data_8RXP
# 
_entry.id   8RXP 
# 
_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   8RXP         pdb_00008rxp 10.2210/pdb8rxp/pdb 
WWPDB D_1292136471 ?            ?                   
# 
_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       2025-02-19 
# 
_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                        8RXP 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-07 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              guichou@cbs.cnrs.fr 
_pdbx_contact_author.name_first         jean-francois 
_pdbx_contact_author.name_last          guichou 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7699-3235 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Guichou, J.F.' 1 ? 
'Gelin, M.'     2 ? 
'Allemand, F.'  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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'TEAD2 with an inhibitor' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Guichou, J.F.' 1 ? 
primary 'Gelin, M.'     2 ? 
primary 'Allemand, F.'  3 ? 
# 
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 'Transcriptional enhancer factor TEF-4'       27489.096 2 ? ? ? ? 
2 non-polymer syn '2-(5-phenylmethoxy-1~{H}-indol-3-yl)ethanol' 267.322   2 ? ? ? ? 
3 water       nat water                                         18.015    7 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'TEA domain family member 2,TEAD-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MAWQARGLGTARLQLVEFSAFVEPPDAVDSYQRHLFVHISQHCPSPGAPPLESVDVRQIYDKFPEKKGGLRELYDRGPPH
AFFLVKFWADLNWGPSGEEAGAGGSISSGGFYGVSSQYESLEHMTLTCSSKVCSFGKQVVEKVETERAQLEDGRFVYRLL
RSPMCEYLVNFLHKLRQLPERYMMNSVLENFTILQVVTNRDTQELLLCTAYVFEVSTSERGAQHHIYRLVRDVEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAWQARGLGTARLQLVEFSAFVEPPDAVDSYQRHLFVHISQHCPSPGAPPLESVDVRQIYDKFPEKKGGLRELYDRGPPH
AFFLVKFWADLNWGPSGEEAGAGGSISSGGFYGVSSQYESLEHMTLTCSSKVCSFGKQVVEKVETERAQLEDGRFVYRLL
RSPMCEYLVNFLHKLRQLPERYMMNSVLENFTILQVVTNRDTQELLLCTAYVFEVSTSERGAQHHIYRLVRDVEHHHHHH
;
_entity_poly.pdbx_strand_id                 B,A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '2-(5-phenylmethoxy-1~{H}-indol-3-yl)ethanol' A1H3Y 
3 water                                         HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   TRP n 
1 4   GLN n 
1 5   ALA n 
1 6   ARG n 
1 7   GLY n 
1 8   LEU n 
1 9   GLY n 
1 10  THR n 
1 11  ALA n 
1 12  ARG n 
1 13  LEU n 
1 14  GLN n 
1 15  LEU n 
1 16  VAL n 
1 17  GLU n 
1 18  PHE n 
1 19  SER n 
1 20  ALA n 
1 21  PHE n 
1 22  VAL n 
1 23  GLU n 
1 24  PRO n 
1 25  PRO n 
1 26  ASP n 
1 27  ALA n 
1 28  VAL n 
1 29  ASP n 
1 30  SER n 
1 31  TYR n 
1 32  GLN n 
1 33  ARG n 
1 34  HIS n 
1 35  LEU n 
1 36  PHE n 
1 37  VAL n 
1 38  HIS n 
1 39  ILE n 
1 40  SER n 
1 41  GLN n 
1 42  HIS n 
1 43  CYS n 
1 44  PRO n 
1 45  SER n 
1 46  PRO n 
1 47  GLY n 
1 48  ALA n 
1 49  PRO n 
1 50  PRO n 
1 51  LEU n 
1 52  GLU n 
1 53  SER n 
1 54  VAL n 
1 55  ASP n 
1 56  VAL n 
1 57  ARG n 
1 58  GLN n 
1 59  ILE n 
1 60  TYR n 
1 61  ASP n 
1 62  LYS n 
1 63  PHE n 
1 64  PRO n 
1 65  GLU n 
1 66  LYS n 
1 67  LYS n 
1 68  GLY n 
1 69  GLY n 
1 70  LEU n 
1 71  ARG n 
1 72  GLU n 
1 73  LEU n 
1 74  TYR n 
1 75  ASP n 
1 76  ARG n 
1 77  GLY n 
1 78  PRO n 
1 79  PRO n 
1 80  HIS n 
1 81  ALA n 
1 82  PHE n 
1 83  PHE n 
1 84  LEU n 
1 85  VAL n 
1 86  LYS n 
1 87  PHE n 
1 88  TRP n 
1 89  ALA n 
1 90  ASP n 
1 91  LEU n 
1 92  ASN n 
1 93  TRP n 
1 94  GLY n 
1 95  PRO n 
1 96  SER n 
1 97  GLY n 
1 98  GLU n 
1 99  GLU n 
1 100 ALA n 
1 101 GLY n 
1 102 ALA n 
1 103 GLY n 
1 104 GLY n 
1 105 SER n 
1 106 ILE n 
1 107 SER n 
1 108 SER n 
1 109 GLY n 
1 110 GLY n 
1 111 PHE n 
1 112 TYR n 
1 113 GLY n 
1 114 VAL n 
1 115 SER n 
1 116 SER n 
1 117 GLN n 
1 118 TYR n 
1 119 GLU n 
1 120 SER n 
1 121 LEU n 
1 122 GLU n 
1 123 HIS n 
1 124 MET n 
1 125 THR n 
1 126 LEU n 
1 127 THR n 
1 128 CYS n 
1 129 SER n 
1 130 SER n 
1 131 LYS n 
1 132 VAL n 
1 133 CYS n 
1 134 SER n 
1 135 PHE n 
1 136 GLY n 
1 137 LYS n 
1 138 GLN n 
1 139 VAL n 
1 140 VAL n 
1 141 GLU n 
1 142 LYS n 
1 143 VAL n 
1 144 GLU n 
1 145 THR n 
1 146 GLU n 
1 147 ARG n 
1 148 ALA n 
1 149 GLN n 
1 150 LEU n 
1 151 GLU n 
1 152 ASP n 
1 153 GLY n 
1 154 ARG n 
1 155 PHE n 
1 156 VAL n 
1 157 TYR n 
1 158 ARG n 
1 159 LEU n 
1 160 LEU n 
1 161 ARG n 
1 162 SER n 
1 163 PRO n 
1 164 MET n 
1 165 CYS n 
1 166 GLU n 
1 167 TYR n 
1 168 LEU n 
1 169 VAL n 
1 170 ASN n 
1 171 PHE n 
1 172 LEU n 
1 173 HIS n 
1 174 LYS n 
1 175 LEU n 
1 176 ARG n 
1 177 GLN n 
1 178 LEU n 
1 179 PRO n 
1 180 GLU n 
1 181 ARG n 
1 182 TYR n 
1 183 MET n 
1 184 MET n 
1 185 ASN n 
1 186 SER n 
1 187 VAL n 
1 188 LEU n 
1 189 GLU n 
1 190 ASN n 
1 191 PHE n 
1 192 THR n 
1 193 ILE n 
1 194 LEU n 
1 195 GLN n 
1 196 VAL n 
1 197 VAL n 
1 198 THR n 
1 199 ASN n 
1 200 ARG n 
1 201 ASP n 
1 202 THR n 
1 203 GLN n 
1 204 GLU n 
1 205 LEU n 
1 206 LEU n 
1 207 LEU n 
1 208 CYS n 
1 209 THR n 
1 210 ALA n 
1 211 TYR n 
1 212 VAL n 
1 213 PHE n 
1 214 GLU n 
1 215 VAL n 
1 216 SER n 
1 217 THR n 
1 218 SER n 
1 219 GLU n 
1 220 ARG n 
1 221 GLY n 
1 222 ALA n 
1 223 GLN n 
1 224 HIS n 
1 225 HIS n 
1 226 ILE n 
1 227 TYR n 
1 228 ARG n 
1 229 LEU n 
1 230 VAL n 
1 231 ARG n 
1 232 ASP n 
1 233 VAL n 
1 234 GLU n 
1 235 HIS n 
1 236 HIS n 
1 237 HIS n 
1 238 HIS n 
1 239 HIS n 
1 240 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   240 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TEAD2, TEF4' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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                   ? 
# 
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 
A1H3Y non-polymer         . '2-(5-phenylmethoxy-1~{H}-indol-3-yl)ethanol' ? 'C17 H17 N O2'   267.322 
ALA   'L-peptide linking' y ALANINE                                       ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                      ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                    ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                               ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                      ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                     ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                               ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                       ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                     ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                         ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                    ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                       ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                        ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                    ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                 ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                       ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                        ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                     ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                    ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                      ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                        ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   216 ?   ?   ?   B . n 
A 1 2   ALA 2   217 ?   ?   ?   B . n 
A 1 3   TRP 3   218 ?   ?   ?   B . n 
A 1 4   GLN 4   219 ?   ?   ?   B . n 
A 1 5   ALA 5   220 220 ALA ALA B . n 
A 1 6   ARG 6   221 221 ARG ARG B . n 
A 1 7   GLY 7   222 222 GLY GLY B . n 
A 1 8   LEU 8   223 223 LEU LEU B . n 
A 1 9   GLY 9   224 224 GLY GLY B . n 
A 1 10  THR 10  225 225 THR THR B . n 
A 1 11  ALA 11  226 226 ALA ALA B . n 
A 1 12  ARG 12  227 227 ARG ARG B . n 
A 1 13  LEU 13  228 228 LEU LEU B . n 
A 1 14  GLN 14  229 229 GLN GLN B . n 
A 1 15  LEU 15  230 230 LEU LEU B . n 
A 1 16  VAL 16  231 231 VAL VAL B . n 
A 1 17  GLU 17  232 232 GLU GLU B . n 
A 1 18  PHE 18  233 233 PHE PHE B . n 
A 1 19  SER 19  234 234 SER SER B . n 
A 1 20  ALA 20  235 235 ALA ALA B . n 
A 1 21  PHE 21  236 236 PHE PHE B . n 
A 1 22  VAL 22  237 237 VAL VAL B . n 
A 1 23  GLU 23  238 238 GLU GLU B . n 
A 1 24  PRO 24  239 239 PRO PRO B . n 
A 1 25  PRO 25  240 240 PRO PRO B . n 
A 1 26  ASP 26  241 241 ASP ASP B . n 
A 1 27  ALA 27  242 242 ALA ALA B . n 
A 1 28  VAL 28  243 243 VAL VAL B . n 
A 1 29  ASP 29  244 244 ASP ASP B . n 
A 1 30  SER 30  245 245 SER SER B . n 
A 1 31  TYR 31  246 246 TYR TYR B . n 
A 1 32  GLN 32  247 247 GLN GLN B . n 
A 1 33  ARG 33  248 248 ARG ARG B . n 
A 1 34  HIS 34  249 249 HIS HIS B . n 
A 1 35  LEU 35  250 250 LEU LEU B . n 
A 1 36  PHE 36  251 251 PHE PHE B . n 
A 1 37  VAL 37  252 252 VAL VAL B . n 
A 1 38  HIS 38  253 253 HIS HIS B . n 
A 1 39  ILE 39  254 254 ILE ILE B . n 
A 1 40  SER 40  255 255 SER SER B . n 
A 1 41  GLN 41  256 256 GLN GLN B . n 
A 1 42  HIS 42  257 257 HIS HIS B . n 
A 1 43  CYS 43  258 ?   ?   ?   B . n 
A 1 44  PRO 44  259 ?   ?   ?   B . n 
A 1 45  SER 45  260 ?   ?   ?   B . n 
A 1 46  PRO 46  261 ?   ?   ?   B . n 
A 1 47  GLY 47  262 ?   ?   ?   B . n 
A 1 48  ALA 48  263 ?   ?   ?   B . n 
A 1 49  PRO 49  264 264 PRO PRO B . n 
A 1 50  PRO 50  265 265 PRO PRO B . n 
A 1 51  LEU 51  266 266 LEU LEU B . n 
A 1 52  GLU 52  267 267 GLU GLU B . n 
A 1 53  SER 53  268 268 SER SER B . n 
A 1 54  VAL 54  269 269 VAL VAL B . n 
A 1 55  ASP 55  270 270 ASP ASP B . n 
A 1 56  VAL 56  271 271 VAL VAL B . n 
A 1 57  ARG 57  272 272 ARG ARG B . n 
A 1 58  GLN 58  273 273 GLN GLN B . n 
A 1 59  ILE 59  274 274 ILE ILE B . n 
A 1 60  TYR 60  275 275 TYR TYR B . n 
A 1 61  ASP 61  276 276 ASP ASP B . n 
A 1 62  LYS 62  277 277 LYS LYS B . n 
A 1 63  PHE 63  278 278 PHE PHE B . n 
A 1 64  PRO 64  279 279 PRO PRO B . n 
A 1 65  GLU 65  280 280 GLU GLU B . n 
A 1 66  LYS 66  281 281 LYS LYS B . n 
A 1 67  LYS 67  282 282 LYS LYS B . n 
A 1 68  GLY 68  283 283 GLY GLY B . n 
A 1 69  GLY 69  284 284 GLY GLY B . n 
A 1 70  LEU 70  285 285 LEU LEU B . n 
A 1 71  ARG 71  286 286 ARG ARG B . n 
A 1 72  GLU 72  287 287 GLU GLU B . n 
A 1 73  LEU 73  288 288 LEU LEU B . n 
A 1 74  TYR 74  289 289 TYR TYR B . n 
A 1 75  ASP 75  290 290 ASP ASP B . n 
A 1 76  ARG 76  291 291 ARG ARG B . n 
A 1 77  GLY 77  292 292 GLY GLY B . n 
A 1 78  PRO 78  293 293 PRO PRO B . n 
A 1 79  PRO 79  294 294 PRO PRO B . n 
A 1 80  HIS 80  295 295 HIS HIS B . n 
A 1 81  ALA 81  296 296 ALA ALA B . n 
A 1 82  PHE 82  297 297 PHE PHE B . n 
A 1 83  PHE 83  298 298 PHE PHE B . n 
A 1 84  LEU 84  299 299 LEU LEU B . n 
A 1 85  VAL 85  300 300 VAL VAL B . n 
A 1 86  LYS 86  301 301 LYS LYS B . n 
A 1 87  PHE 87  302 302 PHE PHE B . n 
A 1 88  TRP 88  303 303 TRP TRP B . n 
A 1 89  ALA 89  304 304 ALA ALA B . n 
A 1 90  ASP 90  305 305 ASP ASP B . n 
A 1 91  LEU 91  306 306 LEU LEU B . n 
A 1 92  ASN 92  307 307 ASN ASN B . n 
A 1 93  TRP 93  308 308 TRP TRP B . n 
A 1 94  GLY 94  309 ?   ?   ?   B . n 
A 1 95  PRO 95  310 ?   ?   ?   B . n 
A 1 96  SER 96  311 ?   ?   ?   B . n 
A 1 97  GLY 97  312 ?   ?   ?   B . n 
A 1 98  GLU 98  313 ?   ?   ?   B . n 
A 1 99  GLU 99  314 ?   ?   ?   B . n 
A 1 100 ALA 100 315 ?   ?   ?   B . n 
A 1 101 GLY 101 316 ?   ?   ?   B . n 
A 1 102 ALA 102 317 ?   ?   ?   B . n 
A 1 103 GLY 103 318 ?   ?   ?   B . n 
A 1 104 GLY 104 319 ?   ?   ?   B . n 
A 1 105 SER 105 320 ?   ?   ?   B . n 
A 1 106 ILE 106 321 ?   ?   ?   B . n 
A 1 107 SER 107 322 ?   ?   ?   B . n 
A 1 108 SER 108 323 323 SER SER B . n 
A 1 109 GLY 109 324 324 GLY GLY B . n 
A 1 110 GLY 110 325 325 GLY GLY B . n 
A 1 111 PHE 111 326 326 PHE PHE B . n 
A 1 112 TYR 112 327 327 TYR TYR B . n 
A 1 113 GLY 113 328 328 GLY GLY B . n 
A 1 114 VAL 114 329 329 VAL VAL B . n 
A 1 115 SER 115 330 330 SER SER B . n 
A 1 116 SER 116 331 331 SER SER B . n 
A 1 117 GLN 117 332 332 GLN GLN B . n 
A 1 118 TYR 118 333 333 TYR TYR B . n 
A 1 119 GLU 119 334 334 GLU GLU B . n 
A 1 120 SER 120 335 335 SER SER B . n 
A 1 121 LEU 121 336 336 LEU LEU B . n 
A 1 122 GLU 122 337 337 GLU GLU B . n 
A 1 123 HIS 123 338 338 HIS HIS B . n 
A 1 124 MET 124 339 339 MET MET B . n 
A 1 125 THR 125 340 340 THR THR B . n 
A 1 126 LEU 126 341 341 LEU LEU B . n 
A 1 127 THR 127 342 342 THR THR B . n 
A 1 128 CYS 128 343 343 CYS CYS B . n 
A 1 129 SER 129 344 344 SER SER B . n 
A 1 130 SER 130 345 345 SER SER B . n 
A 1 131 LYS 131 346 346 LYS LYS B . n 
A 1 132 VAL 132 347 347 VAL VAL B . n 
A 1 133 CYS 133 348 348 CYS CYS B . n 
A 1 134 SER 134 349 349 SER SER B . n 
A 1 135 PHE 135 350 350 PHE PHE B . n 
A 1 136 GLY 136 351 351 GLY GLY B . n 
A 1 137 LYS 137 352 352 LYS LYS B . n 
A 1 138 GLN 138 353 353 GLN GLN B . n 
A 1 139 VAL 139 354 354 VAL VAL B . n 
A 1 140 VAL 140 355 355 VAL VAL B . n 
A 1 141 GLU 141 356 356 GLU GLU B . n 
A 1 142 LYS 142 357 357 LYS LYS B . n 
A 1 143 VAL 143 358 358 VAL VAL B . n 
A 1 144 GLU 144 359 359 GLU GLU B . n 
A 1 145 THR 145 360 360 THR THR B . n 
A 1 146 GLU 146 361 361 GLU GLU B . n 
A 1 147 ARG 147 362 362 ARG ARG B . n 
A 1 148 ALA 148 363 363 ALA ALA B . n 
A 1 149 GLN 149 364 364 GLN GLN B . n 
A 1 150 LEU 150 365 365 LEU LEU B . n 
A 1 151 GLU 151 366 366 GLU GLU B . n 
A 1 152 ASP 152 367 367 ASP ASP B . n 
A 1 153 GLY 153 368 368 GLY GLY B . n 
A 1 154 ARG 154 369 369 ARG ARG B . n 
A 1 155 PHE 155 370 370 PHE PHE B . n 
A 1 156 VAL 156 371 371 VAL VAL B . n 
A 1 157 TYR 157 372 372 TYR TYR B . n 
A 1 158 ARG 158 373 373 ARG ARG B . n 
A 1 159 LEU 159 374 374 LEU LEU B . n 
A 1 160 LEU 160 375 375 LEU LEU B . n 
A 1 161 ARG 161 376 376 ARG ARG B . n 
A 1 162 SER 162 377 377 SER SER B . n 
A 1 163 PRO 163 378 378 PRO PRO B . n 
A 1 164 MET 164 379 379 MET MET B . n 
A 1 165 CYS 165 380 380 CYS CYS B . n 
A 1 166 GLU 166 381 381 GLU GLU B . n 
A 1 167 TYR 167 382 382 TYR TYR B . n 
A 1 168 LEU 168 383 383 LEU LEU B . n 
A 1 169 VAL 169 384 384 VAL VAL B . n 
A 1 170 ASN 170 385 385 ASN ASN B . n 
A 1 171 PHE 171 386 386 PHE PHE B . n 
A 1 172 LEU 172 387 387 LEU LEU B . n 
A 1 173 HIS 173 388 388 HIS HIS B . n 
A 1 174 LYS 174 389 389 LYS LYS B . n 
A 1 175 LEU 175 390 390 LEU LEU B . n 
A 1 176 ARG 176 391 391 ARG ARG B . n 
A 1 177 GLN 177 392 392 GLN GLN B . n 
A 1 178 LEU 178 393 393 LEU LEU B . n 
A 1 179 PRO 179 394 394 PRO PRO B . n 
A 1 180 GLU 180 395 395 GLU GLU B . n 
A 1 181 ARG 181 396 396 ARG ARG B . n 
A 1 182 TYR 182 397 397 TYR TYR B . n 
A 1 183 MET 183 398 398 MET MET B . n 
A 1 184 MET 184 399 399 MET MET B . n 
A 1 185 ASN 185 400 400 ASN ASN B . n 
A 1 186 SER 186 401 401 SER SER B . n 
A 1 187 VAL 187 402 402 VAL VAL B . n 
A 1 188 LEU 188 403 403 LEU LEU B . n 
A 1 189 GLU 189 404 404 GLU GLU B . n 
A 1 190 ASN 190 405 405 ASN ASN B . n 
A 1 191 PHE 191 406 406 PHE PHE B . n 
A 1 192 THR 192 407 407 THR THR B . n 
A 1 193 ILE 193 408 408 ILE ILE B . n 
A 1 194 LEU 194 409 409 LEU LEU B . n 
A 1 195 GLN 195 410 410 GLN GLN B . n 
A 1 196 VAL 196 411 411 VAL VAL B . n 
A 1 197 VAL 197 412 412 VAL VAL B . n 
A 1 198 THR 198 413 413 THR THR B . n 
A 1 199 ASN 199 414 414 ASN ASN B . n 
A 1 200 ARG 200 415 415 ARG ARG B . n 
A 1 201 ASP 201 416 416 ASP ASP B . n 
A 1 202 THR 202 417 417 THR THR B . n 
A 1 203 GLN 203 418 418 GLN GLN B . n 
A 1 204 GLU 204 419 419 GLU GLU B . n 
A 1 205 LEU 205 420 420 LEU LEU B . n 
A 1 206 LEU 206 421 421 LEU LEU B . n 
A 1 207 LEU 207 422 422 LEU LEU B . n 
A 1 208 CYS 208 423 423 CYS CYS B . n 
A 1 209 THR 209 424 424 THR THR B . n 
A 1 210 ALA 210 425 425 ALA ALA B . n 
A 1 211 TYR 211 426 426 TYR TYR B . n 
A 1 212 VAL 212 427 427 VAL VAL B . n 
A 1 213 PHE 213 428 428 PHE PHE B . n 
A 1 214 GLU 214 429 429 GLU GLU B . n 
A 1 215 VAL 215 430 430 VAL VAL B . n 
A 1 216 SER 216 431 431 SER SER B . n 
A 1 217 THR 217 432 432 THR THR B . n 
A 1 218 SER 218 433 433 SER SER B . n 
A 1 219 GLU 219 434 434 GLU GLU B . n 
A 1 220 ARG 220 435 435 ARG ARG B . n 
A 1 221 GLY 221 436 436 GLY GLY B . n 
A 1 222 ALA 222 437 437 ALA ALA B . n 
A 1 223 GLN 223 438 438 GLN GLN B . n 
A 1 224 HIS 224 439 439 HIS HIS B . n 
A 1 225 HIS 225 440 440 HIS HIS B . n 
A 1 226 ILE 226 441 441 ILE ILE B . n 
A 1 227 TYR 227 442 442 TYR TYR B . n 
A 1 228 ARG 228 443 443 ARG ARG B . n 
A 1 229 LEU 229 444 444 LEU LEU B . n 
A 1 230 VAL 230 445 445 VAL VAL B . n 
A 1 231 ARG 231 446 446 ARG ARG B . n 
A 1 232 ASP 232 447 ?   ?   ?   B . n 
A 1 233 VAL 233 448 ?   ?   ?   B . n 
A 1 234 GLU 234 449 ?   ?   ?   B . n 
A 1 235 HIS 235 450 ?   ?   ?   B . n 
A 1 236 HIS 236 451 ?   ?   ?   B . n 
A 1 237 HIS 237 452 ?   ?   ?   B . n 
A 1 238 HIS 238 453 ?   ?   ?   B . n 
A 1 239 HIS 239 454 ?   ?   ?   B . n 
A 1 240 HIS 240 455 ?   ?   ?   B . n 
B 1 1   MET 1   216 ?   ?   ?   A . n 
B 1 2   ALA 2   217 ?   ?   ?   A . n 
B 1 3   TRP 3   218 ?   ?   ?   A . n 
B 1 4   GLN 4   219 ?   ?   ?   A . n 
B 1 5   ALA 5   220 ?   ?   ?   A . n 
B 1 6   ARG 6   221 ?   ?   ?   A . n 
B 1 7   GLY 7   222 222 GLY GLY A . n 
B 1 8   LEU 8   223 223 LEU LEU A . n 
B 1 9   GLY 9   224 224 GLY GLY A . n 
B 1 10  THR 10  225 225 THR THR A . n 
B 1 11  ALA 11  226 226 ALA ALA A . n 
B 1 12  ARG 12  227 227 ARG ARG A . n 
B 1 13  LEU 13  228 228 LEU LEU A . n 
B 1 14  GLN 14  229 229 GLN GLN A . n 
B 1 15  LEU 15  230 230 LEU LEU A . n 
B 1 16  VAL 16  231 231 VAL VAL A . n 
B 1 17  GLU 17  232 232 GLU GLU A . n 
B 1 18  PHE 18  233 233 PHE PHE A . n 
B 1 19  SER 19  234 234 SER SER A . n 
B 1 20  ALA 20  235 235 ALA ALA A . n 
B 1 21  PHE 21  236 236 PHE PHE A . n 
B 1 22  VAL 22  237 237 VAL VAL A . n 
B 1 23  GLU 23  238 238 GLU GLU A . n 
B 1 24  PRO 24  239 239 PRO PRO A . n 
B 1 25  PRO 25  240 240 PRO PRO A . n 
B 1 26  ASP 26  241 ?   ?   ?   A . n 
B 1 27  ALA 27  242 ?   ?   ?   A . n 
B 1 28  VAL 28  243 ?   ?   ?   A . n 
B 1 29  ASP 29  244 ?   ?   ?   A . n 
B 1 30  SER 30  245 ?   ?   ?   A . n 
B 1 31  TYR 31  246 ?   ?   ?   A . n 
B 1 32  GLN 32  247 ?   ?   ?   A . n 
B 1 33  ARG 33  248 248 ARG ARG A . n 
B 1 34  HIS 34  249 249 HIS HIS A . n 
B 1 35  LEU 35  250 250 LEU LEU A . n 
B 1 36  PHE 36  251 251 PHE PHE A . n 
B 1 37  VAL 37  252 252 VAL VAL A . n 
B 1 38  HIS 38  253 253 HIS HIS A . n 
B 1 39  ILE 39  254 254 ILE ILE A . n 
B 1 40  SER 40  255 255 SER SER A . n 
B 1 41  GLN 41  256 256 GLN GLN A . n 
B 1 42  HIS 42  257 257 HIS HIS A . n 
B 1 43  CYS 43  258 ?   ?   ?   A . n 
B 1 44  PRO 44  259 ?   ?   ?   A . n 
B 1 45  SER 45  260 ?   ?   ?   A . n 
B 1 46  PRO 46  261 ?   ?   ?   A . n 
B 1 47  GLY 47  262 ?   ?   ?   A . n 
B 1 48  ALA 48  263 ?   ?   ?   A . n 
B 1 49  PRO 49  264 264 PRO PRO A . n 
B 1 50  PRO 50  265 265 PRO PRO A . n 
B 1 51  LEU 51  266 266 LEU LEU A . n 
B 1 52  GLU 52  267 267 GLU GLU A . n 
B 1 53  SER 53  268 268 SER SER A . n 
B 1 54  VAL 54  269 269 VAL VAL A . n 
B 1 55  ASP 55  270 270 ASP ASP A . n 
B 1 56  VAL 56  271 271 VAL VAL A . n 
B 1 57  ARG 57  272 272 ARG ARG A . n 
B 1 58  GLN 58  273 273 GLN GLN A . n 
B 1 59  ILE 59  274 274 ILE ILE A . n 
B 1 60  TYR 60  275 275 TYR TYR A . n 
B 1 61  ASP 61  276 276 ASP ASP A . n 
B 1 62  LYS 62  277 277 LYS LYS A . n 
B 1 63  PHE 63  278 278 PHE PHE A . n 
B 1 64  PRO 64  279 279 PRO PRO A . n 
B 1 65  GLU 65  280 280 GLU GLU A . n 
B 1 66  LYS 66  281 281 LYS LYS A . n 
B 1 67  LYS 67  282 282 LYS LYS A . n 
B 1 68  GLY 68  283 283 GLY GLY A . n 
B 1 69  GLY 69  284 284 GLY GLY A . n 
B 1 70  LEU 70  285 285 LEU LEU A . n 
B 1 71  ARG 71  286 286 ARG ARG A . n 
B 1 72  GLU 72  287 287 GLU GLU A . n 
B 1 73  LEU 73  288 288 LEU LEU A . n 
B 1 74  TYR 74  289 289 TYR TYR A . n 
B 1 75  ASP 75  290 290 ASP ASP A . n 
B 1 76  ARG 76  291 291 ARG ARG A . n 
B 1 77  GLY 77  292 292 GLY GLY A . n 
B 1 78  PRO 78  293 293 PRO PRO A . n 
B 1 79  PRO 79  294 294 PRO PRO A . n 
B 1 80  HIS 80  295 295 HIS HIS A . n 
B 1 81  ALA 81  296 296 ALA ALA A . n 
B 1 82  PHE 82  297 297 PHE PHE A . n 
B 1 83  PHE 83  298 298 PHE PHE A . n 
B 1 84  LEU 84  299 299 LEU LEU A . n 
B 1 85  VAL 85  300 300 VAL VAL A . n 
B 1 86  LYS 86  301 301 LYS LYS A . n 
B 1 87  PHE 87  302 302 PHE PHE A . n 
B 1 88  TRP 88  303 303 TRP TRP A . n 
B 1 89  ALA 89  304 304 ALA ALA A . n 
B 1 90  ASP 90  305 305 ASP ASP A . n 
B 1 91  LEU 91  306 306 LEU LEU A . n 
B 1 92  ASN 92  307 307 ASN ASN A . n 
B 1 93  TRP 93  308 308 TRP TRP A . n 
B 1 94  GLY 94  309 ?   ?   ?   A . n 
B 1 95  PRO 95  310 ?   ?   ?   A . n 
B 1 96  SER 96  311 ?   ?   ?   A . n 
B 1 97  GLY 97  312 ?   ?   ?   A . n 
B 1 98  GLU 98  313 ?   ?   ?   A . n 
B 1 99  GLU 99  314 ?   ?   ?   A . n 
B 1 100 ALA 100 315 ?   ?   ?   A . n 
B 1 101 GLY 101 316 ?   ?   ?   A . n 
B 1 102 ALA 102 317 ?   ?   ?   A . n 
B 1 103 GLY 103 318 ?   ?   ?   A . n 
B 1 104 GLY 104 319 ?   ?   ?   A . n 
B 1 105 SER 105 320 ?   ?   ?   A . n 
B 1 106 ILE 106 321 ?   ?   ?   A . n 
B 1 107 SER 107 322 ?   ?   ?   A . n 
B 1 108 SER 108 323 323 SER ALA A . n 
B 1 109 GLY 109 324 324 GLY GLY A . n 
B 1 110 GLY 110 325 325 GLY GLY A . n 
B 1 111 PHE 111 326 326 PHE PHE A . n 
B 1 112 TYR 112 327 327 TYR TYR A . n 
B 1 113 GLY 113 328 328 GLY GLY A . n 
B 1 114 VAL 114 329 329 VAL VAL A . n 
B 1 115 SER 115 330 330 SER SER A . n 
B 1 116 SER 116 331 331 SER SER A . n 
B 1 117 GLN 117 332 332 GLN GLN A . n 
B 1 118 TYR 118 333 333 TYR TYR A . n 
B 1 119 GLU 119 334 334 GLU GLU A . n 
B 1 120 SER 120 335 335 SER SER A . n 
B 1 121 LEU 121 336 336 LEU LEU A . n 
B 1 122 GLU 122 337 337 GLU GLU A . n 
B 1 123 HIS 123 338 338 HIS HIS A . n 
B 1 124 MET 124 339 339 MET MET A . n 
B 1 125 THR 125 340 340 THR THR A . n 
B 1 126 LEU 126 341 341 LEU LEU A . n 
B 1 127 THR 127 342 342 THR THR A . n 
B 1 128 CYS 128 343 343 CYS CYS A . n 
B 1 129 SER 129 344 344 SER SER A . n 
B 1 130 SER 130 345 345 SER SER A . n 
B 1 131 LYS 131 346 346 LYS LYS A . n 
B 1 132 VAL 132 347 347 VAL VAL A . n 
B 1 133 CYS 133 348 348 CYS CYS A . n 
B 1 134 SER 134 349 349 SER SER A . n 
B 1 135 PHE 135 350 350 PHE PHE A . n 
B 1 136 GLY 136 351 351 GLY GLY A . n 
B 1 137 LYS 137 352 352 LYS LYS A . n 
B 1 138 GLN 138 353 353 GLN GLN A . n 
B 1 139 VAL 139 354 354 VAL VAL A . n 
B 1 140 VAL 140 355 355 VAL VAL A . n 
B 1 141 GLU 141 356 356 GLU GLU A . n 
B 1 142 LYS 142 357 357 LYS LYS A . n 
B 1 143 VAL 143 358 358 VAL VAL A . n 
B 1 144 GLU 144 359 359 GLU GLU A . n 
B 1 145 THR 145 360 360 THR THR A . n 
B 1 146 GLU 146 361 361 GLU GLU A . n 
B 1 147 ARG 147 362 362 ARG ARG A . n 
B 1 148 ALA 148 363 363 ALA ALA A . n 
B 1 149 GLN 149 364 364 GLN GLN A . n 
B 1 150 LEU 150 365 365 LEU LEU A . n 
B 1 151 GLU 151 366 366 GLU GLU A . n 
B 1 152 ASP 152 367 367 ASP ASP A . n 
B 1 153 GLY 153 368 368 GLY GLY A . n 
B 1 154 ARG 154 369 369 ARG ARG A . n 
B 1 155 PHE 155 370 370 PHE PHE A . n 
B 1 156 VAL 156 371 371 VAL VAL A . n 
B 1 157 TYR 157 372 372 TYR TYR A . n 
B 1 158 ARG 158 373 373 ARG ARG A . n 
B 1 159 LEU 159 374 374 LEU LEU A . n 
B 1 160 LEU 160 375 375 LEU LEU A . n 
B 1 161 ARG 161 376 376 ARG ARG A . n 
B 1 162 SER 162 377 377 SER SER A . n 
B 1 163 PRO 163 378 378 PRO PRO A . n 
B 1 164 MET 164 379 379 MET MET A . n 
B 1 165 CYS 165 380 380 CYS CYS A . n 
B 1 166 GLU 166 381 381 GLU GLU A . n 
B 1 167 TYR 167 382 382 TYR TYR A . n 
B 1 168 LEU 168 383 383 LEU LEU A . n 
B 1 169 VAL 169 384 384 VAL VAL A . n 
B 1 170 ASN 170 385 385 ASN ASN A . n 
B 1 171 PHE 171 386 386 PHE PHE A . n 
B 1 172 LEU 172 387 387 LEU LEU A . n 
B 1 173 HIS 173 388 388 HIS HIS A . n 
B 1 174 LYS 174 389 389 LYS LYS A . n 
B 1 175 LEU 175 390 390 LEU LEU A . n 
B 1 176 ARG 176 391 391 ARG ARG A . n 
B 1 177 GLN 177 392 392 GLN GLN A . n 
B 1 178 LEU 178 393 393 LEU LEU A . n 
B 1 179 PRO 179 394 394 PRO PRO A . n 
B 1 180 GLU 180 395 395 GLU GLU A . n 
B 1 181 ARG 181 396 396 ARG ARG A . n 
B 1 182 TYR 182 397 397 TYR TYR A . n 
B 1 183 MET 183 398 398 MET MET A . n 
B 1 184 MET 184 399 399 MET MET A . n 
B 1 185 ASN 185 400 400 ASN ASN A . n 
B 1 186 SER 186 401 401 SER SER A . n 
B 1 187 VAL 187 402 402 VAL VAL A . n 
B 1 188 LEU 188 403 403 LEU LEU A . n 
B 1 189 GLU 189 404 404 GLU GLU A . n 
B 1 190 ASN 190 405 405 ASN ASN A . n 
B 1 191 PHE 191 406 406 PHE PHE A . n 
B 1 192 THR 192 407 407 THR THR A . n 
B 1 193 ILE 193 408 408 ILE ILE A . n 
B 1 194 LEU 194 409 409 LEU LEU A . n 
B 1 195 GLN 195 410 410 GLN GLN A . n 
B 1 196 VAL 196 411 411 VAL VAL A . n 
B 1 197 VAL 197 412 412 VAL VAL A . n 
B 1 198 THR 198 413 413 THR THR A . n 
B 1 199 ASN 199 414 414 ASN ASN A . n 
B 1 200 ARG 200 415 415 ARG ARG A . n 
B 1 201 ASP 201 416 416 ASP ASP A . n 
B 1 202 THR 202 417 417 THR THR A . n 
B 1 203 GLN 203 418 418 GLN GLN A . n 
B 1 204 GLU 204 419 419 GLU GLU A . n 
B 1 205 LEU 205 420 420 LEU LEU A . n 
B 1 206 LEU 206 421 421 LEU LEU A . n 
B 1 207 LEU 207 422 422 LEU LEU A . n 
B 1 208 CYS 208 423 423 CYS CYS A . n 
B 1 209 THR 209 424 424 THR THR A . n 
B 1 210 ALA 210 425 425 ALA ALA A . n 
B 1 211 TYR 211 426 426 TYR TYR A . n 
B 1 212 VAL 212 427 427 VAL VAL A . n 
B 1 213 PHE 213 428 428 PHE PHE A . n 
B 1 214 GLU 214 429 429 GLU GLU A . n 
B 1 215 VAL 215 430 430 VAL VAL A . n 
B 1 216 SER 216 431 431 SER SER A . n 
B 1 217 THR 217 432 432 THR THR A . n 
B 1 218 SER 218 433 433 SER SER A . n 
B 1 219 GLU 219 434 434 GLU GLU A . n 
B 1 220 ARG 220 435 435 ARG ARG A . n 
B 1 221 GLY 221 436 436 GLY GLY A . n 
B 1 222 ALA 222 437 437 ALA ALA A . n 
B 1 223 GLN 223 438 438 GLN GLN A . n 
B 1 224 HIS 224 439 439 HIS HIS A . n 
B 1 225 HIS 225 440 440 HIS HIS A . n 
B 1 226 ILE 226 441 441 ILE ILE A . n 
B 1 227 TYR 227 442 442 TYR TYR A . n 
B 1 228 ARG 228 443 443 ARG ARG A . n 
B 1 229 LEU 229 444 444 LEU LEU A . n 
B 1 230 VAL 230 445 445 VAL VAL A . n 
B 1 231 ARG 231 446 446 ARG ARG A . n 
B 1 232 ASP 232 447 ?   ?   ?   A . n 
B 1 233 VAL 233 448 ?   ?   ?   A . n 
B 1 234 GLU 234 449 ?   ?   ?   A . n 
B 1 235 HIS 235 450 ?   ?   ?   A . n 
B 1 236 HIS 236 451 ?   ?   ?   A . n 
B 1 237 HIS 237 452 ?   ?   ?   A . n 
B 1 238 HIS 238 453 ?   ?   ?   A . n 
B 1 239 HIS 239 454 ?   ?   ?   A . n 
B 1 240 HIS 240 455 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H3Y 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H3Y 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1H3Y 1 501 501 A1H3Y FT1 B . 
D 2 A1H3Y 1 501 501 A1H3Y FT1 A . 
E 3 HOH   1 601 8   HOH   HOH B . 
E 3 HOH   2 602 5   HOH   HOH B . 
E 3 HOH   3 603 4   HOH   HOH B . 
E 3 HOH   4 604 7   HOH   HOH B . 
F 3 HOH   1 601 9   HOH   HOH A . 
F 3 HOH   2 602 10  HOH   HOH A . 
F 3 HOH   3 603 6   HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 B LYS 281 ? CG ? A LYS 66  CG 
2  1 Y 1 B LYS 281 ? CD ? A LYS 66  CD 
3  1 Y 1 B LYS 281 ? CE ? A LYS 66  CE 
4  1 Y 1 B LYS 281 ? NZ ? A LYS 66  NZ 
5  1 Y 1 B LYS 282 ? CG ? A LYS 67  CG 
6  1 Y 1 B LYS 282 ? CD ? A LYS 67  CD 
7  1 Y 1 B LYS 282 ? CE ? A LYS 67  CE 
8  1 Y 1 B LYS 282 ? NZ ? A LYS 67  NZ 
9  1 Y 1 A LYS 281 ? CG ? B LYS 66  CG 
10 1 Y 1 A LYS 281 ? CD ? B LYS 66  CD 
11 1 Y 1 A LYS 281 ? CE ? B LYS 66  CE 
12 1 Y 1 A LYS 281 ? NZ ? B LYS 66  NZ 
13 1 Y 1 A LYS 282 ? CD ? B LYS 67  CD 
14 1 Y 1 A LYS 282 ? CE ? B LYS 67  CE 
15 1 Y 1 A LYS 282 ? NZ ? B LYS 67  NZ 
16 1 Y 1 A SER 323 ? OG ? B SER 108 OG 
# 
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'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   111.60 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RXP 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     113.754 
_cell.length_a_esd                 ? 
_cell.length_b                     61.320 
_cell.length_b_esd                 ? 
_cell.length_c                     80.055 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8RXP 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8RXP 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.75 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.24 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '2.8M sodium formate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-07-15 
_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   0.9697 
_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 BM30A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9697 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BM30A 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8RXP 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.49 
_reflns.d_resolution_low                               47.55 
_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                                     18061 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.95 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.15 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.945 
_reflns.pdbx_CC_star                                   0.986 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.49 
_reflns_shell.d_res_low                                     2.58 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1823 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.454 
_reflns_shell.pdbx_CC_star                                  0.790 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8RXP 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.49 
_refine.ls_d_res_low                             47.55 
_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                     17837 
_refine.ls_number_reflns_R_free                  889 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.93 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2173 
_refine.ls_R_factor_R_free                       0.2740 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2143 
_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                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 33.43 
_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                            0.31 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.49 
_refine_hist.d_res_low                        47.55 
_refine_hist.number_atoms_solvent             7 
_refine_hist.number_atoms_total               3360 
_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        3313 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_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' ? 0.010 ? 3446 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.147 ? 4657 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 9.743 ? 460  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054 ? 497  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010 ? 595  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.49 2.64  . . 147 2826 99.00 . . . . 0.3040 . . . . . . . . . . . 0.3659 
'X-RAY DIFFRACTION' 2.64 2.85  . . 146 2822 98.00 . . . . 0.3044 . . . . . . . . . . . 0.3867 
'X-RAY DIFFRACTION' 2.85 3.13  . . 150 2840 99.00 . . . . 0.2667 . . . . . . . . . . . 0.3209 
'X-RAY DIFFRACTION' 3.13 3.59  . . 148 2802 97.00 . . . . 0.2331 . . . . . . . . . . . 0.2704 
'X-RAY DIFFRACTION' 3.59 4.52  . . 147 2798 97.00 . . . . 0.1833 . . . . . . . . . . . 0.2598 
'X-RAY DIFFRACTION' 4.52 47.55 . . 151 2860 97.00 . . . . 0.1862 . . . . . . . . . . . 0.2376 
# 
_struct.entry_id                     8RXP 
_struct.title                        'TEAD2 with an inhibitor' 
_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        8RXP 
_struct_keywords.text            'inhibitor, complex, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    TEAD2_HUMAN 
_struct_ref.pdbx_db_accession          Q15562 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AWQARGLGTARLQLVEFSAFVEPPDAVDSYQRHLFVHISQHCPSPGAPPLESVDVRQIYDKFPEKKGGLRELYDRGPPHA
FFLVKFWADLNWGPSGEEAGAGGSISSGGFYGVSSQYESLEHMTLTCSSKVCSFGKQVVEKVETERAQLEDGRFVYRLLR
SPMCEYLVNFLHKLRQLPERYMMNSVLENFTILQVVTNRDTQELLLCTAYVFEVSTSERGAQHHIYRLVRD
;
_struct_ref.pdbx_align_begin           0 
# 
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 8RXP B 2 ? 232 ? Q15562 217 ? 447 ? 217 447 
2 1 8RXP A 2 ? 232 ? Q15562 217 ? 447 ? 217 447 
# 
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 8RXP MET B 1   ? UNP Q15562 ? ? 'initiating methionine' 216 1  
1 8RXP VAL B 233 ? UNP Q15562 ? ? 'expression tag'        448 2  
1 8RXP GLU B 234 ? UNP Q15562 ? ? 'expression tag'        449 3  
1 8RXP HIS B 235 ? UNP Q15562 ? ? 'expression tag'        450 4  
1 8RXP HIS B 236 ? UNP Q15562 ? ? 'expression tag'        451 5  
1 8RXP HIS B 237 ? UNP Q15562 ? ? 'expression tag'        452 6  
1 8RXP HIS B 238 ? UNP Q15562 ? ? 'expression tag'        453 7  
1 8RXP HIS B 239 ? UNP Q15562 ? ? 'expression tag'        454 8  
1 8RXP HIS B 240 ? UNP Q15562 ? ? 'expression tag'        455 9  
2 8RXP MET A 1   ? UNP Q15562 ? ? 'initiating methionine' 216 10 
2 8RXP VAL A 233 ? UNP Q15562 ? ? 'expression tag'        448 11 
2 8RXP GLU A 234 ? UNP Q15562 ? ? 'expression tag'        449 12 
2 8RXP HIS A 235 ? UNP Q15562 ? ? 'expression tag'        450 13 
2 8RXP HIS A 236 ? UNP Q15562 ? ? 'expression tag'        451 14 
2 8RXP HIS A 237 ? UNP Q15562 ? ? 'expression tag'        452 15 
2 8RXP HIS A 238 ? UNP Q15562 ? ? 'expression tag'        453 16 
2 8RXP HIS A 239 ? UNP Q15562 ? ? 'expression tag'        454 17 
2 8RXP HIS A 240 ? UNP Q15562 ? ? 'expression tag'        455 18 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E 
2 1 B,D,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 24  ? ASP A 29  ? PRO B 239 ASP B 244 5 ? 6  
HELX_P HELX_P2  AA2 ARG A 57  ? PHE A 63  ? ARG B 272 PHE B 278 5 ? 7  
HELX_P HELX_P3  AA3 GLY A 69  ? GLY A 77  ? GLY B 284 GLY B 292 1 ? 9  
HELX_P HELX_P4  AA4 PRO A 78  ? HIS A 80  ? PRO B 293 HIS B 295 5 ? 3  
HELX_P HELX_P5  AA5 CYS A 165 ? LEU A 178 ? CYS B 380 LEU B 393 1 ? 14 
HELX_P HELX_P6  AA6 GLU A 180 ? GLU A 189 ? GLU B 395 GLU B 404 1 ? 10 
HELX_P HELX_P7  AA7 ARG B 57  ? TYR B 60  ? ARG A 272 TYR A 275 5 ? 4  
HELX_P HELX_P8  AA8 GLY B 69  ? GLY B 77  ? GLY A 284 GLY A 292 1 ? 9  
HELX_P HELX_P9  AA9 PRO B 78  ? HIS B 80  ? PRO A 293 HIS A 295 5 ? 3  
HELX_P HELX_P10 AB1 CYS B 165 ? LEU B 178 ? CYS A 380 LEU A 393 1 ? 14 
HELX_P HELX_P11 AB2 GLU B 180 ? GLU B 189 ? GLU A 395 GLU A 404 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 77 A . ? GLY 292 B PRO 78 A ? PRO 293 B 1 -2.34 
2 GLY 77 B . ? GLY 292 A PRO 78 B ? PRO 293 A 1 -1.62 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5  ? 
AA2 ? 14 ? 
AA3 ? 5  ? 
# 
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 
AA2 1  2  ? parallel      
AA2 2  3  ? anti-parallel 
AA2 3  4  ? parallel      
AA2 4  5  ? anti-parallel 
AA2 5  6  ? anti-parallel 
AA2 6  7  ? anti-parallel 
AA2 7  8  ? parallel      
AA2 8  9  ? anti-parallel 
AA2 9  10 ? anti-parallel 
AA2 10 11 ? anti-parallel 
AA2 11 12 ? parallel      
AA2 12 13 ? anti-parallel 
AA2 13 14 ? parallel      
AA3 1  2  ? anti-parallel 
AA3 2  3  ? anti-parallel 
AA3 3  4  ? anti-parallel 
AA3 4  5  ? 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  HIS A 34  ? SER A 40  ? HIS B 249 SER B 255 
AA1 2  GLN A 14  ? GLU A 23  ? GLN B 229 GLU B 238 
AA1 3  PHE A 111 ? SER A 120 ? PHE B 326 SER B 335 
AA1 4  PHE A 155 ? PRO A 163 ? PHE B 370 PRO B 378 
AA1 5  GLN A 149 ? LEU A 150 ? GLN B 364 LEU B 365 
AA2 1  GLU A 52  ? ASP A 55  ? GLU B 267 ASP B 270 
AA2 2  GLN A 223 ? VAL A 230 ? GLN B 438 VAL B 445 
AA2 3  PHE A 82  ? ALA A 89  ? PHE B 297 ALA B 304 
AA2 4  LEU A 205 ? VAL A 215 ? LEU B 420 VAL B 430 
AA2 5  PHE A 191 ? ASN A 199 ? PHE B 406 ASN B 414 
AA2 6  THR A 125 ? SER A 134 ? THR B 340 SER B 349 
AA2 7  GLN A 138 ? ARG A 147 ? GLN B 353 ARG B 362 
AA2 8  LYS B 137 ? ARG B 147 ? LYS A 352 ARG A 362 
AA2 9  THR B 125 ? SER B 134 ? THR A 340 SER A 349 
AA2 10 PHE B 191 ? ASN B 199 ? PHE A 406 ASN A 414 
AA2 11 LEU B 205 ? VAL B 215 ? LEU A 420 VAL A 430 
AA2 12 PHE B 82  ? ALA B 89  ? PHE A 297 ALA A 304 
AA2 13 GLN B 223 ? VAL B 230 ? GLN A 438 VAL A 445 
AA2 14 GLU B 52  ? ASP B 55  ? GLU A 267 ASP A 270 
AA3 1  HIS B 34  ? SER B 40  ? HIS A 249 SER A 255 
AA3 2  GLN B 14  ? GLU B 23  ? GLN A 229 GLU A 238 
AA3 3  PHE B 111 ? SER B 120 ? PHE A 326 SER A 335 
AA3 4  ARG B 154 ? PRO B 163 ? ARG A 369 PRO A 378 
AA3 5  GLN B 149 ? GLU B 151 ? GLN A 364 GLU A 366 
# 
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 ILE A 39  ? O ILE B 254 N PHE A 18  ? N PHE B 233 
AA1 2  3  N GLU A 23  ? N GLU B 238 O PHE A 111 ? O PHE B 326 
AA1 3  4  N SER A 120 ? N SER B 335 O PHE A 155 ? O PHE B 370 
AA1 4  5  O VAL A 156 ? O VAL B 371 N GLN A 149 ? N GLN B 364 
AA2 1  2  N GLU A 52  ? N GLU B 267 O ARG A 228 ? O ARG B 443 
AA2 2  3  O TYR A 227 ? O TYR B 442 N LEU A 84  ? N LEU B 299 
AA2 3  4  N VAL A 85  ? N VAL B 300 O ALA A 210 ? O ALA B 425 
AA2 4  5  O LEU A 207 ? O LEU B 422 N VAL A 197 ? N VAL B 412 
AA2 5  6  O VAL A 196 ? O VAL B 411 N SER A 129 ? N SER B 344 
AA2 6  7  N VAL A 132 ? N VAL B 347 O VAL A 139 ? O VAL B 354 
AA2 7  8  N GLU A 141 ? N GLU B 356 O VAL B 139 ? O VAL A 354 
AA2 8  9  O GLU B 144 ? O GLU A 359 N CYS B 128 ? N CYS A 343 
AA2 9  10 N CYS B 133 ? N CYS A 348 O THR B 192 ? O THR A 407 
AA2 10 11 N VAL B 197 ? N VAL A 412 O LEU B 206 ? O LEU A 421 
AA2 11 12 O ALA B 210 ? O ALA A 425 N VAL B 85  ? N VAL A 300 
AA2 12 13 N LEU B 84  ? N LEU A 299 O TYR B 227 ? O TYR A 442 
AA2 13 14 O ARG B 228 ? O ARG A 443 N VAL B 54  ? N VAL A 269 
AA3 1  2  O ILE B 39  ? O ILE A 254 N PHE B 18  ? N PHE A 233 
AA3 2  3  N VAL B 16  ? N VAL A 231 O GLN B 117 ? O GLN A 332 
AA3 3  4  N SER B 116 ? N SER A 331 O LEU B 159 ? O LEU A 374 
AA3 4  5  O ARG B 154 ? O ARG A 369 N GLU B 151 ? N GLU A 366 
# 
_pdbx_entry_details.entry_id                   8RXP 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP B 244 ? ? -93.44  -71.55  
2  1 GLN B 256 ? ? -114.29 55.19   
3  1 ASP B 276 ? ? -68.09  0.59    
4  1 PRO B 279 ? ? -59.23  171.23  
5  1 LYS B 281 ? ? 56.49   -158.58 
6  1 LYS B 282 ? ? 34.95   30.20   
7  1 LEU B 306 ? ? -99.83  32.17   
8  1 GLU B 366 ? ? -142.83 -127.68 
9  1 LEU B 374 ? ? -118.71 79.68   
10 1 GLN B 418 ? ? 81.68   -6.82   
11 1 THR B 432 ? ? -68.10  99.56   
12 1 SER B 433 ? ? -68.57  16.24   
13 1 GLN A 256 ? ? -120.43 -96.95  
14 1 LYS A 281 ? ? -107.55 59.88   
15 1 LYS A 282 ? ? 61.50   135.89  
16 1 HIS A 295 ? ? -56.68  -6.61   
17 1 GLU A 404 ? ? -56.36  -8.22   
18 1 LEU A 421 ? ? -103.79 -71.78  
19 1 ARG A 435 ? ? 80.23   -11.27  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -27.1466 -15.0009 27.8792 0.4983 ? -0.0159 ? -0.0137 ? 0.6157 ? -0.0315 ? 0.3935 ? 9.3352 ? 
-0.9922 ? 3.7104  ? 2.9907 ? 0.9334  ? 8.8883 ? 0.1842  ? -0.6867 ? 0.0651  ? -0.0414 ? 0.0996 ? -0.3852 ? 0.3778  ? 0.4960  ? 
-0.2254 ? 
2 'X-RAY DIFFRACTION' ? refined -29.9501 -17.0673 19.5881 0.6688 ? 0.0407  ? 0.0250  ? 0.2903 ? -0.0318 ? 0.2573 ? 8.9156 ? 
-0.5413 ? 0.6101  ? 4.0203 ? 1.3564  ? 7.9332 ? -0.2565 ? 0.2092  ? -0.6097 ? 0.1390  ? 0.2401 ? -0.2235 ? 0.3288  ? -0.0730 ? 
-0.1359 ? 
3 'X-RAY DIFFRACTION' ? refined -24.5928 -10.2503 19.4724 0.5782 ? -0.0546 ? 0.0999  ? 0.3407 ? -0.0132 ? 0.3757 ? 5.0330 ? 
-0.6662 ? 2.3079  ? 3.1527 ? 1.4913  ? 8.1201 ? -0.1682 ? 0.0582  ? 0.1761  ? -0.2182 ? 0.3176 ? -0.4838 ? -0.4514 ? 0.7527  ? 
-0.1699 ? 
4 'X-RAY DIFFRACTION' ? refined -26.7849 -2.1779  23.7513 0.6311 ? 0.0516  ? 0.0456  ? 0.4615 ? -0.0292 ? 0.4538 ? 4.0283 ? 0.5741 
? 1.3659  ? 4.0299 ? 2.5576  ? 5.4496 ? 0.0510  ? -0.4397 ? 0.3787  ? -0.4163 ? 0.1058 ? -0.0341 ? -1.7692 ? 0.0187  ? -0.2250 ? 
5 'X-RAY DIFFRACTION' ? refined -32.9727 -8.9989  34.2203 0.4732 ? 0.0738  ? 0.1551  ? 0.8626 ? -0.0930 ? 0.4789 ? 5.2048 ? 
-0.5346 ? 2.3804  ? 3.0334 ? 2.0133  ? 6.6682 ? -0.2364 ? -1.2449 ? -0.1524 ? 0.2873  ? 0.1403 ? -0.1899 ? 0.0416  ? -1.0549 ? 
0.1765  ? 
6 'X-RAY DIFFRACTION' ? refined -28.9729 -10.1359 13.2923 0.4991 ? 0.0514  ? 0.0670  ? 0.2624 ? 0.0575  ? 0.3557 ? 4.6077 ? 1.0332 
? 2.0775  ? 2.8539 ? 2.7863  ? 9.6875 ? -0.1056 ? 0.0609  ? 0.0101  ? -0.5397 ? 0.2574 ? -0.2701 ? -0.5649 ? 0.0749  ? -0.0890 ? 
7 'X-RAY DIFFRACTION' ? refined -23.6820 -22.0555 16.6419 0.4407 ? 0.1961  ? -0.0983 ? 0.3488 ? 0.0692  ? 0.4475 ? 8.1476 ? 3.2085 
? 2.3428  ? 6.2248 ? 2.7657  ? 8.4655 ? 0.0829  ? -0.4865 ? -0.9025 ? -0.0248 ? 0.3549 ? -0.4812 ? 0.5543  ? 0.0445  ? -0.5199 ? 
8 'X-RAY DIFFRACTION' ? refined -38.5600 18.4416  21.2647 0.5359 ? 0.0444  ? 0.0022  ? 0.3446 ? 0.0349  ? 0.3809 ? 8.7648 ? 
-0.3534 ? -1.9826 ? 3.4487 ? -1.1416 ? 5.3805 ? 0.0605  ? 0.3585  ? 0.0232  ? -0.1437 ? 0.2361 ? 0.3531  ? -0.1646 ? -0.2906 ? 
-0.3127 ? 
9 'X-RAY DIFFRACTION' ? refined -32.4838 16.2553  21.5779 0.4835 ? 0.0669  ? -0.0145 ? 0.3009 ? -0.0194 ? 0.3972 ? 3.7253 ? 0.6897 
? -3.1455 ? 1.3868 ? -0.5508 ? 7.9051 ? 0.0899  ? -0.3191 ? 0.1063  ? 0.0370  ? 0.0958 ? 0.0719  ? 0.0147  ? 0.3394  ? -0.1765 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 220 through 238 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 239 through 277 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 278 through 335 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 336 through 362 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 363 through 380 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 381 through 430 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 431 through 446 )
;
8 'X-RAY DIFFRACTION' 8 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 222 through 293 )
;
9 'X-RAY DIFFRACTION' 9 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 294 through 446 )
;
# 
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 B MET 216 ? A MET 1   
2  1 Y 1 B ALA 217 ? A ALA 2   
3  1 Y 1 B TRP 218 ? A TRP 3   
4  1 Y 1 B GLN 219 ? A GLN 4   
5  1 Y 1 B CYS 258 ? A CYS 43  
6  1 Y 1 B PRO 259 ? A PRO 44  
7  1 Y 1 B SER 260 ? A SER 45  
8  1 Y 1 B PRO 261 ? A PRO 46  
9  1 Y 1 B GLY 262 ? A GLY 47  
10 1 Y 1 B ALA 263 ? A ALA 48  
11 1 Y 1 B GLY 309 ? A GLY 94  
12 1 Y 1 B PRO 310 ? A PRO 95  
13 1 Y 1 B SER 311 ? A SER 96  
14 1 Y 1 B GLY 312 ? A GLY 97  
15 1 Y 1 B GLU 313 ? A GLU 98  
16 1 Y 1 B GLU 314 ? A GLU 99  
17 1 Y 1 B ALA 315 ? A ALA 100 
18 1 Y 1 B GLY 316 ? A GLY 101 
19 1 Y 1 B ALA 317 ? A ALA 102 
20 1 Y 1 B GLY 318 ? A GLY 103 
21 1 Y 1 B GLY 319 ? A GLY 104 
22 1 Y 1 B SER 320 ? A SER 105 
23 1 Y 1 B ILE 321 ? A ILE 106 
24 1 Y 1 B SER 322 ? A SER 107 
25 1 Y 1 B ASP 447 ? A ASP 232 
26 1 Y 1 B VAL 448 ? A VAL 233 
27 1 Y 1 B GLU 449 ? A GLU 234 
28 1 Y 1 B HIS 450 ? A HIS 235 
29 1 Y 1 B HIS 451 ? A HIS 236 
30 1 Y 1 B HIS 452 ? A HIS 237 
31 1 Y 1 B HIS 453 ? A HIS 238 
32 1 Y 1 B HIS 454 ? A HIS 239 
33 1 Y 1 B HIS 455 ? A HIS 240 
34 1 Y 1 A MET 216 ? B MET 1   
35 1 Y 1 A ALA 217 ? B ALA 2   
36 1 Y 1 A TRP 218 ? B TRP 3   
37 1 Y 1 A GLN 219 ? B GLN 4   
38 1 Y 1 A ALA 220 ? B ALA 5   
39 1 Y 1 A ARG 221 ? B ARG 6   
40 1 Y 1 A ASP 241 ? B ASP 26  
41 1 Y 1 A ALA 242 ? B ALA 27  
42 1 Y 1 A VAL 243 ? B VAL 28  
43 1 Y 1 A ASP 244 ? B ASP 29  
44 1 Y 1 A SER 245 ? B SER 30  
45 1 Y 1 A TYR 246 ? B TYR 31  
46 1 Y 1 A GLN 247 ? B GLN 32  
47 1 Y 1 A CYS 258 ? B CYS 43  
48 1 Y 1 A PRO 259 ? B PRO 44  
49 1 Y 1 A SER 260 ? B SER 45  
50 1 Y 1 A PRO 261 ? B PRO 46  
51 1 Y 1 A GLY 262 ? B GLY 47  
52 1 Y 1 A ALA 263 ? B ALA 48  
53 1 Y 1 A GLY 309 ? B GLY 94  
54 1 Y 1 A PRO 310 ? B PRO 95  
55 1 Y 1 A SER 311 ? B SER 96  
56 1 Y 1 A GLY 312 ? B GLY 97  
57 1 Y 1 A GLU 313 ? B GLU 98  
58 1 Y 1 A GLU 314 ? B GLU 99  
59 1 Y 1 A ALA 315 ? B ALA 100 
60 1 Y 1 A GLY 316 ? B GLY 101 
61 1 Y 1 A ALA 317 ? B ALA 102 
62 1 Y 1 A GLY 318 ? B GLY 103 
63 1 Y 1 A GLY 319 ? B GLY 104 
64 1 Y 1 A SER 320 ? B SER 105 
65 1 Y 1 A ILE 321 ? B ILE 106 
66 1 Y 1 A SER 322 ? B SER 107 
67 1 Y 1 A ASP 447 ? B ASP 232 
68 1 Y 1 A VAL 448 ? B VAL 233 
69 1 Y 1 A GLU 449 ? B GLU 234 
70 1 Y 1 A HIS 450 ? B HIS 235 
71 1 Y 1 A HIS 451 ? B HIS 236 
72 1 Y 1 A HIS 452 ? B HIS 237 
73 1 Y 1 A HIS 453 ? B HIS 238 
74 1 Y 1 A HIS 454 ? B HIS 239 
75 1 Y 1 A HIS 455 ? B HIS 240 
# 
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 
A1H3Y C10  C Y N 1   
A1H3Y C12  C N N 2   
A1H3Y C13  C Y N 3   
A1H3Y C14  C Y N 4   
A1H3Y C02  C N N 5   
A1H3Y C03  C N N 6   
A1H3Y C04  C Y N 7   
A1H3Y C05  C Y N 8   
A1H3Y C07  C Y N 9   
A1H3Y C08  C Y N 10  
A1H3Y C09  C Y N 11  
A1H3Y C15  C Y N 12  
A1H3Y C16  C Y N 13  
A1H3Y C17  C Y N 14  
A1H3Y C18  C Y N 15  
A1H3Y C19  C Y N 16  
A1H3Y C20  C Y N 17  
A1H3Y N06  N Y N 18  
A1H3Y O01  O N N 19  
A1H3Y O11  O N N 20  
A1H3Y H121 H N N 21  
A1H3Y H122 H N N 22  
A1H3Y H141 H N N 23  
A1H3Y H021 H N N 24  
A1H3Y H022 H N N 25  
A1H3Y H031 H N N 26  
A1H3Y H032 H N N 27  
A1H3Y H051 H N N 28  
A1H3Y H091 H N N 29  
A1H3Y H151 H N N 30  
A1H3Y H161 H N N 31  
A1H3Y H171 H N N 32  
A1H3Y H181 H N N 33  
A1H3Y H191 H N N 34  
A1H3Y H201 H N N 35  
A1H3Y H061 H N N 36  
A1H3Y H011 H N N 37  
ALA   N    N N N 38  
ALA   CA   C N S 39  
ALA   C    C N N 40  
ALA   O    O N N 41  
ALA   CB   C N N 42  
ALA   OXT  O N N 43  
ALA   H    H N N 44  
ALA   H2   H N N 45  
ALA   HA   H N N 46  
ALA   HB1  H N N 47  
ALA   HB2  H N N 48  
ALA   HB3  H N N 49  
ALA   HXT  H N N 50  
ARG   N    N N N 51  
ARG   CA   C N S 52  
ARG   C    C N N 53  
ARG   O    O N N 54  
ARG   CB   C N N 55  
ARG   CG   C N N 56  
ARG   CD   C N N 57  
ARG   NE   N N N 58  
ARG   CZ   C N N 59  
ARG   NH1  N N N 60  
ARG   NH2  N N N 61  
ARG   OXT  O N N 62  
ARG   H    H N N 63  
ARG   H2   H N N 64  
ARG   HA   H N N 65  
ARG   HB2  H N N 66  
ARG   HB3  H N N 67  
ARG   HG2  H N N 68  
ARG   HG3  H N N 69  
ARG   HD2  H N N 70  
ARG   HD3  H N N 71  
ARG   HE   H N N 72  
ARG   HH11 H N N 73  
ARG   HH12 H N N 74  
ARG   HH21 H N N 75  
ARG   HH22 H N N 76  
ARG   HXT  H N N 77  
ASN   N    N N N 78  
ASN   CA   C N S 79  
ASN   C    C N N 80  
ASN   O    O N N 81  
ASN   CB   C N N 82  
ASN   CG   C N N 83  
ASN   OD1  O N N 84  
ASN   ND2  N N N 85  
ASN   OXT  O N N 86  
ASN   H    H N N 87  
ASN   H2   H N N 88  
ASN   HA   H N N 89  
ASN   HB2  H N N 90  
ASN   HB3  H N N 91  
ASN   HD21 H N N 92  
ASN   HD22 H N N 93  
ASN   HXT  H N N 94  
ASP   N    N N N 95  
ASP   CA   C N S 96  
ASP   C    C N N 97  
ASP   O    O N N 98  
ASP   CB   C N N 99  
ASP   CG   C N N 100 
ASP   OD1  O N N 101 
ASP   OD2  O N N 102 
ASP   OXT  O N N 103 
ASP   H    H N N 104 
ASP   H2   H N N 105 
ASP   HA   H N N 106 
ASP   HB2  H N N 107 
ASP   HB3  H N N 108 
ASP   HD2  H N N 109 
ASP   HXT  H N N 110 
CYS   N    N N N 111 
CYS   CA   C N R 112 
CYS   C    C N N 113 
CYS   O    O N N 114 
CYS   CB   C N N 115 
CYS   SG   S N N 116 
CYS   OXT  O N N 117 
CYS   H    H N N 118 
CYS   H2   H N N 119 
CYS   HA   H N N 120 
CYS   HB2  H N N 121 
CYS   HB3  H N N 122 
CYS   HG   H N N 123 
CYS   HXT  H N N 124 
GLN   N    N N N 125 
GLN   CA   C N S 126 
GLN   C    C N N 127 
GLN   O    O N N 128 
GLN   CB   C N N 129 
GLN   CG   C N N 130 
GLN   CD   C N N 131 
GLN   OE1  O N N 132 
GLN   NE2  N N N 133 
GLN   OXT  O N N 134 
GLN   H    H N N 135 
GLN   H2   H N N 136 
GLN   HA   H N N 137 
GLN   HB2  H N N 138 
GLN   HB3  H N N 139 
GLN   HG2  H N N 140 
GLN   HG3  H N N 141 
GLN   HE21 H N N 142 
GLN   HE22 H N N 143 
GLN   HXT  H N N 144 
GLU   N    N N N 145 
GLU   CA   C N S 146 
GLU   C    C N N 147 
GLU   O    O N N 148 
GLU   CB   C N N 149 
GLU   CG   C N N 150 
GLU   CD   C N N 151 
GLU   OE1  O N N 152 
GLU   OE2  O N N 153 
GLU   OXT  O N N 154 
GLU   H    H N N 155 
GLU   H2   H N N 156 
GLU   HA   H N N 157 
GLU   HB2  H N N 158 
GLU   HB3  H N N 159 
GLU   HG2  H N N 160 
GLU   HG3  H N N 161 
GLU   HE2  H N N 162 
GLU   HXT  H N N 163 
GLY   N    N N N 164 
GLY   CA   C N N 165 
GLY   C    C N N 166 
GLY   O    O N N 167 
GLY   OXT  O N N 168 
GLY   H    H N N 169 
GLY   H2   H N N 170 
GLY   HA2  H N N 171 
GLY   HA3  H N N 172 
GLY   HXT  H N N 173 
HIS   N    N N N 174 
HIS   CA   C N S 175 
HIS   C    C N N 176 
HIS   O    O N N 177 
HIS   CB   C N N 178 
HIS   CG   C Y N 179 
HIS   ND1  N Y N 180 
HIS   CD2  C Y N 181 
HIS   CE1  C Y N 182 
HIS   NE2  N Y N 183 
HIS   OXT  O N N 184 
HIS   H    H N N 185 
HIS   H2   H N N 186 
HIS   HA   H N N 187 
HIS   HB2  H N N 188 
HIS   HB3  H N N 189 
HIS   HD1  H N N 190 
HIS   HD2  H N N 191 
HIS   HE1  H N N 192 
HIS   HE2  H N N 193 
HIS   HXT  H N N 194 
HOH   O    O N N 195 
HOH   H1   H N N 196 
HOH   H2   H N N 197 
ILE   N    N N N 198 
ILE   CA   C N S 199 
ILE   C    C N N 200 
ILE   O    O N N 201 
ILE   CB   C N S 202 
ILE   CG1  C N N 203 
ILE   CG2  C N N 204 
ILE   CD1  C N N 205 
ILE   OXT  O N N 206 
ILE   H    H N N 207 
ILE   H2   H N N 208 
ILE   HA   H N N 209 
ILE   HB   H N N 210 
ILE   HG12 H N N 211 
ILE   HG13 H N N 212 
ILE   HG21 H N N 213 
ILE   HG22 H N N 214 
ILE   HG23 H N N 215 
ILE   HD11 H N N 216 
ILE   HD12 H N N 217 
ILE   HD13 H N N 218 
ILE   HXT  H N N 219 
LEU   N    N N N 220 
LEU   CA   C N S 221 
LEU   C    C N N 222 
LEU   O    O N N 223 
LEU   CB   C N N 224 
LEU   CG   C N N 225 
LEU   CD1  C N N 226 
LEU   CD2  C N N 227 
LEU   OXT  O N N 228 
LEU   H    H N N 229 
LEU   H2   H N N 230 
LEU   HA   H N N 231 
LEU   HB2  H N N 232 
LEU   HB3  H N N 233 
LEU   HG   H N N 234 
LEU   HD11 H N N 235 
LEU   HD12 H N N 236 
LEU   HD13 H N N 237 
LEU   HD21 H N N 238 
LEU   HD22 H N N 239 
LEU   HD23 H N N 240 
LEU   HXT  H N N 241 
LYS   N    N N N 242 
LYS   CA   C N S 243 
LYS   C    C N N 244 
LYS   O    O N N 245 
LYS   CB   C N N 246 
LYS   CG   C N N 247 
LYS   CD   C N N 248 
LYS   CE   C N N 249 
LYS   NZ   N N N 250 
LYS   OXT  O N N 251 
LYS   H    H N N 252 
LYS   H2   H N N 253 
LYS   HA   H N N 254 
LYS   HB2  H N N 255 
LYS   HB3  H N N 256 
LYS   HG2  H N N 257 
LYS   HG3  H N N 258 
LYS   HD2  H N N 259 
LYS   HD3  H N N 260 
LYS   HE2  H N N 261 
LYS   HE3  H N N 262 
LYS   HZ1  H N N 263 
LYS   HZ2  H N N 264 
LYS   HZ3  H N N 265 
LYS   HXT  H N N 266 
MET   N    N N N 267 
MET   CA   C N S 268 
MET   C    C N N 269 
MET   O    O N N 270 
MET   CB   C N N 271 
MET   CG   C N N 272 
MET   SD   S N N 273 
MET   CE   C N N 274 
MET   OXT  O N N 275 
MET   H    H N N 276 
MET   H2   H N N 277 
MET   HA   H N N 278 
MET   HB2  H N N 279 
MET   HB3  H N N 280 
MET   HG2  H N N 281 
MET   HG3  H N N 282 
MET   HE1  H N N 283 
MET   HE2  H N N 284 
MET   HE3  H N N 285 
MET   HXT  H N N 286 
PHE   N    N N N 287 
PHE   CA   C N S 288 
PHE   C    C N N 289 
PHE   O    O N N 290 
PHE   CB   C N N 291 
PHE   CG   C Y N 292 
PHE   CD1  C Y N 293 
PHE   CD2  C Y N 294 
PHE   CE1  C Y N 295 
PHE   CE2  C Y N 296 
PHE   CZ   C Y N 297 
PHE   OXT  O N N 298 
PHE   H    H N N 299 
PHE   H2   H N N 300 
PHE   HA   H N N 301 
PHE   HB2  H N N 302 
PHE   HB3  H N N 303 
PHE   HD1  H N N 304 
PHE   HD2  H N N 305 
PHE   HE1  H N N 306 
PHE   HE2  H N N 307 
PHE   HZ   H N N 308 
PHE   HXT  H N N 309 
PRO   N    N N N 310 
PRO   CA   C N S 311 
PRO   C    C N N 312 
PRO   O    O N N 313 
PRO   CB   C N N 314 
PRO   CG   C N N 315 
PRO   CD   C N N 316 
PRO   OXT  O N N 317 
PRO   H    H N N 318 
PRO   HA   H N N 319 
PRO   HB2  H N N 320 
PRO   HB3  H N N 321 
PRO   HG2  H N N 322 
PRO   HG3  H N N 323 
PRO   HD2  H N N 324 
PRO   HD3  H N N 325 
PRO   HXT  H N N 326 
SER   N    N N N 327 
SER   CA   C N S 328 
SER   C    C N N 329 
SER   O    O N N 330 
SER   CB   C N N 331 
SER   OG   O N N 332 
SER   OXT  O N N 333 
SER   H    H N N 334 
SER   H2   H N N 335 
SER   HA   H N N 336 
SER   HB2  H N N 337 
SER   HB3  H N N 338 
SER   HG   H N N 339 
SER   HXT  H N N 340 
THR   N    N N N 341 
THR   CA   C N S 342 
THR   C    C N N 343 
THR   O    O N N 344 
THR   CB   C N R 345 
THR   OG1  O N N 346 
THR   CG2  C N N 347 
THR   OXT  O N N 348 
THR   H    H N N 349 
THR   H2   H N N 350 
THR   HA   H N N 351 
THR   HB   H N N 352 
THR   HG1  H N N 353 
THR   HG21 H N N 354 
THR   HG22 H N N 355 
THR   HG23 H N N 356 
THR   HXT  H N N 357 
TRP   N    N N N 358 
TRP   CA   C N S 359 
TRP   C    C N N 360 
TRP   O    O N N 361 
TRP   CB   C N N 362 
TRP   CG   C Y N 363 
TRP   CD1  C Y N 364 
TRP   CD2  C Y N 365 
TRP   NE1  N Y N 366 
TRP   CE2  C Y N 367 
TRP   CE3  C Y N 368 
TRP   CZ2  C Y N 369 
TRP   CZ3  C Y N 370 
TRP   CH2  C Y N 371 
TRP   OXT  O N N 372 
TRP   H    H N N 373 
TRP   H2   H N N 374 
TRP   HA   H N N 375 
TRP   HB2  H N N 376 
TRP   HB3  H N N 377 
TRP   HD1  H N N 378 
TRP   HE1  H N N 379 
TRP   HE3  H N N 380 
TRP   HZ2  H N N 381 
TRP   HZ3  H N N 382 
TRP   HH2  H N N 383 
TRP   HXT  H N N 384 
TYR   N    N N N 385 
TYR   CA   C N S 386 
TYR   C    C N N 387 
TYR   O    O N N 388 
TYR   CB   C N N 389 
TYR   CG   C Y N 390 
TYR   CD1  C Y N 391 
TYR   CD2  C Y N 392 
TYR   CE1  C Y N 393 
TYR   CE2  C Y N 394 
TYR   CZ   C Y N 395 
TYR   OH   O N N 396 
TYR   OXT  O N N 397 
TYR   H    H N N 398 
TYR   H2   H N N 399 
TYR   HA   H N N 400 
TYR   HB2  H N N 401 
TYR   HB3  H N N 402 
TYR   HD1  H N N 403 
TYR   HD2  H N N 404 
TYR   HE1  H N N 405 
TYR   HE2  H N N 406 
TYR   HH   H N N 407 
TYR   HXT  H N N 408 
VAL   N    N N N 409 
VAL   CA   C N S 410 
VAL   C    C N N 411 
VAL   O    O N N 412 
VAL   CB   C N N 413 
VAL   CG1  C N N 414 
VAL   CG2  C N N 415 
VAL   OXT  O N N 416 
VAL   H    H N N 417 
VAL   H2   H N N 418 
VAL   HA   H N N 419 
VAL   HB   H N N 420 
VAL   HG11 H N N 421 
VAL   HG12 H N N 422 
VAL   HG13 H N N 423 
VAL   HG21 H N N 424 
VAL   HG22 H N N 425 
VAL   HG23 H N N 426 
VAL   HXT  H N N 427 
# 
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 
A1H3Y C16 C17  doub Y N 1   
A1H3Y C16 C15  sing Y N 2   
A1H3Y C17 C18  sing Y N 3   
A1H3Y C15 C14  doub Y N 4   
A1H3Y C18 C13  doub Y N 5   
A1H3Y C14 C13  sing Y N 6   
A1H3Y C13 C12  sing N N 7   
A1H3Y C12 O11  sing N N 8   
A1H3Y O11 C10  sing N N 9   
A1H3Y C10 C19  doub Y N 10  
A1H3Y C10 C09  sing Y N 11  
A1H3Y C19 C20  sing Y N 12  
A1H3Y C09 C08  doub Y N 13  
A1H3Y C20 C07  doub Y N 14  
A1H3Y C08 C07  sing Y N 15  
A1H3Y C08 C04  sing Y N 16  
A1H3Y C07 N06  sing Y N 17  
A1H3Y O01 C02  sing N N 18  
A1H3Y C04 C03  sing N N 19  
A1H3Y C04 C05  doub Y N 20  
A1H3Y C03 C02  sing N N 21  
A1H3Y N06 C05  sing Y N 22  
A1H3Y C12 H121 sing N N 23  
A1H3Y C12 H122 sing N N 24  
A1H3Y C14 H141 sing N N 25  
A1H3Y C02 H021 sing N N 26  
A1H3Y C02 H022 sing N N 27  
A1H3Y C03 H031 sing N N 28  
A1H3Y C03 H032 sing N N 29  
A1H3Y C05 H051 sing N N 30  
A1H3Y C09 H091 sing N N 31  
A1H3Y C15 H151 sing N N 32  
A1H3Y C16 H161 sing N N 33  
A1H3Y C17 H171 sing N N 34  
A1H3Y C18 H181 sing N N 35  
A1H3Y C19 H191 sing N N 36  
A1H3Y C20 H201 sing N N 37  
A1H3Y N06 H061 sing N N 38  
A1H3Y O01 H011 sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
GLN   N   CA   sing N N 122 
GLN   N   H    sing N N 123 
GLN   N   H2   sing N N 124 
GLN   CA  C    sing N N 125 
GLN   CA  CB   sing N N 126 
GLN   CA  HA   sing N N 127 
GLN   C   O    doub N N 128 
GLN   C   OXT  sing N N 129 
GLN   CB  CG   sing N N 130 
GLN   CB  HB2  sing N N 131 
GLN   CB  HB3  sing N N 132 
GLN   CG  CD   sing N N 133 
GLN   CG  HG2  sing N N 134 
GLN   CG  HG3  sing N N 135 
GLN   CD  OE1  doub N N 136 
GLN   CD  NE2  sing N N 137 
GLN   NE2 HE21 sing N N 138 
GLN   NE2 HE22 sing N N 139 
GLN   OXT HXT  sing N N 140 
GLU   N   CA   sing N N 141 
GLU   N   H    sing N N 142 
GLU   N   H2   sing N N 143 
GLU   CA  C    sing N N 144 
GLU   CA  CB   sing N N 145 
GLU   CA  HA   sing N N 146 
GLU   C   O    doub N N 147 
GLU   C   OXT  sing N N 148 
GLU   CB  CG   sing N N 149 
GLU   CB  HB2  sing N N 150 
GLU   CB  HB3  sing N N 151 
GLU   CG  CD   sing N N 152 
GLU   CG  HG2  sing N N 153 
GLU   CG  HG3  sing N N 154 
GLU   CD  OE1  doub N N 155 
GLU   CD  OE2  sing N N 156 
GLU   OE2 HE2  sing N N 157 
GLU   OXT HXT  sing N N 158 
GLY   N   CA   sing N N 159 
GLY   N   H    sing N N 160 
GLY   N   H2   sing N N 161 
GLY   CA  C    sing N N 162 
GLY   CA  HA2  sing N N 163 
GLY   CA  HA3  sing N N 164 
GLY   C   O    doub N N 165 
GLY   C   OXT  sing N N 166 
GLY   OXT HXT  sing N N 167 
HIS   N   CA   sing N N 168 
HIS   N   H    sing N N 169 
HIS   N   H2   sing N N 170 
HIS   CA  C    sing N N 171 
HIS   CA  CB   sing N N 172 
HIS   CA  HA   sing N N 173 
HIS   C   O    doub N N 174 
HIS   C   OXT  sing N N 175 
HIS   CB  CG   sing N N 176 
HIS   CB  HB2  sing N N 177 
HIS   CB  HB3  sing N N 178 
HIS   CG  ND1  sing Y N 179 
HIS   CG  CD2  doub Y N 180 
HIS   ND1 CE1  doub Y N 181 
HIS   ND1 HD1  sing N N 182 
HIS   CD2 NE2  sing Y N 183 
HIS   CD2 HD2  sing N N 184 
HIS   CE1 NE2  sing Y N 185 
HIS   CE1 HE1  sing N N 186 
HIS   NE2 HE2  sing N N 187 
HIS   OXT HXT  sing N N 188 
HOH   O   H1   sing N N 189 
HOH   O   H2   sing N N 190 
ILE   N   CA   sing N N 191 
ILE   N   H    sing N N 192 
ILE   N   H2   sing N N 193 
ILE   CA  C    sing N N 194 
ILE   CA  CB   sing N N 195 
ILE   CA  HA   sing N N 196 
ILE   C   O    doub N N 197 
ILE   C   OXT  sing N N 198 
ILE   CB  CG1  sing N N 199 
ILE   CB  CG2  sing N N 200 
ILE   CB  HB   sing N N 201 
ILE   CG1 CD1  sing N N 202 
ILE   CG1 HG12 sing N N 203 
ILE   CG1 HG13 sing N N 204 
ILE   CG2 HG21 sing N N 205 
ILE   CG2 HG22 sing N N 206 
ILE   CG2 HG23 sing N N 207 
ILE   CD1 HD11 sing N N 208 
ILE   CD1 HD12 sing N N 209 
ILE   CD1 HD13 sing N N 210 
ILE   OXT HXT  sing N N 211 
LEU   N   CA   sing N N 212 
LEU   N   H    sing N N 213 
LEU   N   H2   sing N N 214 
LEU   CA  C    sing N N 215 
LEU   CA  CB   sing N N 216 
LEU   CA  HA   sing N N 217 
LEU   C   O    doub N N 218 
LEU   C   OXT  sing N N 219 
LEU   CB  CG   sing N N 220 
LEU   CB  HB2  sing N N 221 
LEU   CB  HB3  sing N N 222 
LEU   CG  CD1  sing N N 223 
LEU   CG  CD2  sing N N 224 
LEU   CG  HG   sing N N 225 
LEU   CD1 HD11 sing N N 226 
LEU   CD1 HD12 sing N N 227 
LEU   CD1 HD13 sing N N 228 
LEU   CD2 HD21 sing N N 229 
LEU   CD2 HD22 sing N N 230 
LEU   CD2 HD23 sing N N 231 
LEU   OXT HXT  sing N N 232 
LYS   N   CA   sing N N 233 
LYS   N   H    sing N N 234 
LYS   N   H2   sing N N 235 
LYS   CA  C    sing N N 236 
LYS   CA  CB   sing N N 237 
LYS   CA  HA   sing N N 238 
LYS   C   O    doub N N 239 
LYS   C   OXT  sing N N 240 
LYS   CB  CG   sing N N 241 
LYS   CB  HB2  sing N N 242 
LYS   CB  HB3  sing N N 243 
LYS   CG  CD   sing N N 244 
LYS   CG  HG2  sing N N 245 
LYS   CG  HG3  sing N N 246 
LYS   CD  CE   sing N N 247 
LYS   CD  HD2  sing N N 248 
LYS   CD  HD3  sing N N 249 
LYS   CE  NZ   sing N N 250 
LYS   CE  HE2  sing N N 251 
LYS   CE  HE3  sing N N 252 
LYS   NZ  HZ1  sing N N 253 
LYS   NZ  HZ2  sing N N 254 
LYS   NZ  HZ3  sing N N 255 
LYS   OXT HXT  sing N N 256 
MET   N   CA   sing N N 257 
MET   N   H    sing N N 258 
MET   N   H2   sing N N 259 
MET   CA  C    sing N N 260 
MET   CA  CB   sing N N 261 
MET   CA  HA   sing N N 262 
MET   C   O    doub N N 263 
MET   C   OXT  sing N N 264 
MET   CB  CG   sing N N 265 
MET   CB  HB2  sing N N 266 
MET   CB  HB3  sing N N 267 
MET   CG  SD   sing N N 268 
MET   CG  HG2  sing N N 269 
MET   CG  HG3  sing N N 270 
MET   SD  CE   sing N N 271 
MET   CE  HE1  sing N N 272 
MET   CE  HE2  sing N N 273 
MET   CE  HE3  sing N N 274 
MET   OXT HXT  sing N N 275 
PHE   N   CA   sing N N 276 
PHE   N   H    sing N N 277 
PHE   N   H2   sing N N 278 
PHE   CA  C    sing N N 279 
PHE   CA  CB   sing N N 280 
PHE   CA  HA   sing N N 281 
PHE   C   O    doub N N 282 
PHE   C   OXT  sing N N 283 
PHE   CB  CG   sing N N 284 
PHE   CB  HB2  sing N N 285 
PHE   CB  HB3  sing N N 286 
PHE   CG  CD1  doub Y N 287 
PHE   CG  CD2  sing Y N 288 
PHE   CD1 CE1  sing Y N 289 
PHE   CD1 HD1  sing N N 290 
PHE   CD2 CE2  doub Y N 291 
PHE   CD2 HD2  sing N N 292 
PHE   CE1 CZ   doub Y N 293 
PHE   CE1 HE1  sing N N 294 
PHE   CE2 CZ   sing Y N 295 
PHE   CE2 HE2  sing N N 296 
PHE   CZ  HZ   sing N N 297 
PHE   OXT HXT  sing N N 298 
PRO   N   CA   sing N N 299 
PRO   N   CD   sing N N 300 
PRO   N   H    sing N N 301 
PRO   CA  C    sing N N 302 
PRO   CA  CB   sing N N 303 
PRO   CA  HA   sing N N 304 
PRO   C   O    doub N N 305 
PRO   C   OXT  sing N N 306 
PRO   CB  CG   sing N N 307 
PRO   CB  HB2  sing N N 308 
PRO   CB  HB3  sing N N 309 
PRO   CG  CD   sing N N 310 
PRO   CG  HG2  sing N N 311 
PRO   CG  HG3  sing N N 312 
PRO   CD  HD2  sing N N 313 
PRO   CD  HD3  sing N N 314 
PRO   OXT HXT  sing N N 315 
SER   N   CA   sing N N 316 
SER   N   H    sing N N 317 
SER   N   H2   sing N N 318 
SER   CA  C    sing N N 319 
SER   CA  CB   sing N N 320 
SER   CA  HA   sing N N 321 
SER   C   O    doub N N 322 
SER   C   OXT  sing N N 323 
SER   CB  OG   sing N N 324 
SER   CB  HB2  sing N N 325 
SER   CB  HB3  sing N N 326 
SER   OG  HG   sing N N 327 
SER   OXT HXT  sing N N 328 
THR   N   CA   sing N N 329 
THR   N   H    sing N N 330 
THR   N   H2   sing N N 331 
THR   CA  C    sing N N 332 
THR   CA  CB   sing N N 333 
THR   CA  HA   sing N N 334 
THR   C   O    doub N N 335 
THR   C   OXT  sing N N 336 
THR   CB  OG1  sing N N 337 
THR   CB  CG2  sing N N 338 
THR   CB  HB   sing N N 339 
THR   OG1 HG1  sing N N 340 
THR   CG2 HG21 sing N N 341 
THR   CG2 HG22 sing N N 342 
THR   CG2 HG23 sing N N 343 
THR   OXT HXT  sing N N 344 
TRP   N   CA   sing N N 345 
TRP   N   H    sing N N 346 
TRP   N   H2   sing N N 347 
TRP   CA  C    sing N N 348 
TRP   CA  CB   sing N N 349 
TRP   CA  HA   sing N N 350 
TRP   C   O    doub N N 351 
TRP   C   OXT  sing N N 352 
TRP   CB  CG   sing N N 353 
TRP   CB  HB2  sing N N 354 
TRP   CB  HB3  sing N N 355 
TRP   CG  CD1  doub Y N 356 
TRP   CG  CD2  sing Y N 357 
TRP   CD1 NE1  sing Y N 358 
TRP   CD1 HD1  sing N N 359 
TRP   CD2 CE2  doub Y N 360 
TRP   CD2 CE3  sing Y N 361 
TRP   NE1 CE2  sing Y N 362 
TRP   NE1 HE1  sing N N 363 
TRP   CE2 CZ2  sing Y N 364 
TRP   CE3 CZ3  doub Y N 365 
TRP   CE3 HE3  sing N N 366 
TRP   CZ2 CH2  doub Y N 367 
TRP   CZ2 HZ2  sing N N 368 
TRP   CZ3 CH2  sing Y N 369 
TRP   CZ3 HZ3  sing N N 370 
TRP   CH2 HH2  sing N N 371 
TRP   OXT HXT  sing N N 372 
TYR   N   CA   sing N N 373 
TYR   N   H    sing N N 374 
TYR   N   H2   sing N N 375 
TYR   CA  C    sing N N 376 
TYR   CA  CB   sing N N 377 
TYR   CA  HA   sing N N 378 
TYR   C   O    doub N N 379 
TYR   C   OXT  sing N N 380 
TYR   CB  CG   sing N N 381 
TYR   CB  HB2  sing N N 382 
TYR   CB  HB3  sing N N 383 
TYR   CG  CD1  doub Y N 384 
TYR   CG  CD2  sing Y N 385 
TYR   CD1 CE1  sing Y N 386 
TYR   CD1 HD1  sing N N 387 
TYR   CD2 CE2  doub Y N 388 
TYR   CD2 HD2  sing N N 389 
TYR   CE1 CZ   doub Y N 390 
TYR   CE1 HE1  sing N N 391 
TYR   CE2 CZ   sing Y N 392 
TYR   CE2 HE2  sing N N 393 
TYR   CZ  OH   sing N N 394 
TYR   OH  HH   sing N N 395 
TYR   OXT HXT  sing N N 396 
VAL   N   CA   sing N N 397 
VAL   N   H    sing N N 398 
VAL   N   H2   sing N N 399 
VAL   CA  C    sing N N 400 
VAL   CA  CB   sing N N 401 
VAL   CA  HA   sing N N 402 
VAL   C   O    doub N N 403 
VAL   C   OXT  sing N N 404 
VAL   CB  CG1  sing N N 405 
VAL   CB  CG2  sing N N 406 
VAL   CB  HB   sing N N 407 
VAL   CG1 HG11 sing N N 408 
VAL   CG1 HG12 sing N N 409 
VAL   CG1 HG13 sing N N 410 
VAL   CG2 HG21 sing N N 411 
VAL   CG2 HG22 sing N N 412 
VAL   CG2 HG23 sing N N 413 
VAL   OXT HXT  sing N N 414 
# 
_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   6S60 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8RXP 
_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]   0.008791 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003481 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016308 
_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]   0.013435 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    . ALA   A 1 5   ? -12.555 -19.885 28.874 1.00 91.52  ? 220 ALA   B N    1 
ATOM   2    C CA   . ALA   A 1 5   ? -13.977 -19.520 28.842 1.00 90.68  ? 220 ALA   B CA   1 
ATOM   3    C C    . ALA   A 1 5   ? -14.837 -20.735 28.488 1.00 92.35  ? 220 ALA   B C    1 
ATOM   4    O O    . ALA   A 1 5   ? -14.549 -21.437 27.510 1.00 92.81  ? 220 ALA   B O    1 
ATOM   5    C CB   . ALA   A 1 5   ? -14.220 -18.385 27.845 1.00 86.83  ? 220 ALA   B CB   1 
ATOM   6    N N    . ARG   A 1 6   ? -15.892 -20.989 29.279 1.00 88.79  ? 221 ARG   B N    1 
ATOM   7    C CA   . ARG   A 1 6   ? -16.717 -22.179 29.091 1.00 88.25  ? 221 ARG   B CA   1 
ATOM   8    C C    . ARG   A 1 6   ? -18.170 -21.874 28.746 1.00 80.96  ? 221 ARG   B C    1 
ATOM   9    O O    . ARG   A 1 6   ? -18.960 -22.812 28.575 1.00 78.23  ? 221 ARG   B O    1 
ATOM   10   C CB   . ARG   A 1 6   ? -16.645 -23.078 30.336 1.00 88.74  ? 221 ARG   B CB   1 
ATOM   11   C CG   . ARG   A 1 6   ? -15.215 -23.412 30.757 1.00 93.22  ? 221 ARG   B CG   1 
ATOM   12   C CD   . ARG   A 1 6   ? -15.135 -24.696 31.580 1.00 99.18  ? 221 ARG   B CD   1 
ATOM   13   N NE   . ARG   A 1 6   ? -13.879 -25.407 31.367 1.00 101.46 ? 221 ARG   B NE   1 
ATOM   14   C CZ   . ARG   A 1 6   ? -13.608 -26.616 31.843 1.00 104.71 ? 221 ARG   B CZ   1 
ATOM   15   N NH1  . ARG   A 1 6   ? -14.482 -27.280 32.584 1.00 105.17 ? 221 ARG   B NH1  1 
ATOM   16   N NH2  . ARG   A 1 6   ? -12.425 -27.171 31.579 1.00 104.14 ? 221 ARG   B NH2  1 
ATOM   17   N N    . GLY   A 1 7   ? -18.539 -20.600 28.618 1.00 77.91  ? 222 GLY   B N    1 
ATOM   18   C CA   . GLY   A 1 7   ? -19.855 -20.203 28.155 1.00 69.10  ? 222 GLY   B CA   1 
ATOM   19   C C    . GLY   A 1 7   ? -19.804 -18.772 27.670 1.00 63.21  ? 222 GLY   B C    1 
ATOM   20   O O    . GLY   A 1 7   ? -18.756 -18.122 27.698 1.00 64.60  ? 222 GLY   B O    1 
ATOM   21   N N    . LEU   A 1 8   ? -20.952 -18.283 27.204 1.00 58.90  ? 223 LEU   B N    1 
ATOM   22   C CA   . LEU   A 1 8   ? -21.074 -16.886 26.795 1.00 58.56  ? 223 LEU   B CA   1 
ATOM   23   C C    . LEU   A 1 8   ? -21.139 -16.008 28.042 1.00 60.58  ? 223 LEU   B C    1 
ATOM   24   O O    . LEU   A 1 8   ? -22.206 -15.624 28.533 1.00 56.24  ? 223 LEU   B O    1 
ATOM   25   C CB   . LEU   A 1 8   ? -22.292 -16.692 25.905 1.00 60.81  ? 223 LEU   B CB   1 
ATOM   26   C CG   . LEU   A 1 8   ? -22.532 -15.282 25.370 1.00 55.84  ? 223 LEU   B CG   1 
ATOM   27   C CD1  . LEU   A 1 8   ? -21.238 -14.711 24.937 1.00 56.66  ? 223 LEU   B CD1  1 
ATOM   28   C CD2  . LEU   A 1 8   ? -23.474 -15.382 24.190 1.00 52.38  ? 223 LEU   B CD2  1 
ATOM   29   N N    . GLY   A 1 9   ? -19.959 -15.682 28.560 1.00 62.22  ? 224 GLY   B N    1 
ATOM   30   C CA   . GLY   A 1 9   ? -19.877 -14.777 29.680 1.00 61.20  ? 224 GLY   B CA   1 
ATOM   31   C C    . GLY   A 1 9   ? -18.491 -14.688 30.273 1.00 64.87  ? 224 GLY   B C    1 
ATOM   32   O O    . GLY   A 1 9   ? -17.639 -15.548 30.040 1.00 65.50  ? 224 GLY   B O    1 
ATOM   33   N N    . THR   A 1 10  ? -18.255 -13.643 31.040 1.00 61.46  ? 225 THR   B N    1 
ATOM   34   C CA   . THR   A 1 10  ? -16.990 -13.449 31.711 1.00 65.99  ? 225 THR   B CA   1 
ATOM   35   C C    . THR   A 1 10  ? -17.198 -13.539 33.208 1.00 67.40  ? 225 THR   B C    1 
ATOM   36   O O    . THR   A 1 10  ? -18.292 -13.818 33.707 1.00 68.36  ? 225 THR   B O    1 
ATOM   37   C CB   . THR   A 1 10  ? -16.353 -12.099 31.355 1.00 70.67  ? 225 THR   B CB   1 
ATOM   38   O OG1  . THR   A 1 10  ? -16.893 -11.067 32.216 1.00 65.99  ? 225 THR   B OG1  1 
ATOM   39   C CG2  . THR   A 1 10  ? -16.538 -11.765 29.843 1.00 63.68  ? 225 THR   B CG2  1 
ATOM   40   N N    . ALA   A 1 11  ? -16.130 -13.261 33.932 1.00 76.50  ? 226 ALA   B N    1 
ATOM   41   C CA   . ALA   A 1 11  ? -16.144 -13.412 35.372 1.00 75.83  ? 226 ALA   B CA   1 
ATOM   42   C C    . ALA   A 1 11  ? -16.980 -12.341 36.064 1.00 73.91  ? 226 ALA   B C    1 
ATOM   43   O O    . ALA   A 1 11  ? -17.372 -12.531 37.217 1.00 74.18  ? 226 ALA   B O    1 
ATOM   44   C CB   . ALA   A 1 11  ? -14.699 -13.392 35.856 1.00 78.82  ? 226 ALA   B CB   1 
ATOM   45   N N    . ARG   A 1 12  ? -17.250 -11.224 35.389 1.00 71.68  ? 227 ARG   B N    1 
ATOM   46   C CA   . ARG   A 1 12  ? -18.096 -10.156 35.905 1.00 67.15  ? 227 ARG   B CA   1 
ATOM   47   C C    . ARG   A 1 12  ? -19.539 -10.299 35.472 1.00 63.70  ? 227 ARG   B C    1 
ATOM   48   O O    . ARG   A 1 12  ? -20.441 -9.926  36.223 1.00 66.24  ? 227 ARG   B O    1 
ATOM   49   C CB   . ARG   A 1 12  ? -17.605 -8.790  35.415 1.00 68.88  ? 227 ARG   B CB   1 
ATOM   50   C CG   . ARG   A 1 12  ? -16.214 -8.400  35.855 1.00 72.32  ? 227 ARG   B CG   1 
ATOM   51   C CD   . ARG   A 1 12  ? -15.846 -7.048  35.276 1.00 74.45  ? 227 ARG   B CD   1 
ATOM   52   N NE   . ARG   A 1 12  ? -16.512 -5.968  35.991 1.00 77.47  ? 227 ARG   B NE   1 
ATOM   53   C CZ   . ARG   A 1 12  ? -16.153 -4.695  35.916 1.00 80.80  ? 227 ARG   B CZ   1 
ATOM   54   N NH1  . ARG   A 1 12  ? -15.157 -4.304  35.129 1.00 82.00  ? 227 ARG   B NH1  1 
ATOM   55   N NH2  . ARG   A 1 12  ? -16.805 -3.794  36.651 1.00 82.83  ? 227 ARG   B NH2  1 
ATOM   56   N N    . LEU   A 1 13  ? -19.784 -10.785 34.262 1.00 66.28  ? 228 LEU   B N    1 
ATOM   57   C CA   . LEU   A 1 13  ? -21.126 -10.781 33.716 1.00 61.58  ? 228 LEU   B CA   1 
ATOM   58   C C    . LEU   A 1 13  ? -21.333 -12.057 32.924 1.00 62.76  ? 228 LEU   B C    1 
ATOM   59   O O    . LEU   A 1 13  ? -20.491 -12.430 32.105 1.00 64.77  ? 228 LEU   B O    1 
ATOM   60   C CB   . LEU   A 1 13  ? -21.362 -9.550  32.839 1.00 59.19  ? 228 LEU   B CB   1 
ATOM   61   C CG   . LEU   A 1 13  ? -22.836 -9.296  32.506 1.00 61.09  ? 228 LEU   B CG   1 
ATOM   62   C CD1  . LEU   A 1 13  ? -23.632 -8.864  33.759 1.00 61.38  ? 228 LEU   B CD1  1 
ATOM   63   C CD2  . LEU   A 1 13  ? -22.955 -8.261  31.393 1.00 57.65  ? 228 LEU   B CD2  1 
ATOM   64   N N    . GLN   A 1 14  ? -22.441 -12.733 33.193 1.00 57.01  ? 229 GLN   B N    1 
ATOM   65   C CA   . GLN   A 1 14  ? -22.798 -13.967 32.518 1.00 55.53  ? 229 GLN   B CA   1 
ATOM   66   C C    . GLN   A 1 14  ? -24.163 -13.788 31.881 1.00 55.27  ? 229 GLN   B C    1 
ATOM   67   O O    . GLN   A 1 14  ? -25.069 -13.196 32.480 1.00 54.74  ? 229 GLN   B O    1 
ATOM   68   C CB   . GLN   A 1 14  ? -22.841 -15.170 33.481 1.00 59.27  ? 229 GLN   B CB   1 
ATOM   69   C CG   . GLN   A 1 14  ? -23.499 -16.403 32.836 1.00 63.95  ? 229 GLN   B CG   1 
ATOM   70   C CD   . GLN   A 1 14  ? -22.623 -17.659 32.810 1.00 67.96  ? 229 GLN   B CD   1 
ATOM   71   O OE1  . GLN   A 1 14  ? -22.060 -18.072 33.837 1.00 69.73  ? 229 GLN   B OE1  1 
ATOM   72   N NE2  . GLN   A 1 14  ? -22.469 -18.246 31.615 1.00 65.26  ? 229 GLN   B NE2  1 
ATOM   73   N N    . LEU   A 1 15  ? -24.310 -14.303 30.670 1.00 55.92  ? 230 LEU   B N    1 
ATOM   74   C CA   . LEU   A 1 15  ? -25.602 -14.312 30.004 1.00 54.83  ? 230 LEU   B CA   1 
ATOM   75   C C    . LEU   A 1 15  ? -26.362 -15.555 30.431 1.00 56.89  ? 230 LEU   B C    1 
ATOM   76   O O    . LEU   A 1 15  ? -25.852 -16.675 30.339 1.00 61.34  ? 230 LEU   B O    1 
ATOM   77   C CB   . LEU   A 1 15  ? -25.445 -14.236 28.486 1.00 55.98  ? 230 LEU   B CB   1 
ATOM   78   C CG   . LEU   A 1 15  ? -26.803 -14.136 27.797 1.00 54.04  ? 230 LEU   B CG   1 
ATOM   79   C CD1  . LEU   A 1 15  ? -26.874 -12.862 27.034 1.00 51.81  ? 230 LEU   B CD1  1 
ATOM   80   C CD2  . LEU   A 1 15  ? -26.991 -15.326 26.846 1.00 55.81  ? 230 LEU   B CD2  1 
ATOM   81   N N    . VAL   A 1 16  ? -27.553 -15.350 30.961 1.00 57.02  ? 231 VAL   B N    1 
ATOM   82   C CA   . VAL   A 1 16  ? -28.353 -16.466 31.425 1.00 60.95  ? 231 VAL   B CA   1 
ATOM   83   C C    . VAL   A 1 16  ? -29.271 -16.947 30.327 1.00 62.39  ? 231 VAL   B C    1 
ATOM   84   O O    . VAL   A 1 16  ? -29.410 -18.150 30.101 1.00 67.06  ? 231 VAL   B O    1 
ATOM   85   C CB   . VAL   A 1 16  ? -29.151 -16.047 32.672 1.00 58.74  ? 231 VAL   B CB   1 
ATOM   86   C CG1  . VAL   A 1 16  ? -30.071 -17.156 33.081 1.00 64.07  ? 231 VAL   B CG1  1 
ATOM   87   C CG2  . VAL   A 1 16  ? -28.201 -15.686 33.779 1.00 60.51  ? 231 VAL   B CG2  1 
ATOM   88   N N    . GLU   A 1 17  ? -29.894 -16.000 29.642 1.00 55.80  ? 232 GLU   B N    1 
ATOM   89   C CA   . GLU   A 1 17  ? -30.887 -16.333 28.646 1.00 58.10  ? 232 GLU   B CA   1 
ATOM   90   C C    . GLU   A 1 17  ? -30.941 -15.206 27.636 1.00 53.76  ? 232 GLU   B C    1 
ATOM   91   O O    . GLU   A 1 17  ? -30.684 -14.041 27.953 1.00 52.11  ? 232 GLU   B O    1 
ATOM   92   C CB   . GLU   A 1 17  ? -32.265 -16.597 29.273 1.00 61.41  ? 232 GLU   B CB   1 
ATOM   93   C CG   . GLU   A 1 17  ? -32.619 -18.094 29.250 1.00 67.34  ? 232 GLU   B CG   1 
ATOM   94   C CD   . GLU   A 1 17  ? -34.107 -18.391 29.366 1.00 71.17  ? 232 GLU   B CD   1 
ATOM   95   O OE1  . GLU   A 1 17  ? -34.713 -18.845 28.361 1.00 66.55  ? 232 GLU   B OE1  1 
ATOM   96   O OE2  . GLU   A 1 17  ? -34.658 -18.223 30.480 1.00 79.45  ? 232 GLU   B OE2  1 
ATOM   97   N N    . PHE   A 1 18  ? -31.203 -15.588 26.397 1.00 53.58  ? 233 PHE   B N    1 
ATOM   98   C CA   . PHE   A 1 18  ? -31.506 -14.634 25.356 1.00 47.22  ? 233 PHE   B CA   1 
ATOM   99   C C    . PHE   A 1 18  ? -32.410 -15.345 24.377 1.00 49.11  ? 233 PHE   B C    1 
ATOM   100  O O    . PHE   A 1 18  ? -32.217 -16.533 24.100 1.00 51.19  ? 233 PHE   B O    1 
ATOM   101  C CB   . PHE   A 1 18  ? -30.244 -14.142 24.661 1.00 48.30  ? 233 PHE   B CB   1 
ATOM   102  C CG   . PHE   A 1 18  ? -30.508 -13.454 23.367 1.00 49.28  ? 233 PHE   B CG   1 
ATOM   103  C CD1  . PHE   A 1 18  ? -30.594 -14.175 22.182 1.00 50.75  ? 233 PHE   B CD1  1 
ATOM   104  C CD2  . PHE   A 1 18  ? -30.690 -12.083 23.328 1.00 49.88  ? 233 PHE   B CD2  1 
ATOM   105  C CE1  . PHE   A 1 18  ? -30.834 -13.524 20.964 1.00 50.16  ? 233 PHE   B CE1  1 
ATOM   106  C CE2  . PHE   A 1 18  ? -30.930 -11.439 22.122 1.00 49.63  ? 233 PHE   B CE2  1 
ATOM   107  C CZ   . PHE   A 1 18  ? -31.005 -12.163 20.947 1.00 47.81  ? 233 PHE   B CZ   1 
ATOM   108  N N    . SER   A 1 19  ? -33.389 -14.627 23.849 1.00 50.46  ? 234 SER   B N    1 
ATOM   109  C CA   . SER   A 1 19  ? -34.165 -15.212 22.774 1.00 46.90  ? 234 SER   B CA   1 
ATOM   110  C C    . SER   A 1 19  ? -34.898 -14.111 22.032 1.00 46.29  ? 234 SER   B C    1 
ATOM   111  O O    . SER   A 1 19  ? -35.131 -13.012 22.550 1.00 45.41  ? 234 SER   B O    1 
ATOM   112  C CB   . SER   A 1 19  ? -35.142 -16.270 23.291 1.00 49.16  ? 234 SER   B CB   1 
ATOM   113  O OG   . SER   A 1 19  ? -36.084 -15.703 24.165 1.00 50.11  ? 234 SER   B OG   1 
ATOM   114  N N    . ALA   A 1 20  ? -35.224 -14.423 20.788 1.00 48.25  ? 235 ALA   B N    1 
ATOM   115  C CA   . ALA   A 1 20  ? -36.062 -13.592 19.957 1.00 45.23  ? 235 ALA   B CA   1 
ATOM   116  C C    . ALA   A 1 20  ? -37.233 -14.471 19.585 1.00 43.87  ? 235 ALA   B C    1 
ATOM   117  O O    . ALA   A 1 20  ? -37.033 -15.624 19.199 1.00 47.23  ? 235 ALA   B O    1 
ATOM   118  C CB   . ALA   A 1 20  ? -35.297 -13.109 18.729 1.00 46.27  ? 235 ALA   B CB   1 
ATOM   119  N N    . PHE   A 1 21  ? -38.446 -13.959 19.733 1.00 44.80  ? 236 PHE   B N    1 
ATOM   120  C CA   . PHE   A 1 21  ? -39.608 -14.825 19.646 1.00 46.15  ? 236 PHE   B CA   1 
ATOM   121  C C    . PHE   A 1 21  ? -40.744 -14.021 19.055 1.00 42.70  ? 236 PHE   B C    1 
ATOM   122  O O    . PHE   A 1 21  ? -40.688 -12.795 19.001 1.00 43.70  ? 236 PHE   B O    1 
ATOM   123  C CB   . PHE   A 1 21  ? -39.987 -15.381 21.039 1.00 51.55  ? 236 PHE   B CB   1 
ATOM   124  C CG   . PHE   A 1 21  ? -40.292 -14.310 22.058 1.00 45.78  ? 236 PHE   B CG   1 
ATOM   125  C CD1  . PHE   A 1 21  ? -41.573 -13.810 22.190 1.00 48.02  ? 236 PHE   B CD1  1 
ATOM   126  C CD2  . PHE   A 1 21  ? -39.285 -13.785 22.866 1.00 49.84  ? 236 PHE   B CD2  1 
ATOM   127  C CE1  . PHE   A 1 21  ? -41.848 -12.801 23.116 1.00 51.88  ? 236 PHE   B CE1  1 
ATOM   128  C CE2  . PHE   A 1 21  ? -39.549 -12.777 23.803 1.00 46.98  ? 236 PHE   B CE2  1 
ATOM   129  C CZ   . PHE   A 1 21  ? -40.830 -12.286 23.918 1.00 48.24  ? 236 PHE   B CZ   1 
ATOM   130  N N    . VAL   A 1 22  ? -41.792 -14.722 18.637 1.00 47.28  ? 237 VAL   B N    1 
ATOM   131  C CA   . VAL   A 1 22  ? -43.070 -14.108 18.290 1.00 52.34  ? 237 VAL   B CA   1 
ATOM   132  C C    . VAL   A 1 22  ? -44.187 -14.887 18.984 1.00 54.63  ? 237 VAL   B C    1 
ATOM   133  O O    . VAL   A 1 22  ? -44.201 -16.127 18.955 1.00 53.38  ? 237 VAL   B O    1 
ATOM   134  C CB   . VAL   A 1 22  ? -43.306 -14.064 16.762 1.00 54.08  ? 237 VAL   B CB   1 
ATOM   135  C CG1  . VAL   A 1 22  ? -43.202 -15.449 16.135 1.00 52.22  ? 237 VAL   B CG1  1 
ATOM   136  C CG2  . VAL   A 1 22  ? -44.674 -13.452 16.447 1.00 54.62  ? 237 VAL   B CG2  1 
ATOM   137  N N    . GLU   A 1 23  ? -45.113 -14.160 19.621 1.00 55.92  ? 238 GLU   B N    1 
ATOM   138  C CA   . GLU   A 1 23  ? -46.329 -14.771 20.158 1.00 62.16  ? 238 GLU   B CA   1 
ATOM   139  C C    . GLU   A 1 23  ? -47.480 -14.464 19.211 1.00 64.43  ? 238 GLU   B C    1 
ATOM   140  O O    . GLU   A 1 23  ? -47.726 -13.285 18.922 1.00 62.58  ? 238 GLU   B O    1 
ATOM   141  C CB   . GLU   A 1 23  ? -46.652 -14.255 21.570 1.00 60.43  ? 238 GLU   B CB   1 
ATOM   142  C CG   . GLU   A 1 23  ? -45.549 -14.444 22.636 1.00 58.27  ? 238 GLU   B CG   1 
ATOM   143  C CD   . GLU   A 1 23  ? -45.700 -13.508 23.840 1.00 58.79  ? 238 GLU   B CD   1 
ATOM   144  O OE1  . GLU   A 1 23  ? -46.307 -12.429 23.680 1.00 59.65  ? 238 GLU   B OE1  1 
ATOM   145  O OE2  . GLU   A 1 23  ? -45.224 -13.846 24.952 1.00 58.71  ? 238 GLU   B OE2  1 
ATOM   146  N N    . PRO   A 1 24  ? -48.205 -15.454 18.705 1.00 68.71  ? 239 PRO   B N    1 
ATOM   147  C CA   . PRO   A 1 24  ? -49.267 -15.162 17.745 1.00 72.49  ? 239 PRO   B CA   1 
ATOM   148  C C    . PRO   A 1 24  ? -50.453 -14.549 18.457 1.00 77.40  ? 239 PRO   B C    1 
ATOM   149  O O    . PRO   A 1 24  ? -50.576 -14.686 19.685 1.00 83.12  ? 239 PRO   B O    1 
ATOM   150  C CB   . PRO   A 1 24  ? -49.613 -16.542 17.176 1.00 74.73  ? 239 PRO   B CB   1 
ATOM   151  C CG   . PRO   A 1 24  ? -49.368 -17.453 18.340 1.00 74.12  ? 239 PRO   B CG   1 
ATOM   152  C CD   . PRO   A 1 24  ? -48.222 -16.865 19.129 1.00 67.94  ? 239 PRO   B CD   1 
ATOM   153  N N    . PRO   A 1 25  ? -51.350 -13.881 17.733 1.00 84.42  ? 240 PRO   B N    1 
ATOM   154  C CA   . PRO   A 1 25  ? -52.520 -13.285 18.402 1.00 87.06  ? 240 PRO   B CA   1 
ATOM   155  C C    . PRO   A 1 25  ? -53.304 -14.283 19.239 1.00 94.67  ? 240 PRO   B C    1 
ATOM   156  O O    . PRO   A 1 25  ? -53.817 -13.921 20.308 1.00 96.03  ? 240 PRO   B O    1 
ATOM   157  C CB   . PRO   A 1 25  ? -53.347 -12.737 17.231 1.00 86.50  ? 240 PRO   B CB   1 
ATOM   158  C CG   . PRO   A 1 25  ? -52.361 -12.567 16.109 1.00 82.34  ? 240 PRO   B CG   1 
ATOM   159  C CD   . PRO   A 1 25  ? -51.390 -13.695 16.274 1.00 83.81  ? 240 PRO   B CD   1 
ATOM   160  N N    . ASP   A 1 26  ? -53.391 -15.541 18.795 1.00 103.93 ? 241 ASP   B N    1 
ATOM   161  C CA   . ASP   A 1 26  ? -54.001 -16.601 19.592 1.00 103.82 ? 241 ASP   B CA   1 
ATOM   162  C C    . ASP   A 1 26  ? -53.367 -16.753 20.966 1.00 102.86 ? 241 ASP   B C    1 
ATOM   163  O O    . ASP   A 1 26  ? -53.905 -17.499 21.790 1.00 106.14 ? 241 ASP   B O    1 
ATOM   164  C CB   . ASP   A 1 26  ? -53.885 -17.945 18.870 1.00 106.43 ? 241 ASP   B CB   1 
ATOM   165  C CG   . ASP   A 1 26  ? -54.684 -17.991 17.602 1.00 113.21 ? 241 ASP   B CG   1 
ATOM   166  O OD1  . ASP   A 1 26  ? -54.303 -17.274 16.650 1.00 112.98 ? 241 ASP   B OD1  1 
ATOM   167  O OD2  . ASP   A 1 26  ? -55.697 -18.728 17.566 1.00 120.38 ? 241 ASP   B OD2  1 
ATOM   168  N N    . ALA   A 1 27  ? -52.232 -16.093 21.217 1.00 94.89  ? 242 ALA   B N    1 
ATOM   169  C CA   . ALA   A 1 27  ? -51.460 -16.362 22.424 1.00 91.87  ? 242 ALA   B CA   1 
ATOM   170  C C    . ALA   A 1 27  ? -52.282 -16.126 23.678 1.00 93.58  ? 242 ALA   B C    1 
ATOM   171  O O    . ALA   A 1 27  ? -52.130 -16.860 24.660 1.00 90.03  ? 242 ALA   B O    1 
ATOM   172  C CB   . ALA   A 1 27  ? -50.200 -15.499 22.440 1.00 85.07  ? 242 ALA   B CB   1 
ATOM   173  N N    . VAL   A 1 28  ? -53.166 -15.124 23.648 1.00 95.07  ? 243 VAL   B N    1 
ATOM   174  C CA   . VAL   A 1 28  ? -54.002 -14.761 24.792 1.00 98.46  ? 243 VAL   B CA   1 
ATOM   175  C C    . VAL   A 1 28  ? -55.183 -15.695 24.994 1.00 102.59 ? 243 VAL   B C    1 
ATOM   176  O O    . VAL   A 1 28  ? -55.915 -15.556 25.987 1.00 106.04 ? 243 VAL   B O    1 
ATOM   177  C CB   . VAL   A 1 28  ? -54.523 -13.323 24.617 1.00 97.65  ? 243 VAL   B CB   1 
ATOM   178  C CG1  . VAL   A 1 28  ? -53.414 -12.432 24.073 1.00 98.77  ? 243 VAL   B CG1  1 
ATOM   179  C CG2  . VAL   A 1 28  ? -55.727 -13.309 23.690 1.00 103.55 ? 243 VAL   B CG2  1 
ATOM   180  N N    . ASP   A 1 29  ? -55.409 -16.622 24.068 1.00 105.27 ? 244 ASP   B N    1 
ATOM   181  C CA   . ASP   A 1 29  ? -56.403 -17.685 24.254 1.00 110.55 ? 244 ASP   B CA   1 
ATOM   182  C C    . ASP   A 1 29  ? -55.710 -18.913 24.832 1.00 109.73 ? 244 ASP   B C    1 
ATOM   183  O O    . ASP   A 1 29  ? -55.896 -19.250 26.006 1.00 112.93 ? 244 ASP   B O    1 
ATOM   184  C CB   . ASP   A 1 29  ? -57.103 -17.983 22.930 1.00 113.11 ? 244 ASP   B CB   1 
ATOM   185  C CG   . ASP   A 1 29  ? -58.215 -17.005 22.641 1.00 120.55 ? 244 ASP   B CG   1 
ATOM   186  O OD1  . ASP   A 1 29  ? -58.220 -15.913 23.258 1.00 117.64 ? 244 ASP   B OD1  1 
ATOM   187  O OD2  . ASP   A 1 29  ? -59.071 -17.318 21.785 1.00 131.52 ? 244 ASP   B OD2  1 
ATOM   188  N N    . SER   A 1 30  ? -54.906 -19.584 24.015 1.00 102.60 ? 245 SER   B N    1 
ATOM   189  C CA   . SER   A 1 30  ? -53.969 -20.593 24.483 1.00 98.55  ? 245 SER   B CA   1 
ATOM   190  C C    . SER   A 1 30  ? -52.565 -20.129 24.119 1.00 92.05  ? 245 SER   B C    1 
ATOM   191  O O    . SER   A 1 30  ? -52.324 -19.689 22.989 1.00 90.23  ? 245 SER   B O    1 
ATOM   192  C CB   . SER   A 1 30  ? -54.271 -21.962 23.874 1.00 102.14 ? 245 SER   B CB   1 
ATOM   193  O OG   . SER   A 1 30  ? -53.842 -22.995 24.746 1.00 104.00 ? 245 SER   B OG   1 
ATOM   194  N N    . TYR   A 1 31  ? -51.648 -20.216 25.075 1.00 85.88  ? 246 TYR   B N    1 
ATOM   195  C CA   . TYR   A 1 31  ? -50.372 -19.550 24.914 1.00 77.76  ? 246 TYR   B CA   1 
ATOM   196  C C    . TYR   A 1 31  ? -49.433 -20.348 24.011 1.00 74.07  ? 246 TYR   B C    1 
ATOM   197  O O    . TYR   A 1 31  ? -49.422 -21.580 24.007 1.00 76.08  ? 246 TYR   B O    1 
ATOM   198  C CB   . TYR   A 1 31  ? -49.707 -19.310 26.267 1.00 75.50  ? 246 TYR   B CB   1 
ATOM   199  C CG   . TYR   A 1 31  ? -48.402 -18.580 26.103 1.00 69.32  ? 246 TYR   B CG   1 
ATOM   200  C CD1  . TYR   A 1 31  ? -48.380 -17.279 25.627 1.00 66.75  ? 246 TYR   B CD1  1 
ATOM   201  C CD2  . TYR   A 1 31  ? -47.194 -19.199 26.381 1.00 66.71  ? 246 TYR   B CD2  1 
ATOM   202  C CE1  . TYR   A 1 31  ? -47.197 -16.609 25.442 1.00 63.93  ? 246 TYR   B CE1  1 
ATOM   203  C CE2  . TYR   A 1 31  ? -46.010 -18.536 26.214 1.00 63.23  ? 246 TYR   B CE2  1 
ATOM   204  C CZ   . TYR   A 1 31  ? -46.012 -17.238 25.736 1.00 62.26  ? 246 TYR   B CZ   1 
ATOM   205  O OH   . TYR   A 1 31  ? -44.824 -16.558 25.540 1.00 60.48  ? 246 TYR   B OH   1 
ATOM   206  N N    . GLN   A 1 32  ? -48.633 -19.622 23.245 1.00 68.81  ? 247 GLN   B N    1 
ATOM   207  C CA   . GLN   A 1 32  ? -47.553 -20.219 22.478 1.00 68.72  ? 247 GLN   B CA   1 
ATOM   208  C C    . GLN   A 1 32  ? -46.588 -19.105 22.134 1.00 63.28  ? 247 GLN   B C    1 
ATOM   209  O O    . GLN   A 1 32  ? -46.992 -17.947 22.009 1.00 64.95  ? 247 GLN   B O    1 
ATOM   210  C CB   . GLN   A 1 32  ? -48.055 -20.886 21.197 1.00 67.73  ? 247 GLN   B CB   1 
ATOM   211  C CG   . GLN   A 1 32  ? -48.969 -19.982 20.397 1.00 69.79  ? 247 GLN   B CG   1 
ATOM   212  C CD   . GLN   A 1 32  ? -49.619 -20.680 19.228 1.00 75.69  ? 247 GLN   B CD   1 
ATOM   213  O OE1  . GLN   A 1 32  ? -48.939 -21.251 18.354 1.00 70.88  ? 247 GLN   B OE1  1 
ATOM   214  N NE2  . GLN   A 1 32  ? -50.957 -20.681 19.222 1.00 80.86  ? 247 GLN   B NE2  1 
ATOM   215  N N    . ARG   A 1 33  ? -45.314 -19.455 22.001 1.00 57.81  ? 248 ARG   B N    1 
ATOM   216  C CA   . ARG   A 1 33  ? -44.359 -18.529 21.410 1.00 57.36  ? 248 ARG   B CA   1 
ATOM   217  C C    . ARG   A 1 33  ? -43.430 -19.307 20.493 1.00 53.52  ? 248 ARG   B C    1 
ATOM   218  O O    . ARG   A 1 33  ? -43.003 -20.416 20.817 1.00 51.76  ? 248 ARG   B O    1 
ATOM   219  C CB   . ARG   A 1 33  ? -43.543 -17.770 22.473 1.00 53.41  ? 248 ARG   B CB   1 
ATOM   220  C CG   . ARG   A 1 33  ? -42.464 -18.612 23.136 1.00 56.14  ? 248 ARG   B CG   1 
ATOM   221  C CD   . ARG   A 1 33  ? -41.312 -17.757 23.644 1.00 52.84  ? 248 ARG   B CD   1 
ATOM   222  N NE   . ARG   A 1 33  ? -41.715 -17.039 24.843 1.00 59.38  ? 248 ARG   B NE   1 
ATOM   223  C CZ   . ARG   A 1 33  ? -40.875 -16.514 25.728 1.00 60.12  ? 248 ARG   B CZ   1 
ATOM   224  N NH1  . ARG   A 1 33  ? -39.556 -16.617 25.583 1.00 55.70  ? 248 ARG   B NH1  1 
ATOM   225  N NH2  . ARG   A 1 33  ? -41.371 -15.868 26.780 1.00 56.90  ? 248 ARG   B NH2  1 
ATOM   226  N N    . HIS   A 1 34  ? -43.124 -18.731 19.345 1.00 56.12  ? 249 HIS   B N    1 
ATOM   227  C CA   . HIS   A 1 34  ? -42.127 -19.297 18.450 1.00 50.73  ? 249 HIS   B CA   1 
ATOM   228  C C    . HIS   A 1 34  ? -40.803 -18.592 18.692 1.00 47.29  ? 249 HIS   B C    1 
ATOM   229  O O    . HIS   A 1 34  ? -40.751 -17.353 18.738 1.00 48.49  ? 249 HIS   B O    1 
ATOM   230  C CB   . HIS   A 1 34  ? -42.538 -19.143 16.993 1.00 51.83  ? 249 HIS   B CB   1 
ATOM   231  C CG   . HIS   A 1 34  ? -41.456 -19.511 16.028 1.00 58.10  ? 249 HIS   B CG   1 
ATOM   232  N ND1  . HIS   A 1 34  ? -41.221 -20.811 15.631 1.00 56.19  ? 249 HIS   B ND1  1 
ATOM   233  C CD2  . HIS   A 1 34  ? -40.533 -18.749 15.390 1.00 55.63  ? 249 HIS   B CD2  1 
ATOM   234  C CE1  . HIS   A 1 34  ? -40.209 -20.832 14.783 1.00 57.00  ? 249 HIS   B CE1  1 
ATOM   235  N NE2  . HIS   A 1 34  ? -39.775 -19.593 14.619 1.00 58.56  ? 249 HIS   B NE2  1 
ATOM   236  N N    . LEU   A 1 35  ? -39.741 -19.382 18.835 1.00 46.29  ? 250 LEU   B N    1 
ATOM   237  C CA   . LEU   A 1 35  ? -38.395 -18.867 19.052 1.00 45.53  ? 250 LEU   B CA   1 
ATOM   238  C C    . LEU   A 1 35  ? -37.620 -18.846 17.728 1.00 54.29  ? 250 LEU   B C    1 
ATOM   239  O O    . LEU   A 1 35  ? -37.460 -19.881 17.065 1.00 47.97  ? 250 LEU   B O    1 
ATOM   240  C CB   . LEU   A 1 35  ? -37.668 -19.707 20.101 1.00 44.71  ? 250 LEU   B CB   1 
ATOM   241  C CG   . LEU   A 1 35  ? -38.182 -19.558 21.538 1.00 47.47  ? 250 LEU   B CG   1 
ATOM   242  C CD1  . LEU   A 1 35  ? -37.801 -20.768 22.330 1.00 46.26  ? 250 LEU   B CD1  1 
ATOM   243  C CD2  . LEU   A 1 35  ? -37.598 -18.311 22.176 1.00 46.59  ? 250 LEU   B CD2  1 
ATOM   244  N N    . PHE   A 1 36  ? -37.147 -17.666 17.346 1.00 48.24  ? 251 PHE   B N    1 
ATOM   245  C CA   . PHE   A 1 36  ? -36.257 -17.582 16.198 1.00 51.82  ? 251 PHE   B CA   1 
ATOM   246  C C    . PHE   A 1 36  ? -34.850 -18.033 16.568 1.00 51.02  ? 251 PHE   B C    1 
ATOM   247  O O    . PHE   A 1 36  ? -34.188 -18.759 15.803 1.00 48.36  ? 251 PHE   B O    1 
ATOM   248  C CB   . PHE   A 1 36  ? -36.241 -16.149 15.673 1.00 48.61  ? 251 PHE   B CB   1 
ATOM   249  C CG   . PHE   A 1 36  ? -37.601 -15.618 15.294 1.00 50.41  ? 251 PHE   B CG   1 
ATOM   250  C CD1  . PHE   A 1 36  ? -38.222 -16.029 14.109 1.00 47.30  ? 251 PHE   B CD1  1 
ATOM   251  C CD2  . PHE   A 1 36  ? -38.238 -14.680 16.097 1.00 41.17  ? 251 PHE   B CD2  1 
ATOM   252  C CE1  . PHE   A 1 36  ? -39.467 -15.532 13.749 1.00 47.91  ? 251 PHE   B CE1  1 
ATOM   253  C CE2  . PHE   A 1 36  ? -39.469 -14.173 15.746 1.00 40.71  ? 251 PHE   B CE2  1 
ATOM   254  C CZ   . PHE   A 1 36  ? -40.090 -14.598 14.565 1.00 55.57  ? 251 PHE   B CZ   1 
ATOM   255  N N    . VAL   A 1 37  ? -34.384 -17.590 17.732 1.00 45.84  ? 252 VAL   B N    1 
ATOM   256  C CA   . VAL   A 1 37  ? -33.077 -17.928 18.279 1.00 47.63  ? 252 VAL   B CA   1 
ATOM   257  C C    . VAL   A 1 37  ? -33.198 -17.911 19.791 1.00 48.33  ? 252 VAL   B C    1 
ATOM   258  O O    . VAL   A 1 37  ? -33.917 -17.077 20.351 1.00 47.28  ? 252 VAL   B O    1 
ATOM   259  C CB   . VAL   A 1 37  ? -32.013 -16.933 17.796 1.00 45.71  ? 252 VAL   B CB   1 
ATOM   260  C CG1  . VAL   A 1 37  ? -31.817 -17.089 16.304 1.00 46.14  ? 252 VAL   B CG1  1 
ATOM   261  C CG2  . VAL   A 1 37  ? -32.493 -15.555 18.110 1.00 48.89  ? 252 VAL   B CG2  1 
ATOM   262  N N    . HIS   A 1 38  ? -32.489 -18.828 20.452 1.00 48.60  ? 253 HIS   B N    1 
ATOM   263  C CA   . HIS   A 1 38  ? -32.624 -19.008 21.894 1.00 50.07  ? 253 HIS   B CA   1 
ATOM   264  C C    . HIS   A 1 38  ? -31.308 -19.479 22.476 1.00 50.24  ? 253 HIS   B C    1 
ATOM   265  O O    . HIS   A 1 38  ? -30.879 -20.588 22.179 1.00 50.15  ? 253 HIS   B O    1 
ATOM   266  C CB   . HIS   A 1 38  ? -33.723 -20.035 22.218 1.00 47.81  ? 253 HIS   B CB   1 
ATOM   267  C CG   . HIS   A 1 38  ? -33.987 -20.215 23.688 1.00 54.49  ? 253 HIS   B CG   1 
ATOM   268  N ND1  . HIS   A 1 38  ? -33.665 -21.368 24.375 1.00 58.84  ? 253 HIS   B ND1  1 
ATOM   269  C CD2  . HIS   A 1 38  ? -34.507 -19.369 24.613 1.00 54.03  ? 253 HIS   B CD2  1 
ATOM   270  C CE1  . HIS   A 1 38  ? -34.014 -21.245 25.644 1.00 54.13  ? 253 HIS   B CE1  1 
ATOM   271  N NE2  . HIS   A 1 38  ? -34.519 -20.036 25.817 1.00 54.91  ? 253 HIS   B NE2  1 
ATOM   272  N N    . ILE   A 1 39  ? -30.711 -18.698 23.363 1.00 52.62  ? 254 ILE   B N    1 
ATOM   273  C CA   . ILE   A 1 39  ? -29.643 -19.209 24.218 1.00 50.65  ? 254 ILE   B CA   1 
ATOM   274  C C    . ILE   A 1 39  ? -30.185 -19.386 25.627 1.00 56.51  ? 254 ILE   B C    1 
ATOM   275  O O    . ILE   A 1 39  ? -30.880 -18.509 26.171 1.00 57.71  ? 254 ILE   B O    1 
ATOM   276  C CB   . ILE   A 1 39  ? -28.411 -18.283 24.205 1.00 52.62  ? 254 ILE   B CB   1 
ATOM   277  C CG1  . ILE   A 1 39  ? -28.081 -17.841 22.767 1.00 50.99  ? 254 ILE   B CG1  1 
ATOM   278  C CG2  . ILE   A 1 39  ? -27.225 -18.997 24.820 1.00 53.06  ? 254 ILE   B CG2  1 
ATOM   279  C CD1  . ILE   A 1 39  ? -26.757 -17.076 22.631 1.00 48.42  ? 254 ILE   B CD1  1 
ATOM   280  N N    . SER   A 1 40  ? -29.867 -20.520 26.233 1.00 62.50  ? 255 SER   B N    1 
ATOM   281  C CA   . SER   A 1 40  ? -30.269 -20.786 27.607 1.00 62.10  ? 255 SER   B CA   1 
ATOM   282  C C    . SER   A 1 40  ? -29.060 -21.358 28.329 1.00 65.12  ? 255 SER   B C    1 
ATOM   283  O O    . SER   A 1 40  ? -28.641 -22.484 28.041 1.00 65.70  ? 255 SER   B O    1 
ATOM   284  C CB   . SER   A 1 40  ? -31.457 -21.747 27.657 1.00 63.48  ? 255 SER   B CB   1 
ATOM   285  O OG   . SER   A 1 40  ? -31.785 -22.078 28.999 1.00 77.55  ? 255 SER   B OG   1 
ATOM   286  N N    . GLN   A 1 41  ? -28.491 -20.584 29.251 1.00 66.90  ? 256 GLN   B N    1 
ATOM   287  C CA   . GLN   A 1 41  ? -27.372 -21.073 30.047 1.00 71.50  ? 256 GLN   B CA   1 
ATOM   288  C C    . GLN   A 1 41  ? -27.790 -21.183 31.514 1.00 77.06  ? 256 GLN   B C    1 
ATOM   289  O O    . GLN   A 1 41  ? -27.145 -20.610 32.397 1.00 74.48  ? 256 GLN   B O    1 
ATOM   290  C CB   . GLN   A 1 41  ? -26.152 -20.158 29.864 1.00 65.76  ? 256 GLN   B CB   1 
ATOM   291  C CG   . GLN   A 1 41  ? -25.820 -19.894 28.384 1.00 67.11  ? 256 GLN   B CG   1 
ATOM   292  C CD   . GLN   A 1 41  ? -24.451 -19.254 28.143 1.00 64.07  ? 256 GLN   B CD   1 
ATOM   293  O OE1  . GLN   A 1 41  ? -23.572 -19.867 27.530 1.00 64.71  ? 256 GLN   B OE1  1 
ATOM   294  N NE2  . GLN   A 1 41  ? -24.277 -18.015 28.593 1.00 59.77  ? 256 GLN   B NE2  1 
ATOM   295  N N    . HIS   A 1 42  ? -28.870 -21.922 31.780 1.00 87.67  ? 257 HIS   B N    1 
ATOM   296  C CA   . HIS   A 1 42  ? -29.360 -22.158 33.150 1.00 92.44  ? 257 HIS   B CA   1 
ATOM   297  C C    . HIS   A 1 42  ? -28.577 -23.259 33.861 1.00 96.53  ? 257 HIS   B C    1 
ATOM   298  O O    . HIS   A 1 42  ? -29.026 -24.401 33.945 1.00 99.25  ? 257 HIS   B O    1 
ATOM   299  C CB   . HIS   A 1 42  ? -30.847 -22.517 33.118 1.00 94.09  ? 257 HIS   B CB   1 
ATOM   300  C CG   . HIS   A 1 42  ? -31.735 -21.369 32.744 1.00 96.85  ? 257 HIS   B CG   1 
ATOM   301  N ND1  . HIS   A 1 42  ? -32.289 -20.516 33.677 1.00 96.05  ? 257 HIS   B ND1  1 
ATOM   302  C CD2  . HIS   A 1 42  ? -32.108 -20.892 31.530 1.00 89.45  ? 257 HIS   B CD2  1 
ATOM   303  C CE1  . HIS   A 1 42  ? -33.004 -19.592 33.057 1.00 92.48  ? 257 HIS   B CE1  1 
ATOM   304  N NE2  . HIS   A 1 42  ? -32.906 -19.795 31.753 1.00 91.59  ? 257 HIS   B NE2  1 
ATOM   305  N N    . PRO   A 1 49  ? -15.291 -28.457 28.970 1.00 110.37 ? 264 PRO   B N    1 
ATOM   306  C CA   . PRO   A 1 49  ? -14.389 -27.985 27.918 1.00 109.41 ? 264 PRO   B CA   1 
ATOM   307  C C    . PRO   A 1 49  ? -14.596 -26.519 27.658 1.00 105.20 ? 264 PRO   B C    1 
ATOM   308  O O    . PRO   A 1 49  ? -15.686 -26.026 27.919 1.00 102.43 ? 264 PRO   B O    1 
ATOM   309  C CB   . PRO   A 1 49  ? -14.833 -28.779 26.692 1.00 110.68 ? 264 PRO   B CB   1 
ATOM   310  C CG   . PRO   A 1 49  ? -16.258 -29.095 26.946 1.00 116.24 ? 264 PRO   B CG   1 
ATOM   311  C CD   . PRO   A 1 49  ? -16.409 -29.243 28.432 1.00 115.31 ? 264 PRO   B CD   1 
ATOM   312  N N    . PRO   A 1 50  ? -13.578 -25.836 27.143 1.00 105.68 ? 265 PRO   B N    1 
ATOM   313  C CA   . PRO   A 1 50  ? -13.713 -24.428 26.758 1.00 100.48 ? 265 PRO   B CA   1 
ATOM   314  C C    . PRO   A 1 50  ? -14.312 -24.325 25.361 1.00 96.78  ? 265 PRO   B C    1 
ATOM   315  O O    . PRO   A 1 50  ? -14.235 -25.289 24.600 1.00 96.97  ? 265 PRO   B O    1 
ATOM   316  C CB   . PRO   A 1 50  ? -12.267 -23.932 26.750 1.00 100.20 ? 265 PRO   B CB   1 
ATOM   317  C CG   . PRO   A 1 50  ? -11.571 -24.805 27.738 1.00 102.30 ? 265 PRO   B CG   1 
ATOM   318  C CD   . PRO   A 1 50  ? -12.222 -26.154 27.622 1.00 104.82 ? 265 PRO   B CD   1 
ATOM   319  N N    . LEU   A 1 51  ? -14.904 -23.182 25.027 1.00 90.90  ? 266 LEU   B N    1 
ATOM   320  C CA   . LEU   A 1 51  ? -15.533 -23.032 23.747 1.00 84.51  ? 266 LEU   B CA   1 
ATOM   321  C C    . LEU   A 1 51  ? -14.461 -22.990 22.694 1.00 86.11  ? 266 LEU   B C    1 
ATOM   322  O O    . LEU   A 1 51  ? -13.292 -22.892 23.004 1.00 89.09  ? 266 LEU   B O    1 
ATOM   323  C CB   . LEU   A 1 51  ? -16.342 -21.751 23.717 1.00 77.54  ? 266 LEU   B CB   1 
ATOM   324  C CG   . LEU   A 1 51  ? -17.303 -21.593 24.875 1.00 74.39  ? 266 LEU   B CG   1 
ATOM   325  C CD1  . LEU   A 1 51  ? -17.601 -20.140 25.102 1.00 69.02  ? 266 LEU   B CD1  1 
ATOM   326  C CD2  . LEU   A 1 51  ? -18.579 -22.321 24.553 1.00 68.94  ? 266 LEU   B CD2  1 
ATOM   327  N N    . GLU   A 1 52  ? -14.875 -23.055 21.443 1.00 79.94  ? 267 GLU   B N    1 
ATOM   328  C CA   . GLU   A 1 52  ? -13.937 -22.984 20.319 1.00 81.17  ? 267 GLU   B CA   1 
ATOM   329  C C    . GLU   A 1 52  ? -13.521 -21.536 20.065 1.00 78.09  ? 267 GLU   B C    1 
ATOM   330  O O    . GLU   A 1 52  ? -14.200 -20.595 20.463 1.00 75.98  ? 267 GLU   B O    1 
ATOM   331  C CB   . GLU   A 1 52  ? -14.536 -23.588 19.035 1.00 81.62  ? 267 GLU   B CB   1 
ATOM   332  C CG   . GLU   A 1 52  ? -14.832 -25.081 19.145 1.00 83.85  ? 267 GLU   B CG   1 
ATOM   333  C CD   . GLU   A 1 52  ? -15.172 -25.717 17.795 1.00 90.38  ? 267 GLU   B CD   1 
ATOM   334  O OE1  . GLU   A 1 52  ? -14.520 -25.384 16.770 1.00 93.82  ? 267 GLU   B OE1  1 
ATOM   335  O OE2  . GLU   A 1 52  ? -16.098 -26.556 17.758 1.00 92.71  ? 267 GLU   B OE2  1 
ATOM   336  N N    . SER   A 1 53  ? -12.387 -21.368 19.394 1.00 84.62  ? 268 SER   B N    1 
ATOM   337  C CA   . SER   A 1 53  ? -11.892 -20.053 19.024 1.00 84.45  ? 268 SER   B CA   1 
ATOM   338  C C    . SER   A 1 53  ? -12.313 -19.702 17.608 1.00 83.75  ? 268 SER   B C    1 
ATOM   339  O O    . SER   A 1 53  ? -12.505 -20.574 16.756 1.00 85.84  ? 268 SER   B O    1 
ATOM   340  C CB   . SER   A 1 53  ? -10.370 -19.994 19.114 1.00 89.86  ? 268 SER   B CB   1 
ATOM   341  O OG   . SER   A 1 53  ? -9.885  -20.763 20.197 1.00 95.12  ? 268 SER   B OG   1 
ATOM   342  N N    . VAL   A 1 54  ? -12.455 -18.405 17.372 1.00 77.01  ? 269 VAL   B N    1 
ATOM   343  C CA   . VAL   A 1 54  ? -12.523 -17.841 16.034 1.00 75.06  ? 269 VAL   B CA   1 
ATOM   344  C C    . VAL   A 1 54  ? -11.765 -16.523 16.063 1.00 80.63  ? 269 VAL   B C    1 
ATOM   345  O O    . VAL   A 1 54  ? -11.934 -15.717 16.987 1.00 78.09  ? 269 VAL   B O    1 
ATOM   346  C CB   . VAL   A 1 54  ? -13.967 -17.624 15.552 1.00 70.12  ? 269 VAL   B CB   1 
ATOM   347  C CG1  . VAL   A 1 54  ? -13.958 -16.865 14.234 1.00 72.52  ? 269 VAL   B CG1  1 
ATOM   348  C CG2  . VAL   A 1 54  ? -14.685 -18.945 15.430 1.00 70.87  ? 269 VAL   B CG2  1 
ATOM   349  N N    . ASP   A 1 55  ? -10.925 -16.307 15.056 1.00 75.82  ? 270 ASP   B N    1 
ATOM   350  C CA   . ASP   A 1 55  ? -10.068 -15.133 15.031 1.00 80.08  ? 270 ASP   B CA   1 
ATOM   351  C C    . ASP   A 1 55  ? -10.875 -13.907 14.624 1.00 80.96  ? 270 ASP   B C    1 
ATOM   352  O O    . ASP   A 1 55  ? -11.581 -13.918 13.610 1.00 77.55  ? 270 ASP   B O    1 
ATOM   353  C CB   . ASP   A 1 55  ? -8.894  -15.347 14.080 1.00 81.49  ? 270 ASP   B CB   1 
ATOM   354  C CG   . ASP   A 1 55  ? -8.030  -14.116 13.947 1.00 90.23  ? 270 ASP   B CG   1 
ATOM   355  O OD1  . ASP   A 1 55  ? -8.502  -13.132 13.339 1.00 92.23  ? 270 ASP   B OD1  1 
ATOM   356  O OD2  . ASP   A 1 55  ? -6.890  -14.123 14.467 1.00 92.54  ? 270 ASP   B OD2  1 
ATOM   357  N N    . VAL   A 1 56  ? -10.767 -12.846 15.427 1.00 84.71  ? 271 VAL   B N    1 
ATOM   358  C CA   . VAL   A 1 56  ? -11.622 -11.682 15.234 1.00 84.55  ? 271 VAL   B CA   1 
ATOM   359  C C    . VAL   A 1 56  ? -11.378 -11.049 13.866 1.00 89.32  ? 271 VAL   B C    1 
ATOM   360  O O    . VAL   A 1 56  ? -12.303 -10.498 13.256 1.00 88.90  ? 271 VAL   B O    1 
ATOM   361  C CB   . VAL   A 1 56  ? -11.410 -10.687 16.400 1.00 82.89  ? 271 VAL   B CB   1 
ATOM   362  C CG1  . VAL   A 1 56  ? -9.925  -10.425 16.641 1.00 87.61  ? 271 VAL   B CG1  1 
ATOM   363  C CG2  . VAL   A 1 56  ? -12.190 -9.403  16.190 1.00 83.42  ? 271 VAL   B CG2  1 
ATOM   364  N N    . ARG   A 1 57  ? -10.147 -11.143 13.348 1.00 86.57  ? 272 ARG   B N    1 
ATOM   365  C CA   . ARG   A 1 57  ? -9.840  -10.586 12.029 1.00 91.79  ? 272 ARG   B CA   1 
ATOM   366  C C    . ARG   A 1 57  ? -10.781 -11.128 10.951 1.00 91.10  ? 272 ARG   B C    1 
ATOM   367  O O    . ARG   A 1 57  ? -11.095 -10.422 9.985  1.00 93.93  ? 272 ARG   B O    1 
ATOM   368  C CB   . ARG   A 1 57  ? -8.374  -10.876 11.654 1.00 92.76  ? 272 ARG   B CB   1 
ATOM   369  C CG   . ARG   A 1 57  ? -7.322  -10.462 12.710 1.00 95.93  ? 272 ARG   B CG   1 
ATOM   370  C CD   . ARG   A 1 57  ? -5.896  -10.899 12.328 1.00 100.52 ? 272 ARG   B CD   1 
ATOM   371  N NE   . ARG   A 1 57  ? -5.150  -11.500 13.433 1.00 102.01 ? 272 ARG   B NE   1 
ATOM   372  C CZ   . ARG   A 1 57  ? -4.204  -10.887 14.137 1.00 105.85 ? 272 ARG   B CZ   1 
ATOM   373  N NH1  . ARG   A 1 57  ? -3.862  -9.633  13.894 1.00 109.69 ? 272 ARG   B NH1  1 
ATOM   374  N NH2  . ARG   A 1 57  ? -3.584  -11.550 15.111 1.00 106.96 ? 272 ARG   B NH2  1 
ATOM   375  N N    . GLN   A 1 58  ? -11.240 -12.374 11.107 1.00 90.88  ? 273 GLN   B N    1 
ATOM   376  C CA   . GLN   A 1 58  ? -12.162 -13.003 10.161 1.00 91.26  ? 273 GLN   B CA   1 
ATOM   377  C C    . GLN   A 1 58  ? -13.469 -12.228 9.991  1.00 91.59  ? 273 GLN   B C    1 
ATOM   378  O O    . GLN   A 1 58  ? -14.070 -12.264 8.909  1.00 97.53  ? 273 GLN   B O    1 
ATOM   379  C CB   . GLN   A 1 58  ? -12.496 -14.415 10.642 1.00 89.83  ? 273 GLN   B CB   1 
ATOM   380  C CG   . GLN   A 1 58  ? -11.594 -15.510 10.158 1.00 92.92  ? 273 GLN   B CG   1 
ATOM   381  C CD   . GLN   A 1 58  ? -12.264 -16.857 10.318 1.00 96.58  ? 273 GLN   B CD   1 
ATOM   382  O OE1  . GLN   A 1 58  ? -13.488 -16.939 10.426 1.00 95.73  ? 273 GLN   B OE1  1 
ATOM   383  N NE2  . GLN   A 1 58  ? -11.470 -17.921 10.328 1.00 103.88 ? 273 GLN   B NE2  1 
ATOM   384  N N    . ILE   A 1 59  ? -13.953 -11.565 11.042 1.00 91.73  ? 274 ILE   B N    1 
ATOM   385  C CA   . ILE   A 1 59  ? -15.293 -10.992 11.034 1.00 89.50  ? 274 ILE   B CA   1 
ATOM   386  C C    . ILE   A 1 59  ? -15.270 -9.467  11.078 1.00 90.94  ? 274 ILE   B C    1 
ATOM   387  O O    . ILE   A 1 59  ? -16.316 -8.842  11.293 1.00 90.52  ? 274 ILE   B O    1 
ATOM   388  C CB   . ILE   A 1 59  ? -16.151 -11.556 12.179 1.00 84.88  ? 274 ILE   B CB   1 
ATOM   389  C CG1  . ILE   A 1 59  ? -15.504 -11.264 13.533 1.00 82.00  ? 274 ILE   B CG1  1 
ATOM   390  C CG2  . ILE   A 1 59  ? -16.353 -13.052 12.010 1.00 78.23  ? 274 ILE   B CG2  1 
ATOM   391  C CD1  . ILE   A 1 59  ? -16.018 -12.138 14.661 1.00 74.05  ? 274 ILE   B CD1  1 
ATOM   392  N N    . TYR   A 1 60  ? -14.104 -8.844  10.886 1.00 91.52  ? 275 TYR   B N    1 
ATOM   393  C CA   . TYR   A 1 60  ? -14.048 -7.383  10.818 1.00 95.48  ? 275 TYR   B CA   1 
ATOM   394  C C    . TYR   A 1 60  ? -14.981 -6.848  9.731  1.00 95.97  ? 275 TYR   B C    1 
ATOM   395  O O    . TYR   A 1 60  ? -15.840 -5.998  9.994  1.00 93.59  ? 275 TYR   B O    1 
ATOM   396  C CB   . TYR   A 1 60  ? -12.608 -6.911  10.562 1.00 97.66  ? 275 TYR   B CB   1 
ATOM   397  C CG   . TYR   A 1 60  ? -11.666 -6.998  11.756 1.00 97.17  ? 275 TYR   B CG   1 
ATOM   398  C CD1  . TYR   A 1 60  ? -12.157 -7.097  13.057 1.00 93.47  ? 275 TYR   B CD1  1 
ATOM   399  C CD2  . TYR   A 1 60  ? -10.282 -6.988  11.575 1.00 99.94  ? 275 TYR   B CD2  1 
ATOM   400  C CE1  . TYR   A 1 60  ? -11.294 -7.177  14.149 1.00 92.65  ? 275 TYR   B CE1  1 
ATOM   401  C CE2  . TYR   A 1 60  ? -9.412  -7.074  12.657 1.00 101.16 ? 275 TYR   B CE2  1 
ATOM   402  C CZ   . TYR   A 1 60  ? -9.924  -7.168  13.946 1.00 96.53  ? 275 TYR   B CZ   1 
ATOM   403  O OH   . TYR   A 1 60  ? -9.074  -7.252  15.033 1.00 98.25  ? 275 TYR   B OH   1 
ATOM   404  N N    . ASP   A 1 61  ? -14.830 -7.344  8.499  1.00 98.83  ? 276 ASP   B N    1 
ATOM   405  C CA   . ASP   A 1 61  ? -15.583 -6.827  7.361  1.00 97.96  ? 276 ASP   B CA   1 
ATOM   406  C C    . ASP   A 1 61  ? -17.077 -7.127  7.426  1.00 96.46  ? 276 ASP   B C    1 
ATOM   407  O O    . ASP   A 1 61  ? -17.800 -6.745  6.494  1.00 96.00  ? 276 ASP   B O    1 
ATOM   408  C CB   . ASP   A 1 61  ? -15.006 -7.377  6.055  1.00 102.01 ? 276 ASP   B CB   1 
ATOM   409  C CG   . ASP   A 1 61  ? -14.982 -8.901  6.008  1.00 103.95 ? 276 ASP   B CG   1 
ATOM   410  O OD1  . ASP   A 1 61  ? -15.499 -9.563  6.935  1.00 98.84  ? 276 ASP   B OD1  1 
ATOM   411  O OD2  . ASP   A 1 61  ? -14.418 -9.437  5.024  1.00 112.97 ? 276 ASP   B OD2  1 
ATOM   412  N N    . LYS   A 1 62  ? -17.560 -7.795  8.472  1.00 90.75  ? 277 LYS   B N    1 
ATOM   413  C CA   . LYS   A 1 62  ? -18.988 -8.030  8.650  1.00 86.55  ? 277 LYS   B CA   1 
ATOM   414  C C    . LYS   A 1 62  ? -19.655 -7.014  9.571  1.00 80.08  ? 277 LYS   B C    1 
ATOM   415  O O    . LYS   A 1 62  ? -20.880 -7.056  9.728  1.00 73.55  ? 277 LYS   B O    1 
ATOM   416  C CB   . LYS   A 1 62  ? -19.225 -9.445  9.183  1.00 84.19  ? 277 LYS   B CB   1 
ATOM   417  C CG   . LYS   A 1 62  ? -18.290 -10.485 8.582  1.00 87.01  ? 277 LYS   B CG   1 
ATOM   418  C CD   . LYS   A 1 62  ? -18.853 -11.884 8.810  1.00 84.36  ? 277 LYS   B CD   1 
ATOM   419  C CE   . LYS   A 1 62  ? -20.043 -12.138 7.900  1.00 81.57  ? 277 LYS   B CE   1 
ATOM   420  N NZ   . LYS   A 1 62  ? -19.608 -12.335 6.488  1.00 77.81  ? 277 LYS   B NZ   1 
ATOM   421  N N    . PHE   A 1 63  ? -18.886 -6.094  10.162 1.00 82.86  ? 278 PHE   B N    1 
ATOM   422  C CA   . PHE   A 1 63  ? -19.427 -5.133  11.116 1.00 84.88  ? 278 PHE   B CA   1 
ATOM   423  C C    . PHE   A 1 63  ? -18.933 -3.728  10.798 1.00 88.31  ? 278 PHE   B C    1 
ATOM   424  O O    . PHE   A 1 63  ? -18.061 -3.558  9.936  1.00 92.58  ? 278 PHE   B O    1 
ATOM   425  C CB   . PHE   A 1 63  ? -19.053 -5.548  12.545 1.00 81.76  ? 278 PHE   B CB   1 
ATOM   426  C CG   . PHE   A 1 63  ? -19.586 -6.894  12.927 1.00 74.68  ? 278 PHE   B CG   1 
ATOM   427  C CD1  . PHE   A 1 63  ? -18.970 -8.057  12.478 1.00 76.39  ? 278 PHE   B CD1  1 
ATOM   428  C CD2  . PHE   A 1 63  ? -20.730 -6.999  13.692 1.00 64.50  ? 278 PHE   B CD2  1 
ATOM   429  C CE1  . PHE   A 1 63  ? -19.479 -9.305  12.808 1.00 72.91  ? 278 PHE   B CE1  1 
ATOM   430  C CE2  . PHE   A 1 63  ? -21.244 -8.234  14.021 1.00 59.59  ? 278 PHE   B CE2  1 
ATOM   431  C CZ   . PHE   A 1 63  ? -20.622 -9.394  13.573 1.00 61.55  ? 278 PHE   B CZ   1 
ATOM   432  N N    . PRO   A 1 64  ? -19.455 -2.699  11.462 1.00 91.54  ? 279 PRO   B N    1 
ATOM   433  C CA   . PRO   A 1 64  ? -18.999 -1.330  11.165 1.00 97.50  ? 279 PRO   B CA   1 
ATOM   434  C C    . PRO   A 1 64  ? -17.500 -1.208  11.408 1.00 101.53 ? 279 PRO   B C    1 
ATOM   435  O O    . PRO   A 1 64  ? -16.854 -2.110  11.948 1.00 101.70 ? 279 PRO   B O    1 
ATOM   436  C CB   . PRO   A 1 64  ? -19.808 -0.443  12.124 1.00 96.48  ? 279 PRO   B CB   1 
ATOM   437  C CG   . PRO   A 1 64  ? -20.765 -1.379  12.881 1.00 89.16  ? 279 PRO   B CG   1 
ATOM   438  C CD   . PRO   A 1 64  ? -20.291 -2.781  12.678 1.00 87.16  ? 279 PRO   B CD   1 
ATOM   439  N N    . GLU   A 1 65  ? -16.937 -0.072  11.003 1.00 107.53 ? 280 GLU   B N    1 
ATOM   440  C CA   . GLU   A 1 65  ? -15.498 0.154   11.104 1.00 114.93 ? 280 GLU   B CA   1 
ATOM   441  C C    . GLU   A 1 65  ? -15.202 1.245   12.127 1.00 119.52 ? 280 GLU   B C    1 
ATOM   442  O O    . GLU   A 1 65  ? -15.620 2.397   11.955 1.00 118.39 ? 280 GLU   B O    1 
ATOM   443  C CB   . GLU   A 1 65  ? -14.906 0.513   9.743  1.00 115.40 ? 280 GLU   B CB   1 
ATOM   444  C CG   . GLU   A 1 65  ? -14.653 -0.712  8.885  1.00 116.50 ? 280 GLU   B CG   1 
ATOM   445  C CD   . GLU   A 1 65  ? -13.289 -1.323  9.143  1.00 117.26 ? 280 GLU   B CD   1 
ATOM   446  O OE1  . GLU   A 1 65  ? -12.568 -0.802  10.026 1.00 116.44 ? 280 GLU   B OE1  1 
ATOM   447  O OE2  . GLU   A 1 65  ? -12.949 -2.329  8.478  1.00 116.13 ? 280 GLU   B OE2  1 
ATOM   448  N N    . LYS   A 1 66  ? -14.467 0.879   13.184 1.00 128.15 ? 281 LYS   B N    1 
ATOM   449  C CA   . LYS   A 1 66  ? -14.082 1.820   14.229 1.00 125.45 ? 281 LYS   B CA   1 
ATOM   450  C C    . LYS   A 1 66  ? -15.324 2.470   14.821 1.00 123.21 ? 281 LYS   B C    1 
ATOM   451  O O    . LYS   A 1 66  ? -16.420 1.907   14.731 1.00 120.87 ? 281 LYS   B O    1 
ATOM   452  C CB   . LYS   A 1 66  ? -13.122 2.881   13.677 1.00 125.28 ? 281 LYS   B CB   1 
ATOM   453  N N    . LYS   A 1 67  ? -15.153 3.637   15.450 1.00 120.79 ? 282 LYS   B N    1 
ATOM   454  C CA   . LYS   A 1 67  ? -16.250 4.479   15.926 1.00 117.90 ? 282 LYS   B CA   1 
ATOM   455  C C    . LYS   A 1 67  ? -17.455 3.688   16.431 1.00 113.46 ? 282 LYS   B C    1 
ATOM   456  O O    . LYS   A 1 67  ? -18.593 4.165   16.353 1.00 112.63 ? 282 LYS   B O    1 
ATOM   457  C CB   . LYS   A 1 67  ? -16.684 5.432   14.810 1.00 121.91 ? 282 LYS   B CB   1 
ATOM   458  N N    . GLY   A 1 68  ? -17.221 2.492   16.965 1.00 111.93 ? 283 GLY   B N    1 
ATOM   459  C CA   . GLY   A 1 68  ? -18.305 1.619   17.370 1.00 109.00 ? 283 GLY   B CA   1 
ATOM   460  C C    . GLY   A 1 68  ? -18.192 0.268   16.698 1.00 105.53 ? 283 GLY   B C    1 
ATOM   461  O O    . GLY   A 1 68  ? -19.102 -0.568  16.787 1.00 97.57  ? 283 GLY   B O    1 
ATOM   462  N N    . GLY   A 1 69  ? -17.056 0.049   16.023 1.00 106.56 ? 284 GLY   B N    1 
ATOM   463  C CA   . GLY   A 1 69  ? -16.814 -1.169  15.282 1.00 103.91 ? 284 GLY   B CA   1 
ATOM   464  C C    . GLY   A 1 69  ? -16.011 -2.199  16.068 1.00 102.04 ? 284 GLY   B C    1 
ATOM   465  O O    . GLY   A 1 69  ? -15.453 -1.923  17.127 1.00 102.34 ? 284 GLY   B O    1 
ATOM   466  N N    . LEU   A 1 70  ? -15.942 -3.406  15.496 1.00 92.99  ? 285 LEU   B N    1 
ATOM   467  C CA   . LEU   A 1 70  ? -15.388 -4.543  16.226 1.00 88.74  ? 285 LEU   B CA   1 
ATOM   468  C C    . LEU   A 1 70  ? -13.913 -4.342  16.555 1.00 93.00  ? 285 LEU   B C    1 
ATOM   469  O O    . LEU   A 1 70  ? -13.477 -4.623  17.676 1.00 93.28  ? 285 LEU   B O    1 
ATOM   470  C CB   . LEU   A 1 70  ? -15.589 -5.832  15.432 1.00 84.43  ? 285 LEU   B CB   1 
ATOM   471  C CG   . LEU   A 1 70  ? -15.391 -7.111  16.251 1.00 79.61  ? 285 LEU   B CG   1 
ATOM   472  C CD1  . LEU   A 1 70  ? -16.100 -6.963  17.571 1.00 72.86  ? 285 LEU   B CD1  1 
ATOM   473  C CD2  . LEU   A 1 70  ? -15.884 -8.359  15.516 1.00 76.34  ? 285 LEU   B CD2  1 
ATOM   474  N N    . ARG   A 1 71  ? -13.122 -3.859  15.594 1.00 93.66  ? 286 ARG   B N    1 
ATOM   475  C CA   . ARG   A 1 71  ? -11.679 -3.842  15.816 1.00 95.92  ? 286 ARG   B CA   1 
ATOM   476  C C    . ARG   A 1 71  ? -11.260 -2.716  16.750 1.00 98.47  ? 286 ARG   B C    1 
ATOM   477  O O    . ARG   A 1 71  ? -10.303 -2.877  17.518 1.00 97.78  ? 286 ARG   B O    1 
ATOM   478  C CB   . ARG   A 1 71  ? -10.932 -3.754  14.484 1.00 99.26  ? 286 ARG   B CB   1 
ATOM   479  C CG   . ARG   A 1 71  ? -11.071 -2.432  13.753 1.00 102.83 ? 286 ARG   B CG   1 
ATOM   480  C CD   . ARG   A 1 71  ? -10.131 -2.383  12.552 1.00 103.63 ? 286 ARG   B CD   1 
ATOM   481  N NE   . ARG   A 1 71  ? -10.754 -2.945  11.359 1.00 105.48 ? 286 ARG   B NE   1 
ATOM   482  C CZ   . ARG   A 1 71  ? -10.088 -3.535  10.377 1.00 103.03 ? 286 ARG   B CZ   1 
ATOM   483  N NH1  . ARG   A 1 71  ? -8.773  -3.673  10.422 1.00 98.52  ? 286 ARG   B NH1  1 
ATOM   484  N NH2  . ARG   A 1 71  ? -10.760 -4.011  9.330  1.00 106.30 ? 286 ARG   B NH2  1 
ATOM   485  N N    . GLU   A 1 72  ? -11.947 -1.572  16.699 1.00 98.54  ? 287 GLU   B N    1 
ATOM   486  C CA   . GLU   A 1 72  ? -11.749 -0.555  17.728 1.00 100.14 ? 287 GLU   B CA   1 
ATOM   487  C C    . GLU   A 1 72  ? -12.073 -1.109  19.110 1.00 99.80  ? 287 GLU   B C    1 
ATOM   488  O O    . GLU   A 1 72  ? -11.389 -0.791  20.090 1.00 101.50 ? 287 GLU   B O    1 
ATOM   489  C CB   . GLU   A 1 72  ? -12.619 0.667   17.444 1.00 104.92 ? 287 GLU   B CB   1 
ATOM   490  C CG   . GLU   A 1 72  ? -11.922 1.987   17.649 1.00 108.67 ? 287 GLU   B CG   1 
ATOM   491  C CD   . GLU   A 1 72  ? -10.510 1.986   17.095 1.00 113.59 ? 287 GLU   B CD   1 
ATOM   492  O OE1  . GLU   A 1 72  ? -10.273 1.264   16.100 1.00 115.16 ? 287 GLU   B OE1  1 
ATOM   493  O OE2  . GLU   A 1 72  ? -9.642  2.723   17.626 1.00 111.51 ? 287 GLU   B OE2  1 
ATOM   494  N N    . LEU   A 1 73  ? -13.119 -1.938  19.206 1.00 99.84  ? 288 LEU   B N    1 
ATOM   495  C CA   . LEU   A 1 73  ? -13.527 -2.496  20.493 1.00 96.39  ? 288 LEU   B CA   1 
ATOM   496  C C    . LEU   A 1 73  ? -12.543 -3.549  20.974 1.00 97.10  ? 288 LEU   B C    1 
ATOM   497  O O    . LEU   A 1 73  ? -12.002 -3.459  22.082 1.00 97.69  ? 288 LEU   B O    1 
ATOM   498  C CB   . LEU   A 1 73  ? -14.929 -3.096  20.387 1.00 88.62  ? 288 LEU   B CB   1 
ATOM   499  C CG   . LEU   A 1 73  ? -16.083 -2.101  20.403 1.00 90.52  ? 288 LEU   B CG   1 
ATOM   500  C CD1  . LEU   A 1 73  ? -17.328 -2.715  19.816 1.00 84.90  ? 288 LEU   B CD1  1 
ATOM   501  C CD2  . LEU   A 1 73  ? -16.339 -1.634  21.818 1.00 85.42  ? 288 LEU   B CD2  1 
ATOM   502  N N    . TYR   A 1 74  ? -12.313 -4.574  20.157 1.00 87.33  ? 289 TYR   B N    1 
ATOM   503  C CA   . TYR   A 1 74  ? -11.397 -5.630  20.562 1.00 88.59  ? 289 TYR   B CA   1 
ATOM   504  C C    . TYR   A 1 74  ? -10.025 -5.077  20.916 1.00 98.30  ? 289 TYR   B C    1 
ATOM   505  O O    . TYR   A 1 74  ? -9.322  -5.656  21.753 1.00 100.08 ? 289 TYR   B O    1 
ATOM   506  C CB   . TYR   A 1 74  ? -11.275 -6.673  19.460 1.00 85.18  ? 289 TYR   B CB   1 
ATOM   507  C CG   . TYR   A 1 74  ? -10.583 -7.925  19.912 1.00 82.50  ? 289 TYR   B CG   1 
ATOM   508  C CD1  . TYR   A 1 74  ? -9.197  -8.015  19.912 1.00 87.13  ? 289 TYR   B CD1  1 
ATOM   509  C CD2  . TYR   A 1 74  ? -11.312 -9.018  20.343 1.00 77.21  ? 289 TYR   B CD2  1 
ATOM   510  C CE1  . TYR   A 1 74  ? -8.560  -9.168  20.325 1.00 88.79  ? 289 TYR   B CE1  1 
ATOM   511  C CE2  . TYR   A 1 74  ? -10.689 -10.173 20.758 1.00 77.17  ? 289 TYR   B CE2  1 
ATOM   512  C CZ   . TYR   A 1 74  ? -9.314  -10.246 20.749 1.00 83.55  ? 289 TYR   B CZ   1 
ATOM   513  O OH   . TYR   A 1 74  ? -8.690  -11.402 21.160 1.00 84.68  ? 289 TYR   B OH   1 
ATOM   514  N N    . ASP   A 1 75  ? -9.629  -3.960  20.301 1.00 106.63 ? 290 ASP   B N    1 
ATOM   515  C CA   . ASP   A 1 75  ? -8.347  -3.342  20.610 1.00 104.49 ? 290 ASP   B CA   1 
ATOM   516  C C    . ASP   A 1 75  ? -8.342  -2.611  21.943 1.00 106.35 ? 290 ASP   B C    1 
ATOM   517  O O    . ASP   A 1 75  ? -7.264  -2.367  22.494 1.00 110.57 ? 290 ASP   B O    1 
ATOM   518  C CB   . ASP   A 1 75  ? -7.948  -2.389  19.491 1.00 107.90 ? 290 ASP   B CB   1 
ATOM   519  C CG   . ASP   A 1 75  ? -6.961  -3.012  18.542 1.00 112.98 ? 290 ASP   B CG   1 
ATOM   520  O OD1  . ASP   A 1 75  ? -5.917  -3.508  19.018 1.00 113.29 ? 290 ASP   B OD1  1 
ATOM   521  O OD2  . ASP   A 1 75  ? -7.244  -3.042  17.329 1.00 114.92 ? 290 ASP   B OD2  1 
ATOM   522  N N    . ARG   A 1 76  ? -9.507  -2.254  22.471 1.00 116.84 ? 291 ARG   B N    1 
ATOM   523  C CA   . ARG   A 1 76  ? -9.602  -1.726  23.824 1.00 117.52 ? 291 ARG   B CA   1 
ATOM   524  C C    . ARG   A 1 76  ? -9.862  -2.820  24.856 1.00 114.35 ? 291 ARG   B C    1 
ATOM   525  O O    . ARG   A 1 76  ? -9.982  -2.514  26.049 1.00 113.61 ? 291 ARG   B O    1 
ATOM   526  C CB   . ARG   A 1 76  ? -10.688 -0.645  23.888 1.00 116.50 ? 291 ARG   B CB   1 
ATOM   527  C CG   . ARG   A 1 76  ? -10.427 0.508   22.917 1.00 121.05 ? 291 ARG   B CG   1 
ATOM   528  C CD   . ARG   A 1 76  ? -11.333 1.707   23.161 1.00 124.77 ? 291 ARG   B CD   1 
ATOM   529  N NE   . ARG   A 1 76  ? -12.648 1.324   23.663 1.00 126.24 ? 291 ARG   B NE   1 
ATOM   530  C CZ   . ARG   A 1 76  ? -13.756 1.312   22.933 1.00 123.55 ? 291 ARG   B CZ   1 
ATOM   531  N NH1  . ARG   A 1 76  ? -13.742 1.638   21.649 1.00 121.83 ? 291 ARG   B NH1  1 
ATOM   532  N NH2  . ARG   A 1 76  ? -14.907 0.970   23.506 1.00 118.63 ? 291 ARG   B NH2  1 
ATOM   533  N N    . GLY   A 1 77  ? -9.937  -4.081  24.421 1.00 101.72 ? 292 GLY   B N    1 
ATOM   534  C CA   . GLY   A 1 77  ? -10.033 -5.213  25.314 1.00 93.13  ? 292 GLY   B CA   1 
ATOM   535  C C    . GLY   A 1 77  ? -11.234 -5.142  26.225 1.00 88.27  ? 292 GLY   B C    1 
ATOM   536  O O    . GLY   A 1 77  ? -12.071 -4.241  26.119 1.00 87.62  ? 292 GLY   B O    1 
ATOM   537  N N    . PRO   A 1 78  ? -11.344 -6.105  27.149 1.00 80.82  ? 293 PRO   B N    1 
ATOM   538  C CA   . PRO   A 1 78  ? -10.445 -7.253  27.342 1.00 76.48  ? 293 PRO   B CA   1 
ATOM   539  C C    . PRO   A 1 78  ? -10.831 -8.422  26.451 1.00 74.04  ? 293 PRO   B C    1 
ATOM   540  O O    . PRO   A 1 78  ? -12.012 -8.759  26.378 1.00 71.49  ? 293 PRO   B O    1 
ATOM   541  C CB   . PRO   A 1 78  ? -10.619 -7.592  28.830 1.00 74.33  ? 293 PRO   B CB   1 
ATOM   542  C CG   . PRO   A 1 78  ? -11.946 -6.993  29.253 1.00 73.58  ? 293 PRO   B CG   1 
ATOM   543  C CD   . PRO   A 1 78  ? -12.411 -6.048  28.168 1.00 75.71  ? 293 PRO   B CD   1 
ATOM   544  N N    . PRO   A 1 79  ? -9.854  -9.066  25.800 1.00 73.65  ? 294 PRO   B N    1 
ATOM   545  C CA   . PRO   A 1 79  ? -10.182 -10.090 24.791 1.00 71.62  ? 294 PRO   B CA   1 
ATOM   546  C C    . PRO   A 1 79  ? -11.074 -11.198 25.298 1.00 69.52  ? 294 PRO   B C    1 
ATOM   547  O O    . PRO   A 1 79  ? -11.722 -11.864 24.480 1.00 70.39  ? 294 PRO   B O    1 
ATOM   548  C CB   . PRO   A 1 79  ? -8.809  -10.643 24.380 1.00 74.40  ? 294 PRO   B CB   1 
ATOM   549  C CG   . PRO   A 1 79  ? -7.892  -10.278 25.505 1.00 75.36  ? 294 PRO   B CG   1 
ATOM   550  C CD   . PRO   A 1 79  ? -8.409  -8.986  26.063 1.00 75.43  ? 294 PRO   B CD   1 
ATOM   551  N N    . HIS   A 1 80  ? -11.109 -11.447 26.609 1.00 70.95  ? 295 HIS   B N    1 
ATOM   552  C CA   . HIS   A 1 80  ? -11.954 -12.505 27.145 1.00 65.56  ? 295 HIS   B CA   1 
ATOM   553  C C    . HIS   A 1 80  ? -13.415 -12.105 27.203 1.00 62.77  ? 295 HIS   B C    1 
ATOM   554  O O    . HIS   A 1 80  ? -14.262 -12.946 27.512 1.00 60.15  ? 295 HIS   B O    1 
ATOM   555  C CB   . HIS   A 1 80  ? -11.469 -12.916 28.536 1.00 69.64  ? 295 HIS   B CB   1 
ATOM   556  C CG   . HIS   A 1 80  ? -11.740 -11.894 29.595 1.00 70.09  ? 295 HIS   B CG   1 
ATOM   557  N ND1  . HIS   A 1 80  ? -11.130 -10.659 29.611 1.00 72.90  ? 295 HIS   B ND1  1 
ATOM   558  C CD2  . HIS   A 1 80  ? -12.563 -11.920 30.669 1.00 70.36  ? 295 HIS   B CD2  1 
ATOM   559  C CE1  . HIS   A 1 80  ? -11.566 -9.968  30.650 1.00 72.53  ? 295 HIS   B CE1  1 
ATOM   560  N NE2  . HIS   A 1 80  ? -12.433 -10.712 31.311 1.00 72.06  ? 295 HIS   B NE2  1 
ATOM   561  N N    . ALA   A 1 81  ? -13.723 -10.852 26.892 1.00 65.69  ? 296 ALA   B N    1 
ATOM   562  C CA   . ALA   A 1 81  ? -15.084 -10.347 26.840 1.00 61.74  ? 296 ALA   B CA   1 
ATOM   563  C C    . ALA   A 1 81  ? -15.796 -10.606 25.515 1.00 61.63  ? 296 ALA   B C    1 
ATOM   564  O O    . ALA   A 1 81  ? -17.019 -10.428 25.460 1.00 60.41  ? 296 ALA   B O    1 
ATOM   565  C CB   . ALA   A 1 81  ? -15.075 -8.843  27.100 1.00 65.10  ? 296 ALA   B CB   1 
ATOM   566  N N    . PHE   A 1 82  ? -15.082 -10.998 24.452 1.00 62.72  ? 297 PHE   B N    1 
ATOM   567  C CA   . PHE   A 1 82  ? -15.637 -11.036 23.101 1.00 60.37  ? 297 PHE   B CA   1 
ATOM   568  C C    . PHE   A 1 82  ? -16.009 -12.454 22.685 1.00 59.20  ? 297 PHE   B C    1 
ATOM   569  O O    . PHE   A 1 82  ? -15.194 -13.381 22.793 1.00 58.23  ? 297 PHE   B O    1 
ATOM   570  C CB   . PHE   A 1 82  ? -14.650 -10.444 22.095 1.00 63.13  ? 297 PHE   B CB   1 
ATOM   571  C CG   . PHE   A 1 82  ? -14.402 -8.997  22.308 1.00 65.66  ? 297 PHE   B CG   1 
ATOM   572  C CD1  . PHE   A 1 82  ? -13.565 -8.572  23.328 1.00 68.36  ? 297 PHE   B CD1  1 
ATOM   573  C CD2  . PHE   A 1 82  ? -15.041 -8.052  21.527 1.00 64.47  ? 297 PHE   B CD2  1 
ATOM   574  C CE1  . PHE   A 1 82  ? -13.347 -7.225  23.547 1.00 73.70  ? 297 PHE   B CE1  1 
ATOM   575  C CE2  . PHE   A 1 82  ? -14.833 -6.705  21.744 1.00 70.66  ? 297 PHE   B CE2  1 
ATOM   576  C CZ   . PHE   A 1 82  ? -13.980 -6.289  22.756 1.00 73.11  ? 297 PHE   B CZ   1 
ATOM   577  N N    . PHE   A 1 83  ? -17.227 -12.601 22.172 1.00 54.37  ? 298 PHE   B N    1 
ATOM   578  C CA   . PHE   A 1 83  ? -17.764 -13.887 21.769 1.00 55.90  ? 298 PHE   B CA   1 
ATOM   579  C C    . PHE   A 1 83  ? -18.444 -13.749 20.420 1.00 54.06  ? 298 PHE   B C    1 
ATOM   580  O O    . PHE   A 1 83  ? -18.954 -12.679 20.079 1.00 52.01  ? 298 PHE   B O    1 
ATOM   581  C CB   . PHE   A 1 83  ? -18.770 -14.422 22.802 1.00 54.20  ? 298 PHE   B CB   1 
ATOM   582  C CG   . PHE   A 1 83  ? -18.150 -14.770 24.104 1.00 55.13  ? 298 PHE   B CG   1 
ATOM   583  C CD1  . PHE   A 1 83  ? -18.000 -13.808 25.086 1.00 55.05  ? 298 PHE   B CD1  1 
ATOM   584  C CD2  . PHE   A 1 83  ? -17.694 -16.054 24.344 1.00 55.17  ? 298 PHE   B CD2  1 
ATOM   585  C CE1  . PHE   A 1 83  ? -17.424 -14.120 26.293 1.00 57.14  ? 298 PHE   B CE1  1 
ATOM   586  C CE2  . PHE   A 1 83  ? -17.113 -16.374 25.560 1.00 61.63  ? 298 PHE   B CE2  1 
ATOM   587  C CZ   . PHE   A 1 83  ? -16.985 -15.402 26.540 1.00 58.79  ? 298 PHE   B CZ   1 
ATOM   588  N N    . LEU   A 1 84  ? -18.453 -14.850 19.667 1.00 54.11  ? 299 LEU   B N    1 
ATOM   589  C CA   . LEU   A 1 84  ? -19.184 -14.968 18.412 1.00 51.45  ? 299 LEU   B CA   1 
ATOM   590  C C    . LEU   A 1 84  ? -20.236 -16.058 18.563 1.00 50.00  ? 299 LEU   B C    1 
ATOM   591  O O    . LEU   A 1 84  ? -19.929 -17.185 18.973 1.00 49.54  ? 299 LEU   B O    1 
ATOM   592  C CB   . LEU   A 1 84  ? -18.244 -15.291 17.239 1.00 51.85  ? 299 LEU   B CB   1 
ATOM   593  C CG   . LEU   A 1 84  ? -18.793 -15.853 15.919 1.00 49.92  ? 299 LEU   B CG   1 
ATOM   594  C CD1  . LEU   A 1 84  ? -19.750 -14.874 15.284 1.00 50.65  ? 299 LEU   B CD1  1 
ATOM   595  C CD2  . LEU   A 1 84  ? -17.640 -16.129 14.950 1.00 54.15  ? 299 LEU   B CD2  1 
ATOM   596  N N    . VAL   A 1 85  ? -21.473 -15.717 18.238 1.00 47.17  ? 300 VAL   B N    1 
ATOM   597  C CA   . VAL   A 1 85  ? -22.594 -16.635 18.314 1.00 49.16  ? 300 VAL   B CA   1 
ATOM   598  C C    . VAL   A 1 85  ? -23.100 -16.786 16.895 1.00 48.25  ? 300 VAL   B C    1 
ATOM   599  O O    . VAL   A 1 85  ? -23.473 -15.796 16.255 1.00 48.94  ? 300 VAL   B O    1 
ATOM   600  C CB   . VAL   A 1 85  ? -23.694 -16.119 19.259 1.00 49.35  ? 300 VAL   B CB   1 
ATOM   601  C CG1  . VAL   A 1 85  ? -24.835 -17.112 19.352 1.00 47.59  ? 300 VAL   B CG1  1 
ATOM   602  C CG2  . VAL   A 1 85  ? -23.119 -15.857 20.645 1.00 44.70  ? 300 VAL   B CG2  1 
ATOM   603  N N    . LYS   A 1 86  ? -23.003 -17.991 16.369 1.00 48.67  ? 301 LYS   B N    1 
ATOM   604  C CA   . LYS   A 1 86  ? -23.632 -18.346 15.113 1.00 45.85  ? 301 LYS   B CA   1 
ATOM   605  C C    . LYS   A 1 86  ? -25.007 -18.918 15.443 1.00 48.40  ? 301 LYS   B C    1 
ATOM   606  O O    . LYS   A 1 86  ? -25.115 -19.892 16.203 1.00 46.83  ? 301 LYS   B O    1 
ATOM   607  C CB   . LYS   A 1 86  ? -22.760 -19.353 14.370 1.00 51.07  ? 301 LYS   B CB   1 
ATOM   608  C CG   . LYS   A 1 86  ? -23.495 -20.239 13.386 1.00 55.24  ? 301 LYS   B CG   1 
ATOM   609  C CD   . LYS   A 1 86  ? -23.616 -19.576 12.022 1.00 56.22  ? 301 LYS   B CD   1 
ATOM   610  C CE   . LYS   A 1 86  ? -22.355 -19.750 11.199 1.00 63.35  ? 301 LYS   B CE   1 
ATOM   611  N NZ   . LYS   A 1 86  ? -22.233 -21.044 10.464 1.00 66.15  ? 301 LYS   B NZ   1 
ATOM   612  N N    . PHE   A 1 87  ? -26.056 -18.288 14.918 1.00 49.31  ? 302 PHE   B N    1 
ATOM   613  C CA   . PHE   A 1 87  ? -27.417 -18.777 15.074 1.00 47.99  ? 302 PHE   B CA   1 
ATOM   614  C C    . PHE   A 1 87  ? -27.875 -19.507 13.810 1.00 50.75  ? 302 PHE   B C    1 
ATOM   615  O O    . PHE   A 1 87  ? -27.501 -19.146 12.690 1.00 50.44  ? 302 PHE   B O    1 
ATOM   616  C CB   . PHE   A 1 87  ? -28.372 -17.621 15.350 1.00 48.39  ? 302 PHE   B CB   1 
ATOM   617  C CG   . PHE   A 1 87  ? -28.391 -17.148 16.778 1.00 46.87  ? 302 PHE   B CG   1 
ATOM   618  C CD1  . PHE   A 1 87  ? -28.471 -18.048 17.830 1.00 49.15  ? 302 PHE   B CD1  1 
ATOM   619  C CD2  . PHE   A 1 87  ? -28.372 -15.791 17.064 1.00 45.33  ? 302 PHE   B CD2  1 
ATOM   620  C CE1  . PHE   A 1 87  ? -28.527 -17.603 19.169 1.00 46.45  ? 302 PHE   B CE1  1 
ATOM   621  C CE2  . PHE   A 1 87  ? -28.424 -15.338 18.385 1.00 50.19  ? 302 PHE   B CE2  1 
ATOM   622  C CZ   . PHE   A 1 87  ? -28.500 -16.256 19.445 1.00 46.79  ? 302 PHE   B CZ   1 
ATOM   623  N N    . TRP   A 1 88  ? -28.691 -20.537 14.011 1.00 48.97  ? 303 TRP   B N    1 
ATOM   624  C CA   . TRP   A 1 88  ? -29.509 -21.156 12.978 1.00 50.70  ? 303 TRP   B CA   1 
ATOM   625  C C    . TRP   A 1 88  ? -30.955 -20.847 13.329 1.00 49.03  ? 303 TRP   B C    1 
ATOM   626  O O    . TRP   A 1 88  ? -31.550 -21.499 14.190 1.00 55.00  ? 303 TRP   B O    1 
ATOM   627  C CB   . TRP   A 1 88  ? -29.274 -22.664 12.908 1.00 53.93  ? 303 TRP   B CB   1 
ATOM   628  C CG   . TRP   A 1 88  ? -28.013 -22.996 12.253 1.00 57.74  ? 303 TRP   B CG   1 
ATOM   629  C CD1  . TRP   A 1 88  ? -27.803 -23.179 10.913 1.00 55.01  ? 303 TRP   B CD1  1 
ATOM   630  C CD2  . TRP   A 1 88  ? -26.748 -23.150 12.888 1.00 58.94  ? 303 TRP   B CD2  1 
ATOM   631  N NE1  . TRP   A 1 88  ? -26.489 -23.462 10.688 1.00 57.71  ? 303 TRP   B NE1  1 
ATOM   632  C CE2  . TRP   A 1 88  ? -25.813 -23.446 11.879 1.00 59.43  ? 303 TRP   B CE2  1 
ATOM   633  C CE3  . TRP   A 1 88  ? -26.314 -23.075 14.216 1.00 56.51  ? 303 TRP   B CE3  1 
ATOM   634  C CZ2  . TRP   A 1 88  ? -24.471 -23.675 12.153 1.00 63.74  ? 303 TRP   B CZ2  1 
ATOM   635  C CZ3  . TRP   A 1 88  ? -24.982 -23.300 14.489 1.00 58.95  ? 303 TRP   B CZ3  1 
ATOM   636  C CH2  . TRP   A 1 88  ? -24.074 -23.596 13.459 1.00 66.61  ? 303 TRP   B CH2  1 
ATOM   637  N N    . ALA   A 1 89  ? -31.522 -19.883 12.645 1.00 48.23  ? 304 ALA   B N    1 
ATOM   638  C CA   . ALA   A 1 89  ? -32.803 -19.323 13.020 1.00 51.97  ? 304 ALA   B CA   1 
ATOM   639  C C    . ALA   A 1 89  ? -33.942 -20.141 12.432 1.00 54.55  ? 304 ALA   B C    1 
ATOM   640  O O    . ALA   A 1 89  ? -33.878 -20.579 11.291 1.00 55.35  ? 304 ALA   B O    1 
ATOM   641  C CB   . ALA   A 1 89  ? -32.899 -17.863 12.562 1.00 53.05  ? 304 ALA   B CB   1 
ATOM   642  N N    . ASP   A 1 90  ? -34.982 -20.359 13.237 1.00 59.85  ? 305 ASP   B N    1 
ATOM   643  C CA   . ASP   A 1 90  ? -36.177 -21.073 12.801 1.00 58.35  ? 305 ASP   B CA   1 
ATOM   644  C C    . ASP   A 1 90  ? -37.161 -20.039 12.275 1.00 60.30  ? 305 ASP   B C    1 
ATOM   645  O O    . ASP   A 1 90  ? -37.794 -19.318 13.049 1.00 59.86  ? 305 ASP   B O    1 
ATOM   646  C CB   . ASP   A 1 90  ? -36.751 -21.890 13.951 1.00 55.37  ? 305 ASP   B CB   1 
ATOM   647  C CG   . ASP   A 1 90  ? -37.993 -22.666 13.563 1.00 64.87  ? 305 ASP   B CG   1 
ATOM   648  O OD1  . ASP   A 1 90  ? -38.630 -22.312 12.550 1.00 67.24  ? 305 ASP   B OD1  1 
ATOM   649  O OD2  . ASP   A 1 90  ? -38.345 -23.627 14.283 1.00 66.56  ? 305 ASP   B OD2  1 
ATOM   650  N N    . LEU   A 1 91  ? -37.273 -19.940 10.950 1.00 57.43  ? 306 LEU   B N    1 
ATOM   651  C CA   . LEU   A 1 91  ? -38.147 -18.969 10.302 1.00 61.73  ? 306 LEU   B CA   1 
ATOM   652  C C    . LEU   A 1 91  ? -39.461 -19.590 9.850  1.00 66.89  ? 306 LEU   B C    1 
ATOM   653  O O    . LEU   A 1 91  ? -40.033 -19.159 8.844  1.00 69.00  ? 306 LEU   B O    1 
ATOM   654  C CB   . LEU   A 1 91  ? -37.444 -18.314 9.108  1.00 60.73  ? 306 LEU   B CB   1 
ATOM   655  C CG   . LEU   A 1 91  ? -36.233 -17.407 9.349  1.00 57.78  ? 306 LEU   B CG   1 
ATOM   656  C CD1  . LEU   A 1 91  ? -35.068 -18.239 9.867  1.00 58.66  ? 306 LEU   B CD1  1 
ATOM   657  C CD2  . LEU   A 1 91  ? -35.816 -16.750 8.061  1.00 59.14  ? 306 LEU   B CD2  1 
ATOM   658  N N    . ASN   A 1 92  ? -39.958 -20.584 10.576 1.00 73.06  ? 307 ASN   B N    1 
ATOM   659  C CA   . ASN   A 1 92  ? -41.161 -21.316 10.188 1.00 73.40  ? 307 ASN   B CA   1 
ATOM   660  C C    . ASN   A 1 92  ? -42.184 -21.193 11.310 1.00 73.69  ? 307 ASN   B C    1 
ATOM   661  O O    . ASN   A 1 92  ? -42.116 -21.941 12.292 1.00 74.05  ? 307 ASN   B O    1 
ATOM   662  C CB   . ASN   A 1 92  ? -40.821 -22.778 9.904  1.00 79.93  ? 307 ASN   B CB   1 
ATOM   663  C CG   . ASN   A 1 92  ? -41.799 -23.435 8.949  1.00 86.58  ? 307 ASN   B CG   1 
ATOM   664  O OD1  . ASN   A 1 92  ? -42.785 -24.046 9.376  1.00 84.77  ? 307 ASN   B OD1  1 
ATOM   665  N ND2  . ASN   A 1 92  ? -41.540 -23.301 7.643  1.00 87.07  ? 307 ASN   B ND2  1 
ATOM   666  N N    . TRP   A 1 93  ? -43.142 -20.276 11.167 1.00 72.53  ? 308 TRP   B N    1 
ATOM   667  C CA   . TRP   A 1 93  ? -44.126 -20.057 12.245 1.00 73.00  ? 308 TRP   B CA   1 
ATOM   668  C C    . TRP   A 1 93  ? -45.511 -19.599 11.764 1.00 74.94  ? 308 TRP   B C    1 
ATOM   669  O O    . TRP   A 1 93  ? -46.401 -20.410 11.482 1.00 76.73  ? 308 TRP   B O    1 
ATOM   670  C CB   . TRP   A 1 93  ? -43.568 -19.040 13.248 1.00 68.86  ? 308 TRP   B CB   1 
ATOM   671  C CG   . TRP   A 1 93  ? -43.648 -17.602 12.807 1.00 68.87  ? 308 TRP   B CG   1 
ATOM   672  C CD1  . TRP   A 1 93  ? -44.600 -16.688 13.164 1.00 69.82  ? 308 TRP   B CD1  1 
ATOM   673  C CD2  . TRP   A 1 93  ? -42.740 -16.909 11.929 1.00 70.32  ? 308 TRP   B CD2  1 
ATOM   674  N NE1  . TRP   A 1 93  ? -44.339 -15.469 12.569 1.00 69.69  ? 308 TRP   B NE1  1 
ATOM   675  C CE2  . TRP   A 1 93  ? -43.205 -15.578 11.811 1.00 67.75  ? 308 TRP   B CE2  1 
ATOM   676  C CE3  . TRP   A 1 93  ? -41.581 -17.288 11.224 1.00 70.02  ? 308 TRP   B CE3  1 
ATOM   677  C CZ2  . TRP   A 1 93  ? -42.553 -14.624 11.026 1.00 68.23  ? 308 TRP   B CZ2  1 
ATOM   678  C CZ3  . TRP   A 1 93  ? -40.928 -16.336 10.447 1.00 67.95  ? 308 TRP   B CZ3  1 
ATOM   679  C CH2  . TRP   A 1 93  ? -41.416 -15.014 10.359 1.00 66.18  ? 308 TRP   B CH2  1 
ATOM   680  N N    . SER   A 1 108 ? -50.543 -13.472 10.258 1.00 100.70 ? 323 SER   B N    1 
ATOM   681  C CA   . SER   A 1 108 ? -49.623 -12.447 10.731 1.00 97.36  ? 323 SER   B CA   1 
ATOM   682  C C    . SER   A 1 108 ? -50.243 -11.526 11.783 1.00 97.40  ? 323 SER   B C    1 
ATOM   683  O O    . SER   A 1 108 ? -51.432 -11.634 12.100 1.00 94.24  ? 323 SER   B O    1 
ATOM   684  C CB   . SER   A 1 108 ? -49.127 -11.614 9.557  1.00 93.83  ? 323 SER   B CB   1 
ATOM   685  O OG   . SER   A 1 108 ? -47.726 -11.738 9.442  1.00 93.11  ? 323 SER   B OG   1 
ATOM   686  N N    . GLY   A 1 109 ? -49.424 -10.621 12.323 1.00 93.78  ? 324 GLY   B N    1 
ATOM   687  C CA   . GLY   A 1 109 ? -49.912 -9.591  13.221 1.00 88.75  ? 324 GLY   B CA   1 
ATOM   688  C C    . GLY   A 1 109 ? -49.874 -9.952  14.694 1.00 87.43  ? 324 GLY   B C    1 
ATOM   689  O O    . GLY   A 1 109 ? -50.880 -9.809  15.394 1.00 89.03  ? 324 GLY   B O    1 
ATOM   690  N N    . GLY   A 1 110 ? -48.723 -10.410 15.186 1.00 79.39  ? 325 GLY   B N    1 
ATOM   691  C CA   . GLY   A 1 110 ? -48.607 -10.788 16.583 1.00 69.92  ? 325 GLY   B CA   1 
ATOM   692  C C    . GLY   A 1 110 ? -47.571 -9.961  17.314 1.00 65.11  ? 325 GLY   B C    1 
ATOM   693  O O    . GLY   A 1 110 ? -47.217 -8.862  16.870 1.00 65.03  ? 325 GLY   B O    1 
ATOM   694  N N    . PHE   A 1 111 ? -47.068 -10.463 18.435 1.00 59.49  ? 326 PHE   B N    1 
ATOM   695  C CA   . PHE   A 1 111 ? -46.075 -9.735  19.213 1.00 58.10  ? 326 PHE   B CA   1 
ATOM   696  C C    . PHE   A 1 111 ? -44.714 -10.380 19.016 1.00 54.06  ? 326 PHE   B C    1 
ATOM   697  O O    . PHE   A 1 111 ? -44.548 -11.586 19.242 1.00 54.30  ? 326 PHE   B O    1 
ATOM   698  C CB   . PHE   A 1 111 ? -46.419 -9.676  20.699 1.00 53.33  ? 326 PHE   B CB   1 
ATOM   699  C CG   . PHE   A 1 111 ? -45.330 -9.076  21.535 1.00 51.22  ? 326 PHE   B CG   1 
ATOM   700  C CD1  . PHE   A 1 111 ? -45.157 -7.697  21.587 1.00 51.77  ? 326 PHE   B CD1  1 
ATOM   701  C CD2  . PHE   A 1 111 ? -44.473 -9.888  22.274 1.00 50.66  ? 326 PHE   B CD2  1 
ATOM   702  C CE1  . PHE   A 1 111 ? -44.135 -7.134  22.364 1.00 50.25  ? 326 PHE   B CE1  1 
ATOM   703  C CE2  . PHE   A 1 111 ? -43.456 -9.340  23.049 1.00 49.90  ? 326 PHE   B CE2  1 
ATOM   704  C CZ   . PHE   A 1 111 ? -43.285 -7.955  23.088 1.00 49.05  ? 326 PHE   B CZ   1 
ATOM   705  N N    . TYR   A 1 112 ? -43.754 -9.562  18.606 1.00 52.46  ? 327 TYR   B N    1 
ATOM   706  C CA   . TYR   A 1 112 ? -42.384 -9.963  18.356 1.00 51.10  ? 327 TYR   B CA   1 
ATOM   707  C C    . TYR   A 1 112 ? -41.501 -9.333  19.423 1.00 50.81  ? 327 TYR   B C    1 
ATOM   708  O O    . TYR   A 1 112 ? -41.510 -8.106  19.598 1.00 51.03  ? 327 TYR   B O    1 
ATOM   709  C CB   . TYR   A 1 112 ? -41.951 -9.503  16.965 1.00 50.76  ? 327 TYR   B CB   1 
ATOM   710  C CG   . TYR   A 1 112 ? -42.644 -10.183 15.799 1.00 51.82  ? 327 TYR   B CG   1 
ATOM   711  C CD1  . TYR   A 1 112 ? -43.975 -9.923  15.510 1.00 54.79  ? 327 TYR   B CD1  1 
ATOM   712  C CD2  . TYR   A 1 112 ? -41.948 -11.063 14.952 1.00 54.23  ? 327 TYR   B CD2  1 
ATOM   713  C CE1  . TYR   A 1 112 ? -44.606 -10.530 14.411 1.00 57.41  ? 327 TYR   B CE1  1 
ATOM   714  C CE2  . TYR   A 1 112 ? -42.573 -11.679 13.846 1.00 52.45  ? 327 TYR   B CE2  1 
ATOM   715  C CZ   . TYR   A 1 112 ? -43.905 -11.402 13.598 1.00 55.42  ? 327 TYR   B CZ   1 
ATOM   716  O OH   . TYR   A 1 112 ? -44.561 -11.989 12.547 1.00 63.94  ? 327 TYR   B OH   1 
ATOM   717  N N    . GLY   A 1 113 ? -40.744 -10.157 20.142 1.00 49.31  ? 328 GLY   B N    1 
ATOM   718  C CA   . GLY   A 1 113 ? -40.017 -9.661  21.283 1.00 46.25  ? 328 GLY   B CA   1 
ATOM   719  C C    . GLY   A 1 113 ? -38.641 -10.275 21.399 1.00 44.15  ? 328 GLY   B C    1 
ATOM   720  O O    . GLY   A 1 113 ? -38.339 -11.318 20.810 1.00 44.51  ? 328 GLY   B O    1 
ATOM   721  N N    . VAL   A 1 114 ? -37.815 -9.588  22.187 1.00 47.75  ? 329 VAL   B N    1 
ATOM   722  C CA   . VAL   A 1 114 ? -36.457 -9.986  22.532 1.00 50.01  ? 329 VAL   B CA   1 
ATOM   723  C C    . VAL   A 1 114 ? -36.323 -9.910  24.045 1.00 45.40  ? 329 VAL   B C    1 
ATOM   724  O O    . VAL   A 1 114 ? -36.842 -8.983  24.679 1.00 46.14  ? 329 VAL   B O    1 
ATOM   725  C CB   . VAL   A 1 114 ? -35.406 -9.079  21.848 1.00 47.35  ? 329 VAL   B CB   1 
ATOM   726  C CG1  . VAL   A 1 114 ? -33.986 -9.530  22.200 1.00 44.12  ? 329 VAL   B CG1  1 
ATOM   727  C CG2  . VAL   A 1 114 ? -35.625 -9.069  20.321 1.00 51.31  ? 329 VAL   B CG2  1 
ATOM   728  N N    . SER   A 1 115 ? -35.612 -10.872 24.616 1.00 45.10  ? 330 SER   B N    1 
ATOM   729  C CA   . SER   A 1 115 ? -35.491 -11.044 26.055 1.00 47.84  ? 330 SER   B CA   1 
ATOM   730  C C    . SER   A 1 115 ? -34.050 -11.379 26.388 1.00 45.29  ? 330 SER   B C    1 
ATOM   731  O O    . SER   A 1 115 ? -33.475 -12.306 25.794 1.00 44.08  ? 330 SER   B O    1 
ATOM   732  C CB   . SER   A 1 115 ? -36.411 -12.157 26.549 1.00 44.88  ? 330 SER   B CB   1 
ATOM   733  O OG   . SER   A 1 115 ? -37.773 -11.787 26.414 1.00 46.35  ? 330 SER   B OG   1 
ATOM   734  N N    . SER   A 1 116 ? -33.475 -10.617 27.319 1.00 42.67  ? 331 SER   B N    1 
ATOM   735  C CA   . SER   A 1 116 ? -32.103 -10.811 27.761 1.00 47.15  ? 331 SER   B CA   1 
ATOM   736  C C    . SER   A 1 116 ? -32.080 -10.851 29.280 1.00 51.19  ? 331 SER   B C    1 
ATOM   737  O O    . SER   A 1 116 ? -32.686 -9.996  29.934 1.00 52.27  ? 331 SER   B O    1 
ATOM   738  C CB   . SER   A 1 116 ? -31.194 -9.685  27.278 1.00 46.82  ? 331 SER   B CB   1 
ATOM   739  O OG   . SER   A 1 116 ? -31.257 -9.524  25.859 1.00 56.45  ? 331 SER   B OG   1 
ATOM   740  N N    . GLN   A 1 117 ? -31.360 -11.810 29.841 1.00 47.97  ? 332 GLN   B N    1 
ATOM   741  C CA   . GLN   A 1 117 ? -31.081 -11.815 31.263 1.00 56.02  ? 332 GLN   B CA   1 
ATOM   742  C C    . GLN   A 1 117 ? -29.593 -12.075 31.445 1.00 53.64  ? 332 GLN   B C    1 
ATOM   743  O O    . GLN   A 1 117 ? -29.045 -12.988 30.823 1.00 52.86  ? 332 GLN   B O    1 
ATOM   744  C CB   . GLN   A 1 117 ? -31.943 -12.863 32.006 1.00 53.26  ? 332 GLN   B CB   1 
ATOM   745  C CG   . GLN   A 1 117 ? -31.785 -12.821 33.498 1.00 59.73  ? 332 GLN   B CG   1 
ATOM   746  C CD   . GLN   A 1 117 ? -32.864 -13.604 34.265 1.00 64.12  ? 332 GLN   B CD   1 
ATOM   747  O OE1  . GLN   A 1 117 ? -34.060 -13.538 33.946 1.00 65.30  ? 332 GLN   B OE1  1 
ATOM   748  N NE2  . GLN   A 1 117 ? -32.432 -14.359 35.278 1.00 61.81  ? 332 GLN   B NE2  1 
ATOM   749  N N    . TYR   A 1 118 ? -28.947 -11.257 32.282 1.00 53.94  ? 333 TYR   B N    1 
ATOM   750  C CA   . TYR   A 1 118 ? -27.556 -11.412 32.695 1.00 54.88  ? 333 TYR   B CA   1 
ATOM   751  C C    . TYR   A 1 118 ? -27.488 -11.551 34.210 1.00 59.51  ? 333 TYR   B C    1 
ATOM   752  O O    . TYR   A 1 118 ? -28.444 -11.261 34.929 1.00 60.41  ? 333 TYR   B O    1 
ATOM   753  C CB   . TYR   A 1 118 ? -26.698 -10.213 32.265 1.00 55.65  ? 333 TYR   B CB   1 
ATOM   754  C CG   . TYR   A 1 118 ? -26.754 -9.882  30.796 1.00 52.85  ? 333 TYR   B CG   1 
ATOM   755  C CD1  . TYR   A 1 118 ? -25.861 -10.457 29.900 1.00 50.10  ? 333 TYR   B CD1  1 
ATOM   756  C CD2  . TYR   A 1 118 ? -27.695 -8.993  30.308 1.00 50.98  ? 333 TYR   B CD2  1 
ATOM   757  C CE1  . TYR   A 1 118 ? -25.902 -10.141 28.563 1.00 50.93  ? 333 TYR   B CE1  1 
ATOM   758  C CE2  . TYR   A 1 118 ? -27.748 -8.675  28.978 1.00 51.23  ? 333 TYR   B CE2  1 
ATOM   759  C CZ   . TYR   A 1 118 ? -26.846 -9.248  28.102 1.00 51.95  ? 333 TYR   B CZ   1 
ATOM   760  O OH   . TYR   A 1 118 ? -26.905 -8.932  26.758 1.00 52.40  ? 333 TYR   B OH   1 
ATOM   761  N N    . GLU   A 1 119 ? -26.319 -11.952 34.697 1.00 57.49  ? 334 GLU   B N    1 
ATOM   762  C CA   . GLU   A 1 119 ? -26.137 -12.232 36.109 1.00 57.68  ? 334 GLU   B CA   1 
ATOM   763  C C    . GLU   A 1 119 ? -24.714 -11.895 36.499 1.00 59.70  ? 334 GLU   B C    1 
ATOM   764  O O    . GLU   A 1 119 ? -23.773 -12.289 35.806 1.00 60.31  ? 334 GLU   B O    1 
ATOM   765  C CB   . GLU   A 1 119 ? -26.411 -13.699 36.407 1.00 63.02  ? 334 GLU   B CB   1 
ATOM   766  C CG   . GLU   A 1 119 ? -27.866 -14.058 36.286 1.00 66.42  ? 334 GLU   B CG   1 
ATOM   767  C CD   . GLU   A 1 119 ? -28.212 -15.334 37.034 1.00 71.00  ? 334 GLU   B CD   1 
ATOM   768  O OE1  . GLU   A 1 119 ? -27.363 -15.815 37.821 1.00 74.39  ? 334 GLU   B OE1  1 
ATOM   769  O OE2  . GLU   A 1 119 ? -29.341 -15.840 36.836 1.00 69.08  ? 334 GLU   B OE2  1 
ATOM   770  N N    . SER   A 1 120 ? -24.553 -11.187 37.605 1.00 63.32  ? 335 SER   B N    1 
ATOM   771  C CA   . SER   A 1 120 ? -23.227 -10.950 38.135 1.00 65.46  ? 335 SER   B CA   1 
ATOM   772  C C    . SER   A 1 120 ? -23.248 -11.054 39.652 1.00 72.32  ? 335 SER   B C    1 
ATOM   773  O O    . SER   A 1 120 ? -24.301 -11.123 40.299 1.00 70.38  ? 335 SER   B O    1 
ATOM   774  C CB   . SER   A 1 120 ? -22.688 -9.584  37.715 1.00 65.26  ? 335 SER   B CB   1 
ATOM   775  O OG   . SER   A 1 120 ? -23.284 -8.561  38.484 1.00 69.24  ? 335 SER   B OG   1 
ATOM   776  N N    . LEU   A 1 121 ? -22.051 -11.067 40.213 1.00 69.90  ? 336 LEU   B N    1 
ATOM   777  C CA   . LEU   A 1 121 ? -21.899 -10.984 41.647 1.00 65.66  ? 336 LEU   B CA   1 
ATOM   778  C C    . LEU   A 1 121 ? -21.694 -9.549  42.105 1.00 69.24  ? 336 LEU   B C    1 
ATOM   779  O O    . LEU   A 1 121 ? -22.065 -9.215  43.238 1.00 75.38  ? 336 LEU   B O    1 
ATOM   780  C CB   . LEU   A 1 121 ? -20.742 -11.875 42.084 1.00 66.12  ? 336 LEU   B CB   1 
ATOM   781  C CG   . LEU   A 1 121 ? -21.229 -13.268 42.469 1.00 70.88  ? 336 LEU   B CG   1 
ATOM   782  C CD1  . LEU   A 1 121 ? -20.200 -14.313 42.092 1.00 72.42  ? 336 LEU   B CD1  1 
ATOM   783  C CD2  . LEU   A 1 121 ? -21.523 -13.317 43.968 1.00 73.73  ? 336 LEU   B CD2  1 
ATOM   784  N N    . GLU   A 1 122 ? -21.146 -8.686  41.245 1.00 67.48  ? 337 GLU   B N    1 
ATOM   785  C CA   . GLU   A 1 122 ? -21.045 -7.263  41.553 1.00 68.31  ? 337 GLU   B CA   1 
ATOM   786  C C    . GLU   A 1 122 ? -22.347 -6.560  41.215 1.00 66.99  ? 337 GLU   B C    1 
ATOM   787  O O    . GLU   A 1 122 ? -22.986 -6.869  40.206 1.00 65.05  ? 337 GLU   B O    1 
ATOM   788  C CB   . GLU   A 1 122 ? -19.927 -6.574  40.772 1.00 67.71  ? 337 GLU   B CB   1 
ATOM   789  C CG   . GLU   A 1 122 ? -18.897 -7.476  40.178 1.00 74.44  ? 337 GLU   B CG   1 
ATOM   790  C CD   . GLU   A 1 122 ? -17.697 -6.695  39.709 1.00 79.25  ? 337 GLU   B CD   1 
ATOM   791  O OE1  . GLU   A 1 122 ? -16.803 -7.306  39.086 1.00 79.18  ? 337 GLU   B OE1  1 
ATOM   792  O OE2  . GLU   A 1 122 ? -17.648 -5.470  39.979 1.00 80.02  ? 337 GLU   B OE2  1 
ATOM   793  N N    . HIS   A 1 123 ? -22.725 -5.601  42.069 1.00 69.30  ? 338 HIS   B N    1 
ATOM   794  C CA   . HIS   A 1 123 ? -23.809 -4.677  41.763 1.00 66.67  ? 338 HIS   B CA   1 
ATOM   795  C C    . HIS   A 1 123 ? -23.314 -3.667  40.740 1.00 65.86  ? 338 HIS   B C    1 
ATOM   796  O O    . HIS   A 1 123 ? -22.290 -3.005  40.955 1.00 64.36  ? 338 HIS   B O    1 
ATOM   797  C CB   . HIS   A 1 123 ? -24.287 -3.954  43.024 1.00 68.74  ? 338 HIS   B CB   1 
ATOM   798  C CG   . HIS   A 1 123 ? -25.427 -3.013  42.776 1.00 68.69  ? 338 HIS   B CG   1 
ATOM   799  N ND1  . HIS   A 1 123 ? -26.721 -3.289  43.166 1.00 70.18  ? 338 HIS   B ND1  1 
ATOM   800  C CD2  . HIS   A 1 123 ? -25.476 -1.823  42.129 1.00 68.94  ? 338 HIS   B CD2  1 
ATOM   801  C CE1  . HIS   A 1 123 ? -27.511 -2.293  42.800 1.00 71.04  ? 338 HIS   B CE1  1 
ATOM   802  N NE2  . HIS   A 1 123 ? -26.781 -1.394  42.163 1.00 69.19  ? 338 HIS   B NE2  1 
ATOM   803  N N    . MET   A 1 124 ? -24.026 -3.561  39.624 1.00 67.68  ? 339 MET   B N    1 
ATOM   804  C CA   . MET   A 1 124 ? -23.630 -2.665  38.557 1.00 64.08  ? 339 MET   B CA   1 
ATOM   805  C C    . MET   A 1 124 ? -24.879 -2.052  37.950 1.00 62.31  ? 339 MET   B C    1 
ATOM   806  O O    . MET   A 1 124 ? -25.998 -2.529  38.155 1.00 61.07  ? 339 MET   B O    1 
ATOM   807  C CB   . MET   A 1 124 ? -22.838 -3.394  37.471 1.00 64.81  ? 339 MET   B CB   1 
ATOM   808  C CG   . MET   A 1 124 ? -21.383 -3.638  37.797 1.00 66.28  ? 339 MET   B CG   1 
ATOM   809  S SD   . MET   A 1 124 ? -20.626 -4.889  36.715 1.00 70.84  ? 339 MET   B SD   1 
ATOM   810  C CE   . MET   A 1 124 ? -21.994 -5.986  36.309 1.00 59.32  ? 339 MET   B CE   1 
ATOM   811  N N    . THR   A 1 125 ? -24.681 -0.987  37.190 1.00 59.79  ? 340 THR   B N    1 
ATOM   812  C CA   . THR   A 1 125 ? -25.669 -0.609  36.199 1.00 62.84  ? 340 THR   B CA   1 
ATOM   813  C C    . THR   A 1 125 ? -25.103 -0.869  34.810 1.00 62.52  ? 340 THR   B C    1 
ATOM   814  O O    . THR   A 1 125 ? -23.918 -0.634  34.551 1.00 62.27  ? 340 THR   B O    1 
ATOM   815  C CB   . THR   A 1 125 ? -26.095 0.834   36.351 1.00 64.53  ? 340 THR   B CB   1 
ATOM   816  O OG1  . THR   A 1 125 ? -26.083 1.161   37.733 1.00 69.37  ? 340 THR   B OG1  1 
ATOM   817  C CG2  . THR   A 1 125 ? -27.515 0.991   35.856 1.00 65.64  ? 340 THR   B CG2  1 
ATOM   818  N N    . LEU   A 1 126 ? -25.952 -1.396  33.934 1.00 62.31  ? 341 LEU   B N    1 
ATOM   819  C CA   . LEU   A 1 126 ? -25.549 -1.881  32.622 1.00 60.72  ? 341 LEU   B CA   1 
ATOM   820  C C    . LEU   A 1 126 ? -26.144 -1.016  31.516 1.00 57.91  ? 341 LEU   B C    1 
ATOM   821  O O    . LEU   A 1 126 ? -27.302 -0.601  31.587 1.00 61.76  ? 341 LEU   B O    1 
ATOM   822  C CB   . LEU   A 1 126 ? -26.000 -3.331  32.426 1.00 58.63  ? 341 LEU   B CB   1 
ATOM   823  C CG   . LEU   A 1 126 ? -25.414 -4.434  33.303 1.00 58.42  ? 341 LEU   B CG   1 
ATOM   824  C CD1  . LEU   A 1 126 ? -25.776 -5.817  32.729 1.00 56.02  ? 341 LEU   B CD1  1 
ATOM   825  C CD2  . LEU   A 1 126 ? -23.914 -4.258  33.430 1.00 58.58  ? 341 LEU   B CD2  1 
ATOM   826  N N    . THR   A 1 127 ? -25.350 -0.735  30.501 1.00 59.19  ? 342 THR   B N    1 
ATOM   827  C CA   . THR   A 1 127 ? -25.861 -0.273  29.219 1.00 60.84  ? 342 THR   B CA   1 
ATOM   828  C C    . THR   A 1 127 ? -25.694 -1.408  28.216 1.00 57.45  ? 342 THR   B C    1 
ATOM   829  O O    . THR   A 1 127 ? -24.602 -1.972  28.094 1.00 54.68  ? 342 THR   B O    1 
ATOM   830  C CB   . THR   A 1 127 ? -25.126 0.983   28.737 1.00 60.65  ? 342 THR   B CB   1 
ATOM   831  O OG1  . THR   A 1 127 ? -25.121 1.983   29.770 1.00 60.94  ? 342 THR   B OG1  1 
ATOM   832  C CG2  . THR   A 1 127 ? -25.803 1.550   27.499 1.00 56.64  ? 342 THR   B CG2  1 
ATOM   833  N N    . CYS   A 1 128 ? -26.779 -1.772  27.536 1.00 53.14  ? 343 CYS   B N    1 
ATOM   834  C CA   . CYS   A 1 128 ? -26.742 -2.794  26.497 1.00 51.86  ? 343 CYS   B CA   1 
ATOM   835  C C    . CYS   A 1 128 ? -27.052 -2.123  25.168 1.00 52.60  ? 343 CYS   B C    1 
ATOM   836  O O    . CYS   A 1 128 ? -28.195 -1.722  24.914 1.00 53.87  ? 343 CYS   B O    1 
ATOM   837  C CB   . CYS   A 1 128 ? -27.719 -3.935  26.774 1.00 54.88  ? 343 CYS   B CB   1 
ATOM   838  S SG   . CYS   A 1 128 ? -28.037 -4.352  28.570 1.00 66.30  ? 343 CYS   B SG   1 
ATOM   839  N N    . SER   A 1 129 ? -26.027 -1.986  24.338 1.00 55.82  ? 344 SER   B N    1 
ATOM   840  C CA   . SER   A 1 129 ? -26.162 -1.501  22.971 1.00 54.38  ? 344 SER   B CA   1 
ATOM   841  C C    . SER   A 1 129 ? -26.245 -2.703  22.051 1.00 55.27  ? 344 SER   B C    1 
ATOM   842  O O    . SER   A 1 129 ? -25.411 -3.610  22.137 1.00 54.82  ? 344 SER   B O    1 
ATOM   843  C CB   . SER   A 1 129 ? -24.966 -0.648  22.578 1.00 53.89  ? 344 SER   B CB   1 
ATOM   844  O OG   . SER   A 1 129 ? -24.976 -0.393  21.188 1.00 63.79  ? 344 SER   B OG   1 
ATOM   845  N N    . SER   A 1 130 ? -27.257 -2.736  21.197 1.00 52.79  ? 345 SER   B N    1 
ATOM   846  C CA   . SER   A 1 130 ? -27.309 -3.761  20.164 1.00 56.39  ? 345 SER   B CA   1 
ATOM   847  C C    . SER   A 1 130 ? -27.426 -3.063  18.820 1.00 56.73  ? 345 SER   B C    1 
ATOM   848  O O    . SER   A 1 130 ? -28.355 -2.276  18.606 1.00 58.84  ? 345 SER   B O    1 
ATOM   849  C CB   . SER   A 1 130 ? -28.448 -4.762  20.403 1.00 55.35  ? 345 SER   B CB   1 
ATOM   850  O OG   . SER   A 1 130 ? -29.580 -4.149  20.971 1.00 59.15  ? 345 SER   B OG   1 
ATOM   851  N N    . LYS   A 1 131 ? -26.450 -3.306  17.946 1.00 56.97  ? 346 LYS   B N    1 
ATOM   852  C CA   . LYS   A 1 131 ? -26.374 -2.692  16.623 1.00 58.97  ? 346 LYS   B CA   1 
ATOM   853  C C    . LYS   A 1 131 ? -26.667 -3.734  15.557 1.00 55.38  ? 346 LYS   B C    1 
ATOM   854  O O    . LYS   A 1 131 ? -26.031 -4.788  15.536 1.00 53.88  ? 346 LYS   B O    1 
ATOM   855  C CB   . LYS   A 1 131 ? -24.992 -2.087  16.375 1.00 59.10  ? 346 LYS   B CB   1 
ATOM   856  C CG   . LYS   A 1 131 ? -24.480 -1.190  17.494 1.00 64.00  ? 346 LYS   B CG   1 
ATOM   857  C CD   . LYS   A 1 131 ? -23.005 -0.911  17.275 1.00 71.06  ? 346 LYS   B CD   1 
ATOM   858  C CE   . LYS   A 1 131 ? -22.680 0.559   17.354 1.00 76.71  ? 346 LYS   B CE   1 
ATOM   859  N NZ   . LYS   A 1 131 ? -21.556 0.811   16.406 1.00 85.53  ? 346 LYS   B NZ   1 
ATOM   860  N N    . VAL   A 1 132 ? -27.616 -3.435  14.677 1.00 59.32  ? 347 VAL   B N    1 
ATOM   861  C CA   . VAL   A 1 132 ? -27.972 -4.305  13.561 1.00 58.11  ? 347 VAL   B CA   1 
ATOM   862  C C    . VAL   A 1 132 ? -27.288 -3.776  12.309 1.00 62.28  ? 347 VAL   B C    1 
ATOM   863  O O    . VAL   A 1 132 ? -27.520 -2.629  11.902 1.00 63.48  ? 347 VAL   B O    1 
ATOM   864  C CB   . VAL   A 1 132 ? -29.493 -4.366  13.363 1.00 57.16  ? 347 VAL   B CB   1 
ATOM   865  C CG1  . VAL   A 1 132 ? -29.840 -5.243  12.164 1.00 56.58  ? 347 VAL   B CG1  1 
ATOM   866  C CG2  . VAL   A 1 132 ? -30.169 -4.837  14.642 1.00 56.24  ? 347 VAL   B CG2  1 
ATOM   867  N N    . CYS   A 1 133 ? -26.463 -4.607  11.682 1.00 58.78  ? 348 CYS   B N    1 
ATOM   868  C CA   . CYS   A 1 133 ? -25.652 -4.186  10.550 1.00 62.65  ? 348 CYS   B CA   1 
ATOM   869  C C    . CYS   A 1 133 ? -26.056 -4.966  9.309  1.00 62.32  ? 348 CYS   B C    1 
ATOM   870  O O    . CYS   A 1 133 ? -26.174 -6.196  9.344  1.00 57.19  ? 348 CYS   B O    1 
ATOM   871  C CB   . CYS   A 1 133 ? -24.160 -4.369  10.843 1.00 66.99  ? 348 CYS   B CB   1 
ATOM   872  S SG   . CYS   A 1 133 ? -23.630 -3.639  12.442 1.00 76.61  ? 348 CYS   B SG   1 
ATOM   873  N N    . SER   A 1 134 ? -26.266 -4.240  8.218  1.00 65.61  ? 349 SER   B N    1 
ATOM   874  C CA   . SER   A 1 134 ? -26.523 -4.816  6.908  1.00 66.41  ? 349 SER   B CA   1 
ATOM   875  C C    . SER   A 1 134 ? -25.334 -4.508  6.010  1.00 69.54  ? 349 SER   B C    1 
ATOM   876  O O    . SER   A 1 134 ? -25.035 -3.332  5.758  1.00 72.26  ? 349 SER   B O    1 
ATOM   877  C CB   . SER   A 1 134 ? -27.809 -4.250  6.317  1.00 64.73  ? 349 SER   B CB   1 
ATOM   878  O OG   . SER   A 1 134 ? -27.811 -4.434  4.923  1.00 69.71  ? 349 SER   B OG   1 
ATOM   879  N N    . PHE   A 1 135 ? -24.666 -5.554  5.514  1.00 65.83  ? 350 PHE   B N    1 
ATOM   880  C CA   . PHE   A 1 135 ? -23.445 -5.380  4.713  1.00 67.90  ? 350 PHE   B CA   1 
ATOM   881  C C    . PHE   A 1 135 ? -22.387 -4.604  5.494  1.00 77.61  ? 350 PHE   B C    1 
ATOM   882  O O    . PHE   A 1 135 ? -21.652 -3.784  4.927  1.00 78.19  ? 350 PHE   B O    1 
ATOM   883  C CB   . PHE   A 1 135 ? -23.725 -4.675  3.383  1.00 62.82  ? 350 PHE   B CB   1 
ATOM   884  C CG   . PHE   A 1 135 ? -24.519 -5.494  2.423  1.00 63.98  ? 350 PHE   B CG   1 
ATOM   885  C CD1  . PHE   A 1 135 ? -25.907 -5.515  2.495  1.00 61.74  ? 350 PHE   B CD1  1 
ATOM   886  C CD2  . PHE   A 1 135 ? -23.876 -6.271  1.456  1.00 64.10  ? 350 PHE   B CD2  1 
ATOM   887  C CE1  . PHE   A 1 135 ? -26.644 -6.286  1.606  1.00 61.44  ? 350 PHE   B CE1  1 
ATOM   888  C CE2  . PHE   A 1 135 ? -24.604 -7.053  0.571  1.00 64.14  ? 350 PHE   B CE2  1 
ATOM   889  C CZ   . PHE   A 1 135 ? -25.986 -7.055  0.630  1.00 62.83  ? 350 PHE   B CZ   1 
ATOM   890  N N    . GLY   A 1 136 ? -22.339 -4.829  6.805  1.00 77.48  ? 351 GLY   B N    1 
ATOM   891  C CA   . GLY   A 1 136 ? -21.350 -4.179  7.649  1.00 82.34  ? 351 GLY   B CA   1 
ATOM   892  C C    . GLY   A 1 136 ? -21.531 -2.683  7.813  1.00 85.90  ? 351 GLY   B C    1 
ATOM   893  O O    . GLY   A 1 136 ? -20.539 -1.938  7.813  1.00 90.30  ? 351 GLY   B O    1 
ATOM   894  N N    . LYS   A 1 137 ? -22.774 -2.223  7.955  1.00 81.89  ? 352 LYS   B N    1 
ATOM   895  C CA   . LYS   A 1 137 ? -23.079 -0.811  8.163  1.00 77.85  ? 352 LYS   B CA   1 
ATOM   896  C C    . LYS   A 1 137 ? -24.293 -0.729  9.065  1.00 77.14  ? 352 LYS   B C    1 
ATOM   897  O O    . LYS   A 1 137 ? -25.360 -1.233  8.701  1.00 75.57  ? 352 LYS   B O    1 
ATOM   898  C CB   . LYS   A 1 137 ? -23.353 -0.091  6.839  1.00 80.33  ? 352 LYS   B CB   1 
ATOM   899  C CG   . LYS   A 1 137 ? -24.677 -0.479  6.170  1.00 80.33  ? 352 LYS   B CG   1 
ATOM   900  C CD   . LYS   A 1 137 ? -25.687 0.675   6.186  1.00 83.29  ? 352 LYS   B CD   1 
ATOM   901  C CE   . LYS   A 1 137 ? -26.590 0.656   4.941  1.00 83.17  ? 352 LYS   B CE   1 
ATOM   902  N NZ   . LYS   A 1 137 ? -27.464 1.862   4.881  1.00 87.25  ? 352 LYS   B NZ   1 
ATOM   903  N N    . GLN   A 1 138 ? -24.130 -0.113  10.237 1.00 73.94  ? 353 GLN   B N    1 
ATOM   904  C CA   . GLN   A 1 138 ? -25.233 0.045   11.168 1.00 67.96  ? 353 GLN   B CA   1 
ATOM   905  C C    . GLN   A 1 138 ? -26.482 0.494   10.429 1.00 68.42  ? 353 GLN   B C    1 
ATOM   906  O O    . GLN   A 1 138 ? -26.453 1.477   9.690  1.00 77.21  ? 353 GLN   B O    1 
ATOM   907  C CB   . GLN   A 1 138 ? -24.867 1.063   12.248 1.00 69.50  ? 353 GLN   B CB   1 
ATOM   908  C CG   . GLN   A 1 138 ? -25.924 1.150   13.350 1.00 69.06  ? 353 GLN   B CG   1 
ATOM   909  C CD   . GLN   A 1 138 ? -25.652 2.233   14.379 1.00 67.50  ? 353 GLN   B CD   1 
ATOM   910  O OE1  . GLN   A 1 138 ? -26.401 3.205   14.481 1.00 63.29  ? 353 GLN   B OE1  1 
ATOM   911  N NE2  . GLN   A 1 138 ? -24.588 2.062   15.156 1.00 68.29  ? 353 GLN   B NE2  1 
ATOM   912  N N    . VAL   A 1 139 ? -27.570 -0.257  10.574 1.00 66.46  ? 354 VAL   B N    1 
ATOM   913  C CA   . VAL   A 1 139 ? -28.855 0.105   9.990  1.00 65.49  ? 354 VAL   B CA   1 
ATOM   914  C C    . VAL   A 1 139 ? -29.848 0.534   11.062 1.00 64.42  ? 354 VAL   B C    1 
ATOM   915  O O    . VAL   A 1 139 ? -30.645 1.450   10.844 1.00 65.65  ? 354 VAL   B O    1 
ATOM   916  C CB   . VAL   A 1 139 ? -29.429 -1.054  9.135  1.00 66.83  ? 354 VAL   B CB   1 
ATOM   917  C CG1  . VAL   A 1 139 ? -30.946 -0.974  9.065  1.00 64.59  ? 354 VAL   B CG1  1 
ATOM   918  C CG2  . VAL   A 1 139 ? -28.844 -1.016  7.724  1.00 70.00  ? 354 VAL   B CG2  1 
ATOM   919  N N    . VAL   A 1 140 ? -29.810 -0.110  12.230 1.00 62.32  ? 355 VAL   B N    1 
ATOM   920  C CA   . VAL   A 1 140 ? -30.609 0.310   13.375 1.00 62.48  ? 355 VAL   B CA   1 
ATOM   921  C C    . VAL   A 1 140 ? -29.870 -0.062  14.652 1.00 60.41  ? 355 VAL   B C    1 
ATOM   922  O O    . VAL   A 1 140 ? -29.314 -1.158  14.776 1.00 60.79  ? 355 VAL   B O    1 
ATOM   923  C CB   . VAL   A 1 140 ? -32.024 -0.311  13.353 1.00 60.99  ? 355 VAL   B CB   1 
ATOM   924  C CG1  . VAL   A 1 140 ? -32.794 0.197   12.166 1.00 62.56  ? 355 VAL   B CG1  1 
ATOM   925  C CG2  . VAL   A 1 140 ? -31.954 -1.806  13.329 1.00 60.63  ? 355 VAL   B CG2  1 
ATOM   926  N N    . GLU   A 1 141 ? -29.880 0.857   15.608 1.00 59.24  ? 356 GLU   B N    1 
ATOM   927  C CA   . GLU   A 1 141 ? -29.253 0.647   16.904 1.00 61.55  ? 356 GLU   B CA   1 
ATOM   928  C C    . GLU   A 1 141 ? -30.263 0.905   18.010 1.00 59.20  ? 356 GLU   B C    1 
ATOM   929  O O    . GLU   A 1 141 ? -31.060 1.844   17.924 1.00 58.26  ? 356 GLU   B O    1 
ATOM   930  C CB   . GLU   A 1 141 ? -28.036 1.563   17.075 1.00 59.98  ? 356 GLU   B CB   1 
ATOM   931  C CG   . GLU   A 1 141 ? -27.530 1.628   18.475 1.00 60.28  ? 356 GLU   B CG   1 
ATOM   932  C CD   . GLU   A 1 141 ? -26.299 2.483   18.604 1.00 66.42  ? 356 GLU   B CD   1 
ATOM   933  O OE1  . GLU   A 1 141 ? -26.163 3.484   17.858 1.00 67.84  ? 356 GLU   B OE1  1 
ATOM   934  O OE2  . GLU   A 1 141 ? -25.465 2.141   19.473 1.00 71.39  ? 356 GLU   B OE2  1 
ATOM   935  N N    . LYS   A 1 142 ? -30.241 0.052   19.034 1.00 58.64  ? 357 LYS   B N    1 
ATOM   936  C CA   . LYS   A 1 142 ? -31.007 0.249   20.262 1.00 58.19  ? 357 LYS   B CA   1 
ATOM   937  C C    . LYS   A 1 142 ? -30.061 0.239   21.455 1.00 56.75  ? 357 LYS   B C    1 
ATOM   938  O O    . LYS   A 1 142 ? -29.160 -0.608  21.541 1.00 53.45  ? 357 LYS   B O    1 
ATOM   939  C CB   . LYS   A 1 142 ? -32.093 -0.837  20.466 1.00 61.48  ? 357 LYS   B CB   1 
ATOM   940  C CG   . LYS   A 1 142 ? -33.056 -1.071  19.275 1.00 64.48  ? 357 LYS   B CG   1 
ATOM   941  C CD   . LYS   A 1 142 ? -34.152 0.008   19.238 1.00 65.70  ? 357 LYS   B CD   1 
ATOM   942  C CE   . LYS   A 1 142 ? -35.179 -0.195  18.109 1.00 69.15  ? 357 LYS   B CE   1 
ATOM   943  N NZ   . LYS   A 1 142 ? -36.599 0.024   18.579 1.00 68.34  ? 357 LYS   B NZ   1 
ATOM   944  N N    . VAL   A 1 143 ? -30.269 1.178   22.376 1.00 58.30  ? 358 VAL   B N    1 
ATOM   945  C CA   . VAL   A 1 143 ? -29.458 1.274   23.584 1.00 59.82  ? 358 VAL   B CA   1 
ATOM   946  C C    . VAL   A 1 143 ? -30.389 1.282   24.788 1.00 59.64  ? 358 VAL   B C    1 
ATOM   947  O O    . VAL   A 1 143 ? -31.233 2.176   24.913 1.00 60.08  ? 358 VAL   B O    1 
ATOM   948  C CB   . VAL   A 1 143 ? -28.570 2.528   23.567 1.00 60.61  ? 358 VAL   B CB   1 
ATOM   949  C CG1  . VAL   A 1 143 ? -27.459 2.410   24.591 1.00 59.19  ? 358 VAL   B CG1  1 
ATOM   950  C CG2  . VAL   A 1 143 ? -28.011 2.757   22.166 1.00 57.90  ? 358 VAL   B CG2  1 
ATOM   951  N N    . GLU   A 1 144 ? -30.245 0.292   25.668 1.00 59.47  ? 359 GLU   B N    1 
ATOM   952  C CA   . GLU   A 1 144 ? -31.028 0.205   26.904 1.00 59.27  ? 359 GLU   B CA   1 
ATOM   953  C C    . GLU   A 1 144 ? -30.110 0.264   28.118 1.00 58.58  ? 359 GLU   B C    1 
ATOM   954  O O    . GLU   A 1 144 ? -28.908 -0.014  28.027 1.00 59.32  ? 359 GLU   B O    1 
ATOM   955  C CB   . GLU   A 1 144 ? -31.850 -1.101  26.988 1.00 60.82  ? 359 GLU   B CB   1 
ATOM   956  C CG   . GLU   A 1 144 ? -33.004 -1.259  25.984 1.00 62.52  ? 359 GLU   B CG   1 
ATOM   957  C CD   . GLU   A 1 144 ? -33.241 -2.727  25.579 1.00 69.19  ? 359 GLU   B CD   1 
ATOM   958  O OE1  . GLU   A 1 144 ? -32.256 -3.499  25.428 1.00 68.81  ? 359 GLU   B OE1  1 
ATOM   959  O OE2  . GLU   A 1 144 ? -34.429 -3.107  25.419 1.00 70.48  ? 359 GLU   B OE2  1 
ATOM   960  N N    . THR   A 1 145 ? -30.701 0.584   29.272 1.00 58.86  ? 360 THR   B N    1 
ATOM   961  C CA   . THR   A 1 145 ? -30.011 0.569   30.561 1.00 57.84  ? 360 THR   B CA   1 
ATOM   962  C C    . THR   A 1 145 ? -30.805 -0.245  31.578 1.00 58.80  ? 360 THR   B C    1 
ATOM   963  O O    . THR   A 1 145 ? -32.014 -0.035  31.743 1.00 59.42  ? 360 THR   B O    1 
ATOM   964  C CB   . THR   A 1 145 ? -29.813 1.999   31.079 1.00 64.07  ? 360 THR   B CB   1 
ATOM   965  O OG1  . THR   A 1 145 ? -29.514 2.857   29.973 1.00 66.00  ? 360 THR   B OG1  1 
ATOM   966  C CG2  . THR   A 1 145 ? -28.695 2.080   32.117 1.00 62.73  ? 360 THR   B CG2  1 
ATOM   967  N N    . GLU   A 1 146 ? -30.122 -1.142  32.289 1.00 56.57  ? 361 GLU   B N    1 
ATOM   968  C CA   . GLU   A 1 146 ? -30.765 -2.001  33.276 1.00 58.04  ? 361 GLU   B CA   1 
ATOM   969  C C    . GLU   A 1 146 ? -29.961 -1.978  34.568 1.00 60.75  ? 361 GLU   B C    1 
ATOM   970  O O    . GLU   A 1 146 ? -28.801 -2.402  34.587 1.00 58.81  ? 361 GLU   B O    1 
ATOM   971  C CB   . GLU   A 1 146 ? -30.912 -3.437  32.763 1.00 59.13  ? 361 GLU   B CB   1 
ATOM   972  C CG   . GLU   A 1 146 ? -31.782 -4.314  33.674 1.00 61.22  ? 361 GLU   B CG   1 
ATOM   973  C CD   . GLU   A 1 146 ? -33.188 -3.770  33.840 1.00 61.93  ? 361 GLU   B CD   1 
ATOM   974  O OE1  . GLU   A 1 146 ? -33.670 -3.086  32.909 1.00 62.76  ? 361 GLU   B OE1  1 
ATOM   975  O OE2  . GLU   A 1 146 ? -33.818 -4.032  34.888 1.00 65.65  ? 361 GLU   B OE2  1 
ATOM   976  N N    . ARG   A 1 147 ? -30.578 -1.470  35.635 1.00 62.87  ? 362 ARG   B N    1 
ATOM   977  C CA   . ARG   A 1 147 ? -29.994 -1.507  36.969 1.00 64.59  ? 362 ARG   B CA   1 
ATOM   978  C C    . ARG   A 1 147 ? -30.075 -2.921  37.533 1.00 63.30  ? 362 ARG   B C    1 
ATOM   979  O O    . ARG   A 1 147 ? -30.960 -3.702  37.177 1.00 62.61  ? 362 ARG   B O    1 
ATOM   980  C CB   . ARG   A 1 147 ? -30.720 -0.530  37.904 1.00 68.21  ? 362 ARG   B CB   1 
ATOM   981  C CG   . ARG   A 1 147 ? -29.797 0.249   38.839 1.00 71.10  ? 362 ARG   B CG   1 
ATOM   982  C CD   . ARG   A 1 147 ? -30.570 0.922   39.984 1.00 80.23  ? 362 ARG   B CD   1 
ATOM   983  N NE   . ARG   A 1 147 ? -30.169 2.310   40.207 1.00 87.02  ? 362 ARG   B NE   1 
ATOM   984  C CZ   . ARG   A 1 147 ? -30.890 3.212   40.866 1.00 91.04  ? 362 ARG   B CZ   1 
ATOM   985  N NH1  . ARG   A 1 147 ? -32.067 2.909   41.391 1.00 91.62  ? 362 ARG   B NH1  1 
ATOM   986  N NH2  . ARG   A 1 147 ? -30.413 4.450   41.006 1.00 92.09  ? 362 ARG   B NH2  1 
ATOM   987  N N    . ALA   A 1 148 ? -29.137 -3.252  38.415 1.00 64.92  ? 363 ALA   B N    1 
ATOM   988  C CA   . ALA   A 1 148 ? -29.084 -4.604  38.952 1.00 66.01  ? 363 ALA   B CA   1 
ATOM   989  C C    . ALA   A 1 148 ? -30.209 -4.842  39.952 1.00 67.92  ? 363 ALA   B C    1 
ATOM   990  O O    . ALA   A 1 148 ? -30.786 -3.912  40.528 1.00 70.15  ? 363 ALA   B O    1 
ATOM   991  C CB   . ALA   A 1 148 ? -27.741 -4.875  39.624 1.00 66.15  ? 363 ALA   B CB   1 
ATOM   992  N N    . GLN   A 1 149 ? -30.518 -6.116  40.161 1.00 68.41  ? 364 GLN   B N    1 
ATOM   993  C CA   . GLN   A 1 149 ? -31.558 -6.490  41.106 1.00 73.74  ? 364 GLN   B CA   1 
ATOM   994  C C    . GLN   A 1 149 ? -31.047 -7.656  41.932 1.00 76.98  ? 364 GLN   B C    1 
ATOM   995  O O    . GLN   A 1 149 ? -30.762 -8.729  41.395 1.00 76.40  ? 364 GLN   B O    1 
ATOM   996  C CB   . GLN   A 1 149 ? -32.854 -6.844  40.383 1.00 71.93  ? 364 GLN   B CB   1 
ATOM   997  C CG   . GLN   A 1 149 ? -33.693 -5.613  40.148 1.00 74.24  ? 364 GLN   B CG   1 
ATOM   998  C CD   . GLN   A 1 149 ? -35.068 -5.918  39.607 1.00 78.35  ? 364 GLN   B CD   1 
ATOM   999  O OE1  . GLN   A 1 149 ? -35.409 -5.526  38.491 1.00 81.75  ? 364 GLN   B OE1  1 
ATOM   1000 N NE2  . GLN   A 1 149 ? -35.881 -6.594  40.407 1.00 78.83  ? 364 GLN   B NE2  1 
ATOM   1001 N N    . LEU   A 1 150 ? -30.903 -7.431  43.232 1.00 90.40  ? 365 LEU   B N    1 
ATOM   1002 C CA   . LEU   A 1 150 ? -30.405 -8.470  44.117 1.00 92.01  ? 365 LEU   B CA   1 
ATOM   1003 C C    . LEU   A 1 150 ? -31.330 -9.678  44.075 1.00 94.04  ? 365 LEU   B C    1 
ATOM   1004 O O    . LEU   A 1 150 ? -32.549 -9.545  43.940 1.00 91.47  ? 365 LEU   B O    1 
ATOM   1005 C CB   . LEU   A 1 150 ? -30.288 -7.937  45.539 1.00 94.02  ? 365 LEU   B CB   1 
ATOM   1006 C CG   . LEU   A 1 150 ? -29.209 -8.592  46.404 1.00 98.94  ? 365 LEU   B CG   1 
ATOM   1007 C CD1  . LEU   A 1 150 ? -28.930 -7.764  47.656 1.00 100.59 ? 365 LEU   B CD1  1 
ATOM   1008 C CD2  . LEU   A 1 150 ? -29.613 -10.002 46.781 1.00 101.37 ? 365 LEU   B CD2  1 
ATOM   1009 N N    . GLU   A 1 151 ? -30.732 -10.866 44.139 1.00 89.47  ? 366 GLU   B N    1 
ATOM   1010 C CA   . GLU   A 1 151 ? -31.489 -12.106 44.219 1.00 85.80  ? 366 GLU   B CA   1 
ATOM   1011 C C    . GLU   A 1 151 ? -30.740 -13.051 45.142 1.00 89.30  ? 366 GLU   B C    1 
ATOM   1012 O O    . GLU   A 1 151 ? -30.415 -12.657 46.268 1.00 94.74  ? 366 GLU   B O    1 
ATOM   1013 C CB   . GLU   A 1 151 ? -31.725 -12.681 42.828 1.00 84.81  ? 366 GLU   B CB   1 
ATOM   1014 C CG   . GLU   A 1 151 ? -32.690 -11.802 42.039 1.00 81.05  ? 366 GLU   B CG   1 
ATOM   1015 C CD   . GLU   A 1 151 ? -33.889 -12.562 41.516 1.00 77.68  ? 366 GLU   B CD   1 
ATOM   1016 O OE1  . GLU   A 1 151 ? -33.735 -13.760 41.183 1.00 81.89  ? 366 GLU   B OE1  1 
ATOM   1017 O OE2  . GLU   A 1 151 ? -34.988 -11.965 41.443 1.00 74.63  ? 366 GLU   B OE2  1 
ATOM   1018 N N    . ASP   A 1 152 ? -30.448 -14.283 44.730 1.00 88.32  ? 367 ASP   B N    1 
ATOM   1019 C CA   . ASP   A 1 152 ? -29.841 -15.199 45.700 1.00 92.25  ? 367 ASP   B CA   1 
ATOM   1020 C C    . ASP   A 1 152 ? -28.334 -14.941 45.746 1.00 93.02  ? 367 ASP   B C    1 
ATOM   1021 O O    . ASP   A 1 152 ? -27.513 -15.707 45.234 1.00 92.71  ? 367 ASP   B O    1 
ATOM   1022 C CB   . ASP   A 1 152 ? -30.165 -16.652 45.388 1.00 90.52  ? 367 ASP   B CB   1 
ATOM   1023 C CG   . ASP   A 1 152 ? -30.040 -17.541 46.624 1.00 91.90  ? 367 ASP   B CG   1 
ATOM   1024 O OD1  . ASP   A 1 152 ? -30.270 -17.024 47.747 1.00 89.54  ? 367 ASP   B OD1  1 
ATOM   1025 O OD2  . ASP   A 1 152 ? -29.718 -18.742 46.488 1.00 94.74  ? 367 ASP   B OD2  1 
ATOM   1026 N N    . GLY   A 1 153 ? -27.971 -13.834 46.400 1.00 98.04  ? 368 GLY   B N    1 
ATOM   1027 C CA   . GLY   A 1 153 ? -26.596 -13.378 46.442 1.00 96.78  ? 368 GLY   B CA   1 
ATOM   1028 C C    . GLY   A 1 153 ? -26.199 -12.732 45.132 1.00 96.83  ? 368 GLY   B C    1 
ATOM   1029 O O    . GLY   A 1 153 ? -25.665 -11.618 45.113 1.00 94.87  ? 368 GLY   B O    1 
ATOM   1030 N N    . ARG   A 1 154 ? -26.474 -13.426 44.028 1.00 90.19  ? 369 ARG   B N    1 
ATOM   1031 C CA   . ARG   A 1 154 ? -26.202 -12.908 42.695 1.00 83.09  ? 369 ARG   B CA   1 
ATOM   1032 C C    . ARG   A 1 154 ? -27.106 -11.720 42.372 1.00 80.21  ? 369 ARG   B C    1 
ATOM   1033 O O    . ARG   A 1 154 ? -28.136 -11.482 43.009 1.00 81.66  ? 369 ARG   B O    1 
ATOM   1034 C CB   . ARG   A 1 154 ? -26.402 -13.996 41.634 1.00 79.15  ? 369 ARG   B CB   1 
ATOM   1035 C CG   . ARG   A 1 154 ? -25.220 -14.942 41.468 1.00 82.20  ? 369 ARG   B CG   1 
ATOM   1036 C CD   . ARG   A 1 154 ? -24.612 -14.907 40.045 1.00 78.56  ? 369 ARG   B CD   1 
ATOM   1037 N NE   . ARG   A 1 154 ? -23.704 -16.031 39.818 1.00 78.35  ? 369 ARG   B NE   1 
ATOM   1038 C CZ   . ARG   A 1 154 ? -22.663 -16.018 38.994 1.00 80.65  ? 369 ARG   B CZ   1 
ATOM   1039 N NH1  . ARG   A 1 154 ? -22.360 -14.948 38.272 1.00 73.32  ? 369 ARG   B NH1  1 
ATOM   1040 N NH2  . ARG   A 1 154 ? -21.904 -17.108 38.892 1.00 84.52  ? 369 ARG   B NH2  1 
ATOM   1041 N N    . PHE   A 1 155 ? -26.712 -10.983 41.343 1.00 78.42  ? 370 PHE   B N    1 
ATOM   1042 C CA   . PHE   A 1 155 ? -27.521 -9.914  40.785 1.00 73.35  ? 370 PHE   B CA   1 
ATOM   1043 C C    . PHE   A 1 155 ? -28.040 -10.341 39.420 1.00 69.23  ? 370 PHE   B C    1 
ATOM   1044 O O    . PHE   A 1 155 ? -27.323 -10.974 38.641 1.00 71.04  ? 370 PHE   B O    1 
ATOM   1045 C CB   . PHE   A 1 155 ? -26.699 -8.637  40.698 1.00 69.46  ? 370 PHE   B CB   1 
ATOM   1046 C CG   . PHE   A 1 155 ? -26.409 -8.041  42.035 1.00 74.06  ? 370 PHE   B CG   1 
ATOM   1047 C CD1  . PHE   A 1 155 ? -27.427 -7.912  42.982 1.00 80.28  ? 370 PHE   B CD1  1 
ATOM   1048 C CD2  . PHE   A 1 155 ? -25.142 -7.584  42.350 1.00 73.17  ? 370 PHE   B CD2  1 
ATOM   1049 C CE1  . PHE   A 1 155 ? -27.182 -7.355  44.237 1.00 80.24  ? 370 PHE   B CE1  1 
ATOM   1050 C CE2  . PHE   A 1 155 ? -24.879 -7.036  43.602 1.00 76.97  ? 370 PHE   B CE2  1 
ATOM   1051 C CZ   . PHE   A 1 155 ? -25.908 -6.912  44.551 1.00 76.15  ? 370 PHE   B CZ   1 
ATOM   1052 N N    . VAL   A 1 156 ? -29.297 -10.031 39.148 1.00 66.21  ? 371 VAL   B N    1 
ATOM   1053 C CA   . VAL   A 1 156 ? -29.932 -10.352 37.876 1.00 64.40  ? 371 VAL   B CA   1 
ATOM   1054 C C    . VAL   A 1 156 ? -30.235 -9.045  37.158 1.00 63.37  ? 371 VAL   B C    1 
ATOM   1055 O O    . VAL   A 1 156 ? -30.699 -8.074  37.774 1.00 64.64  ? 371 VAL   B O    1 
ATOM   1056 C CB   . VAL   A 1 156 ? -31.227 -11.166 38.071 1.00 68.32  ? 371 VAL   B CB   1 
ATOM   1057 C CG1  . VAL   A 1 156 ? -31.732 -11.682 36.734 1.00 62.89  ? 371 VAL   B CG1  1 
ATOM   1058 C CG2  . VAL   A 1 156 ? -31.017 -12.297 39.058 1.00 73.19  ? 371 VAL   B CG2  1 
ATOM   1059 N N    . TYR   A 1 157 ? -29.986 -9.021  35.858 1.00 61.03  ? 372 TYR   B N    1 
ATOM   1060 C CA   . TYR   A 1 157 ? -30.312 -7.872  35.020 1.00 60.10  ? 372 TYR   B CA   1 
ATOM   1061 C C    . TYR   A 1 157 ? -31.295 -8.344  33.966 1.00 57.27  ? 372 TYR   B C    1 
ATOM   1062 O O    . TYR   A 1 157 ? -30.980 -9.242  33.185 1.00 56.97  ? 372 TYR   B O    1 
ATOM   1063 C CB   . TYR   A 1 157 ? -29.058 -7.286  34.381 1.00 57.99  ? 372 TYR   B CB   1 
ATOM   1064 C CG   . TYR   A 1 157 ? -27.947 -6.979  35.372 1.00 61.79  ? 372 TYR   B CG   1 
ATOM   1065 C CD1  . TYR   A 1 157 ? -27.170 -7.995  35.924 1.00 60.55  ? 372 TYR   B CD1  1 
ATOM   1066 C CD2  . TYR   A 1 157 ? -27.670 -5.670  35.747 1.00 61.90  ? 372 TYR   B CD2  1 
ATOM   1067 C CE1  . TYR   A 1 157 ? -26.150 -7.712  36.813 1.00 59.96  ? 372 TYR   B CE1  1 
ATOM   1068 C CE2  . TYR   A 1 157 ? -26.657 -5.380  36.637 1.00 61.60  ? 372 TYR   B CE2  1 
ATOM   1069 C CZ   . TYR   A 1 157 ? -25.895 -6.404  37.157 1.00 61.62  ? 372 TYR   B CZ   1 
ATOM   1070 O OH   . TYR   A 1 157 ? -24.886 -6.108  38.044 1.00 65.49  ? 372 TYR   B OH   1 
ATOM   1071 N N    . ARG   A 1 158 ? -32.493 -7.806  33.986 1.00 55.55  ? 373 ARG   B N    1 
ATOM   1072 C CA   . ARG   A 1 158 ? -33.553 -8.370  33.200 1.00 55.35  ? 373 ARG   B CA   1 
ATOM   1073 C C    . ARG   A 1 158 ? -34.120 -7.384  32.237 1.00 53.78  ? 373 ARG   B C    1 
ATOM   1074 O O    . ARG   A 1 158 ? -34.721 -6.414  32.617 1.00 52.06  ? 373 ARG   B O    1 
ATOM   1075 C CB   . ARG   A 1 158 ? -34.663 -8.868  34.099 1.00 54.58  ? 373 ARG   B CB   1 
ATOM   1076 C CG   . ARG   A 1 158 ? -34.305 -10.084 34.893 1.00 56.75  ? 373 ARG   B CG   1 
ATOM   1077 C CD   . ARG   A 1 158 ? -35.550 -10.763 35.387 1.00 64.67  ? 373 ARG   B CD   1 
ATOM   1078 N NE   . ARG   A 1 158 ? -35.584 -10.720 36.821 1.00 71.36  ? 373 ARG   B NE   1 
ATOM   1079 C CZ   . ARG   A 1 158 ? -35.240 -11.735 37.597 1.00 71.32  ? 373 ARG   B CZ   1 
ATOM   1080 N NH1  . ARG   A 1 158 ? -34.859 -12.886 37.070 1.00 63.71  ? 373 ARG   B NH1  1 
ATOM   1081 N NH2  . ARG   A 1 158 ? -35.284 -11.602 38.907 1.00 72.65  ? 373 ARG   B NH2  1 
ATOM   1082 N N    . LEU   A 1 159 ? -33.915 -7.667  30.971 1.00 51.97  ? 374 LEU   B N    1 
ATOM   1083 C CA   . LEU   A 1 159 ? -34.462 -6.890  29.864 1.00 50.73  ? 374 LEU   B CA   1 
ATOM   1084 C C    . LEU   A 1 159 ? -35.357 -7.846  29.085 1.00 53.21  ? 374 LEU   B C    1 
ATOM   1085 O O    . LEU   A 1 159 ? -34.962 -8.429  28.064 1.00 50.69  ? 374 LEU   B O    1 
ATOM   1086 C CB   . LEU   A 1 159 ? -33.357 -6.313  29.004 1.00 51.03  ? 374 LEU   B CB   1 
ATOM   1087 C CG   . LEU   A 1 159 ? -32.189 -5.698  29.779 1.00 54.89  ? 374 LEU   B CG   1 
ATOM   1088 C CD1  . LEU   A 1 159 ? -31.161 -6.767  30.186 1.00 50.85  ? 374 LEU   B CD1  1 
ATOM   1089 C CD2  . LEU   A 1 159 ? -31.530 -4.580  28.970 1.00 58.15  ? 374 LEU   B CD2  1 
ATOM   1090 N N    . LEU   A 1 160 ? -36.555 -8.047  29.603 1.00 49.07  ? 375 LEU   B N    1 
ATOM   1091 C CA   . LEU   A 1 160 ? -37.458 -9.049  29.070 1.00 50.83  ? 375 LEU   B CA   1 
ATOM   1092 C C    . LEU   A 1 160 ? -38.485 -8.392  28.162 1.00 49.47  ? 375 LEU   B C    1 
ATOM   1093 O O    . LEU   A 1 160 ? -38.949 -7.279  28.420 1.00 48.24  ? 375 LEU   B O    1 
ATOM   1094 C CB   . LEU   A 1 160 ? -38.157 -9.815  30.204 1.00 51.91  ? 375 LEU   B CB   1 
ATOM   1095 C CG   . LEU   A 1 160 ? -37.148 -10.423 31.178 1.00 53.19  ? 375 LEU   B CG   1 
ATOM   1096 C CD1  . LEU   A 1 160 ? -37.852 -11.108 32.290 1.00 54.57  ? 375 LEU   B CD1  1 
ATOM   1097 C CD2  . LEU   A 1 160 ? -36.216 -11.387 30.474 1.00 48.81  ? 375 LEU   B CD2  1 
ATOM   1098 N N    . ARG   A 1 161 ? -38.822 -9.079  27.080 1.00 51.87  ? 376 ARG   B N    1 
ATOM   1099 C CA   . ARG   A 1 161 ? -39.950 -8.673  26.253 1.00 51.56  ? 376 ARG   B CA   1 
ATOM   1100 C C    . ARG   A 1 161 ? -39.792 -7.267  25.665 1.00 48.83  ? 376 ARG   B C    1 
ATOM   1101 O O    . ARG   A 1 161 ? -40.791 -6.596  25.411 1.00 49.47  ? 376 ARG   B O    1 
ATOM   1102 C CB   . ARG   A 1 161 ? -41.247 -8.777  27.051 1.00 50.70  ? 376 ARG   B CB   1 
ATOM   1103 C CG   . ARG   A 1 161 ? -41.478 -10.177 27.607 1.00 54.53  ? 376 ARG   B CG   1 
ATOM   1104 C CD   . ARG   A 1 161 ? -42.758 -10.293 28.420 1.00 55.14  ? 376 ARG   B CD   1 
ATOM   1105 N NE   . ARG   A 1 161 ? -43.956 -10.093 27.611 1.00 57.60  ? 376 ARG   B NE   1 
ATOM   1106 C CZ   . ARG   A 1 161 ? -44.404 -10.956 26.706 1.00 57.32  ? 376 ARG   B CZ   1 
ATOM   1107 N NH1  . ARG   A 1 161 ? -43.723 -12.055 26.399 1.00 56.06  ? 376 ARG   B NH1  1 
ATOM   1108 N NH2  . ARG   A 1 161 ? -45.568 -10.714 26.100 1.00 59.46  ? 376 ARG   B NH2  1 
ATOM   1109 N N    . SER   A 1 162 ? -38.555 -6.810  25.409 1.00 46.68  ? 377 SER   B N    1 
ATOM   1110 C CA   . SER   A 1 162 ? -38.382 -5.613  24.591 1.00 48.46  ? 377 SER   B CA   1 
ATOM   1111 C C    . SER   A 1 162 ? -39.060 -5.855  23.249 1.00 48.65  ? 377 SER   B C    1 
ATOM   1112 O O    . SER   A 1 162 ? -38.789 -6.880  22.597 1.00 49.74  ? 377 SER   B O    1 
ATOM   1113 C CB   . SER   A 1 162 ? -36.911 -5.287  24.332 1.00 47.31  ? 377 SER   B CB   1 
ATOM   1114 O OG   . SER   A 1 162 ? -36.100 -5.662  25.425 1.00 55.99  ? 377 SER   B OG   1 
ATOM   1115 N N    . PRO   A 1 163 ? -39.921 -4.955  22.790 1.00 49.62  ? 378 PRO   B N    1 
ATOM   1116 C CA   . PRO   A 1 163 ? -40.461 -5.096  21.429 1.00 49.86  ? 378 PRO   B CA   1 
ATOM   1117 C C    . PRO   A 1 163 ? -39.349 -5.082  20.390 1.00 50.42  ? 378 PRO   B C    1 
ATOM   1118 O O    . PRO   A 1 163 ? -38.470 -4.213  20.393 1.00 49.86  ? 378 PRO   B O    1 
ATOM   1119 C CB   . PRO   A 1 163 ? -41.384 -3.890  21.288 1.00 51.98  ? 378 PRO   B CB   1 
ATOM   1120 C CG   . PRO   A 1 163 ? -41.701 -3.484  22.724 1.00 52.89  ? 378 PRO   B CG   1 
ATOM   1121 C CD   . PRO   A 1 163 ? -40.440 -3.770  23.481 1.00 50.62  ? 378 PRO   B CD   1 
ATOM   1122 N N    . MET   A 1 164 ? -39.382 -6.075  19.506 1.00 49.00  ? 379 MET   B N    1 
ATOM   1123 C CA   . MET   A 1 164 ? -38.439 -6.124  18.404 1.00 50.30  ? 379 MET   B CA   1 
ATOM   1124 C C    . MET   A 1 164 ? -38.630 -4.882  17.538 1.00 51.95  ? 379 MET   B C    1 
ATOM   1125 O O    . MET   A 1 164 ? -39.760 -4.450  17.292 1.00 50.84  ? 379 MET   B O    1 
ATOM   1126 C CB   . MET   A 1 164 ? -38.667 -7.416  17.609 1.00 46.77  ? 379 MET   B CB   1 
ATOM   1127 C CG   . MET   A 1 164 ? -37.502 -7.836  16.805 1.00 51.73  ? 379 MET   B CG   1 
ATOM   1128 S SD   . MET   A 1 164 ? -37.624 -9.487  16.073 1.00 49.56  ? 379 MET   B SD   1 
ATOM   1129 C CE   . MET   A 1 164 ? -39.349 -9.775  15.903 1.00 49.93  ? 379 MET   B CE   1 
ATOM   1130 N N    . CYS   A 1 165 ? -37.530 -4.270  17.101 1.00 54.19  ? 380 CYS   B N    1 
ATOM   1131 C CA   . CYS   A 1 165 ? -37.682 -3.070  16.285 1.00 58.78  ? 380 CYS   B CA   1 
ATOM   1132 C C    . CYS   A 1 165 ? -38.315 -3.435  14.949 1.00 58.44  ? 380 CYS   B C    1 
ATOM   1133 O O    . CYS   A 1 165 ? -38.067 -4.513  14.406 1.00 58.53  ? 380 CYS   B O    1 
ATOM   1134 C CB   . CYS   A 1 165 ? -36.339 -2.364  16.063 1.00 62.85  ? 380 CYS   B CB   1 
ATOM   1135 S SG   . CYS   A 1 165 ? -34.948 -3.390  15.571 1.00 63.95  ? 380 CYS   B SG   1 
ATOM   1136 N N    . GLU   A 1 166 ? -39.150 -2.536  14.418 1.00 63.86  ? 381 GLU   B N    1 
ATOM   1137 C CA   . GLU   A 1 166 ? -39.899 -2.859  13.205 1.00 68.01  ? 381 GLU   B CA   1 
ATOM   1138 C C    . GLU   A 1 166 ? -39.016 -3.099  11.976 1.00 66.32  ? 381 GLU   B C    1 
ATOM   1139 O O    . GLU   A 1 166 ? -39.519 -3.604  10.960 1.00 64.33  ? 381 GLU   B O    1 
ATOM   1140 C CB   . GLU   A 1 166 ? -40.897 -1.757  12.883 1.00 75.20  ? 381 GLU   B CB   1 
ATOM   1141 C CG   . GLU   A 1 166 ? -42.325 -2.076  13.227 1.00 84.11  ? 381 GLU   B CG   1 
ATOM   1142 C CD   . GLU   A 1 166 ? -43.155 -0.819  13.205 1.00 105.26 ? 381 GLU   B CD   1 
ATOM   1143 O OE1  . GLU   A 1 166 ? -44.297 -0.789  13.732 1.00 111.03 ? 381 GLU   B OE1  1 
ATOM   1144 O OE2  . GLU   A 1 166 ? -42.627 0.161   12.649 1.00 108.00 ? 381 GLU   B OE2  1 
ATOM   1145 N N    . TYR   A 1 167 ? -37.732 -2.739  12.011 1.00 64.05  ? 382 TYR   B N    1 
ATOM   1146 C CA   . TYR   A 1 167 ? -36.881 -3.126  10.894 1.00 60.12  ? 382 TYR   B CA   1 
ATOM   1147 C C    . TYR   A 1 167 ? -36.706 -4.636  10.870 1.00 58.28  ? 382 TYR   B C    1 
ATOM   1148 O O    . TYR   A 1 167 ? -36.730 -5.255  9.797  1.00 58.41  ? 382 TYR   B O    1 
ATOM   1149 C CB   . TYR   A 1 167 ? -35.519 -2.424  10.961 1.00 59.17  ? 382 TYR   B CB   1 
ATOM   1150 C CG   . TYR   A 1 167 ? -34.537 -2.953  9.926  1.00 62.85  ? 382 TYR   B CG   1 
ATOM   1151 C CD1  . TYR   A 1 167 ? -33.776 -4.093  10.168 1.00 60.11  ? 382 TYR   B CD1  1 
ATOM   1152 C CD2  . TYR   A 1 167 ? -34.397 -2.327  8.690  1.00 64.03  ? 382 TYR   B CD2  1 
ATOM   1153 C CE1  . TYR   A 1 167 ? -32.903 -4.594  9.208  1.00 60.54  ? 382 TYR   B CE1  1 
ATOM   1154 C CE2  . TYR   A 1 167 ? -33.529 -2.810  7.739  1.00 60.48  ? 382 TYR   B CE2  1 
ATOM   1155 C CZ   . TYR   A 1 167 ? -32.782 -3.932  8.002  1.00 61.71  ? 382 TYR   B CZ   1 
ATOM   1156 O OH   . TYR   A 1 167 ? -31.915 -4.389  7.037  1.00 65.17  ? 382 TYR   B OH   1 
ATOM   1157 N N    . LEU   A 1 168 ? -36.520 -5.250  12.042 1.00 61.42  ? 383 LEU   B N    1 
ATOM   1158 C CA   . LEU   A 1 168 ? -36.297 -6.693  12.086 1.00 56.71  ? 383 LEU   B CA   1 
ATOM   1159 C C    . LEU   A 1 168 ? -37.589 -7.460  11.845 1.00 56.07  ? 383 LEU   B C    1 
ATOM   1160 O O    . LEU   A 1 168 ? -37.588 -8.479  11.149 1.00 54.76  ? 383 LEU   B O    1 
ATOM   1161 C CB   . LEU   A 1 168 ? -35.676 -7.093  13.412 1.00 55.92  ? 383 LEU   B CB   1 
ATOM   1162 C CG   . LEU   A 1 168 ? -34.153 -6.971  13.519 1.00 58.52  ? 383 LEU   B CG   1 
ATOM   1163 C CD1  . LEU   A 1 168 ? -33.720 -7.176  14.983 1.00 58.96  ? 383 LEU   B CD1  1 
ATOM   1164 C CD2  . LEU   A 1 168 ? -33.444 -7.964  12.601 1.00 54.23  ? 383 LEU   B CD2  1 
ATOM   1165 N N    . VAL   A 1 169 ? -38.707 -6.983  12.391 1.00 59.87  ? 384 VAL   B N    1 
ATOM   1166 C CA   . VAL   A 1 169 ? -39.978 -7.640  12.113 1.00 58.19  ? 384 VAL   B CA   1 
ATOM   1167 C C    . VAL   A 1 169 ? -40.251 -7.626  10.620 1.00 56.44  ? 384 VAL   B C    1 
ATOM   1168 O O    . VAL   A 1 169 ? -40.636 -8.642  10.033 1.00 56.49  ? 384 VAL   B O    1 
ATOM   1169 C CB   . VAL   A 1 169 ? -41.121 -6.983  12.901 1.00 56.67  ? 384 VAL   B CB   1 
ATOM   1170 C CG1  . VAL   A 1 169 ? -42.401 -7.753  12.665 1.00 55.40  ? 384 VAL   B CG1  1 
ATOM   1171 C CG2  . VAL   A 1 169 ? -40.784 -6.936  14.380 1.00 55.69  ? 384 VAL   B CG2  1 
ATOM   1172 N N    . ASN   A 1 170 ? -40.060 -6.470  9.979  1.00 56.20  ? 385 ASN   B N    1 
ATOM   1173 C CA   . ASN   A 1 170 ? -40.162 -6.417  8.524  1.00 52.67  ? 385 ASN   B CA   1 
ATOM   1174 C C    . ASN   A 1 170 ? -39.139 -7.334  7.870  1.00 53.10  ? 385 ASN   B C    1 
ATOM   1175 O O    . ASN   A 1 170 ? -39.484 -8.161  7.017  1.00 52.17  ? 385 ASN   B O    1 
ATOM   1176 C CB   . ASN   A 1 170 ? -39.973 -4.988  8.029  1.00 60.98  ? 385 ASN   B CB   1 
ATOM   1177 C CG   . ASN   A 1 170 ? -41.170 -4.122  8.299  1.00 67.16  ? 385 ASN   B CG   1 
ATOM   1178 O OD1  . ASN   A 1 170 ? -42.247 -4.623  8.632  1.00 69.33  ? 385 ASN   B OD1  1 
ATOM   1179 N ND2  . ASN   A 1 170 ? -40.999 -2.811  8.155  1.00 70.63  ? 385 ASN   B ND2  1 
ATOM   1180 N N    . PHE   A 1 171 ? -37.866 -7.193  8.242  1.00 52.19  ? 386 PHE   B N    1 
ATOM   1181 C CA   . PHE   A 1 171 ? -36.846 -8.033  7.633  1.00 51.42  ? 386 PHE   B CA   1 
ATOM   1182 C C    . PHE   A 1 171 ? -37.231 -9.516  7.713  1.00 56.53  ? 386 PHE   B C    1 
ATOM   1183 O O    . PHE   A 1 171 ? -37.211 -10.226 6.697  1.00 56.16  ? 386 PHE   B O    1 
ATOM   1184 C CB   . PHE   A 1 171 ? -35.487 -7.765  8.283  1.00 50.60  ? 386 PHE   B CB   1 
ATOM   1185 C CG   . PHE   A 1 171 ? -34.398 -8.685  7.787  1.00 53.64  ? 386 PHE   B CG   1 
ATOM   1186 C CD1  . PHE   A 1 171 ? -33.976 -8.631  6.454  1.00 55.06  ? 386 PHE   B CD1  1 
ATOM   1187 C CD2  . PHE   A 1 171 ? -33.825 -9.629  8.629  1.00 51.08  ? 386 PHE   B CD2  1 
ATOM   1188 C CE1  . PHE   A 1 171 ? -32.983 -9.490  5.978  1.00 52.35  ? 386 PHE   B CE1  1 
ATOM   1189 C CE2  . PHE   A 1 171 ? -32.833 -10.483 8.174  1.00 54.58  ? 386 PHE   B CE2  1 
ATOM   1190 C CZ   . PHE   A 1 171 ? -32.404 -10.413 6.832  1.00 52.46  ? 386 PHE   B CZ   1 
ATOM   1191 N N    . LEU   A 1 172 ? -37.625 -9.993  8.909  1.00 54.26  ? 387 LEU   B N    1 
ATOM   1192 C CA   . LEU   A 1 172 ? -38.005 -11.395 9.085  1.00 53.07  ? 387 LEU   B CA   1 
ATOM   1193 C C    . LEU   A 1 172 ? -39.157 -11.788 8.171  1.00 54.94  ? 387 LEU   B C    1 
ATOM   1194 O O    . LEU   A 1 172 ? -39.131 -12.850 7.542  1.00 53.85  ? 387 LEU   B O    1 
ATOM   1195 C CB   . LEU   A 1 172 ? -38.396 -11.668 10.535 1.00 51.88  ? 387 LEU   B CB   1 
ATOM   1196 C CG   . LEU   A 1 172 ? -37.284 -11.781 11.562 1.00 54.58  ? 387 LEU   B CG   1 
ATOM   1197 C CD1  . LEU   A 1 172 ? -37.891 -11.638 12.964 1.00 53.31  ? 387 LEU   B CD1  1 
ATOM   1198 C CD2  . LEU   A 1 172 ? -36.497 -13.085 11.418 1.00 49.48  ? 387 LEU   B CD2  1 
ATOM   1199 N N    . HIS   A 1 173 ? -40.203 -10.972 8.120  1.00 49.63  ? 388 HIS   B N    1 
ATOM   1200 C CA   . HIS   A 1 173 ? -41.291 -11.268 7.195  1.00 55.45  ? 388 HIS   B CA   1 
ATOM   1201 C C    . HIS   A 1 173 ? -40.771 -11.404 5.765  1.00 56.76  ? 388 HIS   B C    1 
ATOM   1202 O O    . HIS   A 1 173 ? -41.073 -12.381 5.070  1.00 60.01  ? 388 HIS   B O    1 
ATOM   1203 C CB   . HIS   A 1 173 ? -42.359 -10.178 7.290  1.00 57.62  ? 388 HIS   B CB   1 
ATOM   1204 C CG   . HIS   A 1 173 ? -43.400 -10.475 8.316  1.00 66.37  ? 388 HIS   B CG   1 
ATOM   1205 N ND1  . HIS   A 1 173 ? -44.148 -11.633 8.290  1.00 70.52  ? 388 HIS   B ND1  1 
ATOM   1206 C CD2  . HIS   A 1 173 ? -43.748 -9.822  9.453  1.00 65.23  ? 388 HIS   B CD2  1 
ATOM   1207 C CE1  . HIS   A 1 173 ? -44.950 -11.654 9.342  1.00 74.28  ? 388 HIS   B CE1  1 
ATOM   1208 N NE2  . HIS   A 1 173 ? -44.730 -10.566 10.061 1.00 67.21  ? 388 HIS   B NE2  1 
ATOM   1209 N N    . LYS   A 1 174 ? -39.977 -10.433 5.307  1.00 52.02  ? 389 LYS   B N    1 
ATOM   1210 C CA   . LYS   A 1 174 ? -39.394 -10.552 3.975  1.00 59.58  ? 389 LYS   B CA   1 
ATOM   1211 C C    . LYS   A 1 174 ? -38.627 -11.862 3.818  1.00 59.21  ? 389 LYS   B C    1 
ATOM   1212 O O    . LYS   A 1 174 ? -38.747 -12.543 2.793  1.00 58.70  ? 389 LYS   B O    1 
ATOM   1213 C CB   . LYS   A 1 174 ? -38.478 -9.367  3.694  1.00 54.59  ? 389 LYS   B CB   1 
ATOM   1214 C CG   . LYS   A 1 174 ? -39.194 -8.129  3.271  1.00 52.46  ? 389 LYS   B CG   1 
ATOM   1215 C CD   . LYS   A 1 174 ? -38.308 -6.987  3.601  1.00 55.19  ? 389 LYS   B CD   1 
ATOM   1216 C CE   . LYS   A 1 174 ? -39.019 -5.662  3.496  1.00 55.77  ? 389 LYS   B CE   1 
ATOM   1217 N NZ   . LYS   A 1 174 ? -38.056 -4.696  4.070  1.00 64.49  ? 389 LYS   B NZ   1 
ATOM   1218 N N    . LEU   A 1 175 ? -37.831 -12.231 4.830  1.00 54.74  ? 390 LEU   B N    1 
ATOM   1219 C CA   . LEU   A 1 175 ? -37.009 -13.432 4.715  1.00 53.76  ? 390 LEU   B CA   1 
ATOM   1220 C C    . LEU   A 1 175 ? -37.876 -14.686 4.662  1.00 56.08  ? 390 LEU   B C    1 
ATOM   1221 O O    . LEU   A 1 175 ? -37.571 -15.634 3.926  1.00 58.46  ? 390 LEU   B O    1 
ATOM   1222 C CB   . LEU   A 1 175 ? -36.034 -13.492 5.885  1.00 52.33  ? 390 LEU   B CB   1 
ATOM   1223 C CG   . LEU   A 1 175 ? -34.638 -14.068 5.736  1.00 52.52  ? 390 LEU   B CG   1 
ATOM   1224 C CD1  . LEU   A 1 175 ? -33.982 -13.427 4.536  1.00 52.31  ? 390 LEU   B CD1  1 
ATOM   1225 C CD2  . LEU   A 1 175 ? -33.830 -13.791 6.993  1.00 51.23  ? 390 LEU   B CD2  1 
ATOM   1226 N N    . ARG   A 1 176 ? -38.970 -14.703 5.430  1.00 56.96  ? 391 ARG   B N    1 
ATOM   1227 C CA   . ARG   A 1 176 ? -39.917 -15.815 5.394  1.00 58.36  ? 391 ARG   B CA   1 
ATOM   1228 C C    . ARG   A 1 176 ? -40.363 -16.131 3.972  1.00 60.51  ? 391 ARG   B C    1 
ATOM   1229 O O    . ARG   A 1 176 ? -40.616 -17.295 3.649  1.00 60.47  ? 391 ARG   B O    1 
ATOM   1230 C CB   . ARG   A 1 176 ? -41.130 -15.466 6.257  1.00 61.05  ? 391 ARG   B CB   1 
ATOM   1231 C CG   . ARG   A 1 176 ? -42.075 -16.591 6.642  1.00 65.37  ? 391 ARG   B CG   1 
ATOM   1232 C CD   . ARG   A 1 176 ? -42.879 -16.096 7.850  1.00 70.12  ? 391 ARG   B CD   1 
ATOM   1233 N NE   . ARG   A 1 176 ? -43.669 -17.115 8.534  1.00 74.62  ? 391 ARG   B NE   1 
ATOM   1234 C CZ   . ARG   A 1 176 ? -44.883 -16.911 9.033  1.00 75.00  ? 391 ARG   B CZ   1 
ATOM   1235 N NH1  . ARG   A 1 176 ? -45.474 -15.725 8.968  1.00 72.56  ? 391 ARG   B NH1  1 
ATOM   1236 N NH2  . ARG   A 1 176 ? -45.523 -17.924 9.611  1.00 75.91  ? 391 ARG   B NH2  1 
ATOM   1237 N N    . GLN   A 1 177 ? -40.450 -15.110 3.111  1.00 59.95  ? 392 GLN   B N    1 
ATOM   1238 C CA   . GLN   A 1 177 ? -41.030 -15.254 1.776  1.00 62.99  ? 392 GLN   B CA   1 
ATOM   1239 C C    . GLN   A 1 177 ? -40.080 -15.879 0.766  1.00 62.72  ? 392 GLN   B C    1 
ATOM   1240 O O    . GLN   A 1 177 ? -40.539 -16.484 -0.214 1.00 62.37  ? 392 GLN   B O    1 
ATOM   1241 C CB   . GLN   A 1 177 ? -41.462 -13.886 1.236  1.00 67.40  ? 392 GLN   B CB   1 
ATOM   1242 C CG   . GLN   A 1 177 ? -42.936 -13.639 1.432  1.00 73.61  ? 392 GLN   B CG   1 
ATOM   1243 C CD   . GLN   A 1 177 ? -43.267 -12.184 1.649  1.00 75.24  ? 392 GLN   B CD   1 
ATOM   1244 O OE1  . GLN   A 1 177 ? -42.784 -11.300 0.925  1.00 71.79  ? 392 GLN   B OE1  1 
ATOM   1245 N NE2  . GLN   A 1 177 ? -44.062 -11.916 2.692  1.00 75.66  ? 392 GLN   B NE2  1 
ATOM   1246 N N    . LEU   A 1 178 ? -38.779 -15.700 0.945  1.00 60.09  ? 393 LEU   B N    1 
ATOM   1247 C CA   . LEU   A 1 178 ? -37.837 -16.144 -0.066 1.00 57.89  ? 393 LEU   B CA   1 
ATOM   1248 C C    . LEU   A 1 178 ? -38.145 -17.588 -0.459 1.00 59.29  ? 393 LEU   B C    1 
ATOM   1249 O O    . LEU   A 1 178 ? -38.556 -18.387 0.396  1.00 57.33  ? 393 LEU   B O    1 
ATOM   1250 C CB   . LEU   A 1 178 ? -36.412 -16.017 0.462  1.00 55.78  ? 393 LEU   B CB   1 
ATOM   1251 C CG   . LEU   A 1 178 ? -36.012 -14.613 0.900  1.00 53.81  ? 393 LEU   B CG   1 
ATOM   1252 C CD1  . LEU   A 1 178 ? -34.523 -14.605 1.109  1.00 55.32  ? 393 LEU   B CD1  1 
ATOM   1253 C CD2  . LEU   A 1 178 ? -36.415 -13.555 -0.123 1.00 54.52  ? 393 LEU   B CD2  1 
ATOM   1254 N N    . PRO   A 1 179 ? -37.979 -17.954 -1.737 1.00 56.03  ? 394 PRO   B N    1 
ATOM   1255 C CA   . PRO   A 1 179 ? -38.443 -19.269 -2.205 1.00 55.70  ? 394 PRO   B CA   1 
ATOM   1256 C C    . PRO   A 1 179 ? -37.515 -20.422 -1.868 1.00 57.04  ? 394 PRO   B C    1 
ATOM   1257 O O    . PRO   A 1 179 ? -37.919 -21.578 -2.041 1.00 59.44  ? 394 PRO   B O    1 
ATOM   1258 C CB   . PRO   A 1 179 ? -38.540 -19.085 -3.736 1.00 53.33  ? 394 PRO   B CB   1 
ATOM   1259 C CG   . PRO   A 1 179 ? -38.294 -17.600 -3.997 1.00 54.79  ? 394 PRO   B CG   1 
ATOM   1260 C CD   . PRO   A 1 179 ? -37.449 -17.144 -2.847 1.00 55.53  ? 394 PRO   B CD   1 
ATOM   1261 N N    . GLU   A 1 180 ? -36.302 -20.164 -1.386 1.00 54.02  ? 395 GLU   B N    1 
ATOM   1262 C CA   . GLU   A 1 180 ? -35.307 -21.217 -1.227 1.00 53.27  ? 395 GLU   B CA   1 
ATOM   1263 C C    . GLU   A 1 180 ? -34.452 -20.925 -0.000 1.00 53.49  ? 395 GLU   B C    1 
ATOM   1264 O O    . GLU   A 1 180 ? -34.063 -19.776 0.227  1.00 53.51  ? 395 GLU   B O    1 
ATOM   1265 C CB   . GLU   A 1 180 ? -34.409 -21.299 -2.462 1.00 56.26  ? 395 GLU   B CB   1 
ATOM   1266 C CG   . GLU   A 1 180 ? -35.079 -21.623 -3.781 1.00 54.67  ? 395 GLU   B CG   1 
ATOM   1267 C CD   . GLU   A 1 180 ? -35.303 -23.097 -3.929 1.00 61.27  ? 395 GLU   B CD   1 
ATOM   1268 O OE1  . GLU   A 1 180 ? -36.065 -23.515 -4.848 1.00 61.45  ? 395 GLU   B OE1  1 
ATOM   1269 O OE2  . GLU   A 1 180 ? -34.757 -23.836 -3.065 1.00 60.92  ? 395 GLU   B OE2  1 
ATOM   1270 N N    . ARG   A 1 181 ? -34.138 -21.969 0.774  1.00 55.34  ? 396 ARG   B N    1 
ATOM   1271 C CA   . ARG   A 1 181 ? -33.311 -21.777 1.966  1.00 52.91  ? 396 ARG   B CA   1 
ATOM   1272 C C    . ARG   A 1 181 ? -31.963 -21.169 1.600  1.00 49.88  ? 396 ARG   B C    1 
ATOM   1273 O O    . ARG   A 1 181 ? -31.451 -20.295 2.313  1.00 46.26  ? 396 ARG   B O    1 
ATOM   1274 C CB   . ARG   A 1 181 ? -33.121 -23.109 2.713  1.00 57.45  ? 396 ARG   B CB   1 
ATOM   1275 C CG   . ARG   A 1 181 ? -34.221 -23.400 3.749  1.00 64.83  ? 396 ARG   B CG   1 
ATOM   1276 C CD   . ARG   A 1 181 ? -33.871 -24.541 4.737  1.00 73.05  ? 396 ARG   B CD   1 
ATOM   1277 N NE   . ARG   A 1 181 ? -32.528 -24.419 5.298  1.00 71.27  ? 396 ARG   B NE   1 
ATOM   1278 C CZ   . ARG   A 1 181 ? -31.502 -25.186 4.963  1.00 71.41  ? 396 ARG   B CZ   1 
ATOM   1279 N NH1  . ARG   A 1 181 ? -31.633 -26.169 4.089  1.00 76.31  ? 396 ARG   B NH1  1 
ATOM   1280 N NH2  . ARG   A 1 181 ? -30.319 -24.969 5.530  1.00 71.36  ? 396 ARG   B NH2  1 
ATOM   1281 N N    . TYR   A 1 182 ? -31.377 -21.594 0.477  1.00 48.38  ? 397 TYR   B N    1 
ATOM   1282 C CA   . TYR   A 1 182 ? -30.062 -21.066 0.151  1.00 47.58  ? 397 TYR   B CA   1 
ATOM   1283 C C    . TYR   A 1 182 ? -30.113 -19.581 -0.177 1.00 46.32  ? 397 TYR   B C    1 
ATOM   1284 O O    . TYR   A 1 182 ? -29.068 -18.916 -0.091 1.00 46.36  ? 397 TYR   B O    1 
ATOM   1285 C CB   . TYR   A 1 182 ? -29.419 -21.853 -0.996 1.00 53.55  ? 397 TYR   B CB   1 
ATOM   1286 C CG   . TYR   A 1 182 ? -29.841 -21.393 -2.364 1.00 52.59  ? 397 TYR   B CG   1 
ATOM   1287 C CD1  . TYR   A 1 182 ? -29.271 -20.265 -2.957 1.00 52.92  ? 397 TYR   B CD1  1 
ATOM   1288 C CD2  . TYR   A 1 182 ? -30.819 -22.079 -3.056 1.00 54.11  ? 397 TYR   B CD2  1 
ATOM   1289 C CE1  . TYR   A 1 182 ? -29.679 -19.843 -4.225 1.00 56.90  ? 397 TYR   B CE1  1 
ATOM   1290 C CE2  . TYR   A 1 182 ? -31.220 -21.679 -4.301 1.00 57.37  ? 397 TYR   B CE2  1 
ATOM   1291 C CZ   . TYR   A 1 182 ? -30.658 -20.565 -4.874 1.00 56.10  ? 397 TYR   B CZ   1 
ATOM   1292 O OH   . TYR   A 1 182 ? -31.107 -20.195 -6.093 1.00 58.22  ? 397 TYR   B OH   1 
ATOM   1293 N N    . MET   A 1 183 ? -31.292 -19.026 -0.517 1.00 45.70  ? 398 MET   B N    1 
ATOM   1294 C CA   . MET   A 1 183 ? -31.360 -17.572 -0.709 1.00 47.54  ? 398 MET   B CA   1 
ATOM   1295 C C    . MET   A 1 183 ? -31.412 -16.829 0.614  1.00 48.53  ? 398 MET   B C    1 
ATOM   1296 O O    . MET   A 1 183 ? -30.689 -15.832 0.796  1.00 45.50  ? 398 MET   B O    1 
ATOM   1297 C CB   . MET   A 1 183 ? -32.548 -17.159 -1.582 1.00 49.45  ? 398 MET   B CB   1 
ATOM   1298 C CG   . MET   A 1 183 ? -32.476 -17.689 -2.969 1.00 49.12  ? 398 MET   B CG   1 
ATOM   1299 S SD   . MET   A 1 183 ? -33.987 -17.413 -3.914 1.00 53.40  ? 398 MET   B SD   1 
ATOM   1300 C CE   . MET   A 1 183 ? -33.527 -18.226 -5.454 1.00 54.41  ? 398 MET   B CE   1 
ATOM   1301 N N    . MET   A 1 184 ? -32.284 -17.273 1.538  1.00 49.20  ? 399 MET   B N    1 
ATOM   1302 C CA   . MET   A 1 184 ? -32.230 -16.788 2.917  1.00 48.46  ? 399 MET   B CA   1 
ATOM   1303 C C    . MET   A 1 184 ? -30.798 -16.816 3.417  1.00 44.92  ? 399 MET   B C    1 
ATOM   1304 O O    . MET   A 1 184 ? -30.290 -15.840 3.976  1.00 44.17  ? 399 MET   B O    1 
ATOM   1305 C CB   . MET   A 1 184 ? -33.128 -17.635 3.830  1.00 51.86  ? 399 MET   B CB   1 
ATOM   1306 C CG   . MET   A 1 184 ? -34.550 -17.793 3.343  1.00 53.06  ? 399 MET   B CG   1 
ATOM   1307 S SD   . MET   A 1 184 ? -35.479 -19.023 4.285  1.00 49.75  ? 399 MET   B SD   1 
ATOM   1308 C CE   . MET   A 1 184 ? -37.151 -18.633 3.771  1.00 52.61  ? 399 MET   B CE   1 
ATOM   1309 N N    . ASN   A 1 185 ? -30.103 -17.914 3.165  1.00 44.38  ? 400 ASN   B N    1 
ATOM   1310 C CA   . ASN   A 1 185 ? -28.753 -18.015 3.695  1.00 48.45  ? 400 ASN   B CA   1 
ATOM   1311 C C    . ASN   A 1 185 ? -27.812 -16.978 3.078  1.00 47.66  ? 400 ASN   B C    1 
ATOM   1312 O O    . ASN   A 1 185 ? -27.008 -16.372 3.800  1.00 49.26  ? 400 ASN   B O    1 
ATOM   1313 C CB   . ASN   A 1 185 ? -28.247 -19.444 3.530  1.00 45.04  ? 400 ASN   B CB   1 
ATOM   1314 C CG   . ASN   A 1 185 ? -28.611 -20.304 4.730  1.00 47.55  ? 400 ASN   B CG   1 
ATOM   1315 O OD1  . ASN   A 1 185 ? -28.952 -19.765 5.788  1.00 48.66  ? 400 ASN   B OD1  1 
ATOM   1316 N ND2  . ASN   A 1 185 ? -28.559 -21.629 4.580  1.00 46.32  ? 400 ASN   B ND2  1 
ATOM   1317 N N    . SER   A 1 186 ? -27.913 -16.697 1.777  1.00 43.01  ? 401 SER   B N    1 
ATOM   1318 C CA   . SER   A 1 186 ? -26.972 -15.696 1.295  1.00 50.41  ? 401 SER   B CA   1 
ATOM   1319 C C    . SER   A 1 186 ? -27.425 -14.293 1.628  1.00 45.55  ? 401 SER   B C    1 
ATOM   1320 O O    . SER   A 1 186 ? -26.574 -13.411 1.785  1.00 44.74  ? 401 SER   B O    1 
ATOM   1321 C CB   . SER   A 1 186 ? -26.707 -15.796 -0.221 1.00 49.85  ? 401 SER   B CB   1 
ATOM   1322 O OG   . SER   A 1 186 ? -27.898 -15.806 -0.980 1.00 51.43  ? 401 SER   B OG   1 
ATOM   1323 N N    . VAL   A 1 187 ? -28.738 -14.044 1.720  1.00 44.45  ? 402 VAL   B N    1 
ATOM   1324 C CA   . VAL   A 1 187 ? -29.175 -12.783 2.323  1.00 48.17  ? 402 VAL   B CA   1 
ATOM   1325 C C    . VAL   A 1 187 ? -28.585 -12.658 3.721  1.00 48.32  ? 402 VAL   B C    1 
ATOM   1326 O O    . VAL   A 1 187 ? -27.836 -11.722 4.017  1.00 43.10  ? 402 VAL   B O    1 
ATOM   1327 C CB   . VAL   A 1 187 ? -30.707 -12.673 2.368  1.00 46.01  ? 402 VAL   B CB   1 
ATOM   1328 C CG1  . VAL   A 1 187 ? -31.083 -11.387 3.118  1.00 44.15  ? 402 VAL   B CG1  1 
ATOM   1329 C CG2  . VAL   A 1 187 ? -31.291 -12.654 0.986  1.00 46.78  ? 402 VAL   B CG2  1 
ATOM   1330 N N    . LEU   A 1 188 ? -28.890 -13.628 4.594  1.00 46.11  ? 403 LEU   B N    1 
ATOM   1331 C CA   . LEU   A 1 188 ? -28.377 -13.572 5.964  1.00 49.92  ? 403 LEU   B CA   1 
ATOM   1332 C C    . LEU   A 1 188 ? -26.857 -13.499 6.023  1.00 50.32  ? 403 LEU   B C    1 
ATOM   1333 O O    . LEU   A 1 188 ? -26.310 -13.130 7.065  1.00 49.82  ? 403 LEU   B O    1 
ATOM   1334 C CB   . LEU   A 1 188 ? -28.858 -14.775 6.766  1.00 45.02  ? 403 LEU   B CB   1 
ATOM   1335 C CG   . LEU   A 1 188 ? -30.373 -14.791 7.016  1.00 47.17  ? 403 LEU   B CG   1 
ATOM   1336 C CD1  . LEU   A 1 188 ? -30.790 -16.151 7.547  1.00 48.42  ? 403 LEU   B CD1  1 
ATOM   1337 C CD2  . LEU   A 1 188 ? -30.835 -13.661 7.966  1.00 46.38  ? 403 LEU   B CD2  1 
ATOM   1338 N N    . GLU   A 1 189 ? -26.163 -13.829 4.928  1.00 48.55  ? 404 GLU   B N    1 
ATOM   1339 C CA   . GLU   A 1 189 ? -24.702 -13.742 4.898  1.00 51.66  ? 404 GLU   B CA   1 
ATOM   1340 C C    . GLU   A 1 189 ? -24.224 -12.322 5.172  1.00 52.81  ? 404 GLU   B C    1 
ATOM   1341 O O    . GLU   A 1 189 ? -23.110 -12.110 5.680  1.00 52.71  ? 404 GLU   B O    1 
ATOM   1342 C CB   . GLU   A 1 189 ? -24.191 -14.218 3.533  1.00 51.12  ? 404 GLU   B CB   1 
ATOM   1343 C CG   . GLU   A 1 189 ? -22.763 -14.697 3.467  1.00 55.73  ? 404 GLU   B CG   1 
ATOM   1344 C CD   . GLU   A 1 189 ? -22.361 -14.993 2.017  1.00 65.92  ? 404 GLU   B CD   1 
ATOM   1345 O OE1  . GLU   A 1 189 ? -22.763 -16.061 1.474  1.00 70.44  ? 404 GLU   B OE1  1 
ATOM   1346 O OE2  . GLU   A 1 189 ? -21.671 -14.147 1.397  1.00 67.78  ? 404 GLU   B OE2  1 
ATOM   1347 N N    . ASN   A 1 190 ? -25.049 -11.336 4.841  1.00 51.09  ? 405 ASN   B N    1 
ATOM   1348 C CA   . ASN   A 1 190 ? -24.680 -9.943  4.994  1.00 52.63  ? 405 ASN   B CA   1 
ATOM   1349 C C    . ASN   A 1 190 ? -25.351 -9.294  6.191  1.00 52.07  ? 405 ASN   B C    1 
ATOM   1350 O O    . ASN   A 1 190 ? -25.301 -8.067  6.328  1.00 56.46  ? 405 ASN   B O    1 
ATOM   1351 C CB   . ASN   A 1 190 ? -25.020 -9.206  3.705  1.00 56.35  ? 405 ASN   B CB   1 
ATOM   1352 C CG   . ASN   A 1 190 ? -24.231 -9.728  2.532  1.00 56.85  ? 405 ASN   B CG   1 
ATOM   1353 O OD1  . ASN   A 1 190 ? -24.800 -10.080 1.501  1.00 59.79  ? 405 ASN   B OD1  1 
ATOM   1354 N ND2  . ASN   A 1 190 ? -22.900 -9.776  2.677  1.00 55.75  ? 405 ASN   B ND2  1 
ATOM   1355 N N    . PHE   A 1 191 ? -25.951 -10.081 7.079  1.00 50.80  ? 406 PHE   B N    1 
ATOM   1356 C CA   . PHE   A 1 191 ? -26.768 -9.542  8.166  1.00 51.93  ? 406 PHE   B CA   1 
ATOM   1357 C C    . PHE   A 1 191 ? -26.147 -9.969  9.485  1.00 50.67  ? 406 PHE   B C    1 
ATOM   1358 O O    . PHE   A 1 191 ? -26.270 -11.128 9.889  1.00 54.07  ? 406 PHE   B O    1 
ATOM   1359 C CB   . PHE   A 1 191 ? -28.209 -10.028 8.048  1.00 50.41  ? 406 PHE   B CB   1 
ATOM   1360 C CG   . PHE   A 1 191 ? -29.078 -9.622  9.191  1.00 50.73  ? 406 PHE   B CG   1 
ATOM   1361 C CD1  . PHE   A 1 191 ? -29.729 -8.397  9.181  1.00 53.16  ? 406 PHE   B CD1  1 
ATOM   1362 C CD2  . PHE   A 1 191 ? -29.249 -10.457 10.277 1.00 51.44  ? 406 PHE   B CD2  1 
ATOM   1363 C CE1  . PHE   A 1 191 ? -30.527 -8.010  10.241 1.00 51.16  ? 406 PHE   B CE1  1 
ATOM   1364 C CE2  . PHE   A 1 191 ? -30.058 -10.084 11.354 1.00 49.59  ? 406 PHE   B CE2  1 
ATOM   1365 C CZ   . PHE   A 1 191 ? -30.696 -8.861  11.329 1.00 53.71  ? 406 PHE   B CZ   1 
ATOM   1366 N N    . THR   A 1 192 ? -25.499 -9.048  10.174 1.00 53.28  ? 407 THR   B N    1 
ATOM   1367 C CA   . THR   A 1 192 ? -24.942 -9.365  11.473 1.00 55.39  ? 407 THR   B CA   1 
ATOM   1368 C C    . THR   A 1 192 ? -25.488 -8.417  12.531 1.00 56.38  ? 407 THR   B C    1 
ATOM   1369 O O    . THR   A 1 192 ? -26.033 -7.351  12.229 1.00 53.23  ? 407 THR   B O    1 
ATOM   1370 C CB   . THR   A 1 192 ? -23.425 -9.280  11.458 1.00 57.35  ? 407 THR   B CB   1 
ATOM   1371 O OG1  . THR   A 1 192 ? -23.050 -7.906  11.307 1.00 61.53  ? 407 THR   B OG1  1 
ATOM   1372 C CG2  . THR   A 1 192 ? -22.881 -10.096 10.302 1.00 58.34  ? 407 THR   B CG2  1 
ATOM   1373 N N    . ILE   A 1 193 ? -25.317 -8.814  13.789 1.00 55.49  ? 408 ILE   B N    1 
ATOM   1374 C CA   . ILE   A 1 193 ? -25.735 -8.004  14.922 1.00 51.47  ? 408 ILE   B CA   1 
ATOM   1375 C C    . ILE   A 1 193 ? -24.589 -7.957  15.925 1.00 50.49  ? 408 ILE   B C    1 
ATOM   1376 O O    . ILE   A 1 193 ? -23.896 -8.959  16.138 1.00 49.90  ? 408 ILE   B O    1 
ATOM   1377 C CB   . ILE   A 1 193 ? -27.001 -8.586  15.568 1.00 52.84  ? 408 ILE   B CB   1 
ATOM   1378 C CG1  . ILE   A 1 193 ? -28.240 -8.146  14.801 1.00 51.27  ? 408 ILE   B CG1  1 
ATOM   1379 C CG2  . ILE   A 1 193 ? -27.094 -8.161  17.005 1.00 53.86  ? 408 ILE   B CG2  1 
ATOM   1380 C CD1  . ILE   A 1 193 ? -29.367 -9.129  14.910 1.00 51.56  ? 408 ILE   B CD1  1 
ATOM   1381 N N    . LEU   A 1 194 ? -24.376 -6.801  16.538 1.00 51.09  ? 409 LEU   B N    1 
ATOM   1382 C CA   . LEU   A 1 194 ? -23.323 -6.655  17.535 1.00 52.78  ? 409 LEU   B CA   1 
ATOM   1383 C C    . LEU   A 1 194 ? -23.932 -6.127  18.824 1.00 54.27  ? 409 LEU   B C    1 
ATOM   1384 O O    . LEU   A 1 194 ? -24.504 -5.033  18.836 1.00 57.12  ? 409 LEU   B O    1 
ATOM   1385 C CB   . LEU   A 1 194 ? -22.224 -5.722  17.045 1.00 52.71  ? 409 LEU   B CB   1 
ATOM   1386 C CG   . LEU   A 1 194 ? -20.965 -5.650  17.907 1.00 53.79  ? 409 LEU   B CG   1 
ATOM   1387 C CD1  . LEU   A 1 194 ? -20.112 -6.893  17.740 1.00 50.61  ? 409 LEU   B CD1  1 
ATOM   1388 C CD2  . LEU   A 1 194 ? -20.171 -4.391  17.584 1.00 58.71  ? 409 LEU   B CD2  1 
ATOM   1389 N N    . GLN   A 1 195 ? -23.824 -6.899  19.900 1.00 51.57  ? 410 GLN   B N    1 
ATOM   1390 C CA   . GLN   A 1 195 ? -24.279 -6.463  21.218 1.00 51.13  ? 410 GLN   B CA   1 
ATOM   1391 C C    . GLN   A 1 195 ? -23.075 -6.071  22.055 1.00 52.46  ? 410 GLN   B C    1 
ATOM   1392 O O    . GLN   A 1 195 ? -22.102 -6.823  22.135 1.00 54.87  ? 410 GLN   B O    1 
ATOM   1393 C CB   . GLN   A 1 195 ? -25.070 -7.560  21.925 1.00 49.06  ? 410 GLN   B CB   1 
ATOM   1394 C CG   . GLN   A 1 195 ? -26.471 -7.666  21.388 1.00 53.24  ? 410 GLN   B CG   1 
ATOM   1395 C CD   . GLN   A 1 195 ? -27.406 -8.410  22.302 1.00 53.93  ? 410 GLN   B CD   1 
ATOM   1396 O OE1  . GLN   A 1 195 ? -27.165 -9.567  22.660 1.00 52.76  ? 410 GLN   B OE1  1 
ATOM   1397 N NE2  . GLN   A 1 195 ? -28.511 -7.770  22.648 1.00 53.09  ? 410 GLN   B NE2  1 
ATOM   1398 N N    . VAL   A 1 196 ? -23.134 -4.895  22.670 1.00 54.19  ? 411 VAL   B N    1 
ATOM   1399 C CA   . VAL   A 1 196 ? -22.052 -4.402  23.520 1.00 54.22  ? 411 VAL   B CA   1 
ATOM   1400 C C    . VAL   A 1 196 ? -22.640 -4.060  24.887 1.00 53.77  ? 411 VAL   B C    1 
ATOM   1401 O O    . VAL   A 1 196 ? -23.476 -3.157  24.999 1.00 53.39  ? 411 VAL   B O    1 
ATOM   1402 C CB   . VAL   A 1 196 ? -21.342 -3.195  22.892 1.00 53.19  ? 411 VAL   B CB   1 
ATOM   1403 C CG1  . VAL   A 1 196 ? -20.192 -2.719  23.768 1.00 54.06  ? 411 VAL   B CG1  1 
ATOM   1404 C CG2  . VAL   A 1 196 ? -20.821 -3.579  21.520 1.00 50.90  ? 411 VAL   B CG2  1 
ATOM   1405 N N    . VAL   A 1 197 ? -22.238 -4.803  25.915 1.00 58.66  ? 412 VAL   B N    1 
ATOM   1406 C CA   . VAL   A 1 197 ? -22.698 -4.580  27.283 1.00 55.60  ? 412 VAL   B CA   1 
ATOM   1407 C C    . VAL   A 1 197 ? -21.582 -3.887  28.043 1.00 58.79  ? 412 VAL   B C    1 
ATOM   1408 O O    . VAL   A 1 197 ? -20.487 -4.439  28.205 1.00 57.42  ? 412 VAL   B O    1 
ATOM   1409 C CB   . VAL   A 1 197 ? -23.096 -5.888  27.983 1.00 53.55  ? 412 VAL   B CB   1 
ATOM   1410 C CG1  . VAL   A 1 197 ? -23.687 -5.584  29.373 1.00 55.25  ? 412 VAL   B CG1  1 
ATOM   1411 C CG2  . VAL   A 1 197 ? -24.081 -6.661  27.146 1.00 53.99  ? 412 VAL   B CG2  1 
ATOM   1412 N N    . THR   A 1 198 ? -21.865 -2.690  28.538 1.00 58.51  ? 413 THR   B N    1 
ATOM   1413 C CA   . THR   A 1 198 ? -20.859 -1.891  29.212 1.00 60.84  ? 413 THR   B CA   1 
ATOM   1414 C C    . THR   A 1 198 ? -21.370 -1.480  30.582 1.00 62.07  ? 413 THR   B C    1 
ATOM   1415 O O    . THR   A 1 198 ? -22.572 -1.298  30.784 1.00 61.40  ? 413 THR   B O    1 
ATOM   1416 C CB   . THR   A 1 198 ? -20.511 -0.657  28.395 1.00 61.43  ? 413 THR   B CB   1 
ATOM   1417 O OG1  . THR   A 1 198 ? -21.398 0.399   28.766 1.00 64.94  ? 413 THR   B OG1  1 
ATOM   1418 C CG2  . THR   A 1 198 ? -20.701 -0.931  26.920 1.00 57.35  ? 413 THR   B CG2  1 
ATOM   1419 N N    . ASN   A 1 199 ? -20.441 -1.341  31.522 1.00 69.25  ? 414 ASN   B N    1 
ATOM   1420 C CA   . ASN   A 1 199 ? -20.742 -0.817  32.852 1.00 70.10  ? 414 ASN   B CA   1 
ATOM   1421 C C    . ASN   A 1 199 ? -21.029 0.675   32.733 1.00 72.36  ? 414 ASN   B C    1 
ATOM   1422 O O    . ASN   A 1 199 ? -20.125 1.451   32.407 1.00 75.75  ? 414 ASN   B O    1 
ATOM   1423 C CB   . ASN   A 1 199 ? -19.557 -1.090  33.771 1.00 73.28  ? 414 ASN   B CB   1 
ATOM   1424 C CG   . ASN   A 1 199 ? -19.827 -0.725  35.207 1.00 74.34  ? 414 ASN   B CG   1 
ATOM   1425 O OD1  . ASN   A 1 199 ? -20.493 0.272   35.500 1.00 75.25  ? 414 ASN   B OD1  1 
ATOM   1426 N ND2  . ASN   A 1 199 ? -19.296 -1.528  36.124 1.00 73.47  ? 414 ASN   B ND2  1 
ATOM   1427 N N    . ARG   A 1 200 ? -22.283 1.088   32.980 1.00 67.90  ? 415 ARG   B N    1 
ATOM   1428 C CA   . ARG   A 1 200 ? -22.661 2.475   32.697 1.00 71.66  ? 415 ARG   B CA   1 
ATOM   1429 C C    . ARG   A 1 200 ? -21.911 3.461   33.575 1.00 74.62  ? 415 ARG   B C    1 
ATOM   1430 O O    . ARG   A 1 200 ? -21.667 4.599   33.161 1.00 76.76  ? 415 ARG   B O    1 
ATOM   1431 C CB   . ARG   A 1 200 ? -24.168 2.700   32.865 1.00 67.13  ? 415 ARG   B CB   1 
ATOM   1432 C CG   . ARG   A 1 200 ? -24.615 4.166   32.632 1.00 64.40  ? 415 ARG   B CG   1 
ATOM   1433 C CD   . ARG   A 1 200 ? -25.241 4.728   33.903 1.00 76.70  ? 415 ARG   B CD   1 
ATOM   1434 N NE   . ARG   A 1 200 ? -26.076 5.916   33.734 1.00 79.94  ? 415 ARG   B NE   1 
ATOM   1435 C CZ   . ARG   A 1 200 ? -27.106 6.209   34.520 1.00 80.71  ? 415 ARG   B CZ   1 
ATOM   1436 N NH1  . ARG   A 1 200 ? -27.499 5.380   35.473 1.00 77.04  ? 415 ARG   B NH1  1 
ATOM   1437 N NH2  . ARG   A 1 200 ? -27.753 7.365   34.352 1.00 84.83  ? 415 ARG   B NH2  1 
ATOM   1438 N N    . ASP   A 1 201 ? -21.547 3.065   34.788 1.00 73.44  ? 416 ASP   B N    1 
ATOM   1439 C CA   . ASP   A 1 201 ? -20.830 4.017   35.623 1.00 80.54  ? 416 ASP   B CA   1 
ATOM   1440 C C    . ASP   A 1 201 ? -19.352 4.065   35.254 1.00 82.73  ? 416 ASP   B C    1 
ATOM   1441 O O    . ASP   A 1 201 ? -18.748 5.144   35.220 1.00 86.68  ? 416 ASP   B O    1 
ATOM   1442 C CB   . ASP   A 1 201 ? -21.031 3.682   37.108 1.00 80.84  ? 416 ASP   B CB   1 
ATOM   1443 C CG   . ASP   A 1 201 ? -22.510 3.648   37.510 1.00 78.90  ? 416 ASP   B CG   1 
ATOM   1444 O OD1  . ASP   A 1 201 ? -23.269 4.539   37.065 1.00 77.00  ? 416 ASP   B OD1  1 
ATOM   1445 O OD2  . ASP   A 1 201 ? -22.916 2.746   38.282 1.00 79.32  ? 416 ASP   B OD2  1 
ATOM   1446 N N    . THR   A 1 202 ? -18.768 2.914   34.937 1.00 82.84  ? 417 THR   B N    1 
ATOM   1447 C CA   . THR   A 1 202 ? -17.333 2.809   34.707 1.00 83.91  ? 417 THR   B CA   1 
ATOM   1448 C C    . THR   A 1 202 ? -16.930 2.987   33.250 1.00 86.11  ? 417 THR   B C    1 
ATOM   1449 O O    . THR   A 1 202 ? -15.835 3.491   32.979 1.00 89.01  ? 417 THR   B O    1 
ATOM   1450 C CB   . THR   A 1 202 ? -16.825 1.452   35.203 1.00 82.79  ? 417 THR   B CB   1 
ATOM   1451 O OG1  . THR   A 1 202 ? -16.617 1.508   36.622 1.00 86.72  ? 417 THR   B OG1  1 
ATOM   1452 C CG2  . THR   A 1 202 ? -15.544 1.100   34.522 1.00 87.27  ? 417 THR   B CG2  1 
ATOM   1453 N N    . GLN   A 1 203 ? -17.772 2.586   32.306 1.00 87.34  ? 418 GLN   B N    1 
ATOM   1454 C CA   . GLN   A 1 203 ? -17.478 2.542   30.883 1.00 85.61  ? 418 GLN   B CA   1 
ATOM   1455 C C    . GLN   A 1 203 ? -16.707 1.277   30.537 1.00 85.57  ? 418 GLN   B C    1 
ATOM   1456 O O    . GLN   A 1 203 ? -16.471 1.027   29.361 1.00 86.44  ? 418 GLN   B O    1 
ATOM   1457 C CB   . GLN   A 1 203 ? -16.682 3.764   30.382 1.00 90.25  ? 418 GLN   B CB   1 
ATOM   1458 C CG   . GLN   A 1 203 ? -17.260 5.112   30.788 1.00 92.32  ? 418 GLN   B CG   1 
ATOM   1459 C CD   . GLN   A 1 203 ? -18.702 5.287   30.359 1.00 93.29  ? 418 GLN   B CD   1 
ATOM   1460 O OE1  . GLN   A 1 203 ? -19.563 4.465   30.677 1.00 91.95  ? 418 GLN   B OE1  1 
ATOM   1461 N NE2  . GLN   A 1 203 ? -18.977 6.376   29.645 1.00 95.33  ? 418 GLN   B NE2  1 
ATOM   1462 N N    . GLU   A 1 204 ? -16.287 0.478   31.518 1.00 80.76  ? 419 GLU   B N    1 
ATOM   1463 C CA   . GLU   A 1 204 ? -15.657 -0.800  31.218 1.00 77.64  ? 419 GLU   B CA   1 
ATOM   1464 C C    . GLU   A 1 204 ? -16.603 -1.652  30.378 1.00 72.54  ? 419 GLU   B C    1 
ATOM   1465 O O    . GLU   A 1 204 ? -17.755 -1.885  30.758 1.00 70.10  ? 419 GLU   B O    1 
ATOM   1466 C CB   . GLU   A 1 204 ? -15.283 -1.545  32.508 1.00 78.62  ? 419 GLU   B CB   1 
ATOM   1467 C CG   . GLU   A 1 204 ? -13.887 -1.234  33.078 1.00 82.86  ? 419 GLU   B CG   1 
ATOM   1468 C CD   . GLU   A 1 204 ? -13.777 -1.467  34.603 1.00 88.42  ? 419 GLU   B CD   1 
ATOM   1469 O OE1  . GLU   A 1 204 ? -14.826 -1.530  35.310 1.00 85.65  ? 419 GLU   B OE1  1 
ATOM   1470 O OE2  . GLU   A 1 204 ? -12.627 -1.549  35.105 1.00 86.99  ? 419 GLU   B OE2  1 
ATOM   1471 N N    . LEU   A 1 205 ? -16.124 -2.096  29.220 1.00 73.61  ? 420 LEU   B N    1 
ATOM   1472 C CA   . LEU   A 1 205 ? -16.855 -3.107  28.475 1.00 67.29  ? 420 LEU   B CA   1 
ATOM   1473 C C    . LEU   A 1 205 ? -16.886 -4.399  29.285 1.00 64.03  ? 420 LEU   B C    1 
ATOM   1474 O O    . LEU   A 1 205 ? -15.856 -4.854  29.797 1.00 64.83  ? 420 LEU   B O    1 
ATOM   1475 C CB   . LEU   A 1 205 ? -16.204 -3.326  27.105 1.00 66.37  ? 420 LEU   B CB   1 
ATOM   1476 C CG   . LEU   A 1 205 ? -16.955 -4.172  26.073 1.00 60.91  ? 420 LEU   B CG   1 
ATOM   1477 C CD1  . LEU   A 1 205 ? -16.864 -3.556  24.678 1.00 61.98  ? 420 LEU   B CD1  1 
ATOM   1478 C CD2  . LEU   A 1 205 ? -16.374 -5.568  26.079 1.00 61.56  ? 420 LEU   B CD2  1 
ATOM   1479 N N    . LEU   A 1 206 ? -18.079 -4.974  29.432 1.00 63.06  ? 421 LEU   B N    1 
ATOM   1480 C CA   . LEU   A 1 206 ? -18.237 -6.223  30.165 1.00 61.41  ? 421 LEU   B CA   1 
ATOM   1481 C C    . LEU   A 1 206 ? -18.459 -7.431  29.266 1.00 61.99  ? 421 LEU   B C    1 
ATOM   1482 O O    . LEU   A 1 206 ? -18.037 -8.539  29.616 1.00 62.24  ? 421 LEU   B O    1 
ATOM   1483 C CB   . LEU   A 1 206 ? -19.404 -6.113  31.154 1.00 60.22  ? 421 LEU   B CB   1 
ATOM   1484 C CG   . LEU   A 1 206 ? -19.350 -5.056  32.273 1.00 60.89  ? 421 LEU   B CG   1 
ATOM   1485 C CD1  . LEU   A 1 206 ? -20.713 -4.953  32.933 1.00 58.90  ? 421 LEU   B CD1  1 
ATOM   1486 C CD2  . LEU   A 1 206 ? -18.280 -5.357  33.315 1.00 61.84  ? 421 LEU   B CD2  1 
ATOM   1487 N N    . LEU   A 1 207 ? -19.090 -7.242  28.110 1.00 57.82  ? 422 LEU   B N    1 
ATOM   1488 C CA   . LEU   A 1 207 ? -19.382 -8.343  27.208 1.00 55.28  ? 422 LEU   B CA   1 
ATOM   1489 C C    . LEU   A 1 207 ? -19.616 -7.768  25.824 1.00 56.82  ? 422 LEU   B C    1 
ATOM   1490 O O    . LEU   A 1 207 ? -20.331 -6.773  25.680 1.00 56.87  ? 422 LEU   B O    1 
ATOM   1491 C CB   . LEU   A 1 207 ? -20.610 -9.126  27.677 1.00 55.75  ? 422 LEU   B CB   1 
ATOM   1492 C CG   . LEU   A 1 207 ? -20.644 -10.620 27.345 1.00 55.50  ? 422 LEU   B CG   1 
ATOM   1493 C CD1  . LEU   A 1 207 ? -19.429 -11.378 27.907 1.00 56.28  ? 422 LEU   B CD1  1 
ATOM   1494 C CD2  . LEU   A 1 207 ? -21.915 -11.187 27.899 1.00 57.02  ? 422 LEU   B CD2  1 
ATOM   1495 N N    . CYS   A 1 208 ? -19.001 -8.381  24.814 1.00 56.24  ? 423 CYS   B N    1 
ATOM   1496 C CA   . CYS   A 1 208 ? -19.232 -8.032  23.415 1.00 53.41  ? 423 CYS   B CA   1 
ATOM   1497 C C    . CYS   A 1 208 ? -19.555 -9.304  22.650 1.00 50.52  ? 423 CYS   B C    1 
ATOM   1498 O O    . CYS   A 1 208 ? -18.785 -10.263 22.699 1.00 51.71  ? 423 CYS   B O    1 
ATOM   1499 C CB   . CYS   A 1 208 ? -18.021 -7.341  22.801 1.00 56.73  ? 423 CYS   B CB   1 
ATOM   1500 S SG   . CYS   A 1 208 ? -18.316 -6.873  21.079 1.00 53.76  ? 423 CYS   B SG   1 
ATOM   1501 N N    . THR   A 1 209 ? -20.681 -9.308  21.942 1.00 48.57  ? 424 THR   B N    1 
ATOM   1502 C CA   . THR   A 1 209 ? -21.196 -10.506 21.286 1.00 51.66  ? 424 THR   B CA   1 
ATOM   1503 C C    . THR   A 1 209 ? -21.560 -10.157 19.846 1.00 50.22  ? 424 THR   B C    1 
ATOM   1504 O O    . THR   A 1 209 ? -22.465 -9.348  19.610 1.00 48.78  ? 424 THR   B O    1 
ATOM   1505 C CB   . THR   A 1 209 ? -22.407 -11.066 22.047 1.00 51.51  ? 424 THR   B CB   1 
ATOM   1506 O OG1  . THR   A 1 209 ? -21.992 -11.487 23.345 1.00 49.97  ? 424 THR   B OG1  1 
ATOM   1507 C CG2  . THR   A 1 209 ? -22.989 -12.261 21.331 1.00 52.84  ? 424 THR   B CG2  1 
ATOM   1508 N N    . ALA   A 1 210 ? -20.840 -10.739 18.894 1.00 47.52  ? 425 ALA   B N    1 
ATOM   1509 C CA   . ALA   A 1 210 ? -21.201 -10.648 17.486 1.00 51.56  ? 425 ALA   B CA   1 
ATOM   1510 C C    . ALA   A 1 210 ? -22.055 -11.847 17.107 1.00 51.66  ? 425 ALA   B C    1 
ATOM   1511 O O    . ALA   A 1 210 ? -21.767 -12.984 17.506 1.00 47.98  ? 425 ALA   B O    1 
ATOM   1512 C CB   . ALA   A 1 210 ? -19.959 -10.598 16.588 1.00 51.34  ? 425 ALA   B CB   1 
ATOM   1513 N N    . TYR   A 1 211 ? -23.091 -11.588 16.315 1.00 49.91  ? 426 TYR   B N    1 
ATOM   1514 C CA   . TYR   A 1 211 ? -24.036 -12.608 15.869 1.00 47.68  ? 426 TYR   B CA   1 
ATOM   1515 C C    . TYR   A 1 211 ? -23.999 -12.714 14.344 1.00 48.12  ? 426 TYR   B C    1 
ATOM   1516 O O    . TYR   A 1 211 ? -24.212 -11.716 13.647 1.00 47.65  ? 426 TYR   B O    1 
ATOM   1517 C CB   . TYR   A 1 211 ? -25.447 -12.257 16.337 1.00 44.58  ? 426 TYR   B CB   1 
ATOM   1518 C CG   . TYR   A 1 211 ? -25.632 -12.205 17.836 1.00 49.16  ? 426 TYR   B CG   1 
ATOM   1519 C CD1  . TYR   A 1 211 ? -25.914 -13.363 18.565 1.00 49.56  ? 426 TYR   B CD1  1 
ATOM   1520 C CD2  . TYR   A 1 211 ? -25.549 -11.009 18.526 1.00 49.53  ? 426 TYR   B CD2  1 
ATOM   1521 C CE1  . TYR   A 1 211 ? -26.107 -13.330 19.945 1.00 49.99  ? 426 TYR   B CE1  1 
ATOM   1522 C CE2  . TYR   A 1 211 ? -25.747 -10.957 19.906 1.00 50.28  ? 426 TYR   B CE2  1 
ATOM   1523 C CZ   . TYR   A 1 211 ? -26.027 -12.120 20.612 1.00 52.78  ? 426 TYR   B CZ   1 
ATOM   1524 O OH   . TYR   A 1 211 ? -26.224 -12.076 21.986 1.00 51.97  ? 426 TYR   B OH   1 
ATOM   1525 N N    . VAL   A 1 212 ? -23.757 -13.922 13.828 1.00 49.58  ? 427 VAL   B N    1 
ATOM   1526 C CA   . VAL   A 1 212 ? -23.928 -14.216 12.404 1.00 50.17  ? 427 VAL   B CA   1 
ATOM   1527 C C    . VAL   A 1 212 ? -25.051 -15.237 12.274 1.00 47.65  ? 427 VAL   B C    1 
ATOM   1528 O O    . VAL   A 1 212 ? -25.404 -15.910 13.239 1.00 51.02  ? 427 VAL   B O    1 
ATOM   1529 C CB   . VAL   A 1 212 ? -22.628 -14.719 11.725 1.00 45.38  ? 427 VAL   B CB   1 
ATOM   1530 C CG1  . VAL   A 1 212 ? -21.527 -13.700 11.876 1.00 47.18  ? 427 VAL   B CG1  1 
ATOM   1531 C CG2  . VAL   A 1 212 ? -22.168 -16.053 12.298 1.00 46.62  ? 427 VAL   B CG2  1 
ATOM   1532 N N    . PHE   A 1 213 ? -25.605 -15.369 11.066 1.00 50.23  ? 428 PHE   B N    1 
ATOM   1533 C CA   . PHE   A 1 213 ? -26.892 -16.041 10.908 1.00 46.97  ? 428 PHE   B CA   1 
ATOM   1534 C C    . PHE   A 1 213 ? -26.944 -16.983 9.704  1.00 50.40  ? 428 PHE   B C    1 
ATOM   1535 O O    . PHE   A 1 213 ? -26.292 -16.772 8.675  1.00 51.77  ? 428 PHE   B O    1 
ATOM   1536 C CB   . PHE   A 1 213 ? -28.010 -15.016 10.796 1.00 46.88  ? 428 PHE   B CB   1 
ATOM   1537 C CG   . PHE   A 1 213 ? -28.230 -14.221 12.067 1.00 50.09  ? 428 PHE   B CG   1 
ATOM   1538 C CD1  . PHE   A 1 213 ? -27.528 -13.049 12.301 1.00 49.08  ? 428 PHE   B CD1  1 
ATOM   1539 C CD2  . PHE   A 1 213 ? -29.145 -14.644 13.023 1.00 46.10  ? 428 PHE   B CD2  1 
ATOM   1540 C CE1  . PHE   A 1 213 ? -27.754 -12.311 13.487 1.00 50.91  ? 428 PHE   B CE1  1 
ATOM   1541 C CE2  . PHE   A 1 213 ? -29.345 -13.928 14.179 1.00 47.20  ? 428 PHE   B CE2  1 
ATOM   1542 C CZ   . PHE   A 1 213 ? -28.654 -12.764 14.415 1.00 45.83  ? 428 PHE   B CZ   1 
ATOM   1543 N N    . GLU   A 1 214 ? -27.726 -18.047 9.882  1.00 48.12  ? 429 GLU   B N    1 
ATOM   1544 C CA   . GLU   A 1 214 ? -28.233 -18.927 8.843  1.00 47.39  ? 429 GLU   B CA   1 
ATOM   1545 C C    . GLU   A 1 214 ? -29.645 -19.336 9.244  1.00 50.78  ? 429 GLU   B C    1 
ATOM   1546 O O    . GLU   A 1 214 ? -30.116 -19.011 10.338 1.00 49.18  ? 429 GLU   B O    1 
ATOM   1547 C CB   . GLU   A 1 214 ? -27.371 -20.172 8.683  1.00 49.61  ? 429 GLU   B CB   1 
ATOM   1548 C CG   . GLU   A 1 214 ? -26.033 -19.928 8.063  1.00 52.14  ? 429 GLU   B CG   1 
ATOM   1549 C CD   . GLU   A 1 214 ? -25.255 -21.210 7.937  1.00 56.01  ? 429 GLU   B CD   1 
ATOM   1550 O OE1  . GLU   A 1 214 ? -25.848 -22.247 7.546  1.00 53.64  ? 429 GLU   B OE1  1 
ATOM   1551 O OE2  . GLU   A 1 214 ? -24.050 -21.197 8.266  1.00 64.08  ? 429 GLU   B OE2  1 
ATOM   1552 N N    . VAL   A 1 215 ? -30.326 -20.077 8.374  1.00 50.46  ? 430 VAL   B N    1 
ATOM   1553 C CA   . VAL   A 1 215 ? -31.644 -20.594 8.720  1.00 52.11  ? 430 VAL   B CA   1 
ATOM   1554 C C    . VAL   A 1 215 ? -31.512 -22.073 9.035  1.00 54.97  ? 430 VAL   B C    1 
ATOM   1555 O O    . VAL   A 1 215 ? -30.521 -22.728 8.712  1.00 58.31  ? 430 VAL   B O    1 
ATOM   1556 C CB   . VAL   A 1 215 ? -32.685 -20.372 7.610  1.00 51.66  ? 430 VAL   B CB   1 
ATOM   1557 C CG1  . VAL   A 1 215 ? -32.994 -18.888 7.495  1.00 56.02  ? 430 VAL   B CG1  1 
ATOM   1558 C CG2  . VAL   A 1 215 ? -32.189 -20.941 6.304  1.00 56.19  ? 430 VAL   B CG2  1 
ATOM   1559 N N    . SER   A 1 216 ? -32.534 -22.620 9.658  1.00 66.03  ? 431 SER   B N    1 
ATOM   1560 C CA   . SER   A 1 216 ? -32.534 -24.023 10.016 1.00 73.64  ? 431 SER   B CA   1 
ATOM   1561 C C    . SER   A 1 216 ? -33.699 -24.715 9.318  1.00 81.95  ? 431 SER   B C    1 
ATOM   1562 O O    . SER   A 1 216 ? -34.781 -24.141 9.174  1.00 83.19  ? 431 SER   B O    1 
ATOM   1563 C CB   . SER   A 1 216 ? -32.605 -24.175 11.542 1.00 66.91  ? 431 SER   B CB   1 
ATOM   1564 O OG   . SER   A 1 216 ? -33.001 -25.468 11.915 1.00 73.18  ? 431 SER   B OG   1 
ATOM   1565 N N    . THR   A 1 217 ? -33.454 -25.936 8.853  1.00 89.08  ? 432 THR   B N    1 
ATOM   1566 C CA   . THR   A 1 217 ? -34.479 -26.792 8.249  1.00 95.73  ? 432 THR   B CA   1 
ATOM   1567 C C    . THR   A 1 217 ? -35.464 -27.202 9.340  1.00 97.51  ? 432 THR   B C    1 
ATOM   1568 O O    . THR   A 1 217 ? -35.219 -28.146 10.097 1.00 97.44  ? 432 THR   B O    1 
ATOM   1569 C CB   . THR   A 1 217 ? -33.822 -28.005 7.602  1.00 98.69  ? 432 THR   B CB   1 
ATOM   1570 O OG1  . THR   A 1 217 ? -33.696 -29.058 8.570  1.00 98.57  ? 432 THR   B OG1  1 
ATOM   1571 C CG2  . THR   A 1 217 ? -32.432 -27.634 7.098  1.00 94.48  ? 432 THR   B CG2  1 
ATOM   1572 N N    . SER   A 1 218 ? -36.606 -26.514 9.395  1.00 105.48 ? 433 SER   B N    1 
ATOM   1573 C CA   . SER   A 1 218 ? -37.344 -26.349 10.645 1.00 104.77 ? 433 SER   B CA   1 
ATOM   1574 C C    . SER   A 1 218 ? -37.995 -27.603 11.224 1.00 108.97 ? 433 SER   B C    1 
ATOM   1575 O O    . SER   A 1 218 ? -38.851 -27.488 12.109 1.00 111.39 ? 433 SER   B O    1 
ATOM   1576 C CB   . SER   A 1 218 ? -38.404 -25.260 10.477 1.00 106.71 ? 433 SER   B CB   1 
ATOM   1577 O OG   . SER   A 1 218 ? -37.781 -23.999 10.290 1.00 103.96 ? 433 SER   B OG   1 
ATOM   1578 N N    . GLU   A 1 219 ? -37.603 -28.800 10.777 1.00 96.42  ? 434 GLU   B N    1 
ATOM   1579 C CA   . GLU   A 1 219 ? -37.718 -29.939 11.683 1.00 85.98  ? 434 GLU   B CA   1 
ATOM   1580 C C    . GLU   A 1 219 ? -36.757 -29.750 12.845 1.00 81.26  ? 434 GLU   B C    1 
ATOM   1581 O O    . GLU   A 1 219 ? -37.133 -29.899 14.017 1.00 79.40  ? 434 GLU   B O    1 
ATOM   1582 C CB   . GLU   A 1 219 ? -37.428 -31.259 10.969 1.00 87.95  ? 434 GLU   B CB   1 
ATOM   1583 C CG   . GLU   A 1 219 ? -37.954 -31.369 9.546  1.00 95.03  ? 434 GLU   B CG   1 
ATOM   1584 C CD   . GLU   A 1 219 ? -37.346 -32.549 8.799  1.00 92.03  ? 434 GLU   B CD   1 
ATOM   1585 O OE1  . GLU   A 1 219 ? -36.298 -32.359 8.138  1.00 93.97  ? 434 GLU   B OE1  1 
ATOM   1586 O OE2  . GLU   A 1 219 ? -37.906 -33.663 8.891  1.00 89.86  ? 434 GLU   B OE2  1 
ATOM   1587 N N    . ARG   A 1 220 ? -35.505 -29.420 12.533 1.00 84.12  ? 435 ARG   B N    1 
ATOM   1588 C CA   . ARG   A 1 220 ? -34.621 -28.848 13.531 1.00 78.34  ? 435 ARG   B CA   1 
ATOM   1589 C C    . ARG   A 1 220 ? -35.122 -27.456 13.864 1.00 78.41  ? 435 ARG   B C    1 
ATOM   1590 O O    . ARG   A 1 220 ? -35.455 -26.671 12.971 1.00 83.61  ? 435 ARG   B O    1 
ATOM   1591 C CB   . ARG   A 1 220 ? -33.186 -28.773 13.018 1.00 72.37  ? 435 ARG   B CB   1 
ATOM   1592 C CG   . ARG   A 1 220 ? -32.785 -29.887 12.094 1.00 73.14  ? 435 ARG   B CG   1 
ATOM   1593 C CD   . ARG   A 1 220 ? -31.302 -29.812 11.787 1.00 69.59  ? 435 ARG   B CD   1 
ATOM   1594 N NE   . ARG   A 1 220 ? -30.475 -29.896 12.986 1.00 70.71  ? 435 ARG   B NE   1 
ATOM   1595 C CZ   . ARG   A 1 220 ? -29.164 -30.098 12.966 1.00 70.02  ? 435 ARG   B CZ   1 
ATOM   1596 N NH1  . ARG   A 1 220 ? -28.506 -30.217 11.823 1.00 70.04  ? 435 ARG   B NH1  1 
ATOM   1597 N NH2  . ARG   A 1 220 ? -28.500 -30.188 14.117 1.00 67.06  ? 435 ARG   B NH2  1 
ATOM   1598 N N    . GLY   A 1 221 ? -35.205 -27.142 15.138 1.00 66.38  ? 436 GLY   B N    1 
ATOM   1599 C CA   . GLY   A 1 221 ? -35.539 -25.792 15.512 1.00 63.50  ? 436 GLY   B CA   1 
ATOM   1600 C C    . GLY   A 1 221 ? -34.304 -24.924 15.510 1.00 56.90  ? 436 GLY   B C    1 
ATOM   1601 O O    . GLY   A 1 221 ? -33.257 -25.271 14.967 1.00 60.16  ? 436 GLY   B O    1 
ATOM   1602 N N    . ALA   A 1 222 ? -34.425 -23.781 16.165 1.00 59.15  ? 437 ALA   B N    1 
ATOM   1603 C CA   . ALA   A 1 222 ? -33.278 -22.915 16.349 1.00 53.46  ? 437 ALA   B CA   1 
ATOM   1604 C C    . ALA   A 1 222 ? -32.142 -23.688 16.983 1.00 49.44  ? 437 ALA   B C    1 
ATOM   1605 O O    . ALA   A 1 222 ? -32.352 -24.540 17.837 1.00 56.71  ? 437 ALA   B O    1 
ATOM   1606 C CB   . ALA   A 1 222 ? -33.658 -21.730 17.227 1.00 53.17  ? 437 ALA   B CB   1 
ATOM   1607 N N    . GLN   A 1 223 ? -30.931 -23.406 16.546 1.00 51.31  ? 438 GLN   B N    1 
ATOM   1608 C CA   . GLN   A 1 223 ? -29.749 -23.959 17.179 1.00 50.07  ? 438 GLN   B CA   1 
ATOM   1609 C C    . GLN   A 1 223 ? -28.712 -22.849 17.192 1.00 49.33  ? 438 GLN   B C    1 
ATOM   1610 O O    . GLN   A 1 223 ? -28.878 -21.822 16.524 1.00 46.23  ? 438 GLN   B O    1 
ATOM   1611 C CB   . GLN   A 1 223 ? -29.244 -25.199 16.431 1.00 56.62  ? 438 GLN   B CB   1 
ATOM   1612 C CG   . GLN   A 1 223 ? -28.572 -26.243 17.305 1.00 62.22  ? 438 GLN   B CG   1 
ATOM   1613 C CD   . GLN   A 1 223 ? -28.579 -27.611 16.649 1.00 69.18  ? 438 GLN   B CD   1 
ATOM   1614 O OE1  . GLN   A 1 223 ? -28.875 -27.734 15.447 1.00 72.84  ? 438 GLN   B OE1  1 
ATOM   1615 N NE2  . GLN   A 1 223 ? -28.277 -28.652 17.428 1.00 67.26  ? 438 GLN   B NE2  1 
ATOM   1616 N N    . HIS   A 1 224 ? -27.634 -23.049 17.943 1.00 48.25  ? 439 HIS   B N    1 
ATOM   1617 C CA   . HIS   A 1 224 ? -26.616 -22.013 18.029 1.00 50.47  ? 439 HIS   B CA   1 
ATOM   1618 C C    . HIS   A 1 224 ? -25.295 -22.651 18.420 1.00 48.70  ? 439 HIS   B C    1 
ATOM   1619 O O    . HIS   A 1 224 ? -25.229 -23.824 18.780 1.00 53.11  ? 439 HIS   B O    1 
ATOM   1620 C CB   . HIS   A 1 224 ? -27.010 -20.926 19.037 1.00 49.81  ? 439 HIS   B CB   1 
ATOM   1621 C CG   . HIS   A 1 224 ? -27.158 -21.453 20.425 1.00 49.69  ? 439 HIS   B CG   1 
ATOM   1622 N ND1  . HIS   A 1 224 ? -26.074 -21.735 21.227 1.00 49.54  ? 439 HIS   B ND1  1 
ATOM   1623 C CD2  . HIS   A 1 224 ? -28.255 -21.815 21.127 1.00 48.00  ? 439 HIS   B CD2  1 
ATOM   1624 C CE1  . HIS   A 1 224 ? -26.497 -22.222 22.376 1.00 44.11  ? 439 HIS   B CE1  1 
ATOM   1625 N NE2  . HIS   A 1 224 ? -27.817 -22.280 22.341 1.00 47.52  ? 439 HIS   B NE2  1 
ATOM   1626 N N    . HIS   A 1 225 ? -24.238 -21.854 18.342 1.00 50.38  ? 440 HIS   B N    1 
ATOM   1627 C CA   . HIS   A 1 225 ? -22.878 -22.298 18.609 1.00 52.17  ? 440 HIS   B CA   1 
ATOM   1628 C C    . HIS   A 1 225 ? -22.124 -21.055 19.045 1.00 52.62  ? 440 HIS   B C    1 
ATOM   1629 O O    . HIS   A 1 225 ? -22.250 -20.007 18.406 1.00 51.60  ? 440 HIS   B O    1 
ATOM   1630 C CB   . HIS   A 1 225 ? -22.238 -22.928 17.363 1.00 58.00  ? 440 HIS   B CB   1 
ATOM   1631 C CG   . HIS   A 1 225 ? -21.091 -23.844 17.649 1.00 59.62  ? 440 HIS   B CG   1 
ATOM   1632 N ND1  . HIS   A 1 225 ? -20.036 -23.490 18.460 1.00 58.13  ? 440 HIS   B ND1  1 
ATOM   1633 C CD2  . HIS   A 1 225 ? -20.804 -25.082 17.181 1.00 67.98  ? 440 HIS   B CD2  1 
ATOM   1634 C CE1  . HIS   A 1 225 ? -19.166 -24.481 18.516 1.00 62.94  ? 440 HIS   B CE1  1 
ATOM   1635 N NE2  . HIS   A 1 225 ? -19.605 -25.458 17.743 1.00 70.02  ? 440 HIS   B NE2  1 
ATOM   1636 N N    . ILE   A 1 226 ? -21.379 -21.163 20.140 1.00 53.66  ? 441 ILE   B N    1 
ATOM   1637 C CA   . ILE   A 1 226 ? -20.745 -20.026 20.784 1.00 53.12  ? 441 ILE   B CA   1 
ATOM   1638 C C    . ILE   A 1 226 ? -19.240 -20.220 20.742 1.00 57.16  ? 441 ILE   B C    1 
ATOM   1639 O O    . ILE   A 1 226 ? -18.732 -21.270 21.140 1.00 58.71  ? 441 ILE   B O    1 
ATOM   1640 C CB   . ILE   A 1 226 ? -21.233 -19.866 22.230 1.00 56.33  ? 441 ILE   B CB   1 
ATOM   1641 C CG1  . ILE   A 1 226 ? -22.744 -19.609 22.253 1.00 54.46  ? 441 ILE   B CG1  1 
ATOM   1642 C CG2  . ILE   A 1 226 ? -20.450 -18.774 22.939 1.00 57.76  ? 441 ILE   B CG2  1 
ATOM   1643 C CD1  . ILE   A 1 226 ? -23.359 -19.636 23.679 1.00 52.39  ? 441 ILE   B CD1  1 
ATOM   1644 N N    . TYR   A 1 227 ? -18.530 -19.210 20.261 1.00 59.88  ? 442 TYR   B N    1 
ATOM   1645 C CA   . TYR   A 1 227 ? -17.079 -19.235 20.180 1.00 63.12  ? 442 TYR   B CA   1 
ATOM   1646 C C    . TYR   A 1 227 ? -16.505 -18.101 21.016 1.00 59.44  ? 442 TYR   B C    1 
ATOM   1647 O O    . TYR   A 1 227 ? -17.153 -17.065 21.199 1.00 56.24  ? 442 TYR   B O    1 
ATOM   1648 C CB   . TYR   A 1 227 ? -16.601 -19.070 18.721 1.00 64.29  ? 442 TYR   B CB   1 
ATOM   1649 C CG   . TYR   A 1 227 ? -17.218 -20.039 17.734 1.00 63.24  ? 442 TYR   B CG   1 
ATOM   1650 C CD1  . TYR   A 1 227 ? -18.521 -19.863 17.279 1.00 59.39  ? 442 TYR   B CD1  1 
ATOM   1651 C CD2  . TYR   A 1 227 ? -16.492 -21.116 17.244 1.00 67.11  ? 442 TYR   B CD2  1 
ATOM   1652 C CE1  . TYR   A 1 227 ? -19.086 -20.739 16.390 1.00 58.45  ? 442 TYR   B CE1  1 
ATOM   1653 C CE2  . TYR   A 1 227 ? -17.048 -21.993 16.346 1.00 67.36  ? 442 TYR   B CE2  1 
ATOM   1654 C CZ   . TYR   A 1 227 ? -18.346 -21.800 15.922 1.00 63.71  ? 442 TYR   B CZ   1 
ATOM   1655 O OH   . TYR   A 1 227 ? -18.908 -22.676 15.024 1.00 69.63  ? 442 TYR   B OH   1 
ATOM   1656 N N    . ARG   A 1 228 ? -15.278 -18.284 21.496 1.00 61.15  ? 443 ARG   B N    1 
ATOM   1657 C CA   . ARG   A 1 228 ? -14.486 -17.138 21.921 1.00 63.82  ? 443 ARG   B CA   1 
ATOM   1658 C C    . ARG   A 1 228 ? -13.856 -16.456 20.711 1.00 66.01  ? 443 ARG   B C    1 
ATOM   1659 O O    . ARG   A 1 228 ? -13.455 -17.115 19.749 1.00 71.56  ? 443 ARG   B O    1 
ATOM   1660 C CB   . ARG   A 1 228 ? -13.375 -17.544 22.883 1.00 67.29  ? 443 ARG   B CB   1 
ATOM   1661 C CG   . ARG   A 1 228 ? -13.771 -18.445 24.020 1.00 72.91  ? 443 ARG   B CG   1 
ATOM   1662 C CD   . ARG   A 1 228 ? -12.520 -18.745 24.828 1.00 79.27  ? 443 ARG   B CD   1 
ATOM   1663 N NE   . ARG   A 1 228 ? -12.356 -20.161 25.117 1.00 84.11  ? 443 ARG   B NE   1 
ATOM   1664 C CZ   . ARG   A 1 228 ? -11.718 -21.006 24.319 1.00 87.01  ? 443 ARG   B CZ   1 
ATOM   1665 N NH1  . ARG   A 1 228 ? -11.241 -20.624 23.145 1.00 83.14  ? 443 ARG   B NH1  1 
ATOM   1666 N NH2  . ARG   A 1 228 ? -11.565 -22.270 24.701 1.00 89.94  ? 443 ARG   B NH2  1 
ATOM   1667 N N    . LEU   A 1 229 ? -13.767 -15.128 20.762 1.00 65.75  ? 444 LEU   B N    1 
ATOM   1668 C CA   . LEU   A 1 229 ? -13.084 -14.350 19.730 1.00 68.23  ? 444 LEU   B CA   1 
ATOM   1669 C C    . LEU   A 1 229 ? -11.664 -14.032 20.184 1.00 74.85  ? 444 LEU   B C    1 
ATOM   1670 O O    . LEU   A 1 229 ? -11.464 -13.441 21.252 1.00 76.74  ? 444 LEU   B O    1 
ATOM   1671 C CB   . LEU   A 1 229 ? -13.830 -13.054 19.418 1.00 63.88  ? 444 LEU   B CB   1 
ATOM   1672 C CG   . LEU   A 1 229 ? -14.951 -13.132 18.387 1.00 63.69  ? 444 LEU   B CG   1 
ATOM   1673 C CD1  . LEU   A 1 229 ? -15.545 -11.762 18.178 1.00 61.70  ? 444 LEU   B CD1  1 
ATOM   1674 C CD2  . LEU   A 1 229 ? -14.451 -13.708 17.057 1.00 69.50  ? 444 LEU   B CD2  1 
ATOM   1675 N N    . VAL   A 1 230 ? -10.689 -14.390 19.349 1.00 75.56  ? 445 VAL   B N    1 
ATOM   1676 C CA   . VAL   A 1 230 ? -9.278  -14.377 19.719 1.00 79.47  ? 445 VAL   B CA   1 
ATOM   1677 C C    . VAL   A 1 230 ? -8.437  -13.646 18.676 1.00 84.70  ? 445 VAL   B C    1 
ATOM   1678 O O    . VAL   A 1 230 ? -8.973  -13.007 17.764 1.00 83.67  ? 445 VAL   B O    1 
ATOM   1679 C CB   . VAL   A 1 230 ? -8.785  -15.817 19.902 1.00 78.69  ? 445 VAL   B CB   1 
ATOM   1680 C CG1  . VAL   A 1 230 ? -9.434  -16.430 21.141 1.00 76.52  ? 445 VAL   B CG1  1 
ATOM   1681 C CG2  . VAL   A 1 230 ? -9.128  -16.617 18.660 1.00 76.59  ? 445 VAL   B CG2  1 
ATOM   1682 N N    . ARG   A 1 231 ? -7.115  -13.741 18.799 1.00 92.09  ? 446 ARG   B N    1 
ATOM   1683 C CA   . ARG   A 1 231 ? -6.213  -13.088 17.848 1.00 97.32  ? 446 ARG   B CA   1 
ATOM   1684 C C    . ARG   A 1 231 ? -4.942  -13.904 17.580 1.00 98.55  ? 446 ARG   B C    1 
ATOM   1685 O O    . ARG   A 1 231 ? -4.020  -13.932 18.395 1.00 102.99 ? 446 ARG   B O    1 
ATOM   1686 C CB   . ARG   A 1 231 ? -5.852  -11.694 18.357 1.00 100.02 ? 446 ARG   B CB   1 
ATOM   1687 C CG   . ARG   A 1 231 ? -5.543  -10.695 17.266 1.00 102.15 ? 446 ARG   B CG   1 
ATOM   1688 C CD   . ARG   A 1 231 ? -5.323  -9.307  17.844 1.00 104.28 ? 446 ARG   B CD   1 
ATOM   1689 N NE   . ARG   A 1 231 ? -4.800  -9.318  19.207 1.00 105.09 ? 446 ARG   B NE   1 
ATOM   1690 C CZ   . ARG   A 1 231 ? -3.718  -9.974  19.612 1.00 110.38 ? 446 ARG   B CZ   1 
ATOM   1691 N NH1  . ARG   A 1 231 ? -2.999  -10.715 18.779 1.00 111.26 ? 446 ARG   B NH1  1 
ATOM   1692 N NH2  . ARG   A 1 231 ? -3.342  -9.881  20.886 1.00 112.29 ? 446 ARG   B NH2  1 
ATOM   1693 N N    . GLY   B 1 7   ? -42.674 28.454  27.644 1.00 70.02  ? 222 GLY   A N    1 
ATOM   1694 C CA   . GLY   B 1 7   ? -41.623 27.500  27.963 1.00 63.45  ? 222 GLY   A CA   1 
ATOM   1695 C C    . GLY   B 1 7   ? -41.861 26.127  27.362 1.00 60.86  ? 222 GLY   A C    1 
ATOM   1696 O O    . GLY   B 1 7   ? -42.969 25.813  26.936 1.00 61.13  ? 222 GLY   A O    1 
ATOM   1697 N N    . LEU   B 1 8   ? -40.821 25.298  27.329 1.00 60.80  ? 223 LEU   A N    1 
ATOM   1698 C CA   . LEU   B 1 8   ? -40.937 23.919  26.853 1.00 59.59  ? 223 LEU   A CA   1 
ATOM   1699 C C    . LEU   B 1 8   ? -41.311 23.039  28.051 1.00 61.10  ? 223 LEU   A C    1 
ATOM   1700 O O    . LEU   B 1 8   ? -40.454 22.563  28.800 1.00 60.22  ? 223 LEU   A O    1 
ATOM   1701 C CB   . LEU   B 1 8   ? -39.634 23.494  26.181 1.00 58.21  ? 223 LEU   A CB   1 
ATOM   1702 C CG   . LEU   B 1 8   ? -39.371 22.048  25.718 1.00 63.01  ? 223 LEU   A CG   1 
ATOM   1703 C CD1  . LEU   B 1 8   ? -40.578 21.413  25.032 1.00 63.14  ? 223 LEU   A CD1  1 
ATOM   1704 C CD2  . LEU   B 1 8   ? -38.133 21.955  24.786 1.00 56.28  ? 223 LEU   A CD2  1 
ATOM   1705 N N    . GLY   B 1 9   ? -42.607 22.835  28.262 1.00 59.73  ? 224 GLY   A N    1 
ATOM   1706 C CA   . GLY   B 1 9   ? -43.021 21.967  29.343 1.00 60.57  ? 224 GLY   A CA   1 
ATOM   1707 C C    . GLY   B 1 9   ? -44.507 22.053  29.601 1.00 60.05  ? 224 GLY   A C    1 
ATOM   1708 O O    . GLY   B 1 9   ? -45.220 22.867  29.006 1.00 61.94  ? 224 GLY   A O    1 
ATOM   1709 N N    . THR   B 1 10  ? -44.966 21.186  30.512 1.00 58.30  ? 225 THR   A N    1 
ATOM   1710 C CA   . THR   B 1 10  ? -46.367 21.161  30.918 1.00 62.16  ? 225 THR   A CA   1 
ATOM   1711 C C    . THR   B 1 10  ? -46.485 21.579  32.386 1.00 62.88  ? 225 THR   A C    1 
ATOM   1712 O O    . THR   B 1 10  ? -45.508 21.971  33.039 1.00 62.03  ? 225 THR   A O    1 
ATOM   1713 C CB   . THR   B 1 10  ? -46.987 19.773  30.744 1.00 61.33  ? 225 THR   A CB   1 
ATOM   1714 O OG1  . THR   B 1 10  ? -46.170 18.809  31.414 1.00 61.69  ? 225 THR   A OG1  1 
ATOM   1715 C CG2  . THR   B 1 10  ? -47.077 19.394  29.261 1.00 59.18  ? 225 THR   A CG2  1 
ATOM   1716 N N    . ALA   B 1 11  ? -47.705 21.469  32.910 1.00 63.16  ? 226 ALA   A N    1 
ATOM   1717 C CA   . ALA   B 1 11  ? -47.938 21.601  34.345 1.00 63.91  ? 226 ALA   A CA   1 
ATOM   1718 C C    . ALA   B 1 11  ? -47.195 20.551  35.162 1.00 62.74  ? 226 ALA   A C    1 
ATOM   1719 O O    . ALA   B 1 11  ? -47.058 20.717  36.380 1.00 66.40  ? 226 ALA   A O    1 
ATOM   1720 C CB   . ALA   B 1 11  ? -49.432 21.488  34.638 1.00 69.25  ? 226 ALA   A CB   1 
ATOM   1721 N N    . ARG   B 1 12  ? -46.742 19.462  34.537 1.00 61.82  ? 227 ARG   A N    1 
ATOM   1722 C CA   . ARG   B 1 12  ? -46.146 18.348  35.257 1.00 61.86  ? 227 ARG   A CA   1 
ATOM   1723 C C    . ARG   B 1 12  ? -44.642 18.253  35.095 1.00 60.77  ? 227 ARG   A C    1 
ATOM   1724 O O    . ARG   B 1 12  ? -43.985 17.628  35.926 1.00 58.95  ? 227 ARG   A O    1 
ATOM   1725 C CB   . ARG   B 1 12  ? -46.756 17.022  34.779 1.00 61.37  ? 227 ARG   A CB   1 
ATOM   1726 C CG   . ARG   B 1 12  ? -48.219 16.837  35.114 1.00 64.30  ? 227 ARG   A CG   1 
ATOM   1727 C CD   . ARG   B 1 12  ? -48.653 15.453  34.709 1.00 65.08  ? 227 ARG   A CD   1 
ATOM   1728 N NE   . ARG   B 1 12  ? -48.431 14.471  35.762 1.00 63.29  ? 227 ARG   A NE   1 
ATOM   1729 C CZ   . ARG   B 1 12  ? -48.654 13.174  35.608 1.00 66.01  ? 227 ARG   A CZ   1 
ATOM   1730 N NH1  . ARG   B 1 12  ? -49.037 12.678  34.441 1.00 69.73  ? 227 ARG   A NH1  1 
ATOM   1731 N NH2  . ARG   B 1 12  ? -48.482 12.353  36.645 1.00 62.36  ? 227 ARG   A NH2  1 
ATOM   1732 N N    . LEU   B 1 13  ? -44.084 18.815  34.035 1.00 64.44  ? 228 LEU   A N    1 
ATOM   1733 C CA   . LEU   B 1 13  ? -42.671 18.617  33.770 1.00 61.70  ? 228 LEU   A CA   1 
ATOM   1734 C C    . LEU   B 1 13  ? -42.223 19.695  32.801 1.00 63.13  ? 228 LEU   A C    1 
ATOM   1735 O O    . LEU   B 1 13  ? -42.957 20.057  31.872 1.00 61.85  ? 228 LEU   A O    1 
ATOM   1736 C CB   . LEU   B 1 13  ? -42.412 17.217  33.202 1.00 56.14  ? 228 LEU   A CB   1 
ATOM   1737 C CG   . LEU   B 1 13  ? -40.965 16.753  33.115 1.00 57.63  ? 228 LEU   A CG   1 
ATOM   1738 C CD1  . LEU   B 1 13  ? -40.505 16.267  34.486 1.00 58.35  ? 228 LEU   A CD1  1 
ATOM   1739 C CD2  . LEU   B 1 13  ? -40.821 15.674  32.062 1.00 54.59  ? 228 LEU   A CD2  1 
ATOM   1740 N N    . GLN   B 1 14  ? -41.039 20.234  33.049 1.00 59.15  ? 229 GLN   A N    1 
ATOM   1741 C CA   . GLN   B 1 14  ? -40.484 21.251  32.182 1.00 58.20  ? 229 GLN   A CA   1 
ATOM   1742 C C    . GLN   B 1 14  ? -39.023 20.935  31.943 1.00 60.54  ? 229 GLN   A C    1 
ATOM   1743 O O    . GLN   B 1 14  ? -38.328 20.448  32.840 1.00 60.08  ? 229 GLN   A O    1 
ATOM   1744 C CB   . GLN   B 1 14  ? -40.601 22.658  32.771 1.00 61.32  ? 229 GLN   A CB   1 
ATOM   1745 C CG   . GLN   B 1 14  ? -41.877 22.941  33.492 1.00 62.33  ? 229 GLN   A CG   1 
ATOM   1746 C CD   . GLN   B 1 14  ? -41.669 23.014  34.993 1.00 70.33  ? 229 GLN   A CD   1 
ATOM   1747 O OE1  . GLN   B 1 14  ? -41.498 21.983  35.675 1.00 73.44  ? 229 GLN   A OE1  1 
ATOM   1748 N NE2  . GLN   B 1 14  ? -41.683 24.242  35.530 1.00 83.20  ? 229 GLN   A NE2  1 
ATOM   1749 N N    . LEU   B 1 15  ? -38.564 21.308  30.766 1.00 62.80  ? 230 LEU   A N    1 
ATOM   1750 C CA   . LEU   B 1 15  ? -37.179 21.290  30.432 1.00 57.98  ? 230 LEU   A CA   1 
ATOM   1751 C C    . LEU   B 1 15  ? -36.555 22.471  31.089 1.00 56.93  ? 230 LEU   A C    1 
ATOM   1752 O O    . LEU   B 1 15  ? -37.069 23.550  31.008 1.00 61.47  ? 230 LEU   A O    1 
ATOM   1753 C CB   . LEU   B 1 15  ? -37.060 21.454  28.939 1.00 60.83  ? 230 LEU   A CB   1 
ATOM   1754 C CG   . LEU   B 1 15  ? -36.066 20.631  28.153 1.00 58.86  ? 230 LEU   A CG   1 
ATOM   1755 C CD1  . LEU   B 1 15  ? -35.278 21.587  27.299 1.00 61.45  ? 230 LEU   A CD1  1 
ATOM   1756 C CD2  . LEU   B 1 15  ? -35.138 19.851  29.048 1.00 54.24  ? 230 LEU   A CD2  1 
ATOM   1757 N N    . VAL   B 1 16  ? -35.436 22.280  31.738 1.00 60.46  ? 231 VAL   A N    1 
ATOM   1758 C CA   . VAL   B 1 16  ? -34.729 23.420  32.300 1.00 68.47  ? 231 VAL   A CA   1 
ATOM   1759 C C    . VAL   B 1 16  ? -33.440 23.714  31.538 1.00 71.60  ? 231 VAL   A C    1 
ATOM   1760 O O    . VAL   B 1 16  ? -33.037 24.882  31.440 1.00 73.68  ? 231 VAL   A O    1 
ATOM   1761 C CB   . VAL   B 1 16  ? -34.448 23.255  33.819 1.00 71.39  ? 231 VAL   A CB   1 
ATOM   1762 C CG1  . VAL   B 1 16  ? -35.733 22.975  34.573 1.00 65.47  ? 231 VAL   A CG1  1 
ATOM   1763 C CG2  . VAL   B 1 16  ? -33.410 22.178  34.111 1.00 69.23  ? 231 VAL   A CG2  1 
ATOM   1764 N N    . GLU   B 1 17  ? -32.810 22.692  30.965 1.00 62.87  ? 232 GLU   A N    1 
ATOM   1765 C CA   . GLU   B 1 17  ? -31.641 22.829  30.120 1.00 58.98  ? 232 GLU   A CA   1 
ATOM   1766 C C    . GLU   B 1 17  ? -31.530 21.598  29.252 1.00 57.53  ? 232 GLU   A C    1 
ATOM   1767 O O    . GLU   B 1 17  ? -31.918 20.502  29.659 1.00 56.67  ? 232 GLU   A O    1 
ATOM   1768 C CB   . GLU   B 1 17  ? -30.361 22.998  30.934 1.00 62.79  ? 232 GLU   A CB   1 
ATOM   1769 C CG   . GLU   B 1 17  ? -29.505 24.135  30.446 1.00 69.46  ? 232 GLU   A CG   1 
ATOM   1770 C CD   . GLU   B 1 17  ? -28.356 24.390  31.366 1.00 74.16  ? 232 GLU   A CD   1 
ATOM   1771 O OE1  . GLU   B 1 17  ? -27.210 24.495  30.864 1.00 68.37  ? 232 GLU   A OE1  1 
ATOM   1772 O OE2  . GLU   B 1 17  ? -28.623 24.465  32.600 1.00 85.49  ? 232 GLU   A OE2  1 
ATOM   1773 N N    . PHE   B 1 18  ? -30.994 21.797  28.050 1.00 57.16  ? 233 PHE   A N    1 
ATOM   1774 C CA   . PHE   B 1 18  ? -30.635 20.706  27.158 1.00 55.00  ? 233 PHE   A CA   1 
ATOM   1775 C C    . PHE   B 1 18  ? -29.485 21.187  26.286 1.00 55.67  ? 233 PHE   A C    1 
ATOM   1776 O O    . PHE   B 1 18  ? -29.552 22.269  25.690 1.00 56.25  ? 233 PHE   A O    1 
ATOM   1777 C CB   . PHE   B 1 18  ? -31.810 20.257  26.282 1.00 54.31  ? 233 PHE   A CB   1 
ATOM   1778 C CG   . PHE   B 1 18  ? -31.402 19.319  25.190 1.00 51.37  ? 233 PHE   A CG   1 
ATOM   1779 C CD1  . PHE   B 1 18  ? -30.947 19.807  23.968 1.00 55.80  ? 233 PHE   A CD1  1 
ATOM   1780 C CD2  . PHE   B 1 18  ? -31.416 17.949  25.393 1.00 50.25  ? 233 PHE   A CD2  1 
ATOM   1781 C CE1  . PHE   B 1 18  ? -30.535 18.927  22.950 1.00 56.21  ? 233 PHE   A CE1  1 
ATOM   1782 C CE2  . PHE   B 1 18  ? -31.009 17.068  24.391 1.00 53.54  ? 233 PHE   A CE2  1 
ATOM   1783 C CZ   . PHE   B 1 18  ? -30.567 17.550  23.169 1.00 53.74  ? 233 PHE   A CZ   1 
ATOM   1784 N N    . SER   B 1 19  ? -28.435 20.384  26.217 1.00 52.61  ? 234 SER   A N    1 
ATOM   1785 C CA   . SER   B 1 19  ? -27.293 20.712  25.391 1.00 54.66  ? 234 SER   A CA   1 
ATOM   1786 C C    . SER   B 1 19  ? -26.742 19.432  24.778 1.00 52.75  ? 234 SER   A C    1 
ATOM   1787 O O    . SER   B 1 19  ? -26.843 18.347  25.360 1.00 51.52  ? 234 SER   A O    1 
ATOM   1788 C CB   . SER   B 1 19  ? -26.216 21.444  26.197 1.00 54.19  ? 234 SER   A CB   1 
ATOM   1789 O OG   . SER   B 1 19  ? -25.542 20.573  27.084 1.00 57.30  ? 234 SER   A OG   1 
ATOM   1790 N N    . ALA   B 1 20  ? -26.180 19.565  23.583 1.00 54.73  ? 235 ALA   A N    1 
ATOM   1791 C CA   . ALA   B 1 20  ? -25.338 18.525  23.007 1.00 55.78  ? 235 ALA   A CA   1 
ATOM   1792 C C    . ALA   B 1 20  ? -24.003 19.169  22.679 1.00 53.23  ? 235 ALA   A C    1 
ATOM   1793 O O    . ALA   B 1 20  ? -23.960 20.334  22.276 1.00 51.86  ? 235 ALA   A O    1 
ATOM   1794 C CB   . ALA   B 1 20  ? -25.986 17.892  21.781 1.00 50.03  ? 235 ALA   A CB   1 
ATOM   1795 N N    . PHE   B 1 21  ? -22.912 18.444  22.904 1.00 53.66  ? 236 PHE   A N    1 
ATOM   1796 C CA   . PHE   B 1 21  ? -21.616 19.112  22.978 1.00 56.53  ? 236 PHE   A CA   1 
ATOM   1797 C C    . PHE   B 1 21  ? -20.483 18.143  22.683 1.00 56.08  ? 236 PHE   A C    1 
ATOM   1798 O O    . PHE   B 1 21  ? -20.653 16.923  22.733 1.00 56.31  ? 236 PHE   A O    1 
ATOM   1799 C CB   . PHE   B 1 21  ? -21.409 19.730  24.364 1.00 58.02  ? 236 PHE   A CB   1 
ATOM   1800 C CG   . PHE   B 1 21  ? -21.580 18.750  25.493 1.00 60.82  ? 236 PHE   A CG   1 
ATOM   1801 C CD1  . PHE   B 1 21  ? -20.516 17.989  25.947 1.00 65.53  ? 236 PHE   A CD1  1 
ATOM   1802 C CD2  . PHE   B 1 21  ? -22.811 18.588  26.103 1.00 62.31  ? 236 PHE   A CD2  1 
ATOM   1803 C CE1  . PHE   B 1 21  ? -20.677 17.096  27.003 1.00 67.87  ? 236 PHE   A CE1  1 
ATOM   1804 C CE2  . PHE   B 1 21  ? -22.975 17.690  27.166 1.00 62.10  ? 236 PHE   A CE2  1 
ATOM   1805 C CZ   . PHE   B 1 21  ? -21.907 16.948  27.610 1.00 64.71  ? 236 PHE   A CZ   1 
ATOM   1806 N N    . VAL   B 1 22  ? -19.310 18.706  22.403 1.00 60.00  ? 237 VAL   A N    1 
ATOM   1807 C CA   . VAL   B 1 22  ? -18.081 17.931  22.329 1.00 64.47  ? 237 VAL   A CA   1 
ATOM   1808 C C    . VAL   B 1 22  ? -17.082 18.551  23.289 1.00 71.12  ? 237 VAL   A C    1 
ATOM   1809 O O    . VAL   B 1 22  ? -16.896 19.771  23.297 1.00 70.18  ? 237 VAL   A O    1 
ATOM   1810 C CB   . VAL   B 1 22  ? -17.509 17.837  20.897 1.00 66.70  ? 237 VAL   A CB   1 
ATOM   1811 C CG1  . VAL   B 1 22  ? -17.252 19.227  20.250 1.00 62.32  ? 237 VAL   A CG1  1 
ATOM   1812 C CG2  . VAL   B 1 22  ? -16.236 17.001  20.912 1.00 69.32  ? 237 VAL   A CG2  1 
ATOM   1813 N N    . GLU   B 1 23  ? -16.488 17.709  24.131 1.00 79.79  ? 238 GLU   A N    1 
ATOM   1814 C CA   . GLU   B 1 23  ? -15.507 18.048  25.151 1.00 86.63  ? 238 GLU   A CA   1 
ATOM   1815 C C    . GLU   B 1 23  ? -14.159 17.501  24.715 1.00 96.02  ? 238 GLU   A C    1 
ATOM   1816 O O    . GLU   B 1 23  ? -14.084 16.323  24.339 1.00 96.45  ? 238 GLU   A O    1 
ATOM   1817 C CB   . GLU   B 1 23  ? -15.903 17.434  26.512 1.00 84.21  ? 238 GLU   A CB   1 
ATOM   1818 C CG   . GLU   B 1 23  ? -16.428 18.393  27.577 1.00 81.44  ? 238 GLU   A CG   1 
ATOM   1819 C CD   . GLU   B 1 23  ? -17.198 17.663  28.692 1.00 83.44  ? 238 GLU   A CD   1 
ATOM   1820 O OE1  . GLU   B 1 23  ? -17.179 16.413  28.697 1.00 82.79  ? 238 GLU   A OE1  1 
ATOM   1821 O OE2  . GLU   B 1 23  ? -17.820 18.328  29.563 1.00 82.26  ? 238 GLU   A OE2  1 
ATOM   1822 N N    . PRO   B 1 24  ? -13.084 18.286  24.739 1.00 110.19 ? 239 PRO   A N    1 
ATOM   1823 C CA   . PRO   B 1 24  ? -11.807 17.812  24.174 1.00 115.78 ? 239 PRO   A CA   1 
ATOM   1824 C C    . PRO   B 1 24  ? -11.218 16.690  25.012 1.00 117.94 ? 239 PRO   A C    1 
ATOM   1825 O O    . PRO   B 1 24  ? -11.684 16.434  26.134 1.00 113.78 ? 239 PRO   A O    1 
ATOM   1826 C CB   . PRO   B 1 24  ? -10.915 19.066  24.201 1.00 119.77 ? 239 PRO   A CB   1 
ATOM   1827 C CG   . PRO   B 1 24  ? -11.849 20.222  24.490 1.00 116.31 ? 239 PRO   A CG   1 
ATOM   1828 C CD   . PRO   B 1 24  ? -12.962 19.641  25.300 1.00 110.68 ? 239 PRO   A CD   1 
ATOM   1829 N N    . PRO   B 1 25  ? -10.182 15.990  24.498 1.00 114.18 ? 240 PRO   A N    1 
ATOM   1830 C CA   . PRO   B 1 25  ? -9.520  14.839  25.125 1.00 111.80 ? 240 PRO   A CA   1 
ATOM   1831 C C    . PRO   B 1 25  ? -9.532  14.862  26.650 1.00 114.44 ? 240 PRO   A C    1 
ATOM   1832 O O    . PRO   B 1 25  ? -10.489 14.354  27.235 1.00 115.24 ? 240 PRO   A O    1 
ATOM   1833 C CB   . PRO   B 1 25  ? -8.090  14.946  24.598 1.00 112.16 ? 240 PRO   A CB   1 
ATOM   1834 C CG   . PRO   B 1 25  ? -8.239  15.572  23.244 1.00 111.23 ? 240 PRO   A CG   1 
ATOM   1835 C CD   . PRO   B 1 25  ? -9.565  16.312  23.197 1.00 109.54 ? 240 PRO   A CD   1 
ATOM   1836 N N    . ARG   B 1 33  ? -15.924 23.022  26.601 1.00 72.34  ? 248 ARG   A N    1 
ATOM   1837 C CA   . ARG   B 1 33  ? -16.840 22.333  25.702 1.00 67.62  ? 248 ARG   A CA   1 
ATOM   1838 C C    . ARG   B 1 33  ? -17.071 23.147  24.434 1.00 64.82  ? 248 ARG   A C    1 
ATOM   1839 O O    . ARG   B 1 33  ? -16.629 24.291  24.320 1.00 67.54  ? 248 ARG   A O    1 
ATOM   1840 C CB   . ARG   B 1 33  ? -18.189 22.073  26.376 1.00 66.89  ? 248 ARG   A CB   1 
ATOM   1841 C CG   . ARG   B 1 33  ? -18.092 21.423  27.738 1.00 73.00  ? 248 ARG   A CG   1 
ATOM   1842 C CD   . ARG   B 1 33  ? -19.056 20.252  27.922 1.00 71.48  ? 248 ARG   A CD   1 
ATOM   1843 N NE   . ARG   B 1 33  ? -20.426 20.639  28.237 1.00 73.72  ? 248 ARG   A NE   1 
ATOM   1844 C CZ   . ARG   B 1 33  ? -21.174 20.066  29.180 1.00 76.49  ? 248 ARG   A CZ   1 
ATOM   1845 N NH1  . ARG   B 1 33  ? -20.684 19.136  29.995 1.00 74.05  ? 248 ARG   A NH1  1 
ATOM   1846 N NH2  . ARG   B 1 33  ? -22.441 20.450  29.325 1.00 73.72  ? 248 ARG   A NH2  1 
ATOM   1847 N N    . HIS   B 1 34  ? -17.739 22.518  23.468 1.00 63.63  ? 249 HIS   A N    1 
ATOM   1848 C CA   . HIS   B 1 34  ? -18.345 23.187  22.329 1.00 59.36  ? 249 HIS   A CA   1 
ATOM   1849 C C    . HIS   B 1 34  ? -19.767 22.671  22.239 1.00 55.98  ? 249 HIS   A C    1 
ATOM   1850 O O    . HIS   B 1 34  ? -19.982 21.460  22.131 1.00 57.59  ? 249 HIS   A O    1 
ATOM   1851 C CB   . HIS   B 1 34  ? -17.596 22.897  21.021 1.00 61.05  ? 249 HIS   A CB   1 
ATOM   1852 C CG   . HIS   B 1 34  ? -18.392 23.224  19.792 1.00 59.73  ? 249 HIS   A CG   1 
ATOM   1853 N ND1  . HIS   B 1 34  ? -18.448 24.493  19.251 1.00 62.71  ? 249 HIS   A ND1  1 
ATOM   1854 C CD2  . HIS   B 1 34  ? -19.204 22.454  19.028 1.00 58.32  ? 249 HIS   A CD2  1 
ATOM   1855 C CE1  . HIS   B 1 34  ? -19.240 24.484  18.193 1.00 63.57  ? 249 HIS   A CE1  1 
ATOM   1856 N NE2  . HIS   B 1 34  ? -19.720 23.262  18.042 1.00 60.18  ? 249 HIS   A NE2  1 
ATOM   1857 N N    . LEU   B 1 35  ? -20.734 23.571  22.290 1.00 56.21  ? 250 LEU   A N    1 
ATOM   1858 C CA   . LEU   B 1 35  ? -22.131 23.169  22.234 1.00 55.77  ? 250 LEU   A CA   1 
ATOM   1859 C C    . LEU   B 1 35  ? -22.623 23.197  20.792 1.00 52.98  ? 250 LEU   A C    1 
ATOM   1860 O O    . LEU   B 1 35  ? -22.667 24.258  20.162 1.00 54.33  ? 250 LEU   A O    1 
ATOM   1861 C CB   . LEU   B 1 35  ? -22.981 24.079  23.117 1.00 52.28  ? 250 LEU   A CB   1 
ATOM   1862 C CG   . LEU   B 1 35  ? -22.421 24.262  24.540 1.00 55.71  ? 250 LEU   A CG   1 
ATOM   1863 C CD1  . LEU   B 1 35  ? -23.228 25.288  25.323 1.00 55.58  ? 250 LEU   A CD1  1 
ATOM   1864 C CD2  . LEU   B 1 35  ? -22.324 22.940  25.290 1.00 56.23  ? 250 LEU   A CD2  1 
ATOM   1865 N N    . PHE   B 1 36  ? -22.993 22.030  20.274 1.00 52.47  ? 251 PHE   A N    1 
ATOM   1866 C CA   . PHE   B 1 36  ? -23.682 21.967  18.990 1.00 51.14  ? 251 PHE   A CA   1 
ATOM   1867 C C    . PHE   B 1 36  ? -25.053 22.619  19.070 1.00 53.91  ? 251 PHE   A C    1 
ATOM   1868 O O    . PHE   B 1 36  ? -25.473 23.307  18.138 1.00 55.73  ? 251 PHE   A O    1 
ATOM   1869 C CB   . PHE   B 1 36  ? -23.836 20.518  18.544 1.00 51.87  ? 251 PHE   A CB   1 
ATOM   1870 C CG   . PHE   B 1 36  ? -22.548 19.748  18.507 1.00 55.05  ? 251 PHE   A CG   1 
ATOM   1871 C CD1  . PHE   B 1 36  ? -21.546 20.074  17.575 1.00 52.63  ? 251 PHE   A CD1  1 
ATOM   1872 C CD2  . PHE   B 1 36  ? -22.348 18.675  19.385 1.00 49.07  ? 251 PHE   A CD2  1 
ATOM   1873 C CE1  . PHE   B 1 36  ? -20.362 19.359  17.534 1.00 52.42  ? 251 PHE   A CE1  1 
ATOM   1874 C CE2  . PHE   B 1 36  ? -21.172 17.949  19.349 1.00 53.37  ? 251 PHE   A CE2  1 
ATOM   1875 C CZ   . PHE   B 1 36  ? -20.168 18.292  18.412 1.00 57.53  ? 251 PHE   A CZ   1 
ATOM   1876 N N    . VAL   B 1 37  ? -25.782 22.383  20.161 1.00 52.46  ? 252 VAL   A N    1 
ATOM   1877 C CA   . VAL   B 1 37  ? -27.085 22.995  20.389 1.00 50.47  ? 252 VAL   A CA   1 
ATOM   1878 C C    . VAL   B 1 37  ? -27.300 23.076  21.890 1.00 54.93  ? 252 VAL   A C    1 
ATOM   1879 O O    . VAL   B 1 37  ? -26.765 22.264  22.654 1.00 55.38  ? 252 VAL   A O    1 
ATOM   1880 C CB   . VAL   B 1 37  ? -28.223 22.201  19.709 1.00 52.44  ? 252 VAL   A CB   1 
ATOM   1881 C CG1  . VAL   B 1 37  ? -28.023 22.167  18.165 1.00 52.64  ? 252 VAL   A CG1  1 
ATOM   1882 C CG2  . VAL   B 1 37  ? -28.305 20.808  20.294 1.00 50.24  ? 252 VAL   A CG2  1 
ATOM   1883 N N    . HIS   B 1 38  ? -28.106 24.047  22.317 1.00 53.24  ? 253 HIS   A N    1 
ATOM   1884 C CA   . HIS   B 1 38  ? -28.265 24.292  23.748 1.00 55.60  ? 253 HIS   A CA   1 
ATOM   1885 C C    . HIS   B 1 38  ? -29.586 24.997  24.018 1.00 57.88  ? 253 HIS   A C    1 
ATOM   1886 O O    . HIS   B 1 38  ? -29.828 26.084  23.486 1.00 58.31  ? 253 HIS   A O    1 
ATOM   1887 C CB   . HIS   B 1 38  ? -27.080 25.110  24.279 1.00 55.91  ? 253 HIS   A CB   1 
ATOM   1888 C CG   . HIS   B 1 38  ? -27.218 25.512  25.718 1.00 64.55  ? 253 HIS   A CG   1 
ATOM   1889 N ND1  . HIS   B 1 38  ? -26.332 25.096  26.694 1.00 65.86  ? 253 HIS   A ND1  1 
ATOM   1890 C CD2  . HIS   B 1 38  ? -28.088 26.346  26.338 1.00 64.36  ? 253 HIS   A CD2  1 
ATOM   1891 C CE1  . HIS   B 1 38  ? -26.673 25.623  27.856 1.00 64.21  ? 253 HIS   A CE1  1 
ATOM   1892 N NE2  . HIS   B 1 38  ? -27.731 26.390  27.666 1.00 65.15  ? 253 HIS   A NE2  1 
ATOM   1893 N N    . ILE   B 1 39  ? -30.433 24.393  24.853 1.00 60.36  ? 254 ILE   A N    1 
ATOM   1894 C CA   . ILE   B 1 39  ? -31.642 25.034  25.358 1.00 60.88  ? 254 ILE   A CA   1 
ATOM   1895 C C    . ILE   B 1 39  ? -31.427 25.276  26.842 1.00 65.26  ? 254 ILE   A C    1 
ATOM   1896 O O    . ILE   B 1 39  ? -31.360 24.325  27.631 1.00 63.59  ? 254 ILE   A O    1 
ATOM   1897 C CB   . ILE   B 1 39  ? -32.900 24.186  25.124 1.00 59.71  ? 254 ILE   A CB   1 
ATOM   1898 C CG1  . ILE   B 1 39  ? -33.104 23.924  23.627 1.00 56.25  ? 254 ILE   A CG1  1 
ATOM   1899 C CG2  . ILE   B 1 39  ? -34.110 24.852  25.773 1.00 57.88  ? 254 ILE   A CG2  1 
ATOM   1900 C CD1  . ILE   B 1 39  ? -34.220 22.963  23.280 1.00 51.30  ? 254 ILE   A CD1  1 
ATOM   1901 N N    . SER   B 1 40  ? -31.300 26.540  27.230 1.00 68.84  ? 255 SER   A N    1 
ATOM   1902 C CA   . SER   B 1 40  ? -31.208 26.914  28.632 1.00 67.76  ? 255 SER   A CA   1 
ATOM   1903 C C    . SER   B 1 40  ? -32.446 27.708  29.003 1.00 71.23  ? 255 SER   A C    1 
ATOM   1904 O O    . SER   B 1 40  ? -32.758 28.713  28.369 1.00 72.23  ? 255 SER   A O    1 
ATOM   1905 C CB   . SER   B 1 40  ? -29.958 27.737  28.914 1.00 69.05  ? 255 SER   A CB   1 
ATOM   1906 O OG   . SER   B 1 40  ? -30.120 28.446  30.131 1.00 79.69  ? 255 SER   A OG   1 
ATOM   1907 N N    . GLN   B 1 41  ? -33.157 27.261  30.034 1.00 75.39  ? 256 GLN   A N    1 
ATOM   1908 C CA   . GLN   B 1 41  ? -34.396 27.916  30.405 1.00 83.00  ? 256 GLN   A CA   1 
ATOM   1909 C C    . GLN   B 1 41  ? -34.252 28.407  31.835 1.00 91.14  ? 256 GLN   A C    1 
ATOM   1910 O O    . GLN   B 1 41  ? -33.690 29.489  32.063 1.00 93.37  ? 256 GLN   A O    1 
ATOM   1911 C CB   . GLN   B 1 41  ? -35.575 26.971  30.124 1.00 74.93  ? 256 GLN   A CB   1 
ATOM   1912 C CG   . GLN   B 1 41  ? -36.213 27.205  28.744 1.00 69.74  ? 256 GLN   A CG   1 
ATOM   1913 C CD   . GLN   B 1 41  ? -37.246 26.156  28.373 1.00 64.36  ? 256 GLN   A CD   1 
ATOM   1914 O OE1  . GLN   B 1 41  ? -38.014 26.319  27.420 1.00 64.45  ? 256 GLN   A OE1  1 
ATOM   1915 N NE2  . GLN   B 1 41  ? -37.258 25.063  29.113 1.00 65.03  ? 256 GLN   A NE2  1 
ATOM   1916 N N    . HIS   B 1 42  ? -34.739 27.659  32.827 1.00 103.47 ? 257 HIS   A N    1 
ATOM   1917 C CA   . HIS   B 1 42  ? -34.588 27.971  34.257 1.00 108.33 ? 257 HIS   A CA   1 
ATOM   1918 C C    . HIS   B 1 42  ? -35.665 28.930  34.791 1.00 111.14 ? 257 HIS   A C    1 
ATOM   1919 O O    . HIS   B 1 42  ? -35.963 29.969  34.193 1.00 111.89 ? 257 HIS   A O    1 
ATOM   1920 C CB   . HIS   B 1 42  ? -33.195 28.551  34.558 1.00 109.86 ? 257 HIS   A CB   1 
ATOM   1921 C CG   . HIS   B 1 42  ? -32.078 27.557  34.432 1.00 111.54 ? 257 HIS   A CG   1 
ATOM   1922 N ND1  . HIS   B 1 42  ? -31.418 27.040  35.527 1.00 112.01 ? 257 HIS   A ND1  1 
ATOM   1923 C CD2  . HIS   B 1 42  ? -31.481 27.014  33.343 1.00 108.20 ? 257 HIS   A CD2  1 
ATOM   1924 C CE1  . HIS   B 1 42  ? -30.478 26.205  35.119 1.00 111.70 ? 257 HIS   A CE1  1 
ATOM   1925 N NE2  . HIS   B 1 42  ? -30.494 26.171  33.798 1.00 107.50 ? 257 HIS   A NE2  1 
ATOM   1926 N N    . PRO   B 1 49  ? -44.376 36.347  25.991 1.00 124.35 ? 264 PRO   A N    1 
ATOM   1927 C CA   . PRO   B 1 49  ? -45.223 35.855  24.901 1.00 117.86 ? 264 PRO   A CA   1 
ATOM   1928 C C    . PRO   B 1 49  ? -45.223 34.339  24.748 1.00 115.84 ? 264 PRO   A C    1 
ATOM   1929 O O    . PRO   B 1 49  ? -44.195 33.700  24.968 1.00 117.51 ? 264 PRO   A O    1 
ATOM   1930 C CB   . PRO   B 1 49  ? -44.604 36.544  23.666 1.00 118.34 ? 264 PRO   A CB   1 
ATOM   1931 C CG   . PRO   B 1 49  ? -43.280 37.132  24.205 1.00 125.09 ? 264 PRO   A CG   1 
ATOM   1932 C CD   . PRO   B 1 49  ? -43.708 37.574  25.543 1.00 127.11 ? 264 PRO   A CD   1 
ATOM   1933 N N    . PRO   B 1 50  ? -46.371 33.777  24.376 1.00 104.91 ? 265 PRO   A N    1 
ATOM   1934 C CA   . PRO   B 1 50  ? -46.480 32.320  24.233 1.00 98.25  ? 265 PRO   A CA   1 
ATOM   1935 C C    . PRO   B 1 50  ? -45.578 31.801  23.125 1.00 89.48  ? 265 PRO   A C    1 
ATOM   1936 O O    . PRO   B 1 50  ? -44.997 32.553  22.342 1.00 90.01  ? 265 PRO   A O    1 
ATOM   1937 C CB   . PRO   B 1 50  ? -47.955 32.100  23.881 1.00 97.38  ? 265 PRO   A CB   1 
ATOM   1938 C CG   . PRO   B 1 50  ? -48.652 33.362  24.323 1.00 97.61  ? 265 PRO   A CG   1 
ATOM   1939 C CD   . PRO   B 1 50  ? -47.655 34.459  24.143 1.00 101.09 ? 265 PRO   A CD   1 
ATOM   1940 N N    . LEU   B 1 51  ? -45.480 30.481  23.056 1.00 85.84  ? 266 LEU   A N    1 
ATOM   1941 C CA   . LEU   B 1 51  ? -44.770 29.863  21.954 1.00 79.57  ? 266 LEU   A CA   1 
ATOM   1942 C C    . LEU   B 1 51  ? -45.627 29.913  20.697 1.00 82.97  ? 266 LEU   A C    1 
ATOM   1943 O O    . LEU   B 1 51  ? -46.862 29.896  20.763 1.00 86.29  ? 266 LEU   A O    1 
ATOM   1944 C CB   . LEU   B 1 51  ? -44.408 28.420  22.289 1.00 71.14  ? 266 LEU   A CB   1 
ATOM   1945 C CG   . LEU   B 1 51  ? -43.509 28.295  23.512 1.00 69.01  ? 266 LEU   A CG   1 
ATOM   1946 C CD1  . LEU   B 1 51  ? -43.486 26.843  24.036 1.00 62.83  ? 266 LEU   A CD1  1 
ATOM   1947 C CD2  . LEU   B 1 51  ? -42.103 28.833  23.207 1.00 60.92  ? 266 LEU   A CD2  1 
ATOM   1948 N N    . GLU   B 1 52  ? -44.958 30.008  19.548 1.00 74.16  ? 267 GLU   A N    1 
ATOM   1949 C CA   . GLU   B 1 52  ? -45.645 29.862  18.278 1.00 76.20  ? 267 GLU   A CA   1 
ATOM   1950 C C    . GLU   B 1 52  ? -46.136 28.426  18.138 1.00 74.79  ? 267 GLU   A C    1 
ATOM   1951 O O    . GLU   B 1 52  ? -45.670 27.512  18.827 1.00 71.47  ? 267 GLU   A O    1 
ATOM   1952 C CB   . GLU   B 1 52  ? -44.718 30.225  17.115 1.00 79.81  ? 267 GLU   A CB   1 
ATOM   1953 C CG   . GLU   B 1 52  ? -45.299 31.244  16.141 1.00 79.66  ? 267 GLU   A CG   1 
ATOM   1954 C CD   . GLU   B 1 52  ? -44.235 31.920  15.289 1.00 82.73  ? 267 GLU   A CD   1 
ATOM   1955 O OE1  . GLU   B 1 52  ? -43.583 31.229  14.469 1.00 81.55  ? 267 GLU   A OE1  1 
ATOM   1956 O OE2  . GLU   B 1 52  ? -44.073 33.152  15.408 1.00 87.46  ? 267 GLU   A OE2  1 
ATOM   1957 N N    . SER   B 1 53  ? -47.102 28.226  17.250 1.00 79.53  ? 268 SER   A N    1 
ATOM   1958 C CA   . SER   B 1 53  ? -47.679 26.904  17.060 1.00 79.02  ? 268 SER   A CA   1 
ATOM   1959 C C    . SER   B 1 53  ? -47.430 26.427  15.638 1.00 78.47  ? 268 SER   A C    1 
ATOM   1960 O O    . SER   B 1 53  ? -47.456 27.217  14.688 1.00 79.88  ? 268 SER   A O    1 
ATOM   1961 C CB   . SER   B 1 53  ? -49.184 26.888  17.382 1.00 80.91  ? 268 SER   A CB   1 
ATOM   1962 O OG   . SER   B 1 53  ? -49.952 27.414  16.319 1.00 87.93  ? 268 SER   A OG   1 
ATOM   1963 N N    . VAL   B 1 54  ? -47.178 25.127  15.517 1.00 78.37  ? 269 VAL   A N    1 
ATOM   1964 C CA   . VAL   B 1 54  ? -46.891 24.445  14.262 1.00 75.38  ? 269 VAL   A CA   1 
ATOM   1965 C C    . VAL   B 1 54  ? -47.817 23.248  14.161 1.00 77.97  ? 269 VAL   A C    1 
ATOM   1966 O O    . VAL   B 1 54  ? -47.932 22.471  15.118 1.00 76.95  ? 269 VAL   A O    1 
ATOM   1967 C CB   . VAL   B 1 54  ? -45.426 23.976  14.193 1.00 72.01  ? 269 VAL   A CB   1 
ATOM   1968 C CG1  . VAL   B 1 54  ? -45.179 23.234  12.909 1.00 73.19  ? 269 VAL   A CG1  1 
ATOM   1969 C CG2  . VAL   B 1 54  ? -44.485 25.161  14.314 1.00 72.65  ? 269 VAL   A CG2  1 
ATOM   1970 N N    . ASP   B 1 55  ? -48.468 23.084  13.011 1.00 80.18  ? 270 ASP   A N    1 
ATOM   1971 C CA   . ASP   B 1 55  ? -49.377 21.958  12.853 1.00 82.75  ? 270 ASP   A CA   1 
ATOM   1972 C C    . ASP   B 1 55  ? -48.580 20.671  12.681 1.00 83.87  ? 270 ASP   A C    1 
ATOM   1973 O O    . ASP   B 1 55  ? -47.820 20.526  11.718 1.00 86.71  ? 270 ASP   A O    1 
ATOM   1974 C CB   . ASP   B 1 55  ? -50.324 22.169  11.683 1.00 87.20  ? 270 ASP   A CB   1 
ATOM   1975 C CG   . ASP   B 1 55  ? -51.566 21.315  11.803 1.00 94.92  ? 270 ASP   A CG   1 
ATOM   1976 O OD1  . ASP   B 1 55  ? -51.490 20.123  11.440 1.00 95.96  ? 270 ASP   A OD1  1 
ATOM   1977 O OD2  . ASP   B 1 55  ? -52.611 21.822  12.280 1.00 96.42  ? 270 ASP   A OD2  1 
ATOM   1978 N N    . VAL   B 1 56  ? -48.765 19.740  13.623 1.00 86.19  ? 271 VAL   A N    1 
ATOM   1979 C CA   . VAL   B 1 56  ? -48.011 18.488  13.655 1.00 84.79  ? 271 VAL   A CA   1 
ATOM   1980 C C    . VAL   B 1 56  ? -48.144 17.731  12.342 1.00 92.28  ? 271 VAL   A C    1 
ATOM   1981 O O    . VAL   B 1 56  ? -47.213 17.034  11.916 1.00 91.85  ? 271 VAL   A O    1 
ATOM   1982 C CB   . VAL   B 1 56  ? -48.478 17.632  14.853 1.00 81.13  ? 271 VAL   A CB   1 
ATOM   1983 C CG1  . VAL   B 1 56  ? -49.909 17.171  14.648 1.00 85.63  ? 271 VAL   A CG1  1 
ATOM   1984 C CG2  . VAL   B 1 56  ? -47.561 16.451  15.055 1.00 79.96  ? 271 VAL   A CG2  1 
ATOM   1985 N N    . ARG   B 1 57  ? -49.297 17.848  11.680 1.00 100.11 ? 272 ARG   A N    1 
ATOM   1986 C CA   . ARG   B 1 57  ? -49.459 17.231  10.369 1.00 99.67  ? 272 ARG   A CA   1 
ATOM   1987 C C    . ARG   B 1 57  ? -48.307 17.576  9.444  1.00 98.60  ? 272 ARG   A C    1 
ATOM   1988 O O    . ARG   B 1 57  ? -47.895 16.743  8.628  1.00 99.60  ? 272 ARG   A O    1 
ATOM   1989 C CB   . ARG   B 1 57  ? -50.787 17.661  9.742  1.00 101.20 ? 272 ARG   A CB   1 
ATOM   1990 C CG   . ARG   B 1 57  ? -52.020 17.219  10.532 1.00 104.67 ? 272 ARG   A CG   1 
ATOM   1991 C CD   . ARG   B 1 57  ? -53.302 17.728  9.901  1.00 106.02 ? 272 ARG   A CD   1 
ATOM   1992 N NE   . ARG   B 1 57  ? -53.687 19.042  10.402 1.00 106.40 ? 272 ARG   A NE   1 
ATOM   1993 C CZ   . ARG   B 1 57  ? -53.645 20.164  9.695  1.00 111.21 ? 272 ARG   A CZ   1 
ATOM   1994 N NH1  . ARG   B 1 57  ? -53.155 20.193  8.461  1.00 109.03 ? 272 ARG   A NH1  1 
ATOM   1995 N NH2  . ARG   B 1 57  ? -54.092 21.290  10.246 1.00 115.37 ? 272 ARG   A NH2  1 
ATOM   1996 N N    . GLN   B 1 58  ? -47.761 18.789  9.566  1.00 91.54  ? 273 GLN   A N    1 
ATOM   1997 C CA   . GLN   B 1 58  ? -46.717 19.250  8.654  1.00 91.56  ? 273 GLN   A CA   1 
ATOM   1998 C C    . GLN   B 1 58  ? -45.412 18.473  8.806  1.00 90.50  ? 273 GLN   A C    1 
ATOM   1999 O O    . GLN   B 1 58  ? -44.493 18.691  8.008  1.00 90.49  ? 273 GLN   A O    1 
ATOM   2000 C CB   . GLN   B 1 58  ? -46.444 20.744  8.876  1.00 89.86  ? 273 GLN   A CB   1 
ATOM   2001 C CG   . GLN   B 1 58  ? -47.692 21.626  9.034  1.00 91.67  ? 273 GLN   A CG   1 
ATOM   2002 C CD   . GLN   B 1 58  ? -48.380 22.019  7.734  1.00 94.96  ? 273 GLN   A CD   1 
ATOM   2003 O OE1  . GLN   B 1 58  ? -48.037 21.544  6.649  1.00 98.24  ? 273 GLN   A OE1  1 
ATOM   2004 N NE2  . GLN   B 1 58  ? -49.387 22.882  7.849  1.00 94.60  ? 273 GLN   A NE2  1 
ATOM   2005 N N    . ILE   B 1 59  ? -45.299 17.575  9.788  1.00 91.66  ? 274 ILE   A N    1 
ATOM   2006 C CA   . ILE   B 1 59  ? -44.022 16.913  10.035 1.00 89.42  ? 274 ILE   A CA   1 
ATOM   2007 C C    . ILE   B 1 59  ? -44.192 15.416  10.289 1.00 93.93  ? 274 ILE   A C    1 
ATOM   2008 O O    . ILE   B 1 59  ? -43.335 14.787  10.922 1.00 91.72  ? 274 ILE   A O    1 
ATOM   2009 C CB   . ILE   B 1 59  ? -43.284 17.583  11.210 1.00 82.38  ? 274 ILE   A CB   1 
ATOM   2010 C CG1  . ILE   B 1 59  ? -44.199 17.702  12.425 1.00 82.76  ? 274 ILE   A CG1  1 
ATOM   2011 C CG2  . ILE   B 1 59  ? -42.804 18.961  10.830 1.00 80.93  ? 274 ILE   A CG2  1 
ATOM   2012 C CD1  . ILE   B 1 59  ? -43.455 17.736  13.740 1.00 72.87  ? 274 ILE   A CD1  1 
ATOM   2013 N N    . TYR   B 1 60  ? -45.286 14.827  9.796  1.00 91.81  ? 275 TYR   A N    1 
ATOM   2014 C CA   . TYR   B 1 60  ? -45.475 13.385  9.961  1.00 95.57  ? 275 TYR   A CA   1 
ATOM   2015 C C    . TYR   B 1 60  ? -44.498 12.603  9.091  1.00 96.00  ? 275 TYR   A C    1 
ATOM   2016 O O    . TYR   B 1 60  ? -43.974 11.560  9.504  1.00 92.25  ? 275 TYR   A O    1 
ATOM   2017 C CB   . TYR   B 1 60  ? -46.914 12.998  9.619  1.00 98.41  ? 275 TYR   A CB   1 
ATOM   2018 C CG   . TYR   B 1 60  ? -47.924 13.272  10.710 1.00 99.36  ? 275 TYR   A CG   1 
ATOM   2019 C CD1  . TYR   B 1 60  ? -47.564 13.216  12.051 1.00 94.15  ? 275 TYR   A CD1  1 
ATOM   2020 C CD2  . TYR   B 1 60  ? -49.247 13.566  10.396 1.00 101.37 ? 275 TYR   A CD2  1 
ATOM   2021 C CE1  . TYR   B 1 60  ? -48.491 13.457  13.048 1.00 94.28  ? 275 TYR   A CE1  1 
ATOM   2022 C CE2  . TYR   B 1 60  ? -50.182 13.810  11.386 1.00 101.32 ? 275 TYR   A CE2  1 
ATOM   2023 C CZ   . TYR   B 1 60  ? -49.800 13.754  12.711 1.00 99.66  ? 275 TYR   A CZ   1 
ATOM   2024 O OH   . TYR   B 1 60  ? -50.729 13.994  13.704 1.00 98.06  ? 275 TYR   A OH   1 
ATOM   2025 N N    . ASP   B 1 61  ? -44.273 13.091  7.870  1.00 100.99 ? 276 ASP   A N    1 
ATOM   2026 C CA   . ASP   B 1 61  ? -43.265 12.553  6.958  1.00 103.20 ? 276 ASP   A CA   1 
ATOM   2027 C C    . ASP   B 1 61  ? -41.901 12.392  7.618  1.00 101.89 ? 276 ASP   A C    1 
ATOM   2028 O O    . ASP   B 1 61  ? -41.124 11.508  7.233  1.00 99.74  ? 276 ASP   A O    1 
ATOM   2029 C CB   . ASP   B 1 61  ? -43.131 13.513  5.784  1.00 103.46 ? 276 ASP   A CB   1 
ATOM   2030 C CG   . ASP   B 1 61  ? -42.962 14.946  6.262  1.00 104.41 ? 276 ASP   A CG   1 
ATOM   2031 O OD1  . ASP   B 1 61  ? -41.821 15.320  6.610  1.00 104.31 ? 276 ASP   A OD1  1 
ATOM   2032 O OD2  . ASP   B 1 61  ? -43.973 15.675  6.364  1.00 105.78 ? 276 ASP   A OD2  1 
ATOM   2033 N N    . LYS   B 1 62  ? -41.580 13.261  8.585  1.00 91.96  ? 277 LYS   A N    1 
ATOM   2034 C CA   . LYS   B 1 62  ? -40.248 13.348  9.174  1.00 82.68  ? 277 LYS   A CA   1 
ATOM   2035 C C    . LYS   B 1 62  ? -39.997 12.310  10.254 1.00 76.35  ? 277 LYS   A C    1 
ATOM   2036 O O    . LYS   B 1 62  ? -38.914 12.314  10.849 1.00 69.99  ? 277 LYS   A O    1 
ATOM   2037 C CB   . LYS   B 1 62  ? -40.008 14.747  9.759  1.00 77.58  ? 277 LYS   A CB   1 
ATOM   2038 C CG   . LYS   B 1 62  ? -39.967 15.862  8.725  1.00 84.43  ? 277 LYS   A CG   1 
ATOM   2039 C CD   . LYS   B 1 62  ? -38.679 16.680  8.793  1.00 81.04  ? 277 LYS   A CD   1 
ATOM   2040 C CE   . LYS   B 1 62  ? -38.973 18.188  8.804  1.00 80.78  ? 277 LYS   A CE   1 
ATOM   2041 N NZ   . LYS   B 1 62  ? -37.752 19.059  8.645  1.00 77.35  ? 277 LYS   A NZ   1 
ATOM   2042 N N    . PHE   B 1 63  ? -40.950 11.429  10.541 1.00 86.26  ? 278 PHE   A N    1 
ATOM   2043 C CA   . PHE   B 1 63  ? -40.779 10.445  11.578 1.00 84.88  ? 278 PHE   A CA   1 
ATOM   2044 C C    . PHE   B 1 63  ? -41.496 9.141   11.161 1.00 92.02  ? 278 PHE   A C    1 
ATOM   2045 O O    . PHE   B 1 63  ? -42.399 9.205   10.324 1.00 95.84  ? 278 PHE   A O    1 
ATOM   2046 C CB   . PHE   B 1 63  ? -41.323 10.930  12.930 1.00 83.57  ? 278 PHE   A CB   1 
ATOM   2047 C CG   . PHE   B 1 63  ? -40.663 12.201  13.418 1.00 73.76  ? 278 PHE   A CG   1 
ATOM   2048 C CD1  . PHE   B 1 63  ? -41.090 13.437  12.967 1.00 70.88  ? 278 PHE   A CD1  1 
ATOM   2049 C CD2  . PHE   B 1 63  ? -39.608 12.150  14.310 1.00 65.14  ? 278 PHE   A CD2  1 
ATOM   2050 C CE1  . PHE   B 1 63  ? -40.478 14.580  13.391 1.00 68.69  ? 278 PHE   A CE1  1 
ATOM   2051 C CE2  . PHE   B 1 63  ? -39.003 13.291  14.741 1.00 60.58  ? 278 PHE   A CE2  1 
ATOM   2052 C CZ   . PHE   B 1 63  ? -39.435 14.506  14.287 1.00 61.79  ? 278 PHE   A CZ   1 
ATOM   2053 N N    . PRO   B 1 64  ? -41.091 8.027   11.719 1.00 102.29 ? 279 PRO   A N    1 
ATOM   2054 C CA   . PRO   B 1 64  ? -41.763 6.758   11.366 1.00 106.87 ? 279 PRO   A CA   1 
ATOM   2055 C C    . PRO   B 1 64  ? -43.260 6.848   11.610 1.00 109.41 ? 279 PRO   A C    1 
ATOM   2056 O O    . PRO   B 1 64  ? -43.714 7.166   12.714 1.00 109.26 ? 279 PRO   A O    1 
ATOM   2057 C CB   . PRO   B 1 64  ? -41.091 5.731   12.290 1.00 104.92 ? 279 PRO   A CB   1 
ATOM   2058 C CG   . PRO   B 1 64  ? -40.455 6.536   13.383 1.00 101.91 ? 279 PRO   A CG   1 
ATOM   2059 C CD   . PRO   B 1 64  ? -40.042 7.819   12.729 1.00 100.12 ? 279 PRO   A CD   1 
ATOM   2060 N N    . GLU   B 1 65  ? -44.031 6.590   10.556 1.00 110.31 ? 280 GLU   A N    1 
ATOM   2061 C CA   . GLU   B 1 65  ? -45.451 6.328   10.723 1.00 112.66 ? 280 GLU   A CA   1 
ATOM   2062 C C    . GLU   B 1 65  ? -45.694 4.940   11.281 1.00 119.91 ? 280 GLU   A C    1 
ATOM   2063 O O    . GLU   B 1 65  ? -46.836 4.469   11.299 1.00 120.18 ? 280 GLU   A O    1 
ATOM   2064 C CB   . GLU   B 1 65  ? -46.180 6.501   9.390  1.00 110.05 ? 280 GLU   A CB   1 
ATOM   2065 C CG   . GLU   B 1 65  ? -45.921 7.839   8.716  1.00 106.51 ? 280 GLU   A CG   1 
ATOM   2066 C CD   . GLU   B 1 65  ? -47.115 8.779   8.800  1.00 106.71 ? 280 GLU   A CD   1 
ATOM   2067 O OE1  . GLU   B 1 65  ? -48.121 8.427   9.455  1.00 106.80 ? 280 GLU   A OE1  1 
ATOM   2068 O OE2  . GLU   B 1 65  ? -47.046 9.878   8.211  1.00 106.38 ? 280 GLU   A OE2  1 
ATOM   2069 N N    . LYS   B 1 66  ? -44.634 4.298   11.756 1.00 137.39 ? 281 LYS   A N    1 
ATOM   2070 C CA   . LYS   B 1 66  ? -44.629 2.864   12.019 1.00 138.28 ? 281 LYS   A CA   1 
ATOM   2071 C C    . LYS   B 1 66  ? -44.648 2.594   13.523 1.00 136.92 ? 281 LYS   A C    1 
ATOM   2072 O O    . LYS   B 1 66  ? -43.753 1.970   14.095 1.00 135.14 ? 281 LYS   A O    1 
ATOM   2073 C CB   . LYS   B 1 66  ? -43.423 2.224   11.340 1.00 136.11 ? 281 LYS   A CB   1 
ATOM   2074 N N    . LYS   B 1 67  ? -45.712 3.092   14.154 1.00 118.11 ? 282 LYS   A N    1 
ATOM   2075 C CA   . LYS   B 1 67  ? -45.988 2.876   15.569 1.00 109.54 ? 282 LYS   A CA   1 
ATOM   2076 C C    . LYS   B 1 67  ? -44.888 3.445   16.454 1.00 106.90 ? 282 LYS   A C    1 
ATOM   2077 O O    . LYS   B 1 67  ? -43.694 3.264   16.188 1.00 108.71 ? 282 LYS   A O    1 
ATOM   2078 C CB   . LYS   B 1 67  ? -46.186 1.390   15.867 1.00 110.86 ? 282 LYS   A CB   1 
ATOM   2079 C CG   . LYS   B 1 67  ? -46.314 1.086   17.353 1.00 108.03 ? 282 LYS   A CG   1 
ATOM   2080 N N    . GLY   B 1 68  ? -45.292 4.126   17.525 1.00 100.16 ? 283 GLY   A N    1 
ATOM   2081 C CA   . GLY   B 1 68  ? -44.366 4.845   18.361 1.00 93.28  ? 283 GLY   A CA   1 
ATOM   2082 C C    . GLY   B 1 68  ? -43.934 6.177   17.807 1.00 91.38  ? 283 GLY   A C    1 
ATOM   2083 O O    . GLY   B 1 68  ? -43.337 6.968   18.548 1.00 91.99  ? 283 GLY   A O    1 
ATOM   2084 N N    . GLY   B 1 69  ? -44.219 6.455   16.530 1.00 91.94  ? 284 GLY   A N    1 
ATOM   2085 C CA   . GLY   B 1 69  ? -43.867 7.718   15.920 1.00 89.91  ? 284 GLY   A CA   1 
ATOM   2086 C C    . GLY   B 1 69  ? -44.932 8.781   16.140 1.00 87.04  ? 284 GLY   A C    1 
ATOM   2087 O O    . GLY   B 1 69  ? -45.989 8.536   16.724 1.00 86.88  ? 284 GLY   A O    1 
ATOM   2088 N N    . LEU   B 1 70  ? -44.639 9.983   15.631 1.00 83.87  ? 285 LEU   A N    1 
ATOM   2089 C CA   . LEU   B 1 70  ? -45.460 11.166  15.868 1.00 81.91  ? 285 LEU   A CA   1 
ATOM   2090 C C    . LEU   B 1 70  ? -46.960 10.917  15.768 1.00 85.12  ? 285 LEU   A C    1 
ATOM   2091 O O    . LEU   B 1 70  ? -47.679 11.070  16.759 1.00 83.38  ? 285 LEU   A O    1 
ATOM   2092 C CB   . LEU   B 1 70  ? -45.066 12.281  14.902 1.00 80.25  ? 285 LEU   A CB   1 
ATOM   2093 C CG   . LEU   B 1 70  ? -45.159 13.662  15.557 1.00 78.82  ? 285 LEU   A CG   1 
ATOM   2094 C CD1  . LEU   B 1 70  ? -44.623 13.594  16.993 1.00 73.80  ? 285 LEU   A CD1  1 
ATOM   2095 C CD2  . LEU   B 1 70  ? -44.419 14.730  14.748 1.00 73.97  ? 285 LEU   A CD2  1 
ATOM   2096 N N    . ARG   B 1 71  ? -47.447 10.558  14.580 1.00 95.34  ? 286 ARG   A N    1 
ATOM   2097 C CA   . ARG   B 1 71  ? -48.888 10.408  14.392 1.00 98.68  ? 286 ARG   A CA   1 
ATOM   2098 C C    . ARG   B 1 71  ? -49.512 9.581   15.512 1.00 96.99  ? 286 ARG   A C    1 
ATOM   2099 O O    . ARG   B 1 71  ? -50.541 9.962   16.084 1.00 99.11  ? 286 ARG   A O    1 
ATOM   2100 C CB   . ARG   B 1 71  ? -49.178 9.783   13.025 1.00 101.09 ? 286 ARG   A CB   1 
ATOM   2101 C CG   . ARG   B 1 71  ? -50.540 10.158  12.455 1.00 104.47 ? 286 ARG   A CG   1 
ATOM   2102 C CD   . ARG   B 1 71  ? -50.996 9.161   11.396 1.00 109.08 ? 286 ARG   A CD   1 
ATOM   2103 N NE   . ARG   B 1 71  ? -50.718 9.622   10.037 1.00 112.15 ? 286 ARG   A NE   1 
ATOM   2104 C CZ   . ARG   B 1 71  ? -51.202 10.737  9.504  1.00 112.12 ? 286 ARG   A CZ   1 
ATOM   2105 N NH1  . ARG   B 1 71  ? -51.989 11.550  10.194 1.00 113.37 ? 286 ARG   A NH1  1 
ATOM   2106 N NH2  . ARG   B 1 71  ? -50.891 11.045  8.247  1.00 109.85 ? 286 ARG   A NH2  1 
ATOM   2107 N N    . GLU   B 1 72  ? -48.884 8.455   15.833 1.00 89.71  ? 287 GLU   A N    1 
ATOM   2108 C CA   . GLU   B 1 72  ? -49.375 7.581   16.893 1.00 86.15  ? 287 GLU   A CA   1 
ATOM   2109 C C    . GLU   B 1 72  ? -49.453 8.310   18.232 1.00 83.84  ? 287 GLU   A C    1 
ATOM   2110 O O    . GLU   B 1 72  ? -50.528 8.436   18.819 1.00 81.51  ? 287 GLU   A O    1 
ATOM   2111 C CB   . GLU   B 1 72  ? -48.485 6.343   17.020 1.00 87.17  ? 287 GLU   A CB   1 
ATOM   2112 C CG   . GLU   B 1 72  ? -49.240 5.026   16.941 1.00 88.47  ? 287 GLU   A CG   1 
ATOM   2113 C CD   . GLU   B 1 72  ? -48.830 4.052   18.028 1.00 94.29  ? 287 GLU   A CD   1 
ATOM   2114 O OE1  . GLU   B 1 72  ? -48.022 4.438   18.899 1.00 95.37  ? 287 GLU   A OE1  1 
ATOM   2115 O OE2  . GLU   B 1 72  ? -49.315 2.902   18.013 1.00 94.72  ? 287 GLU   A OE2  1 
ATOM   2116 N N    . LEU   B 1 73  ? -48.308 8.787   18.709 1.00 81.66  ? 288 LEU   A N    1 
ATOM   2117 C CA   . LEU   B 1 73  ? -48.236 9.489   19.989 1.00 76.85  ? 288 LEU   A CA   1 
ATOM   2118 C C    . LEU   B 1 73  ? -49.232 10.633  20.050 1.00 77.09  ? 288 LEU   A C    1 
ATOM   2119 O O    . LEU   B 1 73  ? -50.003 10.752  21.007 1.00 77.46  ? 288 LEU   A O    1 
ATOM   2120 C CB   . LEU   B 1 73  ? -46.821 10.012  20.237 1.00 72.40  ? 288 LEU   A CB   1 
ATOM   2121 C CG   . LEU   B 1 73  ? -45.803 8.905   20.483 1.00 73.88  ? 288 LEU   A CG   1 
ATOM   2122 C CD1  . LEU   B 1 73  ? -44.500 9.434   21.042 1.00 68.38  ? 288 LEU   A CD1  1 
ATOM   2123 C CD2  . LEU   B 1 73  ? -46.415 7.895   21.417 1.00 74.38  ? 288 LEU   A CD2  1 
ATOM   2124 N N    . TYR   B 1 74  ? -49.235 11.490  19.035 1.00 77.02  ? 289 TYR   A N    1 
ATOM   2125 C CA   . TYR   B 1 74  ? -50.140 12.629  19.084 1.00 77.12  ? 289 TYR   A CA   1 
ATOM   2126 C C    . TYR   B 1 74  ? -51.584 12.191  19.267 1.00 80.77  ? 289 TYR   A C    1 
ATOM   2127 O O    . TYR   B 1 74  ? -52.361 12.882  19.935 1.00 78.61  ? 289 TYR   A O    1 
ATOM   2128 C CB   . TYR   B 1 74  ? -50.007 13.482  17.825 1.00 77.49  ? 289 TYR   A CB   1 
ATOM   2129 C CG   . TYR   B 1 74  ? -50.503 14.877  18.064 1.00 73.98  ? 289 TYR   A CG   1 
ATOM   2130 C CD1  . TYR   B 1 74  ? -49.723 15.802  18.745 1.00 70.69  ? 289 TYR   A CD1  1 
ATOM   2131 C CD2  . TYR   B 1 74  ? -51.770 15.259  17.654 1.00 79.66  ? 289 TYR   A CD2  1 
ATOM   2132 C CE1  . TYR   B 1 74  ? -50.182 17.081  18.983 1.00 70.52  ? 289 TYR   A CE1  1 
ATOM   2133 C CE2  . TYR   B 1 74  ? -52.239 16.533  17.891 1.00 80.47  ? 289 TYR   A CE2  1 
ATOM   2134 C CZ   . TYR   B 1 74  ? -51.444 17.440  18.557 1.00 76.32  ? 289 TYR   A CZ   1 
ATOM   2135 O OH   . TYR   B 1 74  ? -51.925 18.711  18.790 1.00 79.12  ? 289 TYR   A OH   1 
ATOM   2136 N N    . ASP   B 1 75  ? -51.959 11.041  18.706 1.00 83.03  ? 290 ASP   A N    1 
ATOM   2137 C CA   . ASP   B 1 75  ? -53.365 10.655  18.717 1.00 86.50  ? 290 ASP   A CA   1 
ATOM   2138 C C    . ASP   B 1 75  ? -53.816 10.186  20.097 1.00 84.23  ? 290 ASP   A C    1 
ATOM   2139 O O    . ASP   B 1 75  ? -54.991 10.338  20.447 1.00 83.91  ? 290 ASP   A O    1 
ATOM   2140 C CB   . ASP   B 1 75  ? -53.614 9.579   17.661 1.00 90.66  ? 290 ASP   A CB   1 
ATOM   2141 C CG   . ASP   B 1 75  ? -53.762 10.164  16.264 1.00 97.64  ? 290 ASP   A CG   1 
ATOM   2142 O OD1  . ASP   B 1 75  ? -53.569 11.396  16.115 1.00 97.56  ? 290 ASP   A OD1  1 
ATOM   2143 O OD2  . ASP   B 1 75  ? -54.084 9.404   15.321 1.00 101.07 ? 290 ASP   A OD2  1 
ATOM   2144 N N    . ARG   B 1 76  ? -52.905 9.621   20.890 1.00 80.80  ? 291 ARG   A N    1 
ATOM   2145 C CA   . ARG   B 1 76  ? -53.203 9.290   22.276 1.00 79.35  ? 291 ARG   A CA   1 
ATOM   2146 C C    . ARG   B 1 76  ? -53.152 10.505  23.193 1.00 78.64  ? 291 ARG   A C    1 
ATOM   2147 O O    . ARG   B 1 76  ? -53.797 10.497  24.245 1.00 85.63  ? 291 ARG   A O    1 
ATOM   2148 C CB   . ARG   B 1 76  ? -52.233 8.218   22.781 1.00 83.43  ? 291 ARG   A CB   1 
ATOM   2149 C CG   . ARG   B 1 76  ? -52.385 6.869   22.081 1.00 87.64  ? 291 ARG   A CG   1 
ATOM   2150 C CD   . ARG   B 1 76  ? -51.772 5.742   22.901 1.00 90.23  ? 291 ARG   A CD   1 
ATOM   2151 N NE   . ARG   B 1 76  ? -50.316 5.817   22.959 1.00 90.46  ? 291 ARG   A NE   1 
ATOM   2152 C CZ   . ARG   B 1 76  ? -49.499 4.886   22.483 1.00 90.87  ? 291 ARG   A CZ   1 
ATOM   2153 N NH1  . ARG   B 1 76  ? -49.962 3.789   21.905 1.00 93.66  ? 291 ARG   A NH1  1 
ATOM   2154 N NH2  . ARG   B 1 76  ? -48.184 5.047   22.613 1.00 89.49  ? 291 ARG   A NH2  1 
ATOM   2155 N N    . GLY   B 1 77  ? -52.412 11.542  22.828 1.00 75.97  ? 292 GLY   A N    1 
ATOM   2156 C CA   . GLY   B 1 77  ? -52.381 12.760  23.602 1.00 71.64  ? 292 GLY   A CA   1 
ATOM   2157 C C    . GLY   B 1 77  ? -51.512 12.630  24.833 1.00 69.30  ? 292 GLY   A C    1 
ATOM   2158 O O    . GLY   B 1 77  ? -50.789 11.643  25.012 1.00 69.87  ? 292 GLY   A O    1 
ATOM   2159 N N    . PRO   B 1 78  ? -51.570 13.637  25.718 1.00 68.41  ? 293 PRO   A N    1 
ATOM   2160 C CA   . PRO   B 1 78  ? -52.366 14.870  25.600 1.00 66.79  ? 293 PRO   A CA   1 
ATOM   2161 C C    . PRO   B 1 78  ? -51.704 15.873  24.680 1.00 62.65  ? 293 PRO   A C    1 
ATOM   2162 O O    . PRO   B 1 78  ? -50.506 16.119  24.791 1.00 61.82  ? 293 PRO   A O    1 
ATOM   2163 C CB   . PRO   B 1 78  ? -52.429 15.380  27.045 1.00 66.98  ? 293 PRO   A CB   1 
ATOM   2164 C CG   . PRO   B 1 78  ? -51.129 14.909  27.649 1.00 63.30  ? 293 PRO   A CG   1 
ATOM   2165 C CD   . PRO   B 1 78  ? -50.865 13.558  27.015 1.00 63.04  ? 293 PRO   A CD   1 
ATOM   2166 N N    . PRO   B 1 79  ? -52.481 16.486  23.788 1.00 59.86  ? 294 PRO   A N    1 
ATOM   2167 C CA   . PRO   B 1 79  ? -51.882 17.425  22.817 1.00 59.81  ? 294 PRO   A CA   1 
ATOM   2168 C C    . PRO   B 1 79  ? -50.896 18.397  23.444 1.00 59.81  ? 294 PRO   A C    1 
ATOM   2169 O O    . PRO   B 1 79  ? -49.770 18.545  22.957 1.00 62.71  ? 294 PRO   A O    1 
ATOM   2170 C CB   . PRO   B 1 79  ? -53.095 18.161  22.232 1.00 62.76  ? 294 PRO   A CB   1 
ATOM   2171 C CG   . PRO   B 1 79  ? -54.317 17.413  22.672 1.00 61.81  ? 294 PRO   A CG   1 
ATOM   2172 C CD   . PRO   B 1 79  ? -53.951 16.422  23.730 1.00 59.64  ? 294 PRO   A CD   1 
ATOM   2173 N N    . HIS   B 1 80  ? -51.291 19.058  24.531 1.00 60.78  ? 295 HIS   A N    1 
ATOM   2174 C CA   . HIS   B 1 80  ? -50.488 20.110  25.149 1.00 59.25  ? 295 HIS   A CA   1 
ATOM   2175 C C    . HIS   B 1 80  ? -49.086 19.657  25.547 1.00 57.88  ? 295 HIS   A C    1 
ATOM   2176 O O    . HIS   B 1 80  ? -48.281 20.504  25.959 1.00 58.10  ? 295 HIS   A O    1 
ATOM   2177 C CB   . HIS   B 1 80  ? -51.213 20.656  26.389 1.00 65.05  ? 295 HIS   A CB   1 
ATOM   2178 C CG   . HIS   B 1 80  ? -51.199 19.710  27.548 1.00 65.38  ? 295 HIS   A CG   1 
ATOM   2179 N ND1  . HIS   B 1 80  ? -50.147 19.641  28.438 1.00 63.27  ? 295 HIS   A ND1  1 
ATOM   2180 C CD2  . HIS   B 1 80  ? -52.096 18.783  27.955 1.00 69.65  ? 295 HIS   A CD2  1 
ATOM   2181 C CE1  . HIS   B 1 80  ? -50.395 18.712  29.343 1.00 63.58  ? 295 HIS   A CE1  1 
ATOM   2182 N NE2  . HIS   B 1 80  ? -51.572 18.177  29.074 1.00 73.21  ? 295 HIS   A NE2  1 
ATOM   2183 N N    . ALA   B 1 81  ? -48.764 18.369  25.435 1.00 60.35  ? 296 ALA   A N    1 
ATOM   2184 C CA   . ALA   B 1 81  ? -47.441 17.875  25.802 1.00 59.77  ? 296 ALA   A CA   1 
ATOM   2185 C C    . ALA   B 1 81  ? -46.431 17.886  24.649 1.00 58.82  ? 296 ALA   A C    1 
ATOM   2186 O O    . ALA   B 1 81  ? -45.264 17.541  24.881 1.00 54.79  ? 296 ALA   A O    1 
ATOM   2187 C CB   . ALA   B 1 81  ? -47.546 16.453  26.355 1.00 54.54  ? 296 ALA   A CB   1 
ATOM   2188 N N    . PHE   B 1 82  ? -46.836 18.265  23.433 1.00 54.52  ? 297 PHE   A N    1 
ATOM   2189 C CA   . PHE   B 1 82  ? -46.053 18.016  22.220 1.00 59.95  ? 297 PHE   A CA   1 
ATOM   2190 C C    . PHE   B 1 82  ? -45.423 19.300  21.700 1.00 59.11  ? 297 PHE   A C    1 
ATOM   2191 O O    . PHE   B 1 82  ? -46.128 20.240  21.323 1.00 60.86  ? 297 PHE   A O    1 
ATOM   2192 C CB   . PHE   B 1 82  ? -46.917 17.379  21.135 1.00 58.68  ? 297 PHE   A CB   1 
ATOM   2193 C CG   . PHE   B 1 82  ? -47.238 15.948  21.410 1.00 60.75  ? 297 PHE   A CG   1 
ATOM   2194 C CD1  . PHE   B 1 82  ? -48.158 15.610  22.384 1.00 60.16  ? 297 PHE   A CD1  1 
ATOM   2195 C CD2  . PHE   B 1 82  ? -46.584 14.937  20.734 1.00 58.04  ? 297 PHE   A CD2  1 
ATOM   2196 C CE1  . PHE   B 1 82  ? -48.433 14.290  22.648 1.00 62.24  ? 297 PHE   A CE1  1 
ATOM   2197 C CE2  . PHE   B 1 82  ? -46.862 13.622  20.997 1.00 61.76  ? 297 PHE   A CE2  1 
ATOM   2198 C CZ   . PHE   B 1 82  ? -47.785 13.298  21.953 1.00 62.29  ? 297 PHE   A CZ   1 
ATOM   2199 N N    . PHE   B 1 83  ? -44.098 19.322  21.657 1.00 51.69  ? 298 PHE   A N    1 
ATOM   2200 C CA   . PHE   B 1 83  ? -43.354 20.488  21.232 1.00 53.11  ? 298 PHE   A CA   1 
ATOM   2201 C C    . PHE   B 1 83  ? -42.428 20.155  20.070 1.00 53.96  ? 298 PHE   A C    1 
ATOM   2202 O O    . PHE   B 1 83  ? -41.884 19.045  19.983 1.00 52.09  ? 298 PHE   A O    1 
ATOM   2203 C CB   . PHE   B 1 83  ? -42.528 21.072  22.368 1.00 51.10  ? 298 PHE   A CB   1 
ATOM   2204 C CG   . PHE   B 1 83  ? -43.351 21.598  23.505 1.00 59.23  ? 298 PHE   A CG   1 
ATOM   2205 C CD1  . PHE   B 1 83  ? -44.274 20.790  24.174 1.00 57.38  ? 298 PHE   A CD1  1 
ATOM   2206 C CD2  . PHE   B 1 83  ? -43.296 22.955  23.822 1.00 59.00  ? 298 PHE   A CD2  1 
ATOM   2207 C CE1  . PHE   B 1 83  ? -45.044 21.303  25.194 1.00 58.27  ? 298 PHE   A CE1  1 
ATOM   2208 C CE2  . PHE   B 1 83  ? -44.076 23.478  24.842 1.00 58.66  ? 298 PHE   A CE2  1 
ATOM   2209 C CZ   . PHE   B 1 83  ? -44.952 22.649  25.524 1.00 59.88  ? 298 PHE   A CZ   1 
ATOM   2210 N N    . LEU   B 1 84  ? -42.250 21.137  19.183 1.00 57.45  ? 299 LEU   A N    1 
ATOM   2211 C CA   . LEU   B 1 84  ? -41.269 21.091  18.101 1.00 53.91  ? 299 LEU   A CA   1 
ATOM   2212 C C    . LEU   B 1 84  ? -40.173 22.101  18.407 1.00 53.45  ? 299 LEU   A C    1 
ATOM   2213 O O    . LEU   B 1 84  ? -40.459 23.279  18.634 1.00 58.95  ? 299 LEU   A O    1 
ATOM   2214 C CB   . LEU   B 1 84  ? -41.910 21.406  16.743 1.00 56.49  ? 299 LEU   A CB   1 
ATOM   2215 C CG   . LEU   B 1 84  ? -40.984 21.659  15.527 1.00 55.77  ? 299 LEU   A CG   1 
ATOM   2216 C CD1  . LEU   B 1 84  ? -40.335 20.403  15.042 1.00 50.49  ? 299 LEU   A CD1  1 
ATOM   2217 C CD2  . LEU   B 1 84  ? -41.716 22.323  14.381 1.00 57.52  ? 299 LEU   A CD2  1 
ATOM   2218 N N    . VAL   B 1 85  ? -38.927 21.642  18.410 1.00 52.74  ? 300 VAL   A N    1 
ATOM   2219 C CA   . VAL   B 1 85  ? -37.753 22.504  18.520 1.00 53.28  ? 300 VAL   A CA   1 
ATOM   2220 C C    . VAL   B 1 85  ? -37.046 22.492  17.173 1.00 52.80  ? 300 VAL   A C    1 
ATOM   2221 O O    . VAL   B 1 85  ? -36.703 21.422  16.665 1.00 48.53  ? 300 VAL   A O    1 
ATOM   2222 C CB   . VAL   B 1 85  ? -36.800 22.030  19.627 1.00 52.69  ? 300 VAL   A CB   1 
ATOM   2223 C CG1  . VAL   B 1 85  ? -35.507 22.819  19.579 1.00 51.05  ? 300 VAL   A CG1  1 
ATOM   2224 C CG2  . VAL   B 1 85  ? -37.470 22.159  21.008 1.00 54.38  ? 300 VAL   A CG2  1 
ATOM   2225 N N    . LYS   B 1 86  ? -36.826 23.667  16.592 1.00 50.85  ? 301 LYS   A N    1 
ATOM   2226 C CA   . LYS   B 1 86  ? -35.960 23.792  15.426 1.00 51.36  ? 301 LYS   A CA   1 
ATOM   2227 C C    . LYS   B 1 86  ? -34.588 24.232  15.923 1.00 51.60  ? 301 LYS   A C    1 
ATOM   2228 O O    . LYS   B 1 86  ? -34.484 25.212  16.670 1.00 53.42  ? 301 LYS   A O    1 
ATOM   2229 C CB   . LYS   B 1 86  ? -36.492 24.803  14.413 1.00 52.70  ? 301 LYS   A CB   1 
ATOM   2230 C CG   . LYS   B 1 86  ? -36.270 24.371  12.956 1.00 57.58  ? 301 LYS   A CG   1 
ATOM   2231 C CD   . LYS   B 1 86  ? -34.950 24.866  12.350 1.00 56.57  ? 301 LYS   A CD   1 
ATOM   2232 C CE   . LYS   B 1 86  ? -34.765 24.514  10.837 1.00 58.94  ? 301 LYS   A CE   1 
ATOM   2233 N NZ   . LYS   B 1 86  ? -35.683 25.238  9.852  1.00 60.97  ? 301 LYS   A NZ   1 
ATOM   2234 N N    . PHE   B 1 87  ? -33.552 23.481  15.558 1.00 52.81  ? 302 PHE   A N    1 
ATOM   2235 C CA   . PHE   B 1 87  ? -32.190 23.775  15.974 1.00 52.02  ? 302 PHE   A CA   1 
ATOM   2236 C C    . PHE   B 1 87  ? -31.389 24.306  14.787 1.00 55.40  ? 302 PHE   A C    1 
ATOM   2237 O O    . PHE   B 1 87  ? -31.495 23.784  13.668 1.00 53.05  ? 302 PHE   A O    1 
ATOM   2238 C CB   . PHE   B 1 87  ? -31.511 22.534  16.545 1.00 49.50  ? 302 PHE   A CB   1 
ATOM   2239 C CG   . PHE   B 1 87  ? -31.774 22.309  18.003 1.00 50.38  ? 302 PHE   A CG   1 
ATOM   2240 C CD1  . PHE   B 1 87  ? -31.784 23.364  18.897 1.00 55.69  ? 302 PHE   A CD1  1 
ATOM   2241 C CD2  . PHE   B 1 87  ? -31.992 21.038  18.489 1.00 51.29  ? 302 PHE   A CD2  1 
ATOM   2242 C CE1  . PHE   B 1 87  ? -32.032 23.155  20.255 1.00 52.39  ? 302 PHE   A CE1  1 
ATOM   2243 C CE2  . PHE   B 1 87  ? -32.239 20.822  19.830 1.00 52.07  ? 302 PHE   A CE2  1 
ATOM   2244 C CZ   . PHE   B 1 87  ? -32.255 21.880  20.713 1.00 52.02  ? 302 PHE   A CZ   1 
ATOM   2245 N N    . TRP   B 1 88  ? -30.616 25.373  15.022 1.00 51.37  ? 303 TRP   A N    1 
ATOM   2246 C CA   . TRP   B 1 88  ? -29.561 25.782  14.101 1.00 53.83  ? 303 TRP   A CA   1 
ATOM   2247 C C    . TRP   B 1 88  ? -28.238 25.455  14.784 1.00 53.58  ? 303 TRP   A C    1 
ATOM   2248 O O    . TRP   B 1 88  ? -27.793 26.191  15.665 1.00 52.29  ? 303 TRP   A O    1 
ATOM   2249 C CB   . TRP   B 1 88  ? -29.674 27.255  13.736 1.00 53.75  ? 303 TRP   A CB   1 
ATOM   2250 C CG   . TRP   B 1 88  ? -30.825 27.542  12.825 1.00 56.17  ? 303 TRP   A CG   1 
ATOM   2251 C CD1  . TRP   B 1 88  ? -30.795 27.604  11.473 1.00 54.22  ? 303 TRP   A CD1  1 
ATOM   2252 C CD2  . TRP   B 1 88  ? -32.191 27.800  13.209 1.00 62.30  ? 303 TRP   A CD2  1 
ATOM   2253 N NE1  . TRP   B 1 88  ? -32.046 27.894  10.978 1.00 57.57  ? 303 TRP   A NE1  1 
ATOM   2254 C CE2  . TRP   B 1 88  ? -32.924 28.015  12.022 1.00 61.36  ? 303 TRP   A CE2  1 
ATOM   2255 C CE3  . TRP   B 1 88  ? -32.860 27.892  14.445 1.00 59.52  ? 303 TRP   A CE3  1 
ATOM   2256 C CZ2  . TRP   B 1 88  ? -34.292 28.316  12.028 1.00 69.32  ? 303 TRP   A CZ2  1 
ATOM   2257 C CZ3  . TRP   B 1 88  ? -34.225 28.190  14.449 1.00 60.58  ? 303 TRP   A CZ3  1 
ATOM   2258 C CH2  . TRP   B 1 88  ? -34.923 28.398  13.251 1.00 66.38  ? 303 TRP   A CH2  1 
ATOM   2259 N N    . ALA   B 1 89  ? -27.615 24.348  14.371 1.00 52.21  ? 304 ALA   A N    1 
ATOM   2260 C CA   . ALA   B 1 89  ? -26.501 23.773  15.112 1.00 51.75  ? 304 ALA   A CA   1 
ATOM   2261 C C    . ALA   B 1 89  ? -25.183 24.429  14.742 1.00 56.77  ? 304 ALA   A C    1 
ATOM   2262 O O    . ALA   B 1 89  ? -24.942 24.769  13.578 1.00 60.76  ? 304 ALA   A O    1 
ATOM   2263 C CB   . ALA   B 1 89  ? -26.408 22.273  14.852 1.00 49.69  ? 304 ALA   A CB   1 
ATOM   2264 N N    . ASP   B 1 90  ? -24.314 24.579  15.733 1.00 55.49  ? 305 ASP   A N    1 
ATOM   2265 C CA   . ASP   B 1 90  ? -22.963 25.090  15.514 1.00 59.14  ? 305 ASP   A CA   1 
ATOM   2266 C C    . ASP   B 1 90  ? -22.041 23.889  15.315 1.00 62.61  ? 305 ASP   A C    1 
ATOM   2267 O O    . ASP   B 1 90  ? -21.681 23.209  16.279 1.00 64.19  ? 305 ASP   A O    1 
ATOM   2268 C CB   . ASP   B 1 90  ? -22.533 25.957  16.693 1.00 59.63  ? 305 ASP   A CB   1 
ATOM   2269 C CG   . ASP   B 1 90  ? -21.225 26.687  16.445 1.00 62.56  ? 305 ASP   A CG   1 
ATOM   2270 O OD1  . ASP   B 1 90  ? -20.452 26.232  15.584 1.00 66.73  ? 305 ASP   A OD1  1 
ATOM   2271 O OD2  . ASP   B 1 90  ? -20.961 27.703  17.121 1.00 63.59  ? 305 ASP   A OD2  1 
ATOM   2272 N N    . LEU   B 1 91  ? -21.663 23.612  14.061 1.00 60.10  ? 306 LEU   A N    1 
ATOM   2273 C CA   . LEU   B 1 91  ? -20.783 22.492  13.729 1.00 65.17  ? 306 LEU   A CA   1 
ATOM   2274 C C    . LEU   B 1 91  ? -19.331 22.925  13.541 1.00 71.34  ? 306 LEU   A C    1 
ATOM   2275 O O    . LEU   B 1 91  ? -18.572 22.256  12.830 1.00 72.07  ? 306 LEU   A O    1 
ATOM   2276 C CB   . LEU   B 1 91  ? -21.268 21.767  12.470 1.00 60.10  ? 306 LEU   A CB   1 
ATOM   2277 C CG   . LEU   B 1 91  ? -22.707 21.248  12.428 1.00 56.66  ? 306 LEU   A CG   1 
ATOM   2278 C CD1  . LEU   B 1 91  ? -22.854 20.220  11.329 1.00 58.60  ? 306 LEU   A CD1  1 
ATOM   2279 C CD2  . LEU   B 1 91  ? -23.132 20.649  13.761 1.00 58.81  ? 306 LEU   A CD2  1 
ATOM   2280 N N    . ASN   B 1 92  ? -18.931 24.032  14.156 1.00 81.38  ? 307 ASN   A N    1 
ATOM   2281 C CA   . ASN   B 1 92  ? -17.606 24.621  13.972 1.00 83.43  ? 307 ASN   A CA   1 
ATOM   2282 C C    . ASN   B 1 92  ? -16.835 24.484  15.283 1.00 82.96  ? 307 ASN   A C    1 
ATOM   2283 O O    . ASN   B 1 92  ? -17.037 25.275  16.211 1.00 81.32  ? 307 ASN   A O    1 
ATOM   2284 C CB   . ASN   B 1 92  ? -17.733 26.086  13.552 1.00 84.07  ? 307 ASN   A CB   1 
ATOM   2285 C CG   . ASN   B 1 92  ? -16.788 26.462  12.429 1.00 89.54  ? 307 ASN   A CG   1 
ATOM   2286 O OD1  . ASN   B 1 92  ? -16.873 25.921  11.326 1.00 93.55  ? 307 ASN   A OD1  1 
ATOM   2287 N ND2  . ASN   B 1 92  ? -15.888 27.408  12.701 1.00 91.59  ? 307 ASN   A ND2  1 
ATOM   2288 N N    . TRP   B 1 93  ? -15.956 23.486  15.362 1.00 73.83  ? 308 TRP   A N    1 
ATOM   2289 C CA   . TRP   B 1 93  ? -15.150 23.286  16.570 1.00 71.00  ? 308 TRP   A CA   1 
ATOM   2290 C C    . TRP   B 1 93  ? -13.736 22.773  16.272 1.00 70.09  ? 308 TRP   A C    1 
ATOM   2291 O O    . TRP   B 1 93  ? -13.411 22.448  15.120 1.00 73.28  ? 308 TRP   A O    1 
ATOM   2292 C CB   . TRP   B 1 93  ? -15.869 22.334  17.534 1.00 66.51  ? 308 TRP   A CB   1 
ATOM   2293 C CG   . TRP   B 1 93  ? -15.839 20.868  17.159 1.00 64.17  ? 308 TRP   A CG   1 
ATOM   2294 C CD1  . TRP   B 1 93  ? -14.973 19.921  17.637 1.00 62.58  ? 308 TRP   A CD1  1 
ATOM   2295 C CD2  . TRP   B 1 93  ? -16.738 20.174  16.269 1.00 64.18  ? 308 TRP   A CD2  1 
ATOM   2296 N NE1  . TRP   B 1 93  ? -15.261 18.692  17.084 1.00 65.51  ? 308 TRP   A NE1  1 
ATOM   2297 C CE2  . TRP   B 1 93  ? -16.337 18.818  16.242 1.00 64.20  ? 308 TRP   A CE2  1 
ATOM   2298 C CE3  . TRP   B 1 93  ? -17.830 20.571  15.482 1.00 65.77  ? 308 TRP   A CE3  1 
ATOM   2299 C CZ2  . TRP   B 1 93  ? -16.990 17.853  15.460 1.00 63.45  ? 308 TRP   A CZ2  1 
ATOM   2300 C CZ3  . TRP   B 1 93  ? -18.486 19.612  14.709 1.00 63.04  ? 308 TRP   A CZ3  1 
ATOM   2301 C CH2  . TRP   B 1 93  ? -18.059 18.268  14.703 1.00 63.71  ? 308 TRP   A CH2  1 
ATOM   2302 N N    . SER   B 1 108 ? -11.184 15.326  15.633 1.00 91.88  ? 323 SER   A N    1 
ATOM   2303 C CA   . SER   B 1 108 ? -11.303 13.948  16.100 1.00 93.62  ? 323 SER   A CA   1 
ATOM   2304 C C    . SER   B 1 108 ? -10.588 13.722  17.437 1.00 99.20  ? 323 SER   A C    1 
ATOM   2305 O O    . SER   B 1 108 ? -9.380  13.941  17.534 1.00 101.05 ? 323 SER   A O    1 
ATOM   2306 C CB   . SER   B 1 108 ? -10.753 12.998  15.055 1.00 89.63  ? 323 SER   A CB   1 
ATOM   2307 N N    . GLY   B 1 109 ? -11.325 13.283  18.464 1.00 90.34  ? 324 GLY   A N    1 
ATOM   2308 C CA   . GLY   B 1 109 ? -10.683 12.844  19.690 1.00 86.96  ? 324 GLY   A CA   1 
ATOM   2309 C C    . GLY   B 1 109 ? -11.440 12.995  21.003 1.00 92.11  ? 324 GLY   A C    1 
ATOM   2310 O O    . GLY   B 1 109 ? -11.111 12.321  21.986 1.00 90.21  ? 324 GLY   A O    1 
ATOM   2311 N N    . GLY   B 1 110 ? -12.449 13.871  21.052 1.00 86.79  ? 325 GLY   A N    1 
ATOM   2312 C CA   . GLY   B 1 110 ? -13.078 14.231  22.307 1.00 83.96  ? 325 GLY   A CA   1 
ATOM   2313 C C    . GLY   B 1 110 ? -14.295 13.386  22.654 1.00 76.08  ? 325 GLY   A C    1 
ATOM   2314 O O    . GLY   B 1 110 ? -14.669 12.451  21.950 1.00 75.66  ? 325 GLY   A O    1 
ATOM   2315 N N    . PHE   B 1 111 ? -14.923 13.748  23.772 1.00 77.54  ? 326 PHE   A N    1 
ATOM   2316 C CA   . PHE   B 1 111 ? -16.087 13.049  24.308 1.00 69.49  ? 326 PHE   A CA   1 
ATOM   2317 C C    . PHE   B 1 111 ? -17.355 13.783  23.876 1.00 68.12  ? 326 PHE   A C    1 
ATOM   2318 O O    . PHE   B 1 111 ? -17.509 14.977  24.156 1.00 69.34  ? 326 PHE   A O    1 
ATOM   2319 C CB   . PHE   B 1 111 ? -15.986 12.963  25.832 1.00 70.27  ? 326 PHE   A CB   1 
ATOM   2320 C CG   . PHE   B 1 111 ? -17.276 12.625  26.512 1.00 65.55  ? 326 PHE   A CG   1 
ATOM   2321 C CD1  . PHE   B 1 111 ? -17.648 11.309  26.703 1.00 63.67  ? 326 PHE   A CD1  1 
ATOM   2322 C CD2  . PHE   B 1 111 ? -18.124 13.630  26.957 1.00 67.08  ? 326 PHE   A CD2  1 
ATOM   2323 C CE1  . PHE   B 1 111 ? -18.853 10.996  27.330 1.00 64.96  ? 326 PHE   A CE1  1 
ATOM   2324 C CE2  . PHE   B 1 111 ? -19.328 13.326  27.584 1.00 67.46  ? 326 PHE   A CE2  1 
ATOM   2325 C CZ   . PHE   B 1 111 ? -19.692 12.006  27.774 1.00 63.29  ? 326 PHE   A CZ   1 
ATOM   2326 N N    . TYR   B 1 112 ? -18.248 13.075  23.178 1.00 61.65  ? 327 TYR   A N    1 
ATOM   2327 C CA   . TYR   B 1 112 ? -19.487 13.638  22.655 1.00 57.70  ? 327 TYR   A CA   1 
ATOM   2328 C C    . TYR   B 1 112 ? -20.628 13.194  23.553 1.00 61.58  ? 327 TYR   A C    1 
ATOM   2329 O O    . TYR   B 1 112 ? -20.857 11.988  23.720 1.00 62.10  ? 327 TYR   A O    1 
ATOM   2330 C CB   . TYR   B 1 112 ? -19.740 13.177  21.220 1.00 61.97  ? 327 TYR   A CB   1 
ATOM   2331 C CG   . TYR   B 1 112 ? -18.684 13.601  20.218 1.00 61.51  ? 327 TYR   A CG   1 
ATOM   2332 C CD1  . TYR   B 1 112 ? -17.428 13.020  20.229 1.00 64.33  ? 327 TYR   A CD1  1 
ATOM   2333 C CD2  . TYR   B 1 112 ? -18.930 14.596  19.282 1.00 60.57  ? 327 TYR   A CD2  1 
ATOM   2334 C CE1  . TYR   B 1 112 ? -16.454 13.397  19.324 1.00 65.83  ? 327 TYR   A CE1  1 
ATOM   2335 C CE2  . TYR   B 1 112 ? -17.953 14.971  18.355 1.00 58.02  ? 327 TYR   A CE2  1 
ATOM   2336 C CZ   . TYR   B 1 112 ? -16.720 14.377  18.404 1.00 62.72  ? 327 TYR   A CZ   1 
ATOM   2337 O OH   . TYR   B 1 112 ? -15.726 14.739  17.517 1.00 71.24  ? 327 TYR   A OH   1 
ATOM   2338 N N    . GLY   B 1 113 ? -21.337 14.163  24.132 1.00 62.14  ? 328 GLY   A N    1 
ATOM   2339 C CA   . GLY   B 1 113 ? -22.367 13.860  25.102 1.00 58.78  ? 328 GLY   A CA   1 
ATOM   2340 C C    . GLY   B 1 113 ? -23.565 14.765  24.911 1.00 55.42  ? 328 GLY   A C    1 
ATOM   2341 O O    . GLY   B 1 113 ? -23.502 15.779  24.210 1.00 52.69  ? 328 GLY   A O    1 
ATOM   2342 N N    . VAL   B 1 114 ? -24.673 14.354  25.526 1.00 52.97  ? 329 VAL   A N    1 
ATOM   2343 C CA   . VAL   B 1 114 ? -25.887 15.157  25.625 1.00 55.45  ? 329 VAL   A CA   1 
ATOM   2344 C C    . VAL   B 1 114 ? -26.232 15.281  27.101 1.00 55.48  ? 329 VAL   A C    1 
ATOM   2345 O O    . VAL   B 1 114 ? -26.070 14.318  27.862 1.00 57.99  ? 329 VAL   A O    1 
ATOM   2346 C CB   . VAL   B 1 114 ? -27.063 14.530  24.846 1.00 54.06  ? 329 VAL   A CB   1 
ATOM   2347 C CG1  . VAL   B 1 114 ? -26.784 14.537  23.345 1.00 55.74  ? 329 VAL   A CG1  1 
ATOM   2348 C CG2  . VAL   B 1 114 ? -27.287 13.106  25.312 1.00 59.94  ? 329 VAL   A CG2  1 
ATOM   2349 N N    . SER   B 1 115 ? -26.686 16.462  27.517 1.00 58.87  ? 330 SER   A N    1 
ATOM   2350 C CA   . SER   B 1 115 ? -27.139 16.678  28.891 1.00 56.39  ? 330 SER   A CA   1 
ATOM   2351 C C    . SER   B 1 115 ? -28.568 17.194  28.867 1.00 54.33  ? 330 SER   A C    1 
ATOM   2352 O O    . SER   B 1 115 ? -28.860 18.182  28.183 1.00 53.41  ? 330 SER   A O    1 
ATOM   2353 C CB   . SER   B 1 115 ? -26.231 17.653  29.639 1.00 56.55  ? 330 SER   A CB   1 
ATOM   2354 O OG   . SER   B 1 115 ? -25.088 17.000  30.167 1.00 57.87  ? 330 SER   A OG   1 
ATOM   2355 N N    . SER   B 1 116 ? -29.459 16.504  29.579 1.00 52.31  ? 331 SER   A N    1 
ATOM   2356 C CA   . SER   B 1 116 ? -30.839 16.939  29.770 1.00 54.32  ? 331 SER   A CA   1 
ATOM   2357 C C    . SER   B 1 116 ? -31.109 17.217  31.245 1.00 57.85  ? 331 SER   A C    1 
ATOM   2358 O O    . SER   B 1 116 ? -30.561 16.564  32.142 1.00 57.27  ? 331 SER   A O    1 
ATOM   2359 C CB   . SER   B 1 116 ? -31.842 15.892  29.270 1.00 55.58  ? 331 SER   A CB   1 
ATOM   2360 O OG   . SER   B 1 116 ? -32.094 16.014  27.878 1.00 58.72  ? 331 SER   A OG   1 
ATOM   2361 N N    . GLN   B 1 117 ? -31.974 18.182  31.504 1.00 55.33  ? 332 GLN   A N    1 
ATOM   2362 C CA   . GLN   B 1 117 ? -32.369 18.426  32.885 1.00 57.93  ? 332 GLN   A CA   1 
ATOM   2363 C C    . GLN   B 1 117 ? -33.811 18.881  32.894 1.00 57.44  ? 332 GLN   A C    1 
ATOM   2364 O O    . GLN   B 1 117 ? -34.138 19.902  32.282 1.00 56.68  ? 332 GLN   A O    1 
ATOM   2365 C CB   . GLN   B 1 117 ? -31.478 19.463  33.564 1.00 56.63  ? 332 GLN   A CB   1 
ATOM   2366 C CG   . GLN   B 1 117 ? -31.547 19.356  35.080 1.00 62.80  ? 332 GLN   A CG   1 
ATOM   2367 C CD   . GLN   B 1 117 ? -30.615 20.320  35.766 1.00 65.65  ? 332 GLN   A CD   1 
ATOM   2368 O OE1  . GLN   B 1 117 ? -29.404 20.330  35.497 1.00 68.64  ? 332 GLN   A OE1  1 
ATOM   2369 N NE2  . GLN   B 1 117 ? -31.155 21.114  36.684 1.00 66.06  ? 332 GLN   A NE2  1 
ATOM   2370 N N    . TYR   B 1 118 ? -34.661 18.117  33.569 1.00 58.29  ? 333 TYR   A N    1 
ATOM   2371 C CA   . TYR   B 1 118 ? -36.053 18.474  33.743 1.00 58.33  ? 333 TYR   A CA   1 
ATOM   2372 C C    . TYR   B 1 118 ? -36.314 18.763  35.210 1.00 62.19  ? 333 TYR   A C    1 
ATOM   2373 O O    . TYR   B 1 118 ? -35.534 18.392  36.095 1.00 64.10  ? 333 TYR   A O    1 
ATOM   2374 C CB   . TYR   B 1 118 ? -36.980 17.359  33.270 1.00 57.41  ? 333 TYR   A CB   1 
ATOM   2375 C CG   . TYR   B 1 118 ? -36.720 16.877  31.863 1.00 57.15  ? 333 TYR   A CG   1 
ATOM   2376 C CD1  . TYR   B 1 118 ? -35.729 15.943  31.595 1.00 55.15  ? 333 TYR   A CD1  1 
ATOM   2377 C CD2  . TYR   B 1 118 ? -37.497 17.338  30.802 1.00 56.16  ? 333 TYR   A CD2  1 
ATOM   2378 C CE1  . TYR   B 1 118 ? -35.507 15.487  30.283 1.00 58.84  ? 333 TYR   A CE1  1 
ATOM   2379 C CE2  . TYR   B 1 118 ? -37.289 16.896  29.506 1.00 55.01  ? 333 TYR   A CE2  1 
ATOM   2380 C CZ   . TYR   B 1 118 ? -36.298 15.977  29.243 1.00 57.58  ? 333 TYR   A CZ   1 
ATOM   2381 O OH   . TYR   B 1 118 ? -36.110 15.568  27.929 1.00 60.31  ? 333 TYR   A OH   1 
ATOM   2382 N N    . GLU   B 1 119 ? -37.432 19.426  35.470 1.00 61.20  ? 334 GLU   A N    1 
ATOM   2383 C CA   . GLU   B 1 119 ? -37.817 19.675  36.840 1.00 63.41  ? 334 GLU   A CA   1 
ATOM   2384 C C    . GLU   B 1 119 ? -39.328 19.548  36.950 1.00 64.38  ? 334 GLU   A C    1 
ATOM   2385 O O    . GLU   B 1 119 ? -40.041 19.522  35.939 1.00 58.79  ? 334 GLU   A O    1 
ATOM   2386 C CB   . GLU   B 1 119 ? -37.284 21.030  37.320 1.00 65.18  ? 334 GLU   A CB   1 
ATOM   2387 C CG   . GLU   B 1 119 ? -38.072 22.227  36.884 1.00 66.62  ? 334 GLU   A CG   1 
ATOM   2388 C CD   . GLU   B 1 119 ? -37.545 23.498  37.516 1.00 74.01  ? 334 GLU   A CD   1 
ATOM   2389 O OE1  . GLU   B 1 119 ? -36.774 23.402  38.507 1.00 76.55  ? 334 GLU   A OE1  1 
ATOM   2390 O OE2  . GLU   B 1 119 ? -37.886 24.593  37.015 1.00 78.19  ? 334 GLU   A OE2  1 
ATOM   2391 N N    . SER   B 1 120 ? -39.798 19.419  38.196 1.00 66.21  ? 335 SER   A N    1 
ATOM   2392 C CA   . SER   B 1 120 ? -41.209 19.171  38.464 1.00 64.09  ? 335 SER   A CA   1 
ATOM   2393 C C    . SER   B 1 120 ? -41.537 19.421  39.934 1.00 61.53  ? 335 SER   A C    1 
ATOM   2394 O O    . SER   B 1 120 ? -40.656 19.494  40.796 1.00 60.04  ? 335 SER   A O    1 
ATOM   2395 C CB   . SER   B 1 120 ? -41.599 17.743  38.082 1.00 60.33  ? 335 SER   A CB   1 
ATOM   2396 O OG   . SER   B 1 120 ? -42.972 17.529  38.351 1.00 63.97  ? 335 SER   A OG   1 
ATOM   2397 N N    . LEU   B 1 121 ? -42.833 19.535  40.203 1.00 58.20  ? 336 LEU   A N    1 
ATOM   2398 C CA   . LEU   B 1 121 ? -43.336 19.607  41.570 1.00 60.72  ? 336 LEU   A CA   1 
ATOM   2399 C C    . LEU   B 1 121 ? -43.707 18.242  42.147 1.00 61.74  ? 336 LEU   A C    1 
ATOM   2400 O O    . LEU   B 1 121 ? -43.900 18.141  43.358 1.00 61.48  ? 336 LEU   A O    1 
ATOM   2401 C CB   . LEU   B 1 121 ? -44.548 20.549  41.648 1.00 53.25  ? 336 LEU   A CB   1 
ATOM   2402 C CG   . LEU   B 1 121 ? -44.264 22.032  41.344 1.00 61.59  ? 336 LEU   A CG   1 
ATOM   2403 C CD1  . LEU   B 1 121 ? -45.549 22.803  41.080 1.00 56.34  ? 336 LEU   A CD1  1 
ATOM   2404 C CD2  . LEU   B 1 121 ? -43.460 22.722  42.464 1.00 57.77  ? 336 LEU   A CD2  1 
ATOM   2405 N N    . GLU   B 1 122 ? -43.808 17.199  41.325 1.00 60.39  ? 337 GLU   A N    1 
ATOM   2406 C CA   . GLU   B 1 122 ? -44.105 15.854  41.794 1.00 61.31  ? 337 GLU   A CA   1 
ATOM   2407 C C    . GLU   B 1 122 ? -42.834 15.023  41.798 1.00 62.59  ? 337 GLU   A C    1 
ATOM   2408 O O    . GLU   B 1 122 ? -41.925 15.246  40.995 1.00 60.65  ? 337 GLU   A O    1 
ATOM   2409 C CB   . GLU   B 1 122 ? -45.090 15.126  40.890 1.00 65.80  ? 337 GLU   A CB   1 
ATOM   2410 C CG   . GLU   B 1 122 ? -46.529 15.567  40.947 1.00 68.85  ? 337 GLU   A CG   1 
ATOM   2411 C CD   . GLU   B 1 122 ? -47.082 15.603  39.516 1.00 72.93  ? 337 GLU   A CD   1 
ATOM   2412 O OE1  . GLU   B 1 122 ? -47.353 14.510  38.957 1.00 69.74  ? 337 GLU   A OE1  1 
ATOM   2413 O OE2  . GLU   B 1 122 ? -47.177 16.709  38.924 1.00 72.94  ? 337 GLU   A OE2  1 
ATOM   2414 N N    . HIS   B 1 123 ? -42.799 14.038  42.691 1.00 61.68  ? 338 HIS   A N    1 
ATOM   2415 C CA   . HIS   B 1 123 ? -41.770 13.013  42.680 1.00 60.20  ? 338 HIS   A CA   1 
ATOM   2416 C C    . HIS   B 1 123 ? -42.214 11.900  41.750 1.00 59.79  ? 338 HIS   A C    1 
ATOM   2417 O O    . HIS   B 1 123 ? -43.267 11.292  41.972 1.00 57.26  ? 338 HIS   A O    1 
ATOM   2418 C CB   . HIS   B 1 123 ? -41.524 12.451  44.075 1.00 60.11  ? 338 HIS   A CB   1 
ATOM   2419 C CG   . HIS   B 1 123 ? -40.428 11.436  44.113 1.00 61.48  ? 338 HIS   A CG   1 
ATOM   2420 N ND1  . HIS   B 1 123 ? -39.166 11.720  44.595 1.00 62.11  ? 338 HIS   A ND1  1 
ATOM   2421 C CD2  . HIS   B 1 123 ? -40.392 10.149  43.694 1.00 59.96  ? 338 HIS   A CD2  1 
ATOM   2422 C CE1  . HIS   B 1 123 ? -38.408 10.641  44.492 1.00 61.72  ? 338 HIS   A CE1  1 
ATOM   2423 N NE2  . HIS   B 1 123 ? -39.129 9.674   43.951 1.00 61.28  ? 338 HIS   A NE2  1 
ATOM   2424 N N    . MET   B 1 124 ? -41.393 11.626  40.733 1.00 61.16  ? 339 MET   A N    1 
ATOM   2425 C CA   . MET   B 1 124 ? -41.656 10.645  39.689 1.00 57.14  ? 339 MET   A CA   1 
ATOM   2426 C C    . MET   B 1 124 ? -40.355 9.940   39.349 1.00 57.52  ? 339 MET   A C    1 
ATOM   2427 O O    . MET   B 1 124 ? -39.270 10.359  39.754 1.00 59.77  ? 339 MET   A O    1 
ATOM   2428 C CB   . MET   B 1 124 ? -42.182 11.323  38.418 1.00 62.68  ? 339 MET   A CB   1 
ATOM   2429 C CG   . MET   B 1 124 ? -43.385 12.202  38.623 1.00 60.63  ? 339 MET   A CG   1 
ATOM   2430 S SD   . MET   B 1 124 ? -43.753 13.056  37.100 1.00 56.94  ? 339 MET   A SD   1 
ATOM   2431 C CE   . MET   B 1 124 ? -45.533 12.942  37.062 1.00 60.53  ? 339 MET   A CE   1 
ATOM   2432 N N    . THR   B 1 125 ? -40.457 8.882   38.556 1.00 58.20  ? 340 THR   A N    1 
ATOM   2433 C CA   . THR   B 1 125 ? -39.308 8.348   37.836 1.00 60.69  ? 340 THR   A CA   1 
ATOM   2434 C C    . THR   B 1 125 ? -39.613 8.472   36.349 1.00 59.28  ? 340 THR   A C    1 
ATOM   2435 O O    . THR   B 1 125 ? -40.660 8.001   35.885 1.00 58.23  ? 340 THR   A O    1 
ATOM   2436 C CB   . THR   B 1 125 ? -39.002 6.899   38.229 1.00 63.43  ? 340 THR   A CB   1 
ATOM   2437 O OG1  . THR   B 1 125 ? -40.226 6.199   38.481 1.00 67.97  ? 340 THR   A OG1  1 
ATOM   2438 C CG2  . THR   B 1 125 ? -38.138 6.854   39.492 1.00 64.56  ? 340 THR   A CG2  1 
ATOM   2439 N N    . LEU   B 1 126 ? -38.731 9.145   35.616 1.00 61.99  ? 341 LEU   A N    1 
ATOM   2440 C CA   . LEU   B 1 126 ? -38.947 9.375   34.191 1.00 64.33  ? 341 LEU   A CA   1 
ATOM   2441 C C    . LEU   B 1 126 ? -38.255 8.294   33.358 1.00 64.67  ? 341 LEU   A C    1 
ATOM   2442 O O    . LEU   B 1 126 ? -37.107 7.922   33.627 1.00 65.46  ? 341 LEU   A O    1 
ATOM   2443 C CB   . LEU   B 1 126 ? -38.441 10.764  33.784 1.00 61.29  ? 341 LEU   A CB   1 
ATOM   2444 C CG   . LEU   B 1 126 ? -38.855 12.012  34.573 1.00 55.97  ? 341 LEU   A CG   1 
ATOM   2445 C CD1  . LEU   B 1 126 ? -37.998 13.185  34.140 1.00 56.42  ? 341 LEU   A CD1  1 
ATOM   2446 C CD2  . LEU   B 1 126 ? -40.342 12.347  34.411 1.00 53.90  ? 341 LEU   A CD2  1 
ATOM   2447 N N    . THR   B 1 127 ? -38.961 7.769   32.365 1.00 59.92  ? 342 THR   A N    1 
ATOM   2448 C CA   . THR   B 1 127 ? -38.321 7.009   31.294 1.00 62.29  ? 342 THR   A CA   1 
ATOM   2449 C C    . THR   B 1 127 ? -38.235 7.895   30.064 1.00 56.86  ? 342 THR   A C    1 
ATOM   2450 O O    . THR   B 1 127 ? -39.269 8.323   29.536 1.00 55.73  ? 342 THR   A O    1 
ATOM   2451 C CB   . THR   B 1 127 ? -39.065 5.728   30.946 1.00 59.45  ? 342 THR   A CB   1 
ATOM   2452 O OG1  . THR   B 1 127 ? -38.458 5.177   29.775 1.00 60.70  ? 342 THR   A OG1  1 
ATOM   2453 C CG2  . THR   B 1 127 ? -40.476 6.036   30.616 1.00 59.53  ? 342 THR   A CG2  1 
ATOM   2454 N N    . CYS   B 1 128 ? -37.011 8.190   29.631 1.00 57.95  ? 343 CYS   A N    1 
ATOM   2455 C CA   . CYS   B 1 128 ? -36.770 9.063   28.486 1.00 59.20  ? 343 CYS   A CA   1 
ATOM   2456 C C    . CYS   B 1 128 ? -36.272 8.252   27.297 1.00 55.98  ? 343 CYS   A C    1 
ATOM   2457 O O    . CYS   B 1 128 ? -35.357 7.432   27.424 1.00 57.47  ? 343 CYS   A O    1 
ATOM   2458 C CB   . CYS   B 1 128 ? -35.790 10.177  28.839 1.00 57.57  ? 343 CYS   A CB   1 
ATOM   2459 S SG   . CYS   B 1 128 ? -35.926 10.780  30.570 1.00 66.90  ? 343 CYS   A SG   1 
ATOM   2460 N N    . SER   B 1 129 ? -36.902 8.455   26.155 1.00 54.15  ? 344 SER   A N    1 
ATOM   2461 C CA   . SER   B 1 129 ? -36.591 7.701   24.953 1.00 54.38  ? 344 SER   A CA   1 
ATOM   2462 C C    . SER   B 1 129 ? -36.219 8.666   23.834 1.00 53.76  ? 344 SER   A C    1 
ATOM   2463 O O    . SER   B 1 129 ? -36.916 9.662   23.604 1.00 52.79  ? 344 SER   A O    1 
ATOM   2464 C CB   . SER   B 1 129 ? -37.777 6.835   24.549 1.00 53.30  ? 344 SER   A CB   1 
ATOM   2465 O OG   . SER   B 1 129 ? -37.821 6.699   23.144 1.00 64.23  ? 344 SER   A OG   1 
ATOM   2466 N N    . SER   B 1 130 ? -35.106 8.406   23.169 1.00 53.06  ? 345 SER   A N    1 
ATOM   2467 C CA   . SER   B 1 130 ? -34.711 9.200   22.019 1.00 52.79  ? 345 SER   A CA   1 
ATOM   2468 C C    . SER   B 1 130 ? -34.748 8.311   20.795 1.00 55.80  ? 345 SER   A C    1 
ATOM   2469 O O    . SER   B 1 130 ? -34.197 7.201   20.809 1.00 56.37  ? 345 SER   A O    1 
ATOM   2470 C CB   . SER   B 1 130 ? -33.318 9.798   22.186 1.00 54.81  ? 345 SER   A CB   1 
ATOM   2471 O OG   . SER   B 1 130 ? -33.065 10.092  23.538 1.00 59.30  ? 345 SER   A OG   1 
ATOM   2472 N N    . LYS   B 1 131 ? -35.427 8.781   19.759 1.00 54.15  ? 346 LYS   A N    1 
ATOM   2473 C CA   . LYS   B 1 131 ? -35.474 8.097   18.478 1.00 53.68  ? 346 LYS   A CA   1 
ATOM   2474 C C    . LYS   B 1 131 ? -34.798 9.011   17.475 1.00 53.26  ? 346 LYS   A C    1 
ATOM   2475 O O    . LYS   B 1 131 ? -35.335 10.071  17.137 1.00 51.32  ? 346 LYS   A O    1 
ATOM   2476 C CB   . LYS   B 1 131 ? -36.908 7.783   18.059 1.00 57.41  ? 346 LYS   A CB   1 
ATOM   2477 C CG   . LYS   B 1 131 ? -37.609 6.734   18.908 1.00 61.52  ? 346 LYS   A CG   1 
ATOM   2478 C CD   . LYS   B 1 131 ? -39.124 6.780   18.686 1.00 68.58  ? 346 LYS   A CD   1 
ATOM   2479 C CE   . LYS   B 1 131 ? -39.887 6.146   19.848 1.00 76.03  ? 346 LYS   A CE   1 
ATOM   2480 N NZ   . LYS   B 1 131 ? -41.366 6.221   19.659 1.00 79.92  ? 346 LYS   A NZ   1 
ATOM   2481 N N    . VAL   B 1 132 ? -33.609 8.637   17.037 1.00 54.50  ? 347 VAL   A N    1 
ATOM   2482 C CA   . VAL   B 1 132 ? -32.982 9.334   15.927 1.00 53.24  ? 347 VAL   A CA   1 
ATOM   2483 C C    . VAL   B 1 132 ? -33.516 8.732   14.637 1.00 55.67  ? 347 VAL   A C    1 
ATOM   2484 O O    . VAL   B 1 132 ? -33.564 7.503   14.489 1.00 57.00  ? 347 VAL   A O    1 
ATOM   2485 C CB   . VAL   B 1 132 ? -31.457 9.233   16.021 1.00 55.46  ? 347 VAL   A CB   1 
ATOM   2486 C CG1  . VAL   B 1 132 ? -30.800 10.054  14.915 1.00 53.98  ? 347 VAL   A CG1  1 
ATOM   2487 C CG2  . VAL   B 1 132 ? -31.011 9.715   17.407 1.00 54.25  ? 347 VAL   A CG2  1 
ATOM   2488 N N    . CYS   B 1 133 ? -33.981 9.584   13.728 1.00 53.93  ? 348 CYS   A N    1 
ATOM   2489 C CA   . CYS   B 1 133 ? -34.477 9.136   12.435 1.00 57.78  ? 348 CYS   A CA   1 
ATOM   2490 C C    . CYS   B 1 133 ? -33.679 9.763   11.287 1.00 57.49  ? 348 CYS   A C    1 
ATOM   2491 O O    . CYS   B 1 133 ? -33.283 10.928  11.337 1.00 50.84  ? 348 CYS   A O    1 
ATOM   2492 C CB   . CYS   B 1 133 ? -35.965 9.471   12.253 1.00 60.87  ? 348 CYS   A CB   1 
ATOM   2493 S SG   . CYS   B 1 133 ? -37.110 8.893   13.509 1.00 68.00  ? 348 CYS   A SG   1 
ATOM   2494 N N    . SER   B 1 134 ? -33.444 8.984   10.246 1.00 60.71  ? 349 SER   A N    1 
ATOM   2495 C CA   . SER   B 1 134 ? -32.986 9.536   8.986  1.00 57.77  ? 349 SER   A CA   1 
ATOM   2496 C C    . SER   B 1 134 ? -33.912 8.999   7.914  1.00 59.02  ? 349 SER   A C    1 
ATOM   2497 O O    . SER   B 1 134 ? -34.269 7.820   7.942  1.00 57.48  ? 349 SER   A O    1 
ATOM   2498 C CB   . SER   B 1 134 ? -31.525 9.198   8.716  1.00 56.19  ? 349 SER   A CB   1 
ATOM   2499 O OG   . SER   B 1 134 ? -31.309 7.824   8.854  1.00 61.81  ? 349 SER   A OG   1 
ATOM   2500 N N    . PHE   B 1 135 ? -34.366 9.887   7.030  1.00 59.68  ? 350 PHE   A N    1 
ATOM   2501 C CA   . PHE   B 1 135 ? -35.375 9.548   6.031  1.00 62.35  ? 350 PHE   A CA   1 
ATOM   2502 C C    . PHE   B 1 135 ? -36.583 8.863   6.689  1.00 63.68  ? 350 PHE   A C    1 
ATOM   2503 O O    . PHE   B 1 135 ? -37.001 7.765   6.319  1.00 69.19  ? 350 PHE   A O    1 
ATOM   2504 C CB   . PHE   B 1 135 ? -34.741 8.702   4.907  1.00 55.36  ? 350 PHE   A CB   1 
ATOM   2505 C CG   . PHE   B 1 135 ? -33.500 9.347   4.302  1.00 57.36  ? 350 PHE   A CG   1 
ATOM   2506 C CD1  . PHE   B 1 135 ? -33.600 10.234  3.226  1.00 57.71  ? 350 PHE   A CD1  1 
ATOM   2507 C CD2  . PHE   B 1 135 ? -32.236 9.116   4.844  1.00 60.12  ? 350 PHE   A CD2  1 
ATOM   2508 C CE1  . PHE   B 1 135 ? -32.447 10.857  2.669  1.00 54.06  ? 350 PHE   A CE1  1 
ATOM   2509 C CE2  . PHE   B 1 135 ? -31.085 9.740   4.313  1.00 57.62  ? 350 PHE   A CE2  1 
ATOM   2510 C CZ   . PHE   B 1 135 ? -31.194 10.612  3.219  1.00 53.23  ? 350 PHE   A CZ   1 
ATOM   2511 N N    . GLY   B 1 136 ? -37.142 9.526   7.697  1.00 71.76  ? 351 GLY   A N    1 
ATOM   2512 C CA   . GLY   B 1 136 ? -38.335 9.048   8.382  1.00 77.72  ? 351 GLY   A CA   1 
ATOM   2513 C C    . GLY   B 1 136 ? -38.284 7.625   8.916  1.00 80.41  ? 351 GLY   A C    1 
ATOM   2514 O O    . GLY   B 1 136 ? -39.322 7.042   9.255  1.00 84.39  ? 351 GLY   A O    1 
ATOM   2515 N N    . LYS   B 1 137 ? -37.086 7.051   8.988  1.00 72.31  ? 352 LYS   A N    1 
ATOM   2516 C CA   . LYS   B 1 137 ? -36.882 5.698   9.481  1.00 67.95  ? 352 LYS   A CA   1 
ATOM   2517 C C    . LYS   B 1 137 ? -35.955 5.758   10.684 1.00 64.08  ? 352 LYS   A C    1 
ATOM   2518 O O    . LYS   B 1 137 ? -34.920 6.432   10.640 1.00 63.03  ? 352 LYS   A O    1 
ATOM   2519 C CB   . LYS   B 1 137 ? -36.310 4.799   8.383  1.00 66.44  ? 352 LYS   A CB   1 
ATOM   2520 C CG   . LYS   B 1 137 ? -36.706 3.342   8.527  1.00 70.14  ? 352 LYS   A CG   1 
ATOM   2521 C CD   . LYS   B 1 137 ? -38.203 3.126   8.312  1.00 76.65  ? 352 LYS   A CD   1 
ATOM   2522 C CE   . LYS   B 1 137 ? -38.765 2.040   9.268  1.00 79.46  ? 352 LYS   A CE   1 
ATOM   2523 N NZ   . LYS   B 1 137 ? -39.110 2.608   10.630 1.00 75.34  ? 352 LYS   A NZ   1 
ATOM   2524 N N    . GLN   B 1 138 ? -36.348 5.081   11.762 1.00 65.37  ? 353 GLN   A N    1 
ATOM   2525 C CA   . GLN   B 1 138 ? -35.611 5.125   13.024 1.00 62.37  ? 353 GLN   A CA   1 
ATOM   2526 C C    . GLN   B 1 138 ? -34.329 4.306   12.922 1.00 57.61  ? 353 GLN   A C    1 
ATOM   2527 O O    . GLN   B 1 138 ? -34.378 3.097   12.692 1.00 59.81  ? 353 GLN   A O    1 
ATOM   2528 C CB   . GLN   B 1 138 ? -36.495 4.615   14.174 1.00 62.66  ? 353 GLN   A CB   1 
ATOM   2529 C CG   . GLN   B 1 138 ? -35.786 4.553   15.536 1.00 60.93  ? 353 GLN   A CG   1 
ATOM   2530 C CD   . GLN   B 1 138 ? -36.357 3.476   16.490 1.00 68.15  ? 353 GLN   A CD   1 
ATOM   2531 O OE1  . GLN   B 1 138 ? -37.385 3.704   17.144 1.00 65.51  ? 353 GLN   A OE1  1 
ATOM   2532 N NE2  . GLN   B 1 138 ? -35.716 2.286   16.532 1.00 63.48  ? 353 GLN   A NE2  1 
ATOM   2533 N N    . VAL   B 1 139 ? -33.183 4.953   13.125 1.00 58.66  ? 354 VAL   A N    1 
ATOM   2534 C CA   . VAL   B 1 139 ? -31.913 4.238   13.122 1.00 61.29  ? 354 VAL   A CA   1 
ATOM   2535 C C    . VAL   B 1 139 ? -31.326 4.010   14.513 1.00 61.84  ? 354 VAL   A C    1 
ATOM   2536 O O    . VAL   B 1 139 ? -30.495 3.101   14.672 1.00 59.98  ? 354 VAL   A O    1 
ATOM   2537 C CB   . VAL   B 1 139 ? -30.885 4.949   12.220 1.00 58.89  ? 354 VAL   A CB   1 
ATOM   2538 C CG1  . VAL   B 1 139 ? -31.278 4.748   10.771 1.00 60.64  ? 354 VAL   A CG1  1 
ATOM   2539 C CG2  . VAL   B 1 139 ? -30.813 6.426   12.543 1.00 56.23  ? 354 VAL   A CG2  1 
ATOM   2540 N N    . VAL   B 1 140 ? -31.737 4.789   15.518 1.00 56.81  ? 355 VAL   A N    1 
ATOM   2541 C CA   . VAL   B 1 140 ? -31.181 4.736   16.865 1.00 57.35  ? 355 VAL   A CA   1 
ATOM   2542 C C    . VAL   B 1 140 ? -32.296 4.996   17.869 1.00 60.80  ? 355 VAL   A C    1 
ATOM   2543 O O    . VAL   B 1 140 ? -32.941 6.051   17.818 1.00 57.36  ? 355 VAL   A O    1 
ATOM   2544 C CB   . VAL   B 1 140 ? -30.069 5.784   17.093 1.00 60.05  ? 355 VAL   A CB   1 
ATOM   2545 C CG1  . VAL   B 1 140 ? -29.416 5.563   18.474 1.00 59.47  ? 355 VAL   A CG1  1 
ATOM   2546 C CG2  . VAL   B 1 140 ? -29.027 5.760   15.974 1.00 61.03  ? 355 VAL   A CG2  1 
ATOM   2547 N N    . GLU   B 1 141 ? -32.500 4.066   18.808 1.00 58.23  ? 356 GLU   A N    1 
ATOM   2548 C CA   . GLU   B 1 141 ? -33.349 4.336   19.958 1.00 57.82  ? 356 GLU   A CA   1 
ATOM   2549 C C    . GLU   B 1 141 ? -32.555 4.178   21.248 1.00 57.73  ? 356 GLU   A C    1 
ATOM   2550 O O    . GLU   B 1 141 ? -31.933 3.133   21.485 1.00 56.52  ? 356 GLU   A O    1 
ATOM   2551 C CB   . GLU   B 1 141 ? -34.594 3.454   20.008 1.00 59.87  ? 356 GLU   A CB   1 
ATOM   2552 C CG   . GLU   B 1 141 ? -35.469 3.980   21.153 1.00 62.47  ? 356 GLU   A CG   1 
ATOM   2553 C CD   . GLU   B 1 141 ? -36.823 3.320   21.314 1.00 65.73  ? 356 GLU   A CD   1 
ATOM   2554 O OE1  . GLU   B 1 141 ? -36.971 2.102   21.038 1.00 68.76  ? 356 GLU   A OE1  1 
ATOM   2555 O OE2  . GLU   B 1 141 ? -37.748 4.061   21.731 1.00 64.50  ? 356 GLU   A OE2  1 
ATOM   2556 N N    . LYS   B 1 142 ? -32.596 5.218   22.074 1.00 54.30  ? 357 LYS   A N    1 
ATOM   2557 C CA   . LYS   B 1 142 ? -31.944 5.274   23.369 1.00 56.73  ? 357 LYS   A CA   1 
ATOM   2558 C C    . LYS   B 1 142 ? -33.021 5.386   24.442 1.00 56.16  ? 357 LYS   A C    1 
ATOM   2559 O O    . LYS   B 1 142 ? -33.894 6.253   24.354 1.00 54.07  ? 357 LYS   A O    1 
ATOM   2560 C CB   . LYS   B 1 142 ? -31.026 6.491   23.428 1.00 59.06  ? 357 LYS   A CB   1 
ATOM   2561 C CG   . LYS   B 1 142 ? -29.611 6.298   23.912 1.00 62.72  ? 357 LYS   A CG   1 
ATOM   2562 C CD   . LYS   B 1 142 ? -28.917 7.664   23.792 1.00 66.04  ? 357 LYS   A CD   1 
ATOM   2563 C CE   . LYS   B 1 142 ? -27.561 7.727   24.488 1.00 67.91  ? 357 LYS   A CE   1 
ATOM   2564 N NZ   . LYS   B 1 142 ? -27.182 9.160   24.678 1.00 67.38  ? 357 LYS   A NZ   1 
ATOM   2565 N N    . VAL   B 1 143 ? -32.962 4.531   25.454 1.00 55.85  ? 358 VAL   A N    1 
ATOM   2566 C CA   . VAL   B 1 143 ? -33.914 4.599   26.560 1.00 61.75  ? 358 VAL   A CA   1 
ATOM   2567 C C    . VAL   B 1 143 ? -33.148 4.627   27.874 1.00 64.87  ? 358 VAL   A C    1 
ATOM   2568 O O    . VAL   B 1 143 ? -32.353 3.719   28.146 1.00 62.55  ? 358 VAL   A O    1 
ATOM   2569 C CB   . VAL   B 1 143 ? -34.902 3.421   26.556 1.00 58.81  ? 358 VAL   A CB   1 
ATOM   2570 C CG1  . VAL   B 1 143 ? -35.936 3.617   27.661 1.00 56.73  ? 358 VAL   A CG1  1 
ATOM   2571 C CG2  . VAL   B 1 143 ? -35.567 3.304   25.193 1.00 60.94  ? 358 VAL   A CG2  1 
ATOM   2572 N N    . GLU   B 1 144 ? -33.386 5.654   28.694 1.00 64.65  ? 359 GLU   A N    1 
ATOM   2573 C CA   . GLU   B 1 144 ? -32.913 5.589   30.073 1.00 66.86  ? 359 GLU   A CA   1 
ATOM   2574 C C    . GLU   B 1 144 ? -33.971 6.127   31.023 1.00 67.49  ? 359 GLU   A C    1 
ATOM   2575 O O    . GLU   B 1 144 ? -34.959 6.755   30.621 1.00 66.75  ? 359 GLU   A O    1 
ATOM   2576 C CB   . GLU   B 1 144 ? -31.600 6.346   30.301 1.00 67.75  ? 359 GLU   A CB   1 
ATOM   2577 C CG   . GLU   B 1 144 ? -31.451 7.587   29.487 1.00 72.30  ? 359 GLU   A CG   1 
ATOM   2578 C CD   . GLU   B 1 144 ? -29.995 7.899   29.199 1.00 82.13  ? 359 GLU   A CD   1 
ATOM   2579 O OE1  . GLU   B 1 144 ? -29.283 7.007   28.679 1.00 82.67  ? 359 GLU   A OE1  1 
ATOM   2580 O OE2  . GLU   B 1 144 ? -29.561 9.034   29.519 1.00 87.18  ? 359 GLU   A OE2  1 
ATOM   2581 N N    . THR   B 1 145 ? -33.734 5.868   32.306 1.00 68.12  ? 360 THR   A N    1 
ATOM   2582 C CA   . THR   B 1 145 ? -34.626 6.266   33.377 1.00 66.88  ? 360 THR   A CA   1 
ATOM   2583 C C    . THR   B 1 145 ? -33.854 7.124   34.376 1.00 67.26  ? 360 THR   A C    1 
ATOM   2584 O O    . THR   B 1 145 ? -32.651 6.926   34.594 1.00 67.58  ? 360 THR   A O    1 
ATOM   2585 C CB   . THR   B 1 145 ? -35.199 5.036   34.061 1.00 67.51  ? 360 THR   A CB   1 
ATOM   2586 O OG1  . THR   B 1 145 ? -34.204 4.512   34.936 1.00 70.73  ? 360 THR   A OG1  1 
ATOM   2587 C CG2  . THR   B 1 145 ? -35.522 3.956   33.009 1.00 62.98  ? 360 THR   A CG2  1 
ATOM   2588 N N    . GLU   B 1 146 ? -34.548 8.095   34.970 1.00 67.87  ? 361 GLU   A N    1 
ATOM   2589 C CA   . GLU   B 1 146 ? -33.963 8.977   35.972 1.00 68.51  ? 361 GLU   A CA   1 
ATOM   2590 C C    . GLU   B 1 146 ? -34.976 9.142   37.091 1.00 68.45  ? 361 GLU   A C    1 
ATOM   2591 O O    . GLU   B 1 146 ? -36.152 9.432   36.834 1.00 62.58  ? 361 GLU   A O    1 
ATOM   2592 C CB   . GLU   B 1 146 ? -33.572 10.344  35.372 1.00 64.73  ? 361 GLU   A CB   1 
ATOM   2593 C CG   . GLU   B 1 146 ? -32.932 11.344  36.353 1.00 62.31  ? 361 GLU   A CG   1 
ATOM   2594 C CD   . GLU   B 1 146 ? -31.523 10.944  36.813 1.00 67.71  ? 361 GLU   A CD   1 
ATOM   2595 O OE1  . GLU   B 1 146 ? -30.957 9.964   36.272 1.00 71.83  ? 361 GLU   A OE1  1 
ATOM   2596 O OE2  . GLU   B 1 146 ? -30.974 11.610  37.726 1.00 67.30  ? 361 GLU   A OE2  1 
ATOM   2597 N N    . ARG   B 1 147 ? -34.528 8.922   38.325 1.00 75.62  ? 362 ARG   A N    1 
ATOM   2598 C CA   . ARG   B 1 147 ? -35.377 9.111   39.498 1.00 76.59  ? 362 ARG   A CA   1 
ATOM   2599 C C    . ARG   B 1 147 ? -35.339 10.571  39.937 1.00 74.19  ? 362 ARG   A C    1 
ATOM   2600 O O    . ARG   B 1 147 ? -34.321 11.255  39.776 1.00 74.25  ? 362 ARG   A O    1 
ATOM   2601 C CB   . ARG   B 1 147 ? -34.938 8.179   40.634 1.00 80.38  ? 362 ARG   A CB   1 
ATOM   2602 C CG   . ARG   B 1 147 ? -34.276 6.908   40.114 1.00 86.91  ? 362 ARG   A CG   1 
ATOM   2603 C CD   . ARG   B 1 147 ? -33.939 5.894   41.190 1.00 93.56  ? 362 ARG   A CD   1 
ATOM   2604 N NE   . ARG   B 1 147 ? -33.155 6.460   42.279 1.00 99.45  ? 362 ARG   A NE   1 
ATOM   2605 C CZ   . ARG   B 1 147 ? -33.330 6.156   43.558 1.00 101.32 ? 362 ARG   A CZ   1 
ATOM   2606 N NH1  . ARG   B 1 147 ? -34.267 5.304   43.946 1.00 102.21 ? 362 ARG   A NH1  1 
ATOM   2607 N NH2  . ARG   B 1 147 ? -32.545 6.718   44.473 1.00 104.59 ? 362 ARG   A NH2  1 
ATOM   2608 N N    . ALA   B 1 148 ? -36.467 11.060  40.447 1.00 71.78  ? 363 ALA   A N    1 
ATOM   2609 C CA   . ALA   B 1 148 ? -36.501 12.429  40.936 1.00 69.23  ? 363 ALA   A CA   1 
ATOM   2610 C C    . ALA   B 1 148 ? -35.487 12.606  42.057 1.00 68.98  ? 363 ALA   A C    1 
ATOM   2611 O O    . ALA   B 1 148 ? -35.161 11.666  42.782 1.00 68.55  ? 363 ALA   A O    1 
ATOM   2612 C CB   . ALA   B 1 148 ? -37.896 12.794  41.430 1.00 66.67  ? 363 ALA   A CB   1 
ATOM   2613 N N    . GLN   B 1 149 ? -34.961 13.821  42.170 1.00 67.20  ? 364 GLN   A N    1 
ATOM   2614 C CA   . GLN   B 1 149 ? -34.062 14.200  43.250 1.00 68.28  ? 364 GLN   A CA   1 
ATOM   2615 C C    . GLN   B 1 149 ? -34.543 15.522  43.836 1.00 66.87  ? 364 GLN   A C    1 
ATOM   2616 O O    . GLN   B 1 149 ? -34.845 16.460  43.093 1.00 65.60  ? 364 GLN   A O    1 
ATOM   2617 C CB   . GLN   B 1 149 ? -32.611 14.318  42.758 1.00 70.94  ? 364 GLN   A CB   1 
ATOM   2618 C CG   . GLN   B 1 149 ? -31.681 14.916  43.805 1.00 79.14  ? 364 GLN   A CG   1 
ATOM   2619 C CD   . GLN   B 1 149 ? -31.065 13.852  44.704 1.00 85.80  ? 364 GLN   A CD   1 
ATOM   2620 O OE1  . GLN   B 1 149 ? -30.544 14.144  45.796 1.00 86.36  ? 364 GLN   A OE1  1 
ATOM   2621 N NE2  . GLN   B 1 149 ? -31.085 12.608  44.227 1.00 85.86  ? 364 GLN   A NE2  1 
ATOM   2622 N N    . LEU   B 1 150 ? -34.626 15.597  45.160 1.00 72.20  ? 365 LEU   A N    1 
ATOM   2623 C CA   . LEU   B 1 150 ? -35.119 16.806  45.808 1.00 70.47  ? 365 LEU   A CA   1 
ATOM   2624 C C    . LEU   B 1 150 ? -34.039 17.879  45.793 1.00 74.69  ? 365 LEU   A C    1 
ATOM   2625 O O    . LEU   B 1 150 ? -32.878 17.613  46.123 1.00 76.00  ? 365 LEU   A O    1 
ATOM   2626 C CB   . LEU   B 1 150 ? -35.564 16.517  47.239 1.00 72.40  ? 365 LEU   A CB   1 
ATOM   2627 C CG   . LEU   B 1 150 ? -35.966 17.757  48.047 1.00 75.35  ? 365 LEU   A CG   1 
ATOM   2628 C CD1  . LEU   B 1 150 ? -37.359 18.209  47.630 1.00 66.09  ? 365 LEU   A CD1  1 
ATOM   2629 C CD2  . LEU   B 1 150 ? -35.919 17.489  49.569 1.00 76.23  ? 365 LEU   A CD2  1 
ATOM   2630 N N    . GLU   B 1 151 ? -34.419 19.089  45.391 1.00 68.77  ? 366 GLU   A N    1 
ATOM   2631 C CA   . GLU   B 1 151 ? -33.467 20.194  45.338 1.00 73.55  ? 366 GLU   A CA   1 
ATOM   2632 C C    . GLU   B 1 151 ? -34.219 21.511  45.344 1.00 77.33  ? 366 GLU   A C    1 
ATOM   2633 O O    . GLU   B 1 151 ? -34.950 21.806  44.390 1.00 76.09  ? 366 GLU   A O    1 
ATOM   2634 C CB   . GLU   B 1 151 ? -32.595 20.096  44.098 1.00 74.29  ? 366 GLU   A CB   1 
ATOM   2635 C CG   . GLU   B 1 151 ? -31.249 20.788  44.210 1.00 76.72  ? 366 GLU   A CG   1 
ATOM   2636 C CD   . GLU   B 1 151 ? -30.528 20.829  42.872 1.00 77.27  ? 366 GLU   A CD   1 
ATOM   2637 O OE1  . GLU   B 1 151 ? -31.047 21.455  41.908 1.00 75.82  ? 366 GLU   A OE1  1 
ATOM   2638 O OE2  . GLU   B 1 151 ? -29.451 20.198  42.785 1.00 75.28  ? 366 GLU   A OE2  1 
ATOM   2639 N N    . ASP   B 1 152 ? -34.016 22.316  46.393 1.00 76.98  ? 367 ASP   A N    1 
ATOM   2640 C CA   . ASP   B 1 152 ? -34.525 23.683  46.411 1.00 75.99  ? 367 ASP   A CA   1 
ATOM   2641 C C    . ASP   B 1 152 ? -36.040 23.670  46.236 1.00 75.21  ? 367 ASP   A C    1 
ATOM   2642 O O    . ASP   B 1 152 ? -36.586 24.301  45.327 1.00 77.09  ? 367 ASP   A O    1 
ATOM   2643 C CB   . ASP   B 1 152 ? -33.857 24.524  45.313 1.00 83.08  ? 367 ASP   A CB   1 
ATOM   2644 C CG   . ASP   B 1 152 ? -32.434 24.958  45.670 1.00 89.13  ? 367 ASP   A CG   1 
ATOM   2645 O OD1  . ASP   B 1 152 ? -31.770 24.275  46.484 1.00 90.95  ? 367 ASP   A OD1  1 
ATOM   2646 O OD2  . ASP   B 1 152 ? -31.959 25.963  45.092 1.00 93.46  ? 367 ASP   A OD2  1 
ATOM   2647 N N    . GLY   B 1 153 ? -36.714 22.889  47.083 1.00 72.83  ? 368 GLY   A N    1 
ATOM   2648 C CA   . GLY   B 1 153 ? -38.160 22.794  47.057 1.00 67.73  ? 368 GLY   A CA   1 
ATOM   2649 C C    . GLY   B 1 153 ? -38.731 22.257  45.760 1.00 71.91  ? 368 GLY   A C    1 
ATOM   2650 O O    . GLY   B 1 153 ? -39.953 22.243  45.583 1.00 71.79  ? 368 GLY   A O    1 
ATOM   2651 N N    . ARG   B 1 154 ? -37.872 21.803  44.851 1.00 68.03  ? 369 ARG   A N    1 
ATOM   2652 C CA   . ARG   B 1 154 ? -38.297 21.293  43.555 1.00 70.67  ? 369 ARG   A CA   1 
ATOM   2653 C C    . ARG   B 1 154 ? -37.802 19.861  43.364 1.00 65.93  ? 369 ARG   A C    1 
ATOM   2654 O O    . ARG   B 1 154 ? -36.885 19.392  44.047 1.00 66.75  ? 369 ARG   A O    1 
ATOM   2655 C CB   . ARG   B 1 154 ? -37.779 22.189  42.408 1.00 72.13  ? 369 ARG   A CB   1 
ATOM   2656 C CG   . ARG   B 1 154 ? -38.812 23.218  41.952 1.00 75.90  ? 369 ARG   A CG   1 
ATOM   2657 C CD   . ARG   B 1 154 ? -38.693 23.644  40.479 1.00 77.28  ? 369 ARG   A CD   1 
ATOM   2658 N NE   . ARG   B 1 154 ? -39.665 22.941  39.642 1.00 76.73  ? 369 ARG   A NE   1 
ATOM   2659 C CZ   . ARG   B 1 154 ? -40.834 23.441  39.251 1.00 73.08  ? 369 ARG   A CZ   1 
ATOM   2660 N NH1  . ARG   B 1 154 ? -41.266 24.618  39.690 1.00 74.21  ? 369 ARG   A NH1  1 
ATOM   2661 N NH2  . ARG   B 1 154 ? -41.603 22.727  38.424 1.00 68.71  ? 369 ARG   A NH2  1 
ATOM   2662 N N    . PHE   B 1 155 ? -38.422 19.155  42.433 1.00 65.94  ? 370 PHE   A N    1 
ATOM   2663 C CA   . PHE   B 1 155 ? -37.859 17.892  41.996 1.00 68.66  ? 370 PHE   A CA   1 
ATOM   2664 C C    . PHE   B 1 155 ? -37.101 18.103  40.692 1.00 67.79  ? 370 PHE   A C    1 
ATOM   2665 O O    . PHE   B 1 155 ? -37.565 18.807  39.785 1.00 66.58  ? 370 PHE   A O    1 
ATOM   2666 C CB   . PHE   B 1 155 ? -38.946 16.824  41.856 1.00 65.32  ? 370 PHE   A CB   1 
ATOM   2667 C CG   . PHE   B 1 155 ? -39.479 16.345  43.177 1.00 63.06  ? 370 PHE   A CG   1 
ATOM   2668 C CD1  . PHE   B 1 155 ? -38.651 15.676  44.072 1.00 64.81  ? 370 PHE   A CD1  1 
ATOM   2669 C CD2  . PHE   B 1 155 ? -40.796 16.585  43.545 1.00 65.46  ? 370 PHE   A CD2  1 
ATOM   2670 C CE1  . PHE   B 1 155 ? -39.134 15.244  45.305 1.00 64.24  ? 370 PHE   A CE1  1 
ATOM   2671 C CE2  . PHE   B 1 155 ? -41.289 16.148  44.773 1.00 59.30  ? 370 PHE   A CE2  1 
ATOM   2672 C CZ   . PHE   B 1 155 ? -40.456 15.481  45.650 1.00 59.24  ? 370 PHE   A CZ   1 
ATOM   2673 N N    . VAL   B 1 156 ? -35.905 17.536  40.624 1.00 65.28  ? 371 VAL   A N    1 
ATOM   2674 C CA   . VAL   B 1 156 ? -35.023 17.720  39.479 1.00 67.77  ? 371 VAL   A CA   1 
ATOM   2675 C C    . VAL   B 1 156 ? -34.642 16.350  38.938 1.00 65.46  ? 371 VAL   A C    1 
ATOM   2676 O O    . VAL   B 1 156 ? -34.513 15.385  39.702 1.00 68.24  ? 371 VAL   A O    1 
ATOM   2677 C CB   . VAL   B 1 156 ? -33.781 18.557  39.860 1.00 71.14  ? 371 VAL   A CB   1 
ATOM   2678 C CG1  . VAL   B 1 156 ? -34.207 19.745  40.727 1.00 73.12  ? 371 VAL   A CG1  1 
ATOM   2679 C CG2  . VAL   B 1 156 ? -32.781 17.714  40.630 1.00 72.24  ? 371 VAL   A CG2  1 
ATOM   2680 N N    . TYR   B 1 157 ? -34.515 16.257  37.616 1.00 62.09  ? 372 TYR   A N    1 
ATOM   2681 C CA   . TYR   B 1 157 ? -34.156 15.018  36.936 1.00 62.62  ? 372 TYR   A CA   1 
ATOM   2682 C C    . TYR   B 1 157 ? -32.971 15.310  36.040 1.00 63.80  ? 372 TYR   A C    1 
ATOM   2683 O O    . TYR   B 1 157 ? -33.076 16.137  35.126 1.00 62.88  ? 372 TYR   A O    1 
ATOM   2684 C CB   . TYR   B 1 157 ? -35.324 14.474  36.113 1.00 59.87  ? 372 TYR   A CB   1 
ATOM   2685 C CG   . TYR   B 1 157 ? -36.615 14.464  36.883 1.00 61.65  ? 372 TYR   A CG   1 
ATOM   2686 C CD1  . TYR   B 1 157 ? -37.362 15.625  37.031 1.00 60.72  ? 372 TYR   A CD1  1 
ATOM   2687 C CD2  . TYR   B 1 157 ? -37.086 13.291  37.485 1.00 61.87  ? 372 TYR   A CD2  1 
ATOM   2688 C CE1  . TYR   B 1 157 ? -38.550 15.614  37.747 1.00 63.45  ? 372 TYR   A CE1  1 
ATOM   2689 C CE2  . TYR   B 1 157 ? -38.275 13.271  38.195 1.00 58.95  ? 372 TYR   A CE2  1 
ATOM   2690 C CZ   . TYR   B 1 157 ? -38.997 14.435  38.328 1.00 59.89  ? 372 TYR   A CZ   1 
ATOM   2691 O OH   . TYR   B 1 157 ? -40.170 14.446  39.033 1.00 59.19  ? 372 TYR   A OH   1 
ATOM   2692 N N    . ARG   B 1 158 ? -31.844 14.653  36.299 1.00 61.02  ? 373 ARG   A N    1 
ATOM   2693 C CA   . ARG   B 1 158 ? -30.606 15.008  35.618 1.00 59.86  ? 373 ARG   A CA   1 
ATOM   2694 C C    . ARG   B 1 158 ? -30.063 13.800  34.865 1.00 61.92  ? 373 ARG   A C    1 
ATOM   2695 O O    . ARG   B 1 158 ? -29.634 12.812  35.474 1.00 62.53  ? 373 ARG   A O    1 
ATOM   2696 C CB   . ARG   B 1 158 ? -29.594 15.580  36.608 1.00 61.61  ? 373 ARG   A CB   1 
ATOM   2697 C CG   . ARG   B 1 158 ? -29.976 17.010  37.076 1.00 63.40  ? 373 ARG   A CG   1 
ATOM   2698 C CD   . ARG   B 1 158 ? -28.810 17.780  37.679 1.00 61.91  ? 373 ARG   A CD   1 
ATOM   2699 N NE   . ARG   B 1 158 ? -28.842 17.715  39.136 1.00 71.92  ? 373 ARG   A NE   1 
ATOM   2700 C CZ   . ARG   B 1 158 ? -29.124 18.741  39.932 1.00 72.22  ? 373 ARG   A CZ   1 
ATOM   2701 N NH1  . ARG   B 1 158 ? -29.380 19.949  39.448 1.00 70.61  ? 373 ARG   A NH1  1 
ATOM   2702 N NH2  . ARG   B 1 158 ? -29.150 18.552  41.247 1.00 73.31  ? 373 ARG   A NH2  1 
ATOM   2703 N N    . LEU   B 1 159 ? -30.109 13.880  33.536 1.00 60.56  ? 374 LEU   A N    1 
ATOM   2704 C CA   . LEU   B 1 159 ? -29.459 12.923  32.647 1.00 60.06  ? 374 LEU   A CA   1 
ATOM   2705 C C    . LEU   B 1 159 ? -28.299 13.682  31.997 1.00 60.56  ? 374 LEU   A C    1 
ATOM   2706 O O    . LEU   B 1 159 ? -28.444 14.293  30.933 1.00 61.53  ? 374 LEU   A O    1 
ATOM   2707 C CB   . LEU   B 1 159 ? -30.454 12.365  31.619 1.00 59.49  ? 374 LEU   A CB   1 
ATOM   2708 C CG   . LEU   B 1 159 ? -31.796 11.856  32.163 1.00 61.98  ? 374 LEU   A CG   1 
ATOM   2709 C CD1  . LEU   B 1 159 ? -32.797 12.987  32.281 1.00 59.45  ? 374 LEU   A CD1  1 
ATOM   2710 C CD2  . LEU   B 1 159 ? -32.353 10.763  31.282 1.00 62.01  ? 374 LEU   A CD2  1 
ATOM   2711 N N    . LEU   B 1 160 ? -27.143 13.653  32.648 1.00 59.37  ? 375 LEU   A N    1 
ATOM   2712 C CA   . LEU   B 1 160 ? -26.004 14.461  32.244 1.00 60.13  ? 375 LEU   A CA   1 
ATOM   2713 C C    . LEU   B 1 160 ? -24.881 13.578  31.711 1.00 63.78  ? 375 LEU   A C    1 
ATOM   2714 O O    . LEU   B 1 160 ? -24.664 12.459  32.198 1.00 59.76  ? 375 LEU   A O    1 
ATOM   2715 C CB   . LEU   B 1 160 ? -25.495 15.311  33.411 1.00 63.20  ? 375 LEU   A CB   1 
ATOM   2716 C CG   . LEU   B 1 160 ? -26.517 16.191  34.141 1.00 62.49  ? 375 LEU   A CG   1 
ATOM   2717 C CD1  . LEU   B 1 160 ? -25.841 17.189  35.068 1.00 60.19  ? 375 LEU   A CD1  1 
ATOM   2718 C CD2  . LEU   B 1 160 ? -27.367 16.909  33.116 1.00 59.56  ? 375 LEU   A CD2  1 
ATOM   2719 N N    . ARG   B 1 161 ? -24.187 14.094  30.691 1.00 62.21  ? 376 ARG   A N    1 
ATOM   2720 C CA   . ARG   B 1 161 ? -23.059 13.420  30.048 1.00 63.10  ? 376 ARG   A CA   1 
ATOM   2721 C C    . ARG   B 1 161 ? -23.435 12.013  29.586 1.00 62.03  ? 376 ARG   A C    1 
ATOM   2722 O O    . ARG   B 1 161 ? -22.652 11.072  29.721 1.00 63.54  ? 376 ARG   A O    1 
ATOM   2723 C CB   . ARG   B 1 161 ? -21.812 13.367  30.951 1.00 64.89  ? 376 ARG   A CB   1 
ATOM   2724 C CG   . ARG   B 1 161 ? -21.172 14.719  31.387 1.00 68.78  ? 376 ARG   A CG   1 
ATOM   2725 C CD   . ARG   B 1 161 ? -22.226 15.824  31.559 1.00 73.09  ? 376 ARG   A CD   1 
ATOM   2726 N NE   . ARG   B 1 161 ? -21.776 16.994  32.314 1.00 82.47  ? 376 ARG   A NE   1 
ATOM   2727 C CZ   . ARG   B 1 161 ? -22.461 18.129  32.425 1.00 81.33  ? 376 ARG   A CZ   1 
ATOM   2728 N NH1  . ARG   B 1 161 ? -23.576 18.339  31.728 1.00 73.22  ? 376 ARG   A NH1  1 
ATOM   2729 N NH2  . ARG   B 1 161 ? -22.014 19.080  33.249 1.00 81.95  ? 376 ARG   A NH2  1 
ATOM   2730 N N    . SER   B 1 162 ? -24.628 11.860  29.017 1.00 58.53  ? 377 SER   A N    1 
ATOM   2731 C CA   . SER   B 1 162 ? -24.909 10.634  28.267 1.00 61.38  ? 377 SER   A CA   1 
ATOM   2732 C C    . SER   B 1 162 ? -23.988 10.559  27.048 1.00 62.43  ? 377 SER   A C    1 
ATOM   2733 O O    . SER   B 1 162 ? -23.984 11.486  26.215 1.00 56.55  ? 377 SER   A O    1 
ATOM   2734 C CB   . SER   B 1 162 ? -26.362 10.576  27.816 1.00 59.95  ? 377 SER   A CB   1 
ATOM   2735 O OG   . SER   B 1 162 ? -27.210 11.073  28.826 1.00 67.57  ? 377 SER   A OG   1 
ATOM   2736 N N    . PRO   B 1 163 ? -23.205 9.496   26.894 1.00 58.24  ? 378 PRO   A N    1 
ATOM   2737 C CA   . PRO   B 1 163 ? -22.427 9.325   25.656 1.00 61.00  ? 378 PRO   A CA   1 
ATOM   2738 C C    . PRO   B 1 163 ? -23.339 9.327   24.440 1.00 59.85  ? 378 PRO   A C    1 
ATOM   2739 O O    . PRO   B 1 163 ? -24.219 8.473   24.294 1.00 58.81  ? 378 PRO   A O    1 
ATOM   2740 C CB   . PRO   B 1 163 ? -21.742 7.972   25.850 1.00 58.69  ? 378 PRO   A CB   1 
ATOM   2741 C CG   . PRO   B 1 163 ? -21.760 7.745   27.367 1.00 59.64  ? 378 PRO   A CG   1 
ATOM   2742 C CD   . PRO   B 1 163 ? -23.037 8.372   27.827 1.00 56.77  ? 378 PRO   A CD   1 
ATOM   2743 N N    . MET   B 1 164 ? -23.132 10.320  23.579 1.00 59.26  ? 379 MET   A N    1 
ATOM   2744 C CA   . MET   B 1 164 ? -23.849 10.387  22.319 1.00 60.95  ? 379 MET   A CA   1 
ATOM   2745 C C    . MET   B 1 164 ? -23.620 9.104   21.528 1.00 62.40  ? 379 MET   A C    1 
ATOM   2746 O O    . MET   B 1 164 ? -22.486 8.624   21.419 1.00 61.63  ? 379 MET   A O    1 
ATOM   2747 C CB   . MET   B 1 164 ? -23.381 11.620  21.550 1.00 61.22  ? 379 MET   A CB   1 
ATOM   2748 C CG   . MET   B 1 164 ? -24.320 12.081  20.459 1.00 66.33  ? 379 MET   A CG   1 
ATOM   2749 S SD   . MET   B 1 164 ? -23.556 13.329  19.390 1.00 63.08  ? 379 MET   A SD   1 
ATOM   2750 C CE   . MET   B 1 164 ? -23.565 14.781  20.440 1.00 53.18  ? 379 MET   A CE   1 
ATOM   2751 N N    . CYS   B 1 165 ? -24.704 8.513   21.023 1.00 62.58  ? 380 CYS   A N    1 
ATOM   2752 C CA   . CYS   B 1 165 ? -24.568 7.238   20.324 1.00 66.27  ? 380 CYS   A CA   1 
ATOM   2753 C C    . CYS   B 1 165 ? -23.605 7.404   19.165 1.00 68.91  ? 380 CYS   A C    1 
ATOM   2754 O O    . CYS   B 1 165 ? -23.595 8.437   18.491 1.00 66.44  ? 380 CYS   A O    1 
ATOM   2755 C CB   . CYS   B 1 165 ? -25.912 6.733   19.802 1.00 67.79  ? 380 CYS   A CB   1 
ATOM   2756 S SG   . CYS   B 1 165 ? -26.786 7.941   18.804 1.00 72.72  ? 380 CYS   A SG   1 
ATOM   2757 N N    . GLU   B 1 166 ? -22.777 6.387   18.946 1.00 77.13  ? 381 GLU   A N    1 
ATOM   2758 C CA   . GLU   B 1 166 ? -21.702 6.540   17.983 1.00 78.47  ? 381 GLU   A CA   1 
ATOM   2759 C C    . GLU   B 1 166 ? -22.225 6.801   16.579 1.00 75.99  ? 381 GLU   A C    1 
ATOM   2760 O O    . GLU   B 1 166 ? -21.491 7.342   15.745 1.00 74.90  ? 381 GLU   A O    1 
ATOM   2761 C CB   . GLU   B 1 166 ? -20.800 5.315   18.011 1.00 86.81  ? 381 GLU   A CB   1 
ATOM   2762 C CG   . GLU   B 1 166 ? -19.742 5.409   19.109 1.00 93.11  ? 381 GLU   A CG   1 
ATOM   2763 C CD   . GLU   B 1 166 ? -18.844 6.630   18.934 1.00 93.12  ? 381 GLU   A CD   1 
ATOM   2764 O OE1  . GLU   B 1 166 ? -18.616 7.352   19.941 1.00 91.14  ? 381 GLU   A OE1  1 
ATOM   2765 O OE2  . GLU   B 1 166 ? -18.377 6.866   17.790 1.00 91.64  ? 381 GLU   A OE2  1 
ATOM   2766 N N    . TYR   B 1 167 ? -23.484 6.467   16.299 1.00 73.01  ? 382 TYR   A N    1 
ATOM   2767 C CA   . TYR   B 1 167 ? -24.066 6.880   15.030 1.00 67.45  ? 382 TYR   A CA   1 
ATOM   2768 C C    . TYR   B 1 167 ? -24.021 8.399   14.898 1.00 66.97  ? 382 TYR   A C    1 
ATOM   2769 O O    . TYR   B 1 167 ? -23.446 8.939   13.944 1.00 65.33  ? 382 TYR   A O    1 
ATOM   2770 C CB   . TYR   B 1 167 ? -25.499 6.350   14.900 1.00 68.73  ? 382 TYR   A CB   1 
ATOM   2771 C CG   . TYR   B 1 167 ? -26.180 6.810   13.638 1.00 64.97  ? 382 TYR   A CG   1 
ATOM   2772 C CD1  . TYR   B 1 167 ? -26.797 8.050   13.589 1.00 60.97  ? 382 TYR   A CD1  1 
ATOM   2773 C CD2  . TYR   B 1 167 ? -26.186 6.015   12.484 1.00 64.03  ? 382 TYR   A CD2  1 
ATOM   2774 C CE1  . TYR   B 1 167 ? -27.398 8.501   12.442 1.00 63.70  ? 382 TYR   A CE1  1 
ATOM   2775 C CE2  . TYR   B 1 167 ? -26.803 6.459   11.312 1.00 58.97  ? 382 TYR   A CE2  1 
ATOM   2776 C CZ   . TYR   B 1 167 ? -27.399 7.709   11.307 1.00 63.80  ? 382 TYR   A CZ   1 
ATOM   2777 O OH   . TYR   B 1 167 ? -28.022 8.205   10.193 1.00 64.10  ? 382 TYR   A OH   1 
ATOM   2778 N N    . LEU   B 1 168 ? -24.618 9.112   15.853 1.00 67.00  ? 383 LEU   A N    1 
ATOM   2779 C CA   . LEU   B 1 168 ? -24.582 10.569  15.802 1.00 63.58  ? 383 LEU   A CA   1 
ATOM   2780 C C    . LEU   B 1 168 ? -23.159 11.101  15.644 1.00 61.26  ? 383 LEU   A C    1 
ATOM   2781 O O    . LEU   B 1 168 ? -22.931 12.078  14.925 1.00 58.26  ? 383 LEU   A O    1 
ATOM   2782 C CB   . LEU   B 1 168 ? -25.225 11.154  17.059 1.00 64.32  ? 383 LEU   A CB   1 
ATOM   2783 C CG   . LEU   B 1 168 ? -26.742 11.299  16.952 1.00 65.83  ? 383 LEU   A CG   1 
ATOM   2784 C CD1  . LEU   B 1 168 ? -27.281 12.325  17.964 1.00 62.65  ? 383 LEU   A CD1  1 
ATOM   2785 C CD2  . LEU   B 1 168 ? -27.131 11.663  15.511 1.00 63.39  ? 383 LEU   A CD2  1 
ATOM   2786 N N    . VAL   B 1 169 ? -22.189 10.488  16.325 1.00 67.11  ? 384 VAL   A N    1 
ATOM   2787 C CA   . VAL   B 1 169 ? -20.811 10.978  16.254 1.00 66.43  ? 384 VAL   A CA   1 
ATOM   2788 C C    . VAL   B 1 169 ? -20.298 10.949  14.820 1.00 65.20  ? 384 VAL   A C    1 
ATOM   2789 O O    . VAL   B 1 169 ? -19.840 11.963  14.286 1.00 62.71  ? 384 VAL   A O    1 
ATOM   2790 C CB   . VAL   B 1 169 ? -19.894 10.170  17.183 1.00 67.82  ? 384 VAL   A CB   1 
ATOM   2791 C CG1  . VAL   B 1 169 ? -18.617 10.953  17.460 1.00 62.52  ? 384 VAL   A CG1  1 
ATOM   2792 C CG2  . VAL   B 1 169 ? -20.640 9.849   18.483 1.00 72.72  ? 384 VAL   A CG2  1 
ATOM   2793 N N    . ASN   B 1 170 ? -20.339 9.776   14.189 1.00 63.60  ? 385 ASN   A N    1 
ATOM   2794 C CA   . ASN   B 1 170 ? -19.841 9.657   12.823 1.00 64.24  ? 385 ASN   A CA   1 
ATOM   2795 C C    . ASN   B 1 170 ? -20.627 10.553  11.864 1.00 61.75  ? 385 ASN   A C    1 
ATOM   2796 O O    . ASN   B 1 170 ? -20.039 11.197  10.989 1.00 59.34  ? 385 ASN   A O    1 
ATOM   2797 C CB   . ASN   B 1 170 ? -19.870 8.185   12.407 1.00 69.76  ? 385 ASN   A CB   1 
ATOM   2798 C CG   . ASN   B 1 170 ? -18.979 7.299   13.316 1.00 79.04  ? 385 ASN   A CG   1 
ATOM   2799 O OD1  . ASN   B 1 170 ? -17.827 7.642   13.609 1.00 80.53  ? 385 ASN   A OD1  1 
ATOM   2800 N ND2  . ASN   B 1 170 ? -19.524 6.170   13.770 1.00 81.17  ? 385 ASN   A ND2  1 
ATOM   2801 N N    . PHE   B 1 171 ? -21.948 10.664  12.056 1.00 59.56  ? 386 PHE   A N    1 
ATOM   2802 C CA   . PHE   B 1 171 ? -22.727 11.608  11.262 1.00 56.07  ? 386 PHE   A CA   1 
ATOM   2803 C C    . PHE   B 1 171 ? -22.239 13.039  11.468 1.00 59.54  ? 386 PHE   A C    1 
ATOM   2804 O O    . PHE   B 1 171 ? -22.129 13.807  10.504 1.00 62.62  ? 386 PHE   A O    1 
ATOM   2805 C CB   . PHE   B 1 171 ? -24.217 11.504  11.589 1.00 53.65  ? 386 PHE   A CB   1 
ATOM   2806 C CG   . PHE   B 1 171 ? -25.079 12.471  10.804 1.00 53.43  ? 386 PHE   A CG   1 
ATOM   2807 C CD1  . PHE   B 1 171 ? -25.194 12.357  9.415  1.00 55.37  ? 386 PHE   A CD1  1 
ATOM   2808 C CD2  . PHE   B 1 171 ? -25.785 13.468  11.444 1.00 50.62  ? 386 PHE   A CD2  1 
ATOM   2809 C CE1  . PHE   B 1 171 ? -25.988 13.222  8.691  1.00 51.76  ? 386 PHE   A CE1  1 
ATOM   2810 C CE2  . PHE   B 1 171 ? -26.581 14.339  10.733 1.00 52.78  ? 386 PHE   A CE2  1 
ATOM   2811 C CZ   . PHE   B 1 171 ? -26.677 14.220  9.349  1.00 55.38  ? 386 PHE   A CZ   1 
ATOM   2812 N N    . LEU   B 1 172 ? -21.940 13.421  12.708 1.00 59.82  ? 387 LEU   A N    1 
ATOM   2813 C CA   . LEU   B 1 172 ? -21.374 14.746  12.932 1.00 59.69  ? 387 LEU   A CA   1 
ATOM   2814 C C    . LEU   B 1 172 ? -20.049 14.903  12.205 1.00 60.13  ? 387 LEU   A C    1 
ATOM   2815 O O    . LEU   B 1 172 ? -19.721 15.991  11.725 1.00 62.59  ? 387 LEU   A O    1 
ATOM   2816 C CB   . LEU   B 1 172 ? -21.182 15.001  14.428 1.00 55.49  ? 387 LEU   A CB   1 
ATOM   2817 C CG   . LEU   B 1 172 ? -22.416 15.392  15.227 1.00 55.96  ? 387 LEU   A CG   1 
ATOM   2818 C CD1  . LEU   B 1 172 ? -22.032 15.639  16.706 1.00 54.55  ? 387 LEU   A CD1  1 
ATOM   2819 C CD2  . LEU   B 1 172 ? -23.111 16.598  14.615 1.00 49.79  ? 387 LEU   A CD2  1 
ATOM   2820 N N    . HIS   B 1 173 ? -19.266 13.833  12.130 1.00 60.27  ? 388 HIS   A N    1 
ATOM   2821 C CA   A HIS   B 1 173 ? -17.948 13.979  11.539 0.50 59.54  ? 388 HIS   A CA   1 
ATOM   2822 C CA   B HIS   B 1 173 ? -17.933 13.896  11.535 0.50 59.74  ? 388 HIS   A CA   1 
ATOM   2823 C C    . HIS   B 1 173 ? -18.012 14.018  10.016 1.00 65.23  ? 388 HIS   A C    1 
ATOM   2824 O O    . HIS   B 1 173 ? -17.216 14.729  9.393  1.00 65.76  ? 388 HIS   A O    1 
ATOM   2825 C CB   A HIS   B 1 173 ? -17.034 12.863  12.035 0.50 63.69  ? 388 HIS   A CB   1 
ATOM   2826 C CB   B HIS   B 1 173 ? -17.146 12.647  11.937 0.50 64.45  ? 388 HIS   A CB   1 
ATOM   2827 C CG   A HIS   B 1 173 ? -16.228 13.245  13.238 0.50 64.20  ? 388 HIS   A CG   1 
ATOM   2828 C CG   B HIS   B 1 173 ? -15.679 12.714  11.641 0.50 64.37  ? 388 HIS   A CG   1 
ATOM   2829 N ND1  A HIS   B 1 173 ? -15.288 14.254  13.216 0.50 64.86  ? 388 HIS   A ND1  1 
ATOM   2830 N ND1  B HIS   B 1 173 ? -14.775 13.330  12.482 0.50 63.99  ? 388 HIS   A ND1  1 
ATOM   2831 C CD2  A HIS   B 1 173 ? -16.242 12.771  14.508 0.50 61.87  ? 388 HIS   A CD2  1 
ATOM   2832 C CD2  B HIS   B 1 173 ? -14.953 12.214  10.611 0.50 61.90  ? 388 HIS   A CD2  1 
ATOM   2833 C CE1  A HIS   B 1 173 ? -14.743 14.370  14.414 0.50 66.85  ? 388 HIS   A CE1  1 
ATOM   2834 C CE1  B HIS   B 1 173 ? -13.559 13.218  11.976 0.50 64.21  ? 388 HIS   A CE1  1 
ATOM   2835 N NE2  A HIS   B 1 173 ? -15.308 13.485  15.218 0.50 64.43  ? 388 HIS   A NE2  1 
ATOM   2836 N NE2  B HIS   B 1 173 ? -13.640 12.545  10.842 0.50 61.24  ? 388 HIS   A NE2  1 
ATOM   2837 N N    . LYS   B 1 174 ? -18.951 13.305  9.395  1.00 59.63  ? 389 LYS   A N    1 
ATOM   2838 C CA   . LYS   B 1 174 ? -19.130 13.482  7.962  1.00 59.18  ? 389 LYS   A CA   1 
ATOM   2839 C C    . LYS   B 1 174 ? -19.837 14.786  7.644  1.00 59.11  ? 389 LYS   A C    1 
ATOM   2840 O O    . LYS   B 1 174 ? -19.587 15.375  6.590  1.00 60.42  ? 389 LYS   A O    1 
ATOM   2841 C CB   . LYS   B 1 174 ? -19.896 12.318  7.352  1.00 53.80  ? 389 LYS   A CB   1 
ATOM   2842 C CG   . LYS   B 1 174 ? -19.253 10.995  7.584  1.00 55.62  ? 389 LYS   A CG   1 
ATOM   2843 C CD   . LYS   B 1 174 ? -20.311 9.924   7.619  1.00 56.90  ? 389 LYS   A CD   1 
ATOM   2844 C CE   . LYS   B 1 174 ? -19.701 8.566   7.533  1.00 58.78  ? 389 LYS   A CE   1 
ATOM   2845 N NZ   . LYS   B 1 174 ? -20.780 7.553   7.629  1.00 65.54  ? 389 LYS   A NZ   1 
ATOM   2846 N N    . LEU   B 1 175 ? -20.731 15.247  8.519  1.00 60.39  ? 390 LEU   A N    1 
ATOM   2847 C CA   . LEU   B 1 175 ? -21.390 16.524  8.269  1.00 57.97  ? 390 LEU   A CA   1 
ATOM   2848 C C    . LEU   B 1 175 ? -20.402 17.665  8.414  1.00 58.87  ? 390 LEU   A C    1 
ATOM   2849 O O    . LEU   B 1 175 ? -20.445 18.646  7.664  1.00 55.37  ? 390 LEU   A O    1 
ATOM   2850 C CB   . LEU   B 1 175 ? -22.549 16.699  9.230  1.00 55.46  ? 390 LEU   A CB   1 
ATOM   2851 C CG   . LEU   B 1 175 ? -23.760 17.490  8.765  1.00 54.81  ? 390 LEU   A CG   1 
ATOM   2852 C CD1  . LEU   B 1 175 ? -24.327 16.834  7.521  1.00 54.90  ? 390 LEU   A CD1  1 
ATOM   2853 C CD2  . LEU   B 1 175 ? -24.804 17.552  9.895  1.00 55.03  ? 390 LEU   A CD2  1 
ATOM   2854 N N    . ARG   B 1 176 ? -19.470 17.579  9.321  1.00 61.07  ? 391 ARG   A N    1 
ATOM   2855 C CA   . ARG   B 1 176 ? -18.669 18.763  9.516  1.00 61.10  ? 391 ARG   A CA   1 
ATOM   2856 C C    . ARG   B 1 176 ? -17.791 19.119  8.350  1.00 62.39  ? 391 ARG   A C    1 
ATOM   2857 O O    . ARG   B 1 176 ? -17.372 20.248  8.226  1.00 62.33  ? 391 ARG   A O    1 
ATOM   2858 C CB   . ARG   B 1 176 ? -17.884 18.716  10.816 1.00 60.74  ? 391 ARG   A CB   1 
ATOM   2859 C CG   . ARG   B 1 176 ? -16.845 17.627  10.932 1.00 63.06  ? 391 ARG   A CG   1 
ATOM   2860 C CD   . ARG   B 1 176 ? -15.879 17.899  12.078 1.00 63.66  ? 391 ARG   A CD   1 
ATOM   2861 N NE   . ARG   B 1 176 ? -15.760 19.311  12.411 1.00 65.62  ? 391 ARG   A NE   1 
ATOM   2862 C CZ   . ARG   B 1 176 ? -14.945 19.780  13.330 1.00 66.99  ? 391 ARG   A CZ   1 
ATOM   2863 N NH1  . ARG   B 1 176 ? -14.178 18.948  13.997 1.00 69.74  ? 391 ARG   A NH1  1 
ATOM   2864 N NH2  . ARG   B 1 176 ? -14.905 21.073  13.565 1.00 66.37  ? 391 ARG   A NH2  1 
ATOM   2865 N N    . GLN   B 1 177 ? -17.515 18.160  7.487  1.00 63.38  ? 392 GLN   A N    1 
ATOM   2866 C CA   . GLN   B 1 177 ? -16.584 18.435  6.403  1.00 64.13  ? 392 GLN   A CA   1 
ATOM   2867 C C    . GLN   B 1 177 ? -17.251 18.897  5.116  1.00 63.09  ? 392 GLN   A C    1 
ATOM   2868 O O    . GLN   B 1 177 ? -16.552 19.402  4.230  1.00 65.27  ? 392 GLN   A O    1 
ATOM   2869 C CB   . GLN   B 1 177 ? -15.753 17.182  6.099  1.00 68.34  ? 392 GLN   A CB   1 
ATOM   2870 C CG   . GLN   B 1 177 ? -14.995 16.649  7.312  1.00 70.64  ? 392 GLN   A CG   1 
ATOM   2871 C CD   . GLN   B 1 177 ? -14.703 15.162  7.196  1.00 75.92  ? 392 GLN   A CD   1 
ATOM   2872 O OE1  . GLN   B 1 177 ? -14.968 14.538  6.159  1.00 75.40  ? 392 GLN   A OE1  1 
ATOM   2873 N NE2  . GLN   B 1 177 ? -14.180 14.578  8.274  1.00 75.55  ? 392 GLN   A NE2  1 
ATOM   2874 N N    . LEU   B 1 178 ? -18.560 18.735  4.980  1.00 58.68  ? 393 LEU   A N    1 
ATOM   2875 C CA   . LEU   B 1 178 ? -19.240 19.294  3.828  1.00 56.99  ? 393 LEU   A CA   1 
ATOM   2876 C C    . LEU   B 1 178 ? -18.752 20.708  3.537  1.00 59.35  ? 393 LEU   A C    1 
ATOM   2877 O O    . LEU   B 1 178 ? -18.539 21.511  4.456  1.00 57.92  ? 393 LEU   A O    1 
ATOM   2878 C CB   . LEU   B 1 178 ? -20.746 19.300  4.009  1.00 54.23  ? 393 LEU   A CB   1 
ATOM   2879 C CG   . LEU   B 1 178 ? -21.363 17.923  4.141  1.00 54.05  ? 393 LEU   A CG   1 
ATOM   2880 C CD1  . LEU   B 1 178 ? -22.714 17.963  3.445  1.00 54.09  ? 393 LEU   A CD1  1 
ATOM   2881 C CD2  . LEU   B 1 178 ? -20.441 16.867  3.574  1.00 52.23  ? 393 LEU   A CD2  1 
ATOM   2882 N N    . PRO   B 1 179 ? -18.542 21.028  2.259  1.00 54.78  ? 394 PRO   A N    1 
ATOM   2883 C CA   . PRO   B 1 179 ? -17.927 22.317  1.913  1.00 55.18  ? 394 PRO   A CA   1 
ATOM   2884 C C    . PRO   B 1 179 ? -18.818 23.528  2.145  1.00 50.90  ? 394 PRO   A C    1 
ATOM   2885 O O    . PRO   B 1 179 ? -18.284 24.641  2.268  1.00 52.08  ? 394 PRO   A O    1 
ATOM   2886 C CB   . PRO   B 1 179 ? -17.594 22.150  0.421  1.00 52.95  ? 394 PRO   A CB   1 
ATOM   2887 C CG   . PRO   B 1 179 ? -17.527 20.627  0.229  1.00 55.03  ? 394 PRO   A CG   1 
ATOM   2888 C CD   . PRO   B 1 179 ? -18.570 20.087  1.123  1.00 52.38  ? 394 PRO   A CD   1 
ATOM   2889 N N    . GLU   B 1 180 ? -20.139 23.373  2.181  1.00 47.43  ? 395 GLU   A N    1 
ATOM   2890 C CA   . GLU   B 1 180 ? -21.022 24.529  2.170  1.00 49.17  ? 395 GLU   A CA   1 
ATOM   2891 C C    . GLU   B 1 180 ? -22.192 24.291  3.114  1.00 53.51  ? 395 GLU   A C    1 
ATOM   2892 O O    . GLU   B 1 180 ? -22.710 23.169  3.218  1.00 49.69  ? 395 GLU   A O    1 
ATOM   2893 C CB   . GLU   B 1 180 ? -21.558 24.813  0.769  1.00 52.41  ? 395 GLU   A CB   1 
ATOM   2894 C CG   . GLU   B 1 180 ? -20.516 25.030  -0.338 1.00 54.24  ? 395 GLU   A CG   1 
ATOM   2895 C CD   . GLU   B 1 180 ? -19.843 26.384  -0.303 1.00 56.05  ? 395 GLU   A CD   1 
ATOM   2896 O OE1  . GLU   B 1 180 ? -20.246 27.254  0.514  1.00 54.21  ? 395 GLU   A OE1  1 
ATOM   2897 O OE2  . GLU   B 1 180 ? -18.958 26.608  -1.172 1.00 59.13  ? 395 GLU   A OE2  1 
ATOM   2898 N N    . ARG   B 1 181 ? -22.601 25.366  3.798  1.00 50.91  ? 396 ARG   A N    1 
ATOM   2899 C CA   . ARG   B 1 181 ? -23.687 25.268  4.760  1.00 49.05  ? 396 ARG   A CA   1 
ATOM   2900 C C    . ARG   B 1 181 ? -24.959 24.766  4.100  1.00 49.11  ? 396 ARG   A C    1 
ATOM   2901 O O    . ARG   B 1 181 ? -25.680 23.935  4.676  1.00 44.03  ? 396 ARG   A O    1 
ATOM   2902 C CB   . ARG   B 1 181 ? -23.914 26.628  5.416  1.00 52.70  ? 396 ARG   A CB   1 
ATOM   2903 C CG   . ARG   B 1 181 ? -22.829 26.958  6.429  1.00 58.75  ? 396 ARG   A CG   1 
ATOM   2904 C CD   . ARG   B 1 181 ? -23.072 28.282  7.133  1.00 65.46  ? 396 ARG   A CD   1 
ATOM   2905 N NE   . ARG   B 1 181 ? -24.469 28.438  7.514  1.00 64.82  ? 396 ARG   A NE   1 
ATOM   2906 C CZ   . ARG   B 1 181 ? -25.334 29.227  6.890  1.00 66.40  ? 396 ARG   A CZ   1 
ATOM   2907 N NH1  . ARG   B 1 181 ? -24.968 29.980  5.861  1.00 62.35  ? 396 ARG   A NH1  1 
ATOM   2908 N NH2  . ARG   B 1 181 ? -26.592 29.278  7.327  1.00 67.59  ? 396 ARG   A NH2  1 
ATOM   2909 N N    . TYR   B 1 182 ? -25.235 25.226  2.867  1.00 47.51  ? 397 TYR   A N    1 
ATOM   2910 C CA   . TYR   B 1 182 ? -26.454 24.783  2.198  1.00 48.64  ? 397 TYR   A CA   1 
ATOM   2911 C C    . TYR   B 1 182 ? -26.406 23.296  1.902  1.00 46.02  ? 397 TYR   A C    1 
ATOM   2912 O O    . TYR   B 1 182 ? -27.464 22.658  1.786  1.00 46.68  ? 397 TYR   A O    1 
ATOM   2913 C CB   . TYR   B 1 182 ? -26.729 25.594  0.918  1.00 49.08  ? 397 TYR   A CB   1 
ATOM   2914 C CG   . TYR   B 1 182 ? -25.938 25.180  -0.302 1.00 50.47  ? 397 TYR   A CG   1 
ATOM   2915 C CD1  . TYR   B 1 182 ? -26.324 24.099  -1.074 1.00 48.79  ? 397 TYR   A CD1  1 
ATOM   2916 C CD2  . TYR   B 1 182 ? -24.829 25.910  -0.704 1.00 50.68  ? 397 TYR   A CD2  1 
ATOM   2917 C CE1  . TYR   B 1 182 ? -25.607 23.733  -2.179 1.00 51.61  ? 397 TYR   A CE1  1 
ATOM   2918 C CE2  . TYR   B 1 182 ? -24.108 25.569  -1.818 1.00 52.05  ? 397 TYR   A CE2  1 
ATOM   2919 C CZ   . TYR   B 1 182 ? -24.496 24.477  -2.555 1.00 55.23  ? 397 TYR   A CZ   1 
ATOM   2920 O OH   . TYR   B 1 182 ? -23.754 24.128  -3.669 1.00 53.56  ? 397 TYR   A OH   1 
ATOM   2921 N N    . MET   B 1 183 ? -25.209 22.717  1.845  1.00 44.37  ? 398 MET   A N    1 
ATOM   2922 C CA   . MET   B 1 183 ? -25.111 21.272  1.718  1.00 47.20  ? 398 MET   A CA   1 
ATOM   2923 C C    . MET   B 1 183 ? -25.396 20.561  3.034  1.00 48.35  ? 398 MET   A C    1 
ATOM   2924 O O    . MET   B 1 183 ? -25.997 19.478  3.022  1.00 42.59  ? 398 MET   A O    1 
ATOM   2925 C CB   . MET   B 1 183 ? -23.739 20.900  1.171  1.00 45.12  ? 398 MET   A CB   1 
ATOM   2926 C CG   . MET   B 1 183 ? -23.579 21.319  -0.269 1.00 47.50  ? 398 MET   A CG   1 
ATOM   2927 S SD   . MET   B 1 183 ? -22.047 20.740  -0.962 1.00 49.94  ? 398 MET   A SD   1 
ATOM   2928 C CE   . MET   B 1 183 ? -22.174 21.451  -2.607 1.00 56.18  ? 398 MET   A CE   1 
ATOM   2929 N N    . MET   B 1 184 ? -24.997 21.148  4.177  1.00 47.97  ? 399 MET   A N    1 
ATOM   2930 C CA   . MET   B 1 184 ? -25.391 20.565  5.455  1.00 48.47  ? 399 MET   A CA   1 
ATOM   2931 C C    . MET   B 1 184 ? -26.901 20.615  5.620  1.00 46.02  ? 399 MET   A C    1 
ATOM   2932 O O    . MET   B 1 184 ? -27.523 19.595  5.919  1.00 44.14  ? 399 MET   A O    1 
ATOM   2933 C CB   . MET   B 1 184 ? -24.682 21.257  6.622  1.00 48.72  ? 399 MET   A CB   1 
ATOM   2934 C CG   . MET   B 1 184 ? -23.174 21.074  6.587  1.00 48.53  ? 399 MET   A CG   1 
ATOM   2935 S SD   . MET   B 1 184 ? -22.212 22.395  7.323  1.00 44.32  ? 399 MET   A SD   1 
ATOM   2936 C CE   . MET   B 1 184 ? -20.670 21.524  7.631  1.00 52.34  ? 399 MET   A CE   1 
ATOM   2937 N N    . ASN   B 1 185 ? -27.516 21.773  5.360  1.00 47.16  ? 400 ASN   A N    1 
ATOM   2938 C CA   . ASN   B 1 185 ? -28.970 21.860  5.448  1.00 48.24  ? 400 ASN   A CA   1 
ATOM   2939 C C    . ASN   B 1 185 ? -29.638 20.812  4.578  1.00 47.36  ? 400 ASN   A C    1 
ATOM   2940 O O    . ASN   B 1 185 ? -30.632 20.199  4.992  1.00 49.26  ? 400 ASN   A O    1 
ATOM   2941 C CB   . ASN   B 1 185 ? -29.465 23.252  5.052  1.00 49.78  ? 400 ASN   A CB   1 
ATOM   2942 C CG   . ASN   B 1 185 ? -29.127 24.290  6.080  1.00 50.50  ? 400 ASN   A CG   1 
ATOM   2943 O OD1  . ASN   B 1 185 ? -28.509 23.975  7.105  1.00 48.00  ? 400 ASN   A OD1  1 
ATOM   2944 N ND2  . ASN   B 1 185 ? -29.534 25.539  5.831  1.00 49.76  ? 400 ASN   A ND2  1 
ATOM   2945 N N    . SER   B 1 186 ? -29.112 20.594  3.367  1.00 49.59  ? 401 SER   A N    1 
ATOM   2946 C CA   . SER   B 1 186 ? -29.680 19.575  2.486  1.00 50.07  ? 401 SER   A CA   1 
ATOM   2947 C C    . SER   B 1 186 ? -29.665 18.207  3.146  1.00 48.06  ? 401 SER   A C    1 
ATOM   2948 O O    . SER   B 1 186 ? -30.683 17.511  3.158  1.00 49.78  ? 401 SER   A O    1 
ATOM   2949 C CB   . SER   B 1 186 ? -28.924 19.520  1.165  1.00 49.10  ? 401 SER   A CB   1 
ATOM   2950 O OG   . SER   B 1 186 ? -29.466 20.463  0.259  1.00 57.10  ? 401 SER   A OG   1 
ATOM   2951 N N    . VAL   B 1 187 ? -28.507 17.797  3.675  1.00 43.41  ? 402 VAL   A N    1 
ATOM   2952 C CA   . VAL   B 1 187 ? -28.406 16.509  4.353  1.00 49.98  ? 402 VAL   A CA   1 
ATOM   2953 C C    . VAL   B 1 187 ? -29.314 16.488  5.581  1.00 52.70  ? 402 VAL   A C    1 
ATOM   2954 O O    . VAL   B 1 187 ? -30.108 15.566  5.779  1.00 49.90  ? 402 VAL   A O    1 
ATOM   2955 C CB   . VAL   B 1 187 ? -26.943 16.224  4.741  1.00 50.80  ? 402 VAL   A CB   1 
ATOM   2956 C CG1  . VAL   B 1 187 ? -26.853 14.954  5.607  1.00 47.32  ? 402 VAL   A CG1  1 
ATOM   2957 C CG2  . VAL   B 1 187 ? -26.082 16.112  3.510  1.00 49.33  ? 402 VAL   A CG2  1 
ATOM   2958 N N    . LEU   B 1 188 ? -29.214 17.521  6.413  1.00 48.88  ? 403 LEU   A N    1 
ATOM   2959 C CA   . LEU   B 1 188 ? -29.985 17.586  7.645  1.00 50.51  ? 403 LEU   A CA   1 
ATOM   2960 C C    . LEU   B 1 188 ? -31.486 17.582  7.397  1.00 51.88  ? 403 LEU   A C    1 
ATOM   2961 O O    . LEU   B 1 188 ? -32.241 17.071  8.225  1.00 51.61  ? 403 LEU   A O    1 
ATOM   2962 C CB   . LEU   B 1 188 ? -29.580 18.825  8.421  1.00 48.26  ? 403 LEU   A CB   1 
ATOM   2963 C CG   . LEU   B 1 188 ? -28.142 18.682  8.892  1.00 48.18  ? 403 LEU   A CG   1 
ATOM   2964 C CD1  . LEU   B 1 188 ? -27.655 20.035  9.369  1.00 47.39  ? 403 LEU   A CD1  1 
ATOM   2965 C CD2  . LEU   B 1 188 ? -28.066 17.627  9.994  1.00 49.36  ? 403 LEU   A CD2  1 
ATOM   2966 N N    . GLU   B 1 189 ? -31.951 18.099  6.266  1.00 51.36  ? 404 GLU   A N    1 
ATOM   2967 C CA   . GLU   B 1 189 ? -33.401 18.095  6.059  1.00 54.86  ? 404 GLU   A CA   1 
ATOM   2968 C C    . GLU   B 1 189 ? -34.019 16.688  6.156  1.00 55.95  ? 404 GLU   A C    1 
ATOM   2969 O O    . GLU   B 1 189 ? -35.248 16.578  6.225  1.00 59.17  ? 404 GLU   A O    1 
ATOM   2970 C CB   . GLU   B 1 189 ? -33.731 18.849  4.721  1.00 57.57  ? 404 GLU   A CB   1 
ATOM   2971 C CG   . GLU   B 1 189 ? -33.678 18.113  3.348  1.00 61.99  ? 404 GLU   A CG   1 
ATOM   2972 C CD   . GLU   B 1 189 ? -33.998 19.074  2.141  1.00 71.89  ? 404 GLU   A CD   1 
ATOM   2973 O OE1  . GLU   B 1 189 ? -34.739 20.069  2.369  1.00 74.74  ? 404 GLU   A OE1  1 
ATOM   2974 O OE2  . GLU   B 1 189 ? -33.525 18.846  0.972  1.00 66.67  ? 404 GLU   A OE2  1 
ATOM   2975 N N    . ASN   B 1 190 ? -33.208 15.621  6.242  1.00 56.15  ? 405 ASN   A N    1 
ATOM   2976 C CA   . ASN   B 1 190 ? -33.680 14.240  6.342  1.00 54.74  ? 405 ASN   A CA   1 
ATOM   2977 C C    . ASN   B 1 190 ? -33.409 13.606  7.700  1.00 53.64  ? 405 ASN   A C    1 
ATOM   2978 O O    . ASN   B 1 190 ? -33.528 12.381  7.846  1.00 50.59  ? 405 ASN   A O    1 
ATOM   2979 C CB   . ASN   B 1 190 ? -33.023 13.369  5.275  1.00 53.07  ? 405 ASN   A CB   1 
ATOM   2980 C CG   . ASN   B 1 190 ? -33.187 13.926  3.895  1.00 56.70  ? 405 ASN   A CG   1 
ATOM   2981 O OD1  . ASN   B 1 190 ? -34.305 13.982  3.366  1.00 56.52  ? 405 ASN   A OD1  1 
ATOM   2982 N ND2  . ASN   B 1 190 ? -32.070 14.314  3.277  1.00 51.42  ? 405 ASN   A ND2  1 
ATOM   2983 N N    . PHE   B 1 191 ? -33.009 14.388  8.683  1.00 48.63  ? 406 PHE   A N    1 
ATOM   2984 C CA   . PHE   B 1 191 ? -32.503 13.840  9.930  1.00 49.84  ? 406 PHE   A CA   1 
ATOM   2985 C C    . PHE   B 1 191 ? -33.282 14.489  11.065 1.00 49.84  ? 406 PHE   A C    1 
ATOM   2986 O O    . PHE   B 1 191 ? -33.344 15.722  11.146 1.00 51.14  ? 406 PHE   A O    1 
ATOM   2987 C CB   . PHE   B 1 191 ? -30.994 14.091  9.995  1.00 49.66  ? 406 PHE   A CB   1 
ATOM   2988 C CG   . PHE   B 1 191 ? -30.372 13.899  11.341 1.00 50.76  ? 406 PHE   A CG   1 
ATOM   2989 C CD1  . PHE   B 1 191 ? -30.474 14.876  12.324 1.00 50.83  ? 406 PHE   A CD1  1 
ATOM   2990 C CD2  . PHE   B 1 191 ? -29.628 12.754  11.605 1.00 53.26  ? 406 PHE   A CD2  1 
ATOM   2991 C CE1  . PHE   B 1 191 ? -29.872 14.710  13.568 1.00 51.40  ? 406 PHE   A CE1  1 
ATOM   2992 C CE2  . PHE   B 1 191 ? -29.021 12.566  12.854 1.00 56.25  ? 406 PHE   A CE2  1 
ATOM   2993 C CZ   . PHE   B 1 191 ? -29.146 13.555  13.838 1.00 56.27  ? 406 PHE   A CZ   1 
ATOM   2994 N N    . THR   B 1 192 ? -33.933 13.676  11.898 1.00 52.55  ? 407 THR   A N    1 
ATOM   2995 C CA   . THR   B 1 192 ? -34.750 14.225  12.979 1.00 55.58  ? 407 THR   A CA   1 
ATOM   2996 C C    . THR   B 1 192 ? -34.614 13.385  14.239 1.00 54.80  ? 407 THR   A C    1 
ATOM   2997 O O    . THR   B 1 192 ? -34.216 12.216  14.200 1.00 51.98  ? 407 THR   A O    1 
ATOM   2998 C CB   . THR   B 1 192 ? -36.234 14.326  12.602 1.00 55.51  ? 407 THR   A CB   1 
ATOM   2999 O OG1  . THR   B 1 192 ? -36.797 13.015  12.492 1.00 57.59  ? 407 THR   A OG1  1 
ATOM   3000 C CG2  . THR   B 1 192 ? -36.398 15.071  11.293 1.00 58.28  ? 407 THR   A CG2  1 
ATOM   3001 N N    . ILE   B 1 193 ? -34.953 14.002  15.370 1.00 51.55  ? 408 ILE   A N    1 
ATOM   3002 C CA   . ILE   B 1 193 ? -34.904 13.336  16.665 1.00 51.97  ? 408 ILE   A CA   1 
ATOM   3003 C C    . ILE   B 1 193 ? -36.224 13.545  17.396 1.00 51.38  ? 408 ILE   A C    1 
ATOM   3004 O O    . ILE   B 1 193 ? -36.727 14.672  17.481 1.00 51.18  ? 408 ILE   A O    1 
ATOM   3005 C CB   . ILE   B 1 193 ? -33.743 13.836  17.531 1.00 50.30  ? 408 ILE   A CB   1 
ATOM   3006 C CG1  . ILE   B 1 193 ? -32.421 13.544  16.843 1.00 49.72  ? 408 ILE   A CG1  1 
ATOM   3007 C CG2  . ILE   B 1 193 ? -33.786 13.110  18.857 1.00 52.73  ? 408 ILE   A CG2  1 
ATOM   3008 C CD1  . ILE   B 1 193 ? -31.248 14.151  17.515 1.00 54.18  ? 408 ILE   A CD1  1 
ATOM   3009 N N    . LEU   B 1 194 ? -36.778 12.461  17.921 1.00 53.18  ? 409 LEU   A N    1 
ATOM   3010 C CA   . LEU   B 1 194 ? -38.007 12.487  18.696 1.00 52.90  ? 409 LEU   A CA   1 
ATOM   3011 C C    . LEU   B 1 194 ? -37.661 12.041  20.100 1.00 53.20  ? 409 LEU   A C    1 
ATOM   3012 O O    . LEU   B 1 194 ? -36.946 11.049  20.274 1.00 52.32  ? 409 LEU   A O    1 
ATOM   3013 C CB   . LEU   B 1 194 ? -39.087 11.579  18.095 1.00 52.92  ? 409 LEU   A CB   1 
ATOM   3014 C CG   . LEU   B 1 194 ? -40.455 11.656  18.779 1.00 51.99  ? 409 LEU   A CG   1 
ATOM   3015 C CD1  . LEU   B 1 194 ? -41.120 12.978  18.433 1.00 51.80  ? 409 LEU   A CD1  1 
ATOM   3016 C CD2  . LEU   B 1 194 ? -41.358 10.488  18.399 1.00 56.97  ? 409 LEU   A CD2  1 
ATOM   3017 N N    . GLN   B 1 195 ? -38.132 12.790  21.093 1.00 50.73  ? 410 GLN   A N    1 
ATOM   3018 C CA   . GLN   B 1 195 ? -37.907 12.477  22.500 1.00 48.86  ? 410 GLN   A CA   1 
ATOM   3019 C C    . GLN   B 1 195 ? -39.234 12.365  23.225 1.00 49.73  ? 410 GLN   A C    1 
ATOM   3020 O O    . GLN   B 1 195 ? -40.002 13.333  23.273 1.00 48.68  ? 410 GLN   A O    1 
ATOM   3021 C CB   . GLN   B 1 195 ? -37.033 13.537  23.152 1.00 49.02  ? 410 GLN   A CB   1 
ATOM   3022 C CG   . GLN   B 1 195 ? -35.586 13.400  22.783 1.00 53.00  ? 410 GLN   A CG   1 
ATOM   3023 C CD   . GLN   B 1 195 ? -34.730 14.085  23.813 1.00 59.00  ? 410 GLN   A CD   1 
ATOM   3024 O OE1  . GLN   B 1 195 ? -33.504 13.956  23.818 1.00 57.65  ? 410 GLN   A OE1  1 
ATOM   3025 N NE2  . GLN   B 1 195 ? -35.369 14.916  24.633 1.00 61.31  ? 410 GLN   A NE2  1 
ATOM   3026 N N    . VAL   B 1 196 ? -39.489 11.197  23.797 1.00 50.64  ? 411 VAL   A N    1 
ATOM   3027 C CA   . VAL   B 1 196 ? -40.711 10.931  24.538 1.00 54.61  ? 411 VAL   A CA   1 
ATOM   3028 C C    . VAL   B 1 196 ? -40.332 10.698  25.999 1.00 54.05  ? 411 VAL   A C    1 
ATOM   3029 O O    . VAL   B 1 196 ? -39.670 9.703   26.325 1.00 49.64  ? 411 VAL   A O    1 
ATOM   3030 C CB   . VAL   B 1 196 ? -41.472 9.732   23.952 1.00 55.47  ? 411 VAL   A CB   1 
ATOM   3031 C CG1  . VAL   B 1 196 ? -42.895 9.665   24.520 1.00 51.39  ? 411 VAL   A CG1  1 
ATOM   3032 C CG2  . VAL   B 1 196 ? -41.468 9.808   22.391 1.00 52.56  ? 411 VAL   A CG2  1 
ATOM   3033 N N    . VAL   B 1 197 ? -40.719 11.634  26.871 1.00 54.13  ? 412 VAL   A N    1 
ATOM   3034 C CA   . VAL   B 1 197 ? -40.583 11.487  28.320 1.00 53.30  ? 412 VAL   A CA   1 
ATOM   3035 C C    . VAL   B 1 197 ? -41.933 11.071  28.874 1.00 54.47  ? 412 VAL   A C    1 
ATOM   3036 O O    . VAL   B 1 197 ? -42.935 11.777  28.702 1.00 53.40  ? 412 VAL   A O    1 
ATOM   3037 C CB   . VAL   B 1 197 ? -40.103 12.783  28.999 1.00 56.02  ? 412 VAL   A CB   1 
ATOM   3038 C CG1  . VAL   B 1 197 ? -39.801 12.524  30.502 1.00 53.51  ? 412 VAL   A CG1  1 
ATOM   3039 C CG2  . VAL   B 1 197 ? -38.898 13.383  28.283 1.00 51.33  ? 412 VAL   A CG2  1 
ATOM   3040 N N    . THR   B 1 198 ? -41.959 9.923   29.536 1.00 55.03  ? 413 THR   A N    1 
ATOM   3041 C CA   . THR   B 1 198 ? -43.168 9.398   30.137 1.00 56.56  ? 413 THR   A CA   1 
ATOM   3042 C C    . THR   B 1 198 ? -42.903 9.084   31.605 1.00 58.26  ? 413 THR   A C    1 
ATOM   3043 O O    . THR   B 1 198 ? -41.755 8.908   32.033 1.00 55.34  ? 413 THR   A O    1 
ATOM   3044 C CB   . THR   B 1 198 ? -43.639 8.135   29.433 1.00 57.27  ? 413 THR   A CB   1 
ATOM   3045 O OG1  . THR   B 1 198 ? -42.631 7.151   29.601 1.00 59.98  ? 413 THR   A OG1  1 
ATOM   3046 C CG2  . THR   B 1 198 ? -43.831 8.361   27.943 1.00 55.22  ? 413 THR   A CG2  1 
ATOM   3047 N N    . ASN   B 1 199 ? -43.995 9.039   32.371 1.00 62.50  ? 414 ASN   A N    1 
ATOM   3048 C CA   . ASN   B 1 199 ? -43.982 8.595   33.762 1.00 63.33  ? 414 ASN   A CA   1 
ATOM   3049 C C    . ASN   B 1 199 ? -43.698 7.096   33.806 1.00 63.50  ? 414 ASN   A C    1 
ATOM   3050 O O    . ASN   B 1 199 ? -44.550 6.283   33.428 1.00 64.29  ? 414 ASN   A O    1 
ATOM   3051 C CB   . ASN   B 1 199 ? -45.326 8.913   34.404 1.00 65.18  ? 414 ASN   A CB   1 
ATOM   3052 C CG   . ASN   B 1 199 ? -45.272 8.902   35.902 1.00 63.40  ? 414 ASN   A CG   1 
ATOM   3053 O OD1  . ASN   B 1 199 ? -44.525 8.145   36.504 1.00 64.76  ? 414 ASN   A OD1  1 
ATOM   3054 N ND2  . ASN   B 1 199 ? -46.055 9.774   36.518 1.00 63.73  ? 414 ASN   A ND2  1 
ATOM   3055 N N    . ARG   B 1 200 ? -42.496 6.725   34.249 1.00 59.88  ? 415 ARG   A N    1 
ATOM   3056 C CA   . ARG   B 1 200 ? -42.139 5.313   34.305 1.00 64.11  ? 415 ARG   A CA   1 
ATOM   3057 C C    . ARG   B 1 200 ? -43.206 4.517   35.043 1.00 67.06  ? 415 ARG   A C    1 
ATOM   3058 O O    . ARG   B 1 200 ? -43.705 3.506   34.533 1.00 66.68  ? 415 ARG   A O    1 
ATOM   3059 C CB   . ARG   B 1 200 ? -40.776 5.136   34.981 1.00 63.62  ? 415 ARG   A CB   1 
ATOM   3060 C CG   . ARG   B 1 200 ? -40.079 3.812   34.663 1.00 61.54  ? 415 ARG   A CG   1 
ATOM   3061 C CD   . ARG   B 1 200 ? -40.644 2.703   35.470 1.00 63.12  ? 415 ARG   A CD   1 
ATOM   3062 N NE   . ARG   B 1 200 ? -40.643 3.040   36.892 1.00 72.67  ? 415 ARG   A NE   1 
ATOM   3063 C CZ   . ARG   B 1 200 ? -39.650 2.781   37.735 1.00 70.23  ? 415 ARG   A CZ   1 
ATOM   3064 N NH1  . ARG   B 1 200 ? -38.573 2.106   37.353 1.00 67.18  ? 415 ARG   A NH1  1 
ATOM   3065 N NH2  . ARG   B 1 200 ? -39.740 3.211   38.992 1.00 69.52  ? 415 ARG   A NH2  1 
ATOM   3066 N N    . ASP   B 1 201 ? -43.595 4.989   36.237 1.00 61.51  ? 416 ASP   A N    1 
ATOM   3067 C CA   . ASP   B 1 201 ? -44.460 4.213   37.117 1.00 67.27  ? 416 ASP   A CA   1 
ATOM   3068 C C    . ASP   B 1 201 ? -45.873 4.090   36.586 1.00 68.93  ? 416 ASP   A C    1 
ATOM   3069 O O    . ASP   B 1 201 ? -46.614 3.206   37.030 1.00 72.94  ? 416 ASP   A O    1 
ATOM   3070 C CB   . ASP   B 1 201 ? -44.523 4.851   38.510 1.00 66.95  ? 416 ASP   A CB   1 
ATOM   3071 C CG   . ASP   B 1 201 ? -43.206 4.758   39.241 1.00 69.32  ? 416 ASP   A CG   1 
ATOM   3072 O OD1  . ASP   B 1 201 ? -42.411 3.856   38.894 1.00 69.74  ? 416 ASP   A OD1  1 
ATOM   3073 O OD2  . ASP   B 1 201 ? -42.941 5.603   40.127 1.00 69.67  ? 416 ASP   A OD2  1 
ATOM   3074 N N    . THR   B 1 202 ? -46.273 4.959   35.674 1.00 69.34  ? 417 THR   A N    1 
ATOM   3075 C CA   . THR   B 1 202 ? -47.675 5.073   35.342 1.00 68.70  ? 417 THR   A CA   1 
ATOM   3076 C C    . THR   B 1 202 ? -47.929 5.136   33.845 1.00 73.34  ? 417 THR   A C    1 
ATOM   3077 O O    . THR   B 1 202 ? -49.095 5.152   33.437 1.00 73.91  ? 417 THR   A O    1 
ATOM   3078 C CB   . THR   B 1 202 ? -48.264 6.307   36.026 1.00 69.37  ? 417 THR   A CB   1 
ATOM   3079 O OG1  . THR   B 1 202 ? -49.666 6.118   36.214 1.00 76.16  ? 417 THR   A OG1  1 
ATOM   3080 C CG2  . THR   B 1 202 ? -48.030 7.542   35.169 1.00 68.18  ? 417 THR   A CG2  1 
ATOM   3081 N N    . GLN   B 1 203 ? -46.879 5.159   33.020 1.00 78.44  ? 418 GLN   A N    1 
ATOM   3082 C CA   . GLN   B 1 203 ? -46.925 5.107   31.561 1.00 77.51  ? 418 GLN   A CA   1 
ATOM   3083 C C    . GLN   B 1 203 ? -47.493 6.362   30.918 1.00 77.75  ? 418 GLN   A C    1 
ATOM   3084 O O    . GLN   B 1 203 ? -47.579 6.416   29.687 1.00 78.94  ? 418 GLN   A O    1 
ATOM   3085 C CB   . GLN   B 1 203 ? -47.711 3.896   31.039 1.00 80.09  ? 418 GLN   A CB   1 
ATOM   3086 C CG   . GLN   B 1 203 ? -47.206 2.586   31.582 1.00 84.13  ? 418 GLN   A CG   1 
ATOM   3087 C CD   . GLN   B 1 203 ? -45.766 2.343   31.174 1.00 89.17  ? 418 GLN   A CD   1 
ATOM   3088 O OE1  . GLN   B 1 203 ? -44.851 2.469   31.993 1.00 91.71  ? 418 GLN   A OE1  1 
ATOM   3089 N NE2  . GLN   B 1 203 ? -45.551 2.038   29.894 1.00 89.60  ? 418 GLN   A NE2  1 
ATOM   3090 N N    . GLU   B 1 204 ? -47.881 7.369   31.697 1.00 68.13  ? 419 GLU   A N    1 
ATOM   3091 C CA   . GLU   B 1 204 ? -48.347 8.628   31.131 1.00 65.57  ? 419 GLU   A CA   1 
ATOM   3092 C C    . GLU   B 1 204 ? -47.232 9.330   30.361 1.00 60.20  ? 419 GLU   A C    1 
ATOM   3093 O O    . GLU   B 1 204 ? -46.064 9.309   30.760 1.00 56.64  ? 419 GLU   A O    1 
ATOM   3094 C CB   . GLU   B 1 204 ? -48.861 9.538   32.246 1.00 65.99  ? 419 GLU   A CB   1 
ATOM   3095 C CG   . GLU   B 1 204 ? -49.809 8.841   33.220 1.00 71.95  ? 419 GLU   A CG   1 
ATOM   3096 C CD   . GLU   B 1 204 ? -50.459 9.798   34.203 1.00 71.74  ? 419 GLU   A CD   1 
ATOM   3097 O OE1  . GLU   B 1 204 ? -49.699 10.467  34.947 1.00 70.76  ? 419 GLU   A OE1  1 
ATOM   3098 O OE2  . GLU   B 1 204 ? -51.712 9.885   34.233 1.00 70.66  ? 419 GLU   A OE2  1 
ATOM   3099 N N    . LEU   B 1 205 ? -47.609 9.971   29.256 1.00 59.34  ? 420 LEU   A N    1 
ATOM   3100 C CA   . LEU   B 1 205 ? -46.676 10.766  28.467 1.00 55.29  ? 420 LEU   A CA   1 
ATOM   3101 C C    . LEU   B 1 205 ? -46.565 12.162  29.054 1.00 51.02  ? 420 LEU   A C    1 
ATOM   3102 O O    . LEU   B 1 205 ? -47.581 12.816  29.295 1.00 52.75  ? 420 LEU   A O    1 
ATOM   3103 C CB   . LEU   B 1 205 ? -47.151 10.850  27.021 1.00 55.80  ? 420 LEU   A CB   1 
ATOM   3104 C CG   . LEU   B 1 205 ? -46.691 12.141  26.342 1.00 54.14  ? 420 LEU   A CG   1 
ATOM   3105 C CD1  . LEU   B 1 205 ? -45.187 12.107  26.187 1.00 53.39  ? 420 LEU   A CD1  1 
ATOM   3106 C CD2  . LEU   B 1 205 ? -47.373 12.338  25.004 1.00 58.08  ? 420 LEU   A CD2  1 
ATOM   3107 N N    . LEU   B 1 206 ? -45.336 12.629  29.273 1.00 52.08  ? 421 LEU   A N    1 
ATOM   3108 C CA   . LEU   B 1 206 ? -45.151 13.934  29.902 1.00 52.43  ? 421 LEU   A CA   1 
ATOM   3109 C C    . LEU   B 1 206 ? -44.753 14.976  28.868 1.00 55.26  ? 421 LEU   A C    1 
ATOM   3110 O O    . LEU   B 1 206 ? -45.553 15.853  28.534 1.00 56.66  ? 421 LEU   A O    1 
ATOM   3111 C CB   . LEU   B 1 206 ? -44.121 13.853  31.038 1.00 53.87  ? 421 LEU   A CB   1 
ATOM   3112 C CG   . LEU   B 1 206 ? -44.477 12.909  32.213 1.00 53.72  ? 421 LEU   A CG   1 
ATOM   3113 C CD1  . LEU   B 1 206 ? -43.338 12.801  33.237 1.00 53.16  ? 421 LEU   A CD1  1 
ATOM   3114 C CD2  . LEU   B 1 206 ? -45.779 13.328  32.888 1.00 51.02  ? 421 LEU   A CD2  1 
ATOM   3115 N N    . LEU   B 1 207 ? -43.526 14.900  28.364 1.00 55.12  ? 422 LEU   A N    1 
ATOM   3116 C CA   . LEU   B 1 207 ? -43.087 15.692  27.224 1.00 53.35  ? 422 LEU   A CA   1 
ATOM   3117 C C    . LEU   B 1 207 ? -42.863 14.783  26.025 1.00 52.57  ? 422 LEU   A C    1 
ATOM   3118 O O    . LEU   B 1 207 ? -42.438 13.629  26.167 1.00 48.24  ? 422 LEU   A O    1 
ATOM   3119 C CB   . LEU   B 1 207 ? -41.784 16.436  27.507 1.00 49.83  ? 422 LEU   A CB   1 
ATOM   3120 C CG   . LEU   B 1 207 ? -41.678 17.539  28.528 1.00 54.43  ? 422 LEU   A CG   1 
ATOM   3121 C CD1  . LEU   B 1 207 ? -40.207 17.897  28.667 1.00 54.52  ? 422 LEU   A CD1  1 
ATOM   3122 C CD2  . LEU   B 1 207 ? -42.505 18.742  28.095 1.00 56.68  ? 422 LEU   A CD2  1 
ATOM   3123 N N    . CYS   B 1 208 ? -43.142 15.328  24.838 1.00 53.07  ? 423 CYS   A N    1 
ATOM   3124 C CA   . CYS   B 1 208 ? -42.730 14.722  23.567 1.00 51.93  ? 423 CYS   A CA   1 
ATOM   3125 C C    . CYS   B 1 208 ? -42.279 15.858  22.660 1.00 49.50  ? 423 CYS   A C    1 
ATOM   3126 O O    . CYS   B 1 208 ? -43.101 16.695  22.277 1.00 48.31  ? 423 CYS   A O    1 
ATOM   3127 C CB   . CYS   B 1 208 ? -43.855 13.920  22.913 1.00 52.39  ? 423 CYS   A CB   1 
ATOM   3128 S SG   . CYS   B 1 208 ? -43.491 13.384  21.183 1.00 51.24  ? 423 CYS   A SG   1 
ATOM   3129 N N    . THR   B 1 209 ? -40.981 15.907  22.354 1.00 47.01  ? 424 THR   A N    1 
ATOM   3130 C CA   . THR   B 1 209 ? -40.392 16.913  21.479 1.00 48.52  ? 424 THR   A CA   1 
ATOM   3131 C C    . THR   B 1 209 ? -39.900 16.307  20.177 1.00 50.96  ? 424 THR   A C    1 
ATOM   3132 O O    . THR   B 1 209 ? -39.224 15.268  20.166 1.00 48.88  ? 424 THR   A O    1 
ATOM   3133 C CB   . THR   B 1 209 ? -39.198 17.607  22.122 1.00 50.87  ? 424 THR   A CB   1 
ATOM   3134 O OG1  . THR   B 1 209 ? -39.496 17.884  23.481 1.00 56.18  ? 424 THR   A OG1  1 
ATOM   3135 C CG2  . THR   B 1 209 ? -38.904 18.927  21.406 1.00 50.94  ? 424 THR   A CG2  1 
ATOM   3136 N N    . ALA   B 1 210 ? -40.200 16.994  19.087 1.00 51.66  ? 425 ALA   A N    1 
ATOM   3137 C CA   . ALA   B 1 210 ? -39.591 16.721  17.797 1.00 48.71  ? 425 ALA   A CA   1 
ATOM   3138 C C    . ALA   B 1 210 ? -38.479 17.737  17.566 1.00 50.27  ? 425 ALA   A C    1 
ATOM   3139 O O    . ALA   B 1 210 ? -38.685 18.943  17.783 1.00 50.28  ? 425 ALA   A O    1 
ATOM   3140 C CB   . ALA   B 1 210 ? -40.638 16.797  16.690 1.00 50.18  ? 425 ALA   A CB   1 
ATOM   3141 N N    . TYR   B 1 211 ? -37.299 17.249  17.170 1.00 47.19  ? 426 TYR   A N    1 
ATOM   3142 C CA   . TYR   B 1 211 ? -36.176 18.095  16.763 1.00 49.18  ? 426 TYR   A CA   1 
ATOM   3143 C C    . TYR   B 1 211 ? -35.946 18.009  15.259 1.00 49.78  ? 426 TYR   A C    1 
ATOM   3144 O O    . TYR   B 1 211 ? -35.804 16.908  14.715 1.00 50.23  ? 426 TYR   A O    1 
ATOM   3145 C CB   . TYR   B 1 211 ? -34.888 17.698  17.478 1.00 47.21  ? 426 TYR   A CB   1 
ATOM   3146 C CG   . TYR   B 1 211 ? -34.973 17.813  18.959 1.00 48.97  ? 426 TYR   A CG   1 
ATOM   3147 C CD1  . TYR   B 1 211 ? -34.926 19.045  19.580 1.00 51.75  ? 426 TYR   A CD1  1 
ATOM   3148 C CD2  . TYR   B 1 211 ? -35.119 16.700  19.740 1.00 51.31  ? 426 TYR   A CD2  1 
ATOM   3149 C CE1  . TYR   B 1 211 ? -35.008 19.152  20.953 1.00 53.87  ? 426 TYR   A CE1  1 
ATOM   3150 C CE2  . TYR   B 1 211 ? -35.214 16.801  21.110 1.00 54.20  ? 426 TYR   A CE2  1 
ATOM   3151 C CZ   . TYR   B 1 211 ? -35.152 18.025  21.708 1.00 51.77  ? 426 TYR   A CZ   1 
ATOM   3152 O OH   . TYR   B 1 211 ? -35.244 18.120  23.077 1.00 56.35  ? 426 TYR   A OH   1 
ATOM   3153 N N    . VAL   B 1 212 ? -35.884 19.175  14.600 1.00 50.40  ? 427 VAL   A N    1 
ATOM   3154 C CA   . VAL   B 1 212 ? -35.442 19.308  13.217 1.00 51.13  ? 427 VAL   A CA   1 
ATOM   3155 C C    . VAL   B 1 212 ? -34.237 20.243  13.194 1.00 51.97  ? 427 VAL   A C    1 
ATOM   3156 O O    . VAL   B 1 212 ? -34.030 21.042  14.111 1.00 50.57  ? 427 VAL   A O    1 
ATOM   3157 C CB   . VAL   B 1 212 ? -36.553 19.838  12.291 1.00 53.40  ? 427 VAL   A CB   1 
ATOM   3158 C CG1  . VAL   B 1 212 ? -37.705 18.844  12.226 1.00 54.38  ? 427 VAL   A CG1  1 
ATOM   3159 C CG2  . VAL   B 1 212 ? -37.025 21.224  12.749 1.00 50.06  ? 427 VAL   A CG2  1 
ATOM   3160 N N    . PHE   B 1 213 ? -33.448 20.160  12.116 1.00 52.00  ? 428 PHE   A N    1 
ATOM   3161 C CA   . PHE   B 1 213 ? -32.100 20.710  12.154 1.00 51.93  ? 428 PHE   A CA   1 
ATOM   3162 C C    . PHE   B 1 213 ? -31.728 21.478  10.894 1.00 50.22  ? 428 PHE   A C    1 
ATOM   3163 O O    . PHE   B 1 213 ? -32.106 21.111  9.780  1.00 52.12  ? 428 PHE   A O    1 
ATOM   3164 C CB   . PHE   B 1 213 ? -31.062 19.610  12.385 1.00 50.35  ? 428 PHE   A CB   1 
ATOM   3165 C CG   . PHE   B 1 213 ? -31.163 18.963  13.735 1.00 49.31  ? 428 PHE   A CG   1 
ATOM   3166 C CD1  . PHE   B 1 213 ? -30.493 19.504  14.827 1.00 49.86  ? 428 PHE   A CD1  1 
ATOM   3167 C CD2  . PHE   B 1 213 ? -31.908 17.798  13.913 1.00 50.48  ? 428 PHE   A CD2  1 
ATOM   3168 C CE1  . PHE   B 1 213 ? -30.586 18.917  16.081 1.00 50.64  ? 428 PHE   A CE1  1 
ATOM   3169 C CE2  . PHE   B 1 213 ? -31.998 17.197  15.189 1.00 50.86  ? 428 PHE   A CE2  1 
ATOM   3170 C CZ   . PHE   B 1 213 ? -31.338 17.760  16.261 1.00 47.86  ? 428 PHE   A CZ   1 
ATOM   3171 N N    . GLU   B 1 214 ? -31.002 22.570  11.109 1.00 49.92  ? 429 GLU   A N    1 
ATOM   3172 C CA   . GLU   B 1 214 ? -30.213 23.261  10.109 1.00 49.66  ? 429 GLU   A CA   1 
ATOM   3173 C C    . GLU   B 1 214 ? -28.897 23.605  10.766 1.00 49.58  ? 429 GLU   A C    1 
ATOM   3174 O O    . GLU   B 1 214 ? -28.627 23.216  11.903 1.00 53.86  ? 429 GLU   A O    1 
ATOM   3175 C CB   . GLU   B 1 214 ? -30.905 24.518  9.579  1.00 49.91  ? 429 GLU   A CB   1 
ATOM   3176 C CG   . GLU   B 1 214 ? -32.147 24.200  8.809  1.00 51.69  ? 429 GLU   A CG   1 
ATOM   3177 C CD   . GLU   B 1 214 ? -32.652 25.380  8.042  1.00 56.09  ? 429 GLU   A CD   1 
ATOM   3178 O OE1  . GLU   B 1 214 ? -31.882 26.349  7.874  1.00 55.62  ? 429 GLU   A OE1  1 
ATOM   3179 O OE2  . GLU   B 1 214 ? -33.816 25.340  7.593  1.00 62.95  ? 429 GLU   A OE2  1 
ATOM   3180 N N    . VAL   B 1 215 ? -28.093 24.375  10.077 1.00 49.57  ? 430 VAL   A N    1 
ATOM   3181 C CA   . VAL   B 1 215 ? -26.748 24.670  10.529 1.00 52.69  ? 430 VAL   A CA   1 
ATOM   3182 C C    . VAL   B 1 215 ? -26.637 26.177  10.640 1.00 56.41  ? 430 VAL   A C    1 
ATOM   3183 O O    . VAL   B 1 215 ? -27.105 26.914  9.764  1.00 56.95  ? 430 VAL   A O    1 
ATOM   3184 C CB   . VAL   B 1 215 ? -25.689 24.079  9.568  1.00 53.55  ? 430 VAL   A CB   1 
ATOM   3185 C CG1  . VAL   B 1 215 ? -24.345 24.734  9.756  1.00 55.17  ? 430 VAL   A CG1  1 
ATOM   3186 C CG2  . VAL   B 1 215 ? -25.572 22.589  9.804  1.00 49.38  ? 430 VAL   A CG2  1 
ATOM   3187 N N    . SER   B 1 216 ? -26.064 26.630  11.741 1.00 56.55  ? 431 SER   A N    1 
ATOM   3188 C CA   . SER   B 1 216 ? -25.752 28.030  11.896 1.00 59.91  ? 431 SER   A CA   1 
ATOM   3189 C C    . SER   B 1 216 ? -24.350 28.295  11.367 1.00 63.06  ? 431 SER   A C    1 
ATOM   3190 O O    . SER   B 1 216 ? -23.659 27.397  10.884 1.00 64.64  ? 431 SER   A O    1 
ATOM   3191 C CB   . SER   B 1 216 ? -25.861 28.448  13.351 1.00 57.21  ? 431 SER   A CB   1 
ATOM   3192 O OG   . SER   B 1 216 ? -25.590 29.836  13.451 1.00 65.24  ? 431 SER   A OG   1 
ATOM   3193 N N    . THR   B 1 217 ? -23.916 29.539  11.474 1.00 68.05  ? 432 THR   A N    1 
ATOM   3194 C CA   . THR   B 1 217 ? -22.548 29.889  11.155 1.00 71.73  ? 432 THR   A CA   1 
ATOM   3195 C C    . THR   B 1 217 ? -21.758 30.096  12.444 1.00 75.77  ? 432 THR   A C    1 
ATOM   3196 O O    . THR   B 1 217 ? -22.298 30.096  13.552 1.00 74.71  ? 432 THR   A O    1 
ATOM   3197 C CB   . THR   B 1 217 ? -22.508 31.137  10.272 1.00 72.11  ? 432 THR   A CB   1 
ATOM   3198 O OG1  . THR   B 1 217 ? -22.811 32.278  11.071 1.00 78.06  ? 432 THR   A OG1  1 
ATOM   3199 C CG2  . THR   B 1 217 ? -23.543 31.031  9.157  1.00 67.76  ? 432 THR   A CG2  1 
ATOM   3200 N N    . SER   B 1 218 ? -20.446 30.246  12.279 1.00 83.95  ? 433 SER   A N    1 
ATOM   3201 C CA   . SER   B 1 218 ? -19.563 30.444  13.422 1.00 82.78  ? 433 SER   A CA   1 
ATOM   3202 C C    . SER   B 1 218 ? -19.940 31.709  14.191 1.00 83.02  ? 433 SER   A C    1 
ATOM   3203 O O    . SER   B 1 218 ? -20.117 31.680  15.418 1.00 80.31  ? 433 SER   A O    1 
ATOM   3204 C CB   . SER   B 1 218 ? -18.120 30.508  12.925 1.00 83.98  ? 433 SER   A CB   1 
ATOM   3205 O OG   . SER   B 1 218 ? -18.081 31.155  11.658 1.00 80.77  ? 433 SER   A OG   1 
ATOM   3206 N N    . GLU   B 1 219 ? -20.057 32.833  13.486 1.00 81.54  ? 434 GLU   A N    1 
ATOM   3207 C CA   . GLU   B 1 219 ? -20.612 34.031  14.088 1.00 83.66  ? 434 GLU   A CA   1 
ATOM   3208 C C    . GLU   B 1 219 ? -22.130 33.904  14.182 1.00 83.00  ? 434 GLU   A C    1 
ATOM   3209 O O    . GLU   B 1 219 ? -22.797 33.471  13.238 1.00 81.93  ? 434 GLU   A O    1 
ATOM   3210 C CB   . GLU   B 1 219 ? -20.183 35.279  13.306 1.00 84.32  ? 434 GLU   A CB   1 
ATOM   3211 C CG   . GLU   B 1 219 ? -21.173 35.908  12.333 1.00 83.41  ? 434 GLU   A CG   1 
ATOM   3212 C CD   . GLU   B 1 219 ? -20.635 37.234  11.794 1.00 88.78  ? 434 GLU   A CD   1 
ATOM   3213 O OE1  . GLU   B 1 219 ? -20.284 38.087  12.633 1.00 92.83  ? 434 GLU   A OE1  1 
ATOM   3214 O OE2  . GLU   B 1 219 ? -20.522 37.424  10.555 1.00 89.99  ? 434 GLU   A OE2  1 
ATOM   3215 N N    . ARG   B 1 220 ? -22.665 34.258  15.341 1.00 82.05  ? 435 ARG   A N    1 
ATOM   3216 C CA   . ARG   B 1 220 ? -24.048 34.087  15.779 1.00 81.28  ? 435 ARG   A CA   1 
ATOM   3217 C C    . ARG   B 1 220 ? -24.357 32.667  16.281 1.00 78.24  ? 435 ARG   A C    1 
ATOM   3218 O O    . ARG   B 1 220 ? -25.400 32.471  16.905 1.00 78.41  ? 435 ARG   A O    1 
ATOM   3219 C CB   . ARG   B 1 220 ? -25.084 34.509  14.716 1.00 76.75  ? 435 ARG   A CB   1 
ATOM   3220 C CG   . ARG   B 1 220 ? -25.586 33.518  13.704 1.00 72.33  ? 435 ARG   A CG   1 
ATOM   3221 C CD   . ARG   B 1 220 ? -26.911 34.120  13.243 1.00 73.75  ? 435 ARG   A CD   1 
ATOM   3222 N NE   . ARG   B 1 220 ? -27.218 34.058  11.818 1.00 76.96  ? 435 ARG   A NE   1 
ATOM   3223 C CZ   . ARG   B 1 220 ? -28.377 34.464  11.304 1.00 77.50  ? 435 ARG   A CZ   1 
ATOM   3224 N NH1  . ARG   B 1 220 ? -29.373 34.882  12.085 1.00 73.78  ? 435 ARG   A NH1  1 
ATOM   3225 N NH2  . ARG   B 1 220 ? -28.536 34.471  9.978  1.00 74.17  ? 435 ARG   A NH2  1 
ATOM   3226 N N    . GLY   B 1 221 ? -23.484 31.692  16.079 1.00 73.56  ? 436 GLY   A N    1 
ATOM   3227 C CA   . GLY   B 1 221 ? -23.580 30.444  16.815 1.00 70.60  ? 436 GLY   A CA   1 
ATOM   3228 C C    . GLY   B 1 221 ? -24.951 29.803  16.926 1.00 65.31  ? 436 GLY   A C    1 
ATOM   3229 O O    . GLY   B 1 221 ? -25.933 30.280  16.341 1.00 62.81  ? 436 GLY   A O    1 
ATOM   3230 N N    . ALA   B 1 222 ? -25.008 28.711  17.697 1.00 63.11  ? 437 ALA   A N    1 
ATOM   3231 C CA   . ALA   B 1 222 ? -26.224 27.924  17.876 1.00 59.50  ? 437 ALA   A CA   1 
ATOM   3232 C C    . ALA   B 1 222 ? -27.437 28.787  18.185 1.00 57.05  ? 437 ALA   A C    1 
ATOM   3233 O O    . ALA   B 1 222 ? -27.356 29.769  18.930 1.00 63.47  ? 437 ALA   A O    1 
ATOM   3234 C CB   . ALA   B 1 222 ? -26.025 26.912  19.006 1.00 56.44  ? 437 ALA   A CB   1 
ATOM   3235 N N    . GLN   B 1 223 ? -28.567 28.424  17.587 1.00 49.55  ? 438 GLN   A N    1 
ATOM   3236 C CA   . GLN   B 1 223 ? -29.844 29.005  17.965 1.00 54.42  ? 438 GLN   A CA   1 
ATOM   3237 C C    . GLN   B 1 223 ? -30.913 27.923  17.893 1.00 55.55  ? 438 GLN   A C    1 
ATOM   3238 O O    . GLN   B 1 223 ? -30.715 26.851  17.311 1.00 52.56  ? 438 GLN   A O    1 
ATOM   3239 C CB   . GLN   B 1 223 ? -30.263 30.204  17.098 1.00 59.25  ? 438 GLN   A CB   1 
ATOM   3240 C CG   . GLN   B 1 223 ? -31.651 30.709  17.534 1.00 63.67  ? 438 GLN   A CG   1 
ATOM   3241 C CD   . GLN   B 1 223 ? -31.611 31.720  18.685 1.00 70.72  ? 438 GLN   A CD   1 
ATOM   3242 O OE1  . GLN   B 1 223 ? -30.714 32.595  18.740 1.00 75.48  ? 438 GLN   A OE1  1 
ATOM   3243 N NE2  . GLN   B 1 223 ? -32.500 31.527  19.675 1.00 64.97  ? 438 GLN   A NE2  1 
ATOM   3244 N N    . HIS   B 1 224 ? -32.050 28.195  18.525 1.00 56.78  ? 439 HIS   A N    1 
ATOM   3245 C CA   . HIS   B 1 224 ? -33.170 27.272  18.484 1.00 57.40  ? 439 HIS   A CA   1 
ATOM   3246 C C    . HIS   B 1 224 ? -34.434 28.097  18.443 1.00 54.14  ? 439 HIS   A C    1 
ATOM   3247 O O    . HIS   B 1 224 ? -34.408 29.316  18.587 1.00 56.86  ? 439 HIS   A O    1 
ATOM   3248 C CB   . HIS   B 1 224 ? -33.154 26.308  19.685 1.00 58.04  ? 439 HIS   A CB   1 
ATOM   3249 C CG   . HIS   B 1 224 ? -33.190 27.008  20.997 1.00 57.72  ? 439 HIS   A CG   1 
ATOM   3250 N ND1  . HIS   B 1 224 ? -34.372 27.332  21.634 1.00 59.82  ? 439 HIS   A ND1  1 
ATOM   3251 C CD2  . HIS   B 1 224 ? -32.195 27.524  21.759 1.00 59.96  ? 439 HIS   A CD2  1 
ATOM   3252 C CE1  . HIS   B 1 224 ? -34.102 27.985  22.752 1.00 59.02  ? 439 HIS   A CE1  1 
ATOM   3253 N NE2  . HIS   B 1 224 ? -32.790 28.122  22.848 1.00 62.21  ? 439 HIS   A NE2  1 
ATOM   3254 N N    . HIS   B 1 225 ? -35.541 27.429  18.181 1.00 55.97  ? 440 HIS   A N    1 
ATOM   3255 C CA   . HIS   B 1 225 ? -36.834 28.099  18.175 1.00 60.36  ? 440 HIS   A CA   1 
ATOM   3256 C C    . HIS   B 1 225 ? -37.840 27.035  18.569 1.00 57.90  ? 440 HIS   A C    1 
ATOM   3257 O O    . HIS   B 1 225 ? -37.989 26.024  17.875 1.00 56.15  ? 440 HIS   A O    1 
ATOM   3258 C CB   . HIS   B 1 225 ? -37.147 28.731  16.805 1.00 60.20  ? 440 HIS   A CB   1 
ATOM   3259 C CG   . HIS   B 1 225 ? -38.320 29.660  16.809 1.00 63.69  ? 440 HIS   A CG   1 
ATOM   3260 N ND1  . HIS   B 1 225 ? -38.525 30.602  15.820 1.00 72.29  ? 440 HIS   A ND1  1 
ATOM   3261 C CD2  . HIS   B 1 225 ? -39.378 29.762  17.651 1.00 64.92  ? 440 HIS   A CD2  1 
ATOM   3262 C CE1  . HIS   B 1 225 ? -39.633 31.280  16.082 1.00 74.58  ? 440 HIS   A CE1  1 
ATOM   3263 N NE2  . HIS   B 1 225 ? -40.171 30.788  17.187 1.00 71.89  ? 440 HIS   A NE2  1 
ATOM   3264 N N    . ILE   B 1 226 ? -38.467 27.243  19.709 1.00 58.53  ? 441 ILE   A N    1 
ATOM   3265 C CA   . ILE   B 1 226 ? -39.330 26.250  20.324 1.00 58.53  ? 441 ILE   A CA   1 
ATOM   3266 C C    . ILE   B 1 226 ? -40.742 26.537  19.864 1.00 59.84  ? 441 ILE   A C    1 
ATOM   3267 O O    . ILE   B 1 226 ? -41.192 27.685  19.925 1.00 63.51  ? 441 ILE   A O    1 
ATOM   3268 C CB   . ILE   B 1 226 ? -39.213 26.309  21.857 1.00 54.47  ? 441 ILE   A CB   1 
ATOM   3269 C CG1  . ILE   B 1 226 ? -37.780 25.950  22.260 1.00 55.23  ? 441 ILE   A CG1  1 
ATOM   3270 C CG2  . ILE   B 1 226 ? -40.255 25.421  22.506 1.00 54.93  ? 441 ILE   A CG2  1 
ATOM   3271 C CD1  . ILE   B 1 226 ? -37.508 25.927  23.717 1.00 54.88  ? 441 ILE   A CD1  1 
ATOM   3272 N N    . TYR   B 1 227 ? -41.431 25.516  19.372 1.00 59.72  ? 442 TYR   A N    1 
ATOM   3273 C CA   . TYR   B 1 227 ? -42.810 25.691  18.951 1.00 62.22  ? 442 TYR   A CA   1 
ATOM   3274 C C    . TYR   B 1 227 ? -43.714 24.716  19.686 1.00 63.26  ? 442 TYR   A C    1 
ATOM   3275 O O    . TYR   B 1 227 ? -43.267 23.756  20.322 1.00 60.93  ? 442 TYR   A O    1 
ATOM   3276 C CB   . TYR   B 1 227 ? -42.965 25.490  17.442 1.00 63.93  ? 442 TYR   A CB   1 
ATOM   3277 C CG   . TYR   B 1 227 ? -42.112 26.389  16.588 1.00 63.67  ? 442 TYR   A CG   1 
ATOM   3278 C CD1  . TYR   B 1 227 ? -40.788 26.069  16.297 1.00 60.80  ? 442 TYR   A CD1  1 
ATOM   3279 C CD2  . TYR   B 1 227 ? -42.636 27.548  16.052 1.00 68.11  ? 442 TYR   A CD2  1 
ATOM   3280 C CE1  . TYR   B 1 227 ? -40.012 26.908  15.490 1.00 65.37  ? 442 TYR   A CE1  1 
ATOM   3281 C CE2  . TYR   B 1 227 ? -41.882 28.374  15.251 1.00 69.43  ? 442 TYR   A CE2  1 
ATOM   3282 C CZ   . TYR   B 1 227 ? -40.577 28.057  14.970 1.00 66.96  ? 442 TYR   A CZ   1 
ATOM   3283 O OH   . TYR   B 1 227 ? -39.853 28.917  14.182 1.00 69.85  ? 442 TYR   A OH   1 
ATOM   3284 N N    . ARG   B 1 228 ? -45.004 24.967  19.563 1.00 66.06  ? 443 ARG   A N    1 
ATOM   3285 C CA   . ARG   B 1 228 ? -46.034 24.083  20.080 1.00 70.46  ? 443 ARG   A CA   1 
ATOM   3286 C C    . ARG   B 1 228 ? -46.613 23.282  18.923 1.00 70.06  ? 443 ARG   A C    1 
ATOM   3287 O O    . ARG   B 1 228 ? -46.771 23.805  17.816 1.00 70.24  ? 443 ARG   A O    1 
ATOM   3288 C CB   . ARG   B 1 228 ? -47.134 24.893  20.760 1.00 74.32  ? 443 ARG   A CB   1 
ATOM   3289 C CG   . ARG   B 1 228 ? -48.184 24.080  21.455 1.00 78.43  ? 443 ARG   A CG   1 
ATOM   3290 C CD   . ARG   B 1 228 ? -48.627 24.831  22.685 1.00 85.37  ? 443 ARG   A CD   1 
ATOM   3291 N NE   . ARG   B 1 228 ? -49.061 26.175  22.320 1.00 89.20  ? 443 ARG   A NE   1 
ATOM   3292 C CZ   . ARG   B 1 228 ? -50.066 26.435  21.493 1.00 93.33  ? 443 ARG   A CZ   1 
ATOM   3293 N NH1  . ARG   B 1 228 ? -50.807 25.465  20.981 1.00 95.03  ? 443 ARG   A NH1  1 
ATOM   3294 N NH2  . ARG   B 1 228 ? -50.334 27.701  21.172 1.00 90.38  ? 443 ARG   A NH2  1 
ATOM   3295 N N    . LEU   B 1 229 ? -46.926 22.016  19.175 1.00 66.75  ? 444 LEU   A N    1 
ATOM   3296 C CA   . LEU   B 1 229 ? -47.525 21.163  18.159 1.00 67.96  ? 444 LEU   A CA   1 
ATOM   3297 C C    . LEU   B 1 229 ? -49.034 21.123  18.363 1.00 69.35  ? 444 LEU   A C    1 
ATOM   3298 O O    . LEU   B 1 229 ? -49.512 20.733  19.432 1.00 71.78  ? 444 LEU   A O    1 
ATOM   3299 C CB   . LEU   B 1 229 ? -46.912 19.760  18.185 1.00 67.66  ? 444 LEU   A CB   1 
ATOM   3300 C CG   . LEU   B 1 229 ? -45.559 19.622  17.452 1.00 65.07  ? 444 LEU   A CG   1 
ATOM   3301 C CD1  . LEU   B 1 229 ? -44.929 18.253  17.648 1.00 60.23  ? 444 LEU   A CD1  1 
ATOM   3302 C CD2  . LEU   B 1 229 ? -45.712 19.925  15.965 1.00 64.07  ? 444 LEU   A CD2  1 
ATOM   3303 N N    . VAL   B 1 230 ? -49.777 21.550  17.344 1.00 77.37  ? 445 VAL   A N    1 
ATOM   3304 C CA   . VAL   B 1 230 ? -51.230 21.607  17.367 1.00 79.05  ? 445 VAL   A CA   1 
ATOM   3305 C C    . VAL   B 1 230 ? -51.759 20.930  16.107 1.00 85.23  ? 445 VAL   A C    1 
ATOM   3306 O O    . VAL   B 1 230 ? -50.994 20.521  15.233 1.00 85.51  ? 445 VAL   A O    1 
ATOM   3307 C CB   . VAL   B 1 230 ? -51.757 23.056  17.471 1.00 79.76  ? 445 VAL   A CB   1 
ATOM   3308 C CG1  . VAL   B 1 230 ? -51.089 23.779  18.624 1.00 80.93  ? 445 VAL   A CG1  1 
ATOM   3309 C CG2  . VAL   B 1 230 ? -51.531 23.809  16.174 1.00 78.15  ? 445 VAL   A CG2  1 
ATOM   3310 N N    . ARG   B 1 231 ? -53.085 20.828  16.011 1.00 91.73  ? 446 ARG   A N    1 
ATOM   3311 C CA   . ARG   B 1 231 ? -53.696 20.257  14.811 1.00 96.19  ? 446 ARG   A CA   1 
ATOM   3312 C C    . ARG   B 1 231 ? -55.118 20.762  14.561 1.00 95.10  ? 446 ARG   A C    1 
ATOM   3313 O O    . ARG   B 1 231 ? -55.730 21.389  15.425 1.00 92.24  ? 446 ARG   A O    1 
ATOM   3314 C CB   . ARG   B 1 231 ? -53.699 18.734  14.901 1.00 97.61  ? 446 ARG   A CB   1 
ATOM   3315 C CG   . ARG   B 1 231 ? -54.724 18.160  15.857 1.00 99.95  ? 446 ARG   A CG   1 
ATOM   3316 C CD   . ARG   B 1 231 ? -55.379 16.972  15.196 1.00 104.47 ? 446 ARG   A CD   1 
ATOM   3317 N NE   . ARG   B 1 231 ? -54.510 15.807  15.296 1.00 108.16 ? 446 ARG   A NE   1 
ATOM   3318 C CZ   . ARG   B 1 231 ? -54.360 14.903  14.339 1.00 107.67 ? 446 ARG   A CZ   1 
ATOM   3319 N NH1  . ARG   B 1 231 ? -54.980 15.020  13.174 1.00 108.34 ? 446 ARG   A NH1  1 
ATOM   3320 N NH2  . ARG   B 1 231 ? -53.547 13.869  14.546 1.00 108.32 ? 446 ARG   A NH2  1 
HETATM 3321 C C10  . A1H3Y C 2 .   ? -32.062 -11.222 17.331 1.00 51.74  ? 501 A1H3Y B C10  1 
HETATM 3322 C C12  . A1H3Y C 2 .   ? -33.470 -11.568 15.437 1.00 55.05  ? 501 A1H3Y B C12  1 
HETATM 3323 C C13  . A1H3Y C 2 .   ? -33.221 -12.408 14.165 1.00 53.57  ? 501 A1H3Y B C13  1 
HETATM 3324 C C14  . A1H3Y C 2 .   ? -32.613 -11.835 13.045 1.00 55.18  ? 501 A1H3Y B C14  1 
HETATM 3325 C C02  . A1H3Y C 2 .   ? -33.092 -5.364  19.060 1.00 62.11  ? 501 A1H3Y B C02  1 
HETATM 3326 C C03  . A1H3Y C 2 .   ? -33.305 -6.858  18.819 1.00 61.55  ? 501 A1H3Y B C03  1 
HETATM 3327 C C04  . A1H3Y C 2 .   ? -32.035 -7.710  18.970 1.00 59.72  ? 501 A1H3Y B C04  1 
HETATM 3328 C C05  . A1H3Y C 2 .   ? -30.889 -7.318  19.649 1.00 59.44  ? 501 A1H3Y B C05  1 
HETATM 3329 C C07  . A1H3Y C 2 .   ? -30.534 -9.389  18.860 1.00 54.08  ? 501 A1H3Y B C07  1 
HETATM 3330 C C08  . A1H3Y C 2 .   ? -31.811 -9.038  18.467 1.00 57.15  ? 501 A1H3Y B C08  1 
HETATM 3331 C C09  . A1H3Y C 2 .   ? -32.585 -9.970  17.698 1.00 54.72  ? 501 A1H3Y B C09  1 
HETATM 3332 C C15  . A1H3Y C 2 .   ? -32.377 -12.587 11.883 1.00 53.96  ? 501 A1H3Y B C15  1 
HETATM 3333 C C16  . A1H3Y C 2 .   ? -32.762 -13.922 11.819 1.00 49.30  ? 501 A1H3Y B C16  1 
HETATM 3334 C C17  . A1H3Y C 2 .   ? -33.377 -14.486 12.933 1.00 54.03  ? 501 A1H3Y B C17  1 
HETATM 3335 C C18  . A1H3Y C 2 .   ? -33.606 -13.739 14.095 1.00 49.40  ? 501 A1H3Y B C18  1 
HETATM 3336 C C19  . A1H3Y C 2 .   ? -30.758 -11.570 17.738 1.00 51.70  ? 501 A1H3Y B C19  1 
HETATM 3337 C C20  . A1H3Y C 2 .   ? -29.996 -10.663 18.498 1.00 52.05  ? 501 A1H3Y B C20  1 
HETATM 3338 N N06  . A1H3Y C 2 .   ? -30.003 -8.325  19.564 1.00 58.48  ? 501 A1H3Y B N06  1 
HETATM 3339 O O01  . A1H3Y C 2 .   ? -34.337 -4.748  18.871 1.00 64.47  ? 501 A1H3Y B O01  1 
HETATM 3340 O O11  . A1H3Y C 2 .   ? -32.836 -12.131 16.573 1.00 52.35  ? 501 A1H3Y B O11  1 
HETATM 3341 H H121 . A1H3Y C 2 .   ? -34.425 -11.524 15.601 1.00 66.81  ? 501 A1H3Y B H121 1 
HETATM 3342 H H122 . A1H3Y C 2 .   ? -33.121 -10.674 15.295 1.00 66.81  ? 501 A1H3Y B H122 1 
HETATM 3343 H H141 . A1H3Y C 2 .   ? -32.359 -10.941 13.069 1.00 66.98  ? 501 A1H3Y B H141 1 
HETATM 3344 H H021 . A1H3Y C 2 .   ? -32.778 -5.213  19.965 1.00 75.29  ? 501 A1H3Y B H021 1 
HETATM 3345 H H022 . A1H3Y C 2 .   ? -32.446 -5.013  18.427 1.00 75.29  ? 501 A1H3Y B H022 1 
HETATM 3346 H H031 . A1H3Y C 2 .   ? -33.966 -7.179  19.453 1.00 74.62  ? 501 A1H3Y B H031 1 
HETATM 3347 H H032 . A1H3Y C 2 .   ? -33.649 -6.977  17.920 1.00 74.62  ? 501 A1H3Y B H032 1 
HETATM 3348 H H051 . A1H3Y C 2 .   ? -30.759 -6.506  20.084 1.00 72.09  ? 501 A1H3Y B H051 1 
HETATM 3349 H H091 . A1H3Y C 2 .   ? -33.448 -9.741  17.438 1.00 66.42  ? 501 A1H3Y B H091 1 
HETATM 3350 H H151 . A1H3Y C 2 .   ? -31.962 -12.191 11.152 1.00 65.52  ? 501 A1H3Y B H151 1 
HETATM 3351 H H161 . A1H3Y C 2 .   ? -32.612 -14.425 11.051 1.00 59.92  ? 501 A1H3Y B H161 1 
HETATM 3352 H H171 . A1H3Y C 2 .   ? -33.642 -15.377 12.905 1.00 65.60  ? 501 A1H3Y B H171 1 
HETATM 3353 H H181 . A1H3Y C 2 .   ? -34.021 -14.138 14.826 1.00 60.04  ? 501 A1H3Y B H181 1 
HETATM 3354 H H191 . A1H3Y C 2 .   ? -30.403 -12.397 17.506 1.00 62.80  ? 501 A1H3Y B H191 1 
HETATM 3355 H H201 . A1H3Y C 2 .   ? -29.136 -10.894 18.766 1.00 63.22  ? 501 A1H3Y B H201 1 
HETATM 3356 H H061 . A1H3Y C 2 .   ? -29.213 -8.310  19.901 1.00 70.93  ? 501 A1H3Y B H061 1 
HETATM 3357 H H011 . A1H3Y C 2 .   ? -34.559 -4.336  19.583 1.00 78.12  ? 501 A1H3Y B H011 1 
HETATM 3358 C C10  . A1H3Y D 2 .   ? -29.038 15.996  19.598 1.00 56.40  ? 501 A1H3Y A C10  1 
HETATM 3359 C C12  . A1H3Y D 2 .   ? -27.124 16.139  18.182 1.00 56.73  ? 501 A1H3Y A C12  1 
HETATM 3360 C C13  . A1H3Y D 2 .   ? -27.071 16.796  16.795 1.00 54.77  ? 501 A1H3Y A C13  1 
HETATM 3361 C C14  . A1H3Y D 2 .   ? -26.634 18.103  16.653 1.00 53.87  ? 501 A1H3Y A C14  1 
HETATM 3362 C C02  . A1H3Y D 2 .   ? -28.718 10.174  21.741 1.00 62.18  ? 501 A1H3Y A C02  1 
HETATM 3363 C C03  . A1H3Y D 2 .   ? -28.400 11.632  21.400 1.00 63.61  ? 501 A1H3Y A C03  1 
HETATM 3364 C C04  . A1H3Y D 2 .   ? -29.602 12.585  21.343 1.00 61.94  ? 501 A1H3Y A C04  1 
HETATM 3365 C C05  . A1H3Y D 2 .   ? -30.860 12.332  21.876 1.00 62.48  ? 501 A1H3Y A C05  1 
HETATM 3366 C C07  . A1H3Y D 2 .   ? -30.913 14.381  20.954 1.00 59.78  ? 501 A1H3Y A C07  1 
HETATM 3367 C C08  . A1H3Y D 2 .   ? -29.639 13.896  20.759 1.00 58.76  ? 501 A1H3Y A C08  1 
HETATM 3368 C C09  . A1H3Y D 2 .   ? -28.693 14.723  20.079 1.00 59.75  ? 501 A1H3Y A C09  1 
HETATM 3369 C C15  . A1H3Y D 2 .   ? -26.600 18.691  15.387 1.00 56.25  ? 501 A1H3Y A C15  1 
HETATM 3370 C C16  . A1H3Y D 2 .   ? -26.990 17.973  14.255 1.00 52.71  ? 501 A1H3Y A C16  1 
HETATM 3371 C C17  . A1H3Y D 2 .   ? -27.431 16.665  14.396 1.00 54.41  ? 501 A1H3Y A C17  1 
HETATM 3372 C C18  . A1H3Y D 2 .   ? -27.471 16.081  15.663 1.00 56.58  ? 501 A1H3Y A C18  1 
HETATM 3373 C C19  . A1H3Y D 2 .   ? -30.340 16.480  19.799 1.00 54.97  ? 501 A1H3Y A C19  1 
HETATM 3374 C C20  . A1H3Y D 2 .   ? -31.275 15.688  20.475 1.00 58.18  ? 501 A1H3Y A C20  1 
HETATM 3375 N N06  . A1H3Y D 2 .   ? -31.628 13.409  21.625 1.00 62.99  ? 501 A1H3Y A N06  1 
HETATM 3376 O O01  . A1H3Y D 2 .   ? -27.607 9.407   21.331 1.00 66.04  ? 501 A1H3Y A O01  1 
HETATM 3377 O O11  . A1H3Y D 2 .   ? -28.101 16.809  18.929 1.00 56.77  ? 501 A1H3Y A O11  1 
HETATM 3378 H H121 . A1H3Y D 2 .   ? -26.261 16.220  18.619 1.00 68.83  ? 501 A1H3Y A H121 1 
HETATM 3379 H H122 . A1H3Y D 2 .   ? -27.359 15.202  18.095 1.00 68.83  ? 501 A1H3Y A H122 1 
HETATM 3380 H H141 . A1H3Y D 2 .   ? -26.363 18.588  17.399 1.00 65.40  ? 501 A1H3Y A H141 1 
HETATM 3381 H H021 . A1H3Y D 2 .   ? -28.855 10.078  22.696 1.00 75.38  ? 501 A1H3Y A H021 1 
HETATM 3382 H H022 . A1H3Y D 2 .   ? -29.514 9.888   21.266 1.00 75.38  ? 501 A1H3Y A H022 1 
HETATM 3383 H H031 . A1H3Y D 2 .   ? -27.783 11.968  22.069 1.00 77.09  ? 501 A1H3Y A H031 1 
HETATM 3384 H H032 . A1H3Y D 2 .   ? -27.964 11.649  20.534 1.00 77.09  ? 501 A1H3Y A H032 1 
HETATM 3385 H H051 . A1H3Y D 2 .   ? -31.123 11.561  22.324 1.00 75.74  ? 501 A1H3Y A H051 1 
HETATM 3386 H H091 . A1H3Y D 2 .   ? -27.826 14.411  19.952 1.00 72.46  ? 501 A1H3Y A H091 1 
HETATM 3387 H H151 . A1H3Y D 2 .   ? -26.315 19.571  15.297 1.00 68.26  ? 501 A1H3Y A H151 1 
HETATM 3388 H H161 . A1H3Y D 2 .   ? -26.954 18.369  13.414 1.00 64.01  ? 501 A1H3Y A H161 1 
HETATM 3389 H H171 . A1H3Y D 2 .   ? -27.699 16.180  13.649 1.00 66.04  ? 501 A1H3Y A H171 1 
HETATM 3390 H H181 . A1H3Y D 2 .   ? -27.768 15.205  15.755 1.00 68.65  ? 501 A1H3Y A H181 1 
HETATM 3391 H H191 . A1H3Y D 2 .   ? -30.580 17.321  19.484 1.00 66.72  ? 501 A1H3Y A H191 1 
HETATM 3392 H H201 . A1H3Y D 2 .   ? -32.136 16.010  20.615 1.00 70.58  ? 501 A1H3Y A H201 1 
HETATM 3393 H H061 . A1H3Y D 2 .   ? -32.454 13.482  21.853 1.00 76.34  ? 501 A1H3Y A H061 1 
HETATM 3394 H H011 . A1H3Y D 2 .   ? -27.001 9.911   21.012 1.00 80.01  ? 501 A1H3Y A H011 1 
HETATM 3395 O O    . HOH   E 3 .   ? -32.511 -5.372  23.514 1.00 64.43  ? 601 HOH   B O    1 
HETATM 3396 O O    . HOH   E 3 .   ? -37.398 -4.180  6.665  1.00 60.89  ? 602 HOH   B O    1 
HETATM 3397 O O    . HOH   E 3 .   ? -46.245 -7.892  24.946 1.00 58.75  ? 603 HOH   B O    1 
HETATM 3398 O O    . HOH   E 3 .   ? -46.725 -18.240 16.077 1.00 66.96  ? 604 HOH   B O    1 
HETATM 3399 O O    . HOH   F 3 .   ? -32.215 21.073  7.164  1.00 50.45  ? 601 HOH   A O    1 
HETATM 3400 O O    . HOH   F 3 .   ? -32.485 9.375   26.653 1.00 61.56  ? 602 HOH   A O    1 
HETATM 3401 O O    . HOH   F 3 .   ? -35.063 21.501  49.544 1.00 70.13  ? 603 HOH   A 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   . ALA A 5   ? 0.8335 1.6426 1.0012 0.3130  -0.1087 -0.2034 220 ALA B N   
2    C CA  . ALA A 5   ? 0.8750 1.5703 1.0003 0.2687  -0.0978 -0.1746 220 ALA B CA  
3    C C   . ALA A 5   ? 0.9550 1.5284 1.0254 0.3034  -0.1188 -0.1610 220 ALA B C   
4    O O   . ALA A 5   ? 0.9628 1.5337 1.0297 0.3444  -0.1211 -0.1803 220 ALA B O   
5    C CB  . ALA A 5   ? 0.8124 1.5305 0.9564 0.2171  -0.0568 -0.1745 220 ALA B CB  
6    N N   . ARG A 6   ? 0.9555 1.4337 0.9844 0.2862  -0.1354 -0.1297 221 ARG B N   
7    C CA  . ARG A 6   ? 1.0046 1.3630 0.9853 0.3102  -0.1614 -0.1112 221 ARG B CA  
8    C C   . ARG A 6   ? 0.9506 1.2256 0.8999 0.2643  -0.1454 -0.0882 221 ARG B C   
9    O O   . ARG A 6   ? 0.9615 1.1366 0.8742 0.2735  -0.1670 -0.0710 221 ARG B O   
10   C CB  . ARG A 6   ? 1.0320 1.3512 0.9883 0.3360  -0.2040 -0.0863 221 ARG B CB  
11   C CG  . ARG A 6   ? 1.0500 1.4548 1.0371 0.3880  -0.2256 -0.1092 221 ARG B CG  
12   C CD  . ARG A 6   ? 1.1606 1.4940 1.1137 0.4333  -0.2781 -0.0839 221 ARG B CD  
13   N NE  . ARG A 6   ? 1.1658 1.5460 1.1434 0.5062  -0.3054 -0.1164 221 ARG B NE  
14   C CZ  . ARG A 6   ? 1.2373 1.5505 1.1905 0.5618  -0.3577 -0.1025 221 ARG B CZ  
15   N NH1 . ARG A 6   ? 1.2994 1.4950 1.2014 0.5464  -0.3880 -0.0495 221 ARG B NH1 
16   N NH2 . ARG A 6   ? 1.2023 1.5711 1.1836 0.6342  -0.3812 -0.1408 221 ARG B NH2 
17   N N   . GLY A 7   ? 0.8945 1.2059 0.8597 0.2161  -0.1119 -0.0885 222 GLY B N   
18   C CA  . GLY A 7   ? 0.8122 1.0597 0.7537 0.1785  -0.0956 -0.0727 222 GLY B CA  
19   C C   . GLY A 7   ? 0.7103 1.0112 0.6803 0.1409  -0.0606 -0.0836 222 GLY B C   
20   O O   . GLY A 7   ? 0.6867 1.0716 0.6960 0.1379  -0.0492 -0.1008 222 GLY B O   
21   N N   . LEU A 8   ? 0.6786 0.9291 0.6303 0.1109  -0.0464 -0.0717 223 LEU B N   
22   C CA  . LEU A 8   ? 0.6576 0.9363 0.6310 0.0739  -0.0194 -0.0755 223 LEU B CA  
23   C C   . LEU A 8   ? 0.6690 0.9740 0.6589 0.0487  -0.0224 -0.0767 223 LEU B C   
24   O O   . LEU A 8   ? 0.6316 0.9012 0.6043 0.0300  -0.0238 -0.0680 223 LEU B O   
25   C CB  . LEU A 8   ? 0.7159 0.9320 0.6625 0.0581  -0.0086 -0.0640 223 LEU B CB  
26   C CG  . LEU A 8   ? 0.6444 0.8704 0.6069 0.0236  0.0140  -0.0622 223 LEU B CG  
27   C CD1 . LEU A 8   ? 0.6183 0.9168 0.6176 0.0170  0.0292  -0.0714 223 LEU B CD1 
28   C CD2 . LEU A 8   ? 0.6270 0.8031 0.5602 0.0227  0.0220  -0.0526 223 LEU B CD2 
29   N N   . GLY A 9   ? 0.6533 1.0317 0.6791 0.0507  -0.0249 -0.0926 224 GLY B N   
30   C CA  . GLY A 9   ? 0.6228 1.0346 0.6681 0.0282  -0.0304 -0.1031 224 GLY B CA  
31   C C   . GLY A 9   ? 0.6268 1.1263 0.7118 0.0361  -0.0395 -0.1225 224 GLY B C   
32   O O   . GLY A 9   ? 0.6204 1.1560 0.7124 0.0683  -0.0460 -0.1254 224 GLY B O   
33   N N   . THR A 10  ? 0.5617 1.0985 0.6749 0.0095  -0.0430 -0.1404 225 THR B N   
34   C CA  . THR A 10  ? 0.5749 1.2025 0.7300 0.0115  -0.0550 -0.1626 225 THR B CA  
35   C C   . THR A 10  ? 0.5926 1.2386 0.7296 0.0223  -0.0794 -0.1715 225 THR B C   
36   O O   . THR A 10  ? 0.6366 1.2324 0.7285 0.0280  -0.0846 -0.1572 225 THR B O   
37   C CB  . THR A 10  ? 0.6021 1.2698 0.8132 -0.0341 -0.0434 -0.1802 225 THR B CB  
38   O OG1 . THR A 10  ? 0.5490 1.1943 0.7639 -0.0603 -0.0550 -0.1984 225 THR B OG1 
39   C CG2 . THR A 10  ? 0.5234 1.1574 0.7389 -0.0555 -0.0158 -0.1610 225 THR B CG2 
40   N N   . ALA A 11  ? 0.6670 1.3984 0.8411 0.0228  -0.0942 -0.1959 226 ALA B N   
41   C CA  . ALA A 11  ? 0.6522 1.4213 0.8075 0.0384  -0.1198 -0.2061 226 ALA B CA  
42   C C   . ALA A 11  ? 0.6365 1.3875 0.7841 0.0113  -0.1224 -0.2266 226 ALA B C   
43   O O   . ALA A 11  ? 0.6433 1.4173 0.7577 0.0264  -0.1394 -0.2301 226 ALA B O   
44   C CB  . ALA A 11  ? 0.6393 1.5144 0.8411 0.0482  -0.1368 -0.2310 226 ALA B CB  
45   N N   . ARG A 12  ? 0.6114 1.3245 0.7874 -0.0254 -0.1080 -0.2402 227 ARG B N   
46   C CA  . ARG A 12  ? 0.5659 1.2485 0.7370 -0.0446 -0.1136 -0.2655 227 ARG B CA  
47   C C   . ARG A 12  ? 0.5640 1.1661 0.6903 -0.0403 -0.0991 -0.2423 227 ARG B C   
48   O O   . ARG A 12  ? 0.6062 1.2029 0.7078 -0.0352 -0.1067 -0.2583 227 ARG B O   
49   C CB  . ARG A 12  ? 0.5720 1.2439 0.8012 -0.0878 -0.1132 -0.2920 227 ARG B CB  
50   C CG  . ARG A 12  ? 0.5679 1.3258 0.8541 -0.1046 -0.1296 -0.3213 227 ARG B CG  
51   C CD  . ARG A 12  ? 0.5848 1.3154 0.9284 -0.1577 -0.1302 -0.3381 227 ARG B CD  
52   N NE  . ARG A 12  ? 0.6380 1.3239 0.9814 -0.1688 -0.1524 -0.3781 227 ARG B NE  
53   C CZ  . ARG A 12  ? 0.6717 1.3315 1.0669 -0.2130 -0.1690 -0.4062 227 ARG B CZ  
54   N NH1 . ARG A 12  ? 0.6614 1.3403 1.1139 -0.2591 -0.1619 -0.3909 227 ARG B NH1 
55   N NH2 . ARG A 12  ? 0.7134 1.3297 1.1039 -0.2113 -0.1950 -0.4513 227 ARG B NH2 
56   N N   . LEU A 13  ? 0.6173 1.1664 0.7346 -0.0412 -0.0791 -0.2096 228 LEU B N   
57   C CA  . LEU A 13  ? 0.5934 1.0693 0.6769 -0.0420 -0.0665 -0.1912 228 LEU B CA  
58   C C   . LEU A 13  ? 0.6288 1.0733 0.6826 -0.0240 -0.0555 -0.1527 228 LEU B C   
59   O O   . LEU A 13  ? 0.6453 1.0984 0.7173 -0.0212 -0.0479 -0.1443 228 LEU B O   
60   C CB  . LEU A 13  ? 0.5715 0.9952 0.6824 -0.0715 -0.0573 -0.2006 228 LEU B CB  
61   C CG  . LEU A 13  ? 0.6277 0.9860 0.7074 -0.0683 -0.0511 -0.1925 228 LEU B CG  
62   C CD1 . LEU A 13  ? 0.6290 1.0098 0.6933 -0.0558 -0.0668 -0.2232 228 LEU B CD1 
63   C CD2 . LEU A 13  ? 0.5971 0.8939 0.6994 -0.0936 -0.0432 -0.1891 228 LEU B CD2 
64   N N   . GLN A 14  ? 0.5805 0.9953 0.5902 -0.0120 -0.0567 -0.1322 229 GLN B N   
65   C CA  . GLN A 14  ? 0.5863 0.9575 0.5659 0.0025  -0.0531 -0.0983 229 GLN B CA  
66   C C   . GLN A 14  ? 0.6093 0.9229 0.5678 -0.0087 -0.0416 -0.0864 229 GLN B C   
67   O O   . GLN A 14  ? 0.6030 0.9240 0.5527 -0.0163 -0.0423 -0.0957 229 GLN B O   
68   C CB  . GLN A 14  ? 0.6394 1.0272 0.5853 0.0229  -0.0716 -0.0753 229 GLN B CB  
69   C CG  . GLN A 14  ? 0.7319 1.0533 0.6445 0.0315  -0.0739 -0.0400 229 GLN B CG  
70   C CD  . GLN A 14  ? 0.7887 1.1001 0.6935 0.0611  -0.0931 -0.0244 229 GLN B CD  
71   O OE1 . GLN A 14  ? 0.8005 1.1511 0.6979 0.0764  -0.1124 -0.0176 229 GLN B OE1 
72   N NE2 . GLN A 14  ? 0.7706 1.0324 0.6764 0.0741  -0.0905 -0.0223 229 GLN B NE2 
73   N N   . LEU A 15  ? 0.6361 0.9015 0.5869 -0.0059 -0.0325 -0.0700 230 LEU B N   
74   C CA  . LEU A 15  ? 0.6465 0.8610 0.5758 -0.0137 -0.0249 -0.0571 230 LEU B CA  
75   C C   . LEU A 15  ? 0.6902 0.8868 0.5846 -0.0076 -0.0367 -0.0302 230 LEU B C   
76   O O   . LEU A 15  ? 0.7561 0.9354 0.6391 0.0075  -0.0485 -0.0150 230 LEU B O   
77   C CB  . LEU A 15  ? 0.6718 0.8491 0.6060 -0.0148 -0.0117 -0.0537 230 LEU B CB  
78   C CG  . LEU A 15  ? 0.6696 0.8006 0.5830 -0.0219 -0.0066 -0.0435 230 LEU B CG  
79   C CD1 . LEU A 15  ? 0.6403 0.7579 0.5704 -0.0348 0.0054  -0.0521 230 LEU B CD1 
80   C CD2 . LEU A 15  ? 0.7129 0.8049 0.6029 -0.0097 -0.0094 -0.0284 230 LEU B CD2 
81   N N   . VAL A 16  ? 0.6940 0.8988 0.5737 -0.0192 -0.0362 -0.0245 231 VAL B N   
82   C CA  . VAL A 16  ? 0.7565 0.9530 0.6062 -0.0245 -0.0469 0.0078  231 VAL B CA  
83   C C   . VAL A 16  ? 0.7973 0.9370 0.6363 -0.0329 -0.0446 0.0218  231 VAL B C   
84   O O   . VAL A 16  ? 0.8766 0.9736 0.6977 -0.0340 -0.0585 0.0469  231 VAL B O   
85   C CB  . VAL A 16  ? 0.7098 0.9717 0.5501 -0.0343 -0.0463 0.0074  231 VAL B CB  
86   C CG1 . VAL A 16  ? 0.7872 1.0486 0.5984 -0.0501 -0.0546 0.0492  231 VAL B CG1 
87   C CG2 . VAL A 16  ? 0.7107 1.0315 0.5571 -0.0234 -0.0532 -0.0090 231 VAL B CG2 
88   N N   . GLU A 17  ? 0.7116 0.8468 0.5618 -0.0378 -0.0311 0.0043  232 GLU B N   
89   C CA  . GLU A 17  ? 0.7576 0.8523 0.5979 -0.0454 -0.0301 0.0141  232 GLU B CA  
90   C C   . GLU A 17  ? 0.7029 0.7827 0.5571 -0.0405 -0.0172 -0.0070 232 GLU B C   
91   O O   . GLU A 17  ? 0.6684 0.7711 0.5405 -0.0384 -0.0107 -0.0269 232 GLU B O   
92   C CB  . GLU A 17  ? 0.7925 0.9183 0.6223 -0.0640 -0.0332 0.0306  232 GLU B CB  
93   C CG  . GLU A 17  ? 0.8860 0.9760 0.6964 -0.0794 -0.0501 0.0656  232 GLU B CG  
94   C CD  . GLU A 17  ? 0.9276 1.0424 0.7340 -0.1065 -0.0518 0.0844  232 GLU B CD  
95   O OE1 . GLU A 17  ? 0.8843 0.9549 0.6895 -0.1150 -0.0584 0.0876  232 GLU B OE1 
96   O OE2 . GLU A 17  ? 1.0086 1.1967 0.8133 -0.1199 -0.0475 0.0955  232 GLU B OE2 
97   N N   . PHE A 18  ? 0.7183 0.7549 0.5627 -0.0385 -0.0170 -0.0019 233 PHE B N   
98   C CA  . PHE A 18  ? 0.6416 0.6623 0.4903 -0.0358 -0.0073 -0.0117 233 PHE B CA  
99   C C   . PHE A 18  ? 0.6820 0.6721 0.5119 -0.0370 -0.0136 -0.0030 233 PHE B C   
100  O O   . PHE A 18  ? 0.7214 0.6855 0.5379 -0.0352 -0.0242 0.0043  233 PHE B O   
101  C CB  . PHE A 18  ? 0.6545 0.6677 0.5129 -0.0290 0.0028  -0.0183 233 PHE B CB  
102  C CG  . PHE A 18  ? 0.6766 0.6667 0.5289 -0.0281 0.0109  -0.0162 233 PHE B CG  
103  C CD1 . PHE A 18  ? 0.7094 0.6792 0.5397 -0.0196 0.0108  -0.0110 233 PHE B CD1 
104  C CD2 . PHE A 18  ? 0.6811 0.6669 0.5471 -0.0340 0.0149  -0.0199 233 PHE B CD2 
105  C CE1 . PHE A 18  ? 0.7100 0.6672 0.5285 -0.0179 0.0180  -0.0053 233 PHE B CE1 
106  C CE2 . PHE A 18  ? 0.6899 0.6500 0.5457 -0.0337 0.0195  -0.0099 233 PHE B CE2 
107  C CZ  . PHE A 18  ? 0.6782 0.6298 0.5084 -0.0261 0.0226  -0.0005 233 PHE B CZ  
108  N N   . SER A 19  ? 0.6990 0.6896 0.5286 -0.0377 -0.0114 -0.0066 234 SER B N   
109  C CA  . SER A 19  ? 0.6675 0.6341 0.4803 -0.0375 -0.0188 -0.0024 234 SER B CA  
110  C C   . SER A 19  ? 0.6595 0.6270 0.4723 -0.0301 -0.0153 -0.0074 234 SER B C   
111  O O   . SER A 19  ? 0.6376 0.6222 0.4656 -0.0262 -0.0120 -0.0146 234 SER B O   
112  C CB  . SER A 19  ? 0.6942 0.6696 0.5043 -0.0550 -0.0332 0.0081  234 SER B CB  
113  O OG  . SER A 19  ? 0.6841 0.7112 0.5085 -0.0637 -0.0308 0.0079  234 SER B OG  
114  N N   . ALA A 20  ? 0.6978 0.6439 0.4916 -0.0242 -0.0198 -0.0058 235 ALA B N   
115  C CA  . ALA A 20  ? 0.6619 0.6073 0.4491 -0.0147 -0.0222 -0.0061 235 ALA B CA  
116  C C   . ALA A 20  ? 0.6439 0.5989 0.4240 -0.0207 -0.0377 -0.0086 235 ALA B C   
117  O O   . ALA A 20  ? 0.6972 0.6329 0.4645 -0.0263 -0.0461 -0.0101 235 ALA B O   
118  C CB  . ALA A 20  ? 0.6896 0.6118 0.4568 -0.0038 -0.0138 0.0012  235 ALA B CB  
119  N N   . PHE A 21  ? 0.6413 0.6279 0.4330 -0.0189 -0.0445 -0.0124 236 PHE B N   
120  C CA  . PHE A 21  ? 0.6480 0.6614 0.4441 -0.0335 -0.0596 -0.0143 236 PHE B CA  
121  C C   . PHE A 21  ? 0.5933 0.6362 0.3927 -0.0171 -0.0678 -0.0215 236 PHE B C   
122  O O   . PHE A 21  ? 0.6067 0.6459 0.4078 0.0056  -0.0634 -0.0237 236 PHE B O   
123  C CB  . PHE A 21  ? 0.6947 0.7503 0.5135 -0.0583 -0.0597 -0.0085 236 PHE B CB  
124  C CG  . PHE A 21  ? 0.5974 0.7052 0.4370 -0.0479 -0.0501 -0.0163 236 PHE B CG  
125  C CD1 . PHE A 21  ? 0.5985 0.7701 0.4560 -0.0410 -0.0554 -0.0269 236 PHE B CD1 
126  C CD2 . PHE A 21  ? 0.6508 0.7492 0.4935 -0.0411 -0.0383 -0.0187 236 PHE B CD2 
127  C CE1 . PHE A 21  ? 0.6242 0.8467 0.5002 -0.0224 -0.0497 -0.0434 236 PHE B CE1 
128  C CE2 . PHE A 21  ? 0.5933 0.7375 0.4541 -0.0271 -0.0339 -0.0349 236 PHE B CE2 
129  C CZ  . PHE A 21  ? 0.5842 0.7885 0.4604 -0.0152 -0.0398 -0.0490 236 PHE B CZ  
130  N N   . VAL A 22  ? 0.6409 0.7117 0.4438 -0.0288 -0.0837 -0.0255 237 VAL B N   
131  C CA  . VAL A 22  ? 0.6840 0.8058 0.4989 -0.0144 -0.0950 -0.0347 237 VAL B CA  
132  C C   . VAL A 22  ? 0.6787 0.8724 0.5244 -0.0450 -0.1037 -0.0364 237 VAL B C   
133  O O   . VAL A 22  ? 0.6675 0.8477 0.5130 -0.0787 -0.1129 -0.0293 237 VAL B O   
134  C CB  . VAL A 22  ? 0.7231 0.8220 0.5098 0.0035  -0.1088 -0.0380 237 VAL B CB  
135  C CG1 . VAL A 22  ? 0.7122 0.7879 0.4841 -0.0188 -0.1216 -0.0424 237 VAL B CG1 
136  C CG2 . VAL A 22  ? 0.7050 0.8637 0.5066 0.0219  -0.1245 -0.0480 237 VAL B CG2 
137  N N   . GLU A 23  ? 0.6597 0.9318 0.5334 -0.0336 -0.1025 -0.0459 238 GLU B N   
138  C CA  . GLU A 23  ? 0.6957 1.0634 0.6026 -0.0629 -0.1095 -0.0464 238 GLU B CA  
139  C C   . GLU A 23  ? 0.7055 1.1204 0.6221 -0.0447 -0.1284 -0.0619 238 GLU B C   
140  O O   . GLU A 23  ? 0.6794 1.1038 0.5945 0.0017  -0.1310 -0.0765 238 GLU B O   
141  C CB  . GLU A 23  ? 0.6360 1.0898 0.5703 -0.0606 -0.0948 -0.0511 238 GLU B CB  
142  C CG  . GLU A 23  ? 0.6225 1.0447 0.5469 -0.0741 -0.0775 -0.0378 238 GLU B CG  
143  C CD  . GLU A 23  ? 0.5981 1.0959 0.5399 -0.0508 -0.0646 -0.0553 238 GLU B CD  
144  O OE1 . GLU A 23  ? 0.5923 1.1273 0.5469 -0.0089 -0.0699 -0.0830 238 GLU B OE1 
145  O OE2 . GLU A 23  ? 0.5894 1.1108 0.5307 -0.0704 -0.0523 -0.0439 238 GLU B OE2 
146  N N   . PRO A 24  ? 0.7629 1.2532 0.5945 0.0081  0.0329  -0.1060 239 PRO B N   
147  C CA  . PRO A 24  ? 0.7635 1.3603 0.6303 0.0199  0.0110  -0.1264 239 PRO B CA  
148  C C   . PRO A 24  ? 0.7761 1.4839 0.6811 0.0505  0.0167  -0.1340 239 PRO B C   
149  O O   . PRO A 24  ? 0.8441 1.5595 0.7544 0.0441  0.0444  -0.1267 239 PRO B O   
150  C CB  . PRO A 24  ? 0.7684 1.3990 0.6720 -0.0471 0.0174  -0.1448 239 PRO B CB  
151  C CG  . PRO A 24  ? 0.7735 1.3598 0.6831 -0.0898 0.0521  -0.1304 239 PRO B CG  
152  C CD  . PRO A 24  ? 0.7494 1.2292 0.6028 -0.0554 0.0583  -0.1044 239 PRO B CD  
153  N N   . PRO A 25  ? 0.8244 1.6272 0.7559 0.0866  -0.0088 -0.1487 240 PRO B N   
154  C CA  . PRO A 25  ? 0.8035 1.7253 0.7791 0.1225  -0.0037 -0.1611 240 PRO B CA  
155  C C   . PRO A 25  ? 0.8518 1.8647 0.8804 0.0676  0.0316  -0.1703 240 PRO B C   
156  O O   . PRO A 25  ? 0.8441 1.9154 0.8890 0.0889  0.0529  -0.1721 240 PRO B O   
157  C CB  . PRO A 25  ? 0.7560 1.7724 0.7583 0.1582  -0.0409 -0.1761 240 PRO B CB  
158  C CG  . PRO A 25  ? 0.7563 1.6697 0.7027 0.1627  -0.0669 -0.1615 240 PRO B CG  
159  C CD  . PRO A 25  ? 0.8137 1.6329 0.7377 0.0971  -0.0433 -0.1558 240 PRO B CD  
160  N N   . ASP A 26  ? 0.9569 1.9806 1.0114 -0.0047 0.0399  -0.1766 241 ASP B N   
161  C CA  . ASP A 26  ? 0.9194 2.0049 1.0204 -0.0696 0.0765  -0.1772 241 ASP B CA  
162  C C   . ASP A 26  ? 0.9456 1.9537 1.0087 -0.0765 0.1113  -0.1484 241 ASP B C   
163  O O   . ASP A 26  ? 0.9584 2.0215 1.0530 -0.1244 0.1455  -0.1403 241 ASP B O   
164  C CB  . ASP A 26  ? 0.9542 2.0128 1.0767 -0.1474 0.0774  -0.1865 241 ASP B CB  
165  C CG  . ASP A 26  ? 0.9900 2.1535 1.1579 -0.1535 0.0459  -0.2213 241 ASP B CG  
166  O OD1 . ASP A 26  ? 1.0078 2.1446 1.1404 -0.1058 0.0108  -0.2263 241 ASP B OD1 
167  O OD2 . ASP A 26  ? 1.0194 2.2968 1.2575 -0.2072 0.0561  -0.2425 241 ASP B OD2 
168  N N   . ALA A 27  ? 0.9078 1.7937 0.9041 -0.0336 0.1031  -0.1314 242 ALA B N   
169  C CA  . ALA A 27  ? 0.9113 1.7145 0.8649 -0.0441 0.1308  -0.1044 242 ALA B CA  
170  C C   . ALA A 27  ? 0.8930 1.7976 0.8649 -0.0343 0.1611  -0.1030 242 ALA B C   
171  O O   . ALA A 27  ? 0.8577 1.7463 0.8168 -0.0732 0.1937  -0.0789 242 ALA B O   
172  C CB  . ALA A 27  ? 0.8887 1.5674 0.7761 0.0063  0.1119  -0.0946 242 ALA B CB  
173  N N   . VAL A 28  ? 0.8660 1.8791 0.8672 0.0194  0.1510  -0.1278 243 VAL B N   
174  C CA  . VAL A 28  ? 0.8639 1.9918 0.8853 0.0398  0.1794  -0.1354 243 VAL B CA  
175  C C   . VAL A 28  ? 0.8455 2.1159 0.9366 -0.0220 0.2097  -0.1379 243 VAL B C   
176  O O   . VAL A 28  ? 0.8454 2.2271 0.9566 -0.0161 0.2410  -0.1415 243 VAL B O   
177  C CB  . VAL A 28  ? 0.8288 2.0192 0.8623 0.1270  0.1547  -0.1660 243 VAL B CB  
178  C CG1 . VAL A 28  ? 0.9108 1.9556 0.8863 0.1774  0.1188  -0.1623 243 VAL B CG1 
179  C CG2 . VAL A 28  ? 0.8321 2.1613 0.9408 0.1292  0.1379  -0.1908 243 VAL B CG2 
180  N N   . ASP A 29  ? 0.8640 2.1409 0.9949 -0.0820 0.2018  -0.1396 244 ASP B N   
181  C CA  . ASP A 29  ? 0.8701 2.2612 1.0690 -0.1588 0.2322  -0.1390 244 ASP B CA  
182  C C   . ASP A 29  ? 0.9069 2.1877 1.0747 -0.2320 0.2618  -0.0989 244 ASP B C   
183  O O   . ASP A 29  ? 0.9401 2.2518 1.0989 -0.2568 0.3020  -0.0723 244 ASP B O   
184  C CB  . ASP A 29  ? 0.8553 2.3224 1.1199 -0.1836 0.2039  -0.1703 244 ASP B CB  
185  C CG  . ASP A 29  ? 0.8758 2.5097 1.1949 -0.1248 0.1863  -0.2054 244 ASP B CG  
186  O OD1 . ASP A 29  ? 0.8411 2.4934 1.1352 -0.0493 0.1864  -0.2088 244 ASP B OD1 
187  O OD2 . ASP A 29  ? 0.9545 2.7003 1.3422 -0.1510 0.1697  -0.2326 244 ASP B OD2 
188  N N   . SER A 30  ? 0.8653 2.0185 1.0144 -0.2636 0.2421  -0.0936 245 SER B N   
189  C CA  . SER A 30  ? 0.8753 1.8874 0.9818 -0.3117 0.2604  -0.0552 245 SER B CA  
190  C C   . SER A 30  ? 0.8675 1.7270 0.9030 -0.2625 0.2314  -0.0503 245 SER B C   
191  O O   . SER A 30  ? 0.8513 1.6896 0.8873 -0.2345 0.1961  -0.0770 245 SER B O   
192  C CB  . SER A 30  ? 0.9095 1.9051 1.0664 -0.3995 0.2664  -0.0572 245 SER B CB  
193  O OG  . SER A 30  ? 0.9706 1.8769 1.1042 -0.4537 0.2990  -0.0115 245 SER B OG  
194  N N   . TYR A 31  ? 0.8421 1.6046 0.8164 -0.2528 0.2462  -0.0155 246 TYR B N   
195  C CA  . TYR A 31  ? 0.7994 1.4445 0.7107 -0.1987 0.2208  -0.0135 246 TYR B CA  
196  C C   . TYR A 31  ? 0.7979 1.3181 0.6983 -0.2265 0.2030  -0.0120 246 TYR B C   
197  O O   . TYR A 31  ? 0.8317 1.3089 0.7500 -0.2868 0.2177  0.0028  246 TYR B O   
198  C CB  . TYR A 31  ? 0.8061 1.4054 0.6571 -0.1746 0.2390  0.0176  246 TYR B CB  
199  C CG  . TYR A 31  ? 0.7835 1.2725 0.5779 -0.1226 0.2115  0.0151  246 TYR B CG  
200  C CD1 . TYR A 31  ? 0.7464 1.2544 0.5354 -0.0626 0.1852  -0.0142 246 TYR B CD1 
201  C CD2 . TYR A 31  ? 0.8057 1.1722 0.5568 -0.1344 0.2107  0.0426  246 TYR B CD2 
202  C CE1 . TYR A 31  ? 0.7591 1.1678 0.5021 -0.0234 0.1617  -0.0155 246 TYR B CE1 
203  C CE2 . TYR A 31  ? 0.8048 1.0849 0.5127 -0.0914 0.1864  0.0378  246 TYR B CE2 
204  C CZ  . TYR A 31  ? 0.7866 1.0879 0.4913 -0.0398 0.1630  0.0088  246 TYR B CZ  
205  O OH  . TYR A 31  ? 0.8056 1.0207 0.4718 -0.0043 0.1402  0.0050  246 TYR B OH  
206  N N   . GLN A 32  ? 0.7609 1.2216 0.6319 -0.1812 0.1719  -0.0280 247 GLN B N   
207  C CA  . GLN A 32  ? 0.8054 1.1491 0.6564 -0.1947 0.1563  -0.0284 247 GLN B CA  
208  C C   . GLN A 32  ? 0.7698 1.0594 0.5752 -0.1346 0.1311  -0.0342 247 GLN B C   
209  O O   . GLN A 32  ? 0.7720 1.1197 0.5763 -0.0899 0.1180  -0.0474 247 GLN B O   
210  C CB  . GLN A 32  ? 0.7685 1.1392 0.6657 -0.2339 0.1433  -0.0590 247 GLN B CB  
211  C CG  . GLN A 32  ? 0.7470 1.2320 0.6727 -0.2058 0.1224  -0.0898 247 GLN B CG  
212  C CD  . GLN A 32  ? 0.7883 1.3249 0.7625 -0.2484 0.1093  -0.1234 247 GLN B CD  
213  O OE1 . GLN A 32  ? 0.7555 1.2192 0.7182 -0.2654 0.0958  -0.1382 247 GLN B OE1 
214  N NE2 . GLN A 32  ? 0.7896 1.4609 0.8217 -0.2676 0.1139  -0.1400 247 GLN B NE2 
215  N N   . ARG A 33  ? 0.7490 0.9273 0.5203 -0.1336 0.1247  -0.0238 248 ARG B N   
216  C CA  . ARG A 33  ? 0.7713 0.8997 0.5084 -0.0897 0.1007  -0.0318 248 ARG B CA  
217  C C   . ARG A 33  ? 0.7503 0.8005 0.4825 -0.1099 0.0916  -0.0397 248 ARG B C   
218  O O   . ARG A 33  ? 0.7471 0.7379 0.4817 -0.1406 0.1041  -0.0284 248 ARG B O   
219  C CB  . ARG A 33  ? 0.7508 0.8345 0.4438 -0.0515 0.1023  -0.0132 248 ARG B CB  
220  C CG  . ARG A 33  ? 0.8231 0.8191 0.4908 -0.0663 0.1117  0.0103  248 ARG B CG  
221  C CD  . ARG A 33  ? 0.8131 0.7564 0.4383 -0.0260 0.1001  0.0165  248 ARG B CD  
222  N NE  . ARG A 33  ? 0.8877 0.8743 0.4943 -0.0014 0.1084  0.0227  248 ARG B NE  
223  C CZ  . ARG A 33  ? 0.9209 0.8736 0.4898 0.0257  0.1039  0.0296  248 ARG B CZ  
224  N NH1 . ARG A 33  ? 0.8962 0.7742 0.4460 0.0312  0.0910  0.0344  248 ARG B NH1 
225  N NH2 . ARG A 33  ? 0.8688 0.8723 0.4209 0.0483  0.1122  0.0274  248 ARG B NH2 
226  N N   . HIS A 34  ? 0.7858 0.8367 0.5098 -0.0907 0.0704  -0.0583 249 HIS B N   
227  C CA  . HIS A 34  ? 0.7427 0.7286 0.4560 -0.1011 0.0625  -0.0699 249 HIS B CA  
228  C C   . HIS A 34  ? 0.7343 0.6546 0.4079 -0.0669 0.0563  -0.0554 249 HIS B C   
229  O O   . HIS A 34  ? 0.7508 0.6864 0.4051 -0.0325 0.0458  -0.0495 249 HIS B O   
230  C CB  . HIS A 34  ? 0.7367 0.7728 0.4600 -0.1042 0.0446  -0.0985 249 HIS B CB  
231  C CG  . HIS A 34  ? 0.8402 0.8225 0.5449 -0.1066 0.0373  -0.1136 249 HIS B CG  
232  N ND1 . HIS A 34  ? 0.8215 0.7689 0.5446 -0.1412 0.0434  -0.1358 249 HIS B ND1 
233  C CD2 . HIS A 34  ? 0.8278 0.7874 0.4986 -0.0790 0.0263  -0.1108 249 HIS B CD2 
234  C CE1 . HIS A 34  ? 0.8502 0.7642 0.5514 -0.1304 0.0365  -0.1502 249 HIS B CE1 
235  N NE2 . HIS A 34  ? 0.8770 0.8018 0.5461 -0.0954 0.0274  -0.1330 249 HIS B NE2 
236  N N   . LEU A 35  ? 0.7486 0.5958 0.4142 -0.0763 0.0618  -0.0514 250 LEU B N   
237  C CA  . LEU A 35  ? 0.7669 0.5598 0.4034 -0.0493 0.0561  -0.0411 250 LEU B CA  
238  C C   . LEU A 35  ? 0.8838 0.6642 0.5149 -0.0476 0.0464  -0.0613 250 LEU B C   
239  O O   . LEU A 35  ? 0.8039 0.5684 0.4501 -0.0687 0.0493  -0.0814 250 LEU B O   
240  C CB  . LEU A 35  ? 0.7781 0.5106 0.4100 -0.0536 0.0665  -0.0224 250 LEU B CB  
241  C CG  . LEU A 35  ? 0.8116 0.5582 0.4337 -0.0493 0.0770  0.0036  250 LEU B CG  
242  C CD1 . LEU A 35  ? 0.8145 0.5069 0.4362 -0.0650 0.0885  0.0256  250 LEU B CD1 
243  C CD2 . LEU A 35  ? 0.8100 0.5576 0.4028 -0.0130 0.0678  0.0106  250 LEU B CD2 
244  N N   . PHE A 36  ? 0.8123 0.5994 0.4212 -0.0235 0.0358  -0.0567 251 PHE B N   
245  C CA  . PHE A 36  ? 0.8641 0.6430 0.4620 -0.0223 0.0308  -0.0692 251 PHE B CA  
246  C C   . PHE A 36  ? 0.8720 0.5979 0.4688 -0.0181 0.0364  -0.0677 251 PHE B C   
247  O O   . PHE A 36  ? 0.8393 0.5554 0.4426 -0.0257 0.0398  -0.0878 251 PHE B O   
248  C CB  . PHE A 36  ? 0.8242 0.6242 0.3986 -0.0022 0.0190  -0.0573 251 PHE B CB  
249  C CG  . PHE A 36  ? 0.8276 0.6839 0.4039 0.0037  0.0092  -0.0571 251 PHE B CG  
250  C CD1 . PHE A 36  ? 0.7701 0.6771 0.3502 -0.0096 0.0032  -0.0759 251 PHE B CD1 
251  C CD2 . PHE A 36  ? 0.7080 0.5732 0.2828 0.0261  0.0040  -0.0421 251 PHE B CD2 
252  C CE1 . PHE A 36  ? 0.7550 0.7253 0.3401 -0.0003 -0.0095 -0.0761 251 PHE B CE1 
253  C CE2 . PHE A 36  ? 0.6806 0.6042 0.2621 0.0385  -0.0066 -0.0434 251 PHE B CE2 
254  C CZ  . PHE A 36  ? 0.8482 0.8271 0.4360 0.0255  -0.0144 -0.0585 251 PHE B CZ  
255  N N   . VAL A 37  ? 0.8177 0.5168 0.4072 -0.0030 0.0361  -0.0479 252 VAL B N   
256  C CA  . VAL A 37  ? 0.8532 0.5125 0.4440 0.0060  0.0376  -0.0440 252 VAL B CA  
257  C C   . VAL A 37  ? 0.8702 0.5118 0.4545 0.0158  0.0379  -0.0233 252 VAL B C   
258  O O   . VAL A 37  ? 0.8539 0.5161 0.4263 0.0233  0.0354  -0.0142 252 VAL B O   
259  C CB  . VAL A 37  ? 0.8309 0.4944 0.4116 0.0162  0.0317  -0.0441 252 VAL B CB  
260  C CG1 . VAL A 37  ? 0.8280 0.5162 0.4091 0.0057  0.0349  -0.0622 252 VAL B CG1 
261  C CG2 . VAL A 37  ? 0.8735 0.5470 0.4373 0.0260  0.0235  -0.0300 252 VAL B CG2 
262  N N   . HIS A 38  ? 0.8836 0.4896 0.4734 0.0195  0.0404  -0.0165 253 HIS B N   
263  C CA  . HIS A 38  ? 0.9110 0.5037 0.4878 0.0278  0.0415  0.0073  253 HIS B CA  
264  C C   . HIS A 38  ? 0.9238 0.4846 0.5004 0.0454  0.0347  0.0148  253 HIS B C   
265  O O   . HIS A 38  ? 0.9282 0.4557 0.5214 0.0439  0.0374  0.0119  253 HIS B O   
266  C CB  . HIS A 38  ? 0.8822 0.4680 0.4664 0.0066  0.0544  0.0191  253 HIS B CB  
267  C CG  . HIS A 38  ? 0.9750 0.5568 0.5388 0.0119  0.0596  0.0495  253 HIS B CG  
268  N ND1 . HIS A 38  ? 1.0463 0.5822 0.6073 0.0094  0.0641  0.0740  253 HIS B ND1 
269  C CD2 . HIS A 38  ? 0.9641 0.5837 0.5051 0.0224  0.0607  0.0596  253 HIS B CD2 
270  C CE1 . HIS A 38  ? 0.9908 0.5418 0.5243 0.0147  0.0692  0.1023  253 HIS B CE1 
271  N NE2 . HIS A 38  ? 0.9863 0.5920 0.5079 0.0231  0.0678  0.0903  253 HIS B NE2 
272  N N   . ILE A 39  ? 0.9563 0.5273 0.5158 0.0640  0.0244  0.0225  254 ILE B N   
273  C CA  . ILE A 39  ? 0.9387 0.4909 0.4949 0.0837  0.0152  0.0350  254 ILE B CA  
274  C C   . ILE A 39  ? 1.0229 0.5755 0.5486 0.0903  0.0163  0.0632  254 ILE B C   
275  O O   . ILE A 39  ? 1.0349 0.6183 0.5395 0.0902  0.0177  0.0633  254 ILE B O   
276  C CB  . ILE A 39  ? 0.9544 0.5286 0.5163 0.0979  0.0002  0.0196  254 ILE B CB  
277  C CG1 . ILE A 39  ? 0.9219 0.5089 0.5066 0.0852  0.0042  -0.0041 254 ILE B CG1 
278  C CG2 . ILE A 39  ? 0.9604 0.5253 0.5302 0.1205  -0.0115 0.0272  254 ILE B CG2 
279  C CD1 . ILE A 39  ? 0.8763 0.4874 0.4761 0.0910  -0.0065 -0.0177 254 ILE B CD1 
280  N N   . SER A 40  ? 1.1116 0.6304 0.6328 0.0983  0.0161  0.0881  255 SER B N   
281  C CA  . SER A 40  ? 1.1179 0.6391 0.6027 0.1048  0.0182  0.1228  255 SER B CA  
282  C C   . SER A 40  ? 1.1658 0.6670 0.6415 0.1342  0.0008  0.1416  255 SER B C   
283  O O   . SER A 40  ? 1.1838 0.6349 0.6778 0.1396  0.0003  0.1537  255 SER B O   
284  C CB  . SER A 40  ? 1.1437 0.6403 0.6279 0.0777  0.0394  0.1478  255 SER B CB  
285  O OG  . SER A 40  ? 1.3335 0.8348 0.7783 0.0819  0.0447  0.1884  255 SER B OG  
286  N N   . GLN A 41  ? 1.1837 0.7249 0.6333 0.1557  -0.0156 0.1406  256 GLN B N   
287  C CA  . GLN A 41  ? 1.2469 0.7846 0.6850 0.1874  -0.0363 0.1594  256 GLN B CA  
288  C C   . GLN A 41  ? 1.3165 0.8898 0.7215 0.1901  -0.0358 0.1891  256 GLN B C   
289  O O   . GLN A 41  ? 1.2732 0.8946 0.6620 0.2093  -0.0546 0.1822  256 GLN B O   
290  C CB  . GLN A 41  ? 1.1530 0.7330 0.6126 0.2036  -0.0588 0.1231  256 GLN B CB  
291  C CG  . GLN A 41  ? 1.1551 0.7299 0.6649 0.1884  -0.0526 0.0876  256 GLN B CG  
292  C CD  . GLN A 41  ? 1.0925 0.7087 0.6332 0.2007  -0.0717 0.0581  256 GLN B CD  
293  O OE1 . GLN A 41  ? 1.0893 0.7022 0.6671 0.2129  -0.0753 0.0495  256 GLN B OE1 
294  N NE2 . GLN A 41  ? 1.0280 0.6852 0.5578 0.1960  -0.0829 0.0389  256 GLN B NE2 
295  N N   . HIS A 42  ? 1.4586 1.0152 0.8574 0.1674  -0.0143 0.2200  257 HIS B N   
296  C CA  . HIS A 42  ? 1.5164 1.1107 0.8852 0.1640  -0.0102 0.2539  257 HIS B CA  
297  C C   . HIS A 42  ? 1.5770 1.1476 0.9432 0.1820  -0.0249 0.2938  257 HIS B C   
298  O O   . HIS A 42  ? 1.6247 1.1498 0.9965 0.1665  -0.0137 0.3333  257 HIS B O   
299  C CB  . HIS A 42  ? 1.5398 1.1311 0.9041 0.1287  0.0194  0.2744  257 HIS B CB  
300  C CG  . HIS A 42  ? 1.5612 1.1959 0.9226 0.1165  0.0321  0.2395  257 HIS B CG  
301  N ND1 . HIS A 42  ? 1.5354 1.2419 0.8723 0.1184  0.0356  0.2302  257 HIS B ND1 
302  C CD2 . HIS A 42  ? 1.4668 1.0842 0.8475 0.1058  0.0394  0.2088  257 HIS B CD2 
303  C CE1 . HIS A 42  ? 1.4792 1.2086 0.8261 0.1118  0.0447  0.1959  257 HIS B CE1 
304  N NE2 . HIS A 42  ? 1.4771 1.1543 0.8484 0.1036  0.0465  0.1849  257 HIS B NE2 
305  N N   . PRO A 49  ? 1.5852 1.1794 1.4288 0.5828  -0.2159 0.1096  264 PRO B N   
306  C CA  . PRO A 49  ? 1.5297 1.1965 1.4310 0.5960  -0.2129 0.0492  264 PRO B CA  
307  C C   . PRO A 49  ? 1.4625 1.1913 1.3434 0.5660  -0.2108 0.0260  264 PRO B C   
308  O O   . PRO A 49  ? 1.4622 1.1393 1.2904 0.5262  -0.1953 0.0423  264 PRO B O   
309  C CB  . PRO A 49  ? 1.5617 1.1522 1.4915 0.5847  -0.1831 0.0250  264 PRO B CB  
310  C CG  . PRO A 49  ? 1.6822 1.1633 1.5713 0.5609  -0.1729 0.0723  264 PRO B CG  
311  C CD  . PRO A 49  ? 1.6832 1.1667 1.5315 0.5719  -0.1960 0.1289  264 PRO B CD  
312  N N   . PRO A 50  ? 1.4145 1.2532 1.3478 0.5826  -0.2222 -0.0170 265 PRO B N   
313  C CA  . PRO A 50  ? 1.3236 1.2316 1.2627 0.5205  -0.2039 -0.0489 265 PRO B CA  
314  C C   . PRO A 50  ? 1.2774 1.1624 1.2373 0.4853  -0.1655 -0.0814 265 PRO B C   
315  O O   . PRO A 50  ? 1.2804 1.1326 1.2714 0.5143  -0.1553 -0.0981 265 PRO B O   
316  C CB  . PRO A 50  ? 1.2562 1.2970 1.2541 0.5450  -0.2294 -0.0771 265 PRO B CB  
317  C CG  . PRO A 50  ? 1.2871 1.2830 1.3167 0.6047  -0.2314 -0.0768 265 PRO B CG  
318  C CD  . PRO A 50  ? 1.3527 1.2915 1.3383 0.6240  -0.2497 -0.0304 265 PRO B CD  
319  N N   . LEU A 51  ? 1.2086 1.1019 1.1433 0.4247  -0.1460 -0.0878 266 LEU B N   
320  C CA  . LEU A 51  ? 1.1356 1.0040 1.0715 0.3856  -0.1114 -0.1095 266 LEU B CA  
321  C C   . LEU A 51  ? 1.1047 1.0609 1.1062 0.3897  -0.0971 -0.1560 266 LEU B C   
322  O O   . LEU A 51  ? 1.0957 1.1421 1.1473 0.4154  -0.1125 -0.1735 266 LEU B O   
323  C CB  . LEU A 51  ? 1.0605 0.9283 0.9573 0.3277  -0.0997 -0.1026 266 LEU B CB  
324  C CG  . LEU A 51  ? 1.0625 0.8687 0.8954 0.3153  -0.1085 -0.0646 266 LEU B CG  
325  C CD1 . LEU A 51  ? 0.9887 0.8309 0.8030 0.2732  -0.1086 -0.0695 266 LEU B CD1 
326  C CD2 . LEU A 51  ? 1.0353 0.7499 0.8343 0.3016  -0.0881 -0.0487 266 LEU B CD2 
327  N N   . GLU A 52  ? 1.0320 0.9719 1.0336 0.3639  -0.0667 -0.1779 267 GLU B N   
328  C CA  . GLU A 52  ? 0.9985 1.0303 1.0553 0.3645  -0.0478 -0.2219 267 GLU B CA  
329  C C   . GLU A 52  ? 0.9254 1.0477 0.9938 0.3137  -0.0387 -0.2279 267 GLU B C   
330  O O   . GLU A 52  ? 0.9222 1.0152 0.9495 0.2737  -0.0415 -0.2036 267 GLU B O   
331  C CB  . GLU A 52  ? 1.0202 1.0123 1.0686 0.3561  -0.0188 -0.2470 267 GLU B CB  
332  C CG  . GLU A 52  ? 1.0792 0.9784 1.1281 0.4041  -0.0261 -0.2503 267 GLU B CG  
333  C CD  . GLU A 52  ? 1.1665 1.0473 1.2202 0.4003  0.0005  -0.2919 267 GLU B CD  
334  O OE1 . GLU A 52  ? 1.1682 1.1448 1.2518 0.3920  0.0217  -0.3311 267 GLU B OE1 
335  O OE2 . GLU A 52  ? 1.2402 1.0147 1.2675 0.4032  0.0009  -0.2867 267 GLU B OE2 
336  N N   . SER A 53  ? 0.9517 1.1842 1.0793 0.3156  -0.0270 -0.2614 268 SER B N   
337  C CA  . SER A 53  ? 0.9140 1.2342 1.0605 0.2621  -0.0141 -0.2669 268 SER B CA  
338  C C   . SER A 53  ? 0.9083 1.2368 1.0370 0.2208  0.0239  -0.2770 268 SER B C   
339  O O   . SER A 53  ? 0.9396 1.2550 1.0668 0.2424  0.0417  -0.2988 268 SER B O   
340  C CB  . SER A 53  ? 0.9112 1.3657 1.1374 0.2802  -0.0208 -0.2953 268 SER B CB  
341  O OG  . SER A 53  ? 0.9703 1.4250 1.2189 0.3403  -0.0562 -0.2932 268 SER B OG  
342  N N   . VAL A 54  ? 0.8217 1.1697 0.9345 0.1621  0.0346  -0.2611 269 VAL B N   
343  C CA  . VAL A 54  ? 0.7868 1.1748 0.8904 0.1185  0.0700  -0.2658 269 VAL B CA  
344  C C   . VAL A 54  ? 0.8222 1.2856 0.9557 0.0664  0.0749  -0.2574 269 VAL B C   
345  O O   . VAL A 54  ? 0.8055 1.2328 0.9287 0.0456  0.0527  -0.2373 269 VAL B O   
346  C CB  . VAL A 54  ? 0.7813 1.0715 0.8114 0.0947  0.0795  -0.2419 269 VAL B CB  
347  C CG1 . VAL A 54  ? 0.8001 1.1399 0.8156 0.0476  0.1125  -0.2385 269 VAL B CG1 
348  C CG2 . VAL A 54  ? 0.8207 1.0428 0.8291 0.1372  0.0771  -0.2549 269 VAL B CG2 
349  N N   . ASP A 55  ? 0.7131 1.2831 0.8847 0.0437  0.1049  -0.2749 270 ASP B N   
350  C CA  . ASP A 55  ? 0.7262 1.3783 0.9381 -0.0108 0.1129  -0.2682 270 ASP B CA  
351  C C   . ASP A 55  ? 0.7789 1.3626 0.9346 -0.0725 0.1246  -0.2285 270 ASP B C   
352  O O   . ASP A 55  ? 0.7624 1.3159 0.8682 -0.0845 0.1484  -0.2151 270 ASP B O   
353  C CB  . ASP A 55  ? 0.6745 1.4739 0.9479 -0.0162 0.1452  -0.2980 270 ASP B CB  
354  C CG  . ASP A 55  ? 0.7411 1.6289 1.0585 -0.0839 0.1591  -0.2876 270 ASP B CG  
355  O OD1 . ASP A 55  ? 0.7931 1.6431 1.0683 -0.1429 0.1788  -0.2532 270 ASP B OD1 
356  O OD2 . ASP A 55  ? 0.7089 1.7024 1.1049 -0.0789 0.1486  -0.3123 270 ASP B OD2 
357  N N   . VAL A 56  ? 0.8320 1.3908 0.9958 -0.1090 0.1054  -0.2117 271 VAL B N   
358  C CA  . VAL A 56  ? 0.8777 1.3475 0.9874 -0.1578 0.1089  -0.1737 271 VAL B CA  
359  C C   . VAL A 56  ? 0.9239 1.4425 1.0274 -0.2097 0.1489  -0.1540 271 VAL B C   
360  O O   . VAL A 56  ? 0.9641 1.4082 1.0055 -0.2320 0.1592  -0.1199 271 VAL B O   
361  C CB  . VAL A 56  ? 0.8606 1.2995 0.9894 -0.1848 0.0791  -0.1699 271 VAL B CB  
362  C CG1 . VAL A 56  ? 0.8500 1.4137 1.0651 -0.2095 0.0785  -0.1952 271 VAL B CG1 
363  C CG2 . VAL A 56  ? 0.9148 1.2587 0.9962 -0.2339 0.0822  -0.1337 271 VAL B CG2 
364  N N   . ARG A 57  ? 0.8239 1.4751 0.9901 -0.2272 0.1725  -0.1734 272 ARG B N   
365  C CA  . ARG A 57  ? 0.8717 1.5853 1.0305 -0.2786 0.2151  -0.1519 272 ARG B CA  
366  C C   . ARG A 57  ? 0.8988 1.5777 0.9848 -0.2574 0.2356  -0.1410 272 ARG B C   
367  O O   . ARG A 57  ? 0.9522 1.6232 0.9934 -0.3002 0.2609  -0.1038 272 ARG B O   
368  C CB  . ARG A 57  ? 0.7995 1.6828 1.0420 -0.2887 0.2399  -0.1838 272 ARG B CB  
369  C CG  . ARG A 57  ? 0.7905 1.7365 1.1179 -0.3068 0.2172  -0.2040 272 ARG B CG  
370  C CD  . ARG A 57  ? 0.7563 1.8884 1.1745 -0.3067 0.2411  -0.2416 272 ARG B CD  
371  N NE  . ARG A 57  ? 0.7306 1.9240 1.2211 -0.2601 0.2062  -0.2841 272 ARG B NE  
372  C CZ  . ARG A 57  ? 0.7280 1.9993 1.2946 -0.2948 0.1904  -0.2975 272 ARG B CZ  
373  N NH1 . ARG A 57  ? 0.7642 2.0534 1.3501 -0.3821 0.2073  -0.2728 272 ARG B NH1 
374  N NH2 . ARG A 57  ? 0.7023 2.0342 1.3275 -0.2414 0.1553  -0.3359 272 ARG B NH2 
375  N N   . GLN A 58  ? 0.9078 1.5647 0.9806 -0.1928 0.2234  -0.1721 273 GLN B N   
376  C CA  . GLN A 58  ? 0.9444 1.5697 0.9533 -0.1702 0.2377  -0.1724 273 GLN B CA  
377  C C   . GLN A 58  ? 1.0133 1.5226 0.9442 -0.1933 0.2294  -0.1258 273 GLN B C   
378  O O   . GLN A 58  ? 1.1065 1.6168 0.9823 -0.1997 0.2486  -0.1127 273 GLN B O   
379  C CB  . GLN A 58  ? 0.9351 1.5282 0.9498 -0.1009 0.2179  -0.2126 273 GLN B CB  
380  C CG  . GLN A 58  ? 0.9221 1.6225 0.9859 -0.0624 0.2356  -0.2636 273 GLN B CG  
381  C CD  . GLN A 58  ? 0.9960 1.6308 1.0427 -0.0008 0.2199  -0.2950 273 GLN B CD  
382  O OE1 . GLN A 58  ? 1.0404 1.5679 1.0292 0.0021  0.2060  -0.2767 273 GLN B OE1 
383  N NE2 . GLN A 58  ? 1.0493 1.7479 1.1499 0.0484  0.2220  -0.3429 273 GLN B NE2 
384  N N   . ILE A 59  ? 1.0491 1.4630 0.9730 -0.2005 0.1992  -0.1043 274 ILE B N   
385  C CA  . ILE A 59  ? 1.0814 1.3820 0.9370 -0.2062 0.1859  -0.0683 274 ILE B CA  
386  C C   . ILE A 59  ? 1.1176 1.3745 0.9631 -0.2605 0.1854  -0.0240 274 ILE B C   
387  O O   . ILE A 59  ? 1.1615 1.3175 0.9601 -0.2616 0.1686  0.0047  274 ILE B O   
388  C CB  . ILE A 59  ? 1.0560 1.2685 0.9004 -0.1619 0.1519  -0.0812 274 ILE B CB  
389  C CG1 . ILE A 59  ? 1.0055 1.2115 0.8984 -0.1607 0.1272  -0.0923 274 ILE B CG1 
390  C CG2 . ILE A 59  ? 0.9651 1.1968 0.8107 -0.1125 0.1532  -0.1175 274 ILE B CG2 
391  C CD1 . ILE A 59  ? 0.9229 1.0773 0.8133 -0.1106 0.0989  -0.1108 274 ILE B CD1 
392  N N   . TYR A 60  ? 1.0851 1.4148 0.9775 -0.3060 0.2033  -0.0187 275 TYR B N   
393  C CA  . TYR A 60  ? 1.1546 1.4341 1.0388 -0.3646 0.2055  0.0259  275 TYR B CA  
394  C C   . TYR A 60  ? 1.2045 1.4306 1.0112 -0.3792 0.2196  0.0759  275 TYR B C   
395  O O   . TYR A 60  ? 1.2247 1.3387 0.9926 -0.3853 0.2005  0.1089  275 TYR B O   
396  C CB  . TYR A 60  ? 1.1253 1.5103 1.0749 -0.4190 0.2302  0.0247  275 TYR B CB  
397  C CG  . TYR A 60  ? 1.0778 1.5058 1.1082 -0.4181 0.2089  -0.0159 275 TYR B CG  
398  C CD1 . TYR A 60  ? 1.0576 1.4054 1.0886 -0.3829 0.1677  -0.0362 275 TYR B CD1 
399  C CD2 . TYR A 60  ? 1.0432 1.6046 1.1493 -0.4517 0.2299  -0.0348 275 TYR B CD2 
400  C CE1 . TYR A 60  ? 1.0086 1.4042 1.1076 -0.3797 0.1450  -0.0731 275 TYR B CE1 
401  C CE2 . TYR A 60  ? 1.0160 1.6294 1.1983 -0.4486 0.2066  -0.0738 275 TYR B CE2 
402  C CZ  . TYR A 60  ? 0.9879 1.5162 1.1635 -0.4116 0.1626  -0.0925 275 TYR B CZ  
403  O OH  . TYR A 60  ? 0.9673 1.5533 1.2122 -0.4058 0.1359  -0.1309 275 TYR B OH  
404  N N   . ASP A 61  ? 1.2211 1.5311 1.0030 -0.3806 0.2515  0.0800  276 ASP B N   
405  C CA  . ASP A 61  ? 1.2451 1.5263 0.9506 -0.3965 0.2661  0.1304  276 ASP B CA  
406  C C   . ASP A 61  ? 1.2766 1.4677 0.9206 -0.3502 0.2400  0.1342  276 ASP B C   
407  O O   . ASP A 61  ? 1.2998 1.4703 0.8776 -0.3556 0.2466  0.1747  276 ASP B O   
408  C CB  . ASP A 61  ? 1.2573 1.6690 0.9496 -0.4062 0.3070  0.1253  276 ASP B CB  
409  C CG  . ASP A 61  ? 1.2534 1.7347 0.9615 -0.3503 0.3081  0.0599  276 ASP B CG  
410  O OD1 . ASP A 61  ? 1.2037 1.6251 0.9265 -0.3054 0.2775  0.0264  276 ASP B OD1 
411  O OD2 . ASP A 61  ? 1.3307 1.9221 1.0394 -0.3488 0.3379  0.0415  276 ASP B OD2 
412  N N   . LYS A 62  ? 1.2133 1.3583 0.8765 -0.3061 0.2113  0.0959  277 LYS B N   
413  C CA  . LYS A 62  ? 1.2032 1.2678 0.8177 -0.2673 0.1869  0.0989  277 LYS B CA  
414  C C   . LYS A 62  ? 1.1623 1.1113 0.7691 -0.2692 0.1581  0.1240  277 LYS B C   
415  O O   . LYS A 62  ? 1.1131 0.9995 0.6820 -0.2387 0.1385  0.1301  277 LYS B O   
416  C CB  . LYS A 62  ? 1.1603 1.2433 0.7952 -0.2188 0.1760  0.0449  277 LYS B CB  
417  C CG  . LYS A 62  ? 1.1492 1.3427 0.8140 -0.2114 0.2011  0.0055  277 LYS B CG  
418  C CD  . LYS A 62  ? 1.1172 1.3050 0.7830 -0.1621 0.1899  -0.0397 277 LYS B CD  
419  C CE  . LYS A 62  ? 1.1080 1.2805 0.7108 -0.1515 0.1900  -0.0328 277 LYS B CE  
420  N NZ  . LYS A 62  ? 1.0366 1.3046 0.6152 -0.1650 0.2207  -0.0387 277 LYS B NZ  
421  N N   . PHE A 63  ? 1.1789 1.1010 0.8683 -0.3255 0.2563  0.0451  278 PHE B N   
422  C CA  . PHE A 63  ? 1.2377 1.0718 0.9155 -0.3343 0.2321  0.0564  278 PHE B CA  
423  C C   . PHE A 63  ? 1.3003 1.1000 0.9552 -0.3861 0.2314  0.0790  278 PHE B C   
424  O O   . PHE A 63  ? 1.3326 1.1919 0.9931 -0.4136 0.2488  0.0849  278 PHE B O   
425  C CB  . PHE A 63  ? 1.1671 1.0355 0.9038 -0.3138 0.2177  0.0298  278 PHE B CB  
426  C CG  . PHE A 63  ? 1.0629 0.9524 0.8221 -0.2568 0.2087  0.0103  278 PHE B CG  
427  C CD1 . PHE A 63  ? 1.0473 1.0197 0.8354 -0.2362 0.2227  -0.0095 278 PHE B CD1 
428  C CD2 . PHE A 63  ? 0.9593 0.7841 0.7072 -0.2244 0.1858  0.0118  278 PHE B CD2 
429  C CE1 . PHE A 63  ? 0.9979 0.9728 0.7998 -0.1867 0.2109  -0.0253 278 PHE B CE1 
430  C CE2 . PHE A 63  ? 0.8870 0.7257 0.6514 -0.1804 0.1779  -0.0015 278 PHE B CE2 
431  C CZ  . PHE A 63  ? 0.8812 0.7871 0.6704 -0.1627 0.1891  -0.0188 278 PHE B CZ  
432  N N   . PRO A 64  ? 1.3785 1.0870 1.0128 -0.3910 0.2053  0.0887  279 PRO B N   
433  C CA  . PRO A 64  ? 1.4735 1.1426 1.0885 -0.4307 0.1963  0.1074  279 PRO B CA  
434  C C   . PRO A 64  ? 1.4789 1.2355 1.1434 -0.4762 0.2125  0.0968  279 PRO B C   
435  O O   . PRO A 64  ? 1.4336 1.2802 1.1505 -0.4730 0.2267  0.0719  279 PRO B O   
436  C CB  . PRO A 64  ? 1.5023 1.0676 1.0959 -0.4170 0.1631  0.1078  279 PRO B CB  
437  C CG  . PRO A 64  ? 1.4108 0.9654 1.0115 -0.3685 0.1561  0.0912  279 PRO B CG  
438  C CD  . PRO A 64  ? 1.3417 0.9922 0.9776 -0.3619 0.1841  0.0777  279 PRO B CD  
439  N N   . GLU A 65  ? 1.5677 1.3013 1.2167 -0.5186 0.2095  0.1150  280 GLU B N   
440  C CA  . GLU A 65  ? 1.6170 1.4379 1.3118 -0.5664 0.2244  0.1072  280 GLU B CA  
441  C C   . GLU A 65  ? 1.6909 1.4562 1.3943 -0.5957 0.2004  0.1039  280 GLU B C   
442  O O   . GLU A 65  ? 1.7260 1.3892 1.3831 -0.6087 0.1811  0.1253  280 GLU B O   
443  C CB  . GLU A 65  ? 1.6183 1.4740 1.2922 -0.5990 0.2449  0.1304  280 GLU B CB  
444  C CG  . GLU A 65  ? 1.5921 1.5519 1.2823 -0.5771 0.2737  0.1205  280 GLU B CG  
445  C CD  . GLU A 65  ? 1.5309 1.6335 1.2911 -0.5943 0.2948  0.0931  280 GLU B CD  
446  O OE1 . GLU A 65  ? 1.5018 1.6230 1.2995 -0.6254 0.2865  0.0825  280 GLU B OE1 
447  O OE2 . GLU A 65  ? 1.4785 1.6767 1.2572 -0.5727 0.3172  0.0791  280 GLU B OE2 
448  N N   . LYS A 66  ? 1.7572 1.5919 1.5201 -0.6041 0.2000  0.0749  281 LYS B N   
449  C CA  . LYS A 66  ? 1.7309 1.5263 1.5092 -0.6314 0.1761  0.0653  281 LYS B CA  
450  C C   . LYS A 66  ? 1.7646 1.4221 1.4946 -0.6008 0.1434  0.0703  281 LYS B C   
451  O O   . LYS A 66  ? 1.7574 1.3753 1.4598 -0.5538 0.1404  0.0725  281 LYS B O   
452  C CB  . LYS A 66  ? 1.7272 1.5296 1.5032 -0.6908 0.1807  0.0829  281 LYS B CB  
453  N N   . LYS A 67  ? 1.7594 1.3487 1.4813 -0.6244 0.1180  0.0691  282 LYS B N   
454  C CA  . LYS A 67  ? 1.7829 1.2408 1.4560 -0.5953 0.0846  0.0725  282 LYS B CA  
455  C C   . LYS A 67  ? 1.7395 1.1713 1.4002 -0.5327 0.0759  0.0596  282 LYS B C   
456  O O   . LYS A 67  ? 1.7761 1.1148 1.3884 -0.4969 0.0561  0.0685  282 LYS B O   
457  C CB  . LYS A 67  ? 1.8824 1.2556 1.4942 -0.6057 0.0804  0.1072  282 LYS B CB  
458  N N   . GLY A 68  ? 1.6772 1.1935 1.3821 -0.5187 0.0899  0.0376  283 GLY B N   
459  C CA  . GLY A 68  ? 1.6496 1.1485 1.3436 -0.4646 0.0865  0.0279  283 GLY B CA  
460  C C   . GLY A 68  ? 1.5700 1.1547 1.2847 -0.4552 0.1187  0.0304  283 GLY B C   
461  O O   . GLY A 68  ? 1.4718 1.0550 1.1804 -0.4028 0.1179  0.0267  283 GLY B O   
462  N N   . GLY A 69  ? 1.5419 1.2180 1.2887 -0.4928 0.1436  0.0336  284 GLY B N   
463  C CA  . GLY A 69  ? 1.4707 1.2386 1.2386 -0.4824 0.1746  0.0325  284 GLY B CA  
464  C C   . GLY A 69  ? 1.3831 1.2699 1.2240 -0.4579 0.1781  -0.0014 284 GLY B C   
465  O O   . GLY A 69  ? 1.3674 1.2765 1.2444 -0.4665 0.1621  -0.0222 284 GLY B O   
466  N N   . LEU A 70  ? 1.2373 1.1990 1.0968 -0.4244 0.1966  -0.0082 285 LEU B N   
467  C CA  . LEU A 70  ? 1.1322 1.1888 1.0508 -0.3840 0.1939  -0.0395 285 LEU B CA  
468  C C   . LEU A 70  ? 1.1312 1.2938 1.1086 -0.4217 0.2008  -0.0600 285 LEU B C   
469  O O   . LEU A 70  ? 1.1069 1.3109 1.1264 -0.4016 0.1829  -0.0852 285 LEU B O   
470  C CB  . LEU A 70  ? 1.0615 1.1650 0.9816 -0.3420 0.2097  -0.0438 285 LEU B CB  
471  C CG  . LEU A 70  ? 0.9672 1.1276 0.9301 -0.2856 0.1978  -0.0717 285 LEU B CG  
472  C CD1 . LEU A 70  ? 0.9060 1.0001 0.8622 -0.2608 0.1690  -0.0735 285 LEU B CD1 
473  C CD2 . LEU A 70  ? 0.9271 1.0959 0.8777 -0.2401 0.2054  -0.0745 285 LEU B CD2 
474  N N   . ARG A 71  ? 1.1210 1.3356 1.1020 -0.4777 0.2265  -0.0495 286 ARG B N   
475  C CA  . ARG A 71  ? 1.0844 1.4285 1.1316 -0.5114 0.2366  -0.0728 286 ARG B CA  
476  C C   . ARG A 71  ? 1.1215 1.4364 1.1835 -0.5596 0.2159  -0.0772 286 ARG B C   
477  O O   . ARG A 71  ? 1.0604 1.4703 1.1845 -0.5633 0.2078  -0.1071 286 ARG B O   
478  C CB  . ARG A 71  ? 1.1022 1.5207 1.1487 -0.5450 0.2676  -0.0612 286 ARG B CB  
479  C CG  . ARG A 71  ? 1.1968 1.5231 1.1872 -0.5921 0.2653  -0.0237 286 ARG B CG  
480  C CD  . ARG A 71  ? 1.1755 1.5896 1.1725 -0.6169 0.2905  -0.0161 286 ARG B CD  
481  N NE  . ARG A 71  ? 1.2180 1.6180 1.1717 -0.5890 0.3074  -0.0007 286 ARG B NE  
482  C CZ  . ARG A 71  ? 1.1483 1.6504 1.1161 -0.5824 0.3314  -0.0079 286 ARG B CZ  
483  N NH1 . ARG A 71  ? 1.0292 1.6599 1.0543 -0.5996 0.3425  -0.0303 286 ARG B NH1 
484  N NH2 . ARG A 71  ? 1.2128 1.6899 1.1362 -0.5550 0.3426  0.0050  286 ARG B NH2 
485  N N   . GLU A 72  ? 1.1863 1.3680 1.1899 -0.5883 0.2019  -0.0502 287 GLU B N   
486  C CA  . GLU A 72  ? 1.2228 1.3510 1.2312 -0.6146 0.1722  -0.0588 287 GLU B CA  
487  C C   . GLU A 72  ? 1.2094 1.3393 1.2430 -0.5638 0.1459  -0.0896 287 GLU B C   
488  O O   . GLU A 72  ? 1.2051 1.3730 1.2784 -0.5787 0.1266  -0.1151 287 GLU B O   
489  C CB  . GLU A 72  ? 1.3604 1.3317 1.2945 -0.6259 0.1544  -0.0272 287 GLU B CB  
490  C CG  . GLU A 72  ? 1.4184 1.3574 1.3531 -0.6752 0.1383  -0.0222 287 GLU B CG  
491  C CD  . GLU A 72  ? 1.4235 1.4861 1.4063 -0.7194 0.1610  -0.0244 287 GLU B CD  
492  O OE1 . GLU A 72  ? 1.4160 1.5550 1.4044 -0.7132 0.1909  -0.0162 287 GLU B OE1 
493  O OE2 . GLU A 72  ? 1.3798 1.4639 1.3932 -0.7592 0.1484  -0.0352 287 GLU B OE2 
494  N N   . LEU A 73  ? 1.2325 1.3212 1.2400 -0.4953 0.1412  -0.0862 288 LEU B N   
495  C CA  . LEU A 73  ? 1.1866 1.2695 1.2064 -0.4363 0.1151  -0.1084 288 LEU B CA  
496  C C   . LEU A 73  ? 1.1298 1.3448 1.2149 -0.4088 0.1166  -0.1375 288 LEU B C   
497  O O   . LEU A 73  ? 1.1137 1.3665 1.2317 -0.4036 0.0948  -0.1627 288 LEU B O   
498  C CB  . LEU A 73  ? 1.1287 1.1359 1.1024 -0.3792 0.1122  -0.0932 288 LEU B CB  
499  C CG  . LEU A 73  ? 1.2180 1.0920 1.1293 -0.3832 0.0974  -0.0745 288 LEU B CG  
500  C CD1 . LEU A 73  ? 1.1760 1.0017 1.0482 -0.3403 0.1042  -0.0558 288 LEU B CD1 
501  C CD2 . LEU A 73  ? 1.1666 1.0026 1.0762 -0.3647 0.0661  -0.0948 288 LEU B CD2 
502  N N   . TYR A 74  ? 0.9773 1.2622 1.0788 -0.3859 0.1391  -0.1368 289 TYR B N   
503  C CA  . TYR A 74  ? 0.9336 1.3391 1.0932 -0.3505 0.1373  -0.1663 289 TYR B CA  
504  C C   . TYR A 74  ? 1.0023 1.5113 1.2212 -0.3963 0.1352  -0.1903 289 TYR B C   
505  O O   . TYR A 74  ? 0.9815 1.5738 1.2473 -0.3652 0.1187  -0.2197 289 TYR B O   
506  C CB  . TYR A 74  ? 0.8691 1.3324 1.0347 -0.3246 0.1623  -0.1651 289 TYR B CB  
507  C CG  . TYR A 74  ? 0.7870 1.3480 0.9995 -0.2688 0.1536  -0.1955 289 TYR B CG  
508  C CD1 . TYR A 74  ? 0.7780 1.4777 1.0550 -0.2829 0.1595  -0.2241 289 TYR B CD1 
509  C CD2 . TYR A 74  ? 0.7426 1.2572 0.9340 -0.2024 0.1377  -0.1955 289 TYR B CD2 
510  C CE1 . TYR A 74  ? 0.7566 1.5431 1.0739 -0.2238 0.1471  -0.2542 289 TYR B CE1 
511  C CE2 . TYR A 74  ? 0.7061 1.2940 0.9321 -0.1484 0.1252  -0.2212 289 TYR B CE2 
512  C CZ  . TYR A 74  ? 0.7215 1.4435 1.0094 -0.1552 0.1286  -0.2516 289 TYR B CZ  
513  O OH  . TYR A 74  ? 0.7017 1.4941 1.0214 -0.0937 0.1119  -0.2794 289 TYR B OH  
514  N N   . ASP A 75  ? 1.1102 1.6151 1.3264 -0.4715 0.1498  -0.1774 290 ASP B N   
515  C CA  . ASP A 75  ? 1.0308 1.6344 1.3050 -0.5271 0.1479  -0.1989 290 ASP B CA  
516  C C   . ASP A 75  ? 1.0690 1.6250 1.3468 -0.5364 0.1114  -0.2153 290 ASP B C   
517  O O   . ASP A 75  ? 1.0710 1.7237 1.4066 -0.5646 0.1010  -0.2432 290 ASP B O   
518  C CB  . ASP A 75  ? 1.0792 1.6811 1.3396 -0.6059 0.1745  -0.1737 290 ASP B CB  
519  C CG  . ASP A 75  ? 1.0871 1.8223 1.3832 -0.6015 0.2032  -0.1797 290 ASP B CG  
520  O OD1 . ASP A 75  ? 1.0261 1.8907 1.3875 -0.5854 0.1979  -0.2138 290 ASP B OD1 
521  O OD2 . ASP A 75  ? 1.1333 1.8440 1.3892 -0.6079 0.2282  -0.1529 290 ASP B OD2 
522  N N   . ARG A 76  ? 1.2675 1.6853 1.4864 -0.5122 0.0909  -0.2018 291 ARG B N   
523  C CA  . ARG A 76  ? 1.2910 1.6664 1.5078 -0.5043 0.0542  -0.2225 291 ARG B CA  
524  C C   . ARG A 76  ? 1.2384 1.6426 1.4637 -0.4233 0.0347  -0.2413 291 ARG B C   
525  O O   . ARG A 76  ? 1.2400 1.6172 1.4594 -0.4070 0.0041  -0.2596 291 ARG B O   
526  C CB  . ARG A 76  ? 1.3551 1.5698 1.5018 -0.5216 0.0406  -0.2018 291 ARG B CB  
527  C CG  . ARG A 76  ? 1.4351 1.6016 1.5628 -0.6047 0.0547  -0.1791 291 ARG B CG  
528  C CD  . ARG A 76  ? 1.5589 1.5624 1.6193 -0.6211 0.0309  -0.1664 291 ARG B CD  
529  N NE  . ARG A 76  ? 1.6199 1.5426 1.6342 -0.5468 0.0169  -0.1638 291 ARG B NE  
530  C CZ  . ARG A 76  ? 1.6337 1.4684 1.5923 -0.5249 0.0269  -0.1346 291 ARG B CZ  
531  N NH1 . ARG A 76  ? 1.6291 1.4362 1.5637 -0.5670 0.0502  -0.1035 291 ARG B NH1 
532  N NH2 . ARG A 76  ? 1.6010 1.3799 1.5263 -0.4600 0.0132  -0.1367 291 ARG B NH2 
533  N N   . GLY A 77  ? 1.0583 1.5133 1.2932 -0.3734 0.0503  -0.2371 292 GLY B N   
534  C CA  . GLY A 77  ? 0.9362 1.4229 1.1792 -0.3011 0.0322  -0.2518 292 GLY B CA  
535  C C   . GLY A 77  ? 0.9294 1.3076 1.1169 -0.2640 0.0111  -0.2419 292 GLY B C   
536  O O   . GLY A 77  ? 0.9697 1.2469 1.1127 -0.2871 0.0102  -0.2260 292 GLY B O   
537  N N   . PRO A 78  ? 0.8281 1.2277 1.0151 -0.2037 -0.0071 -0.2511 293 PRO B N   
538  C CA  . PRO A 78  ? 0.7236 1.2279 0.9542 -0.1639 -0.0125 -0.2695 293 PRO B CA  
539  C C   . PRO A 78  ? 0.6983 1.1973 0.9177 -0.1276 0.0070  -0.2524 293 PRO B C   
540  O O   . PRO A 78  ? 0.7127 1.1214 0.8821 -0.1048 0.0104  -0.2276 293 PRO B O   
541  C CB  . PRO A 78  ? 0.7053 1.1998 0.9191 -0.1175 -0.0455 -0.2804 293 PRO B CB  
542  C CG  . PRO A 78  ? 0.7555 1.1328 0.9072 -0.1180 -0.0496 -0.2607 293 PRO B CG  
543  C CD  . PRO A 78  ? 0.8081 1.1240 0.9445 -0.1695 -0.0268 -0.2439 293 PRO B CD  
544  N N   . PRO A 79  ? 0.6445 1.2435 0.9105 -0.1200 0.0180  -0.2684 294 PRO B N   
545  C CA  . PRO A 79  ? 0.6254 1.2165 0.8792 -0.0897 0.0370  -0.2564 294 PRO B CA  
546  C C   . PRO A 79  ? 0.6371 1.1559 0.8483 -0.0288 0.0215  -0.2418 294 PRO B C   
547  O O   . PRO A 79  ? 0.6718 1.1456 0.8571 -0.0123 0.0356  -0.2257 294 PRO B O   
548  C CB  . PRO A 79  ? 0.5933 1.3232 0.9103 -0.0781 0.0417  -0.2876 294 PRO B CB  
549  C CG  . PRO A 79  ? 0.5669 1.3713 0.9252 -0.0805 0.0156  -0.3151 294 PRO B CG  
550  C CD  . PRO A 79  ? 0.6006 1.3316 0.9337 -0.1303 0.0095  -0.3031 294 PRO B CD  
551  N N   . HIS A 80  ? 0.6622 1.1701 0.8634 0.0034  -0.0077 -0.2466 295 HIS B N   
552  C CA  . HIS A 80  ? 0.6326 1.0698 0.7885 0.0549  -0.0222 -0.2278 295 HIS B CA  
553  C C   . HIS A 80  ? 0.6517 0.9806 0.7526 0.0398  -0.0141 -0.1968 295 HIS B C   
554  O O   . HIS A 80  ? 0.6519 0.9198 0.7136 0.0721  -0.0209 -0.1765 295 HIS B O   
555  C CB  . HIS A 80  ? 0.6740 1.1403 0.8315 0.0941  -0.0560 -0.2407 295 HIS B CB  
556  C CG  . HIS A 80  ? 0.6921 1.1373 0.8336 0.0720  -0.0692 -0.2415 295 HIS B CG  
557  N ND1 . HIS A 80  ? 0.7014 1.1919 0.8767 0.0242  -0.0672 -0.2620 295 HIS B ND1 
558  C CD2 . HIS A 80  ? 0.7322 1.1162 0.8250 0.0907  -0.0850 -0.2259 295 HIS B CD2 
559  C CE1 . HIS A 80  ? 0.7188 1.1709 0.8660 0.0185  -0.0839 -0.2623 295 HIS B CE1 
560  N NE2 . HIS A 80  ? 0.7490 1.1425 0.8464 0.0599  -0.0935 -0.2411 295 HIS B NE2 
561  N N   . ALA A 81  ? 0.6981 1.0027 0.7951 -0.0086 -0.0010 -0.1930 296 ALA B N   
562  C CA  . ALA A 81  ? 0.6955 0.9061 0.7443 -0.0212 0.0063  -0.1683 296 ALA B CA  
563  C C   . ALA A 81  ? 0.7139 0.8823 0.7454 -0.0302 0.0303  -0.1487 296 ALA B C   
564  O O   . ALA A 81  ? 0.7360 0.8314 0.7279 -0.0307 0.0342  -0.1281 296 ALA B O   
565  C CB  . ALA A 81  ? 0.7443 0.9376 0.7917 -0.0642 0.0040  -0.1757 296 ALA B CB  
566  N N   . PHE A 82  ? 0.7016 0.9203 0.7612 -0.0360 0.0459  -0.1568 297 PHE B N   
567  C CA  . PHE A 82  ? 0.6883 0.8750 0.7306 -0.0512 0.0693  -0.1417 297 PHE B CA  
568  C C   . PHE A 82  ? 0.6824 0.8541 0.7127 -0.0096 0.0691  -0.1368 297 PHE B C   
569  O O   . PHE A 82  ? 0.6442 0.8688 0.6995 0.0225  0.0605  -0.1544 297 PHE B O   
570  C CB  . PHE A 82  ? 0.6905 0.9433 0.7649 -0.0905 0.0898  -0.1533 297 PHE B CB  
571  C CG  . PHE A 82  ? 0.7233 0.9699 0.8015 -0.1416 0.0905  -0.1532 297 PHE B CG  
572  C CD1 . PHE A 82  ? 0.7304 1.0262 0.8407 -0.1497 0.0730  -0.1740 297 PHE B CD1 
573  C CD2 . PHE A 82  ? 0.7405 0.9235 0.7855 -0.1803 0.1045  -0.1327 297 PHE B CD2 
574  C CE1 . PHE A 82  ? 0.8032 1.0827 0.9145 -0.1997 0.0698  -0.1760 297 PHE B CE1 
575  C CE2 . PHE A 82  ? 0.8279 0.9874 0.8696 -0.2276 0.1006  -0.1319 297 PHE B CE2 
576  C CZ  . PHE A 82  ? 0.8320 1.0381 0.9077 -0.2393 0.0832  -0.1544 297 PHE B CZ  
577  N N   . PHE A 83  ? 0.6582 0.7574 0.6504 -0.0100 0.0763  -0.1150 298 PHE B N   
578  C CA  . PHE A 83  ? 0.6936 0.7617 0.6685 0.0226  0.0737  -0.1086 298 PHE B CA  
579  C C   . PHE A 83  ? 0.6876 0.7247 0.6420 0.0047  0.0931  -0.0982 298 PHE B C   
580  O O   . PHE A 83  ? 0.6757 0.6862 0.6142 -0.0275 0.1037  -0.0860 298 PHE B O   
581  C CB  . PHE A 83  ? 0.7026 0.7098 0.6470 0.0440  0.0562  -0.0902 298 PHE B CB  
582  C CG  . PHE A 83  ? 0.7026 0.7350 0.6569 0.0685  0.0348  -0.0978 298 PHE B CG  
583  C CD1 . PHE A 83  ? 0.6955 0.7428 0.6533 0.0550  0.0277  -0.1009 298 PHE B CD1 
584  C CD2 . PHE A 83  ? 0.7008 0.7383 0.6570 0.1078  0.0185  -0.1035 298 PHE B CD2 
585  C CE1 . PHE A 83  ? 0.7114 0.7854 0.6745 0.0793  0.0061  -0.1088 298 PHE B CE1 
586  C CE2 . PHE A 83  ? 0.7746 0.8331 0.7341 0.1338  -0.0044 -0.1088 298 PHE B CE2 
587  C CZ  . PHE A 83  ? 0.7301 0.8106 0.6931 0.1190  -0.0099 -0.1111 298 PHE B CZ  
588  N N   . LEU A 84  ? 0.6897 0.7255 0.6406 0.0289  0.0944  -0.1044 299 LEU B N   
589  C CA  . LEU A 84  ? 0.6749 0.6786 0.6014 0.0200  0.1082  -0.0966 299 LEU B CA  
590  C C   . LEU A 84  ? 0.6872 0.6250 0.5875 0.0443  0.0936  -0.0855 299 LEU B C   
591  O O   . LEU A 84  ? 0.6816 0.6146 0.5862 0.0770  0.0771  -0.0942 299 LEU B O   
592  C CB  . LEU A 84  ? 0.6535 0.7196 0.5969 0.0243  0.1235  -0.1184 299 LEU B CB  
593  C CG  . LEU A 84  ? 0.6452 0.6884 0.5630 0.0307  0.1327  -0.1197 299 LEU B CG  
594  C CD1 . LEU A 84  ? 0.6794 0.6799 0.5653 -0.0042 0.1455  -0.0965 299 LEU B CD1 
595  C CD2 . LEU A 84  ? 0.6640 0.7907 0.6028 0.0392  0.1484  -0.1470 299 LEU B CD2 
596  N N   . VAL A 85  ? 0.6778 0.5642 0.5502 0.0277  0.0975  -0.0663 300 VAL B N   
597  C CA  . VAL A 85  ? 0.7298 0.5588 0.5794 0.0397  0.0856  -0.0541 300 VAL B CA  
598  C C   . VAL A 85  ? 0.7285 0.5433 0.5614 0.0332  0.0953  -0.0570 300 VAL B C   
599  O O   . VAL A 85  ? 0.7408 0.5564 0.5621 0.0105  0.1085  -0.0496 300 VAL B O   
600  C CB  . VAL A 85  ? 0.7482 0.5439 0.5830 0.0275  0.0803  -0.0318 300 VAL B CB  
601  C CG1 . VAL A 85  ? 0.7482 0.4962 0.5639 0.0329  0.0697  -0.0179 300 VAL B CG1 
602  C CG2 . VAL A 85  ? 0.6784 0.4945 0.5255 0.0343  0.0712  -0.0316 300 VAL B CG2 
603  N N   . LYS A 86  ? 0.7398 0.5410 0.5686 0.0553  0.0868  -0.0701 301 LYS B N   
604  C CA  . LYS A 86  ? 0.7180 0.4980 0.5262 0.0532  0.0902  -0.0750 301 LYS B CA  
605  C C   . LYS A 86  ? 0.7765 0.4955 0.5668 0.0481  0.0753  -0.0577 301 LYS B C   
606  O O   . LYS A 86  ? 0.7680 0.4536 0.5577 0.0611  0.0575  -0.0539 301 LYS B O   
607  C CB  . LYS A 86  ? 0.7761 0.5754 0.5890 0.0822  0.0866  -0.1042 301 LYS B CB  
608  C CG  . LYS A 86  ? 0.8513 0.6081 0.6396 0.0907  0.0777  -0.1137 301 LYS B CG  
609  C CD  . LYS A 86  ? 0.8593 0.6453 0.6315 0.0764  0.0972  -0.1196 301 LYS B CD  
610  C CE  . LYS A 86  ? 0.9253 0.7759 0.7059 0.0957  0.1101  -0.1496 301 LYS B CE  
611  N NZ  . LYS A 86  ? 0.9702 0.8048 0.7386 0.1304  0.0957  -0.1809 301 LYS B NZ  
612  N N   . PHE A 87  ? 0.7973 0.5039 0.5721 0.0278  0.0815  -0.0456 302 PHE B N   
613  C CA  . PHE A 87  ? 0.7983 0.4640 0.5612 0.0187  0.0693  -0.0320 302 PHE B CA  
614  C C   . PHE A 87  ? 0.8454 0.4905 0.5923 0.0215  0.0633  -0.0461 302 PHE B C   
615  O O   . PHE A 87  ? 0.8374 0.5044 0.5745 0.0244  0.0739  -0.0598 302 PHE B O   
616  C CB  . PHE A 87  ? 0.8025 0.4753 0.5609 0.0000  0.0760  -0.0138 302 PHE B CB  
617  C CG  . PHE A 87  ? 0.7769 0.4580 0.5458 -0.0025 0.0753  0.0003  302 PHE B CG  
618  C CD1 . PHE A 87  ? 0.8097 0.4751 0.5828 0.0021  0.0638  0.0091  302 PHE B CD1 
619  C CD2 . PHE A 87  ? 0.7516 0.4507 0.5201 -0.0096 0.0841  0.0053  302 PHE B CD2 
620  C CE1 . PHE A 87  ? 0.7698 0.4481 0.5470 0.0010  0.0634  0.0220  302 PHE B CE1 
621  C CE2 . PHE A 87  ? 0.8080 0.5161 0.5830 -0.0090 0.0816  0.0139  302 PHE B CE2 
622  C CZ  . PHE A 87  ? 0.7651 0.4680 0.5446 -0.0030 0.0723  0.0219  302 PHE B CZ  
623  N N   . TRP A 88  ? 0.8386 0.4415 0.5803 0.0180  0.0456  -0.0421 303 TRP B N   
624  C CA  . TRP A 88  ? 0.8738 0.4520 0.6007 0.0126  0.0352  -0.0526 303 TRP B CA  
625  C C   . TRP A 88  ? 0.8526 0.4288 0.5813 -0.0129 0.0319  -0.0319 303 TRP B C   
626  O O   . TRP A 88  ? 0.9343 0.4868 0.6687 -0.0263 0.0209  -0.0172 303 TRP B O   
627  C CB  . TRP A 88  ? 0.9339 0.4609 0.6541 0.0259  0.0135  -0.0677 303 TRP B CB  
628  C CG  . TRP A 88  ? 0.9793 0.5183 0.6963 0.0572  0.0152  -0.0968 303 TRP B CG  
629  C CD1 . TRP A 88  ? 0.9459 0.4960 0.6481 0.0704  0.0166  -0.1246 303 TRP B CD1 
630  C CD2 . TRP A 88  ? 0.9851 0.5395 0.7149 0.0822  0.0163  -0.1041 303 TRP B CD2 
631  N NE1 . TRP A 88  ? 0.9704 0.5456 0.6768 0.1022  0.0203  -0.1495 303 TRP B NE1 
632  C CE2 . TRP A 88  ? 0.9840 0.5640 0.7098 0.1105  0.0193  -0.1382 303 TRP B CE2 
633  C CE3 . TRP A 88  ? 0.9496 0.5044 0.6931 0.0854  0.0139  -0.0870 303 TRP B CE3 
634  C CZ2 . TRP A 88  ? 1.0231 0.6350 0.7637 0.1423  0.0200  -0.1569 303 TRP B CZ2 
635  C CZ3 . TRP A 88  ? 0.9681 0.5480 0.7239 0.1167  0.0123  -0.1045 303 TRP B CZ3 
636  C CH2 . TRP A 88  ? 1.0543 0.6653 0.8112 0.1451  0.0153  -0.1399 303 TRP B CH2 
637  N N   . ALA A 89  ? 0.8358 0.4391 0.5578 -0.0193 0.0406  -0.0308 304 ALA B N   
638  C CA  . ALA A 89  ? 0.8758 0.4952 0.6035 -0.0360 0.0393  -0.0144 304 ALA B CA  
639  C C   . ALA A 89  ? 0.9132 0.5200 0.6394 -0.0505 0.0228  -0.0202 304 ALA B C   
640  O O   . ALA A 89  ? 0.9328 0.5261 0.6443 -0.0449 0.0154  -0.0396 304 ALA B O   
641  C CB  . ALA A 89  ? 0.8837 0.5311 0.6008 -0.0314 0.0512  -0.0112 304 ALA B CB  
642  N N   . ASP A 90  ? 0.9718 0.5885 0.7137 -0.0710 0.0171  -0.0046 305 ASP B N   
643  C CA  . ASP A 90  ? 0.9511 0.5672 0.6987 -0.0930 0.0013  -0.0084 305 ASP B CA  
644  C C   . ASP A 90  ? 0.9580 0.6246 0.7084 -0.0912 0.0033  -0.0102 305 ASP B C   
645  O O   . ASP A 90  ? 0.9340 0.6417 0.6988 -0.0942 0.0101  0.0034  305 ASP B O   
646  C CB  . ASP A 90  ? 0.9110 0.5186 0.6741 -0.1209 -0.0045 0.0113  305 ASP B CB  
647  C CG  . ASP A 90  ? 1.0265 0.6378 0.8002 -0.1529 -0.0209 0.0084  305 ASP B CG  
648  O OD1 . ASP A 90  ? 1.0469 0.6862 0.8216 -0.1505 -0.0268 -0.0079 305 ASP B OD1 
649  O OD2 . ASP A 90  ? 1.0543 0.6407 0.8339 -0.1829 -0.0292 0.0238  305 ASP B OD2 
650  N N   . LEU A 91  ? 0.9282 0.5928 0.6611 -0.0817 -0.0040 -0.0287 306 LEU B N   
651  C CA  . LEU A 91  ? 0.9710 0.6760 0.6984 -0.0736 -0.0068 -0.0316 306 LEU B CA  
652  C C   . LEU A 91  ? 1.0232 0.7530 0.7654 -0.0929 -0.0263 -0.0415 306 LEU B C   
653  O O   . LEU A 91  ? 1.0470 0.7983 0.7762 -0.0823 -0.0364 -0.0538 306 LEU B O   
654  C CB  . LEU A 91  ? 0.9748 0.6667 0.6662 -0.0506 -0.0024 -0.0421 306 LEU B CB  
655  C CG  . LEU A 91  ? 0.9464 0.6266 0.6222 -0.0355 0.0173  -0.0324 306 LEU B CG  
656  C CD1 . LEU A 91  ? 0.9633 0.6175 0.6480 -0.0372 0.0246  -0.0355 306 LEU B CD1 
657  C CD2 . LEU A 91  ? 0.9784 0.6537 0.6151 -0.0213 0.0210  -0.0389 306 LEU B CD2 
658  N N   . ASN A 92  ? 1.0932 0.8217 0.8611 -0.1232 -0.0330 -0.0354 307 ASN B N   
659  C CA  . ASN A 92  ? 1.0832 0.8355 0.8701 -0.1513 -0.0526 -0.0454 307 ASN B CA  
660  C C   . ASN A 92  ? 1.0542 0.8680 0.8775 -0.1761 -0.0474 -0.0271 307 ASN B C   
661  O O   . ASN A 92  ? 1.0604 0.8570 0.8960 -0.2040 -0.0433 -0.0098 307 ASN B O   
662  C CB  . ASN A 92  ? 1.1903 0.8766 0.9701 -0.1728 -0.0685 -0.0562 307 ASN B CB  
663  C CG  . ASN A 92  ? 1.2690 0.9656 1.0552 -0.1940 -0.0937 -0.0784 307 ASN B CG  
664  O OD1 . ASN A 92  ? 1.2285 0.9486 1.0439 -0.2344 -0.1041 -0.0726 307 ASN B OD1 
665  N ND2 . ASN A 92  ? 1.2886 0.9731 1.0466 -0.1690 -0.1037 -0.1043 307 ASN B ND2 
666  N N   . TRP A 93  ? 1.0099 0.8977 0.8481 -0.1647 -0.0484 -0.0311 308 TRP B N   
667  C CA  . TRP A 93  ? 0.9779 0.9431 0.8528 -0.1824 -0.0408 -0.0177 308 TRP B CA  
668  C C   . TRP A 93  ? 0.9633 1.0194 0.8645 -0.1801 -0.0537 -0.0330 308 TRP B C   
669  O O   . TRP A 93  ? 0.9653 1.0567 0.8934 -0.2160 -0.0681 -0.0413 308 TRP B O   
670  C CB  . TRP A 93  ? 0.9253 0.8984 0.7928 -0.1550 -0.0201 -0.0025 308 TRP B CB  
671  C CG  . TRP A 93  ? 0.9227 0.9190 0.7749 -0.1098 -0.0203 -0.0122 308 TRP B CG  
672  C CD1 . TRP A 93  ? 0.9033 0.9762 0.7732 -0.0905 -0.0210 -0.0164 308 TRP B CD1 
673  C CD2 . TRP A 93  ? 0.9735 0.9127 0.7857 -0.0780 -0.0213 -0.0183 308 TRP B CD2 
674  N NE1 . TRP A 93  ? 0.9186 0.9715 0.7579 -0.0470 -0.0259 -0.0239 308 TRP B NE1 
675  C CE2 . TRP A 93  ? 0.9332 0.9047 0.7362 -0.0428 -0.0247 -0.0225 308 TRP B CE2 
676  C CE3 . TRP A 93  ? 1.0037 0.8708 0.7857 -0.0757 -0.0198 -0.0210 308 TRP B CE3 
677  C CZ2 . TRP A 93  ? 0.9692 0.8933 0.7299 -0.0122 -0.0267 -0.0240 308 TRP B CZ2 
678  C CZ3 . TRP A 93  ? 1.0001 0.8366 0.7450 -0.0463 -0.0178 -0.0239 308 TRP B CZ3 
679  C CH2 . TRP A 93  ? 0.9740 0.8341 0.7065 -0.0180 -0.0213 -0.0228 308 TRP B CH2 
680  N N   . SER A 108 ? 1.1433 1.6028 1.0798 0.0539  -0.1251 -0.1178 323 SER B N   
681  C CA  . SER A 108 ? 1.1414 1.5234 1.0343 0.0897  -0.1134 -0.1043 323 SER B CA  
682  C C   . SER A 108 ? 1.1107 1.5654 1.0246 0.1266  -0.1102 -0.1127 323 SER B C   
683  O O   . SER A 108 ? 1.0133 1.5905 0.9769 0.1287  -0.1162 -0.1301 323 SER B O   
684  C CB  . SER A 108 ? 1.1471 1.4420 0.9758 0.1297  -0.1319 -0.1041 323 SER B CB  
685  O OG  . SER A 108 ? 1.1883 1.3737 0.9759 0.1133  -0.1149 -0.0842 323 SER B OG  
686  N N   . GLY A 109 ? 1.1013 1.4843 0.9778 0.1554  -0.1012 -0.1029 324 GLY B N   
687  C CA  . GLY A 109 ? 1.0187 1.4514 0.9019 0.2014  -0.1031 -0.1157 324 GLY B CA  
688  C C   . GLY A 109 ? 0.9712 1.4607 0.8900 0.1773  -0.0754 -0.1101 324 GLY B C   
689  O O   . GLY A 109 ? 0.9384 1.5465 0.8979 0.1916  -0.0740 -0.1270 324 GLY B O   
690  N N   . GLY A 110 ? 0.9002 1.3132 0.8029 0.1429  -0.0535 -0.0873 325 GLY B N   
691  C CA  . GLY A 110 ? 0.7570 1.2153 0.6844 0.1195  -0.0283 -0.0785 325 GLY B CA  
692  C C   . GLY A 110 ? 0.7346 1.1150 0.6242 0.1438  -0.0201 -0.0726 325 GLY B C   
693  O O   . GLY A 110 ? 0.7701 1.0809 0.6197 0.1866  -0.0362 -0.0804 325 GLY B O   
694  N N   . PHE A 111 ? 0.6583 1.0453 0.5566 0.1156  0.0028  -0.0582 326 PHE B N   
695  C CA  . PHE A 111 ? 0.6733 0.9947 0.5394 0.1355  0.0095  -0.0551 326 PHE B CA  
696  C C   . PHE A 111 ? 0.6622 0.8843 0.5075 0.0996  0.0195  -0.0319 326 PHE B C   
697  O O   . PHE A 111 ? 0.6557 0.8881 0.5192 0.0546  0.0326  -0.0147 326 PHE B O   
698  C CB  . PHE A 111 ? 0.5795 0.9830 0.4636 0.1398  0.0258  -0.0593 326 PHE B CB  
699  C CG  . PHE A 111 ? 0.5862 0.9220 0.4380 0.1542  0.0316  -0.0568 326 PHE B CG  
700  C CD1 . PHE A 111 ? 0.6178 0.9101 0.4390 0.2066  0.0151  -0.0779 326 PHE B CD1 
701  C CD2 . PHE A 111 ? 0.5880 0.8992 0.4376 0.1158  0.0503  -0.0342 326 PHE B CD2 
702  C CE1 . PHE A 111 ? 0.6291 0.8583 0.4218 0.2159  0.0179  -0.0783 326 PHE B CE1 
703  C CE2 . PHE A 111 ? 0.6060 0.8618 0.4282 0.1291  0.0533  -0.0345 326 PHE B CE2 
704  C CZ  . PHE A 111 ? 0.6171 0.8338 0.4127 0.1771  0.0374  -0.0575 326 PHE B CZ  
705  N N   . TYR A 112 ? 0.6866 0.8136 0.4930 0.1199  0.0118  -0.0322 327 TYR B N   
706  C CA  . TYR A 112 ? 0.7052 0.7448 0.4914 0.0940  0.0200  -0.0154 327 TYR B CA  
707  C C   . TYR A 112 ? 0.7176 0.7251 0.4879 0.1048  0.0272  -0.0152 327 TYR B C   
708  O O   . TYR A 112 ? 0.7352 0.7200 0.4835 0.1405  0.0159  -0.0290 327 TYR B O   
709  C CB  . TYR A 112 ? 0.7364 0.7018 0.4904 0.1029  0.0070  -0.0152 327 TYR B CB  
710  C CG  . TYR A 112 ? 0.7396 0.7265 0.5029 0.0913  -0.0021 -0.0166 327 TYR B CG  
711  C CD1 . TYR A 112 ? 0.7494 0.8042 0.5282 0.1130  -0.0171 -0.0314 327 TYR B CD1 
712  C CD2 . TYR A 112 ? 0.7875 0.7297 0.5434 0.0620  0.0020  -0.0071 327 TYR B CD2 
713  C CE1 . TYR A 112 ? 0.7724 0.8493 0.5597 0.1022  -0.0286 -0.0355 327 TYR B CE1 
714  C CE2 . TYR A 112 ? 0.7576 0.7167 0.5183 0.0526  -0.0092 -0.0124 327 TYR B CE2 
715  C CZ  . TYR A 112 ? 0.7676 0.7937 0.5443 0.0711  -0.0249 -0.0261 327 TYR B CZ  
716  O OH  . TYR A 112 ? 0.8655 0.9149 0.6489 0.0620  -0.0388 -0.0341 327 TYR B OH  
717  N N   . GLY A 113 ? 0.6980 0.6992 0.4765 0.0760  0.0423  -0.0010 328 GLY B N   
718  C CA  . GLY A 113 ? 0.6673 0.6551 0.4348 0.0857  0.0479  -0.0029 328 GLY B CA  
719  C C   . GLY A 113 ? 0.6611 0.5940 0.4224 0.0603  0.0563  0.0115  328 GLY B C   
720  O O   . GLY A 113 ? 0.6687 0.5845 0.4379 0.0338  0.0604  0.0241  328 GLY B O   
721  N N   . VAL A 114 ? 0.7199 0.6275 0.4670 0.0720  0.0562  0.0059  329 VAL B N   
722  C CA  . VAL A 114 ? 0.7626 0.6315 0.5061 0.0551  0.0620  0.0144  329 VAL B CA  
723  C C   . VAL A 114 ? 0.6930 0.5964 0.4358 0.0630  0.0658  0.0119  329 VAL B C   
724  O O   . VAL A 114 ? 0.6968 0.6251 0.4313 0.0890  0.0606  -0.0043 329 VAL B O   
725  C CB  . VAL A 114 ? 0.7577 0.5587 0.4825 0.0581  0.0556  0.0078  329 VAL B CB  
726  C CG1 . VAL A 114 ? 0.7229 0.5016 0.4519 0.0411  0.0616  0.0131  329 VAL B CG1 
727  C CG2 . VAL A 114 ? 0.8206 0.5915 0.5375 0.0528  0.0522  0.0112  329 VAL B CG2 
728  N N   . SER A 115 ? 0.6878 0.5907 0.4352 0.0444  0.0726  0.0263  330 SER B N   
729  C CA  . SER A 115 ? 0.7124 0.6511 0.4543 0.0486  0.0765  0.0293  330 SER B CA  
730  C C   . SER A 115 ? 0.6942 0.5950 0.4316 0.0415  0.0742  0.0336  330 SER B C   
731  O O   . SER A 115 ? 0.6863 0.5579 0.4308 0.0243  0.0752  0.0460  330 SER B O   
732  C CB  . SER A 115 ? 0.6544 0.6465 0.4042 0.0305  0.0865  0.0495  330 SER B CB  
733  O OG  . SER A 115 ? 0.6507 0.7003 0.4102 0.0389  0.0891  0.0416  330 SER B OG  
734  N N   . SER A 116 ? 0.6637 0.5679 0.3898 0.0575  0.0688  0.0197  331 SER B N   
735  C CA  . SER A 116 ? 0.7284 0.6102 0.4531 0.0542  0.0639  0.0191  331 SER B CA  
736  C C   . SER A 116 ? 0.7717 0.6926 0.4809 0.0663  0.0622  0.0187  331 SER B C   
737  O O   . SER A 116 ? 0.7794 0.7297 0.4768 0.0852  0.0604  0.0028  331 SER B O   
738  C CB  . SER A 116 ? 0.7371 0.5792 0.4627 0.0575  0.0553  -0.0015 331 SER B CB  
739  O OG  . SER A 116 ? 0.8685 0.6761 0.6004 0.0467  0.0577  0.0002  331 SER B OG  
740  N N   . GLN A 117 ? 0.7325 0.6525 0.4378 0.0596  0.0608  0.0342  332 GLN B N   
741  C CA  . GLN A 117 ? 0.8308 0.7819 0.5156 0.0724  0.0562  0.0337  332 GLN B CA  
742  C C   . GLN A 117 ? 0.8075 0.7343 0.4964 0.0743  0.0441  0.0296  332 GLN B C   
743  O O   . GLN A 117 ? 0.8031 0.7023 0.5032 0.0639  0.0431  0.0429  332 GLN B O   
744  C CB  . GLN A 117 ? 0.7899 0.7771 0.4566 0.0634  0.0659  0.0634  332 GLN B CB  
745  C CG  . GLN A 117 ? 0.8689 0.8946 0.5058 0.0778  0.0628  0.0650  332 GLN B CG  
746  C CD  . GLN A 117 ? 0.9160 0.9904 0.5299 0.0654  0.0768  0.0947  332 GLN B CD  
747  O OE1 . GLN A 117 ? 0.9155 1.0264 0.5392 0.0557  0.0905  0.0981  332 GLN B OE1 
748  N NE2 . GLN A 117 ? 0.8960 0.9742 0.4784 0.0642  0.0728  0.1174  332 GLN B NE2 
749  N N   . TYR A 118 ? 0.8093 0.7500 0.4903 0.0896  0.0329  0.0075  333 TYR B N   
750  C CA  . TYR A 118 ? 0.8209 0.7574 0.5069 0.0945  0.0187  -0.0009 333 TYR B CA  
751  C C   . TYR A 118 ? 0.8776 0.8505 0.5331 0.1122  0.0102  0.0007  333 TYR B C   
752  O O   . TYR A 118 ? 0.8866 0.8908 0.5178 0.1209  0.0164  0.0017  333 TYR B O   
753  C CB  . TYR A 118 ? 0.8289 0.7500 0.5355 0.0915  0.0095  -0.0326 333 TYR B CB  
754  C CG  . TYR A 118 ? 0.7978 0.6839 0.5263 0.0734  0.0181  -0.0341 333 TYR B CG  
755  C CD1 . TYR A 118 ? 0.7591 0.6326 0.5119 0.0604  0.0203  -0.0297 333 TYR B CD1 
756  C CD2 . TYR A 118 ? 0.7823 0.6508 0.5037 0.0730  0.0228  -0.0411 333 TYR B CD2 
757  C CE1 . TYR A 118 ? 0.7739 0.6203 0.5407 0.0438  0.0292  -0.0303 333 TYR B CE1 
758  C CE2 . TYR A 118 ? 0.7930 0.6269 0.5265 0.0577  0.0288  -0.0400 333 TYR B CE2 
759  C CZ  . TYR A 118 ? 0.7984 0.6221 0.5534 0.0411  0.0333  -0.0335 333 TYR B CZ  
760  O OH  . TYR A 118 ? 0.8120 0.6055 0.5733 0.0255  0.0407  -0.0313 333 TYR B OH  
761  N N   . GLU A 119 ? 0.8510 0.8264 0.5069 0.1201  -0.0049 -0.0019 334 GLU B N   
762  C CA  . GLU A 119 ? 0.8544 0.8614 0.4757 0.1384  -0.0158 0.0031  334 GLU B CA  
763  C C   . GLU A 119 ? 0.8721 0.8894 0.5068 0.1501  -0.0380 -0.0227 334 GLU B C   
764  O O   . GLU A 119 ? 0.8746 0.8772 0.5396 0.1452  -0.0440 -0.0253 334 GLU B O   
765  C CB  . GLU A 119 ? 0.9341 0.9311 0.5292 0.1363  -0.0130 0.0448  334 GLU B CB  
766  C CG  . GLU A 119 ? 0.9808 0.9831 0.5598 0.1203  0.0080  0.0712  334 GLU B CG  
767  C CD  . GLU A 119 ? 1.0537 1.0528 0.5913 0.1150  0.0088  0.1139  334 GLU B CD  
768  O OE1 . GLU A 119 ? 1.1068 1.1007 0.6192 0.1312  -0.0090 0.1216  334 GLU B OE1 
769  O OE2 . GLU A 119 ? 1.0314 1.0331 0.5601 0.0933  0.0260  0.1404  334 GLU B OE2 
770  N N   . SER A 120 ? 0.9144 0.9638 0.5278 0.1663  -0.0507 -0.0443 335 SER B N   
771  C CA  . SER A 120 ? 0.9314 1.0003 0.5555 0.1775  -0.0749 -0.0691 335 SER B CA  
772  C C   . SER A 120 ? 1.0216 1.1281 0.5982 0.2027  -0.0889 -0.0692 335 SER B C   
773  O O   . SER A 120 ? 1.0054 1.1275 0.5411 0.2098  -0.0774 -0.0541 335 SER B O   
774  C CB  . SER A 120 ? 0.9192 0.9839 0.5765 0.1650  -0.0827 -0.1105 335 SER B CB  
775  O OG  . SER A 120 ? 0.9752 1.0501 0.6054 0.1759  -0.0876 -0.1341 335 SER B OG  
776  N N   . LEU A 121 ? 0.7407 1.2281 0.6871 -0.0536 -0.1489 0.0668  336 LEU B N   
777  C CA  . LEU A 121 ? 0.7007 1.2054 0.5889 -0.0613 -0.1621 0.0699  336 LEU B CA  
778  C C   . LEU A 121 ? 0.7596 1.2612 0.6101 -0.0658 -0.1453 0.0293  336 LEU B C   
779  O O   . LEU A 121 ? 0.8529 1.3677 0.6437 -0.0699 -0.1406 0.0276  336 LEU B O   
780  C CB  . LEU A 121 ? 0.6980 1.2142 0.6000 -0.0635 -0.2084 0.0811  336 LEU B CB  
781  C CG  . LEU A 121 ? 0.7619 1.2771 0.6542 -0.0628 -0.2285 0.1300  336 LEU B CG  
782  C CD1 . LEU A 121 ? 0.7652 1.2775 0.7090 -0.0549 -0.2722 0.1398  336 LEU B CD1 
783  C CD2 . LEU A 121 ? 0.8211 1.3474 0.6328 -0.0729 -0.2358 0.1475  336 LEU B CD2 
784  N N   . GLU A 122 ? 0.7341 1.2157 0.6141 -0.0668 -0.1346 -0.0038 337 GLU B N   
785  C CA  . GLU A 122 ? 0.7618 1.2275 0.6063 -0.0720 -0.1165 -0.0430 337 GLU B CA  
786  C C   . GLU A 122 ? 0.7597 1.2025 0.5833 -0.0598 -0.0801 -0.0473 337 GLU B C   
787  O O   . GLU A 122 ? 0.7288 1.1581 0.5847 -0.0496 -0.0669 -0.0324 337 GLU B O   
788  C CB  . GLU A 122 ? 0.7487 1.1959 0.6281 -0.0833 -0.1185 -0.0763 337 GLU B CB  
789  C CG  . GLU A 122 ? 0.8072 1.2740 0.7472 -0.0876 -0.1446 -0.0696 337 GLU B CG  
790  C CD  . GLU A 122 ? 0.8606 1.3230 0.8274 -0.1057 -0.1453 -0.1092 337 GLU B CD  
791  O OE1 . GLU A 122 ? 0.8336 1.3172 0.8577 -0.1099 -0.1621 -0.1126 337 GLU B OE1 
792  O OE2 . GLU A 122 ? 0.8903 1.3288 0.8214 -0.1168 -0.1289 -0.1391 337 GLU B OE2 
793  N N   . HIS A 123 ? 0.8075 1.2476 0.5779 -0.0589 -0.0662 -0.0712 338 HIS B N   
794  C CA  . HIS A 123 ? 0.7890 1.2034 0.5408 -0.0436 -0.0346 -0.0881 338 HIS B CA  
795  C C   . HIS A 123 ? 0.7914 1.1515 0.5594 -0.0453 -0.0264 -0.1161 338 HIS B C   
796  O O   . HIS A 123 ? 0.7808 1.1251 0.5394 -0.0618 -0.0356 -0.1434 338 HIS B O   
797  C CB  . HIS A 123 ? 0.8306 1.2598 0.5212 -0.0409 -0.0240 -0.1106 338 HIS B CB  
798  C CG  . HIS A 123 ? 0.8428 1.2497 0.5175 -0.0198 0.0055  -0.1326 338 HIS B CG  
799  N ND1 . HIS A 123 ? 0.8540 1.2963 0.5161 -0.0053 0.0246  -0.1226 338 HIS B ND1 
800  C CD2 . HIS A 123 ? 0.8655 1.2167 0.5372 -0.0098 0.0174  -0.1643 338 HIS B CD2 
801  C CE1 . HIS A 123 ? 0.8760 1.2911 0.5321 0.0170  0.0452  -0.1510 338 HIS B CE1 
802  N NE2 . HIS A 123 ? 0.8723 1.2258 0.5307 0.0156  0.0397  -0.1746 338 HIS B NE2 
803  N N   . MET A 124 ? 0.8169 1.1476 0.6071 -0.0307 -0.0102 -0.1090 339 MET B N   
804  C CA  . MET A 124 ? 0.7887 1.0597 0.5864 -0.0339 -0.0019 -0.1291 339 MET B CA  
805  C C   . MET A 124 ? 0.7828 1.0171 0.5677 -0.0076 0.0187  -0.1329 339 MET B C   
806  O O   . MET A 124 ? 0.7552 1.0217 0.5435 0.0121  0.0264  -0.1177 339 MET B O   
807  C CB  . MET A 124 ? 0.7810 1.0514 0.6300 -0.0465 -0.0120 -0.1128 339 MET B CB  
808  C CG  . MET A 124 ? 0.7857 1.0793 0.6534 -0.0721 -0.0325 -0.1231 339 MET B CG  
809  S SD  . MET A 124 ? 0.8115 1.1302 0.7497 -0.0794 -0.0474 -0.1017 339 MET B SD  
810  C CE  . MET A 124 ? 0.6548 0.9882 0.6108 -0.0534 -0.0433 -0.0612 339 MET B CE  
811  N N   . THR A 125 ? 0.7786 0.9447 0.5485 -0.0080 0.0267  -0.1539 340 THR B N   
812  C CA  . THR A 125 ? 0.8319 0.9549 0.6008 0.0175  0.0387  -0.1504 340 THR B CA  
813  C C   . THR A 125 ? 0.8297 0.9197 0.6260 0.0053  0.0367  -0.1358 340 THR B C   
814  O O   . THR A 125 ? 0.8326 0.9022 0.6311 -0.0238 0.0330  -0.1451 340 THR B O   
815  C CB  . THR A 125 ? 0.8908 0.9497 0.6114 0.0327  0.0479  -0.1833 340 THR B CB  
816  O OG1 . THR A 125 ? 0.9513 1.0406 0.6437 0.0312  0.0478  -0.2054 340 THR B OG1 
817  C CG2 . THR A 125 ? 0.9085 0.9558 0.6296 0.0720  0.0562  -0.1801 340 THR B CG2 
818  N N   . LEU A 126 ? 0.8186 0.9110 0.6379 0.0261  0.0397  -0.1149 341 LEU B N   
819  C CA  . LEU A 126 ? 0.7946 0.8699 0.6425 0.0171  0.0376  -0.0981 341 LEU B CA  
820  C C   . LEU A 126 ? 0.7937 0.7932 0.6135 0.0347  0.0453  -0.1026 341 LEU B C   
821  O O   . LEU A 126 ? 0.8526 0.8385 0.6556 0.0671  0.0484  -0.1071 341 LEU B O   
822  C CB  . LEU A 126 ? 0.7301 0.8690 0.6284 0.0255  0.0306  -0.0687 341 LEU B CB  
823  C CG  . LEU A 126 ? 0.6950 0.9013 0.6234 0.0095  0.0173  -0.0553 341 LEU B CG  
824  C CD1 . LEU A 126 ? 0.6351 0.8804 0.6131 0.0157  0.0092  -0.0259 341 LEU B CD1 
825  C CD2 . LEU A 126 ? 0.6973 0.8993 0.6291 -0.0203 0.0091  -0.0697 341 LEU B CD2 
826  N N   . THR A 127 ? 0.8284 0.7795 0.6411 0.0134  0.0478  -0.1024 342 THR B N   
827  C CA  . THR A 127 ? 0.8795 0.7636 0.6687 0.0278  0.0515  -0.0960 342 THR B CA  
828  C C   . THR A 127 ? 0.8101 0.7294 0.6434 0.0223  0.0487  -0.0735 342 THR B C   
829  O O   . THR A 127 ? 0.7550 0.7053 0.6174 -0.0080 0.0485  -0.0724 342 THR B O   
830  C CB  . THR A 127 ? 0.9262 0.7172 0.6612 0.0040  0.0587  -0.1118 342 THR B CB  
831  O OG1 . THR A 127 ? 0.9520 0.7130 0.6504 0.0050  0.0595  -0.1368 342 THR B OG1 
832  C CG2 . THR A 127 ? 0.9153 0.6254 0.6112 0.0238  0.0590  -0.1028 342 THR B CG2 
833  N N   . CYS A 128 ? 0.7520 0.6725 0.5948 0.0530  0.0450  -0.0592 343 CYS B N   
834  C CA  . CYS A 128 ? 0.7142 0.6615 0.5948 0.0512  0.0414  -0.0407 343 CYS B CA  
835  C C   . CYS A 128 ? 0.7636 0.6333 0.6017 0.0606  0.0435  -0.0380 343 CYS B C   
836  O O   . CYS A 128 ? 0.7960 0.6373 0.6136 0.0959  0.0378  -0.0366 343 CYS B O   
837  C CB  . CYS A 128 ? 0.7118 0.7309 0.6423 0.0752  0.0332  -0.0254 343 CYS B CB  
838  S SG  . CYS A 128 ? 0.8256 0.9170 0.7765 0.0779  0.0315  -0.0269 343 CYS B SG  
839  N N   . SER A 129 ? 0.8201 0.6574 0.6434 0.0288  0.0510  -0.0384 344 SER B N   
840  C CA  . SER A 129 ? 0.8410 0.6062 0.6189 0.0300  0.0537  -0.0316 344 SER B CA  
841  C C   . SER A 129 ? 0.8210 0.6356 0.6434 0.0331  0.0496  -0.0180 344 SER B C   
842  O O   . SER A 129 ? 0.7777 0.6545 0.6508 0.0101  0.0521  -0.0193 344 SER B O   
843  C CB  . SER A 129 ? 0.8712 0.5739 0.6024 -0.0135 0.0686  -0.0411 344 SER B CB  
844  O OG  . SER A 129 ? 1.0316 0.6733 0.7189 -0.0193 0.0728  -0.0306 344 SER B OG  
845  N N   . SER A 130 ? 0.8034 0.5927 0.6098 0.0639  0.0405  -0.0074 345 SER B N   
846  C CA  . SER A 130 ? 0.8264 0.6507 0.6653 0.0650  0.0365  0.0026  345 SER B CA  
847  C C   . SER A 130 ? 0.8815 0.6224 0.6517 0.0660  0.0377  0.0083  345 SER B C   
848  O O   . SER A 130 ? 0.9446 0.6245 0.6668 0.0968  0.0272  0.0117  345 SER B O   
849  C CB  . SER A 130 ? 0.7719 0.6631 0.6682 0.0994  0.0214  0.0104  345 SER B CB  
850  O OG  . SER A 130 ? 0.8306 0.7065 0.7104 0.1337  0.0139  0.0080  345 SER B OG  
851  N N   . LYS A 131 ? 0.8885 0.6253 0.6506 0.0320  0.0501  0.0077  346 LYS B N   
852  C CA  . LYS A 131 ? 0.9650 0.6224 0.6531 0.0229  0.0549  0.0148  346 LYS B CA  
853  C C   . LYS A 131 ? 0.8966 0.5951 0.6125 0.0337  0.0480  0.0205  346 LYS B C   
854  O O   . LYS A 131 ? 0.8309 0.6057 0.6108 0.0169  0.0535  0.0131  346 LYS B O   
855  C CB  . LYS A 131 ? 0.9917 0.6126 0.6411 -0.0313 0.0796  0.0067  346 LYS B CB  
856  C CG  . LYS A 131 ? 1.0679 0.6615 0.7022 -0.0503 0.0876  -0.0041 346 LYS B CG  
857  C CD  . LYS A 131 ? 1.1625 0.7523 0.7851 -0.1095 0.1132  -0.0168 346 LYS B CD  
858  C CE  . LYS A 131 ? 1.2980 0.7810 0.8358 -0.1357 0.1240  -0.0183 346 LYS B CE  
859  N NZ  . LYS A 131 ? 1.4302 0.8883 0.9312 -0.1923 0.1506  -0.0221 346 LYS B NZ  
860  N N   . VAL A 132 ? 0.9800 0.6264 0.6474 0.0635  0.0333  0.0315  347 VAL B N   
861  C CA  . VAL A 132 ? 0.9504 0.6254 0.6321 0.0753  0.0243  0.0354  347 VAL B CA  
862  C C   . VAL A 132 ? 1.0532 0.6599 0.6533 0.0445  0.0387  0.0397  347 VAL B C   
863  O O   . VAL A 132 ? 1.1328 0.6382 0.6408 0.0470  0.0361  0.0507  347 VAL B O   
864  C CB  . VAL A 132 ? 0.9398 0.6095 0.6225 0.1286  -0.0038 0.0425  347 VAL B CB  
865  C CG1 . VAL A 132 ? 0.9195 0.6167 0.6136 0.1391  -0.0147 0.0442  347 VAL B CG1 
866  C CG2 . VAL A 132 ? 0.8793 0.6189 0.6385 0.1529  -0.0128 0.0374  347 VAL B CG2 
867  N N   . CYS A 133 ? 0.9813 0.6406 0.6117 0.0159  0.0531  0.0307  348 CYS B N   
868  C CA  . CYS A 133 ? 1.0709 0.6808 0.6287 -0.0227 0.0739  0.0312  348 CYS B CA  
869  C C   . CYS A 133 ? 1.0610 0.6920 0.6148 -0.0084 0.0645  0.0318  348 CYS B C   
870  O O   . CYS A 133 ? 0.9381 0.6579 0.5770 0.0052  0.0563  0.0202  348 CYS B O   
871  C CB  . CYS A 133 ? 1.0984 0.7559 0.6910 -0.0753 0.1045  0.0125  348 CYS B CB  
872  S SG  . CYS A 133 ? 1.2142 0.8674 0.8290 -0.0918 0.1122  0.0061  348 CYS B SG  
873  N N   . SER A 134 ? 1.1662 0.7101 0.6165 -0.0120 0.0640  0.0456  349 SER B N   
874  C CA  . SER A 134 ? 1.1823 0.7340 0.6070 -0.0052 0.0577  0.0456  349 SER B CA  
875  C C   . SER A 134 ? 1.2525 0.7778 0.6117 -0.0617 0.0922  0.0411  349 SER B C   
876  O O   . SER A 134 ? 1.3537 0.7802 0.6119 -0.0885 0.1050  0.0564  349 SER B O   
877  C CB  . SER A 134 ? 1.2120 0.6847 0.5626 0.0394  0.0253  0.0655  349 SER B CB  
878  O OG  . SER A 134 ? 1.3041 0.7539 0.5908 0.0329  0.0246  0.0687  349 SER B OG  
879  N N   . PHE A 135 ? 1.1582 0.7701 0.5730 -0.0810 0.1075  0.0188  350 PHE B N   
880  C CA  . PHE A 135 ? 1.2001 0.8109 0.5687 -0.1385 0.1457  0.0069  350 PHE B CA  
881  C C   . PHE A 135 ? 1.3294 0.9250 0.6945 -0.1856 0.1752  0.0021  350 PHE B C   
882  O O   . PHE A 135 ? 1.3847 0.9220 0.6642 -0.2354 0.2047  0.0061  350 PHE B O   
883  C CB  . PHE A 135 ? 1.2132 0.7274 0.4463 -0.1488 0.1477  0.0268  350 PHE B CB  
884  C CG  . PHE A 135 ? 1.2195 0.7594 0.4520 -0.1130 0.1240  0.0245  350 PHE B CG  
885  C CD1 . PHE A 135 ? 1.2018 0.7125 0.4317 -0.0539 0.0809  0.0408  350 PHE B CD1 
886  C CD2 . PHE A 135 ? 1.1981 0.7993 0.4383 -0.1380 0.1445  0.0014  350 PHE B CD2 
887  C CE1 . PHE A 135 ? 1.1875 0.7262 0.4206 -0.0220 0.0572  0.0356  350 PHE B CE1 
888  C CE2 . PHE A 135 ? 1.1898 0.8165 0.4307 -0.1050 0.1212  -0.0042 350 PHE B CE2 
889  C CZ  . PHE A 135 ? 1.1859 0.7796 0.4216 -0.0481 0.0769  0.0137  350 PHE B CZ  
890  N N   . GLY A 136 ? 1.2821 0.9266 0.7354 -0.1717 0.1666  -0.0058 351 GLY B N   
891  C CA  . GLY A 136 ? 1.3414 0.9832 0.8040 -0.2131 0.1903  -0.0147 351 GLY B CA  
892  C C   . GLY A 136 ? 1.4634 0.9798 0.8207 -0.2276 0.1934  0.0088  351 GLY B C   
893  O O   . GLY A 136 ? 1.5432 1.0281 0.8597 -0.2827 0.2240  0.0032  351 GLY B O   
894  N N   . LYS A 137 ? 1.4507 0.8950 0.7655 -0.1798 0.1617  0.0326  352 LYS B N   
895  C CA  . LYS A 137 ? 1.4746 0.7917 0.6917 -0.1830 0.1571  0.0538  352 LYS B CA  
896  C C   . LYS A 137 ? 1.4579 0.7657 0.7074 -0.1210 0.1208  0.0617  352 LYS B C   
897  O O   . LYS A 137 ? 1.4297 0.7505 0.6910 -0.0716 0.0928  0.0692  352 LYS B O   
898  C CB  . LYS A 137 ? 1.5881 0.7921 0.6719 -0.1931 0.1570  0.0778  352 LYS B CB  
899  C CG  . LYS A 137 ? 1.5999 0.7882 0.6642 -0.1322 0.1194  0.0925  352 LYS B CG  
900  C CD  . LYS A 137 ? 1.7126 0.7691 0.6830 -0.0951 0.0883  0.1185  352 LYS B CD  
901  C CE  . LYS A 137 ? 1.7546 0.7569 0.6486 -0.0610 0.0605  0.1367  352 LYS B CE  
902  N NZ  . LYS A 137 ? 1.8574 0.7609 0.6968 -0.0251 0.0272  0.1470  352 LYS B NZ  
903  N N   . GLN A 138 ? 1.4170 0.7087 0.6835 -0.1246 0.1221  0.0569  353 GLN B N   
904  C CA  . GLN A 138 ? 1.3333 0.6199 0.6288 -0.0694 0.0921  0.0603  353 GLN B CA  
905  C C   . GLN A 138 ? 1.3909 0.5946 0.6141 -0.0217 0.0618  0.0802  353 GLN B C   
906  O O   . GLN A 138 ? 1.5782 0.6647 0.6908 -0.0349 0.0618  0.0969  353 GLN B O   
907  C CB  . GLN A 138 ? 1.3754 0.6121 0.6532 -0.0859 0.0992  0.0548  353 GLN B CB  
908  C CG  . GLN A 138 ? 1.3512 0.6022 0.6707 -0.0311 0.0727  0.0516  353 GLN B CG  
909  C CD  . GLN A 138 ? 1.3595 0.5526 0.6526 -0.0429 0.0770  0.0437  353 GLN B CD  
910  O OE1 . GLN A 138 ? 1.3585 0.4570 0.5893 -0.0129 0.0586  0.0504  353 GLN B OE1 
911  N NE2 . GLN A 138 ? 1.3341 0.5844 0.6762 -0.0841 0.0986  0.0266  353 GLN B NE2 
912  N N   . VAL A 139 ? 1.3255 0.5898 0.6097 0.0322  0.0349  0.0785  354 VAL B N   
913  C CA  . VAL A 139 ? 1.3509 0.5536 0.5837 0.0854  0.0007  0.0920  354 VAL B CA  
914  C C   . VAL A 139 ? 1.3285 0.5277 0.5916 0.1347  -0.0225 0.0862  354 VAL B C   
915  O O   . VAL A 139 ? 1.3977 0.5043 0.5922 0.1707  -0.0474 0.0947  354 VAL B O   
916  C CB  . VAL A 139 ? 1.3304 0.6046 0.6043 0.1097  -0.0140 0.0912  354 VAL B CB  
917  C CG1 . VAL A 139 ? 1.3052 0.5676 0.5812 0.1765  -0.0541 0.0945  354 VAL B CG1 
918  C CG2 . VAL A 139 ? 1.4137 0.6403 0.6057 0.0765  -0.0018 0.1016  354 VAL B CG2 
919  N N   . VAL A 140 ? 1.2355 0.5339 0.5984 0.1377  -0.0156 0.0706  355 VAL B N   
920  C CA  . VAL A 140 ? 1.2253 0.5303 0.6182 0.1761  -0.0302 0.0611  355 VAL B CA  
921  C C   . VAL A 140 ? 1.1500 0.5308 0.6145 0.1477  -0.0085 0.0473  355 VAL B C   
922  O O   . VAL A 140 ? 1.1005 0.5739 0.6355 0.1248  0.0043  0.0431  355 VAL B O   
923  C CB  . VAL A 140 ? 1.1682 0.5334 0.6157 0.2345  -0.0589 0.0571  355 VAL B CB  
924  C CG1 . VAL A 140 ? 1.2408 0.5243 0.6121 0.2683  -0.0863 0.0686  355 VAL B CG1 
925  C CG2 . VAL A 140 ? 1.0922 0.5782 0.6334 0.2257  -0.0528 0.0531  355 VAL B CG2 
926  N N   . GLU A 141 ? 1.1558 0.4946 0.6004 0.1517  -0.0075 0.0389  356 GLU B N   
927  C CA  . GLU A 141 ? 1.1448 0.5472 0.6467 0.1288  0.0091  0.0248  356 GLU B CA  
928  C C   . GLU A 141 ? 1.0971 0.5234 0.6291 0.1727  -0.0050 0.0124  356 GLU B C   
929  O O   . GLU A 141 ? 1.1271 0.4784 0.6081 0.2089  -0.0222 0.0098  356 GLU B O   
930  C CB  . GLU A 141 ? 1.1666 0.4992 0.6132 0.0787  0.0300  0.0209  356 GLU B CB  
931  C CG  . GLU A 141 ? 1.1401 0.5197 0.6305 0.0628  0.0406  0.0036  356 GLU B CG  
932  C CD  . GLU A 141 ? 1.2543 0.5725 0.6968 0.0098  0.0607  -0.0034 356 GLU B CD  
933  O OE1 . GLU A 141 ? 1.3401 0.5436 0.6939 -0.0038 0.0622  0.0050  356 GLU B OE1 
934  O OE2 . GLU A 141 ? 1.2782 0.6628 0.7716 -0.0195 0.0738  -0.0174 356 GLU B OE2 
935  N N   . LYS A 142 ? 1.0279 0.5590 0.6412 0.1703  0.0015  0.0040  357 LYS B N   
936  C CA  . LYS A 142 ? 0.9997 0.5676 0.6437 0.2006  -0.0042 -0.0106 357 LYS B CA  
937  C C   . LYS A 142 ? 0.9621 0.5657 0.6286 0.1655  0.0131  -0.0211 357 LYS B C   
938  O O   . LYS A 142 ? 0.8874 0.5488 0.5947 0.1303  0.0244  -0.0165 357 LYS B O   
939  C CB  . LYS A 142 ? 0.9826 0.6511 0.7024 0.2336  -0.0146 -0.0099 357 LYS B CB  
940  C CG  . LYS A 142 ? 1.0264 0.6828 0.7408 0.2684  -0.0345 -0.0019 357 LYS B CG  
941  C CD  . LYS A 142 ? 1.0764 0.6714 0.7486 0.3190  -0.0544 -0.0134 357 LYS B CD  
942  C CE  . LYS A 142 ? 1.1220 0.7130 0.7923 0.3560  -0.0789 -0.0086 357 LYS B CE  
943  N NZ  . LYS A 142 ? 1.0770 0.7284 0.7912 0.3858  -0.0918 -0.0276 357 LYS B NZ  
944  N N   . VAL A 143 ? 1.0016 0.5717 0.6420 0.1776  0.0128  -0.0377 358 VAL B N   
945  C CA  . VAL A 143 ? 1.0053 0.6067 0.6609 0.1482  0.0260  -0.0509 358 VAL B CA  
946  C C   . VAL A 143 ? 0.9751 0.6309 0.6601 0.1818  0.0219  -0.0664 358 VAL B C   
947  O O   . VAL A 143 ? 1.0078 0.6148 0.6600 0.2186  0.0126  -0.0805 358 VAL B O   
948  C CB  . VAL A 143 ? 1.0724 0.5725 0.6579 0.1188  0.0335  -0.0607 358 VAL B CB  
949  C CG1 . VAL A 143 ? 1.0319 0.5760 0.6411 0.0779  0.0470  -0.0733 358 VAL B CG1 
950  C CG2 . VAL A 143 ? 1.0790 0.5049 0.6160 0.0942  0.0369  -0.0447 358 VAL B CG2 
951  N N   . GLU A 144 ? 0.9198 0.6754 0.6644 0.1698  0.0281  -0.0648 359 GLU B N   
952  C CA  . GLU A 144 ? 0.8878 0.7058 0.6584 0.1926  0.0290  -0.0786 359 GLU B CA  
953  C C   . GLU A 144 ? 0.8699 0.7150 0.6407 0.1609  0.0386  -0.0892 359 GLU B C   
954  O O   . GLU A 144 ? 0.8782 0.7231 0.6527 0.1217  0.0427  -0.0827 359 GLU B O   
955  C CB  . GLU A 144 ? 0.8522 0.7693 0.6892 0.2066  0.0268  -0.0650 359 GLU B CB  
956  C CG  . GLU A 144 ? 0.8708 0.7847 0.7202 0.2441  0.0150  -0.0599 359 GLU B CG  
957  C CD  . GLU A 144 ? 0.9083 0.9000 0.8208 0.2368  0.0126  -0.0393 359 GLU B CD  
958  O OE1 . GLU A 144 ? 0.8912 0.9008 0.8225 0.2020  0.0158  -0.0242 359 GLU B OE1 
959  O OE2 . GLU A 144 ? 0.8984 0.9349 0.8445 0.2667  0.0063  -0.0409 359 GLU B OE2 
960  N N   . THR A 145 ? 0.8632 0.7400 0.6331 0.1790  0.0415  -0.1078 360 THR B N   
961  C CA  . THR A 145 ? 0.8380 0.7523 0.6074 0.1541  0.0483  -0.1191 360 THR B CA  
962  C C   . THR A 145 ? 0.8048 0.8175 0.6120 0.1665  0.0524  -0.1172 360 THR B C   
963  O O   . THR A 145 ? 0.8042 0.8369 0.6166 0.2020  0.0543  -0.1288 360 THR B O   
964  C CB  . THR A 145 ? 0.9599 0.8018 0.6727 0.1578  0.0499  -0.1496 360 THR B CB  
965  O OG1 . THR A 145 ? 1.0336 0.7705 0.7035 0.1560  0.0454  -0.1494 360 THR B OG1 
966  C CG2 . THR A 145 ? 0.9394 0.8004 0.6439 0.1208  0.0542  -0.1611 360 THR B CG2 
967  N N   . GLU A 146 ? 0.7482 0.8218 0.5795 0.1369  0.0534  -0.1042 361 GLU B N   
968  C CA  . GLU A 146 ? 0.7281 0.8901 0.5869 0.1400  0.0579  -0.0966 361 GLU B CA  
969  C C   . GLU A 146 ? 0.7605 0.9483 0.5993 0.1147  0.0589  -0.1044 361 GLU B C   
970  O O   . GLU A 146 ? 0.7337 0.9215 0.5793 0.0850  0.0504  -0.0937 361 GLU B O   
971  C CB  . GLU A 146 ? 0.7074 0.9210 0.6183 0.1315  0.0528  -0.0639 361 GLU B CB  
972  C CG  . GLU A 146 ? 0.6975 0.9952 0.6333 0.1337  0.0592  -0.0531 361 GLU B CG  
973  C CD  . GLU A 146 ? 0.7000 1.0185 0.6347 0.1677  0.0707  -0.0736 361 GLU B CD  
974  O OE1 . GLU A 146 ? 0.7268 0.9993 0.6583 0.1956  0.0673  -0.0863 361 GLU B OE1 
975  O OE2 . GLU A 146 ? 0.7251 1.1076 0.6616 0.1670  0.0824  -0.0778 361 GLU B OE2 
976  N N   . ARG A 147 ? 0.7871 1.0000 0.6018 0.1280  0.0680  -0.1263 362 ARG B N   
977  C CA  . ARG A 147 ? 0.8052 1.0525 0.5963 0.1068  0.0686  -0.1342 362 ARG B CA  
978  C C   . ARG A 147 ? 0.7541 1.0788 0.5724 0.0897  0.0664  -0.1023 362 ARG B C   
979  O O   . ARG A 147 ? 0.7213 1.0841 0.5733 0.0996  0.0710  -0.0827 362 ARG B O   
980  C CB  . ARG A 147 ? 0.8615 1.1143 0.6159 0.1281  0.0808  -0.1705 362 ARG B CB  
981  C CG  . ARG A 147 ? 0.9209 1.1504 0.6303 0.1104  0.0776  -0.1967 362 ARG B CG  
982  C CD  . ARG A 147 ? 1.0377 1.2966 0.7139 0.1294  0.0908  -0.2314 362 ARG B CD  
983  N NE  . ARG A 147 ? 1.1611 1.3507 0.7944 0.1355  0.0886  -0.2725 362 ARG B NE  
984  C CZ  . ARG A 147 ? 1.2220 1.4101 0.8270 0.1621  0.0982  -0.3127 362 ARG B CZ  
985  N NH1 . ARG A 147 ? 1.2015 1.4620 0.8178 0.1848  0.1136  -0.3199 362 ARG B NH1 
986  N NH2 . ARG A 147 ? 1.2733 1.3867 0.8391 0.1646  0.0929  -0.3490 362 ARG B NH2 
987  N N   . ALA A 148 ? 0.7011 1.0784 0.6873 0.1955  0.0593  -0.2435 363 ALA B N   
988  C CA  . ALA A 148 ? 0.7032 1.1191 0.6860 0.1840  0.0705  -0.2117 363 ALA B CA  
989  C C   . ALA A 148 ? 0.7115 1.2051 0.6639 0.1991  0.0741  -0.2069 363 ALA B C   
990  O O   . ALA A 148 ? 0.7330 1.2629 0.6694 0.2262  0.0637  -0.2364 363 ALA B O   
991  C CB  . ALA A 148 ? 0.7027 1.1128 0.6980 0.1835  0.0581  -0.2133 363 ALA B CB  
992  N N   . GLN A 149 ? 0.7117 1.2321 0.6555 0.1805  0.0884  -0.1698 364 GLN B N   
993  C CA  . GLN A 149 ? 0.7624 1.3632 0.6763 0.1853  0.0964  -0.1579 364 GLN B CA  
994  C C   . GLN A 149 ? 0.8050 1.4176 0.7022 0.1717  0.0969  -0.1223 364 GLN B C   
995  O O   . GLN A 149 ? 0.8082 1.3796 0.7150 0.1459  0.1040  -0.0897 364 GLN B O   
996  C CB  . GLN A 149 ? 0.7307 1.3558 0.6463 0.1699  0.1155  -0.1445 364 GLN B CB  
997  C CG  . GLN A 149 ? 0.7524 1.4002 0.6682 0.1962  0.1092  -0.1824 364 GLN B CG  
998  C CD  . GLN A 149 ? 0.7936 1.4681 0.7151 0.1807  0.1188  -0.1690 364 GLN B CD  
999  O OE1 . GLN A 149 ? 0.8448 1.4806 0.7808 0.1809  0.1178  -0.1787 364 GLN B OE1 
1000 N NE2 . GLN A 149 ? 0.7809 1.5242 0.6903 0.1671  0.1271  -0.1478 364 GLN B NE2 
1001 N N   . LEU A 150 ? 0.9670 1.6314 0.8362 0.1918  0.0864  -0.1304 365 LEU B N   
1002 C CA  . LEU A 150 ? 0.9929 1.6665 0.8366 0.1831  0.0826  -0.0956 365 LEU B CA  
1003 C C   . LEU A 150 ? 1.0181 1.7125 0.8425 0.1505  0.1032  -0.0477 365 LEU B C   
1004 O O   . LEU A 150 ? 0.9695 1.7172 0.7888 0.1425  0.1206  -0.0481 365 LEU B O   
1005 C CB  . LEU A 150 ? 1.0083 1.7465 0.8176 0.2122  0.0688  -0.1144 365 LEU B CB  
1006 C CG  . LEU A 150 ? 1.0817 1.8066 0.8710 0.2169  0.0511  -0.0952 365 LEU B CG  
1007 C CD1 . LEU A 150 ? 1.0923 1.8748 0.8549 0.2524  0.0322  -0.1287 365 LEU B CD1 
1008 C CD2 . LEU A 150 ? 1.1218 1.8545 0.8754 0.1897  0.0627  -0.0366 365 LEU B CD2 
1009 N N   . GLU A 151 ? 0.9780 1.6269 0.7944 0.1310  0.0992  -0.0081 366 GLU B N   
1010 C CA  . GLU A 151 ? 0.9370 1.5929 0.7301 0.0956  0.1141  0.0421  366 GLU B CA  
1011 C C   . GLU A 151 ? 1.0014 1.6338 0.7579 0.0933  0.0984  0.0790  366 GLU B C   
1012 O O   . GLU A 151 ? 1.0663 1.7422 0.7911 0.1171  0.0868  0.0707  366 GLU B O   
1013 C CB  . GLU A 151 ? 0.9326 1.5286 0.7611 0.0685  0.1242  0.0532  366 GLU B CB  
1014 C CG  . GLU A 151 ? 0.8652 1.4960 0.7182 0.0709  0.1393  0.0223  366 GLU B CG  
1015 C CD  . GLU A 151 ? 0.8151 1.4658 0.6704 0.0346  0.1594  0.0487  366 GLU B CD  
1016 O OE1 . GLU A 151 ? 0.8862 1.4837 0.7416 0.0046  0.1595  0.0853  366 GLU B OE1 
1017 O OE2 . GLU A 151 ? 0.7522 1.4726 0.6109 0.0371  0.1727  0.0304  366 GLU B OE2 
1018 N N   . ASP A 152 ? 1.0122 1.5750 0.7686 0.0686  0.0944  0.1180  367 ASP B N   
1019 C CA  . ASP A 152 ? 1.0850 1.6234 0.7969 0.0688  0.0759  0.1568  367 ASP B CA  
1020 C C   . ASP A 152 ? 1.1029 1.5964 0.8351 0.1043  0.0473  0.1299  367 ASP B C   
1021 O O   . ASP A 152 ? 1.1180 1.5363 0.8682 0.1041  0.0315  0.1404  367 ASP B O   
1022 C CB  . ASP A 152 ? 1.0886 1.5660 0.7846 0.0296  0.0777  0.2109  367 ASP B CB  
1023 C CG  . ASP A 152 ? 1.1304 1.6023 0.7593 0.0217  0.0642  0.2620  367 ASP B CG  
1024 O OD1 . ASP A 152 ? 1.0883 1.6376 0.6761 0.0345  0.0672  0.2613  367 ASP B OD1 
1025 O OD2 . ASP A 152 ? 1.1990 1.5882 0.8124 0.0042  0.0489  0.3024  367 ASP B OD2 
1026 N N   . GLY A 153 ? 1.1493 1.6955 0.8802 0.1364  0.0392  0.0912  368 GLY B N   
1027 C CA  . GLY A 153 ? 1.1326 1.6532 0.8912 0.1682  0.0137  0.0568  368 GLY B CA  
1028 C C   . GLY A 153 ? 1.1233 1.6091 0.9469 0.1683  0.0193  0.0180  368 GLY B C   
1029 O O   . GLY A 153 ? 1.0837 1.5869 0.9341 0.1889  0.0119  -0.0271 368 GLY B O   
1030 N N   . ARG A 154 ? 1.0483 1.4837 0.8946 0.1432  0.0320  0.0360  369 ARG B N   
1031 C CA  . ARG A 154 ? 0.9511 1.3545 0.8517 0.1391  0.0408  0.0052  369 ARG B CA  
1032 C C   . ARG A 154 ? 0.8985 1.3426 0.8065 0.1381  0.0587  -0.0220 369 ARG B C   
1033 O O   . ARG A 154 ? 0.9092 1.4083 0.7852 0.1366  0.0685  -0.0147 369 ARG B O   
1034 C CB  . ARG A 154 ? 0.9153 1.2605 0.8314 0.1140  0.0493  0.0308  369 ARG B CB  
1035 C CG  . ARG A 154 ? 0.9681 1.2564 0.8988 0.1231  0.0279  0.0383  369 ARG B CG  
1036 C CD  . ARG A 154 ? 0.9173 1.1656 0.9022 0.1202  0.0331  0.0124  369 ARG B CD  
1037 N NE  . ARG A 154 ? 0.9278 1.1241 0.9249 0.1287  0.0135  0.0216  369 ARG B NE  
1038 C CZ  . ARG A 154 ? 0.9476 1.1252 0.9915 0.1400  0.0082  -0.0082 369 ARG B CZ  
1039 N NH1 . ARG A 154 ? 0.8344 1.0356 0.9159 0.1384  0.0228  -0.0447 369 ARG B NH1 
1040 N NH2 . ARG A 154 ? 1.0084 1.1428 1.0600 0.1534  -0.0132 -0.0014 369 ARG B NH2 
1041 N N   . PHE A 155 ? 0.8710 1.2882 0.8206 0.1393  0.0622  -0.0536 370 PHE B N   
1042 C CA  . PHE A 155 ? 0.7982 1.2329 0.7560 0.1388  0.0755  -0.0780 370 PHE B CA  
1043 C C   . PHE A 155 ? 0.7519 1.1494 0.7293 0.1154  0.0930  -0.0666 370 PHE B C   
1044 O O   . PHE A 155 ? 0.7827 1.1319 0.7845 0.1055  0.0922  -0.0605 370 PHE B O   
1045 C CB  . PHE A 155 ? 0.7434 1.1702 0.7255 0.1565  0.0634  -0.1212 370 PHE B CB  
1046 C CG  . PHE A 155 ? 0.7938 1.2649 0.7551 0.1817  0.0453  -0.1401 370 PHE B CG  
1047 C CD1 . PHE A 155 ? 0.8659 1.3976 0.7869 0.1924  0.0483  -0.1351 370 PHE B CD1 
1048 C CD2 . PHE A 155 ? 0.7788 1.2396 0.7618 0.1947  0.0253  -0.1663 370 PHE B CD2 
1049 C CE1 . PHE A 155 ? 0.8576 1.4360 0.7552 0.2187  0.0309  -0.1557 370 PHE B CE1 
1050 C CE2 . PHE A 155 ? 0.8193 1.3230 0.7822 0.2195  0.0058  -0.1871 370 PHE B CE2 
1051 C CZ  . PHE A 155 ? 0.8048 1.3661 0.7225 0.2331  0.0082  -0.1822 370 PHE B CZ  
1052 N N   . VAL A 156 ? 0.7076 1.1337 0.6743 0.1090  0.1073  -0.0662 371 VAL B N   
1053 C CA  . VAL A 156 ? 0.6884 1.0878 0.6708 0.0889  0.1222  -0.0588 371 VAL B CA  
1054 C C   . VAL A 156 ? 0.6729 1.0687 0.6662 0.1008  0.1244  -0.0920 371 VAL B C   
1055 O O   . VAL A 156 ? 0.6806 1.1158 0.6596 0.1210  0.1192  -0.1135 371 VAL B O   
1056 C CB  . VAL A 156 ? 0.7320 1.1692 0.6946 0.0687  0.1356  -0.0294 371 VAL B CB  
1057 C CG1 . VAL A 156 ? 0.6680 1.0717 0.6501 0.0467  0.1470  -0.0221 371 VAL B CG1 
1058 C CG2 . VAL A 156 ? 0.8002 1.2424 0.7385 0.0575  0.1304  0.0068  371 VAL B CG2 
1059 N N   . TYR A 157 ? 0.6523 0.9992 0.6672 0.0899  0.1302  -0.0967 372 TYR B N   
1060 C CA  . TYR A 157 ? 0.6450 0.9750 0.6634 0.0978  0.1313  -0.1213 372 TYR B CA  
1061 C C   . TYR A 157 ? 0.6104 0.9358 0.6297 0.0828  0.1445  -0.1098 372 TYR B C   
1062 O O   . TYR A 157 ? 0.6128 0.9058 0.6459 0.0641  0.1514  -0.0948 372 TYR B O   
1063 C CB  . TYR A 157 ? 0.6289 0.9066 0.6677 0.0962  0.1263  -0.1378 372 TYR B CB  
1064 C CG  . TYR A 157 ? 0.6725 0.9566 0.7186 0.1071  0.1119  -0.1504 372 TYR B CG  
1065 C CD1 . TYR A 157 ? 0.6518 0.9419 0.7069 0.1037  0.1079  -0.1354 372 TYR B CD1 
1066 C CD2 . TYR A 157 ? 0.6759 0.9566 0.7195 0.1222  0.0986  -0.1791 372 TYR B CD2 
1067 C CE1 . TYR A 157 ? 0.6382 0.9390 0.7012 0.1161  0.0921  -0.1496 372 TYR B CE1 
1068 C CE2 . TYR A 157 ? 0.6659 0.9556 0.7190 0.1312  0.0834  -0.1943 372 TYR B CE2 
1069 C CZ  . TYR A 157 ? 0.6580 0.9617 0.7218 0.1284  0.0807  -0.1798 372 TYR B CZ  
1070 O OH  . TYR A 157 ? 0.6988 1.0167 0.7729 0.1400  0.0630  -0.1975 372 TYR B OH  
1071 N N   . ARG A 158 ? 0.5809 0.9426 0.5870 0.0937  0.1457  -0.1200 373 ARG B N   
1072 C CA  . ARG A 158 ? 0.5716 0.9529 0.5786 0.0797  0.1568  -0.1084 373 ARG B CA  
1073 C C   . ARG A 158 ? 0.5592 0.9215 0.5626 0.0934  0.1535  -0.1300 373 ARG B C   
1074 O O   . ARG A 158 ? 0.5321 0.9234 0.5226 0.1189  0.1444  -0.1519 373 ARG B O   
1075 C CB  . ARG A 158 ? 0.5391 1.0001 0.5345 0.0783  0.1619  -0.0989 373 ARG B CB  
1076 C CG  . ARG A 158 ? 0.5650 1.0316 0.5596 0.0524  0.1679  -0.0652 373 ARG B CG  
1077 C CD  . ARG A 158 ? 0.6438 1.1930 0.6203 0.0483  0.1741  -0.0532 373 ARG B CD  
1078 N NE  . ARG A 158 ? 0.7295 1.2733 0.7085 0.0109  0.1832  -0.0171 373 ARG B NE  
1079 C CZ  . ARG A 158 ? 0.7113 1.3043 0.6944 -0.0118 0.1951  -0.0069 373 ARG B CZ  
1080 N NH1 . ARG A 158 ? 0.5882 1.2624 0.5702 0.0017  0.2009  -0.0283 373 ARG B NH1 
1081 N NH2 . ARG A 158 ? 0.7362 1.2965 0.7276 -0.0480 0.1993  0.0218  373 ARG B NH2 
1082 N N   . LEU A 159 ? 0.5501 0.8630 0.5616 0.0793  0.1586  -0.1249 374 LEU B N   
1083 C CA  . LEU A 159 ? 0.5457 0.8347 0.5473 0.0897  0.1551  -0.1393 374 LEU B CA  
1084 C C   . LEU A 159 ? 0.5681 0.8766 0.5772 0.0727  0.1643  -0.1279 374 LEU B C   
1085 O O   . LEU A 159 ? 0.5473 0.8154 0.5631 0.0558  0.1705  -0.1199 374 LEU B O   
1086 C CB  . LEU A 159 ? 0.5744 0.7910 0.5737 0.0863  0.1532  -0.1438 374 LEU B CB  
1087 C CG  . LEU A 159 ? 0.6288 0.8249 0.6318 0.0912  0.1460  -0.1518 374 LEU B CG  
1088 C CD1 . LEU A 159 ? 0.5695 0.7674 0.5950 0.0732  0.1535  -0.1372 374 LEU B CD1 
1089 C CD2 . LEU A 159 ? 0.6949 0.8274 0.6871 0.0918  0.1401  -0.1627 374 LEU B CD2 
1090 N N   . LEU A 160 ? 0.4924 0.8697 0.5022 0.0758  0.1655  -0.1292 375 LEU B N   
1091 C CA  . LEU A 160 ? 0.5005 0.9080 0.5227 0.0540  0.1737  -0.1184 375 LEU B CA  
1092 C C   . LEU A 160 ? 0.4802 0.9032 0.4961 0.0718  0.1667  -0.1387 375 LEU B C   
1093 O O   . LEU A 160 ? 0.4619 0.9063 0.4645 0.1034  0.1554  -0.1603 375 LEU B O   
1094 C CB  . LEU A 160 ? 0.4867 0.9693 0.5164 0.0378  0.1814  -0.1039 375 LEU B CB  
1095 C CG  . LEU A 160 ? 0.5098 0.9735 0.5378 0.0249  0.1841  -0.0822 375 LEU B CG  
1096 C CD1 . LEU A 160 ? 0.5043 1.0389 0.5301 0.0072  0.1919  -0.0636 375 LEU B CD1 
1097 C CD2 . LEU A 160 ? 0.4744 0.8670 0.5131 0.0034  0.1855  -0.0655 375 LEU B CD2 
1098 N N   . ARG A 161 ? 0.5124 0.9217 0.5366 0.0546  0.1701  -0.1341 376 ARG B N   
1099 C CA  . ARG A 161 ? 0.5004 0.9377 0.5208 0.0696  0.1621  -0.1523 376 ARG B CA  
1100 C C   . ARG A 161 ? 0.4909 0.8819 0.4824 0.1055  0.1466  -0.1712 376 ARG B C   
1101 O O   . ARG A 161 ? 0.4908 0.9151 0.4739 0.1322  0.1336  -0.1913 376 ARG B O   
1102 C CB  . ARG A 161 ? 0.4506 0.9903 0.4857 0.0721  0.1633  -0.1609 376 ARG B CB  
1103 C CG  . ARG A 161 ? 0.4773 1.0582 0.5362 0.0294  0.1784  -0.1370 376 ARG B CG  
1104 C CD  . ARG A 161 ? 0.4488 1.1255 0.5207 0.0239  0.1779  -0.1399 376 ARG B CD  
1105 N NE  . ARG A 161 ? 0.4620 1.1815 0.5451 0.0329  0.1678  -0.1610 376 ARG B NE  
1106 C CZ  . ARG A 161 ? 0.4473 1.1802 0.5503 0.0068  0.1739  -0.1604 376 ARG B CZ  
1107 N NH1 . ARG A 161 ? 0.4454 1.1285 0.5562 -0.0295 0.1844  -0.1377 376 ARG B NH1 
1108 N NH2 . ARG A 161 ? 0.4531 1.2384 0.5675 0.0182  0.1622  -0.1831 376 ARG B NH2 
1109 N N   . SER A 162 ? 0.4947 0.8083 0.4706 0.1058  0.1463  -0.1651 377 SER B N   
1110 C CA  . SER A 162 ? 0.5480 0.8016 0.4916 0.1296  0.1321  -0.1760 377 SER B CA  
1111 C C   . SER A 162 ? 0.5560 0.8031 0.4893 0.1296  0.1287  -0.1786 377 SER B C   
1112 O O   . SER A 162 ? 0.5685 0.8074 0.5142 0.1029  0.1412  -0.1671 377 SER B O   
1113 C CB  . SER A 162 ? 0.5631 0.7391 0.4955 0.1172  0.1371  -0.1651 377 SER B CB  
1114 O OG  . SER A 162 ? 0.6621 0.8500 0.6155 0.1046  0.1454  -0.1580 377 SER B OG  
1115 N N   . PRO A 163 ? 0.5758 0.8242 0.4852 0.1617  0.1093  -0.1955 378 PRO B N   
1116 C CA  . PRO A 163 ? 0.5892 0.8235 0.4816 0.1647  0.1030  -0.1980 378 PRO B CA  
1117 C C   . PRO A 163 ? 0.6327 0.7839 0.4991 0.1471  0.1110  -0.1814 378 PRO B C   
1118 O O   . PRO A 163 ? 0.6557 0.7422 0.4964 0.1503  0.1085  -0.1746 378 PRO B O   
1119 C CB  . PRO A 163 ? 0.6248 0.8615 0.4888 0.2101  0.0754  -0.2194 378 PRO B CB  
1120 C CG  . PRO A 163 ? 0.6116 0.9033 0.4947 0.2283  0.0709  -0.2341 378 PRO B CG  
1121 C CD  . PRO A 163 ? 0.5890 0.8508 0.4838 0.2007  0.0890  -0.2159 378 PRO B CD  
1122 N N   . MET A 164 ? 0.6099 0.7675 0.4846 0.1263  0.1211  -0.1766 379 MET B N   
1123 C CA  . MET A 164 ? 0.6560 0.7504 0.5049 0.1115  0.1301  -0.1650 379 MET B CA  
1124 C C   . MET A 164 ? 0.7139 0.7535 0.5065 0.1366  0.1122  -0.1654 379 MET B C   
1125 O O   . MET A 164 ? 0.6982 0.7583 0.4751 0.1654  0.0912  -0.1789 379 MET B O   
1126 C CB  . MET A 164 ? 0.5967 0.7167 0.4638 0.0918  0.1390  -0.1673 379 MET B CB  
1127 C CG  . MET A 164 ? 0.6774 0.7534 0.5348 0.0712  0.1549  -0.1582 379 MET B CG  
1128 S SD  . MET A 164 ? 0.6314 0.7345 0.5173 0.0494  0.1631  -0.1664 379 MET B SD  
1129 C CE  . MET A 164 ? 0.6128 0.7750 0.5093 0.0610  0.1446  -0.1828 379 MET B CE  
1130 N N   . CYS A 165 ? 0.7760 0.7460 0.5370 0.1257  0.1188  -0.1504 380 CYS B N   
1131 C CA  . CYS A 165 ? 0.8762 0.7815 0.5756 0.1455  0.1003  -0.1448 380 CYS B CA  
1132 C C   . CYS A 165 ? 0.8801 0.7900 0.5503 0.1520  0.0951  -0.1468 380 CYS B C   
1133 O O   . CYS A 165 ? 0.8658 0.8031 0.5548 0.1303  0.1128  -0.1472 380 CYS B O   
1134 C CB  . CYS A 165 ? 0.9619 0.7932 0.6329 0.1234  0.1111  -0.1249 380 CYS B CB  
1135 S SG  . CYS A 165 ? 0.9654 0.8046 0.6596 0.0790  0.1476  -0.1135 380 CYS B SG  
1136 N N   . GLU A 166 ? 0.9849 0.7577 0.6838 0.3683  -0.1162 -0.0148 381 GLU B N   
1137 C CA  . GLU A 166 ? 1.0373 0.8246 0.7221 0.3765  -0.1288 -0.0084 381 GLU B CA  
1138 C C   . GLU A 166 ? 1.0588 0.7595 0.7015 0.3407  -0.1192 0.0224  381 GLU B C   
1139 O O   . GLU A 166 ? 1.0310 0.7498 0.6637 0.3413  -0.1262 0.0303  381 GLU B O   
1140 C CB  . GLU A 166 ? 1.1411 0.9173 0.7989 0.4177  -0.1572 -0.0304 381 GLU B CB  
1141 C CG  . GLU A 166 ? 1.1965 1.1019 0.8973 0.4515  -0.1692 -0.0602 381 GLU B CG  
1142 C CD  . GLU A 166 ? 1.4808 1.3661 1.1524 0.4969  -0.1972 -0.0877 381 GLU B CD  
1143 O OE1 . GLU A 166 ? 1.5082 1.4985 1.2118 0.5282  -0.2071 -0.1216 381 GLU B OE1 
1144 O OE2 . GLU A 166 ? 1.5763 1.3387 1.1885 0.4986  -0.2094 -0.0757 381 GLU B OE2 
1145 N N   . TYR A 167 ? 1.0663 0.6832 0.6840 0.3071  -0.1032 0.0367  382 TYR B N   
1146 C CA  . TYR A 167 ? 1.0451 0.6075 0.6318 0.2672  -0.0885 0.0611  382 TYR B CA  
1147 C C   . TYR A 167 ? 0.9802 0.6183 0.6159 0.2362  -0.0657 0.0660  382 TYR B C   
1148 O O   . TYR A 167 ? 0.9859 0.6247 0.6086 0.2195  -0.0618 0.0762  382 TYR B O   
1149 C CB  . TYR A 167 ? 1.0700 0.5505 0.6278 0.2302  -0.0734 0.0696  382 TYR B CB  
1150 C CG  . TYR A 167 ? 1.1341 0.5838 0.6702 0.1842  -0.0521 0.0891  382 TYR B CG  
1151 C CD1 . TYR A 167 ? 1.0712 0.5650 0.6478 0.1544  -0.0254 0.0921  382 TYR B CD1 
1152 C CD2 . TYR A 167 ? 1.1882 0.5771 0.6674 0.1695  -0.0585 0.1001  382 TYR B CD2 
1153 C CE1 . TYR A 167 ? 1.0860 0.5665 0.6479 0.1153  -0.0053 0.1021  382 TYR B CE1 
1154 C CE2 . TYR A 167 ? 1.1550 0.5287 0.6142 0.1275  -0.0378 0.1137  382 TYR B CE2 
1155 C CZ  . TYR A 167 ? 1.1439 0.5600 0.6409 0.1027  -0.0108 0.1144  382 TYR B CZ  
1156 O OH  . TYR A 167 ? 1.1973 0.6053 0.6737 0.0631  0.0108  0.1223  382 TYR B OH  
1157 N N   . LEU A 168 ? 0.9800 0.6824 0.6712 0.2240  -0.0508 0.0567  383 LEU B N   
1158 C CA  . LEU A 168 ? 0.8864 0.6482 0.6203 0.1903  -0.0314 0.0608  383 LEU B CA  
1159 C C   . LEU A 168 ? 0.8447 0.6852 0.6005 0.1992  -0.0414 0.0539  383 LEU B C   
1160 O O   . LEU A 168 ? 0.8208 0.6770 0.5829 0.1747  -0.0338 0.0600  383 LEU B O   
1161 C CB  . LEU A 168 ? 0.8518 0.6464 0.6266 0.1740  -0.0166 0.0568  383 LEU B CB  
1162 C CG  . LEU A 168 ? 0.9034 0.6468 0.6734 0.1476  0.0007  0.0633  383 LEU B CG  
1163 C CD1 . LEU A 168 ? 0.8839 0.6654 0.6911 0.1419  0.0078  0.0567  383 LEU B CD1 
1164 C CD2 . LEU A 168 ? 0.8507 0.5867 0.6232 0.1184  0.0155  0.0719  383 LEU B CD2 
1165 N N   . VAL A 169 ? 0.8706 0.7660 0.6381 0.2335  -0.0588 0.0375  384 VAL B N   
1166 C CA  . VAL A 169 ? 0.8127 0.7965 0.6016 0.2389  -0.0686 0.0271  384 VAL B CA  
1167 C C   . VAL A 169 ? 0.8139 0.7645 0.5662 0.2450  -0.0810 0.0343  384 VAL B C   
1168 O O   . VAL A 169 ? 0.7962 0.7892 0.5607 0.2210  -0.0771 0.0353  384 VAL B O   
1169 C CB  . VAL A 169 ? 0.7613 0.8221 0.5696 0.2808  -0.0864 0.0015  384 VAL B CB  
1170 C CG1 . VAL A 169 ? 0.6983 0.8712 0.5354 0.2772  -0.0932 -0.0124 384 VAL B CG1 
1171 C CG2 . VAL A 169 ? 0.7289 0.8206 0.5667 0.2730  -0.0731 -0.0061 384 VAL B CG2 
1172 N N   . ASN A 170 ? 0.8556 0.7240 0.5557 0.2749  -0.0976 0.0398  385 ASN B N   
1173 C CA  . ASN A 170 ? 0.8414 0.6655 0.4943 0.2764  -0.1090 0.0513  385 ASN B CA  
1174 C C   . ASN A 170 ? 0.8588 0.6515 0.5073 0.2256  -0.0828 0.0670  385 ASN B C   
1175 O O   . ASN A 170 ? 0.8369 0.6598 0.4856 0.2097  -0.0822 0.0671  385 ASN B O   
1176 C CB  . ASN A 170 ? 1.0047 0.7240 0.5884 0.3101  -0.1314 0.0602  385 ASN B CB  
1177 C CG  . ASN A 170 ? 1.0699 0.8236 0.6583 0.3618  -0.1604 0.0365  385 ASN B CG  
1178 O OD1 . ASN A 170 ? 1.0462 0.9099 0.6782 0.3834  -0.1704 0.0166  385 ASN B OD1 
1179 N ND2 . ASN A 170 ? 1.1570 0.8241 0.7024 0.3759  -0.1724 0.0346  385 ASN B ND2 
1180 N N   . PHE A 171 ? 0.8671 0.6040 0.5121 0.2011  -0.0620 0.0764  386 PHE B N   
1181 C CA  . PHE A 171 ? 0.8641 0.5810 0.5084 0.1595  -0.0381 0.0847  386 PHE B CA  
1182 C C   . PHE A 171 ? 0.8895 0.6782 0.5801 0.1389  -0.0297 0.0764  386 PHE B C   
1183 O O   . PHE A 171 ? 0.8889 0.6778 0.5669 0.1216  -0.0260 0.0766  386 PHE B O   
1184 C CB  . PHE A 171 ? 0.8652 0.5415 0.5160 0.1386  -0.0176 0.0886  386 PHE B CB  
1185 C CG  . PHE A 171 ? 0.9011 0.5750 0.5621 0.1021  0.0065  0.0895  386 PHE B CG  
1186 C CD1 . PHE A 171 ? 0.9461 0.5837 0.5624 0.0854  0.0125  0.0953  386 PHE B CD1 
1187 C CD2 . PHE A 171 ? 0.8396 0.5499 0.5514 0.0871  0.0210  0.0825  386 PHE B CD2 
1188 C CE1 . PHE A 171 ? 0.9043 0.5517 0.5331 0.0564  0.0348  0.0887  386 PHE B CE1 
1189 C CE2 . PHE A 171 ? 0.8804 0.5905 0.6030 0.0632  0.0389  0.0776  386 PHE B CE2 
1190 C CZ  . PHE A 171 ? 0.8751 0.5587 0.5593 0.0487  0.0469  0.0780  386 PHE B CZ  
1191 N N   . LEU A 172 ? 0.8258 0.6724 0.5635 0.1381  -0.0280 0.0688  387 LEU B N   
1192 C CA  . LEU A 172 ? 0.7814 0.6820 0.5529 0.1119  -0.0220 0.0639  387 LEU B CA  
1193 C C   . LEU A 172 ? 0.7935 0.7375 0.5564 0.1132  -0.0363 0.0566  387 LEU B C   
1194 O O   . LEU A 172 ? 0.7784 0.7255 0.5421 0.0863  -0.0309 0.0546  387 LEU B O   
1195 C CB  . LEU A 172 ? 0.7349 0.6911 0.5453 0.1086  -0.0205 0.0597  387 LEU B CB  
1196 C CG  . LEU A 172 ? 0.7726 0.7017 0.5995 0.0972  -0.0062 0.0660  387 LEU B CG  
1197 C CD1 . LEU A 172 ? 0.7277 0.7170 0.5810 0.1024  -0.0092 0.0609  387 LEU B CD1 
1198 C CD2 . LEU A 172 ? 0.7131 0.6183 0.5486 0.0664  0.0054  0.0712  387 LEU B CD2 
1199 N N   . HIS A 173 ? 0.7159 0.6980 0.4720 0.1464  -0.0567 0.0489  388 HIS B N   
1200 C CA  . HIS A 173 ? 0.7756 0.8076 0.5236 0.1510  -0.0733 0.0394  388 HIS B CA  
1201 C C   . HIS A 173 ? 0.8269 0.7986 0.5310 0.1411  -0.0722 0.0477  388 HIS B C   
1202 O O   . HIS A 173 ? 0.8590 0.8561 0.5649 0.1162  -0.0709 0.0414  388 HIS B O   
1203 C CB  . HIS A 173 ? 0.7904 0.8660 0.5330 0.2008  -0.1002 0.0274  388 HIS B CB  
1204 C CG  . HIS A 173 ? 0.8471 1.0352 0.6395 0.2023  -0.1035 0.0078  388 HIS B CG  
1205 N ND1 . HIS A 173 ? 0.8617 1.1342 0.6833 0.1655  -0.0994 -0.0025 388 HIS B ND1 
1206 C CD2 . HIS A 173 ? 0.8100 1.0422 0.6265 0.2287  -0.1075 -0.0046 388 HIS B CD2 
1207 C CE1 . HIS A 173 ? 0.8638 1.2343 0.7243 0.1667  -0.1000 -0.0191 388 HIS B CE1 
1208 N NE2 . HIS A 173 ? 0.7805 1.1326 0.6405 0.2076  -0.1048 -0.0222 388 HIS B NE2 
1209 N N   . LYS A 174 ? 0.8087 0.6995 0.4684 0.1560  -0.0722 0.0609  389 LYS B N   
1210 C CA  . LYS A 174 ? 0.9374 0.7759 0.5507 0.1404  -0.0672 0.0689  389 LYS B CA  
1211 C C   . LYS A 174 ? 0.9245 0.7644 0.5606 0.0994  -0.0428 0.0636  389 LYS B C   
1212 O O   . LYS A 174 ? 0.9214 0.7678 0.5410 0.0834  -0.0425 0.0573  389 LYS B O   
1213 C CB  . LYS A 174 ? 0.9216 0.6704 0.4824 0.1486  -0.0649 0.0857  389 LYS B CB  
1214 C CG  . LYS A 174 ? 0.9230 0.6388 0.4316 0.1892  -0.0958 0.0933  389 LYS B CG  
1215 C CD  . LYS A 174 ? 1.0000 0.6265 0.4704 0.1926  -0.0922 0.1080  389 LYS B CD  
1216 C CE  . LYS A 174 ? 1.0376 0.6186 0.4627 0.2378  -0.1261 0.1120  389 LYS B CE  
1217 N NZ  . LYS A 174 ? 1.1759 0.6844 0.5901 0.2242  -0.1141 0.1174  389 LYS B NZ  
1218 N N   . LEU A 175 ? 0.8586 0.6907 0.5304 0.0854  -0.0249 0.0639  390 LEU B N   
1219 C CA  . LEU A 175 ? 0.8435 0.6659 0.5332 0.0557  -0.0064 0.0569  390 LEU B CA  
1220 C C   . LEU A 175 ? 0.8506 0.7181 0.5620 0.0375  -0.0130 0.0453  390 LEU B C   
1221 O O   . LEU A 175 ? 0.8876 0.7416 0.5920 0.0178  -0.0071 0.0350  390 LEU B O   
1222 C CB  . LEU A 175 ? 0.8203 0.6267 0.5412 0.0514  0.0080  0.0600  390 LEU B CB  
1223 C CG  . LEU A 175 ? 0.8308 0.6063 0.5585 0.0359  0.0273  0.0538  390 LEU B CG  
1224 C CD1 . LEU A 175 ? 0.8525 0.5976 0.5375 0.0323  0.0365  0.0539  390 LEU B CD1 
1225 C CD2 . LEU A 175 ? 0.8072 0.5762 0.5633 0.0398  0.0352  0.0580  390 LEU B CD2 
1226 N N   . ARG A 176 ? 0.8350 0.7585 0.5706 0.0414  -0.0253 0.0439  391 ARG B N   
1227 C CA  . ARG A 176 ? 0.8310 0.8040 0.5826 0.0154  -0.0322 0.0330  391 ARG B CA  
1228 C C   . ARG A 176 ? 0.8655 0.8451 0.5887 0.0091  -0.0407 0.0223  391 ARG B C   
1229 O O   . ARG A 176 ? 0.8617 0.8481 0.5879 -0.0218 -0.0406 0.0109  391 ARG B O   
1230 C CB  . ARG A 176 ? 0.8298 0.8829 0.6067 0.0232  -0.0442 0.0298  391 ARG B CB  
1231 C CG  . ARG A 176 ? 0.8567 0.9716 0.6553 -0.0155 -0.0471 0.0204  391 ARG B CG  
1232 C CD  . ARG A 176 ? 0.8804 1.0748 0.7090 -0.0073 -0.0509 0.0181  391 ARG B CD  
1233 N NE  . ARG A 176 ? 0.9103 1.1668 0.7583 -0.0542 -0.0488 0.0129  391 ARG B NE  
1234 C CZ  . ARG A 176 ? 0.8697 1.2382 0.7416 -0.0579 -0.0557 -0.0011 391 ARG B CZ  
1235 N NH1 . ARG A 176 ? 0.8147 1.2447 0.6975 -0.0082 -0.0685 -0.0140 391 ARG B NH1 
1236 N NH2 . ARG A 176 ? 0.8607 1.2809 0.7427 -0.1133 -0.0508 -0.0038 391 ARG B NH2 
1237 N N   . GLN A 177 ? 0.8728 0.8431 0.5618 0.0367  -0.0500 0.0261  392 GLN B N   
1238 C CA  . GLN A 177 ? 0.9165 0.9035 0.5733 0.0353  -0.0628 0.0169  392 GLN B CA  
1239 C C   . GLN A 177 ? 0.9398 0.8745 0.5687 0.0150  -0.0483 0.0115  392 GLN B C   
1240 O O   . GLN A 177 ? 0.9352 0.8888 0.5459 0.0009  -0.0554 -0.0025 392 GLN B O   
1241 C CB  . GLN A 177 ? 0.9854 0.9710 0.6044 0.0755  -0.0827 0.0261  392 GLN B CB  
1242 C CG  . GLN A 177 ? 1.0290 1.1018 0.6663 0.0967  -0.1086 0.0149  392 GLN B CG  
1243 C CD  . GLN A 177 ? 1.0590 1.1234 0.6764 0.1485  -0.1294 0.0236  392 GLN B CD  
1244 O OE1 . GLN A 177 ? 1.0582 1.0504 0.6191 0.1692  -0.1369 0.0390  392 GLN B OE1 
1245 N NE2 . GLN A 177 ? 1.0271 1.1610 0.6866 0.1684  -0.1389 0.0129  392 GLN B NE2 
1246 N N   . LEU A 178 ? 0.9268 0.8050 0.5515 0.0144  -0.0286 0.0184  393 LEU B N   
1247 C CA  . LEU A 178 ? 0.9198 0.7621 0.5175 0.0000  -0.0137 0.0085  393 LEU B CA  
1248 C C   . LEU A 178 ? 0.9292 0.7853 0.5383 -0.0249 -0.0151 -0.0147 393 LEU B C   
1249 O O   . LEU A 178 ? 0.8887 0.7572 0.5325 -0.0385 -0.0191 -0.0189 393 LEU B O   
1250 C CB  . LEU A 178 ? 0.9023 0.7041 0.5129 -0.0010 0.0087  0.0115  393 LEU B CB  
1251 C CG  . LEU A 178 ? 0.8897 0.6686 0.4860 0.0159  0.0112  0.0327  393 LEU B CG  
1252 C CD1 . LEU A 178 ? 0.9153 0.6666 0.5202 0.0067  0.0353  0.0290  393 LEU B CD1 
1253 C CD2 . LEU A 178 ? 0.9243 0.6878 0.4596 0.0263  -0.0008 0.0456  393 LEU B CD2 
1254 N N   . PRO A 179 ? 0.9013 0.7517 0.4759 -0.0344 -0.0129 -0.0304 394 PRO B N   
1255 C CA  . PRO A 179 ? 0.8925 0.7534 0.4706 -0.0582 -0.0190 -0.0556 394 PRO B CA  
1256 C C   . PRO A 179 ? 0.9171 0.7342 0.5160 -0.0700 -0.0062 -0.0741 394 PRO B C   
1257 O O   . PRO A 179 ? 0.9496 0.7584 0.5504 -0.0912 -0.0143 -0.0942 394 PRO B O   
1258 C CB  . PRO A 179 ? 0.8759 0.7471 0.4031 -0.0597 -0.0218 -0.0667 394 PRO B CB  
1259 C CG  . PRO A 179 ? 0.9085 0.7724 0.4007 -0.0374 -0.0210 -0.0409 394 PRO B CG  
1260 C CD  . PRO A 179 ? 0.9174 0.7521 0.4403 -0.0277 -0.0064 -0.0256 394 PRO B CD  
1261 N N   . GLU A 180 ? 0.8843 0.6714 0.4968 -0.0565 0.0106  -0.0700 395 GLU B N   
1262 C CA  . GLU A 180 ? 0.8825 0.6304 0.5110 -0.0573 0.0194  -0.0929 395 GLU B CA  
1263 C C   . GLU A 180 ? 0.8801 0.6103 0.5421 -0.0422 0.0276  -0.0789 395 GLU B C   
1264 O O   . GLU A 180 ? 0.8754 0.6201 0.5377 -0.0310 0.0375  -0.0608 395 GLU B O   
1265 C CB  . GLU A 180 ? 0.9291 0.6772 0.5312 -0.0534 0.0346  -0.1193 395 GLU B CB  
1266 C CG  . GLU A 180 ? 0.9160 0.6818 0.4794 -0.0677 0.0278  -0.1377 395 GLU B CG  
1267 C CD  . GLU A 180 ? 1.0079 0.7442 0.5757 -0.0800 0.0169  -0.1690 395 GLU B CD  
1268 O OE1 . GLU A 180 ? 1.0148 0.7653 0.5547 -0.0969 0.0067  -0.1856 395 GLU B OE1 
1269 O OE2 . GLU A 180 ? 1.0085 0.7018 0.6042 -0.0732 0.0153  -0.1758 395 GLU B OE2 
1270 N N   . ARG A 181 ? 0.9085 0.6012 0.5929 -0.0426 0.0214  -0.0875 396 ARG B N   
1271 C CA  . ARG A 181 ? 0.8725 0.5504 0.5874 -0.0266 0.0260  -0.0755 396 ARG B CA  
1272 C C   . ARG A 181 ? 0.8273 0.5198 0.5479 -0.0079 0.0462  -0.0875 396 ARG B C   
1273 O O   . ARG A 181 ? 0.7713 0.4777 0.5087 0.0010  0.0547  -0.0709 396 ARG B O   
1274 C CB  . ARG A 181 ? 0.9449 0.5676 0.6706 -0.0277 0.0115  -0.0841 396 ARG B CB  
1275 C CG  . ARG A 181 ? 1.0406 0.6544 0.7683 -0.0515 -0.0041 -0.0586 396 ARG B CG  
1276 C CD  . ARG A 181 ? 1.1671 0.7123 0.8961 -0.0534 -0.0196 -0.0568 396 ARG B CD  
1277 N NE  . ARG A 181 ? 1.1427 0.6719 0.8933 -0.0191 -0.0152 -0.0608 396 ARG B NE  
1278 C CZ  . ARG A 181 ? 1.1582 0.6461 0.9090 0.0063  -0.0196 -0.0896 396 ARG B CZ  
1279 N NH1 . ARG A 181 ? 1.2423 0.6880 0.9693 0.0019  -0.0290 -0.1173 396 ARG B NH1 
1280 N NH2 . ARG A 181 ? 1.1472 0.6402 0.9237 0.0387  -0.0162 -0.0945 396 ARG B NH2 
1281 N N   . TYR A 182 ? 0.8122 0.5086 0.5176 -0.0050 0.0552  -0.1191 397 TYR B N   
1282 C CA  . TYR A 182 ? 0.7900 0.5152 0.5028 0.0067  0.0771  -0.1345 397 TYR B CA  
1283 C C   . TYR A 182 ? 0.7716 0.5270 0.4612 -0.0057 0.0915  -0.1100 397 TYR B C   
1284 O O   . TYR A 182 ? 0.7618 0.5404 0.4594 -0.0044 0.1099  -0.1128 397 TYR B O   
1285 C CB  . TYR A 182 ? 0.8661 0.6011 0.5674 0.0123  0.0854  -0.1790 397 TYR B CB  
1286 C CG  . TYR A 182 ? 0.8600 0.6224 0.5159 -0.0074 0.0953  -0.1830 397 TYR B CG  
1287 C CD1 . TYR A 182 ? 0.8584 0.6609 0.4915 -0.0191 0.1178  -0.1759 397 TYR B CD1 
1288 C CD2 . TYR A 182 ? 0.8934 0.6393 0.5233 -0.0184 0.0807  -0.1926 397 TYR B CD2 
1289 C CE1 . TYR A 182 ? 0.9205 0.7408 0.5005 -0.0386 0.1240  -0.1755 397 TYR B CE1 
1290 C CE2 . TYR A 182 ? 0.9408 0.7134 0.5257 -0.0347 0.0867  -0.1960 397 TYR B CE2 
1291 C CZ  . TYR A 182 ? 0.9220 0.7294 0.4802 -0.0433 0.1074  -0.1859 397 TYR B CZ  
1292 O OH  . TYR A 182 ? 0.9606 0.7869 0.4648 -0.0603 0.1097  -0.1854 397 TYR B OH  
1293 N N   . MET A 183 ? 0.7746 0.5286 0.4333 -0.0176 0.0813  -0.0866 398 MET B N   
1294 C CA  . MET A 183 ? 0.8051 0.5675 0.4339 -0.0239 0.0883  -0.0601 398 MET B CA  
1295 C C   . MET A 183 ? 0.8122 0.5653 0.4664 -0.0150 0.0837  -0.0340 398 MET B C   
1296 O O   . MET A 183 ? 0.7766 0.5289 0.4231 -0.0182 0.0966  -0.0235 398 MET B O   
1297 C CB  . MET A 183 ? 0.8441 0.6083 0.4267 -0.0309 0.0745  -0.0466 398 MET B CB  
1298 C CG  . MET A 183 ? 0.8472 0.6240 0.3950 -0.0424 0.0800  -0.0707 398 MET B CG  
1299 S SD  . MET A 183 ? 0.9152 0.7006 0.4133 -0.0471 0.0568  -0.0582 398 MET B SD  
1300 C CE  . MET A 183 ? 0.9339 0.7367 0.3966 -0.0628 0.0693  -0.0955 398 MET B CE  
1301 N N   . MET A 184 ? 0.8138 0.5616 0.4940 -0.0082 0.0658  -0.0242 399 MET B N   
1302 C CA  . MET A 184 ? 0.7954 0.5405 0.5053 0.0010  0.0626  -0.0060 399 MET B CA  
1303 C C   . MET A 184 ? 0.7420 0.4866 0.4780 0.0059  0.0781  -0.0168 399 MET B C   
1304 O O   . MET A 184 ? 0.7304 0.4771 0.4706 0.0074  0.0857  -0.0049 399 MET B O   
1305 C CB  . MET A 184 ? 0.8298 0.5754 0.5652 0.0004  0.0454  -0.0012 399 MET B CB  
1306 C CG  . MET A 184 ? 0.8448 0.6089 0.5623 -0.0085 0.0300  0.0022  399 MET B CG  
1307 S SD  . MET A 184 ? 0.7938 0.5617 0.5350 -0.0257 0.0143  0.0029  399 MET B SD  
1308 C CE  . MET A 184 ? 0.8171 0.6389 0.5429 -0.0335 -0.0010 0.0068  399 MET B CE  
1309 N N   . ASN A 185 ? 0.7302 0.4738 0.4824 0.0099  0.0818  -0.0433 400 ASN B N   
1310 C CA  . ASN A 185 ? 0.7670 0.5230 0.5508 0.0209  0.0928  -0.0586 400 ASN B CA  
1311 C C   . ASN A 185 ? 0.7519 0.5376 0.5211 0.0089  0.1165  -0.0642 400 ASN B C   
1312 O O   . ASN A 185 ? 0.7600 0.5616 0.5500 0.0094  0.1250  -0.0614 400 ASN B O   
1313 C CB  . ASN A 185 ? 0.7214 0.4669 0.5232 0.0360  0.0865  -0.0903 400 ASN B CB  
1314 C CG  . ASN A 185 ? 0.7590 0.4667 0.5810 0.0471  0.0641  -0.0799 400 ASN B CG  
1315 O OD1 . ASN A 185 ? 0.7699 0.4770 0.6021 0.0447  0.0588  -0.0531 400 ASN B OD1 
1316 N ND2 . ASN A 185 ? 0.7557 0.4269 0.5774 0.0576  0.0497  -0.1009 400 ASN B ND2 
1317 N N   . SER A 186 ? 0.7040 0.4977 0.4323 -0.0072 0.1272  -0.0702 401 SER B N   
1318 C CA  . SER A 186 ? 0.7962 0.6149 0.5041 -0.0277 0.1507  -0.0722 401 SER B CA  
1319 C C   . SER A 186 ? 0.7557 0.5439 0.4310 -0.0408 0.1477  -0.0357 401 SER B C   
1320 O O   . SER A 186 ? 0.7451 0.5419 0.4131 -0.0590 0.1636  -0.0325 401 SER B O   
1321 C CB  . SER A 186 ? 0.7951 0.6368 0.4621 -0.0464 0.1670  -0.0917 401 SER B CB  
1322 O OG  . SER A 186 ? 0.8392 0.6527 0.4622 -0.0502 0.1531  -0.0769 401 SER B OG  
1323 N N   . VAL A 187 ? 0.7603 0.5146 0.4140 -0.0323 0.1267  -0.0112 402 VAL B N   
1324 C CA  . VAL A 187 ? 0.8252 0.5470 0.4580 -0.0319 0.1179  0.0183  402 VAL B CA  
1325 C C   . VAL A 187 ? 0.8082 0.5385 0.4892 -0.0236 0.1197  0.0180  402 VAL B C   
1326 O O   . VAL A 187 ? 0.7476 0.4707 0.4194 -0.0379 0.1308  0.0232  402 VAL B O   
1327 C CB  . VAL A 187 ? 0.8095 0.5124 0.4262 -0.0143 0.0920  0.0365  402 VAL B CB  
1328 C CG1 . VAL A 187 ? 0.8021 0.4727 0.4028 -0.0047 0.0806  0.0599  402 VAL B CG1 
1329 C CG2 . VAL A 187 ? 0.8394 0.5351 0.4031 -0.0215 0.0870  0.0382  402 VAL B CG2 
1330 N N   . LEU A 188 ? 0.7599 0.5038 0.4881 -0.0043 0.1082  0.0117  403 LEU B N   
1331 C CA  . LEU A 188 ? 0.7912 0.5444 0.5612 0.0049  0.1069  0.0126  403 LEU B CA  
1332 C C   . LEU A 188 ? 0.7794 0.5621 0.5705 -0.0044 0.1263  -0.0073 403 LEU B C   
1333 O O   . LEU A 188 ? 0.7608 0.5538 0.5784 -0.0014 0.1268  -0.0060 403 LEU B O   
1334 C CB  . LEU A 188 ? 0.7157 0.4733 0.5216 0.0217  0.0912  0.0099  403 LEU B CB  
1335 C CG  . LEU A 188 ? 0.7500 0.4978 0.5446 0.0258  0.0730  0.0279  403 LEU B CG  
1336 C CD1 . LEU A 188 ? 0.7583 0.5055 0.5760 0.0289  0.0603  0.0240  403 LEU B CD1 
1337 C CD2 . LEU A 188 ? 0.7405 0.4874 0.5343 0.0326  0.0667  0.0460  403 LEU B CD2 
1338 N N   . GLU A 189 ? 0.7525 0.5587 0.5334 -0.0163 0.1426  -0.0290 404 GLU B N   
1339 C CA  . GLU A 189 ? 0.7679 0.6229 0.5719 -0.0272 0.1633  -0.0543 404 GLU B CA  
1340 C C   . GLU A 189 ? 0.7916 0.6412 0.5738 -0.0556 0.1755  -0.0401 404 GLU B C   
1341 O O   . GLU A 189 ? 0.7655 0.6587 0.5785 -0.0645 0.1877  -0.0567 404 GLU B O   
1342 C CB  . GLU A 189 ? 0.7550 0.6441 0.5431 -0.0390 0.1807  -0.0816 404 GLU B CB  
1343 C CG  . GLU A 189 ? 0.7752 0.7377 0.6048 -0.0364 0.1981  -0.1227 404 GLU B CG  
1344 C CD  . GLU A 189 ? 0.8992 0.9017 0.7039 -0.0528 0.2183  -0.1506 404 GLU B CD  
1345 O OE1 . GLU A 189 ? 0.9581 0.9534 0.7651 -0.0303 0.2088  -0.1684 404 GLU B OE1 
1346 O OE2 . GLU A 189 ? 0.9198 0.9588 0.6967 -0.0923 0.2441  -0.1549 404 GLU B OE2 
1347 N N   . ASN A 190 ? 0.8067 0.6011 0.5335 -0.0696 0.1699  -0.0110 405 ASN B N   
1348 C CA  . ASN A 190 ? 0.8481 0.6135 0.5380 -0.0991 0.1778  0.0044  405 ASN B CA  
1349 C C   . ASN A 190 ? 0.8534 0.5768 0.5484 -0.0809 0.1579  0.0249  405 ASN B C   
1350 O O   . ASN A 190 ? 0.9384 0.6150 0.5919 -0.1001 0.1575  0.0403  405 ASN B O   
1351 C CB  . ASN A 190 ? 0.9368 0.6573 0.5469 -0.1271 0.1829  0.0216  405 ASN B CB  
1352 C CG  . ASN A 190 ? 0.9290 0.7015 0.5295 -0.1523 0.2072  -0.0017 405 ASN B CG  
1353 O OD1 . ASN A 190 ? 0.9811 0.7439 0.5468 -0.1512 0.2047  0.0007  405 ASN B OD1 
1354 N ND2 . ASN A 190 ? 0.8824 0.7207 0.5152 -0.1753 0.2311  -0.0284 405 ASN B ND2 
1355 N N   . PHE A 191 ? 0.8175 0.5545 0.5581 -0.0467 0.1411  0.0240  406 PHE B N   
1356 C CA  . PHE A 191 ? 0.8403 0.5484 0.5844 -0.0273 0.1221  0.0407  406 PHE B CA  
1357 C C   . PHE A 191 ? 0.7922 0.5397 0.5934 -0.0163 0.1212  0.0292  406 PHE B C   
1358 O O   . PHE A 191 ? 0.8133 0.5885 0.6526 0.0031  0.1138  0.0222  406 PHE B O   
1359 C CB  . PHE A 191 ? 0.8269 0.5229 0.5654 -0.0022 0.1023  0.0522  406 PHE B CB  
1360 C CG  . PHE A 191 ? 0.8298 0.5182 0.5796 0.0197  0.0845  0.0626  406 PHE B CG  
1361 C CD1 . PHE A 191 ? 0.8893 0.5332 0.5974 0.0272  0.0726  0.0752  406 PHE B CD1 
1362 C CD2 . PHE A 191 ? 0.8112 0.5350 0.6081 0.0336  0.0779  0.0586  406 PHE B CD2 
1363 C CE1 . PHE A 191 ? 0.8582 0.5062 0.5795 0.0513  0.0566  0.0779  406 PHE B CE1 
1364 C CE2 . PHE A 191 ? 0.7827 0.5124 0.5891 0.0504  0.0640  0.0655  406 PHE B CE2 
1365 C CZ  . PHE A 191 ? 0.8567 0.5550 0.6292 0.0608  0.0544  0.0722  406 PHE B CZ  
1366 N N   . THR A 192 ? 0.8263 0.5703 0.6279 -0.0296 0.1261  0.0279  407 THR B N   
1367 C CA  . THR A 192 ? 0.8235 0.6065 0.6748 -0.0182 0.1223  0.0177  407 THR B CA  
1368 C C   . THR A 192 ? 0.8489 0.6032 0.6902 -0.0110 0.1099  0.0291  407 THR B C   
1369 O O   . THR A 192 ? 0.8425 0.5429 0.6372 -0.0170 0.1057  0.0407  407 THR B O   
1370 C CB  . THR A 192 ? 0.8244 0.6553 0.6992 -0.0408 0.1405  -0.0050 407 THR B CB  
1371 O OG1 . THR A 192 ? 0.9009 0.7008 0.7363 -0.0755 0.1508  -0.0010 407 THR B OG1 
1372 C CG2 . THR A 192 ? 0.8234 0.6889 0.7044 -0.0467 0.1545  -0.0223 407 THR B CG2 
1373 N N   . ILE A 193 ? 0.8128 0.6011 0.6943 0.0044  0.1018  0.0241  408 ILE B N   
1374 C CA  . ILE A 193 ? 0.7676 0.5427 0.6454 0.0125  0.0910  0.0286  408 ILE B CA  
1375 C C   . ILE A 193 ? 0.7295 0.5468 0.6419 0.0050  0.0945  0.0134  408 ILE B C   
1376 O O   . ILE A 193 ? 0.6936 0.5582 0.6440 0.0120  0.0950  0.0038  408 ILE B O   
1377 C CB  . ILE A 193 ? 0.7791 0.5624 0.6663 0.0397  0.0743  0.0398  408 ILE B CB  
1378 C CG1 . ILE A 193 ? 0.7840 0.5300 0.6339 0.0489  0.0671  0.0507  408 ILE B CG1 
1379 C CG2 . ILE A 193 ? 0.7813 0.5825 0.6824 0.0491  0.0657  0.0368  408 ILE B CG2 
1380 C CD1 . ILE A 193 ? 0.7747 0.5465 0.6378 0.0650  0.0565  0.0583  408 ILE B CD1 
1381 N N   . LEU A 194 ? 0.7485 0.5469 0.6457 -0.0068 0.0941  0.0089  409 LEU B N   
1382 C CA  . LEU A 194 ? 0.7447 0.5878 0.6731 -0.0160 0.0958  -0.0077 409 LEU B CA  
1383 C C   . LEU A 194 ? 0.7666 0.6027 0.6928 -0.0001 0.0813  -0.0063 409 LEU B C   
1384 O O   . LEU A 194 ? 0.8333 0.6154 0.7216 -0.0023 0.0773  -0.0044 409 LEU B O   
1385 C CB  . LEU A 194 ? 0.7512 0.5884 0.6632 -0.0575 0.1126  -0.0217 409 LEU B CB  
1386 C CG  . LEU A 194 ? 0.7301 0.6326 0.6809 -0.0725 0.1164  -0.0448 409 LEU B CG  
1387 C CD1 . LEU A 194 ? 0.6460 0.6287 0.6483 -0.0605 0.1201  -0.0594 409 LEU B CD1 
1388 C CD2 . LEU A 194 ? 0.8105 0.6903 0.7299 -0.1231 0.1312  -0.0565 409 LEU B CD2 
1389 N N   . GLN A 195 ? 0.7036 0.5908 0.6652 0.0177  0.0716  -0.0082 410 GLN B N   
1390 C CA  . GLN A 195 ? 0.6949 0.5916 0.6561 0.0299  0.0597  -0.0104 410 GLN B CA  
1391 C C   . GLN A 195 ? 0.6921 0.6270 0.6739 0.0149  0.0607  -0.0299 410 GLN B C   
1392 O O   . GLN A 195 ? 0.6947 0.6800 0.7100 0.0136  0.0615  -0.0373 410 GLN B O   
1393 C CB  . GLN A 195 ? 0.6537 0.5809 0.6294 0.0538  0.0472  0.0037  410 GLN B CB  
1394 C CG  . GLN A 195 ? 0.7230 0.6232 0.6769 0.0658  0.0444  0.0178  410 GLN B CG  
1395 C CD  . GLN A 195 ? 0.7185 0.6527 0.6778 0.0790  0.0337  0.0288  410 GLN B CD  
1396 O OE1 . GLN A 195 ? 0.6915 0.6480 0.6650 0.0793  0.0279  0.0393  410 GLN B OE1 
1397 N NE2 . GLN A 195 ? 0.7122 0.6493 0.6558 0.0899  0.0297  0.0259  410 GLN B NE2 
1398 N N   . VAL A 196 ? 0.7283 0.6408 0.6899 0.0060  0.0584  -0.0416 411 VAL B N   
1399 C CA  . VAL A 196 ? 0.7110 0.6604 0.6888 -0.0124 0.0584  -0.0632 411 VAL B CA  
1400 C C   . VAL A 196 ? 0.7026 0.6643 0.6759 0.0055  0.0445  -0.0688 411 VAL B C   
1401 O O   . VAL A 196 ? 0.7256 0.6372 0.6657 0.0122  0.0407  -0.0722 411 VAL B O   
1402 C CB  . VAL A 196 ? 0.7214 0.6275 0.6721 -0.0531 0.0710  -0.0777 411 VAL B CB  
1403 C CG1 . VAL A 196 ? 0.7097 0.6641 0.6802 -0.0780 0.0712  -0.1035 411 VAL B CG1 
1404 C CG2 . VAL A 196 ? 0.6925 0.5974 0.6442 -0.0734 0.0871  -0.0724 411 VAL B CG2 
1405 N N   . VAL A 197 ? 0.7324 0.7608 0.7356 0.0166  0.0350  -0.0706 412 VAL B N   
1406 C CA  . VAL A 197 ? 0.6866 0.7411 0.6846 0.0301  0.0228  -0.0767 412 VAL B CA  
1407 C C   . VAL A 197 ? 0.7129 0.7994 0.7213 0.0099  0.0208  -0.1034 412 VAL B C   
1408 O O   . VAL A 197 ? 0.6666 0.8086 0.7066 0.0033  0.0184  -0.1096 412 VAL B O   
1409 C CB  . VAL A 197 ? 0.6409 0.7419 0.6520 0.0521  0.0108  -0.0565 412 VAL B CB  
1410 C CG1 . VAL A 197 ? 0.6564 0.7886 0.6541 0.0613  0.0011  -0.0627 412 VAL B CG1 
1411 C CG2 . VAL A 197 ? 0.6588 0.7313 0.6614 0.0638  0.0136  -0.0320 412 VAL B CG2 
1412 N N   . THR A 198 ? 0.7286 0.7837 0.7107 0.0026  0.0194  -0.1226 413 THR B N   
1413 C CA  . THR A 198 ? 0.7499 0.8262 0.7356 -0.0230 0.0178  -0.1516 413 THR B CA  
1414 C C   . THR A 198 ? 0.7622 0.8605 0.7356 -0.0074 0.0053  -0.1667 413 THR B C   
1415 O O   . THR A 198 ? 0.7698 0.8424 0.7206 0.0172  0.0018  -0.1626 413 THR B O   
1416 C CB  . THR A 198 ? 0.7931 0.7932 0.7478 -0.0582 0.0283  -0.1662 413 THR B CB  
1417 O OG1 . THR A 198 ? 0.8745 0.8065 0.7864 -0.0472 0.0208  -0.1782 413 THR B OG1 
1418 C CG2 . THR A 198 ? 0.7606 0.7130 0.7055 -0.0640 0.0406  -0.1447 413 THR B CG2 
1419 N N   . ASN A 199 ? 0.8284 0.9847 0.8181 -0.0213 -0.0015 -0.1877 414 ASN B N   
1420 C CA  . ASN A 199 ? 0.8355 1.0171 0.8107 -0.0128 -0.0126 -0.2089 414 ASN B CA  
1421 C C   . ASN A 199 ? 0.9042 1.0045 0.8407 -0.0262 -0.0103 -0.2368 414 ASN B C   
1422 O O   . ASN A 199 ? 0.9597 1.0290 0.8895 -0.0637 -0.0057 -0.2559 414 ASN B O   
1423 C CB  . ASN A 199 ? 0.8384 1.1049 0.8411 -0.0260 -0.0224 -0.2244 414 ASN B CB  
1424 C CG  . ASN A 199 ? 0.8436 1.1500 0.8311 -0.0168 -0.0349 -0.2446 414 ASN B CG  
1425 O OD1 . ASN A 199 ? 0.8805 1.1419 0.8368 -0.0147 -0.0341 -0.2662 414 ASN B OD1 
1426 N ND2 . ASN A 199 ? 0.7983 1.1890 0.8043 -0.0086 -0.0490 -0.2396 414 ASN B ND2 
1427 N N   . ARG A 200 ? 0.8692 0.9336 0.7773 0.0035  -0.0147 -0.2410 415 ARG B N   
1428 C CA  . ARG A 200 ? 0.9645 0.9297 0.8284 0.0010  -0.0174 -0.2660 415 ARG B CA  
1429 C C   . ARG A 200 ? 1.0083 0.9692 0.8576 -0.0243 -0.0244 -0.3056 415 ARG B C   
1430 O O   . ARG A 200 ? 1.0803 0.9451 0.8912 -0.0475 -0.0261 -0.3249 415 ARG B O   
1431 C CB  . ARG A 200 ? 0.9217 0.8656 0.7635 0.0474  -0.0243 -0.2702 415 ARG B CB  
1432 C CG  . ARG A 200 ? 0.9419 0.7729 0.7320 0.0572  -0.0344 -0.3002 415 ARG B CG  
1433 C CD  . ARG A 200 ? 1.0909 0.9541 0.8692 0.0875  -0.0462 -0.3395 415 ARG B CD  
1434 N NE  . ARG A 200 ? 1.1801 0.9458 0.9113 0.1205  -0.0610 -0.3694 415 ARG B NE  
1435 C CZ  . ARG A 200 ? 1.1797 0.9818 0.9049 0.1674  -0.0707 -0.4004 415 ARG B CZ  
1436 N NH1 . ARG A 200 ? 1.0781 1.0116 0.8374 0.1803  -0.0642 -0.4006 415 ARG B NH1 
1437 N NH2 . ARG A 200 ? 1.2797 0.9837 0.9596 0.2023  -0.0887 -0.4333 415 ARG B NH2 
1438 N N   . ASP A 201 ? 0.9538 1.0104 0.8262 -0.0226 -0.0303 -0.3181 416 ASP B N   
1439 C CA  . ASP A 201 ? 1.0487 1.1047 0.9068 -0.0486 -0.0377 -0.3593 416 ASP B CA  
1440 C C   . ASP A 201 ? 1.0639 1.1371 0.9425 -0.1012 -0.0317 -0.3633 416 ASP B C   
1441 O O   . ASP A 201 ? 1.1416 1.1582 0.9937 -0.1405 -0.0324 -0.3927 416 ASP B O   
1442 C CB  . ASP A 201 ? 1.0162 1.1707 0.8846 -0.0277 -0.0479 -0.3752 416 ASP B CB  
1443 C CG  . ASP A 201 ? 0.9968 1.1544 0.8466 0.0197  -0.0508 -0.3766 416 ASP B CG  
1444 O OD1 . ASP A 201 ? 1.0130 1.0822 0.8303 0.0375  -0.0528 -0.3935 416 ASP B OD1 
1445 O OD2 . ASP A 201 ? 0.9665 1.2163 0.8311 0.0385  -0.0524 -0.3624 416 ASP B OD2 
1446 N N   . THR A 202 ? 1.0250 1.1743 0.9481 -0.1034 -0.0263 -0.3364 417 THR B N   
1447 C CA  . THR A 202 ? 1.0107 1.2124 0.9653 -0.1466 -0.0215 -0.3459 417 THR B CA  
1448 C C   . THR A 202 ? 1.0596 1.2021 1.0100 -0.1801 -0.0044 -0.3331 417 THR B C   
1449 O O   . THR A 202 ? 1.0906 1.2450 1.0465 -0.2323 0.0029  -0.3537 417 THR B O   
1450 C CB  . THR A 202 ? 0.9394 1.2620 0.9444 -0.1246 -0.0295 -0.3296 417 THR B CB  
1451 O OG1 . THR A 202 ? 0.9648 1.3581 0.9722 -0.1172 -0.0460 -0.3516 417 THR B OG1 
1452 C CG2 . THR A 202 ? 0.9649 1.3411 1.0100 -0.1554 -0.0221 -0.3329 417 THR B CG2 
1453 N N   . GLN A 203 ? 1.0977 1.1840 1.0369 -0.1557 0.0026  -0.3011 418 GLN B N   
1454 C CA  . GLN A 203 ? 1.0924 1.1333 1.0272 -0.1818 0.0189  -0.2835 418 GLN B CA  
1455 C C   . GLN A 203 ? 1.0384 1.1818 1.0312 -0.1779 0.0249  -0.2698 418 GLN B C   
1456 O O   . GLN A 203 ? 1.0540 1.1801 1.0502 -0.1938 0.0394  -0.2556 418 GLN B O   
1457 C CB  . GLN A 203 ? 1.1846 1.1606 1.0839 -0.2472 0.0283  -0.3059 418 GLN B CB  
1458 C CG  . GLN A 203 ? 1.2705 1.1318 1.1056 -0.2538 0.0174  -0.3264 418 GLN B CG  
1459 C CD  . GLN A 203 ? 1.3299 1.0911 1.1237 -0.2057 0.0101  -0.3060 418 GLN B CD  
1460 O OE1 . GLN A 203 ? 1.2890 1.0970 1.1077 -0.1514 0.0048  -0.2903 418 GLN B OE1 
1461 N NE2 . GLN A 203 ? 1.4248 1.0465 1.1509 -0.2268 0.0078  -0.3071 418 GLN B NE2 
1462 N N   . GLU A 204 ? 0.9289 1.1763 0.9633 -0.1554 0.0120  -0.2752 419 GLU B N   
1463 C CA  . GLU A 204 ? 0.8439 1.1772 0.9287 -0.1380 0.0109  -0.2624 419 GLU B CA  
1464 C C   . GLU A 204 ? 0.7966 1.0842 0.8752 -0.1039 0.0152  -0.2252 419 GLU B C   
1465 O O   . GLU A 204 ? 0.7849 1.0368 0.8417 -0.0710 0.0075  -0.2058 419 GLU B O   
1466 C CB  . GLU A 204 ? 0.8138 1.2444 0.9290 -0.1086 -0.0114 -0.2681 419 GLU B CB  
1467 C CG  . GLU A 204 ? 0.8246 1.3506 0.9731 -0.1384 -0.0172 -0.3057 419 GLU B CG  
1468 C CD  . GLU A 204 ? 0.8706 1.4648 1.0243 -0.1147 -0.0425 -0.3156 419 GLU B CD  
1469 O OE1 . GLU A 204 ? 0.8587 1.4157 0.9798 -0.0874 -0.0513 -0.2990 419 GLU B OE1 
1470 O OE2 . GLU A 204 ? 0.8075 1.5005 0.9970 -0.1256 -0.0535 -0.3426 419 GLU B OE2 
1471 N N   . LEU A 205 ? 0.8015 1.0963 0.8989 -0.1149 0.0286  -0.2186 420 LEU B N   
1472 C CA  . LEU A 205 ? 0.7295 0.9986 0.8286 -0.0813 0.0299  -0.1869 420 LEU B CA  
1473 C C   . LEU A 205 ? 0.6586 0.9893 0.7851 -0.0370 0.0089  -0.1736 420 LEU B C   
1474 O O   . LEU A 205 ? 0.6287 1.0429 0.7916 -0.0316 -0.0026 -0.1899 420 LEU B O   
1475 C CB  . LEU A 205 ? 0.7105 0.9864 0.8249 -0.1034 0.0484  -0.1888 420 LEU B CB  
1476 C CG  . LEU A 205 ? 0.6575 0.8916 0.7654 -0.0783 0.0535  -0.1601 420 LEU B CG  
1477 C CD1 . LEU A 205 ? 0.6966 0.8790 0.7792 -0.1160 0.0766  -0.1598 420 LEU B CD1 
1478 C CD2 . LEU A 205 ? 0.6252 0.9345 0.7795 -0.0454 0.0430  -0.1595 420 LEU B CD2 
1479 N N   . LEU A 206 ? 0.6672 0.9565 0.7721 -0.0065 0.0019  -0.1444 421 LEU B N   
1480 C CA  . LEU A 206 ? 0.6309 0.9569 0.7454 0.0293  -0.0190 -0.1249 421 LEU B CA  
1481 C C   . LEU A 206 ? 0.6422 0.9483 0.7648 0.0510  -0.0200 -0.1011 421 LEU B C   
1482 O O   . LEU A 206 ? 0.6292 0.9685 0.7671 0.0775  -0.0395 -0.0926 421 LEU B O   
1483 C CB  . LEU A 206 ? 0.6339 0.9400 0.7142 0.0415  -0.0274 -0.1101 421 LEU B CB  
1484 C CG  . LEU A 206 ? 0.6397 0.9673 0.7065 0.0285  -0.0311 -0.1347 421 LEU B CG  
1485 C CD1 . LEU A 206 ? 0.6330 0.9396 0.6654 0.0420  -0.0333 -0.1221 421 LEU B CD1 
1486 C CD2 . LEU A 206 ? 0.6181 1.0255 0.7060 0.0318  -0.0499 -0.1490 421 LEU B CD2 
1487 N N   . LEU A 207 ? 0.6134 0.8614 0.7221 0.0420  -0.0023 -0.0915 422 LEU B N   
1488 C CA  . LEU A 207 ? 0.5878 0.8122 0.7004 0.0600  -0.0025 -0.0717 422 LEU B CA  
1489 C C   . LEU A 207 ? 0.6261 0.8043 0.7285 0.0389  0.0206  -0.0740 422 LEU B C   
1490 O O   . LEU A 207 ? 0.6524 0.7832 0.7252 0.0234  0.0302  -0.0726 422 LEU B O   
1491 C CB  . LEU A 207 ? 0.6136 0.8056 0.6991 0.0800  -0.0147 -0.0402 422 LEU B CB  
1492 C CG  . LEU A 207 ? 0.6136 0.7930 0.7021 0.1037  -0.0287 -0.0200 422 LEU B CG  
1493 C CD1 . LEU A 207 ? 0.5989 0.8269 0.7126 0.1261  -0.0510 -0.0300 422 LEU B CD1 
1494 C CD2 . LEU A 207 ? 0.6551 0.8029 0.7085 0.1082  -0.0377 0.0104  422 LEU B CD2 
1495 N N   . CYS A 208 ? 0.6074 0.7989 0.7307 0.0407  0.0274  -0.0794 423 CYS B N   
1496 C CA  . CYS A 208 ? 0.5906 0.7401 0.6988 0.0212  0.0483  -0.0780 423 CYS B CA  
1497 C C   . CYS A 208 ? 0.5566 0.6926 0.6703 0.0458  0.0443  -0.0640 423 CYS B C   
1498 O O   . CYS A 208 ? 0.5468 0.7266 0.6912 0.0672  0.0337  -0.0741 423 CYS B O   
1499 C CB  . CYS A 208 ? 0.6143 0.8026 0.7386 -0.0136 0.0664  -0.1064 423 CYS B CB  
1500 S SG  . CYS A 208 ? 0.6067 0.7378 0.6980 -0.0438 0.0919  -0.1004 423 CYS B SG  
1501 N N   . THR A 209 ? 0.5623 0.6377 0.6455 0.0449  0.0503  -0.0439 424 THR B N   
1502 C CA  . THR A 209 ? 0.6095 0.6625 0.6908 0.0651  0.0447  -0.0293 424 THR B CA  
1503 C C   . THR A 209 ? 0.6105 0.6265 0.6711 0.0479  0.0635  -0.0279 424 THR B C   
1504 O O   . THR A 209 ? 0.6181 0.5893 0.6462 0.0366  0.0689  -0.0160 424 THR B O   
1505 C CB  . THR A 209 ? 0.6240 0.6481 0.6849 0.0809  0.0285  -0.0028 424 THR B CB  
1506 O OG1 . THR A 209 ? 0.5899 0.6466 0.6623 0.0950  0.0098  -0.0017 424 THR B OG1 
1507 C CG2 . THR A 209 ? 0.6543 0.6464 0.7068 0.0933  0.0229  0.0118  424 THR B CG2 
1508 N N   . ALA A 210 ? 0.5635 0.6010 0.6410 0.0486  0.0716  -0.0424 425 ALA B N   
1509 C CA  . ALA A 210 ? 0.6329 0.6387 0.6874 0.0345  0.0874  -0.0398 425 ALA B CA  
1510 C C   . ALA A 210 ? 0.6468 0.6216 0.6944 0.0582  0.0759  -0.0250 425 ALA B C   
1511 O O   . ALA A 210 ? 0.5886 0.5772 0.6573 0.0839  0.0600  -0.0284 425 ALA B O   
1512 C CB  . ALA A 210 ? 0.6071 0.6629 0.6806 0.0171  0.1060  -0.0680 425 ALA B CB  
1513 N N   . TYR A 211 ? 0.6513 0.5799 0.6652 0.0491  0.0815  -0.0096 426 TYR B N   
1514 C CA  . TYR A 211 ? 0.6370 0.5355 0.6393 0.0629  0.0720  0.0037  426 TYR B CA  
1515 C C   . TYR A 211 ? 0.6514 0.5388 0.6383 0.0526  0.0863  -0.0046 426 TYR B C   
1516 O O   . TYR A 211 ? 0.6610 0.5303 0.6193 0.0320  0.0993  -0.0009 426 TYR B O   
1517 C CB  . TYR A 211 ? 0.6156 0.4846 0.5934 0.0629  0.0636  0.0267  426 TYR B CB  
1518 C CG  . TYR A 211 ? 0.6652 0.5501 0.6525 0.0708  0.0506  0.0348  426 TYR B CG  
1519 C CD1 . TYR A 211 ? 0.6684 0.5539 0.6608 0.0821  0.0340  0.0461  426 TYR B CD1 
1520 C CD2 . TYR A 211 ? 0.6683 0.5617 0.6519 0.0644  0.0538  0.0314  426 TYR B CD2 
1521 C CE1 . TYR A 211 ? 0.6678 0.5703 0.6612 0.0853  0.0225  0.0556  426 TYR B CE1 
1522 C CE2 . TYR A 211 ? 0.6687 0.5830 0.6586 0.0713  0.0426  0.0363  426 TYR B CE2 
1523 C CZ  . TYR A 211 ? 0.6959 0.6190 0.6904 0.0808  0.0278  0.0492  426 TYR B CZ  
1524 O OH  . TYR A 211 ? 0.6781 0.6248 0.6717 0.0835  0.0173  0.0557  426 TYR B OH  
1525 N N   . VAL A 212 ? 0.6643 0.5559 0.6636 0.0676  0.0816  -0.0157 427 VAL B N   
1526 C CA  . VAL A 212 ? 0.6816 0.5619 0.6628 0.0603  0.0924  -0.0238 427 VAL B CA  
1527 C C   . VAL A 212 ? 0.6679 0.5080 0.6346 0.0715  0.0762  -0.0100 427 VAL B C   
1528 O O   . VAL A 212 ? 0.7130 0.5385 0.6870 0.0842  0.0578  0.0016  427 VAL B O   
1529 C CB  . VAL A 212 ? 0.5970 0.5239 0.6034 0.0660  0.1033  -0.0582 427 VAL B CB  
1530 C CG1 . VAL A 212 ? 0.5976 0.5761 0.6188 0.0456  0.1211  -0.0735 427 VAL B CG1 
1531 C CG2 . VAL A 212 ? 0.6003 0.5338 0.6374 0.1022  0.0824  -0.0724 427 VAL B CG2 
1532 N N   . PHE A 213 ? 0.7147 0.5373 0.6564 0.0624  0.0829  -0.0112 428 PHE B N   
1533 C CA  . PHE A 213 ? 0.6914 0.4798 0.6136 0.0627  0.0693  0.0040  428 PHE B CA  
1534 C C   . PHE A 213 ? 0.7430 0.5182 0.6539 0.0639  0.0701  -0.0127 428 PHE B C   
1535 O O   . PHE A 213 ? 0.7555 0.5498 0.6616 0.0590  0.0861  -0.0321 428 PHE B O   
1536 C CB  . PHE A 213 ? 0.7021 0.4818 0.5973 0.0500  0.0707  0.0243  428 PHE B CB  
1537 C CG  . PHE A 213 ? 0.7373 0.5254 0.6406 0.0525  0.0657  0.0384  428 PHE B CG  
1538 C CD1 . PHE A 213 ? 0.7217 0.5180 0.6250 0.0474  0.0761  0.0353  428 PHE B CD1 
1539 C CD2 . PHE A 213 ? 0.6849 0.4743 0.5922 0.0558  0.0511  0.0528  428 PHE B CD2 
1540 C CE1 . PHE A 213 ? 0.7412 0.5432 0.6499 0.0512  0.0702  0.0442  428 PHE B CE1 
1541 C CE2 . PHE A 213 ? 0.6915 0.4965 0.6053 0.0588  0.0475  0.0614  428 PHE B CE2 
1542 C CZ  . PHE A 213 ? 0.6721 0.4819 0.5875 0.0593  0.0562  0.0559  428 PHE B CZ  
1543 N N   . GLU A 214 ? 0.7273 0.4701 0.6310 0.0667  0.0526  -0.0059 429 GLU B N   
1544 C CA  . GLU A 214 ? 0.7325 0.4514 0.6167 0.0623  0.0486  -0.0168 429 GLU B CA  
1545 C C   . GLU A 214 ? 0.7892 0.4846 0.6558 0.0469  0.0333  0.0054  429 GLU B C   
1546 O O   . GLU A 214 ? 0.7649 0.4671 0.6367 0.0423  0.0270  0.0264  429 GLU B O   
1547 C CB  . GLU A 214 ? 0.7638 0.4617 0.6595 0.0833  0.0393  -0.0434 429 GLU B CB  
1548 C CG  . GLU A 214 ? 0.7750 0.5152 0.6908 0.0978  0.0558  -0.0752 429 GLU B CG  
1549 C CD  . GLU A 214 ? 0.8257 0.5477 0.7548 0.1284  0.0417  -0.1071 429 GLU B CD  
1550 O OE1 . GLU A 214 ? 0.8208 0.4895 0.7279 0.1301  0.0263  -0.1122 429 GLU B OE1 
1551 O OE2 . GLU A 214 ? 0.9047 0.6646 0.8656 0.1524  0.0435  -0.1293 429 GLU B OE2 
1552 N N   . VAL A 215 ? 0.7989 0.4737 0.6447 0.0358  0.0279  -0.0021 430 VAL B N   
1553 C CA  . VAL A 215 ? 0.8295 0.4908 0.6597 0.0140  0.0138  0.0147  430 VAL B CA  
1554 C C   . VAL A 215 ? 0.8889 0.4906 0.7090 0.0112  -0.0044 0.0095  430 VAL B C   
1555 O O   . VAL A 215 ? 0.9406 0.5109 0.7642 0.0325  -0.0080 -0.0124 430 VAL B O   
1556 C CB  . VAL A 215 ? 0.8241 0.5053 0.6334 -0.0022 0.0164  0.0115  430 VAL B CB  
1557 C CG1 . VAL A 215 ? 0.8648 0.5895 0.6740 0.0032  0.0264  0.0227  430 VAL B CG1 
1558 C CG2 . VAL A 215 ? 0.8921 0.5550 0.6881 0.0019  0.0207  -0.0154 430 VAL B CG2 
1559 N N   . SER A 216 ? 0.8967 0.8037 0.8086 0.0721  -0.1580 0.0747  431 SER B N   
1560 C CA  . SER A 216 ? 0.9916 0.8857 0.9207 0.0514  -0.1510 0.0754  431 SER B CA  
1561 C C   . SER A 216 ? 1.0901 1.0005 1.0232 0.0211  -0.1680 0.0729  431 SER B C   
1562 O O   . SER A 216 ? 1.0830 1.0473 1.0306 0.0216  -0.1849 0.0780  431 SER B O   
1563 C CB  . SER A 216 ? 0.8857 0.8101 0.8463 0.0591  -0.1416 0.0944  431 SER B CB  
1564 O OG  . SER A 216 ? 0.9641 0.8786 0.9379 0.0309  -0.1430 0.1053  431 SER B OG  
1565 N N   . THR A 217 ? 1.1987 1.0628 1.1231 -0.0038 -0.1660 0.0607  432 THR B N   
1566 C CA  . THR A 217 ? 1.2792 1.1508 1.2072 -0.0405 -0.1815 0.0548  432 THR B CA  
1567 C C   . THR A 217 ? 1.2714 1.1927 1.2409 -0.0577 -0.1831 0.0781  432 THR B C   
1568 O O   . THR A 217 ? 1.2787 1.1662 1.2574 -0.0729 -0.1752 0.0904  432 THR B O   
1569 C CB  . THR A 217 ? 1.3473 1.1447 1.2575 -0.0601 -0.1766 0.0302  432 THR B CB  
1570 O OG1 . THR A 217 ? 1.3484 1.1116 1.2851 -0.0697 -0.1725 0.0444  432 THR B OG1 
1571 C CG2 . THR A 217 ? 1.3165 1.0738 1.1996 -0.0361 -0.1601 0.0072  432 THR B CG2 
1572 N N   . SER A 218 ? 1.3366 1.3400 1.3312 -0.0578 -0.1953 0.0835  433 SER B N   
1573 C CA  . SER A 218 ? 1.2886 1.3666 1.3255 -0.0602 -0.1868 0.1011  433 SER B CA  
1574 C C   . SER A 218 ? 1.3327 1.4206 1.3870 -0.1105 -0.1822 0.1143  433 SER B C   
1575 O O   . SER A 218 ? 1.3241 1.4953 1.4131 -0.1251 -0.1742 0.1249  433 SER B O   
1576 C CB  . SER A 218 ? 1.2703 1.4418 1.3423 -0.0414 -0.2024 0.0938  433 SER B CB  
1577 O OG  . SER A 218 ? 1.2466 1.4013 1.3020 0.0052  -0.2061 0.0897  433 SER B OG  
1578 N N   . GLU A 219 ? 1.2095 1.2136 1.2403 -0.1399 -0.1859 0.1121  434 GLU B N   
1579 C CA  . GLU A 219 ? 1.0866 1.0605 1.1196 -0.1800 -0.1793 0.1363  434 GLU B CA  
1580 C C   . GLU A 219 ? 1.0401 0.9862 1.0611 -0.1533 -0.1651 0.1595  434 GLU B C   
1581 O O   . GLU A 219 ? 1.0019 0.9868 1.0283 -0.1748 -0.1552 0.1869  434 GLU B O   
1582 C CB  . GLU A 219 ? 1.1525 1.0242 1.1651 -0.2114 -0.1910 0.1260  434 GLU B CB  
1583 C CG  . GLU A 219 ? 1.2419 1.1188 1.2499 -0.2279 -0.2069 0.0922  434 GLU B CG  
1584 C CD  . GLU A 219 ? 1.2502 1.0132 1.2333 -0.2460 -0.2143 0.0694  434 GLU B CD  
1585 O OE1 . GLU A 219 ? 1.2996 1.0105 1.2602 -0.2113 -0.2101 0.0434  434 GLU B OE1 
1586 O OE2 . GLU A 219 ? 1.2333 0.9601 1.2210 -0.2967 -0.2231 0.0744  434 GLU B OE2 
1587 N N   . ARG A 220 ? 1.1025 0.9885 1.1052 -0.1106 -0.1638 0.1474  435 ARG B N   
1588 C CA  . ARG A 220 ? 1.0310 0.9174 1.0283 -0.0765 -0.1529 0.1623  435 ARG B CA  
1589 C C   . ARG A 220 ? 0.9944 0.9774 1.0075 -0.0530 -0.1434 0.1573  435 ARG B C   
1590 O O   . ARG A 220 ? 1.0484 1.0606 1.0679 -0.0364 -0.1494 0.1357  435 ARG B O   
1591 C CB  . ARG A 220 ? 0.9838 0.7985 0.9676 -0.0389 -0.1530 0.1434  435 ARG B CB  
1592 C CG  . ARG A 220 ? 1.0238 0.7536 1.0015 -0.0512 -0.1627 0.1232  435 ARG B CG  
1593 C CD  . ARG A 220 ? 0.9964 0.6749 0.9727 -0.0121 -0.1578 0.1000  435 ARG B CD  
1594 N NE  . ARG A 220 ? 1.0133 0.6750 0.9985 0.0101  -0.1599 0.1245  435 ARG B NE  
1595 C CZ  . ARG A 220 ? 1.0149 0.6329 1.0128 0.0430  -0.1613 0.1079  435 ARG B CZ  
1596 N NH1 . ARG A 220 ? 1.0219 0.6135 1.0256 0.0563  -0.1541 0.0630  435 ARG B NH1 
1597 N NH2 . ARG A 220 ? 0.9778 0.5862 0.9838 0.0615  -0.1703 0.1345  435 ARG B NH2 
1598 N N   . GLY A 221 ? 0.8250 0.8551 0.8420 -0.0519 -0.1314 0.1761  436 GLY B N   
1599 C CA  . GLY A 221 ? 0.7550 0.8675 0.7903 -0.0223 -0.1219 0.1630  436 GLY B CA  
1600 C C   . GLY A 221 ? 0.6894 0.7641 0.7083 0.0228  -0.1193 0.1531  436 GLY B C   
1601 O O   . GLY A 221 ? 0.7624 0.7611 0.7623 0.0332  -0.1242 0.1497  436 GLY B O   
1602 N N   . ALA A 222 ? 0.6946 0.8283 0.7247 0.0481  -0.1101 0.1440  437 ALA B N   
1603 C CA  . ALA A 222 ? 0.6378 0.7411 0.6522 0.0837  -0.1065 0.1351  437 ALA B CA  
1604 C C   . ALA A 222 ? 0.6121 0.6624 0.6041 0.0786  -0.1050 0.1536  437 ALA B C   
1605 O O   . ALA A 222 ? 0.7045 0.7610 0.6890 0.0520  -0.1042 0.1784  437 ALA B O   
1606 C CB  . ALA A 222 ? 0.6051 0.7796 0.6355 0.1054  -0.0962 0.1214  437 ALA B CB  
1607 N N   . GLN A 223 ? 0.6562 0.6553 0.6381 0.1020  -0.1072 0.1426  438 GLN B N   
1608 C CA  . GLN A 223 ? 0.6565 0.6166 0.6295 0.1079  -0.1104 0.1544  438 GLN B CA  
1609 C C   . GLN A 223 ? 0.6471 0.6088 0.6183 0.1374  -0.1046 0.1342  438 GLN B C   
1610 O O   . GLN A 223 ? 0.6052 0.5762 0.5752 0.1487  -0.0997 0.1143  438 GLN B O   
1611 C CB  . GLN A 223 ? 0.7622 0.6508 0.7381 0.1001  -0.1214 0.1555  438 GLN B CB  
1612 C CG  . GLN A 223 ? 0.8474 0.6953 0.8215 0.0973  -0.1359 0.1811  438 GLN B CG  
1613 C CD  . GLN A 223 ? 0.9573 0.7327 0.9386 0.0829  -0.1501 0.1836  438 GLN B CD  
1614 O OE1 . GLN A 223 ? 1.0075 0.7661 0.9941 0.0772  -0.1455 0.1580  438 GLN B OE1 
1615 N NE2 . GLN A 223 ? 0.9507 0.6771 0.9278 0.0750  -0.1706 0.2144  438 GLN B NE2 
1616 N N   . HIS A 224 ? 0.6378 0.5876 0.6078 0.1478  -0.1089 0.1407  439 HIS B N   
1617 C CA  . HIS A 224 ? 0.6628 0.6211 0.6339 0.1693  -0.1032 0.1199  439 HIS B CA  
1618 C C   . HIS A 224 ? 0.6425 0.5796 0.6281 0.1775  -0.1131 0.1220  439 HIS B C   
1619 O O   . HIS A 224 ? 0.7053 0.6167 0.6957 0.1726  -0.1283 0.1446  439 HIS B O   
1620 C CB  . HIS A 224 ? 0.6397 0.6518 0.6008 0.1737  -0.0959 0.1169  439 HIS B CB  
1621 C CG  . HIS A 224 ? 0.6323 0.6754 0.5803 0.1619  -0.1010 0.1416  439 HIS B CG  
1622 N ND1 . HIS A 224 ? 0.6344 0.6717 0.5760 0.1677  -0.1135 0.1521  439 HIS B ND1 
1623 C CD2 . HIS A 224 ? 0.6017 0.6840 0.5381 0.1396  -0.0968 0.1600  439 HIS B CD2 
1624 C CE1 . HIS A 224 ? 0.5652 0.6291 0.4818 0.1486  -0.1192 0.1802  439 HIS B CE1 
1625 N NE2 . HIS A 224 ? 0.6000 0.6935 0.5118 0.1284  -0.1058 0.1845  439 HIS B NE2 
1626 N N   . HIS A 225 ? 0.6564 0.6051 0.6528 0.1874  -0.1055 0.0979  440 HIS B N   
1627 C CA  . HIS A 225 ? 0.6708 0.6169 0.6947 0.1975  -0.1134 0.0910  440 HIS B CA  
1628 C C   . HIS A 225 ? 0.6659 0.6465 0.6868 0.2049  -0.1074 0.0720  440 HIS B C   
1629 O O   . HIS A 225 ? 0.6577 0.6386 0.6642 0.2061  -0.0937 0.0530  440 HIS B O   
1630 C CB  . HIS A 225 ? 0.7469 0.6607 0.7960 0.2067  -0.1094 0.0673  440 HIS B CB  
1631 C CG  . HIS A 225 ? 0.7553 0.6653 0.8445 0.2205  -0.1211 0.0626  440 HIS B CG  
1632 N ND1 . HIS A 225 ? 0.7177 0.6639 0.8270 0.2305  -0.1285 0.0585  440 HIS B ND1 
1633 C CD2 . HIS A 225 ? 0.8646 0.7387 0.9794 0.2286  -0.1284 0.0566  440 HIS B CD2 
1634 C CE1 . HIS A 225 ? 0.7690 0.7063 0.9162 0.2456  -0.1408 0.0538  440 HIS B CE1 
1635 N NE2 . HIS A 225 ? 0.8728 0.7639 1.0237 0.2458  -0.1400 0.0509  440 HIS B NE2 
1636 N N   . ILE A 226 ? 0.6678 0.6729 0.6979 0.2098  -0.1217 0.0796  441 ILE B N   
1637 C CA  . ILE A 226 ? 0.6508 0.6938 0.6737 0.2164  -0.1212 0.0632  441 ILE B CA  
1638 C C   . ILE A 226 ? 0.6822 0.7426 0.7470 0.2292  -0.1309 0.0447  441 ILE B C   
1639 O O   . ILE A 226 ? 0.6943 0.7511 0.7852 0.2338  -0.1491 0.0598  441 ILE B O   
1640 C CB  . ILE A 226 ? 0.6920 0.7655 0.6828 0.2107  -0.1325 0.0843  441 ILE B CB  
1641 C CG1 . ILE A 226 ? 0.6779 0.7540 0.6373 0.2026  -0.1196 0.0942  441 ILE B CG1 
1642 C CG2 . ILE A 226 ? 0.6979 0.8144 0.6825 0.2191  -0.1364 0.0629  441 ILE B CG2 
1643 C CD1 . ILE A 226 ? 0.6494 0.7700 0.5711 0.1944  -0.1265 0.1155  441 ILE B CD1 
1644 N N   . TYR A 227 ? 0.7060 0.7878 0.7813 0.2334  -0.1194 0.0116  442 TYR B N   
1645 C CA  . TYR A 227 ? 0.7182 0.8370 0.8432 0.2411  -0.1241 -0.0157 442 TYR B CA  
1646 C C   . TYR A 227 ? 0.6600 0.8219 0.7765 0.2301  -0.1259 -0.0301 442 TYR B C   
1647 O O   . TYR A 227 ? 0.6379 0.7877 0.7113 0.2140  -0.1129 -0.0317 442 TYR B O   
1648 C CB  . TYR A 227 ? 0.7281 0.8403 0.8744 0.2303  -0.0960 -0.0495 442 TYR B CB  
1649 C CG  . TYR A 227 ? 0.7293 0.7975 0.8759 0.2350  -0.0895 -0.0446 442 TYR B CG  
1650 C CD1 . TYR A 227 ? 0.7118 0.7359 0.8087 0.2215  -0.0803 -0.0254 442 TYR B CD1 
1651 C CD2 . TYR A 227 ? 0.7580 0.8322 0.9597 0.2541  -0.0943 -0.0646 442 TYR B CD2 
1652 C CE1 . TYR A 227 ? 0.7128 0.7001 0.8079 0.2215  -0.0765 -0.0233 442 TYR B CE1 
1653 C CE2 . TYR A 227 ? 0.7764 0.8070 0.9760 0.2560  -0.0884 -0.0664 442 TYR B CE2 
1654 C CZ  . TYR A 227 ? 0.7636 0.7508 0.9062 0.2367  -0.0795 -0.0444 442 TYR B CZ  
1655 O OH  . TYR A 227 ? 0.8534 0.8000 0.9921 0.2344  -0.0755 -0.0484 442 TYR B OH  
1656 N N   . ARG A 228 ? 0.6493 0.8619 0.8123 0.2402  -0.1441 -0.0450 443 ARG B N   
1657 C CA  . ARG A 228 ? 0.6666 0.9249 0.8332 0.2219  -0.1398 -0.0726 443 ARG B CA  
1658 C C   . ARG A 228 ? 0.6860 0.9495 0.8727 0.1980  -0.1069 -0.1097 443 ARG B C   
1659 O O   . ARG A 228 ? 0.7417 1.0097 0.9676 0.2040  -0.0952 -0.1244 443 ARG B O   
1660 C CB  . ARG A 228 ? 0.6738 0.9964 0.8864 0.2383  -0.1751 -0.0767 443 ARG B CB  
1661 C CG  . ARG A 228 ? 0.7568 1.0675 0.9458 0.2538  -0.2105 -0.0329 443 ARG B CG  
1662 C CD  . ARG A 228 ? 0.8065 1.1681 1.0373 0.2589  -0.2408 -0.0363 443 ARG B CD  
1663 N NE  . ARG A 228 ? 0.8719 1.2020 1.1221 0.2732  -0.2641 0.0002  443 ARG B NE  
1664 C CZ  . ARG A 228 ? 0.8907 1.2138 1.2017 0.2914  -0.2609 -0.0124 443 ARG B CZ  
1665 N NH1 . ARG A 228 ? 0.8191 1.1655 1.1742 0.2928  -0.2322 -0.0597 443 ARG B NH1 
1666 N NH2 . ARG A 228 ? 0.9324 1.2274 1.2577 0.3077  -0.2862 0.0209  443 ARG B NH2 
1667 N N   . LEU A 229 ? 0.6939 0.9544 0.8499 0.1673  -0.0916 -0.1266 444 LEU B N   
1668 C CA  . LEU A 229 ? 0.7217 0.9859 0.8850 0.1320  -0.0620 -0.1576 444 LEU B CA  
1669 C C   . LEU A 229 ? 0.7601 1.1062 0.9775 0.1182  -0.0676 -0.1912 444 LEU B C   
1670 O O   . LEU A 229 ? 0.7797 1.1483 0.9877 0.1131  -0.0857 -0.1945 444 LEU B O   
1671 C CB  . LEU A 229 ? 0.7119 0.9079 0.8074 0.1023  -0.0461 -0.1535 444 LEU B CB  
1672 C CG  . LEU A 229 ? 0.7485 0.8715 0.8000 0.1020  -0.0330 -0.1322 444 LEU B CG  
1673 C CD1 . LEU A 229 ? 0.7653 0.8203 0.7587 0.0777  -0.0275 -0.1296 444 LEU B CD1 
1674 C CD2 . LEU A 229 ? 0.8128 0.9447 0.8832 0.0877  -0.0106 -0.1445 444 LEU B CD2 
1675 N N   . VAL A 230 ? 0.7327 1.1305 1.0077 0.1091  -0.0502 -0.2212 445 VAL B N   
1676 C CA  . VAL A 230 ? 0.7230 1.2220 1.0744 0.1038  -0.0580 -0.2580 445 VAL B CA  
1677 C C   . VAL A 230 ? 0.7724 1.3071 1.1389 0.0504  -0.0169 -0.2975 445 VAL B C   
1678 O O   . VAL A 230 ? 0.8035 1.2706 1.1051 0.0134  0.0132  -0.2898 445 VAL B O   
1679 C CB  . VAL A 230 ? 0.6678 1.2209 1.1012 0.1562  -0.0842 -0.2621 445 VAL B CB  
1680 C CG1 . VAL A 230 ? 0.6573 1.1816 1.0684 0.1965  -0.1307 -0.2188 445 VAL B CG1 
1681 C CG2 . VAL A 230 ? 0.6491 1.1700 1.0908 0.1667  -0.0589 -0.2670 445 VAL B CG2 
1682 N N   . ARG A 231 ? 0.8010 1.4456 1.2526 0.0433  -0.0172 -0.3391 446 ARG B N   
1683 C CA  . ARG A 231 ? 0.8422 1.5410 1.3145 -0.0160 0.0258  -0.3812 446 ARG B CA  
1684 C C   . ARG A 231 ? 0.7716 1.6059 1.3670 0.0010  0.0314  -0.4331 446 ARG B C   
1685 O O   . ARG A 231 ? 0.7701 1.7005 1.4424 0.0127  0.0053  -0.4575 446 ARG B O   
1686 C CB  . ARG A 231 ? 0.8883 1.5861 1.3257 -0.0721 0.0276  -0.3886 446 ARG B CB  
1687 C CG  . ARG A 231 ? 0.9363 1.6152 1.3300 -0.1514 0.0745  -0.4050 446 ARG B CG  
1688 C CD  . ARG A 231 ? 0.9873 1.6373 1.3375 -0.2059 0.0697  -0.4075 446 ARG B CD  
1689 N NE  . ARG A 231 ? 0.9562 1.6766 1.3602 -0.1815 0.0310  -0.4222 446 ARG B NE  
1690 C CZ  . ARG A 231 ? 0.9413 1.7996 1.4530 -0.1611 0.0168  -0.4575 446 ARG B CZ  
1691 N NH1 . ARG A 231 ? 0.8958 1.8454 1.4863 -0.1572 0.0414  -0.4895 446 ARG B NH1 
1692 N NH2 . ARG A 231 ? 0.9378 1.8478 1.4808 -0.1430 -0.0249 -0.4644 446 ARG B NH2 
1693 N N   . GLY B 7   ? 1.0530 0.6512 0.9563 0.1690  0.1892  -0.0037 222 GLY A N   
1694 C CA  . GLY B 7   ? 0.9720 0.5960 0.8428 0.1405  0.1665  -0.0224 222 GLY A CA  
1695 C C   . GLY B 7   ? 0.9207 0.5974 0.7943 0.1359  0.1401  0.0074  222 GLY A C   
1696 O O   . GLY B 7   ? 0.9069 0.6110 0.8049 0.1520  0.1380  0.0372  222 GLY A O   
1697 N N   . LEU B 8   ? 0.9218 0.6140 0.7742 0.1133  0.1204  -0.0020 223 LEU A N   
1698 C CA  . LEU B 8   ? 0.8920 0.6248 0.7473 0.1070  0.0982  0.0186  223 LEU A CA  
1699 C C   . LEU B 8   ? 0.9023 0.6696 0.7494 0.1098  0.0992  0.0155  223 LEU A C   
1700 O O   . LEU B 8   ? 0.8951 0.6740 0.7192 0.0990  0.0942  -0.0002 223 LEU A O   
1701 C CB  . LEU B 8   ? 0.8803 0.6095 0.7219 0.0865  0.0815  0.0124  223 LEU A CB  
1702 C CG  . LEU B 8   ? 0.9313 0.6904 0.7723 0.0772  0.0611  0.0227  223 LEU A CG  
1703 C CD1 . LEU B 8   ? 0.9178 0.6998 0.7813 0.0841  0.0531  0.0467  223 LEU A CD1 
1704 C CD2 . LEU B 8   ? 0.8518 0.6030 0.6835 0.0627  0.0509  0.0175  223 LEU A CD2 
1705 N N   . GLY B 9   ? 0.8700 0.6609 0.7387 0.1255  0.1069  0.0346  224 GLY A N   
1706 C CA  . GLY B 9   ? 0.8695 0.6972 0.7345 0.1280  0.1106  0.0394  224 GLY A CA  
1707 C C   . GLY B 9   ? 0.8444 0.6984 0.7387 0.1471  0.1254  0.0596  224 GLY A C   
1708 O O   . GLY B 9   ? 0.8638 0.7081 0.7815 0.1617  0.1334  0.0687  224 GLY A O   
1709 N N   . THR B 10  ? 0.8086 0.7014 0.7050 0.1484  0.1304  0.0714  225 THR A N   
1710 C CA  . THR B 10  ? 0.8352 0.7644 0.7623 0.1654  0.1473  0.0927  225 THR A CA  
1711 C C   . THR B 10  ? 0.8485 0.7925 0.7480 0.1808  0.1739  0.0769  225 THR A C   
1712 O O   . THR B 10  ? 0.8583 0.7844 0.7143 0.1768  0.1769  0.0463  225 THR A O   
1713 C CB  . THR B 10  ? 0.8001 0.7693 0.7608 0.1527  0.1354  0.1241  225 THR A CB  
1714 O OG1 . THR B 10  ? 0.8111 0.7843 0.7485 0.1395  0.1298  0.1240  225 THR A OG1 
1715 C CG2 . THR B 10  ? 0.7657 0.7288 0.7540 0.1375  0.1102  0.1340  225 THR A CG2 
1716 N N   . ALA B 11  ? 0.8297 0.8149 0.7553 0.1975  0.1932  0.0973  226 ALA A N   
1717 C CA  . ALA B 11  ? 0.8381 0.8536 0.7365 0.2122  0.2198  0.0879  226 ALA A CA  
1718 C C   . ALA B 11  ? 0.8250 0.8673 0.6914 0.1972  0.2113  0.0944  226 ALA A C   
1719 O O   . ALA B 11  ? 0.8754 0.9446 0.7028 0.2069  0.2293  0.0808  226 ALA A O   
1720 C CB  . ALA B 11  ? 0.8747 0.9401 0.8162 0.2316  0.2419  0.1176  226 ALA A CB  
1721 N N   . ARG B 12  ? 0.8091 0.8481 0.6916 0.1760  0.1860  0.1159  227 ARG A N   
1722 C CA  . ARG B 12  ? 0.8068 0.8721 0.6717 0.1662  0.1803  0.1337  227 ARG A CA  
1723 C C   . ARG B 12  ? 0.8135 0.8518 0.6438 0.1529  0.1593  0.1129  227 ARG A C   
1724 O O   . ARG B 12  ? 0.7899 0.8558 0.5943 0.1516  0.1576  0.1223  227 ARG A O   
1725 C CB  . ARG B 12  ? 0.7779 0.8587 0.6953 0.1529  0.1717  0.1762  227 ARG A CB  
1726 C CG  . ARG B 12  ? 0.7861 0.9113 0.7455 0.1617  0.1924  0.2059  227 ARG A CG  
1727 C CD  . ARG B 12  ? 0.7746 0.9111 0.7869 0.1409  0.1829  0.2437  227 ARG A CD  
1728 N NE  . ARG B 12  ? 0.7450 0.9094 0.7503 0.1400  0.1945  0.2753  227 ARG A NE  
1729 C CZ  . ARG B 12  ? 0.7637 0.9298 0.8145 0.1217  0.1910  0.3106  227 ARG A CZ  
1730 N NH1 . ARG B 12  ? 0.8019 0.9439 0.9036 0.0993  0.1735  0.3103  227 ARG A NH1 
1731 N NH2 . ARG B 12  ? 0.7100 0.9035 0.7558 0.1253  0.2059  0.3470  227 ARG A NH2 
1732 N N   . LEU B 13  ? 0.8746 0.8668 0.7070 0.1439  0.1438  0.0901  228 LEU A N   
1733 C CA  . LEU B 13  ? 0.8540 0.8269 0.6633 0.1300  0.1241  0.0752  228 LEU A CA  
1734 C C   . LEU B 13  ? 0.8887 0.8146 0.6954 0.1245  0.1173  0.0455  228 LEU A C   
1735 O O   . LEU B 13  ? 0.8694 0.7753 0.7052 0.1274  0.1178  0.0519  228 LEU A O   
1736 C CB  . LEU B 13  ? 0.7745 0.7470 0.6115 0.1183  0.1077  0.1045  228 LEU A CB  
1737 C CG  . LEU B 13  ? 0.8018 0.7674 0.6205 0.1095  0.0911  0.0979  228 LEU A CG  
1738 C CD1 . LEU B 13  ? 0.8042 0.8165 0.5964 0.1177  0.0968  0.1123  228 LEU A CD1 
1739 C CD2 . LEU B 13  ? 0.7594 0.7019 0.6130 0.0988  0.0772  0.1146  228 LEU A CD2 
1740 N N   . GLN B 14  ? 0.8528 0.7677 0.6269 0.1164  0.1117  0.0160  229 GLN A N   
1741 C CA  . GLN B 14  ? 0.8559 0.7255 0.6298 0.1081  0.1076  -0.0091 229 GLN A CA  
1742 C C   . GLN B 14  ? 0.8903 0.7596 0.6503 0.0909  0.0889  -0.0193 229 GLN A C   
1743 O O   . GLN B 14  ? 0.8798 0.7853 0.6175 0.0881  0.0836  -0.0219 229 GLN A O   
1744 C CB  . GLN B 14  ? 0.9087 0.7575 0.6637 0.1142  0.1275  -0.0447 229 GLN A CB  
1745 C CG  . GLN B 14  ? 0.9150 0.7795 0.6739 0.1357  0.1514  -0.0407 229 GLN A CG  
1746 C CD  . GLN B 14  ? 1.0177 0.9203 0.7342 0.1391  0.1632  -0.0642 229 GLN A CD  
1747 O OE1 . GLN B 14  ? 1.0450 0.9983 0.7471 0.1383  0.1559  -0.0439 229 GLN A OE1 
1748 N NE2 . GLN B 14  ? 1.1953 1.0744 0.8914 0.1437  0.1830  -0.1073 229 GLN A NE2 
1749 N N   . LEU B 15  ? 0.9250 0.7611 0.6999 0.0815  0.0796  -0.0209 230 LEU A N   
1750 C CA  . LEU B 15  ? 0.8679 0.7015 0.6335 0.0654  0.0664  -0.0349 230 LEU A CA  
1751 C C   . LEU B 15  ? 0.8650 0.6886 0.6094 0.0556  0.0746  -0.0727 230 LEU A C   
1752 O O   . LEU B 15  ? 0.9331 0.7218 0.6807 0.0598  0.0909  -0.0877 230 LEU A O   
1753 C CB  . LEU B 15  ? 0.9067 0.7115 0.6932 0.0599  0.0587  -0.0241 230 LEU A CB  
1754 C CG  . LEU B 15  ? 0.8809 0.6845 0.6711 0.0475  0.0454  -0.0239 230 LEU A CG  
1755 C CD1 . LEU B 15  ? 0.9212 0.7081 0.7055 0.0322  0.0482  -0.0467 230 LEU A CD1 
1756 C CD2 . LEU B 15  ? 0.8115 0.6501 0.5994 0.0484  0.0350  -0.0150 230 LEU A CD2 
1757 N N   . VAL B 16  ? 0.9049 0.7624 0.6298 0.0435  0.0646  -0.0891 231 VAL A N   
1758 C CA  . VAL B 16  ? 1.0141 0.8660 0.7216 0.0264  0.0689  -0.1317 231 VAL A CA  
1759 C C   . VAL B 16  ? 1.0520 0.8957 0.7729 0.0040  0.0576  -0.1413 231 VAL A C   
1760 O O   . VAL B 16  ? 1.0879 0.8993 0.8122 -0.0139 0.0655  -0.1722 231 VAL A O   
1761 C CB  . VAL B 16  ? 1.0434 0.9539 0.7152 0.0256  0.0663  -0.1513 231 VAL A CB  
1762 C CG1 . VAL B 16  ? 0.9682 0.8921 0.6271 0.0486  0.0815  -0.1385 231 VAL A CG1 
1763 C CG2 . VAL B 16  ? 0.9967 0.9697 0.6639 0.0222  0.0447  -0.1325 231 VAL A CG2 
1764 N N   . GLU B 17  ? 0.9290 0.7979 0.6619 0.0050  0.0423  -0.1153 232 GLU A N   
1765 C CA  . GLU B 17  ? 0.8745 0.7423 0.6242 -0.0122 0.0340  -0.1176 232 GLU A CA  
1766 C C   . GLU B 17  ? 0.8477 0.7254 0.6130 0.0005  0.0254  -0.0835 232 GLU A C   
1767 O O   . GLU B 17  ? 0.8298 0.7311 0.5925 0.0168  0.0208  -0.0625 232 GLU A O   
1768 C CB  . GLU B 17  ? 0.9083 0.8278 0.6495 -0.0317 0.0223  -0.1421 232 GLU A CB  
1769 C CG  . GLU B 17  ? 0.9949 0.8921 0.7520 -0.0605 0.0257  -0.1685 232 GLU A CG  
1770 C CD  . GLU B 17  ? 1.0372 0.9930 0.7876 -0.0844 0.0127  -0.1988 232 GLU A CD  
1771 O OE1 . GLU B 17  ? 0.9485 0.9268 0.7225 -0.1037 0.0051  -0.2002 232 GLU A OE1 
1772 O OE2 . GLU B 17  ? 1.1799 1.1672 0.9011 -0.0835 0.0100  -0.2206 232 GLU A OE2 
1773 N N   . PHE B 18  ? 0.8439 0.7018 0.6261 -0.0078 0.0255  -0.0790 233 PHE A N   
1774 C CA  . PHE B 18  ? 0.8086 0.6776 0.6037 0.0012  0.0189  -0.0567 233 PHE A CA  
1775 C C   . PHE B 18  ? 0.8116 0.6837 0.6199 -0.0146 0.0196  -0.0625 233 PHE A C   
1776 O O   . PHE B 18  ? 0.8285 0.6677 0.6412 -0.0270 0.0291  -0.0688 233 PHE A O   
1777 C CB  . PHE B 18  ? 0.8092 0.6460 0.6083 0.0150  0.0226  -0.0381 233 PHE A CB  
1778 C CG  . PHE B 18  ? 0.7672 0.6080 0.5767 0.0199  0.0182  -0.0260 233 PHE A CG  
1779 C CD1 . PHE B 18  ? 0.8260 0.6554 0.6388 0.0121  0.0220  -0.0266 233 PHE A CD1 
1780 C CD2 . PHE B 18  ? 0.7456 0.6015 0.5623 0.0326  0.0131  -0.0141 233 PHE A CD2 
1781 C CE1 . PHE B 18  ? 0.8270 0.6644 0.6444 0.0177  0.0203  -0.0210 233 PHE A CE1 
1782 C CE2 . PHE B 18  ? 0.7845 0.6387 0.6112 0.0378  0.0123  -0.0102 233 PHE A CE2 
1783 C CZ  . PHE B 18  ? 0.7901 0.6374 0.6143 0.0306  0.0156  -0.0164 233 PHE A CZ  
1784 N N   . SER B 19  ? 0.7557 0.6688 0.5745 -0.0125 0.0120  -0.0564 234 SER A N   
1785 C CA  . SER B 19  ? 0.7713 0.6986 0.6067 -0.0257 0.0145  -0.0586 234 SER A CA  
1786 C C   . SER B 19  ? 0.7352 0.6870 0.5822 -0.0081 0.0122  -0.0425 234 SER A C   
1787 O O   . SER B 19  ? 0.7131 0.6832 0.5614 0.0100  0.0063  -0.0320 234 SER A O   
1788 C CB  . SER B 19  ? 0.7493 0.7161 0.5935 -0.0489 0.0093  -0.0786 234 SER A CB  
1789 O OG  . SER B 19  ? 0.7668 0.7956 0.6145 -0.0400 -0.0038 -0.0743 234 SER A OG  
1790 N N   . ALA B 20  ? 0.7578 0.7078 0.6141 -0.0121 0.0201  -0.0393 235 ALA A N   
1791 C CA  . ALA B 20  ? 0.7561 0.7363 0.6271 0.0026  0.0221  -0.0310 235 ALA A CA  
1792 C C   . ALA B 20  ? 0.7036 0.7237 0.5953 -0.0143 0.0269  -0.0342 235 ALA A C   
1793 O O   . ALA B 20  ? 0.6916 0.6954 0.5835 -0.0363 0.0337  -0.0387 235 ALA A O   
1794 C CB  . ALA B 20  ? 0.6977 0.6453 0.5579 0.0164  0.0293  -0.0265 235 ALA A CB  
1795 N N   . PHE B 21  ? 0.6832 0.7575 0.5980 -0.0042 0.0246  -0.0289 236 PHE A N   
1796 C CA  . PHE B 21  ? 0.6922 0.8212 0.6343 -0.0247 0.0252  -0.0324 236 PHE A CA  
1797 C C   . PHE B 21  ? 0.6577 0.8441 0.6289 -0.0043 0.0295  -0.0204 236 PHE A C   
1798 O O   . PHE B 21  ? 0.6615 0.8448 0.6333 0.0268  0.0302  -0.0107 236 PHE A O   
1799 C CB  . PHE B 21  ? 0.6995 0.8600 0.6449 -0.0449 0.0094  -0.0452 236 PHE A CB  
1800 C CG  . PHE B 21  ? 0.7270 0.9172 0.6668 -0.0223 -0.0045 -0.0369 236 PHE A CG  
1801 C CD1 . PHE B 21  ? 0.7523 1.0178 0.7196 -0.0077 -0.0120 -0.0229 236 PHE A CD1 
1802 C CD2 . PHE B 21  ? 0.7698 0.9175 0.6802 -0.0134 -0.0084 -0.0378 236 PHE A CD2 
1803 C CE1 . PHE B 21  ? 0.7731 1.0689 0.7366 0.0158  -0.0234 -0.0068 236 PHE A CE1 
1804 C CE2 . PHE B 21  ? 0.7584 0.9368 0.6643 0.0076  -0.0187 -0.0236 236 PHE A CE2 
1805 C CZ  . PHE B 21  ? 0.7587 1.0097 0.6902 0.0225  -0.0262 -0.0065 236 PHE A CZ  
1806 N N   . VAL B 22  ? 0.6799 0.9189 0.6810 -0.0221 0.0344  -0.0203 237 VAL A N   
1807 C CA  . VAL B 22  ? 0.6999 1.0113 0.7382 -0.0037 0.0379  -0.0079 237 VAL A CA  
1808 C C   . VAL B 22  ? 0.7472 1.1372 0.8177 -0.0292 0.0228  -0.0112 237 VAL A C   
1809 O O   . VAL B 22  ? 0.7332 1.1236 0.8097 -0.0686 0.0219  -0.0252 237 VAL A O   
1810 C CB  . VAL B 22  ? 0.7223 1.0401 0.7719 0.0032  0.0618  -0.0025 237 VAL A CB  
1811 C CG1 . VAL B 22  ? 0.6663 0.9812 0.7204 -0.0352 0.0717  -0.0057 237 VAL A CG1 
1812 C CG2 . VAL B 22  ? 0.7145 1.1114 0.8080 0.0270  0.0677  0.0107  237 VAL A CG2 
1813 N N   . GLU B 23  ? 0.8275 1.2838 0.9202 -0.0073 0.0104  0.0019  238 GLU A N   
1814 C CA  . GLU B 23  ? 0.8717 1.4242 0.9957 -0.0256 -0.0092 0.0012  238 GLU A CA  
1815 C C   . GLU B 23  ? 0.9442 1.5826 1.1217 -0.0083 -0.0007 0.0212  238 GLU A C   
1816 O O   . GLU B 23  ? 0.9477 1.5825 1.1343 0.0366  0.0118  0.0417  238 GLU A O   
1817 C CB  . GLU B 23  ? 0.8385 1.4154 0.9457 -0.0075 -0.0307 0.0094  238 GLU A CB  
1818 C CG  . GLU B 23  ? 0.8147 1.3882 0.8915 -0.0424 -0.0500 -0.0170 238 GLU A CG  
1819 C CD  . GLU B 23  ? 0.8507 1.4234 0.8960 -0.0166 -0.0632 -0.0045 238 GLU A CD  
1820 O OE1 . GLU B 23  ? 0.8356 1.4178 0.8920 0.0264  -0.0587 0.0287  238 GLU A OE1 
1821 O OE2 . GLU B 23  ? 0.8508 1.4125 0.8620 -0.0383 -0.0752 -0.0270 238 GLU A OE2 
1822 N N   . PRO B 24  ? 1.0843 1.8000 1.3022 -0.0416 -0.0050 0.0156  239 PRO A N   
1823 C CA  . PRO B 24  ? 1.1082 1.9087 1.3822 -0.0242 0.0079  0.0366  239 PRO A CA  
1824 C C   . PRO B 24  ? 1.0977 1.9824 1.4012 0.0168  -0.0054 0.0636  239 PRO A C   
1825 O O   . PRO B 24  ? 1.0501 1.9417 1.3314 0.0233  -0.0281 0.0662  239 PRO A O   
1826 C CB  . PRO B 24  ? 1.1243 1.9897 1.4369 -0.0796 0.0023  0.0223  239 PRO A CB  
1827 C CG  . PRO B 24  ? 1.1212 1.9056 1.3925 -0.1237 -0.0055 -0.0089 239 PRO A CG  
1828 C CD  . PRO B 24  ? 1.0847 1.8160 1.3045 -0.0981 -0.0201 -0.0120 239 PRO A CD  
1829 N N   . PRO B 25  ? 1.0097 1.9637 1.3650 0.0484  0.0104  0.0877  240 PRO A N   
1830 C CA  . PRO B 25  ? 0.9390 1.9750 1.3340 0.0970  0.0044  0.1223  240 PRO A CA  
1831 C C   . PRO B 25  ? 0.9512 2.0549 1.3421 0.0901  -0.0324 0.1308  240 PRO A C   
1832 O O   . PRO B 25  ? 0.9953 2.0392 1.3443 0.1097  -0.0395 0.1363  240 PRO A O   
1833 C CB  . PRO B 25  ? 0.8838 2.0289 1.3487 0.0969  0.0164  0.1357  240 PRO A CB  
1834 C CG  . PRO B 25  ? 0.8988 1.9777 1.3496 0.0744  0.0454  0.1151  240 PRO A CG  
1835 C CD  . PRO B 25  ? 0.9404 1.8998 1.3217 0.0409  0.0394  0.0858  240 PRO A CD  
1836 N N   . ARG B 33  ? 0.7166 1.2098 0.8221 -0.2047 -0.0325 -0.1118 248 ARG A N   
1837 C CA  . ARG B 33  ? 0.6916 1.1090 0.7687 -0.1650 -0.0150 -0.0880 248 ARG A CA  
1838 C C   . ARG B 33  ? 0.6775 1.0261 0.7591 -0.1811 0.0101  -0.0844 248 ARG A C   
1839 O O   . ARG B 33  ? 0.7045 1.0501 0.8116 -0.2229 0.0163  -0.0988 248 ARG A O   
1840 C CB  . ARG B 33  ? 0.7194 1.0759 0.7461 -0.1459 -0.0217 -0.0950 248 ARG A CB  
1841 C CG  . ARG B 33  ? 0.7787 1.2007 0.7942 -0.1326 -0.0451 -0.0963 248 ARG A CG  
1842 C CD  . ARG B 33  ? 0.7808 1.1697 0.7655 -0.0876 -0.0445 -0.0730 248 ARG A CD  
1843 N NE  . ARG B 33  ? 0.8488 1.1605 0.7917 -0.0885 -0.0410 -0.0870 248 ARG A NE  
1844 C CZ  . ARG B 33  ? 0.8929 1.2064 0.8069 -0.0682 -0.0494 -0.0809 248 ARG A CZ  
1845 N NH1 . ARG B 33  ? 0.8351 1.2237 0.7548 -0.0467 -0.0634 -0.0599 248 ARG A NH1 
1846 N NH2 . ARG B 33  ? 0.8920 1.1354 0.7735 -0.0680 -0.0422 -0.0921 248 ARG A NH2 
1847 N N   . HIS B 34  ? 0.6870 0.9849 0.7458 -0.1479 0.0248  -0.0635 249 HIS A N   
1848 C CA  . HIS B 34  ? 0.6613 0.8868 0.7075 -0.1540 0.0462  -0.0554 249 HIS A CA  
1849 C C   . HIS B 34  ? 0.6567 0.8134 0.6568 -0.1242 0.0452  -0.0520 249 HIS A C   
1850 O O   . HIS B 34  ? 0.6784 0.8444 0.6653 -0.0900 0.0418  -0.0419 249 HIS A O   
1851 C CB  . HIS B 34  ? 0.6662 0.9209 0.7326 -0.1446 0.0661  -0.0322 249 HIS A CB  
1852 C CG  . HIS B 34  ? 0.6801 0.8695 0.7198 -0.1371 0.0858  -0.0169 249 HIS A CG  
1853 N ND1 . HIS B 34  ? 0.7262 0.8802 0.7764 -0.1664 0.1017  -0.0094 249 HIS A ND1 
1854 C CD2 . HIS B 34  ? 0.6856 0.8414 0.6889 -0.1040 0.0912  -0.0071 249 HIS A CD2 
1855 C CE1 . HIS B 34  ? 0.7621 0.8715 0.7816 -0.1483 0.1152  0.0095  249 HIS A CE1 
1856 N NE2 . HIS B 34  ? 0.7285 0.8405 0.7176 -0.1124 0.1076  0.0078  249 HIS A NE2 
1857 N N   . LEU B 35  ? 0.6887 0.7773 0.6697 -0.1369 0.0496  -0.0599 250 LEU A N   
1858 C CA  . LEU B 35  ? 0.7150 0.7459 0.6582 -0.1113 0.0482  -0.0557 250 LEU A CA  
1859 C C   . LEU B 35  ? 0.6958 0.6911 0.6263 -0.0989 0.0644  -0.0340 250 LEU A C   
1860 O O   . LEU B 35  ? 0.7200 0.6861 0.6582 -0.1165 0.0790  -0.0250 250 LEU A O   
1861 C CB  . LEU B 35  ? 0.6910 0.6743 0.6213 -0.1260 0.0451  -0.0751 250 LEU A CB  
1862 C CG  . LEU B 35  ? 0.7175 0.7438 0.6556 -0.1451 0.0294  -0.1028 250 LEU A CG  
1863 C CD1 . LEU B 35  ? 0.7379 0.7123 0.6618 -0.1612 0.0318  -0.1290 250 LEU A CD1 
1864 C CD2 . LEU B 35  ? 0.7101 0.7896 0.6369 -0.1187 0.0120  -0.0974 250 LEU A CD2 
1865 N N   . PHE B 36  ? 0.6943 0.6934 0.6060 -0.0691 0.0625  -0.0253 251 PHE A N   
1866 C CA  . PHE B 36  ? 0.6944 0.6645 0.5840 -0.0562 0.0732  -0.0101 251 PHE A CA  
1867 C C   . PHE B 36  ? 0.7551 0.6680 0.6251 -0.0560 0.0717  -0.0066 251 PHE A C   
1868 O O   . PHE B 36  ? 0.7883 0.6786 0.6506 -0.0580 0.0829  0.0110  251 PHE A O   
1869 C CB  . PHE B 36  ? 0.7043 0.6879 0.5788 -0.0277 0.0700  -0.0116 251 PHE A CB  
1870 C CG  . PHE B 36  ? 0.7187 0.7570 0.6162 -0.0193 0.0741  -0.0138 251 PHE A CG  
1871 C CD1 . PHE B 36  ? 0.6712 0.7461 0.5826 -0.0261 0.0909  -0.0049 251 PHE A CD1 
1872 C CD2 . PHE B 36  ? 0.6331 0.6900 0.5413 -0.0017 0.0636  -0.0201 251 PHE A CD2 
1873 C CE1 . PHE B 36  ? 0.6410 0.7722 0.5787 -0.0148 0.0970  -0.0055 251 PHE A CE1 
1874 C CE2 . PHE B 36  ? 0.6611 0.7708 0.5961 0.0115  0.0690  -0.0177 251 PHE A CE2 
1875 C CZ  . PHE B 36  ? 0.6956 0.8439 0.6463 0.0055  0.0859  -0.0121 251 PHE A CZ  
1876 N N   . VAL B 37  ? 0.7452 0.6401 0.6079 -0.0506 0.0592  -0.0193 252 VAL A N   
1877 C CA  . VAL B 37  ? 0.7405 0.5869 0.5901 -0.0478 0.0594  -0.0170 252 VAL A CA  
1878 C C   . VAL B 37  ? 0.7978 0.6407 0.6484 -0.0522 0.0503  -0.0370 252 VAL A C   
1879 O O   . VAL B 37  ? 0.7904 0.6704 0.6433 -0.0484 0.0396  -0.0462 252 VAL A O   
1880 C CB  . VAL B 37  ? 0.7768 0.6112 0.6047 -0.0253 0.0546  -0.0060 252 VAL A CB  
1881 C CG1 . VAL B 37  ? 0.7782 0.6252 0.5967 -0.0214 0.0631  0.0107  252 VAL A CG1 
1882 C CG2 . VAL B 37  ? 0.7440 0.5967 0.5682 -0.0108 0.0424  -0.0161 252 VAL A CG2 
1883 N N   . HIS B 38  ? 0.7911 0.5923 0.6394 -0.0573 0.0563  -0.0420 253 HIS A N   
1884 C CA  . HIS B 38  ? 0.8225 0.6229 0.6672 -0.0636 0.0511  -0.0663 253 HIS A CA  
1885 C C   . HIS B 38  ? 0.8707 0.6211 0.7076 -0.0548 0.0602  -0.0670 253 HIS A C   
1886 O O   . HIS B 38  ? 0.8862 0.5946 0.7347 -0.0609 0.0753  -0.0606 253 HIS A O   
1887 C CB  . HIS B 38  ? 0.8148 0.6318 0.6777 -0.0942 0.0529  -0.0891 253 HIS A CB  
1888 C CG  . HIS B 38  ? 0.9263 0.7460 0.7801 -0.1045 0.0481  -0.1213 253 HIS A CG  
1889 N ND1 . HIS B 38  ? 0.9229 0.8039 0.7757 -0.1154 0.0327  -0.1401 253 HIS A ND1 
1890 C CD2 . HIS B 38  ? 0.9421 0.7164 0.7870 -0.1056 0.0579  -0.1397 253 HIS A CD2 
1891 C CE1 . HIS B 38  ? 0.9085 0.7851 0.7460 -0.1242 0.0315  -0.1706 253 HIS A CE1 
1892 N NE2 . HIS B 38  ? 0.9447 0.7532 0.7775 -0.1183 0.0483  -0.1732 253 HIS A NE2 
1893 N N   . ILE B 39  ? 0.9052 0.6618 0.7266 -0.0387 0.0535  -0.0713 254 ILE A N   
1894 C CA  . ILE B 39  ? 0.9257 0.6454 0.7419 -0.0286 0.0637  -0.0758 254 ILE A CA  
1895 C C   . ILE B 39  ? 0.9804 0.7144 0.7846 -0.0377 0.0625  -0.1087 254 ILE A C   
1896 O O   . ILE B 39  ? 0.9496 0.7269 0.7394 -0.0305 0.0502  -0.1103 254 ILE A O   
1897 C CB  . ILE B 39  ? 0.9120 0.6349 0.7219 -0.0035 0.0593  -0.0534 254 ILE A CB  
1898 C CG1 . ILE B 39  ? 0.8672 0.5864 0.6835 0.0031  0.0575  -0.0262 254 ILE A CG1 
1899 C CG2 . ILE B 39  ? 0.8984 0.5935 0.7074 0.0090  0.0719  -0.0578 254 ILE A CG2 
1900 C CD1 . ILE B 39  ? 0.8012 0.5329 0.6150 0.0208  0.0491  -0.0085 254 ILE A CD1 
1901 N N   . SER B 40  ? 1.0355 0.7345 0.8456 -0.0538 0.0762  -0.1352 255 SER A N   
1902 C CA  . SER B 40  ? 1.0235 0.7345 0.8167 -0.0639 0.0770  -0.1747 255 SER A CA  
1903 C C   . SER B 40  ? 1.0855 0.7457 0.8754 -0.0486 0.0978  -0.1849 255 SER A C   
1904 O O   . SER B 40  ? 1.1107 0.7113 0.9223 -0.0490 0.1165  -0.1812 255 SER A O   
1905 C CB  . SER B 40  ? 1.0346 0.7497 0.8392 -0.1003 0.0765  -0.2095 255 SER A CB  
1906 O OG  . SER B 40  ? 1.1773 0.8851 0.9653 -0.1114 0.0833  -0.2557 255 SER A OG  
1907 N N   . GLN B 41  ? 1.1377 0.8235 0.9031 -0.0325 0.0971  -0.1939 256 GLN A N   
1908 C CA  . GLN B 41  ? 1.2479 0.8937 1.0119 -0.0127 0.1193  -0.2013 256 GLN A CA  
1909 C C   . GLN B 41  ? 1.3560 1.0148 1.0922 -0.0228 0.1262  -0.2527 256 GLN A C   
1910 O O   . GLN B 41  ? 1.3944 1.0174 1.1358 -0.0464 0.1368  -0.2941 256 GLN A O   
1911 C CB  . GLN B 41  ? 1.1390 0.8038 0.9043 0.0181  0.1167  -0.1599 256 GLN A CB  
1912 C CG  . GLN B 41  ? 1.0755 0.7033 0.8708 0.0317  0.1226  -0.1225 256 GLN A CG  
1913 C CD  . GLN B 41  ? 0.9956 0.6536 0.7961 0.0540  0.1141  -0.0849 256 GLN A CD  
1914 O OE1 . GLN B 41  ? 0.9949 0.6371 0.8168 0.0683  0.1179  -0.0557 256 GLN A OE1 
1915 N NE2 . GLN B 41  ? 0.9939 0.6994 0.7775 0.0559  0.1023  -0.0834 256 GLN A NE2 
1916 N N   . HIS B 42  ? 1.5047 1.2154 1.2111 -0.0074 0.1217  -0.2531 257 HIS A N   
1917 C CA  . HIS B 42  ? 1.5681 1.3109 1.2372 -0.0154 0.1258  -0.3012 257 HIS A CA  
1918 C C   . HIS B 42  ? 1.6211 1.3171 1.2844 0.0014  0.1577  -0.3303 257 HIS A C   
1919 O O   . HIS B 42  ? 1.6464 1.2664 1.3386 0.0023  0.1788  -0.3396 257 HIS A O   
1920 C CB  . HIS B 42  ? 1.5851 1.3402 1.2489 -0.0548 0.1141  -0.3463 257 HIS A CB  
1921 C CG  . HIS B 42  ? 1.5834 1.4083 1.2464 -0.0680 0.0835  -0.3244 257 HIS A CG  
1922 N ND1 . HIS B 42  ? 1.5721 1.4816 1.2022 -0.0770 0.0647  -0.3412 257 HIS A ND1 
1923 C CD2 . HIS B 42  ? 1.5309 1.3572 1.2231 -0.0714 0.0702  -0.2870 257 HIS A CD2 
1924 C CE1 . HIS B 42  ? 1.5474 1.5051 1.1917 -0.0830 0.0417  -0.3117 257 HIS A CE1 
1925 N NE2 . HIS B 42  ? 1.4990 1.4053 1.1803 -0.0801 0.0457  -0.2814 257 HIS A NE2 
1926 N N   . PRO B 49  ? 1.7744 1.0768 1.8736 0.2605  0.3352  0.0460  264 PRO A N   
1927 C CA  . PRO B 49  ? 1.6660 1.0268 1.7854 0.2854  0.3211  0.1107  264 PRO A CA  
1928 C C   . PRO B 49  ? 1.6296 1.0514 1.7204 0.2796  0.2922  0.1200  264 PRO A C   
1929 O O   . PRO B 49  ? 1.6660 1.0776 1.7214 0.2507  0.2789  0.0913  264 PRO A O   
1930 C CB  . PRO B 49  ? 1.6733 1.0122 1.8109 0.2757  0.3188  0.1471  264 PRO A CB  
1931 C CG  . PRO B 49  ? 1.7862 1.0569 1.9098 0.2393  0.3282  0.0965  264 PRO A CG  
1932 C CD  . PRO B 49  ? 1.8218 1.0636 1.9443 0.2470  0.3493  0.0470  264 PRO A CD  
1933 N N   . PRO B 50  ? 1.4633 0.9502 1.5725 0.3060  0.2828  0.1599  265 PRO A N   
1934 C CA  . PRO B 50  ? 1.3659 0.9125 1.4546 0.3012  0.2554  0.1701  265 PRO A CA  
1935 C C   . PRO B 50  ? 1.2586 0.8140 1.3272 0.2783  0.2287  0.1897  265 PRO A C   
1936 O O   . PRO B 50  ? 1.2723 0.8006 1.3469 0.2697  0.2311  0.2047  265 PRO A O   
1937 C CB  . PRO B 50  ? 1.3184 0.9372 1.4443 0.3321  0.2510  0.2141  265 PRO A CB  
1938 C CG  . PRO B 50  ? 1.3202 0.9097 1.4787 0.3567  0.2836  0.2126  265 PRO A CG  
1939 C CD  . PRO B 50  ? 1.3921 0.9034 1.5455 0.3411  0.2978  0.1956  265 PRO A CD  
1940 N N   . LEU B 51  ? 1.2019 0.8143 1.2452 0.2590  0.1982  0.1846  266 LEU A N   
1941 C CA  . LEU B 51  ? 1.1202 0.7606 1.1426 0.2353  0.1692  0.1995  266 LEU A CA  
1942 C C   . LEU B 51  ? 1.1367 0.8315 1.1842 0.2566  0.1567  0.2559  266 LEU A C   
1943 O O   . LEU B 51  ? 1.1537 0.8919 1.2329 0.2827  0.1583  0.2803  266 LEU A O   
1944 C CB  . LEU B 51  ? 1.0097 0.6929 1.0004 0.2066  0.1417  0.1718  266 LEU A CB  
1945 C CG  . LEU B 51  ? 1.0043 0.6501 0.9676 0.1865  0.1500  0.1217  266 LEU A CG  
1946 C CD1 . LEU B 51  ? 0.9168 0.6102 0.8600 0.1690  0.1282  0.1049  266 LEU A CD1 
1947 C CD2 . LEU B 51  ? 0.9238 0.5215 0.8695 0.1642  0.1532  0.1056  266 LEU A CD2 
1948 N N   . GLU B 52  ? 1.0281 0.7278 1.0620 0.2460  0.1449  0.2782  267 GLU A N   
1949 C CA  . GLU B 52  ? 1.0268 0.7964 1.0719 0.2604  0.1256  0.3286  267 GLU A CA  
1950 C C   . GLU B 52  ? 0.9873 0.8357 1.0189 0.2429  0.0912  0.3155  267 GLU A C   
1951 O O   . GLU B 52  ? 0.9553 0.7962 0.9641 0.2171  0.0822  0.2725  267 GLU A O   
1952 C CB  . GLU B 52  ? 1.0815 0.8441 1.1067 0.2500  0.1220  0.3515  267 GLU A CB  
1953 C CG  . GLU B 52  ? 1.0603 0.8524 1.1140 0.2697  0.1281  0.3965  267 GLU A CG  
1954 C CD  . GLU B 52  ? 1.1127 0.8775 1.1533 0.2578  0.1367  0.4120  267 GLU A CD  
1955 O OE1 . GLU B 52  ? 1.0982 0.8981 1.1022 0.2409  0.1170  0.4174  267 GLU A OE1 
1956 O OE2 . GLU B 52  ? 1.1810 0.8927 1.2495 0.2656  0.1645  0.4201  267 GLU A OE2 
1957 N N   . SER B 53  ? 1.0152 0.9419 1.0648 0.2568  0.0722  0.3542  268 SER A N   
1958 C CA  . SER B 53  ? 0.9848 0.9875 1.0301 0.2372  0.0399  0.3408  268 SER A CA  
1959 C C   . SER B 53  ? 0.9671 1.0294 0.9849 0.2224  0.0107  0.3544  268 SER A C   
1960 O O   . SER B 53  ? 0.9781 1.0603 0.9969 0.2415  0.0125  0.3977  268 SER A O   
1961 C CB  . SER B 53  ? 0.9725 1.0347 1.0671 0.2600  0.0388  0.3647  268 SER A CB  
1962 O OG  . SER B 53  ? 1.0310 1.1600 1.1498 0.2849  0.0289  0.4182  268 SER A OG  
1963 N N   . VAL B 54  ? 0.9651 1.0544 0.9582 0.1895  -0.0140 0.3171  269 VAL A N   
1964 C CA  . VAL B 54  ? 0.9197 1.0646 0.8796 0.1697  -0.0420 0.3131  269 VAL A CA  
1965 C C   . VAL B 54  ? 0.9240 1.1397 0.8988 0.1497  -0.0708 0.2947  269 VAL A C   
1966 O O   . VAL B 54  ? 0.9145 1.1065 0.9026 0.1338  -0.0689 0.2630  269 VAL A O   
1967 C CB  . VAL B 54  ? 0.9094 1.0029 0.8238 0.1450  -0.0391 0.2749  269 VAL A CB  
1968 C CG1 . VAL B 54  ? 0.9165 1.0693 0.7949 0.1266  -0.0649 0.2652  269 VAL A CG1 
1969 C CG2 . VAL B 54  ? 0.9426 0.9689 0.8491 0.1586  -0.0107 0.2914  269 VAL A CG2 
1970 N N   . ASP B 55  ? 0.9225 1.2282 0.8958 0.1486  -0.0973 0.3149  270 ASP A N   
1971 C CA  . ASP B 55  ? 0.9245 1.3024 0.9170 0.1237  -0.1265 0.2937  270 ASP A CA  
1972 C C   . ASP B 55  ? 0.9586 1.3134 0.9147 0.0844  -0.1394 0.2358  270 ASP A C   
1973 O O   . ASP B 55  ? 1.0071 1.3709 0.9165 0.0751  -0.1482 0.2230  270 ASP A O   
1974 C CB  . ASP B 55  ? 0.9396 1.4318 0.9418 0.1319  -0.1540 0.3294  270 ASP A CB  
1975 C CG  . ASP B 55  ? 0.9962 1.5674 1.0428 0.1119  -0.1791 0.3184  270 ASP A CG  
1976 O OD1 . ASP B 55  ? 1.0069 1.6014 1.0376 0.0718  -0.2027 0.2714  270 ASP A OD1 
1977 O OD2 . ASP B 55  ? 0.9846 1.5929 1.0862 0.1354  -0.1732 0.3552  270 ASP A OD2 
1978 N N   . VAL B 56  ? 0.9898 1.3154 0.9697 0.0638  -0.1376 0.2033  271 VAL A N   
1979 C CA  . VAL B 56  ? 0.9923 1.2809 0.9485 0.0306  -0.1434 0.1507  271 VAL A CA  
1980 C C   . VAL B 56  ? 1.0731 1.4275 1.0054 0.0049  -0.1738 0.1249  271 VAL A C   
1981 O O   . VAL B 56  ? 1.0905 1.4147 0.9846 -0.0131 -0.1753 0.0852  271 VAL A O   
1982 C CB  . VAL B 56  ? 0.9409 1.2029 0.9389 0.0152  -0.1369 0.1333  271 VAL A CB  
1983 C CG1 . VAL B 56  ? 0.9542 1.2991 1.0004 0.0002  -0.1587 0.1407  271 VAL A CG1 
1984 C CG2 . VAL B 56  ? 0.9513 1.1570 0.9299 -0.0110 -0.1349 0.0870  271 VAL A CG2 
1985 N N   . ARG B 57  ? 1.1330 1.5833 1.0875 0.0031  -0.1982 0.1449  272 ARG A N   
1986 C CA  . ARG B 57  ? 1.1114 1.6381 1.0373 -0.0219 -0.2296 0.1184  272 ARG A CA  
1987 C C   . ARG B 57  ? 1.1246 1.6385 0.9831 -0.0132 -0.2251 0.1131  272 ARG A C   
1988 O O   . ARG B 57  ? 1.1440 1.6760 0.9642 -0.0389 -0.2396 0.0669  272 ARG A O   
1989 C CB  . ARG B 57  ? 1.0810 1.7276 1.0367 -0.0155 -0.2562 0.1555  272 ARG A CB  
1990 C CG  . ARG B 57  ? 1.0899 1.7690 1.1182 -0.0287 -0.2633 0.1592  272 ARG A CG  
1991 C CD  . ARG B 57  ? 1.0521 1.8609 1.1151 -0.0181 -0.2894 0.2017  272 ARG A CD  
1992 N NE  . ARG B 57  ? 1.0469 1.8556 1.1402 0.0320  -0.2674 0.2685  272 ARG A NE  
1993 C CZ  . ARG B 57  ? 1.1011 1.9491 1.1752 0.0694  -0.2665 0.3199  272 ARG A CZ  
1994 N NH1 . ARG B 57  ? 1.0800 1.9659 1.0968 0.0634  -0.2826 0.3133  272 ARG A NH1 
1995 N NH2 . ARG B 57  ? 1.1433 1.9831 1.2570 0.1148  -0.2430 0.3776  272 ARG A NH2 
1996 N N   . GLN B 58  ? 1.0506 1.5314 0.8961 0.0218  -0.2022 0.1580  273 GLN A N   
1997 C CA  . GLN B 58  ? 1.0711 1.5493 0.8586 0.0316  -0.1952 0.1642  273 GLN A CA  
1998 C C   . GLN B 58  ? 1.0941 1.4972 0.8473 0.0137  -0.1811 0.1122  273 GLN A C   
1999 O O   . GLN B 58  ? 1.1090 1.5153 0.8138 0.0181  -0.1745 0.1105  273 GLN A O   
2000 C CB  . GLN B 58  ? 1.0574 1.5053 0.8515 0.0703  -0.1695 0.2259  273 GLN A CB  
2001 C CG  . GLN B 58  ? 1.0472 1.5462 0.8894 0.0978  -0.1731 0.2832  273 GLN A CG  
2002 C CD  . GLN B 58  ? 1.0541 1.6710 0.8828 0.1096  -0.1979 0.3238  273 GLN A CD  
2003 O OE1 . GLN B 58  ? 1.0948 1.7632 0.8747 0.0923  -0.2153 0.3014  273 GLN A OE1 
2004 N NE2 . GLN B 58  ? 1.0220 1.6729 0.8996 0.1379  -0.1934 0.3753  273 GLN A NE2 
2005 N N   . ILE B 59  ? 1.1208 1.4619 0.9000 -0.0041 -0.1747 0.0742  274 ILE A N   
2006 C CA  . ILE B 59  ? 1.1249 1.3934 0.8795 -0.0139 -0.1580 0.0336  274 ILE A CA  
2007 C C   . ILE B 59  ? 1.1829 1.4321 0.9540 -0.0449 -0.1673 -0.0218 274 ILE A C   
2008 O O   . ILE B 59  ? 1.1781 1.3558 0.9509 -0.0492 -0.1502 -0.0482 274 ILE A O   
2009 C CB  . ILE B 59  ? 1.0576 1.2450 0.8275 0.0053  -0.1287 0.0547  274 ILE A CB  
2010 C CG1 . ILE B 59  ? 1.0509 1.2207 0.8729 0.0101  -0.1252 0.0720  274 ILE A CG1 
2011 C CG2 . ILE B 59  ? 1.0450 1.2346 0.7955 0.0305  -0.1145 0.0991  274 ILE A CG2 
2012 C CD1 . ILE B 59  ? 0.9482 1.0379 0.7825 0.0163  -0.1010 0.0672  274 ILE A CD1 
2013 N N   . TYR B 60  ? 1.1291 1.4428 0.9165 -0.0673 -0.1939 -0.0385 275 TYR A N   
2014 C CA  . TYR B 60  ? 1.1773 1.4679 0.9859 -0.1012 -0.2013 -0.0933 275 TYR A CA  
2015 C C   . TYR B 60  ? 1.2045 1.4781 0.9650 -0.1144 -0.1991 -0.1477 275 TYR A C   
2016 O O   . TYR B 60  ? 1.1753 1.3817 0.9481 -0.1282 -0.1867 -0.1883 275 TYR A O   
2017 C CB  . TYR B 60  ? 1.1749 1.5458 1.0184 -0.1269 -0.2314 -0.0997 275 TYR A CB  
2018 C CG  . TYR B 60  ? 1.1643 1.5386 1.0724 -0.1219 -0.2289 -0.0612 275 TYR A CG  
2019 C CD1 . TYR B 60  ? 1.1165 1.4079 1.0528 -0.1103 -0.2019 -0.0480 275 TYR A CD1 
2020 C CD2 . TYR B 60  ? 1.1470 1.6166 1.0880 -0.1280 -0.2534 -0.0376 275 TYR A CD2 
2021 C CE1 . TYR B 60  ? 1.0969 1.3970 1.0882 -0.1045 -0.1967 -0.0143 275 TYR A CE1 
2022 C CE2 . TYR B 60  ? 1.1228 1.6012 1.1256 -0.1212 -0.2480 -0.0021 275 TYR A CE2 
2023 C CZ  . TYR B 60  ? 1.1231 1.5147 1.1489 -0.1094 -0.2182 0.0083  275 TYR A CZ  
2024 O OH  . TYR B 60  ? 1.0792 1.4841 1.1623 -0.1012 -0.2097 0.0424  275 TYR A OH  
2025 N N   . ASP B 61  ? 1.2644 1.6019 0.9710 -0.1080 -0.2094 -0.1467 276 ASP A N   
2026 C CA  . ASP B 61  ? 1.3128 1.6439 0.9645 -0.1134 -0.2029 -0.1936 276 ASP A CA  
2027 C C   . ASP B 61  ? 1.3287 1.5659 0.9770 -0.0973 -0.1697 -0.2000 276 ASP A C   
2028 O O   . ASP B 61  ? 1.3190 1.5253 0.9452 -0.1056 -0.1593 -0.2510 276 ASP A O   
2029 C CB  . ASP B 61  ? 1.3072 1.7216 0.9023 -0.0967 -0.2111 -0.1649 276 ASP A CB  
2030 C CG  . ASP B 61  ? 1.3190 1.7244 0.9235 -0.0623 -0.1960 -0.0896 276 ASP A CG  
2031 O OD1 . ASP B 61  ? 1.3418 1.6866 0.9349 -0.0448 -0.1685 -0.0781 276 ASP A OD1 
2032 O OD2 . ASP B 61  ? 1.3111 1.7661 0.9417 -0.0533 -0.2102 -0.0436 276 ASP A OD2 
2033 N N   . LYS B 62  ? 1.2093 1.4054 0.8795 -0.0733 -0.1523 -0.1501 277 LYS A N   
2034 C CA  . LYS B 62  ? 1.1165 1.2430 0.7820 -0.0563 -0.1237 -0.1472 277 LYS A CA  
2035 C C   . LYS B 62  ? 1.0478 1.0991 0.7540 -0.0640 -0.1117 -0.1722 277 LYS A C   
2036 O O   . LYS B 62  ? 0.9836 0.9836 0.6920 -0.0493 -0.0899 -0.1680 277 LYS A O   
2037 C CB  . LYS B 62  ? 1.0529 1.1697 0.7250 -0.0314 -0.1110 -0.0879 277 LYS A CB  
2038 C CG  . LYS B 62  ? 1.1320 1.3096 0.7662 -0.0177 -0.1139 -0.0529 277 LYS A CG  
2039 C CD  . LYS B 62  ? 1.1050 1.2519 0.7222 0.0002  -0.0880 -0.0289 277 LYS A CD  
2040 C CE  . LYS B 62  ? 1.0941 1.2575 0.7179 0.0190  -0.0829 0.0332  277 LYS A CE  
2041 N NZ  . LYS B 62  ? 1.0627 1.2057 0.6707 0.0311  -0.0580 0.0582  277 LYS A NZ  
2042 N N   . PHE B 63  ? 1.1626 1.2099 0.9050 -0.0866 -0.1247 -0.1941 278 PHE A N   
2043 C CA  . PHE B 63  ? 1.1540 1.1312 0.9397 -0.0927 -0.1113 -0.2087 278 PHE A CA  
2044 C C   . PHE B 63  ? 1.2376 1.2134 1.0455 -0.1261 -0.1239 -0.2595 278 PHE A C   
2045 O O   . PHE B 63  ? 1.2673 1.3087 1.0654 -0.1458 -0.1482 -0.2734 278 PHE A O   
2046 C CB  . PHE B 63  ? 1.1292 1.0884 0.9577 -0.0836 -0.1070 -0.1625 278 PHE A CB  
2047 C CG  . PHE B 63  ? 1.0125 0.9662 0.8238 -0.0554 -0.0939 -0.1203 278 PHE A CG  
2048 C CD1 . PHE B 63  ? 0.9656 0.9684 0.7590 -0.0448 -0.1022 -0.0881 278 PHE A CD1 
2049 C CD2 . PHE B 63  ? 0.9193 0.8205 0.7355 -0.0403 -0.0732 -0.1131 278 PHE A CD2 
2050 C CE1 . PHE B 63  ? 0.9462 0.9347 0.7290 -0.0229 -0.0879 -0.0542 278 PHE A CE1 
2051 C CE2 . PHE B 63  ? 0.8671 0.7646 0.6702 -0.0209 -0.0626 -0.0819 278 PHE A CE2 
2052 C CZ  . PHE B 63  ? 0.8749 0.8104 0.6624 -0.0135 -0.0687 -0.0545 278 PHE A CZ  
2053 N N   . PRO B 64  ? 1.3805 1.2866 1.2195 -0.1322 -0.1076 -0.2846 279 PRO A N   
2054 C CA  . PRO B 64  ? 1.4333 1.3254 1.3019 -0.1676 -0.1159 -0.3356 279 PRO A CA  
2055 C C   . PRO B 64  ? 1.4361 1.3753 1.3456 -0.1931 -0.1388 -0.3190 279 PRO A C   
2056 O O   . PRO B 64  ? 1.4243 1.3539 1.3732 -0.1851 -0.1338 -0.2723 279 PRO A O   
2057 C CB  . PRO B 64  ? 1.4258 1.2247 1.3359 -0.1611 -0.0884 -0.3417 279 PRO A CB  
2058 C CG  . PRO B 64  ? 1.3927 1.1751 1.3045 -0.1268 -0.0733 -0.2833 279 PRO A CG  
2059 C CD  . PRO B 64  ? 1.3704 1.2080 1.2257 -0.1085 -0.0807 -0.2665 279 PRO A CD  
2060 N N   . GLU B 65  ? 1.4310 1.4307 1.3297 -0.2237 -0.1643 -0.3580 280 GLU A N   
2061 C CA  . GLU B 65  ? 1.4289 1.4723 1.3793 -0.2568 -0.1860 -0.3552 280 GLU A CA  
2062 C C   . GLU B 65  ? 1.5238 1.4956 1.5369 -0.2874 -0.1741 -0.3872 280 GLU A C   
2063 O O   . GLU B 65  ? 1.5000 1.5035 1.5629 -0.3248 -0.1910 -0.3982 280 GLU A O   
2064 C CB  . GLU B 65  ? 1.3727 1.5169 1.2919 -0.2817 -0.2203 -0.3872 280 GLU A CB  
2065 C CG  . GLU B 65  ? 1.3244 1.5413 1.1812 -0.2501 -0.2303 -0.3514 280 GLU A CG  
2066 C CD  . GLU B 65  ? 1.2889 1.5969 1.1685 -0.2468 -0.2536 -0.2984 280 GLU A CD  
2067 O OE1 . GLU B 65  ? 1.2655 1.5827 1.2098 -0.2677 -0.2610 -0.2880 280 GLU A OE1 
2068 O OE2 . GLU B 65  ? 1.2780 1.6497 1.1145 -0.2214 -0.2623 -0.2637 280 GLU A OE2 
2069 N N   . LYS B 66  ? 1.7751 1.6532 1.7920 -0.2714 -0.1440 -0.3976 281 LYS A N   
2070 C CA  . LYS B 66  ? 1.7956 1.5933 1.8651 -0.2977 -0.1278 -0.4373 281 LYS A CA  
2071 C C   . LYS B 66  ? 1.7784 1.5158 1.9082 -0.2844 -0.1041 -0.3825 281 LYS A C   
2072 O O   . LYS B 66  ? 1.7783 1.4337 1.9229 -0.2651 -0.0754 -0.3786 281 LYS A O   
2073 C CB  . LYS B 66  ? 1.7999 1.5391 1.8326 -0.2869 -0.1088 -0.4917 281 LYS A CB  
2074 N N   . LYS B 67  ? 1.5118 1.2997 1.6763 -0.2927 -0.1163 -0.3371 282 LYS A N   
2075 C CA  . LYS B 67  ? 1.3963 1.1478 1.6180 -0.2849 -0.0964 -0.2830 282 LYS A CA  
2076 C C   . LYS B 67  ? 1.3842 1.1005 1.5770 -0.2354 -0.0737 -0.2374 282 LYS A C   
2077 O O   . LYS B 67  ? 1.4334 1.1047 1.5924 -0.2139 -0.0602 -0.2567 282 LYS A O   
2078 C CB  . LYS B 67  ? 1.4152 1.0913 1.7055 -0.3166 -0.0792 -0.3071 282 LYS A CB  
2079 C CG  . LYS B 67  ? 1.3744 1.0099 1.7204 -0.3038 -0.0536 -0.2449 282 LYS A CG  
2080 N N   . GLY B 68  ? 1.2856 1.0271 1.4931 -0.2178 -0.0689 -0.1787 283 GLY A N   
2081 C CA  . GLY B 68  ? 1.2140 0.9403 1.3898 -0.1749 -0.0527 -0.1382 283 GLY A CA  
2082 C C   . GLY B 68  ? 1.1957 0.9684 1.3077 -0.1517 -0.0652 -0.1354 283 GLY A C   
2083 O O   . GLY B 68  ? 1.2117 0.9828 1.3007 -0.1207 -0.0546 -0.1011 283 GLY A O   
2084 N N   . GLY B 69  ? 1.1977 1.0143 1.2812 -0.1670 -0.0869 -0.1698 284 GLY A N   
2085 C CA  . GLY B 69  ? 1.1755 1.0381 1.2026 -0.1458 -0.0972 -0.1613 284 GLY A CA  
2086 C C   . GLY B 69  ? 1.1143 1.0427 1.1499 -0.1413 -0.1102 -0.1230 284 GLY A C   
2087 O O   . GLY B 69  ? 1.0896 1.0371 1.1743 -0.1556 -0.1127 -0.1051 284 GLY A O   
2088 N N   . LEU B 70  ? 1.0774 1.0415 1.0679 -0.1198 -0.1162 -0.1083 285 LEU A N   
2089 C CA  . LEU B 70  ? 1.0330 1.0500 1.0293 -0.1050 -0.1225 -0.0669 285 LEU A CA  
2090 C C   . LEU B 70  ? 1.0378 1.1149 1.0814 -0.1278 -0.1404 -0.0609 285 LEU A C   
2091 O O   . LEU B 70  ? 0.9998 1.0838 1.0844 -0.1229 -0.1316 -0.0294 285 LEU A O   
2092 C CB  . LEU B 70  ? 1.0166 1.0698 0.9627 -0.0870 -0.1304 -0.0592 285 LEU A CB  
2093 C CG  . LEU B 70  ? 0.9972 1.0563 0.9414 -0.0561 -0.1190 -0.0121 285 LEU A CG  
2094 C CD1 . LEU B 70  ? 0.9493 0.9475 0.9071 -0.0435 -0.0950 -0.0003 285 LEU A CD1 
2095 C CD2 . LEU B 70  ? 0.9481 1.0182 0.8444 -0.0365 -0.1177 -0.0011 285 LEU A CD2 
2096 N N   . ARG B 71  ? 1.1515 1.2809 1.1900 -0.1530 -0.1653 -0.0910 286 ARG A N   
2097 C CA  . ARG B 71  ? 1.1531 1.3571 1.2390 -0.1766 -0.1865 -0.0846 286 ARG A CA  
2098 C C   . ARG B 71  ? 1.1189 1.2949 1.2714 -0.1949 -0.1739 -0.0761 286 ARG A C   
2099 O O   . ARG B 71  ? 1.1154 1.3384 1.3119 -0.1918 -0.1744 -0.0401 286 ARG A O   
2100 C CB  . ARG B 71  ? 1.1711 1.4269 1.2430 -0.2111 -0.2154 -0.1334 286 ARG A CB  
2101 C CG  . ARG B 71  ? 1.1668 1.5358 1.2668 -0.2252 -0.2455 -0.1182 286 ARG A CG  
2102 C CD  . ARG B 71  ? 1.2077 1.6244 1.3123 -0.2738 -0.2745 -0.1772 286 ARG A CD  
2103 N NE  . ARG B 71  ? 1.2467 1.7286 1.2860 -0.2692 -0.2968 -0.1951 286 ARG A NE  
2104 C CZ  . ARG B 71  ? 1.2213 1.7959 1.2429 -0.2455 -0.3139 -0.1521 286 ARG A CZ  
2105 N NH1 . ARG B 71  ? 1.2106 1.8207 1.2761 -0.2221 -0.3105 -0.0918 286 ARG A NH1 
2106 N NH2 . ARG B 71  ? 1.1933 1.8281 1.1523 -0.2428 -0.3327 -0.1680 286 ARG A NH2 
2107 N N   . GLU B 72  ? 1.0483 1.1484 1.2117 -0.2112 -0.1595 -0.1050 287 GLU A N   
2108 C CA  . GLU B 72  ? 0.9915 1.0615 1.2202 -0.2292 -0.1445 -0.0919 287 GLU A CA  
2109 C C   . GLU B 72  ? 0.9624 1.0228 1.2005 -0.1950 -0.1213 -0.0364 287 GLU A C   
2110 O O   . GLU B 72  ? 0.9023 1.0058 1.1891 -0.1995 -0.1188 -0.0051 287 GLU A O   
2111 C CB  . GLU B 72  ? 1.0312 1.0127 1.2679 -0.2454 -0.1289 -0.1271 287 GLU A CB  
2112 C CG  . GLU B 72  ? 1.0269 1.0006 1.3339 -0.2934 -0.1320 -0.1502 287 GLU A CG  
2113 C CD  . GLU B 72  ? 1.1287 1.0021 1.4517 -0.3035 -0.1099 -0.1779 287 GLU A CD  
2114 O OE1 . GLU B 72  ? 1.1735 0.9902 1.4598 -0.2684 -0.0900 -0.1669 287 GLU A OE1 
2115 O OE2 . GLU B 72  ? 1.1236 0.9758 1.4995 -0.3468 -0.1119 -0.2111 287 GLU A OE2 
2116 N N   . LEU B 73  ? 0.9673 0.9760 1.1594 -0.1615 -0.1034 -0.0262 288 LEU A N   
2117 C CA  . LEU B 73  ? 0.9095 0.9090 1.1016 -0.1301 -0.0816 0.0178  288 LEU A CA  
2118 C C   . LEU B 73  ? 0.8863 0.9554 1.0875 -0.1149 -0.0875 0.0484  288 LEU A C   
2119 O O   . LEU B 73  ? 0.8712 0.9621 1.1099 -0.1089 -0.0742 0.0801  288 LEU A O   
2120 C CB  . LEU B 73  ? 0.8883 0.8382 1.0243 -0.0999 -0.0685 0.0170  288 LEU A CB  
2121 C CG  . LEU B 73  ? 0.9298 0.8121 1.0651 -0.1051 -0.0560 -0.0011 288 LEU A CG  
2122 C CD1 . LEU B 73  ? 0.8861 0.7336 0.9784 -0.0742 -0.0414 0.0083  288 LEU A CD1 
2123 C CD2 . LEU B 73  ? 0.9222 0.7885 1.1152 -0.1204 -0.0425 0.0177  288 LEU A CD2 
2124 N N   . TYR B 74  ? 0.8833 0.9905 1.0525 -0.1057 -0.1049 0.0425  289 TYR A N   
2125 C CA  . TYR B 74  ? 0.8596 1.0293 1.0414 -0.0847 -0.1074 0.0765  289 TYR A CA  
2126 C C   . TYR B 74  ? 0.8615 1.0964 1.1110 -0.1056 -0.1151 0.0914  289 TYR A C   
2127 O O   . TYR B 74  ? 0.8126 1.0845 1.0899 -0.0846 -0.1033 0.1272  289 TYR A O   
2128 C CB  . TYR B 74  ? 0.8639 1.0723 1.0082 -0.0742 -0.1267 0.0732  289 TYR A CB  
2129 C CG  . TYR B 74  ? 0.8073 1.0493 0.9544 -0.0380 -0.1182 0.1143  289 TYR A CG  
2130 C CD1 . TYR B 74  ? 0.7938 0.9822 0.9099 -0.0060 -0.0940 0.1280  289 TYR A CD1 
2131 C CD2 . TYR B 74  ? 0.8373 1.1655 1.0238 -0.0359 -0.1328 0.1388  289 TYR A CD2 
2132 C CE1 . TYR B 74  ? 0.7827 0.9908 0.9058 0.0275  -0.0820 0.1617  289 TYR A CE1 
2133 C CE2 . TYR B 74  ? 0.8359 1.1900 1.0315 0.0022  -0.1208 0.1787  289 TYR A CE2 
2134 C CZ  . TYR B 74  ? 0.8161 1.1041 0.9798 0.0339  -0.0938 0.1885  289 TYR A CZ  
2135 O OH  . TYR B 74  ? 0.8416 1.1459 1.0186 0.0721  -0.0782 0.2244  289 TYR A OH  
2136 N N   . ASP B 75  ? 0.8749 1.1246 1.1551 -0.1476 -0.1327 0.0625  290 ASP A N   
2137 C CA  . ASP B 75  ? 0.8706 1.1954 1.2207 -0.1737 -0.1444 0.0745  290 ASP A CA  
2138 C C   . ASP B 75  ? 0.8307 1.1371 1.2324 -0.1755 -0.1171 0.1028  290 ASP A C   
2139 O O   . ASP B 75  ? 0.7849 1.1605 1.2429 -0.1788 -0.1160 0.1317  290 ASP A O   
2140 C CB  . ASP B 75  ? 0.9100 1.2564 1.2781 -0.2237 -0.1724 0.0280  290 ASP A CB  
2141 C CG  . ASP B 75  ? 0.9862 1.4041 1.3197 -0.2242 -0.2050 0.0122  290 ASP A CG  
2142 O OD1 . ASP B 75  ? 0.9905 1.4294 1.2869 -0.1832 -0.2029 0.0418  290 ASP A OD1 
2143 O OD2 . ASP B 75  ? 1.0137 1.4687 1.3579 -0.2657 -0.2318 -0.0291 290 ASP A OD2 
2144 N N   . ARG B 76  ? 0.8212 1.0430 1.2058 -0.1715 -0.0940 0.0990  291 ARG A N   
2145 C CA  . ARG B 76  ? 0.7956 1.0022 1.2171 -0.1656 -0.0648 0.1333  291 ARG A CA  
2146 C C   . ARG B 76  ? 0.7926 1.0089 1.1866 -0.1184 -0.0430 0.1681  291 ARG A C   
2147 O O   . ARG B 76  ? 0.8616 1.1012 1.2907 -0.1103 -0.0209 0.2014  291 ARG A O   
2148 C CB  . ARG B 76  ? 0.8788 0.9982 1.2930 -0.1758 -0.0485 0.1217  291 ARG A CB  
2149 C CG  . ARG B 76  ? 0.9256 1.0227 1.3814 -0.2246 -0.0614 0.0870  291 ARG A CG  
2150 C CD  . ARG B 76  ? 0.9781 0.9959 1.4542 -0.2316 -0.0360 0.0948  291 ARG A CD  
2151 N NE  . ARG B 76  ? 1.0249 0.9734 1.4389 -0.2037 -0.0276 0.0822  291 ARG A NE  
2152 C CZ  . ARG B 76  ? 1.0539 0.9351 1.4638 -0.2174 -0.0270 0.0489  291 ARG A CZ  
2153 N NH1 . ARG B 76  ? 1.0780 0.9414 1.5391 -0.2607 -0.0335 0.0192  291 ARG A NH1 
2154 N NH2 . ARG B 76  ? 1.0707 0.9015 1.4279 -0.1874 -0.0180 0.0440  291 ARG A NH2 
2155 N N   . GLY B 77  ? 0.7846 0.9835 1.1184 -0.0883 -0.0465 0.1601  292 GLY A N   
2156 C CA  . GLY B 77  ? 0.7365 0.9397 1.0459 -0.0464 -0.0259 0.1849  292 GLY A CA  
2157 C C   . GLY B 77  ? 0.7360 0.8815 1.0155 -0.0303 0.0005  0.1908  292 GLY A C   
2158 O O   . GLY B 77  ? 0.7609 0.8591 1.0346 -0.0468 0.0022  0.1793  292 GLY A O   
2159 N N   . PRO B 78  ? 0.7291 0.8806 0.9896 0.0038  0.0225  0.2085  293 PRO A N   
2160 C CA  . PRO B 78  ? 0.6904 0.8876 0.9600 0.0306  0.0272  0.2235  293 PRO A CA  
2161 C C   . PRO B 78  ? 0.6600 0.8343 0.8862 0.0465  0.0147  0.2076  293 PRO A C   
2162 O O   . PRO B 78  ? 0.6856 0.8023 0.8610 0.0532  0.0183  0.1893  293 PRO A O   
2163 C CB  . PRO B 78  ? 0.6980 0.8911 0.9561 0.0590  0.0610  0.2395  293 PRO A CB  
2164 C CG  . PRO B 78  ? 0.6875 0.8194 0.8982 0.0553  0.0669  0.2241  293 PRO A CG  
2165 C CD  . PRO B 78  ? 0.6830 0.7982 0.9140 0.0193  0.0472  0.2154  293 PRO A CD  
2166 N N   . PRO B 79  ? 0.5533 1.0371 0.6839 0.0777  0.0219  0.1351  294 PRO A N   
2167 C CA  . PRO B 79  ? 0.5611 1.0188 0.6924 0.1121  0.0207  0.1453  294 PRO A CA  
2168 C C   . PRO B 79  ? 0.5985 0.9578 0.7161 0.1459  0.0364  0.1386  294 PRO A C   
2169 O O   . PRO B 79  ? 0.6649 0.9538 0.7642 0.1450  0.0318  0.1297  294 PRO A O   
2170 C CB  . PRO B 79  ? 0.5508 1.1197 0.7141 0.1460  0.0248  0.1747  294 PRO A CB  
2171 C CG  . PRO B 79  ? 0.4993 1.1687 0.6806 0.1180  0.0224  0.1771  294 PRO A CG  
2172 C CD  . PRO B 79  ? 0.4993 1.1079 0.6588 0.0757  0.0230  0.1518  294 PRO A CD  
2173 N N   . HIS B 80  ? 0.6102 0.9651 0.7342 0.1723  0.0564  0.1407  295 HIS A N   
2174 C CA  . HIS B 80  ? 0.6255 0.8927 0.7332 0.2019  0.0760  0.1327  295 HIS A CA  
2175 C C   . HIS B 80  ? 0.6476 0.8253 0.7264 0.1738  0.0688  0.1071  295 HIS A C   
2176 O O   . HIS B 80  ? 0.6793 0.7871 0.7412 0.1895  0.0833  0.0969  295 HIS A O   
2177 C CB  . HIS B 80  ? 0.6925 0.9724 0.8068 0.2250  0.0997  0.1341  295 HIS A CB  
2178 C CG  . HIS B 80  ? 0.7012 0.9764 0.8066 0.1895  0.0955  0.1161  295 HIS A CG  
2179 N ND1 . HIS B 80  ? 0.7105 0.9051 0.7885 0.1752  0.0988  0.0936  295 HIS A ND1 
2180 C CD2 . HIS B 80  ? 0.7282 1.0720 0.8461 0.1640  0.0890  0.1185  295 HIS A CD2 
2181 C CE1 . HIS B 80  ? 0.7104 0.9213 0.7838 0.1469  0.0945  0.0856  295 HIS A CE1 
2182 N NE2 . HIS B 80  ? 0.7967 1.0922 0.8928 0.1381  0.0896  0.0996  295 HIS A NE2 
2183 N N   . ALA B 81  ? 0.6814 0.8599 0.7516 0.1331  0.0493  0.0967  296 ALA A N   
2184 C CA  . ALA B 81  ? 0.7074 0.8118 0.7516 0.1126  0.0429  0.0769  296 ALA A CA  
2185 C C   . ALA B 81  ? 0.7108 0.7789 0.7451 0.1092  0.0317  0.0741  296 ALA A C   
2186 O O   . ALA B 81  ? 0.6844 0.6983 0.6991 0.0967  0.0271  0.0596  296 ALA A O   
2187 C CB  . ALA B 81  ? 0.6430 0.7533 0.6762 0.0759  0.0333  0.0694  296 ALA A CB  
2188 N N   . PHE B 82  ? 0.6405 0.7436 0.6876 0.1212  0.0275  0.0889  297 PHE A N   
2189 C CA  . PHE B 82  ? 0.7190 0.8020 0.7567 0.1109  0.0144  0.0869  297 PHE A CA  
2190 C C   . PHE B 82  ? 0.7224 0.7669 0.7566 0.1404  0.0249  0.0921  297 PHE A C   
2191 O O   . PHE B 82  ? 0.7311 0.8035 0.7777 0.1711  0.0358  0.1111  297 PHE A O   
2192 C CB  . PHE B 82  ? 0.6757 0.8295 0.7243 0.0950  0.0008  0.0985  297 PHE A CB  
2193 C CG  . PHE B 82  ? 0.6997 0.8692 0.7392 0.0536  -0.0084 0.0878  297 PHE A CG  
2194 C CD1 . PHE B 82  ? 0.6771 0.8834 0.7252 0.0449  -0.0026 0.0892  297 PHE A CD1 
2195 C CD2 . PHE B 82  ? 0.6829 0.8217 0.7007 0.0231  -0.0191 0.0756  297 PHE A CD2 
2196 C CE1 . PHE B 82  ? 0.7070 0.9171 0.7406 0.0038  -0.0071 0.0794  297 PHE A CE1 
2197 C CE2 . PHE B 82  ? 0.7361 0.8729 0.7374 -0.0153 -0.0216 0.0654  297 PHE A CE2 
2198 C CZ  . PHE B 82  ? 0.7294 0.8999 0.7376 -0.0264 -0.0154 0.0675  297 PHE A CZ  
2199 N N   . PHE B 83  ? 0.6553 0.6378 0.6709 0.1315  0.0232  0.0767  298 PHE A N   
2200 C CA  . PHE B 83  ? 0.6918 0.6283 0.6979 0.1506  0.0354  0.0774  298 PHE A CA  
2201 C C   . PHE B 83  ? 0.7110 0.6315 0.7077 0.1372  0.0223  0.0741  298 PHE A C   
2202 O O   . PHE B 83  ? 0.6904 0.6082 0.6804 0.1122  0.0076  0.0623  298 PHE A O   
2203 C CB  . PHE B 83  ? 0.6906 0.5702 0.6807 0.1500  0.0506  0.0589  298 PHE A CB  
2204 C CG  . PHE B 83  ? 0.7905 0.6756 0.7845 0.1654  0.0687  0.0600  298 PHE A CG  
2205 C CD1 . PHE B 83  ? 0.7467 0.6796 0.7539 0.1585  0.0622  0.0632  298 PHE A CD1 
2206 C CD2 . PHE B 83  ? 0.8066 0.6469 0.7883 0.1878  0.0961  0.0591  298 PHE A CD2 
2207 C CE1 . PHE B 83  ? 0.7538 0.6953 0.7649 0.1742  0.0805  0.0645  298 PHE A CE1 
2208 C CE2 . PHE B 83  ? 0.8019 0.6429 0.7841 0.2047  0.1168  0.0593  298 PHE A CE2 
2209 C CZ  . PHE B 83  ? 0.7935 0.6895 0.7924 0.1990  0.1079  0.0624  298 PHE A CZ  
2210 N N   . LEU B 84  ? 0.7612 0.6669 0.7546 0.1561  0.0308  0.0857  299 LEU A N   
2211 C CA  . LEU B 84  ? 0.7275 0.6113 0.7093 0.1464  0.0231  0.0824  299 LEU A CA  
2212 C C   . LEU B 84  ? 0.7495 0.5677 0.7136 0.1498  0.0407  0.0708  299 LEU A C   
2213 O O   . LEU B 84  ? 0.8307 0.6206 0.7887 0.1719  0.0631  0.0789  299 LEU A O   
2214 C CB  . LEU B 84  ? 0.7451 0.6682 0.7330 0.1617  0.0194  0.1064  299 LEU A CB  
2215 C CG  . LEU B 84  ? 0.7486 0.6478 0.7224 0.1577  0.0165  0.1075  299 LEU A CG  
2216 C CD1 . LEU B 84  ? 0.6811 0.5880 0.6493 0.1265  -0.0031 0.0913  299 LEU A CD1 
2217 C CD2 . LEU B 84  ? 0.7575 0.6932 0.7347 0.1826  0.0190  0.1370  299 LEU A CD2 
2218 N N   . VAL B 85  ? 0.7519 0.5466 0.7053 0.1274  0.0330  0.0520  300 VAL A N   
2219 C CA  . VAL B 85  ? 0.7814 0.5262 0.7169 0.1212  0.0472  0.0386  300 VAL A CA  
2220 C C   . VAL B 85  ? 0.7785 0.5196 0.7079 0.1157  0.0407  0.0426  300 VAL A C   
2221 O O   . VAL B 85  ? 0.7149 0.4806 0.6484 0.1030  0.0220  0.0387  300 VAL A O   
2222 C CB  . VAL B 85  ? 0.7785 0.5156 0.7079 0.1000  0.0438  0.0148  300 VAL A CB  
2223 C CG1 . VAL B 85  ? 0.7752 0.4775 0.6868 0.0856  0.0558  -0.0007 300 VAL A CG1 
2224 C CG2 . VAL B 85  ? 0.7988 0.5372 0.7301 0.1042  0.0528  0.0100  300 VAL A CG2 
2225 N N   . LYS B 86  ? 0.7703 0.4756 0.6860 0.1255  0.0588  0.0504  301 LYS A N   
2226 C CA  . LYS B 86  ? 0.7835 0.4788 0.6890 0.1167  0.0563  0.0513  301 LYS A CA  
2227 C C   . LYS B 86  ? 0.8041 0.4631 0.6936 0.0935  0.0674  0.0275  301 LYS A C   
2228 O O   . LYS B 86  ? 0.8460 0.4631 0.7205 0.0914  0.0902  0.0194  301 LYS A O   
2229 C CB  . LYS B 86  ? 0.8093 0.4879 0.7054 0.1401  0.0710  0.0770  301 LYS A CB  
2230 C CG  . LYS B 86  ? 0.8618 0.5685 0.7575 0.1369  0.0559  0.0881  301 LYS A CG  
2231 C CD  . LYS B 86  ? 0.8682 0.5370 0.7442 0.1199  0.0652  0.0782  301 LYS A CD  
2232 C CE  . LYS B 86  ? 0.8903 0.5863 0.7628 0.1183  0.0527  0.0904  301 LYS A CE  
2233 N NZ  . LYS B 86  ? 0.9156 0.6198 0.7813 0.1466  0.0602  0.1247  301 LYS A NZ  
2234 N N   . PHE B 87  ? 0.8122 0.4911 0.7033 0.0748  0.0528  0.0151  302 PHE A N   
2235 C CA  . PHE B 87  ? 0.8100 0.4769 0.6899 0.0506  0.0601  -0.0070 302 PHE A CA  
2236 C C   . PHE B 87  ? 0.8622 0.5135 0.7290 0.0415  0.0673  -0.0048 302 PHE A C   
2237 O O   . PHE B 87  ? 0.8244 0.4949 0.6963 0.0491  0.0550  0.0074  302 PHE A O   
2238 C CB  . PHE B 87  ? 0.7599 0.4691 0.6517 0.0405  0.0409  -0.0207 302 PHE A CB  
2239 C CG  . PHE B 87  ? 0.7667 0.4849 0.6624 0.0390  0.0406  -0.0300 302 PHE A CG  
2240 C CD1 . PHE B 87  ? 0.8477 0.5380 0.7302 0.0298  0.0602  -0.0409 302 PHE A CD1 
2241 C CD2 . PHE B 87  ? 0.7638 0.5134 0.6714 0.0451  0.0234  -0.0285 302 PHE A CD2 
2242 C CE1 . PHE B 87  ? 0.8015 0.5038 0.6854 0.0270  0.0602  -0.0503 302 PHE A CE1 
2243 C CE2 . PHE B 87  ? 0.7700 0.5294 0.6790 0.0441  0.0234  -0.0349 302 PHE A CE2 
2244 C CZ  . PHE B 87  ? 0.7793 0.5194 0.6778 0.0350  0.0405  -0.0460 302 PHE A CZ  
2245 N N   . TRP B 88  ? 0.8302 0.4452 0.6765 0.0220  0.0893  -0.0177 303 TRP A N   
2246 C CA  . TRP B 88  ? 0.8684 0.4755 0.7013 0.0036  0.0966  -0.0220 303 TRP A CA  
2247 C C   . TRP B 88  ? 0.8522 0.4959 0.6878 -0.0262 0.0921  -0.0485 303 TRP A C   
2248 O O   . TRP B 88  ? 0.8466 0.4732 0.6671 -0.0500 0.1090  -0.0670 303 TRP A O   
2249 C CB  . TRP B 88  ? 0.9008 0.4381 0.7033 0.0007  0.1287  -0.0150 303 TRP A CB  
2250 C CG  . TRP B 88  ? 0.9392 0.4556 0.7395 0.0355  0.1320  0.0174  303 TRP A CG  
2251 C CD1 . TRP B 88  ? 0.9153 0.4343 0.7103 0.0442  0.1296  0.0365  303 TRP A CD1 
2252 C CD2 . TRP B 88  ? 1.0205 0.5218 0.8248 0.0679  0.1382  0.0363  303 TRP A CD2 
2253 N NE1 . TRP B 88  ? 0.9606 0.4715 0.7554 0.0801  0.1329  0.0674  303 TRP A NE1 
2254 C CE2 . TRP B 88  ? 1.0090 0.5113 0.8110 0.0964  0.1383  0.0684  303 TRP A CE2 
2255 C CE3 . TRP B 88  ? 0.9868 0.4790 0.7957 0.0761  0.1447  0.0298  303 TRP A CE3 
2256 C CZ2 . TRP B 88  ? 1.1081 0.6105 0.9151 0.1349  0.1442  0.0958  303 TRP A CZ2 
2257 C CZ3 . TRP B 88  ? 1.0009 0.4865 0.8143 0.1139  0.1519  0.0555  303 TRP A CZ3 
2258 C CH2 . TRP B 88  ? 1.0714 0.5656 0.8851 0.1438  0.1514  0.0888  303 TRP A CH2 
2259 N N   . ALA B 89  ? 0.8115 0.5084 0.6641 -0.0245 0.0709  -0.0500 304 ALA A N   
2260 C CA  . ALA B 89  ? 0.7847 0.5352 0.6464 -0.0408 0.0624  -0.0688 304 ALA A CA  
2261 C C   . ALA B 89  ? 0.8474 0.6120 0.6975 -0.0719 0.0749  -0.0835 304 ALA A C   
2262 O O   . ALA B 89  ? 0.9065 0.6541 0.7481 -0.0751 0.0814  -0.0764 304 ALA A O   
2263 C CB  . ALA B 89  ? 0.7372 0.5326 0.6183 -0.0198 0.0394  -0.0618 304 ALA A CB  
2264 N N   . ASP B 90  ? 0.8184 0.6223 0.6676 -0.0972 0.0778  -0.1039 305 ASP A N   
2265 C CA  . ASP B 90  ? 0.8558 0.6946 0.6967 -0.1328 0.0880  -0.1209 305 ASP A CA  
2266 C C   . ASP B 90  ? 0.8630 0.7873 0.7287 -0.1197 0.0677  -0.1192 305 ASP A C   
2267 O O   . ASP B 90  ? 0.8585 0.8425 0.7379 -0.1139 0.0555  -0.1240 305 ASP A O   
2268 C CB  . ASP B 90  ? 0.8663 0.7100 0.6895 -0.1724 0.1042  -0.1456 305 ASP A CB  
2269 C CG  . ASP B 90  ? 0.8979 0.7726 0.7065 -0.2199 0.1197  -0.1660 305 ASP A CG  
2270 O OD1 . ASP B 90  ? 0.9303 0.8527 0.7525 -0.2169 0.1113  -0.1610 305 ASP A OD1 
2271 O OD2 . ASP B 90  ? 0.9273 0.7801 0.7086 -0.2627 0.1419  -0.1886 305 ASP A OD2 
2272 N N   . LEU B 91  ? 0.8281 0.7580 0.6972 -0.1116 0.0657  -0.1106 306 LEU A N   
2273 C CA  . LEU B 91  ? 0.8618 0.8640 0.7506 -0.0942 0.0516  -0.1078 306 LEU A CA  
2274 C C   . LEU B 91  ? 0.9176 0.9859 0.8071 -0.1258 0.0603  -0.1227 306 LEU A C   
2275 O O   . LEU B 91  ? 0.9064 1.0238 0.8080 -0.1123 0.0553  -0.1185 306 LEU A O   
2276 C CB  . LEU B 91  ? 0.8064 0.7797 0.6973 -0.0648 0.0447  -0.0910 306 LEU A CB  
2277 C CG  . LEU B 91  ? 0.7811 0.7004 0.6713 -0.0374 0.0356  -0.0760 306 LEU A CG  
2278 C CD1 . LEU B 91  ? 0.8057 0.7231 0.6976 -0.0137 0.0273  -0.0655 306 LEU A CD1 
2279 C CD2 . LEU B 91  ? 0.8007 0.7332 0.7004 -0.0241 0.0260  -0.0764 306 LEU A CD2 
2280 N N   . ASN B 92  ? 1.0488 1.1201 0.9233 -0.1696 0.0755  -0.1414 307 ASN A N   
2281 C CA  . ASN B 92  ? 1.0554 1.1887 0.9259 -0.2115 0.0872  -0.1587 307 ASN A CA  
2282 C C   . ASN B 92  ? 1.0142 1.2426 0.8952 -0.2307 0.0811  -0.1747 307 ASN A C   
2283 O O   . ASN B 92  ? 1.0061 1.2148 0.8688 -0.2643 0.0916  -0.1916 307 ASN A O   
2284 C CB  . ASN B 92  ? 1.1012 1.1561 0.9370 -0.2556 0.1149  -0.1696 307 ASN A CB  
2285 C CG  . ASN B 92  ? 1.1655 1.2420 0.9947 -0.2802 0.1270  -0.1728 307 ASN A CG  
2286 O OD1 . ASN B 92  ? 1.2156 1.2852 1.0536 -0.2510 0.1200  -0.1558 307 ASN A OD1 
2287 N ND2 . ASN B 92  ? 1.1888 1.2918 0.9995 -0.3385 0.1468  -0.1964 307 ASN A ND2 
2288 N N   . TRP B 93  ? 0.8546 1.1879 0.7627 -0.2079 0.0658  -0.1686 308 TRP A N   
2289 C CA  . TRP B 93  ? 0.7774 1.2223 0.6978 -0.2212 0.0580  -0.1791 308 TRP A CA  
2290 C C   . TRP B 93  ? 0.7145 1.2902 0.6583 -0.2177 0.0530  -0.1778 308 TRP A C   
2291 O O   . TRP B 93  ? 0.7532 1.3268 0.7045 -0.1997 0.0554  -0.1683 308 TRP A O   
2292 C CB  . TRP B 93  ? 0.7171 1.1615 0.6484 -0.1770 0.0406  -0.1641 308 TRP A CB  
2293 C CG  . TRP B 93  ? 0.6719 1.1411 0.6253 -0.1137 0.0257  -0.1381 308 TRP A CG  
2294 C CD1 . TRP B 93  ? 0.6087 1.1863 0.5827 -0.0831 0.0151  -0.1268 308 TRP A CD1 
2295 C CD2 . TRP B 93  ? 0.7020 1.0826 0.6540 -0.0733 0.0228  -0.1203 308 TRP A CD2 
2296 N NE1 . TRP B 93  ? 0.6530 1.2011 0.6348 -0.0254 0.0095  -0.1036 308 TRP A NE1 
2297 C CE2 . TRP B 93  ? 0.6807 1.1099 0.6486 -0.0227 0.0136  -0.1016 308 TRP A CE2 
2298 C CE3 . TRP B 93  ? 0.7643 1.0338 0.7008 -0.0754 0.0286  -0.1177 308 TRP A CE3 
2299 C CZ2 . TRP B 93  ? 0.6949 1.0566 0.6596 0.0186  0.0118  -0.0854 308 TRP A CZ2 
2300 C CZ3 . TRP B 93  ? 0.7461 0.9652 0.6842 -0.0349 0.0227  -0.1004 308 TRP A CZ3 
2301 C CH2 . TRP B 93  ? 0.7365 0.9977 0.6866 0.0081  0.0152  -0.0868 308 TRP A CH2 
2302 N N   . SER B 108 ? 0.8544 1.7361 0.9005 0.1334  0.0186  -0.0457 323 SER A N   
2303 C CA  . SER B 108 ? 0.8792 1.7546 0.9234 0.2042  0.0188  -0.0171 323 SER A CA  
2304 C C   . SER B 108 ? 0.9001 1.9088 0.9604 0.2223  0.0099  -0.0026 323 SER A C   
2305 O O   . SER B 108 ? 0.8684 2.0205 0.9507 0.2182  0.0099  -0.0021 323 SER A O   
2306 C CB  . SER B 108 ? 0.8296 1.7017 0.8741 0.2561  0.0340  -0.0028 323 SER A CB  
2307 N N   . GLY B 109 ? 0.8043 1.7745 0.8535 0.2412  0.0024  0.0099  324 GLY A N   
2308 C CA  . GLY B 109 ? 0.7168 1.8101 0.7774 0.2716  -0.0050 0.0310  324 GLY A CA  
2309 C C   . GLY B 109 ? 0.7913 1.8677 0.8407 0.2569  -0.0173 0.0317  324 GLY A C   
2310 O O   . GLY B 109 ? 0.7410 1.8936 0.7930 0.2983  -0.0218 0.0575  324 GLY A O   
2311 N N   . GLY B 110 ? 0.7602 1.7411 0.7961 0.2017  -0.0214 0.0058  325 GLY A N   
2312 C CA  . GLY B 110 ? 0.7285 1.7069 0.7547 0.1775  -0.0316 0.0006  325 GLY A CA  
2313 C C   . GLY B 110 ? 0.6754 1.5336 0.6817 0.2138  -0.0310 0.0183  325 GLY A C   
2314 O O   . GLY B 110 ? 0.7016 1.4744 0.6986 0.2575  -0.0217 0.0347  325 GLY A O   
2315 N N   . PHE B 111 ? 0.6991 1.5513 0.6959 0.1903  -0.0392 0.0124  326 PHE A N   
2316 C CA  . PHE B 111 ? 0.6363 1.3899 0.6142 0.2163  -0.0392 0.0276  326 PHE A CA  
2317 C C   . PHE B 111 ? 0.6650 1.2917 0.6316 0.1743  -0.0370 0.0037  326 PHE A C   
2318 O O   . PHE B 111 ? 0.6777 1.3130 0.6440 0.1200  -0.0393 -0.0229 326 PHE A O   
2319 C CB  . PHE B 111 ? 0.6206 1.4549 0.5945 0.2197  -0.0488 0.0383  326 PHE A CB  
2320 C CG  . PHE B 111 ? 0.6001 1.3367 0.5538 0.2252  -0.0492 0.0447  326 PHE A CG  
2321 C CD1 . PHE B 111 ? 0.5984 1.2835 0.5374 0.2833  -0.0432 0.0777  326 PHE A CD1 
2322 C CD2 . PHE B 111 ? 0.6366 1.3290 0.5829 0.1720  -0.0523 0.0176  326 PHE A CD2 
2323 C CE1 . PHE B 111 ? 0.6504 1.2480 0.5699 0.2837  -0.0424 0.0829  326 PHE A CE1 
2324 C CE2 . PHE B 111 ? 0.6746 1.2846 0.6042 0.1771  -0.0520 0.0236  326 PHE A CE2 
2325 C CZ  . PHE B 111 ? 0.6404 1.2067 0.5577 0.2308  -0.0480 0.0559  326 PHE A CZ  
2326 N N   . TYR B 112 ? 0.6256 1.1366 0.5804 0.1991  -0.0304 0.0133  327 TYR A N   
2327 C CA  . TYR B 112 ? 0.6156 1.0151 0.5617 0.1679  -0.0284 -0.0037 327 TYR A CA  
2328 C C   . TYR B 112 ? 0.6890 1.0303 0.6206 0.1767  -0.0305 0.0058  327 TYR A C   
2329 O O   . TYR B 112 ? 0.7100 1.0197 0.6296 0.2185  -0.0265 0.0290  327 TYR A O   
2330 C CB  . TYR B 112 ? 0.6968 1.0193 0.6386 0.1826  -0.0202 -0.0016 327 TYR A CB  
2331 C CG  . TYR B 112 ? 0.6702 1.0421 0.6247 0.1736  -0.0163 -0.0109 327 TYR A CG  
2332 C CD1 . TYR B 112 ? 0.6724 1.1347 0.6370 0.2060  -0.0138 0.0026  327 TYR A CD1 
2333 C CD2 . TYR B 112 ? 0.6709 1.0040 0.6266 0.1346  -0.0138 -0.0310 327 TYR A CD2 
2334 C CE1 . TYR B 112 ? 0.6697 1.1846 0.6471 0.1969  -0.0093 -0.0060 327 TYR A CE1 
2335 C CE2 . TYR B 112 ? 0.6205 0.9984 0.5856 0.1246  -0.0088 -0.0389 327 TYR A CE2 
2336 C CZ  . TYR B 112 ? 0.6450 1.1161 0.6220 0.1537  -0.0070 -0.0278 327 TYR A CZ  
2337 O OH  . TYR B 112 ? 0.7313 1.2564 0.7192 0.1430  -0.0012 -0.0356 327 TYR A OH  
2338 N N   . GLY B 113 ? 0.7029 1.0260 0.6322 0.1376  -0.0336 -0.0121 328 GLY A N   
2339 C CA  . GLY B 113 ? 0.6776 0.9609 0.5949 0.1419  -0.0354 -0.0049 328 GLY A CA  
2340 C C   . GLY B 113 ? 0.6612 0.8691 0.5753 0.1078  -0.0325 -0.0232 328 GLY A C   
2341 O O   . GLY B 113 ? 0.6298 0.8237 0.5486 0.0784  -0.0286 -0.0418 328 GLY A O   
2342 N N   . VAL B 114 ? 0.6499 0.8086 0.5542 0.1151  -0.0324 -0.0151 329 VAL A N   
2343 C CA  . VAL B 114 ? 0.7014 0.8024 0.6031 0.0893  -0.0288 -0.0283 329 VAL A CA  
2344 C C   . VAL B 114 ? 0.6959 0.8227 0.5894 0.0825  -0.0301 -0.0292 329 VAL A C   
2345 O O   . VAL B 114 ? 0.7211 0.8748 0.6076 0.1072  -0.0340 -0.0107 329 VAL A O   
2346 C CB  . VAL B 114 ? 0.7119 0.7319 0.6104 0.1016  -0.0265 -0.0185 329 VAL A CB  
2347 C CG1 . VAL B 114 ? 0.7398 0.7349 0.6434 0.1029  -0.0247 -0.0207 329 VAL A CG1 
2348 C CG2 . VAL B 114 ? 0.7950 0.8013 0.6812 0.1318  -0.0268 0.0033  329 VAL A CG2 
2349 N N   . SER B 115 ? 0.7433 0.8595 0.6340 0.0506  -0.0243 -0.0498 330 SER A N   
2350 C CA  . SER B 115 ? 0.7098 0.8430 0.5896 0.0404  -0.0228 -0.0543 330 SER A CA  
2351 C C   . SER B 115 ? 0.7085 0.7696 0.5860 0.0318  -0.0138 -0.0601 330 SER A C   
2352 O O   . SER B 115 ? 0.7094 0.7311 0.5888 0.0150  -0.0044 -0.0741 330 SER A O   
2353 C CB  . SER B 115 ? 0.6920 0.8921 0.5646 0.0072  -0.0202 -0.0769 330 SER A CB  
2354 O OG  . SER B 115 ? 0.6775 0.9699 0.5515 0.0198  -0.0308 -0.0659 330 SER A OG  
2355 N N   . SER B 116 ? 0.6899 0.7352 0.5625 0.0458  -0.0151 -0.0469 331 SER A N   
2356 C CA  . SER B 116 ? 0.7324 0.7274 0.6041 0.0397  -0.0063 -0.0507 331 SER A CA  
2357 C C   . SER B 116 ? 0.7731 0.7936 0.6313 0.0286  -0.0017 -0.0582 331 SER A C   
2358 O O   . SER B 116 ? 0.7521 0.8224 0.6016 0.0353  -0.0089 -0.0496 331 SER A O   
2359 C CB  . SER B 116 ? 0.7605 0.7142 0.6372 0.0600  -0.0095 -0.0303 331 SER A CB  
2360 O OG  . SER B 116 ? 0.8087 0.7263 0.6960 0.0621  -0.0093 -0.0293 331 SER A OG  
2361 N N   . GLN B 117 ? 0.7535 0.7408 0.6081 0.0144  0.0121  -0.0726 332 GLN A N   
2362 C CA  . GLN B 117 ? 0.7855 0.7907 0.6251 0.0041  0.0191  -0.0809 332 GLN A CA  
2363 C C   . GLN B 117 ? 0.7950 0.7495 0.6379 0.0078  0.0329  -0.0818 332 GLN A C   
2364 O O   . GLN B 117 ? 0.7983 0.7124 0.6430 0.0020  0.0470  -0.0932 332 GLN A O   
2365 C CB  . GLN B 117 ? 0.7636 0.8027 0.5852 -0.0274 0.0276  -0.1085 332 GLN A CB  
2366 C CG  . GLN B 117 ? 0.8338 0.9158 0.6366 -0.0373 0.0289  -0.1138 332 GLN A CG  
2367 C CD  . GLN B 117 ? 0.8630 0.9877 0.6437 -0.0755 0.0371  -0.1441 332 GLN A CD  
2368 O OE1 . GLN B 117 ? 0.8830 1.0600 0.6649 -0.0874 0.0282  -0.1488 332 GLN A OE1 
2369 N NE2 . GLN B 117 ? 0.8812 0.9893 0.6395 -0.0971 0.0554  -0.1660 332 GLN A NE2 
2370 N N   . TYR B 118 ? 0.8045 0.7631 0.6471 0.0191  0.0306  -0.0675 333 TYR A N   
2371 C CA  . TYR B 118 ? 0.8137 0.7417 0.6609 0.0235  0.0438  -0.0668 333 TYR A CA  
2372 C C   . TYR B 118 ? 0.8619 0.8105 0.6905 0.0126  0.0540  -0.0779 333 TYR A C   
2373 O O   . TYR B 118 ? 0.8769 0.8685 0.6900 0.0041  0.0466  -0.0800 333 TYR A O   
2374 C CB  . TYR B 118 ? 0.8006 0.7185 0.6621 0.0401  0.0353  -0.0427 333 TYR A CB  
2375 C CG  . TYR B 118 ? 0.7985 0.6993 0.6735 0.0485  0.0247  -0.0320 333 TYR A CG  
2376 C CD1 . TYR B 118 ? 0.7708 0.6836 0.6410 0.0539  0.0116  -0.0228 333 TYR A CD1 
2377 C CD2 . TYR B 118 ? 0.7890 0.6647 0.6801 0.0536  0.0292  -0.0296 333 TYR A CD2 
2378 C CE1 . TYR B 118 ? 0.8211 0.7144 0.7003 0.0609  0.0045  -0.0151 333 TYR A CE1 
2379 C CE2 . TYR B 118 ? 0.7753 0.6388 0.6758 0.0585  0.0197  -0.0210 333 TYR A CE2 
2380 C CZ  . TYR B 118 ? 0.8084 0.6773 0.7021 0.0604  0.0080  -0.0157 333 TYR A CZ  
2381 O OH  . TYR B 118 ? 0.8462 0.6993 0.7462 0.0643  0.0013  -0.0096 333 TYR A OH  
2382 N N   . GLU B 119 ? 0.8577 0.7806 0.6871 0.0149  0.0719  -0.0838 334 GLU A N   
2383 C CA  . GLU B 119 ? 0.8865 0.8255 0.6972 0.0055  0.0841  -0.0947 334 GLU A CA  
2384 C C   . GLU B 119 ? 0.8989 0.8246 0.7224 0.0210  0.0943  -0.0827 334 GLU A C   
2385 O O   . GLU B 119 ? 0.8273 0.7332 0.6732 0.0365  0.0942  -0.0699 334 GLU A O   
2386 C CB  . GLU B 119 ? 0.9219 0.8469 0.7078 -0.0172 0.1047  -0.1270 334 GLU A CB  
2387 C CG  . GLU B 119 ? 0.9598 0.8264 0.7451 -0.0104 0.1321  -0.1381 334 GLU A CG  
2388 C CD  . GLU B 119 ? 1.0737 0.9148 0.8235 -0.0378 0.1583  -0.1730 334 GLU A CD  
2389 O OE1 . GLU B 119 ? 1.0998 0.9823 0.8265 -0.0649 0.1541  -0.1896 334 GLU A OE1 
2390 O OE2 . GLU B 119 ? 1.1500 0.9293 0.8914 -0.0332 0.1849  -0.1835 334 GLU A OE2 
2391 N N   . SER B 120 ? 0.9198 0.8667 0.7291 0.0158  0.1021  -0.0860 335 SER A N   
2392 C CA  . SER B 120 ? 0.8884 0.8373 0.7095 0.0281  0.1113  -0.0738 335 SER A CA  
2393 C C   . SER B 120 ? 0.8573 0.8251 0.6555 0.0182  0.1264  -0.0862 335 SER A C   
2394 O O   . SER B 120 ? 0.8403 0.8285 0.6124 0.0005  0.1244  -0.1000 335 SER A O   
2395 C CB  . SER B 120 ? 0.8304 0.7953 0.6666 0.0346  0.0923  -0.0461 335 SER A CB  
2396 O OG  . SER B 120 ? 0.8690 0.8450 0.7167 0.0405  0.1020  -0.0360 335 SER A OG  
2397 N N   . LEU B 121 ? 0.8114 0.7805 0.6196 0.0294  0.1416  -0.0807 336 LEU A N   
2398 C CA  . LEU B 121 ? 0.8427 0.8331 0.6314 0.0222  0.1563  -0.0888 336 LEU A CA  
2399 C C   . LEU B 121 ? 0.8433 0.8704 0.6321 0.0188  0.1417  -0.0659 336 LEU A C   
2400 O O   . LEU B 121 ? 0.8393 0.8898 0.6069 0.0096  0.1499  -0.0706 336 LEU A O   
2401 C CB  . LEU B 121 ? 0.7507 0.7251 0.5476 0.0386  0.1858  -0.0959 336 LEU A CB  
2402 C CG  . LEU B 121 ? 0.8779 0.8009 0.6613 0.0432  0.2114  -0.1204 336 LEU A CG  
2403 C CD1 . LEU B 121 ? 0.8121 0.7177 0.6110 0.0733  0.2398  -0.1157 336 LEU A CD1 
2404 C CD2 . LEU B 121 ? 0.8479 0.7598 0.5874 0.0163  0.2271  -0.1534 336 LEU A CD2 
2405 N N   . GLU B 122 ? 0.8199 0.8476 0.6270 0.0240  0.1231  -0.0420 337 GLU A N   
2406 C CA  . GLU B 122 ? 0.8274 0.8744 0.6275 0.0185  0.1133  -0.0195 337 GLU A CA  
2407 C C   . GLU B 122 ? 0.8501 0.8962 0.6320 0.0161  0.0941  -0.0091 337 GLU A C   
2408 O O   . GLU B 122 ? 0.8282 0.8604 0.6159 0.0199  0.0838  -0.0139 337 GLU A O   
2409 C CB  . GLU B 122 ? 0.8771 0.9208 0.7020 0.0215  0.1095  -0.0004 337 GLU A CB  
2410 C CG  . GLU B 122 ? 0.9016 0.9672 0.7472 0.0257  0.1265  -0.0007 337 GLU A CG  
2411 C CD  . GLU B 122 ? 0.9430 1.0071 0.8208 0.0335  0.1212  0.0076  337 GLU A CD  
2412 O OE1 . GLU B 122 ? 0.9003 0.9669 0.7827 0.0217  0.1098  0.0235  337 GLU A OE1 
2413 O OE2 . GLU B 122 ? 0.9401 0.9971 0.8342 0.0503  0.1295  -0.0018 337 GLU A OE2 
2414 N N   . HIS B 123 ? 0.8406 0.9028 0.6000 0.0123  0.0910  0.0078  338 HIS A N   
2415 C CA  . HIS B 123 ? 0.8285 0.8890 0.5698 0.0183  0.0758  0.0272  338 HIS A CA  
2416 C C   . HIS B 123 ? 0.8329 0.8569 0.5821 0.0219  0.0716  0.0490  338 HIS A C   
2417 O O   . HIS B 123 ? 0.8037 0.8211 0.5507 0.0133  0.0804  0.0603  338 HIS A O   
2418 C CB  . HIS B 123 ? 0.8283 0.9196 0.5361 0.0165  0.0773  0.0396  338 HIS A CB  
2419 C CG  . HIS B 123 ? 0.8517 0.9455 0.5388 0.0310  0.0643  0.0642  338 HIS A CG  
2420 N ND1 . HIS B 123 ? 0.8497 0.9879 0.5224 0.0360  0.0545  0.0606  338 HIS A ND1 
2421 C CD2 . HIS B 123 ? 0.8479 0.9056 0.5245 0.0431  0.0621  0.0932  338 HIS A CD2 
2422 C CE1 . HIS B 123 ? 0.8507 0.9863 0.5080 0.0567  0.0460  0.0899  338 HIS A CE1 
2423 N NE2 . HIS B 123 ? 0.8644 0.9430 0.5211 0.0621  0.0522  0.1097  338 HIS A NE2 
2424 N N   . MET B 124 ? 0.8556 0.8573 0.6110 0.0312  0.0601  0.0532  339 MET A N   
2425 C CA  . MET B 124 ? 0.8172 0.7775 0.5762 0.0321  0.0575  0.0685  339 MET A CA  
2426 C C   . MET B 124 ? 0.8331 0.7767 0.5757 0.0491  0.0478  0.0822  339 MET A C   
2427 O O   . MET B 124 ? 0.8530 0.8280 0.5901 0.0596  0.0405  0.0781  339 MET A O   
2428 C CB  . MET B 124 ? 0.8796 0.8302 0.6718 0.0276  0.0559  0.0544  339 MET A CB  
2429 C CG  . MET B 124 ? 0.8386 0.8133 0.6517 0.0198  0.0667  0.0421  339 MET A CG  
2430 S SD  . MET B 124 ? 0.7817 0.7510 0.6305 0.0241  0.0640  0.0313  339 MET A SD  
2431 C CE  . MET B 124 ? 0.8113 0.8092 0.6794 0.0134  0.0752  0.0373  339 MET A CE  
2432 N N   . THR B 125 ? 0.8604 0.7568 0.5942 0.0509  0.0496  0.0973  340 THR A N   
2433 C CA  . THR B 125 ? 0.9025 0.7755 0.6278 0.0700  0.0429  0.1067  340 THR A CA  
2434 C C   . THR B 125 ? 0.8875 0.7305 0.6345 0.0611  0.0402  0.0953  340 THR A C   
2435 O O   . THR B 125 ? 0.8833 0.6986 0.6305 0.0425  0.0475  0.0962  340 THR A O   
2436 C CB  . THR B 125 ? 0.9641 0.7967 0.6491 0.0848  0.0523  0.1365  340 THR A CB  
2437 O OG1 . THR B 125 ? 1.0387 0.8363 0.7077 0.0636  0.0667  0.1441  340 THR A OG1 
2438 C CG2 . THR B 125 ? 0.9704 0.8475 0.6350 0.1060  0.0495  0.1518  340 THR A CG2 
2439 N N   . LEU B 126 ? 0.9115 0.7675 0.6764 0.0709  0.0300  0.0837  341 LEU A N   
2440 C CA  . LEU B 126 ? 0.9416 0.7759 0.7268 0.0637  0.0265  0.0730  341 LEU A CA  
2441 C C   . LEU B 126 ? 0.9675 0.7560 0.7337 0.0753  0.0277  0.0851  341 LEU A C   
2442 O O   . LEU B 126 ? 0.9815 0.7730 0.7328 0.0986  0.0260  0.0963  341 LEU A O   
2443 C CB  . LEU B 126 ? 0.8835 0.7497 0.6956 0.0655  0.0183  0.0532  341 LEU A CB  
2444 C CG  . LEU B 126 ? 0.7998 0.7020 0.6248 0.0579  0.0216  0.0375  341 LEU A CG  
2445 C CD1 . LEU B 126 ? 0.7960 0.7132 0.6343 0.0597  0.0174  0.0196  341 LEU A CD1 
2446 C CD2 . LEU B 126 ? 0.7684 0.6698 0.6097 0.0458  0.0294  0.0338  341 LEU A CD2 
2447 N N   . THR B 127 ? 0.9207 0.6705 0.6854 0.0593  0.0324  0.0832  342 THR A N   
2448 C CA  . THR B 127 ? 0.9710 0.6750 0.7209 0.0670  0.0349  0.0868  342 THR A CA  
2449 C C   . THR B 127 ? 0.8863 0.6077 0.6663 0.0611  0.0242  0.0694  342 THR A C   
2450 O O   . THR B 127 ? 0.8620 0.5954 0.6601 0.0396  0.0225  0.0598  342 THR A O   
2451 C CB  . THR B 127 ? 0.9666 0.6077 0.6843 0.0481  0.0507  0.0940  342 THR A CB  
2452 O OG1 . THR B 127 ? 1.0018 0.5983 0.7062 0.0536  0.0544  0.0918  342 THR A OG1 
2453 C CG2 . THR B 127 ? 0.9557 0.6153 0.6908 0.0131  0.0503  0.0821  342 THR A CG2 
2454 N N   . CYS B 128 ? 0.8955 0.6252 0.6810 0.0812  0.0177  0.0673  343 CYS A N   
2455 C CA  . CYS B 128 ? 0.8980 0.6425 0.7086 0.0775  0.0088  0.0526  343 CYS A CA  
2456 C C   . CYS B 128 ? 0.8764 0.5786 0.6718 0.0816  0.0124  0.0539  343 CYS A C   
2457 O O   . CYS B 128 ? 0.9108 0.5891 0.6835 0.1031  0.0188  0.0651  343 CYS A O   
2458 C CB  . CYS B 128 ? 0.8561 0.6464 0.6847 0.0897  0.0004  0.0448  343 CYS A CB  
2459 S SG  . CYS B 128 ? 0.9598 0.7933 0.7887 0.0894  0.0009  0.0446  343 CYS A SG  
2460 N N   . SER B 129 ? 0.8525 0.5472 0.6578 0.0627  0.0101  0.0438  344 SER A N   
2461 C CA  . SER B 129 ? 0.8751 0.5283 0.6627 0.0599  0.0152  0.0412  344 SER A CA  
2462 C C   . SER B 129 ? 0.8503 0.5299 0.6626 0.0596  0.0046  0.0298  344 SER A C   
2463 O O   . SER B 129 ? 0.8179 0.5322 0.6557 0.0481  -0.0031 0.0239  344 SER A O   
2464 C CB  . SER B 129 ? 0.8799 0.4983 0.6468 0.0292  0.0247  0.0389  344 SER A CB  
2465 O OG  . SER B 129 ? 1.0244 0.6285 0.7874 0.0147  0.0242  0.0283  344 SER A OG  
2466 N N   . SER B 130 ? 0.8492 0.5134 0.6532 0.0755  0.0061  0.0290  345 SER A N   
2467 C CA  . SER B 130 ? 0.8336 0.5166 0.6555 0.0735  -0.0017 0.0191  345 SER A CA  
2468 C C   . SER B 130 ? 0.8935 0.5344 0.6923 0.0636  0.0057  0.0143  345 SER A C   
2469 O O   . SER B 130 ? 0.9260 0.5211 0.6945 0.0757  0.0189  0.0188  345 SER A O   
2470 C CB  . SER B 130 ? 0.8456 0.5576 0.6794 0.0958  -0.0059 0.0188  345 SER A CB  
2471 O OG  . SER B 130 ? 0.8911 0.6317 0.7304 0.1058  -0.0076 0.0242  345 SER A OG  
2472 N N   . LYS B 131 ? 0.8644 0.5195 0.6736 0.0427  -0.0004 0.0061  346 LYS A N   
2473 C CA  . LYS B 131 ? 0.8760 0.5006 0.6629 0.0276  0.0053  -0.0022 346 LYS A CA  
2474 C C   . LYS B 131 ? 0.8552 0.5078 0.6607 0.0349  -0.0033 -0.0070 346 LYS A C   
2475 O O   . LYS B 131 ? 0.8088 0.5020 0.6390 0.0273  -0.0139 -0.0068 346 LYS A O   
2476 C CB  . LYS B 131 ? 0.9244 0.5532 0.7038 -0.0084 0.0053  -0.0072 346 LYS A CB  
2477 C CG  . LYS B 131 ? 0.9969 0.5901 0.7503 -0.0239 0.0179  -0.0046 346 LYS A CG  
2478 C CD  . LYS B 131 ? 1.0726 0.7015 0.8318 -0.0617 0.0137  -0.0086 346 LYS A CD  
2479 C CE  . LYS B 131 ? 1.1762 0.7903 0.9224 -0.0750 0.0231  -0.0032 346 LYS A CE  
2480 N NZ  . LYS B 131 ? 1.2054 0.8699 0.9612 -0.1128 0.0189  -0.0068 346 LYS A NZ  
2481 N N   . VAL B 132 ? 0.8821 0.5137 0.6750 0.0523  0.0031  -0.0092 347 VAL A N   
2482 C CA  . VAL B 132 ? 0.8554 0.5080 0.6595 0.0542  -0.0022 -0.0150 347 VAL A CA  
2483 C C   . VAL B 132 ? 0.9016 0.5313 0.6823 0.0305  0.0021  -0.0246 347 VAL A C   
2484 O O   . VAL B 132 ? 0.9473 0.5256 0.6928 0.0237  0.0168  -0.0299 347 VAL A O   
2485 C CB  . VAL B 132 ? 0.8837 0.5366 0.6868 0.0827  0.0031  -0.0135 347 VAL A CB  
2486 C CG1 . VAL B 132 ? 0.8520 0.5310 0.6679 0.0815  -0.0018 -0.0196 347 VAL A CG1 
2487 C CG2 . VAL B 132 ? 0.8518 0.5358 0.6735 0.1001  -0.0012 -0.0052 347 VAL A CG2 
2488 N N   . CYS B 133 ? 0.8625 0.5284 0.6583 0.0161  -0.0085 -0.0265 348 CYS A N   
2489 C CA  . CYS B 133 ? 0.9203 0.5805 0.6947 -0.0095 -0.0068 -0.0360 348 CYS A CA  
2490 C C   . CYS B 133 ? 0.9094 0.5865 0.6885 -0.0030 -0.0100 -0.0387 348 CYS A C   
2491 O O   . CYS B 133 ? 0.8053 0.5150 0.6115 0.0113  -0.0180 -0.0310 348 CYS A O   
2492 C CB  . CYS B 133 ? 0.9421 0.6442 0.7265 -0.0359 -0.0169 -0.0328 348 CYS A CB  
2493 S SG  . CYS B 133 ? 1.0341 0.7325 0.8170 -0.0504 -0.0142 -0.0293 348 CYS A SG  
2494 N N   . SER B 134 ? 0.9693 0.6196 0.7176 -0.0160 -0.0009 -0.0509 349 SER A N   
2495 C CA  . SER B 134 ? 0.9246 0.5972 0.6733 -0.0183 -0.0045 -0.0541 349 SER A CA  
2496 C C   . SER B 134 ? 0.9479 0.6253 0.6695 -0.0543 -0.0044 -0.0647 349 SER A C   
2497 O O   . SER B 134 ? 0.9541 0.5885 0.6415 -0.0746 0.0085  -0.0777 349 SER A O   
2498 C CB  . SER B 134 ? 0.9177 0.5622 0.6552 0.0043  0.0079  -0.0599 349 SER A CB  
2499 O OG  . SER B 134 ? 1.0209 0.6054 0.7223 0.0054  0.0268  -0.0698 349 SER A OG  
2500 N N   . PHE B 135 ? 0.9338 0.6653 0.6684 -0.0640 -0.0175 -0.0580 350 PHE A N   
2501 C CA  . PHE B 135 ? 0.9645 0.7262 0.6782 -0.1006 -0.0217 -0.0651 350 PHE A CA  
2502 C C   . PHE B 135 ? 0.9828 0.7480 0.6889 -0.1271 -0.0215 -0.0688 350 PHE A C   
2503 O O   . PHE B 135 ? 1.0739 0.8132 0.7417 -0.1625 -0.0109 -0.0875 350 PHE A O   
2504 C CB  . PHE B 135 ? 0.9022 0.6275 0.5739 -0.1170 -0.0080 -0.0858 350 PHE A CB  
2505 C CG  . PHE B 135 ? 0.9247 0.6501 0.6046 -0.0911 -0.0066 -0.0822 350 PHE A CG  
2506 C CD1 . PHE B 135 ? 0.9092 0.6874 0.5962 -0.0959 -0.0176 -0.0737 350 PHE A CD1 
2507 C CD2 . PHE B 135 ? 0.9739 0.6546 0.6559 -0.0608 0.0060  -0.0846 350 PHE A CD2 
2508 C CE1 . PHE B 135 ? 0.8612 0.6390 0.5541 -0.0754 -0.0145 -0.0703 350 PHE A CE1 
2509 C CE2 . PHE B 135 ? 0.9354 0.6268 0.6273 -0.0403 0.0076  -0.0817 350 PHE A CE2 
2510 C CZ  . PHE B 135 ? 0.8633 0.5995 0.5596 -0.0498 -0.0020 -0.0756 350 PHE A CZ  
2511 N N   . GLY B 136 ? 1.0637 0.8588 0.8042 -0.1121 -0.0309 -0.0521 351 GLY A N   
2512 C CA  . GLY B 136 ? 1.1337 0.9455 0.8738 -0.1355 -0.0319 -0.0524 351 GLY A CA  
2513 C C   . GLY B 136 ? 1.2046 0.9440 0.9067 -0.1560 -0.0133 -0.0703 351 GLY A C   
2514 O O   . GLY B 136 ? 1.2551 1.0052 0.9459 -0.1880 -0.0109 -0.0753 351 GLY A O   
2515 N N   . LYS B 137 ? 1.1337 0.7999 0.8138 -0.1371 0.0023  -0.0786 352 LYS A N   
2516 C CA  . LYS B 137 ? 1.1205 0.7028 0.7584 -0.1468 0.0257  -0.0916 352 LYS A CA  
2517 C C   . LYS B 137 ? 1.0786 0.6245 0.7317 -0.1015 0.0311  -0.0784 352 LYS A C   
2518 O O   . LYS B 137 ? 1.0539 0.6118 0.7293 -0.0668 0.0258  -0.0707 352 LYS A O   
2519 C CB  . LYS B 137 ? 1.1369 0.6624 0.7252 -0.1630 0.0451  -0.1128 352 LYS A CB  
2520 C CG  . LYS B 137 ? 1.2303 0.6742 0.7607 -0.1968 0.0725  -0.1315 352 LYS A CG  
2521 C CD  . LYS B 137 ? 1.3015 0.7897 0.8211 -0.2556 0.0665  -0.1418 352 LYS A CD  
2522 C CE  . LYS B 137 ? 1.3715 0.7917 0.8559 -0.2792 0.0884  -0.1478 352 LYS A CE  
2523 N NZ  . LYS B 137 ? 1.2925 0.7481 0.8220 -0.2533 0.0744  -0.1242 352 LYS A NZ  
2524 N N   . GLN B 138 ? 1.1113 0.6203 0.7519 -0.1046 0.0413  -0.0754 353 GLN A N   
2525 C CA  . GLN B 138 ? 1.0761 0.5631 0.7305 -0.0637 0.0448  -0.0603 353 GLN A CA  
2526 C C   . GLN B 138 ? 1.0493 0.4671 0.6724 -0.0343 0.0664  -0.0623 353 GLN A C   
2527 O O   . GLN B 138 ? 1.1195 0.4611 0.6918 -0.0480 0.0914  -0.0728 353 GLN A O   
2528 C CB  . GLN B 138 ? 1.0878 0.5583 0.7346 -0.0774 0.0503  -0.0548 353 GLN A CB  
2529 C CG  . GLN B 138 ? 1.0700 0.5198 0.7252 -0.0370 0.0549  -0.0381 353 GLN A CG  
2530 C CD  . GLN B 138 ? 1.1921 0.5842 0.8130 -0.0491 0.0736  -0.0343 353 GLN A CD  
2531 O OE1 . GLN B 138 ? 1.1430 0.5676 0.7784 -0.0697 0.0658  -0.0307 353 GLN A OE1 
2532 N NE2 . GLN B 138 ? 1.1790 0.4822 0.7509 -0.0360 0.1013  -0.0345 353 GLN A NE2 
2533 N N   . VAL B 139 ? 1.0448 0.4885 0.6954 0.0063  0.0596  -0.0520 354 VAL A N   
2534 C CA  . VAL B 139 ? 1.1021 0.4974 0.7293 0.0423  0.0796  -0.0493 354 VAL A CA  
2535 C C   . VAL B 139 ? 1.1093 0.4975 0.7430 0.0812  0.0846  -0.0299 354 VAL A C   
2536 O O   . VAL B 139 ? 1.1130 0.4492 0.7168 0.1129  0.1073  -0.0234 354 VAL A O   
2537 C CB  . VAL B 139 ? 1.0518 0.4867 0.6992 0.0596  0.0724  -0.0524 354 VAL A CB  
2538 C CG1 . VAL B 139 ? 1.0869 0.5073 0.7097 0.0262  0.0766  -0.0716 354 VAL A CG1 
2539 C CG2 . VAL B 139 ? 0.9731 0.4897 0.6735 0.0645  0.0461  -0.0439 354 VAL A CG2 
2540 N N   . VAL B 140 ? 1.0166 0.4562 0.6855 0.0815  0.0661  -0.0195 355 VAL A N   
2541 C CA  . VAL B 140 ? 1.0166 0.4675 0.6949 0.1155  0.0670  -0.0012 355 VAL A CA  
2542 C C   . VAL B 140 ? 1.0512 0.5177 0.7413 0.0956  0.0574  0.0037  355 VAL A C   
2543 O O   . VAL B 140 ? 0.9787 0.4986 0.7020 0.0756  0.0383  -0.0010 355 VAL A O   
2544 C CB  . VAL B 140 ? 1.0130 0.5372 0.7314 0.1426  0.0517  0.0050  355 VAL A CB  
2545 C CG1 . VAL B 140 ? 0.9984 0.5409 0.7202 0.1775  0.0542  0.0241  355 VAL A CG1 
2546 C CG2 . VAL B 140 ? 1.0257 0.5525 0.7407 0.1571  0.0579  -0.0016 355 VAL A CG2 
2547 N N   . GLU B 141 ? 1.0434 0.4635 0.7054 0.1044  0.0728  0.0152  356 GLU A N   
2548 C CA  . GLU B 141 ? 1.0263 0.4691 0.7015 0.0930  0.0645  0.0228  356 GLU A CA  
2549 C C   . GLU B 141 ? 1.0210 0.4756 0.6968 0.1325  0.0674  0.0435  356 GLU A C   
2550 O O   . GLU B 141 ? 1.0350 0.4368 0.6756 0.1610  0.0884  0.0567  356 GLU A O   
2551 C CB  . GLU B 141 ? 1.0820 0.4698 0.7230 0.0567  0.0786  0.0179  356 GLU A CB  
2552 C CG  . GLU B 141 ? 1.0927 0.5236 0.7573 0.0454  0.0666  0.0251  356 GLU A CG  
2553 C CD  . GLU B 141 ? 1.1522 0.5525 0.7927 0.0038  0.0768  0.0202  356 GLU A CD  
2554 O OE1 . GLU B 141 ? 1.2342 0.5542 0.8242 -0.0112 0.1015  0.0168  356 GLU A OE1 
2555 O OE2 . GLU B 141 ? 1.1072 0.5652 0.7784 -0.0148 0.0620  0.0192  356 GLU A OE2 
2556 N N   . LYS B 142 ? 0.9422 0.4660 0.6550 0.1346  0.0485  0.0467  357 LYS A N   
2557 C CA  . LYS B 142 ? 0.9603 0.5171 0.6782 0.1646  0.0465  0.0640  357 LYS A CA  
2558 C C   . LYS B 142 ? 0.9503 0.5135 0.6699 0.1458  0.0434  0.0679  357 LYS A C   
2559 O O   . LYS B 142 ? 0.9052 0.4992 0.6502 0.1178  0.0311  0.0556  357 LYS A O   
2560 C CB  . LYS B 142 ? 0.9502 0.5872 0.7067 0.1757  0.0287  0.0594  357 LYS A CB  
2561 C CG  . LYS B 142 ? 0.9840 0.6589 0.7401 0.2158  0.0307  0.0741  357 LYS A CG  
2562 C CD  . LYS B 142 ? 0.9867 0.7416 0.7809 0.2086  0.0131  0.0615  357 LYS A CD  
2563 C CE  . LYS B 142 ? 0.9845 0.8095 0.7861 0.2397  0.0104  0.0739  357 LYS A CE  
2564 N NZ  . LYS B 142 ? 0.9425 0.8418 0.7758 0.2175  -0.0052 0.0575  357 LYS A NZ  
2565 N N   . VAL B 143 ? 0.9648 0.5006 0.6568 0.1639  0.0562  0.0869  358 VAL A N   
2566 C CA  . VAL B 143 ? 1.0366 0.5813 0.7281 0.1476  0.0548  0.0920  358 VAL A CA  
2567 C C   . VAL B 143 ? 1.0627 0.6485 0.7535 0.1802  0.0525  0.1118  358 VAL A C   
2568 O O   . VAL B 143 ? 1.0519 0.6107 0.7139 0.2155  0.0665  0.1327  358 VAL A O   
2569 C CB  . VAL B 143 ? 1.0400 0.5046 0.6898 0.1262  0.0758  0.0959  358 VAL A CB  
2570 C CG1 . VAL B 143 ? 1.0050 0.4908 0.6596 0.1059  0.0730  0.0997  358 VAL A CG1 
2571 C CG2 . VAL B 143 ? 1.0790 0.5114 0.7249 0.0911  0.0786  0.0753  358 VAL A CG2 
2572 N N   . GLU B 144 ? 1.0285 0.6802 0.7477 0.1699  0.0369  0.1061  359 GLU A N   
2573 C CA  . GLU B 144 ? 1.0455 0.7373 0.7575 0.1921  0.0358  0.1240  359 GLU A CA  
2574 C C   . GLU B 144 ? 1.0430 0.7576 0.7639 0.1665  0.0312  0.1183  359 GLU A C   
2575 O O   . GLU B 144 ? 1.0274 0.7412 0.7676 0.1358  0.0266  0.1002  359 GLU A O   
2576 C CB  . GLU B 144 ? 1.0226 0.7947 0.7568 0.2134  0.0223  0.1235  359 GLU A CB  
2577 C CG  . GLU B 144 ? 1.0567 0.8645 0.8261 0.1921  0.0087  0.0974  359 GLU A CG  
2578 C CD  . GLU B 144 ? 1.1585 1.0220 0.9401 0.2136  0.0022  0.0979  359 GLU A CD  
2579 O OE1 . GLU B 144 ? 1.1781 1.0188 0.9442 0.2431  0.0113  0.1126  359 GLU A OE1 
2580 O OE2 . GLU B 144 ? 1.1927 1.1228 0.9970 0.1999  -0.0095 0.0833  359 GLU A OE2 
2581 N N   . THR B 145 ? 1.0474 0.7878 0.7531 0.1828  0.0332  0.1361  360 THR A N   
2582 C CA  . THR B 145 ? 1.0229 0.7870 0.7312 0.1632  0.0315  0.1336  360 THR A CA  
2583 C C   . THR B 145 ? 0.9953 0.8438 0.7167 0.1724  0.0191  0.1317  360 THR A C   
2584 O O   . THR B 145 ? 0.9885 0.8750 0.7041 0.2009  0.0156  0.1450  360 THR A O   
2585 C CB  . THR B 145 ? 1.0622 0.7722 0.7304 0.1678  0.0493  0.1571  360 THR A CB  
2586 O OG1 . THR B 145 ? 1.1029 0.8361 0.7485 0.2055  0.0523  0.1840  360 THR A OG1 
2587 C CG2 . THR B 145 ? 1.0438 0.6631 0.6860 0.1633  0.0664  0.1608  360 THR A CG2 
2588 N N   . GLU B 146 ? 0.9864 0.8683 0.7243 0.1472  0.0140  0.1141  361 GLU A N   
2589 C CA  . GLU B 146 ? 0.9669 0.9244 0.7116 0.1457  0.0054  0.1061  361 GLU A CA  
2590 C C   . GLU B 146 ? 0.9668 0.9313 0.7028 0.1290  0.0110  0.1048  361 GLU A C   
2591 O O   . GLU B 146 ? 0.8989 0.8333 0.6458 0.1080  0.0163  0.0929  361 GLU A O   
2592 C CB  . GLU B 146 ? 0.8985 0.8886 0.6725 0.1283  -0.0033 0.0767  361 GLU A CB  
2593 C CG  . GLU B 146 ? 0.8425 0.9070 0.6180 0.1169  -0.0090 0.0616  361 GLU A CG  
2594 C CD  . GLU B 146 ? 0.8923 1.0232 0.6572 0.1388  -0.0169 0.0771  361 GLU A CD  
2595 O OE1 . GLU B 146 ? 0.9518 1.0669 0.7106 0.1687  -0.0167 0.1001  361 GLU A OE1 
2596 O OE2 . GLU B 146 ? 0.8644 1.0674 0.6253 0.1264  -0.0218 0.0664  361 GLU A OE2 
2597 N N   . ARG B 147 ? 1.0490 1.0593 0.7650 0.1400  0.0102  0.1189  362 ARG A N   
2598 C CA  . ARG B 147 ? 1.0599 1.0854 0.7647 0.1245  0.0159  0.1173  362 ARG A CA  
2599 C C   . ARG B 147 ? 1.0065 1.0844 0.7278 0.1007  0.0114  0.0854  362 ARG A C   
2600 O O   . ARG B 147 ? 0.9895 1.1120 0.7196 0.0991  0.0029  0.0717  362 ARG A O   
2601 C CB  . ARG B 147 ? 1.1112 1.1611 0.7817 0.1474  0.0187  0.1491  362 ARG A CB  
2602 C CG  . ARG B 147 ? 1.2136 1.2241 0.8645 0.1828  0.0234  0.1812  362 ARG A CG  
2603 C CD  . ARG B 147 ? 1.3069 1.3289 0.9188 0.2123  0.0309  0.2195  362 ARG A CD  
2604 N NE  . ARG B 147 ? 1.3481 1.4730 0.9577 0.2177  0.0188  0.2210  362 ARG A NE  
2605 C CZ  . ARG B 147 ? 1.3700 1.5277 0.9520 0.2226  0.0225  0.2402  362 ARG A CZ  
2606 N NH1 . ARG B 147 ? 1.4124 1.5043 0.9667 0.2229  0.0390  0.2603  362 ARG A NH1 
2607 N NH2 . ARG B 147 ? 1.3773 1.6395 0.9571 0.2237  0.0101  0.2385  362 ARG A NH2 
2608 N N   . ALA B 148 ? 0.9783 1.0473 0.7018 0.0805  0.0203  0.0724  363 ALA A N   
2609 C CA  . ALA B 148 ? 0.9316 1.0364 0.6625 0.0589  0.0227  0.0414  363 ALA A CA  
2610 C C   . ALA B 148 ? 0.9114 1.0886 0.6210 0.0573  0.0167  0.0406  363 ALA A C   
2611 O O   . ALA B 148 ? 0.9049 1.1076 0.5923 0.0743  0.0134  0.0679  363 ALA A O   
2612 C CB  . ALA B 148 ? 0.9046 0.9911 0.6374 0.0441  0.0365  0.0320  363 ALA A CB  
2613 N N   . GLN B 149 ? 0.8763 1.0875 0.5895 0.0358  0.0169  0.0095  364 GLN A N   
2614 C CA  . GLN B 149 ? 0.8705 1.1614 0.5624 0.0229  0.0124  0.0002  364 GLN A CA  
2615 C C   . GLN B 149 ? 0.8553 1.1465 0.5390 -0.0113 0.0274  -0.0383 364 GLN A C   
2616 O O   . GLN B 149 ? 0.8496 1.0952 0.5477 -0.0244 0.0375  -0.0631 364 GLN A O   
2617 C CB  . GLN B 149 ? 0.8850 1.2275 0.5828 0.0255  -0.0011 -0.0015 364 GLN A CB  
2618 C CG  . GLN B 149 ? 0.9639 1.4023 0.6409 0.0017  -0.0055 -0.0185 364 GLN A CG  
2619 C CD  . GLN B 149 ? 1.0294 1.5435 0.6872 0.0275  -0.0174 0.0177  364 GLN A CD  
2620 O OE1 . GLN B 149 ? 1.0148 1.6158 0.6505 0.0102  -0.0212 0.0103  364 GLN A OE1 
2621 N NE2 . GLN B 149 ? 1.0394 1.5210 0.7020 0.0696  -0.0217 0.0576  364 GLN A NE2 
2622 N N   . LEU B 150 ? 0.9160 1.2544 0.5729 -0.0241 0.0315  -0.0425 365 LEU A N   
2623 C CA  . LEU B 150 ? 0.9011 1.2335 0.5431 -0.0564 0.0505  -0.0805 365 LEU A CA  
2624 C C   . LEU B 150 ? 0.9456 1.3156 0.5766 -0.0890 0.0518  -0.1154 365 LEU A C   
2625 O O   . LEU B 150 ? 0.9388 1.3892 0.5597 -0.0943 0.0360  -0.1099 365 LEU A O   
2626 C CB  . LEU B 150 ? 0.9220 1.2937 0.5352 -0.0623 0.0559  -0.0752 365 LEU A CB  
2627 C CG  . LEU B 150 ? 0.9676 1.3380 0.5573 -0.0973 0.0785  -0.1172 365 LEU A CG  
2628 C CD1 . LEU B 150 ? 0.8723 1.1605 0.4782 -0.0903 0.1003  -0.1260 365 LEU A CD1 
2629 C CD2 . LEU B 150 ? 0.9676 1.4076 0.5213 -0.1097 0.0788  -0.1147 365 LEU A CD2 
2630 N N   . GLU B 151 ? 0.8896 1.2026 0.5208 -0.1107 0.0725  -0.1502 366 GLU A N   
2631 C CA  . GLU B 151 ? 0.9492 1.2818 0.5637 -0.1492 0.0799  -0.1878 366 GLU A CA  
2632 C C   . GLU B 151 ? 1.0278 1.2835 0.6268 -0.1717 0.1134  -0.2254 366 GLU A C   
2633 O O   . GLU B 151 ? 1.0314 1.2078 0.6520 -0.1525 0.1246  -0.2219 366 GLU A O   
2634 C CB  . GLU B 151 ? 0.9506 1.2823 0.5898 -0.1415 0.0657  -0.1803 366 GLU A CB  
2635 C CG  . GLU B 151 ? 0.9659 1.3613 0.5878 -0.1813 0.0634  -0.2084 366 GLU A CG  
2636 C CD  . GLU B 151 ? 0.9689 1.3504 0.6165 -0.1746 0.0543  -0.2037 366 GLU A CD  
2637 O OE1 . GLU B 151 ? 0.9766 1.2686 0.6356 -0.1724 0.0696  -0.2138 366 GLU A OE1 
2638 O OE2 . GLU B 151 ? 0.9131 1.3775 0.5695 -0.1676 0.0324  -0.1869 366 GLU A OE2 
2639 N N   . ASP B 152 ? 1.0290 1.3082 0.5876 -0.2115 0.1311  -0.2610 367 ASP A N   
2640 C CA  . ASP B 152 ? 1.0516 1.2506 0.5852 -0.2363 0.1692  -0.3016 367 ASP A CA  
2641 C C   . ASP B 152 ? 1.0613 1.1849 0.6116 -0.2001 0.1869  -0.2875 367 ASP A C   
2642 O O   . ASP B 152 ? 1.1077 1.1501 0.6712 -0.1851 0.2055  -0.2910 367 ASP A O   
2643 C CB  . ASP B 152 ? 1.1563 1.3082 0.6923 -0.2535 0.1783  -0.3211 367 ASP A CB  
2644 C CG  . ASP B 152 ? 1.2130 1.4304 0.7433 -0.2976 0.1677  -0.3374 367 ASP A CG  
2645 O OD1 . ASP B 152 ? 1.2013 1.5208 0.7334 -0.3048 0.1434  -0.3250 367 ASP A OD1 
2646 O OD2 . ASP B 152 ? 1.2843 1.4538 0.8129 -0.3229 0.1838  -0.3578 367 ASP A OD2 
2647 N N   . GLY B 153 ? 1.0191 1.1779 0.5703 -0.1839 0.1801  -0.2677 368 GLY A N   
2648 C CA  . GLY B 153 ? 0.9659 1.0743 0.5332 -0.1530 0.1958  -0.2537 368 GLY A CA  
2649 C C   . GLY B 153 ? 1.0160 1.0862 0.6302 -0.1140 0.1838  -0.2210 368 GLY A C   
2650 O O   . GLY B 153 ? 1.0203 1.0554 0.6521 -0.0890 0.1970  -0.2091 368 GLY A O   
2651 N N   . ARG B 154 ? 0.9558 1.0393 0.5899 -0.1094 0.1594  -0.2064 369 ARG A N   
2652 C CA  . ARG B 154 ? 0.9871 1.0369 0.6613 -0.0777 0.1475  -0.1784 369 ARG A CA  
2653 C C   . ARG B 154 ? 0.9057 1.0030 0.5965 -0.0629 0.1147  -0.1441 369 ARG A C   
2654 O O   . ARG B 154 ? 0.9017 1.0592 0.5752 -0.0742 0.0999  -0.1412 369 ARG A O   
2655 C CB  . ARG B 154 ? 1.0194 1.0212 0.7000 -0.0828 0.1551  -0.1937 369 ARG A CB  
2656 C CG  . ARG B 154 ? 1.0910 1.0183 0.7744 -0.0692 0.1867  -0.2040 369 ARG A CG  
2657 C CD  . ARG B 154 ? 1.1180 0.9958 0.8223 -0.0552 0.1877  -0.1978 369 ARG A CD  
2658 N NE  . ARG B 154 ? 1.0995 0.9730 0.8428 -0.0195 0.1760  -0.1645 369 ARG A NE  
2659 C CZ  . ARG B 154 ? 1.0611 0.8979 0.8177 0.0060  0.1962  -0.1571 369 ARG A CZ  
2660 N NH1 . ARG B 154 ? 1.0985 0.8899 0.8312 0.0065  0.2324  -0.1784 369 ARG A NH1 
2661 N NH2 . ARG B 154 ? 0.9898 0.8389 0.7821 0.0318  0.1814  -0.1274 369 ARG A NH2 
2662 N N   . PHE B 155 ? 0.9045 0.9752 0.6258 -0.0367 0.1054  -0.1173 370 PHE A N   
2663 C CA  . PHE B 155 ? 0.9273 1.0214 0.6602 -0.0220 0.0799  -0.0877 370 PHE A CA  
2664 C C   . PHE B 155 ? 0.9170 0.9912 0.6675 -0.0185 0.0707  -0.0894 370 PHE A C   
2665 O O   . PHE B 155 ? 0.9120 0.9396 0.6782 -0.0150 0.0811  -0.0978 370 PHE A O   
2666 C CB  . PHE B 155 ? 0.8853 0.9638 0.6326 -0.0026 0.0765  -0.0585 370 PHE A CB  
2667 C CG  . PHE B 155 ? 0.8540 0.9611 0.5809 -0.0062 0.0819  -0.0507 370 PHE A CG  
2668 C CD1 . PHE B 155 ? 0.8683 1.0236 0.5708 -0.0080 0.0705  -0.0390 370 PHE A CD1 
2669 C CD2 . PHE B 155 ? 0.8877 0.9805 0.6192 -0.0060 0.0992  -0.0535 370 PHE A CD2 
2670 C CE1 . PHE B 155 ? 0.8594 1.0418 0.5396 -0.0113 0.0761  -0.0301 370 PHE A CE1 
2671 C CE2 . PHE B 155 ? 0.8071 0.9278 0.5183 -0.0109 0.1053  -0.0466 370 PHE A CE2 
2672 C CZ  . PHE B 155 ? 0.8014 0.9638 0.4857 -0.0146 0.0938  -0.0350 370 PHE A CZ  
2673 N N   . VAL B 156 ? 0.8731 0.9877 0.6194 -0.0177 0.0527  -0.0803 371 VAL A N   
2674 C CA  . VAL B 156 ? 0.9025 1.0095 0.6630 -0.0164 0.0440  -0.0830 371 VAL A CA  
2675 C C   . VAL B 156 ? 0.8666 0.9829 0.6379 0.0095  0.0253  -0.0503 371 VAL A C   
2676 O O   . VAL B 156 ? 0.8954 1.0437 0.6537 0.0215  0.0180  -0.0290 371 VAL A O   
2677 C CB  . VAL B 156 ? 0.9357 1.0887 0.6786 -0.0445 0.0448  -0.1094 371 VAL A CB  
2678 C CG1 . VAL B 156 ? 0.9729 1.1135 0.6918 -0.0733 0.0681  -0.1424 371 VAL A CG1 
2679 C CG2 . VAL B 156 ? 0.9261 1.1618 0.6570 -0.0407 0.0269  -0.0937 371 VAL A CG2 
2680 N N   . TYR B 157 ? 0.8287 0.9106 0.6198 0.0195  0.0207  -0.0454 372 TYR A N   
2681 C CA  . TYR B 157 ? 0.8350 0.9113 0.6329 0.0434  0.0078  -0.0181 372 TYR A CA  
2682 C C   . TYR B 157 ? 0.8416 0.9336 0.6488 0.0431  0.0003  -0.0250 372 TYR A C   
2683 O O   . TYR B 157 ? 0.8362 0.8966 0.6565 0.0330  0.0053  -0.0409 372 TYR A O   
2684 C CB  . TYR B 157 ? 0.8152 0.8330 0.6264 0.0534  0.0112  -0.0053 372 TYR A CB  
2685 C CG  . TYR B 157 ? 0.8430 0.8495 0.6500 0.0479  0.0215  -0.0039 372 TYR A CG  
2686 C CD1 . TYR B 157 ? 0.8322 0.8289 0.6461 0.0354  0.0346  -0.0243 372 TYR A CD1 
2687 C CD2 . TYR B 157 ? 0.8514 0.8550 0.6445 0.0564  0.0213  0.0188  372 TYR A CD2 
2688 C CE1 . TYR B 157 ? 0.8684 0.8621 0.6801 0.0329  0.0456  -0.0224 372 TYR A CE1 
2689 C CE2 . TYR B 157 ? 0.8170 0.8161 0.6068 0.0489  0.0316  0.0199  372 TYR A CE2 
2690 C CZ  . TYR B 157 ? 0.8249 0.8244 0.6261 0.0378  0.0428  -0.0009 372 TYR A CZ  
2691 O OH  . TYR B 157 ? 0.8157 0.8178 0.6153 0.0328  0.0545  0.0003  372 TYR A OH  
2692 N N   . ARG B 158 ? 0.7914 0.9356 0.5915 0.0561  -0.0105 -0.0112 373 ARG A N   
2693 C CA  . ARG B 158 ? 0.7623 0.9411 0.5710 0.0528  -0.0171 -0.0195 373 ARG A CA  
2694 C C   . ARG B 158 ? 0.7884 0.9620 0.6022 0.0866  -0.0249 0.0082  373 ARG A C   
2695 O O   . ARG B 158 ? 0.7895 0.9961 0.5904 0.1118  -0.0293 0.0334  373 ARG A O   
2696 C CB  . ARG B 158 ? 0.7597 1.0255 0.5556 0.0329  -0.0205 -0.0338 373 ARG A CB  
2697 C CG  . ARG B 158 ? 0.7890 1.0445 0.5753 -0.0080 -0.0068 -0.0706 373 ARG A CG  
2698 C CD  . ARG B 158 ? 0.7476 1.0845 0.5203 -0.0409 -0.0079 -0.0944 373 ARG A CD  
2699 N NE  . ARG B 158 ? 0.8627 1.2572 0.6126 -0.0518 -0.0083 -0.0966 373 ARG A NE  
2700 C CZ  . ARG B 158 ? 0.8740 1.2683 0.6018 -0.0900 0.0063  -0.1288 373 ARG A CZ  
2701 N NH1 . ARG B 158 ? 0.8752 1.2092 0.5985 -0.1195 0.0252  -0.1610 373 ARG A NH1 
2702 N NH2 . ARG B 158 ? 0.8759 1.3278 0.5818 -0.0978 0.0046  -0.1280 373 ARG A NH2 
2703 N N   . LEU B 159 ? 0.7814 0.9092 0.6103 0.0889  -0.0241 0.0045  374 LEU A N   
2704 C CA  . LEU B 159 ? 0.7766 0.8962 0.6090 0.1168  -0.0282 0.0238  374 LEU A CA  
2705 C C   . LEU B 159 ? 0.7637 0.9280 0.6092 0.1058  -0.0324 0.0078  374 LEU A C   
2706 O O   . LEU B 159 ? 0.7842 0.9115 0.6419 0.0925  -0.0296 -0.0066 374 LEU A O   
2707 C CB  . LEU B 159 ? 0.7963 0.8321 0.6319 0.1234  -0.0229 0.0305  374 LEU A CB  
2708 C CG  . LEU B 159 ? 0.8462 0.8376 0.6710 0.1214  -0.0167 0.0394  374 LEU A CG  
2709 C CD1 . LEU B 159 ? 0.8146 0.7935 0.6508 0.0949  -0.0125 0.0185  374 LEU A CD1 
2710 C CD2 . LEU B 159 ? 0.8707 0.7972 0.6884 0.1333  -0.0116 0.0540  374 LEU A CD2 
2711 N N   . LEU B 160 ? 0.7209 0.9719 0.5631 0.1103  -0.0388 0.0115  375 LEU A N   
2712 C CA  . LEU B 160 ? 0.7067 1.0182 0.5597 0.0912  -0.0421 -0.0067 375 LEU A CA  
2713 C C   . LEU B 160 ? 0.7354 1.0930 0.5952 0.1263  -0.0476 0.0155  375 LEU A C   
2714 O O   . LEU B 160 ? 0.6807 1.0589 0.5309 0.1650  -0.0493 0.0455  375 LEU A O   
2715 C CB  . LEU B 160 ? 0.7213 1.1149 0.5650 0.0588  -0.0441 -0.0259 375 LEU A CB  
2716 C CG  . LEU B 160 ? 0.7298 1.0836 0.5608 0.0261  -0.0347 -0.0487 375 LEU A CG  
2717 C CD1 . LEU B 160 ? 0.6797 1.1103 0.4970 -0.0158 -0.0328 -0.0763 375 LEU A CD1 
2718 C CD2 . LEU B 160 ? 0.7216 0.9809 0.5606 0.0124  -0.0237 -0.0646 375 LEU A CD2 
2719 N N   . ARG B 161 ? 0.7067 1.0762 0.5809 0.1147  -0.0474 0.0019  376 ARG A N   
2720 C CA  . ARG B 161 ? 0.6988 1.1164 0.5822 0.1459  -0.0502 0.0189  376 ARG A CA  
2721 C C   . ARG B 161 ? 0.7104 1.0614 0.5852 0.1946  -0.0448 0.0492  376 ARG A C   
2722 O O   . ARG B 161 ? 0.7164 1.1107 0.5872 0.2368  -0.0440 0.0758  376 ARG A O   
2723 C CB  . ARG B 161 ? 0.6761 1.2283 0.5612 0.1527  -0.0583 0.0272  376 ARG A CB  
2724 C CG  . ARG B 161 ? 0.6962 1.3321 0.5851 0.0974  -0.0618 -0.0061 376 ARG A CG  
2725 C CD  . ARG B 161 ? 0.7799 1.3384 0.6586 0.0498  -0.0539 -0.0377 376 ARG A CD  
2726 N NE  . ARG B 161 ? 0.8798 1.5047 0.7490 -0.0037 -0.0521 -0.0693 376 ARG A NE  
2727 C CZ  . ARG B 161 ? 0.8905 1.4531 0.7465 -0.0481 -0.0398 -0.1006 376 ARG A CZ  
2728 N NH1 . ARG B 161 ? 0.8272 1.2712 0.6838 -0.0439 -0.0302 -0.1031 376 ARG A NH1 
2729 N NH2 . ARG B 161 ? 0.8838 1.5065 0.7232 -0.0978 -0.0351 -0.1299 376 ARG A NH2 
2730 N N   . SER B 162 ? 0.7029 0.9488 0.5723 0.1888  -0.0387 0.0455  377 SER A N   
2731 C CA  . SER B 162 ? 0.7668 0.9405 0.6247 0.2235  -0.0300 0.0660  377 SER A CA  
2732 C C   . SER B 162 ? 0.7727 0.9581 0.6413 0.2357  -0.0275 0.0640  377 SER A C   
2733 O O   . SER B 162 ? 0.6956 0.8743 0.5787 0.2055  -0.0298 0.0411  377 SER A O   
2734 C CB  . SER B 162 ? 0.7843 0.8581 0.6355 0.2059  -0.0248 0.0584  377 SER A CB  
2735 O OG  . SER B 162 ? 0.8815 0.9556 0.7302 0.1841  -0.0275 0.0516  377 SER A OG  
2736 N N   . PRO B 163 ? 0.7177 0.9179 0.5774 0.2811  -0.0205 0.0884  378 PRO A N   
2737 C CA  . PRO B 163 ? 0.7499 0.9508 0.6171 0.2955  -0.0148 0.0866  378 PRO A CA  
2738 C C   . PRO B 163 ? 0.7711 0.8699 0.6330 0.2761  -0.0088 0.0716  378 PRO A C   
2739 O O   . PRO B 163 ? 0.7944 0.8065 0.6338 0.2852  0.0010  0.0800  378 PRO A O   
2740 C CB  . PRO B 163 ? 0.7243 0.9322 0.5735 0.3558  -0.0021 0.1204  378 PRO A CB  
2741 C CG  . PRO B 163 ? 0.7222 0.9812 0.5627 0.3702  -0.0070 0.1402  378 PRO A CG  
2742 C CD  . PRO B 163 ? 0.7029 0.9124 0.5415 0.3251  -0.0140 0.1211  378 PRO A CD  
2743 N N   . MET B 164 ? 0.7527 0.8659 0.6330 0.2458  -0.0139 0.0492  379 MET A N   
2744 C CA  . MET B 164 ? 0.8016 0.8363 0.6780 0.2290  -0.0095 0.0368  379 MET A CA  
2745 C C   . MET B 164 ? 0.8439 0.8273 0.6998 0.2639  0.0052  0.0503  379 MET A C   
2746 O O   . MET B 164 ? 0.8193 0.8467 0.6756 0.2975  0.0116  0.0624  379 MET A O   
2747 C CB  . MET B 164 ? 0.7866 0.8564 0.6832 0.1983  -0.0149 0.0158  379 MET A CB  
2748 C CG  . MET B 164 ? 0.8746 0.8759 0.7698 0.1725  -0.0140 0.0024  379 MET A CG  
2749 S SD  . MET B 164 ? 0.8168 0.8520 0.7281 0.1454  -0.0149 -0.0159 379 MET A SD  
2750 C CE  . MET B 164 ? 0.6735 0.7518 0.5953 0.1093  -0.0199 -0.0310 379 MET A CE  
2751 N N   . CYS B 165 ? 0.8835 0.7756 0.7187 0.2563  0.0128  0.0486  380 CYS A N   
2752 C CA  . CYS B 165 ? 0.9615 0.7891 0.7674 0.2846  0.0319  0.0582  380 CYS A CA  
2753 C C   . CYS B 165 ? 0.9843 0.8357 0.7984 0.2926  0.0359  0.0505  380 CYS A C   
2754 O O   . CYS B 165 ? 0.9373 0.8147 0.7723 0.2620  0.0251  0.0328  380 CYS A O   
2755 C CB  . CYS B 165 ? 1.0205 0.7532 0.8019 0.2606  0.0391  0.0502  380 CYS A CB  
2756 S SG  . CYS B 165 ? 1.0761 0.8085 0.8785 0.2104  0.0240  0.0254  380 CYS A SG  
2757 N N   . GLU B 166 ? 1.0980 0.9390 0.8935 0.3362  0.0541  0.0654  381 GLU A N   
2758 C CA  . GLU B 166 ? 1.0983 0.9788 0.9043 0.3494  0.0590  0.0604  381 GLU A CA  
2759 C C   . GLU B 166 ? 1.0871 0.9137 0.8865 0.3167  0.0606  0.0383  381 GLU A C   
2760 O O   . GLU B 166 ? 1.0538 0.9230 0.8690 0.3117  0.0588  0.0287  381 GLU A O   
2761 C CB  . GLU B 166 ? 1.2144 1.0861 0.9977 0.4091  0.0828  0.0830  381 GLU A CB  
2762 C CG  . GLU B 166 ? 1.2508 1.2319 1.0552 0.4453  0.0768  0.1056  381 GLU A CG  
2763 C CD  . GLU B 166 ? 1.1971 1.2973 1.0437 0.4235  0.0584  0.0926  381 GLU A CD  
2764 O OE1 . GLU B 166 ? 1.1355 1.3222 1.0051 0.4096  0.0409  0.0943  381 GLU A OE1 
2765 O OE2 . GLU B 166 ? 1.1745 1.2797 1.0276 0.4166  0.0632  0.0793  381 GLU A OE2 
2766 N N   . TYR B 167 ? 1.0848 0.8276 0.8615 0.2914  0.0635  0.0300  382 TYR A N   
2767 C CA  . TYR B 167 ? 1.0259 0.7370 0.7998 0.2554  0.0604  0.0098  382 TYR A CA  
2768 C C   . TYR B 167 ? 0.9853 0.7628 0.7963 0.2249  0.0390  -0.0006 382 TYR A C   
2769 O O   . TYR B 167 ? 0.9526 0.7564 0.7733 0.2168  0.0381  -0.0098 382 TYR A O   
2770 C CB  . TYR B 167 ? 1.0780 0.7087 0.8246 0.2284  0.0641  0.0034  382 TYR A CB  
2771 C CG  . TYR B 167 ? 1.0367 0.6504 0.7814 0.1903  0.0584  -0.0150 382 TYR A CG  
2772 C CD1 . TYR B 167 ? 0.9630 0.6170 0.7366 0.1599  0.0376  -0.0207 382 TYR A CD1 
2773 C CD2 . TYR B 167 ? 1.0548 0.6128 0.7653 0.1866  0.0758  -0.0258 382 TYR A CD2 
2774 C CE1 . TYR B 167 ? 1.0003 0.6481 0.7721 0.1306  0.0322  -0.0323 382 TYR A CE1 
2775 C CE2 . TYR B 167 ? 0.9927 0.5475 0.7006 0.1507  0.0689  -0.0414 382 TYR A CE2 
2776 C CZ  . TYR B 167 ? 1.0266 0.6306 0.7668 0.1249  0.0460  -0.0424 382 TYR A CZ  
2777 O OH  . TYR B 167 ? 1.0289 0.6390 0.7676 0.0945  0.0384  -0.0523 382 TYR A OH  
2778 N N   . LEU B 168 ? 0.9725 0.7724 0.8008 0.2075  0.0248  0.0007  383 LEU A N   
2779 C CA  . LEU B 168 ? 0.9035 0.7525 0.7598 0.1794  0.0105  -0.0092 383 LEU A CA  
2780 C C   . LEU B 168 ? 0.8442 0.7651 0.7183 0.1876  0.0105  -0.0112 383 LEU A C   
2781 O O   . LEU B 168 ? 0.7956 0.7366 0.6813 0.1643  0.0070  -0.0221 383 LEU A O   
2782 C CB  . LEU B 168 ? 0.9038 0.7682 0.7719 0.1668  0.0004  -0.0070 383 LEU A CB  
2783 C CG  . LEU B 168 ? 0.9416 0.7557 0.8038 0.1438  -0.0035 -0.0103 383 LEU A CG  
2784 C CD1 . LEU B 168 ? 0.8879 0.7258 0.7667 0.1272  -0.0122 -0.0123 383 LEU A CD1 
2785 C CD2 . LEU B 168 ? 0.9192 0.7107 0.7786 0.1251  -0.0038 -0.0190 383 LEU A CD2 
2786 N N   . VAL B 169 ? 0.9028 0.8684 0.7787 0.2204  0.0155  0.0008  384 VAL A N   
2787 C CA  . VAL B 169 ? 0.8584 0.9116 0.7540 0.2265  0.0151  -0.0006 384 VAL A CA  
2788 C C   . VAL B 169 ? 0.8468 0.8917 0.7390 0.2263  0.0237  -0.0084 384 VAL A C   
2789 O O   . VAL B 169 ? 0.7970 0.8815 0.7042 0.1998  0.0198  -0.0202 384 VAL A O   
2790 C CB  . VAL B 169 ? 0.8562 0.9676 0.7532 0.2698  0.0199  0.0188  384 VAL A CB  
2791 C CG1 . VAL B 169 ? 0.7409 0.9699 0.6645 0.2636  0.0138  0.0155  384 VAL A CG1 
2792 C CG2 . VAL B 169 ? 0.9270 1.0198 0.8161 0.2754  0.0148  0.0298  384 VAL A CG2 
2793 N N   . ASN B 170 ? 0.8527 0.8428 0.7209 0.2549  0.0386  -0.0024 385 ASN A N   
2794 C CA  . ASN B 170 ? 0.8664 0.8472 0.7272 0.2564  0.0492  -0.0106 385 ASN A CA  
2795 C C   . ASN B 170 ? 0.8462 0.7936 0.7065 0.2120  0.0410  -0.0266 385 ASN A C   
2796 O O   . ASN B 170 ? 0.8024 0.7810 0.6711 0.1978  0.0418  -0.0350 385 ASN A O   
2797 C CB  . ASN B 170 ? 0.9707 0.8827 0.7972 0.2930  0.0709  -0.0035 385 ASN A CB  
2798 C CG  . ASN B 170 ? 1.0770 1.0244 0.9017 0.3473  0.0831  0.0185  385 ASN A CG  
2799 O OD1 . ASN B 170 ? 1.0548 1.0999 0.9051 0.3654  0.0806  0.0259  385 ASN A OD1 
2800 N ND2 . ASN B 170 ? 1.1400 1.0114 0.9328 0.3726  0.0975  0.0303  385 ASN A ND2 
2801 N N   . PHE B 171 ? 0.8398 0.7319 0.6914 0.1904  0.0332  -0.0288 386 PHE A N   
2802 C CA  . PHE B 171 ? 0.8012 0.6743 0.6549 0.1537  0.0248  -0.0385 386 PHE A CA  
2803 C C   . PHE B 171 ? 0.8184 0.7471 0.6967 0.1317  0.0167  -0.0426 386 PHE A C   
2804 O O   . PHE B 171 ? 0.8560 0.7880 0.7351 0.1115  0.0173  -0.0487 386 PHE A O   
2805 C CB  . PHE B 171 ? 0.7909 0.6125 0.6352 0.1382  0.0178  -0.0372 386 PHE A CB  
2806 C CG  . PHE B 171 ? 0.7908 0.6015 0.6378 0.1075  0.0097  -0.0417 386 PHE A CG  
2807 C CD1 . PHE B 171 ? 0.8266 0.6195 0.6579 0.0974  0.0135  -0.0473 386 PHE A CD1 
2808 C CD2 . PHE B 171 ? 0.7475 0.5660 0.6098 0.0918  0.0002  -0.0389 386 PHE A CD2 
2809 C CE1 . PHE B 171 ? 0.7814 0.5715 0.6137 0.0744  0.0062  -0.0466 386 PHE A CE1 
2810 C CE2 . PHE B 171 ? 0.7779 0.5866 0.6408 0.0720  -0.0043 -0.0380 386 PHE A CE2 
2811 C CZ  . PHE B 171 ? 0.8192 0.6172 0.6679 0.0643  -0.0022 -0.0401 386 PHE A CZ  
2812 N N   . LEU B 172 ? 0.8027 0.7730 0.6970 0.1325  0.0114  -0.0399 387 LEU A N   
2813 C CA  . LEU B 172 ? 0.7792 0.7987 0.6901 0.1061  0.0085  -0.0478 387 LEU A CA  
2814 C C   . LEU B 172 ? 0.7642 0.8388 0.6818 0.1066  0.0157  -0.0524 387 LEU A C   
2815 O O   . LEU B 172 ? 0.7886 0.8794 0.7101 0.0771  0.0179  -0.0612 387 LEU A O   
2816 C CB  . LEU B 172 ? 0.7077 0.7702 0.6303 0.1049  0.0031  -0.0469 387 LEU A CB  
2817 C CG  . LEU B 172 ? 0.7287 0.7490 0.6483 0.0919  -0.0028 -0.0466 387 LEU A CG  
2818 C CD1 . LEU B 172 ? 0.6903 0.7636 0.6188 0.0889  -0.0068 -0.0479 387 LEU A CD1 
2819 C CD2 . LEU B 172 ? 0.6645 0.6461 0.5811 0.0619  -0.0010 -0.0538 387 LEU A CD2 
2820 N N   . HIS B 173 ? 0.7567 0.8596 0.6736 0.1411  0.0220  -0.0456 388 HIS A N   
2821 C CA  A HIS B 173 ? 0.7217 0.8921 0.6486 0.1442  0.0295  -0.0490 388 HIS A CA  
2822 C CA  B HIS B 173 ? 0.7245 0.8944 0.6509 0.1469  0.0299  -0.0484 388 HIS A CA  
2823 C C   . HIS B 173 ? 0.8110 0.9430 0.7244 0.1359  0.0372  -0.0550 388 HIS A C   
2824 O O   . HIS B 173 ? 0.8005 0.9767 0.7215 0.1169  0.0416  -0.0621 388 HIS A O   
2825 C CB  A HIS B 173 ? 0.7550 0.9782 0.6867 0.1908  0.0361  -0.0362 388 HIS A CB  
2826 C CB  B HIS B 173 ? 0.7709 0.9795 0.6984 0.1964  0.0377  -0.0349 388 HIS A CB  
2827 C CG  A HIS B 173 ? 0.7211 1.0432 0.6749 0.1900  0.0295  -0.0328 388 HIS A CG  
2828 C CG  B HIS B 173 ? 0.7321 1.0373 0.6764 0.2081  0.0451  -0.0345 388 HIS A CG  
2829 N ND1 A HIS B 173 ? 0.6946 1.1033 0.6666 0.1586  0.0281  -0.0439 388 HIS A ND1 
2830 N ND1 B HIS B 173 ? 0.6837 1.0956 0.6518 0.1967  0.0391  -0.0351 388 HIS A ND1 
2831 C CD2 A HIS B 173 ? 0.6804 1.0320 0.6381 0.2124  0.0242  -0.0203 388 HIS A CD2 
2832 C CD2 B HIS B 173 ? 0.6979 1.0160 0.6379 0.2293  0.0590  -0.0340 388 HIS A CD2 
2833 C CE1 A HIS B 173 ? 0.6865 1.1804 0.6732 0.1601  0.0215  -0.0400 388 HIS A CE1 
2834 C CE1 B HIS B 173 ? 0.6552 1.1485 0.6359 0.2104  0.0480  -0.0338 388 HIS A CE1 
2835 N NE2 A HIS B 173 ? 0.6690 1.1312 0.6479 0.1946  0.0183  -0.0245 388 HIS A NE2 
2836 N NE2 B HIS B 173 ? 0.6422 1.0781 0.6066 0.2326  0.0608  -0.0326 388 HIS A NE2 
2837 N N   . LYS B 174 ? 0.7735 0.8274 0.6648 0.1448  0.0395  -0.0534 389 LYS A N   
2838 C CA  . LYS B 174 ? 0.7834 0.8054 0.6596 0.1299  0.0448  -0.0600 389 LYS A CA  
2839 C C   . LYS B 174 ? 0.7885 0.7914 0.6659 0.0913  0.0367  -0.0632 389 LYS A C   
2840 O O   . LYS B 174 ? 0.8060 0.8119 0.6777 0.0738  0.0412  -0.0669 389 LYS A O   
2841 C CB  . LYS B 174 ? 0.7485 0.6994 0.5961 0.1452  0.0511  -0.0601 389 LYS A CB  
2842 C CG  . LYS B 174 ? 0.7760 0.7245 0.6129 0.1870  0.0659  -0.0556 389 LYS A CG  
2843 C CD  . LYS B 174 ? 0.8302 0.6949 0.6366 0.1946  0.0713  -0.0554 389 LYS A CD  
2844 C CE  . LYS B 174 ? 0.8709 0.7088 0.6537 0.2362  0.0943  -0.0521 389 LYS A CE  
2845 N NZ  . LYS B 174 ? 0.9989 0.7456 0.7458 0.2355  0.1027  -0.0541 389 LYS A NZ  
2846 N N   . LEU B 175 ? 0.8105 0.7911 0.6929 0.0804  0.0272  -0.0600 390 LEU A N   
2847 C CA  . LEU B 175 ? 0.7877 0.7462 0.6689 0.0506  0.0241  -0.0599 390 LEU A CA  
2848 C C   . LEU B 175 ? 0.7808 0.7840 0.6721 0.0274  0.0303  -0.0664 390 LEU A C   
2849 O O   . LEU B 175 ? 0.7445 0.7320 0.6273 0.0044  0.0362  -0.0668 390 LEU A O   
2850 C CB  . LEU B 175 ? 0.7658 0.6921 0.6494 0.0488  0.0158  -0.0550 390 LEU A CB  
2851 C CG  . LEU B 175 ? 0.7749 0.6577 0.6501 0.0340  0.0133  -0.0485 390 LEU A CG  
2852 C CD1 . LEU B 175 ? 0.7894 0.6484 0.6482 0.0383  0.0116  -0.0449 390 LEU A CD1 
2853 C CD2 . LEU B 175 ? 0.7825 0.6449 0.6635 0.0369  0.0068  -0.0440 390 LEU A CD2 
2854 N N   . ARG B 176 ? 0.7839 0.8457 0.6907 0.0319  0.0304  -0.0709 391 ARG A N   
2855 C CA  . ARG B 176 ? 0.7633 0.8794 0.6787 0.0026  0.0368  -0.0808 391 ARG A CA  
2856 C C   . ARG B 176 ? 0.7786 0.9051 0.6868 -0.0152 0.0474  -0.0846 391 ARG A C   
2857 O O   . ARG B 176 ? 0.7819 0.9035 0.6829 -0.0511 0.0564  -0.0911 391 ARG A O   
2858 C CB  . ARG B 176 ? 0.7243 0.9254 0.6581 0.0189  0.0342  -0.0823 391 ARG A CB  
2859 C CG  . ARG B 176 ? 0.7306 0.9916 0.6738 -0.0126 0.0350  -0.0935 391 ARG A CG  
2860 C CD  . ARG B 176 ? 0.6949 1.0660 0.6581 0.0077  0.0325  -0.0913 391 ARG A CD  
2861 N NE  . ARG B 176 ? 0.6931 1.1356 0.6647 -0.0213 0.0302  -0.1019 391 ARG A NE  
2862 C CZ  . ARG B 176 ? 0.7098 1.1619 0.6738 -0.0757 0.0384  -0.1203 391 ARG A CZ  
2863 N NH1 . ARG B 176 ? 0.7718 1.1590 0.7191 -0.1043 0.0500  -0.1269 391 ARG A NH1 
2864 N NH2 . ARG B 176 ? 0.6762 1.2009 0.6447 -0.1036 0.0369  -0.1322 391 ARG A NH2 
2865 N N   . GLN B 177 ? 0.7895 0.9235 0.6951 0.0088  0.0495  -0.0811 392 GLN A N   
2866 C CA  . GLN B 177 ? 0.7889 0.9564 0.6915 -0.0031 0.0604  -0.0855 392 GLN A CA  
2867 C C   . GLN B 177 ? 0.8036 0.9097 0.6838 -0.0166 0.0644  -0.0814 392 GLN A C   
2868 O O   . GLN B 177 ? 0.8262 0.9535 0.7003 -0.0347 0.0749  -0.0846 392 GLN A O   
2869 C CB  . GLN B 177 ? 0.8240 1.0388 0.7338 0.0337  0.0643  -0.0841 392 GLN A CB  
2870 C CG  . GLN B 177 ? 0.8209 1.1101 0.7528 0.0555  0.0614  -0.0824 392 GLN A CG  
2871 C CD  . GLN B 177 ? 0.8859 1.1822 0.8164 0.1077  0.0664  -0.0740 392 GLN A CD  
2872 O OE1 . GLN B 177 ? 0.9021 1.1489 0.8137 0.1224  0.0741  -0.0738 392 GLN A OE1 
2873 N NE2 . GLN B 177 ? 0.8566 1.2109 0.8030 0.1364  0.0643  -0.0662 392 GLN A NE2 
2874 N N   . LEU B 178 ? 0.7741 0.8135 0.6418 -0.0087 0.0567  -0.0733 393 LEU A N   
2875 C CA  . LEU B 178 ? 0.7752 0.7684 0.6219 -0.0215 0.0593  -0.0658 393 LEU A CA  
2876 C C   . LEU B 178 ? 0.8068 0.8019 0.6463 -0.0549 0.0719  -0.0661 393 LEU A C   
2877 O O   . LEU B 178 ? 0.7851 0.7850 0.6306 -0.0742 0.0764  -0.0711 393 LEU A O   
2878 C CB  . LEU B 178 ? 0.7616 0.6986 0.6003 -0.0150 0.0493  -0.0552 393 LEU A CB  
2879 C CG  . LEU B 178 ? 0.7640 0.6881 0.6015 0.0100  0.0398  -0.0558 393 LEU A CG  
2880 C CD1 . LEU B 178 ? 0.7836 0.6670 0.6045 0.0076  0.0330  -0.0454 393 LEU A CD1 
2881 C CD2 . LEU B 178 ? 0.7335 0.6840 0.5672 0.0256  0.0465  -0.0644 393 LEU A CD2 
2882 N N   . PRO B 179 ? 0.7568 0.7455 0.5791 -0.0649 0.0803  -0.0618 394 PRO A N   
2883 C CA  . PRO B 179 ? 0.7660 0.7540 0.5765 -0.0988 0.0969  -0.0621 394 PRO A CA  
2884 C C   . PRO B 179 ? 0.7398 0.6613 0.5327 -0.1134 0.1038  -0.0504 394 PRO A C   
2885 O O   . PRO B 179 ? 0.7626 0.6730 0.5434 -0.1450 0.1216  -0.0542 394 PRO A O   
2886 C CB  . PRO B 179 ? 0.7408 0.7365 0.5346 -0.0994 0.1031  -0.0578 394 PRO A CB  
2887 C CG  . PRO B 179 ? 0.7547 0.7780 0.5583 -0.0675 0.0927  -0.0640 394 PRO A CG  
2888 C CD  . PRO B 179 ? 0.7287 0.7212 0.5403 -0.0478 0.0782  -0.0607 394 PRO A CD  
2889 N N   . GLU B 180 ? 0.7124 0.5892 0.5006 -0.0922 0.0934  -0.0360 395 GLU A N   
2890 C CA  . GLU B 180 ? 0.7622 0.5759 0.5303 -0.0975 0.1034  -0.0192 395 GLU A CA  
2891 C C   . GLU B 180 ? 0.8214 0.6110 0.6006 -0.0767 0.0914  -0.0135 395 GLU A C   
2892 O O   . GLU B 180 ? 0.7617 0.5714 0.5550 -0.0552 0.0730  -0.0143 395 GLU A O   
2893 C CB  . GLU B 180 ? 0.8192 0.6091 0.5632 -0.0905 0.1066  0.0026  395 GLU A CB  
2894 C CG  . GLU B 180 ? 0.8402 0.6516 0.5692 -0.1098 0.1190  0.0001  395 GLU A CG  
2895 C CD  . GLU B 180 ? 0.8805 0.6605 0.5887 -0.1422 0.1457  0.0001  395 GLU A CD  
2896 O OE1 . GLU B 180 ? 0.8769 0.6066 0.5765 -0.1494 0.1576  0.0032  395 GLU A OE1 
2897 O OE2 . GLU B 180 ? 0.9173 0.7167 0.6125 -0.1619 0.1577  -0.0022 395 GLU A OE2 
2898 N N   . ARG B 181 ? 0.8077 0.5499 0.5766 -0.0849 0.1052  -0.0087 396 ARG A N   
2899 C CA  . ARG B 181 ? 0.7883 0.5084 0.5670 -0.0662 0.0972  -0.0037 396 ARG A CA  
2900 C C   . ARG B 181 ? 0.7903 0.5065 0.5693 -0.0372 0.0826  0.0179  396 ARG A C   
2901 O O   . ARG B 181 ? 0.7150 0.4467 0.5113 -0.0207 0.0659  0.0166  396 ARG A O   
2902 C CB  . ARG B 181 ? 0.8611 0.5209 0.6206 -0.0791 0.1211  -0.0010 396 ARG A CB  
2903 C CG  . ARG B 181 ? 0.9320 0.6063 0.6938 -0.1127 0.1319  -0.0285 396 ARG A CG  
2904 C CD  . ARG B 181 ? 1.0493 0.6535 0.7846 -0.1305 0.1597  -0.0309 396 ARG A CD  
2905 N NE  . ARG B 181 ? 1.0562 0.6160 0.7905 -0.0982 0.1587  -0.0126 396 ARG A NE  
2906 C CZ  . ARG B 181 ? 1.1046 0.6030 0.8153 -0.0781 0.1748  0.0143  396 ARG A CZ  
2907 N NH1 . ARG B 181 ? 1.0747 0.5377 0.7565 -0.0878 0.1947  0.0270  396 ARG A NH1 
2908 N NH2 . ARG B 181 ? 1.1260 0.6007 0.8412 -0.0457 0.1725  0.0308  396 ARG A NH2 
2909 N N   . TYR B 182 ? 0.7815 0.4836 0.5399 -0.0328 0.0887  0.0382  397 TYR A N   
2910 C CA  . TYR B 182 ? 0.7922 0.5060 0.5497 -0.0088 0.0740  0.0592  397 TYR A CA  
2911 C C   . TYR B 182 ? 0.7386 0.5005 0.5096 -0.0068 0.0525  0.0453  397 TYR A C   
2912 O O   . TYR B 182 ? 0.7399 0.5182 0.5155 0.0066  0.0374  0.0533  397 TYR A O   
2913 C CB  . TYR B 182 ? 0.8123 0.5099 0.5425 -0.0033 0.0850  0.0866  397 TYR A CB  
2914 C CG  . TYR B 182 ? 0.8239 0.5514 0.5425 -0.0166 0.0827  0.0820  397 TYR A CG  
2915 C CD1 . TYR B 182 ? 0.7869 0.5592 0.5078 -0.0108 0.0633  0.0810  397 TYR A CD1 
2916 C CD2 . TYR B 182 ? 0.8384 0.5476 0.5398 -0.0381 0.1028  0.0778  397 TYR A CD2 
2917 C CE1 . TYR B 182 ? 0.8191 0.6157 0.5262 -0.0228 0.0639  0.0751  397 TYR A CE1 
2918 C CE2 . TYR B 182 ? 0.8496 0.5881 0.5401 -0.0497 0.1026  0.0741  397 TYR A CE2 
2919 C CZ  . TYR B 182 ? 0.8745 0.6560 0.5679 -0.0403 0.0831  0.0727  397 TYR A CZ  
2920 O OH  . TYR B 182 ? 0.8489 0.6578 0.5284 -0.0521 0.0853  0.0668  397 TYR A OH  
2921 N N   . MET B 183 ? 0.7085 0.4930 0.4844 -0.0203 0.0531  0.0238  398 MET A N   
2922 C CA  . MET B 183 ? 0.7311 0.5469 0.5153 -0.0149 0.0388  0.0092  398 MET A CA  
2923 C C   . MET B 183 ? 0.7385 0.5557 0.5429 -0.0059 0.0297  -0.0017 398 MET A C   
2924 O O   . MET B 183 ? 0.6629 0.4871 0.4683 0.0024  0.0182  -0.0052 398 MET A O   
2925 C CB  . MET B 183 ? 0.6973 0.5384 0.4787 -0.0250 0.0459  -0.0064 398 MET A CB  
2926 C CG  . MET B 183 ? 0.7342 0.5781 0.4925 -0.0333 0.0526  0.0039  398 MET A CG  
2927 S SD  . MET B 183 ? 0.7539 0.6342 0.5095 -0.0424 0.0616  -0.0152 398 MET A SD  
2928 C CE  . MET B 183 ? 0.8448 0.7208 0.5689 -0.0533 0.0693  0.0025  398 MET A CE  
2929 N N   . MET B 184 ? 0.7324 0.5415 0.5489 -0.0103 0.0363  -0.0076 399 MET A N   
2930 C CA  . MET B 184 ? 0.7327 0.5433 0.5658 -0.0009 0.0278  -0.0144 399 MET A CA  
2931 C C   . MET B 184 ? 0.7078 0.4997 0.5410 0.0104  0.0200  0.0006  399 MET A C   
2932 O O   . MET B 184 ? 0.6797 0.4791 0.5184 0.0185  0.0084  -0.0021 399 MET A O   
2933 C CB  . MET B 184 ? 0.7321 0.5444 0.5748 -0.0119 0.0367  -0.0247 399 MET A CB  
2934 C CG  . MET B 184 ? 0.7147 0.5669 0.5622 -0.0234 0.0423  -0.0400 399 MET A CG  
2935 S SD  . MET B 184 ? 0.6598 0.5185 0.5056 -0.0544 0.0595  -0.0518 399 MET A SD  
2936 C CE  . MET B 184 ? 0.7284 0.6678 0.5926 -0.0554 0.0560  -0.0684 399 MET A CE  
2937 N N   . ASN B 185 ? 0.7330 0.5015 0.5575 0.0118  0.0283  0.0180  400 ASN A N   
2938 C CA  . ASN B 185 ? 0.7474 0.5115 0.5741 0.0270  0.0217  0.0359  400 ASN A CA  
2939 C C   . ASN B 185 ? 0.7272 0.5219 0.5504 0.0293  0.0061  0.0394  400 ASN A C   
2940 O O   . ASN B 185 ? 0.7442 0.5521 0.5756 0.0348  -0.0046 0.0416  400 ASN A O   
2941 C CB  . ASN B 185 ? 0.7809 0.5167 0.5940 0.0355  0.0366  0.0594  400 ASN A CB  
2942 C CG  . ASN B 185 ? 0.8048 0.4983 0.6156 0.0312  0.0557  0.0545  400 ASN A CG  
2943 O OD1 . ASN B 185 ? 0.7684 0.4653 0.5903 0.0195  0.0547  0.0328  400 ASN A OD1 
2944 N ND2 . ASN B 185 ? 0.8153 0.4674 0.6078 0.0409  0.0754  0.0749  400 ASN A ND2 
2945 N N   . SER B 186 ? 0.7562 0.5636 0.5644 0.0213  0.0062  0.0383  401 SER A N   
2946 C CA  . SER B 186 ? 0.7564 0.5915 0.5544 0.0167  -0.0060 0.0368  401 SER A CA  
2947 C C   . SER B 186 ? 0.7293 0.5641 0.5327 0.0127  -0.0130 0.0160  401 SER A C   
2948 O O   . SER B 186 ? 0.7474 0.5953 0.5485 0.0090  -0.0225 0.0166  401 SER A O   
2949 C CB  . SER B 186 ? 0.7475 0.5925 0.5256 0.0069  -0.0018 0.0341  401 SER A CB  
2950 O OG  . SER B 186 ? 0.8496 0.7049 0.6151 0.0113  0.0002  0.0595  401 SER A OG  
2951 N N   . VAL B 187 ? 0.6728 0.4953 0.4811 0.0133  -0.0066 -0.0012 402 VAL A N   
2952 C CA  . VAL B 187 ? 0.7584 0.5727 0.5678 0.0158  -0.0089 -0.0169 402 VAL A CA  
2953 C C   . VAL B 187 ? 0.7900 0.5980 0.6144 0.0212  -0.0150 -0.0121 402 VAL A C   
2954 O O   . VAL B 187 ? 0.7577 0.5620 0.5763 0.0174  -0.0203 -0.0157 402 VAL A O   
2955 C CB  . VAL B 187 ? 0.7673 0.5814 0.5817 0.0228  0.0002  -0.0301 402 VAL A CB  
2956 C CG1 . VAL B 187 ? 0.7276 0.5284 0.5418 0.0337  0.0008  -0.0404 402 VAL A CG1 
2957 C CG2 . VAL B 187 ? 0.7503 0.5742 0.5496 0.0181  0.0076  -0.0361 402 VAL A CG2 
2958 N N   . LEU B 188 ? 0.7374 0.5419 0.5778 0.0271  -0.0118 -0.0052 403 LEU A N   
2959 C CA  . LEU B 188 ? 0.7553 0.5543 0.6095 0.0331  -0.0153 -0.0017 403 LEU A CA  
2960 C C   . LEU B 188 ? 0.7688 0.5796 0.6228 0.0328  -0.0231 0.0119  403 LEU A C   
2961 O O   . LEU B 188 ? 0.7626 0.5747 0.6238 0.0338  -0.0278 0.0111  403 LEU A O   
2962 C CB  . LEU B 188 ? 0.7267 0.5160 0.5911 0.0356  -0.0064 0.0010  403 LEU A CB  
2963 C CG  . LEU B 188 ? 0.7223 0.5181 0.5901 0.0319  -0.0009 -0.0143 403 LEU A CG  
2964 C CD1 . LEU B 188 ? 0.7147 0.5014 0.5845 0.0234  0.0111  -0.0152 403 LEU A CD1 
2965 C CD2 . LEU B 188 ? 0.7328 0.5345 0.6081 0.0398  -0.0062 -0.0225 403 LEU A CD2 
2966 N N   . GLU B 189 ? 0.7595 0.5867 0.6052 0.0314  -0.0246 0.0255  404 GLU A N   
2967 C CA  . GLU B 189 ? 0.7930 0.6500 0.6414 0.0326  -0.0330 0.0408  404 GLU A CA  
2968 C C   . GLU B 189 ? 0.8047 0.6745 0.6468 0.0164  -0.0419 0.0279  404 GLU A C   
2969 O O   . GLU B 189 ? 0.8327 0.7354 0.6801 0.0130  -0.0492 0.0375  404 GLU A O   
2970 C CB  . GLU B 189 ? 0.8223 0.7052 0.6599 0.0360  -0.0335 0.0609  404 GLU A CB  
2971 C CG  . GLU B 189 ? 0.8765 0.7861 0.6926 0.0181  -0.0403 0.0553  404 GLU A CG  
2972 C CD  . GLU B 189 ? 0.9952 0.9350 0.8011 0.0263  -0.0400 0.0812  404 GLU A CD  
2973 O OE1 . GLU B 189 ? 1.0242 0.9753 0.8404 0.0479  -0.0371 0.1074  404 GLU A OE1 
2974 O OE2 . GLU B 189 ? 0.9320 0.8835 0.7175 0.0140  -0.0406 0.0773  404 GLU A OE2 
2975 N N   . ASN B 190 ? 0.8202 0.6635 0.6497 0.0072  -0.0387 0.0071  405 ASN A N   
2976 C CA  . ASN B 190 ? 0.8101 0.6458 0.6240 -0.0101 -0.0403 -0.0072 405 ASN A CA  
2977 C C   . ASN B 190 ? 0.8053 0.6083 0.6247 -0.0028 -0.0355 -0.0156 405 ASN A C   
2978 O O   . ASN B 190 ? 0.7814 0.5596 0.5812 -0.0145 -0.0309 -0.0283 405 ASN A O   
2979 C CB  . ASN B 190 ? 0.8039 0.6239 0.5886 -0.0239 -0.0346 -0.0235 405 ASN A CB  
2980 C CG  . ASN B 190 ? 0.8415 0.6961 0.6166 -0.0325 -0.0391 -0.0158 405 ASN A CG  
2981 O OD1 . ASN B 190 ? 0.8265 0.7233 0.5977 -0.0469 -0.0482 -0.0075 405 ASN A OD1 
2982 N ND2 . ASN B 190 ? 0.7796 0.6241 0.5498 -0.0246 -0.0327 -0.0178 405 ASN A ND2 
2983 N N   . PHE B 191 ? 0.7360 0.5348 0.5767 0.0150  -0.0340 -0.0093 406 PHE A N   
2984 C CA  . PHE B 191 ? 0.7582 0.5330 0.6026 0.0244  -0.0293 -0.0162 406 PHE A CA  
2985 C C   . PHE B 191 ? 0.7477 0.5338 0.6123 0.0303  -0.0326 -0.0067 406 PHE A C   
2986 O O   . PHE B 191 ? 0.7553 0.5534 0.6343 0.0380  -0.0320 0.0024  406 PHE A O   
2987 C CB  . PHE B 191 ? 0.7573 0.5253 0.6043 0.0374  -0.0228 -0.0218 406 PHE A CB  
2988 C CG  . PHE B 191 ? 0.7699 0.5328 0.6261 0.0509  -0.0197 -0.0241 406 PHE A CG  
2989 C CD1 . PHE B 191 ? 0.7603 0.5359 0.6350 0.0542  -0.0212 -0.0195 406 PHE A CD1 
2990 C CD2 . PHE B 191 ? 0.8117 0.5575 0.6546 0.0619  -0.0129 -0.0301 406 PHE A CD2 
2991 C CE1 . PHE B 191 ? 0.7637 0.5445 0.6449 0.0638  -0.0193 -0.0222 406 PHE A CE1 
2992 C CE2 . PHE B 191 ? 0.8448 0.5970 0.6956 0.0778  -0.0107 -0.0283 406 PHE A CE2 
2993 C CZ  . PHE B 191 ? 0.8309 0.6056 0.7017 0.0764  -0.0156 -0.0251 406 PHE A CZ  
2994 N N   . THR B 192 ? 0.7856 0.5635 0.6474 0.0259  -0.0331 -0.0086 407 THR A N   
2995 C CA  . THR B 192 ? 0.8135 0.6049 0.6933 0.0309  -0.0350 -0.0003 407 THR A CA  
2996 C C   . THR B 192 ? 0.8120 0.5827 0.6874 0.0338  -0.0315 -0.0051 407 THR A C   
2997 O O   . THR B 192 ? 0.7923 0.5356 0.6473 0.0307  -0.0268 -0.0121 407 THR A O   
2998 C CB  . THR B 192 ? 0.7999 0.6245 0.6848 0.0199  -0.0409 0.0092  407 THR A CB  
2999 O OG1 . THR B 192 ? 0.8343 0.6530 0.7007 -0.0017 -0.0414 0.0012  407 THR A OG1 
3000 C CG2 . THR B 192 ? 0.8259 0.6769 0.7116 0.0201  -0.0445 0.0182  407 THR A CG2 
3001 N N   . ILE B 193 ? 0.7624 0.5428 0.6536 0.0415  -0.0312 -0.0002 408 ILE A N   
3002 C CA  . ILE B 193 ? 0.7732 0.5408 0.6606 0.0453  -0.0282 -0.0017 408 ILE A CA  
3003 C C   . ILE B 193 ? 0.7563 0.5414 0.6544 0.0400  -0.0293 0.0049  408 ILE A C   
3004 O O   . ILE B 193 ? 0.7409 0.5473 0.6562 0.0460  -0.0292 0.0107  408 ILE A O   
3005 C CB  . ILE B 193 ? 0.7495 0.5187 0.6431 0.0595  -0.0254 -0.0050 408 ILE A CB  
3006 C CG1 . ILE B 193 ? 0.7469 0.5104 0.6320 0.0660  -0.0237 -0.0103 408 ILE A CG1 
3007 C CG2 . ILE B 193 ? 0.7843 0.5473 0.6719 0.0647  -0.0231 -0.0031 408 ILE A CG2 
3008 C CD1 . ILE B 193 ? 0.7941 0.5773 0.6873 0.0747  -0.0219 -0.0143 408 ILE A CD1 
3009 N N   . LEU B 194 ? 0.7873 0.5605 0.6727 0.0300  -0.0273 0.0046  409 LEU A N   
3010 C CA  . LEU B 194 ? 0.7741 0.5677 0.6683 0.0226  -0.0270 0.0102  409 LEU A CA  
3011 C C   . LEU B 194 ? 0.7863 0.5615 0.6736 0.0302  -0.0219 0.0104  409 LEU A C   
3012 O O   . LEU B 194 ? 0.7935 0.5352 0.6592 0.0327  -0.0173 0.0085  409 LEU A O   
3013 C CB  . LEU B 194 ? 0.7756 0.5776 0.6576 -0.0038 -0.0277 0.0096  409 LEU A CB  
3014 C CG  . LEU B 194 ? 0.7471 0.5862 0.6419 -0.0142 -0.0276 0.0162  409 LEU A CG  
3015 C CD1 . LEU B 194 ? 0.7176 0.6093 0.6414 -0.0009 -0.0324 0.0265  409 LEU A CD1 
3016 C CD2 . LEU B 194 ? 0.8158 0.6584 0.6905 -0.0492 -0.0253 0.0115  409 LEU A CD2 
3017 N N   . GLN B 195 ? 0.7426 0.5392 0.6457 0.0367  -0.0207 0.0138  410 GLN A N   
3018 C CA  . GLN B 195 ? 0.7237 0.5126 0.6203 0.0427  -0.0164 0.0148  410 GLN A CA  
3019 C C   . GLN B 195 ? 0.7266 0.5343 0.6287 0.0326  -0.0134 0.0198  410 GLN A C   
3020 O O   . GLN B 195 ? 0.6964 0.5347 0.6186 0.0359  -0.0128 0.0220  410 GLN A O   
3021 C CB  . GLN B 195 ? 0.7191 0.5182 0.6252 0.0570  -0.0156 0.0101  410 GLN A CB  
3022 C CG  . GLN B 195 ? 0.7753 0.5649 0.6737 0.0655  -0.0176 0.0057  410 GLN A CG  
3023 C CD  . GLN B 195 ? 0.8443 0.6523 0.7452 0.0721  -0.0159 0.0002  410 GLN A CD  
3024 O OE1 . GLN B 195 ? 0.8258 0.6427 0.7218 0.0791  -0.0176 -0.0025 410 GLN A OE1 
3025 N NE2 . GLN B 195 ? 0.8672 0.6867 0.7756 0.0686  -0.0113 -0.0030 410 GLN A NE2 
3026 N N   . VAL B 196 ? 0.7514 0.5391 0.6334 0.0223  -0.0088 0.0228  411 VAL A N   
3027 C CA  . VAL B 196 ? 0.7951 0.6010 0.6788 0.0085  -0.0043 0.0273  411 VAL A CA  
3028 C C   . VAL B 196 ? 0.7955 0.5902 0.6680 0.0185  0.0011  0.0310  411 VAL A C   
3029 O O   . VAL B 196 ? 0.7607 0.5184 0.6070 0.0218  0.0057  0.0352  411 VAL A O   
3030 C CB  . VAL B 196 ? 0.8176 0.6089 0.6813 -0.0204 -0.0004 0.0271  411 VAL A CB  
3031 C CG1 . VAL B 196 ? 0.7499 0.5799 0.6226 -0.0397 0.0031  0.0310  411 VAL A CG1 
3032 C CG2 . VAL B 196 ? 0.7775 0.5757 0.6438 -0.0305 -0.0066 0.0216  411 VAL A CG2 
3033 N N   . VAL B 197 ? 0.7803 0.6064 0.6701 0.0260  0.0025  0.0305  412 VAL A N   
3034 C CA  . VAL B 197 ? 0.7729 0.6000 0.6522 0.0312  0.0078  0.0334  412 VAL A CA  
3035 C C   . VAL B 197 ? 0.7824 0.6258 0.6616 0.0146  0.0145  0.0388  412 VAL A C   
3036 O O   . VAL B 197 ? 0.7489 0.6292 0.6509 0.0112  0.0157  0.0377  412 VAL A O   
3037 C CB  . VAL B 197 ? 0.7959 0.6446 0.6879 0.0452  0.0086  0.0253  412 VAL A CB  
3038 C CG1 . VAL B 197 ? 0.7675 0.6223 0.6432 0.0485  0.0128  0.0277  412 VAL A CG1 
3039 C CG2 . VAL B 197 ? 0.7379 0.5791 0.6335 0.0549  0.0031  0.0177  412 VAL A CG2 
3040 N N   . THR B 198 ? 0.8071 0.6245 0.6594 0.0060  0.0207  0.0466  413 THR A N   
3041 C CA  . THR B 198 ? 0.8241 0.6539 0.6709 -0.0145 0.0292  0.0517  413 THR A CA  
3042 C C   . THR B 198 ? 0.8547 0.6768 0.6820 -0.0068 0.0360  0.0594  413 THR A C   
3043 O O   . THR B 198 ? 0.8301 0.6316 0.6410 0.0120  0.0343  0.0636  413 THR A O   
3044 C CB  . THR B 198 ? 0.8521 0.6488 0.6752 -0.0423 0.0351  0.0541  413 THR A CB  
3045 O OG1 . THR B 198 ? 0.9194 0.6535 0.7062 -0.0332 0.0413  0.0608  413 THR A OG1 
3046 C CG2 . THR B 198 ? 0.8172 0.6261 0.6550 -0.0525 0.0274  0.0461  413 THR A CG2 
3047 N N   . ASN B 199 ? 0.8988 0.7471 0.7287 -0.0212 0.0438  0.0622  414 ASN A N   
3048 C CA  . ASN B 199 ? 0.9187 0.7616 0.7259 -0.0197 0.0523  0.0714  414 ASN A CA  
3049 C C   . ASN B 199 ? 0.9552 0.7375 0.7201 -0.0289 0.0615  0.0850  414 ASN A C   
3050 O O   . ASN B 199 ? 0.9763 0.7391 0.7275 -0.0579 0.0708  0.0866  414 ASN A O   
3051 C CB  . ASN B 199 ? 0.9221 0.8103 0.7440 -0.0353 0.0602  0.0704  414 ASN A CB  
3052 C CG  . ASN B 199 ? 0.9020 0.7992 0.7077 -0.0292 0.0676  0.0762  414 ASN A CG  
3053 O OD1 . ASN B 199 ? 0.9414 0.8046 0.7148 -0.0224 0.0701  0.0876  414 ASN A OD1 
3054 N ND2 . ASN B 199 ? 0.8830 0.8287 0.7096 -0.0285 0.0726  0.0696  414 ASN A ND2 
3055 N N   . ARG B 200 ? 0.9269 0.6799 0.6684 -0.0044 0.0612  0.0951  415 ARG A N   
3056 C CA  . ARG B 200 ? 1.0182 0.7036 0.7143 -0.0038 0.0747  0.1120  415 ARG A CA  
3057 C C   . ARG B 200 ? 1.0700 0.7375 0.7404 -0.0304 0.0915  0.1214  415 ARG A C   
3058 O O   . ARG B 200 ? 1.0926 0.7063 0.7346 -0.0562 0.1061  0.1236  415 ARG A O   
3059 C CB  . ARG B 200 ? 1.0206 0.6988 0.6978 0.0337  0.0728  0.1273  415 ARG A CB  
3060 C CG  . ARG B 200 ? 1.0343 0.6364 0.6675 0.0492  0.0872  0.1459  415 ARG A CG  
3061 C CD  . ARG B 200 ? 1.0860 0.6380 0.6744 0.0391  0.1087  0.1654  415 ARG A CD  
3062 N NE  . ARG B 200 ? 1.1910 0.7910 0.7789 0.0507  0.1059  0.1771  415 ARG A NE  
3063 C CZ  . ARG B 200 ? 1.1645 0.7728 0.7312 0.0873  0.1065  0.1997  415 ARG A CZ  
3064 N NH1 . ARG B 200 ? 1.1469 0.7155 0.6901 0.1210  0.1122  0.2168  415 ARG A NH1 
3065 N NH2 . ARG B 200 ? 1.1366 0.8000 0.7049 0.0914  0.1020  0.2059  415 ARG A NH2 
3066 N N   . ASP B 201 ? 0.9824 0.6947 0.6600 -0.0287 0.0916  0.1247  416 ASP A N   
3067 C CA  . ASP B 201 ? 1.0701 0.7667 0.7190 -0.0507 0.1088  0.1368  416 ASP A CA  
3068 C C   . ASP B 201 ? 1.0818 0.7940 0.7433 -0.0938 0.1154  0.1253  416 ASP A C   
3069 O O   . ASP B 201 ? 1.1516 0.8371 0.7826 -0.1221 0.1333  0.1338  416 ASP A O   
3070 C CB  . ASP B 201 ? 1.0461 0.7959 0.7016 -0.0385 0.1067  0.1409  416 ASP A CB  
3071 C CG  . ASP B 201 ? 1.0851 0.8294 0.7191 -0.0019 0.1025  0.1564  416 ASP A CG  
3072 O OD1 . ASP B 201 ? 1.1197 0.8069 0.7231 0.0148  0.1081  0.1724  416 ASP A OD1 
3073 O OD2 . ASP B 201 ? 1.0666 0.8670 0.7134 0.0106  0.0947  0.1520  416 ASP A OD2 
3074 N N   . THR B 202 ? 1.0568 0.8169 0.7611 -0.0999 0.1025  0.1076  417 THR A N   
3075 C CA  . THR B 202 ? 1.0258 0.8335 0.7511 -0.1356 0.1060  0.0987  417 THR A CA  
3076 C C   . THR B 202 ? 1.0759 0.8920 0.8189 -0.1526 0.0984  0.0861  417 THR A C   
3077 O O   . THR B 202 ? 1.0607 0.9268 0.8208 -0.1848 0.1004  0.0797  417 THR A O   
3078 C CB  . THR B 202 ? 0.9936 0.8825 0.7595 -0.1226 0.1005  0.0933  417 THR A CB  
3079 O OG1 . THR B 202 ? 1.0607 0.9974 0.8358 -0.1560 0.1104  0.0925  417 THR A OG1 
3080 C CG2 . THR B 202 ? 0.9513 0.8794 0.7598 -0.1001 0.0850  0.0810  417 THR A CG2 
3081 N N   . GLN B 203 ? 1.1549 0.9315 0.8941 -0.1327 0.0898  0.0831  418 GLN A N   
3082 C CA  . GLN B 203 ? 1.1412 0.9150 0.8886 -0.1475 0.0833  0.0719  418 GLN A CA  
3083 C C   . GLN B 203 ? 1.0989 0.9566 0.8987 -0.1412 0.0679  0.0630  418 GLN A C   
3084 O O   . GLN B 203 ? 1.1074 0.9754 0.9166 -0.1523 0.0608  0.0553  418 GLN A O   
3085 C CB  . GLN B 203 ? 1.1962 0.9374 0.9095 -0.1986 0.0988  0.0677  418 GLN A CB  
3086 C CG  . GLN B 203 ? 1.3008 0.9422 0.9535 -0.2047 0.1205  0.0783  418 GLN A CG  
3087 C CD  . GLN B 203 ? 1.3946 0.9668 1.0268 -0.1681 0.1194  0.0828  418 GLN A CD  
3088 O OE1 . GLN B 203 ? 1.4342 0.9898 1.0606 -0.1276 0.1179  0.0970  418 GLN A OE1 
3089 N NE2 . GLN B 203 ? 1.4131 0.9553 1.0359 -0.1817 0.1195  0.0705  418 GLN A NE2 
3090 N N   . GLU B 204 ? 0.9475 0.8628 0.7783 -0.1220 0.0650  0.0649  419 GLU A N   
3091 C CA  . GLU B 204 ? 0.8769 0.8614 0.7531 -0.1062 0.0551  0.0604  419 GLU A CA  
3092 C C   . GLU B 204 ? 0.8135 0.7745 0.6994 -0.0771 0.0434  0.0558  419 GLU A C   
3093 O O   . GLU B 204 ? 0.7898 0.7035 0.6589 -0.0573 0.0420  0.0557  419 GLU A O   
3094 C CB  . GLU B 204 ? 0.8589 0.8913 0.7571 -0.0872 0.0606  0.0629  419 GLU A CB  
3095 C CG  . GLU B 204 ? 0.9321 0.9844 0.8174 -0.1136 0.0738  0.0683  419 GLU A CG  
3096 C CD  . GLU B 204 ? 0.9023 1.0114 0.8122 -0.0949 0.0811  0.0693  419 GLU A CD  
3097 O OE1 . GLU B 204 ? 0.8983 0.9856 0.8046 -0.0665 0.0819  0.0663  419 GLU A OE1 
3098 O OE2 . GLU B 204 ? 0.8584 1.0367 0.7896 -0.1095 0.0873  0.0721  419 GLU A OE2 
3099 N N   . LEU B 205 ? 0.7799 0.7819 0.6928 -0.0745 0.0354  0.0533  420 LEU A N   
3100 C CA  . LEU B 205 ? 0.7304 0.7162 0.6542 -0.0484 0.0260  0.0496  420 LEU A CA  
3101 C C   . LEU B 205 ? 0.6613 0.6688 0.6083 -0.0152 0.0287  0.0494  420 LEU A C   
3102 O O   . LEU B 205 ? 0.6576 0.7187 0.6278 -0.0083 0.0346  0.0537  420 LEU A O   
3103 C CB  . LEU B 205 ? 0.7206 0.7406 0.6589 -0.0598 0.0180  0.0494  420 LEU A CB  
3104 C CG  . LEU B 205 ? 0.6876 0.7198 0.6496 -0.0272 0.0117  0.0504  420 LEU A CG  
3105 C CD1 . LEU B 205 ? 0.7061 0.6727 0.6498 -0.0145 0.0079  0.0435  420 LEU A CD1 
3106 C CD2 . LEU B 205 ? 0.7143 0.7990 0.6935 -0.0348 0.0042  0.0550  420 LEU A CD2 
3107 N N   . LEU B 206 ? 0.6910 0.6582 0.6295 0.0046  0.0267  0.0436  421 LEU A N   
3108 C CA  . LEU B 206 ? 0.6887 0.6639 0.6394 0.0291  0.0336  0.0388  421 LEU A CA  
3109 C C   . LEU B 206 ? 0.7211 0.6924 0.6863 0.0471  0.0311  0.0365  421 LEU A C   
3110 O O   . LEU B 206 ? 0.7214 0.7243 0.7074 0.0618  0.0378  0.0418  421 LEU A O   
3111 C CB  . LEU B 206 ? 0.7248 0.6689 0.6533 0.0333  0.0359  0.0322  421 LEU A CB  
3112 C CG  . LEU B 206 ? 0.7285 0.6742 0.6382 0.0199  0.0409  0.0377  421 LEU A CG  
3113 C CD1 . LEU B 206 ? 0.7364 0.6610 0.6226 0.0268  0.0406  0.0345  421 LEU A CD1 
3114 C CD2 . LEU B 206 ? 0.6751 0.6639 0.5997 0.0184  0.0524  0.0396  421 LEU A CD2 
3115 N N   . LEU B 207 ? 0.7356 0.6697 0.6890 0.0485  0.0236  0.0306  422 LEU A N   
3116 C CA  . LEU B 207 ? 0.7128 0.6388 0.6756 0.0601  0.0206  0.0295  422 LEU A CA  
3117 C C   . LEU B 207 ? 0.7066 0.6261 0.6646 0.0465  0.0083  0.0327  422 LEU A C   
3118 O O   . LEU B 207 ? 0.6657 0.5625 0.6046 0.0323  0.0040  0.0313  422 LEU A O   
3119 C CB  . LEU B 207 ? 0.6828 0.5757 0.6349 0.0690  0.0236  0.0176  422 LEU A CB  
3120 C CG  . LEU B 207 ? 0.7445 0.6306 0.6929 0.0781  0.0387  0.0077  422 LEU A CG  
3121 C CD1 . LEU B 207 ? 0.7594 0.6200 0.6922 0.0740  0.0375  -0.0063 422 LEU A CD1 
3122 C CD2 . LEU B 207 ? 0.7667 0.6574 0.7293 0.0968  0.0532  0.0125  422 LEU A CD2 
3123 N N   . CYS B 208 ? 0.7029 0.6391 0.6745 0.0527  0.0052  0.0378  423 CYS A N   
3124 C CA  . CYS B 208 ? 0.6939 0.6206 0.6584 0.0413  -0.0052 0.0375  423 CYS A CA  
3125 C C   . CYS B 208 ? 0.6614 0.5845 0.6349 0.0595  -0.0049 0.0396  423 CYS A C   
3126 O O   . CYS B 208 ? 0.6299 0.5855 0.6202 0.0738  -0.0005 0.0505  423 CYS A O   
3127 C CB  . CYS B 208 ? 0.6856 0.6517 0.6531 0.0192  -0.0102 0.0436  423 CYS A CB  
3128 S SG  . CYS B 208 ? 0.6762 0.6378 0.6328 0.0031  -0.0207 0.0411  423 CYS A SG  
3129 N N   . THR B 209 ? 0.6464 0.5320 0.6079 0.0610  -0.0074 0.0310  424 THR A N   
3130 C CA  . THR B 209 ? 0.6683 0.5424 0.6328 0.0735  -0.0054 0.0317  424 THR A CA  
3131 C C   . THR B 209 ? 0.7033 0.5728 0.6602 0.0634  -0.0156 0.0312  424 THR A C   
3132 O O   . THR B 209 ? 0.6886 0.5379 0.6307 0.0515  -0.0206 0.0235  424 THR A O   
3133 C CB  . THR B 209 ? 0.7121 0.5531 0.6678 0.0790  0.0020  0.0197  424 THR A CB  
3134 O OG1 . THR B 209 ? 0.7791 0.6210 0.7345 0.0817  0.0110  0.0153  424 THR A OG1 
3135 C CG2 . THR B 209 ? 0.7177 0.5430 0.6747 0.0910  0.0114  0.0217  424 THR A CG2 
3136 N N   . ALA B 210 ? 0.7042 0.5900 0.6685 0.0713  -0.0161 0.0406  425 ALA A N   
3137 C CA  . ALA B 210 ? 0.6719 0.5515 0.6273 0.0641  -0.0234 0.0392  425 ALA A CA  
3138 C C   . ALA B 210 ? 0.7034 0.5518 0.6548 0.0759  -0.0164 0.0356  425 ALA A C   
3139 O O   . ALA B 210 ? 0.7039 0.5458 0.6608 0.0920  -0.0047 0.0421  425 ALA A O   
3140 C CB  . ALA B 210 ? 0.6723 0.5989 0.6354 0.0626  -0.0292 0.0535  425 ALA A CB  
3141 N N   . TYR B 211 ? 0.6755 0.5024 0.6150 0.0674  -0.0203 0.0248  426 TYR A N   
3142 C CA  . TYR B 211 ? 0.7096 0.5150 0.6440 0.0716  -0.0143 0.0200  426 TYR A CA  
3143 C C   . TYR B 211 ? 0.7175 0.5280 0.6459 0.0682  -0.0194 0.0245  426 TYR A C   
3144 O O   . TYR B 211 ? 0.7244 0.5394 0.6447 0.0573  -0.0276 0.0198  426 TYR A O   
3145 C CB  . TYR B 211 ? 0.6919 0.4829 0.6191 0.0662  -0.0140 0.0050  426 TYR A CB  
3146 C CG  . TYR B 211 ? 0.7135 0.5042 0.6430 0.0675  -0.0093 -0.0003 426 TYR A CG  
3147 C CD1 . TYR B 211 ? 0.7522 0.5321 0.6821 0.0697  0.0033  -0.0044 426 TYR A CD1 
3148 C CD2 . TYR B 211 ? 0.7421 0.5386 0.6687 0.0655  -0.0148 -0.0013 426 TYR A CD2 
3149 C CE1 . TYR B 211 ? 0.7788 0.5606 0.7073 0.0681  0.0085  -0.0115 426 TYR A CE1 
3150 C CE2 . TYR B 211 ? 0.7773 0.5779 0.7041 0.0665  -0.0108 -0.0049 426 TYR A CE2 
3151 C CZ  . TYR B 211 ? 0.7471 0.5440 0.6757 0.0670  -0.0001 -0.0110 426 TYR A CZ  
3152 O OH  . TYR B 211 ? 0.8042 0.6072 0.7298 0.0653  0.0046  -0.0169 426 TYR A OH  
3153 N N   . VAL B 212 ? 0.7275 0.5317 0.6556 0.0773  -0.0115 0.0335  427 VAL A N   
3154 C CA  . VAL B 212 ? 0.7391 0.5451 0.6586 0.0746  -0.0138 0.0379  427 VAL A CA  
3155 C C   . VAL B 212 ? 0.7629 0.5375 0.6741 0.0736  -0.0015 0.0308  427 VAL A C   
3156 O O   . VAL B 212 ? 0.7528 0.5052 0.6636 0.0758  0.0109  0.0258  427 VAL A O   
3157 C CB  . VAL B 212 ? 0.7576 0.5912 0.6802 0.0862  -0.0145 0.0603  427 VAL A CB  
3158 C CG1 . VAL B 212 ? 0.7527 0.6310 0.6823 0.0785  -0.0275 0.0644  427 VAL A CG1 
3159 C CG2 . VAL B 212 ? 0.7199 0.5364 0.6459 0.1087  0.0025  0.0749  427 VAL A CG2 
3160 N N   . PHE B 213 ? 0.7667 0.5406 0.6686 0.0667  -0.0034 0.0287  428 PHE A N   
3161 C CA  . PHE B 213 ? 0.7748 0.5292 0.6692 0.0577  0.0063  0.0166  428 PHE A CA  
3162 C C   . PHE B 213 ? 0.7607 0.5048 0.6427 0.0564  0.0139  0.0255  428 PHE A C   
3163 O O   . PHE B 213 ? 0.7801 0.5417 0.6583 0.0590  0.0059  0.0359  428 PHE A O   
3164 C CB  . PHE B 213 ? 0.7497 0.5184 0.6451 0.0490  -0.0018 0.0000  428 PHE A CB  
3165 C CG  . PHE B 213 ? 0.7319 0.5067 0.6349 0.0510  -0.0058 -0.0077 428 PHE A CG  
3166 C CD1 . PHE B 213 ? 0.7385 0.5128 0.6432 0.0456  0.0014  -0.0182 428 PHE A CD1 
3167 C CD2 . PHE B 213 ? 0.7438 0.5257 0.6483 0.0547  -0.0156 -0.0049 428 PHE A CD2 
3168 C CE1 . PHE B 213 ? 0.7430 0.5282 0.6528 0.0483  -0.0026 -0.0232 428 PHE A CE1 
3169 C CE2 . PHE B 213 ? 0.7467 0.5310 0.6549 0.0574  -0.0175 -0.0094 428 PHE A CE2 
3170 C CZ  . PHE B 213 ? 0.7062 0.4944 0.6179 0.0564  -0.0119 -0.0172 428 PHE A CZ  
3171 N N   . GLU B 214 ? 0.7699 0.4848 0.6422 0.0492  0.0311  0.0207  429 GLU A N   
3172 C CA  . GLU B 214 ? 0.7767 0.4766 0.6334 0.0402  0.0418  0.0230  429 GLU A CA  
3173 C C   . GLU B 214 ? 0.7792 0.4729 0.6318 0.0178  0.0520  0.0010  429 GLU A C   
3174 O O   . GLU B 214 ? 0.8253 0.5336 0.6875 0.0122  0.0479  -0.0138 429 GLU A O   
3175 C CB  . GLU B 214 ? 0.7973 0.4606 0.6385 0.0537  0.0596  0.0455  429 GLU A CB  
3176 C CG  . GLU B 214 ? 0.8092 0.4991 0.6558 0.0759  0.0480  0.0700  429 GLU A CG  
3177 C CD  . GLU B 214 ? 0.8799 0.5426 0.7087 0.0946  0.0656  0.0978  429 GLU A CD  
3178 O OE1 . GLU B 214 ? 0.8971 0.5117 0.7045 0.0857  0.0875  0.0963  429 GLU A OE1 
3179 O OE2 . GLU B 214 ? 0.9553 0.6471 0.7895 0.1180  0.0590  0.1225  429 GLU A OE2 
3180 N N   . VAL B 215 ? 0.7901 0.4669 0.6266 0.0031  0.0662  -0.0005 430 VAL A N   
3181 C CA  . VAL B 215 ? 0.8279 0.5142 0.6601 -0.0247 0.0754  -0.0225 430 VAL A CA  
3182 C C   . VAL B 215 ? 0.9031 0.5314 0.7087 -0.0416 0.1045  -0.0233 430 VAL A C   
3183 O O   . VAL B 215 ? 0.9302 0.5164 0.7174 -0.0321 0.1181  -0.0038 430 VAL A O   
3184 C CB  . VAL B 215 ? 0.8247 0.5500 0.6597 -0.0335 0.0681  -0.0278 430 VAL A CB  
3185 C CG1 . VAL B 215 ? 0.8444 0.5813 0.6707 -0.0658 0.0831  -0.0462 430 VAL A CG1 
3186 C CG2 . VAL B 215 ? 0.7493 0.5221 0.6047 -0.0195 0.0465  -0.0332 430 VAL A CG2 
3187 N N   . SER B 216 ? 0.9083 0.5324 0.7081 -0.0662 0.1161  -0.0449 431 SER A N   
3188 C CA  . SER B 216 ? 0.9820 0.5453 0.7490 -0.0925 0.1488  -0.0528 431 SER A CA  
3189 C C   . SER B 216 ? 1.0178 0.6038 0.7745 -0.1293 0.1570  -0.0682 431 SER A C   
3190 O O   . SER B 216 ? 1.0090 0.6605 0.7866 -0.1287 0.1373  -0.0708 431 SER A O   
3191 C CB  . SER B 216 ? 0.9561 0.5022 0.7156 -0.1079 0.1604  -0.0722 431 SER A CB  
3192 O OG  . SER B 216 ? 1.0955 0.5685 0.8148 -0.1367 0.1977  -0.0821 431 SER A OG  
3193 N N   . THR B 217 ? 1.1113 0.6412 0.8331 -0.1630 0.1895  -0.0794 432 THR A N   
3194 C CA  . THR B 217 ? 1.1532 0.7094 0.8629 -0.2079 0.2009  -0.0986 432 THR A CA  
3195 C C   . THR B 217 ? 1.1937 0.7851 0.9002 -0.2507 0.2071  -0.1323 432 THR A C   
3196 O O   . THR B 217 ? 1.1833 0.7645 0.8910 -0.2461 0.2065  -0.1405 432 THR A O   
3197 C CB  . THR B 217 ? 1.2014 0.6710 0.8676 -0.2240 0.2360  -0.0887 432 THR A CB  
3198 O OG1 . THR B 217 ? 1.3180 0.7021 0.9460 -0.2447 0.2707  -0.0998 432 THR A OG1 
3199 C CG2 . THR B 217 ? 1.1581 0.5921 0.8245 -0.1756 0.2306  -0.0508 432 THR A CG2 
3200 N N   . SER B 218 ? 1.2810 0.9248 0.9839 -0.2941 0.2126  -0.1522 433 SER A N   
3201 C CA  . SER B 218 ? 1.2490 0.9478 0.9485 -0.3415 0.2175  -0.1853 433 SER A CA  
3202 C C   . SER B 218 ? 1.2989 0.9035 0.9521 -0.3755 0.2539  -0.2027 433 SER A C   
3203 O O   . SER B 218 ? 1.2596 0.8790 0.9127 -0.3854 0.2521  -0.2200 433 SER A O   
3204 C CB  . SER B 218 ? 1.2385 1.0123 0.9398 -0.3844 0.2208  -0.2010 433 SER A CB  
3205 O OG  . SER B 218 ? 1.2281 0.9368 0.9042 -0.3905 0.2414  -0.1879 433 SER A OG  
3206 N N   . GLU B 219 ? 1.3289 0.8313 0.9380 -0.3933 0.2901  -0.1982 434 GLU A N   
3207 C CA  . GLU B 219 ? 1.4027 0.8090 0.9668 -0.4013 0.3259  -0.2034 434 GLU A CA  
3208 C C   . GLU B 219 ? 1.4142 0.7547 0.9848 -0.3399 0.3223  -0.1753 434 GLU A C   
3209 O O   . GLU B 219 ? 1.4043 0.7200 0.9887 -0.2978 0.3111  -0.1452 434 GLU A O   
3210 C CB  . GLU B 219 ? 1.4482 0.7904 0.9650 -0.4226 0.3625  -0.2007 434 GLU A CB  
3211 C CG  . GLU B 219 ? 1.4783 0.7187 0.9722 -0.3751 0.3810  -0.1649 434 GLU A CG  
3212 C CD  . GLU B 219 ? 1.5854 0.7627 1.0250 -0.4028 0.4208  -0.1701 434 GLU A CD  
3213 O OE1 . GLU B 219 ? 1.6560 0.8118 1.0595 -0.4380 0.4479  -0.1959 434 GLU A OE1 
3214 O OE2 . GLU B 219 ? 1.6132 0.7632 1.0429 -0.3926 0.4263  -0.1500 434 GLU A OE2 
3215 N N   . ARG B 220 ? 1.4114 0.7337 0.9726 -0.3359 0.3316  -0.1848 435 ARG A N   
3216 C CA  . ARG B 220 ? 1.4105 0.6951 0.9826 -0.2836 0.3266  -0.1647 435 ARG A CA  
3217 C C   . ARG B 220 ? 1.3351 0.6856 0.9520 -0.2641 0.2874  -0.1671 435 ARG A C   
3218 O O   . ARG B 220 ? 1.3393 0.6739 0.9660 -0.2291 0.2825  -0.1570 435 ARG A O   
3219 C CB  . ARG B 220 ? 1.3795 0.5937 0.9430 -0.2306 0.3375  -0.1248 435 ARG A CB  
3220 C CG  . ARG B 220 ? 1.3058 0.5404 0.9019 -0.1897 0.3090  -0.0958 435 ARG A CG  
3221 C CD  . ARG B 220 ? 1.3453 0.5243 0.9324 -0.1340 0.3223  -0.0590 435 ARG A CD  
3222 N NE  . ARG B 220 ? 1.3891 0.5574 0.9778 -0.1031 0.3178  -0.0250 435 ARG A NE  
3223 C CZ  . ARG B 220 ? 1.4054 0.5476 0.9919 -0.0519 0.3243  0.0099  435 ARG A CZ  
3224 N NH1 . ARG B 220 ? 1.3642 0.4889 0.9503 -0.0239 0.3348  0.0159  435 ARG A NH1 
3225 N NH2 . ARG B 220 ? 1.3647 0.5048 0.9487 -0.0291 0.3210  0.0399  435 ARG A NH2 
3226 N N   . GLY B 221 ? 1.2298 0.6839 0.8813 -0.2740 0.2551  -0.1730 436 GLY A N   
3227 C CA  . GLY B 221 ? 1.1470 0.6939 0.8416 -0.2524 0.2174  -0.1733 436 GLY A CA  
3228 C C   . GLY B 221 ? 1.0774 0.6093 0.7948 -0.1959 0.2003  -0.1474 436 GLY A C   
3229 O O   . GLY B 221 ? 1.0741 0.5328 0.7795 -0.1659 0.2143  -0.1247 436 GLY A O   
3230 N N   . ALA B 222 ? 1.0141 0.6205 0.7634 -0.1815 0.1709  -0.1494 437 ALA A N   
3231 C CA  . ALA B 222 ? 0.9600 0.5674 0.7332 -0.1345 0.1518  -0.1276 437 ALA A CA  
3232 C C   . ALA B 222 ? 0.9642 0.4872 0.7162 -0.1175 0.1764  -0.1194 437 ALA A C   
3233 O O   . ALA B 222 ? 1.0728 0.5463 0.7926 -0.1438 0.2054  -0.1392 437 ALA A O   
3234 C CB  . ALA B 222 ? 0.8884 0.5715 0.6847 -0.1329 0.1279  -0.1371 437 ALA A CB  
3235 N N   . GLN B 223 ? 0.8686 0.3774 0.6365 -0.0735 0.1668  -0.0903 438 GLN A N   
3236 C CA  . GLN B 223 ? 0.9530 0.4044 0.7103 -0.0463 0.1850  -0.0775 438 GLN A CA  
3237 C C   . GLN B 223 ? 0.9405 0.4373 0.7330 -0.0070 0.1567  -0.0548 438 GLN A C   
3238 O O   . GLN B 223 ? 0.8757 0.4282 0.6931 -0.0002 0.1281  -0.0469 438 GLN A O   
3239 C CB  . GLN B 223 ? 1.0527 0.4190 0.7794 -0.0328 0.2178  -0.0597 438 GLN A CB  
3240 C CG  . GLN B 223 ? 1.1266 0.4457 0.8467 0.0052  0.2365  -0.0422 438 GLN A CG  
3241 C CD  . GLN B 223 ? 1.2370 0.5203 0.9296 -0.0157 0.2654  -0.0631 438 GLN A CD  
3242 O OE1 . GLN B 223 ? 1.3189 0.5695 0.9795 -0.0532 0.2886  -0.0818 438 GLN A OE1 
3243 N NE2 . GLN B 223 ? 1.1573 0.4509 0.8605 0.0030  0.2642  -0.0632 438 GLN A NE2 
3244 N N   . HIS B 224 ? 0.9646 0.4366 0.7562 0.0167  0.1674  -0.0462 439 HIS A N   
3245 C CA  . HIS B 224 ? 0.9477 0.4633 0.7698 0.0497  0.1445  -0.0252 439 HIS A CA  
3246 C C   . HIS B 224 ? 0.9238 0.3959 0.7375 0.0841  0.1676  -0.0038 439 HIS A C   
3247 O O   . HIS B 224 ? 0.9927 0.3932 0.7745 0.0839  0.2028  -0.0069 439 HIS A O   
3248 C CB  . HIS B 224 ? 0.9335 0.4986 0.7730 0.0405  0.1253  -0.0402 439 HIS A CB  
3249 C CG  . HIS B 224 ? 0.9463 0.4809 0.7660 0.0271  0.1475  -0.0602 439 HIS A CG  
3250 N ND1 . HIS B 224 ? 0.9800 0.4940 0.7990 0.0506  0.1613  -0.0520 439 HIS A ND1 
3251 C CD2 . HIS B 224 ? 0.9865 0.5087 0.7831 -0.0095 0.1613  -0.0893 439 HIS A CD2 
3252 C CE1 . HIS B 224 ? 0.9882 0.4717 0.7827 0.0297  0.1831  -0.0764 439 HIS A CE1 
3253 N NE2 . HIS B 224 ? 1.0318 0.5206 0.8112 -0.0093 0.1832  -0.1001 439 HIS A NE2 
3254 N N   . HIS B 225 ? 0.9235 0.4396 0.7636 0.1141  0.1499  0.0192  440 HIS A N   
3255 C CA  . HIS B 225 ? 0.9861 0.4824 0.8248 0.1531  0.1693  0.0437  440 HIS A CA  
3256 C C   . HIS B 225 ? 0.9202 0.4875 0.7922 0.1669  0.1444  0.0528  440 HIS A C   
3257 O O   . HIS B 225 ? 0.8717 0.4965 0.7654 0.1651  0.1156  0.0620  440 HIS A O   
3258 C CB  . HIS B 225 ? 0.9931 0.4711 0.8232 0.1800  0.1795  0.0745  440 HIS A CB  
3259 C CG  . HIS B 225 ? 1.0414 0.5109 0.8675 0.2173  0.2019  0.0991  440 HIS A CG  
3260 N ND1 . HIS B 225 ? 1.1620 0.6127 0.9721 0.2366  0.2186  0.1226  440 HIS A ND1 
3261 C CD2 . HIS B 225 ? 1.0475 0.5348 0.8843 0.2394  0.2096  0.1049  440 HIS A CD2 
3262 C CE1 . HIS B 225 ? 1.1897 0.6446 0.9992 0.2698  0.2371  0.1414  440 HIS A CE1 
3263 N NE2 . HIS B 225 ? 1.1424 0.6204 0.9688 0.2717  0.2318  0.1308  440 HIS A NE2 
3264 N N   . ILE B 226 ? 0.9307 0.4907 0.8026 0.1755  0.1575  0.0469  441 ILE A N   
3265 C CA  . ILE B 226 ? 0.9004 0.5235 0.8000 0.1809  0.1373  0.0503  441 ILE A CA  
3266 C C   . ILE B 226 ? 0.9021 0.5548 0.8167 0.2221  0.1440  0.0828  441 ILE A C   
3267 O O   . ILE B 226 ? 0.9689 0.5766 0.8675 0.2516  0.1758  0.0953  441 ILE A O   
3268 C CB  . ILE B 226 ? 0.8574 0.4641 0.7480 0.1662  0.1481  0.0260  441 ILE A CB  
3269 C CG1 . ILE B 226 ? 0.8738 0.4725 0.7522 0.1260  0.1380  -0.0030 441 ILE A CG1 
3270 C CG2 . ILE B 226 ? 0.8350 0.5012 0.7509 0.1751  0.1330  0.0332  441 ILE A CG2 
3271 C CD1 . ILE B 226 ? 0.8742 0.4693 0.7417 0.1066  0.1446  -0.0275 441 ILE A CD1 
3272 N N   . TYR B 227 ? 0.8660 0.5948 0.8083 0.2243  0.1165  0.0972  442 TYR A N   
3273 C CA  . TYR B 227 ? 0.8738 0.6554 0.8347 0.2605  0.1192  0.1287  442 TYR A CA  
3274 C C   . TYR B 227 ? 0.8559 0.7059 0.8419 0.2536  0.1032  0.1270  442 TYR A C   
3275 O O   . TYR B 227 ? 0.8238 0.6796 0.8118 0.2208  0.0867  0.1047  442 TYR A O   
3276 C CB  . TYR B 227 ? 0.8787 0.7032 0.8471 0.2679  0.1031  0.1519  442 TYR A CB  
3277 C CG  . TYR B 227 ? 0.9047 0.6668 0.8477 0.2740  0.1180  0.1572  442 TYR A CG  
3278 C CD1 . TYR B 227 ? 0.8845 0.6119 0.8136 0.2388  0.1080  0.1342  442 TYR A CD1 
3279 C CD2 . TYR B 227 ? 0.9722 0.7120 0.9036 0.3169  0.1440  0.1876  442 TYR A CD2 
3280 C CE1 . TYR B 227 ? 0.9687 0.6416 0.8734 0.2410  0.1231  0.1391  442 TYR A CE1 
3281 C CE2 . TYR B 227 ? 1.0162 0.7011 0.9208 0.3143  0.1581  0.1903  442 TYR A CE2 
3282 C CZ  . TYR B 227 ? 1.0031 0.6476 0.8936 0.2809  0.1497  0.1691  442 TYR A CZ  
3283 O OH  . TYR B 227 ? 1.0655 0.6591 0.9293 0.2764  0.1656  0.1722  442 TYR A OH  
3284 N N   . ARG B 228 ? 0.8668 0.7723 0.8709 0.2863  0.1096  0.1534  443 ARG A N   
3285 C CA  . ARG B 228 ? 0.8874 0.8725 0.9172 0.2797  0.0955  0.1564  443 ARG A CA  
3286 C C   . ARG B 228 ? 0.8469 0.9193 0.8956 0.2706  0.0693  0.1735  443 ARG A C   
3287 O O   . ARG B 228 ? 0.8427 0.9345 0.8915 0.2931  0.0703  0.1968  443 ARG A O   
3288 C CB  . ARG B 228 ? 0.9272 0.9304 0.9661 0.3213  0.1216  0.1738  443 ARG A CB  
3289 C CG  . ARG B 228 ? 0.9438 1.0281 1.0082 0.3130  0.1114  0.1749  443 ARG A CG  
3290 C CD  . ARG B 228 ? 1.0428 1.0981 1.1027 0.3391  0.1418  0.1720  443 ARG A CD  
3291 N NE  . ARG B 228 ? 1.1011 1.1336 1.1545 0.3949  0.1734  0.1982  443 ARG A NE  
3292 C CZ  . ARG B 228 ? 1.1199 1.2313 1.1949 0.4337  0.1742  0.2351  443 ARG A CZ  
3293 N NH1 . ARG B 228 ? 1.0929 1.3193 1.1986 0.4173  0.1447  0.2470  443 ARG A NH1 
3294 N NH2 . ARG B 228 ? 1.1036 1.1754 1.1550 0.4631  0.2005  0.2510  443 ARG A NH2 
3295 N N   . LEU B 229 ? 0.7843 0.9075 0.8446 0.2354  0.0477  0.1616  444 LEU A N   
3296 C CA  . LEU B 229 ? 0.7673 0.9746 0.8404 0.2164  0.0247  0.1720  444 LEU A CA  
3297 C C   . LEU B 229 ? 0.7419 1.0512 0.8421 0.2314  0.0260  0.1929  444 LEU A C   
3298 O O   . LEU B 229 ? 0.7652 1.0885 0.8736 0.2215  0.0299  0.1836  444 LEU A O   
3299 C CB  . LEU B 229 ? 0.7722 0.9647 0.8339 0.1646  0.0045  0.1454  444 LEU A CB  
3300 C CG  . LEU B 229 ? 0.7682 0.8963 0.8080 0.1499  -0.0025 0.1317  444 LEU A CG  
3301 C CD1 . LEU B 229 ? 0.7201 0.8230 0.7454 0.1074  -0.0161 0.1069  444 LEU A CD1 
3302 C CD2 . LEU B 229 ? 0.7421 0.9099 0.7825 0.1588  -0.0100 0.1504  444 LEU A CD2 
3303 N N   . VAL B 230 ? 0.8130 1.1997 0.9269 0.2566  0.0234  0.2227  445 VAL A N   
3304 C CA  . VAL B 230 ? 0.7852 1.2904 0.9281 0.2762  0.0242  0.2480  445 VAL A CA  
3305 C C   . VAL B 230 ? 0.8250 1.4365 0.9767 0.2512  -0.0003 0.2593  445 VAL A C   
3306 O O   . VAL B 230 ? 0.8446 1.4264 0.9778 0.2242  -0.0146 0.2481  445 VAL A O   
3307 C CB  . VAL B 230 ? 0.7903 1.2986 0.9417 0.3468  0.0525  0.2813  445 VAL A CB  
3308 C CG1 . VAL B 230 ? 0.8515 1.2394 0.9842 0.3646  0.0798  0.2646  445 VAL A CG1 
3309 C CG2 . VAL B 230 ? 0.7721 1.2825 0.9149 0.3789  0.0541  0.3088  445 VAL A CG2 
3310 N N   . ARG B 231 ? 0.8543 1.5971 1.0338 0.2595  -0.0042 0.2811  446 ARG A N   
3311 C CA  . ARG B 231 ? 0.8680 1.7312 1.0557 0.2337  -0.0268 0.2928  446 ARG A CA  
3312 C C   . ARG B 231 ? 0.7979 1.8019 1.0137 0.2684  -0.0218 0.3290  446 ARG A C   
3313 O O   . ARG B 231 ? 0.7585 1.7614 0.9846 0.3047  0.0003  0.3399  446 ARG A O   
3314 C CB  . ARG B 231 ? 0.8841 1.7635 1.0612 0.1554  -0.0459 0.2579  446 ARG A CB  
3315 C CG  . ARG B 231 ? 0.8830 1.8347 1.0799 0.1336  -0.0436 0.2525  446 ARG A CG  
3316 C CD  . ARG B 231 ? 0.9065 1.9618 1.1009 0.0670  -0.0637 0.2405  446 ARG A CD  
3317 N NE  . ARG B 231 ? 0.9989 1.9534 1.1570 0.0053  -0.0697 0.2008  446 ARG A NE  
3318 C CZ  . ARG B 231 ? 0.9950 1.9667 1.1291 -0.0496 -0.0840 0.1832  446 ARG A CZ  
3319 N NH1 . ARG B 231 ? 0.9608 2.0523 1.1034 -0.0558 -0.0974 0.1998  446 ARG A NH1 
3320 N NH2 . ARG B 231 ? 1.0507 1.9161 1.1488 -0.0974 -0.0833 0.1488  446 ARG A NH2 
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