   35.11500  1.000 38.62255  ? 169 THR A HG1  1 
ATOM   2625 H HG21 . THR A 1 169 ? -8.57500  8.25300   36.55000  1.000 50.76842  ? 169 THR A HG21 1 
ATOM   2626 H HG22 . THR A 1 169 ? -8.84500  9.70000   35.97800  1.000 50.76842  ? 169 THR A HG22 1 
ATOM   2627 H HG23 . THR A 1 169 ? -10.05600 8.78400   36.41300  1.000 50.76842  ? 169 THR A HG23 1 
ATOM   2628 N N    . GLY A 1 170 ? -10.95500 8.37300   31.52800  1.000 29.70504  ? 170 GLY A N    1 
ATOM   2629 C CA   . GLY A 1 170 ? -10.76100 8.10200   30.11900  1.000 27.33255  ? 170 GLY A CA   1 
ATOM   2630 C C    . GLY A 1 170 ? -10.35000 6.68200   29.79900  1.000 27.57053  ? 170 GLY A C    1 
ATOM   2631 O O    . GLY A 1 170 ? -10.02800 6.41200   28.64000  1.000 32.62900  ? 170 GLY A O    1 
ATOM   2632 H H    . GLY A 1 170 ? -11.76000 8.25500   31.80600  1.000 35.64685  ? 170 GLY A H    1 
ATOM   2633 H HA2  . GLY A 1 170 ? -11.58800 8.28700   29.64700  1.000 32.79986  ? 170 GLY A HA2  1 
ATOM   2634 H HA3  . GLY A 1 170 ? -10.07800 8.69700   29.77200  1.000 32.79986  ? 170 GLY A HA3  1 
ATOM   2635 N N    . VAL A 1 171 ? -10.30400 5.77600   30.79200  1.000 25.52473  ? 171 VAL A N    1 
ATOM   2636 C CA   . VAL A 1 171 ? -10.06700 4.35600   30.53700  1.000 26.62912  ? 171 VAL A CA   1 
ATOM   2637 C C    . VAL A 1 171 ? -11.41500 3.65100   30.51000  1.000 26.74645  ? 171 VAL A C    1 
ATOM   2638 O O    . VAL A 1 171 ? -12.45800 4.25800   30.79700  1.000 24.74897  ? 171 VAL A O    1 
ATOM   2639 C CB   . VAL A 1 171 ? -9.15400  3.71900   31.61400  1.000 27.29088  ? 171 VAL A CB   1 
ATOM   2640 C CG1  . VAL A 1 171 ? -7.79700  4.41400   31.66300  1.000 31.46805  ? 171 VAL A CG1  1 
ATOM   2641 C CG2  . VAL A 1 171 ? -9.81400  3.80200   32.98600  1.000 26.85929  ? 171 VAL A CG2  1 
ATOM   2642 H H    . VAL A 1 171 ? -10.41000 5.96900   31.62300  1.000 30.63048  ? 171 VAL A H    1 
ATOM   2643 H HA   . VAL A 1 171 ? -9.64400  4.24600   29.67100  1.000 31.95574  ? 171 VAL A HA   1 
ATOM   2644 H HB   . VAL A 1 171 ? -9.01000  2.78400   31.40100  1.000 32.74986  ? 171 VAL A HB   1 
ATOM   2645 H HG11 . VAL A 1 171 ? -7.24300  3.97700   32.32800  1.000 37.76246  ? 171 VAL A HG11 1 
ATOM   2646 H HG12 . VAL A 1 171 ? -7.37900  4.35100   30.79000  1.000 37.76246  ? 171 VAL A HG12 1 
ATOM   2647 H HG13 . VAL A 1 171 ? -7.92800  5.34500   31.90100  1.000 37.76246  ? 171 VAL A HG13 1 
ATOM   2648 H HG21 . VAL A 1 171 ? -9.18100  3.49900   33.65500  1.000 32.23195  ? 171 VAL A HG21 1 
ATOM   2649 H HG22 . VAL A 1 171 ? -10.06600 4.72000   33.16700  1.000 32.23195  ? 171 VAL A HG22 1 
ATOM   2650 H HG23 . VAL A 1 171 ? -10.60000 3.23400   32.99900  1.000 32.23195  ? 171 VAL A HG23 1 
ATOM   2651 N N    . HIS A 1 172 ? -11.39800 2.34900   30.23800  1.000 24.20090  ? 172 HIS A N    1 
ATOM   2652 C CA   . HIS A 1 172 ? -12.60500 1.65400   29.82500  1.000 25.29796  ? 172 HIS A CA   1 
ATOM   2653 C C    . HIS A 1 172 ? -12.88900 0.44900   30.70200  1.000 27.47997  ? 172 HIS A C    1 
ATOM   2654 O O    . HIS A 1 172 ? -11.96800 -0.15800  31.26400  1.000 25.28768  ? 172 HIS A O    1 
ATOM   2655 C CB   . HIS A 1 172 ? -12.44800 1.26100   28.34300  1.000 25.55362  ? 172 HIS A CB   1 
ATOM   2656 C CG   . HIS A 1 172 ? -12.26900 2.47700   27.49500  1.000 26.07354  ? 172 HIS A CG   1 
ATOM   2657 N ND1  . HIS A 1 172 ? -11.04300 2.86800   26.98700  1.000 23.56790  ? 172 HIS A ND1  1 
ATOM   2658 C CD2  . HIS A 1 172 ? -13.14600 3.46100   27.18900  1.000 24.91027  ? 172 HIS A CD2  1 
ATOM   2659 C CE1  . HIS A 1 172 ? -11.19700 4.01900   26.34500  1.000 25.90212  ? 172 HIS A CE1  1 
ATOM   2660 N NE2  . HIS A 1 172 ? -12.45800 4.41300   26.47500  1.000 26.65296  ? 172 HIS A NE2  1 
ATOM   2661 H H    . HIS A 1 172 ? -10.70000 1.84900   30.28600  1.000 29.04188  ? 172 HIS A H    1 
ATOM   2662 H HA   . HIS A 1 172 ? -13.36200 2.25700   29.89400  1.000 30.35836  ? 172 HIS A HA   1 
ATOM   2663 H HB2  . HIS A 1 172 ? -11.66200 0.70200   28.24200  1.000 30.66515  ? 172 HIS A HB2  1 
ATOM   2664 H HB3  . HIS A 1 172 ? -13.23700 0.78500   28.04900  1.000 30.66515  ? 172 HIS A HB3  1 
ATOM   2665 H HD2  . HIS A 1 172 ? -14.04600 3.48900   27.42000  1.000 29.89312  ? 172 HIS A HD2  1 
ATOM   2666 H HE1  . HIS A 1 172 ? -10.52700 4.48400   25.89700  1.000 31.08335  ? 172 HIS A HE1  1 
ATOM   2667 H HE2  . HIS A 1 172 ? -12.79900 5.12300   26.13000  1.000 31.98435  ? 172 HIS A HE2  1 
ATOM   2668 N N    . ALA A 1 173 ? -14.19100 0.09200   30.77000  1.000 23.76510  ? 173 ALA A N    1 
ATOM   2669 C CA   . ALA A 1 173 ? -14.62300 -1.05600  31.54500  1.000 23.70596  ? 173 ALA A CA   1 
ATOM   2670 C C    . ALA A 1 173 ? -15.60300 -1.88200  30.72300  1.000 24.36278  ? 173 ALA A C    1 
ATOM   2671 O O    . ALA A 1 173 ? -16.42600 -1.33000  29.97900  1.000 23.43339  ? 173 ALA A O    1 
ATOM   2672 C CB   . ALA A 1 173 ? -15.25000 -0.59200  32.86800  1.000 24.86892  ? 173 ALA A CB   1 
ATOM   2673 H H    . ALA A 1 173 ? -14.83000 0.50700   30.37200  1.000 28.51892  ? 173 ALA A H    1 
ATOM   2674 H HA   . ALA A 1 173 ? -13.85600 -1.61200  31.75100  1.000 28.44795  ? 173 ALA A HA   1 
ATOM   2675 H HB1  . ALA A 1 173 ? -15.53300 -1.37000  33.37300  1.000 29.84350  ? 173 ALA A HB1  1 
ATOM   2676 H HB2  . ALA A 1 173 ? -14.58900 -0.09200  33.37200  1.000 29.84350  ? 173 ALA A HB2  1 
ATOM   2677 H HB3  . ALA A 1 173 ? -16.01400 -0.02700  32.67400  1.000 29.84350  ? 173 ALA A HB3  1 
ATOM   2678 N N    . GLY A 1 174 ? -15.55600 -3.20100  30.87900  1.000 21.21232  ? 174 GLY A N    1 
ATOM   2679 C CA   . GLY A 1 174 ? -16.49800 -4.02000  30.14000  1.000 22.23618  ? 174 GLY A CA   1 
ATOM   2680 C C    . GLY A 1 174 ? -16.53100 -5.38800  30.75500  1.000 21.50730  ? 174 GLY A C    1 
ATOM   2681 O O    . GLY A 1 174 ? -16.06200 -5.58800  31.86900  1.000 21.88132  ? 174 GLY A O    1 
ATOM   2682 H H    . GLY A 1 174 ? -15.01000 -3.62900  31.38700  1.000 25.45559  ? 174 GLY A H    1 
ATOM   2683 H HA2  . GLY A 1 174 ? -17.38500 -3.63100  30.18100  1.000 26.68421  ? 174 GLY A HA2  1 
ATOM   2684 H HA3  . GLY A 1 174 ? -16.22300 -4.09300  29.21300  1.000 26.68421  ? 174 GLY A HA3  1 
ATOM   2685 N N    . THR A 1 175 ? -17.05600 -6.35100  30.01200  1.000 22.19125  ? 175 THR A N    1 
ATOM   2686 C CA   . THR A 1 175 ? -17.36700 -7.65400  30.57400  1.000 23.81621  ? 175 THR A CA   1 
ATOM   2687 C C    . THR A 1 175 ? -16.63800 -8.73700  29.79900  1.000 23.54917  ? 175 THR A C    1 
ATOM   2688 O O    . THR A 1 175 ? -16.14300 -8.53100  28.68600  1.000 21.87161  ? 175 THR A O    1 
ATOM   2689 C CB   . THR A 1 175 ? -18.88800 -7.94400  30.52500  1.000 24.82434  ? 175 THR A CB   1 
ATOM   2690 O OG1  . THR A 1 175 ? -19.32500 -7.99600  29.15000  1.000 23.61227  ? 175 THR A OG1  1 
ATOM   2691 C CG2  . THR A 1 175 ? -19.65800 -6.84600  31.30000  1.000 22.10186  ? 175 THR A CG2  1 
ATOM   2692 H H    . THR A 1 175 ? -17.24200 -6.27400  29.17600  1.000 26.63030  ? 175 THR A H    1 
ATOM   2693 H HA   . THR A 1 175 ? -17.07700 -7.69300  31.49800  1.000 28.58025  ? 175 THR A HA   1 
ATOM   2694 H HB   . THR A 1 175 ? -19.06500 -8.79800  30.95000  1.000 29.79001  ? 175 THR A HB   1 
ATOM   2695 H HG1  . THR A 1 175 ? -18.98300 -8.65800  28.76300  1.000 28.33553  ? 175 THR A HG1  1 
ATOM   2696 H HG21 . THR A 1 175 ? -20.61300 -6.96800  31.18100  1.000 26.52304  ? 175 THR A HG21 1 
ATOM   2697 H HG22 . THR A 1 175 ? -19.45100 -6.89800  32.24500  1.000 26.52304  ? 175 THR A HG22 1 
ATOM   2698 H HG23 . THR A 1 175 ? -19.41100 -5.96800  30.97000  1.000 26.52304  ? 175 THR A HG23 1 
ATOM   2699 N N    . ASP A 1 176 ? -16.65900 -9.94100  30.37100  1.000 25.06091  ? 176 ASP A N    1 
ATOM   2700 C CA   . ASP A 1 176 ? -16.43100 -11.09800 29.52300  1.000 24.99313  ? 176 ASP A CA   1 
ATOM   2701 C C    . ASP A 1 176 ? -17.69800 -11.38000 28.69300  1.000 26.95033  ? 176 ASP A C    1 
ATOM   2702 O O    . ASP A 1 176 ? -18.70400 -10.64000 28.73200  1.000 25.57402  ? 176 ASP A O    1 
ATOM   2703 C CB   . ASP A 1 176 ? -15.98200 -12.30000 30.36700  1.000 26.34435  ? 176 ASP A CB   1 
ATOM   2704 C CG   . ASP A 1 176 ? -17.06700 -12.78200 31.38900  1.000 27.17148  ? 176 ASP A CG   1 
ATOM   2705 O OD1  . ASP A 1 176 ? -18.28100 -12.59700 31.18500  1.000 27.02986  ? 176 ASP A OD1  1 
ATOM   2706 O OD2  . ASP A 1 176 ? -16.68700 -13.37400 32.39400  1.000 30.14186  ? 176 ASP A OD2  1 
ATOM   2707 H H    . ASP A 1 176 ? -16.79600 -10.10600 31.20400  1.000 30.07390  ? 176 ASP A H    1 
ATOM   2708 H HA   . ASP A 1 176 ? -15.71400 -10.89400 28.90300  1.000 29.99256  ? 176 ASP A HA   1 
ATOM   2709 H HB2  . ASP A 1 176 ? -15.77900 -13.04200 29.77800  1.000 31.61402  ? 176 ASP A HB2  1 
ATOM   2710 H HB3  . ASP A 1 176 ? -15.19000 -12.05200 30.86900  1.000 31.61402  ? 176 ASP A HB3  1 
ATOM   2711 N N    . LEU A 1 177 ? -17.64900 -12.43400 27.89500  1.000 24.91764  ? 177 LEU A N    1 
ATOM   2712 C CA   . LEU A 1 177 ? -18.75200 -12.70200 26.99100  1.000 25.76814  ? 177 LEU A CA   1 
ATOM   2713 C C    . LEU A 1 177 ? -19.87400 -13.45900 27.67700  1.000 25.00824  ? 177 LEU A C    1 
ATOM   2714 O O    . LEU A 1 177 ? -20.90500 -13.72700 27.05000  1.000 29.28919  ? 177 LEU A O    1 
ATOM   2715 C CB   . LEU A 1 177 ? -18.25400 -13.42100 25.74100  1.000 26.36289  ? 177 LEU A CB   1 
ATOM   2716 C CG   . LEU A 1 177 ? -17.88500 -12.50300 24.55300  1.000 27.37932  ? 177 LEU A CG   1 
ATOM   2717 C CD1  . LEU A 1 177 ? -19.13500 -11.81600 23.94900  1.000 30.93100  ? 177 LEU A CD1  1 
ATOM   2718 C CD2  . LEU A 1 177 ? -16.86700 -11.44600 24.96500  1.000 26.72879  ? 177 LEU A CD2  1 
ATOM   2719 H H    . LEU A 1 177 ? -17.00200 -12.99900 27.85800  1.000 29.90197  ? 177 LEU A H    1 
ATOM   2720 H HA   . LEU A 1 177 ? -19.11900 -11.85200 26.70300  1.000 30.92257  ? 177 LEU A HA   1 
ATOM   2721 H HB2  . LEU A 1 177 ? -17.46200 -13.93000 25.97300  1.000 31.63626  ? 177 LEU A HB2  1 
ATOM   2722 H HB3  . LEU A 1 177 ? -18.94900 -14.02500 25.43700  1.000 31.63626  ? 177 LEU A HB3  1 
ATOM   2723 H HG   . LEU A 1 177 ? -17.48200 -13.04400 23.85700  1.000 32.85599  ? 177 LEU A HG   1 
ATOM   2724 H HD11 . LEU A 1 177 ? -18.87600 -11.34600 23.14100  1.000 37.11800  ? 177 LEU A HD11 1 
ATOM   2725 H HD12 . LEU A 1 177 ? -19.79700 -12.49400 23.74000  1.000 37.11800  ? 177 LEU A HD12 1 
ATOM   2726 H HD13 . LEU A 1 177 ? -19.49600 -11.18900 24.59500  1.000 37.11800  ? 177 LEU A HD13 1 
ATOM   2727 H HD21 . LEU A 1 177 ? -16.58600 -10.95600 24.17700  1.000 32.07535  ? 177 LEU A HD21 1 
ATOM   2728 H HD22 . LEU A 1 177 ? -17.27800 -10.84100 25.60200  1.000 32.07535  ? 177 LEU A HD22 1 
ATOM   2729 H HD23 . LEU A 1 177 ? -16.10300 -11.88500 25.37000  1.000 32.07535  ? 177 LEU A HD23 1 
ATOM   2730 N N    . GLU A 1 178 ? -19.71400 -13.76800 28.95800  1.000 27.49689  ? 178 GLU A N    1 
ATOM   2731 C CA   . GLU A 1 178 ? -20.83000 -14.21200 29.78300  1.000 31.82996  ? 178 GLU A CA   1 
ATOM   2732 C C    . GLU A 1 178 ? -21.45700 -13.06000 30.52700  1.000 27.63682  ? 178 GLU A C    1 
ATOM   2733 O O    . GLU A 1 178 ? -22.32000 -13.28700 31.38000  1.000 29.69573  ? 178 GLU A O    1 
ATOM   2734 C CB   . GLU A 1 178 ? -20.37400 -15.29400 30.77100  1.000 31.39251  ? 178 GLU A CB   1 
ATOM   2735 C CG   . GLU A 1 178 ? -19.79500 -16.53600 30.07600  1.000 41.74350  ? 178 GLU A CG   1 
ATOM   2736 C CD   . GLU A 1 178 ? -19.48700 -17.71700 31.00800  1.000 48.21207  ? 178 GLU A CD   1 
ATOM   2737 O OE1  . GLU A 1 178 ? -19.20000 -17.53300 32.21500  1.000 48.68831  ? 178 GLU A OE1  1 
ATOM   2738 O OE2  . GLU A 1 178 ? -19.60300 -18.86500 30.52900  1.000 58.09825  ? 178 GLU A OE2  1 
ATOM   2739 H H    . GLU A 1 178 ? -18.96400 -13.73100 29.37800  1.000 32.99707  ? 178 GLU A H    1 
ATOM   2740 H HA   . GLU A 1 178 ? -21.51000 -14.60200 29.21200  1.000 38.19675  ? 178 GLU A HA   1 
ATOM   2741 H HB2  . GLU A 1 178 ? -19.68600 -14.92500 31.34700  1.000 37.67182  ? 178 GLU A HB2  1 
ATOM   2742 H HB3  . GLU A 1 178 ? -21.13500 -15.57600 31.30300  1.000 37.67182  ? 178 GLU A HB3  1 
ATOM   2743 H HG2  . GLU A 1 178 ? -20.43300 -16.84500 29.41400  1.000 50.09300  ? 178 GLU A HG2  1 
ATOM   2744 H HG3  . GLU A 1 178 ? -18.96700 -16.28600 29.63700  1.000 50.09300  ? 178 GLU A HG3  1 
ATOM   2745 N N    . GLY A 1 179 ? -21.01800 -11.84000 30.26000  1.000 26.27302  ? 179 GLY A N    1 
ATOM   2746 C CA   . GLY A 1 179 ? -21.66400 -10.68800 30.85400  1.000 26.91769  ? 179 GLY A CA   1 
ATOM   2747 C C    . GLY A 1 179 ? -21.17000 -10.28200 32.22600  1.000 27.56353  ? 179 GLY A C    1 
ATOM   2748 O O    . GLY A 1 179 ? -21.76800 -9.39100  32.83100  1.000 27.05862  ? 179 GLY A O    1 
ATOM   2749 H H    . GLY A 1 179 ? -20.35600 -11.65200 29.74500  1.000 31.52843  ? 179 GLY A H    1 
ATOM   2750 H HA2  . GLY A 1 179 ? -21.54700 -9.92800  30.26300  1.000 32.30202  ? 179 GLY A HA2  1 
ATOM   2751 H HA3  . GLY A 1 179 ? -22.61500 -10.86600 30.92400  1.000 32.30202  ? 179 GLY A HA3  1 
ATOM   2752 N N    . ASN A 1 180 ? -20.12800 -10.92000 32.73800  1.000 25.49027  ? 180 ASN A N    1 
ATOM   2753 C CA   . ASN A 1 180 ? -19.56800 -10.51600 34.05400  1.000 24.07919  ? 180 ASN A CA   1 
ATOM   2754 C C    . ASN A 1 180 ? -18.53100 -9.39800  33.88000  1.000 23.36597  ? 180 ASN A C    1 
ATOM   2755 O O    . ASN A 1 180 ? -17.55600 -9.61900  33.15700  1.000 24.44037  ? 180 ASN A O    1 
ATOM   2756 C CB   . ASN A 1 180 ? -18.95400 -11.69300 34.79000  1.000 27.63336  ? 180 ASN A CB   1 
ATOM   2757 C CG   . ASN A 1 180 ? -19.89500 -12.86600 34.91000  1.000 32.38638  ? 180 ASN A CG   1 
ATOM   2758 O OD1  . ASN A 1 180 ? -19.70200 -13.89000 34.25100  1.000 39.92037  ? 180 ASN A OD1  1 
ATOM   2759 N ND2  . ASN A 1 180 ? -20.90500 -12.74400 35.75400  1.000 27.78829  ? 180 ASN A ND2  1 
ATOM   2760 H H    . ASN A 1 180 ? -19.72200 -11.58000 32.36400  1.000 30.58913  ? 180 ASN A H    1 
ATOM   2761 H HA   . ASN A 1 180 ? -20.28600 -10.16800 34.60500  1.000 28.89583  ? 180 ASN A HA   1 
ATOM   2762 H HB2  . ASN A 1 180 ? -18.16600 -11.99000 34.30900  1.000 33.16083  ? 180 ASN A HB2  1 
ATOM   2763 H HB3  . ASN A 1 180 ? -18.71000 -11.41200 35.68600  1.000 33.16083  ? 180 ASN A HB3  1 
ATOM   2764 H HD21 . ASN A 1 180 ? -21.46300 -13.39000 35.85300  1.000 33.34675  ? 180 ASN A HD21 1 
ATOM   2765 H HD22 . ASN A 1 180 ? -21.00600 -12.01600 36.19900  1.000 33.34675  ? 180 ASN A HD22 1 
ATOM   2766 N N    . PHE A 1 181 ? -18.72800 -8.26100  34.55200  1.000 23.33911  ? 181 PHE A N    1 
ATOM   2767 C CA   . PHE A 1 181 ? -17.73200 -7.19500  34.44900  1.000 23.72979  ? 181 PHE A CA   1 
ATOM   2768 C C    . PHE A 1 181 ? -16.38700 -7.69000  34.94400  1.000 25.48710  ? 181 PHE A C    1 
ATOM   2769 O O    . PHE A 1 181 ? -16.29300 -8.50700  35.86400  1.000 23.83027  ? 181 PHE A O    1 
ATOM   2770 C CB   . PHE A 1 181 ? -18.09900 -5.94000  35.26300  1.000 26.68408  ? 181 PHE A CB   1 
ATOM   2771 C CG   . PHE A 1 181 ? -18.81300 -4.89500  34.43500  1.000 24.73033  ? 181 PHE A CG   1 
ATOM   2772 C CD1  . PHE A 1 181 ? -18.10700 -3.95100  33.70900  1.000 23.90053  ? 181 PHE A CD1  1 
ATOM   2773 C CD2  . PHE A 1 181 ? -20.19300 -4.93200  34.33400  1.000 26.86533  ? 181 PHE A CD2  1 
ATOM   2774 C CE1  . PHE A 1 181 ? -18.77600 -3.03400  32.91300  1.000 25.05688  ? 181 PHE A CE1  1 
ATOM   2775 C CE2  . PHE A 1 181 ? -20.88600 -4.03400  33.51300  1.000 27.61649  ? 181 PHE A CE2  1 
ATOM   2776 C CZ   . PHE A 1 181 ? -20.18300 -3.06800  32.82600  1.000 23.99100  ? 181 PHE A CZ   1 
ATOM   2777 H H    . PHE A 1 181 ? -19.40300 -8.08700  35.05500  1.000 28.00774  ? 181 PHE A H    1 
ATOM   2778 H HA   . PHE A 1 181 ? -17.63400 -6.93400  33.52100  1.000 28.47655  ? 181 PHE A HA   1 
ATOM   2779 H HB2  . PHE A 1 181 ? -18.68500 -6.19600  35.99300  1.000 32.02170  ? 181 PHE A HB2  1 
ATOM   2780 H HB3  . PHE A 1 181 ? -17.28700 -5.54200  35.61300  1.000 32.02170  ? 181 PHE A HB3  1 
ATOM   2781 H HD1  . PHE A 1 181 ? -17.17900 -3.92500  33.76400  1.000 28.68144  ? 181 PHE A HD1  1 
ATOM   2782 H HD2  . PHE A 1 181 ? -20.66700 -5.58500  34.79700  1.000 32.23920  ? 181 PHE A HD2  1 
ATOM   2783 H HE1  . PHE A 1 181 ? -18.29700 -2.39100  32.44200  1.000 30.06906  ? 181 PHE A HE1  1 
ATOM   2784 H HE2  . PHE A 1 181 ? -21.81500 -4.05600  33.47300  1.000 33.14058  ? 181 PHE A HE2  1 
ATOM   2785 H HZ   . PHE A 1 181 ? -20.63300 -2.45200  32.29400  1.000 28.79000  ? 181 PHE A HZ   1 
ATOM   2786 N N    . TYR A 1 182 ? -15.34400 -7.18200  34.30200  1.000 24.42231  ? 182 TYR A N    1 
ATOM   2787 C CA   . TYR A 1 182 ? -14.02700 -7.16900  34.90400  1.000 22.72058  ? 182 TYR A CA   1 
ATOM   2788 C C    . TYR A 1 182 ? -13.98200 -6.05600  35.95200  1.000 25.69520  ? 182 TYR A C    1 
ATOM   2789 O O    . TYR A 1 182 ? -14.40400 -4.93200  35.69400  1.000 25.49476  ? 182 TYR A O    1 
ATOM   2790 C CB   . TYR A 1 182 ? -12.99000 -6.94800  33.81700  1.000 23.79639  ? 182 TYR A CB   1 
ATOM   2791 C CG   . TYR A 1 182 ? -12.84500 -8.13300  32.88700  1.000 23.12952  ? 182 TYR A CG   1 
ATOM   2792 C CD1  . TYR A 1 182 ? -12.05100 -9.21800  33.28000  1.000 22.70702  ? 182 TYR A CD1  1 
ATOM   2793 C CD2  . TYR A 1 182 ? -13.48900 -8.17400  31.61000  1.000 22.51421  ? 182 TYR A CD2  1 
ATOM   2794 C CE1  . TYR A 1 182 ? -11.87800 -10.32600 32.43500  1.000 24.47598  ? 182 TYR A CE1  1 
ATOM   2795 C CE2  . TYR A 1 182 ? -13.32100 -9.28000  30.74300  1.000 21.64734  ? 182 TYR A CE2  1 
ATOM   2796 C CZ   . TYR A 1 182 ? -12.51700 -10.35900 31.17600  1.000 20.84197  ? 182 TYR A CZ   1 
ATOM   2797 O OH   . TYR A 1 182 ? -12.32200 -11.46000 30.35500  1.000 23.06990  ? 182 TYR A OH   1 
ATOM   2798 H H    . TYR A 1 182 ? -15.37600 -6.83800  33.51400  1.000 29.30757  ? 182 TYR A H    1 
ATOM   2799 H HA   . TYR A 1 182 ? -13.85300 -8.01900  35.33800  1.000 27.26550  ? 182 TYR A HA   1 
ATOM   2800 H HB2  . TYR A 1 182 ? -13.25000 -6.18000  33.28500  1.000 28.55646  ? 182 TYR A HB2  1 
ATOM   2801 H HB3  . TYR A 1 182 ? -12.12800 -6.78600  34.23200  1.000 28.55646  ? 182 TYR A HB3  1 
ATOM   2802 H HD1  . TYR A 1 182 ? -11.62600 -9.20000  34.10700  1.000 27.24923  ? 182 TYR A HD1  1 
ATOM   2803 H HD2  . TYR A 1 182 ? -14.01300 -7.45500  31.33800  1.000 27.01786  ? 182 TYR A HD2  1 
ATOM   2804 H HE1  . TYR A 1 182 ? -11.34700 -11.04000 32.70600  1.000 29.37198  ? 182 TYR A HE1  1 
ATOM   2805 H HE2  . TYR A 1 182 ? -13.74100 -9.30300  29.91400  1.000 25.97761  ? 182 TYR A HE2  1 
ATOM   2806 H HH   . TYR A 1 182 ? -12.75100 -11.36400 29.63900  1.000 27.68468  ? 182 TYR A HH   1 
ATOM   2807 N N    . GLY A 1 183 ? -13.50900 -6.37000  37.15100  1.000 25.67273  ? 183 GLY A N    1 
ATOM   2808 C CA   . GLY A 1 183 ? -13.38300 -5.33100  38.14100  1.000 27.16341  ? 183 GLY A CA   1 
ATOM   2809 C C    . GLY A 1 183 ? -14.71000 -5.06700  38.83100  1.000 28.83268  ? 183 GLY A C    1 
ATOM   2810 O O    . GLY A 1 183 ? -15.72000 -5.75400  38.62000  1.000 29.90311  ? 183 GLY A O    1 
ATOM   2811 H H    . GLY A 1 183 ? -13.26300 -7.15400  37.40500  1.000 30.80808  ? 183 GLY A H    1 
ATOM   2812 H HA2  . GLY A 1 183 ? -12.73100 -5.59400  38.80900  1.000 32.59689  ? 183 GLY A HA2  1 
ATOM   2813 H HA3  . GLY A 1 183 ? -13.08200 -4.51200  37.71700  1.000 32.59689  ? 183 GLY A HA3  1 
ATOM   2814 N N    . PRO A 1 184 ? -14.71300 -4.09000  39.69400  1.000 25.63768  ? 184 PRO A N    1 
ATOM   2815 C CA   . PRO A 1 184 ? -15.91800 -3.83200  40.49700  1.000 29.64707  ? 184 PRO A CA   1 
ATOM   2816 C C    . PRO A 1 184 ? -16.91800 -2.90400  39.82000  1.000 31.54744  ? 184 PRO A C    1 
ATOM   2817 O O    . PRO A 1 184 ? -17.68400 -2.21300  40.49300  1.000 38.44344  ? 184 PRO A O    1 
ATOM   2818 C CB   . PRO A 1 184 ? -15.34200 -3.18700  41.75900  1.000 31.21275  ? 184 PRO A CB   1 
ATOM   2819 C CG   . PRO A 1 184 ? -14.13400 -2.40200  41.23700  1.000 31.23473  ? 184 PRO A CG   1 
ATOM   2820 C CD   . PRO A 1 184 ? -13.58600 -3.22200  40.04200  1.000 30.11931  ? 184 PRO A CD   1 
ATOM   2821 H HA   . PRO A 1 184 ? -16.35600 -4.66500  40.73200  1.000 35.57729  ? 184 PRO A HA   1 
ATOM   2822 H HB2  . PRO A 1 184 ? -15.99500 -2.59400  42.16100  1.000 37.45610  ? 184 PRO A HB2  1 
ATOM   2823 H HB3  . PRO A 1 184 ? -15.06500 -3.87400  42.38500  1.000 37.45610  ? 184 PRO A HB3  1 
ATOM   2824 H HG2  . PRO A 1 184 ? -14.41900 -1.52200  40.94500  1.000 37.48247  ? 184 PRO A HG2  1 
ATOM   2825 H HG3  . PRO A 1 184 ? -13.46600 -2.33000  41.93700  1.000 37.48247  ? 184 PRO A HG3  1 
ATOM   2826 H HD2  . PRO A 1 184 ? -13.36700 -2.63600  39.30000  1.000 36.14398  ? 184 PRO A HD2  1 
ATOM   2827 H HD3  . PRO A 1 184 ? -12.82100 -3.75100  40.31800  1.000 36.14398  ? 184 PRO A HD3  1 
ATOM   2828 N N    . PHE A 1 185 ? -17.01000 -2.93100  38.51600  1.000 26.29876  ? 185 PHE A N    1 
ATOM   2829 C CA   . PHE A 1 185 ? -17.78100 -1.90400  37.82300  1.000 26.88119  ? 185 PHE A CA   1 
ATOM   2830 C C    . PHE A 1 185 ? -19.15800 -2.44800  37.52800  1.000 27.64596  ? 185 PHE A C    1 
ATOM   2831 O O    . PHE A 1 185 ? -19.36300 -3.66100  37.53500  1.000 26.90246  ? 185 PHE A O    1 
ATOM   2832 C CB   . PHE A 1 185 ? -17.07900 -1.49500  36.50300  1.000 26.94458  ? 185 PHE A CB   1 
ATOM   2833 C CG   . PHE A 1 185 ? -15.67200 -0.99200  36.74700  1.000 24.69432  ? 185 PHE A CG   1 
ATOM   2834 C CD1  . PHE A 1 185 ? -15.49300 0.17000   37.50500  1.000 28.19216  ? 185 PHE A CD1  1 
ATOM   2835 C CD2  . PHE A 1 185 ? -14.56800 -1.71000  36.35200  1.000 27.12315  ? 185 PHE A CD2  1 
ATOM   2836 C CE1  . PHE A 1 185 ? -14.24500 0.64100   37.83600  1.000 30.04276  ? 185 PHE A CE1  1 
ATOM   2837 C CE2  . PHE A 1 185 ? -13.31500 -1.25700  36.71400  1.000 25.54637  ? 185 PHE A CE2  1 
ATOM   2838 C CZ   . PHE A 1 185 ? -13.14500 -0.06900  37.43000  1.000 27.32429  ? 185 PHE A CZ   1 
ATOM   2839 H H    . PHE A 1 185 ? -16.64600 -3.51900  38.00400  1.000 31.55932  ? 185 PHE A H    1 
ATOM   2840 H HA   . PHE A 1 185 ? -17.86900 -1.11800  38.38400  1.000 32.25823  ? 185 PHE A HA   1 
ATOM   2841 H HB2  . PHE A 1 185 ? -17.02800 -2.26600  35.91700  1.000 32.33430  ? 185 PHE A HB2  1 
ATOM   2842 H HB3  . PHE A 1 185 ? -17.58600 -0.78500  36.07900  1.000 32.33430  ? 185 PHE A HB3  1 
ATOM   2843 H HD1  . PHE A 1 185 ? -16.24200 0.64400   37.78700  1.000 33.83139  ? 185 PHE A HD1  1 
ATOM   2844 H HD2  . PHE A 1 185 ? -14.66500 -2.50800  35.88400  1.000 32.54859  ? 185 PHE A HD2  1 
ATOM   2845 H HE1  . PHE A 1 185 ? -14.14900 1.42800   38.32200  1.000 36.05211  ? 185 PHE A HE1  1 
ATOM   2846 H HE2  . PHE A 1 185 ? -12.56400 -1.72200  36.42200  1.000 30.65644  ? 185 PHE A HE2  1 
ATOM   2847 H HZ   . PHE A 1 185 ? -12.29000 0.23700   37.63100  1.000 32.78995  ? 185 PHE A HZ   1 
ATOM   2848 N N    . VAL A 1 186 ? -20.12300 -1.52400  37.34900  1.000 25.62543  ? 186 VAL A N    1 
ATOM   2849 C CA   . VAL A 1 186 ? -21.51100 -1.88200  37.05200  1.000 29.02495  ? 186 VAL A CA   1 
ATOM   2850 C C    . VAL A 1 186 ? -21.95900 -1.07300  35.84000  1.000 27.50354  ? 186 VAL A C    1 
ATOM   2851 O O    . VAL A 1 186 ? -21.41200 -0.00100  35.55800  1.000 28.06729  ? 186 VAL A O    1 
ATOM   2852 C CB   . VAL A 1 186 ? -22.47900 -1.65000  38.23700  1.000 29.46874  ? 186 VAL A CB   1 
ATOM   2853 C CG1  . VAL A 1 186 ? -22.09400 -2.56200  39.43000  1.000 32.66537  ? 186 VAL A CG1  1 
ATOM   2854 C CG2  . VAL A 1 186 ? -22.44200 -0.19100  38.69700  1.000 30.87497  ? 186 VAL A CG2  1 
ATOM   2855 H H    . VAL A 1 186 ? -19.98900 -0.67600  37.39700  1.000 30.75132  ? 186 VAL A H    1 
ATOM   2856 H HA   . VAL A 1 186 ? -21.55100 -2.82200  36.81500  1.000 34.83074  ? 186 VAL A HA   1 
ATOM   2857 H HB   . VAL A 1 186 ? -23.38500 -1.86500  37.96400  1.000 35.36329  ? 186 VAL A HB   1 
ATOM   2858 H HG11 . VAL A 1 186 ? -22.71200 -2.40400  40.16000  1.000 39.19925  ? 186 VAL A HG11 1 
ATOM   2859 H HG12 . VAL A 1 186 ? -22.14500 -3.48900  39.14800  1.000 39.19925  ? 186 VAL A HG12 1 
ATOM   2860 H HG13 . VAL A 1 186 ? -21.19000 -2.35000  39.71000  1.000 39.19925  ? 186 VAL A HG13 1 
ATOM   2861 H HG21 . VAL A 1 186 ? -22.99100 -0.09800  39.49100  1.000 37.05077  ? 186 VAL A HG21 1 
ATOM   2862 H HG22 . VAL A 1 186 ? -21.52500 0.05300   38.89900  1.000 37.05077  ? 186 VAL A HG22 1 
ATOM   2863 H HG23 . VAL A 1 186 ? -22.78700 0.37400   37.98800  1.000 37.05077  ? 186 VAL A HG23 1 
ATOM   2864 N N    . ASP A 1 187 ? -22.95800 -1.62400  35.12100  1.000 26.69588  ? 187 ASP A N    1 
ATOM   2865 C CA   . ASP A 1 187 ? -23.55100 -0.96500  33.92400  1.000 26.70984  ? 187 ASP A CA   1 
ATOM   2866 C C    . ASP A 1 187 ? -24.57700 0.08300   34.34900  1.000 28.70132  ? 187 ASP A C    1 
ATOM   2867 O O    . ASP A 1 187 ? -25.75700 -0.07400  34.04500  1.000 29.42305  ? 187 ASP A O    1 
ATOM   2868 C CB   . ASP A 1 187 ? -24.01300 -1.94400  32.85000  1.000 28.28429  ? 187 ASP A CB   1 
ATOM   2869 C CG   . ASP A 1 187 ? -24.90300 -3.08000  33.29200  1.000 28.90038  ? 187 ASP A CG   1 
ATOM   2870 O OD1  . ASP A 1 187 ? -25.12000 -3.23900  34.49600  1.000 28.99686  ? 187 ASP A OD1  1 
ATOM   2871 O OD2  . ASP A 1 187 ? -25.36200 -3.79000  32.40700  1.000 26.36677  ? 187 ASP A OD2  1 
ATOM   2872 H H    . ASP A 1 187 ? -23.31500 -2.38500  35.30500  1.000 32.03586  ? 187 ASP A H    1 
ATOM   2873 H HA   . ASP A 1 187 ? -22.83100 -0.46700  33.51600  1.000 32.05261  ? 187 ASP A HA   1 
ATOM   2874 H HB2  . ASP A 1 187 ? -24.50100 -1.44400  32.17700  1.000 33.94195  ? 187 ASP A HB2  1 
ATOM   2875 H HB3  . ASP A 1 187 ? -23.22600 -2.34000  32.44400  1.000 33.94195  ? 187 ASP A HB3  1 
ATOM   2876 N N    . ARG A 1 188 ? -24.10700 1.10600   35.01600  1.000 24.37315  ? 188 ARG A N    1 
ATOM   2877 C CA   . ARG A 1 188 ? -24.89100 2.23300   35.48700  1.000 26.45233  ? 188 ARG A CA   1 
ATOM   2878 C C    . ARG A 1 188 ? -23.99100 3.44600   35.31400  1.000 28.49703  ? 188 ARG A C    1 
ATOM   2879 O O    . ARG A 1 188 ? -22.78300 3.33300   35.49500  1.000 29.09921  ? 188 ARG A O    1 
ATOM   2880 C CB   . ARG A 1 188 ? -25.27500 2.08900   37.01800  1.000 29.26945  ? 188 ARG A CB   1 
ATOM   2881 C CG   . ARG A 1 188 ? -26.28100 0.96800   37.35700  1.000 30.83310  ? 188 ARG A CG   1 
ATOM   2882 C CD   . ARG A 1 188 ? -26.16800 0.53300   38.82800  1.000 32.79665  ? 188 ARG A CD   1 
ATOM   2883 N NE   . ARG A 1 188 ? -26.52800 1.65000   39.69300  1.000 29.43663  ? 188 ARG A NE   1 
ATOM   2884 C CZ   . ARG A 1 188 ? -26.14500 1.78100   40.95300  1.000 32.35971  ? 188 ARG A CZ   1 
ATOM   2885 N NH1  . ARG A 1 188 ? -25.36700 0.87500   41.53900  1.000 32.94946  ? 188 ARG A NH1  1 
ATOM   2886 N NH2  . ARG A 1 188 ? -26.50100 2.87600   41.62200  1.000 29.73498  ? 188 ARG A NH2  1 
ATOM   2887 H H    . ARG A 1 188 ? -23.27600 1.17900   35.22500  1.000 29.24858  ? 188 ARG A H    1 
ATOM   2888 H HA   . ARG A 1 188 ? -25.69400 2.34100   34.95400  1.000 31.74359  ? 188 ARG A HA   1 
ATOM   2889 H HB2  . ARG A 1 188 ? -24.46500 1.91300   37.52100  1.000 35.12414  ? 188 ARG A HB2  1 
ATOM   2890 H HB3  . ARG A 1 188 ? -25.66300 2.92700   37.31500  1.000 35.12414  ? 188 ARG A HB3  1 
ATOM   2891 H HG2  . ARG A 1 188 ? -27.18200 1.29100   37.20800  1.000 37.00052  ? 188 ARG A HG2  1 
ATOM   2892 H HG3  . ARG A 1 188 ? -26.10300 0.19700   36.79600  1.000 37.00052  ? 188 ARG A HG3  1 
ATOM   2893 H HD2  . ARG A 1 188 ? -26.77800 -0.20200  38.99900  1.000 39.35679  ? 188 ARG A HD2  1 
ATOM   2894 H HD3  . ARG A 1 188 ? -25.25400 0.27100   39.01900  1.000 39.35679  ? 188 ARG A HD3  1 
ATOM   2895 H HE   . ARG A 1 188 ? -27.02500 2.26800   39.36100  1.000 35.32476  ? 188 ARG A HE   1 
ATOM   2896 H HH11 . ARG A 1 188 ? -25.12600 0.17000   41.11100  1.000 39.54015  ? 188 ARG A HH11 1 
ATOM   2897 H HH12 . ARG A 1 188 ? -25.12400 0.98400   42.35700  1.000 39.54015  ? 188 ARG A HH12 1 
ATOM   2898 H HH21 . ARG A 1 188 ? -26.99800 3.46800   41.24500  1.000 35.68278  ? 188 ARG A HH21 1 
ATOM   2899 H HH22 . ARG A 1 188 ? -26.25600 2.97900   42.44000  1.000 35.68278  ? 188 ARG A HH22 1 
ATOM   2900 N N    . GLN A 1 189 ? -24.57500 4.62100   35.07300  1.000 28.29601  ? 189 GLN A N    1 
ATOM   2901 C CA   . GLN A 1 189 ? -23.76600 5.82400   34.97000  1.000 31.27200  ? 189 GLN A CA   1 
ATOM   2902 C C    . GLN A 1 189 ? -23.54700 6.49900   36.31300  1.000 33.19420  ? 189 GLN A C    1 
ATOM   2903 O O    . GLN A 1 189 ? -23.24300 7.69800   36.36000  1.000 34.16221  ? 189 GLN A O    1 
ATOM   2904 C CB   . GLN A 1 189 ? -24.38500 6.76800   33.94600  1.000 35.00013  ? 189 GLN A CB   1 
ATOM   2905 C CG   . GLN A 1 189 ? -24.24200 6.11000   32.58600  1.000 32.72744  ? 189 GLN A CG   1 
ATOM   2906 C CD   . GLN A 1 189 ? -24.55600 7.03600   31.40000  1.000 37.56920  ? 189 GLN A CD   1 
ATOM   2907 O OE1  . GLN A 1 189 ? -24.01500 6.85400   30.30400  1.000 34.32889  ? 189 GLN A OE1  1 
ATOM   2908 N NE2  . GLN A 1 189 ? -25.40800 8.01300   31.61900  1.000 38.72176  ? 189 GLN A NE2  1 
ATOM   2909 H H    . GLN A 1 189 ? -25.42000 4.74300   34.96800  1.000 33.95601  ? 189 GLN A H    1 
ATOM   2910 H HA   . GLN A 1 189 ? -22.89100 5.57400   34.63600  1.000 37.52720  ? 189 GLN A HA   1 
ATOM   2911 H HB2  . GLN A 1 189 ? -25.32700 6.89700   34.13900  1.000 42.00096  ? 189 GLN A HB2  1 
ATOM   2912 H HB3  . GLN A 1 189 ? -23.90900 7.61300   33.94100  1.000 42.00096  ? 189 GLN A HB3  1 
ATOM   2913 H HG2  . GLN A 1 189 ? -23.32900 5.80100   32.48100  1.000 39.27373  ? 189 GLN A HG2  1 
ATOM   2914 H HG3  . GLN A 1 189 ? -24.85000 5.35600   32.54000  1.000 39.27373  ? 189 GLN A HG3  1 
ATOM   2915 H HE21 . GLN A 1 189 ? -25.76600 8.11100   32.39400  1.000 46.46691  ? 189 GLN A HE21 1 
ATOM   2916 H HE22 . GLN A 1 189 ? -25.61100 8.55400   30.98200  1.000 46.46691  ? 189 GLN A HE22 1 
ATOM   2917 N N    . THR A 1 190 ? -23.74000 5.76500   37.39900  1.000 32.06002  ? 190 THR A N    1 
ATOM   2918 C CA   . THR A 1 190 ? -23.42500 6.29100   38.70600  1.000 34.13241  ? 190 THR A CA   1 
ATOM   2919 C C    . THR A 1 190 ? -21.91400 6.47200   38.77600  1.000 34.00204  ? 190 THR A C    1 
ATOM   2920 O O    . THR A 1 190 ? -21.14500 5.89800   37.98600  1.000 33.68969  ? 190 THR A O    1 
ATOM   2921 C CB   . THR A 1 190 ? -23.96400 5.31500   39.77900  1.000 33.94827  ? 190 THR A CB   1 
ATOM   2922 O OG1  . THR A 1 190 ? -23.85200 5.85400   41.10800  1.000 35.49618  ? 190 THR A OG1  1 
ATOM   2923 C CG2  . THR A 1 190 ? -23.20800 3.96300   39.66000  1.000 32.88756  ? 190 THR A CG2  1 
ATOM   2924 H H    . THR A 1 190 ? -24.05500 4.96500   37.40200  1.000 38.47283  ? 190 THR A H    1 
ATOM   2925 H HA   . THR A 1 190 ? -23.85000 7.15500   38.82500  1.000 40.95970  ? 190 THR A HA   1 
ATOM   2926 H HB   . THR A 1 190 ? -24.90100 5.14300   39.59500  1.000 40.73873  ? 190 THR A HB   1 
ATOM   2927 H HG1  . THR A 1 190 ? -24.15200 5.30400   41.66700  1.000 42.59622  ? 190 THR A HG1  1 
ATOM   2928 H HG21 . THR A 1 190 ? -23.62300 3.30300   40.23700  1.000 39.46587  ? 190 THR A HG21 1 
ATOM   2929 H HG22 . THR A 1 190 ? -23.23600 3.64000   38.74600  1.000 39.46587  ? 190 THR A HG22 1 
ATOM   2930 H HG23 . THR A 1 190 ? -22.28200 4.07300   39.92700  1.000 39.46587  ? 190 THR A HG23 1 
ATOM   2931 N N    . ALA A 1 191 ? -21.48900 7.25400   39.74900  1.000 34.95583  ? 191 ALA A N    1 
ATOM   2932 C CA   . ALA A 1 191 ? -20.08100 7.57200   39.90400  1.000 37.32318  ? 191 ALA A CA   1 
ATOM   2933 C C    . ALA A 1 191 ? -19.30600 6.31600   40.23700  1.000 34.05084  ? 191 ALA A C    1 
ATOM   2934 O O    . ALA A 1 191 ? -19.68600 5.55400   41.11700  1.000 30.91680  ? 191 ALA A O    1 
ATOM   2935 C CB   . ALA A 1 191 ? -19.90400 8.61500   41.00800  1.000 42.19695  ? 191 ALA A CB   1 
ATOM   2936 H H    . ALA A 1 191 ? -21.99900 7.61700   40.33900  1.000 41.94780  ? 191 ALA A H    1 
ATOM   2937 H HA   . ALA A 1 191 ? -19.73600 7.93800   39.07400  1.000 44.78861  ? 191 ALA A HA   1 
ATOM   2938 H HB1  . ALA A 1 191 ? -18.96000 8.81800   41.10100  1.000 50.63714  ? 191 ALA A HB1  1 
ATOM   2939 H HB2  . ALA A 1 191 ? -20.39300 9.41700   40.76600  1.000 50.63714  ? 191 ALA A HB2  1 
ATOM   2940 H HB3  . ALA A 1 191 ? -20.24900 8.25500   41.84000  1.000 50.63714  ? 191 ALA A HB3  1 
ATOM   2941 N N    . GLN A 1 192 ? -18.27700 6.04700   39.44400  1.000 32.61715  ? 192 GLN A N    1 
ATOM   2942 C CA   . GLN A 1 192 ? -17.40000 4.90800   39.62600  1.000 32.54440  ? 192 GLN A CA   1 
ATOM   2943 C C    . GLN A 1 192 ? -16.01400 5.40700   39.28100  1.000 36.04927  ? 192 GLN A C    1 
ATOM   2944 O O    . GLN A 1 192 ? -15.87000 6.30600   38.44000  1.000 36.82823  ? 192 GLN A O    1 
ATOM   2945 C CB   . GLN A 1 192 ? -17.78100 3.71300   38.74100  1.000 35.52358  ? 192 GLN A CB   1 
ATOM   2946 C CG   . GLN A 1 192 ? -19.24000 3.31600   38.87100  1.000 34.46447  ? 192 GLN A CG   1 
ATOM   2947 C CD   . GLN A 1 192 ? -19.57600 2.19400   37.95700  1.000 34.97672  ? 192 GLN A CD   1 
ATOM   2948 O OE1  . GLN A 1 192 ? -19.01800 1.08200   38.04900  1.000 30.54911  ? 192 GLN A OE1  1 
ATOM   2949 N NE2  . GLN A 1 192 ? -20.46600 2.48500   36.99300  1.000 32.39029  ? 192 GLN A NE2  1 
ATOM   2950 H H    . GLN A 1 192 ? -18.06200 6.53300   38.76700  1.000 39.14138  ? 192 GLN A H    1 
ATOM   2951 H HA   . GLN A 1 192 ? -17.41100 4.62700   40.55400  1.000 39.05408  ? 192 GLN A HA   1 
ATOM   2952 H HB2  . GLN A 1 192 ? -17.61600 3.94300   37.81300  1.000 42.62909  ? 192 GLN A HB2  1 
ATOM   2953 H HB3  . GLN A 1 192 ? -17.24000 2.94900   38.99400  1.000 42.62909  ? 192 GLN A HB3  1 
ATOM   2954 H HG2  . GLN A 1 192 ? -19.41500 3.03000   39.78100  1.000 41.35817  ? 192 GLN A HG2  1 
ATOM   2955 H HG3  . GLN A 1 192 ? -19.80000 4.07200   38.64300  1.000 41.35817  ? 192 GLN A HG3  1 
ATOM   2956 H HE21 . GLN A 1 192 ? -20.82100 3.26800   36.95600  1.000 38.86915  ? 192 GLN A HE21 1 
ATOM   2957 H HE22 . GLN A 1 192 ? -20.70000 1.88100   36.42700  1.000 38.86915  ? 192 GLN A HE22 1 
ATOM   2958 N N    . ALA A 1 193 ? -15.01300 4.90600   39.98600  1.000 40.33133  ? 193 ALA A N    1 
ATOM   2959 C CA   . ALA A 1 193 ? -13.64400 5.30600   39.67500  1.000 36.90353  ? 193 ALA A CA   1 
ATOM   2960 C C    . ALA A 1 193 ? -12.76500 4.06700   39.64400  1.000 32.14003  ? 193 ALA A C    1 
ATOM   2961 O O    . ALA A 1 193 ? -12.92600 3.14300   40.45300  1.000 36.28335  ? 193 ALA A O    1 
ATOM   2962 C CB   . ALA A 1 193 ? -13.09900 6.33700   40.69800  1.000 38.81822  ? 193 ALA A CB   1 
ATOM   2963 H H    . ALA A 1 193 ? -15.09100 4.34600   40.63400  1.000 48.39839  ? 193 ALA A H    1 
ATOM   2964 H HA   . ALA A 1 193 ? -13.61700 5.71200   38.79500  1.000 44.28503  ? 193 ALA A HA   1 
ATOM   2965 H HB1  . ALA A 1 193 ? -12.19100 6.57400   40.45400  1.000 46.58267  ? 193 ALA A HB1  1 
ATOM   2966 H HB2  . ALA A 1 193 ? -13.66300 7.12600   40.68100  1.000 46.58267  ? 193 ALA A HB2  1 
ATOM   2967 H HB3  . ALA A 1 193 ? -13.11100 5.94000   41.58300  1.000 46.58267  ? 193 ALA A HB3  1 
ATOM   2968 N N    . ALA A 1 194 ? -11.82600 4.06400   38.71400  1.000 35.51531  ? 194 ALA A N    1 
ATOM   2969 C CA   . ALA A 1 194 ? -10.81900 3.00700   38.69000  1.000 36.26209  ? 194 ALA A CA   1 
ATOM   2970 C C    . ALA A 1 194 ? -9.87000  3.15800   39.88500  1.000 37.87161  ? 194 ALA A C    1 
ATOM   2971 O O    . ALA A 1 194 ? -9.51500  4.27700   40.26400  1.000 38.11655  ? 194 ALA A O    1 
ATOM   2972 C CB   . ALA A 1 194 ? -10.06300 3.07800   37.37000  1.000 38.68983  ? 194 ALA A CB   1 
ATOM   2973 H H    . ALA A 1 194 ? -11.74600 4.65200   38.09100  1.000 42.61917  ? 194 ALA A H    1 
ATOM   2974 H HA   . ALA A 1 194 ? -11.25500 2.14200   38.75000  1.000 43.51531  ? 194 ALA A HA   1 
ATOM   2975 H HB1  . ALA A 1 194 ? -9.42200  2.35100   37.33300  1.000 46.42860  ? 194 ALA A HB1  1 
ATOM   2976 H HB2  . ALA A 1 194 ? -10.69800 3.00000   36.64100  1.000 46.42860  ? 194 ALA A HB2  1 
ATOM   2977 H HB3  . ALA A 1 194 ? -9.60300  3.93000   37.31600  1.000 46.42860  ? 194 ALA A HB3  1 
ATOM   2978 N N    . GLY A 1 195 ? -9.51400  2.04500   40.52900  1.000 41.32150  ? 195 GLY A N    1 
ATOM   2979 C CA   . GLY A 1 195 ? -8.47500  2.10300   41.54000  1.000 42.53090  ? 195 GLY A CA   1 
ATOM   2980 C C    . GLY A 1 195 ? -7.12700  2.52600   40.93300  1.000 37.96079  ? 195 GLY A C    1 
ATOM   2981 O O    . GLY A 1 195 ? -6.95400  2.68200   39.72000  1.000 33.92648  ? 195 GLY A O    1 
ATOM   2982 H H    . GLY A 1 195 ? -9.85300  1.26500   40.39900  1.000 49.58660  ? 195 GLY A H    1 
ATOM   2983 H HA2  . GLY A 1 195 ? -8.72200  2.74300   42.22600  1.000 51.03788  ? 195 GLY A HA2  1 
ATOM   2984 H HA3  . GLY A 1 195 ? -8.37100  1.23100   41.95200  1.000 51.03788  ? 195 GLY A HA3  1 
ATOM   2985 N N    . THR A 1 196 ? -6.14300  2.77400   41.81400  1.000 34.63319  ? 196 THR A N    1 
ATOM   2986 C CA   . THR A 1 196 ? -4.83300  3.16200   41.31400  1.000 35.31774  ? 196 THR A CA   1 
ATOM   2987 C C    . THR A 1 196 ? -4.28500  2.07200   40.43300  1.000 31.03123  ? 196 THR A C    1 
ATOM   2988 O O    . THR A 1 196 ? -4.36300  0.89200   40.77800  1.000 37.27813  ? 196 THR A O    1 
ATOM   2989 C CB   . THR A 1 196 ? -3.86600  3.43800   42.46700  1.000 34.34348  ? 196 THR A CB   1 
ATOM   2990 O OG1  . THR A 1 196 ? -4.46300  4.41900   43.30600  1.000 40.35076  ? 196 THR A OG1  1 
ATOM   2991 C CG2  . THR A 1 196 ? -2.58200  4.04400   41.92500  1.000 37.56654  ? 196 THR A CG2  1 
ATOM   2992 H H    . THR A 1 196 ? -6.21200  2.72500   42.67000  1.000 41.56063  ? 196 THR A H    1 
ATOM   2993 H HA   . THR A 1 196 ? -4.91700  3.97000   40.78500  1.000 42.38209  ? 196 THR A HA   1 
ATOM   2994 H HB   . THR A 1 196 ? -3.67000  2.62700   42.96200  1.000 41.21298  ? 196 THR A HB   1 
ATOM   2995 H HG1  . THR A 1 196 ? -3.95400  4.59300   43.95100  1.000 48.42172  ? 196 THR A HG1  1 
ATOM   2996 H HG21 . THR A 1 196 ? -2.01600  4.33000   42.65900  1.000 45.08065  ? 196 THR A HG21 1 
ATOM   2997 H HG22 . THR A 1 196 ? -2.10100  3.38900   41.39500  1.000 45.08065  ? 196 THR A HG22 1 
ATOM   2998 H HG23 . THR A 1 196 ? -2.78700  4.81200   41.36900  1.000 45.08065  ? 196 THR A HG23 1 
ATOM   2999 N N    . ASP A 1 197 ? -3.76800  2.46000   39.27900  1.000 32.09749  ? 197 ASP A N    1 
ATOM   3000 C CA   . ASP A 1 197 ? -3.23500  1.42600   38.40900  1.000 32.52312  ? 197 ASP A CA   1 
ATOM   3001 C C    . ASP A 1 197 ? -1.76100  1.19100   38.73700  1.000 35.59045  ? 197 ASP A C    1 
ATOM   3002 O O    . ASP A 1 197 ? -1.07900  2.03700   39.33800  1.000 38.75482  ? 197 ASP A O    1 
ATOM   3003 C CB   . ASP A 1 197 ? -3.37900  1.77500   36.94300  1.000 30.66661  ? 197 ASP A CB   1 
ATOM   3004 C CG   . ASP A 1 197 ? -3.36400  0.52400   36.05800  1.000 32.98465  ? 197 ASP A CG   1 
ATOM   3005 O OD1  . ASP A 1 197 ? -3.53300  -0.62900  36.57400  1.000 35.25531  ? 197 ASP A OD1  1 
ATOM   3006 O OD2  . ASP A 1 197 ? -3.15700  0.68600   34.86600  1.000 32.63012  ? 197 ASP A OD2  1 
ATOM   3007 H H    . ASP A 1 197 ? -3.71400  3.26700   38.98800  1.000 38.51779  ? 197 ASP A H    1 
ATOM   3008 H HA   . ASP A 1 197 ? -3.71400  0.59900   38.56700  1.000 39.02855  ? 197 ASP A HA   1 
ATOM   3009 H HB2  . ASP A 1 197 ? -4.22200  2.23400   36.80500  1.000 36.80073  ? 197 ASP A HB2  1 
ATOM   3010 H HB3  . ASP A 1 197 ? -2.64000  2.34400   36.67600  1.000 36.80073  ? 197 ASP A HB3  1 
ATOM   3011 N N    . THR A 1 198 ? -1.30700  -0.00800  38.40500  1.000 32.31341  ? 198 THR A N    1 
ATOM   3012 C CA   . THR A 1 198 ? 0.06200   -0.41200  38.66500  1.000 33.57813  ? 198 THR A CA   1 
ATOM   3013 C C    . THR A 1 198 ? 0.63400   -0.97200  37.38200  1.000 32.37877  ? 198 THR A C    1 
ATOM   3014 O O    . THR A 1 198 ? -0.10400  -1.28600  36.44600  1.000 29.28534  ? 198 THR A O    1 
ATOM   3015 C CB   . THR A 1 198 ? 0.14000   -1.47200  39.75600  1.000 32.53886  ? 198 THR A CB   1 
ATOM   3016 O OG1  . THR A 1 198 ? -0.81200  -2.49700  39.44700  1.000 33.26174  ? 198 THR A OG1  1 
ATOM   3017 C CG2  . THR A 1 198 ? -0.18400  -0.87400  41.12300  1.000 38.97134  ? 198 THR A CG2  1 
ATOM   3018 H H    . THR A 1 198 ? -1.78100  -0.61400  38.02200  1.000 38.77690  ? 198 THR A H    1 
ATOM   3019 H HA   . THR A 1 198 ? 0.59100   0.35500   38.93400  1.000 40.29456  ? 198 THR A HA   1 
ATOM   3020 H HB   . THR A 1 198 ? 1.03300   -1.85000  39.78400  1.000 39.04743  ? 198 THR A HB   1 
ATOM   3021 H HG1  . THR A 1 198 ? -0.83700  -3.06200  40.06800  1.000 39.91489  ? 198 THR A HG1  1 
ATOM   3022 H HG21 . THR A 1 198 ? -0.13000  -1.56100  41.80600  1.000 46.76641  ? 198 THR A HG21 1 
ATOM   3023 H HG22 . THR A 1 198 ? 0.44800   -0.16900  41.33400  1.000 46.76641  ? 198 THR A HG22 1 
ATOM   3024 H HG23 . THR A 1 198 ? -1.08000  -0.50300  41.11800  1.000 46.76641  ? 198 THR A HG23 1 
ATOM   3025 N N    . THR A 1 199 ? 1.95500   -1.13400  37.36500  1.000 27.89884  ? 199 THR A N    1 
ATOM   3026 C CA   . THR A 1 199 ? 2.63500   -1.65800  36.18600  1.000 26.04931  ? 199 THR A CA   1 
ATOM   3027 C C    . THR A 1 199 ? 2.72800   -3.18600  36.23400  1.000 25.67096  ? 199 THR A C    1 
ATOM   3028 O O    . THR A 1 199 ? 2.94000   -3.78300  37.30900  1.000 25.88544  ? 199 THR A O    1 
ATOM   3029 C CB   . THR A 1 199 ? 4.02200   -1.02900  36.08900  1.000 29.49234  ? 199 THR A CB   1 
ATOM   3030 O OG1  . THR A 1 199 ? 3.86000   0.38000   35.94500  1.000 30.10042  ? 199 THR A OG1  1 
ATOM   3031 C CG2  . THR A 1 199 ? 4.77800   -1.58100  34.93500  1.000 27.86051  ? 199 THR A CG2  1 
ATOM   3032 H H    . THR A 1 199 ? 2.47800   -0.94800  38.02200  1.000 33.47941  ? 199 THR A H    1 
ATOM   3033 H HA   . THR A 1 199 ? 2.13500   -1.41000  35.39300  1.000 31.25997  ? 199 THR A HA   1 
ATOM   3034 H HB   . THR A 1 199 ? 4.51900   -1.21600  36.90000  1.000 35.39161  ? 199 THR A HB   1 
ATOM   3035 H HG1  . THR A 1 199 ? 4.61100   0.75100   35.88900  1.000 36.12130  ? 199 THR A HG1  1 
ATOM   3036 H HG21 . THR A 1 199 ? 5.52500   -1.00000  34.72200  1.000 33.43341  ? 199 THR A HG21 1 
ATOM   3037 H HG22 . THR A 1 199 ? 5.11700   -2.46400  35.14900  1.000 33.43341  ? 199 THR A HG22 1 
ATOM   3038 H HG23 . THR A 1 199 ? 4.19900   -1.64300  34.15900  1.000 33.43341  ? 199 THR A HG23 1 
ATOM   3039 N N    . ILE A 1 200 ? 2.53300   -3.82100  35.07800  1.000 25.11548  ? 200 ILE A N    1 
ATOM   3040 C CA   . ILE A 1 200 ? 2.47700   -5.28500  35.00400  1.000 23.15803  ? 200 ILE A CA   1 
ATOM   3041 C C    . ILE A 1 200 ? 3.91900   -5.79000  34.90900  1.000 26.42926  ? 200 ILE A C    1 
ATOM   3042 O O    . ILE A 1 200 ? 4.51300   -5.85700  33.83100  1.000 23.54084  ? 200 ILE A O    1 
ATOM   3043 C CB   . ILE A 1 200 ? 1.63700   -5.76700  33.83100  1.000 22.33193  ? 200 ILE A CB   1 
ATOM   3044 C CG1  . ILE A 1 200 ? 0.23000   -5.10600  33.87500  1.000 22.74992  ? 200 ILE A CG1  1 
ATOM   3045 C CG2  . ILE A 1 200 ? 1.60900   -7.26400  33.77900  1.000 25.14908  ? 200 ILE A CG2  1 
ATOM   3046 C CD1  . ILE A 1 200 ? -0.39500  -5.12100  32.44400  1.000 22.44403  ? 200 ILE A CD1  1 
ATOM   3047 H H    . ILE A 1 200 ? 2.43000   -3.42800  34.32000  1.000 30.13938  ? 200 ILE A H    1 
ATOM   3048 H HA   . ILE A 1 200 ? 2.08600   -5.63300  35.82100  1.000 27.79044  ? 200 ILE A HA   1 
ATOM   3049 H HB   . ILE A 1 200 ? 2.07200   -5.46000  33.02000  1.000 26.79912  ? 200 ILE A HB   1 
ATOM   3050 H HG12 . ILE A 1 200 ? -0.34700  -5.61000  34.46900  1.000 27.30070  ? 200 ILE A HG12 1 
ATOM   3051 H HG13 . ILE A 1 200 ? 0.29800   -4.18500  34.16800  1.000 27.30070  ? 200 ILE A HG13 1 
ATOM   3052 H HG21 . ILE A 1 200 ? 0.91800   -7.54600  33.15900  1.000 30.17970  ? 200 ILE A HG21 1 
ATOM   3053 H HG22 . ILE A 1 200 ? 2.47300   -7.58800  33.47900  1.000 30.17970  ? 200 ILE A HG22 1 
ATOM   3054 H HG23 . ILE A 1 200 ? 1.41500   -7.60600  34.66600  1.000 30.17970  ? 200 ILE A HG23 1 
ATOM   3055 H HD11 . ILE A 1 200 ? -1.35500  -5.00400  32.51900  1.000 26.93364  ? 200 ILE A HD11 1 
ATOM   3056 H HD12 . ILE A 1 200 ? -0.01300  -4.39500  31.92600  1.000 26.93364  ? 200 ILE A HD12 1 
ATOM   3057 H HD13 . ILE A 1 200 ? -0.19700  -5.96900  32.01900  1.000 26.93364  ? 200 ILE A HD13 1 
ATOM   3058 N N    . THR A 1 201 ? 4.48400   -6.14300  36.07100  1.000 28.09442  ? 201 THR A N    1 
ATOM   3059 C CA   . THR A 1 201 ? 5.91400   -6.42500  36.16400  1.000 26.29782  ? 201 THR A CA   1 
ATOM   3060 C C    . THR A 1 201 ? 6.32400   -7.58900  35.27600  1.000 26.69210  ? 201 THR A C    1 
ATOM   3061 O O    . THR A 1 201 ? 7.35200   -7.52000  34.58700  1.000 25.75708  ? 201 THR A O    1 
ATOM   3062 C CB   . THR A 1 201 ? 6.27100   -6.70700  37.61400  1.000 26.86521  ? 201 THR A CB   1 
ATOM   3063 O OG1  . THR A 1 201 ? 5.75400   -5.66000  38.44700  1.000 28.97342  ? 201 THR A OG1  1 
ATOM   3064 C CG2  . THR A 1 201 ? 7.83900   -6.81900  37.81500  1.000 27.85554  ? 201 THR A CG2  1 
ATOM   3065 H H    . THR A 1 201 ? 4.05900   -6.22500  36.81400  1.000 33.71411  ? 201 THR A H    1 
ATOM   3066 H HA   . THR A 1 201 ? 6.41000   -5.64100  35.87900  1.000 31.55818  ? 201 THR A HA   1 
ATOM   3067 H HB   . THR A 1 201 ? 5.87200   -7.55000  37.88000  1.000 32.23905  ? 201 THR A HB   1 
ATOM   3068 H HG1  . THR A 1 201 ? 5.94800   -5.81000  39.25000  1.000 34.76890  ? 201 THR A HG1  1 
ATOM   3069 H HG21 . THR A 1 201 ? 8.05100   -6.74900  38.75800  1.000 33.42745  ? 201 THR A HG21 1 
ATOM   3070 H HG22 . THR A 1 201 ? 8.15800   -7.67200  37.48000  1.000 33.42745  ? 201 THR A HG22 1 
ATOM   3071 H HG23 . THR A 1 201 ? 8.28700   -6.10300  37.33800  1.000 33.42745  ? 201 THR A HG23 1 
ATOM   3072 N N    . VAL A 1 202 ? 5.57800   -8.69500  35.30600  1.000 24.37609  ? 202 VAL A N    1 
ATOM   3073 C CA   . VAL A 1 202 ? 6.04800   -9.84400  34.50700  1.000 25.12462  ? 202 VAL A CA   1 
ATOM   3074 C C    . VAL A 1 202 ? 6.11200   -9.48500  33.01600  1.000 24.51231  ? 202 VAL A C    1 
ATOM   3075 O O    . VAL A 1 202 ? 6.96100   -10.02300 32.28000  1.000 24.92322  ? 202 VAL A O    1 
ATOM   3076 C CB   . VAL A 1 202 ? 5.14700   -11.07700 34.74700  1.000 24.43827  ? 202 VAL A CB   1 
ATOM   3077 C CG1  . VAL A 1 202 ? 3.65600   -10.81800 34.31600  1.000 28.89778  ? 202 VAL A CG1  1 
ATOM   3078 C CG2  . VAL A 1 202 ? 5.71300   -12.32400 34.05900  1.000 27.15688  ? 202 VAL A CG2  1 
ATOM   3079 H H    . VAL A 1 202 ? 4.84700   -8.80900  35.74500  1.000 29.25211  ? 202 VAL A H    1 
ATOM   3080 H HA   . VAL A 1 202 ? 6.94600   -10.07500 34.79300  1.000 30.15035  ? 202 VAL A HA   1 
ATOM   3081 H HB   . VAL A 1 202 ? 5.13800   -11.25900 35.70000  1.000 29.32673  ? 202 VAL A HB   1 
ATOM   3082 H HG11 . VAL A 1 202 ? 3.12600   -11.60200 34.52800  1.000 34.67814  ? 202 VAL A HG11 1 
ATOM   3083 H HG12 . VAL A 1 202 ? 3.31700   -10.04900 34.80000  1.000 34.67814  ? 202 VAL A HG12 1 
ATOM   3084 H HG13 . VAL A 1 202 ? 3.62700   -10.64800 33.36200  1.000 34.67814  ? 202 VAL A HG13 1 
ATOM   3085 H HG21 . VAL A 1 202 ? 5.16700   -13.09000 34.29800  1.000 32.58906  ? 202 VAL A HG21 1 
ATOM   3086 H HG22 . VAL A 1 202 ? 5.69500   -12.19200 33.09800  1.000 32.58906  ? 202 VAL A HG22 1 
ATOM   3087 H HG23 . VAL A 1 202 ? 6.62500   -12.46200 34.35800  1.000 32.58906  ? 202 VAL A HG23 1 
ATOM   3088 N N    . ASN A 1 203 ? 5.25100   -8.57800  32.57100  1.000 23.96504  ? 203 ASN A N    1 
ATOM   3089 C CA   . ASN A 1 203 ? 5.24200   -8.13900  31.15100  1.000 25.41373  ? 203 ASN A CA   1 
ATOM   3090 C C    . ASN A 1 203 ? 6.46800   -7.26400  30.85700  1.000 25.85459  ? 203 ASN A C    1 
ATOM   3091 O O    . ASN A 1 203 ? 7.05200   -7.44000  29.79700  1.000 23.62807  ? 203 ASN A O    1 
ATOM   3092 C CB   . ASN A 1 203 ? 3.94200   -7.42200  30.80400  1.000 24.06672  ? 203 ASN A CB   1 
ATOM   3093 C CG   . ASN A 1 203 ? 2.75300   -8.34800  30.68700  1.000 25.46716  ? 203 ASN A CG   1 
ATOM   3094 O OD1  . ASN A 1 203 ? 2.84300   -9.52200  31.01900  1.000 24.74673  ? 203 ASN A OD1  1 
ATOM   3095 N ND2  . ASN A 1 203 ? 1.63300   -7.81900  30.22900  1.000 26.47297  ? 203 ASN A ND2  1 
ATOM   3096 H H    . ASN A 1 203 ? 4.65700   -8.19400  33.05900  1.000 28.75884  ? 203 ASN A H    1 
ATOM   3097 H HA   . ASN A 1 203 ? 5.30200   -8.92500  30.58500  1.000 30.49728  ? 203 ASN A HA   1 
ATOM   3098 H HB2  . ASN A 1 203 ? 3.74700   -6.77400  31.49900  1.000 28.88087  ? 203 ASN A HB2  1 
ATOM   3099 H HB3  . ASN A 1 203 ? 4.05100   -6.97000  29.95300  1.000 28.88087  ? 203 ASN A HB3  1 
ATOM   3100 H HD21 . ASN A 1 203 ? 0.93000   -8.30700  30.14600  1.000 31.76836  ? 203 ASN A HD21 1 
ATOM   3101 H HD22 . ASN A 1 203 ? 1.60900   -6.98800  30.00800  1.000 31.76836  ? 203 ASN A HD22 1 
ATOM   3102 N N    . VAL A 1 204 ? 6.79600   -6.33500  31.75200  1.000 24.98478  ? 204 VAL A N    1 
ATOM   3103 C CA   . VAL A 1 204 ? 8.02100   -5.55000  31.58700  1.000 24.24161  ? 204 VAL A CA   1 
ATOM   3104 C C    . VAL A 1 204 ? 9.21900   -6.48500  31.43700  1.000 23.81055  ? 204 VAL A C    1 
ATOM   3105 O O    . VAL A 1 204 ? 10.03900  -6.32500  30.52700  1.000 23.90457  ? 204 VAL A O    1 
ATOM   3106 C CB   . VAL A 1 204 ? 8.20400   -4.56000  32.74900  1.000 25.71294  ? 204 VAL A CB   1 
ATOM   3107 C CG1  . VAL A 1 204 ? 9.53700   -3.82800  32.62600  1.000 26.59745  ? 204 VAL A CG1  1 
ATOM   3108 C CG2  . VAL A 1 204 ? 7.00900   -3.50900  32.76700  1.000 24.89565  ? 204 VAL A CG2  1 
ATOM   3109 H H    . VAL A 1 204 ? 6.33600   -6.14100  32.45200  1.000 29.98254  ? 204 VAL A H    1 
ATOM   3110 H HA   . VAL A 1 204 ? 7.94900   -5.03200  30.77000  1.000 29.09073  ? 204 VAL A HA   1 
ATOM   3111 H HB   . VAL A 1 204 ? 8.19800   -5.04500  33.58900  1.000 30.85632  ? 204 VAL A HB   1 
ATOM   3112 H HG11 . VAL A 1 204 ? 9.53300   -3.06700  33.22700  1.000 31.91774  ? 204 VAL A HG11 1 
ATOM   3113 H HG12 . VAL A 1 204 ? 10.25600  -4.43300  32.86500  1.000 31.91774  ? 204 VAL A HG12 1 
ATOM   3114 H HG13 . VAL A 1 204 ? 9.64700   -3.52500  31.71100  1.000 31.91774  ? 204 VAL A HG13 1 
ATOM   3115 H HG21 . VAL A 1 204 ? 7.15000   -2.88300  33.49500  1.000 29.87558  ? 204 VAL A HG21 1 
ATOM   3116 H HG22 . VAL A 1 204 ? 6.99300   -3.03500  31.92100  1.000 29.87558  ? 204 VAL A HG22 1 
ATOM   3117 H HG23 . VAL A 1 204 ? 6.17300   -3.98400  32.89600  1.000 29.87558  ? 204 VAL A HG23 1 
ATOM   3118 N N    . LEU A 1 205 ? 9.34600   -7.47900  32.32200  1.000 27.14846  ? 205 LEU A N    1 
ATOM   3119 C CA   . LEU A 1 205 ? 10.48400  -8.41100  32.18700  1.000 24.63089  ? 205 LEU A CA   1 
ATOM   3120 C C    . LEU A 1 205 ? 10.45000  -9.15600  30.86200  1.000 28.85015  ? 205 LEU A C    1 
ATOM   3121 O O    . LEU A 1 205 ? 11.50000  -9.40900  30.26200  1.000 29.08375  ? 205 LEU A O    1 
ATOM   3122 C CB   . LEU A 1 205 ? 10.48900  -9.41800  33.33600  1.000 26.07406  ? 205 LEU A CB   1 
ATOM   3123 C CG   . LEU A 1 205 ? 10.79400  -8.76700  34.68500  1.000 26.93483  ? 205 LEU A CG   1 
ATOM   3124 C CD1  . LEU A 1 205 ? 10.42200  -9.69100  35.83400  1.000 29.41695  ? 205 LEU A CD1  1 
ATOM   3125 C CD2  . LEU A 1 205 ? 12.29500  -8.37100  34.79100  1.000 24.97345  ? 205 LEU A CD2  1 
ATOM   3126 H H    . LEU A 1 205 ? 8.81700   -7.63500  32.98100  1.000 32.57895  ? 205 LEU A H    1 
ATOM   3127 H HA   . LEU A 1 205 ? 11.31100  -7.90600  32.22400  1.000 29.55787  ? 205 LEU A HA   1 
ATOM   3128 H HB2  . LEU A 1 205 ? 9.61600   -9.83600  33.39500  1.000 31.28968  ? 205 LEU A HB2  1 
ATOM   3129 H HB3  . LEU A 1 205 ? 11.16800  -10.08900 33.16600  1.000 31.28968  ? 205 LEU A HB3  1 
ATOM   3130 H HG   . LEU A 1 205 ? 10.26600  -7.95800  34.77000  1.000 32.32260  ? 205 LEU A HG   1 
ATOM   3131 H HD11 . LEU A 1 205 ? 10.62800  -9.25000  36.67300  1.000 35.30115  ? 205 LEU A HD11 1 
ATOM   3132 H HD12 . LEU A 1 205 ? 9.47300   -9.88600  35.78700  1.000 35.30115  ? 205 LEU A HD12 1 
ATOM   3133 H HD13 . LEU A 1 205 ? 10.93300  -10.51200 35.75700  1.000 35.30115  ? 205 LEU A HD13 1 
ATOM   3134 H HD21 . LEU A 1 205 ? 12.47300  -8.04800  35.68800  1.000 29.96894  ? 205 LEU A HD21 1 
ATOM   3135 H HD22 . LEU A 1 205 ? 12.84100  -9.15200  34.60600  1.000 29.96894  ? 205 LEU A HD22 1 
ATOM   3136 H HD23 . LEU A 1 205 ? 12.48500  -7.67400  34.14400  1.000 29.96894  ? 205 LEU A HD23 1 
ATOM   3137 N N    . ALA A 1 206 ? 9.27000   -9.62800  30.43900  1.000 26.28879  ? 206 ALA A N    1 
ATOM   3138 C CA   . ALA A 1 206 ? 9.16800   -10.28300 29.13500  1.000 28.50629  ? 206 ALA A CA   1 
ATOM   3139 C C    . ALA A 1 206 ? 9.67900   -9.37200  28.02000  1.000 25.88838  ? 206 ALA A C    1 
ATOM   3140 O O    . ALA A 1 206 ? 10.41600  -9.80100  27.10800  1.000 27.51652  ? 206 ALA A O    1 
ATOM   3141 C CB   . ALA A 1 206 ? 7.71200   -10.69500 28.88500  1.000 28.16662  ? 206 ALA A CB   1 
ATOM   3142 H H    . ALA A 1 206 ? 8.53200   -9.58200  30.87900  1.000 31.54735  ? 206 ALA A H    1 
ATOM   3143 H HA   . ALA A 1 206 ? 9.71200   -11.08600 29.14000  1.000 34.20835  ? 206 ALA A HA   1 
ATOM   3144 H HB1  . ALA A 1 206 ? 7.65600   -11.15600 28.03300  1.000 33.80075  ? 206 ALA A HB1  1 
ATOM   3145 H HB2  . ALA A 1 206 ? 7.42600   -11.28200 29.60000  1.000 33.80075  ? 206 ALA A HB2  1 
ATOM   3146 H HB3  . ALA A 1 206 ? 7.15700   -9.89900  28.86900  1.000 33.80075  ? 206 ALA A HB3  1 
ATOM   3147 N N    . TRP A 1 207 ? 9.31400   -8.10500  28.08600  1.000 24.03107  ? 207 TRP A N    1 
ATOM   3148 C CA   . TRP A 1 207 ? 9.73000   -7.15500  27.08100  1.000 26.76838  ? 207 TRP A CA   1 
ATOM   3149 C C    . TRP A 1 207 ? 11.23800  -6.89400  27.14000  1.000 27.67647  ? 207 TRP A C    1 
ATOM   3150 O O    . TRP A 1 207 ? 11.87400  -6.70700  26.09500  1.000 28.42936  ? 207 TRP A O    1 
ATOM   3151 C CB   . TRP A 1 207 ? 8.89200   -5.88500  27.28900  1.000 27.17243  ? 207 TRP A CB   1 
ATOM   3152 C CG   . TRP A 1 207 ? 9.24900   -4.69500  26.47900  1.000 26.76287  ? 207 TRP A CG   1 
ATOM   3153 C CD1  . TRP A 1 207 ? 8.87500   -4.42700  25.15700  1.000 29.21347  ? 207 TRP A CD1  1 
ATOM   3154 C CD2  . TRP A 1 207 ? 9.94900   -3.55800  26.93200  1.000 29.08546  ? 207 TRP A CD2  1 
ATOM   3155 N NE1  . TRP A 1 207 ? 9.35400   -3.18100  24.79300  1.000 30.60675  ? 207 TRP A NE1  1 
ATOM   3156 C CE2  . TRP A 1 207 ? 10.01500  -2.63700  25.85900  1.000 29.52172  ? 207 TRP A CE2  1 
ATOM   3157 C CE3  . TRP A 1 207 ? 10.56100  -3.22300  28.14200  1.000 30.12682  ? 207 TRP A CE3  1 
ATOM   3158 C CZ2  . TRP A 1 207 ? 10.66400  -1.40500  25.97900  1.000 32.24157  ? 207 TRP A CZ2  1 
ATOM   3159 C CZ3  . TRP A 1 207 ? 11.18700  -1.99200  28.25400  1.000 36.66724  ? 207 TRP A CZ3  1 
ATOM   3160 C CH2  . TRP A 1 207 ? 11.24700  -1.11100  27.17300  1.000 32.58668  ? 207 TRP A CH2  1 
ATOM   3161 H H    . TRP A 1 207 ? 8.82300   -7.77000  28.70700  1.000 28.83809  ? 207 TRP A H    1 
ATOM   3162 H HA   . TRP A 1 207 ? 9.52200   -7.51200  26.20300  1.000 32.12286  ? 207 TRP A HA   1 
ATOM   3163 H HB2  . TRP A 1 207 ? 7.96700   -6.09900  27.08800  1.000 32.60772  ? 207 TRP A HB2  1 
ATOM   3164 H HB3  . TRP A 1 207 ? 8.96400   -5.62700  28.22100  1.000 32.60772  ? 207 TRP A HB3  1 
ATOM   3165 H HD1  . TRP A 1 207 ? 8.38500   -4.99700  24.60900  1.000 35.05697  ? 207 TRP A HD1  1 
ATOM   3166 H HE1  . TRP A 1 207 ? 9.25900   -2.81300  24.02100  1.000 36.72890  ? 207 TRP A HE1  1 
ATOM   3167 H HE3  . TRP A 1 207 ? 10.52600  -3.80400  28.86700  1.000 36.15298  ? 207 TRP A HE3  1 
ATOM   3168 H HZ2  . TRP A 1 207 ? 10.70400  -0.81100  25.26500  1.000 38.69069  ? 207 TRP A HZ2  1 
ATOM   3169 H HZ3  . TRP A 1 207 ? 11.60300  -1.76200  29.05400  1.000 44.00149  ? 207 TRP A HZ3  1 
ATOM   3170 H HH2  . TRP A 1 207 ? 11.68600  -0.29700  27.27500  1.000 39.10482  ? 207 TRP A HH2  1 
ATOM   3171 N N    . LEU A 1 208 ? 11.85100  -6.89700  28.33900  1.000 27.49986  ? 208 LEU A N    1 
ATOM   3172 C CA   . LEU A 1 208 ? 13.30400  -6.76100  28.35900  1.000 28.27380  ? 208 LEU A CA   1 
ATOM   3173 C C    . LEU A 1 208 ? 13.94100  -7.97400  27.69200  1.000 28.17043  ? 208 LEU A C    1 
ATOM   3174 O O    . LEU A 1 208 ? 14.95000  -7.85600  26.98900  1.000 29.20451  ? 208 LEU A O    1 
ATOM   3175 C CB   . LEU A 1 208 ? 13.80300  -6.59700  29.80500  1.000 28.90754  ? 208 LEU A CB   1 
ATOM   3176 C CG   . LEU A 1 208 ? 13.37000  -5.29600  30.50600  1.000 27.86500  ? 208 LEU A CG   1 
ATOM   3177 C CD1  . LEU A 1 208 ? 13.80700  -5.30600  32.00500  1.000 29.20594  ? 208 LEU A CD1  1 
ATOM   3178 C CD2  . LEU A 1 208 ? 14.01600  -4.10100  29.80500  1.000 31.40995  ? 208 LEU A CD2  1 
ATOM   3179 H H    . LEU A 1 208 ? 11.46900  -6.97200  29.10600  1.000 33.00064  ? 208 LEU A H    1 
ATOM   3180 H HA   . LEU A 1 208 ? 13.55800  -5.97300  27.85500  1.000 33.92936  ? 208 LEU A HA   1 
ATOM   3181 H HB2  . LEU A 1 208 ? 13.46600  -7.33800  30.33200  1.000 34.68985  ? 208 LEU A HB2  1 
ATOM   3182 H HB3  . LEU A 1 208 ? 14.77300  -6.61700  29.80000  1.000 34.68985  ? 208 LEU A HB3  1 
ATOM   3183 H HG   . LEU A 1 208 ? 12.40600  -5.20200  30.46100  1.000 33.43880  ? 208 LEU A HG   1 
ATOM   3184 H HD11 . LEU A 1 208 ? 13.52300  -4.47800  32.42200  1.000 35.04792  ? 208 LEU A HD11 1 
ATOM   3185 H HD12 . LEU A 1 208 ? 13.39100  -6.06100  32.45000  1.000 35.04792  ? 208 LEU A HD12 1 
ATOM   3186 H HD13 . LEU A 1 208 ? 14.77300  -5.38600  32.05100  1.000 35.04792  ? 208 LEU A HD13 1 
ATOM   3187 H HD21 . LEU A 1 208 ? 13.86600  -3.30400  30.33800  1.000 37.69275  ? 208 LEU A HD21 1 
ATOM   3188 H HD22 . LEU A 1 208 ? 14.96800  -4.26500  29.71600  1.000 37.69275  ? 208 LEU A HD22 1 
ATOM   3189 H HD23 . LEU A 1 208 ? 13.61500  -3.99300  28.92800  1.000 37.69275  ? 208 LEU A HD23 1 
ATOM   3190 N N    . TYR A 1 209 ? 13.33500  -9.15500  27.88100  1.000 30.47412  ? 209 TYR A N    1 
ATOM   3191 C CA   . TYR A 1 209 ? 13.84500  -10.34600 27.19400  1.000 32.14934  ? 209 TYR A CA   1 
ATOM   3192 C C    . TYR A 1 209 ? 13.71600  -10.20700 25.66900  1.000 31.63673  ? 209 TYR A C    1 
ATOM   3193 O O    . TYR A 1 209 ? 14.64400  -10.58400 24.92500  1.000 32.54907  ? 209 TYR A O    1 
ATOM   3194 C CB   . TYR A 1 209 ? 13.13700  -11.61000 27.71500  1.000 27.20056  ? 209 TYR A CB   1 
ATOM   3195 C CG   . TYR A 1 209 ? 13.70800  -12.18800 29.02200  1.000 30.77109  ? 209 TYR A CG   1 
ATOM   3196 C CD1  . TYR A 1 209 ? 14.96500  -12.79000 29.06300  1.000 34.91067  ? 209 TYR A CD1  1 
ATOM   3197 C CD2  . TYR A 1 209 ? 12.96500  -12.13900 30.21400  1.000 33.42437  ? 209 TYR A CD2  1 
ATOM   3198 C CE1  . TYR A 1 209 ? 15.48200  -13.31500 30.26500  1.000 30.63579  ? 209 TYR A CE1  1 
ATOM   3199 C CE2  . TYR A 1 209 ? 13.46500  -12.67000 31.41500  1.000 28.79495  ? 209 TYR A CE2  1 
ATOM   3200 C CZ   . TYR A 1 209 ? 14.72600  -13.26600 31.42100  1.000 32.62174  ? 209 TYR A CZ   1 
ATOM   3201 O OH   . TYR A 1 209 ? 15.18300  -13.77600 32.61200  1.000 33.88240  ? 209 TYR A OH   1 
ATOM   3202 H H    . TYR A 1 209 ? 12.65100  -9.28900  28.38400  1.000 36.56974  ? 209 TYR A H    1 
ATOM   3203 H HA   . TYR A 1 209 ? 14.78900  -10.43700 27.39800  1.000 38.58001  ? 209 TYR A HA   1 
ATOM   3204 H HB2  . TYR A 1 209 ? 12.20400  -11.39800 27.87300  1.000 32.64147  ? 209 TYR A HB2  1 
ATOM   3205 H HB3  . TYR A 1 209 ? 13.20200  -12.30100 27.03700  1.000 32.64147  ? 209 TYR A HB3  1 
ATOM   3206 H HD1  . TYR A 1 209 ? 15.47700  -12.83300 28.28800  1.000 41.89360  ? 209 TYR A HD1  1 
ATOM   3207 H HD2  . TYR A 1 209 ? 12.12100  -11.74800 30.20700  1.000 40.11004  ? 209 TYR A HD2  1 
ATOM   3208 H HE1  . TYR A 1 209 ? 16.32000  -13.71700 30.27400  1.000 36.76375  ? 209 TYR A HE1  1 
ATOM   3209 H HE2  . TYR A 1 209 ? 12.95900  -12.63100 32.19400  1.000 34.55474  ? 209 TYR A HE2  1 
ATOM   3210 H HH   . TYR A 1 209 ? 15.95200  -14.09900 32.51000  1.000 40.65969  ? 209 TYR A HH   1 
ATOM   3211 N N    . ALA A 1 210 ? 12.58900  -9.66700  25.19100  1.000 32.91898  ? 210 ALA A N    1 
ATOM   3212 C CA   . ALA A 1 210 ? 12.44000  -9.36400  23.76100  1.000 31.87758  ? 210 ALA A CA   1 
ATOM   3213 C C    . ALA A 1 210 ? 13.54100  -8.42300  23.30100  1.000 34.90457  ? 210 ALA A C    1 
ATOM   3214 O O    . ALA A 1 210 ? 14.05700  -8.56400  22.18100  1.000 34.35660  ? 210 ALA A O    1 
ATOM   3215 C CB   . ALA A 1 210 ? 11.07400  -8.73300  23.45000  1.000 28.07042  ? 210 ALA A CB   1 
ATOM   3216 H H    . ALA A 1 210 ? 11.90200  -9.46800  25.66800  1.000 39.50358  ? 210 ALA A H    1 
ATOM   3217 H HA   . ALA A 1 210 ? 12.51500  -10.18700 23.25300  1.000 38.25390  ? 210 ALA A HA   1 
ATOM   3218 H HB1  . ALA A 1 210 ? 11.01400  -8.56400  22.49700  1.000 33.68530  ? 210 ALA A HB1  1 
ATOM   3219 H HB2  . ALA A 1 210 ? 10.37400  -9.34600  23.72200  1.000 33.68530  ? 210 ALA A HB2  1 
ATOM   3220 H HB3  . ALA A 1 210 ? 10.99300  -7.90000  23.94000  1.000 33.68530  ? 210 ALA A HB3  1 
ATOM   3221 N N    . ALA A 1 211 ? 13.91300  -7.44200  24.15300  1.000 29.68111  ? 211 ALA A N    1 
ATOM   3222 C CA   . ALA A 1 211 ? 14.99700  -6.53900  23.76600  1.000 30.66165  ? 211 ALA A CA   1 
ATOM   3223 C C    . ALA A 1 211 ? 16.31600  -7.28800  23.61500  1.000 35.09104  ? 211 ALA A C    1 
ATOM   3224 O O    . ALA A 1 211 ? 17.04200  -7.08300  22.63100  1.000 34.86448  ? 211 ALA A O    1 
ATOM   3225 C CB   . ALA A 1 211 ? 15.13200  -5.38000  24.76100  1.000 36.26422  ? 211 ALA A CB   1 
ATOM   3226 H H    . ALA A 1 211 ? 13.56500  -7.29000  24.92500  1.000 35.61814  ? 211 ALA A H    1 
ATOM   3227 H HA   . ALA A 1 211 ? 14.78100  -6.15500  22.90200  1.000 36.79478  ? 211 ALA A HA   1 
ATOM   3228 H HB1  . ALA A 1 211 ? 15.85600  -4.80100  24.47400  1.000 43.51787  ? 211 ALA A HB1  1 
ATOM   3229 H HB2  . ALA A 1 211 ? 14.29900  -4.88400  24.78200  1.000 43.51787  ? 211 ALA A HB2  1 
ATOM   3230 H HB3  . ALA A 1 211 ? 15.32500  -5.74000  25.64100  1.000 43.51787  ? 211 ALA A HB3  1 
ATOM   3231 N N    . VAL A 1 212 ? 16.63800  -8.18000  24.55800  1.000 32.25801  ? 212 VAL A N    1 
ATOM   3232 C CA   . VAL A 1 212 ? 17.87000  -8.95300  24.43600  1.000 35.63468  ? 212 VAL A CA   1 
ATOM   3233 C C    . VAL A 1 212 ? 17.81000  -9.85400  23.21200  1.000 40.68907  ? 212 VAL A C    1 
ATOM   3234 O O    . VAL A 1 212 ? 18.80300  -10.02400 22.49000  1.000 36.99326  ? 212 VAL A O    1 
ATOM   3235 C CB   . VAL A 1 212 ? 18.12800  -9.77100  25.71600  1.000 36.54772  ? 212 VAL A CB   1 
ATOM   3236 C CG1  . VAL A 1 212 ? 19.29900  -10.69200 25.52700  1.000 40.26945  ? 212 VAL A CG1  1 
ATOM   3237 C CG2  . VAL A 1 212 ? 18.31800  -8.86100  26.93100  1.000 34.50677  ? 212 VAL A CG2  1 
ATOM   3238 H H    . VAL A 1 212 ? 16.17100  -8.35100  25.26000  1.000 38.71041  ? 212 VAL A H    1 
ATOM   3239 H HA   . VAL A 1 212 ? 18.61400  -8.34500  24.31600  1.000 42.76241  ? 212 VAL A HA   1 
ATOM   3240 H HB   . VAL A 1 212 ? 17.35000  -10.32400 25.88700  1.000 43.85807  ? 212 VAL A HB   1 
ATOM   3241 H HG11 . VAL A 1 212 ? 19.61300  -10.98200 26.39800  1.000 48.32414  ? 212 VAL A HG11 1 
ATOM   3242 H HG12 . VAL A 1 212 ? 19.02000  -11.46000 25.00500  1.000 48.32414  ? 212 VAL A HG12 1 
ATOM   3243 H HG13 . VAL A 1 212 ? 20.00500  -10.21400 25.06500  1.000 48.32414  ? 212 VAL A HG13 1 
ATOM   3244 H HG21 . VAL A 1 212 ? 18.48600  -9.41000  27.71300  1.000 41.40892  ? 212 VAL A HG21 1 
ATOM   3245 H HG22 . VAL A 1 212 ? 19.07300  -8.27400  26.77000  1.000 41.40892  ? 212 VAL A HG22 1 
ATOM   3246 H HG23 . VAL A 1 212 ? 17.51300  -8.33600  27.06200  1.000 41.40892  ? 212 VAL A HG23 1 
ATOM   3247 N N    . ILE A 1 213 ? 16.64800  -10.46200 22.96000  1.000 34.52161  ? 213 ILE A N    1 
ATOM   3248 C CA   . ILE A 1 213 ? 16.52600  -11.32400 21.78400  1.000 39.76996  ? 213 ILE A CA   1 
ATOM   3249 C C    . ILE A 1 213 ? 16.77900  -10.53600 20.50200  1.000 36.09778  ? 213 ILE A C    1 
ATOM   3250 O O    . ILE A 1 213 ? 17.37300  -11.05000 19.55400  1.000 37.01485  ? 213 ILE A O    1 
ATOM   3251 C CB   . ILE A 1 213 ? 15.14100  -12.00300 21.77600  1.000 39.92180  ? 213 ILE A CB   1 
ATOM   3252 C CG1  . ILE A 1 213 ? 15.10200  -13.12600 22.83200  1.000 36.38406  ? 213 ILE A CG1  1 
ATOM   3253 C CG2  . ILE A 1 213 ? 14.80100  -12.51200 20.35400  1.000 40.36537  ? 213 ILE A CG2  1 
ATOM   3254 C CD1  . ILE A 1 213 ? 13.67400  -13.63900 23.11600  1.000 44.24940  ? 213 ILE A CD1  1 
ATOM   3255 H H    . ILE A 1 213 ? 15.93700  -10.39500 23.43900  1.000 41.42673  ? 213 ILE A H    1 
ATOM   3256 H HA   . ILE A 1 213 ? 17.19700  -12.02200 21.83900  1.000 47.72475  ? 213 ILE A HA   1 
ATOM   3257 H HB   . ILE A 1 213 ? 14.47900  -11.33800 22.02200  1.000 47.90696  ? 213 ILE A HB   1 
ATOM   3258 H HG12 . ILE A 1 213 ? 15.63100  -13.87500 22.51500  1.000 43.66167  ? 213 ILE A HG12 1 
ATOM   3259 H HG13 . ILE A 1 213 ? 15.47000  -12.78900 23.66400  1.000 43.66167  ? 213 ILE A HG13 1 
ATOM   3260 H HG21 . ILE A 1 213 ? 14.07800  -13.15500 20.41400  1.000 48.43924  ? 213 ILE A HG21 1 
ATOM   3261 H HG22 . ILE A 1 213 ? 14.52700  -11.76200 19.80300  1.000 48.43924  ? 213 ILE A HG22 1 
ATOM   3262 H HG23 . ILE A 1 213 ? 15.58600  -12.93700 19.97400  1.000 48.43924  ? 213 ILE A HG23 1 
ATOM   3263 H HD11 . ILE A 1 213 ? 13.70500  -14.26100 23.86000  1.000 53.10008  ? 213 ILE A HD11 1 
ATOM   3264 H HD12 . ILE A 1 213 ? 13.10700  -12.88400 23.33900  1.000 53.10008  ? 213 ILE A HD12 1 
ATOM   3265 H HD13 . ILE A 1 213 ? 13.33400  -14.08600 22.32500  1.000 53.10008  ? 213 ILE A HD13 1 
ATOM   3266 N N    . ASN A 1 214 ? 16.31700  -9.29000  20.44000  1.000 33.81377  ? 214 ASN A N    1 
ATOM   3267 C CA   . ASN A 1 214 ? 16.57900  -8.43700  19.29800  1.000 37.91830  ? 214 ASN A CA   1 
ATOM   3268 C C    . ASN A 1 214 ? 17.97800  -7.77700  19.36500  1.000 40.12751  ? 214 ASN A C    1 
ATOM   3269 O O    . ASN A 1 214 ? 18.26100  -6.88000  18.56400  1.000 44.59795  ? 214 ASN A O    1 
ATOM   3270 C CB   . ASN A 1 214 ? 15.48400  -7.37200  19.17200  1.000 36.43835  ? 214 ASN A CB   1 
ATOM   3271 C CG   . ASN A 1 214 ? 14.21200  -7.89300  18.46000  1.000 45.02052  ? 214 ASN A CG   1 
ATOM   3272 O OD1  . ASN A 1 214 ? 14.10200  -7.85800  17.21700  1.000 45.99510  ? 214 ASN A OD1  1 
ATOM   3273 N ND2  . ASN A 1 214 ? 13.24800  -8.35000  19.24200  1.000 41.61019  ? 214 ASN A ND2  1 
ATOM   3274 H H    . ASN A 1 214 ? 15.84600  -8.91700  21.05500  1.000 40.57732  ? 214 ASN A H    1 
ATOM   3275 H HA   . ASN A 1 214 ? 16.55100  -8.98000  18.49500  1.000 45.50277  ? 214 ASN A HA   1 
ATOM   3276 H HB2  . ASN A 1 214 ? 15.22900  -7.07500  20.06000  1.000 43.72683  ? 214 ASN A HB2  1 
ATOM   3277 H HB3  . ASN A 1 214 ? 15.82700  -6.62400  18.65900  1.000 43.72683  ? 214 ASN A HB3  1 
ATOM   3278 H HD21 . ASN A 1 214 ? 12.52000  -8.64900  18.89600  1.000 49.93303  ? 214 ASN A HD21 1 
ATOM   3279 H HD22 . ASN A 1 214 ? 13.35400  -8.35700  20.09500  1.000 49.93303  ? 214 ASN A HD22 1 
ATOM   3280 N N    . GLY A 1 215 ? 18.86900  -8.23100  20.25100  1.000 36.87022  ? 215 GLY A N    1 
ATOM   3281 C CA   . GLY A 1 215 ? 20.25700  -7.79800  20.20900  1.000 39.82504  ? 215 GLY A CA   1 
ATOM   3282 C C    . GLY A 1 215 ? 20.65300  -6.60800  21.04400  1.000 42.61169  ? 215 GLY A C    1 
ATOM   3283 O O    . GLY A 1 215 ? 21.75200  -6.05900  20.83600  1.000 45.69185  ? 215 GLY A O    1 
ATOM   3284 H H    . GLY A 1 215 ? 18.69100  -8.78700  20.88200  1.000 44.24507  ? 215 GLY A H    1 
ATOM   3285 H HA2  . GLY A 1 215 ? 20.81400  -8.54200  20.48700  1.000 47.79085  ? 215 GLY A HA2  1 
ATOM   3286 H HA3  . GLY A 1 215 ? 20.48500  -7.59300  19.28900  1.000 47.79085  ? 215 GLY A HA3  1 
ATOM   3287 N N    . ASP A 1 216 ? 19.82900  -6.20300  22.00300  1.000 36.07745  ? 216 ASP A N    1 
ATOM   3288 C CA   . ASP A 1 216 ? 20.13300  -5.08200  22.88000  1.000 37.88170  ? 216 ASP A CA   1 
ATOM   3289 C C    . ASP A 1 216 ? 20.47700  -5.59000  24.28800  1.000 41.21531  ? 216 ASP A C    1 
ATOM   3290 O O    . ASP A 1 216 ? 19.73500  -6.39000  24.86200  1.000 42.60064  ? 216 ASP A O    1 
ATOM   3291 C CB   . ASP A 1 216 ? 18.96700  -4.09400  22.91100  1.000 42.84044  ? 216 ASP A CB   1 
ATOM   3292 C CG   . ASP A 1 216 ? 19.40900  -2.65800  23.16800  1.000 49.75761  ? 216 ASP A CG   1 
ATOM   3293 O OD1  . ASP A 1 216 ? 20.59700  -2.45800  23.57500  1.000 58.74456  ? 216 ASP A OD1  1 
ATOM   3294 O OD2  . ASP A 1 216 ? 18.57000  -1.73200  22.94800  1.000 52.87175  ? 216 ASP A OD2  1 
ATOM   3295 H H    . ASP A 1 216 ? 19.07000  -6.57100  22.16800  1.000 43.29374  ? 216 ASP A H    1 
ATOM   3296 H HA   . ASP A 1 216 ? 20.90900  -4.61400  22.53600  1.000 45.45884  ? 216 ASP A HA   1 
ATOM   3297 H HB2  . ASP A 1 216 ? 18.51400  -4.11600  22.05400  1.000 51.40932  ? 216 ASP A HB2  1 
ATOM   3298 H HB3  . ASP A 1 216 ? 18.35400  -4.35000  23.61700  1.000 51.40932  ? 216 ASP A HB3  1 
ATOM   3299 N N    . ARG A 1 217 ? 21.64200  -5.20700  24.80400  1.000 38.92651  ? 217 ARG A N    1 
ATOM   3300 C CA   . ARG A 1 217 ? 22.07100  -5.64600  26.13000  1.000 39.27604  ? 217 ARG A CA   1 
ATOM   3301 C C    . ARG A 1 217 ? 22.51900  -4.48300  27.00400  1.000 38.61261  ? 217 ARG A C    1 
ATOM   3302 O O    . ARG A 1 217 ? 23.02500  -4.72700  28.11100  1.000 37.62320  ? 217 ARG A O    1 
ATOM   3303 C CB   . ARG A 1 217 ? 23.21600  -6.69100  26.06100  1.000 43.29736  ? 217 ARG A CB   1 
ATOM   3304 C CG   . ARG A 1 217 ? 22.79800  -8.00500  25.43000  1.000 44.93792  ? 217 ARG A CG   1 
ATOM   3305 C CD   . ARG A 1 217 ? 23.92900  -8.92200  25.23600  1.000 41.87207  ? 217 ARG A CD   1 
ATOM   3306 N NE   . ARG A 1 217 ? 24.59100  -9.22100  26.50500  1.000 47.60630  ? 217 ARG A NE   1 
ATOM   3307 C CZ   . ARG A 1 217 ? 24.39700  -10.32400 27.21900  1.000 48.66061  ? 217 ARG A CZ   1 
ATOM   3308 N NH1  . ARG A 1 217 ? 23.56900  -11.27700 26.80600  1.000 49.67968  ? 217 ARG A NH1  1 
ATOM   3309 N NH2  . ARG A 1 217 ? 25.05100  -10.47700 28.37200  1.000 45.10212  ? 217 ARG A NH2  1 
ATOM   3310 H H    . ARG A 1 217 ? 22.20400  -4.69200  24.40600  1.000 46.71261  ? 217 ARG A H    1 
ATOM   3311 H HA   . ARG A 1 217 ? 21.32100  -6.06800  26.57600  1.000 47.13205  ? 217 ARG A HA   1 
ATOM   3312 H HB2  . ARG A 1 217 ? 23.94200  -6.32500  25.53200  1.000 51.95763  ? 217 ARG A HB2  1 
ATOM   3313 H HB3  . ARG A 1 217 ? 23.52600  -6.87700  26.96100  1.000 51.95763  ? 217 ARG A HB3  1 
ATOM   3314 H HG2  . ARG A 1 217 ? 22.15200  -8.44200  26.00700  1.000 53.92630  ? 217 ARG A HG2  1 
ATOM   3315 H HG3  . ARG A 1 217 ? 22.40200  -7.82800  24.56200  1.000 53.92630  ? 217 ARG A HG3  1 
ATOM   3316 H HD2  . ARG A 1 217 ? 23.62200  -9.73800  24.83000  1.000 50.24728  ? 217 ARG A HD2  1 
ATOM   3317 H HD3  . ARG A 1 217 ? 24.58000  -8.49500  24.65800  1.000 50.24728  ? 217 ARG A HD3  1 
ATOM   3318 H HE   . ARG A 1 217 ? 25.14600  -8.64000  26.81100  1.000 57.12837  ? 217 ARG A HE   1 
ATOM   3319 H HH11 . ARG A 1 217 ? 23.14000  -11.19300 26.06700  1.000 59.61641  ? 217 ARG A HH11 1 
ATOM   3320 H HH12 . ARG A 1 217 ? 23.45900  -11.98300 27.28500  1.000 59.61641  ? 217 ARG A HH12 1 
ATOM   3321 H HH21 . ARG A 1 217 ? 25.59000  -9.86500  28.64500  1.000 54.12334  ? 217 ARG A HH21 1 
ATOM   3322 H HH22 . ARG A 1 217 ? 24.93400  -11.18800 28.84200  1.000 54.12334  ? 217 ARG A HH22 1 
ATOM   3323 N N    . TRP A 1 218 ? 22.33900  -3.22500  26.56000  1.000 35.30689  ? 218 TRP A N    1 
ATOM   3324 C CA   . TRP A 1 218 ? 22.97900  -2.11400  27.27700  1.000 38.62229  ? 218 TRP A CA   1 
ATOM   3325 C C    . TRP A 1 218 ? 22.48400  -1.98700  28.72500  1.000 33.08208  ? 218 TRP A C    1 
ATOM   3326 O O    . TRP A 1 218 ? 23.16700  -1.38600  29.55400  1.000 33.10134  ? 218 TRP A O    1 
ATOM   3327 C CB   . TRP A 1 218 ? 22.74000  -0.77900  26.54200  1.000 44.83478  ? 218 TRP A CB   1 
ATOM   3328 C CG   . TRP A 1 218 ? 21.29800  -0.23000  26.56100  1.000 39.78312  ? 218 TRP A CG   1 
ATOM   3329 C CD1  . TRP A 1 218 ? 20.34200  -0.28700  25.54100  1.000 38.79500  ? 218 TRP A CD1  1 
ATOM   3330 C CD2  . TRP A 1 218 ? 20.68200  0.50700   27.62900  1.000 39.91613  ? 218 TRP A CD2  1 
ATOM   3331 N NE1  . TRP A 1 218 ? 19.18300  0.35400   25.94900  1.000 39.84456  ? 218 TRP A NE1  1 
ATOM   3332 C CE2  . TRP A 1 218 ? 19.36200  0.84300   27.21500  1.000 42.24907  ? 218 TRP A CE2  1 
ATOM   3333 C CE3  . TRP A 1 218 ? 21.11700  0.91900   28.90000  1.000 41.58859  ? 218 TRP A CE3  1 
ATOM   3334 C CZ2  . TRP A 1 218 ? 18.48400  1.55900   28.03500  1.000 45.75004  ? 218 TRP A CZ2  1 
ATOM   3335 C CZ3  . TRP A 1 218 ? 20.23500  1.63100   29.70600  1.000 43.87222  ? 218 TRP A CZ3  1 
ATOM   3336 C CH2  . TRP A 1 218 ? 18.93800  1.93800   29.26700  1.000 44.15696  ? 218 TRP A CH2  1 
ATOM   3337 H H    . TRP A 1 218 ? 21.87100  -2.99800  25.87500  1.000 42.36907  ? 218 TRP A H    1 
ATOM   3338 H HA   . TRP A 1 218 ? 23.93600  -2.27000  27.30300  1.000 46.34755  ? 218 TRP A HA   1 
ATOM   3339 H HB2  . TRP A 1 218 ? 23.30900  -0.10500  26.94500  1.000 53.80254  ? 218 TRP A HB2  1 
ATOM   3340 H HB3  . TRP A 1 218 ? 22.99100  -0.89600  25.61200  1.000 53.80254  ? 218 TRP A HB3  1 
ATOM   3341 H HD1  . TRP A 1 218 ? 20.46000  -0.70200  24.72100  1.000 46.55480  ? 218 TRP A HD1  1 
ATOM   3342 H HE1  . TRP A 1 218 ? 18.46300  0.42500   25.48400  1.000 47.81427  ? 218 TRP A HE1  1 
ATOM   3343 H HE3  . TRP A 1 218 ? 21.97300  0.71200   29.19900  1.000 49.90711  ? 218 TRP A HE3  1 
ATOM   3344 H HZ2  . TRP A 1 218 ? 17.62500  1.77300   27.75100  1.000 54.90085  ? 218 TRP A HZ2  1 
ATOM   3345 H HZ3  . TRP A 1 218 ? 20.50600  1.90000   30.55400  1.000 52.64747  ? 218 TRP A HZ3  1 
ATOM   3346 H HH2  . TRP A 1 218 ? 18.37200  2.41500   29.83000  1.000 52.98915  ? 218 TRP A HH2  1 
ATOM   3347 N N    . PHE A 1 219 ? 21.29400  -2.48400  29.01700  1.000 32.05170  ? 219 PHE A N    1 
ATOM   3348 C CA   . PHE A 1 219 ? 20.67400  -2.29900  30.33300  1.000 34.00723  ? 219 PHE A CA   1 
ATOM   3349 C C    . PHE A 1 219 ? 20.91800  -3.44800  31.28600  1.000 37.60653  ? 219 PHE A C    1 
ATOM   3350 O O    . PHE A 1 219 ? 20.46600  -3.38700  32.43800  1.000 37.46360  ? 219 PHE A O    1 
ATOM   3351 C CB   . PHE A 1 219 ? 19.16800  -2.11500  30.17100  1.000 36.86345  ? 219 PHE A CB   1 
ATOM   3352 C CG   . PHE A 1 219 ? 18.54400  -3.16200  29.29800  1.000 34.23133  ? 219 PHE A CG   1 
ATOM   3353 C CD1  . PHE A 1 219 ? 18.18600  -4.38900  29.81800  1.000 34.22994  ? 219 PHE A CD1  1 
ATOM   3354 C CD2  . PHE A 1 219 ? 18.34800  -2.93000  27.94300  1.000 36.33414  ? 219 PHE A CD2  1 
ATOM   3355 C CE1  . PHE A 1 219 ? 17.62500  -5.35700  28.99400  1.000 30.37241  ? 219 PHE A CE1  1 
ATOM   3356 C CE2  . PHE A 1 219 ? 17.79300  -3.90900  27.12400  1.000 35.08085  ? 219 PHE A CE2  1 
ATOM   3357 C CZ   . PHE A 1 219 ? 17.42900  -5.11600  27.66000  1.000 30.54940  ? 219 PHE A CZ   1 
ATOM   3358 H H    . PHE A 1 219 ? 20.82700  -2.94600  28.46600  1.000 38.46284  ? 219 PHE A H    1 
ATOM   3359 H HA   . PHE A 1 219 ? 21.03000  -1.49400  30.73900  1.000 40.80947  ? 219 PHE A HA   1 
ATOM   3360 H HB2  . PHE A 1 219 ? 18.74800  -2.16400  31.04400  1.000 44.23694  ? 219 PHE A HB2  1 
ATOM   3361 H HB3  . PHE A 1 219 ? 18.99700  -1.24900  29.76900  1.000 44.23694  ? 219 PHE A HB3  1 
ATOM   3362 H HD1  . PHE A 1 219 ? 18.31300  -4.56500  30.72200  1.000 41.07674  ? 219 PHE A HD1  1 
ATOM   3363 H HD2  . PHE A 1 219 ? 18.59400  -2.11100  27.57700  1.000 43.60177  ? 219 PHE A HD2  1 
ATOM   3364 H HE1  . PHE A 1 219 ? 17.37900  -6.17900  29.35300  1.000 36.44770  ? 219 PHE A HE1  1 
ATOM   3365 H HE2  . PHE A 1 219 ? 17.65800  -3.74000  26.22000  1.000 42.09783  ? 219 PHE A HE2  1 
ATOM   3366 H HZ   . PHE A 1 219 ? 17.05200  -5.77200  27.11900  1.000 36.66008  ? 219 PHE A HZ   1 
ATOM   3367 N N    . LEU A 1 220 ? 21.55100  -4.52000  30.83200  1.000 36.63559  ? 220 LEU A N    1 
ATOM   3368 C CA   . LEU A 1 220 ? 21.90500  -5.60700  31.73200  1.000 35.93241  ? 220 LEU A CA   1 
ATOM   3369 C C    . LEU A 1 220 ? 22.96200  -5.16100  32.72900  1.000 41.73323  ? 220 LEU A C    1 
ATOM   3370 O O    . LEU A 1 220 ? 23.74600  -4.24800  32.47000  1.000 37.96821  ? 220 LEU A O    1 
ATOM   3371 C CB   . LEU A 1 220 ? 22.44900  -6.78700  30.92800  1.000 35.12108  ? 220 LEU A CB   1 
ATOM   3372 C CG   . LEU A 1 220 ? 21.42400  -7.27500  29.88300  1.000 32.85734  ? 220 LEU A CG   1 
ATOM   3373 C CD1  . LEU A 1 220 ? 22.07200  -8.41500  29.11900  1.000 39.54713  ? 220 LEU A CD1  1 
ATOM   3374 C CD2  . LEU A 1 220 ? 20.14700  -7.71800  30.55800  1.000 40.08453  ? 220 LEU A CD2  1 
ATOM   3375 H H    . LEU A 1 220 ? 21.78600  -4.64300  30.01400  1.000 43.96351  ? 220 LEU A H    1 
ATOM   3376 H HA   . LEU A 1 220 ? 21.12100  -5.89300  32.22600  1.000 43.11969  ? 220 LEU A HA   1 
ATOM   3377 H HB2  . LEU A 1 220 ? 23.25300  -6.51300  30.46100  1.000 42.14609  ? 220 LEU A HB2  1 
ATOM   3378 H HB3  . LEU A 1 220 ? 22.64400  -7.52200  31.53000  1.000 42.14609  ? 220 LEU A HB3  1 
ATOM   3379 H HG   . LEU A 1 220 ? 21.21900  -6.56000  29.26100  1.000 39.42961  ? 220 LEU A HG   1 
ATOM   3380 H HD11 . LEU A 1 220 ? 21.48900  -8.67800  28.39000  1.000 47.45735  ? 220 LEU A HD11 1 
ATOM   3381 H HD12 . LEU A 1 220 ? 22.92500  -8.11500  28.76900  1.000 47.45735  ? 220 LEU A HD12 1 
ATOM   3382 H HD13 . LEU A 1 220 ? 22.20700  -9.16200  29.72300  1.000 47.45735  ? 220 LEU A HD13 1 
ATOM   3383 H HD21 . LEU A 1 220 ? 19.61800  -8.23000  29.92600  1.000 48.10224  ? 220 LEU A HD21 1 
ATOM   3384 H HD22 . LEU A 1 220 ? 20.37100  -8.26900  31.32500  1.000 48.10224  ? 220 LEU A HD22 1 
ATOM   3385 H HD23 . LEU A 1 220 ? 19.65200  -6.93500  30.84600  1.000 48.10224  ? 220 LEU A HD23 1 
ATOM   3386 N N    . ASN A 1 221 ? 23.00600  -5.82000  33.88300  1.000 42.87909  ? 221 ASN A N    1 
ATOM   3387 C CA   . ASN A 1 221 ? 24.08500  -5.56100  34.82200  1.000 40.16084  ? 221 ASN A CA   1 
ATOM   3388 C C    . ASN A 1 221 ? 24.54500  -6.88200  35.42300  1.000 40.38380  ? 221 ASN A C    1 
ATOM   3389 O O    . ASN A 1 221 ? 23.96600  -7.94800  35.18300  1.000 42.20365  ? 221 ASN A O    1 
ATOM   3390 C CB   . ASN A 1 221 ? 23.69500  -4.56500  35.92600  1.000 42.06769  ? 221 ASN A CB   1 
ATOM   3391 C CG   . ASN A 1 221 ? 22.56800  -5.06600  36.82400  1.000 44.46428  ? 221 ASN A CG   1 
ATOM   3392 O OD1  . ASN A 1 221 ? 22.46100  -6.24300  37.11900  1.000 38.61084  ? 221 ASN A OD1  1 
ATOM   3393 N ND2  . ASN A 1 221 ? 21.72800  -4.14800  37.26800  1.000 45.37563  ? 221 ASN A ND2  1 
ATOM   3394 H H    . ASN A 1 221 ? 22.43500  -6.41000  34.14000  1.000 51.45571  ? 221 ASN A H    1 
ATOM   3395 H HA   . ASN A 1 221 ? 24.83800  -5.18400  34.34100  1.000 48.19381  ? 221 ASN A HA   1 
ATOM   3396 H HB2  . ASN A 1 221 ? 24.46900  -4.39700  36.48500  1.000 50.48203  ? 221 ASN A HB2  1 
ATOM   3397 H HB3  . ASN A 1 221 ? 23.40100  -3.73800  35.51300  1.000 50.48203  ? 221 ASN A HB3  1 
ATOM   3398 H HD21 . ASN A 1 221 ? 21.07400  -4.37400  37.77900  1.000 54.45156  ? 221 ASN A HD21 1 
ATOM   3399 H HD22 . ASN A 1 221 ? 21.83200  -3.32500  37.04300  1.000 54.45156  ? 221 ASN A HD22 1 
ATOM   3400 N N    . ARG A 1 222 ? 25.58800  -6.79400  36.22200  1.000 38.03187  ? 222 ARG A N    1 
ATOM   3401 C CA   . ARG A 1 222 ? 26.25000  -7.97200  36.75300  1.000 39.29775  ? 222 ARG A CA   1 
ATOM   3402 C C    . ARG A 1 222 ? 25.53100  -8.54800  37.94500  1.000 42.67542  ? 222 ARG A C    1 
ATOM   3403 O O    . ARG A 1 222 ? 26.04600  -9.50200  38.53800  1.000 44.25942  ? 222 ARG A O    1 
ATOM   3404 C CB   . ARG A 1 222 ? 27.69700  -7.62200  37.06900  1.000 41.98715  ? 222 ARG A CB   1 
ATOM   3405 C CG   . ARG A 1 222 ? 27.93300  -6.78900  38.34200  1.000 43.37547  ? 222 ARG A CG   1 
ATOM   3406 C CD   . ARG A 1 222 ? 29.46500  -6.69300  38.56700  1.000 48.01945  ? 222 ARG A CD   1 
ATOM   3407 N NE   . ARG A 1 222 ? 29.86000  -6.16800  39.86700  1.000 57.10923  ? 222 ARG A NE   1 
ATOM   3408 C CZ   . ARG A 1 222 ? 29.74000  -4.89700  40.23000  1.000 61.38320  ? 222 ARG A CZ   1 
ATOM   3409 N NH1  . ARG A 1 222 ? 29.16400  -4.00300  39.42400  1.000 60.80962  ? 222 ARG A NH1  1 
ATOM   3410 N NH2  . ARG A 1 222 ? 30.23900  -4.50600  41.41500  1.000 53.98380  ? 222 ARG A NH2  1 
ATOM   3411 H H    . ARG A 1 222 ? 25.94000  -6.05200  36.47800  1.000 45.63424  ? 222 ARG A H    1 
ATOM   3412 H HA   . ARG A 1 222 ? 26.26000  -8.65400  36.06400  1.000 47.15329  ? 222 ARG A HA   1 
ATOM   3413 H HB2  . ARG A 1 222 ? 28.19400  -8.44900  37.16800  1.000 50.38539  ? 222 ARG A HB2  1 
ATOM   3414 H HB3  . ARG A 1 222 ? 28.05800  -7.11700  36.32300  1.000 50.38539  ? 222 ARG A HB3  1 
ATOM   3415 H HG2  . ARG A 1 222 ? 27.57400  -5.89600  38.22500  1.000 52.05136  ? 222 ARG A HG2  1 
ATOM   3416 H HG3  . ARG A 1 222 ? 27.53300  -7.22700  39.10900  1.000 52.05136  ? 222 ARG A HG3  1 
ATOM   3417 H HD2  . ARG A 1 222 ? 29.84700  -7.58000  38.48200  1.000 57.62414  ? 222 ARG A HD2  1 
ATOM   3418 H HD3  . ARG A 1 222 ? 29.84100  -6.11000  37.88900  1.000 57.62414  ? 222 ARG A HD3  1 
ATOM   3419 H HE   . ARG A 1 222 ? 30.19300  -6.71800  40.43800  1.000 68.53187  ? 222 ARG A HE   1 
ATOM   3420 H HH11 . ARG A 1 222 ? 28.85100  -4.24600  38.66100  1.000 72.97235  ? 222 ARG A HH11 1 
ATOM   3421 H HH12 . ARG A 1 222 ? 29.09600  -3.18300  39.67300  1.000 72.97235  ? 222 ARG A HH12 1 
ATOM   3422 H HH21 . ARG A 1 222 ? 30.61200  -5.08100  41.93500  1.000 64.78136  ? 222 ARG A HH21 1 
ATOM   3423 H HH22 . ARG A 1 222 ? 30.16600  -3.68600  41.66300  1.000 64.78136  ? 222 ARG A HH22 1 
ATOM   3424 N N    . PHE A 1 223 ? 24.43800  -7.92500  38.37800  1.000 41.15487  ? 223 PHE A N    1 
ATOM   3425 C CA   . PHE A 1 223 ? 23.86700  -8.23900  39.68000  1.000 43.96617  ? 223 PHE A CA   1 
ATOM   3426 C C    . PHE A 1 223 ? 22.70200  -9.19600  39.54400  1.000 40.17935  ? 223 PHE A C    1 
ATOM   3427 O O    . PHE A 1 223 ? 22.10900  -9.35700  38.48800  1.000 39.81844  ? 223 PHE A O    1 
ATOM   3428 C CB   . PHE A 1 223 ? 23.40900  -6.99500  40.47100  1.000 40.18411  ? 223 PHE A CB   1 
ATOM   3429 C CG   . PHE A 1 223 ? 24.51000  -6.04600  40.77800  1.000 47.68342  ? 223 PHE A CG   1 
ATOM   3430 C CD1  . PHE A 1 223 ? 25.55400  -6.44600  41.57500  1.000 46.67236  ? 223 PHE A CD1  1 
ATOM   3431 C CD2  . PHE A 1 223 ? 24.50800  -4.76100  40.26000  1.000 48.14627  ? 223 PHE A CD2  1 
ATOM   3432 C CE1  . PHE A 1 223 ? 26.62100  -5.59200  41.84800  1.000 50.03834  ? 223 PHE A CE1  1 
ATOM   3433 C CE2  . PHE A 1 223 ? 25.57300  -3.88900  40.53300  1.000 51.82971  ? 223 PHE A CE2  1 
ATOM   3434 C CZ   . PHE A 1 223 ? 26.62400  -4.30700  41.32900  1.000 51.93023  ? 223 PHE A CZ   1 
ATOM   3435 H H    . PHE A 1 223 ? 24.01000  -7.32100  37.94000  1.000 49.38665  ? 223 PHE A H    1 
ATOM   3436 H HA   . PHE A 1 223 ? 24.54400  -8.68400  40.21300  1.000 52.76021  ? 223 PHE A HA   1 
ATOM   3437 H HB2  . PHE A 1 223 ? 22.74400  -6.52000  39.94900  1.000 48.22173  ? 223 PHE A HB2  1 
ATOM   3438 H HB3  . PHE A 1 223 ? 23.02200  -7.28400  41.31200  1.000 48.22173  ? 223 PHE A HB3  1 
ATOM   3439 H HD1  . PHE A 1 223 ? 25.56300  -7.31100  41.91500  1.000 56.00763  ? 223 PHE A HD1  1 
ATOM   3440 H HD2  . PHE A 1 223 ? 23.80800  -4.48200  39.71500  1.000 57.77632  ? 223 PHE A HD2  1 
ATOM   3441 H HE1  . PHE A 1 223 ? 27.32000  -5.87800  42.39100  1.000 60.04680  ? 223 PHE A HE1  1 
ATOM   3442 H HE2  . PHE A 1 223 ? 25.56900  -3.02700  40.18400  1.000 62.19646  ? 223 PHE A HE2  1 
ATOM   3443 H HZ   . PHE A 1 223 ? 27.32500  -3.72600  41.52200  1.000 62.31708  ? 223 PHE A HZ   1 
ATOM   3444 N N    . THR A 1 224 ? 22.42200  -9.86800  40.63500  1.000 39.30231  ? 224 THR A N    1 
ATOM   3445 C CA   . THR A 1 224 ? 21.19200  -10.59300 40.75100  1.000 38.55608  ? 224 THR A CA   1 
ATOM   3446 C C    . THR A 1 224 ? 20.48800  -10.09500 42.00600  1.000 44.23577  ? 224 THR A C    1 
ATOM   3447 O O    . THR A 1 224 ? 21.02500  -9.29500  42.78200  1.000 51.33720  ? 224 THR A O    1 
ATOM   3448 C CB   . THR A 1 224 ? 21.43300  -12.10000 40.79600  1.000 41.70841  ? 224 THR A CB   1 
ATOM   3449 O OG1  . THR A 1 224 ? 20.15900  -12.75300 40.67600  1.000 47.77814  ? 224 THR A OG1  1 
ATOM   3450 C CG2  . THR A 1 224 ? 22.09600  -12.48700 42.09900  1.000 50.29651  ? 224 THR A CG2  1 
ATOM   3451 H H    . THR A 1 224 ? 22.93300  -9.91800  41.32500  1.000 47.16358  ? 224 THR A H    1 
ATOM   3452 H HA   . THR A 1 224 ? 20.62400  -10.39900 39.98900  1.000 46.26810  ? 224 THR A HA   1 
ATOM   3453 H HB   . THR A 1 224 ? 22.00900  -12.36300 40.06100  1.000 50.05089  ? 224 THR A HB   1 
ATOM   3454 H HG1  . THR A 1 224 ? 19.81100  -12.84800 41.43400  1.000 57.33457  ? 224 THR A HG1  1 
ATOM   3455 H HG21 . THR A 1 224 ? 22.47100  -13.37900 42.02600  1.000 60.35661  ? 224 THR A HG21 1 
ATOM   3456 H HG22 . THR A 1 224 ? 22.80800  -11.86200 42.30700  1.000 60.35661  ? 224 THR A HG22 1 
ATOM   3457 H HG23 . THR A 1 224 ? 21.44800  -12.47700 42.82000  1.000 60.35661  ? 224 THR A HG23 1 
ATOM   3458 N N    . THR A 1 225 ? 19.29600  -10.60600 42.23600  1.000 37.93861  ? 225 THR A N    1 
ATOM   3459 C CA   . THR A 1 225 ? 18.52600  -10.15600 43.38100  1.000 42.23959  ? 225 THR A CA   1 
ATOM   3460 C C    . THR A 1 225 ? 17.76200  -11.35100 43.91400  1.000 40.67031  ? 225 THR A C    1 
ATOM   3461 O O    . THR A 1 225 ? 17.69400  -12.40500 43.27800  1.000 42.39086  ? 225 THR A O    1 
ATOM   3462 C CB   . THR A 1 225 ? 17.56300  -9.02600  42.99300  1.000 43.13290  ? 225 THR A CB   1 
ATOM   3463 O OG1  . THR A 1 225 ? 16.83800  -8.57700  44.15000  1.000 44.86130  ? 225 THR A OG1  1 
ATOM   3464 C CG2  . THR A 1 225 ? 16.56600  -9.49900  41.91900  1.000 40.46411  ? 225 THR A CG2  1 
ATOM   3465 H H    . THR A 1 225 ? 18.91000  -11.20300 41.75300  1.000 45.52713  ? 225 THR A H    1 
ATOM   3466 H HA   . THR A 1 225 ? 19.12000  -9.83400  44.07700  1.000 50.68831  ? 225 THR A HA   1 
ATOM   3467 H HB   . THR A 1 225 ? 18.07200  -8.28500  42.62800  1.000 51.76028  ? 225 THR A HB   1 
ATOM   3468 H HG1  . THR A 1 225 ? 16.22000  -9.11600  44.33100  1.000 53.83437  ? 225 THR A HG1  1 
ATOM   3469 H HG21 . THR A 1 225 ? 16.05500  -8.74400  41.58700  1.000 48.55773  ? 225 THR A HG21 1 
ATOM   3470 H HG22 . THR A 1 225 ? 17.04300  -9.90400  41.18000  1.000 48.55773  ? 225 THR A HG22 1 
ATOM   3471 H HG23 . THR A 1 225 ? 15.95400  -10.15100 42.29500  1.000 48.55773  ? 225 THR A HG23 1 
ATOM   3472 N N    . THR A 1 226 ? 17.16000  -11.17600 45.06900  1.000 39.50658  ? 226 THR A N    1 
ATOM   3473 C CA   . THR A 1 226 ? 16.20800  -12.18700 45.49800  1.000 41.95520  ? 226 THR A CA   1 
ATOM   3474 C C    . THR A 1 226 ? 14.81700  -11.74300 45.07600  1.000 37.17652  ? 226 THR A C    1 
ATOM   3475 O O    . THR A 1 226 ? 14.55400  -10.55900 44.81700  1.000 35.86314  ? 226 THR A O    1 
ATOM   3476 C CB   . THR A 1 226 ? 16.22300  -12.39300 47.02500  1.000 41.46471  ? 226 THR A CB   1 
ATOM   3477 O OG1  . THR A 1 226 ? 15.69400  -11.22600 47.66900  1.000 36.06668  ? 226 THR A OG1  1 
ATOM   3478 C CG2  . THR A 1 226 ? 17.63500  -12.71800 47.58800  1.000 38.59234  ? 226 THR A CG2  1 
ATOM   3479 H H    . THR A 1 226 ? 17.27300  -10.51400 45.60600  1.000 47.40870  ? 226 THR A H    1 
ATOM   3480 H HA   . THR A 1 226 ? 16.40400  -13.03700 45.07500  1.000 50.34705  ? 226 THR A HA   1 
ATOM   3481 H HB   . THR A 1 226 ? 15.64800  -13.14500 47.23600  1.000 49.75845  ? 226 THR A HB   1 
ATOM   3482 H HG1  . THR A 1 226 ? 15.69900  -11.33100 48.50200  1.000 43.28082  ? 226 THR A HG1  1 
ATOM   3483 H HG21 . THR A 1 226 ? 17.58700  -12.84500 48.54800  1.000 46.31161  ? 226 THR A HG21 1 
ATOM   3484 H HG22 . THR A 1 226 ? 17.97600  -13.52900 47.17900  1.000 46.31161  ? 226 THR A HG22 1 
ATOM   3485 H HG23 . THR A 1 226 ? 18.24400  -11.98800 47.39600  1.000 46.31161  ? 226 THR A HG23 1 
ATOM   3486 N N    . LEU A 1 227 ? 13.90700  -12.71400 44.99900  1.000 39.84515  ? 227 LEU A N    1 
ATOM   3487 C CA   . LEU A 1 227 ? 12.53000  -12.37300 44.67200  1.000 41.09476  ? 227 LEU A CA   1 
ATOM   3488 C C    . LEU A 1 227 ? 11.95000  -11.37100 45.66500  1.000 39.74024  ? 227 LEU A C    1 
ATOM   3489 O O    . LEU A 1 227 ? 11.25900  -10.41800 45.27800  1.000 38.20637  ? 227 LEU A O    1 
ATOM   3490 C CB   . LEU A 1 227 ? 11.68200  -13.64000 44.63200  1.000 41.50954  ? 227 LEU A CB   1 
ATOM   3491 C CG   . LEU A 1 227 ? 10.29600  -13.45100 44.02600  1.000 41.80428  ? 227 LEU A CG   1 
ATOM   3492 C CD1  . LEU A 1 227 ? 10.33900  -12.78800 42.64500  1.000 35.78263  ? 227 LEU A CD1  1 
ATOM   3493 C CD2  . LEU A 1 227 ? 9.61600   -14.80200 43.98600  1.000 46.66121  ? 227 LEU A CD2  1 
ATOM   3494 H H    . LEU A 1 227 ? 14.05700  -13.55100 45.12800  1.000 47.81498  ? 227 LEU A H    1 
ATOM   3495 H HA   . LEU A 1 227 ? 12.51800  -11.96400 43.79400  1.000 49.31451  ? 227 LEU A HA   1 
ATOM   3496 H HB2  . LEU A 1 227 ? 12.14600  -14.30800 44.10300  1.000 49.81225  ? 227 LEU A HB2  1 
ATOM   3497 H HB3  . LEU A 1 227 ? 11.56500  -13.96400 45.53900  1.000 49.81225  ? 227 LEU A HB3  1 
ATOM   3498 H HG   . LEU A 1 227 ? 9.77700   -12.87800 44.61100  1.000 50.16594  ? 227 LEU A HG   1 
ATOM   3499 H HD11 . LEU A 1 227 ? 9.47700   -12.90300 42.21500  1.000 42.93996  ? 227 LEU A HD11 1 
ATOM   3500 H HD12 . LEU A 1 227 ? 10.53000  -11.84300 42.75200  1.000 42.93996  ? 227 LEU A HD12 1 
ATOM   3501 H HD13 . LEU A 1 227 ? 11.03200  -13.21000 42.11400  1.000 42.93996  ? 227 LEU A HD13 1 
ATOM   3502 H HD21 . LEU A 1 227 ? 8.72900   -14.69700 43.60700  1.000 55.99425  ? 227 LEU A HD21 1 
ATOM   3503 H HD22 . LEU A 1 227 ? 10.14200  -15.40400 43.43600  1.000 55.99425  ? 227 LEU A HD22 1 
ATOM   3504 H HD23 . LEU A 1 227 ? 9.55200   -15.14900 44.88900  1.000 55.99425  ? 227 LEU A HD23 1 
ATOM   3505 N N    . ASN A 1 228 ? 12.18300  -11.57100 46.95400  1.000 41.41104  ? 228 ASN A N    1 
ATOM   3506 C CA   . ASN A 1 228 ? 11.53800  -10.66400 47.90300  1.000 41.69807  ? 228 ASN A CA   1 
ATOM   3507 C C    . ASN A 1 228 ? 12.13400  -9.26400  47.84600  1.000 42.08323  ? 228 ASN A C    1 
ATOM   3508 O O    . ASN A 1 228 ? 11.40000  -8.27800  47.97800  1.000 35.89595  ? 228 ASN A O    1 
ATOM   3509 C CB   . ASN A 1 228 ? 11.60700  -11.19900 49.32300  1.000 48.17148  ? 228 ASN A CB   1 
ATOM   3510 C CG   . ASN A 1 228 ? 10.66800  -10.42700 50.24800  1.000 58.02650  ? 228 ASN A CG   1 
ATOM   3511 O OD1  . ASN A 1 228 ? 9.44300   -10.39500 50.02500  1.000 56.21609  ? 228 ASN A OD1  1 
ATOM   3512 N ND2  . ASN A 1 228 ? 11.22900  -9.78300  51.26300  1.000 59.16192  ? 228 ASN A ND2  1 
ATOM   3513 H H    . ASN A 1 228 ? 12.67900  -12.18500 47.29400  1.000 49.69405  ? 228 ASN A H    1 
ATOM   3514 H HA   . ASN A 1 228 ? 10.60000  -10.59000 47.66700  1.000 50.03849  ? 228 ASN A HA   1 
ATOM   3515 H HB2  . ASN A 1 228 ? 11.34200  -12.13200 49.32800  1.000 57.80658  ? 228 ASN A HB2  1 
ATOM   3516 H HB3  . ASN A 1 228 ? 12.51200  -11.10400 49.65800  1.000 57.80658  ? 228 ASN A HB3  1 
ATOM   3517 H HD21 . ASN A 1 228 ? 10.74100  -9.33300  51.80900  1.000 70.99510  ? 228 ASN A HD21 1 
ATOM   3518 H HD22 . ASN A 1 228 ? 12.07900  -9.82500  51.38200  1.000 70.99510  ? 228 ASN A HD22 1 
ATOM   3519 N N    . ASP A 1 229 ? 13.46400  -9.15100  47.68800  1.000 38.27132  ? 229 ASP A N    1 
ATOM   3520 C CA   . ASP A 1 229 ? 14.05800  -7.82200  47.58400  1.000 38.82000  ? 229 ASP A CA   1 
ATOM   3521 C C    . ASP A 1 229 ? 13.58600  -7.10600  46.34300  1.000 38.15212  ? 229 ASP A C    1 
ATOM   3522 O O    . ASP A 1 229 ? 13.32500  -5.90000  46.38900  1.000 34.11510  ? 229 ASP A O    1 
ATOM   3523 C CB   . ASP A 1 229 ? 15.60000  -7.87100  47.59800  1.000 37.07654  ? 229 ASP A CB   1 
ATOM   3524 C CG   . ASP A 1 229 ? 16.15100  -8.20800  48.95000  1.000 41.79616  ? 229 ASP A CG   1 
ATOM   3525 O OD1  . ASP A 1 229 ? 15.40500  -8.04300  49.94600  1.000 41.44971  ? 229 ASP A OD1  1 
ATOM   3526 O OD2  . ASP A 1 229 ? 17.36000  -8.53800  49.04600  1.000 45.08898  ? 229 ASP A OD2  1 
ATOM   3527 H H    . ASP A 1 229 ? 14.01900  -9.80600  47.64000  1.000 45.92639  ? 229 ASP A H    1 
ATOM   3528 H HA   . ASP A 1 229 ? 13.77300  -7.29600  48.34800  1.000 46.58480  ? 229 ASP A HA   1 
ATOM   3529 H HB2  . ASP A 1 229 ? 15.90100  -8.54900  46.97300  1.000 44.49265  ? 229 ASP A HB2  1 
ATOM   3530 H HB3  . ASP A 1 229 ? 15.94700  -7.00300  47.34000  1.000 44.49265  ? 229 ASP A HB3  1 
ATOM   3531 N N    . PHE A 1 230 ? 13.48100  -7.81700  45.21000  1.000 33.78849  ? 230 PHE A N    1 
ATOM   3532 C CA   . PHE A 1 230 ? 12.93500  -7.16900  44.03300  1.000 37.53690  ? 230 PHE A CA   1 
ATOM   3533 C C    . PHE A 1 230 ? 11.52800  -6.64400  44.29300  1.000 38.18139  ? 230 PHE A C    1 
ATOM   3534 O O    . PHE A 1 230 ? 11.19800  -5.52000  43.92200  1.000 33.27683  ? 230 PHE A O    1 
ATOM   3535 C CB   . PHE A 1 230 ? 12.90500  -8.12000  42.85100  1.000 36.41873  ? 230 PHE A CB   1 
ATOM   3536 C CG   . PHE A 1 230 ? 12.18200  -7.55100  41.67900  1.000 33.93068  ? 230 PHE A CG   1 
ATOM   3537 C CD1  . PHE A 1 230 ? 12.80500  -6.63500  40.85200  1.000 34.09594  ? 230 PHE A CD1  1 
ATOM   3538 C CD2  . PHE A 1 230 ? 10.86700  -7.91500  41.40700  1.000 34.32847  ? 230 PHE A CD2  1 
ATOM   3539 C CE1  . PHE A 1 230 ? 12.11800  -6.10300  39.75700  1.000 33.98631  ? 230 PHE A CE1  1 
ATOM   3540 C CE2  . PHE A 1 230 ? 10.18300  -7.37500  40.31900  1.000 33.34485  ? 230 PHE A CE2  1 
ATOM   3541 C CZ   . PHE A 1 230 ? 10.82900  -6.48900  39.48400  1.000 33.69097  ? 230 PHE A CZ   1 
ATOM   3542 H H    . PHE A 1 230 ? 13.71100  -8.64000  45.10800  1.000 40.54699  ? 230 PHE A H    1 
ATOM   3543 H HA   . PHE A 1 230 ? 13.49800  -6.41500  43.79800  1.000 45.04508  ? 230 PHE A HA   1 
ATOM   3544 H HB2  . PHE A 1 230 ? 13.81500  -8.31400  42.57800  1.000 43.70327  ? 230 PHE A HB2  1 
ATOM   3545 H HB3  . PHE A 1 230 ? 12.45500  -8.93800  43.11400  1.000 43.70327  ? 230 PHE A HB3  1 
ATOM   3546 H HD1  . PHE A 1 230 ? 13.68400  -6.38100  41.01800  1.000 40.91593  ? 230 PHE A HD1  1 
ATOM   3547 H HD2  . PHE A 1 230 ? 10.43700  -8.52600  41.96100  1.000 41.19496  ? 230 PHE A HD2  1 
ATOM   3548 H HE1  . PHE A 1 230 ? 12.54500  -5.49500  39.19700  1.000 40.78437  ? 230 PHE A HE1  1 
ATOM   3549 H HE2  . PHE A 1 230 ? 9.30900   -7.63600  40.14100  1.000 40.01463  ? 230 PHE A HE2  1 
ATOM   3550 H HZ   . PHE A 1 230 ? 10.37700  -6.11900  38.76000  1.000 40.42996  ? 230 PHE A HZ   1 
ATOM   3551 N N    . ASN A 1 231 ? 10.67300  -7.45200  44.91500  1.000 34.42716  ? 231 ASN A N    1 
ATOM   3552 C CA   . ASN A 1 231 ? 9.31500   -6.98900  45.17800  1.000 33.93509  ? 231 ASN A CA   1 
ATOM   3553 C C    . ASN A 1 231 ? 9.28100   -5.77700  46.10900  1.000 37.90709  ? 231 ASN A C    1 
ATOM   3554 O O    . ASN A 1 231 ? 8.47700   -4.85600  45.89200  1.000 38.54473  ? 231 ASN A O    1 
ATOM   3555 C CB   . ASN A 1 231 ? 8.49500   -8.16100  45.70100  1.000 37.65239  ? 231 ASN A CB   1 
ATOM   3556 C CG   . ASN A 1 231 ? 8.04500   -9.04300  44.56100  1.000 37.76447  ? 231 ASN A CG   1 
ATOM   3557 O OD1  . ASN A 1 231 ? 7.77000   -8.53100  43.48500  1.000 40.34951  ? 231 ASN A OD1  1 
ATOM   3558 N ND2  . ASN A 1 231 ? 8.03500   -10.35200 44.75300  1.000 40.52965  ? 231 ASN A ND2  1 
ATOM   3559 H H    . ASN A 1 231 ? 10.84700  -8.24900  45.18700  1.000 41.31339  ? 231 ASN A H    1 
ATOM   3560 H HA   . ASN A 1 231 ? 8.92300   -6.70700  44.33700  1.000 40.72291  ? 231 ASN A HA   1 
ATOM   3561 H HB2  . ASN A 1 231 ? 9.03800   -8.69200  46.30400  1.000 45.18367  ? 231 ASN A HB2  1 
ATOM   3562 H HB3  . ASN A 1 231 ? 7.70800   -7.82600  46.15900  1.000 45.18367  ? 231 ASN A HB3  1 
ATOM   3563 H HD21 . ASN A 1 231 ? 7.78900   -10.87800 44.11800  1.000 48.63638  ? 231 ASN A HD21 1 
ATOM   3564 H HD22 . ASN A 1 231 ? 8.24700   -10.67500 45.52100  1.000 48.63638  ? 231 ASN A HD22 1 
ATOM   3565 N N    . LEU A 1 232 ? 10.19400  -5.69800  47.07800  1.000 37.61096  ? 232 LEU A N    1 
ATOM   3566 C CA   . LEU A 1 232 ? 10.25300  -4.50500  47.92000  1.000 37.77286  ? 232 LEU A CA   1 
ATOM   3567 C C    . LEU A 1 232 ? 10.58300  -3.26700  47.10700  1.000 38.27594  ? 232 LEU A C    1 
ATOM   3568 O O    . LEU A 1 232 ? 10.01800  -2.19100  47.33500  1.000 34.30272  ? 232 LEU A O    1 
ATOM   3569 C CB   . LEU A 1 232 ? 11.26500  -4.69100  49.04100  1.000 39.19476  ? 232 LEU A CB   1 
ATOM   3570 C CG   . LEU A 1 232 ? 10.84500  -5.74000  50.07900  1.000 40.43825  ? 232 LEU A CG   1 
ATOM   3571 C CD1  . LEU A 1 232 ? 11.98800  -5.97500  50.99800  1.000 39.79787  ? 232 LEU A CD1  1 
ATOM   3572 C CD2  . LEU A 1 232 ? 9.62200   -5.20400  50.83600  1.000 44.16943  ? 232 LEU A CD2  1 
ATOM   3573 H H    . LEU A 1 232 ? 10.77500  -6.30400  47.26400  1.000 45.13396  ? 232 LEU A H    1 
ATOM   3574 H HA   . LEU A 1 232 ? 9.38100   -4.36400  48.31900  1.000 45.32824  ? 232 LEU A HA   1 
ATOM   3575 H HB2  . LEU A 1 232 ? 12.10900  -4.97500  48.65600  1.000 47.03452  ? 232 LEU A HB2  1 
ATOM   3576 H HB3  . LEU A 1 232 ? 11.38200  -3.84500  49.50100  1.000 47.03452  ? 232 LEU A HB3  1 
ATOM   3577 H HG   . LEU A 1 232 ? 10.61000  -6.57200  49.64000  1.000 48.52670  ? 232 LEU A HG   1 
ATOM   3578 H HD11 . LEU A 1 232 ? 11.72700  -6.62900  51.66500  1.000 47.75824  ? 232 LEU A HD11 1 
ATOM   3579 H HD12 . LEU A 1 232 ? 12.74100  -6.30800  50.48600  1.000 47.75824  ? 232 LEU A HD12 1 
ATOM   3580 H HD13 . LEU A 1 232 ? 12.22400  -5.13800  51.42800  1.000 47.75824  ? 232 LEU A HD13 1 
ATOM   3581 H HD21 . LEU A 1 232 ? 9.49500   -5.73100  51.64100  1.000 53.00411  ? 232 LEU A HD21 1 
ATOM   3582 H HD22 . LEU A 1 232 ? 9.77700   -4.27600  51.07000  1.000 53.00411  ? 232 LEU A HD22 1 
ATOM   3583 H HD23 . LEU A 1 232 ? 8.84000   -5.27600  50.26700  1.000 53.00411  ? 232 LEU A HD23 1 
ATOM   3584 N N    . VAL A 1 233 ? 11.51500  -3.38700  46.16400  1.000 35.38180  ? 233 VAL A N    1 
ATOM   3585 C CA   . VAL A 1 233 ? 11.82200  -2.24700  45.31500  1.000 33.66847  ? 233 VAL A CA   1 
ATOM   3586 C C    . VAL A 1 233 ? 10.67600  -1.97000  44.36100  1.000 33.38832  ? 233 VAL A C    1 
ATOM   3587 O O    . VAL A 1 233 ? 10.27900  -0.81700  44.16200  1.000 36.42289  ? 233 VAL A O    1 
ATOM   3588 C CB   . VAL A 1 233 ? 13.12400  -2.49800  44.53100  1.000 37.29304  ? 233 VAL A CB   1 
ATOM   3589 C CG1  . VAL A 1 233 ? 13.36400  -1.34200  43.55100  1.000 47.17497  ? 233 VAL A CG1  1 
ATOM   3590 C CG2  . VAL A 1 233 ? 14.24600  -2.65800  45.45200  1.000 35.20299  ? 233 VAL A CG2  1 
ATOM   3591 H H    . VAL A 1 233 ? 11.97100  -4.09800  46.00100  1.000 42.45896  ? 233 VAL A H    1 
ATOM   3592 H HA   . VAL A 1 233 ? 11.95000  -1.46200  45.87000  1.000 40.40296  ? 233 VAL A HA   1 
ATOM   3593 H HB   . VAL A 1 233 ? 13.03400  -3.31600  44.01800  1.000 44.75245  ? 233 VAL A HB   1 
ATOM   3594 H HG11 . VAL A 1 233 ? 14.31200  -1.14300  43.52500  1.000 56.61077  ? 233 VAL A HG11 1 
ATOM   3595 H HG12 . VAL A 1 233 ? 13.05200  -1.60200  42.67000  1.000 56.61077  ? 233 VAL A HG12 1 
ATOM   3596 H HG13 . VAL A 1 233 ? 12.88100  -0.55900  43.85900  1.000 56.61077  ? 233 VAL A HG13 1 
ATOM   3597 H HG21 . VAL A 1 233 ? 15.06000  -2.77900  44.93900  1.000 42.24439  ? 233 VAL A HG21 1 
ATOM   3598 H HG22 . VAL A 1 233 ? 14.31700  -1.86300  46.00200  1.000 42.24439  ? 233 VAL A HG22 1 
ATOM   3599 H HG23 . VAL A 1 233 ? 14.08900  -3.43500  46.01100  1.000 42.24439  ? 233 VAL A HG23 1 
ATOM   3600 N N    . ALA A 1 234 ? 10.11900  -3.01800  43.75000  1.000 36.61268  ? 234 ALA A N    1 
ATOM   3601 C CA   . ALA A 1 234 ? 9.14200   -2.79200  42.67600  1.000 40.16437  ? 234 ALA A CA   1 
ATOM   3602 C C    . ALA A 1 234 ? 7.91600   -2.06400  43.19800  1.000 38.16861  ? 234 ALA A C    1 
ATOM   3603 O O    . ALA A 1 234 ? 7.40400   -1.15200  42.53600  1.000 37.11636  ? 234 ALA A O    1 
ATOM   3604 C CB   . ALA A 1 234 ? 8.72500   -4.11000  42.02000  1.000 40.93095  ? 234 ALA A CB   1 
ATOM   3605 H H    . ALA A 1 234 ? 10.28100  -3.84300  43.92900  1.000 43.93601  ? 234 ALA A H    1 
ATOM   3606 H HA   . ALA A 1 234 ? 9.55000   -2.23600  41.99400  1.000 48.19804  ? 234 ALA A HA   1 
ATOM   3607 H HB1  . ALA A 1 234 ? 8.10800   -3.92600  41.29600  1.000 49.11794  ? 234 ALA A HB1  1 
ATOM   3608 H HB2  . ALA A 1 234 ? 9.51600   -4.55200  41.67500  1.000 49.11794  ? 234 ALA A HB2  1 
ATOM   3609 H HB3  . ALA A 1 234 ? 8.29800   -4.67100  42.68600  1.000 49.11794  ? 234 ALA A HB3  1 
ATOM   3610 N N    . MET A 1 235 ? 7.43500   -2.45600  44.38200  1.000 40.96820  ? 235 MET A N    1 
ATOM   3611 C CA   . MET A 1 235 ? 6.30100   -1.79100  45.00600  1.000 44.25044  ? 235 MET A CA   1 
ATOM   3612 C C    . MET A 1 235 ? 6.50600   -0.29000  45.12700  1.000 43.14709  ? 235 MET A C    1 
ATOM   3613 O O    . MET A 1 235 ? 5.54000   0.47300   45.03200  1.000 38.49051  ? 235 MET A O    1 
ATOM   3614 C CB   . MET A 1 235 ? 6.03700   -2.37300  46.39900  1.000 47.47835  ? 235 MET A CB   1 
ATOM   3615 C CG   . MET A 1 235 ? 5.81800   -3.88900  46.44900  1.000 65.15035  ? 235 MET A CG   1 
ATOM   3616 S SD   . MET A 1 235 ? 4.49100   -4.52000  45.38000  1.000 89.89293  ? 235 MET A SD   1 
ATOM   3617 C CE   . MET A 1 235 ? 3.05100   -3.61700  46.01000  1.000 70.32042  ? 235 MET A CE   1 
ATOM   3618 H H    . MET A 1 235 ? 7.75500   -3.10800  44.84200  1.000 49.16264  ? 235 MET A H    1 
ATOM   3619 H HA   . MET A 1 235 ? 5.51200   -1.95300  44.46500  1.000 53.10132  ? 235 MET A HA   1 
ATOM   3620 H HB2  . MET A 1 235 ? 6.79800   -2.17000  46.96500  1.000 56.97483  ? 235 MET A HB2  1 
ATOM   3621 H HB3  . MET A 1 235 ? 5.24200   -1.95200  46.76200  1.000 56.97483  ? 235 MET A HB3  1 
ATOM   3622 H HG2  . MET A 1 235 ? 6.60800   -4.33100  46.16900  1.000 78.18122  ? 235 MET A HG2  1 
ATOM   3623 H HG3  . MET A 1 235 ? 5.60700   -4.14200  47.36100  1.000 78.18122  ? 235 MET A HG3  1 
ATOM   3624 H HE1  . MET A 1 235 ? 2.25700   -3.92500  45.54600  1.000 84.38530  ? 235 MET A HE1  1 
ATOM   3625 H HE2  . MET A 1 235 ? 2.96400   -3.78800  46.96100  1.000 84.38530  ? 235 MET A HE2  1 
ATOM   3626 H HE3  . MET A 1 235 ? 3.18100   -2.66800  45.85500  1.000 84.38530  ? 235 MET A HE3  1 
ATOM   3627 N N    . LYS A 1 236 ? 7.74200   0.15700   45.34700  1.000 36.17452  ? 236 LYS A N    1 
ATOM   3628 C CA   . LYS A 1 236 ? 7.97600   1.58300   45.53600  1.000 35.53066  ? 236 LYS A CA   1 
ATOM   3629 C C    . LYS A 1 236 ? 7.78300   2.36000   44.25800  1.000 38.14971  ? 236 LYS A C    1 
ATOM   3630 O O    . LYS A 1 236 ? 7.75400   3.59700   44.29000  1.000 38.30447  ? 236 LYS A O    1 
ATOM   3631 C CB   . LYS A 1 236 ? 9.37300   1.81800   46.08500  1.000 37.96373  ? 236 LYS A CB   1 
ATOM   3632 C CG   . LYS A 1 236 ? 9.56600   1.08400   47.41800  1.000 40.19289  ? 236 LYS A CG   1 
ATOM   3633 C CD   . LYS A 1 236 ? 10.89000  1.40500   48.11300  1.000 44.71730  ? 236 LYS A CD   1 
ATOM   3634 C CE   . LYS A 1 236 ? 11.03700  0.48900   49.30900  1.000 42.24042  ? 236 LYS A CE   1 
ATOM   3635 N NZ   . LYS A 1 236 ? 12.34800  0.57100   50.01600  1.000 48.53852  ? 236 LYS A NZ   1 
ATOM   3636 H H    . LYS A 1 236 ? 8.44600   -0.33400  45.39000  1.000 43.41023  ? 236 LYS A H    1 
ATOM   3637 H HA   . LYS A 1 236 ? 7.34100   1.92000   46.18700  1.000 42.63760  ? 236 LYS A HA   1 
ATOM   3638 H HB2  . LYS A 1 236 ? 10.02800  1.48300   45.45300  1.000 45.55727  ? 236 LYS A HB2  1 
ATOM   3639 H HB3  . LYS A 1 236 ? 9.50400   2.76700   46.23600  1.000 45.55727  ? 236 LYS A HB3  1 
ATOM   3640 H HG2  . LYS A 1 236 ? 8.84700   1.33400   48.01900  1.000 48.23227  ? 236 LYS A HG2  1 
ATOM   3641 H HG3  . LYS A 1 236 ? 9.54000   0.12900   47.25500  1.000 48.23227  ? 236 LYS A HG3  1 
ATOM   3642 H HD2  . LYS A 1 236 ? 11.62900  1.24700   47.50400  1.000 53.66156  ? 236 LYS A HD2  1 
ATOM   3643 H HD3  . LYS A 1 236 ? 10.88600  2.32500   48.42100  1.000 53.66156  ? 236 LYS A HD3  1 
ATOM   3644 H HE2  . LYS A 1 236 ? 10.34500  0.70900   49.95200  1.000 50.68931  ? 236 LYS A HE2  1 
ATOM   3645 H HE3  . LYS A 1 236 ? 10.92400  -0.42700  49.01100  1.000 50.68931  ? 236 LYS A HE3  1 
ATOM   3646 H HZ1  . LYS A 1 236 ? 12.33900  0.04800   50.73600  1.000 58.24702  ? 236 LYS A HZ1  1 
ATOM   3647 H HZ2  . LYS A 1 236 ? 13.00200  0.30600   49.47400  1.000 58.24702  ? 236 LYS A HZ2  1 
ATOM   3648 H HZ3  . LYS A 1 236 ? 12.50400  1.41000   50.26900  1.000 58.24702  ? 236 LYS A HZ3  1 
ATOM   3649 N N    . TYR A 1 237 ? 7.75800   1.67600   43.12300  1.000 31.48502  ? 237 TYR A N    1 
ATOM   3650 C CA   . TYR A 1 237 ? 7.46600   2.31400   41.85500  1.000 35.15292  ? 237 TYR A CA   1 
ATOM   3651 C C    . TYR A 1 237 ? 6.07300   1.96600   41.34900  1.000 37.09749  ? 237 TYR A C    1 
ATOM   3652 O O    . TYR A 1 237 ? 5.79900   2.14700   40.16000  1.000 34.09559  ? 237 TYR A O    1 
ATOM   3653 C CB   . TYR A 1 237 ? 8.49800   1.92100   40.81700  1.000 34.91546  ? 237 TYR A CB   1 
ATOM   3654 C CG   . TYR A 1 237 ? 9.90600   2.36300   41.15200  1.000 35.36185  ? 237 TYR A CG   1 
ATOM   3655 C CD1  . TYR A 1 237 ? 10.72200  1.59100   41.95200  1.000 38.21011  ? 237 TYR A CD1  1 
ATOM   3656 C CD2  . TYR A 1 237 ? 10.40800  3.56600   40.66800  1.000 35.95645  ? 237 TYR A CD2  1 
ATOM   3657 C CE1  . TYR A 1 237 ? 12.06200  1.99500   42.22600  1.000 40.85364  ? 237 TYR A CE1  1 
ATOM   3658 C CE2  . TYR A 1 237 ? 11.71200  3.97400   40.90500  1.000 39.24354  ? 237 TYR A CE2  1 
ATOM   3659 C CZ   . TYR A 1 237 ? 12.54400  3.19400   41.68500  1.000 40.58706  ? 237 TYR A CZ   1 
ATOM   3660 O OH   . TYR A 1 237 ? 13.82700  3.63200   41.92000  1.000 43.52200  ? 237 TYR A OH   1 
ATOM   3661 H H    . TYR A 1 237 ? 7.91000   0.83200   43.06100  1.000 37.78283  ? 237 TYR A H    1 
ATOM   3662 H HA   . TYR A 1 237 ? 7.50900   3.27600   41.96400  1.000 42.18430  ? 237 TYR A HA   1 
ATOM   3663 H HB2  . TYR A 1 237 ? 8.50300   0.95500   40.73200  1.000 41.89935  ? 237 TYR A HB2  1 
ATOM   3664 H HB3  . TYR A 1 237 ? 8.25700   2.32300   39.96800  1.000 41.89935  ? 237 TYR A HB3  1 
ATOM   3665 H HD1  . TYR A 1 237 ? 10.40800  0.78100   42.28500  1.000 45.85293  ? 237 TYR A HD1  1 
ATOM   3666 H HD2  . TYR A 1 237 ? 9.87000   4.08600   40.11600  1.000 43.14854  ? 237 TYR A HD2  1 
ATOM   3667 H HE1  . TYR A 1 237 ? 12.61400  1.46300   42.75200  1.000 49.02517  ? 237 TYR A HE1  1 
ATOM   3668 H HE2  . TYR A 1 237 ? 12.02100  4.77800   40.55300  1.000 47.09305  ? 237 TYR A HE2  1 
ATOM   3669 H HH   . TYR A 1 237 ? 13.95800  4.36300   41.52700  1.000 52.22720  ? 237 TYR A HH   1 
ATOM   3670 N N    . ASN A 1 238 ? 5.19400   1.46700   42.23200  1.000 34.76243  ? 238 ASN A N    1 
ATOM   3671 C CA   . ASN A 1 238 ? 3.82100   1.05000   41.87200  1.000 35.21167  ? 238 ASN A CA   1 
ATOM   3672 C C    . ASN A 1 238 ? 3.82400   -0.04100  40.79700  1.000 34.93944  ? 238 ASN A C    1 
ATOM   3673 O O    . ASN A 1 238 ? 2.95300   -0.08300  39.90400  1.000 33.73322  ? 238 ASN A O    1 
ATOM   3674 C CB   . ASN A 1 238 ? 2.96600   2.23500   41.43700  1.000 39.45392  ? 238 ASN A CB   1 
ATOM   3675 C CG   . ASN A 1 238 ? 2.26600   2.88100   42.60400  1.000 48.86769  ? 238 ASN A CG   1 
ATOM   3676 O OD1  . ASN A 1 238 ? 2.58400   2.59600   43.76400  1.000 48.98689  ? 238 ASN A OD1  1 
ATOM   3677 N ND2  . ASN A 1 238 ? 1.28800   3.73700   42.31500  1.000 54.00313  ? 238 ASN A ND2  1 
ATOM   3678 H H    . ASN A 1 238 ? 5.37000   1.35700   43.06600  1.000 41.71571  ? 238 ASN A H    1 
ATOM   3679 H HA   . ASN A 1 238 ? 3.40600   0.66700   42.66000  1.000 42.25480  ? 238 ASN A HA   1 
ATOM   3680 H HB2  . ASN A 1 238 ? 3.53200   2.90200   41.01800  1.000 47.34551  ? 238 ASN A HB2  1 
ATOM   3681 H HB3  . ASN A 1 238 ? 2.28700   1.93600   40.81400  1.000 47.34551  ? 238 ASN A HB3  1 
ATOM   3682 H HD21 . ASN A 1 238 ? 0.85800   4.12900   42.94900  1.000 64.80455  ? 238 ASN A HD21 1 
ATOM   3683 H HD22 . ASN A 1 238 ? 1.09400   3.90600   41.49600  1.000 64.80455  ? 238 ASN A HD22 1 
ATOM   3684 N N    . TYR A 1 239 ? 4.76200   -0.97500  40.94100  1.000 28.62736  ? 239 TYR A N    1 
ATOM   3685 C CA   . TYR A 1 239 ? 4.81900   -2.16700  40.11200  1.000 28.75998  ? 239 TYR A CA   1 
ATOM   3686 C C    . TYR A 1 239 ? 4.09300   -3.29100  40.83700  1.000 30.19692  ? 239 TYR A C    1 
ATOM   3687 O O    . TYR A 1 239 ? 4.13500   -3.37400  42.06700  1.000 32.09208  ? 239 TYR A O    1 
ATOM   3688 C CB   . TYR A 1 239 ? 6.28700   -2.57600  39.82900  1.000 31.29559  ? 239 TYR A CB   1 
ATOM   3689 C CG   . TYR A 1 239 ? 6.86300   -1.98000  38.57300  1.000 27.89126  ? 239 TYR A CG   1 
ATOM   3690 C CD1  . TYR A 1 239 ? 6.87500   -0.63200  38.37100  1.000 31.84588  ? 239 TYR A CD1  1 
ATOM   3691 C CD2  . TYR A 1 239 ? 7.42700   -2.78800  37.60500  1.000 29.30846  ? 239 TYR A CD2  1 
ATOM   3692 C CE1  . TYR A 1 239 ? 7.38000   -0.09400  37.22200  1.000 32.24769  ? 239 TYR A CE1  1 
ATOM   3693 C CE2  . TYR A 1 239 ? 7.92000   -2.25700  36.41400  1.000 27.98122  ? 239 TYR A CE2  1 
ATOM   3694 C CZ   . TYR A 1 239 ? 7.89800   -0.90400  36.25300  1.000 27.48605  ? 239 TYR A CZ   1 
ATOM   3695 O OH   . TYR A 1 239 ? 8.39200   -0.37000  35.08400  1.000 30.50068  ? 239 TYR A OH   1 
ATOM   3696 H H    . TYR A 1 239 ? 5.39000   -0.93600  41.52800  1.000 34.35364  ? 239 TYR A H    1 
ATOM   3697 H HA   . TYR A 1 239 ? 4.37300   -2.00200  39.26700  1.000 34.51278  ? 239 TYR A HA   1 
ATOM   3698 H HB2  . TYR A 1 239 ? 6.83800   -2.28300  40.56900  1.000 37.55550  ? 239 TYR A HB2  1 
ATOM   3699 H HB3  . TYR A 1 239 ? 6.33200   -3.54100  39.74700  1.000 37.55550  ? 239 TYR A HB3  1 
ATOM   3700 H HD1  . TYR A 1 239 ? 6.50700   -0.07100  39.01400  1.000 38.21586  ? 239 TYR A HD1  1 
ATOM   3701 H HD2  . TYR A 1 239 ? 7.41500   -3.71100  37.72000  1.000 35.17095  ? 239 TYR A HD2  1 
ATOM   3702 H HE1  . TYR A 1 239 ? 7.35900   0.82700   37.09400  1.000 38.69803  ? 239 TYR A HE1  1 
ATOM   3703 H HE2  . TYR A 1 239 ? 8.28400   -2.80900  35.76000  1.000 33.57827  ? 239 TYR A HE2  1 
ATOM   3704 H HH   . TYR A 1 239 ? 8.32700   0.46700   35.10100  1.000 36.60162  ? 239 TYR A HH   1 
ATOM   3705 N N    . GLU A 1 240 ? 3.40300   -4.13600  40.06800  1.000 28.85744  ? 240 GLU A N    1 
ATOM   3706 C CA   . GLU A 1 240 ? 2.76400   -5.33200  40.61400  1.000 32.07189  ? 240 GLU A CA   1 
ATOM   3707 C C    . GLU A 1 240 ? 3.79100   -6.28600  41.22300  1.000 35.01751  ? 240 GLU A C    1 
ATOM   3708 O O    . GLU A 1 240 ? 4.92000   -6.38900  40.74500  1.000 28.66797  ? 240 GLU A O    1 
ATOM   3709 C CB   . GLU A 1 240 ? 1.99400   -6.07800  39.52000  1.000 31.96359  ? 240 GLU A CB   1 
ATOM   3710 C CG   . GLU A 1 240 ? 0.70500   -5.44800  39.18100  1.000 34.91651  ? 240 GLU A CG   1 
ATOM   3711 C CD   . GLU A 1 240 ? -0.28700  -5.57700  40.34700  1.000 39.21191  ? 240 GLU A CD   1 
ATOM   3712 O OE1  . GLU A 1 240 ? -0.71400  -6.72200  40.63200  1.000 41.15493  ? 240 GLU A OE1  1 
ATOM   3713 O OE2  . GLU A 1 240 ? -0.62300  -4.54600  40.97800  1.000 38.93123  ? 240 GLU A OE2  1 
ATOM   3714 H H    . GLU A 1 240 ? 3.29000   -4.03700  39.22100  1.000 34.62972  ? 240 GLU A H    1 
ATOM   3715 H HA   . GLU A 1 240 ? 2.13800   -5.05500  41.29700  1.000 38.48707  ? 240 GLU A HA   1 
ATOM   3716 H HB2  . GLU A 1 240 ? 2.53500   -6.10200  38.71500  1.000 38.35711  ? 240 GLU A HB2  1 
ATOM   3717 H HB3  . GLU A 1 240 ? 1.81400   -6.98200  39.82300  1.000 38.35711  ? 240 GLU A HB3  1 
ATOM   3718 H HG2  . GLU A 1 240 ? 0.84400   -4.50500  39.00000  1.000 41.90062  ? 240 GLU A HG2  1 
ATOM   3719 H HG3  . GLU A 1 240 ? 0.32500   -5.88900  38.40500  1.000 41.90062  ? 240 GLU A HG3  1 
ATOM   3720 N N    . PRO A 1 241 ? 3.41600   -7.03800  42.24700  1.000 33.44553  ? 241 PRO A N    1 
ATOM   3721 C CA   . PRO A 1 241 ? 4.34700   -8.03700  42.78200  1.000 35.68139  ? 241 PRO A CA   1 
ATOM   3722 C C    . PRO A 1 241 ? 4.60400   -9.11100  41.74800  1.000 36.13746  ? 241 PRO A C    1 
ATOM   3723 O O    . PRO A 1 241 ? 3.71800   -9.48700  40.96700  1.000 34.02754  ? 241 PRO A O    1 
ATOM   3724 C CB   . PRO A 1 241 ? 3.61900   -8.58700  44.01600  1.000 40.45768  ? 241 PRO A CB   1 
ATOM   3725 C CG   . PRO A 1 241 ? 2.63500   -7.50100  44.36700  1.000 38.86935  ? 241 PRO A CG   1 
ATOM   3726 C CD   . PRO A 1 241 ? 2.18900   -6.95000  43.05000  1.000 41.04549  ? 241 PRO A CD   1 
ATOM   3727 H HA   . PRO A 1 241 ? 5.18400   -7.62400  43.04800  1.000 42.81846  ? 241 PRO A HA   1 
ATOM   3728 H HB2  . PRO A 1 241 ? 3.16000   -9.41100  43.78900  1.000 48.55002  ? 241 PRO A HB2  1 
ATOM   3729 H HB3  . PRO A 1 241 ? 4.25200   -8.72800  44.73800  1.000 48.55002  ? 241 PRO A HB3  1 
ATOM   3730 H HG2  . PRO A 1 241 ? 1.88600   -7.88300  44.85000  1.000 46.64402  ? 241 PRO A HG2  1 
ATOM   3731 H HG3  . PRO A 1 241 ? 3.07400   -6.82000  44.89700  1.000 46.64402  ? 241 PRO A HG3  1 
ATOM   3732 H HD2  . PRO A 1 241 ? 1.48900   -7.50200  42.66800  1.000 49.25539  ? 241 PRO A HD2  1 
ATOM   3733 H HD3  . PRO A 1 241 ? 1.90500   -6.03000  43.15700  1.000 49.25539  ? 241 PRO A HD3  1 
ATOM   3734 N N    . LEU A 1 242 ? 5.84000   -9.59400  41.74200  1.000 32.65623  ? 242 LEU A N    1 
ATOM   3735 C CA   . LEU A 1 242 ? 6.26800   -10.69900 40.90500  1.000 30.84856  ? 242 LEU A CA   1 
ATOM   3736 C C    . LEU A 1 242 ? 6.20100   -11.95000 41.77200  1.000 39.45299  ? 242 LEU A C    1 
ATOM   3737 O O    . LEU A 1 242 ? 6.77800   -11.97700 42.87100  1.000 34.75413  ? 242 LEU A O    1 
ATOM   3738 C CB   . LEU A 1 242 ? 7.69700   -10.47500 40.41100  1.000 37.40030  ? 242 LEU A CB   1 
ATOM   3739 C CG   . LEU A 1 242 ? 8.12800   -11.38200 39.27900  1.000 35.07907  ? 242 LEU A CG   1 
ATOM   3740 C CD1  . LEU A 1 242 ? 7.40700   -10.96200 37.96800  1.000 32.37278  ? 242 LEU A CD1  1 
ATOM   3741 C CD2  . LEU A 1 242 ? 9.64600   -11.37800 39.17400  1.000 34.66290  ? 242 LEU A CD2  1 
ATOM   3742 H H    . LEU A 1 242 ? 6.47100   -9.28200  42.23600  1.000 39.18827  ? 242 LEU A H    1 
ATOM   3743 H HA   . LEU A 1 242 ? 5.67300   -10.80000 40.14600  1.000 37.01907  ? 242 LEU A HA   1 
ATOM   3744 H HB2  . LEU A 1 242 ? 7.77600   -9.56000  40.10000  1.000 44.88116  ? 242 LEU A HB2  1 
ATOM   3745 H HB3  . LEU A 1 242 ? 8.30600   -10.62100 41.15200  1.000 44.88116  ? 242 LEU A HB3  1 
ATOM   3746 H HG   . LEU A 1 242 ? 7.85200   -12.28800 39.48700  1.000 42.09569  ? 242 LEU A HG   1 
ATOM   3747 H HD11 . LEU A 1 242 ? 7.76400   -11.48400 37.23200  1.000 38.84814  ? 242 LEU A HD11 1 
ATOM   3748 H HD12 . LEU A 1 242 ? 6.45600   -11.12900 38.06100  1.000 38.84814  ? 242 LEU A HD12 1 
ATOM   3749 H HD13 . LEU A 1 242 ? 7.56400   -10.01800 37.81000  1.000 38.84814  ? 242 LEU A HD13 1 
ATOM   3750 H HD21 . LEU A 1 242 ? 9.91200   -11.94500 38.43400  1.000 41.59628  ? 242 LEU A HD21 1 
ATOM   3751 H HD22 . LEU A 1 242 ? 9.94900   -10.46900 39.02100  1.000 41.59628  ? 242 LEU A HD22 1 
ATOM   3752 H HD23 . LEU A 1 242 ? 10.02100  -11.71700 40.00200  1.000 41.59628  ? 242 LEU A HD23 1 
ATOM   3753 N N    . THR A 1 243 ? 5.47500   -12.95800 41.29700  1.000 33.69502  ? 243 THR A N    1 
ATOM   3754 C CA   . THR A 1 243 ? 5.25500   -14.20400 42.01400  1.000 35.10750  ? 243 THR A CA   1 
ATOM   3755 C C    . THR A 1 243 ? 6.16300   -15.27800 41.46600  1.000 33.70648  ? 243 THR A C    1 
ATOM   3756 O O    . THR A 1 243 ? 6.77500   -15.12600 40.40500  1.000 34.76067  ? 243 THR A O    1 
ATOM   3757 C CB   . THR A 1 243 ? 3.80200   -14.64700 41.86400  1.000 35.90996  ? 243 THR A CB   1 
ATOM   3758 O OG1  . THR A 1 243 ? 3.56900   -14.92000 40.46000  1.000 32.43126  ? 243 THR A OG1  1 
ATOM   3759 C CG2  . THR A 1 243 ? 2.84200   -13.55400 42.32800  1.000 37.08430  ? 243 THR A CG2  1 
ATOM   3760 H H    . THR A 1 243 ? 5.08600   -12.93900 40.53100  1.000 40.43483  ? 243 THR A H    1 
ATOM   3761 H HA   . THR A 1 243 ? 5.44900   -14.08100 42.95600  1.000 42.12981  ? 243 THR A HA   1 
ATOM   3762 H HB   . THR A 1 243 ? 3.64400   -15.44800 42.38700  1.000 43.09275  ? 243 THR A HB   1 
ATOM   3763 H HG1  . THR A 1 243 ? 2.77500   -15.16700 40.34300  1.000 38.91831  ? 243 THR A HG1  1 
ATOM   3764 H HG21 . THR A 1 243 ? 1.92900   -13.88200 42.30100  1.000 44.50196  ? 243 THR A HG21 1 
ATOM   3765 H HG22 . THR A 1 243 ? 3.05500   -13.29000 43.23700  1.000 44.50196  ? 243 THR A HG22 1 
ATOM   3766 H HG23 . THR A 1 243 ? 2.91600   -12.77900 41.74900  1.000 44.50196  ? 243 THR A HG23 1 
ATOM   3767 N N    . GLN A 1 244 ? 6.24500   -16.39200 42.18900  1.000 33.64175  ? 244 GLN A N    1 
ATOM   3768 C CA   . GLN A 1 244 ? 7.01300   -17.50300 41.63800  1.000 36.62139  ? 244 GLN A CA   1 
ATOM   3769 C C    . GLN A 1 244 ? 6.35700   -18.05300 40.37700  1.000 38.82460  ? 244 GLN A C    1 
ATOM   3770 O O    . GLN A 1 244 ? 7.05000   -18.60200 39.52500  1.000 37.60459  ? 244 GLN A O    1 
ATOM   3771 C CB   . GLN A 1 244 ? 7.19400   -18.62000 42.66600  1.000 38.18952  ? 244 GLN A CB   1 
ATOM   3772 C CG   . GLN A 1 244 ? 8.01300   -19.79900 42.14200  1.000 43.16461  ? 244 GLN A CG   1 
ATOM   3773 C CD   . GLN A 1 244 ? 9.47800   -19.43300 41.87700  1.000 46.71462  ? 244 GLN A CD   1 
ATOM   3774 O OE1  . GLN A 1 244 ? 10.06000  -18.61700 42.60100  1.000 48.66205  ? 244 GLN A OE1  1 
ATOM   3775 N NE2  . GLN A 1 244 ? 10.06000  -19.99900 40.81100  1.000 45.03669  ? 244 GLN A NE2  1 
ATOM   3776 H H    . GLN A 1 244 ? 5.88700   -16.52700 42.95900  1.000 40.37090  ? 244 GLN A H    1 
ATOM   3777 H HA   . GLN A 1 244 ? 7.89500   -17.18000 41.39500  1.000 43.94647  ? 244 GLN A HA   1 
ATOM   3778 H HB2  . GLN A 1 244 ? 7.65100   -18.26100 43.44200  1.000 45.82823  ? 244 GLN A HB2  1 
ATOM   3779 H HB3  . GLN A 1 244 ? 6.32100   -18.95500 42.92300  1.000 45.82823  ? 244 GLN A HB3  1 
ATOM   3780 H HG2  . GLN A 1 244 ? 8.00200   -20.50400 42.80800  1.000 51.79833  ? 244 GLN A HG2  1 
ATOM   3781 H HG3  . GLN A 1 244 ? 7.62800   -20.12700 41.31500  1.000 51.79833  ? 244 GLN A HG3  1 
ATOM   3782 H HE21 . GLN A 1 244 ? 9.62000   -20.55600 40.32600  1.000 54.04483  ? 244 GLN A HE21 1 
ATOM   3783 H HE22 . GLN A 1 244 ? 10.88000  -19.81900 40.62300  1.000 54.04483  ? 244 GLN A HE22 1 
ATOM   3784 N N    . ASP A 1 245 ? 5.02800   -17.96000 40.25400  1.000 34.97958  ? 245 ASP A N    1 
ATOM   3785 C CA   . ASP A 1 245 ? 4.39300   -18.33300 38.98600  1.000 39.13660  ? 245 ASP A CA   1 
ATOM   3786 C C    . ASP A 1 245 ? 4.97200   -17.53300 37.82100  1.000 33.88294  ? 245 ASP A C    1 
ATOM   3787 O O    . ASP A 1 245 ? 5.26200   -18.09300 36.76300  1.000 35.46288  ? 245 ASP A O    1 
ATOM   3788 C CB   . ASP A 1 245 ? 2.87800   -18.10600 39.02400  1.000 39.88128  ? 245 ASP A CB   1 
ATOM   3789 C CG   . ASP A 1 245 ? 2.10500   -19.28300 39.60800  1.000 52.57167  ? 245 ASP A CG   1 
ATOM   3790 O OD1  . ASP A 1 245 ? 2.72900   -20.23500 40.13600  1.000 49.03307  ? 245 ASP A OD1  1 
ATOM   3791 O OD2  . ASP A 1 245 ? 0.85200   -19.23500 39.53200  1.000 56.20733  ? 245 ASP A OD2  1 
ATOM   3792 H H    . ASP A 1 245 ? 4.48800   -17.69300 40.86800  1.000 41.97629  ? 245 ASP A H    1 
ATOM   3793 H HA   . ASP A 1 245 ? 4.55500   -19.27400 38.81400  1.000 46.96472  ? 245 ASP A HA   1 
ATOM   3794 H HB2  . ASP A 1 245 ? 2.69100   -17.32600 39.57000  1.000 47.85833  ? 245 ASP A HB2  1 
ATOM   3795 H HB3  . ASP A 1 245 ? 2.56000   -17.96000 38.11900  1.000 47.85833  ? 245 ASP A HB3  1 
ATOM   3796 N N    . HIS A 1 246 ? 5.11100   -16.22900 38.01200  1.000 31.93269  ? 246 HIS A N    1 
ATOM   3797 C CA   . HIS A 1 246 ? 5.65300   -15.34200 36.95400  1.000 32.52890  ? 246 HIS A CA   1 
ATOM   3798 C C    . HIS A 1 246 ? 7.08700   -15.76600 36.65100  1.000 32.91609  ? 246 HIS A C    1 
ATOM   3799 O O    . HIS A 1 246 ? 7.45400   -15.83000 35.48600  1.000 33.73892  ? 246 HIS A O    1 
ATOM   3800 C CB   . HIS A 1 246 ? 5.59800   -13.89000 37.42100  1.000 31.79421  ? 246 HIS A CB   1 
ATOM   3801 C CG   . HIS A 1 246 ? 4.21900   -13.34500 37.56600  1.000 35.28930  ? 246 HIS A CG   1 
ATOM   3802 N ND1  . HIS A 1 246 ? 3.90800   -12.37400 38.48900  1.000 31.63908  ? 246 HIS A ND1  1 
ATOM   3803 C CD2  . HIS A 1 246 ? 3.07800   -13.61800 36.90200  1.000 32.51286  ? 246 HIS A CD2  1 
ATOM   3804 C CE1  . HIS A 1 246 ? 2.63000   -12.08100 38.39700  1.000 36.14153  ? 246 HIS A CE1  1 
ATOM   3805 N NE2  . HIS A 1 246 ? 2.10200   -12.82400 37.42900  1.000 30.53282  ? 246 HIS A NE2  1 
ATOM   3806 H H    . HIS A 1 246 ? 4.90300   -15.82000 38.74000  1.000 38.32003  ? 246 HIS A H    1 
ATOM   3807 H HA   . HIS A 1 246 ? 5.12400   -15.43200 36.14600  1.000 39.03548  ? 246 HIS A HA   1 
ATOM   3808 H HB2  . HIS A 1 246 ? 6.03300   -13.82500 38.28500  1.000 38.15385  ? 246 HIS A HB2  1 
ATOM   3809 H HB3  . HIS A 1 246 ? 6.06700   -13.33800 36.77600  1.000 38.15385  ? 246 HIS A HB3  1 
ATOM   3810 H HD2  . HIS A 1 246 ? 2.97500   -14.23400 36.21300  1.000 39.01624  ? 246 HIS A HD2  1 
ATOM   3811 H HE1  . HIS A 1 246 ? 2.17600   -11.45500 38.91300  1.000 43.37064  ? 246 HIS A HE1  1 
ATOM   3812 H HE2  . HIS A 1 246 ? 1.27900   -12.81100 37.18000  1.000 36.64019  ? 246 HIS A HE2  1 
ATOM   3813 N N    . VAL A 1 247 ? 7.84700   -16.02600 37.70200  1.000 32.62386  ? 247 VAL A N    1 
ATOM   3814 C CA   . VAL A 1 247 ? 9.21300   -16.47900 37.47800  1.000 35.15905  ? 247 VAL A CA   1 
ATOM   3815 C C    . VAL A 1 247 ? 9.22400   -17.73500 36.62200  1.000 40.06695  ? 247 VAL A C    1 
ATOM   3816 O O    . VAL A 1 247 ? 10.03600  -17.86600 35.68800  1.000 36.91084  ? 247 VAL A O    1 
ATOM   3817 C CB   . VAL A 1 247 ? 9.92300   -16.69300 38.81800  1.000 37.56371  ? 247 VAL A CB   1 
ATOM   3818 C CG1  . VAL A 1 247 ? 11.22400  -17.41900 38.59100  1.000 39.55837  ? 247 VAL A CG1  1 
ATOM   3819 C CG2  . VAL A 1 247 ? 10.14500  -15.32400 39.44300  1.000 33.24444  ? 247 VAL A CG2  1 
ATOM   3820 H H    . VAL A 1 247 ? 7.61000   -15.95300 38.52600  1.000 39.14943  ? 247 VAL A H    1 
ATOM   3821 H HA   . VAL A 1 247 ? 9.69500   -15.78900 36.99500  1.000 42.19167  ? 247 VAL A HA   1 
ATOM   3822 H HB   . VAL A 1 247 ? 9.36400   -17.22300 39.40800  1.000 45.07726  ? 247 VAL A HB   1 
ATOM   3823 H HG11 . VAL A 1 247 ? 11.79700  -17.28200 39.36200  1.000 47.47085  ? 247 VAL A HG11 1 
ATOM   3824 H HG12 . VAL A 1 247 ? 11.04600  -18.36600 38.47800  1.000 47.47085  ? 247 VAL A HG12 1 
ATOM   3825 H HG13 . VAL A 1 247 ? 11.65100  -17.06100 37.79700  1.000 47.47085  ? 247 VAL A HG13 1 
ATOM   3826 H HG21 . VAL A 1 247 ? 10.60500  -15.43500 40.29000  1.000 39.89413  ? 247 VAL A HG21 1 
ATOM   3827 H HG22 . VAL A 1 247 ? 10.68400  -14.78600 38.84200  1.000 39.89413  ? 247 VAL A HG22 1 
ATOM   3828 H HG23 . VAL A 1 247 ? 9.28500   -14.89900 39.58700  1.000 39.89413  ? 247 VAL A HG23 1 
ATOM   3829 N N    . ASP A 1 248 ? 8.36400   -18.70200 36.96000  1.000 36.60693  ? 248 ASP A N    1 
ATOM   3830 C CA   . ASP A 1 248 ? 8.25600   -19.92700 36.16000  1.000 38.77553  ? 248 ASP A CA   1 
ATOM   3831 C C    . ASP A 1 248 ? 7.88300   -19.60600 34.72600  1.000 38.59103  ? 248 ASP A C    1 
ATOM   3832 O O    . ASP A 1 248 ? 8.44600   -20.18000 33.78100  1.000 39.56487  ? 248 ASP A O    1 
ATOM   3833 C CB   . ASP A 1 248 ? 7.22200   -20.88900 36.77600  1.000 44.37805  ? 248 ASP A CB   1 
ATOM   3834 C CG   . ASP A 1 248 ? 7.66600   -21.48500 38.12100  1.000 49.16671  ? 248 ASP A CG   1 
ATOM   3835 O OD1  . ASP A 1 248 ? 8.88600   -21.54600 38.41200  1.000 48.85074  ? 248 ASP A OD1  1 
ATOM   3836 O OD2  . ASP A 1 248 ? 6.77900   -21.92700 38.88600  1.000 47.58050  ? 248 ASP A OD2  1 
ATOM   3837 H H    . ASP A 1 248 ? 7.83800   -18.67400 37.64000  1.000 43.92912  ? 248 ASP A H    1 
ATOM   3838 H HA   . ASP A 1 248 ? 9.11600   -20.37600 36.15300  1.000 46.53143  ? 248 ASP A HA   1 
ATOM   3839 H HB2  . ASP A 1 248 ? 6.39300   -20.40700 36.92300  1.000 53.25446  ? 248 ASP A HB2  1 
ATOM   3840 H HB3  . ASP A 1 248 ? 7.07100   -21.62300 36.16000  1.000 53.25446  ? 248 ASP A HB3  1 
ATOM   3841 N N    . ILE A 1 249 ? 6.93800   -18.68500 34.53800  1.000 34.39127  ? 249 ILE A N    1 
ATOM   3842 C CA   . ILE A 1 249 ? 6.45000   -18.37500 33.21100  1.000 37.97315  ? 249 ILE A CA   1 
ATOM   3843 C C    . ILE A 1 249 ? 7.57300   -17.79800 32.35900  1.000 37.06045  ? 249 ILE A C    1 
ATOM   3844 O O    . ILE A 1 249 ? 7.59700   -17.98900 31.14000  1.000 37.29515  ? 249 ILE A O    1 
ATOM   3845 C CB   . ILE A 1 249 ? 5.25000   -17.41600 33.27900  1.000 38.01884  ? 249 ILE A CB   1 
ATOM   3846 C CG1  . ILE A 1 249 ? 4.07600   -18.12000 33.97100  1.000 40.81521  ? 249 ILE A CG1  1 
ATOM   3847 C CG2  . ILE A 1 249 ? 4.83400   -17.00100 31.88200  1.000 44.38732  ? 249 ILE A CG2  1 
ATOM   3848 C CD1  . ILE A 1 249 ? 2.96800   -17.19100 34.37800  1.000 39.27683  ? 249 ILE A CD1  1 
ATOM   3849 H H    . ILE A 1 249 ? 6.56800   -18.23000 35.16700  1.000 41.27033  ? 249 ILE A H    1 
ATOM   3850 H HA   . ILE A 1 249 ? 6.15000   -19.19500 32.78900  1.000 45.56858  ? 249 ILE A HA   1 
ATOM   3851 H HB   . ILE A 1 249 ? 5.49700   -16.62800 33.78800  1.000 45.62341  ? 249 ILE A HB   1 
ATOM   3852 H HG12 . ILE A 1 249 ? 3.69900   -18.76400 33.35100  1.000 48.97905  ? 249 ILE A HG12 1 
ATOM   3853 H HG13 . ILE A 1 249 ? 4.39300   -18.58100 34.75900  1.000 48.97905  ? 249 ILE A HG13 1 
ATOM   3854 H HG21 . ILE A 1 249 ? 3.95700   -16.58900 31.92000  1.000 53.26559  ? 249 ILE A HG21 1 
ATOM   3855 H HG22 . ILE A 1 249 ? 5.47800   -16.36500 31.53300  1.000 53.26559  ? 249 ILE A HG22 1 
ATOM   3856 H HG23 . ILE A 1 249 ? 4.80300   -17.78800 31.31600  1.000 53.26559  ? 249 ILE A HG23 1 
ATOM   3857 H HD11 . ILE A 1 249 ? 2.35200   -17.66900 34.95500  1.000 47.13300  ? 249 ILE A HD11 1 
ATOM   3858 H HD12 . ILE A 1 249 ? 3.34900   -16.43600 34.85400  1.000 47.13300  ? 249 ILE A HD12 1 
ATOM   3859 H HD13 . ILE A 1 249 ? 2.50500   -16.88200 33.58400  1.000 47.13300  ? 249 ILE A HD13 1 
ATOM   3860 N N    . LEU A 1 250 ? 8.50400   -17.07700 32.98400  1.000 36.64658  ? 250 LEU A N    1 
ATOM   3861 C CA   . LEU A 1 250 ? 9.64300   -16.52300 32.25300  1.000 36.83186  ? 250 LEU A CA   1 
ATOM   3862 C C    . LEU A 1 250 ? 10.74400  -17.55800 31.98400  1.000 33.66856  ? 250 LEU A C    1 
ATOM   3863 O O    . LEU A 1 250 ? 11.73000  -17.22700 31.30900  1.000 38.98485  ? 250 LEU A O    1 
ATOM   3864 C CB   . LEU A 1 250 ? 10.18600  -15.29200 33.01500  1.000 30.43790  ? 250 LEU A CB   1 
ATOM   3865 C CG   . LEU A 1 250 ? 9.22400   -14.06200 33.02800  1.000 32.74808  ? 250 LEU A CG   1 
ATOM   3866 C CD1  . LEU A 1 250 ? 9.53700   -13.12900 34.21500  1.000 36.18780  ? 250 LEU A CD1  1 
ATOM   3867 C CD2  . LEU A 1 250 ? 9.17800   -13.24000 31.70700  1.000 31.97061  ? 250 LEU A CD2  1 
ATOM   3868 H H    . LEU A 1 250 ? 8.50000   -16.89500 33.82400  1.000 43.97670  ? 250 LEU A H    1 
ATOM   3869 H HA   . LEU A 1 250 ? 9.32700   -16.21000 31.39100  1.000 44.19904  ? 250 LEU A HA   1 
ATOM   3870 H HB2  . LEU A 1 250 ? 10.35100  -15.54600 33.93600  1.000 36.52629  ? 250 LEU A HB2  1 
ATOM   3871 H HB3  . LEU A 1 250 ? 11.01600  -15.01200 32.59900  1.000 36.52629  ? 250 LEU A HB3  1 
ATOM   3872 H HG   . LEU A 1 250 ? 8.32600   -14.39800 33.17200  1.000 39.29849  ? 250 LEU A HG   1 
ATOM   3873 H HD11 . LEU A 1 250 ? 8.94500   -12.36200 34.17800  1.000 43.42616  ? 250 LEU A HD11 1 
ATOM   3874 H HD12 . LEU A 1 250 ? 9.39800   -13.61500 35.04300  1.000 43.42616  ? 250 LEU A HD12 1 
ATOM   3875 H HD13 . LEU A 1 250 ? 10.46000  -12.83800 34.15200  1.000 43.42616  ? 250 LEU A HD13 1 
ATOM   3876 H HD21 . LEU A 1 250 ? 8.55600   -12.50400 31.81500  1.000 38.36553  ? 250 LEU A HD21 1 
ATOM   3877 H HD22 . LEU A 1 250 ? 10.06600  -12.89800 31.51700  1.000 38.36553  ? 250 LEU A HD22 1 
ATOM   3878 H HD23 . LEU A 1 250 ? 8.88500   -13.81800 30.98600  1.000 38.36553  ? 250 LEU A HD23 1 
ATOM   3879 N N    . GLY A 1 251 ? 10.61400  -18.80300 32.45400  1.000 36.05538  ? 251 GLY A N    1 
ATOM   3880 C CA   . GLY A 1 251 ? 11.66000  -19.80300 32.27100  1.000 37.73566  ? 251 GLY A CA   1 
ATOM   3881 C C    . GLY A 1 251 ? 12.14600  -19.95000 30.83100  1.000 39.37710  ? 251 GLY A C    1 
ATOM   3882 O O    . GLY A 1 251 ? 13.34600  -19.93000 30.54600  1.000 41.28156  ? 251 GLY A O    1 
ATOM   3883 H H    . GLY A 1 251 ? 9.92600   -19.09100 32.88300  1.000 43.26725  ? 251 GLY A H    1 
ATOM   3884 H HA2  . GLY A 1 251 ? 12.42200  -19.56800 32.82300  1.000 45.28359  ? 251 GLY A HA2  1 
ATOM   3885 H HA3  . GLY A 1 251 ? 11.32800  -20.66600 32.56600  1.000 45.28359  ? 251 GLY A HA3  1 
ATOM   3886 N N    . PRO A 1 252 ? 11.21200  -20.13700 29.90100  1.000 41.28048  ? 252 PRO A N    1 
ATOM   3887 C CA   . PRO A 1 252 ? 11.58200  -20.22300 28.46700  1.000 40.00250  ? 252 PRO A CA   1 
ATOM   3888 C C    . PRO A 1 252 ? 12.41800  -19.04800 27.93500  1.000 39.81373  ? 252 PRO A C    1 
ATOM   3889 O O    . PRO A 1 252 ? 13.46600  -19.26800 27.31500  1.000 42.13783  ? 252 PRO A O    1 
ATOM   3890 C CB   . PRO A 1 252 ? 10.20200  -20.30300 27.77900  1.000 43.44514  ? 252 PRO A CB   1 
ATOM   3891 C CG   . PRO A 1 252 ? 9.33700   -20.98700 28.77700  1.000 48.11129  ? 252 PRO A CG   1 
ATOM   3892 C CD   . PRO A 1 252 ? 9.81200   -20.52800 30.14900  1.000 41.74206  ? 252 PRO A CD   1 
ATOM   3893 H HA   . PRO A 1 252 ? 12.06300  -21.04900 28.30100  1.000 48.00380  ? 252 PRO A HA   1 
ATOM   3894 H HB2  . PRO A 1 252 ? 9.87400   -19.40900 27.59200  1.000 52.13497  ? 252 PRO A HB2  1 
ATOM   3895 H HB3  . PRO A 1 252 ? 10.27000  -20.82500 26.96400  1.000 52.13497  ? 252 PRO A HB3  1 
ATOM   3896 H HG2  . PRO A 1 252 ? 8.41400   -20.72900 28.63200  1.000 57.73435  ? 252 PRO A HG2  1 
ATOM   3897 H HG3  . PRO A 1 252 ? 9.43800   -21.94800 28.68700  1.000 57.73435  ? 252 PRO A HG3  1 
ATOM   3898 H HD2  . PRO A 1 252 ? 9.29300   -19.76500 30.44800  1.000 50.09127  ? 252 PRO A HD2  1 
ATOM   3899 H HD3  . PRO A 1 252 ? 9.77100   -21.26000 30.78500  1.000 50.09127  ? 252 PRO A HD3  1 
ATOM   3900 N N    . LEU A 1 253 ? 11.95400  -17.80300 28.12100  1.000 37.37533  ? 253 LEU A N    1 
ATOM   3901 C CA   . LEU A 1 253 ? 12.72900  -16.64300 27.67600  1.000 39.21138  ? 253 LEU A CA   1 
ATOM   3902 C C    . LEU A 1 253 ? 14.07500  -16.58000 28.38100  1.000 39.29911  ? 253 LEU A C    1 
ATOM   3903 O O    . LEU A 1 253 ? 15.10300  -16.23600 27.77300  1.000 35.22210  ? 253 LEU A O    1 
ATOM   3904 C CB   . LEU A 1 253 ? 11.94100  -15.36200 27.92100  1.000 32.54302  ? 253 LEU A CB   1 
ATOM   3905 C CG   . LEU A 1 253 ? 10.70800  -15.15900 27.04400  1.000 34.82443  ? 253 LEU A CG   1 
ATOM   3906 C CD1  . LEU A 1 253 ? 9.92500   -13.94400 27.53000  1.000 29.13607  ? 253 LEU A CD1  1 
ATOM   3907 C CD2  . LEU A 1 253 ? 11.17800  -14.93500 25.58900  1.000 31.22848  ? 253 LEU A CD2  1 
ATOM   3908 H H    . LEU A 1 253 ? 11.20500  -17.60900 28.49700  1.000 44.85120  ? 253 LEU A H    1 
ATOM   3909 H HA   . LEU A 1 253 ? 12.89600  -16.72100 26.72400  1.000 47.05446  ? 253 LEU A HA   1 
ATOM   3910 H HB2  . LEU A 1 253 ? 11.64300  -15.35900 28.84400  1.000 39.05242  ? 253 LEU A HB2  1 
ATOM   3911 H HB3  . LEU A 1 253 ? 12.53100  -14.60700 27.77100  1.000 39.05242  ? 253 LEU A HB3  1 
ATOM   3912 H HG   . LEU A 1 253 ? 10.13800  -15.94300 27.07900  1.000 41.79011  ? 253 LEU A HG   1 
ATOM   3913 H HD11 . LEU A 1 253 ? 9.14600   -13.82400 26.96500  1.000 34.96408  ? 253 LEU A HD11 1 
ATOM   3914 H HD12 . LEU A 1 253 ? 9.64900   -14.09300 28.44800  1.000 34.96408  ? 253 LEU A HD12 1 
ATOM   3915 H HD13 . LEU A 1 253 ? 10.49500  -13.16100 27.47900  1.000 34.96408  ? 253 LEU A HD13 1 
ATOM   3916 H HD21 . LEU A 1 253 ? 10.41800  -14.65900 25.05300  1.000 37.47498  ? 253 LEU A HD21 1 
ATOM   3917 H HD22 . LEU A 1 253 ? 11.85800  -14.24300 25.58000  1.000 37.47498  ? 253 LEU A HD22 1 
ATOM   3918 H HD23 . LEU A 1 253 ? 11.54400  -15.76300 25.24200  1.000 37.47498  ? 253 LEU A HD23 1 
ATOM   3919 N N    . SER A 1 254 ? 14.09200  -16.94700 29.66200  1.000 35.21121  ? 254 SER A N    1 
ATOM   3920 C CA   . SER A 1 254 ? 15.34500  -17.06000 30.39600  1.000 38.60960  ? 254 SER A CA   1 
ATOM   3921 C C    . SER A 1 254 ? 16.31200  -18.06500 29.75500  1.000 45.37905  ? 254 SER A C    1 
ATOM   3922 O O    . SER A 1 254 ? 17.54000  -17.85400 29.74700  1.000 43.29828  ? 254 SER A O    1 
ATOM   3923 C CB   . SER A 1 254 ? 14.99900  -17.47300 31.82500  1.000 38.34331  ? 254 SER A CB   1 
ATOM   3924 O OG   . SER A 1 254 ? 16.15700  -17.73900 32.50500  1.000 47.19425  ? 254 SER A OG   1 
ATOM   3925 H H    . SER A 1 254 ? 13.39200  -17.13500 30.12500  1.000 42.25425  ? 254 SER A H    1 
ATOM   3926 H HA   . SER A 1 254 ? 15.78000  -16.19400 30.42500  1.000 46.33232  ? 254 SER A HA   1 
ATOM   3927 H HB2  . SER A 1 254 ? 14.52900  -16.74700 32.26400  1.000 46.01277  ? 254 SER A HB2  1 
ATOM   3928 H HB3  . SER A 1 254 ? 14.44700  -18.26900 31.80800  1.000 46.01277  ? 254 SER A HB3  1 
ATOM   3929 H HG   . SER A 1 254 ? 16.64400  -17.05500 32.52200  1.000 56.63390  ? 254 SER A HG   1 
ATOM   3930 N N    . ALA A 1 255 ? 15.79600  -19.19600 29.26800  1.000 41.78771  ? 255 ALA A N    1 
ATOM   3931 C CA   . ALA A 1 255 ? 16.67000  -20.20100 28.66600  1.000 46.78661  ? 255 ALA A CA   1 
ATOM   3932 C C    . ALA A 1 255 ? 17.16400  -19.75100 27.29700  1.000 41.76686  ? 255 ALA A C    1 
ATOM   3933 O O    . ALA A 1 255 ? 18.32200  -20.01100 26.92800  1.000 45.20830  ? 255 ALA A O    1 
ATOM   3934 C CB   . ALA A 1 255 ? 15.96600  -21.55300 28.58000  1.000 41.92337  ? 255 ALA A CB   1 
ATOM   3935 H H    . ALA A 1 255 ? 14.96100  -19.40100 29.27400  1.000 50.14606  ? 255 ALA A H    1 
ATOM   3936 H HA   . ALA A 1 255 ? 17.44800  -20.31300 29.23500  1.000 56.14473  ? 255 ALA A HA   1 
ATOM   3937 H HB1  . ALA A 1 255 ? 16.56900  -22.19700 28.17800  1.000 50.30884  ? 255 ALA A HB1  1 
ATOM   3938 H HB2  . ALA A 1 255 ? 15.72400  -21.84000 29.47400  1.000 50.30884  ? 255 ALA A HB2  1 
ATOM   3939 H HB3  . ALA A 1 255 ? 15.16900  -21.45900 28.03500  1.000 50.30884  ? 255 ALA A HB3  1 
ATOM   3940 N N    . GLN A 1 256 ? 16.31200  -19.09500 26.54000  1.000 43.66698  ? 256 GLN A N    1 
ATOM   3941 C CA   . GLN A 1 256 ? 16.65800  -18.68600 25.18800  1.000 45.97043  ? 256 GLN A CA   1 
ATOM   3942 C C    . GLN A 1 256 ? 17.74900  -17.62200 25.19300  1.000 47.97755  ? 256 GLN A C    1 
ATOM   3943 O O    . GLN A 1 256 ? 18.56800  -17.56200 24.26100  1.000 41.89470  ? 256 GLN A O    1 
ATOM   3944 C CB   . GLN A 1 256 ? 15.41200  -18.15500 24.46400  1.000 45.63245  ? 256 GLN A CB   1 
ATOM   3945 C CG   . GLN A 1 256 ? 15.70500  -17.71400 23.03800  1.000 48.95346  ? 256 GLN A CG   1 
ATOM   3946 C CD   . GLN A 1 256 ? 14.48600  -17.18700 22.30600  1.000 52.74747  ? 256 GLN A CD   1 
ATOM   3947 O OE1  . GLN A 1 256 ? 13.33300  -17.42700 22.70400  1.000 58.15705  ? 256 GLN A OE1  1 
ATOM   3948 N NE2  . GLN A 1 256 ? 14.73400  -16.41100 21.25200  1.000 53.32957  ? 256 GLN A NE2  1 
ATOM   3949 H H    . GLN A 1 256 ? 15.51800  -18.87000 26.78300  1.000 52.40118  ? 256 GLN A H    1 
ATOM   3950 H HA   . GLN A 1 256 ? 16.98800  -19.45500 24.69800  1.000 55.16531  ? 256 GLN A HA   1 
ATOM   3951 H HB2  . GLN A 1 256 ? 14.74300  -18.85700 24.43000  1.000 54.75975  ? 256 GLN A HB2  1 
ATOM   3952 H HB3  . GLN A 1 256 ? 15.06600  -17.39000 24.95000  1.000 54.75975  ? 256 GLN A HB3  1 
ATOM   3953 H HG2  . GLN A 1 256 ? 16.36500  -17.00400 23.05200  1.000 58.74496  ? 256 GLN A HG2  1 
ATOM   3954 H HG3  . GLN A 1 256 ? 16.04700  -18.47200 22.53900  1.000 58.74496  ? 256 GLN A HG3  1 
ATOM   3955 H HE21 . GLN A 1 256 ? 15.54600  -16.25900 21.01100  1.000 63.99629  ? 256 GLN A HE21 1 
ATOM   3956 H HE22 . GLN A 1 256 ? 14.08200  -16.07900 20.80000  1.000 63.99629  ? 256 GLN A HE22 1 
ATOM   3957 N N    . THR A 1 257 ? 17.82600  -16.82800 26.26500  1.000 40.84725  ? 257 THR A N    1 
ATOM   3958 C CA   . THR A 1 257 ? 18.76800  -15.72000 26.31300  1.000 41.98148  ? 257 THR A CA   1 
ATOM   3959 C C    . THR A 1 257 ? 19.94900  -16.00000 27.21200  1.000 41.30944  ? 257 THR A C    1 
ATOM   3960 O O    . THR A 1 257 ? 20.95600  -15.28800 27.12700  1.000 46.62082  ? 257 THR A O    1 
ATOM   3961 C CB   . THR A 1 257 ? 18.07600  -14.43300 26.80700  1.000 42.56222  ? 257 THR A CB   1 
ATOM   3962 O OG1  . THR A 1 257 ? 17.50500  -14.66400 28.10100  1.000 37.15049  ? 257 THR A OG1  1 
ATOM   3963 C CG2  . THR A 1 257 ? 17.02200  -13.99100 25.88200  1.000 39.87847  ? 257 THR A CG2  1 
ATOM   3964 H H    . THR A 1 257 ? 17.34400  -16.91300 26.97200  1.000 49.01750  ? 257 THR A H    1 
ATOM   3965 H HA   . THR A 1 257 ? 19.10600  -15.55100 25.42000  1.000 50.37857  ? 257 THR A HA   1 
ATOM   3966 H HB   . THR A 1 257 ? 18.73500  -13.72400 26.87300  1.000 51.07547  ? 257 THR A HB   1 
ATOM   3967 H HG1  . THR A 1 257 ? 16.92900  -15.27400 28.05600  1.000 44.58139  ? 257 THR A HG1  1 
ATOM   3968 H HG21 . THR A 1 257 ? 16.61900  -13.17100 26.20700  1.000 47.85496  ? 257 THR A HG21 1 
ATOM   3969 H HG22 . THR A 1 257 ? 17.39900  -13.83000 25.00300  1.000 47.85496  ? 257 THR A HG22 1 
ATOM   3970 H HG23 . THR A 1 257 ? 16.33600  -14.67300 25.81100  1.000 47.85496  ? 257 THR A HG23 1 
ATOM   3971 N N    . GLY A 1 258 ? 19.86000  -17.02100 28.05400  1.000 43.89459  ? 258 GLY A N    1 
ATOM   3972 C CA   . GLY A 1 258 ? 20.89300  -17.28800 29.01400  1.000 44.54809  ? 258 GLY A CA   1 
ATOM   3973 C C    . GLY A 1 258 ? 20.91500  -16.35500 30.19900  1.000 42.60886  ? 258 GLY A C    1 
ATOM   3974 O O    . GLY A 1 258 ? 21.85700  -16.41900 30.98700  1.000 42.23704  ? 258 GLY A O    1 
ATOM   3975 H H    . GLY A 1 258 ? 19.20200  -17.57400 28.08300  1.000 52.67431  ? 258 GLY A H    1 
ATOM   3976 H HA2  . GLY A 1 258 ? 20.78600  -18.19200 29.34800  1.000 53.45851  ? 258 GLY A HA2  1 
ATOM   3977 H HA3  . GLY A 1 258 ? 21.75500  -17.23100 28.57300  1.000 53.45851  ? 258 GLY A HA3  1 
ATOM   3978 N N    . ILE A 1 259 ? 19.92300  -15.48900 30.35400  1.000 41.86149  ? 259 ILE A N    1 
ATOM   3979 C CA   . ILE A 1 259 ? 19.85100  -14.54100 31.46200  1.000 39.90245  ? 259 ILE A CA   1 
ATOM   3980 C C    . ILE A 1 259 ? 18.83000  -15.05000 32.47200  1.000 43.03390  ? 259 ILE A C    1 
ATOM   3981 O O    . ILE A 1 259 ? 17.63300  -15.09300 32.17400  1.000 35.60032  ? 259 ILE A O    1 
ATOM   3982 C CB   . ILE A 1 259 ? 19.48900  -13.14300 30.95000  1.000 38.45153  ? 259 ILE A CB   1 
ATOM   3983 C CG1  . ILE A 1 259 ? 20.61600  -12.64400 30.04500  1.000 45.55746  ? 259 ILE A CG1  1 
ATOM   3984 C CG2  . ILE A 1 259 ? 19.25500  -12.17500 32.13200  1.000 37.68317  ? 259 ILE A CG2  1 
ATOM   3985 C CD1  . ILE A 1 259 ? 20.22000  -11.40500 29.21600  1.000 38.71965  ? 259 ILE A CD1  1 
ATOM   3986 H H    . ILE A 1 259 ? 19.25700  -15.42800 29.81300  1.000 50.23459  ? 259 ILE A H    1 
ATOM   3987 H HA   . ILE A 1 259 ? 20.71400  -14.48900 31.90100  1.000 47.88374  ? 259 ILE A HA   1 
ATOM   3988 H HB   . ILE A 1 259 ? 18.67300  -13.20300 30.42900  1.000 46.14264  ? 259 ILE A HB   1 
ATOM   3989 H HG12 . ILE A 1 259 ? 21.37800  -12.40400 30.59500  1.000 54.66976  ? 259 ILE A HG12 1 
ATOM   3990 H HG13 . ILE A 1 259 ? 20.86400  -13.34700 29.42500  1.000 54.66976  ? 259 ILE A HG13 1 
ATOM   3991 H HG21 . ILE A 1 259 ? 19.22000  -11.26600 31.79500  1.000 45.22060  ? 259 ILE A HG21 1 
ATOM   3992 H HG22 . ILE A 1 259 ? 18.41600  -12.39700 32.56400  1.000 45.22060  ? 259 ILE A HG22 1 
ATOM   3993 H HG23 . ILE A 1 259 ? 19.98700  -12.26400 32.76200  1.000 45.22060  ? 259 ILE A HG23 1 
ATOM   3994 H HD11 . ILE A 1 259 ? 20.93000  -11.20900 28.58400  1.000 46.46438  ? 259 ILE A HD11 1 
ATOM   3995 H HD12 . ILE A 1 259 ? 19.39600  -11.59500 28.74000  1.000 46.46438  ? 259 ILE A HD12 1 
ATOM   3996 H HD13 . ILE A 1 259 ? 20.09100  -10.65200 29.81300  1.000 46.46438  ? 259 ILE A HD13 1 
ATOM   3997 N N    . ALA A 1 260 ? 19.28600  -15.42000 33.66600  1.000 39.94100  ? 260 ALA A N    1 
ATOM   3998 C CA   . ALA A 1 260 ? 18.37200  -15.90300 34.70300  1.000 38.64641  ? 260 ALA A CA   1 
ATOM   3999 C C    . ALA A 1 260 ? 17.33300  -14.85200 35.03400  1.000 39.21610  ? 260 ALA A C    1 
ATOM   4000 O O    . ALA A 1 260 ? 17.59400  -13.65300 34.92900  1.000 37.70136  ? 260 ALA A O    1 
ATOM   4001 C CB   . ALA A 1 260 ? 19.14600  -16.25500 35.98100  1.000 44.67026  ? 260 ALA A CB   1 
ATOM   4002 H H    . ALA A 1 260 ? 20.11300  -15.40200 33.90100  1.000 47.93000  ? 260 ALA A H    1 
ATOM   4003 H HA   . ALA A 1 260 ? 17.91600  -16.70000 34.38900  1.000 46.37649  ? 260 ALA A HA   1 
ATOM   4004 H HB1  . ALA A 1 260 ? 18.52000  -16.57200 36.65100  1.000 53.60512  ? 260 ALA A HB1  1 
ATOM   4005 H HB2  . ALA A 1 260 ? 19.79200  -16.94900 35.77700  1.000 53.60512  ? 260 ALA A HB2  1 
ATOM   4006 H HB3  . ALA A 1 260 ? 19.60200  -15.46100 36.30200  1.000 53.60512  ? 260 ALA A HB3  1 
ATOM   4007 N N    . VAL A 1 261 ? 16.13500  -15.31300 35.45000  1.000 35.43390  ? 261 VAL A N    1 
ATOM   4008 C CA   . VAL A 1 261 ? 15.03500  -14.39700 35.73300  1.000 36.78379  ? 261 VAL A CA   1 
ATOM   4009 C C    . VAL A 1 261 ? 15.42200  -13.35800 36.79100  1.000 34.54993  ? 261 VAL A C    1 
ATOM   4010 O O    . VAL A 1 261 ? 15.16100  -12.15700 36.63000  1.000 32.08193  ? 261 VAL A O    1 
ATOM   4011 C CB   . VAL A 1 261 ? 13.77000  -15.18500 36.12400  1.000 37.63080  ? 261 VAL A CB   1 
ATOM   4012 C CG1  . VAL A 1 261 ? 12.69200  -14.23100 36.55600  1.000 35.26111  ? 261 VAL A CG1  1 
ATOM   4013 C CG2  . VAL A 1 261 ? 13.25200  -15.95400 34.87200  1.000 37.00265  ? 261 VAL A CG2  1 
ATOM   4014 H H    . VAL A 1 261 ? 15.94600  -16.14300 35.57200  1.000 42.52148  ? 261 VAL A H    1 
ATOM   4015 H HA   . VAL A 1 261 ? 14.82700  -13.91000 34.92200  1.000 44.14134  ? 261 VAL A HA   1 
ATOM   4016 H HB   . VAL A 1 261 ? 13.96100  -15.81200 36.83900  1.000 45.15776  ? 261 VAL A HB   1 
ATOM   4017 H HG11 . VAL A 1 261 ? 11.83800  -14.69000 36.52900  1.000 42.31413  ? 261 VAL A HG11 1 
ATOM   4018 H HG12 . VAL A 1 261 ? 12.87600  -13.93000 37.46000  1.000 42.31413  ? 261 VAL A HG12 1 
ATOM   4019 H HG13 . VAL A 1 261 ? 12.67800  -13.47500 35.94900  1.000 42.31413  ? 261 VAL A HG13 1 
ATOM   4020 H HG21 . VAL A 1 261 ? 12.45700  -16.45300 35.11500  1.000 44.40398  ? 261 VAL A HG21 1 
ATOM   4021 H HG22 . VAL A 1 261 ? 13.04100  -15.31400 34.17400  1.000 44.40398  ? 261 VAL A HG22 1 
ATOM   4022 H HG23 . VAL A 1 261 ? 13.94400  -16.56200 34.56600  1.000 44.40398  ? 261 VAL A HG23 1 
ATOM   4023 N N    . LEU A 1 262 ? 16.02700  -13.79700 37.88600  1.000 32.85864  ? 262 LEU A N    1 
ATOM   4024 C CA   . LEU A 1 262 ? 16.36200  -12.84800 38.94300  1.000 36.14725  ? 262 LEU A CA   1 
ATOM   4025 C C    . LEU A 1 262 ? 17.52200  -11.92700 38.52800  1.000 36.92534  ? 262 LEU A C    1 
ATOM   4026 O O    . LEU A 1 262 ? 17.68300  -10.84000 39.09500  1.000 36.09351  ? 262 LEU A O    1 
ATOM   4027 C CB   . LEU A 1 262 ? 16.67400  -13.60800 40.23700  1.000 38.59156  ? 262 LEU A CB   1 
ATOM   4028 C CG   . LEU A 1 262 ? 15.43700  -14.22900 40.90700  1.000 39.85701  ? 262 LEU A CG   1 
ATOM   4029 C CD1  . LEU A 1 262 ? 15.87100  -15.15900 42.04500  1.000 42.01317  ? 262 LEU A CD1  1 
ATOM   4030 C CD2  . LEU A 1 262 ? 14.46200  -13.15600 41.41300  1.000 39.01184  ? 262 LEU A CD2  1 
ATOM   4031 H H    . LEU A 1 262 ? 16.25000  -14.61300 38.04100  1.000 39.43117  ? 262 LEU A H    1 
ATOM   4032 H HA   . LEU A 1 262 ? 15.59100  -12.28500 39.10800  1.000 43.37750  ? 262 LEU A HA   1 
ATOM   4033 H HB2  . LEU A 1 262 ? 17.29400  -14.32600 40.03600  1.000 46.31068  ? 262 LEU A HB2  1 
ATOM   4034 H HB3  . LEU A 1 262 ? 17.07700  -12.99400 40.87000  1.000 46.31068  ? 262 LEU A HB3  1 
ATOM   4035 H HG   . LEU A 1 262 ? 14.96700  -14.76700 40.25100  1.000 47.82921  ? 262 LEU A HG   1 
ATOM   4036 H HD11 . LEU A 1 262 ? 15.08100  -15.54300 42.45700  1.000 50.41661  ? 262 LEU A HD11 1 
ATOM   4037 H HD12 . LEU A 1 262 ? 16.43100  -15.86300 41.68100  1.000 50.41661  ? 262 LEU A HD12 1 
ATOM   4038 H HD13 . LEU A 1 262 ? 16.36900  -14.64500 42.70000  1.000 50.41661  ? 262 LEU A HD13 1 
ATOM   4039 H HD21 . LEU A 1 262 ? 13.79500  -13.57700 41.97700  1.000 46.81501  ? 262 LEU A HD21 1 
ATOM   4040 H HD22 . LEU A 1 262 ? 14.95700  -12.49600 41.92300  1.000 46.81501  ? 262 LEU A HD22 1 
ATOM   4041 H HD23 . LEU A 1 262 ? 14.03300  -12.73300 40.65300  1.000 46.81501  ? 262 LEU A HD23 1 
ATOM   4042 N N    . ASP A 1 263 ? 18.27400  -12.31700 37.51000  1.000 35.50952  ? 263 ASP A N    1 
ATOM   4043 C CA   . ASP A 1 263 ? 19.32200  -11.42300 36.95600  1.000 34.94019  ? 263 ASP A CA   1 
ATOM   4044 C C    . ASP A 1 263 ? 18.59800  -10.30200 36.20800  1.000 37.95217  ? 263 ASP A C    1 
ATOM   4045 O O    . ASP A 1 263 ? 18.91400  -9.12500  36.42500  1.000 34.13597  ? 263 ASP A O    1 
ATOM   4046 C CB   . ASP A 1 263 ? 20.25800  -12.24600 36.09400  1.000 40.04092  ? 263 ASP A CB   1 
ATOM   4047 C CG   . ASP A 1 263 ? 21.55000  -11.60400 35.62000  1.000 49.41702  ? 263 ASP A CG   1 
ATOM   4048 O OD1  . ASP A 1 263 ? 21.55900  -10.38500 35.39100  1.000 55.86543  ? 263 ASP A OD1  1 
ATOM   4049 O OD2  . ASP A 1 263 ? 22.53200  -12.35000 35.45000  1.000 63.15988  ? 263 ASP A OD2  1 
ATOM   4050 H H    . ASP A 1 263 ? 18.21200  -13.07900 37.11700  1.000 42.61222  ? 263 ASP A H    1 
ATOM   4051 H HA   . ASP A 1 263 ? 19.83300  -11.03100 37.68100  1.000 41.92902  ? 263 ASP A HA   1 
ATOM   4052 H HB2  . ASP A 1 263 ? 20.50500  -13.03800 36.59600  1.000 48.04991  ? 263 ASP A HB2  1 
ATOM   4053 H HB3  . ASP A 1 263 ? 19.77100  -12.51500 35.30000  1.000 48.04991  ? 263 ASP A HB3  1 
ATOM   4054 N N    . MET A 1 264 ? 17.62600  -10.67300 35.37500  1.000 33.95995  ? 264 MET A N    1 
ATOM   4055 C CA   . MET A 1 264 ? 16.83900  -9.64300  34.69600  1.000 30.31334  ? 264 MET A CA   1 
ATOM   4056 C C    . MET A 1 264 ? 16.09600  -8.75200  35.69300  1.000 32.90182  ? 264 MET A C    1 
ATOM   4057 O O    . MET A 1 264 ? 15.91400  -7.55300  35.43000  1.000 33.41047  ? 264 MET A O    1 
ATOM   4058 C CB   . MET A 1 264 ? 15.84400  -10.26000 33.70400  1.000 28.51203  ? 264 MET A CB   1 
ATOM   4059 C CG   . MET A 1 264 ? 15.20900  -9.22300  32.76800  1.000 30.24684  ? 264 MET A CG   1 
ATOM   4060 S SD   . MET A 1 264 ? 16.51200  -8.55500  31.65800  1.000 32.41349  ? 264 MET A SD   1 
ATOM   4061 C CE   . MET A 1 264 ? 16.52800  -9.80200  30.37500  1.000 33.09496  ? 264 MET A CE   1 
ATOM   4062 H H    . MET A 1 264 ? 17.40700  -11.48400 35.19000  1.000 40.75274  ? 264 MET A H    1 
ATOM   4063 H HA   . MET A 1 264 ? 17.45000  -9.08600  34.19000  1.000 36.37681  ? 264 MET A HA   1 
ATOM   4064 H HB2  . MET A 1 264 ? 16.30800  -10.91200 33.15700  1.000 34.21524  ? 264 MET A HB2  1 
ATOM   4065 H HB3  . MET A 1 264 ? 15.13100  -10.69100 34.20000  1.000 34.21524  ? 264 MET A HB3  1 
ATOM   4066 H HG2  . MET A 1 264 ? 14.52500  -9.64600  32.22600  1.000 36.29701  ? 264 MET A HG2  1 
ATOM   4067 H HG3  . MET A 1 264 ? 14.83500  -8.49300  33.28600  1.000 36.29701  ? 264 MET A HG3  1 
ATOM   4068 H HE1  . MET A 1 264 ? 17.19200  -9.56100  29.71000  1.000 39.71475  ? 264 MET A HE1  1 
ATOM   4069 H HE2  . MET A 1 264 ? 16.75100  -10.65900 30.77100  1.000 39.71475  ? 264 MET A HE2  1 
ATOM   4070 H HE3  . MET A 1 264 ? 15.64900  -9.84500  29.96600  1.000 39.71475  ? 264 MET A HE3  1 
ATOM   4071 N N    . CYS A 1 265 ? 15.60100  -9.31700  36.81900  1.000 32.73083  ? 265 CYS A N    1 
ATOM   4072 C CA   . CYS A 1 265 ? 14.98200  -8.46100  37.83700  1.000 30.14255  ? 265 CYS A CA   1 
ATOM   4073 C C    . CYS A 1 265 ? 15.95400  -7.39700  38.34800  1.000 36.64961  ? 265 CYS A C    1 
ATOM   4074 O O    . CYS A 1 265 ? 15.54800  -6.25400  38.61900  1.000 31.52095  ? 265 CYS A O    1 
ATOM   4075 C CB   . CYS A 1 265 ? 14.45800  -9.28700  39.03600  1.000 31.63315  ? 265 CYS A CB   1 
ATOM   4076 S SG   . CYS A 1 265 ? 13.03000  -10.24700 38.54900  1.000 33.72804  ? 265 CYS A SG   1 
ATOM   4077 H H    . CYS A 1 265 ? 15.61300  -10.15700 37.00400  1.000 39.27780  ? 265 CYS A H    1 
ATOM   4078 H HA   . CYS A 1 265 ? 14.22500  -8.00300  37.44000  1.000 36.17186  ? 265 CYS A HA   1 
ATOM   4079 H HB2  . CYS A 1 265 ? 15.15000  -9.89700  39.33500  1.000 37.96058  ? 265 CYS A HB2  1 
ATOM   4080 H HB3  . CYS A 1 265 ? 14.20000  -8.69100  39.75500  1.000 37.96058  ? 265 CYS A HB3  1 
ATOM   4081 H HG   . CYS A 1 265 ? 13.32500  -10.97200 37.64000  1.000 40.47445  ? 265 CYS A HG   1 
ATOM   4082 N N    . ALA A 1 266 ? 17.23500  -7.76300  38.54400  1.000 34.73756  ? 266 ALA A N    1 
ATOM   4083 C CA   . ALA A 1 266 ? 18.18700  -6.76300  39.01800  1.000 35.11444  ? 266 ALA A CA   1 
ATOM   4084 C C    . ALA A 1 266 ? 18.43200  -5.68000  37.98100  1.000 37.69843  ? 266 ALA A C    1 
ATOM   4085 O O    . ALA A 1 266 ? 18.62100  -4.51500  38.33600  1.000 36.39332  ? 266 ALA A O    1 
ATOM   4086 C CB   . ALA A 1 266 ? 19.51000  -7.41500  39.42700  1.000 40.75710  ? 266 ALA A CB   1 
ATOM   4087 H H    . ALA A 1 266 ? 17.55900  -8.54900  38.41400  1.000 41.68587  ? 266 ALA A H    1 
ATOM   4088 H HA   . ALA A 1 266 ? 17.81700  -6.33500  39.80600  1.000 42.13814  ? 266 ALA A HA   1 
ATOM   4089 H HB1  . ALA A 1 266 ? 20.11900  -6.72600  39.73600  1.000 48.90933  ? 266 ALA A HB1  1 
ATOM   4090 H HB2  . ALA A 1 266 ? 19.34100  -8.05200  40.13900  1.000 48.90933  ? 266 ALA A HB2  1 
ATOM   4091 H HB3  . ALA A 1 266 ? 19.88800  -7.87000  38.65800  1.000 48.90933  ? 266 ALA A HB3  1 
ATOM   4092 N N    . SER A 1 267 ? 18.40600  -6.03100  36.69900  1.000 33.85127  ? 267 SER A N    1 
ATOM   4093 C CA   . SER A 1 267 ? 18.48600  -5.01600  35.66300  1.000 37.21304  ? 267 SER A CA   1 
ATOM   4094 C C    . SER A 1 267 ? 17.25400  -4.09800  35.67800  1.000 34.48459  ? 267 SER A C    1 
ATOM   4095 O O    . SER A 1 267 ? 17.37900  -2.88800  35.49700  1.000 31.65846  ? 267 SER A O    1 
ATOM   4096 C CB   . SER A 1 267 ? 18.71300  -5.69900  34.31000  1.000 45.47319  ? 267 SER A CB   1 
ATOM   4097 O OG   . SER A 1 267 ? 18.11200  -4.95200  33.30800  1.000 46.35009  ? 267 SER A OG   1 
ATOM   4098 H H    . SER A 1 267 ? 18.34400  -6.83800  36.41000  1.000 40.62233  ? 267 SER A H    1 
ATOM   4099 H HA   . SER A 1 267 ? 19.26100  -4.46000  35.83900  1.000 44.65645  ? 267 SER A HA   1 
ATOM   4100 H HB2  . SER A 1 267 ? 19.66600  -5.75800  34.13700  1.000 54.56863  ? 267 SER A HB2  1 
ATOM   4101 H HB3  . SER A 1 267 ? 18.31900  -6.58500  34.32700  1.000 54.56863  ? 267 SER A HB3  1 
ATOM   4102 H HG   . SER A 1 267 ? 18.44900  -4.18300  33.28200  1.000 55.62091  ? 267 SER A HG   1 
ATOM   4103 N N    . LEU A 1 268 ? 16.05600  -4.64000  35.90500  1.000 33.08614  ? 268 LEU A N    1 
ATOM   4104 C CA   . LEU A 1 268 ? 14.87300  -3.78000  35.97900  1.000 30.31183  ? 268 LEU A CA   1 
ATOM   4105 C C    . LEU A 1 268 ? 14.95900  -2.82600  37.17000  1.000 30.18541  ? 268 LEU A C    1 
ATOM   4106 O O    . LEU A 1 268 ? 14.61000  -1.64700  37.05300  1.000 30.67090  ? 268 LEU A O    1 
ATOM   4107 C CB   . LEU A 1 268 ? 13.58800  -4.62000  36.04300  1.000 27.82354  ? 268 LEU A CB   1 
ATOM   4108 C CG   . LEU A 1 268 ? 12.24700  -3.89500  36.26100  1.000 30.54245  ? 268 LEU A CG   1 
ATOM   4109 C CD1  . LEU A 1 268 ? 12.00200  -2.79900  35.18900  1.000 29.44375  ? 268 LEU A CD1  1 
ATOM   4110 C CD2  . LEU A 1 268 ? 11.14100  -4.91200  36.09100  1.000 30.45803  ? 268 LEU A CD2  1 
ATOM   4111 H H    . LEU A 1 268 ? 15.90300  -5.47900  36.01700  1.000 39.70417  ? 268 LEU A H    1 
ATOM   4112 H HA   . LEU A 1 268 ? 14.83200  -3.24100  35.17400  1.000 36.37500  ? 268 LEU A HA   1 
ATOM   4113 H HB2  . LEU A 1 268 ? 13.51100  -5.10700  35.20800  1.000 33.38905  ? 268 LEU A HB2  1 
ATOM   4114 H HB3  . LEU A 1 268 ? 13.68500  -5.25500  36.77000  1.000 33.38905  ? 268 LEU A HB3  1 
ATOM   4115 H HG   . LEU A 1 268 ? 12.20300  -3.50600  37.14800  1.000 36.65174  ? 268 LEU A HG   1 
ATOM   4116 H HD11 . LEU A 1 268 ? 11.14000  -2.38600  35.35200  1.000 35.33330  ? 268 LEU A HD11 1 
ATOM   4117 H HD12 . LEU A 1 268 ? 12.70500  -2.13300  35.25200  1.000 35.33330  ? 268 LEU A HD12 1 
ATOM   4118 H HD13 . LEU A 1 268 ? 12.01200  -3.21000  34.31000  1.000 35.33330  ? 268 LEU A HD13 1 
ATOM   4119 H HD21 . LEU A 1 268 ? 10.28700  -4.47700  36.24300  1.000 36.55044  ? 268 LEU A HD21 1 
ATOM   4120 H HD22 . LEU A 1 268 ? 11.17500  -5.26800  35.18900  1.000 36.55044  ? 268 LEU A HD22 1 
ATOM   4121 H HD23 . LEU A 1 268 ? 11.26800  -5.62600  36.73500  1.000 36.55044  ? 268 LEU A HD23 1 
ATOM   4122 N N    . LYS A 1 269 ? 15.42700  -3.31300  38.31700  1.000 31.16721  ? 269 LYS A N    1 
ATOM   4123 C CA   . LYS A 1 269 ? 15.61900  -2.43900  39.46600  1.000 34.36194  ? 269 LYS A CA   1 
ATOM   4124 C C    . LYS A 1 269 ? 16.48600  -1.24500  39.10200  1.000 39.05351  ? 269 LYS A C    1 
ATOM   4125 O O    . LYS A 1 269 ? 16.18200  -0.10400  39.46800  1.000 34.64650  ? 269 LYS A O    1 
ATOM   4126 C CB   . LYS A 1 269 ? 16.23000  -3.26100  40.60000  1.000 38.41979  ? 269 LYS A CB   1 
ATOM   4127 C CG   . LYS A 1 269 ? 16.41600  -2.62400  41.96500  1.000 49.35566  ? 269 LYS A CG   1 
ATOM   4128 C CD   . LYS A 1 269 ? 17.11700  -3.66300  42.83900  1.000 51.04803  ? 269 LYS A CD   1 
ATOM   4129 C CE   . LYS A 1 269 ? 16.19100  -4.91400  42.95100  1.000 47.03766  ? 269 LYS A CE   1 
ATOM   4130 N NZ   . LYS A 1 269 ? 16.76400  -5.96600  43.82400  1.000 48.98187  ? 269 LYS A NZ   1 
ATOM   4131 H H    . LYS A 1 269 ? 15.63800  -4.13600  38.45300  1.000 37.40146  ? 269 LYS A H    1 
ATOM   4132 H HA   . LYS A 1 269 ? 14.75700  -2.10800  39.76200  1.000 41.23513  ? 269 LYS A HA   1 
ATOM   4133 H HB2  . LYS A 1 269 ? 15.62800  -4.00900  40.69600  1.000 46.10454  ? 269 LYS A HB2  1 
ATOM   4134 H HB3  . LYS A 1 269 ? 17.09800  -3.58100  40.31000  1.000 46.10454  ? 269 LYS A HB3  1 
ATOM   4135 H HG2  . LYS A 1 269 ? 16.97300  -1.83300  41.89600  1.000 59.22759  ? 269 LYS A HG2  1 
ATOM   4136 H HG3  . LYS A 1 269 ? 15.55400  -2.41700  42.35100  1.000 59.22759  ? 269 LYS A HG3  1 
ATOM   4137 H HD2  . LYS A 1 269 ? 17.95600  -3.92800  42.43100  1.000 61.25844  ? 269 LYS A HD2  1 
ATOM   4138 H HD3  . LYS A 1 269 ? 17.26300  -3.30200  43.72700  1.000 61.25844  ? 269 LYS A HD3  1 
ATOM   4139 H HE2  . LYS A 1 269 ? 15.33100  -4.64900  43.31300  1.000 56.44600  ? 269 LYS A HE2  1 
ATOM   4140 H HE3  . LYS A 1 269 ? 16.07800  -5.33600  42.08900  1.000 56.44600  ? 269 LYS A HE3  1 
ATOM   4141 H HZ1  . LYS A 1 269 ? 16.21100  -6.66200  43.86400  1.000 58.77905  ? 269 LYS A HZ1  1 
ATOM   4142 H HZ2  . LYS A 1 269 ? 17.54700  -6.23700  43.49900  1.000 58.77905  ? 269 LYS A HZ2  1 
ATOM   4143 H HZ3  . LYS A 1 269 ? 16.88700  -5.64600  44.64500  1.000 58.77905  ? 269 LYS A HZ3  1 
ATOM   4144 N N    . GLU A 1 270 ? 17.60900  -1.48900  38.40700  1.000 33.53506  ? 270 GLU A N    1 
ATOM   4145 C CA   . GLU A 1 270 ? 18.48900  -0.38300  38.03200  1.000 36.02322  ? 270 GLU A CA   1 
ATOM   4146 C C    . GLU A 1 270 ? 17.82100  0.55600   37.01700  1.000 35.80623  ? 270 GLU A C    1 
ATOM   4147 O O    . GLU A 1 270 ? 18.05900  1.76600   37.03800  1.000 38.36729  ? 270 GLU A O    1 
ATOM   4148 C CB   . GLU A 1 270 ? 19.81600  -0.95800  37.49200  1.000 35.90852  ? 270 GLU A CB   1 
ATOM   4149 C CG   . GLU A 1 270 ? 20.78900  0.03900   37.06300  1.000 37.37832  ? 270 GLU A CG   1 
ATOM   4150 C CD   . GLU A 1 270 ? 22.14300  -0.63600  36.73900  1.000 42.51000  ? 270 GLU A CD   1 
ATOM   4151 O OE1  . GLU A 1 270 ? 22.89200  -0.96700  37.68000  1.000 46.57858  ? 270 GLU A OE1  1 
ATOM   4152 O OE2  . GLU A 1 270 ? 22.38500  -0.88700  35.55200  1.000 41.84705  ? 270 GLU A OE2  1 
ATOM   4153 H H    . GLU A 1 270 ? 17.87400  -2.26600  38.14900  1.000 40.24288  ? 270 GLU A H    1 
ATOM   4154 H HA   . GLU A 1 270 ? 18.70100  0.12700   38.82400  1.000 43.22867  ? 270 GLU A HA   1 
ATOM   4155 H HB2  . GLU A 1 270 ? 20.22900  -1.48900  38.19100  1.000 43.09102  ? 270 GLU A HB2  1 
ATOM   4156 H HB3  . GLU A 1 270 ? 19.61900  -1.52300  36.72800  1.000 43.09102  ? 270 GLU A HB3  1 
ATOM   4157 H HG2  . GLU A 1 270 ? 20.46800  0.48200   36.26200  1.000 44.85478  ? 270 GLU A HG2  1 
ATOM   4158 H HG3  . GLU A 1 270 ? 20.92900  0.68300   37.77500  1.000 44.85478  ? 270 GLU A HG3  1 
ATOM   4159 N N    . LEU A 1 271 ? 17.02200  0.02200   36.08300  1.000 33.70587  ? 271 LEU A N    1 
ATOM   4160 C CA   . LEU A 1 271 ? 16.34300  0.88100   35.11200  1.000 35.16951  ? 271 LEU A CA   1 
ATOM   4161 C C    . LEU A 1 271 ? 15.33300  1.78200   35.79800  1.000 39.47068  ? 271 LEU A C    1 
ATOM   4162 O O    . LEU A 1 271 ? 15.18000  2.94600   35.41100  1.000 37.72559  ? 271 LEU A O    1 
ATOM   4163 C CB   . LEU A 1 271 ? 15.65300  0.05300   34.02600  1.000 32.80437  ? 271 LEU A CB   1 
ATOM   4164 C CG   . LEU A 1 271 ? 16.56400  -0.57700  32.95500  1.000 35.68417  ? 271 LEU A CG   1 
ATOM   4165 C CD1  . LEU A 1 271 ? 15.77200  -1.63000  32.19800  1.000 30.61824  ? 271 LEU A CD1  1 
ATOM   4166 C CD2  . LEU A 1 271 ? 17.12300  0.50200   32.01600  1.000 41.38946  ? 271 LEU A CD2  1 
ATOM   4167 H H    . LEU A 1 271 ? 16.86100  -0.81800  35.99400  1.000 40.44785  ? 271 LEU A H    1 
ATOM   4168 H HA   . LEU A 1 271 ? 17.00200  1.44800   34.68200  1.000 42.20421  ? 271 LEU A HA   1 
ATOM   4169 H HB2  . LEU A 1 271 ? 15.17300  -0.67100  34.45700  1.000 39.36604  ? 271 LEU A HB2  1 
ATOM   4170 H HB3  . LEU A 1 271 ? 15.02100  0.62600   33.56400  1.000 39.36604  ? 271 LEU A HB3  1 
ATOM   4171 H HG   . LEU A 1 271 ? 17.31100  -1.01600  33.39100  1.000 42.82181  ? 271 LEU A HG   1 
ATOM   4172 H HD11 . LEU A 1 271 ? 16.33800  -2.01700  31.51200  1.000 36.74269  ? 271 LEU A HD11 1 
ATOM   4173 H HD12 . LEU A 1 271 ? 15.48800  -2.31800  32.81900  1.000 36.74269  ? 271 LEU A HD12 1 
ATOM   4174 H HD13 . LEU A 1 271 ? 14.99800  -1.21000  31.79100  1.000 36.74269  ? 271 LEU A HD13 1 
ATOM   4175 H HD21 . LEU A 1 271 ? 17.64500  0.07400   31.32000  1.000 49.66816  ? 271 LEU A HD21 1 
ATOM   4176 H HD22 . LEU A 1 271 ? 16.38400  0.99100   31.62200  1.000 49.66816  ? 271 LEU A HD22 1 
ATOM   4177 H HD23 . LEU A 1 271 ? 17.68400  1.10600   32.52700  1.000 49.66816  ? 271 LEU A HD23 1 
ATOM   4178 N N    . LEU A 1 272 ? 14.65900  1.26700   36.83400  1.000 35.58831  ? 272 LEU A N    1 
ATOM   4179 C CA   . LEU A 1 272 ? 13.70200  2.08600   37.57900  1.000 36.21680  ? 272 LEU A CA   1 
ATOM   4180 C C    . LEU A 1 272 ? 14.42400  3.23300   38.26200  1.000 44.56940  ? 272 LEU A C    1 
ATOM   4181 O O    . LEU A 1 272 ? 13.94800  4.37300   38.25500  1.000 44.95643  ? 272 LEU A O    1 
ATOM   4182 C CB   . LEU A 1 272 ? 12.95400  1.21700   38.59300  1.000 35.18948  ? 272 LEU A CB   1 
ATOM   4183 C CG   . LEU A 1 272 ? 11.99500  0.26600   37.87600  1.000 33.29833  ? 272 LEU A CG   1 
ATOM   4184 C CD1  . LEU A 1 272 ? 11.32800  -0.72700  38.82900  1.000 34.95763  ? 272 LEU A CD1  1 
ATOM   4185 C CD2  . LEU A 1 272 ? 10.85900  1.02700   37.16200  1.000 33.62167  ? 272 LEU A CD2  1 
ATOM   4186 H H    . LEU A 1 272 ? 14.73700  0.46000   37.12000  1.000 42.70677  ? 272 LEU A H    1 
ATOM   4187 H HA   . LEU A 1 272 ? 13.06100  2.46800   36.96100  1.000 43.46096  ? 272 LEU A HA   1 
ATOM   4188 H HB2  . LEU A 1 272 ? 13.59100  0.68800   39.09800  1.000 42.22817  ? 272 LEU A HB2  1 
ATOM   4189 H HB3  . LEU A 1 272 ? 12.43700  1.78400   39.18600  1.000 42.22817  ? 272 LEU A HB3  1 
ATOM   4190 H HG   . LEU A 1 272 ? 12.48600  -0.23900  37.20900  1.000 39.95880  ? 272 LEU A HG   1 
ATOM   4191 H HD11 . LEU A 1 272 ? 10.77300  -1.33400  38.31500  1.000 41.94996  ? 272 LEU A HD11 1 
ATOM   4192 H HD12 . LEU A 1 272 ? 12.01600  -1.22500  39.29800  1.000 41.94996  ? 272 LEU A HD12 1 
ATOM   4193 H HD13 . LEU A 1 272 ? 10.78300  -0.23700  39.46500  1.000 41.94996  ? 272 LEU A HD13 1 
ATOM   4194 H HD21 . LEU A 1 272 ? 10.16100  0.39900   36.92700  1.000 40.34681  ? 272 LEU A HD21 1 
ATOM   4195 H HD22 . LEU A 1 272 ? 10.50800  1.70400   37.76100  1.000 40.34681  ? 272 LEU A HD22 1 
ATOM   4196 H HD23 . LEU A 1 272 ? 11.21000  1.44400   36.36000  1.000 40.34681  ? 272 LEU A HD23 1 
ATOM   4197 N N    . GLN A 1 273 ? 15.61500  2.96400   38.79200  1.000 40.69562  ? 273 GLN A N    1 
ATOM   4198 C CA   . GLN A 1 273 ? 16.35800  4.02800   39.52200  1.000 40.29867  ? 273 GLN A CA   1 
ATOM   4199 C C    . GLN A 1 273 ? 17.04900  4.99800   38.57300  1.000 43.60142  ? 273 GLN A C    1 
ATOM   4200 O O    . GLN A 1 273 ? 17.16900  6.16800   38.93400  1.000 48.56597  ? 273 GLN A O    1 
ATOM   4201 C CB   . GLN A 1 273 ? 17.35000  3.48000   40.54700  1.000 44.80493  ? 273 GLN A CB   1 
ATOM   4202 C CG   . GLN A 1 273 ? 18.47100  2.61000   40.01900  1.000 48.81017  ? 273 GLN A CG   1 
ATOM   4203 C CD   . GLN A 1 273 ? 19.71400  2.70200   40.87000  1.000 47.82411  ? 273 GLN A CD   1 
ATOM   4204 O OE1  . GLN A 1 273 ? 19.66000  3.07700   42.03600  1.000 52.07088  ? 273 GLN A OE1  1 
ATOM   4205 N NE2  . GLN A 1 273 ? 20.85000  2.35000   40.29300  1.000 44.02696  ? 273 GLN A NE2  1 
ATOM   4206 H H    . GLN A 1 273 ? 16.01500  2.20400   38.75300  1.000 48.83554  ? 273 GLN A H    1 
ATOM   4207 H HA   . GLN A 1 273 ? 15.70700  4.54700   40.02000  1.000 48.35920  ? 273 GLN A HA   1 
ATOM   4208 H HB2  . GLN A 1 273 ? 17.76100  4.23300   40.99900  1.000 53.76672  ? 273 GLN A HB2  1 
ATOM   4209 H HB3  . GLN A 1 273 ? 16.85600  2.95000   41.19200  1.000 53.76672  ? 273 GLN A HB3  1 
ATOM   4210 H HG2  . GLN A 1 273 ? 18.16900  1.69200   40.03500  1.000 58.57300  ? 273 GLN A HG2  1 
ATOM   4211 H HG3  . GLN A 1 273 ? 18.69600  2.87900   39.11500  1.000 58.57300  ? 273 GLN A HG3  1 
ATOM   4212 H HE21 . GLN A 1 273 ? 20.85300  2.09000   39.47300  1.000 52.83315  ? 273 GLN A HE21 1 
ATOM   4213 H HE22 . GLN A 1 273 ? 21.58600  2.38400   40.73600  1.000 52.83315  ? 273 GLN A HE22 1 
ATOM   4214 N N    . ASN A 1 274 ? 17.47700  4.56900   37.40200  1.000 41.51185  ? 274 ASN A N    1 
ATOM   4215 C CA   . ASN A 1 274 ? 18.28800  5.48200   36.55800  1.000 40.77776  ? 274 ASN A CA   1 
ATOM   4216 C C    . ASN A 1 274 ? 17.49800  6.07600   35.39800  1.000 52.00897  ? 274 ASN A C    1 
ATOM   4217 O O    . ASN A 1 274 ? 17.87600  7.15900   34.92800  1.000 46.37996  ? 274 ASN A O    1 
ATOM   4218 C CB   . ASN A 1 274 ? 19.46100  4.73300   35.94900  1.000 43.99948  ? 274 ASN A CB   1 
ATOM   4219 C CG   . ASN A 1 274 ? 20.38900  4.16700   36.99400  1.000 45.02477  ? 274 ASN A CG   1 
ATOM   4220 O OD1  . ASN A 1 274 ? 20.32100  4.55500   38.16300  1.000 46.29689  ? 274 ASN A OD1  1 
ATOM   4221 N ND2  . ASN A 1 274 ? 21.26300  3.25800   36.59200  1.000 41.20704  ? 274 ASN A ND2  1 
ATOM   4222 H H    . ASN A 1 274 ? 17.32900  3.79000   37.06800  1.000 49.81502  ? 274 ASN A H    1 
ATOM   4223 H HA   . ASN A 1 274 ? 18.63700  6.20800   37.09700  1.000 48.93411  ? 274 ASN A HA   1 
ATOM   4224 H HB2  . ASN A 1 274 ? 19.12400  3.99600   35.41500  1.000 52.80017  ? 274 ASN A HB2  1 
ATOM   4225 H HB3  . ASN A 1 274 ? 19.97100  5.34200   35.39200  1.000 52.80017  ? 274 ASN A HB3  1 
ATOM   4226 H HD21 . ASN A 1 274 ? 21.81100  2.91000   37.15600  1.000 49.44925  ? 274 ASN A HD21 1 
ATOM   4227 H HD22 . ASN A 1 274 ? 21.28100  3.01400   35.76800  1.000 49.44925  ? 274 ASN A HD22 1 
ATOM   4228 N N    . GLY A 1 275 ? 16.44700  5.39200   34.95500  1.000 44.71372  ? 275 GLY A N    1 
ATOM   4229 C CA   . GLY A 1 275 ? 15.78400  5.84400   33.73000  1.000 48.86607  ? 275 GLY A CA   1 
ATOM   4230 C C    . GLY A 1 275 ? 16.60700  5.37900   32.54800  1.000 50.83607  ? 275 GLY A C    1 
ATOM   4231 O O    . GLY A 1 275 ? 17.43700  4.47200   32.72300  1.000 46.68689  ? 275 GLY A O    1 
ATOM   4232 H H    . GLY A 1 275 ? 16.10800  4.69300   35.32400  1.000 53.65726  ? 275 GLY A H    1 
ATOM   4233 H HA2  . GLY A 1 275 ? 14.89300  5.46500   33.67000  1.000 58.64008  ? 275 GLY A HA2  1 
ATOM   4234 H HA3  . GLY A 1 275 ? 15.72200  6.81200   33.71700  1.000 58.64008  ? 275 GLY A HA3  1 
ATOM   4235 N N    . MET A 1 276 ? 16.40700  5.97200   31.38100  1.000 54.48081  ? 276 MET A N    1 
ATOM   4236 C CA   . MET A 1 276 ? 17.12200  5.47000   30.18100  1.000 54.18563  ? 276 MET A CA   1 
ATOM   4237 C C    . MET A 1 276 ? 18.20400  6.46500   29.74100  1.000 56.96377  ? 276 MET A C    1 
ATOM   4238 O O    . MET A 1 276 ? 18.93500  6.12100   28.79900  1.000 57.41260  ? 276 MET A O    1 
ATOM   4239 C CB   . MET A 1 276 ? 16.14000  5.15300   29.04900  1.000 54.58523  ? 276 MET A CB   1 
ATOM   4240 C CG   . MET A 1 276 ? 15.22700  3.98500   29.35600  1.000 48.06134  ? 276 MET A CG   1 
ATOM   4241 S SD   . MET A 1 276 ? 14.43600  3.36000   27.86400  1.000 53.36866  ? 276 MET A SD   1 
ATOM   4242 C CE   . MET A 1 276 ? 13.12100  2.38600   28.60100  1.000 44.00892  ? 276 MET A CE   1 
ATOM   4243 H H    . MET A 1 276 ? 15.88600  6.64200   31.24400  1.000 65.37777  ? 276 MET A H    1 
ATOM   4244 H HA   . MET A 1 276 ? 17.56100  4.63600   30.41000  1.000 65.02356  ? 276 MET A HA   1 
ATOM   4245 H HB2  . MET A 1 276 ? 15.58400  5.93200   28.88800  1.000 65.50307  ? 276 MET A HB2  1 
ATOM   4246 H HB3  . MET A 1 276 ? 16.64300  4.93600   28.24900  1.000 65.50307  ? 276 MET A HB3  1 
ATOM   4247 H HG2  . MET A 1 276 ? 15.74700  3.26600   29.74900  1.000 57.67440  ? 276 MET A HG2  1 
ATOM   4248 H HG3  . MET A 1 276 ? 14.53400  4.27300   29.97000  1.000 57.67440  ? 276 MET A HG3  1 
ATOM   4249 H HE1  . MET A 1 276 ? 12.58000  2.00000   27.89500  1.000 52.81150  ? 276 MET A HE1  1 
ATOM   4250 H HE2  . MET A 1 276 ? 13.51700  1.68200   29.13700  1.000 52.81150  ? 276 MET A HE2  1 
ATOM   4251 H HE3  . MET A 1 276 ? 12.57600  2.96200   29.15900  1.000 52.81150  ? 276 MET A HE3  1 
ATOM   4252 N N    . ASN A 1 277 ? 18.27800  7.64400   30.36800  1.000 59.59074  ? 277 ASN A N    1 
ATOM   4253 C CA   . ASN A 1 277 ? 19.39300  8.53100   30.06200  1.000 60.71348  ? 277 ASN A CA   1 
ATOM   4254 C C    . ASN A 1 277 ? 19.53400  8.73600   28.55100  1.000 63.02145  ? 277 ASN A C    1 
ATOM   4255 O O    . ASN A 1 277 ? 20.63000  8.66900   27.98300  1.000 65.64365  ? 277 ASN A O    1 
ATOM   4256 C CB   . ASN A 1 277 ? 20.67400  7.97600   30.68000  1.000 64.41694  ? 277 ASN A CB   1 
ATOM   4257 C CG   . ASN A 1 277 ? 20.63500  7.99600   32.21200  1.000 70.82431  ? 277 ASN A CG   1 
ATOM   4258 O OD1  . ASN A 1 277 ? 20.47000  9.05300   32.83400  1.000 71.92147  ? 277 ASN A OD1  1 
ATOM   4259 N ND2  . ASN A 1 277 ? 20.73800  6.81100   32.82200  1.000 64.14866  ? 277 ASN A ND2  1 
ATOM   4260 H H    . ASN A 1 277 ? 17.71900  7.94200   30.94900  1.000 71.50968  ? 277 ASN A H    1 
ATOM   4261 H HA   . ASN A 1 277 ? 19.22200  9.39700   30.46300  1.000 72.85698  ? 277 ASN A HA   1 
ATOM   4262 H HB2  . ASN A 1 277 ? 20.79600  7.05800   30.39300  1.000 77.30113  ? 277 ASN A HB2  1 
ATOM   4263 H HB3  . ASN A 1 277 ? 21.42500  8.51700   30.39100  1.000 77.30113  ? 277 ASN A HB3  1 
ATOM   4264 H HD21 . ASN A 1 277 ? 20.71800  6.76600   33.68100  1.000 76.97919  ? 277 ASN A HD21 1 
ATOM   4265 H HD22 . ASN A 1 277 ? 20.84300  6.09500   32.35700  1.000 76.97919  ? 277 ASN A HD22 1 
ATOM   4266 N N    . GLY A 1 278 ? 18.39900  8.98100   27.89500  1.000 58.79071  ? 278 GLY A N    1 
ATOM   4267 C CA   . GLY A 1 278 ? 18.37600  9.29400   26.47800  1.000 63.30780  ? 278 GLY A CA   1 
ATOM   4268 C C    . GLY A 1 278 ? 18.46600  8.10900   25.53900  1.000 62.44168  ? 278 GLY A C    1 
ATOM   4269 O O    . GLY A 1 278 ? 18.39100  8.30100   24.31500  1.000 63.47006  ? 278 GLY A O    1 
ATOM   4270 H H    . GLY A 1 278 ? 17.62000  8.97000   28.26000  1.000 70.54965  ? 278 GLY A H    1 
ATOM   4271 H HA2  . GLY A 1 278 ? 17.55400  9.76800   26.27700  1.000 75.97016  ? 278 GLY A HA2  1 
ATOM   4272 H HA3  . GLY A 1 278 ? 19.11800  9.88600   26.27800  1.000 75.97016  ? 278 GLY A HA3  1 
ATOM   4273 N N    . ARG A 1 279 ? 18.61600  6.89600   26.05600  1.000 59.61429  ? 279 ARG A N    1 
ATOM   4274 C CA   . ARG A 1 279 ? 18.59700  5.72000   25.20500  1.000 55.40080  ? 279 ARG A CA   1 
ATOM   4275 C C    . ARG A 1 279 ? 17.15400  5.22100   25.11700  1.000 50.40271  ? 279 ARG A C    1 
ATOM   4276 O O    . ARG A 1 279 ? 16.23800  5.74700   25.75700  1.000 48.49853  ? 279 ARG A O    1 
ATOM   4277 C CB   . ARG A 1 279 ? 19.50700  4.60800   25.75500  1.000 55.29930  ? 279 ARG A CB   1 
ATOM   4278 C CG   . ARG A 1 279 ? 21.00300  4.93400   25.95500  1.000 54.41009  ? 279 ARG A CG   1 
ATOM   4279 C CD   . ARG A 1 279 ? 21.72600  3.73800   26.59600  1.000 57.05573  ? 279 ARG A CD   1 
ATOM   4280 N NE   . ARG A 1 279 ? 23.17100  3.92900   26.72000  1.000 61.68103  ? 279 ARG A NE   1 
ATOM   4281 C CZ   . ARG A 1 279 ? 24.06200  3.54900   25.81100  1.000 66.96519  ? 279 ARG A CZ   1 
ATOM   4282 N NH1  . ARG A 1 279 ? 23.69000  2.95200   24.68400  1.000 68.38274  ? 279 ARG A NH1  1 
ATOM   4283 N NH2  . ARG A 1 279 ? 25.35600  3.79000   26.02700  1.000 75.17881  ? 279 ARG A NH2  1 
ATOM   4284 H H    . ARG A 1 279 ? 18.73000  6.72900   26.89200  1.000 71.53795  ? 279 ARG A H    1 
ATOM   4285 H HA   . ARG A 1 279 ? 18.90000  5.95300   24.31400  1.000 66.48176  ? 279 ARG A HA   1 
ATOM   4286 H HB2  . ARG A 1 279 ? 19.15900  4.33700   26.61900  1.000 66.35996  ? 279 ARG A HB2  1 
ATOM   4287 H HB3  . ARG A 1 279 ? 19.46100  3.85500   25.14500  1.000 66.35996  ? 279 ARG A HB3  1 
ATOM   4288 H HG2  . ARG A 1 279 ? 21.41300  5.11700   25.09500  1.000 65.29291  ? 279 ARG A HG2  1 
ATOM   4289 H HG3  . ARG A 1 279 ? 21.09200  5.70000   26.54400  1.000 65.29291  ? 279 ARG A HG3  1 
ATOM   4290 H HD2  . ARG A 1 279 ? 21.33900  3.56900   27.46600  1.000 68.46768  ? 279 ARG A HD2  1 
ATOM   4291 H HD3  . ARG A 1 279 ? 21.57700  2.96000   26.03700  1.000 68.46768  ? 279 ARG A HD3  1 
ATOM   4292 H HE   . ARG A 1 279 ? 23.46200  4.33700   27.41900  1.000 74.01804  ? 279 ARG A HE   1 
ATOM   4293 H HH11 . ARG A 1 279 ? 22.86000  2.79300   24.52800  1.000 82.06009  ? 279 ARG A HH11 1 
ATOM   4294 H HH12 . ARG A 1 279 ? 24.28500  2.71800   24.10900  1.000 82.06009  ? 279 ARG A HH12 1 
ATOM   4295 H HH21 . ARG A 1 279 ? 25.60600  4.17800   26.75300  1.000 90.21537  ? 279 ARG A HH21 1 
ATOM   4296 H HH22 . ARG A 1 279 ? 25.94100  3.55000   25.44400  1.000 90.21537  ? 279 ARG A HH22 1 
ATOM   4297 N N    . THR A 1 280 ? 16.94500  4.23600   24.26600  1.000 50.68909  ? 280 THR A N    1 
ATOM   4298 C CA   . THR A 1 280 ? 15.64400  3.60500   24.15100  1.000 48.12063  ? 280 THR A CA   1 
ATOM   4299 C C    . THR A 1 280 ? 15.81700  2.09900   24.24800  1.000 44.81703  ? 280 THR A C    1 
ATOM   4300 O O    . THR A 1 280 ? 16.92700  1.56600   24.12400  1.000 42.86519  ? 280 THR A O    1 
ATOM   4301 C CB   . THR A 1 280 ? 14.96500  4.01300   22.85400  1.000 46.40903  ? 280 THR A CB   1 
ATOM   4302 O OG1  . THR A 1 280 ? 15.84100  3.71000   21.76900  1.000 43.41521  ? 280 THR A OG1  1 
ATOM   4303 C CG2  . THR A 1 280 ? 14.70000  5.51600   22.87300  1.000 47.94184  ? 280 THR A CG2  1 
ATOM   4304 H H    . THR A 1 280 ? 17.54300  3.91100   23.74000  1.000 60.82771  ? 280 THR A H    1 
ATOM   4305 H HA   . THR A 1 280 ? 15.08000  3.88800   24.88700  1.000 57.74555  ? 280 THR A HA   1 
ATOM   4306 H HB   . THR A 1 280 ? 14.12400  3.54000   22.75000  1.000 55.69163  ? 280 THR A HB   1 
ATOM   4307 H HG1  . THR A 1 280 ? 15.48300  3.92900   21.04100  1.000 52.09906  ? 280 THR A HG1  1 
ATOM   4308 H HG21 . THR A 1 280 ? 14.22000  5.77800   22.07200  1.000 57.53101  ? 280 THR A HG21 1 
ATOM   4309 H HG22 . THR A 1 280 ? 14.16700  5.74800   23.64900  1.000 57.53101  ? 280 THR A HG22 1 
ATOM   4310 H HG23 . THR A 1 280 ? 15.53900  6.00100   22.91000  1.000 57.53101  ? 280 THR A HG23 1 
ATOM   4311 N N    . ILE A 1 281 ? 14.71000  1.41600   24.51200  1.000 37.08454  ? 281 ILE A N    1 
ATOM   4312 C CA   . ILE A 1 281 ? 14.67000  -0.03500  24.45600  1.000 39.34663  ? 281 ILE A CA   1 
ATOM   4313 C C    . ILE A 1 281 ? 13.54700  -0.40400  23.50200  1.000 39.19650  ? 281 ILE A C    1 
ATOM   4314 O O    . ILE A 1 281 ? 12.40500  0.06000   23.66300  1.000 36.00099  ? 281 ILE A O    1 
ATOM   4315 C CB   . ILE A 1 281 ? 14.46800  -0.67400  25.84300  1.000 40.22373  ? 281 ILE A CB   1 
ATOM   4316 C CG1  . ILE A 1 281 ? 15.63400  -0.32000  26.75100  1.000 40.18111  ? 281 ILE A CG1  1 
ATOM   4317 C CG2  . ILE A 1 281 ? 14.30400  -2.19600  25.71400  1.000 37.55190  ? 281 ILE A CG2  1 
ATOM   4318 C CD1  . ILE A 1 281 ? 15.49200  -0.78900  28.18500  1.000 38.71266  ? 281 ILE A CD1  1 
ATOM   4319 H H    . ILE A 1 281 ? 13.96000  1.77700   24.72900  1.000 44.50225  ? 281 ILE A H    1 
ATOM   4320 H HA   . ILE A 1 281 ? 15.50300  -0.36800  24.08700  1.000 47.21675  ? 281 ILE A HA   1 
ATOM   4321 H HB   . ILE A 1 281 ? 13.65900  -0.30800  26.23100  1.000 48.26928  ? 281 ILE A HB   1 
ATOM   4322 H HG12 . ILE A 1 281 ? 16.44000  -0.72200  26.39000  1.000 48.21813  ? 281 ILE A HG12 1 
ATOM   4323 H HG13 . ILE A 1 281 ? 15.73200  0.64500   26.76800  1.000 48.21813  ? 281 ILE A HG13 1 
ATOM   4324 H HG21 . ILE A 1 281 ? 14.28700  -2.59100  26.59900  1.000 45.06308  ? 281 ILE A HG21 1 
ATOM   4325 H HG22 . ILE A 1 281 ? 13.47200  -2.39000  25.25600  1.000 45.06308  ? 281 ILE A HG22 1 
ATOM   4326 H HG23 . ILE A 1 281 ? 15.05200  -2.55100  25.20800  1.000 45.06308  ? 281 ILE A HG23 1 
ATOM   4327 H HD11 . ILE A 1 281 ? 16.17700  -0.36400  28.72500  1.000 46.45599  ? 281 ILE A HD11 1 
ATOM   4328 H HD12 . ILE A 1 281 ? 14.61300  -0.54100  28.51200  1.000 46.45599  ? 281 ILE A HD12 1 
ATOM   4329 H HD13 . ILE A 1 281 ? 15.59700  -1.75300  28.21600  1.000 46.45599  ? 281 ILE A HD13 1 
ATOM   4330 N N    . LEU A 1 282 ? 13.88100  -1.18400  22.47000  1.000 35.84843  ? 282 LEU A N    1 
ATOM   4331 C CA   . LEU A 1 282 ? 12.88700  -1.56900  21.45800  1.000 40.62643  ? 282 LEU A CA   1 
ATOM   4332 C C    . LEU A 1 282 ? 12.09400  -0.35300  20.99400  1.000 40.92255  ? 282 LEU A C    1 
ATOM   4333 O O    . LEU A 1 282 ? 10.86500  -0.37100  20.93100  1.000 39.30451  ? 282 LEU A O    1 
ATOM   4334 C CB   . LEU A 1 282 ? 11.95500  -2.65100  21.99300  1.000 37.68964  ? 282 LEU A CB   1 
ATOM   4335 C CG   . LEU A 1 282 ? 12.67200  -3.98700  22.05300  1.000 35.37270  ? 282 LEU A CG   1 
ATOM   4336 C CD1  . LEU A 1 282 ? 11.73300  -4.97500  22.70500  1.000 35.62070  ? 282 LEU A CD1  1 
ATOM   4337 C CD2  . LEU A 1 282 ? 13.10600  -4.40500  20.63600  1.000 38.39831  ? 282 LEU A CD2  1 
ATOM   4338 H H    . LEU A 1 282 ? 14.66800  -1.50200  22.33200  1.000 43.01892  ? 282 LEU A H    1 
ATOM   4339 H HA   . LEU A 1 282 ? 13.35500  -1.90800  20.68200  1.000 48.75251  ? 282 LEU A HA   1 
ATOM   4340 H HB2  . LEU A 1 282 ? 11.66700  -2.41600  22.88900  1.000 45.22836  ? 282 LEU A HB2  1 
ATOM   4341 H HB3  . LEU A 1 282 ? 11.19000  -2.74100  21.40400  1.000 45.22836  ? 282 LEU A HB3  1 
ATOM   4342 H HG   . LEU A 1 282 ? 13.46500  -3.90400  22.60600  1.000 42.44804  ? 282 LEU A HG   1 
ATOM   4343 H HD11 . LEU A 1 282 ? 12.16700  -5.84100  22.74800  1.000 42.74564  ? 282 LEU A HD11 1 
ATOM   4344 H HD12 . LEU A 1 282 ? 11.52100  -4.66600  23.60000  1.000 42.74564  ? 282 LEU A HD12 1 
ATOM   4345 H HD13 . LEU A 1 282 ? 10.92300  -5.03700  22.17500  1.000 42.74564  ? 282 LEU A HD13 1 
ATOM   4346 H HD21 . LEU A 1 282 ? 13.15600  -5.37300  20.59500  1.000 46.07877  ? 282 LEU A HD21 1 
ATOM   4347 H HD22 . LEU A 1 282 ? 12.45300  -4.08000  19.99700  1.000 46.07877  ? 282 LEU A HD22 1 
ATOM   4348 H HD23 . LEU A 1 282 ? 13.97600  -4.02100  20.44400  1.000 46.07877  ? 282 LEU A HD23 1 
ATOM   4349 N N    . GLY A 1 283 ? 12.79400  0.75600   20.78700  1.000 38.80391  ? 283 GLY A N    1 
ATOM   4350 C CA   . GLY A 1 283 ? 12.15300  1.93800   20.24700  1.000 46.08523  ? 283 GLY A CA   1 
ATOM   4351 C C    . GLY A 1 283 ? 11.30400  2.72400   21.22200  1.000 47.75360  ? 283 GLY A C    1 
ATOM   4352 O O    . GLY A 1 283 ? 10.63300  3.67400   20.81100  1.000 50.22718  ? 283 GLY A O    1 
ATOM   4353 H H    . GLY A 1 283 ? 13.63400  0.84600   20.95000  1.000 46.56550  ? 283 GLY A H    1 
ATOM   4354 H HA2  . GLY A 1 283 ? 12.83600  2.53400   19.90200  1.000 55.30308  ? 283 GLY A HA2  1 
ATOM   4355 H HA3  . GLY A 1 283 ? 11.58600  1.67400   19.50600  1.000 55.30308  ? 283 GLY A HA3  1 
ATOM   4356 N N    . SER A 1 284 ? 11.34200  2.39400   22.51400  1.000 39.88195  ? 284 SER A N    1 
ATOM   4357 C CA   . SER A 1 284 ? 10.55700  3.08500   23.51200  1.000 40.04851  ? 284 SER A CA   1 
ATOM   4358 C C    . SER A 1 284 ? 11.47400  3.70600   24.56200  1.000 43.31798  ? 284 SER A C    1 
ATOM   4359 O O    . SER A 1 284 ? 12.51600  3.13600   24.91600  1.000 39.42029  ? 284 SER A O    1 
ATOM   4360 C CB   . SER A 1 284 ? 9.54800   2.11600   24.14100  1.000 41.47070  ? 284 SER A CB   1 
ATOM   4361 O OG   . SER A 1 284 ? 8.87600   2.76700   25.20100  1.000 45.47464  ? 284 SER A OG   1 
ATOM   4362 H H    . SER A 1 284 ? 11.82700  1.76000   22.83400  1.000 47.85914  ? 284 SER A H    1 
ATOM   4363 H HA   . SER A 1 284 ? 10.05800  3.80200   23.09100  1.000 48.05901  ? 284 SER A HA   1 
ATOM   4364 H HB2  . SER A 1 284 ? 8.90200   1.84500   23.47000  1.000 49.76564  ? 284 SER A HB2  1 
ATOM   4365 H HB3  . SER A 1 284 ? 10.01900  1.34200   24.48700  1.000 49.76564  ? 284 SER A HB3  1 
ATOM   4366 H HG   . SER A 1 284 ? 9.28900   2.63800   25.92100  1.000 54.57036  ? 284 SER A HG   1 
ATOM   4367 N N    . ALA A 1 285 ? 11.10500  4.89900   25.03000  1.000 41.54050  ? 285 ALA A N    1 
ATOM   4368 C CA   . ALA A 1 285 ? 11.84100  5.57400   26.08500  1.000 39.96088  ? 285 ALA A CA   1 
ATOM   4369 C C    . ALA A 1 285 ? 11.21900  5.33000   27.44300  1.000 42.34754  ? 285 ALA A C    1 
ATOM   4370 O O    . ALA A 1 285 ? 11.62600  5.95800   28.41500  1.000 40.05547  ? 285 ALA A O    1 
ATOM   4371 C CB   . ALA A 1 285 ? 11.92000  7.07800   25.80900  1.000 42.74059  ? 285 ALA A CB   1 
ATOM   4372 H H    . ALA A 1 285 ? 10.42300  5.33900   24.74600  1.000 49.84940  ? 285 ALA A H    1 
ATOM   4373 H HA   . ALA A 1 285 ? 12.74700  5.23000   26.10700  1.000 47.95386  ? 285 ALA A HA   1 
ATOM   4374 H HB1  . ALA A 1 285 ? 12.39900  7.50700   26.53500  1.000 51.28951  ? 285 ALA A HB1  1 
ATOM   4375 H HB2  . ALA A 1 285 ? 12.38900  7.22100   24.97200  1.000 51.28951  ? 285 ALA A HB2  1 
ATOM   4376 H HB3  . ALA A 1 285 ? 11.02000  7.43500   25.74900  1.000 51.28951  ? 285 ALA A HB3  1 
ATOM   4377 N N    . LEU A 1 286 ? 10.20200  4.48500   27.52900  1.000 40.58458  ? 286 LEU A N    1 
ATOM   4378 C CA   . LEU A 1 286 ? 9.72500   4.04400   28.83800  1.000 42.15932  ? 286 LEU A CA   1 
ATOM   4379 C C    . LEU A 1 286 ? 9.53400   2.53100   28.85500  1.000 35.27341  ? 286 LEU A C    1 
ATOM   4380 O O    . LEU A 1 286 ? 9.62900   1.84900   27.82800  1.000 35.87997  ? 286 LEU A O    1 
ATOM   4381 C CB   . LEU A 1 286 ? 8.46000   4.78100   29.25700  1.000 37.72999  ? 286 LEU A CB   1 
ATOM   4382 C CG   . LEU A 1 286 ? 7.35300   5.09200   28.29400  1.000 49.02581  ? 286 LEU A CG   1 
ATOM   4383 C CD1  . LEU A 1 286 ? 6.58700   3.84200   28.01300  1.000 50.73484  ? 286 LEU A CD1  1 
ATOM   4384 C CD2  . LEU A 1 286 ? 6.45800   6.18100   28.90000  1.000 46.88729  ? 286 LEU A CD2  1 
ATOM   4385 H H    . LEU A 1 286 ? 9.77200   4.15900   26.86100  1.000 48.70230  ? 286 LEU A H    1 
ATOM   4386 H HA   . LEU A 1 286 ? 10.40600  4.24900   29.49800  1.000 50.59199  ? 286 LEU A HA   1 
ATOM   4387 H HB2  . LEU A 1 286 ? 8.05500   4.26600   29.97200  1.000 45.27679  ? 286 LEU A HB2  1 
ATOM   4388 H HB3  . LEU A 1 286 ? 8.74200   5.63500   29.62100  1.000 45.27679  ? 286 LEU A HB3  1 
ATOM   4389 H HG   . LEU A 1 286 ? 7.72600   5.42300   27.46200  1.000 58.83177  ? 286 LEU A HG   1 
ATOM   4390 H HD11 . LEU A 1 286 ? 5.85400   4.05100   27.41300  1.000 60.88261  ? 286 LEU A HD11 1 
ATOM   4391 H HD12 . LEU A 1 286 ? 7.17900   3.19500   27.59900  1.000 60.88261  ? 286 LEU A HD12 1 
ATOM   4392 H HD13 . LEU A 1 286 ? 6.24000   3.48800   28.84700  1.000 60.88261  ? 286 LEU A HD13 1 
ATOM   4393 H HD21 . LEU A 1 286 ? 5.71500   6.34900   28.29900  1.000 56.26555  ? 286 LEU A HD21 1 
ATOM   4394 H HD22 . LEU A 1 286 ? 6.12700   5.87500   29.75900  1.000 56.26555  ? 286 LEU A HD22 1 
ATOM   4395 H HD23 . LEU A 1 286 ? 6.97900   6.99100   29.01500  1.000 56.26555  ? 286 LEU A HD23 1 
ATOM   4396 N N    . LEU A 1 287 ? 9.30400   2.00200   30.05000  1.000 30.26249  ? 287 LEU A N    1 
ATOM   4397 C CA   . LEU A 1 287 ? 9.26100   0.55900   30.22300  1.000 33.22796  ? 287 LEU A CA   1 
ATOM   4398 C C    . LEU A 1 287 ? 7.87500   0.05500   29.83900  1.000 30.90529  ? 287 LEU A C    1 
ATOM   4399 O O    . LEU A 1 287 ? 6.89300   0.38200   30.51000  1.000 35.74882  ? 287 LEU A O    1 
ATOM   4400 C CB   . LEU A 1 287 ? 9.60100   0.19500   31.66900  1.000 30.89390  ? 287 LEU A CB   1 
ATOM   4401 C CG   . LEU A 1 287 ? 10.98700  0.73200   32.07900  1.000 35.47328  ? 287 LEU A CG   1 
ATOM   4402 C CD1  . LEU A 1 287 ? 11.28400  0.43600   33.54200  1.000 38.50812  ? 287 LEU A CD1  1 
ATOM   4403 C CD2  . LEU A 1 287 ? 12.08300  0.17000   31.17400  1.000 38.69993  ? 287 LEU A CD2  1 
ATOM   4404 H H    . LEU A 1 287 ? 9.17100   2.45300   30.77000  1.000 36.31578  ? 287 LEU A H    1 
ATOM   4405 H HA   . LEU A 1 287 ? 9.90700   0.14100   29.63300  1.000 39.87436  ? 287 LEU A HA   1 
ATOM   4406 H HB2  . LEU A 1 287 ? 8.93800   0.58300   32.26100  1.000 37.07348  ? 287 LEU A HB2  1 
ATOM   4407 H HB3  . LEU A 1 287 ? 9.61000   -0.77000  31.76200  1.000 37.07348  ? 287 LEU A HB3  1 
ATOM   4408 H HG   . LEU A 1 287 ? 10.98800  1.69600   31.97300  1.000 42.56873  ? 287 LEU A HG   1 
ATOM   4409 H HD11 . LEU A 1 287 ? 12.16200  0.78500   33.76300  1.000 46.21054  ? 287 LEU A HD11 1 
ATOM   4410 H HD12 . LEU A 1 287 ? 10.60900  0.86300   34.09300  1.000 46.21054  ? 287 LEU A HD12 1 
ATOM   4411 H HD13 . LEU A 1 287 ? 11.26500  -0.52400  33.67900  1.000 46.21054  ? 287 LEU A HD13 1 
ATOM   4412 H HD21 . LEU A 1 287 ? 12.94800  0.41400   31.53800  1.000 46.44071  ? 287 LEU A HD21 1 
ATOM   4413 H HD22 . LEU A 1 287 ? 11.99900  -0.79600  31.14100  1.000 46.44071  ? 287 LEU A HD22 1 
ATOM   4414 H HD23 . LEU A 1 287 ? 11.98300  0.54100   30.28500  1.000 46.44071  ? 287 LEU A HD23 1 
ATOM   4415 N N    . GLU A 1 288 ? 7.81200   -0.75200  28.79800  1.000 30.03469  ? 288 GLU A N    1 
ATOM   4416 C CA   . GLU A 1 288 ? 6.55000   -1.21600  28.21300  1.000 30.09026  ? 288 GLU A CA   1 
ATOM   4417 C C    . GLU A 1 288 ? 5.98500   -2.41500  28.97000  1.000 26.85923  ? 288 GLU A C    1 
ATOM   4418 O O    . GLU A 1 288 ? 6.72300   -3.37800  29.22600  1.000 23.93278  ? 288 GLU A O    1 
ATOM   4419 C CB   . GLU A 1 288 ? 6.81600   -1.62800  26.77100  1.000 30.39087  ? 288 GLU A CB   1 
ATOM   4420 C CG   . GLU A 1 288 ? 5.59000   -2.29100  26.17000  1.000 43.62120  ? 288 GLU A CG   1 
ATOM   4421 C CD   . GLU A 1 288 ? 4.40600   -1.31100  26.01000  1.000 47.80391  ? 288 GLU A CD   1 
ATOM   4422 O OE1  . GLU A 1 288 ? 4.67400   -0.13000  25.62200  1.000 47.74399  ? 288 GLU A OE1  1 
ATOM   4423 O OE2  . GLU A 1 288 ? 3.22800   -1.73500  26.28100  1.000 37.59278  ? 288 GLU A OE2  1 
ATOM   4424 H H    . GLU A 1 288 ? 8.50600   -1.05900  28.39300  1.000 36.04243  ? 288 GLU A H    1 
ATOM   4425 H HA   . GLU A 1 288 ? 5.89700   -0.49900  28.22300  1.000 36.10912  ? 288 GLU A HA   1 
ATOM   4426 H HB2  . GLU A 1 288 ? 7.04500   -0.85000  26.24500  1.000 36.46985  ? 288 GLU A HB2  1 
ATOM   4427 H HB3  . GLU A 1 288 ? 7.53800   -2.27100  26.75600  1.000 36.46985  ? 288 GLU A HB3  1 
ATOM   4428 H HG2  . GLU A 1 288 ? 5.83600   -2.58000  25.28300  1.000 52.34625  ? 288 GLU A HG2  1 
ATOM   4429 H HG3  . GLU A 1 288 ? 5.30200   -3.05500  26.69000  1.000 52.34625  ? 288 GLU A HG3  1 
ATOM   4430 N N    . ASP A 1 289 ? 4.66400   -2.40500  29.29500  1.000 28.15521  ? 289 ASP A N    1 
ATOM   4431 C CA   . ASP A 1 289 ? 4.13200   -3.51200  30.09000  1.000 24.40185  ? 289 ASP A CA   1 
ATOM   4432 C C    . ASP A 1 289 ? 2.90100   -4.16200  29.48700  1.000 25.74538  ? 289 ASP A C    1 
ATOM   4433 O O    . ASP A 1 289 ? 2.19300   -4.90500  30.17800  1.000 23.99609  ? 289 ASP A O    1 
ATOM   4434 C CB   . ASP A 1 289 ? 3.84700   -3.06100  31.54500  1.000 26.65355  ? 289 ASP A CB   1 
ATOM   4435 C CG   . ASP A 1 289 ? 2.55100   -2.23500  31.70000  1.000 26.67787  ? 289 ASP A CG   1 
ATOM   4436 O OD1  . ASP A 1 289 ? 1.98900   -1.70900  30.68500  1.000 26.45208  ? 289 ASP A OD1  1 
ATOM   4437 O OD2  . ASP A 1 289 ? 2.10200   -2.09800  32.87300  1.000 25.87248  ? 289 ASP A OD2  1 
ATOM   4438 H H    . ASP A 1 289 ? 4.09500   -1.79900  29.07500  1.000 33.78705  ? 289 ASP A H    1 
ATOM   4439 H HA   . ASP A 1 289 ? 4.80700   -4.20500  30.14300  1.000 29.28302  ? 289 ASP A HA   1 
ATOM   4440 H HB2  . ASP A 1 289 ? 3.76600   -3.84800  32.10600  1.000 31.98506  ? 289 ASP A HB2  1 
ATOM   4441 H HB3  . ASP A 1 289 ? 4.58500   -2.51200  31.85200  1.000 31.98506  ? 289 ASP A HB3  1 
ATOM   4442 N N    . GLU A 1 290 ? 2.65300   -3.97500  28.19300  1.000 24.54998  ? 290 GLU A N    1 
ATOM   4443 C CA   . GLU A 1 290 ? 1.50800   -4.64200  27.56800  1.000 24.35889  ? 290 GLU A CA   1 
ATOM   4444 C C    . GLU A 1 290 ? 1.94900   -5.68700  26.52900  1.000 24.57879  ? 290 GLU A C    1 
ATOM   4445 O O    . GLU A 1 290 ? 1.23100   -5.98300  25.55900  1.000 24.74162  ? 290 GLU A O    1 
ATOM   4446 C CB   . GLU A 1 290 ? 0.55800   -3.56700  27.01200  1.000 26.63391  ? 290 GLU A CB   1 
ATOM   4447 C CG   . GLU A 1 290 ? -0.02900  -2.73100  28.17100  1.000 31.40273  ? 290 GLU A CG   1 
ATOM   4448 C CD   . GLU A 1 290 ? -1.36800  -2.01700  27.82900  1.000 28.53600  ? 290 GLU A CD   1 
ATOM   4449 O OE1  . GLU A 1 290 ? -1.69800  -1.94900  26.62600  1.000 29.36111  ? 290 GLU A OE1  1 
ATOM   4450 O OE2  . GLU A 1 290 ? -2.05500  -1.50600  28.76300  1.000 26.86190  ? 290 GLU A OE2  1 
ATOM   4451 H H    . GLU A 1 290 ? 3.11800   -3.48100  27.66500  1.000 29.46077  ? 290 GLU A H    1 
ATOM   4452 H HA   . GLU A 1 290 ? 1.01400   -5.12300  28.24900  1.000 29.23146  ? 290 GLU A HA   1 
ATOM   4453 H HB2  . GLU A 1 290 ? 1.04800   -2.97400  26.42100  1.000 31.96150  ? 290 GLU A HB2  1 
ATOM   4454 H HB3  . GLU A 1 290 ? -0.17300  -3.99300  26.53800  1.000 31.96150  ? 290 GLU A HB3  1 
ATOM   4455 H HG2  . GLU A 1 290 ? -0.19200  -3.31600  28.92700  1.000 37.68407  ? 290 GLU A HG2  1 
ATOM   4456 H HG3  . GLU A 1 290 ? 0.61400   -2.04800  28.41900  1.000 37.68407  ? 290 GLU A HG3  1 
ATOM   4457 N N    . PHE A 1 291 ? 3.11600   -6.30900  26.74300  1.000 23.09442  ? 291 PHE A N    1 
ATOM   4458 C CA   . PHE A 1 291 ? 3.50400   -7.53500  26.04600  1.000 24.24989  ? 291 PHE A CA   1 
ATOM   4459 C C    . PHE A 1 291 ? 3.69100   -8.64400  27.08500  1.000 22.96096  ? 291 PHE A C    1 
ATOM   4460 O O    . PHE A 1 291 ? 4.57200   -8.53300  27.93900  1.000 24.18838  ? 291 PHE A O    1 
ATOM   4461 C CB   . PHE A 1 291 ? 4.82500   -7.36100  25.26700  1.000 23.54419  ? 291 PHE A CB   1 
ATOM   4462 C CG   . PHE A 1 291 ? 4.74600   -6.34400  24.16000  1.000 29.30513  ? 291 PHE A CG   1 
ATOM   4463 C CD1  . PHE A 1 291 ? 4.21800   -6.69800  22.93000  1.000 31.26442  ? 291 PHE A CD1  1 
ATOM   4464 C CD2  . PHE A 1 291 ? 5.28200   -5.06700  24.31300  1.000 28.25107  ? 291 PHE A CD2  1 
ATOM   4465 C CE1  . PHE A 1 291 ? 4.19300   -5.75800  21.86100  1.000 33.58639  ? 291 PHE A CE1  1 
ATOM   4466 C CE2  . PHE A 1 291 ? 5.26300   -4.13800  23.29300  1.000 33.88719  ? 291 PHE A CE2  1 
ATOM   4467 C CZ   . PHE A 1 291 ? 4.69900   -4.48200  22.04700  1.000 34.51350  ? 291 PHE A CZ   1 
ATOM   4468 H H    . PHE A 1 291 ? 3.71000   -6.03100  27.30000  1.000 27.71411  ? 291 PHE A H    1 
ATOM   4469 H HA   . PHE A 1 291 ? 2.80700   -7.80100  25.42600  1.000 29.10067  ? 291 PHE A HA   1 
ATOM   4470 H HB2  . PHE A 1 291 ? 5.51700   -7.07500  25.88400  1.000 28.25383  ? 291 PHE A HB2  1 
ATOM   4471 H HB3  . PHE A 1 291 ? 5.06900   -8.21200  24.87100  1.000 28.25383  ? 291 PHE A HB3  1 
ATOM   4472 H HD1  . PHE A 1 291 ? 3.87300   -7.55200  22.80300  1.000 37.51810  ? 291 PHE A HD1  1 
ATOM   4473 H HD2  . PHE A 1 291 ? 5.65200   -4.82900  25.13200  1.000 33.90209  ? 291 PHE A HD2  1 
ATOM   4474 H HE1  . PHE A 1 291 ? 3.81700   -5.99400  21.04400  1.000 40.30447  ? 291 PHE A HE1  1 
ATOM   4475 H HE2  . PHE A 1 291 ? 5.60900   -3.28600  23.42600  1.000 40.66543  ? 291 PHE A HE2  1 
ATOM   4476 H HZ   . PHE A 1 291 ? 4.68000   -3.86300  21.35300  1.000 41.41700  ? 291 PHE A HZ   1 
ATOM   4477 N N    . THR A 1 292 ? 2.94200   -9.75000  26.95700  1.000 26.35857  ? 292 THR A N    1 
ATOM   4478 C CA   . THR A 1 292 ? 3.12200   -10.88500 27.86400  1.000 24.17342  ? 292 THR A CA   1 
ATOM   4479 C C    . THR A 1 292 ? 4.28600   -11.76800 27.43200  1.000 25.90172  ? 292 THR A C    1 
ATOM   4480 O O    . THR A 1 292 ? 4.78200   -11.67800 26.30000  1.000 25.13554  ? 292 THR A O    1 
ATOM   4481 C CB   . THR A 1 292 ? 1.88200   -11.76100 27.92300  1.000 23.57737  ? 292 THR A CB   1 
ATOM   4482 O OG1  . THR A 1 292 ? 1.73400   -12.42800 26.66200  1.000 25.56374  ? 292 THR A OG1  1 
ATOM   4483 C CG2  . THR A 1 292 ? 0.59200   -10.89300 28.09700  1.000 27.25214  ? 292 THR A CG2  1 
ATOM   4484 H H    . THR A 1 292 ? 2.33300   -9.86300  26.36100  1.000 31.63109  ? 292 THR A H    1 
ATOM   4485 H HA   . THR A 1 292 ? 3.29800   -10.54500 28.75400  1.000 29.00890  ? 292 THR A HA   1 
ATOM   4486 H HB   . THR A 1 292 ? 1.94500   -12.40400 28.64600  1.000 28.29365  ? 292 THR A HB   1 
ATOM   4487 H HG1  . THR A 1 292 ? 1.05200   -12.91800 26.67500  1.000 30.67729  ? 292 THR A HG1  1 
ATOM   4488 H HG21 . THR A 1 292 ? -0.17200  -11.46600 28.26800  1.000 32.70337  ? 292 THR A HG21 1 
ATOM   4489 H HG22 . THR A 1 292 ? 0.70100   -10.28300 28.84300  1.000 32.70337  ? 292 THR A HG22 1 
ATOM   4490 H HG23 . THR A 1 292 ? 0.42700   -10.37900 27.29100  1.000 32.70337  ? 292 THR A HG23 1 
ATOM   4491 N N    . PRO A 1 293 ? 4.75500   -12.61900 28.33200  1.000 24.81967  ? 293 PRO A N    1 
ATOM   4492 C CA   . PRO A 1 293 ? 5.75200   -13.63000 27.94600  1.000 27.37845  ? 293 PRO A CA   1 
ATOM   4493 C C    . PRO A 1 293 ? 5.31300   -14.42400 26.72100  1.000 32.01391  ? 293 PRO A C    1 
ATOM   4494 O O    . PRO A 1 293 ? 6.12500   -14.77500 25.86400  1.000 28.66248  ? 293 PRO A O    1 
ATOM   4495 C CB   . PRO A 1 293 ? 5.86000   -14.48900 29.21000  1.000 29.46915  ? 293 PRO A CB   1 
ATOM   4496 C CG   . PRO A 1 293 ? 5.61800   -13.48400 30.34000  1.000 29.57614  ? 293 PRO A CG   1 
ATOM   4497 C CD   . PRO A 1 293 ? 4.52100   -12.58900 29.79900  1.000 26.35505  ? 293 PRO A CD   1 
ATOM   4498 H HA   . PRO A 1 293 ? 6.60800   -13.21000 27.76800  1.000 32.85494  ? 293 PRO A HA   1 
ATOM   4499 H HB2  . PRO A 1 293 ? 5.17600   -15.17700 29.20300  1.000 35.36379  ? 293 PRO A HB2  1 
ATOM   4500 H HB3  . PRO A 1 293 ? 6.74700   -14.87700 29.27300  1.000 35.36379  ? 293 PRO A HB3  1 
ATOM   4501 H HG2  . PRO A 1 293 ? 5.32100   -13.95100 31.13700  1.000 35.49217  ? 293 PRO A HG2  1 
ATOM   4502 H HG3  . PRO A 1 293 ? 6.42700   -12.98100 30.51600  1.000 35.49217  ? 293 PRO A HG3  1 
ATOM   4503 H HD2  . PRO A 1 293 ? 3.64900   -12.95600 30.01300  1.000 31.62686  ? 293 PRO A HD2  1 
ATOM   4504 H HD3  . PRO A 1 293 ? 4.62300   -11.68800 30.14200  1.000 31.62686  ? 293 PRO A HD3  1 
ATOM   4505 N N    . PHE A 1 294 ? 4.02900   -14.74800 26.63800  1.000 28.69137  ? 294 PHE A N    1 
ATOM   4506 C CA   . PHE A 1 294 ? 3.53800   -15.46500 25.46900  1.000 30.25467  ? 294 PHE A CA   1 
ATOM   4507 C C    . PHE A 1 294 ? 3.60200   -14.58000 24.22000  1.000 28.73652  ? 294 PHE A C    1 
ATOM   4508 O O    . PHE A 1 294 ? 3.92700   -15.05200 23.12600  1.000 29.92484  ? 294 PHE A O    1 
ATOM   4509 C CB   . PHE A 1 294 ? 2.10500   -15.92600 25.78400  1.000 33.97867  ? 294 PHE A CB   1 
ATOM   4510 C CG   . PHE A 1 294 ? 1.49700   -16.83200 24.75000  1.000 38.53153  ? 294 PHE A CG   1 
ATOM   4511 C CD1  . PHE A 1 294 ? 0.98800   -16.32300 23.57000  1.000 38.92579  ? 294 PHE A CD1  1 
ATOM   4512 C CD2  . PHE A 1 294 ? 1.40200   -18.20500 24.98000  1.000 42.70108  ? 294 PHE A CD2  1 
ATOM   4513 C CE1  . PHE A 1 294 ? 0.42000   -17.16500 22.60400  1.000 38.04214  ? 294 PHE A CE1  1 
ATOM   4514 C CE2  . PHE A 1 294 ? 0.81400   -19.05100 24.01800  1.000 43.70437  ? 294 PHE A CE2  1 
ATOM   4515 C CZ   . PHE A 1 294 ? 0.33900   -18.52200 22.83100  1.000 43.22709  ? 294 PHE A CZ   1 
ATOM   4516 H H    . PHE A 1 294 ? 3.43200   -14.56900 27.23100  1.000 34.43044  ? 294 PHE A H    1 
ATOM   4517 H HA   . PHE A 1 294 ? 4.08700   -16.25000 25.31700  1.000 36.30640  ? 294 PHE A HA   1 
ATOM   4518 H HB2  . PHE A 1 294 ? 2.11200   -16.40600 26.62700  1.000 40.77521  ? 294 PHE A HB2  1 
ATOM   4519 H HB3  . PHE A 1 294 ? 1.53700   -15.14300 25.85900  1.000 40.77521  ? 294 PHE A HB3  1 
ATOM   4520 H HD1  . PHE A 1 294 ? 1.04700   -15.41000 23.40300  1.000 46.71175  ? 294 PHE A HD1  1 
ATOM   4521 H HD2  . PHE A 1 294 ? 1.72900   -18.56400 25.77300  1.000 51.24210  ? 294 PHE A HD2  1 
ATOM   4522 H HE1  . PHE A 1 294 ? 0.09000   -16.80600 21.81200  1.000 45.65137  ? 294 PHE A HE1  1 
ATOM   4523 H HE2  . PHE A 1 294 ? 0.76500   -19.96700 24.17200  1.000 52.44605  ? 294 PHE A HE2  1 
ATOM   4524 H HZ   . PHE A 1 294 ? -0.04800  -19.07900 22.19400  1.000 51.87331  ? 294 PHE A HZ   1 
ATOM   4525 N N    . ASP A 1 295 ? 3.27300   -13.29800 24.36000  1.000 26.90698  ? 295 ASP A N    1 
ATOM   4526 C CA   . ASP A 1 295 ? 3.31200   -12.40800 23.20700  1.000 28.98918  ? 295 ASP A CA   1 
ATOM   4527 C C    . ASP A 1 295 ? 4.72100   -12.33600 22.63600  1.000 33.79558  ? 295 ASP A C    1 
ATOM   4528 O O    . ASP A 1 295 ? 4.91100   -12.22200 21.42100  1.000 29.76604  ? 295 ASP A O    1 
ATOM   4529 C CB   . ASP A 1 295 ? 2.87900   -10.99900 23.60900  1.000 24.87994  ? 295 ASP A CB   1 
ATOM   4530 C CG   . ASP A 1 295 ? 1.41600   -10.89800 23.95900  1.000 29.24892  ? 295 ASP A CG   1 
ATOM   4531 O OD1  . ASP A 1 295 ? 0.62700   -11.82500 23.60300  1.000 30.33831  ? 295 ASP A OD1  1 
ATOM   4532 O OD2  . ASP A 1 295 ? 1.08400   -9.86800  24.58500  1.000 27.69765  ? 295 ASP A OD2  1 
ATOM   4533 H H    . ASP A 1 295 ? 3.02900   -12.92600 25.09600  1.000 32.28918  ? 295 ASP A H    1 
ATOM   4534 H HA   . ASP A 1 295 ? 2.71200   -12.73500 22.51900  1.000 34.78782  ? 295 ASP A HA   1 
ATOM   4535 H HB2  . ASP A 1 295 ? 3.39100   -10.72300 24.38600  1.000 29.85673  ? 295 ASP A HB2  1 
ATOM   4536 H HB3  . ASP A 1 295 ? 3.05100   -10.39500 22.86900  1.000 29.85673  ? 295 ASP A HB3  1 
ATOM   4537 N N    . VAL A 1 296 ? 5.72000   -12.29300 23.51700  1.000 28.29664  ? 296 VAL A N    1 
ATOM   4538 C CA   . VAL A 1 296 ? 7.10000   -12.14600 23.06400  1.000 29.57212  ? 296 VAL A CA   1 
ATOM   4539 C C    . VAL A 1 296 ? 7.51000   -13.36100 22.27600  1.000 31.77149  ? 296 VAL A C    1 
ATOM   4540 O O    . VAL A 1 296 ? 8.12400   -13.24800 21.21400  1.000 32.22600  ? 296 VAL A O    1 
ATOM   4541 C CB   . VAL A 1 296 ? 8.02500   -11.91200 24.28100  1.000 27.67132  ? 296 VAL A CB   1 
ATOM   4542 C CG1  . VAL A 1 296 ? 9.49300   -11.98100 23.89300  1.000 31.78416  ? 296 VAL A CG1  1 
ATOM   4543 C CG2  . VAL A 1 296 ? 7.69100   -10.55500 24.88600  1.000 26.40693  ? 296 VAL A CG2  1 
ATOM   4544 H H    . VAL A 1 296 ? 5.62700   -12.34600 24.37000  1.000 33.95677  ? 296 VAL A H    1 
ATOM   4545 H HA   . VAL A 1 296 ? 7.16400   -11.37200 22.48200  1.000 35.48734  ? 296 VAL A HA   1 
ATOM   4546 H HB   . VAL A 1 296 ? 7.85400   -12.59400 24.94900  1.000 33.20639  ? 296 VAL A HB   1 
ATOM   4547 H HG11 . VAL A 1 296 ? 10.02700  -11.61900 24.61800  1.000 38.14180  ? 296 VAL A HG11 1 
ATOM   4548 H HG12 . VAL A 1 296 ? 9.73800   -12.90600 23.73400  1.000 38.14180  ? 296 VAL A HG12 1 
ATOM   4549 H HG13 . VAL A 1 296 ? 9.63100   -11.45700 23.08800  1.000 38.14180  ? 296 VAL A HG13 1 
ATOM   4550 H HG21 . VAL A 1 296 ? 8.28500   -10.38900 25.63500  1.000 31.68912  ? 296 VAL A HG21 1 
ATOM   4551 H HG22 . VAL A 1 296 ? 7.81100   -9.87000  24.21000  1.000 31.68912  ? 296 VAL A HG22 1 
ATOM   4552 H HG23 . VAL A 1 296 ? 6.77000   -10.56200 25.19000  1.000 31.68912  ? 296 VAL A HG23 1 
ATOM   4553 N N    . VAL A 1 297 ? 7.14600   -14.54500 22.76400  1.000 35.58086  ? 297 VAL A N    1 
ATOM   4554 C CA   . VAL A 1 297 ? 7.48600   -15.77700 22.06800  1.000 36.20872  ? 297 VAL A CA   1 
ATOM   4555 C C    . VAL A 1 297 ? 6.74600   -15.84400 20.73200  1.000 37.86092  ? 297 VAL A C    1 
ATOM   4556 O O    . VAL A 1 297 ? 7.29600   -16.29800 19.72200  1.000 43.55763  ? 297 VAL A O    1 
ATOM   4557 C CB   . VAL A 1 297 ? 7.19300   -16.98300 22.97100  1.000 33.69043  ? 297 VAL A CB   1 
ATOM   4558 C CG1  . VAL A 1 297 ? 7.38200   -18.26600 22.19600  1.000 38.77552  ? 297 VAL A CG1  1 
ATOM   4559 C CG2  . VAL A 1 297 ? 8.11200   -16.92000 24.22100  1.000 40.04194  ? 297 VAL A CG2  1 
ATOM   4560 H H    . VAL A 1 297 ? 6.70400   -14.65900 23.49300  1.000 42.69783  ? 297 VAL A H    1 
ATOM   4561 H HA   . VAL A 1 297 ? 8.43700   -15.77500 21.87800  1.000 43.45127  ? 297 VAL A HA   1 
ATOM   4562 H HB   . VAL A 1 297 ? 6.27100   -16.94200 23.27000  1.000 40.42931  ? 297 VAL A HB   1 
ATOM   4563 H HG11 . VAL A 1 297 ? 7.44300   -19.00400 22.82200  1.000 46.53143  ? 297 VAL A HG11 1 
ATOM   4564 H HG12 . VAL A 1 297 ? 6.62300   -18.39700 21.60600  1.000 46.53143  ? 297 VAL A HG12 1 
ATOM   4565 H HG13 . VAL A 1 297 ? 8.20000   -18.20400 21.67900  1.000 46.53143  ? 297 VAL A HG13 1 
ATOM   4566 H HG21 . VAL A 1 297 ? 7.99000   -17.72800 24.74300  1.000 48.05112  ? 297 VAL A HG21 1 
ATOM   4567 H HG22 . VAL A 1 297 ? 9.03500   -16.85100 23.93000  1.000 48.05112  ? 297 VAL A HG22 1 
ATOM   4568 H HG23 . VAL A 1 297 ? 7.87300   -16.14400 24.75100  1.000 48.05112  ? 297 VAL A HG23 1 
ATOM   4569 N N    . ARG A 1 298 ? 5.49300   -15.39900 20.70800  1.000 36.40821  ? 298 ARG A N    1 
ATOM   4570 C CA   . ARG A 1 298 ? 4.71700   -15.39000 19.46400  1.000 35.28765  ? 298 ARG A CA   1 
ATOM   4571 C C    . ARG A 1 298 ? 5.39800   -14.52300 18.41200  1.000 42.86185  ? 298 ARG A C    1 
ATOM   4572 O O    . ARG A 1 298 ? 5.52300   -14.91400 17.24500  1.000 41.31046  ? 298 ARG A O    1 
ATOM   4573 C CB   . ARG A 1 298 ? 3.28700   -14.87700 19.72800  1.000 41.38758  ? 298 ARG A CB   1 
ATOM   4574 C CG   . ARG A 1 298 ? 2.57200   -14.23100 18.49000  1.000 39.80809  ? 298 ARG A CG   1 
ATOM   4575 C CD   . ARG A 1 298 ? 1.12300   -13.68400 18.78400  1.000 43.01488  ? 298 ARG A CD   1 
ATOM   4576 N NE   . ARG A 1 298 ? 0.55300   -13.09200 17.57000  1.000 34.57753  ? 298 ARG A NE   1 
ATOM   4577 C CZ   . ARG A 1 298 ? -0.02800  -11.89400 17.48700  1.000 37.42332  ? 298 ARG A CZ   1 
ATOM   4578 N NH1  . ARG A 1 298 ? -0.23000  -11.12500 18.56200  1.000 38.24635  ? 298 ARG A NH1  1 
ATOM   4579 N NH2  . ARG A 1 298 ? -0.43800  -11.45800 16.29300  1.000 35.69369  ? 298 ARG A NH2  1 
ATOM   4580 H H    . ARG A 1 298 ? 5.06800   -15.09800 21.39300  1.000 43.69065  ? 298 ARG A H    1 
ATOM   4581 H HA   . ARG A 1 298 ? 4.65600   -16.29400 19.11900  1.000 42.34598  ? 298 ARG A HA   1 
ATOM   4582 H HB2  . ARG A 1 298 ? 2.74200   -15.62300 20.02400  1.000 49.66589  ? 298 ARG A HB2  1 
ATOM   4583 H HB3  . ARG A 1 298 ? 3.32500   -14.20500 20.42700  1.000 49.66589  ? 298 ARG A HB3  1 
ATOM   4584 H HG2  . ARG A 1 298 ? 3.09300   -13.47600 18.17700  1.000 47.77051  ? 298 ARG A HG2  1 
ATOM   4585 H HG3  . ARG A 1 298 ? 2.50100   -14.89600 17.78700  1.000 47.77051  ? 298 ARG A HG3  1 
ATOM   4586 H HD2  . ARG A 1 298 ? 0.55200   -14.41600 19.06600  1.000 51.61865  ? 298 ARG A HD2  1 
ATOM   4587 H HD3  . ARG A 1 298 ? 1.17400   -13.00800 19.47600  1.000 51.61865  ? 298 ARG A HD3  1 
ATOM   4588 H HE   . ARG A 1 298 ? 0.64600   -13.53300 16.83800  1.000 41.49384  ? 298 ARG A HE   1 
ATOM   4589 H HH11 . ARG A 1 298 ? 0.02600   -11.38800 19.33900  1.000 45.89642  ? 298 ARG A HH11 1 
ATOM   4590 H HH12 . ARG A 1 298 ? -0.61200  -10.35900 18.47400  1.000 45.89642  ? 298 ARG A HH12 1 
ATOM   4591 H HH21 . ARG A 1 298 ? -0.31900  -11.94400 15.59400  1.000 42.83322  ? 298 ARG A HH21 1 
ATOM   4592 H HH22 . ARG A 1 298 ? -0.82100  -10.69100 16.22300  1.000 42.83322  ? 298 ARG A HH22 1 
ATOM   4593 N N    . GLN A 1 299 ? 5.89500   -13.36700 18.81300  1.000 35.96682  ? 299 GLN A N    1 
ATOM   4594 C CA   . GLN A 1 299 ? 6.47000   -12.43100 17.85900  1.000 37.92345  ? 299 GLN A CA   1 
ATOM   4595 C C    . GLN A 1 299 ? 7.94500   -12.68700 17.53300  1.000 47.13801  ? 299 GLN A C    1 
ATOM   4596 O O    . GLN A 1 299 ? 8.36800   -12.46900 16.38900  1.000 40.83917  ? 299 GLN A O    1 
ATOM   4597 C CB   . GLN A 1 299 ? 6.25100   -11.00400 18.37200  1.000 38.73124  ? 299 GLN A CB   1 
ATOM   4598 C CG   . GLN A 1 299 ? 6.65700   -9.96300  17.35000  1.000 39.78258  ? 299 GLN A CG   1 
ATOM   4599 C CD   . GLN A 1 299 ? 6.19600   -8.55600  17.69700  1.000 33.27574  ? 299 GLN A CD   1 
ATOM   4600 O OE1  . GLN A 1 299 ? 6.70900   -7.60800  17.12800  1.000 34.06688  ? 299 GLN A OE1  1 
ATOM   4601 N NE2  . GLN A 1 299 ? 5.25500   -8.40900  18.65300  1.000 32.22303  ? 299 GLN A NE2  1 
ATOM   4602 H H    . GLN A 1 299 ? 5.91300   -13.09800 19.63000  1.000 43.16098  ? 299 GLN A H    1 
ATOM   4603 H HA   . GLN A 1 299 ? 5.97900   -12.51100 17.02600  1.000 45.50895  ? 299 GLN A HA   1 
ATOM   4604 H HB2  . GLN A 1 299 ? 5.30700   -10.90100 18.56400  1.000 46.47829  ? 299 GLN A HB2  1 
ATOM   4605 H HB3  . GLN A 1 299 ? 6.77700   -10.86600 19.17600  1.000 46.47829  ? 299 GLN A HB3  1 
ATOM   4606 H HG2  . GLN A 1 299 ? 7.62500   -9.94900  17.28300  1.000 47.73990  ? 299 GLN A HG2  1 
ATOM   4607 H HG3  . GLN A 1 299 ? 6.27100   -10.19900 16.49200  1.000 47.73990  ? 299 GLN A HG3  1 
ATOM   4608 H HE21 . GLN A 1 299 ? 4.91000   -9.08900  19.04500  1.000 38.66843  ? 299 GLN A HE21 1 
ATOM   4609 H HE22 . GLN A 1 299 ? 4.98600   -7.62000  18.86300  1.000 38.66843  ? 299 GLN A HE22 1 
ATOM   4610 N N    . CYS A 1 300 ? 8.75600   -13.09300 18.51200  1.000 41.46538  ? 300 CYS A N    1 
ATOM   4611 C CA   . CYS A 1 300 ? 10.19800  -13.20200 18.32200  1.000 45.48580  ? 300 CYS A CA   1 
ATOM   4612 C C    . CYS A 1 300 ? 10.61300  -14.57000 17.77300  1.000 51.81090  ? 300 CYS A C    1 
ATOM   4613 O O    . CYS A 1 300 ? 9.85400   -15.54400 17.79500  1.000 54.90614  ? 300 CYS A O    1 
ATOM   4614 C CB   . CYS A 1 300 ? 10.93100  -12.93900 19.63500  1.000 44.01117  ? 300 CYS A CB   1 
ATOM   4615 S SG   . CYS A 1 300 ? 10.87600  -11.23800 20.18700  1.000 44.03255  ? 300 CYS A SG   1 
ATOM   4616 H H    . CYS A 1 300 ? 8.49100   -13.31200 19.30000  1.000 49.75926  ? 300 CYS A H    1 
ATOM   4617 H HA   . CYS A 1 300 ? 10.48200  -12.52800 17.68400  1.000 54.58376  ? 300 CYS A HA   1 
ATOM   4618 H HB2  . CYS A 1 300 ? 10.53100  -13.48600 20.32900  1.000 52.81421  ? 300 CYS A HB2  1 
ATOM   4619 H HB3  . CYS A 1 300 ? 11.86300  -13.18200 19.52400  1.000 52.81421  ? 300 CYS A HB3  1 
ATOM   4620 H HG   . CYS A 1 300 ? 11.47800  -11.14300 21.22000  1.000 52.83986  ? 300 CYS A HG   1 
ATOM   4621 N N    . SER A 1 301 ? 11.85600  -14.62800 17.28900  1.000 63.32565  ? 301 SER A N    1 
ATOM   4622 C CA   . SER A 1 301 ? 12.47300  -15.87700 16.82900  1.000 70.09963  ? 301 SER A CA   1 
ATOM   4623 C C    . SER A 1 301 ? 12.81500  -16.80200 17.99900  1.000 69.12831  ? 301 SER A C    1 
ATOM   4624 O O    . SER A 1 301 ? 12.97600  -16.34600 19.13500  1.000 73.21059  ? 301 SER A O    1 
ATOM   4625 C CB   . SER A 1 301 ? 13.74100  -15.58700 16.01500  1.000 75.23629  ? 301 SER A CB   1 
ATOM   4626 O OG   . SER A 1 301 ? 14.72800  -14.95200 16.81200  1.000 78.93623  ? 301 SER A OG   1 
ATOM   4627 H H    . SER A 1 301 ? 12.37200  -13.94400 17.21500  1.000 75.99158  ? 301 SER A H    1 
ATOM   4628 H HA   . SER A 1 301 ? 11.84800  -16.34300 16.25200  1.000 84.12036  ? 301 SER A HA   1 
ATOM   4629 H HB2  . SER A 1 301 ? 14.09800  -16.42400 15.68000  1.000 90.28435  ? 301 SER A HB2  1 
ATOM   4630 H HB3  . SER A 1 301 ? 13.51300  -15.00500 15.27400  1.000 90.28435  ? 301 SER A HB3  1 
ATOM   4631 H HG   . SER A 1 301 ? 15.41500  -14.80000 16.35200  1.000 94.72428  ? 301 SER A HG   1 
ATOM   4632 N N    . SER B 2 1   ? -12.51200 8.40500   24.28000  1.000 30.72632  ? 1   SER B N    1 
ATOM   4633 C CA   . SER B 2 1   ? -11.16200 8.75200   24.72300  1.000 31.27346  ? 1   SER B CA   1 
ATOM   4634 C C    . SER B 2 1   ? -10.21100 7.63400   24.46000  1.000 28.34179  ? 1   SER B C    1 
ATOM   4635 O O    . SER B 2 1   ? -10.59800 6.47600   24.27500  1.000 25.26488  ? 1   SER B O    1 
ATOM   4636 C CB   . SER B 2 1   ? -11.11200 9.07300   26.25200  1.000 30.85621  ? 1   SER B CB   1 
ATOM   4637 O OG   . SER B 2 1   ? -11.91000 10.19100  26.54400  1.000 49.64190  ? 1   SER B OG   1 
ATOM   4638 H H1   . SER B 2 1   ? -12.90700 9.12600   23.93800  1.000 36.87239  ? 1   SER B H1   1 
ATOM   4639 H H2   . SER B 2 1   ? -12.46600 7.76900   23.65900  1.000 36.87239  ? 1   SER B H2   1 
ATOM   4640 H H3   . SER B 2 1   ? -12.98500 8.10900   24.97300  1.000 36.87239  ? 1   SER B H3   1 
ATOM   4641 H HA   . SER B 2 1   ? -10.85600 9.53400   24.23700  1.000 37.52895  ? 1   SER B HA   1 
ATOM   4642 H HB2  . SER B 2 1   ? -11.44000 8.30800   26.74800  1.000 37.02826  ? 1   SER B HB2  1 
ATOM   4643 H HB3  . SER B 2 1   ? -10.19500 9.26400   26.50500  1.000 37.02826  ? 1   SER B HB3  1 
ATOM   4644 H HG   . SER B 2 1   ? -12.70700 10.04000  26.32600  1.000 59.57109  ? 1   SER B HG   1 
ATOM   4645 N N    . GLY B 2 2   ? -8.94800  7.97600   24.53300  1.000 28.82811  ? 2   GLY B N    1 
ATOM   4646 C CA   . GLY B 2 2   ? -7.87900  7.03400   24.31000  1.000 28.94097  ? 2   GLY B CA   1 
ATOM   4647 C C    . GLY B 2 2   ? -7.24000  7.25300   22.95200  1.000 30.80782  ? 2   GLY B C    1 
ATOM   4648 O O    . GLY B 2 2   ? -7.79500  7.90200   22.06400  1.000 28.48951  ? 2   GLY B O    1 
ATOM   4649 H H    . GLY B 2 2   ? -8.67500  8.77100   24.71600  1.000 34.59453  ? 2   GLY B H    1 
ATOM   4650 H HA2  . GLY B 2 2   ? -7.20100  7.13800   24.99600  1.000 34.72997  ? 2   GLY B HA2  1 
ATOM   4651 H HA3  . GLY B 2 2   ? -8.22500  6.13200   24.34800  1.000 34.72997  ? 2   GLY B HA3  1 
ATOM   4652 N N    . PHE B 2 3   ? -6.02400  6.73900   22.80400  1.000 27.85988  ? 3   PHE B N    1 
ATOM   4653 C CA   . PHE B 2 3   ? -5.33800  6.85600   21.52400  1.000 26.06166  ? 3   PHE B CA   1 
ATOM   4654 C C    . PHE B 2 3   ? -4.33000  5.73100   21.42000  1.000 30.26308  ? 3   PHE B C    1 
ATOM   4655 O O    . PHE B 2 3   ? -3.43200  5.62200   22.26500  1.000 29.57106  ? 3   PHE B O    1 
ATOM   4656 C CB   . PHE B 2 3   ? -4.67000  8.22600   21.37100  1.000 28.20052  ? 3   PHE B CB   1 
ATOM   4657 C CG   . PHE B 2 3   ? -4.38800  8.57600   19.93300  1.000 27.48595  ? 3   PHE B CG   1 
ATOM   4658 C CD1  . PHE B 2 3   ? -5.43600  8.92500   19.08100  1.000 28.54763  ? 3   PHE B CD1  1 
ATOM   4659 C CD2  . PHE B 2 3   ? -3.09400  8.50300   19.42800  1.000 28.99370  ? 3   PHE B CD2  1 
ATOM   4660 C CE1  . PHE B 2 3   ? -5.19900  9.20600   17.74200  1.000 32.92279  ? 3   PHE B CE1  1 
ATOM   4661 C CE2  . PHE B 2 3   ? -2.83500  8.80800   18.13400  1.000 29.20475  ? 3   PHE B CE2  1 
ATOM   4662 C CZ   . PHE B 2 3   ? -3.88800  9.14800   17.25600  1.000 29.71764  ? 3   PHE B CZ   1 
ATOM   4663 H H    . PHE B 2 3   ? -5.58200  6.32600   23.41500  1.000 33.43265  ? 3   PHE B H    1 
ATOM   4664 H HA   . PHE B 2 3   ? -5.98200  6.75200   20.80700  1.000 31.27479  ? 3   PHE B HA   1 
ATOM   4665 H HB2  . PHE B 2 3   ? -5.25700  8.90700   21.73600  1.000 33.84143  ? 3   PHE B HB2  1 
ATOM   4666 H HB3  . PHE B 2 3   ? -3.82700  8.22200   21.85000  1.000 33.84143  ? 3   PHE B HB3  1 
ATOM   4667 H HD1  . PHE B 2 3   ? -6.30600  8.95200   19.40900  1.000 34.25796  ? 3   PHE B HD1  1 
ATOM   4668 H HD2  . PHE B 2 3   ? -2.39300  8.27300   19.99400  1.000 34.79324  ? 3   PHE B HD2  1 
ATOM   4669 H HE1  . PHE B 2 3   ? -5.90000  9.44800   17.18000  1.000 39.50815  ? 3   PHE B HE1  1 
ATOM   4670 H HE2  . PHE B 2 3   ? -1.96400  8.75700   17.81300  1.000 35.04650  ? 3   PHE B HE2  1 
ATOM   4671 H HZ   . PHE B 2 3   ? -3.70900  9.35200   16.36700  1.000 35.66196  ? 3   PHE B HZ   1 
ATOM   4672 N N    . ARG B 2 4   ? -4.51300  4.86300   20.42700  1.000 26.74336  ? 4   ARG B N    1 
ATOM   4673 C CA   . ARG B 2 4   ? -3.70000  3.67100   20.26700  1.000 25.74750  ? 4   ARG B CA   1 
ATOM   4674 C C    . ARG B 2 4   ? -3.13000  3.64800   18.85100  1.000 25.81794  ? 4   ARG B C    1 
ATOM   4675 O O    . ARG B 2 4   ? -3.68000  4.24100   17.92600  1.000 24.86042  ? 4   ARG B O    1 
ATOM   4676 C CB   . ARG B 2 4   ? -4.54400  2.40500   20.44300  1.000 27.57743  ? 4   ARG B CB   1 
ATOM   4677 C CG   . ARG B 2 4   ? -5.01300  2.14400   21.85300  1.000 29.94587  ? 4   ARG B CG   1 
ATOM   4678 C CD   . ARG B 2 4   ? -3.80000  1.66800   22.63600  1.000 33.46584  ? 4   ARG B CD   1 
ATOM   4679 N NE   . ARG B 2 4   ? -4.12100  1.06500   23.93100  1.000 33.54561  ? 4   ARG B NE   1 
ATOM   4680 C CZ   . ARG B 2 4   ? -3.22400  0.39400   24.64500  1.000 33.83362  ? 4   ARG B CZ   1 
ATOM   4681 N NH1  . ARG B 2 4   ? -1.99400  0.18000   24.18100  1.000 35.65592  ? 4   ARG B NH1  1 
ATOM   4682 N NH2  . ARG B 2 4   ? -3.56400  -0.08000  25.84300  1.000 31.03967  ? 4   ARG B NH2  1 
ATOM   4683 H H    . ARG B 2 4   ? -5.11800  4.94900   19.82200  1.000 32.09284  ? 4   ARG B H    1 
ATOM   4684 H HA   . ARG B 2 4   ? -2.97100  3.66700   20.90600  1.000 30.89780  ? 4   ARG B HA   1 
ATOM   4685 H HB2  . ARG B 2 4   ? -5.33400  2.48500   19.88500  1.000 33.09372  ? 4   ARG B HB2  1 
ATOM   4686 H HB3  . ARG B 2 4   ? -4.02100  1.64100   20.15400  1.000 33.09372  ? 4   ARG B HB3  1 
ATOM   4687 H HG2  . ARG B 2 4   ? -5.34800  2.96300   22.25100  1.000 35.93585  ? 4   ARG B HG2  1 
ATOM   4688 H HG3  . ARG B 2 4   ? -5.68900  1.44900   21.85900  1.000 35.93585  ? 4   ARG B HG3  1 
ATOM   4689 H HD2  . ARG B 2 4   ? -3.33000  1.00100   22.11200  1.000 40.15981  ? 4   ARG B HD2  1 
ATOM   4690 H HD3  . ARG B 2 4   ? -3.21700  2.42600   22.80100  1.000 40.15981  ? 4   ARG B HD3  1 
ATOM   4691 H HE   . ARG B 2 4   ? -4.84100  1.32000   24.32600  1.000 40.25553  ? 4   ARG B HE   1 
ATOM   4692 H HH11 . ARG B 2 4   ? -1.76100  0.48200   23.41100  1.000 42.78790  ? 4   ARG B HH11 1 
ATOM   4693 H HH12 . ARG B 2 4   ? -1.42800  -0.25900  24.65700  1.000 42.78790  ? 4   ARG B HH12 1 
ATOM   4694 H HH21 . ARG B 2 4   ? -4.35700  0.05100   26.14800  1.000 37.24840  ? 4   ARG B HH21 1 
ATOM   4695 H HH22 . ARG B 2 4   ? -2.99100  -0.52000  26.31000  1.000 37.24840  ? 4   ARG B HH22 1 
ATOM   4696 N N    . LYS B 2 5   ? -2.07300  2.85700   18.67300  1.000 25.96125  ? 5   LYS B N    1 
ATOM   4697 C CA   . LYS B 2 5   ? -1.54100  2.58900   17.31200  1.000 24.54560  ? 5   LYS B CA   1 
ATOM   4698 C C    . LYS B 2 5   ? -2.60200  1.67600   16.70300  1.000 26.57627  ? 5   LYS B C    1 
ATOM   4699 O O    . LYS B 2 5   ? -2.67000  0.52100   17.09900  1.000 28.31218  ? 5   LYS B O    1 
ATOM   4700 C CB   . LYS B 2 5   ? -0.14600  1.96000   17.38200  1.000 29.02159  ? 5   LYS B CB   1 
ATOM   4701 C CG   . LYS B 2 5   ? 0.72200   2.07900   16.13800  1.000 39.26374  ? 5   LYS B CG   1 
ATOM   4702 C CD   . LYS B 2 5   ? 0.82700   3.47000   15.56000  1.000 38.79105  ? 5   LYS B CD   1 
ATOM   4703 C CE   . LYS B 2 5   ? 2.05200   4.23900   16.00800  1.000 39.51580  ? 5   LYS B CE   1 
ATOM   4704 N NZ   . LYS B 2 5   ? 3.15700   3.35600   16.44300  1.000 46.81385  ? 5   LYS B NZ   1 
ATOM   4705 H H    . LYS B 2 5   ? -1.64400  2.46400   19.30600  1.000 31.15430  ? 5   LYS B H    1 
ATOM   4706 H HA   . LYS B 2 5   ? -1.52600  3.41600   16.81400  1.000 29.45552  ? 5   LYS B HA   1 
ATOM   4707 H HB2  . LYS B 2 5   ? 0.33800   2.37900   18.11000  1.000 34.82671  ? 5   LYS B HB2  1 
ATOM   4708 H HB3  . LYS B 2 5   ? -0.24900  1.01400   17.57000  1.000 34.82671  ? 5   LYS B HB3  1 
ATOM   4709 H HG2  . LYS B 2 5   ? 1.59600   1.71500   16.33000  1.000 47.11729  ? 5   LYS B HG2  1 
ATOM   4710 H HG3  . LYS B 2 5   ? 0.30600   1.53100   15.46000  1.000 47.11729  ? 5   LYS B HG3  1 
ATOM   4711 H HD2  . LYS B 2 5   ? 0.87800   3.39100   14.59500  1.000 46.55007  ? 5   LYS B HD2  1 
ATOM   4712 H HD3  . LYS B 2 5   ? 0.05800   4.00200   15.79200  1.000 46.55007  ? 5   LYS B HD3  1 
ATOM   4713 H HE2  . LYS B 2 5   ? 2.37300   4.78100   15.27000  1.000 47.41976  ? 5   LYS B HE2  1 
ATOM   4714 H HE3  . LYS B 2 5   ? 1.81300   4.80600   16.75700  1.000 47.41976  ? 5   LYS B HE3  1 
ATOM   4715 H HZ1  . LYS B 2 5   ? 3.89700   3.83600   16.56200  1.000 56.17742  ? 5   LYS B HZ1  1 
ATOM   4716 H HZ2  . LYS B 2 5   ? 2.94700   2.95800   17.21100  1.000 56.17742  ? 5   LYS B HZ2  1 
ATOM   4717 H HZ3  . LYS B 2 5   ? 3.31400   2.73600   15.82400  1.000 56.17742  ? 5   LYS B HZ3  1 
ATOM   4718 N N    . MET B 2 6   ? -3.38100  2.19200   15.77000  1.000 22.67916  ? 6   MET B N    1 
ATOM   4719 C CA   . MET B 2 6   ? -4.55500  1.47500   15.28600  1.000 23.32013  ? 6   MET B CA   1 
ATOM   4720 C C    . MET B 2 6   ? -4.37100  1.07300   13.82800  1.000 25.32905  ? 6   MET B C    1 
ATOM   4721 O O    . MET B 2 6   ? -4.12500  1.93000   12.97100  1.000 26.15533  ? 6   MET B O    1 
ATOM   4722 C CB   . MET B 2 6   ? -5.78600  2.36100   15.46500  1.000 25.14494  ? 6   MET B CB   1 
ATOM   4723 C CG   . MET B 2 6   ? -7.02700  1.72800   14.94900  1.000 30.44991  ? 6   MET B CG   1 
ATOM   4724 S SD   . MET B 2 6   ? -8.43600  2.85200   15.35200  1.000 36.23888  ? 6   MET B SD   1 
ATOM   4725 C CE   . MET B 2 6   ? -8.49900  2.70300   17.08800  1.000 36.31987  ? 6   MET B CE   1 
ATOM   4726 H H    . MET B 2 6   ? -3.25500  2.95700   15.39700  1.000 27.21580  ? 6   MET B H    1 
ATOM   4727 H HA   . MET B 2 6   ? -4.68400  0.67500   15.81900  1.000 27.98496  ? 6   MET B HA   1 
ATOM   4728 H HB2  . MET B 2 6   ? -5.89100  2.54300   16.40800  1.000 30.17473  ? 6   MET B HB2  1 
ATOM   4729 H HB3  . MET B 2 6   ? -5.65000  3.19100   14.98100  1.000 30.17473  ? 6   MET B HB3  1 
ATOM   4730 H HG2  . MET B 2 6   ? -6.97700  1.62500   13.98600  1.000 36.54070  ? 6   MET B HG2  1 
ATOM   4731 H HG3  . MET B 2 6   ? -7.17000  0.87300   15.38400  1.000 36.54070  ? 6   MET B HG3  1 
ATOM   4732 H HE1  . MET B 2 6   ? -9.06600  3.40700   17.43900  1.000 43.58465  ? 6   MET B HE1  1 
ATOM   4733 H HE2  . MET B 2 6   ? -8.88600  1.84200   17.29900  1.000 43.58465  ? 6   MET B HE2  1 
ATOM   4734 H HE3  . MET B 2 6   ? -7.61400  2.77800   17.47000  1.000 43.58465  ? 6   MET B HE3  1 
ATOM   4735 N N    . ALA B 2 7   ? -4.50200  -0.21000  13.54400  1.000 25.20022  ? 7   ALA B N    1 
ATOM   4736 C CA   . ALA B 2 7   ? -4.43500  -0.66000  12.15700  1.000 22.27053  ? 7   ALA B CA   1 
ATOM   4737 C C    . ALA B 2 7   ? -5.82600  -0.67700  11.53700  1.000 25.98965  ? 7   ALA B C    1 
ATOM   4738 O O    . ALA B 2 7   ? -6.85100  -0.66800  12.22900  1.000 23.30176  ? 7   ALA B O    1 
ATOM   4739 C CB   . ALA B 2 7   ? -3.82400  -2.06100  12.08400  1.000 25.99354  ? 7   ALA B CB   1 
ATOM   4740 H H    . ALA B 2 7   ? -4.62900  -0.83500  14.12100  1.000 30.24106  ? 7   ALA B H    1 
ATOM   4741 H HA   . ALA B 2 7   ? -3.87700  -0.05600  11.64300  1.000 26.72544  ? 7   ALA B HA   1 
ATOM   4742 H HB1  . ALA B 2 7   ? -3.78900  -2.34200  11.15600  1.000 31.19304  ? 7   ALA B HB1  1 
ATOM   4743 H HB2  . ALA B 2 7   ? -2.92900  -2.03400  12.45600  1.000 31.19304  ? 7   ALA B HB2  1 
ATOM   4744 H HB3  . ALA B 2 7   ? -4.37700  -2.67300  12.59500  1.000 31.19304  ? 7   ALA B HB3  1 
ATOM   4745 N N    . PHE B 2 8   ? -5.85700  -0.72400  10.21100  1.000 25.21812  ? 8   PHE B N    1 
ATOM   4746 C CA   . PHE B 2 8   ? -7.12400  -0.92700  9.53900   1.000 25.44638  ? 8   PHE B CA   1 
ATOM   4747 C C    . PHE B 2 8   ? -7.57200  -2.36000  9.79600   1.000 23.54204  ? 8   PHE B C    1 
ATOM   4748 O O    . PHE B 2 8   ? -6.73800  -3.26400  9.95200   1.000 21.31860  ? 8   PHE B O    1 
ATOM   4749 C CB   . PHE B 2 8   ? -6.98300  -0.73200  8.01200   1.000 27.80122  ? 8   PHE B CB   1 
ATOM   4750 C CG   . PHE B 2 8   ? -6.82400  0.71000   7.60000   1.000 25.30402  ? 8   PHE B CG   1 
ATOM   4751 C CD1  . PHE B 2 8   ? -7.92400  1.51900   7.47300   1.000 28.75227  ? 8   PHE B CD1  1 
ATOM   4752 C CD2  . PHE B 2 8   ? -5.56300  1.24300   7.38900   1.000 27.76916  ? 8   PHE B CD2  1 
ATOM   4753 C CE1  . PHE B 2 8   ? -7.79800  2.85400   7.09600   1.000 32.13237  ? 8   PHE B CE1  1 
ATOM   4754 C CE2  . PHE B 2 8   ? -5.43100  2.61400   7.03800   1.000 33.99486  ? 8   PHE B CE2  1 
ATOM   4755 C CZ   . PHE B 2 8   ? -6.53200  3.39100   6.89400   1.000 30.49730  ? 8   PHE B CZ   1 
ATOM   4756 H H    . PHE B 2 8   ? -5.17600  -0.64300  9.69200   1.000 30.26254  ? 8   PHE B H    1 
ATOM   4757 H HA   . PHE B 2 8   ? -7.77000  -0.29500  9.88600   1.000 30.53646  ? 8   PHE B HA   1 
ATOM   4758 H HB2  . PHE B 2 8   ? -6.20100  -1.21700  7.70500   1.000 33.36226  ? 8   PHE B HB2  1 
ATOM   4759 H HB3  . PHE B 2 8   ? -7.77700  -1.07900  7.57700   1.000 33.36226  ? 8   PHE B HB3  1 
ATOM   4760 H HD1  . PHE B 2 8   ? -8.77200  1.16100   7.60900   1.000 34.50352  ? 8   PHE B HD1  1 
ATOM   4761 H HD2  . PHE B 2 8   ? -4.80700  0.71100   7.49200   1.000 33.32379  ? 8   PHE B HD2  1 
ATOM   4762 H HE1  . PHE B 2 8   ? -8.54900  3.39100   7.00800   1.000 38.55964  ? 8   PHE B HE1  1 
ATOM   4763 H HE2  . PHE B 2 8   ? -4.58800  2.97300   6.88700   1.000 40.79464  ? 8   PHE B HE2  1 
ATOM   4764 H HZ   . PHE B 2 8   ? -6.44100  4.28300   6.64800   1.000 36.59756  ? 8   PHE B HZ   1 
ATOM   4765 N N    . PRO B 2 9   ? -8.88000  -2.60100  9.78600   1.000 26.13359  ? 9   PRO B N    1 
ATOM   4766 C CA   . PRO B 2 9   ? -9.38400  -3.98100  9.82200   1.000 26.94277  ? 9   PRO B CA   1 
ATOM   4767 C C    . PRO B 2 9   ? -8.83000  -4.73700  8.63000   1.000 26.46937  ? 9   PRO B C    1 
ATOM   4768 O O    . PRO B 2 9   ? -8.83800  -4.21500  7.51100   1.000 26.82097  ? 9   PRO B O    1 
ATOM   4769 C CB   . PRO B 2 9   ? -10.90100 -3.80700  9.69100   1.000 26.07292  ? 9   PRO B CB   1 
ATOM   4770 C CG   . PRO B 2 9   ? -11.16200 -2.33100  10.05600  1.000 32.10727  ? 9   PRO B CG   1 
ATOM   4771 C CD   . PRO B 2 9   ? -9.93600  -1.60700  9.57200   1.000 26.02549  ? 9   PRO B CD   1 
ATOM   4772 H HA   . PRO B 2 9   ? -9.15700  -4.42700  10.65300  1.000 32.33213  ? 9   PRO B HA   1 
ATOM   4773 H HB2  . PRO B 2 9   ? -11.17400 -3.98900  8.77800   1.000 31.28830  ? 9   PRO B HB2  1 
ATOM   4774 H HB3  . PRO B 2 9   ? -11.35400 -4.40000  10.31100  1.000 31.28830  ? 9   PRO B HB3  1 
ATOM   4775 H HG2  . PRO B 2 9   ? -11.95500 -2.01300  9.59800   1.000 38.52952  ? 9   PRO B HG2  1 
ATOM   4776 H HG3  . PRO B 2 9   ? -11.25700 -2.24100  11.01700  1.000 38.52952  ? 9   PRO B HG3  1 
ATOM   4777 H HD2  . PRO B 2 9   ? -10.01600 -1.38900  8.63000   1.000 31.23139  ? 9   PRO B HD2  1 
ATOM   4778 H HD3  . PRO B 2 9   ? -9.79000  -0.81700  10.11400  1.000 31.23139  ? 9   PRO B HD3  1 
ATOM   4779 N N    . SER B 2 10  ? -8.34800  -5.95700  8.86900   1.000 24.23025  ? 10  SER B N    1 
ATOM   4780 C CA   . SER B 2 10  ? -7.52700  -6.66700  7.89200   1.000 22.75710  ? 10  SER B CA   1 
ATOM   4781 C C    . SER B 2 10  ? -8.30200  -7.72100  7.10100   1.000 23.93446  ? 10  SER B C    1 
ATOM   4782 O O    . SER B 2 10  ? -7.73100  -8.32800  6.18300   1.000 24.43872  ? 10  SER B O    1 
ATOM   4783 C CB   . SER B 2 10  ? -6.32000  -7.32000  8.57700   1.000 25.53826  ? 10  SER B CB   1 
ATOM   4784 O OG   . SER B 2 10  ? -6.73400  -8.25900  9.56200   1.000 26.94036  ? 10  SER B OG   1 
ATOM   4785 H H    . SER B 2 10  ? -8.48400  -6.39700  9.59500   1.000 29.07710  ? 10  SER B H    1 
ATOM   4786 H HA   . SER B 2 10  ? -7.18300  -6.02200  7.25400   1.000 27.30932  ? 10  SER B HA   1 
ATOM   4787 H HB2  . SER B 2 10  ? -5.78900  -7.77900  7.90800   1.000 30.64671  ? 10  SER B HB2  1 
ATOM   4788 H HB3  . SER B 2 10  ? -5.78900  -6.63000  9.00400   1.000 30.64671  ? 10  SER B HB3  1 
ATOM   4789 H HG   . SER B 2 10  ? -7.18500  -8.87100  9.20500   1.000 32.32923  ? 10  SER B HG   1 
ATOM   4790 N N    . GLY B 2 11  ? -9.59600  -7.89500  7.39900   1.000 25.95707  ? 11  GLY B N    1 
ATOM   4791 C CA   . GLY B 2 11  ? -10.35800 -8.98700  6.79100   1.000 27.02603  ? 11  GLY B CA   1 
ATOM   4792 C C    . GLY B 2 11  ? -10.31300 -9.01900  5.27000   1.000 28.57471  ? 11  GLY B C    1 
ATOM   4793 O O    . GLY B 2 11  ? -10.17700 -10.08600 4.66900   1.000 27.83958  ? 11  GLY B O    1 
ATOM   4794 H H    . GLY B 2 11  ? -10.04800 -7.40300  7.94000   1.000 31.14928  ? 11  GLY B H    1 
ATOM   4795 H HA2  . GLY B 2 11  ? -10.01400 -9.83300  7.11900   1.000 32.43203  ? 11  GLY B HA2  1 
ATOM   4796 H HA3  . GLY B 2 11  ? -11.28600 -8.91400  7.06200   1.000 32.43203  ? 11  GLY B HA3  1 
ATOM   4797 N N    . LYS B 2 12  ? -10.46500 -7.86300  4.61700   1.000 25.33071  ? 12  LYS B N    1 
ATOM   4798 C CA   . LYS B 2 12  ? -10.43400 -7.86100  3.15400   1.000 25.60797  ? 12  LYS B CA   1 
ATOM   4799 C C    . LYS B 2 12  ? -9.10800  -8.37000  2.60200   1.000 29.70843  ? 12  LYS B C    1 
ATOM   4800 O O    . LYS B 2 12  ? -9.07700  -9.01700  1.56100   1.000 29.56722  ? 12  LYS B O    1 
ATOM   4801 C CB   . LYS B 2 12  ? -10.71800 -6.44800  2.68200   1.000 30.31689  ? 12  LYS B CB   1 
ATOM   4802 C CG   . LYS B 2 12  ? -12.19400 -6.05100  2.79800   1.000 37.20331  ? 12  LYS B CG   1 
ATOM   4803 C CD   . LYS B 2 12  ? -12.36100 -4.56500  2.43900   1.000 39.46865  ? 12  LYS B CD   1 
ATOM   4804 C CE   . LYS B 2 12  ? -13.85300 -4.20400  2.25000   1.000 54.68308  ? 12  LYS B CE   1 
ATOM   4805 N NZ   . LYS B 2 12  ? -14.60300 -4.27400  3.53200   1.000 63.25079  ? 12  LYS B NZ   1 
ATOM   4806 H H    . LYS B 2 12  ? -10.58300 -7.09400  4.98300   1.000 30.39765  ? 12  LYS B H    1 
ATOM   4807 H HA   . LYS B 2 12  ? -11.13900 -8.43800  2.82100   1.000 30.73036  ? 12  LYS B HA   1 
ATOM   4808 H HB2  . LYS B 2 12  ? -10.20000 -5.82800  3.21900   1.000 36.38107  ? 12  LYS B HB2  1 
ATOM   4809 H HB3  . LYS B 2 12  ? -10.46200 -6.37100  1.75000   1.000 36.38107  ? 12  LYS B HB3  1 
ATOM   4810 H HG2  . LYS B 2 12  ? -12.72300 -6.58000  2.18100   1.000 44.64477  ? 12  LYS B HG2  1 
ATOM   4811 H HG3  . LYS B 2 12  ? -12.49700 -6.18500  3.71000   1.000 44.64477  ? 12  LYS B HG3  1 
ATOM   4812 H HD2  . LYS B 2 12  ? -12.00300 -4.01900  3.15600   1.000 47.36318  ? 12  LYS B HD2  1 
ATOM   4813 H HD3  . LYS B 2 12  ? -11.89400 -4.38000  1.60900   1.000 47.36318  ? 12  LYS B HD3  1 
ATOM   4814 H HE2  . LYS B 2 12  ? -13.92200 -3.29900  1.90700   1.000 65.62050  ? 12  LYS B HE2  1 
ATOM   4815 H HE3  . LYS B 2 12  ? -14.25700 -4.82900  1.62800   1.000 65.62050  ? 12  LYS B HE3  1 
ATOM   4816 H HZ1  . LYS B 2 12  ? -15.45700 -4.06200  3.39700   1.000 75.90175  ? 12  LYS B HZ1  1 
ATOM   4817 H HZ2  . LYS B 2 12  ? -14.55900 -5.09800  3.86600   1.000 75.90175  ? 12  LYS B HZ2  1 
ATOM   4818 H HZ3  . LYS B 2 12  ? -14.25400 -3.70500  4.12000   1.000 75.90175  ? 12  LYS B HZ3  1 
ATOM   4819 N N    . VAL B 2 13  ? -8.00600  -8.14500  3.31200   1.000 24.43095  ? 13  VAL B N    1 
ATOM   4820 C CA   . VAL B 2 13  ? -6.71400  -8.61500  2.80800   1.000 25.19247  ? 13  VAL B CA   1 
ATOM   4821 C C    . VAL B 2 13  ? -6.45900  -10.07900 3.16300   1.000 25.14855  ? 13  VAL B C    1 
ATOM   4822 O O    . VAL B 2 13  ? -5.81500  -10.82000 2.40000   1.000 25.19617  ? 13  VAL B O    1 
ATOM   4823 C CB   . VAL B 2 13  ? -5.61500  -7.69900  3.37900   1.000 23.76209  ? 13  VAL B CB   1 
ATOM   4824 C CG1  . VAL B 2 13  ? -4.19500  -8.18200  2.86400   1.000 24.50242  ? 13  VAL B CG1  1 
ATOM   4825 C CG2  . VAL B 2 13  ? -5.91700  -6.26000  2.97800   1.000 27.78886  ? 13  VAL B CG2  1 
ATOM   4826 H H    . VAL B 2 13  ? -7.97500  -7.73500  4.06700   1.000 29.31794  ? 13  VAL B H    1 
ATOM   4827 H HA   . VAL B 2 13  ? -6.70000  -8.53300  1.84200   1.000 30.23177  ? 13  VAL B HA   1 
ATOM   4828 H HB   . VAL B 2 13  ? -5.62300  -7.75400  4.34700   1.000 28.51530  ? 13  VAL B HB   1 
ATOM   4829 H HG11 . VAL B 2 13  ? -3.53600  -7.50300  3.07900   1.000 29.40370  ? 13  VAL B HG11 1 
ATOM   4830 H HG12 . VAL B 2 13  ? -3.96400  -9.01600  3.30200   1.000 29.40370  ? 13  VAL B HG12 1 
ATOM   4831 H HG13 . VAL B 2 13  ? -4.23500  -8.31100  1.90300   1.000 29.40370  ? 13  VAL B HG13 1 
ATOM   4832 H HG21 . VAL B 2 13  ? -5.14500  -5.70800  3.18000   1.000 33.34744  ? 13  VAL B HG21 1 
ATOM   4833 H HG22 . VAL B 2 13  ? -6.10500  -6.23100  2.02700   1.000 33.34744  ? 13  VAL B HG22 1 
ATOM   4834 H HG23 . VAL B 2 13  ? -6.68700  -5.94600  3.47700   1.000 33.34744  ? 13  VAL B HG23 1 
ATOM   4835 N N    . GLU B 2 14  ? -6.92500  -10.52400 4.33200   1.000 25.01499  ? 14  GLU B N    1 
ATOM   4836 C CA   . GLU B 2 14  ? -6.69900  -11.91900 4.71500   1.000 25.05576  ? 14  GLU B CA   1 
ATOM   4837 C C    . GLU B 2 14  ? -7.20100  -12.88600 3.65500   1.000 25.66196  ? 14  GLU B C    1 
ATOM   4838 O O    . GLU B 2 14  ? -6.56800  -13.91600 3.40000   1.000 29.44369  ? 14  GLU B O    1 
ATOM   4839 C CB   . GLU B 2 14  ? -7.39800  -12.21000 6.06400   1.000 25.24075  ? 14  GLU B CB   1 
ATOM   4840 C CG   . GLU B 2 14  ? -6.80600  -11.46000 7.23200   1.000 25.23655  ? 14  GLU B CG   1 
ATOM   4841 C CD   . GLU B 2 14  ? -7.73900  -11.52600 8.45300   1.000 27.68886  ? 14  GLU B CD   1 
ATOM   4842 O OE1  . GLU B 2 14  ? -8.16700  -12.65100 8.79000   1.000 29.20583  ? 14  GLU B OE1  1 
ATOM   4843 O OE2  . GLU B 2 14  ? -7.98300  -10.46900 9.05600   1.000 23.47444  ? 14  GLU B OE2  1 
ATOM   4844 H H    . GLU B 2 14  ? -7.36200  -10.05500 4.90500   1.000 30.01879  ? 14  GLU B H    1 
ATOM   4845 H HA   . GLU B 2 14  ? -5.74700  -12.06600 4.83100   1.000 30.06771  ? 14  GLU B HA   1 
ATOM   4846 H HB2  . GLU B 2 14  ? -8.33200  -11.95800 5.99300   1.000 30.28970  ? 14  GLU B HB2  1 
ATOM   4847 H HB3  . GLU B 2 14  ? -7.32700  -13.15900 6.25400   1.000 30.28970  ? 14  GLU B HB3  1 
ATOM   4848 H HG2  . GLU B 2 14  ? -5.95600  -11.86000 7.47400   1.000 30.28466  ? 14  GLU B HG2  1 
ATOM   4849 H HG3  . GLU B 2 14  ? -6.68500  -10.52900 6.98900   1.000 30.28466  ? 14  GLU B HG3  1 
ATOM   4850 N N    . GLY B 2 15  ? -8.33600  -12.57800 3.02000   1.000 27.61956  ? 15  GLY B N    1 
ATOM   4851 C CA   . GLY B 2 15  ? -8.86400  -13.47800 2.00800   1.000 29.65456  ? 15  GLY B CA   1 
ATOM   4852 C C    . GLY B 2 15  ? -8.08300  -13.48100 0.70700   1.000 29.24179  ? 15  GLY B C    1 
ATOM   4853 O O    . GLY B 2 15  ? -8.42700  -14.21800 -0.22000  1.000 30.17075  ? 15  GLY B O    1 
ATOM   4854 H H    . GLY B 2 15  ? -8.80500  -11.87000 3.15600   1.000 33.14427  ? 15  GLY B H    1 
ATOM   4855 H HA2  . GLY B 2 15  ? -8.86700  -14.38200 2.35900   1.000 35.58627  ? 15  GLY B HA2  1 
ATOM   4856 H HA3  . GLY B 2 15  ? -9.78000  -13.22800 1.80900   1.000 35.58627  ? 15  GLY B HA3  1 
ATOM   4857 N N    . CYS B 2 16  ? -7.02400  -12.68300 0.62400   1.000 27.87718  ? 16  CYS B N    1 
ATOM   4858 C CA   . CYS B 2 16  ? -6.17800  -12.65000 -0.56100  1.000 25.75684  ? 16  CYS B CA   1 
ATOM   4859 C C    . CYS B 2 16  ? -4.82700  -13.32900 -0.36700  1.000 26.91593  ? 16  CYS B C    1 
ATOM   4860 O O    . CYS B 2 16  ? -4.04400  -13.40600 -1.32600  1.000 27.68061  ? 16  CYS B O    1 
ATOM   4861 C CB   . CYS B 2 16  ? -5.92300  -11.19500 -0.96500  1.000 25.48655  ? 16  CYS B CB   1 
ATOM   4862 S SG   . CYS B 2 16  ? -7.47600  -10.34800 -1.35700  1.000 30.90762  ? 16  CYS B SG   1 
ATOM   4863 H H    . CYS B 2 16  ? -6.77200  -12.14400 1.24500   1.000 33.45342  ? 16  CYS B H    1 
ATOM   4864 H HA   . CYS B 2 16  ? -6.63300  -13.09000 -1.29500  1.000 30.90901  ? 16  CYS B HA   1 
ATOM   4865 H HB2  . CYS B 2 16  ? -5.49700  -10.72700 -0.23000  1.000 30.58466  ? 16  CYS B HB2  1 
ATOM   4866 H HB3  . CYS B 2 16  ? -5.35600  -11.17400 -1.75200  1.000 30.58466  ? 16  CYS B HB3  1 
ATOM   4867 H HG   . CYS B 2 16  ? -8.18700  -10.36900 -0.39000  1.000 37.08995  ? 16  CYS B HG   1 
ATOM   4868 N N    . MET B 2 17  ? -4.49900  -13.78100 0.84300   1.000 27.27155  ? 17  MET B N    1 
ATOM   4869 C CA   . MET B 2 17  ? -3.15000  -14.30000 1.08200   1.000 27.90467  ? 17  MET B CA   1 
ATOM   4870 C C    . MET B 2 17  ? -3.08500  -15.78300 0.73000   1.000 30.32334  ? 17  MET B C    1 
ATOM   4871 O O    . MET B 2 17  ? -4.00100  -16.54200 1.03400   1.000 28.41289  ? 17  MET B O    1 
ATOM   4872 C CB   . MET B 2 17  ? -2.73900  -14.05200 2.54300   1.000 31.49635  ? 17  MET B CB   1 
ATOM   4873 C CG   . MET B 2 17  ? -2.76200  -12.57500 2.96000   1.000 29.58186  ? 17  MET B CG   1 
ATOM   4874 S SD   . MET B 2 17  ? -1.82100  -11.46900 1.83900   1.000 29.27724  ? 17  MET B SD   1 
ATOM   4875 C CE   . MET B 2 17  ? -0.22400  -12.27700 1.83600   1.000 29.85300  ? 17  MET B CE   1 
ATOM   4876 H H    . MET B 2 17  ? -5.02200  -13.79900 1.52600   1.000 32.72666  ? 17  MET B H    1 
ATOM   4877 H HA   . MET B 2 17  ? -2.52600  -13.82200 0.51500   1.000 33.48640  ? 17  MET B HA   1 
ATOM   4878 H HB2  . MET B 2 17  ? -3.35100  -14.53100 3.12300   1.000 37.79643  ? 17  MET B HB2  1 
ATOM   4879 H HB3  . MET B 2 17  ? -1.83700  -14.38400 2.67400   1.000 37.79643  ? 17  MET B HB3  1 
ATOM   4880 H HG2  . MET B 2 17  ? -3.68200  -12.26900 2.97300   1.000 35.49903  ? 17  MET B HG2  1 
ATOM   4881 H HG3  . MET B 2 17  ? -2.37700  -12.49500 3.84700   1.000 35.49903  ? 17  MET B HG3  1 
ATOM   4882 H HE1  . MET B 2 17  ? 0.39800   -11.74300 1.31800   1.000 35.82440  ? 17  MET B HE1  1 
ATOM   4883 H HE2  . MET B 2 17  ? 0.09000   -12.35800 2.75000   1.000 35.82440  ? 17  MET B HE2  1 
ATOM   4884 H HE3  . MET B 2 17  ? -0.31600  -13.15700 1.43800   1.000 35.82440  ? 17  MET B HE3  1 
ATOM   4885 N N    . VAL B 2 18  ? -2.00600  -16.18200 0.06000   1.000 30.43076  ? 18  VAL B N    1 
ATOM   4886 C CA   . VAL B 2 18  ? -1.80400  -17.55700 -0.35600  1.000 32.98244  ? 18  VAL B CA   1 
ATOM   4887 C C    . VAL B 2 18  ? -0.34800  -17.88900 -0.09200  1.000 31.40426  ? 18  VAL B C    1 
ATOM   4888 O O    . VAL B 2 18  ? 0.47600   -17.00900 0.14300   1.000 30.71269  ? 18  VAL B O    1 
ATOM   4889 C CB   . VAL B 2 18  ? -2.15400  -17.78900 -1.85800  1.000 31.24065  ? 18  VAL B CB   1 
ATOM   4890 C CG1  . VAL B 2 18  ? -3.60400  -17.46500 -2.11900  1.000 32.11678  ? 18  VAL B CG1  1 
ATOM   4891 C CG2  . VAL B 2 18  ? -1.25700  -16.93500 -2.76000  1.000 30.23131  ? 18  VAL B CG2  1 
ATOM   4892 H H    . VAL B 2 18  ? -1.36400  -15.65700 -0.16800  1.000 36.51772  ? 18  VAL B H    1 
ATOM   4893 H HA   . VAL B 2 18  ? -2.35600  -18.14500 0.18300   1.000 39.57973  ? 18  VAL B HA   1 
ATOM   4894 H HB   . VAL B 2 18  ? -2.00700  -18.72200 -2.08000  1.000 37.48959  ? 18  VAL B HB   1 
ATOM   4895 H HG11 . VAL B 2 18  ? -3.80500  -17.64700 -3.05000  1.000 38.54094  ? 18  VAL B HG11 1 
ATOM   4896 H HG12 . VAL B 2 18  ? -4.15800  -18.01800 -1.54600  1.000 38.54094  ? 18  VAL B HG12 1 
ATOM   4897 H HG13 . VAL B 2 18  ? -3.75800  -16.52700 -1.92400  1.000 38.54094  ? 18  VAL B HG13 1 
ATOM   4898 H HG21 . VAL B 2 18  ? -1.59200  -16.97900 -3.66900  1.000 36.27837  ? 18  VAL B HG21 1 
ATOM   4899 H HG22 . VAL B 2 18  ? -1.27500  -16.01800 -2.44600  1.000 36.27837  ? 18  VAL B HG22 1 
ATOM   4900 H HG23 . VAL B 2 18  ? -0.35100  -17.27900 -2.72500  1.000 36.27837  ? 18  VAL B HG23 1 
ATOM   4901 N N    . GLN B 2 19  ? -0.02300  -19.17700 -0.21000  1.000 33.56540  ? 19  GLN B N    1 
ATOM   4902 C CA   . GLN B 2 19  ? 1.38100   -19.62600 -0.06900  1.000 33.22483  ? 19  GLN B CA   1 
ATOM   4903 C C    . GLN B 2 19  ? 1.94900   -19.90000 -1.46200  1.000 36.34954  ? 19  GLN B C    1 
ATOM   4904 O O    . GLN B 2 19  ? 1.26700   -20.55100 -2.24600  1.000 37.93094  ? 19  GLN B O    1 
ATOM   4905 C CB   . GLN B 2 19  ? 1.44600   -20.91800 0.73400   1.000 34.68430  ? 19  GLN B CB   1 
ATOM   4906 C CG   . GLN B 2 19  ? 2.86300   -21.37800 1.02400   1.000 42.22476  ? 19  GLN B CG   1 
ATOM   4907 C CD   . GLN B 2 19  ? 2.88900   -22.71300 1.72200   1.000 50.41608  ? 19  GLN B CD   1 
ATOM   4908 O OE1  . GLN B 2 19  ? 3.51700   -22.87500 2.76200   1.000 52.12387  ? 19  GLN B OE1  1 
ATOM   4909 N NE2  . GLN B 2 19  ? 2.20300   -23.68400 1.14800   1.000 54.90867  ? 19  GLN B NE2  1 
ATOM   4910 H H    . GLN B 2 19  ? -0.58300  -19.81000 -0.37000  1.000 40.27928  ? 19  GLN B H    1 
ATOM   4911 H HA   . GLN B 2 19  ? 1.91500   -18.94600 0.37000   1.000 39.87059  ? 19  GLN B HA   1 
ATOM   4912 H HB2  . GLN B 2 19  ? 0.99700   -20.78200 1.58300   1.000 41.62197  ? 19  GLN B HB2  1 
ATOM   4913 H HB3  . GLN B 2 19  ? 0.99800   -21.61700 0.23300   1.000 41.62197  ? 19  GLN B HB3  1 
ATOM   4914 H HG2  . GLN B 2 19  ? 3.35100   -21.46700 0.19100   1.000 50.67051  ? 19  GLN B HG2  1 
ATOM   4915 H HG3  . GLN B 2 19  ? 3.29700   -20.72800 1.59800   1.000 50.67051  ? 19  GLN B HG3  1 
ATOM   4916 H HE21 . GLN B 2 19  ? 1.77400   -23.53600 0.41800   1.000 65.89120  ? 19  GLN B HE21 1 
ATOM   4917 H HE22 . GLN B 2 19  ? 2.18500   -24.46600 1.50500   1.000 65.89120  ? 19  GLN B HE22 1 
ATOM   4918 N N    . VAL B 2 20  ? 3.13800   -19.38400 -1.73800  1.000 32.85456  ? 20  VAL B N    1 
ATOM   4919 C CA   . VAL B 2 20  ? 3.79100   -19.62900 -3.02100  1.000 36.80563  ? 20  VAL B CA   1 
ATOM   4920 C C    . VAL B 2 20  ? 5.07700   -20.37600 -2.73600  1.000 41.56743  ? 20  VAL B C    1 
ATOM   4921 O O    . VAL B 2 20  ? 5.88500   -19.92100 -1.92000  1.000 37.54327  ? 20  VAL B O    1 
ATOM   4922 C CB   . VAL B 2 20  ? 4.10900   -18.33300 -3.78900  1.000 39.41274  ? 20  VAL B CB   1 
ATOM   4923 C CG1  . VAL B 2 20  ? 4.78500   -18.66200 -5.13300  1.000 40.61726  ? 20  VAL B CG1  1 
ATOM   4924 C CG2  . VAL B 2 20  ? 2.85600   -17.50000 -4.01700  1.000 36.34506  ? 20  VAL B CG2  1 
ATOM   4925 H H    . VAL B 2 20  ? 3.59100   -18.88800 -1.20100  1.000 39.42627  ? 20  VAL B H    1 
ATOM   4926 H HA   . VAL B 2 20  ? 3.22600   -20.18700 -3.57800  1.000 44.16755  ? 20  VAL B HA   1 
ATOM   4927 H HB   . VAL B 2 20  ? 4.72900   -17.80200 -3.26600  1.000 47.29608  ? 20  VAL B HB   1 
ATOM   4928 H HG11 . VAL B 2 20  ? 4.80600   -17.86000 -5.67800  1.000 48.74152  ? 20  VAL B HG11 1 
ATOM   4929 H HG12 . VAL B 2 20  ? 5.68900   -18.97100 -4.96800  1.000 48.74152  ? 20  VAL B HG12 1 
ATOM   4930 H HG13 . VAL B 2 20  ? 4.27400   -19.35300 -5.58200  1.000 48.74152  ? 20  VAL B HG13 1 
ATOM   4931 H HG21 . VAL B 2 20  ? 3.09200   -16.70700 -4.52300  1.000 43.61487  ? 20  VAL B HG21 1 
ATOM   4932 H HG22 . VAL B 2 20  ? 2.21200   -18.02900 -4.51300  1.000 43.61487  ? 20  VAL B HG22 1 
ATOM   4933 H HG23 . VAL B 2 20  ? 2.48500   -17.24600 -3.15800  1.000 43.61487  ? 20  VAL B HG23 1 
ATOM   4934 N N    . THR B 2 21  ? 5.27900   -21.50200 -3.42400  1.000 42.35938  ? 21  THR B N    1 
ATOM   4935 C CA   . THR B 2 21  ? 6.48500   -22.30100 -3.24000  1.000 44.49293  ? 21  THR B CA   1 
ATOM   4936 C C    . THR B 2 21  ? 7.14800   -22.56700 -4.58400  1.000 48.33852  ? 21  THR B C    1 
ATOM   4937 O O    . THR B 2 21  ? 6.48300   -22.93700 -5.55800  1.000 47.82375  ? 21  THR B O    1 
ATOM   4938 C CB   . THR B 2 21  ? 6.17800   -23.64000 -2.55700  1.000 44.75170  ? 21  THR B CB   1 
ATOM   4939 O OG1  . THR B 2 21  ? 5.68700   -23.40700 -1.22400  1.000 42.16329  ? 21  THR B OG1  1 
ATOM   4940 C CG2  . THR B 2 21  ? 7.44700   -24.49100 -2.49100  1.000 48.63591  ? 21  THR B CG2  1 
ATOM   4941 H H    . THR B 2 21  ? 4.73000   -21.82300 -4.00300  1.000 50.83205  ? 21  THR B H    1 
ATOM   4942 H HA   . THR B 2 21  ? 7.11400   -21.81500 -2.68400  1.000 53.39232  ? 21  THR B HA   1 
ATOM   4943 H HB   . THR B 2 21  ? 5.51000   -24.12100 -3.07000  1.000 53.70285  ? 21  THR B HB   1 
ATOM   4944 H HG1  . THR B 2 21  ? 6.26400   -22.99600 -0.77300  1.000 50.59675  ? 21  THR B HG1  1 
ATOM   4945 H HG21 . THR B 2 21  ? 7.34800   -25.17800 -1.81400  1.000 58.36389  ? 21  THR B HG21 1 
ATOM   4946 H HG22 . THR B 2 21  ? 7.61000   -24.91700 -3.34700  1.000 58.36389  ? 21  THR B HG22 1 
ATOM   4947 H HG23 . THR B 2 21  ? 8.20800   -23.93400 -2.26300  1.000 58.36389  ? 21  THR B HG23 1 
ATOM   4948 N N    . CYS B 2 22  ? 8.46300   -22.39500 -4.63100  1.000 49.28073  ? 22  CYS B N    1 
ATOM   4949 C CA   . CYS B 2 22  ? 9.23400   -22.75500 -5.81800  1.000 52.76500  ? 22  CYS B CA   1 
ATOM   4950 C C    . CYS B 2 22  ? 10.51600  -23.42400 -5.34800  1.000 53.23226  ? 22  CYS B C    1 
ATOM   4951 O O    . CYS B 2 22  ? 11.37400  -22.77500 -4.74300  1.000 49.45050  ? 22  CYS B O    1 
ATOM   4952 C CB   . CYS B 2 22  ? 9.53800   -21.54500 -6.70200  1.000 51.04741  ? 22  CYS B CB   1 
ATOM   4953 S SG   . CYS B 2 22  ? 10.36800  -21.99000 -8.26300  1.000 61.72921  ? 22  CYS B SG   1 
ATOM   4954 H H    . CYS B 2 22  ? 8.93500   -22.07100 -3.98900  1.000 59.13767  ? 22  CYS B H    1 
ATOM   4955 H HA   . CYS B 2 22  ? 8.73300   -23.39700 -6.34500  1.000 63.31880  ? 22  CYS B HA   1 
ATOM   4956 H HB2  . CYS B 2 22  ? 8.70500   -21.09900 -6.92300  1.000 61.25769  ? 22  CYS B HB2  1 
ATOM   4957 H HB3  . CYS B 2 22  ? 10.11900  -20.93900 -6.21700  1.000 61.25769  ? 22  CYS B HB3  1 
ATOM   4958 H HG   . CYS B 2 22  ? 10.55900  -20.99000 -8.89800  1.000 74.07585  ? 22  CYS B HG   1 
ATOM   4959 N N    . GLY B 2 23  ? 10.64300  -24.71500 -5.62900  1.000 55.44261  ? 23  GLY B N    1 
ATOM   4960 C CA   . GLY B 2 23  ? 11.79700  -25.45300 -5.16100  1.000 54.75279  ? 23  GLY B CA   1 
ATOM   4961 C C    . GLY B 2 23  ? 11.72700  -25.52500 -3.65500  1.000 53.51519  ? 23  GLY B C    1 
ATOM   4962 O O    . GLY B 2 23  ? 10.71900  -25.97400 -3.09400  1.000 57.74513  ? 23  GLY B O    1 
ATOM   4963 H H    . GLY B 2 23  ? 10.08000  -25.17900 -6.08400  1.000 66.53194  ? 23  GLY B H    1 
ATOM   4964 H HA2  . GLY B 2 23  ? 11.79400  -26.35200 -5.52600  1.000 65.70415  ? 23  GLY B HA2  1 
ATOM   4965 H HA3  . GLY B 2 23  ? 12.61500  -25.00200 -5.42400  1.000 65.70415  ? 23  GLY B HA3  1 
ATOM   4966 N N    . THR B 2 24  ? 12.76700  -25.05700 -2.97900  1.000 47.54676  ? 24  THR B N    1 
ATOM   4967 C CA   . THR B 2 24  ? 12.78300  -25.08200 -1.52500  1.000 55.07995  ? 24  THR B CA   1 
ATOM   4968 C C    . THR B 2 24  ? 12.42300  -23.74500 -0.89700  1.000 50.80062  ? 24  THR B C    1 
ATOM   4969 O O    . THR B 2 24  ? 12.34200  -23.66600 0.33900   1.000 52.59459  ? 24  THR B O    1 
ATOM   4970 C CB   . THR B 2 24  ? 14.16100  -25.52200 -1.02000  1.000 53.86886  ? 24  THR B CB   1 
ATOM   4971 O OG1  . THR B 2 24  ? 15.15000  -24.59200 -1.49100  1.000 56.27013  ? 24  THR B OG1  1 
ATOM   4972 C CG2  . THR B 2 24  ? 14.48600  -26.91500 -1.50900  1.000 58.66188  ? 24  THR B CG2  1 
ATOM   4973 H H    . THR B 2 24  ? 13.47300  -24.72100 -3.33700  1.000 57.05691  ? 24  THR B H    1 
ATOM   4974 H HA   . THR B 2 24  ? 12.13700  -25.73500 -1.21400  1.000 66.09674  ? 24  THR B HA   1 
ATOM   4975 H HB   . THR B 2 24  ? 14.16200  -25.53000 -0.05000  1.000 64.64343  ? 24  THR B HB   1 
ATOM   4976 H HG1  . THR B 2 24  ? 15.91200  -24.82100 -1.22100  1.000 67.52496  ? 24  THR B HG1  1 
ATOM   4977 H HG21 . THR B 2 24  ? 15.33600  -27.20500 -1.14300  1.000 70.39506  ? 24  THR B HG21 1 
ATOM   4978 H HG22 . THR B 2 24  ? 13.79400  -27.53400 -1.22800  1.000 70.39506  ? 24  THR B HG22 1 
ATOM   4979 H HG23 . THR B 2 24  ? 14.54100  -26.92300 -2.47700  1.000 70.39506  ? 24  THR B HG23 1 
ATOM   4980 N N    . THR B 2 25  ? 12.11700  -22.72700 -1.71100  1.000 52.49995  ? 25  THR B N    1 
ATOM   4981 C CA   . THR B 2 25  ? 11.78400  -21.39300 -1.21200  1.000 49.95119  ? 25  THR B CA   1 
ATOM   4982 C C    . THR B 2 25  ? 10.27500  -21.30700 -1.06700  1.000 50.03146  ? 25  THR B C    1 
ATOM   4983 O O    . THR B 2 25  ? 9.53500   -21.61100 -2.01500  1.000 45.21104  ? 25  THR B O    1 
ATOM   4984 C CB   . THR B 2 25  ? 12.23800  -20.28900 -2.17900  1.000 51.41635  ? 25  THR B CB   1 
ATOM   4985 O OG1  . THR B 2 25  ? 13.60600  -20.48200 -2.56200  1.000 58.04927  ? 25  THR B OG1  1 
ATOM   4986 C CG2  . THR B 2 25  ? 12.09700  -18.91300 -1.53000  1.000 53.19013  ? 25  THR B CG2  1 
ATOM   4987 H H    . THR B 2 25  ? 12.09600  -22.78700 -2.56800  1.000 63.00074  ? 25  THR B H    1 
ATOM   4988 H HA   . THR B 2 25  ? 12.19600  -21.24700 -0.34600  1.000 59.94223  ? 25  THR B HA   1 
ATOM   4989 H HB   . THR B 2 25  ? 11.67900  -20.30900 -2.97100  1.000 61.70043  ? 25  THR B HB   1 
ATOM   4990 H HG1  . THR B 2 25  ? 13.84500  -19.87400 -3.09000  1.000 69.65992  ? 25  THR B HG1  1 
ATOM   4991 H HG21 . THR B 2 25  ? 12.45400  -18.23100 -2.12000  1.000 63.82896  ? 25  THR B HG21 1 
ATOM   4992 H HG22 . THR B 2 25  ? 11.16200  -18.72100 -1.35600  1.000 63.82896  ? 25  THR B HG22 1 
ATOM   4993 H HG23 . THR B 2 25  ? 12.58500  -18.89000 -0.69200  1.000 63.82896  ? 25  THR B HG23 1 
ATOM   4994 N N    . THR B 2 26  ? 9.81700   -20.90000 0.10700   1.000 47.58286  ? 26  THR B N    1 
ATOM   4995 C CA   . THR B 2 26  ? 8.40200   -20.64200 0.30700   1.000 45.52487  ? 26  THR B CA   1 
ATOM   4996 C C    . THR B 2 26  ? 8.22500   -19.22700 0.84900   1.000 44.36304  ? 26  THR B C    1 
ATOM   4997 O O    . THR B 2 26  ? 9.03200   -18.75700 1.65500   1.000 38.66572  ? 26  THR B O    1 
ATOM   4998 C CB   . THR B 2 26  ? 7.78800   -21.69400 1.24200   1.000 46.77595  ? 26  THR B CB   1 
ATOM   4999 O OG1  . THR B 2 26  ? 7.70300   -22.93400 0.52800   1.000 46.86438  ? 26  THR B OG1  1 
ATOM   5000 C CG2  . THR B 2 26  ? 6.43300   -21.30600 1.66400   1.000 47.79179  ? 26  THR B CG2  1 
ATOM   5001 H H    . THR B 2 26  ? 10.30400  -20.76600 0.80300   1.000 57.10024  ? 26  THR B H    1 
ATOM   5002 H HA   . THR B 2 26  ? 7.94100   -20.69400 -0.54400  1.000 54.63064  ? 26  THR B HA   1 
ATOM   5003 H HB   . THR B 2 26  ? 8.34400   -21.80300 2.02900   1.000 56.13194  ? 26  THR B HB   1 
ATOM   5004 H HG1  . THR B 2 26  ? 7.36900   -23.52700 1.02100   1.000 56.23805  ? 26  THR B HG1  1 
ATOM   5005 H HG21 . THR B 2 26  ? 5.96200   -22.08000 2.01000   1.000 57.35095  ? 26  THR B HG21 1 
ATOM   5006 H HG22 . THR B 2 26  ? 6.47900   -20.63100 2.35900   1.000 57.35095  ? 26  THR B HG22 1 
ATOM   5007 H HG23 . THR B 2 26  ? 5.93900   -20.95100 0.90800   1.000 57.35095  ? 26  THR B HG23 1 
ATOM   5008 N N    . LEU B 2 27  ? 7.22900   -18.52400 0.32200   1.000 38.90723  ? 27  LEU B N    1 
ATOM   5009 C CA   . LEU B 2 27  ? 6.89400   -17.19700 0.87400   1.000 30.94655  ? 27  LEU B CA   1 
ATOM   5010 C C    . LEU B 2 27  ? 5.40300   -16.95800 0.66600   1.000 32.80725  ? 27  LEU B C    1 
ATOM   5011 O O    . LEU B 2 27  ? 4.68400   -17.91400 0.39000   1.000 33.05730  ? 27  LEU B O    1 
ATOM   5012 C CB   . LEU B 2 27  ? 7.78400   -16.09300 0.29500   1.000 32.27575  ? 27  LEU B CB   1 
ATOM   5013 C CG   . LEU B 2 27  ? 8.14500   -16.15700 -1.18400  1.000 37.49823  ? 27  LEU B CG   1 
ATOM   5014 C CD1  . LEU B 2 27  ? 6.97100   -15.75800 -2.06200  1.000 40.30286  ? 27  LEU B CD1  1 
ATOM   5015 C CD2  . LEU B 2 27  ? 9.32300   -15.24200 -1.46000  1.000 47.15383  ? 27  LEU B CD2  1 
ATOM   5016 H H    . LEU B 2 27  ? 6.73900   -18.77600 -0.33800  1.000 46.68948  ? 27  LEU B H    1 
ATOM   5017 H HA   . LEU B 2 27  ? 7.05000   -17.21800 1.83100   1.000 37.13666  ? 27  LEU B HA   1 
ATOM   5018 H HB2  . LEU B 2 27  ? 7.36100   -15.23500 0.44400   1.000 38.73170  ? 27  LEU B HB2  1 
ATOM   5019 H HB3  . LEU B 2 27  ? 8.62200   -16.11300 0.78300   1.000 38.73170  ? 27  LEU B HB3  1 
ATOM   5020 H HG   . LEU B 2 27  ? 8.40400   -17.06200 -1.41400  1.000 44.99867  ? 27  LEU B HG   1 
ATOM   5021 H HD11 . LEU B 2 27  ? 7.27900   -15.65100 -2.97500  1.000 48.36424  ? 27  LEU B HD11 1 
ATOM   5022 H HD12 . LEU B 2 27  ? 6.29600   -16.45300 -2.02000  1.000 48.36424  ? 27  LEU B HD12 1 
ATOM   5023 H HD13 . LEU B 2 27  ? 6.60500   -14.92100 -1.73700  1.000 48.36424  ? 27  LEU B HD13 1 
ATOM   5024 H HD21 . LEU B 2 27  ? 9.54000   -15.28000 -2.40400  1.000 56.58540  ? 27  LEU B HD21 1 
ATOM   5025 H HD22 . LEU B 2 27  ? 9.08300   -14.33600 -1.21200  1.000 56.58540  ? 27  LEU B HD22 1 
ATOM   5026 H HD23 . LEU B 2 27  ? 10.08200  -15.53900 -0.93500  1.000 56.58540  ? 27  LEU B HD23 1 
ATOM   5027 N N    . ASN B 2 28  ? 4.97900   -15.71500 0.83000   1.000 29.55875  ? 28  ASN B N    1 
ATOM   5028 C CA   . ASN B 2 28  ? 3.56700   -15.39100 0.69100   1.000 26.98772  ? 28  ASN B CA   1 
ATOM   5029 C C    . ASN B 2 28  ? 3.24600   -14.75700 -0.66100  1.000 29.06476  ? 28  ASN B C    1 
ATOM   5030 O O    . ASN B 2 28  ? 4.08200   -14.07700 -1.26100  1.000 29.02442  ? 28  ASN B O    1 
ATOM   5031 C CB   . ASN B 2 28  ? 3.12500   -14.46300 1.81800   1.000 25.83924  ? 28  ASN B CB   1 
ATOM   5032 C CG   . ASN B 2 28  ? 3.48300   -15.05000 3.20300   1.000 30.44294  ? 28  ASN B CG   1 
ATOM   5033 O OD1  . ASN B 2 28  ? 2.76700   -15.91100 3.70600   1.000 30.25432  ? 28  ASN B OD1  1 
ATOM   5034 N ND2  . ASN B 2 28  ? 4.62700   -14.63400 3.77000   1.000 29.65807  ? 28  ASN B ND2  1 
ATOM   5035 H H    . ASN B 2 28  ? 5.47800   -15.04400 1.02600   1.000 35.47130  ? 28  ASN B H    1 
ATOM   5036 H HA   . ASN B 2 28  ? 3.04900   -16.20700 0.76400   1.000 32.38607  ? 28  ASN B HA   1 
ATOM   5037 H HB2  . ASN B 2 28  ? 3.57400   -13.60800 1.72400   1.000 31.00789  ? 28  ASN B HB2  1 
ATOM   5038 H HB3  . ASN B 2 28  ? 2.16300   -14.34400 1.77700   1.000 31.00789  ? 28  ASN B HB3  1 
ATOM   5039 H HD21 . ASN B 2 28  ? 4.86300   -14.94200 4.53700   1.000 35.59049  ? 28  ASN B HD21 1 
ATOM   5040 H HD22 . ASN B 2 28  ? 5.10800   -14.03800 3.37900   1.000 35.59049  ? 28  ASN B HD22 1 
ATOM   5041 N N    . GLY B 2 29  ? 2.01400   -14.96300 -1.12000  1.000 29.51323  ? 29  GLY B N    1 
ATOM   5042 C CA   . GLY B 2 29  ? 1.55300   -14.33400 -2.34100  1.000 28.62409  ? 29  GLY B CA   1 
ATOM   5043 C C    . GLY B 2 29  ? 0.23700   -13.61700 -2.08100  1.000 28.49499  ? 29  GLY B C    1 
ATOM   5044 O O    . GLY B 2 29  ? -0.48300  -13.92100 -1.12900  1.000 28.69206  ? 29  GLY B O    1 
ATOM   5045 H H    . GLY B 2 29  ? 1.42900   -15.46400 -0.73800  1.000 35.41668  ? 29  GLY B H    1 
ATOM   5046 H HA2  . GLY B 2 29  ? 2.20500   -13.68900 -2.65600  1.000 34.34971  ? 29  GLY B HA2  1 
ATOM   5047 H HA3  . GLY B 2 29  ? 1.41600   -15.00500 -3.02800  1.000 34.34971  ? 29  GLY B HA3  1 
ATOM   5048 N N    . LEU B 2 30  ? -0.08100  -12.66500 -2.95600  1.000 27.12702  ? 30  LEU B N    1 
ATOM   5049 C CA   . LEU B 2 30  ? -1.29800  -11.86300 -2.83700  1.000 26.52882  ? 30  LEU B CA   1 
ATOM   5050 C C    . LEU B 2 30  ? -2.15000  -12.21200 -4.05000  1.000 26.66702  ? 30  LEU B C    1 
ATOM   5051 O O    . LEU B 2 30  ? -1.77000  -11.90700 -5.19600  1.000 28.18332  ? 30  LEU B O    1 
ATOM   5052 C CB   . LEU B 2 30  ? -0.96700  -10.36900 -2.80100  1.000 24.71298  ? 30  LEU B CB   1 
ATOM   5053 C CG   . LEU B 2 30  ? -2.15800  -9.41200  -2.67700  1.000 23.81127  ? 30  LEU B CG   1 
ATOM   5054 C CD1  . LEU B 2 30  ? -2.76900  -9.55500  -1.27600  1.000 27.13659  ? 30  LEU B CD1  1 
ATOM   5055 C CD2  . LEU B 2 30  ? -1.64500  -7.95900  -2.93200  1.000 25.28845  ? 30  LEU B CD2  1 
ATOM   5056 H H    . LEU B 2 30  ? 0.40000   -12.46100 -3.63900  1.000 32.55322  ? 30  LEU B H    1 
ATOM   5057 H HA   . LEU B 2 30  ? -1.78100  -12.10200 -2.03100  1.000 31.83539  ? 30  LEU B HA   1 
ATOM   5058 H HB2  . LEU B 2 30  ? -0.38500  -10.20500 -2.04200  1.000 29.65638  ? 30  LEU B HB2  1 
ATOM   5059 H HB3  . LEU B 2 30  ? -0.49900  -10.14200 -3.62000  1.000 29.65638  ? 30  LEU B HB3  1 
ATOM   5060 H HG   . LEU B 2 30  ? -2.83100  -9.63000  -3.34000  1.000 28.57433  ? 30  LEU B HG   1 
ATOM   5061 H HD11 . LEU B 2 30  ? -3.48200  -8.90500  -1.17600  1.000 32.56471  ? 30  LEU B HD11 1 
ATOM   5062 H HD12 . LEU B 2 30  ? -3.12200  -10.45300 -1.17500  1.000 32.56471  ? 30  LEU B HD12 1 
ATOM   5063 H HD13 . LEU B 2 30  ? -2.08000  -9.39300  -0.61300  1.000 32.56471  ? 30  LEU B HD13 1 
ATOM   5064 H HD21 . LEU B 2 30  ? -2.37800  -7.33800  -2.79700  1.000 30.34694  ? 30  LEU B HD21 1 
ATOM   5065 H HD22 . LEU B 2 30  ? -0.92700  -7.76300  -2.31200  1.000 30.34694  ? 30  LEU B HD22 1 
ATOM   5066 H HD23 . LEU B 2 30  ? -1.32000  -7.89500  -3.84400  1.000 30.34694  ? 30  LEU B HD23 1 
ATOM   5067 N N    . TRP B 2 31  ? -3.26700  -12.88900 -3.81200  1.000 27.94561  ? 31  TRP B N    1 
ATOM   5068 C CA   . TRP B 2 31  ? -4.12300  -13.44100 -4.86700  1.000 27.32040  ? 31  TRP B CA   1 
ATOM   5069 C C    . TRP B 2 31  ? -5.27900  -12.46300 -5.09600  1.000 27.44715  ? 31  TRP B C    1 
ATOM   5070 O O    . TRP B 2 31  ? -6.14400  -12.31400 -4.23800  1.000 27.14636  ? 31  TRP B O    1 
ATOM   5071 C CB   . TRP B 2 31  ? -4.64800  -14.80800 -4.44300  1.000 29.08936  ? 31  TRP B CB   1 
ATOM   5072 C CG   . TRP B 2 31  ? -5.55000  -15.48600 -5.43700  1.000 29.99823  ? 31  TRP B CG   1 
ATOM   5073 C CD1  . TRP B 2 31  ? -5.63900  -15.25600 -6.77300  1.000 30.62354  ? 31  TRP B CD1  1 
ATOM   5074 C CD2  . TRP B 2 31  ? -6.51600  -16.51100 -5.13900  1.000 31.39673  ? 31  TRP B CD2  1 
ATOM   5075 N NE1  . TRP B 2 31  ? -6.58900  -16.08300 -7.34000  1.000 30.28446  ? 31  TRP B NE1  1 
ATOM   5076 C CE2  . TRP B 2 31  ? -7.13500  -16.86700 -6.35500  1.000 34.83079  ? 31  TRP B CE2  1 
ATOM   5077 C CE3  . TRP B 2 31  ? -6.89900  -17.16900 -3.95800  1.000 30.82682  ? 31  TRP B CE3  1 
ATOM   5078 C CZ2  . TRP B 2 31  ? -8.14000  -17.83700 -6.42400  1.000 36.31582  ? 31  TRP B CZ2  1 
ATOM   5079 C CZ3  . TRP B 2 31  ? -7.87800  -18.13300 -4.02800  1.000 35.19938  ? 31  TRP B CZ3  1 
ATOM   5080 C CH2  . TRP B 2 31  ? -8.48500  -18.46500 -5.25500  1.000 34.87490  ? 31  TRP B CH2  1 
ATOM   5081 H H    . TRP B 2 31  ? -3.56300  -13.04900 -3.02100  1.000 33.53553  ? 31  TRP B H    1 
ATOM   5082 H HA   . TRP B 2 31  ? -3.61900  -13.53600 -5.69000  1.000 32.78528  ? 31  TRP B HA   1 
ATOM   5083 H HB2  . TRP B 2 31  ? -3.89100  -15.39400 -4.28900  1.000 34.90804  ? 31  TRP B HB2  1 
ATOM   5084 H HB3  . TRP B 2 31  ? -5.14900  -14.70300 -3.61900  1.000 34.90804  ? 31  TRP B HB3  1 
ATOM   5085 H HD1  . TRP B 2 31  ? -5.12500  -14.63800 -7.24100  1.000 36.74905  ? 31  TRP B HD1  1 
ATOM   5086 H HE1  . TRP B 2 31  ? -6.80300  -16.10300 -8.17300  1.000 36.34216  ? 31  TRP B HE1  1 
ATOM   5087 H HE3  . TRP B 2 31  ? -6.49800  -16.95800 -3.14600  1.000 36.99299  ? 31  TRP B HE3  1 
ATOM   5088 H HZ2  . TRP B 2 31  ? -8.54200  -18.06200 -7.23200  1.000 43.57979  ? 31  TRP B HZ2  1 
ATOM   5089 H HZ3  . TRP B 2 31  ? -8.14000  -18.57600 -3.25300  1.000 42.24006  ? 31  TRP B HZ3  1 
ATOM   5090 H HH2  . TRP B 2 31  ? -9.14600  -19.11900 -5.27100  1.000 41.85068  ? 31  TRP B HH2  1 
ATOM   5091 N N    . LEU B 2 32  ? -5.24900  -11.76200 -6.22500  1.000 28.69284  ? 32  LEU B N    1 
ATOM   5092 C CA   . LEU B 2 32  ? -6.24300  -10.75700 -6.60400  1.000 30.97135  ? 32  LEU B CA   1 
ATOM   5093 C C    . LEU B 2 32  ? -6.73100  -11.06800 -8.00900  1.000 28.38173  ? 32  LEU B C    1 
ATOM   5094 O O    . LEU B 2 32  ? -5.91800  -11.25800 -8.91100  1.000 27.46583  ? 32  LEU B O    1 
ATOM   5095 C CB   . LEU B 2 32  ? -5.66100  -9.33300  -6.58100  1.000 28.13988  ? 32  LEU B CB   1 
ATOM   5096 C CG   . LEU B 2 32  ? -5.11600  -8.87000  -5.22200  1.000 27.66968  ? 32  LEU B CG   1 
ATOM   5097 C CD1  . LEU B 2 32  ? -4.29600  -7.57500  -5.44900  1.000 29.77436  ? 32  LEU B CD1  1 
ATOM   5098 C CD2  . LEU B 2 32  ? -6.26100  -8.63800  -4.22400  1.000 26.90132  ? 32  LEU B CD2  1 
ATOM   5099 H H    . LEU B 2 32  ? -4.63200  -11.85600 -6.81700  1.000 34.43221  ? 32  LEU B H    1 
ATOM   5100 H HA   . LEU B 2 32  ? -6.99800  -10.79500 -5.99600  1.000 37.16642  ? 32  LEU B HA   1 
ATOM   5101 H HB2  . LEU B 2 32  ? -4.93200  -9.29000  -7.21900  1.000 33.76866  ? 32  LEU B HB2  1 
ATOM   5102 H HB3  . LEU B 2 32  ? -6.35800  -8.71100  -6.84300  1.000 33.76866  ? 32  LEU B HB3  1 
ATOM   5103 H HG   . LEU B 2 32  ? -4.52600  -9.55000  -4.86200  1.000 33.20442  ? 32  LEU B HG   1 
ATOM   5104 H HD11 . LEU B 2 32  ? -3.82600  -7.35200  -4.63000  1.000 35.73003  ? 32  LEU B HD11 1 
ATOM   5105 H HD12 . LEU B 2 32  ? -3.65900  -7.72400  -6.16600  1.000 35.73003  ? 32  LEU B HD12 1 
ATOM   5106 H HD13 . LEU B 2 32  ? -4.90300  -6.85900  -5.68800  1.000 35.73003  ? 32  LEU B HD13 1 
ATOM   5107 H HD21 . LEU B 2 32  ? -5.88900  -8.32900  -3.38300  1.000 32.28239  ? 32  LEU B HD21 1 
ATOM   5108 H HD22 . LEU B 2 32  ? -6.86300  -7.96900  -4.58500  1.000 32.28239  ? 32  LEU B HD22 1 
ATOM   5109 H HD23 . LEU B 2 32  ? -6.73600  -9.47300  -4.08900  1.000 32.28239  ? 32  LEU B HD23 1 
ATOM   5110 N N    . ASP B 2 33  ? -8.04600  -11.12400 -8.20300  1.000 28.80591  ? 33  ASP B N    1 
ATOM   5111 C CA   . ASP B 2 33  ? -8.56400  -11.52500 -9.51700  1.000 30.68668  ? 33  ASP B CA   1 
ATOM   5112 C C    . ASP B 2 33  ? -7.86300  -12.84400 -9.87000  1.000 29.07881  ? 33  ASP B C    1 
ATOM   5113 O O    . ASP B 2 33  ? -7.72900  -13.72000 -9.00600  1.000 31.90575  ? 33  ASP B O    1 
ATOM   5114 C CB   . ASP B 2 33  ? -8.36600  -10.38600 -10.53000 1.000 30.39597  ? 33  ASP B CB   1 
ATOM   5115 C CG   . ASP B 2 33  ? -9.17200  -9.13500  -10.14800 1.000 34.32806  ? 33  ASP B CG   1 
ATOM   5116 O OD1  . ASP B 2 33  ? -10.42500 -9.22100  -10.00900 1.000 35.15292  ? 33  ASP B OD1  1 
ATOM   5117 O OD2  . ASP B 2 33  ? -8.52600  -8.09400  -9.90600  1.000 38.25166  ? 33  ASP B OD2  1 
ATOM   5118 H H    . ASP B 2 33  ? -8.64500  -10.94200 -7.61400  1.000 34.56789  ? 33  ASP B H    1 
ATOM   5119 H HA   . ASP B 2 33  ? -9.51500  -11.70000 -9.44400  1.000 36.82481  ? 33  ASP B HA   1 
ATOM   5120 H HB2  . ASP B 2 33  ? -7.42700  -10.14400 -10.56100 1.000 36.47596  ? 33  ASP B HB2  1 
ATOM   5121 H HB3  . ASP B 2 33  ? -8.66400  -10.68200 -11.40400 1.000 36.47596  ? 33  ASP B HB3  1 
ATOM   5122 N N    . ASP B 2 34  ? -7.38100  -13.03200 -11.07500 1.000 29.03320  ? 34  ASP B N    1 
ATOM   5123 C CA   . ASP B 2 34  ? -6.74000  -14.30300 -11.40700 1.000 31.53368  ? 34  ASP B CA   1 
ATOM   5124 C C    . ASP B 2 34  ? -5.20900  -14.22300 -11.46500 1.000 31.90712  ? 34  ASP B C    1 
ATOM   5125 O O    . ASP B 2 34  ? -4.56900  -14.95300 -12.23200 1.000 34.16918  ? 34  ASP B O    1 
ATOM   5126 C CB   . ASP B 2 34  ? -7.32300  -14.86600 -12.69500 1.000 34.08178  ? 34  ASP B CB   1 
ATOM   5127 C CG   . ASP B 2 34  ? -7.13300  -13.93900 -13.88900 1.000 40.61728  ? 34  ASP B CG   1 
ATOM   5128 O OD1  . ASP B 2 34  ? -6.73300  -12.76700 -13.70200 1.000 38.20352  ? 34  ASP B OD1  1 
ATOM   5129 O OD2  . ASP B 2 34  ? -7.36100  -14.41100 -15.01700 1.000 41.76804  ? 34  ASP B OD2  1 
ATOM   5130 H H    . ASP B 2 34  ? -7.40500  -12.45900 -11.71600 1.000 34.84064  ? 34  ASP B H    1 
ATOM   5131 H HA   . ASP B 2 34  ? -6.95300  -14.94700 -10.71500 1.000 37.84122  ? 34  ASP B HA   1 
ATOM   5132 H HB2  . ASP B 2 34  ? -6.88600  -15.70800 -12.89700 1.000 40.89894  ? 34  ASP B HB2  1 
ATOM   5133 H HB3  . ASP B 2 34  ? -8.27500  -15.00700 -12.57500 1.000 40.89894  ? 34  ASP B HB3  1 
ATOM   5134 N N    . VAL B 2 35  ? -4.59900  -13.37000 -10.64300 1.000 35.07231  ? 35  VAL B N    1 
ATOM   5135 C CA   . VAL B 2 35  ? -3.13900  -13.24200 -10.57400 1.000 32.70617  ? 35  VAL B CA   1 
ATOM   5136 C C    . VAL B 2 35  ? -2.69200  -13.31400 -9.12100  1.000 29.79666  ? 35  VAL B C    1 
ATOM   5137 O O    . VAL B 2 35  ? -3.35200  -12.76900 -8.22500  1.000 27.01496  ? 35  VAL B O    1 
ATOM   5138 C CB   . VAL B 2 35  ? -2.64600  -11.92500 -11.19300 1.000 33.88297  ? 35  VAL B CB   1 
ATOM   5139 C CG1  . VAL B 2 35  ? -1.13000  -11.76700 -10.94700 1.000 33.66590  ? 35  VAL B CG1  1 
ATOM   5140 C CG2  . VAL B 2 35  ? -2.94300  -11.90700 -12.71100 1.000 38.17298  ? 35  VAL B CG2  1 
ATOM   5141 H H    . VAL B 2 35  ? -5.01500  -12.84400 -10.10500 1.000 42.08757  ? 35  VAL B H    1 
ATOM   5142 H HA   . VAL B 2 35  ? -2.72700  -13.97600 -11.05500 1.000 39.24820  ? 35  VAL B HA   1 
ATOM   5143 H HB   . VAL B 2 35  ? -3.10600  -11.17800 -10.77900 1.000 40.66037  ? 35  VAL B HB   1 
ATOM   5144 H HG11 . VAL B 2 35  ? -0.77800  -11.11300 -11.57100 1.000 40.39988  ? 35  VAL B HG11 1 
ATOM   5145 H HG12 . VAL B 2 35  ? -0.98300  -11.46500 -10.03700 1.000 40.39988  ? 35  VAL B HG12 1 
ATOM   5146 H HG13 . VAL B 2 35  ? -0.69700  -12.62300 -11.08900 1.000 40.39988  ? 35  VAL B HG13 1 
ATOM   5147 H HG21 . VAL B 2 35  ? -2.62200  -11.07100 -13.08500 1.000 45.80838  ? 35  VAL B HG21 1 
ATOM   5148 H HG22 . VAL B 2 35  ? -2.48800  -12.65400 -13.13000 1.000 45.80838  ? 35  VAL B HG22 1 
ATOM   5149 H HG23 . VAL B 2 35  ? -3.90000  -11.98500 -12.84600 1.000 45.80838  ? 35  VAL B HG23 1 
ATOM   5150 N N    . VAL B 2 36  ? -1.55500  -13.96600 -8.89800  1.000 30.94388  ? 36  VAL B N    1 
ATOM   5151 C CA   . VAL B 2 36  ? -0.90500  -14.00700 -7.58800  1.000 30.55818  ? 36  VAL B CA   1 
ATOM   5152 C C    . VAL B 2 36  ? 0.39200   -13.20900 -7.70400  1.000 27.08460  ? 36  VAL B C    1 
ATOM   5153 O O    . VAL B 2 36  ? 1.21600   -13.50400 -8.56900  1.000 29.73247  ? 36  VAL B O    1 
ATOM   5154 C CB   . VAL B 2 36  ? -0.63700  -15.45900 -7.15200  1.000 32.69247  ? 36  VAL B CB   1 
ATOM   5155 C CG1  . VAL B 2 36  ? 0.17200   -15.50100 -5.82200  1.000 33.50681  ? 36  VAL B CG1  1 
ATOM   5156 C CG2  . VAL B 2 36  ? -2.01800  -16.20300 -7.00600  1.000 35.09393  ? 36  VAL B CG2  1 
ATOM   5157 H H    . VAL B 2 36  ? -1.12900  -14.40300 -9.50400  1.000 37.13346  ? 36  VAL B H    1 
ATOM   5158 H HA   . VAL B 2 36  ? -1.47300  -13.58500 -6.92500  1.000 36.67062  ? 36  VAL B HA   1 
ATOM   5159 H HB   . VAL B 2 36  ? -0.12000  -15.91000 -7.83700  1.000 39.23177  ? 36  VAL B HB   1 
ATOM   5160 H HG11 . VAL B 2 36  ? 0.17800   -16.41100 -5.48700  1.000 40.20898  ? 36  VAL B HG11 1 
ATOM   5161 H HG12 . VAL B 2 36  ? 1.08000   -15.20600 -5.99200  1.000 40.20898  ? 36  VAL B HG12 1 
ATOM   5162 H HG13 . VAL B 2 36  ? -0.25300  -14.91500 -5.17600  1.000 40.20898  ? 36  VAL B HG13 1 
ATOM   5163 H HG21 . VAL B 2 36  ? -1.85700  -17.10800 -6.69900  1.000 42.11352  ? 36  VAL B HG21 1 
ATOM   5164 H HG22 . VAL B 2 36  ? -2.56600  -15.72700 -6.36200  1.000 42.11352  ? 36  VAL B HG22 1 
ATOM   5165 H HG23 . VAL B 2 36  ? -2.46100  -16.22000 -7.86900  1.000 42.11352  ? 36  VAL B HG23 1 
ATOM   5166 N N    . TYR B 2 37  ? 0.54500   -12.19000 -6.85700  1.000 28.00522  ? 37  TYR B N    1 
ATOM   5167 C CA   . TYR B 2 37  ? 1.71100   -11.32000 -6.81400  1.000 29.19058  ? 37  TYR B CA   1 
ATOM   5168 C C    . TYR B 2 37  ? 2.64000   -11.78900 -5.69800  1.000 29.74760  ? 37  TYR B C    1 
ATOM   5169 O O    . TYR B 2 37  ? 2.16600   -12.02800 -4.59400  1.000 26.76604  ? 37  TYR B O    1 
ATOM   5170 C CB   . TYR B 2 37  ? 1.26900   -9.88000  -6.53300  1.000 27.30949  ? 37  TYR B CB   1 
ATOM   5171 C CG   . TYR B 2 37  ? 0.35000   -9.34300  -7.60600  1.000 29.12280  ? 37  TYR B CG   1 
ATOM   5172 C CD1  . TYR B 2 37  ? -1.00400  -9.63400  -7.59900  1.000 28.71329  ? 37  TYR B CD1  1 
ATOM   5173 C CD2  . TYR B 2 37  ? 0.87400   -8.61000  -8.68400  1.000 28.89437  ? 37  TYR B CD2  1 
ATOM   5174 C CE1  . TYR B 2 37  ? -1.86400  -9.14600  -8.64500  1.000 32.63463  ? 37  TYR B CE1  1 
ATOM   5175 C CE2  . TYR B 2 37  ? 0.03800   -8.12100  -9.72700  1.000 32.51551  ? 37  TYR B CE2  1 
ATOM   5176 C CZ   . TYR B 2 37  ? -1.33600  -8.39000  -9.67100  1.000 33.58694  ? 37  TYR B CZ   1 
ATOM   5177 O OH   . TYR B 2 37  ? -2.17900  -7.93000  -10.66600 1.000 34.74318  ? 37  TYR B OH   1 
ATOM   5178 H H    . TYR B 2 37  ? -0.04700  -11.97800 -6.27100  1.000 33.60706  ? 37  TYR B H    1 
ATOM   5179 H HA   . TYR B 2 37  ? 2.18500   -11.35000 -7.66000  1.000 35.02950  ? 37  TYR B HA   1 
ATOM   5180 H HB2  . TYR B 2 37  ? 0.79400   -9.85300  -5.68800  1.000 32.77219  ? 37  TYR B HB2  1 
ATOM   5181 H HB3  . TYR B 2 37  ? 2.05200   -9.30900  -6.49400  1.000 32.77219  ? 37  TYR B HB3  1 
ATOM   5182 H HD1  . TYR B 2 37  ? -1.36500  -10.12900 -6.89900  1.000 34.45676  ? 37  TYR B HD1  1 
ATOM   5183 H HD2  . TYR B 2 37  ? 1.78400   -8.42100  -8.70500  1.000 34.67404  ? 37  TYR B HD2  1 
ATOM   5184 H HE1  . TYR B 2 37  ? -2.77700  -9.32400  -8.61900  1.000 39.16235  ? 37  TYR B HE1  1 
ATOM   5185 H HE2  . TYR B 2 37  ? 0.39400   -7.61500  -10.42100 1.000 39.01942  ? 37  TYR B HE2  1 
ATOM   5186 H HH   . TYR B 2 37  ? -1.74300  -7.48500  -11.22900 1.000 41.69262  ? 37  TYR B HH   1 
ATOM   5187 N N    . CYS B 2 38  ? 3.94500   -11.88600 -5.96500  1.000 31.57265  ? 38  CYS B N    1 
ATOM   5188 C CA   . CYS B 2 38  ? 4.88900   -12.23800 -4.90000  1.000 31.99765  ? 38  CYS B CA   1 
ATOM   5189 C C    . CYS B 2 38  ? 6.28000   -11.73000 -5.27400  1.000 33.80874  ? 38  CYS B C    1 
ATOM   5190 O O    . CYS B 2 38  ? 6.51100   -11.30900 -6.41500  1.000 33.17553  ? 38  CYS B O    1 
ATOM   5191 C CB   . CYS B 2 38  ? 4.90500   -13.75400 -4.64600  1.000 33.48242  ? 38  CYS B CB   1 
ATOM   5192 S SG   . CYS B 2 38  ? 5.62400   -14.76200 -5.97400  1.000 37.41797  ? 38  CYS B SG   1 
ATOM   5193 H H    . CYS B 2 38  ? 4.30300   -11.75600 -6.73600  1.000 37.88799  ? 38  CYS B H    1 
ATOM   5194 H HA   . CYS B 2 38  ? 4.61300   -11.79800 -4.08200  1.000 38.39798  ? 38  CYS B HA   1 
ATOM   5195 H HB2  . CYS B 2 38  ? 5.41600   -13.92800 -3.84000  1.000 40.17970  ? 38  CYS B HB2  1 
ATOM   5196 H HB3  . CYS B 2 38  ? 3.99100   -14.05200 -4.51900  1.000 40.17970  ? 38  CYS B HB3  1 
ATOM   5197 H HG   . CYS B 2 38  ? 6.76500   -14.43000 -6.14300  1.000 44.90237  ? 38  CYS B HG   1 
ATOM   5198 N N    . PRO B 2 39  ? 7.23300   -11.73700 -4.31800  1.000 31.40693  ? 39  PRO B N    1 
ATOM   5199 C CA   . PRO B 2 39  ? 8.58000   -11.24600 -4.61900  1.000 31.19266  ? 39  PRO B CA   1 
ATOM   5200 C C    . PRO B 2 39  ? 9.25100   -12.15600 -5.63600  1.000 35.37808  ? 39  PRO B C    1 
ATOM   5201 O O    . PRO B 2 39  ? 9.07600   -13.37700 -5.59500  1.000 35.68962  ? 39  PRO B O    1 
ATOM   5202 C CB   . PRO B 2 39  ? 9.30200   -11.32100 -3.25700  1.000 30.09815  ? 39  PRO B CB   1 
ATOM   5203 C CG   . PRO B 2 39  ? 8.18400   -11.16800 -2.22500  1.000 28.57072  ? 39  PRO B CG   1 
ATOM   5204 C CD   . PRO B 2 39  ? 7.05400   -11.98400 -2.87100  1.000 32.77972  ? 39  PRO B CD   1 
ATOM   5205 H HA   . PRO B 2 39  ? 8.56000   -10.33100 -4.94200  1.000 37.43199  ? 39  PRO B HA   1 
ATOM   5206 H HB2  . PRO B 2 39  ? 9.74100   -12.18100 -3.16500  1.000 36.11858  ? 39  PRO B HB2  1 
ATOM   5207 H HB3  . PRO B 2 39  ? 9.94300   -10.59700 -3.18300  1.000 36.11858  ? 39  PRO B HB3  1 
ATOM   5208 H HG2  . PRO B 2 39  ? 8.45500   -11.55000 -1.37600  1.000 34.28566  ? 39  PRO B HG2  1 
ATOM   5209 H HG3  . PRO B 2 39  ? 7.93700   -10.23500 -2.13200  1.000 34.28566  ? 39  PRO B HG3  1 
ATOM   5210 H HD2  . PRO B 2 39  ? 7.16400   -12.92700 -2.67400  1.000 39.33647  ? 39  PRO B HD2  1 
ATOM   5211 H HD3  . PRO B 2 39  ? 6.19300   -11.65600 -2.57000  1.000 39.33647  ? 39  PRO B HD3  1 
ATOM   5212 N N    . ARG B 2 40  ? 10.01000  -11.56300 -6.56200  1.000 33.65720  ? 40  ARG B N    1 
ATOM   5213 C CA   . ARG B 2 40  ? 10.61700  -12.41400 -7.59200  1.000 35.82565  ? 40  ARG B CA   1 
ATOM   5214 C C    . ARG B 2 40  ? 11.71000  -13.30700 -7.02300  1.000 42.83088  ? 40  ARG B C    1 
ATOM   5215 O O    . ARG B 2 40  ? 12.05300  -14.32200 -7.64200  1.000 42.42603  ? 40  ARG B O    1 
ATOM   5216 C CB   . ARG B 2 40  ? 11.17300  -11.58500 -8.74400  1.000 39.10222  ? 40  ARG B CB   1 
ATOM   5217 C CG   . ARG B 2 40  ? 12.28500  -10.66300 -8.38500  1.000 39.64403  ? 40  ARG B CG   1 
ATOM   5218 C CD   . ARG B 2 40  ? 12.82100  -9.99200  -9.60800  1.000 42.89563  ? 40  ARG B CD   1 
ATOM   5219 N NE   . ARG B 2 40  ? 13.88300  -9.08300  -9.22800  1.000 38.70921  ? 40  ARG B NE   1 
ATOM   5220 C CZ   . ARG B 2 40  ? 14.64500  -8.41300  -10.07900 1.000 43.21045  ? 40  ARG B CZ   1 
ATOM   5221 N NH1  . ARG B 2 40  ? 14.44000  -8.46600  -11.39400 1.000 44.87446  ? 40  ARG B NH1  1 
ATOM   5222 N NH2  . ARG B 2 40  ? 15.63100  -7.66600  -9.60400  1.000 40.89963  ? 40  ARG B NH2  1 
ATOM   5223 H H    . ARG B 2 40  ? 10.18200  -10.72200 -6.61800  1.000 40.38944  ? 40  ARG B H    1 
ATOM   5224 H HA   . ARG B 2 40  ? 9.92900   -12.99300 -7.95600  1.000 42.99158  ? 40  ARG B HA   1 
ATOM   5225 H HB2  . ARG B 2 40  ? 11.50400  -12.19000 -9.42600  1.000 46.92346  ? 40  ARG B HB2  1 
ATOM   5226 H HB3  . ARG B 2 40  ? 10.45400  -11.04600 -9.11000  1.000 46.92346  ? 40  ARG B HB3  1 
ATOM   5227 H HG2  . ARG B 2 40  ? 11.95700  -9.98000  -7.77900  1.000 47.57364  ? 40  ARG B HG2  1 
ATOM   5228 H HG3  . ARG B 2 40  ? 13.00600  -11.16400 -7.97300  1.000 47.57364  ? 40  ARG B HG3  1 
ATOM   5229 H HD2  . ARG B 2 40  ? 13.18600  -10.65900 -10.21100 1.000 51.47555  ? 40  ARG B HD2  1 
ATOM   5230 H HD3  . ARG B 2 40  ? 12.11600  -9.48800  -10.04400 1.000 51.47555  ? 40  ARG B HD3  1 
ATOM   5231 H HE   . ARG B 2 40  ? 14.02900  -8.97000  -8.38800  1.000 46.45185  ? 40  ARG B HE   1 
ATOM   5232 H HH11 . ARG B 2 40  ? 13.80400  -8.94900  -11.71300 1.000 53.85015  ? 40  ARG B HH11 1 
ATOM   5233 H HH12 . ARG B 2 40  ? 14.94700  -8.01900  -11.92600 1.000 53.85015  ? 40  ARG B HH12 1 
ATOM   5234 H HH21 . ARG B 2 40  ? 15.76800  -7.62400  -8.75600  1.000 49.08036  ? 40  ARG B HH21 1 
ATOM   5235 H HH22 . ARG B 2 40  ? 16.13100  -7.22100  -10.14300 1.000 49.08036  ? 40  ARG B HH22 1 
ATOM   5236 N N    . ALA B 2 41  ? 12.21900  -12.98600 -5.83000  1.000 40.29302  ? 41  ALA B N    1 
ATOM   5237 C CA   . ALA B 2 41  ? 13.18100  -13.84100 -5.15200  1.000 44.92653  ? 41  ALA B CA   1 
ATOM   5238 C C    . ALA B 2 41  ? 12.63200  -15.22500 -4.83200  1.000 47.32724  ? 41  ALA B C    1 
ATOM   5239 O O    . ALA B 2 41  ? 13.41000  -16.08900 -4.41800  1.000 55.24889  ? 41  ALA B O    1 
ATOM   5240 C CB   . ALA B 2 41  ? 13.65100  -13.18800 -3.85100  1.000 52.32048  ? 41  ALA B CB   1 
ATOM   5241 H H    . ALA B 2 41  ? 12.01900  -12.27200 -5.39400  1.000 48.35243  ? 41  ALA B H    1 
ATOM   5242 H HA   . ALA B 2 41  ? 13.95600  -13.95400 -5.72400  1.000 53.91264  ? 41  ALA B HA   1 
ATOM   5243 H HB1  . ALA B 2 41  ? 14.29000  -13.77400 -3.41700  1.000 62.78537  ? 41  ALA B HB1  1 
ATOM   5244 H HB2  . ALA B 2 41  ? 14.06900  -12.33800 -4.05800  1.000 62.78537  ? 41  ALA B HB2  1 
ATOM   5245 H HB3  . ALA B 2 41  ? 12.88400  -13.04800 -3.27300  1.000 62.78537  ? 41  ALA B HB3  1 
ATOM   5246 N N    . VAL B 2 42  ? 11.32800  -15.47400 -4.99200  1.000 43.53072  ? 42  VAL B N    1 
ATOM   5247 C CA   . VAL B 2 42  ? 10.83700  -16.84000 -4.79600  1.000 43.32043  ? 42  VAL B CA   1 
ATOM   5248 C C    . VAL B 2 42  ? 11.44500  -17.81400 -5.81300  1.000 54.75620  ? 42  VAL B C    1 
ATOM   5249 O O    . VAL B 2 42  ? 11.54100  -19.01900 -5.55100  1.000 54.16097  ? 42  VAL B O    1 
ATOM   5250 C CB   . VAL B 2 42  ? 9.29800   -16.90200 -4.85800  1.000 48.21727  ? 42  VAL B CB   1 
ATOM   5251 C CG1  . VAL B 2 42  ? 8.79000   -16.78100 -6.31500  1.000 42.52041  ? 42  VAL B CG1  1 
ATOM   5252 C CG2  . VAL B 2 42  ? 8.78400   -18.17600 -4.17900  1.000 43.99252  ? 42  VAL B CG2  1 
ATOM   5253 H H    . VAL B 2 42  ? 10.72900  -14.89500 -5.20400  1.000 52.23766  ? 42  VAL B H    1 
ATOM   5254 H HA   . VAL B 2 42  ? 11.10500  -17.13800 -3.91300  1.000 51.98532  ? 42  VAL B HA   1 
ATOM   5255 H HB   . VAL B 2 42  ? 8.94200   -16.14600 -4.36700  1.000 57.86152  ? 42  VAL B HB   1 
ATOM   5256 H HG11 . VAL B 2 42  ? 7.84200   -16.57700 -6.30200  1.000 51.02530  ? 42  VAL B HG11 1 
ATOM   5257 H HG12 . VAL B 2 42  ? 9.27500   -16.06900 -6.76000  1.000 51.02530  ? 42  VAL B HG12 1 
ATOM   5258 H HG13 . VAL B 2 42  ? 8.94000   -17.62100 -6.77600  1.000 51.02530  ? 42  VAL B HG13 1 
ATOM   5259 H HG21 . VAL B 2 42  ? 7.81400   -18.16100 -4.17300  1.000 52.79182  ? 42  VAL B HG21 1 
ATOM   5260 H HG22 . VAL B 2 42  ? 9.10000   -18.94700 -4.67500  1.000 52.79182  ? 42  VAL B HG22 1 
ATOM   5261 H HG23 . VAL B 2 42  ? 9.12000   -18.20700 -3.27000  1.000 52.79182  ? 42  VAL B HG23 1 
ATOM   5262 N N    . ILE B 2 43  ? 11.88800  -17.32700 -6.96700  1.000 50.81850  ? 43  ILE B N    1 
ATOM   5263 C CA   . ILE B 2 43  ? 12.44400  -18.27500 -7.93100  1.000 59.22447  ? 43  ILE B CA   1 
ATOM   5264 C C    . ILE B 2 43  ? 13.90100  -18.60600 -7.66400  1.000 59.33720  ? 43  ILE B C    1 
ATOM   5265 O O    . ILE B 2 43  ? 14.39600  -19.60800 -8.19000  1.000 69.82649  ? 43  ILE B O    1 
ATOM   5266 C CB   . ILE B 2 43  ? 12.34400  -17.75700 -9.37800  1.000 60.16541  ? 43  ILE B CB   1 
ATOM   5267 C CG1  . ILE B 2 43  ? 13.29300  -16.58600 -9.60600  1.000 60.88408  ? 43  ILE B CG1  1 
ATOM   5268 C CG2  . ILE B 2 43  ? 10.92800  -17.36300 -9.72400  1.000 58.25285  ? 43  ILE B CG2  1 
ATOM   5269 C CD1  . ILE B 2 43  ? 13.35700  -16.19100 -11.05900 1.000 67.30336  ? 43  ILE B CD1  1 
ATOM   5270 H H    . ILE B 2 43  ? 11.88100  -16.50200 -7.20900  1.000 60.98300  ? 43  ILE B H    1 
ATOM   5271 H HA   . ILE B 2 43  ? 11.94000  -19.10200 -7.88400  1.000 71.07017  ? 43  ILE B HA   1 
ATOM   5272 H HB   . ILE B 2 43  ? 12.60800  -18.47700 -9.97200  1.000 72.19929  ? 43  ILE B HB   1 
ATOM   5273 H HG12 . ILE B 2 43  ? 12.98300  -15.82100 -9.10200  1.000 73.06170  ? 43  ILE B HG12 1 
ATOM   5274 H HG13 . ILE B 2 43  ? 14.19500  -16.81600 -9.33900  1.000 73.06170  ? 43  ILE B HG13 1 
ATOM   5275 H HG21 . ILE B 2 43  ? 10.85800  -17.23500 -10.68300 1.000 69.90423  ? 43  ILE B HG21 1 
ATOM   5276 H HG22 . ILE B 2 43  ? 10.33300  -18.07200 -9.44000  1.000 69.90423  ? 43  ILE B HG22 1 
ATOM   5277 H HG23 . ILE B 2 43  ? 10.70600  -16.54000 -9.26100  1.000 69.90423  ? 43  ILE B HG23 1 
ATOM   5278 H HD11 . ILE B 2 43  ? 14.16600  -15.67900 -11.21200 1.000 80.76483  ? 43  ILE B HD11 1 
ATOM   5279 H HD12 . ILE B 2 43  ? 13.36300  -16.99200 -11.60500 1.000 80.76483  ? 43  ILE B HD12 1 
ATOM   5280 H HD13 . ILE B 2 43  ? 12.57900  -15.65200 -11.26800 1.000 80.76483  ? 43  ILE B HD13 1 
ATOM   5281 N N    . CYS B 2 44  ? 14.56800  -17.84400 -6.79700  1.000 72.58814  ? 44  CYS B N    1 
ATOM   5282 C CA   . CYS B 2 44  ? 15.98000  -18.04000 -6.44500  1.000 76.86189  ? 44  CYS B CA   1 
ATOM   5283 C C    . CYS B 2 44  ? 16.21100  -19.31800 -5.63200  1.000 74.81224  ? 44  CYS B C    1 
ATOM   5284 O O    . CYS B 2 44  ? 16.01200  -19.33500 -4.41600  1.000 71.05726  ? 44  CYS B O    1 
ATOM   5285 C CB   . CYS B 2 44  ? 16.50700  -16.82300 -5.65700  1.000 77.56308  ? 44  CYS B CB   1 
ATOM   5286 S SG   . CYS B 2 44  ? 16.58900  -15.23500 -6.58100  1.000 97.75730  ? 44  CYS B SG   1 
ATOM   5287 H H    . CYS B 2 44  ? 14.21200  -17.18000 -6.38300  1.000 87.10657  ? 44  CYS B H    1 
ATOM   5288 H HA   . CYS B 2 44  ? 16.49800  -18.11100 -7.26200  1.000 92.23507  ? 44  CYS B HA   1 
ATOM   5289 H HB2  . CYS B 2 44  ? 15.92800  -16.68200 -4.89100  1.000 93.07649  ? 44  CYS B HB2  1 
ATOM   5290 H HB3  . CYS B 2 44  ? 17.40500  -17.02500 -5.34900  1.000 93.07649  ? 44  CYS B HB3  1 
ATOM   5291 H HG   . CYS B 2 44  ? 17.01300  -14.38100 -5.85300  1.000 117.30957 ? 44  CYS B HG   1 
ATOM   5292 N N    . PRO B 2 52  ? 24.48800  -12.36700 -7.20900  1.000 91.76194  ? 52  PRO B N    1 
ATOM   5293 C CA   . PRO B 2 52  ? 24.00700  -11.95900 -8.52200  1.000 94.88812  ? 52  PRO B CA   1 
ATOM   5294 C C    . PRO B 2 52  ? 23.11500  -13.02500 -9.10900  1.000 93.54753  ? 52  PRO B C    1 
ATOM   5295 O O    . PRO B 2 52  ? 23.60400  -13.98200 -9.73100  1.000 95.42001  ? 52  PRO B O    1 
ATOM   5296 C CB   . PRO B 2 52  ? 25.25400  -11.74900 -9.38700  1.000 100.77832 ? 52  PRO B CB   1 
ATOM   5297 C CG   . PRO B 2 52  ? 26.40900  -11.98300 -8.43800  1.000 98.86334  ? 52  PRO B CG   1 
ATOM   5298 C CD   . PRO B 2 52  ? 25.83000  -11.85200 -7.04000  1.000 99.07429  ? 52  PRO B CD   1 
ATOM   5299 H HA   . PRO B 2 52  ? 23.51500  -11.12600 -8.45800  1.000 113.86654 ? 52  PRO B HA   1 
ATOM   5300 H HB2  . PRO B 2 52  ? 25.27100  -12.38800 -10.11600 1.000 120.93479 ? 52  PRO B HB2  1 
ATOM   5301 H HB3  . PRO B 2 52  ? 25.26700  -10.84000 -9.72600  1.000 120.93479 ? 52  PRO B HB3  1 
ATOM   5302 H HG2  . PRO B 2 52  ? 26.76800  -12.87400 -8.57600  1.000 118.63681 ? 52  PRO B HG2  1 
ATOM   5303 H HG3  . PRO B 2 52  ? 27.09300  -11.31200 -8.58800  1.000 118.63681 ? 52  PRO B HG3  1 
ATOM   5304 H HD2  . PRO B 2 52  ? 26.32800  -12.39800 -6.41200  1.000 118.88995 ? 52  PRO B HD2  1 
ATOM   5305 H HD3  . PRO B 2 52  ? 25.80600  -10.92200 -6.76700  1.000 118.88995 ? 52  PRO B HD3  1 
ATOM   5306 N N    . ASN B 2 53  ? 21.81500  -12.86000 -8.91300  1.000 88.15193  ? 53  ASN B N    1 
ATOM   5307 C CA   . ASN B 2 53  ? 20.85300  -13.83200 -9.48100  1.000 86.54396  ? 53  ASN B CA   1 
ATOM   5308 C C    . ASN B 2 53  ? 20.35200  -13.25500 -10.80200 1.000 85.84958  ? 53  ASN B C    1 
ATOM   5309 O O    . ASN B 2 53  ? 20.10700  -12.03500 -10.85700 1.000 84.98802  ? 53  ASN B O    1 
ATOM   5310 C CB   . ASN B 2 53  ? 19.75700  -14.13400 -8.47000  1.000 82.33964  ? 53  ASN B CB   1 
ATOM   5311 C CG   . ASN B 2 53  ? 19.84900  -13.20400 -7.28500  1.000 90.21612  ? 53  ASN B CG   1 
ATOM   5312 O OD1  . ASN B 2 53  ? 20.84500  -13.22600 -6.55400  1.000 91.65498  ? 53  ASN B OD1  1 
ATOM   5313 N ND2  . ASN B 2 53  ? 18.84100  -12.36800 -7.09000  1.000 93.84707  ? 53  ASN B ND2  1 
ATOM   5314 H H    . ASN B 2 53  ? 21.47200  -12.18900 -8.50200  1.000 105.78311 ? 53  ASN B H    1 
ATOM   5315 H HA   . ASN B 2 53  ? 21.31400  -14.66300 -9.67400  1.000 103.85355 ? 53  ASN B HA   1 
ATOM   5316 H HB2  . ASN B 2 53  ? 18.89000  -14.01200 -8.88800  1.000 98.80837  ? 53  ASN B HB2  1 
ATOM   5317 H HB3  . ASN B 2 53  ? 19.85400  -15.04500 -8.15200  1.000 98.80837  ? 53  ASN B HB3  1 
ATOM   5318 H HD21 . ASN B 2 53  ? 18.85800  -11.82100 -6.42600  1.000 112.61729 ? 53  ASN B HD21 1 
ATOM   5319 H HD22 . ASN B 2 53  ? 18.16500  -12.37800 -7.62200  1.000 112.61729 ? 53  ASN B HD22 1 
ATOM   5320 N N    . TYR B 2 54  ? 20.26200  -14.09000 -11.83200 1.000 90.18777  ? 54  TYR B N    1 
ATOM   5321 C CA   . TYR B 2 54  ? 19.70100  -13.62600 -13.12800 1.000 94.95085  ? 54  TYR B CA   1 
ATOM   5322 C C    . TYR B 2 54  ? 18.26300  -14.04400 -13.12700 1.000 90.38526  ? 54  TYR B C    1 
ATOM   5323 O O    . TYR B 2 54  ? 17.92000  -15.07100 -13.74200 1.000 87.07354  ? 54  TYR B O    1 
ATOM   5324 C CB   . TYR B 2 54  ? 20.47800  -14.21500 -14.30800 1.000 100.81945 ? 54  TYR B CB   1 
ATOM   5325 C CG   . TYR B 2 54  ? 21.79300  -13.49600 -14.57000 1.000 111.65022 ? 54  TYR B CG   1 
ATOM   5326 C CD1  . TYR B 2 54  ? 22.96300  -13.88100 -13.92800 1.000 111.88153 ? 54  TYR B CD1  1 
ATOM   5327 C CD2  . TYR B 2 54  ? 21.85800  -12.42000 -15.44700 1.000 109.10483 ? 54  TYR B CD2  1 
ATOM   5328 C CE1  . TYR B 2 54  ? 24.16000  -13.22400 -14.15800 1.000 107.32455 ? 54  TYR B CE1  1 
ATOM   5329 C CE2  . TYR B 2 54  ? 23.04800  -11.75500 -15.68500 1.000 110.38186 ? 54  TYR B CE2  1 
ATOM   5330 C CZ   . TYR B 2 54  ? 24.20300  -12.15800 -15.03800 1.000 110.84514 ? 54  TYR B CZ   1 
ATOM   5331 O OH   . TYR B 2 54  ? 25.37600  -11.50100 -15.27100 1.000 109.90154 ? 54  TYR B OH   1 
ATOM   5332 H H    . TYR B 2 54  ? 20.50900  -14.91400 -11.82200 1.000 108.22612 ? 54  TYR B H    1 
ATOM   5333 H HA   . TYR B 2 54  ? 19.74500  -12.65800 -13.17900 1.000 113.94182 ? 54  TYR B HA   1 
ATOM   5334 H HB2  . TYR B 2 54  ? 20.67000  -15.15000 -14.13300 1.000 120.98415 ? 54  TYR B HB2  1 
ATOM   5335 H HB3  . TYR B 2 54  ? 19.93700  -14.12500 -15.10600 1.000 120.98415 ? 54  TYR B HB3  1 
ATOM   5336 H HD1  . TYR B 2 54  ? 22.94300  -14.59700 -13.33500 1.000 134.25864 ? 54  TYR B HD1  1 
ATOM   5337 H HD2  . TYR B 2 54  ? 21.08600  -12.14300 -15.88600 1.000 130.92660 ? 54  TYR B HD2  1 
ATOM   5338 H HE1  . TYR B 2 54  ? 24.93300  -13.49800 -13.72000 1.000 128.79026 ? 54  TYR B HE1  1 
ATOM   5339 H HE2  . TYR B 2 54  ? 23.07100  -11.03900 -16.27800 1.000 132.45903 ? 54  TYR B HE2  1 
ATOM   5340 H HH   . TYR B 2 54  ? 25.25300  -10.88000 -15.82300 1.000 131.88265 ? 54  TYR B HH   1 
ATOM   5341 N N    . GLU B 2 55  ? 17.43200  -13.28900 -12.40900 1.000 79.45742  ? 55  GLU B N    1 
ATOM   5342 C CA   . GLU B 2 55  ? 16.04500  -13.74000 -12.28500 1.000 74.33346  ? 55  GLU B CA   1 
ATOM   5343 C C    . GLU B 2 55  ? 15.42300  -14.02900 -13.64800 1.000 75.39413  ? 55  GLU B C    1 
ATOM   5344 O O    . GLU B 2 55  ? 14.72700  -15.03800 -13.81100 1.000 75.60498  ? 55  GLU B O    1 
ATOM   5345 C CB   . GLU B 2 55  ? 15.16700  -12.75600 -11.48600 1.000 62.41774  ? 55  GLU B CB   1 
ATOM   5346 C CG   . GLU B 2 55  ? 15.12400  -12.96600 -9.93700  1.000 56.53774  ? 55  GLU B CG   1 
ATOM   5347 C CD   . GLU B 2 55  ? 16.08800  -12.11500 -9.16400  1.000 57.95702  ? 55  GLU B CD   1 
ATOM   5348 O OE1  . GLU B 2 55  ? 16.63700  -11.19400 -9.78300  1.000 60.44673  ? 55  GLU B OE1  1 
ATOM   5349 O OE2  . GLU B 2 55  ? 16.25900  -12.32700 -7.93800  1.000 58.65644  ? 55  GLU B OE2  1 
ATOM   5350 H H    . GLU B 2 55  ? 17.62900  -12.55500 -12.00600 1.000 95.34970  ? 55  GLU B H    1 
ATOM   5351 H HA   . GLU B 2 55  ? 16.05000  -14.57700 -11.79500 1.000 89.20095  ? 55  GLU B HA   1 
ATOM   5352 H HB2  . GLU B 2 55  ? 15.48200  -11.85600 -11.65900 1.000 74.90209  ? 55  GLU B HB2  1 
ATOM   5353 H HB3  . GLU B 2 55  ? 14.25600  -12.83900 -11.80800 1.000 74.90209  ? 55  GLU B HB3  1 
ATOM   5354 H HG2  . GLU B 2 55  ? 14.23100  -12.75800 -9.62100  1.000 67.84608  ? 55  GLU B HG2  1 
ATOM   5355 H HG3  . GLU B 2 55  ? 15.33000  -13.89400 -9.74300  1.000 67.84608  ? 55  GLU B HG3  1 
ATOM   5356 N N    . ASP B 2 56  ? 15.68100  -13.18500 -14.65000 1.000 78.29991  ? 56  ASP B N    1 
ATOM   5357 C CA   . ASP B 2 56  ? 15.08800  -13.43400 -15.96300 1.000 82.48467  ? 56  ASP B CA   1 
ATOM   5358 C C    . ASP B 2 56  ? 15.47700  -14.80100 -16.50500 1.000 85.88561  ? 56  ASP B C    1 
ATOM   5359 O O    . ASP B 2 56  ? 14.62400  -15.53500 -17.02200 1.000 87.34362  ? 56  ASP B O    1 
ATOM   5360 C CB   . ASP B 2 56  ? 15.49400  -12.34400 -16.94700 1.000 81.98528  ? 56  ASP B CB   1 
ATOM   5361 C CG   . ASP B 2 56  ? 14.82800  -12.51500 -18.29100 1.000 87.25064  ? 56  ASP B CG   1 
ATOM   5362 O OD1  . ASP B 2 56  ? 13.58700  -12.33600 -18.37500 1.000 86.40780  ? 56  ASP B OD1  1 
ATOM   5363 O OD2  . ASP B 2 56  ? 15.55800  -12.80100 -19.26600 1.000 88.66654  ? 56  ASP B OD2  1 
ATOM   5364 H H    . ASP B 2 56  ? 16.17800  -12.48500 -14.59900 1.000 93.96069  ? 56  ASP B H    1 
ATOM   5365 H HA   . ASP B 2 56  ? 14.12200  -13.41300 -15.87900 1.000 98.98240  ? 56  ASP B HA   1 
ATOM   5366 H HB2  . ASP B 2 56  ? 15.23500  -11.48000 -16.58900 1.000 98.38314  ? 56  ASP B HB2  1 
ATOM   5367 H HB3  . ASP B 2 56  ? 16.45400  -12.37700 -17.07900 1.000 98.38314  ? 56  ASP B HB3  1 
ATOM   5368 N N    . LEU B 2 57  ? 16.76500  -15.11700 -16.36000 1.000 86.21696  ? 57  LEU B N    1 
ATOM   5369 C CA   . LEU B 2 57  ? 17.27800  -16.41000 -16.87000 1.000 87.56819  ? 57  LEU B CA   1 
ATOM   5370 C C    . LEU B 2 57  ? 16.71600  -17.54000 -16.01400 1.000 86.23089  ? 57  LEU B C    1 
ATOM   5371 O O    . LEU B 2 57  ? 16.57000  -18.65100 -16.53600 1.000 90.03804  ? 57  LEU B O    1 
ATOM   5372 C CB   . LEU B 2 57  ? 18.80600  -16.37800 -16.82800 1.000 84.69548  ? 57  LEU B CB   1 
ATOM   5373 C CG   . LEU B 2 57  ? 19.49400  -16.14800 -18.17000 1.000 77.67005  ? 57  LEU B CG   1 
ATOM   5374 C CD1  . LEU B 2 57  ? 20.93600  -16.61900 -18.11200 1.000 80.79323  ? 57  LEU B CD1  1 
ATOM   5375 C CD2  . LEU B 2 57  ? 18.74600  -16.85700 -19.28600 1.000 76.72355  ? 57  LEU B CD2  1 
ATOM   5376 H H    . LEU B 2 57  ? 17.35400  -14.61800 -15.98000 1.000 103.46115 ? 57  LEU B H    1 
ATOM   5377 H HA   . LEU B 2 57  ? 16.93900  -16.53300 -17.76400 1.000 105.08263 ? 57  LEU B HA   1 
ATOM   5378 H HB2  . LEU B 2 57  ? 19.08400  -15.66900 -16.23300 1.000 101.63538 ? 57  LEU B HB2  1 
ATOM   5379 H HB3  . LEU B 2 57  ? 19.12000  -17.22900 -16.48400 1.000 101.63538 ? 57  LEU B HB3  1 
ATOM   5380 H HG   . LEU B 2 57  ? 19.49600  -15.19800 -18.36600 1.000 93.20486  ? 57  LEU B HG   1 
ATOM   5381 H HD11 . LEU B 2 57  ? 21.14100  -16.15800 -18.92500 1.000 96.95268  ? 57  LEU B HD11 1 
ATOM   5382 H HD12 . LEU B 2 57  ? 21.37200  -16.22600 -17.33900 1.000 96.95268  ? 57  LEU B HD12 1 
ATOM   5383 H HD13 . LEU B 2 57  ? 20.91900  -17.58800 -18.07200 1.000 96.95268  ? 57  LEU B HD13 1 
ATOM   5384 H HD21 . LEU B 2 57  ? 19.35900  -17.01800 -20.02000 1.000 92.06906  ? 57  LEU B HD21 1 
ATOM   5385 H HD22 . LEU B 2 57  ? 18.40400  -17.70300 -18.95500 1.000 92.06906  ? 57  LEU B HD22 1 
ATOM   5386 H HD23 . LEU B 2 57  ? 18.01600  -16.29500 -19.58900 1.000 92.06906  ? 57  LEU B HD23 1 
ATOM   5387 N N    . LEU B 2 58  ? 16.36300  -17.24800 -14.76700 1.000 80.75874  ? 58  LEU B N    1 
ATOM   5388 C CA   . LEU B 2 58  ? 15.91600  -18.34400 -13.87500 1.000 81.24646  ? 58  LEU B CA   1 
ATOM   5389 C C    . LEU B 2 58  ? 14.45000  -18.70600 -14.14500 1.000 85.10787  ? 58  LEU B C    1 
ATOM   5390 O O    . LEU B 2 58  ? 14.08400  -19.83500 -13.79100 1.000 84.90344  ? 58  LEU B O    1 
ATOM   5391 C CB   . LEU B 2 58  ? 16.17200  -17.96200 -12.41600 1.000 79.32307  ? 58  LEU B CB   1 
ATOM   5392 C CG   . LEU B 2 58  ? 17.50400  -18.41900 -11.82900 1.000 85.28566  ? 58  LEU B CG   1 
ATOM   5393 C CD1  . LEU B 2 58  ? 17.93500  -17.49300 -10.70300 1.000 79.22467  ? 58  LEU B CD1  1 
ATOM   5394 C CD2  . LEU B 2 58  ? 17.40600  -19.85200 -11.33000 1.000 84.82349  ? 58  LEU B CD2  1 
ATOM   5395 H H    . LEU B 2 58  ? 16.36800  -16.46400 -14.41300 1.000 96.91129  ? 58  LEU B H    1 
ATOM   5396 H HA   . LEU B 2 58  ? 16.44900  -19.13200 -14.06600 1.000 97.49655  ? 58  LEU B HA   1 
ATOM   5397 H HB2  . LEU B 2 58  ? 16.14000  -16.99500 -12.34300 1.000 95.18848  ? 58  LEU B HB2  1 
ATOM   5398 H HB3  . LEU B 2 58  ? 15.46800  -18.34900 -11.87200 1.000 95.18848  ? 58  LEU B HB3  1 
ATOM   5399 H HG   . LEU B 2 58  ? 18.18300  -18.38700 -12.52100 1.000 102.34359 ? 58  LEU B HG   1 
ATOM   5400 H HD11 . LEU B 2 58  ? 18.77200  -17.81500 -10.33300 1.000 95.07040  ? 58  LEU B HD11 1 
ATOM   5401 H HD12 . LEU B 2 58  ? 18.05300  -16.59800 -11.05800 1.000 95.07040  ? 58  LEU B HD12 1 
ATOM   5402 H HD13 . LEU B 2 58  ? 17.24900  -17.49000 -10.01700 1.000 95.07040  ? 58  LEU B HD13 1 
ATOM   5403 H HD21 . LEU B 2 58  ? 18.26700  -20.12200 -10.97500 1.000 101.78899 ? 58  LEU B HD21 1 
ATOM   5404 H HD22 . LEU B 2 58  ? 16.73200  -19.89800 -10.63400 1.000 101.78899 ? 58  LEU B HD22 1 
ATOM   5405 H HD23 . LEU B 2 58  ? 17.15800  -20.42700 -12.07000 1.000 101.78899 ? 58  LEU B HD23 1 
ATOM   5406 N N    . ILE B 2 59  ? 13.65000  -17.83400 -14.77700 1.000 87.11246  ? 59  ILE B N    1 
ATOM   5407 C CA   . ILE B 2 59  ? 12.19800  -18.16600 -14.95700 1.000 88.64084  ? 59  ILE B CA   1 
ATOM   5408 C C    . ILE B 2 59  ? 12.00200  -19.05500 -16.18300 1.000 87.63997  ? 59  ILE B C    1 
ATOM   5409 O O    . ILE B 2 59  ? 10.96600  -18.90100 -16.84500 1.000 85.30778  ? 59  ILE B O    1 
ATOM   5410 C CB   . ILE B 2 59  ? 11.24200  -16.95300 -14.98500 1.000 86.41280  ? 59  ILE B CB   1 
ATOM   5411 C CG1  . ILE B 2 59  ? 11.16400  -16.19900 -13.65900 1.000 83.68488  ? 59  ILE B CG1  1 
ATOM   5412 C CG2  . ILE B 2 59  ? 9.86200   -17.35500 -15.48700 1.000 85.94840  ? 59  ILE B CG2  1 
ATOM   5413 C CD1  . ILE B 2 59  ? 10.44500  -14.88200 -13.76600 1.000 79.18706  ? 59  ILE B CD1  1 
ATOM   5414 H H    . ILE B 2 59  ? 13.89500  -17.07600 -15.10100 1.000 104.53575 ? 59  ILE B H    1 
ATOM   5415 H HA   . ILE B 2 59  ? 11.93100  -18.69800 -14.19200 1.000 106.36981 ? 59  ILE B HA   1 
ATOM   5416 H HB   . ILE B 2 59  ? 11.60400  -16.33100 -15.63600 1.000 103.69616 ? 59  ILE B HB   1 
ATOM   5417 H HG12 . ILE B 2 59  ? 10.69900  -16.74600 -13.00700 1.000 100.42265 ? 59  ILE B HG12 1 
ATOM   5418 H HG13 . ILE B 2 59  ? 12.06700  -16.01700 -13.36100 1.000 100.42265 ? 59  ILE B HG13 1 
ATOM   5419 H HG21 . ILE B 2 59  ? 9.24400   -16.78600 -15.01200 1.000 103.13888 ? 59  ILE B HG21 1 
ATOM   5420 H HG22 . ILE B 2 59  ? 9.77700   -17.18200 -16.43800 1.000 103.13888 ? 59  ILE B HG22 1 
ATOM   5421 H HG23 . ILE B 2 59  ? 9.66700   -18.27600 -15.25400 1.000 103.13888 ? 59  ILE B HG23 1 
ATOM   5422 H HD11 . ILE B 2 59  ? 10.73500  -14.30600 -13.04100 1.000 95.02528  ? 59  ILE B HD11 1 
ATOM   5423 H HD12 . ILE B 2 59  ? 10.66000  -14.47400 -14.61900 1.000 95.02528  ? 59  ILE B HD12 1 
ATOM   5424 H HD13 . ILE B 2 59  ? 9.48900   -15.03400 -13.70500 1.000 95.02528  ? 59  ILE B HD13 1 
ATOM   5425 N N    . ARG B 2 60  ? 12.93800  -19.96800 -16.45000 1.000 94.01096  ? 60  ARG B N    1 
ATOM   5426 C CA   . ARG B 2 60  ? 12.78700  -20.94800 -17.55900 1.000 93.69478  ? 60  ARG B CA   1 
ATOM   5427 C C    . ARG B 2 60  ? 12.04800  -22.14900 -16.98100 1.000 94.76704  ? 60  ARG B C    1 
ATOM   5428 O O    . ARG B 2 60  ? 12.05500  -23.21500 -17.61400 1.000 98.16452  ? 60  ARG B O    1 
ATOM   5429 C CB   . ARG B 2 60  ? 14.16100  -21.35400 -18.08200 1.000 99.96997  ? 60  ARG B CB   1 
ATOM   5430 C CG   . ARG B 2 60  ? 14.50400  -20.75100 -19.43700 1.000 116.16931 ? 60  ARG B CG   1 
ATOM   5431 C CD   . ARG B 2 60  ? 15.02800  -19.32600 -19.38100 1.000 118.38282 ? 60  ARG B CD   1 
ATOM   5432 N NE   . ARG B 2 60  ? 13.97100  -18.33100 -19.28200 1.000 114.69520 ? 60  ARG B NE   1 
ATOM   5433 C CZ   . ARG B 2 60  ? 14.07900  -17.06800 -19.67200 1.000 113.58078 ? 60  ARG B CZ   1 
ATOM   5434 N NH1  . ARG B 2 60  ? 15.21400  -16.62400 -20.18400 1.000 110.34696 ? 60  ARG B NH1  1 
ATOM   5435 N NH2  . ARG B 2 60  ? 13.05300  -16.24800 -19.53200 1.000 109.94338 ? 60  ARG B NH2  1 
ATOM   5436 H H    . ARG B 2 60  ? 13.67200  -20.05400 -16.01300 1.000 112.81395 ? 60  ARG B H    1 
ATOM   5437 H HA   . ARG B 2 60  ? 12.26400  -20.56400 -18.28000 1.000 112.43454 ? 60  ARG B HA   1 
ATOM   5438 H HB2  . ARG B 2 60  ? 14.83600  -21.06300 -17.44900 1.000 119.96476 ? 60  ARG B HB2  1 
ATOM   5439 H HB3  . ARG B 2 60  ? 14.19300  -22.31900 -18.17200 1.000 119.96476 ? 60  ARG B HB3  1 
ATOM   5440 H HG2  . ARG B 2 60  ? 15.18800  -21.29800 -19.85400 1.000 139.40397 ? 60  ARG B HG2  1 
ATOM   5441 H HG3  . ARG B 2 60  ? 13.70700  -20.75000 -19.99000 1.000 139.40397 ? 60  ARG B HG3  1 
ATOM   5442 H HD2  . ARG B 2 60  ? 15.60400  -19.23100 -18.60800 1.000 142.06018 ? 60  ARG B HD2  1 
ATOM   5443 H HD3  . ARG B 2 60  ? 15.53100  -19.15300 -20.19100 1.000 142.06018 ? 60  ARG B HD3  1 
ATOM   5444 H HE   . ARG B 2 60  ? 13.22000  -18.58100 -18.94500 1.000 137.63504 ? 60  ARG B HE   1 
ATOM   5445 H HH11 . ARG B 2 60  ? 15.88600  -17.15100 -20.27500 1.000 132.41716 ? 60  ARG B HH11 1 
ATOM   5446 H HH12 . ARG B 2 60  ? 15.27800  -15.80300 -20.43300 1.000 132.41716 ? 60  ARG B HH12 1 
ATOM   5447 H HH21 . ARG B 2 60  ? 12.31500  -16.53600 -19.19700 1.000 131.93286 ? 60  ARG B HH21 1 
ATOM   5448 H HH22 . ARG B 2 60  ? 13.12100  -15.42800 -19.78200 1.000 131.93286 ? 60  ARG B HH22 1 
ATOM   5449 N N    . LYS B 2 61  ? 11.44200  -21.96300 -15.80800 1.000 83.39375  ? 61  LYS B N    1 
ATOM   5450 C CA   . LYS B 2 61  ? 10.65700  -23.03800 -15.16800 1.000 74.87624  ? 61  LYS B CA   1 
ATOM   5451 C C    . LYS B 2 61  ? 9.29200   -23.10900 -15.83000 1.000 70.69081  ? 61  LYS B C    1 
ATOM   5452 O O    . LYS B 2 61  ? 8.92000   -22.18200 -16.55300 1.000 70.52484  ? 61  LYS B O    1 
ATOM   5453 C CB   . LYS B 2 61  ? 10.38700  -22.71000 -13.70100 1.000 73.32835  ? 61  LYS B CB   1 
ATOM   5454 C CG   . LYS B 2 61  ? 11.35500  -21.73800 -13.04500 1.000 78.26489  ? 61  LYS B CG   1 
ATOM   5455 C CD   . LYS B 2 61  ? 12.09500  -22.35800 -11.88200 1.000 75.37565  ? 61  LYS B CD   1 
ATOM   5456 C CE   . LYS B 2 61  ? 12.89700  -21.35300 -11.08500 1.000 83.91478  ? 61  LYS B CE   1 
ATOM   5457 N NZ   . LYS B 2 61  ? 14.13300  -21.95400 -10.52900 1.000 81.13160  ? 61  LYS B NZ   1 
ATOM   5458 H H    . LYS B 2 61  ? 11.42900  -21.22400 -15.38300 1.000 100.07331 ? 61  LYS B H    1 
ATOM   5459 H HA   . LYS B 2 61  ? 11.10800  -23.89300 -15.24200 1.000 89.85229  ? 61  LYS B HA   1 
ATOM   5460 H HB2  . LYS B 2 61  ? 9.49800   -22.32900 -13.63000 1.000 87.99483  ? 61  LYS B HB2  1 
ATOM   5461 H HB3  . LYS B 2 61  ? 10.42700  -23.53600 -13.19700 1.000 87.99483  ? 61  LYS B HB3  1 
ATOM   5462 H HG2  . LYS B 2 61  ? 12.04000  -21.43700 -13.65500 1.000 93.91866  ? 61  LYS B HG2  1 
ATOM   5463 H HG3  . LYS B 2 61  ? 10.85600  -20.97700 -12.70900 1.000 93.91866  ? 61  LYS B HG3  1 
ATOM   5464 H HD2  . LYS B 2 61  ? 11.49900  -22.79800 -11.27400 1.000 90.45158  ? 61  LYS B HD2  1 
ATOM   5465 H HD3  . LYS B 2 61  ? 12.72300  -23.00700 -12.23700 1.000 90.45158  ? 61  LYS B HD3  1 
ATOM   5466 H HE2  . LYS B 2 61  ? 13.15100  -20.61600 -11.66200 1.000 100.69854 ? 61  LYS B HE2  1 
ATOM   5467 H HE3  . LYS B 2 61  ? 12.35900  -21.02900 -10.34600 1.000 100.69854 ? 61  LYS B HE3  1 
ATOM   5468 H HZ1  . LYS B 2 61  ? 14.58600  -21.34400 -10.06600 1.000 97.35872  ? 61  LYS B HZ1  1 
ATOM   5469 H HZ2  . LYS B 2 61  ? 13.92600  -22.63100 -9.99000  1.000 97.35872  ? 61  LYS B HZ2  1 
ATOM   5470 H HZ3  . LYS B 2 61  ? 14.64800  -22.25600 -11.18900 1.000 97.35872  ? 61  LYS B HZ3  1 
ATOM   5471 N N    . SER B 2 62  ? 8.58500   -24.19600 -15.57000 1.000 65.90023  ? 62  SER B N    1 
ATOM   5472 C CA   . SER B 2 62  ? 7.24600   -24.34300 -16.10800 1.000 61.35961  ? 62  SER B CA   1 
ATOM   5473 C C    . SER B 2 62  ? 6.24800   -23.80400 -15.08900 1.000 59.30317  ? 62  SER B C    1 
ATOM   5474 O O    . SER B 2 62  ? 6.58900   -23.53500 -13.93100 1.000 58.16319  ? 62  SER B O    1 
ATOM   5475 C CB   . SER B 2 62  ? 6.94300   -25.80800 -16.46600 1.000 58.80893  ? 62  SER B CB   1 
ATOM   5476 O OG   . SER B 2 62  ? 6.53200   -26.55600 -15.32800 1.000 56.24180  ? 62  SER B OG   1 
ATOM   5477 H H    . SER B 2 62  ? 8.85400   -24.85700 -15.09000 1.000 79.08108  ? 62  SER B H    1 
ATOM   5478 H HA   . SER B 2 62  ? 7.16600   -23.81400 -16.91700 1.000 73.63234  ? 62  SER B HA   1 
ATOM   5479 H HB2  . SER B 2 62  ? 6.23300   -25.82800 -17.12600 1.000 70.57152  ? 62  SER B HB2  1 
ATOM   5480 H HB3  . SER B 2 62  ? 7.74500   -26.21200 -16.83300 1.000 70.57152  ? 62  SER B HB3  1 
ATOM   5481 H HG   . SER B 2 62  ? 7.13800   -26.55100 -14.74700 1.000 67.49096  ? 62  SER B HG   1 
ATOM   5482 N N    . ASN B 2 63  ? 5.02100   -23.56900 -15.56100 1.000 56.23954  ? 63  ASN B N    1 
ATOM   5483 C CA   . ASN B 2 63  ? 3.95600   -23.13800 -14.66200 1.000 55.70131  ? 63  ASN B CA   1 
ATOM   5484 C C    . ASN B 2 63  ? 3.82500   -24.06300 -13.44900 1.000 54.79104  ? 63  ASN B C    1 
ATOM   5485 O O    . ASN B 2 63  ? 3.53200   -23.60000 -12.34000 1.000 53.20337  ? 63  ASN B O    1 
ATOM   5486 C CB   . ASN B 2 63  ? 2.63500   -23.05500 -15.43600 1.000 53.32793  ? 63  ASN B CB   1 
ATOM   5487 C CG   . ASN B 2 63  ? 2.60700   -21.88800 -16.42800 1.000 52.58544  ? 63  ASN B CG   1 
ATOM   5488 O OD1  . ASN B 2 63  ? 3.12500   -20.80100 -16.15100 1.000 54.23700  ? 63  ASN B OD1  1 
ATOM   5489 N ND2  . ASN B 2 63  ? 2.00500   -22.11000 -17.57400 1.000 50.26339  ? 63  ASN B ND2  1 
ATOM   5490 H H    . ASN B 2 63  ? 4.78500   -23.65100 -16.38400 1.000 67.48824  ? 63  ASN B H    1 
ATOM   5491 H HA   . ASN B 2 63  ? 4.16400   -22.24900 -14.33500 1.000 66.84237  ? 63  ASN B HA   1 
ATOM   5492 H HB2  . ASN B 2 63  ? 2.50700   -23.87700 -15.93400 1.000 63.99431  ? 63  ASN B HB2  1 
ATOM   5493 H HB3  . ASN B 2 63  ? 1.90900   -22.93100 -14.80600 1.000 63.99431  ? 63  ASN B HB3  1 
ATOM   5494 H HD21 . ASN B 2 63  ? 1.96200   -21.48700 -18.16500 1.000 60.31687  ? 63  ASN B HD21 1 
ATOM   5495 H HD22 . ASN B 2 63  ? 1.65500   -22.87900 -17.73400 1.000 60.31687  ? 63  ASN B HD22 1 
ATOM   5496 N N    . HIS B 2 64  ? 4.02900   -25.37500 -13.63600 1.000 57.48385  ? 64  HIS B N    1 
ATOM   5497 C CA   . HIS B 2 64  ? 3.87700   -26.32500 -12.53300 1.000 58.79031  ? 64  HIS B CA   1 
ATOM   5498 C C    . HIS B 2 64  ? 5.01000   -26.24700 -11.51400 1.000 55.35464  ? 64  HIS B C    1 
ATOM   5499 O O    . HIS B 2 64  ? 4.87900   -26.83500 -10.43300 1.000 55.75513  ? 64  HIS B O    1 
ATOM   5500 C CB   . HIS B 2 64  ? 3.79200   -27.76900 -13.04200 1.000 56.73869  ? 64  HIS B CB   1 
ATOM   5501 C CG   . HIS B 2 64  ? 2.45200   -28.15000 -13.60400 1.000 61.29662  ? 64  HIS B CG   1 
ATOM   5502 N ND1  . HIS B 2 64  ? 1.37100   -28.46300 -12.80700 1.000 61.09981  ? 64  HIS B ND1  1 
ATOM   5503 C CD2  . HIS B 2 64  ? 2.03300   -28.31100 -14.88500 1.000 63.78934  ? 64  HIS B CD2  1 
ATOM   5504 C CE1  . HIS B 2 64  ? 0.33600   -28.76900 -13.57200 1.000 64.18900  ? 64  HIS B CE1  1 
ATOM   5505 N NE2  . HIS B 2 64  ? 0.71300   -28.69200 -14.83700 1.000 66.77169  ? 64  HIS B NE2  1 
ATOM   5506 H H    . HIS B 2 64  ? 4.25400   -25.73300 -14.38500 1.000 68.98143  ? 64  HIS B H    1 
ATOM   5507 H HA   . HIS B 2 64  ? 3.04900   -26.12800 -12.06700 1.000 70.54917  ? 64  HIS B HA   1 
ATOM   5508 H HB2  . HIS B 2 64  ? 4.45100   -27.89000 -13.74300 1.000 68.08722  ? 64  HIS B HB2  1 
ATOM   5509 H HB3  . HIS B 2 64  ? 3.98400   -28.37000 -12.30500 1.000 68.08722  ? 64  HIS B HB3  1 
ATOM   5510 H HD2  . HIS B 2 64  ? 2.53000   -28.16700 -15.64400 1.000 76.54801  ? 64  HIS B HD2  1 
ATOM   5511 H HE1  . HIS B 2 64  ? -0.50900  -29.01400 -13.27100 1.000 77.02760  ? 64  HIS B HE1  1 
ATOM   5512 H HE2  . HIS B 2 64  ? 0.21100   -28.84500 -15.51900 1.000 80.12683  ? 64  HIS B HE2  1 
ATOM   5513 N N    A ASN B 2 65  ? 6.11500   -25.55500 -11.82400 0.740 54.13759  ? 65  ASN B N    1 
ATOM   5514 N N    B ASN B 2 65  ? 6.09900   -25.54400 -11.82800 0.260 53.98350  ? 65  ASN B N    1 
ATOM   5515 C CA   A ASN B 2 65  ? 7.16500   -25.33100 -10.82600 0.740 52.04665  ? 65  ASN B CA   1 
ATOM   5516 C CA   B ASN B 2 65  ? 7.17700   -25.33000 -10.86900 0.260 52.23691  ? 65  ASN B CA   1 
ATOM   5517 C C    A ASN B 2 65  ? 6.71500   -24.43300 -9.68300  0.740 55.61019  ? 65  ASN B C    1 
ATOM   5518 C C    B ASN B 2 65  ? 6.79000   -24.36700 -9.74600  0.260 55.58908  ? 65  ASN B C    1 
ATOM   5519 O O    A ASN B 2 65  ? 7.31400   -24.46900 -8.60100  0.740 53.13271  ? 65  ASN B O    1 
ATOM   5520 O O    B ASN B 2 65  ? 7.48600   -24.32100 -8.72500  0.260 53.49836  ? 65  ASN B O    1 
ATOM   5521 C CB   A ASN B 2 65  ? 8.39500   -24.72100 -11.47700 0.740 56.03607  ? 65  ASN B CB   1 
ATOM   5522 C CB   B ASN B 2 65  ? 8.42000   -24.83800 -11.61700 0.260 56.42541  ? 65  ASN B CB   1 
ATOM   5523 C CG   A ASN B 2 65  ? 9.11400   -25.70300 -12.33000 0.740 57.63911  ? 65  ASN B CG   1 
ATOM   5524 C CG   B ASN B 2 65  ? 9.32400   -23.99300 -10.76200 0.260 57.93667  ? 65  ASN B CG   1 
ATOM   5525 O OD1  A ASN B 2 65  ? 9.06800   -25.62700 -13.55500 0.740 56.37020  ? 65  ASN B OD1  1 
ATOM   5526 O OD1  B ASN B 2 65  ? 9.41800   -22.78400 -10.95900 0.260 59.89224  ? 65  ASN B OD1  1 
ATOM   5527 N ND2  A ASN B 2 65  ? 9.75200   -26.66600 -11.69500 0.740 57.03390  ? 65  ASN B ND2  1 
ATOM   5528 N ND2  B ASN B 2 65  ? 9.99600   -24.61800 -9.79900  0.260 57.71791  ? 65  ASN B ND2  1 
ATOM   5529 H H    A ASN B 2 65  ? 6.27800   -25.21000 -12.59500 0.740 64.96591  ? 65  ASN B H    1 
ATOM   5530 H H    B ASN B 2 65  ? 6.23600   -25.18000 -12.59500 0.260 64.78100  ? 65  ASN B H    1 
ATOM   5531 H HA   A ASN B 2 65  ? 7.42300   -26.18600 -10.44700 0.740 62.45678  ? 65  ASN B HA   1 
ATOM   5532 H HA   B ASN B 2 65  ? 7.39900   -26.18100 -10.46000 0.260 62.68510  ? 65  ASN B HA   1 
ATOM   5533 H HB2  A ASN B 2 65  ? 8.12500   -23.97500 -12.03500 0.740 67.24408  ? 65  ASN B HB2  1 
ATOM   5534 H HB2  B ASN B 2 65  ? 8.92900   -25.60600 -11.92100 0.260 67.71129  ? 65  ASN B HB2  1 
ATOM   5535 H HB3  A ASN B 2 65  ? 9.00400   -24.41800 -10.78600 0.740 67.24408  ? 65  ASN B HB3  1 
ATOM   5536 H HB3  B ASN B 2 65  ? 8.14500   -24.30200 -12.37500 0.260 67.71129  ? 65  ASN B HB3  1 
ATOM   5537 H HD21 A ASN B 2 65  ? 10.18200  -27.26300 -12.14000 0.740 68.44149  ? 65  ASN B HD21 1 
ATOM   5538 H HD21 B ASN B 2 65  ? 10.52400  -24.17400 -9.28600  0.260 69.26230  ? 65  ASN B HD21 1 
ATOM   5539 H HD22 A ASN B 2 65  ? 9.75300   -26.68700 -10.83500 0.740 68.44149  ? 65  ASN B HD22 1 
ATOM   5540 H HD22 B ASN B 2 65  ? 9.90400   -25.46600 -9.69100  0.260 69.26230  ? 65  ASN B HD22 1 
ATOM   5541 N N    . PHE B 2 66  ? 5.69000   -23.62200 -9.89000  1.000 52.29306  ? 66  PHE B N    1 
ATOM   5542 C CA   . PHE B 2 66  ? 5.19600   -22.73000 -8.84500  1.000 50.33633  ? 66  PHE B CA   1 
ATOM   5543 C C    . PHE B 2 66  ? 3.99100   -23.38700 -8.19900  1.000 52.75452  ? 66  PHE B C    1 
ATOM   5544 O O    . PHE B 2 66  ? 2.94200   -23.51400 -8.83600  1.000 55.23481  ? 66  PHE B O    1 
ATOM   5545 C CB   . PHE B 2 66  ? 4.80800   -21.36900 -9.41200  1.000 47.14860  ? 66  PHE B CB   1 
ATOM   5546 C CG   . PHE B 2 66  ? 5.93400   -20.63000 -10.05100 1.000 48.70354  ? 66  PHE B CG   1 
ATOM   5547 C CD1  . PHE B 2 66  ? 6.78900   -19.85600 -9.29000  1.000 51.91078  ? 66  PHE B CD1  1 
ATOM   5548 C CD2  . PHE B 2 66  ? 6.13200   -20.70300 -11.42200 1.000 51.81537  ? 66  PHE B CD2  1 
ATOM   5549 C CE1  . PHE B 2 66  ? 7.83000   -19.16700 -9.89200  1.000 51.81726  ? 66  PHE B CE1  1 
ATOM   5550 C CE2  . PHE B 2 66  ? 7.16700   -20.01500 -12.03100 1.000 53.51047  ? 66  PHE B CE2  1 
ATOM   5551 C CZ   . PHE B 2 66  ? 8.01400   -19.24200 -11.26700 1.000 56.18373  ? 66  PHE B CZ   1 
ATOM   5552 H H    A PHE B 2 66  ? 5.25800   -23.56600 -10.63100 0.740 62.75247  ? 66  PHE B H    1 
ATOM   5553 H H    B PHE B 2 66  ? 5.20500   -23.61800 -10.60000 0.260 62.75247  ? 66  PHE B H    1 
ATOM   5554 H HA   . PHE B 2 66  ? 5.87800   -22.59800 -8.16900  1.000 60.40440  ? 66  PHE B HA   1 
ATOM   5555 H HB2  . PHE B 2 66  ? 4.12000   -21.49600 -10.08300 1.000 56.57912  ? 66  PHE B HB2  1 
ATOM   5556 H HB3  . PHE B 2 66  ? 4.46500   -20.81800 -8.69100  1.000 56.57912  ? 66  PHE B HB3  1 
ATOM   5557 H HD1  . PHE B 2 66  ? 6.66600   -19.79800 -8.37000  1.000 62.29373  ? 66  PHE B HD1  1 
ATOM   5558 H HD2  . PHE B 2 66  ? 5.55800   -21.21900 -11.94100 1.000 62.17925  ? 66  PHE B HD2  1 
ATOM   5559 H HE1  . PHE B 2 66  ? 8.40000   -18.64700 -9.37400  1.000 62.18151  ? 66  PHE B HE1  1 
ATOM   5560 H HE2  . PHE B 2 66  ? 7.28900   -20.07200 -12.95100 1.000 64.21336  ? 66  PHE B HE2  1 
ATOM   5561 H HZ   . PHE B 2 66  ? 8.71500   -18.78200 -11.66900 1.000 67.42127  ? 66  PHE B HZ   1 
ATOM   5562 N N    . LEU B 2 67  ? 4.11800   -23.76300 -6.92600  1.000 44.52846  ? 67  LEU B N    1 
ATOM   5563 C CA   . LEU B 2 67  ? 3.02000   -24.34100 -6.17100  1.000 44.28407  ? 67  LEU B CA   1 
ATOM   5564 C C    . LEU B 2 67  ? 2.35100   -23.22900 -5.37800  1.000 42.52742  ? 67  LEU B C    1 
ATOM   5565 O O    . LEU B 2 67  ? 2.98400   -22.59600 -4.52100  1.000 42.02209  ? 67  LEU B O    1 
ATOM   5566 C CB   . LEU B 2 67  ? 3.48800   -25.45300 -5.23400  1.000 46.88887  ? 67  LEU B CB   1 
ATOM   5567 C CG   . LEU B 2 67  ? 4.32100   -26.53300 -5.92400  1.000 56.36534  ? 67  LEU B CG   1 
ATOM   5568 C CD1  . LEU B 2 67  ? 5.78800   -26.11800 -6.00400  1.000 55.57629  ? 67  LEU B CD1  1 
ATOM   5569 C CD2  . LEU B 2 67  ? 4.16900   -27.89800 -5.25100  1.000 63.14546  ? 67  LEU B CD2  1 
ATOM   5570 H H    . LEU B 2 67  ? 4.84500   -23.68800 -6.47400  1.000 53.43496  ? 67  LEU B H    1 
ATOM   5571 H HA   . LEU B 2 67  ? 2.36800   -24.71400 -6.78400  1.000 53.14169  ? 67  LEU B HA   1 
ATOM   5572 H HB2  . LEU B 2 67  ? 4.02600   -25.06200 -4.52900  1.000 56.26744  ? 67  LEU B HB2  1 
ATOM   5573 H HB3  . LEU B 2 67  ? 2.70800   -25.88300 -4.84900  1.000 56.26744  ? 67  LEU B HB3  1 
ATOM   5574 H HG   . LEU B 2 67  ? 4.00000   -26.62600 -6.83500  1.000 67.63920  ? 67  LEU B HG   1 
ATOM   5575 H HD11 . LEU B 2 67  ? 6.32900   -26.91200 -6.13700  1.000 66.69235  ? 67  LEU B HD11 1 
ATOM   5576 H HD12 . LEU B 2 67  ? 5.90900   -25.51200 -6.75000  1.000 66.69235  ? 67  LEU B HD12 1 
ATOM   5577 H HD13 . LEU B 2 67  ? 6.04300   -25.68300 -5.17500  1.000 66.69235  ? 67  LEU B HD13 1 
ATOM   5578 H HD21 . LEU B 2 67  ? 4.70500   -28.54800 -5.73100  1.000 75.77535  ? 67  LEU B HD21 1 
ATOM   5579 H HD22 . LEU B 2 67  ? 4.47300   -27.83200 -4.33200  1.000 75.77535  ? 67  LEU B HD22 1 
ATOM   5580 H HD23 . LEU B 2 67  ? 3.23500   -28.15800 -5.27300  1.000 75.77535  ? 67  LEU B HD23 1 
ATOM   5581 N N    . VAL B 2 68  ? 1.07800   -22.98900 -5.67100  1.000 42.35396  ? 68  VAL B N    1 
ATOM   5582 C CA   . VAL B 2 68  ? 0.31200   -21.93600 -5.01700  1.000 44.49618  ? 68  VAL B CA   1 
ATOM   5583 C C    . VAL B 2 68  ? -0.79600  -22.61400 -4.24400  1.000 45.68417  ? 68  VAL B C    1 
ATOM   5584 O O    . VAL B 2 68  ? -1.59600  -23.36000 -4.82500  1.000 45.28139  ? 68  VAL B O    1 
ATOM   5585 C CB   . VAL B 2 68  ? -0.26100  -20.94500 -6.03400  1.000 40.04557  ? 68  VAL B CB   1 
ATOM   5586 C CG1  . VAL B 2 68  ? -1.13900  -19.86800 -5.31800  1.000 37.65340  ? 68  VAL B CG1  1 
ATOM   5587 C CG2  . VAL B 2 68  ? 0.85000   -20.33500 -6.83800  1.000 43.85029  ? 68  VAL B CG2  1 
ATOM   5588 H H    . VAL B 2 68  ? 0.62800   -23.43100 -6.25600  1.000 50.82555  ? 68  VAL B H    1 
ATOM   5589 H HA   . VAL B 2 68  ? 0.87700   -21.45200 -4.39700  1.000 53.39622  ? 68  VAL B HA   1 
ATOM   5590 H HB   . VAL B 2 68  ? -0.83400  -21.43000 -6.64800  1.000 48.05548  ? 68  VAL B HB   1 
ATOM   5591 H HG11 . VAL B 2 68  ? -1.37100  -19.17800 -5.95800  1.000 45.18488  ? 68  VAL B HG11 1 
ATOM   5592 H HG12 . VAL B 2 68  ? -1.94500  -20.28700 -4.98000  1.000 45.18488  ? 68  VAL B HG12 1 
ATOM   5593 H HG13 . VAL B 2 68  ? -0.63200  -19.48300 -4.58600  1.000 45.18488  ? 68  VAL B HG13 1 
ATOM   5594 H HG21 . VAL B 2 68  ? 0.48000   -19.65100 -7.41800  1.000 52.62115  ? 68  VAL B HG21 1 
ATOM   5595 H HG22 . VAL B 2 68  ? 1.49800   -19.94200 -6.23300  1.000 52.62115  ? 68  VAL B HG22 1 
ATOM   5596 H HG23 . VAL B 2 68  ? 1.27200   -21.02700 -7.37100  1.000 52.62115  ? 68  VAL B HG23 1 
ATOM   5597 N N    . GLN B 2 69  ? -0.83100  -22.38500 -2.93800  1.000 40.33643  ? 69  GLN B N    1 
ATOM   5598 C CA   . GLN B 2 69  ? -1.82400  -23.01200 -2.08200  1.000 44.31230  ? 69  GLN B CA   1 
ATOM   5599 C C    . GLN B 2 69  ? -2.61200  -21.93600 -1.36700  1.000 42.64668  ? 69  GLN B C    1 
ATOM   5600 O O    . GLN B 2 69  ? -2.04100  -21.11400 -0.64400  1.000 41.31276  ? 69  GLN B O    1 
ATOM   5601 C CB   . GLN B 2 69  ? -1.19300  -23.98900 -1.09200  1.000 51.09773  ? 69  GLN B CB   1 
ATOM   5602 C CG   . GLN B 2 69  ? -0.45900  -25.09100 -1.81700  1.000 59.93210  ? 69  GLN B CG   1 
ATOM   5603 C CD   . GLN B 2 69  ? -0.12600  -26.27600 -0.93500  1.000 64.80544  ? 69  GLN B CD   1 
ATOM   5604 O OE1  . GLN B 2 69  ? -0.52800  -26.33400 0.22400   1.000 68.09844  ? 69  GLN B OE1  1 
ATOM   5605 N NE2  . GLN B 2 69  ? 0.61700   -27.23100 -1.48700  1.000 71.72969  ? 69  GLN B NE2  1 
ATOM   5606 H H    . GLN B 2 69  ? -0.28600  -21.86600 -2.52100  1.000 48.40452  ? 69  GLN B H    1 
ATOM   5607 H HA   . GLN B 2 69  ? -2.44500  -23.51300 -2.63200  1.000 53.17556  ? 69  GLN B HA   1 
ATOM   5608 H HB2  . GLN B 2 69  ? -0.55800  -23.51500 -0.53200  1.000 61.31808  ? 69  GLN B HB2  1 
ATOM   5609 H HB3  . GLN B 2 69  ? -1.88900  -24.39000 -0.54900  1.000 61.31808  ? 69  GLN B HB3  1 
ATOM   5610 H HG2  . GLN B 2 69  ? -1.01300  -25.41000 -2.54700  1.000 71.91932  ? 69  GLN B HG2  1 
ATOM   5611 H HG3  . GLN B 2 69  ? 0.37400   -24.73600 -2.16600  1.000 71.91932  ? 69  GLN B HG3  1 
ATOM   5612 H HE21 . GLN B 2 69  ? 0.88000   -27.15400 -2.30200  1.000 86.07643  ? 69  GLN B HE21 1 
ATOM   5613 H HE22 . GLN B 2 69  ? 0.83400   -27.92600 -1.02900  1.000 86.07643  ? 69  GLN B HE22 1 
ATOM   5614 N N    . ALA B 2 70  ? -3.91900  -21.95800 -1.58100  1.000 42.18096  ? 70  ALA B N    1 
ATOM   5615 C CA   . ALA B 2 70  ? -4.87900  -21.10900 -0.90000  1.000 46.44154  ? 70  ALA B CA   1 
ATOM   5616 C C    . ALA B 2 70  ? -5.60500  -22.00400 0.10100   1.000 52.60379  ? 70  ALA B C    1 
ATOM   5617 O O    . ALA B 2 70  ? -6.46000  -22.81800 -0.27500  1.000 47.72122  ? 70  ALA B O    1 
ATOM   5618 C CB   . ALA B 2 70  ? -5.83400  -20.47600 -1.90400  1.000 45.04235  ? 70  ALA B CB   1 
ATOM   5619 H H    . ALA B 2 70  ? -4.29000  -22.48700 -2.14800  1.000 50.61796  ? 70  ALA B H    1 
ATOM   5620 H HA   . ALA B 2 70  ? -4.41700  -20.40600 -0.41700  1.000 55.73065  ? 70  ALA B HA   1 
ATOM   5621 H HB1  . ALA B 2 70  ? -6.46500  -19.91400 -1.42800  1.000 54.05162  ? 70  ALA B HB1  1 
ATOM   5622 H HB2  . ALA B 2 70  ? -5.32300  -19.94200 -2.53200  1.000 54.05162  ? 70  ALA B HB2  1 
ATOM   5623 H HB3  . ALA B 2 70  ? -6.30700  -21.17900 -2.37600  1.000 54.05162  ? 70  ALA B HB3  1 
ATOM   5624 N N    . GLY B 2 71  ? -5.25100  -21.86000 1.37200   1.000 47.88383  ? 71  GLY B N    1 
ATOM   5625 C CA   . GLY B 2 71  ? -5.76600  -22.78900 2.36300   1.000 55.93481  ? 71  GLY B CA   1 
ATOM   5626 C C    . GLY B 2 71  ? -5.36900  -24.20300 1.98600   1.000 58.34377  ? 71  GLY B C    1 
ATOM   5627 O O    . GLY B 2 71  ? -4.18400  -24.51000 1.77800   1.000 60.71885  ? 71  GLY B O    1 
ATOM   5628 H H    . GLY B 2 71  ? -4.72800  -21.25000 1.67900   1.000 57.46140  ? 71  GLY B H    1 
ATOM   5629 H HA2  . GLY B 2 71  ? -5.40100  -22.58000 3.23700   1.000 67.12257  ? 71  GLY B HA2  1 
ATOM   5630 H HA3  . GLY B 2 71  ? -6.73300  -22.73100 2.40200   1.000 67.12257  ? 71  GLY B HA3  1 
ATOM   5631 N N    . ASN B 2 72  ? -6.38100  -25.04700 1.80100   1.000 62.13862  ? 72  ASN B N    1 
ATOM   5632 C CA   . ASN B 2 72  ? -6.13100  -26.47500 1.47000   1.000 65.34928  ? 72  ASN B CA   1 
ATOM   5633 C C    . ASN B 2 72  ? -6.30200  -26.71600 -0.03100  1.000 62.32827  ? 72  ASN B C    1 
ATOM   5634 O O    . ASN B 2 72  ? -6.27200  -27.88300 -0.44200  1.000 69.05337  ? 72  ASN B O    1 
ATOM   5635 C CB   . ASN B 2 72  ? -7.06400  -27.36600 2.28000   1.000 70.85518  ? 72  ASN B CB   1 
ATOM   5636 C CG   . ASN B 2 72  ? -6.60500  -27.50400 3.71200   1.000 80.28249  ? 72  ASN B CG   1 
ATOM   5637 O OD1  . ASN B 2 72  ? -5.65500  -26.83400 4.12900   1.000 77.51196  ? 72  ASN B OD1  1 
ATOM   5638 N ND2  . ASN B 2 72  ? -7.26000  -28.36300 4.47800   1.000 83.18253  ? 72  ASN B ND2  1 
ATOM   5639 H H    . ASN B 2 72  ? -7.21300  -24.83500 1.85700   1.000 74.56714  ? 72  ASN B H    1 
ATOM   5640 H HA   . ASN B 2 72  ? -5.21900  -26.70300 1.70700   1.000 78.41994  ? 72  ASN B HA   1 
ATOM   5641 H HB2  . ASN B 2 72  ? -7.95300  -26.97800 2.28300   1.000 85.02701  ? 72  ASN B HB2  1 
ATOM   5642 H HB3  . ASN B 2 72  ? -7.08600  -28.25100 1.88300   1.000 85.02701  ? 72  ASN B HB3  1 
ATOM   5643 H HD21 . ASN B 2 72  ? -7.02900  -28.47000 5.29900   1.000 99.81983  ? 72  ASN B HD21 1 
ATOM   5644 H HD22 . ASN B 2 72  ? -7.91700  -28.81300 4.15400   1.000 99.81983  ? 72  ASN B HD22 1 
ATOM   5645 N N    . VAL B 2 73  ? -6.48200  -25.65500 -0.80900  1.000 58.41387  ? 73  VAL B N    1 
ATOM   5646 C CA   . VAL B 2 73  ? -6.68300  -25.78800 -2.24900  1.000 57.94321  ? 73  VAL B CA   1 
ATOM   5647 C C    . VAL B 2 73  ? -5.41600  -25.36900 -2.97900  1.000 55.56445  ? 73  VAL B C    1 
ATOM   5648 O O    . VAL B 2 73  ? -4.83500  -24.31900 -2.67800  1.000 53.04443  ? 73  VAL B O    1 
ATOM   5649 C CB   . VAL B 2 73  ? -7.87100  -24.94900 -2.74100  1.000 60.22287  ? 73  VAL B CB   1 
ATOM   5650 C CG1  . VAL B 2 73  ? -7.92400  -24.99200 -4.26400  1.000 58.54011  ? 73  VAL B CG1  1 
ATOM   5651 C CG2  . VAL B 2 73  ? -9.17300  -25.42400 -2.10800  1.000 60.99421  ? 73  VAL B CG2  1 
ATOM   5652 H H    . VAL B 2 73  ? -6.49200  -24.84200 -0.53000  1.000 70.09745  ? 73  VAL B H    1 
ATOM   5653 H HA   . VAL B 2 73  ? -6.86200  -26.71700 -2.46400  1.000 69.53265  ? 73  VAL B HA   1 
ATOM   5654 H HB   . VAL B 2 73  ? -7.73200  -24.02600 -2.47600  1.000 72.26824  ? 73  VAL B HB   1 
ATOM   5655 H HG11 . VAL B 2 73  ? -8.81800  -24.75200 -4.55300  1.000 70.24893  ? 73  VAL B HG11 1 
ATOM   5656 H HG12 . VAL B 2 73  ? -7.28100  -24.36100 -4.62400  1.000 70.24893  ? 73  VAL B HG12 1 
ATOM   5657 H HG13 . VAL B 2 73  ? -7.71300  -25.89100 -4.56200  1.000 70.24893  ? 73  VAL B HG13 1 
ATOM   5658 H HG21 . VAL B 2 73  ? -9.90400  -24.88300 -2.44600  1.000 73.19385  ? 73  VAL B HG21 1 
ATOM   5659 H HG22 . VAL B 2 73  ? -9.31500  -26.35500 -2.34000  1.000 73.19385  ? 73  VAL B HG22 1 
ATOM   5660 H HG23 . VAL B 2 73  ? -9.10900  -25.32900 -1.14500  1.000 73.19385  ? 73  VAL B HG23 1 
ATOM   5661 N N    . GLN B 2 74  ? -5.01700  -26.15900 -3.97000  1.000 51.42013  ? 74  GLN B N    1 
ATOM   5662 C CA   . GLN B 2 74  ? -3.90400  -25.80800 -4.83000  1.000 54.98241  ? 74  GLN B CA   1 
ATOM   5663 C C    . GLN B 2 74  ? -4.45800  -25.03400 -6.02200  1.000 56.15377  ? 74  GLN B C    1 
ATOM   5664 O O    . GLN B 2 74  ? -5.46800  -25.43800 -6.61800  1.000 57.81152  ? 74  GLN B O    1 
ATOM   5665 C CB   . GLN B 2 74  ? -3.15200  -27.06300 -5.27400  1.000 60.78032  ? 74  GLN B CB   1 
ATOM   5666 C CG   . GLN B 2 74  ? -1.93700  -26.79600 -6.13900  1.000 64.97629  ? 74  GLN B CG   1 
ATOM   5667 C CD   . GLN B 2 74  ? -1.22500  -28.07400 -6.56900  1.000 73.09347  ? 74  GLN B CD   1 
ATOM   5668 O OE1  . GLN B 2 74  ? -1.42400  -29.14000 -5.97900  1.000 78.10978  ? 74  GLN B OE1  1 
ATOM   5669 N NE2  . GLN B 2 74  ? -0.39400  -27.97000 -7.60800  1.000 70.70889  ? 74  GLN B NE2  1 
ATOM   5670 H H    . GLN B 2 74  ? -5.38200  -26.91300 -4.16400  1.000 61.70495  ? 74  GLN B H    1 
ATOM   5671 H HA   . GLN B 2 74  ? -3.28800  -25.23400 -4.34900  1.000 65.97969  ? 74  GLN B HA   1 
ATOM   5672 H HB2  . GLN B 2 74  ? -2.85200  -27.54000 -4.48500  1.000 72.93718  ? 74  GLN B HB2  1 
ATOM   5673 H HB3  . GLN B 2 74  ? -3.75800  -27.62400 -5.78300  1.000 72.93718  ? 74  GLN B HB3  1 
ATOM   5674 H HG2  . GLN B 2 74  ? -2.21500  -26.32500 -6.94000  1.000 77.97234  ? 74  GLN B HG2  1 
ATOM   5675 H HG3  . GLN B 2 74  ? -1.30600  -26.25500 -5.63900  1.000 77.97234  ? 74  GLN B HG3  1 
ATOM   5676 H HE21 . GLN B 2 74  ? -0.28200  -27.21000 -7.99500  1.000 84.85147  ? 74  GLN B HE21 1 
ATOM   5677 H HE22 . GLN B 2 74  ? 0.03100   -28.66200 -7.88900  1.000 84.85147  ? 74  GLN B HE22 1 
ATOM   5678 N N    . LEU B 2 75  ? -3.87200  -23.87100 -6.29400  1.000 51.64096  ? 75  LEU B N    1 
ATOM   5679 C CA   . LEU B 2 75  ? -4.24800  -23.06700 -7.45200  1.000 48.70285  ? 75  LEU B CA   1 
ATOM   5680 C C    . LEU B 2 75  ? -3.43000  -23.50300 -8.65600  1.000 53.80351  ? 75  LEU B C    1 
ATOM   5681 O O    . LEU B 2 75  ? -2.22800  -23.76100 -8.54500  1.000 56.65715  ? 75  LEU B O    1 
ATOM   5682 C CB   . LEU B 2 75  ? -4.04200  -21.57100 -7.18300  1.000 48.32302  ? 75  LEU B CB   1 
ATOM   5683 C CG   . LEU B 2 75  ? -4.93600  -20.99000 -6.11200  1.000 48.39195  ? 75  LEU B CG   1 
ATOM   5684 C CD1  . LEU B 2 75  ? -4.78600  -19.45700 -6.00700  1.000 42.70885  ? 75  LEU B CD1  1 
ATOM   5685 C CD2  . LEU B 2 75  ? -6.36000  -21.38600 -6.41600  1.000 47.53556  ? 75  LEU B CD2  1 
ATOM   5686 H H    . LEU B 2 75  ? -3.24700  -23.52300 -5.81700  1.000 61.96995  ? 75  LEU B H    1 
ATOM   5687 H HA   . LEU B 2 75  ? -5.17800  -23.23000 -7.66700  1.000 58.44422  ? 75  LEU B HA   1 
ATOM   5688 H HB2  . LEU B 2 75  ? -3.12300  -21.43000 -6.90600  1.000 57.98843  ? 75  LEU B HB2  1 
ATOM   5689 H HB3  . LEU B 2 75  ? -4.21300  -21.08300 -8.00400  1.000 57.98843  ? 75  LEU B HB3  1 
ATOM   5690 H HG   . LEU B 2 75  ? -4.69400  -21.37500 -5.25500  1.000 58.07114  ? 75  LEU B HG   1 
ATOM   5691 H HD11 . LEU B 2 75  ? -5.34900  -19.13400 -5.28700  1.000 51.25142  ? 75  LEU B HD11 1 
ATOM   5692 H HD12 . LEU B 2 75  ? -3.85800  -19.24300 -5.82300  1.000 51.25142  ? 75  LEU B HD12 1 
ATOM   5693 H HD13 . LEU B 2 75  ? -5.05900  -19.05500 -6.84700  1.000 51.25142  ? 75  LEU B HD13 1 
ATOM   5694 H HD21 . LEU B 2 75  ? -6.96000  -20.77800 -5.95600  1.000 57.04348  ? 75  LEU B HD21 1 
ATOM   5695 H HD22 . LEU B 2 75  ? -6.50500  -21.33200 -7.37400  1.000 57.04348  ? 75  LEU B HD22 1 
ATOM   5696 H HD23 . LEU B 2 75  ? -6.51000  -22.29400 -6.10900  1.000 57.04348  ? 75  LEU B HD23 1 
ATOM   5697 N N    . ARG B 2 76  ? -4.08800  -23.59000 -9.81100  1.000 49.77572  ? 76  ARG B N    1 
ATOM   5698 C CA   . ARG B 2 76  ? -3.41700  -23.99300 -11.03000 1.000 55.95734  ? 76  ARG B CA   1 
ATOM   5699 C C    . ARG B 2 76  ? -2.82100  -22.74600 -11.67900 1.000 50.66521  ? 76  ARG B C    1 
ATOM   5700 O O    . ARG B 2 76  ? -3.55400  -21.79800 -11.99900 1.000 48.53455  ? 76  ARG B O    1 
ATOM   5701 C CB   . ARG B 2 76  ? -4.40200  -24.70400 -11.95600 1.000 54.27788  ? 76  ARG B CB   1 
ATOM   5702 C CG   . ARG B 2 76  ? -3.78700  -25.10400 -13.25900 1.000 61.67899  ? 76  ARG B CG   1 
ATOM   5703 C CD   . ARG B 2 76  ? -4.68100  -26.03200 -14.05500 1.000 67.95669  ? 76  ARG B CD   1 
ATOM   5704 N NE   . ARG B 2 76  ? -4.20000  -26.09000 -15.42800 1.000 74.82167  ? 76  ARG B NE   1 
ATOM   5705 C CZ   . ARG B 2 76  ? -3.06700  -26.69200 -15.77000 1.000 76.81137  ? 76  ARG B CZ   1 
ATOM   5706 N NH1  . ARG B 2 76  ? -2.28200  -27.25700 -14.85800 1.000 73.97897  ? 76  ARG B NH1  1 
ATOM   5707 N NH2  . ARG B 2 76  ? -2.70700  -26.72200 -17.04900 1.000 73.75541  ? 76  ARG B NH2  1 
ATOM   5708 H H    . ARG B 2 76  ? -4.92500  -23.41900 -9.90900  1.000 59.73166  ? 76  ARG B H    1 
ATOM   5709 H HA   . ARG B 2 76  ? -2.69600  -24.60600 -10.81800 1.000 67.14961  ? 76  ARG B HA   1 
ATOM   5710 H HB2  . ARG B 2 76  ? -4.74300  -25.49900 -11.51800 1.000 65.13426  ? 76  ARG B HB2  1 
ATOM   5711 H HB3  . ARG B 2 76  ? -5.11600  -24.09000 -12.14400 1.000 65.13426  ? 76  ARG B HB3  1 
ATOM   5712 H HG2  . ARG B 2 76  ? -3.63000  -24.31000 -13.79300 1.000 74.01559  ? 76  ARG B HG2  1 
ATOM   5713 H HG3  . ARG B 2 76  ? -2.94900  -25.55600 -13.08200 1.000 74.01559  ? 76  ARG B HG3  1 
ATOM   5714 H HD2  . ARG B 2 76  ? -4.65000  -26.92400 -13.67500 1.000 81.54882  ? 76  ARG B HD2  1 
ATOM   5715 H HD3  . ARG B 2 76  ? -5.58900  -25.69100 -14.05700 1.000 81.54882  ? 76  ARG B HD3  1 
ATOM   5716 H HE   . ARG B 2 76  ? -4.57300  -25.57500 -16.00700 1.000 89.78681  ? 76  ARG B HE   1 
ATOM   5717 H HH11 . ARG B 2 76  ? -2.50200  -27.24900 -14.02800 1.000 88.77556  ? 76  ARG B HH11 1 
ATOM   5718 H HH12 . ARG B 2 76  ? -1.55300  -27.64100 -15.10300 1.000 88.77556  ? 76  ARG B HH12 1 
ATOM   5719 H HH21 . ARG B 2 76  ? -3.20700  -26.35600 -17.64500 1.000 88.50730  ? 76  ARG B HH21 1 
ATOM   5720 H HH22 . ARG B 2 76  ? -1.97300  -27.10700 -17.28000 1.000 88.50730  ? 76  ARG B HH22 1 
ATOM   5721 N N    . VAL B 2 77  ? -1.49600  -22.73100 -11.82900 1.000 43.51802  ? 77  VAL B N    1 
ATOM   5722 C CA   . VAL B 2 77  ? -0.79400  -21.62200 -12.47300 1.000 48.84654  ? 77  VAL B CA   1 
ATOM   5723 C C    . VAL B 2 77  ? -0.82100  -21.82700 -13.98300 1.000 52.33994  ? 77  VAL B C    1 
ATOM   5724 O O    . VAL B 2 77  ? -0.46500  -22.89900 -14.48300 1.000 53.08548  ? 77  VAL B O    1 
ATOM   5725 C CB   . VAL B 2 77  ? 0.64600   -21.51900 -11.95500 1.000 48.51412  ? 77  VAL B CB   1 
ATOM   5726 C CG1  . VAL B 2 77  ? 1.41700   -20.44800 -12.72100 1.000 40.83431  ? 77  VAL B CG1  1 
ATOM   5727 C CG2  . VAL B 2 77  ? 0.65600   -21.25900 -10.42700 1.000 46.43198  ? 77  VAL B CG2  1 
ATOM   5728 H H    . VAL B 2 77  ? -0.97500  -23.36100 -11.56200 1.000 52.22243  ? 77  VAL B H    1 
ATOM   5729 H HA   . VAL B 2 77  ? -1.25100  -20.79100 -12.27000 1.000 58.61665  ? 77  VAL B HA   1 
ATOM   5730 H HB   . VAL B 2 77  ? 1.09100   -22.36700 -12.11000 1.000 58.21775  ? 77  VAL B HB   1 
ATOM   5731 H HG11 . VAL B 2 77  ? 2.22700   -20.23500 -12.23200 1.000 49.00197  ? 77  VAL B HG11 1 
ATOM   5732 H HG12 . VAL B 2 77  ? 1.64300   -20.78600 -13.60200 1.000 49.00197  ? 77  VAL B HG12 1 
ATOM   5733 H HG13 . VAL B 2 77  ? 0.86300   -19.65600 -12.80000 1.000 49.00197  ? 77  VAL B HG13 1 
ATOM   5734 H HG21 . VAL B 2 77  ? 1.57400   -21.16400 -10.12900 1.000 55.71918  ? 77  VAL B HG21 1 
ATOM   5735 H HG22 . VAL B 2 77  ? 0.16200   -20.44500 -10.24300 1.000 55.71918  ? 77  VAL B HG22 1 
ATOM   5736 H HG23 . VAL B 2 77  ? 0.23800   -22.00900 -9.97600  1.000 55.71918  ? 77  VAL B HG23 1 
ATOM   5737 N N    . ILE B 2 78  ? -1.28500  -20.82300 -14.72300 1.000 47.10674  ? 78  ILE B N    1 
ATOM   5738 C CA   . ILE B 2 78  ? -1.38400  -20.97500 -16.17200 1.000 45.47523  ? 78  ILE B CA   1 
ATOM   5739 C C    . ILE B 2 78  ? -0.51900  -19.96700 -16.91500 1.000 48.77143  ? 78  ILE B C    1 
ATOM   5740 O O    . ILE B 2 78  ? -0.59400  -19.87600 -18.14100 1.000 46.40522  ? 78  ILE B O    1 
ATOM   5741 C CB   . ILE B 2 78  ? -2.84500  -20.90200 -16.65800 1.000 47.32341  ? 78  ILE B CB   1 
ATOM   5742 C CG1  . ILE B 2 78  ? -3.48100  -19.55800 -16.25600 1.000 46.34145  ? 78  ILE B CG1  1 
ATOM   5743 C CG2  . ILE B 2 78  ? -3.64900  -22.07900 -16.10100 1.000 47.88160  ? 78  ILE B CG2  1 
ATOM   5744 C CD1  . ILE B 2 78  ? -4.82300  -19.28700 -16.91600 1.000 47.98607  ? 78  ILE B CD1  1 
ATOM   5745 H H    . ILE B 2 78  ? -1.54300  -20.06100 -14.42000 1.000 56.52889  ? 78  ILE B H    1 
ATOM   5746 H HA   . ILE B 2 78  ? -1.05500  -21.85300 -16.41500 1.000 54.57108  ? 78  ILE B HA   1 
ATOM   5747 H HB   . ILE B 2 78  ? -2.84700  -20.96300 -17.62600 1.000 56.78890  ? 78  ILE B HB   1 
ATOM   5748 H HG12 . ILE B 2 78  ? -3.61800  -19.55400 -15.29600 1.000 55.61054  ? 78  ILE B HG12 1 
ATOM   5749 H HG13 . ILE B 2 78  ? -2.88300  -18.83600 -16.50400 1.000 55.61054  ? 78  ILE B HG13 1 
ATOM   5750 H HG21 . ILE B 2 78  ? -4.54400  -22.05600 -16.47500 1.000 57.45872  ? 78  ILE B HG21 1 
ATOM   5751 H HG22 . ILE B 2 78  ? -3.20800  -22.90700 -16.34900 1.000 57.45872  ? 78  ILE B HG22 1 
ATOM   5752 H HG23 . ILE B 2 78  ? -3.69100  -22.00300 -15.13500 1.000 57.45872  ? 78  ILE B HG23 1 
ATOM   5753 H HD11 . ILE B 2 78  ? -5.12700  -18.40200 -16.66100 1.000 57.58409  ? 78  ILE B HD11 1 
ATOM   5754 H HD12 . ILE B 2 78  ? -4.71600  -19.33600 -17.87900 1.000 57.58409  ? 78  ILE B HD12 1 
ATOM   5755 H HD13 . ILE B 2 78  ? -5.46200  -19.95400 -16.62000 1.000 57.58409  ? 78  ILE B HD13 1 
ATOM   5756 N N    . GLY B 2 79  ? 0.27700   -19.18600 -16.19700 1.000 46.61644  ? 79  GLY B N    1 
ATOM   5757 C CA   . GLY B 2 79  ? 1.22400   -18.28300 -16.82900 1.000 49.64876  ? 79  GLY B CA   1 
ATOM   5758 C C    . GLY B 2 79  ? 2.03000   -17.60600 -15.74100 1.000 47.83091  ? 79  GLY B C    1 
ATOM   5759 O O    . GLY B 2 79  ? 1.67700   -17.65900 -14.55800 1.000 43.64691  ? 79  GLY B O    1 
ATOM   5760 H H    . GLY B 2 79  ? 0.28900   -19.15900 -15.33800 1.000 55.94053  ? 79  GLY B H    1 
ATOM   5761 H HA2  . GLY B 2 79  ? 1.82200   -18.77600 -17.41200 1.000 59.57931  ? 79  GLY B HA2  1 
ATOM   5762 H HA3  . GLY B 2 79  ? 0.75400   -17.61000 -17.34600 1.000 59.57931  ? 79  GLY B HA3  1 
ATOM   5763 N N    . HIS B 2 80  ? 3.14800   -17.01400 -16.15700 1.000 49.62763  ? 80  HIS B N    1 
ATOM   5764 C CA   . HIS B 2 80  ? 3.99300   -16.27800 -15.23100 1.000 47.03660  ? 80  HIS B CA   1 
ATOM   5765 C C    . HIS B 2 80  ? 4.76200   -15.20400 -15.98000 1.000 48.96922  ? 80  HIS B C    1 
ATOM   5766 O O    . HIS B 2 80  ? 5.11000   -15.36400 -17.16200 1.000 52.41231  ? 80  HIS B O    1 
ATOM   5767 C CB   . HIS B 2 80  ? 4.95100   -17.19700 -14.46500 1.000 49.14893  ? 80  HIS B CB   1 
ATOM   5768 C CG   . HIS B 2 80  ? 5.86300   -17.98900 -15.34600 1.000 56.23530  ? 80  HIS B CG   1 
ATOM   5769 N ND1  . HIS B 2 80  ? 5.58100   -19.28300 -15.73100 1.000 56.14089  ? 80  HIS B ND1  1 
ATOM   5770 C CD2  . HIS B 2 80  ? 7.05900   -17.68100 -15.90300 1.000 62.04863  ? 80  HIS B CD2  1 
ATOM   5771 C CE1  . HIS B 2 80  ? 6.56000   -19.73400 -16.50000 1.000 62.93024  ? 80  HIS B CE1  1 
ATOM   5772 N NE2  . HIS B 2 80  ? 7.46900   -18.78200 -16.62000 1.000 67.80005  ? 80  HIS B NE2  1 
ATOM   5773 H H    . HIS B 2 80  ? 3.43500   -17.02500 -16.96700 1.000 59.55396  ? 80  HIS B H    1 
ATOM   5774 H HA   . HIS B 2 80  ? 3.42700   -15.83500 -14.58000 1.000 56.44472  ? 80  HIS B HA   1 
ATOM   5775 H HB2  . HIS B 2 80  ? 5.50200   -16.65500 -13.87900 1.000 58.97952  ? 80  HIS B HB2  1 
ATOM   5776 H HB3  . HIS B 2 80  ? 4.42900   -17.82300 -13.93900 1.000 58.97952  ? 80  HIS B HB3  1 
ATOM   5777 H HD1  . HIS B 2 80  ? 4.87700   -19.72600 -15.51000 1.000 67.36987  ? 80  HIS B HD1  1 
ATOM   5778 H HD2  . HIS B 2 80  ? 7.50200   -16.87000 -15.82400 1.000 74.45915  ? 80  HIS B HD2  1 
ATOM   5779 H HE1  . HIS B 2 80  ? 6.60300   -20.57900 -16.88600 1.000 75.51709  ? 80  HIS B HE1  1 
ATOM   5780 N N    . SER B 2 81  ? 4.94800   -14.07400 -15.30200 1.000 41.67052  ? 81  SER B N    1 
ATOM   5781 C CA   . SER B 2 81  ? 5.71800   -12.96900 -15.84200 1.000 48.09470  ? 81  SER B CA   1 
ATOM   5782 C C    . SER B 2 81  ? 6.29400   -12.17700 -14.68600 1.000 43.17576  ? 81  SER B C    1 
ATOM   5783 O O    . SER B 2 81  ? 5.83500   -12.27100 -13.53900 1.000 41.25563  ? 81  SER B O    1 
ATOM   5784 C CB   . SER B 2 81  ? 4.88300   -12.05200 -16.73900 1.000 43.95317  ? 81  SER B CB   1 
ATOM   5785 O OG   . SER B 2 81  ? 3.78700   -11.55200 -16.02100 1.000 43.47462  ? 81  SER B OG   1 
ATOM   5786 H H    . SER B 2 81  ? 4.63200   -13.92600 -14.51600 1.000 50.00543  ? 81  SER B H    1 
ATOM   5787 H HA   . SER B 2 81  ? 6.45400   -13.31900 -16.36800 1.000 57.71444  ? 81  SER B HA   1 
ATOM   5788 H HB2  . SER B 2 81  ? 5.43300   -11.31100 -17.03800 1.000 52.74460  ? 81  SER B HB2  1 
ATOM   5789 H HB3  . SER B 2 81  ? 4.56100   -12.55800 -17.50100 1.000 52.74460  ? 81  SER B HB3  1 
ATOM   5790 H HG   . SER B 2 81  ? 3.32800   -11.04800 -16.51200 1.000 52.17035  ? 81  SER B HG   1 
ATOM   5791 N N    . MET B 2 82  ? 7.28600   -11.36000 -15.00900 1.000 43.92792  ? 82  MET B N    1 
ATOM   5792 C CA   . MET B 2 82  ? 7.96800   -10.58900 -13.98700 1.000 45.20619  ? 82  MET B CA   1 
ATOM   5793 C C    . MET B 2 82  ? 7.79200   -9.10100  -14.27700 1.000 43.66299  ? 82  MET B C    1 
ATOM   5794 O O    . MET B 2 82  ? 7.90500   -8.65500  -15.43100 1.000 44.22460  ? 82  MET B O    1 
ATOM   5795 C CB   . MET B 2 82  ? 9.44100   -11.02600 -13.94600 1.000 52.38983  ? 82  MET B CB   1 
ATOM   5796 C CG   . MET B 2 82  ? 10.28600  -10.37200 -12.89500 1.000 53.78990  ? 82  MET B CG   1 
ATOM   5797 S SD   . MET B 2 82  ? 11.89300  -11.23100 -12.87600 1.000 63.17744  ? 82  MET B SD   1 
ATOM   5798 C CE   . MET B 2 82  ? 12.45900  -10.97700 -14.56400 1.000 69.88702  ? 82  MET B CE   1 
ATOM   5799 H H    . MET B 2 82  ? 7.58100   -11.23600 -15.80700 1.000 52.71431  ? 82  MET B H    1 
ATOM   5800 H HA   . MET B 2 82  ? 7.57900   -10.78500 -13.12100 1.000 54.24823  ? 82  MET B HA   1 
ATOM   5801 H HB2  . MET B 2 82  ? 9.47400   -11.98300 -13.79200 1.000 62.86860  ? 82  MET B HB2  1 
ATOM   5802 H HB3  . MET B 2 82  ? 9.83400   -10.82300 -14.80800 1.000 62.86860  ? 82  MET B HB3  1 
ATOM   5803 H HG2  . MET B 2 82  ? 10.42900  -9.43800  -13.11600 1.000 64.54868  ? 82  MET B HG2  1 
ATOM   5804 H HG3  . MET B 2 82  ? 9.86700   -10.46500 -12.02500 1.000 64.54868  ? 82  MET B HG3  1 
ATOM   5805 H HE1  . MET B 2 82  ? 13.39800  -11.21400 -14.61900 1.000 83.86522  ? 82  MET B HE1  1 
ATOM   5806 H HE2  . MET B 2 82  ? 11.94100  -11.54000 -15.16000 1.000 83.86522  ? 82  MET B HE2  1 
ATOM   5807 H HE3  . MET B 2 82  ? 12.34000  -10.04400 -14.80000 1.000 83.86522  ? 82  MET B HE3  1 
ATOM   5808 N N    . GLN B 2 83  ? 7.50400   -8.33500  -13.23400 1.000 38.11961  ? 83  GLN B N    1 
ATOM   5809 C CA   . GLN B 2 83  ? 7.42500   -6.88400  -13.32300 1.000 38.69640  ? 83  GLN B CA   1 
ATOM   5810 C C    . GLN B 2 83  ? 8.30100   -6.26900  -12.23600 1.000 37.84777  ? 83  GLN B C    1 
ATOM   5811 O O    . GLN B 2 83  ? 7.94700   -6.31900  -11.05100 1.000 34.43041  ? 83  GLN B O    1 
ATOM   5812 C CB   . GLN B 2 83  ? 5.97100   -6.43400  -13.18300 1.000 39.71334  ? 83  GLN B CB   1 
ATOM   5813 C CG   . GLN B 2 83  ? 5.87500   -4.93800  -13.13500 1.000 44.88610  ? 83  GLN B CG   1 
ATOM   5814 C CD   . GLN B 2 83  ? 4.47300   -4.43000  -13.00700 1.000 49.20450  ? 83  GLN B CD   1 
ATOM   5815 O OE1  . GLN B 2 83  ? 3.56700   -5.17800  -12.64100 1.000 47.73059  ? 83  GLN B OE1  1 
ATOM   5816 N NE2  . GLN B 2 83  ? 4.27700   -3.15900  -13.28600 1.000 50.59952  ? 83  GLN B NE2  1 
ATOM   5817 H H    . GLN B 2 83  ? 7.34700   -8.64000  -12.44500 1.000 45.74433  ? 83  GLN B H    1 
ATOM   5818 H HA   . GLN B 2 83  ? 7.75600   -6.59100  -14.18600 1.000 46.43648  ? 83  GLN B HA   1 
ATOM   5819 H HB2  . GLN B 2 83  ? 5.46200   -6.74900  -13.94600 1.000 47.65680  ? 83  GLN B HB2  1 
ATOM   5820 H HB3  . GLN B 2 83  ? 5.60100   -6.79100  -12.36000 1.000 47.65680  ? 83  GLN B HB3  1 
ATOM   5821 H HG2  . GLN B 2 83  ? 6.36600   -4.60600  -12.36800 1.000 53.86412  ? 83  GLN B HG2  1 
ATOM   5822 H HG3  . GLN B 2 83  ? 6.25100   -4.57300  -13.95100 1.000 53.86412  ? 83  GLN B HG3  1 
ATOM   5823 H HE21 . GLN B 2 83  ? 4.93700   -2.66700  -13.53600 1.000 60.72023  ? 83  GLN B HE21 1 
ATOM   5824 H HE22 . GLN B 2 83  ? 3.48800   -2.82200  -13.22500 1.000 60.72023  ? 83  GLN B HE22 1 
ATOM   5825 N N    . ASN B 2 84  ? 9.42500   -5.67100  -12.63100 1.000 38.25789  ? 84  ASN B N    1 
ATOM   5826 C CA   . ASN B 2 84  ? 10.38300  -5.11600  -11.65500 1.000 36.59674  ? 84  ASN B CA   1 
ATOM   5827 C C    . ASN B 2 84  ? 10.71300  -6.26700  -10.71000 1.000 33.95844  ? 84  ASN B C    1 
ATOM   5828 O O    . ASN B 2 84  ? 11.02500  -7.35900  -11.21700 1.000 34.52764  ? 84  ASN B O    1 
ATOM   5829 C CB   . ASN B 2 84  ? 9.79100   -3.86400  -11.00700 1.000 34.86868  ? 84  ASN B CB   1 
ATOM   5830 C CG   . ASN B 2 84  ? 9.49100   -2.78600  -12.03700 1.000 40.02986  ? 84  ASN B CG   1 
ATOM   5831 O OD1  . ASN B 2 84  ? 10.35900  -2.44600  -12.82600 1.000 39.26058  ? 84  ASN B OD1  1 
ATOM   5832 N ND2  . ASN B 2 84  ? 8.25500   -2.29600  -12.07400 1.000 37.10486  ? 84  ASN B ND2  1 
ATOM   5833 H H    . ASN B 2 84  ? 9.66100   -5.57100  -13.45200 1.000 45.91027  ? 84  ASN B H    1 
ATOM   5834 H HA   . ASN B 2 84  ? 11.19700  -4.86100  -12.11600 1.000 43.91689  ? 84  ASN B HA   1 
ATOM   5835 H HB2  . ASN B 2 84  ? 8.96200   -4.09600  -10.56100 1.000 41.84321  ? 84  ASN B HB2  1 
ATOM   5836 H HB3  . ASN B 2 84  ? 10.42600  -3.50500  -10.36800 1.000 41.84321  ? 84  ASN B HB3  1 
ATOM   5837 H HD21 . ASN B 2 84  ? 8.05000   -1.68900  -12.64800 1.000 44.52664  ? 84  ASN B HD21 1 
ATOM   5838 H HD22 . ASN B 2 84  ? 7.66700   -2.56900  -11.50800 1.000 44.52664  ? 84  ASN B HD22 1 
ATOM   5839 N N    . CYS B 2 85  ? 10.58700  -6.09700  -9.38800  1.000 32.93966  ? 85  CYS B N    1 
ATOM   5840 C CA   . CYS B 2 85  ? 10.97200  -7.12300  -8.43100  1.000 35.01600  ? 85  CYS B CA   1 
ATOM   5841 C C    . CYS B 2 85  ? 9.78900   -8.00500  -8.01100  1.000 35.52098  ? 85  CYS B C    1 
ATOM   5842 O O    . CYS B 2 85  ? 9.88400   -8.76700  -7.03300  1.000 32.00371  ? 85  CYS B O    1 
ATOM   5843 C CB   . CYS B 2 85  ? 11.63900  -6.46800  -7.22100  1.000 35.01995  ? 85  CYS B CB   1 
ATOM   5844 S SG   . CYS B 2 85  ? 13.17100  -5.54500  -7.67300  1.000 37.48078  ? 85  CYS B SG   1 
ATOM   5845 H H    . CYS B 2 85  ? 10.27600  -5.38400  -9.02100  1.000 39.52839  ? 85  CYS B H    1 
ATOM   5846 H HA   . CYS B 2 85  ? 11.63200  -7.69700  -8.84700  1.000 42.02000  ? 85  CYS B HA   1 
ATOM   5847 H HB2  . CYS B 2 85  ? 11.01800  -5.84100  -6.81800  1.000 42.02474  ? 85  CYS B HB2  1 
ATOM   5848 H HB3  . CYS B 2 85  ? 11.88000  -7.15600  -6.58100  1.000 42.02474  ? 85  CYS B HB3  1 
ATOM   5849 H HG   . CYS B 2 85  ? 13.67400  -5.05300  -6.70600  1.000 44.97774  ? 85  CYS B HG   1 
ATOM   5850 N N    . VAL B 2 86  ? 8.68900   -7.97500  -8.75000  1.000 32.74726  ? 86  VAL B N    1 
ATOM   5851 C CA   . VAL B 2 86  ? 7.54400   -8.80800  -8.39300  1.000 34.70297  ? 86  VAL B CA   1 
ATOM   5852 C C    . VAL B 2 86  ? 7.28500   -9.80800  -9.50600  1.000 35.76891  ? 86  VAL B C    1 
ATOM   5853 O O    . VAL B 2 86  ? 7.42200   -9.50900  -10.70100 1.000 36.76013  ? 86  VAL B O    1 
ATOM   5854 C CB   . VAL B 2 86  ? 6.24600   -8.02200  -8.06200  1.000 35.28782  ? 86  VAL B CB   1 
ATOM   5855 C CG1  . VAL B 2 86  ? 6.37100   -7.21800  -6.68700  1.000 34.91812  ? 86  VAL B CG1  1 
ATOM   5856 C CG2  . VAL B 2 86  ? 5.82700   -7.18500  -9.22100  1.000 44.95569  ? 86  VAL B CG2  1 
ATOM   5857 H H    . VAL B 2 86  ? 8.57700   -7.49100  -9.45200  1.000 39.29751  ? 86  VAL B H    1 
ATOM   5858 H HA   . VAL B 2 86  ? 7.76500   -9.32200  -7.60200  1.000 41.64437  ? 86  VAL B HA   1 
ATOM   5859 H HB   . VAL B 2 86  ? 5.54000   -8.67500  -7.93000  1.000 42.34618  ? 86  VAL B HB   1 
ATOM   5860 H HG11 . VAL B 2 86  ? 5.73300   -6.48700  -6.69000  1.000 41.90254  ? 86  VAL B HG11 1 
ATOM   5861 H HG12 . VAL B 2 86  ? 6.18200   -7.82100  -5.95100  1.000 41.90254  ? 86  VAL B HG12 1 
ATOM   5862 H HG13 . VAL B 2 86  ? 7.27200   -6.87000  -6.60700  1.000 41.90254  ? 86  VAL B HG13 1 
ATOM   5863 H HG21 . VAL B 2 86  ? 4.91600   -6.88700  -9.07400  1.000 53.94763  ? 86  VAL B HG21 1 
ATOM   5864 H HG22 . VAL B 2 86  ? 6.41500   -6.41700  -9.28000  1.000 53.94763  ? 86  VAL B HG22 1 
ATOM   5865 H HG23 . VAL B 2 86  ? 5.87200   -7.70400  -10.03800 1.000 53.94763  ? 86  VAL B HG23 1 
ATOM   5866 N N    . LEU B 2 87  ? 6.96000   -11.01600 -9.09100  1.000 33.39012  ? 87  LEU B N    1 
ATOM   5867 C CA   . LEU B 2 87  ? 6.50100   -12.06200 -9.97100  1.000 34.39345  ? 87  LEU B CA   1 
ATOM   5868 C C    . LEU B 2 87  ? 4.98000   -12.03900 -10.00300 1.000 35.03798  ? 87  LEU B C    1 
ATOM   5869 O O    . LEU B 2 87  ? 4.34800   -11.82600 -8.97700  1.000 32.12396  ? 87  LEU B O    1 
ATOM   5870 C CB   . LEU B 2 87  ? 7.02400   -13.39500 -9.45000  1.000 36.47169  ? 87  LEU B CB   1 
ATOM   5871 C CG   . LEU B 2 87  ? 6.67700   -14.67400 -10.16800 1.000 42.94005  ? 87  LEU B CG   1 
ATOM   5872 C CD1  . LEU B 2 87  ? 7.19200   -14.60700 -11.57300 1.000 39.34164  ? 87  LEU B CD1  1 
ATOM   5873 C CD2  . LEU B 2 87  ? 7.33200   -15.80200 -9.38300  1.000 46.02842  ? 87  LEU B CD2  1 
ATOM   5874 H H    . LEU B 2 87  ? 7.00000   -11.26100 -8.26800  1.000 40.06894  ? 87  LEU B H    1 
ATOM   5875 H HA   . LEU B 2 87  ? 6.84000   -11.91600 -10.86800 1.000 41.27294  ? 87  LEU B HA   1 
ATOM   5876 H HB2  . LEU B 2 87  ? 7.99200   -13.34200 -9.43500  1.000 43.76683  ? 87  LEU B HB2  1 
ATOM   5877 H HB3  . LEU B 2 87  ? 6.70400   -13.49400 -8.54000  1.000 43.76683  ? 87  LEU B HB3  1 
ATOM   5878 H HG   . LEU B 2 87  ? 5.71600   -14.80500 -10.18100 1.000 51.52886  ? 87  LEU B HG   1 
ATOM   5879 H HD11 . LEU B 2 87  ? 7.04400   -15.46400 -12.00400 1.000 47.21077  ? 87  LEU B HD11 1 
ATOM   5880 H HD12 . LEU B 2 87  ? 6.71600   -13.91100 -12.05000 1.000 47.21077  ? 87  LEU B HD12 1 
ATOM   5881 H HD13 . LEU B 2 87  ? 8.14100   -14.40700 -11.55200 1.000 47.21077  ? 87  LEU B HD13 1 
ATOM   5882 H HD21 . LEU B 2 87  ? 6.96800   -16.64400 -9.69400  1.000 55.23491  ? 87  LEU B HD21 1 
ATOM   5883 H HD22 . LEU B 2 87  ? 8.29000   -15.77700 -9.53100  1.000 55.23491  ? 87  LEU B HD22 1 
ATOM   5884 H HD23 . LEU B 2 87  ? 7.13700   -15.68900 -8.44000  1.000 55.23491  ? 87  LEU B HD23 1 
ATOM   5885 N N    . LYS B 2 88  ? 4.39200   -12.23400 -11.18200 1.000 33.16281  ? 88  LYS B N    1 
ATOM   5886 C CA   . LYS B 2 88  ? 2.94200   -12.26000 -11.36300 1.000 34.22427  ? 88  LYS B CA   1 
ATOM   5887 C C    . LYS B 2 88  ? 2.56900   -13.63900 -11.88300 1.000 36.49889  ? 88  LYS B C    1 
ATOM   5888 O O    . LYS B 2 88  ? 2.86300   -13.96400 -13.03600 1.000 40.07245  ? 88  LYS B O    1 
ATOM   5889 C CB   . LYS B 2 88  ? 2.46100   -11.17000 -12.33200 1.000 35.69626  ? 88  LYS B CB   1 
ATOM   5890 C CG   . LYS B 2 88  ? 2.84100   -9.76300  -11.89300 1.000 38.43067  ? 88  LYS B CG   1 
ATOM   5891 C CD   . LYS B 2 88  ? 2.05800   -8.70100  -12.66100 1.000 43.64176  ? 88  LYS B CD   1 
ATOM   5892 C CE   . LYS B 2 88  ? 2.55200   -8.43900  -14.04400 1.000 51.14136  ? 88  LYS B CE   1 
ATOM   5893 N NZ   . LYS B 2 88  ? 1.79000   -7.29200  -14.66800 1.000 57.37479  ? 88  LYS B NZ   1 
ATOM   5894 H H    . LYS B 2 88  ? 4.82600   -12.35700 -11.91400 1.000 39.79617  ? 88  LYS B H    1 
ATOM   5895 H HA   . LYS B 2 88  ? 2.50400   -12.12500 -10.50800 1.000 41.06993  ? 88  LYS B HA   1 
ATOM   5896 H HB2  . LYS B 2 88  ? 2.85700   -11.32700 -13.20300 1.000 42.83632  ? 88  LYS B HB2  1 
ATOM   5897 H HB3  . LYS B 2 88  ? 1.49400   -11.21300 -12.39600 1.000 42.83632  ? 88  LYS B HB3  1 
ATOM   5898 H HG2  . LYS B 2 88  ? 2.64600   -9.66000  -10.94800 1.000 46.11760  ? 88  LYS B HG2  1 
ATOM   5899 H HG3  . LYS B 2 88  ? 3.78600   -9.62100  -12.05800 1.000 46.11760  ? 88  LYS B HG3  1 
ATOM   5900 H HD2  . LYS B 2 88  ? 1.13300   -8.98500  -12.72900 1.000 52.37091  ? 88  LYS B HD2  1 
ATOM   5901 H HD3  . LYS B 2 88  ? 2.10700   -7.86600  -12.17000 1.000 52.37091  ? 88  LYS B HD3  1 
ATOM   5902 H HE2  . LYS B 2 88  ? 3.49200   -8.20200  -14.01200 1.000 61.37044  ? 88  LYS B HE2  1 
ATOM   5903 H HE3  . LYS B 2 88  ? 2.41900   -9.23000  -14.59000 1.000 61.37044  ? 88  LYS B HE3  1 
ATOM   5904 H HZ1  . LYS B 2 88  ? 2.08900   -7.14100  -15.49200 1.000 68.85055  ? 88  LYS B HZ1  1 
ATOM   5905 H HZ2  . LYS B 2 88  ? 0.92300   -7.48800  -14.70700 1.000 68.85055  ? 88  LYS B HZ2  1 
ATOM   5906 H HZ3  . LYS B 2 88  ? 1.89800   -6.55500  -14.18100 1.000 68.85055  ? 88  LYS B HZ3  1 
ATOM   5907 N N    . LEU B 2 89  ? 1.93000   -14.45800 -11.04800 1.000 36.09528  ? 89  LEU B N    1 
ATOM   5908 C CA   . LEU B 2 89  ? 1.55100   -15.81400 -11.43500 1.000 34.53341  ? 89  LEU B CA   1 
ATOM   5909 C C    . LEU B 2 89  ? 0.10100   -15.79100 -11.87900 1.000 37.62428  ? 89  LEU B C    1 
ATOM   5910 O O    . LEU B 2 89  ? -0.79300  -15.53000 -11.07800 1.000 34.93860  ? 89  LEU B O    1 
ATOM   5911 C CB   . LEU B 2 89  ? 1.75900   -16.79600 -10.28500 1.000 36.89405  ? 89  LEU B CB   1 
ATOM   5912 C CG   . LEU B 2 89  ? 3.22300   -16.86200 -9.86300  1.000 37.39959  ? 89  LEU B CG   1 
ATOM   5913 C CD1  . LEU B 2 89  ? 3.41500   -17.73500 -8.61800  1.000 41.57109  ? 89  LEU B CD1  1 
ATOM   5914 C CD2  . LEU B 2 89  ? 4.01000   -17.40500 -11.01800 1.000 40.27467  ? 89  LEU B CD2  1 
ATOM   5915 H H    . LEU B 2 89  ? 1.70300   -14.24900 -10.24500 1.000 43.31514  ? 89  LEU B H    1 
ATOM   5916 H HA   . LEU B 2 89  ? 2.08600   -16.09700 -12.19100 1.000 41.44089  ? 89  LEU B HA   1 
ATOM   5917 H HB2  . LEU B 2 89  ? 1.23700   -16.50700 -9.52100  1.000 44.27366  ? 89  LEU B HB2  1 
ATOM   5918 H HB3  . LEU B 2 89  ? 1.48000   -17.68200 -10.56500 1.000 44.27366  ? 89  LEU B HB3  1 
ATOM   5919 H HG   . LEU B 2 89  ? 3.54500   -15.96900 -9.66400  1.000 44.88031  ? 89  LEU B HG   1 
ATOM   5920 H HD11 . LEU B 2 89  ? 4.35500   -17.74200 -8.38000  1.000 49.88611  ? 89  LEU B HD11 1 
ATOM   5921 H HD12 . LEU B 2 89  ? 2.89200   -17.36500 -7.89000  1.000 49.88611  ? 89  LEU B HD12 1 
ATOM   5922 H HD13 . LEU B 2 89  ? 3.11600   -18.63600 -8.81600  1.000 49.88611  ? 89  LEU B HD13 1 
ATOM   5923 H HD21 . LEU B 2 89  ? 4.85700   -17.74400 -10.68900 1.000 48.33040  ? 89  LEU B HD21 1 
ATOM   5924 H HD22 . LEU B 2 89  ? 3.50700   -18.12200 -11.43600 1.000 48.33040  ? 89  LEU B HD22 1 
ATOM   5925 H HD23 . LEU B 2 89  ? 4.16600   -16.69400 -11.65900 1.000 48.33040  ? 89  LEU B HD23 1 
ATOM   5926 N N    . LYS B 2 90  ? -0.14100  -16.06700 -13.15800 1.000 37.03565  ? 90  LYS B N    1 
ATOM   5927 C CA   . LYS B 2 90  ? -1.50900  -16.17900 -13.62700 1.000 40.75064  ? 90  LYS B CA   1 
ATOM   5928 C C    . LYS B 2 90  ? -2.07200  -17.53600 -13.22600 1.000 39.38341  ? 90  LYS B C    1 
ATOM   5929 O O    . LYS B 2 90  ? -1.43600  -18.56300 -13.48300 1.000 42.50482  ? 90  LYS B O    1 
ATOM   5930 C CB   . LYS B 2 90  ? -1.56100  -16.00000 -15.14300 1.000 41.84240  ? 90  LYS B CB   1 
ATOM   5931 C CG   . LYS B 2 90  ? -2.95000  -15.87700 -15.67900 1.000 48.55090  ? 90  LYS B CG   1 
ATOM   5932 C CD   . LYS B 2 90  ? -3.40600  -14.41600 -15.62600 1.000 53.75669  ? 90  LYS B CD   1 
ATOM   5933 C CE   . LYS B 2 90  ? -4.54200  -14.14700 -16.64500 1.000 65.79950  ? 90  LYS B CE   1 
ATOM   5934 N NZ   . LYS B 2 90  ? -5.06900  -12.74300 -16.50500 1.000 66.88462  ? 90  LYS B NZ   1 
ATOM   5935 H H    . LYS B 2 90  ? 0.46000   -16.19100 -13.76100 1.000 44.44358  ? 90  LYS B H    1 
ATOM   5936 H HA   . LYS B 2 90  ? -2.05100  -15.48700 -13.21700 1.000 48.90157  ? 90  LYS B HA   1 
ATOM   5937 H HB2  . LYS B 2 90  ? -1.06700  -15.20000 -15.38200 1.000 50.21168  ? 90  LYS B HB2  1 
ATOM   5938 H HB3  . LYS B 2 90  ? -1.15200  -16.77400 -15.56100 1.000 50.21168  ? 90  LYS B HB3  1 
ATOM   5939 H HG2  . LYS B 2 90  ? -2.96700  -16.17100 -16.60300 1.000 58.26188  ? 90  LYS B HG2  1 
ATOM   5940 H HG3  . LYS B 2 90  ? -3.55900  -16.40800 -15.14300 1.000 58.26188  ? 90  LYS B HG3  1 
ATOM   5941 H HD2  . LYS B 2 90  ? -3.74100  -14.21700 -14.73800 1.000 64.50883  ? 90  LYS B HD2  1 
ATOM   5942 H HD3  . LYS B 2 90  ? -2.66300  -13.83200 -15.84500 1.000 64.50883  ? 90  LYS B HD3  1 
ATOM   5943 H HE2  . LYS B 2 90  ? -4.19900  -14.25700 -17.54600 1.000 78.96021  ? 90  LYS B HE2  1 
ATOM   5944 H HE3  . LYS B 2 90  ? -5.27200  -14.76500 -16.48400 1.000 78.96021  ? 90  LYS B HE3  1 
ATOM   5945 H HZ1  . LYS B 2 90  ? -5.72000  -12.60200 -17.09500 1.000 80.26235  ? 90  LYS B HZ1  1 
ATOM   5946 H HZ2  . LYS B 2 90  ? -5.39100  -12.62000 -15.68500 1.000 80.26235  ? 90  LYS B HZ2  1 
ATOM   5947 H HZ3  . LYS B 2 90  ? -4.41500  -12.15700 -16.65000 1.000 80.26235  ? 90  LYS B HZ3  1 
ATOM   5948 N N    . VAL B 2 91  ? -3.27000  -17.54400 -12.61900 1.000 39.83752  ? 91  VAL B N    1 
ATOM   5949 C CA   . VAL B 2 91  ? -3.93400  -18.77400 -12.19100 1.000 40.08789  ? 91  VAL B CA   1 
ATOM   5950 C C    . VAL B 2 91  ? -5.28400  -18.91000 -12.91000 1.000 46.18122  ? 91  VAL B C    1 
ATOM   5951 O O    . VAL B 2 91  ? -5.79700  -17.96300 -13.52000 1.000 41.52673  ? 91  VAL B O    1 
ATOM   5952 C CB   . VAL B 2 91  ? -4.10100  -18.84700 -10.64700 1.000 39.86412  ? 91  VAL B CB   1 
ATOM   5953 C CG1  . VAL B 2 91  ? -2.75700  -18.97300 -9.98000  1.000 41.68203  ? 91  VAL B CG1  1 
ATOM   5954 C CG2  . VAL B 2 91  ? -4.81700  -17.62700 -10.11600 1.000 42.20172  ? 91  VAL B CG2  1 
ATOM   5955 H H    . VAL B 2 91  ? -3.72100  -16.83300 -12.44400 1.000 47.80582  ? 91  VAL B H    1 
ATOM   5956 H HA   . VAL B 2 91  ? -3.38400  -19.52400 -12.46000 1.000 48.10627  ? 91  VAL B HA   1 
ATOM   5957 H HB   . VAL B 2 91  ? -4.62700  -19.63000 -10.42000 1.000 47.83774  ? 91  VAL B HB   1 
ATOM   5958 H HG11 . VAL B 2 91  ? -2.88500  -19.02000 -9.02000  1.000 50.01924  ? 91  VAL B HG11 1 
ATOM   5959 H HG12 . VAL B 2 91  ? -2.32300  -19.78100 -10.29600 1.000 50.01924  ? 91  VAL B HG12 1 
ATOM   5960 H HG13 . VAL B 2 91  ? -2.21900  -18.19800 -10.20500 1.000 50.01924  ? 91  VAL B HG13 1 
ATOM   5961 H HG21 . VAL B 2 91  ? -4.92000  -17.71600 -9.15600  1.000 50.64286  ? 91  VAL B HG21 1 
ATOM   5962 H HG22 . VAL B 2 91  ? -4.29100  -16.83800 -10.31900 1.000 50.64286  ? 91  VAL B HG22 1 
ATOM   5963 H HG23 . VAL B 2 91  ? -5.68800  -17.56300 -10.53700 1.000 50.64286  ? 91  VAL B HG23 1 
ATOM   5964 N N    . ASP B 2 92  ? -5.85400  -20.11800 -12.84200 1.000 43.39300  ? 92  ASP B N    1 
ATOM   5965 C CA   . ASP B 2 92  ? -7.03600  -20.45900 -13.63000 1.000 44.87536  ? 92  ASP B CA   1 
ATOM   5966 C C    . ASP B 2 92  ? -8.35200  -20.07800 -12.96600 1.000 48.49037  ? 92  ASP B C    1 
ATOM   5967 O O    . ASP B 2 92  ? -9.40100  -20.22900 -13.59900 1.000 49.75710  ? 92  ASP B O    1 
ATOM   5968 C CB   . ASP B 2 92  ? -7.02300  -21.96400 -13.95700 1.000 58.59851  ? 92  ASP B CB   1 
ATOM   5969 C CG   . ASP B 2 92  ? -7.23400  -22.85800 -12.71700 1.000 58.46238  ? 92  ASP B CG   1 
ATOM   5970 O OD1  . ASP B 2 92  ? -7.42200  -22.35400 -11.59900 1.000 53.60319  ? 92  ASP B OD1  1 
ATOM   5971 O OD2  . ASP B 2 92  ? -7.19600  -24.10200 -12.86500 1.000 72.48246  ? 92  ASP B OD2  1 
ATOM   5972 H H    . ASP B 2 92  ? -5.57100  -20.75900 -12.34300 1.000 52.07240  ? 92  ASP B H    1 
ATOM   5973 H HA   . ASP B 2 92  ? -6.98900  -19.98000 -14.47200 1.000 53.85123  ? 92  ASP B HA   1 
ATOM   5974 H HB2  . ASP B 2 92  ? -7.73500  -22.15500 -14.58700 1.000 70.31901  ? 92  ASP B HB2  1 
ATOM   5975 H HB3  . ASP B 2 92  ? -6.16500  -22.19300 -14.34800 1.000 70.31901  ? 92  ASP B HB3  1 
ATOM   5976 N N    . THR B 2 93  ? -8.31200  -19.53000 -11.74500 1.000 42.26739  ? 93  THR B N    1 
ATOM   5977 C CA   . THR B 2 93  ? -9.48400  -19.17700 -10.94900 1.000 44.61137  ? 93  THR B CA   1 
ATOM   5978 C C    . THR B 2 93  ? -9.31600  -17.76200 -10.42700 1.000 39.11956  ? 93  THR B C    1 
ATOM   5979 O O    . THR B 2 93  ? -8.28300  -17.44000 -9.83400  1.000 38.42214  ? 93  THR B O    1 
ATOM   5980 C CB   . THR B 2 93  ? -9.66600  -20.15000 -9.77000  1.000 45.92112  ? 93  THR B CB   1 
ATOM   5981 O OG1  . THR B 2 93  ? -9.74600  -21.49100 -10.27600 1.000 50.35140  ? 93  THR B OG1  1 
ATOM   5982 C CG2  . THR B 2 93  ? -10.95000 -19.84800 -9.03100  1.000 51.73019  ? 93  THR B CG2  1 
ATOM   5983 H H    . THR B 2 93  ? -7.57600  -19.34600 -11.34100 1.000 50.72167  ? 93  THR B H    1 
ATOM   5984 H HA   . THR B 2 93  ? -10.27900 -19.21000 -11.50400 1.000 53.53444  ? 93  THR B HA   1 
ATOM   5985 H HB   . THR B 2 93  ? -8.92000  -20.07100 -9.15500  1.000 55.10614  ? 93  THR B HB   1 
ATOM   5986 H HG1  . THR B 2 93  ? -9.03800  -21.68700 -10.68300 1.000 60.42248  ? 93  THR B HG1  1 
ATOM   5987 H HG21 . THR B 2 93  ? -11.12700 -20.54500 -8.38000  1.000 62.07703  ? 93  THR B HG21 1 
ATOM   5988 H HG22 . THR B 2 93  ? -10.87800 -18.99800 -8.57000  1.000 62.07703  ? 93  THR B HG22 1 
ATOM   5989 H HG23 . THR B 2 93  ? -11.69000 -19.80700 -9.65600  1.000 62.07703  ? 93  THR B HG23 1 
ATOM   5990 N N    . ALA B 2 94  ? -10.32700 -16.91800 -10.61700 1.000 36.91612  ? 94  ALA B N    1 
ATOM   5991 C CA   . ALA B 2 94  ? -10.28100 -15.60300 -10.00200 1.000 30.72590  ? 94  ALA B CA   1 
ATOM   5992 C C    . ALA B 2 94  ? -10.63100 -15.74200 -8.52900  1.000 37.82719  ? 94  ALA B C    1 
ATOM   5993 O O    . ALA B 2 94  ? -11.52500 -16.50500 -8.16700  1.000 33.79311  ? 94  ALA B O    1 
ATOM   5994 C CB   . ALA B 2 94  ? -11.24600 -14.64200 -10.70200 1.000 36.23816  ? 94  ALA B CB   1 
ATOM   5995 H H    . ALA B 2 94  ? -11.03100 -17.07900 -11.08500 1.000 44.30014  ? 94  ALA B H    1 
ATOM   5996 H HA   . ALA B 2 94  ? -9.38300  -15.24300 -10.07300 1.000 36.87188  ? 94  ALA B HA   1 
ATOM   5997 H HB1  . ALA B 2 94  ? -11.19400 -13.77400 -10.27200 1.000 43.48660  ? 94  ALA B HB1  1 
ATOM   5998 H HB2  . ALA B 2 94  ? -10.99200 -14.56500 -11.63500 1.000 43.48660  ? 94  ALA B HB2  1 
ATOM   5999 H HB3  . ALA B 2 94  ? -12.14700 -14.99300 -10.63200 1.000 43.48660  ? 94  ALA B HB3  1 
ATOM   6000 N N    . ASN B 2 95  ? -9.92500  -15.00900 -7.67400  1.000 33.85966  ? 95  ASN B N    1 
ATOM   6001 C CA   . ASN B 2 95  ? -10.18700 -15.08200 -6.24500  1.000 32.65954  ? 95  ASN B CA   1 
ATOM   6002 C C    . ASN B 2 95  ? -11.59200 -14.58100 -5.94100  1.000 36.05341  ? 95  ASN B C    1 
ATOM   6003 O O    . ASN B 2 95  ? -11.87200 -13.38400 -6.13700  1.000 32.33570  ? 95  ASN B O    1 
ATOM   6004 C CB   . ASN B 2 95  ? -9.14600  -14.23500 -5.47000  1.000 29.47805  ? 95  ASN B CB   1 
ATOM   6005 C CG   . ASN B 2 95  ? -9.30000  -14.35800 -3.96600  1.000 36.38221  ? 95  ASN B CG   1 
ATOM   6006 O OD1  . ASN B 2 95  ? -10.19400 -15.04800 -3.50100  1.000 30.85623  ? 95  ASN B OD1  1 
ATOM   6007 N ND2  . ASN B 2 95  ? -8.39100  -13.70600 -3.19000  1.000 30.16390  ? 95  ASN B ND2  1 
ATOM   6008 H H    . ASN B 2 95  ? -9.29500  -14.46700 -7.89500  1.000 40.63239  ? 95  ASN B H    1 
ATOM   6009 H HA   . ASN B 2 95  ? -10.10700 -16.00100 -5.95100  1.000 39.19226  ? 95  ASN B HA   1 
ATOM   6010 H HB2  . ASN B 2 95  ? -8.25400  -14.52300 -5.70900  1.000 35.37446  ? 95  ASN B HB2  1 
ATOM   6011 H HB3  . ASN B 2 95  ? -9.25900  -13.30300 -5.70400  1.000 35.37446  ? 95  ASN B HB3  1 
ATOM   6012 H HD21 . ASN B 2 95  ? -8.44400  -13.75500 -2.33300  1.000 36.19749  ? 95  ASN B HD21 1 
ATOM   6013 H HD22 . ASN B 2 95  ? -7.77200  -13.23500 -3.55700  1.000 36.19749  ? 95  ASN B HD22 1 
ATOM   6014 N N    . PRO B 2 96  ? -12.51600 -15.43400 -5.46300  1.000 34.40416  ? 96  PRO B N    1 
ATOM   6015 C CA   . PRO B 2 96  ? -13.87800 -14.93500 -5.21100  1.000 35.75205  ? 96  PRO B CA   1 
ATOM   6016 C C    . PRO B 2 96  ? -13.92500 -13.94200 -4.09600  1.000 33.07025  ? 96  PRO B C    1 
ATOM   6017 O O    . PRO B 2 96  ? -14.91900 -13.22100 -3.96600  1.000 36.96800  ? 96  PRO B O    1 
ATOM   6018 C CB   . PRO B 2 96  ? -14.67000 -16.20600 -4.87200  1.000 41.74469  ? 96  PRO B CB   1 
ATOM   6019 C CG   . PRO B 2 96  ? -13.66500 -17.14800 -4.35900  1.000 44.32393  ? 96  PRO B CG   1 
ATOM   6020 C CD   . PRO B 2 96  ? -12.39700 -16.87200 -5.15200  1.000 34.37960  ? 96  PRO B CD   1 
ATOM   6021 H HA   . PRO B 2 96  ? -14.24400 -14.53400 -6.01500  1.000 42.90326  ? 96  PRO B HA   1 
ATOM   6022 H HB2  . PRO B 2 96  ? -15.33400 -16.00800 -4.19300  1.000 50.09443  ? 96  PRO B HB2  1 
ATOM   6023 H HB3  . PRO B 2 96  ? -15.09000 -16.55400 -5.67400  1.000 50.09443  ? 96  PRO B HB3  1 
ATOM   6024 H HG2  . PRO B 2 96  ? -13.51900 -16.98500 -3.41400  1.000 53.18951  ? 96  PRO B HG2  1 
ATOM   6025 H HG3  . PRO B 2 96  ? -13.96800 -18.05800 -4.50500  1.000 53.18951  ? 96  PRO B HG3  1 
ATOM   6026 H HD2  . PRO B 2 96  ? -11.61300 -17.03900 -4.60600  1.000 41.25632  ? 96  PRO B HD2  1 
ATOM   6027 H HD3  . PRO B 2 96  ? -12.38500 -17.39700 -5.96700  1.000 41.25632  ? 96  PRO B HD3  1 
ATOM   6028 N N    . LYS B 2 97  ? -12.88000 -13.86900 -3.27500  1.000 31.74357  ? 97  LYS B N    1 
ATOM   6029 C CA   . LYS B 2 97  ? -12.80800 -12.91500 -2.18600  1.000 34.37616  ? 97  LYS B CA   1 
ATOM   6030 C C    . LYS B 2 97  ? -12.09100 -11.62500 -2.56700  1.000 35.04697  ? 97  LYS B C    1 
ATOM   6031 O O    . LYS B 2 97  ? -11.76200 -10.84800 -1.67500  1.000 32.06085  ? 97  LYS B O    1 
ATOM   6032 C CB   . LYS B 2 97  ? -12.08700 -13.55400 -0.99100  1.000 36.44866  ? 97  LYS B CB   1 
ATOM   6033 C CG   . LYS B 2 97  ? -12.82300 -14.77300 -0.42500  1.000 42.68662  ? 97  LYS B CG   1 
ATOM   6034 C CD   . LYS B 2 97  ? -11.95900 -15.48700 0.62100   1.000 49.25861  ? 97  LYS B CD   1 
ATOM   6035 C CE   . LYS B 2 97  ? -12.62300 -16.75500 1.15200   1.000 57.75399  ? 97  LYS B CE   1 
ATOM   6036 N NZ   . LYS B 2 97  ? -13.48200 -16.44300 2.32900   1.000 71.02790  ? 97  LYS B NZ   1 
ATOM   6037 H H    . LYS B 2 97  ? -12.18700 -14.37500 -3.33300  1.000 38.09309  ? 97  LYS B H    1 
ATOM   6038 H HA   . LYS B 2 97  ? -13.70800 -12.68600 -1.90500  1.000 41.25220  ? 97  LYS B HA   1 
ATOM   6039 H HB2  . LYS B 2 97  ? -11.20500 -13.84200 -1.27300  1.000 43.73919  ? 97  LYS B HB2  1 
ATOM   6040 H HB3  . LYS B 2 97  ? -12.00900 -12.89700 -0.28200  1.000 43.73919  ? 97  LYS B HB3  1 
ATOM   6041 H HG2  . LYS B 2 97  ? -13.64500 -14.48500 0.00100   1.000 51.22475  ? 97  LYS B HG2  1 
ATOM   6042 H HG3  . LYS B 2 97  ? -13.01400 -15.39700 -1.14200  1.000 51.22475  ? 97  LYS B HG3  1 
ATOM   6043 H HD2  . LYS B 2 97  ? -11.11300 -15.73600 0.21800   1.000 59.11114  ? 97  LYS B HD2  1 
ATOM   6044 H HD3  . LYS B 2 97  ? -11.80800 -14.88900 1.37000   1.000 59.11114  ? 97  LYS B HD3  1 
ATOM   6045 H HE2  . LYS B 2 97  ? -13.18100 -17.14200 0.45900   1.000 69.30559  ? 97  LYS B HE2  1 
ATOM   6046 H HE3  . LYS B 2 97  ? -11.94000 -17.38600 1.42900   1.000 69.30559  ? 97  LYS B HE3  1 
ATOM   6047 H HZ1  . LYS B 2 97  ? -13.86500 -17.18700 2.63200   1.000 85.23428  ? 97  LYS B HZ1  1 
ATOM   6048 H HZ2  . LYS B 2 97  ? -12.98900 -16.08600 2.97900   1.000 85.23428  ? 97  LYS B HZ2  1 
ATOM   6049 H HZ3  . LYS B 2 97  ? -14.11700 -15.86500 2.09700   1.000 85.23428  ? 97  LYS B HZ3  1 
ATOM   6050 N N    . THR B 2 98  ? -11.79800 -11.39700 -3.85600  1.000 30.03793  ? 98  THR B N    1 
ATOM   6051 C CA   . THR B 2 98  ? -11.05100 -10.19700 -4.25900  1.000 31.69688  ? 98  THR B CA   1 
ATOM   6052 C C    . THR B 2 98  ? -11.83000 -8.97600  -3.80000  1.000 28.78050  ? 98  THR B C    1 
ATOM   6053 O O    . THR B 2 98  ? -13.01600 -8.84900  -4.16800  1.000 32.04894  ? 98  THR B O    1 
ATOM   6054 C CB   . THR B 2 98  ? -10.89200 -10.13000 -5.78500  1.000 32.54343  ? 98  THR B CB   1 
ATOM   6055 O OG1  . THR B 2 98  ? -10.28400 -11.32600 -6.28000  1.000 31.47537  ? 98  THR B OG1  1 
ATOM   6056 C CG2  . THR B 2 98  ? -10.06600 -8.89600  -6.22900  1.000 30.07164  ? 98  THR B CG2  1 
ATOM   6057 H H    . THR B 2 98  ? -12.01700 -11.91400 -4.50700  1.000 36.04631  ? 98  THR B H    1 
ATOM   6058 H HA   . THR B 2 98  ? -10.17100 -10.20900 -3.85500  1.000 38.03705  ? 98  THR B HA   1 
ATOM   6059 H HB   . THR B 2 98  ? -11.77300 -10.04700 -6.18200  1.000 39.05291  ? 98  THR B HB   1 
ATOM   6060 H HG1  . THR B 2 98  ? -10.80200 -11.97800 -6.16700  1.000 37.77125  ? 98  THR B HG1  1 
ATOM   6061 H HG21 . THR B 2 98  ? -9.88500  -8.94500  -7.18100  1.000 36.08676  ? 98  THR B HG21 1 
ATOM   6062 H HG22 . THR B 2 98  ? -10.55800 -8.08100  -6.04500  1.000 36.08676  ? 98  THR B HG22 1 
ATOM   6063 H HG23 . THR B 2 98  ? -9.22300  -8.87200  -5.75000  1.000 36.08676  ? 98  THR B HG23 1 
ATOM   6064 N N    . PRO B 2 99  ? -11.24700 -8.07500  -3.01600  1.000 25.81923  ? 99  PRO B N    1 
ATOM   6065 C CA   . PRO B 2 99  ? -11.97600 -6.86900  -2.59200  1.000 28.20976  ? 99  PRO B CA   1 
ATOM   6066 C C    . PRO B 2 99  ? -11.85300 -5.80100  -3.65500  1.000 28.16345  ? 99  PRO B C    1 
ATOM   6067 O O    . PRO B 2 99  ? -11.11000 -5.95400  -4.59300  1.000 29.53930  ? 99  PRO B O    1 
ATOM   6068 C CB   . PRO B 2 99  ? -11.25600 -6.44400  -1.29900  1.000 28.86098  ? 99  PRO B CB   1 
ATOM   6069 C CG   . PRO B 2 99  ? -9.78400  -6.84900  -1.60000  1.000 26.06653  ? 99  PRO B CG   1 
ATOM   6070 C CD   . PRO B 2 99  ? -9.90100  -8.16400  -2.39000  1.000 30.83524  ? 99  PRO B CD   1 
ATOM   6071 H HA   . PRO B 2 99  ? -12.90900 -7.06400  -2.41100  1.000 33.85251  ? 99  PRO B HA   1 
ATOM   6072 H HB2  . PRO B 2 99  ? -11.33800 -5.48600  -1.16800  1.000 34.63398  ? 99  PRO B HB2  1 
ATOM   6073 H HB3  . PRO B 2 99  ? -11.60900 -6.93600  -0.54100  1.000 34.63398  ? 99  PRO B HB3  1 
ATOM   6074 H HG2  . PRO B 2 99  ? -9.35700  -6.16200  -2.13500  1.000 31.28063  ? 99  PRO B HG2  1 
ATOM   6075 H HG3  . PRO B 2 99  ? -9.30400  -6.98800  -0.76800  1.000 31.28063  ? 99  PRO B HG3  1 
ATOM   6076 H HD2  . PRO B 2 99  ? -9.21300  -8.21200  -3.07200  1.000 37.00309  ? 99  PRO B HD2  1 
ATOM   6077 H HD3  . PRO B 2 99  ? -9.86100  -8.92300  -1.78800  1.000 37.00309  ? 99  PRO B HD3  1 
ATOM   6078 N N    . LYS B 2 100 ? -12.61600 -4.71700  -3.50600  1.000 29.61848  ? 100 LYS B N    1 
ATOM   6079 C CA   . LYS B 2 100 ? -12.35400 -3.54400  -4.33700  1.000 33.45705  ? 100 LYS B CA   1 
ATOM   6080 C C    . LYS B 2 100 ? -10.96400 -3.02700  -3.93300  1.000 27.73887  ? 100 LYS B C    1 
ATOM   6081 O O    . LYS B 2 100 ? -10.67900 -2.86500  -2.74400  1.000 25.98373  ? 100 LYS B O    1 
ATOM   6082 C CB   . LYS B 2 100 ? -13.46600 -2.48800  -4.12600  1.000 37.86208  ? 100 LYS B CB   1 
ATOM   6083 C CG   . LYS B 2 100 ? -13.22000 -1.11700  -4.72100  1.000 44.53440  ? 100 LYS B CG   1 
ATOM   6084 C CD   . LYS B 2 100 ? -14.50300 -0.24900  -4.74200  1.000 55.35818  ? 100 LYS B CD   1 
ATOM   6085 C CE   . LYS B 2 100 ? -14.21800 1.20800   -5.17400  1.000 55.05467  ? 100 LYS B CE   1 
ATOM   6086 N NZ   . LYS B 2 100 ? -13.50400 1.25300   -6.47600  1.000 56.87581  ? 100 LYS B NZ   1 
ATOM   6087 H H    . LYS B 2 100 ? -13.26800 -4.63600  -2.95200  1.000 35.54298  ? 100 LYS B H    1 
ATOM   6088 H HA   . LYS B 2 100 ? -12.33500 -3.79900  -5.27300  1.000 40.14926  ? 100 LYS B HA   1 
ATOM   6089 H HB2  . LYS B 2 100 ? -14.28500 -2.82800  -4.51800  1.000 45.43529  ? 100 LYS B HB2  1 
ATOM   6090 H HB3  . LYS B 2 100 ? -13.59300 -2.36800  -3.17200  1.000 45.43529  ? 100 LYS B HB3  1 
ATOM   6091 H HG2  . LYS B 2 100 ? -12.55200 -0.65500  -4.19000  1.000 53.44208  ? 100 LYS B HG2  1 
ATOM   6092 H HG3  . LYS B 2 100 ? -12.90900 -1.21800  -5.63400  1.000 53.44208  ? 100 LYS B HG3  1 
ATOM   6093 H HD2  . LYS B 2 100 ? -15.13500 -0.63200  -5.37000  1.000 66.43062  ? 100 LYS B HD2  1 
ATOM   6094 H HD3  . LYS B 2 100 ? -14.88800 -0.23000  -3.85200  1.000 66.43062  ? 100 LYS B HD3  1 
ATOM   6095 H HE2  . LYS B 2 100 ? -15.05700 1.68400   -5.27000  1.000 66.06641  ? 100 LYS B HE2  1 
ATOM   6096 H HE3  . LYS B 2 100 ? -13.66100 1.63800   -4.50600  1.000 66.06641  ? 100 LYS B HE3  1 
ATOM   6097 H HZ1  . LYS B 2 100 ? -13.37200 2.09800   -6.72100  1.000 68.25177  ? 100 LYS B HZ1  1 
ATOM   6098 H HZ2  . LYS B 2 100 ? -12.71600 0.84600   -6.40500  1.000 68.25177  ? 100 LYS B HZ2  1 
ATOM   6099 H HZ3  . LYS B 2 100 ? -13.98600 0.84300   -7.10100  1.000 68.25177  ? 100 LYS B HZ3  1 
ATOM   6100 N N    . TYR B 2 101 ? -10.06100 -2.88000  -4.89900  1.000 26.35509  ? 101 TYR B N    1 
ATOM   6101 C CA   . TYR B 2 101 ? -8.69000  -2.54800  -4.51700  1.000 27.92123  ? 101 TYR B CA   1 
ATOM   6102 C C    . TYR B 2 101 ? -8.00200  -1.79900  -5.64600  1.000 26.60587  ? 101 TYR B C    1 
ATOM   6103 O O    . TYR B 2 101 ? -8.46600  -1.77400  -6.78700  1.000 27.91586  ? 101 TYR B O    1 
ATOM   6104 C CB   . TYR B 2 101 ? -7.82100  -3.79800  -4.22400  1.000 25.52888  ? 101 TYR B CB   1 
ATOM   6105 C CG   . TYR B 2 101 ? -7.39700  -4.52400  -5.48900  1.000 26.55129  ? 101 TYR B CG   1 
ATOM   6106 C CD1  . TYR B 2 101 ? -8.23000  -5.48500  -6.08600  1.000 30.44032  ? 101 TYR B CD1  1 
ATOM   6107 C CD2  . TYR B 2 101 ? -6.16600  -4.23400  -6.13000  1.000 27.06673  ? 101 TYR B CD2  1 
ATOM   6108 C CE1  . TYR B 2 101 ? -7.84600  -6.15600  -7.24000  1.000 28.00874  ? 101 TYR B CE1  1 
ATOM   6109 C CE2  . TYR B 2 101 ? -5.79500  -4.88500  -7.30000  1.000 28.51498  ? 101 TYR B CE2  1 
ATOM   6110 C CZ   . TYR B 2 101 ? -6.63900  -5.83800  -7.85900  1.000 28.71667  ? 101 TYR B CZ   1 
ATOM   6111 O OH   . TYR B 2 101 ? -6.25600  -6.51000  -8.99300  1.000 29.89143  ? 101 TYR B OH   1 
ATOM   6112 H H    . TYR B 2 101 ? -10.20400 -2.96200  -5.74300  1.000 31.62691  ? 101 TYR B H    1 
ATOM   6113 H HA   . TYR B 2 101 ? -8.69700  -1.98100  -3.73100  1.000 33.50628  ? 101 TYR B HA   1 
ATOM   6114 H HB2  . TYR B 2 101 ? -7.01900  -3.52300  -3.75300  1.000 30.63545  ? 101 TYR B HB2  1 
ATOM   6115 H HB3  . TYR B 2 101 ? -8.33100  -4.41700  -3.67900  1.000 30.63545  ? 101 TYR B HB3  1 
ATOM   6116 H HD1  . TYR B 2 101 ? -9.04100  -5.69800  -5.68400  1.000 36.52918  ? 101 TYR B HD1  1 
ATOM   6117 H HD2  . TYR B 2 101 ? -5.60100  -3.59100  -5.76600  1.000 32.48088  ? 101 TYR B HD2  1 
ATOM   6118 H HE1  . TYR B 2 101 ? -8.40900  -6.79200  -7.61800  1.000 33.61129  ? 101 TYR B HE1  1 
ATOM   6119 H HE2  . TYR B 2 101 ? -4.98000  -4.69100  -7.70300  1.000 34.21877  ? 101 TYR B HE2  1 
ATOM   6120 H HH   . TYR B 2 101 ? -6.83800  -7.08000  -9.20000  1.000 35.87052  ? 101 TYR B HH   1 
ATOM   6121 N N    . LYS B 2 102 ? -6.89000  -1.16600  -5.29500  1.000 26.59666  ? 102 LYS B N    1 
ATOM   6122 C CA   . LYS B 2 102 ? -5.96300  -0.66300  -6.29800  1.000 26.01135  ? 102 LYS B CA   1 
ATOM   6123 C C    . LYS B 2 102 ? -4.55100  -0.69700  -5.71400  1.000 28.02570  ? 102 LYS B C    1 
ATOM   6124 O O    . LYS B 2 102 ? -4.35100  -0.85200  -4.49600  1.000 23.93688  ? 102 LYS B O    1 
ATOM   6125 C CB   . LYS B 2 102 ? -6.33800  0.76600   -6.76300  1.000 31.86010  ? 102 LYS B CB   1 
ATOM   6126 C CG   . LYS B 2 102 ? -6.27700  1.78400   -5.64700  1.000 36.76367  ? 102 LYS B CG   1 
ATOM   6127 C CD   . LYS B 2 102 ? -6.74500  3.17300   -6.11500  1.000 42.83118  ? 102 LYS B CD   1 
ATOM   6128 C CE   . LYS B 2 102 ? -6.71600  4.13600   -4.92700  1.000 45.11018  ? 102 LYS B CE   1 
ATOM   6129 N NZ   . LYS B 2 102 ? -7.82600  3.88900   -3.95000  1.000 62.67117  ? 102 LYS B NZ   1 
ATOM   6130 H H    . LYS B 2 102 ? -6.64900  -1.01500  -4.48300  1.000 31.91679  ? 102 LYS B H    1 
ATOM   6131 H HA   . LYS B 2 102 ? -5.98400  -1.24700  -7.07200  1.000 31.21443  ? 102 LYS B HA   1 
ATOM   6132 H HB2  . LYS B 2 102 ? -5.71900  1.04500   -7.45600  1.000 38.23292  ? 102 LYS B HB2  1 
ATOM   6133 H HB3  . LYS B 2 102 ? -7.24300  0.75700   -7.11100  1.000 38.23292  ? 102 LYS B HB3  1 
ATOM   6134 H HG2  . LYS B 2 102 ? -6.85400  1.49800   -4.92200  1.000 44.11720  ? 102 LYS B HG2  1 
ATOM   6135 H HG3  . LYS B 2 102 ? -5.36200  1.86400   -5.33500  1.000 44.11720  ? 102 LYS B HG3  1 
ATOM   6136 H HD2  . LYS B 2 102 ? -6.14600  3.50700   -6.80100  1.000 51.39822  ? 102 LYS B HD2  1 
ATOM   6137 H HD3  . LYS B 2 102 ? -7.65400  3.11700   -6.44900  1.000 51.39822  ? 102 LYS B HD3  1 
ATOM   6138 H HE2  . LYS B 2 102 ? -5.87400  4.03200   -4.45700  1.000 54.13302  ? 102 LYS B HE2  1 
ATOM   6139 H HE3  . LYS B 2 102 ? -6.80200  5.04500   -5.25500  1.000 54.13302  ? 102 LYS B HE3  1 
ATOM   6140 H HZ1  . LYS B 2 102 ? -7.75300  4.44700   -3.26000  1.000 75.20621  ? 102 LYS B HZ1  1 
ATOM   6141 H HZ2  . LYS B 2 102 ? -8.61300  4.01900   -4.34500  1.000 75.20621  ? 102 LYS B HZ2  1 
ATOM   6142 H HZ3  . LYS B 2 102 ? -7.78700  3.05200   -3.65000  1.000 75.20621  ? 102 LYS B HZ3  1 
ATOM   6143 N N    . PHE B 2 103 ? -3.56000  -0.53400  -6.60400  1.000 28.24993  ? 103 PHE B N    1 
ATOM   6144 C CA   . PHE B 2 103 ? -2.15800  -0.40700  -6.21400  1.000 28.01168  ? 103 PHE B CA   1 
ATOM   6145 C C    . PHE B 2 103 ? -1.77800  1.07000   -6.14200  1.000 28.87538  ? 103 PHE B C    1 
ATOM   6146 O O    . PHE B 2 103 ? -2.05800  1.83200   -7.07500  1.000 28.88232  ? 103 PHE B O    1 
ATOM   6147 C CB   . PHE B 2 103 ? -1.25200  -1.10500  -7.24400  1.000 26.23926  ? 103 PHE B CB   1 
ATOM   6148 C CG   . PHE B 2 103 ? -1.40700  -2.61000  -7.28500  1.000 28.14652  ? 103 PHE B CG   1 
ATOM   6149 C CD1  . PHE B 2 103 ? -2.05300  -3.29700  -6.24200  1.000 28.08547  ? 103 PHE B CD1  1 
ATOM   6150 C CD2  . PHE B 2 103 ? -0.92100  -3.33900  -8.39200  1.000 29.74961  ? 103 PHE B CD2  1 
ATOM   6151 C CE1  . PHE B 2 103 ? -2.17700  -4.70000  -6.28200  1.000 26.01509  ? 103 PHE B CE1  1 
ATOM   6152 C CE2  . PHE B 2 103 ? -1.02700  -4.73100  -8.43200  1.000 30.03255  ? 103 PHE B CE2  1 
ATOM   6153 C CZ   . PHE B 2 103 ? -1.66000  -5.40900  -7.36900  1.000 29.53712  ? 103 PHE B CZ   1 
ATOM   6154 H H    . PHE B 2 103 ? -3.68300  -0.49400  -7.45400  1.000 33.90071  ? 103 PHE B H    1 
ATOM   6155 H HA   . PHE B 2 103 ? -2.01600  -0.80000  -5.33900  1.000 33.61481  ? 103 PHE B HA   1 
ATOM   6156 H HB2  . PHE B 2 103 ? -1.46200  -0.76200  -8.12700  1.000 31.48791  ? 103 PHE B HB2  1 
ATOM   6157 H HB3  . PHE B 2 103 ? -0.32700  -0.90900  -7.02800  1.000 31.48791  ? 103 PHE B HB3  1 
ATOM   6158 H HD1  . PHE B 2 103 ? -2.37900  -2.82900  -5.50800  1.000 33.70337  ? 103 PHE B HD1  1 
ATOM   6159 H HD2  . PHE B 2 103 ? -0.48600  -2.89100  -9.08100  1.000 35.70034  ? 103 PHE B HD2  1 
ATOM   6160 H HE1  . PHE B 2 103 ? -2.59500  -5.15200  -5.58500  1.000 31.21891  ? 103 PHE B HE1  1 
ATOM   6161 H HE2  . PHE B 2 103 ? -0.69800  -5.20600  -9.16100  1.000 36.03986  ? 103 PHE B HE2  1 
ATOM   6162 H HZ   . PHE B 2 103 ? -1.75500  -6.33300  -7.40400  1.000 35.44534  ? 103 PHE B HZ   1 
ATOM   6163 N N    . VAL B 2 104 ? -1.12000  1.47600   -5.06100  1.000 26.79999  ? 104 VAL B N    1 
ATOM   6164 C CA   . VAL B 2 104 ? -0.70000  2.86300   -4.92000  1.000 27.06494  ? 104 VAL B CA   1 
ATOM   6165 C C    . VAL B 2 104 ? 0.72200   2.85000   -4.40500  1.000 32.24840  ? 104 VAL B C    1 
ATOM   6166 O O    . VAL B 2 104 ? 1.15200   1.90200   -3.72900  1.000 32.13227  ? 104 VAL B O    1 
ATOM   6167 C CB   . VAL B 2 104 ? -1.58000  3.69700   -3.96600  1.000 31.94068  ? 104 VAL B CB   1 
ATOM   6168 C CG1  . VAL B 2 104 ? -3.03300  3.70000   -4.44200  1.000 32.21144  ? 104 VAL B CG1  1 
ATOM   6169 C CG2  . VAL B 2 104 ? -1.42100  3.16600   -2.57500  1.000 34.33780  ? 104 VAL B CG2  1 
ATOM   6170 H H    . VAL B 2 104 ? -0.90600  0.97000   -4.39900  1.000 32.16079  ? 104 VAL B H    1 
ATOM   6171 H HA   . VAL B 2 104 ? -0.70200  3.29300   -5.78900  1.000 32.47873  ? 104 VAL B HA   1 
ATOM   6172 H HB   . VAL B 2 104 ? -1.26400  4.61400   -3.97100  1.000 38.32962  ? 104 VAL B HB   1 
ATOM   6173 H HG11 . VAL B 2 104 ? -3.56200  4.24400   -3.83700  1.000 38.65453  ? 104 VAL B HG11 1 
ATOM   6174 H HG12 . VAL B 2 104 ? -3.07000  4.06900   -5.33800  1.000 38.65453  ? 104 VAL B HG12 1 
ATOM   6175 H HG13 . VAL B 2 104 ? -3.36600  2.78900   -4.44500  1.000 38.65453  ? 104 VAL B HG13 1 
ATOM   6176 H HG21 . VAL B 2 104 ? -2.15600  3.49000   -2.03100  1.000 41.20617  ? 104 VAL B HG21 1 
ATOM   6177 H HG22 . VAL B 2 104 ? -1.43200  2.19700   -2.60200  1.000 41.20617  ? 104 VAL B HG22 1 
ATOM   6178 H HG23 . VAL B 2 104 ? -0.58000  3.47800   -2.20600  1.000 41.20617  ? 104 VAL B HG23 1 
ATOM   6179 N N    . ARG B 2 105 ? 1.49000   3.85000   -4.81300  1.000 26.89098  ? 105 ARG B N    1 
ATOM   6180 C CA   . ARG B 2 105 ? 2.82700   4.03200   -4.25500  1.000 29.09179  ? 105 ARG B CA   1 
ATOM   6181 C C    . ARG B 2 105 ? 2.76100   5.15800   -3.24100  1.000 29.94437  ? 105 ARG B C    1 
ATOM   6182 O O    . ARG B 2 105 ? 2.30700   6.25000   -3.57900  1.000 34.29073  ? 105 ARG B O    1 
ATOM   6183 C CB   . ARG B 2 105 ? 3.84600   4.32300   -5.37300  1.000 31.15844  ? 105 ARG B CB   1 
ATOM   6184 C CG   . ARG B 2 105 ? 5.25200   4.45700   -4.82700  1.000 30.96728  ? 105 ARG B CG   1 
ATOM   6185 C CD   . ARG B 2 105 ? 6.27000   4.50800   -5.93900  1.000 35.15168  ? 105 ARG B CD   1 
ATOM   6186 N NE   . ARG B 2 105 ? 7.60300   4.67000   -5.38000  1.000 35.86648  ? 105 ARG B NE   1 
ATOM   6187 C CZ   . ARG B 2 105 ? 8.42300   3.68000   -5.04400  1.000 39.07173  ? 105 ARG B CZ   1 
ATOM   6188 N NH1  . ARG B 2 105 ? 8.05800   2.40400   -5.15400  1.000 33.21306  ? 105 ARG B NH1  1 
ATOM   6189 N NH2  . ARG B 2 105 ? 9.65500   3.98000   -4.61100  1.000 41.65232  ? 105 ARG B NH2  1 
ATOM   6190 H H    . ARG B 2 105 ? 1.26700   4.43200   -5.40500  1.000 32.26997  ? 105 ARG B H    1 
ATOM   6191 H HA   . ARG B 2 105 ? 3.10400   3.22400   -3.79600  1.000 34.91095  ? 105 ARG B HA   1 
ATOM   6192 H HB2  . ARG B 2 105 ? 3.83700   3.59300   -6.01200  1.000 37.39092  ? 105 ARG B HB2  1 
ATOM   6193 H HB3  . ARG B 2 105 ? 3.61000   5.15500   -5.81200  1.000 37.39092  ? 105 ARG B HB3  1 
ATOM   6194 H HG2  . ARG B 2 105 ? 5.32100   5.27800   -4.31400  1.000 37.16153  ? 105 ARG B HG2  1 
ATOM   6195 H HG3  . ARG B 2 105 ? 5.45200   3.69200   -4.26600  1.000 37.16153  ? 105 ARG B HG3  1 
ATOM   6196 H HD2  . ARG B 2 105 ? 6.24000   3.68400   -6.44900  1.000 42.18282  ? 105 ARG B HD2  1 
ATOM   6197 H HD3  . ARG B 2 105 ? 6.08400   5.26800   -6.51200  1.000 42.18282  ? 105 ARG B HD3  1 
ATOM   6198 H HE   . ARG B 2 105 ? 7.88400   5.47300   -5.25700  1.000 43.04058  ? 105 ARG B HE   1 
ATOM   6199 H HH11 . ARG B 2 105 ? 7.27200   2.20200   -5.43600  1.000 39.85647  ? 105 ARG B HH11 1 
ATOM   6200 H HH12 . ARG B 2 105 ? 8.60700   1.78100   -4.93200  1.000 39.85647  ? 105 ARG B HH12 1 
ATOM   6201 H HH21 . ARG B 2 105 ? 9.89700   4.80200   -4.53900  1.000 49.98358  ? 105 ARG B HH21 1 
ATOM   6202 H HH22 . ARG B 2 105 ? 10.19800  3.35100   -4.38900  1.000 49.98358  ? 105 ARG B HH22 1 
ATOM   6203 N N    . ILE B 2 106 ? 3.19100   4.91000   -1.99600  1.000 30.03714  ? 106 ILE B N    1 
ATOM   6204 C CA   . ILE B 2 106 ? 3.07400   5.94400   -0.97800  1.000 29.19731  ? 106 ILE B CA   1 
ATOM   6205 C C    . ILE B 2 106 ? 4.35400   6.77800   -0.87400  1.000 36.31035  ? 106 ILE B C    1 
ATOM   6206 O O    . ILE B 2 106 ? 5.41100   6.46000   -1.43700  1.000 31.23109  ? 106 ILE B O    1 
ATOM   6207 C CB   . ILE B 2 106 ? 2.68800   5.37300   0.39500   1.000 29.17446  ? 106 ILE B CB   1 
ATOM   6208 C CG1  . ILE B 2 106 ? 3.69600   4.31600   0.88500   1.000 31.76157  ? 106 ILE B CG1  1 
ATOM   6209 C CG2  . ILE B 2 106 ? 1.18700   4.91100   0.34100   1.000 33.55970  ? 106 ILE B CG2  1 
ATOM   6210 C CD1  . ILE B 2 106 ? 3.53300   3.93800   2.38900   1.000 34.19065  ? 106 ILE B CD1  1 
ATOM   6211 H H    . ILE B 2 106 ? 3.54300   4.17200   -1.72900  1.000 36.04537  ? 106 ILE B H    1 
ATOM   6212 H HA   . ILE B 2 106 ? 2.36200   6.54900   -1.23900  1.000 35.03758  ? 106 ILE B HA   1 
ATOM   6213 H HB   . ILE B 2 106 ? 2.73000   6.10800   1.02600   1.000 35.01015  ? 106 ILE B HB   1 
ATOM   6214 H HG12 . ILE B 2 106 ? 3.57800   3.50700   0.36300   1.000 38.11468  ? 106 ILE B HG12 1 
ATOM   6215 H HG13 . ILE B 2 106 ? 4.59600   4.65700   0.76300   1.000 38.11468  ? 106 ILE B HG13 1 
ATOM   6216 H HG21 . ILE B 2 106 ? 0.93700   4.54800   1.20500   1.000 40.27244  ? 106 ILE B HG21 1 
ATOM   6217 H HG22 . ILE B 2 106 ? 0.62900   5.67600   0.12900   1.000 40.27244  ? 106 ILE B HG22 1 
ATOM   6218 H HG23 . ILE B 2 106 ? 1.09100   4.23100   -0.34400  1.000 40.27244  ? 106 ILE B HG23 1 
ATOM   6219 H HD11 . ILE B 2 106 ? 4.20600   3.28000   2.62300   1.000 41.02959  ? 106 ILE B HD11 1 
ATOM   6220 H HD12 . ILE B 2 106 ? 3.64700   4.73600   2.92900   1.000 41.02959  ? 106 ILE B HD12 1 
ATOM   6221 H HD13 . ILE B 2 106 ? 2.64700   3.56900   2.52700   1.000 41.02959  ? 106 ILE B HD13 1 
ATOM   6222 N N    . GLN B 2 107 ? 4.21800   7.91100   -0.20100  1.000 31.97326  ? 107 GLN B N    1 
ATOM   6223 C CA   . GLN B 2 107 ? 5.34400   8.80500   0.06000   1.000 37.01414  ? 107 GLN B CA   1 
ATOM   6224 C C    . GLN B 2 107 ? 5.87600   8.57300   1.46400   1.000 33.88324  ? 107 GLN B C    1 
ATOM   6225 O O    . GLN B 2 107 ? 5.13600   8.14100   2.36600   1.000 30.86375  ? 107 GLN B O    1 
ATOM   6226 C CB   . GLN B 2 107 ? 4.92500   10.27200  -0.06700  1.000 41.45044  ? 107 GLN B CB   1 
ATOM   6227 C CG   . GLN B 2 107 ? 4.31700   10.67600  -1.41900  1.000 47.74014  ? 107 GLN B CG   1 
ATOM   6228 C CD   . GLN B 2 107 ? 5.28300   10.60600  -2.58200  1.000 59.79201  ? 107 GLN B CD   1 
ATOM   6229 O OE1  . GLN B 2 107 ? 6.44900   11.02300  -2.48000  1.000 56.97241  ? 107 GLN B OE1  1 
ATOM   6230 N NE2  . GLN B 2 107 ? 4.79500   10.08500  -3.72300  1.000 62.31553  ? 107 GLN B NE2  1 
ATOM   6231 H H    . GLN B 2 107 ? 3.47200   8.19200   0.12200   1.000 38.36872  ? 107 GLN B H    1 
ATOM   6232 H HA   . GLN B 2 107 ? 6.04400   8.62600   -0.58600  1.000 44.41777  ? 107 GLN B HA   1 
ATOM   6233 H HB2  . GLN B 2 107 ? 4.26300   10.46100  0.61700   1.000 49.74133  ? 107 GLN B HB2  1 
ATOM   6234 H HB3  . GLN B 2 107 ? 5.70600   10.82800  0.07700   1.000 49.74133  ? 107 GLN B HB3  1 
ATOM   6235 H HG2  . GLN B 2 107 ? 3.57500   10.08300  -1.61600  1.000 57.28897  ? 107 GLN B HG2  1 
ATOM   6236 H HG3  . GLN B 2 107 ? 3.99800   11.59000  -1.35600  1.000 57.28897  ? 107 GLN B HG3  1 
ATOM   6237 H HE21 . GLN B 2 107 ? 3.98100   9.80900   -3.75600  1.000 74.77943  ? 107 GLN B HE21 1 
ATOM   6238 H HE22 . GLN B 2 107 ? 5.29900   10.02200  -4.41700  1.000 74.77943  ? 107 GLN B HE22 1 
ATOM   6239 N N    . PRO B 2 108 ? 7.14400   8.89100   1.68600   1.000 31.66114  ? 108 PRO B N    1 
ATOM   6240 C CA   . PRO B 2 108 ? 7.68300   8.83800   3.04600   1.000 29.96355  ? 108 PRO B CA   1 
ATOM   6241 C C    . PRO B 2 108 ? 6.86200   9.71000   3.98700   1.000 33.67732  ? 108 PRO B C    1 
ATOM   6242 O O    . PRO B 2 108 ? 6.41800   10.80500  3.63100   1.000 31.45684  ? 108 PRO B O    1 
ATOM   6243 C CB   . PRO B 2 108 ? 9.13300   9.33800   2.87500   1.000 36.40550  ? 108 PRO B CB   1 
ATOM   6244 C CG   . PRO B 2 108 ? 9.25200   9.84000   1.54300   1.000 36.77844  ? 108 PRO B CG   1 
ATOM   6245 C CD   . PRO B 2 108 ? 8.16400   9.25100   0.68400   1.000 36.68803  ? 108 PRO B CD   1 
ATOM   6246 H HA   . PRO B 2 108 ? 7.69100   7.92500   3.37300   1.000 35.95706  ? 108 PRO B HA   1 
ATOM   6247 H HB2  . PRO B 2 108 ? 9.30700   10.04300  3.51800   1.000 43.68740  ? 108 PRO B HB2  1 
ATOM   6248 H HB3  . PRO B 2 108 ? 9.74600   8.59900   3.01200   1.000 43.68740  ? 108 PRO B HB3  1 
ATOM   6249 H HG2  . PRO B 2 108 ? 9.16900   10.80600  1.56300   1.000 44.13493  ? 108 PRO B HG2  1 
ATOM   6250 H HG3  . PRO B 2 108 ? 10.12100  9.59100   1.19100   1.000 44.13493  ? 108 PRO B HG3  1 
ATOM   6251 H HD2  . PRO B 2 108 ? 7.82300   9.91700   0.06700   1.000 44.02644  ? 108 PRO B HD2  1 
ATOM   6252 H HD3  . PRO B 2 108 ? 8.48300   8.46000   0.22100   1.000 44.02644  ? 108 PRO B HD3  1 
ATOM   6253 N N    . GLY B 2 109 ? 6.64100   9.20100   5.19100   1.000 30.11062  ? 109 GLY B N    1 
ATOM   6254 C CA   . GLY B 2 109 ? 5.77600   9.82200   6.16500   1.000 28.11661  ? 109 GLY B CA   1 
ATOM   6255 C C    . GLY B 2 109 ? 4.38600   9.23100   6.16800   1.000 30.80041  ? 109 GLY B C    1 
ATOM   6256 O O    . GLY B 2 109 ? 3.67600   9.32600   7.18200   1.000 33.33693  ? 109 GLY B O    1 
ATOM   6257 H H    . GLY B 2 109 ? 6.99700   8.47000   5.47100   1.000 36.13355  ? 109 GLY B H    1 
ATOM   6258 H HA2  . GLY B 2 109 ? 6.15700   9.71200   7.04900   1.000 33.74073  ? 109 GLY B HA2  1 
ATOM   6259 H HA3  . GLY B 2 109 ? 5.70500   10.77100  5.97800   1.000 33.74073  ? 109 GLY B HA3  1 
ATOM   6260 N N    . GLN B 2 110 ? 3.99400   8.58400   5.06800   1.000 28.28943  ? 110 GLN B N    1 
ATOM   6261 C CA   . GLN B 2 110 ? 2.67900   7.95100   5.02500   1.000 29.31199  ? 110 GLN B CA   1 
ATOM   6262 C C    . GLN B 2 110 ? 2.70300   6.64900   5.81100   1.000 27.31185  ? 110 GLN B C    1 
ATOM   6263 O O    . GLN B 2 110 ? 3.69900   5.93300   5.81900   1.000 27.15056  ? 110 GLN B O    1 
ATOM   6264 C CB   . GLN B 2 110 ? 2.24100   7.72500   3.56600   1.000 29.90641  ? 110 GLN B CB   1 
ATOM   6265 C CG   . GLN B 2 110 ? 0.88000   6.95200   3.48500   1.000 39.85956  ? 110 GLN B CG   1 
ATOM   6266 C CD   . GLN B 2 110 ? -0.27000  7.68600   4.23500   1.000 47.15106  ? 110 GLN B CD   1 
ATOM   6267 O OE1  . GLN B 2 110 ? -0.99300  7.09900   5.08700   1.000 33.13256  ? 110 GLN B OE1  1 
ATOM   6268 N NE2  . GLN B 2 110 ? -0.41500  8.98400   3.94500   1.000 50.90541  ? 110 GLN B NE2  1 
ATOM   6269 H H    . GLN B 2 110 ? 4.45900   8.49900   4.35000   1.000 33.94811  ? 110 GLN B H    1 
ATOM   6270 H HA   . GLN B 2 110 ? 2.03300   8.54100   5.44400   1.000 35.17519  ? 110 GLN B HA   1 
ATOM   6271 H HB2  . GLN B 2 110 ? 2.13000   8.58400   3.12900   1.000 35.88849  ? 110 GLN B HB2  1 
ATOM   6272 H HB3  . GLN B 2 110 ? 2.91600   7.20000   3.10800   1.000 35.88849  ? 110 GLN B HB3  1 
ATOM   6273 H HG2  . GLN B 2 110 ? 0.62200   6.87000   2.55400   1.000 47.83227  ? 110 GLN B HG2  1 
ATOM   6274 H HG3  . GLN B 2 110 ? 0.98400   6.07100   3.87700   1.000 47.83227  ? 110 GLN B HG3  1 
ATOM   6275 H HE21 . GLN B 2 110 ? 0.09900   9.35500   3.36300   1.000 61.08729  ? 110 GLN B HE21 1 
ATOM   6276 H HE22 . GLN B 2 110 ? -1.03200  9.44400   4.32900   1.000 61.08729  ? 110 GLN B HE22 1 
ATOM   6277 N N    . THR B 2 111 ? 1.60100   6.34900   6.49600   1.000 28.61618  ? 111 THR B N    1 
ATOM   6278 C CA   . THR B 2 111 ? 1.48900   5.12800   7.26800   1.000 26.17793  ? 111 THR B CA   1 
ATOM   6279 C C    . THR B 2 111 ? 0.62400   4.11100   6.52700   1.000 26.03662  ? 111 THR B C    1 
ATOM   6280 O O    . THR B 2 111 ? -0.14300  4.45000   5.62700   1.000 25.62747  ? 111 THR B O    1 
ATOM   6281 C CB   . THR B 2 111 ? 0.85100   5.42100   8.62200   1.000 26.37623  ? 111 THR B CB   1 
ATOM   6282 O OG1  . THR B 2 111 ? -0.42300  6.01000   8.36200   1.000 26.27834  ? 111 THR B OG1  1 
ATOM   6283 C CG2  . THR B 2 111 ? 1.75300   6.36100   9.47900   1.000 27.94931  ? 111 THR B CG2  1 
ATOM   6284 H H    . THR B 2 111 ? 0.90000   6.84600   6.52600   1.000 34.34022  ? 111 THR B H    1 
ATOM   6285 H HA   . THR B 2 111 ? 2.36500   4.74300   7.41300   1.000 31.41432  ? 111 THR B HA   1 
ATOM   6286 H HB   . THR B 2 111 ? 0.72800   4.59000   9.10600   1.000 31.65228  ? 111 THR B HB   1 
ATOM   6287 H HG1  . THR B 2 111 ? -0.81100  6.18600   9.08600   1.000 31.53481  ? 111 THR B HG1  1 
ATOM   6288 H HG21 . THR B 2 111 ? 1.29000   6.60900   10.29400  1.000 33.53997  ? 111 THR B HG21 1 
ATOM   6289 H HG22 . THR B 2 111 ? 2.57900   5.90800   9.71000   1.000 33.53997  ? 111 THR B HG22 1 
ATOM   6290 H HG23 . THR B 2 111 ? 1.96300   7.16500   8.98000   1.000 33.53997  ? 111 THR B HG23 1 
ATOM   6291 N N    . PHE B 2 112 ? 0.68400   2.86900   6.99800   1.000 25.38056  ? 112 PHE B N    1 
ATOM   6292 C CA   . PHE B 2 112 ? -0.12000  1.81400   6.43000   1.000 26.75325  ? 112 PHE B CA   1 
ATOM   6293 C C    . PHE B 2 112 ? -0.13200  0.64700   7.40100   1.000 25.51203  ? 112 PHE B C    1 
ATOM   6294 O O    . PHE B 2 112 ? 0.68100   0.57300   8.31900   1.000 25.05449  ? 112 PHE B O    1 
ATOM   6295 C CB   . PHE B 2 112 ? 0.42300   1.39700   5.05300   1.000 24.18873  ? 112 PHE B CB   1 
ATOM   6296 C CG   . PHE B 2 112 ? 1.86800   0.99700   5.06300   1.000 25.51050  ? 112 PHE B CG   1 
ATOM   6297 C CD1  . PHE B 2 112 ? 2.89400   1.94200   4.93800   1.000 27.93345  ? 112 PHE B CD1  1 
ATOM   6298 C CD2  . PHE B 2 112 ? 2.20800   -0.31200  5.19400   1.000 23.82996  ? 112 PHE B CD2  1 
ATOM   6299 C CE1  . PHE B 2 112 ? 4.26600   1.52800   4.89100   1.000 32.29332  ? 112 PHE B CE1  1 
ATOM   6300 C CE2  . PHE B 2 112 ? 3.52200   -0.75100  5.19900   1.000 29.33340  ? 112 PHE B CE2  1 
ATOM   6301 C CZ   . PHE B 2 112 ? 4.58600   0.17100   5.02900   1.000 29.44973  ? 112 PHE B CZ   1 
ATOM   6302 H H    . PHE B 2 112 ? 1.18700   2.61800   7.64900   1.000 30.45747  ? 112 PHE B H    1 
ATOM   6303 H HA   . PHE B 2 112 ? -1.03100  2.12800   6.31700   1.000 32.10470  ? 112 PHE B HA   1 
ATOM   6304 H HB2  . PHE B 2 112 ? -0.09100  0.64000   4.73100   1.000 29.02728  ? 112 PHE B HB2  1 
ATOM   6305 H HB3  . PHE B 2 112 ? 0.32700   2.14300   4.44100   1.000 29.02728  ? 112 PHE B HB3  1 
ATOM   6306 H HD1  . PHE B 2 112 ? 2.68000   2.84000   4.82400   1.000 33.52094  ? 112 PHE B HD1  1 
ATOM   6307 H HD2  . PHE B 2 112 ? 1.52900   -0.94100  5.28600   1.000 28.59675  ? 112 PHE B HD2  1 
ATOM   6308 H HE1  . PHE B 2 112 ? 4.94200   2.16100   4.80700   1.000 38.75278  ? 112 PHE B HE1  1 
ATOM   6309 H HE2  . PHE B 2 112 ? 3.70600   -1.65900  5.28100   1.000 35.20088  ? 112 PHE B HE2  1 
ATOM   6310 H HZ   . PHE B 2 112 ? 5.47000   -0.11500  5.03600   1.000 35.34048  ? 112 PHE B HZ   1 
ATOM   6311 N N    . SER B 2 113 ? -1.09100  -0.25400  7.20400   1.000 24.60580  ? 113 SER B N    1 
ATOM   6312 C CA   . SER B 2 113 ? -1.16800  -1.46500  8.00000   1.000 22.21084  ? 113 SER B CA   1 
ATOM   6313 C C    . SER B 2 113 ? -0.42100  -2.58800  7.31600   1.000 22.12951  ? 113 SER B C    1 
ATOM   6314 O O    . SER B 2 113 ? -0.57000  -2.79900  6.10700   1.000 23.81900  ? 113 SER B O    1 
ATOM   6315 C CB   . SER B 2 113 ? -2.62300  -1.88300  8.20200   1.000 26.17587  ? 113 SER B CB   1 
ATOM   6316 O OG   . SER B 2 113 ? -3.30100  -0.81000  8.87400   1.000 25.32528  ? 113 SER B OG   1 
ATOM   6317 H H    . SER B 2 113 ? -1.71000  -0.18300  6.61100   1.000 29.52776  ? 113 SER B H    1 
ATOM   6318 H HA   . SER B 2 113 ? -0.76800  -1.31100  8.87000   1.000 26.65381  ? 113 SER B HA   1 
ATOM   6319 H HB2  . SER B 2 113 ? -3.03900  -2.04100  7.34000   1.000 31.41185  ? 113 SER B HB2  1 
ATOM   6320 H HB3  . SER B 2 113 ? -2.65800  -2.68300  8.74900   1.000 31.41185  ? 113 SER B HB3  1 
ATOM   6321 H HG   . SER B 2 113 ? -2.93900  -0.66200  9.61700   1.000 30.39114  ? 113 SER B HG   1 
ATOM   6322 N N    . VAL B 2 114 ? 0.30800   -3.36700  8.11200   1.000 23.75097  ? 114 VAL B N    1 
ATOM   6323 C CA   . VAL B 2 114 ? 1.03100   -4.52100  7.60100   1.000 21.64636  ? 114 VAL B CA   1 
ATOM   6324 C C    . VAL B 2 114 ? 0.30800   -5.76500  8.08800   1.000 23.07188  ? 114 VAL B C    1 
ATOM   6325 O O    . VAL B 2 114 ? 0.08200   -5.92100  9.29000   1.000 23.42486  ? 114 VAL B O    1 
ATOM   6326 C CB   . VAL B 2 114 ? 2.48700   -4.54700  8.11000   1.000 25.23907  ? 114 VAL B CB   1 
ATOM   6327 C CG1  . VAL B 2 114 ? 3.15500   -5.87100  7.69000   1.000 27.79367  ? 114 VAL B CG1  1 
ATOM   6328 C CG2  . VAL B 2 114 ? 3.27400   -3.34900  7.56200   1.000 26.24035  ? 114 VAL B CG2  1 
ATOM   6329 H H    . VAL B 2 114 ? 0.39900   -3.24500  8.95800   1.000 28.50197  ? 114 VAL B H    1 
ATOM   6330 H HA   . VAL B 2 114 ? 1.03500   -4.51500  6.63100   1.000 25.97643  ? 114 VAL B HA   1 
ATOM   6331 H HB   . VAL B 2 114 ? 2.49000   -4.49700  9.07900   1.000 30.28769  ? 114 VAL B HB   1 
ATOM   6332 H HG11 . VAL B 2 114 ? 4.10700   -5.79200  7.84400   1.000 33.35321  ? 114 VAL B HG11 1 
ATOM   6333 H HG12 . VAL B 2 114 ? 2.79700   -6.59800  8.22400   1.000 33.35321  ? 114 VAL B HG12 1 
ATOM   6334 H HG13 . VAL B 2 114 ? 2.98200   -6.03000  6.74900   1.000 33.35321  ? 114 VAL B HG13 1 
ATOM   6335 H HG21 . VAL B 2 114 ? 4.18500   -3.39200  7.89200   1.000 31.48922  ? 114 VAL B HG21 1 
ATOM   6336 H HG22 . VAL B 2 114 ? 3.27100   -3.38700  6.59300   1.000 31.48922  ? 114 VAL B HG22 1 
ATOM   6337 H HG23 . VAL B 2 114 ? 2.85100   -2.52900  7.86300   1.000 31.48922  ? 114 VAL B HG23 1 
ATOM   6338 N N    . LEU B 2 115 ? -0.03500  -6.65000  7.17100   1.000 22.41606  ? 115 LEU B N    1 
ATOM   6339 C CA   . LEU B 2 115 ? -0.55100  -7.96900  7.51600   1.000 20.66390  ? 115 LEU B CA   1 
ATOM   6340 C C    . LEU B 2 115 ? 0.62200   -8.93000  7.38400   1.000 24.34917  ? 115 LEU B C    1 
ATOM   6341 O O    . LEU B 2 115 ? 1.00400   -9.31800  6.26900   1.000 23.77130  ? 115 LEU B O    1 
ATOM   6342 C CB   . LEU B 2 115 ? -1.72000  -8.35800  6.59900   1.000 25.10051  ? 115 LEU B CB   1 
ATOM   6343 C CG   . LEU B 2 115 ? -2.34500  -9.69600  6.99700   1.000 24.19593  ? 115 LEU B CG   1 
ATOM   6344 C CD1  . LEU B 2 115 ? -3.06000  -9.59700  8.40700   1.000 25.50308  ? 115 LEU B CD1  1 
ATOM   6345 C CD2  . LEU B 2 115 ? -3.33800  -10.13300 5.93700   1.000 26.98183  ? 115 LEU B CD2  1 
ATOM   6346 H H    . LEU B 2 115 ? 0.02100   -6.51200  6.32400   1.000 26.90008  ? 115 LEU B H    1 
ATOM   6347 H HA   . LEU B 2 115 ? -0.85800  -7.97400  8.43600   1.000 24.79748  ? 115 LEU B HA   1 
ATOM   6348 H HB2  . LEU B 2 115 ? -2.40700  -7.67600  6.65300   1.000 30.12141  ? 115 LEU B HB2  1 
ATOM   6349 H HB3  . LEU B 2 115 ? -1.39700  -8.43500  5.68800   1.000 30.12141  ? 115 LEU B HB3  1 
ATOM   6350 H HG   . LEU B 2 115 ? -1.65100  -10.37100 7.05600   1.000 29.03592  ? 115 LEU B HG   1 
ATOM   6351 H HD11 . LEU B 2 115 ? -3.63400  -10.36900 8.52600   1.000 30.60449  ? 115 LEU B HD11 1 
ATOM   6352 H HD12 . LEU B 2 115 ? -2.38500  -9.57600  9.10300   1.000 30.60449  ? 115 LEU B HD12 1 
ATOM   6353 H HD13 . LEU B 2 115 ? -3.59100  -8.78500  8.43400   1.000 30.60449  ? 115 LEU B HD13 1 
ATOM   6354 H HD21 . LEU B 2 115 ? -3.72800  -10.98100 6.20100   1.000 32.37900  ? 115 LEU B HD21 1 
ATOM   6355 H HD22 . LEU B 2 115 ? -4.03200  -9.46000  5.85800   1.000 32.37900  ? 115 LEU B HD22 1 
ATOM   6356 H HD23 . LEU B 2 115 ? -2.87400  -10.23000 5.09100   1.000 32.37900  ? 115 LEU B HD23 1 
ATOM   6357 N N    . ALA B 2 116 ? 1.25600   -9.23500  8.52400   1.000 23.42361  ? 116 ALA B N    1 
ATOM   6358 C CA   . ALA B 2 116 ? 2.42000   -10.11200 8.54400   1.000 24.84005  ? 116 ALA B CA   1 
ATOM   6359 C C    . ALA B 2 116 ? 1.92900   -11.54800 8.37900   1.000 28.95021  ? 116 ALA B C    1 
ATOM   6360 O O    . ALA B 2 116 ? 1.02200   -11.97900 9.10400   1.000 28.89430  ? 116 ALA B O    1 
ATOM   6361 C CB   . ALA B 2 116 ? 3.19200   -9.93900  9.85300   1.000 28.17114  ? 116 ALA B CB   1 
ATOM   6362 H H    . ALA B 2 116 ? 1.02600   -8.94200  9.29900   1.000 28.10914  ? 116 ALA B H    1 
ATOM   6363 H HA   . ALA B 2 116 ? 3.00800   -9.89500  7.80300   1.000 29.80886  ? 116 ALA B HA   1 
ATOM   6364 H HB1  . ALA B 2 116 ? 3.96100   -10.53000 9.84600   1.000 33.80617  ? 116 ALA B HB1  1 
ATOM   6365 H HB2  . ALA B 2 116 ? 3.48400   -9.01700  9.92800   1.000 33.80617  ? 116 ALA B HB2  1 
ATOM   6366 H HB3  . ALA B 2 116 ? 2.60900   -10.16300 10.59500  1.000 33.80617  ? 116 ALA B HB3  1 
ATOM   6367 N N    . CYS B 2 117 ? 2.48300   -12.26700 7.39800   1.000 28.31510  ? 117 CYS B N    1 
ATOM   6368 C CA   . CYS B 2 117 ? 2.00600   -13.60700 7.06100   1.000 29.37111  ? 117 CYS B CA   1 
ATOM   6369 C C    . CYS B 2 117 ? 3.18400   -14.55800 6.99300   1.000 27.35697  ? 117 CYS B C    1 
ATOM   6370 O O    . CYS B 2 117 ? 4.29600   -14.14800 6.66800   1.000 28.50102  ? 117 CYS B O    1 
ATOM   6371 C CB   . CYS B 2 117 ? 1.30800   -13.65000 5.71100   1.000 28.28510  ? 117 CYS B CB   1 
ATOM   6372 S SG   . CYS B 2 117 ? -0.09500  -12.59800 5.61700   1.000 31.78606  ? 117 CYS B SG   1 
ATOM   6373 H H    . CYS B 2 117 ? 3.13900   -11.99800 6.91200   1.000 33.97893  ? 117 CYS B H    1 
ATOM   6374 H HA   . CYS B 2 117 ? 1.39000   -13.92200 7.74100   1.000 35.24614  ? 117 CYS B HA   1 
ATOM   6375 H HB2  . CYS B 2 117 ? 1.93500   -13.37300 5.02500   1.000 33.94293  ? 117 CYS B HB2  1 
ATOM   6376 H HB3  . CYS B 2 117 ? 1.01200   -14.55800 5.54000   1.000 33.94293  ? 117 CYS B HB3  1 
ATOM   6377 H HG   . CYS B 2 117 ? 0.25100   -11.46500 5.79800   1.000 38.14408  ? 117 CYS B HG   1 
ATOM   6378 N N    . TYR B 2 118 ? 2.91000   -15.84100 7.23800   1.000 30.18253  ? 118 TYR B N    1 
ATOM   6379 C CA   . TYR B 2 118 ? 3.87800   -16.93500 7.13600   1.000 31.75228  ? 118 TYR B CA   1 
ATOM   6380 C C    . TYR B 2 118 ? 3.16900   -18.12900 6.52200   1.000 31.89110  ? 118 TYR B C    1 
ATOM   6381 O O    . TYR B 2 118 ? 2.06800   -18.48400 6.96700   1.000 30.30026  ? 118 TYR B O    1 
ATOM   6382 C CB   . TYR B 2 118 ? 4.46600   -17.32500 8.51200   1.000 39.16275  ? 118 TYR B CB   1 
ATOM   6383 C CG   . TYR B 2 118 ? 5.18400   -16.16900 9.11900   1.000 36.27526  ? 118 TYR B CG   1 
ATOM   6384 C CD1  . TYR B 2 118 ? 4.50100   -15.24200 9.90400   1.000 36.85173  ? 118 TYR B CD1  1 
ATOM   6385 C CD2  . TYR B 2 118 ? 6.53500   -15.96300 8.86900   1.000 33.43742  ? 118 TYR B CD2  1 
ATOM   6386 C CE1  . TYR B 2 118 ? 5.13600   -14.13200 10.40700  1.000 32.26241  ? 118 TYR B CE1  1 
ATOM   6387 C CE2  . TYR B 2 118 ? 7.19800   -14.85300 9.37900   1.000 31.22664  ? 118 TYR B CE2  1 
ATOM   6388 C CZ   . TYR B 2 118 ? 6.47600   -13.94800 10.15100  1.000 30.60716  ? 118 TYR B CZ   1 
ATOM   6389 O OH   . TYR B 2 118 ? 7.10400   -12.85300 10.64500  1.000 32.94931  ? 118 TYR B OH   1 
ATOM   6390 H H    . TYR B 2 118 ? 2.13000   -16.11300 7.47700   1.000 36.21984  ? 118 TYR B H    1 
ATOM   6391 H HA   . TYR B 2 118 ? 4.60600   -16.67300 6.55100   1.000 38.10353  ? 118 TYR B HA   1 
ATOM   6392 H HB2  . TYR B 2 118 ? 3.74700   -17.58800 9.10800   1.000 46.99610  ? 118 TYR B HB2  1 
ATOM   6393 H HB3  . TYR B 2 118 ? 5.09600   -18.05400 8.39900   1.000 46.99610  ? 118 TYR B HB3  1 
ATOM   6394 H HD1  . TYR B 2 118 ? 3.59200   -15.35800 10.06000  1.000 44.22288  ? 118 TYR B HD1  1 
ATOM   6395 H HD2  . TYR B 2 118 ? 6.99900   -16.56800 8.33600   1.000 40.12571  ? 118 TYR B HD2  1 
ATOM   6396 H HE1  . TYR B 2 118 ? 4.66900   -13.52000 10.92900  1.000 38.71570  ? 118 TYR B HE1  1 
ATOM   6397 H HE2  . TYR B 2 118 ? 8.10200   -14.71700 9.20700   1.000 37.47277  ? 118 TYR B HE2  1 
ATOM   6398 H HH   . TYR B 2 118 ? 6.56100   -12.38200 11.08000  1.000 39.53998  ? 118 TYR B HH   1 
ATOM   6399 N N    . ASN B 2 119 ? 3.79300   -18.73500 5.50300   1.000 34.41985  ? 119 ASN B N    1 
ATOM   6400 C CA   . ASN B 2 119 ? 3.22200   -19.89500 4.80700   1.000 34.36238  ? 119 ASN B CA   1 
ATOM   6401 C C    . ASN B 2 119 ? 1.83200   -19.60400 4.25700   1.000 34.26041  ? 119 ASN B C    1 
ATOM   6402 O O    . ASN B 2 119 ? 0.98100   -20.49400 4.22300   1.000 36.25255  ? 119 ASN B O    1 
ATOM   6403 C CB   . ASN B 2 119 ? 3.13700   -21.12400 5.71900   1.000 40.55980  ? 119 ASN B CB   1 
ATOM   6404 C CG   . ASN B 2 119 ? 4.48100   -21.62400 6.11500   1.000 41.58358  ? 119 ASN B CG   1 
ATOM   6405 O OD1  . ASN B 2 119 ? 4.84900   -21.53200 7.27400   1.000 50.72599  ? 119 ASN B OD1  1 
ATOM   6406 N ND2  . ASN B 2 119 ? 5.22700   -22.16300 5.15900   1.000 48.14105  ? 119 ASN B ND2  1 
ATOM   6407 H H    . ASN B 2 119 ? 4.55700   -18.48900 5.19400   1.000 41.30462  ? 119 ASN B H    1 
ATOM   6408 H HA   . ASN B 2 119 ? 3.79500   -20.12100 4.05800   1.000 41.23566  ? 119 ASN B HA   1 
ATOM   6409 H HB2  . ASN B 2 119 ? 2.65200   -20.89000 6.52600   1.000 48.67256  ? 119 ASN B HB2  1 
ATOM   6410 H HB3  . ASN B 2 119 ? 2.68000   -21.83900 5.25000   1.000 48.67256  ? 119 ASN B HB3  1 
ATOM   6411 H HD21 . ASN B 2 119 ? 6.01100   -22.46500 5.34400   1.000 57.77007  ? 119 ASN B HD21 1 
ATOM   6412 H HD22 . ASN B 2 119 ? 4.92800   -22.20900 4.35400   1.000 57.77007  ? 119 ASN B HD22 1 
ATOM   6413 N N    . GLY B 2 120 ? 1.58400   -18.36500 3.84300   1.000 33.63832  ? 120 GLY B N    1 
ATOM   6414 C CA   . GLY B 2 120 ? 0.28800   -17.99200 3.31800   1.000 33.19799  ? 120 GLY B CA   1 
ATOM   6415 C C    . GLY B 2 120 ? -0.77300  -17.71100 4.35200   1.000 34.35718  ? 120 GLY B C    1 
ATOM   6416 O O    . GLY B 2 120 ? -1.90000  -17.38400 3.97100   1.000 33.70487  ? 120 GLY B O    1 
ATOM   6417 H H    . GLY B 2 120 ? 2.15600   -17.72300 3.85800   1.000 40.36678  ? 120 GLY B H    1 
ATOM   6418 H HA2  . GLY B 2 120 ? 0.38900   -17.19600 2.77300   1.000 39.83838  ? 120 GLY B HA2  1 
ATOM   6419 H HA3  . GLY B 2 120 ? -0.03600  -18.70600 2.74700   1.000 39.83838  ? 120 GLY B HA3  1 
ATOM   6420 N N    . SER B 2 121 ? -0.46300  -17.81300 5.65300   1.000 32.01437  ? 121 SER B N    1 
ATOM   6421 C CA   . SER B 2 121 ? -1.48000  -17.58700 6.67400   1.000 33.56248  ? 121 SER B CA   1 
ATOM   6422 C C    . SER B 2 121 ? -1.19100  -16.30300 7.42700   1.000 31.14114  ? 121 SER B C    1 
ATOM   6423 O O    . SER B 2 121 ? -0.08600  -16.12700 7.96600   1.000 31.66554  ? 121 SER B O    1 
ATOM   6424 C CB   . SER B 2 121 ? -1.55800  -18.74200 7.69700   1.000 41.22032  ? 121 SER B CB   1 
ATOM   6425 O OG   . SER B 2 121 ? -1.89200  -19.95400 7.06600   1.000 54.29578  ? 121 SER B OG   1 
ATOM   6426 H H    . SER B 2 121 ? 0.31600   -18.00800 5.96000   1.000 38.41804  ? 121 SER B H    1 
ATOM   6427 H HA   . SER B 2 121 ? -2.34200  -17.55100 6.24300   1.000 40.27578  ? 121 SER B HA   1 
ATOM   6428 H HB2  . SER B 2 121 ? -0.69500  -18.83900 8.12900   1.000 49.46519  ? 121 SER B HB2  1 
ATOM   6429 H HB3  . SER B 2 121 ? -2.23700  -18.53300 8.35700   1.000 49.46519  ? 121 SER B HB3  1 
ATOM   6430 H HG   . SER B 2 121 ? -1.93100  -20.57200 7.63300   1.000 65.15574  ? 121 SER B HG   1 
ATOM   6431 N N    . PRO B 2 122 ? -2.19200  -15.43800 7.55600   1.000 32.05957  ? 122 PRO B N    1 
ATOM   6432 C CA   . PRO B 2 122 ? -1.99300  -14.16900 8.26700   1.000 30.83706  ? 122 PRO B CA   1 
ATOM   6433 C C    . PRO B 2 122 ? -1.73600  -14.43900 9.73700   1.000 34.02904  ? 122 PRO B C    1 
ATOM   6434 O O    . PRO B 2 122 ? -2.43300  -15.23500 10.36900  1.000 32.20343  ? 122 PRO B O    1 
ATOM   6435 C CB   . PRO B 2 122 ? -3.32100  -13.44300 8.05600   1.000 28.40096  ? 122 PRO B CB   1 
ATOM   6436 C CG   . PRO B 2 122 ? -3.80500  -13.96800 6.72900   1.000 34.91891  ? 122 PRO B CG   1 
ATOM   6437 C CD   . PRO B 2 122 ? -3.42400  -15.43500 6.75100   1.000 37.96670  ? 122 PRO B CD   1 
ATOM   6438 H HA   . PRO B 2 122 ? -1.26300  -13.65900 7.88500   1.000 37.00527  ? 122 PRO B HA   1 
ATOM   6439 H HB2  . PRO B 2 122 ? -3.94000  -13.67000 8.76700   1.000 34.08195  ? 122 PRO B HB2  1 
ATOM   6440 H HB3  . PRO B 2 122 ? -3.17100  -12.48600 8.01600   1.000 34.08195  ? 122 PRO B HB3  1 
ATOM   6441 H HG2  . PRO B 2 122 ? -4.76700  -13.86100 6.66300   1.000 41.90349  ? 122 PRO B HG2  1 
ATOM   6442 H HG3  . PRO B 2 122 ? -3.35400  -13.50400 6.00600   1.000 41.90349  ? 122 PRO B HG3  1 
ATOM   6443 H HD2  . PRO B 2 122 ? -4.11600  -15.96200 7.18000   1.000 45.56085  ? 122 PRO B HD2  1 
ATOM   6444 H HD3  . PRO B 2 122 ? -3.25200  -15.73300 5.84500   1.000 45.56085  ? 122 PRO B HD3  1 
ATOM   6445 N N    . SER B 2 123 ? -0.70000  -13.81500 10.27200  1.000 28.95679  ? 123 SER B N    1 
ATOM   6446 C CA   . SER B 2 123 ? -0.36800  -14.04500 11.66300  1.000 32.55441  ? 123 SER B CA   1 
ATOM   6447 C C    . SER B 2 123 ? -0.55500  -12.82900 12.54700  1.000 26.39767  ? 123 SER B C    1 
ATOM   6448 O O    . SER B 2 123 ? -0.74200  -13.01100 13.73400  1.000 27.47851  ? 123 SER B O    1 
ATOM   6449 C CB   . SER B 2 123 ? 1.06100   -14.59200 11.82200  1.000 42.88443  ? 123 SER B CB   1 
ATOM   6450 O OG   . SER B 2 123 ? 2.00400   -13.57400 11.62000  1.000 56.24418  ? 123 SER B OG   1 
ATOM   6451 H H    . SER B 2 123 ? -0.18300  -13.26500 9.86000   1.000 34.74895  ? 123 SER B H    1 
ATOM   6452 H HA   . SER B 2 123 ? -0.96000  -14.72800 12.01100  1.000 39.06609  ? 123 SER B HA   1 
ATOM   6453 H HB2  . SER B 2 123 ? 1.16600   -14.94700 12.71800  1.000 51.46212  ? 123 SER B HB2  1 
ATOM   6454 H HB3  . SER B 2 123 ? 1.20600   -15.29300 11.16700  1.000 51.46212  ? 123 SER B HB3  1 
ATOM   6455 H HG   . SER B 2 123 ? 2.78100   -13.87800 11.71800  1.000 67.49382  ? 123 SER B HG   1 
ATOM   6456 N N    . GLY B 2 124 ? -0.41700  -11.60900 12.02500  1.000 25.80073  ? 124 GLY B N    1 
ATOM   6457 C CA   . GLY B 2 124 ? -0.62200  -10.45000 12.87100  1.000 24.97732  ? 124 GLY B CA   1 
ATOM   6458 C C    . GLY B 2 124 ? -0.72800  -9.21400  12.02000  1.000 24.39934  ? 124 GLY B C    1 
ATOM   6459 O O    . GLY B 2 124 ? -0.43500  -9.23600  10.82800  1.000 24.56057  ? 124 GLY B O    1 
ATOM   6460 H H    . GLY B 2 124 ? -0.21100  -11.43500 11.20800  1.000 30.96167  ? 124 GLY B H    1 
ATOM   6461 H HA2  . GLY B 2 124 ? -1.44000  -10.55300 13.38200  1.000 29.97358  ? 124 GLY B HA2  1 
ATOM   6462 H HA3  . GLY B 2 124 ? 0.12300   -10.35000 13.48400  1.000 29.97358  ? 124 GLY B HA3  1 
ATOM   6463 N N    . VAL B 2 125 ? -1.20000  -8.13200  12.63500  1.000 25.00689  ? 125 VAL B N    1 
ATOM   6464 C CA   . VAL B 2 125 ? -1.41300  -6.89000  11.90700  1.000 23.86038  ? 125 VAL B CA   1 
ATOM   6465 C C    . VAL B 2 125 ? -0.88100  -5.74000  12.75700  1.000 23.97763  ? 125 VAL B C    1 
ATOM   6466 O O    . VAL B 2 125 ? -1.07600  -5.70000  13.97700  1.000 26.31011  ? 125 VAL B O    1 
ATOM   6467 C CB   . VAL B 2 125 ? -2.90100  -6.70700  11.47700  1.000 27.25287  ? 125 VAL B CB   1 
ATOM   6468 C CG1  . VAL B 2 125 ? -3.85600  -6.61100  12.64800  1.000 30.55304  ? 125 VAL B CG1  1 
ATOM   6469 C CG2  . VAL B 2 125 ? -3.04000  -5.49400  10.55400  1.000 27.93253  ? 125 VAL B CG2  1 
ATOM   6470 H H    . VAL B 2 125 ? -1.40300  -8.09300  13.47000  1.000 30.00907  ? 125 VAL B H    1 
ATOM   6471 H HA   . VAL B 2 125 ? -0.88300  -6.91900  11.09900  1.000 28.63326  ? 125 VAL B HA   1 
ATOM   6472 H HB   . VAL B 2 125 ? -3.16200  -7.48700  10.96200  1.000 32.70425  ? 125 VAL B HB   1 
ATOM   6473 H HG11 . VAL B 2 125 ? -4.76200  -6.53700  12.31000  1.000 36.66445  ? 125 VAL B HG11 1 
ATOM   6474 H HG12 . VAL B 2 125 ? -3.76900  -7.40900  13.19200  1.000 36.66445  ? 125 VAL B HG12 1 
ATOM   6475 H HG13 . VAL B 2 125 ? -3.63400  -5.82700  13.17400  1.000 36.66445  ? 125 VAL B HG13 1 
ATOM   6476 H HG21 . VAL B 2 125 ? -3.96100  -5.42900  10.25600  1.000 33.51984  ? 125 VAL B HG21 1 
ATOM   6477 H HG22 . VAL B 2 125 ? -2.79300  -4.69400  11.04400  1.000 33.51984  ? 125 VAL B HG22 1 
ATOM   6478 H HG23 . VAL B 2 125 ? -2.45300  -5.61000  9.79000   1.000 33.51984  ? 125 VAL B HG23 1 
ATOM   6479 N N    . TYR B 2 126 ? -0.15800  -4.82200  12.11900  1.000 24.08459  ? 126 TYR B N    1 
ATOM   6480 C CA   . TYR B 2 126 ? 0.28500   -3.66000  12.86300  1.000 23.90889  ? 126 TYR B CA   1 
ATOM   6481 C C    . TYR B 2 126 ? 0.44200   -2.46600  11.93800  1.000 25.54094  ? 126 TYR B C    1 
ATOM   6482 O O    . TYR B 2 126 ? 0.55600   -2.61400  10.71700  1.000 26.44774  ? 126 TYR B O    1 
ATOM   6483 C CB   . TYR B 2 126 ? 1.59300   -3.93800  13.58400  1.000 24.38766  ? 126 TYR B CB   1 
ATOM   6484 C CG   . TYR B 2 126 ? 2.68400   -4.50200  12.70000  1.000 24.50175  ? 126 TYR B CG   1 
ATOM   6485 C CD1  . TYR B 2 126 ? 3.57400   -3.66200  12.02000  1.000 24.85431  ? 126 TYR B CD1  1 
ATOM   6486 C CD2  . TYR B 2 126 ? 2.85400   -5.87600  12.59700  1.000 27.12374  ? 126 TYR B CD2  1 
ATOM   6487 C CE1  . TYR B 2 126 ? 4.57300   -4.20100  11.19000  1.000 26.61834  ? 126 TYR B CE1  1 
ATOM   6488 C CE2  . TYR B 2 126 ? 3.85500   -6.41600  11.77100  1.000 27.99299  ? 126 TYR B CE2  1 
ATOM   6489 C CZ   . TYR B 2 126 ? 4.70000   -5.57900  11.08600  1.000 28.35933  ? 126 TYR B CZ   1 
ATOM   6490 O OH   . TYR B 2 126 ? 5.71000   -6.15600  10.30100  1.000 32.80596  ? 126 TYR B OH   1 
ATOM   6491 H H    . TYR B 2 126 ? 0.07800   -4.84900  11.29200  1.000 28.90230  ? 126 TYR B H    1 
ATOM   6492 H HA   . TYR B 2 126 ? -0.38300  -3.43500  13.52900  1.000 28.69146  ? 126 TYR B HA   1 
ATOM   6493 H HB2  . TYR B 2 126 ? 1.92100   -3.10800  13.96400  1.000 29.26599  ? 126 TYR B HB2  1 
ATOM   6494 H HB3  . TYR B 2 126 ? 1.42700   -4.57900  14.29300  1.000 29.26599  ? 126 TYR B HB3  1 
ATOM   6495 H HD1  . TYR B 2 126 ? 3.47300   -2.73900  12.07900  1.000 29.82597  ? 126 TYR B HD1  1 
ATOM   6496 H HD2  . TYR B 2 126 ? 2.27200   -6.44600  13.04600  1.000 32.54929  ? 126 TYR B HD2  1 
ATOM   6497 H HE1  . TYR B 2 126 ? 5.15700   -3.64100  10.73200  1.000 31.94281  ? 126 TYR B HE1  1 
ATOM   6498 H HE2  . TYR B 2 126 ? 3.95400   -7.33800  11.70100  1.000 33.59239  ? 126 TYR B HE2  1 
ATOM   6499 H HH   . TYR B 2 126 ? 5.65900   -6.99400  10.33700  1.000 39.36795  ? 126 TYR B HH   1 
ATOM   6500 N N    . GLN B 2 127 ? 0.53800   -1.29300  12.55600  1.000 27.67915  ? 127 GLN B N    1 
ATOM   6501 C CA   . GLN B 2 127 ? 0.72700   -0.03800  11.80200  1.000 28.44852  ? 127 GLN B CA   1 
ATOM   6502 C C    . GLN B 2 127 ? 2.21500   0.24800   11.64100  1.000 32.50669  ? 127 GLN B C    1 
ATOM   6503 O O    . GLN B 2 127 ? 2.95700   0.04200   12.59400  1.000 32.70235  ? 127 GLN B O    1 
ATOM   6504 C CB   . GLN B 2 127 ? 0.15800   1.15100   12.56200  1.000 32.48203  ? 127 GLN B CB   1 
ATOM   6505 C CG   . GLN B 2 127 ? -1.27300  1.49400   12.24200  1.000 34.67205  ? 127 GLN B CG   1 
ATOM   6506 C CD   . GLN B 2 127 ? -1.56500  1.88200   10.81700  1.000 29.72385  ? 127 GLN B CD   1 
ATOM   6507 O OE1  . GLN B 2 127 ? -2.05800  1.08300   10.04200  1.000 33.43671  ? 127 GLN B OE1  1 
ATOM   6508 N NE2  . GLN B 2 127 ? -1.31900  3.13000   10.47300  1.000 33.95105  ? 127 GLN B NE2  1 
ATOM   6509 H H    . GLN B 2 127 ? 0.49800   -1.18800  13.40900  1.000 33.21578  ? 127 GLN B H    1 
ATOM   6510 H HA   . GLN B 2 127 ? 0.31100   -0.09800  10.92800  1.000 34.13903  ? 127 GLN B HA   1 
ATOM   6511 H HB2  . GLN B 2 127 ? 0.20100   0.94600   13.50500  1.000 38.97924  ? 127 GLN B HB2  1 
ATOM   6512 H HB3  . GLN B 2 127 ? 0.70000   1.93200   12.37100  1.000 38.97924  ? 127 GLN B HB3  1 
ATOM   6513 H HG2  . GLN B 2 127 ? -1.82400  0.72300   12.44900  1.000 41.60726  ? 127 GLN B HG2  1 
ATOM   6514 H HG3  . GLN B 2 127 ? -1.54000  2.23900   12.80300  1.000 41.60726  ? 127 GLN B HG3  1 
ATOM   6515 H HE21 . GLN B 2 127 ? -0.97900  3.67500   11.04500  1.000 40.74206  ? 127 GLN B HE21 1 
ATOM   6516 H HE22 . GLN B 2 127 ? -1.47700  3.39400   9.67000   1.000 40.74206  ? 127 GLN B HE22 1 
ATOM   6517 N N    . CYS B 2 128 ? 2.60300   0.71500   10.46800  1.000 28.15131  ? 128 CYS B N    1 
ATOM   6518 C CA   . CYS B 2 128 ? 4.00000   1.07100   10.13800  1.000 32.77041  ? 128 CYS B CA   1 
ATOM   6519 C C    . CYS B 2 128 ? 3.98200   2.38700   9.35600   1.000 31.71997  ? 128 CYS B C    1 
ATOM   6520 O O    . CYS B 2 128 ? 2.92800   2.73500   8.85200   1.000 30.96883  ? 128 CYS B O    1 
ATOM   6521 C CB   . CYS B 2 128 ? 4.58800   0.01800   9.20600   1.000 32.27684  ? 128 CYS B CB   1 
ATOM   6522 S SG   . CYS B 2 128 ? 5.70700   -1.12000  10.04900  1.000 55.94706  ? 128 CYS B SG   1 
ATOM   6523 H H    . CYS B 2 128 ? 2.06200   0.84400   9.81200   1.000 33.78238  ? 128 CYS B H    1 
ATOM   6524 H HA   . CYS B 2 128 ? 4.54300   1.15900   10.93700  1.000 39.32529  ? 128 CYS B HA   1 
ATOM   6525 H HB2  . CYS B 2 128 ? 3.86500   -0.50200  8.82200   1.000 38.73301  ? 128 CYS B HB2  1 
ATOM   6526 H HB3  . CYS B 2 128 ? 5.08700   0.46200   8.50300   1.000 38.73301  ? 128 CYS B HB3  1 
ATOM   6527 H HG   . CYS B 2 128 ? 5.15200   -1.53800  11.02700  1.000 67.13728  ? 128 CYS B HG   1 
ATOM   6528 N N    . ALA B 2 129 ? 5.10100   3.10000   9.30100   1.000 33.04006  ? 129 ALA B N    1 
ATOM   6529 C CA   . ALA B 2 129 ? 5.23600   4.31300   8.51200   1.000 30.34305  ? 129 ALA B CA   1 
ATOM   6530 C C    . ALA B 2 129 ? 6.33600   4.06500   7.49400   1.000 28.89747  ? 129 ALA B C    1 
ATOM   6531 O O    . ALA B 2 129 ? 7.35600   3.45300   7.80800   1.000 32.81311  ? 129 ALA B O    1 
ATOM   6532 C CB   . ALA B 2 129 ? 5.63200   5.53000   9.37500   1.000 31.88349  ? 129 ALA B CB   1 
ATOM   6533 H H    . ALA B 2 129 ? 5.81800   2.89200   9.72800   1.000 39.64887  ? 129 ALA B H    1 
ATOM   6534 H HA   . ALA B 2 129 ? 4.41000   4.50800   8.04600   1.000 36.41246  ? 129 ALA B HA   1 
ATOM   6535 H HB1  . ALA B 2 129 ? 5.69900   6.31200   8.80500   1.000 38.26098  ? 129 ALA B HB1  1 
ATOM   6536 H HB2  . ALA B 2 129 ? 4.95200   5.67100   10.05300  1.000 38.26098  ? 129 ALA B HB2  1 
ATOM   6537 H HB3  . ALA B 2 129 ? 6.48800   5.35300   9.79600   1.000 38.26098  ? 129 ALA B HB3  1 
ATOM   6538 N N    . MET B 2 130 ? 6.17700   4.59200   6.29900   1.000 28.83168  ? 130 MET B N    1 
ATOM   6539 C CA   . MET B 2 130 ? 7.32300   4.63000   5.41400   1.000 30.45370  ? 130 MET B CA   1 
ATOM   6540 C C    . MET B 2 130 ? 8.27900   5.67700   5.97900   1.000 31.82755  ? 130 MET B C    1 
ATOM   6541 O O    . MET B 2 130 ? 7.92300   6.85200   6.06500   1.000 29.32204  ? 130 MET B O    1 
ATOM   6542 C CB   . MET B 2 130 ? 6.87700   4.98300   4.00100   1.000 29.10416  ? 130 MET B CB   1 
ATOM   6543 C CG   . MET B 2 130 ? 7.98400   5.09800   2.94000   1.000 32.10275  ? 130 MET B CG   1 
ATOM   6544 S SD   . MET B 2 130 ? 8.86400   3.52000   2.70900   1.000 33.97530  ? 130 MET B SD   1 
ATOM   6545 C CE   . MET B 2 130 ? 7.49600   2.41800   2.24100   1.000 30.26004  ? 130 MET B CE   1 
ATOM   6546 H H    . MET B 2 130 ? 5.44900   4.92300   5.98300   1.000 34.59882  ? 130 MET B H    1 
ATOM   6547 H HA   . MET B 2 130 ? 7.75700   3.76200   5.39700   1.000 36.54524  ? 130 MET B HA   1 
ATOM   6548 H HB2  . MET B 2 130 ? 6.25100   4.30600   3.70000   1.000 34.92579  ? 130 MET B HB2  1 
ATOM   6549 H HB3  . MET B 2 130 ? 6.42500   5.84100   4.03400   1.000 34.92579  ? 130 MET B HB3  1 
ATOM   6550 H HG2  . MET B 2 130 ? 7.58800   5.35100   2.09200   1.000 38.52410  ? 130 MET B HG2  1 
ATOM   6551 H HG3  . MET B 2 130 ? 8.62900   5.76600   3.22100   1.000 38.52410  ? 130 MET B HG3  1 
ATOM   6552 H HE1  . MET B 2 130 ? 7.86300   1.57600   1.93000   1.000 36.31285  ? 130 MET B HE1  1 
ATOM   6553 H HE2  . MET B 2 130 ? 6.93200   2.26600   3.01500   1.000 36.31285  ? 130 MET B HE2  1 
ATOM   6554 H HE3  . MET B 2 130 ? 6.98300   2.83600   1.53200   1.000 36.31285  ? 130 MET B HE3  1 
ATOM   6555 N N    . ARG B 2 131 ? 9.46500   5.26400   6.43200   1.000 31.27750  ? 131 ARG B N    1 
ATOM   6556 C CA   . ARG B 2 131 ? 10.40400  6.24400   6.99800   1.000 27.38256  ? 131 ARG B CA   1 
ATOM   6557 C C    . ARG B 2 131 ? 10.94000  7.18400   5.91700   1.000 29.17628  ? 131 ARG B C    1 
ATOM   6558 O O    . ARG B 2 131 ? 10.98000  6.83600   4.73900   1.000 30.18608  ? 131 ARG B O    1 
ATOM   6559 C CB   . ARG B 2 131 ? 11.58200  5.54600   7.66700   1.000 32.55728  ? 131 ARG B CB   1 
ATOM   6560 C CG   . ARG B 2 131 ? 11.19900  4.52400   8.73600   1.000 32.47468  ? 131 ARG B CG   1 
ATOM   6561 C CD   . ARG B 2 131 ? 10.38000  5.12400   9.90400   1.000 35.74095  ? 131 ARG B CD   1 
ATOM   6562 N NE   . ARG B 2 131 ? 10.95400  6.39800   10.33300  1.000 31.80398  ? 131 ARG B NE   1 
ATOM   6563 C CZ   . ARG B 2 131 ? 10.35900  7.24000   11.17000  1.000 35.43898  ? 131 ARG B CZ   1 
ATOM   6564 N NH1  . ARG B 2 131 ? 9.16900   6.96000   11.71500  1.000 31.05577  ? 131 ARG B NH1  1 
ATOM   6565 N NH2  . ARG B 2 131 ? 10.95300  8.40700   11.45100  1.000 33.57937  ? 131 ARG B NH2  1 
ATOM   6566 H H    . ARG B 2 131 ? 9.74500   4.45100   6.42600   1.000 37.53381  ? 131 ARG B H    1 
ATOM   6567 H HA   . ARG B 2 131 ? 9.93900   6.76600   7.66900   1.000 32.85987  ? 131 ARG B HA   1 
ATOM   6568 H HB2  . ARG B 2 131 ? 12.08700  5.07700   6.98500   1.000 39.06954  ? 131 ARG B HB2  1 
ATOM   6569 H HB3  . ARG B 2 131 ? 12.14600  6.21600   8.08300   1.000 39.06954  ? 131 ARG B HB3  1 
ATOM   6570 H HG2  . ARG B 2 131 ? 10.66200  3.82800   8.32900   1.000 38.97041  ? 131 ARG B HG2  1 
ATOM   6571 H HG3  . ARG B 2 131 ? 12.00900  4.14100   9.10700   1.000 38.97041  ? 131 ARG B HG3  1 
ATOM   6572 H HD2  . ARG B 2 131 ? 9.46800   5.28100   9.61200   1.000 42.88994  ? 131 ARG B HD2  1 
ATOM   6573 H HD3  . ARG B 2 131 ? 10.39400  4.51200   10.65600  1.000 42.88994  ? 131 ARG B HD3  1 
ATOM   6574 H HE   . ARG B 2 131 ? 11.77900  6.54700   10.14000  1.000 38.16557  ? 131 ARG B HE   1 
ATOM   6575 H HH11 . ARG B 2 131 ? 8.77700   6.21600   11.53700  1.000 37.26772  ? 131 ARG B HH11 1 
ATOM   6576 H HH12 . ARG B 2 131 ? 8.80100   7.52100   12.25200  1.000 37.26772  ? 131 ARG B HH12 1 
ATOM   6577 H HH21 . ARG B 2 131 ? 11.71700  8.59500   11.10300  1.000 40.29604  ? 131 ARG B HH21 1 
ATOM   6578 H HH22 . ARG B 2 131 ? 10.57800  8.96100   11.99100  1.000 40.29604  ? 131 ARG B HH22 1 
ATOM   6579 N N    . PRO B 2 132 ? 11.42600  8.36700   6.31400   1.000 31.96923  ? 132 PRO B N    1 
ATOM   6580 C CA   . PRO B 2 132 ? 12.09700  9.23000   5.34200   1.000 34.68180  ? 132 PRO B CA   1 
ATOM   6581 C C    . PRO B 2 132 ? 13.25300  8.54600   4.63400   1.000 35.51005  ? 132 PRO B C    1 
ATOM   6582 O O    . PRO B 2 132 ? 13.53200  8.89100   3.48800   1.000 35.66088  ? 132 PRO B O    1 
ATOM   6583 C CB   . PRO B 2 132 ? 12.55500  10.42300  6.19700   1.000 34.36849  ? 132 PRO B CB   1 
ATOM   6584 C CG   . PRO B 2 132 ? 11.41300  10.54700  7.22700   1.000 30.76121  ? 132 PRO B CG   1 
ATOM   6585 C CD   . PRO B 2 132 ? 11.10500  9.08100   7.57100   1.000 31.22003  ? 132 PRO B CD   1 
ATOM   6586 H HA   . PRO B 2 132 ? 11.46100  9.54200   4.68000   1.000 41.61896  ? 132 PRO B HA   1 
ATOM   6587 H HB2  . PRO B 2 132 ? 13.39900  10.22000  6.63100   1.000 41.24299  ? 132 PRO B HB2  1 
ATOM   6588 H HB3  . PRO B 2 132 ? 12.62200  11.22100  5.65000   1.000 41.24299  ? 132 PRO B HB3  1 
ATOM   6589 H HG2  . PRO B 2 132 ? 11.72000  11.03300  8.00900   1.000 36.91425  ? 132 PRO B HG2  1 
ATOM   6590 H HG3  . PRO B 2 132 ? 10.64500  10.98000  6.82300   1.000 36.91425  ? 132 PRO B HG3  1 
ATOM   6591 H HD2  . PRO B 2 132 ? 11.67700  8.77400   8.29200   1.000 37.46483  ? 132 PRO B HD2  1 
ATOM   6592 H HD3  . PRO B 2 132 ? 10.16600  8.97800   7.79100   1.000 37.46483  ? 132 PRO B HD3  1 
ATOM   6593 N N    . ASN B 2 133 ? 13.93500  7.59000   5.26800   1.000 34.20329  ? 133 ASN B N    1 
ATOM   6594 C CA   . ASN B 2 133 ? 15.03400  6.89200   4.57800   1.000 35.41489  ? 133 ASN B CA   1 
ATOM   6595 C C    . ASN B 2 133 ? 14.53200  5.67200   3.81100   1.000 35.38507  ? 133 ASN B C    1 
ATOM   6596 O O    . ASN B 2 133 ? 15.34500  4.85300   3.35600   1.000 33.47157  ? 133 ASN B O    1 
ATOM   6597 C CB   . ASN B 2 133 ? 16.14200  6.47700   5.56600   1.000 38.17625  ? 133 ASN B CB   1 
ATOM   6598 C CG   . ASN B 2 133 ? 15.67900  5.41100   6.55000   1.000 42.82592  ? 133 ASN B CG   1 
ATOM   6599 O OD1  . ASN B 2 133 ? 14.51700  4.96400   6.51700   1.000 37.21701  ? 133 ASN B OD1  1 
ATOM   6600 N ND2  . ASN B 2 133 ? 16.57200  5.01100   7.46400   1.000 42.84416  ? 133 ASN B ND2  1 
ATOM   6601 H H    . ASN B 2 133 ? 13.79000  7.33000   6.07500   1.000 41.04475  ? 133 ASN B H    1 
ATOM   6602 H HA   . ASN B 2 133 ? 15.43200  7.49800   3.93400   1.000 42.49867  ? 133 ASN B HA   1 
ATOM   6603 H HB2  . ASN B 2 133 ? 16.89300  6.12000   5.06700   1.000 45.81230  ? 133 ASN B HB2  1 
ATOM   6604 H HB3  . ASN B 2 133 ? 16.42000  7.25500   6.07400   1.000 45.81230  ? 133 ASN B HB3  1 
ATOM   6605 H HD21 . ASN B 2 133 ? 16.35600  4.41300   8.04300   1.000 51.41380  ? 133 ASN B HD21 1 
ATOM   6606 H HD22 . ASN B 2 133 ? 17.36500  5.34300   7.46400   1.000 51.41380  ? 133 ASN B HD22 1 
ATOM   6607 N N    . PHE B 2 134 ? 13.20800  5.55500   3.63500   1.000 33.43964  ? 134 PHE B N    1 
ATOM   6608 C CA   . PHE B 2 134 ? 12.53900  4.52800   2.85000   1.000 32.28583  ? 134 PHE B CA   1 
ATOM   6609 C C    . PHE B 2 134 ? 12.65400  3.13800   3.43100   1.000 33.89667  ? 134 PHE B C    1 
ATOM   6610 O O    . PHE B 2 134 ? 12.45400  2.14700   2.70800   1.000 38.17370  ? 134 PHE B O    1 
ATOM   6611 C CB   . PHE B 2 134 ? 13.02600  4.47900   1.39400   1.000 31.64957  ? 134 PHE B CB   1 
ATOM   6612 C CG   . PHE B 2 134 ? 12.61100  5.65600   0.60100   1.000 32.74640  ? 134 PHE B CG   1 
ATOM   6613 C CD1  . PHE B 2 134 ? 11.28200  5.78500   0.17400   1.000 34.95405  ? 134 PHE B CD1  1 
ATOM   6614 C CD2  . PHE B 2 134 ? 13.52600  6.65800   0.30500   1.000 36.20462  ? 134 PHE B CD2  1 
ATOM   6615 C CE1  . PHE B 2 134 ? 10.87400  6.89300   -0.54200  1.000 36.59258  ? 134 PHE B CE1  1 
ATOM   6616 C CE2  . PHE B 2 134 ? 13.14000  7.77700   -0.41900  1.000 36.93838  ? 134 PHE B CE2  1 
ATOM   6617 C CZ   . PHE B 2 134 ? 11.80800  7.89000   -0.83300  1.000 40.31483  ? 134 PHE B CZ   1 
ATOM   6618 H H    . PHE B 2 134 ? 12.64600  6.10100   3.98900   1.000 40.12836  ? 134 PHE B H    1 
ATOM   6619 H HA   . PHE B 2 134 ? 11.59400  4.74500   2.82400   1.000 38.74379  ? 134 PHE B HA   1 
ATOM   6620 H HB2  . PHE B 2 134 ? 13.99500  4.43900   1.38500   1.000 37.98029  ? 134 PHE B HB2  1 
ATOM   6621 H HB3  . PHE B 2 134 ? 12.65900  3.69200   0.96200   1.000 37.98029  ? 134 PHE B HB3  1 
ATOM   6622 H HD1  . PHE B 2 134 ? 10.66600  5.11900   0.38100   1.000 41.94566  ? 134 PHE B HD1  1 
ATOM   6623 H HD2  . PHE B 2 134 ? 14.40700  6.57700   0.59200   1.000 43.44634  ? 134 PHE B HD2  1 
ATOM   6624 H HE1  . PHE B 2 134 ? 9.99300   6.97300   -0.82800  1.000 43.91189  ? 134 PHE B HE1  1 
ATOM   6625 H HE2  . PHE B 2 134 ? 13.75500  8.44500   -0.61900  1.000 44.32685  ? 134 PHE B HE2  1 
ATOM   6626 H HZ   . PHE B 2 134 ? 11.54400  8.63400   -1.32500  1.000 48.37860  ? 134 PHE B HZ   1 
ATOM   6627 N N    . THR B 2 135 ? 12.92600  3.01000   4.71900   1.000 32.84497  ? 135 THR B N    1 
ATOM   6628 C CA   . THR B 2 135 ? 12.75900  1.71900   5.35700   1.000 31.41089  ? 135 THR B CA   1 
ATOM   6629 C C    . THR B 2 135 ? 11.45000  1.72300   6.11800   1.000 33.05323  ? 135 THR B C    1 
ATOM   6630 O O    . THR B 2 135 ? 10.77900  2.75000   6.23600   1.000 32.04694  ? 135 THR B O    1 
ATOM   6631 C CB   . THR B 2 135 ? 13.94300  1.42100   6.29800   1.000 34.06534  ? 135 THR B CB   1 
ATOM   6632 O OG1  . THR B 2 135 ? 13.97200  2.41800   7.30900   1.000 31.86493  ? 135 THR B OG1  1 
ATOM   6633 C CG2  . THR B 2 135 ? 15.29100  1.42500   5.51800   1.000 38.19045  ? 135 THR B CG2  1 
ATOM   6634 H H    . THR B 2 135 ? 13.20200  3.64000   5.23500   1.000 39.41477  ? 135 THR B H    1 
ATOM   6635 H HA   . THR B 2 135 ? 12.72200  1.01800   4.68900   1.000 37.69387  ? 135 THR B HA   1 
ATOM   6636 H HB   . THR B 2 135 ? 13.82400  0.54900   6.70500   1.000 40.87921  ? 135 THR B HB   1 
ATOM   6637 H HG1  . THR B 2 135 ? 14.08700  3.17500   6.96300   1.000 38.23872  ? 135 THR B HG1  1 
ATOM   6638 H HG21 . THR B 2 135 ? 16.02200  1.21000   6.11900   1.000 45.82934  ? 135 THR B HG21 1 
ATOM   6639 H HG22 . THR B 2 135 ? 15.26400  0.76600   4.80700   1.000 45.82934  ? 135 THR B HG22 1 
ATOM   6640 H HG23 . THR B 2 135 ? 15.44800  2.30000   5.13100   1.000 45.82934  ? 135 THR B HG23 1 
ATOM   6641 N N    . ILE B 2 136 ? 11.06000  0.56200   6.61500   1.000 29.08869  ? 136 ILE B N    1 
ATOM   6642 C CA   . ILE B 2 136 ? 9.97200   0.53000   7.56700   1.000 30.28524  ? 136 ILE B CA   1 
ATOM   6643 C C    . ILE B 2 136 ? 10.46500  -0.20900  8.79300   1.000 31.41362  ? 136 ILE B C    1 
ATOM   6644 O O    . ILE B 2 136 ? 11.26200  -1.15200  8.68600   1.000 30.79800  ? 136 ILE B O    1 
ATOM   6645 C CB   . ILE B 2 136 ? 8.67300   -0.11100  7.00400   1.000 34.00419  ? 136 ILE B CB   1 
ATOM   6646 C CG1  . ILE B 2 136 ? 8.75600   -1.63200  6.97800   1.000 34.39739  ? 136 ILE B CG1  1 
ATOM   6647 C CG2  . ILE B 2 136 ? 8.28000   0.49600   5.60600   1.000 36.30510  ? 136 ILE B CG2  1 
ATOM   6648 C CD1  . ILE B 2 136 ? 7.39100   -2.30000  6.54300   1.000 33.67730  ? 136 ILE B CD1  1 
ATOM   6649 H H    . ILE B 2 136 ? 11.40100  -0.20400  6.42200   1.000 34.90723  ? 136 ILE B H    1 
ATOM   6650 H HA   . ILE B 2 136 ? 9.75800   1.43500   7.84000   1.000 36.34309  ? 136 ILE B HA   1 
ATOM   6651 H HB   . ILE B 2 136 ? 7.95900   0.11900   7.61900   1.000 40.80583  ? 136 ILE B HB   1 
ATOM   6652 H HG12 . ILE B 2 136 ? 9.44100   -1.90300  6.34700   1.000 41.27767  ? 136 ILE B HG12 1 
ATOM   6653 H HG13 . ILE B 2 136 ? 8.96300   -1.97200  7.86100   1.000 41.27767  ? 136 ILE B HG13 1 
ATOM   6654 H HG21 . ILE B 2 136 ? 7.44000   0.11200   5.31500   1.000 43.56692  ? 136 ILE B HG21 1 
ATOM   6655 H HG22 . ILE B 2 136 ? 8.18900   1.45800   5.69500   1.000 43.56692  ? 136 ILE B HG22 1 
ATOM   6656 H HG23 . ILE B 2 136 ? 8.97800   0.28900   4.96500   1.000 43.56692  ? 136 ILE B HG23 1 
ATOM   6657 H HD11 . ILE B 2 136 ? 7.44700   -3.25700  6.69100   1.000 40.41356  ? 136 ILE B HD11 1 
ATOM   6658 H HD12 . ILE B 2 136 ? 6.67300   -1.92400  7.07600   1.000 40.41356  ? 136 ILE B HD12 1 
ATOM   6659 H HD13 . ILE B 2 136 ? 7.23500   -2.11900  5.60300   1.000 40.41356  ? 136 ILE B HD13 1 
ATOM   6660 N N    . LYS B 2 137 ? 10.01300  0.24200   9.96700   1.000 29.98733  ? 137 LYS B N    1 
ATOM   6661 C CA   . LYS B 2 137 ? 10.40900  -0.40700  11.21500  1.000 32.43066  ? 137 LYS B CA   1 
ATOM   6662 C C    . LYS B 2 137 ? 9.35500   -1.47300  11.49700  1.000 34.42588  ? 137 LYS B C    1 
ATOM   6663 O O    . LYS B 2 137 ? 8.38300   -1.26600  12.22100  1.000 34.23786  ? 137 LYS B O    1 
ATOM   6664 C CB   . LYS B 2 137 ? 10.56600  0.61400   12.33500  1.000 40.77016  ? 137 LYS B CB   1 
ATOM   6665 C CG   . LYS B 2 137 ? 11.69400  1.61400   11.99500  1.000 43.80141  ? 137 LYS B CG   1 
ATOM   6666 C CD   . LYS B 2 137 ? 11.92000  2.69600   13.04200  1.000 49.83203  ? 137 LYS B CD   1 
ATOM   6667 C CE   . LYS B 2 137 ? 12.67600  2.16000   14.24900  1.000 58.70624  ? 137 LYS B CE   1 
ATOM   6668 N NZ   . LYS B 2 137 ? 14.13100  2.26500   14.04200  1.000 58.95149  ? 137 LYS B NZ   1 
ATOM   6669 H H    . LYS B 2 137 ? 9.48400   0.91300   10.06500  1.000 35.98560  ? 137 LYS B H    1 
ATOM   6670 H HA   . LYS B 2 137 ? 11.26300  -0.85000  11.09100  1.000 38.91759  ? 137 LYS B HA   1 
ATOM   6671 H HB2  . LYS B 2 137 ? 9.73700   1.10400   12.45500  1.000 48.92500  ? 137 LYS B HB2  1 
ATOM   6672 H HB3  . LYS B 2 137 ? 10.81000  0.14700   13.14500  1.000 48.92500  ? 137 LYS B HB3  1 
ATOM   6673 H HG2  . LYS B 2 137 ? 12.52400  1.12200   11.89700  1.000 52.56249  ? 137 LYS B HG2  1 
ATOM   6674 H HG3  . LYS B 2 137 ? 11.47600  2.05600   11.16000  1.000 52.56249  ? 137 LYS B HG3  1 
ATOM   6675 H HD2  . LYS B 2 137 ? 12.44200  3.41500   12.65200  1.000 59.79924  ? 137 LYS B HD2  1 
ATOM   6676 H HD3  . LYS B 2 137 ? 11.06200  3.03100   13.34600  1.000 59.79924  ? 137 LYS B HD3  1 
ATOM   6677 H HE2  . LYS B 2 137 ? 12.44000  2.67800   15.03400  1.000 70.44829  ? 137 LYS B HE2  1 
ATOM   6678 H HE3  . LYS B 2 137 ? 12.45400  1.22500   14.38000  1.000 70.44829  ? 137 LYS B HE3  1 
ATOM   6679 H HZ1  . LYS B 2 137 ? 14.56300  1.94900   14.75300  1.000 70.74259  ? 137 LYS B HZ1  1 
ATOM   6680 H HZ2  . LYS B 2 137 ? 14.37100  1.79500   13.32500  1.000 70.74259  ? 137 LYS B HZ2  1 
ATOM   6681 H HZ3  . LYS B 2 137 ? 14.36000  3.11600   13.91900  1.000 70.74259  ? 137 LYS B HZ3  1 
ATOM   6682 N N    . GLY B 2 138 ? 9.50900   -2.61400  10.82200  1.000 31.93817  ? 138 GLY B N    1 
ATOM   6683 C CA   . GLY B 2 138 ? 8.52300   -3.67300  10.89200  1.000 31.85347  ? 138 GLY B CA   1 
ATOM   6684 C C    . GLY B 2 138 ? 8.88700   -4.70600  11.93500  1.000 32.68537  ? 138 GLY B C    1 
ATOM   6685 O O    . GLY B 2 138 ? 9.83900   -4.55600  12.69400  1.000 33.02452  ? 138 GLY B O    1 
ATOM   6686 H H    . GLY B 2 138 ? 10.18100  -2.79200  10.31600  1.000 38.32661  ? 138 GLY B H    1 
ATOM   6687 H HA2  . GLY B 2 138 ? 7.65600   -3.30000  11.11400  1.000 38.22497  ? 138 GLY B HA2  1 
ATOM   6688 H HA3  . GLY B 2 138 ? 8.45800   -4.11400  10.03000  1.000 38.22497  ? 138 GLY B HA3  1 
ATOM   6689 N N    . SER B 2 139 ? 8.10300   -5.78200  11.96400  1.000 29.20986  ? 139 SER B N    1 
ATOM   6690 C CA   . SER B 2 139 ? 8.36300   -6.93500  12.81600  1.000 27.34758  ? 139 SER B CA   1 
ATOM   6691 C C    . SER B 2 139 ? 8.17100   -8.13600  11.91100  1.000 31.62747  ? 139 SER B C    1 
ATOM   6692 O O    . SER B 2 139 ? 7.04100   -8.47100  11.55100  1.000 27.46195  ? 139 SER B O    1 
ATOM   6693 C CB   . SER B 2 139 ? 7.41800   -7.00000  14.02900  1.000 30.32000  ? 139 SER B CB   1 
ATOM   6694 O OG   . SER B 2 139 ? 7.69500   -8.19600  14.74500  1.000 32.64910  ? 139 SER B OG   1 
ATOM   6695 H H    . SER B 2 139 ? 7.39500   -5.86700  11.48400  1.000 35.05263  ? 139 SER B H    1 
ATOM   6696 H HA   . SER B 2 139 ? 9.28100   -6.91900  13.13000  1.000 32.81789  ? 139 SER B HA   1 
ATOM   6697 H HB2  . SER B 2 139 ? 7.57500   -6.23500  14.60400  1.000 36.38480  ? 139 SER B HB2  1 
ATOM   6698 H HB3  . SER B 2 139 ? 6.49800   -7.01200  13.72300  1.000 36.38480  ? 139 SER B HB3  1 
ATOM   6699 H HG   . SER B 2 139 ? 7.14100   -8.29100  15.36800  1.000 39.17973  ? 139 SER B HG   1 
ATOM   6700 N N    . PHE B 2 140 ? 9.27000   -8.72500  11.46400  1.000 28.58461  ? 140 PHE B N    1 
ATOM   6701 C CA   . PHE B 2 140 ? 9.18900   -9.73600  10.43000  1.000 31.15002  ? 140 PHE B CA   1 
ATOM   6702 C C    . PHE B 2 140 ? 10.23300  -10.79500 10.72800  1.000 35.92682  ? 140 PHE B C    1 
ATOM   6703 O O    . PHE B 2 140 ? 11.35700  -10.45800 11.09500  1.000 37.09765  ? 140 PHE B O    1 
ATOM   6704 C CB   . PHE B 2 140 ? 9.50000   -9.18400  9.04600   1.000 32.14873  ? 140 PHE B CB   1 
ATOM   6705 C CG   . PHE B 2 140 ? 8.43600   -8.29300  8.46300   1.000 28.62784  ? 140 PHE B CG   1 
ATOM   6706 C CD1  . PHE B 2 140 ? 7.19300   -8.82000  8.09800   1.000 31.55415  ? 140 PHE B CD1  1 
ATOM   6707 C CD2  . PHE B 2 140 ? 8.71700   -6.96900  8.18000   1.000 29.53443  ? 140 PHE B CD2  1 
ATOM   6708 C CE1  . PHE B 2 140 ? 6.23600   -7.99600  7.52300   1.000 27.93952  ? 140 PHE B CE1  1 
ATOM   6709 C CE2  . PHE B 2 140 ? 7.75700   -6.13600  7.58600   1.000 30.50004  ? 140 PHE B CE2  1 
ATOM   6710 C CZ   . PHE B 2 140 ? 6.54500   -6.66200  7.25100   1.000 30.14968  ? 140 PHE B CZ   1 
ATOM   6711 H H    . PHE B 2 140 ? 10.06700  -8.55800  11.74100  1.000 34.30234  ? 140 PHE B H    1 
ATOM   6712 H HA   . PHE B 2 140 ? 8.31100   -10.14800 10.42200  1.000 37.38082  ? 140 PHE B HA   1 
ATOM   6713 H HB2  . PHE B 2 140 ? 10.31900  -8.66600  9.09800   1.000 38.57928  ? 140 PHE B HB2  1 
ATOM   6714 H HB3  . PHE B 2 140 ? 9.62500   -9.92900  8.43800   1.000 38.57928  ? 140 PHE B HB3  1 
ATOM   6715 H HD1  . PHE B 2 140 ? 6.99700   -9.71300  8.27000   1.000 37.86578  ? 140 PHE B HD1  1 
ATOM   6716 H HD2  . PHE B 2 140 ? 9.55100   -6.62200  8.39900   1.000 35.44211  ? 140 PHE B HD2  1 
ATOM   6717 H HE1  . PHE B 2 140 ? 5.40300   -8.33900  7.29100   1.000 33.52823  ? 140 PHE B HE1  1 
ATOM   6718 H HE2  . PHE B 2 140 ? 7.94800   -5.24200  7.41400   1.000 36.60085  ? 140 PHE B HE2  1 
ATOM   6719 H HZ   . PHE B 2 140 ? 5.89800   -6.11100  6.87300   1.000 36.18042  ? 140 PHE B HZ   1 
ATOM   6720 N N    . LEU B 2 141 ? 9.87000   -12.05600 10.53500  1.000 34.03904  ? 141 LEU B N    1 
ATOM   6721 C CA   . LEU B 2 141 ? 10.82100  -13.15000 10.66000  1.000 36.60285  ? 141 LEU B CA   1 
ATOM   6722 C C    . LEU B 2 141 ? 10.96900  -13.80500 9.29200   1.000 39.31815  ? 141 LEU B C    1 
ATOM   6723 O O    . LEU B 2 141 ? 10.25300  -13.48100 8.34400   1.000 36.03296  ? 141 LEU B O    1 
ATOM   6724 C CB   . LEU B 2 141 ? 10.37500  -14.17100 11.72300  1.000 34.49698  ? 141 LEU B CB   1 
ATOM   6725 C CG   . LEU B 2 141 ? 10.12400  -13.55400 13.10200  1.000 41.31181  ? 141 LEU B CG   1 
ATOM   6726 C CD1  . LEU B 2 141 ? 9.33500   -14.49600 14.00900  1.000 44.08717  ? 141 LEU B CD1  1 
ATOM   6727 C CD2  . LEU B 2 141 ? 11.45600  -13.18200 13.74000  1.000 47.04737  ? 141 LEU B CD2  1 
ATOM   6728 H H    . LEU B 2 141 ? 9.07300   -12.30600 10.32900  1.000 40.84765  ? 141 LEU B H    1 
ATOM   6729 H HA   . LEU B 2 141 ? 11.68700  -12.80000 10.92200  1.000 43.92422  ? 141 LEU B HA   1 
ATOM   6730 H HB2  . LEU B 2 141 ? 9.55000   -14.58800 11.43000  1.000 41.39717  ? 141 LEU B HB2  1 
ATOM   6731 H HB3  . LEU B 2 141 ? 11.06700  -14.84400 11.82000  1.000 41.39717  ? 141 LEU B HB3  1 
ATOM   6732 H HG   . LEU B 2 141 ? 9.60600   -12.74100 12.99600  1.000 49.57497  ? 141 LEU B HG   1 
ATOM   6733 H HD11 . LEU B 2 141 ? 9.31700   -14.12900 14.90600  1.000 52.90541  ? 141 LEU B HD11 1 
ATOM   6734 H HD12 . LEU B 2 141 ? 8.43100   -14.58000 13.66700  1.000 52.90541  ? 141 LEU B HD12 1 
ATOM   6735 H HD13 . LEU B 2 141 ? 9.77000   -15.36300 14.01600  1.000 52.90541  ? 141 LEU B HD13 1 
ATOM   6736 H HD21 . LEU B 2 141 ? 11.29300  -12.83900 14.63200  1.000 56.45765  ? 141 LEU B HD21 1 
ATOM   6737 H HD22 . LEU B 2 141 ? 12.01500  -13.97300 13.78700  1.000 56.45765  ? 141 LEU B HD22 1 
ATOM   6738 H HD23 . LEU B 2 141 ? 11.88800  -12.50300 13.19800  1.000 56.45765  ? 141 LEU B HD23 1 
ATOM   6739 N N    A ASN B 2 142 ? 11.92500  -14.73100 9.19100   0.490 38.12203  ? 142 ASN B N    1 
ATOM   6740 N N    B ASN B 2 142 ? 11.93600  -14.71600 9.19200   0.510 38.13187  ? 142 ASN B N    1 
ATOM   6741 C CA   A ASN B 2 142 ? 12.07700  -15.51000 7.96700   0.490 40.49655  ? 142 ASN B CA   1 
ATOM   6742 C CA   B ASN B 2 142 ? 12.09200  -15.50900 7.97900   0.510 40.50741  ? 142 ASN B CA   1 
ATOM   6743 C C    A ASN B 2 142 ? 10.74800  -16.15700 7.59400   0.490 36.61608  ? 142 ASN B C    1 
ATOM   6744 C C    B ASN B 2 142 ? 10.76100  -16.15900 7.59800   0.510 36.61324  ? 142 ASN B C    1 
ATOM   6745 O O    A ASN B 2 142 ? 10.03600  -16.70100 8.44300   0.490 38.03400  ? 142 ASN B O    1 
ATOM   6746 O O    B ASN B 2 142 ? 10.05200  -16.70600 8.44900   0.510 38.08439  ? 142 ASN B O    1 
ATOM   6747 C CB   A ASN B 2 142 ? 13.16200  -16.58500 8.15200   0.490 41.58310  ? 142 ASN B CB   1 
ATOM   6748 C CB   B ASN B 2 142 ? 13.18200  -16.57700 8.19200   0.510 40.89216  ? 142 ASN B CB   1 
ATOM   6749 C CG   A ASN B 2 142 ? 13.85200  -16.98200 6.83700   0.490 42.20569  ? 142 ASN B CG   1 
ATOM   6750 C CG   B ASN B 2 142 ? 14.57700  -15.97800 8.46200   0.510 46.80942  ? 142 ASN B CG   1 
ATOM   6751 O OD1  A ASN B 2 142 ? 13.26400  -16.94900 5.75400   0.490 49.42271  ? 142 ASN B OD1  1 
ATOM   6752 O OD1  B ASN B 2 142 ? 14.80200  -14.77400 8.31600   0.510 49.51867  ? 142 ASN B OD1  1 
ATOM   6753 N ND2  A ASN B 2 142 ? 15.11300  -17.37000 6.94500   0.490 46.70769  ? 142 ASN B ND2  1 
ATOM   6754 N ND2  B ASN B 2 142 ? 15.52600  -16.84000 8.82600   0.510 44.98976  ? 142 ASN B ND2  1 
ATOM   6755 H H    A ASN B 2 142 ? 12.49000  -14.92300 9.81000   0.490 45.74724  ? 142 ASN B H    1 
ATOM   6756 H H    B ASN B 2 142 ? 12.51000  -14.89200 9.80800   0.510 45.75904  ? 142 ASN B H    1 
ATOM   6757 H HA   A ASN B 2 142 ? 12.34700  -14.92400 7.24300   0.490 48.59666  ? 142 ASN B HA   1 
ATOM   6758 H HA   B ASN B 2 142 ? 12.36900  -14.93100 7.25100   0.510 48.60969  ? 142 ASN B HA   1 
ATOM   6759 H HB2  A ASN B 2 142 ? 13.84200  -16.24600 8.75500   0.490 49.90053  ? 142 ASN B HB2  1 
ATOM   6760 H HB2  B ASN B 2 142 ? 12.94000  -17.12500 8.95500   0.510 49.07140  ? 142 ASN B HB2  1 
ATOM   6761 H HB3  A ASN B 2 142 ? 12.75500  -17.38100 8.52800   0.490 49.90053  ? 142 ASN B HB3  1 
ATOM   6762 H HB3  B ASN B 2 142 ? 13.24300  -17.12700 7.39600   0.510 49.07140  ? 142 ASN B HB3  1 
ATOM   6763 H HD21 A ASN B 2 142 ? 15.55200  -17.60500 6.24400   0.490 56.05003  ? 142 ASN B HD21 1 
ATOM   6764 H HD21 B ASN B 2 142 ? 16.32300  -16.56000 8.98600   0.510 53.98852  ? 142 ASN B HD21 1 
ATOM   6765 H HD22 A ASN B 2 142 ? 15.49400  -17.38300 7.71600   0.490 56.05003  ? 142 ASN B HD22 1 
ATOM   6766 H HD22 B ASN B 2 142 ? 15.33800  -17.67500 8.91300   0.510 53.98852  ? 142 ASN B HD22 1 
ATOM   6767 N N    . GLY B 2 143 ? 10.40900  -16.08100 6.31100   1.000 36.78001  ? 143 GLY B N    1 
ATOM   6768 C CA   . GLY B 2 143 ? 9.15200   -16.60700 5.81000   1.000 36.05992  ? 143 GLY B CA   1 
ATOM   6769 C C    . GLY B 2 143 ? 8.08700   -15.53500 5.60100   1.000 33.93013  ? 143 GLY B C    1 
ATOM   6770 O O    . GLY B 2 143 ? 6.99400   -15.84300 5.10000   1.000 32.06971  ? 143 GLY B O    1 
ATOM   6771 H H    A GLY B 2 143 ? 10.90100  -15.72300 5.70300   0.490 44.13682  ? 143 GLY B H    1 
ATOM   6772 H H    B GLY B 2 143 ? 10.89700  -15.71900 5.70200   0.510 44.13682  ? 143 GLY B H    1 
ATOM   6773 H HA2  . GLY B 2 143 ? 9.30800   -17.04700 4.96000   1.000 43.27270  ? 143 GLY B HA2  1 
ATOM   6774 H HA3  . GLY B 2 143 ? 8.80400   -17.26500 6.43200   1.000 43.27270  ? 143 GLY B HA3  1 
ATOM   6775 N N    . SER B 2 144 ? 8.37200   -14.29700 5.99300   1.000 30.46603  ? 144 SER B N    1 
ATOM   6776 C CA   . SER B 2 144 ? 7.42300   -13.19900 5.89400   1.000 29.76331  ? 144 SER B CA   1 
ATOM   6777 C C    . SER B 2 144 ? 7.45200   -12.46500 4.54900   1.000 27.43718  ? 144 SER B C    1 
ATOM   6778 O O    . SER B 2 144 ? 6.57500   -11.62400 4.31200   1.000 26.57926  ? 144 SER B O    1 
ATOM   6779 C CB   . SER B 2 144 ? 7.68700   -12.19200 7.02400   1.000 29.55981  ? 144 SER B CB   1 
ATOM   6780 O OG   . SER B 2 144 ? 8.99000   -11.69400 6.87500   1.000 32.56765  ? 144 SER B OG   1 
ATOM   6781 H H    . SER B 2 144 ? 9.12900   -14.06400 6.32800   1.000 36.56003  ? 144 SER B H    1 
ATOM   6782 H HA   . SER B 2 144 ? 6.52900   -13.55100 6.01600   1.000 35.71677  ? 144 SER B HA   1 
ATOM   6783 H HB2  . SER B 2 144 ? 7.05300   -11.46100 6.95900   1.000 35.47257  ? 144 SER B HB2  1 
ATOM   6784 H HB3  . SER B 2 144 ? 7.60700   -12.63500 7.88200   1.000 35.47257  ? 144 SER B HB3  1 
ATOM   6785 H HG   . SER B 2 144 ? 9.55000   -12.30900 6.99500   1.000 39.08198  ? 144 SER B HG   1 
ATOM   6786 N N    . ALA B 2 145 ? 8.44200   -12.72600 3.67900   1.000 28.34804  ? 145 ALA B N    1 
ATOM   6787 C CA   . ALA B 2 145 ? 8.47100   -12.03200 2.40100   1.000 31.76481  ? 145 ALA B CA   1 
ATOM   6788 C C    . ALA B 2 145 ? 7.14200   -12.24000 1.69000   1.000 30.14936  ? 145 ALA B C    1 
ATOM   6789 O O    . ALA B 2 145 ? 6.54200   -13.31600 1.76300   1.000 27.05953  ? 145 ALA B O    1 
ATOM   6790 C CB   . ALA B 2 145 ? 9.62800   -12.53400 1.53200   1.000 33.98578  ? 145 ALA B CB   1 
ATOM   6791 H H    . ALA B 2 145 ? 9.08400   -13.28300 3.80700   1.000 34.01844  ? 145 ALA B H    1 
ATOM   6792 H HA   . ALA B 2 145 ? 8.59200   -11.08200 2.55300   1.000 38.11858  ? 145 ALA B HA   1 
ATOM   6793 H HB1  . ALA B 2 145 ? 9.61700   -12.05800 0.68700   1.000 40.78374  ? 145 ALA B HB1  1 
ATOM   6794 H HB2  . ALA B 2 145 ? 10.46400  -12.36800 1.99400   1.000 40.78374  ? 145 ALA B HB2  1 
ATOM   6795 H HB3  . ALA B 2 145 ? 9.51700   -13.48500 1.37800   1.000 40.78374  ? 145 ALA B HB3  1 
ATOM   6796 N N    . GLY B 2 146 ? 6.65800   -11.19100 1.01200   1.000 26.17077  ? 146 GLY B N    1 
ATOM   6797 C CA   . GLY B 2 146 ? 5.35400   -11.27000 0.39100   1.000 26.14638  ? 146 GLY B CA   1 
ATOM   6798 C C    . GLY B 2 146 ? 4.19800   -10.80500 1.27400   1.000 30.16916  ? 146 GLY B C    1 
ATOM   6799 O O    . GLY B 2 146 ? 3.08900   -10.64200 0.75600   1.000 28.12958  ? 146 GLY B O    1 
ATOM   6800 H H    . GLY B 2 146 ? 7.06500   -10.44100 0.90400   1.000 31.40572  ? 146 GLY B H    1 
ATOM   6801 H HA2  . GLY B 2 146 ? 5.35500   -10.72400 -0.41100  1.000 31.37645  ? 146 GLY B HA2  1 
ATOM   6802 H HA3  . GLY B 2 146 ? 5.18100   -12.18700 0.12800   1.000 31.37645  ? 146 GLY B HA3  1 
ATOM   6803 N N    . SER B 2 147 ? 4.40600   -10.62100 2.59400   1.000 27.37018  ? 147 SER B N    1 
ATOM   6804 C CA   . SER B 2 147 ? 3.39300   -9.94000  3.42200   1.000 26.19156  ? 147 SER B CA   1 
ATOM   6805 C C    . SER B 2 147 ? 3.16700   -8.55600  2.82200   1.000 24.69485  ? 147 SER B C    1 
ATOM   6806 O O    . SER B 2 147 ? 4.05500   -8.00800  2.15200   1.000 25.31830  ? 147 SER B O    1 
ATOM   6807 C CB   . SER B 2 147 ? 3.87800   -9.77500  4.87200   1.000 28.50527  ? 147 SER B CB   1 
ATOM   6808 O OG   . SER B 2 147 ? 4.16100   -11.01600 5.48400   1.000 26.58741  ? 147 SER B OG   1 
ATOM   6809 H H    . SER B 2 147 ? 5.10700   -10.87500 3.02200   1.000 32.84502  ? 147 SER B H    1 
ATOM   6810 H HA   . SER B 2 147 ? 2.55900   -10.43600 3.41400   1.000 31.43068  ? 147 SER B HA   1 
ATOM   6811 H HB2  . SER B 2 147 ? 4.68700   -9.24000  4.86900   1.000 34.20712  ? 147 SER B HB2  1 
ATOM   6812 H HB3  . SER B 2 147 ? 3.19100   -9.32300  5.38300   1.000 34.20712  ? 147 SER B HB3  1 
ATOM   6813 H HG   . SER B 2 147 ? 4.76200   -11.41700 5.05600   1.000 31.90569  ? 147 SER B HG   1 
ATOM   6814 N N    . VAL B 2 148 ? 1.97600   -7.99100  3.01100   1.000 26.44273  ? 148 VAL B N    1 
ATOM   6815 C CA   . VAL B 2 148 ? 1.65100   -6.75200  2.30400   1.000 24.52964  ? 148 VAL B CA   1 
ATOM   6816 C C    . VAL B 2 148 ? 1.21600   -5.66300  3.27800   1.000 24.37782  ? 148 VAL B C    1 
ATOM   6817 O O    . VAL B 2 148 ? 0.75900   -5.92700  4.39700   1.000 24.40652  ? 148 VAL B O    1 
ATOM   6818 C CB   . VAL B 2 148 ? 0.57400   -6.91400  1.19900   1.000 27.21368  ? 148 VAL B CB   1 
ATOM   6819 C CG1  . VAL B 2 148 ? 1.14400   -7.78900  0.01600   1.000 27.55508  ? 148 VAL B CG1  1 
ATOM   6820 C CG2  . VAL B 2 148 ? -0.79200  -7.42200  1.76000   1.000 25.23590  ? 148 VAL B CG2  1 
ATOM   6821 H H    . VAL B 2 148 ? 1.35600   -8.29200  3.52600   1.000 31.73207  ? 148 VAL B H    1 
ATOM   6822 H HA   . VAL B 2 148 ? 2.45100   -6.42700  1.86600   1.000 29.43637  ? 148 VAL B HA   1 
ATOM   6823 H HB   . VAL B 2 148 ? 0.40500   -6.03300  0.82900   1.000 32.65722  ? 148 VAL B HB   1 
ATOM   6824 H HG11 . VAL B 2 148 ? 0.41700   -8.02300  -0.58100  1.000 33.06690  ? 148 VAL B HG11 1 
ATOM   6825 H HG12 . VAL B 2 148 ? 1.81500   -7.27600  -0.46200  1.000 33.06690  ? 148 VAL B HG12 1 
ATOM   6826 H HG13 . VAL B 2 148 ? 1.54100   -8.59400  0.38300   1.000 33.06690  ? 148 VAL B HG13 1 
ATOM   6827 H HG21 . VAL B 2 148 ? -1.40400  -7.56000  1.02100   1.000 30.28388  ? 148 VAL B HG21 1 
ATOM   6828 H HG22 . VAL B 2 148 ? -0.64800  -8.25700  2.23100   1.000 30.28388  ? 148 VAL B HG22 1 
ATOM   6829 H HG23 . VAL B 2 148 ? -1.15200  -6.75700  2.36800   1.000 30.28388  ? 148 VAL B HG23 1 
ATOM   6830 N N    . GLY B 2 149 ? 1.36200   -4.42900  2.79400   1.000 23.75172  ? 149 GLY B N    1 
ATOM   6831 C CA   . GLY B 2 149 ? 0.93500   -3.24500  3.50600   1.000 23.93816  ? 149 GLY B CA   1 
ATOM   6832 C C    . GLY B 2 149 ? -0.17300  -2.56100  2.72700   1.000 23.13869  ? 149 GLY B C    1 
ATOM   6833 O O    . GLY B 2 149 ? -0.20000  -2.60300  1.48600   1.000 25.48294  ? 149 GLY B O    1 
ATOM   6834 H H    . GLY B 2 149 ? 1.71800   -4.25700  2.03000   1.000 28.50286  ? 149 GLY B H    1 
ATOM   6835 H HA2  . GLY B 2 149 ? 0.60900   -3.49700  4.37900   1.000 28.72659  ? 149 GLY B HA2  1 
ATOM   6836 H HA3  . GLY B 2 149 ? 1.67800   -2.63000  3.60900   1.000 28.72659  ? 149 GLY B HA3  1 
ATOM   6837 N N    . PHE B 2 150 ? -1.09300  -1.91600  3.45300   1.000 22.48555  ? 150 PHE B N    1 
ATOM   6838 C CA   . PHE B 2 150 ? -2.28400  -1.40900  2.78800   1.000 23.64548  ? 150 PHE B CA   1 
ATOM   6839 C C    . PHE B 2 150 ? -2.93000  -0.32800  3.64400   1.000 23.05020  ? 150 PHE B C    1 
ATOM   6840 O O    . PHE B 2 150 ? -2.71200  -0.22600  4.86600   1.000 22.91113  ? 150 PHE B O    1 
ATOM   6841 C CB   . PHE B 2 150 ? -3.33700  -2.51900  2.52100   1.000 25.84300  ? 150 PHE B CB   1 
ATOM   6842 C CG   . PHE B 2 150 ? -3.92100  -3.08900  3.80100   1.000 24.21815  ? 150 PHE B CG   1 
ATOM   6843 C CD1  . PHE B 2 150 ? -3.23100  -4.06300  4.51700   1.000 26.25899  ? 150 PHE B CD1  1 
ATOM   6844 C CD2  . PHE B 2 150 ? -5.14700  -2.66000  4.26300   1.000 27.53687  ? 150 PHE B CD2  1 
ATOM   6845 C CE1  . PHE B 2 150 ? -3.74800  -4.55800  5.72100   1.000 28.00279  ? 150 PHE B CE1  1 
ATOM   6846 C CE2  . PHE B 2 150 ? -5.69100  -3.20200  5.43300   1.000 27.68169  ? 150 PHE B CE2  1 
ATOM   6847 C CZ   . PHE B 2 150 ? -4.97800  -4.10700  6.17400   1.000 26.29329  ? 150 PHE B CZ   1 
ATOM   6848 H H    . PHE B 2 150 ? -1.05000  -1.76600  4.29900   1.000 26.98346  ? 150 PHE B H    1 
ATOM   6849 H HA   . PHE B 2 150 ? -2.03400  -1.01500  1.93800   1.000 28.37538  ? 150 PHE B HA   1 
ATOM   6850 H HB2  . PHE B 2 150 ? -4.06400  -2.14600  1.99900   1.000 31.01241  ? 150 PHE B HB2  1 
ATOM   6851 H HB3  . PHE B 2 150 ? -2.91600  -3.24400  2.03400   1.000 31.01241  ? 150 PHE B HB3  1 
ATOM   6852 H HD1  . PHE B 2 150 ? -2.39200  -4.34100  4.22700   1.000 31.51159  ? 150 PHE B HD1  1 
ATOM   6853 H HD2  . PHE B 2 150 ? -5.62600  -2.02500  3.78200   1.000 33.04504  ? 150 PHE B HD2  1 
ATOM   6854 H HE1  . PHE B 2 150 ? -3.28000  -5.20300  6.20100   1.000 33.60415  ? 150 PHE B HE1  1 
ATOM   6855 H HE2  . PHE B 2 150 ? -6.50900  -2.89100  5.74800   1.000 33.21883  ? 150 PHE B HE2  1 
ATOM   6856 H HZ   . PHE B 2 150 ? -5.34500  -4.46200  6.95100   1.000 31.55275  ? 150 PHE B HZ   1 
ATOM   6857 N N    . ASN B 2 151 ? -3.71700  0.49300   2.97200   1.000 23.81394  ? 151 ASN B N    1 
ATOM   6858 C CA   . ASN B 2 151 ? -4.66100  1.38000   3.63800   1.000 23.83641  ? 151 ASN B CA   1 
ATOM   6859 C C    . ASN B 2 151 ? -6.03800  1.07000   3.05900   1.000 26.07286  ? 151 ASN B C    1 
ATOM   6860 O O    . ASN B 2 151 ? -6.16500  0.48100   1.96600   1.000 26.77949  ? 151 ASN B O    1 
ATOM   6861 C CB   . ASN B 2 151 ? -4.31800  2.86400   3.39700   1.000 31.10997  ? 151 ASN B CB   1 
ATOM   6862 C CG   . ASN B 2 151 ? -3.10900  3.32600   4.17800   1.000 31.05697  ? 151 ASN B CG   1 
ATOM   6863 O OD1  . ASN B 2 151 ? -3.21000  3.61800   5.35700   1.000 34.14425  ? 151 ASN B OD1  1 
ATOM   6864 N ND2  . ASN B 2 151 ? -1.95400  3.38200   3.53000   1.000 28.95358  ? 151 ASN B ND2  1 
ATOM   6865 H H    . ASN B 2 151 ? -3.72600  0.55800   2.11500   1.000 28.57753  ? 151 ASN B H    1 
ATOM   6866 H HA   . ASN B 2 151 ? -4.67100  1.20600   4.59200   1.000 28.60449  ? 151 ASN B HA   1 
ATOM   6867 H HB2  . ASN B 2 151 ? -4.13300  2.99500   2.45400   1.000 37.33276  ? 151 ASN B HB2  1 
ATOM   6868 H HB3  . ASN B 2 151 ? -5.07400  3.41000   3.66500   1.000 37.33276  ? 151 ASN B HB3  1 
ATOM   6869 H HD21 . ASN B 2 151 ? -1.24300  3.63900   3.94000   1.000 34.74510  ? 151 ASN B HD21 1 
ATOM   6870 H HD22 . ASN B 2 151 ? -1.91700  3.16700   2.69800   1.000 34.74510  ? 151 ASN B HD22 1 
ATOM   6871 N N    . ILE B 2 152 ? -7.07000  1.50500   3.75700   1.000 25.39829  ? 152 ILE B N    1 
ATOM   6872 C CA   . ILE B 2 152 ? -8.42700  1.44600   3.20600   1.000 29.42864  ? 152 ILE B CA   1 
ATOM   6873 C C    . ILE B 2 152 ? -8.89900  2.88600   3.01200   1.000 43.57447  ? 152 ILE B C    1 
ATOM   6874 O O    . ILE B 2 152 ? -8.90200  3.66600   3.97000   1.000 35.96128  ? 152 ILE B O    1 
ATOM   6875 C CB   . ILE B 2 152 ? -9.38400  0.67400   4.10800   1.000 31.02836  ? 152 ILE B CB   1 
ATOM   6876 C CG1  . ILE B 2 152 ? -8.75700  -0.66600  4.51400   1.000 30.03005  ? 152 ILE B CG1  1 
ATOM   6877 C CG2  . ILE B 2 152 ? -10.76400 0.50100   3.41700   1.000 37.51578  ? 152 ILE B CG2  1 
ATOM   6878 C CD1  . ILE B 2 152 ? -9.71800  -1.49400  5.38900   1.000 32.90314  ? 152 ILE B CD1  1 
ATOM   6879 H H    . ILE B 2 152 ? -7.02100  1.83900   4.54800   1.000 30.47874  ? 152 ILE B H    1 
ATOM   6880 H HA   . ILE B 2 152 ? -8.41100  1.01200   2.34000   1.000 35.31517  ? 152 ILE B HA   1 
ATOM   6881 H HB   . ILE B 2 152 ? -9.51900  1.19600   4.91500   1.000 37.23483  ? 152 ILE B HB   1 
ATOM   6882 H HG12 . ILE B 2 152 ? -8.55200  -1.17900  3.71700   1.000 36.03686  ? 152 ILE B HG12 1 
ATOM   6883 H HG13 . ILE B 2 152 ? -7.95000  -0.50300  5.02600   1.000 36.03686  ? 152 ILE B HG13 1 
ATOM   6884 H HG21 . ILE B 2 152 ? -11.39200 0.12000   4.05000   1.000 45.01974  ? 152 ILE B HG21 1 
ATOM   6885 H HG22 . ILE B 2 152 ? -11.08400 1.36700   3.12100   1.000 45.01974  ? 152 ILE B HG22 1 
ATOM   6886 H HG23 . ILE B 2 152 ? -10.66200 -0.09000  2.65500   1.000 45.01974  ? 152 ILE B HG23 1 
ATOM   6887 H HD11 . ILE B 2 152 ? -9.23000  -2.23700  5.77700   1.000 39.48457  ? 152 ILE B HD11 1 
ATOM   6888 H HD12 . ILE B 2 152 ? -10.07100 -0.92700  6.09200   1.000 39.48457  ? 152 ILE B HD12 1 
ATOM   6889 H HD13 . ILE B 2 152 ? -10.44300 -1.82700  4.83700   1.000 39.48457  ? 152 ILE B HD13 1 
ATOM   6890 N N    . ASP B 2 153 ? -9.12100  3.29500   1.74000   1.000 45.83345  ? 153 ASP B N    1 
ATOM   6891 C CA   . ASP B 2 153 ? -9.73400  4.58900   1.40700   1.000 54.96323  ? 153 ASP B CA   1 
ATOM   6892 C C    . ASP B 2 153 ? -11.21100 4.35300   1.15100   1.000 58.98256  ? 153 ASP B C    1 
ATOM   6893 O O    . ASP B 2 153 ? -11.56500 3.82800   0.08900   1.000 55.17426  ? 153 ASP B O    1 
ATOM   6894 C CB   . ASP B 2 153 ? -9.11300  5.20300   0.15300   1.000 62.41676  ? 153 ASP B CB   1 
ATOM   6895 C CG   . ASP B 2 153 ? -7.60600  5.37000   0.24700   1.000 76.82261  ? 153 ASP B CG   1 
ATOM   6896 O OD1  . ASP B 2 153 ? -7.09600  5.83900   1.29500   1.000 80.63701  ? 153 ASP B OD1  1 
ATOM   6897 O OD2  . ASP B 2 153 ? -6.92800  5.05100   -0.75600  1.000 81.13658  ? 153 ASP B OD2  1 
ATOM   6898 H H    . ASP B 2 153 ? -8.91900  2.82700   1.04800   1.000 55.00094  ? 153 ASP B H    1 
ATOM   6899 H HA   . ASP B 2 153 ? -9.63400  5.20800   2.14700   1.000 65.95667  ? 153 ASP B HA   1 
ATOM   6900 H HB2  . ASP B 2 153 ? -9.30200  4.62800   -0.60500  1.000 74.90092  ? 153 ASP B HB2  1 
ATOM   6901 H HB3  . ASP B 2 153 ? -9.50100  6.08000   0.00700   1.000 74.90092  ? 153 ASP B HB3  1 
ATOM   6902 N N    . TYR B 2 154 ? -12.08000 4.79700   2.06400   1.000 62.57925  ? 154 TYR B N    1 
ATOM   6903 C CA   . TYR B 2 154 ? -13.51000 4.56300   1.86000   1.000 67.94222  ? 154 TYR B CA   1 
ATOM   6904 C C    . TYR B 2 154 ? -13.84700 3.07900   1.82200   1.000 63.63114  ? 154 TYR B C    1 
ATOM   6905 O O    . TYR B 2 154 ? -14.06500 2.44800   2.86000   1.000 56.41418  ? 154 TYR B O    1 
ATOM   6906 C CB   . TYR B 2 154 ? -14.01700 5.24700   0.58700   1.000 75.87324  ? 154 TYR B CB   1 
ATOM   6907 C CG   . TYR B 2 154 ? -13.84400 6.74200   0.59700   1.000 85.68590  ? 154 TYR B CG   1 
ATOM   6908 C CD1  . TYR B 2 154 ? -14.64400 7.53500   1.42200   1.000 86.07033  ? 154 TYR B CD1  1 
ATOM   6909 C CD2  . TYR B 2 154 ? -12.88500 7.36800   -0.19800  1.000 86.46049  ? 154 TYR B CD2  1 
ATOM   6910 C CE1  . TYR B 2 154 ? -14.50200 8.91400   1.44800   1.000 91.65342  ? 154 TYR B CE1  1 
ATOM   6911 C CE2  . TYR B 2 154 ? -12.73500 8.75100   -0.18100  1.000 90.67509  ? 154 TYR B CE2  1 
ATOM   6912 C CZ   . TYR B 2 154 ? -13.54700 9.51500   0.64500   1.000 97.22405  ? 154 TYR B CZ   1 
ATOM   6913 O OH   . TYR B 2 154 ? -13.40500 10.88300  0.67100   1.000 107.18734 ? 154 TYR B OH   1 
ATOM   6914 H H    . TYR B 2 154 ? -11.87600 5.22100   2.78400   1.000 75.09590  ? 154 TYR B H    1 
ATOM   6915 H HA   . TYR B 2 154 ? -13.99200 4.95000   2.60800   1.000 81.53146  ? 154 TYR B HA   1 
ATOM   6916 H HB2  . TYR B 2 154 ? -13.53900 4.91200   -0.18500  1.000 91.04869  ? 154 TYR B HB2  1 
ATOM   6917 H HB3  . TYR B 2 154 ? -14.96400 5.06100   0.49100   1.000 91.04869  ? 154 TYR B HB3  1 
ATOM   6918 H HD1  . TYR B 2 154 ? -15.28700 7.13200   1.95900   1.000 103.28520 ? 154 TYR B HD1  1 
ATOM   6919 H HD2  . TYR B 2 154 ? -12.34300 6.85500   -0.75300  1.000 103.75339 ? 154 TYR B HD2  1 
ATOM   6920 H HE1  . TYR B 2 154 ? -15.04400 9.43100   2.00000   1.000 109.98491 ? 154 TYR B HE1  1 
ATOM   6921 H HE2  . TYR B 2 154 ? -12.09400 9.16000   -0.71700  1.000 108.81091 ? 154 TYR B HE2  1 
ATOM   6922 H HH   . TYR B 2 154 ? -12.79600 11.11900  0.14200   1.000 128.62560 ? 154 TYR B HH   1 
ATOM   6923 N N    . ASP B 2 155 ? -14.05300 2.56000   0.61000   1.000 60.79150  ? 155 ASP B N    1 
ATOM   6924 C CA   . ASP B 2 155 ? -14.37100 1.15700   0.40900   1.000 61.24354  ? 155 ASP B CA   1 
ATOM   6925 C C    . ASP B 2 155 ? -13.24300 0.40900   -0.29600  1.000 56.09403  ? 155 ASP B C    1 
ATOM   6926 O O    . ASP B 2 155 ? -13.36100 -0.79400  -0.54100  1.000 50.40534  ? 155 ASP B O    1 
ATOM   6927 C CB   . ASP B 2 155 ? -15.66300 1.02000   -0.40400  1.000 64.33946  ? 155 ASP B CB   1 
ATOM   6928 C CG   . ASP B 2 155 ? -16.13600 -0.42000  -0.47900  1.000 70.69536  ? 155 ASP B CG   1 
ATOM   6929 O OD1  . ASP B 2 155 ? -16.46500 -0.98500  0.60000   1.000 69.45979  ? 155 ASP B OD1  1 
ATOM   6930 O OD2  . ASP B 2 155 ? -16.15500 -0.98800  -1.60100  1.000 67.42311  ? 155 ASP B OD2  1 
ATOM   6931 H H    . ASP B 2 155 ? -14.00900 2.99700   -0.12700  1.000 72.95060  ? 155 ASP B H    1 
ATOM   6932 H HA   . ASP B 2 155 ? -14.51500 0.73500   1.27000   1.000 73.49306  ? 155 ASP B HA   1 
ATOM   6933 H HB2  . ASP B 2 155 ? -16.36100 1.54600   0.01600   1.000 77.20816  ? 155 ASP B HB2  1 
ATOM   6934 H HB3  . ASP B 2 155 ? -15.50500 1.33400   -1.30800  1.000 77.20816  ? 155 ASP B HB3  1 
ATOM   6935 N N    . CYS B 2 156 ? -12.16400 1.09600   -0.63100  1.000 43.20653  ? 156 CYS B N    1 
ATOM   6936 C CA   . CYS B 2 156 ? -11.12700 0.59700   -1.51900  1.000 41.05304  ? 156 CYS B CA   1 
ATOM   6937 C C    . CYS B 2 156 ? -9.89900  0.21500   -0.70200  1.000 33.36389  ? 156 CYS B C    1 
ATOM   6938 O O    . CYS B 2 156 ? -9.44400  1.00800   0.11600   1.000 34.37847  ? 156 CYS B O    1 
ATOM   6939 C CB   . CYS B 2 156 ? -10.80400 1.69400   -2.53700  1.000 41.69354  ? 156 CYS B CB   1 
ATOM   6940 S SG   . CYS B 2 156 ? -9.76300  1.21900   -3.84500  1.000 46.10062  ? 156 CYS B SG   1 
ATOM   6941 H H    . CYS B 2 156 ? -12.00100 1.88900   -0.34300  1.000 51.84864  ? 156 CYS B H    1 
ATOM   6942 H HA   . CYS B 2 156 ? -11.44600 -0.18700  -1.99300  1.000 49.26445  ? 156 CYS B HA   1 
ATOM   6943 H HB2  . CYS B 2 156 ? -11.63600 2.00600   -2.92600  1.000 50.03305  ? 156 CYS B HB2  1 
ATOM   6944 H HB3  . CYS B 2 156 ? -10.37000 2.42600   -2.07200  1.000 50.03305  ? 156 CYS B HB3  1 
ATOM   6945 H HG   . CYS B 2 156 ? -9.63900  2.14100   -4.60300  1.000 55.32155  ? 156 CYS B HG   1 
ATOM   6946 N N    . VAL B 2 157 ? -9.36100  -0.98500  -0.93100  1.000 29.86507  ? 157 VAL B N    1 
ATOM   6947 C CA   . VAL B 2 157 ? -8.10300  -1.39500  -0.31400  1.000 29.19898  ? 157 VAL B CA   1 
ATOM   6948 C C    . VAL B 2 157 ? -6.96900  -0.88100  -1.19900  1.000 26.21436  ? 157 VAL B C    1 
ATOM   6949 O O    . VAL B 2 157 ? -6.84600  -1.28900  -2.35100  1.000 27.80739  ? 157 VAL B O    1 
ATOM   6950 C CB   . VAL B 2 157 ? -8.00600  -2.91600  -0.17700  1.000 28.36405  ? 157 VAL B CB   1 
ATOM   6951 C CG1  . VAL B 2 157 ? -6.60800  -3.25000  0.40900   1.000 26.71836  ? 157 VAL B CG1  1 
ATOM   6952 C CG2  . VAL B 2 157 ? -9.13000  -3.46400  0.74500   1.000 27.78203  ? 157 VAL B CG2  1 
ATOM   6953 H H    . VAL B 2 157 ? -9.70900  -1.58200  -1.44300  1.000 35.83888  ? 157 VAL B H    1 
ATOM   6954 H HA   . VAL B 2 157 ? -8.02100  -0.99500  0.56600   1.000 35.03958  ? 157 VAL B HA   1 
ATOM   6955 H HB   . VAL B 2 157 ? -8.08700  -3.33100  -1.05000  1.000 34.03766  ? 157 VAL B HB   1 
ATOM   6956 H HG11 . VAL B 2 157 ? -6.62800  -4.14800  0.77400   1.000 32.06284  ? 157 VAL B HG11 1 
ATOM   6957 H HG12 . VAL B 2 157 ? -5.94500  -3.19700  -0.29700  1.000 32.06284  ? 157 VAL B HG12 1 
ATOM   6958 H HG13 . VAL B 2 157 ? -6.40000  -2.61400  1.11200   1.000 32.06284  ? 157 VAL B HG13 1 
ATOM   6959 H HG21 . VAL B 2 157 ? -9.03400  -4.42600  0.82100   1.000 33.33924  ? 157 VAL B HG21 1 
ATOM   6960 H HG22 . VAL B 2 157 ? -9.04900  -3.05300  1.62000   1.000 33.33924  ? 157 VAL B HG22 1 
ATOM   6961 H HG23 . VAL B 2 157 ? -9.99100  -3.24700  0.35600   1.000 33.33924  ? 157 VAL B HG23 1 
ATOM   6962 N N    . SER B 2 158 ? -6.14500  0.00400   -0.69200  1.000 25.19221  ? 158 SER B N    1 
ATOM   6963 C CA   . SER B 2 158 ? -5.02400  0.50300   -1.49800  1.000 26.03950  ? 158 SER B CA   1 
ATOM   6964 C C    . SER B 2 158 ? -3.79000  -0.24100  -1.02200  1.000 24.32566  ? 158 SER B C    1 
ATOM   6965 O O    . SER B 2 158 ? -3.28800  0.02500   0.07900   1.000 23.83382  ? 158 SER B O    1 
ATOM   6966 C CB   . SER B 2 158 ? -4.83800  2.00800   -1.34300  1.000 29.28782  ? 158 SER B CB   1 
ATOM   6967 O OG   . SER B 2 158 ? -5.92900  2.67100   -1.95000  1.000 37.93824  ? 158 SER B OG   1 
ATOM   6968 H H    . SER B 2 158 ? -6.19800  0.33500   0.10000   1.000 30.23145  ? 158 SER B H    1 
ATOM   6969 H HA   . SER B 2 158 ? -5.16700  0.30500   -2.43600  1.000 31.24820  ? 158 SER B HA   1 
ATOM   6970 H HB2  . SER B 2 158 ? -4.80800  2.23400   -0.40000  1.000 35.14618  ? 158 SER B HB2  1 
ATOM   6971 H HB3  . SER B 2 158 ? -4.01600  2.27600   -1.78100  1.000 35.14618  ? 158 SER B HB3  1 
ATOM   6972 H HG   . SER B 2 158 ? -5.83900  3.50300   -1.87200  1.000 45.52669  ? 158 SER B HG   1 
ATOM   6973 N N    . PHE B 2 159 ? -3.30100  -1.15400  -1.83200  1.000 25.39540  ? 159 PHE B N    1 
ATOM   6974 C CA   . PHE B 2 159 ? -2.07800  -1.89600  -1.48800  1.000 23.73403  ? 159 PHE B CA   1 
ATOM   6975 C C    . PHE B 2 159 ? -0.86600  -1.04700  -1.82200  1.000 24.09774  ? 159 PHE B C    1 
ATOM   6976 O O    . PHE B 2 159 ? -0.75200  -0.55600  -2.94500  1.000 26.86300  ? 159 PHE B O    1 
ATOM   6977 C CB   . PHE B 2 159 ? -1.98100  -3.19500  -2.28600  1.000 25.13278  ? 159 PHE B CB   1 
ATOM   6978 C CG   . PHE B 2 159 ? -3.01100  -4.20900  -1.90700  1.000 24.62444  ? 159 PHE B CG   1 
ATOM   6979 C CD1  . PHE B 2 159 ? -2.86100  -4.92500  -0.71100  1.000 23.30269  ? 159 PHE B CD1  1 
ATOM   6980 C CD2  . PHE B 2 159 ? -4.08500  -4.48300  -2.74900  1.000 25.43807  ? 159 PHE B CD2  1 
ATOM   6981 C CE1  . PHE B 2 159 ? -3.84100  -5.88700  -0.33600  1.000 24.82242  ? 159 PHE B CE1  1 
ATOM   6982 C CE2  . PHE B 2 159 ? -5.05600  -5.44700  -2.40300  1.000 26.31180  ? 159 PHE B CE2  1 
ATOM   6983 C CZ   . PHE B 2 159 ? -4.93600  -6.14100  -1.18500  1.000 26.29886  ? 159 PHE B CZ   1 
ATOM   6984 H H    . PHE B 2 159 ? -3.64700  -1.37200  -2.58800  1.000 30.47529  ? 159 PHE B H    1 
ATOM   6985 H HA   . PHE B 2 159 ? -2.06900  -2.10400  -0.54100  1.000 28.48164  ? 159 PHE B HA   1 
ATOM   6986 H HB2  . PHE B 2 159 ? -2.09500  -2.99300  -3.22800  1.000 30.16013  ? 159 PHE B HB2  1 
ATOM   6987 H HB3  . PHE B 2 159 ? -1.10700  -3.58900  -2.13700  1.000 30.16013  ? 159 PHE B HB3  1 
ATOM   6988 H HD1  . PHE B 2 159 ? -2.14600  -4.74200  -0.14500  1.000 27.96403  ? 159 PHE B HD1  1 
ATOM   6989 H HD2  . PHE B 2 159 ? -4.17200  -4.01200  -3.54600  1.000 30.52649  ? 159 PHE B HD2  1 
ATOM   6990 H HE1  . PHE B 2 159 ? -3.75200  -6.35500  0.46200   1.000 29.78771  ? 159 PHE B HE1  1 
ATOM   6991 H HE2  . PHE B 2 159 ? -5.77800  -5.60900  -2.96600  1.000 31.57496  ? 159 PHE B HE2  1 
ATOM   6992 H HZ   . PHE B 2 159 ? -5.56700  -6.78200  -0.95100  1.000 31.55943  ? 159 PHE B HZ   1 
ATOM   6993 N N    . CYS B 2 160 ? 0.04600   -0.88900  -0.84700  1.000 24.79869  ? 160 CYS B N    1 
ATOM   6994 C CA   . CYS B 2 160 ? 1.16600   0.02500   -1.05800  1.000 22.75802  ? 160 CYS B CA   1 
ATOM   6995 C C    . CYS B 2 160 ? 2.51000   -0.61600  -0.79700  1.000 25.96092  ? 160 CYS B C    1 
ATOM   6996 O O    . CYS B 2 160 ? 3.51800   0.00000   -1.14300  1.000 28.44216  ? 160 CYS B O    1 
ATOM   6997 C CB   . CYS B 2 160 ? 1.06500   1.26600   -0.14600  1.000 23.64061  ? 160 CYS B CB   1 
ATOM   6998 S SG   . CYS B 2 160 ? 0.89200   0.91700   1.60400   1.000 26.85290  ? 160 CYS B SG   1 
ATOM   6999 H H    . CYS B 2 160 ? 0.03600   -1.28600  -0.08400  1.000 29.75923  ? 160 CYS B H    1 
ATOM   7000 H HA   . CYS B 2 160 ? 1.16100   0.33000   -1.97700  1.000 27.31043  ? 160 CYS B HA   1 
ATOM   7001 H HB2  . CYS B 2 160 ? 1.86900   1.79700   -0.25900  1.000 28.36953  ? 160 CYS B HB2  1 
ATOM   7002 H HB3  . CYS B 2 160 ? 0.29200   1.78500   -0.41800  1.000 28.36953  ? 160 CYS B HB3  1 
ATOM   7003 H HG   . CYS B 2 160 ? 1.84700   0.29200   1.97400   1.000 32.22428  ? 160 CYS B HG   1 
ATOM   7004 N N    . TYR B 2 161 ? 2.56200   -1.82200  -0.23000  1.000 25.74682  ? 161 TYR B N    1 
ATOM   7005 C CA   . TYR B 2 161 ? 3.86000   -2.36200  0.17600   1.000 22.68703  ? 161 TYR B CA   1 
ATOM   7006 C C    . TYR B 2 161 ? 3.83300   -3.87000  0.05400   1.000 24.03468  ? 161 TYR B C    1 
ATOM   7007 O O    . TYR B 2 161 ? 2.81500   -4.50300  0.38200   1.000 23.57757  ? 161 TYR B O    1 
ATOM   7008 C CB   . TYR B 2 161 ? 4.17500   -1.94900  1.62100   1.000 23.93704  ? 161 TYR B CB   1 
ATOM   7009 C CG   . TYR B 2 161 ? 5.53700   -2.48300  2.13600   1.000 25.16810  ? 161 TYR B CG   1 
ATOM   7010 C CD1  . TYR B 2 161 ? 6.73300   -1.87200  1.76400   1.000 26.65766  ? 161 TYR B CD1  1 
ATOM   7011 C CD2  . TYR B 2 161 ? 5.59200   -3.57200  2.99200   1.000 24.90776  ? 161 TYR B CD2  1 
ATOM   7012 C CE1  . TYR B 2 161 ? 7.98800   -2.36500  2.24900   1.000 27.15192  ? 161 TYR B CE1  1 
ATOM   7013 C CE2  . TYR B 2 161 ? 6.78400   -4.05300  3.49600   1.000 27.26922  ? 161 TYR B CE2  1 
ATOM   7014 C CZ   . TYR B 2 161 ? 7.99600   -3.46800  3.10800   1.000 27.89697  ? 161 TYR B CZ   1 
ATOM   7015 O OH   . TYR B 2 161 ? 9.21100   -3.98600  3.63000   1.000 27.06017  ? 161 TYR B OH   1 
ATOM   7016 H H    . TYR B 2 161 ? 1.88700   -2.33200  -0.07400  1.000 30.89699  ? 161 TYR B H    1 
ATOM   7017 H HA   . TYR B 2 161 ? 4.55600   -2.01600  -0.40300  1.000 27.22523  ? 161 TYR B HA   1 
ATOM   7018 H HB2  . TYR B 2 161 ? 4.19700   -0.98100  1.67200   1.000 28.72525  ? 161 TYR B HB2  1 
ATOM   7019 H HB3  . TYR B 2 161 ? 3.48100   -2.29400  2.20400   1.000 28.72525  ? 161 TYR B HB3  1 
ATOM   7020 H HD1  . TYR B 2 161 ? 6.71700   -1.14300  1.18700   1.000 31.98999  ? 161 TYR B HD1  1 
ATOM   7021 H HD2  . TYR B 2 161 ? 4.79700   -3.97600  3.25600   1.000 29.89012  ? 161 TYR B HD2  1 
ATOM   7022 H HE1  . TYR B 2 161 ? 8.78500   -1.95800  1.99600   1.000 32.58310  ? 161 TYR B HE1  1 
ATOM   7023 H HE2  . TYR B 2 161 ? 6.78500   -4.79100  4.06200   1.000 32.72387  ? 161 TYR B HE2  1 
ATOM   7024 H HH   . TYR B 2 161 ? 9.04900   -4.49500  4.27700   1.000 32.47301  ? 161 TYR B HH   1 
ATOM   7025 N N    . MET B 2 162 ? 4.93800   -4.43900  -0.44900  1.000 24.80530  ? 162 MET B N    1 
ATOM   7026 C CA   . MET B 2 162 ? 5.16300   -5.86800  -0.35200  1.000 24.46183  ? 162 MET B CA   1 
ATOM   7027 C C    . MET B 2 162 ? 6.52800   -6.08500  0.29400   1.000 25.96773  ? 162 MET B C    1 
ATOM   7028 O O    . MET B 2 162 ? 7.53100   -5.49300  -0.13000  1.000 25.59621  ? 162 MET B O    1 
ATOM   7029 C CB   . MET B 2 162 ? 5.11500   -6.57200  -1.72000  1.000 23.17898  ? 162 MET B CB   1 
ATOM   7030 C CG   . MET B 2 162 ? 5.39100   -8.07800  -1.62000  1.000 24.60106  ? 162 MET B CG   1 
ATOM   7031 S SD   . MET B 2 162 ? 5.01000   -8.98700  -3.14200  1.000 36.30122  ? 162 MET B SD   1 
ATOM   7032 C CE   . MET B 2 162 ? 3.28900   -9.44000  -2.70700  1.000 31.66267  ? 162 MET B CE   1 
ATOM   7033 H H    . MET B 2 162 ? 5.56700   -4.01000  -0.85000  1.000 29.76717  ? 162 MET B H    1 
ATOM   7034 H HA   . MET B 2 162 ? 4.48000   -6.26200  0.21300   1.000 29.35500  ? 162 MET B HA   1 
ATOM   7035 H HB2  . MET B 2 162 ? 4.23300   -6.45300  -2.10600  1.000 27.81558  ? 162 MET B HB2  1 
ATOM   7036 H HB3  . MET B 2 162 ? 5.78700   -6.18200  -2.30000  1.000 27.81558  ? 162 MET B HB3  1 
ATOM   7037 H HG2  . MET B 2 162 ? 6.33100   -8.21300  -1.42300  1.000 29.52207  ? 162 MET B HG2  1 
ATOM   7038 H HG3  . MET B 2 162 ? 4.84800   -8.45000  -0.90800  1.000 29.52207  ? 162 MET B HG3  1 
ATOM   7039 H HE1  . MET B 2 162 ? 2.89600   -9.93100  -3.44500  1.000 37.99601  ? 162 MET B HE1  1 
ATOM   7040 H HE2  . MET B 2 162 ? 3.30000   -9.99200  -1.91000  1.000 37.99601  ? 162 MET B HE2  1 
ATOM   7041 H HE3  . MET B 2 162 ? 2.78200   -8.63000  -2.54200  1.000 37.99601  ? 162 MET B HE3  1 
ATOM   7042 N N    . HIS B 2 163 ? 6.55700   -6.91000  1.33500   1.000 25.92916  ? 163 HIS B N    1 
ATOM   7043 C CA   . HIS B 2 163 ? 7.77900   -7.07600  2.10500   1.000 24.98254  ? 163 HIS B CA   1 
ATOM   7044 C C    . HIS B 2 163 ? 8.76700   -7.97500  1.36600   1.000 28.50627  ? 163 HIS B C    1 
ATOM   7045 O O    . HIS B 2 163 ? 8.38800   -9.03700  0.86000   1.000 27.59006  ? 163 HIS B O    1 
ATOM   7046 C CB   . HIS B 2 163 ? 7.47300   -7.68600  3.46900   1.000 25.65029  ? 163 HIS B CB   1 
ATOM   7047 C CG   . HIS B 2 163 ? 8.71200   -7.83800  4.29300   1.000 28.35603  ? 163 HIS B CG   1 
ATOM   7048 N ND1  . HIS B 2 163 ? 9.59000   -6.79200  4.47100   1.000 29.63605  ? 163 HIS B ND1  1 
ATOM   7049 C CD2  . HIS B 2 163 ? 9.27600   -8.91700  4.88100   1.000 30.55814  ? 163 HIS B CD2  1 
ATOM   7050 C CE1  . HIS B 2 163 ? 10.62600  -7.20800  5.18600   1.000 29.91502  ? 163 HIS B CE1  1 
ATOM   7051 N NE2  . HIS B 2 163 ? 10.44200  -8.48700  5.47900   1.000 29.07265  ? 163 HIS B NE2  1 
ATOM   7052 H H    . HIS B 2 163 ? 5.89100   -7.37900  1.61200   1.000 31.11579  ? 163 HIS B H    1 
ATOM   7053 H HA   . HIS B 2 163 ? 8.19500   -6.21000  2.24200   1.000 29.97985  ? 163 HIS B HA   1 
ATOM   7054 H HB2  . HIS B 2 163 ? 6.85900   -7.10800  3.94800   1.000 30.78115  ? 163 HIS B HB2  1 
ATOM   7055 H HB3  . HIS B 2 163 ? 7.08000   -8.56400  3.34600   1.000 30.78115  ? 163 HIS B HB3  1 
ATOM   7056 H HD2  . HIS B 2 163 ? 8.91100   -9.77100  4.93300   1.000 36.67057  ? 163 HIS B HD2  1 
ATOM   7057 H HE1  . HIS B 2 163 ? 11.34200  -6.68400  5.46500   1.000 35.89882  ? 163 HIS B HE1  1 
ATOM   7058 H HE2  . HIS B 2 163 ? 10.98600  -8.98100  5.92500   1.000 34.88798  ? 163 HIS B HE2  1 
ATOM   7059 N N    . HIS B 2 164 ? 10.04400  -7.57000  1.35100   1.000 27.09288  ? 164 HIS B N    1 
ATOM   7060 C CA   . HIS B 2 164 ? 11.08000  -8.39100  0.75000   1.000 29.43766  ? 164 HIS B CA   1 
ATOM   7061 C C    . HIS B 2 164 ? 12.14900  -8.82800  1.73500   1.000 36.34774  ? 164 HIS B C    1 
ATOM   7062 O O    . HIS B 2 164 ? 12.48600  -10.02500 1.75900   1.000 34.54046  ? 164 HIS B O    1 
ATOM   7063 C CB   . HIS B 2 164 ? 11.76000  -7.65300  -0.43000  1.000 28.81228  ? 164 HIS B CB   1 
ATOM   7064 C CG   . HIS B 2 164 ? 10.86200  -7.53600  -1.63200  1.000 29.34398  ? 164 HIS B CG   1 
ATOM   7065 N ND1  . HIS B 2 164 ? 11.14700  -8.13000  -2.84100  1.000 32.35841  ? 164 HIS B ND1  1 
ATOM   7066 C CD2  . HIS B 2 164 ? 9.67200   -6.90400  -1.78900  1.000 27.18759  ? 164 HIS B CD2  1 
ATOM   7067 C CE1  . HIS B 2 164 ? 10.17000  -7.86800  -3.69800  1.000 33.15102  ? 164 HIS B CE1  1 
ATOM   7068 N NE2  . HIS B 2 164 ? 9.25400   -7.13500  -3.07800  1.000 28.70978  ? 164 HIS B NE2  1 
ATOM   7069 H H    . HIS B 2 164 ? 10.32600  -6.82800  1.68200   1.000 32.51226  ? 164 HIS B H    1 
ATOM   7070 H HA   . HIS B 2 164 ? 10.67400  -9.19500  0.39100   1.000 35.32599  ? 164 HIS B HA   1 
ATOM   7071 H HB2  . HIS B 2 164 ? 12.00100  -6.75700  -0.14700  1.000 34.57554  ? 164 HIS B HB2  1 
ATOM   7072 H HB3  . HIS B 2 164 ? 12.55400  -8.14300  -0.69500  1.000 34.57554  ? 164 HIS B HB3  1 
ATOM   7073 H HD2  . HIS B 2 164 ? 9.21700   -6.42100  -1.14000  1.000 32.62591  ? 164 HIS B HD2  1 
ATOM   7074 H HE1  . HIS B 2 164 ? 10.13000  -8.15600  -4.58100  1.000 39.78202  ? 164 HIS B HE1  1 
ATOM   7075 H HE2  . HIS B 2 164 ? 8.53100   -6.83200  -3.43200  1.000 34.45254  ? 164 HIS B HE2  1 
ATOM   7076 N N    . MET B 2 165 ? 12.75200  -7.90300  2.49000   1.000 30.63371  ? 165 MET B N    1 
ATOM   7077 C CA   . MET B 2 165 ? 13.94500  -8.31100  3.22200   1.000 31.42001  ? 165 MET B CA   1 
ATOM   7078 C C    . MET B 2 165 ? 14.18600  -7.46400  4.46000   1.000 31.14842  ? 165 MET B C    1 
ATOM   7079 O O    . MET B 2 165 ? 13.62700  -6.37700  4.63200   1.000 31.02915  ? 165 MET B O    1 
ATOM   7080 C CB   . MET B 2 165 ? 15.17300  -8.22200  2.31300   1.000 29.43884  ? 165 MET B CB   1 
ATOM   7081 C CG   . MET B 2 165 ? 15.45900  -6.80400  1.98700   1.000 34.63098  ? 165 MET B CG   1 
ATOM   7082 S SD   . MET B 2 165 ? 16.40900  -6.63600  0.44600   1.000 52.24013  ? 165 MET B SD   1 
ATOM   7083 C CE   . MET B 2 165 ? 16.77100  -4.89100  0.54600   1.000 45.44841  ? 165 MET B CE   1 
ATOM   7084 H H    . MET B 2 165 ? 12.50700  -7.08500  2.59000   1.000 36.76126  ? 165 MET B H    1 
ATOM   7085 H HA   . MET B 2 165 ? 13.84700  -9.23500  3.49800   1.000 37.70482  ? 165 MET B HA   1 
ATOM   7086 H HB2  . MET B 2 165 ? 15.94300  -8.59500  2.76900   1.000 35.32740  ? 165 MET B HB2  1 
ATOM   7087 H HB3  . MET B 2 165 ? 15.00100  -8.70000  1.48700   1.000 35.32740  ? 165 MET B HB3  1 
ATOM   7088 H HG2  . MET B 2 165 ? 14.62500  -6.32200  1.88000   1.000 41.55798  ? 165 MET B HG2  1 
ATOM   7089 H HG3  . MET B 2 165 ? 15.98200  -6.41200  2.70400   1.000 41.55798  ? 165 MET B HG3  1 
ATOM   7090 H HE1  . MET B 2 165 ? 17.35300  -4.64800  -0.19100  1.000 54.53890  ? 165 MET B HE1  1 
ATOM   7091 H HE2  . MET B 2 165 ? 15.94100  -4.39300  0.49100   1.000 54.53890  ? 165 MET B HE2  1 
ATOM   7092 H HE3  . MET B 2 165 ? 17.21300  -4.70800  1.39000   1.000 54.53890  ? 165 MET B HE3  1 
ATOM   7093 N N    . GLU B 2 166 ? 15.14300  -7.92400  5.26600   1.000 31.72958  ? 166 GLU B N    1 
ATOM   7094 C CA   . GLU B 2 166 ? 15.57800  -7.21800  6.45700   1.000 35.59261  ? 166 GLU B CA   1 
ATOM   7095 C C    . GLU B 2 166 ? 17.01100  -6.72600  6.30100   1.000 35.39981  ? 166 GLU B C    1 
ATOM   7096 O O    . GLU B 2 166 ? 17.89300  -7.48100  5.87900   1.000 37.29865  ? 166 GLU B O    1 
ATOM   7097 C CB   . GLU B 2 166 ? 15.48000  -8.12700  7.67000   1.000 38.29098  ? 166 GLU B CB   1 
ATOM   7098 C CG   . GLU B 2 166 ? 15.89100  -7.42800  8.94400   1.000 34.39807  ? 166 GLU B CG   1 
ATOM   7099 C CD   . GLU B 2 166 ? 15.53100  -8.24100  10.16600  1.000 41.72923  ? 166 GLU B CD   1 
ATOM   7100 O OE1  . GLU B 2 166 ? 14.31600  -8.53400  10.35800  1.000 40.35161  ? 166 GLU B OE1  1 
ATOM   7101 O OE2  . GLU B 2 166 ? 16.46800  -8.56500  10.94000  1.000 40.86271  ? 166 GLU B OE2  1 
ATOM   7102 H H    . GLU B 2 166 ? 15.56300  -8.66300  5.13500   1.000 38.07630  ? 166 GLU B H    1 
ATOM   7103 H HA   . GLU B 2 166 ? 15.00600  -6.44900  6.60600   1.000 42.71193  ? 166 GLU B HA   1 
ATOM   7104 H HB2  . GLU B 2 166 ? 14.56200  -8.42300  7.77100   1.000 45.94998  ? 166 GLU B HB2  1 
ATOM   7105 H HB3  . GLU B 2 166 ? 16.06500  -8.89000  7.54300   1.000 45.94998  ? 166 GLU B HB3  1 
ATOM   7106 H HG2  . GLU B 2 166 ? 16.85200  -7.29600  8.94300   1.000 41.27849  ? 166 GLU B HG2  1 
ATOM   7107 H HG3  . GLU B 2 166 ? 15.43500  -6.57400  9.00200   1.000 41.27849  ? 166 GLU B HG3  1 
ATOM   7108 N N    . LEU B 2 167 ? 17.25000  -5.47900  6.65300   1.000 36.55543  ? 167 LEU B N    1 
ATOM   7109 C CA   . LEU B 2 167 ? 18.58400  -4.88700  6.57800   1.000 38.87368  ? 167 LEU B CA   1 
ATOM   7110 C C    . LEU B 2 167 ? 19.35900  -5.18500  7.85800   1.000 43.80674  ? 167 LEU B C    1 
ATOM   7111 O O    . LEU B 2 167 ? 18.79600  -5.64000  8.84800   1.000 38.58443  ? 167 LEU B O    1 
ATOM   7112 C CB   . LEU B 2 167 ? 18.46400  -3.38000  6.37500   1.000 34.15257  ? 167 LEU B CB   1 
ATOM   7113 C CG   . LEU B 2 167 ? 17.71000  -3.00200  5.08800   1.000 38.36486  ? 167 LEU B CG   1 
ATOM   7114 C CD1  . LEU B 2 167 ? 17.37900  -1.52000  5.09700   1.000 38.52481  ? 167 LEU B CD1  1 
ATOM   7115 C CD2  . LEU B 2 167 ? 18.62600  -3.30800  3.91200   1.000 41.48893  ? 167 LEU B CD2  1 
ATOM   7116 H H    . LEU B 2 167 ? 16.64800  -4.93900  6.94500   1.000 43.86731  ? 167 LEU B H    1 
ATOM   7117 H HA   . LEU B 2 167 ? 19.06600  -5.26700  5.82800   1.000 46.64922  ? 167 LEU B HA   1 
ATOM   7118 H HB2  . LEU B 2 167 ? 17.96100  -3.01400  7.12000   1.000 40.98388  ? 167 LEU B HB2  1 
ATOM   7119 H HB3  . LEU B 2 167 ? 19.32800  -2.95800  6.33800   1.000 40.98388  ? 167 LEU B HB3  1 
ATOM   7120 H HG   . LEU B 2 167 ? 16.89200  -3.51700  5.00500   1.000 46.03864  ? 167 LEU B HG   1 
ATOM   7121 H HD11 . LEU B 2 167 ? 16.92400  -1.29400  4.27100   1.000 46.23057  ? 167 LEU B HD11 1 
ATOM   7122 H HD12 . LEU B 2 167 ? 16.80400  -1.33000  5.85400   1.000 46.23057  ? 167 LEU B HD12 1 
ATOM   7123 H HD13 . LEU B 2 167 ? 18.20300  -1.01300  5.17100   1.000 46.23057  ? 167 LEU B HD13 1 
ATOM   7124 H HD21 . LEU B 2 167 ? 18.21900  -2.96800  3.10000   1.000 49.78752  ? 167 LEU B HD21 1 
ATOM   7125 H HD22 . LEU B 2 167 ? 19.48300  -2.87700  4.05800   1.000 49.78752  ? 167 LEU B HD22 1 
ATOM   7126 H HD23 . LEU B 2 167 ? 18.74600  -4.26800  3.84400   1.000 49.78752  ? 167 LEU B HD23 1 
ATOM   7127 N N    . PRO B 2 168 ? 20.66700  -4.91200  7.87900   1.000 41.69844  ? 168 PRO B N    1 
ATOM   7128 C CA   . PRO B 2 168 ? 21.48000  -5.34000  9.02700   1.000 43.28015  ? 168 PRO B CA   1 
ATOM   7129 C C    . PRO B 2 168 ? 21.14000  -4.64300  10.31900  1.000 45.81044  ? 168 PRO B C    1 
ATOM   7130 O O    . PRO B 2 168 ? 21.41000  -5.21700  11.37900  1.000 55.22572  ? 168 PRO B O    1 
ATOM   7131 C CB   . PRO B 2 168 ? 22.92100  -5.03400  8.59500   1.000 50.73900  ? 168 PRO B CB   1 
ATOM   7132 C CG   . PRO B 2 168 ? 22.82600  -4.18500  7.35800   1.000 50.46290  ? 168 PRO B CG   1 
ATOM   7133 C CD   . PRO B 2 168 ? 21.47800  -4.44500  6.73900   1.000 41.89534  ? 168 PRO B CD   1 
ATOM   7134 H HA   . PRO B 2 168 ? 21.38900  -6.29700  9.15500   1.000 51.93699  ? 168 PRO B HA   1 
ATOM   7135 H HB2  . PRO B 2 168 ? 23.37500  -4.55100  9.30300   1.000 60.88760  ? 168 PRO B HB2  1 
ATOM   7136 H HB3  . PRO B 2 168 ? 23.38300  -5.86500  8.40100   1.000 60.88760  ? 168 PRO B HB3  1 
ATOM   7137 H HG2  . PRO B 2 168 ? 22.90900  -3.25000  7.60400   1.000 60.55629  ? 168 PRO B HG2  1 
ATOM   7138 H HG3  . PRO B 2 168 ? 23.53300  -4.43500  6.74300   1.000 60.55629  ? 168 PRO B HG3  1 
ATOM   7139 H HD2  . PRO B 2 168 ? 21.14900  -3.62100  6.36400   1.000 50.27521  ? 168 PRO B HD2  1 
ATOM   7140 H HD3  . PRO B 2 168 ? 21.54500  -5.13900  6.06500   1.000 50.27521  ? 168 PRO B HD3  1 
ATOM   7141 N N    . THR B 2 169 ? 20.56600  -3.43800  10.28400  1.000 42.36952  ? 169 THR B N    1 
ATOM   7142 C CA   . THR B 2 169 ? 20.11400  -2.80400  11.51900  1.000 47.51715  ? 169 THR B CA   1 
ATOM   7143 C C    . THR B 2 169 ? 18.78200  -3.34200  12.00200  1.000 46.04526  ? 169 THR B C    1 
ATOM   7144 O O    . THR B 2 169 ? 18.27100  -2.87700  13.03400  1.000 46.32576  ? 169 THR B O    1 
ATOM   7145 C CB   . THR B 2 169 ? 20.00800  -1.29300  11.33900  1.000 52.24196  ? 169 THR B CB   1 
ATOM   7146 O OG1  . THR B 2 169 ? 19.28100  -1.01500  10.14100  1.000 51.01826  ? 169 THR B OG1  1 
ATOM   7147 C CG2  . THR B 2 169 ? 21.40300  -0.69900  11.22500  1.000 57.91132  ? 169 THR B CG2  1 
ATOM   7148 H H    . THR B 2 169 ? 20.43000  -2.97600  9.57100   1.000 50.84423  ? 169 THR B H    1 
ATOM   7149 H HA   . THR B 2 169 ? 20.77000  -2.97300  12.21400  1.000 57.02138  ? 169 THR B HA   1 
ATOM   7150 H HB   . THR B 2 169 ? 19.55700  -0.89800  12.10100  1.000 62.69116  ? 169 THR B HB   1 
ATOM   7151 H HG1  . THR B 2 169 ? 19.21600  -0.18500  10.03100  1.000 61.22272  ? 169 THR B HG1  1 
ATOM   7152 H HG21 . THR B 2 169 ? 21.34500  0.26300   11.11100  1.000 69.49439  ? 169 THR B HG21 1 
ATOM   7153 H HG22 . THR B 2 169 ? 21.91200  -0.89200  12.02800  1.000 69.49439  ? 169 THR B HG22 1 
ATOM   7154 H HG23 . THR B 2 169 ? 21.86400  -1.08000  10.46100  1.000 69.49439  ? 169 THR B HG23 1 
ATOM   7155 N N    . GLY B 2 170 ? 18.20100  -4.30800  11.30300  1.000 42.97813  ? 170 GLY B N    1 
ATOM   7156 C CA   . GLY B 2 170 ? 16.95300  -4.87200  11.76700  1.000 35.21508  ? 170 GLY B CA   1 
ATOM   7157 C C    . GLY B 2 170 ? 15.68600  -4.17700  11.28100  1.000 36.92853  ? 170 GLY B C    1 
ATOM   7158 O O    . GLY B 2 170 ? 14.59600  -4.53600  11.73700  1.000 40.26541  ? 170 GLY B O    1 
ATOM   7159 H H    . GLY B 2 170 ? 18.50300  -4.64600  10.57200  1.000 51.57455  ? 170 GLY B H    1 
ATOM   7160 H HA2  . GLY B 2 170 ? 16.90700  -5.79800  11.48200  1.000 42.25889  ? 170 GLY B HA2  1 
ATOM   7161 H HA3  . GLY B 2 170 ? 16.94400  -4.86100  12.73700  1.000 42.25889  ? 170 GLY B HA3  1 
ATOM   7162 N N    . VAL B 2 171 ? 15.80200  -3.17500  10.40800  1.000 37.66942  ? 171 VAL B N    1 
ATOM   7163 C CA   . VAL B 2 171 ? 14.65100  -2.55300  9.75700   1.000 33.55840  ? 171 VAL B CA   1 
ATOM   7164 C C    . VAL B 2 171 ? 14.46400  -3.22000  8.39800   1.000 32.14955  ? 171 VAL B C    1 
ATOM   7165 O O    . VAL B 2 171 ? 15.27000  -4.06200  7.97700   1.000 31.79243  ? 171 VAL B O    1 
ATOM   7166 C CB   . VAL B 2 171 ? 14.81100  -1.03000  9.60100   1.000 35.01351  ? 171 VAL B CB   1 
ATOM   7167 C CG1  . VAL B 2 171 ? 15.01700  -0.36400  11.01800  1.000 39.19742  ? 171 VAL B CG1  1 
ATOM   7168 C CG2  . VAL B 2 171 ? 15.94600  -0.69400  8.56300   1.000 37.28853  ? 171 VAL B CG2  1 
ATOM   7169 H H    . VAL B 2 171 ? 16.55400  -2.83200  10.17300  1.000 45.20411  ? 171 VAL B H    1 
ATOM   7170 H HA   . VAL B 2 171 ? 13.85600  -2.71900  10.28700  1.000 40.27088  ? 171 VAL B HA   1 
ATOM   7171 H HB   . VAL B 2 171 ? 13.98300  -0.67700  9.24000   1.000 42.01701  ? 171 VAL B HB   1 
ATOM   7172 H HG11 . VAL B 2 171 ? 15.09300  0.59700   10.90700  1.000 47.03770  ? 171 VAL B HG11 1 
ATOM   7173 H HG12 . VAL B 2 171 ? 14.25300  -0.57300  11.57900  1.000 47.03770  ? 171 VAL B HG12 1 
ATOM   7174 H HG13 . VAL B 2 171 ? 15.82800  -0.71600  11.41800  1.000 47.03770  ? 171 VAL B HG13 1 
ATOM   7175 H HG21 . VAL B 2 171 ? 16.20100  0.23700   8.66400   1.000 44.74704  ? 171 VAL B HG21 1 
ATOM   7176 H HG22 . VAL B 2 171 ? 16.71000  -1.26700  8.73300   1.000 44.74704  ? 171 VAL B HG22 1 
ATOM   7177 H HG23 . VAL B 2 171 ? 15.60800  -0.84900  7.66700   1.000 44.74704  ? 171 VAL B HG23 1 
ATOM   7178 N N    . HIS B 2 172 ? 13.40900  -2.83100  7.68900   1.000 32.30148  ? 172 HIS B N    1 
ATOM   7179 C CA   . HIS B 2 172 ? 12.91000  -3.65800  6.60300   1.000 31.09800  ? 172 HIS B CA   1 
ATOM   7180 C C    . HIS B 2 172 ? 12.76300  -2.86000  5.31300   1.000 30.40603  ? 172 HIS B C    1 
ATOM   7181 O O    . HIS B 2 172 ? 12.55900  -1.64200  5.33000   1.000 31.71917  ? 172 HIS B O    1 
ATOM   7182 C CB   . HIS B 2 172 ? 11.60200  -4.28500  7.03500   1.000 33.15011  ? 172 HIS B CB   1 
ATOM   7183 C CG   . HIS B 2 172 ? 11.76600  -5.15100  8.24900   1.000 31.76019  ? 172 HIS B CG   1 
ATOM   7184 N ND1  . HIS B 2 172 ? 11.33500  -4.77600  9.50500   1.000 29.97700  ? 172 HIS B ND1  1 
ATOM   7185 C CD2  . HIS B 2 172 ? 12.41600  -6.33200  8.40700   1.000 32.47202  ? 172 HIS B CD2  1 
ATOM   7186 C CE1  . HIS B 2 172 ? 11.64900  -5.72400  10.37200  1.000 29.69762  ? 172 HIS B CE1  1 
ATOM   7187 N NE2  . HIS B 2 172 ? 12.31500  -6.67600  9.73700   1.000 30.85286  ? 172 HIS B NE2  1 
ATOM   7188 H H    . HIS B 2 172 ? 12.97100  -2.10200  7.81600   1.000 38.76258  ? 172 HIS B H    1 
ATOM   7189 H HA   . HIS B 2 172 ? 13.53800  -4.37700  6.43300   1.000 37.31840  ? 172 HIS B HA   1 
ATOM   7190 H HB2  . HIS B 2 172 ? 10.97100  -3.58100  7.25200   1.000 39.78094  ? 172 HIS B HB2  1 
ATOM   7191 H HB3  . HIS B 2 172 ? 11.25600  -4.82900  6.31300   1.000 39.78094  ? 172 HIS B HB3  1 
ATOM   7192 H HD2  . HIS B 2 172 ? 12.82500  -6.83100  7.73700   1.000 38.96723  ? 172 HIS B HD2  1 
ATOM   7193 H HE1  . HIS B 2 172 ? 11.45400  -5.71300  11.28100  1.000 35.63795  ? 172 HIS B HE1  1 
ATOM   7194 H HE2  . HIS B 2 172 ? 12.62800  -7.39300  10.09400  1.000 37.02424  ? 172 HIS B HE2  1 
ATOM   7195 N N    . ALA B 2 173 ? 12.84200  -3.56800  4.20300   1.000 29.63027  ? 173 ALA B N    1 
ATOM   7196 C CA   . ALA B 2 173 ? 12.75800  -2.94900  2.88800   1.000 29.38514  ? 173 ALA B CA   1 
ATOM   7197 C C    . ALA B 2 173 ? 11.85500  -3.77200  1.98500   1.000 28.89711  ? 173 ALA B C    1 
ATOM   7198 O O    . ALA B 2 173 ? 11.79200  -5.00100  2.08800   1.000 31.28661  ? 173 ALA B O    1 
ATOM   7199 C CB   . ALA B 2 173 ? 14.12500  -2.81000  2.25600   1.000 31.72279  ? 173 ALA B CB   1 
ATOM   7200 H H    . ALA B 2 173 ? 12.94600  -4.42100  4.18000   1.000 35.55713  ? 173 ALA B H    1 
ATOM   7201 H HA   . ALA B 2 173 ? 12.37200  -2.06400  2.97500   1.000 35.26297  ? 173 ALA B HA   1 
ATOM   7202 H HB1  . ALA B 2 173 ? 14.02800  -2.40300  1.38100   1.000 38.06815  ? 173 ALA B HB1  1 
ATOM   7203 H HB2  . ALA B 2 173 ? 14.67900  -2.25000  2.82200   1.000 38.06815  ? 173 ALA B HB2  1 
ATOM   7204 H HB3  . ALA B 2 173 ? 14.52300  -3.69000  2.16900   1.000 38.06815  ? 173 ALA B HB3  1 
ATOM   7205 N N    . GLY B 2 174 ? 11.14500  -3.08700  1.10900   1.000 27.58183  ? 174 GLY B N    1 
ATOM   7206 C CA   . GLY B 2 174 ? 10.28100  -3.79000  0.20100   1.000 27.05529  ? 174 GLY B CA   1 
ATOM   7207 C C    . GLY B 2 174 ? 9.87900   -2.88700  -0.95300  1.000 27.61260  ? 174 GLY B C    1 
ATOM   7208 O O    . GLY B 2 174 ? 10.50800  -1.86100  -1.22900  1.000 27.36105  ? 174 GLY B O    1 
ATOM   7209 H H    . GLY B 2 174 ? 11.14700  -2.23100  1.02400   1.000 33.09900  ? 174 GLY B H    1 
ATOM   7210 H HA2  . GLY B 2 174 ? 10.74000  -4.56700  -0.15500  1.000 32.46715  ? 174 GLY B HA2  1 
ATOM   7211 H HA3  . GLY B 2 174 ? 9.48200   -4.08400  0.66400   1.000 32.46715  ? 174 GLY B HA3  1 
ATOM   7212 N N    . THR B 2 175 ? 8.82400   -3.29400  -1.65300  1.000 26.99133  ? 175 THR B N    1 
ATOM   7213 C CA   . THR B 2 175 ? 8.48700   -2.66000  -2.91500  1.000 25.93537  ? 175 THR B CA   1 
ATOM   7214 C C    . THR B 2 175 ? 7.03600   -2.21400  -2.82500  1.000 26.31738  ? 175 THR B C    1 
ATOM   7215 O O    . THR B 2 175 ? 6.30600   -2.58200  -1.89100  1.000 26.66614  ? 175 THR B O    1 
ATOM   7216 C CB   . THR B 2 175 ? 8.64700   -3.61600  -4.12800  1.000 29.12333  ? 175 THR B CB   1 
ATOM   7217 O OG1  . THR B 2 175 ? 7.71000   -4.71100  -3.99800  1.000 28.09979  ? 175 THR B OG1  1 
ATOM   7218 C CG2  . THR B 2 175 ? 10.10600  -4.12800  -4.23800  1.000 31.80624  ? 175 THR B CG2  1 
ATOM   7219 H H    . THR B 2 175 ? 8.29400   -3.92900  -1.41900  1.000 32.39040  ? 175 THR B H    1 
ATOM   7220 H HA   . THR B 2 175 ? 9.04300   -1.87900  -3.05800  1.000 31.12325  ? 175 THR B HA   1 
ATOM   7221 H HB   . THR B 2 175 ? 8.44300   -3.12600  -4.94000  1.000 34.94880  ? 175 THR B HB   1 
ATOM   7222 H HG1  . THR B 2 175 ? 6.92300   -4.43100  -4.09000  1.000 33.72055  ? 175 THR B HG1  1 
ATOM   7223 H HG21 . THR B 2 175 ? 10.15700  -4.83700  -4.89800  1.000 38.16829  ? 175 THR B HG21 1 
ATOM   7224 H HG22 . THR B 2 175 ? 10.69300  -3.40500  -4.50800  1.000 38.16829  ? 175 THR B HG22 1 
ATOM   7225 H HG23 . THR B 2 175 ? 10.40200  -4.47400  -3.38200  1.000 38.16829  ? 175 THR B HG23 1 
ATOM   7226 N N    . ASP B 2 176 ? 6.62600   -1.41600  -3.81000  1.000 28.37986  ? 176 ASP B N    1 
ATOM   7227 C CA   . ASP B 2 176 ? 5.20000   -1.30300  -4.05800  1.000 28.32247  ? 176 ASP B CA   1 
ATOM   7228 C C    . ASP B 2 176 ? 4.74000   -2.56900  -4.79200  1.000 27.75634  ? 176 ASP B C    1 
ATOM   7229 O O    . ASP B 2 176 ? 5.54600   -3.46700  -5.09900  1.000 27.84622  ? 176 ASP B O    1 
ATOM   7230 C CB   . ASP B 2 176 ? 4.91100   -0.01400  -4.82900  1.000 27.62133  ? 176 ASP B CB   1 
ATOM   7231 C CG   . ASP B 2 176 ? 5.59600   0.05000   -6.18400  1.000 31.41200  ? 176 ASP B CG   1 
ATOM   7232 O OD1  . ASP B 2 176 ? 5.91500   -0.97600  -6.82500  1.000 29.75977  ? 176 ASP B OD1  1 
ATOM   7233 O OD2  . ASP B 2 176 ? 5.80000   1.19000   -6.65700  1.000 32.40528  ? 176 ASP B OD2  1 
ATOM   7234 H H    . ASP B 2 176 ? 7.13200   -0.95000  -4.32600  1.000 34.05663  ? 176 ASP B H    1 
ATOM   7235 H HA   . ASP B 2 176 ? 4.73000   -1.25800  -3.21100  1.000 33.98777  ? 176 ASP B HA   1 
ATOM   7236 H HB2  . ASP B 2 176 ? 3.95500   0.05600   -4.97600  1.000 33.14639  ? 176 ASP B HB2  1 
ATOM   7237 H HB3  . ASP B 2 176 ? 5.22000   0.74100   -4.30400  1.000 33.14639  ? 176 ASP B HB3  1 
ATOM   7238 N N    . LEU B 2 177 ? 3.44300   -2.62900  -5.12400  1.000 26.95614  ? 177 LEU B N    1 
ATOM   7239 C CA   . LEU B 2 177 ? 2.89800   -3.82400  -5.74600  1.000 28.73717  ? 177 LEU B CA   1 
ATOM   7240 C C    . LEU B 2 177 ? 3.19300   -3.88800  -7.23000  1.000 31.14565  ? 177 LEU B C    1 
ATOM   7241 O O    . LEU B 2 177 ? 2.83300   -4.87400  -7.87600  1.000 32.45512  ? 177 LEU B O    1 
ATOM   7242 C CB   . LEU B 2 177 ? 1.36300   -3.89600  -5.50800  1.000 26.64688  ? 177 LEU B CB   1 
ATOM   7243 C CG   . LEU B 2 177 ? 0.99000   -4.68800  -4.25800  1.000 24.80943  ? 177 LEU B CG   1 
ATOM   7244 C CD1  . LEU B 2 177 ? 1.37500   -6.15800  -4.47300  1.000 29.45055  ? 177 LEU B CD1  1 
ATOM   7245 C CD2  . LEU B 2 177 ? 1.70100   -4.11400  -2.97300  1.000 24.39930  ? 177 LEU B CD2  1 
ATOM   7246 H H    . LEU B 2 177 ? 2.87300   -1.99700  -4.99900  1.000 32.34816  ? 177 LEU B H    1 
ATOM   7247 H HA   . LEU B 2 177 ? 3.31000   -4.59800  -5.33400  1.000 34.48540  ? 177 LEU B HA   1 
ATOM   7248 H HB2  . LEU B 2 177 ? 1.01800   -2.99600  -5.40500  1.000 31.97706  ? 177 LEU B HB2  1 
ATOM   7249 H HB3  . LEU B 2 177 ? 0.94500   -4.32400  -6.27100  1.000 31.97706  ? 177 LEU B HB3  1 
ATOM   7250 H HG   . LEU B 2 177 ? 0.03100   -4.64100  -4.12300  1.000 29.77212  ? 177 LEU B HG   1 
ATOM   7251 H HD11 . LEU B 2 177 ? 0.86400   -6.70900  -3.86000  1.000 35.34147  ? 177 LEU B HD11 1 
ATOM   7252 H HD12 . LEU B 2 177 ? 1.17300   -6.40700  -5.38800  1.000 35.34147  ? 177 LEU B HD12 1 
ATOM   7253 H HD13 . LEU B 2 177 ? 2.32300   -6.26800  -4.30200  1.000 35.34147  ? 177 LEU B HD13 1 
ATOM   7254 H HD21 . LEU B 2 177 ? 1.35800   -4.57500  -2.19200  1.000 29.27997  ? 177 LEU B HD21 1 
ATOM   7255 H HD22 . LEU B 2 177 ? 2.65700   -4.25800  -3.04800  1.000 29.27997  ? 177 LEU B HD22 1 
ATOM   7256 H HD23 . LEU B 2 177 ? 1.51200   -3.16500  -2.90600  1.000 29.27997  ? 177 LEU B HD23 1 
ATOM   7257 N N    . GLU B 2 178 ? 3.84200   -2.86700  -7.79300  1.000 31.70056  ? 178 GLU B N    1 
ATOM   7258 C CA   . GLU B 2 178 ? 4.38000   -2.95300  -9.12400  1.000 33.65565  ? 178 GLU B CA   1 
ATOM   7259 C C    . GLU B 2 178 ? 5.84500   -3.35100  -9.10100  1.000 34.88682  ? 178 GLU B C    1 
ATOM   7260 O O    . GLU B 2 178 ? 6.48900   -3.31100  -10.13700 1.000 36.89655  ? 178 GLU B O    1 
ATOM   7261 C CB   . GLU B 2 178 ? 4.18600   -1.62300  -9.86400  1.000 33.03577  ? 178 GLU B CB   1 
ATOM   7262 C CG   . GLU B 2 178 ? 2.71300   -1.23600  -9.74600  1.000 44.56051  ? 178 GLU B CG   1 
ATOM   7263 C CD   . GLU B 2 178 ? 2.28900   -0.08700  -10.60100 1.000 47.53065  ? 178 GLU B CD   1 
ATOM   7264 O OE1  . GLU B 2 178 ? 3.15700   0.67600   -11.06300 1.000 49.10341  ? 178 GLU B OE1  1 
ATOM   7265 O OE2  . GLU B 2 178 ? 1.05200   0.10900   -10.69900 1.000 56.78466  ? 178 GLU B OE2  1 
ATOM   7266 H H    . GLU B 2 178 ? 3.97900   -2.10900  -7.41100  1.000 38.04147  ? 178 GLU B H    1 
ATOM   7267 H HA   . GLU B 2 178 ? 3.89700   -3.63500  -9.61600  1.000 40.38758  ? 178 GLU B HA   1 
ATOM   7268 H HB2  . GLU B 2 178 ? 4.72800   -0.93200  -9.45200  1.000 39.64373  ? 178 GLU B HB2  1 
ATOM   7269 H HB3  . GLU B 2 178 ? 4.41000   -1.72900  -10.80200 1.000 39.64373  ? 178 GLU B HB3  1 
ATOM   7270 H HG2  . GLU B 2 178 ? 2.17200   -2.00200  -9.99400  1.000 53.47342  ? 178 GLU B HG2  1 
ATOM   7271 H HG3  . GLU B 2 178 ? 2.52800   -0.99100  -8.82600  1.000 53.47342  ? 178 GLU B HG3  1 
ATOM   7272 N N    . GLY B 2 179 ? 6.39000   -3.69500  -7.93600  1.000 34.37540  ? 179 GLY B N    1 
ATOM   7273 C CA   . GLY B 2 179 ? 7.75000   -4.21500  -7.86000  1.000 32.80523  ? 179 GLY B CA   1 
ATOM   7274 C C    . GLY B 2 179 ? 8.86600   -3.18700  -7.76900  1.000 31.93778  ? 179 GLY B C    1 
ATOM   7275 O O    . GLY B 2 179 ? 10.03200  -3.56700  -7.86800  1.000 33.10616  ? 179 GLY B O    1 
ATOM   7276 H H    . GLY B 2 179 ? 5.99400   -3.63700  -7.17500  1.000 41.25129  ? 179 GLY B H    1 
ATOM   7277 H HA2  . GLY B 2 179 ? 7.81800   -4.78400  -7.07800  1.000 39.36708  ? 179 GLY B HA2  1 
ATOM   7278 H HA3  . GLY B 2 179 ? 7.91700   -4.76400  -8.64200  1.000 39.36708  ? 179 GLY B HA3  1 
ATOM   7279 N N    . ASN B 2 180 ? 8.55000   -1.90300  -7.62800  1.000 33.40494  ? 180 ASN B N    1 
ATOM   7280 C CA   . ASN B 2 180 ? 9.55800   -0.85000  -7.53100  1.000 34.54824  ? 180 ASN B CA   1 
ATOM   7281 C C    . ASN B 2 180 ? 9.95600   -0.74400  -6.06000  1.000 30.69734  ? 180 ASN B C    1 
ATOM   7282 O O    . ASN B 2 180 ? 9.09400   -0.53500  -5.20700  1.000 29.63857  ? 180 ASN B O    1 
ATOM   7283 C CB   . ASN B 2 180 ? 9.00800   0.51600   -7.97000  1.000 34.09588  ? 180 ASN B CB   1 
ATOM   7284 C CG   . ASN B 2 180 ? 8.34500   0.51500   -9.36400  1.000 39.94078  ? 180 ASN B CG   1 
ATOM   7285 O OD1  . ASN B 2 180 ? 7.12400   0.75500   -9.50200  1.000 39.56033  ? 180 ASN B OD1  1 
ATOM   7286 N ND2  . ASN B 2 180 ? 9.14100   0.36000   -10.37600 1.000 34.47254  ? 180 ASN B ND2  1 
ATOM   7287 H H    . ASN B 2 180 ? 7.74200   -1.61000  -7.58500  1.000 40.08672  ? 180 ASN B H    1 
ATOM   7288 H HA   . ASN B 2 180 ? 10.33800  -1.07300  -8.06300  1.000 41.45869  ? 180 ASN B HA   1 
ATOM   7289 H HB2  . ASN B 2 180 ? 8.34200   0.80400   -7.32700  1.000 40.91586  ? 180 ASN B HB2  1 
ATOM   7290 H HB3  . ASN B 2 180 ? 9.73900   1.15300   -7.99200  1.000 40.91586  ? 180 ASN B HB3  1 
ATOM   7291 H HD21 . ASN B 2 180 ? 8.82600   0.36000   -11.17600 1.000 41.36785  ? 180 ASN B HD21 1 
ATOM   7292 H HD22 . ASN B 2 180 ? 9.97700   0.21600   -10.24300 1.000 41.36785  ? 180 ASN B HD22 1 
ATOM   7293 N N    . PHE B 2 181 ? 11.25200  -0.85200  -5.75700  1.000 31.50030  ? 181 PHE B N    1 
ATOM   7294 C CA   . PHE B 2 181 ? 11.64700  -0.69700  -4.36200  1.000 30.07191  ? 181 PHE B CA   1 
ATOM   7295 C C    . PHE B 2 181 ? 11.31500  0.69000   -3.83600  1.000 30.25070  ? 181 PHE B C    1 
ATOM   7296 O O    . PHE B 2 181 ? 11.45800  1.69100   -4.55500  1.000 33.72230  ? 181 PHE B O    1 
ATOM   7297 C CB   . PHE B 2 181 ? 13.16400  -0.95300  -4.17100  1.000 32.42407  ? 181 PHE B CB   1 
ATOM   7298 C CG   . PHE B 2 181 ? 13.43200  -2.31400  -3.68000  1.000 32.23721  ? 181 PHE B CG   1 
ATOM   7299 C CD1  . PHE B 2 181 ? 13.34200  -2.58500  -2.33800  1.000 31.29810  ? 181 PHE B CD1  1 
ATOM   7300 C CD2  . PHE B 2 181 ? 13.72200  -3.34200  -4.56300  1.000 34.14733  ? 181 PHE B CD2  1 
ATOM   7301 C CE1  . PHE B 2 181 ? 13.54200  -3.88000  -1.85000  1.000 34.54261  ? 181 PHE B CE1  1 
ATOM   7302 C CE2  . PHE B 2 181 ? 13.91000  -4.63000  -4.09200  1.000 39.07950  ? 181 PHE B CE2  1 
ATOM   7303 C CZ   . PHE B 2 181 ? 13.81600  -4.89500  -2.72000  1.000 37.68607  ? 181 PHE B CZ   1 
ATOM   7304 H H    . PHE B 2 181 ? 11.89100  -1.00700  -6.31200  1.000 37.80116  ? 181 PHE B H    1 
ATOM   7305 H HA   . PHE B 2 181 ? 11.16500  -1.34200  -3.82300  1.000 36.08710  ? 181 PHE B HA   1 
ATOM   7306 H HB2  . PHE B 2 181 ? 13.61600  -0.84300  -5.02200  1.000 38.90968  ? 181 PHE B HB2  1 
ATOM   7307 H HB3  . PHE B 2 181 ? 13.51400  -0.32300  -3.52200  1.000 38.90968  ? 181 PHE B HB3  1 
ATOM   7308 H HD1  . PHE B 2 181 ? 13.13600  -1.89900  -1.74500  1.000 37.55852  ? 181 PHE B HD1  1 
ATOM   7309 H HD2  . PHE B 2 181 ? 13.76600  -3.17100  -5.47600  1.000 40.97760  ? 181 PHE B HD2  1 
ATOM   7310 H HE1  . PHE B 2 181 ? 13.48300  -4.05000  -0.93800  1.000 41.45193  ? 181 PHE B HE1  1 
ATOM   7311 H HE2  . PHE B 2 181 ? 14.11200  -5.31800  -4.68400  1.000 46.89620  ? 181 PHE B HE2  1 
ATOM   7312 H HZ   . PHE B 2 181 ? 13.96800  -5.75500  -2.40000  1.000 45.22409  ? 181 PHE B HZ   1 
ATOM   7313 N N    . TYR B 2 182 ? 10.93400  0.74800   -2.56400  1.000 29.02364  ? 182 TYR B N    1 
ATOM   7314 C CA   . TYR B 2 182 ? 11.07300  1.96800   -1.79500  1.000 29.32165  ? 182 TYR B CA   1 
ATOM   7315 C C    . TYR B 2 182 ? 12.52900  2.06100   -1.34000  1.000 34.22270  ? 182 TYR B C    1 
ATOM   7316 O O    . TYR B 2 182 ? 13.04600  1.12600   -0.72300  1.000 32.61659  ? 182 TYR B O    1 
ATOM   7317 C CB   . TYR B 2 182 ? 10.14500  1.97400   -0.57300  1.000 29.98203  ? 182 TYR B CB   1 
ATOM   7318 C CG   . TYR B 2 182 ? 8.66200   2.05200   -0.93800  1.000 28.33906  ? 182 TYR B CG   1 
ATOM   7319 C CD1  . TYR B 2 182 ? 8.07500   3.26600   -1.24900  1.000 34.58089  ? 182 TYR B CD1  1 
ATOM   7320 C CD2  . TYR B 2 182 ? 7.85700   0.89200   -0.98400  1.000 28.57831  ? 182 TYR B CD2  1 
ATOM   7321 C CE1  . TYR B 2 182 ? 6.71900   3.34100   -1.57400  1.000 35.24551  ? 182 TYR B CE1  1 
ATOM   7322 C CE2  . TYR B 2 182 ? 6.49800   0.95600   -1.34100  1.000 26.34059  ? 182 TYR B CE2  1 
ATOM   7323 C CZ   . TYR B 2 182 ? 5.94200   2.18100   -1.61100  1.000 27.99641  ? 182 TYR B CZ   1 
ATOM   7324 O OH   . TYR B 2 182 ? 4.60800   2.29900   -1.94000  1.000 27.23921  ? 182 TYR B OH   1 
ATOM   7325 H H    . TYR B 2 182 ? 10.59200  0.09100   -2.12700  1.000 34.82917  ? 182 TYR B H    1 
ATOM   7326 H HA   . TYR B 2 182 ? 10.86700  2.73600   -2.35100  1.000 35.18678  ? 182 TYR B HA   1 
ATOM   7327 H HB2  . TYR B 2 182 ? 10.28500  1.15800   -0.06800  1.000 35.97923  ? 182 TYR B HB2  1 
ATOM   7328 H HB3  . TYR B 2 182 ? 10.35700  2.74300   -0.02200  1.000 35.97923  ? 182 TYR B HB3  1 
ATOM   7329 H HD1  . TYR B 2 182 ? 8.58400   4.04400   -1.21700  1.000 41.49787  ? 182 TYR B HD1  1 
ATOM   7330 H HD2  . TYR B 2 182 ? 8.23800   0.06600   -0.79100  1.000 34.29477  ? 182 TYR B HD2  1 
ATOM   7331 H HE1  . TYR B 2 182 ? 6.33400   4.16400   -1.77300  1.000 42.29542  ? 182 TYR B HE1  1 
ATOM   7332 H HE2  . TYR B 2 182 ? 5.97600   0.18700   -1.35300  1.000 31.60950  ? 182 TYR B HE2  1 
ATOM   7333 H HH   . TYR B 2 182 ? 4.24200   1.54300   -1.93100  1.000 32.68786  ? 182 TYR B HH   1 
ATOM   7334 N N    . GLY B 2 183 ? 13.16500  3.18600   -1.60000  1.000 33.51284  ? 183 GLY B N    1 
ATOM   7335 C CA   . GLY B 2 183 ? 14.53300  3.39900   -1.18000  1.000 39.42720  ? 183 GLY B CA   1 
ATOM   7336 C C    . GLY B 2 183 ? 15.57500  2.81100   -2.12300  1.000 35.97894  ? 183 GLY B C    1 
ATOM   7337 O O    . GLY B 2 183 ? 15.27300  2.07300   -3.07200  1.000 31.81954  ? 183 GLY B O    1 
ATOM   7338 H H    . GLY B 2 183 ? 12.82100  3.85100   -2.02400  1.000 40.21621  ? 183 GLY B H    1 
ATOM   7339 H HA2  . GLY B 2 183 ? 14.69300  4.35300   -1.10800  1.000 47.31344  ? 183 GLY B HA2  1 
ATOM   7340 H HA3  . GLY B 2 183 ? 14.66100  3.00200   -0.30400  1.000 47.31344  ? 183 GLY B HA3  1 
ATOM   7341 N N    . PRO B 2 184 ? 16.86000  3.05200   -1.80400  1.000 36.12194  ? 184 PRO B N    1 
ATOM   7342 C CA   . PRO B 2 184 ? 17.97200  2.68200   -2.68700  1.000 38.36988  ? 184 PRO B CA   1 
ATOM   7343 C C    . PRO B 2 184 ? 18.42300  1.22300   -2.54000  1.000 43.00419  ? 184 PRO B C    1 
ATOM   7344 O O    . PRO B 2 184 ? 19.61200  0.93200   -2.38100  1.000 40.77426  ? 184 PRO B O    1 
ATOM   7345 C CB   . PRO B 2 184 ? 19.08100  3.65900   -2.26700  1.000 38.43522  ? 184 PRO B CB   1 
ATOM   7346 C CG   . PRO B 2 184 ? 18.81700  3.89400   -0.77400  1.000 40.32826  ? 184 PRO B CG   1 
ATOM   7347 C CD   . PRO B 2 184 ? 17.29300  3.80800   -0.62500  1.000 39.88371  ? 184 PRO B CD   1 
ATOM   7348 H HA   . PRO B 2 184 ? 17.73100  2.85000   -3.61100  1.000 46.04466  ? 184 PRO B HA   1 
ATOM   7349 H HB2  . PRO B 2 184 ? 19.95300  3.26000   -2.40700  1.000 46.12307  ? 184 PRO B HB2  1 
ATOM   7350 H HB3  . PRO B 2 184 ? 18.99600  4.48600   -2.76600  1.000 46.12307  ? 184 PRO B HB3  1 
ATOM   7351 H HG2  . PRO B 2 184 ? 19.25300  3.20300   -0.25100  1.000 48.39471  ? 184 PRO B HG2  1 
ATOM   7352 H HG3  . PRO B 2 184 ? 19.13800  4.77300   -0.51900  1.000 48.39471  ? 184 PRO B HG3  1 
ATOM   7353 H HD2  . PRO B 2 184 ? 17.06100  3.32900   0.18600   1.000 47.86125  ? 184 PRO B HD2  1 
ATOM   7354 H HD3  . PRO B 2 184 ? 16.90600  4.69800   -0.63400  1.000 47.86125  ? 184 PRO B HD3  1 
ATOM   7355 N N    . PHE B 2 185 ? 17.46200  0.31100   -2.51300  1.000 35.92911  ? 185 PHE B N    1 
ATOM   7356 C CA   . PHE B 2 185 ? 17.69900  -1.08800  -2.18900  1.000 33.15751  ? 185 PHE B CA   1 
ATOM   7357 C C    . PHE B 2 185 ? 17.50400  -2.01600  -3.39100  1.000 39.67250  ? 185 PHE B C    1 
ATOM   7358 O O    . PHE B 2 185 ? 16.83600  -1.68100  -4.38500  1.000 40.40460  ? 185 PHE B O    1 
ATOM   7359 C CB   . PHE B 2 185 ? 16.81500  -1.48900  -0.98300  1.000 33.25256  ? 185 PHE B CB   1 
ATOM   7360 C CG   . PHE B 2 185 ? 17.00800  -0.58500  0.22400   1.000 35.87707  ? 185 PHE B CG   1 
ATOM   7361 C CD1  . PHE B 2 185 ? 18.25600  -0.52600  0.86900   1.000 38.18528  ? 185 PHE B CD1  1 
ATOM   7362 C CD2  . PHE B 2 185 ? 15.97600  0.22700   0.68000   1.000 36.96138  ? 185 PHE B CD2  1 
ATOM   7363 C CE1  . PHE B 2 185 ? 18.47200  0.32700   1.94900   1.000 39.79631  ? 185 PHE B CE1  1 
ATOM   7364 C CE2  . PHE B 2 185 ? 16.17500  1.07600   1.78700   1.000 36.34722  ? 185 PHE B CE2  1 
ATOM   7365 C CZ   . PHE B 2 185 ? 17.39900  1.13100   2.41100   1.000 41.34701  ? 185 PHE B CZ   1 
ATOM   7366 H H    . PHE B 2 185 ? 16.63700  0.48400   -2.68500  1.000 43.11573  ? 185 PHE B H    1 
ATOM   7367 H HA   . PHE B 2 185 ? 18.62200  -1.18300  -1.90700  1.000 39.78982  ? 185 PHE B HA   1 
ATOM   7368 H HB2  . PHE B 2 185 ? 15.88300  -1.44100  -1.24600  1.000 39.90388  ? 185 PHE B HB2  1 
ATOM   7369 H HB3  . PHE B 2 185 ? 17.03800  -2.39500  -0.71700  1.000 39.90388  ? 185 PHE B HB3  1 
ATOM   7370 H HD1  . PHE B 2 185 ? 18.95600  -1.05300  0.55700   1.000 45.82314  ? 185 PHE B HD1  1 
ATOM   7371 H HD2  . PHE B 2 185 ? 15.14600  0.19900   0.26200   1.000 44.35446  ? 185 PHE B HD2  1 
ATOM   7372 H HE1  . PHE B 2 185 ? 19.29800  0.35000   2.37500   1.000 47.75637  ? 185 PHE B HE1  1 
ATOM   7373 H HE2  . PHE B 2 185 ? 15.47800  1.61200   2.09000   1.000 43.61746  ? 185 PHE B HE2  1 
ATOM   7374 H HZ   . PHE B 2 185 ? 17.52300  1.69500   3.14000   1.000 49.61721  ? 185 PHE B HZ   1 
ATOM   7375 N N    . VAL B 2 186 ? 18.15200  -3.18900  -3.31600  1.000 37.00024  ? 186 VAL B N    1 
ATOM   7376 C CA   . VAL B 2 186 ? 18.07300  -4.21700  -4.35400  1.000 41.43896  ? 186 VAL B CA   1 
ATOM   7377 C C    . VAL B 2 186 ? 17.78500  -5.57400  -3.71500  1.000 40.03072  ? 186 VAL B C    1 
ATOM   7378 O O    . VAL B 2 186 ? 18.10000  -5.81000  -2.54400  1.000 38.28195  ? 186 VAL B O    1 
ATOM   7379 C CB   . VAL B 2 186 ? 19.37200  -4.29100  -5.19200  1.000 40.77494  ? 186 VAL B CB   1 
ATOM   7380 C CG1  . VAL B 2 186 ? 19.64100  -2.95700  -5.86300  1.000 42.95468  ? 186 VAL B CG1  1 
ATOM   7381 C CG2  . VAL B 2 186 ? 20.55400  -4.73500  -4.31100  1.000 48.96482  ? 186 VAL B CG2  1 
ATOM   7382 H H    . VAL B 2 186 ? 18.65500  -3.41300  -2.65500  1.000 44.40109  ? 186 VAL B H    1 
ATOM   7383 H HA   . VAL B 2 186 ? 17.34100  -4.00700  -4.95400  1.000 49.72755  ? 186 VAL B HA   1 
ATOM   7384 H HB   . VAL B 2 186 ? 19.25600  -4.95500  -5.88900  1.000 48.93073  ? 186 VAL B HB   1 
ATOM   7385 H HG11 . VAL B 2 186 ? 20.43500  -3.03600  -6.41400  1.000 51.54642  ? 186 VAL B HG11 1 
ATOM   7386 H HG12 . VAL B 2 186 ? 18.87800  -2.72200  -6.41300  1.000 51.54642  ? 186 VAL B HG12 1 
ATOM   7387 H HG13 . VAL B 2 186 ? 19.77800  -2.28200  -5.18000  1.000 51.54642  ? 186 VAL B HG13 1 
ATOM   7388 H HG21 . VAL B 2 186 ? 21.32100  -4.90400  -4.88100  1.000 58.75859  ? 186 VAL B HG21 1 
ATOM   7389 H HG22 . VAL B 2 186 ? 20.76100  -4.02300  -3.68600  1.000 58.75859  ? 186 VAL B HG22 1 
ATOM   7390 H HG23 . VAL B 2 186 ? 20.32400  -5.54000  -3.82500  1.000 58.75859  ? 186 VAL B HG23 1 
ATOM   7391 N N    . ASP B 2 187 ? 17.17400  -6.47700  -4.48200  1.000 38.74563  ? 187 ASP B N    1 
ATOM   7392 C CA   . ASP B 2 187 ? 16.82000  -7.79100  -3.93700  1.000 46.08212  ? 187 ASP B CA   1 
ATOM   7393 C C    . ASP B 2 187 ? 17.89700  -8.83900  -4.22500  1.000 51.22923  ? 187 ASP B C    1 
ATOM   7394 O O    . ASP B 2 187 ? 17.67700  -9.85600  -4.88400  1.000 56.60825  ? 187 ASP B O    1 
ATOM   7395 C CB   . ASP B 2 187 ? 15.46700  -8.23700  -4.46300  1.000 41.51853  ? 187 ASP B CB   1 
ATOM   7396 C CG   . ASP B 2 187 ? 15.40200  -8.32000  -5.97300  1.000 38.93560  ? 187 ASP B CG   1 
ATOM   7397 O OD1  . ASP B 2 187 ? 16.36200  -7.95200  -6.68400  1.000 40.74893  ? 187 ASP B OD1  1 
ATOM   7398 O OD2  . ASP B 2 187 ? 14.34000  -8.75900  -6.44700  1.000 40.57115  ? 187 ASP B OD2  1 
ATOM   7399 H H    . ASP B 2 187 ? 16.95700  -6.35800  -5.30600  1.000 46.49556  ? 187 ASP B H    1 
ATOM   7400 H HA   . ASP B 2 187 ? 16.74100  -7.71500  -2.97300  1.000 55.29934  ? 187 ASP B HA   1 
ATOM   7401 H HB2  . ASP B 2 187 ? 15.26800  -9.11700  -4.10800  1.000 49.82304  ? 187 ASP B HB2  1 
ATOM   7402 H HB3  . ASP B 2 187 ? 14.79300  -7.60400  -4.17100  1.000 49.82304  ? 187 ASP B HB3  1 
ATOM   7403 N N    . ARG B 2 188 ? 19.07800  -8.56600  -3.69500  1.000 53.96087  ? 188 ARG B N    1 
ATOM   7404 C CA   . ARG B 2 188 ? 20.17400  -9.55400  -3.80700  1.000 57.26141  ? 188 ARG B CA   1 
ATOM   7405 C C    . ARG B 2 188 ? 21.00300  -9.46900  -2.52900  1.000 66.15615  ? 188 ARG B C    1 
ATOM   7406 O O    . ARG B 2 188 ? 20.86900  -8.47000  -1.80000  1.000 57.70355  ? 188 ARG B O    1 
ATOM   7407 C CB   . ARG B 2 188 ? 20.98400  -9.33600  -5.08600  1.000 61.54694  ? 188 ARG B CB   1 
ATOM   7408 C CG   . ARG B 2 188 ? 21.57500  -7.94600  -5.23500  1.000 60.62055  ? 188 ARG B CG   1 
ATOM   7409 C CD   . ARG B 2 188 ? 21.80300  -7.59400  -6.69000  1.000 64.02813  ? 188 ARG B CD   1 
ATOM   7410 N NE   . ARG B 2 188 ? 23.20800  -7.74100  -7.03000  1.000 72.11052  ? 188 ARG B NE   1 
ATOM   7411 C CZ   . ARG B 2 188 ? 24.08800  -6.75000  -7.04800  1.000 71.70930  ? 188 ARG B CZ   1 
ATOM   7412 N NH1  . ARG B 2 188 ? 23.70900  -5.51800  -6.75800  1.000 67.96008  ? 188 ARG B NH1  1 
ATOM   7413 N NH2  . ARG B 2 188 ? 25.34500  -6.99300  -7.36700  1.000 69.31988  ? 188 ARG B NH2  1 
ATOM   7414 H H    . ARG B 2 188 ? 19.28000  -7.84300  -3.27500  1.000 64.75385  ? 188 ARG B H    1 
ATOM   7415 H HA   . ARG B 2 188 ? 19.79100  -10.44400 -3.84900  1.000 68.71449  ? 188 ARG B HA   1 
ATOM   7416 H HB2  . ARG B 2 188 ? 21.71800  -9.97000  -5.09900  1.000 73.85713  ? 188 ARG B HB2  1 
ATOM   7417 H HB3  . ARG B 2 188 ? 20.40000  -9.49900  -5.84300  1.000 73.85713  ? 188 ARG B HB3  1 
ATOM   7418 H HG2  . ARG B 2 188 ? 20.95900  -7.30100  -4.86200  1.000 72.74547  ? 188 ARG B HG2  1 
ATOM   7419 H HG3  . ARG B 2 188 ? 22.42700  -7.90700  -4.77300  1.000 72.74547  ? 188 ARG B HG3  1 
ATOM   7420 H HD2  . ARG B 2 188 ? 21.29700  -8.19800  -7.25500  1.000 76.83455  ? 188 ARG B HD2  1 
ATOM   7421 H HD3  . ARG B 2 188 ? 21.52100  -6.68200  -6.85200  1.000 76.83455  ? 188 ARG B HD3  1 
ATOM   7422 H HE   . ARG B 2 188 ? 23.48900  -8.52800  -7.23400  1.000 86.53343  ? 188 ARG B HE   1 
ATOM   7423 H HH11 . ARG B 2 188 ? 22.89500  -5.34600  -6.54900  1.000 81.55289  ? 188 ARG B HH11 1 
ATOM   7424 H HH12 . ARG B 2 188 ? 24.28700  -4.88100  -6.77300  1.000 81.55289  ? 188 ARG B HH12 1 
ATOM   7425 H HH21 . ARG B 2 188 ? 25.59300  -7.79400  -7.55800  1.000 83.18466  ? 188 ARG B HH21 1 
ATOM   7426 H HH22 . ARG B 2 188 ? 25.91700  -6.35100  -7.38100  1.000 83.18466  ? 188 ARG B HH22 1 
ATOM   7427 N N    . GLN B 2 189 ? 21.79000  -10.50600 -2.25100  1.000 74.90444  ? 189 GLN B N    1 
ATOM   7428 C CA   . GLN B 2 189 ? 22.67700  -10.49600 -1.08900  1.000 82.86076  ? 189 GLN B CA   1 
ATOM   7429 C C    . GLN B 2 189 ? 23.89100  -9.66400  -1.47700  1.000 74.76508  ? 189 GLN B C    1 
ATOM   7430 O O    . GLN B 2 189 ? 24.82700  -10.13300 -2.12700  1.000 70.71413  ? 189 GLN B O    1 
ATOM   7431 C CB   . GLN B 2 189 ? 23.05900  -11.90300 -0.64900  1.000 83.16761  ? 189 GLN B CB   1 
ATOM   7432 C CG   . GLN B 2 189 ? 21.90200  -12.69900 -0.07100  1.000 89.89587  ? 189 GLN B CG   1 
ATOM   7433 C CD   . GLN B 2 189 ? 22.35500  -13.94300 0.68200   1.000 98.20810  ? 189 GLN B CD   1 
ATOM   7434 O OE1  . GLN B 2 189 ? 23.51600  -14.35300 0.59200   1.000 94.98856  ? 189 GLN B OE1  1 
ATOM   7435 N NE2  . GLN B 2 189 ? 21.43700  -14.54100 1.44100   1.000 91.16769  ? 189 GLN B NE2  1 
ATOM   7436 H H    . GLN B 2 189 ? 21.82900  -11.22700 -2.71900  1.000 89.88612  ? 189 GLN B H    1 
ATOM   7437 H HA   . GLN B 2 189 ? 22.23100  -10.05700 -0.34800  1.000 99.43371  ? 189 GLN B HA   1 
ATOM   7438 H HB2  . GLN B 2 189 ? 23.39900  -12.38900 -1.41600  1.000 99.80193  ? 189 GLN B HB2  1 
ATOM   7439 H HB3  . GLN B 2 189 ? 23.74700  -11.84200 0.03300   1.000 99.80193  ? 189 GLN B HB3  1 
ATOM   7440 H HG2  . GLN B 2 189 ? 21.41000  -12.13700 0.54800   1.000 107.87585 ? 189 GLN B HG2  1 
ATOM   7441 H HG3  . GLN B 2 189 ? 21.32100  -12.98200 -0.79500  1.000 107.87585 ? 189 GLN B HG3  1 
ATOM   7442 H HE21 . GLN B 2 189 ? 20.63800  -14.22400 1.48000   1.000 109.40203 ? 189 GLN B HE21 1 
ATOM   7443 H HE22 . GLN B 2 189 ? 21.64200  -15.24700 1.88800   1.000 109.40203 ? 189 GLN B HE22 1 
ATOM   7444 N N    . THR B 2 190 ? 23.81800  -8.38600  -1.11500  1.000 73.00332  ? 190 THR B N    1 
ATOM   7445 C CA   . THR B 2 190 ? 24.89100  -7.41400  -1.24000  1.000 66.96771  ? 190 THR B CA   1 
ATOM   7446 C C    . THR B 2 190 ? 24.87500  -6.55700  0.02300   1.000 65.97389  ? 190 THR B C    1 
ATOM   7447 O O    . THR B 2 190 ? 23.94400  -6.62500  0.83300   1.000 64.81050  ? 190 THR B O    1 
ATOM   7448 C CB   . THR B 2 190 ? 24.74100  -6.54700  -2.50600  1.000 68.85587  ? 190 THR B CB   1 
ATOM   7449 O OG1  . THR B 2 190 ? 25.85700  -5.65200  -2.60600  1.000 68.74816  ? 190 THR B OG1  1 
ATOM   7450 C CG2  . THR B 2 190 ? 23.45000  -5.73700  -2.46800  1.000 67.20796  ? 190 THR B CG2  1 
ATOM   7451 H H    . THR B 2 190 ? 23.10800  -8.04300  -0.77300  1.000 87.60479  ? 190 THR B H    1 
ATOM   7452 H HA   . THR B 2 190 ? 25.74200  -7.87700  -1.28500  1.000 80.36205  ? 190 THR B HA   1 
ATOM   7453 H HB   . THR B 2 190 ? 24.71800  -7.12100  -3.28800  1.000 82.62784  ? 190 THR B HB   1 
ATOM   7454 H HG1  . THR B 2 190 ? 25.78300  -5.17600  -3.29400  1.000 82.49859  ? 190 THR B HG1  1 
ATOM   7455 H HG21 . THR B 2 190 ? 23.29900  -5.31600  -3.32900  1.000 80.65035  ? 190 THR B HG21 1 
ATOM   7456 H HG22 . THR B 2 190 ? 22.70000  -6.31700  -2.26600  1.000 80.65035  ? 190 THR B HG22 1 
ATOM   7457 H HG23 . THR B 2 190 ? 23.50900  -5.04900  -1.78700  1.000 80.65035  ? 190 THR B HG23 1 
ATOM   7458 N N    . ALA B 2 191 ? 25.95400  -5.81000  0.23700   1.000 63.59659  ? 191 ALA B N    1 
ATOM   7459 C CA   . ALA B 2 191 ? 26.02400  -4.94600  1.41000   1.000 64.49062  ? 191 ALA B CA   1 
ATOM   7460 C C    . ALA B 2 191 ? 25.08800  -3.75600  1.21300   1.000 53.12246  ? 191 ALA B C    1 
ATOM   7461 O O    . ALA B 2 191 ? 25.29600  -2.96000  0.28200   1.000 53.49738  ? 191 ALA B O    1 
ATOM   7462 C CB   . ALA B 2 191 ? 27.47100  -4.49200  1.63000   1.000 58.28079  ? 191 ALA B CB   1 
ATOM   7463 H H    . ALA B 2 191 ? 26.64700  -5.78500  -0.27200  1.000 76.31671  ? 191 ALA B H    1 
ATOM   7464 H HA   . ALA B 2 191 ? 25.73400  -5.43900  2.19300   1.000 77.38954  ? 191 ALA B HA   1 
ATOM   7465 H HB1  . ALA B 2 191 ? 27.50600  -3.91900  2.41200   1.000 69.93774  ? 191 ALA B HB1  1 
ATOM   7466 H HB2  . ALA B 2 191 ? 28.02900  -5.27300  1.76700   1.000 69.93774  ? 191 ALA B HB2  1 
ATOM   7467 H HB3  . ALA B 2 191 ? 27.77100  -4.00400  0.84700   1.000 69.93774  ? 191 ALA B HB3  1 
ATOM   7468 N N    . GLN B 2 192 ? 24.09000  -3.61400  2.09700   1.000 52.96827  ? 192 GLN B N    1 
ATOM   7469 C CA   . GLN B 2 192 ? 23.08800  -2.54900  2.04000   1.000 51.37894  ? 192 GLN B CA   1 
ATOM   7470 C C    . GLN B 2 192 ? 22.81400  -2.02600  3.43800   1.000 50.51502  ? 192 GLN B C    1 
ATOM   7471 O O    . GLN B 2 192 ? 22.72700  -2.80800  4.39000   1.000 49.32839  ? 192 GLN B O    1 
ATOM   7472 C CB   . GLN B 2 192 ? 21.75300  -3.03800  1.44600   1.000 50.17364  ? 192 GLN B CB   1 
ATOM   7473 C CG   . GLN B 2 192 ? 21.94600  -3.89400  0.20200   1.000 49.44111  ? 192 GLN B CG   1 
ATOM   7474 C CD   . GLN B 2 192 ? 20.63300  -4.18500  -0.47700  1.000 48.36542  ? 192 GLN B CD   1 
ATOM   7475 O OE1  . GLN B 2 192 ? 19.98000  -3.25000  -0.92800  1.000 38.93969  ? 192 GLN B OE1  1 
ATOM   7476 N NE2  . GLN B 2 192 ? 20.22200  -5.45500  -0.53500  1.000 47.27041  ? 192 GLN B NE2  1 
ATOM   7477 H H    . GLN B 2 192 ? 23.97300  -4.14600  2.76200   1.000 63.56273  ? 192 GLN B H    1 
ATOM   7478 H HA   . GLN B 2 192 ? 23.42000  -1.81800  1.49600   1.000 61.65553  ? 192 GLN B HA   1 
ATOM   7479 H HB2  . GLN B 2 192 ? 21.28900  -3.57300  2.10900   1.000 60.20917  ? 192 GLN B HB2  1 
ATOM   7480 H HB3  . GLN B 2 192 ? 21.21400  -2.26900  1.20300   1.000 60.20917  ? 192 GLN B HB3  1 
ATOM   7481 H HG2  . GLN B 2 192 ? 22.51500  -3.42200  -0.42600  1.000 59.33013  ? 192 GLN B HG2  1 
ATOM   7482 H HG3  . GLN B 2 192 ? 22.35100  -4.73900  0.45400   1.000 59.33013  ? 192 GLN B HG3  1 
ATOM   7483 H HE21 . GLN B 2 192 ? 20.70900  -6.08000  -0.20200  1.000 56.72530  ? 192 GLN B HE21 1 
ATOM   7484 H HE22 . GLN B 2 192 ? 19.47500  -5.64800  -0.91500  1.000 56.72530  ? 192 GLN B HE22 1 
ATOM   7485 N N    . ALA B 2 193 ? 22.63900  -0.71300  3.56700   1.000 44.77539  ? 193 ALA B N    1 
ATOM   7486 C CA   . ALA B 2 193 ? 22.36800  -0.16000  4.89400   1.000 52.91024  ? 193 ALA B CA   1 
ATOM   7487 C C    . ALA B 2 193 ? 21.25200  0.87400   4.86700   1.000 50.34385  ? 193 ALA B C    1 
ATOM   7488 O O    . ALA B 2 193 ? 21.05500  1.58100   3.87800   1.000 53.94780  ? 193 ALA B O    1 
ATOM   7489 C CB   . ALA B 2 193 ? 23.60500  0.48500   5.52800   1.000 53.19281  ? 193 ALA B CB   1 
ATOM   7490 H H    . ALA B 2 193 ? 22.67000  -0.13800  2.92800   1.000 53.73127  ? 193 ALA B H    1 
ATOM   7491 H HA   . ALA B 2 193 ? 22.08000  -0.87500  5.48200   1.000 63.49308  ? 193 ALA B HA   1 
ATOM   7492 H HB1  . ALA B 2 193 ? 23.36700  0.83200   6.40200   1.000 63.83218  ? 193 ALA B HB1  1 
ATOM   7493 H HB2  . ALA B 2 193 ? 24.30000  -0.18600  5.61700   1.000 63.83218  ? 193 ALA B HB2  1 
ATOM   7494 H HB3  . ALA B 2 193 ? 23.91200  1.20700   4.95700   1.000 63.83218  ? 193 ALA B HB3  1 
ATOM   7495 N N    . ALA B 2 194 ? 20.53100  0.95700   5.98700   1.000 50.27344  ? 194 ALA B N    1 
ATOM   7496 C CA   . ALA B 2 194 ? 19.57600  2.03700   6.16800   1.000 53.12532  ? 194 ALA B CA   1 
ATOM   7497 C C    . ALA B 2 194 ? 20.32500  3.36400   6.26800   1.000 57.09604  ? 194 ALA B C    1 
ATOM   7498 O O    . ALA B 2 194 ? 21.25300  3.50100   7.07700   1.000 50.32270  ? 194 ALA B O    1 
ATOM   7499 C CB   . ALA B 2 194 ? 18.75200  1.79700   7.44100   1.000 50.39451  ? 194 ALA B CB   1 
ATOM   7500 H H    . ALA B 2 194 ? 20.57900  0.40600   6.64600   1.000 60.32893  ? 194 ALA B H    1 
ATOM   7501 H HA   . ALA B 2 194 ? 18.97400  2.07400   5.40800   1.000 63.75118  ? 194 ALA B HA   1 
ATOM   7502 H HB1  . ALA B 2 194 ? 18.12000  2.52500   7.54900   1.000 60.47421  ? 194 ALA B HB1  1 
ATOM   7503 H HB2  . ALA B 2 194 ? 18.27700  0.95500   7.35500   1.000 60.47421  ? 194 ALA B HB2  1 
ATOM   7504 H HB3  . ALA B 2 194 ? 19.35100  1.76300   8.20300   1.000 60.47421  ? 194 ALA B HB3  1 
ATOM   7505 N N    . GLY B 2 195 ? 19.90200  4.34700   5.45700   1.000 57.85167  ? 195 GLY B N    1 
ATOM   7506 C CA   . GLY B 2 195 ? 20.43300  5.69400   5.53900   1.000 54.54131  ? 195 GLY B CA   1 
ATOM   7507 C C    . GLY B 2 195 ? 20.03700  6.41500   6.81700   1.000 55.22475  ? 195 GLY B C    1 
ATOM   7508 O O    . GLY B 2 195 ? 19.18000  5.98500   7.60800   1.000 49.00364  ? 195 GLY B O    1 
ATOM   7509 H H    . GLY B 2 195 ? 19.30200  4.24600   4.84900   1.000 69.42280  ? 195 GLY B H    1 
ATOM   7510 H HA2  . GLY B 2 195 ? 21.40100  5.66000   5.49600   1.000 65.45037  ? 195 GLY B HA2  1 
ATOM   7511 H HA3  . GLY B 2 195 ? 20.11100  6.21200   4.78500   1.000 65.45037  ? 195 GLY B HA3  1 
ATOM   7512 N N    . THR B 2 196 ? 20.67200  7.56700   7.03000   1.000 51.71223  ? 196 THR B N    1 
ATOM   7513 C CA   . THR B 2 196 ? 20.28700  8.35900   8.18700   1.000 52.71854  ? 196 THR B CA   1 
ATOM   7514 C C    . THR B 2 196 ? 18.80100  8.66600   8.09200   1.000 48.33910  ? 196 THR B C    1 
ATOM   7515 O O    . THR B 2 196 ? 18.32600  9.15700   7.06600   1.000 47.82033  ? 196 THR B O    1 
ATOM   7516 C CB   . THR B 2 196 ? 21.08700  9.65400   8.23200   1.000 56.60146  ? 196 THR B CB   1 
ATOM   7517 O OG1  . THR B 2 196 ? 22.48300  9.33800   8.27500   1.000 56.50044  ? 196 THR B OG1  1 
ATOM   7518 C CG2  . THR B 2 196 ? 20.69600  10.46200  9.43500   1.000 54.44530  ? 196 THR B CG2  1 
ATOM   7519 H H    . THR B 2 196 ? 21.29900  7.89700   6.54300   1.000 62.05548  ? 196 THR B H    1 
ATOM   7520 H HA   . THR B 2 196 ? 20.45300  7.85800   9.00100   1.000 63.26305  ? 196 THR B HA   1 
ATOM   7521 H HB   . THR B 2 196 ? 20.89900  10.17700  7.43700   1.000 67.92256  ? 196 THR B HB   1 
ATOM   7522 H HG1  . THR B 2 196 ? 22.93700  10.04400  8.30000   1.000 67.80133  ? 196 THR B HG1  1 
ATOM   7523 H HG21 . THR B 2 196 ? 21.34300  11.17000  9.58100   1.000 65.33516  ? 196 THR B HG21 1 
ATOM   7524 H HG22 . THR B 2 196 ? 19.82100  10.86000  9.30200   1.000 65.33516  ? 196 THR B HG22 1 
ATOM   7525 H HG23 . THR B 2 196 ? 20.67000  9.89400   10.22100  1.000 65.33516  ? 196 THR B HG23 1 
ATOM   7526 N N    . ASP B 2 197 ? 18.07800  8.37900   9.16500   1.000 48.49902  ? 197 ASP B N    1 
ATOM   7527 C CA   . ASP B 2 197 ? 16.65000  8.63600   9.20500   1.000 44.61946  ? 197 ASP B CA   1 
ATOM   7528 C C    . ASP B 2 197 ? 16.40200  10.00700  9.81900   1.000 50.85007  ? 197 ASP B C    1 
ATOM   7529 O O    . ASP B 2 197 ? 17.28400  10.60300  10.44100  1.000 47.79112  ? 197 ASP B O    1 
ATOM   7530 C CB   . ASP B 2 197 ? 15.91600  7.55300   9.98300   1.000 42.25449  ? 197 ASP B CB   1 
ATOM   7531 C CG   . ASP B 2 197 ? 14.46100  7.40600   9.51800   1.000 37.37149  ? 197 ASP B CG   1 
ATOM   7532 O OD1  . ASP B 2 197 ? 14.14500  7.99000   8.45200   1.000 37.69729  ? 197 ASP B OD1  1 
ATOM   7533 O OD2  . ASP B 2 197 ? 13.69000  6.69800   10.18100  1.000 37.84996  ? 197 ASP B OD2  1 
ATOM   7534 H H    . ASP B 2 197 ? 18.39400  8.03300   9.88600   1.000 58.19962  ? 197 ASP B H    1 
ATOM   7535 H HA   . ASP B 2 197 ? 16.31300  8.64700   8.29600   1.000 53.54415  ? 197 ASP B HA   1 
ATOM   7536 H HB2  . ASP B 2 197 ? 16.36500  6.70400   9.84900   1.000 50.70619  ? 197 ASP B HB2  1 
ATOM   7537 H HB3  . ASP B 2 197 ? 15.91100  7.78400   10.92500  1.000 50.70619  ? 197 ASP B HB3  1 
ATOM   7538 N N    . THR B 2 198 ? 15.22200  10.55000  9.54600   1.000 41.99714  ? 198 THR B N    1 
ATOM   7539 C CA   . THR B 2 198 ? 14.80200  11.82000  10.11000  1.000 42.51548  ? 198 THR B CA   1 
ATOM   7540 C C    . THR B 2 198 ? 13.40500  11.62600  10.68800  1.000 42.20024  ? 198 THR B C    1 
ATOM   7541 O O    . THR B 2 198 ? 12.73500  10.61800  10.42500  1.000 37.96532  ? 198 THR B O    1 
ATOM   7542 C CB   . THR B 2 198 ? 14.82500  12.94500  9.05700   1.000 41.58040  ? 198 THR B CB   1 
ATOM   7543 O OG1  . THR B 2 198 ? 14.05700  12.54800  7.91400   1.000 42.47240  ? 198 THR B OG1  1 
ATOM   7544 C CG2  . THR B 2 198 ? 16.27600  13.26400  8.59100   1.000 46.27782  ? 198 THR B CG2  1 
ATOM   7545 H H    . THR B 2 198 ? 14.63700  10.19300  9.02600   1.000 50.39737  ? 198 THR B H    1 
ATOM   7546 H HA   . THR B 2 198 ? 15.39900  12.06700  10.83300  1.000 51.01938  ? 198 THR B HA   1 
ATOM   7547 H HB   . THR B 2 198 ? 14.44200  13.75100  9.43800   1.000 49.89729  ? 198 THR B HB   1 
ATOM   7548 H HG1  . THR B 2 198 ? 14.11300  13.13200  7.31400   1.000 50.96768  ? 198 THR B HG1  1 
ATOM   7549 H HG21 . THR B 2 198 ? 16.26300  13.97400  7.93000   1.000 55.53419  ? 198 THR B HG21 1 
ATOM   7550 H HG22 . THR B 2 198 ? 16.81200  13.54800  9.34800   1.000 55.53419  ? 198 THR B HG22 1 
ATOM   7551 H HG23 . THR B 2 198 ? 16.67900  12.47400  8.19800   1.000 55.53419  ? 198 THR B HG23 1 
ATOM   7552 N N    . THR B 2 199 ? 12.95300  12.58900  11.48100  1.000 39.59858  ? 199 THR B N    1 
ATOM   7553 C CA   . THR B 2 199 ? 11.63000  12.51600  12.12800  1.000 36.15375  ? 199 THR B CA   1 
ATOM   7554 C C    . THR B 2 199 ? 10.55700  13.16200  11.25800  1.000 36.96274  ? 199 THR B C    1 
ATOM   7555 O O    . THR B 2 199 ? 10.77400  14.20800  10.64100  1.000 34.11900  ? 199 THR B O    1 
ATOM   7556 C CB   . THR B 2 199 ? 11.68700  13.19900  13.49900  1.000 42.24419  ? 199 THR B CB   1 
ATOM   7557 O OG1  . THR B 2 199 ? 12.63100  12.50000  14.29300  1.000 38.54399  ? 199 THR B OG1  1 
ATOM   7558 C CG2  . THR B 2 199 ? 10.31700  13.17300  14.21000  1.000 37.72219  ? 199 THR B CG2  1 
ATOM   7559 H H    . THR B 2 199 ? 13.39100  13.30500  11.66700  1.000 47.51910  ? 199 THR B H    1 
ATOM   7560 H HA   . THR B 2 199 ? 11.39100  11.58600  12.26300  1.000 43.38530  ? 199 THR B HA   1 
ATOM   7561 H HB   . THR B 2 199 ? 11.96700  14.12200  13.39400  1.000 50.69383  ? 199 THR B HB   1 
ATOM   7562 H HG1  . THR B 2 199 ? 12.68400  12.85300  15.05300  1.000 46.25358  ? 199 THR B HG1  1 
ATOM   7563 H HG21 . THR B 2 199 ? 10.42900  13.37200  15.15200  1.000 45.26743  ? 199 THR B HG21 1 
ATOM   7564 H HG22 . THR B 2 199 ? 9.72500   13.83300  13.81700  1.000 45.26743  ? 199 THR B HG22 1 
ATOM   7565 H HG23 . THR B 2 199 ? 9.91500   12.29400  14.12200  1.000 45.26743  ? 199 THR B HG23 1 
ATOM   7566 N N    . ILE B 2 200 ? 9.38400   12.53500  11.20600  1.000 35.03407  ? 200 ILE B N    1 
ATOM   7567 C CA   . ILE B 2 200 ? 8.34800   13.01100  10.30100  1.000 32.89912  ? 200 ILE B CA   1 
ATOM   7568 C C    . ILE B 2 200 ? 7.57800   14.11900  11.01300  1.000 33.54922  ? 200 ILE B C    1 
ATOM   7569 O O    . ILE B 2 200 ? 6.60700   13.85800  11.73200  1.000 30.24280  ? 200 ILE B O    1 
ATOM   7570 C CB   . ILE B 2 200 ? 7.43100   11.88200  9.84600   1.000 30.54033  ? 200 ILE B CB   1 
ATOM   7571 C CG1  . ILE B 2 200 ? 8.27500   10.71300  9.28300   1.000 28.13565  ? 200 ILE B CG1  1 
ATOM   7572 C CG2  . ILE B 2 200 ? 6.49800   12.43200  8.79000   1.000 32.93037  ? 200 ILE B CG2  1 
ATOM   7573 C CD1  . ILE B 2 200 ? 7.48200   9.34700   9.38300   1.000 28.04692  ? 200 ILE B CD1  1 
ATOM   7574 H H    . ILE B 2 200 ? 9.16800   11.84700  11.67400  1.000 42.04169  ? 200 ILE B H    1 
ATOM   7575 H HA   . ILE B 2 200 ? 8.76600   13.39300  9.51300   1.000 39.47974  ? 200 ILE B HA   1 
ATOM   7576 H HB   . ILE B 2 200 ? 6.91000   11.56700  10.60200  1.000 36.64920  ? 200 ILE B HB   1 
ATOM   7577 H HG12 . ILE B 2 200 ? 8.47100   10.88200  8.34800   1.000 33.76358  ? 200 ILE B HG12 1 
ATOM   7578 H HG13 . ILE B 2 200 ? 9.09800   10.61700  9.78600   1.000 33.76358  ? 200 ILE B HG13 1 
ATOM   7579 H HG21 . ILE B 2 200 ? 6.01200   11.69600  8.38700   1.000 39.51725  ? 200 ILE B HG21 1 
ATOM   7580 H HG22 . ILE B 2 200 ? 5.87600   13.05000  9.20500   1.000 39.51725  ? 200 ILE B HG22 1 
ATOM   7581 H HG23 . ILE B 2 200 ? 7.02100   12.89000  8.11400   1.000 39.51725  ? 200 ILE B HG23 1 
ATOM   7582 H HD11 . ILE B 2 200 ? 7.82100   8.73600   8.71000   1.000 33.65711  ? 200 ILE B HD11 1 
ATOM   7583 H HD12 . ILE B 2 200 ? 7.61200   8.97100   10.26800  1.000 33.65711  ? 200 ILE B HD12 1 
ATOM   7584 H HD13 . ILE B 2 200 ? 6.53900   9.51700   9.23100   1.000 33.65711  ? 200 ILE B HD13 1 
ATOM   7585 N N    . THR B 2 201 ? 7.96300   15.37100  10.72800  1.000 34.29708  ? 201 THR B N    1 
ATOM   7586 C CA   . THR B 2 201 ? 7.49200   16.51600  11.50100  1.000 33.82997  ? 201 THR B CA   1 
ATOM   7587 C C    . THR B 2 201 ? 5.97000   16.64900  11.47700  1.000 34.33318  ? 201 THR B C    1 
ATOM   7588 O O    . THR B 2 201 ? 5.33600   16.90400  12.51900  1.000 33.20258  ? 201 THR B O    1 
ATOM   7589 C CB   . THR B 2 201 ? 8.15400   17.75900  10.94900  1.000 39.54496  ? 201 THR B CB   1 
ATOM   7590 O OG1  . THR B 2 201 ? 9.54900   17.48100  10.85100  1.000 38.23692  ? 201 THR B OG1  1 
ATOM   7591 C CG2  . THR B 2 201 ? 7.91600   18.95800  11.86000  1.000 39.15017  ? 201 THR B CG2  1 
ATOM   7592 H H    . THR B 2 201 ? 8.49900   15.57900  10.08800  1.000 41.15730  ? 201 THR B H    1 
ATOM   7593 H HA   . THR B 2 201 ? 7.77000   16.41100  12.42400  1.000 40.59677  ? 201 THR B HA   1 
ATOM   7594 H HB   . THR B 2 201 ? 7.79600   17.95800  10.07000  1.000 47.45475  ? 201 THR B HB   1 
ATOM   7595 H HG1  . THR B 2 201 ? 9.95400   18.14900  10.54100  1.000 45.88510  ? 201 THR B HG1  1 
ATOM   7596 H HG21 . THR B 2 201 ? 8.46400   19.70100  11.56700  1.000 46.98101  ? 201 THR B HG21 1 
ATOM   7597 H HG22 . THR B 2 201 ? 6.98300   19.22100  11.82900  1.000 46.98101  ? 201 THR B HG22 1 
ATOM   7598 H HG23 . THR B 2 201 ? 8.15300   18.73300  12.77300  1.000 46.98101  ? 201 THR B HG23 1 
ATOM   7599 N N    . VAL B 2 202 ? 5.36700   16.54300  10.28700  1.000 33.65221  ? 202 VAL B N    1 
ATOM   7600 C CA   . VAL B 2 202 ? 3.93500   16.75100  10.19000  1.000 33.20832  ? 202 VAL B CA   1 
ATOM   7601 C C    . VAL B 2 202 ? 3.18700   15.71800  11.01200  1.000 30.63944  ? 202 VAL B C    1 
ATOM   7602 O O    . VAL B 2 202 ? 2.15800   16.04500  11.61100  1.000 31.34442  ? 202 VAL B O    1 
ATOM   7603 C CB   . VAL B 2 202 ? 3.47000   16.76900  8.70800   1.000 39.38620  ? 202 VAL B CB   1 
ATOM   7604 C CG1  . VAL B 2 202 ? 3.81700   15.45700  7.98300   1.000 37.58975  ? 202 VAL B CG1  1 
ATOM   7605 C CG2  . VAL B 2 202 ? 1.96000   17.04900  8.63700   1.000 39.50688  ? 202 VAL B CG2  1 
ATOM   7606 H H    . VAL B 2 202 ? 5.76000   16.35800  9.54500   1.000 40.38345  ? 202 VAL B H    1 
ATOM   7607 H HA   . VAL B 2 202 ? 3.72900   17.62100  10.56600  1.000 39.85079  ? 202 VAL B HA   1 
ATOM   7608 H HB   . VAL B 2 202 ? 3.92600   17.49000  8.24700   1.000 47.26424  ? 202 VAL B HB   1 
ATOM   7609 H HG11 . VAL B 2 202 ? 3.49300   15.50700  7.07000   1.000 45.10850  ? 202 VAL B HG11 1 
ATOM   7610 H HG12 . VAL B 2 202 ? 4.78000   15.33800  7.98600   1.000 45.10850  ? 202 VAL B HG12 1 
ATOM   7611 H HG13 . VAL B 2 202 ? 3.39100   14.71800  8.44400   1.000 45.10850  ? 202 VAL B HG13 1 
ATOM   7612 H HG21 . VAL B 2 202 ? 1.71300   17.20300  7.71200   1.000 47.40906  ? 202 VAL B HG21 1 
ATOM   7613 H HG22 . VAL B 2 202 ? 1.47700   16.28300  8.98400   1.000 47.40906  ? 202 VAL B HG22 1 
ATOM   7614 H HG23 . VAL B 2 202 ? 1.76000   17.83600  9.16700   1.000 47.40906  ? 202 VAL B HG23 1 
ATOM   7615 N N    . ASN B 2 203 ? 3.74600   14.51600  11.14500  1.000 28.96565  ? 203 ASN B N    1 
ATOM   7616 C CA   . ASN B 2 203 ? 3.10700   13.42100  11.92400  1.000 27.32435  ? 203 ASN B CA   1 
ATOM   7617 C C    . ASN B 2 203 ? 3.21500   13.72000  13.41800  1.000 29.21261  ? 203 ASN B C    1 
ATOM   7618 O O    . ASN B 2 203 ? 2.25000   13.48400  14.13000  1.000 28.33861  ? 203 ASN B O    1 
ATOM   7619 C CB   . ASN B 2 203 ? 3.74700   12.08200  11.58800  1.000 31.26439  ? 203 ASN B CB   1 
ATOM   7620 C CG   . ASN B 2 203 ? 3.32100   11.54300  10.24300  1.000 30.30196  ? 203 ASN B CG   1 
ATOM   7621 O OD1  . ASN B 2 203 ? 2.68500   12.24500  9.46900   1.000 27.74236  ? 203 ASN B OD1  1 
ATOM   7622 N ND2  . ASN B 2 203 ? 3.66400   10.29900  9.96700   1.000 27.20726  ? 203 ASN B ND2  1 
ATOM   7623 H H    . ASN B 2 203 ? 4.50000   14.29500  10.79600  1.000 34.75958  ? 203 ASN B H    1 
ATOM   7624 H HA   . ASN B 2 203 ? 2.16600   13.37300  11.69300  1.000 32.79002  ? 203 ASN B HA   1 
ATOM   7625 H HB2  . ASN B 2 203 ? 4.71100   12.18800  11.57600  1.000 37.51807  ? 203 ASN B HB2  1 
ATOM   7626 H HB3  . ASN B 2 203 ? 3.49400   11.43400  12.26400  1.000 37.51807  ? 203 ASN B HB3  1 
ATOM   7627 H HD21 . ASN B 2 203 ? 3.44300   9.94900   9.21300   1.000 32.64951  ? 203 ASN B HD21 1 
ATOM   7628 H HD22 . ASN B 2 203 ? 4.11100   9.83900   10.54000  1.000 32.64951  ? 203 ASN B HD22 1 
ATOM   7629 N N    . VAL B 2 204 ? 4.37600   14.20100  13.85500  1.000 29.77037  ? 204 VAL B N    1 
ATOM   7630 C CA   . VAL B 2 204 ? 4.50000   14.62300  15.24700  1.000 29.91963  ? 204 VAL B CA   1 
ATOM   7631 C C    . VAL B 2 204 ? 3.42800   15.65900  15.57900  1.000 31.86968  ? 204 VAL B C    1 
ATOM   7632 O O    . VAL B 2 204 ? 2.76900   15.59100  16.61800  1.000 28.66396  ? 204 VAL B O    1 
ATOM   7633 C CB   . VAL B 2 204 ? 5.91600   15.16600  15.52600  1.000 31.26351  ? 204 VAL B CB   1 
ATOM   7634 C CG1  . VAL B 2 204 ? 6.02300   15.67500  17.01100  1.000 34.08217  ? 204 VAL B CG1  1 
ATOM   7635 C CG2  . VAL B 2 204 ? 6.92100   14.10700  15.26100  1.000 30.24192  ? 204 VAL B CG2  1 
ATOM   7636 H H    . VAL B 2 204 ? 5.08700   14.29300  13.38000  1.000 35.72524  ? 204 VAL B H    1 
ATOM   7637 H HA   . VAL B 2 204 ? 4.35800   13.85400  15.82100  1.000 35.90435  ? 204 VAL B HA   1 
ATOM   7638 H HB   . VAL B 2 204 ? 6.09600   15.91300  14.93400  1.000 37.51701  ? 204 VAL B HB   1 
ATOM   7639 H HG11 . VAL B 2 204 ? 6.95500   15.84500  17.21800  1.000 40.89940  ? 204 VAL B HG11 1 
ATOM   7640 H HG12 . VAL B 2 204 ? 5.51000   16.49300  17.10500  1.000 40.89940  ? 204 VAL B HG12 1 
ATOM   7641 H HG13 . VAL B 2 204 ? 5.67200   14.99300  17.60400  1.000 40.89940  ? 204 VAL B HG13 1 
ATOM   7642 H HG21 . VAL B 2 204 ? 7.79300   14.42100  15.54900  1.000 36.29111  ? 204 VAL B HG21 1 
ATOM   7643 H HG22 . VAL B 2 204 ? 6.67700   13.31000  15.75700  1.000 36.29111  ? 204 VAL B HG22 1 
ATOM   7644 H HG23 . VAL B 2 204 ? 6.93600   13.91400  14.31100  1.000 36.29111  ? 204 VAL B HG23 1 
ATOM   7645 N N    . LEU B 2 205 ? 3.26300   16.66300  14.72300  1.000 31.47860  ? 205 LEU B N    1 
ATOM   7646 C CA   . LEU B 2 205 ? 2.25900   17.68000  15.02200  1.000 32.80926  ? 205 LEU B CA   1 
ATOM   7647 C C    . LEU B 2 205 ? 0.87700   17.06700  15.08500  1.000 32.72674  ? 205 LEU B C    1 
ATOM   7648 O O    . LEU B 2 205 ? 0.06800   17.42300  15.95000  1.000 33.32956  ? 205 LEU B O    1 
ATOM   7649 C CB   . LEU B 2 205 ? 2.29500   18.79600  13.97500  1.000 35.78199  ? 205 LEU B CB   1 
ATOM   7650 C CG   . LEU B 2 205 ? 3.56800   19.64800  13.97600  1.000 34.68330  ? 205 LEU B CG   1 
ATOM   7651 C CD1  . LEU B 2 205 ? 3.65800   20.45900  12.68400  1.000 38.40550  ? 205 LEU B CD1  1 
ATOM   7652 C CD2  . LEU B 2 205 ? 3.65100   20.59600  15.20100  1.000 33.95490  ? 205 LEU B CD2  1 
ATOM   7653 H H    . LEU B 2 205 ? 3.70000   16.77700  13.99100  1.000 37.77513  ? 205 LEU B H    1 
ATOM   7654 H HA   . LEU B 2 205 ? 2.45400   18.07200  15.88700  1.000 39.37191  ? 205 LEU B HA   1 
ATOM   7655 H HB2  . LEU B 2 205 ? 2.21200   18.39600  13.09500  1.000 42.93919  ? 205 LEU B HB2  1 
ATOM   7656 H HB3  . LEU B 2 205 ? 1.54500   19.39100  14.13300  1.000 42.93919  ? 205 LEU B HB3  1 
ATOM   7657 H HG   . LEU B 2 205 ? 4.33700   19.05800  14.00800  1.000 41.62077  ? 205 LEU B HG   1 
ATOM   7658 H HD11 . LEU B 2 205 ? 4.46600   20.99500  12.70400  1.000 46.08740  ? 205 LEU B HD11 1 
ATOM   7659 H HD12 . LEU B 2 205 ? 3.68400   19.84900  11.93000  1.000 46.08740  ? 205 LEU B HD12 1 
ATOM   7660 H HD13 . LEU B 2 205 ? 2.88000   21.03400  12.61800  1.000 46.08740  ? 205 LEU B HD13 1 
ATOM   7661 H HD21 . LEU B 2 205 ? 4.46400   21.12100  15.13900  1.000 40.74669  ? 205 LEU B HD21 1 
ATOM   7662 H HD22 . LEU B 2 205 ? 2.87800   21.18200  15.19900  1.000 40.74669  ? 205 LEU B HD22 1 
ATOM   7663 H HD23 . LEU B 2 205 ? 3.66200   20.06400  16.01200  1.000 40.74669  ? 205 LEU B HD23 1 
ATOM   7664 N N    . ALA B 2 206 ? 0.58000   16.15700  14.15500  1.000 30.80495  ? 206 ALA B N    1 
ATOM   7665 C CA   . ALA B 2 206 ? -0.69400  15.45600  14.17100  1.000 29.40767  ? 206 ALA B CA   1 
ATOM   7666 C C    . ALA B 2 206 ? -0.90500  14.78200  15.50800  1.000 32.74398  ? 206 ALA B C    1 
ATOM   7667 O O    . ALA B 2 206 ? -1.99600  14.85300  16.08500  1.000 32.13700  ? 206 ALA B O    1 
ATOM   7668 C CB   . ALA B 2 206 ? -0.73000  14.42000  13.05500  1.000 31.60888  ? 206 ALA B CB   1 
ATOM   7669 H H    . ALA B 2 206 ? 1.10000   15.93100  13.50800  1.000 36.96674  ? 206 ALA B H    1 
ATOM   7670 H HA   . ALA B 2 206 ? -1.41500  16.08900  14.02800  1.000 35.29001  ? 206 ALA B HA   1 
ATOM   7671 H HB1  . ALA B 2 206 ? -1.58700  13.96700  13.07300  1.000 37.93145  ? 206 ALA B HB1  1 
ATOM   7672 H HB2  . ALA B 2 206 ? -0.61100  14.87000  12.20400  1.000 37.93145  ? 206 ALA B HB2  1 
ATOM   7673 H HB3  . ALA B 2 206 ? -0.01400  13.78100  13.19400  1.000 37.93145  ? 206 ALA B HB3  1 
ATOM   7674 N N    . TRP B 2 207 ? 0.14400   14.13600  16.02200  1.000 28.76998  ? 207 TRP B N    1 
ATOM   7675 C CA   . TRP B 2 207 ? 0.03100   13.41900  17.28600  1.000 30.20719  ? 207 TRP B CA   1 
ATOM   7676 C C    . TRP B 2 207 ? -0.11500  14.38300  18.46300  1.000 29.43810  ? 207 TRP B C    1 
ATOM   7677 O O    . TRP B 2 207 ? -0.82800  14.06600  19.42200  1.000 30.01240  ? 207 TRP B O    1 
ATOM   7678 C CB   . TRP B 2 207 ? 1.23700   12.49400  17.40400  1.000 31.17497  ? 207 TRP B CB   1 
ATOM   7679 C CG   . TRP B 2 207 ? 1.49800   11.82600  18.71000  1.000 32.35696  ? 207 TRP B CG   1 
ATOM   7680 C CD1  . TRP B 2 207 ? 0.93300   10.66700  19.21100  1.000 31.82236  ? 207 TRP B CD1  1 
ATOM   7681 C CD2  . TRP B 2 207 ? 2.48200   12.23000  19.64600  1.000 32.22936  ? 207 TRP B CD2  1 
ATOM   7682 N NE1  . TRP B 2 207 ? 1.50600   10.36500  20.43800  1.000 32.40735  ? 207 TRP B NE1  1 
ATOM   7683 C CE2  . TRP B 2 207 ? 2.46400   11.30600  20.71100  1.000 33.18042  ? 207 TRP B CE2  1 
ATOM   7684 C CE3  . TRP B 2 207 ? 3.38100   13.29200  19.68600  1.000 35.60053  ? 207 TRP B CE3  1 
ATOM   7685 C CZ2  . TRP B 2 207 ? 3.30300   11.42700  21.79600  1.000 34.89068  ? 207 TRP B CZ2  1 
ATOM   7686 C CZ3  . TRP B 2 207 ? 4.21200   13.40200  20.75600  1.000 38.58521  ? 207 TRP B CZ3  1 
ATOM   7687 C CH2  . TRP B 2 207 ? 4.17000   12.48000  21.79800  1.000 33.71687  ? 207 TRP B CH2  1 
ATOM   7688 H H    . TRP B 2 207 ? 0.92300   14.10000  15.66000  1.000 34.52477  ? 207 TRP B H    1 
ATOM   7689 H HA   . TRP B 2 207 ? -0.76400  12.86500  17.26000  1.000 36.24943  ? 207 TRP B HA   1 
ATOM   7690 H HB2  . TRP B 2 207 ? 1.13500   11.79000  16.74500  1.000 37.41076  ? 207 TRP B HB2  1 
ATOM   7691 H HB3  . TRP B 2 207 ? 2.02900   13.01200  17.19100  1.000 37.41076  ? 207 TRP B HB3  1 
ATOM   7692 H HD1  . TRP B 2 207 ? 0.25800   10.17800  18.79900  1.000 38.18763  ? 207 TRP B HD1  1 
ATOM   7693 H HE1  . TRP B 2 207 ? 1.30300   9.69500   20.93700  1.000 38.88962  ? 207 TRP B HE1  1 
ATOM   7694 H HE3  . TRP B 2 207 ? 3.42200   13.90600  18.98800  1.000 42.72143  ? 207 TRP B HE3  1 
ATOM   7695 H HZ2  . TRP B 2 207 ? 3.27700   10.81900  22.49900  1.000 41.86961  ? 207 TRP B HZ2  1 
ATOM   7696 H HZ3  . TRP B 2 207 ? 4.81300   14.11000  20.79700  1.000 46.30306  ? 207 TRP B HZ3  1 
ATOM   7697 H HH2  . TRP B 2 207 ? 4.74100   12.59200  22.52300  1.000 40.46104  ? 207 TRP B HH2  1 
ATOM   7698 N N    . LEU B 2 208 ? 0.52700   15.57300  18.40100  1.000 30.26604  ? 208 LEU B N    1 
ATOM   7699 C CA   . LEU B 2 208 ? 0.28500   16.58900  19.43600  1.000 32.62900  ? 208 LEU B CA   1 
ATOM   7700 C C    . LEU B 2 208 ? -1.16600  17.05000  19.40700  1.000 34.17568  ? 208 LEU B C    1 
ATOM   7701 O O    . LEU B 2 208 ? -1.76300  17.29600  20.45700  1.000 35.77046  ? 208 LEU B O    1 
ATOM   7702 C CB   . LEU B 2 208 ? 1.24200   17.77600  19.26300  1.000 33.71167  ? 208 LEU B CB   1 
ATOM   7703 C CG   . LEU B 2 208 ? 2.72800   17.48700  19.52600  1.000 33.60446  ? 208 LEU B CG   1 
ATOM   7704 C CD1  . LEU B 2 208 ? 3.58000   18.72400  19.20400  1.000 32.88557  ? 208 LEU B CD1  1 
ATOM   7705 C CD2  . LEU B 2 208 ? 3.02800   17.02300  21.02300  1.000 35.20861  ? 208 LEU B CD2  1 
ATOM   7706 H H    . LEU B 2 208 ? 1.08700   15.80400  17.79000  1.000 36.32005  ? 208 LEU B H    1 
ATOM   7707 H HA   . LEU B 2 208 ? 0.45300   16.19500  20.30600  1.000 39.15560  ? 208 LEU B HA   1 
ATOM   7708 H HB2  . LEU B 2 208 ? 1.16700   18.09800  18.35100  1.000 40.45481  ? 208 LEU B HB2  1 
ATOM   7709 H HB3  . LEU B 2 208 ? 0.97100   18.47800  19.87500  1.000 40.45481  ? 208 LEU B HB3  1 
ATOM   7710 H HG   . LEU B 2 208 ? 3.01300   16.77300  18.93500  1.000 40.32615  ? 208 LEU B HG   1 
ATOM   7711 H HD11 . LEU B 2 208 ? 4.51200   18.51900  19.37700  1.000 39.46348  ? 208 LEU B HD11 1 
ATOM   7712 H HD12 . LEU B 2 208 ? 3.46000   18.95500  18.27000  1.000 39.46348  ? 208 LEU B HD12 1 
ATOM   7713 H HD13 . LEU B 2 208 ? 3.29300   19.46000  19.76700  1.000 39.46348  ? 208 LEU B HD13 1 
ATOM   7714 H HD21 . LEU B 2 208 ? 3.98500   16.91200  21.13300  1.000 42.25113  ? 208 LEU B HD21 1 
ATOM   7715 H HD22 . LEU B 2 208 ? 2.70100   17.70100  21.63500  1.000 42.25113  ? 208 LEU B HD22 1 
ATOM   7716 H HD23 . LEU B 2 208 ? 2.57600   16.18100  21.19000  1.000 42.25113  ? 208 LEU B HD23 1 
ATOM   7717 N N    . TYR B 2 209 ? -1.77400  17.11000  18.22400  1.000 35.20847  ? 209 TYR B N    1 
ATOM   7718 C CA   . TYR B 2 209 ? -3.19900  17.40600  18.17400  1.000 33.82464  ? 209 TYR B CA   1 
ATOM   7719 C C    . TYR B 2 209 ? -4.00900  16.29800  18.82500  1.000 37.64148  ? 209 TYR B C    1 
ATOM   7720 O O    . TYR B 2 209 ? -4.94800  16.57300  19.57100  1.000 35.64233  ? 209 TYR B O    1 
ATOM   7721 C CB   . TYR B 2 209 ? -3.64000  17.61200  16.72900  1.000 36.26464  ? 209 TYR B CB   1 
ATOM   7722 C CG   . TYR B 2 209 ? -3.30400  19.00200  16.21500  1.000 41.56789  ? 209 TYR B CG   1 
ATOM   7723 C CD1  . TYR B 2 209 ? -3.98600  20.13000  16.69300  1.000 49.25934  ? 209 TYR B CD1  1 
ATOM   7724 C CD2  . TYR B 2 209 ? -2.29400  19.19600  15.28700  1.000 38.10714  ? 209 TYR B CD2  1 
ATOM   7725 C CE1  . TYR B 2 209 ? -3.68300  21.40500  16.24300  1.000 51.62997  ? 209 TYR B CE1  1 
ATOM   7726 C CE2  . TYR B 2 209 ? -1.97600  20.49100  14.81700  1.000 44.03023  ? 209 TYR B CE2  1 
ATOM   7727 C CZ   . TYR B 2 209 ? -2.67800  21.59000  15.31300  1.000 51.98829  ? 209 TYR B CZ   1 
ATOM   7728 O OH   . TYR B 2 209 ? -2.37900  22.86900  14.86500  1.000 53.32999  ? 209 TYR B OH   1 
ATOM   7729 H H    . TYR B 2 209 ? -1.39700  16.98700  17.46100  1.000 42.25096  ? 209 TYR B H    1 
ATOM   7730 H HA   . TYR B 2 209 ? -3.36900  18.22700  18.66200  1.000 40.59037  ? 209 TYR B HA   1 
ATOM   7731 H HB2  . TYR B 2 209 ? -3.19000  16.96600  16.16400  1.000 43.51837  ? 209 TYR B HB2  1 
ATOM   7732 H HB3  . TYR B 2 209 ? -4.60100  17.49300  16.67100  1.000 43.51837  ? 209 TYR B HB3  1 
ATOM   7733 H HD1  . TYR B 2 209 ? -4.66300  20.01900  17.32100  1.000 59.11201  ? 209 TYR B HD1  1 
ATOM   7734 H HD2  . TYR B 2 209 ? -1.82600  18.46200  14.95900  1.000 45.72937  ? 209 TYR B HD2  1 
ATOM   7735 H HE1  . TYR B 2 209 ? -4.15200  22.13700  16.57200  1.000 61.95677  ? 209 TYR B HE1  1 
ATOM   7736 H HE2  . TYR B 2 209 ? -1.29900  20.61000  14.19100  1.000 52.83707  ? 209 TYR B HE2  1 
ATOM   7737 H HH   . TYR B 2 209 ? -2.88100  23.42900  15.23900  1.000 63.99679  ? 209 TYR B HH   1 
ATOM   7738 N N    . ALA B 2 210 ? -3.67700  15.03300  18.53600  1.000 31.11316  ? 210 ALA B N    1 
ATOM   7739 C CA   . ALA B 2 210 ? -4.36100  13.93300  19.19200  1.000 33.42693  ? 210 ALA B CA   1 
ATOM   7740 C C    . ALA B 2 210 ? -4.23900  14.05900  20.70100  1.000 29.20511  ? 210 ALA B C    1 
ATOM   7741 O O    . ALA B 2 210 ? -5.18700  13.77900  21.44900  1.000 31.98733  ? 210 ALA B O    1 
ATOM   7742 C CB   . ALA B 2 210 ? -3.75700  12.60700  18.71900  1.000 30.09238  ? 210 ALA B CB   1 
ATOM   7743 H H    . ALA B 2 210 ? -3.07000  14.79700  17.97400  1.000 37.33659  ? 210 ALA B H    1 
ATOM   7744 H HA   . ALA B 2 210 ? -5.30200  13.94700  18.95500  1.000 40.11311  ? 210 ALA B HA   1 
ATOM   7745 H HB1  . ALA B 2 210 ? -4.21900  11.87600  19.15800  1.000 36.11166  ? 210 ALA B HB1  1 
ATOM   7746 H HB2  . ALA B 2 210 ? -3.86400  12.53700  17.75700  1.000 36.11166  ? 210 ALA B HB2  1 
ATOM   7747 H HB3  . ALA B 2 210 ? -2.81500  12.58900  18.95000  1.000 36.11166  ? 210 ALA B HB3  1 
ATOM   7748 N N    . ALA B 2 211 ? -3.06700  14.47000  21.16100  1.000 31.02558  ? 211 ALA B N    1 
ATOM   7749 C CA   . ALA B 2 211 ? -2.85600  14.63200  22.58800  1.000 34.17905  ? 211 ALA B CA   1 
ATOM   7750 C C    . ALA B 2 211 ? -3.79600  15.69000  23.13100  1.000 34.63205  ? 211 ALA B C    1 
ATOM   7751 O O    . ALA B 2 211 ? -4.45800  15.48500  24.15600  1.000 33.41731  ? 211 ALA B O    1 
ATOM   7752 C CB   . ALA B 2 211 ? -1.40600  15.02000  22.85200  1.000 34.46023  ? 211 ALA B CB   1 
ATOM   7753 H H    . ALA B 2 211 ? -2.38500  14.66000  20.67300  1.000 37.23149  ? 211 ALA B H    1 
ATOM   7754 H HA   . ALA B 2 211 ? -3.04000  13.79400  23.04100  1.000 41.01566  ? 211 ALA B HA   1 
ATOM   7755 H HB1  . ALA B 2 211 ? -1.27500  15.11900  23.80800  1.000 41.35307  ? 211 ALA B HB1  1 
ATOM   7756 H HB2  . ALA B 2 211 ? -0.82600  14.32300  22.50900  1.000 41.35307  ? 211 ALA B HB2  1 
ATOM   7757 H HB3  . ALA B 2 211 ? -1.21700  15.85900  22.40300  1.000 41.35307  ? 211 ALA B HB3  1 
ATOM   7758 N N    . VAL B 2 212 ? -3.90200  16.81900  22.42200  1.000 34.01907  ? 212 VAL B N    1 
ATOM   7759 C CA   . VAL B 2 212 ? -4.79000  17.87700  22.89600  1.000 37.95620  ? 212 VAL B CA   1 
ATOM   7760 C C    . VAL B 2 212 ? -6.24000  17.40900  22.88900  1.000 37.62557  ? 212 VAL B C    1 
ATOM   7761 O O    . VAL B 2 212 ? -6.99100  17.66600  23.84300  1.000 41.05577  ? 212 VAL B O    1 
ATOM   7762 C CB   . VAL B 2 212 ? -4.58500  19.16500  22.07500  1.000 41.22926  ? 212 VAL B CB   1 
ATOM   7763 C CG1  . VAL B 2 212 ? -5.68000  20.15300  22.41700  1.000 46.93881  ? 212 VAL B CG1  1 
ATOM   7764 C CG2  . VAL B 2 212 ? -3.25100  19.76900  22.43400  1.000 38.02659  ? 212 VAL B CG2  1 
ATOM   7765 H H    . VAL B 2 212 ? -3.48500  16.99000  21.69000  1.000 40.82368  ? 212 VAL B H    1 
ATOM   7766 H HA   . VAL B 2 212 ? -4.55800  18.08100  23.81500  1.000 45.54824  ? 212 VAL B HA   1 
ATOM   7767 H HB   . VAL B 2 212 ? -4.60800  18.97100  21.12500  1.000 49.47592  ? 212 VAL B HB   1 
ATOM   7768 H HG11 . VAL B 2 212 ? -5.39700  21.04000  22.14500  1.000 56.32737  ? 212 VAL B HG11 1 
ATOM   7769 H HG12 . VAL B 2 212 ? -6.49100  19.90700  21.94500  1.000 56.32737  ? 212 VAL B HG12 1 
ATOM   7770 H HG13 . VAL B 2 212 ? -5.83300  20.13600  23.37500  1.000 56.32737  ? 212 VAL B HG13 1 
ATOM   7771 H HG21 . VAL B 2 212 ? -3.11500  20.57000  21.90400  1.000 45.63271  ? 212 VAL B HG21 1 
ATOM   7772 H HG22 . VAL B 2 212 ? -3.24900  19.99200  23.37800  1.000 45.63271  ? 212 VAL B HG22 1 
ATOM   7773 H HG23 . VAL B 2 212 ? -2.55200  19.12400  22.24500  1.000 45.63271  ? 212 VAL B HG23 1 
ATOM   7774 N N    . ILE B 2 213 ? -6.64700  16.67500  21.84900  1.000 35.02858  ? 213 ILE B N    1 
ATOM   7775 C CA   . ILE B 2 213 ? -8.00800  16.14800  21.79200  1.000 39.77436  ? 213 ILE B CA   1 
ATOM   7776 C C    . ILE B 2 213 ? -8.28300  15.26900  23.00400  1.000 39.63735  ? 213 ILE B C    1 
ATOM   7777 O O    . ILE B 2 213 ? -9.40300  15.25300  23.54000  1.000 37.63517  ? 213 ILE B O    1 
ATOM   7778 C CB   . ILE B 2 213 ? -8.22000  15.38500  20.47400  1.000 40.84952  ? 213 ILE B CB   1 
ATOM   7779 C CG1  . ILE B 2 213 ? -8.34100  16.36300  19.29500  1.000 42.49223  ? 213 ILE B CG1  1 
ATOM   7780 C CG2  . ILE B 2 213 ? -9.42200  14.42500  20.56400  1.000 40.70215  ? 213 ILE B CG2  1 
ATOM   7781 C CD1  . ILE B 2 213 ? -8.24600  15.68800  17.96800  1.000 46.84941  ? 213 ILE B CD1  1 
ATOM   7782 H H    . ILE B 2 213 ? -6.15800  16.47100  21.17200  1.000 42.03509  ? 213 ILE B H    1 
ATOM   7783 H HA   . ILE B 2 213 ? -8.63400  16.88900  21.81200  1.000 47.73003  ? 213 ILE B HA   1 
ATOM   7784 H HB   . ILE B 2 213 ? -7.42900  14.84400  20.32200  1.000 49.02023  ? 213 ILE B HB   1 
ATOM   7785 H HG12 . ILE B 2 213 ? -9.20100  16.81000  19.34300  1.000 50.99147  ? 213 ILE B HG12 1 
ATOM   7786 H HG13 . ILE B 2 213 ? -7.62500  17.01500  19.35100  1.000 50.99147  ? 213 ILE B HG13 1 
ATOM   7787 H HG21 . ILE B 2 213 ? -9.67800  14.14900  19.67100  1.000 48.84338  ? 213 ILE B HG21 1 
ATOM   7788 H HG22 . ILE B 2 213 ? -9.17000  13.64700  21.08600  1.000 48.84338  ? 213 ILE B HG22 1 
ATOM   7789 H HG23 . ILE B 2 213 ? -10.16200 14.88600  20.98900  1.000 48.84338  ? 213 ILE B HG23 1 
ATOM   7790 H HD11 . ILE B 2 213 ? -8.12300  16.36100  17.28100  1.000 56.22009  ? 213 ILE B HD11 1 
ATOM   7791 H HD12 . ILE B 2 213 ? -7.48900  15.08200  17.97600  1.000 56.22009  ? 213 ILE B HD12 1 
ATOM   7792 H HD13 . ILE B 2 213 ? -9.06400  15.19300  17.80400  1.000 56.22009  ? 213 ILE B HD13 1 
ATOM   7793 N N    . ASN B 2 214 ? -7.27700  14.51500  23.45000  1.000 31.50495  ? 214 ASN B N    1 
ATOM   7794 C CA   . ASN B 2 214 ? -7.37300  13.69500  24.64100  1.000 33.37944  ? 214 ASN B CA   1 
ATOM   7795 C C    . ASN B 2 214 ? -7.07200  14.43700  25.94300  1.000 38.92453  ? 214 ASN B C    1 
ATOM   7796 O O    . ASN B 2 214 ? -6.89600  13.78700  26.98200  1.000 39.29185  ? 214 ASN B O    1 
ATOM   7797 C CB   . ASN B 2 214 ? -6.45900  12.49200  24.50200  1.000 34.64623  ? 214 ASN B CB   1 
ATOM   7798 C CG   . ASN B 2 214 ? -7.10300  11.41600  23.71200  1.000 38.32177  ? 214 ASN B CG   1 
ATOM   7799 O OD1  . ASN B 2 214 ? -7.83600  10.57900  24.27000  1.000 39.50880  ? 214 ASN B OD1  1 
ATOM   7800 N ND2  . ASN B 2 214 ? -6.92800  11.46300  22.40100  1.000 39.55903  ? 214 ASN B ND2  1 
ATOM   7801 H H    . ASN B 2 214 ? -6.51100  14.46600  23.06300  1.000 37.80675  ? 214 ASN B H    1 
ATOM   7802 H HA   . ASN B 2 214 ? -8.28100  13.36000  24.70600  1.000 40.05613  ? 214 ASN B HA   1 
ATOM   7803 H HB2  . ASN B 2 214 ? -5.64500  12.75800  24.04600  1.000 41.57627  ? 214 ASN B HB2  1 
ATOM   7804 H HB3  . ASN B 2 214 ? -6.25200  12.13900  25.38100  1.000 41.57627  ? 214 ASN B HB3  1 
ATOM   7805 H HD21 . ASN B 2 214 ? -7.28800  10.86600  21.89800  1.000 47.47164  ? 214 ASN B HD21 1 
ATOM   7806 H HD22 . ASN B 2 214 ? -6.42500  12.06900  22.05600  1.000 47.47164  ? 214 ASN B HD22 1 
ATOM   7807 N N    . GLY B 2 215 ? -7.00400  15.76300  25.92600  1.000 37.34746  ? 215 GLY B N    1 
ATOM   7808 C CA   . GLY B 2 215 ? -6.88400  16.48800  27.17600  1.000 39.83528  ? 215 GLY B CA   1 
ATOM   7809 C C    . GLY B 2 215 ? -5.47300  16.58400  27.71600  1.000 43.47881  ? 215 GLY B C    1 
ATOM   7810 O O    . GLY B 2 215 ? -5.28500  17.01100  28.86100  1.000 45.77750  ? 215 GLY B O    1 
ATOM   7811 H H    . GLY B 2 215 ? -7.02500  16.25400  25.22000  1.000 44.81775  ? 215 GLY B H    1 
ATOM   7812 H HA2  . GLY B 2 215 ? -7.21900  17.39000  27.05100  1.000 47.80314  ? 215 GLY B HA2  1 
ATOM   7813 H HA3  . GLY B 2 215 ? -7.43400  16.05400  27.84700  1.000 47.80314  ? 215 GLY B HA3  1 
ATOM   7814 N N    . ASP B 2 216 ? -4.47300  16.23400  26.92800  1.000 39.44740  ? 216 ASP B N    1 
ATOM   7815 C CA   . ASP B 2 216 ? -3.09000  16.28000  27.36700  1.000 38.75029  ? 216 ASP B CA   1 
ATOM   7816 C C    . ASP B 2 216 ? -2.51300  17.52500  26.70700  1.000 47.64402  ? 216 ASP B C    1 
ATOM   7817 O O    . ASP B 2 216 ? -2.20500  17.50000  25.50600  1.000 46.52944  ? 216 ASP B O    1 
ATOM   7818 C CB   . ASP B 2 216 ? -2.38400  15.00100  26.91800  1.000 43.53443  ? 216 ASP B CB   1 
ATOM   7819 C CG   . ASP B 2 216 ? -1.28800  14.57300  27.86600  1.000 47.19719  ? 216 ASP B CG   1 
ATOM   7820 O OD1  . ASP B 2 216 ? -0.92200  15.36200  28.76300  1.000 48.59759  ? 216 ASP B OD1  1 
ATOM   7821 O OD2  . ASP B 2 216 ? -0.77600  13.44900  27.70100  1.000 45.01023  ? 216 ASP B OD2  1 
ATOM   7822 H H    . ASP B 2 216 ? -4.57000  15.96100  26.11800  1.000 47.33768  ? 216 ASP B H    1 
ATOM   7823 H HA   . ASP B 2 216 ? -3.03800  16.36500  28.33100  1.000 46.50115  ? 216 ASP B HA   1 
ATOM   7824 H HB2  . ASP B 2 216 ? -3.03400  14.28300  26.86900  1.000 52.24211  ? 216 ASP B HB2  1 
ATOM   7825 H HB3  . ASP B 2 216 ? -1.98600  15.14600  26.04600  1.000 52.24211  ? 216 ASP B HB3  1 
ATOM   7826 N N    . ARG B 2 217 ? -2.30500  18.57700  27.51100  1.000 40.90411  ? 217 ARG B N    1 
ATOM   7827 C CA   . ARG B 2 217 ? -2.07700  19.93300  27.02100  1.000 46.09331  ? 217 ARG B CA   1 
ATOM   7828 C C    . ARG B 2 217 ? -0.90000  20.65800  27.65200  1.000 39.29673  ? 217 ARG B C    1 
ATOM   7829 O O    . ARG B 2 217 ? -0.76500  21.87200  27.43900  1.000 45.03424  ? 217 ARG B O    1 
ATOM   7830 C CB   . ARG B 2 217 ? -3.32900  20.77900  27.28200  1.000 50.14397  ? 217 ARG B CB   1 
ATOM   7831 C CG   . ARG B 2 217 ? -4.55400  20.25200  26.58100  1.000 52.77712  ? 217 ARG B CG   1 
ATOM   7832 C CD   . ARG B 2 217 ? -5.78400  20.99300  27.07700  1.000 55.68212  ? 217 ARG B CD   1 
ATOM   7833 N NE   . ARG B 2 217 ? -5.72000  22.42800  26.83400  1.000 59.10039  ? 217 ARG B NE   1 
ATOM   7834 C CZ   . ARG B 2 217 ? -6.28500  23.01700  25.78600  1.000 59.43035  ? 217 ARG B CZ   1 
ATOM   7835 N NH1  . ARG B 2 217 ? -6.95600  22.32100  24.87900  1.000 58.68712  ? 217 ARG B NH1  1 
ATOM   7836 N NH2  . ARG B 2 217 ? -6.19100  24.33700  25.65200  1.000 59.43909  ? 217 ARG B NH2  1 
ATOM   7837 H H    . ARG B 2 217 ? -2.29200  18.52200  28.36900  1.000 49.08573  ? 217 ARG B H    1 
ATOM   7838 H HA   . ARG B 2 217 ? -1.93000  19.90200  26.06300  1.000 55.31278  ? 217 ARG B HA   1 
ATOM   7839 H HB2  . ARG B 2 217 ? -3.51000  20.78800  28.23500  1.000 60.17356  ? 217 ARG B HB2  1 
ATOM   7840 H HB3  . ARG B 2 217 ? -3.17100  21.68200  26.96700  1.000 60.17356  ? 217 ARG B HB3  1 
ATOM   7841 H HG2  . ARG B 2 217 ? -4.47000  20.39600  25.62500  1.000 63.33335  ? 217 ARG B HG2  1 
ATOM   7842 H HG3  . ARG B 2 217 ? -4.66400  19.30800  26.77600  1.000 63.33335  ? 217 ARG B HG3  1 
ATOM   7843 H HD2  . ARG B 2 217 ? -6.57200  20.63000  26.64700  1.000 66.81934  ? 217 ARG B HD2  1 
ATOM   7844 H HD3  . ARG B 2 217 ? -5.85200  20.86400  28.03600  1.000 66.81934  ? 217 ARG B HD3  1 
ATOM   7845 H HE   . ARG B 2 217 ? -5.18100  22.89400  27.31500  1.000 70.92127  ? 217 ARG B HE   1 
ATOM   7846 H HH11 . ARG B 2 217 ? -7.03000  21.46800  24.94700  1.000 70.42535  ? 217 ARG B HH11 1 
ATOM   7847 H HH12 . ARG B 2 217 ? -7.31400  22.72700  24.21100  1.000 70.42535  ? 217 ARG B HH12 1 
ATOM   7848 H HH21 . ARG B 2 217 ? -5.76000  24.79900  26.23600  1.000 71.32771  ? 217 ARG B HH21 1 
ATOM   7849 H HH22 . ARG B 2 217 ? -6.55500  24.72800  24.97800  1.000 71.32771  ? 217 ARG B HH22 1 
ATOM   7850 N N    . TRP B 2 218 ? -0.08400  19.98900  28.46800  1.000 41.00053  ? 218 TRP B N    1 
ATOM   7851 C CA   . TRP B 2 218 ? 0.92500   20.70500  29.24900  1.000 47.35243  ? 218 TRP B CA   1 
ATOM   7852 C C    . TRP B 2 218 ? 1.94600   21.42000  28.37800  1.000 43.31504  ? 218 TRP B C    1 
ATOM   7853 O O    . TRP B 2 218 ? 2.55000   22.39800  28.83000  1.000 43.39477  ? 218 TRP B O    1 
ATOM   7854 C CB   . TRP B 2 218 ? 1.61600   19.75000  30.22900  1.000 48.23990  ? 218 TRP B CB   1 
ATOM   7855 C CG   . TRP B 2 218 ? 2.36800   18.64800  29.59800  1.000 46.57211  ? 218 TRP B CG   1 
ATOM   7856 C CD1  . TRP B 2 218 ? 1.94900   17.32700  29.44900  1.000 43.21472  ? 218 TRP B CD1  1 
ATOM   7857 C CD2  . TRP B 2 218 ? 3.66900   18.72400  29.01300  1.000 45.28908  ? 218 TRP B CD2  1 
ATOM   7858 N NE1  . TRP B 2 218 ? 2.92900   16.59600  28.80300  1.000 41.84856  ? 218 TRP B NE1  1 
ATOM   7859 C CE2  . TRP B 2 218 ? 3.99200   17.42900  28.52800  1.000 45.16832  ? 218 TRP B CE2  1 
ATOM   7860 C CE3  . TRP B 2 218 ? 4.59300   19.76700  28.83200  1.000 45.53738  ? 218 TRP B CE3  1 
ATOM   7861 C CZ2  . TRP B 2 218 ? 5.20400   17.15500  27.88300  1.000 43.76369  ? 218 TRP B CZ2  1 
ATOM   7862 C CZ3  . TRP B 2 218 ? 5.80000   19.48700  28.21200  1.000 44.19894  ? 218 TRP B CZ3  1 
ATOM   7863 C CH2  . TRP B 2 218 ? 6.09500   18.19200  27.73800  1.000 46.42207  ? 218 TRP B CH2  1 
ATOM   7864 H H    . TRP B 2 218 ? -0.09300  19.13700  28.58600  1.000 49.20144  ? 218 TRP B H    1 
ATOM   7865 H HA   . TRP B 2 218 ? 0.47400   21.38200  29.77700  1.000 56.82372  ? 218 TRP B HA   1 
ATOM   7866 H HB2  . TRP B 2 218 ? 2.24100   20.26000  30.76800  1.000 57.88868  ? 218 TRP B HB2  1 
ATOM   7867 H HB3  . TRP B 2 218 ? 0.94100   19.35300  30.80100  1.000 57.88868  ? 218 TRP B HB3  1 
ATOM   7868 H HD1  . TRP B 2 218 ? 1.13500   16.98700  29.74300  1.000 51.85846  ? 218 TRP B HD1  1 
ATOM   7869 H HE1  . TRP B 2 218 ? 2.88500   15.75900  28.61100  1.000 50.21907  ? 218 TRP B HE1  1 
ATOM   7870 H HE3  . TRP B 2 218 ? 4.40900   20.62300  29.14600  1.000 54.64566  ? 218 TRP B HE3  1 
ATOM   7871 H HZ2  . TRP B 2 218 ? 5.40200   16.30100  27.57500  1.000 52.51723  ? 218 TRP B HZ2  1 
ATOM   7872 H HZ3  . TRP B 2 218 ? 6.42000   20.16900  28.09200  1.000 53.03952  ? 218 TRP B HZ3  1 
ATOM   7873 H HH2  . TRP B 2 218 ? 6.91000   18.03600  27.31700  1.000 55.70728  ? 218 TRP B HH2  1 
ATOM   7874 N N    . PHE B 2 219 ? 2.12200   20.98100  27.13500  1.000 43.24917  ? 219 PHE B N    1 
ATOM   7875 C CA   . PHE B 2 219 ? 3.13500   21.51000  26.23700  1.000 45.62921  ? 219 PHE B CA   1 
ATOM   7876 C C    . PHE B 2 219 ? 2.62000   22.69100  25.43000  1.000 44.61689  ? 219 PHE B C    1 
ATOM   7877 O O    . PHE B 2 219 ? 3.38400   23.30000  24.68300  1.000 40.25284  ? 219 PHE B O    1 
ATOM   7878 C CB   . PHE B 2 219 ? 3.59600   20.39600  25.27300  1.000 43.08244  ? 219 PHE B CB   1 
ATOM   7879 C CG   . PHE B 2 219 ? 2.45900   19.71200  24.61000  1.000 36.60390  ? 219 PHE B CG   1 
ATOM   7880 C CD1  . PHE B 2 219 ? 1.85900   20.26700  23.49000  1.000 37.50564  ? 219 PHE B CD1  1 
ATOM   7881 C CD2  . PHE B 2 219 ? 1.95600   18.52500  25.12600  1.000 40.24104  ? 219 PHE B CD2  1 
ATOM   7882 C CE1  . PHE B 2 219 ? 0.76300   19.65100  22.89700  1.000 37.06739  ? 219 PHE B CE1  1 
ATOM   7883 C CE2  . PHE B 2 219 ? 0.88400   17.89500  24.53300  1.000 36.51535  ? 219 PHE B CE2  1 
ATOM   7884 C CZ   . PHE B 2 219 ? 0.27300   18.46200  23.42200  1.000 38.83137  ? 219 PHE B CZ   1 
ATOM   7885 H H    . PHE B 2 219 ? 1.63900   20.36300  26.79000  1.000 51.89981  ? 219 PHE B H    1 
ATOM   7886 H HA   . PHE B 2 219 ? 3.90100   21.80400  26.75400  1.000 54.75586  ? 219 PHE B HA   1 
ATOM   7887 H HB2  . PHE B 2 219 ? 4.15600   20.78600  24.58300  1.000 51.69973  ? 219 PHE B HB2  1 
ATOM   7888 H HB3  . PHE B 2 219 ? 4.09700   19.73200  25.77200  1.000 51.69973  ? 219 PHE B HB3  1 
ATOM   7889 H HD1  . PHE B 2 219 ? 2.17700   21.07100  23.14800  1.000 45.00757  ? 219 PHE B HD1  1 
ATOM   7890 H HD2  . PHE B 2 219 ? 2.35100   18.14800  25.87900  1.000 48.29005  ? 219 PHE B HD2  1 
ATOM   7891 H HE1  . PHE B 2 219 ? 0.36800   20.02600  22.14300  1.000 44.48167  ? 219 PHE B HE1  1 
ATOM   7892 H HE2  . PHE B 2 219 ? 0.55700   17.10000  24.88800  1.000 43.81922  ? 219 PHE B HE2  1 
ATOM   7893 H HZ   . PHE B 2 219 ? -0.44600  18.03400  23.01600  1.000 46.59844  ? 219 PHE B HZ   1 
ATOM   7894 N N    . LEU B 2 220 ? 1.34400   23.03300  25.52100  1.000 39.46775  ? 220 LEU B N    1 
ATOM   7895 C CA   . LEU B 2 220 ? 0.93900   24.24800  24.83900  1.000 43.70315  ? 220 LEU B CA   1 
ATOM   7896 C C    . LEU B 2 220 ? 1.61000   25.45000  25.49600  1.000 43.33135  ? 220 LEU B C    1 
ATOM   7897 O O    . LEU B 2 220 ? 1.88900   25.46900  26.71400  1.000 42.06803  ? 220 LEU B O    1 
ATOM   7898 C CB   . LEU B 2 220 ? -0.58600  24.39800  24.83400  1.000 43.88481  ? 220 LEU B CB   1 
ATOM   7899 C CG   . LEU B 2 220 ? -1.34900  23.25900  24.15900  1.000 41.65801  ? 220 LEU B CG   1 
ATOM   7900 C CD1  . LEU B 2 220 ? -2.83400  23.47900  24.24400  1.000 45.87114  ? 220 LEU B CD1  1 
ATOM   7901 C CD2  . LEU B 2 220 ? -0.90800  23.12100  22.67500  1.000 40.90359  ? 220 LEU B CD2  1 
ATOM   7902 H H    . LEU B 2 220 ? 0.72700   22.60900  25.94400  1.000 47.36211  ? 220 LEU B H    1 
ATOM   7903 H HA   . LEU B 2 220 ? 1.23800   24.20900  23.91800  1.000 52.44458  ? 220 LEU B HA   1 
ATOM   7904 H HB2  . LEU B 2 220 ? -0.89300  24.45100  25.75300  1.000 52.66257  ? 220 LEU B HB2  1 
ATOM   7905 H HB3  . LEU B 2 220 ? -0.81300  25.21800  24.36800  1.000 52.66257  ? 220 LEU B HB3  1 
ATOM   7906 H HG   . LEU B 2 220 ? -1.14200  22.42700  24.61300  1.000 49.99042  ? 220 LEU B HG   1 
ATOM   7907 H HD11 . LEU B 2 220 ? -3.28800  22.74000  23.80900  1.000 55.04617  ? 220 LEU B HD11 1 
ATOM   7908 H HD12 . LEU B 2 220 ? -3.09300  23.52400  25.17800  1.000 55.04617  ? 220 LEU B HD12 1 
ATOM   7909 H HD13 . LEU B 2 220 ? -3.05500  24.31200  23.79900  1.000 55.04617  ? 220 LEU B HD13 1 
ATOM   7910 H HD21 . LEU B 2 220 ? -1.51100  22.51100  22.22200  1.000 49.08511  ? 220 LEU B HD21 1 
ATOM   7911 H HD22 . LEU B 2 220 ? -0.94300  23.99400  22.25400  1.000 49.08511  ? 220 LEU B HD22 1 
ATOM   7912 H HD23 . LEU B 2 220 ? -0.00200  22.77500  22.64500  1.000 49.08511  ? 220 LEU B HD23 1 
ATOM   7913 N N    . ASN B 2 221 ? 1.90000   26.43300  24.62900  1.000 43.11560  ? 221 ASN B N    1 
ATOM   7914 C CA   . ASN B 2 221 ? 2.55500   27.68200  25.09000  1.000 43.00008  ? 221 ASN B CA   1 
ATOM   7915 C C    . ASN B 2 221 ? 1.92200   28.88700  24.39700  1.000 42.82590  ? 221 ASN B C    1 
ATOM   7916 O O    . ASN B 2 221 ? 1.09200   28.70500  23.50800  1.000 41.26030  ? 221 ASN B O    1 
ATOM   7917 C CB   . ASN B 2 221 ? 4.08200   27.64500  24.98400  1.000 43.13143  ? 221 ASN B CB   1 
ATOM   7918 C CG   . ASN B 2 221 ? 4.68000   27.43400  23.60700  1.000 42.54502  ? 221 ASN B CG   1 
ATOM   7919 O OD1  . ASN B 2 221 ? 4.06500   27.76500  22.60400  1.000 44.18602  ? 221 ASN B OD1  1 
ATOM   7920 N ND2  . ASN B 2 221 ? 5.89200   26.93400  23.52700  1.000 47.25369  ? 221 ASN B ND2  1 
ATOM   7921 H H    . ASN B 2 221 ? 1.73400   26.40800  23.78600  1.000 51.73952  ? 221 ASN B H    1 
ATOM   7922 H HA   . ASN B 2 221 ? 2.35500   27.78000  26.03400  1.000 51.60089  ? 221 ASN B HA   1 
ATOM   7923 H HB2  . ASN B 2 221 ? 4.42700   28.48800  25.31800  1.000 51.75852  ? 221 ASN B HB2  1 
ATOM   7924 H HB3  . ASN B 2 221 ? 4.40500   26.92400  25.54700  1.000 51.75852  ? 221 ASN B HB3  1 
ATOM   7925 H HD21 . ASN B 2 221 ? 6.25600   26.80800  22.75800  1.000 56.70523  ? 221 ASN B HD21 1 
ATOM   7926 H HD22 . ASN B 2 221 ? 6.31300   26.71400  24.24400  1.000 56.70523  ? 221 ASN B HD22 1 
ATOM   7927 N N    . ARG B 2 222 ? 2.31800   30.07500  24.81500  1.000 41.01729  ? 222 ARG B N    1 
ATOM   7928 C CA   . ARG B 2 222 ? 1.79300   31.30300  24.25900  1.000 42.66511  ? 222 ARG B CA   1 
ATOM   7929 C C    . ARG B 2 222 ? 2.43100   31.66900  22.92700  1.000 43.41006  ? 222 ARG B C    1 
ATOM   7930 O O    . ARG B 2 222 ? 1.97800   32.61400  22.28200  1.000 44.73211  ? 222 ARG B O    1 
ATOM   7931 C CB   . ARG B 2 222 ? 2.06300   32.46300  25.21500  1.000 44.63237  ? 222 ARG B CB   1 
ATOM   7932 C CG   . ARG B 2 222 ? 3.53300   32.95000  25.18100  1.000 45.98090  ? 222 ARG B CG   1 
ATOM   7933 C CD   . ARG B 2 222 ? 3.76600   34.31300  25.90000  1.000 48.37615  ? 222 ARG B CD   1 
ATOM   7934 N NE   . ARG B 2 222 ? 3.00900   34.41300  27.13400  1.000 48.34070  ? 222 ARG B NE   1 
ATOM   7935 C CZ   . ARG B 2 222 ? 2.18100   35.40500  27.43000  1.000 49.73564  ? 222 ARG B CZ   1 
ATOM   7936 N NH1  . ARG B 2 222 ? 1.95400   36.39700  26.58000  1.000 51.30290  ? 222 ARG B NH1  1 
ATOM   7937 N NH2  . ARG B 2 222 ? 1.54400   35.38700  28.60000  1.000 49.60253  ? 222 ARG B NH2  1 
ATOM   7938 H H    . ARG B 2 222 ? 2.90300   30.19700  25.43300  1.000 49.21674  ? 222 ARG B H    1 
ATOM   7939 H HA   . ARG B 2 222 ? 0.83500   31.22100  24.13200  1.000 51.19413  ? 222 ARG B HA   1 
ATOM   7940 H HB2  . ARG B 2 222 ? 1.49500   33.21100  24.97100  1.000 53.55484  ? 222 ARG B HB2  1 
ATOM   7941 H HB3  . ARG B 2 222 ? 1.86400   32.17800  26.12000  1.000 53.55484  ? 222 ARG B HB3  1 
ATOM   7942 H HG2  . ARG B 2 222 ? 4.08900   32.28700  25.62000  1.000 55.17308  ? 222 ARG B HG2  1 
ATOM   7943 H HG3  . ARG B 2 222 ? 3.83800   33.07900  24.27200  1.000 55.17308  ? 222 ARG B HG3  1 
ATOM   7944 H HD2  . ARG B 2 222 ? 4.70700   34.39200  26.12300  1.000 58.04737  ? 222 ARG B HD2  1 
ATOM   7945 H HD3  . ARG B 2 222 ? 3.51200   35.02500  25.29700  1.000 58.04737  ? 222 ARG B HD3  1 
ATOM   7946 H HE   . ARG B 2 222 ? 3.10400   33.78500  27.71400  1.000 58.00483  ? 222 ARG B HE   1 
ATOM   7947 H HH11 . ARG B 2 222 ? 2.35100   36.42700  25.82000  1.000 61.55948  ? 222 ARG B HH11 1 
ATOM   7948 H HH12 . ARG B 2 222 ? 1.40900   37.02500  26.79800  1.000 61.55948  ? 222 ARG B HH12 1 
ATOM   7949 H HH21 . ARG B 2 222 ? 1.68300   34.74500  29.15500  1.000 59.51903  ? 222 ARG B HH21 1 
ATOM   7950 H HH22 . ARG B 2 222 ? 1.00100   36.02200  28.80400  1.000 59.51903  ? 222 ARG B HH22 1 
ATOM   7951 N N    . PHE B 2 223 ? 3.44200   30.95300  22.49400  1.000 42.67940  ? 223 PHE B N    1 
ATOM   7952 C CA   . PHE B 2 223 ? 4.27400   31.45600  21.40600  1.000 43.78320  ? 223 PHE B CA   1 
ATOM   7953 C C    . PHE B 2 223 ? 3.74600   30.92200  20.08300  1.000 42.74672  ? 223 PHE B C    1 
ATOM   7954 O O    . PHE B 2 223 ? 3.11600   29.86500  20.02500  1.000 42.93125  ? 223 PHE B O    1 
ATOM   7955 C CB   . PHE B 2 223 ? 5.73300   31.03400  21.63500  1.000 43.80577  ? 223 PHE B CB   1 
ATOM   7956 C CG   . PHE B 2 223 ? 6.29200   31.52200  22.94000  1.000 44.88039  ? 223 PHE B CG   1 
ATOM   7957 C CD1  . PHE B 2 223 ? 6.50500   32.88600  23.15200  1.000 47.16176  ? 223 PHE B CD1  1 
ATOM   7958 C CD2  . PHE B 2 223 ? 6.53900   30.63600  23.98900  1.000 43.70515  ? 223 PHE B CD2  1 
ATOM   7959 C CE1  . PHE B 2 223 ? 6.98800   33.34900  24.37900  1.000 48.24569  ? 223 PHE B CE1  1 
ATOM   7960 C CE2  . PHE B 2 223 ? 7.02500   31.09100  25.21300  1.000 44.75370  ? 223 PHE B CE2  1 
ATOM   7961 C CZ   . PHE B 2 223 ? 7.24900   32.45400  25.41000  1.000 47.02912  ? 223 PHE B CZ   1 
ATOM   7962 H H    . PHE B 2 223 ? 3.67300   30.18300  22.80000  1.000 51.21127  ? 223 PHE B H    1 
ATOM   7963 H HA   . PHE B 2 223 ? 4.23400   32.42500  21.38600  1.000 52.53583  ? 223 PHE B HA   1 
ATOM   7964 H HB2  . PHE B 2 223 ? 5.78400   30.06500  21.63200  1.000 52.56292  ? 223 PHE B HB2  1 
ATOM   7965 H HB3  . PHE B 2 223 ? 6.28100   31.39600  20.92100  1.000 52.56292  ? 223 PHE B HB3  1 
ATOM   7966 H HD1  . PHE B 2 223 ? 6.33100   33.49100  22.46800  1.000 56.59011  ? 223 PHE B HD1  1 
ATOM   7967 H HD2  . PHE B 2 223 ? 6.39000   29.72600  23.86500  1.000 52.44217  ? 223 PHE B HD2  1 
ATOM   7968 H HE1  . PHE B 2 223 ? 7.14000   34.25800  24.50400  1.000 57.89082  ? 223 PHE B HE1  1 
ATOM   7969 H HE2  . PHE B 2 223 ? 7.19800   30.48700  25.89900  1.000 53.70043  ? 223 PHE B HE2  1 
ATOM   7970 H HZ   . PHE B 2 223 ? 7.57700   32.76100  26.22400  1.000 56.43094  ? 223 PHE B HZ   1 
ATOM   7971 N N    . THR B 2 224 ? 3.97200   31.67900  19.02200  1.000 44.03559  ? 224 THR B N    1 
ATOM   7972 C CA   . THR B 2 224 ? 3.71100   31.16800  17.68700  1.000 47.08357  ? 224 THR B CA   1 
ATOM   7973 C C    . THR B 2 224 ? 4.98200   31.33700  16.87300  1.000 44.04011  ? 224 THR B C    1 
ATOM   7974 O O    . THR B 2 224 ? 5.95500   31.94800  17.32200  1.000 45.63915  ? 224 THR B O    1 
ATOM   7975 C CB   . THR B 2 224 ? 2.53400   31.89200  17.00900  1.000 48.94593  ? 224 THR B CB   1 
ATOM   7976 O OG1  . THR B 2 224 ? 2.17300   31.18700  15.81600  1.000 62.24617  ? 224 THR B OG1  1 
ATOM   7977 C CG2  . THR B 2 224 ? 2.93700   33.29300  16.62000  1.000 47.95759  ? 224 THR B CG2  1 
ATOM   7978 H H    . THR B 2 224 ? 4.27300   32.48400  19.04600  1.000 52.83870  ? 224 THR B H    1 
ATOM   7979 H HA   . THR B 2 224 ? 3.50300   30.22200  17.73200  1.000 56.50109  ? 224 THR B HA   1 
ATOM   7980 H HB   . THR B 2 224 ? 1.77600   31.93600  17.61300  1.000 58.73592  ? 224 THR B HB   1 
ATOM   7981 H HG1  . THR B 2 224 ? 1.53100   31.57400  15.43700  1.000 74.69621  ? 224 THR B HG1  1 
ATOM   7982 H HG21 . THR B 2 224 ? 2.15600   33.86800  16.59200  1.000 57.54991  ? 224 THR B HG21 1 
ATOM   7983 H HG22 . THR B 2 224 ? 3.56700   33.64700  17.26600  1.000 57.54991  ? 224 THR B HG22 1 
ATOM   7984 H HG23 . THR B 2 224 ? 3.35700   33.28600  15.74600  1.000 57.54991  ? 224 THR B HG23 1 
ATOM   7985 N N    . THR B 2 225 ? 4.97200   30.82500  15.65100  1.000 49.21705  ? 225 THR B N    1 
ATOM   7986 C CA   . THR B 2 225 ? 6.17300   30.90400  14.83200  1.000 52.55072  ? 225 THR B CA   1 
ATOM   7987 C C    . THR B 2 225 ? 5.77300   30.99300  13.36100  1.000 51.93504  ? 225 THR B C    1 
ATOM   7988 O O    . THR B 2 225 ? 4.59300   30.94600  13.00100  1.000 54.42705  ? 225 THR B O    1 
ATOM   7989 C CB   . THR B 2 225 ? 7.09100   29.70300  15.07700  1.000 52.06459  ? 225 THR B CB   1 
ATOM   7990 O OG1  . THR B 2 225 ? 8.32000   29.89200  14.36300  1.000 54.62316  ? 225 THR B OG1  1 
ATOM   7991 C CG2  . THR B 2 225 ? 6.40100   28.42700  14.54800  1.000 47.97642  ? 225 THR B CG2  1 
ATOM   7992 H H    . THR B 2 225 ? 4.30100   30.43600  15.27900  1.000 59.06126  ? 225 THR B H    1 
ATOM   7993 H HA   . THR B 2 225 ? 6.66400   31.71000  15.05700  1.000 63.06167  ? 225 THR B HA   1 
ATOM   7994 H HB   . THR B 2 225 ? 7.26600   29.60200  16.02600  1.000 62.47830  ? 225 THR B HB   1 
ATOM   7995 H HG1  . THR B 2 225 ? 8.23200   29.64500  13.56500  1.000 65.54859  ? 225 THR B HG1  1 
ATOM   7996 H HG21 . THR B 2 225 ? 6.83900   27.64100  14.90900  1.000 57.57250  ? 225 THR B HG21 1 
ATOM   7997 H HG22 . THR B 2 225 ? 5.46900   28.41800  14.81600  1.000 57.57250  ? 225 THR B HG22 1 
ATOM   7998 H HG23 . THR B 2 225 ? 6.45000   28.39700  13.58000  1.000 57.57250  ? 225 THR B HG23 1 
ATOM   7999 N N    . THR B 2 226 ? 6.76100   31.17700  12.51200  1.000 54.75974  ? 226 THR B N    1 
ATOM   8000 C CA   . THR B 2 226 ? 6.54000   31.03800  11.08100  1.000 59.35861  ? 226 THR B CA   1 
ATOM   8001 C C    . THR B 2 226 ? 7.09500   29.72100  10.55200  1.000 56.04370  ? 226 THR B C    1 
ATOM   8002 O O    . THR B 2 226 ? 8.04600   29.14000  11.09500  1.000 54.28296  ? 226 THR B O    1 
ATOM   8003 C CB   . THR B 2 226 ? 7.17100   32.19400  10.31400  1.000 56.75277  ? 226 THR B CB   1 
ATOM   8004 O OG1  . THR B 2 226 ? 8.59400   32.09900  10.43700  1.000 61.77025  ? 226 THR B OG1  1 
ATOM   8005 C CG2  . THR B 2 226 ? 6.68300   33.53100  10.88500  1.000 57.94347  ? 226 THR B CG2  1 
ATOM   8006 H H    . THR B 2 226 ? 7.56700   31.38200  12.73200  1.000 65.71249  ? 226 THR B H    1 
ATOM   8007 H HA   . THR B 2 226 ? 5.58800   31.05100  10.90000  1.000 71.23114  ? 226 THR B HA   1 
ATOM   8008 H HB   . THR B 2 226 ? 6.91900   32.14300  9.37900   1.000 68.10413  ? 226 THR B HB   1 
ATOM   8009 H HG1  . THR B 2 226 ? 8.81300   32.27900  11.22500  1.000 74.12510  ? 226 THR B HG1  1 
ATOM   8010 H HG21 . THR B 2 226 ? 6.99700   34.26200  10.33000  1.000 69.53296  ? 226 THR B HG21 1 
ATOM   8011 H HG22 . THR B 2 226 ? 5.71300   33.54700  10.90800  1.000 69.53296  ? 226 THR B HG22 1 
ATOM   8012 H HG23 . THR B 2 226 ? 7.02200   33.65200  11.78600  1.000 69.53296  ? 226 THR B HG23 1 
ATOM   8013 N N    . LEU B 2 227 ? 6.53700   29.32200  9.40600   1.000 60.59257  ? 227 LEU B N    1 
ATOM   8014 C CA   . LEU B 2 227 ? 7.00900   28.14400  8.69400   1.000 56.64832  ? 227 LEU B CA   1 
ATOM   8015 C C    . LEU B 2 227 ? 8.51800   28.20600  8.48400   1.000 52.61816  ? 227 LEU B C    1 
ATOM   8016 O O    . LEU B 2 227 ? 9.22400   27.22100  8.71400   1.000 50.01512  ? 227 LEU B O    1 
ATOM   8017 C CB   . LEU B 2 227 ? 6.29600   28.07100  7.34800   1.000 56.31236  ? 227 LEU B CB   1 
ATOM   8018 C CG   . LEU B 2 227 ? 6.36700   26.70600  6.72600   1.000 54.07047  ? 227 LEU B CG   1 
ATOM   8019 C CD1  . LEU B 2 227 ? 5.88900   25.76100  7.81400   1.000 53.00212  ? 227 LEU B CD1  1 
ATOM   8020 C CD2  . LEU B 2 227 ? 5.44400   26.66100  5.51500   1.000 58.32008  ? 227 LEU B CD2  1 
ATOM   8021 H H    . LEU B 2 227 ? 5.88000   29.72300  9.02200   1.000 72.71189  ? 227 LEU B H    1 
ATOM   8022 H HA   . LEU B 2 227 ? 6.82100   27.38500  9.25800   1.000 67.97878  ? 227 LEU B HA   1 
ATOM   8023 H HB2  . LEU B 2 227 ? 5.36100   28.29700  7.47200   1.000 67.57564  ? 227 LEU B HB2  1 
ATOM   8024 H HB3  . LEU B 2 227 ? 6.71100   28.70000  6.73700   1.000 67.57564  ? 227 LEU B HB3  1 
ATOM   8025 H HG   . LEU B 2 227 ? 7.27500   26.48600  6.46600   1.000 64.88536  ? 227 LEU B HG   1 
ATOM   8026 H HD11 . LEU B 2 227 ? 5.49300   24.98300  7.39000   1.000 63.60335  ? 227 LEU B HD11 1 
ATOM   8027 H HD12 . LEU B 2 227 ? 6.64400   25.48200  8.35500   1.000 63.60335  ? 227 LEU B HD12 1 
ATOM   8028 H HD13 . LEU B 2 227 ? 5.22000   26.20400  8.36000   1.000 63.60335  ? 227 LEU B HD13 1 
ATOM   8029 H HD21 . LEU B 2 227 ? 5.49900   25.78100  5.11000   1.000 69.98490  ? 227 LEU B HD21 1 
ATOM   8030 H HD22 . LEU B 2 227 ? 4.53500   26.83600  5.80400   1.000 69.98490  ? 227 LEU B HD22 1 
ATOM   8031 H HD23 . LEU B 2 227 ? 5.72500   27.33700  4.87900   1.000 69.98490  ? 227 LEU B HD23 1 
ATOM   8032 N N    . ASN B 2 228 ? 9.03600   29.36900  8.07700   1.000 58.14017  ? 228 ASN B N    1 
ATOM   8033 C CA   . ASN B 2 228 ? 10.46800  29.49900  7.80600   1.000 53.72855  ? 228 ASN B CA   1 
ATOM   8034 C C    . ASN B 2 228 ? 11.29000  29.44000  9.08800   1.000 56.96432  ? 228 ASN B C    1 
ATOM   8035 O O    . ASN B 2 228 ? 12.37500  28.84800  9.11600   1.000 54.93347  ? 228 ASN B O    1 
ATOM   8036 C CB   . ASN B 2 228 ? 10.74400  30.81500  7.07700   1.000 58.66261  ? 228 ASN B CB   1 
ATOM   8037 C CG   . ASN B 2 228 ? 12.16300  30.88300  6.50700   1.000 65.46985  ? 228 ASN B CG   1 
ATOM   8038 O OD1  . ASN B 2 228 ? 12.54300  30.05700  5.67100   1.000 72.70493  ? 228 ASN B OD1  1 
ATOM   8039 N ND2  . ASN B 2 228 ? 12.94400  31.88200  6.93900   1.000 67.68409  ? 228 ASN B ND2  1 
ATOM   8040 H H    . ASN B 2 228 ? 8.58400   30.09000  7.95200   1.000 69.76901  ? 228 ASN B H    1 
ATOM   8041 H HA   . ASN B 2 228 ? 10.75100  28.77000  7.23200   1.000 64.47506  ? 228 ASN B HA   1 
ATOM   8042 H HB2  . ASN B 2 228 ? 10.11900  30.90600  6.34000   1.000 70.39594  ? 228 ASN B HB2  1 
ATOM   8043 H HB3  . ASN B 2 228 ? 10.63400  31.55100  7.69900   1.000 70.39594  ? 228 ASN B HB3  1 
ATOM   8044 H HD21 . ASN B 2 228 ? 13.74800  31.95800  6.64300   1.000 81.22171  ? 228 ASN B HD21 1 
ATOM   8045 H HD22 . ASN B 2 228 ? 12.64500  32.44200  7.51900   1.000 81.22171  ? 228 ASN B HD22 1 
ATOM   8046 N N    . ASP B 2 229 ? 10.81600  30.10800  10.14400  1.000 65.27376  ? 229 ASP B N    1 
ATOM   8047 C CA   . ASP B 2 229 ? 11.51500  30.09800  11.42200  1.000 57.64325  ? 229 ASP B CA   1 
ATOM   8048 C C    . ASP B 2 229 ? 11.49500  28.70600  12.04300  1.000 55.84560  ? 229 ASP B C    1 
ATOM   8049 O O    . ASP B 2 229 ? 12.51000  28.22700  12.56900  1.000 57.82670  ? 229 ASP B O    1 
ATOM   8050 C CB   . ASP B 2 229 ? 10.85400  31.11400  12.35700  1.000 57.70604  ? 229 ASP B CB   1 
ATOM   8051 C CG   . ASP B 2 229 ? 11.11700  32.55400  11.93800  1.000 67.56210  ? 229 ASP B CG   1 
ATOM   8052 O OD1  . ASP B 2 229 ? 12.15400  32.81200  11.28300  1.000 70.80454  ? 229 ASP B OD1  1 
ATOM   8053 O OD2  . ASP B 2 229 ? 10.26500  33.42400  12.22700  1.000 66.65273  ? 229 ASP B OD2  1 
ATOM   8054 H H    . ASP B 2 229 ? 10.09200  30.57300  10.14200  1.000 78.32932  ? 229 ASP B H    1 
ATOM   8055 H HA   . ASP B 2 229 ? 12.43900  30.35900  11.28700  1.000 69.17270  ? 229 ASP B HA   1 
ATOM   8056 H HB2  . ASP B 2 229 ? 9.89600   30.96700  12.35800  1.000 69.24805  ? 229 ASP B HB2  1 
ATOM   8057 H HB3  . ASP B 2 229 ? 11.20700  30.99400  13.25200  1.000 69.24805  ? 229 ASP B HB3  1 
ATOM   8058 N N    . PHE B 2 230 ? 10.35100  28.03500  11.97700  1.000 48.72749  ? 230 PHE B N    1 
ATOM   8059 C CA   . PHE B 2 230 ? 10.29000  26.68100  12.52800  1.000 52.48065  ? 230 PHE B CA   1 
ATOM   8060 C C    . PHE B 2 230 ? 11.24400  25.73800  11.80100  1.000 56.10208  ? 230 PHE B C    1 
ATOM   8061 O O    . PHE B 2 230 ? 12.01100  25.01100  12.43700  1.000 55.09105  ? 230 PHE B O    1 
ATOM   8062 C CB   . PHE B 2 230 ? 8.87800   26.13400  12.45100  1.000 48.02538  ? 230 PHE B CB   1 
ATOM   8063 C CG   . PHE B 2 230 ? 8.79100   24.71400  12.88600  1.000 42.81304  ? 230 PHE B CG   1 
ATOM   8064 C CD1  . PHE B 2 230 ? 8.74400   24.40500  14.23600  1.000 52.23894  ? 230 PHE B CD1  1 
ATOM   8065 C CD2  . PHE B 2 230 ? 8.80600   23.67600  11.96700  1.000 44.32365  ? 230 PHE B CD2  1 
ATOM   8066 C CE1  . PHE B 2 230 ? 8.67500   23.09500  14.65200  1.000 48.45052  ? 230 PHE B CE1  1 
ATOM   8067 C CE2  . PHE B 2 230 ? 8.74800   22.35200  12.38400  1.000 46.23435  ? 230 PHE B CE2  1 
ATOM   8068 C CZ   . PHE B 2 230 ? 8.68000   22.06300  13.73300  1.000 44.94226  ? 230 PHE B CZ   1 
ATOM   8069 H H    . PHE B 2 230 ? 9.61900   28.32500  11.63200  1.000 58.47379  ? 230 PHE B H    1 
ATOM   8070 H HA   . PHE B 2 230 ? 10.55200  26.70400  13.45700  1.000 62.97758  ? 230 PHE B HA   1 
ATOM   8071 H HB2  . PHE B 2 230 ? 8.30300   26.66100  13.02800  1.000 57.63126  ? 230 PHE B HB2  1 
ATOM   8072 H HB3  . PHE B 2 230 ? 8.56800   26.18700  11.53400  1.000 57.63126  ? 230 PHE B HB3  1 
ATOM   8073 H HD1  . PHE B 2 230 ? 8.73700   25.08900  14.86600  1.000 62.68753  ? 230 PHE B HD1  1 
ATOM   8074 H HD2  . PHE B 2 230 ? 8.84900   23.86900  11.05800  1.000 53.18918  ? 230 PHE B HD2  1 
ATOM   8075 H HE1  . PHE B 2 230 ? 8.63500   22.90200  15.56100  1.000 58.14142  ? 230 PHE B HE1  1 
ATOM   8076 H HE2  . PHE B 2 230 ? 8.74800   21.66700  11.75700  1.000 55.48202  ? 230 PHE B HE2  1 
ATOM   8077 H HZ   . PHE B 2 230 ? 8.63700   21.18000  14.02100  1.000 53.93152  ? 230 PHE B HZ   1 
ATOM   8078 N N    . ASN B 2 231 ? 11.23000  25.76900  10.45300  1.000 51.50913  ? 231 ASN B N    1 
ATOM   8079 C CA   . ASN B 2 231 ? 12.06600  24.87200  9.65000   1.000 57.84389  ? 231 ASN B CA   1 
ATOM   8080 C C    . ASN B 2 231 ? 13.54900  25.09300  9.88300   1.000 56.56993  ? 231 ASN B C    1 
ATOM   8081 O O    . ASN B 2 231 ? 14.33400  24.14000  9.81800   1.000 59.46119  ? 231 ASN B O    1 
ATOM   8082 C CB   . ASN B 2 231 ? 11.76700  25.04000  8.15500   1.000 52.46757  ? 231 ASN B CB   1 
ATOM   8083 C CG   . ASN B 2 231 ? 10.53500  24.31200  7.74200   1.000 52.02372  ? 231 ASN B CG   1 
ATOM   8084 O OD1  . ASN B 2 231 ? 10.23200  23.26200  8.28500   1.000 52.05409  ? 231 ASN B OD1  1 
ATOM   8085 N ND2  . ASN B 2 231 ? 9.80400   24.85900  6.80100   1.000 49.99925  ? 231 ASN B ND2  1 
ATOM   8086 H H    . ASN B 2 231 ? 10.74300  26.30300  9.98600   1.000 61.81176  ? 231 ASN B H    1 
ATOM   8087 H HA   . ASN B 2 231 ? 11.86400  23.95600  9.89500   1.000 69.41347  ? 231 ASN B HA   1 
ATOM   8088 H HB2  . ASN B 2 231 ? 11.64100  25.98200  7.96000   1.000 62.96189  ? 231 ASN B HB2  1 
ATOM   8089 H HB3  . ASN B 2 231 ? 12.51100  24.69000  7.64100   1.000 62.96189  ? 231 ASN B HB3  1 
ATOM   8090 H HD21 . ASN B 2 231 ? 9.08400   24.47100  6.53600   1.000 59.99990  ? 231 ASN B HD21 1 
ATOM   8091 H HD22 . ASN B 2 231 ? 10.04800  25.60200  6.44400   1.000 59.99990  ? 231 ASN B HD22 1 
ATOM   8092 N N    . LEU B 2 232 ? 13.95900  26.33700  10.11800  1.000 59.70892  ? 232 LEU B N    1 
ATOM   8093 C CA   . LEU B 2 232 ? 15.36500  26.58900  10.39300  1.000 61.58196  ? 232 LEU B CA   1 
ATOM   8094 C C    . LEU B 2 232 ? 15.81100  25.84100  11.64700  1.000 64.16226  ? 232 LEU B C    1 
ATOM   8095 O O    . LEU B 2 232 ? 16.85700  25.17500  11.64700  1.000 64.57402  ? 232 LEU B O    1 
ATOM   8096 C CB   . LEU B 2 232 ? 15.59200  28.09100  10.53900  1.000 63.11430  ? 232 LEU B CB   1 
ATOM   8097 C CG   . LEU B 2 232 ? 15.29800  28.91700  9.27200   1.000 72.32915  ? 232 LEU B CG   1 
ATOM   8098 C CD1  . LEU B 2 232 ? 15.40900  30.42500  9.52200   1.000 74.96780  ? 232 LEU B CD1  1 
ATOM   8099 C CD2  . LEU B 2 232 ? 16.15600  28.50100  8.07200   1.000 71.25587  ? 232 LEU B CD2  1 
ATOM   8100 H H    . LEU B 2 232 ? 13.45600  27.03400  10.12400  1.000 71.65150  ? 232 LEU B H    1 
ATOM   8101 H HA   . LEU B 2 232 ? 15.89800  26.27100  9.64800   1.000 73.89915  ? 232 LEU B HA   1 
ATOM   8102 H HB2  . LEU B 2 232 ? 15.01600  28.42300  11.24500  1.000 75.73797  ? 232 LEU B HB2  1 
ATOM   8103 H HB3  . LEU B 2 232 ? 16.52000  28.24100  10.77800  1.000 75.73797  ? 232 LEU B HB3  1 
ATOM   8104 H HG   . LEU B 2 232 ? 14.40000  28.73400  9.00500   1.000 86.79578  ? 232 LEU B HG   1 
ATOM   8105 H HD11 . LEU B 2 232 ? 15.21000  30.89700  8.69800   1.000 89.96216  ? 232 LEU B HD11 1 
ATOM   8106 H HD12 . LEU B 2 232 ? 14.77400  30.67800  10.21000  1.000 89.96216  ? 232 LEU B HD12 1 
ATOM   8107 H HD13 . LEU B 2 232 ? 16.31100  30.63100  9.81200   1.000 89.96216  ? 232 LEU B HD13 1 
ATOM   8108 H HD21 . LEU B 2 232 ? 16.00000  29.12200  7.34300   1.000 85.50784  ? 232 LEU B HD21 1 
ATOM   8109 H HD22 . LEU B 2 232 ? 17.09100  28.52200  8.33100   1.000 85.50784  ? 232 LEU B HD22 1 
ATOM   8110 H HD23 . LEU B 2 232 ? 15.90700  27.60400  7.80100   1.000 85.50784  ? 232 LEU B HD23 1 
ATOM   8111 N N    . VAL B 2 233 ? 14.98900  25.88300  12.70600  1.000 60.96302  ? 233 VAL B N    1 
ATOM   8112 C CA   . VAL B 2 233 ? 15.31900  25.17000  13.93400  1.000 60.59077  ? 233 VAL B CA   1 
ATOM   8113 C C    . VAL B 2 233 ? 15.16800  23.66600  13.74200  1.000 59.37271  ? 233 VAL B C    1 
ATOM   8114 O O    . VAL B 2 233 ? 16.00200  22.88200  14.20600  1.000 61.96533  ? 233 VAL B O    1 
ATOM   8115 C CB   . VAL B 2 233 ? 14.44700  25.68800  15.09900  1.000 60.92389  ? 233 VAL B CB   1 
ATOM   8116 C CG1  . VAL B 2 233 ? 14.78200  24.95400  16.37300  1.000 61.44381  ? 233 VAL B CG1  1 
ATOM   8117 C CG2  . VAL B 2 233 ? 14.59100  27.19100  15.26300  1.000 66.11803  ? 233 VAL B CG2  1 
ATOM   8118 H H    . VAL B 2 233 ? 14.24500  26.31300  12.73300  1.000 73.15643  ? 233 VAL B H    1 
ATOM   8119 H HA   . VAL B 2 233 ? 16.24600  25.34700  14.15800  1.000 72.70973  ? 233 VAL B HA   1 
ATOM   8120 H HB   . VAL B 2 233 ? 13.51700  25.50500  14.89300  1.000 73.10947  ? 233 VAL B HB   1 
ATOM   8121 H HG11 . VAL B 2 233 ? 14.37300  25.41900  17.12000  1.000 73.73337  ? 233 VAL B HG11 1 
ATOM   8122 H HG12 . VAL B 2 233 ? 14.43700  24.04900  16.32000  1.000 73.73337  ? 233 VAL B HG12 1 
ATOM   8123 H HG13 . VAL B 2 233 ? 15.74600  24.93700  16.48300  1.000 73.73337  ? 233 VAL B HG13 1 
ATOM   8124 H HG21 . VAL B 2 233 ? 14.09600  27.47100  16.04900  1.000 79.34243  ? 233 VAL B HG21 1 
ATOM   8125 H HG22 . VAL B 2 233 ? 15.53100  27.40800  15.36900  1.000 79.34243  ? 233 VAL B HG22 1 
ATOM   8126 H HG23 . VAL B 2 233 ? 14.23600  27.63100  14.47500  1.000 79.34243  ? 233 VAL B HG23 1 
ATOM   8127 N N    . ALA B 2 234 ? 14.09600  23.23600  13.06900  1.000 57.03582  ? 234 ALA B N    1 
ATOM   8128 C CA   . ALA B 2 234 ? 13.78200  21.81200  12.97400  1.000 60.79595  ? 234 ALA B CA   1 
ATOM   8129 C C    . ALA B 2 234 ? 14.82900  21.03500  12.18600  1.000 58.20599  ? 234 ALA B C    1 
ATOM   8130 O O    . ALA B 2 234 ? 15.17100  19.90500  12.55000  1.000 52.57846  ? 234 ALA B O    1 
ATOM   8131 C CB   . ALA B 2 234 ? 12.40000  21.62200  12.34100  1.000 58.71790  ? 234 ALA B CB   1 
ATOM   8132 H H    . ALA B 2 234 ? 13.53900  23.74800  12.66100  1.000 68.44379  ? 234 ALA B H    1 
ATOM   8133 H HA   . ALA B 2 234 ? 13.75100  21.44000  13.86900  1.000 72.95594  ? 234 ALA B HA   1 
ATOM   8134 H HB1  . ALA B 2 234 ? 12.20500  20.67300  12.28700  1.000 70.46228  ? 234 ALA B HB1  1 
ATOM   8135 H HB2  . ALA B 2 234 ? 11.73700  22.06500  12.89300  1.000 70.46228  ? 234 ALA B HB2  1 
ATOM   8136 H HB3  . ALA B 2 234 ? 12.40400  22.01100  11.45200  1.000 70.46228  ? 234 ALA B HB3  1 
ATOM   8137 N N    . MET B 2 235 ? 15.28700  21.58800  11.05600  1.000 59.99714  ? 235 MET B N    1 
ATOM   8138 C CA   . MET B 2 235 ? 16.33300  20.94600  10.26900  1.000 57.50518  ? 235 MET B CA   1 
ATOM   8139 C C    . MET B 2 235 ? 17.56700  20.63200  11.11000  1.000 58.04769  ? 235 MET B C    1 
ATOM   8140 O O    . MET B 2 235 ? 18.28600  19.66300  10.83600  1.000 57.46174  ? 235 MET B O    1 
ATOM   8141 C CB   . MET B 2 235 ? 16.69100  21.84200  9.07800   1.000 70.24314  ? 235 MET B CB   1 
ATOM   8142 C CG   . MET B 2 235 ? 17.73000  21.25900  8.12000   1.000 82.27822  ? 235 MET B CG   1 
ATOM   8143 S SD   . MET B 2 235 ? 18.00800  22.33500  6.67700   1.000 109.12484 ? 235 MET B SD   1 
ATOM   8144 C CE   . MET B 2 235 ? 16.57100  21.98100  5.64400   1.000 82.76469  ? 235 MET B CE   1 
ATOM   8145 H H    . MET B 2 235 ? 15.00600  22.33200  10.72900  1.000 71.99737  ? 235 MET B H    1 
ATOM   8146 H HA   . MET B 2 235 ? 15.98400  20.11400  9.91400   1.000 69.00702  ? 235 MET B HA   1 
ATOM   8147 H HB2  . MET B 2 235 ? 15.88700  22.01000  8.56900   1.000 84.29257  ? 235 MET B HB2  1 
ATOM   8148 H HB3  . MET B 2 235 ? 17.04300  22.68000  9.41700   1.000 84.29257  ? 235 MET B HB3  1 
ATOM   8149 H HG2  . MET B 2 235 ? 18.57400  21.15800  8.58700   1.000 98.73466  ? 235 MET B HG2  1 
ATOM   8150 H HG3  . MET B 2 235 ? 17.42000  20.39700  7.80000   1.000 98.73466  ? 235 MET B HG3  1 
ATOM   8151 H HE1  . MET B 2 235 ? 16.85800  21.89900  4.72100   1.000 99.31843  ? 235 MET B HE1  1 
ATOM   8152 H HE2  . MET B 2 235 ? 16.16700  21.15000  5.94000   1.000 99.31843  ? 235 MET B HE2  1 
ATOM   8153 H HE3  . MET B 2 235 ? 15.93500  22.70800  5.73000   1.000 99.31843  ? 235 MET B HE3  1 
ATOM   8154 N N    . LYS B 2 236 ? 17.86000  21.46300  12.10800  1.000 56.29867  ? 236 LYS B N    1 
ATOM   8155 C CA   . LYS B 2 236 ? 19.02500  21.22400  12.95000  1.000 54.75949  ? 236 LYS B CA   1 
ATOM   8156 C C    . LYS B 2 236 ? 18.85600  20.00800  13.86100  1.000 57.11878  ? 236 LYS B C    1 
ATOM   8157 O O    . LYS B 2 236 ? 19.85700  19.48600  14.36300  1.000 56.94159  ? 236 LYS B O    1 
ATOM   8158 C CB   . LYS B 2 236 ? 19.30600  22.47000  13.79900  1.000 58.12746  ? 236 LYS B CB   1 
ATOM   8159 C CG   . LYS B 2 236 ? 19.48500  23.77000  12.99200  1.000 62.24378  ? 236 LYS B CG   1 
ATOM   8160 C CD   . LYS B 2 236 ? 19.97200  24.91300  13.92600  1.000 65.65463  ? 236 LYS B CD   1 
ATOM   8161 C CE   . LYS B 2 236 ? 20.00300  26.26500  13.23100  1.000 67.56346  ? 236 LYS B CE   1 
ATOM   8162 N NZ   . LYS B 2 236 ? 20.38400  27.39000  14.14600  1.000 74.15118  ? 236 LYS B NZ   1 
ATOM   8163 H H    . LYS B 2 236 ? 17.40600  22.16300  12.31500  1.000 67.55921  ? 236 LYS B H    1 
ATOM   8164 H HA   . LYS B 2 236 ? 19.79600  21.06800  12.38300  1.000 65.71219  ? 236 LYS B HA   1 
ATOM   8165 H HB2  . LYS B 2 236 ? 18.56400  22.60300  14.40900  1.000 69.75375  ? 236 LYS B HB2  1 
ATOM   8166 H HB3  . LYS B 2 236 ? 20.12100  22.32300  14.30400  1.000 69.75375  ? 236 LYS B HB3  1 
ATOM   8167 H HG2  . LYS B 2 236 ? 20.14900  23.63300  12.29900  1.000 74.69334  ? 236 LYS B HG2  1 
ATOM   8168 H HG3  . LYS B 2 236 ? 18.63600  24.02800  12.60400  1.000 74.69334  ? 236 LYS B HG3  1 
ATOM   8169 H HD2  . LYS B 2 236 ? 19.37100  24.97900  14.68500  1.000 78.78635  ? 236 LYS B HD2  1 
ATOM   8170 H HD3  . LYS B 2 236 ? 20.87100  24.71100  14.23100  1.000 78.78635  ? 236 LYS B HD3  1 
ATOM   8171 H HE2  . LYS B 2 236 ? 20.65200  26.23400  12.51000  1.000 81.07695  ? 236 LYS B HE2  1 
ATOM   8172 H HE3  . LYS B 2 236 ? 19.12100  26.45600  12.87400  1.000 81.07695  ? 236 LYS B HE3  1 
ATOM   8173 H HZ1  . LYS B 2 236 ? 20.38900  28.15900  13.69700  1.000 88.98222  ? 236 LYS B HZ1  1 
ATOM   8174 H HZ2  . LYS B 2 236 ? 19.80000  27.44900  14.81500  1.000 88.98222  ? 236 LYS B HZ2  1 
ATOM   8175 H HZ3  . LYS B 2 236 ? 21.19500  27.24700  14.48300  1.000 88.98222  ? 236 LYS B HZ3  1 
ATOM   8176 N N    . TYR B 2 237 ? 17.61900  19.54800  14.09200  1.000 48.19526  ? 237 TYR B N    1 
ATOM   8177 C CA   . TYR B 2 237 ? 17.36100  18.34800  14.87900  1.000 55.09315  ? 237 TYR B CA   1 
ATOM   8178 C C    . TYR B 2 237 ? 16.97800  17.15500  14.01900  1.000 47.40301  ? 237 TYR B C    1 
ATOM   8179 O O    . TYR B 2 237 ? 16.39500  16.18500  14.53700  1.000 45.76827  ? 237 TYR B O    1 
ATOM   8180 C CB   . TYR B 2 237 ? 16.27200  18.62100  15.91600  1.000 49.45100  ? 237 TYR B CB   1 
ATOM   8181 C CG   . TYR B 2 237 ? 16.73600  19.61000  16.96300  1.000 50.60548  ? 237 TYR B CG   1 
ATOM   8182 C CD1  . TYR B 2 237 ? 16.71300  20.97600  16.72400  1.000 55.25109  ? 237 TYR B CD1  1 
ATOM   8183 C CD2  . TYR B 2 237 ? 17.19000  19.16300  18.19400  1.000 55.09571  ? 237 TYR B CD2  1 
ATOM   8184 C CE1  . TYR B 2 237 ? 17.15400  21.87300  17.69600  1.000 56.91009  ? 237 TYR B CE1  1 
ATOM   8185 C CE2  . TYR B 2 237 ? 17.61300  20.03600  19.16400  1.000 56.40634  ? 237 TYR B CE2  1 
ATOM   8186 C CZ   . TYR B 2 237 ? 17.59800  21.38500  18.91800  1.000 58.33176  ? 237 TYR B CZ   1 
ATOM   8187 O OH   . TYR B 2 237 ? 18.04400  22.23500  19.91200  1.000 60.48350  ? 237 TYR B OH   1 
ATOM   8188 H H    . TYR B 2 237 ? 16.90500  19.92400  13.79600  1.000 57.83512  ? 237 TYR B H    1 
ATOM   8189 H HA   . TYR B 2 237 ? 18.16900  18.11200  15.36100  1.000 66.11258  ? 237 TYR B HA   1 
ATOM   8190 H HB2  . TYR B 2 237 ? 15.49300  18.99200  15.47200  1.000 59.34200  ? 237 TYR B HB2  1 
ATOM   8191 H HB3  . TYR B 2 237 ? 16.04100  17.79200  16.36400  1.000 59.34200  ? 237 TYR B HB3  1 
ATOM   8192 H HD1  . TYR B 2 237 ? 16.41700  21.29500  15.90200  1.000 66.30211  ? 237 TYR B HD1  1 
ATOM   8193 H HD2  . TYR B 2 237 ? 17.20500  18.25000  18.36800  1.000 66.11565  ? 237 TYR B HD2  1 
ATOM   8194 H HE1  . TYR B 2 237 ? 17.14000  22.78800  17.53200  1.000 68.29291  ? 237 TYR B HE1  1 
ATOM   8195 H HE2  . TYR B 2 237 ? 17.91900  19.71400  19.98100  1.000 67.68841  ? 237 TYR B HE2  1 
ATOM   8196 H HH   . TYR B 2 237 ? 18.27700  21.79100  20.58600  1.000 72.58100  ? 237 TYR B HH   1 
ATOM   8197 N N    . ASN B 2 238 ? 17.29100  17.21500  12.71900  1.000 49.68469  ? 238 ASN B N    1 
ATOM   8198 C CA   . ASN B 2 238 ? 16.99100  16.12800  11.79600  1.000 49.61652  ? 238 ASN B CA   1 
ATOM   8199 C C    . ASN B 2 238 ? 15.49300  15.85200  11.73900  1.000 44.51994  ? 238 ASN B C    1 
ATOM   8200 O O    . ASN B 2 238 ? 15.05100  14.71200  11.76100  1.000 41.89895  ? 238 ASN B O    1 
ATOM   8201 C CB   . ASN B 2 238 ? 17.78000  14.87500  12.16100  1.000 49.13286  ? 238 ASN B CB   1 
ATOM   8202 C CG   . ASN B 2 238 ? 19.14500  14.87700  11.50700  1.000 54.86223  ? 238 ASN B CG   1 
ATOM   8203 O OD1  . ASN B 2 238 ? 19.54400  15.88900  10.93800  1.000 53.13787  ? 238 ASN B OD1  1 
ATOM   8204 N ND2  . ASN B 2 238 ? 19.87500  13.77400  11.60400  1.000 59.00556  ? 238 ASN B ND2  1 
ATOM   8205 H H    . ASN B 2 238 ? 17.68300  17.88400  12.34800  1.000 59.62243  ? 238 ASN B H    1 
ATOM   8206 H HA   . ASN B 2 238 ? 17.26300  16.39900  10.90500  1.000 59.54062  ? 238 ASN B HA   1 
ATOM   8207 H HB2  . ASN B 2 238 ? 17.90400  14.83300  13.12200  1.000 58.96023  ? 238 ASN B HB2  1 
ATOM   8208 H HB3  . ASN B 2 238 ? 17.30400  14.08900  11.85100  1.000 58.96023  ? 238 ASN B HB3  1 
ATOM   8209 H HD21 . ASN B 2 238 ? 20.65600  13.74300  11.24600  1.000 70.80748  ? 238 ASN B HD21 1 
ATOM   8210 H HD22 . ASN B 2 238 ? 19.56300  13.08600  12.01500  1.000 70.80748  ? 238 ASN B HD22 1 
ATOM   8211 N N    . TYR B 2 239 ? 14.71000  16.91500  11.70000  1.000 47.70369  ? 239 TYR B N    1 
ATOM   8212 C CA   . TYR B 2 239 ? 13.28700  16.82800  11.43000  1.000 44.15382  ? 239 TYR B CA   1 
ATOM   8213 C C    . TYR B 2 239 ? 13.05300  17.14500  9.96200   1.000 43.74660  ? 239 TYR B C    1 
ATOM   8214 O O    . TYR B 2 239 ? 13.73900  17.99600  9.39100   1.000 41.86276  ? 239 TYR B O    1 
ATOM   8215 C CB   . TYR B 2 239 ? 12.51700  17.79600  12.31200  1.000 43.84940  ? 239 TYR B CB   1 
ATOM   8216 C CG   . TYR B 2 239 ? 12.10100  17.14400  13.59600  1.000 46.06555  ? 239 TYR B CG   1 
ATOM   8217 C CD1  . TYR B 2 239 ? 13.03300  16.56100  14.44700  1.000 44.67022  ? 239 TYR B CD1  1 
ATOM   8218 C CD2  . TYR B 2 239 ? 10.75800  17.05000  13.93000  1.000 45.80982  ? 239 TYR B CD2  1 
ATOM   8219 C CE1  . TYR B 2 239 ? 12.63700  15.94900  15.61000  1.000 48.33434  ? 239 TYR B CE1  1 
ATOM   8220 C CE2  . TYR B 2 239 ? 10.36000  16.44600  15.08300  1.000 42.44240  ? 239 TYR B CE2  1 
ATOM   8221 C CZ   . TYR B 2 239 ? 11.29300  15.90400  15.92500  1.000 46.16449  ? 239 TYR B CZ   1 
ATOM   8222 O OH   . TYR B 2 239 ? 10.84900  15.29800  17.07200  1.000 45.46005  ? 239 TYR B OH   1 
ATOM   8223 H H    . TYR B 2 239 ? 14.98700  17.71900  11.83000  1.000 57.24523  ? 239 TYR B H    1 
ATOM   8224 H HA   . TYR B 2 239 ? 12.97100  15.92800  11.60800  1.000 52.98538  ? 239 TYR B HA   1 
ATOM   8225 H HB2  . TYR B 2 239 ? 13.08200  18.55400  12.52500  1.000 52.62008  ? 239 TYR B HB2  1 
ATOM   8226 H HB3  . TYR B 2 239 ? 11.71900  18.09100  11.84600  1.000 52.62008  ? 239 TYR B HB3  1 
ATOM   8227 H HD1  . TYR B 2 239 ? 13.93800  16.60500  14.23600  1.000 53.60507  ? 239 TYR B HD1  1 
ATOM   8228 H HD2  . TYR B 2 239 ? 10.12000  17.42700  13.36800  1.000 54.97258  ? 239 TYR B HD2  1 
ATOM   8229 H HE1  . TYR B 2 239 ? 13.26700  15.57600  16.18300  1.000 58.00201  ? 239 TYR B HE1  1 
ATOM   8230 H HE2  . TYR B 2 239 ? 9.45700   16.40600  15.30100  1.000 50.93169  ? 239 TYR B HE2  1 
ATOM   8231 H HH   . TYR B 2 239 ? 10.01200  15.35300  17.12100  1.000 54.55286  ? 239 TYR B HH   1 
ATOM   8232 N N    . GLU B 2 240 ? 12.09300  16.45700  9.35100   1.000 41.25149  ? 240 GLU B N    1 
ATOM   8233 C CA   . GLU B 2 240 ? 11.74500  16.76200  7.97100   1.000 41.39933  ? 240 GLU B CA   1 
ATOM   8234 C C    . GLU B 2 240 ? 11.24700  18.19900  7.88700   1.000 47.92790  ? 240 GLU B C    1 
ATOM   8235 O O    . GLU B 2 240 ? 10.66700  18.72200  8.85200   1.000 39.67557  ? 240 GLU B O    1 
ATOM   8236 C CB   . GLU B 2 240 ? 10.66400  15.80700  7.45400   1.000 38.81090  ? 240 GLU B CB   1 
ATOM   8237 C CG   . GLU B 2 240 ? 11.21400  14.44100  7.18600   1.000 42.27718  ? 240 GLU B CG   1 
ATOM   8238 C CD   . GLU B 2 240 ? 12.19900  14.42800  6.02100   1.000 47.23314  ? 240 GLU B CD   1 
ATOM   8239 O OE1  . GLU B 2 240 ? 11.74400  14.65000  4.88800   1.000 49.76744  ? 240 GLU B OE1  1 
ATOM   8240 O OE2  . GLU B 2 240 ? 13.41400  14.21400  6.23100   1.000 47.94536  ? 240 GLU B OE2  1 
ATOM   8241 H H    . GLU B 2 240 ? 11.63700  15.82100  9.70700   1.000 49.50259  ? 240 GLU B H    1 
ATOM   8242 H HA   . GLU B 2 240 ? 12.53800  16.66300  7.42500   1.000 49.68000  ? 240 GLU B HA   1 
ATOM   8243 H HB2  . GLU B 2 240 ? 9.96400   15.72700  8.12000   1.000 46.57388  ? 240 GLU B HB2  1 
ATOM   8244 H HB3  . GLU B 2 240 ? 10.30000  16.15500  6.62500   1.000 46.57388  ? 240 GLU B HB3  1 
ATOM   8245 H HG2  . GLU B 2 240 ? 11.67900  14.12600  7.97700   1.000 50.73341  ? 240 GLU B HG2  1 
ATOM   8246 H HG3  . GLU B 2 240 ? 10.48300  13.84200  6.96900   1.000 50.73341  ? 240 GLU B HG3  1 
ATOM   8247 N N    . PRO B 2 241 ? 11.46000  18.86500  6.75300   1.000 49.34255  ? 241 PRO B N    1 
ATOM   8248 C CA   . PRO B 2 241 ? 10.91400  20.21100  6.60200   1.000 48.31231  ? 241 PRO B CA   1 
ATOM   8249 C C    . PRO B 2 241 ? 9.39800   20.15600  6.66300   1.000 45.68057  ? 241 PRO B C    1 
ATOM   8250 O O    . PRO B 2 241 ? 8.77100   19.16000  6.29800   1.000 46.70251  ? 241 PRO B O    1 
ATOM   8251 C CB   . PRO B 2 241 ? 11.41100  20.64600  5.21500   1.000 52.92014  ? 241 PRO B CB   1 
ATOM   8252 C CG   . PRO B 2 241 ? 12.59200  19.71600  4.90900   1.000 53.27523  ? 241 PRO B CG   1 
ATOM   8253 C CD   . PRO B 2 241 ? 12.15700  18.41400  5.52700   1.000 45.03465  ? 241 PRO B CD   1 
ATOM   8254 H HA   . PRO B 2 241 ? 11.25800  20.80800  7.28500   1.000 57.97558  ? 241 PRO B HA   1 
ATOM   8255 H HB2  . PRO B 2 241 ? 10.70300  20.52900  4.56200   1.000 63.50497  ? 241 PRO B HB2  1 
ATOM   8256 H HB3  . PRO B 2 241 ? 11.70100  21.57100  5.24600   1.000 63.50497  ? 241 PRO B HB3  1 
ATOM   8257 H HG2  . PRO B 2 241 ? 12.70700  19.62700  3.95000   1.000 63.93108  ? 241 PRO B HG2  1 
ATOM   8258 H HG3  . PRO B 2 241 ? 13.39900  20.05100  5.33000   1.000 63.93108  ? 241 PRO B HG3  1 
ATOM   8259 H HD2  . PRO B 2 241 ? 11.54500  17.94500  4.93900   1.000 54.04238  ? 241 PRO B HD2  1 
ATOM   8260 H HD3  . PRO B 2 241 ? 12.93300  17.87600  5.74200   1.000 54.04238  ? 241 PRO B HD3  1 
ATOM   8261 N N    . LEU B 2 242 ? 8.81300   21.20400  7.21900   1.000 49.51319  ? 242 LEU B N    1 
ATOM   8262 C CA   . LEU B 2 242 ? 7.37000   21.36200  7.22000   1.000 46.74939  ? 242 LEU B CA   1 
ATOM   8263 C C    . LEU B 2 242 ? 7.04300   22.30100  6.06700   1.000 49.49075  ? 242 LEU B C    1 
ATOM   8264 O O    . LEU B 2 242 ? 7.58700   23.40700  5.99100   1.000 47.56627  ? 242 LEU B O    1 
ATOM   8265 C CB   . LEU B 2 242 ? 6.88000   21.92700  8.55500   1.000 48.42871  ? 242 LEU B CB   1 
ATOM   8266 C CG   . LEU B 2 242 ? 5.39300   21.81900  8.88600   1.000 47.96925  ? 242 LEU B CG   1 
ATOM   8267 C CD1  . LEU B 2 242 ? 5.05500   20.36500  9.16300   1.000 41.82562  ? 242 LEU B CD1  1 
ATOM   8268 C CD2  . LEU B 2 242 ? 5.06800   22.71100  10.10700  1.000 49.41921  ? 242 LEU B CD2  1 
ATOM   8269 H H    . LEU B 2 242 ? 9.23500   21.84500  7.60700   1.000 59.41662  ? 242 LEU B H    1 
ATOM   8270 H HA   . LEU B 2 242 ? 6.94000   20.50800  7.06200   1.000 56.10007  ? 242 LEU B HA   1 
ATOM   8271 H HB2  . LEU B 2 242 ? 7.36000   21.47100  9.26400   1.000 58.11525  ? 242 LEU B HB2  1 
ATOM   8272 H HB3  . LEU B 2 242 ? 7.10500   22.87000  8.57800   1.000 58.11525  ? 242 LEU B HB3  1 
ATOM   8273 H HG   . LEU B 2 242 ? 4.86700   22.12200  8.13000   1.000 57.56390  ? 242 LEU B HG   1 
ATOM   8274 H HD11 . LEU B 2 242 ? 4.12600   20.30400  9.43500   1.000 50.19154  ? 242 LEU B HD11 1 
ATOM   8275 H HD12 . LEU B 2 242 ? 5.19700   19.84700  8.35500   1.000 50.19154  ? 242 LEU B HD12 1 
ATOM   8276 H HD13 . LEU B 2 242 ? 5.62900   20.03700  9.87300   1.000 50.19154  ? 242 LEU B HD13 1 
ATOM   8277 H HD21 . LEU B 2 242 ? 4.12300   22.63100  10.31300  1.000 59.30385  ? 242 LEU B HD21 1 
ATOM   8278 H HD22 . LEU B 2 242 ? 5.59800   22.41500  10.86400  1.000 59.30385  ? 242 LEU B HD22 1 
ATOM   8279 H HD23 . LEU B 2 242 ? 5.28400   23.63200  9.89100   1.000 59.30385  ? 242 LEU B HD23 1 
ATOM   8280 N N    . THR B 2 243 ? 6.19500   21.84400  5.15700   1.000 51.93684  ? 243 THR B N    1 
ATOM   8281 C CA   . THR B 2 243 ? 5.82000   22.62000  3.98700   1.000 53.98544  ? 243 THR B CA   1 
ATOM   8282 C C    . THR B 2 243 ? 4.46300   23.24900  4.25000   1.000 50.98941  ? 243 THR B C    1 
ATOM   8283 O O    . THR B 2 243 ? 3.76100   22.89400  5.19500   1.000 48.98429  ? 243 THR B O    1 
ATOM   8284 C CB   . THR B 2 243 ? 5.75100   21.73500  2.73900   1.000 52.83758  ? 243 THR B CB   1 
ATOM   8285 O OG1  . THR B 2 243 ? 4.64200   20.84900  2.86300   1.000 58.28167  ? 243 THR B OG1  1 
ATOM   8286 C CG2  . THR B 2 243 ? 7.00200   20.88500  2.61200   1.000 54.44321  ? 243 THR B CG2  1 
ATOM   8287 H H    . THR B 2 243 ? 5.81600   21.07400  5.19600   1.000 62.32501  ? 243 THR B H    1 
ATOM   8288 H HA   . THR B 2 243 ? 6.46800   23.32500  3.83500   1.000 64.78333  ? 243 THR B HA   1 
ATOM   8289 H HB   . THR B 2 243 ? 5.65500   22.28300  1.94400   1.000 63.40590  ? 243 THR B HB   1 
ATOM   8290 H HG1  . THR B 2 243 ? 4.73500   20.36600  3.54400   1.000 69.93881  ? 243 THR B HG1  1 
ATOM   8291 H HG21 . THR B 2 243 ? 7.00600   20.42800  1.75600   1.000 65.33266  ? 243 THR B HG21 1 
ATOM   8292 H HG22 . THR B 2 243 ? 7.79100   21.44600  2.67400   1.000 65.33266  ? 243 THR B HG22 1 
ATOM   8293 H HG23 . THR B 2 243 ? 7.02900   20.22400  3.32200   1.000 65.33266  ? 243 THR B HG23 1 
ATOM   8294 N N    . GLN B 2 244 ? 4.08300   24.18000  3.38300   1.000 53.49539  ? 244 GLN B N    1 
ATOM   8295 C CA   . GLN B 2 244 ? 2.75200   24.75000  3.50400   1.000 48.64599  ? 244 GLN B CA   1 
ATOM   8296 C C    . GLN B 2 244 ? 1.68900   23.70200  3.24100   1.000 51.91760  ? 244 GLN B C    1 
ATOM   8297 O O    . GLN B 2 244 ? 0.59000   23.78300  3.80300   1.000 55.94638  ? 244 GLN B O    1 
ATOM   8298 C CB   . GLN B 2 244 ? 2.58500   25.92900  2.54200   1.000 60.65163  ? 244 GLN B CB   1 
ATOM   8299 C CG   . GLN B 2 244 ? 1.22800   26.61300  2.66900   1.000 56.96847  ? 244 GLN B CG   1 
ATOM   8300 C CD   . GLN B 2 244 ? 1.05600   27.29100  4.01900   1.000 60.64799  ? 244 GLN B CD   1 
ATOM   8301 O OE1  . GLN B 2 244 ? 2.02400   27.78700  4.60200   1.000 59.47106  ? 244 GLN B OE1  1 
ATOM   8302 N NE2  . GLN B 2 244 ? -0.17800  27.31200  4.52500   1.000 60.88763  ? 244 GLN B NE2  1 
ATOM   8303 H H    . GLN B 2 244 ? 4.56000   24.48900  2.73700   1.000 64.19527  ? 244 GLN B H    1 
ATOM   8304 H HA   . GLN B 2 244 ? 2.63200   25.07900  4.40800   1.000 58.37599  ? 244 GLN B HA   1 
ATOM   8305 H HB2  . GLN B 2 244 ? 3.27100   26.58800  2.72900   1.000 72.78275  ? 244 GLN B HB2  1 
ATOM   8306 H HB3  . GLN B 2 244 ? 2.67400   25.60800  1.63100   1.000 72.78275  ? 244 GLN B HB3  1 
ATOM   8307 H HG2  . GLN B 2 244 ? 1.15400   27.29400  1.98200   1.000 68.36297  ? 244 GLN B HG2  1 
ATOM   8308 H HG3  . GLN B 2 244 ? 0.52000   25.95900  2.56400   1.000 68.36297  ? 244 GLN B HG3  1 
ATOM   8309 H HE21 . GLN B 2 244 ? -0.82800  26.95500  4.08900   1.000 73.06596  ? 244 GLN B HE21 1 
ATOM   8310 H HE22 . GLN B 2 244 ? -0.32400  27.68400  5.28600   1.000 73.06596  ? 244 GLN B HE22 1 
ATOM   8311 N N    . ASP B 2 245 ? 1.99100   22.71000  2.40000   1.000 49.16025  ? 245 ASP B N    1 
ATOM   8312 C CA   . ASP B 2 245 ? 1.06800   21.59800  2.21100   1.000 54.47076  ? 245 ASP B CA   1 
ATOM   8313 C C    . ASP B 2 245 ? 0.74800   20.92400  3.54600   1.000 54.91605  ? 245 ASP B C    1 
ATOM   8314 O O    . ASP B 2 245 ? -0.41900  20.64700  3.85800   1.000 51.79580  ? 245 ASP B O    1 
ATOM   8315 C CB   . ASP B 2 245 ? 1.66900   20.60300  1.22100   1.000 52.06333  ? 245 ASP B CB   1 
ATOM   8316 C CG   . ASP B 2 245 ? 0.72600   19.47000  0.89100   1.000 66.71451  ? 245 ASP B CG   1 
ATOM   8317 O OD1  . ASP B 2 245 ? -0.45300  19.74600  0.54900   1.000 67.43342  ? 245 ASP B OD1  1 
ATOM   8318 O OD2  . ASP B 2 245 ? 1.17300   18.29500  0.95600   1.000 72.63424  ? 245 ASP B OD2  1 
ATOM   8319 H H    . ASP B 2 245 ? 2.71300   22.66000  1.93500   1.000 58.99310  ? 245 ASP B H    1 
ATOM   8320 H HA   . ASP B 2 245 ? 0.23900   21.93300  1.83600   1.000 65.36572  ? 245 ASP B HA   1 
ATOM   8321 H HB2  . ASP B 2 245 ? 1.88200   21.06700  0.39600   1.000 62.47679  ? 245 ASP B HB2  1 
ATOM   8322 H HB3  . ASP B 2 245 ? 2.47400   20.22200  1.60500   1.000 62.47679  ? 245 ASP B HB3  1 
ATOM   8323 N N    . HIS B 2 246 ? 1.77200   20.67300  4.34100   1.000 50.41056  ? 246 HIS B N    1 
ATOM   8324 C CA   . HIS B 2 246 ? 1.57400   20.03900  5.66800   1.000 48.19165  ? 246 HIS B CA   1 
ATOM   8325 C C    . HIS B 2 246 ? 0.67100   20.92300  6.52800   1.000 50.32933  ? 246 HIS B C    1 
ATOM   8326 O O    . HIS B 2 246 ? -0.25100  20.39600  7.14400   1.000 49.62844  ? 246 HIS B O    1 
ATOM   8327 C CB   . HIS B 2 246 ? 2.93400   19.78600  6.31000   1.000 49.13388  ? 246 HIS B CB   1 
ATOM   8328 C CG   . HIS B 2 246 ? 3.78600   18.80200  5.59100   1.000 48.29682  ? 246 HIS B CG   1 
ATOM   8329 N ND1  . HIS B 2 246 ? 5.16000   18.84800  5.64800   1.000 48.10072  ? 246 HIS B ND1  1 
ATOM   8330 C CD2  . HIS B 2 246 ? 3.47100   17.73400  4.83200   1.000 43.85582  ? 246 HIS B CD2  1 
ATOM   8331 C CE1  . HIS B 2 246 ? 5.65900   17.86000  4.94100   1.000 47.80245  ? 246 HIS B CE1  1 
ATOM   8332 N NE2  . HIS B 2 246 ? 4.64400   17.16100  4.43200   1.000 52.95516  ? 246 HIS B NE2  1 
ATOM   8333 H H    . HIS B 2 246 ? 2.59200   20.85200  4.15300   1.000 60.49347  ? 246 HIS B H    1 
ATOM   8334 H HA   . HIS B 2 246 ? 1.13200   19.18400  5.54900   1.000 57.83079  ? 246 HIS B HA   1 
ATOM   8335 H HB2  . HIS B 2 246 ? 3.42000   20.62500  6.34600   1.000 58.96146  ? 246 HIS B HB2  1 
ATOM   8336 H HB3  . HIS B 2 246 ? 2.79400   19.45100  7.21000   1.000 58.96146  ? 246 HIS B HB3  1 
ATOM   8337 H HD2  . HIS B 2 246 ? 2.61400   17.44500  4.61600   1.000 52.62779  ? 246 HIS B HD2  1 
ATOM   8338 H HE1  . HIS B 2 246 ? 6.56300   17.67800  4.81900   1.000 57.36374  ? 246 HIS B HE1  1 
ATOM   8339 H HE2  . HIS B 2 246 ? 4.71600   16.46600  3.93100   1.000 63.54700  ? 246 HIS B HE2  1 
ATOM   8340 N N    . VAL B 2 247 ? 0.92700   22.23200  6.53100   1.000 50.91594  ? 247 VAL B N    1 
ATOM   8341 C CA   . VAL B 2 247 ? 0.10400   23.15100  7.30800   1.000 47.94405  ? 247 VAL B CA   1 
ATOM   8342 C C    . VAL B 2 247 ? -1.35400  23.02100  6.89500   1.000 55.68912  ? 247 VAL B C    1 
ATOM   8343 O O    . VAL B 2 247 ? -2.25500  22.94000  7.74600   1.000 51.57668  ? 247 VAL B O    1 
ATOM   8344 C CB   . VAL B 2 247 ? 0.63000   24.59300  7.15000   1.000 51.60944  ? 247 VAL B CB   1 
ATOM   8345 C CG1  . VAL B 2 247 ? -0.34800  25.62300  7.74200   1.000 51.26626  ? 247 VAL B CG1  1 
ATOM   8346 C CG2  . VAL B 2 247 ? 1.98500   24.71200  7.82000   1.000 48.12366  ? 247 VAL B CG2  1 
ATOM   8347 H H    . VAL B 2 247 ? 1.56600   22.60800  6.09500   1.000 61.09993  ? 247 VAL B H    1 
ATOM   8348 H HA   . VAL B 2 247 ? 0.16900   22.91300  8.24600   1.000 57.53367  ? 247 VAL B HA   1 
ATOM   8349 H HB   . VAL B 2 247 ? 0.74100   24.78900  6.20700   1.000 61.93213  ? 247 VAL B HB   1 
ATOM   8350 H HG11 . VAL B 2 247 ? 0.10400   26.47800  7.81800   1.000 61.52032  ? 247 VAL B HG11 1 
ATOM   8351 H HG12 . VAL B 2 247 ? -1.11600  25.70700  7.15500   1.000 61.52032  ? 247 VAL B HG12 1 
ATOM   8352 H HG13 . VAL B 2 247 ? -0.63100  25.32100  8.61900   1.000 61.52032  ? 247 VAL B HG13 1 
ATOM   8353 H HG21 . VAL B 2 247 ? 2.30400   25.62400  7.72700   1.000 57.74919  ? 247 VAL B HG21 1 
ATOM   8354 H HG22 . VAL B 2 247 ? 1.89300   24.48700  8.75900   1.000 57.74919  ? 247 VAL B HG22 1 
ATOM   8355 H HG23 . VAL B 2 247 ? 2.60400   24.10000  7.39200   1.000 57.74919  ? 247 VAL B HG23 1 
ATOM   8356 N N    . ASP B 2 248 ? -1.60400  22.99100  5.57700   1.000 54.69167  ? 248 ASP B N    1 
ATOM   8357 C CA   . ASP B 2 248 ? -2.96100  22.85100  5.06300   1.000 54.77977  ? 248 ASP B CA   1 
ATOM   8358 C C    . ASP B 2 248 ? -3.60700  21.55700  5.54600   1.000 52.85193  ? 248 ASP B C    1 
ATOM   8359 O O    . ASP B 2 248 ? -4.76800  21.54600  5.97600   1.000 54.64873  ? 248 ASP B O    1 
ATOM   8360 C CB   . ASP B 2 248 ? -2.94600  22.89100  3.52900   1.000 55.96006  ? 248 ASP B CB   1 
ATOM   8361 C CG   . ASP B 2 248 ? -2.50700  24.24300  2.96700   1.000 59.34868  ? 248 ASP B CG   1 
ATOM   8362 O OD1  . ASP B 2 248 ? -2.60600  25.26800  3.67400   1.000 62.92690  ? 248 ASP B OD1  1 
ATOM   8363 O OD2  . ASP B 2 248 ? -2.06700  24.27800  1.79500   1.000 78.97772  ? 248 ASP B OD2  1 
ATOM   8364 H H    . ASP B 2 248 ? -1.00100  23.05000  4.96600   1.000 65.63080  ? 248 ASP B H    1 
ATOM   8365 H HA   . ASP B 2 248 ? -3.49900  23.59300  5.37900   1.000 65.73652  ? 248 ASP B HA   1 
ATOM   8366 H HB2  . ASP B 2 248 ? -2.32900  22.21700  3.20300   1.000 67.15287  ? 248 ASP B HB2  1 
ATOM   8367 H HB3  . ASP B 2 248 ? -3.84000  22.70700  3.20100   1.000 67.15287  ? 248 ASP B HB3  1 
ATOM   8368 N N    . ILE B 2 249 ? -2.87000  20.44400  5.46900   1.000 51.93974  ? 249 ILE B N    1 
ATOM   8369 C CA   . ILE B 2 249 ? -3.43100  19.14600  5.84600   1.000 53.14056  ? 249 ILE B CA   1 
ATOM   8370 C C    . ILE B 2 249 ? -3.80400  19.11700  7.32200   1.000 50.98781  ? 249 ILE B C    1 
ATOM   8371 O O    . ILE B 2 249 ? -4.75900  18.43900  7.71800   1.000 52.04667  ? 249 ILE B O    1 
ATOM   8372 C CB   . ILE B 2 249 ? -2.43300  18.02200  5.50800   1.000 50.90579  ? 249 ILE B CB   1 
ATOM   8373 C CG1  . ILE B 2 249 ? -2.20200  17.95500  3.99900   1.000 58.57372  ? 249 ILE B CG1  1 
ATOM   8374 C CG2  . ILE B 2 249 ? -2.97200  16.72900  5.94400   1.000 55.70073  ? 249 ILE B CG2  1 
ATOM   8375 C CD1  . ILE B 2 249 ? -1.00800  17.12500  3.61000   1.000 66.25471  ? 249 ILE B CD1  1 
ATOM   8376 H H    . ILE B 2 249 ? -2.05200  20.41500  5.20500   1.000 62.32849  ? 249 ILE B H    1 
ATOM   8377 H HA   . ILE B 2 249 ? -4.23900  18.99200  5.33200   1.000 63.76948  ? 249 ILE B HA   1 
ATOM   8378 H HB   . ILE B 2 249 ? -1.59000  18.19000  5.95800   1.000 61.08775  ? 249 ILE B HB   1 
ATOM   8379 H HG12 . ILE B 2 249 ? -2.98400  17.56300  3.58100   1.000 70.28927  ? 249 ILE B HG12 1 
ATOM   8380 H HG13 . ILE B 2 249 ? -2.06300  18.85200  3.65800   1.000 70.28927  ? 249 ILE B HG13 1 
ATOM   8381 H HG21 . ILE B 2 249 ? -2.46500  16.01300  5.53200   1.000 66.84168  ? 249 ILE B HG21 1 
ATOM   8382 H HG22 . ILE B 2 249 ? -2.90000  16.66300  6.90900   1.000 66.84168  ? 249 ILE B HG22 1 
ATOM   8383 H HG23 . ILE B 2 249 ? -3.90200  16.67000  5.67500   1.000 66.84168  ? 249 ILE B HG23 1 
ATOM   8384 H HD11 . ILE B 2 249 ? -0.77800  17.31700  2.68700   1.000 79.50646  ? 249 ILE B HD11 1 
ATOM   8385 H HD12 . ILE B 2 249 ? -0.26400  17.35200  4.19000   1.000 79.50646  ? 249 ILE B HD12 1 
ATOM   8386 H HD13 . ILE B 2 249 ? -1.22800  16.18500  3.70700   1.000 79.50646  ? 249 ILE B HD13 1 
ATOM   8387 N N    . LEU B 2 250 ? -3.06000  19.82500  8.15800   1.000 51.32968  ? 250 LEU B N    1 
ATOM   8388 C CA   . LEU B 2 250 ? -3.39000  19.88900  9.57900   1.000 51.23175  ? 250 LEU B CA   1 
ATOM   8389 C C    . LEU B 2 250 ? -4.52300  20.86100  9.87200   1.000 53.65279  ? 250 LEU B C    1 
ATOM   8390 O O    . LEU B 2 250 ? -4.91100  20.99700  11.03400  1.000 56.98716  ? 250 LEU B O    1 
ATOM   8391 C CB   . LEU B 2 250 ? -2.15000  20.29300  10.39100  1.000 44.70416  ? 250 LEU B CB   1 
ATOM   8392 C CG   . LEU B 2 250 ? -1.04300  19.25300  10.43500  1.000 44.46451  ? 250 LEU B CG   1 
ATOM   8393 C CD1  . LEU B 2 250 ? 0.30500   19.89200  10.72400  1.000 37.91382  ? 250 LEU B CD1  1 
ATOM   8394 C CD2  . LEU B 2 250 ? -1.40300  18.18600  11.47900  1.000 38.33676  ? 250 LEU B CD2  1 
ATOM   8395 H H    . LEU B 2 250 ? -2.36300  20.27600  7.93300   1.000 61.59641  ? 250 LEU B H    1 
ATOM   8396 H HA   . LEU B 2 250 ? -3.66800  19.00900  9.87700   1.000 61.47890  ? 250 LEU B HA   1 
ATOM   8397 H HB2  . LEU B 2 250 ? -1.77700  21.09900  10.00200  1.000 53.64580  ? 250 LEU B HB2  1 
ATOM   8398 H HB3  . LEU B 2 250 ? -2.42300  20.46900  11.30500  1.000 53.64580  ? 250 LEU B HB3  1 
ATOM   8399 H HG   . LEU B 2 250 ? -0.98700  18.81700  9.57000   1.000 53.35821  ? 250 LEU B HG   1 
ATOM   8400 H HD11 . LEU B 2 250 ? 0.96900   19.19300  10.83000  1.000 45.49738  ? 250 LEU B HD11 1 
ATOM   8401 H HD12 . LEU B 2 250 ? 0.54600   20.46900  9.98200   1.000 45.49738  ? 250 LEU B HD12 1 
ATOM   8402 H HD13 . LEU B 2 250 ? 0.23900   20.41200  11.54000  1.000 45.49738  ? 250 LEU B HD13 1 
ATOM   8403 H HD21 . LEU B 2 250 ? -0.69700  17.52200  11.50700  1.000 46.00492  ? 250 LEU B HD21 1 
ATOM   8404 H HD22 . LEU B 2 250 ? -1.49300  18.61100  12.34600  1.000 46.00492  ? 250 LEU B HD22 1 
ATOM   8405 H HD23 . LEU B 2 250 ? -2.24100  17.76700  11.22700  1.000 46.00492  ? 250 LEU B HD23 1 
ATOM   8406 N N    . GLY B 2 251 ? -5.04800  21.54000  8.85600   1.000 55.29766  ? 251 GLY B N    1 
ATOM   8407 C CA   . GLY B 2 251 ? -6.04800  22.56500  9.03700   1.000 60.61817  ? 251 GLY B CA   1 
ATOM   8408 C C    . GLY B 2 251 ? -7.22100  22.17400  9.91800   1.000 58.80411  ? 251 GLY B C    1 
ATOM   8409 O O    . GLY B 2 251 ? -7.61000  22.91500  10.83300  1.000 59.75145  ? 251 GLY B O    1 
ATOM   8410 H H    . GLY B 2 251 ? -4.83100  21.41700  8.03300   1.000 66.35800  ? 251 GLY B H    1 
ATOM   8411 H HA2  . GLY B 2 251 ? -5.62800  23.34700  9.42900   1.000 72.74260  ? 251 GLY B HA2  1 
ATOM   8412 H HA3  . GLY B 2 251 ? -6.39900  22.81800  8.16900   1.000 72.74260  ? 251 GLY B HA3  1 
ATOM   8413 N N    . PRO B 2 252 ? -7.83100  21.01600  9.63500   1.000 53.69324  ? 252 PRO B N    1 
ATOM   8414 C CA   . PRO B 2 252 ? -8.93200  20.54400  10.48700  1.000 56.90303  ? 252 PRO B CA   1 
ATOM   8415 C C    . PRO B 2 252 ? -8.56800  20.47100  11.96300  1.000 61.05056  ? 252 PRO B C    1 
ATOM   8416 O O    . PRO B 2 252 ? -9.25300  21.07300  12.80300  1.000 65.28310  ? 252 PRO B O    1 
ATOM   8417 C CB   . PRO B 2 252 ? -9.22800  19.15000  9.91200   1.000 54.86179  ? 252 PRO B CB   1 
ATOM   8418 C CG   . PRO B 2 252 ? -8.79600  19.21300  8.53600   1.000 54.87254  ? 252 PRO B CG   1 
ATOM   8419 C CD   . PRO B 2 252 ? -7.60700  20.11800  8.49200   1.000 53.58331  ? 252 PRO B CD   1 
ATOM   8420 H HA   . PRO B 2 252 ? -9.71200  21.11000  10.37500  1.000 68.28444  ? 252 PRO B HA   1 
ATOM   8421 H HB2  . PRO B 2 252 ? -8.72400  18.47900  10.39900  1.000 65.83494  ? 252 PRO B HB2  1 
ATOM   8422 H HB3  . PRO B 2 252 ? -10.18000 18.97000  9.96500   1.000 65.83494  ? 252 PRO B HB3  1 
ATOM   8423 H HG2  . PRO B 2 252 ? -8.55400  18.32300  8.23400   1.000 65.84785  ? 252 PRO B HG2  1 
ATOM   8424 H HG3  . PRO B 2 252 ? -9.51300  19.57100  7.99000   1.000 65.84785  ? 252 PRO B HG3  1 
ATOM   8425 H HD2  . PRO B 2 252 ? -6.79100  19.60900  8.61500   1.000 64.30077  ? 252 PRO B HD2  1 
ATOM   8426 H HD3  . PRO B 2 252 ? -7.59400  20.62100  7.66300   1.000 64.30077  ? 252 PRO B HD3  1 
ATOM   8427 N N    . LEU B 2 253 ? -7.48700  19.75500  12.29500  1.000 62.07613  ? 253 LEU B N    1 
ATOM   8428 C CA   . LEU B 2 253 ? -7.06600  19.61500  13.68700  1.000 56.79203  ? 253 LEU B CA   1 
ATOM   8429 C C    . LEU B 2 253 ? -6.74600  20.97000  14.30900  1.000 59.42871  ? 253 LEU B C    1 
ATOM   8430 O O    . LEU B 2 253 ? -7.02900  21.20200  15.49200  1.000 61.91735  ? 253 LEU B O    1 
ATOM   8431 C CB   . LEU B 2 253 ? -5.84200  18.69200  13.76000  1.000 51.18705  ? 253 LEU B CB   1 
ATOM   8432 C CG   . LEU B 2 253 ? -6.03700  17.22500  13.34900  1.000 46.46964  ? 253 LEU B CG   1 
ATOM   8433 C CD1  . LEU B 2 253 ? -4.72400  16.41800  13.30300  1.000 39.39457  ? 253 LEU B CD1  1 
ATOM   8434 C CD2  . LEU B 2 253 ? -7.04000  16.52700  14.25500  1.000 51.54566  ? 253 LEU B CD2  1 
ATOM   8435 H H    . LEU B 2 253 ? -6.98400  19.34300  11.73200  1.000 74.49216  ? 253 LEU B H    1 
ATOM   8436 H HA   . LEU B 2 253 ? -7.78400  19.21100  14.19800  1.000 68.15124  ? 253 LEU B HA   1 
ATOM   8437 H HB2  . LEU B 2 253 ? -5.15100  19.06000  13.18700  1.000 61.42527  ? 253 LEU B HB2  1 
ATOM   8438 H HB3  . LEU B 2 253 ? -5.52800  18.68800  14.67700  1.000 61.42527  ? 253 LEU B HB3  1 
ATOM   8439 H HG   . LEU B 2 253 ? -6.40800  17.21300  12.45300  1.000 55.76437  ? 253 LEU B HG   1 
ATOM   8440 H HD11 . LEU B 2 253 ? -4.92200  15.51000  13.02600  1.000 47.27429  ? 253 LEU B HD11 1 
ATOM   8441 H HD12 . LEU B 2 253 ? -4.12000  16.83400  12.66800  1.000 47.27429  ? 253 LEU B HD12 1 
ATOM   8442 H HD13 . LEU B 2 253 ? -4.32400  16.41600  14.18700  1.000 47.27429  ? 253 LEU B HD13 1 
ATOM   8443 H HD21 . LEU B 2 253 ? -7.07400  15.58600  14.02100  1.000 61.85559  ? 253 LEU B HD21 1 
ATOM   8444 H HD22 . LEU B 2 253 ? -6.75600  16.62900  15.17700  1.000 61.85559  ? 253 LEU B HD22 1 
ATOM   8445 H HD23 . LEU B 2 253 ? -7.91300  16.93100  14.13100  1.000 61.85559  ? 253 LEU B HD23 1 
ATOM   8446 N N    . SER B 2 254 ? -6.12500  21.87000  13.52900  1.000 56.07613  ? 254 SER B N    1 
ATOM   8447 C CA   . SER B 2 254 ? -5.84800  23.21900  14.01400  1.000 60.86845  ? 254 SER B CA   1 
ATOM   8448 C C    . SER B 2 254 ? -7.13800  23.92300  14.38300  1.000 63.87246  ? 254 SER B C    1 
ATOM   8449 O O    . SER B 2 254 ? -7.20900  24.62600  15.40400  1.000 66.13233  ? 254 SER B O    1 
ATOM   8450 C CB   . SER B 2 254 ? -5.08900  24.02800  12.95800  1.000 59.68908  ? 254 SER B CB   1 
ATOM   8451 O OG   . SER B 2 254 ? -4.89800  25.38000  13.36400  1.000 65.68532  ? 254 SER B OG   1 
ATOM   8452 H H    . SER B 2 254 ? -5.85900  21.72000  12.72500  1.000 67.29216  ? 254 SER B H    1 
ATOM   8453 H HA   . SER B 2 254 ? -5.29600  23.16500  14.80900  1.000 73.04294  ? 254 SER B HA   1 
ATOM   8454 H HB2  . SER B 2 254 ? -4.22200  23.61800  12.81700  1.000 71.62770  ? 254 SER B HB2  1 
ATOM   8455 H HB3  . SER B 2 254 ? -5.59600  24.01800  12.13100  1.000 71.62770  ? 254 SER B HB3  1 
ATOM   8456 H HG   . SER B 2 254 ? -4.62600  25.83600  12.71300  1.000 78.82318  ? 254 SER B HG   1 
ATOM   8457 N N    . ALA B 2 255 ? -8.17400  23.73300  13.56600  1.000 62.78584  ? 255 ALA B N    1 
ATOM   8458 C CA   . ALA B 2 255 ? -9.44900  24.35600  13.87100  1.000 67.21034  ? 255 ALA B CA   1 
ATOM   8459 C C    . ALA B 2 255 ? -10.11600 23.66300  15.04400  1.000 67.60336  ? 255 ALA B C    1 
ATOM   8460 O O    . ALA B 2 255 ? -10.60100 24.32400  15.96900  1.000 69.87156  ? 255 ALA B O    1 
ATOM   8461 C CB   . ALA B 2 255 ? -10.35700 24.32900  12.63900  1.000 64.69194  ? 255 ALA B CB   1 
ATOM   8462 H H    . ALA B 2 255 ? -8.16200  23.26000  12.84800  1.000 75.34381  ? 255 ALA B H    1 
ATOM   8463 H HA   . ALA B 2 255 ? -9.29900  25.28300  14.11400  1.000 80.65321  ? 255 ALA B HA   1 
ATOM   8464 H HB1  . ALA B 2 255 ? -11.20300 24.74900  12.86100  1.000 77.63113  ? 255 ALA B HB1  1 
ATOM   8465 H HB2  . ALA B 2 255 ? -9.92600  24.81500  11.91900  1.000 77.63113  ? 255 ALA B HB2  1 
ATOM   8466 H HB3  . ALA B 2 255 ? -10.50400 23.40700  12.37600  1.000 77.63113  ? 255 ALA B HB3  1 
ATOM   8467 N N    . GLN B 2 256 ? -10.07800 22.33500  15.06200  1.000 67.11860  ? 256 GLN B N    1 
ATOM   8468 C CA   . GLN B 2 256 ? -10.81000 21.56900  16.06100  1.000 70.31581  ? 256 GLN B CA   1 
ATOM   8469 C C    . GLN B 2 256 ? -10.26300 21.77500  17.46800  1.000 69.32271  ? 256 GLN B C    1 
ATOM   8470 O O    . GLN B 2 256 ? -10.99200 21.56800  18.44000  1.000 76.55046  ? 256 GLN B O    1 
ATOM   8471 C CB   . GLN B 2 256 ? -10.80000 20.09500  15.66900  1.000 71.35845  ? 256 GLN B CB   1 
ATOM   8472 C CG   . GLN B 2 256 ? -11.56300 19.16800  16.58900  1.000 75.58692  ? 256 GLN B CG   1 
ATOM   8473 C CD   . GLN B 2 256 ? -11.50900 17.72200  16.09700  1.000 84.27262  ? 256 GLN B CD   1 
ATOM   8474 O OE1  . GLN B 2 256 ? -11.18700 17.45500  14.93100  1.000 82.71608  ? 256 GLN B OE1  1 
ATOM   8475 N NE2  . GLN B 2 256 ? -11.80500 16.77900  16.99000  1.000 85.27167  ? 256 GLN B NE2  1 
ATOM   8476 H H    . GLN B 2 256 ? -9.63400  21.85300  14.50500  1.000 80.54312  ? 256 GLN B H    1 
ATOM   8477 H HA   . GLN B 2 256 ? -11.73400 21.86500  16.06100  1.000 84.37977  ? 256 GLN B HA   1 
ATOM   8478 H HB2  . GLN B 2 256 ? -11.18900 20.01100  14.78400  1.000 85.63094  ? 256 GLN B HB2  1 
ATOM   8479 H HB3  . GLN B 2 256 ? -9.87900  19.79000  15.64800  1.000 85.63094  ? 256 GLN B HB3  1 
ATOM   8480 H HG2  . GLN B 2 256 ? -11.17100 19.20000  17.47600  1.000 90.70510  ? 256 GLN B HG2  1 
ATOM   8481 H HG3  . GLN B 2 256 ? -12.49200 19.44300  16.62200  1.000 90.70510  ? 256 GLN B HG3  1 
ATOM   8482 H HE21 . GLN B 2 256 ? -12.02100 17.00000  17.79300  1.000 102.32680 ? 256 GLN B HE21 1 
ATOM   8483 H HE22 . GLN B 2 256 ? -11.78700 15.95000  16.76200  1.000 102.32680 ? 256 GLN B HE22 1 
ATOM   8484 N N    . THR B 2 257 ? -9.00600  22.18000  17.60200  1.000 69.51970  ? 257 THR B N    1 
ATOM   8485 C CA   . THR B 2 257 ? -8.39300  22.33900  18.91100  1.000 69.20748  ? 257 THR B CA   1 
ATOM   8486 C C    . THR B 2 257 ? -8.14700  23.79400  19.30500  1.000 68.78373  ? 257 THR B C    1 
ATOM   8487 O O    . THR B 2 257 ? -7.86700  24.06100  20.47800  1.000 70.22957  ? 257 THR B O    1 
ATOM   8488 C CB   . THR B 2 257 ? -7.06500  21.57800  18.96200  1.000 58.73414  ? 257 THR B CB   1 
ATOM   8489 O OG1  . THR B 2 257 ? -6.20600  22.08700  17.94000  1.000 61.17966  ? 257 THR B OG1  1 
ATOM   8490 C CG2  . THR B 2 257 ? -7.29100  20.07600  18.75300  1.000 57.80551  ? 257 THR B CG2  1 
ATOM   8491 H H    . THR B 2 257 ? -8.48400  22.37000  16.94500  1.000 83.42444  ? 257 THR B H    1 
ATOM   8492 H HA   . THR B 2 257 ? -8.97600  21.95000  19.58100  1.000 83.04978  ? 257 THR B HA   1 
ATOM   8493 H HB   . THR B 2 257 ? -6.65400  21.70600  19.83000  1.000 70.48177  ? 257 THR B HB   1 
ATOM   8494 H HG1  . THR B 2 257 ? -6.54900  21.95600  17.18400  1.000 73.41640  ? 257 THR B HG1  1 
ATOM   8495 H HG21 . THR B 2 257 ? -6.44800  19.60200  18.82000  1.000 69.36741  ? 257 THR B HG21 1 
ATOM   8496 H HG22 . THR B 2 257 ? -7.89900  19.73600  19.42800  1.000 69.36741  ? 257 THR B HG22 1 
ATOM   8497 H HG23 . THR B 2 257 ? -7.67300  19.91700  17.87600  1.000 69.36741  ? 257 THR B HG23 1 
ATOM   8498 N N    . GLY B 2 258 ? -8.23500  24.73600  18.37200  1.000 67.15751  ? 258 GLY B N    1 
ATOM   8499 C CA   . GLY B 2 258 ? -7.90400  26.10900  18.67600  1.000 64.47869  ? 258 GLY B CA   1 
ATOM   8500 C C    . GLY B 2 258 ? -6.42400  26.38800  18.74000  1.000 73.95033  ? 258 GLY B C    1 
ATOM   8501 O O    . GLY B 2 258 ? -6.02700  27.51900  19.07700  1.000 63.35931  ? 258 GLY B O    1 
ATOM   8502 H H    . GLY B 2 258 ? -8.48300  24.60100  17.56000  1.000 80.58982  ? 258 GLY B H    1 
ATOM   8503 H HA2  . GLY B 2 258 ? -8.29000  26.68500  17.99800  1.000 77.37522  ? 258 GLY B HA2  1 
ATOM   8504 H HA3  . GLY B 2 258 ? -8.29300  26.34700  19.53200  1.000 77.37522  ? 258 GLY B HA3  1 
ATOM   8505 N N    . ILE B 2 259 ? -5.59100  25.40200  18.42500  1.000 63.27784  ? 259 ILE B N    1 
ATOM   8506 C CA   . ILE B 2 259 ? -4.15800  25.60800  18.33800  1.000 58.28344  ? 259 ILE B CA   1 
ATOM   8507 C C    . ILE B 2 259 ? -3.84400  25.67000  16.85300  1.000 67.06316  ? 259 ILE B C    1 
ATOM   8508 O O    . ILE B 2 259 ? -3.88200  24.64700  16.16200  1.000 60.96667  ? 259 ILE B O    1 
ATOM   8509 C CB   . ILE B 2 259 ? -3.36400  24.49000  19.03400  1.000 58.22783  ? 259 ILE B CB   1 
ATOM   8510 C CG1  . ILE B 2 259 ? -3.64700  24.44000  20.53600  1.000 61.74424  ? 259 ILE B CG1  1 
ATOM   8511 C CG2  . ILE B 2 259 ? -1.85400  24.71700  18.85700  1.000 59.90688  ? 259 ILE B CG2  1 
ATOM   8512 C CD1  . ILE B 2 259 ? -4.89300  23.68300  20.91800  1.000 59.77550  ? 259 ILE B CD1  1 
ATOM   8513 H H    . ILE B 2 259 ? -5.83700  24.59600  18.25600  1.000 75.93421  ? 259 ILE B H    1 
ATOM   8514 H HA   . ILE B 2 259 ? -3.91900  26.45600  18.74300  1.000 69.94093  ? 259 ILE B HA   1 
ATOM   8515 H HB   . ILE B 2 259 ? -3.60400  23.63800  18.63800  1.000 69.87420  ? 259 ILE B HB   1 
ATOM   8516 H HG12 . ILE B 2 259 ? -2.89800  24.01200  20.97800  1.000 74.09389  ? 259 ILE B HG12 1 
ATOM   8517 H HG13 . ILE B 2 259 ? -3.74300  25.34800  20.86300  1.000 74.09389  ? 259 ILE B HG13 1 
ATOM   8518 H HG21 . ILE B 2 259 ? -1.37500  23.97100  19.25100  1.000 71.88906  ? 259 ILE B HG21 1 
ATOM   8519 H HG22 . ILE B 2 259 ? -1.64500  24.78000  17.91300  1.000 71.88906  ? 259 ILE B HG22 1 
ATOM   8520 H HG23 . ILE B 2 259 ? -1.60600  25.54100  19.30400  1.000 71.88906  ? 259 ILE B HG23 1 
ATOM   8521 H HD11 . ILE B 2 259 ? -4.86800  23.49100  21.86900  1.000 71.73140  ? 259 ILE B HD11 1 
ATOM   8522 H HD12 . ILE B 2 259 ? -5.65900  24.23500  20.71200  1.000 71.73140  ? 259 ILE B HD12 1 
ATOM   8523 H HD13 . ILE B 2 259 ? -4.92400  22.85600  20.41300  1.000 71.73140  ? 259 ILE B HD13 1 
ATOM   8524 N N    . ALA B 2 260 ? -3.55200  26.86500  16.35000  1.000 60.69381  ? 260 ALA B N    1 
ATOM   8525 C CA   . ALA B 2 260 ? -3.15200  26.98100  14.96000  1.000 59.84098  ? 260 ALA B CA   1 
ATOM   8526 C C    . ALA B 2 260 ? -1.87500  26.19100  14.74700  1.000 54.69303  ? 260 ALA B C    1 
ATOM   8527 O O    . ALA B 2 260 ? -1.03300  26.08500  15.64400  1.000 57.62444  ? 260 ALA B O    1 
ATOM   8528 C CB   . ALA B 2 260 ? -2.93600  28.44500  14.57400  1.000 61.32682  ? 260 ALA B CB   1 
ATOM   8529 H H    . ALA B 2 260 ? -3.57800  27.60700  16.78400  1.000 72.83337  ? 260 ALA B H    1 
ATOM   8530 H HA   . ALA B 2 260 ? -3.84300  26.65100  14.40300  1.000 71.80998  ? 260 ALA B HA   1 
ATOM   8531 H HB1  . ALA B 2 260 ? -2.67000  28.48900  13.64200  1.000 73.59298  ? 260 ALA B HB1  1 
ATOM   8532 H HB2  . ALA B 2 260 ? -3.76500  28.93100  14.70600  1.000 73.59298  ? 260 ALA B HB2  1 
ATOM   8533 H HB3  . ALA B 2 260 ? -2.23900  28.82000  15.13500  1.000 73.59298  ? 260 ALA B HB3  1 
ATOM   8534 N N    . VAL B 2 261 ? -1.71700  25.66300  13.53800  1.000 52.94376  ? 261 VAL B N    1 
ATOM   8535 C CA   . VAL B 2 261 ? -0.55500  24.83200  13.24200  1.000 57.04676  ? 261 VAL B CA   1 
ATOM   8536 C C    . VAL B 2 261 ? 0.71800   25.54100  13.67100  1.000 47.16662  ? 261 VAL B C    1 
ATOM   8537 O O    . VAL B 2 261 ? 1.59400   24.94700  14.30400  1.000 47.43204  ? 261 VAL B O    1 
ATOM   8538 C CB   . VAL B 2 261 ? -0.51000  24.45700  11.74700  1.000 49.52614  ? 261 VAL B CB   1 
ATOM   8539 C CG1  . VAL B 2 261 ? 0.75100   23.67600  11.44100  1.000 53.46023  ? 261 VAL B CG1  1 
ATOM   8540 C CG2  . VAL B 2 261 ? -1.71600  23.63900  11.36300  1.000 54.53388  ? 261 VAL B CG2  1 
ATOM   8541 H H    . VAL B 2 261 ? -2.26000  25.76900  12.88000  1.000 63.53332  ? 261 VAL B H    1 
ATOM   8542 H HA   . VAL B 2 261 ? -0.61800  24.00900  13.75100  1.000 68.45691  ? 261 VAL B HA   1 
ATOM   8543 H HB   . VAL B 2 261 ? -0.50600  25.26600  11.21200  1.000 59.43217  ? 261 VAL B HB   1 
ATOM   8544 H HG11 . VAL B 2 261 ? 0.65500   23.25000  10.57500  1.000 64.15308  ? 261 VAL B HG11 1 
ATOM   8545 H HG12 . VAL B 2 261 ? 1.50700   24.28400  11.42600  1.000 64.15308  ? 261 VAL B HG12 1 
ATOM   8546 H HG13 . VAL B 2 261 ? 0.87900   23.00200  12.12700  1.000 64.15308  ? 261 VAL B HG13 1 
ATOM   8547 H HG21 . VAL B 2 261 ? -1.62500  23.35700  10.44000  1.000 65.44146  ? 261 VAL B HG21 1 
ATOM   8548 H HG22 . VAL B 2 261 ? -1.76900  22.86400  11.94300  1.000 65.44146  ? 261 VAL B HG22 1 
ATOM   8549 H HG23 . VAL B 2 261 ? -2.51100  24.18400  11.46400  1.000 65.44146  ? 261 VAL B HG23 1 
ATOM   8550 N N    . LEU B 2 262 ? 0.85900   26.82300  13.32100  1.000 52.81554  ? 262 LEU B N    1 
ATOM   8551 C CA   . LEU B 2 262 ? 2.08100   27.51900  13.70900  1.000 49.42542  ? 262 LEU B CA   1 
ATOM   8552 C C    . LEU B 2 262 ? 2.13900   27.77700  15.21700  1.000 47.70615  ? 262 LEU B C    1 
ATOM   8553 O O    . LEU B 2 262 ? 3.23100   27.85900  15.79200  1.000 48.62325  ? 262 LEU B O    1 
ATOM   8554 C CB   . LEU B 2 262 ? 2.21600   28.82900  12.92700  1.000 54.81432  ? 262 LEU B CB   1 
ATOM   8555 C CG   . LEU B 2 262 ? 2.66500   28.63000  11.47800  1.000 55.82137  ? 262 LEU B CG   1 
ATOM   8556 C CD1  . LEU B 2 262 ? 2.52700   29.94100  10.69800  1.000 57.98000  ? 262 LEU B CD1  1 
ATOM   8557 C CD2  . LEU B 2 262 ? 4.12300   28.14800  11.44200  1.000 55.95899  ? 262 LEU B CD2  1 
ATOM   8558 H H    . LEU B 2 262 ? 0.28900   27.29100  12.87900  1.000 63.37945  ? 262 LEU B H    1 
ATOM   8559 H HA   . LEU B 2 262 ? 2.83600   26.95800  13.48000  1.000 59.31131  ? 262 LEU B HA   1 
ATOM   8560 H HB2  . LEU B 2 262 ? 1.35500   29.27500  12.91300  1.000 65.77799  ? 262 LEU B HB2  1 
ATOM   8561 H HB3  . LEU B 2 262 ? 2.86900   29.39000  13.37100  1.000 65.77799  ? 262 LEU B HB3  1 
ATOM   8562 H HG   . LEU B 2 262 ? 2.10700   27.95900  11.05500  1.000 66.98644  ? 262 LEU B HG   1 
ATOM   8563 H HD11 . LEU B 2 262 ? 2.81200   29.79400  9.78200   1.000 69.57680  ? 262 LEU B HD11 1 
ATOM   8564 H HD12 . LEU B 2 262 ? 1.59900   30.22100  10.71500  1.000 69.57680  ? 262 LEU B HD12 1 
ATOM   8565 H HD13 . LEU B 2 262 ? 3.08400   30.61700  11.11400  1.000 69.57680  ? 262 LEU B HD13 1 
ATOM   8566 H HD21 . LEU B 2 262 ? 4.45700   28.22700  10.53500  1.000 67.15159  ? 262 LEU B HD21 1 
ATOM   8567 H HD22 . LEU B 2 262 ? 4.65300   28.69800  12.03900  1.000 67.15159  ? 262 LEU B HD22 1 
ATOM   8568 H HD23 . LEU B 2 262 ? 4.15900   27.22200  11.72700  1.000 67.15159  ? 262 LEU B HD23 1 
ATOM   8569 N N    . ASP B 2 263 ? 0.98700   27.86600  15.87500  1.000 54.95766  ? 263 ASP B N    1 
ATOM   8570 C CA   . ASP B 2 263 ? 0.96400   27.88000  17.33700  1.000 49.91284  ? 263 ASP B CA   1 
ATOM   8571 C C    . ASP B 2 263 ? 1.46500   26.53300  17.87600  1.000 48.81533  ? 263 ASP B C    1 
ATOM   8572 O O    . ASP B 2 263 ? 2.38600   26.47300  18.70300  1.000 47.33798  ? 263 ASP B O    1 
ATOM   8573 C CB   . ASP B 2 263 ? -0.47000  28.19200  17.77600  1.000 55.85902  ? 263 ASP B CB   1 
ATOM   8574 C CG   . ASP B 2 263 ? -0.61400  28.48300  19.24900  1.000 56.42725  ? 263 ASP B CG   1 
ATOM   8575 O OD1  . ASP B 2 263 ? 0.34200   28.31600  20.03800  1.000 52.46859  ? 263 ASP B OD1  1 
ATOM   8576 O OD2  . ASP B 2 263 ? -1.74500  28.85200  19.62300  1.000 64.44538  ? 263 ASP B OD2  1 
ATOM   8577 H H    . ASP B 2 263 ? 0.21200   27.91900  15.50500  1.000 65.95000  ? 263 ASP B H    1 
ATOM   8578 H HA   . ASP B 2 263 ? 1.54800   28.58100  17.66500  1.000 59.89621  ? 263 ASP B HA   1 
ATOM   8579 H HB2  . ASP B 2 263 ? -0.78400  28.97000  17.28800  1.000 67.03163  ? 263 ASP B HB2  1 
ATOM   8580 H HB3  . ASP B 2 263 ? -1.03300  27.42900  17.57500  1.000 67.03163  ? 263 ASP B HB3  1 
ATOM   8581 N N    . MET B 2 264 ? 0.93300   25.43200  17.33600  1.000 51.11344  ? 264 MET B N    1 
ATOM   8582 C CA   . MET B 2 264 ? 1.42700   24.11300  17.72800  1.000 52.64538  ? 264 MET B CA   1 
ATOM   8583 C C    . MET B 2 264 ? 2.89000   23.94700  17.36400  1.000 47.42350  ? 264 MET B C    1 
ATOM   8584 O O    . MET B 2 264 ? 3.66500   23.35900  18.12700  1.000 42.17504  ? 264 MET B O    1 
ATOM   8585 C CB   . MET B 2 264 ? 0.60100   23.01600  17.06800  1.000 45.52431  ? 264 MET B CB   1 
ATOM   8586 C CG   . MET B 2 264 ? 0.93200   21.61800  17.59500  1.000 44.34642  ? 264 MET B CG   1 
ATOM   8587 S SD   . MET B 2 264 ? 0.38000   21.46200  19.30900  1.000 41.73644  ? 264 MET B SD   1 
ATOM   8588 C CE   . MET B 2 264 ? -1.30200  20.96000  19.03200  1.000 41.18991  ? 264 MET B CE   1 
ATOM   8589 H H    . MET B 2 264 ? 0.30000   25.42200  16.75400  1.000 61.33693  ? 264 MET B H    1 
ATOM   8590 H HA   . MET B 2 264 ? 1.33300   24.02100  18.68900  1.000 63.17526  ? 264 MET B HA   1 
ATOM   8591 H HB2  . MET B 2 264 ? -0.33900  23.17900  17.23200  1.000 54.62997  ? 264 MET B HB2  1 
ATOM   8592 H HB3  . MET B 2 264 ? 0.77600   23.02300  16.11400  1.000 54.62997  ? 264 MET B HB3  1 
ATOM   8593 H HG2  . MET B 2 264 ? 0.46900   20.95300  17.06100  1.000 53.21651  ? 264 MET B HG2  1 
ATOM   8594 H HG3  . MET B 2 264 ? 1.89000   21.47100  17.56400  1.000 53.21651  ? 264 MET B HG3  1 
ATOM   8595 H HE1  . MET B 2 264 ? -1.73900  20.83400  19.88900  1.000 49.42870  ? 264 MET B HE1  1 
ATOM   8596 H HE2  . MET B 2 264 ? -1.75800  21.65100  18.52600  1.000 49.42870  ? 264 MET B HE2  1 
ATOM   8597 H HE3  . MET B 2 264 ? -1.30500  20.12800  18.53300  1.000 49.42870  ? 264 MET B HE3  1 
ATOM   8598 N N    . CYS B 2 265 ? 3.29700   24.49200  16.20700  1.000 52.68893  ? 265 CYS B N    1 
ATOM   8599 C CA   . CYS B 2 265 ? 4.69800   24.43700  15.82200  1.000 43.05788  ? 265 CYS B CA   1 
ATOM   8600 C C    . CYS B 2 265 ? 5.59000   25.04700  16.88900  1.000 47.79033  ? 265 CYS B C    1 
ATOM   8601 O O    . CYS B 2 265 ? 6.69600   24.55500  17.14500  1.000 45.14952  ? 265 CYS B O    1 
ATOM   8602 C CB   . CYS B 2 265 ? 4.89900   25.15300  14.47900  1.000 51.81626  ? 265 CYS B CB   1 
ATOM   8603 S SG   . CYS B 2 265 ? 4.16500   24.25100  13.06600  1.000 48.42952  ? 265 CYS B SG   1 
ATOM   8604 H H    . CYS B 2 265 ? 2.78500   24.89100  15.64300  1.000 63.22752  ? 265 CYS B H    1 
ATOM   8605 H HA   . CYS B 2 265 ? 4.95800   23.50900  15.70900  1.000 51.67026  ? 265 CYS B HA   1 
ATOM   8606 H HB2  . CYS B 2 265 ? 4.48900   26.03000  14.52600  1.000 62.18031  ? 265 CYS B HB2  1 
ATOM   8607 H HB3  . CYS B 2 265 ? 5.85000   25.24300  14.31200  1.000 62.18031  ? 265 CYS B HB3  1 
ATOM   8608 H HG   . CYS B 2 265 ? 3.21300   23.61100  13.41500  1.000 58.11622  ? 265 CYS B HG   1 
ATOM   8609 N N    . ALA B 2 266 ? 5.14300   26.15700  17.50700  1.000 47.35866  ? 266 ALA B N    1 
ATOM   8610 C CA   . ALA B 2 266 ? 5.92700   26.73300  18.58700  1.000 44.59962  ? 266 ALA B CA   1 
ATOM   8611 C C    . ALA B 2 266 ? 5.98500   25.79500  19.79100  1.000 44.79685  ? 266 ALA B C    1 
ATOM   8612 O O    . ALA B 2 266 ? 6.99500   25.78400  20.51500  1.000 43.65398  ? 266 ALA B O    1 
ATOM   8613 C CB   . ALA B 2 266 ? 5.37400   28.11900  18.97400  1.000 45.07901  ? 266 ALA B CB   1 
ATOM   8614 H H    . ALA B 2 266 ? 4.41400   26.57400  17.32000  1.000 56.83120  ? 266 ALA B H    1 
ATOM   8615 H HA   . ALA B 2 266 ? 6.83600   26.86000  18.27300  1.000 53.52035  ? 266 ALA B HA   1 
ATOM   8616 H HB1  . ALA B 2 266 ? 5.91000   28.48300  19.69600  1.000 54.09561  ? 266 ALA B HB1  1 
ATOM   8617 H HB2  . ALA B 2 266 ? 5.41800   28.70400  18.20100  1.000 54.09561  ? 266 ALA B HB2  1 
ATOM   8618 H HB3  . ALA B 2 266 ? 4.45400   28.01800  19.26200  1.000 54.09561  ? 266 ALA B HB3  1 
ATOM   8619 N N    . SER B 2 267 ? 4.92300   25.00700  20.02800  1.000 40.73305  ? 267 SER B N    1 
ATOM   8620 C CA   . SER B 2 267 ? 5.00500   23.98800  21.08400  1.000 42.98084  ? 267 SER B CA   1 
ATOM   8621 C C    . SER B 2 267 ? 6.03400   22.92500  20.72200  1.000 46.12309  ? 267 SER B C    1 
ATOM   8622 O O    . SER B 2 267 ? 6.92400   22.60600  21.52800  1.000 39.94613  ? 267 SER B O    1 
ATOM   8623 C CB   . SER B 2 267 ? 3.63400   23.33800  21.33000  1.000 45.43350  ? 267 SER B CB   1 
ATOM   8624 O OG   . SER B 2 267 ? 2.79400   24.18400  22.11700  1.000 49.69533  ? 267 SER B OG   1 
ATOM   8625 H H    . SER B 2 267 ? 4.17300   25.04000  19.60900  1.000 48.88047  ? 267 SER B H    1 
ATOM   8626 H HA   . SER B 2 267 ? 5.28900   24.41100  21.91000  1.000 51.57781  ? 267 SER B HA   1 
ATOM   8627 H HB2  . SER B 2 267 ? 3.20300   23.17500  20.47700  1.000 54.52100  ? 267 SER B HB2  1 
ATOM   8628 H HB3  . SER B 2 267 ? 3.76400   22.50000  21.80000  1.000 54.52100  ? 267 SER B HB3  1 
ATOM   8629 H HG   . SER B 2 267 ? 3.15600   24.33800  22.85900  1.000 59.63519  ? 267 SER B HG   1 
ATOM   8630 N N    . LEU B 2 268 ? 5.97400   22.42500  19.47000  1.000 43.25958  ? 268 LEU B N    1 
ATOM   8631 C CA   . LEU B 2 268 ? 6.95300   21.42900  19.03600  1.000 47.00951  ? 268 LEU B CA   1 
ATOM   8632 C C    . LEU B 2 268 ? 8.35600   22.01300  19.00900  1.000 48.09339  ? 268 LEU B C    1 
ATOM   8633 O O    . LEU B 2 268 ? 9.32400   21.35600  19.43300  1.000 43.84483  ? 268 LEU B O    1 
ATOM   8634 C CB   . LEU B 2 268 ? 6.58100   20.87200  17.65700  1.000 42.44456  ? 268 LEU B CB   1 
ATOM   8635 C CG   . LEU B 2 268 ? 7.58200   19.86900  17.04400  1.000 43.88951  ? 268 LEU B CG   1 
ATOM   8636 C CD1  . LEU B 2 268 ? 7.83300   18.71200  17.97900  1.000 45.13316  ? 268 LEU B CD1  1 
ATOM   8637 C CD2  . LEU B 2 268 ? 7.08100   19.34600  15.70000  1.000 38.58504  ? 268 LEU B CD2  1 
ATOM   8638 H H    . LEU B 2 268 ? 5.39200   22.64400  18.87600  1.000 51.91230  ? 268 LEU B H    1 
ATOM   8639 H HA   . LEU B 2 268 ? 6.94900   20.69300  19.66700  1.000 56.41222  ? 268 LEU B HA   1 
ATOM   8640 H HB2  . LEU B 2 268 ? 5.72600   20.42000  17.73100  1.000 50.93427  ? 268 LEU B HB2  1 
ATOM   8641 H HB3  . LEU B 2 268 ? 6.50000   21.61500  17.03900  1.000 50.93427  ? 268 LEU B HB3  1 
ATOM   8642 H HG   . LEU B 2 268 ? 8.42800   20.31800  16.89100  1.000 52.66822  ? 268 LEU B HG   1 
ATOM   8643 H HD11 . LEU B 2 268 ? 8.37100   18.04800  17.52000  1.000 54.16059  ? 268 LEU B HD11 1 
ATOM   8644 H HD12 . LEU B 2 268 ? 8.30400   19.03400  18.76300  1.000 54.16059  ? 268 LEU B HD12 1 
ATOM   8645 H HD13 . LEU B 2 268 ? 6.98200   18.32500  18.23800  1.000 54.16059  ? 268 LEU B HD13 1 
ATOM   8646 H HD21 . LEU B 2 268 ? 7.73300   18.72500  15.34000  1.000 46.30285  ? 268 LEU B HD21 1 
ATOM   8647 H HD22 . LEU B 2 268 ? 6.23300   18.89500  15.83400  1.000 46.30285  ? 268 LEU B HD22 1 
ATOM   8648 H HD23 . LEU B 2 268 ? 6.96600   20.09400  15.09300  1.000 46.30285  ? 268 LEU B HD23 1 
ATOM   8649 N N    . LYS B 2 269 ? 8.49100   23.26700  18.54700  1.000 44.76766  ? 269 LYS B N    1 
ATOM   8650 C CA   . LYS B 2 269 ? 9.80600   23.88100  18.55100  1.000 47.08936  ? 269 LYS B CA   1 
ATOM   8651 C C    . LYS B 2 269 ? 10.42200  23.80200  19.94000  1.000 52.95939  ? 269 LYS B C    1 
ATOM   8652 O O    . LYS B 2 269 ? 11.59600  23.45500  20.09900  1.000 52.72231  ? 269 LYS B O    1 
ATOM   8653 C CB   . LYS B 2 269 ? 9.73300   25.34400  18.08400  1.000 49.58292  ? 269 LYS B CB   1 
ATOM   8654 C CG   . LYS B 2 269 ? 11.09300  25.89100  17.79800  1.000 54.83654  ? 269 LYS B CG   1 
ATOM   8655 C CD   . LYS B 2 269 ? 11.13100  27.40200  17.45700  1.000 55.16180  ? 269 LYS B CD   1 
ATOM   8656 C CE   . LYS B 2 269 ? 10.37700  27.77900  16.16400  1.000 58.07652  ? 269 LYS B CE   1 
ATOM   8657 N NZ   . LYS B 2 269 ? 10.56900  29.25700  15.78900  1.000 58.89661  ? 269 LYS B NZ   1 
ATOM   8658 H H    . LYS B 2 269 ? 7.85600   23.75900  18.23900  1.000 53.72199  ? 269 LYS B H    1 
ATOM   8659 H HA   . LYS B 2 269 ? 10.38300  23.39800  17.93800  1.000 56.50803  ? 269 LYS B HA   1 
ATOM   8660 H HB2  . LYS B 2 269 ? 9.20700   25.39500  17.27100  1.000 59.50031  ? 269 LYS B HB2  1 
ATOM   8661 H HB3  . LYS B 2 269 ? 9.32800   25.88300  18.78100  1.000 59.50031  ? 269 LYS B HB3  1 
ATOM   8662 H HG2  . LYS B 2 269 ? 11.65500  25.75600  18.57700  1.000 65.80465  ? 269 LYS B HG2  1 
ATOM   8663 H HG3  . LYS B 2 269 ? 11.46500  25.41100  17.04200  1.000 65.80465  ? 269 LYS B HG3  1 
ATOM   8664 H HD2  . LYS B 2 269 ? 10.72800  27.89600  18.18800  1.000 66.19496  ? 269 LYS B HD2  1 
ATOM   8665 H HD3  . LYS B 2 269 ? 12.05600  27.67300  17.34900  1.000 66.19496  ? 269 LYS B HD3  1 
ATOM   8666 H HE2  . LYS B 2 269 ? 10.72100  27.23700  15.44200  1.000 69.69263  ? 269 LYS B HE2  1 
ATOM   8667 H HE3  . LYS B 2 269 ? 9.42900   27.61600  16.28600  1.000 69.69263  ? 269 LYS B HE3  1 
ATOM   8668 H HZ1  . LYS B 2 269 ? 10.12300  29.44100  15.04100  1.000 70.67674  ? 269 LYS B HZ1  1 
ATOM   8669 H HZ2  . LYS B 2 269 ? 10.26500  29.77800  16.44300  1.000 70.67674  ? 269 LYS B HZ2  1 
ATOM   8670 H HZ3  . LYS B 2 269 ? 11.43300  29.42800  15.66000  1.000 70.67674  ? 269 LYS B HZ3  1 
ATOM   8671 N N    . GLU B 2 270 ? 9.62900   24.12800  20.97000  1.000 50.54583  ? 270 GLU B N    1 
ATOM   8672 C CA   . GLU B 2 270 ? 10.14100  24.06600  22.33900  1.000 52.92065  ? 270 GLU B CA   1 
ATOM   8673 C C    . GLU B 2 270 ? 10.43400  22.63000  22.76400  1.000 52.57443  ? 270 GLU B C    1 
ATOM   8674 O O    . GLU B 2 270 ? 11.43000  22.37900  23.44200  1.000 53.75870  ? 270 GLU B O    1 
ATOM   8675 C CB   . GLU B 2 270 ? 9.14600   24.71800  23.31300  1.000 49.21685  ? 270 GLU B CB   1 
ATOM   8676 C CG   . GLU B 2 270 ? 8.94800   26.22900  23.09700  1.000 60.84018  ? 270 GLU B CG   1 
ATOM   8677 C CD   . GLU B 2 270 ? 10.24000  27.08700  23.19800  1.000 60.77462  ? 270 GLU B CD   1 
ATOM   8678 O OE1  . GLU B 2 270 ? 11.11900  26.85000  24.07600  1.000 66.76848  ? 270 GLU B OE1  1 
ATOM   8679 O OE2  . GLU B 2 270 ? 10.37400  28.01600  22.36300  1.000 59.26974  ? 270 GLU B OE2  1 
ATOM   8680 H H    . GLU B 2 270 ? 8.81000   24.38200  20.90200  1.000 60.65580  ? 270 GLU B H    1 
ATOM   8681 H HA   . GLU B 2 270 ? 10.97300  24.56300  22.38500  1.000 63.50558  ? 270 GLU B HA   1 
ATOM   8682 H HB2  . GLU B 2 270 ? 8.28200   24.28900  23.20800  1.000 59.06102  ? 270 GLU B HB2  1 
ATOM   8683 H HB3  . GLU B 2 270 ? 9.46800   24.58900  24.21900  1.000 59.06102  ? 270 GLU B HB3  1 
ATOM   8684 H HG2  . GLU B 2 270 ? 8.56800   26.37200  22.21700  1.000 73.00902  ? 270 GLU B HG2  1 
ATOM   8685 H HG3  . GLU B 2 270 ? 8.33800   26.55500  23.77500  1.000 73.00902  ? 270 GLU B HG3  1 
ATOM   8686 N N    . LEU B 2 271 ? 9.59400   21.66100  22.36600  1.000 41.32381  ? 271 LEU B N    1 
ATOM   8687 C CA   . LEU B 2 271 ? 9.86500   20.29200  22.80700  1.000 48.78012  ? 271 LEU B CA   1 
ATOM   8688 C C    . LEU B 2 271 ? 11.20800  19.78300  22.27300  1.000 53.29609  ? 271 LEU B C    1 
ATOM   8689 O O    . LEU B 2 271 ? 11.91900  19.04500  22.96300  1.000 55.03804  ? 271 LEU B O    1 
ATOM   8690 C CB   . LEU B 2 271 ? 8.73200   19.37000  22.37800  1.000 45.43801  ? 271 LEU B CB   1 
ATOM   8691 C CG   . LEU B 2 271 ? 7.44900   19.60000  23.17100  1.000 45.14627  ? 271 LEU B CG   1 
ATOM   8692 C CD1  . LEU B 2 271 ? 6.27900   18.89300  22.51700  1.000 39.06718  ? 271 LEU B CD1  1 
ATOM   8693 C CD2  . LEU B 2 271 ? 7.62600   19.16100  24.61900  1.000 50.78757  ? 271 LEU B CD2  1 
ATOM   8694 H H    . LEU B 2 271 ? 8.90000   21.76400  21.86900  1.000 49.58938  ? 271 LEU B H    1 
ATOM   8695 H HA   . LEU B 2 271 ? 9.91400   20.28100  23.77500  1.000 58.53695  ? 271 LEU B HA   1 
ATOM   8696 H HB2  . LEU B 2 271 ? 8.53700   19.52500  21.44100  1.000 54.52641  ? 271 LEU B HB2  1 
ATOM   8697 H HB3  . LEU B 2 271 ? 9.00600   18.44900  22.51100  1.000 54.52641  ? 271 LEU B HB3  1 
ATOM   8698 H HG   . LEU B 2 271 ? 7.25300   20.55000  23.17400  1.000 54.17633  ? 271 LEU B HG   1 
ATOM   8699 H HD11 . LEU B 2 271 ? 5.47800   19.05900  23.03900  1.000 46.88142  ? 271 LEU B HD11 1 
ATOM   8700 H HD12 . LEU B 2 271 ? 6.16500   19.23800  21.61700  1.000 46.88142  ? 271 LEU B HD12 1 
ATOM   8701 H HD13 . LEU B 2 271 ? 6.46300   17.94100  22.48600  1.000 46.88142  ? 271 LEU B HD13 1 
ATOM   8702 H HD21 . LEU B 2 271 ? 6.75400   19.10900  25.04100  1.000 60.94588  ? 271 LEU B HD21 1 
ATOM   8703 H HD22 . LEU B 2 271 ? 8.05300   18.29000  24.63400  1.000 60.94588  ? 271 LEU B HD22 1 
ATOM   8704 H HD23 . LEU B 2 271 ? 8.17900   19.80900  25.08200  1.000 60.94588  ? 271 LEU B HD23 1 
ATOM   8705 N N    . LEU B 2 272 ? 11.56800  20.15200  21.04100  1.000 53.23878  ? 272 LEU B N    1 
ATOM   8706 C CA   . LEU B 2 272 ? 12.85600  19.71100  20.49700  1.000 54.75129  ? 272 LEU B CA   1 
ATOM   8707 C C    . LEU B 2 272 ? 14.03900  20.31700  21.22500  1.000 58.27503  ? 272 LEU B C    1 
ATOM   8708 O O    . LEU B 2 272 ? 15.03900  19.63400  21.48100  1.000 61.29548  ? 272 LEU B O    1 
ATOM   8709 C CB   . LEU B 2 272 ? 12.97800  20.09100  19.03600  1.000 58.16250  ? 272 LEU B CB   1 
ATOM   8710 C CG   . LEU B 2 272 ? 12.10400  19.27600  18.13500  1.000 49.09343  ? 272 LEU B CG   1 
ATOM   8711 C CD1  . LEU B 2 272 ? 12.37100  19.81500  16.76500  1.000 49.37320  ? 272 LEU B CD1  1 
ATOM   8712 C CD2  . LEU B 2 272 ? 12.57100  17.86000  18.28800  1.000 52.42147  ? 272 LEU B CD2  1 
ATOM   8713 H H    . LEU B 2 272 ? 11.10000  20.64300  20.51300  1.000 63.88733  ? 272 LEU B H    1 
ATOM   8714 H HA   . LEU B 2 272 ? 12.93400  18.75700  20.61500  1.000 65.70235  ? 272 LEU B HA   1 
ATOM   8715 H HB2  . LEU B 2 272 ? 12.72600  21.02200  18.93400  1.000 69.79581  ? 272 LEU B HB2  1 
ATOM   8716 H HB3  . LEU B 2 272 ? 13.89800  19.96600  18.75500  1.000 69.79581  ? 272 LEU B HB3  1 
ATOM   8717 H HG   . LEU B 2 272 ? 11.16600  19.36200  18.36700  1.000 58.91292  ? 272 LEU B HG   1 
ATOM   8718 H HD11 . LEU B 2 272 ? 11.83400  19.32400  16.12400  1.000 59.24864  ? 272 LEU B HD11 1 
ATOM   8719 H HD12 . LEU B 2 272 ? 12.13400  20.75500  16.74300  1.000 59.24864  ? 272 LEU B HD12 1 
ATOM   8720 H HD13 . LEU B 2 272 ? 13.31300  19.70600  16.56000  1.000 59.24864  ? 272 LEU B HD13 1 
ATOM   8721 H HD21 . LEU B 2 272 ? 12.07800  17.33900  17.66500  1.000 62.90657  ? 272 LEU B HD21 1 
ATOM   8722 H HD22 . LEU B 2 272 ? 13.52100  17.80600  18.10200  1.000 62.90657  ? 272 LEU B HD22 1 
ATOM   8723 H HD23 . LEU B 2 272 ? 12.37700  17.52500  19.17300  1.000 62.90657  ? 272 LEU B HD23 1 
ATOM   8724 N N    . GLN B 2 273 ? 13.98500  21.61100  21.50100  1.000 57.26913  ? 273 GLN B N    1 
ATOM   8725 C CA   . GLN B 2 273 ? 15.15100  22.24100  22.09800  1.000 59.30203  ? 273 GLN B CA   1 
ATOM   8726 C C    . GLN B 2 273 ? 15.25100  21.93000  23.58100  1.000 63.31339  ? 273 GLN B C    1 
ATOM   8727 O O    . GLN B 2 273 ? 16.35600  21.88600  24.12800  1.000 63.89197  ? 273 GLN B O    1 
ATOM   8728 C CB   . GLN B 2 273 ? 15.10100  23.75400  21.85700  1.000 59.82549  ? 273 GLN B CB   1 
ATOM   8729 C CG   . GLN B 2 273 ? 14.85100  24.14300  20.37300  1.000 60.07844  ? 273 GLN B CG   1 
ATOM   8730 C CD   . GLN B 2 273 ? 14.55500  25.62900  20.20400  1.000 59.97178  ? 273 GLN B CD   1 
ATOM   8731 O OE1  . GLN B 2 273 ? 15.26100  26.34500  19.50000  1.000 53.17803  ? 273 GLN B OE1  1 
ATOM   8732 N NE2  . GLN B 2 273 ? 13.50200  26.09800  20.86600  1.000 65.00716  ? 273 GLN B NE2  1 
ATOM   8733 H H    . GLN B 2 273 ? 13.31300  22.12900  21.36000  1.000 68.72376  ? 273 GLN B H    1 
ATOM   8734 H HA   . GLN B 2 273 ? 15.95000  21.89800  21.66700  1.000 71.16323  ? 273 GLN B HA   1 
ATOM   8735 H HB2  . GLN B 2 273 ? 14.38300  24.13100  22.38800  1.000 71.79138  ? 273 GLN B HB2  1 
ATOM   8736 H HB3  . GLN B 2 273 ? 15.94800  24.14200  22.12700  1.000 71.79138  ? 273 GLN B HB3  1 
ATOM   8737 H HG2  . GLN B 2 273 ? 15.64300  23.93300  19.85300  1.000 72.09493  ? 273 GLN B HG2  1 
ATOM   8738 H HG3  . GLN B 2 273 ? 14.09000  23.64800  20.03400  1.000 72.09493  ? 273 GLN B HG3  1 
ATOM   8739 H HE21 . GLN B 2 273 ? 13.02900  25.56900  21.35200  1.000 78.00939  ? 273 GLN B HE21 1 
ATOM   8740 H HE22 . GLN B 2 273 ? 13.29200  26.93000  20.80600  1.000 78.00939  ? 273 GLN B HE22 1 
ATOM   8741 N N    . ASN B 2 274 ? 14.11400  21.73900  24.25300  1.000 58.66766  ? 274 ASN B N    1 
ATOM   8742 C CA   . ASN B 2 274 ? 14.10000  21.59400  25.70200  1.000 58.64861  ? 274 ASN B CA   1 
ATOM   8743 C C    . ASN B 2 274 ? 13.82700  20.18100  26.19700  1.000 59.42105  ? 274 ASN B C    1 
ATOM   8744 O O    . ASN B 2 274 ? 14.01300  19.92700  27.38900  1.000 61.33179  ? 274 ASN B O    1 
ATOM   8745 C CB   . ASN B 2 274 ? 13.06500  22.54300  26.31900  1.000 56.89899  ? 274 ASN B CB   1 
ATOM   8746 C CG   . ASN B 2 274 ? 13.43900  23.99900  26.15300  1.000 62.75132  ? 274 ASN B CG   1 
ATOM   8747 O OD1  . ASN B 2 274 ? 13.30200  24.57700  25.07100  1.000 61.35066  ? 274 ASN B OD1  1 
ATOM   8748 N ND2  . ASN B 2 274 ? 13.91900  24.60700  27.23800  1.000 65.59747  ? 274 ASN B ND2  1 
ATOM   8749 H H    . ASN B 2 274 ? 13.33700  21.69000  23.88800  1.000 70.40199  ? 274 ASN B H    1 
ATOM   8750 H HA   . ASN B 2 274 ? 14.96800  21.85500  26.04600  1.000 70.37913  ? 274 ASN B HA   1 
ATOM   8751 H HB2  . ASN B 2 274 ? 12.20900  22.40200  25.88600  1.000 68.27959  ? 274 ASN B HB2  1 
ATOM   8752 H HB3  . ASN B 2 274 ? 12.99200  22.35800  27.26800  1.000 68.27959  ? 274 ASN B HB3  1 
ATOM   8753 H HD21 . ASN B 2 274 ? 14.14800  25.43500  27.20100  1.000 78.71776  ? 274 ASN B HD21 1 
ATOM   8754 H HD22 . ASN B 2 274 ? 14.00000  24.17100  27.97500  1.000 78.71776  ? 274 ASN B HD22 1 
ATOM   8755 N N    . GLY B 2 275 ? 13.38000  19.26600  25.33200  1.000 56.93284  ? 275 GLY B N    1 
ATOM   8756 C CA   . GLY B 2 275 ? 12.95500  17.95500  25.80000  1.000 55.76009  ? 275 GLY B CA   1 
ATOM   8757 C C    . GLY B 2 275 ? 11.62700  18.03500  26.53000  1.000 55.28739  ? 275 GLY B C    1 
ATOM   8758 O O    . GLY B 2 275 ? 10.99100  19.07500  26.61800  1.000 56.74208  ? 275 GLY B O    1 
ATOM   8759 H H    . GLY B 2 275 ? 13.31500  19.38100  24.48200  1.000 68.32021  ? 275 GLY B H    1 
ATOM   8760 H HA2  . GLY B 2 275 ? 12.85900  17.35400  25.04500  1.000 66.91291  ? 275 GLY B HA2  1 
ATOM   8761 H HA3  . GLY B 2 275 ? 13.62100  17.59200  26.40500  1.000 66.91291  ? 275 GLY B HA3  1 
ATOM   8762 N N    . MET B 2 276 ? 11.22700  16.89900  27.08000  1.000 51.61757  ? 276 MET B N    1 
ATOM   8763 C CA   . MET B 2 276 ? 9.92600   16.78000  27.72100  1.000 52.11422  ? 276 MET B CA   1 
ATOM   8764 C C    . MET B 2 276 ? 9.96700   17.06200  29.22600  1.000 61.73753  ? 276 MET B C    1 
ATOM   8765 O O    . MET B 2 276 ? 8.91300   17.06400  29.87600  1.000 60.50210  ? 276 MET B O    1 
ATOM   8766 C CB   . MET B 2 276 ? 9.33500   15.38600  27.44700  1.000 54.77672  ? 276 MET B CB   1 
ATOM   8767 C CG   . MET B 2 276 ? 8.04900   15.41900  26.61200  1.000 56.23374  ? 276 MET B CG   1 
ATOM   8768 S SD   . MET B 2 276 ? 7.59800   13.84000  25.86800  1.000 58.06151  ? 276 MET B SD   1 
ATOM   8769 C CE   . MET B 2 276 ? 8.94600   13.80700  24.67400  1.000 45.19838  ? 276 MET B CE   1 
ATOM   8770 H H    . MET B 2 276 ? 11.69400  16.17700  27.09600  1.000 61.94189  ? 276 MET B H    1 
ATOM   8771 H HA   . MET B 2 276 ? 9.32900   17.42700  27.31300  1.000 62.53786  ? 276 MET B HA   1 
ATOM   8772 H HB2  . MET B 2 276 ? 9.99200   14.85700  26.96900  1.000 65.73287  ? 276 MET B HB2  1 
ATOM   8773 H HB3  . MET B 2 276 ? 9.12700   14.96300  28.29500  1.000 65.73287  ? 276 MET B HB3  1 
ATOM   8774 H HG2  . MET B 2 276 ? 7.32000   15.68600  27.18900  1.000 67.48129  ? 276 MET B HG2  1 
ATOM   8775 H HG3  . MET B 2 276 ? 8.15500   16.06500  25.89600  1.000 67.48129  ? 276 MET B HG3  1 
ATOM   8776 H HE1  . MET B 2 276 ? 8.76000   13.12700  24.00800  1.000 54.23886  ? 276 MET B HE1  1 
ATOM   8777 H HE2  . MET B 2 276 ? 9.01200   14.67600  24.24900  1.000 54.23886  ? 276 MET B HE2  1 
ATOM   8778 H HE3  . MET B 2 276 ? 9.77400   13.60100  25.13500  1.000 54.23886  ? 276 MET B HE3  1 
ATOM   8779 N N    . ASN B 2 277 ? 11.14900  17.28500  29.79900  1.000 63.05840  ? 277 ASN B N    1 
ATOM   8780 C CA   . ASN B 2 277 ? 11.25200  17.59500  31.22000  1.000 64.09042  ? 277 ASN B CA   1 
ATOM   8781 C C    . ASN B 2 277 ? 10.51700  16.56200  32.06800  1.000 65.38759  ? 277 ASN B C    1 
ATOM   8782 O O    . ASN B 2 277 ? 9.84100   16.89700  33.04500  1.000 66.45188  ? 277 ASN B O    1 
ATOM   8783 C CB   . ASN B 2 277 ? 10.73300  19.00100  31.51200  1.000 66.28382  ? 277 ASN B CB   1 
ATOM   8784 C CG   . ASN B 2 277 ? 11.65400  20.07900  30.98100  1.000 74.05074  ? 277 ASN B CG   1 
ATOM   8785 O OD1  . ASN B 2 277 ? 12.83800  20.13000  31.34200  1.000 74.89218  ? 277 ASN B OD1  1 
ATOM   8786 N ND2  . ASN B 2 277 ? 11.12500  20.94400  30.11100  1.000 75.03619  ? 277 ASN B ND2  1 
ATOM   8787 H H    . ASN B 2 277 ? 11.90400  17.26200  29.38700  1.000 75.67088  ? 277 ASN B H    1 
ATOM   8788 H HA   . ASN B 2 277 ? 12.18800  17.72800  31.25500  1.000 76.90931  ? 277 ASN B HA   1 
ATOM   8789 H HB2  . ASN B 2 277 ? 9.86500   19.11300  31.09400  1.000 79.54138  ? 277 ASN B HB2  1 
ATOM   8790 H HB3  . ASN B 2 277 ? 10.65800  19.11900  32.47200  1.000 79.54138  ? 277 ASN B HB3  1 
ATOM   8791 H HD21 . ASN B 2 277 ? 11.61000  21.57300  29.78100  1.000 90.04423  ? 277 ASN B HD21 1 
ATOM   8792 H HD22 . ASN B 2 277 ? 10.29900  20.87400  29.88400  1.000 90.04423  ? 277 ASN B HD22 1 
ATOM   8793 N N    . GLY B 2 278 ? 10.68700  15.28800  31.70900  1.000 64.48427  ? 278 GLY B N    1 
ATOM   8794 C CA   . GLY B 2 278 ? 10.17000  14.18500  32.49000  1.000 70.07671  ? 278 GLY B CA   1 
ATOM   8795 C C    . GLY B 2 278 ? 8.69600   13.89300  32.32100  1.000 68.04965  ? 278 GLY B C    1 
ATOM   8796 O O    . GLY B 2 278 ? 8.19600   12.93300  32.92900  1.000 68.02712  ? 278 GLY B O    1 
ATOM   8797 H H    . GLY B 2 278 ? 11.10800  15.04100  31.00100  1.000 77.38193  ? 278 GLY B H    1 
ATOM   8798 H HA2  . GLY B 2 278 ? 10.65900  13.38100  32.25500  1.000 84.09286  ? 278 GLY B HA2  1 
ATOM   8799 H HA3  . GLY B 2 278 ? 10.33000  14.36700  33.42900  1.000 84.09286  ? 278 GLY B HA3  1 
ATOM   8800 N N    . ARG B 2 279 ? 7.97900   14.66500  31.51500  1.000 58.14863  ? 279 ARG B N    1 
ATOM   8801 C CA   . ARG B 2 279 ? 6.56900   14.36100  31.33600  1.000 52.84839  ? 279 ARG B CA   1 
ATOM   8802 C C    . ARG B 2 279 ? 6.35800   13.42600  30.15200  1.000 47.56930  ? 279 ARG B C    1 
ATOM   8803 O O    . ARG B 2 279 ? 7.27300   13.10800  29.39000  1.000 50.81370  ? 279 ARG B O    1 
ATOM   8804 C CB   . ARG B 2 279 ? 5.75900   15.65100  31.19200  1.000 53.21983  ? 279 ARG B CB   1 
ATOM   8805 C CG   . ARG B 2 279 ? 5.85700   16.53800  32.42900  1.000 53.80150  ? 279 ARG B CG   1 
ATOM   8806 C CD   . ARG B 2 279 ? 5.08300   17.83300  32.30000  1.000 55.51632  ? 279 ARG B CD   1 
ATOM   8807 N NE   . ARG B 2 279 ? 5.94100   18.91900  31.83400  1.000 66.05236  ? 279 ARG B NE   1 
ATOM   8808 C CZ   . ARG B 2 279 ? 5.90700   20.15700  32.31100  1.000 64.48874  ? 279 ARG B CZ   1 
ATOM   8809 N NH1  . ARG B 2 279 ? 5.07100   20.50000  33.28400  1.000 65.71069  ? 279 ARG B NH1  1 
ATOM   8810 N NH2  . ARG B 2 279 ? 6.73400   21.07200  31.80300  1.000 64.42779  ? 279 ARG B NH2  1 
ATOM   8811 H H    . ARG B 2 279 ? 8.27100   15.34500  31.07600  1.000 69.77916  ? 279 ARG B H    1 
ATOM   8812 H HA   . ARG B 2 279 ? 6.24200   13.90600  32.12700  1.000 63.41887  ? 279 ARG B HA   1 
ATOM   8813 H HB2  . ARG B 2 279 ? 6.09500   16.15400  30.43400  1.000 63.86460  ? 279 ARG B HB2  1 
ATOM   8814 H HB3  . ARG B 2 279 ? 4.82500   15.42600  31.05600  1.000 63.86460  ? 279 ARG B HB3  1 
ATOM   8815 H HG2  . ARG B 2 279 ? 5.50300   16.05400  33.19200  1.000 64.56260  ? 279 ARG B HG2  1 
ATOM   8816 H HG3  . ARG B 2 279 ? 6.78800   16.76200  32.58300  1.000 64.56260  ? 279 ARG B HG3  1 
ATOM   8817 H HD2  . ARG B 2 279 ? 4.36700   17.71400  31.65600  1.000 66.62039  ? 279 ARG B HD2  1 
ATOM   8818 H HD3  . ARG B 2 279 ? 4.71900   18.05900  33.16800  1.000 66.62039  ? 279 ARG B HD3  1 
ATOM   8819 H HE   . ARG B 2 279 ? 6.50600   18.74500  31.20900  1.000 79.26363  ? 279 ARG B HE   1 
ATOM   8820 H HH11 . ARG B 2 279 ? 4.53100   19.92500  33.62200  1.000 78.85362  ? 279 ARG B HH11 1 
ATOM   8821 H HH12 . ARG B 2 279 ? 5.06800   21.30900  33.57600  1.000 78.85362  ? 279 ARG B HH12 1 
ATOM   8822 H HH21 . ARG B 2 279 ? 7.27900   20.85700  31.17400  1.000 77.31414  ? 279 ARG B HH21 1 
ATOM   8823 H HH22 . ARG B 2 279 ? 6.72200   21.87700  32.10500  1.000 77.31414  ? 279 ARG B HH22 1 
ATOM   8824 N N    . THR B 2 280 ? 5.12100   12.97600  30.00300  1.000 42.81190  ? 280 THR B N    1 
ATOM   8825 C CA   . THR B 2 280 ? 4.75900   12.14700  28.87800  1.000 39.90093  ? 280 THR B CA   1 
ATOM   8826 C C    . THR B 2 280 ? 3.65800   12.85600  28.10500  1.000 39.57164  ? 280 THR B C    1 
ATOM   8827 O O    . THR B 2 280 ? 2.98800   13.76900  28.61000  1.000 35.74405  ? 280 THR B O    1 
ATOM   8828 C CB   . THR B 2 280 ? 4.26300   10.74100  29.30100  1.000 38.92244  ? 280 THR B CB   1 
ATOM   8829 O OG1  . THR B 2 280 ? 3.17000   10.86500  30.22300  1.000 40.75240  ? 280 THR B OG1  1 
ATOM   8830 C CG2  . THR B 2 280 ? 5.36700   9.90900   29.90600  1.000 44.93458  ? 280 THR B CG2  1 
ATOM   8831 H H    . THR B 2 280 ? 4.47300   13.14000  30.54500  1.000 51.37508  ? 280 THR B H    1 
ATOM   8832 H HA   . THR B 2 280 ? 5.52100   12.03600  28.28900  1.000 47.88192  ? 280 THR B HA   1 
ATOM   8833 H HB   . THR B 2 280 ? 3.94700   10.27600  28.51100  1.000 46.70773  ? 280 THR B HB   1 
ATOM   8834 H HG1  . THR B 2 280 ? 2.90000   10.10300  30.45300  1.000 48.90368  ? 280 THR B HG1  1 
ATOM   8835 H HG21 . THR B 2 280 ? 5.02400   9.03800   30.15900  1.000 53.92229  ? 280 THR B HG21 1 
ATOM   8836 H HG22 . THR B 2 280 ? 6.08400   9.79100   29.26300  1.000 53.92229  ? 280 THR B HG22 1 
ATOM   8837 H HG23 . THR B 2 280 ? 5.72000   10.35000  30.69400  1.000 53.92229  ? 280 THR B HG23 1 
ATOM   8838 N N    . ILE B 2 281 ? 3.50600   12.43300  26.85700  1.000 34.97595  ? 281 ILE B N    1 
ATOM   8839 C CA   . ILE B 2 281 ? 2.41400   12.87300  25.99900  1.000 34.53419  ? 281 ILE B CA   1 
ATOM   8840 C C    . ILE B 2 281 ? 1.73100   11.62500  25.51700  1.000 32.67387  ? 281 ILE B C    1 
ATOM   8841 O O    . ILE B 2 281 ? 2.38200   10.76000  24.93000  1.000 31.30065  ? 281 ILE B O    1 
ATOM   8842 C CB   . ILE B 2 281 ? 2.92600   13.72400  24.81300  1.000 35.58892  ? 281 ILE B CB   1 
ATOM   8843 C CG1  . ILE B 2 281 ? 3.57900   14.98900  25.37900  1.000 38.55920  ? 281 ILE B CG1  1 
ATOM   8844 C CG2  . ILE B 2 281 ? 1.75100   14.05800  23.88500  1.000 33.53200  ? 281 ILE B CG2  1 
ATOM   8845 C CD1  . ILE B 2 281 ? 4.29300   15.87600  24.32100  1.000 36.52514  ? 281 ILE B CD1  1 
ATOM   8846 H H    . ILE B 2 281 ? 4.03700   11.87600  26.47400  1.000 41.97194  ? 281 ILE B H    1 
ATOM   8847 H HA   . ILE B 2 281 ? 1.78000   13.39900  26.51200  1.000 41.44183  ? 281 ILE B HA   1 
ATOM   8848 H HB   . ILE B 2 281 ? 3.59000   13.21600  24.32300  1.000 42.70751  ? 281 ILE B HB   1 
ATOM   8849 H HG12 . ILE B 2 281 ? 2.89300   15.53000  25.80100  1.000 46.27184  ? 281 ILE B HG12 1 
ATOM   8850 H HG13 . ILE B 2 281 ? 4.24200   14.73100  26.03800  1.000 46.27184  ? 281 ILE B HG13 1 
ATOM   8851 H HG21 . ILE B 2 281 ? 2.03100   14.73500  23.25000  1.000 40.23920  ? 281 ILE B HG21 1 
ATOM   8852 H HG22 . ILE B 2 281 ? 1.48100   13.25600  23.41000  1.000 40.23920  ? 281 ILE B HG22 1 
ATOM   8853 H HG23 . ILE B 2 281 ? 1.01300   14.39200  24.41900  1.000 40.23920  ? 281 ILE B HG23 1 
ATOM   8854 H HD11 . ILE B 2 281 ? 4.77500   16.58400  24.77700  1.000 43.83097  ? 281 ILE B HD11 1 
ATOM   8855 H HD12 . ILE B 2 281 ? 4.91200   15.32600  23.81500  1.000 43.83097  ? 281 ILE B HD12 1 
ATOM   8856 H HD13 . ILE B 2 281 ? 3.62800   16.25800  23.72700  1.000 43.83097  ? 281 ILE B HD13 1 
ATOM   8857 N N    . LEU B 2 282 ? 0.42200   11.50100  25.77300  1.000 33.56581  ? 282 LEU B N    1 
ATOM   8858 C CA   . LEU B 2 282 ? -0.30100  10.31300  25.33000  1.000 30.52784  ? 282 LEU B CA   1 
ATOM   8859 C C    . LEU B 2 282 ? 0.44900   9.03400   25.70000  1.000 35.16444  ? 282 LEU B C    1 
ATOM   8860 O O    . LEU B 2 282 ? 0.47200   8.05600   24.94400  1.000 33.57839  ? 282 LEU B O    1 
ATOM   8861 C CB   . LEU B 2 282 ? -0.56900  10.34400  23.80900  1.000 33.23836  ? 282 LEU B CB   1 
ATOM   8862 C CG   . LEU B 2 282 ? -1.67600  11.28300  23.34200  1.000 35.99364  ? 282 LEU B CG   1 
ATOM   8863 C CD1  . LEU B 2 282 ? -1.81500  11.25700  21.80400  1.000 34.04221  ? 282 LEU B CD1  1 
ATOM   8864 C CD2  . LEU B 2 282 ? -2.97200  10.88300  24.02600  1.000 34.42678  ? 282 LEU B CD2  1 
ATOM   8865 H H    . LEU B 2 282 ? -0.05700  12.07900  26.19200  1.000 40.27977  ? 282 LEU B H    1 
ATOM   8866 H HA   . LEU B 2 282 ? -1.15400  10.28500  25.78900  1.000 36.63421  ? 282 LEU B HA   1 
ATOM   8867 H HB2  . LEU B 2 282 ? 0.24700   10.61400  23.36100  1.000 39.88684  ? 282 LEU B HB2  1 
ATOM   8868 H HB3  . LEU B 2 282 ? -0.81300  9.45100   23.52100  1.000 39.88684  ? 282 LEU B HB3  1 
ATOM   8869 H HG   . LEU B 2 282 ? -1.45900  12.18900  23.61100  1.000 43.19317  ? 282 LEU B HG   1 
ATOM   8870 H HD11 . LEU B 2 282 ? -2.53000  11.85800  21.54200  1.000 40.85145  ? 282 LEU B HD11 1 
ATOM   8871 H HD12 . LEU B 2 282 ? -0.97800  11.54400  21.40700  1.000 40.85145  ? 282 LEU B HD12 1 
ATOM   8872 H HD13 . LEU B 2 282 ? -2.02300  10.35300  21.52100  1.000 40.85145  ? 282 LEU B HD13 1 
ATOM   8873 H HD21 . LEU B 2 282 ? -3.71800  11.25200  23.52800  1.000 41.31293  ? 282 LEU B HD21 1 
ATOM   8874 H HD22 . LEU B 2 282 ? -3.03300  9.91500   24.04400  1.000 41.31293  ? 282 LEU B HD22 1 
ATOM   8875 H HD23 . LEU B 2 282 ? -2.97400  11.23200  24.93100  1.000 41.31293  ? 282 LEU B HD23 1 
ATOM   8876 N N    . GLY B 2 283 ? 1.05200   9.03400   26.88000  1.000 35.05116  ? 283 GLY B N    1 
ATOM   8877 C CA   . GLY B 2 283 ? 1.65700   7.81100   27.37100  1.000 42.22565  ? 283 GLY B CA   1 
ATOM   8878 C C    . GLY B 2 283 ? 2.99500   7.47800   26.76300  1.000 41.13266  ? 283 GLY B C    1 
ATOM   8879 O O    . GLY B 2 283 ? 3.46100   6.33900   26.89400  1.000 41.88987  ? 283 GLY B O    1 
ATOM   8880 H H    . GLY B 2 283 ? 1.12300   9.71200   27.40400  1.000 42.06219  ? 283 GLY B H    1 
ATOM   8881 H HA2  . GLY B 2 283 ? 1.77400   7.88200   28.33100  1.000 50.67158  ? 283 GLY B HA2  1 
ATOM   8882 H HA3  . GLY B 2 283 ? 1.05600   7.07000   27.19600  1.000 50.67158  ? 283 GLY B HA3  1 
ATOM   8883 N N    . SER B 2 284 ? 3.59900   8.41900   26.05300  1.000 36.92385  ? 284 SER B N    1 
ATOM   8884 C CA   . SER B 2 284 ? 4.89400   8.23400   25.42300  1.000 37.44540  ? 284 SER B CA   1 
ATOM   8885 C C    . SER B 2 284 ? 5.88000   9.25800   25.97000  1.000 38.36032  ? 284 SER B C    1 
ATOM   8886 O O    . SER B 2 284 ? 5.52100   10.41000  26.22700  1.000 35.48777  ? 284 SER B O    1 
ATOM   8887 C CB   . SER B 2 284 ? 4.78500   8.38500   23.90600  1.000 40.76838  ? 284 SER B CB   1 
ATOM   8888 O OG   . SER B 2 284 ? 6.07400   8.41800   23.33400  1.000 42.11696  ? 284 SER B OG   1 
ATOM   8889 H H    . SER B 2 284 ? 3.26600   9.20000   25.91800  1.000 44.30943  ? 284 SER B H    1 
ATOM   8890 H HA   . SER B 2 284 ? 5.23100   7.34600   25.62000  1.000 44.93529  ? 284 SER B HA   1 
ATOM   8891 H HB2  . SER B 2 284 ? 4.29500   7.63000   23.54500  1.000 48.92286  ? 284 SER B HB2  1 
ATOM   8892 H HB3  . SER B 2 284 ? 4.32300   9.21300   23.70000  1.000 48.92286  ? 284 SER B HB3  1 
ATOM   8893 H HG   . SER B 2 284 ? 6.34700   9.21100   23.29600  1.000 50.54115  ? 284 SER B HG   1 
ATOM   8894 N N    . ALA B 2 285 ? 7.12100   8.83200   26.15000  1.000 35.69002  ? 285 ALA B N    1 
ATOM   8895 C CA   . ALA B 2 285 ? 8.18200   9.74400   26.53800  1.000 36.47900  ? 285 ALA B CA   1 
ATOM   8896 C C    . ALA B 2 285 ? 9.00700   10.20900  25.35000  1.000 40.11505  ? 285 ALA B C    1 
ATOM   8897 O O    . ALA B 2 285 ? 9.94800   10.99400  25.53100  1.000 43.52586  ? 285 ALA B O    1 
ATOM   8898 C CB   . ALA B 2 285 ? 9.10000   9.09800   27.58400  1.000 47.67372  ? 285 ALA B CB   1 
ATOM   8899 H H    . ALA B 2 285 ? 7.37500   8.01600   26.05300  1.000 42.82883  ? 285 ALA B H    1 
ATOM   8900 H HA   . ALA B 2 285 ? 7.78600   10.53000  26.94500  1.000 43.77560  ? 285 ALA B HA   1 
ATOM   8901 H HB1  . ALA B 2 285 ? 9.80600   9.72300   27.81200  1.000 57.20927  ? 285 ALA B HB1  1 
ATOM   8902 H HB2  . ALA B 2 285 ? 8.57800   8.88500   28.37300  1.000 57.20927  ? 285 ALA B HB2  1 
ATOM   8903 H HB3  . ALA B 2 285 ? 9.48200   8.28800   27.21100  1.000 57.20927  ? 285 ALA B HB3  1 
ATOM   8904 N N    . LEU B 2 286 ? 8.65100   9.80700   24.13200  1.000 37.17827  ? 286 LEU B N    1 
ATOM   8905 C CA   . LEU B 2 286 ? 9.27900   10.43500  22.98200  1.000 37.93238  ? 286 LEU B CA   1 
ATOM   8906 C C    . LEU B 2 286 ? 8.19900   10.96500  22.04700  1.000 38.61282  ? 286 LEU B C    1 
ATOM   8907 O O    . LEU B 2 286 ? 6.99800   10.74400  22.24400  1.000 36.09490  ? 286 LEU B O    1 
ATOM   8908 C CB   . LEU B 2 286 ? 10.23100  9.48600   22.25700  1.000 44.79102  ? 286 LEU B CB   1 
ATOM   8909 C CG   . LEU B 2 286 ? 9.76800   8.06300   22.07800  1.000 48.59499  ? 286 LEU B CG   1 
ATOM   8910 C CD1  . LEU B 2 286 ? 8.68400   7.95100   20.99700  1.000 48.74392  ? 286 LEU B CD1  1 
ATOM   8911 C CD2  . LEU B 2 286 ? 11.00800  7.23800   21.78200  1.000 47.95407  ? 286 LEU B CD2  1 
ATOM   8912 H H    . LEU B 2 286 ? 8.07700   9.19400   23.95200  1.000 44.61472  ? 286 LEU B H    1 
ATOM   8913 H HA   . LEU B 2 286 ? 9.80000   11.19700  23.27600  1.000 45.51965  ? 286 LEU B HA   1 
ATOM   8914 H HB2  . LEU B 2 286 ? 10.40200  9.84500   21.37200  1.000 53.75002  ? 286 LEU B HB2  1 
ATOM   8915 H HB3  . LEU B 2 286 ? 11.06300  9.45600   22.75500  1.000 53.75002  ? 286 LEU B HB3  1 
ATOM   8916 H HG   . LEU B 2 286 ? 9.39200   7.74100   22.91200  1.000 58.31479  ? 286 LEU B HG   1 
ATOM   8917 H HD11 . LEU B 2 286 ? 8.53300   7.01300   20.80000  1.000 58.49351  ? 286 LEU B HD11 1 
ATOM   8918 H HD12 . LEU B 2 286 ? 7.86600   8.35500   21.32500  1.000 58.49351  ? 286 LEU B HD12 1 
ATOM   8919 H HD13 . LEU B 2 286 ? 8.98500   8.41200   20.19800  1.000 58.49351  ? 286 LEU B HD13 1 
ATOM   8920 H HD21 . LEU B 2 286 ? 10.74000  6.32900   21.57700  1.000 57.54568  ? 286 LEU B HD21 1 
ATOM   8921 H HD22 . LEU B 2 286 ? 11.47100  7.62600   21.02300  1.000 57.54568  ? 286 LEU B HD22 1 
ATOM   8922 H HD23 . LEU B 2 286 ? 11.58600  7.24500   22.56100  1.000 57.54568  ? 286 LEU B HD23 1 
ATOM   8923 N N    . LEU B 2 287 ? 8.64400   11.74300  21.06600  1.000 36.34747  ? 287 LEU B N    1 
ATOM   8924 C CA   . LEU B 2 287 ? 7.73400   12.40500  20.15200  1.000 34.62833  ? 287 LEU B CA   1 
ATOM   8925 C C    . LEU B 2 287 ? 7.36100   11.39100  19.07400  1.000 39.38749  ? 287 LEU B C    1 
ATOM   8926 O O    . LEU B 2 287 ? 8.20500   10.98600  18.27500  1.000 49.43226  ? 287 LEU B O    1 
ATOM   8927 C CB   . LEU B 2 287 ? 8.40800   13.65900  19.58100  1.000 34.53307  ? 287 LEU B CB   1 
ATOM   8928 C CG   . LEU B 2 287 ? 8.80600   14.68800  20.64600  1.000 38.41914  ? 287 LEU B CG   1 
ATOM   8929 C CD1  . LEU B 2 287 ? 9.50700   15.88900  20.04100  1.000 46.25668  ? 287 LEU B CD1  1 
ATOM   8930 C CD2  . LEU B 2 287 ? 7.62800   15.14200  21.51200  1.000 45.06872  ? 287 LEU B CD2  1 
ATOM   8931 H H    . LEU B 2 287 ? 9.47500   11.90200  20.91100  1.000 43.61777  ? 287 LEU B H    1 
ATOM   8932 H HA   . LEU B 2 287 ? 6.92800   12.66700  20.62300  1.000 41.55480  ? 287 LEU B HA   1 
ATOM   8933 H HB2  . LEU B 2 287 ? 9.21300   13.39400  19.11000  1.000 41.44049  ? 287 LEU B HB2  1 
ATOM   8934 H HB3  . LEU B 2 287 ? 7.79500   14.09100  18.96600  1.000 41.44049  ? 287 LEU B HB3  1 
ATOM   8935 H HG   . LEU B 2 287 ? 9.44300   14.26400  21.24200  1.000 46.10377  ? 287 LEU B HG   1 
ATOM   8936 H HD11 . LEU B 2 287 ? 9.74900   16.50400  20.75100  1.000 55.50882  ? 287 LEU B HD11 1 
ATOM   8937 H HD12 . LEU B 2 287 ? 10.30400  15.58800  19.57800  1.000 55.50882  ? 287 LEU B HD12 1 
ATOM   8938 H HD13 . LEU B 2 287 ? 8.90500   16.32400  19.41700  1.000 55.50882  ? 287 LEU B HD13 1 
ATOM   8939 H HD21 . LEU B 2 287 ? 7.91600   15.87600  22.07700  1.000 54.08326  ? 287 LEU B HD21 1 
ATOM   8940 H HD22 . LEU B 2 287 ? 6.90600   15.43300  20.93400  1.000 54.08326  ? 287 LEU B HD22 1 
ATOM   8941 H HD23 . LEU B 2 287 ? 7.33300   14.39900  22.06100  1.000 54.08326  ? 287 LEU B HD23 1 
ATOM   8942 N N    . GLU B 2 288 ? 6.10300   10.97300  19.06500  1.000 33.64211  ? 288 GLU B N    1 
ATOM   8943 C CA   . GLU B 2 288 ? 5.65000   9.90800   18.14200  1.000 34.34822  ? 288 GLU B CA   1 
ATOM   8944 C C    . GLU B 2 288 ? 5.45500   10.46600  16.73100  1.000 29.95462  ? 288 GLU B C    1 
ATOM   8945 O O    . GLU B 2 288 ? 4.75500   11.46600  16.59400  1.000 29.81202  ? 288 GLU B O    1 
ATOM   8946 C CB   . GLU B 2 288 ? 4.29900   9.43200   18.66200  1.000 33.19532  ? 288 GLU B CB   1 
ATOM   8947 C CG   . GLU B 2 288 ? 4.14000   7.94600   18.95600  1.000 53.61324  ? 288 GLU B CG   1 
ATOM   8948 C CD   . GLU B 2 288 ? 5.26100   7.17200   19.61200  1.000 58.66332  ? 288 GLU B CD   1 
ATOM   8949 O OE1  . GLU B 2 288 ? 5.39100   7.25400   20.84900  1.000 59.25737  ? 288 GLU B OE1  1 
ATOM   8950 O OE2  . GLU B 2 288 ? 5.97900   6.46100   18.88400  1.000 67.35789  ? 288 GLU B OE2  1 
ATOM   8951 H H    . GLU B 2 288 ? 5.48800   11.28900  19.57500  1.000 40.37133  ? 288 GLU B H    1 
ATOM   8952 H HA   . GLU B 2 288 ? 6.28100   9.17200   18.12300  1.000 41.21867  ? 288 GLU B HA   1 
ATOM   8953 H HB2  . GLU B 2 288 ? 4.13900   9.88100   19.49900  1.000 39.83519  ? 288 GLU B HB2  1 
ATOM   8954 H HB3  . GLU B 2 288 ? 3.61400   9.68000   18.02100  1.000 39.83519  ? 288 GLU B HB3  1 
ATOM   8955 H HG2  . GLU B 2 288 ? 3.38600   7.86700   19.56100  1.000 64.33669  ? 288 GLU B HG2  1 
ATOM   8956 H HG3  . GLU B 2 288 ? 3.90600   7.49900   18.13700  1.000 64.33669  ? 288 GLU B HG3  1 
ATOM   8957 N N    . ASP B 2 289 ? 6.01100   9.78400   15.73100  1.000 28.69049  ? 289 ASP B N    1 
ATOM   8958 C CA   . ASP B 2 289 ? 5.88500   10.31900  14.38000  1.000 27.87512  ? 289 ASP B CA   1 
ATOM   8959 C C    . ASP B 2 289 ? 5.31700   9.29800   13.39800  1.000 29.10638  ? 289 ASP B C    1 
ATOM   8960 O O    . ASP B 2 289 ? 5.48300   9.46800   12.19100  1.000 26.86951  ? 289 ASP B O    1 
ATOM   8961 C CB   . ASP B 2 289 ? 7.23100   10.90400  13.87800  1.000 30.37830  ? 289 ASP B CB   1 
ATOM   8962 C CG   . ASP B 2 289 ? 8.24500   9.84100   13.44500  1.000 32.50847  ? 289 ASP B CG   1 
ATOM   8963 O OD1  . ASP B 2 289 ? 8.10800   8.65400   13.80400  1.000 30.98055  ? 289 ASP B OD1  1 
ATOM   8964 O OD2  . ASP B 2 289 ? 9.18100   10.19200  12.68900  1.000 33.62109  ? 289 ASP B OD2  1 
ATOM   8965 H H    . ASP B 2 289 ? 6.44600   9.04500   15.80200  1.000 34.42939  ? 289 ASP B H    1 
ATOM   8966 H HA   . ASP B 2 289 ? 5.25600   11.05600  14.40000  1.000 33.45095  ? 289 ASP B HA   1 
ATOM   8967 H HB2  . ASP B 2 289 ? 7.05700   11.47600  13.11400  1.000 36.45476  ? 289 ASP B HB2  1 
ATOM   8968 H HB3  . ASP B 2 289 ? 7.63200   11.42200  14.59300  1.000 36.45476  ? 289 ASP B HB3  1 
ATOM   8969 N N    . GLU B 2 290 ? 4.62200   8.25100   13.86300  1.000 28.85705  ? 290 GLU B N    1 
ATOM   8970 C CA   . GLU B 2 290 ? 3.98200   7.33400   12.91400  1.000 29.54093  ? 290 GLU B CA   1 
ATOM   8971 C C    . GLU B 2 290 ? 2.45200   7.40100   12.97000  1.000 28.92758  ? 290 GLU B C    1 
ATOM   8972 O O    . GLU B 2 290 ? 1.77200   6.40500   12.69200  1.000 27.79331  ? 290 GLU B O    1 
ATOM   8973 C CB   . GLU B 2 290 ? 4.48700   5.91000   13.10000  1.000 29.80360  ? 290 GLU B CB   1 
ATOM   8974 C CG   . GLU B 2 290 ? 6.03000   5.88800   12.84400  1.000 31.17380  ? 290 GLU B CG   1 
ATOM   8975 C CD   . GLU B 2 290 ? 6.58800   4.52700   12.47500  1.000 35.83462  ? 290 GLU B CD   1 
ATOM   8976 O OE1  . GLU B 2 290 ? 5.86600   3.52100   12.64100  1.000 34.00297  ? 290 GLU B OE1  1 
ATOM   8977 O OE2  . GLU B 2 290 ? 7.75400   4.48700   11.99600  1.000 36.51875  ? 290 GLU B OE2  1 
ATOM   8978 H H    . GLU B 2 290 ? 4.50900   8.05600   14.69300  1.000 34.62927  ? 290 GLU B H    1 
ATOM   8979 H HA   . GLU B 2 290 ? 4.23200   7.59600   12.01500  1.000 35.44992  ? 290 GLU B HA   1 
ATOM   8980 H HB2  . GLU B 2 290 ? 4.31600   5.61600   14.00900  1.000 35.76513  ? 290 GLU B HB2  1 
ATOM   8981 H HB3  . GLU B 2 290 ? 4.05600   5.32200   12.46100  1.000 35.76513  ? 290 GLU B HB3  1 
ATOM   8982 H HG2  . GLU B 2 290 ? 6.23300   6.49600   12.11600  1.000 37.40936  ? 290 GLU B HG2  1 
ATOM   8983 H HG3  . GLU B 2 290 ? 6.48200   6.18200   13.65000  1.000 37.40936  ? 290 GLU B HG3  1 
ATOM   8984 N N    . PHE B 2 291 ? 1.89400   8.58600   13.27100  1.000 26.76353  ? 291 PHE B N    1 
ATOM   8985 C CA   . PHE B 2 291 ? 0.47300   8.89100   13.01800  1.000 28.60486  ? 291 PHE B CA   1 
ATOM   8986 C C    . PHE B 2 291 ? 0.36400   10.05700  12.04100  1.000 27.87191  ? 291 PHE B C    1 
ATOM   8987 O O    . PHE B 2 291 ? 0.89100   11.13900  12.31100  1.000 25.88368  ? 291 PHE B O    1 
ATOM   8988 C CB   . PHE B 2 291 ? -0.26200  9.29000   14.29300  1.000 28.20113  ? 291 PHE B CB   1 
ATOM   8989 C CG   . PHE B 2 291 ? -0.35100  8.21400   15.32300  1.000 27.86362  ? 291 PHE B CG   1 
ATOM   8990 C CD1  . PHE B 2 291 ? -1.38600  7.26500   15.28400  1.000 28.15815  ? 291 PHE B CD1  1 
ATOM   8991 C CD2  . PHE B 2 291 ? 0.59200   8.15100   16.35800  1.000 29.77158  ? 291 PHE B CD2  1 
ATOM   8992 C CE1  . PHE B 2 291 ? -1.50000  6.29900   16.30300  1.000 29.96750  ? 291 PHE B CE1  1 
ATOM   8993 C CE2  . PHE B 2 291 ? 0.50100   7.19000   17.35600  1.000 29.50114  ? 291 PHE B CE2  1 
ATOM   8994 C CZ   . PHE B 2 291 ? -0.54700  6.24400   17.30800  1.000 31.55466  ? 291 PHE B CZ   1 
ATOM   8995 H H    . PHE B 2 291 ? 2.32500   9.23900   13.62800  1.000 32.11704  ? 291 PHE B H    1 
ATOM   8996 H HA   . PHE B 2 291 ? 0.03200   8.11800   12.63200  1.000 34.32663  ? 291 PHE B HA   1 
ATOM   8997 H HB2  . PHE B 2 291 ? 0.20000   10.04300  14.69400  1.000 33.84216  ? 291 PHE B HB2  1 
ATOM   8998 H HB3  . PHE B 2 291 ? -1.16700  9.54900   14.06000  1.000 33.84216  ? 291 PHE B HB3  1 
ATOM   8999 H HD1  . PHE B 2 291 ? -2.02900  7.30900   14.61400  1.000 33.79058  ? 291 PHE B HD1  1 
ATOM   9000 H HD2  . PHE B 2 291 ? 1.27600   8.78000   16.39100  1.000 35.72670  ? 291 PHE B HD2  1 
ATOM   9001 H HE1  . PHE B 2 291 ? -2.18000  5.66600   16.27000  1.000 35.96180  ? 291 PHE B HE1  1 
ATOM   9002 H HE2  . PHE B 2 291 ? 1.13600   7.15500   18.03500  1.000 35.40217  ? 291 PHE B HE2  1 
ATOM   9003 H HZ   . PHE B 2 291 ? -0.60900  5.59100   17.96700  1.000 37.86639  ? 291 PHE B HZ   1 
ATOM   9004 N N    . THR B 2 292 ? -0.33900  9.86900   10.92200  1.000 28.82501  ? 292 THR B N    1 
ATOM   9005 C CA   . THR B 2 292 ? -0.57200  10.98700  10.00900  1.000 31.22864  ? 292 THR B CA   1 
ATOM   9006 C C    . THR B 2 292 ? -1.74100  11.83500  10.50300  1.000 27.70204  ? 292 THR B C    1 
ATOM   9007 O O    . THR B 2 292 ? -2.51700  11.42600  11.36700  1.000 29.39773  ? 292 THR B O    1 
ATOM   9008 C CB   . THR B 2 292 ? -0.86800  10.47500  8.60000   1.000 31.44286  ? 292 THR B CB   1 
ATOM   9009 O OG1  . THR B 2 292 ? -2.11800  9.76900   8.64400   1.000 30.32184  ? 292 THR B OG1  1 
ATOM   9010 C CG2  . THR B 2 292 ? 0.23700   9.50400   8.11400   1.000 28.26998  ? 292 THR B CG2  1 
ATOM   9011 H H    . THR B 2 292 ? -0.68400  9.12100   10.67400  1.000 34.59081  ? 292 THR B H    1 
ATOM   9012 H HA   . THR B 2 292 ? 0.22300   11.54100  9.97400   1.000 37.47517  ? 292 THR B HA   1 
ATOM   9013 H HB   . THR B 2 292 ? -0.92900  11.21900  7.98100   1.000 37.73223  ? 292 THR B HB   1 
ATOM   9014 H HG1  . THR B 2 292 ? -2.30900  9.47400   7.88100   1.000 36.38700  ? 292 THR B HG1  1 
ATOM   9015 H HG21 . THR B 2 292 ? 0.07800   9.25700   7.19000   1.000 33.92478  ? 292 THR B HG21 1 
ATOM   9016 H HG22 . THR B 2 292 ? 1.10600   9.93100   8.18100   1.000 33.92478  ? 292 THR B HG22 1 
ATOM   9017 H HG23 . THR B 2 292 ? 0.23700   8.70200   8.65900   1.000 33.92478  ? 292 THR B HG23 1 
ATOM   9018 N N    . PRO B 2 293 ? -1.89300  13.04000  9.97400   1.000 30.50598  ? 293 PRO B N    1 
ATOM   9019 C CA   . PRO B 2 293 ? -3.10700  13.81100  10.29300  1.000 29.93643  ? 293 PRO B CA   1 
ATOM   9020 C C    . PRO B 2 293 ? -4.39600  13.01200  10.02500  1.000 32.04173  ? 293 PRO B C    1 
ATOM   9021 O O    . PRO B 2 293 ? -5.31500  13.00300  10.85500  1.000 30.88582  ? 293 PRO B O    1 
ATOM   9022 C CB   . PRO B 2 293 ? -2.96500  15.04000  9.38000   1.000 35.03122  ? 293 PRO B CB   1 
ATOM   9023 C CG   . PRO B 2 293 ? -1.46900  15.24600  9.25500   1.000 36.09310  ? 293 PRO B CG   1 
ATOM   9024 C CD   . PRO B 2 293 ? -0.90900  13.82100  9.19900   1.000 33.69964  ? 293 PRO B CD   1 
ATOM   9025 H HA   . PRO B 2 293 ? -3.09200  14.09600  11.22000  1.000 35.92452  ? 293 PRO B HA   1 
ATOM   9026 H HB2  . PRO B 2 293 ? -3.36100  14.85400  8.51400   1.000 42.03826  ? 293 PRO B HB2  1 
ATOM   9027 H HB3  . PRO B 2 293 ? -3.38600  15.80900  9.79600   1.000 42.03826  ? 293 PRO B HB3  1 
ATOM   9028 H HG2  . PRO B 2 293 ? -1.26900  15.73000  8.43900   1.000 43.31253  ? 293 PRO B HG2  1 
ATOM   9029 H HG3  . PRO B 2 293 ? -1.13400  15.72000  10.03200  1.000 43.31253  ? 293 PRO B HG3  1 
ATOM   9030 H HD2  . PRO B 2 293 ? -0.87400  13.50700  8.28200   1.000 40.44036  ? 293 PRO B HD2  1 
ATOM   9031 H HD3  . PRO B 2 293 ? -0.03700  13.78400  9.62300   1.000 40.44036  ? 293 PRO B HD3  1 
ATOM   9032 N N    . PHE B 2 294 ? -4.47500  12.28700  8.90500   1.000 34.16654  ? 294 PHE B N    1 
ATOM   9033 C CA   . PHE B 2 294 ? -5.67300  11.48300  8.68100   1.000 37.09276  ? 294 PHE B CA   1 
ATOM   9034 C C    . PHE B 2 294 ? -5.80000  10.37500  9.70600   1.000 34.96503  ? 294 PHE B C    1 
ATOM   9035 O O    . PHE B 2 294 ? -6.91700  9.98900   10.06900  1.000 35.65450  ? 294 PHE B O    1 
ATOM   9036 C CB   . PHE B 2 294 ? -5.71300  10.88800  7.27300   1.000 37.67043  ? 294 PHE B CB   1 
ATOM   9037 C CG   . PHE B 2 294 ? -6.97000  10.08700  7.02500   1.000 42.62899  ? 294 PHE B CG   1 
ATOM   9038 C CD1  . PHE B 2 294 ? -8.19700  10.71900  6.89600   1.000 48.60110  ? 294 PHE B CD1  1 
ATOM   9039 C CD2  . PHE B 2 294 ? -6.93400  8.69300   7.02500   1.000 50.35088  ? 294 PHE B CD2  1 
ATOM   9040 C CE1  . PHE B 2 294 ? -9.36800  9.97800   6.70100   1.000 45.00431  ? 294 PHE B CE1  1 
ATOM   9041 C CE2  . PHE B 2 294 ? -8.09000  7.94400   6.83100   1.000 51.32066  ? 294 PHE B CE2  1 
ATOM   9042 C CZ   . PHE B 2 294 ? -9.31200  8.59000   6.67000   1.000 47.81267  ? 294 PHE B CZ   1 
ATOM   9043 H H    . PHE B 2 294 ? -3.87800  12.24500  8.28800   1.000 41.00065  ? 294 PHE B H    1 
ATOM   9044 H HA   . PHE B 2 294 ? -6.44900  12.05700  8.77600   1.000 44.51211  ? 294 PHE B HA   1 
ATOM   9045 H HB2  . PHE B 2 294 ? -5.68100  11.60700  6.62300   1.000 45.20532  ? 294 PHE B HB2  1 
ATOM   9046 H HB3  . PHE B 2 294 ? -4.95200  10.29800  7.15600   1.000 45.20532  ? 294 PHE B HB3  1 
ATOM   9047 H HD1  . PHE B 2 294 ? -8.23900  11.64800  6.91000   1.000 58.32212  ? 294 PHE B HD1  1 
ATOM   9048 H HD2  . PHE B 2 294 ? -6.11900  8.25700   7.12600   1.000 60.42186  ? 294 PHE B HD2  1 
ATOM   9049 H HE1  . PHE B 2 294 ? -10.18300 10.41400  6.59400   1.000 54.00597  ? 294 PHE B HE1  1 
ATOM   9050 H HE2  . PHE B 2 294 ? -8.04700  7.01500   6.81300   1.000 61.58559  ? 294 PHE B HE2  1 
ATOM   9051 H HZ   . PHE B 2 294 ? -10.08900 8.09400   6.54200   1.000 57.37601  ? 294 PHE B HZ   1 
ATOM   9052 N N    . ASP B 2 295 ? -4.68200  9.78400   10.13700  1.000 30.20207  ? 295 ASP B N    1 
ATOM   9053 C CA   . ASP B 2 295 ? -4.77800  8.74100   11.15700  1.000 32.10444  ? 295 ASP B CA   1 
ATOM   9054 C C    . ASP B 2 295 ? -5.44100  9.28000   12.42300  1.000 29.92473  ? 295 ASP B C    1 
ATOM   9055 O O    . ASP B 2 295 ? -6.20300  8.56100   13.09500  1.000 28.45983  ? 295 ASP B O    1 
ATOM   9056 C CB   . ASP B 2 295 ? -3.39500  8.19800   11.52700  1.000 29.88198  ? 295 ASP B CB   1 
ATOM   9057 C CG   . ASP B 2 295 ? -2.77400  7.36200   10.44000  1.000 34.96057  ? 295 ASP B CG   1 
ATOM   9058 O OD1  . ASP B 2 295 ? -3.51100  6.88100   9.53700   1.000 33.06648  ? 295 ASP B OD1  1 
ATOM   9059 O OD2  . ASP B 2 295 ? -1.54100  7.15700   10.51200  1.000 29.20404  ? 295 ASP B OD2  1 
ATOM   9060 H H    . ASP B 2 295 ? -3.88500  9.96100   9.86600   1.000 36.24328  ? 295 ASP B H    1 
ATOM   9061 H HA   . ASP B 2 295 ? -5.31500  8.00800   10.81900  1.000 38.52613  ? 295 ASP B HA   1 
ATOM   9062 H HB2  . ASP B 2 295 ? -2.80200  8.94400   11.70500  1.000 35.85918  ? 295 ASP B HB2  1 
ATOM   9063 H HB3  . ASP B 2 295 ? -3.47600  7.64400   12.31900  1.000 35.85918  ? 295 ASP B HB3  1 
ATOM   9064 N N    . VAL B 2 296 ? -5.11600  10.52200  12.79700  1.000 28.82655  ? 296 VAL B N    1 
ATOM   9065 C CA   . VAL B 2 296 ? -5.70100  11.09700  14.01200  1.000 29.99157  ? 296 VAL B CA   1 
ATOM   9066 C C    . VAL B 2 296 ? -7.20600  11.33100  13.81200  1.000 33.70645  ? 296 VAL B C    1 
ATOM   9067 O O    . VAL B 2 296 ? -8.03300  11.02300  14.69100  1.000 33.89514  ? 296 VAL B O    1 
ATOM   9068 C CB   . VAL B 2 296 ? -4.97100  12.39700  14.39300  1.000 32.33719  ? 296 VAL B CB   1 
ATOM   9069 C CG1  . VAL B 2 296 ? -5.66200  13.02600  15.59800  1.000 34.76279  ? 296 VAL B CG1  1 
ATOM   9070 C CG2  . VAL B 2 296 ? -3.49300  12.11500  14.72500  1.000 31.60752  ? 296 VAL B CG2  1 
ATOM   9071 H H    . VAL B 2 296 ? -4.57300  11.04000  12.37700  1.000 34.59266  ? 296 VAL B H    1 
ATOM   9072 H HA   . VAL B 2 296 ? -5.59100  10.46800  14.74200  1.000 35.99068  ? 296 VAL B HA   1 
ATOM   9073 H HB   . VAL B 2 296 ? -5.00900  13.02200  13.65200  1.000 38.80543  ? 296 VAL B HB   1 
ATOM   9074 H HG11 . VAL B 2 296 ? -5.06700  13.68300  15.99300  1.000 41.71614  ? 296 VAL B HG11 1 
ATOM   9075 H HG12 . VAL B 2 296 ? -6.48100  13.45600  15.30700  1.000 41.71614  ? 296 VAL B HG12 1 
ATOM   9076 H HG13 . VAL B 2 296 ? -5.86200  12.33200  16.24500  1.000 41.71614  ? 296 VAL B HG13 1 
ATOM   9077 H HG21 . VAL B 2 296 ? -3.05700  12.95000  14.95500  1.000 37.92983  ? 296 VAL B HG21 1 
ATOM   9078 H HG22 . VAL B 2 296 ? -3.45000  11.50100  15.47500  1.000 37.92983  ? 296 VAL B HG22 1 
ATOM   9079 H HG23 . VAL B 2 296 ? -3.06400  11.72100  13.94900  1.000 37.92983  ? 296 VAL B HG23 1 
ATOM   9080 N N    . VAL B 2 297 ? -7.58200  11.84200  12.63500  1.000 35.32164  ? 297 VAL B N    1 
ATOM   9081 C CA   . VAL B 2 297 ? -8.99300  12.08300  12.33800  1.000 35.94905  ? 297 VAL B CA   1 
ATOM   9082 C C    . VAL B 2 297 ? -9.77700  10.77900  12.35600  1.000 33.62165  ? 297 VAL B C    1 
ATOM   9083 O O    . VAL B 2 297 ? -10.81500 10.68800  13.01700  1.000 37.72955  ? 297 VAL B O    1 
ATOM   9084 C CB   . VAL B 2 297 ? -9.14100  12.79400  10.97800  1.000 37.84568  ? 297 VAL B CB   1 
ATOM   9085 C CG1  . VAL B 2 297 ? -10.62100 12.83400  10.57500  1.000 40.11648  ? 297 VAL B CG1  1 
ATOM   9086 C CG2  . VAL B 2 297 ? -8.60100  14.17400  11.06900  1.000 38.33815  ? 297 VAL B CG2  1 
ATOM   9087 H H    . VAL B 2 297 ? -7.04400  12.05500  11.99900  1.000 42.38676  ? 297 VAL B H    1 
ATOM   9088 H HA   . VAL B 2 297 ? -9.36400  12.66400  13.02100  1.000 43.13967  ? 297 VAL B HA   1 
ATOM   9089 H HB   . VAL B 2 297 ? -8.64600  12.30900  10.29900  1.000 45.41561  ? 297 VAL B HB   1 
ATOM   9090 H HG11 . VAL B 2 297 ? -10.74400 13.52100  9.90100   1.000 48.14058  ? 297 VAL B HG11 1 
ATOM   9091 H HG12 . VAL B 2 297 ? -10.87700 11.97100  10.21500  1.000 48.14058  ? 297 VAL B HG12 1 
ATOM   9092 H HG13 . VAL B 2 297 ? -11.15600 13.04200  11.35700  1.000 48.14058  ? 297 VAL B HG13 1 
ATOM   9093 H HG21 . VAL B 2 297 ? -8.70200  14.61000  10.20800  1.000 46.00659  ? 297 VAL B HG21 1 
ATOM   9094 H HG22 . VAL B 2 297 ? -9.09500  14.66200  11.74700  1.000 46.00659  ? 297 VAL B HG22 1 
ATOM   9095 H HG23 . VAL B 2 297 ? -7.66200  14.13100  11.31000  1.000 46.00659  ? 297 VAL B HG23 1 
ATOM   9096 N N    . ARG B 2 298 ? -9.26900  9.73400   11.68800  1.000 32.71024  ? 298 ARG B N    1 
ATOM   9097 C CA   . ARG B 2 298 ? -10.01500 8.47800   11.59800  1.000 34.24773  ? 298 ARG B CA   1 
ATOM   9098 C C    . ARG B 2 298 ? -10.21900 7.85700   12.97900  1.000 37.19741  ? 298 ARG B C    1 
ATOM   9099 O O    . ARG B 2 298 ? -11.27800 7.27700   13.26000  1.000 34.64888  ? 298 ARG B O    1 
ATOM   9100 C CB   . ARG B 2 298 ? -9.35800  7.48000   10.61200  1.000 40.45368  ? 298 ARG B CB   1 
ATOM   9101 C CG   . ARG B 2 298 ? -8.20600  6.55100   11.06100  1.000 47.70151  ? 298 ARG B CG   1 
ATOM   9102 C CD   . ARG B 2 298 ? -7.71500  5.62900   9.85600   1.000 41.04269  ? 298 ARG B CD   1 
ATOM   9103 N NE   . ARG B 2 298 ? -6.35100  5.07600   9.94400   1.000 40.78371  ? 298 ARG B NE   1 
ATOM   9104 C CZ   . ARG B 2 298 ? -6.06900  3.89600   10.49900  1.000 45.16404  ? 298 ARG B CZ   1 
ATOM   9105 N NH1  . ARG B 2 298 ? -7.00900  3.16200   11.08800  1.000 42.77502  ? 298 ARG B NH1  1 
ATOM   9106 N NH2  . ARG B 2 298 ? -4.82000  3.42000   10.43200  1.000 44.70826  ? 298 ARG B NH2  1 
ATOM   9107 H H    . ARG B 2 298 ? -8.50900  9.72900   11.28600  1.000 39.25309  ? 298 ARG B H    1 
ATOM   9108 H HA   . ARG B 2 298 ? -10.89600 8.68000   11.24700  1.000 41.09808  ? 298 ARG B HA   1 
ATOM   9109 H HB2  . ARG B 2 298 ? -10.06100 6.89900   10.28200  1.000 48.54522  ? 298 ARG B HB2  1 
ATOM   9110 H HB3  . ARG B 2 298 ? -9.01300  7.99800   9.86800   1.000 48.54522  ? 298 ARG B HB3  1 
ATOM   9111 H HG2  . ARG B 2 298 ? -7.45600  7.08900   11.36000  1.000 57.24261  ? 298 ARG B HG2  1 
ATOM   9112 H HG3  . ARG B 2 298 ? -8.51600  5.97600   11.77800  1.000 57.24261  ? 298 ARG B HG3  1 
ATOM   9113 H HD2  . ARG B 2 298 ? -8.33000  4.88400   9.77300   1.000 49.25203  ? 298 ARG B HD2  1 
ATOM   9114 H HD3  . ARG B 2 298 ? -7.75100  6.15800   9.04400   1.000 49.25203  ? 298 ARG B HD3  1 
ATOM   9115 H HE   . ARG B 2 298 ? -5.69400  5.59100   9.73800   1.000 48.94125  ? 298 ARG B HE   1 
ATOM   9116 H HH11 . ARG B 2 298 ? -7.81800  3.44800   11.13400  1.000 51.33082  ? 298 ARG B HH11 1 
ATOM   9117 H HH12 . ARG B 2 298 ? -6.80300  2.40300   11.43700  1.000 51.33082  ? 298 ARG B HH12 1 
ATOM   9118 H HH21 . ARG B 2 298 ? -4.20300  3.88400   10.05300  1.000 53.65071  ? 298 ARG B HH21 1 
ATOM   9119 H HH22 . ARG B 2 298 ? -4.62900  2.66100   10.78900  1.000 53.65071  ? 298 ARG B HH22 1 
ATOM   9120 N N    . GLN B 2 299 ? -9.21300  7.95100   13.84600  1.000 31.53585  ? 299 GLN B N    1 
ATOM   9121 C CA   . GLN B 2 299 ? -9.33400  7.31500   15.14900  1.000 32.01506  ? 299 GLN B CA   1 
ATOM   9122 C C    . GLN B 2 299 ? -10.20000 8.14300   16.07900  1.000 32.73232  ? 299 GLN B C    1 
ATOM   9123 O O    . GLN B 2 299 ? -11.09200 7.59500   16.73900  1.000 32.49364  ? 299 GLN B O    1 
ATOM   9124 C CB   . GLN B 2 299 ? -7.95600  7.13000   15.79100  1.000 30.46125  ? 299 GLN B CB   1 
ATOM   9125 C CG   . GLN B 2 299 ? -8.08400  6.34700   17.08300  1.000 25.74287  ? 299 GLN B CG   1 
ATOM   9126 C CD   . GLN B 2 299 ? -6.75600  5.85100   17.66900  1.000 26.97181  ? 299 GLN B CD   1 
ATOM   9127 O OE1  . GLN B 2 299 ? -6.71000  5.48700   18.85500  1.000 26.14398  ? 299 GLN B OE1  1 
ATOM   9128 N NE2  . GLN B 2 299 ? -5.67900  5.80900   16.83200  1.000 26.27876  ? 299 GLN B NE2  1 
ATOM   9129 H H    . GLN B 2 299 ? -8.47200  8.36500   13.70800  1.000 37.84382  ? 299 GLN B H    1 
ATOM   9130 H HA   . GLN B 2 299 ? -9.74300  6.44200   15.04500  1.000 38.41888  ? 299 GLN B HA   1 
ATOM   9131 H HB2  . GLN B 2 299 ? -7.39500  6.63600   15.17500  1.000 36.55430  ? 299 GLN B HB2  1 
ATOM   9132 H HB3  . GLN B 2 299 ? -7.56800  7.99700   15.98900  1.000 36.55430  ? 299 GLN B HB3  1 
ATOM   9133 H HG2  . GLN B 2 299 ? -8.50100  6.91300   17.75100  1.000 30.89224  ? 299 GLN B HG2  1 
ATOM   9134 H HG3  . GLN B 2 299 ? -8.64200  5.57100   16.92000  1.000 30.89224  ? 299 GLN B HG3  1 
ATOM   9135 H HE21 . GLN B 2 299 ? -5.74500  6.06300   16.01500  1.000 31.53531  ? 299 GLN B HE21 1 
ATOM   9136 H HE22 . GLN B 2 299 ? -4.92100  5.53300   17.13000  1.000 31.53531  ? 299 GLN B HE22 1 
ATOM   9137 N N    . CYS B 2 300 ? -10.02900 9.46300   16.05800  1.000 32.22273  ? 300 CYS B N    1 
ATOM   9138 C CA   . CYS B 2 300 ? -10.73500 10.30100  17.00100  1.000 33.81518  ? 300 CYS B CA   1 
ATOM   9139 C C    . CYS B 2 300 ? -12.15400 10.64000  16.56100  1.000 37.02984  ? 300 CYS B C    1 
ATOM   9140 O O    . CYS B 2 300 ? -12.91800 11.13200  17.39100  1.000 35.53859  ? 300 CYS B O    1 
ATOM   9141 C CB   . CYS B 2 300 ? -9.97300  11.59200  17.22100  1.000 33.70412  ? 300 CYS B CB   1 
ATOM   9142 S SG   . CYS B 2 300 ? -8.43300  11.24300  18.14000  1.000 41.54406  ? 300 CYS B SG   1 
ATOM   9143 H H    . CYS B 2 300 ? -9.51600  9.88600   15.51300  1.000 38.66808  ? 300 CYS B H    1 
ATOM   9144 H HA   . CYS B 2 300 ? -10.79000 9.83800   17.85200  1.000 40.57902  ? 300 CYS B HA   1 
ATOM   9145 H HB2  . CYS B 2 300 ? -9.74100  11.98400  16.36500  1.000 40.44574  ? 300 CYS B HB2  1 
ATOM   9146 H HB3  . CYS B 2 300 ? -10.51400 12.20500  17.74300  1.000 40.44574  ? 300 CYS B HB3  1 
ATOM   9147 H HG   . CYS B 2 300 ? -7.83700  12.27100  18.30900  1.000 49.85367  ? 300 CYS B HG   1 
ATOM   9148 N N    A SER B 2 301 ? -12.51900 10.38200  15.29800  0.480 34.34451  ? 301 SER B N    1 
ATOM   9149 N N    B SER B 2 301 ? -12.52800 10.39900  15.29800  0.520 34.27340  ? 301 SER B N    1 
ATOM   9150 C CA   A SER B 2 301 ? -13.88600 10.57100  14.83100  0.480 34.19849  ? 301 SER B CA   1 
ATOM   9151 C CA   B SER B 2 301 ? -13.91200 10.57800  14.87500  0.520 33.37585  ? 301 SER B CA   1 
ATOM   9152 C C    A SER B 2 301 ? -14.61300 9.26200   14.55800  0.480 36.22072  ? 301 SER B C    1 
ATOM   9153 C C    B SER B 2 301 ? -14.62800 9.26100   14.59400  0.520 35.71422  ? 301 SER B C    1 
ATOM   9154 O O    A SER B 2 301 ? -15.78500 9.29400   14.16600  0.480 35.51282  ? 301 SER B O    1 
ATOM   9155 O O    B SER B 2 301 ? -15.81000 9.28600   14.23400  0.520 34.99355  ? 301 SER B O    1 
ATOM   9156 C CB   A SER B 2 301 ? -13.90100 11.44500  13.57000  0.480 38.53061  ? 301 SER B CB   1 
ATOM   9157 C CB   B SER B 2 301 ? -13.99100 11.48600  13.63700  0.520 38.80731  ? 301 SER B CB   1 
ATOM   9158 O OG   A SER B 2 301 ? -13.33000 12.70100  13.87400  0.480 37.90308  ? 301 SER B OG   1 
ATOM   9159 O OG   B SER B 2 301 ? -13.50000 10.81700  12.50100  0.520 36.42545  ? 301 SER B OG   1 
ATOM   9160 H H    A SER B 2 301 ? -11.98300 10.09400  14.69100  0.480 41.21422  ? 301 SER B H    1 
ATOM   9161 H H    B SER B 2 301 ? -11.99900 10.13300  14.67400  0.520 41.12888  ? 301 SER B H    1 
ATOM   9162 H HA   A SER B 2 301 ? -14.38600 11.04200  15.51500  0.480 41.03899  ? 301 SER B HA   1 
ATOM   9163 H HA   B SER B 2 301 ? -14.39900 11.02200  15.58600  0.520 40.05182  ? 301 SER B HA   1 
ATOM   9164 H HB2  A SER B 2 301 ? -13.38000 11.01500  12.87400  0.480 46.23753  ? 301 SER B HB2  1 
ATOM   9165 H HB2  B SER B 2 301 ? -14.91700 11.73300  13.48400  0.520 46.56957  ? 301 SER B HB2  1 
ATOM   9166 H HB3  A SER B 2 301 ? -14.81700 11.57100  13.27700  0.480 46.23753  ? 301 SER B HB3  1 
ATOM   9167 H HB3  B SER B 2 301 ? -13.45600 12.28000  13.79200  0.520 46.56957  ? 301 SER B HB3  1 
ATOM   9168 H HG   A SER B 2 301 ? -13.33200 13.19000  13.19100  0.480 45.48450  ? 301 SER B HG   1 
ATOM   9169 H HG   B SER B 2 301 ? -12.69800 10.59600  12.62200  0.520 43.71134  ? 301 SER B HG   1 
ATOM   9170 N N    . GLY B 2 302 ? -13.96200 8.11900   14.75300  1.000 31.53367  ? 302 GLY B N    1 
ATOM   9171 C CA   . GLY B 2 302 ? -14.61000 6.82800   14.58200  1.000 34.86887  ? 302 GLY B CA   1 
ATOM   9172 C C    . GLY B 2 302 ? -14.99400 6.50800   13.15000  1.000 37.10237  ? 302 GLY B C    1 
ATOM   9173 O O    . GLY B 2 302 ? -16.10200 6.00800   12.89800  1.000 32.96412  ? 302 GLY B O    1 
ATOM   9174 H H    A GLY B 2 302 ? -13.13600 8.06500   14.98700  0.480 37.84121  ? 302 GLY B H    1 
ATOM   9175 H H    B GLY B 2 302 ? -13.12900 8.06700   14.96100  0.520 37.84121  ? 302 GLY B H    1 
ATOM   9176 H HA2  . GLY B 2 302 ? -14.01400 6.13000   14.89700  1.000 41.84345  ? 302 GLY B HA2  1 
ATOM   9177 H HA3  . GLY B 2 302 ? -15.41500 6.80400   15.12200  1.000 41.84345  ? 302 GLY B HA3  1 
ATOM   9178 N N    . VAL B 2 303 ? -14.12700 6.82500   12.19700  1.000 35.29857  ? 303 VAL B N    1 
ATOM   9179 C CA   . VAL B 2 303 ? -14.42100 6.50400   10.80400  1.000 34.08416  ? 303 VAL B CA   1 
ATOM   9180 C C    . VAL B 2 303 ? -14.42400 4.98800   10.65400  1.000 34.28792  ? 303 VAL B C    1 
ATOM   9181 O O    . VAL B 2 303 ? -13.57500 4.30000   11.23400  1.000 31.50736  ? 303 VAL B O    1 
ATOM   9182 C CB   . VAL B 2 303 ? -13.37000 7.16500   9.88600   1.000 38.51998  ? 303 VAL B CB   1 
ATOM   9183 C CG1  . VAL B 2 303 ? -13.49600 6.64700   8.43100   1.000 36.54742  ? 303 VAL B CG1  1 
ATOM   9184 C CG2  . VAL B 2 303 ? -13.44400 8.70000   9.98200   1.000 36.94938  ? 303 VAL B CG2  1 
ATOM   9185 H H    . VAL B 2 303 ? -13.37400 7.21900   12.32500  1.000 42.35909  ? 303 VAL B H    1 
ATOM   9186 H HA   . VAL B 2 303 ? -15.29900 6.84300   10.56800  1.000 40.90179  ? 303 VAL B HA   1 
ATOM   9187 H HB   . VAL B 2 303 ? -12.49100 6.90500   10.20300  1.000 46.22478  ? 303 VAL B HB   1 
ATOM   9188 H HG11 . VAL B 2 303 ? -12.98200 7.22600   7.84600   1.000 43.85770  ? 303 VAL B HG11 1 
ATOM   9189 H HG12 . VAL B 2 303 ? -13.15200 5.74100   8.38400   1.000 43.85770  ? 303 VAL B HG12 1 
ATOM   9190 H HG13 . VAL B 2 303 ? -14.43000 6.66200   8.17100   1.000 43.85770  ? 303 VAL B HG13 1 
ATOM   9191 H HG21 . VAL B 2 303 ? -12.80000 9.08600   9.36800   1.000 44.34005  ? 303 VAL B HG21 1 
ATOM   9192 H HG22 . VAL B 2 303 ? -14.34000 8.98800   9.74700   1.000 44.34005  ? 303 VAL B HG22 1 
ATOM   9193 H HG23 . VAL B 2 303 ? -13.23800 8.96900   10.89100  1.000 44.34005  ? 303 VAL B HG23 1 
ATOM   9194 N N    . THR B 2 304 ? -15.39200 4.44400   9.90400   1.000 31.07525  ? 304 THR B N    1 
ATOM   9195 C CA   . THR B 2 304 ? -15.51600 2.99700   9.73800   1.000 34.29911  ? 304 THR B CA   1 
ATOM   9196 C C    . THR B 2 304 ? -15.35700 2.61400   8.27200   1.000 38.70617  ? 304 THR B C    1 
ATOM   9197 O O    . THR B 2 304 ? -15.42900 3.45400   7.37000   1.000 33.23180  ? 304 THR B O    1 
ATOM   9198 C CB   . THR B 2 304 ? -16.87700 2.44700   10.23500  1.000 35.73491  ? 304 THR B CB   1 
ATOM   9199 O OG1  . THR B 2 304 ? -17.94200 3.08700   9.52900   1.000 33.99452  ? 304 THR B OG1  1 
ATOM   9200 C CG2  . THR B 2 304 ? -17.05300 2.68300   11.72300  1.000 33.85452  ? 304 THR B CG2  1 
ATOM   9201 H H    . THR B 2 304 ? -15.98900 4.89600   9.48100   1.000 37.29110  ? 304 THR B H    1 
ATOM   9202 H HA   . THR B 2 304 ? -14.81500 2.55400   10.24000  1.000 41.15974  ? 304 THR B HA   1 
ATOM   9203 H HB   . THR B 2 304 ? -16.91500 1.49100   10.07300  1.000 42.88270  ? 304 THR B HB   1 
ATOM   9204 H HG1  . THR B 2 304 ? -18.68200 2.79200   9.79600   1.000 40.79423  ? 304 THR B HG1  1 
ATOM   9205 H HG21 . THR B 2 304 ? -17.90600 2.32700   12.01600  1.000 40.62623  ? 304 THR B HG21 1 
ATOM   9206 H HG22 . THR B 2 304 ? -16.34200 2.24300   12.21500  1.000 40.62623  ? 304 THR B HG22 1 
ATOM   9207 H HG23 . THR B 2 304 ? -17.02600 3.63400   11.91300  1.000 40.62623  ? 304 THR B HG23 1 
ATOM   9208 N N    . PHE B 2 305 ? -15.14100 1.32800   8.05000   1.000 34.84621  ? 305 PHE B N    1 
ATOM   9209 C CA   . PHE B 2 305 ? -14.91900 0.80900   6.70300   1.000 44.03418  ? 305 PHE B CA   1 
ATOM   9210 C C    . PHE B 2 305 ? -15.89700 -0.32700  6.44300   1.000 53.26846  ? 305 PHE B C    1 
ATOM   9211 O O    . PHE B 2 305 ? -16.06100 -1.21100  7.28900   1.000 54.60949  ? 305 PHE B O    1 
ATOM   9212 C CB   . PHE B 2 305 ? -13.46000 0.38700   6.56000   1.000 40.26362  ? 305 PHE B CB   1 
ATOM   9213 C CG   . PHE B 2 305 ? -12.52900 1.47000   6.96100   1.000 35.96907  ? 305 PHE B CG   1 
ATOM   9214 C CD1  . PHE B 2 305 ? -12.24300 2.51500   6.07000   1.000 37.70623  ? 305 PHE B CD1  1 
ATOM   9215 C CD2  . PHE B 2 305 ? -12.03000 1.52300   8.26200   1.000 33.07670  ? 305 PHE B CD2  1 
ATOM   9216 C CE1  . PHE B 2 305 ? -11.43800 3.56100   6.44100   1.000 38.66328  ? 305 PHE B CE1  1 
ATOM   9217 C CE2  . PHE B 2 305 ? -11.21800 2.56900   8.66500   1.000 38.60456  ? 305 PHE B CE2  1 
ATOM   9218 C CZ   . PHE B 2 305 ? -10.91400 3.60300   7.75100   1.000 40.83686  ? 305 PHE B CZ   1 
ATOM   9219 H H    . PHE B 2 305 ? -15.11700 0.72700   8.66500   1.000 41.81626  ? 305 PHE B H    1 
ATOM   9220 H HA   . PHE B 2 305 ? -15.09400 1.50800   6.05400   1.000 52.84182  ? 305 PHE B HA   1 
ATOM   9221 H HB2  . PHE B 2 305 ? -13.29300 -0.38100  7.12800   1.000 48.31714  ? 305 PHE B HB2  1 
ATOM   9222 H HB3  . PHE B 2 305 ? -13.28200 0.16300   5.63300   1.000 48.31714  ? 305 PHE B HB3  1 
ATOM   9223 H HD1  . PHE B 2 305 ? -12.59400 2.49100   5.20900   1.000 45.24827  ? 305 PHE B HD1  1 
ATOM   9224 H HD2  . PHE B 2 305 ? -12.23800 0.84400   8.86300   1.000 39.69284  ? 305 PHE B HD2  1 
ATOM   9225 H HE1  . PHE B 2 305 ? -11.23800 4.23700   5.83400   1.000 46.39673  ? 305 PHE B HE1  1 
ATOM   9226 H HE2  . PHE B 2 305 ? -10.87000 2.58700   9.52700   1.000 46.32628  ? 305 PHE B HE2  1 
ATOM   9227 H HZ   . PHE B 2 305 ? -10.35700 4.30200   8.00700   1.000 49.00504  ? 305 PHE B HZ   1 
ATOM   9228 N N    . GLN B 2 306 ? -16.59400 -0.26100  5.31200   1.000 73.79824  ? 306 GLN B N    1 
ATOM   9229 C CA   . GLN B 2 306 ? -17.58600 -1.28100  4.96100   1.000 81.88583  ? 306 GLN B CA   1 
ATOM   9230 C C    . GLN B 2 306 ? -17.35100 -1.79700  3.55100   1.000 72.29795  ? 306 GLN B C    1 
ATOM   9231 O O    . GLN B 2 306 ? -16.30500 -2.36900  3.27200   1.000 71.09188  ? 306 GLN B O    1 
ATOM   9232 C CB   . GLN B 2 306 ? -19.01800 -0.73400  5.08900   1.000 88.16180  ? 306 GLN B CB   1 
ATOM   9233 C CG   . GLN B 2 306 ? -20.10500 -1.81200  4.94000   1.000 88.87747  ? 306 GLN B CG   1 
ATOM   9234 C CD   . GLN B 2 306 ? -21.50400 -1.32900  5.32900   1.000 102.10584 ? 306 GLN B CD   1 
ATOM   9235 O OE1  . GLN B 2 306 ? -21.66000 -0.36300  6.08400   1.000 93.31062  ? 306 GLN B OE1  1 
ATOM   9236 N NE2  . GLN B 2 306 ? -22.52900 -2.00800  4.81000   1.000 98.85047  ? 306 GLN B NE2  1 
ATOM   9237 H H    . GLN B 2 306 ? -16.51300 0.36500   4.72800   1.000 88.55869  ? 306 GLN B H    1 
ATOM   9238 H HA   . GLN B 2 306 ? -17.49600 -2.02700  5.56700   1.000 98.26379  ? 306 GLN B HA   1 
ATOM   9239 H HB2  . GLN B 2 306 ? -19.12100 -0.32700  5.96400   1.000 105.79496 ? 306 GLN B HB2  1 
ATOM   9240 H HB3  . GLN B 2 306 ? -19.16200 -0.06900  4.39800   1.000 105.79496 ? 306 GLN B HB3  1 
ATOM   9241 H HG2  . GLN B 2 306 ? -20.14200 -2.08000  4.00900   1.000 106.65377 ? 306 GLN B HG2  1 
ATOM   9242 H HG3  . GLN B 2 306 ? -19.88800 -2.58000  5.48600   1.000 106.65377 ? 306 GLN B HG3  1 
ATOM   9243 H HE21 . GLN B 2 306 ? -22.38200 -2.67600  4.28800   1.000 118.62136 ? 306 GLN B HE21 1 
ATOM   9244 H HE22 . GLN B 2 306 ? -23.33600 -1.77800  4.99700   1.000 118.62136 ? 306 GLN B HE22 1 
ATOM   9245 N N    . GLY C 3 2   ? -19.40500 11.10300  35.99100  1.000 59.54623  ? 2   GLY C N    1 
ATOM   9246 C CA   . GLY C 3 2   ? -18.71800 11.16700  34.70300  1.000 63.88471  ? 2   GLY C CA   1 
ATOM   9247 C C    . GLY C 3 2   ? -18.46500 9.80700   34.05100  1.000 63.32000  ? 2   GLY C C    1 
ATOM   9248 O O    . GLY C 3 2   ? -17.56100 9.65200   33.21300  1.000 58.57302  ? 2   GLY C O    1 
ATOM   9249 H HA2  . GLY C 3 2   ? -19.24700 11.70000  34.08900  1.000 76.66246  ? 2   GLY C HA2  1 
ATOM   9250 H HA3  . GLY C 3 2   ? -17.86200 11.60600  34.82300  1.000 76.66246  ? 2   GLY C HA3  1 
ATOM   9251 N N    . VAL C 3 3   ? -19.26200 8.81600   34.44600  1.000 43.12513  ? 3   VAL C N    1 
ATOM   9252 C CA   . VAL C 3 3   ? -19.21300 7.47500   33.85900  1.000 44.72315  ? 3   VAL C CA   1 
ATOM   9253 C C    . VAL C 3 3   ? -20.15000 7.42200   32.65900  1.000 37.81683  ? 3   VAL C C    1 
ATOM   9254 O O    . VAL C 3 3   ? -21.31900 7.80200   32.77100  1.000 35.39784  ? 3   VAL C O    1 
ATOM   9255 C CB   . VAL C 3 3   ? -19.62400 6.42100   34.88900  1.000 42.84813  ? 3   VAL C CB   1 
ATOM   9256 C CG1  . VAL C 3 3   ? -19.73600 5.07200   34.17900  1.000 34.59340  ? 3   VAL C CG1  1 
ATOM   9257 C CG2  . VAL C 3 3   ? -18.60000 6.41000   36.07600  1.000 46.94887  ? 3   VAL C CG2  1 
ATOM   9258 H H    . VAL C 3 3   ? -19.85300 8.89600   35.06500  1.000 51.75095  ? 3   VAL C H    1 
ATOM   9259 H HA   . VAL C 3 3   ? -18.31100 7.28100   33.55900  1.000 53.66859  ? 3   VAL C HA   1 
ATOM   9260 H HB   . VAL C 3 3   ? -20.49700 6.64800   35.24500  1.000 51.41856  ? 3   VAL C HB   1 
ATOM   9261 H HG11 . VAL C 3 3   ? -19.65500 4.36500   34.83800  1.000 41.51288  ? 3   VAL C HG11 1 
ATOM   9262 H HG12 . VAL C 3 3   ? -20.59800 5.01300   33.73800  1.000 41.51288  ? 3   VAL C HG12 1 
ATOM   9263 H HG13 . VAL C 3 3   ? -19.02100 4.99800   33.52800  1.000 41.51288  ? 3   VAL C HG13 1 
ATOM   9264 H HG21 . VAL C 3 3   ? -18.90100 5.77600   36.74500  1.000 56.33944  ? 3   VAL C HG21 1 
ATOM   9265 H HG22 . VAL C 3 3   ? -17.73000 6.14700   35.73900  1.000 56.33944  ? 3   VAL C HG22 1 
ATOM   9266 H HG23 . VAL C 3 3   ? -18.55200 7.29900   36.46100  1.000 56.33944  ? 3   VAL C HG23 1 
ATOM   9267 N N    . THR C 3 4   ? -19.67500 6.92100   31.52600  1.000 31.10899  ? 4   THR C N    1 
ATOM   9268 C CA   . THR C 3 4   ? -20.50100 7.01200   30.31700  1.000 31.92521  ? 4   THR C CA   1 
ATOM   9269 C C    . THR C 3 4   ? -20.65500 5.65200   29.66900  1.000 31.23942  ? 4   THR C C    1 
ATOM   9270 O O    . THR C 3 4   ? -19.64300 5.03600   29.29100  1.000 30.37751  ? 4   THR C O    1 
ATOM   9271 C CB   . THR C 3 4   ? -19.87900 7.98200   29.29700  1.000 40.59792  ? 4   THR C CB   1 
ATOM   9272 O OG1  . THR C 3 4   ? -19.71300 9.26000   29.91000  1.000 44.83295  ? 4   THR C OG1  1 
ATOM   9273 C CG2  . THR C 3 4   ? -20.80600 8.11800   28.08000  1.000 39.12072  ? 4   THR C CG2  1 
ATOM   9274 H H    . THR C 3 4   ? -18.91200 6.53800   31.42600  1.000 37.33159  ? 4   THR C H    1 
ATOM   9275 H HA   . THR C 3 4   ? -21.38600 7.33800   30.54200  1.000 38.31105  ? 4   THR C HA   1 
ATOM   9276 H HB   . THR C 3 4   ? -19.01900 7.64400   29.00100  1.000 48.71830  ? 4   THR C HB   1 
ATOM   9277 H HG1  . THR C 3 4   ? -19.37400 9.79900   29.36300  1.000 53.80034  ? 4   THR C HG1  1 
ATOM   9278 H HG21 . THR C 3 4   ? -20.87400 9.05000   27.82100  1.000 46.94566  ? 4   THR C HG21 1 
ATOM   9279 H HG22 . THR C 3 4   ? -20.44800 7.61200   27.33500  1.000 46.94566  ? 4   THR C HG22 1 
ATOM   9280 H HG23 . THR C 3 4   ? -21.69200 7.78700   28.29500  1.000 46.94566  ? 4   THR C HG23 1 
ATOM   9281 N N    A PHE C 3 5   ? -21.90900 5.20800   29.51000  0.610 30.84286  ? 5   PHE C N    1 
ATOM   9282 N N    B PHE C 3 5   ? -21.89800 5.20100   29.44700  0.390 30.88875  ? 5   PHE C N    1 
ATOM   9283 C CA   A PHE C 3 5   ? -22.14900 4.12200   28.57800  0.610 29.83033  ? 5   PHE C CA   1 
ATOM   9284 C CA   B PHE C 3 5   ? -22.09300 3.96800   28.67800  0.390 29.77357  ? 5   PHE C CA   1 
ATOM   9285 C C    A PHE C 3 5   ? -21.65300 4.58500   27.23300  0.610 31.29728  ? 5   PHE C C    1 
ATOM   9286 C C    B PHE C 3 5   ? -22.03500 4.30500   27.19300  0.390 31.46374  ? 5   PHE C C    1 
ATOM   9287 O O    A PHE C 3 5   ? -21.84000 5.74500   26.84400  0.610 32.18210  ? 5   PHE C O    1 
ATOM   9288 O O    B PHE C 3 5   ? -22.85300 5.09800   26.70500  0.390 30.24381  ? 5   PHE C O    1 
ATOM   9289 C CB   A PHE C 3 5   ? -23.63800 3.78200   28.42800  0.610 30.25810  ? 5   PHE C CB   1 
ATOM   9290 C CB   B PHE C 3 5   ? -23.42100 3.27300   29.00100  0.390 30.72616  ? 5   PHE C CB   1 
ATOM   9291 C CG   A PHE C 3 5   ? -24.28300 3.26100   29.66000  0.610 28.80839  ? 5   PHE C CG   1 
ATOM   9292 C CG   B PHE C 3 5   ? -23.67500 2.05500   28.14200  0.390 30.21294  ? 5   PHE C CG   1 
ATOM   9293 C CD1  A PHE C 3 5   ? -23.53100 2.81000   30.72700  0.610 33.17685  ? 5   PHE C CD1  1 
ATOM   9294 C CD1  B PHE C 3 5   ? -22.91500 0.91600   28.31100  0.390 32.19829  ? 5   PHE C CD1  1 
ATOM   9295 C CD2  A PHE C 3 5   ? -25.66700 3.20700   29.74500  0.610 35.44560  ? 5   PHE C CD2  1 
ATOM   9296 C CD2  B PHE C 3 5   ? -24.65900 2.05400   27.17000  0.390 33.17120  ? 5   PHE C CD2  1 
ATOM   9297 C CE1  A PHE C 3 5   ? -24.17700 2.34600   31.88800  0.610 30.31853  ? 5   PHE C CE1  1 
ATOM   9298 C CE1  B PHE C 3 5   ? -23.10000 -0.20200  27.53200  0.390 29.68116  ? 5   PHE C CE1  1 
ATOM   9299 C CE2  A PHE C 3 5   ? -26.31600 2.73800   30.89100  0.610 37.46985  ? 5   PHE C CE2  1 
ATOM   9300 C CE2  B PHE C 3 5   ? -24.86200 0.92600   26.37700  0.390 33.32240  ? 5   PHE C CE2  1 
ATOM   9301 C CZ   A PHE C 3 5   ? -25.56200 2.30300   31.94900  0.610 31.55893  ? 5   PHE C CZ   1 
ATOM   9302 C CZ   B PHE C 3 5   ? -24.07700 -0.20400  26.56600  0.390 33.61372  ? 5   PHE C CZ   1 
ATOM   9303 H H    A PHE C 3 5   ? -22.60500 5.50900   29.91500  0.610 37.01224  ? 5   PHE C H    1 
ATOM   9304 H H    B PHE C 3 5   ? -22.62100 5.57800   29.72100  0.390 37.06730  ? 5   PHE C H    1 
ATOM   9305 H HA   A PHE C 3 5   ? -21.65600 3.33000   28.84200  0.610 35.79720  ? 5   PHE C HA   1 
ATOM   9306 H HA   B PHE C 3 5   ? -21.37300 3.34900   28.87700  0.390 35.72909  ? 5   PHE C HA   1 
ATOM   9307 H HB2  A PHE C 3 5   ? -24.11400 4.58500   28.16500  0.610 36.31052  ? 5   PHE C HB2  1 
ATOM   9308 H HB2  B PHE C 3 5   ? -23.41000 2.98800   29.92800  0.390 36.87219  ? 5   PHE C HB2  1 
ATOM   9309 H HB3  A PHE C 3 5   ? -23.73300 3.10600   27.73900  0.610 36.31052  ? 5   PHE C HB3  1 
ATOM   9310 H HB3  B PHE C 3 5   ? -24.14800 3.89900   28.85500  0.390 36.87219  ? 5   PHE C HB3  1 
ATOM   9311 H HD1  A PHE C 3 5   ? -22.61100 2.85400   30.67800  0.610 39.81302  ? 5   PHE C HD1  1 
ATOM   9312 H HD1  B PHE C 3 5   ? -22.24600 0.91100   28.95700  0.390 38.63875  ? 5   PHE C HD1  1 
ATOM   9313 H HD2  A PHE C 3 5   ? -26.17500 3.50300   29.02700  0.610 42.53553  ? 5   PHE C HD2  1 
ATOM   9314 H HD2  B PHE C 3 5   ? -25.18100 2.81200   27.03900  0.390 39.80624  ? 5   PHE C HD2  1 
ATOM   9315 H HE1  A PHE C 3 5   ? -23.67300 2.04500   32.61000  0.610 36.38304  ? 5   PHE C HE1  1 
ATOM   9316 H HE1  B PHE C 3 5   ? -22.57500 -0.95800  27.66700  0.390 35.61820  ? 5   PHE C HE1  1 
ATOM   9317 H HE2  A PHE C 3 5   ? -27.24500 2.71000   30.93000  0.610 44.96462  ? 5   PHE C HE2  1 
ATOM   9318 H HE2  B PHE C 3 5   ? -25.52500 0.92700   25.72600  0.390 39.98768  ? 5   PHE C HE2  1 
ATOM   9319 H HZ   A PHE C 3 5   ? -25.98100 1.98400   32.71500  0.610 37.87152  ? 5   PHE C HZ   1 
ATOM   9320 H HZ   B PHE C 3 5   ? -24.21500 -0.96000  26.04300  0.390 40.33726  ? 5   PHE C HZ   1 
ATOM   9321 N N    . GLN C 3 6   ? -21.09300 3.68500   26.47400  1.000 28.91965  ? 6   GLN C N    1 
ATOM   9322 C CA   . GLN C 3 6   ? -20.74500 4.09500   25.12300  1.000 28.66383  ? 6   GLN C CA   1 
ATOM   9323 C C    . GLN C 3 6   ? -21.62100 3.45200   24.05200  1.000 30.95669  ? 6   GLN C C    1 
ATOM   9324 O O    . GLN C 3 6   ? -21.14800 3.10200   22.96600  1.000 28.49331  ? 6   GLN C O    1 
ATOM   9325 C CB   . GLN C 3 6   ? -19.26100 3.87200   24.88500  1.000 28.88859  ? 6   GLN C CB   1 
ATOM   9326 C CG   . GLN C 3 6   ? -18.51000 4.95000   25.66700  1.000 29.21455  ? 6   GLN C CG   1 
ATOM   9327 C CD   . GLN C 3 6   ? -17.02300 5.01300   25.40600  1.000 29.25532  ? 6   GLN C CD   1 
ATOM   9328 O OE1  . GLN C 3 6   ? -16.33700 4.00500   25.52500  1.000 27.99426  ? 6   GLN C OE1  1 
ATOM   9329 N NE2  . GLN C 3 6   ? -16.50700 6.22400   25.08300  1.000 30.43075  ? 6   GLN C NE2  1 
ATOM   9330 H H    A GLN C 3 6   ? -20.90700 2.87300   26.68900  0.610 34.70438  ? 6   GLN C H    1 
ATOM   9331 H H    B GLN C 3 6   ? -20.63700 3.01300   26.75800  0.390 34.70438  ? 6   GLN C H    1 
ATOM   9332 H HA   . GLN C 3 6   ? -20.88500 5.04800   25.03200  1.000 34.39740  ? 6   GLN C HA   1 
ATOM   9333 H HB2  . GLN C 3 6   ? -18.99800 2.99900   25.21600  1.000 34.66711  ? 6   GLN C HB2  1 
ATOM   9334 H HB3  . GLN C 3 6   ? -19.05600 3.96500   23.94200  1.000 34.66711  ? 6   GLN C HB3  1 
ATOM   9335 H HG2  . GLN C 3 6   ? -18.87900 5.81700   25.43700  1.000 35.05826  ? 6   GLN C HG2  1 
ATOM   9336 H HG3  . GLN C 3 6   ? -18.63300 4.78600   26.61500  1.000 35.05826  ? 6   GLN C HG3  1 
ATOM   9337 H HE21 . GLN C 3 6   ? -17.02400 6.90800   25.01700  1.000 36.51771  ? 6   GLN C HE21 1 
ATOM   9338 H HE22 . GLN C 3 6   ? -15.66500 6.30500   24.93000  1.000 36.51771  ? 6   GLN C HE22 1 
ATOM   9339 N N    . SER C 3 7   ? -22.92700 3.34100   24.32600  1.000 31.95859  ? 7   SER C N    1 
ATOM   9340 C CA   . SER C 3 7   ? -23.91700 3.27200   23.24400  1.000 31.42860  ? 7   SER C CA   1 
ATOM   9341 C C    . SER C 3 7   ? -23.95700 4.61300   22.53300  1.000 34.80098  ? 7   SER C C    1 
ATOM   9342 O O    . SER C 3 7   ? -23.28200 5.57200   22.91100  1.000 35.51730  ? 7   SER C O    1 
ATOM   9343 C CB   . SER C 3 7   ? -25.30800 2.93200   23.78300  1.000 36.40821  ? 7   SER C CB   1 
ATOM   9344 O OG   . SER C 3 7   ? -25.59700 3.75100   24.90900  1.000 36.98298  ? 7   SER C OG   1 
ATOM   9345 H H    . SER C 3 7   ? -23.26100 3.30400   25.11700  1.000 38.35110  ? 7   SER C H    1 
ATOM   9346 H HA   . SER C 3 7   ? -23.65600 2.59000   22.60600  1.000 37.71512  ? 7   SER C HA   1 
ATOM   9347 H HB2  . SER C 3 7   ? -25.96600 3.10500   23.09200  1.000 43.69065  ? 7   SER C HB2  1 
ATOM   9348 H HB3  . SER C 3 7   ? -25.33500 1.99900   24.03400  1.000 43.69065  ? 7   SER C HB3  1 
ATOM   9349 H HG   . SER C 3 7   ? -25.57900 4.56100   24.68700  1.000 44.38038  ? 7   SER C HG   1 
ATOM   9350 N N    . ALA C 3 8   ? -24.75300 4.69600   21.48400  1.000 37.55753  ? 8   ALA C N    1 
ATOM   9351 C CA   . ALA C 3 8   ? -24.97600 5.95300   20.78900  1.000 40.01225  ? 8   ALA C CA   1 
ATOM   9352 C C    . ALA C 3 8   ? -26.47600 6.22900   20.75600  1.000 48.46197  ? 8   ALA C C    1 
ATOM   9353 O O    . ALA C 3 8   ? -27.28500 5.30000   20.63100  1.000 39.85525  ? 8   ALA C O    1 
ATOM   9354 C CB   . ALA C 3 8   ? -24.40300 5.91300   19.37200  1.000 48.37382  ? 8   ALA C CB   1 
ATOM   9355 H H    . ALA C 3 8   ? -25.18300 4.03100   21.14900  1.000 45.06984  ? 8   ALA C H    1 
ATOM   9356 H HA   . ALA C 3 8   ? -24.54600 6.67600   21.27100  1.000 48.01551  ? 8   ALA C HA   1 
ATOM   9357 H HB1  . ALA C 3 8   ? -24.57600 6.76300   18.93800  1.000 58.04939  ? 8   ALA C HB1  1 
ATOM   9358 H HB2  . ALA C 3 8   ? -23.44700 5.75500   19.42300  1.000 58.04939  ? 8   ALA C HB2  1 
ATOM   9359 H HB3  . ALA C 3 8   ? -24.83200 5.19600   18.87900  1.000 58.04939  ? 8   ALA C HB3  1 
ATOM   9360 N N    . VAL C 3 9   ? -26.84300 7.50500   20.89000  1.000 78.68597  ? 9   VAL C N    1 
ATOM   9361 C CA   . VAL C 3 9   ? -28.25600 7.90800   20.89400  1.000 73.86734  ? 9   VAL C CA   1 
ATOM   9362 C C    . VAL C 3 9   ? -28.47100 9.10300   19.96700  1.000 73.15823  ? 9   VAL C C    1 
ATOM   9363 O O    . VAL C 3 9   ? -29.58100 9.32900   19.48100  1.000 82.62383  ? 9   VAL C O    1 
ATOM   9364 C CB   . VAL C 3 9   ? -28.75300 8.23100   22.32600  1.000 77.62221  ? 9   VAL C CB   1 
ATOM   9365 C CG1  . VAL C 3 9   ? -30.24700 8.62800   22.31300  1.000 76.19813  ? 9   VAL C CG1  1 
ATOM   9366 C CG2  . VAL C 3 9   ? -28.51200 7.05200   23.27700  1.000 70.19022  ? 9   VAL C CG2  1 
ATOM   9367 H H    . VAL C 3 9   ? -26.29300 8.16000   20.98100  1.000 94.42397  ? 9   VAL C H    1 
ATOM   9368 H HA   . VAL C 3 9   ? -28.79200 7.17400   20.55500  1.000 88.64161  ? 9   VAL C HA   1 
ATOM   9369 H HB   . VAL C 3 9   ? -28.25100 8.98900   22.66500  1.000 93.14745  ? 9   VAL C HB   1 
ATOM   9370 H HG11 . VAL C 3 9   ? -30.57200 8.65700   23.22600  1.000 91.43856  ? 9   VAL C HG11 1 
ATOM   9371 H HG12 . VAL C 3 9   ? -30.34100 9.50200   21.90200  1.000 91.43856  ? 9   VAL C HG12 1 
ATOM   9372 H HG13 . VAL C 3 9   ? -30.74400 7.96700   21.80600  1.000 91.43856  ? 9   VAL C HG13 1 
ATOM   9373 H HG21 . VAL C 3 9   ? -28.87500 7.27200   24.14900  1.000 84.22906  ? 9   VAL C HG21 1 
ATOM   9374 H HG22 . VAL C 3 9   ? -28.95500 6.26500   22.92300  1.000 84.22906  ? 9   VAL C HG22 1 
ATOM   9375 H HG23 . VAL C 3 9   ? -27.55800 6.89100   23.34600  1.000 84.22906  ? 9   VAL C HG23 1 
HETATM 9376 C C1   . EDO D 4 .   ? -29.91000 -17.59700 24.50100  1.000 53.74164  ? 401 EDO A C1   1 
HETATM 9377 O O1   . EDO D 4 .   ? -29.55000 -18.79800 23.82000  1.000 58.99976  ? 401 EDO A O1   1 
HETATM 9378 C C2   . EDO D 4 .   ? -30.77900 -16.72700 23.59400  1.000 48.27661  ? 401 EDO A C2   1 
HETATM 9379 O O2   . EDO D 4 .   ? -32.14800 -17.14900 23.70000  1.000 53.14235  ? 401 EDO A O2   1 
HETATM 9380 H H11  . EDO D 4 .   ? -30.45700 -17.84000 25.41400  1.000 64.49077  ? 401 EDO A H11  1 
HETATM 9381 H H12  . EDO D 4 .   ? -29.00800 -17.04900 24.77900  1.000 64.49077  ? 401 EDO A H12  1 
HETATM 9382 H HO1  . EDO D 4 .   ? -29.00000 -19.34400 24.39900  1.000 70.80052  ? 401 EDO A HO1  1 
HETATM 9383 H H21  . EDO D 4 .   ? -30.44200 -16.81900 22.55900  1.000 57.93274  ? 401 EDO A H21  1 
HETATM 9384 H H22  . EDO D 4 .   ? -30.69100 -15.68000 23.89000  1.000 57.93274  ? 401 EDO A H22  1 
HETATM 9385 H HO2  . EDO D 4 .   ? -32.70000 -16.60000 23.12700  1.000 63.77162  ? 401 EDO A HO2  1 
HETATM 9386 C C1   . EDO E 4 .   ? -18.61100 8.06400   15.99500  1.000 49.21912  ? 402 EDO A C1   1 
HETATM 9387 O O1   . EDO E 4 .   ? -18.64700 8.94600   17.13700  1.000 52.64227  ? 402 EDO A O1   1 
HETATM 9388 C C2   . EDO E 4 .   ? -20.03000 7.81100   15.49300  1.000 65.70269  ? 402 EDO A C2   1 
HETATM 9389 O O2   . EDO E 4 .   ? -20.01000 7.17500   14.20200  1.000 65.09824  ? 402 EDO A O2   1 
HETATM 9390 H H11  . EDO E 4 .   ? -18.14500 7.11700   16.27500  1.000 59.06374  ? 402 EDO A H11  1 
HETATM 9391 H H12  . EDO E 4 .   ? -18.01400 8.51500   15.20000  1.000 59.06374  ? 402 EDO A H12  1 
HETATM 9392 H HO1  . EDO E 4 .   ? -17.74600 9.10300   17.45100  1.000 63.17153  ? 402 EDO A HO1  1 
HETATM 9393 H H21  . EDO E 4 .   ? -20.56100 7.17500   16.20500  1.000 78.84403  ? 402 EDO A H21  1 
HETATM 9394 H H22  . EDO E 4 .   ? -20.56700 8.75900   15.42400  1.000 78.84403  ? 402 EDO A H22  1 
HETATM 9395 H HO2  . EDO E 4 .   ? -20.91700 7.02400   13.90300  1.000 78.11869  ? 402 EDO A HO2  1 
HETATM 9396 C C1   . EDO F 4 .   ? 0.95500   1.89600   34.63000  1.000 60.29090  ? 403 EDO A C1   1 
HETATM 9397 O O1   . EDO F 4 .   ? 0.45000   3.05700   35.30700  1.000 70.85921  ? 403 EDO A O1   1 
HETATM 9398 C C2   . EDO F 4 .   ? 1.38600   2.21100   33.19000  1.000 63.27657  ? 403 EDO A C2   1 
HETATM 9399 O O2   . EDO F 4 .   ? 0.25600   2.44000   32.31800  1.000 63.99281  ? 403 EDO A O2   1 
HETATM 9400 H H11  . EDO F 4 .   ? 0.18200   1.12500   34.61500  1.000 72.34988  ? 403 EDO A H11  1 
HETATM 9401 H H12  . EDO F 4 .   ? 1.80900   1.50000   35.18300  1.000 72.34988  ? 403 EDO A H12  1 
HETATM 9402 H HO1  . EDO F 4 .   ? 0.19000   2.81800   36.20700  1.000 85.03186  ? 403 EDO A HO1  1 
HETATM 9403 H H21  . EDO F 4 .   ? 1.97700   1.37900   32.80200  1.000 75.93269  ? 403 EDO A H21  1 
HETATM 9404 H H22  . EDO F 4 .   ? 2.02400   3.09700   33.19200  1.000 75.93269  ? 403 EDO A H22  1 
HETATM 9405 H HO2  . EDO F 4 .   ? 0.57200   2.63400   31.42500  1.000 76.79217  ? 403 EDO A HO2  1 
HETATM 9406 C C1   . EDO G 4 .   ? 11.19000  -0.85900  16.87300  1.000 64.49874  ? 404 EDO A C1   1 
HETATM 9407 O O1   . EDO G 4 .   ? 10.58700  -1.44500  18.04600  1.000 58.00809  ? 404 EDO A O1   1 
HETATM 9408 C C2   . EDO G 4 .   ? 10.15500  -0.00100  16.13600  1.000 65.30424  ? 404 EDO A C2   1 
HETATM 9409 O O2   . EDO G 4 .   ? 9.83400   1.17600   16.89600  1.000 69.45475  ? 404 EDO A O2   1 
HETATM 9410 H H11  . EDO G 4 .   ? 12.04100  -0.24100  17.16500  1.000 77.39929  ? 404 EDO A H11  1 
HETATM 9411 H H12  . EDO G 4 .   ? 11.55400  -1.64800  16.21200  1.000 77.39929  ? 404 EDO A H12  1 
HETATM 9412 H HO1  . EDO G 4 .   ? 11.24200  -1.98600  18.50900  1.000 69.61051  ? 404 EDO A HO1  1 
HETATM 9413 H H21  . EDO G 4 .   ? 9.24900   -0.58500  15.95900  1.000 78.36589  ? 404 EDO A H21  1 
HETATM 9414 H H22  . EDO G 4 .   ? 10.55900  0.30100   15.17300  1.000 78.36589  ? 404 EDO A H22  1 
HETATM 9415 H HO2  . EDO G 4 .   ? 9.18100   1.70200   16.41500  1.000 83.34650  ? 404 EDO A HO2  1 
HETATM 9416 C C1   . PEG H 5 .   ? -22.17100 -9.44200  8.87500   1.000 58.92237  ? 405 PEG A C1   1 
HETATM 9417 O O1   . PEG H 5 .   ? -22.03600 -10.79000 8.42300   1.000 64.21179  ? 405 PEG A O1   1 
HETATM 9418 C C2   . PEG H 5 .   ? -20.85900 -8.71600  8.90400   1.000 54.66479  ? 405 PEG A C2   1 
HETATM 9419 O O2   . PEG H 5 .   ? -20.21000 -8.83400  7.63700   1.000 68.18850  ? 405 PEG A O2   1 
HETATM 9420 C C3   . PEG H 5 .   ? -18.90000 -8.26400  7.61300   1.000 63.28539  ? 405 PEG A C3   1 
HETATM 9421 C C4   . PEG H 5 .   ? -18.04800 -8.95500  6.58600   1.000 54.66571  ? 405 PEG A C4   1 
HETATM 9422 O O4   . PEG H 5 .   ? -16.75500 -9.26200  7.09700   1.000 49.69002  ? 405 PEG A O4   1 
HETATM 9423 H H11  . PEG H 5 .   ? -22.77700 -8.97100  8.28100   1.000 70.70764  ? 405 PEG A H11  1 
HETATM 9424 H H12  . PEG H 5 .   ? -22.54700 -9.44600  9.76900   1.000 70.70764  ? 405 PEG A H12  1 
HETATM 9425 H HO1  . PEG H 5 .   ? -22.75200 -11.24500 8.47400   1.000 77.05495  ? 405 PEG A HO1  1 
HETATM 9426 H H21  . PEG H 5 .   ? -20.29600 -9.10100  9.59300   1.000 65.59854  ? 405 PEG A H21  1 
HETATM 9427 H H22  . PEG H 5 .   ? -21.01400 -7.77900  9.10100   1.000 65.59854  ? 405 PEG A H22  1 
HETATM 9428 H H31  . PEG H 5 .   ? -18.48900 -8.36000  8.48600   1.000 75.94327  ? 405 PEG A H31  1 
HETATM 9429 H H32  . PEG H 5 .   ? -18.96600 -7.32200  7.39200   1.000 75.94327  ? 405 PEG A H32  1 
HETATM 9430 H H41  . PEG H 5 .   ? -18.43100 -9.78200  6.33500   1.000 65.59965  ? 405 PEG A H41  1 
HETATM 9431 H H42  . PEG H 5 .   ? -17.96100 -8.38900  5.80300   1.000 65.59965  ? 405 PEG A H42  1 
HETATM 9432 H HO4  . PEG H 5 .   ? -16.23800 -9.62900  6.53100   1.000 59.62883  ? 405 PEG A HO4  1 
HETATM 9433 C C1   . EDO I 4 .   ? -2.70000  4.89300   26.11000  1.000 60.78849  ? 401 EDO B C1   1 
HETATM 9434 O O1   . EDO I 4 .   ? -1.55400  4.07700   25.81300  1.000 60.45462  ? 401 EDO B O1   1 
HETATM 9435 C C2   . EDO I 4 .   ? -2.54100  6.31000   25.54100  1.000 65.90840  ? 401 EDO B C2   1 
HETATM 9436 O O2   . EDO I 4 .   ? -3.49400  7.21100   26.15000  1.000 61.50037  ? 401 EDO B O2   1 
HETATM 9437 H H11  . EDO I 4 .   ? -2.83000  4.95700   27.19100  1.000 72.94699  ? 401 EDO B H11  1 
HETATM 9438 H H12  . EDO I 4 .   ? -3.58100  4.41300   25.69700  1.000 72.94699  ? 401 EDO B H12  1 
HETATM 9439 H HO1  . EDO I 4 .   ? -1.68300  3.19300   26.18300  1.000 72.54634  ? 401 EDO B HO1  1 
HETATM 9440 H H21  . EDO I 4 .   ? -2.69400  6.29100   24.46100  1.000 79.09088  ? 401 EDO B H21  1 
HETATM 9441 H H22  . EDO I 4 .   ? -1.52700  6.66800   25.73100  1.000 79.09088  ? 401 EDO B H22  1 
HETATM 9442 H HO2  . EDO I 4 .   ? -3.38100  8.09800   25.78100  1.000 73.80124  ? 401 EDO B HO2  1 
HETATM 9443 C C1   . PEG J 5 .   ? 5.06900   -17.64700 12.79100  1.000 61.14369  ? 402 PEG B C1   1 
HETATM 9444 O O1   . PEG J 5 .   ? 4.15000   -16.86800 13.52400  1.000 72.11881  ? 402 PEG B O1   1 
HETATM 9445 C C2   . PEG J 5 .   ? 6.43400   -17.02700 12.75500  1.000 67.68972  ? 402 PEG B C2   1 
HETATM 9446 O O2   . PEG J 5 .   ? 7.44200   -18.02600 12.61200  1.000 73.68819  ? 402 PEG B O2   1 
HETATM 9447 C C3   . PEG J 5 .   ? 7.51400   -18.63400 11.32600  1.000 66.26679  ? 402 PEG B C3   1 
HETATM 9448 C C4   . PEG J 5 .   ? 7.11300   -20.06800 11.42800  1.000 77.18012  ? 402 PEG B C4   1 
HETATM 9449 O O4   . PEG J 5 .   ? 5.87400   -20.32700 10.80000  1.000 79.07001  ? 402 PEG B O4   1 
HETATM 9450 H H11  . PEG J 5 .   ? 4.74400   -17.74500 11.88200  1.000 73.37323  ? 402 PEG B H11  1 
HETATM 9451 H H12  . PEG J 5 .   ? 5.13300   -18.52500 13.19900  1.000 73.37323  ? 402 PEG B H12  1 
HETATM 9452 H HO1  . PEG J 5 .   ? 3.36500   -17.19200 13.54900  1.000 86.54337  ? 402 PEG B HO1  1 
HETATM 9453 H H21  . PEG J 5 .   ? 6.48600   -16.40900 12.01000  1.000 81.22847  ? 402 PEG B H21  1 
HETATM 9454 H H22  . PEG J 5 .   ? 6.58400   -16.54100 13.58100  1.000 81.22847  ? 402 PEG B H22  1 
HETATM 9455 H H31  . PEG J 5 .   ? 6.91700   -18.17600 10.71400  1.000 79.52094  ? 402 PEG B H31  1 
HETATM 9456 H H32  . PEG J 5 .   ? 8.42300   -18.57700 10.99300  1.000 79.52094  ? 402 PEG B H32  1 
HETATM 9457 H H41  . PEG J 5 .   ? 7.79700   -20.61600 11.01200  1.000 92.61695  ? 402 PEG B H41  1 
HETATM 9458 H H42  . PEG J 5 .   ? 7.04600   -20.30900 12.36500  1.000 92.61695  ? 402 PEG B H42  1 
HETATM 9459 H HO4  . PEG J 5 .   ? 5.78500   -21.12700 10.52800  1.000 94.88481  ? 402 PEG B HO4  1 
HETATM 9460 N N    . GLN K 6 .   ? 13.78200  -12.69200 3.02000   1.000 59.74331  ? 403 GLN B N    1 
HETATM 9461 C CA   . GLN K 6 .   ? 13.04200  -13.41800 4.06000   1.000 53.46111  ? 403 GLN B CA   1 
HETATM 9462 C C    . GLN K 6 .   ? 11.93500  -14.30800 3.42100   1.000 53.25965  ? 403 GLN B C    1 
HETATM 9463 O O    . GLN K 6 .   ? 10.83400  -14.53500 3.97000   1.000 40.37012  ? 403 GLN B O    1 
HETATM 9464 C CB   . GLN K 6 .   ? 12.46400  -12.43100 5.08600   1.000 48.50811  ? 403 GLN B CB   1 
HETATM 9465 C CG   . GLN K 6 .   ? 13.49400  -11.91500 6.14100   1.000 50.97423  ? 403 GLN B CG   1 
HETATM 9466 C CD   . GLN K 6 .   ? 12.87900  -10.89600 7.13800   1.000 50.17051  ? 403 GLN B CD   1 
HETATM 9467 O OE1  . GLN K 6 .   ? 12.27700  -9.90900  6.71200   1.000 40.86805  ? 403 GLN B OE1  1 
HETATM 9468 N NE2  . GLN K 6 .   ? 13.04100  -11.13900 8.47500   1.000 47.11762  ? 403 GLN B NE2  1 
HETATM 9469 H HA   . GLN K 6 .   ? 13.65700  -14.00400 4.52800   1.000 64.15413  ? 403 GLN B HA   1 
HETATM 9470 H HB2  . GLN K 6 .   ? 12.11700  -11.65900 4.61200   1.000 58.21054  ? 403 GLN B HB2  1 
HETATM 9471 H HB3  . GLN K 6 .   ? 11.74500  -12.86900 5.56800   1.000 58.21054  ? 403 GLN B HB3  1 
HETATM 9472 H HG2  . GLN K 6 .   ? 13.82800  -12.66900 6.65100   1.000 61.16988  ? 403 GLN B HG2  1 
HETATM 9473 H HG3  . GLN K 6 .   ? 14.22600  -11.47700 5.67900   1.000 61.16988  ? 403 GLN B HG3  1 
HETATM 9474 H HE21 . GLN K 6 .   ? 13.46800  -11.83800 8.73600   1.000 56.54194  ? 403 GLN B HE21 1 
HETATM 9475 H HE22 . GLN K 6 .   ? 12.71300  -10.59400 9.05400   1.000 56.54194  ? 403 GLN B HE22 1 
HETATM 9476 O O    . HOH L 7 .   ? -18.76800 10.99000  18.03500  1.000 62.79200  ? 501 HOH A O    1 
HETATM 9477 O O    . HOH L 7 .   ? -33.42200 -13.29200 9.84300   1.000 54.63596  ? 502 HOH A O    1 
HETATM 9478 O O    . HOH L 7 .   ? 21.60100  -8.25900  36.34700  1.000 43.49323  ? 503 HOH A O    1 
HETATM 9479 O O    . HOH L 7 .   ? 6.62500   0.93100   24.88600  1.000 48.53287  ? 504 HOH A O    1 
HETATM 9480 O O    . HOH L 7 .   ? -38.09700 -0.30600  34.54300  1.000 49.35659  ? 505 HOH A O    1 
HETATM 9481 O O    . HOH L 7 .   ? 17.92200  -10.16600 50.63600  1.000 45.70793  ? 506 HOH A O    1 
HETATM 9482 O O    . HOH L 7 .   ? -0.44000  -8.71600  39.41700  1.000 45.12328  ? 507 HOH A O    1 
HETATM 9483 O O    . HOH L 7 .   ? 25.16300  -1.56500  37.83900  1.000 48.41790  ? 508 HOH A O    1 
HETATM 9484 O O    . HOH L 7 .   ? 22.62700  4.40800   28.96900  1.000 68.39709  ? 509 HOH A O    1 
HETATM 9485 O O    . HOH L 7 .   ? -22.21200 0.29200   9.57200   1.000 46.46840  ? 510 HOH A O    1 
HETATM 9486 O O    . HOH L 7 .   ? -35.87000 1.02800   24.62000  1.000 51.00064  ? 511 HOH A O    1 
HETATM 9487 O O    . HOH L 7 .   ? 20.87500  -0.78100  33.70200  1.000 47.89005  ? 512 HOH A O    1 
HETATM 9488 O O    . HOH L 7 .   ? 0.55900   4.00100   40.03000  1.000 44.94116  ? 513 HOH A O    1 
HETATM 9489 O O    . HOH L 7 .   ? -22.90900 -12.89500 7.61800   1.000 51.07058  ? 514 HOH A O    1 
HETATM 9490 O O    . HOH L 7 .   ? -18.03300 8.58900   25.34000  1.000 39.40865  ? 515 HOH A O    1 
HETATM 9491 O O    . HOH L 7 .   ? -21.72500 -10.75500 36.91500  1.000 40.89719  ? 516 HOH A O    1 
HETATM 9492 O O    . HOH L 7 .   ? 18.79400  -14.51200 43.85500  1.000 54.93821  ? 517 HOH A O    1 
HETATM 9493 O O    . HOH L 7 .   ? 0.36600   -14.93100 15.94100  1.000 42.95113  ? 518 HOH A O    1 
HETATM 9494 O O    . HOH L 7 .   ? 16.39400  -2.27300  21.92300  1.000 41.34585  ? 519 HOH A O    1 
HETATM 9495 O O    . HOH L 7 .   ? -34.18600 -7.02200  13.64500  1.000 43.48113  ? 520 HOH A O    1 
HETATM 9496 O O    . HOH L 7 .   ? 13.72400  -9.58500  51.47000  1.000 54.19233  ? 521 HOH A O    1 
HETATM 9497 O O    . HOH L 7 .   ? 8.04700   2.09400   34.67300  1.000 36.62050  ? 522 HOH A O    1 
HETATM 9498 O O    . HOH L 7 .   ? -1.08300  -2.60200  24.25900  1.000 32.18085  ? 523 HOH A O    1 
HETATM 9499 O O    . HOH L 7 .   ? -6.64200  2.45000   34.43600  1.000 35.63185  ? 524 HOH A O    1 
HETATM 9500 O O    . HOH L 7 .   ? 4.38800   2.09700   37.78400  1.000 46.91101  ? 525 HOH A O    1 
HETATM 9501 O O    . HOH L 7 .   ? 19.89900  4.22700   32.02200  1.000 53.01276  ? 526 HOH A O    1 
HETATM 9502 O O    . HOH L 7 .   ? -12.53700 3.66200   18.27800  1.000 30.50485  ? 527 HOH A O    1 
HETATM 9503 O O    . HOH L 7 .   ? -39.14000 -9.92600  27.68500  1.000 46.92035  ? 528 HOH A O    1 
HETATM 9504 O O    . HOH L 7 .   ? -16.08500 -14.34900 10.33000  1.000 32.07382  ? 529 HOH A O    1 
HETATM 9505 O O    . HOH L 7 .   ? -2.11100  -12.54600 34.33400  1.000 37.78325  ? 530 HOH A O    1 
HETATM 9506 O O    . HOH L 7 .   ? 2.99800   -0.03600  28.95400  1.000 38.01766  ? 531 HOH A O    1 
HETATM 9507 O O    . HOH L 7 .   ? -37.20300 -0.52700  19.79100  1.000 50.25566  ? 532 HOH A O    1 
HETATM 9508 O O    . HOH L 7 .   ? -17.76200 -6.08400  10.14900  1.000 41.40084  ? 533 HOH A O    1 
HETATM 9509 O O    . HOH L 7 .   ? -18.28900 -6.07600  39.03600  1.000 36.65230  ? 534 HOH A O    1 
HETATM 9510 O O    . HOH L 7 .   ? -3.73700  -19.61500 23.48800  1.000 35.08212  ? 535 HOH A O    1 
HETATM 9511 O O    . HOH L 7 .   ? -27.02500 -19.71000 8.07000   1.000 46.28767  ? 536 HOH A O    1 
HETATM 9512 O O    . HOH L 7 .   ? -16.69500 -16.02400 32.34900  1.000 43.21911  ? 537 HOH A O    1 
HETATM 9513 O O    . HOH L 7 .   ? -23.54200 -18.45600 20.05400  1.000 38.80453  ? 538 HOH A O    1 
HETATM 9514 O O    . HOH L 7 .   ? -0.31500  -14.01600 27.27900  1.000 32.40466  ? 539 HOH A O    1 
HETATM 9515 O O    . HOH L 7 .   ? -0.60100  -11.65700 21.14400  1.000 32.02777  ? 540 HOH A O    1 
HETATM 9516 O O    . HOH L 7 .   ? -22.69400 2.08400   17.18600  1.000 30.29805  ? 541 HOH A O    1 
HETATM 9517 O O    . HOH L 7 .   ? 14.24700  7.49000   30.95800  1.000 60.31961  ? 542 HOH A O    1 
HETATM 9518 O O    . HOH L 7 .   ? -15.56300 -5.88300  17.82500  1.000 25.85309  ? 543 HOH A O    1 
HETATM 9519 O O    . HOH L 7 .   ? 5.01500   -21.36900 40.97000  1.000 54.78439  ? 544 HOH A O    1 
HETATM 9520 O O    . HOH L 7 .   ? -2.71700  -10.53900 22.64300  1.000 26.95083  ? 545 HOH A O    1 
HETATM 9521 O O    . HOH L 7 .   ? 1.06200   -0.05100  25.94100  1.000 41.01980  ? 546 HOH A O    1 
HETATM 9522 O O    . HOH L 7 .   ? 7.92000   -10.93000 14.21900  1.000 40.61545  ? 547 HOH A O    1 
HETATM 9523 O O    . HOH L 7 .   ? -10.37300 -0.63100  39.76900  1.000 36.91738  ? 548 HOH A O    1 
HETATM 9524 O O    . HOH L 7 .   ? 1.07300   -10.02000 41.02600  1.000 38.10423  ? 549 HOH A O    1 
HETATM 9525 O O    . HOH L 7 .   ? 17.53800  -4.81100  46.13800  1.000 48.95230  ? 550 HOH A O    1 
HETATM 9526 O O    . HOH L 7 .   ? -29.63000 5.58800   17.63900  1.000 51.69379  ? 551 HOH A O    1 
HETATM 9527 O O    . HOH L 7 .   ? 0.97900   -15.07200 39.70800  1.000 37.17116  ? 552 HOH A O    1 
HETATM 9528 O O    . HOH L 7 .   ? 18.76100  -9.26200  46.84900  1.000 42.52031  ? 553 HOH A O    1 
HETATM 9529 O O    . HOH L 7 .   ? 2.15300   -2.40900  43.63600  1.000 50.25056  ? 554 HOH A O    1 
HETATM 9530 O O    . HOH L 7 .   ? 11.54400  4.96800   37.14600  1.000 49.06672  ? 555 HOH A O    1 
HETATM 9531 O O    . HOH L 7 .   ? 22.74300  -11.62700 24.24400  1.000 48.00631  ? 556 HOH A O    1 
HETATM 9532 O O    . HOH L 7 .   ? -38.13300 -14.52600 9.85300   1.000 69.42804  ? 557 HOH A O    1 
HETATM 9533 O O    . HOH L 7 .   ? -14.21100 10.03900  30.22000  1.000 43.48645  ? 558 HOH A O    1 
HETATM 9534 O O    . HOH L 7 .   ? -7.60900  5.30800   35.40700  1.000 43.63694  ? 559 HOH A O    1 
HETATM 9535 O O    . HOH L 7 .   ? 9.15400   -17.36100 28.98400  1.000 40.19503  ? 560 HOH A O    1 
HETATM 9536 O O    . HOH L 7 .   ? -17.91000 -9.63300  37.75800  1.000 40.04635  ? 561 HOH A O    1 
HETATM 9537 O O    . HOH L 7 .   ? -7.12000  -15.52100 11.71800  1.000 36.40522  ? 562 HOH A O    1 
HETATM 9538 O O    . HOH L 7 .   ? 10.93800  -9.97700  15.56500  1.000 44.33724  ? 563 HOH A O    1 
HETATM 9539 O O    . HOH L 7 .   ? 15.61900  -11.58100 50.38500  1.000 44.98088  ? 564 HOH A O    1 
HETATM 9540 O O    . HOH L 7 .   ? 0.65900   -7.61600  23.08000  1.000 28.97396  ? 565 HOH A O    1 
HETATM 9541 O O    . HOH L 7 .   ? 12.37400  -17.14500 42.45700  1.000 46.00003  ? 566 HOH A O    1 
HETATM 9542 O O    . HOH L 7 .   ? 20.38100  -4.15600  40.41500  1.000 44.70487  ? 567 HOH A O    1 
HETATM 9543 O O    . HOH L 7 .   ? -28.85200 -1.58800  37.66600  1.000 38.41756  ? 568 HOH A O    1 
HETATM 9544 O O    . HOH L 7 .   ? 11.52000  -21.05100 37.79100  1.000 46.56005  ? 569 HOH A O    1 
HETATM 9545 O O    . HOH L 7 .   ? 23.36100  -13.73700 28.02000  1.000 49.98080  ? 570 HOH A O    1 
HETATM 9546 O O    . HOH L 7 .   ? -3.26600  -1.80800  40.49000  1.000 39.38734  ? 571 HOH A O    1 
HETATM 9547 O O    . HOH L 7 .   ? -4.85600  -1.53400  28.39800  1.000 24.84738  ? 572 HOH A O    1 
HETATM 9548 O O    . HOH L 7 .   ? 8.13100   -11.73800 47.13400  1.000 45.40208  ? 573 HOH A O    1 
HETATM 9549 O O    . HOH L 7 .   ? 9.58600   -18.47900 45.31400  1.000 55.80500  ? 574 HOH A O    1 
HETATM 9550 O O    . HOH L 7 .   ? 16.10900  -18.05800 35.73200  1.000 49.61803  ? 575 HOH A O    1 
HETATM 9551 O O    . HOH L 7 .   ? 5.60800   -5.64700  28.11200  1.000 23.90968  ? 576 HOH A O    1 
HETATM 9552 O O    . HOH L 7 .   ? -28.67900 -10.18300 34.63900  1.000 40.01213  ? 577 HOH A O    1 
HETATM 9553 O O    . HOH L 7 .   ? -22.56400 -15.93800 27.07300  1.000 35.55275  ? 578 HOH A O    1 
HETATM 9554 O O    . HOH L 7 .   ? -4.87800  -7.09200  39.88200  1.000 34.59081  ? 579 HOH A O    1 
HETATM 9555 O O    . HOH L 7 .   ? 21.58700  -14.12400 24.68800  1.000 58.16492  ? 580 HOH A O    1 
HETATM 9556 O O    . HOH L 7 .   ? 1.01700   -11.37200 31.99400  1.000 29.28480  ? 581 HOH A O    1 
HETATM 9557 O O    . HOH L 7 .   ? -26.36900 -2.25700  36.77600  1.000 35.25065  ? 582 HOH A O    1 
HETATM 9558 O O    . HOH L 7 .   ? -11.17500 6.59800   19.47000  1.000 26.87497  ? 583 HOH A O    1 
HETATM 9559 O O    . HOH L 7 .   ? -33.27700 1.54800   24.59900  1.000 41.90340  ? 584 HOH A O    1 
HETATM 9560 O O    . HOH L 7 .   ? -33.56900 4.23400   23.48900  1.000 48.84624  ? 585 HOH A O    1 
HETATM 9561 O O    . HOH L 7 .   ? -6.60100  -17.59300 21.28900  1.000 37.29160  ? 586 HOH A O    1 
HETATM 9562 O O    . HOH L 7 .   ? -33.60700 -6.85300  5.59600   1.000 56.87227  ? 587 HOH A O    1 
HETATM 9563 O O    . HOH L 7 .   ? 14.63200  -15.30400 45.76300  1.000 44.81741  ? 588 HOH A O    1 
HETATM 9564 O O    . HOH L 7 .   ? 20.66500  0.84600   43.40000  1.000 42.76450  ? 589 HOH A O    1 
HETATM 9565 O O    . HOH L 7 .   ? -23.22900 -17.25700 33.79100  1.000 57.01465  ? 590 HOH A O    1 
HETATM 9566 O O    . HOH L 7 .   ? -29.76200 -1.74400  14.25900  1.000 40.78381  ? 591 HOH A O    1 
HETATM 9567 O O    . HOH L 7 .   ? 16.54000  -4.90300  20.93000  1.000 43.15125  ? 592 HOH A O    1 
HETATM 9568 O O    . HOH L 7 .   ? -15.46600 -14.20700 27.75000  1.000 31.28712  ? 593 HOH A O    1 
HETATM 9569 O O    . HOH L 7 .   ? -12.95900 -8.87000  38.33400  1.000 38.28248  ? 594 HOH A O    1 
HETATM 9570 O O    . HOH L 7 .   ? 15.48100  1.02900   41.95900  1.000 42.89834  ? 595 HOH A O    1 
HETATM 9571 O O    . HOH L 7 .   ? -29.71500 0.77400   41.53900  1.000 33.68694  ? 596 HOH A O    1 
HETATM 9572 O O    . HOH L 7 .   ? -24.69600 -3.13500  29.73200  1.000 26.73539  ? 597 HOH A O    1 
HETATM 9573 O O    . HOH L 7 .   ? -0.11800  -17.06200 18.97900  1.000 46.00914  ? 598 HOH A O    1 
HETATM 9574 O O    . HOH L 7 .   ? -6.54700  -20.61800 22.68200  1.000 41.15887  ? 599 HOH A O    1 
HETATM 9575 O O    . HOH L 7 .   ? -20.99400 -8.05700  36.27000  1.000 30.58121  ? 600 HOH A O    1 
HETATM 9576 O O    . HOH L 7 .   ? 16.03200  9.41100   29.42500  1.000 61.84093  ? 601 HOH A O    1 
HETATM 9577 O O    . HOH L 7 .   ? -11.64700 6.57000   36.74700  1.000 32.97065  ? 602 HOH A O    1 
HETATM 9578 O O    . HOH L 7 .   ? 14.87300  -12.31400 12.83400  1.000 50.11134  ? 603 HOH A O    1 
HETATM 9579 O O    . HOH L 7 .   ? -17.81700 -22.42200 15.34300  1.000 46.30138  ? 604 HOH A O    1 
HETATM 9580 O O    . HOH L 7 .   ? 1.56400   -7.89300  20.37400  1.000 28.98374  ? 605 HOH A O    1 
HETATM 9581 O O    . HOH L 7 .   ? -35.72100 0.74800   35.10900  1.000 45.02092  ? 606 HOH A O    1 
HETATM 9582 O O    . HOH L 7 .   ? -10.15300 -12.10100 36.16100  1.000 39.44138  ? 607 HOH A O    1 
HETATM 9583 O O    . HOH L 7 .   ? -20.81000 -16.52900 34.41100  1.000 46.87656  ? 608 HOH A O    1 
HETATM 9584 O O    . HOH L 7 .   ? -22.29600 -19.08100 29.57000  1.000 50.51659  ? 609 HOH A O    1 
HETATM 9585 O O    . HOH L 7 .   ? 24.65400  -12.53400 30.33100  1.000 52.32634  ? 610 HOH A O    1 
HETATM 9586 O O    . HOH L 7 .   ? -5.53300  4.60800   24.81100  1.000 35.68701  ? 611 HOH A O    1 
HETATM 9587 O O    . HOH L 7 .   ? 13.03900  -14.11100 47.99700  1.000 42.30208  ? 612 HOH A O    1 
HETATM 9588 O O    . HOH L 7 .   ? -3.84300  5.07600   38.08100  1.000 43.73231  ? 613 HOH A O    1 
HETATM 9589 O O    . HOH L 7 .   ? -22.76900 -5.51200  9.87000   1.000 52.45639  ? 614 HOH A O    1 
HETATM 9590 O O    . HOH L 7 .   ? -7.93500  4.79900   27.49700  1.000 27.84762  ? 615 HOH A O    1 
HETATM 9591 O O    . HOH L 7 .   ? 8.62900   -1.60100  22.49500  1.000 36.96217  ? 616 HOH A O    1 
HETATM 9592 O O    . HOH L 7 .   ? 21.67800  -10.12800 22.67100  1.000 47.29331  ? 617 HOH A O    1 
HETATM 9593 O O    . HOH L 7 .   ? -21.40100 -5.70500  37.56600  1.000 30.68368  ? 618 HOH A O    1 
HETATM 9594 O O    . HOH L 7 .   ? -13.80400 -3.63100  33.18700  1.000 26.35965  ? 619 HOH A O    1 
HETATM 9595 O O    . HOH L 7 .   ? -16.57100 -21.10800 25.41800  1.000 38.63584  ? 620 HOH A O    1 
HETATM 9596 O O    . HOH L 7 .   ? -43.32900 -4.24900  23.78800  1.000 63.26465  ? 621 HOH A O    1 
HETATM 9597 O O    . HOH L 7 .   ? -16.31800 -19.25400 29.36000  1.000 49.58710  ? 622 HOH A O    1 
HETATM 9598 O O    . HOH L 7 .   ? 8.94200   3.53400   32.48000  1.000 40.08649  ? 623 HOH A O    1 
HETATM 9599 O O    . HOH L 7 .   ? 12.04300  -19.96600 35.67000  1.000 46.57584  ? 624 HOH A O    1 
HETATM 9600 O O    . HOH L 7 .   ? -14.33100 -10.89100 7.36600   1.000 42.19936  ? 625 HOH A O    1 
HETATM 9601 O O    . HOH L 7 .   ? -42.03100 -10.79300 21.56600  1.000 52.20971  ? 626 HOH A O    1 
HETATM 9602 O O    . HOH L 7 .   ? -18.76900 -2.61600  7.40400   1.000 55.96114  ? 627 HOH A O    1 
HETATM 9603 O O    . HOH L 7 .   ? -23.61000 -4.47200  36.66500  1.000 29.15107  ? 628 HOH A O    1 
HETATM 9604 O O    . HOH L 7 .   ? -6.90600  2.26500   44.58700  1.000 44.77069  ? 629 HOH A O    1 
HETATM 9605 O O    . HOH L 7 .   ? -8.70200  -14.18500 24.55500  1.000 29.78026  ? 630 HOH A O    1 
HETATM 9606 O O    . HOH L 7 .   ? -1.38300  -5.13600  24.45700  1.000 38.34515  ? 631 HOH A O    1 
HETATM 9607 O O    . HOH L 7 .   ? -15.52500 -5.50600  7.55500   1.000 44.71518  ? 632 HOH A O    1 
HETATM 9608 O O    . HOH L 7 .   ? -31.79000 6.43000   35.94500  1.000 48.89813  ? 633 HOH A O    1 
HETATM 9609 O O    . HOH L 7 .   ? 16.50200  -6.74100  52.35700  1.000 48.29702  ? 634 HOH A O    1 
HETATM 9610 O O    . HOH L 7 .   ? -26.64600 9.65200   33.73900  1.000 46.46980  ? 635 HOH A O    1 
HETATM 9611 O O    . HOH L 7 .   ? -12.92400 -18.65100 31.26800  1.000 35.32954  ? 636 HOH A O    1 
HETATM 9612 O O    . HOH L 7 .   ? 17.55700  1.84900   43.70800  1.000 47.14790  ? 637 HOH A O    1 
HETATM 9613 O O    . HOH L 7 .   ? -33.75300 -13.09200 30.62800  1.000 40.55124  ? 638 HOH A O    1 
HETATM 9614 O O    . HOH L 7 .   ? -15.81900 3.55800   42.51900  1.000 44.31170  ? 639 HOH A O    1 
HETATM 9615 O O    . HOH L 7 .   ? -23.90000 10.38300  35.19000  1.000 48.62805  ? 640 HOH A O    1 
HETATM 9616 O O    . HOH L 7 .   ? -30.90100 -4.43500  37.03900  1.000 37.72537  ? 641 HOH A O    1 
HETATM 9617 O O    . HOH L 7 .   ? 3.63900   -9.05700  37.57100  1.000 29.14138  ? 642 HOH A O    1 
HETATM 9618 O O    . HOH L 7 .   ? -23.08100 4.76800   16.42100  1.000 42.75918  ? 643 HOH A O    1 
HETATM 9619 O O    . HOH L 7 .   ? -28.25500 -13.77800 34.53900  1.000 43.68430  ? 644 HOH A O    1 
HETATM 9620 O O    . HOH L 7 .   ? -6.77500  -4.15700  41.60600  1.000 52.64597  ? 645 HOH A O    1 
HETATM 9621 O O    . HOH L 7 .   ? 3.10300   -10.30600 19.95700  1.000 37.74422  ? 646 HOH A O    1 
HETATM 9622 O O    . HOH L 7 .   ? 7.23500   -17.32200 27.04900  1.000 42.61774  ? 647 HOH A O    1 
HETATM 9623 O O    . HOH L 7 .   ? 16.23300  -16.76300 38.46800  1.000 41.04954  ? 648 HOH A O    1 
HETATM 9624 O O    . HOH L 7 .   ? 7.11800   -1.92400  20.33900  1.000 45.41660  ? 649 HOH A O    1 
HETATM 9625 O O    . HOH L 7 .   ? -3.34100  -5.87000  41.90400  1.000 42.74282  ? 650 HOH A O    1 
HETATM 9626 O O    . HOH L 7 .   ? -23.00300 -2.64500  9.76000   1.000 61.85519  ? 651 HOH A O    1 
HETATM 9627 O O    . HOH L 7 .   ? -12.29500 -11.95300 37.97800  1.000 44.56202  ? 652 HOH A O    1 
HETATM 9628 O O    . HOH L 7 .   ? 18.67900  -6.04700  47.86100  1.000 46.15657  ? 653 HOH A O    1 
HETATM 9629 O O    . HOH L 7 .   ? -2.70700  -2.81200  15.34700  1.000 35.05794  ? 654 HOH A O    1 
HETATM 9630 O O    . HOH L 7 .   ? -17.31000 10.10000  22.11300  1.000 39.05914  ? 655 HOH A O    1 
HETATM 9631 O O    . HOH L 7 .   ? -12.31500 -20.55300 12.24700  1.000 45.82921  ? 656 HOH A O    1 
HETATM 9632 O O    . HOH L 7 .   ? 21.28800  1.99200   33.78400  1.000 49.29109  ? 657 HOH A O    1 
HETATM 9633 O O    . HOH L 7 .   ? 2.92200   -18.04200 42.50200  1.000 45.20717  ? 658 HOH A O    1 
HETATM 9634 O O    . HOH L 7 .   ? 2.33600   -15.35500 29.20400  1.000 35.89951  ? 659 HOH A O    1 
HETATM 9635 O O    . HOH L 7 .   ? -20.58400 4.40400   11.22400  1.000 57.10870  ? 660 HOH A O    1 
HETATM 9636 O O    . HOH L 7 .   ? -25.44400 -2.21700  40.93600  1.000 33.77320  ? 661 HOH A O    1 
HETATM 9637 O O    . HOH L 7 .   ? -36.09900 -12.38600 28.75000  1.000 47.07980  ? 662 HOH A O    1 
HETATM 9638 O O    . HOH L 7 .   ? 16.72100  9.30800   32.55200  1.000 65.96900  ? 663 HOH A O    1 
HETATM 9639 O O    . HOH L 7 .   ? 19.62500  -5.91000  42.47900  1.000 52.98197  ? 664 HOH A O    1 
HETATM 9640 O O    . HOH L 7 .   ? 3.86500   -0.45900  17.61600  1.000 36.52634  ? 665 HOH A O    1 
HETATM 9641 O O    . HOH L 7 .   ? 6.24100   -13.44700 45.72000  1.000 48.10849  ? 666 HOH A O    1 
HETATM 9642 O O    . HOH L 7 .   ? -5.58100  -15.00700 31.21700  1.000 17.10974  ? 667 HOH A O    1 
HETATM 9643 O O    . HOH L 7 .   ? -21.56700 -5.40100  7.58200   1.000 58.86844  ? 668 HOH A O    1 
HETATM 9644 O O    . HOH L 7 .   ? -25.06600 -1.83200  9.42100   1.000 59.23705  ? 669 HOH A O    1 
HETATM 9645 O O    . HOH L 7 .   ? -30.36300 2.82800   13.81800  1.000 64.21887  ? 670 HOH A O    1 
HETATM 9646 O O    . HOH L 7 .   ? -14.92600 -13.82200 8.02600   1.000 41.28269  ? 671 HOH A O    1 
HETATM 9647 O O    . HOH L 7 .   ? -43.31100 1.85800   35.34700  1.000 52.15843  ? 672 HOH A O    1 
HETATM 9648 O O    . HOH L 7 .   ? -0.86300  -13.00900 30.56500  1.000 35.09065  ? 673 HOH A O    1 
HETATM 9649 O O    . HOH L 7 .   ? -15.32300 -9.11900  39.39700  1.000 53.50318  ? 674 HOH A O    1 
HETATM 9650 O O    . HOH L 7 .   ? -37.51000 -8.70400  9.21700   1.000 70.95874  ? 675 HOH A O    1 
HETATM 9651 O O    . HOH L 7 .   ? -39.81800 -10.44200 11.12200  1.000 75.23376  ? 676 HOH A O    1 
HETATM 9652 O O    . HOH L 7 .   ? -16.02700 -16.33300 29.60700  1.000 35.86096  ? 677 HOH A O    1 
HETATM 9653 O O    . HOH L 7 .   ? -2.67800  -14.14400 32.35300  1.000 34.47831  ? 678 HOH A O    1 
HETATM 9654 O O    . HOH L 7 .   ? -4.69000  -3.09200  41.72300  1.000 49.38637  ? 679 HOH A O    1 
HETATM 9655 O O    . HOH L 7 .   ? 0.36900   -11.48600 34.35900  1.000 36.90940  ? 680 HOH A O    1 
HETATM 9656 O O    . HOH L 7 .   ? 4.59600   -11.82200 45.91400  1.000 56.76224  ? 681 HOH A O    1 
HETATM 9657 O O    . HOH L 7 .   ? -18.15300 3.38900   43.80700  1.000 49.57132  ? 682 HOH A O    1 
HETATM 9658 O O    . HOH L 7 .   ? -43.17200 -13.86600 20.44000  1.000 71.89257  ? 683 HOH A O    1 
HETATM 9659 O O    . HOH L 7 .   ? -16.55400 -13.80800 37.83600  1.000 51.99021  ? 684 HOH A O    1 
HETATM 9660 O O    . HOH L 7 .   ? 6.91700   -6.64100  49.05700  1.000 53.76065  ? 685 HOH A O    1 
HETATM 9661 O O    . HOH L 7 .   ? -0.25000  -12.69600 40.60100  1.000 43.05246  ? 686 HOH A O    1 
HETATM 9662 O O    . HOH L 7 .   ? -25.02400 -12.58200 6.51100   1.000 56.79843  ? 687 HOH A O    1 
HETATM 9663 O O    . HOH L 7 .   ? -28.41800 -1.73700  40.57200  1.000 39.50701  ? 688 HOH A O    1 
HETATM 9664 O O    . HOH L 7 .   ? -25.54300 -3.95200  38.60000  1.000 34.75093  ? 689 HOH A O    1 
HETATM 9665 O O    . HOH L 7 .   ? 25.49400  -14.55000 25.60700  1.000 61.71551  ? 690 HOH A O    1 
HETATM 9666 O O    . HOH L 7 .   ? -37.69700 -10.93900 29.94300  1.000 48.98988  ? 691 HOH A O    1 
HETATM 9667 O O    . HOH L 7 .   ? -17.47200 -23.39900 13.18300  1.000 55.06399  ? 692 HOH A O    1 
HETATM 9668 O O    . HOH L 7 .   ? -41.95900 -16.22000 20.56700  1.000 77.81346  ? 693 HOH A O    1 
HETATM 9669 O O    . HOH L 7 .   ? -25.49600 0.22600   8.05000   1.000 63.50898  ? 694 HOH A O    1 
HETATM 9670 O O    . HOH L 7 .   ? 19.39900  -14.12900 22.20400  1.000 51.56405  ? 695 HOH A O    1 
HETATM 9671 O O    . HOH L 7 .   ? -27.08200 -9.65300  37.04900  1.000 47.27276  ? 696 HOH A O    1 
HETATM 9672 O O    . HOH L 7 .   ? 13.19300  -16.98900 44.73900  1.000 51.16850  ? 697 HOH A O    1 
HETATM 9673 O O    . HOH L 7 .   ? -16.44200 -16.58200 35.20200  1.000 64.45796  ? 698 HOH A O    1 
HETATM 9674 O O    . HOH L 7 .   ? 25.66100  -12.34800 23.32700  1.000 55.45582  ? 699 HOH A O    1 
HETATM 9675 O O    . HOH L 7 .   ? 20.76600  -10.66200 47.31400  1.000 52.49756  ? 700 HOH A O    1 
HETATM 9676 O O    . HOH L 7 .   ? -15.02400 -18.08600 33.27200  1.000 49.57369  ? 701 HOH A O    1 
HETATM 9677 O O    . HOH L 7 .   ? 18.54700  -17.03100 39.61500  1.000 50.24635  ? 702 HOH A O    1 
HETATM 9678 O O    . HOH L 7 .   ? 5.09400   -7.90700  47.20000  1.000 54.36268  ? 703 HOH A O    1 
HETATM 9679 O O    . HOH L 7 .   ? 17.03600  -16.32500 45.57300  1.000 52.94169  ? 704 HOH A O    1 
HETATM 9680 O O    . HOH L 7 .   ? 2.12100   -13.91600 32.35300  1.000 42.34027  ? 705 HOH A O    1 
HETATM 9681 O O    . HOH L 7 .   ? 14.46600  -18.11400 40.46900  1.000 45.84636  ? 706 HOH A O    1 
HETATM 9682 O O    . HOH L 7 .   ? -34.57100 -11.01800 32.66500  1.000 49.99894  ? 707 HOH A O    1 
HETATM 9683 O O    . HOH L 7 .   ? -17.31900 -17.87200 37.01800  1.000 56.83488  ? 708 HOH A O    1 
HETATM 9684 O O    . HOH L 7 .   ? 16.75600  -18.82800 42.08300  1.000 57.50340  ? 709 HOH A O    1 
HETATM 9685 O O    . HOH M 7 .   ? 2.33100   28.02300  21.22700  1.000 43.24155  ? 501 HOH B O    1 
HETATM 9686 O O    . HOH M 7 .   ? 11.39700  -0.13800  -10.81900 1.000 42.77184  ? 502 HOH B O    1 
HETATM 9687 O O    . HOH M 7 .   ? 7.97300   32.75100  18.27700  1.000 56.59222  ? 503 HOH B O    1 
HETATM 9688 O O    . HOH M 7 .   ? -0.10900  -24.59600 -7.63500  1.000 52.10937  ? 504 HOH B O    1 
HETATM 9689 O O    . HOH M 7 .   ? 1.67700   -12.78600 -15.57000 1.000 47.54458  ? 505 HOH B O    1 
HETATM 9690 O O    . HOH M 7 .   ? -6.48100  29.14700  20.95400  1.000 50.05735  ? 506 HOH B O    1 
HETATM 9691 O O    . HOH M 7 .   ? 3.62600   2.79800   13.65700  1.000 36.96184  ? 507 HOH B O    1 
HETATM 9692 O O    . HOH M 7 .   ? 5.93900   -11.10200 12.13600  1.000 32.49216  ? 508 HOH B O    1 
HETATM 9693 O O    . HOH M 7 .   ? -11.61300 -11.20300 -11.16600 1.000 48.27645  ? 509 HOH B O    1 
HETATM 9694 O O    . HOH M 7 .   ? -2.62700  4.46500   7.73600   1.000 34.66642  ? 510 HOH B O    1 
HETATM 9695 O O    . HOH M 7 .   ? -7.51900  -17.10300 -15.29600 1.000 42.44425  ? 511 HOH B O    1 
HETATM 9696 O O    . HOH M 7 .   ? -12.48900 12.41100  19.64400  1.000 41.44815  ? 512 HOH B O    1 
HETATM 9697 O O    . HOH M 7 .   ? -2.97400  8.51600   6.48700   1.000 37.46435  ? 513 HOH B O    1 
HETATM 9698 O O    . HOH M 7 .   ? 14.94900  2.47100   -5.66400  1.000 52.67924  ? 514 HOH B O    1 
HETATM 9699 O O    . HOH M 7 .   ? 6.32500   -18.30600 4.39100   1.000 35.86761  ? 515 HOH B O    1 
HETATM 9700 O O    . HOH M 7 .   ? 1.55200   -0.44600  -4.94300  1.000 33.40842  ? 516 HOH B O    1 
HETATM 9701 O O    . HOH M 7 .   ? 4.13100   2.09600   -8.55600  1.000 41.11150  ? 517 HOH B O    1 
HETATM 9702 O O    . HOH M 7 .   ? -5.57400  -16.29200 4.16700   1.000 50.29749  ? 518 HOH B O    1 
HETATM 9703 O O    . HOH M 7 .   ? -0.76400  5.22900   12.22600  1.000 30.46413  ? 519 HOH B O    1 
HETATM 9704 O O    . HOH M 7 .   ? -11.14100 -10.66200 0.98800   1.000 36.95314  ? 520 HOH B O    1 
HETATM 9705 O O    . HOH M 7 .   ? 1.84100   -5.12900  -10.56100 1.000 43.72782  ? 521 HOH B O    1 
HETATM 9706 O O    . HOH M 7 .   ? 2.78900   10.85400  14.84100  1.000 26.17256  ? 522 HOH B O    1 
HETATM 9707 O O    . HOH M 7 .   ? 20.99500  -1.06900  8.01600   1.000 44.77832  ? 523 HOH B O    1 
HETATM 9708 O O    . HOH M 7 .   ? 23.00100  8.53800   5.71600   1.000 55.70029  ? 524 HOH B O    1 
HETATM 9709 O O    . HOH M 7 .   ? 12.36500  -7.57800  -13.59300 1.000 41.91207  ? 525 HOH B O    1 
HETATM 9710 O O    . HOH M 7 .   ? -6.87400  -15.04400 8.44300   1.000 40.01130  ? 526 HOH B O    1 
HETATM 9711 O O    . HOH M 7 .   ? 11.94900  -0.24700  1.44300   1.000 34.15142  ? 527 HOH B O    1 
HETATM 9712 O O    . HOH M 7 .   ? 7.69500   7.53800   -2.53800  1.000 41.65343  ? 528 HOH B O    1 
HETATM 9713 O O    . HOH M 7 .   ? 2.48100   12.36100  6.72300   1.000 33.89177  ? 529 HOH B O    1 
HETATM 9714 O O    . HOH M 7 .   ? 12.42800  -3.04000  12.55700  1.000 39.79804  ? 530 HOH B O    1 
HETATM 9715 O O    . HOH M 7 .   ? 8.12500   2.31000   10.21000  1.000 30.46507  ? 531 HOH B O    1 
HETATM 9716 O O    . HOH M 7 .   ? -11.71000 16.53300  22.68100  1.000 54.96457  ? 532 HOH B O    1 
HETATM 9717 O O    . HOH M 7 .   ? -0.74100  5.68500   21.58700  1.000 40.37506  ? 533 HOH B O    1 
HETATM 9718 O O    . HOH M 7 .   ? -8.89800  -13.19200 11.41300  1.000 25.36531  ? 534 HOH B O    1 
HETATM 9719 O O    . HOH M 7 .   ? 15.85100  9.48000   2.07400   1.000 40.13341  ? 535 HOH B O    1 
HETATM 9720 O O    . HOH M 7 .   ? -10.46300 8.47300   21.52000  1.000 32.10015  ? 536 HOH B O    1 
HETATM 9721 O O    . HOH M 7 .   ? 3.19000   -0.54600  15.31100  1.000 59.99654  ? 537 HOH B O    1 
HETATM 9722 O O    . HOH M 7 .   ? 0.64100   11.04000  29.05000  1.000 43.50104  ? 538 HOH B O    1 
HETATM 9723 O O    . HOH M 7 .   ? 12.47400  -10.01800 -4.77800  1.000 35.52405  ? 539 HOH B O    1 
HETATM 9724 O O    . HOH M 7 .   ? 4.69000   6.58800   16.39600  1.000 39.67986  ? 540 HOH B O    1 
HETATM 9725 O O    . HOH M 7 .   ? -0.50000  -1.32900  15.16500  1.000 35.47362  ? 541 HOH B O    1 
HETATM 9726 O O    . HOH M 7 .   ? -11.09300 -5.55600  6.10700   1.000 36.80800  ? 542 HOH B O    1 
HETATM 9727 O O    . HOH M 7 .   ? -14.30400 10.55600  23.92700  1.000 36.98493  ? 543 HOH B O    1 
HETATM 9728 O O    . HOH M 7 .   ? -1.90000  -1.53700  18.87900  1.000 32.67905  ? 544 HOH B O    1 
HETATM 9729 O O    . HOH M 7 .   ? 7.90100   7.23800   16.25600  1.000 47.53376  ? 545 HOH B O    1 
HETATM 9730 O O    . HOH M 7 .   ? 12.36000  5.26800   -3.35800  1.000 36.71907  ? 546 HOH B O    1 
HETATM 9731 O O    . HOH M 7 .   ? 0.83600   -24.75000 -10.29200 1.000 54.80675  ? 547 HOH B O    1 
HETATM 9732 O O    . HOH M 7 .   ? -1.77000  0.28600   -11.03500 1.000 39.70425  ? 548 HOH B O    1 
HETATM 9733 O O    . HOH M 7 .   ? 0.93500   14.19300  30.57800  1.000 47.30920  ? 549 HOH B O    1 
HETATM 9734 O O    . HOH M 7 .   ? 12.52100  11.32900  2.41600   1.000 44.09692  ? 550 HOH B O    1 
HETATM 9735 O O    . HOH M 7 .   ? 2.80700   -23.50000 -1.82300  1.000 44.84811  ? 551 HOH B O    1 
HETATM 9736 O O    . HOH M 7 .   ? 12.45900  2.97200   -6.91100  1.000 48.32373  ? 552 HOH B O    1 
HETATM 9737 O O    . HOH M 7 .   ? 8.86700   17.54100  3.93700   1.000 52.08129  ? 553 HOH B O    1 
HETATM 9738 O O    . HOH M 7 .   ? 4.45100   -29.41100 -9.23600  1.000 49.72130  ? 554 HOH B O    1 
HETATM 9739 O O    . HOH M 7 .   ? -10.65400 -17.39000 -1.89900  1.000 51.51142  ? 555 HOH B O    1 
HETATM 9740 O O    . HOH M 7 .   ? -5.35000  5.95700   13.97800  1.000 33.43502  ? 556 HOH B O    1 
HETATM 9741 O O    . HOH M 7 .   ? -18.33500 5.78300   11.09600  1.000 47.43088  ? 557 HOH B O    1 
HETATM 9742 O O    . HOH M 7 .   ? -3.08400  4.49400   13.80700  1.000 25.07083  ? 558 HOH B O    1 
HETATM 9743 O O    . HOH M 7 .   ? 11.21400  -16.92200 2.15200   1.000 50.19173  ? 559 HOH B O    1 
HETATM 9744 O O    . HOH M 7 .   ? 11.49000  12.24600  20.83700  1.000 45.65907  ? 560 HOH B O    1 
HETATM 9745 O O    . HOH M 7 .   ? 15.80600  3.03400   9.47400   1.000 45.21825  ? 561 HOH B O    1 
HETATM 9746 O O    . HOH M 7 .   ? 24.24800  -13.77800 -4.68000  1.000 70.97435  ? 562 HOH B O    1 
HETATM 9747 O O    . HOH M 7 .   ? -14.29100 -4.51200  -1.13900  1.000 39.92887  ? 563 HOH B O    1 
HETATM 9748 O O    . HOH M 7 .   ? 9.90200   6.81200   -3.97000  1.000 45.15982  ? 564 HOH B O    1 
HETATM 9749 O O    . HOH M 7 .   ? 1.28800   7.84700   21.90700  1.000 37.17921  ? 565 HOH B O    1 
HETATM 9750 O O    . HOH M 7 .   ? -11.80000 4.83300   16.04700  1.000 31.36394  ? 566 HOH B O    1 
HETATM 9751 O O    . HOH M 7 .   ? -15.17200 -6.99400  4.47900   1.000 54.78672  ? 567 HOH B O    1 
HETATM 9752 O O    . HOH M 7 .   ? -2.04000  2.62000   0.67600   1.000 31.05395  ? 568 HOH B O    1 
HETATM 9753 O O    . HOH M 7 .   ? -17.43900 6.23600   8.76800   1.000 42.83847  ? 569 HOH B O    1 
HETATM 9754 O O    . HOH M 7 .   ? 7.01900   16.77900  7.83100   1.000 38.15970  ? 570 HOH B O    1 
HETATM 9755 O O    . HOH M 7 .   ? 9.68800   -5.10800  -15.54900 1.000 43.27346  ? 571 HOH B O    1 
HETATM 9756 O O    . HOH M 7 .   ? 3.68600   -17.48900 -19.05500 1.000 51.91960  ? 572 HOH B O    1 
HETATM 9757 O O    . HOH M 7 .   ? 14.09300  22.54400  7.27900   1.000 61.28273  ? 573 HOH B O    1 
HETATM 9758 O O    . HOH M 7 .   ? 13.80200  -22.53800 -7.50900  1.000 61.41492  ? 574 HOH B O    1 
HETATM 9759 O O    . HOH M 7 .   ? -10.49800 0.50000   -7.14900  1.000 42.13970  ? 575 HOH B O    1 
HETATM 9760 O O    . HOH M 7 .   ? -10.89000 -4.01600  -7.64700  1.000 34.38580  ? 576 HOH B O    1 
HETATM 9761 O O    . HOH M 7 .   ? -12.69200 -0.98500  -8.44900  1.000 51.57437  ? 577 HOH B O    1 
HETATM 9762 O O    . HOH M 7 .   ? 8.13300   6.20000   24.85600  1.000 33.54357  ? 578 HOH B O    1 
HETATM 9763 O O    . HOH M 7 .   ? 22.00000  0.93900   0.98900   1.000 47.94279  ? 579 HOH B O    1 
HETATM 9764 O O    . HOH M 7 .   ? -2.81000  12.55300  6.21900   1.000 35.51704  ? 580 HOH B O    1 
HETATM 9765 O O    . HOH M 7 .   ? 16.48400  -4.80700  -7.25300  1.000 45.30521  ? 581 HOH B O    1 
HETATM 9766 O O    . HOH M 7 .   ? -16.89800 -4.13800  6.12800   1.000 62.03208  ? 582 HOH B O    1 
HETATM 9767 O O    . HOH M 7 .   ? 14.12100  -14.79300 11.62200  1.000 46.58273  ? 583 HOH B O    1 
HETATM 9768 O O    . HOH M 7 .   ? -0.65800  1.21200   21.13500  1.000 26.05446  ? 584 HOH B O    1 
HETATM 9769 O O    . HOH M 7 .   ? 12.21800  5.45200   -6.09200  1.000 51.03532  ? 585 HOH B O    1 
HETATM 9770 O O    . HOH M 7 .   ? 6.36600   4.31500   16.06800  1.000 47.32562  ? 586 HOH B O    1 
HETATM 9771 O O    . HOH M 7 .   ? 1.06700   -3.99000  -14.84800 1.000 59.13723  ? 587 HOH B O    1 
HETATM 9772 O O    . HOH M 7 .   ? 4.94900   13.35700  5.30900   1.000 43.92586  ? 588 HOH B O    1 
HETATM 9773 O O    . HOH M 7 .   ? 13.11700  -13.99900 -0.04500  1.000 48.39888  ? 589 HOH B O    1 
HETATM 9774 O O    . HOH M 7 .   ? 0.06900   -5.41900  -12.36700 1.000 44.36876  ? 590 HOH B O    1 
HETATM 9775 O O    . HOH M 7 .   ? 5.37700   4.36300   24.82300  1.000 61.31142  ? 591 HOH B O    1 
HETATM 9776 O O    . HOH M 7 .   ? -9.48500  -23.88500 2.77800   1.000 63.53759  ? 592 HOH B O    1 
HETATM 9777 O O    . HOH M 7 .   ? -16.20100 12.09300  17.93200  1.000 59.56613  ? 593 HOH B O    1 
HETATM 9778 O O    . HOH M 7 .   ? 14.63500  -12.28600 -0.33800  1.000 55.27667  ? 594 HOH B O    1 
HETATM 9779 O O    . HOH M 7 .   ? -3.50900  10.60500  4.33900   1.000 50.22624  ? 595 HOH B O    1 
HETATM 9780 O O    . HOH M 7 .   ? 12.61200  8.52300   14.57700  1.000 51.41204  ? 596 HOH B O    1 
HETATM 9781 O O    . HOH M 7 .   ? -10.18900 10.88200  21.13700  1.000 41.14930  ? 597 HOH B O    1 
HETATM 9782 O O    . HOH M 7 .   ? 5.25900   20.27000  -0.62100  1.000 53.13808  ? 598 HOH B O    1 
HETATM 9783 O O    . HOH M 7 .   ? 1.79000   1.23100   -7.36300  1.000 38.19931  ? 599 HOH B O    1 
HETATM 9784 O O    . HOH M 7 .   ? -3.17100  4.96500   0.01000   1.000 42.33668  ? 600 HOH B O    1 
HETATM 9785 O O    . HOH M 7 .   ? 11.32100  -6.87200  -16.05200 1.000 51.42290  ? 601 HOH B O    1 
HETATM 9786 O O    . HOH M 7 .   ? 7.26400   14.66800  5.99500   1.000 44.51745  ? 602 HOH B O    1 
HETATM 9787 O O    . HOH M 7 .   ? 14.98300  -17.39100 -0.38700  1.000 62.20223  ? 603 HOH B O    1 
HETATM 9788 O O    . HOH M 7 .   ? -7.14400  -16.41300 6.52600   1.000 54.55389  ? 604 HOH B O    1 
HETATM 9789 O O    . HOH M 7 .   ? 14.70700  8.94000   13.79200  1.000 52.70158  ? 605 HOH B O    1 
HETATM 9790 O O    . HOH M 7 .   ? -9.94200  2.74200   -8.06700  1.000 51.98012  ? 606 HOH B O    1 
HETATM 9791 O O    . HOH M 7 .   ? -0.28000  13.06900  5.56400   1.000 52.82621  ? 607 HOH B O    1 
HETATM 9792 O O    . HOH M 7 .   ? 10.47400  7.90800   -6.66200  1.000 63.42638  ? 608 HOH B O    1 
HETATM 9793 O O    . HOH M 7 .   ? 23.34200  7.11100   3.35600   1.000 57.46818  ? 609 HOH B O    1 
HETATM 9794 O O    . HOH M 7 .   ? 16.56300  -10.81100 -0.52400  1.000 53.11785  ? 610 HOH B O    1 
HETATM 9795 O O    . HOH M 7 .   ? 22.48500  -19.03100 -5.17000  1.000 70.31417  ? 611 HOH B O    1 
HETATM 9796 O O    . HOH N 7 .   ? -17.14400 9.12200   31.04900  1.000 58.75691  ? 101 HOH C O    1 
HETATM 9797 O O    . HOH N 7 .   ? -20.89600 9.54200   36.89600  1.000 57.09785  ? 102 HOH C O    1 
HETATM 9798 O O    . HOH N 7 .   ? -22.28900 10.20400  32.91900  1.000 51.51031  ? 103 HOH C O    1 
HETATM 9799 O O    . HOH N 7 .   ? -27.48900 3.15500   26.63500  1.000 40.67542  ? 104 HOH C O    1 
HETATM 9800 O O    . HOH N 7 .   ? -17.72500 9.43300   38.03500  1.000 60.76082  ? 105 HOH C O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 1   ? 0.44398 0.60530 0.52880 0.06992  0.03364  -0.00088 1   SER A N   
2    C CA  . SER A 1   ? 0.43402 0.61247 0.52767 0.05897  0.03010  0.00105  1   SER A CA  
3    C C   . SER A 1   ? 0.42157 0.58177 0.51288 0.04368  0.02767  -0.00004 1   SER A C   
4    O O   . SER A 1   ? 0.33819 0.47894 0.42286 0.04126  0.02907  -0.00183 1   SER A O   
5    C CB  . SER A 1   ? 0.53604 0.75023 0.63908 0.05644  0.03231  0.00265  1   SER A CB  
6    O OG  . SER A 1   ? 0.54108 0.77134 0.65136 0.04254  0.02937  0.00381  1   SER A OG  
14   N N   . GLY A 2   ? 0.34192 0.50880 0.43788 0.03404  0.02412  0.00095  2   GLY A N   
15   C CA  . GLY A 2   ? 0.40866 0.55830 0.50161 0.02112  0.02177  0.00007  2   GLY A CA  
16   C C   . GLY A 2   ? 0.35517 0.48625 0.44459 0.02344  0.01827  -0.00056 2   GLY A C   
17   O O   . GLY A 2   ? 0.38222 0.50785 0.46932 0.03469  0.01814  -0.00043 2   GLY A O   
21   N N   . PHE A 3   ? 0.34478 0.46482 0.43257 0.01280  0.01573  -0.00120 3   PHE A N   
22   C CA  . PHE A 3   ? 0.37011 0.47379 0.45458 0.01452  0.01270  -0.00187 3   PHE A CA  
23   C C   . PHE A 3   ? 0.43087 0.51648 0.51084 0.00463  0.01148  -0.00325 3   PHE A C   
24   O O   . PHE A 3   ? 0.43527 0.52567 0.51618 -0.00570 0.01079  -0.00310 3   PHE A O   
25   C CB  . PHE A 3   ? 0.37015 0.48954 0.45940 0.01517  0.00982  -0.00053 3   PHE A CB  
26   C CG  . PHE A 3   ? 0.34009 0.44516 0.42533 0.02157  0.00771  -0.00048 3   PHE A CG  
27   C CD1 . PHE A 3   ? 0.37493 0.47485 0.45692 0.03448  0.00914  0.00037  3   PHE A CD1 
28   C CD2 . PHE A 3   ? 0.37334 0.46762 0.45637 0.01448  0.00483  -0.00141 3   PHE A CD2 
29   C CE1 . PHE A 3   ? 0.41547 0.49990 0.49200 0.03945  0.00777  0.00069  3   PHE A CE1 
30   C CE2 . PHE A 3   ? 0.40146 0.48285 0.48031 0.01982  0.00329  -0.00120 3   PHE A CE2 
31   C CZ  . PHE A 3   ? 0.42080 0.49666 0.49618 0.03189  0.00484  0.00001  3   PHE A CZ  
41   N N   . ARG A 4   ? 0.31467 0.37967 0.38890 0.00781  0.01148  -0.00466 4   ARG A N   
42   C CA  . ARG A 4   ? 0.36206 0.41078 0.43161 0.00112  0.01059  -0.00581 4   ARG A CA  
43   C C   . ARG A 4   ? 0.34619 0.38068 0.41274 0.00353  0.00845  -0.00702 4   ARG A C   
44   O O   . ARG A 4   ? 0.32336 0.35508 0.38915 0.01070  0.00854  -0.00720 4   ARG A O   
45   C CB  . ARG A 4   ? 0.40912 0.44974 0.47452 0.00203  0.01289  -0.00642 4   ARG A CB  
46   C CG  . ARG A 4   ? 0.39309 0.44503 0.45966 -0.00257 0.01542  -0.00502 4   ARG A CG  
47   C CD  . ARG A 4   ? 0.49517 0.54186 0.55897 -0.01303 0.01458  -0.00433 4   ARG A CD  
48   N NE  . ARG A 4   ? 0.54014 0.59063 0.60157 -0.01876 0.01736  -0.00283 4   ARG A NE  
49   C CZ  . ARG A 4   ? 0.52910 0.57030 0.58467 -0.02753 0.01768  -0.00189 4   ARG A CZ  
50   N NH1 . ARG A 4   ? 0.61150 0.63855 0.66286 -0.03057 0.01544  -0.00268 4   ARG A NH1 
51   N NH2 . ARG A 4   ? 0.49065 0.53604 0.54339 -0.03326 0.02070  -0.00005 4   ARG A NH2 
65   N N   . LYS A 5   ? 0.40743 0.43145 0.47094 -0.00228 0.00701  -0.00786 5   LYS A N   
66   C CA  . LYS A 5   ? 0.42653 0.43759 0.48689 -0.00040 0.00554  -0.00926 5   LYS A CA  
67   C C   . LYS A 5   ? 0.36028 0.36299 0.41736 0.00361  0.00699  -0.01044 5   LYS A C   
68   O O   . LYS A 5   ? 0.40866 0.40657 0.46299 0.00157  0.00757  -0.01084 5   LYS A O   
69   C CB  . LYS A 5   ? 0.47355 0.47690 0.53099 -0.00647 0.00412  -0.00995 5   LYS A CB  
70   C CG  . LYS A 5   ? 0.53317 0.53108 0.58956 -0.00613 0.00216  -0.01096 5   LYS A CG  
71   C CD  . LYS A 5   ? 0.49391 0.50218 0.55385 -0.00510 0.00098  -0.00997 5   LYS A CD  
72   C CE  . LYS A 5   ? 0.49603 0.50347 0.55470 -0.00899 -0.00117 -0.01068 5   LYS A CE  
73   N NZ  . LYS A 5   ? 0.50805 0.51222 0.56370 -0.01658 -0.00148 -0.01175 5   LYS A NZ  
87   N N   . MET A 6   ? 0.34480 0.34554 0.40101 0.00929  0.00774  -0.01096 6   MET A N   
88   C CA  . MET A 6   ? 0.35775 0.35184 0.40999 0.01228  0.00946  -0.01259 6   MET A CA  
89   C C   . MET A 6   ? 0.32973 0.31251 0.37812 0.01194  0.00857  -0.01454 6   MET A C   
90   O O   . MET A 6   ? 0.36669 0.34584 0.41401 0.01381  0.00822  -0.01434 6   MET A O   
91   C CB  . MET A 6   ? 0.35327 0.35139 0.40504 0.01890  0.01176  -0.01224 6   MET A CB  
92   C CG  . MET A 6   ? 0.45060 0.44055 0.49667 0.02174  0.01382  -0.01451 6   MET A CG  
93   S SD  . MET A 6   ? 0.50088 0.49496 0.54506 0.03114  0.01713  -0.01410 6   MET A SD  
94   C CE  . MET A 6   ? 0.47507 0.48919 0.52663 0.02950  0.01792  -0.01179 6   MET A CE  
104  N N   . ALA A 7   ? 0.28104 0.25940 0.32695 0.00954  0.00828  -0.01619 7   ALA A N   
105  C CA  . ALA A 7   ? 0.29075 0.26188 0.33343 0.00815  0.00761  -0.01841 7   ALA A CA  
106  C C   . ALA A 7   ? 0.30496 0.27003 0.34229 0.00986  0.00948  -0.02074 7   ALA A C   
107  O O   . ALA A 7   ? 0.31377 0.27996 0.34968 0.01304  0.01135  -0.02074 7   ALA A O   
108  C CB  . ALA A 7   ? 0.30069 0.27285 0.34339 0.00533  0.00611  -0.01900 7   ALA A CB  
114  N N   . PHE A 8   ? 0.30019 0.25821 0.33362 0.00743  0.00936  -0.02290 8   PHE A N   
115  C CA  . PHE A 8   ? 0.29456 0.24503 0.32099 0.00700  0.01116  -0.02596 8   PHE A CA  
116  C C   . PHE A 8   ? 0.31681 0.27221 0.34260 0.00450  0.01040  -0.02803 8   PHE A C   
117  O O   . PHE A 8   ? 0.29198 0.25438 0.32165 0.00267  0.00830  -0.02732 8   PHE A O   
118  C CB  . PHE A 8   ? 0.31436 0.25538 0.33558 0.00335  0.01160  -0.02769 8   PHE A CB  
119  C CG  . PHE A 8   ? 0.32933 0.26174 0.34733 0.00743  0.01316  -0.02561 8   PHE A CG  
120  C CD1 . PHE A 8   ? 0.37477 0.29684 0.38517 0.01206  0.01600  -0.02631 8   PHE A CD1 
121  C CD2 . PHE A 8   ? 0.33347 0.26848 0.35529 0.00766  0.01183  -0.02286 8   PHE A CD2 
122  C CE1 . PHE A 8   ? 0.49128 0.40535 0.49760 0.01790  0.01752  -0.02379 8   PHE A CE1 
123  C CE2 . PHE A 8   ? 0.34436 0.27266 0.36265 0.01233  0.01298  -0.02043 8   PHE A CE2 
124  C CZ  . PHE A 8   ? 0.42589 0.34369 0.43634 0.01805  0.01583  -0.02063 8   PHE A CZ  
134  N N   . PRO A 9   ? 0.29353 0.24515 0.31349 0.00515  0.01213  -0.03054 9   PRO A N   
135  C CA  . PRO A 9   ? 0.29878 0.25579 0.31693 0.00244  0.01110  -0.03278 9   PRO A CA  
136  C C   . PRO A 9   ? 0.31247 0.27202 0.33048 -0.00331 0.00911  -0.03494 9   PRO A C   
137  O O   . PRO A 9   ? 0.33796 0.29035 0.35267 -0.00687 0.00985  -0.03669 9   PRO A O   
138  C CB  . PRO A 9   ? 0.35538 0.30491 0.36514 0.00334  0.01371  -0.03607 9   PRO A CB  
139  C CG  . PRO A 9   ? 0.37230 0.31440 0.38092 0.00925  0.01643  -0.03432 9   PRO A CG  
140  C CD  . PRO A 9   ? 0.32289 0.26362 0.33584 0.00841  0.01516  -0.03189 9   PRO A CD  
148  N N   . SER A 10  ? 0.32170 0.29194 0.34285 -0.00389 0.00677  -0.03447 10  SER A N   
149  C CA  . SER A 10  ? 0.30505 0.28245 0.32850 -0.00755 0.00469  -0.03552 10  SER A CA  
150  C C   . SER A 10  ? 0.30747 0.29056 0.32654 -0.01293 0.00390  -0.03990 10  SER A C   
151  O O   . SER A 10  ? 0.30567 0.29723 0.32672 -0.01686 0.00243  -0.04128 10  SER A O   
152  C CB  . SER A 10  ? 0.29519 0.28119 0.32390 -0.00361 0.00265  -0.03219 10  SER A CB  
153  O OG  . SER A 10  ? 0.31405 0.30487 0.34097 -0.00059 0.00197  -0.03122 10  SER A OG  
159  N N   . GLY A 11  ? 0.30387 0.28332 0.31670 -0.01373 0.00500  -0.04245 11  GLY A N   
160  C CA  . GLY A 11  ? 0.32368 0.31074 0.33195 -0.01934 0.00379  -0.04687 11  GLY A CA  
161  C C   . GLY A 11  ? 0.33401 0.32037 0.33971 -0.02824 0.00400  -0.05066 11  GLY A C   
162  O O   . GLY A 11  ? 0.30569 0.30675 0.31269 -0.03301 0.00180  -0.05292 11  GLY A O   
166  N N   . LYS A 12  ? 0.35066 0.32044 0.35187 -0.03070 0.00682  -0.05130 12  LYS A N   
167  C CA  . LYS A 12  ? 0.35940 0.32605 0.35630 -0.04049 0.00764  -0.05463 12  LYS A CA  
168  C C   . LYS A 12  ? 0.35488 0.33769 0.36051 -0.04231 0.00543  -0.05301 12  LYS A C   
169  O O   . LYS A 12  ? 0.37222 0.36287 0.37634 -0.05148 0.00512  -0.05630 12  LYS A O   
170  C CB  . LYS A 12  ? 0.37318 0.31717 0.36285 -0.04092 0.01123  -0.05415 12  LYS A CB  
171  C CG  . LYS A 12  ? 0.50744 0.43363 0.48478 -0.04086 0.01419  -0.05747 12  LYS A CG  
172  C CD  . LYS A 12  ? 0.43513 0.33782 0.40420 -0.03845 0.01792  -0.05614 12  LYS A CD  
173  C CE  . LYS A 12  ? 0.59226 0.47522 0.54649 -0.03847 0.02140  -0.06023 12  LYS A CE  
174  N NZ  . LYS A 12  ? 0.62512 0.51377 0.58337 -0.02833 0.02121  -0.05864 12  LYS A NZ  
188  N N   . VAL A 13  ? 0.29571 0.28392 0.30973 -0.03429 0.00417  -0.04834 13  VAL A N   
189  C CA  . VAL A 13  ? 0.30149 0.30451 0.32298 -0.03437 0.00241  -0.04691 13  VAL A CA  
190  C C   . VAL A 13  ? 0.30774 0.33131 0.33366 -0.03148 -0.00066 -0.04712 13  VAL A C   
191  O O   . VAL A 13  ? 0.28030 0.32060 0.31016 -0.03407 -0.00205 -0.04816 13  VAL A O   
192  C CB  . VAL A 13  ? 0.26666 0.26383 0.29322 -0.02729 0.00271  -0.04219 13  VAL A CB  
193  C CG1 . VAL A 13  ? 0.29048 0.30222 0.32365 -0.02645 0.00124  -0.04107 13  VAL A CG1 
194  C CG2 . VAL A 13  ? 0.35474 0.33328 0.37638 -0.02924 0.00549  -0.04158 13  VAL A CG2 
204  N N   . GLU A 14  ? 0.27375 0.29705 0.29911 -0.02496 -0.00159 -0.04551 14  GLU A N   
205  C CA  . GLU A 14  ? 0.28199 0.32306 0.30941 -0.02109 -0.00445 -0.04518 14  GLU A CA  
206  C C   . GLU A 14  ? 0.31144 0.36823 0.33714 -0.02942 -0.00581 -0.05005 14  GLU A C   
207  O O   . GLU A 14  ? 0.29326 0.37073 0.32298 -0.02729 -0.00835 -0.04993 14  GLU A O   
208  C CB  . GLU A 14  ? 0.28481 0.32122 0.30859 -0.01575 -0.00465 -0.04367 14  GLU A CB  
209  C CG  . GLU A 14  ? 0.31697 0.34241 0.34286 -0.00790 -0.00365 -0.03857 14  GLU A CG  
210  C CD  . GLU A 14  ? 0.34027 0.36023 0.36179 -0.00452 -0.00296 -0.03731 14  GLU A CD  
211  O OE1 . GLU A 14  ? 0.37989 0.40985 0.39858 -0.00298 -0.00469 -0.03776 14  GLU A OE1 
212  O OE2 . GLU A 14  ? 0.30934 0.31658 0.33032 -0.00340 -0.00067 -0.03585 14  GLU A OE2 
219  N N   . GLY A 15  ? 0.28421 0.33160 0.30313 -0.03873 -0.00406 -0.05442 15  GLY A N   
220  C CA  . GLY A 15  ? 0.35426 0.41658 0.37015 -0.04868 -0.00534 -0.05977 15  GLY A CA  
221  C C   . GLY A 15  ? 0.34350 0.41812 0.36318 -0.05644 -0.00529 -0.06147 15  GLY A C   
222  O O   . GLY A 15  ? 0.33142 0.42110 0.34921 -0.06663 -0.00622 -0.06614 15  GLY A O   
226  N N   . CYS A 16  ? 0.29487 0.36355 0.31939 -0.05268 -0.00399 -0.05794 16  CYS A N   
227  C CA  . CYS A 16  ? 0.31472 0.39553 0.34318 -0.05915 -0.00350 -0.05893 16  CYS A CA  
228  C C   . CYS A 16  ? 0.29228 0.39423 0.33033 -0.04975 -0.00573 -0.05571 16  CYS A C   
229  O O   . CYS A 16  ? 0.28275 0.39979 0.32502 -0.05405 -0.00542 -0.05661 16  CYS A O   
230  C CB  . CYS A 16  ? 0.31676 0.37531 0.34211 -0.06231 -0.00002 -0.05754 16  CYS A CB  
231  S SG  . CYS A 16  ? 0.40694 0.43782 0.41822 -0.07236 0.00333  -0.06131 16  CYS A SG  
237  N N   . MET A 17  ? 0.31259 0.41516 0.35312 -0.03697 -0.00754 -0.05193 17  MET A N   
238  C CA  . MET A 17  ? 0.29835 0.41436 0.34550 -0.02668 -0.00882 -0.04852 17  MET A CA  
239  C C   . MET A 17  ? 0.31094 0.45760 0.36161 -0.02496 -0.01173 -0.05002 17  MET A C   
240  O O   . MET A 17  ? 0.30717 0.46207 0.35508 -0.02537 -0.01384 -0.05148 17  MET A O   
241  C CB  . MET A 17  ? 0.27572 0.37732 0.32212 -0.01416 -0.00907 -0.04362 17  MET A CB  
242  C CG  . MET A 17  ? 0.30353 0.37929 0.34768 -0.01517 -0.00652 -0.04193 17  MET A CG  
243  S SD  . MET A 17  ? 0.32134 0.39248 0.36802 -0.02064 -0.00415 -0.04225 17  MET A SD  
244  C CE  . MET A 17  ? 0.27059 0.35925 0.32308 -0.01133 -0.00526 -0.04021 17  MET A CE  
254  N N   . VAL A 18  ? 0.25268 0.41782 0.30927 -0.02268 -0.01183 -0.04971 18  VAL A N   
255  C CA  . VAL A 18  ? 0.30095 0.49945 0.36214 -0.01883 -0.01455 -0.05061 18  VAL A CA  
256  C C   . VAL A 18  ? 0.27560 0.48126 0.34102 -0.00477 -0.01444 -0.04678 18  VAL A C   
257  O O   . VAL A 18  ? 0.25061 0.43629 0.31534 -0.00074 -0.01225 -0.04431 18  VAL A O   
258  C CB  . VAL A 18  ? 0.29572 0.51771 0.35964 -0.03373 -0.01444 -0.05591 18  VAL A CB  
259  C CG1 . VAL A 18  ? 0.32305 0.53522 0.38006 -0.04775 -0.01437 -0.06030 18  VAL A CG1 
260  C CG2 . VAL A 18  ? 0.27272 0.49172 0.33953 -0.04031 -0.01106 -0.05637 18  VAL A CG2 
270  N N   . GLN A 19  ? 0.24780 0.48217 0.31653 0.00346  -0.01698 -0.04637 19  GLN A N   
271  C CA  . GLN A 19  ? 0.28733 0.53128 0.35882 0.01852  -0.01676 -0.04310 19  GLN A CA  
272  C C   . GLN A 19  ? 0.27638 0.55209 0.35540 0.01318  -0.01625 -0.04621 19  GLN A C   
273  O O   . GLN A 19  ? 0.30464 0.60599 0.38668 0.00394  -0.01804 -0.04979 19  GLN A O   
274  C CB  . GLN A 19  ? 0.31029 0.56554 0.37915 0.03422  -0.01971 -0.03976 19  GLN A CB  
275  C CG  . GLN A 19  ? 0.34725 0.60698 0.41586 0.05195  -0.01907 -0.03608 19  GLN A CG  
276  C CD  . GLN A 19  ? 0.45387 0.71772 0.51674 0.06810  -0.02162 -0.03192 19  GLN A CD  
277  O OE1 . GLN A 19  ? 0.51615 0.77256 0.57431 0.08425  -0.02079 -0.02798 19  GLN A OE1 
278  N NE2 . GLN A 19  ? 0.53059 0.80472 0.59224 0.06388  -0.02456 -0.03276 19  GLN A NE2 
287  N N   . VAL A 20  ? 0.25119 0.52480 0.33258 0.01768  -0.01368 -0.04516 20  VAL A N   
288  C CA  . VAL A 20  ? 0.27100 0.57524 0.35956 0.01384  -0.01254 -0.04766 20  VAL A CA  
289  C C   . VAL A 20  ? 0.30804 0.62577 0.39814 0.03336  -0.01242 -0.04472 20  VAL A C   
290  O O   . VAL A 20  ? 0.27676 0.56925 0.36211 0.04373  -0.01063 -0.04171 20  VAL A O   
291  C CB  . VAL A 20  ? 0.25797 0.54883 0.34710 0.00019  -0.00880 -0.04953 20  VAL A CB  
292  C CG1 . VAL A 20  ? 0.25668 0.58255 0.35315 -0.00480 -0.00735 -0.05212 20  VAL A CG1 
293  C CG2 . VAL A 20  ? 0.24835 0.52049 0.33325 -0.01751 -0.00846 -0.05209 20  VAL A CG2 
303  N N   . THR A 21  ? 0.28454 0.64265 0.38086 0.03753  -0.01396 -0.04599 21  THR A N   
304  C CA  . THR A 21  ? 0.28459 0.66031 0.38221 0.05730  -0.01364 -0.04350 21  THR A CA  
305  C C   . THR A 21  ? 0.31236 0.72660 0.41923 0.05317  -0.01192 -0.04652 21  THR A C   
306  O O   . THR A 21  ? 0.27985 0.72504 0.39338 0.03928  -0.01315 -0.05019 21  THR A O   
307  C CB  . THR A 21  ? 0.35546 0.74589 0.45057 0.07263  -0.01751 -0.04073 21  THR A CB  
308  O OG1 . THR A 21  ? 0.33405 0.68645 0.41940 0.07805  -0.01821 -0.03725 21  THR A OG1 
309  C CG2 . THR A 21  ? 0.31006 0.72081 0.40544 0.09452  -0.01710 -0.03810 21  THR A CG2 
317  N N   A CYS A 22  ? 0.28980 0.70328 0.39648 0.06512  -0.00892 -0.04518 22  CYS A N   
318  N N   B CYS A 22  ? 0.27789 0.68921 0.38429 0.06464  -0.00881 -0.04517 22  CYS A N   
319  C CA  A CYS A 22  ? 0.32099 0.77287 0.43616 0.06457  -0.00682 -0.04754 22  CYS A CA  
320  C CA  B CYS A 22  ? 0.32205 0.77016 0.43633 0.06623  -0.00661 -0.04717 22  CYS A CA  
321  C C   A CYS A 22  ? 0.31989 0.77836 0.43232 0.09039  -0.00580 -0.04451 22  CYS A C   
322  C C   B CYS A 22  ? 0.32089 0.77645 0.43212 0.09267  -0.00623 -0.04395 22  CYS A C   
323  O O   A CYS A 22  ? 0.30934 0.73374 0.41361 0.10006  -0.00343 -0.04235 22  CYS A O   
324  O O   B CYS A 22  ? 0.30176 0.72171 0.40376 0.10434  -0.00451 -0.04122 22  CYS A O   
325  C CB  A CYS A 22  ? 0.29786 0.73792 0.41445 0.04805  -0.00270 -0.04993 22  CYS A CB  
326  C CB  B CYS A 22  ? 0.30657 0.74032 0.42135 0.05429  -0.00216 -0.04892 22  CYS A CB  
327  S SG  A CYS A 22  ? 0.28973 0.77917 0.41711 0.04097  0.00030  -0.05338 22  CYS A SG  
328  S SG  B CYS A 22  ? 0.32115 0.76306 0.44059 0.02474  -0.00145 -0.05319 22  CYS A SG  
339  N N   . GLY A 23  ? 0.34419 0.83124 0.45504 0.09924  -0.00761 -0.04351 23  GLY A N   
340  C CA  . GLY A 23  ? 0.42527 0.90896 0.52664 0.12323  -0.00697 -0.03972 23  GLY A CA  
341  C C   . GLY A 23  ? 0.31434 0.76605 0.40679 0.13843  -0.00856 -0.03564 23  GLY A C   
342  O O   . GLY A 23  ? 0.39309 0.84412 0.48534 0.13568  -0.01218 -0.03466 23  GLY A O   
347  N N   . THR A 24  ? 0.34946 0.77163 0.43338 0.15311  -0.00562 -0.03346 24  THR A N   
348  C CA  . THR A 24  ? 0.41833 0.80456 0.49086 0.16683  -0.00632 -0.02942 24  THR A CA  
349  C C   . THR A 24  ? 0.43093 0.77651 0.50086 0.15479  -0.00509 -0.03007 24  THR A C   
350  O O   . THR A 24  ? 0.42860 0.73720 0.48611 0.16321  -0.00484 -0.02676 24  THR A O   
351  C CB  . THR A 24  ? 0.42428 0.79184 0.48167 0.18810  -0.00371 -0.02611 24  THR A CB  
352  O OG1 . THR A 24  ? 0.51892 0.87591 0.57675 0.18705  0.00066  -0.02869 24  THR A OG1 
353  C CG2 . THR A 24  ? 0.50134 0.90056 0.55548 0.19799  -0.00505 -0.02453 24  THR A CG2 
361  N N   . THR A 25  ? 0.36769 0.71544 0.44574 0.13386  -0.00400 -0.03381 25  THR A N   
362  C CA  . THR A 25  ? 0.35715 0.66386 0.43061 0.12012  -0.00268 -0.03418 25  THR A CA  
363  C C   . THR A 25  ? 0.31889 0.62074 0.39535 0.10343  -0.00568 -0.03476 25  THR A C   
364  O O   . THR A 25  ? 0.29860 0.63010 0.38418 0.09148  -0.00708 -0.03756 25  THR A O   
365  C CB  . THR A 25  ? 0.33603 0.64428 0.41419 0.10907  0.00082  -0.03737 25  THR A CB  
366  O OG1 . THR A 25  ? 0.38843 0.70138 0.46298 0.12525  0.00387  -0.03722 25  THR A OG1 
367  C CG2 . THR A 25  ? 0.38388 0.65365 0.45756 0.09607  0.00195  -0.03754 25  THR A CG2 
375  N N   . THR A 26  ? 0.31828 0.58355 0.38653 0.10234  -0.00625 -0.03247 26  THR A N   
376  C CA  . THR A 26  ? 0.33111 0.58854 0.40074 0.08792  -0.00865 -0.03299 26  THR A CA  
377  C C   . THR A 26  ? 0.32812 0.54829 0.39369 0.07706  -0.00702 -0.03295 26  THR A C   
378  O O   . THR A 26  ? 0.32185 0.51565 0.37989 0.08478  -0.00526 -0.03090 26  THR A O   
379  C CB  . THR A 26  ? 0.36723 0.62331 0.43111 0.09842  -0.01168 -0.02968 26  THR A CB  
380  O OG1 . THR A 26  ? 0.45563 0.75090 0.52431 0.10738  -0.01375 -0.02986 26  THR A OG1 
381  C CG2 . THR A 26  ? 0.38223 0.62694 0.44568 0.08533  -0.01372 -0.03015 26  THR A CG2 
389  N N   . LEU A 27  ? 0.26167 0.48119 0.33155 0.05972  -0.00748 -0.03539 27  LEU A N   
390  C CA  . LEU A 27  ? 0.25329 0.43977 0.31939 0.05030  -0.00633 -0.03501 27  LEU A CA  
391  C C   . LEU A 27  ? 0.24032 0.42765 0.30837 0.03633  -0.00788 -0.03685 27  LEU A C   
392  O O   . LEU A 27  ? 0.25879 0.46958 0.32980 0.03503  -0.01006 -0.03822 27  LEU A O   
393  C CB  . LEU A 27  ? 0.25466 0.43264 0.32201 0.04437  -0.00334 -0.03632 27  LEU A CB  
394  C CG  . LEU A 27  ? 0.29992 0.50527 0.37429 0.03802  -0.00188 -0.03927 27  LEU A CG  
395  C CD1 . LEU A 27  ? 0.28799 0.50425 0.36657 0.02080  -0.00245 -0.04207 27  LEU A CD1 
396  C CD2 . LEU A 27  ? 0.29012 0.48291 0.36304 0.03660  0.00123  -0.03948 27  LEU A CD2 
408  N N   . ASN A 28  ? 0.23806 0.40137 0.30396 0.02653  -0.00667 -0.03711 28  ASN A N   
409  C CA  . ASN A 28  ? 0.24241 0.40105 0.30793 0.01428  -0.00744 -0.03895 28  ASN A CA  
410  C C   . ASN A 28  ? 0.25905 0.42466 0.32758 -0.00046 -0.00573 -0.04236 28  ASN A C   
411  O O   . ASN A 28  ? 0.26569 0.42785 0.33530 -0.00239 -0.00346 -0.04233 28  ASN A O   
412  C CB  . ASN A 28  ? 0.27156 0.39909 0.33184 0.01337  -0.00684 -0.03690 28  ASN A CB  
413  C CG  . ASN A 28  ? 0.25531 0.37181 0.31095 0.02618  -0.00778 -0.03322 28  ASN A CG  
414  O OD1 . ASN A 28  ? 0.27760 0.39962 0.33124 0.02983  -0.00970 -0.03240 28  ASN A OD1 
415  N ND2 . ASN A 28  ? 0.28869 0.38864 0.34133 0.03242  -0.00628 -0.03103 28  ASN A ND2 
422  N N   . GLY A 29  ? 0.25221 0.42501 0.32040 -0.01139 -0.00662 -0.04530 29  GLY A N   
423  C CA  . GLY A 29  ? 0.24683 0.42019 0.31466 -0.02716 -0.00462 -0.04854 29  GLY A CA  
424  C C   . GLY A 29  ? 0.23745 0.38784 0.29879 -0.03604 -0.00413 -0.04971 29  GLY A C   
425  O O   . GLY A 29  ? 0.26607 0.40774 0.32464 -0.03121 -0.00579 -0.04883 29  GLY A O   
429  N N   . LEU A 30  ? 0.26403 0.40385 0.32184 -0.04865 -0.00146 -0.05156 30  LEU A N   
430  C CA  . LEU A 30  ? 0.25373 0.36887 0.30348 -0.05652 -0.00020 -0.05274 30  LEU A CA  
431  C C   . LEU A 30  ? 0.29425 0.41884 0.34014 -0.07239 0.00065  -0.05769 30  LEU A C   
432  O O   . LEU A 30  ? 0.32038 0.44920 0.36547 -0.08238 0.00304  -0.05900 30  LEU A O   
433  C CB  . LEU A 30  ? 0.28811 0.37732 0.33394 -0.05670 0.00253  -0.05015 30  LEU A CB  
434  C CG  . LEU A 30  ? 0.29479 0.35671 0.33153 -0.06145 0.00414  -0.05061 30  LEU A CG  
435  C CD1 . LEU A 30  ? 0.35668 0.40970 0.39334 -0.05159 0.00233  -0.04892 30  LEU A CD1 
436  C CD2 . LEU A 30  ? 0.30407 0.34663 0.33725 -0.06222 0.00684  -0.04795 30  LEU A CD2 
448  N N   . TRP A 31  ? 0.28674 0.41442 0.32931 -0.07547 -0.00113 -0.06056 31  TRP A N   
449  C CA  . TRP A 31  ? 0.25952 0.39984 0.29805 -0.09098 -0.00097 -0.06610 31  TRP A CA  
450  C C   . TRP A 31  ? 0.36342 0.47224 0.38933 -0.10089 0.00199  -0.06829 31  TRP A C   
451  O O   . TRP A 31  ? 0.35797 0.45102 0.37858 -0.09687 0.00140  -0.06859 31  TRP A O   
452  C CB  . TRP A 31  ? 0.29804 0.46178 0.33952 -0.08777 -0.00493 -0.06813 31  TRP A CB  
453  C CG  . TRP A 31  ? 0.32173 0.50388 0.35977 -0.10342 -0.00569 -0.07432 31  TRP A CG  
454  C CD1 . TRP A 31  ? 0.34912 0.53805 0.38408 -0.12088 -0.00333 -0.07838 31  TRP A CD1 
455  C CD2 . TRP A 31  ? 0.34415 0.54124 0.38065 -0.10396 -0.00909 -0.07735 31  TRP A CD2 
456  N NE1 . TRP A 31  ? 0.34429 0.55228 0.37605 -0.13309 -0.00519 -0.08422 31  TRP A NE1 
457  C CE2 . TRP A 31  ? 0.37716 0.59114 0.41011 -0.12236 -0.00893 -0.08365 31  TRP A CE2 
458  C CE3 . TRP A 31  ? 0.40228 0.60055 0.43946 -0.09103 -0.01220 -0.07521 31  TRP A CE3 
459  C CZ2 . TRP A 31  ? 0.44609 0.67865 0.47636 -0.12803 -0.01213 -0.08823 31  TRP A CZ2 
460  C CZ3 . TRP A 31  ? 0.37892 0.59504 0.41326 -0.09576 -0.01524 -0.07924 31  TRP A CZ3 
461  C CH2 . TRP A 31  ? 0.39224 0.62556 0.42336 -0.11391 -0.01535 -0.08581 31  TRP A CH2 
472  N N   . LEU A 32  ? 0.33909 0.43814 0.35909 -0.11340 0.00551  -0.06969 32  LEU A N   
473  C CA  . LEU A 32  ? 0.36418 0.43075 0.36960 -0.12294 0.00903  -0.07166 32  LEU A CA  
474  C C   . LEU A 32  ? 0.42329 0.49789 0.42154 -0.14314 0.01089  -0.07730 32  LEU A C   
475  O O   . LEU A 32  ? 0.38869 0.48045 0.39125 -0.15053 0.01200  -0.07730 32  LEU A O   
476  C CB  . LEU A 32  ? 0.35404 0.39488 0.35592 -0.11853 0.01218  -0.06702 32  LEU A CB  
477  C CG  . LEU A 32  ? 0.39718 0.43185 0.40627 -0.10051 0.01050  -0.06163 32  LEU A CG  
478  C CD1 . LEU A 32  ? 0.38541 0.40314 0.39232 -0.09848 0.01323  -0.05748 32  LEU A CD1 
479  C CD2 . LEU A 32  ? 0.40964 0.42528 0.41288 -0.09421 0.01006  -0.06189 32  LEU A CD2 
491  N N   . ASP A 33  ? 0.43363 0.49647 0.42038 -0.15277 0.01145  -0.08239 33  ASP A N   
492  C CA  . ASP A 33  ? 0.43763 0.50926 0.41643 -0.17386 0.01293  -0.08874 33  ASP A CA  
493  C C   . ASP A 33  ? 0.45217 0.57112 0.44572 -0.17604 0.00939  -0.09000 33  ASP A C   
494  O O   . ASP A 33  ? 0.39568 0.53711 0.39961 -0.16385 0.00492  -0.08903 33  ASP A O   
495  C CB  . ASP A 33  ? 0.53888 0.58293 0.50495 -0.18566 0.01845  -0.08833 33  ASP A CB  
496  C CG  . ASP A 33  ? 0.66254 0.66110 0.61249 -0.18211 0.02176  -0.08746 33  ASP A CG  
497  O OD1 . ASP A 33  ? 0.76791 0.75473 0.70813 -0.18531 0.02158  -0.09201 33  ASP A OD1 
498  O OD2 . ASP A 33  ? 0.62309 0.59848 0.56934 -0.17614 0.02465  -0.08242 33  ASP A OD2 
503  N N   . ASP A 34  ? 0.42546 0.56141 0.41998 -0.19055 0.01137  -0.09184 34  ASP A N   
504  C CA  . ASP A 34  ? 0.42368 0.60779 0.43245 -0.19195 0.00819  -0.09315 34  ASP A CA  
505  C C   . ASP A 34  ? 0.40310 0.60343 0.42476 -0.18085 0.00852  -0.08767 34  ASP A C   
506  O O   . ASP A 34  ? 0.40287 0.64070 0.43398 -0.18575 0.00784  -0.08891 34  ASP A O   
507  C CB  . ASP A 34  ? 0.44997 0.64455 0.44981 -0.20993 0.01085  -0.09675 34  ASP A CB  
508  C CG  . ASP A 34  ? 0.48092 0.65200 0.46942 -0.22110 0.01707  -0.09493 34  ASP A CG  
509  O OD1 . ASP A 34  ? 0.46850 0.61192 0.45436 -0.21704 0.01940  -0.09159 34  ASP A OD1 
510  O OD2 . ASP A 34  ? 0.61907 0.79982 0.60021 -0.23451 0.01978  -0.09684 34  ASP A OD2 
515  N N   . VAL A 35  ? 0.38402 0.56010 0.40675 -0.16526 0.00928  -0.08193 35  VAL A N   
516  C CA  . VAL A 35  ? 0.37010 0.55832 0.40339 -0.15413 0.00967  -0.07708 35  VAL A CA  
517  C C   . VAL A 35  ? 0.37265 0.55852 0.41364 -0.13162 0.00633  -0.07261 35  VAL A C   
518  O O   . VAL A 35  ? 0.33364 0.49190 0.36884 -0.12487 0.00584  -0.07121 35  VAL A O   
519  C CB  . VAL A 35  ? 0.35686 0.51614 0.38199 -0.15937 0.01456  -0.07429 35  VAL A CB  
520  C CG1 . VAL A 35  ? 0.35290 0.52465 0.38838 -0.14734 0.01492  -0.06956 35  VAL A CG1 
521  C CG2 . VAL A 35  ? 0.39613 0.55554 0.41135 -0.18331 0.01849  -0.07856 35  VAL A CG2 
531  N N   . VAL A 36  ? 0.31070 0.52471 0.36380 -0.11999 0.00444  -0.07034 36  VAL A N   
532  C CA  . VAL A 36  ? 0.28353 0.49316 0.34238 -0.09912 0.00203  -0.06575 36  VAL A CA  
533  C C   . VAL A 36  ? 0.30646 0.50801 0.36783 -0.09270 0.00454  -0.06189 36  VAL A C   
534  O O   . VAL A 36  ? 0.30896 0.53361 0.37567 -0.09570 0.00592  -0.06239 36  VAL A O   
535  C CB  . VAL A 36  ? 0.27962 0.52407 0.34761 -0.08868 -0.00202 -0.06600 36  VAL A CB  
536  C CG1 . VAL A 36  ? 0.30296 0.53951 0.37472 -0.06749 -0.00361 -0.06087 36  VAL A CG1 
537  C CG2 . VAL A 36  ? 0.29851 0.54906 0.36277 -0.09442 -0.00494 -0.06967 36  VAL A CG2 
547  N N   . TYR A 37  ? 0.31295 0.48325 0.37035 -0.08423 0.00522  -0.05823 37  TYR A N   
548  C CA  . TYR A 37  ? 0.29705 0.45732 0.35550 -0.07831 0.00734  -0.05472 37  TYR A CA  
549  C C   . TYR A 37  ? 0.28519 0.45188 0.35010 -0.06000 0.00502  -0.05176 37  TYR A C   
550  O O   . TYR A 37  ? 0.28026 0.43761 0.34445 -0.05160 0.00265  -0.05059 37  TYR A O   
551  C CB  . TYR A 37  ? 0.28782 0.41127 0.33731 -0.08045 0.00941  -0.05252 37  TYR A CB  
552  C CG  . TYR A 37  ? 0.32891 0.43985 0.36878 -0.09753 0.01234  -0.05503 37  TYR A CG  
553  C CD1 . TYR A 37  ? 0.31024 0.41523 0.34422 -0.10507 0.01165  -0.05843 37  TYR A CD1 
554  C CD2 . TYR A 37  ? 0.33880 0.44153 0.37356 -0.10630 0.01610  -0.05402 37  TYR A CD2 
555  C CE1 . TYR A 37  ? 0.33361 0.42362 0.35620 -0.12115 0.01475  -0.06116 37  TYR A CE1 
556  C CE2 . TYR A 37  ? 0.35120 0.43854 0.37431 -0.12261 0.01933  -0.05613 37  TYR A CE2 
557  C CZ  . TYR A 37  ? 0.40344 0.48359 0.42023 -0.12979 0.01869  -0.05982 37  TYR A CZ  
558  O OH  . TYR A 37  ? 0.40318 0.46547 0.40624 -0.14630 0.02216  -0.06249 37  TYR A OH  
568  N N   . CYS A 38  ? 0.25976 0.44041 0.32956 -0.05377 0.00603  -0.05055 38  CYS A N   
569  C CA  . CYS A 38  ? 0.25344 0.43375 0.32624 -0.03624 0.00432  -0.04784 38  CYS A CA  
570  C C   . CYS A 38  ? 0.28470 0.46772 0.35898 -0.03160 0.00666  -0.04656 38  CYS A C   
571  O O   . CYS A 38  ? 0.23786 0.42809 0.31216 -0.04161 0.00938  -0.04768 38  CYS A O   
572  C CB  . CYS A 38  ? 0.27022 0.47715 0.34817 -0.02761 0.00144  -0.04867 38  CYS A CB  
573  S SG  . CYS A 38  ? 0.27276 0.52331 0.35873 -0.02918 0.00248  -0.05111 38  CYS A SG  
579  N N   . PRO A 39  ? 0.26936 0.44401 0.34332 -0.01732 0.00601  -0.04425 39  PRO A N   
580  C CA  . PRO A 39  ? 0.25764 0.43223 0.33141 -0.01279 0.00839  -0.04347 39  PRO A CA  
581  C C   . PRO A 39  ? 0.20822 0.41675 0.28788 -0.01091 0.00954  -0.04538 39  PRO A C   
582  O O   . PRO A 39  ? 0.22647 0.45671 0.31028 -0.00468 0.00763  -0.04621 39  PRO A O   
583  C CB  . PRO A 39  ? 0.23456 0.39179 0.30508 0.00189  0.00715  -0.04121 39  PRO A CB  
584  C CG  . PRO A 39  ? 0.25531 0.39397 0.32314 -0.00001 0.00488  -0.04009 39  PRO A CG  
585  C CD  . PRO A 39  ? 0.23436 0.39168 0.30558 -0.00702 0.00362  -0.04215 39  PRO A CD  
593  N N   . ARG A 40  ? 0.20585 0.42100 0.28581 -0.01653 0.01272  -0.04596 40  ARG A N   
594  C CA  . ARG A 40  ? 0.23744 0.48860 0.32370 -0.01555 0.01429  -0.04794 40  ARG A CA  
595  C C   . ARG A 40  ? 0.22204 0.48421 0.30987 0.00397  0.01392  -0.04737 40  ARG A C   
596  O O   . ARG A 40  ? 0.24605 0.54132 0.33982 0.00874  0.01420  -0.04880 40  ARG A O   
597  C CB  . ARG A 40  ? 0.19932 0.45580 0.28486 -0.02695 0.01835  -0.04857 40  ARG A CB  
598  C CG  . ARG A 40  ? 0.24378 0.47950 0.32398 -0.02096 0.02038  -0.04676 40  ARG A CG  
599  C CD  . ARG A 40  ? 0.23712 0.48154 0.31628 -0.03244 0.02456  -0.04718 40  ARG A CD  
600  N NE  . ARG A 40  ? 0.25161 0.47687 0.32501 -0.02637 0.02619  -0.04557 40  ARG A NE  
601  C CZ  . ARG A 40  ? 0.29675 0.52712 0.36782 -0.03222 0.02993  -0.04543 40  ARG A CZ  
602  N NH1 . ARG A 40  ? 0.27618 0.52723 0.34951 -0.04580 0.03280  -0.04642 40  ARG A NH1 
603  N NH2 . ARG A 40  ? 0.27217 0.48751 0.33795 -0.02478 0.03095  -0.04443 40  ARG A NH2 
617  N N   . ALA A 41  ? 0.24786 0.48335 0.32978 0.01546  0.01319  -0.04538 41  ALA A N   
618  C CA  . ALA A 41  ? 0.25937 0.49973 0.33968 0.03443  0.01312  -0.04483 41  ALA A CA  
619  C C   . ALA A 41  ? 0.26302 0.52234 0.34653 0.04380  0.01032  -0.04454 41  ALA A C   
620  O O   . ALA A 41  ? 0.30474 0.57240 0.38652 0.06074  0.01053  -0.04391 41  ALA A O   
621  C CB  . ALA A 41  ? 0.30895 0.51318 0.38040 0.04178  0.01290  -0.04301 41  ALA A CB  
627  N N   . VAL A 42  ? 0.23868 0.50460 0.32561 0.03398  0.00780  -0.04495 42  VAL A N   
628  C CA  . VAL A 42  ? 0.27522 0.56514 0.36564 0.04241  0.00499  -0.04484 42  VAL A CA  
629  C C   . VAL A 42  ? 0.26125 0.59356 0.35903 0.04708  0.00623  -0.04664 42  VAL A C   
630  O O   . VAL A 42  ? 0.29710 0.65040 0.39661 0.06089  0.00441  -0.04587 42  VAL A O   
631  C CB  . VAL A 42  ? 0.25041 0.54109 0.34260 0.02922  0.00216  -0.04572 42  VAL A CB  
632  C CG1 . VAL A 42  ? 0.23498 0.55054 0.33336 0.01122  0.00341  -0.04910 42  VAL A CG1 
633  C CG2 . VAL A 42  ? 0.29127 0.59609 0.38383 0.04087  -0.00151 -0.04450 42  VAL A CG2 
643  N N   . ILE A 43  ? 0.24205 0.58890 0.34383 0.03681  0.00950  -0.04874 43  ILE A N   
644  C CA  . ILE A 43  ? 0.27452 0.66500 0.38395 0.04119  0.01102  -0.05050 43  ILE A CA  
645  C C   . ILE A 43  ? 0.35898 0.75034 0.46538 0.06023  0.01382  -0.04966 43  ILE A C   
646  O O   . ILE A 43  ? 0.31444 0.74243 0.42686 0.06627  0.01566  -0.05103 43  ILE A O   
647  C CB  . ILE A 43  ? 0.28142 0.69279 0.39661 0.02025  0.01363  -0.05333 43  ILE A CB  
648  C CG1 . ILE A 43  ? 0.20705 0.59767 0.31775 0.01500  0.01780  -0.05307 43  ILE A CG1 
649  C CG2 . ILE A 43  ? 0.31753 0.72161 0.43266 0.00057  0.01144  -0.05460 43  ILE A CG2 
650  C CD1 . ILE A 43  ? 0.27138 0.68273 0.38623 -0.00473 0.02090  -0.05529 43  ILE A CD1 
662  N N   . CYS A 44  ? 0.31448 0.66723 0.41136 0.06813  0.01467  -0.04793 44  CYS A N   
663  C CA  . CYS A 44  ? 0.44208 0.79200 0.53364 0.08619  0.01757  -0.04770 44  CYS A CA  
664  C C   . CYS A 44  ? 0.50305 0.86462 0.59225 0.10845  0.01609  -0.04614 44  CYS A C   
665  O O   . CYS A 44  ? 0.57553 0.92793 0.66245 0.11234  0.01256  -0.04409 44  CYS A O   
666  C CB  . CYS A 44  ? 0.49343 0.79820 0.57404 0.08780  0.01858  -0.04665 44  CYS A CB  
667  S SG  . CYS A 44  ? 0.46121 0.75174 0.54231 0.06676  0.02073  -0.04778 44  CYS A SG  
673  N N   . THR A 45  ? 0.68530 1.06340 0.77312 0.12447  0.01912  -0.04683 45  THR A N   
674  C CA  . THR A 45  ? 0.74774 1.12692 0.82890 0.14910  0.01850  -0.04477 45  THR A CA  
675  C C   . THR A 45  ? 0.84976 1.18062 0.91491 0.15997  0.02008  -0.04347 45  THR A C   
676  O O   . THR A 45  ? 0.82035 1.12828 0.88106 0.15231  0.02262  -0.04504 45  THR A O   
677  C CB  . THR A 45  ? 0.73780 1.14576 0.81791 0.15770  0.01959  -0.04465 45  THR A CB  
678  O OG1 . THR A 45  ? 0.75366 1.15127 0.82886 0.16151  0.02431  -0.04653 45  THR A OG1 
679  C CG2 . THR A 45  ? 0.66994 1.11911 0.76289 0.14042  0.01822  -0.04632 45  THR A CG2 
687  N N   . SER A 46  ? 1.06566 1.38070 1.12109 0.17734  0.01856  -0.04054 46  SER A N   
688  C CA  . SER A 46  ? 1.10663 1.37514 1.14483 0.18758  0.02037  -0.03945 46  SER A CA  
689  C C   . SER A 46  ? 1.14584 1.40981 1.17732 0.19641  0.02538  -0.04221 46  SER A C   
690  O O   . SER A 46  ? 1.16344 1.38928 1.18315 0.19477  0.02729  -0.04312 46  SER A O   
691  C CB  . SER A 46  ? 1.11784 1.37232 1.14394 0.20548  0.01848  -0.03520 46  SER A CB  
692  O OG  . SER A 46  ? 1.10904 1.38692 1.13194 0.21710  0.01810  -0.03333 46  SER A OG  
698  N N   . GLU A 47  ? 0.97579 1.27135 1.01104 0.19995  0.02615  -0.04243 47  GLU A N   
699  C CA  . GLU A 47  ? 0.91957 1.21080 0.94738 0.20655  0.03039  -0.04455 47  GLU A CA  
700  C C   . GLU A 47  ? 0.88782 1.17664 0.92199 0.19217  0.03375  -0.04888 47  GLU A C   
701  O O   . GLU A 47  ? 1.00014 1.25729 1.02296 0.19520  0.03678  -0.05097 47  GLU A O   
702  C CB  . GLU A 47  ? 0.92311 1.25361 0.95531 0.21215  0.03022  -0.04389 47  GLU A CB  
703  C CG  . GLU A 47  ? 1.02811 1.37095 1.05608 0.22489  0.02654  -0.03972 47  GLU A CG  
704  C CD  . GLU A 47  ? 1.09758 1.40912 1.10485 0.24590  0.02773  -0.03701 47  GLU A CD  
705  O OE1 . GLU A 47  ? 1.17453 1.44392 1.17011 0.24861  0.02838  -0.03625 47  GLU A OE1 
706  O OE2 . GLU A 47  ? 0.95544 1.28411 0.95716 0.25924  0.02814  -0.03565 47  GLU A OE2 
713  N N   . ASP A 48  ? 0.84235 1.16336 0.89316 0.17536  0.03332  -0.05031 48  ASP A N   
714  C CA  . ASP A 48  ? 0.81684 1.13380 0.87056 0.15740  0.03547  -0.05254 48  ASP A CA  
715  C C   . ASP A 48  ? 0.75936 1.04853 0.81386 0.13717  0.03210  -0.05119 48  ASP A C   
716  O O   . ASP A 48  ? 0.72803 1.03363 0.79329 0.11981  0.03033  -0.05090 48  ASP A O   
717  C CB  . ASP A 48  ? 0.91368 1.27939 0.98142 0.14979  0.03765  -0.05433 48  ASP A CB  
718  C CG  . ASP A 48  ? 0.94837 1.34281 1.03015 0.13498  0.03400  -0.05331 48  ASP A CG  
719  O OD1 . ASP A 48  ? 0.81445 1.19058 0.89574 0.12920  0.02972  -0.05128 48  ASP A OD1 
720  O OD2 . ASP A 48  ? 0.82723 1.25755 0.91762 0.12624  0.03472  -0.05410 48  ASP A OD2 
725  N N   A MET A 49  ? 0.61102 0.85714 0.65300 0.13936  0.03151  -0.05054 49  MET A N   
726  N N   B MET A 49  ? 0.61098 0.85698 0.65288 0.13967  0.03144  -0.05048 49  MET A N   
727  C CA  A MET A 49  ? 0.53966 0.75911 0.58141 0.12158  0.02898  -0.04949 49  MET A CA  
728  C CA  B MET A 49  ? 0.53856 0.75680 0.57981 0.12225  0.02891  -0.04942 49  MET A CA  
729  C C   A MET A 49  ? 0.42404 0.61991 0.45818 0.11514  0.03129  -0.05122 49  MET A C   
730  C C   B MET A 49  ? 0.43154 0.62740 0.46566 0.11526  0.03127  -0.05121 49  MET A C   
731  O O   A MET A 49  ? 0.41690 0.59187 0.45046 0.10120  0.02941  -0.05032 49  MET A O   
732  O O   B MET A 49  ? 0.41344 0.58908 0.44727 0.10106  0.02940  -0.05031 49  MET A O   
733  C CB  A MET A 49  ? 0.55522 0.74715 0.59044 0.12586  0.02560  -0.04690 49  MET A CB  
734  C CB  B MET A 49  ? 0.55679 0.74559 0.59054 0.12723  0.02571  -0.04689 49  MET A CB  
735  C CG  A MET A 49  ? 0.59709 0.81195 0.63752 0.13546  0.02338  -0.04501 49  MET A CG  
736  C CG  B MET A 49  ? 0.59441 0.80297 0.63423 0.13327  0.02272  -0.04460 49  MET A CG  
737  S SD  A MET A 49  ? 0.56167 0.78127 0.61213 0.11841  0.01866  -0.04304 49  MET A SD  
738  S SD  B MET A 49  ? 0.63690 0.81058 0.66409 0.14430  0.02021  -0.04124 49  MET A SD  
739  C CE  A MET A 49  ? 0.47461 0.64730 0.51182 0.12219  0.01673  -0.04040 49  MET A CE  
740  C CE  B MET A 49  ? 0.65530 0.85976 0.69370 0.14374  0.01615  -0.03891 49  MET A CE  
759  N N   . LEU A 50  ? 0.38034 0.58095 0.40859 0.12512  0.03535  -0.05376 50  LEU A N   
760  C CA  . LEU A 50  ? 0.37269 0.55375 0.39366 0.11804  0.03742  -0.05567 50  LEU A CA  
761  C C   . LEU A 50  ? 0.38265 0.58581 0.41318 0.10204  0.03877  -0.05597 50  LEU A C   
762  O O   . LEU A 50  ? 0.33525 0.52116 0.36324 0.08908  0.03834  -0.05569 50  LEU A O   
763  C CB  . LEU A 50  ? 0.46156 0.63595 0.47013 0.13505  0.04163  -0.05875 50  LEU A CB  
764  C CG  . LEU A 50  ? 0.49607 0.63089 0.48759 0.14612  0.04146  -0.05939 50  LEU A CG  
765  C CD1 . LEU A 50  ? 0.48111 0.61104 0.45968 0.16132  0.04640  -0.06320 50  LEU A CD1 
766  C CD2 . LEU A 50  ? 0.46062 0.56266 0.44703 0.13109  0.03888  -0.05900 50  LEU A CD2 
779  N N   . ASN A 51  ? 0.34651 0.58806 0.38662 0.10361  0.04086  -0.05658 51  ASN A N   
780  C CA  . ASN A 51  ? 0.32548 0.59065 0.37339 0.08887  0.04316  -0.05694 51  ASN A CA  
781  C C   . ASN A 51  ? 0.28602 0.58833 0.34767 0.08235  0.04236  -0.05615 51  ASN A C   
782  O O   . ASN A 51  ? 0.29434 0.63116 0.36250 0.08098  0.04569  -0.05748 51  ASN A O   
783  C CB  . ASN A 51  ? 0.35391 0.63014 0.39677 0.09681  0.04833  -0.05975 51  ASN A CB  
784  C CG  . ASN A 51  ? 0.31836 0.55766 0.34706 0.09934  0.04890  -0.06102 51  ASN A CG  
785  O OD1 . ASN A 51  ? 0.31933 0.54105 0.34609 0.08504  0.04767  -0.05989 51  ASN A OD1 
786  N ND2 . ASN A 51  ? 0.31393 0.53931 0.33169 0.11746  0.05042  -0.06324 51  ASN A ND2 
793  N N   . PRO A 52  ? 0.31508 0.61216 0.38119 0.07664  0.03809  -0.05420 52  PRO A N   
794  C CA  . PRO A 52  ? 0.38236 0.71448 0.46063 0.06826  0.03711  -0.05403 52  PRO A CA  
795  C C   . PRO A 52  ? 0.30503 0.65294 0.38819 0.04839  0.03980  -0.05447 52  PRO A C   
796  O O   . PRO A 52  ? 0.34564 0.66891 0.42346 0.03665  0.04031  -0.05347 52  PRO A O   
797  C CB  . PRO A 52  ? 0.34035 0.65364 0.41923 0.06348  0.03213  -0.05202 52  PRO A CB  
798  C CG  . PRO A 52  ? 0.42337 0.69287 0.49209 0.06276  0.03099  -0.05083 52  PRO A CG  
799  C CD  . PRO A 52  ? 0.33140 0.59149 0.39135 0.07604  0.03422  -0.05237 52  PRO A CD  
807  N N   . ASN A 53  ? 0.27626 0.66578 0.36880 0.04469  0.04170  -0.05578 53  ASN A N   
808  C CA  . ASN A 53  ? 0.24760 0.65279 0.34446 0.02319  0.04411  -0.05598 53  ASN A CA  
809  C C   . ASN A 53  ? 0.26892 0.68239 0.37209 0.01081  0.04053  -0.05566 53  ASN A C   
810  O O   . ASN A 53  ? 0.25057 0.70062 0.36256 0.01259  0.03987  -0.05705 53  ASN A O   
811  C CB  . ASN A 53  ? 0.33301 0.78036 0.43569 0.02481  0.04900  -0.05800 53  ASN A CB  
812  C CG  . ASN A 53  ? 0.39963 0.85768 0.50368 0.00194  0.05248  -0.05790 53  ASN A CG  
813  O OD1 . ASN A 53  ? 0.34130 0.79938 0.44780 -0.01610 0.05102  -0.05735 53  ASN A OD1 
814  N ND2 . ASN A 53  ? 0.48813 0.95291 0.58887 0.00235  0.05746  -0.05842 53  ASN A ND2 
821  N N   . TYR A 54  ? 0.29223 0.67357 0.39057 -0.00219 0.03839  -0.05403 54  TYR A N   
822  C CA  . TYR A 54  ? 0.25218 0.63618 0.35451 -0.01118 0.03467  -0.05409 54  TYR A CA  
823  C C   . TYR A 54  ? 0.21475 0.63220 0.32364 -0.02927 0.03657  -0.05595 54  TYR A C   
824  O O   . TYR A 54  ? 0.22586 0.66399 0.34084 -0.03277 0.03388  -0.05733 54  TYR A O   
825  C CB  . TYR A 54  ? 0.24916 0.59038 0.34390 -0.01967 0.03237  -0.05205 54  TYR A CB  
826  C CG  . TYR A 54  ? 0.25241 0.56464 0.34215 -0.00351 0.02938  -0.05054 54  TYR A CG  
827  C CD1 . TYR A 54  ? 0.26738 0.58155 0.35957 0.00646  0.02556  -0.05043 54  TYR A CD1 
828  C CD2 . TYR A 54  ? 0.29632 0.58026 0.37815 0.00149  0.03052  -0.04927 54  TYR A CD2 
829  C CE1 . TYR A 54  ? 0.30314 0.58951 0.38946 0.02018  0.02327  -0.04886 54  TYR A CE1 
830  C CE2 . TYR A 54  ? 0.26467 0.52218 0.34115 0.01458  0.02799  -0.04821 54  TYR A CE2 
831  C CZ  . TYR A 54  ? 0.26996 0.52827 0.34849 0.02351  0.02462  -0.04793 54  TYR A CZ  
832  O OH  . TYR A 54  ? 0.27779 0.50842 0.34969 0.03476  0.02266  -0.04670 54  TYR A OH  
842  N N   . GLU A 55  ? 0.27313 0.69588 0.37997 -0.04191 0.04121  -0.05603 55  GLU A N   
843  C CA  . GLU A 55  ? 0.29175 0.74649 0.40365 -0.06119 0.04370  -0.05792 55  GLU A CA  
844  C C   . GLU A 55  ? 0.28226 0.78348 0.40365 -0.05147 0.04303  -0.06005 55  GLU A C   
845  O O   . GLU A 55  ? 0.23146 0.74910 0.35372 -0.06013 0.03992  -0.06126 55  GLU A O   
846  C CB  . GLU A 55  ? 0.35535 0.80529 0.46146 -0.07444 0.04928  -0.05697 55  GLU A CB  
847  C CG  . GLU A 55  ? 0.43553 0.83959 0.52989 -0.08782 0.04916  -0.05436 55  GLU A CG  
848  C CD  . GLU A 55  ? 0.60944 0.97451 0.69617 -0.07306 0.04769  -0.05169 55  GLU A CD  
849  O OE1 . GLU A 55  ? 0.56140 0.93260 0.65008 -0.05463 0.04772  -0.05210 55  GLU A OE1 
850  O OE2 . GLU A 55  ? 0.61002 0.93811 0.68799 -0.07996 0.04658  -0.04932 55  GLU A OE2 
857  N N   . ASP A 56  ? 0.21990 0.73087 0.34202 -0.03169 0.04432  -0.05981 56  ASP A N   
858  C CA  . ASP A 56  ? 0.28290 0.82469 0.40731 -0.01864 0.04184  -0.06041 56  ASP A CA  
859  C C   . ASP A 56  ? 0.26687 0.81229 0.39406 -0.00756 0.03620  -0.06027 56  ASP A C   
860  O O   . ASP A 56  ? 0.25228 0.82402 0.38095 -0.00791 0.03319  -0.06096 56  ASP A O   
861  C CB  . ASP A 56  ? 0.23993 0.78461 0.36214 0.00157  0.04449  -0.06006 56  ASP A CB  
862  C CG  . ASP A 56  ? 0.31310 0.89153 0.43648 0.01273  0.04273  -0.06047 56  ASP A CG  
863  O OD1 . ASP A 56  ? 0.31270 0.91549 0.43692 -0.00044 0.04404  -0.06139 56  ASP A OD1 
864  O OD2 . ASP A 56  ? 0.33986 0.91943 0.46217 0.03446  0.04023  -0.05973 56  ASP A OD2 
869  N N   . LEU A 57  ? 0.23228 0.75218 0.35936 0.00331  0.03486  -0.05933 57  LEU A N   
870  C CA  . LEU A 57  ? 0.21056 0.73105 0.33904 0.01449  0.02965  -0.05868 57  LEU A CA  
871  C C   . LEU A 57  ? 0.24914 0.77642 0.37982 -0.00500 0.02658  -0.05982 57  LEU A C   
872  O O   . LEU A 57  ? 0.23213 0.77714 0.36357 -0.00071 0.02247  -0.05996 57  LEU A O   
873  C CB  . LEU A 57  ? 0.28387 0.76703 0.40820 0.02725  0.02865  -0.05710 57  LEU A CB  
874  C CG  . LEU A 57  ? 0.31119 0.77942 0.42897 0.04897  0.03086  -0.05615 57  LEU A CG  
875  C CD1 . LEU A 57  ? 0.31676 0.73244 0.42365 0.05477  0.02836  -0.05385 57  LEU A CD1 
876  C CD2 . LEU A 57  ? 0.39098 0.88402 0.50864 0.07023  0.02952  -0.05559 57  LEU A CD2 
888  N N   . LEU A 58  ? 0.20612 0.71669 0.33603 -0.02620 0.02862  -0.06063 58  LEU A N   
889  C CA  . LEU A 58  ? 0.23378 0.74373 0.36292 -0.04460 0.02590  -0.06206 58  LEU A CA  
890  C C   . LEU A 58  ? 0.23307 0.77260 0.36048 -0.05664 0.02558  -0.06393 58  LEU A C   
891  O O   . LEU A 58  ? 0.24717 0.79756 0.37387 -0.06276 0.02205  -0.06544 58  LEU A O   
892  C CB  . LEU A 58  ? 0.23908 0.71693 0.36344 -0.06350 0.02841  -0.06197 58  LEU A CB  
893  C CG  . LEU A 58  ? 0.32989 0.79802 0.45157 -0.07991 0.02554  -0.06361 58  LEU A CG  
894  C CD1 . LEU A 58  ? 0.31390 0.77680 0.43691 -0.06611 0.01991  -0.06316 58  LEU A CD1 
895  C CD2 . LEU A 58  ? 0.30738 0.73088 0.41760 -0.09452 0.02751  -0.06228 58  LEU A CD2 
907  N N   . ILE A 59  ? 0.21523 0.76998 0.34157 -0.05934 0.02921  -0.06407 59  ILE A N   
908  C CA  . ILE A 59  ? 0.21764 0.80038 0.34185 -0.07268 0.02909  -0.06617 59  ILE A CA  
909  C C   . ILE A 59  ? 0.27361 0.88873 0.40093 -0.05709 0.02509  -0.06653 59  ILE A C   
910  O O   . ILE A 59  ? 0.26375 0.90228 0.38942 -0.06788 0.02355  -0.06870 59  ILE A O   
911  C CB  . ILE A 59  ? 0.28737 0.87783 0.40905 -0.08153 0.03405  -0.06621 59  ILE A CB  
912  C CG1 . ILE A 59  ? 0.31999 0.93481 0.43782 -0.10047 0.03426  -0.06878 59  ILE A CG1 
913  C CG2 . ILE A 59  ? 0.32492 0.93196 0.45022 -0.05957 0.03514  -0.06493 59  ILE A CG2 
914  C CD1 . ILE A 59  ? 0.36715 0.98713 0.48104 -0.11304 0.03909  -0.06886 59  ILE A CD1 
926  N N   . ARG A 60  ? 0.22470 0.83901 0.35486 -0.03206 0.02335  -0.06440 60  ARG A N   
927  C CA  . ARG A 60  ? 0.23845 0.87964 0.36946 -0.01524 0.01961  -0.06393 60  ARG A CA  
928  C C   . ARG A 60  ? 0.24734 0.88454 0.37820 -0.01432 0.01487  -0.06397 60  ARG A C   
929  O O   . ARG A 60  ? 0.23931 0.89868 0.36973 -0.00173 0.01165  -0.06338 60  ARG A O   
930  C CB  . ARG A 60  ? 0.21954 0.85583 0.35032 0.01155  0.02015  -0.06131 60  ARG A CB  
931  C CG  . ARG A 60  ? 0.22307 0.86290 0.35338 0.01241  0.02492  -0.06142 60  ARG A CG  
932  C CD  . ARG A 60  ? 0.25358 0.88552 0.38131 0.03897  0.02578  -0.05931 60  ARG A CD  
933  N NE  . ARG A 60  ? 0.24029 0.87381 0.36703 0.03874  0.03062  -0.05978 60  ARG A NE  
934  C CZ  . ARG A 60  ? 0.24048 0.90126 0.36647 0.04610  0.03182  -0.06009 60  ARG A CZ  
935  N NH1 . ARG A 60  ? 0.25037 0.94160 0.37642 0.05435  0.02858  -0.05996 60  ARG A NH1 
936  N NH2 . ARG A 60  ? 0.27853 0.93724 0.40327 0.04515  0.03649  -0.06056 60  ARG A NH2 
950  N N   . LYS A 61  ? 0.24728 0.85779 0.37775 -0.02740 0.01452  -0.06461 61  LYS A N   
951  C CA  . LYS A 61  ? 0.32377 0.92779 0.45381 -0.02709 0.01020  -0.06476 61  LYS A CA  
952  C C   . LYS A 61  ? 0.32191 0.93954 0.44896 -0.04937 0.00930  -0.06816 61  LYS A C   
953  O O   . LYS A 61  ? 0.36427 0.97573 0.48829 -0.07050 0.01246  -0.07026 61  LYS A O   
954  C CB  . LYS A 61  ? 0.25441 0.82063 0.38504 -0.02832 0.01012  -0.06378 61  LYS A CB  
955  C CG  . LYS A 61  ? 0.29713 0.84453 0.42930 -0.00710 0.01125  -0.06079 61  LYS A CG  
956  C CD  . LYS A 61  ? 0.33521 0.89030 0.46624 0.01704  0.00772  -0.05833 61  LYS A CD  
957  C CE  . LYS A 61  ? 0.43484 0.96863 0.56402 0.03855  0.00931  -0.05559 61  LYS A CE  
958  N NZ  . LYS A 61  ? 0.57816 1.11870 0.70283 0.06188  0.00621  -0.05277 61  LYS A NZ  
972  N N   . SER A 62  ? 0.30733 0.93828 0.43367 -0.04469 0.00517  -0.06855 62  SER A N   
973  C CA  . SER A 62  ? 0.29113 0.92948 0.41350 -0.06416 0.00385  -0.07198 62  SER A CA  
974  C C   . SER A 62  ? 0.36917 0.97655 0.49011 -0.06861 0.00170  -0.07214 62  SER A C   
975  O O   . SER A 62  ? 0.31136 0.90220 0.43518 -0.05197 -0.00034 -0.06928 62  SER A O   
976  C CB  . SER A 62  ? 0.36989 1.04525 0.49190 -0.05591 0.00078  -0.07247 62  SER A CB  
977  O OG  . SER A 62  ? 0.36098 1.06755 0.48415 -0.05045 0.00254  -0.07234 62  SER A OG  
983  N N   . ASN A 63  ? 0.35204 0.95285 0.46733 -0.09046 0.00197  -0.07565 63  ASN A N   
984  C CA  . ASN A 63  ? 0.32989 0.90322 0.44280 -0.09434 -0.00042 -0.07620 63  ASN A CA  
985  C C   . ASN A 63  ? 0.30049 0.88336 0.41669 -0.07399 -0.00535 -0.07400 63  ASN A C   
986  O O   . ASN A 63  ? 0.33981 0.89859 0.45728 -0.06578 -0.00746 -0.07223 63  ASN A O   
987  C CB  . ASN A 63  ? 0.41430 0.98322 0.51852 -0.11860 0.00036  -0.08064 63  ASN A CB  
988  C CG  . ASN A 63  ? 0.39867 0.94645 0.49618 -0.13939 0.00543  -0.08227 63  ASN A CG  
989  O OD1 . ASN A 63  ? 0.39673 0.91859 0.49522 -0.13820 0.00770  -0.08019 63  ASN A OD1 
990  N ND2 . ASN A 63  ? 0.47407 1.03139 0.56336 -0.15895 0.00743  -0.08594 63  ASN A ND2 
997  N N   . HIS A 64  ? 0.30780 0.92554 0.42458 -0.06516 -0.00714 -0.07383 64  HIS A N   
998  C CA  . HIS A 64  ? 0.36148 0.98788 0.47903 -0.04621 -0.01164 -0.07137 64  HIS A CA  
999  C C   . HIS A 64  ? 0.35854 0.97609 0.47948 -0.02004 -0.01242 -0.06629 64  HIS A C   
1000 O O   . HIS A 64  ? 0.34836 0.96523 0.46808 -0.00348 -0.01588 -0.06348 64  HIS A O   
1001 C CB  . HIS A 64  ? 0.41538 1.08187 0.53108 -0.04494 -0.01313 -0.07265 64  HIS A CB  
1002 C CG  . HIS A 64  ? 0.40654 1.10157 0.52419 -0.03783 -0.01098 -0.07187 64  HIS A CG  
1003 N ND1 . HIS A 64  ? 0.44122 1.15413 0.55761 -0.05629 -0.00781 -0.07538 64  HIS A ND1 
1004 C CD2 . HIS A 64  ? 0.44218 1.15000 0.56166 -0.01415 -0.01140 -0.06800 64  HIS A CD2 
1005 C CE1 . HIS A 64  ? 0.40962 1.14826 0.52813 -0.04430 -0.00671 -0.07385 64  HIS A CE1 
1006 N NE2 . HIS A 64  ? 0.48123 1.21639 0.60139 -0.01848 -0.00876 -0.06944 64  HIS A NE2 
1014 N N   . ASN A 65  ? 0.27621 0.88454 0.39990 -0.01604 -0.00904 -0.06498 65  ASN A N   
1015 C CA  . ASN A 65  ? 0.33255 0.92401 0.45760 0.00701  -0.00908 -0.06061 65  ASN A CA  
1016 C C   . ASN A 65  ? 0.35766 0.91343 0.48328 0.00758  -0.01019 -0.05954 65  ASN A C   
1017 O O   . ASN A 65  ? 0.34873 0.88851 0.47375 0.02724  -0.01068 -0.05586 65  ASN A O   
1018 C CB  . ASN A 65  ? 0.29775 0.88852 0.42486 0.01027  -0.00472 -0.06002 65  ASN A CB  
1019 C CG  . ASN A 65  ? 0.40190 1.02794 0.52827 0.01569  -0.00386 -0.06025 65  ASN A CG  
1020 O OD1 . ASN A 65  ? 0.35809 0.99481 0.48575 0.00538  -0.00048 -0.06205 65  ASN A OD1 
1021 N ND2 . ASN A 65  ? 0.40438 1.04972 0.52797 0.03151  -0.00691 -0.05836 65  ASN A ND2 
1028 N N   . PHE A 66  ? 0.33243 0.87361 0.45780 -0.01336 -0.01022 -0.06270 66  PHE A N   
1029 C CA  . PHE A 66  ? 0.27676 0.78564 0.40254 -0.01435 -0.01138 -0.06217 66  PHE A CA  
1030 C C   . PHE A 66  ? 0.33199 0.84103 0.45470 -0.01300 -0.01616 -0.06235 66  PHE A C   
1031 O O   . PHE A 66  ? 0.33195 0.84990 0.45143 -0.02964 -0.01710 -0.06593 66  PHE A O   
1032 C CB  . PHE A 66  ? 0.29693 0.78270 0.42075 -0.03729 -0.00823 -0.06516 66  PHE A CB  
1033 C CG  . PHE A 66  ? 0.35924 0.84118 0.48464 -0.03959 -0.00336 -0.06463 66  PHE A CG  
1034 C CD1 . PHE A 66  ? 0.38499 0.83201 0.50560 -0.02771 -0.00131 -0.06092 66  PHE A CD1 
1035 C CD2 . PHE A 66  ? 0.32793 0.83193 0.45338 -0.05288 -0.00053 -0.06695 66  PHE A CD2 
1036 C CE1 . PHE A 66  ? 0.34699 0.79197 0.46849 -0.02953 0.00309  -0.06056 66  PHE A CE1 
1037 C CE2 . PHE A 66  ? 0.31017 0.81235 0.43692 -0.05465 0.00399  -0.06631 66  PHE A CE2 
1038 C CZ  . PHE A 66  ? 0.30182 0.77962 0.42907 -0.04336 0.00577  -0.06360 66  PHE A CZ  
1048 N N   . LEU A 67  ? 0.27447 0.76793 0.39471 0.00646  -0.01847 -0.05820 67  LEU A N   
1049 C CA  . LEU A 67  ? 0.29111 0.77891 0.40647 0.00986  -0.02273 -0.05737 67  LEU A CA  
1050 C C   . LEU A 67  ? 0.32602 0.76363 0.43237 0.00189  -0.02145 -0.05683 67  LEU A C   
1051 O O   . LEU A 67  ? 0.29075 0.69457 0.39258 0.01146  -0.01929 -0.05315 67  LEU A O   
1052 C CB  . LEU A 67  ? 0.38108 0.87598 0.49488 0.03662  -0.02506 -0.05208 67  LEU A CB  
1053 C CG  . LEU A 67  ? 0.41251 0.90120 0.51988 0.04677  -0.02925 -0.04925 67  LEU A CG  
1054 C CD1 . LEU A 67  ? 0.53736 1.05689 0.64499 0.03584  -0.03232 -0.05267 67  LEU A CD1 
1055 C CD2 . LEU A 67  ? 0.50739 0.99159 0.60997 0.07472  -0.02992 -0.04287 67  LEU A CD2 
1067 N N   . VAL A 68  ? 0.27430 0.70703 0.37759 -0.01626 -0.02246 -0.06082 68  VAL A N   
1068 C CA  . VAL A 68  ? 0.24727 0.63501 0.34200 -0.02384 -0.02095 -0.06067 68  VAL A CA  
1069 C C   . VAL A 68  ? 0.31781 0.70300 0.40728 -0.02239 -0.02466 -0.06091 68  VAL A C   
1070 O O   . VAL A 68  ? 0.32827 0.74152 0.41912 -0.03176 -0.02736 -0.06494 68  VAL A O   
1071 C CB  . VAL A 68  ? 0.31993 0.69488 0.41249 -0.04650 -0.01760 -0.06509 68  VAL A CB  
1072 C CG1 . VAL A 68  ? 0.36460 0.69422 0.44777 -0.05101 -0.01621 -0.06448 68  VAL A CG1 
1073 C CG2 . VAL A 68  ? 0.29646 0.67457 0.39364 -0.04793 -0.01366 -0.06443 68  VAL A CG2 
1083 N N   . GLN A 69  ? 0.30745 0.66166 0.39089 -0.01021 -0.02480 -0.05652 69  GLN A N   
1084 C CA  . GLN A 69  ? 0.40245 0.75317 0.48011 -0.00635 -0.02806 -0.05580 69  GLN A CA  
1085 C C   . GLN A 69  ? 0.41256 0.72188 0.48214 -0.01267 -0.02616 -0.05575 69  GLN A C   
1086 O O   . GLN A 69  ? 0.34085 0.62142 0.40835 -0.00532 -0.02374 -0.05195 69  GLN A O   
1087 C CB  . GLN A 69  ? 0.41171 0.76666 0.48814 0.01650  -0.03015 -0.04972 69  GLN A CB  
1088 C CG  . GLN A 69  ? 0.51565 0.91316 0.59902 0.02693  -0.03234 -0.04907 69  GLN A CG  
1089 C CD  . GLN A 69  ? 0.65011 1.04870 0.72909 0.05031  -0.03442 -0.04280 69  GLN A CD  
1090 O OE1 . GLN A 69  ? 0.69435 1.06226 0.76490 0.05727  -0.03424 -0.03900 69  GLN A OE1 
1091 N NE2 . GLN A 69  ? 0.67021 1.10455 0.75415 0.06289  -0.03617 -0.04148 69  GLN A NE2 
1100 N N   . ALA A 70  ? 0.40451 0.71239 0.46944 -0.02622 -0.02707 -0.06023 70  ALA A N   
1101 C CA  . ALA A 70  ? 0.43784 0.70993 0.49447 -0.03056 -0.02540 -0.06039 70  ALA A CA  
1102 C C   . ALA A 70  ? 0.54831 0.82457 0.60014 -0.02190 -0.02871 -0.05864 70  ALA A C   
1103 O O   . ALA A 70  ? 0.48608 0.78613 0.53676 -0.02801 -0.03172 -0.06237 70  ALA A O   
1104 C CB  . ALA A 70  ? 0.46519 0.72732 0.51735 -0.05111 -0.02324 -0.06668 70  ALA A CB  
1110 N N   . GLY A 71  ? 0.54205 0.79722 0.59076 -0.00783 -0.02820 -0.05284 71  GLY A N   
1111 C CA  . GLY A 71  ? 0.64550 0.90588 0.68914 0.00235  -0.03115 -0.04996 71  GLY A CA  
1112 C C   . GLY A 71  ? 0.67280 0.97084 0.72063 0.01150  -0.03501 -0.04877 71  GLY A C   
1113 O O   . GLY A 71  ? 0.65427 0.96163 0.70699 0.02223  -0.03474 -0.04553 71  GLY A O   
1117 N N   . ASN A 72  ? 0.73856 1.05907 0.78380 0.00836  -0.03865 -0.05134 72  ASN A N   
1118 C CA  . ASN A 72  ? 0.73263 1.09384 0.78174 0.01671  -0.04294 -0.05053 72  ASN A CA  
1119 C C   . ASN A 72  ? 0.66106 1.05638 0.71740 0.00127  -0.04426 -0.05748 72  ASN A C   
1120 O O   . ASN A 72  ? 0.66717 1.10230 0.72776 0.00578  -0.04812 -0.05787 72  ASN A O   
1121 C CB  . ASN A 72  ? 0.83129 1.20002 0.87266 0.02381  -0.04664 -0.04854 72  ASN A CB  
1122 C CG  . ASN A 72  ? 0.90415 1.26366 0.93920 0.00715  -0.04678 -0.05451 72  ASN A CG  
1123 O OD1 . ASN A 72  ? 0.89879 1.28439 0.93500 -0.00593 -0.04926 -0.06091 72  ASN A OD1 
1124 N ND2 . ASN A 72  ? 0.94781 1.27062 0.97550 0.00739  -0.04394 -0.05270 72  ASN A ND2 
1131 N N   . VAL A 73  ? 0.61542 0.99623 0.67263 -0.01671 -0.04098 -0.06270 73  VAL A N   
1132 C CA  . VAL A 73  ? 0.54150 0.94864 0.60315 -0.03530 -0.04131 -0.06981 73  VAL A CA  
1133 C C   . VAL A 73  ? 0.51516 0.93120 0.58584 -0.03415 -0.03874 -0.06874 73  VAL A C   
1134 O O   . VAL A 73  ? 0.46563 0.85110 0.53596 -0.03032 -0.03496 -0.06574 73  VAL A O   
1135 C CB  . VAL A 73  ? 0.54355 0.92405 0.59738 -0.05604 -0.03857 -0.07603 73  VAL A CB  
1136 C CG1 . VAL A 73  ? 0.57845 0.97910 0.63514 -0.07683 -0.03764 -0.08302 73  VAL A CG1 
1137 C CG2 . VAL A 73  ? 0.64634 1.01946 0.69036 -0.05789 -0.04088 -0.07799 73  VAL A CG2 
1147 N N   . GLN A 74  ? 0.53349 0.99308 0.61229 -0.03720 -0.04075 -0.07116 74  GLN A N   
1148 C CA  . GLN A 74  ? 0.44572 0.91684 0.53306 -0.03814 -0.03783 -0.07092 74  GLN A CA  
1149 C C   . GLN A 74  ? 0.45058 0.92103 0.53743 -0.06412 -0.03502 -0.07787 74  GLN A C   
1150 O O   . GLN A 74  ? 0.47809 0.96309 0.56020 -0.07724 -0.03524 -0.08212 74  GLN A O   
1151 C CB  . GLN A 74  ? 0.51315 1.02532 0.60724 -0.02386 -0.03960 -0.06814 74  GLN A CB  
1152 C CG  . GLN A 74  ? 0.58064 1.10289 0.68057 -0.02547 -0.03538 -0.06801 74  GLN A CG  
1153 C CD  . GLN A 74  ? 0.63213 1.18884 0.73328 -0.01357 -0.03529 -0.06572 74  GLN A CD  
1154 O OE1 . GLN A 74  ? 0.64746 1.21565 0.74604 0.00321  -0.03820 -0.06203 74  GLN A OE1 
1155 N NE2 . GLN A 74  ? 0.54992 1.12285 0.65391 -0.02195 -0.03175 -0.06776 74  GLN A NE2 
1164 N N   . LEU A 75  ? 0.34414 0.78545 0.43001 -0.06953 -0.03020 -0.07729 75  LEU A N   
1165 C CA  . LEU A 75  ? 0.32709 0.76293 0.41052 -0.09329 -0.02672 -0.08290 75  LEU A CA  
1166 C C   . LEU A 75  ? 0.39055 0.85608 0.47987 -0.09606 -0.02426 -0.08285 75  LEU A C   
1167 O O   . LEU A 75  ? 0.48806 0.96559 0.58547 -0.08086 -0.02400 -0.07871 75  LEU A O   
1168 C CB  . LEU A 75  ? 0.37135 0.75872 0.44839 -0.09597 -0.02185 -0.08101 75  LEU A CB  
1169 C CG  . LEU A 75  ? 0.43244 0.77894 0.49952 -0.09255 -0.02161 -0.07976 75  LEU A CG  
1170 C CD1 . LEU A 75  ? 0.38805 0.69239 0.44936 -0.09739 -0.01663 -0.07848 75  LEU A CD1 
1171 C CD2 . LEU A 75  ? 0.48705 0.84013 0.54673 -0.10655 -0.02381 -0.08584 75  LEU A CD2 
1183 N N   . ARG A 76  ? 0.32079 0.79300 0.40358 -0.11499 -0.02145 -0.08710 76  ARG A N   
1184 C CA  . ARG A 76  ? 0.39543 0.89357 0.48092 -0.11933 -0.01831 -0.08716 76  ARG A CA  
1185 C C   . ARG A 76  ? 0.36714 0.84452 0.45188 -0.12933 -0.01338 -0.08715 76  ARG A C   
1186 O O   . ARG A 76  ? 0.38415 0.83239 0.45965 -0.14662 -0.01043 -0.09005 76  ARG A O   
1187 C CB  . ARG A 76  ? 0.44606 0.96349 0.52437 -0.13508 -0.01753 -0.09164 76  ARG A CB  
1188 C CG  . ARG A 76  ? 0.51688 1.05743 0.59497 -0.14561 -0.01357 -0.09301 76  ARG A CG  
1189 C CD  . ARG A 76  ? 0.56317 1.12797 0.63507 -0.15836 -0.01359 -0.09721 76  ARG A CD  
1190 N NE  . ARG A 76  ? 0.66658 1.23911 0.73278 -0.17757 -0.00882 -0.10030 76  ARG A NE  
1191 C CZ  . ARG A 76  ? 0.70958 1.30969 0.78071 -0.17518 -0.00701 -0.09909 76  ARG A CZ  
1192 N NH1 . ARG A 76  ? 0.70858 1.33019 0.79023 -0.15348 -0.00928 -0.09479 76  ARG A NH1 
1193 N NH2 . ARG A 76  ? 0.69482 1.29966 0.75888 -0.19481 -0.00264 -0.10224 76  ARG A NH2 
1207 N N   . VAL A 77  ? 0.37584 0.86631 0.46886 -0.11772 -0.01219 -0.08367 77  VAL A N   
1208 C CA  . VAL A 77  ? 0.32090 0.79467 0.41328 -0.12645 -0.00740 -0.08329 77  VAL A CA  
1209 C C   . VAL A 77  ? 0.35506 0.84584 0.44203 -0.14322 -0.00369 -0.08605 77  VAL A C   
1210 O O   . VAL A 77  ? 0.33080 0.85774 0.42109 -0.13868 -0.00450 -0.08618 77  VAL A O   
1211 C CB  . VAL A 77  ? 0.30464 0.78398 0.40724 -0.10714 -0.00728 -0.07871 77  VAL A CB  
1212 C CG1 . VAL A 77  ? 0.34276 0.80966 0.44450 -0.11661 -0.00196 -0.07830 77  VAL A CG1 
1213 C CG2 . VAL A 77  ? 0.31777 0.77688 0.42432 -0.09219 -0.01055 -0.07616 77  VAL A CG2 
1223 N N   . ILE A 78  ? 0.35039 0.81441 0.42739 -0.16281 0.00049  -0.08830 78  ILE A N   
1224 C CA  . ILE A 78  ? 0.40014 0.87620 0.46956 -0.18083 0.00435  -0.09108 78  ILE A CA  
1225 C C   . ILE A 78  ? 0.40880 0.87187 0.47628 -0.18755 0.00924  -0.08945 78  ILE A C   
1226 O O   . ILE A 78  ? 0.38728 0.85736 0.44738 -0.20317 0.01288  -0.09143 78  ILE A O   
1227 C CB  . ILE A 78  ? 0.43377 0.89114 0.48894 -0.20035 0.00560  -0.09560 78  ILE A CB  
1228 C CG1 . ILE A 78  ? 0.42697 0.83423 0.47276 -0.20704 0.00773  -0.09545 78  ILE A CG1 
1229 C CG2 . ILE A 78  ? 0.41815 0.89300 0.47509 -0.19445 0.00093  -0.09741 78  ILE A CG2 
1230 C CD1 . ILE A 78  ? 0.50077 0.88415 0.52925 -0.22697 0.01047  -0.09974 78  ILE A CD1 
1242 N N   . GLY A 79  ? 0.37637 0.82256 0.45000 -0.17622 0.00951  -0.08587 79  GLY A N   
1243 C CA  . GLY A 79  ? 0.34509 0.78126 0.41751 -0.18087 0.01410  -0.08388 79  GLY A CA  
1244 C C   . GLY A 79  ? 0.34401 0.76432 0.42475 -0.16530 0.01351  -0.08006 79  GLY A C   
1245 O O   . GLY A 79  ? 0.29989 0.70824 0.38433 -0.15513 0.01009  -0.07941 79  GLY A O   
1249 N N   . HIS A 80  ? 0.35320 0.77370 0.43624 -0.16412 0.01711  -0.07769 80  HIS A N   
1250 C CA  . HIS A 80  ? 0.38871 0.79470 0.47917 -0.14993 0.01715  -0.07431 80  HIS A CA  
1251 C C   . HIS A 80  ? 0.40827 0.80129 0.49500 -0.15695 0.02248  -0.07232 80  HIS A C   
1252 O O   . HIS A 80  ? 0.35314 0.76288 0.43678 -0.16528 0.02532  -0.07289 80  HIS A O   
1253 C CB  . HIS A 80  ? 0.32823 0.76380 0.43190 -0.12658 0.01391  -0.07250 80  HIS A CB  
1254 C CG  . HIS A 80  ? 0.36259 0.83270 0.46974 -0.12237 0.01536  -0.07229 80  HIS A CG  
1255 N ND1 . HIS A 80  ? 0.39637 0.89862 0.50386 -0.12203 0.01312  -0.07420 80  HIS A ND1 
1256 C CD2 . HIS A 80  ? 0.31090 0.78878 0.42059 -0.11851 0.01895  -0.07057 80  HIS A CD2 
1257 C CE1 . HIS A 80  ? 0.40284 0.93137 0.51307 -0.11791 0.01508  -0.07367 80  HIS A CE1 
1258 N NE2 . HIS A 80  ? 0.31446 0.82856 0.42618 -0.11517 0.01856  -0.07149 80  HIS A NE2 
1266 N N   . SER A 81  ? 0.35580 0.71575 0.44021 -0.15256 0.02370  -0.06958 81  SER A N   
1267 C CA  . SER A 81  ? 0.37191 0.71612 0.45165 -0.15490 0.02838  -0.06661 81  SER A CA  
1268 C C   . SER A 81  ? 0.37238 0.68543 0.45028 -0.13533 0.02712  -0.06212 81  SER A C   
1269 O O   . SER A 81  ? 0.35232 0.64784 0.42965 -0.12424 0.02340  -0.06125 81  SER A O   
1270 C CB  . SER A 81  ? 0.45555 0.77168 0.52108 -0.17715 0.03266  -0.06706 81  SER A CB  
1271 O OG  . SER A 81  ? 0.42346 0.70021 0.47912 -0.17672 0.03092  -0.06651 81  SER A OG  
1277 N N   . MET A 82  ? 0.31152 0.61801 0.38774 -0.13244 0.03048  -0.05938 82  MET A N   
1278 C CA  . MET A 82  ? 0.29817 0.57844 0.37246 -0.11541 0.02955  -0.05555 82  MET A CA  
1279 C C   . MET A 82  ? 0.37184 0.61563 0.43364 -0.12491 0.03275  -0.05282 82  MET A C   
1280 O O   . MET A 82  ? 0.36593 0.61346 0.42273 -0.13995 0.03710  -0.05292 82  MET A O   
1281 C CB  . MET A 82  ? 0.33149 0.63594 0.41363 -0.10155 0.03053  -0.05480 82  MET A CB  
1282 C CG  . MET A 82  ? 0.33459 0.61446 0.41397 -0.08556 0.02986  -0.05162 82  MET A CG  
1283 S SD  . MET A 82  ? 0.37240 0.68459 0.46028 -0.06857 0.03102  -0.05211 82  MET A SD  
1284 C CE  . MET A 82  ? 0.39756 0.73703 0.48629 -0.08410 0.03693  -0.05324 82  MET A CE  
1294 N N   . GLN A 83  ? 0.33264 0.54235 0.38891 -0.11641 0.03073  -0.05023 83  GLN A N   
1295 C CA  . GLN A 83  ? 0.35460 0.52925 0.39905 -0.12108 0.03313  -0.04686 83  GLN A CA  
1296 C C   . GLN A 83  ? 0.35714 0.51785 0.40300 -0.10360 0.03134  -0.04371 83  GLN A C   
1297 O O   . GLN A 83  ? 0.32229 0.46972 0.36965 -0.09276 0.02775  -0.04311 83  GLN A O   
1298 C CB  . GLN A 83  ? 0.39937 0.54516 0.43398 -0.12945 0.03262  -0.04708 83  GLN A CB  
1299 C CG  . GLN A 83  ? 0.43702 0.54574 0.45872 -0.13093 0.03486  -0.04290 83  GLN A CG  
1300 C CD  . GLN A 83  ? 0.46993 0.54811 0.48021 -0.13736 0.03495  -0.04297 83  GLN A CD  
1301 O OE1 . GLN A 83  ? 0.46737 0.54954 0.47974 -0.13914 0.03277  -0.04625 83  GLN A OE1 
1302 N NE2 . GLN A 83  ? 0.55578 0.60278 0.55297 -0.13977 0.03755  -0.03920 83  GLN A NE2 
1311 N N   . ASN A 84  ? 0.30952 0.47285 0.35399 -0.10181 0.03403  -0.04182 84  ASN A N   
1312 C CA  . ASN A 84  ? 0.32195 0.47426 0.36713 -0.08634 0.03243  -0.03957 84  ASN A CA  
1313 C C   . ASN A 84  ? 0.29649 0.46472 0.35133 -0.07180 0.02890  -0.04155 84  ASN A C   
1314 O O   . ASN A 84  ? 0.30341 0.50225 0.36569 -0.07027 0.02947  -0.04401 84  ASN A O   
1315 C CB  . ASN A 84  ? 0.33857 0.45462 0.37466 -0.08524 0.03133  -0.03623 84  ASN A CB  
1316 C CG  . ASN A 84  ? 0.40491 0.50492 0.42965 -0.09852 0.03516  -0.03381 84  ASN A CG  
1317 O OD1 . ASN A 84  ? 0.38302 0.49270 0.40574 -0.10291 0.03849  -0.03299 84  ASN A OD1 
1318 N ND2 . ASN A 84  ? 0.36953 0.44585 0.38582 -0.10550 0.03522  -0.03280 84  ASN A ND2 
1325 N N   . CYS A 85  ? 0.26998 0.41925 0.32435 -0.06099 0.02552  -0.04036 85  CYS A N   
1326 C CA  . CYS A 85  ? 0.27138 0.43161 0.33233 -0.04675 0.02265  -0.04159 85  CYS A CA  
1327 C C   . CYS A 85  ? 0.26643 0.43038 0.33070 -0.04717 0.01972  -0.04294 85  CYS A C   
1328 O O   . CYS A 85  ? 0.24474 0.41143 0.31232 -0.03508 0.01706  -0.04308 85  CYS A O   
1329 C CB  . CYS A 85  ? 0.28365 0.42275 0.34140 -0.03484 0.02106  -0.03968 85  CYS A CB  
1330 S SG  . CYS A 85  ? 0.30235 0.44076 0.35596 -0.03279 0.02422  -0.03885 85  CYS A SG  
1336 N N   . VAL A 86  ? 0.27384 0.43798 0.33611 -0.06097 0.02039  -0.04406 86  VAL A N   
1337 C CA  . VAL A 86  ? 0.25842 0.42653 0.32279 -0.06253 0.01769  -0.04583 86  VAL A CA  
1338 C C   . VAL A 86  ? 0.26767 0.46687 0.33651 -0.07297 0.01859  -0.04920 86  VAL A C   
1339 O O   . VAL A 86  ? 0.30543 0.51268 0.37222 -0.08576 0.02197  -0.05005 86  VAL A O   
1340 C CB  . VAL A 86  ? 0.28869 0.42581 0.34494 -0.06908 0.01737  -0.04471 86  VAL A CB  
1341 C CG1 . VAL A 86  ? 0.42930 0.57140 0.48437 -0.07911 0.01670  -0.04753 86  VAL A CG1 
1342 C CG2 . VAL A 86  ? 0.31651 0.43363 0.37241 -0.05528 0.01461  -0.04226 86  VAL A CG2 
1352 N N   . LEU A 87  ? 0.25659 0.47539 0.33149 -0.06721 0.01559  -0.05098 87  LEU A N   
1353 C CA  . LEU A 87  ? 0.23406 0.48450 0.31360 -0.07704 0.01552  -0.05448 87  LEU A CA  
1354 C C   . LEU A 87  ? 0.28573 0.52442 0.35996 -0.08929 0.01427  -0.05662 87  LEU A C   
1355 O O   . LEU A 87  ? 0.27399 0.49093 0.34496 -0.08306 0.01185  -0.05555 87  LEU A O   
1356 C CB  . LEU A 87  ? 0.31666 0.59674 0.40510 -0.06182 0.01280  -0.05489 87  LEU A CB  
1357 C CG  . LEU A 87  ? 0.37372 0.69618 0.46988 -0.06540 0.01175  -0.05803 87  LEU A CG  
1358 C CD1 . LEU A 87  ? 0.38052 0.73000 0.48025 -0.07658 0.01567  -0.05981 87  LEU A CD1 
1359 C CD2 . LEU A 87  ? 0.35891 0.69841 0.46079 -0.04435 0.00876  -0.05669 87  LEU A CD2 
1371 N N   . LYS A 88  ? 0.32960 0.58153 0.40187 -0.10743 0.01630  -0.05982 88  LYS A N   
1372 C CA  . LYS A 88  ? 0.34245 0.58437 0.40794 -0.12122 0.01569  -0.06289 88  LYS A CA  
1373 C C   . LYS A 88  ? 0.33100 0.61323 0.40359 -0.12746 0.01370  -0.06713 88  LYS A C   
1374 O O   . LYS A 88  ? 0.31526 0.62493 0.39111 -0.13904 0.01594  -0.06936 88  LYS A O   
1375 C CB  . LYS A 88  ? 0.39915 0.61636 0.45264 -0.13915 0.02008  -0.06330 88  LYS A CB  
1376 C CG  . LYS A 88  ? 0.41006 0.59014 0.45661 -0.13172 0.02162  -0.05877 88  LYS A CG  
1377 C CD  . LYS A 88  ? 0.51239 0.66073 0.54409 -0.14662 0.02555  -0.05849 88  LYS A CD  
1378 C CE  . LYS A 88  ? 0.55675 0.71441 0.58577 -0.15910 0.02999  -0.05820 88  LYS A CE  
1379 N NZ  . LYS A 88  ? 0.72072 0.84311 0.73300 -0.17184 0.03420  -0.05685 88  LYS A NZ  
1393 N N   . LEU A 89  ? 0.28452 0.57253 0.35971 -0.11937 0.00944  -0.06804 89  LEU A N   
1394 C CA  . LEU A 89  ? 0.24406 0.57108 0.32572 -0.12344 0.00661  -0.07186 89  LEU A CA  
1395 C C   . LEU A 89  ? 0.34386 0.65927 0.41614 -0.14197 0.00652  -0.07635 89  LEU A C   
1396 O O   . LEU A 89  ? 0.35478 0.64183 0.42014 -0.13859 0.00505  -0.07601 89  LEU A O   
1397 C CB  . LEU A 89  ? 0.27979 0.62051 0.36846 -0.10258 0.00201  -0.06982 89  LEU A CB  
1398 C CG  . LEU A 89  ? 0.33463 0.67881 0.42939 -0.08200 0.00211  -0.06538 89  LEU A CG  
1399 C CD1 . LEU A 89  ? 0.34078 0.69192 0.43852 -0.06341 -0.00227 -0.06342 89  LEU A CD1 
1400 C CD2 . LEU A 89  ? 0.29862 0.68159 0.40173 -0.08393 0.00420  -0.06650 89  LEU A CD2 
1412 N N   . LYS A 90  ? 0.34015 0.67699 0.41134 -0.16208 0.00845  -0.08076 90  LYS A N   
1413 C CA  . LYS A 90  ? 0.40778 0.73033 0.46565 -0.17770 0.00896  -0.08462 90  LYS A CA  
1414 C C   . LYS A 90  ? 0.41101 0.76113 0.47348 -0.17151 0.00406  -0.08674 90  LYS A C   
1415 O O   . LYS A 90  ? 0.36489 0.75258 0.43668 -0.16285 0.00220  -0.08592 90  LYS A O   
1416 C CB  . LYS A 90  ? 0.39843 0.72242 0.44611 -0.19514 0.01379  -0.08597 90  LYS A CB  
1417 C CG  . LYS A 90  ? 0.49329 0.79435 0.52380 -0.21229 0.01577  -0.08972 90  LYS A CG  
1418 C CD  . LYS A 90  ? 0.60427 0.85633 0.62104 -0.21927 0.01982  -0.08842 90  LYS A CD  
1419 C CE  . LYS A 90  ? 0.69434 0.92468 0.69149 -0.23774 0.02372  -0.09152 90  LYS A CE  
1420 N NZ  . LYS A 90  ? 0.85599 1.03639 0.83771 -0.24198 0.02779  -0.08967 90  LYS A NZ  
1434 N N   . VAL A 91  ? 0.32930 0.66040 0.38458 -0.17446 0.00202  -0.08919 91  VAL A N   
1435 C CA  . VAL A 91  ? 0.36056 0.71559 0.41868 -0.16903 -0.00261 -0.09107 91  VAL A CA  
1436 C C   . VAL A 91  ? 0.44184 0.78581 0.48517 -0.18687 -0.00089 -0.09578 91  VAL A C   
1437 O O   . VAL A 91  ? 0.46373 0.77444 0.49376 -0.20066 0.00343  -0.09726 91  VAL A O   
1438 C CB  . VAL A 91  ? 0.39565 0.74361 0.45953 -0.15291 -0.00739 -0.08955 91  VAL A CB  
1439 C CG1 . VAL A 91  ? 0.40001 0.75648 0.47458 -0.13067 -0.00805 -0.08322 91  VAL A CG1 
1440 C CG2 . VAL A 91  ? 0.38791 0.68331 0.43846 -0.15450 -0.00492 -0.08882 91  VAL A CG2 
1450 N N   . ASP A 92  ? 0.38272 0.75438 0.42733 -0.18599 -0.00403 -0.09794 92  ASP A N   
1451 C CA  . ASP A 92  ? 0.59028 0.95753 0.62126 -0.20357 -0.00220 -0.10285 92  ASP A CA  
1452 C C   . ASP A 92  ? 0.54125 0.87685 0.56194 -0.20594 -0.00335 -0.10551 92  ASP A C   
1453 O O   . ASP A 92  ? 0.55183 0.88069 0.56021 -0.21972 -0.00171 -0.10976 92  ASP A O   
1454 C CB  . ASP A 92  ? 0.57232 0.98423 0.60843 -0.20225 -0.00484 -0.10428 92  ASP A CB  
1455 C CG  . ASP A 92  ? 0.59043 1.02505 0.63753 -0.18241 -0.01094 -0.10200 92  ASP A CG  
1456 O OD1 . ASP A 92  ? 0.70511 1.12836 0.75946 -0.16767 -0.01300 -0.09841 92  ASP A OD1 
1457 O OD2 . ASP A 92  ? 0.66160 1.12442 0.70909 -0.18189 -0.01342 -0.10368 92  ASP A OD2 
1462 N N   . THR A 93  ? 0.44695 0.76421 0.47183 -0.19320 -0.00581 -0.10335 93  THR A N   
1463 C CA  . THR A 93  ? 0.51361 0.80102 0.52883 -0.19335 -0.00694 -0.10580 93  THR A CA  
1464 C C   . THR A 93  ? 0.44829 0.69483 0.45914 -0.19105 -0.00436 -0.10410 93  THR A C   
1465 O O   . THR A 93  ? 0.39145 0.63927 0.41279 -0.17741 -0.00519 -0.09930 93  THR A O   
1466 C CB  . THR A 93  ? 0.47671 0.78547 0.50068 -0.17794 -0.01335 -0.10505 93  THR A CB  
1467 O OG1 . THR A 93  ? 0.50071 0.84857 0.52844 -0.17894 -0.01547 -0.10603 93  THR A OG1 
1468 C CG2 . THR A 93  ? 0.48505 0.76380 0.49737 -0.17898 -0.01427 -0.10826 93  THR A CG2 
1476 N N   . ALA A 94  ? 0.41919 0.62675 0.41307 -0.20124 -0.00049 -0.10674 94  ALA A N   
1477 C CA  . ALA A 94  ? 0.43990 0.60670 0.42782 -0.19663 0.00196  -0.10498 94  ALA A CA  
1478 C C   . ALA A 94  ? 0.44201 0.59938 0.43202 -0.17759 -0.00095 -0.10197 94  ALA A C   
1479 O O   . ALA A 94  ? 0.43187 0.59878 0.41872 -0.17892 -0.00385 -0.10578 94  ALA A O   
1480 C CB  . ALA A 94  ? 0.55316 0.67872 0.52014 -0.20946 0.00786  -0.10711 94  ALA A CB  
1486 N N   . ASN A 95  ? 0.42024 0.56011 0.41522 -0.16061 -0.00014 -0.09519 95  ASN A N   
1487 C CA  . ASN A 95  ? 0.39313 0.52475 0.39044 -0.14306 -0.00247 -0.09177 95  ASN A CA  
1488 C C   . ASN A 95  ? 0.38136 0.48114 0.36300 -0.14764 -0.00032 -0.09546 95  ASN A C   
1489 O O   . ASN A 95  ? 0.37634 0.44254 0.34777 -0.15085 0.00408  -0.09515 95  ASN A O   
1490 C CB  . ASN A 95  ? 0.37880 0.49691 0.38354 -0.12642 -0.00151 -0.08418 95  ASN A CB  
1491 C CG  . ASN A 95  ? 0.39021 0.50219 0.39781 -0.10946 -0.00370 -0.08035 95  ASN A CG  
1492 O OD1 . ASN A 95  ? 0.35778 0.47508 0.36179 -0.10903 -0.00585 -0.08294 95  ASN A OD1 
1493 N ND2 . ASN A 95  ? 0.40609 0.50675 0.41947 -0.09599 -0.00302 -0.07418 95  ASN A ND2 
1500 N N   . PRO A 96  ? 0.42073 0.52922 0.39884 -0.14775 -0.00304 -0.09904 96  PRO A N   
1501 C CA  . PRO A 96  ? 0.48821 0.56529 0.45004 -0.15188 -0.00043 -0.10309 96  PRO A CA  
1502 C C   . PRO A 96  ? 0.49798 0.54609 0.45863 -0.13578 0.00166  -0.09767 96  PRO A C   
1503 O O   . PRO A 96  ? 0.49195 0.50947 0.43862 -0.13746 0.00504  -0.10018 96  PRO A O   
1504 C CB  . PRO A 96  ? 0.54319 0.64352 0.50398 -0.15406 -0.00461 -0.10757 96  PRO A CB  
1505 C CG  . PRO A 96  ? 0.53112 0.66704 0.50922 -0.14072 -0.00951 -0.10226 96  PRO A CG  
1506 C CD  . PRO A 96  ? 0.49793 0.64430 0.48595 -0.14204 -0.00849 -0.09901 96  PRO A CD  
1514 N N   . LYS A 97  ? 0.44658 0.50358 0.42077 -0.12032 -0.00003 -0.09051 97  LYS A N   
1515 C CA  . LYS A 97  ? 0.45843 0.49246 0.43302 -0.10582 0.00168  -0.08521 97  LYS A CA  
1516 C C   . LYS A 97  ? 0.43220 0.44637 0.40688 -0.10454 0.00510  -0.08150 97  LYS A C   
1517 O O   . LYS A 97  ? 0.41170 0.41205 0.38935 -0.09224 0.00606  -0.07641 97  LYS A O   
1518 C CB  . LYS A 97  ? 0.43282 0.48552 0.41987 -0.09031 -0.00200 -0.07973 97  LYS A CB  
1519 C CG  . LYS A 97  ? 0.52230 0.59276 0.50833 -0.08855 -0.00542 -0.08203 97  LYS A CG  
1520 C CD  . LYS A 97  ? 0.60764 0.69467 0.60499 -0.07306 -0.00859 -0.07552 97  LYS A CD  
1521 C CE  . LYS A 97  ? 0.76504 0.87225 0.76180 -0.06952 -0.01235 -0.07640 97  LYS A CE  
1522 N NZ  . LYS A 97  ? 0.75312 0.88189 0.76027 -0.05684 -0.01570 -0.07053 97  LYS A NZ  
1536 N N   . THR A 98  ? 0.40569 0.41995 0.37726 -0.11723 0.00688  -0.08374 98  THR A N   
1537 C CA  . THR A 98  ? 0.42626 0.42297 0.39726 -0.11610 0.01002  -0.07985 98  THR A CA  
1538 C C   . THR A 98  ? 0.46406 0.42467 0.42288 -0.11128 0.01375  -0.07895 98  THR A C   
1539 O O   . THR A 98  ? 0.44388 0.38577 0.38760 -0.12001 0.01633  -0.08401 98  THR A O   
1540 C CB  . THR A 98  ? 0.46828 0.46719 0.43399 -0.13314 0.01222  -0.08307 98  THR A CB  
1541 O OG1 . THR A 98  ? 0.43504 0.47159 0.41229 -0.13768 0.00880  -0.08444 98  THR A OG1 
1542 C CG2 . THR A 98  ? 0.44654 0.42867 0.41178 -0.13064 0.01526  -0.07823 98  THR A CG2 
1550 N N   . PRO A 99  ? 0.44341 0.39365 0.40719 -0.09802 0.01431  -0.07302 99  PRO A N   
1551 C CA  . PRO A 99  ? 0.47599 0.39424 0.42837 -0.09246 0.01802  -0.07181 99  PRO A CA  
1552 C C   . PRO A 99  ? 0.53993 0.43599 0.48157 -0.09966 0.02202  -0.07126 99  PRO A C   
1553 O O   . PRO A 99  ? 0.51538 0.42148 0.46002 -0.10840 0.02199  -0.07109 99  PRO A O   
1554 C CB  . PRO A 99  ? 0.44289 0.36511 0.40687 -0.07620 0.01646  -0.06540 99  PRO A CB  
1555 C CG  . PRO A 99  ? 0.38428 0.32930 0.36188 -0.07627 0.01382  -0.06236 99  PRO A CG  
1556 C CD  . PRO A 99  ? 0.41754 0.38514 0.39698 -0.08725 0.01168  -0.06722 99  PRO A CD  
1564 N N   . LYS A 100 ? 0.51520 0.38092 0.44374 -0.09492 0.02574  -0.07052 100 LYS A N   
1565 C CA  . LYS A 100 ? 0.52311 0.36585 0.44191 -0.09691 0.02945  -0.06769 100 LYS A CA  
1566 C C   . LYS A 100 ? 0.55561 0.41106 0.48885 -0.08740 0.02747  -0.06091 100 LYS A C   
1567 O O   . LYS A 100 ? 0.48079 0.34522 0.42469 -0.07433 0.02520  -0.05748 100 LYS A O   
1568 C CB  . LYS A 100 ? 0.64684 0.45526 0.54866 -0.09000 0.03368  -0.06757 100 LYS A CB  
1569 C CG  . LYS A 100 ? 0.75120 0.53415 0.64242 -0.08717 0.03739  -0.06304 100 LYS A CG  
1570 C CD  . LYS A 100 ? 0.92610 0.67225 0.79567 -0.08249 0.04232  -0.06444 100 LYS A CD  
1571 C CE  . LYS A 100 ? 1.02163 0.74265 0.88047 -0.07604 0.04578  -0.05863 100 LYS A CE  
1572 N NZ  . LYS A 100 ? 1.06755 0.78532 0.92156 -0.09051 0.04712  -0.05805 100 LYS A NZ  
1586 N N   . TYR A 101 ? 0.47232 0.33009 0.40597 -0.09474 0.02833  -0.05918 101 TYR A N   
1587 C CA  . TYR A 101 ? 0.50091 0.37365 0.44864 -0.08624 0.02608  -0.05356 101 TYR A CA  
1588 C C   . TYR A 101 ? 0.50170 0.36285 0.44286 -0.09144 0.02885  -0.05057 101 TYR A C   
1589 O O   . TYR A 101 ? 0.48953 0.33589 0.41697 -0.10415 0.03227  -0.05307 101 TYR A O   
1590 C CB  . TYR A 101 ? 0.45834 0.36535 0.42287 -0.08729 0.02190  -0.05448 101 TYR A CB  
1591 C CG  . TYR A 101 ? 0.43564 0.35558 0.39914 -0.10260 0.02254  -0.05784 101 TYR A CG  
1592 C CD1 . TYR A 101 ? 0.43446 0.35842 0.39163 -0.11479 0.02282  -0.06398 101 TYR A CD1 
1593 C CD2 . TYR A 101 ? 0.45422 0.38377 0.42278 -0.10540 0.02298  -0.05513 101 TYR A CD2 
1594 C CE1 . TYR A 101 ? 0.47020 0.40928 0.42672 -0.13042 0.02348  -0.06737 101 TYR A CE1 
1595 C CE2 . TYR A 101 ? 0.45365 0.39765 0.42172 -0.11979 0.02394  -0.05814 101 TYR A CE2 
1596 C CZ  . TYR A 101 ? 0.46411 0.41396 0.42674 -0.13238 0.02410  -0.06420 101 TYR A CZ  
1597 O OH  . TYR A 101 ? 0.53975 0.50655 0.50220 -0.14775 0.02510  -0.06737 101 TYR A OH  
1607 N N   . LYS A 102 ? 0.44811 0.31609 0.39844 -0.08217 0.02743  -0.04523 102 LYS A N   
1608 C CA  . LYS A 102 ? 0.47813 0.34193 0.42508 -0.08680 0.02934  -0.04213 102 LYS A CA  
1609 C C   . LYS A 102 ? 0.45635 0.34354 0.41966 -0.07946 0.02602  -0.03885 102 LYS A C   
1610 O O   . LYS A 102 ? 0.40988 0.31025 0.38462 -0.06971 0.02274  -0.03824 102 LYS A O   
1611 C CB  . LYS A 102 ? 0.56051 0.39269 0.49203 -0.08188 0.03287  -0.03814 102 LYS A CB  
1612 C CG  . LYS A 102 ? 0.56749 0.39887 0.50528 -0.06500 0.03084  -0.03395 102 LYS A CG  
1613 C CD  . LYS A 102 ? 0.72041 0.52214 0.64250 -0.05783 0.03414  -0.03022 102 LYS A CD  
1614 C CE  . LYS A 102 ? 0.68793 0.49609 0.61896 -0.04161 0.03161  -0.02667 102 LYS A CE  
1615 N NZ  . LYS A 102 ? 0.80621 0.59124 0.72455 -0.03119 0.03414  -0.02260 102 LYS A NZ  
1629 N N   . PHE A 103 ? 0.40973 0.30162 0.37304 -0.08501 0.02721  -0.03703 103 PHE A N   
1630 C CA  . PHE A 103 ? 0.39272 0.30265 0.36848 -0.07811 0.02483  -0.03389 103 PHE A CA  
1631 C C   . PHE A 103 ? 0.39660 0.28956 0.36622 -0.07104 0.02601  -0.02841 103 PHE A C   
1632 O O   . PHE A 103 ? 0.45563 0.32919 0.41160 -0.07654 0.02954  -0.02667 103 PHE A O   
1633 C CB  . PHE A 103 ? 0.38185 0.31208 0.36235 -0.08817 0.02541  -0.03563 103 PHE A CB  
1634 C CG  . PHE A 103 ? 0.39750 0.35050 0.38555 -0.09426 0.02374  -0.04070 103 PHE A CG  
1635 C CD1 . PHE A 103 ? 0.40506 0.36246 0.39763 -0.08888 0.02109  -0.04293 103 PHE A CD1 
1636 C CD2 . PHE A 103 ? 0.41173 0.38446 0.40259 -0.10517 0.02483  -0.04298 103 PHE A CD2 
1637 C CE1 . PHE A 103 ? 0.35971 0.33957 0.35869 -0.09374 0.01924  -0.04718 103 PHE A CE1 
1638 C CE2 . PHE A 103 ? 0.39240 0.39022 0.39099 -0.10973 0.02290  -0.04739 103 PHE A CE2 
1639 C CZ  . PHE A 103 ? 0.44393 0.44452 0.44611 -0.10377 0.01997  -0.04938 103 PHE A CZ  
1649 N N   . VAL A 104 ? 0.36547 0.26625 0.34434 -0.05949 0.02311  -0.02557 104 VAL A N   
1650 C CA  . VAL A 104 ? 0.41440 0.30380 0.38881 -0.05225 0.02347  -0.02041 104 VAL A CA  
1651 C C   . VAL A 104 ? 0.38131 0.28963 0.36734 -0.04741 0.02068  -0.01897 104 VAL A C   
1652 O O   . VAL A 104 ? 0.41375 0.33745 0.41102 -0.04309 0.01779  -0.02073 104 VAL A O   
1653 C CB  . VAL A 104 ? 0.41154 0.28766 0.38287 -0.04151 0.02285  -0.01836 104 VAL A CB  
1654 C CG1 . VAL A 104 ? 0.52082 0.38846 0.48769 -0.03339 0.02283  -0.01275 104 VAL A CG1 
1655 C CG2 . VAL A 104 ? 0.50966 0.36593 0.46855 -0.04513 0.02582  -0.02054 104 VAL A CG2 
1665 N N   . ARG A 105 ? 0.37713 0.28211 0.35897 -0.04724 0.02162  -0.01554 105 ARG A N   
1666 C CA  . ARG A 105 ? 0.36899 0.28872 0.35945 -0.04218 0.01918  -0.01428 105 ARG A CA  
1667 C C   . ARG A 105 ? 0.35456 0.26710 0.34409 -0.03204 0.01732  -0.01056 105 ARG A C   
1668 O O   . ARG A 105 ? 0.40384 0.30000 0.38271 -0.03005 0.01900  -0.00699 105 ARG A O   
1669 C CB  . ARG A 105 ? 0.39014 0.31287 0.37654 -0.04796 0.02122  -0.01291 105 ARG A CB  
1670 C CG  . ARG A 105 ? 0.41099 0.34843 0.40520 -0.04272 0.01887  -0.01241 105 ARG A CG  
1671 C CD  . ARG A 105 ? 0.44429 0.38691 0.43455 -0.04894 0.02135  -0.01163 105 ARG A CD  
1672 N NE  . ARG A 105 ? 0.39884 0.35391 0.39514 -0.04338 0.01925  -0.01168 105 ARG A NE  
1673 C CZ  . ARG A 105 ? 0.36208 0.33432 0.36729 -0.04236 0.01830  -0.01523 105 ARG A CZ  
1674 N NH1 . ARG A 105 ? 0.35798 0.33996 0.36879 -0.04550 0.01865  -0.01870 105 ARG A NH1 
1675 N NH2 . ARG A 105 ? 0.39079 0.37031 0.39830 -0.03768 0.01702  -0.01535 105 ARG A NH2 
1689 N N   . ILE A 106 ? 0.34617 0.27063 0.34587 -0.02569 0.01403  -0.01132 106 ILE A N   
1690 C CA  . ILE A 106 ? 0.36582 0.28780 0.36627 -0.01698 0.01199  -0.00838 106 ILE A CA  
1691 C C   . ILE A 106 ? 0.37008 0.29903 0.37171 -0.01444 0.01029  -0.00615 106 ILE A C   
1692 O O   . ILE A 106 ? 0.36921 0.30566 0.37227 -0.01841 0.01053  -0.00734 106 ILE A O   
1693 C CB  . ILE A 106 ? 0.30120 0.23063 0.31040 -0.01288 0.00979  -0.01044 106 ILE A CB  
1694 C CG1 . ILE A 106 ? 0.32440 0.26865 0.34263 -0.01448 0.00796  -0.01335 106 ILE A CG1 
1695 C CG2 . ILE A 106 ? 0.32560 0.24676 0.33156 -0.01508 0.01163  -0.01248 106 ILE A CG2 
1696 C CD1 . ILE A 106 ? 0.35281 0.30344 0.37841 -0.01047 0.00581  -0.01463 106 ILE A CD1 
1708 N N   . GLN A 107 ? 0.37607 0.30317 0.37621 -0.00765 0.00872  -0.00288 107 GLN A N   
1709 C CA  . GLN A 107 ? 0.37833 0.31293 0.37913 -0.00471 0.00650  -0.00077 107 GLN A CA  
1710 C C   . GLN A 107 ? 0.33589 0.28380 0.34653 -0.00247 0.00324  -0.00291 107 GLN A C   
1711 O O   . GLN A 107 ? 0.33948 0.28899 0.35513 -0.00062 0.00266  -0.00421 107 GLN A O   
1712 C CB  . GLN A 107 ? 0.41349 0.33974 0.40595 0.00177  0.00655  0.00443  107 GLN A CB  
1713 C CG  . GLN A 107 ? 0.49538 0.40438 0.47496 -0.00096 0.01030  0.00704  107 GLN A CG  
1714 C CD  . GLN A 107 ? 0.56540 0.47720 0.54168 -0.00681 0.01119  0.00736  107 GLN A CD  
1715 O OE1 . GLN A 107 ? 0.56342 0.48527 0.54167 -0.00459 0.00882  0.00843  107 GLN A OE1 
1716 N NE2 . GLN A 107 ? 0.62771 0.53212 0.59891 -0.01499 0.01469  0.00606  107 GLN A NE2 
1725 N N   . PRO A 108 ? 0.33746 0.29402 0.34986 -0.00312 0.00133  -0.00343 108 PRO A N   
1726 C CA  . PRO A 108 ? 0.34134 0.30788 0.36060 -0.00205 -0.00152 -0.00533 108 PRO A CA  
1727 C C   . PRO A 108 ? 0.36482 0.33419 0.38588 0.00305  -0.00305 -0.00281 108 PRO A C   
1728 O O   . PRO A 108 ? 0.35124 0.31766 0.36727 0.00762  -0.00295 0.00110  108 PRO A O   
1729 C CB  . PRO A 108 ? 0.36908 0.34163 0.38623 -0.00365 -0.00303 -0.00581 108 PRO A CB  
1730 C CG  . PRO A 108 ? 0.46333 0.43028 0.47277 -0.00414 -0.00121 -0.00313 108 PRO A CG  
1731 C CD  . PRO A 108 ? 0.40769 0.36471 0.41480 -0.00562 0.00196  -0.00264 108 PRO A CD  
1739 N N   . GLY A 109 ? 0.31229 0.28734 0.33988 0.00273  -0.00414 -0.00484 109 GLY A N   
1740 C CA  . GLY A 109 ? 0.33141 0.31179 0.36216 0.00712  -0.00507 -0.00303 109 GLY A CA  
1741 C C   . GLY A 109 ? 0.33178 0.30512 0.36310 0.00935  -0.00285 -0.00320 109 GLY A C   
1742 O O   . GLY A 109 ? 0.33039 0.30956 0.36597 0.01180  -0.00324 -0.00304 109 GLY A O   
1746 N N   . GLN A 110 ? 0.30435 0.26630 0.33135 0.00758  -0.00042 -0.00399 110 GLN A N   
1747 C CA  . GLN A 110 ? 0.28726 0.24166 0.31331 0.00868  0.00170  -0.00483 110 GLN A CA  
1748 C C   . GLN A 110 ? 0.30227 0.26228 0.33506 0.00571  0.00117  -0.00811 110 GLN A C   
1749 O O   . GLN A 110 ? 0.28963 0.25417 0.32540 0.00191  0.00013  -0.01013 110 GLN A O   
1750 C CB  . GLN A 110 ? 0.30401 0.24541 0.32267 0.00532  0.00441  -0.00532 110 GLN A CB  
1751 C CG  . GLN A 110 ? 0.32315 0.25564 0.33914 0.00536  0.00664  -0.00687 110 GLN A CG  
1752 C CD  . GLN A 110 ? 0.36924 0.29609 0.38112 0.01325  0.00753  -0.00424 110 GLN A CD  
1753 O OE1 . GLN A 110 ? 0.35290 0.28733 0.37032 0.01708  0.00678  -0.00464 110 GLN A OE1 
1754 N NE2 . GLN A 110 ? 0.36126 0.27427 0.36242 0.01625  0.00954  -0.00136 110 GLN A NE2 
1763 N N   . THR A 111 ? 0.31334 0.27239 0.34744 0.00824  0.00208  -0.00843 111 THR A N   
1764 C CA  . THR A 111 ? 0.29177 0.25469 0.33064 0.00580  0.00188  -0.01099 111 THR A CA  
1765 C C   . THR A 111 ? 0.30276 0.25804 0.33866 0.00379  0.00377  -0.01321 111 THR A C   
1766 O O   . THR A 111 ? 0.30951 0.25519 0.33916 0.00402  0.00561  -0.01295 111 THR A O   
1767 C CB  . THR A 111 ? 0.29409 0.26395 0.33675 0.00913  0.00159  -0.00999 111 THR A CB  
1768 O OG1 . THR A 111 ? 0.31268 0.27668 0.35127 0.01438  0.00351  -0.00875 111 THR A OG1 
1769 C CG2 . THR A 111 ? 0.31985 0.30033 0.36576 0.00934  -0.00060 -0.00825 111 THR A CG2 
1777 N N   . PHE A 112 ? 0.30848 0.26760 0.34779 0.00158  0.00335  -0.01540 112 PHE A N   
1778 C CA  . PHE A 112 ? 0.29157 0.24711 0.32878 -0.00062 0.00460  -0.01785 112 PHE A CA  
1779 C C   . PHE A 112 ? 0.27920 0.24086 0.32034 -0.00065 0.00370  -0.01904 112 PHE A C   
1780 O O   . PHE A 112 ? 0.29871 0.26497 0.34301 -0.00021 0.00242  -0.01825 112 PHE A O   
1781 C CB  . PHE A 112 ? 0.29668 0.25080 0.33147 -0.00522 0.00509  -0.01940 112 PHE A CB  
1782 C CG  . PHE A 112 ? 0.28166 0.24310 0.32001 -0.00623 0.00364  -0.01963 112 PHE A CG  
1783 C CD1 . PHE A 112 ? 0.33030 0.29164 0.36797 -0.00582 0.00312  -0.01792 112 PHE A CD1 
1784 C CD2 . PHE A 112 ? 0.27244 0.24044 0.31373 -0.00661 0.00287  -0.02149 112 PHE A CD2 
1785 C CE1 . PHE A 112 ? 0.34747 0.31417 0.38692 -0.00651 0.00214  -0.01868 112 PHE A CE1 
1786 C CE2 . PHE A 112 ? 0.32733 0.30009 0.37009 -0.00622 0.00206  -0.02191 112 PHE A CE2 
1787 C CZ  . PHE A 112 ? 0.33503 0.30662 0.37675 -0.00638 0.00179  -0.02078 112 PHE A CZ  
1797 N N   . SER A 113 ? 0.26737 0.22792 0.30687 -0.00156 0.00450  -0.02098 113 SER A N   
1798 C CA  . SER A 113 ? 0.26568 0.23144 0.30724 -0.00124 0.00374  -0.02185 113 SER A CA  
1799 C C   . SER A 113 ? 0.28862 0.25932 0.33084 -0.00329 0.00282  -0.02350 113 SER A C   
1800 O O   . SER A 113 ? 0.28723 0.25806 0.32783 -0.00655 0.00333  -0.02505 113 SER A O   
1801 C CB  . SER A 113 ? 0.27450 0.23817 0.31327 -0.00091 0.00491  -0.02330 113 SER A CB  
1802 O OG  . SER A 113 ? 0.27668 0.23650 0.31436 0.00230  0.00627  -0.02189 113 SER A OG  
1808 N N   . VAL A 114 ? 0.26153 0.23627 0.30535 -0.00124 0.00173  -0.02301 114 VAL A N   
1809 C CA  . VAL A 114 ? 0.24825 0.22943 0.29246 -0.00071 0.00088  -0.02425 114 VAL A CA  
1810 C C   . VAL A 114 ? 0.25796 0.24304 0.30113 0.00126  0.00036  -0.02463 114 VAL A C   
1811 O O   . VAL A 114 ? 0.25259 0.23425 0.29469 0.00349  0.00041  -0.02289 114 VAL A O   
1812 C CB  . VAL A 114 ? 0.25854 0.23894 0.30297 0.00176  0.00029  -0.02317 114 VAL A CB  
1813 C CG1 . VAL A 114 ? 0.25401 0.24158 0.29792 0.00513  -0.00035 -0.02416 114 VAL A CG1 
1814 C CG2 . VAL A 114 ? 0.31146 0.28960 0.35641 -0.00045 0.00062  -0.02301 114 VAL A CG2 
1824 N N   . LEU A 115 ? 0.25402 0.24736 0.29713 -0.00007 -0.00012 -0.02682 115 LEU A N   
1825 C CA  . LEU A 115 ? 0.25034 0.25055 0.29222 0.00256  -0.00118 -0.02713 115 LEU A CA  
1826 C C   . LEU A 115 ? 0.25984 0.26812 0.30242 0.00730  -0.00229 -0.02663 115 LEU A C   
1827 O O   . LEU A 115 ? 0.26746 0.28683 0.31211 0.00598  -0.00270 -0.02857 115 LEU A O   
1828 C CB  . LEU A 115 ? 0.23903 0.24471 0.27972 -0.00229 -0.00115 -0.03022 115 LEU A CB  
1829 C CG  . LEU A 115 ? 0.25841 0.27369 0.29760 0.00056  -0.00269 -0.03058 115 LEU A CG  
1830 C CD1 . LEU A 115 ? 0.25913 0.26660 0.29524 0.00400  -0.00226 -0.02827 115 LEU A CD1 
1831 C CD2 . LEU A 115 ? 0.29843 0.32170 0.33626 -0.00559 -0.00299 -0.03446 115 LEU A CD2 
1843 N N   . ALA A 116 ? 0.25954 0.26152 0.29970 0.01271  -0.00238 -0.02402 116 ALA A N   
1844 C CA  . ALA A 116 ? 0.26863 0.27480 0.30725 0.01913  -0.00295 -0.02332 116 ALA A CA  
1845 C C   . ALA A 116 ? 0.27795 0.29588 0.31523 0.02367  -0.00436 -0.02329 116 ALA A C   
1846 O O   . ALA A 116 ? 0.29104 0.30568 0.32507 0.02497  -0.00467 -0.02178 116 ALA A O   
1847 C CB  . ALA A 116 ? 0.28673 0.27858 0.32028 0.02299  -0.00219 -0.02065 116 ALA A CB  
1853 N N   . CYS A 117 ? 0.23492 0.26834 0.27466 0.02622  -0.00519 -0.02486 117 CYS A N   
1854 C CA  . CYS A 117 ? 0.26047 0.31079 0.30022 0.03013  -0.00697 -0.02530 117 CYS A CA  
1855 C C   . CYS A 117 ? 0.31207 0.37120 0.35053 0.04033  -0.00737 -0.02417 117 CYS A C   
1856 O O   . CYS A 117 ? 0.26077 0.31851 0.30041 0.04177  -0.00616 -0.02473 117 CYS A O   
1857 C CB  . CYS A 117 ? 0.27836 0.34572 0.32317 0.02180  -0.00770 -0.02921 117 CYS A CB  
1858 S SG  . CYS A 117 ? 0.28666 0.34319 0.33078 0.01102  -0.00683 -0.03117 117 CYS A SG  
1864 N N   . TYR A 118 ? 0.29066 0.36071 0.32638 0.04786  -0.00908 -0.02274 118 TYR A N   
1865 C CA  . TYR A 118 ? 0.28833 0.36988 0.32199 0.06003  -0.00964 -0.02136 118 TYR A CA  
1866 C C   . TYR A 118 ? 0.29310 0.40135 0.32992 0.06140  -0.01231 -0.02250 118 TYR A C   
1867 O O   . TYR A 118 ? 0.28062 0.38915 0.31527 0.05893  -0.01373 -0.02200 118 TYR A O   
1868 C CB  . TYR A 118 ? 0.34026 0.40193 0.36310 0.07145  -0.00875 -0.01683 118 TYR A CB  
1869 C CG  . TYR A 118 ? 0.31678 0.35356 0.33631 0.06792  -0.00627 -0.01643 118 TYR A CG  
1870 C CD1 . TYR A 118 ? 0.32091 0.35432 0.33942 0.07200  -0.00476 -0.01730 118 TYR A CD1 
1871 C CD2 . TYR A 118 ? 0.30780 0.32765 0.32612 0.05944  -0.00550 -0.01575 118 TYR A CD2 
1872 C CE1 . TYR A 118 ? 0.32918 0.34193 0.34471 0.06753  -0.00281 -0.01755 118 TYR A CE1 
1873 C CE2 . TYR A 118 ? 0.34167 0.34289 0.35797 0.05516  -0.00361 -0.01576 118 TYR A CE2 
1874 C CZ  . TYR A 118 ? 0.35022 0.34785 0.36489 0.05892  -0.00245 -0.01671 118 TYR A CZ  
1875 O OH  . TYR A 118 ? 0.33790 0.31853 0.35019 0.05392  -0.00089 -0.01712 118 TYR A OH  
1885 N N   . ASN A 119 ? 0.30922 0.44150 0.35123 0.06461  -0.01293 -0.02434 119 ASN A N   
1886 C CA  . ASN A 119 ? 0.33426 0.49680 0.37987 0.06583  -0.01577 -0.02569 119 ASN A CA  
1887 C C   . ASN A 119 ? 0.32700 0.49577 0.37617 0.05084  -0.01692 -0.02933 119 ASN A C   
1888 O O   . ASN A 119 ? 0.34737 0.53170 0.39577 0.05093  -0.01952 -0.02982 119 ASN A O   
1889 C CB  . ASN A 119 ? 0.33879 0.50212 0.37656 0.08060  -0.01750 -0.02123 119 ASN A CB  
1890 C CG  . ASN A 119 ? 0.43487 0.59457 0.46761 0.09680  -0.01617 -0.01810 119 ASN A CG  
1891 O OD1 . ASN A 119 ? 0.52484 0.65799 0.54771 0.10458  -0.01457 -0.01433 119 ASN A OD1 
1892 N ND2 . ASN A 119 ? 0.52044 0.70640 0.55946 0.10113  -0.01639 -0.02004 119 ASN A ND2 
1899 N N   . GLY A 120 ? 0.27438 0.43025 0.32614 0.03835  -0.01493 -0.03193 120 GLY A N   
1900 C CA  . GLY A 120 ? 0.29098 0.44800 0.34390 0.02424  -0.01525 -0.03567 120 GLY A CA  
1901 C C   . GLY A 120 ? 0.33324 0.47033 0.38023 0.02288  -0.01529 -0.03436 120 GLY A C   
1902 O O   . GLY A 120 ? 0.35016 0.48602 0.39639 0.01225  -0.01528 -0.03766 120 GLY A O   
1906 N N   . SER A 121 ? 0.29360 0.41464 0.33537 0.03299  -0.01497 -0.02979 121 SER A N   
1907 C CA  . SER A 121 ? 0.32157 0.42553 0.35761 0.03206  -0.01465 -0.02811 121 SER A CA  
1908 C C   . SER A 121 ? 0.28517 0.36280 0.31925 0.03147  -0.01196 -0.02587 121 SER A C   
1909 O O   . SER A 121 ? 0.29234 0.36211 0.32586 0.03722  -0.01092 -0.02364 121 SER A O   
1910 C CB  . SER A 121 ? 0.37918 0.48766 0.40911 0.04306  -0.01650 -0.02429 121 SER A CB  
1911 O OG  . SER A 121 ? 0.40976 0.54589 0.44192 0.04327  -0.01945 -0.02657 121 SER A OG  
1917 N N   . PRO A 122 ? 0.35576 0.42055 0.38842 0.02467  -0.01073 -0.02669 122 PRO A N   
1918 C CA  . PRO A 122 ? 0.32403 0.36795 0.35598 0.02324  -0.00835 -0.02487 122 PRO A CA  
1919 C C   . PRO A 122 ? 0.33162 0.36255 0.35767 0.03066  -0.00769 -0.02016 122 PRO A C   
1920 O O   . PRO A 122 ? 0.35380 0.38555 0.37462 0.03475  -0.00839 -0.01801 122 PRO A O   
1921 C CB  . PRO A 122 ? 0.37800 0.41605 0.40961 0.01522  -0.00730 -0.02725 122 PRO A CB  
1922 C CG  . PRO A 122 ? 0.41098 0.46007 0.43897 0.01616  -0.00904 -0.02811 122 PRO A CG  
1923 C CD  . PRO A 122 ? 0.35851 0.42809 0.38929 0.01865  -0.01142 -0.02938 122 PRO A CD  
1931 N N   . SER A 123 ? 0.31140 0.32926 0.33717 0.03157  -0.00615 -0.01856 123 SER A N   
1932 C CA  . SER A 123 ? 0.33841 0.34067 0.35716 0.03598  -0.00493 -0.01446 123 SER A CA  
1933 C C   . SER A 123 ? 0.38110 0.37107 0.40012 0.02941  -0.00304 -0.01391 123 SER A C   
1934 O O   . SER A 123 ? 0.35582 0.33768 0.36927 0.03009  -0.00201 -0.01105 123 SER A O   
1935 C CB  . SER A 123 ? 0.39316 0.38788 0.40909 0.04139  -0.00429 -0.01319 123 SER A CB  
1936 O OG  . SER A 123 ? 0.47078 0.44615 0.47833 0.04319  -0.00252 -0.00973 123 SER A OG  
1942 N N   . GLY A 124 ? 0.32368 0.31357 0.34871 0.02327  -0.00246 -0.01640 124 GLY A N   
1943 C CA  . GLY A 124 ? 0.32698 0.30786 0.35279 0.01843  -0.00074 -0.01567 124 GLY A CA  
1944 C C   . GLY A 124 ? 0.28785 0.27045 0.31964 0.01351  -0.00046 -0.01829 124 GLY A C   
1945 O O   . GLY A 124 ? 0.27788 0.26595 0.31250 0.01304  -0.00126 -0.02032 124 GLY A O   
1949 N N   . VAL A 125 ? 0.27889 0.25695 0.31208 0.01020  0.00091  -0.01787 125 VAL A N   
1950 C CA  . VAL A 125 ? 0.27057 0.24857 0.30780 0.00690  0.00136  -0.01959 125 VAL A CA  
1951 C C   . VAL A 125 ? 0.28921 0.26213 0.32771 0.00549  0.00221  -0.01767 125 VAL A C   
1952 O O   . VAL A 125 ? 0.31323 0.28406 0.35007 0.00521  0.00315  -0.01566 125 VAL A O   
1953 C CB  . VAL A 125 ? 0.33188 0.31177 0.36891 0.00514  0.00215  -0.02171 125 VAL A CB  
1954 C CG1 . VAL A 125 ? 0.41907 0.39738 0.45442 0.00591  0.00358  -0.02033 125 VAL A CG1 
1955 C CG2 . VAL A 125 ? 0.31240 0.28937 0.35124 0.00266  0.00287  -0.02313 125 VAL A CG2 
1965 N N   . TYR A 126 ? 0.25037 0.22240 0.29128 0.00414  0.00184  -0.01819 126 TYR A N   
1966 C CA  . TYR A 126 ? 0.28106 0.25099 0.32341 0.00225  0.00219  -0.01674 126 TYR A CA  
1967 C C   . TYR A 126 ? 0.31337 0.28443 0.35844 0.00132  0.00195  -0.01749 126 TYR A C   
1968 O O   . TYR A 126 ? 0.28838 0.25978 0.33341 0.00136  0.00173  -0.01905 126 TYR A O   
1969 C CB  . TYR A 126 ? 0.28337 0.24822 0.32265 0.00168  0.00179  -0.01578 126 TYR A CB  
1970 C CG  . TYR A 126 ? 0.29520 0.25875 0.33298 0.00382  0.00091  -0.01713 126 TYR A CG  
1971 C CD1 . TYR A 126 ? 0.28927 0.25358 0.32885 0.00259  0.00041  -0.01823 126 TYR A CD1 
1972 C CD2 . TYR A 126 ? 0.32657 0.28951 0.36074 0.00790  0.00068  -0.01712 126 TYR A CD2 
1973 C CE1 . TYR A 126 ? 0.30057 0.26517 0.33864 0.00489  0.00004  -0.01958 126 TYR A CE1 
1974 C CE2 . TYR A 126 ? 0.34431 0.30844 0.37734 0.01102  0.00014  -0.01833 126 TYR A CE2 
1975 C CZ  . TYR A 126 ? 0.33592 0.30109 0.37112 0.00926  -0.00001 -0.01969 126 TYR A CZ  
1976 O OH  . TYR A 126 ? 0.36571 0.33390 0.39984 0.01275  -0.00015 -0.02101 126 TYR A OH  
1986 N N   . GLN A 127 ? 0.30017 0.27264 0.34709 0.00020  0.00208  -0.01617 127 GLN A N   
1987 C CA  . GLN A 127 ? 0.29947 0.27300 0.34795 0.00032  0.00174  -0.01608 127 GLN A CA  
1988 C C   . GLN A 127 ? 0.34770 0.32019 0.39565 -0.00150 0.00050  -0.01633 127 GLN A C   
1989 O O   . GLN A 127 ? 0.34865 0.31974 0.39525 -0.00335 0.00012  -0.01616 127 GLN A O   
1990 C CB  . GLN A 127 ? 0.41429 0.39300 0.46515 0.00122  0.00218  -0.01436 127 GLN A CB  
1991 C CG  . GLN A 127 ? 0.38825 0.36689 0.43858 0.00480  0.00379  -0.01433 127 GLN A CG  
1992 C CD  . GLN A 127 ? 0.32958 0.30178 0.37683 0.00638  0.00423  -0.01516 127 GLN A CD  
1993 O OE1 . GLN A 127 ? 0.37889 0.34590 0.42316 0.00557  0.00492  -0.01708 127 GLN A OE1 
1994 N NE2 . GLN A 127 ? 0.37539 0.34802 0.42247 0.00820  0.00390  -0.01362 127 GLN A NE2 
2003 N N   . CYS A 128 ? 0.32407 0.29594 0.37173 -0.00126 0.00023  -0.01676 128 CYS A N   
2004 C CA  . CYS A 128 ? 0.32067 0.29205 0.36722 -0.00269 -0.00071 -0.01724 128 CYS A CA  
2005 C C   . CYS A 128 ? 0.33829 0.31092 0.38480 -0.00229 -0.00094 -0.01607 128 CYS A C   
2006 O O   . CYS A 128 ? 0.34417 0.31594 0.39056 -0.00033 -0.00008 -0.01506 128 CYS A O   
2007 C CB  . CYS A 128 ? 0.34941 0.31936 0.39438 -0.00230 -0.00043 -0.01906 128 CYS A CB  
2008 S SG  . CYS A 128 ? 0.56581 0.53265 0.60768 -0.00159 -0.00077 -0.02020 128 CYS A SG  
2014 N N   . ALA A 129 ? 0.36745 0.34108 0.41280 -0.00363 -0.00193 -0.01611 129 ALA A N   
2015 C CA  . ALA A 129 ? 0.30080 0.27535 0.34472 -0.00288 -0.00227 -0.01458 129 ALA A CA  
2016 C C   . ALA A 129 ? 0.31370 0.28662 0.35486 -0.00448 -0.00219 -0.01586 129 ALA A C   
2017 O O   . ALA A 129 ? 0.32784 0.30045 0.36834 -0.00569 -0.00244 -0.01787 129 ALA A O   
2018 C CB  . ALA A 129 ? 0.33065 0.31184 0.37573 -0.00277 -0.00391 -0.01290 129 ALA A CB  
2024 N N   . MET A 130 ? 0.27401 0.24497 0.31249 -0.00417 -0.00145 -0.01463 130 MET A N   
2025 C CA  . MET A 130 ? 0.27470 0.24599 0.31026 -0.00587 -0.00125 -0.01535 130 MET A CA  
2026 C C   . MET A 130 ? 0.28261 0.25763 0.31694 -0.00608 -0.00320 -0.01468 130 MET A C   
2027 O O   . MET A 130 ? 0.31122 0.28830 0.34469 -0.00439 -0.00416 -0.01197 130 MET A O   
2028 C CB  . MET A 130 ? 0.29125 0.25822 0.32296 -0.00664 0.00059  -0.01393 130 MET A CB  
2029 C CG  . MET A 130 ? 0.29241 0.26059 0.32033 -0.00901 0.00144  -0.01421 130 MET A CG  
2030 S SD  . MET A 130 ? 0.33802 0.31201 0.36865 -0.01032 0.00220  -0.01827 130 MET A SD  
2031 C CE  . MET A 130 ? 0.31450 0.28862 0.34770 -0.01176 0.00367  -0.01944 130 MET A CE  
2041 N N   . ARG A 131 ? 0.29612 0.27212 0.32955 -0.00780 -0.00381 -0.01722 131 ARG A N   
2042 C CA  . ARG A 131 ? 0.28841 0.26788 0.31958 -0.00950 -0.00577 -0.01747 131 ARG A CA  
2043 C C   . ARG A 131 ? 0.31941 0.30050 0.34653 -0.00929 -0.00585 -0.01607 131 ARG A C   
2044 O O   . ARG A 131 ? 0.31013 0.28854 0.33542 -0.00891 -0.00390 -0.01574 131 ARG A O   
2045 C CB  . ARG A 131 ? 0.29119 0.26751 0.31958 -0.01169 -0.00585 -0.02109 131 ARG A CB  
2046 C CG  . ARG A 131 ? 0.33995 0.31201 0.37017 -0.01176 -0.00532 -0.02217 131 ARG A CG  
2047 C CD  . ARG A 131 ? 0.33840 0.31480 0.37219 -0.01356 -0.00660 -0.02041 131 ARG A CD  
2048 N NE  . ARG A 131 ? 0.32237 0.30511 0.35473 -0.01693 -0.00869 -0.02035 131 ARG A NE  
2049 C CZ  . ARG A 131 ? 0.36089 0.35250 0.39677 -0.01856 -0.01013 -0.01869 131 ARG A CZ  
2050 N NH1 . ARG A 131 ? 0.32686 0.32061 0.36737 -0.01689 -0.00937 -0.01702 131 ARG A NH1 
2051 N NH2 . ARG A 131 ? 0.35467 0.35510 0.38940 -0.02167 -0.01238 -0.01872 131 ARG A NH2 
2065 N N   . PRO A 132 ? 0.31825 0.30474 0.34345 -0.01017 -0.00807 -0.01524 132 PRO A N   
2066 C CA  . PRO A 132 ? 0.31894 0.30720 0.33900 -0.00985 -0.00834 -0.01376 132 PRO A CA  
2067 C C   . PRO A 132 ? 0.33791 0.32297 0.35393 -0.01152 -0.00659 -0.01669 132 PRO A C   
2068 O O   . PRO A 132 ? 0.34176 0.32655 0.35383 -0.01117 -0.00541 -0.01506 132 PRO A O   
2069 C CB  . PRO A 132 ? 0.34443 0.34148 0.36352 -0.01133 -0.01160 -0.01356 132 PRO A CB  
2070 C CG  . PRO A 132 ? 0.34614 0.34788 0.37145 -0.01063 -0.01269 -0.01250 132 PRO A CG  
2071 C CD  . PRO A 132 ? 0.32267 0.31581 0.35043 -0.01178 -0.01045 -0.01524 132 PRO A CD  
2079 N N   . ASN A 133 ? 0.31664 0.29893 0.33258 -0.01286 -0.00606 -0.02076 133 ASN A N   
2080 C CA  . ASN A 133 ? 0.33599 0.31625 0.34789 -0.01270 -0.00401 -0.02370 133 ASN A CA  
2081 C C   . ASN A 133 ? 0.38311 0.36253 0.39820 -0.01078 -0.00127 -0.02390 133 ASN A C   
2082 O O   . ASN A 133 ? 0.32895 0.30871 0.34212 -0.00943 0.00062  -0.02675 133 ASN A O   
2083 C CB  . ASN A 133 ? 0.35041 0.32634 0.35813 -0.01392 -0.00445 -0.02811 133 ASN A CB  
2084 C CG  . ASN A 133 ? 0.36172 0.33187 0.37212 -0.01318 -0.00412 -0.02938 133 ASN A CG  
2085 O OD1 . ASN A 133 ? 0.32468 0.29585 0.34094 -0.01174 -0.00381 -0.02720 133 ASN A OD1 
2086 N ND2 . ASN A 133 ? 0.38425 0.34693 0.38885 -0.01419 -0.00392 -0.03293 133 ASN A ND2 
2093 N N   . PHE A 134 ? 0.34845 0.32761 0.36793 -0.01045 -0.00101 -0.02123 134 PHE A N   
2094 C CA  . PHE A 134 ? 0.32478 0.30463 0.34720 -0.01017 0.00121  -0.02130 134 PHE A CA  
2095 C C   . PHE A 134 ? 0.32402 0.30408 0.34914 -0.00798 0.00167  -0.02420 134 PHE A C   
2096 O O   . PHE A 134 ? 0.36051 0.34483 0.38751 -0.00739 0.00342  -0.02520 134 PHE A O   
2097 C CB  . PHE A 134 ? 0.34475 0.32825 0.36409 -0.01192 0.00361  -0.02114 134 PHE A CB  
2098 C CG  . PHE A 134 ? 0.35155 0.33221 0.36685 -0.01385 0.00379  -0.01723 134 PHE A CG  
2099 C CD1 . PHE A 134 ? 0.44585 0.42156 0.46124 -0.01503 0.00472  -0.01459 134 PHE A CD1 
2100 C CD2 . PHE A 134 ? 0.43775 0.41912 0.44786 -0.01388 0.00290  -0.01612 134 PHE A CD2 
2101 C CE1 . PHE A 134 ? 0.45488 0.42462 0.46394 -0.01561 0.00527  -0.01041 134 PHE A CE1 
2102 C CE2 . PHE A 134 ? 0.48284 0.46081 0.48780 -0.01437 0.00303  -0.01178 134 PHE A CE2 
2103 C CZ  . PHE A 134 ? 0.46545 0.43676 0.46956 -0.01481 0.00433  -0.00877 134 PHE A CZ  
2113 N N   . THR A 135 ? 0.34158 0.31751 0.36622 -0.00692 0.00021  -0.02543 135 THR A N   
2114 C CA  . THR A 135 ? 0.31056 0.28421 0.33654 -0.00418 0.00067  -0.02703 135 THR A CA  
2115 C C   . THR A 135 ? 0.31771 0.28973 0.34776 -0.00487 -0.00036 -0.02508 135 THR A C   
2116 O O   . THR A 135 ? 0.29853 0.27106 0.33006 -0.00679 -0.00143 -0.02286 135 THR A O   
2117 C CB  . THR A 135 ? 0.32207 0.28880 0.34229 -0.00274 0.00053  -0.02968 135 THR A CB  
2118 O OG1 . THR A 135 ? 0.33327 0.29568 0.35168 -0.00659 -0.00141 -0.02925 135 THR A OG1 
2119 C CG2 . THR A 135 ? 0.36431 0.33240 0.37938 -0.00145 0.00185  -0.03202 135 THR A CG2 
2127 N N   . ILE A 136 ? 0.29523 0.26591 0.32660 -0.00244 0.00007  -0.02575 136 ILE A N   
2128 C CA  . ILE A 136 ? 0.32032 0.28881 0.35436 -0.00309 -0.00076 -0.02420 136 ILE A CA  
2129 C C   . ILE A 136 ? 0.31905 0.28071 0.34949 -0.00165 -0.00079 -0.02523 136 ILE A C   
2130 O O   . ILE A 136 ? 0.31368 0.27252 0.34025 0.00194  0.00017  -0.02693 136 ILE A O   
2131 C CB  . ILE A 136 ? 0.39183 0.36417 0.42993 -0.00252 -0.00013 -0.02335 136 ILE A CB  
2132 C CG1 . ILE A 136 ? 0.38822 0.36272 0.42634 0.00084  0.00053  -0.02474 136 ILE A CG1 
2133 C CG2 . ILE A 136 ? 0.36512 0.34105 0.40376 -0.00467 0.00071  -0.02279 136 ILE A CG2 
2134 C CD1 . ILE A 136 ? 0.37949 0.35853 0.42091 0.00039  0.00078  -0.02444 136 ILE A CD1 
2146 N N   . LYS A 137 ? 0.32142 0.28015 0.35220 -0.00428 -0.00161 -0.02404 137 LYS A N   
2147 C CA  . LYS A 137 ? 0.36058 0.31052 0.38633 -0.00469 -0.00129 -0.02452 137 LYS A CA  
2148 C C   . LYS A 137 ? 0.35522 0.30529 0.38303 -0.00191 -0.00071 -0.02315 137 LYS A C   
2149 O O   . LYS A 137 ? 0.35611 0.30789 0.38674 -0.00401 -0.00093 -0.02148 137 LYS A O   
2150 C CB  . LYS A 137 ? 0.39973 0.34866 0.42442 -0.01072 -0.00229 -0.02415 137 LYS A CB  
2151 C CG  . LYS A 137 ? 0.41942 0.36914 0.44113 -0.01342 -0.00316 -0.02584 137 LYS A CG  
2152 C CD  . LYS A 137 ? 0.49679 0.44987 0.51823 -0.02029 -0.00465 -0.02567 137 LYS A CD  
2153 C CE  . LYS A 137 ? 0.58747 0.52934 0.60111 -0.02516 -0.00386 -0.02725 137 LYS A CE  
2154 N NZ  . LYS A 137 ? 0.75540 0.70396 0.76875 -0.03338 -0.00554 -0.02787 137 LYS A NZ  
2168 N N   . GLY A 138 ? 0.32227 0.27291 0.34900 0.00328  0.00003  -0.02387 138 GLY A N   
2169 C CA  . GLY A 138 ? 0.36336 0.31651 0.39188 0.00634  0.00024  -0.02275 138 GLY A CA  
2170 C C   . GLY A 138 ? 0.35809 0.30095 0.37934 0.00950  0.00098  -0.02202 138 GLY A C   
2171 O O   . GLY A 138 ? 0.37725 0.30856 0.39119 0.00824  0.00161  -0.02245 138 GLY A O   
2175 N N   . SER A 139 ? 0.32337 0.26958 0.34534 0.01344  0.00100  -0.02091 139 SER A N   
2176 C CA  . SER A 139 ? 0.37220 0.30868 0.38603 0.01832  0.00181  -0.01952 139 SER A CA  
2177 C C   . SER A 139 ? 0.33756 0.28408 0.35288 0.02586  0.00142  -0.01975 139 SER A C   
2178 O O   . SER A 139 ? 0.30150 0.25745 0.32148 0.02577  0.00061  -0.01908 139 SER A O   
2179 C CB  . SER A 139 ? 0.33287 0.26525 0.34563 0.01509  0.00207  -0.01713 139 SER A CB  
2180 O OG  . SER A 139 ? 0.37592 0.29705 0.37890 0.02025  0.00309  -0.01529 139 SER A OG  
2186 N N   . PHE A 140 ? 0.34765 0.29301 0.35857 0.03234  0.00206  -0.02089 140 PHE A N   
2187 C CA  . PHE A 140 ? 0.31571 0.27611 0.32986 0.03917  0.00163  -0.02165 140 PHE A CA  
2188 C C   . PHE A 140 ? 0.33683 0.28971 0.34130 0.04981  0.00282  -0.02126 140 PHE A C   
2189 O O   . PHE A 140 ? 0.38113 0.31983 0.37798 0.05086  0.00428  -0.02222 140 PHE A O   
2190 C CB  . PHE A 140 ? 0.30427 0.27848 0.32596 0.03604  0.00152  -0.02422 140 PHE A CB  
2191 C CG  . PHE A 140 ? 0.28817 0.27005 0.31812 0.02711  0.00067  -0.02461 140 PHE A CG  
2192 C CD1 . PHE A 140 ? 0.30004 0.29198 0.33447 0.02557  -0.00028 -0.02434 140 PHE A CD1 
2193 C CD2 . PHE A 140 ? 0.32840 0.30766 0.36045 0.02094  0.00095  -0.02547 140 PHE A CD2 
2194 C CE1 . PHE A 140 ? 0.28121 0.27728 0.32089 0.01801  -0.00052 -0.02504 140 PHE A CE1 
2195 C CE2 . PHE A 140 ? 0.34127 0.32574 0.37892 0.01439  0.00057  -0.02553 140 PHE A CE2 
2196 C CZ  . PHE A 140 ? 0.28447 0.27617 0.32547 0.01290  0.00005  -0.02545 140 PHE A CZ  
2206 N N   . LEU A 141 ? 0.31141 0.27505 0.31588 0.05805  0.00220  -0.02013 141 LEU A N   
2207 C CA  . LEU A 141 ? 0.34854 0.30811 0.34377 0.07100  0.00325  -0.01917 141 LEU A CA  
2208 C C   . LEU A 141 ? 0.33655 0.32162 0.33911 0.07717  0.00265  -0.02088 141 LEU A C   
2209 O O   . LEU A 141 ? 0.32987 0.33441 0.34381 0.07011  0.00138  -0.02258 141 LEU A O   
2210 C CB  . LEU A 141 ? 0.36551 0.31658 0.35295 0.07667  0.00294  -0.01539 141 LEU A CB  
2211 C CG  . LEU A 141 ? 0.43667 0.36608 0.41797 0.06863  0.00371  -0.01347 141 LEU A CG  
2212 C CD1 . LEU A 141 ? 0.43906 0.36512 0.41476 0.07262  0.00322  -0.00943 141 LEU A CD1 
2213 C CD2 . LEU A 141 ? 0.50005 0.40384 0.46842 0.06902  0.00622  -0.01392 141 LEU A CD2 
2225 N N   . ASN A 142 ? 0.37168 0.35676 0.36680 0.09057  0.00379  -0.02035 142 ASN A N   
2226 C CA  . ASN A 142 ? 0.37451 0.38781 0.37664 0.09784  0.00321  -0.02159 142 ASN A CA  
2227 C C   . ASN A 142 ? 0.34146 0.37682 0.35266 0.09458  0.00045  -0.02080 142 ASN A C   
2228 O O   . ASN A 142 ? 0.36578 0.39424 0.37253 0.09666  -0.00071 -0.01794 142 ASN A O   
2229 C CB  . ASN A 142 ? 0.40540 0.41418 0.39633 0.11541  0.00487  -0.02031 142 ASN A CB  
2230 C CG  . ASN A 142 ? 0.58427 0.57552 0.56681 0.11831  0.00789  -0.02249 142 ASN A CG  
2231 O OD1 . ASN A 142 ? 0.56757 0.56163 0.55642 0.10833  0.00835  -0.02544 142 ASN A OD1 
2232 N ND2 . ASN A 142 ? 0.82689 0.79981 0.79401 0.13252  0.01010  -0.02112 142 ASN A ND2 
2239 N N   . GLY A 143 ? 0.30415 0.36542 0.32700 0.08865  -0.00040 -0.02349 143 GLY A N   
2240 C CA  . GLY A 143 ? 0.30056 0.38338 0.33160 0.08325  -0.00285 -0.02388 143 GLY A CA  
2241 C C   . GLY A 143 ? 0.32362 0.40143 0.36031 0.06747  -0.00349 -0.02523 143 GLY A C   
2242 O O   . GLY A 143 ? 0.29799 0.39137 0.34021 0.06152  -0.00525 -0.02623 143 GLY A O   
2246 N N   . SER A 144 ? 0.29053 0.34656 0.32481 0.06120  -0.00210 -0.02526 144 SER A N   
2247 C CA  . SER A 144 ? 0.27332 0.32289 0.31175 0.04821  -0.00244 -0.02606 144 SER A CA  
2248 C C   . SER A 144 ? 0.26183 0.32357 0.30738 0.03921  -0.00178 -0.02892 144 SER A C   
2249 O O   . SER A 144 ? 0.24806 0.30656 0.29650 0.02903  -0.00191 -0.02972 144 SER A O   
2250 C CB  . SER A 144 ? 0.25960 0.28310 0.29248 0.04562  -0.00141 -0.02457 144 SER A CB  
2251 O OG  . SER A 144 ? 0.30307 0.32027 0.33356 0.04739  0.00017  -0.02556 144 SER A OG  
2257 N N   . ALA A 145 ? 0.25369 0.32876 0.30111 0.04297  -0.00073 -0.03033 145 ALA A N   
2258 C CA  . ALA A 145 ? 0.23272 0.31839 0.28576 0.03331  0.00037  -0.03269 145 ALA A CA  
2259 C C   . ALA A 145 ? 0.24518 0.34477 0.30313 0.02398  -0.00076 -0.03420 145 ALA A C   
2260 O O   . ALA A 145 ? 0.25379 0.36648 0.31282 0.02727  -0.00252 -0.03425 145 ALA A O   
2261 C CB  . ALA A 145 ? 0.25173 0.35449 0.30648 0.03906  0.00187  -0.03408 145 ALA A CB  
2267 N N   . GLY A 146 ? 0.25109 0.34596 0.31047 0.01235  0.00026  -0.03537 146 GLY A N   
2268 C CA  . GLY A 146 ? 0.24707 0.34923 0.30834 0.00204  -0.00026 -0.03722 146 GLY A CA  
2269 C C   . GLY A 146 ? 0.28322 0.36690 0.34115 -0.00089 -0.00108 -0.03627 146 GLY A C   
2270 O O   . GLY A 146 ? 0.25751 0.34061 0.31476 -0.01015 -0.00087 -0.03802 146 GLY A O   
2274 N N   . SER A 147 ? 0.21186 0.28005 0.26682 0.00628  -0.00162 -0.03374 147 SER A N   
2275 C CA  . SER A 147 ? 0.24521 0.29597 0.29739 0.00312  -0.00174 -0.03268 147 SER A CA  
2276 C C   . SER A 147 ? 0.24013 0.28006 0.29159 -0.00478 -0.00008 -0.03303 147 SER A C   
2277 O O   . SER A 147 ? 0.23353 0.27336 0.28554 -0.00561 0.00104  -0.03291 147 SER A O   
2278 C CB  . SER A 147 ? 0.25086 0.28711 0.29982 0.01067  -0.00205 -0.02977 147 SER A CB  
2279 O OG  . SER A 147 ? 0.27659 0.31856 0.32373 0.01882  -0.00328 -0.02864 147 SER A OG  
2285 N N   . VAL A 148 ? 0.25642 0.28606 0.30555 -0.00960 0.00024  -0.03322 148 VAL A N   
2286 C CA  . VAL A 148 ? 0.23363 0.25220 0.28037 -0.01590 0.00200  -0.03320 148 VAL A CA  
2287 C C   . VAL A 148 ? 0.28159 0.28403 0.32622 -0.01336 0.00219  -0.03090 148 VAL A C   
2288 O O   . VAL A 148 ? 0.27894 0.27860 0.32352 -0.00941 0.00132  -0.03001 148 VAL A O   
2289 C CB  . VAL A 148 ? 0.27005 0.29030 0.31383 -0.02518 0.00311  -0.03599 148 VAL A CB  
2290 C CG1 . VAL A 148 ? 0.29757 0.33702 0.34422 -0.02943 0.00322  -0.03826 148 VAL A CG1 
2291 C CG2 . VAL A 148 ? 0.29582 0.31486 0.33733 -0.02602 0.00235  -0.03755 148 VAL A CG2 
2301 N N   . GLY A 149 ? 0.27408 0.26723 0.31666 -0.01570 0.00346  -0.02975 149 GLY A N   
2302 C CA  . GLY A 149 ? 0.28309 0.26363 0.32358 -0.01381 0.00384  -0.02767 149 GLY A CA  
2303 C C   . GLY A 149 ? 0.29082 0.26188 0.32570 -0.01849 0.00571  -0.02839 149 GLY A C   
2304 O O   . GLY A 149 ? 0.29711 0.26858 0.32896 -0.02462 0.00703  -0.02986 149 GLY A O   
2308 N N   . PHE A 150 ? 0.28348 0.24546 0.31592 -0.01576 0.00621  -0.02744 150 PHE A N   
2309 C CA  . PHE A 150 ? 0.28113 0.23153 0.30610 -0.01891 0.00836  -0.02855 150 PHE A CA  
2310 C C   . PHE A 150 ? 0.31698 0.25794 0.33967 -0.01294 0.00911  -0.02643 150 PHE A C   
2311 O O   . PHE A 150 ? 0.29320 0.23952 0.32109 -0.00789 0.00781  -0.02475 150 PHE A O   
2312 C CB  . PHE A 150 ? 0.32643 0.28043 0.34941 -0.02323 0.00847  -0.03227 150 PHE A CB  
2313 C CG  . PHE A 150 ? 0.31255 0.27254 0.33926 -0.01844 0.00701  -0.03231 150 PHE A CG  
2314 C CD1 . PHE A 150 ? 0.34529 0.31861 0.37838 -0.01605 0.00481  -0.03189 150 PHE A CD1 
2315 C CD2 . PHE A 150 ? 0.31968 0.27162 0.34248 -0.01581 0.00814  -0.03262 150 PHE A CD2 
2316 C CE1 . PHE A 150 ? 0.33518 0.31227 0.36998 -0.01173 0.00374  -0.03136 150 PHE A CE1 
2317 C CE2 . PHE A 150 ? 0.31905 0.27699 0.34493 -0.01160 0.00710  -0.03221 150 PHE A CE2 
2318 C CZ  . PHE A 150 ? 0.33502 0.30497 0.36648 -0.01013 0.00489  -0.03149 150 PHE A CZ  
2328 N N   . ASN A 151 ? 0.32751 0.25415 0.34150 -0.01359 0.01152  -0.02642 151 ASN A N   
2329 C CA  . ASN A 151 ? 0.33351 0.25153 0.34379 -0.00708 0.01284  -0.02517 151 ASN A CA  
2330 C C   . ASN A 151 ? 0.35543 0.26161 0.35621 -0.01010 0.01525  -0.02860 151 ASN A C   
2331 O O   . ASN A 151 ? 0.36516 0.26697 0.36059 -0.01820 0.01619  -0.03139 151 ASN A O   
2332 C CB  . ASN A 151 ? 0.34480 0.25434 0.35121 -0.00197 0.01378  -0.02138 151 ASN A CB  
2333 C CG  . ASN A 151 ? 0.34685 0.26914 0.36232 0.00116  0.01118  -0.01845 151 ASN A CG  
2334 O OD1 . ASN A 151 ? 0.37862 0.30961 0.40017 0.00538  0.00998  -0.01755 151 ASN A OD1 
2335 N ND2 . ASN A 151 ? 0.34528 0.26903 0.36113 -0.00190 0.01048  -0.01736 151 ASN A ND2 
2342 N N   . ILE A 152 ? 0.38009 0.28206 0.37843 -0.00419 0.01642  -0.02880 152 ILE A N   
2343 C CA  . ILE A 152 ? 0.36853 0.25641 0.35560 -0.00664 0.01913  -0.03248 152 ILE A CA  
2344 C C   . ILE A 152 ? 0.47891 0.35367 0.45874 0.00280  0.02181  -0.03058 152 ILE A C   
2345 O O   . ILE A 152 ? 0.50055 0.37630 0.47975 0.00800  0.02277  -0.03165 152 ILE A O   
2346 C CB  . ILE A 152 ? 0.37436 0.27158 0.36411 -0.00912 0.01813  -0.03605 152 ILE A CB  
2347 C CG1 . ILE A 152 ? 0.37057 0.28574 0.36998 -0.01449 0.01487  -0.03658 152 ILE A CG1 
2348 C CG2 . ILE A 152 ? 0.47631 0.35807 0.45248 -0.01456 0.02088  -0.04101 152 ILE A CG2 
2349 C CD1 . ILE A 152 ? 0.37739 0.30275 0.37834 -0.01655 0.01358  -0.03976 152 ILE A CD1 
2361 N N   . ASP A 153 ? 0.47348 0.33591 0.44676 0.00544  0.02328  -0.02778 153 ASP A N   
2362 C CA  . ASP A 153 ? 0.66204 0.51044 0.62624 0.01573  0.02614  -0.02571 153 ASP A CA  
2363 C C   . ASP A 153 ? 0.72236 0.54738 0.66979 0.01180  0.02995  -0.02998 153 ASP A C   
2364 O O   . ASP A 153 ? 0.81359 0.62730 0.75316 0.00157  0.03092  -0.03211 153 ASP A O   
2365 C CB  . ASP A 153 ? 0.60685 0.45018 0.56872 0.02076  0.02619  -0.02062 153 ASP A CB  
2366 C CG  . ASP A 153 ? 0.59391 0.46015 0.57133 0.02241  0.02222  -0.01716 153 ASP A CG  
2367 O OD1 . ASP A 153 ? 0.50236 0.38549 0.49025 0.02685  0.02050  -0.01656 153 ASP A OD1 
2368 O OD2 . ASP A 153 ? 0.50738 0.37421 0.48565 0.01811  0.02102  -0.01532 153 ASP A OD2 
2373 N N   . TYR A 154 ? 0.79203 0.61166 0.73433 0.01856  0.03211  -0.03183 154 TYR A N   
2374 C CA  . TYR A 154 ? 0.83548 0.63144 0.76022 0.01599  0.03608  -0.03655 154 TYR A CA  
2375 C C   . TYR A 154 ? 0.79447 0.59551 0.71984 0.00231  0.03487  -0.04241 154 TYR A C   
2376 O O   . TYR A 154 ? 0.81048 0.63235 0.74793 0.00174  0.03214  -0.04349 154 TYR A O   
2377 C CB  . TYR A 154 ? 0.92911 0.69771 0.83707 0.01625  0.03941  -0.03476 154 TYR A CB  
2378 C CG  . TYR A 154 ? 0.91575 0.68728 0.82695 0.03019  0.03918  -0.02794 154 TYR A CG  
2379 C CD1 . TYR A 154 ? 1.00163 0.77380 0.91152 0.04539  0.04085  -0.02607 154 TYR A CD1 
2380 C CD2 . TYR A 154 ? 0.90584 0.68294 0.82228 0.02821  0.03707  -0.02347 154 TYR A CD2 
2381 C CE1 . TYR A 154 ? 1.01638 0.79616 0.93053 0.05812  0.04011  -0.01982 154 TYR A CE1 
2382 C CE2 . TYR A 154 ? 0.99973 0.78262 0.91959 0.04058  0.03626  -0.01733 154 TYR A CE2 
2383 C CZ  . TYR A 154 ? 1.05364 0.83861 0.97256 0.05544  0.03763  -0.01550 154 TYR A CZ  
2384 O OH  . TYR A 154 ? 0.99729 0.79141 0.92000 0.06759  0.03652  -0.00949 154 TYR A OH  
2394 N N   . ASP A 155 ? 0.85187 0.63650 0.76494 -0.00918 0.03661  -0.04596 155 ASP A N   
2395 C CA  . ASP A 155 ? 0.89047 0.68350 0.80423 -0.02155 0.03525  -0.05198 155 ASP A CA  
2396 C C   . ASP A 155 ? 0.83868 0.64681 0.76100 -0.03362 0.03231  -0.05214 155 ASP A C   
2397 O O   . ASP A 155 ? 0.82064 0.63768 0.74337 -0.04508 0.03102  -0.05682 155 ASP A O   
2398 C CB  . ASP A 155 ? 1.02369 0.78968 0.91608 -0.02780 0.03952  -0.05791 155 ASP A CB  
2399 C CG  . ASP A 155 ? 1.14145 0.91851 1.03423 -0.03992 0.03784  -0.06451 155 ASP A CG  
2400 O OD1 . ASP A 155 ? 1.12041 0.91484 1.02219 -0.03521 0.03571  -0.06547 155 ASP A OD1 
2401 O OD2 . ASP A 155 ? 1.11130 0.88064 0.99507 -0.05446 0.03867  -0.06858 155 ASP A OD2 
2406 N N   . OCS A 156 ? 0.73069 0.53987 0.65764 -0.03092 0.03178  -0.04703 156 OCS A N   
2407 C CA  . OCS A 156 ? 0.58443 0.40322 0.51604 -0.04197 0.03025  -0.04692 156 OCS A CA  
2408 C CB  . OCS A 156 ? 0.70244 0.49822 0.62126 -0.04285 0.03359  -0.04394 156 OCS A CB  
2409 S SG  . OCS A 156 ? 0.70501 0.50409 0.62422 -0.05447 0.03364  -0.04234 156 OCS A SG  
2410 C C   . OCS A 156 ? 0.50787 0.35401 0.45895 -0.03803 0.02593  -0.04342 156 OCS A C   
2411 O O   . OCS A 156 ? 0.47384 0.32259 0.43093 -0.02761 0.02513  -0.03871 156 OCS A O   
2412 O OD1 . OCS A 156 ? 0.81947 0.58955 0.72157 -0.05303 0.03778  -0.03943 156 OCS A OD1 
2413 O OD2 . OCS A 156 ? 0.71733 0.52058 0.63252 -0.07054 0.03406  -0.04871 156 OCS A OD2 
2414 O OD3 . OCS A 156 ? 0.70987 0.53549 0.64781 -0.05003 0.02956  -0.03911 156 OCS A OD3 
2419 N N   . VAL A 157 ? 0.45155 0.31661 0.41057 -0.04663 0.02347  -0.04593 157 VAL A N   
2420 C CA  . VAL A 157 ? 0.38490 0.27361 0.36022 -0.04304 0.01977  -0.04301 157 VAL A CA  
2421 C C   . VAL A 157 ? 0.41595 0.30425 0.39183 -0.04665 0.02025  -0.04027 157 VAL A C   
2422 O O   . VAL A 157 ? 0.41785 0.30498 0.38840 -0.05792 0.02160  -0.04270 157 VAL A O   
2423 C CB  . VAL A 157 ? 0.37910 0.29023 0.36291 -0.04800 0.01684  -0.04622 157 VAL A CB  
2424 C CG1 . VAL A 157 ? 0.33507 0.26610 0.33289 -0.04305 0.01370  -0.04300 157 VAL A CG1 
2425 C CG2 . VAL A 157 ? 0.41719 0.32909 0.39916 -0.04529 0.01639  -0.04902 157 VAL A CG2 
2435 N N   . SER A 158 ? 0.38210 0.27182 0.36358 -0.03813 0.01935  -0.03546 158 SER A N   
2436 C CA  . SER A 158 ? 0.37654 0.26727 0.35875 -0.04060 0.01960  -0.03267 158 SER A CA  
2437 C C   . SER A 158 ? 0.33787 0.25225 0.33430 -0.03927 0.01627  -0.03211 158 SER A C   
2438 O O   . SER A 158 ? 0.35965 0.28125 0.36397 -0.03093 0.01414  -0.02982 158 SER A O   
2439 C CB  . SER A 158 ? 0.41230 0.28815 0.38898 -0.03258 0.02091  -0.02790 158 SER A CB  
2440 O OG  . SER A 158 ? 0.49181 0.37419 0.47601 -0.02177 0.01894  -0.02569 158 SER A OG  
2446 N N   . PHE A 159 ? 0.35494 0.28147 0.35387 -0.04765 0.01607  -0.03439 159 PHE A N   
2447 C CA  . PHE A 159 ? 0.33214 0.27977 0.34274 -0.04528 0.01344  -0.03397 159 PHE A CA  
2448 C C   . PHE A 159 ? 0.32879 0.27543 0.34023 -0.04344 0.01383  -0.03060 159 PHE A C   
2449 O O   . PHE A 159 ? 0.36875 0.30816 0.37328 -0.04994 0.01624  -0.03010 159 PHE A O   
2450 C CB  . PHE A 159 ? 0.32958 0.29435 0.34297 -0.05376 0.01310  -0.03783 159 PHE A CB  
2451 C CG  . PHE A 159 ? 0.31597 0.28637 0.32959 -0.05524 0.01192  -0.04133 159 PHE A CG  
2452 C CD1 . PHE A 159 ? 0.32652 0.30869 0.34800 -0.04724 0.00908  -0.04090 159 PHE A CD1 
2453 C CD2 . PHE A 159 ? 0.36339 0.32644 0.36801 -0.06504 0.01376  -0.04509 159 PHE A CD2 
2454 C CE1 . PHE A 159 ? 0.30271 0.29031 0.32361 -0.04801 0.00789  -0.04375 159 PHE A CE1 
2455 C CE2 . PHE A 159 ? 0.36703 0.33625 0.37129 -0.06655 0.01245  -0.04861 159 PHE A CE2 
2456 C CZ  . PHE A 159 ? 0.34627 0.32902 0.35911 -0.05780 0.00939  -0.04779 159 PHE A CZ  
2466 N N   . CYS A 160 ? 0.31661 0.27026 0.33547 -0.03543 0.01164  -0.02838 160 CYS A N   
2467 C CA  . CYS A 160 ? 0.30517 0.25777 0.32404 -0.03344 0.01178  -0.02544 160 CYS A CA  
2468 C C   . CYS A 160 ? 0.28452 0.25307 0.31138 -0.03088 0.01004  -0.02582 160 CYS A C   
2469 O O   . CYS A 160 ? 0.31532 0.28440 0.34164 -0.03020 0.01032  -0.02409 160 CYS A O   
2470 C CB  . CYS A 160 ? 0.33754 0.27967 0.35471 -0.02607 0.01117  -0.02197 160 CYS A CB  
2471 S SG  . CYS A 160 ? 0.36714 0.31549 0.39198 -0.01849 0.00852  -0.02196 160 CYS A SG  
2477 N N   . TYR A 161 ? 0.27859 0.25907 0.31150 -0.02877 0.00843  -0.02792 161 TYR A N   
2478 C CA  . TYR A 161 ? 0.26690 0.25935 0.30538 -0.02435 0.00710  -0.02812 161 TYR A CA  
2479 C C   . TYR A 161 ? 0.26664 0.27431 0.30925 -0.02444 0.00637  -0.03079 161 TYR A C   
2480 O O   . TYR A 161 ? 0.25953 0.26778 0.30235 -0.02476 0.00562  -0.03194 161 TYR A O   
2481 C CB  . TYR A 161 ? 0.27113 0.25844 0.31153 -0.01714 0.00530  -0.02631 161 TYR A CB  
2482 C CG  . TYR A 161 ? 0.24849 0.24337 0.29181 -0.01244 0.00433  -0.02676 161 TYR A CG  
2483 C CD1 . TYR A 161 ? 0.26377 0.25926 0.30589 -0.01205 0.00483  -0.02630 161 TYR A CD1 
2484 C CD2 . TYR A 161 ? 0.24071 0.24044 0.28637 -0.00782 0.00312  -0.02757 161 TYR A CD2 
2485 C CE1 . TYR A 161 ? 0.27326 0.27309 0.31613 -0.00716 0.00434  -0.02719 161 TYR A CE1 
2486 C CE2 . TYR A 161 ? 0.24487 0.24784 0.29071 -0.00230 0.00267  -0.02790 161 TYR A CE2 
2487 C CZ  . TYR A 161 ? 0.26446 0.26720 0.30878 -0.00204 0.00339  -0.02801 161 TYR A CZ  
2488 O OH  . TYR A 161 ? 0.27409 0.27741 0.31669 0.00367  0.00336  -0.02878 161 TYR A OH  
2498 N N   . MET A 162 ? 0.24531 0.26654 0.29083 -0.02358 0.00664  -0.03176 162 MET A N   
2499 C CA  . MET A 162 ? 0.23853 0.27650 0.28839 -0.02018 0.00555  -0.03362 162 MET A CA  
2500 C C   . MET A 162 ? 0.21478 0.25609 0.26617 -0.01147 0.00504  -0.03290 162 MET A C   
2501 O O   . MET A 162 ? 0.24051 0.28156 0.29090 -0.01157 0.00628  -0.03258 162 MET A O   
2502 C CB  . MET A 162 ? 0.25894 0.31428 0.31034 -0.02769 0.00677  -0.03619 162 MET A CB  
2503 C CG  . MET A 162 ? 0.26756 0.34453 0.32408 -0.02227 0.00535  -0.03781 162 MET A CG  
2504 S SD  . MET A 162 ? 0.32762 0.42880 0.38662 -0.03322 0.00618  -0.04138 162 MET A SD  
2505 C CE  . MET A 162 ? 0.31820 0.41266 0.37457 -0.03696 0.00431  -0.04275 162 MET A CE  
2515 N N   . HIS A 163 ? 0.25329 0.29532 0.30547 -0.00387 0.00344  -0.03257 163 HIS A N   
2516 C CA  . HIS A 163 ? 0.27241 0.31141 0.32309 0.00468  0.00324  -0.03185 163 HIS A CA  
2517 C C   . HIS A 163 ? 0.24933 0.30587 0.30179 0.00938  0.00411  -0.03340 163 HIS A C   
2518 O O   . HIS A 163 ? 0.23821 0.31226 0.29410 0.00947  0.00374  -0.03464 163 HIS A O   
2519 C CB  . HIS A 163 ? 0.24416 0.27486 0.29281 0.01089  0.00171  -0.03049 163 HIS A CB  
2520 C CG  . HIS A 163 ? 0.27520 0.29799 0.31954 0.01870  0.00196  -0.02985 163 HIS A CG  
2521 N ND1 . HIS A 163 ? 0.26094 0.27354 0.30248 0.01738  0.00275  -0.02980 163 HIS A ND1 
2522 C CD2 . HIS A 163 ? 0.27489 0.29818 0.31579 0.02799  0.00181  -0.02948 163 HIS A CD2 
2523 C CE1 . HIS A 163 ? 0.27885 0.28438 0.31497 0.02454  0.00315  -0.02989 163 HIS A CE1 
2524 N NE2 . HIS A 163 ? 0.28425 0.29513 0.31944 0.03154  0.00281  -0.02954 163 HIS A NE2 
2532 N N   . HIS A 164 ? 0.22786 0.28115 0.27778 0.01341  0.00532  -0.03355 164 HIS A N   
2533 C CA  . HIS A 164 ? 0.26239 0.33154 0.31309 0.02015  0.00655  -0.03502 164 HIS A CA  
2534 C C   . HIS A 164 ? 0.27833 0.33707 0.32296 0.03144  0.00678  -0.03477 164 HIS A C   
2535 O O   . HIS A 164 ? 0.28194 0.35047 0.32585 0.04111  0.00690  -0.03508 164 HIS A O   
2536 C CB  . HIS A 164 ? 0.26904 0.34674 0.32085 0.01461  0.00885  -0.03619 164 HIS A CB  
2537 C CG  . HIS A 164 ? 0.27288 0.36247 0.32882 0.00351  0.00949  -0.03678 164 HIS A CG  
2538 N ND1 . HIS A 164 ? 0.25575 0.36836 0.31549 0.00051  0.01127  -0.03850 164 HIS A ND1 
2539 C CD2 . HIS A 164 ? 0.26490 0.34545 0.32050 -0.00576 0.00895  -0.03602 164 HIS A CD2 
2540 C CE1 . HIS A 164 ? 0.24716 0.36289 0.30807 -0.01158 0.01183  -0.03884 164 HIS A CE1 
2541 N NE2 . HIS A 164 ? 0.26195 0.35707 0.31977 -0.01494 0.01050  -0.03737 164 HIS A NE2 
2549 N N   . MET A 165 ? 0.28741 0.32801 0.32685 0.03031  0.00719  -0.03448 165 MET A N   
2550 C CA  . MET A 165 ? 0.33904 0.36896 0.37056 0.03998  0.00815  -0.03513 165 MET A CA  
2551 C C   . MET A 165 ? 0.29741 0.30310 0.32172 0.03863  0.00752  -0.03440 165 MET A C   
2552 O O   . MET A 165 ? 0.27205 0.27117 0.29851 0.03019  0.00634  -0.03336 165 MET A O   
2553 C CB  . MET A 165 ? 0.39855 0.43640 0.42878 0.04166  0.01049  -0.03727 165 MET A CB  
2554 C CG  . MET A 165 ? 0.34508 0.38021 0.37649 0.03161  0.01084  -0.03735 165 MET A CG  
2555 S SD  . MET A 165 ? 0.52338 0.57921 0.55693 0.03197  0.01385  -0.03939 165 MET A SD  
2556 C CE  . MET A 165 ? 0.39430 0.47332 0.43323 0.04030  0.01416  -0.03998 165 MET A CE  
2566 N N   . GLU A 166 ? 0.33720 0.33069 0.35233 0.04718  0.00855  -0.03509 166 GLU A N   
2567 C CA  . GLU A 166 ? 0.36458 0.33498 0.37120 0.04476  0.00834  -0.03500 166 GLU A CA  
2568 C C   . GLU A 166 ? 0.39167 0.35453 0.39043 0.04666  0.01021  -0.03784 166 GLU A C   
2569 O O   . GLU A 166 ? 0.36175 0.32878 0.35630 0.05600  0.01226  -0.03950 166 GLU A O   
2570 C CB  . GLU A 166 ? 0.37004 0.32649 0.36912 0.05117  0.00831  -0.03340 166 GLU A CB  
2571 C CG  . GLU A 166 ? 0.41115 0.34381 0.40087 0.04600  0.00838  -0.03352 166 GLU A CG  
2572 C CD  . GLU A 166 ? 0.46410 0.38127 0.44606 0.04928  0.00851  -0.03121 166 GLU A CD  
2573 O OE1 . GLU A 166 ? 0.41705 0.34075 0.40532 0.04726  0.00704  -0.02862 166 GLU A OE1 
2574 O OE2 . GLU A 166 ? 0.49038 0.38775 0.45847 0.05419  0.01041  -0.03204 166 GLU A OE2 
2581 N N   . LEU A 167 ? 0.33133 0.28461 0.32791 0.03830  0.00952  -0.03853 167 LEU A N   
2582 C CA  . LEU A 167 ? 0.37836 0.32388 0.36656 0.03869  0.01102  -0.04158 167 LEU A CA  
2583 C C   . LEU A 167 ? 0.43224 0.35382 0.40636 0.04169  0.01198  -0.04306 167 LEU A C   
2584 O O   . LEU A 167 ? 0.41962 0.33041 0.39114 0.04140  0.01130  -0.04117 167 LEU A O   
2585 C CB  . LEU A 167 ? 0.38600 0.33394 0.37772 0.02818  0.00952  -0.04155 167 LEU A CB  
2586 C CG  . LEU A 167 ? 0.35970 0.32691 0.36256 0.02451  0.00908  -0.03981 167 LEU A CG  
2587 C CD1 . LEU A 167 ? 0.43792 0.40422 0.44244 0.01558  0.00742  -0.03880 167 LEU A CD1 
2588 C CD2 . LEU A 167 ? 0.45443 0.43478 0.45751 0.02966  0.01158  -0.04163 167 LEU A CD2 
2600 N N   . PRO A 168 ? 0.45517 0.36645 0.41849 0.04383  0.01387  -0.04660 168 PRO A N   
2601 C CA  . PRO A 168 ? 0.51198 0.39697 0.45869 0.04715  0.01555  -0.04854 168 PRO A CA  
2602 C C   . PRO A 168 ? 0.51261 0.38213 0.45537 0.03592  0.01381  -0.04796 168 PRO A C   
2603 O O   . PRO A 168 ? 0.52395 0.37125 0.45369 0.03748  0.01520  -0.04834 168 PRO A O   
2604 C CB  . PRO A 168 ? 0.54172 0.42106 0.47817 0.05030  0.01794  -0.05314 168 PRO A CB  
2605 C CG  . PRO A 168 ? 0.62586 0.53152 0.57401 0.05361  0.01832  -0.05289 168 PRO A CG  
2606 C CD  . PRO A 168 ? 0.49672 0.41938 0.46086 0.04482  0.01522  -0.04912 168 PRO A CD  
2614 N N   . THR A 169 ? 0.45656 0.33673 0.40895 0.02484  0.01108  -0.04698 169 THR A N   
2615 C CA  . THR A 169 ? 0.48677 0.35691 0.43707 0.01456  0.00943  -0.04615 169 THR A CA  
2616 C C   . THR A 169 ? 0.51088 0.38392 0.46825 0.01449  0.00847  -0.04202 169 THR A C   
2617 O O   . THR A 169 ? 0.48859 0.35616 0.44553 0.00606  0.00735  -0.04091 169 THR A O   
2618 C CB  . THR A 169 ? 0.50057 0.38249 0.45791 0.00419  0.00681  -0.04642 169 THR A CB  
2619 O OG1 . THR A 169 ? 0.44953 0.35264 0.42071 0.00593  0.00566  -0.04398 169 THR A OG1 
2620 C CG2 . THR A 169 ? 0.59554 0.46985 0.54206 0.00172  0.00756  -0.05101 169 THR A CG2 
2628 N N   . GLY A 170 ? 0.42721 0.31039 0.39106 0.02316  0.00890  -0.03987 170 GLY A N   
2629 C CA  . GLY A 170 ? 0.39430 0.28037 0.36384 0.02344  0.00801  -0.03622 170 GLY A CA  
2630 C C   . GLY A 170 ? 0.38603 0.29091 0.37061 0.01772  0.00567  -0.03398 170 GLY A C   
2631 O O   . GLY A 170 ? 0.44795 0.35493 0.43687 0.01682  0.00494  -0.03130 170 GLY A O   
2635 N N   . VAL A 171 ? 0.35394 0.27083 0.34505 0.01394  0.00471  -0.03491 171 VAL A N   
2636 C CA  . VAL A 171 ? 0.35869 0.29113 0.36196 0.01010  0.00306  -0.03270 171 VAL A CA  
2637 C C   . VAL A 171 ? 0.35371 0.29979 0.36274 0.01544  0.00381  -0.03268 171 VAL A C   
2638 O O   . VAL A 171 ? 0.32975 0.27607 0.33452 0.02228  0.00543  -0.03437 171 VAL A O   
2639 C CB  . VAL A 171 ? 0.36490 0.30155 0.37049 0.00285  0.00164  -0.03298 171 VAL A CB  
2640 C CG1 . VAL A 171 ? 0.42261 0.34980 0.42323 -0.00369 0.00068  -0.03334 171 VAL A CG1 
2641 C CG2 . VAL A 171 ? 0.36006 0.29867 0.36179 0.00441  0.00255  -0.03549 171 VAL A CG2 
2651 N N   . HIS A 172 ? 0.31460 0.27236 0.33257 0.01209  0.00289  -0.03100 172 HIS A N   
2652 C CA  . HIS A 172 ? 0.32225 0.29319 0.34577 0.01510  0.00354  -0.03086 172 HIS A CA  
2653 C C   . HIS A 172 ? 0.34514 0.32597 0.37300 0.01063  0.00385  -0.03084 172 HIS A C   
2654 O O   . HIS A 172 ? 0.31821 0.29610 0.34651 0.00545  0.00301  -0.02977 172 HIS A O   
2655 C CB  . HIS A 172 ? 0.32336 0.29640 0.35116 0.01490  0.00262  -0.02899 172 HIS A CB  
2656 C CG  . HIS A 172 ? 0.33528 0.29805 0.35734 0.01963  0.00269  -0.02848 172 HIS A CG  
2657 N ND1 . HIS A 172 ? 0.30812 0.25983 0.32753 0.01621  0.00207  -0.02712 172 HIS A ND1 
2658 C CD2 . HIS A 172 ? 0.32296 0.28373 0.33979 0.02781  0.00367  -0.02900 172 HIS A CD2 
2659 C CE1 . HIS A 172 ? 0.34343 0.28513 0.35560 0.02118  0.00280  -0.02667 172 HIS A CE1 
2660 N NE2 . HIS A 172 ? 0.35227 0.29822 0.36219 0.02904  0.00374  -0.02770 172 HIS A NE2 
2668 N N   . ALA A 173 ? 0.29293 0.28644 0.32359 0.01275  0.00517  -0.03178 173 ALA A N   
2669 C CA  . ALA A 173 ? 0.28820 0.29080 0.32172 0.00764  0.00611  -0.03163 173 ALA A CA  
2670 C C   . ALA A 173 ? 0.29032 0.30606 0.32929 0.00593  0.00665  -0.03165 173 ALA A C   
2671 O O   . ALA A 173 ? 0.27532 0.29918 0.31586 0.01114  0.00672  -0.03262 173 ALA A O   
2672 C CB  . ALA A 173 ? 0.30293 0.30929 0.33268 0.00988  0.00787  -0.03350 173 ALA A CB  
2678 N N   . GLY A 174 ? 0.24911 0.26699 0.28987 -0.00136 0.00712  -0.03063 174 GLY A N   
2679 C CA  . GLY A 174 ? 0.25685 0.28659 0.30143 -0.00509 0.00781  -0.03130 174 GLY A CA  
2680 C C   . GLY A 174 ? 0.24845 0.27719 0.29155 -0.01376 0.00933  -0.03037 174 GLY A C   
2681 O O   . GLY A 174 ? 0.25656 0.27876 0.29606 -0.01525 0.00999  -0.02912 174 GLY A O   
2685 N N   . THR A 175 ? 0.25494 0.28880 0.29943 -0.01981 0.00993  -0.03093 175 THR A N   
2686 C CA  . THR A 175 ? 0.27702 0.30971 0.31817 -0.02908 0.01219  -0.03035 175 THR A CA  
2687 C C   . THR A 175 ? 0.27944 0.29818 0.31715 -0.03376 0.01198  -0.02929 175 THR A C   
2688 O O   . THR A 175 ? 0.25882 0.27389 0.29831 -0.03069 0.01021  -0.02964 175 THR A O   
2689 C CB  . THR A 175 ? 0.28215 0.33492 0.32614 -0.03456 0.01407  -0.03275 175 THR A CB  
2690 O OG1 . THR A 175 ? 0.26280 0.32393 0.31043 -0.03535 0.01277  -0.03466 175 THR A OG1 
2691 C CG2 . THR A 175 ? 0.24151 0.30964 0.28862 -0.02805 0.01473  -0.03393 175 THR A CG2 
2699 N N   . ASP A 176 ? 0.30335 0.31398 0.33487 -0.04139 0.01426  -0.02804 176 ASP A N   
2700 C CA  . ASP A 176 ? 0.30783 0.30728 0.33451 -0.04729 0.01505  -0.02819 176 ASP A CA  
2701 C C   . ASP A 176 ? 0.32684 0.34115 0.35600 -0.05458 0.01580  -0.03178 176 ASP A C   
2702 O O   . ASP A 176 ? 0.30030 0.33542 0.33598 -0.05357 0.01544  -0.03374 176 ASP A O   
2703 C CB  . ASP A 176 ? 0.33411 0.31613 0.35072 -0.05233 0.01754  -0.02533 176 ASP A CB  
2704 C CG  . ASP A 176 ? 0.34344 0.33246 0.35649 -0.06101 0.02070  -0.02537 176 ASP A CG  
2705 O OD1 . ASP A 176 ? 0.33401 0.34141 0.35159 -0.06628 0.02154  -0.02833 176 ASP A OD1 
2706 O OD2 . ASP A 176 ? 0.38768 0.36460 0.39298 -0.06253 0.02244  -0.02219 176 ASP A OD2 
2711 N N   . LEU A 177 ? 0.30624 0.31074 0.32977 -0.06151 0.01679  -0.03290 177 LEU A N   
2712 C CA  . LEU A 177 ? 0.31143 0.33069 0.33695 -0.06920 0.01699  -0.03679 177 LEU A CA  
2713 C C   . LEU A 177 ? 0.30022 0.32779 0.32220 -0.08159 0.02019  -0.03802 177 LEU A C   
2714 O O   . LEU A 177 ? 0.34850 0.39209 0.37227 -0.09001 0.02053  -0.04156 177 LEU A O   
2715 C CB  . LEU A 177 ? 0.32513 0.33107 0.34547 -0.07180 0.01662  -0.03834 177 LEU A CB  
2716 C CG  . LEU A 177 ? 0.33346 0.34628 0.36055 -0.06287 0.01325  -0.03926 177 LEU A CG  
2717 C CD1 . LEU A 177 ? 0.36661 0.40698 0.40164 -0.06369 0.01155  -0.04227 177 LEU A CD1 
2718 C CD2 . LEU A 177 ? 0.32535 0.33346 0.35677 -0.05055 0.01142  -0.03595 177 LEU A CD2 
2730 N N   . GLU A 178 ? 0.33624 0.35525 0.35327 -0.08322 0.02252  -0.03516 178 GLU A N   
2731 C CA  . GLU A 178 ? 0.38776 0.41878 0.40285 -0.09386 0.02575  -0.03585 178 GLU A CA  
2732 C C   . GLU A 178 ? 0.32357 0.37826 0.34824 -0.08730 0.02511  -0.03593 178 GLU A C   
2733 O O   . GLU A 178 ? 0.34588 0.41265 0.36977 -0.09437 0.02799  -0.03608 178 GLU A O   
2734 C CB  . GLU A 178 ? 0.39456 0.40168 0.39653 -0.10006 0.02926  -0.03239 178 GLU A CB  
2735 C CG  . GLU A 178 ? 0.53878 0.51903 0.52826 -0.10615 0.03073  -0.03234 178 GLU A CG  
2736 C CD  . GLU A 178 ? 0.63453 0.58920 0.60811 -0.11280 0.03486  -0.02866 178 GLU A CD  
2737 O OE1 . GLU A 178 ? 0.64208 0.59390 0.61396 -0.10856 0.03562  -0.02473 178 GLU A OE1 
2738 O OE2 . GLU A 178 ? 0.76983 0.70659 0.73105 -0.12307 0.03765  -0.02986 178 GLU A OE2 
2745 N N   . GLY A 179 ? 0.30200 0.36197 0.33428 -0.07401 0.02185  -0.03575 179 GLY A N   
2746 C CA  . GLY A 179 ? 0.30065 0.38159 0.34050 -0.06661 0.02148  -0.03639 179 GLY A CA  
2747 C C   . GLY A 179 ? 0.31235 0.38549 0.34944 -0.06136 0.02243  -0.03374 179 GLY A C   
2748 O O   . GLY A 179 ? 0.29905 0.38843 0.34062 -0.05571 0.02284  -0.03465 179 GLY A O   
2752 N N   . ASN A 180 ? 0.29655 0.34623 0.32573 -0.06265 0.02287  -0.03062 180 ASN A N   
2753 C CA  . ASN A 180 ? 0.28202 0.32485 0.30803 -0.05747 0.02324  -0.02807 180 ASN A CA  
2754 C C   . ASN A 180 ? 0.27420 0.31019 0.30341 -0.04543 0.01974  -0.02763 180 ASN A C   
2755 O O   . ASN A 180 ? 0.29289 0.31479 0.32094 -0.04339 0.01780  -0.02650 180 ASN A O   
2756 C CB  . ASN A 180 ? 0.33731 0.36010 0.35254 -0.06365 0.02528  -0.02443 180 ASN A CB  
2757 C CG  . ASN A 180 ? 0.39881 0.42355 0.40818 -0.07727 0.02922  -0.02466 180 ASN A CG  
2758 O OD1 . ASN A 180 ? 0.50113 0.51155 0.50412 -0.08406 0.03013  -0.02435 180 ASN A OD1 
2759 N ND2 . ASN A 180 ? 0.33462 0.37621 0.34499 -0.08187 0.03195  -0.02537 180 ASN A ND2 
2766 N N   . PHE A 181 ? 0.26993 0.31492 0.30192 -0.03827 0.01935  -0.02861 181 PHE A N   
2767 C CA  . PHE A 181 ? 0.27741 0.31381 0.31041 -0.02877 0.01642  -0.02842 181 PHE A CA  
2768 C C   . PHE A 181 ? 0.30769 0.32569 0.33502 -0.02918 0.01535  -0.02520 181 PHE A C   
2769 O O   . PHE A 181 ? 0.29043 0.30315 0.31186 -0.03383 0.01705  -0.02292 181 PHE A O   
2770 C CB  . PHE A 181 ? 0.31188 0.35652 0.34547 -0.02159 0.01673  -0.03021 181 PHE A CB  
2771 C CG  . PHE A 181 ? 0.28139 0.33798 0.32027 -0.01444 0.01604  -0.03292 181 PHE A CG  
2772 C CD1 . PHE A 181 ? 0.27373 0.32132 0.31306 -0.00723 0.01351  -0.03318 181 PHE A CD1 
2773 C CD2 . PHE A 181 ? 0.30011 0.37765 0.34301 -0.01531 0.01804  -0.03487 181 PHE A CD2 
2774 C CE1 . PHE A 181 ? 0.28429 0.34106 0.32670 0.00012  0.01304  -0.03497 181 PHE A CE1 
2775 C CE2 . PHE A 181 ? 0.30390 0.39410 0.35131 -0.00742 0.01726  -0.03685 181 PHE A CE2 
2776 C CZ  . PHE A 181 ? 0.26219 0.34070 0.30865 0.00092  0.01481  -0.03672 181 PHE A CZ  
2786 N N   . TYR A 182 ? 0.29660 0.30587 0.32546 -0.02404 0.01257  -0.02480 182 TYR A N   
2787 C CA  . TYR A 182 ? 0.28026 0.27768 0.30533 -0.02176 0.01092  -0.02236 182 TYR A CA  
2788 C C   . TYR A 182 ? 0.31729 0.31807 0.34094 -0.01778 0.01045  -0.02367 182 TYR A C   
2789 O O   . TYR A 182 ? 0.31214 0.31823 0.33831 -0.01337 0.01013  -0.02644 182 TYR A O   
2790 C CB  . TYR A 182 ? 0.29540 0.28560 0.32315 -0.01848 0.00847  -0.02189 182 TYR A CB  
2791 C CG  . TYR A 182 ? 0.28926 0.27328 0.31627 -0.02190 0.00909  -0.02064 182 TYR A CG  
2792 C CD1 . TYR A 182 ? 0.28959 0.26237 0.31080 -0.02328 0.00955  -0.01736 182 TYR A CD1 
2793 C CD2 . TYR A 182 ? 0.27862 0.26737 0.30945 -0.02315 0.00928  -0.02277 182 TYR A CD2 
2794 C CE1 . TYR A 182 ? 0.31599 0.27976 0.33422 -0.02570 0.01061  -0.01647 182 TYR A CE1 
2795 C CE2 . TYR A 182 ? 0.27089 0.25220 0.29941 -0.02675 0.01003  -0.02225 182 TYR A CE2 
2796 C CZ  . TYR A 182 ? 0.26754 0.23512 0.28924 -0.02800 0.01093  -0.01924 182 TYR A CZ  
2797 O OH  . TYR A 182 ? 0.30077 0.25785 0.31793 -0.03076 0.01215  -0.01896 182 TYR A OH  
2807 N N   . GLY A 183 ? 0.32012 0.31702 0.33831 -0.01900 0.01060  -0.02173 183 GLY A N   
2808 C CA  . GLY A 183 ? 0.33922 0.33813 0.35474 -0.01582 0.01004  -0.02347 183 GLY A CA  
2809 C C   . GLY A 183 ? 0.35705 0.36685 0.37162 -0.01617 0.01304  -0.02570 183 GLY A C   
2810 O O   . GLY A 183 ? 0.36736 0.38504 0.38378 -0.01997 0.01552  -0.02558 183 GLY A O   
2814 N N   . PRO A 184 ? 0.31737 0.32834 0.32841 -0.01271 0.01305  -0.02797 184 PRO A N   
2815 C CA  . PRO A 184 ? 0.36499 0.38722 0.37425 -0.01205 0.01629  -0.03012 184 PRO A CA  
2816 C C   . PRO A 184 ? 0.38462 0.41597 0.39808 -0.00627 0.01750  -0.03369 184 PRO A C   
2817 O O   . PRO A 184 ? 0.47023 0.50925 0.48120 -0.00216 0.01973  -0.03643 184 PRO A O   
2818 C CB  . PRO A 184 ? 0.38890 0.40636 0.39068 -0.01028 0.01567  -0.03122 184 PRO A CB  
2819 C CG  . PRO A 184 ? 0.39306 0.39911 0.39460 -0.00770 0.01207  -0.03202 184 PRO A CG  
2820 C CD  . PRO A 184 ? 0.37818 0.38052 0.38569 -0.01003 0.01034  -0.02887 184 PRO A CD  
2828 N N   . PHE A 185 ? 0.31598 0.34801 0.33524 -0.00526 0.01638  -0.03357 185 PHE A N   
2829 C CA  . PHE A 185 ? 0.32016 0.35908 0.34213 0.00227  0.01688  -0.03644 185 PHE A CA  
2830 C C   . PHE A 185 ? 0.32144 0.38005 0.34893 0.00061  0.01935  -0.03696 185 PHE A C   
2831 O O   . PHE A 185 ? 0.30987 0.37304 0.33926 -0.00795 0.02025  -0.03506 185 PHE A O   
2832 C CB  . PHE A 185 ? 0.32336 0.35260 0.34782 0.00492  0.01407  -0.03593 185 PHE A CB  
2833 C CG  . PHE A 185 ? 0.30217 0.31436 0.32174 0.00484  0.01172  -0.03544 185 PHE A CG  
2834 C CD1 . PHE A 185 ? 0.35117 0.35638 0.36362 0.00930  0.01206  -0.03806 185 PHE A CD1 
2835 C CD2 . PHE A 185 ? 0.33501 0.33938 0.35617 -0.00004 0.00951  -0.03271 185 PHE A CD2 
2836 C CE1 . PHE A 185 ? 0.38079 0.37253 0.38817 0.00744  0.00998  -0.03819 185 PHE A CE1 
2837 C CE2 . PHE A 185 ? 0.32007 0.31335 0.33723 -0.00071 0.00743  -0.03243 185 PHE A CE2 
2838 C CZ  . PHE A 185 ? 0.34676 0.33417 0.35727 0.00223  0.00751  -0.03527 185 PHE A CZ  
2848 N N   . VAL A 186 ? 0.29142 0.36192 0.32031 0.00892  0.02072  -0.03964 186 VAL A N   
2849 C CA  . VAL A 186 ? 0.32444 0.41889 0.35948 0.00840  0.02296  -0.04059 186 VAL A CA  
2850 C C   . VAL A 186 ? 0.30187 0.40251 0.34063 0.01748  0.02164  -0.04173 186 VAL A C   
2851 O O   . VAL A 186 ? 0.31525 0.40161 0.34957 0.02602  0.02024  -0.04228 186 VAL A O   
2852 C CB  . VAL A 186 ? 0.32548 0.43558 0.35862 0.01075  0.02676  -0.04252 186 VAL A CB  
2853 C CG1 . VAL A 186 ? 0.36924 0.47402 0.39788 0.00097  0.02824  -0.04075 186 VAL A CG1 
2854 C CG2 . VAL A 186 ? 0.34770 0.45095 0.37446 0.02349  0.02735  -0.04520 186 VAL A CG2 
2864 N N   . ASP A 187 ? 0.28207 0.40411 0.32814 0.01482  0.02213  -0.04197 187 ASP A N   
2865 C CA  . ASP A 187 ? 0.27724 0.41027 0.32734 0.02365  0.02075  -0.04271 187 ASP A CA  
2866 C C   . ASP A 187 ? 0.29746 0.44643 0.34663 0.03656  0.02307  -0.04486 187 ASP A C   
2867 O O   . ASP A 187 ? 0.29524 0.47189 0.35081 0.03825  0.02418  -0.04583 187 ASP A O   
2868 C CB  . ASP A 187 ? 0.28989 0.43752 0.34726 0.01540  0.01952  -0.04224 187 ASP A CB  
2869 C CG  . ASP A 187 ? 0.28932 0.45779 0.35097 0.00364  0.02200  -0.04293 187 ASP A CG  
2870 O OD1 . ASP A 187 ? 0.29038 0.46178 0.34958 0.00095  0.02487  -0.04320 187 ASP A OD1 
2871 O OD2 . ASP A 187 ? 0.25139 0.43251 0.31792 -0.00337 0.02113  -0.04328 187 ASP A OD2 
2876 N N   . ARG A 188 ? 0.25112 0.38303 0.29192 0.04521  0.02382  -0.04574 188 ARG A N   
2877 C CA  . ARG A 188 ? 0.27632 0.41601 0.31274 0.05950  0.02638  -0.04798 188 ARG A CA  
2878 C C   . ARG A 188 ? 0.31561 0.42576 0.34138 0.06864  0.02521  -0.04814 188 ARG A C   
2879 O O   . ARG A 188 ? 0.33238 0.41937 0.35389 0.06152  0.02352  -0.04731 188 ARG A O   
2880 C CB  . ARG A 188 ? 0.31048 0.45763 0.34400 0.05744  0.03014  -0.04988 188 ARG A CB  
2881 C CG  . ARG A 188 ? 0.31724 0.49467 0.35961 0.04793  0.03242  -0.04986 188 ARG A CG  
2882 C CD  . ARG A 188 ? 0.34419 0.51976 0.38218 0.04082  0.03537  -0.05040 188 ARG A CD  
2883 N NE  . ARG A 188 ? 0.30411 0.47963 0.33472 0.05378  0.03831  -0.05326 188 ARG A NE  
2884 C CZ  . ARG A 188 ? 0.34749 0.51203 0.37000 0.05227  0.04028  -0.05442 188 ARG A CZ  
2885 N NH1 . ARG A 188 ? 0.35930 0.51250 0.38013 0.03897  0.03946  -0.05242 188 ARG A NH1 
2886 N NH2 . ARG A 188 ? 0.31737 0.48052 0.33191 0.06523  0.04307  -0.05763 188 ARG A NH2 
2900 N N   . GLN A 189 ? 0.31477 0.42541 0.33495 0.08437  0.02650  -0.04929 189 GLN A N   
2901 C CA  . GLN A 189 ? 0.36710 0.44672 0.37438 0.09233  0.02614  -0.04965 189 GLN A CA  
2902 C C   . GLN A 189 ? 0.40016 0.46503 0.39604 0.09554  0.02901  -0.05279 189 GLN A C   
2903 O O   . GLN A 189 ? 0.42452 0.46635 0.40714 0.10514  0.03003  -0.05419 189 GLN A O   
2904 C CB  . GLN A 189 ? 0.41481 0.49634 0.41869 0.10797  0.02610  -0.04876 189 GLN A CB  
2905 C CG  . GLN A 189 ? 0.38031 0.46974 0.39345 0.10223  0.02253  -0.04567 189 GLN A CG  
2906 C CD  . GLN A 189 ? 0.44449 0.53026 0.45271 0.11641  0.02161  -0.04374 189 GLN A CD  
2907 O OE1 . GLN A 189 ? 0.40519 0.48383 0.41531 0.11250  0.01871  -0.04120 189 GLN A OE1 
2908 N NE2 . GLN A 189 ? 0.46003 0.55016 0.46106 0.13332  0.02423  -0.04475 189 GLN A NE2 
2917 N N   . THR A 190 ? 0.38052 0.45767 0.37995 0.08770  0.03061  -0.05402 190 THR A N   
2918 C CA  . THR A 190 ? 0.41510 0.47824 0.40353 0.08876  0.03297  -0.05709 190 THR A CA  
2919 C C   . THR A 190 ? 0.42596 0.45881 0.40715 0.08031  0.03022  -0.05674 190 THR A C   
2920 O O   . THR A 190 ? 0.42179 0.44933 0.40893 0.07169  0.02682  -0.05381 190 THR A O   
2921 C CB  . THR A 190 ? 0.40337 0.48857 0.39794 0.08084  0.03514  -0.05767 190 THR A CB  
2922 O OG1 . THR A 190 ? 0.42984 0.50551 0.41335 0.08338  0.03793  -0.06104 190 THR A OG1 
2923 C CG2 . THR A 190 ? 0.38708 0.47257 0.38993 0.06371  0.03219  -0.05445 190 THR A CG2 
2931 N N   . ALA A 191 ? 0.44854 0.46296 0.41667 0.08245  0.03183  -0.06003 191 ALA A N   
2932 C CA  . ALA A 191 ? 0.49023 0.47766 0.45023 0.07448  0.02942  -0.06044 191 ALA A CA  
2933 C C   . ALA A 191 ? 0.44376 0.43751 0.41251 0.05945  0.02665  -0.05797 191 ALA A C   
2934 O O   . ALA A 191 ? 0.39775 0.40667 0.37028 0.05510  0.02790  -0.05799 191 ALA A O   
2935 C CB  . ALA A 191 ? 0.56370 0.53260 0.50700 0.07890  0.03201  -0.06530 191 ALA A CB  
2941 N N   . GLN A 192 ? 0.42796 0.41129 0.40006 0.05224  0.02314  -0.05532 192 GLN A N   
2942 C CA  . GLN A 192 ? 0.42367 0.41012 0.40275 0.03971  0.02035  -0.05256 192 GLN A CA  
2943 C C   . GLN A 192 ? 0.47682 0.44232 0.45056 0.03482  0.01754  -0.05238 192 GLN A C   
2944 O O   . GLN A 192 ? 0.49267 0.44500 0.46164 0.03968  0.01746  -0.05282 192 GLN A O   
2945 C CB  . GLN A 192 ? 0.45123 0.45467 0.44383 0.03586  0.01925  -0.04875 192 GLN A CB  
2946 C CG  . GLN A 192 ? 0.42823 0.45472 0.42654 0.04008  0.02214  -0.04914 192 GLN A CG  
2947 C CD  . GLN A 192 ? 0.42600 0.46716 0.43580 0.03468  0.02101  -0.04610 192 GLN A CD  
2948 O OE1 . GLN A 192 ? 0.36857 0.40981 0.38235 0.02459  0.01965  -0.04362 192 GLN A OE1 
2949 N NE2 . GLN A 192 ? 0.38789 0.44065 0.40215 0.04178  0.02147  -0.04621 192 GLN A NE2 
2958 N N   . ALA A 193 ? 0.53221 0.49479 0.50541 0.02561  0.01548  -0.05180 193 ALA A N   
2959 C CA  . ALA A 193 ? 0.49521 0.44228 0.46468 0.01966  0.01267  -0.05159 193 ALA A CA  
2960 C C   . ALA A 193 ? 0.42920 0.38440 0.40758 0.01091  0.00967  -0.04772 193 ALA A C   
2961 O O   . ALA A 193 ? 0.47708 0.44314 0.45838 0.00792  0.00976  -0.04639 193 ALA A O   
2962 C CB  . ALA A 193 ? 0.52929 0.46108 0.48455 0.01803  0.01311  -0.05611 193 ALA A CB  
2968 N N   . ALA A 194 ? 0.47288 0.42210 0.45444 0.00734  0.00732  -0.04575 194 ALA A N   
2969 C CA  . ALA A 194 ? 0.47808 0.43332 0.46640 0.00034  0.00451  -0.04229 194 ALA A CA  
2970 C C   . ALA A 194 ? 0.50132 0.45430 0.48332 -0.00528 0.00278  -0.04368 194 ALA A C   
2971 O O   . ALA A 194 ? 0.51128 0.45321 0.48376 -0.00651 0.00284  -0.04744 194 ALA A O   
2972 C CB  . ALA A 194 ? 0.50890 0.45946 0.50168 -0.00127 0.00286  -0.04024 194 ALA A CB  
2978 N N   . GLY A 195 ? 0.54049 0.50331 0.52622 -0.00860 0.00140  -0.04080 195 GLY A N   
2979 C CA  . GLY A 195 ? 0.55727 0.52074 0.53797 -0.01381 -0.00104 -0.04139 195 GLY A CA  
2980 C C   . GLY A 195 ? 0.50031 0.46007 0.48196 -0.01868 -0.00392 -0.04122 195 GLY A C   
2981 O O   . GLY A 195 ? 0.44888 0.40500 0.43517 -0.01805 -0.00388 -0.04014 195 GLY A O   
2985 N N   . THR A 196 ? 0.45913 0.42104 0.43572 -0.02421 -0.00642 -0.04258 196 THR A N   
2986 C CA  . THR A 196 ? 0.46735 0.42939 0.44517 -0.03014 -0.00909 -0.04258 196 THR A CA  
2987 C C   . THR A 196 ? 0.40612 0.37770 0.39522 -0.02879 -0.01049 -0.03719 196 THR A C   
2988 O O   . THR A 196 ? 0.48090 0.46128 0.47422 -0.02594 -0.01101 -0.03335 196 THR A O   
2989 C CB  . THR A 196 ? 0.45520 0.42293 0.42676 -0.03681 -0.01200 -0.04470 196 THR A CB  
2990 O OG1 . THR A 196 ? 0.53890 0.49586 0.49838 -0.03763 -0.01021 -0.05023 196 THR A OG1 
2991 C CG2 . THR A 196 ? 0.49555 0.46422 0.46759 -0.04446 -0.01430 -0.04569 196 THR A CG2 
2999 N N   . ASP A 197 ? 0.41955 0.38779 0.41221 -0.03054 -0.01065 -0.03687 197 ASP A N   
3000 C CA  . ASP A 197 ? 0.41868 0.39572 0.42133 -0.02858 -0.01162 -0.03212 197 ASP A CA  
3001 C C   . ASP A 197 ? 0.45248 0.44231 0.45748 -0.03316 -0.01500 -0.03063 197 ASP A C   
3002 O O   . ASP A 197 ? 0.49393 0.48512 0.49345 -0.03986 -0.01665 -0.03380 197 ASP A O   
3003 C CB  . ASP A 197 ? 0.39624 0.36644 0.40251 -0.02743 -0.01008 -0.03178 197 ASP A CB  
3004 C CG  . ASP A 197 ? 0.42040 0.39708 0.43578 -0.02304 -0.00991 -0.02733 197 ASP A CG  
3005 O OD1 . ASP A 197 ? 0.44638 0.42918 0.46398 -0.01999 -0.01019 -0.02458 197 ASP A OD1 
3006 O OD2 . ASP A 197 ? 0.41550 0.38988 0.43441 -0.02285 -0.00929 -0.02660 197 ASP A OD2 
3011 N N   . THR A 198 ? 0.40523 0.40497 0.41757 -0.02924 -0.01595 -0.02590 198 THR A N   
3012 C CA  . THR A 198 ? 0.41493 0.43023 0.43066 -0.03097 -0.01910 -0.02358 198 THR A CA  
3013 C C   . THR A 198 ? 0.39546 0.41536 0.41943 -0.02809 -0.01871 -0.02040 198 THR A C   
3014 O O   . THR A 198 ? 0.35844 0.36935 0.38492 -0.02426 -0.01622 -0.01954 198 THR A O   
3015 C CB  . THR A 198 ? 0.39943 0.42315 0.41375 -0.02659 -0.02062 -0.02020 198 THR A CB  
3016 O OG1 . THR A 198 ? 0.41072 0.42681 0.42627 -0.02000 -0.01805 -0.01717 198 THR A OG1 
3017 C CG2 . THR A 198 ? 0.48416 0.50674 0.48984 -0.03030 -0.02148 -0.02351 198 THR A CG2 
3025 N N   . THR A 199 ? 0.33206 0.36785 0.36012 -0.02969 -0.02120 -0.01872 199 THR A N   
3026 C CA  . THR A 199 ? 0.30383 0.34641 0.33952 -0.02652 -0.02069 -0.01582 199 THR A CA  
3027 C C   . THR A 199 ? 0.29661 0.34385 0.33492 -0.01661 -0.02066 -0.01070 199 THR A C   
3028 O O   . THR A 199 ? 0.29803 0.35203 0.33347 -0.01341 -0.02250 -0.00849 199 THR A O   
3029 C CB  . THR A 199 ? 0.34076 0.40017 0.37964 -0.03327 -0.02294 -0.01671 199 THR A CB  
3030 O OG1 . THR A 199 ? 0.35332 0.40309 0.38727 -0.04311 -0.02217 -0.02148 199 THR A OG1 
3031 C CG2 . THR A 199 ? 0.31423 0.38331 0.36103 -0.02944 -0.02218 -0.01370 199 THR A CG2 
3039 N N   . ILE A 200 ? 0.29015 0.33190 0.33223 -0.01162 -0.01835 -0.00882 200 ILE A N   
3040 C CA  . ILE A 200 ? 0.26599 0.30605 0.30785 -0.00226 -0.01739 -0.00441 200 ILE A CA  
3041 C C   . ILE A 200 ? 0.29982 0.35833 0.34604 0.00249  -0.01922 -0.00116 200 ILE A C   
3042 O O   . ILE A 200 ? 0.25970 0.32355 0.31120 0.00413  -0.01823 -0.00069 200 ILE A O   
3043 C CB  . ILE A 200 ? 0.26002 0.28591 0.30258 0.00053  -0.01407 -0.00444 200 ILE A CB  
3044 C CG1 . ILE A 200 ? 0.27092 0.28314 0.31033 -0.00412 -0.01251 -0.00791 200 ILE A CG1 
3045 C CG2 . ILE A 200 ? 0.29825 0.31923 0.33807 0.00906  -0.01270 -0.00039 200 ILE A CG2 
3046 C CD1 . ILE A 200 ? 0.26919 0.27250 0.31108 -0.00361 -0.00997 -0.00901 200 ILE A CD1 
3058 N N   . THR A 201 ? 0.31795 0.38781 0.36170 0.00523  -0.02191 0.00119  201 THR A N   
3059 C CA  . THR A 201 ? 0.28608 0.37883 0.33429 0.00943  -0.02439 0.00397  201 THR A CA  
3060 C C   . THR A 201 ? 0.29050 0.38303 0.34065 0.02064  -0.02230 0.00798  201 THR A C   
3061 O O   . THR A 201 ? 0.27092 0.38000 0.32773 0.02245  -0.02262 0.00858  201 THR A O   
3062 C CB  . THR A 201 ? 0.29120 0.39471 0.33484 0.01187  -0.02767 0.00625  201 THR A CB  
3063 O OG1 . THR A 201 ? 0.32018 0.42050 0.36018 0.00160  -0.02906 0.00191  201 THR A OG1 
3064 C CG2 . THR A 201 ? 0.29188 0.42547 0.34103 0.01548  -0.03109 0.00875  201 THR A CG2 
3072 N N   . VAL A 202 ? 0.26948 0.34375 0.31295 0.02822  -0.01992 0.01074  202 VAL A N   
3073 C CA  . VAL A 202 ? 0.27986 0.35196 0.32280 0.03960  -0.01769 0.01436  202 VAL A CA  
3074 C C   . VAL A 202 ? 0.27040 0.34127 0.31968 0.03701  -0.01535 0.01161  202 VAL A C   
3075 O O   . VAL A 202 ? 0.27176 0.35131 0.32390 0.04481  -0.01428 0.01358  202 VAL A O   
3076 C CB  . VAL A 202 ? 0.28274 0.33087 0.31493 0.04621  -0.01490 0.01725  202 VAL A CB  
3077 C CG1 . VAL A 202 ? 0.34717 0.37377 0.37705 0.03789  -0.01218 0.01343  202 VAL A CG1 
3078 C CG2 . VAL A 202 ? 0.32002 0.36331 0.34851 0.05908  -0.01243 0.02107  202 VAL A CG2 
3088 N N   . ASN A 203 ? 0.26623 0.32721 0.31712 0.02703  -0.01444 0.00729  203 ASN A N   
3089 C CA  . ASN A 203 ? 0.28355 0.34264 0.33942 0.02397  -0.01230 0.00482  203 ASN A CA  
3090 C C   . ASN A 203 ? 0.27881 0.36095 0.34260 0.01965  -0.01397 0.00402  203 ASN A C   
3091 O O   . ASN A 203 ? 0.24713 0.33561 0.31502 0.02272  -0.01223 0.00446  203 ASN A O   
3092 C CB  . ASN A 203 ? 0.27265 0.31496 0.32682 0.01586  -0.01097 0.00104  203 ASN A CB  
3093 C CG  . ASN A 203 ? 0.29924 0.32136 0.34703 0.01919  -0.00853 0.00141  203 ASN A CG  
3094 O OD1 . ASN A 203 ? 0.29353 0.31050 0.33623 0.02667  -0.00770 0.00454  203 ASN A OD1 
3095 N ND2 . ASN A 203 ? 0.31598 0.32671 0.36316 0.01352  -0.00727 -0.00170 203 ASN A ND2 
3102 N N   . VAL A 204 ? 0.26356 0.35716 0.32859 0.01178  -0.01696 0.00249  204 VAL A N   
3103 C CA  . VAL A 204 ? 0.24400 0.36134 0.31573 0.00601  -0.01862 0.00166  204 VAL A CA  
3104 C C   . VAL A 204 ? 0.23000 0.36848 0.30622 0.01676  -0.01901 0.00567  204 VAL A C   
3105 O O   . VAL A 204 ? 0.22425 0.37729 0.30673 0.01661  -0.01784 0.00572  204 VAL A O   
3106 C CB  . VAL A 204 ? 0.26026 0.38620 0.33051 -0.00408 -0.02199 -0.00077 204 VAL A CB  
3107 C CG1 . VAL A 204 ? 0.26040 0.41310 0.33709 -0.01145 -0.02376 -0.00171 204 VAL A CG1 
3108 C CG2 . VAL A 204 ? 0.25927 0.36263 0.32403 -0.01388 -0.02088 -0.00516 204 VAL A CG2 
3118 N N   . LEU A 205 ? 0.27280 0.41353 0.34519 0.02699  -0.02041 0.00936  205 LEU A N   
3119 C CA  . LEU A 205 ? 0.23335 0.39376 0.30875 0.03982  -0.02058 0.01364  205 LEU A CA  
3120 C C   . LEU A 205 ? 0.29006 0.44054 0.36557 0.04828  -0.01633 0.01454  205 LEU A C   
3121 O O   . LEU A 205 ? 0.28446 0.45498 0.36561 0.05464  -0.01559 0.01609  205 LEU A O   
3122 C CB  . LEU A 205 ? 0.25450 0.41338 0.32282 0.05090  -0.02230 0.01808  205 LEU A CB  
3123 C CG  . LEU A 205 ? 0.25986 0.43519 0.32835 0.04418  -0.02699 0.01762  205 LEU A CG  
3124 C CD1 . LEU A 205 ? 0.29776 0.46340 0.35655 0.05342  -0.02815 0.02180  205 LEU A CD1 
3125 C CD2 . LEU A 205 ? 0.21903 0.43319 0.29666 0.04357  -0.03012 0.01824  205 LEU A CD2 
3137 N N   . ALA A 206 ? 0.26983 0.39061 0.33841 0.04951  -0.01343 0.01371  206 ALA A N   
3138 C CA  . ALA A 206 ? 0.30196 0.41172 0.36942 0.05598  -0.00937 0.01366  206 ALA A CA  
3139 C C   . ALA A 206 ? 0.26147 0.38469 0.33748 0.04865  -0.00833 0.01095  206 ALA A C   
3140 O O   . ALA A 206 ? 0.27783 0.41088 0.35679 0.05582  -0.00603 0.01192  206 ALA A O   
3141 C CB  . ALA A 206 ? 0.31111 0.38884 0.37025 0.05419  -0.00694 0.01206  206 ALA A CB  
3147 N N   . TRP A 207 ? 0.23697 0.36019 0.31591 0.03466  -0.00967 0.00765  207 TRP A N   
3148 C CA  . TRP A 207 ? 0.26645 0.39923 0.35140 0.02620  -0.00845 0.00537  207 TRP A CA  
3149 C C   . TRP A 207 ? 0.26405 0.43038 0.35715 0.02604  -0.00973 0.00671  207 TRP A C   
3150 O O   . TRP A 207 ? 0.26803 0.44612 0.36604 0.02535  -0.00744 0.00646  207 TRP A O   
3151 C CB  . TRP A 207 ? 0.27638 0.39665 0.35940 0.01217  -0.00943 0.00185  207 TRP A CB  
3152 C CG  . TRP A 207 ? 0.26792 0.39451 0.35444 0.00111  -0.00842 -0.00036 207 TRP A CG  
3153 C CD1 . TRP A 207 ? 0.30275 0.41857 0.38866 -0.00080 -0.00528 -0.00143 207 TRP A CD1 
3154 C CD2 . TRP A 207 ? 0.29132 0.43334 0.38046 -0.01077 -0.01034 -0.00190 207 TRP A CD2 
3155 N NE1 . TRP A 207 ? 0.31724 0.44074 0.40494 -0.01281 -0.00499 -0.00298 207 TRP A NE1 
3156 C CE2 . TRP A 207 ? 0.29778 0.43668 0.38723 -0.01963 -0.00792 -0.00350 207 TRP A CE2 
3157 C CE3 . TRP A 207 ? 0.29860 0.45712 0.38897 -0.01547 -0.01385 -0.00217 207 TRP A CE3 
3158 C CZ2 . TRP A 207 ? 0.32848 0.47802 0.41853 -0.03366 -0.00855 -0.00535 207 TRP A CZ2 
3159 C CZ3 . TRP A 207 ? 0.37712 0.54741 0.46866 -0.02984 -0.01476 -0.00460 207 TRP A CZ3 
3160 C CH2 . TRP A 207 ? 0.32734 0.49239 0.41842 -0.03899 -0.01192 -0.00612 207 TRP A CH2 
3171 N N   . LEU A 208 ? 0.25525 0.43966 0.34996 0.02666  -0.01335 0.00818  208 LEU A N   
3172 C CA  . LEU A 208 ? 0.25027 0.47061 0.35339 0.02740  -0.01463 0.00957  208 LEU A CA  
3173 C C   . LEU A 208 ? 0.24544 0.47479 0.35013 0.04443  -0.01204 0.01302  208 LEU A C   
3174 O O   . LEU A 208 ? 0.24783 0.50189 0.35992 0.04541  -0.01067 0.01343  208 LEU A O   
3175 C CB  . LEU A 208 ? 0.25174 0.49099 0.35563 0.02553  -0.01942 0.01051  208 LEU A CB  
3176 C CG  . LEU A 208 ? 0.24109 0.47481 0.34284 0.00788  -0.02192 0.00642  208 LEU A CG  
3177 C CD1 . LEU A 208 ? 0.25247 0.50384 0.35338 0.00760  -0.02681 0.00734  208 LEU A CD1 
3178 C CD2 . LEU A 208 ? 0.27921 0.52770 0.38652 -0.00711 -0.02104 0.00335  208 LEU A CD2 
3190 N N   . TYR A 209 ? 0.28442 0.49246 0.38100 0.05784  -0.01089 0.01540  209 TYR A N   
3191 C CA  . TYR A 209 ? 0.30544 0.51569 0.40040 0.07491  -0.00769 0.01828  209 TYR A CA  
3192 C C   . TYR A 209 ? 0.30094 0.50362 0.39748 0.07277  -0.00331 0.01584  209 TYR A C   
3193 O O   . TYR A 209 ? 0.30491 0.52615 0.40565 0.08132  -0.00092 0.01703  209 TYR A O   
3194 C CB  . TYR A 209 ? 0.25575 0.43911 0.33865 0.08790  -0.00685 0.02105  209 TYR A CB  
3195 C CG  . TYR A 209 ? 0.29724 0.49432 0.37760 0.09808  -0.01016 0.02556  209 TYR A CG  
3196 C CD1 . TYR A 209 ? 0.33944 0.56393 0.42307 0.11269  -0.01036 0.02939  209 TYR A CD1 
3197 C CD2 . TYR A 209 ? 0.33757 0.52073 0.41167 0.09380  -0.01297 0.02618  209 TYR A CD2 
3198 C CE1 . TYR A 209 ? 0.28181 0.51983 0.36238 0.12310  -0.01368 0.03402  209 TYR A CE1 
3199 C CE2 . TYR A 209 ? 0.27610 0.47130 0.34667 0.10330  -0.01607 0.03067  209 TYR A CE2 
3200 C CZ  . TYR A 209 ? 0.31449 0.53687 0.38812 0.11827  -0.01652 0.03474  209 TYR A CZ  
3201 O OH  . TYR A 209 ? 0.32789 0.56226 0.39722 0.12834  -0.01983 0.03956  209 TYR A OH  
3211 N N   . ALA A 210 ? 0.32682 0.50409 0.41986 0.06214  -0.00219 0.01254  210 ALA A N   
3212 C CA  . ALA A 210 ? 0.31514 0.48657 0.40949 0.05830  0.00146  0.01018  210 ALA A CA  
3213 C C   . ALA A 210 ? 0.33991 0.54200 0.44431 0.05028  0.00153  0.00967  210 ALA A C   
3214 O O   . ALA A 210 ? 0.32916 0.54001 0.43623 0.05370  0.00497  0.00954  210 ALA A O   
3215 C CB  . ALA A 210 ? 0.27779 0.42135 0.36740 0.04711  0.00178  0.00698  210 ALA A CB  
3221 N N   . ALA A 211 ? 0.26661 0.48526 0.37588 0.03860  -0.00201 0.00912  211 ALA A N   
3222 C CA  . ALA A 211 ? 0.26610 0.51479 0.38412 0.02887  -0.00178 0.00849  211 ALA A CA  
3223 C C   . ALA A 211 ? 0.30883 0.59074 0.43373 0.04143  -0.00091 0.01136  211 ALA A C   
3224 O O   . ALA A 211 ? 0.29809 0.59809 0.42851 0.04016  0.00213  0.01119  211 ALA A O   
3225 C CB  . ALA A 211 ? 0.33322 0.59148 0.45317 0.01303  -0.00568 0.00678  211 ALA A CB  
3231 N N   . VAL A 212 ? 0.27032 0.56096 0.39438 0.05462  -0.00327 0.01429  212 VAL A N   
3232 C CA  . VAL A 212 ? 0.30058 0.62305 0.43032 0.06946  -0.00237 0.01745  212 VAL A CA  
3233 C C   . VAL A 212 ? 0.36999 0.68012 0.49589 0.08308  0.00298  0.01793  212 VAL A C   
3234 O O   . VAL A 212 ? 0.31222 0.64891 0.44445 0.08932  0.00568  0.01876  212 VAL A O   
3235 C CB  . VAL A 212 ? 0.31044 0.64066 0.43755 0.08265  -0.00597 0.02111  212 VAL A CB  
3236 C CG1 . VAL A 212 ? 0.34650 0.70604 0.47752 0.10168  -0.00458 0.02483  212 VAL A CG1 
3237 C CG2 . VAL A 212 ? 0.27763 0.62474 0.40872 0.06892  -0.01143 0.02027  212 VAL A CG2 
3247 N N   . ILE A 213 ? 0.30869 0.57925 0.42373 0.08771  0.00476  0.01713  213 ILE A N   
3248 C CA  . ILE A 213 ? 0.38191 0.63780 0.49136 0.09950  0.00990  0.01680  213 ILE A CA  
3249 C C   . ILE A 213 ? 0.33028 0.59580 0.44546 0.08945  0.01306  0.01423  213 ILE A C   
3250 O O   . ILE A 213 ? 0.33841 0.61375 0.45424 0.09931  0.01716  0.01447  213 ILE A O   
3251 C CB  . ILE A 213 ? 0.40299 0.61457 0.49929 0.10235  0.01091  0.01568  213 ILE A CB  
3252 C CG1 . ILE A 213 ? 0.36408 0.56616 0.45219 0.11717  0.00955  0.01920  213 ILE A CG1 
3253 C CG2 . ILE A 213 ? 0.41667 0.61003 0.50700 0.10722  0.01613  0.01345  213 ILE A CG2 
3254 C CD1 . ILE A 213 ? 0.48187 0.64211 0.55730 0.11560  0.00981  0.01814  213 ILE A CD1 
3266 N N   . ASN A 214 ? 0.30187 0.56306 0.41984 0.07032  0.01156  0.01184  214 ASN A N   
3267 C CA  . ASN A 214 ? 0.34953 0.61945 0.47174 0.05943  0.01446  0.01003  214 ASN A CA  
3268 C C   . ASN A 214 ? 0.35905 0.67269 0.49292 0.05326  0.01414  0.01106  214 ASN A C   
3269 O O   . ASN A 214 ? 0.41142 0.73434 0.54877 0.04069  0.01633  0.00980  214 ASN A O   
3270 C CB  . ASN A 214 ? 0.34059 0.58517 0.45873 0.04247  0.01341  0.00744  214 ASN A CB  
3271 C CG  . ASN A 214 ? 0.46485 0.67268 0.57304 0.04672  0.01550  0.00578  214 ASN A CG  
3272 O OD1 . ASN A 214 ? 0.47973 0.68198 0.58589 0.04643  0.01913  0.00463  214 ASN A OD1 
3273 N ND2 . ASN A 214 ? 0.43168 0.61585 0.53347 0.04971  0.01321  0.00555  214 ASN A ND2 
3280 N N   . GLY A 215 ? 0.30665 0.64820 0.44606 0.06200  0.01172  0.01349  215 GLY A N   
3281 C CA  . GLY A 215 ? 0.32484 0.71249 0.47584 0.05838  0.01185  0.01448  215 GLY A CA  
3282 C C   . GLY A 215 ? 0.35116 0.75948 0.50841 0.03918  0.00778  0.01347  215 GLY A C   
3283 O O   . GLY A 215 ? 0.37436 0.82068 0.54104 0.03134  0.00845  0.01353  215 GLY A O   
3287 N N   . ASP A 216 ? 0.27760 0.66366 0.42952 0.03104  0.00376  0.01231  216 ASP A N   
3288 C CA  . ASP A 216 ? 0.29415 0.69564 0.44954 0.01256  -0.00017 0.01068  216 ASP A CA  
3289 C C   . ASP A 216 ? 0.33019 0.74840 0.48740 0.02061  -0.00531 0.01256  216 ASP A C   
3290 O O   . ASP A 216 ? 0.35805 0.75232 0.50825 0.03286  -0.00678 0.01398  216 ASP A O   
3291 C CB  . ASP A 216 ? 0.37216 0.73654 0.51903 -0.00364 -0.00063 0.00756  216 ASP A CB  
3292 C CG  . ASP A 216 ? 0.45464 0.83252 0.60340 -0.02691 -0.00189 0.00496  216 ASP A CG  
3293 O OD1 . ASP A 216 ? 0.55214 0.97041 0.70947 -0.03176 -0.00355 0.00531  216 ASP A OD1 
3294 O OD2 . ASP A 216 ? 0.50664 0.85473 0.64752 -0.04029 -0.00106 0.00251  216 ASP A OD2 
3299 N N   . ARG A 217 ? 0.28381 0.74503 0.45018 0.01463  -0.00783 0.01289  217 ARG A N   
3300 C CA  . ARG A 217 ? 0.28060 0.76272 0.44900 0.02218  -0.01308 0.01491  217 ARG A CA  
3301 C C   . ARG A 217 ? 0.26377 0.76773 0.43560 0.00089  -0.01741 0.01203  217 ARG A C   
3302 O O   . ARG A 217 ? 0.24567 0.76706 0.41678 0.00492  -0.02178 0.01328  217 ARG A O   
3303 C CB  . ARG A 217 ? 0.31930 0.83367 0.49213 0.04221  -0.01240 0.01891  217 ARG A CB  
3304 C CG  . ARG A 217 ? 0.34764 0.84318 0.51661 0.06625  -0.00871 0.02196  217 ARG A CG  
3305 C CD  . ARG A 217 ? 0.30346 0.81763 0.46986 0.08351  -0.00695 0.02505  217 ARG A CD  
3306 N NE  . ARG A 217 ? 0.37102 0.90314 0.53466 0.08897  -0.01160 0.02747  217 ARG A NE  
3307 C CZ  . ARG A 217 ? 0.39108 0.91104 0.54676 0.10837  -0.01296 0.03132  217 ARG A CZ  
3308 N NH1 . ARG A 217 ? 0.41711 0.90483 0.56567 0.12427  -0.00996 0.03304  217 ARG A NH1 
3309 N NH2 . ARG A 217 ? 0.34039 0.87956 0.49372 0.11152  -0.01709 0.03348  217 ARG A NH2 
3323 N N   . TRP A 218 ? 0.22555 0.72012 0.39583 -0.02181 -0.01584 0.00804  218 TRP A N   
3324 C CA  . TRP A 218 ? 0.26180 0.77428 0.43140 -0.04278 -0.01884 0.00485  218 TRP A CA  
3325 C C   . TRP A 218 ? 0.19555 0.70072 0.36070 -0.04577 -0.02461 0.00359  218 TRP A C   
3326 O O   . TRP A 218 ? 0.19187 0.71217 0.35365 -0.05721 -0.02749 0.00157  218 TRP A O   
3327 C CB  . TRP A 218 ? 0.34670 0.84403 0.51279 -0.06651 -0.01565 0.00094  218 TRP A CB  
3328 C CG  . TRP A 218 ? 0.30287 0.75079 0.45792 -0.07368 -0.01510 -0.00153 218 TRP A CG  
3329 C CD1 . TRP A 218 ? 0.30493 0.71546 0.45364 -0.06942 -0.01075 -0.00117 218 TRP A CD1 
3330 C CD2 . TRP A 218 ? 0.31427 0.74193 0.46043 -0.08575 -0.01865 -0.00491 218 TRP A CD2 
3331 N NE1 . TRP A 218 ? 0.33534 0.70599 0.47258 -0.07724 -0.01160 -0.00381 218 TRP A NE1 
3332 C CE2 . TRP A 218 ? 0.36360 0.74286 0.49881 -0.08693 -0.01614 -0.00618 218 TRP A CE2 
3333 C CE3 . TRP A 218 ? 0.32919 0.77586 0.47513 -0.09547 -0.02371 -0.00718 218 TRP A CE3 
3334 C CZ2 . TRP A 218 ? 0.42137 0.77121 0.54571 -0.09629 -0.01820 -0.00951 218 TRP A CZ2 
3335 C CZ3 . TRP A 218 ? 0.37246 0.78772 0.50676 -0.10558 -0.02569 -0.01081 218 TRP A CZ3 
3336 C CH2 . TRP A 218 ? 0.39553 0.76295 0.51928 -0.10536 -0.02275 -0.01187 218 TRP A CH2 
3347 N N   . PHE A 219 ? 0.19731 0.66553 0.35497 -0.03580 -0.02506 0.00437  219 PHE A N   
3348 C CA  . PHE A 219 ? 0.22973 0.68255 0.37985 -0.03924 -0.02964 0.00289  219 PHE A CA  
3349 C C   . PHE A 219 ? 0.26969 0.73805 0.42113 -0.01986 -0.03344 0.00715  219 PHE A C   
3350 O O   . PHE A 219 ? 0.27322 0.73188 0.41835 -0.02140 -0.03736 0.00644  219 PHE A O   
3351 C CB  . PHE A 219 ? 0.28715 0.68757 0.42592 -0.04037 -0.02755 0.00121  219 PHE A CB  
3352 C CG  . PHE A 219 ? 0.26176 0.63971 0.39916 -0.02215 -0.02371 0.00445  219 PHE A CG  
3353 C CD1 . PHE A 219 ? 0.26547 0.63512 0.39999 -0.00281 -0.02489 0.00814  219 PHE A CD1 
3354 C CD2 . PHE A 219 ? 0.29253 0.65762 0.43037 -0.02482 -0.01877 0.00379  219 PHE A CD2 
3355 C CE1 . PHE A 219 ? 0.22497 0.57245 0.35659 0.01249  -0.02106 0.01054  219 PHE A CE1 
3356 C CE2 . PHE A 219 ? 0.28399 0.62914 0.41978 -0.00878 -0.01531 0.00618  219 PHE A CE2 
3357 C CZ  . PHE A 219 ? 0.23079 0.56669 0.36325 0.00931  -0.01644 0.00927  219 PHE A CZ  
3367 N N   . LEU A 220 ? 0.24850 0.73729 0.40620 -0.00054 -0.03203 0.01175  220 LEU A N   
3368 C CA  . LEU A 220 ? 0.23403 0.73944 0.39180 0.01903  -0.03550 0.01651  220 LEU A CA  
3369 C C   . LEU A 220 ? 0.29759 0.83335 0.45473 0.01073  -0.03933 0.01559  220 LEU A C   
3370 O O   . LEU A 220 ? 0.24342 0.79662 0.40258 -0.00593 -0.03837 0.01226  220 LEU A O   
3371 C CB  . LEU A 220 ? 0.22037 0.73380 0.38027 0.04143  -0.03165 0.02118  220 LEU A CB  
3372 C CG  . LEU A 220 ? 0.20678 0.68001 0.36164 0.04919  -0.02645 0.02140  220 LEU A CG  
3373 C CD1 . LEU A 220 ? 0.28575 0.77314 0.44371 0.07144  -0.02295 0.02559  220 LEU A CD1 
3374 C CD2 . LEU A 220 ? 0.31683 0.74697 0.45923 0.05410  -0.02738 0.02202  220 LEU A CD2 
3386 N N   . ASN A 221 ? 0.31225 0.85238 0.46459 0.02245  -0.04322 0.01870  221 ASN A N   
3387 C CA  . ASN A 221 ? 0.26845 0.83834 0.41914 0.01764  -0.04626 0.01840  221 ASN A CA  
3388 C C   . ASN A 221 ? 0.26911 0.84931 0.41598 0.04239  -0.04730 0.02479  221 ASN A C   
3389 O O   . ASN A 221 ? 0.29994 0.85998 0.44362 0.06197  -0.04572 0.02917  221 ASN A O   
3390 C CB  . ASN A 221 ? 0.29559 0.86111 0.44169 -0.00159 -0.05075 0.01382  221 ASN A CB  
3391 C CG  . ASN A 221 ? 0.33568 0.87798 0.47578 0.00697  -0.05432 0.01567  221 ASN A CG  
3392 O OD1 . ASN A 221 ? 0.26355 0.80266 0.40083 0.02859  -0.05479 0.02145  221 ASN A OD1 
3393 N ND2 . ASN A 221 ? 0.35446 0.87878 0.49083 -0.01042 -0.05655 0.01069  221 ASN A ND2 
3400 N N   . ARG A 222 ? 0.22970 0.83991 0.37543 0.04107  -0.04964 0.02524  222 ARG A N   
3401 C CA  . ARG A 222 ? 0.24225 0.86705 0.38384 0.06375  -0.05007 0.03128  222 ARG A CA  
3402 C C   . ARG A 222 ? 0.29328 0.90159 0.42660 0.07357  -0.05386 0.03445  222 ARG A C   
3403 O O   . ARG A 222 ? 0.31183 0.93014 0.43968 0.09193  -0.05437 0.03971  222 ARG A O   
3404 C CB  . ARG A 222 ? 0.26147 0.92828 0.40557 0.05819  -0.05074 0.03049  222 ARG A CB  
3405 C CG  . ARG A 222 ? 0.27456 0.95723 0.41628 0.04180  -0.05554 0.02720  222 ARG A CG  
3406 C CD  . ARG A 222 ? 0.31772 1.04511 0.46168 0.04092  -0.05549 0.02755  222 ARG A CD  
3407 N NE  . ARG A 222 ? 0.42741 1.17445 0.56803 0.03033  -0.05981 0.02555  222 ARG A NE  
3408 C CZ  . ARG A 222 ? 0.48177 1.22871 0.62180 0.00480  -0.06161 0.01911  222 ARG A CZ  
3409 N NH1 . ARG A 222 ? 0.48097 1.20662 0.62290 -0.01276 -0.05957 0.01425  222 ARG A NH1 
3410 N NH2 . ARG A 222 ? 0.38220 1.15035 0.51858 -0.00331 -0.06518 0.01744  222 ARG A NH2 
3424 N N   . PHE A 223 ? 0.28217 0.86797 0.41356 0.06071  -0.05659 0.03125  223 PHE A N   
3425 C CA  . PHE A 223 ? 0.32396 0.89959 0.44697 0.06557  -0.06093 0.03343  223 PHE A CA  
3426 C C   . PHE A 223 ? 0.29000 0.82989 0.40674 0.08209  -0.05987 0.03790  223 PHE A C   
3427 O O   . PHE A 223 ? 0.29121 0.81093 0.41077 0.08482  -0.05635 0.03765  223 PHE A O   
3428 C CB  . PHE A 223 ? 0.27713 0.85078 0.39890 0.04171  -0.06503 0.02713  223 PHE A CB  
3429 C CG  . PHE A 223 ? 0.36054 0.96585 0.48536 0.02451  -0.06604 0.02264  223 PHE A CG  
3430 C CD1 . PHE A 223 ? 0.33838 0.97362 0.46134 0.03244  -0.06773 0.02554  223 PHE A CD1 
3431 C CD2 . PHE A 223 ? 0.36563 0.96978 0.49393 0.00049  -0.06489 0.01567  223 PHE A CD2 
3432 C CE1 . PHE A 223 ? 0.36964 1.03644 0.49516 0.01658  -0.06841 0.02148  223 PHE A CE1 
3433 C CE2 . PHE A 223 ? 0.40258 1.03484 0.53187 -0.01584 -0.06528 0.01167  223 PHE A CE2 
3434 C CZ  . PHE A 223 ? 0.39338 1.05800 0.52173 -0.00798 -0.06715 0.01449  223 PHE A CZ  
3444 N N   . THR A 224 ? 0.28457 0.81704 0.39170 0.09355  -0.06262 0.04229  224 THR A N   
3445 C CA  . THR A 224 ? 0.29000 0.78635 0.38861 0.10492  -0.06231 0.04605  224 THR A CA  
3446 C C   . THR A 224 ? 0.36615 0.85615 0.45846 0.09466  -0.06760 0.04453  224 THR A C   
3447 O O   . THR A 224 ? 0.44792 0.96088 0.54178 0.08066  -0.07113 0.04073  224 THR A O   
3448 C CB  . THR A 224 ? 0.33689 0.82220 0.42564 0.13159  -0.05930 0.05401  224 THR A CB  
3449 O OG1 . THR A 224 ? 0.43024 0.87521 0.50991 0.14059  -0.05772 0.05717  224 THR A OG1 
3450 C CG2 . THR A 224 ? 0.44216 0.94539 0.52349 0.13900  -0.06244 0.05776  224 THR A CG2 
3458 N N   . THR A 225 ? 0.30337 0.75357 0.38456 0.10019  -0.06595 0.04673  225 THR A N   
3459 C CA  . THR A 225 ? 0.36614 0.80067 0.43810 0.08932  -0.06866 0.04447  225 THR A CA  
3460 C C   . THR A 225 ? 0.36216 0.76419 0.41894 0.10635  -0.06669 0.05132  225 THR A C   
3461 O O   . THR A 225 ? 0.39088 0.77615 0.44363 0.12351  -0.06258 0.05652  225 THR A O   
3462 C CB  . THR A 225 ? 0.38624 0.79373 0.45889 0.06696  -0.06612 0.03606  225 THR A CB  
3463 O OG1 . THR A 225 ? 0.41583 0.80969 0.47900 0.05730  -0.06857 0.03360  225 THR A OG1 
3464 C CG2 . THR A 225 ? 0.36751 0.73301 0.43693 0.07144  -0.05932 0.03631  225 THR A CG2 
3472 N N   . THR A 226 ? 0.35427 0.74545 0.40134 0.10080  -0.06918 0.05105  226 THR A N   
3473 C CA  . THR A 226 ? 0.40303 0.75650 0.43458 0.11258  -0.06614 0.05657  226 THR A CA  
3474 C C   . THR A 226 ? 0.35730 0.66968 0.38556 0.09873  -0.06138 0.05103  226 THR A C   
3475 O O   . THR A 226 ? 0.33789 0.65148 0.37327 0.07994  -0.06163 0.04316  226 THR A O   
3476 C CB  . THR A 226 ? 0.39768 0.75946 0.41834 0.11618  -0.07082 0.06045  226 THR A CB  
3477 O OG1 . THR A 226 ? 0.32959 0.69034 0.35045 0.09515  -0.07309 0.05298  226 THR A OG1 
3478 C CG2 . THR A 226 ? 0.34455 0.75316 0.36863 0.12924  -0.07673 0.06579  226 THR A CG2 
3486 N N   . LEU A 227 ? 0.40745 0.68264 0.42384 0.10826  -0.05679 0.05529  227 LEU A N   
3487 C CA  . LEU A 227 ? 0.43665 0.67523 0.44953 0.09608  -0.05241 0.05050  227 LEU A CA  
3488 C C   . LEU A 227 ? 0.42024 0.65896 0.43075 0.07994  -0.05509 0.04530  227 LEU A C   
3489 O O   . LEU A 227 ? 0.40337 0.63021 0.41810 0.06460  -0.05342 0.03814  227 LEU A O   
3490 C CB  . LEU A 227 ? 0.45894 0.66056 0.45768 0.10802  -0.04748 0.05628  227 LEU A CB  
3491 C CG  . LEU A 227 ? 0.47525 0.64127 0.47185 0.09722  -0.04230 0.05167  227 LEU A CG  
3492 C CD1 . LEU A 227 ? 0.39418 0.56167 0.40373 0.08929  -0.04021 0.04567  227 LEU A CD1 
3493 C CD2 . LEU A 227 ? 0.55284 0.68542 0.53465 0.10883  -0.03751 0.05771  227 LEU A CD2 
3505 N N   . ASN A 228 ? 0.44012 0.69073 0.44258 0.08378  -0.05901 0.04882  228 ASN A N   
3506 C CA  . ASN A 228 ? 0.44625 0.69355 0.44454 0.06888  -0.06088 0.04352  228 ASN A CA  
3507 C C   . ASN A 228 ? 0.43888 0.71220 0.44789 0.05250  -0.06461 0.03541  228 ASN A C   
3508 O O   . ASN A 228 ? 0.36505 0.62561 0.37322 0.03720  -0.06369 0.02831  228 ASN A O   
3509 C CB  . ASN A 228 ? 0.53046 0.78358 0.51625 0.07628  -0.06408 0.04908  228 ASN A CB  
3510 C CG  . ASN A 228 ? 0.66163 0.90268 0.64043 0.06221  -0.06431 0.04380  228 ASN A CG  
3511 O OD1 . ASN A 228 ? 0.65058 0.86025 0.62512 0.05686  -0.05939 0.04150  228 ASN A OD1 
3512 N ND2 . ASN A 228 ? 0.66777 0.93476 0.64536 0.05597  -0.06990 0.04146  228 ASN A ND2 
3519 N N   . ASP A 229 ? 0.37534 0.68539 0.39341 0.05530  -0.06868 0.03631  229 ASP A N   
3520 C CA  . ASP A 229 ? 0.37119 0.70529 0.39850 0.03773  -0.07180 0.02840  229 ASP A CA  
3521 C C   . ASP A 229 ? 0.36646 0.68218 0.40096 0.02664  -0.06730 0.02241  229 ASP A C   
3522 O O   . ASP A 229 ? 0.31623 0.62858 0.35141 0.00909  -0.06757 0.01469  229 ASP A O   
3523 C CB  . ASP A 229 ? 0.33047 0.71120 0.36707 0.04219  -0.07682 0.03060  229 ASP A CB  
3524 C CG  . ASP A 229 ? 0.38413 0.78986 0.41407 0.04869  -0.08269 0.03466  229 ASP A CG  
3525 O OD1 . ASP A 229 ? 0.38880 0.77855 0.40754 0.04395  -0.08345 0.03343  229 ASP A OD1 
3526 O OD2 . ASP A 229 ? 0.41086 0.85534 0.44698 0.05745  -0.08682 0.03852  229 ASP A OD2 
3531 N N   . PHE A 230 ? 0.31412 0.61688 0.35280 0.03681  -0.06299 0.02580  230 PHE A N   
3532 C CA  . PHE A 230 ? 0.36619 0.64966 0.41038 0.02691  -0.05864 0.02052  230 PHE A CA  
3533 C C   . PHE A 230 ? 0.38832 0.63787 0.42453 0.01734  -0.05585 0.01606  230 PHE A C   
3534 O O   . PHE A 230 ? 0.32798 0.56998 0.36640 0.00279  -0.05477 0.00927  230 PHE A O   
3535 C CB  . PHE A 230 ? 0.35484 0.62648 0.40242 0.04010  -0.05427 0.02488  230 PHE A CB  
3536 C CG  . PHE A 230 ? 0.32970 0.57843 0.38108 0.03111  -0.04971 0.02004  230 PHE A CG  
3537 C CD1 . PHE A 230 ? 0.32335 0.58759 0.38455 0.02047  -0.04973 0.01557  230 PHE A CD1 
3538 C CD2 . PHE A 230 ? 0.34906 0.56159 0.39367 0.03273  -0.04536 0.02003  230 PHE A CD2 
3539 C CE1 . PHE A 230 ? 0.32860 0.57071 0.39202 0.01293  -0.04549 0.01164  230 PHE A CE1 
3540 C CE2 . PHE A 230 ? 0.34190 0.53520 0.38985 0.02507  -0.04150 0.01572  230 PHE A CE2 
3541 C CZ  . PHE A 230 ? 0.33844 0.54615 0.39552 0.01604  -0.04161 0.01184  230 PHE A CZ  
3551 N N   . ASN A 231 ? 0.35116 0.57960 0.37731 0.02569  -0.05430 0.01999  231 ASN A N   
3552 C CA  . ASN A 231 ? 0.35695 0.55633 0.37610 0.01738  -0.05140 0.01590  231 ASN A CA  
3553 C C   . ASN A 231 ? 0.40578 0.61299 0.42152 0.00302  -0.05447 0.00942  231 ASN A C   
3554 O O   . ASN A 231 ? 0.42030 0.60968 0.43455 -0.00792 -0.05210 0.00320  231 ASN A O   
3555 C CB  . ASN A 231 ? 0.41448 0.59294 0.42321 0.02860  -0.04901 0.02184  231 ASN A CB  
3556 C CG  . ASN A 231 ? 0.42235 0.58014 0.43239 0.03708  -0.04411 0.02502  231 ASN A CG  
3557 O OD1 . ASN A 231 ? 0.45547 0.60524 0.47239 0.03108  -0.04158 0.02088  231 ASN A OD1 
3558 N ND2 . ASN A 231 ? 0.46271 0.61192 0.46531 0.05095  -0.04275 0.03230  231 ASN A ND2 
3565 N N   . LEU A 232 ? 0.39343 0.62792 0.40769 0.00266  -0.05974 0.01033  232 LEU A N   
3566 C CA  . LEU A 232 ? 0.39421 0.63667 0.40432 -0.01230 -0.06273 0.00328  232 LEU A CA  
3567 C C   . LEU A 232 ? 0.39729 0.64294 0.41407 -0.02720 -0.06221 -0.00405 232 LEU A C   
3568 O O   . LEU A 232 ? 0.35361 0.58495 0.36479 -0.04010 -0.06120 -0.01113 232 LEU A O   
3569 C CB  . LEU A 232 ? 0.40226 0.67700 0.40997 -0.01013 -0.06892 0.00565  232 LEU A CB  
3570 C CG  . LEU A 232 ? 0.42351 0.69223 0.42073 0.00267  -0.06952 0.01244  232 LEU A CG  
3571 C CD1 . LEU A 232 ? 0.40385 0.70820 0.40009 0.00678  -0.07595 0.01566  232 LEU A CD1 
3572 C CD2 . LEU A 232 ? 0.48271 0.72655 0.46898 -0.00549 -0.06734 0.00777  232 LEU A CD2 
3584 N N   . VAL A 233 ? 0.35094 0.61486 0.37854 -0.02552 -0.06262 -0.00240 233 VAL A N   
3585 C CA  . VAL A 233 ? 0.32701 0.59221 0.36003 -0.04005 -0.06148 -0.00872 233 VAL A CA  
3586 C C   . VAL A 233 ? 0.33553 0.56558 0.36749 -0.04149 -0.05569 -0.01089 233 VAL A C   
3587 O O   . VAL A 233 ? 0.38006 0.59550 0.40834 -0.05468 -0.05405 -0.01746 233 VAL A O   
3588 C CB  . VAL A 233 ? 0.35852 0.65471 0.40374 -0.03752 -0.06301 -0.00599 233 VAL A CB  
3589 C CG1 . VAL A 233 ? 0.48289 0.77686 0.53267 -0.05318 -0.06088 -0.01204 233 VAL A CG1 
3590 C CG2 . VAL A 233 ? 0.31894 0.65295 0.36566 -0.03688 -0.06896 -0.00437 233 VAL A CG2 
3600 N N   . ALA A 234 ? 0.38057 0.59591 0.41463 -0.02786 -0.05245 -0.00545 234 ALA A N   
3601 C CA  . ALA A 234 ? 0.43478 0.62171 0.46957 -0.02904 -0.04729 -0.00731 234 ALA A CA  
3602 C C   . ALA A 234 ? 0.42114 0.58263 0.44647 -0.03602 -0.04537 -0.01222 234 ALA A C   
3603 O O   . ALA A 234 ? 0.41359 0.55856 0.43810 -0.04406 -0.04261 -0.01693 234 ALA A O   
3604 C CB  . ALA A 234 ? 0.44753 0.62307 0.48459 -0.01394 -0.04428 -0.00104 234 ALA A CB  
3610 N N   . MET A 235 ? 0.46030 0.61858 0.47772 -0.03227 -0.04658 -0.01094 235 MET A N   
3611 C CA  . MET A 235 ? 0.51203 0.64929 0.52000 -0.03794 -0.04471 -0.01564 235 MET A CA  
3612 C C   . MET A 235 ? 0.49975 0.63587 0.50377 -0.05291 -0.04546 -0.02359 235 MET A C   
3613 O O   . MET A 235 ? 0.45034 0.56384 0.44828 -0.05747 -0.04230 -0.02823 235 MET A O   
3614 C CB  . MET A 235 ? 0.55458 0.69514 0.55425 -0.03309 -0.04661 -0.01315 235 MET A CB  
3615 C CG  . MET A 235 ? 0.77906 0.91745 0.77891 -0.01866 -0.04560 -0.00491 235 MET A CG  
3616 S SD  . MET A 235 ? 1.10156 1.21101 1.10296 -0.01256 -0.03932 -0.00296 235 MET A SD  
3617 C CE  . MET A 235 ? 0.86331 0.95250 0.85605 -0.02021 -0.03647 -0.00917 235 MET A CE  
3627 N N   . LYS A 236 ? 0.40271 0.56270 0.40906 -0.06073 -0.04942 -0.02534 236 LYS A N   
3628 C CA  . LYS A 236 ? 0.39762 0.55472 0.39767 -0.07674 -0.04998 -0.03328 236 LYS A CA  
3629 C C   . LYS A 236 ? 0.43555 0.57607 0.43790 -0.08286 -0.04617 -0.03616 236 LYS A C   
3630 O O   . LYS A 236 ? 0.44398 0.57308 0.43834 -0.09569 -0.04527 -0.04278 236 LYS A O   
3631 C CB  . LYS A 236 ? 0.41697 0.60647 0.41902 -0.08499 -0.05528 -0.03450 236 LYS A CB  
3632 C CG  . LYS A 236 ? 0.44073 0.64739 0.43902 -0.07839 -0.05945 -0.03142 236 LYS A CG  
3633 C CD  . LYS A 236 ? 0.48631 0.72748 0.48526 -0.08741 -0.06533 -0.03340 236 LYS A CD  
3634 C CE  . LYS A 236 ? 0.45040 0.70844 0.44610 -0.07726 -0.06931 -0.02854 236 LYS A CE  
3635 N NZ  . LYS A 236 ? 0.51652 0.81366 0.51406 -0.08274 -0.07575 -0.02895 236 LYS A NZ  
3649 N N   . TYR A 237 ? 0.34822 0.48780 0.36027 -0.07444 -0.04400 -0.03132 237 TYR A N   
3650 C CA  . TYR A 237 ? 0.39974 0.52239 0.41353 -0.07847 -0.04014 -0.03318 237 TYR A CA  
3651 C C   . TYR A 237 ? 0.43359 0.52994 0.44601 -0.06911 -0.03592 -0.03167 237 TYR A C   
3652 O O   . TYR A 237 ? 0.39824 0.48314 0.41410 -0.06837 -0.03286 -0.03126 237 TYR A O   
3653 C CB  . TYR A 237 ? 0.38632 0.52849 0.41182 -0.07732 -0.04054 -0.02960 237 TYR A CB  
3654 C CG  . TYR A 237 ? 0.38129 0.55282 0.40948 -0.08811 -0.04437 -0.03143 237 TYR A CG  
3655 C CD1 . TYR A 237 ? 0.40613 0.60696 0.43872 -0.08294 -0.04881 -0.02811 237 TYR A CD1 
3656 C CD2 . TYR A 237 ? 0.39020 0.56032 0.41567 -0.10384 -0.04344 -0.03641 237 TYR A CD2 
3657 C CE1 . TYR A 237 ? 0.42769 0.66062 0.46394 -0.09326 -0.05266 -0.02986 237 TYR A CE1 
3658 C CE2 . TYR A 237 ? 0.42116 0.62037 0.44955 -0.11558 -0.04671 -0.03833 237 TYR A CE2 
3659 C CZ  . TYR A 237 ? 0.42502 0.65753 0.45957 -0.11042 -0.05151 -0.03524 237 TYR A CZ  
3660 O OH  . TYR A 237 ? 0.45032 0.71506 0.48826 -0.12274 -0.05496 -0.03746 237 TYR A OH  
3670 N N   . ASN A 238 ? 0.40843 0.49667 0.41572 -0.06240 -0.03571 -0.03079 238 ASN A N   
3671 C CA  . ASN A 238 ? 0.42156 0.48855 0.42776 -0.05398 -0.03184 -0.02935 238 ASN A CA  
3672 C C   . ASN A 238 ? 0.41421 0.48325 0.43007 -0.04453 -0.03037 -0.02364 238 ASN A C   
3673 O O   . ASN A 238 ? 0.40381 0.45684 0.42106 -0.04116 -0.02694 -0.02345 238 ASN A O   
3674 C CB  . ASN A 238 ? 0.48522 0.52914 0.48471 -0.05928 -0.02847 -0.03465 238 ASN A CB  
3675 C CG  . ASN A 238 ? 0.61190 0.64519 0.59966 -0.06222 -0.02812 -0.03933 238 ASN A CG  
3676 O OD1 . ASN A 238 ? 0.61068 0.65557 0.59502 -0.06295 -0.03088 -0.03932 238 ASN A OD1 
3677 N ND2 . ASN A 238 ? 0.68652 0.69799 0.66737 -0.06289 -0.02460 -0.04322 238 ASN A ND2 
3684 N N   . TYR A 239 ? 0.32582 0.41461 0.34729 -0.03933 -0.03295 -0.01896 239 TYR A N   
3685 C CA  . TYR A 239 ? 0.32477 0.41494 0.35304 -0.02890 -0.03155 -0.01339 239 TYR A CA  
3686 C C   . TYR A 239 ? 0.34673 0.43003 0.37058 -0.01976 -0.03090 -0.00940 239 TYR A C   
3687 O O   . TYR A 239 ? 0.37077 0.45976 0.38882 -0.01994 -0.03308 -0.00909 239 TYR A O   
3688 C CB  . TYR A 239 ? 0.34596 0.46139 0.38174 -0.02674 -0.03424 -0.01026 239 TYR A CB  
3689 C CG  . TYR A 239 ? 0.29923 0.41879 0.34172 -0.03199 -0.03300 -0.01189 239 TYR A CG  
3690 C CD1 . TYR A 239 ? 0.35197 0.46615 0.39187 -0.04452 -0.03257 -0.01730 239 TYR A CD1 
3691 C CD2 . TYR A 239 ? 0.31180 0.43994 0.36185 -0.02419 -0.03198 -0.00787 239 TYR A CD2 
3692 C CE1 . TYR A 239 ? 0.35467 0.47124 0.39935 -0.04980 -0.03103 -0.01831 239 TYR A CE1 
3693 C CE2 . TYR A 239 ? 0.29180 0.42373 0.34762 -0.02902 -0.03039 -0.00919 239 TYR A CE2 
3694 C CZ  . TYR A 239 ? 0.28825 0.41475 0.34135 -0.04223 -0.03000 -0.01422 239 TYR A CZ  
3695 O OH  . TYR A 239 ? 0.32399 0.45338 0.38152 -0.04762 -0.02813 -0.01509 239 TYR A OH  
3705 N N   . GLU A 240 ? 0.33356 0.40383 0.35906 -0.01269 -0.02770 -0.00653 240 GLU A N   
3706 C CA  . GLU A 240 ? 0.37865 0.44081 0.39912 -0.00468 -0.02643 -0.00217 240 GLU A CA  
3707 C C   . GLU A 240 ? 0.41116 0.48863 0.43071 0.00315  -0.02915 0.00340  240 GLU A C   
3708 O O   . GLU A 240 ? 0.32343 0.41681 0.34901 0.00578  -0.03095 0.00499  240 GLU A O   
3709 C CB  . GLU A 240 ? 0.38193 0.42839 0.40415 0.00007  -0.02252 -0.00050 240 GLU A CB  
3710 C CG  . GLU A 240 ? 0.42480 0.45603 0.44584 -0.00489 -0.01971 -0.00462 240 GLU A CG  
3711 C CD  . GLU A 240 ? 0.48414 0.50828 0.49745 -0.00570 -0.01880 -0.00492 240 GLU A CD  
3712 O OE1 . GLU A 240 ? 0.51223 0.53009 0.52138 -0.00076 -0.01720 -0.00088 240 GLU A OE1 
3713 O OE2 . GLU A 240 ? 0.48161 0.50568 0.49192 -0.01137 -0.01937 -0.00920 240 GLU A OE2 
3720 N N   . PRO A 241 ? 0.39527 0.46862 0.40689 0.00785  -0.02925 0.00687  241 PRO A N   
3721 C CA  . PRO A 241 ? 0.42030 0.50606 0.42937 0.01755  -0.03156 0.01315  241 PRO A CA  
3722 C C   . PRO A 241 ? 0.42741 0.50701 0.43864 0.02733  -0.02915 0.01752  241 PRO A C   
3723 O O   . PRO A 241 ? 0.40750 0.46749 0.41790 0.02754  -0.02515 0.01703  241 PRO A O   
3724 C CB  . PRO A 241 ? 0.48763 0.56401 0.48556 0.01968  -0.03103 0.01590  241 PRO A CB  
3725 C CG  . PRO A 241 ? 0.47061 0.53916 0.46709 0.00895  -0.03000 0.00951  241 PRO A CG  
3726 C CD  . PRO A 241 ? 0.49883 0.55804 0.50268 0.00466  -0.02735 0.00539  241 PRO A CD  
3734 N N   . LEU A 242 ? 0.37647 0.47417 0.39015 0.03562  -0.03162 0.02154  242 LEU A N   
3735 C CA  . LEU A 242 ? 0.35494 0.44843 0.36873 0.04742  -0.02948 0.02621  242 LEU A CA  
3736 C C   . LEU A 242 ? 0.47100 0.55551 0.47252 0.05866  -0.02901 0.03315  242 LEU A C   
3737 O O   . LEU A 242 ? 0.40751 0.50755 0.40543 0.06185  -0.03267 0.03601  242 LEU A O   
3738 C CB  . LEU A 242 ? 0.42565 0.54644 0.44895 0.05114  -0.03219 0.02673  242 LEU A CB  
3739 C CG  . LEU A 242 ? 0.39698 0.51381 0.42206 0.06226  -0.02930 0.02985  242 LEU A CG  
3740 C CD1 . LEU A 242 ? 0.36641 0.46716 0.39645 0.05487  -0.02558 0.02503  242 LEU A CD1 
3741 C CD2 . LEU A 242 ? 0.37848 0.52748 0.41107 0.06919  -0.03241 0.03208  242 LEU A CD2 
3753 N N   . THR A 243 ? 0.40919 0.46798 0.40310 0.06386  -0.02447 0.03574  243 THR A N   
3754 C CA  . THR A 243 ? 0.43720 0.48018 0.41654 0.07352  -0.02277 0.04246  243 THR A CA  
3755 C C   . THR A 243 ? 0.42082 0.46328 0.39659 0.08908  -0.02171 0.04798  243 THR A C   
3756 O O   . THR A 243 ? 0.42810 0.47969 0.41296 0.09162  -0.02143 0.04608  243 THR A O   
3757 C CB  . THR A 243 ? 0.46019 0.47292 0.43130 0.06763  -0.01783 0.04144  243 THR A CB  
3758 O OG1 . THR A 243 ? 0.41908 0.41928 0.39388 0.06776  -0.01436 0.03913  243 THR A OG1 
3759 C CG2 . THR A 243 ? 0.47333 0.48736 0.44835 0.05350  -0.01835 0.03565  243 THR A CG2 
3767 N N   . GLN A 244 ? 0.42886 0.45938 0.39000 0.10026  -0.02073 0.05509  244 GLN A N   
3768 C CA  . GLN A 244 ? 0.47064 0.49537 0.42544 0.11684  -0.01880 0.06053  244 GLN A CA  
3769 C C   . GLN A 244 ? 0.50859 0.50606 0.46050 0.11573  -0.01317 0.05817  244 GLN A C   
3770 O O   . GLN A 244 ? 0.49321 0.49040 0.44519 0.12664  -0.01156 0.05963  244 GLN A O   
3771 C CB  . GLN A 244 ? 0.50039 0.51352 0.43712 0.13001  -0.01839 0.06921  244 GLN A CB  
3772 C CG  . GLN A 244 ? 0.56917 0.57408 0.49681 0.14950  -0.01605 0.07525  244 GLN A CG  
3773 C CD  . GLN A 244 ? 0.59720 0.63992 0.53782 0.15970  -0.02035 0.07592  244 GLN A CD  
3774 O OE1 . GLN A 244 ? 0.60791 0.68298 0.55804 0.15625  -0.02595 0.07523  244 GLN A OE1 
3775 N NE2 . GLN A 244 ? 0.57671 0.61656 0.51791 0.17119  -0.01757 0.07666  244 GLN A NE2 
3784 N N   . ASP A 245 ? 0.46843 0.44362 0.41701 0.10317  -0.01002 0.05454  245 ASP A N   
3785 C CA  . ASP A 245 ? 0.52860 0.48216 0.47626 0.09989  -0.00531 0.05110  245 ASP A CA  
3786 C C   . ASP A 245 ? 0.45018 0.42287 0.41434 0.09793  -0.00665 0.04599  245 ASP A C   
3787 O O   . ASP A 245 ? 0.47348 0.43760 0.43634 0.10449  -0.00381 0.04577  245 ASP A O   
3788 C CB  . ASP A 245 ? 0.54490 0.48020 0.49021 0.08474  -0.00264 0.04697  245 ASP A CB  
3789 C CG  . ASP A 245 ? 0.72222 0.62739 0.64787 0.08585  0.00157  0.05154  245 ASP A CG  
3790 O OD1 . ASP A 245 ? 0.68478 0.58127 0.59698 0.09875  0.00220  0.05848  245 ASP A OD1 
3791 O OD2 . ASP A 245 ? 0.77392 0.66451 0.69719 0.07352  0.00441  0.04822  245 ASP A OD2 
3796 N N   . HIS A 246 ? 0.41283 0.40949 0.39098 0.08843  -0.01056 0.04177  246 HIS A N   
3797 C CA  . HIS A 246 ? 0.40921 0.42427 0.40247 0.08462  -0.01175 0.03700  246 HIS A CA  
3798 C C   . HIS A 246 ? 0.40706 0.44058 0.40302 0.09866  -0.01293 0.04069  246 HIS A C   
3799 O O   . HIS A 246 ? 0.41519 0.45044 0.41629 0.10156  -0.01100 0.03889  246 HIS A O   
3800 C CB  . HIS A 246 ? 0.38959 0.42460 0.39384 0.07201  -0.01564 0.03247  246 HIS A CB  
3801 C CG  . HIS A 246 ? 0.43932 0.45907 0.44245 0.05937  -0.01423 0.02820  246 HIS A CG  
3802 N ND1 . HIS A 246 ? 0.38923 0.41815 0.39475 0.05036  -0.01697 0.02564  246 HIS A ND1 
3803 C CD2 . HIS A 246 ? 0.41258 0.41036 0.41240 0.05451  -0.01038 0.02582  246 HIS A CD2 
3804 C CE1 . HIS A 246 ? 0.45198 0.46538 0.45586 0.04172  -0.01465 0.02217  246 HIS A CE1 
3805 N NE2 . HIS A 246 ? 0.38782 0.38346 0.38882 0.04373  -0.01080 0.02226  246 HIS A NE2 
3813 N N   . VAL A 247 ? 0.39957 0.44797 0.39201 0.10721  -0.01604 0.04571  247 VAL A N   
3814 C CA  . VAL A 247 ? 0.42406 0.49296 0.41887 0.12228  -0.01721 0.04971  247 VAL A CA  
3815 C C   . VAL A 247 ? 0.49770 0.54275 0.48191 0.13549  -0.01205 0.05252  247 VAL A C   
3816 O O   . VAL A 247 ? 0.45187 0.50869 0.44189 0.14344  -0.01096 0.05216  247 VAL A O   
3817 C CB  . VAL A 247 ? 0.44997 0.53701 0.44027 0.13082  -0.02139 0.05542  247 VAL A CB  
3818 C CG1 . VAL A 247 ? 0.46950 0.57425 0.45929 0.14988  -0.02181 0.06069  247 VAL A CG1 
3819 C CG2 . VAL A 247 ? 0.38167 0.49719 0.38428 0.11706  -0.02663 0.05122  247 VAL A CG2 
3829 N N   . ASP A 248 ? 0.47082 0.48199 0.43808 0.13817  -0.00855 0.05542  248 ASP A N   
3830 C CA  . ASP A 248 ? 0.51235 0.49476 0.46618 0.14906  -0.00302 0.05743  248 ASP A CA  
3831 C C   . ASP A 248 ? 0.50954 0.48564 0.47110 0.14123  -0.00017 0.05091  248 ASP A C   
3832 O O   . ASP A 248 ? 0.52382 0.49632 0.48315 0.15184  0.00272  0.05114  248 ASP A O   
3833 C CB  . ASP A 248 ? 0.60263 0.54734 0.53620 0.14830  0.00057  0.06065  248 ASP A CB  
3834 C CG  . ASP A 248 ? 0.66709 0.61269 0.58833 0.15992  -0.00127 0.06867  248 ASP A CG  
3835 O OD1 . ASP A 248 ? 0.65370 0.62421 0.57820 0.17419  -0.00433 0.07289  248 ASP A OD1 
3836 O OD2 . ASP A 248 ? 0.65955 0.58123 0.56706 0.15497  0.00052  0.07102  248 ASP A OD2 
3841 N N   . ILE A 249 ? 0.45386 0.42893 0.42392 0.12348  -0.00084 0.04510  249 ILE A N   
3842 C CA  . ILE A 249 ? 0.49970 0.46738 0.47573 0.11554  0.00174  0.03919  249 ILE A CA  
3843 C C   . ILE A 249 ? 0.47425 0.46967 0.46420 0.11975  0.00036  0.03750  249 ILE A C   
3844 O O   . ILE A 249 ? 0.47912 0.46789 0.47003 0.12111  0.00344  0.03470  249 ILE A O   
3845 C CB  . ILE A 249 ? 0.49917 0.46368 0.48170 0.09718  0.00081  0.03392  249 ILE A CB  
3846 C CG1 . ILE A 249 ? 0.54872 0.48525 0.51682 0.09280  0.00324  0.03537  249 ILE A CG1 
3847 C CG2 . ILE A 249 ? 0.57869 0.53964 0.56819 0.08992  0.00285  0.02819  249 ILE A CG2 
3848 C CD1 . ILE A 249 ? 0.52675 0.46486 0.50073 0.07710  0.00189  0.03132  249 ILE A CD1 
3860 N N   . LEU A 250 ? 0.45478 0.48235 0.45528 0.12087  -0.00417 0.03894  250 LEU A N   
3861 C CA  . LEU A 250 ? 0.44275 0.50011 0.45658 0.12392  -0.00540 0.03766  250 LEU A CA  
3862 C C   . LEU A 250 ? 0.40230 0.46607 0.41087 0.14411  -0.00360 0.04243  250 LEU A C   
3863 O O   . LEU A 250 ? 0.45747 0.54715 0.47663 0.14816  -0.00392 0.04163  250 LEU A O   
3864 C CB  . LEU A 250 ? 0.34653 0.43668 0.37328 0.11487  -0.01086 0.03661  250 LEU A CB  
3865 C CG  . LEU A 250 ? 0.37511 0.46095 0.40822 0.09527  -0.01214 0.03086  250 LEU A CG  
3866 C CD1 . LEU A 250 ? 0.40947 0.51745 0.44805 0.08746  -0.01724 0.03058  250 LEU A CD1 
3867 C CD2 . LEU A 250 ? 0.36053 0.45062 0.40358 0.08623  -0.01057 0.02568  250 LEU A CD2 
3879 N N   . GLY A 251 ? 0.44590 0.48645 0.43759 0.15729  -0.00128 0.04743  251 GLY A N   
3880 C CA  . GLY A 251 ? 0.46805 0.51307 0.45266 0.17875  0.00064  0.05242  251 GLY A CA  
3881 C C   . GLY A 251 ? 0.48630 0.53468 0.47517 0.18433  0.00434  0.04943  251 GLY A C   
3882 O O   . GLY A 251 ? 0.49811 0.57576 0.49464 0.19581  0.00370  0.05116  251 GLY A O   
3886 N N   . PRO A 252 ? 0.52191 0.54123 0.50532 0.17654  0.00840  0.04487  252 PRO A N   
3887 C CA  . PRO A 252 ? 0.50390 0.52519 0.49082 0.18024  0.01208  0.04133  252 PRO A CA  
3888 C C   . PRO A 252 ? 0.48091 0.54305 0.48878 0.17415  0.00941  0.03862  252 PRO A C   
3889 O O   . PRO A 252 ? 0.50246 0.58422 0.51436 0.18636  0.01100  0.03958  252 PRO A O   
3890 C CB  . PRO A 252 ? 0.56132 0.54821 0.54119 0.16666  0.01521  0.03611  252 PRO A CB  
3891 C CG  . PRO A 252 ? 0.63533 0.59299 0.59969 0.16554  0.01563  0.03898  252 PRO A CG  
3892 C CD  . PRO A 252 ? 0.54475 0.52609 0.51518 0.16676  0.01046  0.04351  252 PRO A CD  
3900 N N   . LEU A 253 ? 0.44194 0.51599 0.46216 0.15527  0.00590  0.03509  253 LEU A N   
3901 C CA  . LEU A 253 ? 0.44719 0.55737 0.48529 0.14751  0.00362  0.03265  253 LEU A CA  
3902 C C   . LEU A 253 ? 0.43331 0.58112 0.47876 0.15755  0.00038  0.03692  253 LEU A C   
3903 O O   . LEU A 253 ? 0.36787 0.54629 0.42413 0.16058  0.00061  0.03649  253 LEU A O   
3904 C CB  . LEU A 253 ? 0.35967 0.47085 0.40597 0.12639  0.00058  0.02859  253 LEU A CB  
3905 C CG  . LEU A 253 ? 0.39896 0.48227 0.44194 0.11523  0.00331  0.02381  253 LEU A CG  
3906 C CD1 . LEU A 253 ? 0.32467 0.40858 0.37379 0.09728  0.00009  0.02076  253 LEU A CD1 
3907 C CD2 . LEU A 253 ? 0.34836 0.44075 0.39743 0.11557  0.00631  0.02102  253 LEU A CD2 
3919 N N   . SER A 254 ? 0.38376 0.53108 0.42302 0.16309  -0.00257 0.04125  254 SER A N   
3920 C CA  . SER A 254 ? 0.41337 0.59609 0.45753 0.17512  -0.00584 0.04598  254 SER A CA  
3921 C C   . SER A 254 ? 0.49773 0.68857 0.53790 0.19738  -0.00225 0.04939  254 SER A C   
3922 O O   . SER A 254 ? 0.45427 0.68569 0.50518 0.20487  -0.00402 0.05120  254 SER A O   
3923 C CB  . SER A 254 ? 0.41688 0.58915 0.45085 0.17878  -0.00886 0.05044  254 SER A CB  
3924 O OG  . SER A 254 ? 0.51754 0.72165 0.55398 0.19278  -0.01187 0.05557  254 SER A OG  
3930 N N   . ALA A 255 ? 0.47023 0.62351 0.49401 0.20875  0.00291  0.05037  255 ALA A N   
3931 C CA  . ALA A 255 ? 0.53464 0.69120 0.55184 0.23149  0.00696  0.05340  255 ALA A CA  
3932 C C   . ALA A 255 ? 0.46129 0.63570 0.48996 0.22844  0.00983  0.04881  255 ALA A C   
3933 O O   . ALA A 255 ? 0.49659 0.69395 0.52717 0.23645  0.01109  0.04955  255 ALA A O   
3934 C CB  . ALA A 255 ? 0.49803 0.60409 0.49077 0.24092  0.01205  0.05485  255 ALA A CB  
3940 N N   . GLN A 256 ? 0.48909 0.64829 0.52177 0.21039  0.01104  0.04298  256 GLN A N   
3941 C CA  . GLN A 256 ? 0.51116 0.68285 0.55266 0.20684  0.01418  0.03874  256 GLN A CA  
3942 C C   . GLN A 256 ? 0.51286 0.73564 0.57443 0.20063  0.01090  0.03853  256 GLN A C   
3943 O O   . GLN A 256 ? 0.42591 0.67132 0.49458 0.20611  0.01372  0.03752  256 GLN A O   
3944 C CB  . GLN A 256 ? 0.51661 0.66016 0.55706 0.18780  0.01557  0.03291  256 GLN A CB  
3945 C CG  . GLN A 256 ? 0.55247 0.70691 0.60063 0.18353  0.01887  0.02872  256 GLN A CG  
3946 C CD  . GLN A 256 ? 0.60967 0.73816 0.65633 0.16601  0.01994  0.02341  256 GLN A CD  
3947 O OE1 . GLN A 256 ? 0.69194 0.78870 0.72905 0.15972  0.01944  0.02249  256 GLN A OE1 
3948 N NE2 . GLN A 256 ? 0.60859 0.75268 0.66502 0.15749  0.02128  0.02010  256 GLN A NE2 
3957 N N   . THR A 257 ? 0.41324 0.65564 0.48314 0.18968  0.00519  0.03954  257 THR A N   
3958 C CA  . THR A 257 ? 0.40610 0.69498 0.49403 0.17955  0.00194  0.03853  257 THR A CA  
3959 C C   . THR A 257 ? 0.38403 0.70965 0.47589 0.19217  -0.00140 0.04342  257 THR A C   
3960 O O   . THR A 257 ? 0.43460 0.79853 0.53825 0.18437  -0.00307 0.04234  257 THR A O   
3961 C CB  . THR A 257 ? 0.41199 0.69881 0.50638 0.15474  -0.00214 0.03492  257 THR A CB  
3962 O OG1 . THR A 257 ? 0.35109 0.62278 0.43768 0.15494  -0.00575 0.03729  257 THR A OG1 
3963 C CG2 . THR A 257 ? 0.38886 0.64555 0.48079 0.14116  0.00074  0.03008  257 THR A CG2 
3971 N N   . GLY A 258 ? 0.42802 0.73459 0.50518 0.20606  -0.00186 0.04780  258 GLY A N   
3972 C CA  . GLY A 258 ? 0.42840 0.76037 0.50385 0.21311  -0.00495 0.05167  258 GLY A CA  
3973 C C   . GLY A 258 ? 0.39278 0.74868 0.47749 0.20013  -0.01167 0.05191  258 GLY A C   
3974 O O   . GLY A 258 ? 0.37908 0.76168 0.46405 0.20378  -0.01451 0.05445  258 GLY A O   
3978 N N   . ILE A 259 ? 0.38371 0.73152 0.47531 0.18510  -0.01424 0.04912  259 ILE A N   
3979 C CA  . ILE A 259 ? 0.35117 0.71600 0.44894 0.16938  -0.02038 0.04807  259 ILE A CA  
3980 C C   . ILE A 259 ? 0.40769 0.73665 0.49075 0.17139  -0.02171 0.05041  259 ILE A C   
3981 O O   . ILE A 259 ? 0.32974 0.61815 0.40476 0.16374  -0.01898 0.04778  259 ILE A O   
3982 C CB  . ILE A 259 ? 0.32869 0.69575 0.43654 0.14343  -0.02073 0.04129  259 ILE A CB  
3983 C CG1 . ILE A 259 ? 0.40083 0.80731 0.52283 0.14095  -0.01943 0.03968  259 ILE A CG1 
3984 C CG2 . ILE A 259 ? 0.31531 0.69089 0.42559 0.12617  -0.02646 0.03934  259 ILE A CG2 
3985 C CD1 . ILE A 259 ? 0.31379 0.71473 0.44264 0.11755  -0.01789 0.03347  259 ILE A CD1 
3997 N N   . ALA A 260 ? 0.36432 0.70949 0.44376 0.18118  -0.02590 0.05538  260 ALA A N   
3998 C CA  . ALA A 260 ? 0.36343 0.67671 0.42825 0.18298  -0.02711 0.05816  260 ALA A CA  
3999 C C   . ALA A 260 ? 0.37560 0.67219 0.44225 0.15888  -0.02883 0.05253  260 ALA A C   
4000 O O   . ALA A 260 ? 0.34457 0.66416 0.42375 0.14156  -0.03131 0.04765  260 ALA A O   
4001 C CB  . ALA A 260 ? 0.43219 0.77120 0.49387 0.19424  -0.03192 0.06389  260 ALA A CB  
4007 N N   . VAL A 261 ? 0.34596 0.60148 0.39888 0.15784  -0.02718 0.05326  261 VAL A N   
4008 C CA  . VAL A 261 ? 0.36907 0.60612 0.42243 0.13705  -0.02809 0.04803  261 VAL A CA  
4009 C C   . VAL A 261 ? 0.32860 0.59495 0.38919 0.12463  -0.03415 0.04627  261 VAL A C   
4010 O O   . VAL A 261 ? 0.29318 0.56419 0.36160 0.10568  -0.03529 0.04025  261 VAL A O   
4011 C CB  . VAL A 261 ? 0.39988 0.59293 0.43699 0.13966  -0.02534 0.04990  261 VAL A CB  
4012 C CG1 . VAL A 261 ? 0.37418 0.55343 0.41215 0.11996  -0.02660 0.04488  261 VAL A CG1 
4013 C CG2 . VAL A 261 ? 0.40422 0.56657 0.43514 0.14573  -0.01907 0.04915  261 VAL A CG2 
4023 N N   . LEU A 262 ? 0.30234 0.58721 0.35892 0.13503  -0.03801 0.05140  262 LEU A N   
4024 C CA  . LEU A 262 ? 0.33324 0.64516 0.39504 0.12269  -0.04393 0.04934  262 LEU A CA  
4025 C C   . LEU A 262 ? 0.32309 0.67891 0.40100 0.11416  -0.04660 0.04589  262 LEU A C   
4026 O O   . LEU A 262 ? 0.30458 0.67887 0.38793 0.09733  -0.05058 0.04150  262 LEU A O   
4027 C CB  . LEU A 262 ? 0.36467 0.68490 0.41673 0.13661  -0.04750 0.05611  262 LEU A CB  
4028 C CG  . LEU A 262 ? 0.40015 0.67848 0.43575 0.13866  -0.04549 0.05859  262 LEU A CG  
4029 C CD1 . LEU A 262 ? 0.42884 0.71447 0.45300 0.15607  -0.04826 0.06681  262 LEU A CD1 
4030 C CD2 . LEU A 262 ? 0.39362 0.65911 0.42954 0.11707  -0.04674 0.05226  262 LEU A CD2 
4042 N N   . ASP A 263 ? 0.29798 0.66860 0.38262 0.12420  -0.04395 0.04730  263 ASP A N   
4043 C CA  . ASP A 263 ? 0.27194 0.68341 0.37222 0.11422  -0.04544 0.04370  263 ASP A CA  
4044 C C   . ASP A 263 ? 0.31516 0.70744 0.41941 0.09221  -0.04301 0.03637  263 ASP A C   
4045 O O   . ASP A 263 ? 0.25777 0.67015 0.36909 0.07362  -0.04585 0.03159  263 ASP A O   
4046 C CB  . ASP A 263 ? 0.32844 0.75946 0.43347 0.13300  -0.04265 0.04767  263 ASP A CB  
4047 C CG  . ASP A 263 ? 0.42992 0.90104 0.54666 0.12498  -0.04256 0.04485  263 ASP A CG  
4048 O OD1 . ASP A 263 ? 0.50409 0.98825 0.63029 0.10384  -0.04402 0.03925  263 ASP A OD1 
4049 O OD2 . ASP A 263 ? 0.60030 1.08523 0.71425 0.13928  -0.04018 0.04808  263 ASP A OD2 
4054 N N   . MET A 264 ? 0.27962 0.63275 0.37796 0.09436  -0.03787 0.03558  264 MET A N   
4055 C CA  . MET A 264 ? 0.23951 0.57226 0.34000 0.07528  -0.03564 0.02926  264 MET A CA  
4056 C C   . MET A 264 ? 0.27769 0.59866 0.37377 0.05924  -0.03875 0.02556  264 MET A C   
4057 O O   . MET A 264 ? 0.28312 0.60338 0.38295 0.04093  -0.03882 0.02000  264 MET A O   
4058 C CB  . MET A 264 ? 0.23198 0.52538 0.32596 0.08099  -0.03004 0.02917  264 MET A CB  
4059 C CG  . MET A 264 ? 0.25793 0.53589 0.35542 0.06387  -0.02749 0.02330  264 MET A CG  
4060 S SD  . MET A 264 ? 0.26847 0.58324 0.37985 0.05821  -0.02634 0.02151  264 MET A SD  
4061 C CE  . MET A 264 ? 0.28227 0.58379 0.39139 0.07701  -0.02064 0.02443  264 MET A CE  
4071 N N   . CYS A 265 ? 0.28287 0.59141 0.36935 0.06596  -0.04083 0.02853  265 CYS A N   
4072 C CA  . CYS A 265 ? 0.25410 0.55501 0.33618 0.05141  -0.04382 0.02484  265 CYS A CA  
4073 C C   . CYS A 265 ? 0.32180 0.65934 0.41138 0.03789  -0.04848 0.02142  265 CYS A C   
4074 O O   . CYS A 265 ? 0.25949 0.59025 0.34792 0.01995  -0.04943 0.01562  265 CYS A O   
4075 C CB  . CYS A 265 ? 0.28138 0.56862 0.35192 0.06150  -0.04546 0.02924  265 CYS A CB  
4076 S SG  . CYS A 265 ? 0.32780 0.56634 0.38737 0.06966  -0.03973 0.03120  265 CYS A SG  
4082 N N   . ALA A 266 ? 0.28227 0.65912 0.37849 0.04633  -0.05145 0.02487  266 ALA A N   
4083 C CA  . ALA A 266 ? 0.27205 0.68663 0.37551 0.03183  -0.05598 0.02124  266 ALA A CA  
4084 C C   . ALA A 266 ? 0.30050 0.71998 0.41188 0.01452  -0.05357 0.01557  266 ALA A C   
4085 O O   . ALA A 266 ? 0.28041 0.70977 0.39260 -0.00502 -0.05582 0.01004  266 ALA A O   
4086 C CB  . ALA A 266 ? 0.32644 0.78609 0.43605 0.04531  -0.05979 0.02637  266 ALA A CB  
4092 N N   . SER A 267 ? 0.25337 0.66382 0.36900 0.02081  -0.04873 0.01673  267 SER A N   
4093 C CA  . SER A 267 ? 0.29463 0.70368 0.41562 0.00454  -0.04577 0.01182  267 SER A CA  
4094 C C   . SER A 267 ? 0.27592 0.64583 0.38850 -0.01059 -0.04412 0.00661  267 SER A C   
4095 O O   . SER A 267 ? 0.23925 0.61114 0.35249 -0.02960 -0.04402 0.00144  267 SER A O   
4096 C CB  . SER A 267 ? 0.39778 0.80586 0.52413 0.01659  -0.04091 0.01463  267 SER A CB  
4097 O OG  . SER A 267 ? 0.41705 0.80132 0.54272 0.00440  -0.03687 0.01068  267 SER A OG  
4103 N N   . LEU A 268 ? 0.27307 0.60722 0.37683 -0.00256 -0.04261 0.00789  268 LEU A N   
4104 C CA  . LEU A 268 ? 0.25192 0.55193 0.34786 -0.01523 -0.04112 0.00310  268 LEU A CA  
4105 C C   . LEU A 268 ? 0.24931 0.55691 0.34069 -0.02968 -0.04521 -0.00112 268 LEU A C   
4106 O O   . LEU A 268 ? 0.26118 0.55539 0.34878 -0.04602 -0.04428 -0.00662 268 LEU A O   
4107 C CB  . LEU A 268 ? 0.23483 0.49950 0.32283 -0.00368 -0.03875 0.00543  268 LEU A CB  
4108 C CG  . LEU A 268 ? 0.28334 0.51421 0.36292 -0.01336 -0.03731 0.00117  268 LEU A CG  
4109 C CD1 . LEU A 268 ? 0.27299 0.49176 0.35398 -0.02625 -0.03424 -0.00331 268 LEU A CD1 
4110 C CD2 . LEU A 268 ? 0.29351 0.49614 0.36762 -0.00099 -0.03445 0.00416  268 LEU A CD2 
4122 N N   . LYS A 269 ? 0.25529 0.58331 0.34561 -0.02360 -0.04964 0.00135  269 LYS A N   
4123 C CA  . LYS A 269 ? 0.29372 0.63247 0.37941 -0.03750 -0.05386 -0.00298 269 LYS A CA  
4124 C C   . LYS A 269 ? 0.34455 0.70430 0.43500 -0.05670 -0.05454 -0.00818 269 LYS A C   
4125 O O   . LYS A 269 ? 0.29517 0.64270 0.37854 -0.07396 -0.05488 -0.01433 269 LYS A O   
4126 C CB  . LYS A 269 ? 0.33635 0.70157 0.42186 -0.02617 -0.05878 0.00151  269 LYS A CB  
4127 C CG  . LYS A 269 ? 0.47252 0.85081 0.55197 -0.03709 -0.06384 -0.00203 269 LYS A CG  
4128 C CD  . LYS A 269 ? 0.48389 0.89122 0.56448 -0.02144 -0.06834 0.00430  269 LYS A CD  
4129 C CE  . LYS A 269 ? 0.44512 0.82328 0.51881 -0.00168 -0.06577 0.01068  269 LYS A CE  
4130 N NZ  . LYS A 269 ? 0.46317 0.86316 0.53476 0.01515  -0.06959 0.01767  269 LYS A NZ  
4144 N N   . GLU A 270 ? 0.26015 0.65231 0.36171 -0.05425 -0.05454 -0.00587 270 GLU A N   
4145 C CA  . GLU A 270 ? 0.28272 0.69717 0.38883 -0.07390 -0.05481 -0.01058 270 GLU A CA  
4146 C C   . GLU A 270 ? 0.29239 0.67396 0.39412 -0.08669 -0.04964 -0.01468 270 GLU A C   
4147 O O   . GLU A 270 ? 0.32625 0.70762 0.42391 -0.10719 -0.04954 -0.02029 270 GLU A O   
4148 C CB  . GLU A 270 ? 0.26186 0.72094 0.38156 -0.06653 -0.05553 -0.00661 270 GLU A CB  
4149 C CG  . GLU A 270 ? 0.27200 0.75296 0.39525 -0.08518 -0.05453 -0.01054 270 GLU A CG  
4150 C CD  . GLU A 270 ? 0.32241 0.83932 0.45345 -0.07372 -0.05344 -0.00597 270 GLU A CD  
4151 O OE1 . GLU A 270 ? 0.36635 0.90724 0.49619 -0.06846 -0.05651 -0.00429 270 GLU A OE1 
4152 O OE2 . GLU A 270 ? 0.31080 0.83071 0.44849 -0.06880 -0.04942 -0.00398 270 GLU A OE2 
4159 N N   . LEU A 271 ? 0.27502 0.62895 0.37669 -0.07514 -0.04519 -0.01190 271 LEU A N   
4160 C CA  . LEU A 271 ? 0.30551 0.62843 0.40234 -0.08548 -0.04048 -0.01516 271 LEU A CA  
4161 C C   . LEU A 271 ? 0.37524 0.66556 0.45890 -0.09602 -0.04059 -0.02014 271 LEU A C   
4162 O O   . LEU A 271 ? 0.36059 0.63495 0.43786 -0.11181 -0.03831 -0.02463 271 LEU A O   
4163 C CB  . LEU A 271 ? 0.28188 0.58360 0.38094 -0.07017 -0.03621 -0.01124 271 LEU A CB  
4164 C CG  . LEU A 271 ? 0.30636 0.63291 0.41657 -0.06214 -0.03414 -0.00750 271 LEU A CG  
4165 C CD1 . LEU A 271 ? 0.24998 0.55352 0.35986 -0.04443 -0.03079 -0.00374 271 LEU A CD1 
4166 C CD2 . LEU A 271 ? 0.37566 0.70896 0.48799 -0.07918 -0.03135 -0.01049 271 LEU A CD2 
4178 N N   . LEU A 272 ? 0.33126 0.61126 0.40968 -0.08727 -0.04293 -0.01932 272 LEU A N   
4179 C CA  . LEU A 272 ? 0.35307 0.60429 0.41871 -0.09593 -0.04295 -0.02421 272 LEU A CA  
4180 C C   . LEU A 272 ? 0.45597 0.72103 0.51643 -0.11571 -0.04558 -0.03005 272 LEU A C   
4181 O O   . LEU A 272 ? 0.47273 0.71303 0.52237 -0.12928 -0.04358 -0.03547 272 LEU A O   
4182 C CB  . LEU A 272 ? 0.34423 0.58686 0.40595 -0.08256 -0.04490 -0.02171 272 LEU A CB  
4183 C CG  . LEU A 272 ? 0.32726 0.54734 0.39059 -0.06665 -0.04136 -0.01732 272 LEU A CG  
4184 C CD1 . LEU A 272 ? 0.35195 0.56498 0.41130 -0.05353 -0.04281 -0.01399 272 LEU A CD1 
4185 C CD2 . LEU A 272 ? 0.34544 0.52984 0.40220 -0.07183 -0.03700 -0.02060 272 LEU A CD2 
4197 N N   . GLN A 273 ? 0.39123 0.69630 0.45872 -0.11781 -0.04986 -0.02909 273 GLN A N   
4198 C CA  . GLN A 273 ? 0.38245 0.70411 0.44460 -0.13840 -0.05288 -0.03522 273 GLN A CA  
4199 C C   . GLN A 273 ? 0.42203 0.74922 0.48541 -0.15617 -0.05013 -0.03837 273 GLN A C   
4200 O O   . GLN A 273 ? 0.49135 0.80990 0.54403 -0.17582 -0.05012 -0.04482 273 GLN A O   
4201 C CB  . GLN A 273 ? 0.42322 0.78786 0.49130 -0.13584 -0.05904 -0.03365 273 GLN A CB  
4202 C CG  . GLN A 273 ? 0.45484 0.86108 0.53864 -0.12593 -0.06040 -0.02794 273 GLN A CG  
4203 C CD  . GLN A 273 ? 0.43039 0.87196 0.51474 -0.13006 -0.06349 -0.02814 273 GLN A CD  
4204 O OE1 . GLN A 273 ? 0.48767 0.92798 0.56281 -0.13635 -0.06634 -0.03138 273 GLN A OE1 
4205 N NE2 . GLN A 273 ? 0.36931 0.84046 0.46305 -0.12539 -0.06206 -0.02452 273 GLN A NE2 
4214 N N   . ASN A 274 ? 0.38807 0.72691 0.46228 -0.15028 -0.04741 -0.03423 274 ASN A N   
4215 C CA  . ASN A 274 ? 0.37539 0.72358 0.45040 -0.16793 -0.04458 -0.03673 274 ASN A CA  
4216 C C   . ASN A 274 ? 0.53236 0.84261 0.60114 -0.17180 -0.03874 -0.03746 274 ASN A C   
4217 O O   . ASN A 274 ? 0.46648 0.76802 0.52773 -0.18879 -0.03555 -0.04063 274 ASN A O   
4218 C CB  . ASN A 274 ? 0.39859 0.78535 0.48784 -0.15903 -0.04420 -0.03150 274 ASN A CB  
4219 C CG  . ASN A 274 ? 0.39843 0.82068 0.49163 -0.15241 -0.04859 -0.02964 274 ASN A CG  
4220 O OD1 . ASN A 274 ? 0.41837 0.83793 0.50277 -0.15876 -0.05159 -0.03298 274 ASN A OD1 
4221 N ND2 . ASN A 274 ? 0.33517 0.79006 0.44045 -0.13911 -0.04869 -0.02435 274 ASN A ND2 
4228 N N   . GLY A 275 ? 0.44872 0.73251 0.51770 -0.15405 -0.03644 -0.03381 275 GLY A N   
4229 C CA  . GLY A 275 ? 0.51340 0.76556 0.57773 -0.15505 -0.03089 -0.03343 275 GLY A CA  
4230 C C   . GLY A 275 ? 0.52608 0.80254 0.60292 -0.15163 -0.02865 -0.02936 275 GLY A C   
4231 O O   . GLY A 275 ? 0.45712 0.77033 0.54644 -0.14271 -0.03129 -0.02610 275 GLY A O   
4235 N N   . MET A 276 ? 0.57985 0.83726 0.65291 -0.15767 -0.02380 -0.02932 276 MET A N   
4236 C CA  . MET A 276 ? 0.56489 0.84435 0.64956 -0.15297 -0.02110 -0.02528 276 MET A CA  
4237 C C   . MET A 276 ? 0.59404 0.89221 0.67812 -0.17475 -0.01925 -0.02762 276 MET A C   
4238 O O   . MET A 276 ? 0.58859 0.91019 0.68263 -0.17275 -0.01691 -0.02459 276 MET A O   
4239 C CB  . MET A 276 ? 0.58079 0.82972 0.66348 -0.14087 -0.01685 -0.02239 276 MET A CB  
4240 C CG  . MET A 276 ? 0.50117 0.73842 0.58653 -0.11961 -0.01833 -0.01961 276 MET A CG  
4241 S SD  . MET A 276 ? 0.57501 0.79076 0.66200 -0.10535 -0.01368 -0.01590 276 MET A SD  
4242 C CE  . MET A 276 ? 0.46484 0.65816 0.54913 -0.08773 -0.01571 -0.01481 276 MET A CE  
4252 N N   . ASN A 277 ? 0.63585 0.92131 0.70701 -0.19396 -0.01965 -0.03276 277 ASN A N   
4253 C CA  . ASN A 277 ? 0.64886 0.94410 0.71387 -0.20853 -0.01693 -0.03385 277 ASN A CA  
4254 C C   . ASN A 277 ? 0.67958 0.96913 0.74582 -0.21083 -0.01143 -0.03104 277 ASN A C   
4255 O O   . ASN A 277 ? 0.70150 1.01883 0.77384 -0.21332 -0.00976 -0.02912 277 ASN A O   
4256 C CB  . ASN A 277 ? 0.67705 1.01829 0.75222 -0.20555 -0.02031 -0.03275 277 ASN A CB  
4257 C CG  . ASN A 277 ? 0.75827 1.10384 0.82889 -0.20654 -0.02533 -0.03586 277 ASN A CG  
4258 O OD1 . ASN A 277 ? 0.78471 1.10819 0.83979 -0.22062 -0.02495 -0.04059 277 ASN A OD1 
4259 N ND2 . ASN A 277 ? 0.66076 1.03282 0.74377 -0.19052 -0.02982 -0.03301 277 ASN A ND2 
4266 N N   . GLY A 278 ? 0.64026 0.89356 0.69995 -0.20961 -0.00850 -0.03074 278 GLY A N   
4267 C CA  . GLY A 278 ? 0.70204 0.94366 0.75971 -0.21252 -0.00300 -0.02812 278 GLY A CA  
4268 C C   . GLY A 278 ? 0.67836 0.94154 0.75260 -0.19630 -0.00189 -0.02315 278 GLY A C   
4269 O O   . GLY A 278 ? 0.69561 0.94820 0.76776 -0.19678 0.00283  -0.02069 278 GLY A O   
4273 N N   . ARG A 279 ? 0.62981 0.91796 0.71730 -0.17910 -0.00570 -0.02123 279 ARG A N   
4274 C CA  . ARG A 279 ? 0.56889 0.86836 0.66774 -0.15923 -0.00423 -0.01656 279 ARG A CA  
4275 C C   . ARG A 279 ? 0.52029 0.78145 0.61334 -0.14265 -0.00413 -0.01540 279 ARG A C   
4276 O O   . ARG A 279 ? 0.51003 0.74068 0.59202 -0.14555 -0.00535 -0.01793 279 ARG A O   
4277 C CB  . ARG A 279 ? 0.54748 0.89176 0.66188 -0.14753 -0.00784 -0.01461 279 ARG A CB  
4278 C CG  . ARG A 279 ? 0.51949 0.90728 0.64056 -0.16009 -0.00864 -0.01544 279 ARG A CG  
4279 C CD  . ARG A 279 ? 0.53637 0.96172 0.66976 -0.14280 -0.01254 -0.01283 279 ARG A CD  
4280 N NE  . ARG A 279 ? 0.58348 1.04195 0.71816 -0.14795 -0.01271 -0.01280 279 ARG A NE  
4281 C CZ  . ARG A 279 ? 0.63990 1.12302 0.78145 -0.14246 -0.00964 -0.01013 279 ARG A CZ  
4282 N NH1 . ARG A 279 ? 0.65751 1.13563 0.80509 -0.13132 -0.00589 -0.00727 279 ARG A NH1 
4283 N NH2 . ARG A 279 ? 0.73366 1.24744 0.87535 -0.14861 -0.01013 -0.01056 279 ARG A NH2 
4297 N N   . THR A 280 ? 0.52111 0.78390 0.62094 -0.12588 -0.00227 -0.01183 280 THR A N   
4298 C CA  . THR A 280 ? 0.50019 0.73213 0.59604 -0.11008 -0.00229 -0.01072 280 THR A CA  
4299 C C   . THR A 280 ? 0.44860 0.69918 0.55506 -0.09013 -0.00381 -0.00777 280 THR A C   
4300 O O   . THR A 280 ? 0.40871 0.69452 0.52545 -0.08667 -0.00393 -0.00604 280 THR A O   
4301 C CB  . THR A 280 ? 0.48989 0.69476 0.57869 -0.11053 0.00226  -0.00971 280 THR A CB  
4302 O OG1 . THR A 280 ? 0.44175 0.66968 0.53815 -0.10959 0.00550  -0.00732 280 THR A OG1 
4303 C CG2 . THR A 280 ? 0.52187 0.70271 0.59699 -0.12882 0.00384  -0.01231 280 THR A CG2 
4311 N N   . ILE A 281 ? 0.35978 0.58648 0.46279 -0.07696 -0.00484 -0.00720 281 ILE A N   
4312 C CA  . ILE A 281 ? 0.38375 0.61824 0.49300 -0.05763 -0.00528 -0.00431 281 ILE A CA  
4313 C C   . ILE A 281 ? 0.39357 0.59802 0.49770 -0.04918 -0.00233 -0.00368 281 ILE A C   
4314 O O   . ILE A 281 ? 0.36567 0.54071 0.46150 -0.05197 -0.00255 -0.00530 281 ILE A O   
4315 C CB  . ILE A 281 ? 0.39389 0.63114 0.50329 -0.04996 -0.00964 -0.00405 281 ILE A CB  
4316 C CG1 . ILE A 281 ? 0.38045 0.65114 0.49512 -0.05831 -0.01294 -0.00473 281 ILE A CG1 
4317 C CG2 . ILE A 281 ? 0.35883 0.59669 0.47127 -0.02961 -0.00930 -0.00076 281 ILE A CG2 
4318 C CD1 . ILE A 281 ? 0.36089 0.63557 0.47445 -0.05266 -0.01755 -0.00452 281 ILE A CD1 
4330 N N   . LEU A 282 ? 0.34682 0.55977 0.45548 -0.03929 0.00057  -0.00158 282 LEU A N   
4331 C CA  . LEU A 282 ? 0.41758 0.60477 0.52128 -0.03194 0.00339  -0.00130 282 LEU A CA  
4332 C C   . LEU A 282 ? 0.43233 0.59486 0.52768 -0.04392 0.00472  -0.00302 282 LEU A C   
4333 O O   . LEU A 282 ? 0.42295 0.55866 0.51178 -0.04062 0.00460  -0.00381 282 LEU A O   
4334 C CB  . LEU A 282 ? 0.38703 0.55712 0.48789 -0.01860 0.00182  -0.00090 282 LEU A CB  
4335 C CG  . LEU A 282 ? 0.34982 0.53817 0.45601 -0.00370 0.00203  0.00149  282 LEU A CG  
4336 C CD1 . LEU A 282 ? 0.36134 0.52971 0.46237 0.00711  0.00063  0.00196  282 LEU A CD1 
4337 C CD2 . LEU A 282 ? 0.38529 0.58006 0.49361 0.00207  0.00629  0.00232  282 LEU A CD2 
4349 N N   . GLY A 283 ? 0.40264 0.57444 0.49729 -0.05844 0.00585  -0.00362 283 GLY A N   
4350 C CA  . GLY A 283 ? 0.50634 0.65360 0.59108 -0.06915 0.00779  -0.00461 283 GLY A CA  
4351 C C   . GLY A 283 ? 0.53798 0.66244 0.61400 -0.07539 0.00545  -0.00697 283 GLY A C   
4352 O O   . GLY A 283 ? 0.58071 0.68101 0.64668 -0.08177 0.00713  -0.00761 283 GLY A O   
4356 N N   . SER A 284 ? 0.43507 0.56661 0.51366 -0.07348 0.00179  -0.00818 284 SER A N   
4357 C CA  . SER A 284 ? 0.44673 0.55806 0.51687 -0.07860 -0.00029 -0.01077 284 SER A CA  
4358 C C   . SER A 284 ? 0.48241 0.61067 0.55281 -0.09105 -0.00265 -0.01289 284 SER A C   
4359 O O   . SER A 284 ? 0.41968 0.57858 0.49953 -0.08995 -0.00435 -0.01198 284 SER A O   
4360 C CB  . SER A 284 ? 0.46800 0.56879 0.53891 -0.06507 -0.00243 -0.01060 284 SER A CB  
4361 O OG  . SER A 284 ? 0.52650 0.61151 0.58982 -0.06981 -0.00435 -0.01324 284 SER A OG  
4367 N N   . ALA A 285 ? 0.47018 0.57882 0.52935 -0.10288 -0.00262 -0.01585 285 ALA A N   
4368 C CA  . ALA A 285 ? 0.44702 0.56753 0.50378 -0.11633 -0.00491 -0.01886 285 ALA A CA  
4369 C C   . ALA A 285 ? 0.48031 0.59420 0.53450 -0.11163 -0.00855 -0.02094 285 ALA A C   
4370 O O   . ALA A 285 ? 0.45116 0.56994 0.50082 -0.12269 -0.01065 -0.02417 285 ALA A O   
4371 C CB  . ALA A 285 ? 0.49307 0.59444 0.53643 -0.13382 -0.00219 -0.02136 285 ALA A CB  
4377 N N   . LEU A 286 ? 0.46156 0.56323 0.51724 -0.09665 -0.00910 -0.01945 286 LEU A N   
4378 C CA  . LEU A 286 ? 0.48212 0.58277 0.53698 -0.09115 -0.01245 -0.02066 286 LEU A CA  
4379 C C   . LEU A 286 ? 0.38840 0.49945 0.45238 -0.07459 -0.01358 -0.01710 286 LEU A C   
4380 O O   . LEU A 286 ? 0.39275 0.50797 0.46256 -0.06680 -0.01158 -0.01426 286 LEU A O   
4381 C CB  . LEU A 286 ? 0.44080 0.50940 0.48337 -0.09222 -0.01172 -0.02352 286 LEU A CB  
4382 C CG  . LEU A 286 ? 0.59487 0.63644 0.63145 -0.08741 -0.00843 -0.02289 286 LEU A CG  
4383 C CD1 . LEU A 286 ? 0.61435 0.65561 0.65773 -0.07206 -0.00856 -0.02011 286 LEU A CD1 
4384 C CD2 . LEU A 286 ? 0.58156 0.59591 0.60404 -0.09210 -0.00777 -0.02657 286 LEU A CD2 
4396 N N   . LEU A 287 ? 0.32377 0.43841 0.38766 -0.06957 -0.01660 -0.01730 287 LEU A N   
4397 C CA  . LEU A 287 ? 0.35592 0.48023 0.42636 -0.05481 -0.01766 -0.01368 287 LEU A CA  
4398 C C   . LEU A 287 ? 0.33621 0.43500 0.40306 -0.04557 -0.01564 -0.01298 287 LEU A C   
4399 O O   . LEU A 287 ? 0.40566 0.48692 0.46571 -0.04645 -0.01604 -0.01499 287 LEU A O   
4400 C CB  . LEU A 287 ? 0.32157 0.46015 0.39210 -0.05340 -0.02162 -0.01362 287 LEU A CB  
4401 C CG  . LEU A 287 ? 0.36865 0.53621 0.44295 -0.06378 -0.02410 -0.01476 287 LEU A CG  
4402 C CD1 . LEU A 287 ? 0.40254 0.58472 0.47587 -0.06264 -0.02844 -0.01486 287 LEU A CD1 
4403 C CD2 . LEU A 287 ? 0.39758 0.59068 0.48216 -0.05948 -0.02313 -0.01158 287 LEU A CD2 
4415 N N   . GLU A 288 ? 0.32387 0.42226 0.39505 -0.03697 -0.01347 -0.01041 288 GLU A N   
4416 C CA  . GLU A 288 ? 0.33292 0.40936 0.40102 -0.02981 -0.01133 -0.01007 288 GLU A CA  
4417 C C   . GLU A 288 ? 0.29345 0.36624 0.36083 -0.01972 -0.01236 -0.00833 288 GLU A C   
4418 O O   . GLU A 288 ? 0.25027 0.33762 0.32144 -0.01251 -0.01328 -0.00556 288 GLU A O   
4419 C CB  . GLU A 288 ? 0.33468 0.41331 0.40673 -0.02559 -0.00855 -0.00840 288 GLU A CB  
4420 C CG  . GLU A 288 ? 0.50958 0.56905 0.57878 -0.01804 -0.00672 -0.00814 288 GLU A CG  
4421 C CD  . GLU A 288 ? 0.57151 0.61055 0.63427 -0.02316 -0.00595 -0.01059 288 GLU A CD  
4422 O OE1 . GLU A 288 ? 0.57238 0.60910 0.63257 -0.03155 -0.00521 -0.01181 288 GLU A OE1 
4423 O OE2 . GLU A 288 ? 0.44765 0.47341 0.50729 -0.01864 -0.00587 -0.01113 288 GLU A OE2 
4430 N N   . ASP A 289 ? 0.31818 0.37153 0.38006 -0.01856 -0.01186 -0.00965 289 ASP A N   
4431 C CA  . ASP A 289 ? 0.27258 0.32205 0.33253 -0.01083 -0.01250 -0.00790 289 ASP A CA  
4432 C C   . ASP A 289 ? 0.29623 0.32838 0.35360 -0.00588 -0.01012 -0.00784 289 ASP A C   
4433 O O   . ASP A 289 ? 0.27767 0.30256 0.33152 -0.00202 -0.01011 -0.00701 289 ASP A O   
4434 C CB  . ASP A 289 ? 0.30284 0.35158 0.35830 -0.01484 -0.01480 -0.00938 289 ASP A CB  
4435 C CG  . ASP A 289 ? 0.31110 0.34172 0.36082 -0.01910 -0.01370 -0.01267 289 ASP A CG  
4436 O OD1 . ASP A 289 ? 0.31191 0.33203 0.36112 -0.02059 -0.01164 -0.01404 289 ASP A OD1 
4437 O OD2 . ASP A 289 ? 0.30334 0.33115 0.34855 -0.02030 -0.01490 -0.01380 289 ASP A OD2 
4442 N N   . GLU A 290 ? 0.28258 0.30898 0.34123 -0.00614 -0.00801 -0.00854 290 GLU A N   
4443 C CA  . GLU A 290 ? 0.28558 0.29810 0.34185 -0.00212 -0.00600 -0.00881 290 GLU A CA  
4444 C C   . GLU A 290 ? 0.28722 0.30137 0.34529 0.00421  -0.00417 -0.00709 290 GLU A C   
4445 O O   . GLU A 290 ? 0.29288 0.29769 0.34950 0.00549  -0.00228 -0.00803 290 GLU A O   
4446 C CB  . GLU A 290 ? 0.31850 0.32083 0.37264 -0.00685 -0.00517 -0.01143 290 GLU A CB  
4447 C CG  . GLU A 290 ? 0.38167 0.37955 0.43195 -0.01096 -0.00644 -0.01335 290 GLU A CG  
4448 C CD  . GLU A 290 ? 0.35069 0.33631 0.39724 -0.01182 -0.00526 -0.01560 290 GLU A CD  
4449 O OE1 . GLU A 290 ? 0.36218 0.34405 0.40936 -0.01054 -0.00389 -0.01559 290 GLU A OE1 
4450 O OE2 . GLU A 290 ? 0.33233 0.31328 0.37502 -0.01319 -0.00570 -0.01732 290 GLU A OE2 
4457 N N   . PHE A 291 ? 0.26351 0.28995 0.32402 0.00895  -0.00465 -0.00466 291 PHE A N   
4458 C CA  . PHE A 291 ? 0.27859 0.30438 0.33842 0.01748  -0.00265 -0.00284 291 PHE A CA  
4459 C C   . PHE A 291 ? 0.26396 0.28868 0.31977 0.02465  -0.00326 -0.00005 291 PHE A C   
4460 O O   . PHE A 291 ? 0.27397 0.31304 0.33204 0.02609  -0.00543 0.00184  291 PHE A O   
4461 C CB  . PHE A 291 ? 0.26216 0.30479 0.32762 0.01930  -0.00204 -0.00186 291 PHE A CB  
4462 C CG  . PHE A 291 ? 0.33423 0.37707 0.40216 0.01256  -0.00091 -0.00387 291 PHE A CG  
4463 C CD1 . PHE A 291 ? 0.36312 0.39587 0.42892 0.01474  0.00161  -0.00488 291 PHE A CD1 
4464 C CD2 . PHE A 291 ? 0.31639 0.36944 0.38758 0.00394  -0.00217 -0.00463 291 PHE A CD2 
4465 C CE1 . PHE A 291 ? 0.39194 0.42516 0.45904 0.00921  0.00273  -0.00610 291 PHE A CE1 
4466 C CE2 . PHE A 291 ? 0.38823 0.43955 0.45978 -0.00213 -0.00072 -0.00581 291 PHE A CE2 
4467 C CZ  . PHE A 291 ? 0.40010 0.44157 0.46968 0.00104  0.00171  -0.00628 291 PHE A CZ  
4477 N N   . THR A 292 ? 0.31477 0.32297 0.36377 0.02922  -0.00121 0.00041  292 THR A N   
4478 C CA  . THR A 292 ? 0.29086 0.29421 0.33341 0.03668  -0.00111 0.00369  292 THR A CA  
4479 C C   . THR A 292 ? 0.31090 0.32065 0.35260 0.04769  0.00020  0.00648  292 THR A C   
4480 O O   . THR A 292 ? 0.29814 0.31338 0.34352 0.04944  0.00173  0.00540  292 THR A O   
4481 C CB  . THR A 292 ? 0.29368 0.27493 0.32721 0.03618  0.00112  0.00314  292 THR A CB  
4482 O OG1 . THR A 292 ? 0.32332 0.29431 0.35367 0.03900  0.00414  0.00179  292 THR A OG1 
4483 C CG2 . THR A 292 ? 0.34132 0.31776 0.37637 0.02604  0.00045  -0.00015 292 THR A CG2 
4491 N N   . PRO A 293 ? 0.29901 0.30875 0.33528 0.05607  -0.00024 0.01033  293 PRO A N   
4492 C CA  . PRO A 293 ? 0.33161 0.34413 0.36451 0.06927  0.00160  0.01336  293 PRO A CA  
4493 C C   . PRO A 293 ? 0.39895 0.39219 0.42524 0.07242  0.00581  0.01148  293 PRO A C   
4494 O O   . PRO A 293 ? 0.35417 0.35349 0.38138 0.08026  0.00774  0.01177  293 PRO A O   
4495 C CB  . PRO A 293 ? 0.36302 0.36965 0.38702 0.07697  0.00084  0.01789  293 PRO A CB  
4496 C CG  . PRO A 293 ? 0.35882 0.37693 0.38802 0.06765  -0.00311 0.01741  293 PRO A CG  
4497 C CD  . PRO A 293 ? 0.31941 0.32951 0.35245 0.05469  -0.00268 0.01242  293 PRO A CD  
4505 N N   . PHE A 294 ? 0.36681 0.33753 0.38581 0.06630  0.00741  0.00936  294 PHE A N   
4506 C CA  . PHE A 294 ? 0.39503 0.34753 0.40699 0.06727  0.01118  0.00677  294 PHE A CA  
4507 C C   . PHE A 294 ? 0.36910 0.33248 0.39028 0.06192  0.01124  0.00312  294 PHE A C   
4508 O O   . PHE A 294 ? 0.38632 0.34590 0.40479 0.06681  0.01399  0.00180  294 PHE A O   
4509 C CB  . PHE A 294 ? 0.45285 0.38253 0.45565 0.05967  0.01244  0.00517  294 PHE A CB  
4510 C CG  . PHE A 294 ? 0.52106 0.42927 0.51369 0.05932  0.01633  0.00229  294 PHE A CG  
4511 C CD1 . PHE A 294 ? 0.52387 0.43397 0.52116 0.05258  0.01678  -0.00220 294 PHE A CD1 
4512 C CD2 . PHE A 294 ? 0.58708 0.47163 0.56373 0.06531  0.01966  0.00404  294 PHE A CD2 
4513 C CE1 . PHE A 294 ? 0.52235 0.41353 0.50955 0.05136  0.02017  -0.00542 294 PHE A CE1 
4514 C CE2 . PHE A 294 ? 0.61082 0.47354 0.57620 0.06341  0.02347  0.00060  294 PHE A CE2 
4515 C CZ  . PHE A 294 ? 0.60125 0.46869 0.57250 0.05622  0.02353  -0.00435 294 PHE A CZ  
4525 N N   . ASP A 295 ? 0.33883 0.31410 0.36941 0.05213  0.00851  0.00147  295 ASP A N   
4526 C CA  . ASP A 295 ? 0.36000 0.34379 0.39766 0.04700  0.00869  -0.00134 295 ASP A CA  
4527 C C   . ASP A 295 ? 0.41317 0.41474 0.45617 0.05375  0.00939  0.00011  295 ASP A C   
4528 O O   . ASP A 295 ? 0.36100 0.36458 0.40540 0.05394  0.01137  -0.00168 295 ASP A O   
4529 C CB  . ASP A 295 ? 0.30259 0.29514 0.34759 0.03678  0.00579  -0.00260 295 ASP A CB  
4530 C CG  . ASP A 295 ? 0.36386 0.34240 0.40506 0.03003  0.00542  -0.00462 295 ASP A CG  
4531 O OD1 . ASP A 295 ? 0.38541 0.34813 0.41918 0.03071  0.00754  -0.00583 295 ASP A OD1 
4532 O OD2 . ASP A 295 ? 0.34100 0.32511 0.38627 0.02379  0.00317  -0.00520 295 ASP A OD2 
4537 N N   . VAL A 296 ? 0.33691 0.35456 0.38368 0.05853  0.00758  0.00328  296 VAL A N   
4538 C CA  . VAL A 296 ? 0.34340 0.38343 0.39678 0.06430  0.00803  0.00474  296 VAL A CA  
4539 C C   . VAL A 296 ? 0.37609 0.40849 0.42259 0.07665  0.01186  0.00530  296 VAL A C   
4540 O O   . VAL A 296 ? 0.37740 0.41972 0.42732 0.07906  0.01399  0.00430  296 VAL A O   
4541 C CB  . VAL A 296 ? 0.31070 0.37155 0.36913 0.06682  0.00485  0.00798  296 VAL A CB  
4542 C CG1 . VAL A 296 ? 0.35193 0.43887 0.41685 0.07460  0.00550  0.00989  296 VAL A CG1 
4543 C CG2 . VAL A 296 ? 0.29017 0.35841 0.35476 0.05324  0.00152  0.00638  296 VAL A CG2 
4553 N N   . VAL A 297 ? 0.43467 0.44739 0.46985 0.08444  0.01321  0.00677  297 VAL A N   
4554 C CA  . VAL A 297 ? 0.45010 0.45030 0.47536 0.09692  0.01737  0.00706  297 VAL A CA  
4555 C C   . VAL A 297 ? 0.47744 0.46235 0.49875 0.09168  0.02024  0.00247  297 VAL A C   
4556 O O   . VAL A 297 ? 0.55032 0.53579 0.56888 0.09909  0.02352  0.00137  297 VAL A O   
4557 C CB  . VAL A 297 ? 0.43005 0.40855 0.44149 0.10513  0.01837  0.00990  297 VAL A CB  
4558 C CG1 . VAL A 297 ? 0.50565 0.46427 0.50338 0.11711  0.02331  0.00947  297 VAL A CG1 
4559 C CG2 . VAL A 297 ? 0.50262 0.50063 0.51816 0.11245  0.01534  0.01498  297 VAL A CG2 
4569 N N   . ARG A 298 ? 0.46338 0.43588 0.48409 0.07938  0.01906  -0.00033 298 ARG A N   
4570 C CA  . ARG A 298 ? 0.45427 0.41490 0.47160 0.07356  0.02111  -0.00473 298 ARG A CA  
4571 C C   . ARG A 298 ? 0.54048 0.52080 0.56728 0.07214  0.02141  -0.00580 298 ARG A C   
4572 O O   . ARG A 298 ? 0.52376 0.49957 0.54629 0.07541  0.02449  -0.00811 298 ARG A O   
4573 C CB  . ARG A 298 ? 0.53485 0.48542 0.55227 0.06073  0.01908  -0.00705 298 ARG A CB  
4574 C CG  . ARG A 298 ? 0.51407 0.46451 0.53395 0.05245  0.01935  -0.01105 298 ARG A CG  
4575 C CD  . ARG A 298 ? 0.55666 0.50051 0.57721 0.04113  0.01717  -0.01312 298 ARG A CD  
4576 N NE  . ARG A 298 ? 0.44852 0.39437 0.47090 0.03546  0.01728  -0.01627 298 ARG A NE  
4577 C CZ  . ARG A 298 ? 0.47956 0.43367 0.50868 0.02824  0.01487  -0.01679 298 ARG A CZ  
4578 N NH1 . ARG A 298 ? 0.48630 0.44614 0.52075 0.02465  0.01227  -0.01510 298 ARG A NH1 
4579 N NH2 . ARG A 298 ? 0.45710 0.41277 0.48632 0.02507  0.01522  -0.01906 298 ARG A NH2 
4593 N N   . GLN A 299 ? 0.44211 0.44389 0.48058 0.06711  0.01857  -0.00416 299 GLN A N   
4594 C CA  . GLN A 299 ? 0.45836 0.47764 0.50492 0.06332  0.01902  -0.00492 299 GLN A CA  
4595 C C   . GLN A 299 ? 0.56694 0.60655 0.61754 0.07301  0.02101  -0.00291 299 GLN A C   
4596 O O   . GLN A 299 ? 0.48389 0.53147 0.53634 0.07334  0.02345  -0.00415 299 GLN A O   
4597 C CB  . GLN A 299 ? 0.46218 0.49214 0.51729 0.05167  0.01555  -0.00454 299 GLN A CB  
4598 C CG  . GLN A 299 ? 0.46922 0.51218 0.53015 0.04564  0.01634  -0.00525 299 GLN A CG  
4599 C CD  . GLN A 299 ? 0.38459 0.42988 0.44985 0.03368  0.01362  -0.00547 299 GLN A CD  
4600 O OE1 . GLN A 299 ? 0.38937 0.44616 0.45886 0.02805  0.01411  -0.00516 299 GLN A OE1 
4601 N NE2 . GLN A 299 ? 0.37575 0.40963 0.43895 0.02986  0.01112  -0.00592 299 GLN A NE2 
4610 N N   . CYS A 300 ? 0.49082 0.54151 0.54317 0.08099  0.01998  0.00034  300 CYS A N   
4611 C CA  . CYS A 300 ? 0.53124 0.60754 0.58947 0.09004  0.02133  0.00257  300 CYS A CA  
4612 C C   . CYS A 300 ? 0.61762 0.68470 0.66626 0.10611  0.02561  0.00272  300 CYS A C   
4613 O O   . CYS A 300 ? 0.67041 0.70937 0.70640 0.11055  0.02723  0.00161  300 CYS A O   
4614 C CB  . CYS A 300 ? 0.50354 0.60017 0.56852 0.09155  0.01783  0.00609  300 CYS A CB  
4615 S SG  . CYS A 300 ? 0.49448 0.60787 0.57069 0.07353  0.01355  0.00560  300 CYS A SG  
4621 N N   . SER A 301 ? 0.75353 0.84496 0.80759 0.11468  0.02773  0.00402  301 SER A N   
4622 C CA  . SER A 301 ? 0.84378 0.93067 0.88901 0.13255  0.03209  0.00454  301 SER A CA  
4623 C C   . SER A 301 ? 0.83485 0.91781 0.87390 0.14605  0.03120  0.00848  301 SER A C   
4624 O O   . SER A 301 ? 0.87989 0.97616 0.92562 0.14246  0.02697  0.01135  301 SER A O   
4625 C CB  . SER A 301 ? 0.89526 1.01400 0.94937 0.13807  0.03469  0.00500  301 SER A CB  
4626 O OG  . SER A 301 ? 0.92623 1.07965 0.99334 0.13733  0.03164  0.00842  301 SER A OG  
4632 N N   . SER B 1   ? 0.43326 0.32756 0.40663 0.04842  0.00757  -0.02315 1   SER B N   
4633 C CA  . SER B 1   ? 0.44702 0.32584 0.41539 0.03793  0.00803  -0.02382 1   SER B CA  
4634 C C   . SER B 1   ? 0.40174 0.29291 0.38221 0.02779  0.00613  -0.02304 1   SER B C   
4635 O O   . SER B 1   ? 0.35261 0.26244 0.34490 0.02780  0.00465  -0.02290 1   SER B O   
4636 C CB  . SER B 1   ? 0.44540 0.31790 0.40910 0.03572  0.00890  -0.02761 1   SER B CB  
4637 O OG  . SER B 1   ? 0.69269 0.55059 0.64288 0.04571  0.01123  -0.02873 1   SER B OG  
4645 N N   . GLY B 2   ? 0.41269 0.29329 0.38936 0.01879  0.00641  -0.02286 2   GLY B N   
4646 C CA  . GLY B 2   ? 0.40705 0.29870 0.39387 0.00993  0.00494  -0.02198 2   GLY B CA  
4647 C C   . GLY B 2   ? 0.43266 0.32019 0.41771 0.00777  0.00548  -0.01890 2   GLY B C   
4648 O O   . GLY B 2   ? 0.40849 0.28766 0.38632 0.01405  0.00656  -0.01695 2   GLY B O   
4652 N N   . PHE B 3   ? 0.39121 0.28512 0.38222 -0.00082 0.00489  -0.01825 3   PHE B N   
4653 C CA  . PHE B 3   ? 0.36917 0.26170 0.35935 -0.00357 0.00571  -0.01538 3   PHE B CA  
4654 C C   . PHE B 3   ? 0.41305 0.32187 0.41493 -0.00941 0.00460  -0.01506 3   PHE B C   
4655 O O   . PHE B 3   ? 0.40219 0.31482 0.40655 -0.01619 0.00404  -0.01628 3   PHE B O   
4656 C CB  . PHE B 3   ? 0.40741 0.28021 0.38387 -0.00901 0.00790  -0.01457 3   PHE B CB  
4657 C CG  . PHE B 3   ? 0.40158 0.26926 0.37351 -0.00902 0.00942  -0.01098 3   PHE B CG  
4658 C CD1 . PHE B 3   ? 0.41917 0.28043 0.38507 0.00097  0.00997  -0.00885 3   PHE B CD1 
4659 C CD2 . PHE B 3   ? 0.41851 0.29045 0.39267 -0.01853 0.01025  -0.00960 3   PHE B CD2 
4660 C CE1 . PHE B 3   ? 0.47753 0.33470 0.43868 0.00137  0.01127  -0.00522 3   PHE B CE1 
4661 C CE2 . PHE B 3   ? 0.42408 0.29189 0.39368 -0.01886 0.01195  -0.00624 3   PHE B CE2 
4662 C CZ  . PHE B 3   ? 0.43558 0.29525 0.39831 -0.00888 0.01244  -0.00390 3   PHE B CZ  
4672 N N   . ARG B 4   ? 0.36285 0.28188 0.37139 -0.00609 0.00425  -0.01363 4   ARG B N   
4673 C CA  . ARG B 4   ? 0.34204 0.27557 0.36068 -0.00906 0.00356  -0.01341 4   ARG B CA  
4674 C C   . ARG B 4   ? 0.34238 0.27779 0.36080 -0.00997 0.00485  -0.01106 4   ARG B C   
4675 O O   . ARG B 4   ? 0.33482 0.26284 0.34692 -0.00659 0.00572  -0.00955 4   ARG B O   
4676 C CB  . ARG B 4   ? 0.35942 0.30297 0.38543 -0.00413 0.00227  -0.01462 4   ARG B CB  
4677 C CG  . ARG B 4   ? 0.38839 0.33337 0.41605 -0.00378 0.00122  -0.01666 4   ARG B CG  
4678 C CD  . ARG B 4   ? 0.42949 0.38062 0.46143 -0.00899 0.00059  -0.01668 4   ARG B CD  
4679 N NE  . ARG B 4   ? 0.42839 0.38336 0.46283 -0.00855 -0.00052 -0.01807 4   ARG B NE  
4680 C CZ  . ARG B 4   ? 0.42821 0.39062 0.46670 -0.01108 -0.00142 -0.01769 4   ARG B CZ  
4681 N NH1 . ARG B 4   ? 0.44806 0.41698 0.48972 -0.01363 -0.00134 -0.01622 4   ARG B NH1 
4682 N NH2 . ARG B 4   ? 0.39188 0.35646 0.43102 -0.01052 -0.00231 -0.01857 4   ARG B NH2 
4696 N N   . LYS B 5   ? 0.33806 0.28487 0.36347 -0.01333 0.00498  -0.01066 5   LYS B N   
4697 C CA  . LYS B 5   ? 0.31820 0.26982 0.34460 -0.01336 0.00644  -0.00879 5   LYS B CA  
4698 C C   . LYS B 5   ? 0.34200 0.29691 0.37086 -0.00645 0.00567  -0.00957 5   LYS B C   
4699 O O   . LYS B 5   ? 0.35940 0.32186 0.39447 -0.00477 0.00482  -0.01107 5   LYS B O   
4700 C CB  . LYS B 5   ? 0.36824 0.33295 0.40150 -0.01747 0.00698  -0.00842 5   LYS B CB  
4701 C CG  . LYS B 5   ? 0.49649 0.46612 0.52923 -0.01986 0.00926  -0.00638 5   LYS B CG  
4702 C CD  . LYS B 5   ? 0.49766 0.45553 0.52069 -0.02476 0.01107  -0.00438 5   LYS B CD  
4703 C CE  . LYS B 5   ? 0.50656 0.46671 0.52815 -0.03487 0.01226  -0.00384 5   LYS B CE  
4704 N NZ  . LYS B 5   ? 0.58877 0.56901 0.62093 -0.03679 0.01179  -0.00453 5   LYS B NZ  
4718 N N   . MET B 6   ? 0.29650 0.24563 0.31958 -0.00294 0.00602  -0.00852 6   MET B N   
4719 C CA  . MET B 6   ? 0.30268 0.25610 0.32728 0.00273  0.00487  -0.00976 6   MET B CA  
4720 C C   . MET B 6   ? 0.32696 0.28470 0.35073 0.00392  0.00578  -0.00882 6   MET B C   
4721 O O   . MET B 6   ? 0.34130 0.29378 0.35870 0.00375  0.00702  -0.00626 6   MET B O   
4722 C CB  . MET B 6   ? 0.33011 0.27655 0.34873 0.00743  0.00404  -0.00957 6   MET B CB  
4723 C CG  . MET B 6   ? 0.39409 0.34838 0.41448 0.01252  0.00266  -0.01088 6   MET B CG  
4724 S SD  . MET B 6   ? 0.47129 0.42044 0.48518 0.01982  0.00181  -0.01047 6   MET B SD  
4725 C CE  . MET B 6   ? 0.47124 0.41966 0.48909 0.01749  0.00150  -0.01294 6   MET B CE  
4735 N N   . ALA B 7   ? 0.32105 0.28678 0.34966 0.00496  0.00544  -0.01089 7   ALA B N   
4736 C CA  . ALA B 7   ? 0.28326 0.25288 0.31004 0.00632  0.00629  -0.01079 7   ALA B CA  
4737 C C   . ALA B 7   ? 0.33077 0.30229 0.35442 0.01021  0.00465  -0.01176 7   ALA B C   
4738 O O   . ALA B 7   ? 0.29598 0.26858 0.32080 0.01189  0.00296  -0.01312 7   ALA B O   
4739 C CB  . ALA B 7   ? 0.32694 0.30235 0.35835 0.00568  0.00718  -0.01295 7   ALA B CB  
4745 N N   . PHE B 8   ? 0.32148 0.29550 0.34119 0.01163  0.00517  -0.01112 8   PHE B N   
4746 C CA  . PHE B 8   ? 0.32330 0.30296 0.34059 0.01490  0.00327  -0.01251 8   PHE B CA  
4747 C C   . PHE B 8   ? 0.29563 0.28143 0.31742 0.01268  0.00255  -0.01700 8   PHE B C   
4748 O O   . PHE B 8   ? 0.26715 0.25147 0.29138 0.01011  0.00412  -0.01850 8   PHE B O   
4749 C CB  . PHE B 8   ? 0.35452 0.33609 0.36571 0.01653  0.00395  -0.01096 8   PHE B CB  
4750 C CG  . PHE B 8   ? 0.32792 0.30185 0.33167 0.01913  0.00468  -0.00610 8   PHE B CG  
4751 C CD1 . PHE B 8   ? 0.37355 0.34676 0.37215 0.02482  0.00285  -0.00433 8   PHE B CD1 
4752 C CD2 . PHE B 8   ? 0.36218 0.32951 0.36341 0.01582  0.00746  -0.00323 8   PHE B CD2 
4753 C CE1 . PHE B 8   ? 0.42314 0.38554 0.41221 0.02803  0.00391  0.00053  8   PHE B CE1 
4754 C CE2 . PHE B 8   ? 0.44762 0.40445 0.43959 0.01703  0.00863  0.00146  8   PHE B CE2 
4755 C CZ  . PHE B 8   ? 0.40696 0.35962 0.39218 0.02337  0.00696  0.00338  8   PHE B CZ  
4765 N N   . PRO B 9   ? 0.32606 0.31890 0.34799 0.01368  0.00042  -0.01914 9   PRO B N   
4766 C CA  . PRO B 9   ? 0.33407 0.33178 0.35785 0.00982  0.00006  -0.02368 9   PRO B CA  
4767 C C   . PRO B 9   ? 0.32950 0.32681 0.34941 0.00841  0.00140  -0.02538 9   PRO B C   
4768 O O   . PRO B 9   ? 0.33440 0.33470 0.34998 0.01082  0.00114  -0.02392 9   PRO B O   
4769 C CB  . PRO B 9   ? 0.31932 0.32839 0.34294 0.01104  -0.00256 -0.02509 9   PRO B CB  
4770 C CG  . PRO B 9   ? 0.39642 0.40426 0.41925 0.01716  -0.00337 -0.02103 9   PRO B CG  
4771 C CD  . PRO B 9   ? 0.32419 0.32146 0.34320 0.01860  -0.00152 -0.01736 9   PRO B CD  
4779 N N   . SER B 10  ? 0.30262 0.29521 0.32281 0.00515  0.00306  -0.02833 10  SER B N   
4780 C CA  . SER B 10  ? 0.28648 0.27581 0.30238 0.00504  0.00529  -0.02982 10  SER B CA  
4781 C C   . SER B 10  ? 0.30253 0.29397 0.31291 0.00153  0.00493  -0.03492 10  SER B C   
4782 O O   . SER B 10  ? 0.31176 0.29997 0.31683 0.00170  0.00688  -0.03687 10  SER B O   
4783 C CB  . SER B 10  ? 0.32372 0.30509 0.34153 0.00548  0.00793  -0.02953 10  SER B CB  
4784 O OG  . SER B 10  ? 0.34290 0.31936 0.36135 0.00277  0.00789  -0.03198 10  SER B OG  
4790 N N   . GLY B 11  ? 0.32575 0.32370 0.33681 -0.00194 0.00257  -0.03729 11  GLY B N   
4791 C CA  . GLY B 11  ? 0.34051 0.34048 0.34587 -0.00773 0.00228  -0.04289 11  GLY B CA  
4792 C C   . GLY B 11  ? 0.36089 0.36512 0.35970 -0.00710 0.00216  -0.04454 11  GLY B C   
4793 O O   . GLY B 11  ? 0.35597 0.35417 0.34763 -0.01084 0.00382  -0.04916 11  GLY B O   
4797 N N   . LYS B 12  ? 0.31646 0.32997 0.31602 -0.00231 0.00034  -0.04088 12  LYS B N   
4798 C CA  . LYS B 12  ? 0.32071 0.33902 0.31325 -0.00148 0.00014  -0.04205 12  LYS B CA  
4799 C C   . LYS B 12  ? 0.37782 0.38511 0.36586 -0.00018 0.00401  -0.04257 12  LYS B C   
4800 O O   . LYS B 12  ? 0.37859 0.38583 0.35900 -0.00198 0.00487  -0.04638 12  LYS B O   
4801 C CB  . LYS B 12  ? 0.37714 0.40452 0.37025 0.00467  -0.00204 -0.03670 12  LYS B CB  
4802 C CG  . LYS B 12  ? 0.45855 0.50135 0.45365 0.00494  -0.00610 -0.03707 12  LYS B CG  
4803 C CD  . LYS B 12  ? 0.48600 0.53366 0.47998 0.01343  -0.00769 -0.03070 12  LYS B CD  
4804 C CE  . LYS B 12  ? 0.67220 0.73892 0.66659 0.01588  -0.01189 -0.03107 12  LYS B CE  
4805 N NZ  . LYS B 12  ? 0.77655 0.84817 0.77852 0.01443  -0.01291 -0.03224 12  LYS B NZ  
4819 N N   . VAL B 13  ? 0.31230 0.31124 0.30472 0.00285  0.00648  -0.03922 13  VAL B N   
4820 C CA  . VAL B 13  ? 0.32546 0.31727 0.31447 0.00513  0.01036  -0.03951 13  VAL B CA  
4821 C C   . VAL B 13  ? 0.32988 0.31058 0.31507 0.00289  0.01280  -0.04453 13  VAL B C   
4822 O O   . VAL B 13  ? 0.33467 0.30981 0.31286 0.00427  0.01580  -0.04737 13  VAL B O   
4823 C CB  . VAL B 13  ? 0.30560 0.29631 0.30094 0.00899  0.01188  -0.03368 13  VAL B CB  
4824 C CG1 . VAL B 13  ? 0.31687 0.30425 0.30985 0.01192  0.01622  -0.03377 13  VAL B CG1 
4825 C CG2 . VAL B 13  ? 0.35426 0.35154 0.35005 0.01081  0.00999  -0.02879 13  VAL B CG2 
4835 N N   . GLU B 14  ? 0.32872 0.30460 0.31713 -0.00006 0.01197  -0.04553 14  GLU B N   
4836 C CA  . GLU B 14  ? 0.33585 0.29781 0.31835 -0.00195 0.01463  -0.04971 14  GLU B CA  
4837 C C   . GLU B 14  ? 0.34889 0.30634 0.31981 -0.00639 0.01548  -0.05616 14  GLU B C   
4838 O O   . GLU B 14  ? 0.40416 0.34805 0.36651 -0.00498 0.01910  -0.05941 14  GLU B O   
4839 C CB  . GLU B 14  ? 0.33817 0.29651 0.32436 -0.00612 0.01328  -0.04984 14  GLU B CB  
4840 C CG  . GLU B 14  ? 0.33437 0.29434 0.33016 -0.00203 0.01290  -0.04436 14  GLU B CG  
4841 C CD  . GLU B 14  ? 0.36413 0.32426 0.36366 -0.00656 0.01100  -0.04441 14  GLU B CD  
4842 O OE1 . GLU B 14  ? 0.38861 0.33904 0.38204 -0.01137 0.01219  -0.04803 14  GLU B OE1 
4843 O OE2 . GLU B 14  ? 0.30533 0.27394 0.31265 -0.00527 0.00881  -0.04085 14  GLU B OE2 
4850 N N   . GLY B 15  ? 0.37035 0.33913 0.33993 -0.01142 0.01224  -0.05829 15  GLY B N   
4851 C CA  . GLY B 15  ? 0.40093 0.36690 0.35891 -0.01714 0.01267  -0.06504 15  GLY B CA  
4852 C C   . GLY B 15  ? 0.39820 0.36359 0.34926 -0.01265 0.01486  -0.06598 15  GLY B C   
4853 O O   . GLY B 15  ? 0.41468 0.37700 0.35467 -0.01705 0.01547  -0.07199 15  GLY B O   
4857 N N   . CYS B 16  ? 0.37802 0.34648 0.33470 -0.00467 0.01630  -0.06041 16  CYS B N   
4858 C CA  . CYS B 16  ? 0.35297 0.32206 0.30361 -0.00010 0.01903  -0.06071 16  CYS B CA  
4859 C C   . CYS B 16  ? 0.37253 0.32943 0.32072 0.00606  0.02418  -0.06082 16  CYS B C   
4860 O O   . CYS B 16  ? 0.38375 0.34139 0.32659 0.01042  0.02722  -0.06145 16  CYS B O   
4861 C CB  . CYS B 16  ? 0.34264 0.32576 0.29998 0.00399  0.01745  -0.05408 16  CYS B CB  
4862 S SG  . CYS B 16  ? 0.40579 0.40441 0.36415 -0.00003 0.01156  -0.05334 16  CYS B SG  
4868 N N   . MET B 17  ? 0.37894 0.32630 0.33095 0.00746  0.02532  -0.05979 17  MET B N   
4869 C CA  . MET B 17  ? 0.38998 0.32932 0.34095 0.01540  0.02992  -0.05873 17  MET B CA  
4870 C C   . MET B 17  ? 0.43187 0.35241 0.36786 0.01586  0.03363  -0.06548 17  MET B C   
4871 O O   . MET B 17  ? 0.41392 0.32282 0.34283 0.00899  0.03272  -0.06990 17  MET B O   
4872 C CB  . MET B 17  ? 0.43222 0.37099 0.39351 0.01792  0.02935  -0.05391 17  MET B CB  
4873 C CG  . MET B 17  ? 0.39849 0.35274 0.37275 0.01715  0.02611  -0.04766 17  MET B CG  
4874 S SD  . MET B 17  ? 0.38886 0.35762 0.36593 0.02103  0.02761  -0.04361 17  MET B SD  
4875 C CE  . MET B 17  ? 0.39769 0.36351 0.37308 0.02966  0.03318  -0.04377 17  MET B CE  
4885 N N   . VAL B 18  ? 0.43623 0.35360 0.36640 0.02371  0.03814  -0.06643 18  VAL B N   
4886 C CA  . VAL B 18  ? 0.48070 0.37800 0.39449 0.02618  0.04253  -0.07287 18  VAL B CA  
4887 C C   . VAL B 18  ? 0.46133 0.35601 0.37588 0.03884  0.04731  -0.07019 18  VAL B C   
4888 O O   . VAL B 18  ? 0.44257 0.35435 0.37001 0.04391  0.04711  -0.06414 18  VAL B O   
4889 C CB  . VAL B 18  ? 0.46268 0.36002 0.36430 0.02292  0.04344  -0.07883 18  VAL B CB  
4890 C CG1 . VAL B 18  ? 0.47177 0.37542 0.37309 0.01085  0.03830  -0.08138 18  VAL B CG1 
4891 C CG2 . VAL B 18  ? 0.44222 0.35732 0.34911 0.02936  0.04491  -0.07526 18  VAL B CG2 
4901 N N   . GLN B 19  ? 0.50091 0.37422 0.40020 0.04400  0.05191  -0.07503 19  GLN B N   
4902 C CA  . GLN B 19  ? 0.49778 0.36893 0.39568 0.05834  0.05703  -0.07302 19  GLN B CA  
4903 C C   . GLN B 19  ? 0.54035 0.41268 0.42809 0.06390  0.06140  -0.07715 19  GLN B C   
4904 O O   . GLN B 19  ? 0.57044 0.42793 0.44284 0.05852  0.06234  -0.08416 19  GLN B O   
4905 C CB  . GLN B 19  ? 0.52953 0.37357 0.41474 0.06312  0.06005  -0.07523 19  GLN B CB  
4906 C CG  . GLN B 19  ? 0.62557 0.46890 0.50987 0.07976  0.06493  -0.07235 19  GLN B CG  
4907 C CD  . GLN B 19  ? 0.74495 0.55761 0.61302 0.08571  0.06835  -0.07449 19  GLN B CD  
4908 O OE1 . GLN B 19  ? 0.76511 0.57751 0.63785 0.09445  0.06886  -0.06946 19  GLN B OE1 
4909 N NE2 . GLN B 19  ? 0.81766 0.60342 0.66519 0.08069  0.07079  -0.08198 19  GLN B NE2 
4918 N N   . VAL B 20  ? 0.48706 0.37798 0.38328 0.07336  0.06392  -0.07301 20  VAL B N   
4919 C CA  . VAL B 20  ? 0.53903 0.43324 0.42617 0.07986  0.06873  -0.07647 20  VAL B CA  
4920 C C   . VAL B 20  ? 0.60173 0.49232 0.48531 0.09595  0.07456  -0.07563 20  VAL B C   
4921 O O   . VAL B 20  ? 0.54076 0.44723 0.43849 0.10201  0.07421  -0.06920 20  VAL B O   
4922 C CB  . VAL B 20  ? 0.55874 0.48097 0.45780 0.07703  0.06742  -0.07234 20  VAL B CB  
4923 C CG1 . VAL B 20  ? 0.57651 0.50193 0.46483 0.08387  0.07295  -0.07619 20  VAL B CG1 
4924 C CG2 . VAL B 20  ? 0.51691 0.44419 0.41985 0.06318  0.06142  -0.07204 20  VAL B CG2 
4934 N N   . THR B 21  ? 0.62489 0.49552 0.48905 0.10319  0.07996  -0.08221 21  THR B N   
4935 C CA  . THR B 21  ? 0.65556 0.52128 0.51370 0.12084  0.08612  -0.08185 21  THR B CA  
4936 C C   . THR B 21  ? 0.70624 0.57632 0.55409 0.12890  0.09194  -0.08620 21  THR B C   
4937 O O   . THR B 21  ? 0.70954 0.56535 0.54220 0.12266  0.09286  -0.09324 21  THR B O   
4938 C CB  . THR B 21  ? 0.67679 0.50657 0.51700 0.12544  0.08839  -0.08556 21  THR B CB  
4939 O OG1 . THR B 21  ? 0.64139 0.46899 0.49163 0.11938  0.08353  -0.08077 21  THR B OG1 
4940 C CG2 . THR B 21  ? 0.73080 0.55477 0.56237 0.14629  0.09530  -0.08524 21  THR B CG2 
4948 N N   . CYS B 22  ? 0.70849 0.59962 0.56433 0.14265  0.09595  -0.08224 22  CYS B N   
4949 C CA  . CYS B 22  ? 0.75445 0.65037 0.60001 0.15306  0.10256  -0.08622 22  CYS B CA  
4950 C C   . CYS B 22  ? 0.75960 0.65887 0.60411 0.17361  0.10823  -0.08399 22  CYS B C   
4951 O O   . CYS B 22  ? 0.69580 0.62392 0.55917 0.17869  0.10744  -0.07679 22  CYS B O   
4952 C CB  . CYS B 22  ? 0.71733 0.64617 0.57606 0.14689  0.10179  -0.08318 22  CYS B CB  
4953 S SG  . CYS B 22  ? 0.85544 0.79011 0.69988 0.15819  0.11016  -0.08873 22  CYS B SG  
4959 N N   . GLY B 23  ? 0.80362 0.67527 0.62768 0.18317  0.11270  -0.08938 23  GLY B N   
4960 C CA  . GLY B 23  ? 0.79282 0.66850 0.61903 0.19842  0.11477  -0.08502 23  GLY B CA  
4961 C C   . GLY B 23  ? 0.77618 0.64693 0.61022 0.19986  0.11100  -0.07926 23  GLY B C   
4962 O O   . GLY B 23  ? 0.84283 0.68415 0.66707 0.19174  0.10839  -0.08149 23  GLY B O   
4966 N N   . THR B 24  ? 0.68463 0.58544 0.53649 0.20889  0.11045  -0.07184 24  THR B N   
4967 C CA  . THR B 24  ? 0.77782 0.67723 0.63774 0.21082  0.10669  -0.06598 24  THR B CA  
4968 C C   . THR B 24  ? 0.70985 0.63153 0.58882 0.20161  0.10291  -0.06238 24  THR B C   
4969 O O   . THR B 24  ? 0.73033 0.65141 0.61662 0.20179  0.09943  -0.05776 24  THR B O   
4970 C CB  . THR B 24  ? 0.75439 0.67187 0.62050 0.22697  0.10780  -0.05984 24  THR B CB  
4971 O OG1 . THR B 24  ? 0.76463 0.72496 0.64841 0.23001  0.10916  -0.05678 24  THR B OG1 
4972 C CG2 . THR B 24  ? 0.83056 0.72239 0.67593 0.23749  0.11159  -0.06286 24  THR B CG2 
4980 N N   . THR B 25  ? 0.72245 0.66219 0.61011 0.18926  0.10158  -0.06341 25  THR B N   
4981 C CA  . THR B 25  ? 0.67545 0.63817 0.58429 0.17347  0.09491  -0.05797 25  THR B CA  
4982 C C   . THR B 25  ? 0.68665 0.62451 0.58981 0.15676  0.08979  -0.06086 25  THR B C   
4983 O O   . THR B 25  ? 0.63598 0.55640 0.52543 0.15063  0.09082  -0.06705 25  THR B O   
4984 C CB  . THR B 25  ? 0.67937 0.67406 0.60015 0.16715  0.09554  -0.05637 25  THR B CB  
4985 O OG1 . THR B 25  ? 0.75465 0.77281 0.67815 0.18253  0.10147  -0.05509 25  THR B OG1 
4986 C CG2 . THR B 25  ? 0.68718 0.70497 0.62884 0.15315  0.08942  -0.04998 25  THR B CG2 
4994 N N   . THR B 26  ? 0.65222 0.59005 0.56566 0.14940  0.08433  -0.05662 26  THR B N   
4995 C CA  . THR B 26  ? 0.63235 0.55349 0.54390 0.13300  0.07912  -0.05853 26  THR B CA  
4996 C C   . THR B 26  ? 0.60254 0.54818 0.53488 0.12135  0.07328  -0.05262 26  THR B C   
4997 O O   . THR B 26  ? 0.51912 0.48477 0.46523 0.12563  0.07230  -0.04692 26  THR B O   
4998 C CB  . THR B 26  ? 0.66300 0.55230 0.56197 0.13464  0.07869  -0.06024 26  THR B CB  
4999 O OG1 . THR B 26  ? 0.68125 0.54224 0.55714 0.14169  0.08411  -0.06707 26  THR B OG1 
5000 C CG2 . THR B 26  ? 0.67840 0.55785 0.57962 0.11784  0.07301  -0.06091 26  THR B CG2 
5008 N N   . LEU B 27  ? 0.53308 0.47840 0.46682 0.10723  0.06973  -0.05414 27  LEU B N   
5009 C CA  . LEU B 27  ? 0.42087 0.38363 0.37132 0.09607  0.06421  -0.04890 27  LEU B CA  
5010 C C   . LEU B 27  ? 0.45040 0.39970 0.39644 0.08274  0.05993  -0.05184 27  LEU B C   
5011 O O   . LEU B 27  ? 0.46598 0.39264 0.39741 0.08170  0.06087  -0.05753 27  LEU B O   
5012 C CB  . LEU B 27  ? 0.42395 0.41608 0.38630 0.09543  0.06525  -0.04482 27  LEU B CB  
5013 C CG  . LEU B 27  ? 0.49072 0.48861 0.44543 0.09814  0.06968  -0.04790 27  LEU B CG  
5014 C CD1 . LEU B 27  ? 0.53124 0.52067 0.47941 0.08682  0.06706  -0.05091 27  LEU B CD1 
5015 C CD2 . LEU B 27  ? 0.59871 0.62714 0.56578 0.09969  0.07183  -0.04290 27  LEU B CD2 
5027 N N   . ASN B 28  ? 0.40069 0.36388 0.35853 0.07306  0.05553  -0.04801 28  ASN B N   
5028 C CA  . ASN B 28  ? 0.37182 0.32651 0.32708 0.06164  0.05115  -0.05008 28  ASN B CA  
5029 C C   . ASN B 28  ? 0.39639 0.35938 0.34855 0.05671  0.05103  -0.05136 28  ASN B C   
5030 O O   . ASN B 28  ? 0.38874 0.36835 0.34571 0.05905  0.05310  -0.04830 28  ASN B O   
5031 C CB  . ASN B 28  ? 0.35076 0.31216 0.31885 0.05503  0.04618  -0.04521 28  ASN B CB  
5032 C CG  . ASN B 28  ? 0.41027 0.36500 0.38143 0.06001  0.04613  -0.04342 28  ASN B CG  
5033 O OD1 . ASN B 28  ? 0.41672 0.35276 0.38005 0.05873  0.04555  -0.04640 28  ASN B OD1 
5034 N ND2 . ASN B 28  ? 0.39169 0.36211 0.37307 0.06561  0.04704  -0.03865 28  ASN B ND2 
5041 N N   . GLY B 29  ? 0.40829 0.36084 0.35223 0.04932  0.04849  -0.05567 29  GLY B N   
5042 C CA  . GLY B 29  ? 0.39546 0.35619 0.33594 0.04442  0.04744  -0.05656 29  GLY B CA  
5043 C C   . GLY B 29  ? 0.39191 0.35444 0.33633 0.03490  0.04153  -0.05546 29  GLY B C   
5044 O O   . GLY B 29  ? 0.39662 0.35065 0.34290 0.03122  0.03883  -0.05632 29  GLY B O   
5048 N N   . LEU B 30  ? 0.37055 0.34466 0.31548 0.03150  0.03976  -0.05338 30  LEU B N   
5049 C CA  . LEU B 30  ? 0.36040 0.33894 0.30863 0.02452  0.03430  -0.05168 30  LEU B CA  
5050 C C   . LEU B 30  ? 0.36628 0.34427 0.30268 0.02086  0.03320  -0.05694 30  LEU B C   
5051 O O   . LEU B 30  ? 0.38498 0.36986 0.31600 0.02273  0.03504  -0.05657 30  LEU B O   
5052 C CB  . LEU B 30  ? 0.33007 0.32161 0.28730 0.02441  0.03302  -0.04404 30  LEU B CB  
5053 C CG  . LEU B 30  ? 0.31630 0.31223 0.27619 0.01963  0.02775  -0.04137 30  LEU B CG  
5054 C CD1 . LEU B 30  ? 0.35778 0.34839 0.32489 0.01725  0.02482  -0.04144 30  LEU B CD1 
5055 C CD2 . LEU B 30  ? 0.33067 0.33554 0.29464 0.02035  0.02798  -0.03392 30  LEU B CD2 
5067 N N   . TRP B 31  ? 0.38652 0.35707 0.31822 0.01511  0.03044  -0.06206 31  TRP B N   
5068 C CA  . TRP B 31  ? 0.38306 0.35260 0.30240 0.01010  0.02927  -0.06857 31  TRP B CA  
5069 C C   . TRP B 31  ? 0.37850 0.36261 0.30176 0.00539  0.02351  -0.06597 31  TRP B C   
5070 O O   . TRP B 31  ? 0.37206 0.35785 0.30153 0.00128  0.01987  -0.06535 31  TRP B O   
5071 C CB  . TRP B 31  ? 0.41395 0.36664 0.32468 0.00527  0.03000  -0.07604 31  TRP B CB  
5072 C CG  . TRP B 31  ? 0.43082 0.38130 0.32768 -0.00199 0.02885  -0.08390 31  TRP B CG  
5073 C CD1 . TRP B 31  ? 0.43831 0.39780 0.32744 -0.00224 0.02859  -0.08586 31  TRP B CD1 
5074 C CD2 . TRP B 31  ? 0.45522 0.39411 0.34361 -0.01129 0.02775  -0.09103 31  TRP B CD2 
5075 N NE1 . TRP B 31  ? 0.43971 0.39479 0.31618 -0.01103 0.02713  -0.09419 31  TRP B NE1 
5076 C CE2 . TRP B 31  ? 0.50186 0.44400 0.37755 -0.01728 0.02674  -0.09761 31  TRP B CE2 
5077 C CE3 . TRP B 31  ? 0.45198 0.37785 0.34146 -0.01577 0.02775  -0.09246 31  TRP B CE3 
5078 C CZ2 . TRP B 31  ? 0.52727 0.46089 0.39168 -0.02872 0.02558  -0.10591 31  TRP B CZ2 
5079 C CZ3 . TRP B 31  ? 0.51443 0.43059 0.39240 -0.02684 0.02703  -0.10020 31  TRP B CZ3 
5080 C CH2 . TRP B 31  ? 0.51313 0.43326 0.37870 -0.03371 0.02597  -0.10709 31  TRP B CH2 
5091 N N   . LEU B 32  ? 0.39184 0.38700 0.31136 0.00701  0.02295  -0.06387 32  LEU B N   
5092 C CA  . LEU B 32  ? 0.41526 0.42489 0.33663 0.00512  0.01782  -0.06046 32  LEU B CA  
5093 C C   . LEU B 32  ? 0.38458 0.40053 0.29327 0.00270  0.01689  -0.06523 32  LEU B C   
5094 O O   . LEU B 32  ? 0.37619 0.39014 0.27725 0.00580  0.02074  -0.06625 32  LEU B O   
5095 C CB  . LEU B 32  ? 0.37474 0.39141 0.30304 0.01048  0.01801  -0.05113 32  LEU B CB  
5096 C CG  . LEU B 32  ? 0.36636 0.37818 0.30679 0.01239  0.01879  -0.04616 32  LEU B CG  
5097 C CD1 . LEU B 32  ? 0.39052 0.40682 0.33395 0.01630  0.02044  -0.03799 32  LEU B CD1 
5098 C CD2 . LEU B 32  ? 0.35368 0.36756 0.30089 0.00937  0.01406  -0.04577 32  LEU B CD2 
5110 N N   . ASP B 33  ? 0.38763 0.41292 0.29395 -0.00286 0.01185  -0.06829 33  ASP B N   
5111 C CA  . ASP B 33  ? 0.41336 0.44580 0.30680 -0.00633 0.01053  -0.07384 33  ASP B CA  
5112 C C   . ASP B 33  ? 0.40218 0.41806 0.28462 -0.00822 0.01577  -0.08179 33  ASP B C   
5113 O O   . ASP B 33  ? 0.44267 0.44369 0.32591 -0.01086 0.01788  -0.08561 33  ASP B O   
5114 C CB  . ASP B 33  ? 0.40633 0.45137 0.29721 -0.00043 0.00966  -0.06729 33  ASP B CB  
5115 C CG  . ASP B 33  ? 0.44890 0.50730 0.34811 0.00234  0.00454  -0.05975 33  ASP B CG  
5116 O OD1 . ASP B 33  ? 0.45516 0.52503 0.35547 -0.00179 -0.00060 -0.06235 33  ASP B OD1 
5117 O OD2 . ASP B 33  ? 0.49739 0.55409 0.40191 0.00851  0.00602  -0.05143 33  ASP B OD2 
5122 N N   . ASP B 34  ? 0.40523 0.42155 0.27636 -0.00623 0.01837  -0.08430 34  ASP B N   
5123 C CA  . ASP B 34  ? 0.44669 0.44572 0.30573 -0.00690 0.02374  -0.09231 34  ASP B CA  
5124 C C   . ASP B 34  ? 0.45338 0.44521 0.31374 0.00266  0.03025  -0.08869 34  ASP B C   
5125 O O   . ASP B 34  ? 0.48883 0.47239 0.33705 0.00514  0.03501  -0.09394 34  ASP B O   
5126 C CB  . ASP B 34  ? 0.48322 0.48583 0.32591 -0.01253 0.02269  -0.10026 34  ASP B CB  
5127 C CG  . ASP B 34  ? 0.56163 0.58065 0.40099 -0.00790 0.02188  -0.09567 34  ASP B CG  
5128 O OD1 . ASP B 34  ? 0.52458 0.55266 0.37433 -0.00154 0.02143  -0.08592 34  ASP B OD1 
5129 O OD2 . ASP B 34  ? 0.58030 0.60155 0.40515 -0.01102 0.02202  -0.10201 34  ASP B OD2 
5134 N N   . VAL B 35  ? 0.48754 0.48295 0.36211 0.00792  0.03074  -0.08017 35  VAL B N   
5135 C CA  . VAL B 35  ? 0.45739 0.44990 0.33539 0.01612  0.03664  -0.07631 35  VAL B CA  
5136 C C   . VAL B 35  ? 0.41895 0.40402 0.30918 0.01842  0.03749  -0.07314 35  VAL B C   
5137 O O   . VAL B 35  ? 0.37935 0.36755 0.27954 0.01518  0.03315  -0.06951 35  VAL B O   
5138 C CB  . VAL B 35  ? 0.46585 0.47354 0.34801 0.01971  0.03689  -0.06800 35  VAL B CB  
5139 C CG1 . VAL B 35  ? 0.46117 0.46881 0.34917 0.02663  0.04294  -0.06380 35  VAL B CG1 
5140 C CG2 . VAL B 35  ? 0.52235 0.53735 0.39070 0.01864  0.03677  -0.07089 35  VAL B CG2 
5150 N N   . VAL B 36  ? 0.43672 0.41315 0.32586 0.02483  0.04315  -0.07434 36  VAL B N   
5151 C CA  . VAL B 36  ? 0.42963 0.40140 0.33004 0.02871  0.04447  -0.07062 36  VAL B CA  
5152 C C   . VAL B 36  ? 0.37879 0.36306 0.28724 0.03520  0.04806  -0.06387 36  VAL B C   
5153 O O   . VAL B 36  ? 0.41377 0.40057 0.31537 0.04033  0.05294  -0.06556 36  VAL B O   
5154 C CB  . VAL B 36  ? 0.46605 0.41811 0.35801 0.03170  0.04812  -0.07719 36  VAL B CB  
5155 C CG1 . VAL B 36  ? 0.47357 0.42273 0.37681 0.03751  0.04970  -0.07263 36  VAL B CG1 
5156 C CG2 . VAL B 36  ? 0.50353 0.44304 0.38684 0.02228  0.04449  -0.08394 36  VAL B CG2 
5166 N N   . TYR B 37  ? 0.38314 0.37564 0.30529 0.03424  0.04579  -0.05654 37  TYR B N   
5167 C CA  . TYR B 37  ? 0.39109 0.39624 0.32178 0.03771  0.04870  -0.04978 37  TYR B CA  
5168 C C   . TYR B 37  ? 0.39610 0.39917 0.33501 0.04294  0.05126  -0.04881 37  TYR B C   
5169 O O   . TYR B 37  ? 0.35935 0.35441 0.30323 0.04131  0.04834  -0.04904 37  TYR B O   
5170 C CB  . TYR B 37  ? 0.36190 0.37515 0.30059 0.03259  0.04459  -0.04261 37  TYR B CB  
5171 C CG  . TYR B 37  ? 0.38653 0.40311 0.31689 0.02902  0.04177  -0.04246 37  TYR B CG  
5172 C CD1 . TYR B 37  ? 0.38434 0.39608 0.31056 0.02513  0.03688  -0.04627 37  TYR B CD1 
5173 C CD2 . TYR B 37  ? 0.38206 0.40801 0.30778 0.02968  0.04432  -0.03865 37  TYR B CD2 
5174 C CE1 . TYR B 37  ? 0.43465 0.45251 0.35281 0.02272  0.03391  -0.04604 37  TYR B CE1 
5175 C CE2 . TYR B 37  ? 0.42981 0.45924 0.34639 0.02743  0.04166  -0.03804 37  TYR B CE2 
5176 C CZ  . TYR B 37  ? 0.44564 0.47158 0.35893 0.02442  0.03618  -0.04171 37  TYR B CZ  
5177 O OH  . TYR B 37  ? 0.46119 0.49313 0.36577 0.02300  0.03307  -0.04103 37  TYR B OH  
5187 N N   . CYS B 38  ? 0.41566 0.42776 0.35620 0.04933  0.05658  -0.04741 38  CYS B N   
5188 C CA  . CYS B 38  ? 0.41739 0.43174 0.36664 0.05520  0.05870  -0.04566 38  CYS B CA  
5189 C C   . CYS B 38  ? 0.43188 0.46583 0.38687 0.05921  0.06348  -0.04150 38  CYS B C   
5190 O O   . CYS B 38  ? 0.42264 0.46520 0.37268 0.05808  0.06594  -0.04088 38  CYS B O   
5191 C CB  . CYS B 38  ? 0.44468 0.44242 0.38508 0.06231  0.06104  -0.05212 38  CYS B CB  
5192 S SG  . CYS B 38  ? 0.50034 0.49561 0.42576 0.07149  0.06807  -0.05816 38  CYS B SG  
5198 N N   . PRO B 39  ? 0.39488 0.43805 0.36040 0.06347  0.06488  -0.03840 39  PRO B N   
5199 C CA  . PRO B 39  ? 0.38245 0.44811 0.35462 0.06620  0.06943  -0.03449 39  PRO B CA  
5200 C C   . PRO B 39  ? 0.43764 0.50625 0.40032 0.07586  0.07560  -0.03888 39  PRO B C   
5201 O O   . PRO B 39  ? 0.44964 0.50297 0.40343 0.08381  0.07701  -0.04449 39  PRO B O   
5202 C CB  . PRO B 39  ? 0.36189 0.43548 0.34622 0.06964  0.06883  -0.03160 39  PRO B CB  
5203 C CG  . PRO B 39  ? 0.34714 0.40456 0.33386 0.06363  0.06261  -0.03133 39  PRO B CG  
5204 C CD  . PRO B 39  ? 0.41208 0.44837 0.38503 0.06401  0.06166  -0.03743 39  PRO B CD  
5212 N N   . ARG B 40  ? 0.40957 0.49654 0.37271 0.07499  0.07967  -0.03642 40  ARG B N   
5213 C CA  . ARG B 40  ? 0.43930 0.52949 0.39242 0.08463  0.08592  -0.04096 40  ARG B CA  
5214 C C   . ARG B 40  ? 0.52403 0.62233 0.48102 0.09784  0.09017  -0.04211 40  ARG B C   
5215 O O   . ARG B 40  ? 0.52412 0.61750 0.47038 0.10877  0.09507  -0.04728 40  ARG B O   
5216 C CB  . ARG B 40  ? 0.47491 0.58385 0.42694 0.08058  0.08974  -0.03793 40  ARG B CB  
5217 C CG  . ARG B 40  ? 0.46841 0.60363 0.43425 0.07716  0.09187  -0.03122 40  ARG B CG  
5218 C CD  . ARG B 40  ? 0.50536 0.65705 0.46744 0.07324  0.09657  -0.02875 40  ARG B CD  
5219 N NE  . ARG B 40  ? 0.43951 0.61674 0.41452 0.06774  0.09876  -0.02239 40  ARG B NE  
5220 C CZ  . ARG B 40  ? 0.48991 0.68721 0.46468 0.06322  0.10378  -0.01895 40  ARG B CZ  
5221 N NH1 . ARG B 40  ? 0.51610 0.71075 0.47818 0.06375  0.10697  -0.02069 40  ARG B NH1 
5222 N NH2 . ARG B 40  ? 0.44865 0.66975 0.43559 0.05721  0.10571  -0.01371 40  ARG B NH2 
5236 N N   . ALA B 41  ? 0.48355 0.59296 0.45444 0.09774  0.08824  -0.03762 41  ALA B N   
5237 C CA  . ALA B 41  ? 0.53826 0.65569 0.51306 0.11129  0.09134  -0.03813 41  ALA B CA  
5238 C C   . ALA B 41  ? 0.58229 0.67133 0.54459 0.12126  0.09130  -0.04398 41  ALA B C   
5239 O O   . ALA B 41  ? 0.68199 0.77375 0.64347 0.13527  0.09470  -0.04485 41  ALA B O   
5240 C CB  . ALA B 41  ? 0.62109 0.75435 0.61250 0.10749  0.08799  -0.03230 41  ALA B CB  
5246 N N   . VAL B 42  ? 0.54668 0.60877 0.49852 0.11460  0.08771  -0.04788 42  VAL B N   
5247 C CA  . VAL B 42  ? 0.55843 0.59185 0.49570 0.12270  0.08862  -0.05400 42  VAL B CA  
5248 C C   . VAL B 42  ? 0.70946 0.73886 0.63217 0.13556  0.09582  -0.05949 42  VAL B C   
5249 O O   . VAL B 42  ? 0.71244 0.72208 0.62336 0.14703  0.09867  -0.06362 42  VAL B O   
5250 C CB  . VAL B 42  ? 0.63173 0.63997 0.56034 0.11119  0.08358  -0.05764 42  VAL B CB  
5251 C CG1 . VAL B 42  ? 0.56441 0.56966 0.48152 0.10593  0.08487  -0.06192 42  VAL B CG1 
5252 C CG2 . VAL B 42  ? 0.59195 0.57075 0.50881 0.11648  0.08346  -0.06226 42  VAL B CG2 
5262 N N   . ILE B 43  ? 0.65405 0.70081 0.57602 0.13449  0.09930  -0.05955 43  ILE B N   
5263 C CA  . ILE B 43  ? 0.76697 0.80928 0.67402 0.14729  0.10646  -0.06530 43  ILE B CA  
5264 C C   . ILE B 43  ? 0.75894 0.82312 0.67248 0.16335  0.11217  -0.06283 43  ILE B C   
5265 O O   . ILE B 43  ? 0.89883 0.95536 0.79890 0.17787  0.11840  -0.06777 43  ILE B O   
5266 C CB  . ILE B 43  ? 0.77785 0.82938 0.67878 0.14116  0.10872  -0.06710 43  ILE B CB  
5267 C CG1 . ILE B 43  ? 0.76946 0.85753 0.68633 0.13778  0.11038  -0.06002 43  ILE B CG1 
5268 C CG2 . ILE B 43  ? 0.76131 0.79584 0.65620 0.12608  0.10288  -0.06911 43  ILE B CG2 
5269 C CD1 . ILE B 43  ? 0.85023 0.94774 0.75924 0.13410  0.11393  -0.06151 43  ILE B CD1 
5281 N N   . CYS B 44  ? 0.91164 1.00182 0.84455 0.16162  0.11011  -0.05566 44  CYS B N   
5282 C CA  . CYS B 44  ? 0.95351 1.07125 0.89564 0.17587  0.11472  -0.05249 44  CYS B CA  
5283 C C   . CYS B 44  ? 0.93618 1.03599 0.87035 0.19316  0.11633  -0.05463 44  CYS B C   
5284 O O   . CYS B 44  ? 0.88815 0.98241 0.82929 0.19217  0.11175  -0.05143 44  CYS B O   
5285 C CB  . CYS B 44  ? 0.94435 1.09377 0.90892 0.16623  0.11107  -0.04454 44  CYS B CB  
5286 S SG  . CYS B 44  ? 1.18856 1.36342 1.16235 0.14770  0.11088  -0.04040 44  CYS B SG  
5292 N N   . PRO B 52  ? 1.00938 1.41956 1.05759 0.14402  0.12918  -0.01611 52  PRO B N   
5293 C CA  . PRO B 52  ? 1.05514 1.45726 1.09292 0.13678  0.13378  -0.01772 52  PRO B CA  
5294 C C   . PRO B 52  ? 1.05601 1.42268 1.07569 0.14975  0.13538  -0.02414 52  PRO B C   
5295 O O   . PRO B 52  ? 1.08347 1.44708 1.09497 0.16355  0.13837  -0.02750 52  PRO B O   
5296 C CB  . PRO B 52  ? 1.11833 1.55107 1.15972 0.13559  0.13800  -0.01591 52  PRO B CB  
5297 C CG  . PRO B 52  ? 1.08063 1.54010 1.13562 0.14148  0.13508  -0.01317 52  PRO B CG  
5298 C CD  . PRO B 52  ? 1.08450 1.53360 1.14627 0.13880  0.12914  -0.01181 52  PRO B CD  
5306 N N   . ASN B 53  ? 0.99898 1.33878 1.01161 0.14489  0.13335  -0.02604 53  ASN B N   
5307 C CA  . ASN B 53  ? 0.99704 1.30064 0.99059 0.15476  0.13438  -0.03287 53  ASN B CA  
5308 C C   . ASN B 53  ? 0.99358 1.29179 0.97652 0.14456  0.13707  -0.03390 53  ASN B C   
5309 O O   . ASN B 53  ? 0.97882 1.28269 0.96764 0.12645  0.13422  -0.02887 53  ASN B O   
5310 C CB  . ASN B 53  ? 0.95560 1.22638 0.94655 0.15351  0.12746  -0.03420 53  ASN B CB  
5311 C CG  . ASN B 53  ? 1.04536 1.32914 1.05330 0.14134  0.12171  -0.02806 53  ASN B CG  
5312 O OD1 . ASN B 53  ? 1.04992 1.36179 1.07077 0.14715  0.12272  -0.02513 53  ASN B OD1 
5313 N ND2 . ASN B 53  ? 1.09763 1.36272 1.10541 0.12478  0.11575  -0.02614 53  ASN B ND2 
5320 N N   . TYR B 54  ? 1.05816 1.34320 1.02537 0.15456  0.14131  -0.03968 54  TYR B N   
5321 C CA  . TYR B 54  ? 1.12498 1.40298 1.07975 0.14580  0.14359  -0.04115 54  TYR B CA  
5322 C C   . TYR B 54  ? 1.08563 1.32182 1.02678 0.14280  0.13780  -0.04579 54  TYR B C   
5323 O O   . TYR B 54  ? 1.05608 1.27172 0.98060 0.15315  0.14039  -0.05306 54  TYR B O   
5324 C CB  . TYR B 54  ? 1.19928 1.48573 1.14567 0.15453  0.14954  -0.04425 54  TYR B CB  
5325 C CG  . TYR B 54  ? 1.31899 1.64406 1.27916 0.14931  0.15261  -0.03822 54  TYR B CG  
5326 C CD1 . TYR B 54  ? 1.31065 1.65678 1.28355 0.15777  0.15249  -0.03611 54  TYR B CD1 
5327 C CD2 . TYR B 54  ? 1.28194 1.62211 1.24143 0.13536  0.15537  -0.03440 54  TYR B CD2 
5328 C CE1 . TYR B 54  ? 1.23679 1.61916 1.22190 0.15206  0.15492  -0.03104 54  TYR B CE1 
5329 C CE2 . TYR B 54  ? 1.28301 1.65691 1.25409 0.12899  0.15819  -0.02907 54  TYR B CE2 
5330 C CZ  . TYR B 54  ? 1.27717 1.67298 1.26146 0.13710  0.15789  -0.02770 54  TYR B CZ  
5331 O OH  . TYR B 54  ? 1.25007 1.68025 1.24544 0.13004  0.16035  -0.02286 54  TYR B OH  
5341 N N   . GLU B 55  ? 0.94922 1.17299 0.89680 0.12893  0.13017  -0.04201 55  GLU B N   
5342 C CA  . GLU B 55  ? 0.90053 1.08718 0.83662 0.12632  0.12438  -0.04650 55  GLU B CA  
5343 C C   . GLU B 55  ? 0.92507 1.09700 0.84256 0.12570  0.12645  -0.05185 55  GLU B C   
5344 O O   . GLU B 55  ? 0.94139 1.08659 0.84466 0.13175  0.12573  -0.05905 55  GLU B O   
5345 C CB  . GLU B 55  ? 0.74989 0.92716 0.69453 0.11091  0.11622  -0.04152 55  GLU B CB  
5346 C CG  . GLU B 55  ? 0.67331 0.84543 0.62943 0.11292  0.11156  -0.03988 55  GLU B CG  
5347 C CD  . GLU B 55  ? 0.67560 0.87665 0.64985 0.10838  0.11164  -0.03298 55  GLU B CD  
5348 O OE1 . GLU B 55  ? 0.69868 0.92116 0.67685 0.10030  0.11453  -0.02884 55  GLU B OE1 
5349 O OE2 . GLU B 55  ? 0.68101 0.88288 0.66478 0.11159  0.10867  -0.03161 55  GLU B OE2 
5356 N N   . ASP B 56  ? 0.95677 1.14546 0.87281 0.11816  0.12930  -0.04862 56  ASP B N   
5357 C CA  . ASP B 56  ? 1.02005 1.19618 0.91781 0.11747  0.13101  -0.05355 56  ASP B CA  
5358 C C   . ASP B 56  ? 1.07012 1.23901 0.95413 0.13378  0.13726  -0.06213 56  ASP B C   
5359 O O   . ASP B 56  ? 1.10285 1.24593 0.96988 0.13542  0.13610  -0.06941 56  ASP B O   
5360 C CB  . ASP B 56  ? 1.00644 1.20426 0.90437 0.10843  0.13427  -0.04803 56  ASP B CB  
5361 C CG  . ASP B 56  ? 1.08352 1.26927 0.96233 0.10696  0.13532  -0.05250 56  ASP B CG  
5362 O OD1 . ASP B 56  ? 1.08238 1.24673 0.95399 0.09921  0.12877  -0.05359 56  ASP B OD1 
5363 O OD2 . ASP B 56  ? 1.09933 1.29912 0.97047 0.11354  0.14272  -0.05480 56  ASP B OD2 
5368 N N   . LEU B 57  ? 1.06418 1.25641 0.95526 0.14559  0.14385  -0.06128 57  LEU B N   
5369 C CA  . LEU B 57  ? 1.08783 1.27363 0.96574 0.16294  0.15037  -0.06890 57  LEU B CA  
5370 C C   . LEU B 57  ? 1.08380 1.23766 0.95492 0.17137  0.14723  -0.07441 57  LEU B C   
5371 O O   . LEU B 57  ? 1.14514 1.27575 1.00015 0.17899  0.14895  -0.08164 57  LEU B O   
5372 C CB  . LEU B 57  ? 1.03640 1.25303 0.92861 0.16915  0.15423  -0.06422 57  LEU B CB  
5373 C CG  . LEU B 57  ? 0.94282 1.17777 0.83051 0.16807  0.15973  -0.06395 57  LEU B CG  
5374 C CD1 . LEU B 57  ? 0.97176 1.22902 0.86900 0.17906  0.16338  -0.06223 57  LEU B CD1 
5375 C CD2 . LEU B 57  ? 0.94732 1.15578 0.81204 0.17040  0.16130  -0.07223 57  LEU B CD2 
5387 N N   . LEU B 58  ? 1.01194 1.16135 0.89517 0.16678  0.14141  -0.07047 58  LEU B N   
5388 C CA  . LEU B 58  ? 1.03021 1.15008 0.90671 0.17543  0.13916  -0.07505 58  LEU B CA  
5389 C C   . LEU B 58  ? 1.09652 1.18010 0.95710 0.16620  0.13414  -0.08104 58  LEU B C   
5390 O O   . LEU B 58  ? 1.10782 1.16265 0.95548 0.17407  0.13450  -0.08714 58  LEU B O   
5391 C CB  . LEU B 58  ? 0.99613 1.12587 0.89191 0.17404  0.13463  -0.06836 58  LEU B CB  
5392 C CG  . LEU B 58  ? 1.06153 1.21141 0.96753 0.18832  0.13798  -0.06542 58  LEU B CG  
5393 C CD1 . LEU B 58  ? 0.96860 1.14505 0.89653 0.18332  0.13500  -0.05755 58  LEU B CD1 
5394 C CD2 . LEU B 58  ? 1.06990 1.18867 0.96433 0.20065  0.13725  -0.06991 58  LEU B CD2 
5406 N N   . ILE B 59  ? 1.12181 1.20632 0.98174 0.15065  0.12999  -0.07956 59  ILE B N   
5407 C CA  . ILE B 59  ? 1.15606 1.20958 1.00231 0.14128  0.12443  -0.08518 59  ILE B CA  
5408 C C   . ILE B 59  ? 1.15647 1.19418 0.97927 0.14641  0.12918  -0.09463 59  ILE B C   
5409 O O   . ILE B 59  ? 1.13421 1.16029 0.94681 0.13553  0.12536  -0.09797 59  ILE B O   
5410 C CB  . ILE B 59  ? 1.12377 1.18164 0.97788 0.12363  0.11691  -0.07999 59  ILE B CB  
5411 C CG1 . ILE B 59  ? 1.08040 1.14511 0.95414 0.11749  0.11132  -0.07233 59  ILE B CG1 
5412 C CG2 . ILE B 59  ? 1.13167 1.16425 0.96973 0.11553  0.11251  -0.08673 59  ILE B CG2 
5413 C CD1 . ILE B 59  ? 1.01849 1.09063 0.89963 0.10245  0.10540  -0.06629 59  ILE B CD1 
5425 N N   . ARG B 60  ? 1.24034 1.27747 1.05418 0.16279  0.13711  -0.09900 60  ARG B N   
5426 C CA  . ARG B 60  ? 1.25075 1.26857 1.04066 0.16811  0.14177  -0.10880 60  ARG B CA  
5427 C C   . ARG B 60  ? 1.28181 1.26060 1.05830 0.16913  0.13931  -0.11567 60  ARG B C   
5428 O O   . ARG B 60  ? 1.33722 1.29536 1.09722 0.17287  0.14196  -0.12292 60  ARG B O   
5429 C CB  . ARG B 60  ? 1.32354 1.35799 1.11688 0.17967  0.14797  -0.10757 60  ARG B CB  
5430 C CG  . ARG B 60  ? 1.52264 1.57859 1.31268 0.17624  0.15170  -0.10722 60  ARG B CG  
5431 C CD  . ARG B 60  ? 1.53196 1.62532 1.34072 0.17056  0.15193  -0.09755 60  ARG B CD  
5432 N NE  . ARG B 60  ? 1.48469 1.57777 1.29543 0.15619  0.14614  -0.09462 60  ARG B NE  
5433 C CZ  . ARG B 60  ? 1.45920 1.57609 1.28026 0.14532  0.14473  -0.08695 60  ARG B CZ  
5434 N NH1 . ARG B 60  ? 1.40631 1.55309 1.23329 0.14964  0.15140  -0.08292 60  ARG B NH1 
5435 N NH2 . ARG B 60  ? 1.41396 1.52459 1.23881 0.13030  0.13688  -0.08314 60  ARG B NH2 
5449 N N   . LYS B 61  ? 1.13825 1.10772 0.92261 0.16438  0.13409  -0.11287 61  LYS B N   
5450 C CA  . LYS B 61  ? 1.04743 0.97917 0.81836 0.16366  0.13187  -0.11892 61  LYS B CA  
5451 C C   . LYS B 61  ? 1.00573 0.91846 0.76174 0.14832  0.12749  -0.12571 61  LYS B C   
5452 O O   . LYS B 61  ? 0.99564 0.92698 0.75700 0.13766  0.12425  -0.12334 61  LYS B O   
5453 C CB  . LYS B 61  ? 1.02249 0.95355 0.81010 0.15983  0.12616  -0.11239 61  LYS B CB  
5454 C CG  . LYS B 61  ? 1.06489 1.03085 0.87797 0.16357  0.12571  -0.10193 61  LYS B CG  
5455 C CD  . LYS B 61  ? 1.02793 0.98996 0.84605 0.17771  0.12789  -0.09934 61  LYS B CD  
5456 C CE  . LYS B 61  ? 1.11587 1.11248 0.96003 0.17808  0.12592  -0.08921 61  LYS B CE  
5457 N NZ  . LYS B 61  ? 1.07549 1.08190 0.92524 0.19456  0.12971  -0.08627 61  LYS B NZ  
5471 N N   . SER B 62  ? 0.96261 0.84005 0.70125 0.14636  0.12693  -0.13326 62  SER B N   
5472 C CA  . SER B 62  ? 0.91574 0.77570 0.63994 0.13068  0.12248  -0.14034 62  SER B CA  
5473 C C   . SER B 62  ? 0.88485 0.74464 0.62376 0.11664  0.11368  -0.13547 62  SER B C   
5474 O O   . SER B 62  ? 0.86295 0.72857 0.61841 0.12039  0.11204  -0.12829 62  SER B O   
5475 C CB  . SER B 62  ? 0.90195 0.72811 0.60441 0.13018  0.12447  -0.15004 62  SER B CB  
5476 O OG  . SER B 62  ? 0.87835 0.67900 0.57958 0.12829  0.12207  -0.15019 62  SER B OG  
5482 N N   . ASN B 63  ? 0.84884 0.70557 0.58244 0.10051  0.10786  -0.13911 63  ASN B N   
5483 C CA  . ASN B 63  ? 0.83836 0.69434 0.58370 0.08710  0.09973  -0.13565 63  ASN B CA  
5484 C C   . ASN B 63  ? 0.83739 0.66583 0.57859 0.08950  0.10039  -0.13727 63  ASN B C   
5485 O O   . ASN B 63  ? 0.80998 0.64377 0.56773 0.08537  0.09563  -0.13079 63  ASN B O   
5486 C CB  . ASN B 63  ? 0.81249 0.66610 0.54762 0.07090  0.09438  -0.14161 63  ASN B CB  
5487 C CG  . ASN B 63  ? 0.79036 0.67425 0.53339 0.06723  0.09181  -0.13722 63  ASN B CG  
5488 O OD1 . ASN B 63  ? 0.79664 0.70478 0.55934 0.07022  0.09050  -0.12730 63  ASN B OD1 
5489 N ND2 . ASN B 63  ? 0.76721 0.64883 0.49374 0.06034  0.09117  -0.14452 63  ASN B ND2 
5496 N N   . HIS B 64  ? 0.88973 0.68693 0.60746 0.09627  0.10650  -0.14585 64  HIS B N   
5497 C CA  . HIS B 64  ? 0.91904 0.68576 0.62896 0.09851  0.10769  -0.14748 64  HIS B CA  
5498 C C   . HIS B 64  ? 0.86802 0.64246 0.59274 0.11453  0.11035  -0.13896 64  HIS B C   
5499 O O   . HIS B 64  ? 0.87859 0.63542 0.60442 0.11497  0.10903  -0.13679 64  HIS B O   
5500 C CB  . HIS B 64  ? 0.90912 0.64752 0.59917 0.09799  0.11013  -0.15516 64  HIS B CB  
5501 C CG  . HIS B 64  ? 0.97669 0.70043 0.65188 0.07924  0.10616  -0.16374 64  HIS B CG  
5502 N ND1 . HIS B 64  ? 0.98016 0.68776 0.65359 0.06527  0.10148  -0.16496 64  HIS B ND1 
5503 C CD2 . HIS B 64  ? 1.01245 0.73707 0.67419 0.07185  0.10603  -0.17144 64  HIS B CD2 
5504 C CE1 . HIS B 64  ? 1.02560 0.72696 0.68632 0.04966  0.09840  -0.17286 64  HIS B CE1 
5505 N NE2 . HIS B 64  ? 1.05766 0.76862 0.71074 0.05351  0.10092  -0.17704 64  HIS B NE2 
5513 N N   A ASN B 65  ? 0.83847 0.64191 0.57660 0.12620  0.11319  -0.13323 65  ASN B N   
5514 N N   B ASN B 65  ? 0.83644 0.64003 0.57466 0.12593  0.11309  -0.13323 65  ASN B N   
5515 C CA  A ASN B 65  ? 0.80180 0.61913 0.55661 0.13981  0.11481  -0.12470 65  ASN B CA  
5516 C CA  B ASN B 65  ? 0.80421 0.62182 0.55873 0.13992  0.11495  -0.12484 65  ASN B CA  
5517 C C   A ASN B 65  ? 0.83424 0.66651 0.61218 0.13019  0.10728  -0.11627 65  ASN B C   
5518 C C   B ASN B 65  ? 0.83280 0.66769 0.61164 0.13072  0.10747  -0.11597 65  ASN B C   
5519 O O   A ASN B 65  ? 0.79836 0.63367 0.58677 0.13888  0.10757  -0.11041 65  ASN B O   
5520 O O   B ASN B 65  ? 0.80023 0.64157 0.59089 0.14005  0.10797  -0.10968 65  ASN B O   
5521 C CB  A ASN B 65  ? 0.83816 0.68760 0.60336 0.15144  0.11914  -0.12057 65  ASN B CB  
5522 C CB  B ASN B 65  ? 0.84466 0.69208 0.60716 0.15212  0.11984  -0.12161 65  ASN B CB  
5523 C CG  A ASN B 65  ? 0.86534 0.70675 0.61794 0.16092  0.12439  -0.12491 65  ASN B CG  
5524 C CG  B ASN B 65  ? 0.84515 0.72324 0.63294 0.15884  0.11880  -0.11113 65  ASN B CG  
5525 O OD1 A ASN B 65  ? 0.85062 0.69704 0.59416 0.15835  0.12657  -0.12970 65  ASN B OD1 
5526 O OD1 B ASN B 65  ? 0.85372 0.76227 0.65964 0.15137  0.11548  -0.10509 65  ASN B OD1 
5527 N ND2 A ASN B 65  ? 0.86278 0.69065 0.61359 0.17183  0.12625  -0.12317 65  ASN B ND2 
5528 N ND2 B ASN B 65  ? 0.84354 0.71505 0.63443 0.17071  0.12041  -0.10788 65  ASN B ND2 
5541 N N   . PHE B 66  ? 0.78627 0.62865 0.57197 0.11334  0.10060  -0.11547 66  PHE B N   
5542 C CA  . PHE B 66  ? 0.75012 0.60592 0.55651 0.10425  0.09359  -0.10794 66  PHE B CA  
5543 C C   . PHE B 66  ? 0.79296 0.62159 0.58988 0.09341  0.09002  -0.11221 66  PHE B C   
5544 O O   . PHE B 66  ? 0.83059 0.65094 0.61714 0.08084  0.08738  -0.11823 66  PHE B O   
5545 C CB  . PHE B 66  ? 0.69556 0.57962 0.51624 0.09366  0.08860  -0.10359 66  PHE B CB  
5546 C CG  . PHE B 66  ? 0.70306 0.61448 0.53297 0.10158  0.09208  -0.09887 66  PHE B CG  
5547 C CD1 . PHE B 66  ? 0.72970 0.66320 0.57948 0.10646  0.09177  -0.09013 66  PHE B CD1 
5548 C CD2 . PHE B 66  ? 0.74492 0.66077 0.56306 0.10315  0.09579  -0.10336 66  PHE B CD2 
5549 C CE1 . PHE B 66  ? 0.71695 0.67697 0.57491 0.11199  0.09530  -0.08587 66  PHE B CE1 
5550 C CE2 . PHE B 66  ? 0.75497 0.69701 0.58117 0.10954  0.09945  -0.09883 66  PHE B CE2 
5551 C CZ  . PHE B 66  ? 0.77469 0.73907 0.62097 0.11349  0.09928  -0.09003 66  PHE B CZ  
5562 N N   . LEU B 67  ? 0.69134 0.50832 0.49222 0.09743  0.08970  -0.10885 67  LEU B N   
5563 C CA  . LEU B 67  ? 0.69890 0.49153 0.49216 0.08668  0.08657  -0.11178 67  LEU B CA  
5564 C C   . LEU B 67  ? 0.66252 0.47569 0.47764 0.07570  0.07904  -0.10498 67  LEU B C   
5565 O O   . LEU B 67  ? 0.64474 0.47435 0.47756 0.08165  0.07776  -0.09701 67  LEU B O   
5566 C CB  . LEU B 67  ? 0.74491 0.50971 0.52695 0.09748  0.09094  -0.11200 67  LEU B CB  
5567 C CG  . LEU B 67  ? 0.87918 0.62312 0.63933 0.11231  0.09925  -0.11780 67  LEU B CG  
5568 C CD1 . LEU B 67  ? 0.85664 0.62580 0.62921 0.13047  0.10296  -0.11187 67  LEU B CD1 
5569 C CD2 . LEU B 67  ? 0.98110 0.69146 0.72669 0.11346  0.10045  -0.11903 67  LEU B CD2 
5581 N N   . VAL B 68  ? 0.66093 0.47404 0.47430 0.05994  0.07412  -0.10834 68  VAL B N   
5582 C CA  . VAL B 68  ? 0.67553 0.50748 0.50764 0.04969  0.06707  -0.10266 68  VAL B CA  
5583 C C   . VAL B 68  ? 0.69996 0.51119 0.52464 0.03878  0.06470  -0.10616 68  VAL B C   
5584 O O   . VAL B 68  ? 0.70620 0.50066 0.51364 0.02963  0.06515  -0.11430 68  VAL B O   
5585 C CB  . VAL B 68  ? 0.60970 0.46432 0.44753 0.04146  0.06303  -0.10262 68  VAL B CB  
5586 C CG1 . VAL B 68  ? 0.56771 0.43970 0.42325 0.03194  0.05586  -0.09685 68  VAL B CG1 
5587 C CG2 . VAL B 68  ? 0.65001 0.52318 0.49292 0.05132  0.06617  -0.09927 68  VAL B CG2 
5597 N N   . GLN B 69  ? 0.62787 0.44020 0.46453 0.03905  0.06245  -0.10032 69  GLN B N   
5598 C CA  . GLN B 69  ? 0.68656 0.48014 0.51696 0.02884  0.06066  -0.10271 69  GLN B CA  
5599 C C   . GLN B 69  ? 0.65179 0.46697 0.50162 0.01998  0.05399  -0.09729 69  GLN B C   
5600 O O   . GLN B 69  ? 0.62387 0.45501 0.49082 0.02625  0.05239  -0.08961 69  GLN B O   
5601 C CB  . GLN B 69  ? 0.78380 0.55213 0.60555 0.03803  0.06510  -0.10148 69  GLN B CB  
5602 C CG  . GLN B 69  ? 0.91088 0.65528 0.71098 0.04810  0.07215  -0.10721 69  GLN B CG  
5603 C CD  . GLN B 69  ? 0.98876 0.70016 0.77340 0.05536  0.07681  -0.10755 69  GLN B CD  
5604 O OE1 . GLN B 69  ? 1.03092 0.73634 0.82017 0.05112  0.07463  -0.10384 69  GLN B OE1 
5605 N NE2 . GLN B 69  ? 1.09048 0.77947 0.85545 0.06710  0.08354  -0.11189 69  GLN B NE2 
5614 N N   . ALA B 70  ? 0.64678 0.46280 0.49311 0.00544  0.05029  -0.10164 70  ALA B N   
5615 C CA  . ALA B 70  ? 0.68974 0.52354 0.55129 -0.00366 0.04427  -0.09784 70  ALA B CA  
5616 C C   . ALA B 70  ? 0.77729 0.59049 0.63093 -0.01211 0.04465  -0.10032 70  ALA B C   
5617 O O   . ALA B 70  ? 0.72513 0.52443 0.56362 -0.02357 0.04515  -0.10775 70  ALA B O   
5618 C CB  . ALA B 70  ? 0.66490 0.51821 0.52830 -0.01305 0.03986  -0.10070 70  ALA B CB  
5624 N N   . GLY B 71  ? 0.71504 0.52629 0.57804 -0.00718 0.04456  -0.09417 71  GLY B N   
5625 C CA  . GLY B 71  ? 0.82769 0.61635 0.68123 -0.01359 0.04597  -0.09576 71  GLY B CA  
5626 C C   . GLY B 71  ? 0.87767 0.63242 0.70672 -0.01110 0.05222  -0.10186 71  GLY B C   
5627 O O   . GLY B 71  ? 0.91251 0.65799 0.73654 0.00331  0.05650  -0.10055 71  GLY B O   
5631 N N   . ASN B 72  ? 0.93701 0.67415 0.74983 -0.02550 0.05290  -0.10907 72  ASN B N   
5632 C CA  . ASN B 72  ? 0.99957 0.69849 0.78491 -0.02514 0.05932  -0.11580 72  ASN B CA  
5633 C C   . ASN B 72  ? 0.96587 0.66386 0.73846 -0.02953 0.06035  -0.12416 72  ASN B C   
5634 O O   . ASN B 72  ? 1.06986 0.73607 0.81778 -0.03189 0.06539  -0.13118 72  ASN B O   
5635 C CB  . ASN B 72  ? 1.08183 0.75667 0.85367 -0.03935 0.06043  -0.11874 72  ASN B CB  
5636 C CG  . ASN B 72  ? 1.20330 0.86755 0.97951 -0.03142 0.06175  -0.11114 72  ASN B CG  
5637 O OD1 . ASN B 72  ? 1.15806 0.83721 0.94983 -0.01626 0.06095  -0.10372 72  ASN B OD1 
5638 N ND2 . ASN B 72  ? 1.24962 0.89508 1.01585 -0.04133 0.06270  -0.11086 72  ASN B ND2 
5645 N N   . VAL B 73  ? 0.90038 0.63100 0.68808 -0.03050 0.05580  -0.12323 73  VAL B N   
5646 C CA  . VAL B 73  ? 0.89719 0.63063 0.67376 -0.03487 0.05614  -0.13074 73  VAL B CA  
5647 C C   . VAL B 73  ? 0.86290 0.60497 0.64333 -0.01783 0.05872  -0.12798 73  VAL B C   
5648 O O   . VAL B 73  ? 0.81608 0.58221 0.61716 -0.00850 0.05642  -0.11976 73  VAL B O   
5649 C CB  . VAL B 73  ? 0.91199 0.67628 0.69993 -0.04855 0.04926  -0.13211 73  VAL B CB  
5650 C CG1 . VAL B 73  ? 0.89232 0.66233 0.66960 -0.05070 0.04944  -0.13889 73  VAL B CG1 
5651 C CG2 . VAL B 73  ? 0.92513 0.68384 0.70854 -0.06671 0.04704  -0.13580 73  VAL B CG2 
5661 N N   . GLN B 74  ? 0.82343 0.54680 0.58350 -0.01471 0.06360  -0.13516 74  GLN B N   
5662 C CA  . GLN B 74  ? 0.86457 0.59798 0.62653 -0.00004 0.06642  -0.13374 74  GLN B CA  
5663 C C   . GLN B 74  ? 0.86904 0.62877 0.63578 -0.00756 0.06219  -0.13626 74  GLN B C   
5664 O O   . GLN B 74  ? 0.89572 0.65083 0.65002 -0.02197 0.06040  -0.14408 74  GLN B O   
5665 C CB  . GLN B 74  ? 0.95785 0.65719 0.69434 0.00902  0.07440  -0.14012 74  GLN B CB  
5666 C CG  . GLN B 74  ? 1.00719 0.71695 0.74466 0.02531  0.07828  -0.13891 74  GLN B CG  
5667 C CD  . GLN B 74  ? 1.12822 0.80683 0.84217 0.03537  0.08563  -0.14440 74  GLN B CD  
5668 O OE1 . GLN B 74  ? 1.20276 0.85729 0.90777 0.03294  0.08636  -0.14432 74  GLN B OE1 
5669 N NE2 . GLN B 74  ? 1.09644 0.78344 0.80674 0.04626  0.08925  -0.14615 74  GLN B NE2 
5678 N N   . LEU B 75  ? 0.79609 0.58474 0.58129 0.00096  0.06013  -0.12918 75  LEU B N   
5679 C CA  . LEU B 75  ? 0.74932 0.56275 0.53842 -0.00346 0.05659  -0.13014 75  LEU B CA  
5680 C C   . LEU B 75  ? 0.82134 0.62764 0.59530 0.00482  0.06206  -0.13510 75  LEU B C   
5681 O O   . LEU B 75  ? 0.86063 0.65894 0.63314 0.01922  0.06760  -0.13282 75  LEU B O   
5682 C CB  . LEU B 75  ? 0.72560 0.57093 0.53953 0.00094  0.05214  -0.11989 75  LEU B CB  
5683 C CG  . LEU B 75  ? 0.71794 0.57375 0.54698 -0.00704 0.04638  -0.11521 75  LEU B CG  
5684 C CD1 . LEU B 75  ? 0.62907 0.51430 0.47937 -0.00302 0.04219  -0.10586 75  LEU B CD1 
5685 C CD2 . LEU B 75  ? 0.71040 0.56526 0.53046 -0.02302 0.04260  -0.12229 75  LEU B CD2 
5697 N N   . ARG B 76  ? 0.77267 0.58345 0.53512 -0.00404 0.06049  -0.14200 76  ARG B N   
5698 C CA  . ARG B 76  ? 0.85824 0.66301 0.60487 0.00263  0.06554  -0.14750 76  ARG B CA  
5699 C C   . ARG B 76  ? 0.77570 0.61180 0.53755 0.01040  0.06416  -0.14021 76  ARG B C   
5700 O O   . ARG B 76  ? 0.73722 0.59745 0.50942 0.00300  0.05802  -0.13708 76  ARG B O   
5701 C CB  . ARG B 76  ? 0.84752 0.64177 0.57302 -0.01144 0.06454  -0.15882 76  ARG B CB  
5702 C CG  . ARG B 76  ? 0.94914 0.73742 0.65695 -0.00535 0.06957  -0.16520 76  ARG B CG  
5703 C CD  . ARG B 76  ? 1.04268 0.81373 0.72563 -0.01961 0.06959  -0.17788 76  ARG B CD  
5704 N NE  . ARG B 76  ? 1.13290 0.90755 0.80244 -0.01451 0.07285  -0.18289 76  ARG B NE  
5705 C CZ  . ARG B 76  ? 1.16836 0.92483 0.82529 -0.00024 0.08087  -0.18530 76  ARG B CZ  
5706 N NH1 . ARG B 76  ? 1.13786 0.87543 0.79758 0.01131  0.08519  -0.18146 76  ARG B NH1 
5707 N NH2 . ARG B 76  ? 1.13079 0.89409 0.77750 0.00365  0.08307  -0.18933 76  ARG B NH2 
5721 N N   . VAL B 77  ? 0.68477 0.52087 0.44785 0.02547  0.06997  -0.13705 77  VAL B N   
5722 C CA  . VAL B 77  ? 0.73894 0.60270 0.51430 0.03258  0.07000  -0.13028 77  VAL B CA  
5723 C C   . VAL B 77  ? 0.78804 0.65395 0.54669 0.03143  0.07212  -0.13708 77  VAL B C   
5724 O O   . VAL B 77  ? 0.81132 0.65573 0.54995 0.03548  0.07791  -0.14535 77  VAL B O   
5725 C CB  . VAL B 77  ? 0.73074 0.59716 0.51541 0.04822  0.07541  -0.12403 77  VAL B CB  
5726 C CG1 . VAL B 77  ? 0.62092 0.51493 0.41566 0.05406  0.07646  -0.11782 77  VAL B CG1 
5727 C CG2 . VAL B 77  ? 0.69890 0.56497 0.50033 0.04888  0.07274  -0.11707 77  VAL B CG2 
5737 N N   . ILE B 78  ? 0.71151 0.60184 0.47649 0.02601  0.06750  -0.13388 78  ILE B N   
5738 C CA  . ILE B 78  ? 0.69500 0.58912 0.44373 0.02419  0.06891  -0.14013 78  ILE B CA  
5739 C C   . ILE B 78  ? 0.72623 0.64404 0.48283 0.03247  0.07090  -0.13295 78  ILE B C   
5740 O O   . ILE B 78  ? 0.69752 0.62304 0.44263 0.03117  0.07157  -0.13636 78  ILE B O   
5741 C CB  . ILE B 78  ? 0.71851 0.61870 0.46087 0.00896  0.06188  -0.14503 78  ILE B CB  
5742 C CG1 . ILE B 78  ? 0.69045 0.61678 0.45354 0.00478  0.05438  -0.13521 78  ILE B CG1 
5743 C CG2 . ILE B 78  ? 0.73825 0.61285 0.46818 -0.00096 0.06130  -0.15407 78  ILE B CG2 
5744 C CD1 . ILE B 78  ? 0.70822 0.64857 0.46646 -0.00744 0.04732  -0.13853 78  ILE B CD1 
5756 N N   . GLY B 79  ? 0.68861 0.61860 0.46400 0.03988  0.07179  -0.12304 79  GLY B N   
5757 C CA  . GLY B 79  ? 0.71778 0.66869 0.49996 0.04710  0.07480  -0.11612 79  GLY B CA  
5758 C C   . GLY B 79  ? 0.68481 0.64501 0.48753 0.05309  0.07553  -0.10640 79  GLY B C   
5759 O O   . GLY B 79  ? 0.63091 0.58403 0.44344 0.05064  0.07232  -0.10433 79  GLY B O   
5763 N N   . HIS B 80  ? 0.70029 0.67676 0.50857 0.06057  0.08015  -0.10088 80  HIS B N   
5764 C CA  . HIS B 80  ? 0.65693 0.64585 0.48440 0.06504  0.08102  -0.09166 80  HIS B CA  
5765 C C   . HIS B 80  ? 0.67192 0.68398 0.50471 0.06663  0.08365  -0.08456 80  HIS B C   
5766 O O   . HIS B 80  ? 0.71788 0.73486 0.53868 0.06942  0.08786  -0.08764 80  HIS B O   
5767 C CB  . HIS B 80  ? 0.68661 0.66547 0.51536 0.07580  0.08647  -0.09369 80  HIS B CB  
5768 C CG  . HIS B 80  ? 0.78168 0.75824 0.59676 0.08626  0.09446  -0.09924 80  HIS B CG  
5769 N ND1 . HIS B 80  ? 0.79514 0.74781 0.59015 0.08916  0.09733  -0.10960 80  HIS B ND1 
5770 C CD2 . HIS B 80  ? 0.84825 0.84321 0.66610 0.09457  0.10060  -0.09607 80  HIS B CD2 
5771 C CE1 . HIS B 80  ? 0.88326 0.83896 0.66883 0.09999  0.10491  -0.11269 80  HIS B CE1 
5772 N NE2 . HIS B 80  ? 0.93114 0.91394 0.73101 0.10354  0.10702  -0.10451 80  HIS B NE2 
5780 N N   . SER B 81  ? 0.56952 0.59474 0.41903 0.06363  0.08102  -0.07514 81  SER B N   
5781 C CA  . SER B 81  ? 0.64214 0.68788 0.49736 0.06350  0.08370  -0.06734 81  SER B CA  
5782 C C   . SER B 81  ? 0.57057 0.62547 0.44443 0.06273  0.08289  -0.05910 81  SER B C   
5783 O O   . SER B 81  ? 0.54641 0.59244 0.42868 0.06083  0.07865  -0.05860 81  SER B O   
5784 C CB  . SER B 81  ? 0.58978 0.64132 0.43892 0.05583  0.07963  -0.06415 81  SER B CB  
5785 O OG  . SER B 81  ? 0.58346 0.62945 0.43893 0.04909  0.07212  -0.06150 81  SER B OG  
5791 N N   . MET B 82  ? 0.57207 0.64532 0.45167 0.06315  0.08702  -0.05265 82  MET B N   
5792 C CA  . MET B 82  ? 0.57915 0.66307 0.47541 0.06137  0.08695  -0.04523 82  MET B CA  
5793 C C   . MET B 82  ? 0.55581 0.64836 0.45482 0.05231  0.08487  -0.03665 82  MET B C   
5794 O O   . MET B 82  ? 0.56359 0.66329 0.45346 0.05052  0.08745  -0.03482 82  MET B O   
5795 C CB  . MET B 82  ? 0.66348 0.76242 0.56468 0.06986  0.09438  -0.04543 82  MET B CB  
5796 C CG  . MET B 82  ? 0.67074 0.78400 0.58903 0.06825  0.09481  -0.03880 82  MET B CG  
5797 S SD  . MET B 82  ? 0.78204 0.91389 0.70452 0.08130  0.10328  -0.04107 82  MET B SD  
5798 C CE  . MET B 82  ? 0.86564 1.01289 0.77685 0.08175  0.11018  -0.04112 82  MET B CE  
5808 N N   . GLN B 83  ? 0.48272 0.57295 0.39271 0.04683  0.08044  -0.03137 83  GLN B N   
5809 C CA  . GLN B 83  ? 0.48769 0.58278 0.39981 0.03865  0.07895  -0.02277 83  GLN B CA  
5810 C C   . GLN B 83  ? 0.46912 0.57306 0.39586 0.03552  0.08012  -0.01740 83  GLN B C   
5811 O O   . GLN B 83  ? 0.42536 0.52190 0.36094 0.03476  0.07595  -0.01755 83  GLN B O   
5812 C CB  . GLN B 83  ? 0.50658 0.58763 0.41471 0.03441  0.07160  -0.02186 83  GLN B CB  
5813 C CG  . GLN B 83  ? 0.57144 0.65349 0.48054 0.02742  0.07017  -0.01276 83  GLN B CG  
5814 C CD  . GLN B 83  ? 0.63150 0.70158 0.53646 0.02516  0.06324  -0.01124 83  GLN B CD  
5815 O OE1 . GLN B 83  ? 0.61524 0.67771 0.52060 0.02735  0.05882  -0.01692 83  GLN B OE1 
5816 N NE2 . GLN B 83  ? 0.65131 0.71957 0.55166 0.02088  0.06243  -0.00349 83  GLN B NE2 
5825 N N   . ASN B 84  ? 0.46804 0.58865 0.39694 0.03283  0.08574  -0.01273 84  ASN B N   
5826 C CA  . ASN B 84  ? 0.43840 0.57113 0.38098 0.02868  0.08735  -0.00818 84  ASN B CA  
5827 C C   . ASN B 84  ? 0.40141 0.53569 0.35317 0.03717  0.08705  -0.01363 84  ASN B C   
5828 O O   . ASN B 84  ? 0.40918 0.54633 0.35639 0.04651  0.09054  -0.01934 84  ASN B O   
5829 C CB  . ASN B 84  ? 0.41920 0.54164 0.36401 0.01902  0.08266  -0.00192 84  ASN B CB  
5830 C CG  . ASN B 84  ? 0.48983 0.60857 0.42255 0.01246  0.08362  0.00383  84  ASN B CG  
5831 O OD1 . ASN B 84  ? 0.47681 0.60897 0.40594 0.00961  0.08949  0.00677  84  ASN B OD1 
5832 N ND2 . ASN B 84  ? 0.46096 0.56231 0.38655 0.01089  0.07812  0.00545  84  ASN B ND2 
5839 N N   . CYS B 85  ? 0.38632 0.51648 0.34876 0.03496  0.08303  -0.01229 85  CYS B N   
5840 C CA  . CYS B 85  ? 0.40923 0.54129 0.37992 0.04318  0.08289  -0.01633 85  CYS B CA  
5841 C C   . CYS B 85  ? 0.42470 0.53421 0.39073 0.04765  0.07792  -0.02185 85  CYS B C   
5842 O O   . CYS B 85  ? 0.37954 0.48514 0.35131 0.05324  0.07668  -0.02443 85  CYS B O   
5843 C CB  . CYS B 85  ? 0.40082 0.54418 0.38559 0.03798  0.08181  -0.01172 85  CYS B CB  
5844 S SG  . CYS B 85  ? 0.41991 0.59359 0.41060 0.03118  0.08844  -0.00595 85  CYS B SG  
5850 N N   . VAL B 86  ? 0.39792 0.49338 0.35294 0.04537  0.07525  -0.02383 86  VAL B N   
5851 C CA  . VAL B 86  ? 0.43072 0.50684 0.38100 0.04777  0.07073  -0.02937 86  VAL B CA  
5852 C C   . VAL B 86  ? 0.45101 0.52066 0.38738 0.05325  0.07324  -0.03618 86  VAL B C   
5853 O O   . VAL B 86  ? 0.46416 0.54025 0.39230 0.05233  0.07598  -0.03573 86  VAL B O   
5854 C CB  . VAL B 86  ? 0.44208 0.50668 0.39201 0.04006  0.06408  -0.02695 86  VAL B CB  
5855 C CG1 . VAL B 86  ? 0.43262 0.49857 0.39554 0.03539  0.06109  -0.02172 86  VAL B CG1 
5856 C CG2 . VAL B 86  ? 0.56692 0.63335 0.50784 0.03559  0.06389  -0.02401 86  VAL B CG2 
5866 N N   . LEU B 87  ? 0.42665 0.48271 0.35931 0.05880  0.07270  -0.04255 87  LEU B N   
5867 C CA  . LEU B 87  ? 0.44837 0.49249 0.36593 0.06258  0.07423  -0.05030 87  LEU B CA  
5868 C C   . LEU B 87  ? 0.46322 0.49321 0.37485 0.05531  0.06791  -0.05291 87  LEU B C   
5869 O O   . LEU B 87  ? 0.42587 0.44972 0.34498 0.05136  0.06316  -0.05119 87  LEU B O   
5870 C CB  . LEU B 87  ? 0.47867 0.51342 0.39366 0.07246  0.07766  -0.05564 87  LEU B CB  
5871 C CG  . LEU B 87  ? 0.57215 0.58969 0.46969 0.07734  0.08020  -0.06468 87  LEU B CG  
5872 C CD1 . LEU B 87  ? 0.52626 0.55404 0.41450 0.08010  0.08515  -0.06630 87  LEU B CD1 
5873 C CD2 . LEU B 87  ? 0.61486 0.62251 0.51150 0.08813  0.08371  -0.06768 87  LEU B CD2 
5885 N N   . LYS B 88  ? 0.44493 0.47185 0.34325 0.05344  0.06783  -0.05702 88  LYS B N   
5886 C CA  . LYS B 88  ? 0.46364 0.48124 0.35548 0.04654  0.06189  -0.06010 88  LYS B CA  
5887 C C   . LYS B 88  ? 0.50245 0.50527 0.37907 0.04838  0.06353  -0.07016 88  LYS B C   
5888 O O   . LYS B 88  ? 0.55104 0.55579 0.41575 0.05095  0.06723  -0.07391 88  LYS B O   
5889 C CB  . LYS B 88  ? 0.47997 0.50816 0.36817 0.04163  0.05948  -0.05577 88  LYS B CB  
5890 C CG  . LYS B 88  ? 0.50707 0.54612 0.40700 0.03923  0.05854  -0.04581 88  LYS B CG  
5891 C CD  . LYS B 88  ? 0.57316 0.61725 0.46778 0.03459  0.05490  -0.04123 88  LYS B CD  
5892 C CE  . LYS B 88  ? 0.66875 0.72155 0.55284 0.03583  0.05893  -0.04010 88  LYS B CE  
5893 N NZ  . LYS B 88  ? 0.74819 0.80484 0.62695 0.03213  0.05509  -0.03405 88  LYS B NZ  
5907 N N   . LEU B 89  ? 0.50295 0.48996 0.37854 0.04657  0.06117  -0.07474 89  LEU B N   
5908 C CA  . LEU B 89  ? 0.49470 0.46346 0.35395 0.04688  0.06301  -0.08468 89  LEU B CA  
5909 C C   . LEU B 89  ? 0.53707 0.50347 0.38900 0.03653  0.05720  -0.08868 89  LEU B C   
5910 O O   . LEU B 89  ? 0.50092 0.46637 0.36022 0.03019  0.05183  -0.08705 89  LEU B O   
5911 C CB  . LEU B 89  ? 0.53028 0.48128 0.39024 0.05071  0.06464  -0.08732 89  LEU B CB  
5912 C CG  . LEU B 89  ? 0.53249 0.48893 0.39960 0.06230  0.07025  -0.08340 89  LEU B CG  
5913 C CD1 . LEU B 89  ? 0.59042 0.53024 0.45884 0.06707  0.07125  -0.08453 89  LEU B CD1 
5914 C CD2 . LEU B 89  ? 0.57305 0.52991 0.42729 0.07004  0.07678  -0.08786 89  LEU B CD2 
5926 N N   . LYS B 90  ? 0.53422 0.50144 0.37153 0.03486  0.05823  -0.09407 90  LYS B N   
5927 C CA  . LYS B 90  ? 0.58418 0.55091 0.41324 0.02489  0.05271  -0.09896 90  LYS B CA  
5928 C C   . LYS B 90  ? 0.57811 0.52240 0.39588 0.02024  0.05311  -0.10846 90  LYS B C   
5929 O O   . LYS B 90  ? 0.62743 0.55514 0.43242 0.02528  0.05898  -0.11469 90  LYS B O   
5930 C CB  . LYS B 90  ? 0.59906 0.57532 0.41544 0.02432  0.05350  -0.10152 90  LYS B CB  
5931 C CG  . LYS B 90  ? 0.68403 0.66670 0.49398 0.01444  0.04695  -0.10496 90  LYS B CG  
5932 C CD  . LYS B 90  ? 0.73898 0.74198 0.56155 0.01338  0.04148  -0.09503 90  LYS B CD  
5933 C CE  . LYS B 90  ? 0.89036 0.90620 0.70352 0.00699  0.03596  -0.09748 90  LYS B CE  
5934 N NZ  . LYS B 90  ? 0.89463 0.92788 0.71881 0.00749  0.03054  -0.08747 90  LYS B NZ  
5948 N N   . VAL B 91  ? 0.58304 0.52634 0.40426 0.01062  0.04723  -0.10964 91  VAL B N   
5949 C CA  . VAL B 91  ? 0.59701 0.51906 0.40709 0.00342  0.04729  -0.11833 91  VAL B CA  
5950 C C   . VAL B 91  ? 0.67522 0.60370 0.47576 -0.00924 0.04205  -0.12472 91  VAL B C   
5951 O O   . VAL B 91  ? 0.60715 0.55796 0.41271 -0.01141 0.03738  -0.12102 91  VAL B O   
5952 C CB  . VAL B 91  ? 0.59273 0.50687 0.41505 0.00237  0.04580  -0.11462 91  VAL B CB  
5953 C CG1 . VAL B 91  ? 0.61646 0.52254 0.44472 0.01464  0.05128  -0.11015 91  VAL B CG1 
5954 C CG2 . VAL B 91  ? 0.60944 0.54465 0.44939 -0.00153 0.03919  -0.10695 91  VAL B CG2 
5964 N N   . ASP B 92  ? 0.65162 0.56002 0.43710 -0.01774 0.04299  -0.13443 92  ASP B N   
5965 C CA  . ASP B 92  ? 0.67287 0.58626 0.44593 -0.03090 0.03892  -0.14252 92  ASP B CA  
5966 C C   . ASP B 92  ? 0.71029 0.63810 0.49402 -0.04207 0.03167  -0.14100 92  ASP B C   
5967 O O   . ASP B 92  ? 0.72538 0.66378 0.50138 -0.05335 0.02736  -0.14691 92  ASP B O   
5968 C CB  . ASP B 92  ? 0.86465 0.74822 0.61361 -0.03638 0.04388  -0.15465 92  ASP B CB  
5969 C CG  . ASP B 92  ? 0.87212 0.73043 0.61876 -0.04123 0.04569  -0.15713 92  ASP B CG  
5970 O OD1 . ASP B 92  ? 0.80246 0.66769 0.56652 -0.04079 0.04291  -0.14994 92  ASP B OD1 
5971 O OD2 . ASP B 92  ? 1.06646 0.89566 0.79188 -0.04543 0.05034  -0.16649 92  ASP B OD2 
5976 N N   . THR B 93  ? 0.62435 0.55568 0.42593 -0.03881 0.03012  -0.13309 93  THR B N   
5977 C CA  . THR B 93  ? 0.64594 0.59033 0.45876 -0.04779 0.02405  -0.13114 93  THR B CA  
5978 C C   . THR B 93  ? 0.56264 0.52737 0.39636 -0.03928 0.02086  -0.11942 93  THR B C   
5979 O O   . THR B 93  ? 0.55330 0.51107 0.39550 -0.02922 0.02429  -0.11314 93  THR B O   
5980 C CB  . THR B 93  ? 0.67105 0.59238 0.48136 -0.05386 0.02629  -0.13456 93  THR B CB  
5981 O OG1 . THR B 93  ? 0.74267 0.64004 0.53042 -0.06165 0.03015  -0.14561 93  THR B OG1 
5982 C CG2 . THR B 93  ? 0.73596 0.67290 0.55665 -0.06443 0.02032  -0.13349 93  THR B CG2 
5990 N N   . ALA B 94  ? 0.52386 0.51355 0.36524 -0.04313 0.01439  -0.11651 94  ALA B N   
5991 C CA  . ALA B 94  ? 0.43429 0.43951 0.29364 -0.03561 0.01150  -0.10579 94  ALA B CA  
5992 C C   . ALA B 94  ? 0.52264 0.52185 0.39277 -0.03870 0.01069  -0.10402 94  ALA B C   
5993 O O   . ALA B 94  ? 0.47382 0.47024 0.33993 -0.04956 0.00912  -0.11021 94  ALA B O   
5994 C CB  . ALA B 94  ? 0.49389 0.52675 0.35624 -0.03657 0.00513  -0.10283 94  ALA B CB  
6000 N N   . ASN B 95  ? 0.46862 0.46609 0.35180 -0.03002 0.01192  -0.09572 95  ASN B N   
6001 C CA  . ASN B 95  ? 0.45184 0.44388 0.34519 -0.03206 0.01131  -0.09354 95  ASN B CA  
6002 C C   . ASN B 95  ? 0.48566 0.49797 0.38623 -0.03846 0.00515  -0.09287 95  ASN B C   
6003 O O   . ASN B 95  ? 0.42967 0.46056 0.33838 -0.03298 0.00158  -0.08646 95  ASN B O   
6004 C CB  . ASN B 95  ? 0.40820 0.39773 0.31410 -0.02148 0.01331  -0.08454 95  ASN B CB  
6005 C CG  . ASN B 95  ? 0.49481 0.47738 0.41017 -0.02297 0.01308  -0.08242 95  ASN B CG  
6006 O OD1 . ASN B 95  ? 0.42663 0.40634 0.33943 -0.03182 0.01165  -0.08718 95  ASN B OD1 
6007 N ND2 . ASN B 95  ? 0.41349 0.39341 0.33920 -0.01497 0.01475  -0.07536 95  ASN B ND2 
6014 N N   . PRO B 96  ? 0.46665 0.47659 0.36396 -0.04978 0.00393  -0.09909 96  PRO B N   
6015 C CA  . PRO B 96  ? 0.47316 0.50707 0.37819 -0.05552 -0.00189 -0.09849 96  PRO B CA  
6016 C C   . PRO B 96  ? 0.43146 0.47261 0.35245 -0.04868 -0.00349 -0.09017 96  PRO B C   
6017 O O   . PRO B 96  ? 0.47078 0.53438 0.39945 -0.04897 -0.00823 -0.08770 96  PRO B O   
6018 C CB  . PRO B 96  ? 0.55436 0.58060 0.45115 -0.07052 -0.00145 -0.10738 96  PRO B CB  
6019 C CG  . PRO B 96  ? 0.60016 0.59440 0.48954 -0.06969 0.00474  -0.10942 96  PRO B CG  
6020 C CD  . PRO B 96  ? 0.47836 0.46411 0.36379 -0.05801 0.00799  -0.10682 96  PRO B CD  
6028 N N   . LYS B 97  ? 0.41888 0.44251 0.34472 -0.04205 0.00032  -0.08584 97  LYS B N   
6029 C CA  . LYS B 97  ? 0.44606 0.47422 0.38586 -0.03566 -0.00080 -0.07823 97  LYS B CA  
6030 C C   . LYS B 97  ? 0.45095 0.48477 0.39591 -0.02419 -0.00101 -0.07032 97  LYS B C   
6031 O O   . LYS B 97  ? 0.41033 0.44290 0.36494 -0.01855 -0.00091 -0.06414 97  LYS B O   
6032 C CB  . LYS B 97  ? 0.47870 0.48562 0.42057 -0.03568 0.00321  -0.07790 97  LYS B CB  
6033 C CG  . LYS B 97  ? 0.56251 0.56081 0.49858 -0.04748 0.00387  -0.08463 97  LYS B CG  
6034 C CD  . LYS B 97  ? 0.65424 0.62823 0.58914 -0.04581 0.00842  -0.08393 97  LYS B CD  
6035 C CE  . LYS B 97  ? 0.76922 0.72995 0.69522 -0.05790 0.00992  -0.09032 97  LYS B CE  
6036 N NZ  . LYS B 97  ? 0.93048 0.90152 0.86674 -0.06235 0.00751  -0.08784 97  LYS B NZ  
6050 N N   . THR B 98  ? 0.38843 0.42689 0.32598 -0.02124 -0.00092 -0.07048 98  THR B N   
6051 C CA  . THR B 98  ? 0.40747 0.44896 0.34791 -0.01143 -0.00037 -0.06273 98  THR B CA  
6052 C C   . THR B 98  ? 0.36289 0.41876 0.31188 -0.00726 -0.00454 -0.05653 98  THR B C   
6053 O O   . THR B 98  ? 0.39888 0.47200 0.34683 -0.00958 -0.00891 -0.05821 98  THR B O   
6054 C CB  . THR B 98  ? 0.41970 0.46723 0.34957 -0.00996 -0.00029 -0.06401 98  THR B CB  
6055 O OG1 . THR B 98  ? 0.41390 0.44813 0.33390 -0.01369 0.00367  -0.07086 98  THR B OG1 
6056 C CG2 . THR B 98  ? 0.38751 0.43639 0.31869 -0.00081 0.00100  -0.05558 98  THR B CG2 
6064 N N   . PRO B 99  ? 0.32470 0.37495 0.28136 -0.00110 -0.00341 -0.04970 99  PRO B N   
6065 C CA  . PRO B 99  ? 0.34942 0.41043 0.31200 0.00407  -0.00688 -0.04386 99  PRO B CA  
6066 C C   . PRO B 99  ? 0.34880 0.41574 0.30555 0.01116  -0.00775 -0.03823 99  PRO B C   
6067 O O   . PRO B 99  ? 0.36999 0.43268 0.31969 0.01159  -0.00537 -0.03845 99  PRO B O   
6068 C CB  . PRO B 99  ? 0.35907 0.40753 0.32999 0.00658  -0.00455 -0.03970 99  PRO B CB  
6069 C CG  . PRO B 99  ? 0.32936 0.36379 0.29725 0.00681  0.00030  -0.03976 99  PRO B CG  
6070 C CD  . PRO B 99  ? 0.39263 0.42639 0.35258 0.00120  0.00119  -0.04743 99  PRO B CD  
6078 N N   . LYS B 100 ? 0.36339 0.43991 0.32208 0.01727  -0.01099 -0.03304 100 LYS B N   
6079 C CA  . LYS B 100 ? 0.41422 0.49085 0.36614 0.02526  -0.01101 -0.02594 100 LYS B CA  
6080 C C   . LYS B 100 ? 0.34765 0.40558 0.30072 0.02678  -0.00624 -0.02122 100 LYS B C   
6081 O O   . LYS B 100 ? 0.32573 0.37514 0.28639 0.02622  -0.00506 -0.02013 100 LYS B O   
6082 C CB  . LYS B 100 ? 0.46590 0.55407 0.41862 0.03305  -0.01509 -0.02110 100 LYS B CB  
6083 C CG  . LYS B 100 ? 0.55484 0.63789 0.49937 0.04263  -0.01469 -0.01238 100 LYS B CG  
6084 C CD  . LYS B 100 ? 0.68775 0.78514 0.63047 0.05202  -0.01921 -0.00845 100 LYS B CD  
6085 C CE  . LYS B 100 ? 0.69112 0.77724 0.62347 0.06262  -0.01809 0.00119  100 LYS B CE  
6086 N NZ  . LYS B 100 ? 0.71909 0.80127 0.64066 0.06205  -0.01621 0.00337  100 LYS B NZ  
6100 N N   . TYR B 101 ? 0.33426 0.38714 0.27997 0.02754  -0.00329 -0.01915 101 TYR B N   
6101 C CA  . TYR B 101 ? 0.35824 0.39672 0.30592 0.02705  0.00151  -0.01570 101 TYR B CA  
6102 C C   . TYR B 101 ? 0.34570 0.38160 0.28360 0.02995  0.00399  -0.01031 101 TYR B C   
6103 O O   . TYR B 101 ? 0.36239 0.40670 0.29158 0.03202  0.00239  -0.01026 101 TYR B O   
6104 C CB  . TYR B 101 ? 0.32835 0.36145 0.28018 0.02150  0.00488  -0.02165 101 TYR B CB  
6105 C CG  . TYR B 101 ? 0.34315 0.37904 0.28664 0.02008  0.00696  -0.02531 101 TYR B CG  
6106 C CD1 . TYR B 101 ? 0.39137 0.43505 0.33017 0.01696  0.00456  -0.03219 101 TYR B CD1 
6107 C CD2 . TYR B 101 ? 0.35250 0.38405 0.29187 0.02129  0.01153  -0.02216 101 TYR B CD2 
6108 C CE1 . TYR B 101 ? 0.36320 0.40812 0.29288 0.01561  0.00665  -0.03617 101 TYR B CE1 
6109 C CE2 . TYR B 101 ? 0.37261 0.40720 0.30363 0.02066  0.01374  -0.02569 101 TYR B CE2 
6110 C CZ  . TYR B 101 ? 0.37499 0.41541 0.30071 0.01816  0.01126  -0.03278 101 TYR B CZ  
6111 O OH  . TYR B 101 ? 0.39253 0.43447 0.30874 0.01742  0.01369  -0.03698 101 TYR B OH  
6121 N N   . LYS B 102 ? 0.34888 0.37375 0.28793 0.02947  0.00797  -0.00566 102 LYS B N   
6122 C CA  . LYS B 102 ? 0.34533 0.36713 0.27586 0.02974  0.01179  -0.00133 102 LYS B CA  
6123 C C   . LYS B 102 ? 0.37133 0.38576 0.30775 0.02559  0.01675  -0.00050 102 LYS B C   
6124 O O   . LYS B 102 ? 0.31774 0.32800 0.26375 0.02359  0.01671  -0.00184 102 LYS B O   
6125 C CB  . LYS B 102 ? 0.42427 0.44151 0.34476 0.03491  0.01090  0.00700  102 LYS B CB  
6126 C CG  . LYS B 102 ? 0.48949 0.49444 0.41292 0.03586  0.01117  0.01184  102 LYS B CG  
6127 C CD  . LYS B 102 ? 0.57324 0.57024 0.48391 0.04226  0.01047  0.02003  102 LYS B CD  
6128 C CE  . LYS B 102 ? 0.60652 0.58868 0.51878 0.04303  0.01100  0.02380  102 LYS B CE  
6129 N NZ  . LYS B 102 ? 0.82433 0.81201 0.74488 0.04682  0.00660  0.02029  102 LYS B NZ  
6143 N N   . PHE B 103 ? 0.37608 0.39075 0.30653 0.02429  0.02107  0.00189  103 PHE B N   
6144 C CA  . PHE B 103 ? 0.37252 0.38408 0.30771 0.02030  0.02607  0.00364  103 PHE B CA  
6145 C C   . PHE B 103 ? 0.38836 0.39073 0.31804 0.01876  0.02790  0.01190  103 PHE B C   
6146 O O   . PHE B 103 ? 0.39332 0.39295 0.31113 0.02085  0.02809  0.01683  103 PHE B O   
6147 C CB  . PHE B 103 ? 0.34881 0.36775 0.28041 0.01946  0.03042  0.00123  103 PHE B CB  
6148 C CG  . PHE B 103 ? 0.37013 0.39418 0.30513 0.02052  0.02991  -0.00731 103 PHE B CG  
6149 C CD1 . PHE B 103 ? 0.36757 0.38907 0.31047 0.02044  0.02660  -0.01196 103 PHE B CD1 
6150 C CD2 . PHE B 103 ? 0.39064 0.42054 0.31916 0.02144  0.03312  -0.01075 103 PHE B CD2 
6151 C CE1 . PHE B 103 ? 0.34078 0.36337 0.28430 0.02065  0.02671  -0.01976 103 PHE B CE1 
6152 C CE2 . PHE B 103 ? 0.39372 0.42456 0.32281 0.02239  0.03327  -0.01892 103 PHE B CE2 
6153 C CZ  . PHE B 103 ? 0.38668 0.41278 0.32282 0.02172  0.03008  -0.02331 103 PHE B CZ  
6163 N N   . VAL B 104 ? 0.36159 0.35832 0.29837 0.01479  0.02943  0.01348  104 VAL B N   
6164 C CA  . VAL B 104 ? 0.37094 0.35631 0.30110 0.01150  0.03166  0.02067  104 VAL B CA  
6165 C C   . VAL B 104 ? 0.43315 0.42167 0.37047 0.00419  0.03611  0.02081  104 VAL B C   
6166 O O   . VAL B 104 ? 0.42493 0.42187 0.37408 0.00352  0.03610  0.01576  104 VAL B O   
6167 C CB  . VAL B 104 ? 0.43719 0.41004 0.36636 0.01379  0.02821  0.02302  104 VAL B CB  
6168 C CG1 . VAL B 104 ? 0.44227 0.41615 0.36547 0.02202  0.02353  0.02290  104 VAL B CG1 
6169 C CG2 . VAL B 104 ? 0.46248 0.43696 0.40524 0.01143  0.02693  0.01861  104 VAL B CG2 
6179 N N   . ARG B 105 ? 0.36978 0.35287 0.29908 -0.00132 0.04022  0.02667  105 ARG B N   
6180 C CA  . ARG B 105 ? 0.39397 0.38161 0.32977 -0.00980 0.04433  0.02736  105 ARG B CA  
6181 C C   . ARG B 105 ? 0.41079 0.38282 0.34415 -0.01473 0.04370  0.03079  105 ARG B C   
6182 O O   . ARG B 105 ? 0.47585 0.43156 0.39548 -0.01483 0.04398  0.03618  105 ARG B O   
6183 C CB  . ARG B 105 ? 0.42024 0.41462 0.34902 -0.01485 0.05010  0.03094  105 ARG B CB  
6184 C CG  . ARG B 105 ? 0.41195 0.41604 0.34863 -0.02415 0.05438  0.03130  105 ARG B CG  
6185 C CD  . ARG B 105 ? 0.46249 0.47859 0.39453 -0.02860 0.06033  0.03376  105 ARG B CD  
6186 N NE  . ARG B 105 ? 0.46450 0.49335 0.40492 -0.03804 0.06428  0.03410  105 ARG B NE  
6187 C CZ  . ARG B 105 ? 0.49341 0.54341 0.44773 -0.03652 0.06553  0.02954  105 ARG B CZ  
6188 N NH1 . ARG B 105 ? 0.41461 0.47207 0.37526 -0.02605 0.06340  0.02392  105 ARG B NH1 
6189 N NH2 . ARG B 105 ? 0.51916 0.58328 0.48015 -0.04579 0.06922  0.03068  105 ARG B NH2 
6203 N N   . ILE B 106 ? 0.40684 0.38248 0.35196 -0.01830 0.04288  0.02774  106 ILE B N   
6204 C CA  . ILE B 106 ? 0.40248 0.36243 0.34446 -0.02305 0.04209  0.03008  106 ILE B CA  
6205 C C   . ILE B 106 ? 0.49390 0.45302 0.43271 -0.03549 0.04701  0.03349  106 ILE B C   
6206 O O   . ILE B 106 ? 0.42317 0.39799 0.36548 -0.04043 0.05092  0.03366  106 ILE B O   
6207 C CB  . ILE B 106 ? 0.39738 0.35946 0.35166 -0.02057 0.03809  0.02520  106 ILE B CB  
6208 C CG1 . ILE B 106 ? 0.41858 0.40042 0.38780 -0.02299 0.03909  0.02091  106 ILE B CG1 
6209 C CG2 . ILE B 106 ? 0.45443 0.41264 0.40805 -0.00989 0.03325  0.02294  106 ILE B CG2 
6210 C CD1 . ILE B 106 ? 0.44555 0.42808 0.42546 -0.02258 0.03578  0.01721  106 ILE B CD1 
6222 N N   . GLN B 107 ? 0.44813 0.38809 0.37862 -0.04081 0.04710  0.03630  107 GLN B N   
6223 C CA  . GLN B 107 ? 0.51473 0.45099 0.44065 -0.05482 0.05149  0.03907  107 GLN B CA  
6224 C C   . GLN B 107 ? 0.46801 0.41254 0.40686 -0.06044 0.04993  0.03486  107 GLN B C   
6225 O O   . GLN B 107 ? 0.42811 0.37055 0.37402 -0.05362 0.04546  0.03125  107 GLN B O   
6226 C CB  . GLN B 107 ? 0.58783 0.49395 0.49314 -0.05847 0.05318  0.04472  107 GLN B CB  
6227 C CG  . GLN B 107 ? 0.67667 0.57123 0.56601 -0.05205 0.05453  0.05009  107 GLN B CG  
6228 C CD  . GLN B 107 ? 0.82622 0.73319 0.71241 -0.05869 0.05968  0.05302  107 GLN B CD  
6229 O OE1 . GLN B 107 ? 0.78916 0.70059 0.67494 -0.07243 0.06424  0.05429  107 GLN B OE1 
6230 N NE2 . GLN B 107 ? 0.85679 0.77068 0.74024 -0.04938 0.05909  0.05400  107 GLN B NE2 
6239 N N   . PRO B 108 ? 0.43558 0.39028 0.37712 -0.07336 0.05358  0.03538  108 PRO B N   
6240 C CA  . PRO B 108 ? 0.40815 0.37034 0.35998 -0.07994 0.05200  0.03185  108 PRO B CA  
6241 C C   . PRO B 108 ? 0.46720 0.40271 0.40968 -0.08046 0.04947  0.03185  108 PRO B C   
6242 O O   . PRO B 108 ? 0.45366 0.36330 0.37825 -0.08272 0.05125  0.03588  108 PRO B O   
6243 C CB  . PRO B 108 ? 0.48543 0.46083 0.43699 -0.09577 0.05709  0.03366  108 PRO B CB  
6244 C CG  . PRO B 108 ? 0.49669 0.46542 0.43530 -0.09838 0.06155  0.03859  108 PRO B CG  
6245 C CD  . PRO B 108 ? 0.49827 0.46149 0.43423 -0.08276 0.05933  0.03907  108 PRO B CD  
6253 N N   . GLY B 109 ? 0.41643 0.35754 0.37009 -0.07737 0.04551  0.02740  109 GLY B N   
6254 C CA  . GLY B 109 ? 0.40080 0.31977 0.34774 -0.07545 0.04273  0.02638  109 GLY B CA  
6255 C C   . GLY B 109 ? 0.43583 0.34952 0.38493 -0.05988 0.03857  0.02496  109 GLY B C   
6256 O O   . GLY B 109 ? 0.47081 0.37520 0.42065 -0.05606 0.03547  0.02257  109 GLY B O   
6260 N N   . GLN B 110 ? 0.40105 0.32238 0.35144 -0.05136 0.03847  0.02600  110 GLN B N   
6261 C CA  . GLN B 110 ? 0.41362 0.33342 0.36668 -0.03792 0.03443  0.02420  110 GLN B CA  
6262 C C   . GLN B 110 ? 0.37627 0.31482 0.34663 -0.03410 0.03137  0.01891  110 GLN B C   
6263 O O   . GLN B 110 ? 0.36469 0.32175 0.34515 -0.03768 0.03265  0.01728  110 GLN B O   
6264 C CB  . GLN B 110 ? 0.42256 0.34412 0.36963 -0.03117 0.03522  0.02678  110 GLN B CB  
6265 C CG  . GLN B 110 ? 0.54635 0.47079 0.49734 -0.01843 0.03075  0.02417  110 GLN B CG  
6266 C CD  . GLN B 110 ? 0.64686 0.55363 0.59104 -0.01294 0.02802  0.02467  110 GLN B CD  
6267 O OE1 . GLN B 110 ? 0.46487 0.37630 0.41771 -0.00786 0.02448  0.02077  110 GLN B OE1 
6268 N NE2 . GLN B 110 ? 0.70695 0.59265 0.63458 -0.01392 0.03009  0.02957  110 GLN B NE2 
6277 N N   . THR B 111 ? 0.39352 0.32721 0.36656 -0.02646 0.02754  0.01643  111 THR B N   
6278 C CA  . THR B 111 ? 0.35325 0.30109 0.34031 -0.02269 0.02477  0.01183  111 THR B CA  
6279 C C   . THR B 111 ? 0.34820 0.30293 0.33814 -0.01346 0.02292  0.01003  111 THR B C   
6280 O O   . THR B 111 ? 0.34803 0.29621 0.32949 -0.00884 0.02267  0.01204  111 THR B O   
6281 C CB  . THR B 111 ? 0.35841 0.29727 0.34650 -0.02179 0.02203  0.00989  111 THR B CB  
6282 O OG1 . THR B 111 ? 0.36508 0.28963 0.34375 -0.01488 0.02064  0.01130  111 THR B OG1 
6283 C CG2 . THR B 111 ? 0.38152 0.31390 0.36653 -0.03225 0.02364  0.01058  111 THR B CG2 
6291 N N   . PHE B 112 ? 0.33216 0.29910 0.33309 -0.01080 0.02142  0.00609  112 PHE B N   
6292 C CA  . PHE B 112 ? 0.34703 0.31938 0.35010 -0.00384 0.01976  0.00342  112 PHE B CA  
6293 C C   . PHE B 112 ? 0.32562 0.30501 0.33871 -0.00212 0.01807  -0.00068 112 PHE B C   
6294 O O   . PHE B 112 ? 0.31654 0.29989 0.33552 -0.00552 0.01850  -0.00101 112 PHE B O   
6295 C CB  . PHE B 112 ? 0.31279 0.29291 0.31337 -0.00320 0.02241  0.00403  112 PHE B CB  
6296 C CG  . PHE B 112 ? 0.32363 0.31546 0.33019 -0.00712 0.02554  0.00387  112 PHE B CG  
6297 C CD1 . PHE B 112 ? 0.35486 0.34768 0.35880 -0.01443 0.02858  0.00740  112 PHE B CD1 
6298 C CD2 . PHE B 112 ? 0.29648 0.29853 0.31042 -0.00352 0.02570  0.00028  112 PHE B CD2 
6299 C CE1 . PHE B 112 ? 0.40257 0.41127 0.41316 -0.01781 0.03161  0.00718  112 PHE B CE1 
6300 C CE2 . PHE B 112 ? 0.35991 0.37507 0.37956 -0.00494 0.02860  0.00015  112 PHE B CE2 
6301 C CZ  . PHE B 112 ? 0.35969 0.38062 0.37864 -0.01207 0.03153  0.00361  112 PHE B CZ  
6311 N N   . SER B 113 ? 0.31336 0.29414 0.32740 0.00282  0.01611  -0.00370 113 SER B N   
6312 C CA  . SER B 113 ? 0.27933 0.26418 0.30041 0.00442  0.01501  -0.00741 113 SER B CA  
6313 C C   . SER B 113 ? 0.27532 0.26752 0.29798 0.00623  0.01729  -0.00935 113 SER B C   
6314 O O   . SER B 113 ? 0.29787 0.29156 0.31558 0.00789  0.01837  -0.00985 113 SER B O   
6315 C CB  . SER B 113 ? 0.33081 0.31273 0.35103 0.00732  0.01208  -0.01000 113 SER B CB  
6316 O OG  . SER B 113 ? 0.32269 0.29841 0.34115 0.00715  0.01031  -0.00818 113 SER B OG  
6322 N N   . VAL B 114 ? 0.29249 0.28883 0.32112 0.00688  0.01794  -0.01066 114 VAL B N   
6323 C CA  . VAL B 114 ? 0.26376 0.26566 0.29305 0.01051  0.02042  -0.01268 114 VAL B CA  
6324 C C   . VAL B 114 ? 0.28396 0.27985 0.31282 0.01359  0.01915  -0.01647 114 VAL B C   
6325 O O   . VAL B 114 ? 0.28816 0.28125 0.32063 0.01309  0.01741  -0.01662 114 VAL B O   
6326 C CB  . VAL B 114 ? 0.30382 0.31600 0.33915 0.01037  0.02248  -0.01095 114 VAL B CB  
6327 C CG1 . VAL B 114 ? 0.33462 0.35158 0.36984 0.01674  0.02516  -0.01325 114 VAL B CG1 
6328 C CG2 . VAL B 114 ? 0.31445 0.33323 0.34933 0.00528  0.02439  -0.00739 114 VAL B CG2 
6338 N N   . LEU B 115 ? 0.27838 0.27156 0.30176 0.01606  0.02025  -0.01961 115 LEU B N   
6339 C CA  . LEU B 115 ? 0.25969 0.24516 0.28029 0.01805  0.02009  -0.02356 115 LEU B CA  
6340 C C   . LEU B 115 ? 0.30622 0.29298 0.32596 0.02355  0.02359  -0.02438 115 LEU B C   
6341 O O   . LEU B 115 ? 0.30010 0.28824 0.31486 0.02622  0.02625  -0.02599 115 LEU B O   
6342 C CB  . LEU B 115 ? 0.31982 0.30065 0.33323 0.01637  0.01913  -0.02719 115 LEU B CB  
6343 C CG  . LEU B 115 ? 0.31319 0.28405 0.32210 0.01602  0.01915  -0.03160 115 LEU B CG  
6344 C CD1 . LEU B 115 ? 0.32921 0.29709 0.34271 0.01314  0.01651  -0.03085 115 LEU B CD1 
6345 C CD2 . LEU B 115 ? 0.35189 0.32040 0.35290 0.01318  0.01856  -0.03586 115 LEU B CD2 
6357 N N   . ALA B 116 ? 0.29258 0.28035 0.31706 0.02602  0.02367  -0.02292 116 ALA B N   
6358 C CA  . ALA B 116 ? 0.30968 0.30042 0.33371 0.03321  0.02687  -0.02299 116 ALA B CA  
6359 C C   . ALA B 116 ? 0.37009 0.34540 0.38448 0.03699  0.02838  -0.02720 116 ALA B C   
6360 O O   . ALA B 116 ? 0.37396 0.33811 0.38578 0.03424  0.02653  -0.02860 116 ALA B O   
6361 C CB  . ALA B 116 ? 0.34689 0.34495 0.37854 0.03487  0.02594  -0.01979 116 ALA B CB  
6367 N N   . CYS B 117 ? 0.36473 0.33852 0.37260 0.04255  0.03204  -0.02946 117 CYS B N   
6368 C CA  . CYS B 117 ? 0.38813 0.34409 0.38375 0.04527  0.03407  -0.03422 117 CYS B CA  
6369 C C   . CYS B 117 ? 0.36470 0.31889 0.35586 0.05640  0.03839  -0.03440 117 CYS B C   
6370 O O   . CYS B 117 ? 0.37185 0.34225 0.36881 0.06134  0.04028  -0.03194 117 CYS B O   
6371 C CB  . CYS B 117 ? 0.37821 0.33043 0.36607 0.04132  0.03459  -0.03830 117 CYS B CB  
6372 S SG  . CYS B 117 ? 0.42000 0.37610 0.41163 0.03070  0.02973  -0.03810 117 CYS B SG  
6378 N N   . TYR B 118 ? 0.41105 0.34512 0.39063 0.06027  0.04031  -0.03747 118 TYR B N   
6379 C CA  . TYR B 118 ? 0.43619 0.36285 0.40739 0.07266  0.04494  -0.03825 118 TYR B CA  
6380 C C   . TYR B 118 ? 0.45257 0.35334 0.40580 0.07219  0.04762  -0.04436 118 TYR B C   
6381 O O   . TYR B 118 ? 0.43960 0.32456 0.38711 0.06421  0.04576  -0.04649 118 TYR B O   
6382 C CB  . TYR B 118 ? 0.52946 0.45507 0.50348 0.07988  0.04466  -0.03420 118 TYR B CB  
6383 C CG  . TYR B 118 ? 0.47866 0.43022 0.46941 0.07908  0.04198  -0.02891 118 TYR B CG  
6384 C CD1 . TYR B 118 ? 0.48126 0.43794 0.48100 0.06905  0.03736  -0.02681 118 TYR B CD1 
6385 C CD2 . TYR B 118 ? 0.43383 0.40568 0.43096 0.08765  0.04426  -0.02636 118 TYR B CD2 
6386 C CE1 . TYR B 118 ? 0.41142 0.38979 0.42462 0.06681  0.03510  -0.02265 118 TYR B CE1 
6387 C CE2 . TYR B 118 ? 0.39268 0.38923 0.40456 0.08459  0.04186  -0.02200 118 TYR B CE2 
6388 C CZ  . TYR B 118 ? 0.38201 0.37988 0.40105 0.07376  0.03727  -0.02035 118 TYR B CZ  
6389 O OH  . TYR B 118 ? 0.40041 0.41969 0.43182 0.06963  0.03515  -0.01669 118 TYR B OH  
6399 N N   . ASN B 119 ? 0.48903 0.38591 0.43286 0.08006  0.05219  -0.04744 119 ASN B N   
6400 C CA  . ASN B 119 ? 0.50354 0.37422 0.42786 0.07965  0.05540  -0.05410 119 ASN B CA  
6401 C C   . ASN B 119 ? 0.50466 0.37089 0.42619 0.06479  0.05224  -0.05832 119 ASN B C   
6402 O O   . ASN B 119 ? 0.54225 0.38562 0.44955 0.05921  0.05301  -0.06326 119 ASN B O   
6403 C CB  . ASN B 119 ? 0.59535 0.43925 0.50649 0.08471  0.05755  -0.05467 119 ASN B CB  
6404 C CG  . ASN B 119 ? 0.60809 0.45385 0.51804 0.10176  0.06126  -0.05120 119 ASN B CG  
6405 O OD1 . ASN B 119 ? 0.71981 0.57064 0.63691 0.10607  0.05965  -0.04599 119 ASN B OD1 
6406 N ND2 . ASN B 119 ? 0.69522 0.53811 0.59581 0.11223  0.06628  -0.05408 119 ASN B ND2 
6413 N N   . GLY B 120 ? 0.48530 0.37327 0.41953 0.05818  0.04874  -0.05630 120 GLY B N   
6414 C CA  . GLY B 120 ? 0.48018 0.36824 0.41295 0.04569  0.04533  -0.05956 120 GLY B CA  
6415 C C   . GLY B 120 ? 0.49354 0.37991 0.43196 0.03650  0.04094  -0.05818 120 GLY B C   
6416 O O   . GLY B 120 ? 0.48440 0.37374 0.42249 0.02659  0.03787  -0.06069 120 GLY B O   
6420 N N   . SER B 121 ? 0.46309 0.34658 0.40673 0.03977  0.04049  -0.05419 121 SER B N   
6421 C CA  . SER B 121 ? 0.48172 0.36352 0.42998 0.03120  0.03677  -0.05303 121 SER B CA  
6422 C C   . SER B 121 ? 0.43869 0.34050 0.40403 0.03157  0.03336  -0.04688 121 SER B C   
6423 O O   . SER B 121 ? 0.44108 0.34951 0.41256 0.03955  0.03441  -0.04272 121 SER B O   
6424 C CB  . SER B 121 ? 0.58928 0.44907 0.52783 0.03273  0.03877  -0.05348 121 SER B CB  
6425 O OG  . SER B 121 ? 0.76859 0.60563 0.68877 0.03103  0.04226  -0.05954 121 SER B OG  
6431 N N   . PRO B 122 ? 0.44489 0.35603 0.41720 0.02307  0.02933  -0.04637 122 PRO B N   
6432 C CA  . PRO B 122 ? 0.41939 0.34652 0.40576 0.02286  0.02631  -0.04104 122 PRO B CA  
6433 C C   . PRO B 122 ? 0.46033 0.38271 0.44991 0.02499  0.02596  -0.03811 122 PRO B C   
6434 O O   . PRO B 122 ? 0.44375 0.35278 0.42705 0.02162  0.02605  -0.03993 122 PRO B O   
6435 C CB  . PRO B 122 ? 0.38543 0.31908 0.37460 0.01431  0.02262  -0.04217 122 PRO B CB  
6436 C CG  . PRO B 122 ? 0.47255 0.40233 0.45189 0.01160  0.02368  -0.04725 122 PRO B CG  
6437 C CD  . PRO B 122 ? 0.52148 0.43233 0.48876 0.01437  0.02759  -0.05083 122 PRO B CD  
6445 N N   . SER B 123 ? 0.38942 0.32294 0.38787 0.03016  0.02576  -0.03360 123 SER B N   
6446 C CA  . SER B 123 ? 0.43484 0.36590 0.43618 0.03283  0.02519  -0.03059 123 SER B CA  
6447 C C   . SER B 123 ? 0.34907 0.29236 0.36156 0.02858  0.02161  -0.02720 123 SER B C   
6448 O O   . SER B 123 ? 0.36365 0.30320 0.37720 0.02803  0.02045  -0.02567 123 SER B O   
6449 C CB  . SER B 123 ? 0.56527 0.49824 0.56590 0.04352  0.02805  -0.02837 123 SER B CB  
6450 O OG  . SER B 123 ? 0.72441 0.67724 0.73538 0.04535  0.02752  -0.02531 123 SER B OG  
6456 N N   . GLY B 124 ? 0.33478 0.29129 0.35424 0.02610  0.02023  -0.02579 124 GLY B N   
6457 C CA  . GLY B 124 ? 0.31897 0.28353 0.34653 0.02205  0.01724  -0.02303 124 GLY B CA  
6458 C C   . GLY B 124 ? 0.30772 0.28091 0.33843 0.01879  0.01634  -0.02220 124 GLY B C   
6459 O O   . GLY B 124 ? 0.30992 0.28546 0.33781 0.02012  0.01808  -0.02307 124 GLY B O   
6463 N N   . VAL B 125 ? 0.31289 0.28928 0.34798 0.01477  0.01381  -0.02049 125 VAL B N   
6464 C CA  . VAL B 125 ? 0.29658 0.27761 0.33239 0.01205  0.01304  -0.01919 125 VAL B CA  
6465 C C   . VAL B 125 ? 0.29490 0.28045 0.33569 0.00969  0.01196  -0.01608 125 VAL B C   
6466 O O   . VAL B 125 ? 0.32415 0.30807 0.36744 0.00870  0.01042  -0.01578 125 VAL B O   
6467 C CB  . VAL B 125 ? 0.34190 0.31939 0.37419 0.00972  0.01119  -0.02118 125 VAL B CB  
6468 C CG1 . VAL B 125 ? 0.38393 0.35881 0.41814 0.00763  0.00896  -0.02165 125 VAL B CG1 
6469 C CG2 . VAL B 125 ? 0.34982 0.33085 0.38064 0.00895  0.01079  -0.01924 125 VAL B CG2 
6479 N N   . TYR B 126 ? 0.29436 0.28518 0.33557 0.00811  0.01304  -0.01387 126 TYR B N   
6480 C CA  . TYR B 126 ? 0.29059 0.28347 0.33437 0.00406  0.01222  -0.01144 126 TYR B CA  
6481 C C   . TYR B 126 ? 0.31267 0.30504 0.35273 0.00089  0.01326  -0.00928 126 TYR B C   
6482 O O   . TYR B 126 ? 0.32456 0.31874 0.36160 0.00227  0.01497  -0.00915 126 TYR B O   
6483 C CB  . TYR B 126 ? 0.29173 0.29403 0.34087 0.00407  0.01297  -0.01036 126 TYR B CB  
6484 C CG  . TYR B 126 ? 0.28953 0.30154 0.33989 0.00705  0.01583  -0.00993 126 TYR B CG  
6485 C CD1 . TYR B 126 ? 0.29096 0.31146 0.34193 0.00324  0.01775  -0.00785 126 TYR B CD1 
6486 C CD2 . TYR B 126 ? 0.32281 0.33499 0.37278 0.01368  0.01701  -0.01158 126 TYR B CD2 
6487 C CE1 . TYR B 126 ? 0.30911 0.34081 0.36146 0.00650  0.02079  -0.00757 126 TYR B CE1 
6488 C CE2 . TYR B 126 ? 0.33073 0.35186 0.38101 0.01797  0.02007  -0.01143 126 TYR B CE2 
6489 C CZ  . TYR B 126 ? 0.33101 0.36328 0.38323 0.01456  0.02188  -0.00947 126 TYR B CZ  
6490 O OH  . TYR B 126 ? 0.38335 0.42682 0.43630 0.01946  0.02526  -0.00942 126 TYR B OH  
6500 N N   . GLN B 127 ? 0.34117 0.33020 0.38031 -0.00362 0.01256  -0.00755 127 GLN B N   
6501 C CA  . GLN B 127 ? 0.35432 0.33907 0.38752 -0.00749 0.01394  -0.00494 127 GLN B CA  
6502 C C   . GLN B 127 ? 0.40163 0.39619 0.43728 -0.01261 0.01637  -0.00318 127 GLN B C   
6503 O O   . GLN B 127 ? 0.39959 0.40196 0.44099 -0.01479 0.01589  -0.00363 127 GLN B O   
6504 C CB  . GLN B 127 ? 0.41077 0.38414 0.43926 -0.01037 0.01262  -0.00410 127 GLN B CB  
6505 C CG  . GLN B 127 ? 0.44369 0.40735 0.46634 -0.00575 0.01120  -0.00424 127 GLN B CG  
6506 C CD  . GLN B 127 ? 0.38430 0.34504 0.40004 -0.00368 0.01240  -0.00220 127 GLN B CD  
6507 O OE1 . GLN B 127 ? 0.42933 0.39518 0.44593 0.00039  0.01196  -0.00347 127 GLN B OE1 
6508 N NE2 . GLN B 127 ? 0.44383 0.39498 0.45118 -0.00667 0.01394  0.00095  127 GLN B NE2 
6517 N N   . CYS B 128 ? 0.34768 0.34311 0.37884 -0.01456 0.01888  -0.00113 128 CYS B N   
6518 C CA  . CYS B 128 ? 0.40185 0.40856 0.43472 -0.02057 0.02182  0.00077  128 CYS B CA  
6519 C C   . CYS B 128 ? 0.39529 0.39181 0.41812 -0.02648 0.02386  0.00397  128 CYS B C   
6520 O O   . CYS B 128 ? 0.39263 0.37603 0.40802 -0.02291 0.02304  0.00468  128 CYS B O   
6521 C CB  . CYS B 128 ? 0.39000 0.40983 0.42654 -0.01567 0.02406  0.00010  128 CYS B CB  
6522 S SG  . CYS B 128 ? 0.67982 0.71848 0.72744 -0.01242 0.02419  -0.00150 128 CYS B SG  
6528 N N   . ALA B 129 ? 0.41027 0.41282 0.43229 -0.03542 0.02644  0.00596  129 ALA B N   
6529 C CA  . ALA B 129 ? 0.38342 0.37524 0.39423 -0.04223 0.02923  0.00944  129 ALA B CA  
6530 C C   . ALA B 129 ? 0.35886 0.36721 0.37190 -0.04525 0.03309  0.01099  129 ALA B C   
6531 O O   . ALA B 129 ? 0.39834 0.42704 0.42137 -0.04672 0.03391  0.00976  129 ALA B O   
6532 C CB  . ALA B 129 ? 0.40794 0.39024 0.41324 -0.05322 0.02963  0.01034  129 ALA B CB  
6538 N N   . MET B 130 ? 0.36383 0.36453 0.36712 -0.04610 0.03568  0.01398  130 MET B N   
6539 C CA  . MET B 130 ? 0.37918 0.39495 0.38297 -0.05164 0.04009  0.01595  130 MET B CA  
6540 C C   . MET B 130 ? 0.39689 0.41396 0.39845 -0.06591 0.04219  0.01765  130 MET B C   
6541 O O   . MET B 130 ? 0.37638 0.37222 0.36551 -0.07250 0.04277  0.01998  130 MET B O   
6542 C CB  . MET B 130 ? 0.36916 0.37522 0.36144 -0.04941 0.04240  0.01908  130 MET B CB  
6543 C CG  . MET B 130 ? 0.40287 0.42332 0.39357 -0.05530 0.04762  0.02160  130 MET B CG  
6544 S SD  . MET B 130 ? 0.41126 0.46243 0.41721 -0.04804 0.04885  0.01788  130 MET B SD  
6545 C CE  . MET B 130 ? 0.36775 0.40951 0.37248 -0.03298 0.04540  0.01465  130 MET B CE  
6555 N N   . ARG B 131 ? 0.37810 0.41947 0.39084 -0.07067 0.04322  0.01628  131 ARG B N   
6556 C CA  . ARG B 131 ? 0.32802 0.37347 0.33892 -0.08611 0.04503  0.01731  131 ARG B CA  
6557 C C   . ARG B 131 ? 0.35577 0.39733 0.35546 -0.09684 0.05030  0.02141  131 ARG B C   
6558 O O   . ARG B 131 ? 0.36736 0.41420 0.36537 -0.09203 0.05296  0.02319  131 ARG B O   
6559 C CB  . ARG B 131 ? 0.37784 0.45514 0.40405 -0.08816 0.04478  0.01508  131 ARG B CB  
6560 C CG  . ARG B 131 ? 0.37138 0.45425 0.40826 -0.07738 0.04003  0.01159  131 ARG B CG  
6561 C CD  . ARG B 131 ? 0.42160 0.48295 0.45344 -0.07995 0.03621  0.01016  131 ARG B CD  
6562 N NE  . ARG B 131 ? 0.37578 0.43213 0.40049 -0.09635 0.03766  0.01098  131 ARG B NE  
6563 C CZ  . ARG B 131 ? 0.43219 0.46620 0.44813 -0.10148 0.03575  0.01004  131 ARG B CZ  
6564 N NH1 . ARG B 131 ? 0.38275 0.39989 0.39734 -0.09120 0.03220  0.00845  131 ARG B NH1 
6565 N NH2 . ARG B 131 ? 0.41362 0.44138 0.42087 -0.11769 0.03779  0.01053  131 ARG B NH2 
6579 N N   . PRO B 132 ? 0.39690 0.42969 0.38809 -0.11246 0.05220  0.02281  132 PRO B N   
6580 C CA  . PRO B 132 ? 0.43548 0.46644 0.41583 -0.12487 0.05788  0.02687  132 PRO B CA  
6581 C C   . PRO B 132 ? 0.43055 0.49646 0.42221 -0.12629 0.06139  0.02720  132 PRO B C   
6582 O O   . PRO B 132 ? 0.43532 0.50073 0.41891 -0.13034 0.06606  0.03076  132 PRO B O   
6583 C CB  . PRO B 132 ? 0.43822 0.45767 0.40995 -0.14269 0.05882  0.02679  132 PRO B CB  
6584 C CG  . PRO B 132 ? 0.40186 0.39685 0.37008 -0.13511 0.05379  0.02431  132 PRO B CG  
6585 C CD  . PRO B 132 ? 0.39471 0.41035 0.38116 -0.11882 0.04943  0.02097  132 PRO B CD  
6593 N N   . ASN B 133 ? 0.39796 0.49435 0.40726 -0.12229 0.05954  0.02384  133 ASN B N   
6594 C CA  . ASN B 133 ? 0.39810 0.52937 0.41814 -0.12128 0.06319  0.02409  133 ASN B CA  
6595 C C   . ASN B 133 ? 0.39472 0.53020 0.41955 -0.10257 0.06267  0.02310  133 ASN B C   
6596 O O   . ASN B 133 ? 0.35765 0.52175 0.39237 -0.09736 0.06515  0.02235  133 ASN B O   
6597 C CB  . ASN B 133 ? 0.41648 0.58169 0.45236 -0.12552 0.06200  0.02141  133 ASN B CB  
6598 C CG  . ASN B 133 ? 0.47042 0.63931 0.51746 -0.11064 0.05637  0.01779  133 ASN B CG  
6599 O OD1 . ASN B 133 ? 0.40809 0.55448 0.45151 -0.09818 0.05346  0.01691  133 ASN B OD1 
6600 N ND2 . ASN B 133 ? 0.45668 0.65440 0.51681 -0.11227 0.05474  0.01580  133 ASN B ND2 
6607 N N   . PHE B 134 ? 0.38191 0.48965 0.39899 -0.09262 0.05974  0.02290  134 PHE B N   
6608 C CA  . PHE B 134 ? 0.36762 0.47353 0.38557 -0.07689 0.05908  0.02168  134 PHE B CA  
6609 C C   . PHE B 134 ? 0.37767 0.50065 0.40960 -0.06416 0.05640  0.01751  134 PHE B C   
6610 O O   . PHE B 134 ? 0.42980 0.55739 0.46324 -0.05236 0.05716  0.01595  134 PHE B O   
6611 C CB  . PHE B 134 ? 0.35775 0.47378 0.37100 -0.07713 0.06449  0.02409  134 PHE B CB  
6612 C CG  . PHE B 134 ? 0.38484 0.47823 0.38114 -0.08539 0.06695  0.02866  134 PHE B CG  
6613 C CD1 . PHE B 134 ? 0.42542 0.49192 0.41075 -0.07743 0.06438  0.02956  134 PHE B CD1 
6614 C CD2 . PHE B 134 ? 0.42889 0.52750 0.41923 -0.10133 0.07183  0.03230  134 PHE B CD2 
6615 C CE1 . PHE B 134 ? 0.45929 0.50361 0.42745 -0.08340 0.06655  0.03443  134 PHE B CE1 
6616 C CE2 . PHE B 134 ? 0.45246 0.52650 0.42453 -0.10889 0.07449  0.03716  134 PHE B CE2 
6617 C CZ  . PHE B 134 ? 0.50821 0.55456 0.46900 -0.09894 0.07174  0.03841  134 PHE B CZ  
6627 N N   . THR B 135 ? 0.35896 0.48940 0.39960 -0.06575 0.05329  0.01560  135 THR B N   
6628 C CA  . THR B 135 ? 0.33483 0.47325 0.38539 -0.05231 0.05015  0.01215  135 THR B CA  
6629 C C   . THR B 135 ? 0.36554 0.47809 0.41225 -0.04814 0.04516  0.01063  135 THR B C   
6630 O O   . THR B 135 ? 0.36295 0.45423 0.40045 -0.05517 0.04410  0.01212  135 THR B O   
6631 C CB  . THR B 135 ? 0.35466 0.52175 0.41791 -0.05462 0.04984  0.01124  135 THR B CB  
6632 O OG1 . THR B 135 ? 0.32934 0.49014 0.39124 -0.06716 0.04752  0.01167  135 THR B OG1 
6633 C CG2 . THR B 135 ? 0.39510 0.59276 0.46321 -0.05878 0.05520  0.01277  135 THR B CG2 
6641 N N   . ILE B 136 ? 0.31303 0.42653 0.36568 -0.03622 0.04242  0.00774  136 ILE B N   
6642 C CA  . ILE B 136 ? 0.33510 0.42936 0.38623 -0.03353 0.03777  0.00616  136 ILE B CA  
6643 C C   . ILE B 136 ? 0.34136 0.44952 0.40270 -0.02952 0.03537  0.00435  136 ILE B C   
6644 O O   . ILE B 136 ? 0.32473 0.45238 0.39308 -0.02233 0.03690  0.00366  136 ILE B O   
6645 C CB  . ILE B 136 ? 0.39022 0.46618 0.43560 -0.02376 0.03628  0.00452  136 ILE B CB  
6646 C CG1 . ILE B 136 ? 0.39071 0.47481 0.44143 -0.01175 0.03626  0.00162  136 ILE B CG1 
6647 C CG2 . ILE B 136 ? 0.42605 0.49229 0.46109 -0.02589 0.03884  0.00661  136 ILE B CG2 
6648 C CD1 . ILE B 136 ? 0.38989 0.45536 0.43433 -0.00419 0.03443  -0.00080 136 ILE B CD1 
6660 N N   . LYS B 137 ? 0.32661 0.42485 0.38792 -0.03358 0.03178  0.00377  137 LYS B N   
6661 C CA  . LYS B 137 ? 0.35073 0.46094 0.42054 -0.02990 0.02908  0.00241  137 LYS B CA  
6662 C C   . LYS B 137 ? 0.38108 0.47700 0.44995 -0.01818 0.02667  0.00037  137 LYS B C   
6663 O O   . LYS B 137 ? 0.38529 0.46452 0.45108 -0.01874 0.02363  -0.00057 137 LYS B O   
6664 C CB  . LYS B 137 ? 0.45693 0.56561 0.52654 -0.04118 0.02679  0.00254  137 LYS B CB  
6665 C CG  . LYS B 137 ? 0.49029 0.61406 0.55990 -0.05466 0.02974  0.00427  137 LYS B CG  
6666 C CD  . LYS B 137 ? 0.56833 0.68943 0.63563 -0.06807 0.02792  0.00382  137 LYS B CD  
6667 C CE  . LYS B 137 ? 0.66962 0.81368 0.74728 -0.06693 0.02508  0.00250  137 LYS B CE  
6668 N NZ  . LYS B 137 ? 0.65947 0.83586 0.74455 -0.07393 0.02741  0.00344  137 LYS B NZ  
6682 N N   . GLY B 138 ? 0.34730 0.44873 0.41747 -0.00780 0.02856  -0.00050 138 GLY B N   
6683 C CA  . GLY B 138 ? 0.35227 0.43862 0.41940 0.00193  0.02711  -0.00269 138 GLY B CA  
6684 C C   . GLY B 138 ? 0.35874 0.45217 0.43098 0.00983  0.02563  -0.00335 138 GLY B C   
6685 O O   . GLY B 138 ? 0.35498 0.46602 0.43378 0.00818  0.02501  -0.00207 138 GLY B O   
6689 N N   . SER B 139 ? 0.32079 0.40009 0.38896 0.01827  0.02508  -0.00531 139 SER B N   
6690 C CA  . SER B 139 ? 0.29600 0.37726 0.36583 0.02757  0.02437  -0.00563 139 SER B CA  
6691 C C   . SER B 139 ? 0.35515 0.42781 0.41873 0.03734  0.02726  -0.00768 139 SER B C   
6692 O O   . SER B 139 ? 0.31112 0.36454 0.36777 0.03724  0.02684  -0.00995 139 SER B O   
6693 C CB  . SER B 139 ? 0.33891 0.40582 0.40729 0.02600  0.02066  -0.00613 139 SER B CB  
6694 O OG  . SER B 139 ? 0.36852 0.43552 0.43647 0.03571  0.02054  -0.00593 139 SER B OG  
6700 N N   . PHE B 140 ? 0.31095 0.39872 0.37641 0.04525  0.03045  -0.00716 140 PHE B N   
6701 C CA  . PHE B 140 ? 0.34870 0.42817 0.40669 0.05401  0.03398  -0.00953 140 PHE B CA  
6702 C C   . PHE B 140 ? 0.40527 0.49572 0.46407 0.06729  0.03629  -0.00879 140 PHE B C   
6703 O O   . PHE B 140 ? 0.40901 0.52412 0.47641 0.06842  0.03652  -0.00621 140 PHE B O   
6704 C CB  . PHE B 140 ? 0.35887 0.44650 0.41614 0.05058  0.03710  -0.00986 140 PHE B CB  
6705 C CG  . PHE B 140 ? 0.31990 0.39453 0.37330 0.04044  0.03559  -0.01053 140 PHE B CG  
6706 C CD1 . PHE B 140 ? 0.36699 0.42007 0.41186 0.04128  0.03470  -0.01358 140 PHE B CD1 
6707 C CD2 . PHE B 140 ? 0.32689 0.41136 0.38393 0.03050  0.03551  -0.00811 140 PHE B CD2 
6708 C CE1 . PHE B 140 ? 0.32528 0.36957 0.36673 0.03345  0.03318  -0.01385 140 PHE B CE1 
6709 C CE2 . PHE B 140 ? 0.34511 0.41681 0.39694 0.02301  0.03439  -0.00812 140 PHE B CE2 
6710 C CZ  . PHE B 140 ? 0.34919 0.40251 0.39385 0.02538  0.03312  -0.01087 140 PHE B CZ  
6720 N N   . LEU B 141 ? 0.39062 0.46308 0.43963 0.07722  0.03817  -0.01109 141 LEU B N   
6721 C CA  . LEU B 141 ? 0.42174 0.50069 0.46832 0.09236  0.04119  -0.01046 141 LEU B CA  
6722 C C   . LEU B 141 ? 0.46089 0.53412 0.49890 0.09938  0.04617  -0.01358 141 LEU B C   
6723 O O   . LEU B 141 ? 0.42412 0.48721 0.45776 0.09208  0.04672  -0.01624 141 LEU B O   
6724 C CB  . LEU B 141 ? 0.40399 0.46341 0.44332 0.09960  0.03981  -0.01020 141 LEU B CB  
6725 C CG  . LEU B 141 ? 0.48657 0.55002 0.53307 0.09247  0.03486  -0.00745 141 LEU B CG  
6726 C CD1 . LEU B 141 ? 0.53324 0.57165 0.57022 0.09644  0.03366  -0.00762 141 LEU B CD1 
6727 C CD2 . LEU B 141 ? 0.54511 0.63977 0.60270 0.09645  0.03404  -0.00370 141 LEU B CD2 
6739 N N   A ASN B 142 ? 0.44429 0.52487 0.47930 0.11450  0.04988  -0.01322 142 ASN B N   
6740 N N   B ASN B 142 ? 0.44421 0.52521 0.47941 0.11442  0.04987  -0.01318 142 ASN B N   
6741 C CA  A ASN B 142 ? 0.48065 0.55289 0.50514 0.12320  0.05513  -0.01673 142 ASN B CA  
6742 C CA  B ASN B 142 ? 0.48064 0.55320 0.50526 0.12330  0.05512  -0.01667 142 ASN B CA  
6743 C C   A ASN B 142 ? 0.44822 0.48496 0.45806 0.11984  0.05512  -0.02125 142 ASN B C   
6744 C C   B ASN B 142 ? 0.44809 0.48505 0.45800 0.11995  0.05514  -0.02122 142 ASN B C   
6745 O O   A ASN B 142 ? 0.47518 0.49096 0.47898 0.11969  0.05299  -0.02147 142 ASN B O   
6746 O O   B ASN B 142 ? 0.47573 0.49173 0.47958 0.11986  0.05302  -0.02143 142 ASN B O   
6747 C CB  A ASN B 142 ? 0.49329 0.57278 0.51389 0.14258  0.05903  -0.01568 142 ASN B CB  
6748 C CB  B ASN B 142 ? 0.48423 0.56431 0.50517 0.14266  0.05893  -0.01553 142 ASN B CB  
6749 C CG  A ASN B 142 ? 0.50021 0.58770 0.51571 0.15187  0.06509  -0.01822 142 ASN B CG  
6750 C CG  B ASN B 142 ? 0.54044 0.66150 0.57661 0.14639  0.05922  -0.01135 142 ASN B CG  
6751 O OD1 A ASN B 142 ? 0.59848 0.67284 0.60652 0.14644  0.06697  -0.02216 142 ASN B OD1 
6752 O OD1 B ASN B 142 ? 0.56344 0.70636 0.61169 0.13359  0.05746  -0.00981 142 ASN B OD1 
6753 N ND2 A ASN B 142 ? 0.54821 0.65890 0.56757 0.16658  0.06818  -0.01594 142 ASN B ND2 
6754 N ND2 B ASN B 142 ? 0.51446 0.64595 0.54900 0.16417  0.06173  -0.00954 142 ASN B ND2 
6767 N N   . GLY B 143 ? 0.45410 0.48539 0.45798 0.11625  0.05753  -0.02491 143 GLY B N   
6768 C CA  . GLY B 143 ? 0.45932 0.46106 0.44973 0.11117  0.05738  -0.02978 143 GLY B CA  
6769 C C   . GLY B 143 ? 0.43104 0.43187 0.42628 0.09488  0.05314  -0.03007 143 GLY B C   
6770 O O   . GLY B 143 ? 0.41731 0.39839 0.40280 0.08919  0.05254  -0.03418 143 GLY B O   
6775 N N   . SER B 144 ? 0.37567 0.39711 0.38479 0.08743  0.05024  -0.02590 144 SER B N   
6776 C CA  . SER B 144 ? 0.36579 0.38613 0.37896 0.07371  0.04634  -0.02540 144 SER B CA  
6777 C C   . SER B 144 ? 0.33361 0.36271 0.34616 0.06868  0.04796  -0.02598 144 SER B C   
6778 O O   . SER B 144 ? 0.32374 0.34926 0.33690 0.05883  0.04504  -0.02569 144 SER B O   
6779 C CB  . SER B 144 ? 0.35429 0.38869 0.38017 0.06780  0.04268  -0.02078 144 SER B CB  
6780 O OG  . SER B 144 ? 0.38126 0.44063 0.41553 0.07013  0.04478  -0.01782 144 SER B OG  
6786 N N   . ALA B 145 ? 0.34159 0.38287 0.35264 0.07568  0.05264  -0.02642 145 ALA B N   
6787 C CA  . ALA B 145 ? 0.38271 0.43206 0.39214 0.07065  0.05441  -0.02662 145 ALA B CA  
6788 C C   . ALA B 145 ? 0.37257 0.40179 0.37118 0.06572  0.05284  -0.03071 145 ALA B C   
6789 O O   . ALA B 145 ? 0.34296 0.35315 0.33203 0.06945  0.05301  -0.03504 145 ALA B O   
6790 C CB  . ALA B 145 ? 0.40710 0.47009 0.41411 0.08031  0.06032  -0.02755 145 ALA B CB  
6796 N N   . GLY B 146 ? 0.32060 0.35390 0.31986 0.05686  0.05125  -0.02922 146 GLY B N   
6797 C CA  . GLY B 146 ? 0.32828 0.34660 0.31857 0.05186  0.04894  -0.03259 146 GLY B CA  
6798 C C   . GLY B 146 ? 0.38114 0.39044 0.37471 0.04458  0.04346  -0.03164 146 GLY B C   
6799 O O   . GLY B 146 ? 0.35968 0.36151 0.34761 0.03961  0.04101  -0.03361 146 GLY B O   
6803 N N   . SER B 147 ? 0.34226 0.35323 0.34445 0.04426  0.04146  -0.02888 147 SER B N   
6804 C CA  . SER B 147 ? 0.32782 0.33333 0.33401 0.03718  0.03660  -0.02732 147 SER B CA  
6805 C C   . SER B 147 ? 0.30589 0.31866 0.31375 0.03079  0.03530  -0.02394 147 SER B C   
6806 O O   . SER B 147 ? 0.30961 0.33378 0.31859 0.03078  0.03810  -0.02146 147 SER B O   
6807 C CB  . SER B 147 ? 0.35278 0.36218 0.36811 0.03770  0.03515  -0.02432 147 SER B CB  
6808 O OG  . SER B 147 ? 0.33168 0.33393 0.34459 0.04471  0.03649  -0.02640 147 SER B OG  
6814 N N   . VAL B 148 ? 0.33053 0.33670 0.33747 0.02570  0.03141  -0.02369 148 VAL B N   
6815 C CA  . VAL B 148 ? 0.30570 0.31542 0.31089 0.02136  0.03042  -0.02048 148 VAL B CA  
6816 C C   . VAL B 148 ? 0.30270 0.31054 0.31300 0.01698  0.02718  -0.01690 148 VAL B C   
6817 O O   . VAL B 148 ? 0.30335 0.30635 0.31764 0.01666  0.02480  -0.01788 148 VAL B O   
6818 C CB  . VAL B 148 ? 0.34419 0.34948 0.34033 0.02080  0.02913  -0.02322 148 VAL B CB  
6819 C CG1 . VAL B 148 ? 0.35018 0.35761 0.33917 0.02463  0.03307  -0.02663 148 VAL B CG1 
6820 C CG2 . VAL B 148 ? 0.32230 0.31926 0.31728 0.01919  0.02523  -0.02669 148 VAL B CG2 
6830 N N   . GLY B 149 ? 0.29450 0.30493 0.30303 0.01366  0.02752  -0.01273 149 GLY B N   
6831 C CA  . GLY B 149 ? 0.29789 0.30375 0.30790 0.00982  0.02508  -0.00925 149 GLY B CA  
6832 C C   . GLY B 149 ? 0.29215 0.29264 0.29437 0.00991  0.02309  -0.00798 149 GLY B C   
6833 O O   . GLY B 149 ? 0.32323 0.32614 0.31887 0.01112  0.02446  -0.00789 149 GLY B O   
6837 N N   . PHE B 150 ? 0.28596 0.27997 0.28841 0.00938  0.01989  -0.00689 150 PHE B N   
6838 C CA  . PHE B 150 ? 0.30403 0.29495 0.29944 0.01155  0.01750  -0.00599 150 PHE B CA  
6839 C C   . PHE B 150 ? 0.29914 0.28257 0.29409 0.01153  0.01526  -0.00315 150 PHE B C   
6840 O O   . PHE B 150 ? 0.29639 0.27697 0.29715 0.00958  0.01480  -0.00343 150 PHE B O   
6841 C CB  . PHE B 150 ? 0.33088 0.32511 0.32592 0.01388  0.01507  -0.01114 150 PHE B CB  
6842 C CG  . PHE B 150 ? 0.30868 0.30116 0.31034 0.01330  0.01282  -0.01412 150 PHE B CG  
6843 C CD1 . PHE B 150 ? 0.33289 0.32485 0.33998 0.01236  0.01429  -0.01675 150 PHE B CD1 
6844 C CD2 . PHE B 150 ? 0.35086 0.34283 0.35258 0.01437  0.00949  -0.01401 150 PHE B CD2 
6845 C CE1 . PHE B 150 ? 0.35422 0.34355 0.36621 0.01156  0.01248  -0.01888 150 PHE B CE1 
6846 C CE2 . PHE B 150 ? 0.35100 0.34232 0.35846 0.01326  0.00781  -0.01671 150 PHE B CE2 
6847 C CZ  . PHE B 150 ? 0.33255 0.32167 0.34481 0.01144  0.00934  -0.01888 150 PHE B CZ  
6857 N N   . ASN B 151 ? 0.31261 0.29271 0.29950 0.01444  0.01399  -0.00033 151 ASN B N   
6858 C CA  . ASN B 151 ? 0.31593 0.28921 0.30054 0.01725  0.01151  0.00161  151 ASN B CA  
6859 C C   . ASN B 151 ? 0.34283 0.32304 0.32478 0.02253  0.00819  -0.00011 151 ASN B C   
6860 O O   . ASN B 151 ? 0.35030 0.33793 0.32927 0.02324  0.00809  -0.00164 151 ASN B O   
6861 C CB  . ASN B 151 ? 0.41533 0.37647 0.39023 0.01704  0.01338  0.00764  151 ASN B CB  
6862 C CG  . ASN B 151 ? 0.41599 0.37073 0.39330 0.01026  0.01616  0.00902  151 ASN B CG  
6863 O OD1 . ASN B 151 ? 0.45577 0.40516 0.43639 0.00903  0.01524  0.00828  151 ASN B OD1 
6864 N ND2 . ASN B 151 ? 0.38912 0.34615 0.36483 0.00543  0.01962  0.01079  151 ASN B ND2 
6871 N N   . ILE B 152 ? 0.33449 0.31358 0.31695 0.02624  0.00555  0.00008  152 ILE B N   
6872 C CA  . ILE B 152 ? 0.38340 0.37181 0.36294 0.03185  0.00222  -0.00070 152 ILE B CA  
6873 C C   . ILE B 152 ? 0.56861 0.54869 0.53834 0.03880  0.00183  0.00512  152 ILE B C   
6874 O O   . ILE B 152 ? 0.47593 0.44543 0.44500 0.04011  0.00236  0.00699  152 ILE B O   
6875 C CB  . ILE B 152 ? 0.39787 0.39531 0.38576 0.03145  -0.00048 -0.00547 152 ILE B CB  
6876 C CG1 . ILE B 152 ? 0.38205 0.38145 0.37750 0.02462  0.00075  -0.01044 152 ILE B CG1 
6877 C CG2 . ILE B 152 ? 0.47588 0.48806 0.46150 0.03596  -0.00401 -0.00686 152 ILE B CG2 
6878 C CD1 . ILE B 152 ? 0.41368 0.42064 0.41585 0.02285  -0.00147 -0.01503 152 ILE B CD1 
6890 N N   . ASP B 153 ? 0.59979 0.58174 0.55993 0.04309  0.00156  0.00841  153 ASP B N   
6891 C CA  . ASP B 153 ? 0.72193 0.69605 0.67038 0.05186  0.00095  0.01434  153 ASP B CA  
6892 C C   . ASP B 153 ? 0.76682 0.75803 0.71622 0.05951  -0.00347 0.01277  153 ASP B C   
6893 O O   . ASP B 153 ? 0.71470 0.71942 0.66225 0.06030  -0.00524 0.01161  153 ASP B O   
6894 C CB  . ASP B 153 ? 0.82305 0.78946 0.75904 0.05257  0.00331  0.01965  153 ASP B CB  
6895 C CG  . ASP B 153 ? 1.00983 0.96384 0.94524 0.04368  0.00794  0.02103  153 ASP B CG  
6896 O OD1 . ASP B 153 ? 1.06147 1.00346 0.99891 0.03999  0.00969  0.02147  153 ASP B OD1 
6897 O OD2 . ASP B 153 ? 1.06423 1.02187 0.99672 0.04025  0.00989  0.02163  153 ASP B OD2 
6902 N N   . TYR B 154 ? 0.81150 0.80335 0.76287 0.06541  -0.00517 0.01285  154 TYR B N   
6903 C CA  . TYR B 154 ? 0.87184 0.88429 0.82537 0.07258  -0.00938 0.01121  154 TYR B CA  
6904 C C   . TYR B 154 ? 0.80675 0.83929 0.77165 0.06469  -0.01151 0.00392  154 TYR B C   
6905 O O   . TYR B 154 ? 0.71055 0.74750 0.68543 0.06001  -0.01185 -0.00053 154 TYR B O   
6906 C CB  . TYR B 154 ? 0.97508 0.99153 0.91622 0.08215  -0.01089 0.01640  154 TYR B CB  
6907 C CG  . TYR B 154 ? 1.11151 1.10579 1.03837 0.09116  -0.00866 0.02403  154 TYR B CG  
6908 C CD1 . TYR B 154 ? 1.11855 1.10883 1.04290 0.10109  -0.00935 0.02591  154 TYR B CD1 
6909 C CD2 . TYR B 154 ? 1.13145 1.10757 1.04609 0.08963  -0.00541 0.02929  154 TYR B CD2 
6910 C CE1 . TYR B 154 ? 1.20258 1.16863 1.11120 0.10976  -0.00685 0.03272  154 TYR B CE1 
6911 C CE2 . TYR B 154 ? 1.19797 1.15026 1.09701 0.09694  -0.00287 0.03639  154 TYR B CE2 
6912 C CZ  . TYR B 154 ? 1.28420 1.23020 1.17968 0.10717  -0.00360 0.03798  154 TYR B CZ  
6913 O OH  . TYR B 154 ? 1.42546 1.34415 1.30302 0.11471  -0.00065 0.04478  154 TYR B OH  
6923 N N   . ASP B 155 ? 0.76757 0.81284 0.72939 0.06384  -0.01317 0.00273  155 ASP B N   
6924 C CA  . ASP B 155 ? 0.76529 0.82712 0.73457 0.05557  -0.01490 -0.00448 155 ASP B CA  
6925 C C   . ASP B 155 ? 0.70308 0.75771 0.67053 0.04764  -0.01223 -0.00667 155 ASP B C   
6926 O O   . ASP B 155 ? 0.62679 0.69057 0.59781 0.04044  -0.01290 -0.01289 155 ASP B O   
6927 C CB  . ASP B 155 ? 0.79714 0.88317 0.76429 0.06013  -0.01938 -0.00566 155 ASP B CB  
6928 C CG  . ASP B 155 ? 0.86976 0.97255 0.84379 0.04994  -0.02118 -0.01389 155 ASP B CG  
6929 O OD1 . ASP B 155 ? 0.85012 0.95587 0.83316 0.04477  -0.02117 -0.01789 155 ASP B OD1 
6930 O OD2 . ASP B 155 ? 0.82705 0.93844 0.79628 0.04654  -0.02229 -0.01644 155 ASP B OD2 
6935 N N   . CYS B 156 ? 0.54742 0.58575 0.50849 0.04869  -0.00891 -0.00182 156 CYS B N   
6936 C CA  . CYS B 156 ? 0.52280 0.55683 0.48020 0.04356  -0.00616 -0.00269 156 CYS B CA  
6937 C C   . CYS B 156 ? 0.42752 0.44885 0.39130 0.03694  -0.00232 -0.00415 156 CYS B C   
6938 O O   . CYS B 156 ? 0.44402 0.45334 0.40886 0.03781  -0.00066 -0.00054 156 CYS B O   
6939 C CB  . CYS B 156 ? 0.53735 0.56453 0.48228 0.04934  -0.00493 0.00440  156 CYS B CB  
6940 S SG  . CYS B 156 ? 0.59562 0.62195 0.53405 0.04483  -0.00182 0.00397  156 CYS B SG  
6946 N N   . VAL B 157 ? 0.38127 0.40519 0.34828 0.03076  -0.00086 -0.00945 157 VAL B N   
6947 C CA  . VAL B 157 ? 0.37434 0.38856 0.34652 0.02600  0.00290  -0.01044 157 VAL B CA  
6948 C C   . VAL B 157 ? 0.34060 0.34923 0.30620 0.02601  0.00655  -0.00637 157 VAL B C   
6949 O O   . VAL B 157 ? 0.36099 0.37486 0.32070 0.02593  0.00725  -0.00768 157 VAL B O   
6950 C CB  . VAL B 157 ? 0.36117 0.37877 0.33777 0.02091  0.00337  -0.01759 157 VAL B CB  
6951 C CG1 . VAL B 157 ? 0.34175 0.35049 0.32294 0.01825  0.00741  -0.01755 157 VAL B CG1 
6952 C CG2 . VAL B 157 ? 0.35002 0.37296 0.33260 0.01911  0.00023  -0.02158 157 VAL B CG2 
6962 N N   . SER B 158 ? 0.33090 0.32953 0.29675 0.02536  0.00905  -0.00169 158 SER B N   
6963 C CA  . SER B 158 ? 0.34507 0.33956 0.30475 0.02377  0.01302  0.00228  158 SER B CA  
6964 C C   . SER B 158 ? 0.32061 0.31565 0.28800 0.01892  0.01638  -0.00045 158 SER B C   
6965 O O   . SER B 158 ? 0.31393 0.30406 0.28759 0.01639  0.01715  0.00040  158 SER B O   
6966 C CB  . SER B 158 ? 0.39246 0.37505 0.34530 0.02485  0.01419  0.00938  158 SER B CB  
6967 O OG  . SER B 158 ? 0.50513 0.48745 0.44889 0.03142  0.01143  0.01250  158 SER B OG  
6973 N N   . PHE B 159 ? 0.33239 0.33380 0.29872 0.01823  0.01837  -0.00372 159 PHE B N   
6974 C CA  . PHE B 159 ? 0.30854 0.31201 0.28124 0.01567  0.02194  -0.00606 159 PHE B CA  
6975 C C   . PHE B 159 ? 0.31396 0.31719 0.28446 0.01294  0.02612  -0.00092 159 PHE B C   
6976 O O   . PHE B 159 ? 0.35160 0.35578 0.31330 0.01325  0.02776  0.00208  159 PHE B O   
6977 C CB  . PHE B 159 ? 0.32516 0.33418 0.29559 0.01693  0.02319  -0.01172 159 PHE B CB  
6978 C CG  . PHE B 159 ? 0.31831 0.32686 0.29044 0.01733  0.01992  -0.01765 159 PHE B CG  
6979 C CD1 . PHE B 159 ? 0.30015 0.30516 0.28009 0.01642  0.01979  -0.02050 159 PHE B CD1 
6980 C CD2 . PHE B 159 ? 0.32965 0.34194 0.29494 0.01796  0.01719  -0.02040 159 PHE B CD2 
6981 C CE1 . PHE B 159 ? 0.31987 0.32313 0.30014 0.01539  0.01720  -0.02592 159 PHE B CE1 
6982 C CE2 . PHE B 159 ? 0.34019 0.35302 0.30652 0.01632  0.01438  -0.02632 159 PHE B CE2 
6983 C CZ  . PHE B 159 ? 0.33944 0.34678 0.31302 0.01466  0.01460  -0.02898 159 PHE B CZ  
6993 N N   . CYS B 160 ? 0.32038 0.32338 0.29848 0.00966  0.02787  0.00009  160 CYS B N   
6994 C CA  . CYS B 160 ? 0.29492 0.29873 0.27105 0.00496  0.03176  0.00501  160 CYS B CA  
6995 C C   . CYS B 160 ? 0.32917 0.34397 0.31325 0.00306  0.03537  0.00335  160 CYS B C   
6996 O O   . CYS B 160 ? 0.35940 0.37916 0.34211 -0.00156 0.03915  0.00687  160 CYS B O   
6997 C CB  . CYS B 160 ? 0.30980 0.30315 0.28528 0.00102  0.03071  0.00920  160 CYS B CB  
6998 S SG  . CYS B 160 ? 0.34730 0.33885 0.33413 0.00047  0.02776  0.00608  160 CYS B SG  
7004 N N   . TYR B 161 ? 0.32258 0.34167 0.31401 0.00660  0.03456  -0.00163 161 TYR B N   
7005 C CA  . TYR B 161 ? 0.27748 0.30780 0.27673 0.00641  0.03776  -0.00255 161 TYR B CA  
7006 C C   . TYR B 161 ? 0.29321 0.32610 0.29390 0.01313  0.03822  -0.00815 161 TYR B C   
7007 O O   . TYR B 161 ? 0.29062 0.31495 0.29027 0.01564  0.03499  -0.01164 161 TYR B O   
7008 C CB  . TYR B 161 ? 0.29069 0.32059 0.29821 0.00277  0.03617  -0.00124 161 TYR B CB  
7009 C CG  . TYR B 161 ? 0.29833 0.34319 0.31475 0.00313  0.03894  -0.00185 161 TYR B CG  
7010 C CD1 . TYR B 161 ? 0.31246 0.37018 0.33023 -0.00191 0.04285  0.00132  161 TYR B CD1 
7011 C CD2 . TYR B 161 ? 0.29234 0.33896 0.31508 0.00855  0.03767  -0.00527 161 TYR B CD2 
7012 C CE1 . TYR B 161 ? 0.30968 0.38543 0.33654 -0.00087 0.04519  0.00081  161 TYR B CE1 
7013 C CE2 . TYR B 161 ? 0.31485 0.37602 0.34523 0.01063  0.03981  -0.00539 161 TYR B CE2 
7014 C CZ  . TYR B 161 ? 0.31644 0.39397 0.34954 0.00637  0.04349  -0.00249 161 TYR B CZ  
7015 O OH  . TYR B 161 ? 0.29668 0.39306 0.33842 0.00938  0.04547  -0.00264 161 TYR B OH  
7025 N N   . MET B 162 ? 0.29877 0.34304 0.30068 0.01594  0.04257  -0.00907 162 MET B N   
7026 C CA  . MET B 162 ? 0.29378 0.33899 0.29667 0.02324  0.04384  -0.01408 162 MET B CA  
7027 C C   . MET B 162 ? 0.30521 0.36452 0.31692 0.02537  0.04671  -0.01286 162 MET B C   
7028 O O   . MET B 162 ? 0.29502 0.36857 0.30896 0.02267  0.05013  -0.00976 162 MET B O   
7029 C CB  . MET B 162 ? 0.28061 0.32594 0.27414 0.02755  0.04671  -0.01749 162 MET B CB  
7030 C CG  . MET B 162 ? 0.30006 0.34268 0.29199 0.03570  0.04873  -0.02298 162 MET B CG  
7031 S SD  . MET B 162 ? 0.45485 0.49172 0.43271 0.03989  0.05130  -0.02869 162 MET B SD  
7032 C CE  . MET B 162 ? 0.40383 0.42227 0.37695 0.03659  0.04547  -0.03281 162 MET B CE  
7042 N N   . HIS B 163 ? 0.30410 0.36053 0.32055 0.02992  0.04531  -0.01503 163 HIS B N   
7043 C CA  . HIS B 163 ? 0.28415 0.35552 0.30955 0.03259  0.04711  -0.01345 163 HIS B CA  
7044 C C   . HIS B 163 ? 0.32552 0.40835 0.34925 0.04137  0.05223  -0.01539 163 HIS B C   
7045 O O   . HIS B 163 ? 0.32012 0.39228 0.33590 0.04849  0.05348  -0.01972 163 HIS B O   
7046 C CB  . HIS B 163 ? 0.29367 0.35762 0.32330 0.03567  0.04393  -0.01465 163 HIS B CB  
7047 C CG  . HIS B 163 ? 0.31918 0.40036 0.35786 0.03904  0.04522  -0.01271 163 HIS B CG  
7048 N ND1 . HIS B 163 ? 0.32698 0.42608 0.37297 0.03212  0.04594  -0.00889 163 HIS B ND1 
7049 C CD2 . HIS B 163 ? 0.34525 0.42996 0.38586 0.04886  0.04628  -0.01399 163 HIS B CD2 
7050 C CE1 . HIS B 163 ? 0.32241 0.43823 0.37599 0.03709  0.04687  -0.00806 163 HIS B CE1 
7051 N NE2 . HIS B 163 ? 0.31571 0.42275 0.36618 0.04812  0.04694  -0.01081 163 HIS B NE2 
7059 N N   . HIS B 164 ? 0.29790 0.40281 0.32870 0.04081  0.05537  -0.01246 164 HIS B N   
7060 C CA  . HIS B 164 ? 0.32283 0.44237 0.35329 0.05046  0.06055  -0.01399 164 HIS B CA  
7061 C C   . HIS B 164 ? 0.40129 0.53835 0.44141 0.05702  0.06131  -0.01282 164 HIS B C   
7062 O O   . HIS B 164 ? 0.37964 0.51584 0.41690 0.06986  0.06357  -0.01553 164 HIS B O   
7063 C CB  . HIS B 164 ? 0.30988 0.44564 0.33922 0.04567  0.06492  -0.01178 164 HIS B CB  
7064 C CG  . HIS B 164 ? 0.32553 0.44629 0.34312 0.04336  0.06526  -0.01347 164 HIS B CG  
7065 N ND1 . HIS B 164 ? 0.36516 0.48934 0.37497 0.04962  0.06987  -0.01617 164 HIS B ND1 
7066 C CD2 . HIS B 164 ? 0.30589 0.40925 0.31786 0.03616  0.06140  -0.01288 164 HIS B CD2 
7067 C CE1 . HIS B 164 ? 0.38333 0.49310 0.38317 0.04561  0.06855  -0.01721 164 HIS B CE1 
7068 N NE2 . HIS B 164 ? 0.33069 0.42824 0.33191 0.03790  0.06333  -0.01511 164 HIS B NE2 
7076 N N   . MET B 165 ? 0.31999 0.47363 0.37032 0.04903  0.05985  -0.00891 165 MET B N   
7077 C CA  . MET B 165 ? 0.31894 0.49618 0.37870 0.05585  0.06114  -0.00768 165 MET B CA  
7078 C C   . MET B 165 ? 0.30903 0.49596 0.37851 0.04650  0.05722  -0.00457 165 MET B C   
7079 O O   . MET B 165 ? 0.31063 0.48868 0.37966 0.03350  0.05456  -0.00296 165 MET B O   
7080 C CB  . MET B 165 ? 0.28350 0.48862 0.34642 0.05809  0.06695  -0.00664 165 MET B CB  
7081 C CG  . MET B 165 ? 0.34408 0.56123 0.41050 0.04206  0.06750  -0.00316 165 MET B CG  
7082 S SD  . MET B 165 ? 0.56022 0.80007 0.62460 0.04208  0.07498  -0.00248 165 MET B SD  
7083 C CE  . MET B 165 ? 0.46874 0.72048 0.53762 0.02060  0.07468  0.00248  165 MET B CE  
7093 N N   . GLU B 166 ? 0.30664 0.51447 0.38447 0.05350  0.05733  -0.00361 166 GLU B N   
7094 C CA  . GLU B 166 ? 0.34751 0.56988 0.43496 0.04537  0.05388  -0.00104 166 GLU B CA  
7095 C C   . GLU B 166 ? 0.32919 0.58946 0.42638 0.04147  0.05699  0.00129  166 GLU B C   
7096 O O   . GLU B 166 ? 0.34549 0.62634 0.44536 0.05328  0.06090  0.00100  166 GLU B O   
7097 C CB  . GLU B 166 ? 0.38264 0.60032 0.47192 0.05593  0.05064  -0.00151 166 GLU B CB  
7098 C CG  . GLU B 166 ? 0.32527 0.55798 0.42372 0.04762  0.04667  0.00079  166 GLU B CG  
7099 C CD  . GLU B 166 ? 0.42185 0.64385 0.51981 0.05669  0.04291  0.00057  166 GLU B CD  
7100 O OE1 . GLU B 166 ? 0.41731 0.60850 0.50737 0.05714  0.04070  -0.00109 166 GLU B OE1 
7101 O OE2 . GLU B 166 ? 0.40047 0.64633 0.50581 0.06303  0.04216  0.00228  166 GLU B OE2 
7108 N N   . LEU B 167 ? 0.33913 0.60888 0.44094 0.02500  0.05550  0.00343  167 LEU B N   
7109 C CA  . LEU B 167 ? 0.35298 0.65996 0.46408 0.01753  0.05823  0.00553  167 LEU B CA  
7110 C C   . LEU B 167 ? 0.40374 0.73527 0.52545 0.02145  0.05525  0.00628  167 LEU B C   
7111 O O   . LEU B 167 ? 0.34290 0.65931 0.46383 0.02725  0.05084  0.00562  167 LEU B O   
7112 C CB  . LEU B 167 ? 0.29542 0.59811 0.40411 -0.00365 0.05825  0.00731  167 LEU B CB  
7113 C CG  . LEU B 167 ? 0.36036 0.63971 0.45762 -0.00737 0.06107  0.00737  167 LEU B CG  
7114 C CD1 . LEU B 167 ? 0.36850 0.63490 0.46037 -0.02682 0.06028  0.00949  167 LEU B CD1 
7115 C CD2 . LEU B 167 ? 0.39143 0.69492 0.49004 -0.00306 0.06742  0.00781  167 LEU B CD2 
7127 N N   . PRO B 168 ? 0.36034 0.73192 0.49208 0.01781  0.05753  0.00781  168 PRO B N   
7128 C CA  . PRO B 168 ? 0.36754 0.76728 0.50963 0.02439  0.05472  0.00860  168 PRO B CA  
7129 C C   . PRO B 168 ? 0.40137 0.79391 0.54532 0.01231  0.04877  0.00883  168 PRO B C   
7130 O O   . PRO B 168 ? 0.51515 0.91891 0.66427 0.02116  0.04525  0.00921  168 PRO B O   
7131 C CB  . PRO B 168 ? 0.44283 0.88980 0.59522 0.02023  0.05889  0.01004  168 PRO B CB  
7132 C CG  . PRO B 168 ? 0.44322 0.88401 0.59013 0.00646  0.06353  0.01030  168 PRO B CG  
7133 C CD  . PRO B 168 ? 0.35444 0.74937 0.48802 0.01120  0.06341  0.00882  168 PRO B CD  
7141 N N   . THR B 169 ? 0.36581 0.73944 0.50460 -0.00675 0.04766  0.00870  169 THR B N   
7142 C CA  . THR B 169 ? 0.43518 0.79680 0.57345 -0.01717 0.04217  0.00830  169 THR B CA  
7143 C C   . THR B 169 ? 0.43190 0.75522 0.56239 -0.00825 0.03858  0.00704  169 THR B C   
7144 O O   . THR B 169 ? 0.44035 0.75053 0.56929 -0.01537 0.03415  0.00649  169 THR B O   
7145 C CB  . THR B 169 ? 0.49930 0.85274 0.63291 -0.04033 0.04275  0.00852  169 THR B CB  
7146 O OG1 . THR B 169 ? 0.49585 0.82311 0.61949 -0.04206 0.04614  0.00877  169 THR B OG1 
7147 C CG2 . THR B 169 ? 0.55439 0.94940 0.69658 -0.05267 0.04539  0.00957  169 THR B CG2 
7155 N N   . GLY B 170 ? 0.40084 0.70628 0.52585 0.00646  0.04051  0.00629  170 GLY B N   
7156 C CA  . GLY B 170 ? 0.31629 0.58772 0.43401 0.01389  0.03735  0.00495  170 GLY B CA  
7157 C C   . GLY B 170 ? 0.35265 0.58987 0.46059 0.00491  0.03687  0.00395  170 GLY B C   
7158 O O   . GLY B 170 ? 0.40549 0.61644 0.50798 0.00910  0.03401  0.00273  170 GLY B O   
7162 N N   . VAL B 171 ? 0.36278 0.60050 0.46799 -0.00734 0.03960  0.00471  171 VAL B N   
7163 C CA  . VAL B 171 ? 0.32439 0.53140 0.41927 -0.01344 0.03970  0.00435  171 VAL B CA  
7164 C C   . VAL B 171 ? 0.30986 0.51184 0.39984 -0.00434 0.04363  0.00373  171 VAL B C   
7165 O O   . VAL B 171 ? 0.29741 0.51898 0.39157 0.00565  0.04665  0.00347  171 VAL B O   
7166 C CB  . VAL B 171 ? 0.34438 0.55001 0.43596 -0.03188 0.04053  0.00597  171 VAL B CB  
7167 C CG1 . VAL B 171 ? 0.39478 0.60463 0.48992 -0.04178 0.03660  0.00576  171 VAL B CG1 
7168 C CG2 . VAL B 171 ? 0.36405 0.59469 0.45806 -0.03764 0.04590  0.00771  171 VAL B CG2 
7178 N N   . HIS B 172 ? 0.32346 0.49994 0.40391 -0.00732 0.04369  0.00341  172 HIS B N   
7179 C CA  . HIS B 172 ? 0.31380 0.47974 0.38805 0.00279  0.04598  0.00178  172 HIS B CA  
7180 C C   . HIS B 172 ? 0.30921 0.47002 0.37606 -0.00454 0.04918  0.00324  172 HIS B C   
7181 O O   . HIS B 172 ? 0.32959 0.48283 0.39277 -0.01690 0.04863  0.00545  172 HIS B O   
7182 C CB  . HIS B 172 ? 0.35018 0.49002 0.41936 0.00928  0.04232  -0.00058 172 HIS B CB  
7183 C CG  . HIS B 172 ? 0.32948 0.47307 0.40419 0.01716  0.03975  -0.00156 172 HIS B CG  
7184 N ND1 . HIS B 172 ? 0.30857 0.44490 0.38552 0.01253  0.03545  -0.00124 172 HIS B ND1 
7185 C CD2 . HIS B 172 ? 0.33366 0.48871 0.41142 0.02972  0.04123  -0.00243 172 HIS B CD2 
7186 C CE1 . HIS B 172 ? 0.30167 0.44408 0.38263 0.02168  0.03416  -0.00173 172 HIS B CE1 
7187 N NE2 . HIS B 172 ? 0.31256 0.46588 0.39383 0.03257  0.03761  -0.00228 172 HIS B NE2 
7195 N N   . ALA B 173 ? 0.29991 0.46290 0.36300 0.00359  0.05264  0.00199  173 ALA B N   
7196 C CA  . ALA B 173 ? 0.30043 0.46032 0.35576 -0.00175 0.05604  0.00348  173 ALA B CA  
7197 C C   . ALA B 173 ? 0.30277 0.44582 0.34936 0.00770  0.05636  0.00059  173 ALA B C   
7198 O O   . ALA B 173 ? 0.33320 0.47516 0.38039 0.01939  0.05638  -0.00275 173 ALA B O   
7199 C CB  . ALA B 173 ? 0.31902 0.50748 0.37882 -0.00410 0.06143  0.00517  173 ALA B CB  
7205 N N   . GLY B 174 ? 0.29390 0.42295 0.33113 0.00244  0.05661  0.00189  174 GLY B N   
7206 C CA  . GLY B 174 ? 0.29477 0.40998 0.32322 0.00984  0.05664  -0.00103 174 GLY B CA  
7207 C C   . GLY B 174 ? 0.30758 0.41556 0.32601 0.00356  0.05812  0.00165  174 GLY B C   
7208 O O   . GLY B 174 ? 0.30202 0.41786 0.31972 -0.00554 0.06069  0.00581  174 GLY B O   
7212 N N   . THR B 175 ? 0.30763 0.40063 0.31729 0.00820  0.05660  -0.00072 175 THR B N   
7213 C CA  . THR B 175 ? 0.29939 0.38771 0.29833 0.00498  0.05831  0.00155  175 THR B CA  
7214 C C   . THR B 175 ? 0.31327 0.38115 0.30553 0.00386  0.05328  0.00193  175 THR B C   
7215 O O   . THR B 175 ? 0.31942 0.37824 0.31553 0.00621  0.04903  -0.00047 175 THR B O   
7216 C CB  . THR B 175 ? 0.33995 0.43378 0.33283 0.01257  0.06180  -0.00199 175 THR B CB  
7217 O OG1 . THR B 175 ? 0.33198 0.41344 0.32224 0.02010  0.05867  -0.00757 175 THR B OG1 
7218 C CG2 . THR B 175 ? 0.36421 0.48053 0.36375 0.01589  0.06728  -0.00257 175 THR B CG2 
7226 N N   . ASP B 176 ? 0.34490 0.40668 0.32673 0.00070  0.05395  0.00524  176 ASP B N   
7227 C CA  . ASP B 176 ? 0.35180 0.39831 0.32601 0.00318  0.04952  0.00460  176 ASP B CA  
7228 C C   . ASP B 176 ? 0.34541 0.39319 0.31602 0.01059  0.04926  -0.00128 176 ASP B C   
7229 O O   . ASP B 176 ? 0.34245 0.40028 0.31530 0.01437  0.05287  -0.00454 176 ASP B O   
7230 C CB  . ASP B 176 ? 0.34917 0.38814 0.31217 -0.00146 0.05018  0.01063  176 ASP B CB  
7231 C CG  . ASP B 176 ? 0.39672 0.44471 0.35207 -0.00226 0.05523  0.01247  176 ASP B CG  
7232 O OD1 . ASP B 176 ? 0.37240 0.43026 0.32808 0.00277  0.05743  0.00817  176 ASP B OD1 
7233 O OD2 . ASP B 176 ? 0.41352 0.45712 0.36061 -0.00809 0.05738  0.01855  176 ASP B OD2 
7238 N N   . LEU B 177 ? 0.34077 0.37875 0.30469 0.01271  0.04520  -0.00279 177 LEU B N   
7239 C CA  . LEU B 177 ? 0.36493 0.40261 0.32434 0.01786  0.04448  -0.00911 177 LEU B CA  
7240 C C   . LEU B 177 ? 0.39687 0.44044 0.34609 0.01912  0.04795  -0.00914 177 LEU B C   
7241 O O   . LEU B 177 ? 0.41546 0.45871 0.35898 0.02282  0.04797  -0.01485 177 LEU B O   
7242 C CB  . LEU B 177 ? 0.34242 0.37086 0.29917 0.01853  0.03855  -0.01120 177 LEU B CB  
7243 C CG  . LEU B 177 ? 0.31799 0.34159 0.28306 0.01945  0.03589  -0.01539 177 LEU B CG  
7244 C CD1 . LEU B 177 ? 0.37692 0.40122 0.34084 0.02323  0.03840  -0.02204 177 LEU B CD1 
7245 C CD2 . LEU B 177 ? 0.30926 0.33309 0.28472 0.01700  0.03632  -0.01171 177 LEU B CD2 
7257 N N   . GLU B 178 ? 0.40359 0.45173 0.34916 0.01548  0.05115  -0.00305 178 GLU B N   
7258 C CA  . GLU B 178 ? 0.42863 0.48467 0.36547 0.01641  0.05561  -0.00274 178 GLU B CA  
7259 C C   . GLU B 178 ? 0.43761 0.50726 0.38066 0.01683  0.06166  -0.00336 178 GLU B C   
7260 O O   . GLU B 178 ? 0.46211 0.54080 0.39899 0.01698  0.06639  -0.00238 178 GLU B O   
7261 C CB  . GLU B 178 ? 0.42517 0.47794 0.35210 0.01223  0.05600  0.00468  178 GLU B CB  
7262 C CG  . GLU B 178 ? 0.57669 0.61779 0.49862 0.01376  0.04963  0.00547  178 GLU B CG  
7263 C CD  . GLU B 178 ? 0.62035 0.65618 0.52941 0.01263  0.04933  0.01232  178 GLU B CD  
7264 O OE1 . GLU B 178 ? 0.64136 0.67878 0.54557 0.00837  0.05409  0.01792  178 GLU B OE1 
7265 O OE2 . GLU B 178 ? 0.74130 0.77106 0.64520 0.01592  0.04417  0.01254  178 GLU B OE2 
7272 N N   . GLY B 179 ? 0.42607 0.49896 0.38108 0.01729  0.06165  -0.00464 179 GLY B N   
7273 C CA  . GLY B 179 ? 0.39864 0.48743 0.36038 0.01970  0.06703  -0.00577 179 GLY B CA  
7274 C C   . GLY B 179 ? 0.38166 0.48376 0.34807 0.01230  0.07094  0.00044  179 GLY B C   
7275 O O   . GLY B 179 ? 0.38879 0.50857 0.36052 0.01426  0.07586  -0.00021 179 GLY B O   
7279 N N   . ASN B 180 ? 0.40385 0.49812 0.36727 0.00384  0.06927  0.00633  180 ASN B N   
7280 C CA  . ASN B 180 ? 0.41431 0.51836 0.38001 -0.00569 0.07311  0.01219  180 ASN B CA  
7281 C C   . ASN B 180 ? 0.36017 0.46749 0.33869 -0.00890 0.07106  0.01212  180 ASN B C   
7282 O O   . ASN B 180 ? 0.35137 0.44355 0.33122 -0.00921 0.06587  0.01183  180 ASN B O   
7283 C CB  . ASN B 180 ? 0.41739 0.50674 0.37136 -0.01348 0.07241  0.01867  180 ASN B CB  
7284 C CG  . ASN B 180 ? 0.49829 0.58144 0.43784 -0.00979 0.07292  0.01938  180 ASN B CG  
7285 O OD1 . ASN B 180 ? 0.50137 0.56847 0.43327 -0.00706 0.06823  0.01990  180 ASN B OD1 
7286 N ND2 . ASN B 180 ? 0.42585 0.52269 0.36126 -0.01015 0.07857  0.01997  180 ASN B ND2 
7293 N N   . PHE B 181 ? 0.36018 0.48874 0.34795 -0.01138 0.07507  0.01249  181 PHE B N   
7294 C CA  . PHE B 181 ? 0.33663 0.46996 0.33601 -0.01505 0.07280  0.01259  181 PHE B CA  
7295 C C   . PHE B 181 ? 0.34496 0.46404 0.34039 -0.02693 0.07072  0.01739  181 PHE B C   
7296 O O   . PHE B 181 ? 0.39346 0.50846 0.37937 -0.03541 0.07367  0.02213  181 PHE B O   
7297 C CB  . PHE B 181 ? 0.35298 0.51594 0.36305 -0.01637 0.07752  0.01264  181 PHE B CB  
7298 C CG  . PHE B 181 ? 0.34435 0.51736 0.36316 -0.00368 0.07690  0.00756  181 PHE B CG  
7299 C CD1 . PHE B 181 ? 0.33004 0.50134 0.35780 -0.00193 0.07270  0.00616  181 PHE B CD1 
7300 C CD2 . PHE B 181 ? 0.36655 0.54816 0.38274 0.00717  0.08060  0.00415  181 PHE B CD2 
7301 C CE1 . PHE B 181 ? 0.36710 0.54443 0.40093 0.01081  0.07214  0.00194  181 PHE B CE1 
7302 C CE2 . PHE B 181 ? 0.42573 0.61183 0.44728 0.02004  0.08023  -0.00050 181 PHE B CE2 
7303 C CZ  . PHE B 181 ? 0.40608 0.58952 0.43630 0.02191  0.07595  -0.00130 181 PHE B CZ  
7313 N N   . TYR B 182 ? 0.33000 0.44106 0.33171 -0.02758 0.06612  0.01623  182 TYR B N   
7314 C CA  . TYR B 182 ? 0.33643 0.44036 0.33730 -0.03960 0.06524  0.01989  182 TYR B CA  
7315 C C   . TYR B 182 ? 0.38642 0.51634 0.39754 -0.04699 0.06868  0.02046  182 TYR B C   
7316 O O   . TYR B 182 ? 0.35633 0.50356 0.37939 -0.04041 0.06795  0.01709  182 TYR B O   
7317 C CB  . TYR B 182 ? 0.34939 0.43671 0.35309 -0.03733 0.05922  0.01802  182 TYR B CB  
7318 C CG  . TYR B 182 ? 0.33970 0.40348 0.33357 -0.03140 0.05562  0.01787  182 TYR B CG  
7319 C CD1 . TYR B 182 ? 0.42927 0.47400 0.41065 -0.03701 0.05541  0.02230  182 TYR B CD1 
7320 C CD2 . TYR B 182 ? 0.34279 0.40397 0.33908 -0.02012 0.05259  0.01330  182 TYR B CD2 
7321 C CE1 . TYR B 182 ? 0.44648 0.47324 0.41945 -0.03039 0.05190  0.02239  182 TYR B CE1 
7322 C CE2 . TYR B 182 ? 0.32300 0.36683 0.31099 -0.01547 0.04915  0.01295  182 TYR B CE2 
7323 C CZ  . TYR B 182 ? 0.35268 0.38111 0.32995 -0.02005 0.04863  0.01756  182 TYR B CZ  
7324 O OH  . TYR B 182 ? 0.35042 0.36469 0.31986 -0.01456 0.04506  0.01763  182 TYR B OH  
7334 N N   . GLY B 183 ? 0.37833 0.51083 0.38418 -0.06069 0.07230  0.02478  183 GLY B N   
7335 C CA  . GLY B 183 ? 0.44121 0.60048 0.45637 -0.07021 0.07554  0.02542  183 GLY B CA  
7336 C C   . GLY B 183 ? 0.38630 0.57469 0.40604 -0.06737 0.08131  0.02528  183 GLY B C   
7337 O O   . GLY B 183 ? 0.33495 0.52289 0.35115 -0.05643 0.08277  0.02388  183 GLY B O   
7341 N N   . PRO B 184 ? 0.37559 0.59266 0.40422 -0.07669 0.08460  0.02612  184 PRO B N   
7342 C CA  . PRO B 184 ? 0.39212 0.64064 0.42512 -0.07606 0.09096  0.02659  184 PRO B CA  
7343 C C   . PRO B 184 ? 0.43861 0.71101 0.48434 -0.05880 0.09090  0.02214  184 PRO B C   
7344 O O   . PRO B 184 ? 0.39503 0.70224 0.45196 -0.05917 0.09405  0.02173  184 PRO B O   
7345 C CB  . PRO B 184 ? 0.38478 0.65383 0.42175 -0.09508 0.09398  0.02935  184 PRO B CB  
7346 C CG  . PRO B 184 ? 0.40970 0.67013 0.45246 -0.09887 0.08793  0.02768  184 PRO B CG  
7347 C CD  . PRO B 184 ? 0.42028 0.64127 0.45384 -0.08990 0.08265  0.02676  184 PRO B CD  
7355 N N   . PHE B 185 ? 0.35606 0.60946 0.39963 -0.04372 0.08719  0.01877  185 PHE B N   
7356 C CA  . PHE B 185 ? 0.31343 0.58030 0.36610 -0.02669 0.08640  0.01441  185 PHE B CA  
7357 C C   . PHE B 185 ? 0.39879 0.66379 0.44480 -0.01338 0.08980  0.01188  185 PHE B C   
7358 O O   . PHE B 185 ? 0.41809 0.66525 0.45185 -0.01557 0.09091  0.01289  185 PHE B O   
7359 C CB  . PHE B 185 ? 0.32049 0.56702 0.37594 -0.02089 0.07943  0.01197  185 PHE B CB  
7360 C CG  . PHE B 185 ? 0.35136 0.59941 0.41239 -0.03378 0.07612  0.01391  185 PHE B CG  
7361 C CD1 . PHE B 185 ? 0.36557 0.64654 0.43876 -0.03826 0.07749  0.01446  185 PHE B CD1 
7362 C CD2 . PHE B 185 ? 0.37748 0.59582 0.43106 -0.04148 0.07190  0.01503  185 PHE B CD2 
7363 C CE1 . PHE B 185 ? 0.38387 0.66709 0.46112 -0.05154 0.07454  0.01573  185 PHE B CE1 
7364 C CE2 . PHE B 185 ? 0.36852 0.58690 0.42561 -0.05363 0.06923  0.01628  185 PHE B CE2 
7365 C CZ  . PHE B 185 ? 0.41767 0.66728 0.48605 -0.05931 0.07045  0.01645  185 PHE B CZ  
7375 N N   . VAL B 186 ? 0.35599 0.64058 0.40928 0.00093  0.09177  0.00858  186 VAL B N   
7376 C CA  . VAL B 186 ? 0.41483 0.69821 0.46145 0.01512  0.09538  0.00513  186 VAL B CA  
7377 C C   . VAL B 186 ? 0.39889 0.67428 0.44782 0.03220  0.09272  0.00038  186 VAL B C   
7378 O O   . VAL B 186 ? 0.37077 0.65428 0.42949 0.03487  0.08980  0.00039  186 VAL B O   
7379 C CB  . VAL B 186 ? 0.39373 0.71171 0.44382 0.01643  0.10303  0.00606  186 VAL B CB  
7380 C CG1 . VAL B 186 ? 0.42086 0.74459 0.46664 -0.00166 0.10623  0.01106  186 VAL B CG1 
7381 C CG2 . VAL B 186 ? 0.48111 0.83288 0.54645 0.02214  0.10404  0.00582  186 VAL B CG2 
7391 N N   . ASP B 187 ? 0.39181 0.65003 0.43032 0.04343  0.09379  -0.00372 187 ASP B N   
7392 C CA  . ASP B 187 ? 0.48951 0.73464 0.52676 0.05880  0.09176  -0.00838 187 ASP B CA  
7393 C C   . ASP B 187 ? 0.54662 0.81379 0.58607 0.07463  0.09746  -0.01082 187 ASP B C   
7394 O O   . ASP B 187 ? 0.62204 0.87741 0.65140 0.08713  0.10014  -0.01539 187 ASP B O   
7395 C CB  . ASP B 187 ? 0.44752 0.65892 0.47108 0.06127  0.08923  -0.01215 187 ASP B CB  
7396 C CG  . ASP B 187 ? 0.41900 0.62926 0.43111 0.06258  0.09387  -0.01387 187 ASP B CG  
7397 O OD1 . ASP B 187 ? 0.43331 0.66760 0.44737 0.06080  0.09939  -0.01174 187 ASP B OD1 
7398 O OD2 . ASP B 187 ? 0.45183 0.63724 0.45245 0.06481  0.09186  -0.01753 187 ASP B OD2 
7403 N N   . ARG B 188 ? 0.56593 0.86600 0.61834 0.07396  0.09931  -0.00785 188 ARG B N   
7404 C CA  . ARG B 188 ? 0.59814 0.92324 0.65429 0.09098  0.10450  -0.00964 188 ARG B CA  
7405 C C   . ARG B 188 ? 0.69719 1.04795 0.76848 0.09207  0.10224  -0.00684 188 ARG B C   
7406 O O   . ARG B 188 ? 0.58700 0.93997 0.66551 0.07656  0.09792  -0.00353 188 ARG B O   
7407 C CB  . ARG B 188 ? 0.64489 0.99436 0.69926 0.09060  0.11197  -0.00923 188 ARG B CB  
7408 C CG  . ARG B 188 ? 0.62216 0.99643 0.68471 0.07140  0.11327  -0.00399 188 ARG B CG  
7409 C CD  . ARG B 188 ? 0.66542 1.04737 0.71999 0.06705  0.11960  -0.00361 188 ARG B CD  
7410 N NE  . ARG B 188 ? 0.75059 1.17558 0.81370 0.07223  0.12643  -0.00270 188 ARG B NE  
7411 C CZ  . ARG B 188 ? 0.73305 1.18661 0.80496 0.05716  0.12808  0.00176  188 ARG B CZ  
7412 N NH1 . ARG B 188 ? 0.68737 1.13457 0.76023 0.03680  0.12573  0.00575  188 ARG B NH1 
7413 N NH2 . ARG B 188 ? 0.69226 1.17209 0.76949 0.06130  0.12988  0.00213  188 ARG B NH2 
7427 N N   . GLN B 189 ? 0.80121 1.16903 0.87579 0.11056  0.10493  -0.00829 189 GLN B N   
7428 C CA  . GLN B 189 ? 0.88736 1.28460 0.97638 0.11362  0.10296  -0.00550 189 GLN B CA  
7429 C C   . GLN B 189 ? 0.76798 1.20551 0.86724 0.10300  0.10584  -0.00222 189 GLN B C   
7430 O O   . GLN B 189 ? 0.71192 1.16504 0.80985 0.11127  0.10865  -0.00262 189 GLN B O   
7431 C CB  . GLN B 189 ? 0.89357 1.28716 0.97925 0.13651  0.10288  -0.00745 189 GLN B CB  
7432 C CG  . GLN B 189 ? 0.99532 1.34932 1.07099 0.14527  0.09982  -0.01028 189 GLN B CG  
7433 C CD  . GLN B 189 ? 1.10322 1.45241 1.17583 0.16475  0.09826  -0.01053 189 GLN B CD  
7434 O OE1 . GLN B 189 ? 1.05460 1.42495 1.12958 0.17308  0.09899  -0.00901 189 GLN B OE1 
7435 N NE2 . GLN B 189 ? 1.02645 1.34523 1.09227 0.17097  0.09544  -0.01204 189 GLN B NE2 
7444 N N   . THR B 190 ? 0.73958 1.18765 0.84656 0.08234  0.10416  0.00097  190 THR B N   
7445 C CA  . THR B 190 ? 0.64994 1.12923 0.76530 0.06662  0.10465  0.00436  190 THR B CA  
7446 C C   . THR B 190 ? 0.63172 1.11816 0.75683 0.05166  0.09927  0.00689  190 THR B C   
7447 O O   . THR B 190 ? 0.62556 1.08772 0.74922 0.05197  0.09480  0.00624  190 THR B O   
7448 C CB  . THR B 190 ? 0.67638 1.15460 0.78523 0.05240  0.10993  0.00548  190 THR B CB  
7449 O OG1 . THR B 190 ? 0.66308 1.17017 0.77887 0.03708  0.11036  0.00862  190 THR B OG1 
7450 C CG2 . THR B 190 ? 0.67015 1.11266 0.77079 0.03801  0.10679  0.00627  190 THR B CG2 
7458 N N   . ALA B 191 ? 0.58959 1.10435 0.72245 0.03859  0.09812  0.00937  191 ALA B N   
7459 C CA  . ALA B 191 ? 0.59620 1.11753 0.73662 0.02276  0.09296  0.01121  191 ALA B CA  
7460 C C   . ALA B 191 ? 0.46066 0.96166 0.59609 0.00210  0.09408  0.01261  191 ALA B C   
7461 O O   . ALA B 191 ? 0.46633 0.96958 0.59675 -0.01150 0.09815  0.01427  191 ALA B O   
7462 C CB  . ALA B 191 ? 0.50326 1.06000 0.65114 0.01414  0.09155  0.01284  191 ALA B CB  
7468 N N   . GLN B 192 ? 0.46924 0.94123 0.60208 -0.00046 0.08851  0.01209  192 GLN B N   
7469 C CA  . GLN B 192 ? 0.46455 0.90052 0.58709 -0.01765 0.08598  0.01313  192 GLN B CA  
7470 C C   . GLN B 192 ? 0.45496 0.88303 0.58135 -0.02704 0.07948  0.01334  192 GLN B C   
7471 O O   . GLN B 192 ? 0.43777 0.86688 0.56961 -0.01465 0.07533  0.01188  192 GLN B O   
7472 C CB  . GLN B 192 ? 0.46814 0.86084 0.57739 -0.00786 0.08482  0.01130  192 GLN B CB  
7473 C CG  . GLN B 192 ? 0.45858 0.85667 0.56329 0.00638  0.09049  0.00977  192 GLN B CG  
7474 C CD  . GLN B 192 ? 0.46333 0.82043 0.55390 0.01166  0.08938  0.00788  192 GLN B CD  
7475 O OE1 . GLN B 192 ? 0.35365 0.69020 0.43568 -0.00146 0.08892  0.00968  192 GLN B OE1 
7476 N NE2 . GLN B 192 ? 0.45490 0.79925 0.54191 0.03038  0.08887  0.00432  192 GLN B NE2 
7485 N N   . ALA B 193 ? 0.38735 0.80477 0.50914 -0.04856 0.07875  0.01513  193 ALA B N   
7486 C CA  . ALA B 193 ? 0.49269 0.90108 0.61658 -0.05820 0.07284  0.01482  193 ALA B CA  
7487 C C   . ALA B 193 ? 0.47880 0.84495 0.58909 -0.07144 0.07082  0.01560  193 ALA B C   
7488 O O   . ALA B 193 ? 0.53210 0.88519 0.63248 -0.08075 0.07465  0.01754  193 ALA B O   
7489 C CB  . ALA B 193 ? 0.47963 0.92745 0.61400 -0.07328 0.07329  0.01571  193 ALA B CB  
7495 N N   . ALA B 194 ? 0.48516 0.83051 0.59448 -0.07145 0.06488  0.01429  194 ALA B N   
7496 C CA  . ALA B 194 ? 0.53754 0.84635 0.63463 -0.08437 0.06280  0.01497  194 ALA B CA  
7497 C C   . ALA B 194 ? 0.58504 0.90463 0.67972 -0.10781 0.06513  0.01670  194 ALA B C   
7498 O O   . ALA B 194 ? 0.48626 0.83517 0.59060 -0.11554 0.06407  0.01594  194 ALA B O   
7499 C CB  . ALA B 194 ? 0.50932 0.79840 0.60703 -0.07900 0.05625  0.01289  194 ALA B CB  
7505 N N   . GLY B 195 ? 0.60751 0.90248 0.68811 -0.11941 0.06826  0.01905  195 GLY B N   
7506 C CA  . GLY B 195 ? 0.56785 0.86295 0.64152 -0.14305 0.07076  0.02077  195 GLY B CA  
7507 C C   . GLY B 195 ? 0.58422 0.86032 0.65375 -0.15325 0.06601  0.01909  195 GLY B C   
7508 O O   . GLY B 195 ? 0.51118 0.76913 0.58160 -0.14226 0.06070  0.01701  195 GLY B O   
7512 N N   . THR B 196 ? 0.54058 0.82003 0.60421 -0.17582 0.06827  0.01981  196 THR B N   
7513 C CA  . THR B 196 ? 0.56287 0.82067 0.61952 -0.18692 0.06437  0.01784  196 THR B CA  
7514 C C   . THR B 196 ? 0.52893 0.73713 0.57061 -0.17924 0.06237  0.01849  196 THR B C   
7515 O O   . THR B 196 ? 0.53475 0.71912 0.56308 -0.18052 0.06599  0.02165  196 THR B O   
7516 C CB  . THR B 196 ? 0.61396 0.87499 0.66165 -0.21405 0.06813  0.01855  196 THR B CB  
7517 O OG1 . THR B 196 ? 0.59416 0.89836 0.65424 -0.21546 0.06783  0.01718  196 THR B OG1 
7518 C CG2 . THR B 196 ? 0.59811 0.83400 0.63656 -0.22440 0.06399  0.01571  196 THR B CG2 
7526 N N   . ASP B 197 ? 0.53482 0.72929 0.57864 -0.17102 0.05665  0.01571  197 ASP B N   
7527 C CA  . ASP B 197 ? 0.50425 0.65566 0.53543 -0.16296 0.05437  0.01594  197 ASP B CA  
7528 C C   . ASP B 197 ? 0.59822 0.72055 0.61331 -0.17989 0.05444  0.01551  197 ASP B C   
7529 O O   . ASP B 197 ? 0.55474 0.69091 0.57019 -0.19717 0.05505  0.01398  197 ASP B O   
7530 C CB  . ASP B 197 ? 0.47120 0.62205 0.51223 -0.14437 0.04870  0.01324  197 ASP B CB  
7531 C CG  . ASP B 197 ? 0.42392 0.54034 0.45568 -0.13093 0.04742  0.01412  197 ASP B CG  
7532 O OD1 . ASP B 197 ? 0.43803 0.53660 0.45769 -0.13363 0.05103  0.01718  197 ASP B OD1 
7533 O OD2 . ASP B 197 ? 0.43061 0.54034 0.46718 -0.11816 0.04305  0.01196  197 ASP B OD2 
7538 N N   . THR B 198 ? 0.50483 0.58662 0.50425 -0.17537 0.05435  0.01698  198 THR B N   
7539 C CA  . THR B 198 ? 0.52885 0.57640 0.51015 -0.18781 0.05459  0.01655  198 THR B CA  
7540 C C   . THR B 198 ? 0.53536 0.55517 0.51289 -0.17246 0.05006  0.01505  198 THR B C   
7541 O O   . THR B 198 ? 0.47720 0.50154 0.46377 -0.15428 0.04756  0.01508  198 THR B O   
7542 C CB  . THR B 198 ? 0.53210 0.55462 0.49315 -0.19954 0.06057  0.02098  198 THR B CB  
7543 O OG1 . THR B 198 ? 0.54814 0.55955 0.50606 -0.18425 0.06165  0.02453  198 THR B OG1 
7544 C CG2 . THR B 198 ? 0.58125 0.63212 0.54498 -0.21859 0.06560  0.02223  198 THR B CG2 
7552 N N   . THR B 199 ? 0.51673 0.50769 0.48015 -0.18007 0.04925  0.01347  199 THR B N   
7553 C CA  . THR B 199 ? 0.48310 0.44844 0.44214 -0.16646 0.04528  0.01180  199 THR B CA  
7554 C C   . THR B 199 ? 0.51153 0.44043 0.45246 -0.15942 0.04751  0.01559  199 THR B C   
7555 O O   . THR B 199 ? 0.48816 0.39663 0.41158 -0.17059 0.05212  0.01868  199 THR B O   
7556 C CB  . THR B 199 ? 0.56616 0.52002 0.51890 -0.17693 0.04328  0.00767  199 THR B CB  
7557 O OG1 . THR B 199 ? 0.50107 0.49183 0.47160 -0.18127 0.04055  0.00448  199 THR B OG1 
7558 C CG2 . THR B 199 ? 0.51913 0.44731 0.46682 -0.16297 0.03965  0.00582  199 THR B CG2 
7566 N N   . ILE B 200 ? 0.48856 0.40959 0.43299 -0.14083 0.04429  0.01553  200 ILE B N   
7567 C CA  . ILE B 200 ? 0.47604 0.36855 0.40543 -0.13176 0.04586  0.01940  200 ILE B CA  
7568 C C   . ILE B 200 ? 0.50269 0.35857 0.41346 -0.13323 0.04577  0.01870  200 ILE B C   
7569 O O   . ILE B 200 ? 0.46261 0.31077 0.37571 -0.12161 0.04205  0.01626  200 ILE B O   
7570 C CB  . ILE B 200 ? 0.43928 0.34132 0.37979 -0.11236 0.04267  0.01952  200 ILE B CB  
7571 C CG1 . ILE B 200 ? 0.39091 0.32875 0.34937 -0.11066 0.04293  0.01925  200 ILE B CG1 
7572 C CG2 . ILE B 200 ? 0.48319 0.36013 0.40789 -0.10439 0.04445  0.02397  200 ILE B CG2 
7573 C CD1 . ILE B 200 ? 0.38077 0.33137 0.35351 -0.09315 0.03864  0.01692  200 ILE B CD1 
7585 N N   . THR B 201 ? 0.52709 0.35849 0.41755 -0.14691 0.05040  0.02114  201 THR B N   
7586 C CA  . THR B 201 ? 0.53988 0.33523 0.41027 -0.15150 0.05124  0.01981  201 THR B CA  
7587 C C   . THR B 201 ? 0.55762 0.32776 0.41913 -0.13226 0.04931  0.02101  201 THR B C   
7588 O O   . THR B 201 ? 0.54947 0.30518 0.40690 -0.12795 0.04710  0.01750  201 THR B O   
7589 C CB  . THR B 201 ? 0.62767 0.39913 0.47572 -0.16883 0.05737  0.02312  201 THR B CB  
7590 O OG1 . THR B 201 ? 0.59686 0.39941 0.45655 -0.18562 0.05902  0.02220  201 THR B OG1 
7591 C CG2 . THR B 201 ? 0.64251 0.37660 0.46842 -0.17722 0.05887  0.02071  201 THR B CG2 
7599 N N   . VAL B 202 ? 0.55222 0.31697 0.40943 -0.12077 0.05032  0.02599  202 VAL B N   
7600 C CA  . VAL B 202 ? 0.55702 0.29989 0.40485 -0.10271 0.04865  0.02757  202 VAL B CA  
7601 C C   . VAL B 202 ? 0.51170 0.27392 0.37853 -0.08971 0.04301  0.02303  202 VAL B C   
7602 O O   . VAL B 202 ? 0.52892 0.27341 0.38861 -0.07945 0.04138  0.02176  202 VAL B O   
7603 C CB  . VAL B 202 ? 0.63938 0.37723 0.47988 -0.09302 0.05036  0.03386  202 VAL B CB  
7604 C CG1 . VAL B 202 ? 0.59676 0.37219 0.45929 -0.08936 0.04846  0.03375  202 VAL B CG1 
7605 C CG2 . VAL B 202 ? 0.65122 0.36841 0.48146 -0.07376 0.04840  0.03563  202 VAL B CG2 
7615 N N   . ASN B 203 ? 0.47113 0.26855 0.36089 -0.09085 0.04041  0.02038  203 ASN B N   
7616 C CA  . ASN B 203 ? 0.43801 0.25442 0.34577 -0.07964 0.03535  0.01626  203 ASN B CA  
7617 C C   . ASN B 203 ? 0.46379 0.27481 0.37134 -0.08555 0.03383  0.01152  203 ASN B C   
7618 O O   . ASN B 203 ? 0.45312 0.26046 0.36316 -0.07501 0.03093  0.00915  203 ASN B O   
7619 C CB  . ASN B 203 ? 0.46901 0.32079 0.39811 -0.07908 0.03373  0.01525  203 ASN B CB  
7620 C CG  . ASN B 203 ? 0.45393 0.31240 0.38500 -0.06931 0.03410  0.01858  203 ASN B CG  
7621 O OD1 . ASN B 203 ? 0.43317 0.27150 0.34941 -0.06446 0.03577  0.02238  203 ASN B OD1 
7622 N ND2 . ASN B 203 ? 0.39989 0.28584 0.34801 -0.06591 0.03260  0.01714  203 ASN B ND2 
7629 N N   . VAL B 204 ? 0.47119 0.28392 0.37603 -0.10253 0.03578  0.01007  204 VAL B N   
7630 C CA  . VAL B 204 ? 0.47671 0.28187 0.37823 -0.10956 0.03454  0.00539  204 VAL B CA  
7631 C C   . VAL B 204 ? 0.52081 0.28853 0.40157 -0.10303 0.03567  0.00537  204 VAL B C   
7632 O O   . VAL B 204 ? 0.48133 0.24462 0.36315 -0.09677 0.03318  0.00169  204 VAL B O   
7633 C CB  . VAL B 204 ? 0.49302 0.30359 0.39127 -0.13088 0.03696  0.00402  204 VAL B CB  
7634 C CG1 . VAL B 204 ? 0.53374 0.33487 0.42636 -0.13915 0.03554  -0.00146 204 VAL B CG1 
7635 C CG2 . VAL B 204 ? 0.45980 0.30998 0.37928 -0.13466 0.03574  0.00400  204 VAL B CG2 
7645 N N   . LEU B 205 ? 0.53210 0.27159 0.39235 -0.10419 0.03981  0.00960  205 LEU B N   
7646 C CA  . LEU B 205 ? 0.56862 0.27083 0.40715 -0.09626 0.04131  0.00990  205 LEU B CA  
7647 C C   . LEU B 205 ? 0.56316 0.27070 0.40961 -0.07493 0.03780  0.00991  205 LEU B C   
7648 O O   . LEU B 205 ? 0.57819 0.27055 0.41763 -0.06728 0.03694  0.00716  205 LEU B O   
7649 C CB  . LEU B 205 ? 0.62507 0.29541 0.43907 -0.09921 0.04653  0.01552  205 LEU B CB  
7650 C CG  . LEU B 205 ? 0.61995 0.27748 0.42038 -0.12234 0.05102  0.01541  205 LEU B CG  
7651 C CD1 . LEU B 205 ? 0.68215 0.31507 0.46201 -0.12458 0.05618  0.02229  205 LEU B CD1 
7652 C CD2 . LEU B 205 ? 0.62482 0.25642 0.40889 -0.13141 0.05219  0.01033  205 LEU B CD2 
7664 N N   . ALA B 206 ? 0.52692 0.25630 0.38723 -0.06551 0.03599  0.01279  206 ALA B N   
7665 C CA  . ALA B 206 ? 0.50274 0.24217 0.37246 -0.04720 0.03245  0.01245  206 ALA B CA  
7666 C C   . ALA B 206 ? 0.53521 0.28990 0.41901 -0.04589 0.02892  0.00679  206 ALA B C   
7667 O O   . ALA B 206 ? 0.53055 0.27844 0.41208 -0.03418 0.02743  0.00517  206 ALA B O   
7668 C CB  . ALA B 206 ? 0.51727 0.28205 0.40167 -0.04154 0.03089  0.01509  206 ALA B CB  
7674 N N   . TRP B 207 ? 0.47295 0.24925 0.37092 -0.05755 0.02770  0.00394  207 TRP B N   
7675 C CA  . TRP B 207 ? 0.48139 0.27362 0.39273 -0.05660 0.02428  -0.00092 207 TRP B CA  
7676 C C   . TRP B 207 ? 0.48392 0.25346 0.38113 -0.06072 0.02516  -0.00444 207 TRP B C   
7677 O O   . TRP B 207 ? 0.48853 0.26140 0.39040 -0.05349 0.02284  -0.00769 207 TRP B O   
7678 C CB  . TRP B 207 ? 0.47810 0.29958 0.40683 -0.06652 0.02290  -0.00214 207 TRP B CB  
7679 C CG  . TRP B 207 ? 0.48335 0.32176 0.42430 -0.06902 0.01978  -0.00653 207 TRP B CG  
7680 C CD1 . TRP B 207 ? 0.46550 0.32221 0.42139 -0.05953 0.01638  -0.00818 207 TRP B CD1 
7681 C CD2 . TRP B 207 ? 0.48176 0.32202 0.42079 -0.08296 0.01984  -0.00959 207 TRP B CD2 
7682 N NE1 . TRP B 207 ? 0.46684 0.33515 0.42934 -0.06589 0.01438  -0.01167 207 TRP B NE1 
7683 C CE2 . TRP B 207 ? 0.48261 0.34256 0.43553 -0.08013 0.01621  -0.01271 207 TRP B CE2 
7684 C CE3 . TRP B 207 ? 0.53319 0.36032 0.45915 -0.09844 0.02268  -0.01004 207 TRP B CE3 
7685 C CZ2 . TRP B 207 ? 0.50101 0.36918 0.45549 -0.09118 0.01497  -0.01612 207 TRP B CZ2 
7686 C CZ3 . TRP B 207 ? 0.56736 0.40339 0.49531 -0.11059 0.02147  -0.01394 207 TRP B CZ3 
7687 C CH2 . TRP B 207 ? 0.49387 0.35100 0.43622 -0.10645 0.01746  -0.01690 207 TRP B CH2 
7698 N N   . LEU B 208 ? 0.50877 0.25391 0.38729 -0.07264 0.02884  -0.00401 208 LEU B N   
7699 C CA  . LEU B 208 ? 0.55366 0.27150 0.41459 -0.07574 0.03029  -0.00764 208 LEU B CA  
7700 C C   . LEU B 208 ? 0.58446 0.28060 0.43345 -0.05783 0.03091  -0.00659 208 LEU B C   
7701 O O   . LEU B 208 ? 0.60939 0.29622 0.45351 -0.05296 0.03029  -0.01050 208 LEU B O   
7702 C CB  . LEU B 208 ? 0.58229 0.27546 0.42314 -0.09304 0.03464  -0.00730 208 LEU B CB  
7703 C CG  . LEU B 208 ? 0.57005 0.28565 0.42112 -0.11287 0.03417  -0.00940 208 LEU B CG  
7704 C CD1 . LEU B 208 ? 0.57691 0.26653 0.40606 -0.13092 0.03912  -0.00865 208 LEU B CD1 
7705 C CD2 . LEU B 208 ? 0.58079 0.31409 0.44289 -0.11806 0.03050  -0.01569 208 LEU B CD2 
7717 N N   . TYR B 209 ? 0.60052 0.29157 0.44567 -0.04690 0.03192  -0.00138 209 TYR B N   
7718 C CA  . TYR B 209 ? 0.59018 0.26790 0.42711 -0.02793 0.03187  -0.00016 209 TYR B CA  
7719 C C   . TYR B 209 ? 0.62255 0.32791 0.47975 -0.01740 0.02758  -0.00314 209 TYR B C   
7720 O O   . TYR B 209 ? 0.60186 0.29868 0.45370 -0.00710 0.02737  -0.00547 209 TYR B O   
7721 C CB  . TYR B 209 ? 0.62555 0.29679 0.45554 -0.01851 0.03326  0.00630  209 TYR B CB  
7722 C CG  . TYR B 209 ? 0.71503 0.34745 0.51691 -0.02350 0.03841  0.00981  209 TYR B CG  
7723 C CD1 . TYR B 209 ? 0.83221 0.42914 0.61028 -0.01559 0.04125  0.00937  209 TYR B CD1 
7724 C CD2 . TYR B 209 ? 0.67344 0.30332 0.47114 -0.03628 0.04089  0.01349  209 TYR B CD2 
7725 C CE1 . TYR B 209 ? 0.88324 0.44398 0.63449 -0.02007 0.04613  0.01257  209 TYR B CE1 
7726 C CE2 . TYR B 209 ? 0.77053 0.36216 0.54026 -0.04223 0.04617  0.01704  209 TYR B CE2 
7727 C CZ  . TYR B 209 ? 0.88997 0.44822 0.63713 -0.03388 0.04852  0.01642  209 TYR B CZ  
7728 O OH  . TYR B 209 ? 0.92281 0.45577 0.64772 -0.03820 0.05260  0.01910  209 TYR B OH  
7738 N N   . ALA B 210 ? 0.52155 0.25951 0.40110 -0.01961 0.02450  -0.00304 210 ALA B N   
7739 C CA  . ALA B 210 ? 0.53659 0.29928 0.43420 -0.01194 0.02082  -0.00588 210 ALA B CA  
7740 C C   . ALA B 210 ? 0.48420 0.24415 0.38131 -0.01677 0.02020  -0.01111 210 ALA B C   
7741 O O   . ALA B 210 ? 0.51644 0.28158 0.41736 -0.00734 0.01878  -0.01351 210 ALA B O   
7742 C CB  . ALA B 210 ? 0.47722 0.27048 0.39567 -0.01641 0.01835  -0.00529 210 ALA B CB  
7748 N N   . ALA B 211 ? 0.51095 0.26451 0.40337 -0.03206 0.02129  -0.01301 211 ALA B N   
7749 C CA  . ALA B 211 ? 0.55228 0.30342 0.44294 -0.03805 0.02057  -0.01821 211 ALA B CA  
7750 C C   . ALA B 211 ? 0.57412 0.29643 0.44532 -0.02956 0.02290  -0.02005 211 ALA B C   
7751 O O   . ALA B 211 ? 0.55651 0.28283 0.43036 -0.02339 0.02165  -0.02361 211 ALA B O   
7752 C CB  . ALA B 211 ? 0.55779 0.30685 0.44469 -0.05705 0.02148  -0.01983 211 ALA B CB  
7758 N N   . VAL B 212 ? 0.58319 0.27565 0.43373 -0.02804 0.02661  -0.01737 212 VAL B N   
7759 C CA  . VAL B 212 ? 0.65028 0.31221 0.47967 -0.01820 0.02939  -0.01890 212 VAL B CA  
7760 C C   . VAL B 212 ? 0.63957 0.31351 0.47652 0.00201  0.02783  -0.01804 212 VAL B C   
7761 O O   . VAL B 212 ? 0.68697 0.35445 0.51852 0.01005  0.02824  -0.02161 212 VAL B O   
7762 C CB  . VAL B 212 ? 0.71265 0.33762 0.51626 -0.02008 0.03406  -0.01545 212 VAL B CB  
7763 C CG1 . VAL B 212 ? 0.80254 0.39663 0.58430 -0.00496 0.03702  -0.01614 212 VAL B CG1 
7764 C CG2 . VAL B 212 ? 0.68046 0.29088 0.47350 -0.04178 0.03609  -0.01809 212 VAL B CG2 
7774 N N   . ILE B 213 ? 0.59564 0.28958 0.44571 0.00981  0.02598  -0.01371 213 ILE B N   
7775 C CA  . ILE B 213 ? 0.64737 0.35757 0.50630 0.02723  0.02419  -0.01306 213 ILE B CA  
7776 C C   . ILE B 213 ? 0.63288 0.36563 0.50753 0.02663  0.02156  -0.01783 213 ILE B C   
7777 O O   . ILE B 213 ? 0.60608 0.34299 0.48090 0.03916  0.02145  -0.01945 213 ILE B O   
7778 C CB  . ILE B 213 ? 0.64995 0.38068 0.52146 0.03191  0.02224  -0.00836 213 ILE B CB  
7779 C CG1 . ILE B 213 ? 0.68483 0.39185 0.53783 0.03789  0.02505  -0.00300 213 ILE B CG1 
7780 C CG2 . ILE B 213 ? 0.63340 0.39203 0.52106 0.04438  0.01927  -0.00901 213 ILE B CG2 
7781 C CD1 . ILE B 213 ? 0.73051 0.45561 0.59394 0.03865  0.02341  0.00140  213 ILE B CD1 
7793 N N   . ASN B 214 ? 0.52016 0.26890 0.40798 0.01264  0.01954  -0.01986 214 ASN B N   
7794 C CA  . ASN B 214 ? 0.53317 0.30109 0.43401 0.01052  0.01720  -0.02392 214 ASN B CA  
7795 C C   . ASN B 214 ? 0.61327 0.36400 0.50169 0.00459  0.01861  -0.02880 214 ASN B C   
7796 O O   . ASN B 214 ? 0.60954 0.37563 0.50774 0.00005  0.01661  -0.03209 214 ASN B O   
7797 C CB  . ASN B 214 ? 0.53437 0.32781 0.45422 0.00030  0.01433  -0.02335 214 ASN B CB  
7798 C CG  . ASN B 214 ? 0.56841 0.38426 0.50338 0.00808  0.01236  -0.02069 214 ASN B CG  
7799 O OD1 . ASN B 214 ? 0.57406 0.40722 0.51987 0.01335  0.01064  -0.02224 214 ASN B OD1 
7800 N ND2 . ASN B 214 ? 0.58464 0.39945 0.51898 0.00900  0.01285  -0.01680 214 ASN B ND2 
7807 N N   . GLY B 215 ? 0.61161 0.32992 0.47751 0.00432  0.02209  -0.02941 215 GLY B N   
7808 C CA  . GLY B 215 ? 0.65378 0.35398 0.50580 0.00002  0.02368  -0.03478 215 GLY B CA  
7809 C C   . GLY B 215 ? 0.70075 0.39959 0.55165 -0.01977 0.02302  -0.03769 215 GLY B C   
7810 O O   . GLY B 215 ? 0.73620 0.42513 0.57801 -0.02538 0.02356  -0.04286 215 GLY B O   
7814 N N   . ASP B 216 ? 0.64346 0.35275 0.50261 -0.03056 0.02198  -0.03473 216 ASP B N   
7815 C CA  . ASP B 216 ? 0.63300 0.34643 0.49291 -0.04955 0.02115  -0.03717 216 ASP B CA  
7816 C C   . ASP B 216 ? 0.76323 0.44541 0.60161 -0.05860 0.02513  -0.03612 216 ASP B C   
7817 O O   . ASP B 216 ? 0.74822 0.43127 0.58842 -0.05982 0.02605  -0.03127 216 ASP B O   
7818 C CB  . ASP B 216 ? 0.67396 0.42232 0.55783 -0.05427 0.01769  -0.03440 216 ASP B CB  
7819 C CG  . ASP B 216 ? 0.71152 0.47806 0.60370 -0.06824 0.01509  -0.03776 216 ASP B CG  
7820 O OD1 . ASP B 216 ? 0.73881 0.49031 0.61736 -0.07746 0.01599  -0.04235 216 ASP B OD1 
7821 O OD2 . ASP B 216 ? 0.66764 0.46341 0.57913 -0.06978 0.01218  -0.03585 216 ASP B OD2 
7826 N N   . ARG B 217 ? 0.69399 0.34873 0.51146 -0.06629 0.02762  -0.04086 217 ARG B N   
7827 C CA  . ARG B 217 ? 0.77954 0.39945 0.57235 -0.07128 0.03214  -0.03984 217 ARG B CA  
7828 C C   . ARG B 217 ? 0.69736 0.31398 0.48176 -0.09079 0.03274  -0.04336 217 ARG B C   
7829 O O   . ARG B 217 ? 0.78459 0.37703 0.54948 -0.09369 0.03633  -0.04251 217 ARG B O   
7830 C CB  . ARG B 217 ? 0.84407 0.44058 0.62060 -0.05375 0.03478  -0.04004 217 ARG B CB  
7831 C CG  . ARG B 217 ? 0.87418 0.47424 0.65687 -0.03320 0.03453  -0.03612 217 ARG B CG  
7832 C CD  . ARG B 217 ? 0.92086 0.50471 0.69010 -0.01582 0.03667  -0.03722 217 ARG B CD  
7833 N NE  . ARG B 217 ? 0.98151 0.53652 0.72752 -0.01629 0.04065  -0.03562 217 ARG B NE  
7834 C CZ  . ARG B 217 ? 0.99392 0.53474 0.72942 -0.00462 0.04300  -0.02994 217 ARG B CZ  
7835 N NH1 . ARG B 217 ? 0.97639 0.53047 0.72299 0.00838  0.04156  -0.02539 217 ARG B NH1 
7836 N NH2 . ARG B 217 ? 1.01118 0.52373 0.72351 -0.00576 0.04690  -0.02884 217 ARG B NH2 
7850 N N   . TRP B 218 ? 0.70693 0.34681 0.50409 -0.10370 0.02940  -0.04741 218 TRP B N   
7851 C CA  . TRP B 218 ? 0.79071 0.42924 0.57923 -0.12088 0.02965  -0.05151 218 TRP B CA  
7852 C C   . TRP B 218 ? 0.74404 0.37690 0.52483 -0.13479 0.03223  -0.04846 218 TRP B C   
7853 O O   . TRP B 218 ? 0.75414 0.37469 0.51998 -0.14646 0.03418  -0.05116 218 TRP B O   
7854 C CB  . TRP B 218 ? 0.78598 0.45549 0.59142 -0.13101 0.02498  -0.05578 218 TRP B CB  
7855 C CG  . TRP B 218 ? 0.74780 0.44753 0.57420 -0.13775 0.02216  -0.05297 218 TRP B CG  
7856 C CD1 . TRP B 218 ? 0.68799 0.41651 0.53746 -0.12538 0.01871  -0.05004 218 TRP B CD1 
7857 C CD2 . TRP B 218 ? 0.72473 0.43993 0.55612 -0.15374 0.02223  -0.05098 218 TRP B CD2 
7858 N NE1 . TRP B 218 ? 0.65503 0.41302 0.52200 -0.13267 0.01681  -0.04663 218 TRP B NE1 
7859 C CE2 . TRP B 218 ? 0.70403 0.45276 0.55940 -0.15163 0.01907  -0.04776 218 TRP B CE2 
7860 C CE3 . TRP B 218 ? 0.73479 0.44187 0.55355 -0.16801 0.02483  -0.05108 218 TRP B CE3 
7861 C CZ2 . TRP B 218 ? 0.67512 0.44691 0.54080 -0.16458 0.01867  -0.04539 218 TRP B CZ2 
7862 C CZ3 . TRP B 218 ? 0.70637 0.43731 0.53568 -0.18151 0.02433  -0.04883 218 TRP B CZ3 
7863 C CH2 . TRP B 218 ? 0.71641 0.47873 0.56869 -0.18028 0.02137  -0.04622 218 TRP B CH2 
7874 N N   . PHE B 219 ? 0.73785 0.37830 0.52711 -0.13378 0.03265  -0.04301 219 PHE B N   
7875 C CA  . PHE B 219 ? 0.77007 0.40943 0.55420 -0.14736 0.03510  -0.03985 219 PHE B CA  
7876 C C   . PHE B 219 ? 0.77650 0.38087 0.53786 -0.14076 0.04003  -0.03613 219 PHE B C   
7877 O O   . PHE B 219 ? 0.72621 0.32423 0.47899 -0.15177 0.04284  -0.03354 219 PHE B O   
7878 C CB  . PHE B 219 ? 0.72192 0.38833 0.52668 -0.14942 0.03331  -0.03568 219 PHE B CB  
7879 C CG  . PHE B 219 ? 0.63889 0.30186 0.45002 -0.13100 0.03292  -0.03200 219 PHE B CG  
7880 C CD1 . PHE B 219 ? 0.66178 0.30250 0.46077 -0.12118 0.03629  -0.02667 219 PHE B CD1 
7881 C CD2 . PHE B 219 ? 0.67077 0.35710 0.50110 -0.12132 0.02883  -0.03339 219 PHE B CD2 
7882 C CE1 . PHE B 219 ? 0.65502 0.29397 0.45939 -0.10324 0.03570  -0.02332 219 PHE B CE1 
7883 C CE2 . PHE B 219 ? 0.61823 0.31105 0.45815 -0.10160 0.02781  -0.02947 219 PHE B CE2 
7884 C CZ  . PHE B 219 ? 0.65936 0.32942 0.48664 -0.09258 0.03108  -0.02467 219 PHE B CZ  
7894 N N   . LEU B 220 ? 0.72203 0.30453 0.47303 -0.12264 0.04130  -0.03553 220 LEU B N   
7895 C CA  . LEU B 220 ? 0.79458 0.34396 0.52198 -0.11696 0.04603  -0.03211 220 LEU B CA  
7896 C C   . LEU B 220 ? 0.80310 0.33322 0.51007 -0.13114 0.04892  -0.03598 220 LEU B C   
7897 O O   . LEU B 220 ? 0.78488 0.32093 0.49259 -0.13840 0.04732  -0.04193 220 LEU B O   
7898 C CB  . LEU B 220 ? 0.80475 0.33744 0.52523 -0.09334 0.04677  -0.03059 220 LEU B CB  
7899 C CG  . LEU B 220 ? 0.76454 0.31499 0.50329 -0.07840 0.04415  -0.02681 220 LEU B CG  
7900 C CD1 . LEU B 220 ? 0.82463 0.36193 0.55633 -0.05544 0.04486  -0.02576 220 LEU B CD1 
7901 C CD2 . LEU B 220 ? 0.75343 0.30633 0.49439 -0.08155 0.04538  -0.02029 220 LEU B CD2 
7913 N N   . ASN B 221 ? 0.81429 0.32147 0.50244 -0.13564 0.05328  -0.03238 221 ASN B N   
7914 C CA  . ASN B 221 ? 0.82812 0.31259 0.49310 -0.15001 0.05693  -0.03559 221 ASN B CA  
7915 C C   . ASN B 221 ? 0.84817 0.29336 0.48566 -0.14059 0.06222  -0.03175 221 ASN B C   
7916 O O   . ASN B 221 ? 0.82978 0.26964 0.46829 -0.12410 0.06266  -0.02633 221 ASN B O   
7917 C CB  . ASN B 221 ? 0.82182 0.32483 0.49215 -0.17422 0.05671  -0.03692 221 ASN B CB  
7918 C CG  . ASN B 221 ? 0.80960 0.32152 0.48540 -0.17998 0.05796  -0.03113 221 ASN B CG  
7919 O OD1 . ASN B 221 ? 0.84006 0.33276 0.50605 -0.16875 0.06062  -0.02572 221 ASN B OD1 
7920 N ND2 . ASN B 221 ? 0.85464 0.39582 0.54496 -0.19729 0.05628  -0.03204 221 ASN B ND2 
7927 N N   . ARG B 222 ? 0.84218 0.26109 0.45520 -0.15098 0.06611  -0.03457 222 ARG B N   
7928 C CA  . ARG B 222 ? 0.88610 0.26508 0.46989 -0.14330 0.07155  -0.03140 222 ARG B CA  
7929 C C   . ARG B 222 ? 0.90068 0.27217 0.47653 -0.15176 0.07460  -0.02592 222 ARG B C   
7930 O O   . ARG B 222 ? 0.93620 0.27520 0.48821 -0.14418 0.07908  -0.02221 222 ARG B O   
7931 C CB  . ARG B 222 ? 0.92871 0.28016 0.48695 -0.15325 0.07508  -0.03679 222 ARG B CB  
7932 C CG  . ARG B 222 ? 0.94808 0.30054 0.49844 -0.18042 0.07701  -0.03909 222 ARG B CG  
7933 C CD  . ARG B 222 ? 1.00103 0.31782 0.51923 -0.19051 0.08188  -0.04358 222 ARG B CD  
7934 N NE  . ARG B 222 ? 1.00449 0.31343 0.51881 -0.18052 0.08095  -0.04848 222 ARG B NE  
7935 C CZ  . ARG B 222 ? 1.04354 0.31488 0.53131 -0.16891 0.08515  -0.04900 222 ARG B CZ  
7936 N NH1 . ARG B 222 ? 1.08373 0.32013 0.54542 -0.16478 0.09056  -0.04471 222 ARG B NH1 
7937 N NH2 . ARG B 222 ? 1.04292 0.31178 0.52997 -0.16045 0.08397  -0.05381 222 ARG B NH2 
7951 N N   . PHE B 223 ? 0.87551 0.27610 0.47001 -0.16643 0.07246  -0.02517 223 PHE B N   
7952 C CA  . PHE B 223 ? 0.89548 0.28844 0.47963 -0.17939 0.07599  -0.02128 223 PHE B CA  
7953 C C   . PHE B 223 ? 0.87765 0.27588 0.47065 -0.16553 0.07565  -0.01381 223 PHE B C   
7954 O O   . PHE B 223 ? 0.86551 0.28550 0.48019 -0.15201 0.07162  -0.01237 223 PHE B O   
7955 C CB  . PHE B 223 ? 0.88077 0.30427 0.47938 -0.20368 0.07426  -0.02453 223 PHE B CB  
7956 C CG  . PHE B 223 ? 0.89789 0.31907 0.48829 -0.21798 0.07425  -0.03191 223 PHE B CG  
7957 C CD1 . PHE B 223 ? 0.94924 0.33453 0.50816 -0.22709 0.07945  -0.03396 223 PHE B CD1 
7958 C CD2 . PHE B 223 ? 0.86508 0.31802 0.47750 -0.22147 0.06916  -0.03684 223 PHE B CD2 
7959 C CE1 . PHE B 223 ? 0.96698 0.34913 0.51701 -0.24035 0.07957  -0.04095 223 PHE B CE1 
7960 C CE2 . PHE B 223 ? 0.88171 0.33281 0.48591 -0.23418 0.06902  -0.04360 223 PHE B CE2 
7961 C CZ  . PHE B 223 ? 0.93274 0.34845 0.50570 -0.24386 0.07425  -0.04574 223 PHE B CZ  
7971 N N   . THR B 224 ? 0.90721 0.28407 0.48187 -0.16873 0.08007  -0.00907 224 THR B N   
7972 C CA  . THR B 224 ? 0.94033 0.32512 0.52351 -0.15952 0.07988  -0.00187 224 THR B CA  
7973 C C   . THR B 224 ? 0.89981 0.29201 0.48150 -0.18012 0.08233  0.00011  224 THR B C   
7974 O O   . THR B 224 ? 0.92477 0.31289 0.49642 -0.19997 0.08441  -0.00395 224 THR B O   
7975 C CB  . THR B 224 ? 0.98213 0.33364 0.54395 -0.13857 0.08290  0.00343  224 THR B CB  
7976 O OG1 . THR B 224 ? 1.14194 0.50696 0.71617 -0.12763 0.08158  0.01015  224 THR B OG1 
7977 C CG2 . THR B 224 ? 0.99283 0.30729 0.52205 -0.14780 0.08907  0.00461  224 THR B CG2 
7985 N N   . THR B 225 ? 0.95877 0.36185 0.54941 -0.17559 0.08231  0.00641  225 THR B N   
7986 C CA  . THR B 225 ? 0.99729 0.41094 0.58846 -0.19462 0.08466  0.00854  225 THR B CA  
7987 C C   . THR B 225 ? 0.99567 0.39797 0.57965 -0.18444 0.08711  0.01680  225 THR B C   
7988 O O   . THR B 225 ? 1.03308 0.42196 0.61294 -0.16278 0.08655  0.02071  225 THR B O   
7989 C CB  . THR B 225 ? 0.96537 0.42537 0.58748 -0.20705 0.08062  0.00603  225 THR B CB  
7990 O OG1 . THR B 225 ? 0.99438 0.46550 0.61555 -0.22657 0.08333  0.00752  225 THR B OG1 
7991 C CG2 . THR B 225 ? 0.89801 0.38111 0.54376 -0.19055 0.07686  0.01008  225 THR B CG2 
7999 N N   . THR B 226 ? 1.03055 0.43832 0.61176 -0.20015 0.08998  0.01946  226 THR B N   
8000 C CA  . THR B 226 ? 1.09023 0.49554 0.66958 -0.19249 0.09177  0.02743  226 THR B CA  
8001 C C   . THR B 226 ? 1.02409 0.47211 0.63320 -0.19697 0.08889  0.02940  226 THR B C   
8002 O O   . THR B 226 ? 0.98531 0.46432 0.61287 -0.21234 0.08692  0.02495  226 THR B O   
8003 C CB  . THR B 226 ? 1.07478 0.45370 0.62786 -0.20520 0.09774  0.03023  226 THR B CB  
8004 O OG1 . THR B 226 ? 1.12781 0.52990 0.68928 -0.23028 0.09854  0.02689  226 THR B OG1 
8005 C CG2 . THR B 226 ? 1.11519 0.44986 0.63653 -0.20191 0.10119  0.02789  226 THR B CG2 
8013 N N   . LEU B 227 ? 1.08069 0.52939 0.69216 -0.18370 0.08916  0.03651  227 LEU B N   
8014 C CA  . LEU B 227 ? 1.01054 0.49562 0.64622 -0.18680 0.08752  0.03953  227 LEU B CA  
8015 C C   . LEU B 227 ? 0.95097 0.45656 0.59173 -0.21139 0.08988  0.03800  227 LEU B C   
8016 O O   . LEU B 227 ? 0.89697 0.44087 0.56250 -0.21994 0.08742  0.03559  227 LEU B O   
8017 C CB  . LEU B 227 ? 1.01212 0.48677 0.64072 -0.17159 0.08900  0.04802  227 LEU B CB  
8018 C CG  . LEU B 227 ? 0.96381 0.47340 0.61722 -0.16801 0.08663  0.05114  227 LEU B CG  
8019 C CD1 . LEU B 227 ? 0.93713 0.46555 0.61116 -0.16050 0.08140  0.04596  227 LEU B CD1 
8020 C CD2 . LEU B 227 ? 1.02491 0.52173 0.66925 -0.14973 0.08744  0.05930  227 LEU B CD2 
8032 N N   . ASN B 228 ? 1.03691 0.51812 0.65402 -0.22292 0.09473  0.03915  228 ASN B N   
8033 C CA  . ASN B 228 ? 0.97340 0.47421 0.59383 -0.24646 0.09729  0.03789  228 ASN B CA  
8034 C C   . ASN B 228 ? 1.00473 0.52476 0.63489 -0.26228 0.09508  0.02952  228 ASN B C   
8035 O O   . ASN B 228 ? 0.96034 0.51767 0.60921 -0.27692 0.09422  0.02746  228 ASN B O   
8036 C CB  . ASN B 228 ? 1.05753 0.52380 0.64758 -0.25473 0.10324  0.04112  228 ASN B CB  
8037 C CG  . ASN B 228 ? 1.13516 0.62349 0.72891 -0.27753 0.10630  0.04136  228 ASN B CG  
8038 O OD1 . ASN B 228 ? 1.21102 0.72901 0.82242 -0.27819 0.10618  0.04527  228 ASN B OD1 
8039 N ND2 . ASN B 228 ? 1.17386 0.64785 0.74998 -0.29625 0.10934  0.03718  228 ASN B ND2 
8046 N N   . ASP B 229 ? 1.12294 0.61803 0.73913 -0.25961 0.09442  0.02470  229 ASP B N   
8047 C CA  . ASP B 229 ? 1.01850 0.52982 0.64186 -0.27362 0.09218  0.01676  229 ASP B CA  
8048 C C   . ASP B 229 ? 0.97124 0.52343 0.62721 -0.26821 0.08634  0.01412  229 ASP B C   
8049 O O   . ASP B 229 ? 0.97920 0.56591 0.65205 -0.28260 0.08432  0.00989  229 ASP B O   
8050 C CB  . ASP B 229 ? 1.04020 0.51276 0.63961 -0.26926 0.09316  0.01281  229 ASP B CB  
8051 C CG  . ASP B 229 ? 1.18941 0.62268 0.75496 -0.27923 0.09931  0.01393  229 ASP B CG  
8052 O OD1 . ASP B 229 ? 1.22860 0.67071 0.79094 -0.29678 0.10234  0.01520  229 ASP B OD1 
8053 O OD2 . ASP B 229 ? 1.19920 0.59254 0.74076 -0.26892 0.10135  0.01376  229 ASP B OD2 
8058 N N   . PHE B 230 ? 0.87904 0.42861 0.54377 -0.24729 0.08360  0.01666  230 PHE B N   
8059 C CA  . PHE B 230 ? 0.90436 0.49077 0.59889 -0.24193 0.07833  0.01437  230 PHE B CA  
8060 C C   . PHE B 230 ? 0.92913 0.55659 0.64590 -0.25083 0.07808  0.01667  230 PHE B C   
8061 O O   . PHE B 230 ? 0.89734 0.56102 0.63485 -0.25964 0.07510  0.01254  230 PHE B O   
8062 C CB  . PHE B 230 ? 0.85026 0.42576 0.54872 -0.21828 0.07590  0.01714  230 PHE B CB  
8063 C CG  . PHE B 230 ? 0.76266 0.37385 0.49020 -0.21291 0.07102  0.01534  230 PHE B CG  
8064 C CD1 . PHE B 230 ? 0.87527 0.49706 0.61252 -0.21362 0.06715  0.00887  230 PHE B CD1 
8065 C CD2 . PHE B 230 ? 0.76826 0.40298 0.51286 -0.20800 0.07052  0.01997  230 PHE B CD2 
8066 C CE1 . PHE B 230 ? 0.80799 0.46181 0.57110 -0.20888 0.06275  0.00720  230 PHE B CE1 
8067 C CE2 . PHE B 230 ? 0.77321 0.43996 0.54352 -0.20360 0.06639  0.01810  230 PHE B CE2 
8068 C CZ  . PHE B 230 ? 0.75067 0.42667 0.53026 -0.20398 0.06242  0.01171  230 PHE B CZ  
8078 N N   . ASN B 231 ? 0.87412 0.49700 0.58599 -0.24834 0.08142  0.02339  231 ASN B N   
8079 C CA  . ASN B 231 ? 0.93487 0.59614 0.66679 -0.25501 0.08188  0.02614  231 ASN B CA  
8080 C C   . ASN B 231 ? 0.90842 0.59560 0.64538 -0.27713 0.08300  0.02241  231 ASN B C   
8081 O O   . ASN B 231 ? 0.92289 0.65289 0.68348 -0.28250 0.08143  0.02161  231 ASN B O   
8082 C CB  . ASN B 231 ? 0.87491 0.52227 0.59635 -0.24882 0.08588  0.03415  231 ASN B CB  
8083 C CG  . ASN B 231 ? 0.86964 0.51083 0.59619 -0.22742 0.08398  0.03842  231 ASN B CG  
8084 O OD1 . ASN B 231 ? 0.85603 0.51903 0.60275 -0.22025 0.08001  0.03614  231 ASN B OD1 
8085 N ND2 . ASN B 231 ? 0.86010 0.47178 0.56787 -0.21684 0.08669  0.04459  231 ASN B ND2 
8092 N N   . LEU B 232 ? 0.96386 0.62654 0.67827 -0.28982 0.08590  0.02018  232 LEU B N   
8093 C CA  . LEU B 232 ? 0.97819 0.66564 0.69601 -0.31152 0.08680  0.01622  232 LEU B CA  
8094 C C   . LEU B 232 ? 0.99213 0.71417 0.73157 -0.31508 0.08161  0.00975  232 LEU B C   
8095 O O   . LEU B 232 ? 0.97627 0.74163 0.73562 -0.32453 0.08034  0.00830  232 LEU B O   
8096 C CB  . LEU B 232 ? 1.02037 0.67047 0.70722 -0.32412 0.09086  0.01444  232 LEU B CB  
8097 C CG  . LEU B 232 ? 1.15617 0.77234 0.81967 -0.32247 0.09641  0.02100  232 LEU B CG  
8098 C CD1 . LEU B 232 ? 1.21452 0.78902 0.84489 -0.33362 0.10055  0.01887  232 LEU B CD1 
8099 C CD2 . LEU B 232 ? 1.12963 0.77402 0.80374 -0.33054 0.09901  0.02558  232 LEU B CD2 
8111 N N   . VAL B 233 ? 0.95823 0.66330 0.69478 -0.30587 0.07846  0.00610  233 VAL B N   
8112 C CA  . VAL B 233 ? 0.93678 0.67261 0.69278 -0.30786 0.07334  0.00024  233 VAL B CA  
8113 C C   . VAL B 233 ? 0.89930 0.67174 0.68486 -0.29632 0.06975  0.00218  233 VAL B C   
8114 O O   . VAL B 233 ? 0.91096 0.72551 0.71793 -0.30215 0.06674  -0.00066 233 VAL B O   
8115 C CB  . VAL B 233 ? 0.95552 0.66095 0.69836 -0.30112 0.07146  -0.00408 233 VAL B CB  
8116 C CG1 . VAL B 233 ? 0.94514 0.68212 0.70733 -0.30314 0.06616  -0.00987 233 VAL B CG1 
8117 C CG2 . VAL B 233 ? 1.04431 0.71185 0.75602 -0.31231 0.07566  -0.00600 233 VAL B CG2 
8127 N N   . ALA B 234 ? 0.87450 0.63170 0.66091 -0.27934 0.07006  0.00703  234 ALA B N   
8128 C CA  . ALA B 234 ? 0.90377 0.69050 0.71569 -0.26743 0.06679  0.00845  234 ALA B CA  
8129 C C   . ALA B 234 ? 0.85050 0.67965 0.68142 -0.27416 0.06789  0.01077  234 ALA B C   
8130 O O   . ALA B 234 ? 0.75841 0.62577 0.61356 -0.27145 0.06459  0.00908  234 ALA B O   
8131 C CB  . ALA B 234 ? 0.88898 0.64775 0.69428 -0.24869 0.06741  0.01332  234 ALA B CB  
8137 N N   . MET B 235 ? 0.87890 0.70176 0.69895 -0.28125 0.07270  0.01499  235 MET B N   
8138 C CA  . MET B 235 ? 0.82837 0.69167 0.66490 -0.28785 0.07436  0.01709  235 MET B CA  
8139 C C   . MET B 235 ? 0.81605 0.72073 0.66876 -0.29992 0.07159  0.01166  235 MET B C   
8140 O O   . MET B 235 ? 0.78685 0.73490 0.66153 -0.29940 0.07084  0.01213  235 MET B O   
8141 C CB  . MET B 235 ? 1.00175 0.84738 0.81979 -0.29625 0.08012  0.02165  235 MET B CB  
8142 C CG  . MET B 235 ? 1.13607 1.02123 0.96889 -0.30234 0.08266  0.02433  235 MET B CG  
8143 S SD  . MET B 235 ? 1.49239 1.35243 1.30143 -0.31120 0.08965  0.03026  235 MET B SD  
8144 C CE  . MET B 235 ? 1.17028 1.00207 0.97233 -0.29063 0.09127  0.03774  235 MET B CE  
8154 N N   . LYS B 236 ? 0.80177 0.69447 0.64286 -0.31051 0.07030  0.00657  236 LYS B N   
8155 C CA  . LYS B 236 ? 0.76488 0.69641 0.61932 -0.32200 0.06744  0.00148  236 LYS B CA  
8156 C C   . LYS B 236 ? 0.77664 0.73842 0.65519 -0.31123 0.06175  -0.00122 236 LYS B C   
8157 O O   . LYS B 236 ? 0.75504 0.75848 0.65000 -0.31676 0.05913  -0.00407 236 LYS B O   
8158 C CB  . LYS B 236 ? 0.82259 0.73035 0.65564 -0.33637 0.06783  -0.00334 236 LYS B CB  
8159 C CG  . LYS B 236 ? 0.89481 0.76919 0.70099 -0.34814 0.07367  -0.00113 236 LYS B CG  
8160 C CD  . LYS B 236 ? 0.95005 0.80798 0.73655 -0.36474 0.07412  -0.00684 236 LYS B CD  
8161 C CE  . LYS B 236 ? 0.99757 0.81551 0.75402 -0.37552 0.08005  -0.00496 236 LYS B CE  
8162 N NZ  . LYS B 236 ? 1.09485 0.89282 0.82974 -0.39133 0.08099  -0.01069 236 LYS B NZ  
8176 N N   . TYR B 237 ? 0.66954 0.61170 0.54995 -0.29568 0.05974  -0.00032 237 TYR B N   
8177 C CA  . TYR B 237 ? 0.74079 0.70921 0.64329 -0.28470 0.05463  -0.00242 237 TYR B CA  
8178 C C   . TYR B 237 ? 0.63165 0.61800 0.55145 -0.27115 0.05509  0.00202  237 TYR B C   
8179 O O   . TYR B 237 ? 0.60265 0.59945 0.53688 -0.25931 0.05148  0.00107  237 TYR B O   
8180 C CB  . TYR B 237 ? 0.68313 0.61969 0.57609 -0.27764 0.05170  -0.00554 237 TYR B CB  
8181 C CG  . TYR B 237 ? 0.70581 0.63212 0.58485 -0.29053 0.05077  -0.01088 237 TYR B CG  
8182 C CD1 . TYR B 237 ? 0.78560 0.67541 0.63828 -0.30009 0.05480  -0.01095 237 TYR B CD1 
8183 C CD2 . TYR B 237 ? 0.74963 0.70271 0.64105 -0.29284 0.04599  -0.01576 237 TYR B CD2 
8184 C CE1 . TYR B 237 ? 0.81431 0.69481 0.65321 -0.31268 0.05436  -0.01618 237 TYR B CE1 
8185 C CE2 . TYR B 237 ? 0.77339 0.71816 0.65164 -0.30492 0.04528  -0.02073 237 TYR B CE2 
8186 C CZ  . TYR B 237 ? 0.81857 0.72716 0.67061 -0.31521 0.04957  -0.02112 237 TYR B CZ  
8187 O OH  . TYR B 237 ? 0.85293 0.75393 0.69124 -0.32802 0.04916  -0.02643 237 TYR B OH  
8197 N N   . ASN B 238 ? 0.66015 0.64985 0.57779 -0.27301 0.05969  0.00672  238 ASN B N   
8198 C CA  . ASN B 238 ? 0.64865 0.65574 0.58081 -0.26104 0.06106  0.01100  238 ASN B CA  
8199 C C   . ASN B 238 ? 0.59655 0.57185 0.52316 -0.24686 0.06041  0.01297  238 ASN B C   
8200 O O   . ASN B 238 ? 0.55212 0.54446 0.49539 -0.22939 0.05703  0.01283  238 ASN B O   
8201 C CB  . ASN B 238 ? 0.61587 0.67554 0.57541 -0.25690 0.05807  0.00908  238 ASN B CB  
8202 C CG  . ASN B 238 ? 0.67463 0.76889 0.64100 -0.26568 0.06071  0.01000  238 ASN B CG  
8203 O OD1 . ASN B 238 ? 0.66343 0.74191 0.61366 -0.27755 0.06437  0.01130  238 ASN B OD1 
8204 N ND2 . ASN B 238 ? 0.70396 0.84483 0.69316 -0.25946 0.05891  0.00923  238 ASN B ND2 
8211 N N   . TYR B 239 ? 0.66019 0.58925 0.56309 -0.24712 0.06183  0.01392  239 TYR B N   
8212 C CA  . TYR B 239 ? 0.62912 0.52535 0.52317 -0.23124 0.06145  0.01652  239 TYR B CA  
8213 C C   . TYR B 239 ? 0.63341 0.51352 0.51524 -0.22813 0.06633  0.02298  239 TYR B C   
8214 O O   . TYR B 239 ? 0.61611 0.48933 0.48516 -0.24139 0.07061  0.02504  239 TYR B O   
8215 C CB  . TYR B 239 ? 0.64533 0.50083 0.51992 -0.23145 0.06023  0.01384  239 TYR B CB  
8216 C CG  . TYR B 239 ? 0.66573 0.53128 0.55328 -0.22384 0.05454  0.00868  239 TYR B CG  
8217 C CD1 . TYR B 239 ? 0.62937 0.53271 0.53518 -0.23189 0.05149  0.00440  239 TYR B CD1 
8218 C CD2 . TYR B 239 ? 0.67218 0.51327 0.55511 -0.20549 0.05164  0.00823  239 TYR B CD2 
8219 C CE1 . TYR B 239 ? 0.66884 0.58164 0.58600 -0.22252 0.04589  0.00004  239 TYR B CE1 
8220 C CE2 . TYR B 239 ? 0.62217 0.47351 0.51694 -0.19700 0.04636  0.00364  239 TYR B CE2 
8221 C CZ  . TYR B 239 ? 0.65240 0.53806 0.56358 -0.20557 0.04354  -0.00033 239 TYR B CZ  
8222 O OH  . TYR B 239 ? 0.63721 0.53133 0.55873 -0.19635 0.03838  -0.00438 239 TYR B OH  
8232 N N   . GLU B 240 ? 0.60106 0.47827 0.48804 -0.20652 0.06423  0.02537  240 GLU B N   
8233 C CA  . GLU B 240 ? 0.61280 0.47329 0.48690 -0.20176 0.06828  0.03157  240 GLU B CA  
8234 C C   . GLU B 240 ? 0.72224 0.53315 0.56565 -0.20881 0.07205  0.03451  240 GLU B C   
8235 O O   . GLU B 240 ? 0.62938 0.41506 0.46305 -0.20785 0.07010  0.03154  240 GLU B O   
8236 C CB  . GLU B 240 ? 0.57562 0.43978 0.45924 -0.17723 0.06461  0.03277  240 GLU B CB  
8237 C CG  . GLU B 240 ? 0.59648 0.50449 0.50536 -0.17053 0.06266  0.03113  240 GLU B CG  
8238 C CD  . GLU B 240 ? 0.65281 0.57964 0.56219 -0.17958 0.06795  0.03481  240 GLU B CD  
8239 O OE1 . GLU B 240 ? 0.69379 0.60549 0.59166 -0.17385 0.07062  0.03957  240 GLU B OE1 
8240 O OE2 . GLU B 240 ? 0.64775 0.60538 0.56857 -0.19215 0.06951  0.03307  240 GLU B OE2 
8247 N N   . PRO B 241 ? 0.75123 0.54599 0.57757 -0.21550 0.07778  0.04044  241 PRO B N   
8248 C CA  . PRO B 241 ? 0.76299 0.51171 0.56094 -0.21515 0.07995  0.04284  241 PRO B CA  
8249 C C   . PRO B 241 ? 0.74284 0.46154 0.53128 -0.19557 0.07787  0.04503  241 PRO B C   
8250 O O   . PRO B 241 ? 0.74389 0.48206 0.54853 -0.17718 0.07396  0.04533  241 PRO B O   
8251 C CB  . PRO B 241 ? 0.82571 0.57223 0.61279 -0.22061 0.08520  0.04890  241 PRO B CB  
8252 C CG  . PRO B 241 ? 0.80620 0.60157 0.61645 -0.23054 0.08624  0.04789  241 PRO B CG  
8253 C CD  . PRO B 241 ? 0.68556 0.50626 0.51930 -0.21809 0.08121  0.04443  241 PRO B CD  
8261 N N   . LEU B 242 ? 0.80934 0.49299 0.57895 -0.19183 0.07725  0.04351  242 LEU B N   
8262 C CA  . LEU B 242 ? 0.78823 0.44205 0.54598 -0.17188 0.07557  0.04584  242 LEU B CA  
8263 C C   . LEU B 242 ? 0.84049 0.46547 0.57447 -0.16688 0.07948  0.05262  242 LEU B C   
8264 O O   . LEU B 242 ? 0.82729 0.43508 0.54493 -0.17756 0.08255  0.05242  242 LEU B O   
8265 C CB  . LEU B 242 ? 0.81775 0.45285 0.56948 -0.16872 0.07272  0.03988  242 LEU B CB  
8266 C CG  . LEU B 242 ? 0.82028 0.43519 0.56714 -0.14698 0.06976  0.04032  242 LEU B CG  
8267 C CD1 . LEU B 242 ? 0.72114 0.37170 0.49634 -0.13641 0.06444  0.03764  242 LEU B CD1 
8268 C CD2 . LEU B 242 ? 0.84977 0.44272 0.58521 -0.14624 0.06856  0.03466  242 LEU B CD2 
8280 N N   . THR B 243 ? 0.87366 0.49440 0.60530 -0.15114 0.07941  0.05861  243 THR B N   
8281 C CA  . THR B 243 ? 0.91490 0.51133 0.62497 -0.14416 0.08263  0.06575  243 THR B CA  
8282 C C   . THR B 243 ? 0.89308 0.45732 0.58696 -0.12429 0.08058  0.06679  243 THR B C   
8283 O O   . THR B 243 ? 0.86502 0.42953 0.56663 -0.11471 0.07669  0.06263  243 THR B O   
8284 C CB  . THR B 243 ? 0.89128 0.50747 0.60883 -0.13785 0.08347  0.07169  243 THR B CB  
8285 O OG1 . THR B 243 ? 0.94918 0.58200 0.68325 -0.11535 0.07689  0.06943  243 THR B OG1 
8286 C CG2 . THR B 243 ? 0.88934 0.54870 0.63056 -0.15259 0.08395  0.06854  243 THR B CG2 
8294 N N   . GLN B 244 ? 0.94103 0.47904 0.61251 -0.11735 0.08330  0.07248  244 GLN B N   
8295 C CA  . GLN B 244 ? 0.89349 0.40479 0.55004 -0.09613 0.08147  0.07411  244 GLN B CA  
8296 C C   . GLN B 244 ? 0.92628 0.45182 0.59454 -0.07618 0.07729  0.07666  244 GLN B C   
8297 O O   . GLN B 244 ? 0.98111 0.49715 0.64744 -0.05903 0.07406  0.07510  244 GLN B O   
8298 C CB  . GLN B 244 ? 1.06415 0.54619 0.69414 -0.09218 0.08538  0.08019  244 GLN B CB  
8299 C CG  . GLN B 244 ? 1.03178 0.48740 0.64536 -0.06956 0.08386  0.08178  244 GLN B CG  
8300 C CD  . GLN B 244 ? 1.08601 0.52458 0.69375 -0.07096 0.08344  0.07472  244 GLN B CD  
8301 O OE1 . GLN B 244 ? 1.07389 0.50736 0.67838 -0.09026 0.08589  0.07017  244 GLN B OE1 
8302 N NE2 . GLN B 244 ? 1.09187 0.52341 0.69817 -0.05045 0.08033  0.07363  244 GLN B NE2 
8311 N N   . ASP B 245 ? 0.87946 0.42891 0.55950 -0.07798 0.07746  0.08035  245 ASP B N   
8312 C CA  . ASP B 245 ? 0.92879 0.50986 0.63099 -0.05855 0.07089  0.07844  245 ASP B CA  
8313 C C   . ASP B 245 ? 0.92113 0.52048 0.64495 -0.05526 0.06573  0.06987  245 ASP B C   
8314 O O   . ASP B 245 ? 0.87902 0.48128 0.60771 -0.03690 0.06130  0.06846  245 ASP B O   
8315 C CB  . ASP B 245 ? 0.87980 0.49797 0.60040 -0.06254 0.07031  0.07916  245 ASP B CB  
8316 C CG  . ASP B 245 ? 1.04860 0.69711 0.78913 -0.04391 0.06399  0.07724  245 ASP B CG  
8317 O OD1 . ASP B 245 ? 1.06554 0.70137 0.79526 -0.02564 0.06185  0.08078  245 ASP B OD1 
8318 O OD2 . ASP B 245 ? 1.10270 0.78808 0.86899 -0.04760 0.06129  0.07218  245 ASP B OD2 
8323 N N   . HIS B 246 ? 0.85547 0.46812 0.59178 -0.07302 0.06634  0.06434  246 HIS B N   
8324 C CA  . HIS B 246 ? 0.81508 0.44491 0.57108 -0.07139 0.06168  0.05636  246 HIS B CA  
8325 C C   . HIS B 246 ? 0.85953 0.45511 0.59765 -0.06233 0.06162  0.05547  246 HIS B C   
8326 O O   . HIS B 246 ? 0.84290 0.44971 0.59304 -0.04805 0.05693  0.05189  246 HIS B O   
8327 C CB  . HIS B 246 ? 0.81694 0.46451 0.58542 -0.09303 0.06295  0.05158  246 HIS B CB  
8328 C CG  . HIS B 246 ? 0.78711 0.47231 0.57564 -0.09942 0.06273  0.05162  246 HIS B CG  
8329 N ND1 . HIS B 246 ? 0.77889 0.47705 0.57167 -0.11998 0.06600  0.05044  246 HIS B ND1 
8330 C CD2 . HIS B 246 ? 0.71592 0.42930 0.52111 -0.08801 0.05979  0.05222  246 HIS B CD2 
8331 C CE1 . HIS B 246 ? 0.75751 0.49011 0.56866 -0.11964 0.06530  0.05062  246 HIS B CE1 
8332 N NE2 . HIS B 246 ? 0.81759 0.55851 0.63595 -0.10043 0.06157  0.05154  246 HIS B NE2 
8340 N N   . VAL B 247 ? 0.89052 0.44465 0.59940 -0.07043 0.06713  0.05873  247 VAL B N   
8341 C CA  . VAL B 247 ? 0.86634 0.39460 0.56071 -0.05976 0.06656  0.05625  247 VAL B CA  
8342 C C   . VAL B 247 ? 0.96744 0.49074 0.65776 -0.03385 0.06389  0.06014  247 VAL B C   
8343 O O   . VAL B 247 ? 0.91433 0.43694 0.60840 -0.02088 0.06084  0.05644  247 VAL B O   
8344 C CB  . VAL B 247 ? 0.92986 0.43040 0.60067 -0.06946 0.07120  0.05701  247 VAL B CB  
8345 C CG1 . VAL B 247 ? 0.94101 0.41334 0.59354 -0.05513 0.07131  0.05545  247 VAL B CG1 
8346 C CG2 . VAL B 247 ? 0.88090 0.39005 0.55752 -0.09425 0.07284  0.05159  247 VAL B CG2 
8356 N N   . ASP B 248 ? 0.95747 0.48003 0.64053 -0.02586 0.06487  0.06761  248 ASP B N   
8357 C CA  . ASP B 248 ? 0.95961 0.48238 0.63938 -0.00104 0.06190  0.07174  248 ASP B CA  
8358 C C   . ASP B 248 ? 0.91139 0.47489 0.62185 0.00878  0.05515  0.06596  248 ASP B C   
8359 O O   . ASP B 248 ? 0.93387 0.49751 0.64502 0.02658  0.05211  0.06480  248 ASP B O   
8360 C CB  . ASP B 248 ? 0.97775 0.50049 0.64798 0.00322  0.06354  0.08015  248 ASP B CB  
8361 C CG  . ASP B 248 ? 1.03793 0.53294 0.68411 -0.00319 0.06853  0.08359  248 ASP B CG  
8362 O OD1 . ASP B 248 ? 1.09534 0.56734 0.72826 -0.00388 0.07025  0.08037  248 ASP B OD1 
8363 O OD2 . ASP B 248 ? 1.28852 0.78430 0.92798 -0.00743 0.07097  0.08961  248 ASP B OD2 
8368 N N   . ILE B 249 ? 0.87914 0.47901 0.61533 -0.00245 0.05289  0.06213  249 ILE B N   
8369 C CA  . ILE B 249 ? 0.87197 0.51043 0.63670 0.00563  0.04678  0.05667  249 ILE B CA  
8370 C C   . ILE B 249 ? 0.84308 0.47983 0.61439 0.00726  0.04475  0.05021  249 ILE B C   
8371 O O   . ILE B 249 ? 0.84525 0.50148 0.63080 0.02009  0.04027  0.04711  249 ILE B O   
8372 C CB  . ILE B 249 ? 0.82460 0.49737 0.61222 -0.00736 0.04572  0.05395  249 ILE B CB  
8373 C CG1 . ILE B 249 ? 0.92198 0.59960 0.70396 -0.00671 0.04745  0.06003  249 ILE B CG1 
8374 C CG2 . ILE B 249 ? 0.86531 0.57219 0.67887 -0.00014 0.04013  0.04839  249 ILE B CG2 
8375 C CD1 . ILE B 249 ? 1.00487 0.70914 0.80336 -0.02127 0.04833  0.05812  249 ILE B CD1 
8387 N N   . LEU B 250 ? 0.85816 0.47294 0.61919 -0.00648 0.04805  0.04784  250 LEU B N   
8388 C CA  . LEU B 250 ? 0.85712 0.46773 0.62173 -0.00532 0.04650  0.04167  250 LEU B CA  
8389 C C   . LEU B 250 ? 0.90545 0.48478 0.64834 0.01136  0.04768  0.04356  250 LEU B C   
8390 O O   . LEU B 250 ? 0.94941 0.52304 0.69280 0.01433  0.04680  0.03857  250 LEU B O   
8391 C CB  . LEU B 250 ? 0.77929 0.37905 0.54022 -0.02709 0.04943  0.03783  250 LEU B CB  
8392 C CG  . LEU B 250 ? 0.75622 0.39159 0.54164 -0.04223 0.04769  0.03457  250 LEU B CG  
8393 C CD1 . LEU B 250 ? 0.68055 0.30335 0.45665 -0.06502 0.05184  0.03347  250 LEU B CD1 
8394 C CD2 . LEU B 250 ? 0.66085 0.32514 0.47063 -0.03750 0.04249  0.02809  250 LEU B CD2 
8406 N N   . GLY B 251 ? 0.93956 0.49876 0.66274 0.02292  0.04980  0.05073  251 GLY B N   
8407 C CA  . GLY B 251 ? 1.02284 0.55528 0.72509 0.03947  0.05116  0.05265  251 GLY B CA  
8408 C C   . GLY B 251 ? 0.99211 0.53744 0.70474 0.05615  0.04738  0.04852  251 GLY B C   
8409 O O   . GLY B 251 ? 1.01122 0.54354 0.71553 0.05994  0.04838  0.04467  251 GLY B O   
8413 N N   . PRO B 252 ? 0.90727 0.48975 0.64307 0.06508  0.04234  0.04778  252 PRO B N   
8414 C CA  . PRO B 252 ? 0.93722 0.53863 0.68620 0.07897  0.03858  0.04324  252 PRO B CA  
8415 C C   . PRO B 252 ? 0.98839 0.58743 0.74382 0.06895  0.03878  0.03576  252 PRO B C   
8416 O O   . PRO B 252 ? 1.05126 0.63343 0.79577 0.07907  0.03987  0.03365  252 PRO B O   
8417 C CB  . PRO B 252 ? 0.88695 0.53392 0.66364 0.08095  0.03331  0.04223  252 PRO B CB  
8418 C CG  . PRO B 252 ? 0.88972 0.53521 0.65998 0.07840  0.03440  0.04833  252 PRO B CG  
8419 C CD  . PRO B 252 ? 0.89087 0.50291 0.64215 0.06277  0.03982  0.05047  252 PRO B CD  
8427 N N   . LEU B 253 ? 0.99013 0.60612 0.76237 0.04980  0.03786  0.03178  253 LEU B N   
8428 C CA  . LEU B 253 ? 0.92052 0.53750 0.69982 0.03943  0.03759  0.02480  253 LEU B CA  
8429 C C   . LEU B 253 ? 0.97767 0.55096 0.72938 0.03448  0.04254  0.02413  253 LEU B C   
8430 O O   . LEU B 253 ? 1.01238 0.57840 0.76179 0.03591  0.04261  0.01895  253 LEU B O   
8431 C CB  . LEU B 253 ? 0.83453 0.47631 0.63404 0.02014  0.03607  0.02194  253 LEU B CB  
8432 C CG  . LEU B 253 ? 0.75158 0.43540 0.57866 0.02289  0.03141  0.02107  253 LEU B CG  
8433 C CD1 . LEU B 253 ? 0.64966 0.35412 0.49304 0.00516  0.03080  0.01912  253 LEU B CD1 
8434 C CD2 . LEU B 253 ? 0.80440 0.50799 0.64611 0.03335  0.02775  0.01660  253 LEU B CD2 
8446 N N   . SER B 254 ? 0.94990 0.49855 0.68218 0.02720  0.04653  0.02871  254 SER B N   
8447 C CA  . SER B 254 ? 1.02664 0.54801 0.73808 0.02131  0.05027  0.02705  254 SER B CA  
8448 C C   . SER B 254 ? 1.07221 0.58265 0.77200 0.04168  0.05051  0.02691  254 SER B C   
8449 O O   . SER B 254 ? 1.10876 0.60500 0.79897 0.04005  0.05208  0.02238  254 SER B O   
8450 C CB  . SER B 254 ? 1.02375 0.52618 0.71799 0.01178  0.05424  0.03230  254 SER B CB  
8451 O OG  . SER B 254 ? 1.11697 0.59037 0.78841 0.00732  0.05818  0.03086  254 SER B OG  
8457 N N   . ALA B 255 ? 1.05547 0.57417 0.75594 0.06115  0.04895  0.03182  255 ALA B N   
8458 C CA  . ALA B 255 ? 1.11660 0.62969 0.80739 0.08153  0.04910  0.03195  255 ALA B CA  
8459 C C   . ALA B 255 ? 1.10941 0.64248 0.81673 0.08810  0.04603  0.02600  255 ALA B C   
8460 O O   . ALA B 255 ? 1.14474 0.66707 0.84299 0.09370  0.04747  0.02251  255 ALA B O   
8461 C CB  . ALA B 255 ? 1.08306 0.60398 0.77095 0.10017  0.04792  0.03886  255 ALA B CB  
8467 N N   . GLN B 256 ? 1.08624 0.64713 0.81684 0.08628  0.04218  0.02451  256 GLN B N   
8468 C CA  . GLN B 256 ? 1.11394 0.69664 0.86111 0.09395  0.03918  0.01931  256 GLN B CA  
8469 C C   . GLN B 256 ? 1.10451 0.67838 0.85106 0.08135  0.04033  0.01233  256 GLN B C   
8470 O O   . GLN B 256 ? 1.19057 0.77459 0.94342 0.08951  0.03917  0.00801  256 GLN B O   
8471 C CB  . GLN B 256 ? 1.10660 0.72483 0.87986 0.09225  0.03474  0.01913  256 GLN B CB  
8472 C CG  . GLN B 256 ? 1.14213 0.79273 0.93709 0.09776  0.03108  0.01377  256 GLN B CG  
8473 C CD  . GLN B 256 ? 1.22881 0.92135 1.05182 0.09247  0.02641  0.01332  256 GLN B CD  
8474 O OE1 . GLN B 256 ? 1.20597 0.90535 1.03152 0.08993  0.02564  0.01753  256 GLN B OE1 
8475 N NE2 . GLN B 256 ? 1.22601 0.94517 1.06875 0.09041  0.02360  0.00816  256 GLN B NE2 
8484 N N   . THR B 257 ? 1.11502 0.67224 0.85417 0.06148  0.04256  0.01107  257 THR B N   
8485 C CA  . THR B 257 ? 1.11296 0.66458 0.85203 0.04797  0.04318  0.00435  257 THR B CA  
8486 C C   . THR B 257 ? 1.12616 0.64671 0.84060 0.04358  0.04737  0.00339  257 THR B C   
8487 O O   . THR B 257 ? 1.14729 0.66212 0.85899 0.03576  0.04794  -0.00239 257 THR B O   
8488 C CB  . THR B 257 ? 0.97247 0.53467 0.72449 0.02646  0.04200  0.00232  257 THR B CB  
8489 O OG1 . THR B 257 ? 1.01119 0.56043 0.75293 0.01573  0.04448  0.00693  257 THR B OG1 
8490 C CG2 . THR B 257 ? 0.93944 0.53825 0.71865 0.02973  0.03749  0.00219  257 THR B CG2 
8498 N N   . GLY B 258 ? 1.11882 0.61859 0.81427 0.04823  0.05041  0.00876  258 GLY B N   
8499 C CA  . GLY B 258 ? 1.10396 0.57177 0.77418 0.04257  0.05484  0.00790  258 GLY B CA  
8500 C C   . GLY B 258 ? 1.22875 0.68666 0.89437 0.01761  0.05665  0.00606  258 GLY B C   
8501 O O   . GLY B 258 ? 1.11063 0.54186 0.75488 0.01005  0.06044  0.00452  258 GLY B O   
8505 N N   . ILE B 259 ? 1.08019 0.55944 0.76464 0.00445  0.05423  0.00610  259 ILE B N   
8506 C CA  . ILE B 259 ? 1.01903 0.49444 0.70104 -0.01928 0.05584  0.00501  259 ILE B CA  
8507 C C   . ILE B 259 ? 1.13271 0.60492 0.81046 -0.02046 0.05744  0.01208  259 ILE B C   
8508 O O   . ILE B 259 ? 1.04263 0.53635 0.73747 -0.01760 0.05489  0.01508  259 ILE B O   
8509 C CB  . ILE B 259 ? 1.00125 0.50442 0.70671 -0.03391 0.05233  0.00018  259 ILE B CB  
8510 C CG1 . ILE B 259 ? 1.04371 0.54989 0.75241 -0.03326 0.05078  -0.00686 259 ILE B CG1 
8511 C CG2 . ILE B 259 ? 1.02287 0.52667 0.72665 -0.05836 0.05398  -0.00054 259 ILE B CG2 
8512 C CD1 . ILE B 259 ? 1.00980 0.53039 0.73101 -0.01378 0.04781  -0.00777 259 ILE B CD1 
8524 N N   . ALA B 260 ? 1.06924 0.51374 0.72311 -0.02443 0.06186  0.01480  260 ALA B N   
8525 C CA  . ALA B 260 ? 1.06160 0.50211 0.70997 -0.02745 0.06378  0.02142  260 ALA B CA  
8526 C C   . ALA B 260 ? 0.98339 0.44592 0.64878 -0.04828 0.06273  0.02060  260 ALA B C   
8527 O O   . ALA B 260 ? 1.01566 0.48626 0.68755 -0.06482 0.06219  0.01494  260 ALA B O   
8528 C CB  . ALA B 260 ? 1.10223 0.50744 0.72047 -0.03077 0.06915  0.02370  260 ALA B CB  
8534 N N   . VAL B 261 ? 0.95554 0.42868 0.62739 -0.04736 0.06260  0.02642  261 VAL B N   
8535 C CA  . VAL B 261 ? 0.99388 0.49082 0.68282 -0.06553 0.06185  0.02622  261 VAL B CA  
8536 C C   . VAL B 261 ? 0.87365 0.36401 0.55446 -0.08861 0.06467  0.02263  261 VAL B C   
8537 O O   . VAL B 261 ? 0.86433 0.37683 0.56104 -0.10387 0.06292  0.01813  261 VAL B O   
8538 C CB  . VAL B 261 ? 0.89623 0.39900 0.58653 -0.06211 0.06277  0.03381  261 VAL B CB  
8539 C CG1 . VAL B 261 ? 0.93236 0.45994 0.63894 -0.08160 0.06283  0.03360  261 VAL B CG1 
8540 C CG2 . VAL B 261 ? 0.95270 0.46648 0.65285 -0.04030 0.05940  0.03687  261 VAL B CG2 
8550 N N   . LEU B 262 ? 0.96352 0.42427 0.61896 -0.09165 0.06909  0.02454  262 LEU B N   
8551 C CA  . LEU B 262 ? 0.92557 0.38025 0.57212 -0.11435 0.07188  0.02093  262 LEU B CA  
8552 C C   . LEU B 262 ? 0.90484 0.35707 0.55070 -0.11946 0.07060  0.01315  262 LEU B C   
8553 O O   . LEU B 262 ? 0.91200 0.37427 0.56119 -0.13938 0.07081  0.00866  262 LEU B O   
8554 C CB  . LEU B 262 ? 1.01456 0.43591 0.63222 -0.11682 0.07731  0.02492  262 LEU B CB  
8555 C CG  . LEU B 262 ? 1.02500 0.45246 0.64350 -0.12062 0.07922  0.03182  262 LEU B CG  
8556 C CD1 . LEU B 262 ? 1.07480 0.46556 0.66262 -0.11840 0.08445  0.03634  262 LEU B CD1 
8557 C CD2 . LEU B 262 ? 1.01279 0.46715 0.64624 -0.14466 0.07934  0.02970  262 LEU B CD2 
8569 N N   . ASP B 263 ? 1.00130 0.44312 0.64372 -0.10168 0.06914  0.01146  263 ASP B N   
8570 C CA  . ASP B 263 ? 0.93541 0.38001 0.58104 -0.10500 0.06730  0.00413  263 ASP B CA  
8571 C C   . ASP B 263 ? 0.89882 0.38170 0.57424 -0.11264 0.06250  0.00065  263 ASP B C   
8572 O O   . ASP B 263 ? 0.87410 0.36928 0.55526 -0.12960 0.06160  -0.00461 263 ASP B O   
8573 C CB  . ASP B 263 ? 1.01934 0.44712 0.65593 -0.08211 0.06698  0.00396  263 ASP B CB  
8574 C CG  . ASP B 263 ? 1.02932 0.45211 0.66255 -0.08385 0.06629  -0.00315 263 ASP B CG  
8575 O OD1 . ASP B 263 ? 0.97266 0.40789 0.61302 -0.10197 0.06521  -0.00839 263 ASP B OD1 
8576 O OD2 . ASP B 263 ? 1.13889 0.54702 0.76272 -0.06579 0.06671  -0.00338 263 ASP B OD2 
8581 N N   . MET B 264 ? 0.91508 0.41792 0.60907 -0.10097 0.05953  0.00386  264 MET B N   
8582 C CA  . MET B 264 ? 0.91370 0.45176 0.63483 -0.10800 0.05540  0.00112  264 MET B CA  
8583 C C   . MET B 264 ? 0.83920 0.39514 0.56754 -0.13000 0.05630  0.00118  264 MET B C   
8584 O O   . MET B 264 ? 0.75936 0.33990 0.50320 -0.14247 0.05377  -0.00341 264 MET B O   
8585 C CB  . MET B 264 ? 0.81341 0.36631 0.55000 -0.09192 0.05279  0.00502  264 MET B CB  
8586 C CG  . MET B 264 ? 0.77850 0.36484 0.54162 -0.09666 0.04859  0.00171  264 MET B CG  
8587 S SD  . MET B 264 ? 0.74295 0.33200 0.51085 -0.09182 0.04540  -0.00603 264 MET B SD  
8588 C CE  . MET B 264 ? 0.73629 0.32174 0.50700 -0.06469 0.04373  -0.00339 264 MET B CE  
8598 N N   . CYS B 265 ? 0.91337 0.45843 0.63014 -0.13487 0.05998  0.00640  265 CYS B N   
8599 C CA  . CYS B 265 ? 0.78368 0.34634 0.50598 -0.15587 0.06141  0.00653  265 CYS B CA  
8600 C C   . CYS B 265 ? 0.84514 0.40856 0.56212 -0.17330 0.06172  0.00016  265 CYS B C   
8601 O O   . CYS B 265 ? 0.79703 0.38955 0.52890 -0.18923 0.06034  -0.00241 265 CYS B O   
8602 C CB  . CYS B 265 ? 0.90610 0.45089 0.61179 -0.15780 0.06600  0.01292  265 CYS B CB  
8603 S SG  . CYS B 265 ? 0.85734 0.41029 0.57247 -0.14134 0.06550  0.02097  265 CYS B SG  
8609 N N   . ALA B 266 ? 0.85757 0.38958 0.55226 -0.17048 0.06374  -0.00239 266 ALA B N   
8610 C CA  . ALA B 266 ? 0.82493 0.35650 0.51315 -0.18669 0.06400  -0.00876 266 ALA B CA  
8611 C C   . ALA B 266 ? 0.81103 0.37051 0.52054 -0.18735 0.05889  -0.01434 266 ALA B C   
8612 O O   . ALA B 266 ? 0.78881 0.36616 0.50368 -0.20413 0.05775  -0.01897 266 ALA B O   
8613 C CB  . ALA B 266 ? 0.85506 0.34471 0.51304 -0.18267 0.06775  -0.01019 266 ALA B CB  
8619 N N   . SER B 267 ? 0.75400 0.31838 0.47529 -0.16938 0.05576  -0.01399 267 SER B N   
8620 C CA  . SER B 267 ? 0.76582 0.35872 0.50854 -0.17011 0.05084  -0.01882 267 SER B CA  
8621 C C   . SER B 267 ? 0.78473 0.41661 0.55113 -0.18153 0.04851  -0.01799 267 SER B C   
8622 O O   . SER B 267 ? 0.69468 0.35108 0.47201 -0.19458 0.04609  -0.02240 267 SER B O   
8623 C CB  . SER B 267 ? 0.79544 0.38553 0.54529 -0.14857 0.04831  -0.01844 267 SER B CB  
8624 O OG  . SER B 267 ? 0.86438 0.42729 0.59653 -0.13929 0.04953  -0.02131 267 SER B OG  
8630 N N   . LEU B 268 ? 0.74396 0.38241 0.51730 -0.17698 0.04952  -0.01211 268 LEU B N   
8631 C CA  . LEU B 268 ? 0.77170 0.44757 0.56687 -0.18706 0.04798  -0.01093 268 LEU B CA  
8632 C C   . LEU B 268 ? 0.78288 0.47010 0.57435 -0.20793 0.04992  -0.01234 268 LEU B C   
8633 O O   . LEU B 268 ? 0.71139 0.43392 0.52060 -0.21889 0.04738  -0.01495 268 LEU B O   
8634 C CB  . LEU B 268 ? 0.71157 0.38923 0.51191 -0.17810 0.04943  -0.00420 268 LEU B CB  
8635 C CG  . LEU B 268 ? 0.71003 0.42590 0.53167 -0.18767 0.04886  -0.00229 268 LEU B CG  
8636 C CD1 . LEU B 268 ? 0.70690 0.45612 0.55183 -0.18871 0.04409  -0.00658 268 LEU B CD1 
8637 C CD2 . LEU B 268 ? 0.64261 0.35666 0.46679 -0.17762 0.05069  0.00434  268 LEU B CD2 
8649 N N   . LYS B 269 ? 0.75832 0.41654 0.52610 -0.21350 0.05442  -0.01079 269 LYS B N   
8650 C CA  . LYS B 269 ? 0.78645 0.45397 0.54876 -0.23412 0.05651  -0.01258 269 LYS B CA  
8651 C C   . LYS B 269 ? 0.85243 0.53845 0.62134 -0.24449 0.05328  -0.01949 269 LYS B C   
8652 O O   . LYS B 269 ? 0.83413 0.55325 0.61583 -0.25872 0.05201  -0.02129 269 LYS B O   
8653 C CB  . LYS B 269 ? 0.84144 0.46905 0.57344 -0.23834 0.06186  -0.01099 269 LYS B CB  
8654 C CG  . LYS B 269 ? 0.90618 0.54448 0.63288 -0.25981 0.06455  -0.01177 269 LYS B CG  
8655 C CD  . LYS B 269 ? 0.93468 0.53217 0.62905 -0.26685 0.07012  -0.01105 269 LYS B CD  
8656 C CE  . LYS B 269 ? 0.98570 0.55481 0.66613 -0.25472 0.07382  -0.00394 269 LYS B CE  
8657 N NZ  . LYS B 269 ? 1.01967 0.55035 0.66778 -0.26348 0.07958  -0.00311 269 LYS B NZ  
8671 N N   . GLU B 270 ? 0.83151 0.49752 0.59149 -0.23679 0.05194  -0.02336 270 GLU B N   
8672 C CA  . GLU B 270 ? 0.85459 0.53670 0.61946 -0.24586 0.04882  -0.02990 270 GLU B CA  
8673 C C   . GLU B 270 ? 0.82596 0.55117 0.62046 -0.24378 0.04343  -0.03105 270 GLU B C   
8674 O O   . GLU B 270 ? 0.82789 0.58232 0.63237 -0.25624 0.04101  -0.03458 270 GLU B O   
8675 C CB  . GLU B 270 ? 0.82388 0.47412 0.57202 -0.23671 0.04897  -0.03356 270 GLU B CB  
8676 C CG  . GLU B 270 ? 0.99598 0.60324 0.71243 -0.23990 0.05445  -0.03333 270 GLU B CG  
8677 C CD  . GLU B 270 ? 0.99893 0.60746 0.70277 -0.26295 0.05716  -0.03592 270 GLU B CD  
8678 O OE1 . GLU B 270 ? 1.06302 0.69789 0.77599 -0.27625 0.05449  -0.04069 270 GLU B OE1 
8679 O OE2 . GLU B 270 ? 0.99507 0.57806 0.67885 -0.26776 0.06209  -0.03300 270 GLU B OE2 
8686 N N   . LEU B 271 ? 0.67706 0.40763 0.48543 -0.22804 0.04152  -0.02801 271 LEU B N   
8687 C CA  . LEU B 271 ? 0.74942 0.51949 0.58450 -0.22610 0.03660  -0.02924 271 LEU B CA  
8688 C C   . LEU B 271 ? 0.78846 0.59713 0.63942 -0.23874 0.03634  -0.02763 271 LEU B C   
8689 O O   . LEU B 271 ? 0.79277 0.63725 0.66117 -0.24367 0.03249  -0.03028 271 LEU B O   
8690 C CB  . LEU B 271 ? 0.70477 0.47175 0.54991 -0.20805 0.03524  -0.02620 271 LEU B CB  
8691 C CG  . LEU B 271 ? 0.71346 0.45333 0.54857 -0.19431 0.03424  -0.02882 271 LEU B CG  
8692 C CD1 . LEU B 271 ? 0.63734 0.36912 0.47791 -0.17638 0.03397  -0.02512 271 LEU B CD1 
8693 C CD2 . LEU B 271 ? 0.77577 0.53391 0.62002 -0.19716 0.02986  -0.03472 271 LEU B CD2 
8705 N N   . LEU B 272 ? 0.79141 0.59481 0.63661 -0.24314 0.04041  -0.02311 272 LEU B N   
8706 C CA  . LEU B 272 ? 0.79312 0.63431 0.65287 -0.25460 0.04065  -0.02160 272 LEU B CA  
8707 C C   . LEU B 272 ? 0.83411 0.69041 0.68966 -0.27203 0.04029  -0.02595 272 LEU B C   
8708 O O   . LEU B 272 ? 0.85234 0.75056 0.72605 -0.27844 0.03767  -0.02709 272 LEU B O   
8709 C CB  . LEU B 272 ? 0.84278 0.67259 0.69455 -0.25633 0.04557  -0.01599 272 LEU B CB  
8710 C CG  . LEU B 272 ? 0.72607 0.55290 0.58636 -0.24118 0.04593  -0.01100 272 LEU B CG  
8711 C CD1 . LEU B 272 ? 0.73694 0.55247 0.58655 -0.24528 0.05103  -0.00572 272 LEU B CD1 
8712 C CD2 . LEU B 272 ? 0.74377 0.61582 0.63219 -0.23887 0.04233  -0.01130 272 LEU B CD2 
8724 N N   . GLN B 273 ? 0.84051 0.66399 0.67146 -0.27986 0.04320  -0.02817 273 GLN B N   
8725 C CA  . GLN B 273 ? 0.86378 0.70072 0.68871 -0.29824 0.04344  -0.03226 273 GLN B CA  
8726 C C   . GLN B 273 ? 0.90697 0.75977 0.73888 -0.29922 0.03869  -0.03789 273 GLN B C   
8727 O O   . GLN B 273 ? 0.90217 0.78513 0.74030 -0.31201 0.03696  -0.04086 273 GLN B O   
8728 C CB  . GLN B 273 ? 0.89448 0.68977 0.68884 -0.30754 0.04871  -0.03279 273 GLN B CB  
8729 C CG  . GLN B 273 ? 0.90822 0.68204 0.69244 -0.30483 0.05362  -0.02669 273 GLN B CG  
8730 C CD  . GLN B 273 ? 0.93348 0.65996 0.68522 -0.31024 0.05873  -0.02695 273 GLN B CD  
8731 O OE1 . GLN B 273 ? 0.85366 0.57404 0.59282 -0.32322 0.06281  -0.02546 273 GLN B OE1 
8732 N NE2 . GLN B 273 ? 1.01323 0.70605 0.75069 -0.29993 0.05868  -0.02890 273 GLN B NE2 
8741 N N   . ASN B 274 ? 0.85525 0.68850 0.68535 -0.28586 0.03663  -0.03943 274 ASN B N   
8742 C CA  . ASN B 274 ? 0.85121 0.69331 0.68386 -0.28676 0.03262  -0.04493 274 ASN B CA  
8743 C C   . ASN B 274 ? 0.84239 0.71528 0.70006 -0.27509 0.02708  -0.04496 274 ASN B C   
8744 O O   . ASN B 274 ? 0.85984 0.74804 0.72245 -0.27692 0.02326  -0.04920 274 ASN B O   
8745 C CB  . ASN B 274 ? 0.85196 0.64868 0.66126 -0.28160 0.03451  -0.04775 274 ASN B CB  
8746 C CG  . ASN B 274 ? 0.94500 0.71196 0.72731 -0.29501 0.03965  -0.04905 274 ASN B CG  
8747 O OD1 . ASN B 274 ? 0.93879 0.68338 0.70887 -0.29507 0.04408  -0.04512 274 ASN B OD1 
8748 N ND2 . ASN B 274 ? 0.98487 0.75089 0.75665 -0.30681 0.03918  -0.05460 274 ASN B ND2 
8755 N N   . GLY B 275 ? 0.80311 0.68459 0.67548 -0.26335 0.02669  -0.04039 275 GLY B N   
8756 C CA  . GLY B 275 ? 0.77355 0.67828 0.66680 -0.25134 0.02186  -0.04047 275 GLY B CA  
8757 C C   . GLY B 275 ? 0.78043 0.65532 0.66492 -0.23936 0.02073  -0.04287 275 GLY B C   
8758 O O   . GLY B 275 ? 0.81876 0.65540 0.68178 -0.23841 0.02379  -0.04408 275 GLY B O   
8762 N N   . MET B 276 ? 0.72190 0.61614 0.62320 -0.22969 0.01632  -0.04359 276 MET B N   
8763 C CA  . MET B 276 ? 0.73805 0.60835 0.63370 -0.21697 0.01509  -0.04568 276 MET B CA  
8764 C C   . MET B 276 ? 0.86170 0.73248 0.75156 -0.22069 0.01226  -0.05151 276 MET B C   
8765 O O   . MET B 276 ? 0.85492 0.70558 0.73830 -0.21077 0.01152  -0.05389 276 MET B O   
8766 C CB  . MET B 276 ? 0.75893 0.64769 0.67465 -0.20146 0.01226  -0.04271 276 MET B CB  
8767 C CG  . MET B 276 ? 0.78869 0.64933 0.69860 -0.18401 0.01489  -0.03889 276 MET B CG  
8768 S SD  . MET B 276 ? 0.79450 0.68251 0.72907 -0.16281 0.01252  -0.03319 276 MET B SD  
8769 C CE  . MET B 276 ? 0.62173 0.53206 0.56354 -0.17538 0.01483  -0.02958 276 MET B CE  
8779 N N   . ASN B 277 ? 0.86993 0.76426 0.76175 -0.23440 0.01075  -0.05389 277 ASN B N   
8780 C CA  . ASN B 277 ? 0.88488 0.78023 0.77004 -0.23905 0.00822  -0.05941 277 ASN B CA  
8781 C C   . ASN B 277 ? 0.89390 0.79989 0.79064 -0.22710 0.00361  -0.06099 277 ASN B C   
8782 O O   . ASN B 277 ? 0.91716 0.80472 0.80299 -0.22370 0.00300  -0.06507 277 ASN B O   
8783 C CB  . ASN B 277 ? 0.93600 0.78825 0.79424 -0.24213 0.01239  -0.06243 277 ASN B CB  
8784 C CG  . ASN B 277 ? 1.04138 0.88614 0.88607 -0.25753 0.01645  -0.06208 277 ASN B CG  
8785 O OD1 . ASN B 277 ? 1.04156 0.91344 0.89056 -0.27128 0.01503  -0.06378 277 ASN B OD1 
8786 N ND2 . ASN B 277 ? 1.07156 0.88026 0.89921 -0.25518 0.02158  -0.05972 277 ASN B ND2 
8793 N N   . GLY B 278 ? 0.86482 0.80188 0.78341 -0.22095 0.00048  -0.05779 278 GLY B N   
8794 C CA  . GLY B 278 ? 0.92596 0.87934 0.85730 -0.20962 -0.00414 -0.05843 278 GLY B CA  
8795 C C   . GLY B 278 ? 0.90931 0.83772 0.83855 -0.18926 -0.00276 -0.05622 278 GLY B C   
8796 O O   . GLY B 278 ? 0.90079 0.84285 0.84107 -0.17543 -0.00591 -0.05513 278 GLY B O   
8800 N N   . ARG B 279 ? 0.80024 0.69367 0.71547 -0.18678 0.00187  -0.05527 279 ARG B N   
8801 C CA  . ARG B 279 ? 0.73970 0.61408 0.65422 -0.16701 0.00291  -0.05310 279 ARG B CA  
8802 C C   . ARG B 279 ? 0.66278 0.55113 0.59351 -0.15416 0.00318  -0.04652 279 ARG B C   
8803 O O   . ARG B 279 ? 0.69372 0.60257 0.63440 -0.15994 0.00325  -0.04356 279 ARG B O   
8804 C CB  . ARG B 279 ? 0.76772 0.59683 0.65757 -0.16768 0.00749  -0.05553 279 ARG B CB  
8805 C CG  . ARG B 279 ? 0.78678 0.59882 0.65861 -0.17901 0.00750  -0.06281 279 ARG B CG  
8806 C CD  . ARG B 279 ? 0.83076 0.60010 0.67851 -0.17488 0.01244  -0.06387 279 ARG B CD  
8807 N NE  . ARG B 279 ? 0.97159 0.73107 0.80703 -0.18779 0.01567  -0.06305 279 ARG B NE  
8808 C CZ  . ARG B 279 ? 0.96759 0.70100 0.78168 -0.19251 0.01870  -0.06608 279 ARG B CZ  
8809 N NH1 . ARG B 279 ? 0.99284 0.70806 0.79582 -0.18494 0.01896  -0.07018 279 ARG B NH1 
8810 N NH2 . ARG B 279 ? 0.97322 0.69859 0.77615 -0.20532 0.02182  -0.06509 279 ARG B NH2 
8824 N N   . THR B 280 ? 0.60522 0.48319 0.53825 -0.13668 0.00346  -0.04452 280 THR B N   
8825 C CA  . THR B 280 ? 0.56111 0.44815 0.50679 -0.12443 0.00392  -0.03901 280 THR B CA  
8826 C C   . THR B 280 ? 0.57206 0.42700 0.50449 -0.11618 0.00762  -0.03758 280 THR B C   
8827 O O   . THR B 280 ? 0.53838 0.36582 0.45391 -0.11560 0.00942  -0.04071 280 THR B O   
8828 C CB  . THR B 280 ? 0.53582 0.44463 0.49843 -0.11028 0.00058  -0.03729 280 THR B CB  
8829 O OG1 . THR B 280 ? 0.56616 0.46033 0.52191 -0.10248 0.00019  -0.04004 280 THR B OG1 
8830 C CG2 . THR B 280 ? 0.59634 0.53834 0.57263 -0.11535 -0.00304 -0.03728 280 THR B CG2 
8838 N N   . ILE B 281 ? 0.51008 0.36925 0.44960 -0.10932 0.00882  -0.03281 281 ILE B N   
8839 C CA  . ILE B 281 ? 0.51563 0.35069 0.44582 -0.09857 0.01162  -0.03036 281 ILE B CA  
8840 C C   . ILE B 281 ? 0.48067 0.33354 0.42726 -0.08384 0.00977  -0.02719 281 ILE B C   
8841 O O   . ILE B 281 ? 0.45104 0.32665 0.41160 -0.08448 0.00869  -0.02462 281 ILE B O   
8842 C CB  . ILE B 281 ? 0.53769 0.35756 0.45696 -0.10661 0.01538  -0.02755 281 ILE B CB  
8843 C CG1 . ILE B 281 ? 0.58849 0.38762 0.48897 -0.12313 0.01758  -0.03131 281 ILE B CG1 
8844 C CG2 . ILE B 281 ? 0.52181 0.31983 0.43242 -0.09298 0.01776  -0.02422 281 ILE B CG2 
8845 C CD1 . ILE B 281 ? 0.57187 0.35607 0.45985 -0.13533 0.02173  -0.02872 281 ILE B CD1 
8857 N N   . LEU B 282 ? 0.49576 0.33919 0.44040 -0.07071 0.00955  -0.02761 282 LEU B N   
8858 C CA  . LEU B 282 ? 0.44708 0.30674 0.40610 -0.05814 0.00793  -0.02509 282 LEU B CA  
8859 C C   . LEU B 282 ? 0.49035 0.37906 0.46668 -0.06019 0.00496  -0.02480 282 LEU B C   
8860 O O   . LEU B 282 ? 0.46145 0.36507 0.44931 -0.05489 0.00432  -0.02201 282 LEU B O   
8861 C CB  . LEU B 282 ? 0.48302 0.33835 0.44154 -0.05295 0.00978  -0.02090 282 LEU B CB  
8862 C CG  . LEU B 282 ? 0.53127 0.36133 0.47499 -0.04449 0.01217  -0.01996 282 LEU B CG  
8863 C CD1 . LEU B 282 ? 0.50707 0.33580 0.45058 -0.04005 0.01361  -0.01541 282 LEU B CD1 
8864 C CD2 . LEU B 282 ? 0.50974 0.34185 0.45647 -0.03231 0.01081  -0.02168 282 LEU B CD2 
8876 N N   . GLY B 283 ? 0.48625 0.38233 0.46320 -0.06730 0.00319  -0.02773 283 GLY B N   
8877 C CA  . GLY B 283 ? 0.56336 0.48588 0.55514 -0.06684 0.00025  -0.02713 283 GLY B CA  
8878 C C   . GLY B 283 ? 0.54054 0.48188 0.54044 -0.07401 -0.00001 -0.02509 283 GLY B C   
8879 O O   . GLY B 283 ? 0.53859 0.50194 0.55110 -0.07047 -0.00201 -0.02356 283 GLY B O   
8883 N N   . SER B 284 ? 0.49257 0.42547 0.48490 -0.08329 0.00233  -0.02473 284 SER B N   
8884 C CA  . SER B 284 ? 0.49050 0.44241 0.48984 -0.09126 0.00270  -0.02290 284 SER B CA  
8885 C C   . SER B 284 ? 0.50517 0.45619 0.49616 -0.10787 0.00306  -0.02572 284 SER B C   
8886 O O   . SER B 284 ? 0.48252 0.40820 0.45765 -0.11396 0.00484  -0.02818 284 SER B O   
8887 C CB  . SER B 284 ? 0.53542 0.48033 0.53327 -0.08893 0.00574  -0.01949 284 SER B CB  
8888 O OG  . SER B 284 ? 0.54526 0.50729 0.54771 -0.09851 0.00680  -0.01809 284 SER B OG  
8894 N N   . ALA B 285 ? 0.45876 0.43762 0.45967 -0.11510 0.00150  -0.02552 285 ALA B N   
8895 C CA  . ALA B 285 ? 0.46946 0.45273 0.46385 -0.13294 0.00184  -0.02819 285 ALA B CA  
8896 C C   . ALA B 285 ? 0.51460 0.50178 0.50781 -0.14264 0.00519  -0.02590 285 ALA B C   
8897 O O   . ALA B 285 ? 0.55818 0.54999 0.54561 -0.15962 0.00606  -0.02795 285 ALA B O   
8898 C CB  . ALA B 285 ? 0.59697 0.61209 0.60233 -0.13645 -0.00221 -0.02970 285 ALA B CB  
8904 N N   . LEU B 286 ? 0.47707 0.46141 0.47413 -0.13344 0.00734  -0.02192 286 LEU B N   
8905 C CA  . LEU B 286 ? 0.48905 0.47098 0.48122 -0.14305 0.01125  -0.01969 286 LEU B CA  
8906 C C   . LEU B 286 ? 0.51251 0.46213 0.49246 -0.13605 0.01440  -0.01741 286 LEU B C   
8907 O O   . LEU B 286 ? 0.48666 0.42043 0.46436 -0.12307 0.01334  -0.01756 286 LEU B O   
8908 C CB  . LEU B 286 ? 0.55907 0.57508 0.56770 -0.14088 0.01130  -0.01671 286 LEU B CB  
8909 C CG  . LEU B 286 ? 0.59802 0.62770 0.62068 -0.12247 0.00924  -0.01463 286 LEU B CG  
8910 C CD1 . LEU B 286 ? 0.60851 0.61680 0.62674 -0.11125 0.01142  -0.01205 286 LEU B CD1 
8911 C CD2 . LEU B 286 ? 0.57255 0.63937 0.61012 -0.12285 0.00892  -0.01298 286 LEU B CD2 
8923 N N   . LEU B 287 ? 0.49003 0.43013 0.46087 -0.14558 0.01841  -0.01528 287 LEU B N   
8924 C CA  . LEU B 287 ? 0.48355 0.39210 0.44008 -0.14021 0.02164  -0.01262 287 LEU B CA  
8925 C C   . LEU B 287 ? 0.53570 0.45681 0.50403 -0.12587 0.02157  -0.00876 287 LEU B C   
8926 O O   . LEU B 287 ? 0.65327 0.59503 0.62990 -0.12921 0.02299  -0.00647 287 LEU B O   
8927 C CB  . LEU B 287 ? 0.49350 0.38517 0.43343 -0.15725 0.02625  -0.01163 287 LEU B CB  
8928 C CG  . LEU B 287 ? 0.55222 0.42932 0.47822 -0.17343 0.02661  -0.01622 287 LEU B CG  
8929 C CD1 . LEU B 287 ? 0.66337 0.52258 0.57159 -0.19200 0.03168  -0.01519 287 LEU B CD1 
8930 C CD2 . LEU B 287 ? 0.65057 0.49774 0.56410 -0.16507 0.02551  -0.01915 287 LEU B CD2 
8942 N N   . GLU B 288 ? 0.46655 0.37635 0.43535 -0.11033 0.02002  -0.00839 288 GLU B N   
8943 C CA  . GLU B 288 ? 0.46783 0.38966 0.44759 -0.09678 0.01946  -0.00565 288 GLU B CA  
8944 C C   . GLU B 288 ? 0.42038 0.32764 0.39012 -0.09623 0.02310  -0.00167 288 GLU B C   
8945 O O   . GLU B 288 ? 0.43354 0.31224 0.38694 -0.09573 0.02481  -0.00082 288 GLU B O   
8946 C CB  . GLU B 288 ? 0.45562 0.36872 0.43693 -0.08267 0.01678  -0.00697 288 GLU B CB  
8947 C CG  . GLU B 288 ? 0.70101 0.63686 0.69919 -0.07276 0.01369  -0.00769 288 GLU B CG  
8948 C CD  . GLU B 288 ? 0.75171 0.71450 0.76273 -0.07721 0.01191  -0.00890 288 GLU B CD  
8949 O OE1 . GLU B 288 ? 0.75822 0.72347 0.76982 -0.08068 0.00974  -0.01158 288 GLU B OE1 
8950 O OE2 . GLU B 288 ? 0.85246 0.83431 0.87252 -0.07610 0.01269  -0.00710 288 GLU B OE2 
8957 N N   . ASP B 289 ? 0.39501 0.32129 0.37381 -0.09478 0.02424  0.00076  289 ASP B N   
8958 C CA  . ASP B 289 ? 0.39232 0.30587 0.36094 -0.09486 0.02779  0.00476  289 ASP B CA  
8959 C C   . ASP B 289 ? 0.40182 0.32542 0.37867 -0.08126 0.02709  0.00655  289 ASP B C   
8960 O O   . ASP B 289 ? 0.37555 0.29767 0.34770 -0.08162 0.02991  0.00985  289 ASP B O   
8961 C CB  . ASP B 289 ? 0.42250 0.34400 0.38773 -0.11085 0.03160  0.00643  289 ASP B CB  
8962 C CG  . ASP B 289 ? 0.43194 0.38883 0.41440 -0.11104 0.03171  0.00674  289 ASP B CG  
8963 O OD1 . ASP B 289 ? 0.40157 0.37698 0.39858 -0.10075 0.02859  0.00501  289 ASP B OD1 
8964 O OD2 . ASP B 289 ? 0.44383 0.40942 0.42419 -0.12113 0.03538  0.00896  289 ASP B OD2 
8969 N N   . GLU B 290 ? 0.39207 0.32468 0.37969 -0.06983 0.02359  0.00438  290 GLU B N   
8970 C CA  . GLU B 290 ? 0.39688 0.33581 0.38974 -0.05808 0.02303  0.00549  290 GLU B CA  
8971 C C   . GLU B 290 ? 0.39639 0.31897 0.38376 -0.04719 0.02102  0.00518  290 GLU B C   
8972 O O   . GLU B 290 ? 0.37684 0.30772 0.37146 -0.03761 0.01915  0.00427  290 GLU B O   
8973 C CB  . GLU B 290 ? 0.38631 0.35076 0.39534 -0.05380 0.02145  0.00360  290 GLU B CB  
8974 C CG  . GLU B 290 ? 0.39534 0.37943 0.40969 -0.06327 0.02392  0.00448  290 GLU B CG  
8975 C CD  . GLU B 290 ? 0.44209 0.45014 0.46932 -0.05665 0.02387  0.00390  290 GLU B CD  
8976 O OE1 . GLU B 290 ? 0.41692 0.42577 0.44928 -0.04612 0.02162  0.00228  290 GLU B OE1 
8977 O OE2 . GLU B 290 ? 0.44361 0.46917 0.47477 -0.06222 0.02647  0.00506  290 GLU B OE2 
8984 N N   . PHE B 291 ? 0.38138 0.28062 0.35489 -0.04854 0.02170  0.00593  291 PHE B N   
8985 C CA  . PHE B 291 ? 0.41261 0.29617 0.37807 -0.03749 0.02070  0.00683  291 PHE B CA  
8986 C C   . PHE B 291 ? 0.41601 0.27881 0.36418 -0.03851 0.02387  0.01116  291 PHE B C   
8987 O O   . PHE B 291 ? 0.40057 0.24635 0.33653 -0.04760 0.02641  0.01210  291 PHE B O   
8988 C CB  . PHE B 291 ? 0.41250 0.28444 0.37457 -0.03479 0.01893  0.00410  291 PHE B CB  
8989 C CG  . PHE B 291 ? 0.39768 0.28674 0.37428 -0.03270 0.01585  0.00033  291 PHE B CG  
8990 C CD1 . PHE B 291 ? 0.39578 0.29386 0.38024 -0.02225 0.01343  -0.00082 291 PHE B CD1 
8991 C CD2 . PHE B 291 ? 0.41776 0.31411 0.39931 -0.04171 0.01539  -0.00202 291 PHE B CD2 
8992 C CE1 . PHE B 291 ? 0.41067 0.32156 0.40639 -0.02085 0.01100  -0.00397 291 PHE B CE1 
8993 C CE2 . PHE B 291 ? 0.40574 0.31625 0.39892 -0.03917 0.01262  -0.00492 291 PHE B CE2 
8994 C CZ  . PHE B 291 ? 0.42745 0.34413 0.42735 -0.02865 0.01064  -0.00570 291 PHE B CZ  
9004 N N   . THR B 292 ? 0.42901 0.29174 0.37447 -0.02951 0.02379  0.01384  292 THR B N   
9005 C CA  . THR B 292 ? 0.47267 0.31399 0.39989 -0.02838 0.02662  0.01864  292 THR B CA  
9006 C C   . THR B 292 ? 0.43959 0.25881 0.35415 -0.01944 0.02590  0.01908  292 THR B C   
9007 O O   . THR B 292 ? 0.45697 0.28136 0.37866 -0.01275 0.02298  0.01571  292 THR B O   
9008 C CB  . THR B 292 ? 0.47177 0.32282 0.40009 -0.02166 0.02663  0.02150  292 THR B CB  
9009 O OG1 . THR B 292 ? 0.45244 0.31214 0.38751 -0.00909 0.02288  0.01962  292 THR B OG1 
9010 C CG2 . THR B 292 ? 0.41940 0.29392 0.36081 -0.02843 0.02750  0.02047  292 THR B CG2 
9018 N N   . PRO B 293 ? 0.49030 0.28394 0.38484 -0.01868 0.02888  0.02340  293 PRO B N   
9019 C CA  . PRO B 293 ? 0.49433 0.26743 0.37569 -0.00664 0.02837  0.02436  293 PRO B CA  
9020 C C   . PRO B 293 ? 0.51198 0.30234 0.40313 0.00874  0.02443  0.02367  293 PRO B C   
9021 O O   . PRO B 293 ? 0.49687 0.28677 0.38988 0.01703  0.02239  0.02109  293 PRO B O   
9022 C CB  . PRO B 293 ? 0.57596 0.32117 0.43390 -0.00727 0.03254  0.03046  293 PRO B CB  
9023 C CG  . PRO B 293 ? 0.59018 0.33433 0.44687 -0.02570 0.03596  0.03084  293 PRO B CG  
9024 C CD  . PRO B 293 ? 0.53951 0.31993 0.42100 -0.02950 0.03333  0.02754  293 PRO B CD  
9032 N N   . PHE B 294 ? 0.53087 0.33849 0.42882 0.01190  0.02334  0.02545  294 PHE B N   
9033 C CA  . PHE B 294 ? 0.55871 0.38455 0.46610 0.02424  0.01948  0.02404  294 PHE B CA  
9034 C C   . PHE B 294 ? 0.51890 0.36462 0.44499 0.02238  0.01656  0.01811  294 PHE B C   
9035 O O   . PHE B 294 ? 0.52273 0.37775 0.45422 0.03146  0.01377  0.01603  294 PHE B O   
9036 C CB  . PHE B 294 ? 0.56034 0.40064 0.47033 0.02688  0.01884  0.02641  294 PHE B CB  
9037 C CG  . PHE B 294 ? 0.61383 0.47345 0.53243 0.03800  0.01477  0.02452  294 PHE B CG  
9038 C CD1 . PHE B 294 ? 0.69457 0.54828 0.60377 0.05117  0.01341  0.02687  294 PHE B CD1 
9039 C CD2 . PHE B 294 ? 0.69786 0.58163 0.63362 0.03507  0.01242  0.02003  294 PHE B CD2 
9040 C CE1 . PHE B 294 ? 0.63895 0.51411 0.55689 0.06021  0.00953  0.02476  294 PHE B CE1 
9041 C CE2 . PHE B 294 ? 0.70185 0.60331 0.64479 0.04303  0.00887  0.01774  294 PHE B CE2 
9042 C CZ  . PHE B 294 ? 0.66101 0.55988 0.59577 0.05504  0.00728  0.02001  294 PHE B CZ  
9052 N N   . ASP B 295 ? 0.45221 0.30678 0.38855 0.01101  0.01717  0.01553  295 ASP B N   
9053 C CA  . ASP B 295 ? 0.46550 0.33663 0.41769 0.00976  0.01462  0.01049  295 ASP B CA  
9054 C C   . ASP B 295 ? 0.44247 0.30327 0.39127 0.01323  0.01386  0.00838  295 ASP B C   
9055 O O   . ASP B 295 ? 0.41662 0.28966 0.37506 0.01789  0.01134  0.00515  295 ASP B O   
9056 C CB  . ASP B 295 ? 0.43124 0.31151 0.39263 -0.00195 0.01562  0.00869  295 ASP B CB  
9057 C CG  . ASP B 295 ? 0.48831 0.38371 0.45632 -0.00411 0.01621  0.00950  295 ASP B CG  
9058 O OD1 . ASP B 295 ? 0.46176 0.36415 0.43047 0.00312  0.01501  0.01009  295 ASP B OD1 
9059 O OD2 . ASP B 295 ? 0.41171 0.31357 0.38434 -0.01300 0.01788  0.00921  295 ASP B OD2 
9064 N N   . VAL B 296 ? 0.44103 0.27877 0.37548 0.01005  0.01638  0.00987  296 VAL B N   
9065 C CA  . VAL B 296 ? 0.46149 0.28731 0.39074 0.01347  0.01615  0.00747  296 VAL B CA  
9066 C C   . VAL B 296 ? 0.51059 0.33508 0.43502 0.02889  0.01487  0.00851  296 VAL B C   
9067 O O   . VAL B 296 ? 0.50845 0.34060 0.43881 0.03470  0.01309  0.00538  296 VAL B O   
9068 C CB  . VAL B 296 ? 0.50588 0.30452 0.41826 0.00564  0.01958  0.00844  296 VAL B CB  
9069 C CG1 . VAL B 296 ? 0.54390 0.32822 0.44870 0.01065  0.01963  0.00562  296 VAL B CG1 
9070 C CG2 . VAL B 296 ? 0.49203 0.29766 0.41125 -0.01041 0.02042  0.00677  296 VAL B CG2 
9080 N N   . VAL B 297 ? 0.53698 0.35416 0.45092 0.03593  0.01573  0.01310  297 VAL B N   
9081 C CA  . VAL B 297 ? 0.54584 0.36498 0.45509 0.05163  0.01430  0.01464  297 VAL B CA  
9082 C C   . VAL B 297 ? 0.50004 0.34981 0.42762 0.05552  0.01052  0.01149  297 VAL B C   
9083 O O   . VAL B 297 ? 0.54839 0.40589 0.47928 0.06377  0.00901  0.00933  297 VAL B O   
9084 C CB  . VAL B 297 ? 0.57863 0.38616 0.47317 0.05812  0.01570  0.02072  297 VAL B CB  
9085 C CG1 . VAL B 297 ? 0.60458 0.42225 0.49741 0.07519  0.01334  0.02228  297 VAL B CG1 
9086 C CG2 . VAL B 297 ? 0.60345 0.37670 0.47653 0.05564  0.01985  0.02390  297 VAL B CG2 
9096 N N   . ARG B 298 ? 0.47880 0.34605 0.41798 0.04891  0.00930  0.01080  298 ARG B N   
9097 C CA  . ARG B 298 ? 0.48454 0.37812 0.43859 0.05140  0.00608  0.00770  298 ARG B CA  
9098 C C   . ARG B 298 ? 0.51549 0.41743 0.48041 0.04841  0.00501  0.00292  298 ARG B C   
9099 O O   . ARG B 298 ? 0.47539 0.39348 0.44763 0.05369  0.00287  0.00060  298 ARG B O   
9100 C CB  . ARG B 298 ? 0.55606 0.46304 0.51796 0.04476  0.00557  0.00751  298 ARG B CB  
9101 C CG  . ARG B 298 ? 0.64212 0.55526 0.61505 0.03319  0.00613  0.00454  298 ARG B CG  
9102 C CD  . ARG B 298 ? 0.55203 0.47756 0.52984 0.02982  0.00603  0.00463  298 ARG B CD  
9103 N NE  . ARG B 298 ? 0.54611 0.47365 0.52983 0.02037  0.00773  0.00364  298 ARG B NE  
9104 C CZ  . ARG B 298 ? 0.59390 0.53302 0.58910 0.01661  0.00687  -0.00009 298 ARG B CZ  
9105 N NH1 . ARG B 298 ? 0.55857 0.50645 0.56023 0.01952  0.00462  -0.00330 298 ARG B NH1 
9106 N NH2 . ARG B 298 ? 0.58554 0.52798 0.58519 0.01006  0.00854  -0.00041 298 ARG B NH2 
9120 N N   . GLN B 299 ? 0.44654 0.33917 0.41251 0.03939  0.00647  0.00145  299 GLN B N   
9121 C CA  . GLN B 299 ? 0.44666 0.34743 0.42234 0.03631  0.00543  -0.00271 299 GLN B CA  
9122 C C   . GLN B 299 ? 0.46106 0.35287 0.42976 0.04373  0.00584  -0.00359 299 GLN B C   
9123 O O   . GLN B 299 ? 0.45105 0.35638 0.42718 0.04755  0.00438  -0.00627 299 GLN B O   
9124 C CB  . GLN B 299 ? 0.42733 0.32366 0.40640 0.02475  0.00649  -0.00395 299 GLN B CB  
9125 C CG  . GLN B 299 ? 0.36099 0.26716 0.34997 0.02212  0.00517  -0.00777 299 GLN B CG  
9126 C CD  . GLN B 299 ? 0.37371 0.28230 0.36880 0.01181  0.00543  -0.00897 299 GLN B CD  
9127 O OE1 . GLN B 299 ? 0.36044 0.27264 0.36027 0.00939  0.00467  -0.01149 299 GLN B OE1 
9128 N NE2 . GLN B 299 ? 0.36496 0.27350 0.36001 0.00619  0.00651  -0.00702 299 GLN B NE2 
9137 N N   . CYS B 300 ? 0.46741 0.33630 0.42061 0.04649  0.00812  -0.00126 300 CYS B N   
9138 C CA  . CYS B 300 ? 0.49443 0.35148 0.43891 0.05376  0.00913  -0.00249 300 CYS B CA  
9139 C C   . CYS B 300 ? 0.53477 0.39734 0.47486 0.06920  0.00845  -0.00085 300 CYS B C   
9140 O O   . CYS B 300 ? 0.51874 0.37738 0.45419 0.07712  0.00913  -0.00243 300 CYS B O   
9141 C CB  . CYS B 300 ? 0.50882 0.33580 0.43598 0.05012  0.01230  -0.00113 300 CYS B CB  
9142 S SG  . CYS B 300 ? 0.60658 0.43193 0.53998 0.03212  0.01270  -0.00433 300 CYS B SG  
9148 N N   A SER B 301 ? 0.49681 0.36995 0.43818 0.07394  0.00712  0.00213  301 SER B N   
9149 N N   B SER B 301 ? 0.49605 0.36897 0.43721 0.07411  0.00714  0.00217  301 SER B N   
9150 C CA  A SER B 301 ? 0.49178 0.37654 0.43106 0.08863  0.00578  0.00367  301 SER B CA  
9151 C CA  B SER B 301 ? 0.48133 0.36615 0.42065 0.08882  0.00579  0.00356  301 SER B CA  
9152 C C   A SER B 301 ? 0.50084 0.41833 0.45705 0.08803  0.00249  0.00124  301 SER B C   
9153 C C   B SER B 301 ? 0.49435 0.41195 0.45067 0.08809  0.00250  0.00114  301 SER B C   
9154 O O   A SER B 301 ? 0.48648 0.41965 0.44320 0.09906  0.00090  0.00203  301 SER B O   
9155 O O   B SER B 301 ? 0.47970 0.41317 0.43672 0.09909  0.00091  0.00183  301 SER B O   
9156 C CB  A SER B 301 ? 0.55619 0.42720 0.48060 0.09630  0.00672  0.00937  301 SER B CB  
9157 C CB  B SER B 301 ? 0.55977 0.43084 0.48389 0.09730  0.00673  0.00927  301 SER B CB  
9158 O OG  A SER B 301 ? 0.56533 0.40325 0.47157 0.09669  0.01026  0.01150  301 SER B OG  
9159 O OG  B SER B 301 ? 0.52427 0.40572 0.45401 0.09102  0.00540  0.01087  301 SER B OG  
9170 N N   . GLY B 302 ? 0.43364 0.36179 0.40270 0.07559  0.00154  -0.00170 302 GLY B N   
9171 C CA  . GLY B 302 ? 0.46208 0.41753 0.44525 0.07312  -0.00105 -0.00456 302 GLY B CA  
9172 C C   . GLY B 302 ? 0.48592 0.45443 0.46937 0.07620  -0.00293 -0.00265 302 GLY B C   
9173 O O   . GLY B 302 ? 0.42403 0.41506 0.41340 0.08064  -0.00516 -0.00408 302 GLY B O   
9178 N N   . VAL B 303 ? 0.46956 0.42550 0.44612 0.07375  -0.00203 0.00053  303 VAL B N   
9179 C CA  . VAL B 303 ? 0.45036 0.41839 0.42629 0.07619  -0.00378 0.00227  303 VAL B CA  
9180 C C   . VAL B 303 ? 0.44188 0.42977 0.43114 0.06691  -0.00554 -0.00216 303 VAL B C   
9181 O O   . VAL B 303 ? 0.40589 0.38972 0.40152 0.05706  -0.00449 -0.00466 303 VAL B O   
9182 C CB  . VAL B 303 ? 0.51660 0.46540 0.48158 0.07428  -0.00175 0.00668  303 VAL B CB  
9183 C CG1 . VAL B 303 ? 0.48714 0.44923 0.45226 0.07467  -0.00344 0.00791  303 VAL B CG1 
9184 C CG2 . VAL B 303 ? 0.50997 0.43547 0.45847 0.08345  0.00041  0.01132  303 VAL B CG2 
9194 N N   . THR B 304 ? 0.39289 0.40225 0.38558 0.07002  -0.00819 -0.00329 304 THR B N   
9195 C CA  . THR B 304 ? 0.42459 0.45105 0.42757 0.06075  -0.00964 -0.00801 304 THR B CA  
9196 C C   . THR B 304 ? 0.47931 0.51207 0.47928 0.05936  -0.01077 -0.00739 304 THR B C   
9197 O O   . THR B 304 ? 0.41422 0.44336 0.40507 0.06698  -0.01109 -0.00312 304 THR B O   
9198 C CB  . THR B 304 ? 0.43235 0.48238 0.44304 0.06205  -0.01179 -0.01158 304 THR B CB  
9199 O OG1 . THR B 304 ? 0.40695 0.47134 0.41334 0.07313  -0.01396 -0.00931 304 THR B OG1 
9200 C CG2 . THR B 304 ? 0.40885 0.45448 0.42299 0.06263  -0.01043 -0.01275 304 THR B CG2 
9208 N N   . PHE B 305 ? 0.42561 0.46647 0.43192 0.04976  -0.01115 -0.01170 305 PHE B N   
9209 C CA  . PHE B 305 ? 0.54121 0.58745 0.54444 0.04708  -0.01190 -0.01224 305 PHE B CA  
9210 C C   . PHE B 305 ? 0.64905 0.71716 0.65775 0.04203  -0.01439 -0.01756 305 PHE B C   
9211 O O   . PHE B 305 ? 0.66265 0.73404 0.67822 0.03475  -0.01401 -0.02173 305 PHE B O   
9212 C CB  . PHE B 305 ? 0.49887 0.52940 0.50157 0.03990  -0.00905 -0.01237 305 PHE B CB  
9213 C CG  . PHE B 305 ? 0.45245 0.46368 0.45052 0.04245  -0.00657 -0.00780 305 PHE B CG  
9214 C CD1 . PHE B 305 ? 0.48071 0.48335 0.46861 0.04805  -0.00581 -0.00265 305 PHE B CD1 
9215 C CD2 . PHE B 305 ? 0.41756 0.41913 0.42007 0.03920  -0.00503 -0.00849 305 PHE B CD2 
9216 C CE1 . PHE B 305 ? 0.50123 0.48473 0.48306 0.04900  -0.00323 0.00140  305 PHE B CE1 
9217 C CE2 . PHE B 305 ? 0.49508 0.47932 0.49240 0.04030  -0.00286 -0.00482 305 PHE B CE2 
9218 C CZ  . PHE B 305 ? 0.53020 0.50459 0.51683 0.04466  -0.00179 0.00004  305 PHE B CZ  
9228 N N   . GLN B 306 ? 0.90532 0.98858 0.91010 0.04567  -0.01695 -0.01728 306 GLN B N   
9229 C CA  . GLN B 306 ? 0.99876 1.10496 1.00757 0.03977  -0.01960 -0.02269 306 GLN B CA  
9230 C C   . GLN B 306 ? 0.87788 0.98817 0.88094 0.03633  -0.02051 -0.02424 306 GLN B C   
9231 O O   . GLN B 306 ? 0.86818 0.96385 0.86913 0.03025  -0.01808 -0.02561 306 GLN B O   
9232 C CB  . GLN B 306 ? 1.06971 1.19933 1.08070 0.04776  -0.02274 -0.02190 306 GLN B CB  
9233 C CG  . GLN B 306 ? 1.06800 1.22436 1.08458 0.03931  -0.02536 -0.02812 306 GLN B CG  
9234 C CD  . GLN B 306 ? 1.22516 1.40802 1.24637 0.04662  -0.02801 -0.02768 306 GLN B CD  
9235 O OE1 . GLN B 306 ? 1.11514 1.29340 1.13684 0.05695  -0.02716 -0.02375 306 GLN B OE1 
9236 N NE2 . GLN B 306 ? 1.17339 1.38494 1.19754 0.04114  -0.03112 -0.03204 306 GLN B NE2 
9245 N N   . GLY C 2   ? 0.80445 0.72254 0.73550 0.10225  0.02847  -0.05678 2   GLY C N   
9246 C CA  . GLY C 2   ? 0.86247 0.76992 0.79494 0.09868  0.02589  -0.05308 2   GLY C CA  
9247 C C   . GLY C 2   ? 0.84174 0.77106 0.79308 0.08810  0.02229  -0.04958 2   GLY C C   
9248 O O   . GLY C 2   ? 0.78391 0.70423 0.73737 0.08072  0.01986  -0.04703 2   GLY C O   
9251 N N   . VAL C 3   ? 0.57238 0.52978 0.53640 0.08702  0.02233  -0.04963 3   VAL C N   
9252 C CA  . VAL C 3   ? 0.58041 0.55826 0.56061 0.07772  0.01960  -0.04676 3   VAL C CA  
9253 C C   . VAL C 3   ? 0.48542 0.47959 0.47185 0.08623  0.01914  -0.04451 3   VAL C C   
9254 O O   . VAL C 3   ? 0.45036 0.45860 0.43600 0.09795  0.02126  -0.04551 3   VAL C O   
9255 C CB  . VAL C 3   ? 0.54707 0.54521 0.53575 0.07095  0.02028  -0.04787 3   VAL C CB  
9256 C CG1 . VAL C 3   ? 0.43140 0.44858 0.43441 0.06242  0.01810  -0.04507 3   VAL C CG1 
9257 C CG2 . VAL C 3   ? 0.60618 0.58913 0.58853 0.06213  0.02014  -0.04968 3   VAL C CG2 
9267 N N   . THR C 4   ? 0.39810 0.39298 0.39091 0.08074  0.01639  -0.04158 4   THR C N   
9268 C CA  . THR C 4   ? 0.40257 0.41120 0.39924 0.08934  0.01564  -0.03950 4   THR C CA  
9269 C C   . THR C 4   ? 0.38187 0.41214 0.39294 0.07972  0.01331  -0.03807 4   THR C C   
9270 O O   . THR C 4   ? 0.37295 0.39421 0.38705 0.06906  0.01133  -0.03672 4   THR C O   
9271 C CB  . THR C 4   ? 0.52356 0.50885 0.51013 0.09465  0.01493  -0.03720 4   THR C CB  
9272 O OG1 . THR C 4   ? 0.59060 0.55170 0.56115 0.10260  0.01754  -0.03884 4   THR C OG1 
9273 C CG2 . THR C 4   ? 0.49866 0.49959 0.48816 0.10516  0.01404  -0.03477 4   THR C CG2 
9281 N N   A PHE C 5   ? 0.36470 0.42340 0.38379 0.08356  0.01369  -0.03852 5   PHE C N   
9282 N N   B PHE C 5   ? 0.36524 0.42393 0.38446 0.08352  0.01357  -0.03841 5   PHE C N   
9283 C CA  A PHE C 5   ? 0.34209 0.41923 0.37209 0.07589  0.01142  -0.03731 5   PHE C CA  
9284 C CA  B PHE C 5   ? 0.34099 0.41846 0.37180 0.07396  0.01143  -0.03745 5   PHE C CA  
9285 C C   A PHE C 5   ? 0.36581 0.43102 0.39233 0.07967  0.00926  -0.03472 5   PHE C C   
9286 C C   B PHE C 5   ? 0.36326 0.43897 0.39325 0.07912  0.00918  -0.03506 5   PHE C C   
9287 O O   A PHE C 5   ? 0.38306 0.43889 0.40082 0.09251  0.00980  -0.03361 5   PHE C O   
9288 O O   B PHE C 5   ? 0.34599 0.43022 0.37292 0.09243  0.00943  -0.03438 5   PHE C O   
9289 C CB  A PHE C 5   ? 0.33346 0.44475 0.37146 0.08031  0.01198  -0.03831 5   PHE C CB  
9290 C CB  B PHE C 5   ? 0.33903 0.44950 0.37892 0.07305  0.01255  -0.03908 5   PHE C CB  
9291 C CG  A PHE C 5   ? 0.30824 0.43595 0.35040 0.07605  0.01451  -0.04067 5   PHE C CG  
9292 C CG  B PHE C 5   ? 0.32334 0.45158 0.37304 0.06241  0.01053  -0.03866 5   PHE C CG  
9293 C CD1 A PHE C 5   ? 0.36890 0.48254 0.40913 0.06631  0.01559  -0.04143 5   PHE C CD1 
9294 C CD1 B PHE C 5   ? 0.35020 0.47036 0.40283 0.04755  0.00995  -0.03854 5   PHE C CD1 
9295 C CD2 A PHE C 5   ? 0.37971 0.53931 0.42774 0.08180  0.01587  -0.04194 5   PHE C CD2 
9296 C CD2 B PHE C 5   ? 0.35110 0.50343 0.40583 0.06758  0.00925  -0.03850 5   PHE C CD2 
9297 C CE1 A PHE C 5   ? 0.32661 0.45575 0.36961 0.06259  0.01827  -0.04330 5   PHE C CE1 
9298 C CE1 B PHE C 5   ? 0.31219 0.44430 0.37126 0.03747  0.00852  -0.03860 5   PHE C CE1 
9299 C CE2 A PHE C 5   ? 0.39840 0.57518 0.45010 0.07750  0.01874  -0.04405 5   PHE C CE2 
9300 C CE2 B PHE C 5   ? 0.34554 0.51273 0.40782 0.05635  0.00740  -0.03881 5   PHE C CE2 
9301 C CZ  A PHE C 5   ? 0.33002 0.49031 0.37876 0.06770  0.02000  -0.04461 5   PHE C CZ  
9302 C CZ  B PHE C 5   ? 0.35265 0.50807 0.41646 0.04103  0.00726  -0.03905 5   PHE C CZ  
9321 N N   . GLN C 6   ? 0.33360 0.39932 0.36589 0.06941  0.00710  -0.03362 6   GLN C N   
9322 C CA  . GLN C 6   ? 0.33398 0.39191 0.36320 0.07336  0.00521  -0.03112 6   GLN C CA  
9323 C C   . GLN C 6   ? 0.35192 0.43532 0.38898 0.07329  0.00328  -0.03083 6   GLN C C   
9324 O O   . GLN C 6   ? 0.32141 0.40168 0.35953 0.06921  0.00131  -0.02940 6   GLN C O   
9325 C CB  . GLN C 6   ? 0.34524 0.38030 0.37209 0.06408  0.00432  -0.02987 6   GLN C CB  
9326 C CG  . GLN C 6   ? 0.36131 0.37129 0.37742 0.06735  0.00597  -0.02994 6   GLN C CG  
9327 C CD  . GLN C 6   ? 0.37028 0.35853 0.38275 0.05955  0.00525  -0.02857 6   GLN C CD  
9328 O OE1 . GLN C 6   ? 0.35147 0.34174 0.37045 0.04902  0.00428  -0.02872 6   GLN C OE1 
9329 N NE2 . GLN C 6   ? 0.39614 0.36299 0.39710 0.06483  0.00604  -0.02718 6   GLN C NE2 
9339 N N   . SER C 7   ? 0.35394 0.46423 0.39610 0.07807  0.00389  -0.03236 7   SER C N   
9340 C CA  . SER C 7   ? 0.33736 0.47289 0.38389 0.08359  0.00196  -0.03180 7   SER C CA  
9341 C C   . SER C 7   ? 0.38697 0.51162 0.42369 0.10002  0.00157  -0.02880 7   SER C C   
9342 O O   . SER C 7   ? 0.40871 0.50592 0.43486 0.10610  0.00317  -0.02756 7   SER C O   
9343 C CB  . SER C 7   ? 0.38650 0.55607 0.44077 0.08531  0.00295  -0.03416 7   SER C CB  
9344 O OG  . SER C 7   ? 0.39679 0.56216 0.44623 0.09501  0.00587  -0.03484 7   SER C OG  
9350 N N   . ALA C 8   ? 0.41420 0.55972 0.45310 0.10711  -0.00052 -0.02755 8   ALA C N   
9351 C CA  . ALA C 8   ? 0.45124 0.58920 0.47984 0.12471  -0.00080 -0.02410 8   ALA C CA  
9352 C C   . ALA C 8   ? 0.54555 0.71783 0.57796 0.13806  -0.00102 -0.02441 8   ALA C C   
9353 O O   . ALA C 8   ? 0.42126 0.62737 0.46570 0.13101  -0.00248 -0.02672 8   ALA C O   
9354 C CB  . ALA C 8   ? 0.56095 0.69051 0.58653 0.12290  -0.00346 -0.02119 8   ALA C CB  
9360 N N   . VAL C 9   ? 0.93493 1.09845 0.95633 0.15724  0.00068  -0.02220 9   VAL C N   
9361 C CA  . VAL C 9   ? 0.86220 1.05846 0.88597 0.17347  0.00081  -0.02206 9   VAL C CA  
9362 C C   . VAL C 9   ? 0.86080 1.04757 0.87132 0.19405  0.00016  -0.01719 9   VAL C C   
9363 O O   . VAL C 9   ? 0.96952 1.18725 0.98256 0.20781  -0.00123 -0.01586 9   VAL C O   
9364 C CB  . VAL C 9   ? 0.90868 1.10866 0.93195 0.17929  0.00473  -0.02487 9   VAL C CB  
9365 C CG1 . VAL C 9   ? 0.87684 1.11491 0.90343 0.19718  0.00509  -0.02474 9   VAL C CG1 
9366 C CG2 . VAL C 9   ? 0.80830 1.01561 0.84299 0.15891  0.00560  -0.02905 9   VAL C CG2 
9376 C C1  . EDO D .   ? 0.60098 0.81260 0.62836 -0.20165 0.02909  -0.07311 401 EDO A C1  
9377 O O1  . EDO D .   ? 0.68379 0.86388 0.69405 -0.21355 0.03055  -0.07534 401 EDO A O1  
9378 C C2  . EDO D .   ? 0.51250 0.76762 0.55417 -0.19491 0.02440  -0.07603 401 EDO A C2  
9379 O O2  . EDO D .   ? 0.56622 0.84741 0.60554 -0.20481 0.02604  -0.07784 401 EDO A O2  
9386 C C1  . EDO E .   ? 0.63261 0.62424 0.61326 0.10941  -0.00209 -0.00632 402 EDO A C1  
9387 O O1  . EDO E .   ? 0.68430 0.65897 0.65690 0.11506  0.00059  -0.00702 402 EDO A O1  
9388 C C2  . EDO E .   ? 0.82922 0.85180 0.81538 0.11904  -0.00446 -0.00639 402 EDO A C2  
9389 O O2  . EDO E .   ? 0.81578 0.85180 0.80585 0.11516  -0.00709 -0.00533 402 EDO A O2  
9396 C C1  . EDO F .   ? 0.75649 0.75549 0.77879 -0.04163 -0.01489 -0.02683 403 EDO A C1  
9397 O O1  . EDO F .   ? 0.89816 0.88399 0.91018 -0.04639 -0.01426 -0.03131 403 EDO A O1  
9398 C C2  . EDO F .   ? 0.79364 0.79111 0.81947 -0.04338 -0.01341 -0.02579 403 EDO A C2  
9399 O O2  . EDO F .   ? 0.80857 0.79051 0.83236 -0.03890 -0.01070 -0.02598 403 EDO A O2  
9406 C C1  . EDO G .   ? 0.74216 0.87820 0.83030 -0.03255 0.01526  -0.00074 404 EDO A C1  
9407 O O1  . EDO G .   ? 0.66247 0.79077 0.75081 -0.02639 0.01174  -0.00165 404 EDO A O1  
9408 C C2  . EDO G .   ? 0.76431 0.87409 0.84287 -0.03791 0.01651  -0.00105 404 EDO A C2  
9409 O O2  . EDO G .   ? 0.82280 0.92041 0.89575 -0.04898 0.01483  -0.00194 404 EDO A O2  
9416 C C1  . PEG H .   ? 0.67814 0.84891 0.71173 -0.04793 -0.01734 -0.06327 405 PEG A C1  
9417 O O1  . PEG H .   ? 0.75143 0.91157 0.77675 -0.06252 -0.01580 -0.06917 405 PEG A O1  
9418 C C2  . PEG H .   ? 0.63286 0.77914 0.66501 -0.03615 -0.01599 -0.05791 405 PEG A C2  
9419 O O2  . PEG H .   ? 0.80925 0.94717 0.83444 -0.03496 -0.01654 -0.05853 405 PEG A O2  
9420 C C3  . PEG H .   ? 0.75527 0.87064 0.77865 -0.02595 -0.01479 -0.05389 405 PEG A C3  
9421 C C4  . PEG H .   ? 0.65383 0.75443 0.66879 -0.02951 -0.01349 -0.05629 405 PEG A C4  
9422 O O4  . PEG H .   ? 0.60009 0.67477 0.61314 -0.02852 -0.00993 -0.05469 405 PEG A O4  
9433 C C1  . EDO I .   ? 0.79081 0.71753 0.80135 -0.02479 0.00009  -0.02241 401 EDO B C1  
9434 O O1  . EDO I .   ? 0.77873 0.72033 0.79794 -0.02847 -0.00085 -0.02068 401 EDO B O1  
9435 C C2  . EDO I .   ? 0.86535 0.77471 0.86416 -0.02831 0.00210  -0.02249 401 EDO B C2  
9436 O O2  . EDO I .   ? 0.81845 0.71178 0.80650 -0.02458 0.00313  -0.02473 401 EDO B O2  
9443 C C1  . PEG J .   ? 0.80387 0.73036 0.78896 0.08839  0.03879  -0.02181 402 PEG B C1  
9444 O O1  . PEG J .   ? 0.93991 0.86829 0.93198 0.07658  0.03448  -0.02101 402 PEG B O1  
9445 C C2  . PEG J .   ? 0.87340 0.82807 0.87043 0.09546  0.03890  -0.01831 402 PEG B C2  
9446 O O2  . PEG J .   ? 0.95245 0.90527 0.94209 0.11112  0.04297  -0.01750 402 PEG B O2  
9447 C C3  . PEG J .   ? 0.86526 0.80792 0.84466 0.11578  0.04742  -0.02168 402 PEG B C3  
9448 C C4  . PEG J .   ? 1.02107 0.93066 0.98076 0.12277  0.05077  -0.02402 402 PEG B C4  
9449 O O4  . PEG J .   ? 1.05588 0.94303 1.00540 0.11181  0.05108  -0.02935 402 PEG B O4  
9460 N N   . GLN K .   ? 0.69798 0.83815 0.73384 0.10318  0.06731  -0.01827 403 GLN B N   
9461 C CA  . GLN K .   ? 0.62772 0.74451 0.65905 0.10698  0.06380  -0.01929 403 GLN B CA  
9462 C C   . GLN K .   ? 0.64161 0.72531 0.65670 0.10934  0.06465  -0.02459 403 GLN B C   
9463 O O   . GLN K .   ? 0.48793 0.54802 0.49793 0.10463  0.06104  -0.02604 403 GLN B O   
9464 C CB  . GLN K .   ? 0.56252 0.67826 0.60231 0.09371  0.05785  -0.01637 403 GLN B CB  
9465 C CG  . GLN K .   ? 0.58004 0.72319 0.63356 0.09327  0.05621  -0.01196 403 GLN B CG  
9466 C CD  . GLN K .   ? 0.56891 0.70848 0.62887 0.07948  0.05056  -0.00976 403 GLN B CD  
9467 O OE1 . GLN K .   ? 0.45294 0.58712 0.51274 0.06697  0.04921  -0.00959 403 GLN B OE1 
9468 N NE2 . GLN K .   ? 0.52785 0.67000 0.59240 0.08264  0.04741  -0.00797 403 GLN B NE2 
9476 O O   . HOH L .   ? 0.83338 0.77079 0.78163 0.13162  0.00516  -0.00514 501 HOH A O   
9477 O O   . HOH L .   ? 0.52569 0.96473 0.58550 -0.14526 -0.02161 -0.09674 502 HOH A O   
9478 O O   . HOH L .   ? 0.33743 0.84441 0.47071 0.06539  -0.05058 0.03041  503 HOH A O   
9479 O O   . HOH L .   ? 0.57398 0.63240 0.63765 -0.04453 -0.00408 -0.01134 504 HOH A O   
9480 O O   . HOH L .   ? 0.41019 0.93912 0.52602 0.06138  0.03959  -0.05819 505 HOH A O   
9481 O O   . HOH L .   ? 0.41707 0.88137 0.43825 0.08713  -0.09231 0.05270  506 HOH A O   
9482 O O   . HOH L .   ? 0.56581 0.57353 0.57514 0.00992  -0.01437 0.00611  507 HOH A O   
9483 O O   . HOH L .   ? 0.36722 0.96914 0.50330 -0.05834 -0.05624 0.00017  508 HOH A O   
9484 O O   . HOH L .   ? 0.67649 1.12170 0.80059 -0.15600 -0.02044 -0.01768 509 HOH A O   
9485 O O   . HOH L .   ? 0.52020 0.69089 0.55450 0.06164  -0.02237 -0.02394 510 HOH A O   
9486 O O   . HOH L .   ? 0.44377 0.93463 0.55939 0.09333  0.00569  -0.04797 511 HOH A O   
9487 O O   . HOH L .   ? 0.40211 0.87548 0.54201 -0.06886 -0.04279 -0.00454 512 HOH A O   
9488 O O   . HOH L .   ? 0.57586 0.56798 0.56372 -0.05788 -0.01966 -0.04122 513 HOH A O   
9489 O O   . HOH L .   ? 0.58777 0.75235 0.60033 -0.09081 -0.01499 -0.08133 514 HOH A O   
9490 O O   . HOH L .   ? 0.52170 0.47449 0.50115 0.09195  0.00984  -0.02721 515 HOH A O   
9491 O O   . HOH L .   ? 0.48626 0.55996 0.50769 -0.06897 0.03164  -0.02786 516 HOH A O   
9492 O O   . HOH L .   ? 0.54943 0.94875 0.58922 0.16509  -0.06312 0.07166  517 HOH A O   
9493 O O   . HOH L .   ? 0.56842 0.49048 0.57305 0.04076  0.02289  -0.02123 518 HOH A O   
9494 O O   . HOH L .   ? 0.38750 0.66899 0.51447 -0.02840 0.00240  0.00224  519 HOH A O   
9495 O O   . HOH L .   ? 0.34529 0.85171 0.45509 -0.04285 -0.02469 -0.06993 520 HOH A O   
9496 O O   . HOH L .   ? 0.57619 0.91579 0.56709 0.06217  -0.08013 0.04375  521 HOH A O   
9497 O O   . HOH L .   ? 0.41328 0.51865 0.45949 -0.07067 -0.02568 -0.02353 522 HOH A O   
9498 O O   . HOH L .   ? 0.39545 0.38045 0.44682 -0.00727 -0.00164 -0.01376 523 HOH A O   
9499 O O   . HOH L .   ? 0.46575 0.41507 0.47303 -0.01273 -0.00296 -0.03283 524 HOH A O   
9500 O O   . HOH L .   ? 0.56969 0.62219 0.59053 -0.05977 -0.02555 -0.02906 525 HOH A O   
9501 O O   . HOH L .   ? 0.50442 0.89549 0.61433 -0.15046 -0.03182 -0.02343 526 HOH A O   
9502 O O   . HOH L .   ? 0.39359 0.35752 0.40794 0.03809  -0.00038 -0.01591 527 HOH A O   
9503 O O   . HOH L .   ? 0.37071 0.92652 0.48552 -0.10971 0.02372  -0.07056 528 HOH A O   
9504 O O   . HOH L .   ? 0.40741 0.41183 0.39942 -0.06533 0.00336  -0.06675 529 HOH A O   
9505 O O   . HOH L .   ? 0.49378 0.44381 0.49800 0.01949  -0.00024 0.00834  530 HOH A O   
9506 O O   . HOH L .   ? 0.45766 0.47889 0.50795 -0.03106 -0.00981 -0.01563 531 HOH A O   
9507 O O   . HOH L .   ? 0.41355 0.96435 0.53159 0.07105  -0.00995 -0.04914 532 HOH A O   
9508 O O   . HOH L .   ? 0.48218 0.57462 0.51625 -0.00606 -0.01199 -0.04198 533 HOH A O   
9509 O O   . HOH L .   ? 0.44238 0.48836 0.46189 -0.02496 0.02167  -0.02843 534 HOH A O   
9510 O O   . HOH L .   ? 0.51949 0.34436 0.46911 0.02148  0.02676  -0.01160 535 HOH A O   
9511 O O   . HOH L .   ? 0.54368 0.70809 0.50695 -0.20563 -0.00278 -0.11757 536 HOH A O   
9512 O O   . HOH L .   ? 0.57282 0.51465 0.55465 -0.07839 0.02846  -0.01973 537 HOH A O   
9513 O O   . HOH L .   ? 0.47987 0.52624 0.46829 -0.15885 0.02099  -0.07089 538 HOH A O   
9514 O O   . HOH L .   ? 0.42795 0.36299 0.44029 0.03468  0.00771  0.00124  539 HOH A O   
9515 O O   . HOH L .   ? 0.41049 0.36386 0.44256 0.02446  0.01015  -0.01193 540 HOH A O   
9516 O O   . HOH L .   ? 0.32251 0.46078 0.36790 0.07345  -0.00932 -0.02568 541 HOH A O   
9517 O O   . HOH L .   ? 0.69093 0.86439 0.73655 -0.16366 -0.01806 -0.03362 542 HOH A O   
9518 O O   . HOH L .   ? 0.29966 0.33611 0.34653 -0.00745 -0.00219 -0.03449 543 HOH A O   
9519 O O   . HOH L .   ? 0.75715 0.66787 0.65654 0.13219  -0.00114 0.07163  544 HOH A O   
9520 O O   . HOH L .   ? 0.34575 0.29797 0.38029 0.01215  0.00685  -0.01354 545 HOH A O   
9521 O O   . HOH L .   ? 0.50517 0.49982 0.55357 -0.02288 -0.00428 -0.01491 546 HOH A O   
9522 O O   . HOH L .   ? 0.47833 0.53046 0.53441 0.05856  0.02538  -0.00771 547 HOH A O   
9523 O O   . HOH L .   ? 0.47403 0.45367 0.47499 -0.00803 0.00258  -0.03269 548 HOH A O   
9524 O O   . HOH L .   ? 0.47585 0.49635 0.47559 0.02168  -0.01810 0.01530  549 HOH A O   
9525 O O   . HOH L .   ? 0.45090 0.89353 0.51554 -0.00410 -0.08038 0.01196  550 HOH A O   
9526 O O   . HOH L .   ? 0.54355 0.82644 0.59413 0.15454  -0.01085 -0.02239 551 HOH A O   
9527 O O   . HOH L .   ? 0.49393 0.45511 0.46329 0.05075  -0.00688 0.03300  552 HOH A O   
9528 O O   . HOH L .   ? 0.36179 0.83450 0.41929 0.07448  -0.08292 0.04308  553 HOH A O   
9529 O O   . HOH L .   ? 0.61409 0.67867 0.61653 -0.02672 -0.03063 -0.01574 554 HOH A O   
9530 O O   . HOH L .   ? 0.55445 0.71984 0.59003 -0.12230 -0.03523 -0.03681 555 HOH A O   
9531 O O   . HOH L .   ? 0.40734 0.86135 0.55533 0.12983  0.00069  0.02982  556 HOH A O   
9532 O O   . HOH L .   ? 0.67744 1.22574 0.73476 -0.17637 -0.01536 -0.10367 557 HOH A O   
9533 O O   . HOH L .   ? 0.60836 0.48607 0.55785 0.05888  0.01429  -0.03888 558 HOH A O   
9534 O O   . HOH L .   ? 0.58450 0.50570 0.56780 -0.00995 0.00055  -0.04125 559 HOH A O   
9535 O O   . HOH L .   ? 0.49816 0.52124 0.50784 0.12723  0.00499  0.03050  560 HOH A O   
9536 O O   . HOH L .   ? 0.49468 0.51910 0.50780 -0.04612 0.02361  -0.02162 561 HOH A O   
9537 O O   . HOH L .   ? 0.49977 0.40426 0.47920 -0.01075 0.01930  -0.04744 562 HOH A O   
9538 O O   . HOH L .   ? 0.49688 0.61293 0.57480 0.06133  0.02371  -0.00096 563 HOH A O   
9539 O O   . HOH L .   ? 0.44540 0.81901 0.44466 0.10065  -0.08094 0.05935  564 HOH A O   
9540 O O   . HOH L .   ? 0.35210 0.34362 0.40516 0.01308  0.00250  -0.00895 565 HOH A O   
9541 O O   . HOH L .   ? 0.53653 0.69426 0.51700 0.15797  -0.03565 0.07193  566 HOH A O   
9542 O O   . HOH L .   ? 0.35951 0.86336 0.47571 -0.01205 -0.06749 0.00987  567 HOH A O   
9543 O O   . HOH L .   ? 0.38137 0.63439 0.44393 0.02205  0.03811  -0.05017 568 HOH A O   
9544 O O   . HOH L .   ? 0.59420 0.63320 0.54166 0.19656  -0.00995 0.07490  569 HOH A O   
9545 O O   . HOH L .   ? 0.44008 0.89415 0.56481 0.16518  -0.01015 0.04175  570 HOH A O   
9546 O O   . HOH L .   ? 0.49774 0.49595 0.50285 -0.02052 -0.01362 -0.02238 571 HOH A O   
9547 O O   . HOH L .   ? 0.31197 0.28095 0.35117 -0.00806 -0.00330 -0.01980 572 HOH A O   
9548 O O   . HOH L .   ? 0.53120 0.68256 0.51131 0.06632  -0.04615 0.04370  573 HOH A O   
9549 O O   . HOH L .   ? 0.70199 0.78233 0.63602 0.15197  -0.03156 0.08134  574 HOH A O   
9550 O O   . HOH L .   ? 0.55014 0.76283 0.57230 0.19896  -0.02143 0.06567  575 HOH A O   
9551 O O   . HOH L .   ? 0.25827 0.32361 0.32658 0.00646  -0.00911 -0.00215 576 HOH A O   
9552 O O   . HOH L .   ? 0.40768 0.64335 0.46925 -0.08979 0.03809  -0.04502 577 HOH A O   
9553 O O   . HOH L .   ? 0.43189 0.47759 0.44136 -0.12229 0.02679  -0.04634 578 HOH A O   
9554 O O   . HOH L .   ? 0.44116 0.42696 0.44618 -0.00656 -0.00663 -0.00568 579 HOH A O   
9555 O O   . HOH L .   ? 0.56601 0.95646 0.68754 0.16816  0.00354  0.03523  580 HOH A O   
9556 O O   . HOH L .   ? 0.36787 0.35150 0.39332 0.02989  -0.00417 0.00718  581 HOH A O   
9557 O O   . HOH L .   ? 0.36313 0.55764 0.41860 0.01115  0.03149  -0.04605 582 HOH A O   
9558 O O   . HOH L .   ? 0.37167 0.28794 0.36152 0.03993  0.00368  -0.01344 583 HOH A O   
9559 O O   . HOH L .   ? 0.35936 0.76965 0.46312 0.09664  0.00586  -0.04515 584 HOH A O   
9560 O O   . HOH L .   ? 0.45575 0.85627 0.54392 0.14561  0.00372  -0.03857 585 HOH A O   
9561 O O   . HOH L .   ? 0.52865 0.38779 0.50048 -0.00644 0.02228  -0.02476 586 HOH A O   
9562 O O   . HOH L .   ? 0.51783 1.04713 0.59593 -0.03246 -0.04695 -0.07256 587 HOH A O   
9563 O O   . HOH L .   ? 0.48015 0.74862 0.47409 0.15094  -0.05609 0.07375  588 HOH A O   
9564 O O   . HOH L .   ? 0.34779 0.84371 0.43335 -0.10131 -0.07375 -0.01937 589 HOH A O   
9565 O O   . HOH L .   ? 0.71938 0.74423 0.70269 -0.13932 0.04314  -0.03053 590 HOH A O   
9566 O O   . HOH L .   ? 0.36694 0.72816 0.45450 0.04607  -0.02266 -0.04328 591 HOH A O   
9567 O O   . HOH L .   ? 0.40845 0.69302 0.53809 0.00918  0.00638  0.00641  592 HOH A O   
9568 O O   . HOH L .   ? 0.40862 0.36565 0.41450 -0.06004 0.01868  -0.02849 593 HOH A O   
9569 O O   . HOH L .   ? 0.48861 0.47154 0.49441 -0.02666 0.01295  -0.01415 594 HOH A O   
9570 O O   . HOH L .   ? 0.41098 0.74529 0.47367 -0.09147 -0.06090 -0.02278 595 HOH A O   
9571 O O   . HOH L .   ? 0.32641 0.58513 0.36841 0.05121  0.04999  -0.05674 596 HOH A O   
9572 O O   . HOH L .   ? 0.25855 0.42965 0.32762 0.00607  0.01455  -0.04237 597 HOH A O   
9573 O O   . HOH L .   ? 0.62496 0.51225 0.61093 0.04531  0.02408  -0.01617 598 HOH A O   
9574 O O   . HOH L .   ? 0.60952 0.41124 0.54310 -0.00654 0.03070  -0.02115 599 HOH A O   
9575 O O   . HOH L .   ? 0.34968 0.42938 0.38289 -0.04321 0.02533  -0.03113 600 HOH A O   
9576 O O   . HOH L .   ? 0.70852 0.89430 0.74686 -0.20225 -0.01160 -0.03609 601 HOH A O   
9577 O O   . HOH L .   ? 0.45612 0.37258 0.42403 0.01520  0.00883  -0.04830 602 HOH A O   
9578 O O   . HOH L .   ? 0.54765 0.72746 0.62890 0.10466  0.03905  0.00079  603 HOH A O   
9579 O O   . HOH L .   ? 0.65889 0.52988 0.57048 -0.14128 0.02959  -0.07985 604 HOH A O   
9580 O O   . HOH L .   ? 0.35034 0.34638 0.40453 0.01735  0.00642  -0.00972 605 HOH A O   
9581 O O   . HOH L .   ? 0.38159 0.84279 0.48621 0.07721  0.04243  -0.05810 606 HOH A O   
9582 O O   . HOH L .   ? 0.52042 0.46258 0.51559 -0.02248 0.01188  -0.00453 607 HOH A O   
9583 O O   . HOH L .   ? 0.60294 0.59420 0.58396 -0.11303 0.03844  -0.02367 608 HOH A O   
9584 O O   . HOH L .   ? 0.65614 0.63818 0.62509 -0.15049 0.03965  -0.03971 609 HOH A O   
9585 O O   . HOH L .   ? 0.44713 0.96083 0.58020 0.14691  -0.02102 0.04246  610 HOH A O   
9586 O O   . HOH L .   ? 0.47496 0.39610 0.48488 -0.00646 0.00157  -0.02137 611 HOH A O   
9587 O O   . HOH L .   ? 0.45796 0.71022 0.43911 0.12369  -0.06009 0.06816  612 HOH A O   
9588 O O   . HOH L .   ? 0.58121 0.52011 0.56031 -0.03563 -0.00759 -0.04369 613 HOH A O   
9589 O O   . HOH L .   ? 0.58325 0.77840 0.63145 -0.00458 -0.02096 -0.04769 614 HOH A O   
9590 O O   . HOH L .   ? 0.37759 0.29826 0.38224 0.00325  0.00188  -0.02708 615 HOH A O   
9591 O O   . HOH L .   ? 0.40733 0.50769 0.48937 -0.02525 0.00032  -0.00511 616 HOH A O   
9592 O O   . HOH L .   ? 0.40388 0.83568 0.55737 0.10157  0.00502  0.02313  617 HOH A O   
9593 O O   . HOH L .   ? 0.34578 0.43957 0.38049 -0.02478 0.02566  -0.03446 618 HOH A O   
9594 O O   . HOH L .   ? 0.32251 0.32356 0.35548 -0.00609 0.00683  -0.02807 619 HOH A O   
9595 O O   . HOH L .   ? 0.55978 0.41643 0.49178 -0.11163 0.03619  -0.03840 620 HOH A O   
9596 O O   . HOH L .   ? 0.52281 1.23043 0.65053 -0.00141 0.00393  -0.06509 621 HOH A O   
9597 O O   . HOH L .   ? 0.68259 0.56786 0.63363 -0.09547 0.03400  -0.02487 622 HOH A O   
9598 O O   . HOH L .   ? 0.45775 0.56016 0.50519 -0.08649 -0.02086 -0.02497 623 HOH A O   
9599 O O   . HOH L .   ? 0.57698 0.64195 0.55075 0.18694  -0.00861 0.06463  624 HOH A O   
9600 O O   . HOH L .   ? 0.52472 0.55141 0.52725 -0.03182 -0.00256 -0.05622 625 HOH A O   
9601 O O   . HOH L .   ? 0.41009 1.05717 0.51648 -0.12475 0.00719  -0.08186 626 HOH A O   
9602 O O   . HOH L .   ? 0.65992 0.78107 0.68528 0.02703  -0.01903 -0.03064 627 HOH A O   
9603 O O   . HOH L .   ? 0.30804 0.44499 0.35458 -0.01410 0.02733  -0.03974 628 HOH A O   
9604 O O   . HOH L .   ? 0.58843 0.55975 0.55290 -0.02369 -0.00565 -0.04443 629 HOH A O   
9605 O O   . HOH L .   ? 0.40529 0.31699 0.40923 -0.01764 0.01378  -0.02097 630 HOH A O   
9606 O O   . HOH L .   ? 0.47347 0.45796 0.52551 0.00062  -0.00073 -0.01243 631 HOH A O   
9607 O O   . HOH L .   ? 0.53660 0.60474 0.55763 0.00227  -0.01104 -0.03765 632 HOH A O   
9608 O O   . HOH L .   ? 0.51562 0.78951 0.55277 0.15041  0.04199  -0.05688 633 HOH A O   
9609 O O   . HOH L .   ? 0.45839 0.90660 0.47007 0.02471  -0.09654 0.02684  634 HOH A O   
9610 O O   . HOH L .   ? 0.56497 0.65344 0.54723 0.15889  0.03280  -0.05082 635 HOH A O   
9611 O O   . HOH L .   ? 0.51018 0.37258 0.45960 -0.06008 0.02992  -0.01103 636 HOH A O   
9612 O O   . HOH L .   ? 0.44085 0.84626 0.50430 -0.11338 -0.07166 -0.02839 637 HOH A O   
9613 O O   . HOH L .   ? 0.36119 0.73482 0.44475 -0.15671 0.03885  -0.06267 638 HOH A O   
9614 O O   . HOH L .   ? 0.57498 0.56117 0.54749 0.02031  0.01837  -0.05238 639 HOH A O   
9615 O O   . HOH L .   ? 0.62618 0.63781 0.58366 0.13970  0.03304  -0.05443 640 HOH A O   
9616 O O   . HOH L .   ? 0.34626 0.66141 0.42572 -0.01545 0.04168  -0.05045 641 HOH A O   
9617 O O   . HOH L .   ? 0.34363 0.39306 0.37055 0.02473  -0.01994 0.01150  642 HOH A O   
9618 O O   . HOH L .   ? 0.49154 0.61494 0.51817 0.10636  -0.00923 -0.01798 643 HOH A O   
9619 O O   . HOH L .   ? 0.47813 0.66728 0.51439 -0.13517 0.04405  -0.04267 644 HOH A O   
9620 O O   . HOH L .   ? 0.67072 0.66017 0.66942 -0.01396 -0.00509 -0.01776 645 HOH A O   
9621 O O   . HOH L .   ? 0.46286 0.45945 0.51179 0.03432  0.01045  -0.00755 646 HOH A O   
9622 O O   . HOH L .   ? 0.54406 0.52651 0.54871 0.11009  0.01069  0.02123  647 HOH A O   
9623 O O   . HOH L .   ? 0.42673 0.67921 0.45376 0.18184  -0.03384 0.06729  648 HOH A O   
9624 O O   . HOH L .   ? 0.52638 0.59741 0.60183 -0.01825 0.00482  -0.00526 649 HOH A O   
9625 O O   . HOH L .   ? 0.54048 0.54339 0.54016 -0.00844 -0.01268 -0.00699 650 HOH A O   
9626 O O   . HOH L .   ? 0.70110 0.90111 0.74801 0.02913  -0.02314 -0.03666 651 HOH A O   
9627 O O   . HOH L .   ? 0.58283 0.53710 0.57323 -0.03297 0.01626  -0.00592 652 HOH A O   
9628 O O   . HOH L .   ? 0.40055 0.89233 0.46086 0.01749  -0.08934 0.02186  653 HOH A O   
9629 O O   . HOH L .   ? 0.43781 0.41432 0.47992 0.00221  0.00613  -0.01378 654 HOH A O   
9630 O O   . HOH L .   ? 0.53402 0.45599 0.49406 0.10285  0.00876  -0.01760 655 HOH A O   
9631 O O   . HOH L .   ? 0.65593 0.50582 0.57955 -0.07158 0.02651  -0.07088 656 HOH A O   
9632 O O   . HOH L .   ? 0.42864 0.88941 0.55479 -0.11718 -0.04095 -0.01591 657 HOH A O   
9633 O O   . HOH L .   ? 0.61300 0.56242 0.54224 0.08650  -0.00824 0.05662  658 HOH A O   
9634 O O   . HOH L .   ? 0.47119 0.41746 0.47537 0.05910  0.00601  0.01277  659 HOH A O   
9635 O O   . HOH L .   ? 0.68898 0.78283 0.69806 0.09651  -0.01508 -0.00904 660 HOH A O   
9636 O O   . HOH L .   ? 0.36022 0.52886 0.39415 0.00657  0.03859  -0.04596 661 HOH A O   
9637 O O   . HOH L .   ? 0.41529 0.86290 0.51064 -0.14863 0.03149  -0.06851 662 HOH A O   
9638 O O   . HOH L .   ? 0.74968 0.97027 0.78658 -0.20963 -0.02249 -0.04351 663 HOH A O   
9639 O O   . HOH L .   ? 0.47525 0.96349 0.57433 0.01807  -0.07254 0.01971  664 HOH A O   
9640 O O   . HOH L .   ? 0.43831 0.45498 0.49454 -0.01958 0.00851  -0.00681 665 HOH A O   
9641 O O   . HOH L .   ? 0.59080 0.67776 0.55934 0.07345  -0.03414 0.04776  666 HOH A O   
9642 O O   . HOH L .   ? 0.25378 0.15437 0.24194 0.00347  0.01168  0.00054  667 HOH A O   
9643 O O   . HOH L .   ? 0.67399 0.85273 0.71001 -0.00077 -0.02278 -0.04626 668 HOH A O   
9644 O O   . HOH L .   ? 0.64933 0.90014 0.70127 0.04241  -0.02750 -0.03591 669 HOH A O   
9645 O O   . HOH L .   ? 0.67229 1.02667 0.74107 0.12115  -0.02387 -0.02659 670 HOH A O   
9646 O O   . HOH L .   ? 0.52638 0.52919 0.51299 -0.05445 0.00222  -0.06717 671 HOH A O   
9647 O O   . HOH L .   ? 0.40775 1.05517 0.51887 0.10612  0.03824  -0.05776 672 HOH A O   
9648 O O   . HOH L .   ? 0.45754 0.40489 0.47085 0.02781  0.00263  0.00493  673 HOH A O   
9649 O O   . HOH L .   ? 0.67645 0.67661 0.67982 -0.03525 0.01905  -0.01637 674 HOH A O   
9650 O O   . HOH L .   ? 0.66890 1.26705 0.76016 -0.07170 -0.03140 -0.08116 675 HOH A O   
9651 O O   . HOH L .   ? 0.71044 1.34740 0.80070 -0.10776 -0.02144 -0.08839 676 HOH A O   
9652 O O   . HOH L .   ? 0.48236 0.41407 0.46613 -0.07574 0.02583  -0.02477 677 HOH A O   
9653 O O   . HOH L .   ? 0.46300 0.38747 0.45955 0.02106  0.00543  0.00722  678 HOH A O   
9654 O O   . HOH L .   ? 0.62695 0.62321 0.62630 -0.01646 -0.01075 -0.01934 679 HOH A O   
9655 O O   . HOH L .   ? 0.46821 0.44956 0.48462 0.02737  -0.00603 0.00995  680 HOH A O   
9656 O O   . HOH L .   ? 0.70264 0.77826 0.67581 0.04979  -0.03245 0.03646  681 HOH A O   
9657 O O   . HOH L .   ? 0.63277 0.64634 0.60438 0.02879  0.02567  -0.05525 682 HOH A O   
9658 O O   . HOH L .   ? 0.66587 1.31669 0.74903 -0.18306 0.01124  -0.09242 683 HOH A O   
9659 O O   . HOH L .   ? 0.67456 0.64301 0.65782 -0.06410 0.02853  -0.01052 684 HOH A O   
9660 O O   . HOH L .   ? 0.62962 0.79892 0.61411 0.00806  -0.05267 0.01325  685 HOH A O   
9661 O O   . HOH L .   ? 0.55792 0.53789 0.53998 0.03039  -0.00998 0.02321  686 HOH A O   
9662 O O   . HOH L .   ? 0.63748 0.86455 0.65606 -0.09776 -0.02189 -0.08646 687 HOH A O   
9663 O O   . HOH L .   ? 0.40504 0.64264 0.45340 0.01652  0.04457  -0.05046 688 HOH A O   
9664 O O   . HOH L .   ? 0.36611 0.54150 0.41277 -0.01026 0.03465  -0.04293 689 HOH A O   
9665 O O   . HOH L .   ? 0.57741 1.06484 0.70266 0.18314  0.00023  0.04149  690 HOH A O   
9666 O O   . HOH L .   ? 0.41738 0.91988 0.52413 -0.12752 0.03291  -0.06753 691 HOH A O   
9667 O O   . HOH L .   ? 0.78368 0.63362 0.67488 -0.14660 0.03097  -0.08969 692 HOH A O   
9668 O O   . HOH L .   ? 0.77179 1.35214 0.83263 -0.22160 0.01731  -0.09616 693 HOH A O   
9669 O O   . HOH L .   ? 0.70384 0.96378 0.74544 0.07236  -0.03122 -0.02669 694 HOH A O   
9670 O O   . HOH L .   ? 0.51195 0.82594 0.62131 0.15713  0.01336  0.02708  695 HOH A O   
9671 O O   . HOH L .   ? 0.51811 0.71210 0.56594 -0.07804 0.04034  -0.03928 696 HOH A O   
9672 O O   . HOH L .   ? 0.59166 0.78683 0.56568 0.16375  -0.04476 0.07864  697 HOH A O   
9673 O O   . HOH L .   ? 0.85114 0.77997 0.81800 -0.07899 0.03232  -0.01129 698 HOH A O   
9674 O O   . HOH L .   ? 0.48155 0.99560 0.62992 0.14633  0.00502  0.03268  699 HOH A O   
9675 O O   . HOH L .   ? 0.47410 0.98907 0.53150 0.10255  -0.08257 0.05307  700 HOH A O   
9676 O O   . HOH L .   ? 0.68008 0.56979 0.63370 -0.07566 0.03244  -0.01101 701 HOH A O   
9677 O O   . HOH L .   ? 0.51648 0.84237 0.55028 0.20332  -0.04141 0.07521  702 HOH A O   
9678 O O   . HOH L .   ? 0.65331 0.77262 0.63960 0.01709  -0.04176 0.01715  703 HOH A O   
9679 O O   . HOH L .   ? 0.56135 0.88867 0.56152 0.18470  -0.06050 0.08412  704 HOH A O   
9680 O O   . HOH L .   ? 0.54333 0.51281 0.55259 0.04992  -0.00141 0.01594  705 HOH A O   
9681 O O   . HOH L .   ? 0.52083 0.70897 0.51215 0.18810  -0.03268 0.07584  706 HOH A O   
9682 O O   . HOH L .   ? 0.46251 0.87724 0.55998 -0.12588 0.04242  -0.05976 707 HOH A O   
9683 O O   . HOH L .   ? 0.76490 0.68204 0.71253 -0.09311 0.03929  -0.00632 708 HOH A O   
9684 O O   . HOH L .   ? 0.64741 0.90114 0.63631 0.22074  -0.04162 0.08906  709 HOH A O   
9685 O O   . HOH M .   ? 0.84213 0.30510 0.49575 -0.13775 0.06325  -0.01688 501 HOH B O   
9686 O O   . HOH M .   ? 0.51510 0.64983 0.46021 -0.01260 0.08926  0.01929  502 HOH B O   
9687 O O   . HOH M .   ? 1.06456 0.45995 0.62574 -0.24021 0.08680  -0.01253 503 HOH B O   
9688 O O   . HOH M .   ? 0.81120 0.58772 0.58099 0.04666  0.07791  -0.12794 504 HOH B O   
9689 O O   . HOH M .   ? 0.64606 0.66848 0.49193 0.04193  0.06311  -0.07314 505 HOH B O   
9690 O O   . HOH M .   ? 0.96492 0.35857 0.57846 0.01264  0.06491  -0.00343 506 HOH B O   
9691 O O   . HOH M .   ? 0.46114 0.45036 0.49288 -0.03246 0.01638  -0.00099 507 HOH B O   
9692 O O   . HOH M .   ? 0.39076 0.41098 0.43282 0.05175  0.02761  -0.01405 508 HOH B O   
9693 O O   . HOH M .   ? 0.62532 0.70149 0.50748 -0.01722 -0.00309 -0.07993 509 HOH B O   
9694 O O   . HOH M .   ? 0.46499 0.40196 0.45021 0.00199  0.01530  0.00750  510 HOH B O   
9695 O O   . HOH M .   ? 0.60975 0.59604 0.40689 -0.02290 0.02756  -0.12358 511 HOH B O   
9696 O O   . HOH M .   ? 0.61001 0.43515 0.52968 0.07394  0.01304  -0.00742 512 HOH B O   
9697 O O   . HOH M .   ? 0.53362 0.41630 0.47356 0.00338  0.02086  0.02151  513 HOH B O   
9698 O O   . HOH M .   ? 0.61004 0.78809 0.60344 -0.05634 0.09008  0.02831  514 HOH B O   
9699 O O   . HOH M .   ? 0.49200 0.42555 0.44525 0.09969  0.05859  -0.04378 515 HOH B O   
9700 O O   . HOH M .   ? 0.43289 0.45043 0.38605 0.00934  0.03822  0.00590  516 HOH B O   
9701 O O   . HOH M .   ? 0.53835 0.56452 0.45918 -0.00326 0.05480  0.02413  517 HOH B O   
9702 O O   . HOH M .   ? 0.68633 0.59293 0.63181 -0.00199 0.02648  -0.06456 518 HOH B O   
9703 O O   . HOH M .   ? 0.41009 0.33967 0.40774 -0.01676 0.01486  0.00247  519 HOH B O   
9704 O O   . HOH M .   ? 0.47237 0.48855 0.44313 -0.01590 0.00147  -0.05831 520 HOH B O   
9705 O O   . HOH M .   ? 0.56560 0.61177 0.48409 0.02515  0.04799  -0.01819 521 HOH B O   
9706 O O   . HOH M .   ? 0.39177 0.25923 0.34344 -0.06970 0.02457  0.00422  522 HOH B O   
9707 O O   . HOH M .   ? 0.39892 0.77424 0.52821 -0.04303 0.05722  0.01105  523 HOH B O   
9708 O O   . HOH M .   ? 0.57439 0.90389 0.63808 -0.20339 0.07819  0.02294  524 HOH B O   
9709 O O   . HOH M .   ? 0.49883 0.66231 0.43133 0.05185  0.10315  -0.02049 525 HOH B O   
9710 O O   . HOH M .   ? 0.54306 0.46035 0.51684 -0.00870 0.01942  -0.05316 526 HOH B O   
9711 O O   . HOH M .   ? 0.37598 0.50991 0.41171 -0.02577 0.05812  0.01051  527 HOH B O   
9712 O O   . HOH M .   ? 0.55388 0.54147 0.48729 -0.06158 0.06215  0.04063  528 HOH B O   
9713 O O   . HOH M .   ? 0.51637 0.35195 0.41941 -0.05715 0.03986  0.03136  529 HOH B O   
9714 O O   . HOH M .   ? 0.41990 0.58141 0.51084 -0.00779 0.02824  0.00147  530 HOH B O   
9715 O O   . HOH M .   ? 0.35446 0.40606 0.39701 -0.04464 0.02915  0.00511  531 HOH B O   
9716 O O   . HOH M .   ? 0.83923 0.55722 0.69195 0.07418  0.02470  -0.01486 532 HOH B O   
9717 O O   . HOH M .   ? 0.53368 0.45813 0.54226 -0.03218 0.00512  -0.01406 533 HOH B O   
9718 O O   . HOH M .   ? 0.34129 0.28350 0.33898 -0.01690 0.01193  -0.04616 534 HOH B O   
9719 O O   . HOH M .   ? 0.47806 0.58538 0.46144 -0.15457 0.07767  0.03551  535 HOH B O   
9720 O O   . HOH M .   ? 0.45565 0.33712 0.42688 0.03715  0.00695  -0.01605 536 HOH B O   
9721 O O   . HOH M .   ? 0.74025 0.74853 0.79082 -0.01521 0.01173  -0.00592 537 HOH B O   
9722 O O   . HOH M .   ? 0.61491 0.47501 0.56292 -0.07707 0.00432  -0.03667 538 HOH B O   
9723 O O   . HOH M .   ? 0.40456 0.54372 0.40147 0.07116  0.08173  -0.02351 539 HOH B O   
9724 O O   . HOH M .   ? 0.51243 0.47233 0.52290 -0.06430 0.01664  -0.00232 540 HOH B O   
9725 O O   . HOH M .   ? 0.44105 0.42297 0.48382 -0.00400 0.00827  -0.00979 541 HOH B O   
9726 O O   . HOH M .   ? 0.45583 0.47662 0.46609 0.00611  -0.00280 -0.03201 542 HOH B O   
9727 O O   . HOH M .   ? 0.52745 0.40118 0.47663 0.07443  0.01121  -0.02175 543 HOH B O   
9728 O O   . HOH M .   ? 0.40687 0.38198 0.45280 -0.00439 0.00343  -0.01292 544 HOH B O   
9729 O O   . HOH M .   ? 0.59747 0.59448 0.61412 -0.09156 0.02065  -0.00128 545 HOH B O   
9730 O O   . HOH M .   ? 0.44246 0.53692 0.41578 -0.07421 0.07680  0.03456  546 HOH B O   
9731 O O   . HOH M .   ? 0.84968 0.63467 0.59805 0.05653  0.08539  -0.13709 547 HOH B O   
9732 O O   . HOH M .   ? 0.52985 0.55513 0.42360 0.02469  0.03231  0.01152  548 HOH B O   
9733 O O   . HOH M .   ? 0.69954 0.49884 0.59915 -0.09861 0.00924  -0.04762 549 HOH B O   
9734 O O   . HOH M .   ? 0.57858 0.57765 0.51925 -0.14443 0.07134  0.03971  550 HOH B O   
9735 O O   . HOH M .   ? 0.68932 0.49000 0.52470 0.08486  0.07622  -0.09123 551 HOH B O   
9736 O O   . HOH M .   ? 0.58197 0.70622 0.54788 -0.04839 0.08476  0.03087  552 HOH B O   
9737 O O   . HOH M .   ? 0.78893 0.57478 0.61514 -0.15978 0.07442  0.05179  553 HOH B O   
9738 O O   . HOH M .   ? 0.83120 0.52485 0.53314 0.11384  0.10966  -0.14008 554 HOH B O   
9739 O O   . HOH M .   ? 0.70483 0.64729 0.60507 -0.04638 0.01618  -0.09695 555 HOH B O   
9740 O O   . HOH M .   ? 0.45764 0.36674 0.44600 0.00857  0.00838  -0.00130 556 HOH B O   
9741 O O   . HOH M .   ? 0.59194 0.62735 0.58286 0.09628  -0.01047 -0.00265 557 HOH B O   
9742 O O   . HOH M .   ? 0.34012 0.26890 0.34356 -0.00427 0.00961  -0.00242 558 HOH B O   
9743 O O   . HOH M .   ? 0.63113 0.66452 0.61141 0.12870  0.07200  -0.03562 559 HOH B O   
9744 O O   . HOH M .   ? 0.59032 0.57642 0.56809 -0.17939 0.02099  -0.01588 560 HOH B O   
9745 O O   . HOH M .   ? 0.47939 0.68177 0.55692 -0.08542 0.04470  0.01036  561 HOH B O   
9746 O O   . HOH M .   ? 0.75155 1.14016 0.80500 0.16479  0.11964  -0.01626 562 HOH B O   
9747 O O   . HOH M .   ? 0.48448 0.57238 0.46026 0.01661  -0.01516 -0.03374 563 HOH B O   
9748 O O   . HOH M .   ? 0.58086 0.61263 0.52238 -0.07026 0.07195  0.04118  564 HOH B O   
9749 O O   . HOH M .   ? 0.50327 0.41361 0.49575 -0.05521 0.00796  -0.01478 565 HOH B O   
9750 O O   . HOH M .   ? 0.41380 0.36269 0.41519 0.04247  0.00032  -0.01007 566 HOH B O   
9751 O O   . HOH M .   ? 0.66814 0.73988 0.67362 -0.00608 -0.01152 -0.04484 567 HOH B O   
9752 O O   . HOH M .   ? 0.41476 0.38506 0.38009 0.01034  0.02148  0.01162  568 HOH B O   
9753 O O   . HOH M .   ? 0.54273 0.56546 0.51948 0.09815  -0.01106 0.00384  569 HOH B O   
9754 O O   . HOH M .   ? 0.60667 0.38628 0.45694 -0.13841 0.05908  0.03527  570 HOH B O   
9755 O O   . HOH M .   ? 0.53640 0.66870 0.43909 0.03102  0.09373  -0.00994 571 HOH B O   
9756 O O   . HOH M .   ? 0.73782 0.72180 0.51309 0.06535  0.08873  -0.11083 572 HOH B O   
9757 O O   . HOH M .   ? 0.92876 0.68995 0.70975 -0.26668 0.08514  0.03447  573 HOH B O   
9758 O O   . HOH M .   ? 0.82936 0.81219 0.69194 0.19935  0.12161  -0.07903 574 HOH B O   
9759 O O   . HOH M .   ? 0.54319 0.59671 0.46122 0.04795  -0.00519 0.00195  575 HOH B O   
9760 O O   . HOH M .   ? 0.43446 0.51064 0.36141 0.02472  -0.00648 -0.02706 576 HOH B O   
9761 O O   . HOH M .   ? 0.64989 0.74456 0.56514 0.04653  -0.01453 -0.00909 577 HOH B O   
9762 O O   . HOH M .   ? 0.40287 0.43529 0.43634 -0.09733 0.00009  -0.01834 578 HOH B O   
9763 O O   . HOH M .   ? 0.44767 0.83030 0.54363 -0.07100 0.08825  0.01975  579 HOH B O   
9764 O O   . HOH M .   ? 0.55231 0.35943 0.43774 -0.00018 0.02932  0.03448  580 HOH B O   
9765 O O   . HOH M .   ? 0.48735 0.73205 0.50200 0.02433  0.09965  0.00094  581 HOH B O   
9766 O O   . HOH M .   ? 0.74781 0.84354 0.76559 0.01362  -0.01602 -0.03446 582 HOH B O   
9767 O O   . HOH M .   ? 0.52824 0.65914 0.58255 0.13009  0.04641  -0.00396 583 HOH B O   
9768 O O   . HOH M .   ? 0.32735 0.29566 0.36693 -0.01753 0.00212  -0.01290 584 HOH B O   
9769 O O   . HOH M .   ? 0.63210 0.72368 0.58334 -0.07100 0.08413  0.04020  585 HOH B O   
9770 O O   . HOH M .   ? 0.58393 0.59419 0.62004 -0.05883 0.01611  -0.00213 586 HOH B O   
9771 O O   . HOH M .   ? 0.77032 0.82953 0.64709 0.02638  0.04980  -0.01251 587 HOH B O   
9772 O O   . HOH M .   ? 0.64698 0.48524 0.53677 -0.08584 0.05016  0.03787  588 HOH B O   
9773 O O   . HOH M .   ? 0.57390 0.68528 0.57976 0.11302  0.07681  -0.02864 589 HOH B O   
9774 O O   . HOH M .   ? 0.58036 0.62717 0.47828 0.02613  0.04270  -0.02280 590 HOH B O   
9775 O O   . HOH M .   ? 0.76095 0.77005 0.79856 -0.06562 -0.00126 -0.01649 591 HOH B O   
9776 O O   . HOH M .   ? 0.93212 0.71310 0.76892 -0.06050 0.04064  -0.10921 592 HOH B O   
9777 O O   . HOH M .   ? 0.81989 0.69630 0.74705 0.11458  0.00904  -0.00250 593 HOH B O   
9778 O O   . HOH M .   ? 0.63738 0.79992 0.66297 0.10300  0.07901  -0.02149 594 HOH B O   
9779 O O   . HOH M .   ? 0.71858 0.56802 0.62177 0.01145  0.02505  0.03384  595 HOH B O   
9780 O O   . HOH M .   ? 0.62159 0.68705 0.64478 -0.13756 0.03165  0.00300  596 HOH B O   
9781 O O   . HOH M .   ? 0.59484 0.43265 0.53599 0.04231  0.01116  -0.01337 597 HOH B O   
9782 O O   . HOH M .   ? 0.87648 0.53735 0.60518 -0.11256 0.08308  0.08357  598 HOH B O   
9783 O O   . HOH M .   ? 0.50285 0.51775 0.43080 0.00719  0.04309  0.01663  599 HOH B O   
9784 O O   . HOH M .   ? 0.57331 0.52007 0.51523 0.01645  0.02077  0.02178  600 HOH B O   
9785 O O   . HOH M .   ? 0.63164 0.78606 0.53613 0.04556  0.10420  -0.01927 601 HOH B O   
9786 O O   . HOH M .   ? 0.65803 0.49454 0.53889 -0.12248 0.05750  0.03775  602 HOH B O   
9787 O O   . HOH M .   ? 0.75895 0.86264 0.74182 0.16271  0.09068  -0.03580 603 HOH B O   
9788 O O   . HOH M .   ? 0.73862 0.64218 0.69200 -0.01351 0.02261  -0.06260 604 HOH B O   
9789 O O   . HOH M .   ? 0.62247 0.72850 0.65145 -0.15842 0.03715  0.00486  605 HOH B O   
9790 O O   . HOH M .   ? 0.68082 0.71559 0.57859 0.05850  -0.00204 0.01765  606 HOH B O   
9791 O O   . HOH M .   ? 0.77444 0.57860 0.65412 -0.02705 0.03691  0.03766  607 HOH B O   
9792 O O   . HOH M .   ? 0.82317 0.85065 0.73609 -0.07879 0.08252  0.05183  608 HOH B O   
9793 O O   . HOH M .   ? 0.58335 0.94486 0.65532 -0.18085 0.08762  0.02694  609 HOH B O   
9794 O O   . HOH M .   ? 0.58395 0.80489 0.62940 0.09428  0.08302  -0.01451 610 HOH B O   
9795 O O   . HOH M .   ? 0.81064 1.06351 0.79747 0.22600  0.12323  -0.03455 611 HOH B O   
9796 O O   . HOH N .   ? 0.78109 0.70637 0.74504 0.07780  0.01625  -0.04095 101 HOH C O   
9797 O O   . HOH N .   ? 0.74929 0.71877 0.70140 0.10190  0.02954  -0.05720 102 HOH C O   
9798 O O   . HOH N .   ? 0.67030 0.65620 0.63066 0.12771  0.02641  -0.04775 103 HOH C O   
9799 O O   . HOH N .   ? 0.42352 0.63762 0.48435 0.09409  0.01008  -0.03946 104 HOH C O   
9800 O O   . HOH N .   ? 0.81405 0.73955 0.75503 0.07176  0.02500  -0.05917 105 HOH C O   
# 
